data_9B2N
# 
_entry.id   9B2N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9B2N         pdb_00009b2n 10.2210/pdb9b2n/pdb 
WWPDB D_1000278839 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9B2N 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'GcL lactonase wild type'                            6n9i unspecified 
PDB 'wt GcL bound to substrate C4-HSL'                   6N9R unspecified 
PDB 'wt GcL bound to substrate C4-HSL'                   6N9Q unspecified 
PDB 'wt GcL bound to substrate C6-HSL'                   9AYT unspecified 
PDB 'Gcl mutant G156P'                                   9B2I unspecified 
PDB 'GcL I237M mutant'                                   9B2J unspecified 
PDB 'GcL D122N mutant - bimetallic center H3 spacegroup' 9B2L unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mhelias@umn.edu 
_pdbx_contact_author.name_first         Mikael 
_pdbx_contact_author.name_last          Elias 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0406-7539 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Corbella, M.'     1 ? 
'Bravo, J.A.'      2 ? 
'Demkiv, A.O.'     3 ? 
'Calixto, A.R.'    4 ? 
'Sompiyachoke, K.' 5 ? 
'Bergonzi, C.'     6 ? 
'Kamerlin, S.C.L.' 7 ? 
'Elias, M.'        8 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            4 
_citation.language                  ? 
_citation.page_first                3519 
_citation.page_last                 3536 
_citation.title                     
'Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.4c00404 
_citation.pdbx_database_id_PubMed   39328773 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Corbella, M.'     1 0000-0001-9209-868X 
primary 'Bravo, J.'        2 ?                   
primary 'Demkiv, A.O.'     3 ?                   
primary 'Calixto, A.R.'    4 0000-0002-1123-0413 
primary 'Sompiyachoke, K.' 5 0000-0003-0627-8305 
primary 'Bergonzi, C.'     6 ?                   
primary 'Brownless, A.R.'  7 ?                   
primary 'Elias, M.H.'      8 0000-0003-0406-7539 
primary 'Kamerlin, S.C.L.' 9 0000-0002-3190-1173 
# 
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 'quorum-quenching N-acyl-homoserine lactonase' 34377.926 3   3.1.1.81 D122N ? ? 
2 non-polymer syn 'COBALT (II) ION'                              58.933    3   ?        ?     ? ? 
3 non-polymer syn 'SULFATE ION'                                  96.063    12  ?        ?     ? ? 
4 non-polymer syn GLYCEROL                                       92.094    4   ?        ?     ? ? 
5 non-polymer syn 'ACETATE ION'                                  59.044    2   ?        ?     ? ? 
6 water       nat water                                          18.015    472 ?        ?     ? ? 
# 
_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       
;WSHPQFEKENLYFQSMANVIKARPKLYVMDNGRMRMDKNWMIAMHNPATIHNPNAQTEFVEFPIYTVLIDHPEGKILFDT
SCNPNSMGPQGRWAESTQQMFPWTATEECYLHNRLEQLKVRPEDIRYVVASHLHLNHAGCLEMFTNATIIVHEDEFNGAL
QCYARNQKEGAYIWADIDAWIKNNLQWRTVKRHEDNILLAEGVKVLNFGSGHAWGMLGLHVELPETGGIILASDAIYTAE
SYGPPIKPPGIIYDSLGYMNTVERIRRIAQETKSQVWFGHDAEQFKKFRKSTEGYYE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;WSHPQFEKENLYFQSMANVIKARPKLYVMDNGRMRMDKNWMIAMHNPATIHNPNAQTEFVEFPIYTVLIDHPEGKILFDT
SCNPNSMGPQGRWAESTQQMFPWTATEECYLHNRLEQLKVRPEDIRYVVASHLHLNHAGCLEMFTNATIIVHEDEFNGAL
QCYARNQKEGAYIWADIDAWIKNNLQWRTVKRHEDNILLAEGVKVLNFGSGHAWGMLGLHVELPETGGIILASDAIYTAE
SYGPPIKPPGIIYDSLGYMNTVERIRRIAQETKSQVWFGHDAEQFKKFRKSTEGYYE
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COBALT (II) ION' CO  
3 'SULFATE ION'     SO4 
4 GLYCEROL          GOL 
5 'ACETATE ION'     ACT 
6 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   TRP n 
1 2   SER n 
1 3   HIS n 
1 4   PRO n 
1 5   GLN n 
1 6   PHE n 
1 7   GLU n 
1 8   LYS n 
1 9   GLU n 
1 10  ASN n 
1 11  LEU n 
1 12  TYR n 
1 13  PHE n 
1 14  GLN n 
1 15  SER n 
1 16  MET n 
1 17  ALA n 
1 18  ASN n 
1 19  VAL n 
1 20  ILE n 
1 21  LYS n 
1 22  ALA n 
1 23  ARG n 
1 24  PRO n 
1 25  LYS n 
1 26  LEU n 
1 27  TYR n 
1 28  VAL n 
1 29  MET n 
1 30  ASP n 
1 31  ASN n 
1 32  GLY n 
1 33  ARG n 
1 34  MET n 
1 35  ARG n 
1 36  MET n 
1 37  ASP n 
1 38  LYS n 
1 39  ASN n 
1 40  TRP n 
1 41  MET n 
1 42  ILE n 
1 43  ALA n 
1 44  MET n 
1 45  HIS n 
1 46  ASN n 
1 47  PRO n 
1 48  ALA n 
1 49  THR n 
1 50  ILE n 
1 51  HIS n 
1 52  ASN n 
1 53  PRO n 
1 54  ASN n 
1 55  ALA n 
1 56  GLN n 
1 57  THR n 
1 58  GLU n 
1 59  PHE n 
1 60  VAL n 
1 61  GLU n 
1 62  PHE n 
1 63  PRO n 
1 64  ILE n 
1 65  TYR n 
1 66  THR n 
1 67  VAL n 
1 68  LEU n 
1 69  ILE n 
1 70  ASP n 
1 71  HIS n 
1 72  PRO n 
1 73  GLU n 
1 74  GLY n 
1 75  LYS n 
1 76  ILE n 
1 77  LEU n 
1 78  PHE n 
1 79  ASP n 
1 80  THR n 
1 81  SER n 
1 82  CYS n 
1 83  ASN n 
1 84  PRO n 
1 85  ASN n 
1 86  SER n 
1 87  MET n 
1 88  GLY n 
1 89  PRO n 
1 90  GLN n 
1 91  GLY n 
1 92  ARG n 
1 93  TRP n 
1 94  ALA n 
1 95  GLU n 
1 96  SER n 
1 97  THR n 
1 98  GLN n 
1 99  GLN n 
1 100 MET n 
1 101 PHE n 
1 102 PRO n 
1 103 TRP n 
1 104 THR n 
1 105 ALA n 
1 106 THR n 
1 107 GLU n 
1 108 GLU n 
1 109 CYS n 
1 110 TYR n 
1 111 LEU n 
1 112 HIS n 
1 113 ASN n 
1 114 ARG n 
1 115 LEU n 
1 116 GLU n 
1 117 GLN n 
1 118 LEU n 
1 119 LYS n 
1 120 VAL n 
1 121 ARG n 
1 122 PRO n 
1 123 GLU n 
1 124 ASP n 
1 125 ILE n 
1 126 ARG n 
1 127 TYR n 
1 128 VAL n 
1 129 VAL n 
1 130 ALA n 
1 131 SER n 
1 132 HIS n 
1 133 LEU n 
1 134 HIS n 
1 135 LEU n 
1 136 ASN n 
1 137 HIS n 
1 138 ALA n 
1 139 GLY n 
1 140 CYS n 
1 141 LEU n 
1 142 GLU n 
1 143 MET n 
1 144 PHE n 
1 145 THR n 
1 146 ASN n 
1 147 ALA n 
1 148 THR n 
1 149 ILE n 
1 150 ILE n 
1 151 VAL n 
1 152 HIS n 
1 153 GLU n 
1 154 ASP n 
1 155 GLU n 
1 156 PHE n 
1 157 ASN n 
1 158 GLY n 
1 159 ALA n 
1 160 LEU n 
1 161 GLN n 
1 162 CYS n 
1 163 TYR n 
1 164 ALA n 
1 165 ARG n 
1 166 ASN n 
1 167 GLN n 
1 168 LYS n 
1 169 GLU n 
1 170 GLY n 
1 171 ALA n 
1 172 TYR n 
1 173 ILE n 
1 174 TRP n 
1 175 ALA n 
1 176 ASP n 
1 177 ILE n 
1 178 ASP n 
1 179 ALA n 
1 180 TRP n 
1 181 ILE n 
1 182 LYS n 
1 183 ASN n 
1 184 ASN n 
1 185 LEU n 
1 186 GLN n 
1 187 TRP n 
1 188 ARG n 
1 189 THR n 
1 190 VAL n 
1 191 LYS n 
1 192 ARG n 
1 193 HIS n 
1 194 GLU n 
1 195 ASP n 
1 196 ASN n 
1 197 ILE n 
1 198 LEU n 
1 199 LEU n 
1 200 ALA n 
1 201 GLU n 
1 202 GLY n 
1 203 VAL n 
1 204 LYS n 
1 205 VAL n 
1 206 LEU n 
1 207 ASN n 
1 208 PHE n 
1 209 GLY n 
1 210 SER n 
1 211 GLY n 
1 212 HIS n 
1 213 ALA n 
1 214 TRP n 
1 215 GLY n 
1 216 MET n 
1 217 LEU n 
1 218 GLY n 
1 219 LEU n 
1 220 HIS n 
1 221 VAL n 
1 222 GLU n 
1 223 LEU n 
1 224 PRO n 
1 225 GLU n 
1 226 THR n 
1 227 GLY n 
1 228 GLY n 
1 229 ILE n 
1 230 ILE n 
1 231 LEU n 
1 232 ALA n 
1 233 SER n 
1 234 ASP n 
1 235 ALA n 
1 236 ILE n 
1 237 TYR n 
1 238 THR n 
1 239 ALA n 
1 240 GLU n 
1 241 SER n 
1 242 TYR n 
1 243 GLY n 
1 244 PRO n 
1 245 PRO n 
1 246 ILE n 
1 247 LYS n 
1 248 PRO n 
1 249 PRO n 
1 250 GLY n 
1 251 ILE n 
1 252 ILE n 
1 253 TYR n 
1 254 ASP n 
1 255 SER n 
1 256 LEU n 
1 257 GLY n 
1 258 TYR n 
1 259 MET n 
1 260 ASN n 
1 261 THR n 
1 262 VAL n 
1 263 GLU n 
1 264 ARG n 
1 265 ILE n 
1 266 ARG n 
1 267 ARG n 
1 268 ILE n 
1 269 ALA n 
1 270 GLN n 
1 271 GLU n 
1 272 THR n 
1 273 LYS n 
1 274 SER n 
1 275 GLN n 
1 276 VAL n 
1 277 TRP n 
1 278 PHE n 
1 279 GLY n 
1 280 HIS n 
1 281 ASP n 
1 282 ALA n 
1 283 GLU n 
1 284 GLN n 
1 285 PHE n 
1 286 LYS n 
1 287 LYS n 
1 288 PHE n 
1 289 ARG n 
1 290 LYS n 
1 291 SER n 
1 292 THR n 
1 293 GLU n 
1 294 GLY n 
1 295 TYR n 
1 296 TYR n 
1 297 GLU 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                   297 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GCA01S_030_00190 
_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      'Parageobacillus caldoxylosilyticus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     81408 
_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              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'     ?                               'C2 H3 O2 -1'    59.044  
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 
CO  non-polymer         . 'COBALT (II) ION' ?                               'Co 2'           58.933  
CYS 'L-peptide linking' y CYSTEINE          ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL          'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE         ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE     ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ?                               'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'     ?                               'O4 S -2'        96.063  
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   TRP 1   -13 ?   ?   ?   A . n 
A 1 2   SER 2   -12 ?   ?   ?   A . n 
A 1 3   HIS 3   -11 ?   ?   ?   A . n 
A 1 4   PRO 4   -10 ?   ?   ?   A . n 
A 1 5   GLN 5   -9  ?   ?   ?   A . n 
A 1 6   PHE 6   -8  ?   ?   ?   A . n 
A 1 7   GLU 7   -7  ?   ?   ?   A . n 
A 1 8   LYS 8   -6  ?   ?   ?   A . n 
A 1 9   GLU 9   -5  ?   ?   ?   A . n 
A 1 10  ASN 10  -4  ?   ?   ?   A . n 
A 1 11  LEU 11  -3  ?   ?   ?   A . n 
A 1 12  TYR 12  -2  ?   ?   ?   A . n 
A 1 13  PHE 13  -1  ?   ?   ?   A . n 
A 1 14  GLN 14  0   ?   ?   ?   A . n 
A 1 15  SER 15  1   ?   ?   ?   A . n 
A 1 16  MET 16  2   ?   ?   ?   A . n 
A 1 17  ALA 17  3   ?   ?   ?   A . n 
A 1 18  ASN 18  4   ?   ?   ?   A . n 
A 1 19  VAL 19  5   ?   ?   ?   A . n 
A 1 20  ILE 20  6   ?   ?   ?   A . n 
A 1 21  LYS 21  7   ?   ?   ?   A . n 
A 1 22  ALA 22  8   ?   ?   ?   A . n 
A 1 23  ARG 23  9   9   ARG ARG A . n 
A 1 24  PRO 24  10  10  PRO PRO A . n 
A 1 25  LYS 25  11  11  LYS LYS A . n 
A 1 26  LEU 26  12  12  LEU LEU A . n 
A 1 27  TYR 27  13  13  TYR TYR A . n 
A 1 28  VAL 28  14  14  VAL VAL A . n 
A 1 29  MET 29  15  15  MET MET A . n 
A 1 30  ASP 30  16  16  ASP ASP A . n 
A 1 31  ASN 31  17  17  ASN ASN A . n 
A 1 32  GLY 32  18  18  GLY GLY A . n 
A 1 33  ARG 33  19  19  ARG ARG A . n 
A 1 34  MET 34  20  20  MET MET A . n 
A 1 35  ARG 35  21  21  ARG ARG A . n 
A 1 36  MET 36  22  22  MET MET A . n 
A 1 37  ASP 37  23  23  ASP ASP A . n 
A 1 38  LYS 38  24  24  LYS LYS A . n 
A 1 39  ASN 39  25  25  ASN ASN A . n 
A 1 40  TRP 40  26  26  TRP TRP A . n 
A 1 41  MET 41  27  27  MET MET A . n 
A 1 42  ILE 42  28  28  ILE ILE A . n 
A 1 43  ALA 43  29  29  ALA ALA A . n 
A 1 44  MET 44  30  30  MET MET A . n 
A 1 45  HIS 45  31  31  HIS HIS A . n 
A 1 46  ASN 46  32  32  ASN ASN A . n 
A 1 47  PRO 47  33  33  PRO PRO A . n 
A 1 48  ALA 48  34  34  ALA ALA A . n 
A 1 49  THR 49  35  35  THR THR A . n 
A 1 50  ILE 50  36  36  ILE ILE A . n 
A 1 51  HIS 51  37  37  HIS HIS A . n 
A 1 52  ASN 52  38  38  ASN ASN A . n 
A 1 53  PRO 53  39  39  PRO PRO A . n 
A 1 54  ASN 54  40  40  ASN ASN A . n 
A 1 55  ALA 55  41  41  ALA ALA A . n 
A 1 56  GLN 56  42  42  GLN GLN A . n 
A 1 57  THR 57  43  43  THR THR A . n 
A 1 58  GLU 58  44  44  GLU GLU A . n 
A 1 59  PHE 59  45  45  PHE PHE A . n 
A 1 60  VAL 60  46  46  VAL VAL A . n 
A 1 61  GLU 61  47  47  GLU GLU A . n 
A 1 62  PHE 62  48  48  PHE PHE A . n 
A 1 63  PRO 63  49  49  PRO PRO A . n 
A 1 64  ILE 64  50  50  ILE ILE A . n 
A 1 65  TYR 65  51  51  TYR TYR A . n 
A 1 66  THR 66  52  52  THR THR A . n 
A 1 67  VAL 67  53  53  VAL VAL A . n 
A 1 68  LEU 68  54  54  LEU LEU A . n 
A 1 69  ILE 69  55  55  ILE ILE A . n 
A 1 70  ASP 70  56  56  ASP ASP A . n 
A 1 71  HIS 71  57  57  HIS HIS A . n 
A 1 72  PRO 72  58  58  PRO PRO A . n 
A 1 73  GLU 73  59  59  GLU GLU A . n 
A 1 74  GLY 74  60  60  GLY GLY A . n 
A 1 75  LYS 75  61  61  LYS LYS A . n 
A 1 76  ILE 76  62  62  ILE ILE A . n 
A 1 77  LEU 77  63  63  LEU LEU A . n 
A 1 78  PHE 78  64  64  PHE PHE A . n 
A 1 79  ASP 79  65  65  ASP ASP A . n 
A 1 80  THR 80  66  66  THR THR A . n 
A 1 81  SER 81  67  67  SER SER A . n 
A 1 82  CYS 82  68  68  CYS CYS A . n 
A 1 83  ASN 83  69  69  ASN ASN A . n 
A 1 84  PRO 84  70  70  PRO PRO A . n 
A 1 85  ASN 85  71  71  ASN ASN A . n 
A 1 86  SER 86  72  72  SER SER A . n 
A 1 87  MET 87  73  73  MET MET A . n 
A 1 88  GLY 88  74  74  GLY GLY A . n 
A 1 89  PRO 89  75  75  PRO PRO A . n 
A 1 90  GLN 90  76  76  GLN GLN A . n 
A 1 91  GLY 91  77  77  GLY GLY A . n 
A 1 92  ARG 92  78  78  ARG ARG A . n 
A 1 93  TRP 93  79  79  TRP TRP A . n 
A 1 94  ALA 94  80  80  ALA ALA A . n 
A 1 95  GLU 95  81  81  GLU GLU A . n 
A 1 96  SER 96  82  82  SER SER A . n 
A 1 97  THR 97  83  83  THR THR A . n 
A 1 98  GLN 98  84  84  GLN GLN A . n 
A 1 99  GLN 99  85  85  GLN GLN A . n 
A 1 100 MET 100 86  86  MET MET A . n 
A 1 101 PHE 101 87  87  PHE PHE A . n 
A 1 102 PRO 102 88  88  PRO PRO A . n 
A 1 103 TRP 103 89  89  TRP TRP A . n 
A 1 104 THR 104 90  90  THR THR A . n 
A 1 105 ALA 105 91  91  ALA ALA A . n 
A 1 106 THR 106 92  92  THR THR A . n 
A 1 107 GLU 107 93  93  GLU GLU A . n 
A 1 108 GLU 108 94  94  GLU GLU A . n 
A 1 109 CYS 109 95  95  CYS CYS A . n 
A 1 110 TYR 110 96  96  TYR TYR A . n 
A 1 111 LEU 111 97  97  LEU LEU A . n 
A 1 112 HIS 112 98  98  HIS HIS A . n 
A 1 113 ASN 113 99  99  ASN ASN A . n 
A 1 114 ARG 114 100 100 ARG ARG A . n 
A 1 115 LEU 115 101 101 LEU LEU A . n 
A 1 116 GLU 116 102 102 GLU GLU A . n 
A 1 117 GLN 117 103 103 GLN GLN A . n 
A 1 118 LEU 118 104 104 LEU LEU A . n 
A 1 119 LYS 119 105 105 LYS LYS A . n 
A 1 120 VAL 120 106 106 VAL VAL A . n 
A 1 121 ARG 121 107 107 ARG ARG A . n 
A 1 122 PRO 122 108 108 PRO PRO A . n 
A 1 123 GLU 123 109 109 GLU GLU A . n 
A 1 124 ASP 124 110 110 ASP ASP A . n 
A 1 125 ILE 125 111 111 ILE ILE A . n 
A 1 126 ARG 126 112 112 ARG ARG A . n 
A 1 127 TYR 127 113 113 TYR TYR A . n 
A 1 128 VAL 128 114 114 VAL VAL A . n 
A 1 129 VAL 129 115 115 VAL VAL A . n 
A 1 130 ALA 130 116 116 ALA ALA A . n 
A 1 131 SER 131 117 117 SER SER A . n 
A 1 132 HIS 132 118 118 HIS HIS A . n 
A 1 133 LEU 133 119 119 LEU LEU A . n 
A 1 134 HIS 134 120 120 HIS HIS A . n 
A 1 135 LEU 135 121 121 LEU LEU A . n 
A 1 136 ASN 136 122 122 ASN ASN A . n 
A 1 137 HIS 137 123 123 HIS HIS A . n 
A 1 138 ALA 138 124 124 ALA ALA A . n 
A 1 139 GLY 139 125 125 GLY GLY A . n 
A 1 140 CYS 140 126 126 CYS CYS A . n 
A 1 141 LEU 141 127 127 LEU LEU A . n 
A 1 142 GLU 142 128 128 GLU GLU A . n 
A 1 143 MET 143 129 129 MET MET A . n 
A 1 144 PHE 144 130 130 PHE PHE A . n 
A 1 145 THR 145 131 131 THR THR A . n 
A 1 146 ASN 146 132 132 ASN ASN A . n 
A 1 147 ALA 147 133 133 ALA ALA A . n 
A 1 148 THR 148 134 134 THR THR A . n 
A 1 149 ILE 149 135 135 ILE ILE A . n 
A 1 150 ILE 150 136 136 ILE ILE A . n 
A 1 151 VAL 151 137 137 VAL VAL A . n 
A 1 152 HIS 152 138 138 HIS HIS A . n 
A 1 153 GLU 153 139 139 GLU GLU A . n 
A 1 154 ASP 154 140 140 ASP ASP A . n 
A 1 155 GLU 155 141 141 GLU GLU A . n 
A 1 156 PHE 156 142 142 PHE PHE A . n 
A 1 157 ASN 157 143 143 ASN ASN A . n 
A 1 158 GLY 158 144 144 GLY GLY A . n 
A 1 159 ALA 159 145 145 ALA ALA A . n 
A 1 160 LEU 160 146 146 LEU LEU A . n 
A 1 161 GLN 161 147 147 GLN GLN A . n 
A 1 162 CYS 162 148 148 CYS CYS A . n 
A 1 163 TYR 163 149 149 TYR TYR A . n 
A 1 164 ALA 164 150 150 ALA ALA A . n 
A 1 165 ARG 165 151 151 ARG ARG A . n 
A 1 166 ASN 166 152 152 ASN ASN A . n 
A 1 167 GLN 167 153 153 GLN GLN A . n 
A 1 168 LYS 168 154 154 LYS LYS A . n 
A 1 169 GLU 169 155 155 GLU GLU A . n 
A 1 170 GLY 170 156 156 GLY GLY A . n 
A 1 171 ALA 171 157 157 ALA ALA A . n 
A 1 172 TYR 172 158 158 TYR TYR A . n 
A 1 173 ILE 173 159 159 ILE ILE A . n 
A 1 174 TRP 174 160 160 TRP TRP A . n 
A 1 175 ALA 175 161 161 ALA ALA A . n 
A 1 176 ASP 176 162 162 ASP ASP A . n 
A 1 177 ILE 177 163 163 ILE ILE A . n 
A 1 178 ASP 178 164 164 ASP ASP A . n 
A 1 179 ALA 179 165 165 ALA ALA A . n 
A 1 180 TRP 180 166 166 TRP TRP A . n 
A 1 181 ILE 181 167 167 ILE ILE A . n 
A 1 182 LYS 182 168 168 LYS LYS A . n 
A 1 183 ASN 183 169 169 ASN ASN A . n 
A 1 184 ASN 184 170 170 ASN ASN A . n 
A 1 185 LEU 185 171 171 LEU LEU A . n 
A 1 186 GLN 186 172 172 GLN GLN A . n 
A 1 187 TRP 187 173 173 TRP TRP A . n 
A 1 188 ARG 188 174 174 ARG ARG A . n 
A 1 189 THR 189 175 175 THR THR A . n 
A 1 190 VAL 190 176 176 VAL VAL A . n 
A 1 191 LYS 191 177 177 LYS LYS A . n 
A 1 192 ARG 192 178 178 ARG ARG A . n 
A 1 193 HIS 193 179 179 HIS HIS A . n 
A 1 194 GLU 194 180 180 GLU GLU A . n 
A 1 195 ASP 195 181 181 ASP ASP A . n 
A 1 196 ASN 196 182 182 ASN ASN A . n 
A 1 197 ILE 197 183 183 ILE ILE A . n 
A 1 198 LEU 198 184 184 LEU LEU A . n 
A 1 199 LEU 199 185 185 LEU LEU A . n 
A 1 200 ALA 200 186 186 ALA ALA A . n 
A 1 201 GLU 201 187 187 GLU GLU A . n 
A 1 202 GLY 202 188 188 GLY GLY A . n 
A 1 203 VAL 203 189 189 VAL VAL A . n 
A 1 204 LYS 204 190 190 LYS LYS A . n 
A 1 205 VAL 205 191 191 VAL VAL A . n 
A 1 206 LEU 206 192 192 LEU LEU A . n 
A 1 207 ASN 207 193 193 ASN ASN A . n 
A 1 208 PHE 208 194 194 PHE PHE A . n 
A 1 209 GLY 209 195 195 GLY GLY A . n 
A 1 210 SER 210 196 196 SER SER A . n 
A 1 211 GLY 211 197 197 GLY GLY A . n 
A 1 212 HIS 212 198 198 HIS HIS A . n 
A 1 213 ALA 213 199 199 ALA ALA A . n 
A 1 214 TRP 214 200 200 TRP TRP A . n 
A 1 215 GLY 215 201 201 GLY GLY A . n 
A 1 216 MET 216 202 202 MET MET A . n 
A 1 217 LEU 217 203 203 LEU LEU A . n 
A 1 218 GLY 218 204 204 GLY GLY A . n 
A 1 219 LEU 219 205 205 LEU LEU A . n 
A 1 220 HIS 220 206 206 HIS HIS A . n 
A 1 221 VAL 221 207 207 VAL VAL A . n 
A 1 222 GLU 222 208 208 GLU GLU A . n 
A 1 223 LEU 223 209 209 LEU LEU A . n 
A 1 224 PRO 224 210 210 PRO PRO A . n 
A 1 225 GLU 225 211 211 GLU GLU A . n 
A 1 226 THR 226 212 212 THR THR A . n 
A 1 227 GLY 227 213 213 GLY GLY A . n 
A 1 228 GLY 228 214 214 GLY GLY A . n 
A 1 229 ILE 229 215 215 ILE ILE A . n 
A 1 230 ILE 230 216 216 ILE ILE A . n 
A 1 231 LEU 231 217 217 LEU LEU A . n 
A 1 232 ALA 232 218 218 ALA ALA A . n 
A 1 233 SER 233 219 219 SER SER A . n 
A 1 234 ASP 234 220 220 ASP ASP A . n 
A 1 235 ALA 235 221 221 ALA ALA A . n 
A 1 236 ILE 236 222 222 ILE ILE A . n 
A 1 237 TYR 237 223 223 TYR TYR A . n 
A 1 238 THR 238 224 224 THR THR A . n 
A 1 239 ALA 239 225 225 ALA ALA A . n 
A 1 240 GLU 240 226 226 GLU GLU A . n 
A 1 241 SER 241 227 227 SER SER A . n 
A 1 242 TYR 242 228 228 TYR TYR A . n 
A 1 243 GLY 243 229 229 GLY GLY A . n 
A 1 244 PRO 244 230 230 PRO PRO A . n 
A 1 245 PRO 245 231 231 PRO PRO A . n 
A 1 246 ILE 246 232 232 ILE ILE A . n 
A 1 247 LYS 247 233 233 LYS LYS A . n 
A 1 248 PRO 248 234 234 PRO PRO A . n 
A 1 249 PRO 249 235 235 PRO PRO A . n 
A 1 250 GLY 250 236 236 GLY GLY A . n 
A 1 251 ILE 251 237 237 ILE ILE A . n 
A 1 252 ILE 252 238 238 ILE ILE A . n 
A 1 253 TYR 253 239 239 TYR TYR A . n 
A 1 254 ASP 254 240 240 ASP ASP A . n 
A 1 255 SER 255 241 241 SER SER A . n 
A 1 256 LEU 256 242 242 LEU LEU A . n 
A 1 257 GLY 257 243 243 GLY GLY A . n 
A 1 258 TYR 258 244 244 TYR TYR A . n 
A 1 259 MET 259 245 245 MET MET A . n 
A 1 260 ASN 260 246 246 ASN ASN A . n 
A 1 261 THR 261 247 247 THR THR A . n 
A 1 262 VAL 262 248 248 VAL VAL A . n 
A 1 263 GLU 263 249 249 GLU GLU A . n 
A 1 264 ARG 264 250 250 ARG ARG A . n 
A 1 265 ILE 265 251 251 ILE ILE A . n 
A 1 266 ARG 266 252 252 ARG ARG A . n 
A 1 267 ARG 267 253 253 ARG ARG A . n 
A 1 268 ILE 268 254 254 ILE ILE A . n 
A 1 269 ALA 269 255 255 ALA ALA A . n 
A 1 270 GLN 270 256 256 GLN GLN A . n 
A 1 271 GLU 271 257 257 GLU GLU A . n 
A 1 272 THR 272 258 258 THR THR A . n 
A 1 273 LYS 273 259 259 LYS LYS A . n 
A 1 274 SER 274 260 260 SER SER A . n 
A 1 275 GLN 275 261 261 GLN GLN A . n 
A 1 276 VAL 276 262 262 VAL VAL A . n 
A 1 277 TRP 277 263 263 TRP TRP A . n 
A 1 278 PHE 278 264 264 PHE PHE A . n 
A 1 279 GLY 279 265 265 GLY GLY A . n 
A 1 280 HIS 280 266 266 HIS HIS A . n 
A 1 281 ASP 281 267 267 ASP ASP A . n 
A 1 282 ALA 282 268 268 ALA ALA A . n 
A 1 283 GLU 283 269 269 GLU GLU A . n 
A 1 284 GLN 284 270 270 GLN GLN A . n 
A 1 285 PHE 285 271 271 PHE PHE A . n 
A 1 286 LYS 286 272 272 LYS LYS A . n 
A 1 287 LYS 287 273 273 LYS LYS A . n 
A 1 288 PHE 288 274 274 PHE PHE A . n 
A 1 289 ARG 289 275 275 ARG ARG A . n 
A 1 290 LYS 290 276 276 LYS LYS A . n 
A 1 291 SER 291 277 277 SER SER A . n 
A 1 292 THR 292 278 278 THR THR A . n 
A 1 293 GLU 293 279 279 GLU GLU A . n 
A 1 294 GLY 294 280 280 GLY GLY A . n 
A 1 295 TYR 295 281 281 TYR TYR A . n 
A 1 296 TYR 296 282 282 TYR TYR A . n 
A 1 297 GLU 297 283 283 GLU GLU A . n 
B 1 1   TRP 1   -13 ?   ?   ?   B . n 
B 1 2   SER 2   -12 ?   ?   ?   B . n 
B 1 3   HIS 3   -11 ?   ?   ?   B . n 
B 1 4   PRO 4   -10 ?   ?   ?   B . n 
B 1 5   GLN 5   -9  ?   ?   ?   B . n 
B 1 6   PHE 6   -8  ?   ?   ?   B . n 
B 1 7   GLU 7   -7  ?   ?   ?   B . n 
B 1 8   LYS 8   -6  ?   ?   ?   B . n 
B 1 9   GLU 9   -5  ?   ?   ?   B . n 
B 1 10  ASN 10  -4  ?   ?   ?   B . n 
B 1 11  LEU 11  -3  ?   ?   ?   B . n 
B 1 12  TYR 12  -2  ?   ?   ?   B . n 
B 1 13  PHE 13  -1  ?   ?   ?   B . n 
B 1 14  GLN 14  0   ?   ?   ?   B . n 
B 1 15  SER 15  1   ?   ?   ?   B . n 
B 1 16  MET 16  2   ?   ?   ?   B . n 
B 1 17  ALA 17  3   ?   ?   ?   B . n 
B 1 18  ASN 18  4   ?   ?   ?   B . n 
B 1 19  VAL 19  5   ?   ?   ?   B . n 
B 1 20  ILE 20  6   ?   ?   ?   B . n 
B 1 21  LYS 21  7   ?   ?   ?   B . n 
B 1 22  ALA 22  8   8   ALA ALA B . n 
B 1 23  ARG 23  9   9   ARG ARG B . n 
B 1 24  PRO 24  10  10  PRO PRO B . n 
B 1 25  LYS 25  11  11  LYS LYS B . n 
B 1 26  LEU 26  12  12  LEU LEU B . n 
B 1 27  TYR 27  13  13  TYR TYR B . n 
B 1 28  VAL 28  14  14  VAL VAL B . n 
B 1 29  MET 29  15  15  MET MET B . n 
B 1 30  ASP 30  16  16  ASP ASP B . n 
B 1 31  ASN 31  17  17  ASN ASN B . n 
B 1 32  GLY 32  18  18  GLY GLY B . n 
B 1 33  ARG 33  19  19  ARG ARG B . n 
B 1 34  MET 34  20  20  MET MET B . n 
B 1 35  ARG 35  21  21  ARG ARG B . n 
B 1 36  MET 36  22  22  MET MET B . n 
B 1 37  ASP 37  23  23  ASP ASP B . n 
B 1 38  LYS 38  24  24  LYS LYS B . n 
B 1 39  ASN 39  25  25  ASN ASN B . n 
B 1 40  TRP 40  26  26  TRP TRP B . n 
B 1 41  MET 41  27  27  MET MET B . n 
B 1 42  ILE 42  28  28  ILE ILE B . n 
B 1 43  ALA 43  29  29  ALA ALA B . n 
B 1 44  MET 44  30  30  MET MET B . n 
B 1 45  HIS 45  31  31  HIS HIS B . n 
B 1 46  ASN 46  32  32  ASN ASN B . n 
B 1 47  PRO 47  33  33  PRO PRO B . n 
B 1 48  ALA 48  34  34  ALA ALA B . n 
B 1 49  THR 49  35  35  THR THR B . n 
B 1 50  ILE 50  36  36  ILE ILE B . n 
B 1 51  HIS 51  37  37  HIS HIS B . n 
B 1 52  ASN 52  38  38  ASN ASN B . n 
B 1 53  PRO 53  39  39  PRO PRO B . n 
B 1 54  ASN 54  40  40  ASN ASN B . n 
B 1 55  ALA 55  41  41  ALA ALA B . n 
B 1 56  GLN 56  42  42  GLN GLN B . n 
B 1 57  THR 57  43  43  THR THR B . n 
B 1 58  GLU 58  44  44  GLU GLU B . n 
B 1 59  PHE 59  45  45  PHE PHE B . n 
B 1 60  VAL 60  46  46  VAL VAL B . n 
B 1 61  GLU 61  47  47  GLU GLU B . n 
B 1 62  PHE 62  48  48  PHE PHE B . n 
B 1 63  PRO 63  49  49  PRO PRO B . n 
B 1 64  ILE 64  50  50  ILE ILE B . n 
B 1 65  TYR 65  51  51  TYR TYR B . n 
B 1 66  THR 66  52  52  THR THR B . n 
B 1 67  VAL 67  53  53  VAL VAL B . n 
B 1 68  LEU 68  54  54  LEU LEU B . n 
B 1 69  ILE 69  55  55  ILE ILE B . n 
B 1 70  ASP 70  56  56  ASP ASP B . n 
B 1 71  HIS 71  57  57  HIS HIS B . n 
B 1 72  PRO 72  58  58  PRO PRO B . n 
B 1 73  GLU 73  59  59  GLU GLU B . n 
B 1 74  GLY 74  60  60  GLY GLY B . n 
B 1 75  LYS 75  61  61  LYS LYS B . n 
B 1 76  ILE 76  62  62  ILE ILE B . n 
B 1 77  LEU 77  63  63  LEU LEU B . n 
B 1 78  PHE 78  64  64  PHE PHE B . n 
B 1 79  ASP 79  65  65  ASP ASP B . n 
B 1 80  THR 80  66  66  THR THR B . n 
B 1 81  SER 81  67  67  SER SER B . n 
B 1 82  CYS 82  68  68  CYS CYS B . n 
B 1 83  ASN 83  69  69  ASN ASN B . n 
B 1 84  PRO 84  70  70  PRO PRO B . n 
B 1 85  ASN 85  71  71  ASN ASN B . n 
B 1 86  SER 86  72  72  SER SER B . n 
B 1 87  MET 87  73  73  MET MET B . n 
B 1 88  GLY 88  74  74  GLY GLY B . n 
B 1 89  PRO 89  75  75  PRO PRO B . n 
B 1 90  GLN 90  76  76  GLN GLN B . n 
B 1 91  GLY 91  77  77  GLY GLY B . n 
B 1 92  ARG 92  78  78  ARG ARG B . n 
B 1 93  TRP 93  79  79  TRP TRP B . n 
B 1 94  ALA 94  80  80  ALA ALA B . n 
B 1 95  GLU 95  81  81  GLU GLU B . n 
B 1 96  SER 96  82  82  SER SER B . n 
B 1 97  THR 97  83  83  THR THR B . n 
B 1 98  GLN 98  84  84  GLN GLN B . n 
B 1 99  GLN 99  85  85  GLN GLN B . n 
B 1 100 MET 100 86  86  MET MET B . n 
B 1 101 PHE 101 87  87  PHE PHE B . n 
B 1 102 PRO 102 88  88  PRO PRO B . n 
B 1 103 TRP 103 89  89  TRP TRP B . n 
B 1 104 THR 104 90  90  THR THR B . n 
B 1 105 ALA 105 91  91  ALA ALA B . n 
B 1 106 THR 106 92  92  THR THR B . n 
B 1 107 GLU 107 93  93  GLU GLU B . n 
B 1 108 GLU 108 94  94  GLU GLU B . n 
B 1 109 CYS 109 95  95  CYS CYS B . n 
B 1 110 TYR 110 96  96  TYR TYR B . n 
B 1 111 LEU 111 97  97  LEU LEU B . n 
B 1 112 HIS 112 98  98  HIS HIS B . n 
B 1 113 ASN 113 99  99  ASN ASN B . n 
B 1 114 ARG 114 100 100 ARG ARG B . n 
B 1 115 LEU 115 101 101 LEU LEU B . n 
B 1 116 GLU 116 102 102 GLU GLU B . n 
B 1 117 GLN 117 103 103 GLN GLN B . n 
B 1 118 LEU 118 104 104 LEU LEU B . n 
B 1 119 LYS 119 105 105 LYS LYS B . n 
B 1 120 VAL 120 106 106 VAL VAL B . n 
B 1 121 ARG 121 107 107 ARG ARG B . n 
B 1 122 PRO 122 108 108 PRO PRO B . n 
B 1 123 GLU 123 109 109 GLU GLU B . n 
B 1 124 ASP 124 110 110 ASP ASP B . n 
B 1 125 ILE 125 111 111 ILE ILE B . n 
B 1 126 ARG 126 112 112 ARG ARG B . n 
B 1 127 TYR 127 113 113 TYR TYR B . n 
B 1 128 VAL 128 114 114 VAL VAL B . n 
B 1 129 VAL 129 115 115 VAL VAL B . n 
B 1 130 ALA 130 116 116 ALA ALA B . n 
B 1 131 SER 131 117 117 SER SER B . n 
B 1 132 HIS 132 118 118 HIS HIS B . n 
B 1 133 LEU 133 119 119 LEU LEU B . n 
B 1 134 HIS 134 120 120 HIS HIS B . n 
B 1 135 LEU 135 121 121 LEU LEU B . n 
B 1 136 ASN 136 122 122 ASN ASN B . n 
B 1 137 HIS 137 123 123 HIS HIS B . n 
B 1 138 ALA 138 124 124 ALA ALA B . n 
B 1 139 GLY 139 125 125 GLY GLY B . n 
B 1 140 CYS 140 126 126 CYS CYS B . n 
B 1 141 LEU 141 127 127 LEU LEU B . n 
B 1 142 GLU 142 128 128 GLU GLU B . n 
B 1 143 MET 143 129 129 MET MET B . n 
B 1 144 PHE 144 130 130 PHE PHE B . n 
B 1 145 THR 145 131 131 THR THR B . n 
B 1 146 ASN 146 132 132 ASN ASN B . n 
B 1 147 ALA 147 133 133 ALA ALA B . n 
B 1 148 THR 148 134 134 THR THR B . n 
B 1 149 ILE 149 135 135 ILE ILE B . n 
B 1 150 ILE 150 136 136 ILE ILE B . n 
B 1 151 VAL 151 137 137 VAL VAL B . n 
B 1 152 HIS 152 138 138 HIS HIS B . n 
B 1 153 GLU 153 139 139 GLU GLU B . n 
B 1 154 ASP 154 140 140 ASP ASP B . n 
B 1 155 GLU 155 141 141 GLU GLU B . n 
B 1 156 PHE 156 142 142 PHE PHE B . n 
B 1 157 ASN 157 143 143 ASN ASN B . n 
B 1 158 GLY 158 144 144 GLY GLY B . n 
B 1 159 ALA 159 145 145 ALA ALA B . n 
B 1 160 LEU 160 146 146 LEU LEU B . n 
B 1 161 GLN 161 147 147 GLN GLN B . n 
B 1 162 CYS 162 148 148 CYS CYS B . n 
B 1 163 TYR 163 149 149 TYR TYR B . n 
B 1 164 ALA 164 150 150 ALA ALA B . n 
B 1 165 ARG 165 151 151 ARG ARG B . n 
B 1 166 ASN 166 152 152 ASN ASN B . n 
B 1 167 GLN 167 153 153 GLN GLN B . n 
B 1 168 LYS 168 154 154 LYS LYS B . n 
B 1 169 GLU 169 155 155 GLU GLU B . n 
B 1 170 GLY 170 156 156 GLY GLY B . n 
B 1 171 ALA 171 157 157 ALA ALA B . n 
B 1 172 TYR 172 158 158 TYR TYR B . n 
B 1 173 ILE 173 159 159 ILE ILE B . n 
B 1 174 TRP 174 160 160 TRP TRP B . n 
B 1 175 ALA 175 161 161 ALA ALA B . n 
B 1 176 ASP 176 162 162 ASP ASP B . n 
B 1 177 ILE 177 163 163 ILE ILE B . n 
B 1 178 ASP 178 164 164 ASP ASP B . n 
B 1 179 ALA 179 165 165 ALA ALA B . n 
B 1 180 TRP 180 166 166 TRP TRP B . n 
B 1 181 ILE 181 167 167 ILE ILE B . n 
B 1 182 LYS 182 168 168 LYS LYS B . n 
B 1 183 ASN 183 169 169 ASN ASN B . n 
B 1 184 ASN 184 170 170 ASN ASN B . n 
B 1 185 LEU 185 171 171 LEU LEU B . n 
B 1 186 GLN 186 172 172 GLN GLN B . n 
B 1 187 TRP 187 173 173 TRP TRP B . n 
B 1 188 ARG 188 174 174 ARG ARG B . n 
B 1 189 THR 189 175 175 THR THR B . n 
B 1 190 VAL 190 176 176 VAL VAL B . n 
B 1 191 LYS 191 177 177 LYS LYS B . n 
B 1 192 ARG 192 178 178 ARG ARG B . n 
B 1 193 HIS 193 179 179 HIS HIS B . n 
B 1 194 GLU 194 180 180 GLU GLU B . n 
B 1 195 ASP 195 181 181 ASP ASP B . n 
B 1 196 ASN 196 182 182 ASN ASN B . n 
B 1 197 ILE 197 183 183 ILE ILE B . n 
B 1 198 LEU 198 184 184 LEU LEU B . n 
B 1 199 LEU 199 185 185 LEU LEU B . n 
B 1 200 ALA 200 186 186 ALA ALA B . n 
B 1 201 GLU 201 187 187 GLU GLU B . n 
B 1 202 GLY 202 188 188 GLY GLY B . n 
B 1 203 VAL 203 189 189 VAL VAL B . n 
B 1 204 LYS 204 190 190 LYS LYS B . n 
B 1 205 VAL 205 191 191 VAL VAL B . n 
B 1 206 LEU 206 192 192 LEU LEU B . n 
B 1 207 ASN 207 193 193 ASN ASN B . n 
B 1 208 PHE 208 194 194 PHE PHE B . n 
B 1 209 GLY 209 195 195 GLY GLY B . n 
B 1 210 SER 210 196 196 SER SER B . n 
B 1 211 GLY 211 197 197 GLY GLY B . n 
B 1 212 HIS 212 198 198 HIS HIS B . n 
B 1 213 ALA 213 199 199 ALA ALA B . n 
B 1 214 TRP 214 200 200 TRP TRP B . n 
B 1 215 GLY 215 201 201 GLY GLY B . n 
B 1 216 MET 216 202 202 MET MET B . n 
B 1 217 LEU 217 203 203 LEU LEU B . n 
B 1 218 GLY 218 204 204 GLY GLY B . n 
B 1 219 LEU 219 205 205 LEU LEU B . n 
B 1 220 HIS 220 206 206 HIS HIS B . n 
B 1 221 VAL 221 207 207 VAL VAL B . n 
B 1 222 GLU 222 208 208 GLU GLU B . n 
B 1 223 LEU 223 209 209 LEU LEU B . n 
B 1 224 PRO 224 210 210 PRO PRO B . n 
B 1 225 GLU 225 211 211 GLU GLU B . n 
B 1 226 THR 226 212 212 THR THR B . n 
B 1 227 GLY 227 213 213 GLY GLY B . n 
B 1 228 GLY 228 214 214 GLY GLY B . n 
B 1 229 ILE 229 215 215 ILE ILE B . n 
B 1 230 ILE 230 216 216 ILE ILE B . n 
B 1 231 LEU 231 217 217 LEU LEU B . n 
B 1 232 ALA 232 218 218 ALA ALA B . n 
B 1 233 SER 233 219 219 SER SER B . n 
B 1 234 ASP 234 220 220 ASP ASP B . n 
B 1 235 ALA 235 221 221 ALA ALA B . n 
B 1 236 ILE 236 222 222 ILE ILE B . n 
B 1 237 TYR 237 223 223 TYR TYR B . n 
B 1 238 THR 238 224 224 THR THR B . n 
B 1 239 ALA 239 225 225 ALA ALA B . n 
B 1 240 GLU 240 226 226 GLU GLU B . n 
B 1 241 SER 241 227 227 SER SER B . n 
B 1 242 TYR 242 228 228 TYR TYR B . n 
B 1 243 GLY 243 229 229 GLY GLY B . n 
B 1 244 PRO 244 230 230 PRO PRO B . n 
B 1 245 PRO 245 231 231 PRO PRO B . n 
B 1 246 ILE 246 232 232 ILE ILE B . n 
B 1 247 LYS 247 233 233 LYS LYS B . n 
B 1 248 PRO 248 234 234 PRO PRO B . n 
B 1 249 PRO 249 235 235 PRO PRO B . n 
B 1 250 GLY 250 236 236 GLY GLY B . n 
B 1 251 ILE 251 237 237 ILE ILE B . n 
B 1 252 ILE 252 238 238 ILE ILE B . n 
B 1 253 TYR 253 239 239 TYR TYR B . n 
B 1 254 ASP 254 240 240 ASP ASP B . n 
B 1 255 SER 255 241 241 SER SER B . n 
B 1 256 LEU 256 242 242 LEU LEU B . n 
B 1 257 GLY 257 243 243 GLY GLY B . n 
B 1 258 TYR 258 244 244 TYR TYR B . n 
B 1 259 MET 259 245 245 MET MET B . n 
B 1 260 ASN 260 246 246 ASN ASN B . n 
B 1 261 THR 261 247 247 THR THR B . n 
B 1 262 VAL 262 248 248 VAL VAL B . n 
B 1 263 GLU 263 249 249 GLU GLU B . n 
B 1 264 ARG 264 250 250 ARG ARG B . n 
B 1 265 ILE 265 251 251 ILE ILE B . n 
B 1 266 ARG 266 252 252 ARG ARG B . n 
B 1 267 ARG 267 253 253 ARG ARG B . n 
B 1 268 ILE 268 254 254 ILE ILE B . n 
B 1 269 ALA 269 255 255 ALA ALA B . n 
B 1 270 GLN 270 256 256 GLN GLN B . n 
B 1 271 GLU 271 257 257 GLU GLU B . n 
B 1 272 THR 272 258 258 THR THR B . n 
B 1 273 LYS 273 259 259 LYS LYS B . n 
B 1 274 SER 274 260 260 SER SER B . n 
B 1 275 GLN 275 261 261 GLN GLN B . n 
B 1 276 VAL 276 262 262 VAL VAL B . n 
B 1 277 TRP 277 263 263 TRP TRP B . n 
B 1 278 PHE 278 264 264 PHE PHE B . n 
B 1 279 GLY 279 265 265 GLY GLY B . n 
B 1 280 HIS 280 266 266 HIS HIS B . n 
B 1 281 ASP 281 267 267 ASP ASP B . n 
B 1 282 ALA 282 268 268 ALA ALA B . n 
B 1 283 GLU 283 269 269 GLU GLU B . n 
B 1 284 GLN 284 270 270 GLN GLN B . n 
B 1 285 PHE 285 271 271 PHE PHE B . n 
B 1 286 LYS 286 272 272 LYS LYS B . n 
B 1 287 LYS 287 273 273 LYS LYS B . n 
B 1 288 PHE 288 274 274 PHE PHE B . n 
B 1 289 ARG 289 275 275 ARG ARG B . n 
B 1 290 LYS 290 276 276 LYS LYS B . n 
B 1 291 SER 291 277 277 SER SER B . n 
B 1 292 THR 292 278 278 THR THR B . n 
B 1 293 GLU 293 279 279 GLU GLU B . n 
B 1 294 GLY 294 280 280 GLY GLY B . n 
B 1 295 TYR 295 281 281 TYR TYR B . n 
B 1 296 TYR 296 282 282 TYR TYR B . n 
B 1 297 GLU 297 283 283 GLU GLU B . n 
C 1 1   TRP 1   -13 ?   ?   ?   C . n 
C 1 2   SER 2   -12 ?   ?   ?   C . n 
C 1 3   HIS 3   -11 ?   ?   ?   C . n 
C 1 4   PRO 4   -10 ?   ?   ?   C . n 
C 1 5   GLN 5   -9  ?   ?   ?   C . n 
C 1 6   PHE 6   -8  ?   ?   ?   C . n 
C 1 7   GLU 7   -7  ?   ?   ?   C . n 
C 1 8   LYS 8   -6  ?   ?   ?   C . n 
C 1 9   GLU 9   -5  ?   ?   ?   C . n 
C 1 10  ASN 10  -4  ?   ?   ?   C . n 
C 1 11  LEU 11  -3  ?   ?   ?   C . n 
C 1 12  TYR 12  -2  ?   ?   ?   C . n 
C 1 13  PHE 13  -1  ?   ?   ?   C . n 
C 1 14  GLN 14  0   ?   ?   ?   C . n 
C 1 15  SER 15  1   ?   ?   ?   C . n 
C 1 16  MET 16  2   ?   ?   ?   C . n 
C 1 17  ALA 17  3   ?   ?   ?   C . n 
C 1 18  ASN 18  4   ?   ?   ?   C . n 
C 1 19  VAL 19  5   ?   ?   ?   C . n 
C 1 20  ILE 20  6   ?   ?   ?   C . n 
C 1 21  LYS 21  7   ?   ?   ?   C . n 
C 1 22  ALA 22  8   8   ALA ALA C . n 
C 1 23  ARG 23  9   9   ARG ARG C . n 
C 1 24  PRO 24  10  10  PRO PRO C . n 
C 1 25  LYS 25  11  11  LYS LYS C . n 
C 1 26  LEU 26  12  12  LEU LEU C . n 
C 1 27  TYR 27  13  13  TYR TYR C . n 
C 1 28  VAL 28  14  14  VAL VAL C . n 
C 1 29  MET 29  15  15  MET MET C . n 
C 1 30  ASP 30  16  16  ASP ASP C . n 
C 1 31  ASN 31  17  17  ASN ASN C . n 
C 1 32  GLY 32  18  18  GLY GLY C . n 
C 1 33  ARG 33  19  19  ARG ARG C . n 
C 1 34  MET 34  20  20  MET MET C . n 
C 1 35  ARG 35  21  21  ARG ARG C . n 
C 1 36  MET 36  22  22  MET MET C . n 
C 1 37  ASP 37  23  23  ASP ASP C . n 
C 1 38  LYS 38  24  24  LYS LYS C . n 
C 1 39  ASN 39  25  25  ASN ASN C . n 
C 1 40  TRP 40  26  26  TRP TRP C . n 
C 1 41  MET 41  27  27  MET MET C . n 
C 1 42  ILE 42  28  28  ILE ILE C . n 
C 1 43  ALA 43  29  29  ALA ALA C . n 
C 1 44  MET 44  30  30  MET MET C . n 
C 1 45  HIS 45  31  31  HIS HIS C . n 
C 1 46  ASN 46  32  32  ASN ASN C . n 
C 1 47  PRO 47  33  33  PRO PRO C . n 
C 1 48  ALA 48  34  34  ALA ALA C . n 
C 1 49  THR 49  35  35  THR THR C . n 
C 1 50  ILE 50  36  36  ILE ILE C . n 
C 1 51  HIS 51  37  37  HIS HIS C . n 
C 1 52  ASN 52  38  38  ASN ASN C . n 
C 1 53  PRO 53  39  39  PRO PRO C . n 
C 1 54  ASN 54  40  40  ASN ASN C . n 
C 1 55  ALA 55  41  41  ALA ALA C . n 
C 1 56  GLN 56  42  42  GLN GLN C . n 
C 1 57  THR 57  43  43  THR THR C . n 
C 1 58  GLU 58  44  44  GLU GLU C . n 
C 1 59  PHE 59  45  45  PHE PHE C . n 
C 1 60  VAL 60  46  46  VAL VAL C . n 
C 1 61  GLU 61  47  47  GLU GLU C . n 
C 1 62  PHE 62  48  48  PHE PHE C . n 
C 1 63  PRO 63  49  49  PRO PRO C . n 
C 1 64  ILE 64  50  50  ILE ILE C . n 
C 1 65  TYR 65  51  51  TYR TYR C . n 
C 1 66  THR 66  52  52  THR THR C . n 
C 1 67  VAL 67  53  53  VAL VAL C . n 
C 1 68  LEU 68  54  54  LEU LEU C . n 
C 1 69  ILE 69  55  55  ILE ILE C . n 
C 1 70  ASP 70  56  56  ASP ASP C . n 
C 1 71  HIS 71  57  57  HIS HIS C . n 
C 1 72  PRO 72  58  58  PRO PRO C . n 
C 1 73  GLU 73  59  59  GLU GLU C . n 
C 1 74  GLY 74  60  60  GLY GLY C . n 
C 1 75  LYS 75  61  61  LYS LYS C . n 
C 1 76  ILE 76  62  62  ILE ILE C . n 
C 1 77  LEU 77  63  63  LEU LEU C . n 
C 1 78  PHE 78  64  64  PHE PHE C . n 
C 1 79  ASP 79  65  65  ASP ASP C . n 
C 1 80  THR 80  66  66  THR THR C . n 
C 1 81  SER 81  67  67  SER SER C . n 
C 1 82  CYS 82  68  68  CYS CYS C . n 
C 1 83  ASN 83  69  69  ASN ASN C . n 
C 1 84  PRO 84  70  70  PRO PRO C . n 
C 1 85  ASN 85  71  71  ASN ASN C . n 
C 1 86  SER 86  72  72  SER SER C . n 
C 1 87  MET 87  73  73  MET MET C . n 
C 1 88  GLY 88  74  74  GLY GLY C . n 
C 1 89  PRO 89  75  75  PRO PRO C . n 
C 1 90  GLN 90  76  76  GLN GLN C . n 
C 1 91  GLY 91  77  77  GLY GLY C . n 
C 1 92  ARG 92  78  78  ARG ARG C . n 
C 1 93  TRP 93  79  79  TRP TRP C . n 
C 1 94  ALA 94  80  80  ALA ALA C . n 
C 1 95  GLU 95  81  81  GLU GLU C . n 
C 1 96  SER 96  82  82  SER SER C . n 
C 1 97  THR 97  83  83  THR THR C . n 
C 1 98  GLN 98  84  84  GLN GLN C . n 
C 1 99  GLN 99  85  85  GLN GLN C . n 
C 1 100 MET 100 86  86  MET MET C . n 
C 1 101 PHE 101 87  87  PHE PHE C . n 
C 1 102 PRO 102 88  88  PRO PRO C . n 
C 1 103 TRP 103 89  89  TRP TRP C . n 
C 1 104 THR 104 90  90  THR THR C . n 
C 1 105 ALA 105 91  91  ALA ALA C . n 
C 1 106 THR 106 92  92  THR THR C . n 
C 1 107 GLU 107 93  93  GLU GLU C . n 
C 1 108 GLU 108 94  94  GLU GLU C . n 
C 1 109 CYS 109 95  95  CYS CYS C . n 
C 1 110 TYR 110 96  96  TYR TYR C . n 
C 1 111 LEU 111 97  97  LEU LEU C . n 
C 1 112 HIS 112 98  98  HIS HIS C . n 
C 1 113 ASN 113 99  99  ASN ASN C . n 
C 1 114 ARG 114 100 100 ARG ARG C . n 
C 1 115 LEU 115 101 101 LEU LEU C . n 
C 1 116 GLU 116 102 102 GLU GLU C . n 
C 1 117 GLN 117 103 103 GLN GLN C . n 
C 1 118 LEU 118 104 104 LEU LEU C . n 
C 1 119 LYS 119 105 105 LYS LYS C . n 
C 1 120 VAL 120 106 106 VAL VAL C . n 
C 1 121 ARG 121 107 107 ARG ARG C . n 
C 1 122 PRO 122 108 108 PRO PRO C . n 
C 1 123 GLU 123 109 109 GLU GLU C . n 
C 1 124 ASP 124 110 110 ASP ASP C . n 
C 1 125 ILE 125 111 111 ILE ILE C . n 
C 1 126 ARG 126 112 112 ARG ARG C . n 
C 1 127 TYR 127 113 113 TYR TYR C . n 
C 1 128 VAL 128 114 114 VAL VAL C . n 
C 1 129 VAL 129 115 115 VAL VAL C . n 
C 1 130 ALA 130 116 116 ALA ALA C . n 
C 1 131 SER 131 117 117 SER SER C . n 
C 1 132 HIS 132 118 118 HIS HIS C . n 
C 1 133 LEU 133 119 119 LEU LEU C . n 
C 1 134 HIS 134 120 120 HIS HIS C . n 
C 1 135 LEU 135 121 121 LEU LEU C . n 
C 1 136 ASN 136 122 122 ASN ASN C . n 
C 1 137 HIS 137 123 123 HIS HIS C . n 
C 1 138 ALA 138 124 124 ALA ALA C . n 
C 1 139 GLY 139 125 125 GLY GLY C . n 
C 1 140 CYS 140 126 126 CYS CYS C . n 
C 1 141 LEU 141 127 127 LEU LEU C . n 
C 1 142 GLU 142 128 128 GLU GLU C . n 
C 1 143 MET 143 129 129 MET MET C . n 
C 1 144 PHE 144 130 130 PHE PHE C . n 
C 1 145 THR 145 131 131 THR THR C . n 
C 1 146 ASN 146 132 132 ASN ASN C . n 
C 1 147 ALA 147 133 133 ALA ALA C . n 
C 1 148 THR 148 134 134 THR THR C . n 
C 1 149 ILE 149 135 135 ILE ILE C . n 
C 1 150 ILE 150 136 136 ILE ILE C . n 
C 1 151 VAL 151 137 137 VAL VAL C . n 
C 1 152 HIS 152 138 138 HIS HIS C . n 
C 1 153 GLU 153 139 139 GLU GLU C . n 
C 1 154 ASP 154 140 140 ASP ASP C . n 
C 1 155 GLU 155 141 141 GLU GLU C . n 
C 1 156 PHE 156 142 142 PHE PHE C . n 
C 1 157 ASN 157 143 143 ASN ASN C . n 
C 1 158 GLY 158 144 144 GLY GLY C . n 
C 1 159 ALA 159 145 145 ALA ALA C . n 
C 1 160 LEU 160 146 146 LEU LEU C . n 
C 1 161 GLN 161 147 147 GLN GLN C . n 
C 1 162 CYS 162 148 148 CYS CYS C . n 
C 1 163 TYR 163 149 149 TYR TYR C . n 
C 1 164 ALA 164 150 150 ALA ALA C . n 
C 1 165 ARG 165 151 151 ARG ARG C . n 
C 1 166 ASN 166 152 152 ASN ASN C . n 
C 1 167 GLN 167 153 153 GLN GLN C . n 
C 1 168 LYS 168 154 154 LYS LYS C . n 
C 1 169 GLU 169 155 155 GLU GLU C . n 
C 1 170 GLY 170 156 156 GLY GLY C . n 
C 1 171 ALA 171 157 157 ALA ALA C . n 
C 1 172 TYR 172 158 158 TYR TYR C . n 
C 1 173 ILE 173 159 159 ILE ILE C . n 
C 1 174 TRP 174 160 160 TRP TRP C . n 
C 1 175 ALA 175 161 161 ALA ALA C . n 
C 1 176 ASP 176 162 162 ASP ASP C . n 
C 1 177 ILE 177 163 163 ILE ILE C . n 
C 1 178 ASP 178 164 164 ASP ASP C . n 
C 1 179 ALA 179 165 165 ALA ALA C . n 
C 1 180 TRP 180 166 166 TRP TRP C . n 
C 1 181 ILE 181 167 167 ILE ILE C . n 
C 1 182 LYS 182 168 168 LYS LYS C . n 
C 1 183 ASN 183 169 169 ASN ASN C . n 
C 1 184 ASN 184 170 170 ASN ASN C . n 
C 1 185 LEU 185 171 171 LEU LEU C . n 
C 1 186 GLN 186 172 172 GLN GLN C . n 
C 1 187 TRP 187 173 173 TRP TRP C . n 
C 1 188 ARG 188 174 174 ARG ARG C . n 
C 1 189 THR 189 175 175 THR THR C . n 
C 1 190 VAL 190 176 176 VAL VAL C . n 
C 1 191 LYS 191 177 177 LYS LYS C . n 
C 1 192 ARG 192 178 178 ARG ARG C . n 
C 1 193 HIS 193 179 179 HIS HIS C . n 
C 1 194 GLU 194 180 180 GLU GLU C . n 
C 1 195 ASP 195 181 181 ASP ASP C . n 
C 1 196 ASN 196 182 182 ASN ASN C . n 
C 1 197 ILE 197 183 183 ILE ILE C . n 
C 1 198 LEU 198 184 184 LEU LEU C . n 
C 1 199 LEU 199 185 185 LEU LEU C . n 
C 1 200 ALA 200 186 186 ALA ALA C . n 
C 1 201 GLU 201 187 187 GLU GLU C . n 
C 1 202 GLY 202 188 188 GLY GLY C . n 
C 1 203 VAL 203 189 189 VAL VAL C . n 
C 1 204 LYS 204 190 190 LYS LYS C . n 
C 1 205 VAL 205 191 191 VAL VAL C . n 
C 1 206 LEU 206 192 192 LEU LEU C . n 
C 1 207 ASN 207 193 193 ASN ASN C . n 
C 1 208 PHE 208 194 194 PHE PHE C . n 
C 1 209 GLY 209 195 195 GLY GLY C . n 
C 1 210 SER 210 196 196 SER SER C . n 
C 1 211 GLY 211 197 197 GLY GLY C . n 
C 1 212 HIS 212 198 198 HIS HIS C . n 
C 1 213 ALA 213 199 199 ALA ALA C . n 
C 1 214 TRP 214 200 200 TRP TRP C . n 
C 1 215 GLY 215 201 201 GLY GLY C . n 
C 1 216 MET 216 202 202 MET MET C . n 
C 1 217 LEU 217 203 203 LEU LEU C . n 
C 1 218 GLY 218 204 204 GLY GLY C . n 
C 1 219 LEU 219 205 205 LEU LEU C . n 
C 1 220 HIS 220 206 206 HIS HIS C . n 
C 1 221 VAL 221 207 207 VAL VAL C . n 
C 1 222 GLU 222 208 208 GLU GLU C . n 
C 1 223 LEU 223 209 209 LEU LEU C . n 
C 1 224 PRO 224 210 210 PRO PRO C . n 
C 1 225 GLU 225 211 211 GLU GLU C . n 
C 1 226 THR 226 212 212 THR THR C . n 
C 1 227 GLY 227 213 213 GLY GLY C . n 
C 1 228 GLY 228 214 214 GLY GLY C . n 
C 1 229 ILE 229 215 215 ILE ILE C . n 
C 1 230 ILE 230 216 216 ILE ILE C . n 
C 1 231 LEU 231 217 217 LEU LEU C . n 
C 1 232 ALA 232 218 218 ALA ALA C . n 
C 1 233 SER 233 219 219 SER SER C . n 
C 1 234 ASP 234 220 220 ASP ASP C . n 
C 1 235 ALA 235 221 221 ALA ALA C . n 
C 1 236 ILE 236 222 222 ILE ILE C . n 
C 1 237 TYR 237 223 223 TYR TYR C . n 
C 1 238 THR 238 224 224 THR THR C . n 
C 1 239 ALA 239 225 225 ALA ALA C . n 
C 1 240 GLU 240 226 226 GLU GLU C . n 
C 1 241 SER 241 227 227 SER SER C . n 
C 1 242 TYR 242 228 228 TYR TYR C . n 
C 1 243 GLY 243 229 229 GLY GLY C . n 
C 1 244 PRO 244 230 230 PRO PRO C . n 
C 1 245 PRO 245 231 231 PRO PRO C . n 
C 1 246 ILE 246 232 232 ILE ILE C . n 
C 1 247 LYS 247 233 233 LYS LYS C . n 
C 1 248 PRO 248 234 234 PRO PRO C . n 
C 1 249 PRO 249 235 235 PRO PRO C . n 
C 1 250 GLY 250 236 236 GLY GLY C . n 
C 1 251 ILE 251 237 237 ILE ILE C . n 
C 1 252 ILE 252 238 238 ILE ILE C . n 
C 1 253 TYR 253 239 239 TYR TYR C . n 
C 1 254 ASP 254 240 240 ASP ASP C . n 
C 1 255 SER 255 241 241 SER SER C . n 
C 1 256 LEU 256 242 242 LEU LEU C . n 
C 1 257 GLY 257 243 243 GLY GLY C . n 
C 1 258 TYR 258 244 244 TYR TYR C . n 
C 1 259 MET 259 245 245 MET MET C . n 
C 1 260 ASN 260 246 246 ASN ASN C . n 
C 1 261 THR 261 247 247 THR THR C . n 
C 1 262 VAL 262 248 248 VAL VAL C . n 
C 1 263 GLU 263 249 249 GLU GLU C . n 
C 1 264 ARG 264 250 250 ARG ARG C . n 
C 1 265 ILE 265 251 251 ILE ILE C . n 
C 1 266 ARG 266 252 252 ARG ARG C . n 
C 1 267 ARG 267 253 253 ARG ARG C . n 
C 1 268 ILE 268 254 254 ILE ILE C . n 
C 1 269 ALA 269 255 255 ALA ALA C . n 
C 1 270 GLN 270 256 256 GLN GLN C . n 
C 1 271 GLU 271 257 257 GLU GLU C . n 
C 1 272 THR 272 258 258 THR THR C . n 
C 1 273 LYS 273 259 259 LYS LYS C . n 
C 1 274 SER 274 260 260 SER SER C . n 
C 1 275 GLN 275 261 261 GLN GLN C . n 
C 1 276 VAL 276 262 262 VAL VAL C . n 
C 1 277 TRP 277 263 263 TRP TRP C . n 
C 1 278 PHE 278 264 264 PHE PHE C . n 
C 1 279 GLY 279 265 265 GLY GLY C . n 
C 1 280 HIS 280 266 266 HIS HIS C . n 
C 1 281 ASP 281 267 267 ASP ASP C . n 
C 1 282 ALA 282 268 268 ALA ALA C . n 
C 1 283 GLU 283 269 269 GLU GLU C . n 
C 1 284 GLN 284 270 270 GLN GLN C . n 
C 1 285 PHE 285 271 271 PHE PHE C . n 
C 1 286 LYS 286 272 272 LYS LYS C . n 
C 1 287 LYS 287 273 273 LYS LYS C . n 
C 1 288 PHE 288 274 274 PHE PHE C . n 
C 1 289 ARG 289 275 275 ARG ARG C . n 
C 1 290 LYS 290 276 276 LYS LYS C . n 
C 1 291 SER 291 277 277 SER SER C . n 
C 1 292 THR 292 278 278 THR THR C . n 
C 1 293 GLU 293 279 279 GLU GLU C . n 
C 1 294 GLY 294 280 280 GLY GLY C . n 
C 1 295 TYR 295 281 281 TYR TYR C . n 
C 1 296 TYR 296 282 282 TYR TYR C . n 
C 1 297 GLU 297 283 283 GLU GLU C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CO 
_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 
D  2 CO  1   301 4   CO  CO  A . 
E  3 SO4 1   302 7   SO4 SO4 A . 
F  3 SO4 1   303 14  SO4 SO4 A . 
G  3 SO4 1   304 19  SO4 SO4 A . 
H  4 GOL 1   305 8   GOL GOL A . 
I  2 CO  1   301 2   CO  CO  B . 
J  3 SO4 1   302 1   SO4 SO4 B . 
K  3 SO4 1   303 2   SO4 SO4 B . 
L  3 SO4 1   304 3   SO4 SO4 B . 
M  3 SO4 1   305 6   SO4 SO4 B . 
N  3 SO4 1   306 13  SO4 SO4 B . 
O  3 SO4 1   307 17  SO4 SO4 B . 
P  3 SO4 1   308 18  SO4 SO4 B . 
Q  4 GOL 1   309 3   GOL GOL B . 
R  4 GOL 1   310 5   GOL GOL B . 
S  4 GOL 1   311 9   GOL GOL B . 
T  5 ACT 1   312 1   ACT ACT B . 
U  2 CO  1   301 5   CO  CO  C . 
V  3 SO4 1   302 15  SO4 SO4 C . 
W  3 SO4 1   303 16  SO4 SO4 C . 
X  5 ACT 1   304 2   ACT ACT C . 
Y  6 HOH 1   401 371 HOH HOH A . 
Y  6 HOH 2   402 434 HOH HOH A . 
Y  6 HOH 3   403 71  HOH HOH A . 
Y  6 HOH 4   404 341 HOH HOH A . 
Y  6 HOH 5   405 523 HOH HOH A . 
Y  6 HOH 6   406 235 HOH HOH A . 
Y  6 HOH 7   407 457 HOH HOH A . 
Y  6 HOH 8   408 484 HOH HOH A . 
Y  6 HOH 9   409 385 HOH HOH A . 
Y  6 HOH 10  410 103 HOH HOH A . 
Y  6 HOH 11  411 162 HOH HOH A . 
Y  6 HOH 12  412 333 HOH HOH A . 
Y  6 HOH 13  413 332 HOH HOH A . 
Y  6 HOH 14  414 291 HOH HOH A . 
Y  6 HOH 15  415 93  HOH HOH A . 
Y  6 HOH 16  416 340 HOH HOH A . 
Y  6 HOH 17  417 113 HOH HOH A . 
Y  6 HOH 18  418 88  HOH HOH A . 
Y  6 HOH 19  419 251 HOH HOH A . 
Y  6 HOH 20  420 277 HOH HOH A . 
Y  6 HOH 21  421 50  HOH HOH A . 
Y  6 HOH 22  422 365 HOH HOH A . 
Y  6 HOH 23  423 304 HOH HOH A . 
Y  6 HOH 24  424 142 HOH HOH A . 
Y  6 HOH 25  425 194 HOH HOH A . 
Y  6 HOH 26  426 518 HOH HOH A . 
Y  6 HOH 27  427 375 HOH HOH A . 
Y  6 HOH 28  428 459 HOH HOH A . 
Y  6 HOH 29  429 318 HOH HOH A . 
Y  6 HOH 30  430 391 HOH HOH A . 
Y  6 HOH 31  431 432 HOH HOH A . 
Y  6 HOH 32  432 192 HOH HOH A . 
Y  6 HOH 33  433 465 HOH HOH A . 
Y  6 HOH 34  434 450 HOH HOH A . 
Y  6 HOH 35  435 211 HOH HOH A . 
Y  6 HOH 36  436 226 HOH HOH A . 
Y  6 HOH 37  437 301 HOH HOH A . 
Y  6 HOH 38  438 492 HOH HOH A . 
Y  6 HOH 39  439 163 HOH HOH A . 
Y  6 HOH 40  440 30  HOH HOH A . 
Y  6 HOH 41  441 282 HOH HOH A . 
Y  6 HOH 42  442 132 HOH HOH A . 
Y  6 HOH 43  443 448 HOH HOH A . 
Y  6 HOH 44  444 118 HOH HOH A . 
Y  6 HOH 45  445 272 HOH HOH A . 
Y  6 HOH 46  446 281 HOH HOH A . 
Y  6 HOH 47  447 425 HOH HOH A . 
Y  6 HOH 48  448 61  HOH HOH A . 
Y  6 HOH 49  449 378 HOH HOH A . 
Y  6 HOH 50  450 187 HOH HOH A . 
Y  6 HOH 51  451 221 HOH HOH A . 
Y  6 HOH 52  452 334 HOH HOH A . 
Y  6 HOH 53  453 297 HOH HOH A . 
Y  6 HOH 54  454 3   HOH HOH A . 
Y  6 HOH 55  455 181 HOH HOH A . 
Y  6 HOH 56  456 164 HOH HOH A . 
Y  6 HOH 57  457 491 HOH HOH A . 
Y  6 HOH 58  458 39  HOH HOH A . 
Y  6 HOH 59  459 177 HOH HOH A . 
Y  6 HOH 60  460 207 HOH HOH A . 
Y  6 HOH 61  461 426 HOH HOH A . 
Y  6 HOH 62  462 519 HOH HOH A . 
Y  6 HOH 63  463 255 HOH HOH A . 
Y  6 HOH 64  464 51  HOH HOH A . 
Y  6 HOH 65  465 244 HOH HOH A . 
Y  6 HOH 66  466 200 HOH HOH A . 
Y  6 HOH 67  467 417 HOH HOH A . 
Y  6 HOH 68  468 435 HOH HOH A . 
Y  6 HOH 69  469 386 HOH HOH A . 
Y  6 HOH 70  470 265 HOH HOH A . 
Y  6 HOH 71  471 453 HOH HOH A . 
Y  6 HOH 72  472 260 HOH HOH A . 
Y  6 HOH 73  473 35  HOH HOH A . 
Y  6 HOH 74  474 83  HOH HOH A . 
Y  6 HOH 75  475 157 HOH HOH A . 
Y  6 HOH 76  476 506 HOH HOH A . 
Y  6 HOH 77  477 306 HOH HOH A . 
Y  6 HOH 78  478 481 HOH HOH A . 
Y  6 HOH 79  479 15  HOH HOH A . 
Y  6 HOH 80  480 84  HOH HOH A . 
Y  6 HOH 81  481 144 HOH HOH A . 
Y  6 HOH 82  482 447 HOH HOH A . 
Y  6 HOH 83  483 195 HOH HOH A . 
Y  6 HOH 84  484 24  HOH HOH A . 
Y  6 HOH 85  485 213 HOH HOH A . 
Y  6 HOH 86  486 183 HOH HOH A . 
Y  6 HOH 87  487 382 HOH HOH A . 
Y  6 HOH 88  488 89  HOH HOH A . 
Y  6 HOH 89  489 443 HOH HOH A . 
Y  6 HOH 90  490 307 HOH HOH A . 
Y  6 HOH 91  491 369 HOH HOH A . 
Y  6 HOH 92  492 476 HOH HOH A . 
Y  6 HOH 93  493 339 HOH HOH A . 
Y  6 HOH 94  494 173 HOH HOH A . 
Y  6 HOH 95  495 470 HOH HOH A . 
Y  6 HOH 96  496 495 HOH HOH A . 
Y  6 HOH 97  497 143 HOH HOH A . 
Y  6 HOH 98  498 300 HOH HOH A . 
Y  6 HOH 99  499 295 HOH HOH A . 
Y  6 HOH 100 500 218 HOH HOH A . 
Y  6 HOH 101 501 8   HOH HOH A . 
Y  6 HOH 102 502 440 HOH HOH A . 
Y  6 HOH 103 503 475 HOH HOH A . 
Y  6 HOH 104 504 323 HOH HOH A . 
Y  6 HOH 105 505 503 HOH HOH A . 
Y  6 HOH 106 506 57  HOH HOH A . 
Y  6 HOH 107 507 415 HOH HOH A . 
Y  6 HOH 108 508 185 HOH HOH A . 
Y  6 HOH 109 509 296 HOH HOH A . 
Y  6 HOH 110 510 438 HOH HOH A . 
Y  6 HOH 111 511 241 HOH HOH A . 
Y  6 HOH 112 512 353 HOH HOH A . 
Y  6 HOH 113 513 180 HOH HOH A . 
Y  6 HOH 114 514 193 HOH HOH A . 
Y  6 HOH 115 515 217 HOH HOH A . 
Y  6 HOH 116 516 367 HOH HOH A . 
Y  6 HOH 117 517 273 HOH HOH A . 
Y  6 HOH 118 518 366 HOH HOH A . 
Y  6 HOH 119 519 381 HOH HOH A . 
Y  6 HOH 120 520 41  HOH HOH A . 
Y  6 HOH 121 521 311 HOH HOH A . 
Y  6 HOH 122 522 467 HOH HOH A . 
Y  6 HOH 123 523 380 HOH HOH A . 
Y  6 HOH 124 524 342 HOH HOH A . 
Y  6 HOH 125 525 321 HOH HOH A . 
Y  6 HOH 126 526 227 HOH HOH A . 
Y  6 HOH 127 527 368 HOH HOH A . 
Y  6 HOH 128 528 14  HOH HOH A . 
Y  6 HOH 129 529 460 HOH HOH A . 
Y  6 HOH 130 530 238 HOH HOH A . 
Y  6 HOH 131 531 77  HOH HOH A . 
Y  6 HOH 132 532 156 HOH HOH A . 
Y  6 HOH 133 533 174 HOH HOH A . 
Y  6 HOH 134 534 469 HOH HOH A . 
Y  6 HOH 135 535 520 HOH HOH A . 
Y  6 HOH 136 536 136 HOH HOH A . 
Y  6 HOH 137 537 242 HOH HOH A . 
Y  6 HOH 138 538 254 HOH HOH A . 
Y  6 HOH 139 539 436 HOH HOH A . 
Z  6 HOH 1   401 483 HOH HOH B . 
Z  6 HOH 2   402 480 HOH HOH B . 
Z  6 HOH 3   403 169 HOH HOH B . 
Z  6 HOH 4   404 28  HOH HOH B . 
Z  6 HOH 5   405 288 HOH HOH B . 
Z  6 HOH 6   406 445 HOH HOH B . 
Z  6 HOH 7   407 130 HOH HOH B . 
Z  6 HOH 8   408 65  HOH HOH B . 
Z  6 HOH 9   409 396 HOH HOH B . 
Z  6 HOH 10  410 394 HOH HOH B . 
Z  6 HOH 11  411 452 HOH HOH B . 
Z  6 HOH 12  412 80  HOH HOH B . 
Z  6 HOH 13  413 129 HOH HOH B . 
Z  6 HOH 14  414 171 HOH HOH B . 
Z  6 HOH 15  415 384 HOH HOH B . 
Z  6 HOH 16  416 379 HOH HOH B . 
Z  6 HOH 17  417 96  HOH HOH B . 
Z  6 HOH 18  418 444 HOH HOH B . 
Z  6 HOH 19  419 283 HOH HOH B . 
Z  6 HOH 20  420 337 HOH HOH B . 
Z  6 HOH 21  421 262 HOH HOH B . 
Z  6 HOH 22  422 393 HOH HOH B . 
Z  6 HOH 23  423 208 HOH HOH B . 
Z  6 HOH 24  424 313 HOH HOH B . 
Z  6 HOH 25  425 165 HOH HOH B . 
Z  6 HOH 26  426 298 HOH HOH B . 
Z  6 HOH 27  427 34  HOH HOH B . 
Z  6 HOH 28  428 498 HOH HOH B . 
Z  6 HOH 29  429 98  HOH HOH B . 
Z  6 HOH 30  430 66  HOH HOH B . 
Z  6 HOH 31  431 416 HOH HOH B . 
Z  6 HOH 32  432 104 HOH HOH B . 
Z  6 HOH 33  433 68  HOH HOH B . 
Z  6 HOH 34  434 47  HOH HOH B . 
Z  6 HOH 35  435 317 HOH HOH B . 
Z  6 HOH 36  436 23  HOH HOH B . 
Z  6 HOH 37  437 67  HOH HOH B . 
Z  6 HOH 38  438 487 HOH HOH B . 
Z  6 HOH 39  439 526 HOH HOH B . 
Z  6 HOH 40  440 151 HOH HOH B . 
Z  6 HOH 41  441 175 HOH HOH B . 
Z  6 HOH 42  442 85  HOH HOH B . 
Z  6 HOH 43  443 290 HOH HOH B . 
Z  6 HOH 44  444 22  HOH HOH B . 
Z  6 HOH 45  445 108 HOH HOH B . 
Z  6 HOH 46  446 437 HOH HOH B . 
Z  6 HOH 47  447 494 HOH HOH B . 
Z  6 HOH 48  448 446 HOH HOH B . 
Z  6 HOH 49  449 266 HOH HOH B . 
Z  6 HOH 50  450 166 HOH HOH B . 
Z  6 HOH 51  451 81  HOH HOH B . 
Z  6 HOH 52  452 148 HOH HOH B . 
Z  6 HOH 53  453 400 HOH HOH B . 
Z  6 HOH 54  454 161 HOH HOH B . 
Z  6 HOH 55  455 504 HOH HOH B . 
Z  6 HOH 56  456 117 HOH HOH B . 
Z  6 HOH 57  457 292 HOH HOH B . 
Z  6 HOH 58  458 319 HOH HOH B . 
Z  6 HOH 59  459 397 HOH HOH B . 
Z  6 HOH 60  460 134 HOH HOH B . 
Z  6 HOH 61  461 95  HOH HOH B . 
Z  6 HOH 62  462 404 HOH HOH B . 
Z  6 HOH 63  463 87  HOH HOH B . 
Z  6 HOH 64  464 100 HOH HOH B . 
Z  6 HOH 65  465 186 HOH HOH B . 
Z  6 HOH 66  466 127 HOH HOH B . 
Z  6 HOH 67  467 493 HOH HOH B . 
Z  6 HOH 68  468 276 HOH HOH B . 
Z  6 HOH 69  469 477 HOH HOH B . 
Z  6 HOH 70  470 138 HOH HOH B . 
Z  6 HOH 71  471 376 HOH HOH B . 
Z  6 HOH 72  472 405 HOH HOH B . 
Z  6 HOH 73  473 147 HOH HOH B . 
Z  6 HOH 74  474 395 HOH HOH B . 
Z  6 HOH 75  475 249 HOH HOH B . 
Z  6 HOH 76  476 114 HOH HOH B . 
Z  6 HOH 77  477 152 HOH HOH B . 
Z  6 HOH 78  478 79  HOH HOH B . 
Z  6 HOH 79  479 312 HOH HOH B . 
Z  6 HOH 80  480 4   HOH HOH B . 
Z  6 HOH 81  481 46  HOH HOH B . 
Z  6 HOH 82  482 124 HOH HOH B . 
Z  6 HOH 83  483 451 HOH HOH B . 
Z  6 HOH 84  484 233 HOH HOH B . 
Z  6 HOH 85  485 472 HOH HOH B . 
Z  6 HOH 86  486 44  HOH HOH B . 
Z  6 HOH 87  487 285 HOH HOH B . 
Z  6 HOH 88  488 197 HOH HOH B . 
Z  6 HOH 89  489 29  HOH HOH B . 
Z  6 HOH 90  490 168 HOH HOH B . 
Z  6 HOH 91  491 468 HOH HOH B . 
Z  6 HOH 92  492 303 HOH HOH B . 
Z  6 HOH 93  493 203 HOH HOH B . 
Z  6 HOH 94  494 499 HOH HOH B . 
Z  6 HOH 95  495 214 HOH HOH B . 
Z  6 HOH 96  496 253 HOH HOH B . 
Z  6 HOH 97  497 331 HOH HOH B . 
Z  6 HOH 98  498 419 HOH HOH B . 
Z  6 HOH 99  499 329 HOH HOH B . 
Z  6 HOH 100 500 27  HOH HOH B . 
Z  6 HOH 101 501 413 HOH HOH B . 
Z  6 HOH 102 502 154 HOH HOH B . 
Z  6 HOH 103 503 17  HOH HOH B . 
Z  6 HOH 104 504 324 HOH HOH B . 
Z  6 HOH 105 505 338 HOH HOH B . 
Z  6 HOH 106 506 36  HOH HOH B . 
Z  6 HOH 107 507 422 HOH HOH B . 
Z  6 HOH 108 508 92  HOH HOH B . 
Z  6 HOH 109 509 158 HOH HOH B . 
Z  6 HOH 110 510 344 HOH HOH B . 
Z  6 HOH 111 511 216 HOH HOH B . 
Z  6 HOH 112 512 412 HOH HOH B . 
Z  6 HOH 113 513 13  HOH HOH B . 
Z  6 HOH 114 514 31  HOH HOH B . 
Z  6 HOH 115 515 6   HOH HOH B . 
Z  6 HOH 116 516 212 HOH HOH B . 
Z  6 HOH 117 517 11  HOH HOH B . 
Z  6 HOH 118 518 361 HOH HOH B . 
Z  6 HOH 119 519 287 HOH HOH B . 
Z  6 HOH 120 520 270 HOH HOH B . 
Z  6 HOH 121 521 289 HOH HOH B . 
Z  6 HOH 122 522 330 HOH HOH B . 
Z  6 HOH 123 523 420 HOH HOH B . 
Z  6 HOH 124 524 7   HOH HOH B . 
Z  6 HOH 125 525 223 HOH HOH B . 
Z  6 HOH 126 526 343 HOH HOH B . 
Z  6 HOH 127 527 202 HOH HOH B . 
Z  6 HOH 128 528 496 HOH HOH B . 
Z  6 HOH 129 529 299 HOH HOH B . 
Z  6 HOH 130 530 115 HOH HOH B . 
Z  6 HOH 131 531 49  HOH HOH B . 
Z  6 HOH 132 532 512 HOH HOH B . 
Z  6 HOH 133 533 471 HOH HOH B . 
Z  6 HOH 134 534 398 HOH HOH B . 
Z  6 HOH 135 535 383 HOH HOH B . 
Z  6 HOH 136 536 116 HOH HOH B . 
Z  6 HOH 137 537 458 HOH HOH B . 
Z  6 HOH 138 538 70  HOH HOH B . 
Z  6 HOH 139 539 178 HOH HOH B . 
Z  6 HOH 140 540 402 HOH HOH B . 
Z  6 HOH 141 541 128 HOH HOH B . 
Z  6 HOH 142 542 256 HOH HOH B . 
Z  6 HOH 143 543 489 HOH HOH B . 
Z  6 HOH 144 544 94  HOH HOH B . 
Z  6 HOH 145 545 43  HOH HOH B . 
Z  6 HOH 146 546 234 HOH HOH B . 
Z  6 HOH 147 547 210 HOH HOH B . 
Z  6 HOH 148 548 284 HOH HOH B . 
Z  6 HOH 149 549 131 HOH HOH B . 
Z  6 HOH 150 550 511 HOH HOH B . 
Z  6 HOH 151 551 101 HOH HOH B . 
Z  6 HOH 152 552 327 HOH HOH B . 
Z  6 HOH 153 553 325 HOH HOH B . 
Z  6 HOH 154 554 62  HOH HOH B . 
Z  6 HOH 155 555 509 HOH HOH B . 
Z  6 HOH 156 556 322 HOH HOH B . 
Z  6 HOH 157 557 501 HOH HOH B . 
Z  6 HOH 158 558 508 HOH HOH B . 
Z  6 HOH 159 559 513 HOH HOH B . 
Z  6 HOH 160 560 510 HOH HOH B . 
Z  6 HOH 161 561 328 HOH HOH B . 
Z  6 HOH 162 562 167 HOH HOH B . 
Z  6 HOH 163 563 439 HOH HOH B . 
AA 6 HOH 1   401 316 HOH HOH C . 
AA 6 HOH 2   402 32  HOH HOH C . 
AA 6 HOH 3   403 354 HOH HOH C . 
AA 6 HOH 4   404 348 HOH HOH C . 
AA 6 HOH 5   405 346 HOH HOH C . 
AA 6 HOH 6   406 97  HOH HOH C . 
AA 6 HOH 7   407 350 HOH HOH C . 
AA 6 HOH 8   408 239 HOH HOH C . 
AA 6 HOH 9   409 42  HOH HOH C . 
AA 6 HOH 10  410 399 HOH HOH C . 
AA 6 HOH 11  411 279 HOH HOH C . 
AA 6 HOH 12  412 429 HOH HOH C . 
AA 6 HOH 13  413 160 HOH HOH C . 
AA 6 HOH 14  414 421 HOH HOH C . 
AA 6 HOH 15  415 247 HOH HOH C . 
AA 6 HOH 16  416 479 HOH HOH C . 
AA 6 HOH 17  417 516 HOH HOH C . 
AA 6 HOH 18  418 363 HOH HOH C . 
AA 6 HOH 19  419 521 HOH HOH C . 
AA 6 HOH 20  420 189 HOH HOH C . 
AA 6 HOH 21  421 485 HOH HOH C . 
AA 6 HOH 22  422 464 HOH HOH C . 
AA 6 HOH 23  423 153 HOH HOH C . 
AA 6 HOH 24  424 111 HOH HOH C . 
AA 6 HOH 25  425 280 HOH HOH C . 
AA 6 HOH 26  426 462 HOH HOH C . 
AA 6 HOH 27  427 293 HOH HOH C . 
AA 6 HOH 28  428 389 HOH HOH C . 
AA 6 HOH 29  429 345 HOH HOH C . 
AA 6 HOH 30  430 222 HOH HOH C . 
AA 6 HOH 31  431 442 HOH HOH C . 
AA 6 HOH 32  432 123 HOH HOH C . 
AA 6 HOH 33  433 403 HOH HOH C . 
AA 6 HOH 34  434 502 HOH HOH C . 
AA 6 HOH 35  435 53  HOH HOH C . 
AA 6 HOH 36  436 473 HOH HOH C . 
AA 6 HOH 37  437 40  HOH HOH C . 
AA 6 HOH 38  438 48  HOH HOH C . 
AA 6 HOH 39  439 37  HOH HOH C . 
AA 6 HOH 40  440 315 HOH HOH C . 
AA 6 HOH 41  441 463 HOH HOH C . 
AA 6 HOH 42  442 150 HOH HOH C . 
AA 6 HOH 43  443 20  HOH HOH C . 
AA 6 HOH 44  444 411 HOH HOH C . 
AA 6 HOH 45  445 109 HOH HOH C . 
AA 6 HOH 46  446 230 HOH HOH C . 
AA 6 HOH 47  447 82  HOH HOH C . 
AA 6 HOH 48  448 76  HOH HOH C . 
AA 6 HOH 49  449 392 HOH HOH C . 
AA 6 HOH 50  450 358 HOH HOH C . 
AA 6 HOH 51  451 9   HOH HOH C . 
AA 6 HOH 52  452 33  HOH HOH C . 
AA 6 HOH 53  453 119 HOH HOH C . 
AA 6 HOH 54  454 488 HOH HOH C . 
AA 6 HOH 55  455 122 HOH HOH C . 
AA 6 HOH 56  456 90  HOH HOH C . 
AA 6 HOH 57  457 112 HOH HOH C . 
AA 6 HOH 58  458 302 HOH HOH C . 
AA 6 HOH 59  459 261 HOH HOH C . 
AA 6 HOH 60  460 55  HOH HOH C . 
AA 6 HOH 61  461 56  HOH HOH C . 
AA 6 HOH 62  462 86  HOH HOH C . 
AA 6 HOH 63  463 133 HOH HOH C . 
AA 6 HOH 64  464 268 HOH HOH C . 
AA 6 HOH 65  465 441 HOH HOH C . 
AA 6 HOH 66  466 18  HOH HOH C . 
AA 6 HOH 67  467 198 HOH HOH C . 
AA 6 HOH 68  468 149 HOH HOH C . 
AA 6 HOH 69  469 190 HOH HOH C . 
AA 6 HOH 70  470 461 HOH HOH C . 
AA 6 HOH 71  471 58  HOH HOH C . 
AA 6 HOH 72  472 141 HOH HOH C . 
AA 6 HOH 73  473 250 HOH HOH C . 
AA 6 HOH 74  474 155 HOH HOH C . 
AA 6 HOH 75  475 206 HOH HOH C . 
AA 6 HOH 76  476 126 HOH HOH C . 
AA 6 HOH 77  477 517 HOH HOH C . 
AA 6 HOH 78  478 456 HOH HOH C . 
AA 6 HOH 79  479 38  HOH HOH C . 
AA 6 HOH 80  480 423 HOH HOH C . 
AA 6 HOH 81  481 286 HOH HOH C . 
AA 6 HOH 82  482 267 HOH HOH C . 
AA 6 HOH 83  483 191 HOH HOH C . 
AA 6 HOH 84  484 390 HOH HOH C . 
AA 6 HOH 85  485 225 HOH HOH C . 
AA 6 HOH 86  486 428 HOH HOH C . 
AA 6 HOH 87  487 188 HOH HOH C . 
AA 6 HOH 88  488 352 HOH HOH C . 
AA 6 HOH 89  489 356 HOH HOH C . 
AA 6 HOH 90  490 52  HOH HOH C . 
AA 6 HOH 91  491 466 HOH HOH C . 
AA 6 HOH 92  492 201 HOH HOH C . 
AA 6 HOH 93  493 259 HOH HOH C . 
AA 6 HOH 94  494 219 HOH HOH C . 
AA 6 HOH 95  495 102 HOH HOH C . 
AA 6 HOH 96  496 237 HOH HOH C . 
AA 6 HOH 97  497 524 HOH HOH C . 
AA 6 HOH 98  498 258 HOH HOH C . 
AA 6 HOH 99  499 357 HOH HOH C . 
AA 6 HOH 100 500 449 HOH HOH C . 
AA 6 HOH 101 501 19  HOH HOH C . 
AA 6 HOH 102 502 474 HOH HOH C . 
AA 6 HOH 103 503 231 HOH HOH C . 
AA 6 HOH 104 504 335 HOH HOH C . 
AA 6 HOH 105 505 25  HOH HOH C . 
AA 6 HOH 106 506 500 HOH HOH C . 
AA 6 HOH 107 507 401 HOH HOH C . 
AA 6 HOH 108 508 224 HOH HOH C . 
AA 6 HOH 109 509 59  HOH HOH C . 
AA 6 HOH 110 510 45  HOH HOH C . 
AA 6 HOH 111 511 205 HOH HOH C . 
AA 6 HOH 112 512 349 HOH HOH C . 
AA 6 HOH 113 513 91  HOH HOH C . 
AA 6 HOH 114 514 26  HOH HOH C . 
AA 6 HOH 115 515 99  HOH HOH C . 
AA 6 HOH 116 516 121 HOH HOH C . 
AA 6 HOH 117 517 514 HOH HOH C . 
AA 6 HOH 118 518 21  HOH HOH C . 
AA 6 HOH 119 519 373 HOH HOH C . 
AA 6 HOH 120 520 431 HOH HOH C . 
AA 6 HOH 121 521 347 HOH HOH C . 
AA 6 HOH 122 522 326 HOH HOH C . 
AA 6 HOH 123 523 387 HOH HOH C . 
AA 6 HOH 124 524 240 HOH HOH C . 
AA 6 HOH 125 525 137 HOH HOH C . 
AA 6 HOH 126 526 16  HOH HOH C . 
AA 6 HOH 127 527 220 HOH HOH C . 
AA 6 HOH 128 528 424 HOH HOH C . 
AA 6 HOH 129 529 274 HOH HOH C . 
AA 6 HOH 130 530 418 HOH HOH C . 
AA 6 HOH 131 531 515 HOH HOH C . 
AA 6 HOH 132 532 454 HOH HOH C . 
AA 6 HOH 133 533 308 HOH HOH C . 
AA 6 HOH 134 534 106 HOH HOH C . 
AA 6 HOH 135 535 176 HOH HOH C . 
AA 6 HOH 136 536 407 HOH HOH C . 
AA 6 HOH 137 537 135 HOH HOH C . 
AA 6 HOH 138 538 229 HOH HOH C . 
AA 6 HOH 139 539 63  HOH HOH C . 
AA 6 HOH 140 540 228 HOH HOH C . 
AA 6 HOH 141 541 427 HOH HOH C . 
AA 6 HOH 142 542 146 HOH HOH C . 
AA 6 HOH 143 543 107 HOH HOH C . 
AA 6 HOH 144 544 246 HOH HOH C . 
AA 6 HOH 145 545 529 HOH HOH C . 
AA 6 HOH 146 546 505 HOH HOH C . 
AA 6 HOH 147 547 525 HOH HOH C . 
AA 6 HOH 148 548 139 HOH HOH C . 
AA 6 HOH 149 549 522 HOH HOH C . 
AA 6 HOH 150 550 377 HOH HOH C . 
AA 6 HOH 151 551 72  HOH HOH C . 
AA 6 HOH 152 552 430 HOH HOH C . 
AA 6 HOH 153 553 140 HOH HOH C . 
AA 6 HOH 154 554 105 HOH HOH C . 
AA 6 HOH 155 555 269 HOH HOH C . 
AA 6 HOH 156 556 179 HOH HOH C . 
AA 6 HOH 157 557 530 HOH HOH C . 
AA 6 HOH 158 558 75  HOH HOH C . 
AA 6 HOH 159 559 263 HOH HOH C . 
AA 6 HOH 160 560 275 HOH HOH C . 
AA 6 HOH 161 561 243 HOH HOH C . 
AA 6 HOH 162 562 245 HOH HOH C . 
AA 6 HOH 163 563 507 HOH HOH C . 
AA 6 HOH 164 564 145 HOH HOH C . 
AA 6 HOH 165 565 199 HOH HOH C . 
AA 6 HOH 166 566 232 HOH HOH C . 
AA 6 HOH 167 567 478 HOH HOH C . 
AA 6 HOH 168 568 294 HOH HOH C . 
AA 6 HOH 169 569 490 HOH HOH C . 
AA 6 HOH 170 570 410 HOH HOH C . 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   115.95 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B2N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     146.360 
_cell.length_a_esd                 ? 
_cell.length_b                     109.080 
_cell.length_b_esd                 ? 
_cell.length_c                     78.740 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9B2N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 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                   9B2N 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.54 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.0 - 1.25 M ammonium sulfate and 0.1 M sodium acetate pH 4.0 - 5.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-03-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.03317 
_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                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03317 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B2N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.9 
_reflns.d_resolution_low                               19.65 
_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                                     85892 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.17 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.11 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.076 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.9 
_reflns_shell.d_res_low                                     2.0 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.49 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12226 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.72 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.88 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.84 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -2.30 
_refine.aniso_B[2][2]                            3.54 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.45 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.838 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9B2N 
_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                            1.90 
_refine.ls_d_res_low                             19.65 
_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                     82670 
_refine.ls_number_reflns_R_free                  4352 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21384 
_refine.ls_R_factor_R_free                       0.22346 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21333 
_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                       0.156 
_refine.pdbx_overall_ESU_R_Free                  0.130 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.111 
_refine.overall_SU_ML                            0.113 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        19.65 
_refine_hist.number_atoms_solvent             472 
_refine_hist.number_atoms_total               7273 
_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        6706 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         95 
_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' ? 0.002  0.012  7212  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.016  6539  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.775  1.822  9817  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.288  1.771  15061 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.914  5.000  870   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.475  5.000  47    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.094 10.000 1194  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.040  0.200  1013  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  8721  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1755  ? 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' ? 2.384  2.951  3416  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.382  2.950  3413  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.257  5.308  4297  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.257  5.308  4298  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.261  3.336  3796  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.261  3.337  3797  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.927  5.966  5518  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.548  35.66  8087  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.548  35.66  8088  ? 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                       1.900 
_refine_ls_shell.d_res_low                        1.949 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             321 
_refine_ls_shell.number_reflns_R_work             6081 
_refine_ls_shell.percent_reflns_obs               99.61 
_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                  0.359 
_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                  0.354 
# 
_struct.entry_id                     9B2N 
_struct.title                        'Structure of the quorum quenching lactonase GcL D122N mutant - monometal center' 
_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        9B2N 
_struct_keywords.text            'quorum sensing, quorum quenching, lactonase, metalloenzyme, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 3 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 4 ? 
I  N N 2 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 5 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 5 ? 
Y  N N 6 ? 
Z  N N 6 ? 
AA N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A023DFE8_9BACI 
_struct_ref.pdbx_db_accession          A0A023DFE8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MANVIKARPKLYVMDNGRMRMDKNWMIAMHNPATIHNPNAQTEFVEFPIYTVLIDHPEGKILFDTSCNPNSMGPQGRWAE
STQQMFPWTATEECYLHNRLEQLKVRPEDIRYVVASHLHLDHAGCLEMFTNATIIVHEDEFNGALQCYARNQKEGAYIWA
DIDAWIKNNLQWRTVKRHEDNILLAEGVKVLNFGSGHAWGMLGLHVELPETGGIILASDAIYTAESYGPPIKPPGIIYDS
LGYMNTVERIRRIAQETKSQVWFGHDAEQFKKFRKSTEGYYE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9B2N A 16 ? 297 ? A0A023DFE8 1 ? 282 ? 2 283 
2 1 9B2N B 16 ? 297 ? A0A023DFE8 1 ? 282 ? 2 283 
3 1 9B2N C 16 ? 297 ? A0A023DFE8 1 ? 282 ? 2 283 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9B2N TRP A 1   ? UNP A0A023DFE8 ?   ?   'expression tag'      -13 1  
1 9B2N SER A 2   ? UNP A0A023DFE8 ?   ?   'expression tag'      -12 2  
1 9B2N HIS A 3   ? UNP A0A023DFE8 ?   ?   'expression tag'      -11 3  
1 9B2N PRO A 4   ? UNP A0A023DFE8 ?   ?   'expression tag'      -10 4  
1 9B2N GLN A 5   ? UNP A0A023DFE8 ?   ?   'expression tag'      -9  5  
1 9B2N PHE A 6   ? UNP A0A023DFE8 ?   ?   'expression tag'      -8  6  
1 9B2N GLU A 7   ? UNP A0A023DFE8 ?   ?   'expression tag'      -7  7  
1 9B2N LYS A 8   ? UNP A0A023DFE8 ?   ?   'expression tag'      -6  8  
1 9B2N GLU A 9   ? UNP A0A023DFE8 ?   ?   'expression tag'      -5  9  
1 9B2N ASN A 10  ? UNP A0A023DFE8 ?   ?   'expression tag'      -4  10 
1 9B2N LEU A 11  ? UNP A0A023DFE8 ?   ?   'expression tag'      -3  11 
1 9B2N TYR A 12  ? UNP A0A023DFE8 ?   ?   'expression tag'      -2  12 
1 9B2N PHE A 13  ? UNP A0A023DFE8 ?   ?   'expression tag'      -1  13 
1 9B2N GLN A 14  ? UNP A0A023DFE8 ?   ?   'expression tag'      0   14 
1 9B2N SER A 15  ? UNP A0A023DFE8 ?   ?   'expression tag'      1   15 
1 9B2N ASN A 136 ? UNP A0A023DFE8 ASP 121 'engineered mutation' 122 16 
2 9B2N TRP B 1   ? UNP A0A023DFE8 ?   ?   'expression tag'      -13 17 
2 9B2N SER B 2   ? UNP A0A023DFE8 ?   ?   'expression tag'      -12 18 
2 9B2N HIS B 3   ? UNP A0A023DFE8 ?   ?   'expression tag'      -11 19 
2 9B2N PRO B 4   ? UNP A0A023DFE8 ?   ?   'expression tag'      -10 20 
2 9B2N GLN B 5   ? UNP A0A023DFE8 ?   ?   'expression tag'      -9  21 
2 9B2N PHE B 6   ? UNP A0A023DFE8 ?   ?   'expression tag'      -8  22 
2 9B2N GLU B 7   ? UNP A0A023DFE8 ?   ?   'expression tag'      -7  23 
2 9B2N LYS B 8   ? UNP A0A023DFE8 ?   ?   'expression tag'      -6  24 
2 9B2N GLU B 9   ? UNP A0A023DFE8 ?   ?   'expression tag'      -5  25 
2 9B2N ASN B 10  ? UNP A0A023DFE8 ?   ?   'expression tag'      -4  26 
2 9B2N LEU B 11  ? UNP A0A023DFE8 ?   ?   'expression tag'      -3  27 
2 9B2N TYR B 12  ? UNP A0A023DFE8 ?   ?   'expression tag'      -2  28 
2 9B2N PHE B 13  ? UNP A0A023DFE8 ?   ?   'expression tag'      -1  29 
2 9B2N GLN B 14  ? UNP A0A023DFE8 ?   ?   'expression tag'      0   30 
2 9B2N SER B 15  ? UNP A0A023DFE8 ?   ?   'expression tag'      1   31 
2 9B2N ASN B 136 ? UNP A0A023DFE8 ASP 121 'engineered mutation' 122 32 
3 9B2N TRP C 1   ? UNP A0A023DFE8 ?   ?   'expression tag'      -13 33 
3 9B2N SER C 2   ? UNP A0A023DFE8 ?   ?   'expression tag'      -12 34 
3 9B2N HIS C 3   ? UNP A0A023DFE8 ?   ?   'expression tag'      -11 35 
3 9B2N PRO C 4   ? UNP A0A023DFE8 ?   ?   'expression tag'      -10 36 
3 9B2N GLN C 5   ? UNP A0A023DFE8 ?   ?   'expression tag'      -9  37 
3 9B2N PHE C 6   ? UNP A0A023DFE8 ?   ?   'expression tag'      -8  38 
3 9B2N GLU C 7   ? UNP A0A023DFE8 ?   ?   'expression tag'      -7  39 
3 9B2N LYS C 8   ? UNP A0A023DFE8 ?   ?   'expression tag'      -6  40 
3 9B2N GLU C 9   ? UNP A0A023DFE8 ?   ?   'expression tag'      -5  41 
3 9B2N ASN C 10  ? UNP A0A023DFE8 ?   ?   'expression tag'      -4  42 
3 9B2N LEU C 11  ? UNP A0A023DFE8 ?   ?   'expression tag'      -3  43 
3 9B2N TYR C 12  ? UNP A0A023DFE8 ?   ?   'expression tag'      -2  44 
3 9B2N PHE C 13  ? UNP A0A023DFE8 ?   ?   'expression tag'      -1  45 
3 9B2N GLN C 14  ? UNP A0A023DFE8 ?   ?   'expression tag'      0   46 
3 9B2N SER C 15  ? UNP A0A023DFE8 ?   ?   'expression tag'      1   47 
3 9B2N ASN C 136 ? UNP A0A023DFE8 ASP 121 'engineered mutation' 122 48 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3890  ? 
1 MORE         -104  ? 
1 'SSA (A^2)'  23030 ? 
2 'ABSA (A^2)' 6240  ? 
2 MORE         -198  ? 
2 'SSA (A^2)'  23770 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,D,E,F,G,H,Y               
1 3   C,U,V,W,X,AA                
2 1,2 B,I,J,K,L,M,N,O,P,Q,R,S,T,Z 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z             1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000 0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_656 -x+1,y,-z+1       -1.0000000000 0.0000000000 0.0000000000 111.9044284232 0.0000000000 
1.0000000000 0.0000000000 0.0000000000  0.0000000000 0.0000000000 -1.0000000000 70.8011383193 
3 'crystal symmetry operation' 4_556 -x+1/2,y+1/2,-z+1 -1.0000000000 0.0000000000 0.0000000000 38.7244284232  0.0000000000 
1.0000000000 0.0000000000 54.5400000000 0.0000000000 0.0000000000 -1.0000000000 70.8011383193 
# 
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 LYS A 38  ? ILE A 42  ? LYS A 24  ILE A 28  1 ? 5  
HELX_P HELX_P2  AA2 ALA A 94  ? PHE A 101 ? ALA A 80  PHE A 87  1 ? 8  
HELX_P HELX_P3  AA3 THR A 106 ? CYS A 109 ? THR A 92  CYS A 95  5 ? 4  
HELX_P HELX_P4  AA4 TYR A 110 ? LEU A 118 ? TYR A 96  LEU A 104 1 ? 9  
HELX_P HELX_P5  AA5 ARG A 121 ? GLU A 123 ? ARG A 107 GLU A 109 5 ? 3  
HELX_P HELX_P6  AA6 CYS A 140 ? PHE A 144 ? CYS A 126 PHE A 130 5 ? 5  
HELX_P HELX_P7  AA7 GLU A 153 ? ARG A 165 ? GLU A 139 ARG A 151 1 ? 13 
HELX_P HELX_P8  AA8 ILE A 173 ? ASN A 183 ? ILE A 159 ASN A 169 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 234 ? ILE A 236 ? ASP A 220 ILE A 222 5 ? 3  
HELX_P HELX_P10 AB1 THR A 238 ? GLY A 243 ? THR A 224 GLY A 229 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 254 ? LYS A 273 ? ASP A 240 LYS A 259 1 ? 20 
HELX_P HELX_P12 AB3 ASP A 281 ? PHE A 288 ? ASP A 267 PHE A 274 1 ? 8  
HELX_P HELX_P13 AB4 LYS B 38  ? ILE B 42  ? LYS B 24  ILE B 28  1 ? 5  
HELX_P HELX_P14 AB5 ALA B 94  ? PHE B 101 ? ALA B 80  PHE B 87  1 ? 8  
HELX_P HELX_P15 AB6 THR B 106 ? CYS B 109 ? THR B 92  CYS B 95  5 ? 4  
HELX_P HELX_P16 AB7 TYR B 110 ? GLN B 117 ? TYR B 96  GLN B 103 1 ? 8  
HELX_P HELX_P17 AB8 ARG B 121 ? GLU B 123 ? ARG B 107 GLU B 109 5 ? 3  
HELX_P HELX_P18 AB9 CYS B 140 ? PHE B 144 ? CYS B 126 PHE B 130 5 ? 5  
HELX_P HELX_P19 AC1 GLU B 153 ? ARG B 165 ? GLU B 139 ARG B 151 1 ? 13 
HELX_P HELX_P20 AC2 ILE B 173 ? ASN B 183 ? ILE B 159 ASN B 169 1 ? 11 
HELX_P HELX_P21 AC3 ASP B 234 ? ILE B 236 ? ASP B 220 ILE B 222 5 ? 3  
HELX_P HELX_P22 AC4 THR B 238 ? GLY B 243 ? THR B 224 GLY B 229 1 ? 6  
HELX_P HELX_P23 AC5 ASP B 254 ? LYS B 273 ? ASP B 240 LYS B 259 1 ? 20 
HELX_P HELX_P24 AC6 ASP B 281 ? PHE B 288 ? ASP B 267 PHE B 274 1 ? 8  
HELX_P HELX_P25 AC7 LYS C 38  ? ILE C 42  ? LYS C 24  ILE C 28  1 ? 5  
HELX_P HELX_P26 AC8 ALA C 94  ? PHE C 101 ? ALA C 80  PHE C 87  1 ? 8  
HELX_P HELX_P27 AC9 THR C 106 ? CYS C 109 ? THR C 92  CYS C 95  5 ? 4  
HELX_P HELX_P28 AD1 TYR C 110 ? GLN C 117 ? TYR C 96  GLN C 103 1 ? 8  
HELX_P HELX_P29 AD2 ARG C 121 ? GLU C 123 ? ARG C 107 GLU C 109 5 ? 3  
HELX_P HELX_P30 AD3 CYS C 140 ? PHE C 144 ? CYS C 126 PHE C 130 5 ? 5  
HELX_P HELX_P31 AD4 GLU C 153 ? ARG C 165 ? GLU C 139 ARG C 151 1 ? 13 
HELX_P HELX_P32 AD5 ILE C 173 ? ASN C 183 ? ILE C 159 ASN C 169 1 ? 11 
HELX_P HELX_P33 AD6 ASP C 234 ? ILE C 236 ? ASP C 220 ILE C 222 5 ? 3  
HELX_P HELX_P34 AD7 THR C 238 ? GLY C 243 ? THR C 224 GLY C 229 1 ? 6  
HELX_P HELX_P35 AD8 ASP C 254 ? LYS C 273 ? ASP C 240 LYS C 259 1 ? 20 
HELX_P HELX_P36 AD9 ASP C 281 ? PHE C 288 ? ASP C 267 PHE C 274 1 ? 8  
# 
_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 
metalc1  metalc ? ? A HIS 132 NE2 ? ? ? 1_555 D  CO  . CO ? ? A HIS 118 A CO  301 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc2  metalc ? ? A HIS 134 ND1 ? ? ? 1_555 D  CO  . CO ? ? A HIS 120 A CO  301 1_555 ? ? ? ? ? ? ? 2.213 ? ? 
metalc3  metalc ? ? A HIS 212 NE2 ? ? ? 1_555 D  CO  . CO ? ? A HIS 198 A CO  301 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc4  metalc ? ? A ASP 234 OD2 ? ? ? 1_555 D  CO  . CO ? ? A ASP 220 A CO  301 1_555 ? ? ? ? ? ? ? 2.160 ? ? 
metalc5  metalc ? ? D CO  .   CO  ? ? ? 1_555 Y  HOH . O  ? ? A CO  301 A HOH 412 1_555 ? ? ? ? ? ? ? 2.246 ? ? 
metalc6  metalc ? ? D CO  .   CO  ? ? ? 1_555 Y  HOH . O  ? ? A CO  301 A HOH 413 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc7  metalc ? ? B HIS 132 NE2 ? ? ? 1_555 I  CO  . CO ? ? B HIS 118 B CO  301 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc8  metalc ? ? B HIS 134 ND1 ? ? ? 1_555 I  CO  . CO ? ? B HIS 120 B CO  301 1_555 ? ? ? ? ? ? ? 2.178 ? ? 
metalc9  metalc ? ? B HIS 212 NE2 ? ? ? 1_555 I  CO  . CO ? ? B HIS 198 B CO  301 1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc10 metalc ? ? B ASP 234 OD2 ? ? ? 1_555 I  CO  . CO ? ? B ASP 220 B CO  301 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc11 metalc ? ? I CO  .   CO  ? ? ? 1_555 Z  HOH . O  ? ? B CO  301 B HOH 497 1_555 ? ? ? ? ? ? ? 2.206 ? ? 
metalc12 metalc ? ? I CO  .   CO  ? ? ? 1_555 Z  HOH . O  ? ? B CO  301 B HOH 499 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc13 metalc ? ? C HIS 132 NE2 ? ? ? 1_555 U  CO  . CO ? ? C HIS 118 C CO  301 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc14 metalc ? ? C HIS 134 ND1 ? ? ? 1_555 U  CO  . CO ? ? C HIS 120 C CO  301 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc15 metalc ? ? C HIS 212 NE2 ? ? ? 1_555 U  CO  . CO ? ? C HIS 198 C CO  301 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc16 metalc ? ? C ASP 234 OD2 ? ? ? 1_555 U  CO  . CO ? ? C ASP 220 C CO  301 1_555 ? ? ? ? ? ? ? 2.188 ? ? 
metalc17 metalc ? ? U CO  .   CO  ? ? ? 1_555 AA HOH . O  ? ? C CO  301 C HOH 450 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc18 metalc ? ? U CO  .   CO  ? ? ? 1_555 AA HOH . O  ? ? C CO  301 C HOH 504 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A  HIS 132 ? A HIS 118 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 ND1 ? A  HIS 134 ? A HIS 120 ? 1_555 87.2  ? 
2  NE2 ? A  HIS 132 ? A HIS 118 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 NE2 ? A  HIS 212 ? A HIS 198 ? 1_555 102.3 ? 
3  ND1 ? A  HIS 134 ? A HIS 120 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 NE2 ? A  HIS 212 ? A HIS 198 ? 1_555 95.1  ? 
4  NE2 ? A  HIS 132 ? A HIS 118 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 OD2 ? A  ASP 234 ? A ASP 220 ? 1_555 91.7  ? 
5  ND1 ? A  HIS 134 ? A HIS 120 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 OD2 ? A  ASP 234 ? A ASP 220 ? 1_555 165.1 ? 
6  NE2 ? A  HIS 212 ? A HIS 198 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 OD2 ? A  ASP 234 ? A ASP 220 ? 1_555 99.7  ? 
7  NE2 ? A  HIS 132 ? A HIS 118 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 412 ? 1_555 172.4 ? 
8  ND1 ? A  HIS 134 ? A HIS 120 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 412 ? 1_555 98.6  ? 
9  NE2 ? A  HIS 212 ? A HIS 198 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 412 ? 1_555 82.1  ? 
10 OD2 ? A  ASP 234 ? A ASP 220 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 412 ? 1_555 81.4  ? 
11 NE2 ? A  HIS 132 ? A HIS 118 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 413 ? 1_555 113.3 ? 
12 ND1 ? A  HIS 134 ? A HIS 120 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 413 ? 1_555 91.5  ? 
13 NE2 ? A  HIS 212 ? A HIS 198 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 413 ? 1_555 144.1 ? 
14 OD2 ? A  ASP 234 ? A ASP 220 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 413 ? 1_555 75.3  ? 
15 O   ? Y  HOH .   ? A HOH 412 ? 1_555 CO ? D CO . ? A CO 301 ? 1_555 O   ? Y  HOH .   ? A HOH 413 ? 1_555 61.9  ? 
16 NE2 ? B  HIS 132 ? B HIS 118 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 ND1 ? B  HIS 134 ? B HIS 120 ? 1_555 90.3  ? 
17 NE2 ? B  HIS 132 ? B HIS 118 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 NE2 ? B  HIS 212 ? B HIS 198 ? 1_555 103.6 ? 
18 ND1 ? B  HIS 134 ? B HIS 120 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 NE2 ? B  HIS 212 ? B HIS 198 ? 1_555 90.5  ? 
19 NE2 ? B  HIS 132 ? B HIS 118 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 OD2 ? B  ASP 234 ? B ASP 220 ? 1_555 86.1  ? 
20 ND1 ? B  HIS 134 ? B HIS 120 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 OD2 ? B  ASP 234 ? B ASP 220 ? 1_555 167.5 ? 
21 NE2 ? B  HIS 212 ? B HIS 198 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 OD2 ? B  ASP 234 ? B ASP 220 ? 1_555 101.9 ? 
22 NE2 ? B  HIS 132 ? B HIS 118 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 497 ? 1_555 169.1 ? 
23 ND1 ? B  HIS 134 ? B HIS 120 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 497 ? 1_555 91.7  ? 
24 NE2 ? B  HIS 212 ? B HIS 198 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 497 ? 1_555 87.1  ? 
25 OD2 ? B  ASP 234 ? B ASP 220 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 497 ? 1_555 89.7  ? 
26 NE2 ? B  HIS 132 ? B HIS 118 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 499 ? 1_555 108.3 ? 
27 ND1 ? B  HIS 134 ? B HIS 120 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 499 ? 1_555 83.7  ? 
28 NE2 ? B  HIS 212 ? B HIS 198 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 499 ? 1_555 147.6 ? 
29 OD2 ? B  ASP 234 ? B ASP 220 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 499 ? 1_555 86.1  ? 
30 O   ? Z  HOH .   ? B HOH 497 ? 1_555 CO ? I CO . ? B CO 301 ? 1_555 O   ? Z  HOH .   ? B HOH 499 ? 1_555 61.4  ? 
31 NE2 ? C  HIS 132 ? C HIS 118 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 ND1 ? C  HIS 134 ? C HIS 120 ? 1_555 88.2  ? 
32 NE2 ? C  HIS 132 ? C HIS 118 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 NE2 ? C  HIS 212 ? C HIS 198 ? 1_555 102.9 ? 
33 ND1 ? C  HIS 134 ? C HIS 120 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 NE2 ? C  HIS 212 ? C HIS 198 ? 1_555 92.7  ? 
34 NE2 ? C  HIS 132 ? C HIS 118 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 OD2 ? C  ASP 234 ? C ASP 220 ? 1_555 91.0  ? 
35 ND1 ? C  HIS 134 ? C HIS 120 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 OD2 ? C  ASP 234 ? C ASP 220 ? 1_555 166.9 ? 
36 NE2 ? C  HIS 212 ? C HIS 198 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 OD2 ? C  ASP 234 ? C ASP 220 ? 1_555 100.2 ? 
37 NE2 ? C  HIS 132 ? C HIS 118 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 450 ? 1_555 174.3 ? 
38 ND1 ? C  HIS 134 ? C HIS 120 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 450 ? 1_555 93.9  ? 
39 NE2 ? C  HIS 212 ? C HIS 198 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 450 ? 1_555 82.4  ? 
40 OD2 ? C  ASP 234 ? C ASP 220 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 450 ? 1_555 85.8  ? 
41 NE2 ? C  HIS 132 ? C HIS 118 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 504 ? 1_555 119.5 ? 
42 ND1 ? C  HIS 134 ? C HIS 120 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 504 ? 1_555 85.9  ? 
43 NE2 ? C  HIS 212 ? C HIS 198 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 504 ? 1_555 137.5 ? 
44 OD2 ? C  ASP 234 ? C ASP 220 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 504 ? 1_555 83.1  ? 
45 O   ? AA HOH .   ? C HOH 450 ? 1_555 CO ? U CO . ? C CO 301 ? 1_555 O   ? AA HOH .   ? C HOH 504 ? 1_555 55.4  ? 
# 
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 GLY 243 A . ? GLY 229 A PRO 244 A ? PRO 230 A 1 6.91  
2 PRO 244 A . ? PRO 230 A PRO 245 A ? PRO 231 A 1 -1.10 
3 GLY 243 B . ? GLY 229 B PRO 244 B ? PRO 230 B 1 4.16  
4 PRO 244 B . ? PRO 230 B PRO 245 B ? PRO 231 B 1 -6.05 
5 GLY 243 C . ? GLY 229 C PRO 244 C ? PRO 230 C 1 -0.64 
6 PRO 244 C . ? PRO 230 C PRO 245 C ? PRO 231 C 1 -1.50 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
AA5 ? 7 ? 
AA6 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? 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 TRP A 103 ? THR A 104 ? TRP A 89  THR A 90  
AA1 2 LYS A 25  ? ASP A 37  ? LYS A 11  ASP A 23  
AA1 3 PHE A 59  ? ASP A 70  ? PHE A 45  ASP A 56  
AA1 4 LYS A 75  ? PHE A 78  ? LYS A 61  PHE A 64  
AA1 5 ILE A 125 ? VAL A 129 ? ILE A 111 VAL A 115 
AA1 6 THR A 148 ? HIS A 152 ? THR A 134 HIS A 138 
AA1 7 GLN A 186 ? VAL A 190 ? GLN A 172 VAL A 176 
AA2 1 ILE A 197 ? ALA A 200 ? ILE A 183 ALA A 186 
AA2 2 VAL A 203 ? GLY A 209 ? VAL A 189 GLY A 195 
AA2 3 MET A 216 ? LEU A 223 ? MET A 202 LEU A 209 
AA2 4 GLY A 227 ? SER A 233 ? GLY A 213 SER A 219 
AA2 5 SER A 274 ? PHE A 278 ? SER A 260 PHE A 264 
AA3 1 TRP B 103 ? THR B 104 ? TRP B 89  THR B 90  
AA3 2 LYS B 25  ? ASP B 37  ? LYS B 11  ASP B 23  
AA3 3 PHE B 59  ? HIS B 71  ? PHE B 45  HIS B 57  
AA3 4 GLY B 74  ? PHE B 78  ? GLY B 60  PHE B 64  
AA3 5 ILE B 125 ? VAL B 129 ? ILE B 111 VAL B 115 
AA3 6 THR B 148 ? HIS B 152 ? THR B 134 HIS B 138 
AA3 7 GLN B 186 ? VAL B 190 ? GLN B 172 VAL B 176 
AA4 1 ILE B 197 ? ALA B 200 ? ILE B 183 ALA B 186 
AA4 2 VAL B 203 ? GLY B 209 ? VAL B 189 GLY B 195 
AA4 3 MET B 216 ? LEU B 223 ? MET B 202 LEU B 209 
AA4 4 GLY B 227 ? SER B 233 ? GLY B 213 SER B 219 
AA4 5 SER B 274 ? PHE B 278 ? SER B 260 PHE B 264 
AA5 1 TRP C 103 ? THR C 104 ? TRP C 89  THR C 90  
AA5 2 LYS C 25  ? ASP C 37  ? LYS C 11  ASP C 23  
AA5 3 PHE C 59  ? ASP C 70  ? PHE C 45  ASP C 56  
AA5 4 LYS C 75  ? PHE C 78  ? LYS C 61  PHE C 64  
AA5 5 ILE C 125 ? VAL C 129 ? ILE C 111 VAL C 115 
AA5 6 THR C 148 ? HIS C 152 ? THR C 134 HIS C 138 
AA5 7 GLN C 186 ? VAL C 190 ? GLN C 172 VAL C 176 
AA6 1 ILE C 197 ? ALA C 200 ? ILE C 183 ALA C 186 
AA6 2 VAL C 203 ? GLY C 209 ? VAL C 189 GLY C 195 
AA6 3 MET C 216 ? LEU C 223 ? MET C 202 LEU C 209 
AA6 4 GLY C 227 ? SER C 233 ? GLY C 213 SER C 219 
AA6 5 SER C 274 ? PHE C 278 ? SER C 260 PHE C 264 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O THR A 104 ? O THR A 90  N ARG A 33  ? N ARG A 19  
AA1 2 3 N LYS A 25  ? N LYS A 11  O ASP A 70  ? O ASP A 56  
AA1 3 4 N ILE A 69  ? N ILE A 55  O ILE A 76  ? O ILE A 62  
AA1 4 5 N LEU A 77  ? N LEU A 63  O VAL A 129 ? O VAL A 115 
AA1 5 6 N VAL A 128 ? N VAL A 114 O ILE A 150 ? O ILE A 136 
AA1 6 7 N ILE A 149 ? N ILE A 135 O GLN A 186 ? O GLN A 172 
AA2 1 2 N ALA A 200 ? N ALA A 186 O VAL A 203 ? O VAL A 189 
AA2 2 3 N LYS A 204 ? N LYS A 190 O HIS A 220 ? O HIS A 206 
AA2 3 4 N LEU A 223 ? N LEU A 209 O GLY A 227 ? O GLY A 213 
AA2 4 5 N ILE A 230 ? N ILE A 216 O TRP A 277 ? O TRP A 263 
AA3 1 2 O THR B 104 ? O THR B 90  N ARG B 33  ? N ARG B 19  
AA3 2 3 N TYR B 27  ? N TYR B 13  O LEU B 68  ? O LEU B 54  
AA3 3 4 N ILE B 69  ? N ILE B 55  O ILE B 76  ? O ILE B 62  
AA3 4 5 N LEU B 77  ? N LEU B 63  O VAL B 129 ? O VAL B 115 
AA3 5 6 N VAL B 128 ? N VAL B 114 O ILE B 150 ? O ILE B 136 
AA3 6 7 N ILE B 149 ? N ILE B 135 O GLN B 186 ? O GLN B 172 
AA4 1 2 N ALA B 200 ? N ALA B 186 O VAL B 203 ? O VAL B 189 
AA4 2 3 N LEU B 206 ? N LEU B 192 O GLY B 218 ? O GLY B 204 
AA4 3 4 N VAL B 221 ? N VAL B 207 O ILE B 229 ? O ILE B 215 
AA4 4 5 N ILE B 230 ? N ILE B 216 O TRP B 277 ? O TRP B 263 
AA5 1 2 O THR C 104 ? O THR C 90  N ARG C 33  ? N ARG C 19  
AA5 2 3 N TYR C 27  ? N TYR C 13  O LEU C 68  ? O LEU C 54  
AA5 3 4 N ILE C 69  ? N ILE C 55  O ILE C 76  ? O ILE C 62  
AA5 4 5 N LEU C 77  ? N LEU C 63  O VAL C 129 ? O VAL C 115 
AA5 5 6 N VAL C 128 ? N VAL C 114 O ILE C 150 ? O ILE C 136 
AA5 6 7 N ILE C 149 ? N ILE C 135 O GLN C 186 ? O GLN C 172 
AA6 1 2 N ILE C 197 ? N ILE C 183 O VAL C 205 ? O VAL C 191 
AA6 2 3 N GLY C 209 ? N GLY C 195 O MET C 216 ? O MET C 202 
AA6 3 4 N VAL C 221 ? N VAL C 207 O ILE C 229 ? O ILE C 215 
AA6 4 5 N ILE C 230 ? N ILE C 216 O TRP C 277 ? O TRP C 263 
# 
_pdbx_entry_details.entry_id                   9B2N 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 491 ? ? O A HOH 528 ? ? 1.61 
2 1 O A HOH 515 ? ? O A HOH 533 ? ? 1.71 
3 1 O C HOH 504 ? ? O C HOH 557 ? ? 1.80 
4 1 O A HOH 528 ? ? O A HOH 530 ? ? 2.04 
5 1 O B HOH 473 ? ? O B HOH 502 ? ? 2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 CG B GLN 103 ? ? 1_555 NH1 C ARG 9 ? ? 2_555 1.69 
2 1 CB B GLN 103 ? ? 1_555 NH1 C ARG 9 ? ? 2_555 1.89 
3 1 CA B GLN 103 ? ? 1_555 NH1 C ARG 9 ? ? 2_555 2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 65  ? ? 70.27   164.48  
2  1 SER A 67  ? ? 59.66   -150.75 
3  1 PRO A 108 ? ? -39.92  -39.39  
4  1 HIS A 123 ? ? -132.13 -30.40  
5  1 PHE A 130 ? ? -100.44 77.51   
6  1 GLU A 211 ? ? -91.25  -61.34  
7  1 SER A 219 ? ? 49.22   -138.84 
8  1 HIS A 266 ? ? -154.95 62.84   
9  1 HIS A 266 ? ? -158.81 70.38   
10 1 ASP B 65  ? ? 72.64   165.71  
11 1 THR B 66  ? ? -143.47 12.52   
12 1 SER B 67  ? ? 56.47   -146.45 
13 1 ASN B 71  ? ? -104.62 43.89   
14 1 PHE B 130 ? ? -101.22 74.98   
15 1 SER B 219 ? ? 48.92   -137.00 
16 1 HIS B 266 ? ? -157.55 53.90   
17 1 HIS B 266 ? ? -161.98 62.90   
18 1 ARG C 9   ? ? -151.29 66.10   
19 1 ASN C 38  ? ? -154.63 60.16   
20 1 ASP C 65  ? ? 71.82   164.89  
21 1 SER C 67  ? ? 67.60   -149.67 
22 1 ASN C 71  ? ? -104.78 43.38   
23 1 SER C 219 ? ? 51.27   -138.93 
24 1 HIS C 266 ? A -153.90 55.58   
25 1 HIS C 266 ? B -152.31 69.82   
# 
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 B HOH 461 ? Z HOH . 
2 1 B HOH 562 ? Z HOH . 
# 
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 TRP -13 ? A TRP 1  
2  1 Y 1 A SER -12 ? A SER 2  
3  1 Y 1 A HIS -11 ? A HIS 3  
4  1 Y 1 A PRO -10 ? A PRO 4  
5  1 Y 1 A GLN -9  ? A GLN 5  
6  1 Y 1 A PHE -8  ? A PHE 6  
7  1 Y 1 A GLU -7  ? A GLU 7  
8  1 Y 1 A LYS -6  ? A LYS 8  
9  1 Y 1 A GLU -5  ? A GLU 9  
10 1 Y 1 A ASN -4  ? A ASN 10 
11 1 Y 1 A LEU -3  ? A LEU 11 
12 1 Y 1 A TYR -2  ? A TYR 12 
13 1 Y 1 A PHE -1  ? A PHE 13 
14 1 Y 1 A GLN 0   ? A GLN 14 
15 1 Y 1 A SER 1   ? A SER 15 
16 1 Y 1 A MET 2   ? A MET 16 
17 1 Y 1 A ALA 3   ? A ALA 17 
18 1 Y 1 A ASN 4   ? A ASN 18 
19 1 Y 1 A VAL 5   ? A VAL 19 
20 1 Y 1 A ILE 6   ? A ILE 20 
21 1 Y 1 A LYS 7   ? A LYS 21 
22 1 Y 1 A ALA 8   ? A ALA 22 
23 1 Y 1 B TRP -13 ? B TRP 1  
24 1 Y 1 B SER -12 ? B SER 2  
25 1 Y 1 B HIS -11 ? B HIS 3  
26 1 Y 1 B PRO -10 ? B PRO 4  
27 1 Y 1 B GLN -9  ? B GLN 5  
28 1 Y 1 B PHE -8  ? B PHE 6  
29 1 Y 1 B GLU -7  ? B GLU 7  
30 1 Y 1 B LYS -6  ? B LYS 8  
31 1 Y 1 B GLU -5  ? B GLU 9  
32 1 Y 1 B ASN -4  ? B ASN 10 
33 1 Y 1 B LEU -3  ? B LEU 11 
34 1 Y 1 B TYR -2  ? B TYR 12 
35 1 Y 1 B PHE -1  ? B PHE 13 
36 1 Y 1 B GLN 0   ? B GLN 14 
37 1 Y 1 B SER 1   ? B SER 15 
38 1 Y 1 B MET 2   ? B MET 16 
39 1 Y 1 B ALA 3   ? B ALA 17 
40 1 Y 1 B ASN 4   ? B ASN 18 
41 1 Y 1 B VAL 5   ? B VAL 19 
42 1 Y 1 B ILE 6   ? B ILE 20 
43 1 Y 1 B LYS 7   ? B LYS 21 
44 1 Y 1 C TRP -13 ? C TRP 1  
45 1 Y 1 C SER -12 ? C SER 2  
46 1 Y 1 C HIS -11 ? C HIS 3  
47 1 Y 1 C PRO -10 ? C PRO 4  
48 1 Y 1 C GLN -9  ? C GLN 5  
49 1 Y 1 C PHE -8  ? C PHE 6  
50 1 Y 1 C GLU -7  ? C GLU 7  
51 1 Y 1 C LYS -6  ? C LYS 8  
52 1 Y 1 C GLU -5  ? C GLU 9  
53 1 Y 1 C ASN -4  ? C ASN 10 
54 1 Y 1 C LEU -3  ? C LEU 11 
55 1 Y 1 C TYR -2  ? C TYR 12 
56 1 Y 1 C PHE -1  ? C PHE 13 
57 1 Y 1 C GLN 0   ? C GLN 14 
58 1 Y 1 C SER 1   ? C SER 15 
59 1 Y 1 C MET 2   ? C MET 16 
60 1 Y 1 C ALA 3   ? C ALA 17 
61 1 Y 1 C ASN 4   ? C ASN 18 
62 1 Y 1 C VAL 5   ? C VAL 19 
63 1 Y 1 C ILE 6   ? C ILE 20 
64 1 Y 1 C LYS 7   ? C LYS 21 
# 
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 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
CO  CO   CO N N 81  
CYS N    N  N N 82  
CYS CA   C  N R 83  
CYS C    C  N N 84  
CYS O    O  N N 85  
CYS CB   C  N N 86  
CYS SG   S  N N 87  
CYS OXT  O  N N 88  
CYS H    H  N N 89  
CYS H2   H  N N 90  
CYS HA   H  N N 91  
CYS HB2  H  N N 92  
CYS HB3  H  N N 93  
CYS HG   H  N N 94  
CYS HXT  H  N N 95  
GLN N    N  N N 96  
GLN CA   C  N S 97  
GLN C    C  N N 98  
GLN O    O  N N 99  
GLN CB   C  N N 100 
GLN CG   C  N N 101 
GLN CD   C  N N 102 
GLN OE1  O  N N 103 
GLN NE2  N  N N 104 
GLN OXT  O  N N 105 
GLN H    H  N N 106 
GLN H2   H  N N 107 
GLN HA   H  N N 108 
GLN HB2  H  N N 109 
GLN HB3  H  N N 110 
GLN HG2  H  N N 111 
GLN HG3  H  N N 112 
GLN HE21 H  N N 113 
GLN HE22 H  N N 114 
GLN HXT  H  N N 115 
GLU N    N  N N 116 
GLU CA   C  N S 117 
GLU C    C  N N 118 
GLU O    O  N N 119 
GLU CB   C  N N 120 
GLU CG   C  N N 121 
GLU CD   C  N N 122 
GLU OE1  O  N N 123 
GLU OE2  O  N N 124 
GLU OXT  O  N N 125 
GLU H    H  N N 126 
GLU H2   H  N N 127 
GLU HA   H  N N 128 
GLU HB2  H  N N 129 
GLU HB3  H  N N 130 
GLU HG2  H  N N 131 
GLU HG3  H  N N 132 
GLU HE2  H  N N 133 
GLU HXT  H  N N 134 
GLY N    N  N N 135 
GLY CA   C  N N 136 
GLY C    C  N N 137 
GLY O    O  N N 138 
GLY OXT  O  N N 139 
GLY H    H  N N 140 
GLY H2   H  N N 141 
GLY HA2  H  N N 142 
GLY HA3  H  N N 143 
GLY HXT  H  N N 144 
GOL C1   C  N N 145 
GOL O1   O  N N 146 
GOL C2   C  N N 147 
GOL O2   O  N N 148 
GOL C3   C  N N 149 
GOL O3   O  N N 150 
GOL H11  H  N N 151 
GOL H12  H  N N 152 
GOL HO1  H  N N 153 
GOL H2   H  N N 154 
GOL HO2  H  N N 155 
GOL H31  H  N N 156 
GOL H32  H  N N 157 
GOL HO3  H  N N 158 
HIS N    N  N N 159 
HIS CA   C  N S 160 
HIS C    C  N N 161 
HIS O    O  N N 162 
HIS CB   C  N N 163 
HIS CG   C  Y N 164 
HIS ND1  N  Y N 165 
HIS CD2  C  Y N 166 
HIS CE1  C  Y N 167 
HIS NE2  N  Y N 168 
HIS OXT  O  N N 169 
HIS H    H  N N 170 
HIS H2   H  N N 171 
HIS HA   H  N N 172 
HIS HB2  H  N N 173 
HIS HB3  H  N N 174 
HIS HD1  H  N N 175 
HIS HD2  H  N N 176 
HIS HE1  H  N N 177 
HIS HE2  H  N N 178 
HIS HXT  H  N N 179 
HOH O    O  N N 180 
HOH H1   H  N N 181 
HOH H2   H  N N 182 
ILE N    N  N N 183 
ILE CA   C  N S 184 
ILE C    C  N N 185 
ILE O    O  N N 186 
ILE CB   C  N S 187 
ILE CG1  C  N N 188 
ILE CG2  C  N N 189 
ILE CD1  C  N N 190 
ILE OXT  O  N N 191 
ILE H    H  N N 192 
ILE H2   H  N N 193 
ILE HA   H  N N 194 
ILE HB   H  N N 195 
ILE HG12 H  N N 196 
ILE HG13 H  N N 197 
ILE HG21 H  N N 198 
ILE HG22 H  N N 199 
ILE HG23 H  N N 200 
ILE HD11 H  N N 201 
ILE HD12 H  N N 202 
ILE HD13 H  N N 203 
ILE HXT  H  N N 204 
LEU N    N  N N 205 
LEU CA   C  N S 206 
LEU C    C  N N 207 
LEU O    O  N N 208 
LEU CB   C  N N 209 
LEU CG   C  N N 210 
LEU CD1  C  N N 211 
LEU CD2  C  N N 212 
LEU OXT  O  N N 213 
LEU H    H  N N 214 
LEU H2   H  N N 215 
LEU HA   H  N N 216 
LEU HB2  H  N N 217 
LEU HB3  H  N N 218 
LEU HG   H  N N 219 
LEU HD11 H  N N 220 
LEU HD12 H  N N 221 
LEU HD13 H  N N 222 
LEU HD21 H  N N 223 
LEU HD22 H  N N 224 
LEU HD23 H  N N 225 
LEU HXT  H  N N 226 
LYS N    N  N N 227 
LYS CA   C  N S 228 
LYS C    C  N N 229 
LYS O    O  N N 230 
LYS CB   C  N N 231 
LYS CG   C  N N 232 
LYS CD   C  N N 233 
LYS CE   C  N N 234 
LYS NZ   N  N N 235 
LYS OXT  O  N N 236 
LYS H    H  N N 237 
LYS H2   H  N N 238 
LYS HA   H  N N 239 
LYS HB2  H  N N 240 
LYS HB3  H  N N 241 
LYS HG2  H  N N 242 
LYS HG3  H  N N 243 
LYS HD2  H  N N 244 
LYS HD3  H  N N 245 
LYS HE2  H  N N 246 
LYS HE3  H  N N 247 
LYS HZ1  H  N N 248 
LYS HZ2  H  N N 249 
LYS HZ3  H  N N 250 
LYS HXT  H  N N 251 
MET N    N  N N 252 
MET CA   C  N S 253 
MET C    C  N N 254 
MET O    O  N N 255 
MET CB   C  N N 256 
MET CG   C  N N 257 
MET SD   S  N N 258 
MET CE   C  N N 259 
MET OXT  O  N N 260 
MET H    H  N N 261 
MET H2   H  N N 262 
MET HA   H  N N 263 
MET HB2  H  N N 264 
MET HB3  H  N N 265 
MET HG2  H  N N 266 
MET HG3  H  N N 267 
MET HE1  H  N N 268 
MET HE2  H  N N 269 
MET HE3  H  N N 270 
MET HXT  H  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 
SO4 S    S  N N 326 
SO4 O1   O  N N 327 
SO4 O2   O  N N 328 
SO4 O3   O  N N 329 
SO4 O4   O  N N 330 
THR N    N  N N 331 
THR CA   C  N S 332 
THR C    C  N N 333 
THR O    O  N N 334 
THR CB   C  N R 335 
THR OG1  O  N N 336 
THR CG2  C  N N 337 
THR OXT  O  N N 338 
THR H    H  N N 339 
THR H2   H  N N 340 
THR HA   H  N N 341 
THR HB   H  N N 342 
THR HG1  H  N N 343 
THR HG21 H  N N 344 
THR HG22 H  N N 345 
THR HG23 H  N N 346 
THR HXT  H  N N 347 
TRP N    N  N N 348 
TRP CA   C  N S 349 
TRP C    C  N N 350 
TRP O    O  N N 351 
TRP CB   C  N N 352 
TRP CG   C  Y N 353 
TRP CD1  C  Y N 354 
TRP CD2  C  Y N 355 
TRP NE1  N  Y N 356 
TRP CE2  C  Y N 357 
TRP CE3  C  Y N 358 
TRP CZ2  C  Y N 359 
TRP CZ3  C  Y N 360 
TRP CH2  C  Y N 361 
TRP OXT  O  N N 362 
TRP H    H  N N 363 
TRP H2   H  N N 364 
TRP HA   H  N N 365 
TRP HB2  H  N N 366 
TRP HB3  H  N N 367 
TRP HD1  H  N N 368 
TRP HE1  H  N N 369 
TRP HE3  H  N N 370 
TRP HZ2  H  N N 371 
TRP HZ3  H  N N 372 
TRP HH2  H  N N 373 
TRP HXT  H  N N 374 
TYR N    N  N N 375 
TYR CA   C  N S 376 
TYR C    C  N N 377 
TYR O    O  N N 378 
TYR CB   C  N N 379 
TYR CG   C  Y N 380 
TYR CD1  C  Y N 381 
TYR CD2  C  Y N 382 
TYR CE1  C  Y N 383 
TYR CE2  C  Y N 384 
TYR CZ   C  Y N 385 
TYR OH   O  N N 386 
TYR OXT  O  N N 387 
TYR H    H  N N 388 
TYR H2   H  N N 389 
TYR HA   H  N N 390 
TYR HB2  H  N N 391 
TYR HB3  H  N N 392 
TYR HD1  H  N N 393 
TYR HD2  H  N N 394 
TYR HE1  H  N N 395 
TYR HE2  H  N N 396 
TYR HH   H  N N 397 
TYR HXT  H  N N 398 
VAL N    N  N N 399 
VAL CA   C  N S 400 
VAL C    C  N N 401 
VAL O    O  N N 402 
VAL CB   C  N N 403 
VAL CG1  C  N N 404 
VAL CG2  C  N N 405 
VAL OXT  O  N N 406 
VAL H    H  N N 407 
VAL H2   H  N N 408 
VAL HA   H  N N 409 
VAL HB   H  N N 410 
VAL HG11 H  N N 411 
VAL HG12 H  N N 412 
VAL HG13 H  N N 413 
VAL HG21 H  N N 414 
VAL HG22 H  N N 415 
VAL HG23 H  N N 416 
VAL HXT  H  N N 417 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
GOL C1  O1   sing N N 135 
GOL C1  C2   sing N N 136 
GOL C1  H11  sing N N 137 
GOL C1  H12  sing N N 138 
GOL O1  HO1  sing N N 139 
GOL C2  O2   sing N N 140 
GOL C2  C3   sing N N 141 
GOL C2  H2   sing N N 142 
GOL O2  HO2  sing N N 143 
GOL C3  O3   sing N N 144 
GOL C3  H31  sing N N 145 
GOL C3  H32  sing N N 146 
GOL O3  HO3  sing N N 147 
HIS N   CA   sing N N 148 
HIS N   H    sing N N 149 
HIS N   H2   sing N N 150 
HIS CA  C    sing N N 151 
HIS CA  CB   sing N N 152 
HIS CA  HA   sing N N 153 
HIS C   O    doub N N 154 
HIS C   OXT  sing N N 155 
HIS CB  CG   sing N N 156 
HIS CB  HB2  sing N N 157 
HIS CB  HB3  sing N N 158 
HIS CG  ND1  sing Y N 159 
HIS CG  CD2  doub Y N 160 
HIS ND1 CE1  doub Y N 161 
HIS ND1 HD1  sing N N 162 
HIS CD2 NE2  sing Y N 163 
HIS CD2 HD2  sing N N 164 
HIS CE1 NE2  sing Y N 165 
HIS CE1 HE1  sing N N 166 
HIS NE2 HE2  sing N N 167 
HIS OXT HXT  sing N N 168 
HOH O   H1   sing N N 169 
HOH O   H2   sing N N 170 
ILE N   CA   sing N N 171 
ILE N   H    sing N N 172 
ILE N   H2   sing N N 173 
ILE CA  C    sing N N 174 
ILE CA  CB   sing N N 175 
ILE CA  HA   sing N N 176 
ILE C   O    doub N N 177 
ILE C   OXT  sing N N 178 
ILE CB  CG1  sing N N 179 
ILE CB  CG2  sing N N 180 
ILE CB  HB   sing N N 181 
ILE CG1 CD1  sing N N 182 
ILE CG1 HG12 sing N N 183 
ILE CG1 HG13 sing N N 184 
ILE CG2 HG21 sing N N 185 
ILE CG2 HG22 sing N N 186 
ILE CG2 HG23 sing N N 187 
ILE CD1 HD11 sing N N 188 
ILE CD1 HD12 sing N N 189 
ILE CD1 HD13 sing N N 190 
ILE OXT HXT  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 
SO4 S   O1   doub N N 309 
SO4 S   O2   doub N N 310 
SO4 S   O3   sing N N 311 
SO4 S   O4   sing N N 312 
THR N   CA   sing N N 313 
THR N   H    sing N N 314 
THR N   H2   sing N N 315 
THR CA  C    sing N N 316 
THR CA  CB   sing N N 317 
THR CA  HA   sing N N 318 
THR C   O    doub N N 319 
THR C   OXT  sing N N 320 
THR CB  OG1  sing N N 321 
THR CB  CG2  sing N N 322 
THR CB  HB   sing N N 323 
THR OG1 HG1  sing N N 324 
THR CG2 HG21 sing N N 325 
THR CG2 HG22 sing N N 326 
THR CG2 HG23 sing N N 327 
THR OXT HXT  sing N N 328 
TRP N   CA   sing N N 329 
TRP N   H    sing N N 330 
TRP N   H2   sing N N 331 
TRP CA  C    sing N N 332 
TRP CA  CB   sing N N 333 
TRP CA  HA   sing N N 334 
TRP C   O    doub N N 335 
TRP C   OXT  sing N N 336 
TRP CB  CG   sing N N 337 
TRP CB  HB2  sing N N 338 
TRP CB  HB3  sing N N 339 
TRP CG  CD1  doub Y N 340 
TRP CG  CD2  sing Y N 341 
TRP CD1 NE1  sing Y N 342 
TRP CD1 HD1  sing N N 343 
TRP CD2 CE2  doub Y N 344 
TRP CD2 CE3  sing Y N 345 
TRP NE1 CE2  sing Y N 346 
TRP NE1 HE1  sing N N 347 
TRP CE2 CZ2  sing Y N 348 
TRP CE3 CZ3  doub Y N 349 
TRP CE3 HE3  sing N N 350 
TRP CZ2 CH2  doub Y N 351 
TRP CZ2 HZ2  sing N N 352 
TRP CZ3 CH2  sing Y N 353 
TRP CZ3 HZ3  sing N N 354 
TRP CH2 HH2  sing N N 355 
TRP OXT HXT  sing N N 356 
TYR N   CA   sing N N 357 
TYR N   H    sing N N 358 
TYR N   H2   sing N N 359 
TYR CA  C    sing N N 360 
TYR CA  CB   sing N N 361 
TYR CA  HA   sing N N 362 
TYR C   O    doub N N 363 
TYR C   OXT  sing N N 364 
TYR CB  CG   sing N N 365 
TYR CB  HB2  sing N N 366 
TYR CB  HB3  sing N N 367 
TYR CG  CD1  doub Y N 368 
TYR CG  CD2  sing Y N 369 
TYR CD1 CE1  sing Y N 370 
TYR CD1 HD1  sing N N 371 
TYR CD2 CE2  doub Y N 372 
TYR CD2 HD2  sing N N 373 
TYR CE1 CZ   doub Y N 374 
TYR CE1 HE1  sing N N 375 
TYR CE2 CZ   sing Y N 376 
TYR CE2 HE2  sing N N 377 
TYR CZ  OH   sing N N 378 
TYR OH  HH   sing N N 379 
TYR OXT HXT  sing N N 380 
VAL N   CA   sing N N 381 
VAL N   H    sing N N 382 
VAL N   H2   sing N N 383 
VAL CA  C    sing N N 384 
VAL CA  CB   sing N N 385 
VAL CA  HA   sing N N 386 
VAL C   O    doub N N 387 
VAL C   OXT  sing N N 388 
VAL CB  CG1  sing N N 389 
VAL CB  CG2  sing N N 390 
VAL CB  HB   sing N N 391 
VAL CG1 HG11 sing N N 392 
VAL CG1 HG12 sing N N 393 
VAL CG1 HG13 sing N N 394 
VAL CG2 HG21 sing N N 395 
VAL CG2 HG22 sing N N 396 
VAL CG2 HG23 sing N N 397 
VAL OXT HXT  sing N N 398 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM133487 
_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   6n9i 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9B2N 
_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]   0.006832 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003325 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009168 
_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]   0.014124 
_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  
CO 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG A  1 23  ? 14.476  14.822  26.642  1.00 71.09  ? 9   ARG A N   1 
ATOM   2    C  CA  . ARG A  1 23  ? 14.492  16.249  27.063  1.00 61.75  ? 9   ARG A CA  1 
ATOM   3    C  C   . ARG A  1 23  ? 14.541  16.316  28.589  1.00 52.46  ? 9   ARG A C   1 
ATOM   4    O  O   . ARG A  1 23  ? 13.567  15.984  29.261  1.00 47.80  ? 9   ARG A O   1 
ATOM   5    C  CB  . ARG A  1 23  ? 13.284  16.994  26.481  1.00 58.79  ? 9   ARG A CB  1 
ATOM   6    C  CG  . ARG A  1 23  ? 13.204  16.907  24.964  1.00 61.98  ? 9   ARG A CG  1 
ATOM   7    C  CD  . ARG A  1 23  ? 12.860  18.239  24.317  1.00 67.27  ? 9   ARG A CD  1 
ATOM   8    N  NE  . ARG A  1 23  ? 13.341  18.282  22.931  1.00 71.99  ? 9   ARG A NE  1 
ATOM   9    C  CZ  . ARG A  1 23  ? 13.520  19.387  22.219  1.00 74.81  ? 9   ARG A CZ  1 
ATOM   10   N  NH1 . ARG A  1 23  ? 14.028  19.311  21.001  1.00 80.05  ? 9   ARG A NH1 1 
ATOM   11   N  NH2 . ARG A  1 23  ? 13.220  20.567  22.734  1.00 73.67  ? 9   ARG A NH2 1 
ATOM   12   N  N   . PRO A  1 24  ? 15.683  16.742  29.177  1.00 49.61  ? 10  PRO A N   1 
ATOM   13   C  CA  . PRO A  1 24  ? 15.850  16.739  30.633  1.00 44.74  ? 10  PRO A CA  1 
ATOM   14   C  C   . PRO A  1 24  ? 14.981  17.763  31.358  1.00 41.87  ? 10  PRO A C   1 
ATOM   15   O  O   . PRO A  1 24  ? 14.567  18.762  30.773  1.00 42.19  ? 10  PRO A O   1 
ATOM   16   C  CB  . PRO A  1 24  ? 17.354  17.040  30.803  1.00 45.86  ? 10  PRO A CB  1 
ATOM   17   C  CG  . PRO A  1 24  ? 17.712  17.854  29.578  1.00 47.49  ? 10  PRO A CG  1 
ATOM   18   C  CD  . PRO A  1 24  ? 16.870  17.249  28.467  1.00 47.72  ? 10  PRO A CD  1 
ATOM   19   N  N   . LYS A  1 25  ? 14.716  17.496  32.643  1.00 38.66  ? 11  LYS A N   1 
ATOM   20   C  CA  . LYS A  1 25  ? 14.047  18.442  33.523  1.00 37.74  ? 11  LYS A CA  1 
ATOM   21   C  C   . LYS A  1 25  ? 14.937  18.688  34.742  1.00 32.76  ? 11  LYS A C   1 
ATOM   22   O  O   . LYS A  1 25  ? 15.417  17.740  35.359  1.00 33.96  ? 11  LYS A O   1 
ATOM   23   C  CB  . LYS A  1 25  ? 12.669  17.912  33.949  1.00 35.57  ? 11  LYS A CB  1 
ATOM   24   C  CG  . LYS A  1 25  ? 11.632  17.752  32.837  1.00 39.80  ? 11  LYS A CG  1 
ATOM   25   C  CD  . LYS A  1 25  ? 10.386  16.983  33.273  1.00 45.53  ? 11  LYS A CD  1 
ATOM   26   C  CE  . LYS A  1 25  ? 9.452   16.625  32.151  1.00 47.80  ? 11  LYS A CE  1 
ATOM   27   N  NZ  . LYS A  1 25  ? 8.440   17.657  31.903  1.00 52.93  ? 11  LYS A NZ  1 
ATOM   28   N  N   . LEU A  1 26  ? 15.145  19.966  35.085  1.00 33.25  ? 12  LEU A N   1 
ATOM   29   C  CA  . LEU A  1 26  ? 16.053  20.344  36.158  1.00 34.86  ? 12  LEU A CA  1 
ATOM   30   C  C   . LEU A  1 26  ? 15.263  20.971  37.306  1.00 32.01  ? 12  LEU A C   1 
ATOM   31   O  O   . LEU A  1 26  ? 14.464  21.880  37.090  1.00 29.64  ? 12  LEU A O   1 
ATOM   32   C  CB  . LEU A  1 26  ? 17.121  21.291  35.604  1.00 34.82  ? 12  LEU A CB  1 
ATOM   33   C  CG  . LEU A  1 26  ? 18.213  21.737  36.583  1.00 32.67  ? 12  LEU A CG  1 
ATOM   34   C  CD1 . LEU A  1 26  ? 19.525  22.003  35.857  1.00 31.49  ? 12  LEU A CD1 1 
ATOM   35   C  CD2 . LEU A  1 26  ? 17.780  22.975  37.351  1.00 32.15  ? 12  LEU A CD2 1 
ATOM   36   N  N   . TYR A  1 27  ? 15.508  20.476  38.528  1.00 33.32  ? 13  TYR A N   1 
ATOM   37   C  CA  . TYR A  1 27  ? 14.784  20.913  39.713  1.00 34.14  ? 13  TYR A CA  1 
ATOM   38   C  C   . TYR A  1 27  ? 15.755  21.554  40.706  1.00 37.51  ? 13  TYR A C   1 
ATOM   39   O  O   . TYR A  1 27  ? 16.845  21.034  40.939  1.00 36.45  ? 13  TYR A O   1 
ATOM   40   C  CB  . TYR A  1 27  ? 14.059  19.733  40.375  1.00 34.73  ? 13  TYR A CB  1 
ATOM   41   C  CG  . TYR A  1 27  ? 13.101  18.963  39.474  1.00 38.87  ? 13  TYR A CG  1 
ATOM   42   C  CD1 . TYR A  1 27  ? 13.577  18.042  38.547  1.00 42.55  ? 13  TYR A CD1 1 
ATOM   43   C  CD2 . TYR A  1 27  ? 11.723  19.138  39.562  1.00 38.10  ? 13  TYR A CD2 1 
ATOM   44   C  CE1 . TYR A  1 27  ? 12.714  17.333  37.726  1.00 45.07  ? 13  TYR A CE1 1 
ATOM   45   C  CE2 . TYR A  1 27  ? 10.850  18.435  38.747  1.00 35.80  ? 13  TYR A CE2 1 
ATOM   46   C  CZ  . TYR A  1 27  ? 11.348  17.529  37.827  1.00 39.72  ? 13  TYR A CZ  1 
ATOM   47   O  OH  . TYR A  1 27  ? 10.498  16.830  37.019  1.00 43.31  ? 13  TYR A OH  1 
ATOM   48   N  N   . VAL A  1 28  ? 15.335  22.686  41.287  1.00 30.98  ? 14  VAL A N   1 
ATOM   49   C  CA  . VAL A  1 28  ? 16.053  23.327  42.378  1.00 32.88  ? 14  VAL A CA  1 
ATOM   50   C  C   . VAL A  1 28  ? 15.355  22.964  43.689  1.00 37.92  ? 14  VAL A C   1 
ATOM   51   O  O   . VAL A  1 28  ? 14.172  23.252  43.862  1.00 37.10  ? 14  VAL A O   1 
ATOM   52   C  CB  . VAL A  1 28  ? 16.123  24.858  42.197  1.00 33.58  ? 14  VAL A CB  1 
ATOM   53   C  CG1 . VAL A  1 28  ? 16.802  25.538  43.380  1.00 36.75  ? 14  VAL A CG1 1 
ATOM   54   C  CG2 . VAL A  1 28  ? 16.803  25.257  40.892  1.00 37.85  ? 14  VAL A CG2 1 
ATOM   55   N  N   . MET A  1 29  ? 16.102  22.343  44.612  1.00 34.29  ? 15  MET A N   1 
ATOM   56   C  CA  . MET A  1 29  ? 15.537  21.840  45.855  1.00 34.59  ? 15  MET A CA  1 
ATOM   57   C  C   . MET A  1 29  ? 16.037  22.679  47.032  1.00 40.30  ? 15  MET A C   1 
ATOM   58   O  O   . MET A  1 29  ? 17.242  22.809  47.244  1.00 36.63  ? 15  MET A O   1 
ATOM   59   C  CB  . MET A  1 29  ? 15.899  20.363  46.053  1.00 34.03  ? 15  MET A CB  1 
ATOM   60   C  CG  . MET A  1 29  ? 15.105  19.413  45.168  1.00 33.07  ? 15  MET A CG  1 
ATOM   61   S  SD  . MET A  1 29  ? 15.637  17.692  45.287  1.00 35.21  ? 15  MET A SD  1 
ATOM   62   C  CE  . MET A  1 29  ? 17.316  17.804  44.651  1.00 37.18  ? 15  MET A CE  1 
ATOM   63   N  N   . ASP A  1 30  ? 15.086  23.242  47.789  1.00 36.98  ? 16  ASP A N   1 
ATOM   64   C  CA  . ASP A  1 30  ? 15.379  24.102  48.926  1.00 36.13  ? 16  ASP A CA  1 
ATOM   65   C  C   . ASP A  1 30  ? 15.739  23.235  50.130  1.00 37.72  ? 16  ASP A C   1 
ATOM   66   O  O   . ASP A  1 30  ? 14.911  22.459  50.603  1.00 32.40  ? 16  ASP A O   1 
ATOM   67   C  CB  . ASP A  1 30  ? 14.202  25.021  49.224  1.00 37.41  ? 16  ASP A CB  1 
ATOM   68   C  CG  . ASP A  1 30  ? 14.430  26.044  50.328  1.00 40.57  ? 16  ASP A CG  1 
ATOM   69   O  OD1 . ASP A  1 30  ? 15.428  25.899  51.066  1.00 42.66  ? 16  ASP A OD1 1 
ATOM   70   O  OD2 . ASP A  1 30  ? 13.621  26.990  50.425  1.00 41.28  ? 16  ASP A OD2 1 
ATOM   71   N  N   . ASN A  1 31  ? 16.976  23.381  50.627  1.00 33.06  ? 17  ASN A N   1 
ATOM   72   C  CA  . ASN A  1 31  ? 17.485  22.504  51.671  1.00 33.05  ? 17  ASN A CA  1 
ATOM   73   C  C   . ASN A  1 31  ? 17.751  23.301  52.947  1.00 32.87  ? 17  ASN A C   1 
ATOM   74   O  O   . ASN A  1 31  ? 18.571  22.900  53.771  1.00 33.58  ? 17  ASN A O   1 
ATOM   75   C  CB  . ASN A  1 31  ? 18.724  21.736  51.215  1.00 32.54  ? 17  ASN A CB  1 
ATOM   76   C  CG  . ASN A  1 31  ? 18.409  20.744  50.120  1.00 33.33  ? 17  ASN A CG  1 
ATOM   77   O  OD1 . ASN A  1 31  ? 19.096  20.716  49.092  1.00 36.24  ? 17  ASN A OD1 1 
ATOM   78   N  ND2 . ASN A  1 31  ? 17.391  19.920  50.325  1.00 28.60  ? 17  ASN A ND2 1 
ATOM   79   N  N   . GLY A  1 32  ? 17.039  24.422  53.112  1.00 33.04  ? 18  GLY A N   1 
ATOM   80   C  CA  . GLY A  1 32  ? 17.075  25.173  54.356  1.00 34.65  ? 18  GLY A CA  1 
ATOM   81   C  C   . GLY A  1 32  ? 18.010  26.379  54.276  1.00 38.07  ? 18  GLY A C   1 
ATOM   82   O  O   . GLY A  1 32  ? 18.322  26.863  53.190  1.00 35.28  ? 18  GLY A O   1 
ATOM   83   N  N   . ARG A  1 33  ? 18.448  26.857  55.448  1.00 35.34  ? 19  ARG A N   1 
ATOM   84   C  CA  . ARG A  1 33  ? 19.203  28.095  55.547  1.00 35.30  ? 19  ARG A CA  1 
ATOM   85   C  C   . ARG A  1 33  ? 20.331  27.930  56.566  1.00 33.87  ? 19  ARG A C   1 
ATOM   86   O  O   . ARG A  1 33  ? 20.196  27.189  57.538  1.00 35.68  ? 19  ARG A O   1 
ATOM   87   C  CB  . ARG A  1 33  ? 18.266  29.243  55.944  1.00 40.55  ? 19  ARG A CB  1 
ATOM   88   C  CG  . ARG A  1 33  ? 17.076  29.448  55.016  1.00 42.21  ? 19  ARG A CG  1 
ATOM   89   C  CD  . ARG A  1 33  ? 17.383  30.296  53.791  1.00 47.16  ? 19  ARG A CD  1 
ATOM   90   N  NE  . ARG A  1 33  ? 16.199  30.340  52.926  1.00 46.58  ? 19  ARG A NE  1 
ATOM   91   C  CZ  . ARG A  1 33  ? 15.734  29.296  52.250  1.00 50.87  ? 19  ARG A CZ  1 
ATOM   92   N  NH1 . ARG A  1 33  ? 16.484  28.217  52.106  1.00 47.42  ? 19  ARG A NH1 1 
ATOM   93   N  NH2 . ARG A  1 33  ? 14.538  29.348  51.687  1.00 53.99  ? 19  ARG A NH2 1 
ATOM   94   N  N   . MET A  1 34  ? 21.448  28.626  56.318  1.00 32.29  ? 20  MET A N   1 
ATOM   95   C  CA  . MET A  1 34  ? 22.586  28.633  57.225  1.00 34.44  ? 20  MET A CA  1 
ATOM   96   C  C   . MET A  1 34  ? 22.992  30.083  57.488  1.00 31.82  ? 20  MET A C   1 
ATOM   97   O  O   . MET A  1 34  ? 22.725  30.961  56.670  1.00 34.32  ? 20  MET A O   1 
ATOM   98   C  CB  . MET A  1 34  ? 23.758  27.839  56.631  1.00 35.54  ? 20  MET A CB  1 
ATOM   99   C  CG  . MET A  1 34  ? 25.043  27.891  57.441  1.00 39.49  ? 20  MET A CG  1 
ATOM   100  S  SD  . MET A  1 34  ? 26.267  26.707  56.840  1.00 39.47  ? 20  MET A SD  1 
ATOM   101  C  CE  . MET A  1 34  ? 25.245  25.235  56.683  1.00 36.17  ? 20  MET A CE  1 
ATOM   102  N  N   . ARG A  1 35  ? 23.611  30.327  58.649  1.00 30.59  ? 21  ARG A N   1 
ATOM   103  C  CA  . ARG A  1 35  ? 24.103  31.650  59.001  1.00 34.16  ? 21  ARG A CA  1 
ATOM   104  C  C   . ARG A  1 35  ? 25.583  31.561  59.370  1.00 30.87  ? 21  ARG A C   1 
ATOM   105  O  O   . ARG A  1 35  ? 26.033  30.544  59.895  1.00 30.10  ? 21  ARG A O   1 
ATOM   106  C  CB  . ARG A  1 35  ? 23.295  32.250  60.161  1.00 37.82  ? 21  ARG A CB  1 
ATOM   107  C  CG  . ARG A  1 35  ? 21.983  32.911  59.756  1.00 39.65  ? 21  ARG A CG  1 
ATOM   108  C  CD  . ARG A  1 35  ? 21.225  33.500  60.941  1.00 37.41  ? 21  ARG A CD  1 
ATOM   109  N  NE  . ARG A  1 35  ? 20.829  32.469  61.906  1.00 40.01  ? 21  ARG A NE  1 
ATOM   110  C  CZ  . ARG A  1 35  ? 20.949  32.572  63.224  1.00 43.44  ? 21  ARG A CZ  1 
ATOM   111  N  NH1 . ARG A  1 35  ? 21.383  33.698  63.763  1.00 43.99  ? 21  ARG A NH1 1 
ATOM   112  N  NH2 . ARG A  1 35  ? 20.613  31.554  63.997  1.00 42.93  ? 21  ARG A NH2 1 
ATOM   113  N  N   . MET A  1 36  ? 26.331  32.639  59.094  1.00 30.30  ? 22  MET A N   1 
ATOM   114  C  CA  . MET A  1 36  ? 27.732  32.724  59.480  1.00 32.78  ? 22  MET A CA  1 
ATOM   115  C  C   . MET A  1 36  ? 28.233  34.161  59.350  1.00 30.49  ? 22  MET A C   1 
ATOM   116  O  O   . MET A  1 36  ? 27.597  34.995  58.708  1.00 30.37  ? 22  MET A O   1 
ATOM   117  C  CB  . MET A  1 36  ? 28.607  31.822  58.601  1.00 30.82  ? 22  MET A CB  1 
ATOM   118  C  CG  . MET A  1 36  ? 28.630  32.224  57.138  1.00 29.69  ? 22  MET A CG  1 
ATOM   119  S  SD  . MET A  1 36  ? 29.649  31.117  56.140  1.00 34.58  ? 22  MET A SD  1 
ATOM   120  C  CE  . MET A  1 36  ? 29.705  32.031  54.593  1.00 33.11  ? 22  MET A CE  1 
ATOM   121  N  N   . ASP A  1 37  ? 29.394  34.424  59.965  1.00 31.71  ? 23  ASP A N   1 
ATOM   122  C  CA  . ASP A  1 37  ? 30.089  35.697  59.842  1.00 32.59  ? 23  ASP A CA  1 
ATOM   123  C  C   . ASP A  1 37  ? 30.200  36.066  58.364  1.00 32.85  ? 23  ASP A C   1 
ATOM   124  O  O   . ASP A  1 37  ? 30.576  35.232  57.542  1.00 33.58  ? 23  ASP A O   1 
ATOM   125  C  CB  . ASP A  1 37  ? 31.464  35.633  60.493  1.00 29.06  ? 23  ASP A CB  1 
ATOM   126  C  CG  . ASP A  1 37  ? 32.149  36.973  60.716  1.00 27.86  ? 23  ASP A CG  1 
ATOM   127  O  OD1 . ASP A  1 37  ? 32.089  37.822  59.802  1.00 32.45  ? 23  ASP A OD1 1 
ATOM   128  O  OD2 . ASP A  1 37  ? 32.756  37.146  61.793  1.00 31.40  ? 23  ASP A OD2 1 
ATOM   129  N  N   . LYS A  1 38  ? 29.887  37.328  58.045  1.00 30.54  ? 24  LYS A N   1 
ATOM   130  C  CA  . LYS A  1 38  ? 29.894  37.815  56.674  1.00 31.88  ? 24  LYS A CA  1 
ATOM   131  C  C   . LYS A  1 38  ? 31.323  37.839  56.130  1.00 33.61  ? 24  LYS A C   1 
ATOM   132  O  O   . LYS A  1 38  ? 31.519  37.973  54.923  1.00 37.88  ? 24  LYS A O   1 
ATOM   133  C  CB  . LYS A  1 38  ? 29.273  39.216  56.590  1.00 33.69  ? 24  LYS A CB  1 
ATOM   134  C  CG  . LYS A  1 38  ? 29.056  39.763  55.180  1.00 37.18  ? 24  LYS A CG  1 
ATOM   135  C  CD  . LYS A  1 38  ? 28.654  41.234  55.147  1.00 44.42  ? 24  LYS A CD  1 
ATOM   136  C  CE  . LYS A  1 38  ? 28.805  41.884  53.801  1.00 48.55  ? 24  LYS A CE  1 
ATOM   137  N  NZ  . LYS A  1 38  ? 27.635  41.686  52.939  1.00 51.86  ? 24  LYS A NZ  1 
ATOM   138  N  N   . ASN A  1 39  ? 32.316  37.723  57.022  1.00 31.87  ? 25  ASN A N   1 
ATOM   139  C  CA  . ASN A  1 39  ? 33.716  37.765  56.621  1.00 34.83  ? 25  ASN A CA  1 
ATOM   140  C  C   . ASN A  1 39  ? 34.104  36.437  55.970  1.00 32.96  ? 25  ASN A C   1 
ATOM   141  O  O   . ASN A  1 39  ? 35.005  36.404  55.135  1.00 37.83  ? 25  ASN A O   1 
ATOM   142  C  CB  . ASN A  1 39  ? 34.648  38.125  57.776  1.00 33.18  ? 25  ASN A CB  1 
ATOM   143  C  CG  . ASN A  1 39  ? 34.623  39.598  58.115  1.00 35.00  ? 25  ASN A CG  1 
ATOM   144  O  OD1 . ASN A  1 39  ? 34.796  40.449  57.234  1.00 31.90  ? 25  ASN A OD1 1 
ATOM   145  N  ND2 . ASN A  1 39  ? 34.417  39.920  59.384  1.00 38.66  ? 25  ASN A ND2 1 
ATOM   146  N  N   . TRP A  1 40  ? 33.429  35.345  56.357  1.00 34.23  ? 26  TRP A N   1 
ATOM   147  C  CA  . TRP A  1 40  ? 33.610  34.060  55.698  1.00 34.59  ? 26  TRP A CA  1 
ATOM   148  C  C   . TRP A  1 40  ? 33.183  34.185  54.236  1.00 35.15  ? 26  TRP A C   1 
ATOM   149  O  O   . TRP A  1 40  ? 33.776  33.570  53.352  1.00 35.61  ? 26  TRP A O   1 
ATOM   150  C  CB  . TRP A  1 40  ? 32.798  32.947  56.382  1.00 31.94  ? 26  TRP A CB  1 
ATOM   151  C  CG  . TRP A  1 40  ? 33.183  32.603  57.799  1.00 33.53  ? 26  TRP A CG  1 
ATOM   152  C  CD1 . TRP A  1 40  ? 32.355  32.668  58.882  1.00 37.95  ? 26  TRP A CD1 1 
ATOM   153  C  CD2 . TRP A  1 40  ? 34.436  32.064  58.286  1.00 36.30  ? 26  TRP A CD2 1 
ATOM   154  N  NE1 . TRP A  1 40  ? 33.009  32.252  60.010  1.00 39.45  ? 26  TRP A NE1 1 
ATOM   155  C  CE2 . TRP A  1 40  ? 34.282  31.868  59.678  1.00 39.07  ? 26  TRP A CE2 1 
ATOM   156  C  CE3 . TRP A  1 40  ? 35.667  31.741  57.698  1.00 36.88  ? 26  TRP A CE3 1 
ATOM   157  C  CZ2 . TRP A  1 40  ? 35.307  31.367  60.478  1.00 38.79  ? 26  TRP A CZ2 1 
ATOM   158  C  CZ3 . TRP A  1 40  ? 36.676  31.238  58.491  1.00 35.50  ? 26  TRP A CZ3 1 
ATOM   159  C  CH2 . TRP A  1 40  ? 36.496  31.053  59.861  1.00 39.00  ? 26  TRP A CH2 1 
ATOM   160  N  N   . MET A  1 41  ? 32.134  34.985  54.007  1.00 35.18  ? 27  MET A N   1 
ATOM   161  C  CA  . MET A  1 41  ? 31.506  35.127  52.703  1.00 38.31  ? 27  MET A CA  1 
ATOM   162  C  C   . MET A  1 41  ? 32.305  36.110  51.848  1.00 35.55  ? 27  MET A C   1 
ATOM   163  O  O   . MET A  1 41  ? 32.672  35.800  50.717  1.00 33.08  ? 27  MET A O   1 
ATOM   164  C  CB  . MET A  1 41  ? 30.070  35.647  52.857  1.00 41.70  ? 27  MET A CB  1 
ATOM   165  C  CG  . MET A  1 41  ? 29.285  35.728  51.562  1.00 53.55  ? 27  MET A CG  1 
ATOM   166  S  SD  . MET A  1 41  ? 28.261  34.266  51.299  1.00 67.40  ? 27  MET A SD  1 
ATOM   167  C  CE  . MET A  1 41  ? 27.146  34.397  52.705  1.00 64.39  ? 27  MET A CE  1 
ATOM   168  N  N   . ILE A  1 42  ? 32.546  37.304  52.405  1.00 37.62  ? 28  ILE A N   1 
ATOM   169  C  CA  . ILE A  1 42  ? 33.290  38.361  51.736  1.00 35.92  ? 28  ILE A CA  1 
ATOM   170  C  C   . ILE A  1 42  ? 34.383  38.853  52.687  1.00 41.98  ? 28  ILE A C   1 
ATOM   171  O  O   . ILE A  1 42  ? 34.089  39.539  53.664  1.00 38.80  ? 28  ILE A O   1 
ATOM   172  C  CB  . ILE A  1 42  ? 32.356  39.514  51.313  1.00 36.76  ? 28  ILE A CB  1 
ATOM   173  C  CG1 . ILE A  1 42  ? 31.078  39.014  50.624  1.00 37.42  ? 28  ILE A CG1 1 
ATOM   174  C  CG2 . ILE A  1 42  ? 33.103  40.529  50.446  1.00 35.80  ? 28  ILE A CG2 1 
ATOM   175  C  CD1 . ILE A  1 42  ? 31.273  38.581  49.183  1.00 37.23  ? 28  ILE A CD1 1 
ATOM   176  N  N   . ALA A  1 43  ? 35.642  38.500  52.393  1.00 37.35  ? 29  ALA A N   1 
ATOM   177  C  CA  . ALA A  1 43  ? 36.759  38.830  53.265  1.00 35.80  ? 29  ALA A CA  1 
ATOM   178  C  C   . ALA A  1 43  ? 36.867  40.345  53.441  1.00 33.76  ? 29  ALA A C   1 
ATOM   179  O  O   . ALA A  1 43  ? 36.696  41.102  52.487  1.00 34.16  ? 29  ALA A O   1 
ATOM   180  C  CB  . ALA A  1 43  ? 38.045  38.244  52.712  1.00 32.60  ? 29  ALA A CB  1 
ATOM   181  N  N   . MET A  1 44  ? 37.140  40.770  54.682  1.00 34.31  ? 30  MET A N   1 
ATOM   182  C  CA  . MET A  1 44  ? 37.459  42.155  54.991  1.00 33.86  ? 30  MET A CA  1 
ATOM   183  C  C   . MET A  1 44  ? 36.385  43.092  54.439  1.00 36.09  ? 30  MET A C   1 
ATOM   184  O  O   . MET A  1 44  ? 36.708  44.099  53.813  1.00 33.53  ? 30  MET A O   1 
ATOM   185  C  CB  . MET A  1 44  ? 38.825  42.545  54.408  1.00 34.76  ? 30  MET A CB  1 
ATOM   186  C  CG  . MET A  1 44  ? 40.003  41.801  55.018  1.00 37.01  ? 30  MET A CG  1 
ATOM   187  S  SD  . MET A  1 44  ? 40.017  41.814  56.823  1.00 38.88  ? 30  MET A SD  1 
ATOM   188  C  CE  . MET A  1 44  ? 39.811  43.570  57.154  1.00 35.45  ? 30  MET A CE  1 
ATOM   189  N  N   . HIS A  1 45  ? 35.109  42.779  54.708  1.00 37.75  ? 31  HIS A N   1 
ATOM   190  C  CA  . HIS A  1 45  ? 34.001  43.553  54.166  1.00 41.91  ? 31  HIS A CA  1 
ATOM   191  C  C   . HIS A  1 45  ? 33.900  44.909  54.868  1.00 42.10  ? 31  HIS A C   1 
ATOM   192  O  O   . HIS A  1 45  ? 33.621  45.918  54.223  1.00 44.90  ? 31  HIS A O   1 
ATOM   193  C  CB  . HIS A  1 45  ? 32.685  42.762  54.228  1.00 44.18  ? 31  HIS A CB  1 
ATOM   194  C  CG  . HIS A  1 45  ? 32.106  42.613  55.597  1.00 40.94  ? 31  HIS A CG  1 
ATOM   195  N  ND1 . HIS A  1 45  ? 31.109  43.437  56.072  1.00 41.53  ? 31  HIS A ND1 1 
ATOM   196  C  CD2 . HIS A  1 45  ? 32.360  41.736  56.578  1.00 41.48  ? 31  HIS A CD2 1 
ATOM   197  C  CE1 . HIS A  1 45  ? 30.787  43.069  57.305  1.00 43.15  ? 31  HIS A CE1 1 
ATOM   198  N  NE2 . HIS A  1 45  ? 31.535  42.037  57.632  1.00 42.42  ? 31  HIS A NE2 1 
ATOM   199  N  N   . ASN A  1 46  ? 34.126  44.928  56.188  1.00 35.86  ? 32  ASN A N   1 
ATOM   200  C  CA  . ASN A  1 46  ? 33.973  46.144  56.977  1.00 38.00  ? 32  ASN A CA  1 
ATOM   201  C  C   . ASN A  1 46  ? 35.235  46.368  57.811  1.00 36.30  ? 32  ASN A C   1 
ATOM   202  O  O   . ASN A  1 46  ? 35.237  46.119  59.015  1.00 36.45  ? 32  ASN A O   1 
ATOM   203  C  CB  . ASN A  1 46  ? 32.705  46.093  57.829  1.00 40.12  ? 32  ASN A CB  1 
ATOM   204  C  CG  . ASN A  1 46  ? 32.431  47.387  58.561  1.00 39.08  ? 32  ASN A CG  1 
ATOM   205  O  OD1 . ASN A  1 46  ? 32.599  48.473  57.996  1.00 39.71  ? 32  ASN A OD1 1 
ATOM   206  N  ND2 . ASN A  1 46  ? 32.011  47.292  59.815  1.00 39.33  ? 32  ASN A ND2 1 
ATOM   207  N  N   . PRO A  1 47  ? 36.345  46.855  57.202  1.00 35.99  ? 33  PRO A N   1 
ATOM   208  C  CA  . PRO A  1 47  ? 37.624  46.998  57.903  1.00 36.74  ? 33  PRO A CA  1 
ATOM   209  C  C   . PRO A  1 47  ? 37.606  48.107  58.949  1.00 37.85  ? 33  PRO A C   1 
ATOM   210  O  O   . PRO A  1 47  ? 37.071  49.185  58.702  1.00 35.66  ? 33  PRO A O   1 
ATOM   211  C  CB  . PRO A  1 47  ? 38.640  47.318  56.786  1.00 38.29  ? 33  PRO A CB  1 
ATOM   212  C  CG  . PRO A  1 47  ? 37.900  47.047  55.490  1.00 37.18  ? 33  PRO A CG  1 
ATOM   213  C  CD  . PRO A  1 47  ? 36.432  47.293  55.801  1.00 35.95  ? 33  PRO A CD  1 
ATOM   214  N  N   . ALA A  1 48  ? 38.227  47.836  60.103  1.00 37.58  ? 34  ALA A N   1 
ATOM   215  C  CA  . ALA A  1 48  ? 38.387  48.839  61.144  1.00 35.81  ? 34  ALA A CA  1 
ATOM   216  C  C   . ALA A  1 48  ? 39.120  50.057  60.584  1.00 38.03  ? 34  ALA A C   1 
ATOM   217  O  O   . ALA A  1 48  ? 40.006  49.923  59.741  1.00 32.41  ? 34  ALA A O   1 
ATOM   218  C  CB  . ALA A  1 48  ? 39.124  48.244  62.324  1.00 33.26  ? 34  ALA A CB  1 
ATOM   219  N  N   . THR A  1 49  ? 38.726  51.245  61.063  1.00 36.90  ? 35  THR A N   1 
ATOM   220  C  CA  . THR A  1 49  ? 39.383  52.496  60.713  1.00 36.76  ? 35  THR A CA  1 
ATOM   221  C  C   . THR A  1 49  ? 39.671  53.267  61.999  1.00 38.53  ? 35  THR A C   1 
ATOM   222  O  O   . THR A  1 49  ? 39.289  52.834  63.084  1.00 33.00  ? 35  THR A O   1 
ATOM   223  C  CB  . THR A  1 49  ? 38.520  53.322  59.757  1.00 40.87  ? 35  THR A CB  1 
ATOM   224  O  OG1 . THR A  1 49  ? 37.305  53.605  60.446  1.00 43.93  ? 35  THR A OG1 1 
ATOM   225  C  CG2 . THR A  1 49  ? 38.213  52.598  58.459  1.00 42.83  ? 35  THR A CG2 1 
ATOM   226  N  N   . ILE A  1 50  ? 40.343  54.416  61.862  1.00 40.41  ? 36  ILE A N   1 
ATOM   227  C  CA  . ILE A  1 50  ? 40.696  55.234  63.011  1.00 50.14  ? 36  ILE A CA  1 
ATOM   228  C  C   . ILE A  1 50  ? 39.412  55.802  63.619  1.00 49.18  ? 36  ILE A C   1 
ATOM   229  O  O   . ILE A  1 50  ? 39.390  56.158  64.795  1.00 59.44  ? 36  ILE A O   1 
ATOM   230  C  CB  . ILE A  1 50  ? 41.700  56.338  62.617  1.00 49.90  ? 36  ILE A CB  1 
ATOM   231  C  CG1 . ILE A  1 50  ? 42.610  56.737  63.786  1.00 53.58  ? 36  ILE A CG1 1 
ATOM   232  C  CG2 . ILE A  1 50  ? 40.977  57.547  62.023  1.00 57.55  ? 36  ILE A CG2 1 
ATOM   233  C  CD1 . ILE A  1 50  ? 43.784  57.618  63.390  1.00 56.17  ? 36  ILE A CD1 1 
ATOM   234  N  N   . HIS A  1 51  ? 38.341  55.865  62.814  1.00 50.16  ? 37  HIS A N   1 
ATOM   235  C  CA  . HIS A  1 51  ? 37.069  56.423  63.253  1.00 50.95  ? 37  HIS A CA  1 
ATOM   236  C  C   . HIS A  1 51  ? 36.089  55.306  63.620  1.00 54.02  ? 37  HIS A C   1 
ATOM   237  O  O   . HIS A  1 51  ? 35.123  55.547  64.342  1.00 49.61  ? 37  HIS A O   1 
ATOM   238  C  CB  . HIS A  1 51  ? 36.501  57.389  62.203  1.00 59.20  ? 37  HIS A CB  1 
ATOM   239  C  CG  . HIS A  1 51  ? 37.288  58.655  62.064  1.00 78.38  ? 37  HIS A CG  1 
ATOM   240  N  ND1 . HIS A  1 51  ? 37.977  59.002  60.920  1.00 85.23  ? 37  HIS A ND1 1 
ATOM   241  C  CD2 . HIS A  1 51  ? 37.473  59.667  62.925  1.00 79.72  ? 37  HIS A CD2 1 
ATOM   242  C  CE1 . HIS A  1 51  ? 38.565  60.177  61.101  1.00 77.15  ? 37  HIS A CE1 1 
ATOM   243  N  NE2 . HIS A  1 51  ? 38.274  60.598  62.313  1.00 81.12  ? 37  HIS A NE2 1 
ATOM   244  N  N   . ASN A  1 52  ? 36.339  54.089  63.119  1.00 46.70  ? 38  ASN A N   1 
ATOM   245  C  CA  . ASN A  1 52  ? 35.551  52.920  63.487  1.00 43.04  ? 38  ASN A CA  1 
ATOM   246  C  C   . ASN A  1 52  ? 36.504  51.796  63.895  1.00 41.02  ? 38  ASN A C   1 
ATOM   247  O  O   . ASN A  1 52  ? 36.533  50.741  63.265  1.00 39.84  ? 38  ASN A O   1 
ATOM   248  C  CB  . ASN A  1 52  ? 34.599  52.501  62.368  1.00 43.86  ? 38  ASN A CB  1 
ATOM   249  C  CG  . ASN A  1 52  ? 33.572  51.486  62.821  1.00 47.46  ? 38  ASN A CG  1 
ATOM   250  O  OD1 . ASN A  1 52  ? 33.488  51.173  64.014  1.00 48.01  ? 38  ASN A OD1 1 
ATOM   251  N  ND2 . ASN A  1 52  ? 32.781  50.968  61.892  1.00 53.74  ? 38  ASN A ND2 1 
ATOM   252  N  N   . PRO A  1 53  ? 37.296  51.987  64.978  1.00 43.25  ? 39  PRO A N   1 
ATOM   253  C  CA  . PRO A  1 53  ? 38.355  51.044  65.356  1.00 42.72  ? 39  PRO A CA  1 
ATOM   254  C  C   . PRO A  1 53  ? 37.872  49.667  65.801  1.00 42.51  ? 39  PRO A C   1 
ATOM   255  O  O   . PRO A  1 53  ? 38.638  48.705  65.789  1.00 38.69  ? 39  PRO A O   1 
ATOM   256  C  CB  . PRO A  1 53  ? 39.063  51.774  66.512  1.00 42.33  ? 39  PRO A CB  1 
ATOM   257  C  CG  . PRO A  1 53  ? 37.981  52.646  67.110  1.00 43.84  ? 39  PRO A CG  1 
ATOM   258  C  CD  . PRO A  1 53  ? 37.193  53.125  65.905  1.00 44.08  ? 39  PRO A CD  1 
ATOM   259  N  N   . ASN A  1 54  ? 36.602  49.591  66.214  1.00 41.92  ? 40  ASN A N   1 
ATOM   260  C  CA  . ASN A  1 54  ? 36.030  48.358  66.729  1.00 45.42  ? 40  ASN A CA  1 
ATOM   261  C  C   . ASN A  1 54  ? 34.911  47.901  65.796  1.00 46.68  ? 40  ASN A C   1 
ATOM   262  O  O   . ASN A  1 54  ? 33.842  47.491  66.246  1.00 46.92  ? 40  ASN A O   1 
ATOM   263  C  CB  . ASN A  1 54  ? 35.557  48.534  68.169  1.00 51.17  ? 40  ASN A CB  1 
ATOM   264  C  CG  . ASN A  1 54  ? 36.691  48.908  69.095  1.00 53.15  ? 40  ASN A CG  1 
ATOM   265  O  OD1 . ASN A  1 54  ? 37.579  48.088  69.356  1.00 58.62  ? 40  ASN A OD1 1 
ATOM   266  N  ND2 . ASN A  1 54  ? 36.680  50.134  69.599  1.00 54.76  ? 40  ASN A ND2 1 
ATOM   267  N  N   . ALA A  1 55  ? 35.181  47.977  64.488  1.00 42.01  ? 41  ALA A N   1 
ATOM   268  C  CA  . ALA A  1 55  ? 34.207  47.618  63.470  1.00 40.37  ? 41  ALA A CA  1 
ATOM   269  C  C   . ALA A  1 55  ? 33.584  46.259  63.791  1.00 39.89  ? 41  ALA A C   1 
ATOM   270  O  O   . ALA A  1 55  ? 34.275  45.339  64.226  1.00 40.48  ? 41  ALA A O   1 
ATOM   271  C  CB  . ALA A  1 55  ? 34.868  47.626  62.108  1.00 44.54  ? 41  ALA A CB  1 
ATOM   272  N  N   A GLN A  1 56  ? 32.264  46.140  63.617  0.70 40.47  ? 42  GLN A N   1 
ATOM   273  N  N   B GLN A  1 56  ? 32.278  46.164  63.504  0.30 39.85  ? 42  GLN A N   1 
ATOM   274  C  CA  A GLN A  1 56  ? 31.583  44.888  63.905  0.70 42.25  ? 42  GLN A CA  1 
ATOM   275  C  CA  B GLN A  1 56  ? 31.444  45.008  63.802  0.30 41.27  ? 42  GLN A CA  1 
ATOM   276  C  C   A GLN A  1 56  ? 31.261  44.178  62.593  0.70 39.38  ? 42  GLN A C   1 
ATOM   277  C  C   B GLN A  1 56  ? 31.271  44.177  62.531  0.30 39.06  ? 42  GLN A C   1 
ATOM   278  O  O   A GLN A  1 56  ? 31.105  44.815  61.554  0.70 39.14  ? 42  GLN A O   1 
ATOM   279  O  O   B GLN A  1 56  ? 31.224  44.736  61.438  0.30 39.02  ? 42  GLN A O   1 
ATOM   280  C  CB  A GLN A  1 56  ? 30.313  45.107  64.730  0.70 44.47  ? 42  GLN A CB  1 
ATOM   281  C  CB  B GLN A  1 56  ? 30.092  45.545  64.283  0.30 41.31  ? 42  GLN A CB  1 
ATOM   282  C  CG  A GLN A  1 56  ? 30.558  45.732  66.100  0.70 43.66  ? 42  GLN A CG  1 
ATOM   283  C  CG  B GLN A  1 56  ? 29.270  44.591  65.145  0.30 42.32  ? 42  GLN A CG  1 
ATOM   284  C  CD  A GLN A  1 56  ? 29.276  46.101  66.813  0.70 42.98  ? 42  GLN A CD  1 
ATOM   285  C  CD  B GLN A  1 56  ? 28.047  45.266  65.731  0.30 41.19  ? 42  GLN A CD  1 
ATOM   286  O  OE1 A GLN A  1 56  ? 28.590  45.253  67.394  0.70 46.40  ? 42  GLN A OE1 1 
ATOM   287  O  OE1 B GLN A  1 56  ? 27.329  46.002  65.045  0.30 36.57  ? 42  GLN A OE1 1 
ATOM   288  N  NE2 A GLN A  1 56  ? 28.944  47.384  66.782  0.70 38.84  ? 42  GLN A NE2 1 
ATOM   289  N  NE2 B GLN A  1 56  ? 27.812  45.048  67.017  0.30 43.73  ? 42  GLN A NE2 1 
ATOM   290  N  N   . THR A  1 57  ? 31.178  42.846  62.669  1.00 38.41  ? 43  THR A N   1 
ATOM   291  C  CA  . THR A  1 57  ? 30.780  42.011  61.545  1.00 38.32  ? 43  THR A CA  1 
ATOM   292  C  C   . THR A  1 57  ? 29.278  41.752  61.668  1.00 44.40  ? 43  THR A C   1 
ATOM   293  O  O   . THR A  1 57  ? 28.658  42.175  62.642  1.00 39.08  ? 43  THR A O   1 
ATOM   294  C  CB  . THR A  1 57  ? 31.589  40.711  61.503  1.00 35.43  ? 43  THR A CB  1 
ATOM   295  O  OG1 . THR A  1 57  ? 31.304  40.111  60.243  1.00 38.41  ? 43  THR A OG1 1 
ATOM   296  C  CG2 . THR A  1 57  ? 31.232  39.746  62.619  1.00 39.06  ? 43  THR A CG2 1 
ATOM   297  N  N   . GLU A  1 58  ? 28.699  41.072  60.670  1.00 41.52  ? 44  GLU A N   1 
ATOM   298  C  CA  . GLU A  1 58  ? 27.298  40.682  60.713  1.00 41.61  ? 44  GLU A CA  1 
ATOM   299  C  C   . GLU A  1 58  ? 27.198  39.160  60.623  1.00 42.89  ? 44  GLU A C   1 
ATOM   300  O  O   . GLU A  1 58  ? 28.154  38.495  60.228  1.00 44.34  ? 44  GLU A O   1 
ATOM   301  C  CB  . GLU A  1 58  ? 26.496  41.284  59.557  1.00 48.63  ? 44  GLU A CB  1 
ATOM   302  C  CG  . GLU A  1 58  ? 26.979  42.661  59.111  1.00 52.86  ? 44  GLU A CG  1 
ATOM   303  C  CD  . GLU A  1 58  ? 26.243  43.186  57.891  1.00 58.09  ? 44  GLU A CD  1 
ATOM   304  O  OE1 . GLU A  1 58  ? 25.265  42.530  57.473  1.00 55.15  ? 44  GLU A OE1 1 
ATOM   305  O  OE2 . GLU A  1 58  ? 26.649  44.238  57.354  1.00 62.45  ? 44  GLU A OE2 1 
ATOM   306  N  N   . PHE A  1 59  ? 26.022  38.626  60.978  1.00 36.12  ? 45  PHE A N   1 
ATOM   307  C  CA  . PHE A  1 59  ? 25.754  37.198  60.903  1.00 39.22  ? 45  PHE A CA  1 
ATOM   308  C  C   . PHE A  1 59  ? 24.704  36.965  59.817  1.00 48.19  ? 45  PHE A C   1 
ATOM   309  O  O   . PHE A  1 59  ? 23.510  36.905  60.108  1.00 51.42  ? 45  PHE A O   1 
ATOM   310  C  CB  . PHE A  1 59  ? 25.290  36.705  62.279  1.00 36.71  ? 45  PHE A CB  1 
ATOM   311  C  CG  . PHE A  1 59  ? 25.608  35.252  62.611  1.00 35.11  ? 45  PHE A CG  1 
ATOM   312  C  CD1 . PHE A  1 59  ? 26.916  34.780  62.574  1.00 35.76  ? 45  PHE A CD1 1 
ATOM   313  C  CD2 . PHE A  1 59  ? 24.596  34.364  62.962  1.00 33.41  ? 45  PHE A CD2 1 
ATOM   314  C  CE1 . PHE A  1 59  ? 27.201  33.459  62.884  1.00 37.07  ? 45  PHE A CE1 1 
ATOM   315  C  CE2 . PHE A  1 59  ? 24.886  33.043  63.267  1.00 37.81  ? 45  PHE A CE2 1 
ATOM   316  C  CZ  . PHE A  1 59  ? 26.187  32.593  63.226  1.00 39.72  ? 45  PHE A CZ  1 
ATOM   317  N  N   . VAL A  1 60  ? 25.159  36.839  58.563  1.00 45.75  ? 46  VAL A N   1 
ATOM   318  C  CA  . VAL A  1 60  ? 24.270  36.893  57.411  1.00 42.92  ? 46  VAL A CA  1 
ATOM   319  C  C   . VAL A  1 60  ? 23.679  35.509  57.138  1.00 39.83  ? 46  VAL A C   1 
ATOM   320  O  O   . VAL A  1 60  ? 24.297  34.489  57.437  1.00 37.79  ? 46  VAL A O   1 
ATOM   321  C  CB  . VAL A  1 60  ? 24.988  37.456  56.167  1.00 46.31  ? 46  VAL A CB  1 
ATOM   322  C  CG1 . VAL A  1 60  ? 25.422  38.904  56.371  1.00 47.02  ? 46  VAL A CG1 1 
ATOM   323  C  CG2 . VAL A  1 60  ? 26.176  36.598  55.746  1.00 50.29  ? 46  VAL A CG2 1 
ATOM   324  N  N   . GLU A  1 61  ? 22.469  35.500  56.558  1.00 38.63  ? 47  GLU A N   1 
ATOM   325  C  CA  . GLU A  1 61  ? 21.741  34.275  56.261  1.00 38.38  ? 47  GLU A CA  1 
ATOM   326  C  C   . GLU A  1 61  ? 21.804  34.000  54.761  1.00 34.26  ? 47  GLU A C   1 
ATOM   327  O  O   . GLU A  1 61  ? 21.760  34.928  53.956  1.00 33.91  ? 47  GLU A O   1 
ATOM   328  C  CB  . GLU A  1 61  ? 20.278  34.380  56.703  1.00 38.31  ? 47  GLU A CB  1 
ATOM   329  C  CG  . GLU A  1 61  ? 19.501  33.074  56.564  1.00 37.96  ? 47  GLU A CG  1 
ATOM   330  C  CD  . GLU A  1 61  ? 18.085  33.117  57.114  1.00 41.85  ? 47  GLU A CD  1 
ATOM   331  O  OE1 . GLU A  1 61  ? 17.224  33.770  56.487  1.00 46.62  ? 47  GLU A OE1 1 
ATOM   332  O  OE2 . GLU A  1 61  ? 17.849  32.505  58.178  1.00 43.12  ? 47  GLU A OE2 1 
ATOM   333  N  N   . PHE A  1 62  ? 21.894  32.715  54.398  1.00 32.00  ? 48  PHE A N   1 
ATOM   334  C  CA  . PHE A  1 62  ? 21.983  32.325  53.001  1.00 32.21  ? 48  PHE A CA  1 
ATOM   335  C  C   . PHE A  1 62  ? 21.344  30.951  52.809  1.00 28.98  ? 48  PHE A C   1 
ATOM   336  O  O   . PHE A  1 62  ? 21.293  30.143  53.736  1.00 33.76  ? 48  PHE A O   1 
ATOM   337  C  CB  . PHE A  1 62  ? 23.443  32.360  52.532  1.00 34.00  ? 48  PHE A CB  1 
ATOM   338  C  CG  . PHE A  1 62  ? 24.389  31.440  53.290  1.00 32.98  ? 48  PHE A CG  1 
ATOM   339  C  CD1 . PHE A  1 62  ? 24.555  30.114  52.908  1.00 31.52  ? 48  PHE A CD1 1 
ATOM   340  C  CD2 . PHE A  1 62  ? 25.111  31.906  54.383  1.00 37.17  ? 48  PHE A CD2 1 
ATOM   341  C  CE1 . PHE A  1 62  ? 25.418  29.279  53.601  1.00 32.02  ? 48  PHE A CE1 1 
ATOM   342  C  CE2 . PHE A  1 62  ? 25.973  31.066  55.072  1.00 35.88  ? 48  PHE A CE2 1 
ATOM   343  C  CZ  . PHE A  1 62  ? 26.124  29.756  54.680  1.00 35.07  ? 48  PHE A CZ  1 
ATOM   344  N  N   . PRO A  1 63  ? 20.828  30.663  51.592  1.00 28.44  ? 49  PRO A N   1 
ATOM   345  C  CA  . PRO A  1 63  ? 20.197  29.376  51.290  1.00 29.48  ? 49  PRO A CA  1 
ATOM   346  C  C   . PRO A  1 63  ? 21.167  28.227  51.017  1.00 31.28  ? 49  PRO A C   1 
ATOM   347  O  O   . PRO A  1 63  ? 22.211  28.425  50.402  1.00 31.95  ? 49  PRO A O   1 
ATOM   348  C  CB  . PRO A  1 63  ? 19.353  29.701  50.038  1.00 30.26  ? 49  PRO A CB  1 
ATOM   349  C  CG  . PRO A  1 63  ? 20.095  30.836  49.354  1.00 31.49  ? 49  PRO A CG  1 
ATOM   350  C  CD  . PRO A  1 63  ? 20.810  31.596  50.454  1.00 29.35  ? 49  PRO A CD  1 
ATOM   351  N  N   . ILE A  1 64  ? 20.805  27.029  51.495  1.00 30.57  ? 50  ILE A N   1 
ATOM   352  C  CA  . ILE A  1 64  ? 21.420  25.789  51.048  1.00 33.89  ? 50  ILE A CA  1 
ATOM   353  C  C   . ILE A  1 64  ? 20.472  25.144  50.040  1.00 34.88  ? 50  ILE A C   1 
ATOM   354  O  O   . ILE A  1 64  ? 19.284  25.000  50.324  1.00 35.08  ? 50  ILE A O   1 
ATOM   355  C  CB  . ILE A  1 64  ? 21.704  24.832  52.224  1.00 34.38  ? 50  ILE A CB  1 
ATOM   356  C  CG1 . ILE A  1 64  ? 22.450  25.516  53.374  1.00 34.57  ? 50  ILE A CG1 1 
ATOM   357  C  CG2 . ILE A  1 64  ? 22.433  23.577  51.741  1.00 35.18  ? 50  ILE A CG2 1 
ATOM   358  C  CD1 . ILE A  1 64  ? 23.664  26.320  52.945  1.00 36.41  ? 50  ILE A CD1 1 
ATOM   359  N  N   . TYR A  1 65  ? 20.989  24.757  48.867  1.00 32.65  ? 51  TYR A N   1 
ATOM   360  C  CA  . TYR A  1 65  ? 20.144  24.120  47.868  1.00 32.73  ? 51  TYR A CA  1 
ATOM   361  C  C   . TYR A  1 65  ? 20.937  23.079  47.080  1.00 31.14  ? 51  TYR A C   1 
ATOM   362  O  O   . TYR A  1 65  ? 22.166  23.056  47.112  1.00 33.05  ? 51  TYR A O   1 
ATOM   363  C  CB  . TYR A  1 65  ? 19.491  25.152  46.940  1.00 35.40  ? 51  TYR A CB  1 
ATOM   364  C  CG  . TYR A  1 65  ? 20.384  25.787  45.881  1.00 33.93  ? 51  TYR A CG  1 
ATOM   365  C  CD1 . TYR A  1 65  ? 21.128  26.932  46.149  1.00 36.40  ? 51  TYR A CD1 1 
ATOM   366  C  CD2 . TYR A  1 65  ? 20.460  25.256  44.599  1.00 34.60  ? 51  TYR A CD2 1 
ATOM   367  C  CE1 . TYR A  1 65  ? 21.932  27.516  45.181  1.00 33.95  ? 51  TYR A CE1 1 
ATOM   368  C  CE2 . TYR A  1 65  ? 21.259  25.831  43.623  1.00 33.70  ? 51  TYR A CE2 1 
ATOM   369  C  CZ  . TYR A  1 65  ? 21.996  26.965  43.913  1.00 34.74  ? 51  TYR A CZ  1 
ATOM   370  O  OH  . TYR A  1 65  ? 22.784  27.535  42.953  1.00 31.55  ? 51  TYR A OH  1 
ATOM   371  N  N   . THR A  1 66  ? 20.185  22.217  46.383  1.00 29.10  ? 52  THR A N   1 
ATOM   372  C  CA  . THR A  1 66  ? 20.731  21.177  45.525  1.00 28.70  ? 52  THR A CA  1 
ATOM   373  C  C   . THR A  1 66  ? 19.974  21.201  44.197  1.00 29.83  ? 52  THR A C   1 
ATOM   374  O  O   . THR A  1 66  ? 18.931  21.844  44.084  1.00 30.38  ? 52  THR A O   1 
ATOM   375  C  CB  . THR A  1 66  ? 20.627  19.812  46.211  1.00 30.33  ? 52  THR A CB  1 
ATOM   376  O  OG1 . THR A  1 66  ? 19.277  19.688  46.653  1.00 30.16  ? 52  THR A OG1 1 
ATOM   377  C  CG2 . THR A  1 66  ? 21.563  19.670  47.398  1.00 30.61  ? 52  THR A CG2 1 
ATOM   378  N  N   . VAL A  1 67  ? 20.512  20.499  43.194  1.00 28.70  ? 53  VAL A N   1 
ATOM   379  C  CA  . VAL A  1 67  ? 19.913  20.469  41.869  1.00 28.89  ? 53  VAL A CA  1 
ATOM   380  C  C   . VAL A  1 67  ? 19.763  19.016  41.425  1.00 33.11  ? 53  VAL A C   1 
ATOM   381  O  O   . VAL A  1 67  ? 20.723  18.249  41.470  1.00 34.66  ? 53  VAL A O   1 
ATOM   382  C  CB  . VAL A  1 67  ? 20.748  21.275  40.851  1.00 29.38  ? 53  VAL A CB  1 
ATOM   383  C  CG1 . VAL A  1 67  ? 20.188  21.161  39.438  1.00 30.25  ? 53  VAL A CG1 1 
ATOM   384  C  CG2 . VAL A  1 67  ? 20.885  22.740  41.249  1.00 29.60  ? 53  VAL A CG2 1 
ATOM   385  N  N   . LEU A  1 68  ? 18.545  18.650  41.002  1.00 29.97  ? 54  LEU A N   1 
ATOM   386  C  CA  . LEU A  1 68  ? 18.297  17.360  40.378  1.00 29.88  ? 54  LEU A CA  1 
ATOM   387  C  C   . LEU A  1 68  ? 18.119  17.571  38.876  1.00 29.11  ? 54  LEU A C   1 
ATOM   388  O  O   . LEU A  1 68  ? 17.278  18.362  38.456  1.00 31.83  ? 54  LEU A O   1 
ATOM   389  C  CB  . LEU A  1 68  ? 17.066  16.692  40.997  1.00 30.86  ? 54  LEU A CB  1 
ATOM   390  C  CG  . LEU A  1 68  ? 16.595  15.394  40.330  1.00 32.20  ? 54  LEU A CG  1 
ATOM   391  C  CD1 . LEU A  1 68  ? 17.640  14.296  40.470  1.00 33.26  ? 54  LEU A CD1 1 
ATOM   392  C  CD2 . LEU A  1 68  ? 15.256  14.926  40.889  1.00 31.48  ? 54  LEU A CD2 1 
ATOM   393  N  N   . ILE A  1 69  ? 18.934  16.877  38.073  1.00 32.20  ? 55  ILE A N   1 
ATOM   394  C  CA  . ILE A  1 69  ? 18.713  16.825  36.637  1.00 34.93  ? 55  ILE A CA  1 
ATOM   395  C  C   . ILE A  1 69  ? 18.120  15.457  36.304  1.00 34.00  ? 55  ILE A C   1 
ATOM   396  O  O   . ILE A  1 69  ? 18.823  14.449  36.334  1.00 28.20  ? 55  ILE A O   1 
ATOM   397  C  CB  . ILE A  1 69  ? 19.999  17.101  35.828  1.00 34.66  ? 55  ILE A CB  1 
ATOM   398  C  CG1 . ILE A  1 69  ? 20.728  18.377  36.274  1.00 34.83  ? 55  ILE A CG1 1 
ATOM   399  C  CG2 . ILE A  1 69  ? 19.692  17.138  34.331  1.00 30.86  ? 55  ILE A CG2 1 
ATOM   400  C  CD1 . ILE A  1 69  ? 21.866  18.134  37.250  1.00 36.97  ? 55  ILE A CD1 1 
ATOM   401  N  N   . ASP A  1 70  ? 16.811  15.435  36.015  1.00 38.12  ? 56  ASP A N   1 
ATOM   402  C  CA  . ASP A  1 70  ? 16.138  14.223  35.574  1.00 39.03  ? 56  ASP A CA  1 
ATOM   403  C  C   . ASP A  1 70  ? 16.396  14.056  34.079  1.00 36.35  ? 56  ASP A C   1 
ATOM   404  O  O   . ASP A  1 70  ? 15.726  14.675  33.256  1.00 33.54  ? 56  ASP A O   1 
ATOM   405  C  CB  . ASP A  1 70  ? 14.652  14.249  35.907  1.00 39.78  ? 56  ASP A CB  1 
ATOM   406  C  CG  . ASP A  1 70  ? 13.929  12.920  35.737  1.00 38.43  ? 56  ASP A CG  1 
ATOM   407  O  OD1 . ASP A  1 70  ? 14.600  11.931  35.375  1.00 42.19  ? 56  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A  1 70  ? 12.704  12.884  35.972  1.00 43.21  ? 56  ASP A OD2 1 
ATOM   409  N  N   . HIS A  1 71  ? 17.383  13.217  33.747  1.00 37.52  ? 57  HIS A N   1 
ATOM   410  C  CA  . HIS A  1 71  ? 17.907  13.121  32.393  1.00 37.86  ? 57  HIS A CA  1 
ATOM   411  C  C   . HIS A  1 71  ? 17.625  11.721  31.849  1.00 34.41  ? 57  HIS A C   1 
ATOM   412  O  O   . HIS A  1 71  ? 17.734  10.737  32.576  1.00 35.93  ? 57  HIS A O   1 
ATOM   413  C  CB  . HIS A  1 71  ? 19.401  13.474  32.392  1.00 36.68  ? 57  HIS A CB  1 
ATOM   414  C  CG  . HIS A  1 71  ? 20.033  13.614  31.044  1.00 37.15  ? 57  HIS A CG  1 
ATOM   415  N  ND1 . HIS A  1 71  ? 20.200  12.559  30.172  1.00 33.06  ? 57  HIS A ND1 1 
ATOM   416  C  CD2 . HIS A  1 71  ? 20.540  14.692  30.423  1.00 36.58  ? 57  HIS A CD2 1 
ATOM   417  C  CE1 . HIS A  1 71  ? 20.789  12.995  29.067  1.00 34.29  ? 57  HIS A CE1 1 
ATOM   418  N  NE2 . HIS A  1 71  ? 21.008  14.286  29.200  1.00 34.22  ? 57  HIS A NE2 1 
ATOM   419  N  N   . PRO A  1 72  ? 17.249  11.590  30.557  1.00 38.05  ? 58  PRO A N   1 
ATOM   420  C  CA  . PRO A  1 72  ? 16.957  10.280  29.968  1.00 39.19  ? 58  PRO A CA  1 
ATOM   421  C  C   . PRO A  1 72  ? 17.992  9.207   30.302  1.00 39.90  ? 58  PRO A C   1 
ATOM   422  O  O   . PRO A  1 72  ? 17.642  8.043   30.487  1.00 39.80  ? 58  PRO A O   1 
ATOM   423  C  CB  . PRO A  1 72  ? 16.919  10.566  28.454  1.00 42.86  ? 58  PRO A CB  1 
ATOM   424  C  CG  . PRO A  1 72  ? 16.568  12.036  28.338  1.00 43.58  ? 58  PRO A CG  1 
ATOM   425  C  CD  . PRO A  1 72  ? 17.073  12.701  29.608  1.00 41.87  ? 58  PRO A CD  1 
ATOM   426  N  N   . GLU A  1 73  ? 19.268  9.610   30.363  1.00 40.17  ? 59  GLU A N   1 
ATOM   427  C  CA  . GLU A  1 73  ? 20.374  8.675   30.512  1.00 39.37  ? 59  GLU A CA  1 
ATOM   428  C  C   . GLU A  1 73  ? 20.553  8.298   31.981  1.00 38.18  ? 59  GLU A C   1 
ATOM   429  O  O   . GLU A  1 73  ? 21.308  7.381   32.297  1.00 39.13  ? 59  GLU A O   1 
ATOM   430  C  CB  . GLU A  1 73  ? 21.669  9.269   29.956  1.00 38.11  ? 59  GLU A CB  1 
ATOM   431  C  CG  . GLU A  1 73  ? 21.610  9.585   28.464  1.00 40.35  ? 59  GLU A CG  1 
ATOM   432  C  CD  . GLU A  1 73  ? 22.842  10.298  27.933  1.00 36.84  ? 59  GLU A CD  1 
ATOM   433  O  OE1 . GLU A  1 73  ? 23.962  9.850   28.255  1.00 37.60  ? 59  GLU A OE1 1 
ATOM   434  O  OE2 . GLU A  1 73  ? 22.683  11.288  27.189  1.00 36.92  ? 59  GLU A OE2 1 
ATOM   435  N  N   . GLY A  1 74  ? 19.854  9.014   32.870  1.00 36.11  ? 60  GLY A N   1 
ATOM   436  C  CA  . GLY A  1 74  ? 19.937  8.764   34.301  1.00 34.74  ? 60  GLY A CA  1 
ATOM   437  C  C   . GLY A  1 74  ? 19.860  10.063  35.100  1.00 33.71  ? 60  GLY A C   1 
ATOM   438  O  O   . GLY A  1 74  ? 20.280  11.116  34.624  1.00 35.70  ? 60  GLY A O   1 
ATOM   439  N  N   . LYS A  1 75  ? 19.318  9.970   36.320  1.00 33.68  ? 61  LYS A N   1 
ATOM   440  C  CA  . LYS A  1 75  ? 19.160  11.123  37.192  1.00 34.31  ? 61  LYS A CA  1 
ATOM   441  C  C   . LYS A  1 75  ? 20.521  11.529  37.760  1.00 29.33  ? 61  LYS A C   1 
ATOM   442  O  O   . LYS A  1 75  ? 21.264  10.691  38.266  1.00 27.47  ? 61  LYS A O   1 
ATOM   443  C  CB  . LYS A  1 75  ? 18.149  10.806  38.302  1.00 34.99  ? 61  LYS A CB  1 
ATOM   444  C  CG  . LYS A  1 75  ? 16.683  10.769  37.871  1.00 40.14  ? 61  LYS A CG  1 
ATOM   445  C  CD  . LYS A  1 75  ? 15.765  10.027  38.838  1.00 43.05  ? 61  LYS A CD  1 
ATOM   446  C  CE  . LYS A  1 75  ? 14.304  10.188  38.524  1.00 44.35  ? 61  LYS A CE  1 
ATOM   447  N  NZ  . LYS A  1 75  ? 13.972  9.778   37.155  1.00 43.21  ? 61  LYS A NZ  1 
ATOM   448  N  N   . ILE A  1 76  ? 20.826  12.829  37.670  1.00 30.47  ? 62  ILE A N   1 
ATOM   449  C  CA  . ILE A  1 76  ? 22.079  13.388  38.159  1.00 32.95  ? 62  ILE A CA  1 
ATOM   450  C  C   . ILE A  1 76  ? 21.767  14.366  39.291  1.00 31.91  ? 62  ILE A C   1 
ATOM   451  O  O   . ILE A  1 76  ? 20.920  15.242  39.135  1.00 32.44  ? 62  ILE A O   1 
ATOM   452  C  CB  . ILE A  1 76  ? 22.850  14.073  37.011  1.00 37.59  ? 62  ILE A CB  1 
ATOM   453  C  CG1 . ILE A  1 76  ? 23.143  13.099  35.865  1.00 37.81  ? 62  ILE A CG1 1 
ATOM   454  C  CG2 . ILE A  1 76  ? 24.130  14.740  37.520  1.00 36.34  ? 62  ILE A CG2 1 
ATOM   455  C  CD1 . ILE A  1 76  ? 23.437  13.778  34.539  1.00 37.90  ? 62  ILE A CD1 1 
ATOM   456  N  N   . LEU A  1 77  ? 22.460  14.210  40.426  1.00 31.56  ? 63  LEU A N   1 
ATOM   457  C  CA  . LEU A  1 77  ? 22.277  15.092  41.570  1.00 32.55  ? 63  LEU A CA  1 
ATOM   458  C  C   . LEU A  1 77  ? 23.561  15.883  41.826  1.00 30.78  ? 63  LEU A C   1 
ATOM   459  O  O   . LEU A  1 77  ? 24.646  15.308  41.878  1.00 30.49  ? 63  LEU A O   1 
ATOM   460  C  CB  . LEU A  1 77  ? 21.872  14.270  42.794  1.00 33.91  ? 63  LEU A CB  1 
ATOM   461  C  CG  . LEU A  1 77  ? 21.635  15.061  44.085  1.00 33.59  ? 63  LEU A CG  1 
ATOM   462  C  CD1 . LEU A  1 77  ? 20.406  15.946  43.965  1.00 34.17  ? 63  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A  1 77  ? 21.513  14.134  45.284  1.00 35.34  ? 63  LEU A CD2 1 
ATOM   464  N  N   . PHE A  1 78  ? 23.416  17.204  41.999  1.00 29.49  ? 64  PHE A N   1 
ATOM   465  C  CA  . PHE A  1 78  ? 24.541  18.092  42.258  1.00 27.46  ? 64  PHE A CA  1 
ATOM   466  C  C   . PHE A  1 78  ? 24.451  18.601  43.696  1.00 28.52  ? 64  PHE A C   1 
ATOM   467  O  O   . PHE A  1 78  ? 23.544  19.363  44.022  1.00 27.80  ? 64  PHE A O   1 
ATOM   468  C  CB  . PHE A  1 78  ? 24.546  19.249  41.250  1.00 26.39  ? 64  PHE A CB  1 
ATOM   469  C  CG  . PHE A  1 78  ? 25.726  20.206  41.368  1.00 25.64  ? 64  PHE A CG  1 
ATOM   470  C  CD1 . PHE A  1 78  ? 26.949  19.912  40.771  1.00 27.65  ? 64  PHE A CD1 1 
ATOM   471  C  CD2 . PHE A  1 78  ? 25.610  21.400  42.069  1.00 27.45  ? 64  PHE A CD2 1 
ATOM   472  C  CE1 . PHE A  1 78  ? 28.021  20.786  40.879  1.00 27.40  ? 64  PHE A CE1 1 
ATOM   473  C  CE2 . PHE A  1 78  ? 26.686  22.270  42.174  1.00 27.88  ? 64  PHE A CE2 1 
ATOM   474  C  CZ  . PHE A  1 78  ? 27.888  21.961  41.580  1.00 27.03  ? 64  PHE A CZ  1 
ATOM   475  N  N   . ASP A  1 79  ? 25.408  18.182  44.539  1.00 26.79  ? 65  ASP A N   1 
ATOM   476  C  CA  . ASP A  1 79  ? 25.429  18.532  45.955  1.00 28.89  ? 65  ASP A CA  1 
ATOM   477  C  C   . ASP A  1 79  ? 24.296  17.812  46.692  1.00 28.76  ? 65  ASP A C   1 
ATOM   478  O  O   . ASP A  1 79  ? 23.375  17.299  46.058  1.00 27.18  ? 65  ASP A O   1 
ATOM   479  C  CB  . ASP A  1 79  ? 25.432  20.042  46.143  1.00 29.86  ? 65  ASP A CB  1 
ATOM   480  C  CG  . ASP A  1 79  ? 26.782  20.716  45.928  1.00 32.05  ? 65  ASP A CG  1 
ATOM   481  O  OD1 . ASP A  1 79  ? 27.792  19.987  45.831  1.00 31.31  ? 65  ASP A OD1 1 
ATOM   482  O  OD2 . ASP A  1 79  ? 26.815  21.962  45.851  1.00 35.50  ? 65  ASP A OD2 1 
ATOM   483  N  N   . THR A  1 80  ? 24.375  17.774  48.035  1.00 26.76  ? 66  THR A N   1 
ATOM   484  C  CA  . THR A  1 80  ? 23.459  16.974  48.844  1.00 28.40  ? 66  THR A CA  1 
ATOM   485  C  C   . THR A  1 80  ? 23.046  17.694  50.131  1.00 29.24  ? 66  THR A C   1 
ATOM   486  O  O   . THR A  1 80  ? 22.422  17.080  50.994  1.00 30.67  ? 66  THR A O   1 
ATOM   487  C  CB  . THR A  1 80  ? 24.089  15.625  49.200  1.00 26.39  ? 66  THR A CB  1 
ATOM   488  O  OG1 . THR A  1 80  ? 25.182  15.900  50.071  1.00 26.42  ? 66  THR A OG1 1 
ATOM   489  C  CG2 . THR A  1 80  ? 24.559  14.838  47.990  1.00 26.76  ? 66  THR A CG2 1 
ATOM   490  N  N   . SER A  1 81  ? 23.405  18.975  50.272  1.00 27.04  ? 67  SER A N   1 
ATOM   491  C  CA  . SER A  1 81  ? 23.043  19.762  51.445  1.00 29.80  ? 67  SER A CA  1 
ATOM   492  C  C   . SER A  1 81  ? 23.608  19.129  52.720  1.00 33.63  ? 67  SER A C   1 
ATOM   493  O  O   . SER A  1 81  ? 24.656  18.485  52.687  1.00 31.51  ? 67  SER A O   1 
ATOM   494  C  CB  . SER A  1 81  ? 21.541  19.961  51.539  1.00 30.34  ? 67  SER A CB  1 
ATOM   495  O  OG  . SER A  1 81  ? 20.860  18.737  51.781  1.00 26.82  ? 67  SER A OG  1 
ATOM   496  N  N   . CYS A  1 82  ? 22.909  19.338  53.847  1.00 29.71  ? 68  CYS A N   1 
ATOM   497  C  CA  . CYS A  1 82  ? 23.381  18.912  55.158  1.00 29.58  ? 68  CYS A CA  1 
ATOM   498  C  C   . CYS A  1 82  ? 22.658  17.636  55.595  1.00 28.28  ? 68  CYS A C   1 
ATOM   499  O  O   . CYS A  1 82  ? 21.568  17.343  55.111  1.00 28.05  ? 68  CYS A O   1 
ATOM   500  C  CB  . CYS A  1 82  ? 23.152  19.998  56.206  1.00 28.76  ? 68  CYS A CB  1 
ATOM   501  S  SG  . CYS A  1 82  ? 23.599  21.666  55.654  1.00 32.09  ? 68  CYS A SG  1 
ATOM   502  N  N   . ASN A  1 83  ? 23.272  16.882  56.517  1.00 27.68  ? 69  ASN A N   1 
ATOM   503  C  CA  . ASN A  1 83  ? 22.644  15.691  57.071  1.00 29.02  ? 69  ASN A CA  1 
ATOM   504  C  C   . ASN A  1 83  ? 21.532  16.128  58.026  1.00 28.31  ? 69  ASN A C   1 
ATOM   505  O  O   . ASN A  1 83  ? 21.699  17.089  58.774  1.00 26.69  ? 69  ASN A O   1 
ATOM   506  C  CB  . ASN A  1 83  ? 23.647  14.778  57.775  1.00 28.18  ? 69  ASN A CB  1 
ATOM   507  C  CG  . ASN A  1 83  ? 23.168  13.346  57.875  1.00 32.47  ? 69  ASN A CG  1 
ATOM   508  O  OD1 . ASN A  1 83  ? 23.288  12.576  56.914  1.00 33.17  ? 69  ASN A OD1 1 
ATOM   509  N  ND2 . ASN A  1 83  ? 22.650  12.959  59.031  1.00 31.00  ? 69  ASN A ND2 1 
ATOM   510  N  N   . PRO A  1 84  ? 20.353  15.465  58.013  1.00 30.12  ? 70  PRO A N   1 
ATOM   511  C  CA  . PRO A  1 84  ? 19.289  15.762  58.978  1.00 31.56  ? 70  PRO A CA  1 
ATOM   512  C  C   . PRO A  1 84  ? 19.733  15.716  60.439  1.00 34.40  ? 70  PRO A C   1 
ATOM   513  O  O   . PRO A  1 84  ? 19.153  16.396  61.283  1.00 36.97  ? 70  PRO A O   1 
ATOM   514  C  CB  . PRO A  1 84  ? 18.230  14.680  58.680  1.00 29.20  ? 70  PRO A CB  1 
ATOM   515  C  CG  . PRO A  1 84  ? 18.457  14.325  57.229  1.00 32.21  ? 70  PRO A CG  1 
ATOM   516  C  CD  . PRO A  1 84  ? 19.964  14.434  57.036  1.00 32.09  ? 70  PRO A CD  1 
ATOM   517  N  N   . ASN A  1 85  ? 20.765  14.912  60.728  1.00 35.32  ? 71  ASN A N   1 
ATOM   518  C  CA  . ASN A  1 85  ? 21.211  14.684  62.096  1.00 35.61  ? 71  ASN A CA  1 
ATOM   519  C  C   . ASN A  1 85  ? 22.389  15.597  62.439  1.00 30.99  ? 71  ASN A C   1 
ATOM   520  O  O   . ASN A  1 85  ? 23.216  15.244  63.277  1.00 33.18  ? 71  ASN A O   1 
ATOM   521  C  CB  . ASN A  1 85  ? 21.617  13.230  62.331  1.00 43.24  ? 71  ASN A CB  1 
ATOM   522  C  CG  . ASN A  1 85  ? 20.487  12.252  62.101  1.00 50.80  ? 71  ASN A CG  1 
ATOM   523  O  OD1 . ASN A  1 85  ? 19.468  12.301  62.799  1.00 55.97  ? 71  ASN A OD1 1 
ATOM   524  N  ND2 . ASN A  1 85  ? 20.653  11.353  61.141  1.00 55.39  ? 71  ASN A ND2 1 
ATOM   525  N  N   . SER A  1 86  ? 22.451  16.776  61.808  1.00 31.75  ? 72  SER A N   1 
ATOM   526  C  CA  . SER A  1 86  ? 23.607  17.653  61.933  1.00 35.44  ? 72  SER A CA  1 
ATOM   527  C  C   . SER A  1 86  ? 23.558  18.446  63.238  1.00 36.16  ? 72  SER A C   1 
ATOM   528  O  O   . SER A  1 86  ? 24.531  18.463  63.991  1.00 35.37  ? 72  SER A O   1 
ATOM   529  C  CB  . SER A  1 86  ? 23.718  18.582  60.746  1.00 34.94  ? 72  SER A CB  1 
ATOM   530  O  OG  . SER A  1 86  ? 23.985  17.857  59.553  1.00 36.56  ? 72  SER A OG  1 
ATOM   531  N  N   . MET A  1 87  ? 22.419  19.101  63.491  1.00 39.24  ? 73  MET A N   1 
ATOM   532  C  CA  . MET A  1 87  ? 22.320  20.118  64.527  1.00 36.28  ? 73  MET A CA  1 
ATOM   533  C  C   . MET A  1 87  ? 21.759  19.518  65.815  1.00 39.21  ? 73  MET A C   1 
ATOM   534  O  O   . MET A  1 87  ? 21.153  18.448  65.798  1.00 34.24  ? 73  MET A O   1 
ATOM   535  C  CB  . MET A  1 87  ? 21.417  21.265  64.060  1.00 36.50  ? 73  MET A CB  1 
ATOM   536  C  CG  . MET A  1 87  ? 22.001  22.077  62.918  1.00 35.88  ? 73  MET A CG  1 
ATOM   537  S  SD  . MET A  1 87  ? 23.383  23.118  63.430  1.00 34.62  ? 73  MET A SD  1 
ATOM   538  C  CE  . MET A  1 87  ? 22.575  24.138  64.673  1.00 36.01  ? 73  MET A CE  1 
ATOM   539  N  N   . GLY A  1 88  ? 21.974  20.227  66.931  1.00 40.77  ? 74  GLY A N   1 
ATOM   540  C  CA  . GLY A  1 88  ? 21.403  19.848  68.214  1.00 46.80  ? 74  GLY A CA  1 
ATOM   541  C  C   . GLY A  1 88  ? 22.400  19.088  69.088  1.00 46.64  ? 74  GLY A C   1 
ATOM   542  O  O   . GLY A  1 88  ? 23.496  18.752  68.646  1.00 42.49  ? 74  GLY A O   1 
ATOM   543  N  N   . PRO A  1 89  ? 22.035  18.781  70.354  1.00 42.53  ? 75  PRO A N   1 
ATOM   544  C  CA  . PRO A  1 89  ? 22.978  18.198  71.312  1.00 43.66  ? 75  PRO A CA  1 
ATOM   545  C  C   . PRO A  1 89  ? 23.281  16.715  71.100  1.00 40.35  ? 75  PRO A C   1 
ATOM   546  O  O   . PRO A  1 89  ? 24.212  16.182  71.700  1.00 42.94  ? 75  PRO A O   1 
ATOM   547  C  CB  . PRO A  1 89  ? 22.293  18.466  72.669  1.00 48.51  ? 75  PRO A CB  1 
ATOM   548  C  CG  . PRO A  1 89  ? 20.809  18.503  72.355  1.00 48.22  ? 75  PRO A CG  1 
ATOM   549  C  CD  . PRO A  1 89  ? 20.692  18.990  70.921  1.00 47.25  ? 75  PRO A CD  1 
ATOM   550  N  N   . GLN A  1 90  ? 22.486  16.053  70.251  1.00 38.16  ? 76  GLN A N   1 
ATOM   551  C  CA  . GLN A  1 90  ? 22.789  14.697  69.820  1.00 42.16  ? 76  GLN A CA  1 
ATOM   552  C  C   . GLN A  1 90  ? 23.235  14.728  68.358  1.00 41.40  ? 76  GLN A C   1 
ATOM   553  O  O   . GLN A  1 90  ? 23.229  13.700  67.683  1.00 42.01  ? 76  GLN A O   1 
ATOM   554  C  CB  . GLN A  1 90  ? 21.595  13.751  69.980  1.00 44.34  ? 76  GLN A CB  1 
ATOM   555  C  CG  . GLN A  1 90  ? 21.239  13.396  71.421  1.00 47.48  ? 76  GLN A CG  1 
ATOM   556  C  CD  . GLN A  1 90  ? 20.394  14.451  72.103  1.00 44.52  ? 76  GLN A CD  1 
ATOM   557  O  OE1 . GLN A  1 90  ? 19.448  14.993  71.522  1.00 40.52  ? 76  GLN A OE1 1 
ATOM   558  N  NE2 . GLN A  1 90  ? 20.737  14.761  73.344  1.00 44.26  ? 76  GLN A NE2 1 
ATOM   559  N  N   . GLY A  1 91  ? 23.631  15.914  67.881  1.00 37.97  ? 77  GLY A N   1 
ATOM   560  C  CA  . GLY A  1 91  ? 23.926  16.130  66.471  1.00 41.24  ? 77  GLY A CA  1 
ATOM   561  C  C   . GLY A  1 91  ? 25.315  15.626  66.082  1.00 36.69  ? 77  GLY A C   1 
ATOM   562  O  O   . GLY A  1 91  ? 26.142  15.331  66.942  1.00 38.09  ? 77  GLY A O   1 
ATOM   563  N  N   . ARG A  1 92  ? 25.558  15.537  64.769  1.00 38.21  ? 78  ARG A N   1 
ATOM   564  C  CA  . ARG A  1 92  ? 26.831  15.068  64.240  1.00 35.94  ? 78  ARG A CA  1 
ATOM   565  C  C   . ARG A  1 92  ? 27.862  16.195  64.277  1.00 33.51  ? 78  ARG A C   1 
ATOM   566  O  O   . ARG A  1 92  ? 29.044  15.949  64.509  1.00 35.01  ? 78  ARG A O   1 
ATOM   567  C  CB  . ARG A  1 92  ? 26.664  14.550  62.806  1.00 34.67  ? 78  ARG A CB  1 
ATOM   568  C  CG  . ARG A  1 92  ? 25.962  13.206  62.682  1.00 33.75  ? 78  ARG A CG  1 
ATOM   569  C  CD  . ARG A  1 92  ? 25.783  12.828  61.220  1.00 32.25  ? 78  ARG A CD  1 
ATOM   570  N  NE  . ARG A  1 92  ? 25.304  11.456  61.028  1.00 34.97  ? 78  ARG A NE  1 
ATOM   571  C  CZ  . ARG A  1 92  ? 25.270  10.840  59.853  1.00 35.26  ? 78  ARG A CZ  1 
ATOM   572  N  NH1 . ARG A  1 92  ? 25.739  11.448  58.777  1.00 34.25  ? 78  ARG A NH1 1 
ATOM   573  N  NH2 . ARG A  1 92  ? 24.783  9.615   59.760  1.00 34.58  ? 78  ARG A NH2 1 
ATOM   574  N  N   . TRP A  1 93  ? 27.403  17.430  64.037  1.00 29.24  ? 79  TRP A N   1 
ATOM   575  C  CA  . TRP A  1 93  ? 28.279  18.592  64.026  1.00 31.74  ? 79  TRP A CA  1 
ATOM   576  C  C   . TRP A  1 93  ? 28.730  18.924  65.447  1.00 36.74  ? 79  TRP A C   1 
ATOM   577  O  O   . TRP A  1 93  ? 27.935  18.864  66.383  1.00 37.00  ? 79  TRP A O   1 
ATOM   578  C  CB  . TRP A  1 93  ? 27.572  19.805  63.403  1.00 30.06  ? 79  TRP A CB  1 
ATOM   579  C  CG  . TRP A  1 93  ? 27.236  19.678  61.939  1.00 27.85  ? 79  TRP A CG  1 
ATOM   580  C  CD1 . TRP A  1 93  ? 27.329  18.567  61.152  1.00 27.58  ? 79  TRP A CD1 1 
ATOM   581  C  CD2 . TRP A  1 93  ? 26.717  20.727  61.092  1.00 25.99  ? 79  TRP A CD2 1 
ATOM   582  N  NE1 . TRP A  1 93  ? 26.922  18.854  59.875  1.00 28.03  ? 79  TRP A NE1 1 
ATOM   583  C  CE2 . TRP A  1 93  ? 26.537  20.168  59.808  1.00 25.84  ? 79  TRP A CE2 1 
ATOM   584  C  CE3 . TRP A  1 93  ? 26.391  22.074  61.292  1.00 28.56  ? 79  TRP A CE3 1 
ATOM   585  C  CZ2 . TRP A  1 93  ? 26.047  20.914  58.738  1.00 27.53  ? 79  TRP A CZ2 1 
ATOM   586  C  CZ3 . TRP A  1 93  ? 25.909  22.809  60.231  1.00 27.15  ? 79  TRP A CZ3 1 
ATOM   587  C  CH2 . TRP A  1 93  ? 25.738  22.234  58.973  1.00 28.00  ? 79  TRP A CH2 1 
ATOM   588  N  N   . ALA A  1 94  ? 30.010  19.293  65.587  1.00 38.01  ? 80  ALA A N   1 
ATOM   589  C  CA  . ALA A  1 94  ? 30.538  19.805  66.842  1.00 39.62  ? 80  ALA A CA  1 
ATOM   590  C  C   . ALA A  1 94  ? 29.778  21.072  67.224  1.00 42.11  ? 80  ALA A C   1 
ATOM   591  O  O   . ALA A  1 94  ? 29.287  21.786  66.353  1.00 37.73  ? 80  ALA A O   1 
ATOM   592  C  CB  . ALA A  1 94  ? 32.022  20.075  66.713  1.00 36.46  ? 80  ALA A CB  1 
ATOM   593  N  N   . GLU A  1 95  ? 29.696  21.347  68.531  1.00 43.49  ? 81  GLU A N   1 
ATOM   594  C  CA  . GLU A  1 95  ? 28.960  22.501  69.021  1.00 43.25  ? 81  GLU A CA  1 
ATOM   595  C  C   . GLU A  1 95  ? 29.612  23.777  68.488  1.00 35.15  ? 81  GLU A C   1 
ATOM   596  O  O   . GLU A  1 95  ? 28.924  24.751  68.194  1.00 34.58  ? 81  GLU A O   1 
ATOM   597  C  CB  . GLU A  1 95  ? 28.890  22.484  70.550  1.00 49.32  ? 81  GLU A CB  1 
ATOM   598  C  CG  . GLU A  1 95  ? 27.882  23.475  71.127  1.00 50.52  ? 81  GLU A CG  1 
ATOM   599  C  CD  . GLU A  1 95  ? 26.475  23.343  70.567  1.00 53.19  ? 81  GLU A CD  1 
ATOM   600  O  OE1 . GLU A  1 95  ? 25.951  22.209  70.541  1.00 58.68  ? 81  GLU A OE1 1 
ATOM   601  O  OE2 . GLU A  1 95  ? 25.902  24.378  70.165  1.00 60.09  ? 81  GLU A OE2 1 
ATOM   602  N  N   . SER A  1 96  ? 30.945  23.756  68.364  1.00 34.32  ? 82  SER A N   1 
ATOM   603  C  CA  . SER A  1 96  ? 31.691  24.889  67.836  1.00 31.16  ? 82  SER A CA  1 
ATOM   604  C  C   . SER A  1 96  ? 31.214  25.211  66.422  1.00 30.29  ? 82  SER A C   1 
ATOM   605  O  O   . SER A  1 96  ? 31.034  26.375  66.070  1.00 29.94  ? 82  SER A O   1 
ATOM   606  C  CB  . SER A  1 96  ? 33.181  24.627  67.865  1.00 32.67  ? 82  SER A CB  1 
ATOM   607  O  OG  . SER A  1 96  ? 33.497  23.396  67.228  1.00 33.86  ? 82  SER A OG  1 
ATOM   608  N  N   . THR A  1 97  ? 31.014  24.158  65.622  1.00 32.11  ? 83  THR A N   1 
ATOM   609  C  CA  . THR A  1 97  ? 30.590  24.303  64.239  1.00 34.78  ? 83  THR A CA  1 
ATOM   610  C  C   . THR A  1 97  ? 29.125  24.736  64.207  1.00 31.01  ? 83  THR A C   1 
ATOM   611  O  O   . THR A  1 97  ? 28.755  25.623  63.440  1.00 31.69  ? 83  THR A O   1 
ATOM   612  C  CB  . THR A  1 97  ? 30.806  22.994  63.475  1.00 35.79  ? 83  THR A CB  1 
ATOM   613  O  OG1 . THR A  1 97  ? 32.142  22.574  63.743  1.00 34.55  ? 83  THR A OG1 1 
ATOM   614  C  CG2 . THR A  1 97  ? 30.602  23.156  61.979  1.00 37.75  ? 83  THR A CG2 1 
ATOM   615  N  N   . GLN A  1 98  ? 28.295  24.102  65.045  1.00 31.22  ? 84  GLN A N   1 
ATOM   616  C  CA  . GLN A  1 98  ? 26.872  24.402  65.095  1.00 33.14  ? 84  GLN A CA  1 
ATOM   617  C  C   . GLN A  1 98  ? 26.661  25.889  65.380  1.00 31.80  ? 84  GLN A C   1 
ATOM   618  O  O   . GLN A  1 98  ? 25.701  26.482  64.892  1.00 37.05  ? 84  GLN A O   1 
ATOM   619  C  CB  . GLN A  1 98  ? 26.147  23.571  66.156  1.00 30.65  ? 84  GLN A CB  1 
ATOM   620  C  CG  . GLN A  1 98  ? 26.088  22.074  65.867  1.00 31.57  ? 84  GLN A CG  1 
ATOM   621  C  CD  . GLN A  1 98  ? 25.066  21.364  66.728  1.00 32.20  ? 84  GLN A CD  1 
ATOM   622  O  OE1 . GLN A  1 98  ? 24.133  21.983  67.253  1.00 34.67  ? 84  GLN A OE1 1 
ATOM   623  N  NE2 . GLN A  1 98  ? 25.217  20.054  66.866  1.00 28.85  ? 84  GLN A NE2 1 
ATOM   624  N  N   . GLN A  1 99  ? 27.567  26.484  66.166  1.00 34.60  ? 85  GLN A N   1 
ATOM   625  C  CA  . GLN A  1 99  ? 27.385  27.843  66.657  1.00 35.23  ? 85  GLN A CA  1 
ATOM   626  C  C   . GLN A  1 99  ? 27.979  28.865  65.684  1.00 32.14  ? 85  GLN A C   1 
ATOM   627  O  O   . GLN A  1 99  ? 27.578  30.028  65.695  1.00 30.84  ? 85  GLN A O   1 
ATOM   628  C  CB  . GLN A  1 99  ? 27.962  27.991  68.068  1.00 38.88  ? 85  GLN A CB  1 
ATOM   629  C  CG  . GLN A  1 99  ? 27.142  27.286  69.147  1.00 41.14  ? 85  GLN A CG  1 
ATOM   630  C  CD  . GLN A  1 99  ? 27.484  27.726  70.555  1.00 41.25  ? 85  GLN A CD  1 
ATOM   631  O  OE1 . GLN A  1 99  ? 27.175  27.041  71.537  1.00 47.38  ? 85  GLN A OE1 1 
ATOM   632  N  NE2 . GLN A  1 99  ? 28.136  28.873  70.670  1.00 38.45  ? 85  GLN A NE2 1 
ATOM   633  N  N   . MET A  1 100 ? 28.932  28.442  64.842  1.00 31.73  ? 86  MET A N   1 
ATOM   634  C  CA  . MET A  1 100 ? 29.538  29.346  63.872  1.00 30.91  ? 86  MET A CA  1 
ATOM   635  C  C   . MET A  1 100 ? 28.804  29.245  62.533  1.00 26.60  ? 86  MET A C   1 
ATOM   636  O  O   . MET A  1 100 ? 28.764  30.213  61.778  1.00 26.86  ? 86  MET A O   1 
ATOM   637  C  CB  . MET A  1 100 ? 31.031  29.045  63.671  1.00 37.29  ? 86  MET A CB  1 
ATOM   638  C  CG  . MET A  1 100 ? 31.895  30.291  63.500  1.00 42.00  ? 86  MET A CG  1 
ATOM   639  S  SD  . MET A  1 100 ? 33.668  29.989  63.648  1.00 48.95  ? 86  MET A SD  1 
ATOM   640  C  CE  . MET A  1 100 ? 33.840  29.717  65.417  1.00 52.44  ? 86  MET A CE  1 
ATOM   641  N  N   . PHE A  1 101 ? 28.218  28.072  62.248  1.00 26.50  ? 87  PHE A N   1 
ATOM   642  C  CA  . PHE A  1 101 ? 27.578  27.824  60.964  1.00 28.26  ? 87  PHE A CA  1 
ATOM   643  C  C   . PHE A  1 101 ? 26.210  27.169  61.165  1.00 28.22  ? 87  PHE A C   1 
ATOM   644  O  O   . PHE A  1 101 ? 25.925  26.142  60.554  1.00 28.03  ? 87  PHE A O   1 
ATOM   645  C  CB  . PHE A  1 101 ? 28.470  26.926  60.096  1.00 30.78  ? 87  PHE A CB  1 
ATOM   646  C  CG  . PHE A  1 101 ? 29.886  27.443  59.876  1.00 31.68  ? 87  PHE A CG  1 
ATOM   647  C  CD1 . PHE A  1 101 ? 30.135  28.488  58.992  1.00 34.50  ? 87  PHE A CD1 1 
ATOM   648  C  CD2 . PHE A  1 101 ? 30.967  26.872  60.540  1.00 38.40  ? 87  PHE A CD2 1 
ATOM   649  C  CE1 . PHE A  1 101 ? 31.427  28.954  58.792  1.00 35.66  ? 87  PHE A CE1 1 
ATOM   650  C  CE2 . PHE A  1 101 ? 32.258  27.340  60.332  1.00 36.39  ? 87  PHE A CE2 1 
ATOM   651  C  CZ  . PHE A  1 101 ? 32.484  28.380  59.461  1.00 32.92  ? 87  PHE A CZ  1 
ATOM   652  N  N   . PRO A  1 102 ? 25.304  27.747  61.988  1.00 28.11  ? 88  PRO A N   1 
ATOM   653  C  CA  . PRO A  1 102 ? 24.025  27.098  62.301  1.00 27.15  ? 88  PRO A CA  1 
ATOM   654  C  C   . PRO A  1 102 ? 23.145  26.875  61.072  1.00 26.59  ? 88  PRO A C   1 
ATOM   655  O  O   . PRO A  1 102 ? 22.970  27.781  60.260  1.00 26.19  ? 88  PRO A O   1 
ATOM   656  C  CB  . PRO A  1 102 ? 23.366  28.065  63.306  1.00 25.08  ? 88  PRO A CB  1 
ATOM   657  C  CG  . PRO A  1 102 ? 24.008  29.405  63.007  1.00 28.07  ? 88  PRO A CG  1 
ATOM   658  C  CD  . PRO A  1 102 ? 25.442  29.069  62.619  1.00 28.23  ? 88  PRO A CD  1 
ATOM   659  N  N   . TRP A  1 103 ? 22.587  25.663  60.961  1.00 29.70  ? 89  TRP A N   1 
ATOM   660  C  CA  . TRP A  1 103 ? 21.689  25.303  59.873  1.00 29.57  ? 89  TRP A CA  1 
ATOM   661  C  C   . TRP A  1 103 ? 20.254  25.219  60.396  1.00 33.48  ? 89  TRP A C   1 
ATOM   662  O  O   . TRP A  1 103 ? 19.989  24.517  61.369  1.00 33.71  ? 89  TRP A O   1 
ATOM   663  C  CB  . TRP A  1 103 ? 22.143  23.974  59.246  1.00 27.61  ? 89  TRP A CB  1 
ATOM   664  C  CG  . TRP A  1 103 ? 21.278  23.459  58.123  1.00 26.49  ? 89  TRP A CG  1 
ATOM   665  C  CD1 . TRP A  1 103 ? 20.839  24.148  57.029  1.00 27.19  ? 89  TRP A CD1 1 
ATOM   666  C  CD2 . TRP A  1 103 ? 20.750  22.118  57.991  1.00 27.71  ? 89  TRP A CD2 1 
ATOM   667  N  NE1 . TRP A  1 103 ? 20.080  23.335  56.229  1.00 26.53  ? 89  TRP A NE1 1 
ATOM   668  C  CE2 . TRP A  1 103 ? 20.006  22.086  56.791  1.00 27.43  ? 89  TRP A CE2 1 
ATOM   669  C  CE3 . TRP A  1 103 ? 20.830  20.953  58.764  1.00 27.18  ? 89  TRP A CE3 1 
ATOM   670  C  CZ2 . TRP A  1 103 ? 19.354  20.934  56.354  1.00 29.83  ? 89  TRP A CZ2 1 
ATOM   671  C  CZ3 . TRP A  1 103 ? 20.186  19.815  58.329  1.00 30.47  ? 89  TRP A CZ3 1 
ATOM   672  C  CH2 . TRP A  1 103 ? 19.460  19.808  57.138  1.00 30.59  ? 89  TRP A CH2 1 
ATOM   673  N  N   . THR A  1 104 ? 19.337  25.950  59.747  1.00 40.78  ? 90  THR A N   1 
ATOM   674  C  CA  . THR A  1 104 ? 17.922  25.935  60.100  1.00 41.80  ? 90  THR A CA  1 
ATOM   675  C  C   . THR A  1 104 ? 17.125  25.324  58.948  1.00 40.83  ? 90  THR A C   1 
ATOM   676  O  O   . THR A  1 104 ? 17.195  25.813  57.823  1.00 44.75  ? 90  THR A O   1 
ATOM   677  C  CB  . THR A  1 104 ? 17.435  27.349  60.427  1.00 37.75  ? 90  THR A CB  1 
ATOM   678  O  OG1 . THR A  1 104 ? 17.822  28.174  59.332  1.00 42.68  ? 90  THR A OG1 1 
ATOM   679  C  CG2 . THR A  1 104 ? 18.027  27.898  61.712  1.00 35.09  ? 90  THR A CG2 1 
ATOM   680  N  N   . ALA A  1 105 ? 16.366  24.255  59.235  1.00 40.34  ? 91  ALA A N   1 
ATOM   681  C  CA  . ALA A  1 105 ? 15.620  23.548  58.204  1.00 40.53  ? 91  ALA A CA  1 
ATOM   682  C  C   . ALA A  1 105 ? 14.407  22.824  58.791  1.00 38.43  ? 91  ALA A C   1 
ATOM   683  O  O   . ALA A  1 105 ? 14.513  22.153  59.815  1.00 39.42  ? 91  ALA A O   1 
ATOM   684  C  CB  . ALA A  1 105 ? 16.541  22.577  57.493  1.00 44.15  ? 91  ALA A CB  1 
ATOM   685  N  N   . THR A  1 106 ? 13.256  22.961  58.116  1.00 38.99  ? 92  THR A N   1 
ATOM   686  C  CA  . THR A  1 106 ? 12.073  22.160  58.405  1.00 40.98  ? 92  THR A CA  1 
ATOM   687  C  C   . THR A  1 106 ? 12.235  20.797  57.732  1.00 47.96  ? 92  THR A C   1 
ATOM   688  O  O   . THR A  1 106 ? 13.035  20.654  56.809  1.00 42.96  ? 92  THR A O   1 
ATOM   689  C  CB  . THR A  1 106 ? 10.805  22.878  57.933  1.00 42.83  ? 92  THR A CB  1 
ATOM   690  O  OG1 . THR A  1 106 ? 11.000  23.172  56.552  1.00 44.29  ? 92  THR A OG1 1 
ATOM   691  C  CG2 . THR A  1 106 ? 10.528  24.161  58.697  1.00 42.74  ? 92  THR A CG2 1 
ATOM   692  N  N   . GLU A  1 107 ? 11.473  19.801  58.205  1.00 43.30  ? 93  GLU A N   1 
ATOM   693  C  CA  . GLU A  1 107 ? 11.577  18.438  57.704  1.00 46.04  ? 93  GLU A CA  1 
ATOM   694  C  C   . GLU A  1 107 ? 11.378  18.420  56.189  1.00 43.83  ? 93  GLU A C   1 
ATOM   695  O  O   . GLU A  1 107 ? 11.917  17.552  55.505  1.00 43.58  ? 93  GLU A O   1 
ATOM   696  C  CB  . GLU A  1 107 ? 10.574  17.509  58.392  1.00 52.03  ? 93  GLU A CB  1 
ATOM   697  C  CG  . GLU A  1 107 ? 10.999  17.077  59.793  1.00 58.53  ? 93  GLU A CG  1 
ATOM   698  C  CD  . GLU A  1 107 ? 10.049  16.103  60.467  1.00 64.30  ? 93  GLU A CD  1 
ATOM   699  O  OE1 . GLU A  1 107 ? 9.049   15.712  59.829  1.00 61.72  ? 93  GLU A OE1 1 
ATOM   700  O  OE2 . GLU A  1 107 ? 10.308  15.737  61.633  1.00 75.49  ? 93  GLU A OE2 1 
ATOM   701  N  N   . GLU A  1 108 ? 10.603  19.381  55.673  1.00 40.13  ? 94  GLU A N   1 
ATOM   702  C  CA  . GLU A  1 108 ? 10.289  19.432  54.253  1.00 45.76  ? 94  GLU A CA  1 
ATOM   703  C  C   . GLU A  1 108 ? 11.544  19.790  53.456  1.00 41.47  ? 94  GLU A C   1 
ATOM   704  O  O   . GLU A  1 108 ? 11.625  19.507  52.262  1.00 34.24  ? 94  GLU A O   1 
ATOM   705  C  CB  . GLU A  1 108 ? 9.158   20.427  53.981  1.00 46.90  ? 94  GLU A CB  1 
ATOM   706  C  CG  . GLU A  1 108 ? 9.538   21.877  54.266  1.00 57.48  ? 94  GLU A CG  1 
ATOM   707  C  CD  . GLU A  1 108 ? 8.386   22.862  54.168  1.00 64.51  ? 94  GLU A CD  1 
ATOM   708  O  OE1 . GLU A  1 108 ? 7.262   22.425  53.840  1.00 61.99  ? 94  GLU A OE1 1 
ATOM   709  O  OE2 . GLU A  1 108 ? 8.609   24.065  54.423  1.00 68.58  ? 94  GLU A OE2 1 
ATOM   710  N  N   . CYS A  1 109 ? 12.521  20.413  54.129  1.00 41.90  ? 95  CYS A N   1 
ATOM   711  C  CA  . CYS A  1 109 ? 13.744  20.871  53.484  1.00 41.03  ? 95  CYS A CA  1 
ATOM   712  C  C   . CYS A  1 109 ? 14.757  19.730  53.368  1.00 38.34  ? 95  CYS A C   1 
ATOM   713  O  O   . CYS A  1 109 ? 15.659  19.788  52.536  1.00 37.57  ? 95  CYS A O   1 
ATOM   714  C  CB  . CYS A  1 109 ? 14.365  22.047  54.232  1.00 37.50  ? 95  CYS A CB  1 
ATOM   715  S  SG  . CYS A  1 109 ? 13.452  23.604  54.051  1.00 38.99  ? 95  CYS A SG  1 
ATOM   716  N  N   . TYR A  1 110 ? 14.608  18.698  54.208  1.00 36.04  ? 96  TYR A N   1 
ATOM   717  C  CA  . TYR A  1 110 ? 15.518  17.562  54.193  1.00 38.04  ? 96  TYR A CA  1 
ATOM   718  C  C   . TYR A  1 110 ? 15.537  16.968  52.784  1.00 41.95  ? 96  TYR A C   1 
ATOM   719  O  O   . TYR A  1 110 ? 14.492  16.833  52.152  1.00 34.59  ? 96  TYR A O   1 
ATOM   720  C  CB  . TYR A  1 110 ? 15.120  16.520  55.246  1.00 40.02  ? 96  TYR A CB  1 
ATOM   721  C  CG  . TYR A  1 110 ? 15.201  16.981  56.697  1.00 43.04  ? 96  TYR A CG  1 
ATOM   722  C  CD1 . TYR A  1 110 ? 15.826  18.174  57.045  1.00 40.76  ? 96  TYR A CD1 1 
ATOM   723  C  CD2 . TYR A  1 110 ? 14.667  16.208  57.724  1.00 46.95  ? 96  TYR A CD2 1 
ATOM   724  C  CE1 . TYR A  1 110 ? 15.903  18.590  58.364  1.00 41.83  ? 96  TYR A CE1 1 
ATOM   725  C  CE2 . TYR A  1 110 ? 14.740  16.612  59.047  1.00 44.77  ? 96  TYR A CE2 1 
ATOM   726  C  CZ  . TYR A  1 110 ? 15.359  17.807  59.367  1.00 40.99  ? 96  TYR A CZ  1 
ATOM   727  O  OH  . TYR A  1 110 ? 15.431  18.205  60.671  1.00 42.09  ? 96  TYR A OH  1 
ATOM   728  N  N   . LEU A  1 111 ? 16.736  16.607  52.305  1.00 40.37  ? 97  LEU A N   1 
ATOM   729  C  CA  . LEU A  1 111 ? 16.925  16.193  50.923  1.00 40.53  ? 97  LEU A CA  1 
ATOM   730  C  C   . LEU A  1 111 ? 16.026  14.999  50.596  1.00 36.48  ? 97  LEU A C   1 
ATOM   731  O  O   . LEU A  1 111 ? 15.366  14.989  49.560  1.00 35.48  ? 97  LEU A O   1 
ATOM   732  C  CB  . LEU A  1 111 ? 18.398  15.871  50.662  1.00 41.42  ? 97  LEU A CB  1 
ATOM   733  C  CG  . LEU A  1 111 ? 18.757  15.515  49.215  1.00 41.01  ? 97  LEU A CG  1 
ATOM   734  C  CD1 . LEU A  1 111 ? 18.465  16.685  48.286  1.00 40.52  ? 97  LEU A CD1 1 
ATOM   735  C  CD2 . LEU A  1 111 ? 20.211  15.080  49.087  1.00 38.25  ? 97  LEU A CD2 1 
ATOM   736  N  N   A HIS A  1 112 ? 16.020  14.000  51.486  0.80 36.54  ? 98  HIS A N   1 
ATOM   737  N  N   C HIS A  1 112 ? 16.011  13.998  51.485  0.20 35.58  ? 98  HIS A N   1 
ATOM   738  C  CA  A HIS A  1 112 ? 15.255  12.778  51.283  0.68 38.14  ? 98  HIS A CA  1 
ATOM   739  C  CA  C HIS A  1 112 ? 15.254  12.775  51.254  0.32 35.13  ? 98  HIS A CA  1 
ATOM   740  C  C   A HIS A  1 112 ? 13.787  13.121  51.029  0.80 38.69  ? 98  HIS A C   1 
ATOM   741  C  C   C HIS A  1 112 ? 13.778  13.110  51.039  0.20 37.45  ? 98  HIS A C   1 
ATOM   742  O  O   A HIS A  1 112 ? 13.114  12.448  50.250  0.80 38.39  ? 98  HIS A O   1 
ATOM   743  O  O   C HIS A  1 112 ? 13.088  12.417  50.293  0.20 38.17  ? 98  HIS A O   1 
ATOM   744  C  CB  A HIS A  1 112 ? 15.401  11.836  52.487  0.68 43.01  ? 98  HIS A CB  1 
ATOM   745  C  CB  C HIS A  1 112 ? 15.467  11.765  52.391  0.32 34.58  ? 98  HIS A CB  1 
ATOM   746  C  CG  A HIS A  1 112 ? 14.996  10.418  52.227  0.68 48.53  ? 98  HIS A CG  1 
ATOM   747  C  CG  C HIS A  1 112 ? 14.944  12.196  53.723  0.32 33.46  ? 98  HIS A CG  1 
ATOM   748  N  ND1 A HIS A  1 112 ? 13.709  10.037  51.911  0.68 55.94  ? 98  HIS A ND1 1 
ATOM   749  N  ND1 C HIS A  1 112 ? 13.786  11.688  54.273  0.32 31.70  ? 98  HIS A ND1 1 
ATOM   750  C  CD2 A HIS A  1 112 ? 15.725  9.291   52.219  0.68 54.60  ? 98  HIS A CD2 1 
ATOM   751  C  CD2 C HIS A  1 112 ? 15.432  13.059  54.624  0.32 33.99  ? 98  HIS A CD2 1 
ATOM   752  C  CE1 A HIS A  1 112 ? 13.671  8.723   51.733  0.68 52.53  ? 98  HIS A CE1 1 
ATOM   753  C  CE1 C HIS A  1 112 ? 13.583  12.244  55.459  0.32 31.54  ? 98  HIS A CE1 1 
ATOM   754  N  NE2 A HIS A  1 112 ? 14.884  8.249   51.918  0.68 49.31  ? 98  HIS A NE2 1 
ATOM   755  N  NE2 C HIS A  1 112 ? 14.571  13.081  55.691  0.32 34.62  ? 98  HIS A NE2 1 
ATOM   756  N  N   . ASN A  1 113 ? 13.303  14.177  51.692  1.00 39.53  ? 99  ASN A N   1 
ATOM   757  C  CA  . ASN A  1 113 ? 11.903  14.569  51.612  1.00 42.55  ? 99  ASN A CA  1 
ATOM   758  C  C   . ASN A  1 113 ? 11.642  15.324  50.307  1.00 43.00  ? 99  ASN A C   1 
ATOM   759  O  O   . ASN A  1 113 ? 10.611  15.117  49.672  1.00 38.20  ? 99  ASN A O   1 
ATOM   760  C  CB  . ASN A  1 113 ? 11.459  15.355  52.845  1.00 39.17  ? 99  ASN A CB  1 
ATOM   761  C  CG  . ASN A  1 113 ? 11.317  14.475  54.066  1.00 41.79  ? 99  ASN A CG  1 
ATOM   762  O  OD1 . ASN A  1 113 ? 10.779  13.366  53.973  1.00 44.19  ? 99  ASN A OD1 1 
ATOM   763  N  ND2 . ASN A  1 113 ? 11.802  14.936  55.210  1.00 42.58  ? 99  ASN A ND2 1 
ATOM   764  N  N   . ARG A  1 114 ? 12.578  16.197  49.910  1.00 42.06  ? 100 ARG A N   1 
ATOM   765  C  CA  . ARG A  1 114 ? 12.447  16.944  48.666  1.00 42.78  ? 100 ARG A CA  1 
ATOM   766  C  C   . ARG A  1 114 ? 12.373  15.967  47.493  1.00 40.79  ? 100 ARG A C   1 
ATOM   767  O  O   . ARG A  1 114 ? 11.587  16.162  46.569  1.00 41.50  ? 100 ARG A O   1 
ATOM   768  C  CB  . ARG A  1 114 ? 13.603  17.936  48.476  1.00 41.04  ? 100 ARG A CB  1 
ATOM   769  C  CG  . ARG A  1 114 ? 13.574  19.139  49.409  1.00 41.77  ? 100 ARG A CG  1 
ATOM   770  C  CD  . ARG A  1 114 ? 12.417  20.087  49.122  1.00 43.65  ? 100 ARG A CD  1 
ATOM   771  N  NE  . ARG A  1 114 ? 12.440  21.256  50.009  1.00 44.21  ? 100 ARG A NE  1 
ATOM   772  C  CZ  . ARG A  1 114 ? 11.393  22.030  50.273  1.00 46.04  ? 100 ARG A CZ  1 
ATOM   773  N  NH1 . ARG A  1 114 ? 10.216  21.764  49.733  1.00 48.80  ? 100 ARG A NH1 1 
ATOM   774  N  NH2 . ARG A  1 114 ? 11.525  23.060  51.088  1.00 46.87  ? 100 ARG A NH2 1 
ATOM   775  N  N   . LEU A  1 115 ? 13.202  14.918  47.544  1.00 44.07  ? 101 LEU A N   1 
ATOM   776  C  CA  . LEU A  1 115 ? 13.246  13.912  46.494  1.00 42.62  ? 101 LEU A CA  1 
ATOM   777  C  C   . LEU A  1 115 ? 11.945  13.110  46.513  1.00 43.48  ? 101 LEU A C   1 
ATOM   778  O  O   . LEU A  1 115 ? 11.344  12.873  45.467  1.00 42.81  ? 101 LEU A O   1 
ATOM   779  C  CB  . LEU A  1 115 ? 14.471  13.015  46.682  1.00 36.19  ? 101 LEU A CB  1 
ATOM   780  C  CG  . LEU A  1 115 ? 15.826  13.616  46.285  1.00 36.68  ? 101 LEU A CG  1 
ATOM   781  C  CD1 . LEU A  1 115 ? 16.969  12.691  46.675  1.00 32.28  ? 101 LEU A CD1 1 
ATOM   782  C  CD2 . LEU A  1 115 ? 15.881  13.922  44.797  1.00 35.34  ? 101 LEU A CD2 1 
ATOM   783  N  N   . GLU A  1 116 ? 11.524  12.699  47.716  1.00 41.93  ? 102 GLU A N   1 
ATOM   784  C  CA  . GLU A  1 116 ? 10.274  11.976  47.908  1.00 47.18  ? 102 GLU A CA  1 
ATOM   785  C  C   . GLU A  1 116 ? 9.121   12.755  47.276  1.00 43.67  ? 102 GLU A C   1 
ATOM   786  O  O   . GLU A  1 116 ? 8.274   12.173  46.602  1.00 47.89  ? 102 GLU A O   1 
ATOM   787  C  CB  . GLU A  1 116 ? 10.028  11.711  49.396  1.00 49.87  ? 102 GLU A CB  1 
ATOM   788  C  CG  . GLU A  1 116 ? 8.690   11.039  49.693  1.00 52.86  ? 102 GLU A CG  1 
ATOM   789  C  CD  . GLU A  1 116 ? 8.642   10.285  51.012  1.00 58.43  ? 102 GLU A CD  1 
ATOM   790  O  OE1 . GLU A  1 116 ? 9.096   10.842  52.035  1.00 64.93  ? 102 GLU A OE1 1 
ATOM   791  O  OE2 . GLU A  1 116 ? 8.138   9.142   51.019  1.00 72.29  ? 102 GLU A OE2 1 
ATOM   792  N  N   . GLN A  1 117 ? 9.096   14.075  47.501  1.00 45.12  ? 103 GLN A N   1 
ATOM   793  C  CA  . GLN A  1 117 ? 8.060   14.934  46.947  1.00 47.15  ? 103 GLN A CA  1 
ATOM   794  C  C   . GLN A  1 117 ? 8.043   14.807  45.425  1.00 47.83  ? 103 GLN A C   1 
ATOM   795  O  O   . GLN A  1 117 ? 6.985   14.890  44.805  1.00 53.29  ? 103 GLN A O   1 
ATOM   796  C  CB  . GLN A  1 117 ? 8.284   16.395  47.340  1.00 48.17  ? 103 GLN A CB  1 
ATOM   797  C  CG  . GLN A  1 117 ? 8.137   16.681  48.831  1.00 53.81  ? 103 GLN A CG  1 
ATOM   798  C  CD  . GLN A  1 117 ? 8.861   17.941  49.258  1.00 55.45  ? 103 GLN A CD  1 
ATOM   799  O  OE1 . GLN A  1 117 ? 8.875   18.950  48.543  1.00 43.18  ? 103 GLN A OE1 1 
ATOM   800  N  NE2 . GLN A  1 117 ? 9.493   17.887  50.422  1.00 50.03  ? 103 GLN A NE2 1 
ATOM   801  N  N   . LEU A  1 118 ? 9.229   14.615  44.834  1.00 50.09  ? 104 LEU A N   1 
ATOM   802  C  CA  . LEU A  1 118 ? 9.379   14.535  43.389  1.00 48.15  ? 104 LEU A CA  1 
ATOM   803  C  C   . LEU A  1 118 ? 9.197   13.089  42.930  1.00 41.88  ? 104 LEU A C   1 
ATOM   804  O  O   . LEU A  1 118 ? 9.376   12.782  41.753  1.00 38.66  ? 104 LEU A O   1 
ATOM   805  C  CB  . LEU A  1 118 ? 10.750  15.080  42.980  1.00 44.77  ? 104 LEU A CB  1 
ATOM   806  C  CG  . LEU A  1 118 ? 10.983  16.578  43.212  1.00 41.61  ? 104 LEU A CG  1 
ATOM   807  C  CD1 . LEU A  1 118 ? 12.340  17.021  42.678  1.00 39.00  ? 104 LEU A CD1 1 
ATOM   808  C  CD2 . LEU A  1 118 ? 9.867   17.402  42.587  1.00 42.22  ? 104 LEU A CD2 1 
ATOM   809  N  N   . LYS A  1 119 ? 8.846   12.207  43.873  1.00 40.25  ? 105 LYS A N   1 
ATOM   810  C  CA  . LYS A  1 119 ? 8.656   10.792  43.587  1.00 45.20  ? 105 LYS A CA  1 
ATOM   811  C  C   . LYS A  1 119 ? 9.958   10.199  43.047  1.00 41.24  ? 105 LYS A C   1 
ATOM   812  O  O   . LYS A  1 119 ? 9.935   9.405   42.110  1.00 41.65  ? 105 LYS A O   1 
ATOM   813  C  CB  . LYS A  1 119 ? 7.482   10.592  42.618  1.00 54.27  ? 105 LYS A CB  1 
ATOM   814  C  CG  . LYS A  1 119 ? 6.100   10.919  43.188  1.00 57.08  ? 105 LYS A CG  1 
ATOM   815  C  CD  . LYS A  1 119 ? 4.995   11.052  42.144  1.00 64.05  ? 105 LYS A CD  1 
ATOM   816  C  CE  . LYS A  1 119 ? 3.711   11.580  42.720  1.00 71.64  ? 105 LYS A CE  1 
ATOM   817  N  NZ  . LYS A  1 119 ? 3.079   12.564  41.834  1.00 76.96  ? 105 LYS A NZ  1 
ATOM   818  N  N   . VAL A  1 120 ? 11.089  10.593  43.650  1.00 40.64  ? 106 VAL A N   1 
ATOM   819  C  CA  . VAL A  1 120 ? 12.392  10.043  43.303  1.00 37.45  ? 106 VAL A CA  1 
ATOM   820  C  C   . VAL A  1 120 ? 12.982  9.368   44.541  1.00 34.00  ? 106 VAL A C   1 
ATOM   821  O  O   . VAL A  1 120 ? 13.046  9.975   45.607  1.00 34.06  ? 106 VAL A O   1 
ATOM   822  C  CB  . VAL A  1 120 ? 13.353  11.117  42.750  1.00 36.31  ? 106 VAL A CB  1 
ATOM   823  C  CG1 . VAL A  1 120 ? 14.727  10.541  42.420  1.00 36.34  ? 106 VAL A CG1 1 
ATOM   824  C  CG2 . VAL A  1 120 ? 12.771  11.834  41.536  1.00 37.84  ? 106 VAL A CG2 1 
ATOM   825  N  N   . ARG A  1 121 ? 13.401  8.105   44.386  1.00 39.38  ? 107 ARG A N   1 
ATOM   826  C  CA  . ARG A  1 121 ? 14.078  7.369   45.443  1.00 47.78  ? 107 ARG A CA  1 
ATOM   827  C  C   . ARG A  1 121 ? 15.586  7.591   45.332  1.00 44.89  ? 107 ARG A C   1 
ATOM   828  O  O   . ARG A  1 121 ? 16.127  7.656   44.230  1.00 43.65  ? 107 ARG A O   1 
ATOM   829  C  CB  . ARG A  1 121 ? 13.780  5.867   45.347  1.00 59.23  ? 107 ARG A CB  1 
ATOM   830  C  CG  . ARG A  1 121 ? 12.303  5.498   45.382  1.00 67.27  ? 107 ARG A CG  1 
ATOM   831  C  CD  . ARG A  1 121 ? 12.053  4.056   44.959  1.00 74.21  ? 107 ARG A CD  1 
ATOM   832  N  NE  . ARG A  1 121 ? 12.728  3.086   45.830  1.00 82.21  ? 107 ARG A NE  1 
ATOM   833  C  CZ  . ARG A  1 121 ? 12.111  2.318   46.721  1.00 87.35  ? 107 ARG A CZ  1 
ATOM   834  N  NH1 . ARG A  1 121 ? 10.810  2.442   46.918  1.00 82.70  ? 107 ARG A NH1 1 
ATOM   835  N  NH2 . ARG A  1 121 ? 12.803  1.440   47.427  1.00 91.35  ? 107 ARG A NH2 1 
ATOM   836  N  N   . PRO A  1 122 ? 16.307  7.729   46.468  1.00 48.10  ? 108 PRO A N   1 
ATOM   837  C  CA  . PRO A  1 122 ? 17.771  7.728   46.466  1.00 46.03  ? 108 PRO A CA  1 
ATOM   838  C  C   . PRO A  1 122 ? 18.372  6.704   45.506  1.00 42.94  ? 108 PRO A C   1 
ATOM   839  O  O   . PRO A  1 122 ? 19.368  6.978   44.839  1.00 40.69  ? 108 PRO A O   1 
ATOM   840  C  CB  . PRO A  1 122 ? 18.137  7.381   47.923  1.00 47.33  ? 108 PRO A CB  1 
ATOM   841  C  CG  . PRO A  1 122 ? 16.911  7.728   48.753  1.00 51.12  ? 108 PRO A CG  1 
ATOM   842  C  CD  . PRO A  1 122 ? 15.739  7.934   47.808  1.00 49.93  ? 108 PRO A CD  1 
ATOM   843  N  N   A GLU A  1 123 ? 17.736  5.529   45.458  0.80 46.23  ? 109 GLU A N   1 
ATOM   844  N  N   B GLU A  1 123 ? 17.766  5.514   45.450  0.20 39.68  ? 109 GLU A N   1 
ATOM   845  C  CA  A GLU A  1 123 ? 18.243  4.387   44.716  0.80 50.10  ? 109 GLU A CA  1 
ATOM   846  C  CA  B GLU A  1 123 ? 18.327  4.408   44.691  0.20 37.76  ? 109 GLU A CA  1 
ATOM   847  C  C   A GLU A  1 123 ? 18.166  4.669   43.216  0.80 40.10  ? 109 GLU A C   1 
ATOM   848  C  C   B GLU A  1 123 ? 18.229  4.712   43.198  0.20 36.19  ? 109 GLU A C   1 
ATOM   849  O  O   A GLU A  1 123 ? 18.785  3.967   42.420  0.80 46.52  ? 109 GLU A O   1 
ATOM   850  O  O   B GLU A  1 123 ? 18.890  4.065   42.389  0.20 38.19  ? 109 GLU A O   1 
ATOM   851  C  CB  A GLU A  1 123 ? 17.460  3.127   45.098  0.80 61.33  ? 109 GLU A CB  1 
ATOM   852  C  CB  B GLU A  1 123 ? 17.618  3.089   45.007  0.20 36.65  ? 109 GLU A CB  1 
ATOM   853  C  CG  A GLU A  1 123 ? 17.562  2.750   46.575  0.80 68.83  ? 109 GLU A CG  1 
ATOM   854  C  CG  B GLU A  1 123 ? 16.502  2.747   44.023  0.20 34.68  ? 109 GLU A CG  1 
ATOM   855  C  CD  A GLU A  1 123 ? 16.600  3.479   47.499  0.80 73.66  ? 109 GLU A CD  1 
ATOM   856  C  CD  B GLU A  1 123 ? 15.708  1.501   44.376  0.20 33.22  ? 109 GLU A CD  1 
ATOM   857  O  OE1 A GLU A  1 123 ? 17.076  4.193   48.407  0.80 65.83  ? 109 GLU A OE1 1 
ATOM   858  O  OE1 B GLU A  1 123 ? 16.319  0.417   44.490  0.20 31.82  ? 109 GLU A OE1 1 
ATOM   859  O  OE2 A GLU A  1 123 ? 15.373  3.324   47.317  0.80 80.91  ? 109 GLU A OE2 1 
ATOM   860  O  OE2 B GLU A  1 123 ? 14.473  1.616   44.532  0.20 30.94  ? 109 GLU A OE2 1 
ATOM   861  N  N   . ASP A  1 124 ? 17.405  5.706   42.844  1.00 34.19  ? 110 ASP A N   1 
ATOM   862  C  CA  . ASP A  1 124 ? 17.183  6.057   41.448  1.00 36.97  ? 110 ASP A CA  1 
ATOM   863  C  C   . ASP A  1 124 ? 18.253  7.026   40.941  1.00 33.65  ? 110 ASP A C   1 
ATOM   864  O  O   . ASP A  1 124 ? 18.256  7.371   39.762  1.00 31.78  ? 110 ASP A O   1 
ATOM   865  C  CB  . ASP A  1 124 ? 15.800  6.656   41.229  1.00 42.88  ? 110 ASP A CB  1 
ATOM   866  C  CG  . ASP A  1 124 ? 14.624  5.741   41.545  1.00 49.41  ? 110 ASP A CG  1 
ATOM   867  O  OD1 . ASP A  1 124 ? 14.618  4.598   41.039  1.00 46.63  ? 110 ASP A OD1 1 
ATOM   868  O  OD2 . ASP A  1 124 ? 13.717  6.183   42.283  1.00 55.48  ? 110 ASP A OD2 1 
ATOM   869  N  N   . ILE A  1 125 ? 19.147  7.484   41.827  1.00 34.26  ? 111 ILE A N   1 
ATOM   870  C  CA  . ILE A  1 125 ? 20.185  8.427   41.433  1.00 32.82  ? 111 ILE A CA  1 
ATOM   871  C  C   . ILE A  1 125 ? 21.368  7.653   40.857  1.00 31.92  ? 111 ILE A C   1 
ATOM   872  O  O   . ILE A  1 125 ? 21.949  6.805   41.530  1.00 37.44  ? 111 ILE A O   1 
ATOM   873  C  CB  . ILE A  1 125 ? 20.620  9.325   42.607  1.00 33.22  ? 111 ILE A CB  1 
ATOM   874  C  CG1 . ILE A  1 125 ? 19.437  10.084  43.219  1.00 32.74  ? 111 ILE A CG1 1 
ATOM   875  C  CG2 . ILE A  1 125 ? 21.735  10.278  42.169  1.00 33.73  ? 111 ILE A CG2 1 
ATOM   876  C  CD1 . ILE A  1 125 ? 18.800  11.100  42.288  1.00 32.21  ? 111 ILE A CD1 1 
ATOM   877  N  N   . ARG A  1 126 ? 21.717  7.967   39.604  1.00 33.72  ? 112 ARG A N   1 
ATOM   878  C  CA  . ARG A  1 126 ? 22.822  7.317   38.918  1.00 34.95  ? 112 ARG A CA  1 
ATOM   879  C  C   . ARG A  1 126 ? 24.137  8.001   39.287  1.00 30.67  ? 112 ARG A C   1 
ATOM   880  O  O   . ARG A  1 126 ? 25.146  7.334   39.505  1.00 32.58  ? 112 ARG A O   1 
ATOM   881  C  CB  . ARG A  1 126 ? 22.608  7.364   37.401  1.00 33.35  ? 112 ARG A CB  1 
ATOM   882  C  CG  . ARG A  1 126 ? 23.503  6.404   36.631  1.00 38.81  ? 112 ARG A CG  1 
ATOM   883  C  CD  . ARG A  1 126 ? 23.331  6.519   35.128  1.00 43.72  ? 112 ARG A CD  1 
ATOM   884  N  NE  . ARG A  1 126 ? 24.281  5.646   34.433  1.00 50.91  ? 112 ARG A NE  1 
ATOM   885  C  CZ  . ARG A  1 126 ? 24.636  5.771   33.161  1.00 52.65  ? 112 ARG A CZ  1 
ATOM   886  N  NH1 . ARG A  1 126 ? 24.132  6.746   32.426  1.00 55.48  ? 112 ARG A NH1 1 
ATOM   887  N  NH2 . ARG A  1 126 ? 25.506  4.928   32.636  1.00 57.42  ? 112 ARG A NH2 1 
ATOM   888  N  N   . TYR A  1 127 ? 24.110  9.338   39.347  1.00 30.56  ? 113 TYR A N   1 
ATOM   889  C  CA  . TYR A  1 127 ? 25.306  10.131  39.592  1.00 29.87  ? 113 TYR A CA  1 
ATOM   890  C  C   . TYR A  1 127 ? 25.028  11.214  40.630  1.00 28.01  ? 113 TYR A C   1 
ATOM   891  O  O   . TYR A  1 127 ? 24.051  11.950  40.516  1.00 29.68  ? 113 TYR A O   1 
ATOM   892  C  CB  . TYR A  1 127 ? 25.804  10.812  38.314  1.00 29.88  ? 113 TYR A CB  1 
ATOM   893  C  CG  . TYR A  1 127 ? 26.328  9.858   37.249  1.00 30.84  ? 113 TYR A CG  1 
ATOM   894  C  CD1 . TYR A  1 127 ? 27.432  9.052   37.494  1.00 32.46  ? 113 TYR A CD1 1 
ATOM   895  C  CD2 . TYR A  1 127 ? 25.736  9.785   35.994  1.00 33.29  ? 113 TYR A CD2 1 
ATOM   896  C  CE1 . TYR A  1 127 ? 27.921  8.185   36.531  1.00 35.02  ? 113 TYR A CE1 1 
ATOM   897  C  CE2 . TYR A  1 127 ? 26.217  8.924   35.021  1.00 33.85  ? 113 TYR A CE2 1 
ATOM   898  C  CZ  . TYR A  1 127 ? 27.311  8.122   35.291  1.00 36.00  ? 113 TYR A CZ  1 
ATOM   899  O  OH  . TYR A  1 127 ? 27.797  7.272   34.339  1.00 35.79  ? 113 TYR A OH  1 
ATOM   900  N  N   . VAL A  1 128 ? 25.919  11.302  41.624  1.00 26.99  ? 114 VAL A N   1 
ATOM   901  C  CA  . VAL A  1 128 ? 25.974  12.433  42.535  1.00 25.73  ? 114 VAL A CA  1 
ATOM   902  C  C   . VAL A  1 128 ? 27.286  13.178  42.280  1.00 25.09  ? 114 VAL A C   1 
ATOM   903  O  O   . VAL A  1 128 ? 28.360  12.589  42.376  1.00 25.33  ? 114 VAL A O   1 
ATOM   904  C  CB  . VAL A  1 128 ? 25.869  11.979  44.006  1.00 26.42  ? 114 VAL A CB  1 
ATOM   905  C  CG1 . VAL A  1 128 ? 25.845  13.165  44.962  1.00 27.65  ? 114 VAL A CG1 1 
ATOM   906  C  CG2 . VAL A  1 128 ? 24.664  11.074  44.248  1.00 28.73  ? 114 VAL A CG2 1 
ATOM   907  N  N   . VAL A  1 129 ? 27.194  14.469  41.938  1.00 24.95  ? 115 VAL A N   1 
ATOM   908  C  CA  . VAL A  1 129 ? 28.382  15.293  41.765  1.00 22.90  ? 115 VAL A CA  1 
ATOM   909  C  C   . VAL A  1 129 ? 28.591  16.109  43.040  1.00 24.07  ? 115 VAL A C   1 
ATOM   910  O  O   . VAL A  1 129 ? 27.784  16.977  43.371  1.00 24.70  ? 115 VAL A O   1 
ATOM   911  C  CB  . VAL A  1 129 ? 28.306  16.201  40.520  1.00 23.15  ? 115 VAL A CB  1 
ATOM   912  C  CG1 . VAL A  1 129 ? 29.501  17.146  40.423  1.00 22.05  ? 115 VAL A CG1 1 
ATOM   913  C  CG2 . VAL A  1 129 ? 28.166  15.387  39.237  1.00 24.77  ? 115 VAL A CG2 1 
ATOM   914  N  N   . ALA A  1 130 ? 29.680  15.801  43.754  1.00 23.89  ? 116 ALA A N   1 
ATOM   915  C  CA  . ALA A  1 130 ? 30.062  16.534  44.950  1.00 22.88  ? 116 ALA A CA  1 
ATOM   916  C  C   . ALA A  1 130 ? 30.940  17.721  44.564  1.00 22.78  ? 116 ALA A C   1 
ATOM   917  O  O   . ALA A  1 130 ? 32.101  17.539  44.205  1.00 25.33  ? 116 ALA A O   1 
ATOM   918  C  CB  . ALA A  1 130 ? 30.778  15.608  45.910  1.00 21.95  ? 116 ALA A CB  1 
ATOM   919  N  N   . SER A  1 131 ? 30.375  18.934  44.638  1.00 21.90  ? 117 SER A N   1 
ATOM   920  C  CA  . SER A  1 131 ? 31.116  20.145  44.315  1.00 23.26  ? 117 SER A CA  1 
ATOM   921  C  C   . SER A  1 131 ? 32.363  20.223  45.192  1.00 22.35  ? 117 SER A C   1 
ATOM   922  O  O   . SER A  1 131 ? 33.430  20.639  44.743  1.00 25.24  ? 117 SER A O   1 
ATOM   923  C  CB  . SER A  1 131 ? 30.253  21.377  44.474  1.00 23.48  ? 117 SER A CB  1 
ATOM   924  O  OG  . SER A  1 131 ? 29.888  21.576  45.832  1.00 23.60  ? 117 SER A OG  1 
ATOM   925  N  N   . HIS A  1 132 ? 32.186  19.815  46.452  1.00 21.56  ? 118 HIS A N   1 
ATOM   926  C  CA  . HIS A  1 132 ? 33.257  19.675  47.427  1.00 22.23  ? 118 HIS A CA  1 
ATOM   927  C  C   . HIS A  1 132 ? 32.641  19.002  48.654  1.00 22.57  ? 118 HIS A C   1 
ATOM   928  O  O   . HIS A  1 132 ? 31.447  18.709  48.648  1.00 23.38  ? 118 HIS A O   1 
ATOM   929  C  CB  . HIS A  1 132 ? 33.975  21.012  47.663  1.00 24.00  ? 118 HIS A CB  1 
ATOM   930  C  CG  . HIS A  1 132 ? 33.155  22.084  48.306  1.00 23.53  ? 118 HIS A CG  1 
ATOM   931  N  ND1 . HIS A  1 132 ? 31.949  22.541  47.817  1.00 24.71  ? 118 HIS A ND1 1 
ATOM   932  C  CD2 . HIS A  1 132 ? 33.413  22.820  49.399  1.00 24.03  ? 118 HIS A CD2 1 
ATOM   933  C  CE1 . HIS A  1 132 ? 31.493  23.506  48.606  1.00 23.40  ? 118 HIS A CE1 1 
ATOM   934  N  NE2 . HIS A  1 132 ? 32.365  23.689  49.576  1.00 23.67  ? 118 HIS A NE2 1 
ATOM   935  N  N   . LEU A  1 133 ? 33.445  18.739  49.692  1.00 22.38  ? 119 LEU A N   1 
ATOM   936  C  CA  . LEU A  1 133 ? 33.009  17.859  50.767  1.00 22.23  ? 119 LEU A CA  1 
ATOM   937  C  C   . LEU A  1 133 ? 32.791  18.641  52.062  1.00 21.75  ? 119 LEU A C   1 
ATOM   938  O  O   . LEU A  1 133 ? 32.942  18.092  53.151  1.00 25.16  ? 119 LEU A O   1 
ATOM   939  C  CB  . LEU A  1 133 ? 34.027  16.731  50.938  1.00 20.87  ? 119 LEU A CB  1 
ATOM   940  C  CG  . LEU A  1 133 ? 34.155  15.773  49.749  1.00 20.96  ? 119 LEU A CG  1 
ATOM   941  C  CD1 . LEU A  1 133 ? 35.154  14.661  50.028  1.00 23.85  ? 119 LEU A CD1 1 
ATOM   942  C  CD2 . LEU A  1 133 ? 32.798  15.196  49.374  1.00 22.77  ? 119 LEU A CD2 1 
ATOM   943  N  N   . HIS A  1 134 ? 32.402  19.915  51.933  1.00 23.05  ? 120 HIS A N   1 
ATOM   944  C  CA  . HIS A  1 134 ? 32.061  20.743  53.081  1.00 24.03  ? 120 HIS A CA  1 
ATOM   945  C  C   . HIS A  1 134 ? 30.730  20.284  53.679  1.00 26.13  ? 120 HIS A C   1 
ATOM   946  O  O   . HIS A  1 134 ? 29.949  19.600  53.021  1.00 24.88  ? 120 HIS A O   1 
ATOM   947  C  CB  . HIS A  1 134 ? 32.024  22.228  52.699  1.00 24.89  ? 120 HIS A CB  1 
ATOM   948  C  CG  . HIS A  1 134 ? 33.344  22.924  52.796  1.00 25.64  ? 120 HIS A CG  1 
ATOM   949  N  ND1 . HIS A  1 134 ? 33.562  24.201  52.322  1.00 24.98  ? 120 HIS A ND1 1 
ATOM   950  C  CD2 . HIS A  1 134 ? 34.502  22.531  53.345  1.00 27.97  ? 120 HIS A CD2 1 
ATOM   951  C  CE1 . HIS A  1 134 ? 34.818  24.550  52.567  1.00 28.33  ? 120 HIS A CE1 1 
ATOM   952  N  NE2 . HIS A  1 134 ? 35.408  23.549  53.186  1.00 25.91  ? 120 HIS A NE2 1 
ATOM   953  N  N   . LEU A  1 135 ? 30.479  20.705  54.925  1.00 27.11  ? 121 LEU A N   1 
ATOM   954  C  CA  . LEU A  1 135 ? 29.383  20.194  55.736  1.00 29.25  ? 121 LEU A CA  1 
ATOM   955  C  C   . LEU A  1 135 ? 28.031  20.411  55.053  1.00 27.99  ? 121 LEU A C   1 
ATOM   956  O  O   . LEU A  1 135 ? 27.121  19.602  55.227  1.00 31.82  ? 121 LEU A O   1 
ATOM   957  C  CB  . LEU A  1 135 ? 29.434  20.847  57.120  1.00 29.10  ? 121 LEU A CB  1 
ATOM   958  C  CG  . LEU A  1 135 ? 29.110  22.344  57.189  1.00 30.39  ? 121 LEU A CG  1 
ATOM   959  C  CD1 . LEU A  1 135 ? 29.134  22.824  58.635  1.00 30.63  ? 121 LEU A CD1 1 
ATOM   960  C  CD2 . LEU A  1 135 ? 30.062  23.175  56.345  1.00 29.68  ? 121 LEU A CD2 1 
ATOM   961  N  N   . ASN A  1 136 ? 27.903  21.495  54.276  1.00 28.08  ? 122 ASN A N   1 
ATOM   962  C  CA  . ASN A  1 136 ? 26.616  21.889  53.719  1.00 28.62  ? 122 ASN A CA  1 
ATOM   963  C  C   . ASN A  1 136 ? 26.515  21.493  52.246  1.00 30.46  ? 122 ASN A C   1 
ATOM   964  O  O   . ASN A  1 136 ? 25.660  22.012  51.530  1.00 31.82  ? 122 ASN A O   1 
ATOM   965  C  CB  . ASN A  1 136 ? 26.345  23.381  53.907  1.00 30.29  ? 122 ASN A CB  1 
ATOM   966  C  CG  . ASN A  1 136 ? 27.491  24.250  53.442  1.00 32.27  ? 122 ASN A CG  1 
ATOM   967  O  OD1 . ASN A  1 136 ? 28.558  23.736  53.093  1.00 31.87  ? 122 ASN A OD1 1 
ATOM   968  N  ND2 . ASN A  1 136 ? 27.297  25.562  53.444  1.00 34.87  ? 122 ASN A ND2 1 
ATOM   969  N  N   . HIS A  1 137 ? 27.370  20.563  51.799  1.00 28.73  ? 123 HIS A N   1 
ATOM   970  C  CA  . HIS A  1 137 ? 27.331  20.107  50.417  1.00 26.14  ? 123 HIS A CA  1 
ATOM   971  C  C   . HIS A  1 137 ? 27.360  18.579  50.344  1.00 25.27  ? 123 HIS A C   1 
ATOM   972  O  O   . HIS A  1 137 ? 26.800  18.000  49.416  1.00 25.86  ? 123 HIS A O   1 
ATOM   973  C  CB  . HIS A  1 137 ? 28.456  20.751  49.594  1.00 27.88  ? 123 HIS A CB  1 
ATOM   974  C  CG  . HIS A  1 137 ? 28.296  22.226  49.401  1.00 24.62  ? 123 HIS A CG  1 
ATOM   975  N  ND1 . HIS A  1 137 ? 27.768  22.787  48.258  1.00 25.52  ? 123 HIS A ND1 1 
ATOM   976  C  CD2 . HIS A  1 137 ? 28.596  23.253  50.209  1.00 29.21  ? 123 HIS A CD2 1 
ATOM   977  C  CE1 . HIS A  1 137 ? 27.749  24.108  48.384  1.00 25.99  ? 123 HIS A CE1 1 
ATOM   978  N  NE2 . HIS A  1 137 ? 28.249  24.413  49.562  1.00 27.47  ? 123 HIS A NE2 1 
ATOM   979  N  N   . ALA A  1 138 ? 28.010  17.930  51.318  1.00 24.58  ? 124 ALA A N   1 
ATOM   980  C  CA  . ALA A  1 138 ? 28.227  16.490  51.268  1.00 24.36  ? 124 ALA A CA  1 
ATOM   981  C  C   . ALA A  1 138 ? 27.425  15.782  52.360  1.00 23.91  ? 124 ALA A C   1 
ATOM   982  O  O   . ALA A  1 138 ? 27.652  14.606  52.636  1.00 24.47  ? 124 ALA A O   1 
ATOM   983  C  CB  . ALA A  1 138 ? 29.707  16.192  51.392  1.00 24.30  ? 124 ALA A CB  1 
ATOM   984  N  N   . GLY A  1 139 ? 26.464  16.499  52.952  1.00 24.17  ? 125 GLY A N   1 
ATOM   985  C  CA  . GLY A  1 139 ? 25.765  16.044  54.145  1.00 27.39  ? 125 GLY A CA  1 
ATOM   986  C  C   . GLY A  1 139 ? 25.058  14.699  53.967  1.00 26.42  ? 125 GLY A C   1 
ATOM   987  O  O   . GLY A  1 139 ? 24.979  13.921  54.917  1.00 27.45  ? 125 GLY A O   1 
ATOM   988  N  N   . CYS A  1 140 ? 24.539  14.428  52.762  1.00 25.42  ? 126 CYS A N   1 
ATOM   989  C  CA  . CYS A  1 140 ? 23.666  13.280  52.555  1.00 28.62  ? 126 CYS A CA  1 
ATOM   990  C  C   . CYS A  1 140 ? 24.197  12.348  51.465  1.00 29.17  ? 126 CYS A C   1 
ATOM   991  O  O   . CYS A  1 140 ? 23.426  11.588  50.883  1.00 29.56  ? 126 CYS A O   1 
ATOM   992  C  CB  . CYS A  1 140 ? 22.252  13.716  52.184  1.00 29.97  ? 126 CYS A CB  1 
ATOM   993  S  SG  . CYS A  1 140 ? 21.483  14.816  53.402  1.00 32.27  ? 126 CYS A SG  1 
ATOM   994  N  N   . LEU A  1 141 ? 25.509  12.395  51.201  1.00 28.36  ? 127 LEU A N   1 
ATOM   995  C  CA  . LEU A  1 141 ? 26.129  11.471  50.263  1.00 27.63  ? 127 LEU A CA  1 
ATOM   996  C  C   . LEU A  1 141 ? 25.731  10.035  50.617  1.00 29.29  ? 127 LEU A C   1 
ATOM   997  O  O   . LEU A  1 141 ? 25.543  9.205   49.730  1.00 29.93  ? 127 LEU A O   1 
ATOM   998  C  CB  . LEU A  1 141 ? 27.651  11.638  50.272  1.00 28.29  ? 127 LEU A CB  1 
ATOM   999  C  CG  . LEU A  1 141 ? 28.212  12.909  49.622  1.00 28.96  ? 127 LEU A CG  1 
ATOM   1000 C  CD1 . LEU A  1 141 ? 29.737  12.906  49.647  1.00 28.81  ? 127 LEU A CD1 1 
ATOM   1001 C  CD2 . LEU A  1 141 ? 27.707  13.069  48.197  1.00 29.73  ? 127 LEU A CD2 1 
ATOM   1002 N  N   . GLU A  1 142 ? 25.597  9.755   51.920  1.00 31.23  ? 128 GLU A N   1 
ATOM   1003 C  CA  . GLU A  1 142 ? 25.487  8.390   52.418  1.00 32.45  ? 128 GLU A CA  1 
ATOM   1004 C  C   . GLU A  1 142 ? 24.175  7.747   51.964  1.00 33.94  ? 128 GLU A C   1 
ATOM   1005 O  O   . GLU A  1 142 ? 24.015  6.532   52.056  1.00 35.62  ? 128 GLU A O   1 
ATOM   1006 C  CB  . GLU A  1 142 ? 25.621  8.366   53.943  1.00 31.89  ? 128 GLU A CB  1 
ATOM   1007 C  CG  . GLU A  1 142 ? 24.417  8.942   54.685  1.00 32.73  ? 128 GLU A CG  1 
ATOM   1008 C  CD  . GLU A  1 142 ? 24.690  9.254   56.147  1.00 32.07  ? 128 GLU A CD  1 
ATOM   1009 O  OE1 . GLU A  1 142 ? 24.222  8.493   57.020  1.00 35.62  ? 128 GLU A OE1 1 
ATOM   1010 O  OE2 . GLU A  1 142 ? 25.369  10.267  56.417  1.00 32.61  ? 128 GLU A OE2 1 
ATOM   1011 N  N   . MET A  1 143 ? 23.248  8.570   51.461  1.00 32.50  ? 129 MET A N   1 
ATOM   1012 C  CA  . MET A  1 143 ? 21.934  8.108   51.035  1.00 37.37  ? 129 MET A CA  1 
ATOM   1013 C  C   . MET A  1 143 ? 22.044  7.309   49.739  1.00 38.52  ? 129 MET A C   1 
ATOM   1014 O  O   . MET A  1 143 ? 21.253  6.400   49.493  1.00 36.01  ? 129 MET A O   1 
ATOM   1015 C  CB  . MET A  1 143 ? 20.995  9.293   50.775  1.00 39.58  ? 129 MET A CB  1 
ATOM   1016 C  CG  . MET A  1 143 ? 20.229  9.774   51.989  1.00 40.92  ? 129 MET A CG  1 
ATOM   1017 S  SD  . MET A  1 143 ? 19.352  11.313  51.648  1.00 46.18  ? 129 MET A SD  1 
ATOM   1018 C  CE  . MET A  1 143 ? 18.201  10.777  50.374  1.00 49.79  ? 129 MET A CE  1 
ATOM   1019 N  N   . PHE A  1 144 ? 23.032  7.669   48.912  1.00 33.94  ? 130 PHE A N   1 
ATOM   1020 C  CA  . PHE A  1 144 ? 23.059  7.252   47.520  1.00 31.62  ? 130 PHE A CA  1 
ATOM   1021 C  C   . PHE A  1 144 ? 24.016  6.075   47.352  1.00 33.63  ? 130 PHE A C   1 
ATOM   1022 O  O   . PHE A  1 144 ? 25.129  6.230   46.852  1.00 36.91  ? 130 PHE A O   1 
ATOM   1023 C  CB  . PHE A  1 144 ? 23.398  8.481   46.670  1.00 32.31  ? 130 PHE A CB  1 
ATOM   1024 C  CG  . PHE A  1 144 ? 22.447  9.640   46.932  1.00 34.15  ? 130 PHE A CG  1 
ATOM   1025 C  CD1 . PHE A  1 144 ? 21.136  9.601   46.468  1.00 34.54  ? 130 PHE A CD1 1 
ATOM   1026 C  CD2 . PHE A  1 144 ? 22.853  10.748  47.667  1.00 33.16  ? 130 PHE A CD2 1 
ATOM   1027 C  CE1 . PHE A  1 144 ? 20.264  10.647  46.719  1.00 31.49  ? 130 PHE A CE1 1 
ATOM   1028 C  CE2 . PHE A  1 144 ? 21.976  11.792  47.915  1.00 34.45  ? 130 PHE A CE2 1 
ATOM   1029 C  CZ  . PHE A  1 144 ? 20.684  11.739  47.441  1.00 35.01  ? 130 PHE A CZ  1 
ATOM   1030 N  N   . THR A  1 145 ? 23.543  4.890   47.752  1.00 31.56  ? 131 THR A N   1 
ATOM   1031 C  CA  . THR A  1 145 ? 24.355  3.684   47.770  1.00 32.72  ? 131 THR A CA  1 
ATOM   1032 C  C   . THR A  1 145 ? 24.322  2.994   46.406  1.00 32.24  ? 131 THR A C   1 
ATOM   1033 O  O   . THR A  1 145 ? 25.023  2.007   46.200  1.00 33.64  ? 131 THR A O   1 
ATOM   1034 C  CB  . THR A  1 145 ? 23.866  2.745   48.876  1.00 35.31  ? 131 THR A CB  1 
ATOM   1035 O  OG1 . THR A  1 145 ? 22.446  2.702   48.750  1.00 35.53  ? 131 THR A OG1 1 
ATOM   1036 C  CG2 . THR A  1 145 ? 24.246  3.222   50.267  1.00 33.02  ? 131 THR A CG2 1 
ATOM   1037 N  N   A ASN A  1 146 ? 23.511  3.526   45.484  0.80 37.33  ? 132 ASN A N   1 
ATOM   1038 N  N   B ASN A  1 146 ? 23.506  3.522   45.485  0.20 32.76  ? 132 ASN A N   1 
ATOM   1039 C  CA  A ASN A  1 146 ? 23.354  2.938   44.162  0.80 39.81  ? 132 ASN A CA  1 
ATOM   1040 C  CA  B ASN A  1 146 ? 23.363  2.931   44.163  0.20 32.30  ? 132 ASN A CA  1 
ATOM   1041 C  C   A ASN A  1 146 ? 23.933  3.873   43.099  0.80 34.62  ? 132 ASN A C   1 
ATOM   1042 C  C   B ASN A  1 146 ? 23.857  3.913   43.100  0.20 31.69  ? 132 ASN A C   1 
ATOM   1043 O  O   A ASN A  1 146 ? 23.866  3.574   41.909  0.80 33.04  ? 132 ASN A O   1 
ATOM   1044 O  O   B ASN A  1 146 ? 23.649  3.691   41.910  0.20 31.26  ? 132 ASN A O   1 
ATOM   1045 C  CB  A ASN A  1 146 ? 21.893  2.609   43.862  0.80 41.45  ? 132 ASN A CB  1 
ATOM   1046 C  CB  B ASN A  1 146 ? 21.923  2.498   43.891  0.20 31.35  ? 132 ASN A CB  1 
ATOM   1047 C  CG  A ASN A  1 146 ? 21.433  1.334   44.530  0.80 48.03  ? 132 ASN A CG  1 
ATOM   1048 C  CG  B ASN A  1 146 ? 21.810  1.583   42.694  0.20 31.13  ? 132 ASN A CG  1 
ATOM   1049 O  OD1 A ASN A  1 146 ? 20.697  1.382   45.522  0.80 59.18  ? 132 ASN A OD1 1 
ATOM   1050 O  OD1 B ASN A  1 146 ? 22.824  1.079   42.198  0.20 29.71  ? 132 ASN A OD1 1 
ATOM   1051 N  ND2 A ASN A  1 146 ? 21.854  0.191   44.008  0.80 47.31  ? 132 ASN A ND2 1 
ATOM   1052 N  ND2 B ASN A  1 146 ? 20.593  1.343   42.226  0.20 31.46  ? 132 ASN A ND2 1 
ATOM   1053 N  N   . ALA A  1 147 ? 24.511  4.998   43.537  1.00 31.01  ? 133 ALA A N   1 
ATOM   1054 C  CA  . ALA A  1 147 ? 25.027  6.009   42.621  1.00 30.56  ? 133 ALA A CA  1 
ATOM   1055 C  C   . ALA A  1 147 ? 26.548  5.903   42.501  1.00 28.80  ? 133 ALA A C   1 
ATOM   1056 O  O   . ALA A  1 147 ? 27.200  5.283   43.339  1.00 29.75  ? 133 ALA A O   1 
ATOM   1057 C  CB  . ALA A  1 147 ? 24.615  7.388   43.097  1.00 28.39  ? 133 ALA A CB  1 
ATOM   1058 N  N   . THR A  1 148 ? 27.106  6.505   41.439  1.00 29.18  ? 134 THR A N   1 
ATOM   1059 C  CA  . THR A  1 148 ? 28.530  6.811   41.387  1.00 30.15  ? 134 THR A CA  1 
ATOM   1060 C  C   . THR A  1 148 ? 28.720  8.228   41.924  1.00 26.46  ? 134 THR A C   1 
ATOM   1061 O  O   . THR A  1 148 ? 28.142  9.175   41.396  1.00 29.15  ? 134 THR A O   1 
ATOM   1062 C  CB  . THR A  1 148 ? 29.088  6.673   39.968  1.00 30.31  ? 134 THR A CB  1 
ATOM   1063 O  OG1 . THR A  1 148 ? 28.896  5.311   39.598  1.00 31.38  ? 134 THR A OG1 1 
ATOM   1064 C  CG2 . THR A  1 148 ? 30.565  7.026   39.879  1.00 29.51  ? 134 THR A CG2 1 
ATOM   1065 N  N   . ILE A  1 149 ? 29.508  8.358   42.996  1.00 24.85  ? 135 ILE A N   1 
ATOM   1066 C  CA  . ILE A  1 149 ? 29.760  9.656   43.601  1.00 25.22  ? 135 ILE A CA  1 
ATOM   1067 C  C   . ILE A  1 149 ? 30.999  10.269  42.948  1.00 25.56  ? 135 ILE A C   1 
ATOM   1068 O  O   . ILE A  1 149 ? 32.111  9.767   43.113  1.00 24.55  ? 135 ILE A O   1 
ATOM   1069 C  CB  . ILE A  1 149 ? 29.912  9.544   45.130  1.00 28.48  ? 135 ILE A CB  1 
ATOM   1070 C  CG1 . ILE A  1 149 ? 28.826  8.659   45.757  1.00 29.70  ? 135 ILE A CG1 1 
ATOM   1071 C  CG2 . ILE A  1 149 ? 29.944  10.934  45.766  1.00 28.83  ? 135 ILE A CG2 1 
ATOM   1072 C  CD1 . ILE A  1 149 ? 27.410  9.153   45.525  1.00 28.99  ? 135 ILE A CD1 1 
ATOM   1073 N  N   . ILE A  1 150 ? 30.784  11.358  42.202  1.00 23.66  ? 136 ILE A N   1 
ATOM   1074 C  CA  . ILE A  1 150 ? 31.857  12.056  41.512  1.00 25.98  ? 136 ILE A CA  1 
ATOM   1075 C  C   . ILE A  1 150 ? 32.360  13.190  42.405  1.00 25.15  ? 136 ILE A C   1 
ATOM   1076 O  O   . ILE A  1 150 ? 31.584  14.039  42.843  1.00 23.45  ? 136 ILE A O   1 
ATOM   1077 C  CB  . ILE A  1 150 ? 31.379  12.548  40.132  1.00 25.72  ? 136 ILE A CB  1 
ATOM   1078 C  CG1 . ILE A  1 150 ? 30.899  11.375  39.272  1.00 26.02  ? 136 ILE A CG1 1 
ATOM   1079 C  CG2 . ILE A  1 150 ? 32.467  13.361  39.427  1.00 26.07  ? 136 ILE A CG2 1 
ATOM   1080 C  CD1 . ILE A  1 150 ? 30.236  11.782  37.970  1.00 28.77  ? 136 ILE A CD1 1 
ATOM   1081 N  N   . VAL A  1 151 ? 33.671  13.176  42.675  1.00 20.97  ? 137 VAL A N   1 
ATOM   1082 C  CA  . VAL A  1 151 ? 34.297  14.107  43.600  1.00 19.55  ? 137 VAL A CA  1 
ATOM   1083 C  C   . VAL A  1 151 ? 35.737  14.345  43.146  1.00 20.56  ? 137 VAL A C   1 
ATOM   1084 O  O   . VAL A  1 151 ? 36.352  13.456  42.559  1.00 19.56  ? 137 VAL A O   1 
ATOM   1085 C  CB  . VAL A  1 151 ? 34.247  13.556  45.040  1.00 20.19  ? 137 VAL A CB  1 
ATOM   1086 C  CG1 . VAL A  1 151 ? 35.081  12.289  45.194  1.00 21.02  ? 137 VAL A CG1 1 
ATOM   1087 C  CG2 . VAL A  1 151 ? 34.673  14.600  46.063  1.00 19.62  ? 137 VAL A CG2 1 
ATOM   1088 N  N   . HIS A  1 152 ? 36.266  15.545  43.417  1.00 18.41  ? 138 HIS A N   1 
ATOM   1089 C  CA  . HIS A  1 152 ? 37.645  15.867  43.074  1.00 20.71  ? 138 HIS A CA  1 
ATOM   1090 C  C   . HIS A  1 152 ? 38.572  15.067  43.989  1.00 20.17  ? 138 HIS A C   1 
ATOM   1091 O  O   . HIS A  1 152 ? 38.336  14.987  45.192  1.00 20.86  ? 138 HIS A O   1 
ATOM   1092 C  CB  . HIS A  1 152 ? 37.898  17.379  43.157  1.00 19.76  ? 138 HIS A CB  1 
ATOM   1093 C  CG  . HIS A  1 152 ? 39.149  17.809  42.456  1.00 20.67  ? 138 HIS A CG  1 
ATOM   1094 N  ND1 . HIS A  1 152 ? 40.406  17.414  42.861  1.00 19.12  ? 138 HIS A ND1 1 
ATOM   1095 C  CD2 . HIS A  1 152 ? 39.336  18.558  41.357  1.00 19.32  ? 138 HIS A CD2 1 
ATOM   1096 C  CE1 . HIS A  1 152 ? 41.314  17.933  42.045  1.00 19.69  ? 138 HIS A CE1 1 
ATOM   1097 N  NE2 . HIS A  1 152 ? 40.686  18.628  41.122  1.00 17.90  ? 138 HIS A NE2 1 
ATOM   1098 N  N   . GLU A  1 153 ? 39.625  14.469  43.415  1.00 19.81  ? 139 GLU A N   1 
ATOM   1099 C  CA  . GLU A  1 153 ? 40.470  13.551  44.164  1.00 18.21  ? 139 GLU A CA  1 
ATOM   1100 C  C   . GLU A  1 153 ? 41.170  14.298  45.298  1.00 18.17  ? 139 GLU A C   1 
ATOM   1101 O  O   . GLU A  1 153 ? 41.358  13.741  46.376  1.00 18.58  ? 139 GLU A O   1 
ATOM   1102 C  CB  . GLU A  1 153 ? 41.462  12.797  43.273  1.00 21.16  ? 139 GLU A CB  1 
ATOM   1103 C  CG  . GLU A  1 153 ? 42.553  13.661  42.648  1.00 21.44  ? 139 GLU A CG  1 
ATOM   1104 C  CD  . GLU A  1 153 ? 43.624  12.841  41.947  1.00 24.92  ? 139 GLU A CD  1 
ATOM   1105 O  OE1 . GLU A  1 153 ? 43.599  11.597  42.095  1.00 26.80  ? 139 GLU A OE1 1 
ATOM   1106 O  OE2 . GLU A  1 153 ? 44.477  13.437  41.253  1.00 25.35  ? 139 GLU A OE2 1 
ATOM   1107 N  N   . ASP A  1 154 ? 41.532  15.565  45.064  1.00 17.99  ? 140 ASP A N   1 
ATOM   1108 C  CA  . ASP A  1 154 ? 42.235  16.346  46.070  1.00 18.68  ? 140 ASP A CA  1 
ATOM   1109 C  C   . ASP A  1 154 ? 41.292  16.641  47.239  1.00 18.95  ? 140 ASP A C   1 
ATOM   1110 O  O   . ASP A  1 154 ? 41.715  16.632  48.393  1.00 19.73  ? 140 ASP A O   1 
ATOM   1111 C  CB  . ASP A  1 154 ? 42.885  17.585  45.470  1.00 18.76  ? 140 ASP A CB  1 
ATOM   1112 C  CG  . ASP A  1 154 ? 44.048  17.296  44.529  1.00 17.77  ? 140 ASP A CG  1 
ATOM   1113 O  OD1 . ASP A  1 154 ? 44.832  16.374  44.838  1.00 17.12  ? 140 ASP A OD1 1 
ATOM   1114 O  OD2 . ASP A  1 154 ? 44.172  18.001  43.508  1.00 18.18  ? 140 ASP A OD2 1 
ATOM   1115 N  N   . GLU A  1 155 ? 40.012  16.886  46.932  1.00 20.86  ? 141 GLU A N   1 
ATOM   1116 C  CA  . GLU A  1 155 ? 39.008  17.149  47.955  1.00 20.02  ? 141 GLU A CA  1 
ATOM   1117 C  C   . GLU A  1 155 ? 38.788  15.884  48.785  1.00 21.10  ? 141 GLU A C   1 
ATOM   1118 O  O   . GLU A  1 155 ? 38.691  15.948  50.010  1.00 18.61  ? 141 GLU A O   1 
ATOM   1119 C  CB  . GLU A  1 155 ? 37.700  17.622  47.317  1.00 21.53  ? 141 GLU A CB  1 
ATOM   1120 C  CG  . GLU A  1 155 ? 36.646  18.080  48.323  1.00 21.17  ? 141 GLU A CG  1 
ATOM   1121 C  CD  . GLU A  1 155 ? 36.959  19.395  49.013  1.00 22.11  ? 141 GLU A CD  1 
ATOM   1122 O  OE1 . GLU A  1 155 ? 37.977  20.021  48.646  1.00 20.56  ? 141 GLU A OE1 1 
ATOM   1123 O  OE2 . GLU A  1 155 ? 36.186  19.796  49.912  1.00 18.64  ? 141 GLU A OE2 1 
ATOM   1124 N  N   . PHE A  1 156 ? 38.724  14.739  48.093  1.00 22.59  ? 142 PHE A N   1 
ATOM   1125 C  CA  . PHE A  1 156 ? 38.493  13.443  48.715  1.00 22.17  ? 142 PHE A CA  1 
ATOM   1126 C  C   . PHE A  1 156 ? 39.643  13.127  49.670  1.00 21.71  ? 142 PHE A C   1 
ATOM   1127 O  O   . PHE A  1 156 ? 39.415  12.724  50.808  1.00 20.96  ? 142 PHE A O   1 
ATOM   1128 C  CB  . PHE A  1 156 ? 38.347  12.377  47.622  1.00 22.76  ? 142 PHE A CB  1 
ATOM   1129 C  CG  . PHE A  1 156 ? 37.814  11.019  48.062  1.00 21.89  ? 142 PHE A CG  1 
ATOM   1130 C  CD1 . PHE A  1 156 ? 36.714  10.914  48.909  1.00 25.22  ? 142 PHE A CD1 1 
ATOM   1131 C  CD2 . PHE A  1 156 ? 38.402  9.845   47.604  1.00 22.69  ? 142 PHE A CD2 1 
ATOM   1132 C  CE1 . PHE A  1 156 ? 36.227  9.671   49.289  1.00 24.00  ? 142 PHE A CE1 1 
ATOM   1133 C  CE2 . PHE A  1 156 ? 37.913  8.605   47.990  1.00 22.88  ? 142 PHE A CE2 1 
ATOM   1134 C  CZ  . PHE A  1 156 ? 36.828  8.520   48.831  1.00 24.84  ? 142 PHE A CZ  1 
ATOM   1135 N  N   . ASN A  1 157 ? 40.880  13.296  49.182  1.00 21.75  ? 143 ASN A N   1 
ATOM   1136 C  CA  . ASN A  1 157 ? 42.077  13.036  49.965  1.00 20.82  ? 143 ASN A CA  1 
ATOM   1137 C  C   . ASN A  1 157 ? 42.060  13.911  51.216  1.00 20.65  ? 143 ASN A C   1 
ATOM   1138 O  O   . ASN A  1 157 ? 42.329  13.435  52.316  1.00 23.61  ? 143 ASN A O   1 
ATOM   1139 C  CB  . ASN A  1 157 ? 43.348  13.256  49.144  1.00 22.57  ? 143 ASN A CB  1 
ATOM   1140 C  CG  . ASN A  1 157 ? 43.531  12.223  48.054  1.00 21.93  ? 143 ASN A CG  1 
ATOM   1141 O  OD1 . ASN A  1 157 ? 42.862  11.184  48.058  1.00 21.74  ? 143 ASN A OD1 1 
ATOM   1142 N  ND2 . ASN A  1 157 ? 44.440  12.479  47.123  1.00 18.84  ? 143 ASN A ND2 1 
ATOM   1143 N  N   . GLY A  1 158 ? 41.740  15.197  51.029  1.00 20.91  ? 144 GLY A N   1 
ATOM   1144 C  CA  . GLY A  1 158 ? 41.739  16.161  52.118  1.00 23.20  ? 144 GLY A CA  1 
ATOM   1145 C  C   . GLY A  1 158 ? 40.747  15.784  53.217  1.00 23.86  ? 144 GLY A C   1 
ATOM   1146 O  O   . GLY A  1 158 ? 41.076  15.847  54.401  1.00 22.92  ? 144 GLY A O   1 
ATOM   1147 N  N   . ALA A  1 159 ? 39.529  15.406  52.811  1.00 22.08  ? 145 ALA A N   1 
ATOM   1148 C  CA  . ALA A  1 159 ? 38.478  15.039  53.749  1.00 21.71  ? 145 ALA A CA  1 
ATOM   1149 C  C   . ALA A  1 159 ? 38.865  13.767  54.502  1.00 23.19  ? 145 ALA A C   1 
ATOM   1150 O  O   . ALA A  1 159 ? 38.608  13.646  55.698  1.00 26.77  ? 145 ALA A O   1 
ATOM   1151 C  CB  . ALA A  1 159 ? 37.163  14.873  53.015  1.00 20.98  ? 145 ALA A CB  1 
ATOM   1152 N  N   . LEU A  1 160 ? 39.494  12.822  53.796  1.00 22.52  ? 146 LEU A N   1 
ATOM   1153 C  CA  . LEU A  1 160 ? 39.861  11.543  54.384  1.00 21.68  ? 146 LEU A CA  1 
ATOM   1154 C  C   . LEU A  1 160 ? 40.950  11.746  55.437  1.00 21.96  ? 146 LEU A C   1 
ATOM   1155 O  O   . LEU A  1 160 ? 40.999  11.016  56.424  1.00 20.91  ? 146 LEU A O   1 
ATOM   1156 C  CB  . LEU A  1 160 ? 40.314  10.573  53.293  1.00 22.60  ? 146 LEU A CB  1 
ATOM   1157 C  CG  . LEU A  1 160 ? 39.217  10.051  52.360  1.00 24.11  ? 146 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A  1 160 ? 39.811  9.144   51.295  1.00 23.23  ? 146 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A  1 160 ? 38.128  9.321   53.135  1.00 24.38  ? 146 LEU A CD2 1 
ATOM   1160 N  N   . GLN A  1 161 ? 41.832  12.728  55.214  1.00 21.12  ? 147 GLN A N   1 
ATOM   1161 C  CA  . GLN A  1 161 ? 42.871  13.048  56.180  1.00 21.83  ? 147 GLN A CA  1 
ATOM   1162 C  C   . GLN A  1 161 ? 42.233  13.629  57.441  1.00 20.18  ? 147 GLN A C   1 
ATOM   1163 O  O   . GLN A  1 161 ? 42.664  13.323  58.552  1.00 21.40  ? 147 GLN A O   1 
ATOM   1164 C  CB  . GLN A  1 161 ? 43.914  14.023  55.629  1.00 23.10  ? 147 GLN A CB  1 
ATOM   1165 C  CG  . GLN A  1 161 ? 44.961  13.389  54.718  1.00 22.69  ? 147 GLN A CG  1 
ATOM   1166 C  CD  . GLN A  1 161 ? 46.252  14.180  54.679  1.00 24.91  ? 147 GLN A CD  1 
ATOM   1167 O  OE1 . GLN A  1 161 ? 46.600  14.891  55.629  1.00 23.09  ? 147 GLN A OE1 1 
ATOM   1168 N  NE2 . GLN A  1 161 ? 46.996  14.042  53.591  1.00 22.52  ? 147 GLN A NE2 1 
ATOM   1169 N  N   . CYS A  1 162 ? 41.230  14.495  57.263  1.00 21.19  ? 148 CYS A N   1 
ATOM   1170 C  CA  . CYS A  1 162 ? 40.486  15.030  58.393  1.00 24.06  ? 148 CYS A CA  1 
ATOM   1171 C  C   . CYS A  1 162 ? 39.967  13.867  59.236  1.00 24.26  ? 148 CYS A C   1 
ATOM   1172 O  O   . CYS A  1 162 ? 40.089  13.874  60.459  1.00 27.75  ? 148 CYS A O   1 
ATOM   1173 C  CB  . CYS A  1 162 ? 39.341  15.931  57.941  1.00 23.89  ? 148 CYS A CB  1 
ATOM   1174 S  SG  . CYS A  1 162 ? 39.895  17.475  57.169  1.00 26.04  ? 148 CYS A SG  1 
ATOM   1175 N  N   . TYR A  1 163 ? 39.418  12.856  58.554  1.00 22.77  ? 149 TYR A N   1 
ATOM   1176 C  CA  . TYR A  1 163 ? 38.840  11.689  59.201  1.00 23.57  ? 149 TYR A CA  1 
ATOM   1177 C  C   . TYR A  1 163 ? 39.918  10.924  59.967  1.00 24.35  ? 149 TYR A C   1 
ATOM   1178 O  O   . TYR A  1 163 ? 39.756  10.635  61.150  1.00 24.36  ? 149 TYR A O   1 
ATOM   1179 C  CB  . TYR A  1 163 ? 38.166  10.789  58.159  1.00 24.43  ? 149 TYR A CB  1 
ATOM   1180 C  CG  . TYR A  1 163 ? 37.470  9.567   58.748  1.00 24.43  ? 149 TYR A CG  1 
ATOM   1181 C  CD1 . TYR A  1 163 ? 36.301  9.697   59.489  1.00 27.17  ? 149 TYR A CD1 1 
ATOM   1182 C  CD2 . TYR A  1 163 ? 37.977  8.285   58.563  1.00 25.33  ? 149 TYR A CD2 1 
ATOM   1183 C  CE1 . TYR A  1 163 ? 35.659  8.593   60.029  1.00 26.79  ? 149 TYR A CE1 1 
ATOM   1184 C  CE2 . TYR A  1 163 ? 37.345  7.173   59.099  1.00 29.22  ? 149 TYR A CE2 1 
ATOM   1185 C  CZ  . TYR A  1 163 ? 36.182  7.328   59.833  1.00 29.15  ? 149 TYR A CZ  1 
ATOM   1186 O  OH  . TYR A  1 163 ? 35.549  6.242   60.367  1.00 35.25  ? 149 TYR A OH  1 
ATOM   1187 N  N   . ALA A  1 164 ? 41.015  10.593  59.275  1.00 23.89  ? 150 ALA A N   1 
ATOM   1188 C  CA  . ALA A  1 164 ? 42.071  9.762   59.833  1.00 22.80  ? 150 ALA A CA  1 
ATOM   1189 C  C   . ALA A  1 164 ? 42.755  10.468  61.001  1.00 22.31  ? 150 ALA A C   1 
ATOM   1190 O  O   . ALA A  1 164 ? 43.258  9.813   61.910  1.00 24.42  ? 150 ALA A O   1 
ATOM   1191 C  CB  . ALA A  1 164 ? 43.073  9.407   58.753  1.00 22.46  ? 150 ALA A CB  1 
ATOM   1192 N  N   . ARG A  1 165 ? 42.779  11.805  60.952  1.00 21.94  ? 151 ARG A N   1 
ATOM   1193 C  CA  . ARG A  1 165 ? 43.425  12.614  61.974  1.00 24.17  ? 151 ARG A CA  1 
ATOM   1194 C  C   . ARG A  1 165 ? 42.445  12.890  63.112  1.00 28.54  ? 151 ARG A C   1 
ATOM   1195 O  O   . ARG A  1 165 ? 42.778  13.591  64.066  1.00 26.11  ? 151 ARG A O   1 
ATOM   1196 C  CB  . ARG A  1 165 ? 43.932  13.936  61.381  1.00 24.78  ? 151 ARG A CB  1 
ATOM   1197 C  CG  . ARG A  1 165 ? 45.083  13.805  60.393  1.00 23.44  ? 151 ARG A CG  1 
ATOM   1198 C  CD  . ARG A  1 165 ? 45.366  15.122  59.673  1.00 25.65  ? 151 ARG A CD  1 
ATOM   1199 N  NE  . ARG A  1 165 ? 46.388  14.995  58.627  1.00 26.01  ? 151 ARG A NE  1 
ATOM   1200 C  CZ  . ARG A  1 165 ? 47.657  15.361  58.763  1.00 29.17  ? 151 ARG A CZ  1 
ATOM   1201 N  NH1 . ARG A  1 165 ? 48.101  15.781  59.934  1.00 32.45  ? 151 ARG A NH1 1 
ATOM   1202 N  NH2 . ARG A  1 165 ? 48.487  15.281  57.737  1.00 30.65  ? 151 ARG A NH2 1 
ATOM   1203 N  N   . ASN A  1 166 ? 41.228  12.346  62.997  1.00 27.91  ? 152 ASN A N   1 
ATOM   1204 C  CA  . ASN A  1 166 ? 40.227  12.476  64.045  1.00 30.78  ? 152 ASN A CA  1 
ATOM   1205 C  C   . ASN A  1 166 ? 39.975  13.957  64.327  1.00 31.96  ? 152 ASN A C   1 
ATOM   1206 O  O   . ASN A  1 166 ? 39.936  14.377  65.482  1.00 32.55  ? 152 ASN A O   1 
ATOM   1207 C  CB  . ASN A  1 166 ? 40.627  11.690  65.293  1.00 30.12  ? 152 ASN A CB  1 
ATOM   1208 C  CG  . ASN A  1 166 ? 40.490  10.197  65.099  1.00 31.77  ? 152 ASN A CG  1 
ATOM   1209 O  OD1 . ASN A  1 166 ? 39.375  9.693   64.930  1.00 36.12  ? 152 ASN A OD1 1 
ATOM   1210 N  ND2 . ASN A  1 166 ? 41.601  9.475   65.124  1.00 35.99  ? 152 ASN A ND2 1 
ATOM   1211 N  N   A GLN A  1 167 ? 39.801  14.739  63.254  0.70 28.85  ? 153 GLN A N   1 
ATOM   1212 N  N   B GLN A  1 167 ? 39.815  14.742  63.254  0.30 32.72  ? 153 GLN A N   1 
ATOM   1213 C  CA  A GLN A  1 167 ? 39.453  16.146  63.370  0.70 31.09  ? 153 GLN A CA  1 
ATOM   1214 C  CA  B GLN A  1 167 ? 39.448  16.146  63.364  0.30 35.35  ? 153 GLN A CA  1 
ATOM   1215 C  C   A GLN A  1 167 ? 37.937  16.255  63.535  0.70 34.47  ? 153 GLN A C   1 
ATOM   1216 C  C   B GLN A  1 167 ? 37.933  16.242  63.539  0.30 37.17  ? 153 GLN A C   1 
ATOM   1217 O  O   A GLN A  1 167 ? 37.187  15.963  62.606  0.70 32.65  ? 153 GLN A O   1 
ATOM   1218 O  O   B GLN A  1 167 ? 37.179  15.935  62.618  0.30 36.17  ? 153 GLN A O   1 
ATOM   1219 C  CB  A GLN A  1 167 ? 39.983  16.919  62.159  0.70 31.94  ? 153 GLN A CB  1 
ATOM   1220 C  CB  B GLN A  1 167 ? 39.917  16.929  62.136  0.30 37.08  ? 153 GLN A CB  1 
ATOM   1221 C  CG  A GLN A  1 167 ? 41.484  16.756  61.934  0.70 33.06  ? 153 GLN A CG  1 
ATOM   1222 C  CG  B GLN A  1 167 ? 39.448  18.381  62.111  0.30 38.49  ? 153 GLN A CG  1 
ATOM   1223 C  CD  A GLN A  1 167 ? 42.056  17.722  60.918  0.70 32.72  ? 153 GLN A CD  1 
ATOM   1224 C  CD  B GLN A  1 167 ? 39.952  19.184  63.291  0.30 40.81  ? 153 GLN A CD  1 
ATOM   1225 O  OE1 A GLN A  1 167 ? 41.325  18.434  60.220  0.70 36.07  ? 153 GLN A OE1 1 
ATOM   1226 O  OE1 B GLN A  1 167 ? 39.195  19.536  64.203  0.30 41.94  ? 153 GLN A OE1 1 
ATOM   1227 N  NE2 A GLN A  1 167 ? 43.378  17.752  60.823  0.70 33.49  ? 153 GLN A NE2 1 
ATOM   1228 N  NE2 B GLN A  1 167 ? 41.246  19.472  63.289  0.30 40.60  ? 153 GLN A NE2 1 
ATOM   1229 N  N   . LYS A  1 168 ? 37.499  16.666  64.732  1.00 39.18  ? 154 LYS A N   1 
ATOM   1230 C  CA  . LYS A  1 168 ? 36.083  16.686  65.079  1.00 45.79  ? 154 LYS A CA  1 
ATOM   1231 C  C   . LYS A  1 168 ? 35.509  18.099  64.973  1.00 44.45  ? 154 LYS A C   1 
ATOM   1232 O  O   . LYS A  1 168 ? 34.335  18.308  65.276  1.00 53.95  ? 154 LYS A O   1 
ATOM   1233 C  CB  . LYS A  1 168 ? 35.851  16.110  66.483  1.00 48.80  ? 154 LYS A CB  1 
ATOM   1234 C  CG  . LYS A  1 168 ? 35.362  14.663  66.542  1.00 51.04  ? 154 LYS A CG  1 
ATOM   1235 C  CD  . LYS A  1 168 ? 36.268  13.657  65.844  1.00 55.23  ? 154 LYS A CD  1 
ATOM   1236 C  CE  . LYS A  1 168 ? 35.974  12.238  66.236  1.00 52.31  ? 154 LYS A CE  1 
ATOM   1237 N  NZ  . LYS A  1 168 ? 37.082  11.338  65.896  1.00 55.02  ? 154 LYS A NZ  1 
ATOM   1238 N  N   . GLU A  1 169 ? 36.333  19.063  64.545  1.00 44.29  ? 155 GLU A N   1 
ATOM   1239 C  CA  . GLU A  1 169 ? 35.854  20.414  64.290  1.00 49.69  ? 155 GLU A CA  1 
ATOM   1240 C  C   . GLU A  1 169 ? 36.176  20.794  62.847  1.00 44.93  ? 155 GLU A C   1 
ATOM   1241 O  O   . GLU A  1 169 ? 36.864  20.057  62.145  1.00 42.73  ? 155 GLU A O   1 
ATOM   1242 C  CB  . GLU A  1 169 ? 36.466  21.433  65.252  1.00 58.76  ? 155 GLU A CB  1 
ATOM   1243 C  CG  . GLU A  1 169 ? 36.659  20.896  66.667  1.00 64.33  ? 155 GLU A CG  1 
ATOM   1244 C  CD  . GLU A  1 169 ? 36.471  21.935  67.758  1.00 64.30  ? 155 GLU A CD  1 
ATOM   1245 O  OE1 . GLU A  1 169 ? 37.057  23.032  67.643  1.00 66.46  ? 155 GLU A OE1 1 
ATOM   1246 O  OE2 . GLU A  1 169 ? 35.738  21.643  68.726  1.00 67.08  ? 155 GLU A OE2 1 
ATOM   1247 N  N   . GLY A  1 170 ? 35.669  21.954  62.416  1.00 41.31  ? 156 GLY A N   1 
ATOM   1248 C  CA  . GLY A  1 170 ? 35.908  22.446  61.069  1.00 43.23  ? 156 GLY A CA  1 
ATOM   1249 C  C   . GLY A  1 170 ? 34.723  22.167  60.145  1.00 41.88  ? 156 GLY A C   1 
ATOM   1250 O  O   . GLY A  1 170 ? 33.639  21.807  60.602  1.00 37.07  ? 156 GLY A O   1 
ATOM   1251 N  N   . ALA A  1 171 ? 34.958  22.327  58.838  1.00 36.03  ? 157 ALA A N   1 
ATOM   1252 C  CA  . ALA A  1 171 ? 33.899  22.287  57.844  1.00 33.72  ? 157 ALA A CA  1 
ATOM   1253 C  C   . ALA A  1 171 ? 33.746  20.880  57.268  1.00 28.81  ? 157 ALA A C   1 
ATOM   1254 O  O   . ALA A  1 171 ? 32.888  20.649  56.420  1.00 29.51  ? 157 ALA A O   1 
ATOM   1255 C  CB  . ALA A  1 171 ? 34.190  23.301  56.758  1.00 31.35  ? 157 ALA A CB  1 
ATOM   1256 N  N   . TYR A  1 172 ? 34.589  19.948  57.730  1.00 26.96  ? 158 TYR A N   1 
ATOM   1257 C  CA  . TYR A  1 172 ? 34.524  18.559  57.300  1.00 25.77  ? 158 TYR A CA  1 
ATOM   1258 C  C   . TYR A  1 172 ? 34.032  17.710  58.472  1.00 26.95  ? 158 TYR A C   1 
ATOM   1259 O  O   . TYR A  1 172 ? 34.702  17.621  59.498  1.00 28.24  ? 158 TYR A O   1 
ATOM   1260 C  CB  . TYR A  1 172 ? 35.890  18.129  56.749  1.00 24.56  ? 158 TYR A CB  1 
ATOM   1261 C  CG  . TYR A  1 172 ? 36.266  18.864  55.469  1.00 22.85  ? 158 TYR A CG  1 
ATOM   1262 C  CD1 . TYR A  1 172 ? 35.776  18.452  54.234  1.00 21.76  ? 158 TYR A CD1 1 
ATOM   1263 C  CD2 . TYR A  1 172 ? 37.080  19.991  55.498  1.00 24.15  ? 158 TYR A CD2 1 
ATOM   1264 C  CE1 . TYR A  1 172 ? 36.095  19.131  53.069  1.00 21.97  ? 158 TYR A CE1 1 
ATOM   1265 C  CE2 . TYR A  1 172 ? 37.411  20.675  54.339  1.00 25.70  ? 158 TYR A CE2 1 
ATOM   1266 C  CZ  . TYR A  1 172 ? 36.917  20.244  53.120  1.00 24.35  ? 158 TYR A CZ  1 
ATOM   1267 O  OH  . TYR A  1 172 ? 37.241  20.924  51.982  1.00 22.12  ? 158 TYR A OH  1 
ATOM   1268 N  N   . ILE A  1 173 ? 32.853  17.096  58.303  1.00 29.14  ? 159 ILE A N   1 
ATOM   1269 C  CA  . ILE A  1 173 ? 32.148  16.442  59.397  1.00 24.88  ? 159 ILE A CA  1 
ATOM   1270 C  C   . ILE A  1 173 ? 32.617  14.992  59.510  1.00 23.48  ? 159 ILE A C   1 
ATOM   1271 O  O   . ILE A  1 173 ? 32.375  14.185  58.616  1.00 29.49  ? 159 ILE A O   1 
ATOM   1272 C  CB  . ILE A  1 173 ? 30.622  16.546  59.195  1.00 27.64  ? 159 ILE A CB  1 
ATOM   1273 C  CG1 . ILE A  1 173 ? 30.180  17.997  58.976  1.00 27.75  ? 159 ILE A CG1 1 
ATOM   1274 C  CG2 . ILE A  1 173 ? 29.863  15.896  60.353  1.00 29.25  ? 159 ILE A CG2 1 
ATOM   1275 C  CD1 . ILE A  1 173 ? 30.645  18.954  60.060  1.00 29.39  ? 159 ILE A CD1 1 
ATOM   1276 N  N   . TRP A  1 174 ? 33.276  14.675  60.633  1.00 23.16  ? 160 TRP A N   1 
ATOM   1277 C  CA  . TRP A  1 174 ? 33.839  13.353  60.866  1.00 24.48  ? 160 TRP A CA  1 
ATOM   1278 C  C   . TRP A  1 174 ? 32.744  12.290  60.769  1.00 26.32  ? 160 TRP A C   1 
ATOM   1279 O  O   . TRP A  1 174 ? 32.961  11.221  60.201  1.00 22.43  ? 160 TRP A O   1 
ATOM   1280 C  CB  . TRP A  1 174 ? 34.546  13.299  62.231  1.00 25.40  ? 160 TRP A CB  1 
ATOM   1281 C  CG  . TRP A  1 174 ? 35.472  12.121  62.416  1.00 26.98  ? 160 TRP A CG  1 
ATOM   1282 C  CD1 . TRP A  1 174 ? 36.820  12.104  62.196  1.00 28.65  ? 160 TRP A CD1 1 
ATOM   1283 C  CD2 . TRP A  1 174 ? 35.124  10.789  62.865  1.00 28.55  ? 160 TRP A CD2 1 
ATOM   1284 N  NE1 . TRP A  1 174 ? 37.334  10.864  62.470  1.00 28.91  ? 160 TRP A NE1 1 
ATOM   1285 C  CE2 . TRP A  1 174 ? 36.321  10.037  62.882  1.00 28.90  ? 160 TRP A CE2 1 
ATOM   1286 C  CE3 . TRP A  1 174 ? 33.931  10.162  63.249  1.00 28.76  ? 160 TRP A CE3 1 
ATOM   1287 C  CZ2 . TRP A  1 174 ? 36.352  8.697   63.267  1.00 28.59  ? 160 TRP A CZ2 1 
ATOM   1288 C  CZ3 . TRP A  1 174 ? 33.964  8.837   63.629  1.00 28.91  ? 160 TRP A CZ3 1 
ATOM   1289 C  CH2 . TRP A  1 174 ? 35.159  8.116   63.637  1.00 30.47  ? 160 TRP A CH2 1 
ATOM   1290 N  N   . ALA A  1 175 ? 31.565  12.601  61.326  1.00 25.19  ? 161 ALA A N   1 
ATOM   1291 C  CA  . ALA A  1 175 ? 30.473  11.644  61.421  1.00 25.77  ? 161 ALA A CA  1 
ATOM   1292 C  C   . ALA A  1 175 ? 29.895  11.358  60.036  1.00 26.00  ? 161 ALA A C   1 
ATOM   1293 O  O   . ALA A  1 175 ? 29.437  10.249  59.769  1.00 28.23  ? 161 ALA A O   1 
ATOM   1294 C  CB  . ALA A  1 175 ? 29.409  12.163  62.370  1.00 28.09  ? 161 ALA A CB  1 
ATOM   1295 N  N   . ASP A  1 176 ? 29.921  12.370  59.161  1.00 24.33  ? 162 ASP A N   1 
ATOM   1296 C  CA  . ASP A  1 176 ? 29.430  12.225  57.799  1.00 24.63  ? 162 ASP A CA  1 
ATOM   1297 C  C   . ASP A  1 176 ? 30.360  11.298  57.019  1.00 26.38  ? 162 ASP A C   1 
ATOM   1298 O  O   . ASP A  1 176 ? 29.905  10.363  56.363  1.00 24.52  ? 162 ASP A O   1 
ATOM   1299 C  CB  . ASP A  1 176 ? 29.269  13.577  57.116  1.00 25.02  ? 162 ASP A CB  1 
ATOM   1300 C  CG  . ASP A  1 176 ? 28.091  14.417  57.590  1.00 27.47  ? 162 ASP A CG  1 
ATOM   1301 O  OD1 . ASP A  1 176 ? 27.347  13.940  58.474  1.00 29.52  ? 162 ASP A OD1 1 
ATOM   1302 O  OD2 . ASP A  1 176 ? 27.919  15.537  57.062  1.00 26.78  ? 162 ASP A OD2 1 
ATOM   1303 N  N   . ILE A  1 177 ? 31.668  11.575  57.100  1.00 28.17  ? 163 ILE A N   1 
ATOM   1304 C  CA  . ILE A  1 177 ? 32.683  10.798  56.402  1.00 25.96  ? 163 ILE A CA  1 
ATOM   1305 C  C   . ILE A  1 177 ? 32.601  9.345   56.867  1.00 28.56  ? 163 ILE A C   1 
ATOM   1306 O  O   . ILE A  1 177 ? 32.673  8.420   56.058  1.00 27.10  ? 163 ILE A O   1 
ATOM   1307 C  CB  . ILE A  1 177 ? 34.086  11.397  56.634  1.00 27.51  ? 163 ILE A CB  1 
ATOM   1308 C  CG1 . ILE A  1 177 ? 34.163  12.861  56.181  1.00 27.55  ? 163 ILE A CG1 1 
ATOM   1309 C  CG2 . ILE A  1 177 ? 35.166  10.543  55.967  1.00 26.13  ? 163 ILE A CG2 1 
ATOM   1310 C  CD1 . ILE A  1 177 ? 35.333  13.633  56.768  1.00 30.71  ? 163 ILE A CD1 1 
ATOM   1311 N  N   . ASP A  1 178 ? 32.453  9.166   58.183  1.00 30.48  ? 164 ASP A N   1 
ATOM   1312 C  CA  . ASP A  1 178 ? 32.353  7.849   58.792  1.00 29.87  ? 164 ASP A CA  1 
ATOM   1313 C  C   . ASP A  1 178 ? 31.254  7.051   58.093  1.00 29.13  ? 164 ASP A C   1 
ATOM   1314 O  O   . ASP A  1 178 ? 31.424  5.867   57.813  1.00 31.14  ? 164 ASP A O   1 
ATOM   1315 C  CB  . ASP A  1 178 ? 32.119  7.968   60.291  1.00 30.28  ? 164 ASP A CB  1 
ATOM   1316 C  CG  . ASP A  1 178 ? 32.132  6.658   61.064  1.00 34.36  ? 164 ASP A CG  1 
ATOM   1317 O  OD1 . ASP A  1 178 ? 33.157  5.948   60.995  1.00 31.71  ? 164 ASP A OD1 1 
ATOM   1318 O  OD2 . ASP A  1 178 ? 31.120  6.364   61.731  1.00 40.31  ? 164 ASP A OD2 1 
ATOM   1319 N  N   . ALA A  1 179 ? 30.131  7.721   57.807  1.00 31.67  ? 165 ALA A N   1 
ATOM   1320 C  CA  . ALA A  1 179 ? 28.961  7.079   57.227  1.00 30.70  ? 165 ALA A CA  1 
ATOM   1321 C  C   . ALA A  1 179 ? 29.200  6.760   55.752  1.00 29.29  ? 165 ALA A C   1 
ATOM   1322 O  O   . ALA A  1 179 ? 28.775  5.712   55.271  1.00 30.92  ? 165 ALA A O   1 
ATOM   1323 C  CB  . ALA A  1 179 ? 27.741  7.959   57.412  1.00 31.34  ? 165 ALA A CB  1 
ATOM   1324 N  N   . TRP A  1 180 ? 29.869  7.672   55.033  1.00 30.41  ? 166 TRP A N   1 
ATOM   1325 C  CA  . TRP A  1 180 ? 30.195  7.437   53.635  1.00 29.39  ? 166 TRP A CA  1 
ATOM   1326 C  C   . TRP A  1 180 ? 30.929  6.103   53.507  1.00 27.53  ? 166 TRP A C   1 
ATOM   1327 O  O   . TRP A  1 180 ? 30.659  5.323   52.597  1.00 30.06  ? 166 TRP A O   1 
ATOM   1328 C  CB  . TRP A  1 180 ? 31.051  8.571   53.048  1.00 26.47  ? 166 TRP A CB  1 
ATOM   1329 C  CG  . TRP A  1 180 ? 30.511  9.966   53.239  1.00 27.35  ? 166 TRP A CG  1 
ATOM   1330 C  CD1 . TRP A  1 180 ? 29.238  10.337  53.568  1.00 27.83  ? 166 TRP A CD1 1 
ATOM   1331 C  CD2 . TRP A  1 180 ? 31.262  11.194  53.095  1.00 27.74  ? 166 TRP A CD2 1 
ATOM   1332 N  NE1 . TRP A  1 180 ? 29.147  11.702  53.649  1.00 26.66  ? 166 TRP A NE1 1 
ATOM   1333 C  CE2 . TRP A  1 180 ? 30.370  12.256  53.363  1.00 28.00  ? 166 TRP A CE2 1 
ATOM   1334 C  CE3 . TRP A  1 180 ? 32.591  11.495  52.771  1.00 27.04  ? 166 TRP A CE3 1 
ATOM   1335 C  CZ2 . TRP A  1 180 ? 30.772  13.590  53.315  1.00 28.53  ? 166 TRP A CZ2 1 
ATOM   1336 C  CZ3 . TRP A  1 180 ? 32.986  12.814  52.725  1.00 25.46  ? 166 TRP A CZ3 1 
ATOM   1337 C  CH2 . TRP A  1 180 ? 32.088  13.846  52.998  1.00 27.61  ? 166 TRP A CH2 1 
ATOM   1338 N  N   . ILE A  1 181 ? 31.862  5.858   54.436  1.00 28.66  ? 167 ILE A N   1 
ATOM   1339 C  CA  . ILE A  1 181 ? 32.715  4.681   54.389  1.00 30.07  ? 167 ILE A CA  1 
ATOM   1340 C  C   . ILE A  1 181 ? 31.898  3.443   54.762  1.00 35.78  ? 167 ILE A C   1 
ATOM   1341 O  O   . ILE A  1 181 ? 32.048  2.391   54.144  1.00 35.87  ? 167 ILE A O   1 
ATOM   1342 C  CB  . ILE A  1 181 ? 33.949  4.865   55.297  1.00 29.21  ? 167 ILE A CB  1 
ATOM   1343 C  CG1 . ILE A  1 181 ? 34.846  6.011   54.806  1.00 31.37  ? 167 ILE A CG1 1 
ATOM   1344 C  CG2 . ILE A  1 181 ? 34.732  3.558   55.431  1.00 30.21  ? 167 ILE A CG2 1 
ATOM   1345 C  CD1 . ILE A  1 181 ? 36.021  6.322   55.718  1.00 32.71  ? 167 ILE A CD1 1 
ATOM   1346 N  N   . LYS A  1 182 ? 31.020  3.579   55.765  1.00 33.45  ? 168 LYS A N   1 
ATOM   1347 C  CA  . LYS A  1 182 ? 30.240  2.452   56.258  1.00 36.37  ? 168 LYS A CA  1 
ATOM   1348 C  C   . LYS A  1 182 ? 29.188  2.049   55.224  1.00 34.37  ? 168 LYS A C   1 
ATOM   1349 O  O   . LYS A  1 182 ? 28.837  0.875   55.127  1.00 37.24  ? 168 LYS A O   1 
ATOM   1350 C  CB  . LYS A  1 182 ? 29.633  2.775   57.630  1.00 37.36  ? 168 LYS A CB  1 
ATOM   1351 C  CG  . LYS A  1 182 ? 30.658  2.821   58.758  1.00 44.68  ? 168 LYS A CG  1 
ATOM   1352 C  CD  . LYS A  1 182 ? 30.111  3.136   60.144  1.00 50.24  ? 168 LYS A CD  1 
ATOM   1353 C  CE  . LYS A  1 182 ? 31.146  2.893   61.205  1.00 56.18  ? 168 LYS A CE  1 
ATOM   1354 N  NZ  . LYS A  1 182 ? 31.042  3.850   62.311  1.00 56.61  ? 168 LYS A NZ  1 
ATOM   1355 N  N   . ASN A  1 183 ? 28.709  3.020   54.436  1.00 34.22  ? 169 ASN A N   1 
ATOM   1356 C  CA  . ASN A  1 183 ? 27.658  2.767   53.461  1.00 33.39  ? 169 ASN A CA  1 
ATOM   1357 C  C   . ASN A  1 183 ? 28.260  2.257   52.150  1.00 33.49  ? 169 ASN A C   1 
ATOM   1358 O  O   . ASN A  1 183 ? 27.527  1.984   51.203  1.00 33.22  ? 169 ASN A O   1 
ATOM   1359 C  CB  . ASN A  1 183 ? 26.776  3.993   53.229  1.00 35.06  ? 169 ASN A CB  1 
ATOM   1360 C  CG  . ASN A  1 183 ? 25.817  4.259   54.368  1.00 40.88  ? 169 ASN A CG  1 
ATOM   1361 O  OD1 . ASN A  1 183 ? 25.982  3.717   55.466  1.00 40.60  ? 169 ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A  1 183 ? 24.817  5.096   54.132  1.00 44.81  ? 169 ASN A ND2 1 
ATOM   1363 N  N   . ASN A  1 184 ? 29.595  2.144   52.096  1.00 34.69  ? 170 ASN A N   1 
ATOM   1364 C  CA  . ASN A  1 184 ? 30.279  1.527   50.968  1.00 33.55  ? 170 ASN A CA  1 
ATOM   1365 C  C   . ASN A  1 184 ? 29.906  2.248   49.672  1.00 28.63  ? 170 ASN A C   1 
ATOM   1366 O  O   . ASN A  1 184 ? 29.572  1.606   48.680  1.00 30.38  ? 170 ASN A O   1 
ATOM   1367 C  CB  . ASN A  1 184 ? 29.979  0.030   50.900  1.00 35.89  ? 170 ASN A CB  1 
ATOM   1368 C  CG  . ASN A  1 184 ? 30.778  -0.692  49.838  1.00 43.84  ? 170 ASN A CG  1 
ATOM   1369 O  OD1 . ASN A  1 184 ? 31.963  -0.399  49.638  1.00 43.60  ? 170 ASN A OD1 1 
ATOM   1370 N  ND2 . ASN A  1 184 ? 30.151  -1.632  49.146  1.00 47.46  ? 170 ASN A ND2 1 
ATOM   1371 N  N   . LEU A  1 185 ? 29.982  3.586   49.685  1.00 32.48  ? 171 LEU A N   1 
ATOM   1372 C  CA  . LEU A  1 185 ? 29.664  4.398   48.518  1.00 34.00  ? 171 LEU A CA  1 
ATOM   1373 C  C   . LEU A  1 185 ? 30.628  4.071   47.379  1.00 33.56  ? 171 LEU A C   1 
ATOM   1374 O  O   . LEU A  1 185 ? 31.755  3.641   47.619  1.00 28.00  ? 171 LEU A O   1 
ATOM   1375 C  CB  . LEU A  1 185 ? 29.723  5.883   48.874  1.00 33.57  ? 171 LEU A CB  1 
ATOM   1376 C  CG  . LEU A  1 185 ? 28.680  6.381   49.880  1.00 36.13  ? 171 LEU A CG  1 
ATOM   1377 C  CD1 . LEU A  1 185 ? 28.745  7.896   50.017  1.00 37.64  ? 171 LEU A CD1 1 
ATOM   1378 C  CD2 . LEU A  1 185 ? 27.278  5.939   49.491  1.00 38.33  ? 171 LEU A CD2 1 
ATOM   1379 N  N   . GLN A  1 186 ? 30.167  4.300   46.141  1.00 30.65  ? 172 GLN A N   1 
ATOM   1380 C  CA  A GLN A  1 186 ? 30.945  4.023   44.943  0.40 32.35  ? 172 GLN A CA  1 
ATOM   1381 C  CA  B GLN A  1 186 ? 30.957  4.018   44.952  0.60 32.04  ? 172 GLN A CA  1 
ATOM   1382 C  C   . GLN A  1 186 ? 31.559  5.322   44.425  1.00 31.08  ? 172 GLN A C   1 
ATOM   1383 O  O   . GLN A  1 186 ? 30.856  6.164   43.872  1.00 36.01  ? 172 GLN A O   1 
ATOM   1384 C  CB  A GLN A  1 186 ? 30.056  3.372   43.881  0.40 33.68  ? 172 GLN A CB  1 
ATOM   1385 C  CB  B GLN A  1 186 ? 30.090  3.288   43.925  0.60 33.02  ? 172 GLN A CB  1 
ATOM   1386 C  CG  A GLN A  1 186 ? 30.660  3.381   42.480  0.40 34.60  ? 172 GLN A CG  1 
ATOM   1387 C  CG  B GLN A  1 186 ? 29.553  1.947   44.418  0.60 32.98  ? 172 GLN A CG  1 
ATOM   1388 C  CD  A GLN A  1 186 ? 29.933  2.471   41.514  0.40 36.95  ? 172 GLN A CD  1 
ATOM   1389 C  CD  B GLN A  1 186 ? 30.643  1.025   44.924  0.60 35.90  ? 172 GLN A CD  1 
ATOM   1390 O  OE1 A GLN A  1 186 ? 28.720  2.583   41.305  0.40 41.21  ? 172 GLN A OE1 1 
ATOM   1391 O  OE1 B GLN A  1 186 ? 30.570  0.488   46.035  0.60 33.48  ? 172 GLN A OE1 1 
ATOM   1392 N  NE2 A GLN A  1 186 ? 30.676  1.550   40.917  0.40 35.26  ? 172 GLN A NE2 1 
ATOM   1393 N  NE2 B GLN A  1 186 ? 31.668  0.829   44.108  0.60 37.26  ? 172 GLN A NE2 1 
ATOM   1394 N  N   . TRP A  1 187 ? 32.881  5.462   44.594  1.00 29.48  ? 173 TRP A N   1 
ATOM   1395 C  CA  . TRP A  1 187 ? 33.589  6.705   44.315  1.00 29.96  ? 173 TRP A CA  1 
ATOM   1396 C  C   . TRP A  1 187 ? 34.158  6.738   42.897  1.00 27.03  ? 173 TRP A C   1 
ATOM   1397 O  O   . TRP A  1 187 ? 34.717  5.754   42.420  1.00 28.77  ? 173 TRP A O   1 
ATOM   1398 C  CB  . TRP A  1 187 ? 34.715  6.904   45.339  1.00 25.63  ? 173 TRP A CB  1 
ATOM   1399 C  CG  . TRP A  1 187 ? 34.229  6.980   46.762  1.00 24.79  ? 173 TRP A CG  1 
ATOM   1400 C  CD1 . TRP A  1 187 ? 34.250  5.987   47.696  1.00 26.02  ? 173 TRP A CD1 1 
ATOM   1401 C  CD2 . TRP A  1 187 ? 33.635  8.128   47.406  1.00 25.21  ? 173 TRP A CD2 1 
ATOM   1402 N  NE1 . TRP A  1 187 ? 33.718  6.434   48.876  1.00 29.00  ? 173 TRP A NE1 1 
ATOM   1403 C  CE2 . TRP A  1 187 ? 33.330  7.740   48.729  1.00 27.31  ? 173 TRP A CE2 1 
ATOM   1404 C  CE3 . TRP A  1 187 ? 33.335  9.433   46.998  1.00 28.11  ? 173 TRP A CE3 1 
ATOM   1405 C  CZ2 . TRP A  1 187 ? 32.740  8.615   49.638  1.00 28.91  ? 173 TRP A CZ2 1 
ATOM   1406 C  CZ3 . TRP A  1 187 ? 32.754  10.295  47.900  1.00 28.77  ? 173 TRP A CZ3 1 
ATOM   1407 C  CH2 . TRP A  1 187 ? 32.461  9.889   49.200  1.00 26.46  ? 173 TRP A CH2 1 
ATOM   1408 N  N   . ARG A  1 188 ? 34.021  7.908   42.261  1.00 27.18  ? 174 ARG A N   1 
ATOM   1409 C  CA  . ARG A  1 188 ? 34.688  8.240   41.012  1.00 29.03  ? 174 ARG A CA  1 
ATOM   1410 C  C   . ARG A  1 188 ? 35.427  9.565   41.204  1.00 25.44  ? 174 ARG A C   1 
ATOM   1411 O  O   . ARG A  1 188 ? 34.812  10.627  41.145  1.00 27.25  ? 174 ARG A O   1 
ATOM   1412 C  CB  . ARG A  1 188 ? 33.657  8.345   39.879  1.00 30.97  ? 174 ARG A CB  1 
ATOM   1413 C  CG  . ARG A  1 188 ? 34.133  9.074   38.629  1.00 38.30  ? 174 ARG A CG  1 
ATOM   1414 C  CD  . ARG A  1 188 ? 35.093  8.257   37.780  1.00 42.78  ? 174 ARG A CD  1 
ATOM   1415 N  NE  . ARG A  1 188 ? 35.359  8.873   36.473  1.00 48.18  ? 174 ARG A NE  1 
ATOM   1416 C  CZ  . ARG A  1 188 ? 36.219  9.861   36.242  1.00 51.51  ? 174 ARG A CZ  1 
ATOM   1417 N  NH1 . ARG A  1 188 ? 36.956  10.350  37.224  1.00 55.39  ? 174 ARG A NH1 1 
ATOM   1418 N  NH2 . ARG A  1 188 ? 36.355  10.343  35.019  1.00 48.64  ? 174 ARG A NH2 1 
ATOM   1419 N  N   . THR A  1 189 ? 36.742  9.504   41.454  1.00 26.68  ? 175 THR A N   1 
ATOM   1420 C  CA  . THR A  1 189 ? 37.511  10.716  41.709  1.00 28.68  ? 175 THR A CA  1 
ATOM   1421 C  C   . THR A  1 189 ? 37.908  11.356  40.381  1.00 26.33  ? 175 THR A C   1 
ATOM   1422 O  O   . THR A  1 189 ? 38.365  10.674  39.465  1.00 25.05  ? 175 THR A O   1 
ATOM   1423 C  CB  . THR A  1 189 ? 38.739  10.445  42.582  1.00 27.51  ? 175 THR A CB  1 
ATOM   1424 O  OG1 . THR A  1 189 ? 39.500  9.419   41.952  1.00 29.15  ? 175 THR A OG1 1 
ATOM   1425 C  CG2 . THR A  1 189 ? 38.372  10.038  43.998  1.00 29.76  ? 175 THR A CG2 1 
ATOM   1426 N  N   . VAL A  1 190 ? 37.719  12.679  40.302  1.00 22.97  ? 176 VAL A N   1 
ATOM   1427 C  CA  . VAL A  1 190 ? 38.214  13.484  39.197  1.00 22.25  ? 176 VAL A CA  1 
ATOM   1428 C  C   . VAL A  1 190 ? 39.677  13.823  39.484  1.00 23.00  ? 176 VAL A C   1 
ATOM   1429 O  O   . VAL A  1 190 ? 39.987  14.481  40.475  1.00 23.98  ? 176 VAL A O   1 
ATOM   1430 C  CB  . VAL A  1 190 ? 37.351  14.747  38.997  1.00 23.65  ? 176 VAL A CB  1 
ATOM   1431 C  CG1 . VAL A  1 190 ? 37.852  15.609  37.843  1.00 22.21  ? 176 VAL A CG1 1 
ATOM   1432 C  CG2 . VAL A  1 190 ? 35.875  14.405  38.807  1.00 25.41  ? 176 VAL A CG2 1 
ATOM   1433 N  N   . LYS A  1 191 ? 40.582  13.344  38.622  1.00 25.29  ? 177 LYS A N   1 
ATOM   1434 C  CA  . LYS A  1 191 ? 42.012  13.499  38.846  1.00 24.38  ? 177 LYS A CA  1 
ATOM   1435 C  C   . LYS A  1 191 ? 42.391  14.973  38.699  1.00 24.61  ? 177 LYS A C   1 
ATOM   1436 O  O   . LYS A  1 191 ? 41.704  15.727  38.014  1.00 23.12  ? 177 LYS A O   1 
ATOM   1437 C  CB  . LYS A  1 191 ? 42.791  12.585  37.892  1.00 27.88  ? 177 LYS A CB  1 
ATOM   1438 C  CG  . LYS A  1 191 ? 42.324  11.129  37.884  1.00 30.48  ? 177 LYS A CG  1 
ATOM   1439 C  CD  . LYS A  1 191 ? 42.240  10.501  39.271  1.00 31.51  ? 177 LYS A CD  1 
ATOM   1440 C  CE  . LYS A  1 191 ? 41.889  9.039   39.261  1.00 30.51  ? 177 LYS A CE  1 
ATOM   1441 N  NZ  . LYS A  1 191 ? 40.450  8.795   39.111  1.00 32.49  ? 177 LYS A NZ  1 
ATOM   1442 N  N   . ARG A  1 192 ? 43.490  15.373  39.354  1.00 24.04  ? 178 ARG A N   1 
ATOM   1443 C  CA  . ARG A  1 192 ? 43.887  16.772  39.420  1.00 24.96  ? 178 ARG A CA  1 
ATOM   1444 C  C   . ARG A  1 192 ? 43.961  17.370  38.015  1.00 28.77  ? 178 ARG A C   1 
ATOM   1445 O  O   . ARG A  1 192 ? 43.493  18.485  37.788  1.00 29.71  ? 178 ARG A O   1 
ATOM   1446 C  CB  . ARG A  1 192 ? 45.226  16.947  40.152  1.00 24.72  ? 178 ARG A CB  1 
ATOM   1447 C  CG  . ARG A  1 192 ? 45.729  18.386  40.189  1.00 23.18  ? 178 ARG A CG  1 
ATOM   1448 C  CD  . ARG A  1 192 ? 46.995  18.564  41.011  1.00 21.78  ? 178 ARG A CD  1 
ATOM   1449 N  NE  . ARG A  1 192 ? 46.816  18.133  42.400  1.00 22.41  ? 178 ARG A NE  1 
ATOM   1450 C  CZ  . ARG A  1 192 ? 47.793  18.040  43.293  1.00 21.33  ? 178 ARG A CZ  1 
ATOM   1451 N  NH1 . ARG A  1 192 ? 49.040  18.308  42.946  1.00 20.83  ? 178 ARG A NH1 1 
ATOM   1452 N  NH2 . ARG A  1 192 ? 47.519  17.667  44.528  1.00 20.48  ? 178 ARG A NH2 1 
ATOM   1453 N  N   . HIS A  1 193 ? 44.551  16.628  37.071  1.00 30.34  ? 179 HIS A N   1 
ATOM   1454 C  CA  . HIS A  1 193 ? 44.796  17.163  35.740  1.00 36.21  ? 179 HIS A CA  1 
ATOM   1455 C  C   . HIS A  1 193 ? 43.823  16.547  34.734  1.00 34.23  ? 179 HIS A C   1 
ATOM   1456 O  O   . HIS A  1 193 ? 44.142  16.434  33.553  1.00 40.06  ? 179 HIS A O   1 
ATOM   1457 C  CB  . HIS A  1 193 ? 46.271  16.970  35.359  1.00 36.54  ? 179 HIS A CB  1 
ATOM   1458 C  CG  . HIS A  1 193 ? 47.201  17.736  36.244  1.00 40.49  ? 179 HIS A CG  1 
ATOM   1459 N  ND1 . HIS A  1 193 ? 47.064  19.093  36.446  1.00 41.47  ? 179 HIS A ND1 1 
ATOM   1460 C  CD2 . HIS A  1 193 ? 48.262  17.357  36.971  1.00 38.73  ? 179 HIS A CD2 1 
ATOM   1461 C  CE1 . HIS A  1 193 ? 48.011  19.509  37.274  1.00 37.12  ? 179 HIS A CE1 1 
ATOM   1462 N  NE2 . HIS A  1 193 ? 48.749  18.472  37.607  1.00 40.07  ? 179 HIS A NE2 1 
ATOM   1463 N  N   . GLU A  1 194 ? 42.624  16.176  35.201  1.00 28.23  ? 180 GLU A N   1 
ATOM   1464 C  CA  . GLU A  1 194 ? 41.655  15.499  34.352  1.00 26.40  ? 180 GLU A CA  1 
ATOM   1465 C  C   . GLU A  1 194 ? 40.801  16.524  33.609  1.00 24.62  ? 180 GLU A C   1 
ATOM   1466 O  O   . GLU A  1 194 ? 40.389  17.535  34.173  1.00 26.40  ? 180 GLU A O   1 
ATOM   1467 C  CB  . GLU A  1 194 ? 40.769  14.545  35.157  1.00 27.26  ? 180 GLU A CB  1 
ATOM   1468 C  CG  . GLU A  1 194 ? 39.863  13.684  34.279  1.00 26.49  ? 180 GLU A CG  1 
ATOM   1469 C  CD  . GLU A  1 194 ? 39.171  12.541  34.999  1.00 26.15  ? 180 GLU A CD  1 
ATOM   1470 O  OE1 . GLU A  1 194 ? 39.433  12.349  36.206  1.00 25.17  ? 180 GLU A OE1 1 
ATOM   1471 O  OE2 . GLU A  1 194 ? 38.367  11.844  34.342  1.00 27.74  ? 180 GLU A OE2 1 
ATOM   1472 N  N   . ASP A  1 195 ? 40.537  16.237  32.330  1.00 26.02  ? 181 ASP A N   1 
ATOM   1473 C  CA  . ASP A  1 195 ? 39.653  17.049  31.510  1.00 27.96  ? 181 ASP A CA  1 
ATOM   1474 C  C   . ASP A  1 195 ? 38.226  16.970  32.051  1.00 27.97  ? 181 ASP A C   1 
ATOM   1475 O  O   . ASP A  1 195 ? 37.890  16.067  32.817  1.00 25.40  ? 181 ASP A O   1 
ATOM   1476 C  CB  . ASP A  1 195 ? 39.694  16.615  30.051  1.00 31.71  ? 181 ASP A CB  1 
ATOM   1477 C  CG  . ASP A  1 195 ? 40.913  17.072  29.261  1.00 34.72  ? 181 ASP A CG  1 
ATOM   1478 O  OD1 . ASP A  1 195 ? 41.779  17.752  29.853  1.00 31.28  ? 181 ASP A OD1 1 
ATOM   1479 O  OD2 . ASP A  1 195 ? 40.982  16.750  28.056  1.00 33.64  ? 181 ASP A OD2 1 
ATOM   1480 N  N   . ASN A  1 196 ? 37.395  17.928  31.626  1.00 26.32  ? 182 ASN A N   1 
ATOM   1481 C  CA  . ASN A  1 196 ? 35.969  17.926  31.912  1.00 31.26  ? 182 ASN A CA  1 
ATOM   1482 C  C   . ASN A  1 196 ? 35.389  16.558  31.549  1.00 31.96  ? 182 ASN A C   1 
ATOM   1483 O  O   . ASN A  1 196 ? 35.888  15.892  30.643  1.00 32.31  ? 182 ASN A O   1 
ATOM   1484 C  CB  . ASN A  1 196 ? 35.263  19.062  31.174  1.00 30.25  ? 182 ASN A CB  1 
ATOM   1485 C  CG  . ASN A  1 196 ? 35.758  20.427  31.594  1.00 33.00  ? 182 ASN A CG  1 
ATOM   1486 O  OD1 . ASN A  1 196 ? 35.608  21.400  30.846  1.00 41.42  ? 182 ASN A OD1 1 
ATOM   1487 N  ND2 . ASN A  1 196 ? 36.365  20.520  32.770  1.00 33.38  ? 182 ASN A ND2 1 
ATOM   1488 N  N   . ILE A  1 197 ? 34.335  16.145  32.266  1.00 29.07  ? 183 ILE A N   1 
ATOM   1489 C  CA  . ILE A  1 197 ? 33.711  14.847  32.058  1.00 30.58  ? 183 ILE A CA  1 
ATOM   1490 C  C   . ILE A  1 197 ? 32.318  15.047  31.463  1.00 31.03  ? 183 ILE A C   1 
ATOM   1491 O  O   . ILE A  1 197 ? 31.483  15.728  32.056  1.00 29.61  ? 183 ILE A O   1 
ATOM   1492 C  CB  . ILE A  1 197 ? 33.637  14.052  33.376  1.00 32.17  ? 183 ILE A CB  1 
ATOM   1493 C  CG1 . ILE A  1 197 ? 35.017  13.865  34.009  1.00 29.27  ? 183 ILE A CG1 1 
ATOM   1494 C  CG2 . ILE A  1 197 ? 32.923  12.713  33.167  1.00 32.58  ? 183 ILE A CG2 1 
ATOM   1495 C  CD1 . ILE A  1 197 ? 34.975  13.506  35.483  1.00 29.50  ? 183 ILE A CD1 1 
ATOM   1496 N  N   . LEU A  1 198 ? 32.080  14.441  30.293  1.00 31.24  ? 184 LEU A N   1 
ATOM   1497 C  CA  . LEU A  1 198 ? 30.748  14.397  29.711  1.00 37.85  ? 184 LEU A CA  1 
ATOM   1498 C  C   . LEU A  1 198 ? 29.954  13.284  30.395  1.00 37.56  ? 184 LEU A C   1 
ATOM   1499 O  O   . LEU A  1 198 ? 30.192  12.103  30.152  1.00 37.02  ? 184 LEU A O   1 
ATOM   1500 C  CB  . LEU A  1 198 ? 30.817  14.189  28.198  1.00 39.48  ? 184 LEU A CB  1 
ATOM   1501 C  CG  . LEU A  1 198 ? 29.477  14.295  27.460  1.00 44.38  ? 184 LEU A CG  1 
ATOM   1502 C  CD1 . LEU A  1 198 ? 28.921  15.710  27.550  1.00 41.92  ? 184 LEU A CD1 1 
ATOM   1503 C  CD2 . LEU A  1 198 ? 29.602  13.859  26.010  1.00 46.25  ? 184 LEU A CD2 1 
ATOM   1504 N  N   . LEU A  1 199 ? 29.008  13.688  31.252  1.00 36.93  ? 185 LEU A N   1 
ATOM   1505 C  CA  . LEU A  1 199 ? 28.272  12.773  32.112  1.00 36.05  ? 185 LEU A CA  1 
ATOM   1506 C  C   . LEU A  1 199 ? 27.067  12.218  31.357  1.00 35.23  ? 185 LEU A C   1 
ATOM   1507 O  O   . LEU A  1 199 ? 26.720  11.045  31.484  1.00 39.56  ? 185 LEU A O   1 
ATOM   1508 C  CB  . LEU A  1 199 ? 27.847  13.559  33.352  1.00 38.79  ? 185 LEU A CB  1 
ATOM   1509 C  CG  . LEU A  1 199 ? 27.595  12.743  34.623  1.00 41.60  ? 185 LEU A CG  1 
ATOM   1510 C  CD1 . LEU A  1 199 ? 28.791  11.862  34.940  1.00 45.16  ? 185 LEU A CD1 1 
ATOM   1511 C  CD2 . LEU A  1 199 ? 27.279  13.667  35.790  1.00 39.96  ? 185 LEU A CD2 1 
ATOM   1512 N  N   . ALA A  1 200 ? 26.441  13.102  30.576  1.00 33.91  ? 186 ALA A N   1 
ATOM   1513 C  CA  . ALA A  1 200 ? 25.271  12.795  29.773  1.00 37.05  ? 186 ALA A CA  1 
ATOM   1514 C  C   . ALA A  1 200 ? 25.127  13.893  28.724  1.00 34.94  ? 186 ALA A C   1 
ATOM   1515 O  O   . ALA A  1 200 ? 25.779  14.930  28.826  1.00 35.50  ? 186 ALA A O   1 
ATOM   1516 C  CB  . ALA A  1 200 ? 24.039  12.693  30.653  1.00 38.84  ? 186 ALA A CB  1 
ATOM   1517 N  N   . GLU A  1 201 ? 24.283  13.663  27.715  1.00 36.33  ? 187 GLU A N   1 
ATOM   1518 C  CA  . GLU A  1 201 ? 24.066  14.664  26.684  1.00 33.52  ? 187 GLU A CA  1 
ATOM   1519 C  C   . GLU A  1 201 ? 23.741  16.000  27.351  1.00 31.99  ? 187 GLU A C   1 
ATOM   1520 O  O   . GLU A  1 201 ? 22.748  16.116  28.068  1.00 29.78  ? 187 GLU A O   1 
ATOM   1521 C  CB  . GLU A  1 201 ? 22.951  14.234  25.730  1.00 34.50  ? 187 GLU A CB  1 
ATOM   1522 C  CG  . GLU A  1 201 ? 22.838  15.124  24.496  1.00 36.79  ? 187 GLU A CG  1 
ATOM   1523 C  CD  . GLU A  1 201 ? 21.683  14.773  23.574  1.00 41.80  ? 187 GLU A CD  1 
ATOM   1524 O  OE1 . GLU A  1 201 ? 21.587  13.598  23.166  1.00 48.18  ? 187 GLU A OE1 1 
ATOM   1525 O  OE2 . GLU A  1 201 ? 20.883  15.680  23.261  1.00 47.65  ? 187 GLU A OE2 1 
ATOM   1526 N  N   . GLY A  1 202 ? 24.602  16.999  27.121  1.00 27.62  ? 188 GLY A N   1 
ATOM   1527 C  CA  . GLY A  1 202 ? 24.373  18.355  27.594  1.00 28.32  ? 188 GLY A CA  1 
ATOM   1528 C  C   . GLY A  1 202 ? 24.678  18.530  29.082  1.00 27.97  ? 188 GLY A C   1 
ATOM   1529 O  O   . GLY A  1 202 ? 24.266  19.524  29.677  1.00 32.50  ? 188 GLY A O   1 
ATOM   1530 N  N   . VAL A  1 203 ? 25.394  17.569  29.683  1.00 29.54  ? 189 VAL A N   1 
ATOM   1531 C  CA  . VAL A  1 203 ? 25.779  17.670  31.084  1.00 30.26  ? 189 VAL A CA  1 
ATOM   1532 C  C   . VAL A  1 203 ? 27.268  17.349  31.223  1.00 30.54  ? 189 VAL A C   1 
ATOM   1533 O  O   . VAL A  1 203 ? 27.685  16.218  30.983  1.00 28.22  ? 189 VAL A O   1 
ATOM   1534 C  CB  . VAL A  1 203 ? 24.938  16.753  31.996  1.00 32.53  ? 189 VAL A CB  1 
ATOM   1535 C  CG1 . VAL A  1 203 ? 25.269  16.973  33.467  1.00 34.04  ? 189 VAL A CG1 1 
ATOM   1536 C  CG2 . VAL A  1 203 ? 23.440  16.915  31.758  1.00 33.32  ? 189 VAL A CG2 1 
ATOM   1537 N  N   . LYS A  1 204 ? 28.053  18.352  31.642  1.00 30.24  ? 190 LYS A N   1 
ATOM   1538 C  CA  . LYS A  1 204 ? 29.496  18.218  31.788  1.00 31.35  ? 190 LYS A CA  1 
ATOM   1539 C  C   . LYS A  1 204 ? 29.916  18.597  33.208  1.00 27.44  ? 190 LYS A C   1 
ATOM   1540 O  O   . LYS A  1 204 ? 29.499  19.631  33.725  1.00 28.21  ? 190 LYS A O   1 
ATOM   1541 C  CB  . LYS A  1 204 ? 30.224  19.125  30.787  1.00 38.17  ? 190 LYS A CB  1 
ATOM   1542 C  CG  . LYS A  1 204 ? 30.095  18.737  29.318  1.00 51.02  ? 190 LYS A CG  1 
ATOM   1543 C  CD  . LYS A  1 204 ? 30.471  19.863  28.360  1.00 62.67  ? 190 LYS A CD  1 
ATOM   1544 C  CE  . LYS A  1 204 ? 31.905  20.303  28.456  1.00 65.54  ? 190 LYS A CE  1 
ATOM   1545 N  NZ  . LYS A  1 204 ? 32.787  19.556  27.552  1.00 69.90  ? 190 LYS A NZ  1 
ATOM   1546 N  N   . VAL A  1 205 ? 30.752  17.750  33.825  1.00 26.23  ? 191 VAL A N   1 
ATOM   1547 C  CA  . VAL A  1 205 ? 31.381  18.068  35.099  1.00 22.63  ? 191 VAL A CA  1 
ATOM   1548 C  C   . VAL A  1 205 ? 32.630  18.904  34.820  1.00 23.90  ? 191 VAL A C   1 
ATOM   1549 O  O   . VAL A  1 205 ? 33.524  18.460  34.102  1.00 23.74  ? 191 VAL A O   1 
ATOM   1550 C  CB  . VAL A  1 205 ? 31.737  16.802  35.904  1.00 22.16  ? 191 VAL A CB  1 
ATOM   1551 C  CG1 . VAL A  1 205 ? 32.330  17.148  37.265  1.00 23.21  ? 191 VAL A CG1 1 
ATOM   1552 C  CG2 . VAL A  1 205 ? 30.548  15.860  36.064  1.00 22.86  ? 191 VAL A CG2 1 
ATOM   1553 N  N   . LEU A  1 206 ? 32.686  20.112  35.393  1.00 24.33  ? 192 LEU A N   1 
ATOM   1554 C  CA  . LEU A  1 206 ? 33.826  21.001  35.225  1.00 25.21  ? 192 LEU A CA  1 
ATOM   1555 C  C   . LEU A  1 206 ? 34.809  20.783  36.375  1.00 23.88  ? 192 LEU A C   1 
ATOM   1556 O  O   . LEU A  1 206 ? 34.417  20.817  37.540  1.00 23.66  ? 192 LEU A O   1 
ATOM   1557 C  CB  . LEU A  1 206 ? 33.342  22.452  35.172  1.00 24.72  ? 192 LEU A CB  1 
ATOM   1558 C  CG  . LEU A  1 206 ? 32.177  22.743  34.219  1.00 26.15  ? 192 LEU A CG  1 
ATOM   1559 C  CD1 . LEU A  1 206 ? 31.711  24.187  34.341  1.00 26.60  ? 192 LEU A CD1 1 
ATOM   1560 C  CD2 . LEU A  1 206 ? 32.556  22.428  32.784  1.00 29.36  ? 192 LEU A CD2 1 
ATOM   1561 N  N   . ASN A  1 207 ? 36.085  20.560  36.032  1.00 21.28  ? 193 ASN A N   1 
ATOM   1562 C  CA  . ASN A  1 207 ? 37.146  20.367  37.010  1.00 21.98  ? 193 ASN A CA  1 
ATOM   1563 C  C   . ASN A  1 207 ? 37.777  21.720  37.336  1.00 21.73  ? 193 ASN A C   1 
ATOM   1564 O  O   . ASN A  1 207 ? 38.667  22.180  36.622  1.00 21.07  ? 193 ASN A O   1 
ATOM   1565 C  CB  . ASN A  1 207 ? 38.180  19.362  36.506  1.00 23.08  ? 193 ASN A CB  1 
ATOM   1566 C  CG  . ASN A  1 207 ? 39.295  19.118  37.496  1.00 20.14  ? 193 ASN A CG  1 
ATOM   1567 O  OD1 . ASN A  1 207 ? 39.293  19.697  38.588  1.00 19.11  ? 193 ASN A OD1 1 
ATOM   1568 N  ND2 . ASN A  1 207 ? 40.252  18.276  37.133  1.00 24.33  ? 193 ASN A ND2 1 
ATOM   1569 N  N   . PHE A  1 208 ? 37.309  22.352  38.420  1.00 21.28  ? 194 PHE A N   1 
ATOM   1570 C  CA  . PHE A  1 208 ? 37.759  23.686  38.793  1.00 23.19  ? 194 PHE A CA  1 
ATOM   1571 C  C   . PHE A  1 208 ? 39.090  23.619  39.543  1.00 22.15  ? 194 PHE A C   1 
ATOM   1572 O  O   . PHE A  1 208 ? 39.827  24.602  39.584  1.00 22.98  ? 194 PHE A O   1 
ATOM   1573 C  CB  . PHE A  1 208 ? 36.704  24.403  39.645  1.00 24.57  ? 194 PHE A CB  1 
ATOM   1574 C  CG  . PHE A  1 208 ? 35.451  24.849  38.903  1.00 26.52  ? 194 PHE A CG  1 
ATOM   1575 C  CD1 . PHE A  1 208 ? 35.522  25.305  37.592  1.00 27.89  ? 194 PHE A CD1 1 
ATOM   1576 C  CD2 . PHE A  1 208 ? 34.207  24.827  39.525  1.00 27.40  ? 194 PHE A CD2 1 
ATOM   1577 C  CE1 . PHE A  1 208 ? 34.379  25.715  36.922  1.00 27.61  ? 194 PHE A CE1 1 
ATOM   1578 C  CE2 . PHE A  1 208 ? 33.067  25.237  38.849  1.00 29.13  ? 194 PHE A CE2 1 
ATOM   1579 C  CZ  . PHE A  1 208 ? 33.156  25.680  37.550  1.00 29.42  ? 194 PHE A CZ  1 
ATOM   1580 N  N   . GLY A  1 209 ? 39.387  22.466  40.152  1.00 21.69  ? 195 GLY A N   1 
ATOM   1581 C  CA  . GLY A  1 209 ? 40.607  22.303  40.929  1.00 21.95  ? 195 GLY A CA  1 
ATOM   1582 C  C   . GLY A  1 209 ? 40.572  23.106  42.229  1.00 21.09  ? 195 GLY A C   1 
ATOM   1583 O  O   . GLY A  1 209 ? 39.503  23.367  42.781  1.00 19.71  ? 195 GLY A O   1 
ATOM   1584 N  N   . SER A  1 210 ? 41.760  23.499  42.707  1.00 20.24  ? 196 SER A N   1 
ATOM   1585 C  CA  . SER A  1 210 ? 41.906  24.069  44.038  1.00 22.10  ? 196 SER A CA  1 
ATOM   1586 C  C   . SER A  1 210 ? 41.545  25.554  44.029  1.00 21.69  ? 196 SER A C   1 
ATOM   1587 O  O   . SER A  1 210 ? 41.823  26.272  43.069  1.00 19.42  ? 196 SER A O   1 
ATOM   1588 C  CB  . SER A  1 210 ? 43.297  23.837  44.584  1.00 22.62  ? 196 SER A CB  1 
ATOM   1589 O  OG  . SER A  1 210 ? 44.292  24.379  43.726  1.00 22.02  ? 196 SER A OG  1 
ATOM   1590 N  N   . GLY A  1 211 ? 40.912  25.996  45.121  1.00 22.46  ? 197 GLY A N   1 
ATOM   1591 C  CA  . GLY A  1 211 ? 40.506  27.382  45.287  1.00 21.60  ? 197 GLY A CA  1 
ATOM   1592 C  C   . GLY A  1 211 ? 39.820  27.585  46.636  1.00 21.03  ? 197 GLY A C   1 
ATOM   1593 O  O   . GLY A  1 211 ? 40.485  27.653  47.670  1.00 20.62  ? 197 GLY A O   1 
ATOM   1594 N  N   . HIS A  1 212 ? 38.484  27.671  46.610  1.00 22.28  ? 198 HIS A N   1 
ATOM   1595 C  CA  . HIS A  1 212 ? 37.689  27.707  47.828  1.00 21.69  ? 198 HIS A CA  1 
ATOM   1596 C  C   . HIS A  1 212 ? 38.132  26.562  48.735  1.00 20.73  ? 198 HIS A C   1 
ATOM   1597 O  O   . HIS A  1 212 ? 38.396  26.767  49.918  1.00 20.82  ? 198 HIS A O   1 
ATOM   1598 C  CB  . HIS A  1 212 ? 36.189  27.653  47.507  1.00 23.73  ? 198 HIS A CB  1 
ATOM   1599 C  CG  . HIS A  1 212 ? 35.308  27.408  48.692  1.00 23.50  ? 198 HIS A CG  1 
ATOM   1600 N  ND1 . HIS A  1 212 ? 35.152  28.320  49.713  1.00 27.86  ? 198 HIS A ND1 1 
ATOM   1601 C  CD2 . HIS A  1 212 ? 34.553  26.349  49.025  1.00 24.43  ? 198 HIS A CD2 1 
ATOM   1602 C  CE1 . HIS A  1 212 ? 34.319  27.823  50.621  1.00 27.80  ? 198 HIS A CE1 1 
ATOM   1603 N  NE2 . HIS A  1 212 ? 33.942  26.628  50.221  1.00 23.40  ? 198 HIS A NE2 1 
ATOM   1604 N  N   . ALA A  1 213 ? 38.224  25.361  48.153  1.00 19.84  ? 199 ALA A N   1 
ATOM   1605 C  CA  . ALA A  1 213 ? 38.621  24.166  48.881  1.00 20.38  ? 199 ALA A CA  1 
ATOM   1606 C  C   . ALA A  1 213 ? 39.711  23.429  48.100  1.00 20.13  ? 199 ALA A C   1 
ATOM   1607 O  O   . ALA A  1 213 ? 40.239  23.958  47.125  1.00 20.28  ? 199 ALA A O   1 
ATOM   1608 C  CB  . ALA A  1 213 ? 37.409  23.294  49.130  1.00 20.53  ? 199 ALA A CB  1 
ATOM   1609 N  N   . TRP A  1 214 ? 40.047  22.209  48.537  1.00 19.54  ? 200 TRP A N   1 
ATOM   1610 C  CA  . TRP A  1 214 ? 41.126  21.449  47.921  1.00 22.01  ? 200 TRP A CA  1 
ATOM   1611 C  C   . TRP A  1 214 ? 40.802  21.137  46.461  1.00 20.97  ? 200 TRP A C   1 
ATOM   1612 O  O   . TRP A  1 214 ? 41.682  21.189  45.605  1.00 22.66  ? 200 TRP A O   1 
ATOM   1613 C  CB  . TRP A  1 214 ? 41.406  20.152  48.696  1.00 22.16  ? 200 TRP A CB  1 
ATOM   1614 C  CG  . TRP A  1 214 ? 41.927  20.360  50.094  1.00 26.34  ? 200 TRP A CG  1 
ATOM   1615 C  CD1 . TRP A  1 214 ? 43.086  20.980  50.461  1.00 27.82  ? 200 TRP A CD1 1 
ATOM   1616 C  CD2 . TRP A  1 214 ? 41.312  19.898  51.318  1.00 26.36  ? 200 TRP A CD2 1 
ATOM   1617 N  NE1 . TRP A  1 214 ? 43.224  20.961  51.823  1.00 30.80  ? 200 TRP A NE1 1 
ATOM   1618 C  CE2 . TRP A  1 214 ? 42.157  20.300  52.376  1.00 29.24  ? 200 TRP A CE2 1 
ATOM   1619 C  CE3 . TRP A  1 214 ? 40.139  19.197  51.620  1.00 25.35  ? 200 TRP A CE3 1 
ATOM   1620 C  CZ2 . TRP A  1 214 ? 41.858  20.020  53.708  1.00 26.30  ? 200 TRP A CZ2 1 
ATOM   1621 C  CZ3 . TRP A  1 214 ? 39.848  18.919  52.937  1.00 24.44  ? 200 TRP A CZ3 1 
ATOM   1622 C  CH2 . TRP A  1 214 ? 40.698  19.326  53.965  1.00 27.47  ? 200 TRP A CH2 1 
ATOM   1623 N  N   . GLY A  1 215 ? 39.536  20.799  46.188  1.00 18.99  ? 201 GLY A N   1 
ATOM   1624 C  CA  . GLY A  1 215 ? 39.131  20.352  44.864  1.00 21.12  ? 201 GLY A CA  1 
ATOM   1625 C  C   . GLY A  1 215 ? 37.659  20.648  44.583  1.00 21.31  ? 201 GLY A C   1 
ATOM   1626 O  O   . GLY A  1 215 ? 36.773  20.018  45.157  1.00 23.33  ? 201 GLY A O   1 
ATOM   1627 N  N   . MET A  1 216 ? 37.420  21.594  43.668  1.00 20.65  ? 202 MET A N   1 
ATOM   1628 C  CA  . MET A  1 216 ? 36.084  22.088  43.374  1.00 22.57  ? 202 MET A CA  1 
ATOM   1629 C  C   . MET A  1 216 ? 35.596  21.524  42.040  1.00 23.12  ? 202 MET A C   1 
ATOM   1630 O  O   . MET A  1 216 ? 36.324  21.539  41.050  1.00 22.37  ? 202 MET A O   1 
ATOM   1631 C  CB  . MET A  1 216 ? 36.078  23.619  43.296  1.00 22.16  ? 202 MET A CB  1 
ATOM   1632 C  CG  . MET A  1 216 ? 36.611  24.297  44.545  1.00 25.90  ? 202 MET A CG  1 
ATOM   1633 S  SD  . MET A  1 216 ? 35.607  23.948  46.003  1.00 26.66  ? 202 MET A SD  1 
ATOM   1634 C  CE  . MET A  1 216 ? 34.069  24.782  45.586  1.00 29.13  ? 202 MET A CE  1 
ATOM   1635 N  N   . LEU A  1 217 ? 34.349  21.038  42.029  1.00 21.75  ? 203 LEU A N   1 
ATOM   1636 C  CA  . LEU A  1 217 ? 33.702  20.581  40.808  1.00 22.82  ? 203 LEU A CA  1 
ATOM   1637 C  C   . LEU A  1 217 ? 32.502  21.475  40.509  1.00 26.27  ? 203 LEU A C   1 
ATOM   1638 O  O   . LEU A  1 217 ? 31.740  21.821  41.411  1.00 24.87  ? 203 LEU A O   1 
ATOM   1639 C  CB  . LEU A  1 217 ? 33.276  19.118  40.944  1.00 23.40  ? 203 LEU A CB  1 
ATOM   1640 C  CG  . LEU A  1 217 ? 34.405  18.092  41.088  1.00 22.64  ? 203 LEU A CG  1 
ATOM   1641 C  CD1 . LEU A  1 217 ? 33.854  16.674  41.101  1.00 21.71  ? 203 LEU A CD1 1 
ATOM   1642 C  CD2 . LEU A  1 217 ? 35.440  18.261  39.987  1.00 21.76  ? 203 LEU A CD2 1 
ATOM   1643 N  N   . GLY A  1 218 ? 32.348  21.841  39.232  1.00 26.44  ? 204 GLY A N   1 
ATOM   1644 C  CA  . GLY A  1 218 ? 31.166  22.544  38.759  1.00 24.95  ? 204 GLY A CA  1 
ATOM   1645 C  C   . GLY A  1 218 ? 30.398  21.702  37.743  1.00 22.93  ? 204 GLY A C   1 
ATOM   1646 O  O   . GLY A  1 218 ? 30.798  20.582  37.430  1.00 21.90  ? 204 GLY A O   1 
ATOM   1647 N  N   . LEU A  1 219 ? 29.288  22.250  37.235  1.00 23.00  ? 205 LEU A N   1 
ATOM   1648 C  CA  . LEU A  1 219 ? 28.488  21.571  36.230  1.00 23.99  ? 205 LEU A CA  1 
ATOM   1649 C  C   . LEU A  1 219 ? 28.076  22.586  35.167  1.00 25.03  ? 205 LEU A C   1 
ATOM   1650 O  O   . LEU A  1 219 ? 27.661  23.696  35.491  1.00 26.47  ? 205 LEU A O   1 
ATOM   1651 C  CB  . LEU A  1 219 ? 27.268  20.921  36.888  1.00 27.12  ? 205 LEU A CB  1 
ATOM   1652 C  CG  . LEU A  1 219 ? 26.717  19.661  36.213  1.00 29.15  ? 205 LEU A CG  1 
ATOM   1653 C  CD1 . LEU A  1 219 ? 27.620  18.468  36.491  1.00 34.18  ? 205 LEU A CD1 1 
ATOM   1654 C  CD2 . LEU A  1 219 ? 25.289  19.362  36.657  1.00 29.40  ? 205 LEU A CD2 1 
ATOM   1655 N  N   . HIS A  1 220 ? 28.225  22.203  33.894  1.00 26.00  ? 206 HIS A N   1 
ATOM   1656 C  CA  . HIS A  1 220 ? 27.579  22.925  32.811  1.00 27.53  ? 206 HIS A CA  1 
ATOM   1657 C  C   . HIS A  1 220 ? 26.431  22.065  32.288  1.00 27.91  ? 206 HIS A C   1 
ATOM   1658 O  O   . HIS A  1 220 ? 26.638  20.914  31.908  1.00 28.49  ? 206 HIS A O   1 
ATOM   1659 C  CB  . HIS A  1 220 ? 28.578  23.325  31.718  1.00 29.93  ? 206 HIS A CB  1 
ATOM   1660 C  CG  . HIS A  1 220 ? 27.931  24.083  30.604  1.00 34.17  ? 206 HIS A CG  1 
ATOM   1661 N  ND1 . HIS A  1 220 ? 27.588  23.501  29.403  1.00 38.79  ? 206 HIS A ND1 1 
ATOM   1662 C  CD2 . HIS A  1 220 ? 27.546  25.365  30.516  1.00 32.02  ? 206 HIS A CD2 1 
ATOM   1663 C  CE1 . HIS A  1 220 ? 27.023  24.411  28.621  1.00 40.06  ? 206 HIS A CE1 1 
ATOM   1664 N  NE2 . HIS A  1 220 ? 26.986  25.551  29.277  1.00 32.11  ? 206 HIS A NE2 1 
ATOM   1665 N  N   . VAL A  1 221 ? 25.217  22.630  32.307  1.00 29.12  ? 207 VAL A N   1 
ATOM   1666 C  CA  . VAL A  1 221 ? 24.031  21.950  31.812  1.00 29.49  ? 207 VAL A CA  1 
ATOM   1667 C  C   . VAL A  1 221 ? 23.491  22.728  30.613  1.00 30.42  ? 207 VAL A C   1 
ATOM   1668 O  O   . VAL A  1 221 ? 23.240  23.928  30.711  1.00 34.07  ? 207 VAL A O   1 
ATOM   1669 C  CB  . VAL A  1 221 ? 22.958  21.801  32.911  1.00 31.36  ? 207 VAL A CB  1 
ATOM   1670 C  CG1 . VAL A  1 221 ? 21.699  21.108  32.396  1.00 33.22  ? 207 VAL A CG1 1 
ATOM   1671 C  CG2 . VAL A  1 221 ? 23.500  21.079  34.139  1.00 29.76  ? 207 VAL A CG2 1 
ATOM   1672 N  N   . GLU A  1 222 ? 23.333  22.033  29.481  1.00 30.48  ? 208 GLU A N   1 
ATOM   1673 C  CA  . GLU A  1 222 ? 22.717  22.610  28.296  1.00 34.55  ? 208 GLU A CA  1 
ATOM   1674 C  C   . GLU A  1 222 ? 21.274  22.113  28.198  1.00 36.19  ? 208 GLU A C   1 
ATOM   1675 O  O   . GLU A  1 222 ? 21.035  20.962  27.837  1.00 35.15  ? 208 GLU A O   1 
ATOM   1676 C  CB  . GLU A  1 222 ? 23.519  22.243  27.046  1.00 40.18  ? 208 GLU A CB  1 
ATOM   1677 C  CG  . GLU A  1 222 ? 23.001  22.903  25.771  1.00 42.22  ? 208 GLU A CG  1 
ATOM   1678 C  CD  . GLU A  1 222 ? 23.115  24.417  25.758  1.00 45.72  ? 208 GLU A CD  1 
ATOM   1679 O  OE1 . GLU A  1 222 ? 24.241  24.926  25.939  1.00 51.68  ? 208 GLU A OE1 1 
ATOM   1680 O  OE2 . GLU A  1 222 ? 22.079  25.088  25.566  1.00 53.33  ? 208 GLU A OE2 1 
ATOM   1681 N  N   . LEU A  1 223 ? 20.321  22.991  28.538  1.00 36.50  ? 209 LEU A N   1 
ATOM   1682 C  CA  . LEU A  1 223 ? 18.902  22.663  28.503  1.00 38.81  ? 209 LEU A CA  1 
ATOM   1683 C  C   . LEU A  1 223 ? 18.294  23.150  27.188  1.00 36.57  ? 209 LEU A C   1 
ATOM   1684 O  O   . LEU A  1 223 ? 18.481  24.302  26.803  1.00 36.56  ? 209 LEU A O   1 
ATOM   1685 C  CB  . LEU A  1 223 ? 18.197  23.289  29.707  1.00 39.14  ? 209 LEU A CB  1 
ATOM   1686 C  CG  . LEU A  1 223 ? 18.477  22.642  31.067  1.00 39.30  ? 209 LEU A CG  1 
ATOM   1687 C  CD1 . LEU A  1 223 ? 17.792  23.410  32.183  1.00 37.15  ? 209 LEU A CD1 1 
ATOM   1688 C  CD2 . LEU A  1 223 ? 18.041  21.185  31.079  1.00 41.40  ? 209 LEU A CD2 1 
ATOM   1689 N  N   . PRO A  1 224 ? 17.537  22.290  26.466  1.00 36.79  ? 210 PRO A N   1 
ATOM   1690 C  CA  . PRO A  1 224 ? 16.949  22.666  25.177  1.00 39.47  ? 210 PRO A CA  1 
ATOM   1691 C  C   . PRO A  1 224 ? 16.311  24.054  25.150  1.00 40.19  ? 210 PRO A C   1 
ATOM   1692 O  O   . PRO A  1 224 ? 16.547  24.830  24.226  1.00 42.41  ? 210 PRO A O   1 
ATOM   1693 C  CB  . PRO A  1 224 ? 15.904  21.557  24.957  1.00 38.50  ? 210 PRO A CB  1 
ATOM   1694 C  CG  . PRO A  1 224 ? 16.507  20.345  25.629  1.00 38.43  ? 210 PRO A CG  1 
ATOM   1695 C  CD  . PRO A  1 224 ? 17.222  20.904  26.852  1.00 40.11  ? 210 PRO A CD  1 
ATOM   1696 N  N   . GLU A  1 225 ? 15.502  24.355  26.172  1.00 41.81  ? 211 GLU A N   1 
ATOM   1697 C  CA  . GLU A  1 225 ? 14.747  25.598  26.216  1.00 46.16  ? 211 GLU A CA  1 
ATOM   1698 C  C   . GLU A  1 225 ? 15.554  26.679  26.936  1.00 45.42  ? 211 GLU A C   1 
ATOM   1699 O  O   . GLU A  1 225 ? 15.877  27.706  26.342  1.00 50.03  ? 211 GLU A O   1 
ATOM   1700 C  CB  . GLU A  1 225 ? 13.387  25.377  26.882  1.00 48.34  ? 211 GLU A CB  1 
ATOM   1701 C  CG  . GLU A  1 225 ? 12.520  24.333  26.183  1.00 55.99  ? 211 GLU A CG  1 
ATOM   1702 C  CD  . GLU A  1 225 ? 12.262  24.606  24.712  1.00 59.18  ? 211 GLU A CD  1 
ATOM   1703 O  OE1 . GLU A  1 225 ? 12.563  23.718  23.885  1.00 60.13  ? 211 GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A  1 225 ? 11.765  25.707  24.393  1.00 60.60  ? 211 GLU A OE2 1 
ATOM   1705 N  N   . THR A  1 226 ? 15.873  26.438  28.215  1.00 42.96  ? 212 THR A N   1 
ATOM   1706 C  CA  . THR A  1 226 ? 16.502  27.444  29.062  1.00 39.99  ? 212 THR A CA  1 
ATOM   1707 C  C   . THR A  1 226 ? 17.877  27.811  28.504  1.00 35.61  ? 212 THR A C   1 
ATOM   1708 O  O   . THR A  1 226 ? 18.329  28.944  28.656  1.00 32.31  ? 212 THR A O   1 
ATOM   1709 C  CB  . THR A  1 226 ? 16.614  26.939  30.502  1.00 42.04  ? 212 THR A CB  1 
ATOM   1710 O  OG1 . THR A  1 226 ? 15.332  26.439  30.873  1.00 42.25  ? 212 THR A OG1 1 
ATOM   1711 C  CG2 . THR A  1 226 ? 17.050  28.032  31.463  1.00 40.64  ? 212 THR A CG2 1 
ATOM   1712 N  N   . GLY A  1 227 ? 18.544  26.842  27.868  1.00 33.69  ? 213 GLY A N   1 
ATOM   1713 C  CA  . GLY A  1 227 ? 19.902  27.038  27.382  1.00 33.29  ? 213 GLY A CA  1 
ATOM   1714 C  C   . GLY A  1 227 ? 20.937  26.624  28.429  1.00 30.74  ? 213 GLY A C   1 
ATOM   1715 O  O   . GLY A  1 227 ? 20.744  25.635  29.133  1.00 30.06  ? 213 GLY A O   1 
ATOM   1716 N  N   . GLY A  1 228 ? 22.019  27.407  28.536  1.00 30.95  ? 214 GLY A N   1 
ATOM   1717 C  CA  . GLY A  1 228 ? 23.186  27.027  29.319  1.00 32.61  ? 214 GLY A CA  1 
ATOM   1718 C  C   . GLY A  1 228 ? 23.095  27.472  30.779  1.00 30.06  ? 214 GLY A C   1 
ATOM   1719 O  O   . GLY A  1 228 ? 22.682  28.593  31.074  1.00 30.06  ? 214 GLY A O   1 
ATOM   1720 N  N   . ILE A  1 229 ? 23.518  26.576  31.681  1.00 29.55  ? 215 ILE A N   1 
ATOM   1721 C  CA  . ILE A  1 229 ? 23.561  26.847  33.110  1.00 30.85  ? 215 ILE A CA  1 
ATOM   1722 C  C   . ILE A  1 229 ? 24.885  26.336  33.675  1.00 26.38  ? 215 ILE A C   1 
ATOM   1723 O  O   . ILE A  1 229 ? 25.249  25.184  33.453  1.00 27.81  ? 215 ILE A O   1 
ATOM   1724 C  CB  . ILE A  1 229 ? 22.377  26.184  33.843  1.00 32.25  ? 215 ILE A CB  1 
ATOM   1725 C  CG1 . ILE A  1 229 ? 21.016  26.622  33.294  1.00 35.37  ? 215 ILE A CG1 1 
ATOM   1726 C  CG2 . ILE A  1 229 ? 22.482  26.426  35.349  1.00 35.30  ? 215 ILE A CG2 1 
ATOM   1727 C  CD1 . ILE A  1 229 ? 19.838  25.868  33.891  1.00 37.29  ? 215 ILE A CD1 1 
ATOM   1728 N  N   . ILE A  1 230 ? 25.579  27.193  34.437  1.00 27.30  ? 216 ILE A N   1 
ATOM   1729 C  CA  . ILE A  1 230 ? 26.767  26.794  35.178  1.00 26.50  ? 216 ILE A CA  1 
ATOM   1730 C  C   . ILE A  1 230 ? 26.425  26.760  36.667  1.00 25.50  ? 216 ILE A C   1 
ATOM   1731 O  O   . ILE A  1 230 ? 26.070  27.784  37.244  1.00 26.66  ? 216 ILE A O   1 
ATOM   1732 C  CB  . ILE A  1 230 ? 27.951  27.744  34.896  1.00 26.33  ? 216 ILE A CB  1 
ATOM   1733 C  CG1 . ILE A  1 230 ? 28.330  27.776  33.412  1.00 27.24  ? 216 ILE A CG1 1 
ATOM   1734 C  CG2 . ILE A  1 230 ? 29.156  27.390  35.769  1.00 27.07  ? 216 ILE A CG2 1 
ATOM   1735 C  CD1 . ILE A  1 230 ? 29.290  28.895  33.040  1.00 26.05  ? 216 ILE A CD1 1 
ATOM   1736 N  N   . LEU A  1 231 ? 26.522  25.569  37.273  1.00 28.54  ? 217 LEU A N   1 
ATOM   1737 C  CA  . LEU A  1 231 ? 26.452  25.430  38.719  1.00 26.22  ? 217 LEU A CA  1 
ATOM   1738 C  C   . LEU A  1 231 ? 27.858  25.642  39.281  1.00 25.21  ? 217 LEU A C   1 
ATOM   1739 O  O   . LEU A  1 231 ? 28.734  24.799  39.102  1.00 26.13  ? 217 LEU A O   1 
ATOM   1740 C  CB  . LEU A  1 231 ? 25.886  24.057  39.093  1.00 26.30  ? 217 LEU A CB  1 
ATOM   1741 C  CG  . LEU A  1 231 ? 24.577  23.647  38.405  1.00 27.91  ? 217 LEU A CG  1 
ATOM   1742 C  CD1 . LEU A  1 231 ? 24.047  22.334  38.969  1.00 29.50  ? 217 LEU A CD1 1 
ATOM   1743 C  CD2 . LEU A  1 231 ? 23.519  24.734  38.514  1.00 29.67  ? 217 LEU A CD2 1 
ATOM   1744 N  N   . ALA A  1 232 ? 28.068  26.788  39.942  1.00 28.80  ? 218 ALA A N   1 
ATOM   1745 C  CA  . ALA A  1 232 ? 29.388  27.184  40.412  1.00 28.19  ? 218 ALA A CA  1 
ATOM   1746 C  C   . ALA A  1 232 ? 29.637  26.647  41.820  1.00 26.22  ? 218 ALA A C   1 
ATOM   1747 O  O   . ALA A  1 232 ? 30.785  26.472  42.228  1.00 23.50  ? 218 ALA A O   1 
ATOM   1748 C  CB  . ALA A  1 232 ? 29.513  28.693  40.377  1.00 30.23  ? 218 ALA A CB  1 
ATOM   1749 N  N   . SER A  1 233 ? 28.550  26.392  42.556  1.00 25.07  ? 219 SER A N   1 
ATOM   1750 C  CA  . SER A  1 233 ? 28.647  26.084  43.973  1.00 24.81  ? 219 SER A CA  1 
ATOM   1751 C  C   . SER A  1 233 ? 29.530  27.131  44.652  1.00 23.76  ? 219 SER A C   1 
ATOM   1752 O  O   . SER A  1 233 ? 29.442  28.314  44.330  1.00 22.59  ? 219 SER A O   1 
ATOM   1753 C  CB  . SER A  1 233 ? 29.155  24.681  44.193  1.00 26.34  ? 219 SER A CB  1 
ATOM   1754 O  OG  . SER A  1 233 ? 29.266  24.388  45.579  1.00 26.88  ? 219 SER A OG  1 
ATOM   1755 N  N   . ASP A  1 234 ? 30.398  26.689  45.571  1.00 22.96  ? 220 ASP A N   1 
ATOM   1756 C  CA  . ASP A  1 234 ? 31.140  27.606  46.425  1.00 24.19  ? 220 ASP A CA  1 
ATOM   1757 C  C   . ASP A  1 234 ? 32.358  28.189  45.704  1.00 25.78  ? 220 ASP A C   1 
ATOM   1758 O  O   . ASP A  1 234 ? 33.167  28.874  46.325  1.00 24.76  ? 220 ASP A O   1 
ATOM   1759 C  CB  . ASP A  1 234 ? 31.537  26.949  47.739  1.00 24.85  ? 220 ASP A CB  1 
ATOM   1760 C  CG  . ASP A  1 234 ? 30.414  26.832  48.762  1.00 30.65  ? 220 ASP A CG  1 
ATOM   1761 O  OD1 . ASP A  1 234 ? 29.291  27.282  48.446  1.00 31.22  ? 220 ASP A OD1 1 
ATOM   1762 O  OD2 . ASP A  1 234 ? 30.671  26.297  49.862  1.00 30.15  ? 220 ASP A OD2 1 
ATOM   1763 N  N   . ALA A  1 235 ? 32.492  27.928  44.399  1.00 26.71  ? 221 ALA A N   1 
ATOM   1764 C  CA  . ALA A  1 235 ? 33.536  28.573  43.617  1.00 27.62  ? 221 ALA A CA  1 
ATOM   1765 C  C   . ALA A  1 235 ? 33.212  30.062  43.492  1.00 29.28  ? 221 ALA A C   1 
ATOM   1766 O  O   . ALA A  1 235 ? 34.105  30.889  43.321  1.00 28.48  ? 221 ALA A O   1 
ATOM   1767 C  CB  . ALA A  1 235 ? 33.675  27.906  42.266  1.00 29.22  ? 221 ALA A CB  1 
ATOM   1768 N  N   . ILE A  1 236 ? 31.913  30.376  43.588  1.00 28.86  ? 222 ILE A N   1 
ATOM   1769 C  CA  . ILE A  1 236 ? 31.421  31.744  43.659  1.00 27.99  ? 222 ILE A CA  1 
ATOM   1770 C  C   . ILE A  1 236 ? 30.215  31.770  44.599  1.00 29.83  ? 222 ILE A C   1 
ATOM   1771 O  O   . ILE A  1 236 ? 29.143  31.277  44.251  1.00 30.32  ? 222 ILE A O   1 
ATOM   1772 C  CB  . ILE A  1 236 ? 31.047  32.287  42.266  1.00 25.86  ? 222 ILE A CB  1 
ATOM   1773 C  CG1 . ILE A  1 236 ? 32.047  31.862  41.186  1.00 28.12  ? 222 ILE A CG1 1 
ATOM   1774 C  CG2 . ILE A  1 236 ? 30.871  33.806  42.309  1.00 27.23  ? 222 ILE A CG2 1 
ATOM   1775 C  CD1 . ILE A  1 236 ? 31.559  32.096  39.767  1.00 27.51  ? 222 ILE A CD1 1 
ATOM   1776 N  N   . TYR A  1 237 ? 30.402  32.356  45.786  1.00 28.73  ? 223 TYR A N   1 
ATOM   1777 C  CA  . TYR A  1 237 ? 29.365  32.409  46.805  1.00 28.10  ? 223 TYR A CA  1 
ATOM   1778 C  C   . TYR A  1 237 ? 28.143  33.176  46.292  1.00 27.89  ? 223 TYR A C   1 
ATOM   1779 O  O   . TYR A  1 237 ? 27.026  32.662  46.342  1.00 28.46  ? 223 TYR A O   1 
ATOM   1780 C  CB  . TYR A  1 237 ? 29.943  33.051  48.072  1.00 28.34  ? 223 TYR A CB  1 
ATOM   1781 C  CG  . TYR A  1 237 ? 30.600  32.120  49.086  1.00 25.88  ? 223 TYR A CG  1 
ATOM   1782 C  CD1 . TYR A  1 237 ? 30.308  30.760  49.133  1.00 26.64  ? 223 TYR A CD1 1 
ATOM   1783 C  CD2 . TYR A  1 237 ? 31.493  32.617  50.029  1.00 28.20  ? 223 TYR A CD2 1 
ATOM   1784 C  CE1 . TYR A  1 237 ? 30.895  29.925  50.071  1.00 26.52  ? 223 TYR A CE1 1 
ATOM   1785 C  CE2 . TYR A  1 237 ? 32.084  31.795  50.974  1.00 27.91  ? 223 TYR A CE2 1 
ATOM   1786 C  CZ  . TYR A  1 237 ? 31.786  30.444  50.995  1.00 28.87  ? 223 TYR A CZ  1 
ATOM   1787 O  OH  . TYR A  1 237 ? 32.371  29.633  51.927  1.00 30.62  ? 223 TYR A OH  1 
ATOM   1788 N  N   . THR A  1 238 ? 28.362  34.411  45.815  1.00 28.58  ? 224 THR A N   1 
ATOM   1789 C  CA  . THR A  1 238 ? 27.276  35.329  45.494  1.00 30.29  ? 224 THR A CA  1 
ATOM   1790 C  C   . THR A  1 238 ? 27.663  36.217  44.312  1.00 34.16  ? 224 THR A C   1 
ATOM   1791 O  O   . THR A  1 238 ? 28.800  36.179  43.845  1.00 36.18  ? 224 THR A O   1 
ATOM   1792 C  CB  . THR A  1 238 ? 26.931  36.194  46.708  1.00 32.19  ? 224 THR A CB  1 
ATOM   1793 O  OG1 . THR A  1 238 ? 27.955  37.180  46.815  1.00 30.22  ? 224 THR A OG1 1 
ATOM   1794 C  CG2 . THR A  1 238 ? 26.827  35.397  47.994  1.00 32.64  ? 224 THR A CG2 1 
ATOM   1795 N  N   . ALA A  1 239 ? 26.698  37.029  43.854  1.00 29.28  ? 225 ALA A N   1 
ATOM   1796 C  CA  . ALA A  1 239 ? 26.924  37.983  42.779  1.00 30.67  ? 225 ALA A CA  1 
ATOM   1797 C  C   . ALA A  1 239 ? 27.955  39.018  43.222  1.00 31.56  ? 225 ALA A C   1 
ATOM   1798 O  O   . ALA A  1 239 ? 28.688  39.568  42.401  1.00 34.63  ? 225 ALA A O   1 
ATOM   1799 C  CB  . ALA A  1 239 ? 25.616  38.635  42.374  1.00 34.37  ? 225 ALA A CB  1 
ATOM   1800 N  N   . GLU A  1 240 ? 28.003  39.265  44.535  1.00 33.57  ? 226 GLU A N   1 
ATOM   1801 C  CA  . GLU A  1 240 ? 28.961  40.191  45.117  1.00 34.38  ? 226 GLU A CA  1 
ATOM   1802 C  C   . GLU A  1 240 ? 30.372  39.618  44.976  1.00 33.59  ? 226 GLU A C   1 
ATOM   1803 O  O   . GLU A  1 240 ? 31.324  40.351  44.714  1.00 32.92  ? 226 GLU A O   1 
ATOM   1804 C  CB  . GLU A  1 240 ? 28.617  40.460  46.583  1.00 35.95  ? 226 GLU A CB  1 
ATOM   1805 C  CG  . GLU A  1 240 ? 29.277  41.720  47.135  1.00 38.48  ? 226 GLU A CG  1 
ATOM   1806 C  CD  . GLU A  1 240 ? 29.152  41.913  48.635  1.00 39.54  ? 226 GLU A CD  1 
ATOM   1807 O  OE1 . GLU A  1 240 ? 28.521  41.069  49.308  1.00 40.43  ? 226 GLU A OE1 1 
ATOM   1808 O  OE2 . GLU A  1 240 ? 29.702  42.918  49.131  1.00 44.38  ? 226 GLU A OE2 1 
ATOM   1809 N  N   . SER A  1 241 ? 30.495  38.298  45.161  1.00 32.98  ? 227 SER A N   1 
ATOM   1810 C  CA  . SER A  1 241 ? 31.758  37.604  44.961  1.00 31.58  ? 227 SER A CA  1 
ATOM   1811 C  C   . SER A  1 241 ? 32.219  37.785  43.517  1.00 28.57  ? 227 SER A C   1 
ATOM   1812 O  O   . SER A  1 241 ? 33.387  38.071  43.257  1.00 31.10  ? 227 SER A O   1 
ATOM   1813 C  CB  . SER A  1 241 ? 31.632  36.138  45.307  1.00 31.02  ? 227 SER A CB  1 
ATOM   1814 O  OG  . SER A  1 241 ? 30.990  35.957  46.562  1.00 34.10  ? 227 SER A OG  1 
ATOM   1815 N  N   . TYR A  1 242 ? 31.264  37.633  42.592  1.00 31.01  ? 228 TYR A N   1 
ATOM   1816 C  CA  . TYR A  1 242 ? 31.527  37.548  41.165  1.00 28.27  ? 228 TYR A CA  1 
ATOM   1817 C  C   . TYR A  1 242 ? 32.020  38.893  40.633  1.00 31.27  ? 228 TYR A C   1 
ATOM   1818 O  O   . TYR A  1 242 ? 32.975  38.945  39.861  1.00 28.71  ? 228 TYR A O   1 
ATOM   1819 C  CB  . TYR A  1 242 ? 30.226  37.094  40.492  1.00 28.60  ? 228 TYR A CB  1 
ATOM   1820 C  CG  . TYR A  1 242 ? 30.341  36.564  39.068  1.00 29.65  ? 228 TYR A CG  1 
ATOM   1821 C  CD1 . TYR A  1 242 ? 31.344  35.671  38.703  1.00 28.92  ? 228 TYR A CD1 1 
ATOM   1822 C  CD2 . TYR A  1 242 ? 29.425  36.940  38.092  1.00 31.07  ? 228 TYR A CD2 1 
ATOM   1823 C  CE1 . TYR A  1 242 ? 31.436  35.178  37.411  1.00 28.19  ? 228 TYR A CE1 1 
ATOM   1824 C  CE2 . TYR A  1 242 ? 29.506  36.454  36.798  1.00 28.49  ? 228 TYR A CE2 1 
ATOM   1825 C  CZ  . TYR A  1 242 ? 30.513  35.570  36.457  1.00 29.93  ? 228 TYR A CZ  1 
ATOM   1826 O  OH  . TYR A  1 242 ? 30.588  35.096  35.180  1.00 28.35  ? 228 TYR A OH  1 
ATOM   1827 N  N   . GLY A  1 243 ? 31.348  39.976  41.034  1.00 33.26  ? 229 GLY A N   1 
ATOM   1828 C  CA  . GLY A  1 243 ? 31.685  41.302  40.540  1.00 35.55  ? 229 GLY A CA  1 
ATOM   1829 C  C   . GLY A  1 243 ? 31.383  41.436  39.049  1.00 35.32  ? 229 GLY A C   1 
ATOM   1830 O  O   . GLY A  1 243 ? 30.338  40.982  38.586  1.00 35.98  ? 229 GLY A O   1 
ATOM   1831 N  N   . PRO A  1 244 ? 32.290  42.044  38.247  1.00 37.29  ? 230 PRO A N   1 
ATOM   1832 C  CA  . PRO A  1 244 ? 33.614  42.448  38.722  1.00 41.84  ? 230 PRO A CA  1 
ATOM   1833 C  C   . PRO A  1 244 ? 33.537  43.680  39.620  1.00 44.79  ? 230 PRO A C   1 
ATOM   1834 O  O   . PRO A  1 244 ? 32.564  44.427  39.569  1.00 42.66  ? 230 PRO A O   1 
ATOM   1835 C  CB  . PRO A  1 244 ? 34.425  42.734  37.436  1.00 43.06  ? 230 PRO A CB  1 
ATOM   1836 C  CG  . PRO A  1 244 ? 33.483  42.427  36.280  1.00 38.98  ? 230 PRO A CG  1 
ATOM   1837 C  CD  . PRO A  1 244 ? 32.071  42.408  36.840  1.00 37.73  ? 230 PRO A CD  1 
ATOM   1838 N  N   . PRO A  1 245 ? 34.557  43.926  40.473  1.00 45.36  ? 231 PRO A N   1 
ATOM   1839 C  CA  . PRO A  1 245 ? 35.716  43.040  40.579  1.00 39.91  ? 231 PRO A CA  1 
ATOM   1840 C  C   . PRO A  1 245 ? 35.403  41.899  41.544  1.00 36.18  ? 231 PRO A C   1 
ATOM   1841 O  O   . PRO A  1 245 ? 34.398  41.943  42.250  1.00 30.60  ? 231 PRO A O   1 
ATOM   1842 C  CB  . PRO A  1 245 ? 36.800  44.002  41.097  1.00 38.73  ? 231 PRO A CB  1 
ATOM   1843 C  CG  . PRO A  1 245 ? 36.039  44.970  41.986  1.00 42.67  ? 231 PRO A CG  1 
ATOM   1844 C  CD  . PRO A  1 245 ? 34.627  45.055  41.414  1.00 44.25  ? 231 PRO A CD  1 
ATOM   1845 N  N   . ILE A  1 246 ? 36.261  40.874  41.565  1.00 33.99  ? 232 ILE A N   1 
ATOM   1846 C  CA  . ILE A  1 246 ? 36.046  39.727  42.434  1.00 32.38  ? 232 ILE A CA  1 
ATOM   1847 C  C   . ILE A  1 246 ? 36.218  40.164  43.886  1.00 33.18  ? 232 ILE A C   1 
ATOM   1848 O  O   . ILE A  1 246 ? 37.126  40.928  44.205  1.00 34.38  ? 232 ILE A O   1 
ATOM   1849 C  CB  . ILE A  1 246 ? 36.997  38.569  42.075  1.00 31.60  ? 232 ILE A CB  1 
ATOM   1850 C  CG1 . ILE A  1 246 ? 36.756  38.058  40.654  1.00 35.06  ? 232 ILE A CG1 1 
ATOM   1851 C  CG2 . ILE A  1 246 ? 36.891  37.442  43.102  1.00 31.45  ? 232 ILE A CG2 1 
ATOM   1852 C  CD1 . ILE A  1 246 ? 37.881  37.199  40.105  1.00 35.53  ? 232 ILE A CD1 1 
ATOM   1853 N  N   . LYS A  1 247 ? 35.332  39.667  44.757  1.00 32.02  ? 233 LYS A N   1 
ATOM   1854 C  CA  . LYS A  1 247 ? 35.468  39.847  46.194  1.00 31.90  ? 233 LYS A CA  1 
ATOM   1855 C  C   . LYS A  1 247 ? 35.589  38.468  46.840  1.00 30.15  ? 233 LYS A C   1 
ATOM   1856 O  O   . LYS A  1 247 ? 34.586  37.800  47.092  1.00 28.93  ? 233 LYS A O   1 
ATOM   1857 C  CB  . LYS A  1 247 ? 34.301  40.680  46.742  1.00 34.09  ? 233 LYS A CB  1 
ATOM   1858 C  CG  . LYS A  1 247 ? 34.191  42.084  46.151  1.00 36.40  ? 233 LYS A CG  1 
ATOM   1859 C  CD  . LYS A  1 247 ? 32.986  42.888  46.626  1.00 40.68  ? 233 LYS A CD  1 
ATOM   1860 C  CE  . LYS A  1 247 ? 33.217  43.627  47.909  1.00 42.95  ? 233 LYS A CE  1 
ATOM   1861 N  NZ  . LYS A  1 247 ? 32.019  44.362  48.330  1.00 47.19  ? 233 LYS A NZ  1 
ATOM   1862 N  N   . PRO A  1 248 ? 36.832  38.002  47.106  1.00 32.37  ? 234 PRO A N   1 
ATOM   1863 C  CA  . PRO A  1 248 ? 37.070  36.636  47.581  1.00 33.58  ? 234 PRO A CA  1 
ATOM   1864 C  C   . PRO A  1 248 ? 36.620  36.389  49.018  1.00 30.89  ? 234 PRO A C   1 
ATOM   1865 O  O   . PRO A  1 248 ? 36.515  37.322  49.811  1.00 31.65  ? 234 PRO A O   1 
ATOM   1866 C  CB  . PRO A  1 248 ? 38.593  36.438  47.419  1.00 32.03  ? 234 PRO A CB  1 
ATOM   1867 C  CG  . PRO A  1 248 ? 39.181  37.837  47.369  1.00 33.76  ? 234 PRO A CG  1 
ATOM   1868 C  CD  . PRO A  1 248 ? 38.071  38.777  46.936  1.00 31.90  ? 234 PRO A CD  1 
ATOM   1869 N  N   . PRO A  1 249 ? 36.348  35.115  49.389  1.00 29.17  ? 235 PRO A N   1 
ATOM   1870 C  CA  . PRO A  1 249 ? 35.899  34.770  50.739  1.00 31.71  ? 235 PRO A CA  1 
ATOM   1871 C  C   . PRO A  1 249 ? 37.025  34.616  51.757  1.00 33.46  ? 235 PRO A C   1 
ATOM   1872 O  O   . PRO A  1 249 ? 38.200  34.579  51.395  1.00 39.74  ? 235 PRO A O   1 
ATOM   1873 C  CB  . PRO A  1 249 ? 35.184  33.429  50.493  1.00 28.66  ? 235 PRO A CB  1 
ATOM   1874 C  CG  . PRO A  1 249 ? 36.004  32.783  49.395  1.00 28.31  ? 235 PRO A CG  1 
ATOM   1875 C  CD  . PRO A  1 249 ? 36.444  33.939  48.508  1.00 27.34  ? 235 PRO A CD  1 
ATOM   1876 N  N   . GLY A  1 250 ? 36.638  34.518  53.034  1.00 33.78  ? 236 GLY A N   1 
ATOM   1877 C  CA  . GLY A  1 250 ? 37.559  34.182  54.107  1.00 37.82  ? 236 GLY A CA  1 
ATOM   1878 C  C   . GLY A  1 250 ? 37.790  32.673  54.195  1.00 40.05  ? 236 GLY A C   1 
ATOM   1879 O  O   . GLY A  1 250 ? 38.875  32.236  54.573  1.00 41.00  ? 236 GLY A O   1 
ATOM   1880 N  N   . ILE A  1 251 ? 36.757  31.883  53.861  1.00 46.53  ? 237 ILE A N   1 
ATOM   1881 C  CA  . ILE A  1 251 ? 36.909  30.440  53.719  1.00 46.47  ? 237 ILE A CA  1 
ATOM   1882 C  C   . ILE A  1 251 ? 37.562  30.166  52.365  1.00 43.00  ? 237 ILE A C   1 
ATOM   1883 O  O   . ILE A  1 251 ? 36.889  30.203  51.336  1.00 37.21  ? 237 ILE A O   1 
ATOM   1884 C  CB  . ILE A  1 251 ? 35.568  29.684  53.850  1.00 47.50  ? 237 ILE A CB  1 
ATOM   1885 C  CG1 . ILE A  1 251 ? 34.833  29.989  55.160  1.00 48.76  ? 237 ILE A CG1 1 
ATOM   1886 C  CG2 . ILE A  1 251 ? 35.786  28.179  53.679  1.00 45.01  ? 237 ILE A CG2 1 
ATOM   1887 C  CD1 . ILE A  1 251 ? 33.685  29.037  55.461  1.00 47.25  ? 237 ILE A CD1 1 
ATOM   1888 N  N   . ILE A  1 252 ? 38.871  29.877  52.379  1.00 41.68  ? 238 ILE A N   1 
ATOM   1889 C  CA  . ILE A  1 252 ? 39.656  29.818  51.154  1.00 37.76  ? 238 ILE A CA  1 
ATOM   1890 C  C   . ILE A  1 252 ? 40.933  29.013  51.400  1.00 32.00  ? 238 ILE A C   1 
ATOM   1891 O  O   . ILE A  1 252 ? 41.594  29.186  52.421  1.00 37.56  ? 238 ILE A O   1 
ATOM   1892 C  CB  . ILE A  1 252 ? 39.964  31.245  50.662  1.00 38.33  ? 238 ILE A CB  1 
ATOM   1893 C  CG1 . ILE A  1 252 ? 40.408  31.275  49.198  1.00 36.86  ? 238 ILE A CG1 1 
ATOM   1894 C  CG2 . ILE A  1 252 ? 40.984  31.923  51.577  1.00 36.51  ? 238 ILE A CG2 1 
ATOM   1895 C  CD1 . ILE A  1 252 ? 40.275  32.638  48.542  1.00 40.59  ? 238 ILE A CD1 1 
ATOM   1896 N  N   . TYR A  1 253 ? 41.267  28.135  50.447  1.00 24.42  ? 239 TYR A N   1 
ATOM   1897 C  CA  . TYR A  1 253 ? 42.459  27.305  50.523  1.00 22.27  ? 239 TYR A CA  1 
ATOM   1898 C  C   . TYR A  1 253 ? 43.550  27.881  49.618  1.00 19.80  ? 239 TYR A C   1 
ATOM   1899 O  O   . TYR A  1 253 ? 44.658  28.158  50.072  1.00 20.35  ? 239 TYR A O   1 
ATOM   1900 C  CB  . TYR A  1 253 ? 42.105  25.862  50.141  1.00 21.98  ? 239 TYR A CB  1 
ATOM   1901 C  CG  . TYR A  1 253 ? 43.311  24.968  49.879  1.00 21.28  ? 239 TYR A CG  1 
ATOM   1902 C  CD1 . TYR A  1 253 ? 44.209  24.658  50.895  1.00 22.40  ? 239 TYR A CD1 1 
ATOM   1903 C  CD2 . TYR A  1 253 ? 43.547  24.421  48.622  1.00 20.50  ? 239 TYR A CD2 1 
ATOM   1904 C  CE1 . TYR A  1 253 ? 45.313  23.852  50.665  1.00 21.43  ? 239 TYR A CE1 1 
ATOM   1905 C  CE2 . TYR A  1 253 ? 44.644  23.610  48.381  1.00 21.36  ? 239 TYR A CE2 1 
ATOM   1906 C  CZ  . TYR A  1 253 ? 45.528  23.322  49.405  1.00 20.59  ? 239 TYR A CZ  1 
ATOM   1907 O  OH  . TYR A  1 253 ? 46.612  22.524  49.174  1.00 23.18  ? 239 TYR A OH  1 
ATOM   1908 N  N   . ASP A  1 254 ? 43.208  28.058  48.337  1.00 18.65  ? 240 ASP A N   1 
ATOM   1909 C  CA  . ASP A  1 254 ? 44.156  28.449  47.305  1.00 19.59  ? 240 ASP A CA  1 
ATOM   1910 C  C   . ASP A  1 254 ? 43.675  29.739  46.644  1.00 17.87  ? 240 ASP A C   1 
ATOM   1911 O  O   . ASP A  1 254 ? 42.854  29.702  45.731  1.00 19.33  ? 240 ASP A O   1 
ATOM   1912 C  CB  . ASP A  1 254 ? 44.331  27.325  46.292  1.00 20.33  ? 240 ASP A CB  1 
ATOM   1913 C  CG  . ASP A  1 254 ? 45.138  27.672  45.048  1.00 20.44  ? 240 ASP A CG  1 
ATOM   1914 O  OD1 . ASP A  1 254 ? 45.720  28.776  45.010  1.00 20.61  ? 240 ASP A OD1 1 
ATOM   1915 O  OD2 . ASP A  1 254 ? 45.169  26.836  44.120  1.00 22.07  ? 240 ASP A OD2 1 
ATOM   1916 N  N   . SER A  1 255 ? 44.201  30.879  47.106  1.00 21.36  ? 241 SER A N   1 
ATOM   1917 C  CA  . SER A  1 255 ? 43.700  32.183  46.691  1.00 21.84  ? 241 SER A CA  1 
ATOM   1918 C  C   . SER A  1 255 ? 43.880  32.389  45.187  1.00 21.45  ? 241 SER A C   1 
ATOM   1919 O  O   . SER A  1 255 ? 42.980  32.899  44.524  1.00 22.74  ? 241 SER A O   1 
ATOM   1920 C  CB  . SER A  1 255 ? 44.342  33.298  47.482  1.00 20.83  ? 241 SER A CB  1 
ATOM   1921 O  OG  . SER A  1 255 ? 45.756  33.283  47.344  1.00 23.88  ? 241 SER A OG  1 
ATOM   1922 N  N   A LEU A  1 256 ? 45.043  31.991  44.656  0.60 21.25  ? 242 LEU A N   1 
ATOM   1923 N  N   B LEU A  1 256 ? 45.055  32.004  44.670  0.40 21.28  ? 242 LEU A N   1 
ATOM   1924 C  CA  A LEU A  1 256 ? 45.328  32.157  43.240  0.60 22.20  ? 242 LEU A CA  1 
ATOM   1925 C  CA  B LEU A  1 256 ? 45.363  32.126  43.253  0.40 21.58  ? 242 LEU A CA  1 
ATOM   1926 C  C   A LEU A  1 256 ? 44.370  31.286  42.428  0.60 22.42  ? 242 LEU A C   1 
ATOM   1927 C  C   B LEU A  1 256 ? 44.365  31.293  42.451  0.40 21.89  ? 242 LEU A C   1 
ATOM   1928 O  O   A LEU A  1 256 ? 43.774  31.751  41.457  0.60 20.78  ? 242 LEU A O   1 
ATOM   1929 O  O   B LEU A  1 256 ? 43.742  31.789  41.514  0.40 20.42  ? 242 LEU A O   1 
ATOM   1930 C  CB  A LEU A  1 256 ? 46.792  31.829  42.939  0.60 21.04  ? 242 LEU A CB  1 
ATOM   1931 C  CB  B LEU A  1 256 ? 46.803  31.681  42.981  0.40 20.31  ? 242 LEU A CB  1 
ATOM   1932 C  CG  A LEU A  1 256 ? 47.829  32.813  43.493  0.60 22.68  ? 242 LEU A CG  1 
ATOM   1933 C  CG  B LEU A  1 256 ? 47.917  32.619  43.461  0.40 20.82  ? 242 LEU A CG  1 
ATOM   1934 C  CD1 A LEU A  1 256 ? 49.125  32.766  42.690  0.60 22.03  ? 242 LEU A CD1 1 
ATOM   1935 C  CD1 B LEU A  1 256 ? 49.288  32.092  43.053  0.40 20.50  ? 242 LEU A CD1 1 
ATOM   1936 C  CD2 A LEU A  1 256 ? 47.274  34.228  43.529  0.60 24.11  ? 242 LEU A CD2 1 
ATOM   1937 C  CD2 B LEU A  1 256 ? 47.718  34.033  42.935  0.40 20.68  ? 242 LEU A CD2 1 
ATOM   1938 N  N   . GLY A  1 257 ? 44.233  30.018  42.833  1.00 22.04  ? 243 GLY A N   1 
ATOM   1939 C  CA  . GLY A  1 257 ? 43.333  29.091  42.163  1.00 21.24  ? 243 GLY A CA  1 
ATOM   1940 C  C   . GLY A  1 257 ? 41.883  29.573  42.214  1.00 19.77  ? 243 GLY A C   1 
ATOM   1941 O  O   . GLY A  1 257 ? 41.126  29.384  41.265  1.00 19.37  ? 243 GLY A O   1 
ATOM   1942 N  N   . TYR A  1 258 ? 41.504  30.200  43.332  1.00 19.93  ? 244 TYR A N   1 
ATOM   1943 C  CA  . TYR A  1 258 ? 40.150  30.707  43.493  1.00 22.02  ? 244 TYR A CA  1 
ATOM   1944 C  C   . TYR A  1 258 ? 39.892  31.800  42.457  1.00 21.95  ? 244 TYR A C   1 
ATOM   1945 O  O   . TYR A  1 258 ? 38.855  31.802  41.798  1.00 22.43  ? 244 TYR A O   1 
ATOM   1946 C  CB  . TYR A  1 258 ? 39.896  31.243  44.906  1.00 22.42  ? 244 TYR A CB  1 
ATOM   1947 C  CG  . TYR A  1 258 ? 38.586  32.013  45.018  1.00 22.39  ? 244 TYR A CG  1 
ATOM   1948 C  CD1 . TYR A  1 258 ? 38.512  33.352  44.652  1.00 25.58  ? 244 TYR A CD1 1 
ATOM   1949 C  CD2 . TYR A  1 258 ? 37.417  31.398  45.457  1.00 23.79  ? 244 TYR A CD2 1 
ATOM   1950 C  CE1 . TYR A  1 258 ? 37.323  34.059  44.732  1.00 26.87  ? 244 TYR A CE1 1 
ATOM   1951 C  CE2 . TYR A  1 258 ? 36.222  32.095  45.544  1.00 23.60  ? 244 TYR A CE2 1 
ATOM   1952 C  CZ  . TYR A  1 258 ? 36.174  33.429  45.178  1.00 24.57  ? 244 TYR A CZ  1 
ATOM   1953 O  OH  . TYR A  1 258 ? 35.002  34.124  45.260  1.00 24.78  ? 244 TYR A OH  1 
ATOM   1954 N  N   . MET A  1 259 ? 40.847  32.727  42.319  1.00 23.45  ? 245 MET A N   1 
ATOM   1955 C  CA  . MET A  1 259 ? 40.706  33.844  41.398  1.00 25.43  ? 245 MET A CA  1 
ATOM   1956 C  C   . MET A  1 259 ? 40.648  33.315  39.966  1.00 23.57  ? 245 MET A C   1 
ATOM   1957 O  O   . MET A  1 259 ? 39.828  33.764  39.169  1.00 23.52  ? 245 MET A O   1 
ATOM   1958 C  CB  . MET A  1 259 ? 41.866  34.837  41.550  1.00 26.49  ? 245 MET A CB  1 
ATOM   1959 C  CG  . MET A  1 259 ? 41.979  35.447  42.939  1.00 28.43  ? 245 MET A CG  1 
ATOM   1960 S  SD  . MET A  1 259 ? 40.562  36.461  43.411  1.00 31.99  ? 245 MET A SD  1 
ATOM   1961 C  CE  . MET A  1 259 ? 40.698  37.823  42.246  1.00 36.62  ? 245 MET A CE  1 
ATOM   1962 N  N   . ASN A  1 260 ? 41.527  32.354  39.653  1.00 24.94  ? 246 ASN A N   1 
ATOM   1963 C  CA  . ASN A  1 260 ? 41.586  31.757  38.328  1.00 22.78  ? 246 ASN A CA  1 
ATOM   1964 C  C   . ASN A  1 260 ? 40.240  31.108  37.998  1.00 24.01  ? 246 ASN A C   1 
ATOM   1965 O  O   . ASN A  1 260 ? 39.729  31.260  36.888  1.00 24.47  ? 246 ASN A O   1 
ATOM   1966 C  CB  . ASN A  1 260 ? 42.740  30.761  38.209  1.00 26.34  ? 246 ASN A CB  1 
ATOM   1967 C  CG  . ASN A  1 260 ? 44.104  31.417  38.236  1.00 29.42  ? 246 ASN A CG  1 
ATOM   1968 O  OD1 . ASN A  1 260 ? 44.220  32.630  38.028  1.00 30.98  ? 246 ASN A OD1 1 
ATOM   1969 N  ND2 . ASN A  1 260 ? 45.148  30.635  38.471  1.00 33.95  ? 246 ASN A ND2 1 
ATOM   1970 N  N   . THR A  1 261 ? 39.667  30.380  38.967  1.00 23.16  ? 247 THR A N   1 
ATOM   1971 C  CA  . THR A  1 261 ? 38.431  29.641  38.745  1.00 21.56  ? 247 THR A CA  1 
ATOM   1972 C  C   . THR A  1 261 ? 37.293  30.606  38.413  1.00 20.79  ? 247 THR A C   1 
ATOM   1973 O  O   . THR A  1 261 ? 36.542  30.363  37.472  1.00 19.51  ? 247 THR A O   1 
ATOM   1974 C  CB  . THR A  1 261 ? 38.102  28.754  39.949  1.00 23.54  ? 247 THR A CB  1 
ATOM   1975 O  OG1 . THR A  1 261 ? 39.055  27.696  39.909  1.00 21.38  ? 247 THR A OG1 1 
ATOM   1976 C  CG2 . THR A  1 261 ? 36.703  28.165  39.889  1.00 23.43  ? 247 THR A CG2 1 
ATOM   1977 N  N   . VAL A  1 262 ? 37.174  31.701  39.175  1.00 22.02  ? 248 VAL A N   1 
ATOM   1978 C  CA  . VAL A  1 262 ? 36.091  32.657  38.981  1.00 25.07  ? 248 VAL A CA  1 
ATOM   1979 C  C   . VAL A  1 262 ? 36.163  33.224  37.563  1.00 26.18  ? 248 VAL A C   1 
ATOM   1980 O  O   . VAL A  1 262 ? 35.140  33.338  36.890  1.00 24.64  ? 248 VAL A O   1 
ATOM   1981 C  CB  . VAL A  1 262 ? 36.104  33.796  40.020  1.00 23.47  ? 248 VAL A CB  1 
ATOM   1982 C  CG1 . VAL A  1 262 ? 35.009  34.822  39.747  1.00 22.71  ? 248 VAL A CG1 1 
ATOM   1983 C  CG2 . VAL A  1 262 ? 35.999  33.270  41.447  1.00 21.46  ? 248 VAL A CG2 1 
ATOM   1984 N  N   . GLU A  1 263 ? 37.376  33.587  37.123  1.00 27.06  ? 249 GLU A N   1 
ATOM   1985 C  CA  . GLU A  1 263 ? 37.564  34.230  35.832  1.00 24.90  ? 249 GLU A CA  1 
ATOM   1986 C  C   . GLU A  1 263 ? 37.317  33.220  34.715  1.00 23.99  ? 249 GLU A C   1 
ATOM   1987 O  O   . GLU A  1 263 ? 36.844  33.580  33.640  1.00 22.61  ? 249 GLU A O   1 
ATOM   1988 C  CB  . GLU A  1 263 ? 38.951  34.870  35.725  1.00 28.88  ? 249 GLU A CB  1 
ATOM   1989 C  CG  . GLU A  1 263 ? 39.088  36.148  36.548  1.00 32.68  ? 249 GLU A CG  1 
ATOM   1990 C  CD  . GLU A  1 263 ? 38.018  37.193  36.268  1.00 35.02  ? 249 GLU A CD  1 
ATOM   1991 O  OE1 . GLU A  1 263 ? 37.302  37.068  35.254  1.00 41.95  ? 249 GLU A OE1 1 
ATOM   1992 O  OE2 . GLU A  1 263 ? 37.890  38.131  37.079  1.00 44.07  ? 249 GLU A OE2 1 
ATOM   1993 N  N   . ARG A  1 264 ? 37.642  31.951  34.978  1.00 23.77  ? 250 ARG A N   1 
ATOM   1994 C  CA  . ARG A  1 264 ? 37.408  30.888  34.015  1.00 25.72  ? 250 ARG A CA  1 
ATOM   1995 C  C   . ARG A  1 264 ? 35.904  30.701  33.821  1.00 26.52  ? 250 ARG A C   1 
ATOM   1996 O  O   . ARG A  1 264 ? 35.438  30.492  32.702  1.00 26.60  ? 250 ARG A O   1 
ATOM   1997 C  CB  . ARG A  1 264 ? 38.077  29.593  34.490  1.00 25.81  ? 250 ARG A CB  1 
ATOM   1998 C  CG  . ARG A  1 264 ? 37.754  28.373  33.640  1.00 27.79  ? 250 ARG A CG  1 
ATOM   1999 C  CD  . ARG A  1 264 ? 38.267  27.101  34.295  1.00 29.34  ? 250 ARG A CD  1 
ATOM   2000 N  NE  . ARG A  1 264 ? 37.824  25.895  33.589  1.00 31.36  ? 250 ARG A NE  1 
ATOM   2001 C  CZ  . ARG A  1 264 ? 38.021  24.658  34.025  1.00 31.71  ? 250 ARG A CZ  1 
ATOM   2002 N  NH1 . ARG A  1 264 ? 38.661  24.450  35.162  1.00 32.75  ? 250 ARG A NH1 1 
ATOM   2003 N  NH2 . ARG A  1 264 ? 37.577  23.634  33.319  1.00 34.20  ? 250 ARG A NH2 1 
ATOM   2004 N  N   . ILE A  1 265 ? 35.150  30.776  34.925  1.00 27.95  ? 251 ILE A N   1 
ATOM   2005 C  CA  . ILE A  1 265 ? 33.701  30.638  34.884  1.00 26.20  ? 251 ILE A CA  1 
ATOM   2006 C  C   . ILE A  1 265 ? 33.110  31.800  34.087  1.00 27.51  ? 251 ILE A C   1 
ATOM   2007 O  O   . ILE A  1 265 ? 32.186  31.606  33.298  1.00 27.30  ? 251 ILE A O   1 
ATOM   2008 C  CB  . ILE A  1 265 ? 33.115  30.541  36.306  1.00 24.74  ? 251 ILE A CB  1 
ATOM   2009 C  CG1 . ILE A  1 265 ? 33.476  29.205  36.968  1.00 24.84  ? 251 ILE A CG1 1 
ATOM   2010 C  CG2 . ILE A  1 265 ? 31.603  30.770  36.299  1.00 22.62  ? 251 ILE A CG2 1 
ATOM   2011 C  CD1 . ILE A  1 265 ? 33.220  29.156  38.463  1.00 25.97  ? 251 ILE A CD1 1 
ATOM   2012 N  N   . ARG A  1 266 ? 33.664  33.003  34.285  1.00 29.61  ? 252 ARG A N   1 
ATOM   2013 C  CA  . ARG A  1 266 ? 33.186  34.192  33.595  1.00 32.11  ? 252 ARG A CA  1 
ATOM   2014 C  C   . ARG A  1 266 ? 33.350  33.997  32.089  1.00 33.42  ? 252 ARG A C   1 
ATOM   2015 O  O   . ARG A  1 266 ? 32.475  34.378  31.315  1.00 33.70  ? 252 ARG A O   1 
ATOM   2016 C  CB  . ARG A  1 266 ? 33.922  35.451  34.070  1.00 33.54  ? 252 ARG A CB  1 
ATOM   2017 C  CG  . ARG A  1 266 ? 33.217  36.759  33.734  1.00 34.51  ? 252 ARG A CG  1 
ATOM   2018 C  CD  . ARG A  1 266 ? 34.076  37.985  34.009  1.00 32.62  ? 252 ARG A CD  1 
ATOM   2019 N  NE  . ARG A  1 266 ? 34.657  37.988  35.356  1.00 32.50  ? 252 ARG A NE  1 
ATOM   2020 C  CZ  . ARG A  1 266 ? 33.973  38.150  36.483  1.00 36.41  ? 252 ARG A CZ  1 
ATOM   2021 N  NH1 . ARG A  1 266 ? 32.663  38.332  36.450  1.00 35.57  ? 252 ARG A NH1 1 
ATOM   2022 N  NH2 . ARG A  1 266 ? 34.606  38.137  37.643  1.00 36.39  ? 252 ARG A NH2 1 
ATOM   2023 N  N   . ARG A  1 267 ? 34.476  33.394  31.683  1.00 28.52  ? 253 ARG A N   1 
ATOM   2024 C  CA  . ARG A  1 267 ? 34.768  33.175  30.274  1.00 28.23  ? 253 ARG A CA  1 
ATOM   2025 C  C   . ARG A  1 267 ? 33.806  32.140  29.693  1.00 27.09  ? 253 ARG A C   1 
ATOM   2026 O  O   . ARG A  1 267 ? 33.257  32.340  28.613  1.00 25.26  ? 253 ARG A O   1 
ATOM   2027 C  CB  . ARG A  1 267 ? 36.215  32.718  30.039  1.00 29.97  ? 253 ARG A CB  1 
ATOM   2028 C  CG  . ARG A  1 267 ? 36.440  32.141  28.646  1.00 33.19  ? 253 ARG A CG  1 
ATOM   2029 C  CD  . ARG A  1 267 ? 37.877  31.725  28.368  1.00 34.79  ? 253 ARG A CD  1 
ATOM   2030 N  NE  . ARG A  1 267 ? 38.387  30.712  29.298  1.00 33.84  ? 253 ARG A NE  1 
ATOM   2031 C  CZ  . ARG A  1 267 ? 38.059  29.424  29.295  1.00 36.58  ? 253 ARG A CZ  1 
ATOM   2032 N  NH1 . ARG A  1 267 ? 37.189  28.955  28.418  1.00 36.02  ? 253 ARG A NH1 1 
ATOM   2033 N  NH2 . ARG A  1 267 ? 38.613  28.604  30.171  1.00 36.58  ? 253 ARG A NH2 1 
ATOM   2034 N  N   . ILE A  1 268 ? 33.626  31.021  30.406  1.00 27.63  ? 254 ILE A N   1 
ATOM   2035 C  CA  . ILE A  1 268 ? 32.758  29.948  29.944  1.00 30.40  ? 254 ILE A CA  1 
ATOM   2036 C  C   . ILE A  1 268 ? 31.335  30.484  29.790  1.00 30.74  ? 254 ILE A C   1 
ATOM   2037 O  O   . ILE A  1 268 ? 30.654  30.171  28.816  1.00 31.41  ? 254 ILE A O   1 
ATOM   2038 C  CB  . ILE A  1 268 ? 32.810  28.732  30.891  1.00 32.71  ? 254 ILE A CB  1 
ATOM   2039 C  CG1 . ILE A  1 268 ? 34.197  28.075  30.898  1.00 33.61  ? 254 ILE A CG1 1 
ATOM   2040 C  CG2 . ILE A  1 268 ? 31.713  27.725  30.539  1.00 33.37  ? 254 ILE A CG2 1 
ATOM   2041 C  CD1 . ILE A  1 268 ? 34.383  27.028  31.983  1.00 34.34  ? 254 ILE A CD1 1 
ATOM   2042 N  N   . ALA A  1 269 ? 30.895  31.288  30.764  1.00 29.95  ? 255 ALA A N   1 
ATOM   2043 C  CA  . ALA A  1 269 ? 29.562  31.869  30.743  1.00 31.72  ? 255 ALA A CA  1 
ATOM   2044 C  C   . ALA A  1 269 ? 29.388  32.705  29.476  1.00 36.00  ? 255 ALA A C   1 
ATOM   2045 O  O   . ALA A  1 269 ? 28.396  32.559  28.763  1.00 30.16  ? 255 ALA A O   1 
ATOM   2046 C  CB  . ALA A  1 269 ? 29.338  32.697  31.990  1.00 30.74  ? 255 ALA A CB  1 
ATOM   2047 N  N   . GLN A  1 270 ? 30.374  33.571  29.210  1.00 38.82  ? 256 GLN A N   1 
ATOM   2048 C  CA  . GLN A  1 270 ? 30.368  34.441  28.043  1.00 37.95  ? 256 GLN A CA  1 
ATOM   2049 C  C   . GLN A  1 270 ? 30.352  33.601  26.766  1.00 40.78  ? 256 GLN A C   1 
ATOM   2050 O  O   . GLN A  1 270 ? 29.498  33.799  25.905  1.00 43.29  ? 256 GLN A O   1 
ATOM   2051 C  CB  . GLN A  1 270 ? 31.569  35.389  28.088  1.00 46.24  ? 256 GLN A CB  1 
ATOM   2052 C  CG  . GLN A  1 270 ? 31.421  36.525  29.097  1.00 51.97  ? 256 GLN A CG  1 
ATOM   2053 C  CD  . GLN A  1 270 ? 32.708  37.278  29.356  1.00 52.54  ? 256 GLN A CD  1 
ATOM   2054 O  OE1 . GLN A  1 270 ? 33.779  36.926  28.847  1.00 57.37  ? 256 GLN A OE1 1 
ATOM   2055 N  NE2 . GLN A  1 270 ? 32.617  38.325  30.164  1.00 50.54  ? 256 GLN A NE2 1 
ATOM   2056 N  N   . GLU A  1 271 ? 31.291  32.654  26.659  1.00 37.41  ? 257 GLU A N   1 
ATOM   2057 C  CA  . GLU A  1 271 ? 31.513  31.920  25.421  1.00 37.90  ? 257 GLU A CA  1 
ATOM   2058 C  C   . GLU A  1 271 ? 30.348  30.971  25.124  1.00 41.05  ? 257 GLU A C   1 
ATOM   2059 O  O   . GLU A  1 271 ? 30.055  30.714  23.958  1.00 39.61  ? 257 GLU A O   1 
ATOM   2060 C  CB  . GLU A  1 271 ? 32.849  31.170  25.466  1.00 38.23  ? 257 GLU A CB  1 
ATOM   2061 C  CG  . GLU A  1 271 ? 34.074  32.078  25.375  1.00 41.39  ? 257 GLU A CG  1 
ATOM   2062 C  CD  . GLU A  1 271 ? 35.407  31.352  25.277  1.00 40.77  ? 257 GLU A CD  1 
ATOM   2063 O  OE1 . GLU A  1 271 ? 35.425  30.115  25.460  1.00 41.42  ? 257 GLU A OE1 1 
ATOM   2064 O  OE2 . GLU A  1 271 ? 36.426  32.024  25.006  1.00 38.25  ? 257 GLU A OE2 1 
ATOM   2065 N  N   . THR A  1 272 ? 29.687  30.444  26.167  1.00 38.91  ? 258 THR A N   1 
ATOM   2066 C  CA  . THR A  1 272 ? 28.601  29.486  25.981  1.00 36.57  ? 258 THR A CA  1 
ATOM   2067 C  C   . THR A  1 272 ? 27.245  30.156  26.210  1.00 34.98  ? 258 THR A C   1 
ATOM   2068 O  O   . THR A  1 272 ? 26.212  29.491  26.155  1.00 32.32  ? 258 THR A O   1 
ATOM   2069 C  CB  . THR A  1 272 ? 28.754  28.277  26.910  1.00 35.13  ? 258 THR A CB  1 
ATOM   2070 O  OG1 . THR A  1 272 ? 28.758  28.771  28.247  1.00 32.72  ? 258 THR A OG1 1 
ATOM   2071 C  CG2 . THR A  1 272 ? 30.015  27.472  26.647  1.00 37.51  ? 258 THR A CG2 1 
ATOM   2072 N  N   . LYS A  1 273 ? 27.251  31.468  26.472  1.00 34.21  ? 259 LYS A N   1 
ATOM   2073 C  CA  . LYS A  1 273 ? 26.036  32.198  26.807  1.00 41.36  ? 259 LYS A CA  1 
ATOM   2074 C  C   . LYS A  1 273 ? 25.258  31.439  27.883  1.00 36.61  ? 259 LYS A C   1 
ATOM   2075 O  O   . LYS A  1 273 ? 24.086  31.118  27.694  1.00 37.25  ? 259 LYS A O   1 
ATOM   2076 C  CB  . LYS A  1 273 ? 25.122  32.397  25.591  1.00 50.39  ? 259 LYS A CB  1 
ATOM   2077 C  CG  . LYS A  1 273 ? 25.797  32.826  24.294  1.00 56.70  ? 259 LYS A CG  1 
ATOM   2078 C  CD  . LYS A  1 273 ? 24.789  33.113  23.186  1.00 69.49  ? 259 LYS A CD  1 
ATOM   2079 C  CE  . LYS A  1 273 ? 25.141  32.478  21.872  1.00 76.82  ? 259 LYS A CE  1 
ATOM   2080 N  NZ  . LYS A  1 273 ? 26.321  33.074  21.239  1.00 84.06  ? 259 LYS A NZ  1 
ATOM   2081 N  N   . SER A  1 274 ? 25.920  31.161  29.013  1.00 33.17  ? 260 SER A N   1 
ATOM   2082 C  CA  . SER A  1 274 ? 25.298  30.445  30.117  1.00 31.44  ? 260 SER A CA  1 
ATOM   2083 C  C   . SER A  1 274 ? 25.000  31.405  31.268  1.00 32.62  ? 260 SER A C   1 
ATOM   2084 O  O   . SER A  1 274 ? 25.690  32.407  31.442  1.00 29.48  ? 260 SER A O   1 
ATOM   2085 C  CB  . SER A  1 274 ? 26.166  29.299  30.589  1.00 30.35  ? 260 SER A CB  1 
ATOM   2086 O  OG  . SER A  1 274 ? 26.297  28.296  29.592  1.00 33.50  ? 260 SER A OG  1 
ATOM   2087 N  N   . GLN A  1 275 ? 23.950  31.084  32.034  1.00 30.20  ? 261 GLN A N   1 
ATOM   2088 C  CA  . GLN A  1 275 ? 23.714  31.691  33.334  1.00 32.15  ? 261 GLN A CA  1 
ATOM   2089 C  C   . GLN A  1 275 ? 24.696  31.097  34.341  1.00 28.19  ? 261 GLN A C   1 
ATOM   2090 O  O   . GLN A  1 275 ? 25.056  29.927  34.237  1.00 30.89  ? 261 GLN A O   1 
ATOM   2091 C  CB  . GLN A  1 275 ? 22.311  31.381  33.859  1.00 32.31  ? 261 GLN A CB  1 
ATOM   2092 C  CG  . GLN A  1 275 ? 21.171  32.083  33.131  1.00 38.37  ? 261 GLN A CG  1 
ATOM   2093 C  CD  . GLN A  1 275 ? 19.822  31.579  33.598  1.00 41.00  ? 261 GLN A CD  1 
ATOM   2094 O  OE1 . GLN A  1 275 ? 19.460  31.708  34.773  1.00 35.68  ? 261 GLN A OE1 1 
ATOM   2095 N  NE2 . GLN A  1 275 ? 19.080  30.964  32.688  1.00 40.46  ? 261 GLN A NE2 1 
ATOM   2096 N  N   . VAL A  1 276 ? 25.101  31.906  35.327  1.00 29.54  ? 262 VAL A N   1 
ATOM   2097 C  CA  . VAL A  1 276 ? 25.926  31.430  36.426  1.00 29.41  ? 262 VAL A CA  1 
ATOM   2098 C  C   . VAL A  1 276 ? 25.063  31.355  37.686  1.00 29.57  ? 262 VAL A C   1 
ATOM   2099 O  O   . VAL A  1 276 ? 24.575  32.377  38.165  1.00 29.09  ? 262 VAL A O   1 
ATOM   2100 C  CB  . VAL A  1 276 ? 27.163  32.328  36.641  1.00 31.91  ? 262 VAL A CB  1 
ATOM   2101 C  CG1 . VAL A  1 276 ? 27.996  31.873  37.834  1.00 32.79  ? 262 VAL A CG1 1 
ATOM   2102 C  CG2 . VAL A  1 276 ? 28.033  32.416  35.391  1.00 30.35  ? 262 VAL A CG2 1 
ATOM   2103 N  N   . TRP A  1 277 ? 24.869  30.132  38.202  1.00 27.80  ? 263 TRP A N   1 
ATOM   2104 C  CA  . TRP A  1 277 ? 24.139  29.911  39.443  1.00 28.38  ? 263 TRP A CA  1 
ATOM   2105 C  C   . TRP A  1 277 ? 25.129  29.794  40.603  1.00 28.87  ? 263 TRP A C   1 
ATOM   2106 O  O   . TRP A  1 277 ? 25.888  28.829  40.685  1.00 26.65  ? 263 TRP A O   1 
ATOM   2107 C  CB  . TRP A  1 277 ? 23.247  28.662  39.336  1.00 30.48  ? 263 TRP A CB  1 
ATOM   2108 C  CG  . TRP A  1 277 ? 22.060  28.820  38.418  1.00 30.45  ? 263 TRP A CG  1 
ATOM   2109 C  CD1 . TRP A  1 277 ? 21.858  29.817  37.509  1.00 31.38  ? 263 TRP A CD1 1 
ATOM   2110 C  CD2 . TRP A  1 277 ? 20.910  27.945  38.314  1.00 28.71  ? 263 TRP A CD2 1 
ATOM   2111 N  NE1 . TRP A  1 277 ? 20.671  29.629  36.850  1.00 33.33  ? 263 TRP A NE1 1 
ATOM   2112 C  CE2 . TRP A  1 277 ? 20.067  28.491  37.320  1.00 31.92  ? 263 TRP A CE2 1 
ATOM   2113 C  CE3 . TRP A  1 277 ? 20.510  26.766  38.956  1.00 31.23  ? 263 TRP A CE3 1 
ATOM   2114 C  CZ2 . TRP A  1 277 ? 18.856  27.899  36.962  1.00 32.69  ? 263 TRP A CZ2 1 
ATOM   2115 C  CZ3 . TRP A  1 277 ? 19.313  26.182  38.600  1.00 32.18  ? 263 TRP A CZ3 1 
ATOM   2116 C  CH2 . TRP A  1 277 ? 18.498  26.742  37.618  1.00 30.94  ? 263 TRP A CH2 1 
ATOM   2117 N  N   . PHE A  1 278 ? 25.100  30.790  41.498  1.00 25.37  ? 264 PHE A N   1 
ATOM   2118 C  CA  . PHE A  1 278 ? 26.073  30.907  42.575  1.00 24.73  ? 264 PHE A CA  1 
ATOM   2119 C  C   . PHE A  1 278 ? 25.746  29.907  43.680  1.00 27.36  ? 264 PHE A C   1 
ATOM   2120 O  O   . PHE A  1 278 ? 24.671  29.311  43.692  1.00 30.94  ? 264 PHE A O   1 
ATOM   2121 C  CB  . PHE A  1 278 ? 26.101  32.347  43.096  1.00 25.73  ? 264 PHE A CB  1 
ATOM   2122 C  CG  . PHE A  1 278 ? 26.298  33.387  42.002  1.00 26.75  ? 264 PHE A CG  1 
ATOM   2123 C  CD1 . PHE A  1 278 ? 27.473  33.424  41.260  1.00 24.99  ? 264 PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A  1 278 ? 25.310  34.325  41.719  1.00 28.60  ? 264 PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A  1 278 ? 27.651  34.366  40.260  1.00 26.72  ? 264 PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A  1 278 ? 25.494  35.267  40.717  1.00 28.95  ? 264 PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A  1 278 ? 26.663  35.286  39.991  1.00 29.61  ? 264 PHE A CZ  1 
ATOM   2128 N  N   . GLY A  1 279 ? 26.696  29.736  44.608  1.00 27.65  ? 265 GLY A N   1 
ATOM   2129 C  CA  . GLY A  1 279 ? 26.565  28.772  45.687  1.00 27.22  ? 265 GLY A CA  1 
ATOM   2130 C  C   . GLY A  1 279 ? 25.435  29.137  46.648  1.00 32.27  ? 265 GLY A C   1 
ATOM   2131 O  O   . GLY A  1 279 ? 24.658  28.266  47.038  1.00 29.91  ? 265 GLY A O   1 
ATOM   2132 N  N   . HIS A  1 280 ? 25.347  30.423  47.025  1.00 33.00  ? 266 HIS A N   1 
ATOM   2133 C  CA  A HIS A  1 280 ? 24.398  30.880  48.023  0.30 32.74  ? 266 HIS A CA  1 
ATOM   2134 C  CA  B HIS A  1 280 ? 24.309  30.855  47.954  0.70 37.03  ? 266 HIS A CA  1 
ATOM   2135 C  C   . HIS A  1 280 ? 24.063  32.360  47.838  1.00 35.60  ? 266 HIS A C   1 
ATOM   2136 O  O   . HIS A  1 280 ? 24.357  33.147  48.735  1.00 40.88  ? 266 HIS A O   1 
ATOM   2137 C  CB  A HIS A  1 280 ? 25.005  30.795  49.428  0.30 30.64  ? 266 HIS A CB  1 
ATOM   2138 C  CB  B HIS A  1 280 ? 24.565  30.295  49.361  0.70 42.71  ? 266 HIS A CB  1 
ATOM   2139 C  CG  A HIS A  1 280 ? 25.666  29.497  49.752  0.30 28.36  ? 266 HIS A CG  1 
ATOM   2140 C  CG  B HIS A  1 280 ? 25.908  30.579  49.951  0.70 46.22  ? 266 HIS A CG  1 
ATOM   2141 N  ND1 A HIS A  1 280 ? 27.023  29.393  49.974  0.30 28.43  ? 266 HIS A ND1 1 
ATOM   2142 N  ND1 B HIS A  1 280 ? 26.740  29.562  50.368  0.70 54.30  ? 266 HIS A ND1 1 
ATOM   2143 C  CD2 A HIS A  1 280 ? 25.164  28.269  49.937  0.30 26.08  ? 266 HIS A CD2 1 
ATOM   2144 C  CD2 B HIS A  1 280 ? 26.563  31.720  50.200  0.70 48.64  ? 266 HIS A CD2 1 
ATOM   2145 C  CE1 A HIS A  1 280 ? 27.323  28.134  50.259  0.30 26.36  ? 266 HIS A CE1 1 
ATOM   2146 C  CE1 B HIS A  1 280 ? 27.858  30.083  50.855  0.70 53.15  ? 266 HIS A CE1 1 
ATOM   2147 N  NE2 A HIS A  1 280 ? 26.209  27.433  50.238  0.30 26.76  ? 266 HIS A NE2 1 
ATOM   2148 N  NE2 B HIS A  1 280 ? 27.771  31.392  50.764  0.70 51.80  ? 266 HIS A NE2 1 
ATOM   2149 N  N   . ASP A  1 281 ? 23.463  32.742  46.705  1.00 34.38  ? 267 ASP A N   1 
ATOM   2150 C  CA  . ASP A  1 281 ? 22.995  34.106  46.513  1.00 37.94  ? 267 ASP A CA  1 
ATOM   2151 C  C   . ASP A  1 281 ? 21.508  34.159  46.867  1.00 33.22  ? 267 ASP A C   1 
ATOM   2152 O  O   . ASP A  1 281 ? 20.692  33.516  46.213  1.00 30.42  ? 267 ASP A O   1 
ATOM   2153 C  CB  . ASP A  1 281 ? 23.272  34.611  45.104  1.00 38.68  ? 267 ASP A CB  1 
ATOM   2154 C  CG  . ASP A  1 281 ? 23.034  36.100  44.895  1.00 39.89  ? 267 ASP A CG  1 
ATOM   2155 O  OD1 . ASP A  1 281 ? 21.859  36.517  44.941  1.00 48.50  ? 267 ASP A OD1 1 
ATOM   2156 O  OD2 . ASP A  1 281 ? 24.027  36.831  44.707  1.00 41.50  ? 267 ASP A OD2 1 
ATOM   2157 N  N   . ALA A  1 282 ? 21.173  34.926  47.912  1.00 36.23  ? 268 ALA A N   1 
ATOM   2158 C  CA  . ALA A  1 282 ? 19.817  34.983  48.441  1.00 39.01  ? 268 ALA A CA  1 
ATOM   2159 C  C   . ALA A  1 282 ? 18.844  35.500  47.383  1.00 38.84  ? 268 ALA A C   1 
ATOM   2160 O  O   . ALA A  1 282 ? 17.772  34.928  47.193  1.00 43.95  ? 268 ALA A O   1 
ATOM   2161 C  CB  . ALA A  1 282 ? 19.784  35.847  49.684  1.00 37.36  ? 268 ALA A CB  1 
ATOM   2162 N  N   . GLU A  1 283 ? 19.226  36.591  46.707  1.00 38.61  ? 269 GLU A N   1 
ATOM   2163 C  CA  . GLU A  1 283 ? 18.387  37.207  45.691  1.00 43.32  ? 269 GLU A CA  1 
ATOM   2164 C  C   . GLU A  1 283 ? 18.132  36.215  44.559  1.00 44.74  ? 269 GLU A C   1 
ATOM   2165 O  O   . GLU A  1 283 ? 16.998  36.051  44.115  1.00 43.10  ? 269 GLU A O   1 
ATOM   2166 C  CB  . GLU A  1 283 ? 19.032  38.471  45.120  1.00 49.91  ? 269 GLU A CB  1 
ATOM   2167 C  CG  . GLU A  1 283 ? 19.184  39.600  46.135  1.00 58.38  ? 269 GLU A CG  1 
ATOM   2168 C  CD  . GLU A  1 283 ? 19.440  40.960  45.508  1.00 76.58  ? 269 GLU A CD  1 
ATOM   2169 O  OE1 . GLU A  1 283 ? 18.661  41.350  44.612  1.00 79.76  ? 269 GLU A OE1 1 
ATOM   2170 O  OE2 . GLU A  1 283 ? 20.409  41.633  45.919  1.00 89.03  ? 269 GLU A OE2 1 
ATOM   2171 N  N   . GLN A  1 284 ? 19.207  35.568  44.094  1.00 41.26  ? 270 GLN A N   1 
ATOM   2172 C  CA  . GLN A  1 284 ? 19.130  34.668  42.956  1.00 36.98  ? 270 GLN A CA  1 
ATOM   2173 C  C   . GLN A  1 284 ? 18.263  33.462  43.313  1.00 34.50  ? 270 GLN A C   1 
ATOM   2174 O  O   . GLN A  1 284 ? 17.405  33.059  42.531  1.00 36.07  ? 270 GLN A O   1 
ATOM   2175 C  CB  . GLN A  1 284 ? 20.529  34.227  42.523  1.00 32.99  ? 270 GLN A CB  1 
ATOM   2176 C  CG  . GLN A  1 284 ? 20.551  33.430  41.224  1.00 31.81  ? 270 GLN A CG  1 
ATOM   2177 C  CD  . GLN A  1 284 ? 21.940  32.963  40.847  1.00 33.29  ? 270 GLN A CD  1 
ATOM   2178 O  OE1 . GLN A  1 284 ? 22.637  32.316  41.636  1.00 33.13  ? 270 GLN A OE1 1 
ATOM   2179 N  NE2 . GLN A  1 284 ? 22.361  33.298  39.635  1.00 29.29  ? 270 GLN A NE2 1 
ATOM   2180 N  N   . PHE A  1 285 ? 18.507  32.886  44.496  1.00 32.56  ? 271 PHE A N   1 
ATOM   2181 C  CA  . PHE A  1 285 ? 17.773  31.712  44.944  1.00 37.17  ? 271 PHE A CA  1 
ATOM   2182 C  C   . PHE A  1 285 ? 16.282  32.038  44.998  1.00 40.18  ? 271 PHE A C   1 
ATOM   2183 O  O   . PHE A  1 285 ? 15.444  31.222  44.617  1.00 39.28  ? 271 PHE A O   1 
ATOM   2184 C  CB  . PHE A  1 285 ? 18.261  31.236  46.315  1.00 33.58  ? 271 PHE A CB  1 
ATOM   2185 C  CG  . PHE A  1 285 ? 17.524  30.004  46.822  1.00 35.47  ? 271 PHE A CG  1 
ATOM   2186 C  CD1 . PHE A  1 285 ? 17.851  28.738  46.350  1.00 37.46  ? 271 PHE A CD1 1 
ATOM   2187 C  CD2 . PHE A  1 285 ? 16.494  30.115  47.749  1.00 37.16  ? 271 PHE A CD2 1 
ATOM   2188 C  CE1 . PHE A  1 285 ? 17.174  27.616  46.802  1.00 38.89  ? 271 PHE A CE1 1 
ATOM   2189 C  CE2 . PHE A  1 285 ? 15.823  28.988  48.200  1.00 40.07  ? 271 PHE A CE2 1 
ATOM   2190 C  CZ  . PHE A  1 285 ? 16.163  27.742  47.725  1.00 40.27  ? 271 PHE A CZ  1 
ATOM   2191 N  N   . LYS A  1 286 ? 15.976  33.243  45.488  1.00 43.40  ? 272 LYS A N   1 
ATOM   2192 C  CA  . LYS A  1 286 ? 14.610  33.731  45.590  1.00 48.50  ? 272 LYS A CA  1 
ATOM   2193 C  C   . LYS A  1 286 ? 13.907  33.575  44.244  1.00 41.98  ? 272 LYS A C   1 
ATOM   2194 O  O   . LYS A  1 286 ? 12.777  33.096  44.183  1.00 42.50  ? 272 LYS A O   1 
ATOM   2195 C  CB  . LYS A  1 286 ? 14.631  35.197  46.042  1.00 57.20  ? 272 LYS A CB  1 
ATOM   2196 C  CG  . LYS A  1 286 ? 13.268  35.836  46.286  1.00 68.21  ? 272 LYS A CG  1 
ATOM   2197 C  CD  . LYS A  1 286 ? 12.472  35.197  47.418  1.00 77.67  ? 272 LYS A CD  1 
ATOM   2198 C  CE  . LYS A  1 286 ? 11.148  35.864  47.659  1.00 81.42  ? 272 LYS A CE  1 
ATOM   2199 N  NZ  . LYS A  1 286 ? 11.297  37.263  48.074  1.00 84.16  ? 272 LYS A NZ  1 
ATOM   2200 N  N   . LYS A  1 287 ? 14.602  33.965  43.169  1.00 38.83  ? 273 LYS A N   1 
ATOM   2201 C  CA  . LYS A  1 287 ? 14.014  34.048  41.842  1.00 40.56  ? 273 LYS A CA  1 
ATOM   2202 C  C   . LYS A  1 287 ? 13.831  32.653  41.242  1.00 42.28  ? 273 LYS A C   1 
ATOM   2203 O  O   . LYS A  1 287 ? 12.951  32.451  40.408  1.00 45.28  ? 273 LYS A O   1 
ATOM   2204 C  CB  . LYS A  1 287 ? 14.892  34.916  40.932  1.00 47.18  ? 273 LYS A CB  1 
ATOM   2205 C  CG  . LYS A  1 287 ? 15.206  36.312  41.461  1.00 52.12  ? 273 LYS A CG  1 
ATOM   2206 C  CD  . LYS A  1 287 ? 16.061  37.158  40.524  1.00 58.33  ? 273 LYS A CD  1 
ATOM   2207 C  CE  . LYS A  1 287 ? 15.576  37.122  39.105  1.00 66.61  ? 273 LYS A CE  1 
ATOM   2208 N  NZ  . LYS A  1 287 ? 16.078  38.253  38.317  1.00 69.06  ? 273 LYS A NZ  1 
ATOM   2209 N  N   . PHE A  1 288 ? 14.667  31.695  41.662  1.00 38.96  ? 274 PHE A N   1 
ATOM   2210 C  CA  . PHE A  1 288 ? 14.630  30.346  41.115  1.00 40.80  ? 274 PHE A CA  1 
ATOM   2211 C  C   . PHE A  1 288 ? 13.221  29.765  41.225  1.00 40.56  ? 274 PHE A C   1 
ATOM   2212 O  O   . PHE A  1 288 ? 12.486  30.073  42.161  1.00 40.65  ? 274 PHE A O   1 
ATOM   2213 C  CB  . PHE A  1 288 ? 15.599  29.406  41.842  1.00 43.32  ? 274 PHE A CB  1 
ATOM   2214 C  CG  . PHE A  1 288 ? 17.081  29.611  41.552  1.00 43.16  ? 274 PHE A CG  1 
ATOM   2215 C  CD1 . PHE A  1 288 ? 17.512  30.240  40.388  1.00 46.17  ? 274 PHE A CD1 1 
ATOM   2216 C  CD2 . PHE A  1 288 ? 18.045  29.152  42.444  1.00 44.80  ? 274 PHE A CD2 1 
ATOM   2217 C  CE1 . PHE A  1 288 ? 18.866  30.415  40.134  1.00 41.26  ? 274 PHE A CE1 1 
ATOM   2218 C  CE2 . PHE A  1 288 ? 19.396  29.329  42.185  1.00 41.50  ? 274 PHE A CE2 1 
ATOM   2219 C  CZ  . PHE A  1 288 ? 19.804  29.960  41.032  1.00 40.58  ? 274 PHE A CZ  1 
ATOM   2220 N  N   . ARG A  1 289 ? 12.867  28.905  40.262  1.00 40.10  ? 275 ARG A N   1 
ATOM   2221 C  CA  . ARG A  1 289 ? 11.674  28.078  40.350  1.00 44.45  ? 275 ARG A CA  1 
ATOM   2222 C  C   . ARG A  1 289 ? 12.030  26.802  41.111  1.00 41.64  ? 275 ARG A C   1 
ATOM   2223 O  O   . ARG A  1 289 ? 12.801  25.980  40.622  1.00 38.39  ? 275 ARG A O   1 
ATOM   2224 C  CB  . ARG A  1 289 ? 11.145  27.765  38.945  1.00 49.13  ? 275 ARG A CB  1 
ATOM   2225 C  CG  . ARG A  1 289 ? 9.829   27.000  38.898  1.00 53.94  ? 275 ARG A CG  1 
ATOM   2226 C  CD  . ARG A  1 289 ? 9.343   26.862  37.463  1.00 56.96  ? 275 ARG A CD  1 
ATOM   2227 N  NE  . ARG A  1 289 ? 9.780   28.015  36.668  1.00 61.73  ? 275 ARG A NE  1 
ATOM   2228 C  CZ  . ARG A  1 289 ? 10.490  27.941  35.547  1.00 64.65  ? 275 ARG A CZ  1 
ATOM   2229 N  NH1 . ARG A  1 289 ? 10.708  26.769  34.975  1.00 63.20  ? 275 ARG A NH1 1 
ATOM   2230 N  NH2 . ARG A  1 289 ? 10.957  29.043  34.985  1.00 59.78  ? 275 ARG A NH2 1 
ATOM   2231 N  N   . LYS A  1 290 ? 11.468  26.650  42.315  1.00 40.69  ? 276 LYS A N   1 
ATOM   2232 C  CA  . LYS A  1 290 ? 11.847  25.562  43.203  1.00 40.14  ? 276 LYS A CA  1 
ATOM   2233 C  C   . LYS A  1 290 ? 11.086  24.294  42.820  1.00 35.54  ? 276 LYS A C   1 
ATOM   2234 O  O   . LYS A  1 290 ? 10.123  24.349  42.057  1.00 39.67  ? 276 LYS A O   1 
ATOM   2235 C  CB  . LYS A  1 290 ? 11.569  25.934  44.665  1.00 40.94  ? 276 LYS A CB  1 
ATOM   2236 C  CG  . LYS A  1 290 ? 11.815  27.393  45.037  1.00 42.71  ? 276 LYS A CG  1 
ATOM   2237 C  CD  . LYS A  1 290 ? 13.274  27.835  45.005  1.00 37.50  ? 276 LYS A CD  1 
ATOM   2238 C  CE  . LYS A  1 290 ? 13.480  29.196  45.605  1.00 36.60  ? 276 LYS A CE  1 
ATOM   2239 N  NZ  . LYS A  1 290 ? 12.871  30.265  44.807  1.00 36.32  ? 276 LYS A NZ  1 
ATOM   2240 N  N   . SER A  1 291 ? 11.528  23.160  43.378  1.00 33.26  ? 277 SER A N   1 
ATOM   2241 C  CA  . SER A  1 291 ? 10.983  21.849  43.060  1.00 35.90  ? 277 SER A CA  1 
ATOM   2242 C  C   . SER A  1 291 ? 9.484   21.784  43.359  1.00 38.83  ? 277 SER A C   1 
ATOM   2243 O  O   . SER A  1 291 ? 8.764   21.007  42.733  1.00 34.75  ? 277 SER A O   1 
ATOM   2244 C  CB  . SER A  1 291 ? 11.730  20.769  43.805  1.00 35.18  ? 277 SER A CB  1 
ATOM   2245 O  OG  . SER A  1 291 ? 11.727  21.022  45.203  1.00 36.92  ? 277 SER A OG  1 
ATOM   2246 N  N   . THR A  1 292 ? 9.025   22.591  44.325  1.00 37.49  ? 278 THR A N   1 
ATOM   2247 C  CA  . THR A  1 292 ? 7.631   22.568  44.750  1.00 42.62  ? 278 THR A CA  1 
ATOM   2248 C  C   . THR A  1 292 ? 6.743   23.245  43.706  1.00 45.80  ? 278 THR A C   1 
ATOM   2249 O  O   . THR A  1 292 ? 5.542   22.987  43.662  1.00 51.06  ? 278 THR A O   1 
ATOM   2250 C  CB  . THR A  1 292 ? 7.456   23.230  46.120  1.00 37.36  ? 278 THR A CB  1 
ATOM   2251 O  OG1 . THR A  1 292 ? 8.208   24.440  46.087  1.00 44.74  ? 278 THR A OG1 1 
ATOM   2252 C  CG2 . THR A  1 292 ? 7.921   22.350  47.267  1.00 38.05  ? 278 THR A CG2 1 
ATOM   2253 N  N   . GLU A  1 293 ? 7.329   24.115  42.872  1.00 49.52  ? 279 GLU A N   1 
ATOM   2254 C  CA  . GLU A  1 293 ? 6.543   24.892  41.924  1.00 50.72  ? 279 GLU A CA  1 
ATOM   2255 C  C   . GLU A  1 293 ? 6.708   24.345  40.505  1.00 52.06  ? 279 GLU A C   1 
ATOM   2256 O  O   . GLU A  1 293 ? 5.786   24.448  39.700  1.00 53.55  ? 279 GLU A O   1 
ATOM   2257 C  CB  . GLU A  1 293 ? 6.889   26.382  41.961  1.00 53.22  ? 279 GLU A CB  1 
ATOM   2258 C  CG  . GLU A  1 293 ? 6.827   26.999  43.356  1.00 66.16  ? 279 GLU A CG  1 
ATOM   2259 C  CD  . GLU A  1 293 ? 8.178   27.131  44.036  1.00 71.87  ? 279 GLU A CD  1 
ATOM   2260 O  OE1 . GLU A  1 293 ? 9.052   27.831  43.479  1.00 60.79  ? 279 GLU A OE1 1 
ATOM   2261 O  OE2 . GLU A  1 293 ? 8.352   26.542  45.124  1.00 77.11  ? 279 GLU A OE2 1 
ATOM   2262 N  N   . GLY A  1 294 ? 7.879   23.776  40.189  1.00 49.57  ? 280 GLY A N   1 
ATOM   2263 C  CA  . GLY A  1 294 ? 8.097   23.215  38.863  1.00 47.49  ? 280 GLY A CA  1 
ATOM   2264 C  C   . GLY A  1 294 ? 9.559   22.856  38.592  1.00 47.71  ? 280 GLY A C   1 
ATOM   2265 O  O   . GLY A  1 294 ? 10.283  22.436  39.493  1.00 41.24  ? 280 GLY A O   1 
ATOM   2266 N  N   . TYR A  1 295 ? 9.970   23.014  37.326  1.00 44.73  ? 281 TYR A N   1 
ATOM   2267 C  CA  . TYR A  1 295 ? 11.288  22.597  36.870  1.00 42.57  ? 281 TYR A CA  1 
ATOM   2268 C  C   . TYR A  1 295 ? 11.757  23.507  35.734  1.00 42.68  ? 281 TYR A C   1 
ATOM   2269 O  O   . TYR A  1 295 ? 11.011  24.367  35.271  1.00 41.56  ? 281 TYR A O   1 
ATOM   2270 C  CB  . TYR A  1 295 ? 11.229  21.128  36.436  1.00 43.36  ? 281 TYR A CB  1 
ATOM   2271 C  CG  . TYR A  1 295 ? 10.078  20.799  35.493  1.00 50.48  ? 281 TYR A CG  1 
ATOM   2272 C  CD1 . TYR A  1 295 ? 10.183  21.020  34.124  1.00 48.83  ? 281 TYR A CD1 1 
ATOM   2273 C  CD2 . TYR A  1 295 ? 8.881   20.273  35.972  1.00 54.92  ? 281 TYR A CD2 1 
ATOM   2274 C  CE1 . TYR A  1 295 ? 9.137   20.729  33.264  1.00 53.61  ? 281 TYR A CE1 1 
ATOM   2275 C  CE2 . TYR A  1 295 ? 7.828   19.976  35.121  1.00 54.59  ? 281 TYR A CE2 1 
ATOM   2276 C  CZ  . TYR A  1 295 ? 7.956   20.205  33.763  1.00 55.26  ? 281 TYR A CZ  1 
ATOM   2277 O  OH  . TYR A  1 295 ? 6.922   19.912  32.921  1.00 52.50  ? 281 TYR A OH  1 
ATOM   2278 N  N   . TYR A  1 296 ? 13.012  23.309  35.310  1.00 42.51  ? 282 TYR A N   1 
ATOM   2279 C  CA  . TYR A  1 296 ? 13.577  23.993  34.158  1.00 40.92  ? 282 TYR A CA  1 
ATOM   2280 C  C   . TYR A  1 296 ? 13.718  22.978  33.026  1.00 41.32  ? 282 TYR A C   1 
ATOM   2281 O  O   . TYR A  1 296 ? 13.948  21.798  33.280  1.00 42.03  ? 282 TYR A O   1 
ATOM   2282 C  CB  . TYR A  1 296 ? 14.929  24.634  34.501  1.00 40.20  ? 282 TYR A CB  1 
ATOM   2283 C  CG  . TYR A  1 296 ? 14.869  25.834  35.439  1.00 35.40  ? 282 TYR A CG  1 
ATOM   2284 C  CD1 . TYR A  1 296 ? 14.677  25.672  36.807  1.00 34.08  ? 282 TYR A CD1 1 
ATOM   2285 C  CD2 . TYR A  1 296 ? 15.031  27.130  34.959  1.00 37.68  ? 282 TYR A CD2 1 
ATOM   2286 C  CE1 . TYR A  1 296 ? 14.629  26.761  37.662  1.00 34.87  ? 282 TYR A CE1 1 
ATOM   2287 C  CE2 . TYR A  1 296 ? 14.986  28.227  35.804  1.00 37.61  ? 282 TYR A CE2 1 
ATOM   2288 C  CZ  . TYR A  1 296 ? 14.785  28.041  37.160  1.00 38.46  ? 282 TYR A CZ  1 
ATOM   2289 O  OH  . TYR A  1 296 ? 14.742  29.128  37.986  1.00 39.76  ? 282 TYR A OH  1 
ATOM   2290 N  N   . GLU A  1 297 ? 13.563  23.445  31.782  1.00 42.53  ? 283 GLU A N   1 
ATOM   2291 C  CA  . GLU A  1 297 ? 13.735  22.591  30.619  1.00 44.32  ? 283 GLU A CA  1 
ATOM   2292 C  C   . GLU A  1 297 ? 14.323  23.422  29.466  1.00 36.20  ? 283 GLU A C   1 
ATOM   2293 O  O   . GLU A  1 297 ? 14.679  22.794  28.445  1.00 41.66  ? 283 GLU A O   1 
ATOM   2294 C  CB  . GLU A  1 297 ? 12.410  21.936  30.226  1.00 45.77  ? 283 GLU A CB  1 
ATOM   2295 C  CG  . GLU A  1 297 ? 11.365  22.919  29.703  1.00 51.53  ? 283 GLU A CG  1 
ATOM   2296 C  CD  . GLU A  1 297 ? 9.961   22.343  29.604  1.00 53.49  ? 283 GLU A CD  1 
ATOM   2297 O  OE1 . GLU A  1 297 ? 9.009   23.007  30.067  1.00 45.06  ? 283 GLU A OE1 1 
ATOM   2298 O  OE2 . GLU A  1 297 ? 9.823   21.218  29.077  1.00 47.46  ? 283 GLU A OE2 1 
ATOM   2299 N  N   . ALA B  1 22  ? 35.916  14.002  1.167   1.00 39.77  ? 8   ALA B N   1 
ATOM   2300 C  CA  . ALA B  1 22  ? 36.832  12.870  0.883   1.00 43.47  ? 8   ALA B CA  1 
ATOM   2301 C  C   . ALA B  1 22  ? 36.122  11.545  1.162   1.00 41.94  ? 8   ALA B C   1 
ATOM   2302 O  O   . ALA B  1 22  ? 35.405  11.420  2.153   1.00 42.49  ? 8   ALA B O   1 
ATOM   2303 C  CB  . ALA B  1 22  ? 38.095  13.009  1.709   1.00 45.07  ? 8   ALA B CB  1 
ATOM   2304 N  N   A ARG B  1 23  ? 36.344  10.564  0.278   0.50 44.72  ? 9   ARG B N   1 
ATOM   2305 N  N   B ARG B  1 23  ? 36.324  10.567  0.273   0.50 42.57  ? 9   ARG B N   1 
ATOM   2306 C  CA  A ARG B  1 23  ? 35.743  9.243   0.393   0.50 43.49  ? 9   ARG B CA  1 
ATOM   2307 C  CA  B ARG B  1 23  ? 35.741  9.245   0.439   0.50 39.93  ? 9   ARG B CA  1 
ATOM   2308 C  C   A ARG B  1 23  ? 36.852  8.190   0.420   0.50 38.15  ? 9   ARG B C   1 
ATOM   2309 C  C   B ARG B  1 23  ? 36.858  8.203   0.420   0.50 36.46  ? 9   ARG B C   1 
ATOM   2310 O  O   A ARG B  1 23  ? 37.044  7.464   -0.554  0.50 32.95  ? 9   ARG B O   1 
ATOM   2311 O  O   B ARG B  1 23  ? 37.058  7.509   -0.574  0.50 31.92  ? 9   ARG B O   1 
ATOM   2312 C  CB  A ARG B  1 23  ? 34.785  8.995   -0.783  0.50 46.83  ? 9   ARG B CB  1 
ATOM   2313 C  CB  B ARG B  1 23  ? 34.672  8.970   -0.626  0.50 40.09  ? 9   ARG B CB  1 
ATOM   2314 C  CG  A ARG B  1 23  ? 33.687  10.035  -0.974  0.50 50.92  ? 9   ARG B CG  1 
ATOM   2315 C  CG  B ARG B  1 23  ? 33.579  10.030  -0.688  0.50 40.81  ? 9   ARG B CG  1 
ATOM   2316 C  CD  A ARG B  1 23  ? 32.292  9.606   -0.526  0.50 54.67  ? 9   ARG B CD  1 
ATOM   2317 C  CD  B ARG B  1 23  ? 32.197  9.469   -0.998  0.50 41.40  ? 9   ARG B CD  1 
ATOM   2318 N  NE  A ARG B  1 23  ? 31.633  8.641   -1.416  0.50 58.51  ? 9   ARG B NE  1 
ATOM   2319 N  NE  B ARG B  1 23  ? 31.510  8.970   0.200   0.50 43.18  ? 9   ARG B NE  1 
ATOM   2320 C  CZ  A ARG B  1 23  ? 30.738  8.959   -2.347  0.50 57.59  ? 9   ARG B CZ  1 
ATOM   2321 C  CZ  B ARG B  1 23  ? 30.528  9.614   0.822   0.50 38.49  ? 9   ARG B CZ  1 
ATOM   2322 N  NH1 A ARG B  1 23  ? 30.603  10.216  -2.735  0.50 57.89  ? 9   ARG B NH1 1 
ATOM   2323 N  NH1 B ARG B  1 23  ? 30.190  10.833  0.436   0.50 42.43  ? 9   ARG B NH1 1 
ATOM   2324 N  NH2 A ARG B  1 23  ? 30.020  8.013   -2.927  0.50 54.72  ? 9   ARG B NH2 1 
ATOM   2325 N  NH2 B ARG B  1 23  ? 29.905  9.052   1.842   0.50 36.40  ? 9   ARG B NH2 1 
ATOM   2326 N  N   . PRO B  1 24  ? 37.620  8.068   1.529   1.00 33.35  ? 10  PRO B N   1 
ATOM   2327 C  CA  . PRO B  1 24  ? 38.721  7.101   1.599   1.00 34.23  ? 10  PRO B CA  1 
ATOM   2328 C  C   . PRO B  1 24  ? 38.292  5.644   1.772   1.00 30.02  ? 10  PRO B C   1 
ATOM   2329 O  O   . PRO B  1 24  ? 37.154  5.364   2.145   1.00 30.83  ? 10  PRO B O   1 
ATOM   2330 C  CB  . PRO B  1 24  ? 39.499  7.601   2.831   1.00 34.51  ? 10  PRO B CB  1 
ATOM   2331 C  CG  . PRO B  1 24  ? 38.429  8.189   3.723   1.00 37.98  ? 10  PRO B CG  1 
ATOM   2332 C  CD  . PRO B  1 24  ? 37.455  8.853   2.763   1.00 38.19  ? 10  PRO B CD  1 
ATOM   2333 N  N   . LYS B  1 25  ? 39.228  4.727   1.498   1.00 27.18  ? 11  LYS B N   1 
ATOM   2334 C  CA  . LYS B  1 25  ? 39.062  3.312   1.796   1.00 26.49  ? 11  LYS B CA  1 
ATOM   2335 C  C   . LYS B  1 25  ? 40.161  2.876   2.765   1.00 24.39  ? 11  LYS B C   1 
ATOM   2336 O  O   . LYS B  1 25  ? 41.347  3.068   2.494   1.00 23.41  ? 11  LYS B O   1 
ATOM   2337 C  CB  . LYS B  1 25  ? 39.122  2.462   0.521   1.00 25.42  ? 11  LYS B CB  1 
ATOM   2338 C  CG  . LYS B  1 25  ? 37.941  2.593   -0.435  1.00 27.14  ? 11  LYS B CG  1 
ATOM   2339 C  CD  . LYS B  1 25  ? 38.114  1.797   -1.725  1.00 30.14  ? 11  LYS B CD  1 
ATOM   2340 C  CE  . LYS B  1 25  ? 36.933  1.879   -2.649  1.00 29.80  ? 11  LYS B CE  1 
ATOM   2341 N  NZ  . LYS B  1 25  ? 36.536  3.263   -2.930  1.00 29.57  ? 11  LYS B NZ  1 
ATOM   2342 N  N   . LEU B  1 26  ? 39.758  2.280   3.893   1.00 21.88  ? 12  LEU B N   1 
ATOM   2343 C  CA  . LEU B  1 26  ? 40.703  1.870   4.922   1.00 25.99  ? 12  LEU B CA  1 
ATOM   2344 C  C   . LEU B  1 26  ? 40.845  0.347   4.913   1.00 25.02  ? 12  LEU B C   1 
ATOM   2345 O  O   . LEU B  1 26  ? 39.848  -0.369  4.971   1.00 28.42  ? 12  LEU B O   1 
ATOM   2346 C  CB  . LEU B  1 26  ? 40.234  2.405   6.277   1.00 23.49  ? 12  LEU B CB  1 
ATOM   2347 C  CG  . LEU B  1 26  ? 41.154  2.122   7.470   1.00 24.09  ? 12  LEU B CG  1 
ATOM   2348 C  CD1 . LEU B  1 26  ? 40.961  3.159   8.568   1.00 24.50  ? 12  LEU B CD1 1 
ATOM   2349 C  CD2 . LEU B  1 26  ? 40.923  0.725   8.022   1.00 21.97  ? 12  LEU B CD2 1 
ATOM   2350 N  N   . TYR B  1 27  ? 42.100  -0.130  4.849   1.00 24.42  ? 13  TYR B N   1 
ATOM   2351 C  CA  . TYR B  1 27  ? 42.398  -1.551  4.722   1.00 25.75  ? 13  TYR B CA  1 
ATOM   2352 C  C   . TYR B  1 27  ? 43.174  -2.063  5.936   1.00 26.72  ? 13  TYR B C   1 
ATOM   2353 O  O   . TYR B  1 27  ? 44.124  -1.425  6.386   1.00 26.94  ? 13  TYR B O   1 
ATOM   2354 C  CB  . TYR B  1 27  ? 43.263  -1.857  3.493   1.00 24.68  ? 13  TYR B CB  1 
ATOM   2355 C  CG  . TYR B  1 27  ? 42.667  -1.470  2.146   1.00 26.51  ? 13  TYR B CG  1 
ATOM   2356 C  CD1 . TYR B  1 27  ? 42.735  -0.161  1.683   1.00 24.06  ? 13  TYR B CD1 1 
ATOM   2357 C  CD2 . TYR B  1 27  ? 42.064  -2.418  1.328   1.00 25.54  ? 13  TYR B CD2 1 
ATOM   2358 C  CE1 . TYR B  1 27  ? 42.202  0.197   0.456   1.00 26.79  ? 13  TYR B CE1 1 
ATOM   2359 C  CE2 . TYR B  1 27  ? 41.529  -2.073  0.099   1.00 25.50  ? 13  TYR B CE2 1 
ATOM   2360 C  CZ  . TYR B  1 27  ? 41.600  -0.761  -0.338  1.00 26.17  ? 13  TYR B CZ  1 
ATOM   2361 O  OH  . TYR B  1 27  ? 41.080  -0.402  -1.547  1.00 26.40  ? 13  TYR B OH  1 
ATOM   2362 N  N   . VAL B  1 28  ? 42.781  -3.250  6.423   1.00 27.46  ? 14  VAL B N   1 
ATOM   2363 C  CA  . VAL B  1 28  ? 43.513  -3.967  7.458   1.00 25.35  ? 14  VAL B CA  1 
ATOM   2364 C  C   . VAL B  1 28  ? 44.320  -5.087  6.800   1.00 25.26  ? 14  VAL B C   1 
ATOM   2365 O  O   . VAL B  1 28  ? 43.750  -5.981  6.177   1.00 24.92  ? 14  VAL B O   1 
ATOM   2366 C  CB  . VAL B  1 28  ? 42.559  -4.532  8.531   1.00 25.88  ? 14  VAL B CB  1 
ATOM   2367 C  CG1 . VAL B  1 28  ? 43.291  -5.415  9.536   1.00 27.53  ? 14  VAL B CG1 1 
ATOM   2368 C  CG2 . VAL B  1 28  ? 41.785  -3.431  9.248   1.00 27.07  ? 14  VAL B CG2 1 
ATOM   2369 N  N   . MET B  1 29  ? 45.649  -5.040  6.956   1.00 22.60  ? 15  MET B N   1 
ATOM   2370 C  CA  . MET B  1 29  ? 46.539  -5.988  6.298   1.00 23.55  ? 15  MET B CA  1 
ATOM   2371 C  C   . MET B  1 29  ? 47.127  -6.953  7.329   1.00 25.11  ? 15  MET B C   1 
ATOM   2372 O  O   . MET B  1 29  ? 47.732  -6.527  8.312   1.00 21.88  ? 15  MET B O   1 
ATOM   2373 C  CB  . MET B  1 29  ? 47.657  -5.248  5.549   1.00 22.99  ? 15  MET B CB  1 
ATOM   2374 C  CG  . MET B  1 29  ? 47.178  -4.496  4.312   1.00 22.88  ? 15  MET B CG  1 
ATOM   2375 S  SD  . MET B  1 29  ? 48.442  -3.476  3.523   1.00 27.10  ? 15  MET B SD  1 
ATOM   2376 C  CE  . MET B  1 29  ? 48.866  -2.353  4.862   1.00 27.44  ? 15  MET B CE  1 
ATOM   2377 N  N   . ASP B  1 30  ? 46.942  -8.258  7.083   1.00 25.82  ? 16  ASP B N   1 
ATOM   2378 C  CA  . ASP B  1 30  ? 47.413  -9.314  7.969   1.00 27.22  ? 16  ASP B CA  1 
ATOM   2379 C  C   . ASP B  1 30  ? 48.895  -9.583  7.707   1.00 26.61  ? 16  ASP B C   1 
ATOM   2380 O  O   . ASP B  1 30  ? 49.253  -10.080 6.642   1.00 26.31  ? 16  ASP B O   1 
ATOM   2381 C  CB  . ASP B  1 30  ? 46.574  -10.575 7.797   1.00 29.65  ? 16  ASP B CB  1 
ATOM   2382 C  CG  . ASP B  1 30  ? 46.989  -11.764 8.653   1.00 31.41  ? 16  ASP B CG  1 
ATOM   2383 O  OD1 . ASP B  1 30  ? 48.116  -11.734 9.190   1.00 31.36  ? 16  ASP B OD1 1 
ATOM   2384 O  OD2 . ASP B  1 30  ? 46.170  -12.700 8.791   1.00 35.70  ? 16  ASP B OD2 1 
ATOM   2385 N  N   . ASN B  1 31  ? 49.753  -9.280  8.695   1.00 24.41  ? 17  ASN B N   1 
ATOM   2386 C  CA  . ASN B  1 31  ? 51.195  -9.403  8.526   1.00 24.59  ? 17  ASN B CA  1 
ATOM   2387 C  C   . ASN B  1 31  ? 51.754  -10.515 9.415   1.00 26.15  ? 17  ASN B C   1 
ATOM   2388 O  O   . ASN B  1 31  ? 52.913  -10.454 9.824   1.00 30.05  ? 17  ASN B O   1 
ATOM   2389 C  CB  . ASN B  1 31  ? 51.923  -8.089  8.803   1.00 24.90  ? 17  ASN B CB  1 
ATOM   2390 C  CG  . ASN B  1 31  ? 51.468  -6.963  7.904   1.00 27.07  ? 17  ASN B CG  1 
ATOM   2391 O  OD1 . ASN B  1 31  ? 50.996  -5.929  8.390   1.00 28.06  ? 17  ASN B OD1 1 
ATOM   2392 N  ND2 . ASN B  1 31  ? 51.611  -7.136  6.597   1.00 26.58  ? 17  ASN B ND2 1 
ATOM   2393 N  N   . GLY B  1 32  ? 50.931  -11.530 9.709   1.00 29.85  ? 18  GLY B N   1 
ATOM   2394 C  CA  . GLY B  1 32  ? 51.402  -12.725 10.394  1.00 31.18  ? 18  GLY B CA  1 
ATOM   2395 C  C   . GLY B  1 32  ? 51.115  -12.690 11.894  1.00 31.21  ? 18  GLY B C   1 
ATOM   2396 O  O   . GLY B  1 32  ? 50.278  -11.918 12.358  1.00 29.14  ? 18  GLY B O   1 
ATOM   2397 N  N   . ARG B  1 33  ? 51.829  -13.542 12.641  1.00 28.95  ? 19  ARG B N   1 
ATOM   2398 C  CA  . ARG B  1 33  ? 51.568  -13.747 14.057  1.00 32.96  ? 19  ARG B CA  1 
ATOM   2399 C  C   . ARG B  1 33  ? 52.893  -13.793 14.818  1.00 31.71  ? 19  ARG B C   1 
ATOM   2400 O  O   . ARG B  1 33  ? 53.897  -14.276 14.300  1.00 31.86  ? 19  ARG B O   1 
ATOM   2401 C  CB  . ARG B  1 33  ? 50.791  -15.055 14.261  1.00 35.08  ? 19  ARG B CB  1 
ATOM   2402 C  CG  . ARG B  1 33  ? 49.563  -15.223 13.375  1.00 33.22  ? 19  ARG B CG  1 
ATOM   2403 C  CD  . ARG B  1 33  ? 48.316  -14.548 13.927  1.00 38.09  ? 19  ARG B CD  1 
ATOM   2404 N  NE  . ARG B  1 33  ? 47.186  -14.669 12.999  1.00 39.50  ? 19  ARG B NE  1 
ATOM   2405 C  CZ  . ARG B  1 33  ? 47.057  -13.974 11.874  1.00 39.98  ? 19  ARG B CZ  1 
ATOM   2406 N  NH1 . ARG B  1 33  ? 47.907  -13.001 11.595  1.00 38.00  ? 19  ARG B NH1 1 
ATOM   2407 N  NH2 . ARG B  1 33  ? 46.059  -14.235 11.048  1.00 42.40  ? 19  ARG B NH2 1 
ATOM   2408 N  N   . MET B  1 34  ? 52.885  -13.273 16.049  1.00 33.33  ? 20  MET B N   1 
ATOM   2409 C  CA  . MET B  1 34  ? 54.007  -13.443 16.958  1.00 31.12  ? 20  MET B CA  1 
ATOM   2410 C  C   . MET B  1 34  ? 53.522  -14.182 18.203  1.00 28.25  ? 20  MET B C   1 
ATOM   2411 O  O   . MET B  1 34  ? 52.321  -14.261 18.461  1.00 29.53  ? 20  MET B O   1 
ATOM   2412 C  CB  . MET B  1 34  ? 54.626  -12.098 17.364  1.00 36.60  ? 20  MET B CB  1 
ATOM   2413 C  CG  . MET B  1 34  ? 55.468  -11.440 16.279  1.00 44.52  ? 20  MET B CG  1 
ATOM   2414 S  SD  . MET B  1 34  ? 56.534  -10.113 16.888  1.00 53.43  ? 20  MET B SD  1 
ATOM   2415 C  CE  . MET B  1 34  ? 56.402  -10.358 18.666  1.00 35.71  ? 20  MET B CE  1 
ATOM   2416 N  N   . ARG B  1 35  ? 54.474  -14.728 18.965  1.00 25.82  ? 21  ARG B N   1 
ATOM   2417 C  CA  . ARG B  1 35  ? 54.185  -15.310 20.264  1.00 30.24  ? 21  ARG B CA  1 
ATOM   2418 C  C   . ARG B  1 35  ? 55.136  -14.698 21.287  1.00 28.55  ? 21  ARG B C   1 
ATOM   2419 O  O   . ARG B  1 35  ? 56.251  -14.312 20.941  1.00 28.36  ? 21  ARG B O   1 
ATOM   2420 C  CB  . ARG B  1 35  ? 54.347  -16.835 20.240  1.00 35.03  ? 21  ARG B CB  1 
ATOM   2421 C  CG  . ARG B  1 35  ? 53.390  -17.576 19.315  1.00 40.08  ? 21  ARG B CG  1 
ATOM   2422 C  CD  . ARG B  1 35  ? 53.732  -19.058 19.250  1.00 41.10  ? 21  ARG B CD  1 
ATOM   2423 N  NE  . ARG B  1 35  ? 55.003  -19.291 18.553  1.00 49.68  ? 21  ARG B NE  1 
ATOM   2424 C  CZ  . ARG B  1 35  ? 55.752  -20.382 18.674  1.00 50.27  ? 21  ARG B CZ  1 
ATOM   2425 N  NH1 . ARG B  1 35  ? 55.424  -21.320 19.545  1.00 50.31  ? 21  ARG B NH1 1 
ATOM   2426 N  NH2 . ARG B  1 35  ? 56.844  -20.519 17.941  1.00 51.61  ? 21  ARG B NH2 1 
ATOM   2427 N  N   . MET B  1 36  ? 54.682  -14.611 22.542  1.00 28.51  ? 22  MET B N   1 
ATOM   2428 C  CA  . MET B  1 36  ? 55.547  -14.192 23.632  1.00 27.42  ? 22  MET B CA  1 
ATOM   2429 C  C   . MET B  1 36  ? 54.902  -14.542 24.970  1.00 25.17  ? 22  MET B C   1 
ATOM   2430 O  O   . MET B  1 36  ? 53.720  -14.878 25.032  1.00 25.31  ? 22  MET B O   1 
ATOM   2431 C  CB  . MET B  1 36  ? 55.833  -12.685 23.580  1.00 27.67  ? 22  MET B CB  1 
ATOM   2432 C  CG  . MET B  1 36  ? 54.617  -11.801 23.809  1.00 27.96  ? 22  MET B CG  1 
ATOM   2433 S  SD  . MET B  1 36  ? 54.989  -10.055 23.530  1.00 31.08  ? 22  MET B SD  1 
ATOM   2434 C  CE  . MET B  1 36  ? 53.444  -9.286  24.041  1.00 34.00  ? 22  MET B CE  1 
ATOM   2435 N  N   . ASP B  1 37  ? 55.718  -14.459 26.027  1.00 26.47  ? 23  ASP B N   1 
ATOM   2436 C  CA  . ASP B  1 37  ? 55.276  -14.642 27.400  1.00 25.97  ? 23  ASP B CA  1 
ATOM   2437 C  C   . ASP B  1 37  ? 54.051  -13.761 27.647  1.00 24.87  ? 23  ASP B C   1 
ATOM   2438 O  O   . ASP B  1 37  ? 54.060  -12.584 27.294  1.00 25.66  ? 23  ASP B O   1 
ATOM   2439 C  CB  . ASP B  1 37  ? 56.410  -14.298 28.356  1.00 26.92  ? 23  ASP B CB  1 
ATOM   2440 C  CG  . ASP B  1 37  ? 56.234  -14.773 29.790  1.00 30.32  ? 23  ASP B CG  1 
ATOM   2441 O  OD1 . ASP B  1 37  ? 55.080  -14.769 30.272  1.00 29.72  ? 23  ASP B OD1 1 
ATOM   2442 O  OD2 . ASP B  1 37  ? 57.258  -15.112 30.419  1.00 32.84  ? 23  ASP B OD2 1 
ATOM   2443 N  N   . LYS B  1 38  ? 53.003  -14.331 28.261  1.00 22.07  ? 24  LYS B N   1 
ATOM   2444 C  CA  . LYS B  1 38  ? 51.780  -13.590 28.536  1.00 27.52  ? 24  LYS B CA  1 
ATOM   2445 C  C   . LYS B  1 38  ? 52.073  -12.434 29.492  1.00 25.91  ? 24  LYS B C   1 
ATOM   2446 O  O   . LYS B  1 38  ? 51.367  -11.427 29.479  1.00 26.45  ? 24  LYS B O   1 
ATOM   2447 C  CB  . LYS B  1 38  ? 50.682  -14.490 29.122  1.00 28.93  ? 24  LYS B CB  1 
ATOM   2448 C  CG  . LYS B  1 38  ? 49.307  -13.834 29.262  1.00 34.62  ? 24  LYS B CG  1 
ATOM   2449 C  CD  . LYS B  1 38  ? 48.172  -14.806 29.570  1.00 41.57  ? 24  LYS B CD  1 
ATOM   2450 C  CE  . LYS B  1 38  ? 46.911  -14.139 30.042  1.00 41.43  ? 24  LYS B CE  1 
ATOM   2451 N  NZ  . LYS B  1 38  ? 46.420  -13.131 29.098  1.00 47.07  ? 24  LYS B NZ  1 
ATOM   2452 N  N   . ASN B  1 39  ? 53.110  -12.597 30.325  1.00 27.12  ? 25  ASN B N   1 
ATOM   2453 C  CA  . ASN B  1 39  ? 53.486  -11.587 31.304  1.00 28.59  ? 25  ASN B CA  1 
ATOM   2454 C  C   . ASN B  1 39  ? 53.896  -10.289 30.603  1.00 28.85  ? 25  ASN B C   1 
ATOM   2455 O  O   . ASN B  1 39  ? 53.665  -9.209  31.142  1.00 32.98  ? 25  ASN B O   1 
ATOM   2456 C  CB  . ASN B  1 39  ? 54.574  -12.081 32.254  1.00 28.41  ? 25  ASN B CB  1 
ATOM   2457 C  CG  . ASN B  1 39  ? 54.035  -13.010 33.318  1.00 29.06  ? 25  ASN B CG  1 
ATOM   2458 O  OD1 . ASN B  1 39  ? 54.601  -14.084 33.550  1.00 38.23  ? 25  ASN B OD1 1 
ATOM   2459 N  ND2 . ASN B  1 39  ? 52.963  -12.609 33.986  1.00 26.46  ? 25  ASN B ND2 1 
ATOM   2460 N  N   . TRP B  1 40  ? 54.512  -10.389 29.416  1.00 27.90  ? 26  TRP B N   1 
ATOM   2461 C  CA  . TRP B  1 40  ? 54.801  -9.205  28.617  1.00 30.81  ? 26  TRP B CA  1 
ATOM   2462 C  C   . TRP B  1 40  ? 53.494  -8.459  28.333  1.00 30.55  ? 26  TRP B C   1 
ATOM   2463 O  O   . TRP B  1 40  ? 53.462  -7.231  28.332  1.00 32.50  ? 26  TRP B O   1 
ATOM   2464 C  CB  . TRP B  1 40  ? 55.502  -9.554  27.292  1.00 30.57  ? 26  TRP B CB  1 
ATOM   2465 C  CG  . TRP B  1 40  ? 56.896  -10.135 27.364  1.00 29.04  ? 26  TRP B CG  1 
ATOM   2466 C  CD1 . TRP B  1 40  ? 57.288  -11.298 26.767  1.00 32.07  ? 26  TRP B CD1 1 
ATOM   2467 C  CD2 . TRP B  1 40  ? 58.092  -9.575  27.961  1.00 31.41  ? 26  TRP B CD2 1 
ATOM   2468 N  NE1 . TRP B  1 40  ? 58.621  -11.527 26.983  1.00 32.13  ? 26  TRP B NE1 1 
ATOM   2469 C  CE2 . TRP B  1 40  ? 59.144  -10.486 27.704  1.00 31.95  ? 26  TRP B CE2 1 
ATOM   2470 C  CE3 . TRP B  1 40  ? 58.381  -8.416  28.691  1.00 29.41  ? 26  TRP B CE3 1 
ATOM   2471 C  CZ2 . TRP B  1 40  ? 60.448  -10.271 28.150  1.00 32.67  ? 26  TRP B CZ2 1 
ATOM   2472 C  CZ3 . TRP B  1 40  ? 59.672  -8.203  29.126  1.00 29.88  ? 26  TRP B CZ3 1 
ATOM   2473 C  CH2 . TRP B  1 40  ? 60.690  -9.117  28.858  1.00 32.78  ? 26  TRP B CH2 1 
ATOM   2474 N  N   . MET B  1 41  ? 52.418  -9.222  28.089  1.00 32.20  ? 27  MET B N   1 
ATOM   2475 C  CA  . MET B  1 41  ? 51.153  -8.684  27.606  1.00 35.46  ? 27  MET B CA  1 
ATOM   2476 C  C   . MET B  1 41  ? 50.316  -8.158  28.771  1.00 31.45  ? 27  MET B C   1 
ATOM   2477 O  O   . MET B  1 41  ? 49.816  -7.037  28.723  1.00 27.96  ? 27  MET B O   1 
ATOM   2478 C  CB  . MET B  1 41  ? 50.342  -9.769  26.888  1.00 39.46  ? 27  MET B CB  1 
ATOM   2479 C  CG  . MET B  1 41  ? 49.075  -9.263  26.222  1.00 52.01  ? 27  MET B CG  1 
ATOM   2480 S  SD  . MET B  1 41  ? 49.299  -9.012  24.450  1.00 67.99  ? 27  MET B SD  1 
ATOM   2481 C  CE  . MET B  1 41  ? 49.563  -10.719 23.947  1.00 68.03  ? 27  MET B CE  1 
ATOM   2482 N  N   . ILE B  1 42  ? 50.132  -9.008  29.788  1.00 28.68  ? 28  ILE B N   1 
ATOM   2483 C  CA  . ILE B  1 42  ? 49.415  -8.653  31.003  1.00 28.64  ? 28  ILE B CA  1 
ATOM   2484 C  C   . ILE B  1 42  ? 50.339  -8.937  32.187  1.00 32.10  ? 28  ILE B C   1 
ATOM   2485 O  O   . ILE B  1 42  ? 50.607  -10.096 32.504  1.00 30.34  ? 28  ILE B O   1 
ATOM   2486 C  CB  . ILE B  1 42  ? 48.087  -9.433  31.120  1.00 30.31  ? 28  ILE B CB  1 
ATOM   2487 C  CG1 . ILE B  1 42  ? 47.207  -9.297  29.869  1.00 30.27  ? 28  ILE B CG1 1 
ATOM   2488 C  CG2 . ILE B  1 42  ? 47.325  -9.030  32.383  1.00 30.64  ? 28  ILE B CG2 1 
ATOM   2489 C  CD1 . ILE B  1 42  ? 46.503  -7.959  29.735  1.00 29.82  ? 28  ILE B CD1 1 
ATOM   2490 N  N   . ALA B  1 43  ? 50.830  -7.873  32.834  1.00 28.55  ? 29  ALA B N   1 
ATOM   2491 C  CA  . ALA B  1 43  ? 51.816  -8.014  33.895  1.00 28.80  ? 29  ALA B CA  1 
ATOM   2492 C  C   . ALA B  1 43  ? 51.259  -8.882  35.022  1.00 28.12  ? 29  ALA B C   1 
ATOM   2493 O  O   . ALA B  1 43  ? 50.095  -8.750  35.398  1.00 26.45  ? 29  ALA B O   1 
ATOM   2494 C  CB  . ALA B  1 43  ? 52.234  -6.649  34.401  1.00 30.44  ? 29  ALA B CB  1 
ATOM   2495 N  N   . MET B  1 44  ? 52.108  -9.779  35.540  1.00 31.59  ? 30  MET B N   1 
ATOM   2496 C  CA  . MET B  1 44  ? 51.800  -10.562 36.728  1.00 30.35  ? 30  MET B CA  1 
ATOM   2497 C  C   . MET B  1 44  ? 50.414  -11.192 36.603  1.00 28.61  ? 30  MET B C   1 
ATOM   2498 O  O   . MET B  1 44  ? 49.589  -11.055 37.503  1.00 34.23  ? 30  MET B O   1 
ATOM   2499 C  CB  . MET B  1 44  ? 51.840  -9.676  37.979  1.00 31.05  ? 30  MET B CB  1 
ATOM   2500 C  CG  . MET B  1 44  ? 53.206  -9.085  38.283  1.00 30.00  ? 30  MET B CG  1 
ATOM   2501 S  SD  . MET B  1 44  ? 54.473  -10.336 38.577  1.00 36.00  ? 30  MET B SD  1 
ATOM   2502 C  CE  . MET B  1 44  ? 53.572  -11.488 39.626  1.00 32.76  ? 30  MET B CE  1 
ATOM   2503 N  N   . HIS B  1 45  ? 50.171  -11.901 35.493  1.00 30.93  ? 31  HIS B N   1 
ATOM   2504 C  CA  . HIS B  1 45  ? 48.841  -12.404 35.181  1.00 31.18  ? 31  HIS B CA  1 
ATOM   2505 C  C   . HIS B  1 45  ? 48.503  -13.632 36.027  1.00 32.35  ? 31  HIS B C   1 
ATOM   2506 O  O   . HIS B  1 45  ? 47.329  -13.917 36.253  1.00 35.92  ? 31  HIS B O   1 
ATOM   2507 C  CB  . HIS B  1 45  ? 48.711  -12.718 33.685  1.00 30.38  ? 31  HIS B CB  1 
ATOM   2508 C  CG  . HIS B  1 45  ? 49.381  -13.986 33.267  1.00 29.49  ? 31  HIS B CG  1 
ATOM   2509 N  ND1 . HIS B  1 45  ? 50.738  -14.087 33.041  1.00 33.24  ? 31  HIS B ND1 1 
ATOM   2510 C  CD2 . HIS B  1 45  ? 48.877  -15.208 33.047  1.00 29.54  ? 31  HIS B CD2 1 
ATOM   2511 C  CE1 . HIS B  1 45  ? 51.033  -15.331 32.690  1.00 29.25  ? 31  HIS B CE1 1 
ATOM   2512 N  NE2 . HIS B  1 45  ? 49.917  -16.029 32.688  1.00 28.21  ? 31  HIS B NE2 1 
ATOM   2513 N  N   . ASN B  1 46  ? 49.530  -14.365 36.477  1.00 34.53  ? 32  ASN B N   1 
ATOM   2514 C  CA  . ASN B  1 46  ? 49.322  -15.602 37.219  1.00 34.34  ? 32  ASN B CA  1 
ATOM   2515 C  C   . ASN B  1 46  ? 50.357  -15.710 38.338  1.00 30.38  ? 32  ASN B C   1 
ATOM   2516 O  O   . ASN B  1 46  ? 51.265  -16.536 38.270  1.00 30.51  ? 32  ASN B O   1 
ATOM   2517 C  CB  . ASN B  1 46  ? 49.358  -16.819 36.297  1.00 35.37  ? 32  ASN B CB  1 
ATOM   2518 C  CG  . ASN B  1 46  ? 49.075  -18.116 37.023  1.00 35.74  ? 32  ASN B CG  1 
ATOM   2519 O  OD1 . ASN B  1 46  ? 48.191  -18.168 37.885  1.00 34.03  ? 32  ASN B OD1 1 
ATOM   2520 N  ND2 . ASN B  1 46  ? 49.816  -19.167 36.700  1.00 39.23  ? 32  ASN B ND2 1 
ATOM   2521 N  N   . PRO B  1 47  ? 50.244  -14.890 39.408  1.00 30.64  ? 33  PRO B N   1 
ATOM   2522 C  CA  . PRO B  1 47  ? 51.239  -14.881 40.484  1.00 32.82  ? 33  PRO B CA  1 
ATOM   2523 C  C   . PRO B  1 47  ? 51.347  -16.201 41.243  1.00 31.38  ? 33  PRO B C   1 
ATOM   2524 O  O   . PRO B  1 47  ? 50.337  -16.843 41.525  1.00 33.22  ? 33  PRO B O   1 
ATOM   2525 C  CB  . PRO B  1 47  ? 50.750  -13.749 41.413  1.00 33.66  ? 33  PRO B CB  1 
ATOM   2526 C  CG  . PRO B  1 47  ? 49.825  -12.914 40.552  1.00 33.37  ? 33  PRO B CG  1 
ATOM   2527 C  CD  . PRO B  1 47  ? 49.163  -13.915 39.623  1.00 31.92  ? 33  PRO B CD  1 
ATOM   2528 N  N   . ALA B  1 48  ? 52.584  -16.581 41.584  1.00 34.97  ? 34  ALA B N   1 
ATOM   2529 C  CA  . ALA B  1 48  ? 52.838  -17.737 42.428  1.00 33.86  ? 34  ALA B CA  1 
ATOM   2530 C  C   . ALA B  1 48  ? 52.116  -17.576 43.765  1.00 35.86  ? 34  ALA B C   1 
ATOM   2531 O  O   . ALA B  1 48  ? 51.951  -16.459 44.256  1.00 32.32  ? 34  ALA B O   1 
ATOM   2532 C  CB  . ALA B  1 48  ? 54.332  -17.915 42.619  1.00 35.88  ? 34  ALA B CB  1 
ATOM   2533 N  N   . THR B  1 49  ? 51.677  -18.708 44.332  1.00 35.79  ? 35  THR B N   1 
ATOM   2534 C  CA  . THR B  1 49  ? 51.056  -18.751 45.648  1.00 36.87  ? 35  THR B CA  1 
ATOM   2535 C  C   . THR B  1 49  ? 51.742  -19.830 46.485  1.00 35.85  ? 35  THR B C   1 
ATOM   2536 O  O   . THR B  1 49  ? 52.639  -20.523 46.007  1.00 33.77  ? 35  THR B O   1 
ATOM   2537 C  CB  . THR B  1 49  ? 49.554  -19.026 45.541  1.00 36.81  ? 35  THR B CB  1 
ATOM   2538 O  OG1 . THR B  1 49  ? 49.447  -20.268 44.850  1.00 43.05  ? 35  THR B OG1 1 
ATOM   2539 C  CG2 . THR B  1 49  ? 48.794  -17.937 44.805  1.00 39.52  ? 35  THR B CG2 1 
ATOM   2540 N  N   . ILE B  1 50  ? 51.297  -19.964 47.739  1.00 33.75  ? 36  ILE B N   1 
ATOM   2541 C  CA  . ILE B  1 50  ? 51.826  -20.968 48.647  1.00 42.54  ? 36  ILE B CA  1 
ATOM   2542 C  C   . ILE B  1 50  ? 51.532  -22.357 48.082  1.00 43.41  ? 36  ILE B C   1 
ATOM   2543 O  O   . ILE B  1 50  ? 52.292  -23.296 48.312  1.00 49.23  ? 36  ILE B O   1 
ATOM   2544 C  CB  . ILE B  1 50  ? 51.242  -20.779 50.062  1.00 46.49  ? 36  ILE B CB  1 
ATOM   2545 C  CG1 . ILE B  1 50  ? 51.940  -21.673 51.092  1.00 52.65  ? 36  ILE B CG1 1 
ATOM   2546 C  CG2 . ILE B  1 50  ? 49.727  -20.990 50.060  1.00 44.59  ? 36  ILE B CG2 1 
ATOM   2547 C  CD1 . ILE B  1 50  ? 51.618  -21.320 52.534  1.00 51.63  ? 36  ILE B CD1 1 
ATOM   2548 N  N   . HIS B  1 51  ? 50.434  -22.474 47.324  1.00 44.89  ? 37  HIS B N   1 
ATOM   2549 C  CA  . HIS B  1 51  ? 49.987  -23.762 46.813  1.00 46.22  ? 37  HIS B CA  1 
ATOM   2550 C  C   . HIS B  1 51  ? 50.301  -23.887 45.321  1.00 47.21  ? 37  HIS B C   1 
ATOM   2551 O  O   . HIS B  1 51  ? 50.091  -24.947 44.737  1.00 43.72  ? 37  HIS B O   1 
ATOM   2552 C  CB  . HIS B  1 51  ? 48.511  -24.001 47.158  1.00 54.84  ? 37  HIS B CB  1 
ATOM   2553 C  CG  . HIS B  1 51  ? 48.295  -24.369 48.592  1.00 67.36  ? 37  HIS B CG  1 
ATOM   2554 N  ND1 . HIS B  1 51  ? 47.654  -23.559 49.505  1.00 67.09  ? 37  HIS B ND1 1 
ATOM   2555 C  CD2 . HIS B  1 51  ? 48.637  -25.480 49.262  1.00 66.55  ? 37  HIS B CD2 1 
ATOM   2556 C  CE1 . HIS B  1 51  ? 47.622  -24.166 50.684  1.00 67.38  ? 37  HIS B CE1 1 
ATOM   2557 N  NE2 . HIS B  1 51  ? 48.215  -25.333 50.559  1.00 73.57  ? 37  HIS B NE2 1 
ATOM   2558 N  N   . ASN B  1 52  ? 50.807  -22.805 44.713  1.00 43.60  ? 38  ASN B N   1 
ATOM   2559 C  CA  . ASN B  1 52  ? 51.314  -22.851 43.349  1.00 39.57  ? 38  ASN B CA  1 
ATOM   2560 C  C   . ASN B  1 52  ? 52.596  -22.020 43.282  1.00 40.61  ? 38  ASN B C   1 
ATOM   2561 O  O   . ASN B  1 52  ? 52.647  -20.998 42.601  1.00 36.53  ? 38  ASN B O   1 
ATOM   2562 C  CB  . ASN B  1 52  ? 50.253  -22.430 42.333  1.00 40.28  ? 38  ASN B CB  1 
ATOM   2563 C  CG  . ASN B  1 52  ? 50.687  -22.671 40.905  1.00 39.76  ? 38  ASN B CG  1 
ATOM   2564 O  OD1 . ASN B  1 52  ? 51.375  -23.658 40.623  1.00 42.38  ? 38  ASN B OD1 1 
ATOM   2565 N  ND2 . ASN B  1 52  ? 50.319  -21.778 39.996  1.00 39.15  ? 38  ASN B ND2 1 
ATOM   2566 N  N   . PRO B  1 53  ? 53.674  -22.450 43.983  1.00 39.35  ? 39  PRO B N   1 
ATOM   2567 C  CA  . PRO B  1 53  ? 54.892  -21.644 44.127  1.00 41.39  ? 39  PRO B CA  1 
ATOM   2568 C  C   . PRO B  1 53  ? 55.760  -21.548 42.875  1.00 41.90  ? 39  PRO B C   1 
ATOM   2569 O  O   . PRO B  1 53  ? 56.607  -20.662 42.769  1.00 34.62  ? 39  PRO B O   1 
ATOM   2570 C  CB  . PRO B  1 53  ? 55.637  -22.372 45.262  1.00 39.64  ? 39  PRO B CB  1 
ATOM   2571 C  CG  . PRO B  1 53  ? 55.218  -23.818 45.108  1.00 39.20  ? 39  PRO B CG  1 
ATOM   2572 C  CD  . PRO B  1 53  ? 53.762  -23.744 44.681  1.00 38.92  ? 39  PRO B CD  1 
ATOM   2573 N  N   . ASN B  1 54  ? 55.562  -22.487 41.946  1.00 37.10  ? 40  ASN B N   1 
ATOM   2574 C  CA  . ASN B  1 54  ? 56.305  -22.498 40.697  1.00 38.24  ? 40  ASN B CA  1 
ATOM   2575 C  C   . ASN B  1 54  ? 55.331  -22.205 39.557  1.00 33.23  ? 40  ASN B C   1 
ATOM   2576 O  O   . ASN B  1 54  ? 55.361  -22.864 38.519  1.00 35.11  ? 40  ASN B O   1 
ATOM   2577 C  CB  . ASN B  1 54  ? 57.074  -23.804 40.514  1.00 42.78  ? 40  ASN B CB  1 
ATOM   2578 C  CG  . ASN B  1 54  ? 58.099  -24.028 41.602  1.00 44.68  ? 40  ASN B CG  1 
ATOM   2579 O  OD1 . ASN B  1 54  ? 58.009  -25.011 42.347  1.00 48.40  ? 40  ASN B OD1 1 
ATOM   2580 N  ND2 . ASN B  1 54  ? 59.073  -23.136 41.713  1.00 42.06  ? 40  ASN B ND2 1 
ATOM   2581 N  N   . ALA B  1 55  ? 54.477  -21.198 39.771  1.00 34.75  ? 41  ALA B N   1 
ATOM   2582 C  CA  . ALA B  1 55  ? 53.422  -20.845 38.834  1.00 36.25  ? 41  ALA B CA  1 
ATOM   2583 C  C   . ALA B  1 55  ? 54.000  -20.702 37.430  1.00 33.19  ? 41  ALA B C   1 
ATOM   2584 O  O   . ALA B  1 55  ? 55.093  -20.170 37.249  1.00 31.96  ? 41  ALA B O   1 
ATOM   2585 C  CB  . ALA B  1 55  ? 52.730  -19.573 39.281  1.00 39.27  ? 41  ALA B CB  1 
ATOM   2586 N  N   . GLN B  1 56  ? 53.234  -21.181 36.444  1.00 30.24  ? 42  GLN B N   1 
ATOM   2587 C  CA  . GLN B  1 56  ? 53.672  -21.215 35.060  1.00 33.34  ? 42  GLN B CA  1 
ATOM   2588 C  C   . GLN B  1 56  ? 53.047  -20.057 34.286  1.00 28.63  ? 42  GLN B C   1 
ATOM   2589 O  O   . GLN B  1 56  ? 51.907  -19.676 34.542  1.00 34.13  ? 42  GLN B O   1 
ATOM   2590 C  CB  . GLN B  1 56  ? 53.283  -22.554 34.430  1.00 36.01  ? 42  GLN B CB  1 
ATOM   2591 C  CG  . GLN B  1 56  ? 54.219  -23.706 34.781  1.00 41.54  ? 42  GLN B CG  1 
ATOM   2592 C  CD  . GLN B  1 56  ? 53.714  -25.040 34.275  1.00 42.75  ? 42  GLN B CD  1 
ATOM   2593 O  OE1 . GLN B  1 56  ? 53.132  -25.134 33.188  1.00 39.50  ? 42  GLN B OE1 1 
ATOM   2594 N  NE2 . GLN B  1 56  ? 53.905  -26.080 35.073  1.00 40.51  ? 42  GLN B NE2 1 
ATOM   2595 N  N   . THR B  1 57  ? 53.812  -19.504 33.336  1.00 30.76  ? 43  THR B N   1 
ATOM   2596 C  CA  . THR B  1 57  ? 53.269  -18.566 32.364  1.00 35.51  ? 43  THR B CA  1 
ATOM   2597 C  C   . THR B  1 57  ? 52.826  -19.363 31.139  1.00 37.49  ? 43  THR B C   1 
ATOM   2598 O  O   . THR B  1 57  ? 52.880  -20.592 31.141  1.00 36.82  ? 43  THR B O   1 
ATOM   2599 C  CB  . THR B  1 57  ? 54.295  -17.487 32.005  1.00 34.92  ? 43  THR B CB  1 
ATOM   2600 O  OG1 . THR B  1 57  ? 53.600  -16.488 31.262  1.00 31.83  ? 43  THR B OG1 1 
ATOM   2601 C  CG2 . THR B  1 57  ? 55.458  -18.016 31.184  1.00 37.18  ? 43  THR B CG2 1 
ATOM   2602 N  N   . GLU B  1 58  ? 52.378  -18.648 30.102  1.00 35.00  ? 44  GLU B N   1 
ATOM   2603 C  CA  . GLU B  1 58  ? 52.023  -19.263 28.833  1.00 43.61  ? 44  GLU B CA  1 
ATOM   2604 C  C   . GLU B  1 58  ? 52.568  -18.402 27.692  1.00 43.96  ? 44  GLU B C   1 
ATOM   2605 O  O   . GLU B  1 58  ? 52.708  -17.188 27.831  1.00 37.99  ? 44  GLU B O   1 
ATOM   2606 C  CB  . GLU B  1 58  ? 50.512  -19.501 28.755  1.00 45.44  ? 44  GLU B CB  1 
ATOM   2607 C  CG  . GLU B  1 58  ? 49.669  -18.271 29.080  1.00 54.94  ? 44  GLU B CG  1 
ATOM   2608 C  CD  . GLU B  1 58  ? 48.189  -18.552 29.277  1.00 59.04  ? 44  GLU B CD  1 
ATOM   2609 O  OE1 . GLU B  1 58  ? 47.564  -19.105 28.347  1.00 64.67  ? 44  GLU B OE1 1 
ATOM   2610 O  OE2 . GLU B  1 58  ? 47.660  -18.215 30.359  1.00 56.29  ? 44  GLU B OE2 1 
ATOM   2611 N  N   . PHE B  1 59  ? 52.899  -19.066 26.577  1.00 38.91  ? 45  PHE B N   1 
ATOM   2612 C  CA  . PHE B  1 59  ? 53.427  -18.424 25.382  1.00 38.51  ? 45  PHE B CA  1 
ATOM   2613 C  C   . PHE B  1 59  ? 52.260  -18.184 24.423  1.00 37.24  ? 45  PHE B C   1 
ATOM   2614 O  O   . PHE B  1 59  ? 51.811  -19.110 23.753  1.00 35.62  ? 45  PHE B O   1 
ATOM   2615 C  CB  . PHE B  1 59  ? 54.501  -19.347 24.790  1.00 35.60  ? 45  PHE B CB  1 
ATOM   2616 C  CG  . PHE B  1 59  ? 55.665  -18.699 24.048  1.00 36.61  ? 45  PHE B CG  1 
ATOM   2617 C  CD1 . PHE B  1 59  ? 56.429  -17.697 24.637  1.00 36.60  ? 45  PHE B CD1 1 
ATOM   2618 C  CD2 . PHE B  1 59  ? 56.017  -19.123 22.770  1.00 36.31  ? 45  PHE B CD2 1 
ATOM   2619 C  CE1 . PHE B  1 59  ? 57.502  -17.131 23.962  1.00 35.81  ? 45  PHE B CE1 1 
ATOM   2620 C  CE2 . PHE B  1 59  ? 57.089  -18.551 22.099  1.00 35.54  ? 45  PHE B CE2 1 
ATOM   2621 C  CZ  . PHE B  1 59  ? 57.827  -17.555 22.695  1.00 38.45  ? 45  PHE B CZ  1 
ATOM   2622 N  N   . VAL B  1 60  ? 51.764  -16.942 24.375  1.00 32.83  ? 46  VAL B N   1 
ATOM   2623 C  CA  . VAL B  1 60  ? 50.516  -16.637 23.688  1.00 33.09  ? 46  VAL B CA  1 
ATOM   2624 C  C   . VAL B  1 60  ? 50.811  -16.103 22.287  1.00 32.60  ? 46  VAL B C   1 
ATOM   2625 O  O   . VAL B  1 60  ? 51.764  -15.352 22.087  1.00 31.67  ? 46  VAL B O   1 
ATOM   2626 C  CB  . VAL B  1 60  ? 49.654  -15.642 24.491  1.00 36.22  ? 46  VAL B CB  1 
ATOM   2627 C  CG1 . VAL B  1 60  ? 48.969  -16.310 25.678  1.00 40.97  ? 46  VAL B CG1 1 
ATOM   2628 C  CG2 . VAL B  1 60  ? 50.458  -14.427 24.940  1.00 36.68  ? 46  VAL B CG2 1 
ATOM   2629 N  N   . GLU B  1 61  ? 49.969  -16.502 21.325  1.00 30.18  ? 47  GLU B N   1 
ATOM   2630 C  CA  . GLU B  1 61  ? 50.066  -16.018 19.957  1.00 31.23  ? 47  GLU B CA  1 
ATOM   2631 C  C   . GLU B  1 61  ? 49.166  -14.796 19.784  1.00 30.48  ? 47  GLU B C   1 
ATOM   2632 O  O   . GLU B  1 61  ? 48.062  -14.753 20.325  1.00 30.60  ? 47  GLU B O   1 
ATOM   2633 C  CB  . GLU B  1 61  ? 49.658  -17.102 18.958  1.00 33.09  ? 47  GLU B CB  1 
ATOM   2634 C  CG  . GLU B  1 61  ? 50.100  -16.792 17.530  1.00 34.77  ? 47  GLU B CG  1 
ATOM   2635 C  CD  . GLU B  1 61  ? 49.755  -17.861 16.508  1.00 39.16  ? 47  GLU B CD  1 
ATOM   2636 O  OE1 . GLU B  1 61  ? 48.549  -18.073 16.260  1.00 39.90  ? 47  GLU B OE1 1 
ATOM   2637 O  OE2 . GLU B  1 61  ? 50.694  -18.476 15.958  1.00 39.76  ? 47  GLU B OE2 1 
ATOM   2638 N  N   . PHE B  1 62  ? 49.640  -13.810 19.011  1.00 29.90  ? 48  PHE B N   1 
ATOM   2639 C  CA  . PHE B  1 62  ? 48.855  -12.614 18.746  1.00 30.21  ? 48  PHE B CA  1 
ATOM   2640 C  C   . PHE B  1 62  ? 49.078  -12.147 17.309  1.00 27.15  ? 48  PHE B C   1 
ATOM   2641 O  O   . PHE B  1 62  ? 50.136  -12.381 16.726  1.00 28.38  ? 48  PHE B O   1 
ATOM   2642 C  CB  . PHE B  1 62  ? 49.185  -11.506 19.753  1.00 29.63  ? 48  PHE B CB  1 
ATOM   2643 C  CG  . PHE B  1 62  ? 50.657  -11.133 19.864  1.00 28.73  ? 48  PHE B CG  1 
ATOM   2644 C  CD1 . PHE B  1 62  ? 51.521  -11.873 20.664  1.00 32.75  ? 48  PHE B CD1 1 
ATOM   2645 C  CD2 . PHE B  1 62  ? 51.169  -10.030 19.189  1.00 28.50  ? 48  PHE B CD2 1 
ATOM   2646 C  CE1 . PHE B  1 62  ? 52.860  -11.526 20.772  1.00 35.72  ? 48  PHE B CE1 1 
ATOM   2647 C  CE2 . PHE B  1 62  ? 52.510  -9.686  19.303  1.00 29.81  ? 48  PHE B CE2 1 
ATOM   2648 C  CZ  . PHE B  1 62  ? 53.350  -10.434 20.094  1.00 31.82  ? 48  PHE B CZ  1 
ATOM   2649 N  N   . PRO B  1 63  ? 48.075  -11.463 16.707  1.00 27.10  ? 49  PRO B N   1 
ATOM   2650 C  CA  . PRO B  1 63  ? 48.184  -10.942 15.341  1.00 28.43  ? 49  PRO B CA  1 
ATOM   2651 C  C   . PRO B  1 63  ? 49.047  -9.688  15.187  1.00 29.85  ? 49  PRO B C   1 
ATOM   2652 O  O   . PRO B  1 63  ? 49.001  -8.791  16.025  1.00 30.38  ? 49  PRO B O   1 
ATOM   2653 C  CB  . PRO B  1 63  ? 46.708  -10.643 15.007  1.00 31.28  ? 49  PRO B CB  1 
ATOM   2654 C  CG  . PRO B  1 63  ? 46.115  -10.228 16.332  1.00 33.84  ? 49  PRO B CG  1 
ATOM   2655 C  CD  . PRO B  1 63  ? 46.772  -11.169 17.327  1.00 32.03  ? 49  PRO B CD  1 
ATOM   2656 N  N   . ILE B  1 64  ? 49.828  -9.640  14.100  1.00 29.12  ? 50  ILE B N   1 
ATOM   2657 C  CA  . ILE B  1 64  ? 50.540  -8.438  13.689  1.00 26.69  ? 50  ILE B CA  1 
ATOM   2658 C  C   . ILE B  1 64  ? 49.818  -7.862  12.469  1.00 25.53  ? 50  ILE B C   1 
ATOM   2659 O  O   . ILE B  1 64  ? 49.636  -8.568  11.481  1.00 26.12  ? 50  ILE B O   1 
ATOM   2660 C  CB  . ILE B  1 64  ? 52.021  -8.752  13.381  1.00 26.86  ? 50  ILE B CB  1 
ATOM   2661 C  CG1 . ILE B  1 64  ? 52.732  -9.417  14.563  1.00 27.49  ? 50  ILE B CG1 1 
ATOM   2662 C  CG2 . ILE B  1 64  ? 52.769  -7.504  12.910  1.00 28.36  ? 50  ILE B CG2 1 
ATOM   2663 C  CD1 . ILE B  1 64  ? 52.716  -8.595  15.838  1.00 29.11  ? 50  ILE B CD1 1 
ATOM   2664 N  N   . TYR B  1 65  ? 49.394  -6.590  12.530  1.00 24.58  ? 51  TYR B N   1 
ATOM   2665 C  CA  . TYR B  1 65  ? 48.664  -6.005  11.412  1.00 23.90  ? 51  TYR B CA  1 
ATOM   2666 C  C   . TYR B  1 65  ? 49.075  -4.547  11.194  1.00 28.16  ? 51  TYR B C   1 
ATOM   2667 O  O   . TYR B  1 65  ? 49.622  -3.896  12.084  1.00 24.73  ? 51  TYR B O   1 
ATOM   2668 C  CB  . TYR B  1 65  ? 47.145  -6.146  11.583  1.00 24.44  ? 51  TYR B CB  1 
ATOM   2669 C  CG  . TYR B  1 65  ? 46.463  -5.222  12.584  1.00 26.39  ? 51  TYR B CG  1 
ATOM   2670 C  CD1 . TYR B  1 65  ? 46.436  -5.521  13.941  1.00 28.50  ? 51  TYR B CD1 1 
ATOM   2671 C  CD2 . TYR B  1 65  ? 45.804  -4.070  12.165  1.00 27.40  ? 51  TYR B CD2 1 
ATOM   2672 C  CE1 . TYR B  1 65  ? 45.801  -4.692  14.851  1.00 25.83  ? 51  TYR B CE1 1 
ATOM   2673 C  CE2 . TYR B  1 65  ? 45.164  -3.233  13.065  1.00 28.82  ? 51  TYR B CE2 1 
ATOM   2674 C  CZ  . TYR B  1 65  ? 45.163  -3.545  14.413  1.00 28.54  ? 51  TYR B CZ  1 
ATOM   2675 O  OH  . TYR B  1 65  ? 44.536  -2.727  15.309  1.00 30.16  ? 51  TYR B OH  1 
ATOM   2676 N  N   . THR B  1 66  ? 48.805  -4.067  9.972   1.00 25.75  ? 52  THR B N   1 
ATOM   2677 C  CA  . THR B  1 66  ? 49.032  -2.686  9.571   1.00 23.67  ? 52  THR B CA  1 
ATOM   2678 C  C   . THR B  1 66  ? 47.746  -2.159  8.934   1.00 25.26  ? 52  THR B C   1 
ATOM   2679 O  O   . THR B  1 66  ? 46.888  -2.942  8.531   1.00 24.42  ? 52  THR B O   1 
ATOM   2680 C  CB  . THR B  1 66  ? 50.216  -2.587  8.603   1.00 24.04  ? 52  THR B CB  1 
ATOM   2681 O  OG1 . THR B  1 66  ? 49.943  -3.490  7.536   1.00 24.97  ? 52  THR B OG1 1 
ATOM   2682 C  CG2 . THR B  1 66  ? 51.548  -2.936  9.243   1.00 24.86  ? 52  THR B CG2 1 
ATOM   2683 N  N   . VAL B  1 67  ? 47.618  -0.830  8.847   1.00 22.70  ? 53  VAL B N   1 
ATOM   2684 C  CA  . VAL B  1 67  ? 46.432  -0.212  8.277   1.00 23.53  ? 53  VAL B CA  1 
ATOM   2685 C  C   . VAL B  1 67  ? 46.855  0.740   7.162   1.00 24.45  ? 53  VAL B C   1 
ATOM   2686 O  O   . VAL B  1 67  ? 47.726  1.585   7.360   1.00 24.23  ? 53  VAL B O   1 
ATOM   2687 C  CB  . VAL B  1 67  ? 45.597  0.519   9.347   1.00 24.02  ? 53  VAL B CB  1 
ATOM   2688 C  CG1 . VAL B  1 67  ? 44.458  1.324   8.731   1.00 23.84  ? 53  VAL B CG1 1 
ATOM   2689 C  CG2 . VAL B  1 67  ? 45.061  -0.443  10.403  1.00 25.56  ? 53  VAL B CG2 1 
ATOM   2690 N  N   . LEU B  1 68  ? 46.231  0.580   5.990   1.00 23.53  ? 54  LEU B N   1 
ATOM   2691 C  CA  . LEU B  1 68  ? 46.386  1.522   4.894   1.00 26.36  ? 54  LEU B CA  1 
ATOM   2692 C  C   . LEU B  1 68  ? 45.113  2.354   4.773   1.00 25.12  ? 54  LEU B C   1 
ATOM   2693 O  O   . LEU B  1 68  ? 44.020  1.805   4.655   1.00 28.01  ? 54  LEU B O   1 
ATOM   2694 C  CB  . LEU B  1 68  ? 46.674  0.777   3.591   1.00 29.48  ? 54  LEU B CB  1 
ATOM   2695 C  CG  . LEU B  1 68  ? 46.753  1.649   2.333   1.00 29.61  ? 54  LEU B CG  1 
ATOM   2696 C  CD1 . LEU B  1 68  ? 48.026  2.483   2.327   1.00 30.17  ? 54  LEU B CD1 1 
ATOM   2697 C  CD2 . LEU B  1 68  ? 46.656  0.802   1.075   1.00 28.53  ? 54  LEU B CD2 1 
ATOM   2698 N  N   . ILE B  1 69  ? 45.263  3.683   4.810   1.00 25.32  ? 55  ILE B N   1 
ATOM   2699 C  CA  . ILE B  1 69  ? 44.168  4.573   4.463   1.00 26.61  ? 55  ILE B CA  1 
ATOM   2700 C  C   . ILE B  1 69  ? 44.434  5.128   3.068   1.00 27.67  ? 55  ILE B C   1 
ATOM   2701 O  O   . ILE B  1 69  ? 45.276  6.006   2.895   1.00 29.56  ? 55  ILE B O   1 
ATOM   2702 C  CB  . ILE B  1 69  ? 43.979  5.700   5.498   1.00 28.72  ? 55  ILE B CB  1 
ATOM   2703 C  CG1 . ILE B  1 69  ? 43.857  5.165   6.927   1.00 30.06  ? 55  ILE B CG1 1 
ATOM   2704 C  CG2 . ILE B  1 69  ? 42.782  6.576   5.124   1.00 27.65  ? 55  ILE B CG2 1 
ATOM   2705 C  CD1 . ILE B  1 69  ? 45.187  4.954   7.625   1.00 31.10  ? 55  ILE B CD1 1 
ATOM   2706 N  N   . ASP B  1 70  ? 43.719  4.587   2.075   1.00 29.72  ? 56  ASP B N   1 
ATOM   2707 C  CA  . ASP B  1 70  ? 43.753  5.129   0.728   1.00 30.22  ? 56  ASP B CA  1 
ATOM   2708 C  C   . ASP B  1 70  ? 42.902  6.395   0.695   1.00 29.04  ? 56  ASP B C   1 
ATOM   2709 O  O   . ASP B  1 70  ? 41.686  6.330   0.518   1.00 27.71  ? 56  ASP B O   1 
ATOM   2710 C  CB  . ASP B  1 70  ? 43.301  4.107   -0.304  1.00 32.51  ? 56  ASP B CB  1 
ATOM   2711 C  CG  . ASP B  1 70  ? 43.546  4.518   -1.749  1.00 32.51  ? 56  ASP B CG  1 
ATOM   2712 O  OD1 . ASP B  1 70  ? 44.091  5.622   -1.959  1.00 29.78  ? 56  ASP B OD1 1 
ATOM   2713 O  OD2 . ASP B  1 70  ? 43.195  3.730   -2.651  1.00 41.31  ? 56  ASP B OD2 1 
ATOM   2714 N  N   . HIS B  1 71  ? 43.566  7.541   0.875   1.00 29.24  ? 57  HIS B N   1 
ATOM   2715 C  CA  . HIS B  1 71  ? 42.901  8.830   0.981   1.00 26.60  ? 57  HIS B CA  1 
ATOM   2716 C  C   . HIS B  1 71  ? 43.154  9.620   -0.302  1.00 26.01  ? 57  HIS B C   1 
ATOM   2717 O  O   . HIS B  1 71  ? 44.241  9.543   -0.871  1.00 27.80  ? 57  HIS B O   1 
ATOM   2718 C  CB  . HIS B  1 71  ? 43.417  9.576   2.219   1.00 27.20  ? 57  HIS B CB  1 
ATOM   2719 C  CG  . HIS B  1 71  ? 42.551  10.698  2.691   1.00 28.05  ? 57  HIS B CG  1 
ATOM   2720 N  ND1 . HIS B  1 71  ? 42.474  11.921  2.061   1.00 29.34  ? 57  HIS B ND1 1 
ATOM   2721 C  CD2 . HIS B  1 71  ? 41.721  10.772  3.743   1.00 30.79  ? 57  HIS B CD2 1 
ATOM   2722 C  CE1 . HIS B  1 71  ? 41.622  12.698  2.717   1.00 30.89  ? 57  HIS B CE1 1 
ATOM   2723 N  NE2 . HIS B  1 71  ? 41.154  12.020  3.742   1.00 28.96  ? 57  HIS B NE2 1 
ATOM   2724 N  N   . PRO B  1 72  ? 42.164  10.392  -0.809  1.00 29.40  ? 58  PRO B N   1 
ATOM   2725 C  CA  . PRO B  1 72  ? 42.370  11.220  -2.000  1.00 31.32  ? 58  PRO B CA  1 
ATOM   2726 C  C   . PRO B  1 72  ? 43.547  12.190  -1.890  1.00 32.45  ? 58  PRO B C   1 
ATOM   2727 O  O   . PRO B  1 72  ? 44.140  12.560  -2.901  1.00 31.27  ? 58  PRO B O   1 
ATOM   2728 C  CB  . PRO B  1 72  ? 41.028  11.964  -2.181  1.00 32.36  ? 58  PRO B CB  1 
ATOM   2729 C  CG  . PRO B  1 72  ? 40.305  11.801  -0.858  1.00 32.72  ? 58  PRO B CG  1 
ATOM   2730 C  CD  . PRO B  1 72  ? 40.792  10.483  -0.283  1.00 28.52  ? 58  PRO B CD  1 
ATOM   2731 N  N   . GLU B  1 73  ? 43.885  12.595  -0.659  1.00 31.60  ? 59  GLU B N   1 
ATOM   2732 C  CA  . GLU B  1 73  ? 44.968  13.540  -0.433  1.00 30.70  ? 59  GLU B CA  1 
ATOM   2733 C  C   . GLU B  1 73  ? 46.313  12.812  -0.463  1.00 30.49  ? 59  GLU B C   1 
ATOM   2734 O  O   . GLU B  1 73  ? 47.365  13.445  -0.528  1.00 32.94  ? 59  GLU B O   1 
ATOM   2735 C  CB  . GLU B  1 73  ? 44.786  14.278  0.895   1.00 30.26  ? 59  GLU B CB  1 
ATOM   2736 C  CG  . GLU B  1 73  ? 43.569  15.198  0.925   1.00 30.00  ? 59  GLU B CG  1 
ATOM   2737 C  CD  . GLU B  1 73  ? 43.362  15.904  2.253   1.00 29.56  ? 59  GLU B CD  1 
ATOM   2738 O  OE1 . GLU B  1 73  ? 44.340  16.479  2.771   1.00 33.32  ? 59  GLU B OE1 1 
ATOM   2739 O  OE2 . GLU B  1 73  ? 42.226  15.889  2.768   1.00 34.89  ? 59  GLU B OE2 1 
ATOM   2740 N  N   . GLY B  1 74  ? 46.267  11.476  -0.414  1.00 26.70  ? 60  GLY B N   1 
ATOM   2741 C  CA  . GLY B  1 74  ? 47.475  10.664  -0.419  1.00 25.39  ? 60  GLY B CA  1 
ATOM   2742 C  C   . GLY B  1 74  ? 47.333  9.446   0.491   1.00 23.85  ? 60  GLY B C   1 
ATOM   2743 O  O   . GLY B  1 74  ? 46.558  9.464   1.444   1.00 27.07  ? 60  GLY B O   1 
ATOM   2744 N  N   . LYS B  1 75  ? 48.087  8.387   0.180   1.00 25.11  ? 61  LYS B N   1 
ATOM   2745 C  CA  . LYS B  1 75  ? 48.020  7.140   0.925   1.00 24.81  ? 61  LYS B CA  1 
ATOM   2746 C  C   . LYS B  1 75  ? 48.779  7.285   2.242   1.00 24.93  ? 61  LYS B C   1 
ATOM   2747 O  O   . LYS B  1 75  ? 49.907  7.777   2.270   1.00 22.80  ? 61  LYS B O   1 
ATOM   2748 C  CB  . LYS B  1 75  ? 48.550  5.986   0.068   1.00 24.85  ? 61  LYS B CB  1 
ATOM   2749 C  CG  . LYS B  1 75  ? 47.593  5.536   -1.031  1.00 27.52  ? 61  LYS B CG  1 
ATOM   2750 C  CD  . LYS B  1 75  ? 48.240  4.702   -2.128  1.00 31.73  ? 61  LYS B CD  1 
ATOM   2751 C  CE  . LYS B  1 75  ? 47.237  4.139   -3.091  1.00 35.14  ? 61  LYS B CE  1 
ATOM   2752 N  NZ  . LYS B  1 75  ? 46.359  5.174   -3.648  1.00 38.50  ? 61  LYS B NZ  1 
ATOM   2753 N  N   . ILE B  1 76  ? 48.124  6.852   3.326   1.00 23.76  ? 62  ILE B N   1 
ATOM   2754 C  CA  . ILE B  1 76  ? 48.674  6.914   4.670   1.00 23.66  ? 62  ILE B CA  1 
ATOM   2755 C  C   . ILE B  1 76  ? 48.763  5.490   5.219   1.00 23.72  ? 62  ILE B C   1 
ATOM   2756 O  O   . ILE B  1 76  ? 47.792  4.740   5.164   1.00 28.28  ? 62  ILE B O   1 
ATOM   2757 C  CB  . ILE B  1 76  ? 47.803  7.815   5.567   1.00 24.87  ? 62  ILE B CB  1 
ATOM   2758 C  CG1 . ILE B  1 76  ? 47.700  9.244   5.022   1.00 26.33  ? 62  ILE B CG1 1 
ATOM   2759 C  CG2 . ILE B  1 76  ? 48.309  7.796   7.010   1.00 26.40  ? 62  ILE B CG2 1 
ATOM   2760 C  CD1 . ILE B  1 76  ? 46.488  10.011  5.522   1.00 26.57  ? 62  ILE B CD1 1 
ATOM   2761 N  N   . LEU B  1 77  ? 49.938  5.137   5.754   1.00 22.72  ? 63  LEU B N   1 
ATOM   2762 C  CA  . LEU B  1 77  ? 50.186  3.810   6.295   1.00 23.44  ? 63  LEU B CA  1 
ATOM   2763 C  C   . LEU B  1 77  ? 50.469  3.922   7.791   1.00 22.93  ? 63  LEU B C   1 
ATOM   2764 O  O   . LEU B  1 77  ? 51.353  4.668   8.201   1.00 23.02  ? 63  LEU B O   1 
ATOM   2765 C  CB  . LEU B  1 77  ? 51.358  3.175   5.544   1.00 23.39  ? 63  LEU B CB  1 
ATOM   2766 C  CG  . LEU B  1 77  ? 51.747  1.753   5.964   1.00 26.96  ? 63  LEU B CG  1 
ATOM   2767 C  CD1 . LEU B  1 77  ? 50.605  0.776   5.733   1.00 29.02  ? 63  LEU B CD1 1 
ATOM   2768 C  CD2 . LEU B  1 77  ? 52.999  1.293   5.231   1.00 28.03  ? 63  LEU B CD2 1 
ATOM   2769 N  N   . PHE B  1 78  ? 49.701  3.176   8.597   1.00 23.94  ? 64  PHE B N   1 
ATOM   2770 C  CA  . PHE B  1 78  ? 49.892  3.139   10.038  1.00 23.82  ? 64  PHE B CA  1 
ATOM   2771 C  C   . PHE B  1 78  ? 50.625  1.847   10.401  1.00 22.83  ? 64  PHE B C   1 
ATOM   2772 O  O   . PHE B  1 78  ? 50.069  0.760   10.255  1.00 23.05  ? 64  PHE B O   1 
ATOM   2773 C  CB  . PHE B  1 78  ? 48.535  3.279   10.741  1.00 23.08  ? 64  PHE B CB  1 
ATOM   2774 C  CG  . PHE B  1 78  ? 48.623  3.378   12.258  1.00 23.96  ? 64  PHE B CG  1 
ATOM   2775 C  CD1 . PHE B  1 78  ? 48.911  4.590   12.877  1.00 24.85  ? 64  PHE B CD1 1 
ATOM   2776 C  CD2 . PHE B  1 78  ? 48.415  2.261   13.060  1.00 22.89  ? 64  PHE B CD2 1 
ATOM   2777 C  CE1 . PHE B  1 78  ? 48.999  4.676   14.258  1.00 26.10  ? 64  PHE B CE1 1 
ATOM   2778 C  CE2 . PHE B  1 78  ? 48.498  2.355   14.441  1.00 24.83  ? 64  PHE B CE2 1 
ATOM   2779 C  CZ  . PHE B  1 78  ? 48.790  3.561   15.037  1.00 23.49  ? 64  PHE B CZ  1 
ATOM   2780 N  N   . ASP B  1 79  ? 51.879  1.986   10.855  1.00 23.63  ? 65  ASP B N   1 
ATOM   2781 C  CA  . ASP B  1 79  ? 52.723  0.860   11.244  1.00 26.60  ? 65  ASP B CA  1 
ATOM   2782 C  C   . ASP B  1 79  ? 53.184  0.096   10.002  1.00 23.22  ? 65  ASP B C   1 
ATOM   2783 O  O   . ASP B  1 79  ? 52.633  0.294   8.921   1.00 22.51  ? 65  ASP B O   1 
ATOM   2784 C  CB  . ASP B  1 79  ? 52.030  -0.025  12.270  1.00 26.88  ? 65  ASP B CB  1 
ATOM   2785 C  CG  . ASP B  1 79  ? 52.064  0.497   13.701  1.00 30.19  ? 65  ASP B CG  1 
ATOM   2786 O  OD1 . ASP B  1 79  ? 52.795  1.479   13.950  1.00 25.38  ? 65  ASP B OD1 1 
ATOM   2787 O  OD2 . ASP B  1 79  ? 51.359  -0.081  14.557  1.00 32.41  ? 65  ASP B OD2 1 
ATOM   2788 N  N   . THR B  1 80  ? 54.195  -0.777  10.167  1.00 23.98  ? 66  THR B N   1 
ATOM   2789 C  CA  . THR B  1 80  ? 54.837  -1.440  9.037   1.00 25.10  ? 66  THR B CA  1 
ATOM   2790 C  C   . THR B  1 80  ? 55.229  -2.884  9.370   1.00 24.95  ? 66  THR B C   1 
ATOM   2791 O  O   . THR B  1 80  ? 55.979  -3.501  8.615   1.00 32.36  ? 66  THR B O   1 
ATOM   2792 C  CB  . THR B  1 80  ? 56.066  -0.646  8.581   1.00 22.92  ? 66  THR B CB  1 
ATOM   2793 O  OG1 . THR B  1 80  ? 57.053  -0.739  9.605   1.00 23.21  ? 66  THR B OG1 1 
ATOM   2794 C  CG2 . THR B  1 80  ? 55.765  0.815   8.299   1.00 23.26  ? 66  THR B CG2 1 
ATOM   2795 N  N   . SER B  1 81  ? 54.730  -3.425  10.489  1.00 25.44  ? 67  SER B N   1 
ATOM   2796 C  CA  . SER B  1 81  ? 54.986  -4.809  10.878  1.00 27.91  ? 67  SER B CA  1 
ATOM   2797 C  C   . SER B  1 81  ? 56.491  -5.084  10.976  1.00 29.88  ? 67  SER B C   1 
ATOM   2798 O  O   . SER B  1 81  ? 57.257  -4.208  11.375  1.00 32.29  ? 67  SER B O   1 
ATOM   2799 C  CB  . SER B  1 81  ? 54.299  -5.786  9.944   1.00 31.18  ? 67  SER B CB  1 
ATOM   2800 O  OG  . SER B  1 81  ? 54.891  -5.785  8.652   1.00 28.15  ? 67  SER B OG  1 
ATOM   2801 N  N   . CYS B  1 82  ? 56.904  -6.316  10.637  1.00 26.65  ? 68  CYS B N   1 
ATOM   2802 C  CA  . CYS B  1 82  ? 58.281  -6.761  10.818  1.00 26.83  ? 68  CYS B CA  1 
ATOM   2803 C  C   . CYS B  1 82  ? 59.001  -6.836  9.470   1.00 28.40  ? 68  CYS B C   1 
ATOM   2804 O  O   . CYS B  1 82  ? 58.364  -7.032  8.437   1.00 33.98  ? 68  CYS B O   1 
ATOM   2805 C  CB  . CYS B  1 82  ? 58.349  -8.140  11.472  1.00 27.56  ? 68  CYS B CB  1 
ATOM   2806 S  SG  . CYS B  1 82  ? 57.193  -8.380  12.848  1.00 26.75  ? 68  CYS B SG  1 
ATOM   2807 N  N   . ASN B  1 83  ? 60.334  -6.693  9.485   1.00 26.89  ? 69  ASN B N   1 
ATOM   2808 C  CA  . ASN B  1 83  ? 61.131  -6.839  8.275   1.00 28.56  ? 69  ASN B CA  1 
ATOM   2809 C  C   . ASN B  1 83  ? 61.081  -8.299  7.829   1.00 29.28  ? 69  ASN B C   1 
ATOM   2810 O  O   . ASN B  1 83  ? 61.209  -9.206  8.649   1.00 28.18  ? 69  ASN B O   1 
ATOM   2811 C  CB  . ASN B  1 83  ? 62.582  -6.401  8.460   1.00 28.56  ? 69  ASN B CB  1 
ATOM   2812 C  CG  . ASN B  1 83  ? 63.283  -6.165  7.141   1.00 29.74  ? 69  ASN B CG  1 
ATOM   2813 O  OD1 . ASN B  1 83  ? 63.112  -5.106  6.525   1.00 28.88  ? 69  ASN B OD1 1 
ATOM   2814 N  ND2 . ASN B  1 83  ? 64.082  -7.126  6.701   1.00 28.13  ? 69  ASN B ND2 1 
ATOM   2815 N  N   . PRO B  1 84  ? 60.868  -8.573  6.522   1.00 31.54  ? 70  PRO B N   1 
ATOM   2816 C  CA  . PRO B  1 84  ? 60.887  -9.947  6.012   1.00 35.04  ? 70  PRO B CA  1 
ATOM   2817 C  C   . PRO B  1 84  ? 62.131  -10.765 6.366   1.00 35.22  ? 70  PRO B C   1 
ATOM   2818 O  O   . PRO B  1 84  ? 62.070  -11.993 6.402   1.00 39.38  ? 70  PRO B O   1 
ATOM   2819 C  CB  . PRO B  1 84  ? 60.756  -9.750  4.488   1.00 32.24  ? 70  PRO B CB  1 
ATOM   2820 C  CG  . PRO B  1 84  ? 60.029  -8.428  4.337   1.00 35.30  ? 70  PRO B CG  1 
ATOM   2821 C  CD  . PRO B  1 84  ? 60.533  -7.577  5.491   1.00 31.56  ? 70  PRO B CD  1 
ATOM   2822 N  N   . ASN B  1 85  ? 63.259  -10.086 6.622   1.00 34.82  ? 71  ASN B N   1 
ATOM   2823 C  CA  . ASN B  1 85  ? 64.508  -10.764 6.944   1.00 34.47  ? 71  ASN B CA  1 
ATOM   2824 C  C   . ASN B  1 85  ? 64.790  -10.648 8.440   1.00 33.21  ? 71  ASN B C   1 
ATOM   2825 O  O   . ASN B  1 85  ? 65.922  -10.386 8.838   1.00 33.53  ? 71  ASN B O   1 
ATOM   2826 C  CB  . ASN B  1 85  ? 65.695  -10.213 6.152   1.00 39.34  ? 71  ASN B CB  1 
ATOM   2827 C  CG  . ASN B  1 85  ? 66.936  -11.072 6.279   1.00 46.21  ? 71  ASN B CG  1 
ATOM   2828 O  OD1 . ASN B  1 85  ? 66.848  -12.246 6.657   1.00 42.60  ? 71  ASN B OD1 1 
ATOM   2829 N  ND2 . ASN B  1 85  ? 68.096  -10.519 5.951   1.00 50.01  ? 71  ASN B ND2 1 
ATOM   2830 N  N   . SER B  1 86  ? 63.755  -10.857 9.263   1.00 33.68  ? 72  SER B N   1 
ATOM   2831 C  CA  . SER B  1 86  ? 63.874  -10.694 10.704  1.00 32.64  ? 72  SER B CA  1 
ATOM   2832 C  C   . SER B  1 86  ? 64.322  -12.003 11.354  1.00 32.10  ? 72  SER B C   1 
ATOM   2833 O  O   . SER B  1 86  ? 65.252  -12.013 12.158  1.00 27.66  ? 72  SER B O   1 
ATOM   2834 C  CB  . SER B  1 86  ? 62.570  -10.208 11.311  1.00 27.69  ? 72  SER B CB  1 
ATOM   2835 O  OG  . SER B  1 86  ? 62.212  -8.920  10.829  1.00 25.82  ? 72  SER B OG  1 
ATOM   2836 N  N   A MET B  1 87  ? 63.656  -13.102 10.979  0.60 30.46  ? 73  MET B N   1 
ATOM   2837 N  N   B MET B  1 87  ? 63.652  -13.102 10.986  0.40 31.87  ? 73  MET B N   1 
ATOM   2838 C  CA  A MET B  1 87  ? 63.830  -14.390 11.633  0.60 32.67  ? 73  MET B CA  1 
ATOM   2839 C  CA  B MET B  1 87  ? 63.832  -14.389 11.642  0.40 34.60  ? 73  MET B CA  1 
ATOM   2840 C  C   A MET B  1 87  ? 64.838  -15.237 10.858  0.60 35.45  ? 73  MET B C   1 
ATOM   2841 C  C   B MET B  1 87  ? 64.839  -15.234 10.862  0.40 36.61  ? 73  MET B C   1 
ATOM   2842 O  O   A MET B  1 87  ? 65.076  -14.998 9.677   0.60 35.08  ? 73  MET B O   1 
ATOM   2843 O  O   B MET B  1 87  ? 65.078  -14.989 9.682   0.40 36.39  ? 73  MET B O   1 
ATOM   2844 C  CB  A MET B  1 87  ? 62.490  -15.134 11.715  0.60 33.04  ? 73  MET B CB  1 
ATOM   2845 C  CB  B MET B  1 87  ? 62.494  -15.135 11.732  0.40 35.75  ? 73  MET B CB  1 
ATOM   2846 C  CG  A MET B  1 87  ? 61.432  -14.409 12.529  0.60 32.66  ? 73  MET B CG  1 
ATOM   2847 C  CG  B MET B  1 87  ? 61.428  -14.400 12.528  0.40 36.31  ? 73  MET B CG  1 
ATOM   2848 S  SD  A MET B  1 87  ? 61.747  -14.492 14.303  0.60 31.28  ? 73  MET B SD  1 
ATOM   2849 S  SD  B MET B  1 87  ? 61.709  -14.474 14.309  0.40 36.95  ? 73  MET B SD  1 
ATOM   2850 C  CE  A MET B  1 87  ? 61.545  -16.254 14.604  0.60 32.25  ? 73  MET B CE  1 
ATOM   2851 C  CE  B MET B  1 87  ? 61.585  -16.244 14.600  0.40 37.23  ? 73  MET B CE  1 
ATOM   2852 N  N   . GLY B  1 88  ? 65.428  -16.229 11.540  1.00 38.64  ? 74  GLY B N   1 
ATOM   2853 C  CA  . GLY B  1 88  ? 66.333  -17.177 10.902  1.00 40.79  ? 74  GLY B CA  1 
ATOM   2854 C  C   . GLY B  1 88  ? 67.794  -16.972 11.306  1.00 43.50  ? 74  GLY B C   1 
ATOM   2855 O  O   . GLY B  1 88  ? 68.145  -15.956 11.901  1.00 41.40  ? 74  GLY B O   1 
ATOM   2856 N  N   . PRO B  1 89  ? 68.691  -17.934 10.976  1.00 42.13  ? 75  PRO B N   1 
ATOM   2857 C  CA  . PRO B  1 89  ? 70.113  -17.836 11.322  1.00 43.53  ? 75  PRO B CA  1 
ATOM   2858 C  C   . PRO B  1 89  ? 70.823  -16.619 10.731  1.00 37.96  ? 75  PRO B C   1 
ATOM   2859 O  O   . PRO B  1 89  ? 71.784  -16.120 11.312  1.00 37.48  ? 75  PRO B O   1 
ATOM   2860 C  CB  . PRO B  1 89  ? 70.708  -19.155 10.779  1.00 45.61  ? 75  PRO B CB  1 
ATOM   2861 C  CG  . PRO B  1 89  ? 69.728  -19.598 9.713   1.00 45.57  ? 75  PRO B CG  1 
ATOM   2862 C  CD  . PRO B  1 89  ? 68.371  -19.171 10.247  1.00 47.09  ? 75  PRO B CD  1 
ATOM   2863 N  N   . GLN B  1 90  ? 70.354  -16.164 9.563   1.00 38.54  ? 76  GLN B N   1 
ATOM   2864 C  CA  . GLN B  1 90  ? 70.915  -14.994 8.904   1.00 44.79  ? 76  GLN B CA  1 
ATOM   2865 C  C   . GLN B  1 90  ? 69.974  -13.802 9.074   1.00 43.41  ? 76  GLN B C   1 
ATOM   2866 O  O   . GLN B  1 90  ? 70.075  -12.819 8.342   1.00 39.54  ? 76  GLN B O   1 
ATOM   2867 C  CB  . GLN B  1 90  ? 71.166  -15.255 7.417   1.00 46.28  ? 76  GLN B CB  1 
ATOM   2868 C  CG  . GLN B  1 90  ? 72.467  -15.996 7.124   1.00 55.56  ? 76  GLN B CG  1 
ATOM   2869 C  CD  . GLN B  1 90  ? 72.503  -17.381 7.729   1.00 61.26  ? 76  GLN B CD  1 
ATOM   2870 O  OE1 . GLN B  1 90  ? 71.700  -18.256 7.384   1.00 62.51  ? 76  GLN B OE1 1 
ATOM   2871 N  NE2 . GLN B  1 90  ? 73.437  -17.593 8.645   1.00 60.04  ? 76  GLN B NE2 1 
ATOM   2872 N  N   . GLY B  1 91  ? 69.065  -13.896 10.051  1.00 39.24  ? 77  GLY B N   1 
ATOM   2873 C  CA  . GLY B  1 91  ? 68.064  -12.865 10.280  1.00 41.56  ? 77  GLY B CA  1 
ATOM   2874 C  C   . GLY B  1 91  ? 68.632  -11.671 11.048  1.00 41.23  ? 77  GLY B C   1 
ATOM   2875 O  O   . GLY B  1 91  ? 69.685  -11.769 11.675  1.00 38.55  ? 77  GLY B O   1 
ATOM   2876 N  N   . ARG B  1 92  ? 67.903  -10.548 10.997  1.00 39.54  ? 78  ARG B N   1 
ATOM   2877 C  CA  . ARG B  1 92  ? 68.325  -9.302  11.619  1.00 35.87  ? 78  ARG B CA  1 
ATOM   2878 C  C   . ARG B  1 92  ? 68.130  -9.361  13.133  1.00 32.51  ? 78  ARG B C   1 
ATOM   2879 O  O   . ARG B  1 92  ? 68.914  -8.783  13.881  1.00 34.84  ? 78  ARG B O   1 
ATOM   2880 C  CB  . ARG B  1 92  ? 67.534  -8.119  11.047  1.00 33.65  ? 78  ARG B CB  1 
ATOM   2881 C  CG  . ARG B  1 92  ? 67.844  -7.778  9.597   1.00 33.96  ? 78  ARG B CG  1 
ATOM   2882 C  CD  . ARG B  1 92  ? 67.035  -6.575  9.140   1.00 30.77  ? 78  ARG B CD  1 
ATOM   2883 N  NE  . ARG B  1 92  ? 67.358  -6.155  7.774   1.00 30.92  ? 78  ARG B NE  1 
ATOM   2884 C  CZ  . ARG B  1 92  ? 66.901  -5.046  7.207   1.00 33.11  ? 78  ARG B CZ  1 
ATOM   2885 N  NH1 . ARG B  1 92  ? 66.114  -4.231  7.888   1.00 31.30  ? 78  ARG B NH1 1 
ATOM   2886 N  NH2 . ARG B  1 92  ? 67.239  -4.751  5.965   1.00 31.63  ? 78  ARG B NH2 1 
ATOM   2887 N  N   . TRP B  1 93  ? 67.065  -10.038 13.579  1.00 31.43  ? 79  TRP B N   1 
ATOM   2888 C  CA  . TRP B  1 93  ? 66.761  -10.138 14.999  1.00 30.95  ? 79  TRP B CA  1 
ATOM   2889 C  C   . TRP B  1 93  ? 67.792  -11.035 15.685  1.00 35.22  ? 79  TRP B C   1 
ATOM   2890 O  O   . TRP B  1 93  ? 68.116  -12.108 15.181  1.00 36.46  ? 79  TRP B O   1 
ATOM   2891 C  CB  . TRP B  1 93  ? 65.341  -10.687 15.219  1.00 28.88  ? 79  TRP B CB  1 
ATOM   2892 C  CG  . TRP B  1 93  ? 64.212  -9.793  14.765  1.00 27.06  ? 79  TRP B CG  1 
ATOM   2893 C  CD1 . TRP B  1 93  ? 64.295  -8.626  14.062  1.00 25.33  ? 79  TRP B CD1 1 
ATOM   2894 C  CD2 . TRP B  1 93  ? 62.800  -10.031 14.976  1.00 25.17  ? 79  TRP B CD2 1 
ATOM   2895 N  NE1 . TRP B  1 93  ? 63.042  -8.117  13.837  1.00 23.88  ? 79  TRP B NE1 1 
ATOM   2896 C  CE2 . TRP B  1 93  ? 62.104  -8.956  14.380  1.00 22.37  ? 79  TRP B CE2 1 
ATOM   2897 C  CE3 . TRP B  1 93  ? 62.060  -11.039 15.608  1.00 25.89  ? 79  TRP B CE3 1 
ATOM   2898 C  CZ2 . TRP B  1 93  ? 60.712  -8.867  14.401  1.00 24.72  ? 79  TRP B CZ2 1 
ATOM   2899 C  CZ3 . TRP B  1 93  ? 60.685  -10.949 15.627  1.00 23.53  ? 79  TRP B CZ3 1 
ATOM   2900 C  CH2 . TRP B  1 93  ? 60.022  -9.878  15.032  1.00 24.39  ? 79  TRP B CH2 1 
ATOM   2901 N  N   . ALA B  1 94  ? 68.297  -10.591 16.842  1.00 29.95  ? 80  ALA B N   1 
ATOM   2902 C  CA  . ALA B  1 94  ? 69.163  -11.417 17.669  1.00 29.69  ? 80  ALA B CA  1 
ATOM   2903 C  C   . ALA B  1 94  ? 68.430  -12.705 18.041  1.00 33.92  ? 80  ALA B C   1 
ATOM   2904 O  O   . ALA B  1 94  ? 67.201  -12.731 18.085  1.00 36.61  ? 80  ALA B O   1 
ATOM   2905 C  CB  . ALA B  1 94  ? 69.594  -10.645 18.897  1.00 29.54  ? 80  ALA B CB  1 
ATOM   2906 N  N   . GLU B  1 95  ? 69.195  -13.768 18.315  1.00 41.07  ? 81  GLU B N   1 
ATOM   2907 C  CA  . GLU B  1 95  ? 68.624  -15.086 18.549  1.00 43.67  ? 81  GLU B CA  1 
ATOM   2908 C  C   . GLU B  1 95  ? 67.732  -15.039 19.788  1.00 34.77  ? 81  GLU B C   1 
ATOM   2909 O  O   . GLU B  1 95  ? 66.664  -15.647 19.813  1.00 38.04  ? 81  GLU B O   1 
ATOM   2910 C  CB  . GLU B  1 95  ? 69.733  -16.135 18.671  1.00 50.44  ? 81  GLU B CB  1 
ATOM   2911 C  CG  . GLU B  1 95  ? 70.867  -15.941 17.666  1.00 64.58  ? 81  GLU B CG  1 
ATOM   2912 C  CD  . GLU B  1 95  ? 71.980  -15.008 18.120  1.00 79.16  ? 81  GLU B CD  1 
ATOM   2913 O  OE1 . GLU B  1 95  ? 72.741  -15.403 19.030  1.00 91.50  ? 81  GLU B OE1 1 
ATOM   2914 O  OE2 . GLU B  1 95  ? 72.087  -13.889 17.571  1.00 60.45  ? 81  GLU B OE2 1 
ATOM   2915 N  N   . SER B  1 96  ? 68.186  -14.301 20.807  1.00 34.90  ? 82  SER B N   1 
ATOM   2916 C  CA  . SER B  1 96  ? 67.423  -14.092 22.028  1.00 34.66  ? 82  SER B CA  1 
ATOM   2917 C  C   . SER B  1 96  ? 66.025  -13.570 21.699  1.00 33.80  ? 82  SER B C   1 
ATOM   2918 O  O   . SER B  1 96  ? 65.033  -14.052 22.243  1.00 32.31  ? 82  SER B O   1 
ATOM   2919 C  CB  . SER B  1 96  ? 68.148  -13.146 22.956  1.00 36.64  ? 82  SER B CB  1 
ATOM   2920 O  OG  . SER B  1 96  ? 68.529  -11.958 22.277  1.00 37.79  ? 82  SER B OG  1 
ATOM   2921 N  N   . THR B  1 97  ? 65.969  -12.567 20.815  1.00 34.62  ? 83  THR B N   1 
ATOM   2922 C  CA  . THR B  1 97  ? 64.721  -11.909 20.460  1.00 34.79  ? 83  THR B CA  1 
ATOM   2923 C  C   . THR B  1 97  ? 63.834  -12.888 19.691  1.00 31.17  ? 83  THR B C   1 
ATOM   2924 O  O   . THR B  1 97  ? 62.618  -12.900 19.872  1.00 27.77  ? 83  THR B O   1 
ATOM   2925 C  CB  . THR B  1 97  ? 65.020  -10.637 19.661  1.00 35.12  ? 83  THR B CB  1 
ATOM   2926 O  OG1 . THR B  1 97  ? 65.793  -9.796  20.513  1.00 35.53  ? 83  THR B OG1 1 
ATOM   2927 C  CG2 . THR B  1 97  ? 63.767  -9.898  19.223  1.00 34.84  ? 83  THR B CG2 1 
ATOM   2928 N  N   . GLN B  1 98  ? 64.460  -13.716 18.844  1.00 30.49  ? 84  GLN B N   1 
ATOM   2929 C  CA  . GLN B  1 98  ? 63.743  -14.688 18.031  1.00 32.52  ? 84  GLN B CA  1 
ATOM   2930 C  C   . GLN B  1 98  ? 63.094  -15.749 18.920  1.00 30.45  ? 84  GLN B C   1 
ATOM   2931 O  O   . GLN B  1 98  ? 62.025  -16.264 18.597  1.00 37.33  ? 84  GLN B O   1 
ATOM   2932 C  CB  . GLN B  1 98  ? 64.683  -15.333 17.011  1.00 30.49  ? 84  GLN B CB  1 
ATOM   2933 C  CG  . GLN B  1 98  ? 65.192  -14.374 15.938  1.00 31.07  ? 84  GLN B CG  1 
ATOM   2934 C  CD  . GLN B  1 98  ? 65.771  -15.089 14.737  1.00 31.67  ? 84  GLN B CD  1 
ATOM   2935 O  OE1 . GLN B  1 98  ? 65.275  -16.140 14.316  1.00 33.60  ? 84  GLN B OE1 1 
ATOM   2936 N  NE2 . GLN B  1 98  ? 66.836  -14.533 14.176  1.00 27.43  ? 84  GLN B NE2 1 
ATOM   2937 N  N   . GLN B  1 99  ? 63.750  -16.070 20.042  1.00 33.05  ? 85  GLN B N   1 
ATOM   2938 C  CA  . GLN B  1 99  ? 63.289  -17.120 20.938  1.00 32.78  ? 85  GLN B CA  1 
ATOM   2939 C  C   . GLN B  1 99  ? 62.196  -16.589 21.863  1.00 31.60  ? 85  GLN B C   1 
ATOM   2940 O  O   . GLN B  1 99  ? 61.315  -17.340 22.277  1.00 30.37  ? 85  GLN B O   1 
ATOM   2941 C  CB  . GLN B  1 99  ? 64.474  -17.695 21.717  1.00 38.67  ? 85  GLN B CB  1 
ATOM   2942 C  CG  . GLN B  1 99  ? 65.147  -18.875 21.021  1.00 45.17  ? 85  GLN B CG  1 
ATOM   2943 C  CD  . GLN B  1 99  ? 66.642  -18.930 21.247  1.00 56.44  ? 85  GLN B CD  1 
ATOM   2944 O  OE1 . GLN B  1 99  ? 67.222  -18.089 21.944  1.00 71.48  ? 85  GLN B OE1 1 
ATOM   2945 N  NE2 . GLN B  1 99  ? 67.287  -19.920 20.647  1.00 68.93  ? 85  GLN B NE2 1 
ATOM   2946 N  N   . MET B  1 100 ? 62.256  -15.287 22.170  1.00 30.48  ? 86  MET B N   1 
ATOM   2947 C  CA  . MET B  1 100 ? 61.329  -14.672 23.109  1.00 30.29  ? 86  MET B CA  1 
ATOM   2948 C  C   . MET B  1 100 ? 60.121  -14.087 22.378  1.00 26.59  ? 86  MET B C   1 
ATOM   2949 O  O   . MET B  1 100 ? 59.025  -14.044 22.936  1.00 31.00  ? 86  MET B O   1 
ATOM   2950 C  CB  . MET B  1 100 ? 62.020  -13.569 23.920  1.00 31.14  ? 86  MET B CB  1 
ATOM   2951 C  CG  . MET B  1 100 ? 62.624  -14.054 25.224  1.00 34.38  ? 86  MET B CG  1 
ATOM   2952 S  SD  . MET B  1 100 ? 63.139  -12.694 26.292  1.00 37.77  ? 86  MET B SD  1 
ATOM   2953 C  CE  . MET B  1 100 ? 64.286  -11.818 25.218  1.00 36.06  ? 86  MET B CE  1 
ATOM   2954 N  N   . PHE B  1 101 ? 60.326  -13.641 21.132  1.00 25.72  ? 87  PHE B N   1 
ATOM   2955 C  CA  . PHE B  1 101 ? 59.285  -12.950 20.384  1.00 26.88  ? 87  PHE B CA  1 
ATOM   2956 C  C   . PHE B  1 101 ? 59.189  -13.489 18.958  1.00 28.07  ? 87  PHE B C   1 
ATOM   2957 O  O   . PHE B  1 101 ? 59.227  -12.717 18.004  1.00 28.78  ? 87  PHE B O   1 
ATOM   2958 C  CB  . PHE B  1 101 ? 59.573  -11.446 20.347  1.00 28.07  ? 87  PHE B CB  1 
ATOM   2959 C  CG  . PHE B  1 101 ? 59.799  -10.832 21.719  1.00 28.68  ? 87  PHE B CG  1 
ATOM   2960 C  CD1 . PHE B  1 101 ? 58.725  -10.556 22.558  1.00 26.83  ? 87  PHE B CD1 1 
ATOM   2961 C  CD2 . PHE B  1 101 ? 61.083  -10.537 22.165  1.00 30.68  ? 87  PHE B CD2 1 
ATOM   2962 C  CE1 . PHE B  1 101 ? 58.933  -10.003 23.811  1.00 25.85  ? 87  PHE B CE1 1 
ATOM   2963 C  CE2 . PHE B  1 101 ? 61.283  -9.981  23.419  1.00 32.02  ? 87  PHE B CE2 1 
ATOM   2964 C  CZ  . PHE B  1 101 ? 60.209  -9.718  24.238  1.00 29.01  ? 87  PHE B CZ  1 
ATOM   2965 N  N   . PRO B  1 102 ? 59.014  -14.816 18.762  1.00 29.74  ? 88  PRO B N   1 
ATOM   2966 C  CA  . PRO B  1 102 ? 59.011  -15.398 17.417  1.00 30.13  ? 88  PRO B CA  1 
ATOM   2967 C  C   . PRO B  1 102 ? 57.922  -14.843 16.501  1.00 26.26  ? 88  PRO B C   1 
ATOM   2968 O  O   . PRO B  1 102 ? 56.754  -14.782 16.881  1.00 29.05  ? 88  PRO B O   1 
ATOM   2969 C  CB  . PRO B  1 102 ? 58.808  -16.904 17.683  1.00 31.64  ? 88  PRO B CB  1 
ATOM   2970 C  CG  . PRO B  1 102 ? 58.138  -16.956 19.040  1.00 34.73  ? 88  PRO B CG  1 
ATOM   2971 C  CD  . PRO B  1 102 ? 58.784  -15.818 19.815  1.00 34.46  ? 88  PRO B CD  1 
ATOM   2972 N  N   . TRP B  1 103 ? 58.327  -14.457 15.285  1.00 25.99  ? 89  TRP B N   1 
ATOM   2973 C  CA  . TRP B  1 103 ? 57.404  -14.050 14.236  1.00 26.02  ? 89  TRP B CA  1 
ATOM   2974 C  C   . TRP B  1 103 ? 57.272  -15.179 13.217  1.00 28.49  ? 89  TRP B C   1 
ATOM   2975 O  O   . TRP B  1 103 ? 58.278  -15.703 12.743  1.00 33.91  ? 89  TRP B O   1 
ATOM   2976 C  CB  . TRP B  1 103 ? 57.911  -12.761 13.566  1.00 26.89  ? 89  TRP B CB  1 
ATOM   2977 C  CG  . TRP B  1 103 ? 57.038  -12.209 12.466  1.00 26.72  ? 89  TRP B CG  1 
ATOM   2978 C  CD1 . TRP B  1 103 ? 55.685  -12.034 12.485  1.00 26.82  ? 89  TRP B CD1 1 
ATOM   2979 C  CD2 . TRP B  1 103 ? 57.484  -11.732 11.175  1.00 27.66  ? 89  TRP B CD2 1 
ATOM   2980 N  NE1 . TRP B  1 103 ? 55.258  -11.486 11.304  1.00 29.76  ? 89  TRP B NE1 1 
ATOM   2981 C  CE2 . TRP B  1 103 ? 56.336  -11.289 10.481  1.00 28.21  ? 89  TRP B CE2 1 
ATOM   2982 C  CE3 . TRP B  1 103 ? 58.732  -11.637 10.544  1.00 26.21  ? 89  TRP B CE3 1 
ATOM   2983 C  CZ2 . TRP B  1 103 ? 56.406  -10.763 9.192   1.00 26.69  ? 89  TRP B CZ2 1 
ATOM   2984 C  CZ3 . TRP B  1 103 ? 58.798  -11.114 9.271   1.00 25.94  ? 89  TRP B CZ3 1 
ATOM   2985 C  CH2 . TRP B  1 103 ? 57.650  -10.683 8.606   1.00 27.29  ? 89  TRP B CH2 1 
ATOM   2986 N  N   . THR B  1 104 ? 56.031  -15.555 12.892  1.00 30.99  ? 90  THR B N   1 
ATOM   2987 C  CA  . THR B  1 104 ? 55.789  -16.502 11.814  1.00 32.45  ? 90  THR B CA  1 
ATOM   2988 C  C   . THR B  1 104 ? 54.842  -15.857 10.805  1.00 32.36  ? 90  THR B C   1 
ATOM   2989 O  O   . THR B  1 104 ? 53.816  -15.289 11.176  1.00 29.82  ? 90  THR B O   1 
ATOM   2990 C  CB  . THR B  1 104 ? 55.258  -17.830 12.358  1.00 32.34  ? 90  THR B CB  1 
ATOM   2991 O  OG1 . THR B  1 104 ? 54.042  -17.518 13.033  1.00 34.92  ? 90  THR B OG1 1 
ATOM   2992 C  CG2 . THR B  1 104 ? 56.246  -18.514 13.290  1.00 33.24  ? 90  THR B CG2 1 
ATOM   2993 N  N   . ALA B  1 105 ? 55.224  -15.935 9.526   1.00 32.73  ? 91  ALA B N   1 
ATOM   2994 C  CA  . ALA B  1 105 ? 54.478  -15.308 8.448   1.00 34.62  ? 91  ALA B CA  1 
ATOM   2995 C  C   . ALA B  1 105 ? 54.716  -16.067 7.147   1.00 32.45  ? 91  ALA B C   1 
ATOM   2996 O  O   . ALA B  1 105 ? 55.849  -16.426 6.834   1.00 36.83  ? 91  ALA B O   1 
ATOM   2997 C  CB  . ALA B  1 105 ? 54.894  -13.858 8.307   1.00 32.65  ? 91  ALA B CB  1 
ATOM   2998 N  N   . THR B  1 106 ? 53.633  -16.303 6.399   1.00 33.87  ? 92  THR B N   1 
ATOM   2999 C  CA  . THR B  1 106 ? 53.740  -16.774 5.028   1.00 37.89  ? 92  THR B CA  1 
ATOM   3000 C  C   . THR B  1 106 ? 54.101  -15.568 4.159   1.00 43.58  ? 92  THR B C   1 
ATOM   3001 O  O   . THR B  1 106 ? 53.981  -14.428 4.606   1.00 34.95  ? 92  THR B O   1 
ATOM   3002 C  CB  . THR B  1 106 ? 52.439  -17.461 4.604   1.00 40.69  ? 92  THR B CB  1 
ATOM   3003 O  OG1 . THR B  1 106 ? 51.399  -16.492 4.706   1.00 41.99  ? 92  THR B OG1 1 
ATOM   3004 C  CG2 . THR B  1 106 ? 52.091  -18.653 5.481   1.00 41.65  ? 92  THR B CG2 1 
ATOM   3005 N  N   . GLU B  1 107 ? 54.574  -15.821 2.932   1.00 41.60  ? 93  GLU B N   1 
ATOM   3006 C  CA  . GLU B  1 107 ? 55.062  -14.754 2.070   1.00 40.54  ? 93  GLU B CA  1 
ATOM   3007 C  C   . GLU B  1 107 ? 53.934  -13.763 1.782   1.00 37.11  ? 93  GLU B C   1 
ATOM   3008 O  O   . GLU B  1 107 ? 54.187  -12.576 1.595   1.00 37.42  ? 93  GLU B O   1 
ATOM   3009 C  CB  . GLU B  1 107 ? 55.688  -15.312 0.790   1.00 50.04  ? 93  GLU B CB  1 
ATOM   3010 C  CG  . GLU B  1 107 ? 57.186  -15.583 0.918   1.00 59.90  ? 93  GLU B CG  1 
ATOM   3011 C  CD  . GLU B  1 107 ? 57.777  -16.474 -0.161  1.00 67.44  ? 93  GLU B CD  1 
ATOM   3012 O  OE1 . GLU B  1 107 ? 57.038  -16.855 -1.092  1.00 66.83  ? 93  GLU B OE1 1 
ATOM   3013 O  OE2 . GLU B  1 107 ? 58.981  -16.793 -0.061  1.00 81.74  ? 93  GLU B OE2 1 
ATOM   3014 N  N   . GLU B  1 108 ? 52.688  -14.253 1.764   1.00 35.61  ? 94  GLU B N   1 
ATOM   3015 C  CA  . GLU B  1 108 ? 51.542  -13.411 1.453   1.00 37.22  ? 94  GLU B CA  1 
ATOM   3016 C  C   . GLU B  1 108 ? 51.334  -12.393 2.575   1.00 36.57  ? 94  GLU B C   1 
ATOM   3017 O  O   . GLU B  1 108 ? 50.622  -11.407 2.391   1.00 32.21  ? 94  GLU B O   1 
ATOM   3018 C  CB  . GLU B  1 108 ? 50.280  -14.241 1.203   1.00 40.92  ? 94  GLU B CB  1 
ATOM   3019 C  CG  . GLU B  1 108 ? 49.800  -15.038 2.413   1.00 52.01  ? 94  GLU B CG  1 
ATOM   3020 C  CD  . GLU B  1 108 ? 48.423  -15.661 2.245   1.00 64.87  ? 94  GLU B CD  1 
ATOM   3021 O  OE1 . GLU B  1 108 ? 48.280  -16.546 1.376   1.00 74.18  ? 94  GLU B OE1 1 
ATOM   3022 O  OE2 . GLU B  1 108 ? 47.492  -15.257 2.976   1.00 73.66  ? 94  GLU B OE2 1 
ATOM   3023 N  N   . CYS B  1 109 ? 51.977  -12.632 3.725   1.00 31.12  ? 95  CYS B N   1 
ATOM   3024 C  CA  . CYS B  1 109 ? 51.791  -11.803 4.908   1.00 30.13  ? 95  CYS B CA  1 
ATOM   3025 C  C   . CYS B  1 109 ? 52.775  -10.631 4.927   1.00 29.90  ? 95  CYS B C   1 
ATOM   3026 O  O   . CYS B  1 109 ? 52.521  -9.634  5.601   1.00 29.76  ? 95  CYS B O   1 
ATOM   3027 C  CB  . CYS B  1 109 ? 51.923  -12.624 6.188   1.00 28.50  ? 95  CYS B CB  1 
ATOM   3028 S  SG  . CYS B  1 109 ? 50.457  -13.616 6.581   1.00 30.67  ? 95  CYS B SG  1 
ATOM   3029 N  N   . TYR B  1 110 ? 53.895  -10.746 4.199   1.00 28.72  ? 96  TYR B N   1 
ATOM   3030 C  CA  . TYR B  1 110 ? 54.873  -9.667  4.124   1.00 27.98  ? 96  TYR B CA  1 
ATOM   3031 C  C   . TYR B  1 110 ? 54.169  -8.399  3.636   1.00 28.38  ? 96  TYR B C   1 
ATOM   3032 O  O   . TYR B  1 110 ? 53.361  -8.450  2.712   1.00 26.39  ? 96  TYR B O   1 
ATOM   3033 C  CB  . TYR B  1 110 ? 56.058  -10.008 3.210   1.00 30.00  ? 96  TYR B CB  1 
ATOM   3034 C  CG  . TYR B  1 110 ? 56.908  -11.203 3.631   1.00 33.77  ? 96  TYR B CG  1 
ATOM   3035 C  CD1 . TYR B  1 110 ? 56.896  -11.677 4.938   1.00 34.13  ? 96  TYR B CD1 1 
ATOM   3036 C  CD2 . TYR B  1 110 ? 57.735  -11.852 2.718   1.00 36.76  ? 96  TYR B CD2 1 
ATOM   3037 C  CE1 . TYR B  1 110 ? 57.669  -12.762 5.320   1.00 37.33  ? 96  TYR B CE1 1 
ATOM   3038 C  CE2 . TYR B  1 110 ? 58.512  -12.938 3.089   1.00 34.90  ? 96  TYR B CE2 1 
ATOM   3039 C  CZ  . TYR B  1 110 ? 58.480  -13.394 4.394   1.00 38.11  ? 96  TYR B CZ  1 
ATOM   3040 O  OH  . TYR B  1 110 ? 59.242  -14.462 4.772   1.00 38.72  ? 96  TYR B OH  1 
ATOM   3041 N  N   . LEU B  1 111 ? 54.494  -7.259  4.259   1.00 27.71  ? 97  LEU B N   1 
ATOM   3042 C  CA  . LEU B  1 111 ? 53.808  -6.005  3.985   1.00 27.09  ? 97  LEU B CA  1 
ATOM   3043 C  C   . LEU B  1 111 ? 53.888  -5.664  2.496   1.00 25.30  ? 97  LEU B C   1 
ATOM   3044 O  O   . LEU B  1 111 ? 52.903  -5.213  1.917   1.00 23.65  ? 97  LEU B O   1 
ATOM   3045 C  CB  . LEU B  1 111 ? 54.393  -4.886  4.848   1.00 28.98  ? 97  LEU B CB  1 
ATOM   3046 C  CG  . LEU B  1 111 ? 53.824  -3.484  4.601   1.00 29.32  ? 97  LEU B CG  1 
ATOM   3047 C  CD1 . LEU B  1 111 ? 52.330  -3.446  4.881   1.00 31.72  ? 97  LEU B CD1 1 
ATOM   3048 C  CD2 . LEU B  1 111 ? 54.553  -2.438  5.431   1.00 28.91  ? 97  LEU B CD2 1 
ATOM   3049 N  N   . HIS B  1 112 ? 55.062  -5.869  1.882   1.00 28.06  ? 98  HIS B N   1 
ATOM   3050 C  CA  . HIS B  1 112 ? 55.271  -5.456  0.501   1.00 29.75  ? 98  HIS B CA  1 
ATOM   3051 C  C   . HIS B  1 112 ? 54.346  -6.265  -0.410  1.00 27.87  ? 98  HIS B C   1 
ATOM   3052 O  O   . HIS B  1 112 ? 53.893  -5.766  -1.437  1.00 24.57  ? 98  HIS B O   1 
ATOM   3053 C  CB  . HIS B  1 112 ? 56.759  -5.500  0.112   1.00 35.15  ? 98  HIS B CB  1 
ATOM   3054 C  CG  . HIS B  1 112 ? 57.320  -6.851  -0.198  1.00 42.73  ? 98  HIS B CG  1 
ATOM   3055 N  ND1 . HIS B  1 112 ? 58.128  -7.544  0.679   1.00 47.87  ? 98  HIS B ND1 1 
ATOM   3056 C  CD2 . HIS B  1 112 ? 57.235  -7.613  -1.299  1.00 44.63  ? 98  HIS B CD2 1 
ATOM   3057 C  CE1 . HIS B  1 112 ? 58.490  -8.695  0.127   1.00 45.22  ? 98  HIS B CE1 1 
ATOM   3058 N  NE2 . HIS B  1 112 ? 57.957  -8.758  -1.074  1.00 47.30  ? 98  HIS B NE2 1 
ATOM   3059 N  N   . ASN B  1 113 ? 54.040  -7.502  -0.003  1.00 26.87  ? 99  ASN B N   1 
ATOM   3060 C  CA  . ASN B  1 113 ? 53.166  -8.376  -0.772  1.00 27.82  ? 99  ASN B CA  1 
ATOM   3061 C  C   . ASN B  1 113 ? 51.709  -7.950  -0.583  1.00 28.30  ? 99  ASN B C   1 
ATOM   3062 O  O   . ASN B  1 113 ? 50.951  -7.901  -1.548  1.00 26.97  ? 99  ASN B O   1 
ATOM   3063 C  CB  . ASN B  1 113 ? 53.400  -9.843  -0.420  1.00 27.80  ? 99  ASN B CB  1 
ATOM   3064 C  CG  . ASN B  1 113 ? 54.712  -10.360 -0.963  1.00 28.30  ? 99  ASN B CG  1 
ATOM   3065 O  OD1 . ASN B  1 113 ? 55.280  -11.314 -0.420  1.00 31.11  ? 99  ASN B OD1 1 
ATOM   3066 N  ND2 . ASN B  1 113 ? 55.223  -9.731  -2.011  1.00 30.84  ? 99  ASN B ND2 1 
ATOM   3067 N  N   . ARG B  1 114 ? 51.326  -7.638  0.661   1.00 28.61  ? 100 ARG B N   1 
ATOM   3068 C  CA  . ARG B  1 114 ? 49.966  -7.217  0.966   1.00 29.38  ? 100 ARG B CA  1 
ATOM   3069 C  C   . ARG B  1 114 ? 49.621  -5.970  0.153   1.00 27.84  ? 100 ARG B C   1 
ATOM   3070 O  O   . ARG B  1 114 ? 48.529  -5.869  -0.405  1.00 33.31  ? 100 ARG B O   1 
ATOM   3071 C  CB  . ARG B  1 114 ? 49.802  -6.969  2.471   1.00 30.35  ? 100 ARG B CB  1 
ATOM   3072 C  CG  . ARG B  1 114 ? 49.744  -8.230  3.323   1.00 30.10  ? 100 ARG B CG  1 
ATOM   3073 C  CD  . ARG B  1 114 ? 48.431  -8.989  3.163   1.00 30.14  ? 100 ARG B CD  1 
ATOM   3074 N  NE  . ARG B  1 114 ? 48.339  -10.135 4.075   1.00 28.55  ? 100 ARG B NE  1 
ATOM   3075 C  CZ  . ARG B  1 114 ? 47.808  -11.314 3.768   1.00 30.52  ? 100 ARG B CZ  1 
ATOM   3076 N  NH1 . ARG B  1 114 ? 47.250  -11.502 2.586   1.00 29.12  ? 100 ARG B NH1 1 
ATOM   3077 N  NH2 . ARG B  1 114 ? 47.817  -12.293 4.656   1.00 29.82  ? 100 ARG B NH2 1 
ATOM   3078 N  N   . LEU B  1 115 ? 50.566  -5.024  0.095   1.00 29.06  ? 101 LEU B N   1 
ATOM   3079 C  CA  . LEU B  1 115 ? 50.399  -3.791  -0.659  1.00 28.95  ? 101 LEU B CA  1 
ATOM   3080 C  C   . LEU B  1 115 ? 50.294  -4.107  -2.150  1.00 25.83  ? 101 LEU B C   1 
ATOM   3081 O  O   . LEU B  1 115 ? 49.460  -3.538  -2.851  1.00 25.78  ? 101 LEU B O   1 
ATOM   3082 C  CB  . LEU B  1 115 ? 51.573  -2.854  -0.375  1.00 26.37  ? 101 LEU B CB  1 
ATOM   3083 C  CG  . LEU B  1 115 ? 51.589  -2.186  1.004   1.00 27.59  ? 101 LEU B CG  1 
ATOM   3084 C  CD1 . LEU B  1 115 ? 52.881  -1.415  1.222   1.00 25.85  ? 101 LEU B CD1 1 
ATOM   3085 C  CD2 . LEU B  1 115 ? 50.389  -1.269  1.174   1.00 25.30  ? 101 LEU B CD2 1 
ATOM   3086 N  N   . GLU B  1 116 ? 51.162  -5.012  -2.618  1.00 29.09  ? 102 GLU B N   1 
ATOM   3087 C  CA  . GLU B  1 116 ? 51.192  -5.414  -4.015  1.00 31.86  ? 102 GLU B CA  1 
ATOM   3088 C  C   . GLU B  1 116 ? 49.823  -5.964  -4.413  1.00 31.02  ? 102 GLU B C   1 
ATOM   3089 O  O   . GLU B  1 116 ? 49.306  -5.629  -5.476  1.00 28.45  ? 102 GLU B O   1 
ATOM   3090 C  CB  . GLU B  1 116 ? 52.311  -6.432  -4.249  1.00 32.38  ? 102 GLU B CB  1 
ATOM   3091 C  CG  . GLU B  1 116 ? 52.339  -6.999  -5.666  1.00 38.73  ? 102 GLU B CG  1 
ATOM   3092 C  CD  . GLU B  1 116 ? 53.519  -7.911  -5.959  1.00 44.43  ? 102 GLU B CD  1 
ATOM   3093 O  OE1 . GLU B  1 116 ? 54.417  -8.028  -5.097  1.00 41.58  ? 102 GLU B OE1 1 
ATOM   3094 O  OE2 . GLU B  1 116 ? 53.533  -8.515  -7.052  1.00 53.57  ? 102 GLU B OE2 1 
ATOM   3095 N  N   . GLN B  1 117 ? 49.245  -6.799  -3.537  1.00 32.81  ? 103 GLN B N   1 
ATOM   3096 C  CA  . GLN B  1 117 ? 47.945  -7.415  -3.766  1.00 33.17  ? 103 GLN B CA  1 
ATOM   3097 C  C   . GLN B  1 117 ? 46.877  -6.336  -3.932  1.00 31.58  ? 103 GLN B C   1 
ATOM   3098 O  O   . GLN B  1 117 ? 45.791  -6.610  -4.437  1.00 36.16  ? 103 GLN B O   1 
ATOM   3099 C  CB  . GLN B  1 117 ? 47.565  -8.337  -2.602  1.00 41.90  ? 103 GLN B CB  1 
ATOM   3100 C  CG  . GLN B  1 117 ? 48.604  -9.409  -2.272  1.00 44.09  ? 103 GLN B CG  1 
ATOM   3101 C  CD  . GLN B  1 117 ? 48.460  -9.981  -0.877  1.00 48.44  ? 103 GLN B CD  1 
ATOM   3102 O  OE1 . GLN B  1 117 ? 47.440  -9.800  -0.200  1.00 37.92  ? 103 GLN B OE1 1 
ATOM   3103 N  NE2 . GLN B  1 117 ? 49.490  -10.688 -0.431  1.00 35.56  ? 103 GLN B NE2 1 
ATOM   3104 N  N   . LEU B  1 118 ? 47.191  -5.113  -3.491  1.00 30.03  ? 104 LEU B N   1 
ATOM   3105 C  CA  . LEU B  1 118 ? 46.257  -4.001  -3.559  1.00 31.84  ? 104 LEU B CA  1 
ATOM   3106 C  C   . LEU B  1 118 ? 46.652  -3.055  -4.693  1.00 30.54  ? 104 LEU B C   1 
ATOM   3107 O  O   . LEU B  1 118 ? 45.996  -2.038  -4.910  1.00 31.74  ? 104 LEU B O   1 
ATOM   3108 C  CB  . LEU B  1 118 ? 46.231  -3.277  -2.212  1.00 31.85  ? 104 LEU B CB  1 
ATOM   3109 C  CG  . LEU B  1 118 ? 45.584  -4.035  -1.047  1.00 30.14  ? 104 LEU B CG  1 
ATOM   3110 C  CD1 . LEU B  1 118 ? 45.707  -3.245  0.247   1.00 28.05  ? 104 LEU B CD1 1 
ATOM   3111 C  CD2 . LEU B  1 118 ? 44.124  -4.353  -1.337  1.00 32.55  ? 104 LEU B CD2 1 
ATOM   3112 N  N   . LYS B  1 119 ? 47.734  -3.397  -5.404  1.00 29.40  ? 105 LYS B N   1 
ATOM   3113 C  CA  . LYS B  1 119 ? 48.244  -2.575  -6.493  1.00 32.59  ? 105 LYS B CA  1 
ATOM   3114 C  C   . LYS B  1 119 ? 48.755  -1.254  -5.922  1.00 30.12  ? 105 LYS B C   1 
ATOM   3115 O  O   . LYS B  1 119 ? 48.537  -0.187  -6.491  1.00 28.58  ? 105 LYS B O   1 
ATOM   3116 C  CB  . LYS B  1 119 ? 47.169  -2.367  -7.568  1.00 38.58  ? 105 LYS B CB  1 
ATOM   3117 C  CG  . LYS B  1 119 ? 46.707  -3.644  -8.261  1.00 43.87  ? 105 LYS B CG  1 
ATOM   3118 C  CD  . LYS B  1 119 ? 45.567  -3.439  -9.252  1.00 51.89  ? 105 LYS B CD  1 
ATOM   3119 C  CE  . LYS B  1 119 ? 45.911  -2.489  -10.360 1.00 53.62  ? 105 LYS B CE  1 
ATOM   3120 N  NZ  . LYS B  1 119 ? 44.811  -2.357  -11.323 1.00 59.68  ? 105 LYS B NZ  1 
ATOM   3121 N  N   . VAL B  1 120 ? 49.439  -1.353  -4.779  1.00 30.41  ? 106 VAL B N   1 
ATOM   3122 C  CA  . VAL B  1 120 ? 50.047  -0.205  -4.128  1.00 31.00  ? 106 VAL B CA  1 
ATOM   3123 C  C   . VAL B  1 120 ? 51.537  -0.494  -3.957  1.00 30.33  ? 106 VAL B C   1 
ATOM   3124 O  O   . VAL B  1 120 ? 51.907  -1.449  -3.278  1.00 32.70  ? 106 VAL B O   1 
ATOM   3125 C  CB  . VAL B  1 120 ? 49.368  0.084   -2.773  1.00 30.80  ? 106 VAL B CB  1 
ATOM   3126 C  CG1 . VAL B  1 120 ? 50.082  1.189   -2.004  1.00 30.51  ? 106 VAL B CG1 1 
ATOM   3127 C  CG2 . VAL B  1 120 ? 47.884  0.409   -2.931  1.00 30.48  ? 106 VAL B CG2 1 
ATOM   3128 N  N   A ARG B  1 121 ? 52.387  0.321   -4.592  0.60 32.52  ? 107 ARG B N   1 
ATOM   3129 N  N   B ARG B  1 121 ? 52.372  0.339   -4.592  0.40 30.90  ? 107 ARG B N   1 
ATOM   3130 C  CA  A ARG B  1 121 ? 53.828  0.181   -4.441  0.60 37.63  ? 107 ARG B CA  1 
ATOM   3131 C  CA  B ARG B  1 121 ? 53.819  0.254   -4.463  0.40 33.39  ? 107 ARG B CA  1 
ATOM   3132 C  C   A ARG B  1 121 ? 54.294  1.085   -3.301  0.60 33.02  ? 107 ARG B C   1 
ATOM   3133 C  C   B ARG B  1 121 ? 54.256  1.072   -3.251  0.40 30.90  ? 107 ARG B C   1 
ATOM   3134 O  O   A ARG B  1 121 ? 53.708  2.138   -3.056  0.60 32.46  ? 107 ARG B O   1 
ATOM   3135 O  O   B ARG B  1 121 ? 53.608  2.056   -2.901  0.40 29.28  ? 107 ARG B O   1 
ATOM   3136 C  CB  A ARG B  1 121 ? 54.558  0.466   -5.761  0.60 44.54  ? 107 ARG B CB  1 
ATOM   3137 C  CB  B ARG B  1 121 ? 54.507  0.781   -5.729  0.40 35.94  ? 107 ARG B CB  1 
ATOM   3138 C  CG  A ARG B  1 121 ? 54.583  -0.721  -6.715  0.60 50.77  ? 107 ARG B CG  1 
ATOM   3139 C  CG  B ARG B  1 121 ? 54.166  -0.004  -6.987  0.40 38.98  ? 107 ARG B CG  1 
ATOM   3140 C  CD  A ARG B  1 121 ? 55.013  -0.360  -8.133  0.60 54.49  ? 107 ARG B CD  1 
ATOM   3141 C  CD  B ARG B  1 121 ? 54.378  0.820   -8.248  0.40 40.53  ? 107 ARG B CD  1 
ATOM   3142 N  NE  A ARG B  1 121 ? 56.429  0.004   -8.256  0.60 57.77  ? 107 ARG B NE  1 
ATOM   3143 N  NE  B ARG B  1 121 ? 54.098  2.244   -8.037  0.40 41.16  ? 107 ARG B NE  1 
ATOM   3144 C  CZ  A ARG B  1 121 ? 57.006  0.397   -9.387  0.60 58.94  ? 107 ARG B CZ  1 
ATOM   3145 C  CZ  B ARG B  1 121 ? 53.560  3.057   -8.942  0.40 41.93  ? 107 ARG B CZ  1 
ATOM   3146 N  NH1 A ARG B  1 121 ? 56.285  0.514   -10.488 0.60 59.09  ? 107 ARG B NH1 1 
ATOM   3147 N  NH1 B ARG B  1 121 ? 53.142  2.575   -10.099 0.40 44.30  ? 107 ARG B NH1 1 
ATOM   3148 N  NH2 A ARG B  1 121 ? 58.298  0.680   -9.414  0.60 52.29  ? 107 ARG B NH2 1 
ATOM   3149 N  NH2 B ARG B  1 121 ? 53.442  4.348   -8.686  0.40 41.27  ? 107 ARG B NH2 1 
ATOM   3150 N  N   . PRO B  1 122 ? 55.356  0.691   -2.563  1.00 34.10  ? 108 PRO B N   1 
ATOM   3151 C  CA  . PRO B  1 122 ? 55.862  1.497   -1.451  1.00 32.47  ? 108 PRO B CA  1 
ATOM   3152 C  C   . PRO B  1 122 ? 56.055  2.966   -1.828  1.00 33.77  ? 108 PRO B C   1 
ATOM   3153 O  O   . PRO B  1 122 ? 55.892  3.850   -0.990  1.00 30.70  ? 108 PRO B O   1 
ATOM   3154 C  CB  . PRO B  1 122 ? 57.189  0.794   -1.109  1.00 33.27  ? 108 PRO B CB  1 
ATOM   3155 C  CG  . PRO B  1 122 ? 56.964  -0.645  -1.526  1.00 33.33  ? 108 PRO B CG  1 
ATOM   3156 C  CD  . PRO B  1 122 ? 56.126  -0.544  -2.790  1.00 33.60  ? 108 PRO B CD  1 
ATOM   3157 N  N   A GLU B  1 123 ? 56.394  3.209   -3.100  0.50 33.14  ? 109 GLU B N   1 
ATOM   3158 N  N   B GLU B  1 123 ? 56.390  3.211   -3.101  0.50 34.65  ? 109 GLU B N   1 
ATOM   3159 C  CA  A GLU B  1 123 ? 56.689  4.550   -3.579  0.50 33.11  ? 109 GLU B CA  1 
ATOM   3160 C  CA  B GLU B  1 123 ? 56.685  4.553   -3.579  0.50 35.78  ? 109 GLU B CA  1 
ATOM   3161 C  C   A GLU B  1 123 ? 55.408  5.387   -3.608  0.50 33.17  ? 109 GLU B C   1 
ATOM   3162 C  C   B GLU B  1 123 ? 55.407  5.391   -3.591  0.50 34.47  ? 109 GLU B C   1 
ATOM   3163 O  O   A GLU B  1 123 ? 55.470  6.608   -3.737  0.50 34.54  ? 109 GLU B O   1 
ATOM   3164 O  O   B GLU B  1 123 ? 55.469  6.615   -3.693  0.50 35.50  ? 109 GLU B O   1 
ATOM   3165 C  CB  A GLU B  1 123 ? 57.360  4.500   -4.955  0.50 35.09  ? 109 GLU B CB  1 
ATOM   3166 C  CB  B GLU B  1 123 ? 57.325  4.509   -4.969  0.50 40.48  ? 109 GLU B CB  1 
ATOM   3167 C  CG  A GLU B  1 123 ? 58.740  3.846   -4.953  0.50 34.16  ? 109 GLU B CG  1 
ATOM   3168 C  CG  B GLU B  1 123 ? 56.373  4.036   -6.064  0.50 41.70  ? 109 GLU B CG  1 
ATOM   3169 C  CD  A GLU B  1 123 ? 58.733  2.329   -4.874  0.50 34.11  ? 109 GLU B CD  1 
ATOM   3170 C  CD  B GLU B  1 123 ? 56.915  4.181   -7.476  0.50 44.32  ? 109 GLU B CD  1 
ATOM   3171 O  OE1 A GLU B  1 123 ? 57.634  1.739   -4.887  0.50 29.97  ? 109 GLU B OE1 1 
ATOM   3172 O  OE1 B GLU B  1 123 ? 57.316  5.306   -7.846  0.50 46.83  ? 109 GLU B OE1 1 
ATOM   3173 O  OE2 A GLU B  1 123 ? 59.831  1.737   -4.802  0.50 36.57  ? 109 GLU B OE2 1 
ATOM   3174 O  OE2 B GLU B  1 123 ? 56.925  3.170   -8.209  0.50 42.57  ? 109 GLU B OE2 1 
ATOM   3175 N  N   . ASP B  1 124 ? 54.251  4.724   -3.474  1.00 35.52  ? 110 ASP B N   1 
ATOM   3176 C  CA  . ASP B  1 124 ? 52.958  5.391   -3.571  1.00 34.24  ? 110 ASP B CA  1 
ATOM   3177 C  C   . ASP B  1 124 ? 52.501  5.924   -2.213  1.00 31.48  ? 110 ASP B C   1 
ATOM   3178 O  O   . ASP B  1 124 ? 51.515  6.655   -2.136  1.00 29.64  ? 110 ASP B O   1 
ATOM   3179 C  CB  . ASP B  1 124 ? 51.889  4.472   -4.147  1.00 43.01  ? 110 ASP B CB  1 
ATOM   3180 C  CG  . ASP B  1 124 ? 52.146  3.985   -5.566  1.00 46.70  ? 110 ASP B CG  1 
ATOM   3181 O  OD1 . ASP B  1 124 ? 52.475  4.831   -6.423  1.00 40.35  ? 110 ASP B OD1 1 
ATOM   3182 O  OD2 . ASP B  1 124 ? 52.001  2.767   -5.804  1.00 51.95  ? 110 ASP B OD2 1 
ATOM   3183 N  N   . ILE B  1 125 ? 53.212  5.553   -1.145  1.00 26.08  ? 111 ILE B N   1 
ATOM   3184 C  CA  . ILE B  1 125 ? 52.826  5.950   0.199   1.00 26.83  ? 111 ILE B CA  1 
ATOM   3185 C  C   . ILE B  1 125 ? 53.336  7.365   0.470   1.00 27.22  ? 111 ILE B C   1 
ATOM   3186 O  O   . ILE B  1 125 ? 54.525  7.639   0.319   1.00 26.99  ? 111 ILE B O   1 
ATOM   3187 C  CB  . ILE B  1 125 ? 53.345  4.941   1.241   1.00 26.19  ? 111 ILE B CB  1 
ATOM   3188 C  CG1 . ILE B  1 125 ? 52.787  3.533   1.000   1.00 25.23  ? 111 ILE B CG1 1 
ATOM   3189 C  CG2 . ILE B  1 125 ? 53.052  5.429   2.659   1.00 24.22  ? 111 ILE B CG2 1 
ATOM   3190 C  CD1 . ILE B  1 125 ? 51.270  3.455   0.985   1.00 25.63  ? 111 ILE B CD1 1 
ATOM   3191 N  N   . ARG B  1 126 ? 52.419  8.250   0.882   1.00 26.44  ? 112 ARG B N   1 
ATOM   3192 C  CA  . ARG B  1 126 ? 52.742  9.645   1.138   1.00 29.09  ? 112 ARG B CA  1 
ATOM   3193 C  C   . ARG B  1 126 ? 53.217  9.807   2.581   1.00 27.43  ? 112 ARG B C   1 
ATOM   3194 O  O   . ARG B  1 126 ? 54.186  10.520  2.840   1.00 25.71  ? 112 ARG B O   1 
ATOM   3195 C  CB  . ARG B  1 126 ? 51.536  10.557  0.876   1.00 31.21  ? 112 ARG B CB  1 
ATOM   3196 C  CG  . ARG B  1 126 ? 51.913  12.028  0.748   1.00 38.38  ? 112 ARG B CG  1 
ATOM   3197 C  CD  . ARG B  1 126 ? 50.741  12.994  0.841   1.00 43.01  ? 112 ARG B CD  1 
ATOM   3198 N  NE  . ARG B  1 126 ? 51.239  14.374  0.823   1.00 52.00  ? 112 ARG B NE  1 
ATOM   3199 C  CZ  . ARG B  1 126 ? 50.529  15.459  1.104   1.00 53.15  ? 112 ARG B CZ  1 
ATOM   3200 N  NH1 . ARG B  1 126 ? 49.252  15.353  1.428   1.00 50.27  ? 112 ARG B NH1 1 
ATOM   3201 N  NH2 . ARG B  1 126 ? 51.106  16.648  1.065   1.00 56.38  ? 112 ARG B NH2 1 
ATOM   3202 N  N   . TYR B  1 127 ? 52.522  9.143   3.514   1.00 23.67  ? 113 TYR B N   1 
ATOM   3203 C  CA  . TYR B  1 127 ? 52.820  9.257   4.933   1.00 24.26  ? 113 TYR B CA  1 
ATOM   3204 C  C   . TYR B  1 127 ? 52.857  7.874   5.579   1.00 23.95  ? 113 TYR B C   1 
ATOM   3205 O  O   . TYR B  1 127 ? 51.985  7.044   5.330   1.00 27.18  ? 113 TYR B O   1 
ATOM   3206 C  CB  . TYR B  1 127 ? 51.772  10.085  5.685   1.00 26.19  ? 113 TYR B CB  1 
ATOM   3207 C  CG  . TYR B  1 127 ? 51.711  11.560  5.312   1.00 28.29  ? 113 TYR B CG  1 
ATOM   3208 C  CD1 . TYR B  1 127 ? 52.748  12.427  5.639   1.00 29.38  ? 113 TYR B CD1 1 
ATOM   3209 C  CD2 . TYR B  1 127 ? 50.604  12.092  4.659   1.00 32.19  ? 113 TYR B CD2 1 
ATOM   3210 C  CE1 . TYR B  1 127 ? 52.698  13.772  5.309   1.00 31.69  ? 113 TYR B CE1 1 
ATOM   3211 C  CE2 . TYR B  1 127 ? 50.541  13.436  4.326   1.00 35.10  ? 113 TYR B CE2 1 
ATOM   3212 C  CZ  . TYR B  1 127 ? 51.590  14.278  4.652   1.00 31.45  ? 113 TYR B CZ  1 
ATOM   3213 O  OH  . TYR B  1 127 ? 51.535  15.603  4.329   1.00 37.38  ? 113 TYR B OH  1 
ATOM   3214 N  N   . VAL B  1 128 ? 53.865  7.662   6.434   1.00 23.01  ? 114 VAL B N   1 
ATOM   3215 C  CA  . VAL B  1 128 ? 53.912  6.515   7.326   1.00 23.66  ? 114 VAL B CA  1 
ATOM   3216 C  C   . VAL B  1 128 ? 53.874  7.039   8.760   1.00 24.01  ? 114 VAL B C   1 
ATOM   3217 O  O   . VAL B  1 128 ? 54.722  7.839   9.147   1.00 22.80  ? 114 VAL B O   1 
ATOM   3218 C  CB  . VAL B  1 128 ? 55.165  5.645   7.094   1.00 25.34  ? 114 VAL B CB  1 
ATOM   3219 C  CG1 . VAL B  1 128 ? 55.211  4.450   8.040   1.00 26.34  ? 114 VAL B CG1 1 
ATOM   3220 C  CG2 . VAL B  1 128 ? 55.284  5.188   5.645   1.00 27.16  ? 114 VAL B CG2 1 
ATOM   3221 N  N   . VAL B  1 129 ? 52.870  6.598   9.530   1.00 21.78  ? 115 VAL B N   1 
ATOM   3222 C  CA  . VAL B  1 129 ? 52.792  6.922   10.945  1.00 21.38  ? 115 VAL B CA  1 
ATOM   3223 C  C   . VAL B  1 129 ? 53.340  5.733   11.734  1.00 20.65  ? 115 VAL B C   1 
ATOM   3224 O  O   . VAL B  1 129 ? 52.747  4.657   11.728  1.00 21.01  ? 115 VAL B O   1 
ATOM   3225 C  CB  . VAL B  1 129 ? 51.353  7.277   11.379  1.00 22.23  ? 115 VAL B CB  1 
ATOM   3226 C  CG1 . VAL B  1 129 ? 51.266  7.563   12.873  1.00 22.07  ? 115 VAL B CG1 1 
ATOM   3227 C  CG2 . VAL B  1 129 ? 50.786  8.447   10.581  1.00 22.63  ? 115 VAL B CG2 1 
ATOM   3228 N  N   . ALA B  1 130 ? 54.492  5.940   12.386  1.00 22.17  ? 116 ALA B N   1 
ATOM   3229 C  CA  . ALA B  1 130 ? 55.106  4.933   13.238  1.00 21.86  ? 116 ALA B CA  1 
ATOM   3230 C  C   . ALA B  1 130 ? 54.591  5.091   14.667  1.00 22.04  ? 116 ALA B C   1 
ATOM   3231 O  O   . ALA B  1 130 ? 54.979  6.027   15.365  1.00 21.28  ? 116 ALA B O   1 
ATOM   3232 C  CB  . ALA B  1 130 ? 56.616  5.058   13.175  1.00 22.87  ? 116 ALA B CB  1 
ATOM   3233 N  N   . SER B  1 131 ? 53.714  4.172   15.094  1.00 21.20  ? 117 SER B N   1 
ATOM   3234 C  CA  . SER B  1 131 ? 53.123  4.235   16.423  1.00 23.17  ? 117 SER B CA  1 
ATOM   3235 C  C   . SER B  1 131 ? 54.237  4.262   17.466  1.00 20.00  ? 117 SER B C   1 
ATOM   3236 O  O   . SER B  1 131 ? 54.148  4.979   18.460  1.00 18.36  ? 117 SER B O   1 
ATOM   3237 C  CB  . SER B  1 131 ? 52.160  3.089   16.662  1.00 21.97  ? 117 SER B CB  1 
ATOM   3238 O  OG  . SER B  1 131 ? 52.841  1.843   16.706  1.00 25.11  ? 117 SER B OG  1 
ATOM   3239 N  N   . HIS B  1 132 ? 55.274  3.455   17.211  1.00 18.74  ? 118 HIS B N   1 
ATOM   3240 C  CA  . HIS B  1 132 ? 56.517  3.445   17.968  1.00 19.79  ? 118 HIS B CA  1 
ATOM   3241 C  C   . HIS B  1 132 ? 57.528  2.656   17.134  1.00 20.52  ? 118 HIS B C   1 
ATOM   3242 O  O   . HIS B  1 132 ? 57.199  2.238   16.028  1.00 20.73  ? 118 HIS B O   1 
ATOM   3243 C  CB  . HIS B  1 132 ? 56.292  2.945   19.402  1.00 20.21  ? 118 HIS B CB  1 
ATOM   3244 C  CG  . HIS B  1 132 ? 55.774  1.548   19.533  1.00 20.20  ? 118 HIS B CG  1 
ATOM   3245 N  ND1 . HIS B  1 132 ? 54.688  1.055   18.841  1.00 23.91  ? 118 HIS B ND1 1 
ATOM   3246 C  CD2 . HIS B  1 132 ? 56.192  0.544   20.324  1.00 22.19  ? 118 HIS B CD2 1 
ATOM   3247 C  CE1 . HIS B  1 132 ? 54.476  -0.208  19.199  1.00 22.68  ? 118 HIS B CE1 1 
ATOM   3248 N  NE2 . HIS B  1 132 ? 55.381  -0.540  20.095  1.00 19.71  ? 118 HIS B NE2 1 
ATOM   3249 N  N   . LEU B  1 133 ? 58.752  2.457   17.642  1.00 19.46  ? 119 LEU B N   1 
ATOM   3250 C  CA  . LEU B  1 133 ? 59.821  1.919   16.810  1.00 18.44  ? 119 LEU B CA  1 
ATOM   3251 C  C   . LEU B  1 133 ? 60.224  0.514   17.266  1.00 18.95  ? 119 LEU B C   1 
ATOM   3252 O  O   . LEU B  1 133 ? 61.340  0.067   17.004  1.00 20.68  ? 119 LEU B O   1 
ATOM   3253 C  CB  . LEU B  1 133 ? 60.988  2.908   16.807  1.00 18.26  ? 119 LEU B CB  1 
ATOM   3254 C  CG  . LEU B  1 133 ? 60.716  4.231   16.082  1.00 19.98  ? 119 LEU B CG  1 
ATOM   3255 C  CD1 . LEU B  1 133 ? 61.928  5.152   16.081  1.00 21.74  ? 119 LEU B CD1 1 
ATOM   3256 C  CD2 . LEU B  1 133 ? 60.248  3.969   14.658  1.00 21.30  ? 119 LEU B CD2 1 
ATOM   3257 N  N   . HIS B  1 134 ? 59.282  -0.196  17.898  1.00 19.11  ? 120 HIS B N   1 
ATOM   3258 C  CA  . HIS B  1 134 ? 59.465  -1.591  18.273  1.00 22.29  ? 120 HIS B CA  1 
ATOM   3259 C  C   . HIS B  1 134 ? 59.580  -2.468  17.025  1.00 24.37  ? 120 HIS B C   1 
ATOM   3260 O  O   . HIS B  1 134 ? 59.171  -2.066  15.936  1.00 23.43  ? 120 HIS B O   1 
ATOM   3261 C  CB  . HIS B  1 134 ? 58.336  -2.063  19.199  1.00 24.95  ? 120 HIS B CB  1 
ATOM   3262 C  CG  . HIS B  1 134 ? 58.589  -1.784  20.645  1.00 26.14  ? 120 HIS B CG  1 
ATOM   3263 N  ND1 . HIS B  1 134 ? 57.641  -1.960  21.631  1.00 27.40  ? 120 HIS B ND1 1 
ATOM   3264 C  CD2 . HIS B  1 134 ? 59.704  -1.377  21.267  1.00 24.92  ? 120 HIS B CD2 1 
ATOM   3265 C  CE1 . HIS B  1 134 ? 58.174  -1.650  22.806  1.00 25.60  ? 120 HIS B CE1 1 
ATOM   3266 N  NE2 . HIS B  1 134 ? 59.425  -1.291  22.607  1.00 25.21  ? 120 HIS B NE2 1 
ATOM   3267 N  N   . LEU B  1 135 ? 60.113  -3.683  17.214  1.00 22.13  ? 121 LEU B N   1 
ATOM   3268 C  CA  . LEU B  1 135 ? 60.563  -4.532  16.121  1.00 24.39  ? 121 LEU B CA  1 
ATOM   3269 C  C   . LEU B  1 135 ? 59.411  -4.882  15.178  1.00 25.92  ? 121 LEU B C   1 
ATOM   3270 O  O   . LEU B  1 135 ? 59.629  -5.014  13.976  1.00 27.39  ? 121 LEU B O   1 
ATOM   3271 C  CB  . LEU B  1 135 ? 61.243  -5.786  16.678  1.00 26.55  ? 121 LEU B CB  1 
ATOM   3272 C  CG  . LEU B  1 135 ? 60.352  -6.785  17.427  1.00 27.27  ? 121 LEU B CG  1 
ATOM   3273 C  CD1 . LEU B  1 135 ? 61.174  -7.970  17.922  1.00 26.47  ? 121 LEU B CD1 1 
ATOM   3274 C  CD2 . LEU B  1 135 ? 59.621  -6.133  18.587  1.00 27.93  ? 121 LEU B CD2 1 
ATOM   3275 N  N   . ASN B  1 136 ? 58.188  -5.018  15.713  1.00 26.66  ? 122 ASN B N   1 
ATOM   3276 C  CA  . ASN B  1 136 ? 57.063  -5.513  14.931  1.00 28.80  ? 122 ASN B CA  1 
ATOM   3277 C  C   . ASN B  1 136 ? 56.139  -4.369  14.505  1.00 28.38  ? 122 ASN B C   1 
ATOM   3278 O  O   . ASN B  1 136 ? 54.992  -4.615  14.137  1.00 28.89  ? 122 ASN B O   1 
ATOM   3279 C  CB  . ASN B  1 136 ? 56.277  -6.597  15.669  1.00 29.16  ? 122 ASN B CB  1 
ATOM   3280 C  CG  . ASN B  1 136 ? 55.874  -6.187  17.065  1.00 31.35  ? 122 ASN B CG  1 
ATOM   3281 O  OD1 . ASN B  1 136 ? 56.358  -5.175  17.583  1.00 29.42  ? 122 ASN B OD1 1 
ATOM   3282 N  ND2 . ASN B  1 136 ? 55.001  -6.962  17.693  1.00 33.23  ? 122 ASN B ND2 1 
ATOM   3283 N  N   . HIS B  1 137 ? 56.640  -3.126  14.536  1.00 24.80  ? 123 HIS B N   1 
ATOM   3284 C  CA  . HIS B  1 137 ? 55.865  -1.983  14.072  1.00 24.06  ? 123 HIS B CA  1 
ATOM   3285 C  C   . HIS B  1 137 ? 56.658  -1.154  13.058  1.00 23.44  ? 123 HIS B C   1 
ATOM   3286 O  O   . HIS B  1 137 ? 56.062  -0.520  12.190  1.00 22.85  ? 123 HIS B O   1 
ATOM   3287 C  CB  . HIS B  1 137 ? 55.377  -1.132  15.252  1.00 25.12  ? 123 HIS B CB  1 
ATOM   3288 C  CG  . HIS B  1 137 ? 54.380  -1.831  16.120  1.00 24.18  ? 123 HIS B CG  1 
ATOM   3289 N  ND1 . HIS B  1 137 ? 53.027  -1.564  16.089  1.00 26.18  ? 123 HIS B ND1 1 
ATOM   3290 C  CD2 . HIS B  1 137 ? 54.546  -2.786  17.048  1.00 23.45  ? 123 HIS B CD2 1 
ATOM   3291 C  CE1 . HIS B  1 137 ? 52.405  -2.342  16.967  1.00 25.64  ? 123 HIS B CE1 1 
ATOM   3292 N  NE2 . HIS B  1 137 ? 53.310  -3.093  17.561  1.00 25.02  ? 123 HIS B NE2 1 
ATOM   3293 N  N   . ALA B  1 138 ? 57.995  -1.170  13.164  1.00 22.36  ? 124 ALA B N   1 
ATOM   3294 C  CA  . ALA B  1 138 ? 58.847  -0.310  12.350  1.00 22.09  ? 124 ALA B CA  1 
ATOM   3295 C  C   . ALA B  1 138 ? 59.732  -1.137  11.415  1.00 23.41  ? 124 ALA B C   1 
ATOM   3296 O  O   . ALA B  1 138 ? 60.688  -0.620  10.841  1.00 22.56  ? 124 ALA B O   1 
ATOM   3297 C  CB  . ALA B  1 138 ? 59.691  0.571   13.248  1.00 23.09  ? 124 ALA B CB  1 
ATOM   3298 N  N   . GLY B  1 139 ? 59.399  -2.423  11.266  1.00 25.97  ? 125 GLY B N   1 
ATOM   3299 C  CA  . GLY B  1 139 ? 60.211  -3.369  10.515  1.00 28.46  ? 125 GLY B CA  1 
ATOM   3300 C  C   . GLY B  1 139 ? 60.442  -2.973  9.055   1.00 26.42  ? 125 GLY B C   1 
ATOM   3301 O  O   . GLY B  1 139 ? 61.495  -3.285  8.501   1.00 28.60  ? 125 GLY B O   1 
ATOM   3302 N  N   . CYS B  1 140 ? 59.465  -2.303  8.428   1.00 26.65  ? 126 CYS B N   1 
ATOM   3303 C  CA  . CYS B  1 140 ? 59.509  -2.079  6.989   1.00 27.13  ? 126 CYS B CA  1 
ATOM   3304 C  C   . CYS B  1 140 ? 59.533  -0.591  6.637   1.00 24.12  ? 126 CYS B C   1 
ATOM   3305 O  O   . CYS B  1 140 ? 59.182  -0.218  5.519   1.00 26.12  ? 126 CYS B O   1 
ATOM   3306 C  CB  . CYS B  1 140 ? 58.326  -2.746  6.294   1.00 27.16  ? 126 CYS B CB  1 
ATOM   3307 S  SG  . CYS B  1 140 ? 58.299  -4.549  6.471   1.00 29.66  ? 126 CYS B SG  1 
ATOM   3308 N  N   . LEU B  1 141 ? 59.971  0.254   7.578   1.00 25.56  ? 127 LEU B N   1 
ATOM   3309 C  CA  . LEU B  1 141 ? 60.072  1.687   7.339   1.00 23.39  ? 127 LEU B CA  1 
ATOM   3310 C  C   . LEU B  1 141 ? 60.933  1.961   6.105   1.00 22.98  ? 127 LEU B C   1 
ATOM   3311 O  O   . LEU B  1 141 ? 60.633  2.858   5.320   1.00 21.89  ? 127 LEU B O   1 
ATOM   3312 C  CB  . LEU B  1 141 ? 60.656  2.378   8.573   1.00 25.41  ? 127 LEU B CB  1 
ATOM   3313 C  CG  . LEU B  1 141 ? 59.685  2.662   9.723   1.00 27.51  ? 127 LEU B CG  1 
ATOM   3314 C  CD1 . LEU B  1 141 ? 60.382  3.457   10.819  1.00 26.34  ? 127 LEU B CD1 1 
ATOM   3315 C  CD2 . LEU B  1 141 ? 58.446  3.397   9.239   1.00 24.33  ? 127 LEU B CD2 1 
ATOM   3316 N  N   . GLU B  1 142 ? 62.006  1.178   5.945   1.00 23.66  ? 128 GLU B N   1 
ATOM   3317 C  CA  . GLU B  1 142 ? 63.032  1.444   4.946   1.00 28.31  ? 128 GLU B CA  1 
ATOM   3318 C  C   . GLU B  1 142 ? 62.449  1.412   3.532   1.00 29.19  ? 128 GLU B C   1 
ATOM   3319 O  O   . GLU B  1 142 ? 63.035  1.975   2.610   1.00 32.04  ? 128 GLU B O   1 
ATOM   3320 C  CB  . GLU B  1 142 ? 64.177  0.436   5.080   1.00 27.37  ? 128 GLU B CB  1 
ATOM   3321 C  CG  . GLU B  1 142 ? 63.760  -1.010  4.830   1.00 28.88  ? 128 GLU B CG  1 
ATOM   3322 C  CD  . GLU B  1 142 ? 64.772  -2.033  5.316   1.00 33.33  ? 128 GLU B CD  1 
ATOM   3323 O  OE1 . GLU B  1 142 ? 65.456  -2.649  4.472   1.00 35.50  ? 128 GLU B OE1 1 
ATOM   3324 O  OE2 . GLU B  1 142 ? 64.867  -2.223  6.546   1.00 30.86  ? 128 GLU B OE2 1 
ATOM   3325 N  N   . MET B  1 143 ? 61.294  0.757   3.370   1.00 28.52  ? 129 MET B N   1 
ATOM   3326 C  CA  . MET B  1 143 ? 60.673  0.574   2.066   1.00 29.77  ? 129 MET B CA  1 
ATOM   3327 C  C   . MET B  1 143 ? 60.105  1.891   1.539   1.00 27.60  ? 129 MET B C   1 
ATOM   3328 O  O   . MET B  1 143 ? 59.941  2.057   0.333   1.00 27.97  ? 129 MET B O   1 
ATOM   3329 C  CB  . MET B  1 143 ? 59.512  -0.424  2.148   1.00 32.27  ? 129 MET B CB  1 
ATOM   3330 C  CG  . MET B  1 143 ? 59.917  -1.885  2.154   1.00 35.57  ? 129 MET B CG  1 
ATOM   3331 S  SD  . MET B  1 143 ? 58.517  -2.945  2.577   1.00 44.77  ? 129 MET B SD  1 
ATOM   3332 C  CE  . MET B  1 143 ? 57.230  -2.234  1.544   1.00 46.45  ? 129 MET B CE  1 
ATOM   3333 N  N   . PHE B  1 144 ? 59.778  2.814   2.452   1.00 25.17  ? 130 PHE B N   1 
ATOM   3334 C  CA  . PHE B  1 144 ? 58.969  3.974   2.110   1.00 24.38  ? 130 PHE B CA  1 
ATOM   3335 C  C   . PHE B  1 144 ? 59.864  5.201   1.940   1.00 27.93  ? 130 PHE B C   1 
ATOM   3336 O  O   . PHE B  1 144 ? 59.875  6.090   2.788   1.00 29.05  ? 130 PHE B O   1 
ATOM   3337 C  CB  . PHE B  1 144 ? 57.879  4.113   3.178   1.00 25.43  ? 130 PHE B CB  1 
ATOM   3338 C  CG  . PHE B  1 144 ? 57.041  2.848   3.300   1.00 22.72  ? 130 PHE B CG  1 
ATOM   3339 C  CD1 . PHE B  1 144 ? 56.146  2.492   2.297   1.00 23.24  ? 130 PHE B CD1 1 
ATOM   3340 C  CD2 . PHE B  1 144 ? 57.181  1.996   4.389   1.00 20.80  ? 130 PHE B CD2 1 
ATOM   3341 C  CE1 . PHE B  1 144 ? 55.401  1.326   2.392   1.00 25.11  ? 130 PHE B CE1 1 
ATOM   3342 C  CE2 . PHE B  1 144 ? 56.430  0.833   4.480   1.00 24.49  ? 130 PHE B CE2 1 
ATOM   3343 C  CZ  . PHE B  1 144 ? 55.543  0.501   3.482   1.00 24.50  ? 130 PHE B CZ  1 
ATOM   3344 N  N   . THR B  1 145 ? 60.578  5.242   0.807   1.00 27.21  ? 131 THR B N   1 
ATOM   3345 C  CA  . THR B  1 145 ? 61.599  6.248   0.548   1.00 27.72  ? 131 THR B CA  1 
ATOM   3346 C  C   . THR B  1 145 ? 60.976  7.500   -0.077  1.00 28.59  ? 131 THR B C   1 
ATOM   3347 O  O   . THR B  1 145 ? 61.663  8.505   -0.246  1.00 28.85  ? 131 THR B O   1 
ATOM   3348 C  CB  . THR B  1 145 ? 62.699  5.659   -0.342  1.00 32.14  ? 131 THR B CB  1 
ATOM   3349 O  OG1 . THR B  1 145 ? 62.056  5.084   -1.476  1.00 29.30  ? 131 THR B OG1 1 
ATOM   3350 C  CG2 . THR B  1 145 ? 63.527  4.598   0.364   1.00 28.82  ? 131 THR B CG2 1 
ATOM   3351 N  N   . ASN B  1 146 ? 59.680  7.440   -0.414  1.00 29.22  ? 132 ASN B N   1 
ATOM   3352 C  CA  . ASN B  1 146 ? 58.975  8.579   -0.989  1.00 33.46  ? 132 ASN B CA  1 
ATOM   3353 C  C   . ASN B  1 146 ? 58.073  9.231   0.059   1.00 30.71  ? 132 ASN B C   1 
ATOM   3354 O  O   . ASN B  1 146 ? 57.427  10.240  -0.218  1.00 30.41  ? 132 ASN B O   1 
ATOM   3355 C  CB  . ASN B  1 146 ? 58.132  8.188   -2.201  1.00 39.24  ? 132 ASN B CB  1 
ATOM   3356 C  CG  . ASN B  1 146 ? 58.934  8.079   -3.477  1.00 43.45  ? 132 ASN B CG  1 
ATOM   3357 O  OD1 . ASN B  1 146 ? 60.108  8.464   -3.514  1.00 47.91  ? 132 ASN B OD1 1 
ATOM   3358 N  ND2 . ASN B  1 146 ? 58.313  7.576   -4.534  1.00 44.44  ? 132 ASN B ND2 1 
ATOM   3359 N  N   . ALA B  1 147 ? 58.035  8.653   1.264   1.00 25.66  ? 133 ALA B N   1 
ATOM   3360 C  CA  . ALA B  1 147 ? 57.069  9.056   2.274   1.00 24.44  ? 133 ALA B CA  1 
ATOM   3361 C  C   . ALA B  1 147 ? 57.717  9.964   3.318   1.00 22.81  ? 133 ALA B C   1 
ATOM   3362 O  O   . ALA B  1 147 ? 58.932  9.943   3.508   1.00 24.33  ? 133 ALA B O   1 
ATOM   3363 C  CB  . ALA B  1 147 ? 56.464  7.824   2.918   1.00 24.54  ? 133 ALA B CB  1 
ATOM   3364 N  N   . THR B  1 148 ? 56.881  10.771  3.982   1.00 23.86  ? 134 THR B N   1 
ATOM   3365 C  CA  . THR B  1 148 ? 57.261  11.428  5.223   1.00 24.26  ? 134 THR B CA  1 
ATOM   3366 C  C   . THR B  1 148 ? 56.964  10.460  6.368   1.00 22.99  ? 134 THR B C   1 
ATOM   3367 O  O   . THR B  1 148 ? 55.831  10.001  6.510   1.00 22.72  ? 134 THR B O   1 
ATOM   3368 C  CB  . THR B  1 148 ? 56.511  12.754  5.376   1.00 25.28  ? 134 THR B CB  1 
ATOM   3369 O  OG1 . THR B  1 148 ? 56.976  13.607  4.334   1.00 28.59  ? 134 THR B OG1 1 
ATOM   3370 C  CG2 . THR B  1 148 ? 56.763  13.425  6.715   1.00 25.63  ? 134 THR B CG2 1 
ATOM   3371 N  N   . ILE B  1 149 ? 58.000  10.126  7.151   1.00 22.17  ? 135 ILE B N   1 
ATOM   3372 C  CA  . ILE B  1 149 ? 57.865  9.188   8.255   1.00 22.04  ? 135 ILE B CA  1 
ATOM   3373 C  C   . ILE B  1 149 ? 57.579  9.978   9.530   1.00 21.76  ? 135 ILE B C   1 
ATOM   3374 O  O   . ILE B  1 149 ? 58.427  10.732  10.000  1.00 21.27  ? 135 ILE B O   1 
ATOM   3375 C  CB  . ILE B  1 149 ? 59.119  8.304   8.410   1.00 24.13  ? 135 ILE B CB  1 
ATOM   3376 C  CG1 . ILE B  1 149 ? 59.579  7.705   7.077   1.00 25.82  ? 135 ILE B CG1 1 
ATOM   3377 C  CG2 . ILE B  1 149 ? 58.887  7.220   9.463   1.00 24.49  ? 135 ILE B CG2 1 
ATOM   3378 C  CD1 . ILE B  1 149 ? 58.580  6.750   6.448   1.00 25.70  ? 135 ILE B CD1 1 
ATOM   3379 N  N   . ILE B  1 150 ? 56.371  9.798   10.077  1.00 21.05  ? 136 ILE B N   1 
ATOM   3380 C  CA  . ILE B  1 150 ? 55.946  10.518  11.266  1.00 20.38  ? 136 ILE B CA  1 
ATOM   3381 C  C   . ILE B  1 150 ? 56.157  9.620   12.485  1.00 20.35  ? 136 ILE B C   1 
ATOM   3382 O  O   . ILE B  1 150 ? 55.642  8.504   12.543  1.00 20.10  ? 136 ILE B O   1 
ATOM   3383 C  CB  . ILE B  1 150 ? 54.486  10.989  11.128  1.00 21.02  ? 136 ILE B CB  1 
ATOM   3384 C  CG1 . ILE B  1 150 ? 54.291  11.853  9.878   1.00 22.94  ? 136 ILE B CG1 1 
ATOM   3385 C  CG2 . ILE B  1 150 ? 54.022  11.715  12.392  1.00 20.30  ? 136 ILE B CG2 1 
ATOM   3386 C  CD1 . ILE B  1 150 ? 52.840  12.135  9.537   1.00 24.42  ? 136 ILE B CD1 1 
ATOM   3387 N  N   . VAL B  1 151 ? 56.921  10.138  13.454  1.00 18.32  ? 137 VAL B N   1 
ATOM   3388 C  CA  . VAL B  1 151 ? 57.303  9.394   14.643  1.00 18.91  ? 137 VAL B CA  1 
ATOM   3389 C  C   . VAL B  1 151 ? 57.455  10.384  15.798  1.00 20.26  ? 137 VAL B C   1 
ATOM   3390 O  O   . VAL B  1 151 ? 57.785  11.549  15.585  1.00 20.31  ? 137 VAL B O   1 
ATOM   3391 C  CB  . VAL B  1 151 ? 58.602  8.598   14.397  1.00 18.84  ? 137 VAL B CB  1 
ATOM   3392 C  CG1 . VAL B  1 151 ? 59.786  9.514   14.105  1.00 20.63  ? 137 VAL B CG1 1 
ATOM   3393 C  CG2 . VAL B  1 151 ? 58.926  7.656   15.551  1.00 18.81  ? 137 VAL B CG2 1 
ATOM   3394 N  N   . HIS B  1 152 ? 57.182  9.914   17.020  1.00 20.62  ? 138 HIS B N   1 
ATOM   3395 C  CA  . HIS B  1 152 ? 57.358  10.728  18.213  1.00 20.92  ? 138 HIS B CA  1 
ATOM   3396 C  C   . HIS B  1 152 ? 58.853  10.962  18.421  1.00 20.85  ? 138 HIS B C   1 
ATOM   3397 O  O   . HIS B  1 152 ? 59.643  10.028  18.301  1.00 20.17  ? 138 HIS B O   1 
ATOM   3398 C  CB  . HIS B  1 152 ? 56.703  10.053  19.425  1.00 18.88  ? 138 HIS B CB  1 
ATOM   3399 C  CG  . HIS B  1 152 ? 56.499  10.969  20.586  1.00 20.44  ? 138 HIS B CG  1 
ATOM   3400 N  ND1 . HIS B  1 152 ? 57.543  11.510  21.306  1.00 18.23  ? 138 HIS B ND1 1 
ATOM   3401 C  CD2 . HIS B  1 152 ? 55.375  11.459  21.134  1.00 19.87  ? 138 HIS B CD2 1 
ATOM   3402 C  CE1 . HIS B  1 152 ? 57.056  12.288  22.262  1.00 21.42  ? 138 HIS B CE1 1 
ATOM   3403 N  NE2 . HIS B  1 152 ? 55.742  12.272  22.177  1.00 18.77  ? 138 HIS B NE2 1 
ATOM   3404 N  N   . GLU B  1 153 ? 59.235  12.209  18.731  1.00 20.39  ? 139 GLU B N   1 
ATOM   3405 C  CA  . GLU B  1 153 ? 60.642  12.580  18.787  1.00 21.52  ? 139 GLU B CA  1 
ATOM   3406 C  C   . GLU B  1 153 ? 61.346  11.802  19.900  1.00 19.04  ? 139 GLU B C   1 
ATOM   3407 O  O   . GLU B  1 153 ? 62.516  11.455  19.761  1.00 17.01  ? 139 GLU B O   1 
ATOM   3408 C  CB  . GLU B  1 153 ? 60.841  14.093  18.918  1.00 24.57  ? 139 GLU B CB  1 
ATOM   3409 C  CG  . GLU B  1 153 ? 60.586  14.653  20.314  1.00 25.68  ? 139 GLU B CG  1 
ATOM   3410 C  CD  . GLU B  1 153 ? 60.881  16.141  20.424  1.00 29.33  ? 139 GLU B CD  1 
ATOM   3411 O  OE1 . GLU B  1 153 ? 61.627  16.660  19.562  1.00 26.78  ? 139 GLU B OE1 1 
ATOM   3412 O  OE2 . GLU B  1 153 ? 60.344  16.784  21.355  1.00 25.92  ? 139 GLU B OE2 1 
ATOM   3413 N  N   . ASP B  1 154 ? 60.624  11.498  20.986  1.00 17.87  ? 140 ASP B N   1 
ATOM   3414 C  CA  . ASP B  1 154 ? 61.208  10.785  22.113  1.00 18.61  ? 140 ASP B CA  1 
ATOM   3415 C  C   . ASP B  1 154 ? 61.465  9.328   21.727  1.00 18.93  ? 140 ASP B C   1 
ATOM   3416 O  O   . ASP B  1 154 ? 62.448  8.735   22.169  1.00 19.02  ? 140 ASP B O   1 
ATOM   3417 C  CB  . ASP B  1 154 ? 60.369  10.927  23.376  1.00 19.13  ? 140 ASP B CB  1 
ATOM   3418 C  CG  . ASP B  1 154 ? 60.309  12.334  23.959  1.00 19.21  ? 140 ASP B CG  1 
ATOM   3419 O  OD1 . ASP B  1 154 ? 61.353  13.022  23.939  1.00 17.61  ? 140 ASP B OD1 1 
ATOM   3420 O  OD2 . ASP B  1 154 ? 59.227  12.724  24.449  1.00 17.18  ? 140 ASP B OD2 1 
ATOM   3421 N  N   . GLU B  1 155 ? 60.578  8.754   20.904  1.00 19.07  ? 141 GLU B N   1 
ATOM   3422 C  CA  . GLU B  1 155 ? 60.756  7.389   20.433  1.00 18.30  ? 141 GLU B CA  1 
ATOM   3423 C  C   . GLU B  1 155 ? 61.962  7.343   19.496  1.00 18.31  ? 141 GLU B C   1 
ATOM   3424 O  O   . GLU B  1 155 ? 62.799  6.449   19.594  1.00 17.30  ? 141 GLU B O   1 
ATOM   3425 C  CB  . GLU B  1 155 ? 59.504  6.873   19.724  1.00 20.44  ? 141 GLU B CB  1 
ATOM   3426 C  CG  . GLU B  1 155 ? 59.574  5.391   19.363  1.00 19.78  ? 141 GLU B CG  1 
ATOM   3427 C  CD  . GLU B  1 155 ? 59.448  4.432   20.536  1.00 21.43  ? 141 GLU B CD  1 
ATOM   3428 O  OE1 . GLU B  1 155 ? 59.270  4.915   21.675  1.00 21.35  ? 141 GLU B OE1 1 
ATOM   3429 O  OE2 . GLU B  1 155 ? 59.530  3.203   20.311  1.00 21.44  ? 141 GLU B OE2 1 
ATOM   3430 N  N   . PHE B  1 156 ? 62.030  8.328   18.592  1.00 19.02  ? 142 PHE B N   1 
ATOM   3431 C  CA  . PHE B  1 156 ? 63.111  8.450   17.625  1.00 20.33  ? 142 PHE B CA  1 
ATOM   3432 C  C   . PHE B  1 156 ? 64.446  8.547   18.365  1.00 20.12  ? 142 PHE B C   1 
ATOM   3433 O  O   . PHE B  1 156 ? 65.389  7.830   18.041  1.00 20.43  ? 142 PHE B O   1 
ATOM   3434 C  CB  . PHE B  1 156 ? 62.828  9.659   16.723  1.00 20.90  ? 142 PHE B CB  1 
ATOM   3435 C  CG  . PHE B  1 156 ? 63.671  9.762   15.458  1.00 20.71  ? 142 PHE B CG  1 
ATOM   3436 C  CD1 . PHE B  1 156 ? 63.966  8.634   14.700  1.00 23.88  ? 142 PHE B CD1 1 
ATOM   3437 C  CD2 . PHE B  1 156 ? 64.147  10.992  15.018  1.00 21.47  ? 142 PHE B CD2 1 
ATOM   3438 C  CE1 . PHE B  1 156 ? 64.729  8.735   13.546  1.00 23.48  ? 142 PHE B CE1 1 
ATOM   3439 C  CE2 . PHE B  1 156 ? 64.910  11.088  13.865  1.00 22.56  ? 142 PHE B CE2 1 
ATOM   3440 C  CZ  . PHE B  1 156 ? 65.197  9.960   13.130  1.00 23.79  ? 142 PHE B CZ  1 
ATOM   3441 N  N   . ASN B  1 157 ? 64.511  9.436   19.365  1.00 18.71  ? 143 ASN B N   1 
ATOM   3442 C  CA  . ASN B  1 157 ? 65.731  9.674   20.122  1.00 19.13  ? 143 ASN B CA  1 
ATOM   3443 C  C   . ASN B  1 157 ? 66.183  8.380   20.802  1.00 19.92  ? 143 ASN B C   1 
ATOM   3444 O  O   . ASN B  1 157 ? 67.359  8.022   20.743  1.00 20.38  ? 143 ASN B O   1 
ATOM   3445 C  CB  . ASN B  1 157 ? 65.551  10.812  21.125  1.00 19.92  ? 143 ASN B CB  1 
ATOM   3446 C  CG  . ASN B  1 157 ? 65.428  12.166  20.460  1.00 20.65  ? 143 ASN B CG  1 
ATOM   3447 O  OD1 . ASN B  1 157 ? 65.756  12.312  19.278  1.00 22.86  ? 143 ASN B OD1 1 
ATOM   3448 N  ND2 . ASN B  1 157 ? 64.978  13.168  21.202  1.00 19.60  ? 143 ASN B ND2 1 
ATOM   3449 N  N   . GLY B  1 158 ? 65.239  7.686   21.449  1.00 18.31  ? 144 GLY B N   1 
ATOM   3450 C  CA  . GLY B  1 158 ? 65.535  6.462   22.179  1.00 19.22  ? 144 GLY B CA  1 
ATOM   3451 C  C   . GLY B  1 158 ? 66.113  5.372   21.277  1.00 19.52  ? 144 GLY B C   1 
ATOM   3452 O  O   . GLY B  1 158 ? 67.089  4.717   21.638  1.00 19.86  ? 144 GLY B O   1 
ATOM   3453 N  N   . ALA B  1 159 ? 65.493  5.179   20.107  1.00 18.99  ? 145 ALA B N   1 
ATOM   3454 C  CA  . ALA B  1 159 ? 65.924  4.156   19.168  1.00 19.49  ? 145 ALA B CA  1 
ATOM   3455 C  C   . ALA B  1 159 ? 67.310  4.498   18.622  1.00 19.56  ? 145 ALA B C   1 
ATOM   3456 O  O   . ALA B  1 159 ? 68.146  3.615   18.451  1.00 21.92  ? 145 ALA B O   1 
ATOM   3457 C  CB  . ALA B  1 159 ? 64.903  4.016   18.057  1.00 20.88  ? 145 ALA B CB  1 
ATOM   3458 N  N   . LEU B  1 160 ? 67.540  5.789   18.353  1.00 20.35  ? 146 LEU B N   1 
ATOM   3459 C  CA  . LEU B  1 160 ? 68.816  6.262   17.836  1.00 20.21  ? 146 LEU B CA  1 
ATOM   3460 C  C   . LEU B  1 160 ? 69.924  6.015   18.861  1.00 21.71  ? 146 LEU B C   1 
ATOM   3461 O  O   . LEU B  1 160 ? 71.065  5.746   18.489  1.00 20.22  ? 146 LEU B O   1 
ATOM   3462 C  CB  . LEU B  1 160 ? 68.715  7.740   17.459  1.00 21.12  ? 146 LEU B CB  1 
ATOM   3463 C  CG  . LEU B  1 160 ? 67.915  8.057   16.191  1.00 21.68  ? 146 LEU B CG  1 
ATOM   3464 C  CD1 . LEU B  1 160 ? 68.022  9.527   15.819  1.00 22.97  ? 146 LEU B CD1 1 
ATOM   3465 C  CD2 . LEU B  1 160 ? 68.371  7.180   15.038  1.00 22.97  ? 146 LEU B CD2 1 
ATOM   3466 N  N   . GLN B  1 161 ? 69.585  6.110   20.152  1.00 22.97  ? 147 GLN B N   1 
ATOM   3467 C  CA  . GLN B  1 161 ? 70.559  5.872   21.208  1.00 23.66  ? 147 GLN B CA  1 
ATOM   3468 C  C   . GLN B  1 161 ? 70.930  4.389   21.248  1.00 25.19  ? 147 GLN B C   1 
ATOM   3469 O  O   . GLN B  1 161 ? 72.098  4.049   21.429  1.00 23.19  ? 147 GLN B O   1 
ATOM   3470 C  CB  . GLN B  1 161 ? 70.061  6.363   22.567  1.00 22.41  ? 147 GLN B CB  1 
ATOM   3471 C  CG  . GLN B  1 161 ? 70.257  7.859   22.793  1.00 21.28  ? 147 GLN B CG  1 
ATOM   3472 C  CD  . GLN B  1 161 ? 70.367  8.217   24.258  1.00 20.84  ? 147 GLN B CD  1 
ATOM   3473 O  OE1 . GLN B  1 161 ? 70.941  7.468   25.056  1.00 21.24  ? 147 GLN B OE1 1 
ATOM   3474 N  NE2 . GLN B  1 161 ? 69.804  9.358   24.630  1.00 20.00  ? 147 GLN B NE2 1 
ATOM   3475 N  N   . CYS B  1 162 ? 69.931  3.513   21.081  1.00 23.74  ? 148 CYS B N   1 
ATOM   3476 C  CA  . CYS B  1 162 ? 70.178  2.080   21.035  1.00 27.23  ? 148 CYS B CA  1 
ATOM   3477 C  C   . CYS B  1 162 ? 71.186  1.779   19.927  1.00 27.64  ? 148 CYS B C   1 
ATOM   3478 O  O   . CYS B  1 162 ? 72.102  0.982   20.113  1.00 26.11  ? 148 CYS B O   1 
ATOM   3479 C  CB  . CYS B  1 162 ? 68.895  1.286   20.805  1.00 26.78  ? 148 CYS B CB  1 
ATOM   3480 S  SG  . CYS B  1 162 ? 67.688  1.413   22.152  1.00 29.30  ? 148 CYS B SG  1 
ATOM   3481 N  N   . TYR B  1 163 ? 71.000  2.443   18.780  1.00 27.85  ? 149 TYR B N   1 
ATOM   3482 C  CA  . TYR B  1 163 ? 71.855  2.270   17.616  1.00 29.26  ? 149 TYR B CA  1 
ATOM   3483 C  C   . TYR B  1 163 ? 73.275  2.726   17.944  1.00 27.42  ? 149 TYR B C   1 
ATOM   3484 O  O   . TYR B  1 163 ? 74.235  1.994   17.707  1.00 27.50  ? 149 TYR B O   1 
ATOM   3485 C  CB  . TYR B  1 163 ? 71.286  3.058   16.429  1.00 30.58  ? 149 TYR B CB  1 
ATOM   3486 C  CG  . TYR B  1 163 ? 72.055  2.887   15.124  1.00 29.25  ? 149 TYR B CG  1 
ATOM   3487 C  CD1 . TYR B  1 163 ? 71.945  1.718   14.380  1.00 30.53  ? 149 TYR B CD1 1 
ATOM   3488 C  CD2 . TYR B  1 163 ? 72.882  3.892   14.632  1.00 29.86  ? 149 TYR B CD2 1 
ATOM   3489 C  CE1 . TYR B  1 163 ? 72.641  1.549   13.193  1.00 31.84  ? 149 TYR B CE1 1 
ATOM   3490 C  CE2 . TYR B  1 163 ? 73.582  3.735   13.445  1.00 34.12  ? 149 TYR B CE2 1 
ATOM   3491 C  CZ  . TYR B  1 163 ? 73.462  2.560   12.725  1.00 31.17  ? 149 TYR B CZ  1 
ATOM   3492 O  OH  . TYR B  1 163 ? 74.146  2.396   11.553  1.00 31.41  ? 149 TYR B OH  1 
ATOM   3493 N  N   . ALA B  1 164 ? 73.388  3.948   18.476  1.00 26.42  ? 150 ALA B N   1 
ATOM   3494 C  CA  . ALA B  1 164 ? 74.672  4.564   18.770  1.00 28.60  ? 150 ALA B CA  1 
ATOM   3495 C  C   . ALA B  1 164 ? 75.415  3.764   19.838  1.00 26.76  ? 150 ALA B C   1 
ATOM   3496 O  O   . ALA B  1 164 ? 76.643  3.737   19.846  1.00 26.70  ? 150 ALA B O   1 
ATOM   3497 C  CB  . ALA B  1 164 ? 74.464  5.999   19.207  1.00 28.18  ? 150 ALA B CB  1 
ATOM   3498 N  N   . ARG B  1 165 ? 74.654  3.121   20.733  1.00 26.83  ? 151 ARG B N   1 
ATOM   3499 C  CA  . ARG B  1 165 ? 75.218  2.354   21.834  1.00 27.79  ? 151 ARG B CA  1 
ATOM   3500 C  C   . ARG B  1 165 ? 75.459  0.908   21.399  1.00 28.08  ? 151 ARG B C   1 
ATOM   3501 O  O   . ARG B  1 165 ? 75.906  0.087   22.197  1.00 28.87  ? 151 ARG B O   1 
ATOM   3502 C  CB  . ARG B  1 165 ? 74.284  2.418   23.050  1.00 28.44  ? 151 ARG B CB  1 
ATOM   3503 C  CG  . ARG B  1 165 ? 74.152  3.804   23.666  1.00 27.45  ? 151 ARG B CG  1 
ATOM   3504 C  CD  . ARG B  1 165 ? 73.065  3.859   24.733  1.00 28.42  ? 151 ARG B CD  1 
ATOM   3505 N  NE  . ARG B  1 165 ? 72.854  5.211   25.262  1.00 27.32  ? 151 ARG B NE  1 
ATOM   3506 C  CZ  . ARG B  1 165 ? 73.314  5.636   26.431  1.00 27.38  ? 151 ARG B CZ  1 
ATOM   3507 N  NH1 . ARG B  1 165 ? 74.130  4.872   27.135  1.00 30.74  ? 151 ARG B NH1 1 
ATOM   3508 N  NH2 . ARG B  1 165 ? 72.980  6.832   26.882  1.00 30.97  ? 151 ARG B NH2 1 
ATOM   3509 N  N   . ASN B  1 166 ? 75.151  0.607   20.132  1.00 27.59  ? 152 ASN B N   1 
ATOM   3510 C  CA  . ASN B  1 166 ? 75.388  -0.709  19.553  1.00 31.25  ? 152 ASN B CA  1 
ATOM   3511 C  C   . ASN B  1 166 ? 74.705  -1.782  20.401  1.00 31.85  ? 152 ASN B C   1 
ATOM   3512 O  O   . ASN B  1 166 ? 75.305  -2.811  20.706  1.00 30.68  ? 152 ASN B O   1 
ATOM   3513 C  CB  . ASN B  1 166 ? 76.878  -0.985  19.354  1.00 32.69  ? 152 ASN B CB  1 
ATOM   3514 C  CG  . ASN B  1 166 ? 77.448  -0.248  18.163  1.00 34.81  ? 152 ASN B CG  1 
ATOM   3515 O  OD1 . ASN B  1 166 ? 77.082  -0.542  17.019  1.00 36.60  ? 152 ASN B OD1 1 
ATOM   3516 N  ND2 . ASN B  1 166 ? 78.340  0.703   18.405  1.00 33.68  ? 152 ASN B ND2 1 
ATOM   3517 N  N   . GLN B  1 167 ? 73.438  -1.536  20.761  1.00 32.42  ? 153 GLN B N   1 
ATOM   3518 C  CA  . GLN B  1 167 ? 72.611  -2.528  21.433  1.00 33.49  ? 153 GLN B CA  1 
ATOM   3519 C  C   . GLN B  1 167 ? 72.041  -3.475  20.380  1.00 32.21  ? 153 GLN B C   1 
ATOM   3520 O  O   . GLN B  1 167 ? 71.294  -3.050  19.504  1.00 29.97  ? 153 GLN B O   1 
ATOM   3521 C  CB  . GLN B  1 167 ? 71.509  -1.832  22.236  1.00 35.40  ? 153 GLN B CB  1 
ATOM   3522 C  CG  . GLN B  1 167 ? 72.023  -0.698  23.117  1.00 42.05  ? 153 GLN B CG  1 
ATOM   3523 C  CD  . GLN B  1 167 ? 70.974  -0.135  24.052  1.00 39.97  ? 153 GLN B CD  1 
ATOM   3524 O  OE1 . GLN B  1 167 ? 69.795  -0.501  24.000  1.00 47.14  ? 153 GLN B OE1 1 
ATOM   3525 N  NE2 . GLN B  1 167 ? 71.400  0.771   24.921  1.00 42.46  ? 153 GLN B NE2 1 
ATOM   3526 N  N   . LYS B  1 168 ? 72.412  -4.758  20.463  1.00 41.38  ? 154 LYS B N   1 
ATOM   3527 C  CA  . LYS B  1 168 ? 72.075  -5.723  19.427  1.00 45.52  ? 154 LYS B CA  1 
ATOM   3528 C  C   . LYS B  1 168 ? 70.968  -6.659  19.915  1.00 42.87  ? 154 LYS B C   1 
ATOM   3529 O  O   . LYS B  1 168 ? 70.621  -7.615  19.226  1.00 51.10  ? 154 LYS B O   1 
ATOM   3530 C  CB  . LYS B  1 168 ? 73.324  -6.507  19.000  1.00 47.48  ? 154 LYS B CB  1 
ATOM   3531 C  CG  . LYS B  1 168 ? 74.483  -5.669  18.458  1.00 51.03  ? 154 LYS B CG  1 
ATOM   3532 C  CD  . LYS B  1 168 ? 74.186  -4.948  17.147  1.00 51.57  ? 154 LYS B CD  1 
ATOM   3533 C  CE  . LYS B  1 168 ? 75.239  -3.949  16.749  1.00 54.82  ? 154 LYS B CE  1 
ATOM   3534 N  NZ  . LYS B  1 168 ? 76.387  -4.559  16.070  1.00 54.03  ? 154 LYS B NZ  1 
ATOM   3535 N  N   . GLU B  1 169 ? 70.414  -6.375  21.102  1.00 41.69  ? 155 GLU B N   1 
ATOM   3536 C  CA  . GLU B  1 169 ? 69.319  -7.161  21.654  1.00 50.78  ? 155 GLU B CA  1 
ATOM   3537 C  C   . GLU B  1 169 ? 68.221  -6.220  22.151  1.00 48.25  ? 155 GLU B C   1 
ATOM   3538 O  O   . GLU B  1 169 ? 68.425  -5.011  22.229  1.00 45.52  ? 155 GLU B O   1 
ATOM   3539 C  CB  . GLU B  1 169 ? 69.830  -8.088  22.760  1.00 59.28  ? 155 GLU B CB  1 
ATOM   3540 C  CG  . GLU B  1 169 ? 70.968  -9.001  22.307  1.00 60.39  ? 155 GLU B CG  1 
ATOM   3541 C  CD  . GLU B  1 169 ? 71.263  -10.168 23.234  1.00 62.54  ? 155 GLU B CD  1 
ATOM   3542 O  OE1 . GLU B  1 169 ? 70.603  -10.272 24.289  1.00 60.10  ? 155 GLU B OE1 1 
ATOM   3543 O  OE2 . GLU B  1 169 ? 72.150  -10.980 22.895  1.00 68.81  ? 155 GLU B OE2 1 
ATOM   3544 N  N   . GLY B  1 170 ? 67.052  -6.786  22.480  1.00 43.94  ? 156 GLY B N   1 
ATOM   3545 C  CA  . GLY B  1 170 ? 65.899  -5.996  22.888  1.00 38.82  ? 156 GLY B CA  1 
ATOM   3546 C  C   . GLY B  1 170 ? 64.930  -5.781  21.725  1.00 39.61  ? 156 GLY B C   1 
ATOM   3547 O  O   . GLY B  1 170 ? 65.070  -6.404  20.675  1.00 34.27  ? 156 GLY B O   1 
ATOM   3548 N  N   . ALA B  1 171 ? 63.963  -4.873  21.921  1.00 38.36  ? 157 ALA B N   1 
ATOM   3549 C  CA  . ALA B  1 171 ? 62.835  -4.729  21.013  1.00 32.90  ? 157 ALA B CA  1 
ATOM   3550 C  C   . ALA B  1 171 ? 63.132  -3.703  19.919  1.00 29.62  ? 157 ALA B C   1 
ATOM   3551 O  O   . ALA B  1 171 ? 62.295  -3.474  19.049  1.00 32.55  ? 157 ALA B O   1 
ATOM   3552 C  CB  . ALA B  1 171 ? 61.592  -4.356  21.798  1.00 33.62  ? 157 ALA B CB  1 
ATOM   3553 N  N   . TYR B  1 172 ? 64.323  -3.091  19.966  1.00 26.34  ? 158 TYR B N   1 
ATOM   3554 C  CA  . TYR B  1 172 ? 64.749  -2.143  18.945  1.00 25.82  ? 158 TYR B CA  1 
ATOM   3555 C  C   . TYR B  1 172 ? 65.851  -2.790  18.106  1.00 30.43  ? 158 TYR B C   1 
ATOM   3556 O  O   . TYR B  1 172 ? 66.927  -3.089  18.616  1.00 27.52  ? 158 TYR B O   1 
ATOM   3557 C  CB  . TYR B  1 172 ? 65.163  -0.826  19.612  1.00 26.64  ? 158 TYR B CB  1 
ATOM   3558 C  CG  . TYR B  1 172 ? 63.997  -0.099  20.271  1.00 27.72  ? 158 TYR B CG  1 
ATOM   3559 C  CD1 . TYR B  1 172 ? 63.108  0.663   19.519  1.00 26.59  ? 158 TYR B CD1 1 
ATOM   3560 C  CD2 . TYR B  1 172 ? 63.760  -0.203  21.637  1.00 27.94  ? 158 TYR B CD2 1 
ATOM   3561 C  CE1 . TYR B  1 172 ? 62.032  1.308   20.107  1.00 26.59  ? 158 TYR B CE1 1 
ATOM   3562 C  CE2 . TYR B  1 172 ? 62.689  0.440   22.238  1.00 27.28  ? 158 TYR B CE2 1 
ATOM   3563 C  CZ  . TYR B  1 172 ? 61.821  1.198   21.470  1.00 26.30  ? 158 TYR B CZ  1 
ATOM   3564 O  OH  . TYR B  1 172 ? 60.757  1.835   22.043  1.00 23.73  ? 158 TYR B OH  1 
ATOM   3565 N  N   . ILE B  1 173 ? 65.560  -2.996  16.813  1.00 28.46  ? 159 ILE B N   1 
ATOM   3566 C  CA  . ILE B  1 173 ? 66.385  -3.819  15.941  1.00 26.66  ? 159 ILE B CA  1 
ATOM   3567 C  C   . ILE B  1 173 ? 67.475  -2.958  15.297  1.00 26.42  ? 159 ILE B C   1 
ATOM   3568 O  O   . ILE B  1 173 ? 67.186  -2.093  14.471  1.00 26.58  ? 159 ILE B O   1 
ATOM   3569 C  CB  . ILE B  1 173 ? 65.508  -4.526  14.888  1.00 26.53  ? 159 ILE B CB  1 
ATOM   3570 C  CG1 . ILE B  1 173 ? 64.342  -5.295  15.531  1.00 25.28  ? 159 ILE B CG1 1 
ATOM   3571 C  CG2 . ILE B  1 173 ? 66.353  -5.429  13.987  1.00 28.01  ? 159 ILE B CG2 1 
ATOM   3572 C  CD1 . ILE B  1 173 ? 64.758  -6.241  16.643  1.00 25.28  ? 159 ILE B CD1 1 
ATOM   3573 N  N   . TRP B  1 174 ? 68.735  -3.226  15.667  1.00 27.41  ? 160 TRP B N   1 
ATOM   3574 C  CA  . TRP B  1 174 ? 69.876  -2.439  15.217  1.00 26.76  ? 160 TRP B CA  1 
ATOM   3575 C  C   . TRP B  1 174 ? 69.935  -2.407  13.691  1.00 30.40  ? 160 TRP B C   1 
ATOM   3576 O  O   . TRP B  1 174 ? 70.190  -1.359  13.098  1.00 27.00  ? 160 TRP B O   1 
ATOM   3577 C  CB  . TRP B  1 174 ? 71.184  -2.994  15.805  1.00 26.58  ? 160 TRP B CB  1 
ATOM   3578 C  CG  . TRP B  1 174 ? 72.358  -2.050  15.704  1.00 28.97  ? 160 TRP B CG  1 
ATOM   3579 C  CD1 . TRP B  1 174 ? 72.764  -1.156  16.652  1.00 29.47  ? 160 TRP B CD1 1 
ATOM   3580 C  CD2 . TRP B  1 174 ? 73.282  -1.901  14.599  1.00 28.38  ? 160 TRP B CD2 1 
ATOM   3581 N  NE1 . TRP B  1 174 ? 73.864  -0.463  16.219  1.00 30.67  ? 160 TRP B NE1 1 
ATOM   3582 C  CE2 . TRP B  1 174 ? 74.206  -0.896  14.965  1.00 29.22  ? 160 TRP B CE2 1 
ATOM   3583 C  CE3 . TRP B  1 174 ? 73.418  -2.510  13.347  1.00 32.47  ? 160 TRP B CE3 1 
ATOM   3584 C  CZ2 . TRP B  1 174 ? 75.245  -0.493  14.126  1.00 29.23  ? 160 TRP B CZ2 1 
ATOM   3585 C  CZ3 . TRP B  1 174 ? 74.445  -2.111  12.518  1.00 33.04  ? 160 TRP B CZ3 1 
ATOM   3586 C  CH2 . TRP B  1 174 ? 75.344  -1.115  12.903  1.00 34.52  ? 160 TRP B CH2 1 
ATOM   3587 N  N   . ALA B  1 175 ? 69.704  -3.568  13.066  1.00 32.42  ? 161 ALA B N   1 
ATOM   3588 C  CA  . ALA B  1 175 ? 69.833  -3.708  11.624  1.00 33.65  ? 161 ALA B CA  1 
ATOM   3589 C  C   . ALA B  1 175 ? 68.722  -2.935  10.914  1.00 28.35  ? 161 ALA B C   1 
ATOM   3590 O  O   . ALA B  1 175 ? 68.926  -2.421  9.816   1.00 28.43  ? 161 ALA B O   1 
ATOM   3591 C  CB  . ALA B  1 175 ? 69.831  -5.175  11.244  1.00 32.72  ? 161 ALA B CB  1 
ATOM   3592 N  N   . ASP B  1 176 ? 67.544  -2.856  11.547  1.00 25.90  ? 162 ASP B N   1 
ATOM   3593 C  CA  . ASP B  1 176 ? 66.427  -2.106  10.992  1.00 26.25  ? 162 ASP B CA  1 
ATOM   3594 C  C   . ASP B  1 176 ? 66.768  -0.617  10.978  1.00 24.16  ? 162 ASP B C   1 
ATOM   3595 O  O   . ASP B  1 176 ? 66.537  0.066   9.983   1.00 25.69  ? 162 ASP B O   1 
ATOM   3596 C  CB  . ASP B  1 176 ? 65.127  -2.388  11.735  1.00 26.56  ? 162 ASP B CB  1 
ATOM   3597 C  CG  . ASP B  1 176 ? 64.488  -3.739  11.442  1.00 27.90  ? 162 ASP B CG  1 
ATOM   3598 O  OD1 . ASP B  1 176 ? 65.047  -4.486  10.610  1.00 29.31  ? 162 ASP B OD1 1 
ATOM   3599 O  OD2 . ASP B  1 176 ? 63.429  -4.029  12.040  1.00 25.48  ? 162 ASP B OD2 1 
ATOM   3600 N  N   . ILE B  1 177 ? 67.322  -0.124  12.091  1.00 27.34  ? 163 ILE B N   1 
ATOM   3601 C  CA  . ILE B  1 177 ? 67.647  1.288   12.231  1.00 26.94  ? 163 ILE B CA  1 
ATOM   3602 C  C   . ILE B  1 177 ? 68.745  1.646   11.230  1.00 27.91  ? 163 ILE B C   1 
ATOM   3603 O  O   . ILE B  1 177 ? 68.703  2.707   10.608  1.00 27.00  ? 163 ILE B O   1 
ATOM   3604 C  CB  . ILE B  1 177 ? 68.062  1.617   13.678  1.00 27.43  ? 163 ILE B CB  1 
ATOM   3605 C  CG1 . ILE B  1 177 ? 66.978  1.213   14.683  1.00 26.87  ? 163 ILE B CG1 1 
ATOM   3606 C  CG2 . ILE B  1 177 ? 68.435  3.095   13.809  1.00 28.23  ? 163 ILE B CG2 1 
ATOM   3607 C  CD1 . ILE B  1 177 ? 67.477  1.061   16.108  1.00 28.02  ? 163 ILE B CD1 1 
ATOM   3608 N  N   . ASP B  1 178 ? 69.725  0.744   11.087  1.00 28.42  ? 164 ASP B N   1 
ATOM   3609 C  CA  . ASP B  1 178 ? 70.812  0.911   10.134  1.00 26.55  ? 164 ASP B CA  1 
ATOM   3610 C  C   . ASP B  1 178 ? 70.227  1.184   8.748   1.00 25.22  ? 164 ASP B C   1 
ATOM   3611 O  O   . ASP B  1 178 ? 70.668  2.096   8.053   1.00 25.01  ? 164 ASP B O   1 
ATOM   3612 C  CB  . ASP B  1 178 ? 71.733  -0.300  10.139  1.00 29.40  ? 164 ASP B CB  1 
ATOM   3613 C  CG  . ASP B  1 178 ? 73.067  -0.115  9.429   1.00 32.59  ? 164 ASP B CG  1 
ATOM   3614 O  OD1 . ASP B  1 178 ? 73.833  0.781   9.843   1.00 31.96  ? 164 ASP B OD1 1 
ATOM   3615 O  OD2 . ASP B  1 178 ? 73.328  -0.874  8.472   1.00 35.53  ? 164 ASP B OD2 1 
ATOM   3616 N  N   . ALA B  1 179 ? 69.216  0.393   8.368   1.00 27.86  ? 165 ALA B N   1 
ATOM   3617 C  CA  . ALA B  1 179 ? 68.609  0.481   7.048   1.00 26.91  ? 165 ALA B CA  1 
ATOM   3618 C  C   . ALA B  1 179 ? 67.842  1.794   6.889   1.00 28.02  ? 165 ALA B C   1 
ATOM   3619 O  O   . ALA B  1 179 ? 67.860  2.397   5.817   1.00 30.47  ? 165 ALA B O   1 
ATOM   3620 C  CB  . ALA B  1 179 ? 67.710  -0.715  6.812   1.00 28.36  ? 165 ALA B CB  1 
ATOM   3621 N  N   . TRP B  1 180 ? 67.155  2.231   7.953   1.00 29.20  ? 166 TRP B N   1 
ATOM   3622 C  CA  . TRP B  1 180 ? 66.393  3.469   7.902   1.00 27.55  ? 166 TRP B CA  1 
ATOM   3623 C  C   . TRP B  1 180 ? 67.312  4.625   7.501   1.00 29.62  ? 166 TRP B C   1 
ATOM   3624 O  O   . TRP B  1 180 ? 66.951  5.458   6.671   1.00 29.52  ? 166 TRP B O   1 
ATOM   3625 C  CB  . TRP B  1 180 ? 65.715  3.768   9.249   1.00 23.68  ? 166 TRP B CB  1 
ATOM   3626 C  CG  . TRP B  1 180 ? 64.853  2.666   9.813   1.00 24.58  ? 166 TRP B CG  1 
ATOM   3627 C  CD1 . TRP B  1 180 ? 64.322  1.588   9.164   1.00 26.09  ? 166 TRP B CD1 1 
ATOM   3628 C  CD2 . TRP B  1 180 ? 64.411  2.560   11.185  1.00 27.85  ? 166 TRP B CD2 1 
ATOM   3629 N  NE1 . TRP B  1 180 ? 63.596  0.816   10.035  1.00 27.16  ? 166 TRP B NE1 1 
ATOM   3630 C  CE2 . TRP B  1 180 ? 63.629  1.387   11.281  1.00 29.18  ? 166 TRP B CE2 1 
ATOM   3631 C  CE3 . TRP B  1 180 ? 64.601  3.337   12.334  1.00 27.60  ? 166 TRP B CE3 1 
ATOM   3632 C  CZ2 . TRP B  1 180 ? 63.043  0.980   12.479  1.00 29.38  ? 166 TRP B CZ2 1 
ATOM   3633 C  CZ3 . TRP B  1 180 ? 64.020  2.934   13.516  1.00 29.27  ? 166 TRP B CZ3 1 
ATOM   3634 C  CH2 . TRP B  1 180 ? 63.255  1.770   13.586  1.00 29.63  ? 166 TRP B CH2 1 
ATOM   3635 N  N   . ILE B  1 181 ? 68.503  4.667   8.110   1.00 27.38  ? 167 ILE B N   1 
ATOM   3636 C  CA  . ILE B  1 181 ? 69.444  5.759   7.909   1.00 30.49  ? 167 ILE B CA  1 
ATOM   3637 C  C   . ILE B  1 181 ? 70.066  5.648   6.519   1.00 32.42  ? 167 ILE B C   1 
ATOM   3638 O  O   . ILE B  1 181 ? 70.194  6.646   5.813   1.00 31.44  ? 167 ILE B O   1 
ATOM   3639 C  CB  . ILE B  1 181 ? 70.513  5.762   9.019   1.00 32.69  ? 167 ILE B CB  1 
ATOM   3640 C  CG1 . ILE B  1 181 ? 69.883  6.022   10.390  1.00 33.04  ? 167 ILE B CG1 1 
ATOM   3641 C  CG2 . ILE B  1 181 ? 71.632  6.760   8.708   1.00 32.14  ? 167 ILE B CG2 1 
ATOM   3642 C  CD1 . ILE B  1 181 ? 70.691  5.488   11.558  1.00 36.43  ? 167 ILE B CD1 1 
ATOM   3643 N  N   . LYS B  1 182 ? 70.439  4.422   6.133   1.00 35.39  ? 168 LYS B N   1 
ATOM   3644 C  CA  . LYS B  1 182 ? 71.095  4.183   4.857   1.00 34.62  ? 168 LYS B CA  1 
ATOM   3645 C  C   . LYS B  1 182 ? 70.154  4.549   3.707   1.00 32.96  ? 168 LYS B C   1 
ATOM   3646 O  O   . LYS B  1 182 ? 70.610  5.007   2.662   1.00 32.28  ? 168 LYS B O   1 
ATOM   3647 C  CB  . LYS B  1 182 ? 71.588  2.732   4.781   1.00 36.70  ? 168 LYS B CB  1 
ATOM   3648 C  CG  . LYS B  1 182 ? 72.895  2.456   5.523   1.00 39.98  ? 168 LYS B CG  1 
ATOM   3649 C  CD  . LYS B  1 182 ? 73.293  0.986   5.609   1.00 43.25  ? 168 LYS B CD  1 
ATOM   3650 C  CE  . LYS B  1 182 ? 74.760  0.800   5.873   1.00 47.78  ? 168 LYS B CE  1 
ATOM   3651 N  NZ  . LYS B  1 182 ? 75.058  -0.499  6.487   1.00 45.89  ? 168 LYS B NZ  1 
ATOM   3652 N  N   . ASN B  1 183 ? 68.842  4.367   3.915   1.00 30.21  ? 169 ASN B N   1 
ATOM   3653 C  CA  . ASN B  1 183 ? 67.855  4.588   2.867   1.00 30.72  ? 169 ASN B CA  1 
ATOM   3654 C  C   . ASN B  1 183 ? 67.375  6.041   2.873   1.00 26.65  ? 169 ASN B C   1 
ATOM   3655 O  O   . ASN B  1 183 ? 66.460  6.391   2.133   1.00 28.21  ? 169 ASN B O   1 
ATOM   3656 C  CB  . ASN B  1 183 ? 66.684  3.611   2.976   1.00 32.18  ? 169 ASN B CB  1 
ATOM   3657 C  CG  . ASN B  1 183 ? 67.049  2.216   2.520   1.00 36.51  ? 169 ASN B CG  1 
ATOM   3658 O  OD1 . ASN B  1 183 ? 67.480  2.030   1.378   1.00 44.30  ? 169 ASN B OD1 1 
ATOM   3659 N  ND2 . ASN B  1 183 ? 66.883  1.228   3.387   1.00 42.74  ? 169 ASN B ND2 1 
ATOM   3660 N  N   . ASN B  1 184 ? 67.995  6.881   3.711   1.00 26.42  ? 170 ASN B N   1 
ATOM   3661 C  CA  . ASN B  1 184 ? 67.747  8.318   3.718   1.00 28.03  ? 170 ASN B CA  1 
ATOM   3662 C  C   . ASN B  1 184 ? 66.249  8.617   3.812   1.00 25.78  ? 170 ASN B C   1 
ATOM   3663 O  O   . ASN B  1 184 ? 65.720  9.375   3.002   1.00 25.49  ? 170 ASN B O   1 
ATOM   3664 C  CB  . ASN B  1 184 ? 68.331  9.001   2.481   1.00 31.62  ? 170 ASN B CB  1 
ATOM   3665 C  CG  . ASN B  1 184 ? 68.288  10.511  2.566   1.00 39.74  ? 170 ASN B CG  1 
ATOM   3666 O  OD1 . ASN B  1 184 ? 68.151  11.072  3.659   1.00 46.33  ? 170 ASN B OD1 1 
ATOM   3667 N  ND2 . ASN B  1 184 ? 68.423  11.187  1.434   1.00 43.51  ? 170 ASN B ND2 1 
ATOM   3668 N  N   . LEU B  1 185 ? 65.572  8.050   4.818   1.00 24.51  ? 171 LEU B N   1 
ATOM   3669 C  CA  . LEU B  1 185 ? 64.149  8.291   5.022   1.00 25.39  ? 171 LEU B CA  1 
ATOM   3670 C  C   . LEU B  1 185 ? 63.920  9.755   5.402   1.00 25.42  ? 171 LEU B C   1 
ATOM   3671 O  O   . LEU B  1 185 ? 64.798  10.390  5.983   1.00 24.68  ? 171 LEU B O   1 
ATOM   3672 C  CB  . LEU B  1 185 ? 63.612  7.344   6.097   1.00 25.20  ? 171 LEU B CB  1 
ATOM   3673 C  CG  . LEU B  1 185 ? 63.620  5.852   5.748   1.00 27.79  ? 171 LEU B CG  1 
ATOM   3674 C  CD1 . LEU B  1 185 ? 62.858  5.037   6.783   1.00 26.81  ? 171 LEU B CD1 1 
ATOM   3675 C  CD2 . LEU B  1 185 ? 63.047  5.624   4.358   1.00 29.36  ? 171 LEU B CD2 1 
ATOM   3676 N  N   A GLN B  1 186 ? 62.738  10.281  5.053   0.60 26.88  ? 172 GLN B N   1 
ATOM   3677 N  N   B GLN B  1 186 ? 62.729  10.273  5.073   0.40 25.91  ? 172 GLN B N   1 
ATOM   3678 C  CA  A GLN B  1 186 ? 62.348  11.631  5.434   0.60 27.86  ? 172 GLN B CA  1 
ATOM   3679 C  CA  B GLN B  1 186 ? 62.345  11.629  5.433   0.40 26.28  ? 172 GLN B CA  1 
ATOM   3680 C  C   A GLN B  1 186 ? 61.543  11.572  6.730   0.60 27.32  ? 172 GLN B C   1 
ATOM   3681 C  C   B GLN B  1 186 ? 61.530  11.596  6.724   0.40 26.32  ? 172 GLN B C   1 
ATOM   3682 O  O   A GLN B  1 186 ? 60.435  11.040  6.754   0.60 29.86  ? 172 GLN B O   1 
ATOM   3683 O  O   B GLN B  1 186 ? 60.404  11.101  6.740   0.40 27.70  ? 172 GLN B O   1 
ATOM   3684 C  CB  A GLN B  1 186 ? 61.509  12.326  4.361   0.60 27.75  ? 172 GLN B CB  1 
ATOM   3685 C  CB  B GLN B  1 186 ? 61.556  12.291  4.301   0.40 25.43  ? 172 GLN B CB  1 
ATOM   3686 C  CG  A GLN B  1 186 ? 61.226  13.793  4.668   0.60 29.78  ? 172 GLN B CG  1 
ATOM   3687 C  CG  B GLN B  1 186 ? 62.327  12.380  2.988   0.40 26.69  ? 172 GLN B CG  1 
ATOM   3688 C  CD  A GLN B  1 186 ? 60.018  14.344  3.941   0.60 33.89  ? 172 GLN B CD  1 
ATOM   3689 C  CD  B GLN B  1 186 ? 63.722  12.940  3.163   0.40 26.44  ? 172 GLN B CD  1 
ATOM   3690 O  OE1 A GLN B  1 186 ? 59.850  14.155  2.732   0.60 34.34  ? 172 GLN B OE1 1 
ATOM   3691 O  OE1 B GLN B  1 186 ? 63.909  14.075  3.616   0.40 28.86  ? 172 GLN B OE1 1 
ATOM   3692 N  NE2 A GLN B  1 186 ? 59.157  15.031  4.678   0.60 38.29  ? 172 GLN B NE2 1 
ATOM   3693 N  NE2 B GLN B  1 186 ? 64.721  12.143  2.812   0.40 23.22  ? 172 GLN B NE2 1 
ATOM   3694 N  N   . TRP B  1 187 ? 62.112  12.144  7.797   1.00 26.59  ? 173 TRP B N   1 
ATOM   3695 C  CA  . TRP B  1 187 ? 61.514  12.085  9.121   1.00 25.39  ? 173 TRP B CA  1 
ATOM   3696 C  C   . TRP B  1 187 ? 60.762  13.375  9.443   1.00 23.79  ? 173 TRP B C   1 
ATOM   3697 O  O   . TRP B  1 187 ? 61.218  14.468  9.116   1.00 21.37  ? 173 TRP B O   1 
ATOM   3698 C  CB  . TRP B  1 187 ? 62.598  11.821  10.177  1.00 23.94  ? 173 TRP B CB  1 
ATOM   3699 C  CG  . TRP B  1 187 ? 63.360  10.535  9.983   1.00 23.25  ? 173 TRP B CG  1 
ATOM   3700 C  CD1 . TRP B  1 187 ? 64.563  10.388  9.357   1.00 23.50  ? 173 TRP B CD1 1 
ATOM   3701 C  CD2 . TRP B  1 187 ? 62.977  9.215   10.431  1.00 22.40  ? 173 TRP B CD2 1 
ATOM   3702 N  NE1 . TRP B  1 187 ? 64.953  9.076   9.376   1.00 23.15  ? 173 TRP B NE1 1 
ATOM   3703 C  CE2 . TRP B  1 187 ? 64.003  8.332   10.027  1.00 23.43  ? 173 TRP B CE2 1 
ATOM   3704 C  CE3 . TRP B  1 187 ? 61.878  8.695   11.125  1.00 25.57  ? 173 TRP B CE3 1 
ATOM   3705 C  CZ2 . TRP B  1 187 ? 63.958  6.966   10.297  1.00 24.76  ? 173 TRP B CZ2 1 
ATOM   3706 C  CZ3 . TRP B  1 187 ? 61.837  7.344   11.393  1.00 24.57  ? 173 TRP B CZ3 1 
ATOM   3707 C  CH2 . TRP B  1 187 ? 62.864  6.494   10.985  1.00 24.63  ? 173 TRP B CH2 1 
ATOM   3708 N  N   . ARG B  1 188 ? 59.604  13.215  10.095  1.00 24.24  ? 174 ARG B N   1 
ATOM   3709 C  CA  . ARG B  1 188 ? 58.878  14.312  10.714  1.00 23.73  ? 174 ARG B CA  1 
ATOM   3710 C  C   . ARG B  1 188 ? 58.573  13.900  12.152  1.00 23.33  ? 174 ARG B C   1 
ATOM   3711 O  O   . ARG B  1 188 ? 57.716  13.048  12.382  1.00 23.02  ? 174 ARG B O   1 
ATOM   3712 C  CB  . ARG B  1 188 ? 57.603  14.637  9.922   1.00 26.53  ? 174 ARG B CB  1 
ATOM   3713 C  CG  . ARG B  1 188 ? 56.959  15.984  10.229  1.00 30.46  ? 174 ARG B CG  1 
ATOM   3714 C  CD  . ARG B  1 188 ? 55.983  15.922  11.391  1.00 32.40  ? 174 ARG B CD  1 
ATOM   3715 N  NE  . ARG B  1 188 ? 55.152  17.123  11.531  1.00 34.58  ? 174 ARG B NE  1 
ATOM   3716 C  CZ  . ARG B  1 188 ? 54.864  17.709  12.688  1.00 35.72  ? 174 ARG B CZ  1 
ATOM   3717 N  NH1 . ARG B  1 188 ? 55.430  17.285  13.804  1.00 34.01  ? 174 ARG B NH1 1 
ATOM   3718 N  NH2 . ARG B  1 188 ? 54.015  18.720  12.724  1.00 35.36  ? 174 ARG B NH2 1 
ATOM   3719 N  N   . THR B  1 189 ? 59.309  14.477  13.111  1.00 21.02  ? 175 THR B N   1 
ATOM   3720 C  CA  . THR B  1 189 ? 59.159  14.098  14.508  1.00 20.90  ? 175 THR B CA  1 
ATOM   3721 C  C   . THR B  1 189 ? 57.998  14.878  15.122  1.00 19.75  ? 175 THR B C   1 
ATOM   3722 O  O   . THR B  1 189 ? 57.855  16.079  14.899  1.00 21.60  ? 175 THR B O   1 
ATOM   3723 C  CB  . THR B  1 189 ? 60.453  14.320  15.297  1.00 21.27  ? 175 THR B CB  1 
ATOM   3724 O  OG1 . THR B  1 189 ? 60.838  15.677  15.103  1.00 23.83  ? 175 THR B OG1 1 
ATOM   3725 C  CG2 . THR B  1 189 ? 61.578  13.393  14.867  1.00 22.36  ? 175 THR B CG2 1 
ATOM   3726 N  N   . VAL B  1 190 ? 57.169  14.164  15.890  1.00 18.61  ? 176 VAL B N   1 
ATOM   3727 C  CA  . VAL B  1 190 ? 56.134  14.781  16.704  1.00 18.57  ? 176 VAL B CA  1 
ATOM   3728 C  C   . VAL B  1 190 ? 56.778  15.205  18.023  1.00 18.87  ? 176 VAL B C   1 
ATOM   3729 O  O   . VAL B  1 190 ? 57.284  14.370  18.768  1.00 21.25  ? 176 VAL B O   1 
ATOM   3730 C  CB  . VAL B  1 190 ? 54.946  13.823  16.932  1.00 17.72  ? 176 VAL B CB  1 
ATOM   3731 C  CG1 . VAL B  1 190 ? 53.816  14.491  17.710  1.00 17.33  ? 176 VAL B CG1 1 
ATOM   3732 C  CG2 . VAL B  1 190 ? 54.423  13.247  15.620  1.00 18.73  ? 176 VAL B CG2 1 
ATOM   3733 N  N   . LYS B  1 191 ? 56.768  16.515  18.292  1.00 20.32  ? 177 LYS B N   1 
ATOM   3734 C  CA  . LYS B  1 191 ? 57.441  17.063  19.459  1.00 21.93  ? 177 LYS B CA  1 
ATOM   3735 C  C   . LYS B  1 191 ? 56.689  16.632  20.718  1.00 22.79  ? 177 LYS B C   1 
ATOM   3736 O  O   . LYS B  1 191 ? 55.500  16.320  20.666  1.00 20.54  ? 177 LYS B O   1 
ATOM   3737 C  CB  . LYS B  1 191 ? 57.565  18.586  19.318  1.00 24.56  ? 177 LYS B CB  1 
ATOM   3738 C  CG  . LYS B  1 191 ? 58.144  19.066  17.985  1.00 29.42  ? 177 LYS B CG  1 
ATOM   3739 C  CD  . LYS B  1 191 ? 59.478  18.422  17.619  1.00 28.40  ? 177 LYS B CD  1 
ATOM   3740 C  CE  . LYS B  1 191 ? 60.091  18.947  16.350  1.00 27.33  ? 177 LYS B CE  1 
ATOM   3741 N  NZ  . LYS B  1 191 ? 59.542  18.324  15.142  1.00 26.07  ? 177 LYS B NZ  1 
ATOM   3742 N  N   . ARG B  1 192 ? 57.401  16.620  21.852  1.00 23.13  ? 178 ARG B N   1 
ATOM   3743 C  CA  . ARG B  1 192 ? 56.868  16.081  23.092  1.00 24.44  ? 178 ARG B CA  1 
ATOM   3744 C  C   . ARG B  1 192 ? 55.559  16.777  23.469  1.00 25.88  ? 178 ARG B C   1 
ATOM   3745 O  O   . ARG B  1 192 ? 54.627  16.127  23.938  1.00 27.07  ? 178 ARG B O   1 
ATOM   3746 C  CB  . ARG B  1 192 ? 57.893  16.199  24.227  1.00 23.28  ? 178 ARG B CB  1 
ATOM   3747 C  CG  . ARG B  1 192 ? 57.397  15.651  25.558  1.00 22.95  ? 178 ARG B CG  1 
ATOM   3748 C  CD  . ARG B  1 192 ? 58.455  15.742  26.646  1.00 22.69  ? 178 ARG B CD  1 
ATOM   3749 N  NE  . ARG B  1 192 ? 59.607  14.876  26.368  1.00 21.31  ? 178 ARG B NE  1 
ATOM   3750 C  CZ  . ARG B  1 192 ? 60.716  14.845  27.094  1.00 21.68  ? 178 ARG B CZ  1 
ATOM   3751 N  NH1 . ARG B  1 192 ? 60.842  15.641  28.141  1.00 22.38  ? 178 ARG B NH1 1 
ATOM   3752 N  NH2 . ARG B  1 192 ? 61.700  14.027  26.768  1.00 23.17  ? 178 ARG B NH2 1 
ATOM   3753 N  N   . HIS B  1 193 ? 55.488  18.097  23.273  1.00 27.26  ? 179 HIS B N   1 
ATOM   3754 C  CA  . HIS B  1 193 ? 54.323  18.848  23.718  1.00 34.50  ? 179 HIS B CA  1 
ATOM   3755 C  C   . HIS B  1 193 ? 53.483  19.299  22.523  1.00 32.47  ? 179 HIS B C   1 
ATOM   3756 O  O   . HIS B  1 193 ? 52.701  20.242  22.632  1.00 34.11  ? 179 HIS B O   1 
ATOM   3757 C  CB  . HIS B  1 193 ? 54.747  19.995  24.644  1.00 33.61  ? 179 HIS B CB  1 
ATOM   3758 C  CG  . HIS B  1 193 ? 55.402  19.511  25.898  1.00 38.74  ? 179 HIS B CG  1 
ATOM   3759 N  ND1 . HIS B  1 193 ? 54.746  18.689  26.790  1.00 44.56  ? 179 HIS B ND1 1 
ATOM   3760 C  CD2 . HIS B  1 193 ? 56.640  19.674  26.386  1.00 39.30  ? 179 HIS B CD2 1 
ATOM   3761 C  CE1 . HIS B  1 193 ? 55.559  18.393  27.793  1.00 38.88  ? 179 HIS B CE1 1 
ATOM   3762 N  NE2 . HIS B  1 193 ? 56.713  18.984  27.570  1.00 40.79  ? 179 HIS B NE2 1 
ATOM   3763 N  N   . GLU B  1 194 ? 53.617  18.594  21.395  1.00 27.34  ? 180 GLU B N   1 
ATOM   3764 C  CA  . GLU B  1 194 ? 52.934  18.982  20.171  1.00 25.35  ? 180 GLU B CA  1 
ATOM   3765 C  C   . GLU B  1 194 ? 51.490  18.477  20.186  1.00 24.22  ? 180 GLU B C   1 
ATOM   3766 O  O   . GLU B  1 194 ? 51.222  17.360  20.622  1.00 23.17  ? 180 GLU B O   1 
ATOM   3767 C  CB  . GLU B  1 194 ? 53.678  18.460  18.942  1.00 24.51  ? 180 GLU B CB  1 
ATOM   3768 C  CG  . GLU B  1 194 ? 53.193  19.096  17.644  1.00 24.52  ? 180 GLU B CG  1 
ATOM   3769 C  CD  . GLU B  1 194 ? 53.925  18.653  16.393  1.00 22.13  ? 180 GLU B CD  1 
ATOM   3770 O  OE1 . GLU B  1 194 ? 54.974  17.987  16.512  1.00 28.55  ? 180 GLU B OE1 1 
ATOM   3771 O  OE2 . GLU B  1 194 ? 53.425  18.969  15.293  1.00 23.36  ? 180 GLU B OE2 1 
ATOM   3772 N  N   . ASP B  1 195 ? 50.570  19.322  19.700  1.00 23.56  ? 181 ASP B N   1 
ATOM   3773 C  CA  . ASP B  1 195 ? 49.163  18.970  19.584  1.00 26.79  ? 181 ASP B CA  1 
ATOM   3774 C  C   . ASP B  1 195 ? 48.994  17.942  18.469  1.00 24.59  ? 181 ASP B C   1 
ATOM   3775 O  O   . ASP B  1 195 ? 49.908  17.722  17.677  1.00 25.12  ? 181 ASP B O   1 
ATOM   3776 C  CB  . ASP B  1 195 ? 48.292  20.192  19.323  1.00 27.99  ? 181 ASP B CB  1 
ATOM   3777 C  CG  . ASP B  1 195 ? 48.064  21.107  20.518  1.00 30.37  ? 181 ASP B CG  1 
ATOM   3778 O  OD1 . ASP B  1 195 ? 48.591  20.795  21.607  1.00 33.55  ? 181 ASP B OD1 1 
ATOM   3779 O  OD2 . ASP B  1 195 ? 47.357  22.121  20.348  1.00 31.04  ? 181 ASP B OD2 1 
ATOM   3780 N  N   . ASN B  1 196 ? 47.809  17.325  18.422  1.00 24.99  ? 182 ASN B N   1 
ATOM   3781 C  CA  . ASN B  1 196 ? 47.469  16.359  17.390  1.00 29.63  ? 182 ASN B CA  1 
ATOM   3782 C  C   . ASN B  1 196 ? 47.708  16.996  16.021  1.00 30.65  ? 182 ASN B C   1 
ATOM   3783 O  O   . ASN B  1 196 ? 47.675  18.218  15.884  1.00 27.71  ? 182 ASN B O   1 
ATOM   3784 C  CB  . ASN B  1 196 ? 46.043  15.845  17.580  1.00 32.52  ? 182 ASN B CB  1 
ATOM   3785 C  CG  . ASN B  1 196 ? 45.832  15.228  18.944  1.00 34.05  ? 182 ASN B CG  1 
ATOM   3786 O  OD1 . ASN B  1 196 ? 46.800  14.856  19.619  1.00 36.90  ? 182 ASN B OD1 1 
ATOM   3787 N  ND2 . ASN B  1 196 ? 44.580  15.098  19.361  1.00 39.37  ? 182 ASN B ND2 1 
ATOM   3788 N  N   . ILE B  1 197 ? 47.963  16.155  15.011  1.00 26.25  ? 183 ILE B N   1 
ATOM   3789 C  CA  . ILE B  1 197 ? 48.260  16.630  13.668  1.00 27.50  ? 183 ILE B CA  1 
ATOM   3790 C  C   . ILE B  1 197 ? 47.143  16.188  12.726  1.00 27.13  ? 183 ILE B C   1 
ATOM   3791 O  O   . ILE B  1 197 ? 46.887  14.993  12.588  1.00 28.12  ? 183 ILE B O   1 
ATOM   3792 C  CB  . ILE B  1 197 ? 49.634  16.115  13.190  1.00 28.28  ? 183 ILE B CB  1 
ATOM   3793 C  CG1 . ILE B  1 197 ? 50.756  16.458  14.176  1.00 27.35  ? 183 ILE B CG1 1 
ATOM   3794 C  CG2 . ILE B  1 197 ? 49.946  16.628  11.783  1.00 32.22  ? 183 ILE B CG2 1 
ATOM   3795 C  CD1 . ILE B  1 197 ? 52.061  15.728  13.910  1.00 29.91  ? 183 ILE B CD1 1 
ATOM   3796 N  N   . LEU B  1 198 ? 46.488  17.162  12.082  1.00 28.09  ? 184 LEU B N   1 
ATOM   3797 C  CA  . LEU B  1 198 ? 45.531  16.873  11.026  1.00 30.23  ? 184 LEU B CA  1 
ATOM   3798 C  C   . LEU B  1 198 ? 46.313  16.514  9.765   1.00 28.20  ? 184 LEU B C   1 
ATOM   3799 O  O   . LEU B  1 198 ? 46.809  17.392  9.062   1.00 30.51  ? 184 LEU B O   1 
ATOM   3800 C  CB  . LEU B  1 198 ? 44.593  18.058  10.793  1.00 30.21  ? 184 LEU B CB  1 
ATOM   3801 C  CG  . LEU B  1 198 ? 43.427  17.805  9.830   1.00 34.68  ? 184 LEU B CG  1 
ATOM   3802 C  CD1 . LEU B  1 198 ? 42.631  16.583  10.263  1.00 33.14  ? 184 LEU B CD1 1 
ATOM   3803 C  CD2 . LEU B  1 198 ? 42.513  19.018  9.722   1.00 35.66  ? 184 LEU B CD2 1 
ATOM   3804 N  N   . LEU B  1 199 ? 46.428  15.209  9.503   1.00 28.03  ? 185 LEU B N   1 
ATOM   3805 C  CA  . LEU B  1 199 ? 47.260  14.711  8.421   1.00 31.62  ? 185 LEU B CA  1 
ATOM   3806 C  C   . LEU B  1 199 ? 46.489  14.799  7.105   1.00 29.20  ? 185 LEU B C   1 
ATOM   3807 O  O   . LEU B  1 199 ? 47.074  15.039  6.052   1.00 29.72  ? 185 LEU B O   1 
ATOM   3808 C  CB  . LEU B  1 199 ? 47.686  13.279  8.745   1.00 31.25  ? 185 LEU B CB  1 
ATOM   3809 C  CG  . LEU B  1 199 ? 48.885  12.742  7.958   1.00 33.86  ? 185 LEU B CG  1 
ATOM   3810 C  CD1 . LEU B  1 199 ? 50.080  13.679  8.086   1.00 35.47  ? 185 LEU B CD1 1 
ATOM   3811 C  CD2 . LEU B  1 199 ? 49.248  11.338  8.416   1.00 31.04  ? 185 LEU B CD2 1 
ATOM   3812 N  N   . ALA B  1 200 ? 45.169  14.600  7.189   1.00 27.99  ? 186 ALA B N   1 
ATOM   3813 C  CA  . ALA B  1 200 ? 44.279  14.686  6.042   1.00 29.32  ? 186 ALA B CA  1 
ATOM   3814 C  C   . ALA B  1 200 ? 42.845  14.828  6.547   1.00 29.28  ? 186 ALA B C   1 
ATOM   3815 O  O   . ALA B  1 200 ? 42.594  14.650  7.735   1.00 28.22  ? 186 ALA B O   1 
ATOM   3816 C  CB  . ALA B  1 200 ? 44.447  13.463  5.161   1.00 31.44  ? 186 ALA B CB  1 
ATOM   3817 N  N   . GLU B  1 201 ? 41.910  15.157  5.647   1.00 30.66  ? 187 GLU B N   1 
ATOM   3818 C  CA  . GLU B  1 201 ? 40.511  15.276  6.029   1.00 30.39  ? 187 GLU B CA  1 
ATOM   3819 C  C   . GLU B  1 201 ? 40.093  13.994  6.749   1.00 31.64  ? 187 GLU B C   1 
ATOM   3820 O  O   . GLU B  1 201 ? 40.078  12.919  6.153   1.00 28.24  ? 187 GLU B O   1 
ATOM   3821 C  CB  . GLU B  1 201 ? 39.622  15.557  4.814   1.00 30.65  ? 187 GLU B CB  1 
ATOM   3822 C  CG  . GLU B  1 201 ? 38.140  15.684  5.158   1.00 35.46  ? 187 GLU B CG  1 
ATOM   3823 C  CD  . GLU B  1 201 ? 37.229  15.935  3.967   1.00 37.07  ? 187 GLU B CD  1 
ATOM   3824 O  OE1 . GLU B  1 201 ? 37.754  16.134  2.852   1.00 44.20  ? 187 GLU B OE1 1 
ATOM   3825 O  OE2 . GLU B  1 201 ? 35.995  15.923  4.157   1.00 42.05  ? 187 GLU B OE2 1 
ATOM   3826 N  N   . GLY B  1 202 ? 39.785  14.121  8.046   1.00 28.02  ? 188 GLY B N   1 
ATOM   3827 C  CA  . GLY B  1 202 ? 39.277  13.015  8.843   1.00 30.57  ? 188 GLY B CA  1 
ATOM   3828 C  C   . GLY B  1 202 ? 40.384  12.113  9.394   1.00 27.87  ? 188 GLY B C   1 
ATOM   3829 O  O   . GLY B  1 202 ? 40.089  11.060  9.954   1.00 28.98  ? 188 GLY B O   1 
ATOM   3830 N  N   . VAL B  1 203 ? 41.652  12.524  9.239   1.00 26.21  ? 189 VAL B N   1 
ATOM   3831 C  CA  . VAL B  1 203 ? 42.777  11.724  9.707   1.00 25.95  ? 189 VAL B CA  1 
ATOM   3832 C  C   . VAL B  1 203 ? 43.667  12.574  10.614  1.00 26.13  ? 189 VAL B C   1 
ATOM   3833 O  O   . VAL B  1 203 ? 44.294  13.532  10.161  1.00 24.22  ? 189 VAL B O   1 
ATOM   3834 C  CB  . VAL B  1 203 ? 43.600  11.131  8.545   1.00 24.96  ? 189 VAL B CB  1 
ATOM   3835 C  CG1 . VAL B  1 203 ? 44.689  10.190  9.049   1.00 23.91  ? 189 VAL B CG1 1 
ATOM   3836 C  CG2 . VAL B  1 203 ? 42.714  10.423  7.526   1.00 26.00  ? 189 VAL B CG2 1 
ATOM   3837 N  N   . LYS B  1 204 ? 43.742  12.183  11.892  1.00 25.27  ? 190 LYS B N   1 
ATOM   3838 C  CA  . LYS B  1 204 ? 44.499  12.925  12.887  1.00 26.70  ? 190 LYS B CA  1 
ATOM   3839 C  C   . LYS B  1 204 ? 45.501  12.004  13.581  1.00 23.87  ? 190 LYS B C   1 
ATOM   3840 O  O   . LYS B  1 204 ? 45.141  10.924  14.043  1.00 21.78  ? 190 LYS B O   1 
ATOM   3841 C  CB  . LYS B  1 204 ? 43.538  13.538  13.913  1.00 30.65  ? 190 LYS B CB  1 
ATOM   3842 C  CG  . LYS B  1 204 ? 42.621  14.636  13.384  1.00 37.35  ? 190 LYS B CG  1 
ATOM   3843 C  CD  . LYS B  1 204 ? 41.350  14.806  14.212  1.00 42.42  ? 190 LYS B CD  1 
ATOM   3844 C  CE  . LYS B  1 204 ? 40.620  16.086  13.940  1.00 43.76  ? 190 LYS B CE  1 
ATOM   3845 N  NZ  . LYS B  1 204 ? 39.871  16.531  15.121  1.00 49.22  ? 190 LYS B NZ  1 
ATOM   3846 N  N   . VAL B  1 205 ? 46.762  12.454  13.651  1.00 24.67  ? 191 VAL B N   1 
ATOM   3847 C  CA  . VAL B  1 205 ? 47.785  11.791  14.445  1.00 24.30  ? 191 VAL B CA  1 
ATOM   3848 C  C   . VAL B  1 205 ? 47.622  12.237  15.896  1.00 21.98  ? 191 VAL B C   1 
ATOM   3849 O  O   . VAL B  1 205 ? 47.667  13.431  16.183  1.00 25.44  ? 191 VAL B O   1 
ATOM   3850 C  CB  . VAL B  1 205 ? 49.203  12.102  13.921  1.00 22.44  ? 191 VAL B CB  1 
ATOM   3851 C  CG1 . VAL B  1 205 ? 50.284  11.414  14.749  1.00 23.75  ? 191 VAL B CG1 1 
ATOM   3852 C  CG2 . VAL B  1 205 ? 49.353  11.746  12.447  1.00 22.95  ? 191 VAL B CG2 1 
ATOM   3853 N  N   . LEU B  1 206 ? 47.427  11.268  16.799  1.00 22.01  ? 192 LEU B N   1 
ATOM   3854 C  CA  . LEU B  1 206 ? 47.257  11.545  18.218  1.00 22.92  ? 192 LEU B CA  1 
ATOM   3855 C  C   . LEU B  1 206 ? 48.606  11.385  18.921  1.00 21.87  ? 192 LEU B C   1 
ATOM   3856 O  O   . LEU B  1 206 ? 49.263  10.358  18.777  1.00 21.42  ? 192 LEU B O   1 
ATOM   3857 C  CB  . LEU B  1 206 ? 46.201  10.604  18.803  1.00 22.32  ? 192 LEU B CB  1 
ATOM   3858 C  CG  . LEU B  1 206 ? 44.878  10.501  18.034  1.00 24.13  ? 192 LEU B CG  1 
ATOM   3859 C  CD1 . LEU B  1 206 ? 43.951  9.462   18.659  1.00 25.90  ? 192 LEU B CD1 1 
ATOM   3860 C  CD2 . LEU B  1 206 ? 44.181  11.850  17.948  1.00 25.91  ? 192 LEU B CD2 1 
ATOM   3861 N  N   . ASN B  1 207 ? 49.009  12.414  19.678  1.00 20.83  ? 193 ASN B N   1 
ATOM   3862 C  CA  . ASN B  1 207 ? 50.272  12.410  20.405  1.00 21.39  ? 193 ASN B CA  1 
ATOM   3863 C  C   . ASN B  1 207 ? 50.039  11.842  21.805  1.00 20.94  ? 193 ASN B C   1 
ATOM   3864 O  O   . ASN B  1 207 ? 49.625  12.565  22.708  1.00 19.51  ? 193 ASN B O   1 
ATOM   3865 C  CB  . ASN B  1 207 ? 50.896  13.805  20.440  1.00 21.71  ? 193 ASN B CB  1 
ATOM   3866 C  CG  . ASN B  1 207 ? 52.243  13.830  21.125  1.00 19.42  ? 193 ASN B CG  1 
ATOM   3867 O  OD1 . ASN B  1 207 ? 52.741  12.782  21.552  1.00 19.32  ? 193 ASN B OD1 1 
ATOM   3868 N  ND2 . ASN B  1 207 ? 52.842  15.006  21.246  1.00 21.55  ? 193 ASN B ND2 1 
ATOM   3869 N  N   . PHE B  1 208 ? 50.320  10.543  21.978  1.00 20.48  ? 194 PHE B N   1 
ATOM   3870 C  CA  . PHE B  1 208 ? 50.028  9.842   23.221  1.00 20.73  ? 194 PHE B CA  1 
ATOM   3871 C  C   . PHE B  1 208 ? 51.158  10.034  24.232  1.00 21.26  ? 194 PHE B C   1 
ATOM   3872 O  O   . PHE B  1 208 ? 50.945  9.874   25.432  1.00 21.34  ? 194 PHE B O   1 
ATOM   3873 C  CB  . PHE B  1 208 ? 49.802  8.347   22.971  1.00 21.50  ? 194 PHE B CB  1 
ATOM   3874 C  CG  . PHE B  1 208 ? 48.486  7.987   22.294  1.00 21.68  ? 194 PHE B CG  1 
ATOM   3875 C  CD1 . PHE B  1 208 ? 47.359  8.792   22.433  1.00 23.99  ? 194 PHE B CD1 1 
ATOM   3876 C  CD2 . PHE B  1 208 ? 48.378  6.832   21.527  1.00 21.68  ? 194 PHE B CD2 1 
ATOM   3877 C  CE1 . PHE B  1 208 ? 46.164  8.452   21.817  1.00 22.96  ? 194 PHE B CE1 1 
ATOM   3878 C  CE2 . PHE B  1 208 ? 47.181  6.500   20.911  1.00 21.55  ? 194 PHE B CE2 1 
ATOM   3879 C  CZ  . PHE B  1 208 ? 46.077  7.308   21.059  1.00 21.99  ? 194 PHE B CZ  1 
ATOM   3880 N  N   . GLY B  1 209 ? 52.363  10.350  23.742  1.00 21.23  ? 195 GLY B N   1 
ATOM   3881 C  CA  . GLY B  1 209 ? 53.514  10.568  24.606  1.00 21.02  ? 195 GLY B CA  1 
ATOM   3882 C  C   . GLY B  1 209 ? 54.042  9.263   25.202  1.00 20.16  ? 195 GLY B C   1 
ATOM   3883 O  O   . GLY B  1 209 ? 53.829  8.187   24.646  1.00 19.69  ? 195 GLY B O   1 
ATOM   3884 N  N   . SER B  1 210 ? 54.728  9.379   26.347  1.00 18.09  ? 196 SER B N   1 
ATOM   3885 C  CA  . SER B  1 210 ? 55.409  8.256   26.973  1.00 18.04  ? 196 SER B CA  1 
ATOM   3886 C  C   . SER B  1 210 ? 54.407  7.324   27.654  1.00 18.90  ? 196 SER B C   1 
ATOM   3887 O  O   . SER B  1 210 ? 53.412  7.768   28.226  1.00 19.50  ? 196 SER B O   1 
ATOM   3888 C  CB  . SER B  1 210 ? 56.463  8.737   27.947  1.00 19.23  ? 196 SER B CB  1 
ATOM   3889 O  OG  . SER B  1 210 ? 55.909  9.628   28.902  1.00 19.54  ? 196 SER B OG  1 
ATOM   3890 N  N   . GLY B  1 211 ? 54.689  6.018   27.583  1.00 18.41  ? 197 GLY B N   1 
ATOM   3891 C  CA  . GLY B  1 211 ? 53.858  5.002   28.211  1.00 18.69  ? 197 GLY B CA  1 
ATOM   3892 C  C   . GLY B  1 211 ? 54.449  3.609   28.013  1.00 18.08  ? 197 GLY B C   1 
ATOM   3893 O  O   . GLY B  1 211 ? 55.438  3.253   28.650  1.00 18.13  ? 197 GLY B O   1 
ATOM   3894 N  N   . HIS B  1 212 ? 53.823  2.829   27.124  1.00 19.59  ? 198 HIS B N   1 
ATOM   3895 C  CA  . HIS B  1 212 ? 54.349  1.538   26.712  1.00 18.43  ? 198 HIS B CA  1 
ATOM   3896 C  C   . HIS B  1 212 ? 55.806  1.697   26.283  1.00 19.01  ? 198 HIS B C   1 
ATOM   3897 O  O   . HIS B  1 212 ? 56.658  0.882   26.633  1.00 21.57  ? 198 HIS B O   1 
ATOM   3898 C  CB  . HIS B  1 212 ? 53.485  0.956   25.587  1.00 19.73  ? 198 HIS B CB  1 
ATOM   3899 C  CG  . HIS B  1 212 ? 54.123  -0.168  24.842  1.00 21.20  ? 198 HIS B CG  1 
ATOM   3900 N  ND1 . HIS B  1 212 ? 54.318  -1.419  25.386  1.00 23.57  ? 198 HIS B ND1 1 
ATOM   3901 C  CD2 . HIS B  1 212 ? 54.627  -0.220  23.603  1.00 24.12  ? 198 HIS B CD2 1 
ATOM   3902 C  CE1 . HIS B  1 212 ? 54.910  -2.197  24.490  1.00 23.66  ? 198 HIS B CE1 1 
ATOM   3903 N  NE2 . HIS B  1 212 ? 55.108  -1.488  23.401  1.00 24.41  ? 198 HIS B NE2 1 
ATOM   3904 N  N   . ALA B  1 213 ? 56.072  2.756   25.509  1.00 19.56  ? 199 ALA B N   1 
ATOM   3905 C  CA  . ALA B  1 213 ? 57.414  3.076   25.044  1.00 19.64  ? 199 ALA B CA  1 
ATOM   3906 C  C   . ALA B  1 213 ? 57.700  4.561   25.275  1.00 18.80  ? 199 ALA B C   1 
ATOM   3907 O  O   . ALA B  1 213 ? 56.919  5.243   25.939  1.00 18.10  ? 199 ALA B O   1 
ATOM   3908 C  CB  . ALA B  1 213 ? 57.552  2.691   23.586  1.00 21.05  ? 199 ALA B CB  1 
ATOM   3909 N  N   . TRP B  1 214 ? 58.821  5.054   24.726  1.00 17.84  ? 200 TRP B N   1 
ATOM   3910 C  CA  . TRP B  1 214 ? 59.260  6.427   24.940  1.00 19.69  ? 200 TRP B CA  1 
ATOM   3911 C  C   . TRP B  1 214 ? 58.252  7.419   24.359  1.00 17.82  ? 200 TRP B C   1 
ATOM   3912 O  O   . TRP B  1 214 ? 57.967  8.443   24.973  1.00 18.75  ? 200 TRP B O   1 
ATOM   3913 C  CB  . TRP B  1 214 ? 60.654  6.675   24.336  1.00 21.34  ? 200 TRP B CB  1 
ATOM   3914 C  CG  . TRP B  1 214 ? 61.778  5.909   24.987  1.00 23.57  ? 200 TRP B CG  1 
ATOM   3915 C  CD1 . TRP B  1 214 ? 62.204  6.006   26.280  1.00 28.00  ? 200 TRP B CD1 1 
ATOM   3916 C  CD2 . TRP B  1 214 ? 62.658  4.957   24.349  1.00 24.06  ? 200 TRP B CD2 1 
ATOM   3917 N  NE1 . TRP B  1 214 ? 63.261  5.162   26.499  1.00 26.45  ? 200 TRP B NE1 1 
ATOM   3918 C  CE2 . TRP B  1 214 ? 63.567  4.510   25.334  1.00 26.50  ? 200 TRP B CE2 1 
ATOM   3919 C  CE3 . TRP B  1 214 ? 62.759  4.436   23.055  1.00 24.41  ? 200 TRP B CE3 1 
ATOM   3920 C  CZ2 . TRP B  1 214 ? 64.559  3.571   25.059  1.00 25.75  ? 200 TRP B CZ2 1 
ATOM   3921 C  CZ3 . TRP B  1 214 ? 63.743  3.511   22.784  1.00 25.76  ? 200 TRP B CZ3 1 
ATOM   3922 C  CH2 . TRP B  1 214 ? 64.630  3.086   23.773  1.00 27.57  ? 200 TRP B CH2 1 
ATOM   3923 N  N   . GLY B  1 215 ? 57.742  7.127   23.157  1.00 16.74  ? 201 GLY B N   1 
ATOM   3924 C  CA  . GLY B  1 215 ? 56.852  8.045   22.462  1.00 17.67  ? 201 GLY B CA  1 
ATOM   3925 C  C   . GLY B  1 215 ? 55.846  7.304   21.585  1.00 17.10  ? 201 GLY B C   1 
ATOM   3926 O  O   . GLY B  1 215 ? 56.220  6.738   20.563  1.00 22.83  ? 201 GLY B O   1 
ATOM   3927 N  N   . MET B  1 216 ? 54.569  7.340   21.991  1.00 17.86  ? 202 MET B N   1 
ATOM   3928 C  CA  . MET B  1 216 ? 53.504  6.599   21.330  1.00 18.97  ? 202 MET B CA  1 
ATOM   3929 C  C   . MET B  1 216 ? 52.660  7.545   20.474  1.00 19.47  ? 202 MET B C   1 
ATOM   3930 O  O   . MET B  1 216 ? 52.278  8.628   20.918  1.00 18.17  ? 202 MET B O   1 
ATOM   3931 C  CB  . MET B  1 216 ? 52.602  5.903   22.359  1.00 18.54  ? 202 MET B CB  1 
ATOM   3932 C  CG  . MET B  1 216 ? 53.341  4.961   23.298  1.00 20.93  ? 202 MET B CG  1 
ATOM   3933 S  SD  . MET B  1 216 ? 54.183  3.602   22.457  1.00 24.44  ? 202 MET B SD  1 
ATOM   3934 C  CE  . MET B  1 216 ? 52.796  2.660   21.814  1.00 23.41  ? 202 MET B CE  1 
ATOM   3935 N  N   . LEU B  1 217 ? 52.374  7.118   19.239  1.00 17.32  ? 203 LEU B N   1 
ATOM   3936 C  CA  . LEU B  1 217 ? 51.476  7.839   18.350  1.00 18.14  ? 203 LEU B CA  1 
ATOM   3937 C  C   . LEU B  1 217 ? 50.252  6.971   18.068  1.00 20.27  ? 203 LEU B C   1 
ATOM   3938 O  O   . LEU B  1 217 ? 50.382  5.769   17.848  1.00 19.56  ? 203 LEU B O   1 
ATOM   3939 C  CB  . LEU B  1 217 ? 52.191  8.207   17.048  1.00 18.53  ? 203 LEU B CB  1 
ATOM   3940 C  CG  . LEU B  1 217 ? 53.363  9.189   17.157  1.00 17.85  ? 203 LEU B CG  1 
ATOM   3941 C  CD1 . LEU B  1 217 ? 53.862  9.597   15.777  1.00 18.20  ? 203 LEU B CD1 1 
ATOM   3942 C  CD2 . LEU B  1 217 ? 52.983  10.417  17.968  1.00 18.29  ? 203 LEU B CD2 1 
ATOM   3943 N  N   . GLY B  1 218 ? 49.068  7.597   18.081  1.00 20.19  ? 204 GLY B N   1 
ATOM   3944 C  CA  . GLY B  1 218 ? 47.839  6.945   17.657  1.00 19.93  ? 204 GLY B CA  1 
ATOM   3945 C  C   . GLY B  1 218 ? 47.260  7.629   16.421  1.00 20.60  ? 204 GLY B C   1 
ATOM   3946 O  O   . GLY B  1 218 ? 47.823  8.607   15.933  1.00 20.00  ? 204 GLY B O   1 
ATOM   3947 N  N   . LEU B  1 219 ? 46.141  7.097   15.917  1.00 21.24  ? 205 LEU B N   1 
ATOM   3948 C  CA  . LEU B  1 219 ? 45.440  7.702   14.796  1.00 24.61  ? 205 LEU B CA  1 
ATOM   3949 C  C   . LEU B  1 219 ? 43.942  7.739   15.098  1.00 23.49  ? 205 LEU B C   1 
ATOM   3950 O  O   . LEU B  1 219 ? 43.389  6.771   15.615  1.00 21.84  ? 205 LEU B O   1 
ATOM   3951 C  CB  . LEU B  1 219 ? 45.733  6.902   13.527  1.00 27.68  ? 205 LEU B CB  1 
ATOM   3952 C  CG  . LEU B  1 219 ? 45.743  7.699   12.219  1.00 29.17  ? 205 LEU B CG  1 
ATOM   3953 C  CD1 . LEU B  1 219 ? 46.929  8.654   12.179  1.00 26.65  ? 205 LEU B CD1 1 
ATOM   3954 C  CD2 . LEU B  1 219 ? 45.762  6.771   11.014  1.00 29.63  ? 205 LEU B CD2 1 
ATOM   3955 N  N   . HIS B  1 220 ? 43.296  8.871   14.796  1.00 23.57  ? 206 HIS B N   1 
ATOM   3956 C  CA  . HIS B  1 220 ? 41.843  8.919   14.754  1.00 24.70  ? 206 HIS B CA  1 
ATOM   3957 C  C   . HIS B  1 220 ? 41.400  9.112   13.307  1.00 24.96  ? 206 HIS B C   1 
ATOM   3958 O  O   . HIS B  1 220 ? 41.794  10.077  12.655  1.00 26.23  ? 206 HIS B O   1 
ATOM   3959 C  CB  . HIS B  1 220 ? 41.262  10.015  15.656  1.00 26.44  ? 206 HIS B CB  1 
ATOM   3960 C  CG  . HIS B  1 220 ? 39.774  10.143  15.523  1.00 29.42  ? 206 HIS B CG  1 
ATOM   3961 N  ND1 . HIS B  1 220 ? 38.890  9.258   16.106  1.00 29.80  ? 206 HIS B ND1 1 
ATOM   3962 C  CD2 . HIS B  1 220 ? 39.022  11.024  14.847  1.00 28.80  ? 206 HIS B CD2 1 
ATOM   3963 C  CE1 . HIS B  1 220 ? 37.648  9.612   15.800  1.00 30.14  ? 206 HIS B CE1 1 
ATOM   3964 N  NE2 . HIS B  1 220 ? 37.705  10.683  15.037  1.00 35.18  ? 206 HIS B NE2 1 
ATOM   3965 N  N   . VAL B  1 221 ? 40.585  8.172   12.818  1.00 26.13  ? 207 VAL B N   1 
ATOM   3966 C  CA  . VAL B  1 221 ? 40.059  8.238   11.465  1.00 24.41  ? 207 VAL B CA  1 
ATOM   3967 C  C   . VAL B  1 221 ? 38.544  8.426   11.528  1.00 24.13  ? 207 VAL B C   1 
ATOM   3968 O  O   . VAL B  1 221 ? 37.850  7.679   12.212  1.00 23.74  ? 207 VAL B O   1 
ATOM   3969 C  CB  . VAL B  1 221 ? 40.430  6.979   10.657  1.00 25.66  ? 207 VAL B CB  1 
ATOM   3970 C  CG1 . VAL B  1 221 ? 39.849  7.029   9.249   1.00 24.83  ? 207 VAL B CG1 1 
ATOM   3971 C  CG2 . VAL B  1 221 ? 41.938  6.751   10.611  1.00 26.57  ? 207 VAL B CG2 1 
ATOM   3972 N  N   . GLU B  1 222 ? 38.047  9.440   10.808  1.00 25.25  ? 208 GLU B N   1 
ATOM   3973 C  CA  . GLU B  1 222 ? 36.617  9.641   10.626  1.00 29.50  ? 208 GLU B CA  1 
ATOM   3974 C  C   . GLU B  1 222 ? 36.251  9.229   9.200   1.00 27.60  ? 208 GLU B C   1 
ATOM   3975 O  O   . GLU B  1 222 ? 36.561  9.940   8.247   1.00 27.95  ? 208 GLU B O   1 
ATOM   3976 C  CB  . GLU B  1 222 ? 36.248  11.098  10.923  1.00 30.50  ? 208 GLU B CB  1 
ATOM   3977 C  CG  . GLU B  1 222 ? 34.745  11.372  10.971  1.00 34.13  ? 208 GLU B CG  1 
ATOM   3978 C  CD  . GLU B  1 222 ? 33.989  10.676  12.090  1.00 34.58  ? 208 GLU B CD  1 
ATOM   3979 O  OE1 . GLU B  1 222 ? 34.491  10.680  13.232  1.00 39.91  ? 208 GLU B OE1 1 
ATOM   3980 O  OE2 . GLU B  1 222 ? 32.886  10.153  11.830  1.00 32.47  ? 208 GLU B OE2 1 
ATOM   3981 N  N   . LEU B  1 223 ? 35.618  8.056   9.069   1.00 26.80  ? 209 LEU B N   1 
ATOM   3982 C  CA  . LEU B  1 223 ? 35.197  7.529   7.779   1.00 27.76  ? 209 LEU B CA  1 
ATOM   3983 C  C   . LEU B  1 223 ? 33.733  7.889   7.530   1.00 28.14  ? 209 LEU B C   1 
ATOM   3984 O  O   . LEU B  1 223 ? 32.889  7.699   8.403   1.00 31.55  ? 209 LEU B O   1 
ATOM   3985 C  CB  . LEU B  1 223 ? 35.396  6.012   7.750   1.00 26.93  ? 209 LEU B CB  1 
ATOM   3986 C  CG  . LEU B  1 223 ? 36.844  5.511   7.769   1.00 28.63  ? 209 LEU B CG  1 
ATOM   3987 C  CD1 . LEU B  1 223 ? 36.886  3.992   7.784   1.00 28.78  ? 209 LEU B CD1 1 
ATOM   3988 C  CD2 . LEU B  1 223 ? 37.634  6.057   6.591   1.00 30.99  ? 209 LEU B CD2 1 
ATOM   3989 N  N   . PRO B  1 224 ? 33.385  8.415   6.333   1.00 31.37  ? 210 PRO B N   1 
ATOM   3990 C  CA  . PRO B  1 224 ? 31.990  8.727   6.006   1.00 32.94  ? 210 PRO B CA  1 
ATOM   3991 C  C   . PRO B  1 224 ? 30.967  7.676   6.438   1.00 31.53  ? 210 PRO B C   1 
ATOM   3992 O  O   . PRO B  1 224 ? 29.982  8.009   7.094   1.00 30.78  ? 210 PRO B O   1 
ATOM   3993 C  CB  . PRO B  1 224 ? 32.060  8.883   4.476   1.00 32.43  ? 210 PRO B CB  1 
ATOM   3994 C  CG  . PRO B  1 224 ? 33.432  9.477   4.236   1.00 35.49  ? 210 PRO B CG  1 
ATOM   3995 C  CD  . PRO B  1 224 ? 34.322  8.782   5.257   1.00 32.14  ? 210 PRO B CD  1 
ATOM   3996 N  N   . GLU B  1 225 ? 31.203  6.410   6.067   1.00 27.98  ? 211 GLU B N   1 
ATOM   3997 C  CA  . GLU B  1 225 ? 30.242  5.344   6.312   1.00 32.99  ? 211 GLU B CA  1 
ATOM   3998 C  C   . GLU B  1 225 ? 30.447  4.748   7.705   1.00 35.44  ? 211 GLU B C   1 
ATOM   3999 O  O   . GLU B  1 225 ? 29.495  4.602   8.470   1.00 38.71  ? 211 GLU B O   1 
ATOM   4000 C  CB  . GLU B  1 225 ? 30.355  4.240   5.257   1.00 37.53  ? 211 GLU B CB  1 
ATOM   4001 C  CG  . GLU B  1 225 ? 29.469  3.028   5.542   1.00 45.82  ? 211 GLU B CG  1 
ATOM   4002 C  CD  . GLU B  1 225 ? 29.760  1.800   4.695   1.00 52.15  ? 211 GLU B CD  1 
ATOM   4003 O  OE1 . GLU B  1 225 ? 30.142  0.759   5.273   1.00 60.45  ? 211 GLU B OE1 1 
ATOM   4004 O  OE2 . GLU B  1 225 ? 29.598  1.878   3.458   1.00 48.69  ? 211 GLU B OE2 1 
ATOM   4005 N  N   . THR B  1 226 ? 31.700  4.403   8.025   1.00 34.12  ? 212 THR B N   1 
ATOM   4006 C  CA  . THR B  1 226 ? 32.006  3.587   9.192   1.00 32.64  ? 212 THR B CA  1 
ATOM   4007 C  C   . THR B  1 226 ? 32.010  4.441   10.460  1.00 31.39  ? 212 THR B C   1 
ATOM   4008 O  O   . THR B  1 226 ? 31.741  3.932   11.547  1.00 29.18  ? 212 THR B O   1 
ATOM   4009 C  CB  . THR B  1 226 ? 33.348  2.878   8.999   1.00 33.48  ? 212 THR B CB  1 
ATOM   4010 O  OG1 . THR B  1 226 ? 33.163  1.949   7.934   1.00 33.56  ? 212 THR B OG1 1 
ATOM   4011 C  CG2 . THR B  1 226 ? 33.803  2.141   10.246  1.00 33.96  ? 212 THR B CG2 1 
ATOM   4012 N  N   . GLY B  1 227 ? 32.327  5.733   10.319  1.00 28.18  ? 213 GLY B N   1 
ATOM   4013 C  CA  . GLY B  1 227 ? 32.435  6.617   11.468  1.00 27.59  ? 213 GLY B CA  1 
ATOM   4014 C  C   . GLY B  1 227 ? 33.837  6.580   12.075  1.00 26.24  ? 213 GLY B C   1 
ATOM   4015 O  O   . GLY B  1 227 ? 34.821  6.392   11.362  1.00 24.67  ? 213 GLY B O   1 
ATOM   4016 N  N   . GLY B  1 228 ? 33.910  6.742   13.402  1.00 29.31  ? 214 GLY B N   1 
ATOM   4017 C  CA  . GLY B  1 228 ? 35.167  7.011   14.088  1.00 26.42  ? 214 GLY B CA  1 
ATOM   4018 C  C   . GLY B  1 228 ? 35.933  5.740   14.456  1.00 23.72  ? 214 GLY B C   1 
ATOM   4019 O  O   . GLY B  1 228 ? 35.362  4.797   14.998  1.00 21.37  ? 214 GLY B O   1 
ATOM   4020 N  N   . ILE B  1 229 ? 37.244  5.746   14.171  1.00 22.41  ? 215 ILE B N   1 
ATOM   4021 C  CA  . ILE B  1 229 ? 38.142  4.664   14.546  1.00 23.70  ? 215 ILE B CA  1 
ATOM   4022 C  C   . ILE B  1 229 ? 39.385  5.247   15.219  1.00 23.15  ? 215 ILE B C   1 
ATOM   4023 O  O   . ILE B  1 229 ? 40.005  6.169   14.691  1.00 24.38  ? 215 ILE B O   1 
ATOM   4024 C  CB  . ILE B  1 229 ? 38.537  3.823   13.317  1.00 26.84  ? 215 ILE B CB  1 
ATOM   4025 C  CG1 . ILE B  1 229 ? 37.315  3.300   12.564  1.00 28.38  ? 215 ILE B CG1 1 
ATOM   4026 C  CG2 . ILE B  1 229 ? 39.487  2.692   13.715  1.00 26.53  ? 215 ILE B CG2 1 
ATOM   4027 C  CD1 . ILE B  1 229 ? 37.636  2.745   11.189  1.00 31.82  ? 215 ILE B CD1 1 
ATOM   4028 N  N   . ILE B  1 230 ? 39.752  4.686   16.379  1.00 22.63  ? 216 ILE B N   1 
ATOM   4029 C  CA  . ILE B  1 230 ? 41.008  5.019   17.033  1.00 21.26  ? 216 ILE B CA  1 
ATOM   4030 C  C   . ILE B  1 230 ? 41.966  3.836   16.902  1.00 20.93  ? 216 ILE B C   1 
ATOM   4031 O  O   . ILE B  1 230 ? 41.688  2.748   17.403  1.00 20.36  ? 216 ILE B O   1 
ATOM   4032 C  CB  . ILE B  1 230 ? 40.795  5.396   18.510  1.00 22.87  ? 216 ILE B CB  1 
ATOM   4033 C  CG1 . ILE B  1 230 ? 39.970  6.677   18.668  1.00 24.85  ? 216 ILE B CG1 1 
ATOM   4034 C  CG2 . ILE B  1 230 ? 42.140  5.500   19.231  1.00 23.22  ? 216 ILE B CG2 1 
ATOM   4035 C  CD1 . ILE B  1 230 ? 39.338  6.838   20.040  1.00 25.26  ? 216 ILE B CD1 1 
ATOM   4036 N  N   . LEU B  1 231 ? 43.100  4.063   16.229  1.00 20.81  ? 217 LEU B N   1 
ATOM   4037 C  CA  . LEU B  1 231 ? 44.180  3.091   16.187  1.00 21.59  ? 217 LEU B CA  1 
ATOM   4038 C  C   . LEU B  1 231 ? 45.094  3.323   17.388  1.00 20.90  ? 217 LEU B C   1 
ATOM   4039 O  O   . LEU B  1 231 ? 45.836  4.304   17.424  1.00 22.71  ? 217 LEU B O   1 
ATOM   4040 C  CB  . LEU B  1 231 ? 44.949  3.218   14.871  1.00 22.49  ? 217 LEU B CB  1 
ATOM   4041 C  CG  . LEU B  1 231 ? 44.119  3.114   13.587  1.00 24.12  ? 217 LEU B CG  1 
ATOM   4042 C  CD1 . LEU B  1 231 ? 45.023  3.166   12.364  1.00 23.45  ? 217 LEU B CD1 1 
ATOM   4043 C  CD2 . LEU B  1 231 ? 43.267  1.854   13.580  1.00 24.82  ? 217 LEU B CD2 1 
ATOM   4044 N  N   . ALA B  1 232 ? 45.041  2.399   18.356  1.00 21.09  ? 218 ALA B N   1 
ATOM   4045 C  CA  . ALA B  1 232 ? 45.725  2.554   19.630  1.00 21.73  ? 218 ALA B CA  1 
ATOM   4046 C  C   . ALA B  1 232 ? 47.131  1.957   19.581  1.00 20.58  ? 218 ALA B C   1 
ATOM   4047 O  O   . ALA B  1 232 ? 47.996  2.337   20.369  1.00 21.09  ? 218 ALA B O   1 
ATOM   4048 C  CB  . ALA B  1 232 ? 44.906  1.900   20.723  1.00 23.88  ? 218 ALA B CB  1 
ATOM   4049 N  N   . SER B  1 233 ? 47.342  0.995   18.677  1.00 18.82  ? 219 SER B N   1 
ATOM   4050 C  CA  . SER B  1 233 ? 48.564  0.205   18.669  1.00 20.27  ? 219 SER B CA  1 
ATOM   4051 C  C   . SER B  1 233 ? 48.851  -0.317  20.078  1.00 20.10  ? 219 SER B C   1 
ATOM   4052 O  O   . SER B  1 233 ? 47.939  -0.757  20.779  1.00 20.27  ? 219 SER B O   1 
ATOM   4053 C  CB  . SER B  1 233 ? 49.727  0.999   18.115  1.00 22.31  ? 219 SER B CB  1 
ATOM   4054 O  OG  . SER B  1 233 ? 50.885  0.186   17.977  1.00 24.74  ? 219 SER B OG  1 
ATOM   4055 N  N   . ASP B  1 234 ? 50.122  -0.247  20.495  1.00 23.08  ? 220 ASP B N   1 
ATOM   4056 C  CA  . ASP B  1 234 ? 50.571  -0.866  21.735  1.00 23.77  ? 220 ASP B CA  1 
ATOM   4057 C  C   . ASP B  1 234 ? 50.266  0.023   22.939  1.00 22.36  ? 220 ASP B C   1 
ATOM   4058 O  O   . ASP B  1 234 ? 50.702  -0.281  24.047  1.00 24.06  ? 220 ASP B O   1 
ATOM   4059 C  CB  . ASP B  1 234 ? 52.051  -1.217  21.685  1.00 25.59  ? 220 ASP B CB  1 
ATOM   4060 C  CG  . ASP B  1 234 ? 52.396  -2.428  20.831  1.00 27.51  ? 220 ASP B CG  1 
ATOM   4061 O  OD1 . ASP B  1 234 ? 51.451  -3.054  20.304  1.00 24.23  ? 220 ASP B OD1 1 
ATOM   4062 O  OD2 . ASP B  1 234 ? 53.602  -2.732  20.702  1.00 33.33  ? 220 ASP B OD2 1 
ATOM   4063 N  N   . ALA B  1 235 ? 49.525  1.114   22.722  1.00 22.24  ? 221 ALA B N   1 
ATOM   4064 C  CA  . ALA B  1 235 ? 48.978  1.883   23.827  1.00 20.29  ? 221 ALA B CA  1 
ATOM   4065 C  C   . ALA B  1 235 ? 47.952  1.023   24.567  1.00 23.09  ? 221 ALA B C   1 
ATOM   4066 O  O   . ALA B  1 235 ? 47.767  1.172   25.773  1.00 20.99  ? 221 ALA B O   1 
ATOM   4067 C  CB  . ALA B  1 235 ? 48.372  3.176   23.324  1.00 19.56  ? 221 ALA B CB  1 
ATOM   4068 N  N   . ILE B  1 236 ? 47.298  0.117   23.824  1.00 20.34  ? 222 ILE B N   1 
ATOM   4069 C  CA  . ILE B  1 236 ? 46.378  -0.860  24.394  1.00 21.62  ? 222 ILE B CA  1 
ATOM   4070 C  C   . ILE B  1 236 ? 46.497  -2.163  23.602  1.00 21.55  ? 222 ILE B C   1 
ATOM   4071 O  O   . ILE B  1 236 ? 45.972  -2.268  22.496  1.00 22.13  ? 222 ILE B O   1 
ATOM   4072 C  CB  . ILE B  1 236 ? 44.924  -0.341  24.392  1.00 22.22  ? 222 ILE B CB  1 
ATOM   4073 C  CG1 . ILE B  1 236 ? 44.821  1.110   24.877  1.00 22.72  ? 222 ILE B CG1 1 
ATOM   4074 C  CG2 . ILE B  1 236 ? 44.016  -1.272  25.199  1.00 23.24  ? 222 ILE B CG2 1 
ATOM   4075 C  CD1 . ILE B  1 236 ? 43.472  1.759   24.609  1.00 22.71  ? 222 ILE B CD1 1 
ATOM   4076 N  N   . TYR B  1 237 ? 47.183  -3.152  24.188  1.00 22.52  ? 223 TYR B N   1 
ATOM   4077 C  CA  . TYR B  1 237 ? 47.411  -4.444  23.554  1.00 23.10  ? 223 TYR B CA  1 
ATOM   4078 C  C   . TYR B  1 237 ? 46.084  -5.106  23.163  1.00 23.99  ? 223 TYR B C   1 
ATOM   4079 O  O   . TYR B  1 237 ? 45.905  -5.480  22.006  1.00 28.04  ? 223 TYR B O   1 
ATOM   4080 C  CB  . TYR B  1 237 ? 48.211  -5.357  24.492  1.00 21.39  ? 223 TYR B CB  1 
ATOM   4081 C  CG  . TYR B  1 237 ? 49.735  -5.264  24.452  1.00 22.88  ? 223 TYR B CG  1 
ATOM   4082 C  CD1 . TYR B  1 237 ? 50.420  -4.828  23.322  1.00 23.26  ? 223 TYR B CD1 1 
ATOM   4083 C  CD2 . TYR B  1 237 ? 50.497  -5.652  25.551  1.00 24.01  ? 223 TYR B CD2 1 
ATOM   4084 C  CE1 . TYR B  1 237 ? 51.806  -4.765  23.293  1.00 22.97  ? 223 TYR B CE1 1 
ATOM   4085 C  CE2 . TYR B  1 237 ? 51.882  -5.593  25.534  1.00 24.49  ? 223 TYR B CE2 1 
ATOM   4086 C  CZ  . TYR B  1 237 ? 52.540  -5.149  24.402  1.00 24.87  ? 223 TYR B CZ  1 
ATOM   4087 O  OH  . TYR B  1 237 ? 53.906  -5.098  24.392  1.00 29.67  ? 223 TYR B OH  1 
ATOM   4088 N  N   . THR B  1 238 ? 45.167  -5.274  24.131  1.00 23.63  ? 224 THR B N   1 
ATOM   4089 C  CA  . THR B  1 238 ? 43.964  -6.077  23.937  1.00 24.48  ? 224 THR B CA  1 
ATOM   4090 C  C   . THR B  1 238 ? 42.786  -5.503  24.723  1.00 26.18  ? 224 THR B C   1 
ATOM   4091 O  O   . THR B  1 238 ? 42.937  -4.558  25.494  1.00 25.85  ? 224 THR B O   1 
ATOM   4092 C  CB  . THR B  1 238 ? 44.189  -7.525  24.380  1.00 25.47  ? 224 THR B CB  1 
ATOM   4093 O  OG1 . THR B  1 238 ? 44.275  -7.483  25.802  1.00 27.76  ? 224 THR B OG1 1 
ATOM   4094 C  CG2 . THR B  1 238 ? 45.437  -8.156  23.790  1.00 24.68  ? 224 THR B CG2 1 
ATOM   4095 N  N   . ALA B  1 239 ? 41.612  -6.124  24.536  1.00 26.45  ? 225 ALA B N   1 
ATOM   4096 C  CA  . ALA B  1 239 ? 40.415  -5.788  25.291  1.00 25.94  ? 225 ALA B CA  1 
ATOM   4097 C  C   . ALA B  1 239 ? 40.671  -5.994  26.782  1.00 24.35  ? 225 ALA B C   1 
ATOM   4098 O  O   . ALA B  1 239 ? 40.135  -5.262  27.611  1.00 25.00  ? 225 ALA B O   1 
ATOM   4099 C  CB  . ALA B  1 239 ? 39.240  -6.621  24.813  1.00 25.19  ? 225 ALA B CB  1 
ATOM   4100 N  N   . GLU B  1 240 ? 41.503  -6.992  27.108  1.00 24.93  ? 226 GLU B N   1 
ATOM   4101 C  CA  . GLU B  1 240 ? 41.802  -7.334  28.491  1.00 26.14  ? 226 GLU B CA  1 
ATOM   4102 C  C   . GLU B  1 240 ? 42.608  -6.201  29.127  1.00 27.17  ? 226 GLU B C   1 
ATOM   4103 O  O   . GLU B  1 240 ? 42.377  -5.843  30.280  1.00 25.98  ? 226 GLU B O   1 
ATOM   4104 C  CB  . GLU B  1 240 ? 42.546  -8.669  28.583  1.00 28.26  ? 226 GLU B CB  1 
ATOM   4105 C  CG  . GLU B  1 240 ? 42.695  -9.182  30.013  1.00 33.12  ? 226 GLU B CG  1 
ATOM   4106 C  CD  . GLU B  1 240 ? 43.520  -10.448 30.175  1.00 35.07  ? 226 GLU B CD  1 
ATOM   4107 O  OE1 . GLU B  1 240 ? 44.008  -10.990 29.161  1.00 36.33  ? 226 GLU B OE1 1 
ATOM   4108 O  OE2 . GLU B  1 240 ? 43.677  -10.894 31.331  1.00 37.87  ? 226 GLU B OE2 1 
ATOM   4109 N  N   . SER B  1 241 ? 43.560  -5.646  28.364  1.00 25.11  ? 227 SER B N   1 
ATOM   4110 C  CA  . SER B  1 241 ? 44.316  -4.481  28.794  1.00 23.76  ? 227 SER B CA  1 
ATOM   4111 C  C   . SER B  1 241 ? 43.354  -3.351  29.151  1.00 21.59  ? 227 SER B C   1 
ATOM   4112 O  O   . SER B  1 241 ? 43.512  -2.689  30.175  1.00 21.62  ? 227 SER B O   1 
ATOM   4113 C  CB  . SER B  1 241 ? 45.291  -4.031  27.726  1.00 24.05  ? 227 SER B CB  1 
ATOM   4114 O  OG  . SER B  1 241 ? 46.096  -5.106  27.264  1.00 23.83  ? 227 SER B OG  1 
ATOM   4115 N  N   . TYR B  1 242 ? 42.345  -3.171  28.292  1.00 20.51  ? 228 TYR B N   1 
ATOM   4116 C  CA  . TYR B  1 242 ? 41.476  -2.005  28.297  1.00 22.33  ? 228 TYR B CA  1 
ATOM   4117 C  C   . TYR B  1 242 ? 40.511  -2.045  29.480  1.00 23.94  ? 228 TYR B C   1 
ATOM   4118 O  O   . TYR B  1 242 ? 40.181  -1.003  30.043  1.00 23.90  ? 228 TYR B O   1 
ATOM   4119 C  CB  . TYR B  1 242 ? 40.735  -2.002  26.955  1.00 22.57  ? 228 TYR B CB  1 
ATOM   4120 C  CG  . TYR B  1 242 ? 40.070  -0.690  26.555  1.00 24.02  ? 228 TYR B CG  1 
ATOM   4121 C  CD1 . TYR B  1 242 ? 40.754  0.520   26.630  1.00 24.42  ? 228 TYR B CD1 1 
ATOM   4122 C  CD2 . TYR B  1 242 ? 38.759  -0.664  26.091  1.00 23.67  ? 228 TYR B CD2 1 
ATOM   4123 C  CE1 . TYR B  1 242 ? 40.156  1.712   26.253  1.00 25.49  ? 228 TYR B CE1 1 
ATOM   4124 C  CE2 . TYR B  1 242 ? 38.149  0.522   25.714  1.00 24.42  ? 228 TYR B CE2 1 
ATOM   4125 C  CZ  . TYR B  1 242 ? 38.849  1.713   25.793  1.00 25.12  ? 228 TYR B CZ  1 
ATOM   4126 O  OH  . TYR B  1 242 ? 38.245  2.880   25.420  1.00 24.96  ? 228 TYR B OH  1 
ATOM   4127 N  N   . GLY B  1 243 ? 40.043  -3.247  29.838  1.00 25.58  ? 229 GLY B N   1 
ATOM   4128 C  CA  . GLY B  1 243 ? 39.045  -3.394  30.888  1.00 26.95  ? 229 GLY B CA  1 
ATOM   4129 C  C   . GLY B  1 243 ? 37.822  -2.518  30.619  1.00 27.48  ? 229 GLY B C   1 
ATOM   4130 O  O   . GLY B  1 243 ? 37.269  -2.548  29.521  1.00 29.94  ? 229 GLY B O   1 
ATOM   4131 N  N   . PRO B  1 244 ? 37.366  -1.698  31.595  1.00 32.82  ? 230 PRO B N   1 
ATOM   4132 C  CA  . PRO B  1 244 ? 38.053  -1.547  32.881  1.00 34.81  ? 230 PRO B CA  1 
ATOM   4133 C  C   . PRO B  1 244 ? 37.888  -2.738  33.821  1.00 36.79  ? 230 PRO B C   1 
ATOM   4134 O  O   . PRO B  1 244 ? 37.016  -3.579  33.618  1.00 38.50  ? 230 PRO B O   1 
ATOM   4135 C  CB  . PRO B  1 244 ? 37.419  -0.273  33.477  1.00 35.44  ? 230 PRO B CB  1 
ATOM   4136 C  CG  . PRO B  1 244 ? 36.040  -0.191  32.848  1.00 36.37  ? 230 PRO B CG  1 
ATOM   4137 C  CD  . PRO B  1 244 ? 36.149  -0.875  31.496  1.00 34.10  ? 230 PRO B CD  1 
ATOM   4138 N  N   . PRO B  1 245 ? 38.729  -2.849  34.875  1.00 35.16  ? 231 PRO B N   1 
ATOM   4139 C  CA  . PRO B  1 245 ? 39.864  -1.940  35.063  1.00 33.07  ? 231 PRO B CA  1 
ATOM   4140 C  C   . PRO B  1 245 ? 41.018  -2.230  34.104  1.00 30.87  ? 231 PRO B C   1 
ATOM   4141 O  O   . PRO B  1 245 ? 41.071  -3.301  33.504  1.00 27.47  ? 231 PRO B O   1 
ATOM   4142 C  CB  . PRO B  1 245 ? 40.263  -2.185  36.531  1.00 34.96  ? 231 PRO B CB  1 
ATOM   4143 C  CG  . PRO B  1 245 ? 39.846  -3.618  36.800  1.00 35.89  ? 231 PRO B CG  1 
ATOM   4144 C  CD  . PRO B  1 245 ? 38.605  -3.846  35.952  1.00 33.77  ? 231 PRO B CD  1 
ATOM   4145 N  N   . ILE B  1 246 ? 41.945  -1.271  33.973  1.00 25.80  ? 232 ILE B N   1 
ATOM   4146 C  CA  . ILE B  1 246 ? 43.119  -1.443  33.129  1.00 25.31  ? 232 ILE B CA  1 
ATOM   4147 C  C   . ILE B  1 246 ? 43.987  -2.564  33.694  1.00 25.20  ? 232 ILE B C   1 
ATOM   4148 O  O   . ILE B  1 246 ? 44.229  -2.620  34.897  1.00 24.48  ? 232 ILE B O   1 
ATOM   4149 C  CB  . ILE B  1 246 ? 43.922  -0.131  33.006  1.00 25.56  ? 232 ILE B CB  1 
ATOM   4150 C  CG1 . ILE B  1 246 ? 43.128  0.962   32.286  1.00 28.95  ? 232 ILE B CG1 1 
ATOM   4151 C  CG2 . ILE B  1 246 ? 45.272  -0.384  32.329  1.00 24.86  ? 232 ILE B CG2 1 
ATOM   4152 C  CD1 . ILE B  1 246 ? 43.652  2.367   32.526  1.00 33.43  ? 232 ILE B CD1 1 
ATOM   4153 N  N   . LYS B  1 247 ? 44.454  -3.451  32.807  1.00 28.52  ? 233 LYS B N   1 
ATOM   4154 C  CA  . LYS B  1 247 ? 45.488  -4.418  33.141  1.00 29.42  ? 233 LYS B CA  1 
ATOM   4155 C  C   . LYS B  1 247 ? 46.751  -4.084  32.346  1.00 24.76  ? 233 LYS B C   1 
ATOM   4156 O  O   . LYS B  1 247 ? 46.836  -4.405  31.163  1.00 25.77  ? 233 LYS B O   1 
ATOM   4157 C  CB  . LYS B  1 247 ? 45.037  -5.854  32.843  1.00 29.60  ? 233 LYS B CB  1 
ATOM   4158 C  CG  . LYS B  1 247 ? 43.917  -6.401  33.724  1.00 35.14  ? 233 LYS B CG  1 
ATOM   4159 C  CD  . LYS B  1 247 ? 43.910  -7.925  33.788  1.00 40.32  ? 233 LYS B CD  1 
ATOM   4160 C  CE  . LYS B  1 247 ? 42.680  -8.503  34.422  1.00 44.82  ? 233 LYS B CE  1 
ATOM   4161 N  NZ  . LYS B  1 247 ? 42.429  -9.868  33.945  1.00 47.77  ? 233 LYS B NZ  1 
ATOM   4162 N  N   . PRO B  1 248 ? 47.762  -3.428  32.964  1.00 25.17  ? 234 PRO B N   1 
ATOM   4163 C  CA  . PRO B  1 248 ? 48.966  -2.999  32.244  1.00 26.16  ? 234 PRO B CA  1 
ATOM   4164 C  C   . PRO B  1 248 ? 49.902  -4.123  31.803  1.00 24.19  ? 234 PRO B C   1 
ATOM   4165 O  O   . PRO B  1 248 ? 49.876  -5.218  32.358  1.00 25.66  ? 234 PRO B O   1 
ATOM   4166 C  CB  . PRO B  1 248 ? 49.661  -2.063  33.252  1.00 26.94  ? 234 PRO B CB  1 
ATOM   4167 C  CG  . PRO B  1 248 ? 49.199  -2.559  34.606  1.00 27.84  ? 234 PRO B CG  1 
ATOM   4168 C  CD  . PRO B  1 248 ? 47.775  -3.037  34.383  1.00 27.04  ? 234 PRO B CD  1 
ATOM   4169 N  N   . PRO B  1 249 ? 50.757  -3.867  30.784  1.00 25.83  ? 235 PRO B N   1 
ATOM   4170 C  CA  . PRO B  1 249 ? 51.736  -4.849  30.302  1.00 27.01  ? 235 PRO B CA  1 
ATOM   4171 C  C   . PRO B  1 249 ? 53.035  -4.943  31.097  1.00 32.09  ? 235 PRO B C   1 
ATOM   4172 O  O   . PRO B  1 249 ? 53.316  -4.089  31.935  1.00 27.70  ? 235 PRO B O   1 
ATOM   4173 C  CB  . PRO B  1 249 ? 52.017  -4.314  28.888  1.00 29.28  ? 235 PRO B CB  1 
ATOM   4174 C  CG  . PRO B  1 249 ? 51.949  -2.811  29.059  1.00 26.24  ? 235 PRO B CG  1 
ATOM   4175 C  CD  . PRO B  1 249 ? 50.785  -2.612  30.014  1.00 23.85  ? 235 PRO B CD  1 
ATOM   4176 N  N   . GLY B  1 250 ? 53.833  -5.977  30.796  1.00 29.58  ? 236 GLY B N   1 
ATOM   4177 C  CA  . GLY B  1 250 ? 55.184  -6.106  31.321  1.00 34.54  ? 236 GLY B CA  1 
ATOM   4178 C  C   . GLY B  1 250 ? 56.182  -5.258  30.531  1.00 37.64  ? 236 GLY B C   1 
ATOM   4179 O  O   . GLY B  1 250 ? 57.118  -4.703  31.103  1.00 37.25  ? 236 GLY B O   1 
ATOM   4180 N  N   . ILE B  1 251 ? 55.979  -5.177  29.210  1.00 42.19  ? 237 ILE B N   1 
ATOM   4181 C  CA  . ILE B  1 251 ? 56.757  -4.287  28.359  1.00 39.49  ? 237 ILE B CA  1 
ATOM   4182 C  C   . ILE B  1 251 ? 56.207  -2.871  28.526  1.00 35.24  ? 237 ILE B C   1 
ATOM   4183 O  O   . ILE B  1 251 ? 55.174  -2.533  27.951  1.00 30.35  ? 237 ILE B O   1 
ATOM   4184 C  CB  . ILE B  1 251 ? 56.728  -4.754  26.889  1.00 45.37  ? 237 ILE B CB  1 
ATOM   4185 C  CG1 . ILE B  1 251 ? 57.340  -6.151  26.723  1.00 47.43  ? 237 ILE B CG1 1 
ATOM   4186 C  CG2 . ILE B  1 251 ? 57.407  -3.733  25.974  1.00 42.58  ? 237 ILE B CG2 1 
ATOM   4187 C  CD1 . ILE B  1 251 ? 57.328  -6.672  25.296  1.00 47.29  ? 237 ILE B CD1 1 
ATOM   4188 N  N   . ILE B  1 252 ? 56.903  -2.055  29.329  1.00 33.22  ? 238 ILE B N   1 
ATOM   4189 C  CA  . ILE B  1 252 ? 56.410  -0.740  29.714  1.00 32.16  ? 238 ILE B CA  1 
ATOM   4190 C  C   . ILE B  1 252 ? 57.588  0.156   30.100  1.00 31.11  ? 238 ILE B C   1 
ATOM   4191 O  O   . ILE B  1 252 ? 58.577  -0.315  30.659  1.00 31.02  ? 238 ILE B O   1 
ATOM   4192 C  CB  . ILE B  1 252 ? 55.391  -0.871  30.861  1.00 31.82  ? 238 ILE B CB  1 
ATOM   4193 C  CG1 . ILE B  1 252 ? 54.608  0.425   31.091  1.00 31.17  ? 238 ILE B CG1 1 
ATOM   4194 C  CG2 . ILE B  1 252 ? 56.080  -1.356  32.138  1.00 31.79  ? 238 ILE B CG2 1 
ATOM   4195 C  CD1 . ILE B  1 252 ? 53.388  0.261   31.981  1.00 33.17  ? 238 ILE B CD1 1 
ATOM   4196 N  N   . TYR B  1 253 ? 57.457  1.457   29.806  1.00 22.25  ? 239 TYR B N   1 
ATOM   4197 C  CA  . TYR B  1 253 ? 58.506  2.429   30.074  1.00 21.57  ? 239 TYR B CA  1 
ATOM   4198 C  C   . TYR B  1 253 ? 58.057  3.386   31.176  1.00 18.54  ? 239 TYR B C   1 
ATOM   4199 O  O   . TYR B  1 253 ? 58.751  3.562   32.174  1.00 20.46  ? 239 TYR B O   1 
ATOM   4200 C  CB  . TYR B  1 253 ? 58.865  3.215   28.808  1.00 20.48  ? 239 TYR B CB  1 
ATOM   4201 C  CG  . TYR B  1 253 ? 59.688  4.472   29.067  1.00 20.08  ? 239 TYR B CG  1 
ATOM   4202 C  CD1 . TYR B  1 253 ? 60.962  4.394   29.618  1.00 21.60  ? 239 TYR B CD1 1 
ATOM   4203 C  CD2 . TYR B  1 253 ? 59.199  5.736   28.752  1.00 20.31  ? 239 TYR B CD2 1 
ATOM   4204 C  CE1 . TYR B  1 253 ? 61.717  5.531   29.861  1.00 21.26  ? 239 TYR B CE1 1 
ATOM   4205 C  CE2 . TYR B  1 253 ? 59.945  6.880   28.987  1.00 22.47  ? 239 TYR B CE2 1 
ATOM   4206 C  CZ  . TYR B  1 253 ? 61.207  6.778   29.543  1.00 21.15  ? 239 TYR B CZ  1 
ATOM   4207 O  OH  . TYR B  1 253 ? 61.942  7.906   29.768  1.00 22.19  ? 239 TYR B OH  1 
ATOM   4208 N  N   . ASP B  1 254 ? 56.893  4.005   30.964  1.00 17.92  ? 240 ASP B N   1 
ATOM   4209 C  CA  . ASP B  1 254 ? 56.344  5.015   31.855  1.00 18.01  ? 240 ASP B CA  1 
ATOM   4210 C  C   . ASP B  1 254 ? 54.947  4.567   32.285  1.00 17.27  ? 240 ASP B C   1 
ATOM   4211 O  O   . ASP B  1 254 ? 53.983  4.745   31.546  1.00 19.49  ? 240 ASP B O   1 
ATOM   4212 C  CB  . ASP B  1 254 ? 56.337  6.373   31.166  1.00 19.77  ? 240 ASP B CB  1 
ATOM   4213 C  CG  . ASP B  1 254 ? 55.576  7.479   31.881  1.00 20.11  ? 240 ASP B CG  1 
ATOM   4214 O  OD1 . ASP B  1 254 ? 55.236  7.284   33.066  1.00 22.08  ? 240 ASP B OD1 1 
ATOM   4215 O  OD2 . ASP B  1 254 ? 55.311  8.517   31.237  1.00 22.31  ? 240 ASP B OD2 1 
ATOM   4216 N  N   . SER B  1 255 ? 54.852  3.957   33.472  1.00 17.39  ? 241 SER B N   1 
ATOM   4217 C  CA  . SER B  1 255 ? 53.617  3.331   33.927  1.00 18.47  ? 241 SER B CA  1 
ATOM   4218 C  C   . SER B  1 255 ? 52.503  4.367   34.082  1.00 17.36  ? 241 SER B C   1 
ATOM   4219 O  O   . SER B  1 255 ? 51.364  4.116   33.697  1.00 19.26  ? 241 SER B O   1 
ATOM   4220 C  CB  . SER B  1 255 ? 53.837  2.560   35.209  1.00 20.24  ? 241 SER B CB  1 
ATOM   4221 O  OG  . SER B  1 255 ? 54.409  3.387   36.211  1.00 22.21  ? 241 SER B OG  1 
ATOM   4222 N  N   . LEU B  1 256 ? 52.834  5.531   34.650  1.00 17.09  ? 242 LEU B N   1 
ATOM   4223 C  CA  . LEU B  1 256 ? 51.849  6.582   34.858  1.00 19.05  ? 242 LEU B CA  1 
ATOM   4224 C  C   . LEU B  1 256 ? 51.314  7.050   33.507  1.00 18.80  ? 242 LEU B C   1 
ATOM   4225 O  O   . LEU B  1 256 ? 50.106  7.164   33.318  1.00 17.24  ? 242 LEU B O   1 
ATOM   4226 C  CB  . LEU B  1 256 ? 52.464  7.739   35.643  1.00 21.08  ? 242 LEU B CB  1 
ATOM   4227 C  CG  . LEU B  1 256 ? 52.869  7.430   37.088  1.00 22.93  ? 242 LEU B CG  1 
ATOM   4228 C  CD1 . LEU B  1 256 ? 53.148  8.718   37.853  1.00 23.53  ? 242 LEU B CD1 1 
ATOM   4229 C  CD2 . LEU B  1 256 ? 51.804  6.600   37.793  1.00 23.97  ? 242 LEU B CD2 1 
ATOM   4230 N  N   . GLY B  1 257 ? 52.235  7.338   32.580  1.00 19.59  ? 243 GLY B N   1 
ATOM   4231 C  CA  . GLY B  1 257 ? 51.868  7.804   31.254  1.00 18.53  ? 243 GLY B CA  1 
ATOM   4232 C  C   . GLY B  1 257 ? 51.025  6.765   30.518  1.00 18.35  ? 243 GLY B C   1 
ATOM   4233 O  O   . GLY B  1 257 ? 50.115  7.117   29.771  1.00 17.45  ? 243 GLY B O   1 
ATOM   4234 N  N   . TYR B  1 258 ? 51.345  5.484   30.737  1.00 17.95  ? 244 TYR B N   1 
ATOM   4235 C  CA  . TYR B  1 258 ? 50.611  4.391   30.120  1.00 19.14  ? 244 TYR B CA  1 
ATOM   4236 C  C   . TYR B  1 258 ? 49.145  4.462   30.545  1.00 19.34  ? 244 TYR B C   1 
ATOM   4237 O  O   . TYR B  1 258 ? 48.246  4.394   29.708  1.00 18.58  ? 244 TYR B O   1 
ATOM   4238 C  CB  . TYR B  1 258 ? 51.172  3.013   30.491  1.00 19.52  ? 244 TYR B CB  1 
ATOM   4239 C  CG  . TYR B  1 258 ? 50.267  1.873   30.041  1.00 19.91  ? 244 TYR B CG  1 
ATOM   4240 C  CD1 . TYR B  1 258 ? 50.376  1.332   28.765  1.00 19.59  ? 244 TYR B CD1 1 
ATOM   4241 C  CD2 . TYR B  1 258 ? 49.271  1.370   30.873  1.00 21.49  ? 244 TYR B CD2 1 
ATOM   4242 C  CE1 . TYR B  1 258 ? 49.542  0.311   28.339  1.00 20.80  ? 244 TYR B CE1 1 
ATOM   4243 C  CE2 . TYR B  1 258 ? 48.429  0.352   30.459  1.00 22.39  ? 244 TYR B CE2 1 
ATOM   4244 C  CZ  . TYR B  1 258 ? 48.561  -0.176  29.186  1.00 22.70  ? 244 TYR B CZ  1 
ATOM   4245 O  OH  . TYR B  1 258 ? 47.733  -1.180  28.779  1.00 22.31  ? 244 TYR B OH  1 
ATOM   4246 N  N   . MET B  1 259 ? 48.923  4.594   31.857  1.00 22.15  ? 245 MET B N   1 
ATOM   4247 C  CA  . MET B  1 259 ? 47.583  4.575   32.427  1.00 23.21  ? 245 MET B CA  1 
ATOM   4248 C  C   . MET B  1 259 ? 46.806  5.797   31.942  1.00 23.06  ? 245 MET B C   1 
ATOM   4249 O  O   . MET B  1 259 ? 45.631  5.693   31.596  1.00 27.30  ? 245 MET B O   1 
ATOM   4250 C  CB  . MET B  1 259 ? 47.637  4.568   33.960  1.00 26.05  ? 245 MET B CB  1 
ATOM   4251 C  CG  . MET B  1 259 ? 48.372  3.374   34.552  1.00 25.71  ? 245 MET B CG  1 
ATOM   4252 S  SD  . MET B  1 259 ? 47.552  1.790   34.268  1.00 29.03  ? 245 MET B SD  1 
ATOM   4253 C  CE  . MET B  1 259 ? 46.033  2.008   35.207  1.00 30.70  ? 245 MET B CE  1 
ATOM   4254 N  N   . ASN B  1 260 ? 47.478  6.954   31.923  1.00 23.89  ? 246 ASN B N   1 
ATOM   4255 C  CA  . ASN B  1 260 ? 46.868  8.197   31.476  1.00 24.06  ? 246 ASN B CA  1 
ATOM   4256 C  C   . ASN B  1 260 ? 46.411  8.041   30.025  1.00 22.81  ? 246 ASN B C   1 
ATOM   4257 O  O   . ASN B  1 260 ? 45.329  8.497   29.663  1.00 22.67  ? 246 ASN B O   1 
ATOM   4258 C  CB  . ASN B  1 260 ? 47.812  9.387   31.641  1.00 25.32  ? 246 ASN B CB  1 
ATOM   4259 C  CG  . ASN B  1 260 ? 48.082  9.727   33.089  1.00 28.11  ? 246 ASN B CG  1 
ATOM   4260 O  OD1 . ASN B  1 260 ? 47.332  9.314   33.980  1.00 29.31  ? 246 ASN B OD1 1 
ATOM   4261 N  ND2 . ASN B  1 260 ? 49.133  10.493  33.340  1.00 29.62  ? 246 ASN B ND2 1 
ATOM   4262 N  N   . THR B  1 261 ? 47.242  7.387   29.203  1.00 20.85  ? 247 THR B N   1 
ATOM   4263 C  CA  . THR B  1 261 ? 46.975  7.274   27.777  1.00 19.51  ? 247 THR B CA  1 
ATOM   4264 C  C   . THR B  1 261 ? 45.734  6.406   27.557  1.00 19.77  ? 247 THR B C   1 
ATOM   4265 O  O   . THR B  1 261 ? 44.882  6.746   26.739  1.00 21.20  ? 247 THR B O   1 
ATOM   4266 C  CB  . THR B  1 261 ? 48.196  6.734   27.026  1.00 20.52  ? 247 THR B CB  1 
ATOM   4267 O  OG1 . THR B  1 261 ? 49.190  7.756   26.997  1.00 19.28  ? 247 THR B OG1 1 
ATOM   4268 C  CG2 . THR B  1 261 ? 47.870  6.356   25.592  1.00 20.65  ? 247 THR B CG2 1 
ATOM   4269 N  N   . VAL B  1 262 ? 45.628  5.289   28.288  1.00 18.11  ? 248 VAL B N   1 
ATOM   4270 C  CA  . VAL B  1 262 ? 44.496  4.386   28.134  1.00 20.37  ? 248 VAL B CA  1 
ATOM   4271 C  C   . VAL B  1 262 ? 43.213  5.148   28.463  1.00 20.68  ? 248 VAL B C   1 
ATOM   4272 O  O   . VAL B  1 262 ? 42.226  5.049   27.736  1.00 23.64  ? 248 VAL B O   1 
ATOM   4273 C  CB  . VAL B  1 262 ? 44.614  3.111   28.993  1.00 21.17  ? 248 VAL B CB  1 
ATOM   4274 C  CG1 . VAL B  1 262 ? 43.410  2.190   28.812  1.00 21.44  ? 248 VAL B CG1 1 
ATOM   4275 C  CG2 . VAL B  1 262 ? 45.909  2.356   28.714  1.00 20.03  ? 248 VAL B CG2 1 
ATOM   4276 N  N   . GLU B  1 263 ? 43.238  5.913   29.560  1.00 21.23  ? 249 GLU B N   1 
ATOM   4277 C  CA  . GLU B  1 263 ? 42.058  6.631   30.019  1.00 21.70  ? 249 GLU B CA  1 
ATOM   4278 C  C   . GLU B  1 263 ? 41.741  7.769   29.051  1.00 22.07  ? 249 GLU B C   1 
ATOM   4279 O  O   . GLU B  1 263 ? 40.580  8.122   28.857  1.00 20.64  ? 249 GLU B O   1 
ATOM   4280 C  CB  . GLU B  1 263 ? 42.253  7.117   31.456  1.00 25.61  ? 249 GLU B CB  1 
ATOM   4281 C  CG  . GLU B  1 263 ? 42.208  5.984   32.478  1.00 27.59  ? 249 GLU B CG  1 
ATOM   4282 C  CD  . GLU B  1 263 ? 40.950  5.129   32.399  1.00 33.01  ? 249 GLU B CD  1 
ATOM   4283 O  OE1 . GLU B  1 263 ? 39.963  5.571   31.773  1.00 40.70  ? 249 GLU B OE1 1 
ATOM   4284 O  OE2 . GLU B  1 263 ? 40.959  4.007   32.945  1.00 40.47  ? 249 GLU B OE2 1 
ATOM   4285 N  N   . ARG B  1 264 ? 42.784  8.333   28.432  1.00 20.89  ? 250 ARG B N   1 
ATOM   4286 C  CA  . ARG B  1 264 ? 42.602  9.398   27.460  1.00 20.56  ? 250 ARG B CA  1 
ATOM   4287 C  C   . ARG B  1 264 ? 41.887  8.833   26.235  1.00 19.95  ? 250 ARG B C   1 
ATOM   4288 O  O   . ARG B  1 264 ? 40.954  9.445   25.717  1.00 19.94  ? 250 ARG B O   1 
ATOM   4289 C  CB  . ARG B  1 264 ? 43.945  10.033  27.080  1.00 23.46  ? 250 ARG B CB  1 
ATOM   4290 C  CG  . ARG B  1 264 ? 43.850  11.060  25.959  1.00 24.31  ? 250 ARG B CG  1 
ATOM   4291 C  CD  . ARG B  1 264 ? 45.210  11.618  25.573  1.00 26.67  ? 250 ARG B CD  1 
ATOM   4292 N  NE  . ARG B  1 264 ? 45.144  12.458  24.372  1.00 28.00  ? 250 ARG B NE  1 
ATOM   4293 C  CZ  . ARG B  1 264 ? 46.205  12.867  23.683  1.00 31.46  ? 250 ARG B CZ  1 
ATOM   4294 N  NH1 . ARG B  1 264 ? 47.422  12.530  24.073  1.00 30.63  ? 250 ARG B NH1 1 
ATOM   4295 N  NH2 . ARG B  1 264 ? 46.041  13.609  22.602  1.00 34.98  ? 250 ARG B NH2 1 
ATOM   4296 N  N   . ILE B  1 265 ? 42.340  7.656   25.786  1.00 19.62  ? 251 ILE B N   1 
ATOM   4297 C  CA  . ILE B  1 265 ? 41.730  6.965   24.662  1.00 20.77  ? 251 ILE B CA  1 
ATOM   4298 C  C   . ILE B  1 265 ? 40.269  6.649   24.989  1.00 23.19  ? 251 ILE B C   1 
ATOM   4299 O  O   . ILE B  1 265 ? 39.388  6.841   24.150  1.00 22.66  ? 251 ILE B O   1 
ATOM   4300 C  CB  . ILE B  1 265 ? 42.534  5.701   24.295  1.00 20.82  ? 251 ILE B CB  1 
ATOM   4301 C  CG1 . ILE B  1 265 ? 43.916  6.054   23.726  1.00 20.49  ? 251 ILE B CG1 1 
ATOM   4302 C  CG2 . ILE B  1 265 ? 41.743  4.813   23.335  1.00 21.50  ? 251 ILE B CG2 1 
ATOM   4303 C  CD1 . ILE B  1 265 ? 44.864  4.875   23.606  1.00 19.78  ? 251 ILE B CD1 1 
ATOM   4304 N  N   . ARG B  1 266 ? 40.009  6.168   26.211  1.00 23.80  ? 252 ARG B N   1 
ATOM   4305 C  CA  . ARG B  1 266 ? 38.653  5.829   26.620  1.00 24.84  ? 252 ARG B CA  1 
ATOM   4306 C  C   . ARG B  1 266 ? 37.756  7.052   26.425  1.00 26.70  ? 252 ARG B C   1 
ATOM   4307 O  O   . ARG B  1 266 ? 36.679  6.951   25.844  1.00 29.55  ? 252 ARG B O   1 
ATOM   4308 C  CB  . ARG B  1 266 ? 38.599  5.312   28.064  1.00 26.78  ? 252 ARG B CB  1 
ATOM   4309 C  CG  . ARG B  1 266 ? 37.320  4.559   28.413  1.00 28.77  ? 252 ARG B CG  1 
ATOM   4310 C  CD  . ARG B  1 266 ? 37.221  4.139   29.876  1.00 29.87  ? 252 ARG B CD  1 
ATOM   4311 N  NE  . ARG B  1 266 ? 38.434  3.495   30.393  1.00 28.54  ? 252 ARG B NE  1 
ATOM   4312 C  CZ  . ARG B  1 266 ? 38.853  2.273   30.083  1.00 30.74  ? 252 ARG B CZ  1 
ATOM   4313 N  NH1 . ARG B  1 266 ? 38.147  1.510   29.268  1.00 28.74  ? 252 ARG B NH1 1 
ATOM   4314 N  NH2 . ARG B  1 266 ? 39.978  1.813   30.601  1.00 33.54  ? 252 ARG B NH2 1 
ATOM   4315 N  N   . ARG B  1 267 ? 38.224  8.215   26.894  1.00 25.95  ? 253 ARG B N   1 
ATOM   4316 C  CA  . ARG B  1 267 ? 37.443  9.442   26.828  1.00 28.10  ? 253 ARG B CA  1 
ATOM   4317 C  C   . ARG B  1 267 ? 37.171  9.823   25.373  1.00 25.86  ? 253 ARG B C   1 
ATOM   4318 O  O   . ARG B  1 267 ? 36.036  10.128  25.017  1.00 22.10  ? 253 ARG B O   1 
ATOM   4319 C  CB  . ARG B  1 267 ? 38.142  10.609  27.536  1.00 29.99  ? 253 ARG B CB  1 
ATOM   4320 C  CG  . ARG B  1 267 ? 37.396  11.929  27.382  1.00 32.10  ? 253 ARG B CG  1 
ATOM   4321 C  CD  . ARG B  1 267 ? 38.133  13.138  27.939  1.00 35.69  ? 253 ARG B CD  1 
ATOM   4322 N  NE  . ARG B  1 267 ? 39.574  13.110  27.666  1.00 36.69  ? 253 ARG B NE  1 
ATOM   4323 C  CZ  . ARG B  1 267 ? 40.164  13.651  26.607  1.00 34.99  ? 253 ARG B CZ  1 
ATOM   4324 N  NH1 . ARG B  1 267 ? 39.438  14.117  25.605  1.00 36.64  ? 253 ARG B NH1 1 
ATOM   4325 N  NH2 . ARG B  1 267 ? 41.484  13.681  26.532  1.00 33.72  ? 253 ARG B NH2 1 
ATOM   4326 N  N   . ILE B  1 268 ? 38.225  9.825   24.544  1.00 25.07  ? 254 ILE B N   1 
ATOM   4327 C  CA  . ILE B  1 268 ? 38.111  10.228  23.151  1.00 26.63  ? 254 ILE B CA  1 
ATOM   4328 C  C   . ILE B  1 268 ? 37.119  9.304   22.443  1.00 26.46  ? 254 ILE B C   1 
ATOM   4329 O  O   . ILE B  1 268 ? 36.295  9.762   21.653  1.00 28.83  ? 254 ILE B O   1 
ATOM   4330 C  CB  . ILE B  1 268 ? 39.487  10.236  22.452  1.00 27.68  ? 254 ILE B CB  1 
ATOM   4331 C  CG1 . ILE B  1 268 ? 40.441  11.269  23.067  1.00 24.17  ? 254 ILE B CG1 1 
ATOM   4332 C  CG2 . ILE B  1 268 ? 39.328  10.457  20.947  1.00 28.80  ? 254 ILE B CG2 1 
ATOM   4333 C  CD1 . ILE B  1 268 ? 41.869  11.184  22.552  1.00 26.42  ? 254 ILE B CD1 1 
ATOM   4334 N  N   . ALA B  1 269 ? 37.204  8.001   22.733  1.00 24.16  ? 255 ALA B N   1 
ATOM   4335 C  CA  . ALA B  1 269 ? 36.304  7.020   22.147  1.00 24.14  ? 255 ALA B CA  1 
ATOM   4336 C  C   . ALA B  1 269 ? 34.850  7.401   22.430  1.00 27.76  ? 255 ALA B C   1 
ATOM   4337 O  O   . ALA B  1 269 ? 34.005  7.347   21.537  1.00 24.91  ? 255 ALA B O   1 
ATOM   4338 C  CB  . ALA B  1 269 ? 36.625  5.637   22.675  1.00 22.99  ? 255 ALA B CB  1 
ATOM   4339 N  N   . GLN B  1 270 ? 34.570  7.781   23.682  1.00 29.27  ? 256 GLN B N   1 
ATOM   4340 C  CA  . GLN B  1 270 ? 33.216  8.087   24.122  1.00 31.83  ? 256 GLN B CA  1 
ATOM   4341 C  C   . GLN B  1 270 ? 32.737  9.395   23.495  1.00 32.98  ? 256 GLN B C   1 
ATOM   4342 O  O   . GLN B  1 270 ? 31.617  9.471   22.996  1.00 36.17  ? 256 GLN B O   1 
ATOM   4343 C  CB  . GLN B  1 270 ? 33.141  8.154   25.649  1.00 38.43  ? 256 GLN B CB  1 
ATOM   4344 C  CG  . GLN B  1 270 ? 32.889  6.807   26.320  1.00 46.91  ? 256 GLN B CG  1 
ATOM   4345 C  CD  . GLN B  1 270 ? 32.990  6.859   27.829  1.00 57.30  ? 256 GLN B CD  1 
ATOM   4346 O  OE1 . GLN B  1 270 ? 34.062  7.095   28.397  1.00 58.22  ? 256 GLN B OE1 1 
ATOM   4347 N  NE2 . GLN B  1 270 ? 31.869  6.627   28.498  1.00 62.22  ? 256 GLN B NE2 1 
ATOM   4348 N  N   . GLU B  1 271 ? 33.597  10.419  23.517  1.00 34.09  ? 257 GLU B N   1 
ATOM   4349 C  CA  . GLU B  1 271 ? 33.215  11.754  23.084  1.00 31.27  ? 257 GLU B CA  1 
ATOM   4350 C  C   . GLU B  1 271 ? 33.055  11.797  21.564  1.00 32.95  ? 257 GLU B C   1 
ATOM   4351 O  O   . GLU B  1 271 ? 32.263  12.587  21.054  1.00 33.38  ? 257 GLU B O   1 
ATOM   4352 C  CB  . GLU B  1 271 ? 34.226  12.786  23.588  1.00 34.07  ? 257 GLU B CB  1 
ATOM   4353 C  CG  . GLU B  1 271 ? 34.214  12.940  25.106  1.00 34.64  ? 257 GLU B CG  1 
ATOM   4354 C  CD  . GLU B  1 271 ? 35.119  14.030  25.653  1.00 37.74  ? 257 GLU B CD  1 
ATOM   4355 O  OE1 . GLU B  1 271 ? 35.967  14.543  24.893  1.00 40.63  ? 257 GLU B OE1 1 
ATOM   4356 O  OE2 . GLU B  1 271 ? 34.965  14.374  26.845  1.00 38.89  ? 257 GLU B OE2 1 
ATOM   4357 N  N   . THR B  1 272 ? 33.801  10.945  20.847  1.00 30.05  ? 258 THR B N   1 
ATOM   4358 C  CA  . THR B  1 272 ? 33.784  10.954  19.390  1.00 31.18  ? 258 THR B CA  1 
ATOM   4359 C  C   . THR B  1 272 ? 32.953  9.783   18.864  1.00 28.92  ? 258 THR B C   1 
ATOM   4360 O  O   . THR B  1 272 ? 32.786  9.644   17.654  1.00 30.17  ? 258 THR B O   1 
ATOM   4361 C  CB  . THR B  1 272 ? 35.203  10.908  18.813  1.00 29.38  ? 258 THR B CB  1 
ATOM   4362 O  OG1 . THR B  1 272 ? 35.778  9.667   19.211  1.00 28.86  ? 258 THR B OG1 1 
ATOM   4363 C  CG2 . THR B  1 272 ? 36.080  12.059  19.276  1.00 30.55  ? 258 THR B CG2 1 
ATOM   4364 N  N   . LYS B  1 273 ? 32.447  8.941   19.774  1.00 32.37  ? 259 LYS B N   1 
ATOM   4365 C  CA  . LYS B  1 273 ? 31.707  7.744   19.402  1.00 34.77  ? 259 LYS B CA  1 
ATOM   4366 C  C   . LYS B  1 273 ? 32.545  6.903   18.439  1.00 33.76  ? 259 LYS B C   1 
ATOM   4367 O  O   . LYS B  1 273 ? 32.061  6.505   17.382  1.00 33.89  ? 259 LYS B O   1 
ATOM   4368 C  CB  . LYS B  1 273 ? 30.354  8.095   18.766  1.00 39.84  ? 259 LYS B CB  1 
ATOM   4369 C  CG  . LYS B  1 273 ? 29.351  8.796   19.681  1.00 43.88  ? 259 LYS B CG  1 
ATOM   4370 C  CD  . LYS B  1 273 ? 28.008  9.099   19.027  1.00 49.76  ? 259 LYS B CD  1 
ATOM   4371 C  CE  . LYS B  1 273 ? 26.902  9.302   20.024  1.00 55.71  ? 259 LYS B CE  1 
ATOM   4372 N  NZ  . LYS B  1 273 ? 27.315  10.148  21.149  1.00 58.33  ? 259 LYS B NZ  1 
ATOM   4373 N  N   . SER B  1 274 ? 33.798  6.625   18.821  1.00 28.63  ? 260 SER B N   1 
ATOM   4374 C  CA  . SER B  1 274 ? 34.720  5.882   17.973  1.00 28.60  ? 260 SER B CA  1 
ATOM   4375 C  C   . SER B  1 274 ? 34.928  4.468   18.511  1.00 29.47  ? 260 SER B C   1 
ATOM   4376 O  O   . SER B  1 274 ? 34.882  4.243   19.718  1.00 31.31  ? 260 SER B O   1 
ATOM   4377 C  CB  . SER B  1 274 ? 36.048  6.599   17.838  1.00 25.20  ? 260 SER B CB  1 
ATOM   4378 O  OG  . SER B  1 274 ? 35.893  7.876   17.235  1.00 27.91  ? 260 SER B OG  1 
ATOM   4379 N  N   . GLN B  1 275 ? 35.156  3.524   17.589  1.00 28.32  ? 261 GLN B N   1 
ATOM   4380 C  CA  . GLN B  1 275 ? 35.681  2.211   17.925  1.00 30.86  ? 261 GLN B CA  1 
ATOM   4381 C  C   . GLN B  1 275 ? 37.153  2.356   18.302  1.00 27.79  ? 261 GLN B C   1 
ATOM   4382 O  O   . GLN B  1 275 ? 37.848  3.221   17.768  1.00 27.50  ? 261 GLN B O   1 
ATOM   4383 C  CB  . GLN B  1 275 ? 35.624  1.250   16.737  1.00 32.91  ? 261 GLN B CB  1 
ATOM   4384 C  CG  . GLN B  1 275 ? 34.238  1.037   16.141  1.00 35.64  ? 261 GLN B CG  1 
ATOM   4385 C  CD  . GLN B  1 275 ? 34.300  0.268   14.839  1.00 37.02  ? 261 GLN B CD  1 
ATOM   4386 O  OE1 . GLN B  1 275 ? 34.939  -0.787  14.746  1.00 31.82  ? 261 GLN B OE1 1 
ATOM   4387 N  NE2 . GLN B  1 275 ? 33.672  0.811   13.807  1.00 34.82  ? 261 GLN B NE2 1 
ATOM   4388 N  N   . VAL B  1 276 ? 37.619  1.495   19.213  1.00 25.30  ? 262 VAL B N   1 
ATOM   4389 C  CA  . VAL B  1 276 ? 39.032  1.424   19.547  1.00 24.12  ? 262 VAL B CA  1 
ATOM   4390 C  C   . VAL B  1 276 ? 39.598  0.124   18.982  1.00 24.18  ? 262 VAL B C   1 
ATOM   4391 O  O   . VAL B  1 276 ? 39.130  -0.961  19.324  1.00 26.74  ? 262 VAL B O   1 
ATOM   4392 C  CB  . VAL B  1 276 ? 39.268  1.520   21.067  1.00 24.57  ? 262 VAL B CB  1 
ATOM   4393 C  CG1 . VAL B  1 276 ? 40.743  1.350   21.416  1.00 23.97  ? 262 VAL B CG1 1 
ATOM   4394 C  CG2 . VAL B  1 276 ? 38.717  2.821   21.641  1.00 24.00  ? 262 VAL B CG2 1 
ATOM   4395 N  N   . TRP B  1 277 ? 40.598  0.248   18.102  1.00 21.50  ? 263 TRP B N   1 
ATOM   4396 C  CA  . TRP B  1 277 ? 41.293  -0.909  17.561  1.00 22.95  ? 263 TRP B CA  1 
ATOM   4397 C  C   . TRP B  1 277 ? 42.595  -1.132  18.326  1.00 23.62  ? 263 TRP B C   1 
ATOM   4398 O  O   . TRP B  1 277 ? 43.527  -0.335  18.237  1.00 21.83  ? 263 TRP B O   1 
ATOM   4399 C  CB  . TRP B  1 277 ? 41.543  -0.739  16.056  1.00 26.03  ? 263 TRP B CB  1 
ATOM   4400 C  CG  . TRP B  1 277 ? 40.287  -0.816  15.226  1.00 25.41  ? 263 TRP B CG  1 
ATOM   4401 C  CD1 . TRP B  1 277 ? 39.002  -0.844  15.686  1.00 27.13  ? 263 TRP B CD1 1 
ATOM   4402 C  CD2 . TRP B  1 277 ? 40.197  -0.859  13.785  1.00 26.69  ? 263 TRP B CD2 1 
ATOM   4403 N  NE1 . TRP B  1 277 ? 38.121  -0.910  14.639  1.00 28.95  ? 263 TRP B NE1 1 
ATOM   4404 C  CE2 . TRP B  1 277 ? 38.823  -0.917  13.462  1.00 25.21  ? 263 TRP B CE2 1 
ATOM   4405 C  CE3 . TRP B  1 277 ? 41.135  -0.856  12.746  1.00 28.59  ? 263 TRP B CE3 1 
ATOM   4406 C  CZ2 . TRP B  1 277 ? 38.371  -0.972  12.146  1.00 25.76  ? 263 TRP B CZ2 1 
ATOM   4407 C  CZ3 . TRP B  1 277 ? 40.685  -0.910  11.445  1.00 27.83  ? 263 TRP B CZ3 1 
ATOM   4408 C  CH2 . TRP B  1 277 ? 39.322  -0.966  11.152  1.00 28.38  ? 263 TRP B CH2 1 
ATOM   4409 N  N   . PHE B  1 278 ? 42.638  -2.242  19.069  1.00 20.94  ? 264 PHE B N   1 
ATOM   4410 C  CA  . PHE B  1 278 ? 43.759  -2.556  19.938  1.00 21.46  ? 264 PHE B CA  1 
ATOM   4411 C  C   . PHE B  1 278 ? 44.960  -2.976  19.093  1.00 20.68  ? 264 PHE B C   1 
ATOM   4412 O  O   . PHE B  1 278 ? 44.828  -3.270  17.906  1.00 23.32  ? 264 PHE B O   1 
ATOM   4413 C  CB  . PHE B  1 278 ? 43.323  -3.627  20.944  1.00 22.21  ? 264 PHE B CB  1 
ATOM   4414 C  CG  . PHE B  1 278 ? 42.038  -3.280  21.686  1.00 22.77  ? 264 PHE B CG  1 
ATOM   4415 C  CD1 . PHE B  1 278 ? 41.989  -2.191  22.548  1.00 23.06  ? 264 PHE B CD1 1 
ATOM   4416 C  CD2 . PHE B  1 278 ? 40.886  -4.041  21.523  1.00 23.20  ? 264 PHE B CD2 1 
ATOM   4417 C  CE1 . PHE B  1 278 ? 40.818  -1.869  23.220  1.00 23.67  ? 264 PHE B CE1 1 
ATOM   4418 C  CE2 . PHE B  1 278 ? 39.717  -3.718  22.199  1.00 23.69  ? 264 PHE B CE2 1 
ATOM   4419 C  CZ  . PHE B  1 278 ? 39.687  -2.634  23.047  1.00 23.89  ? 264 PHE B CZ  1 
ATOM   4420 N  N   . GLY B  1 279 ? 46.135  -2.987  19.726  1.00 20.63  ? 265 GLY B N   1 
ATOM   4421 C  CA  . GLY B  1 279 ? 47.378  -3.339  19.062  1.00 22.32  ? 265 GLY B CA  1 
ATOM   4422 C  C   . GLY B  1 279 ? 47.355  -4.764  18.512  1.00 23.44  ? 265 GLY B C   1 
ATOM   4423 O  O   . GLY B  1 279 ? 47.788  -4.984  17.384  1.00 24.58  ? 265 GLY B O   1 
ATOM   4424 N  N   . HIS B  1 280 ? 46.851  -5.727  19.301  1.00 27.33  ? 266 HIS B N   1 
ATOM   4425 C  CA  A HIS B  1 280 ? 46.936  -7.135  18.956  0.70 27.34  ? 266 HIS B CA  1 
ATOM   4426 C  CA  B HIS B  1 280 ? 46.848  -7.119  18.859  0.30 27.04  ? 266 HIS B CA  1 
ATOM   4427 C  C   . HIS B  1 280 ? 45.864  -7.962  19.669  1.00 27.61  ? 266 HIS B C   1 
ATOM   4428 O  O   . HIS B  1 280 ? 46.221  -8.939  20.324  1.00 31.88  ? 266 HIS B O   1 
ATOM   4429 C  CB  A HIS B  1 280 ? 48.282  -7.712  19.416  0.70 29.22  ? 266 HIS B CB  1 
ATOM   4430 C  CB  B HIS B  1 280 ? 48.271  -7.691  18.762  0.30 27.88  ? 266 HIS B CB  1 
ATOM   4431 C  CG  A HIS B  1 280 ? 49.497  -6.961  18.972  0.70 32.62  ? 266 HIS B CG  1 
ATOM   4432 C  CG  B HIS B  1 280 ? 49.149  -7.544  19.963  0.30 28.39  ? 266 HIS B CG  1 
ATOM   4433 N  ND1 A HIS B  1 280 ? 50.297  -6.243  19.836  0.70 35.52  ? 266 HIS B ND1 1 
ATOM   4434 N  ND1 B HIS B  1 280 ? 50.377  -6.924  19.863  0.30 30.95  ? 266 HIS B ND1 1 
ATOM   4435 C  CD2 A HIS B  1 280 ? 50.076  -6.858  17.769  0.70 34.10  ? 266 HIS B CD2 1 
ATOM   4436 C  CD2 B HIS B  1 280 ? 49.027  -7.919  21.244  0.30 27.85  ? 266 HIS B CD2 1 
ATOM   4437 C  CE1 A HIS B  1 280 ? 51.306  -5.709  19.161  0.70 31.14  ? 266 HIS B CE1 1 
ATOM   4438 C  CE1 B HIS B  1 280 ? 50.967  -6.926  21.049  0.30 31.22  ? 266 HIS B CE1 1 
ATOM   4439 N  NE2 A HIS B  1 280 ? 51.190  -6.069  17.902  0.70 35.10  ? 266 HIS B NE2 1 
ATOM   4440 N  NE2 B HIS B  1 280 ? 50.166  -7.526  21.902  0.30 29.23  ? 266 HIS B NE2 1 
ATOM   4441 N  N   . ASP B  1 281 ? 44.579  -7.599  19.552  1.00 24.89  ? 267 ASP B N   1 
ATOM   4442 C  CA  . ASP B  1 281 ? 43.504  -8.386  20.142  1.00 26.03  ? 267 ASP B CA  1 
ATOM   4443 C  C   . ASP B  1 281 ? 43.037  -9.427  19.123  1.00 28.47  ? 267 ASP B C   1 
ATOM   4444 O  O   . ASP B  1 281 ? 42.471  -9.074  18.091  1.00 26.09  ? 267 ASP B O   1 
ATOM   4445 C  CB  . ASP B  1 281 ? 42.365  -7.499  20.624  1.00 25.80  ? 267 ASP B CB  1 
ATOM   4446 C  CG  . ASP B  1 281 ? 41.267  -8.210  21.403  1.00 28.38  ? 267 ASP B CG  1 
ATOM   4447 O  OD1 . ASP B  1 281 ? 40.526  -9.001  20.783  1.00 35.27  ? 267 ASP B OD1 1 
ATOM   4448 O  OD2 . ASP B  1 281 ? 41.172  -7.970  22.624  1.00 31.49  ? 267 ASP B OD2 1 
ATOM   4449 N  N   . ALA B  1 282 ? 43.274  -10.710 19.427  1.00 32.33  ? 268 ALA B N   1 
ATOM   4450 C  CA  . ALA B  1 282 ? 43.077  -11.789 18.469  1.00 32.78  ? 268 ALA B CA  1 
ATOM   4451 C  C   . ALA B  1 282 ? 41.614  -11.878 18.036  1.00 30.87  ? 268 ALA B C   1 
ATOM   4452 O  O   . ALA B  1 282 ? 41.332  -12.088 16.859  1.00 33.13  ? 268 ALA B O   1 
ATOM   4453 C  CB  . ALA B  1 282 ? 43.560  -13.101 19.057  1.00 33.97  ? 268 ALA B CB  1 
ATOM   4454 N  N   . GLU B  1 283 ? 40.688  -11.731 18.991  1.00 33.46  ? 269 GLU B N   1 
ATOM   4455 C  CA  . GLU B  1 283 ? 39.268  -11.899 18.714  1.00 35.90  ? 269 GLU B CA  1 
ATOM   4456 C  C   . GLU B  1 283 ? 38.774  -10.723 17.871  1.00 34.24  ? 269 GLU B C   1 
ATOM   4457 O  O   . GLU B  1 283 ? 37.928  -10.896 16.996  1.00 32.33  ? 269 GLU B O   1 
ATOM   4458 C  CB  . GLU B  1 283 ? 38.485  -12.073 20.018  1.00 41.06  ? 269 GLU B CB  1 
ATOM   4459 C  CG  . GLU B  1 283 ? 38.762  -13.404 20.713  1.00 51.32  ? 269 GLU B CG  1 
ATOM   4460 C  CD  . GLU B  1 283 ? 38.297  -13.487 22.156  1.00 68.18  ? 269 GLU B CD  1 
ATOM   4461 O  OE1 . GLU B  1 283 ? 38.729  -12.637 22.964  1.00 79.19  ? 269 GLU B OE1 1 
ATOM   4462 O  OE2 . GLU B  1 283 ? 37.513  -14.407 22.476  1.00 76.09  ? 269 GLU B OE2 1 
ATOM   4463 N  N   . GLN B  1 284 ? 39.324  -9.532  18.131  1.00 32.95  ? 270 GLN B N   1 
ATOM   4464 C  CA  . GLN B  1 284 ? 38.966  -8.334  17.385  1.00 30.02  ? 270 GLN B CA  1 
ATOM   4465 C  C   . GLN B  1 284 ? 39.509  -8.425  15.960  1.00 26.93  ? 270 GLN B C   1 
ATOM   4466 O  O   . GLN B  1 284 ? 38.811  -8.088  15.006  1.00 29.34  ? 270 GLN B O   1 
ATOM   4467 C  CB  . GLN B  1 284 ? 39.509  -7.075  18.062  1.00 28.48  ? 270 GLN B CB  1 
ATOM   4468 C  CG  . GLN B  1 284 ? 39.138  -5.781  17.344  1.00 27.36  ? 270 GLN B CG  1 
ATOM   4469 C  CD  . GLN B  1 284 ? 39.705  -4.547  18.014  1.00 26.72  ? 270 GLN B CD  1 
ATOM   4470 O  OE1 . GLN B  1 284 ? 40.923  -4.387  18.147  1.00 25.68  ? 270 GLN B OE1 1 
ATOM   4471 N  NE2 . GLN B  1 284 ? 38.819  -3.658  18.438  1.00 23.19  ? 270 GLN B NE2 1 
ATOM   4472 N  N   . PHE B  1 285 ? 40.767  -8.864  15.831  1.00 24.63  ? 271 PHE B N   1 
ATOM   4473 C  CA  . PHE B  1 285 ? 41.415  -8.972  14.533  1.00 28.55  ? 271 PHE B CA  1 
ATOM   4474 C  C   . PHE B  1 285 ? 40.634  -9.955  13.661  1.00 27.42  ? 271 PHE B C   1 
ATOM   4475 O  O   . PHE B  1 285 ? 40.454  -9.723  12.468  1.00 25.89  ? 271 PHE B O   1 
ATOM   4476 C  CB  . PHE B  1 285 ? 42.884  -9.383  14.696  1.00 26.12  ? 271 PHE B CB  1 
ATOM   4477 C  CG  . PHE B  1 285 ? 43.638  -9.554  13.385  1.00 31.40  ? 271 PHE B CG  1 
ATOM   4478 C  CD1 . PHE B  1 285 ? 44.063  -8.448  12.654  1.00 35.73  ? 271 PHE B CD1 1 
ATOM   4479 C  CD2 . PHE B  1 285 ? 43.927  -10.820 12.891  1.00 31.51  ? 271 PHE B CD2 1 
ATOM   4480 C  CE1 . PHE B  1 285 ? 44.750  -8.610  11.460  1.00 36.46  ? 271 PHE B CE1 1 
ATOM   4481 C  CE2 . PHE B  1 285 ? 44.614  -10.976 11.697  1.00 30.87  ? 271 PHE B CE2 1 
ATOM   4482 C  CZ  . PHE B  1 285 ? 45.023  -9.873  10.985  1.00 35.36  ? 271 PHE B CZ  1 
ATOM   4483 N  N   . LYS B  1 286 ? 40.169  -11.053 14.271  1.00 32.12  ? 272 LYS B N   1 
ATOM   4484 C  CA  . LYS B  1 286 ? 39.405  -12.069 13.561  1.00 32.16  ? 272 LYS B CA  1 
ATOM   4485 C  C   . LYS B  1 286 ? 38.178  -11.435 12.909  1.00 29.50  ? 272 LYS B C   1 
ATOM   4486 O  O   . LYS B  1 286 ? 37.813  -11.791 11.791  1.00 29.25  ? 272 LYS B O   1 
ATOM   4487 C  CB  . LYS B  1 286 ? 38.986  -13.211 14.498  1.00 38.32  ? 272 LYS B CB  1 
ATOM   4488 C  CG  . LYS B  1 286 ? 40.046  -14.280 14.754  1.00 47.44  ? 272 LYS B CG  1 
ATOM   4489 C  CD  . LYS B  1 286 ? 39.571  -15.427 15.641  1.00 55.20  ? 272 LYS B CD  1 
ATOM   4490 C  CE  . LYS B  1 286 ? 40.662  -16.024 16.483  1.00 59.44  ? 272 LYS B CE  1 
ATOM   4491 N  NZ  . LYS B  1 286 ? 40.870  -15.265 17.721  1.00 66.35  ? 272 LYS B NZ  1 
ATOM   4492 N  N   . LYS B  1 287 ? 37.552  -10.486 13.618  1.00 29.25  ? 273 LYS B N   1 
ATOM   4493 C  CA  . LYS B  1 287 ? 36.298  -9.889  13.183  1.00 29.56  ? 273 LYS B CA  1 
ATOM   4494 C  C   . LYS B  1 287 ? 36.538  -8.827  12.109  1.00 29.47  ? 273 LYS B C   1 
ATOM   4495 O  O   . LYS B  1 287 ? 35.611  -8.456  11.394  1.00 29.32  ? 273 LYS B O   1 
ATOM   4496 C  CB  . LYS B  1 287 ? 35.549  -9.293  14.382  1.00 36.87  ? 273 LYS B CB  1 
ATOM   4497 C  CG  . LYS B  1 287 ? 34.818  -10.300 15.268  1.00 43.11  ? 273 LYS B CG  1 
ATOM   4498 C  CD  . LYS B  1 287 ? 34.511  -9.796  16.673  1.00 50.80  ? 273 LYS B CD  1 
ATOM   4499 C  CE  . LYS B  1 287 ? 33.499  -10.644 17.392  1.00 57.69  ? 273 LYS B CE  1 
ATOM   4500 N  NZ  . LYS B  1 287 ? 33.630  -10.545 18.850  1.00 64.27  ? 273 LYS B NZ  1 
ATOM   4501 N  N   . PHE B  1 288 ? 37.779  -8.336  11.989  1.00 26.85  ? 274 PHE B N   1 
ATOM   4502 C  CA  . PHE B  1 288 ? 38.090  -7.300  11.013  1.00 25.81  ? 274 PHE B CA  1 
ATOM   4503 C  C   . PHE B  1 288 ? 37.872  -7.821  9.594   1.00 26.74  ? 274 PHE B C   1 
ATOM   4504 O  O   . PHE B  1 288 ? 38.093  -8.999  9.319   1.00 28.33  ? 274 PHE B O   1 
ATOM   4505 C  CB  . PHE B  1 288 ? 39.549  -6.831  11.071  1.00 27.96  ? 274 PHE B CB  1 
ATOM   4506 C  CG  . PHE B  1 288 ? 39.948  -5.970  12.259  1.00 29.11  ? 274 PHE B CG  1 
ATOM   4507 C  CD1 . PHE B  1 288 ? 39.071  -5.038  12.801  1.00 29.74  ? 274 PHE B CD1 1 
ATOM   4508 C  CD2 . PHE B  1 288 ? 41.221  -6.077  12.809  1.00 33.94  ? 274 PHE B CD2 1 
ATOM   4509 C  CE1 . PHE B  1 288 ? 39.452  -4.251  13.877  1.00 31.00  ? 274 PHE B CE1 1 
ATOM   4510 C  CE2 . PHE B  1 288 ? 41.597  -5.287  13.884  1.00 33.71  ? 274 PHE B CE2 1 
ATOM   4511 C  CZ  . PHE B  1 288 ? 40.712  -4.378  14.416  1.00 30.17  ? 274 PHE B CZ  1 
ATOM   4512 N  N   A ARG B  1 289 ? 37.438  -6.927  8.699   0.66 28.22  ? 275 ARG B N   1 
ATOM   4513 N  N   B ARG B  1 289 ? 37.454  -6.920  8.698   0.34 24.27  ? 275 ARG B N   1 
ATOM   4514 C  CA  A ARG B  1 289 ? 37.453  -7.205  7.272   0.66 29.79  ? 275 ARG B CA  1 
ATOM   4515 C  CA  B ARG B  1 289 ? 37.451  -7.191  7.269   0.34 22.78  ? 275 ARG B CA  1 
ATOM   4516 C  C   A ARG B  1 289 ? 38.858  -6.896  6.757   0.66 26.92  ? 275 ARG B C   1 
ATOM   4517 C  C   B ARG B  1 289 ? 38.848  -6.888  6.728   0.34 23.80  ? 275 ARG B C   1 
ATOM   4518 O  O   A ARG B  1 289 ? 39.292  -5.748  6.797   0.66 28.63  ? 275 ARG B O   1 
ATOM   4519 O  O   B ARG B  1 289 ? 39.265  -5.733  6.708   0.34 25.31  ? 275 ARG B O   1 
ATOM   4520 C  CB  A ARG B  1 289 ? 36.365  -6.393  6.558   0.66 35.31  ? 275 ARG B CB  1 
ATOM   4521 C  CB  B ARG B  1 289 ? 36.354  -6.361  6.589   0.34 20.96  ? 275 ARG B CB  1 
ATOM   4522 C  CG  A ARG B  1 289 ? 36.003  -6.894  5.166   0.66 39.21  ? 275 ARG B CG  1 
ATOM   4523 C  CG  B ARG B  1 289 ? 36.192  -6.610  5.095   0.34 18.86  ? 275 ARG B CG  1 
ATOM   4524 C  CD  A ARG B  1 289 ? 34.595  -6.454  4.785   0.66 43.70  ? 275 ARG B CD  1 
ATOM   4525 C  CD  B ARG B  1 289 ? 34.901  -6.015  4.546   0.34 17.16  ? 275 ARG B CD  1 
ATOM   4526 N  NE  A ARG B  1 289 ? 33.699  -6.565  5.942   0.66 51.62  ? 275 ARG B NE  1 
ATOM   4527 N  NE  B ARG B  1 289 ? 34.712  -4.602  4.892   0.34 15.30  ? 275 ARG B NE  1 
ATOM   4528 C  CZ  A ARG B  1 289 ? 33.130  -7.686  6.379   0.66 52.17  ? 275 ARG B CZ  1 
ATOM   4529 C  CZ  B ARG B  1 289 ? 33.730  -4.143  5.659   0.34 14.61  ? 275 ARG B CZ  1 
ATOM   4530 N  NH1 A ARG B  1 289 ? 33.099  -8.763  5.612   0.66 46.08  ? 275 ARG B NH1 1 
ATOM   4531 N  NH1 B ARG B  1 289 ? 32.895  -4.987  6.239   0.34 15.26  ? 275 ARG B NH1 1 
ATOM   4532 N  NH2 A ARG B  1 289 ? 32.542  -7.710  7.563   0.66 51.45  ? 275 ARG B NH2 1 
ATOM   4533 N  NH2 B ARG B  1 289 ? 33.595  -2.844  5.856   0.34 14.01  ? 275 ARG B NH2 1 
ATOM   4534 N  N   . LYS B  1 290 ? 39.571  -7.936  6.307   1.00 25.29  ? 276 LYS B N   1 
ATOM   4535 C  CA  . LYS B  1 290 ? 40.974  -7.811  5.930   1.00 26.64  ? 276 LYS B CA  1 
ATOM   4536 C  C   . LYS B  1 290 ? 41.113  -7.427  4.457   1.00 26.42  ? 276 LYS B C   1 
ATOM   4537 O  O   . LYS B  1 290 ? 40.129  -7.398  3.720   1.00 28.43  ? 276 LYS B O   1 
ATOM   4538 C  CB  . LYS B  1 290 ? 41.747  -9.118  6.149   1.00 29.20  ? 276 LYS B CB  1 
ATOM   4539 C  CG  . LYS B  1 290 ? 41.312  -9.976  7.331   1.00 34.12  ? 276 LYS B CG  1 
ATOM   4540 C  CD  . LYS B  1 290 ? 41.754  -9.475  8.699   1.00 31.42  ? 276 LYS B CD  1 
ATOM   4541 C  CE  . LYS B  1 290 ? 41.534  -10.510 9.766   1.00 31.05  ? 276 LYS B CE  1 
ATOM   4542 N  NZ  . LYS B  1 290 ? 40.117  -10.853 9.935   1.00 29.86  ? 276 LYS B NZ  1 
ATOM   4543 N  N   . SER B  1 291 ? 42.366  -7.182  4.043   1.00 22.92  ? 277 SER B N   1 
ATOM   4544 C  CA  . SER B  1 291 ? 42.689  -6.650  2.727   1.00 24.89  ? 277 SER B CA  1 
ATOM   4545 C  C   . SER B  1 291 ? 42.282  -7.629  1.626   1.00 25.23  ? 277 SER B C   1 
ATOM   4546 O  O   . SER B  1 291 ? 42.082  -7.222  0.483   1.00 25.53  ? 277 SER B O   1 
ATOM   4547 C  CB  . SER B  1 291 ? 44.162  -6.300  2.628   1.00 20.70  ? 277 SER B CB  1 
ATOM   4548 O  OG  . SER B  1 291 ? 44.982  -7.425  2.911   1.00 24.46  ? 277 SER B OG  1 
ATOM   4549 N  N   . THR B  1 292 ? 42.158  -8.916  1.976   1.00 26.67  ? 278 THR B N   1 
ATOM   4550 C  CA  . THR B  1 292 ? 41.840  -9.950  1.001   1.00 30.72  ? 278 THR B CA  1 
ATOM   4551 C  C   . THR B  1 292 ? 40.329  -9.999  0.753   1.00 30.39  ? 278 THR B C   1 
ATOM   4552 O  O   . THR B  1 292 ? 39.880  -10.681 -0.166  1.00 29.80  ? 278 THR B O   1 
ATOM   4553 C  CB  . THR B  1 292 ? 42.386  -11.307 1.455   1.00 31.37  ? 278 THR B CB  1 
ATOM   4554 O  OG1 . THR B  1 292 ? 42.088  -11.413 2.845   1.00 39.68  ? 278 THR B OG1 1 
ATOM   4555 C  CG2 . THR B  1 292 ? 43.885  -11.446 1.249   1.00 30.02  ? 278 THR B CG2 1 
ATOM   4556 N  N   . GLU B  1 293 ? 39.544  -9.270  1.559   1.00 28.12  ? 279 GLU B N   1 
ATOM   4557 C  CA  . GLU B  1 293 ? 38.092  -9.323  1.455   1.00 29.50  ? 279 GLU B CA  1 
ATOM   4558 C  C   . GLU B  1 293 ? 37.507  -7.933  1.196   1.00 28.54  ? 279 GLU B C   1 
ATOM   4559 O  O   . GLU B  1 293 ? 36.401  -7.823  0.670   1.00 24.88  ? 279 GLU B O   1 
ATOM   4560 C  CB  . GLU B  1 293 ? 37.453  -9.929  2.706   1.00 35.53  ? 279 GLU B CB  1 
ATOM   4561 C  CG  . GLU B  1 293 ? 37.911  -11.355 3.000   1.00 42.14  ? 279 GLU B CG  1 
ATOM   4562 C  CD  . GLU B  1 293 ? 36.969  -12.145 3.894   1.00 49.14  ? 279 GLU B CD  1 
ATOM   4563 O  OE1 . GLU B  1 293 ? 36.613  -11.640 4.980   1.00 53.74  ? 279 GLU B OE1 1 
ATOM   4564 O  OE2 . GLU B  1 293 ? 36.594  -13.271 3.502   1.00 58.51  ? 279 GLU B OE2 1 
ATOM   4565 N  N   . GLY B  1 294 ? 38.228  -6.875  1.589   1.00 26.68  ? 280 GLY B N   1 
ATOM   4566 C  CA  . GLY B  1 294 ? 37.771  -5.519  1.319   1.00 25.92  ? 280 GLY B CA  1 
ATOM   4567 C  C   . GLY B  1 294 ? 38.326  -4.489  2.301   1.00 25.49  ? 280 GLY B C   1 
ATOM   4568 O  O   . GLY B  1 294 ? 39.486  -4.559  2.702   1.00 27.43  ? 280 GLY B O   1 
ATOM   4569 N  N   . TYR B  1 295 ? 37.466  -3.534  2.681   1.00 24.31  ? 281 TYR B N   1 
ATOM   4570 C  CA  . TYR B  1 295 ? 37.899  -2.310  3.333   1.00 24.05  ? 281 TYR B CA  1 
ATOM   4571 C  C   . TYR B  1 295 ? 36.732  -1.646  4.063   1.00 25.35  ? 281 TYR B C   1 
ATOM   4572 O  O   . TYR B  1 295 ? 35.616  -2.163  4.069   1.00 25.31  ? 281 TYR B O   1 
ATOM   4573 C  CB  . TYR B  1 295 ? 38.469  -1.391  2.248   1.00 25.55  ? 281 TYR B CB  1 
ATOM   4574 C  CG  . TYR B  1 295 ? 37.646  -1.414  0.965   1.00 25.79  ? 281 TYR B CG  1 
ATOM   4575 C  CD1 . TYR B  1 295 ? 36.401  -0.798  0.894   1.00 26.32  ? 281 TYR B CD1 1 
ATOM   4576 C  CD2 . TYR B  1 295 ? 38.104  -2.074  -0.168  1.00 26.81  ? 281 TYR B CD2 1 
ATOM   4577 C  CE1 . TYR B  1 295 ? 35.642  -0.830  -0.265  1.00 27.31  ? 281 TYR B CE1 1 
ATOM   4578 C  CE2 . TYR B  1 295 ? 37.355  -2.112  -1.333  1.00 26.45  ? 281 TYR B CE2 1 
ATOM   4579 C  CZ  . TYR B  1 295 ? 36.121  -1.489  -1.383  1.00 25.46  ? 281 TYR B CZ  1 
ATOM   4580 O  OH  . TYR B  1 295 ? 35.382  -1.529  -2.533  1.00 28.39  ? 281 TYR B OH  1 
ATOM   4581 N  N   . TYR B  1 296 ? 37.022  -0.487  4.667   1.00 25.67  ? 282 TYR B N   1 
ATOM   4582 C  CA  . TYR B  1 296 ? 36.040  0.319   5.376   1.00 24.31  ? 282 TYR B CA  1 
ATOM   4583 C  C   . TYR B  1 296 ? 35.953  1.693   4.711   1.00 26.29  ? 282 TYR B C   1 
ATOM   4584 O  O   . TYR B  1 296 ? 36.978  2.327   4.464   1.00 28.14  ? 282 TYR B O   1 
ATOM   4585 C  CB  . TYR B  1 296 ? 36.442  0.454   6.850   1.00 25.03  ? 282 TYR B CB  1 
ATOM   4586 C  CG  . TYR B  1 296 ? 36.511  -0.854  7.631   1.00 25.64  ? 282 TYR B CG  1 
ATOM   4587 C  CD1 . TYR B  1 296 ? 37.599  -1.714  7.505   1.00 24.14  ? 282 TYR B CD1 1 
ATOM   4588 C  CD2 . TYR B  1 296 ? 35.491  -1.227  8.501   1.00 28.51  ? 282 TYR B CD2 1 
ATOM   4589 C  CE1 . TYR B  1 296 ? 37.664  -2.905  8.212   1.00 25.04  ? 282 TYR B CE1 1 
ATOM   4590 C  CE2 . TYR B  1 296 ? 35.545  -2.415  9.213   1.00 26.66  ? 282 TYR B CE2 1 
ATOM   4591 C  CZ  . TYR B  1 296 ? 36.634  -3.257  9.067   1.00 27.68  ? 282 TYR B CZ  1 
ATOM   4592 O  OH  . TYR B  1 296 ? 36.688  -4.429  9.769   1.00 25.78  ? 282 TYR B OH  1 
ATOM   4593 N  N   A GLU B  1 297 ? 34.725  2.141   4.427   0.60 26.03  ? 283 GLU B N   1 
ATOM   4594 N  N   B GLU B  1 297 ? 34.721  2.126   4.411   0.40 22.91  ? 283 GLU B N   1 
ATOM   4595 C  CA  A GLU B  1 297 ? 34.499  3.455   3.845   0.60 29.07  ? 283 GLU B CA  1 
ATOM   4596 C  CA  B GLU B  1 297 ? 34.468  3.441   3.843   0.40 22.48  ? 283 GLU B CA  1 
ATOM   4597 C  C   A GLU B  1 297 ? 33.727  4.326   4.852   0.60 27.87  ? 283 GLU B C   1 
ATOM   4598 C  C   B GLU B  1 297 ? 33.967  4.385   4.951   0.40 21.19  ? 283 GLU B C   1 
ATOM   4599 O  O   A GLU B  1 297 ? 33.511  3.833   5.984   0.60 22.77  ? 283 GLU B O   1 
ATOM   4600 O  O   B GLU B  1 297 ? 33.438  5.462   4.593   0.40 16.13  ? 283 GLU B O   1 
ATOM   4601 C  CB  A GLU B  1 297 ? 33.734  3.345   2.525   0.60 29.45  ? 283 GLU B CB  1 
ATOM   4602 C  CB  B GLU B  1 297 ? 33.447  3.369   2.705   0.40 21.41  ? 283 GLU B CB  1 
ATOM   4603 C  CG  A GLU B  1 297 ? 34.419  2.448   1.498   0.60 31.26  ? 283 GLU B CG  1 
ATOM   4604 C  CG  B GLU B  1 297 ? 33.996  2.727   1.435   0.40 21.68  ? 283 GLU B CG  1 
ATOM   4605 C  CD  A GLU B  1 297 ? 33.721  2.414   0.150   0.60 33.42  ? 283 GLU B CD  1 
ATOM   4606 C  CD  B GLU B  1 297 ? 33.108  2.894   0.214   0.40 21.15  ? 283 GLU B CD  1 
ATOM   4607 O  OE1 A GLU B  1 297 ? 32.682  3.096   0.011   0.60 32.08  ? 283 GLU B OE1 1 
ATOM   4608 O  OE1 B GLU B  1 297 ? 31.944  3.322   0.374   0.40 19.02  ? 283 GLU B OE1 1 
ATOM   4609 O  OE2 A GLU B  1 297 ? 34.212  1.711   -0.761  0.60 35.51  ? 283 GLU B OE2 1 
ATOM   4610 O  OE2 B GLU B  1 297 ? 33.592  2.612   -0.904  0.40 21.93  ? 283 GLU B OE2 1 
ATOM   4611 N  N   . ALA C  1 22  ? -44.566 -14.075 13.137  1.00 42.66  ? 8   ALA C N   1 
ATOM   4612 C  CA  . ALA C  1 22  ? -45.228 -15.043 12.227  1.00 45.56  ? 8   ALA C CA  1 
ATOM   4613 C  C   . ALA C  1 22  ? -44.937 -14.680 10.771  1.00 43.74  ? 8   ALA C C   1 
ATOM   4614 O  O   . ALA C  1 22  ? -44.993 -15.543 9.898   1.00 56.19  ? 8   ALA C O   1 
ATOM   4615 C  CB  . ALA C  1 22  ? -46.716 -15.089 12.510  1.00 42.70  ? 8   ALA C CB  1 
ATOM   4616 N  N   . ARG C  1 23  ? -44.622 -13.402 10.519  1.00 48.62  ? 9   ARG C N   1 
ATOM   4617 C  CA  . ARG C  1 23  ? -44.344 -12.924 9.171   1.00 49.47  ? 9   ARG C CA  1 
ATOM   4618 C  C   . ARG C  1 23  ? -43.375 -11.741 9.246   1.00 43.78  ? 9   ARG C C   1 
ATOM   4619 O  O   . ARG C  1 23  ? -43.725 -10.609 8.914   1.00 40.81  ? 9   ARG C O   1 
ATOM   4620 C  CB  . ARG C  1 23  ? -45.681 -12.629 8.478   1.00 50.66  ? 9   ARG C CB  1 
ATOM   4621 C  CG  . ARG C  1 23  ? -45.617 -11.753 7.236   1.00 61.77  ? 9   ARG C CG  1 
ATOM   4622 C  CD  . ARG C  1 23  ? -47.027 -11.299 6.886   1.00 64.75  ? 9   ARG C CD  1 
ATOM   4623 N  NE  . ARG C  1 23  ? -47.108 -10.516 5.650   1.00 50.54  ? 9   ARG C NE  1 
ATOM   4624 C  CZ  . ARG C  1 23  ? -48.247 -10.196 5.054   1.00 46.98  ? 9   ARG C CZ  1 
ATOM   4625 N  NH1 . ARG C  1 23  ? -48.219 -9.534  3.917   1.00 56.84  ? 9   ARG C NH1 1 
ATOM   4626 N  NH2 . ARG C  1 23  ? -49.408 -10.550 5.577   1.00 46.30  ? 9   ARG C NH2 1 
ATOM   4627 N  N   . PRO C  1 24  ? -42.119 -11.982 9.691   1.00 37.88  ? 10  PRO C N   1 
ATOM   4628 C  CA  . PRO C  1 24  ? -41.108 -10.929 9.846   1.00 38.85  ? 10  PRO C CA  1 
ATOM   4629 C  C   . PRO C  1 24  ? -40.395 -10.494 8.566   1.00 31.34  ? 10  PRO C C   1 
ATOM   4630 O  O   . PRO C  1 24  ? -40.514 -11.147 7.532   1.00 29.78  ? 10  PRO C O   1 
ATOM   4631 C  CB  . PRO C  1 24  ? -40.089 -11.569 10.821  1.00 41.47  ? 10  PRO C CB  1 
ATOM   4632 C  CG  . PRO C  1 24  ? -40.714 -12.882 11.260  1.00 42.72  ? 10  PRO C CG  1 
ATOM   4633 C  CD  . PRO C  1 24  ? -41.619 -13.294 10.122  1.00 40.99  ? 10  PRO C CD  1 
ATOM   4634 N  N   . LYS C  1 25  ? -39.627 -9.399  8.674   1.00 28.39  ? 11  LYS C N   1 
ATOM   4635 C  CA  . LYS C  1 25  ? -38.717 -8.954  7.627   1.00 28.53  ? 11  LYS C CA  1 
ATOM   4636 C  C   . LYS C  1 25  ? -37.308 -8.808  8.206   1.00 27.06  ? 11  LYS C C   1 
ATOM   4637 O  O   . LYS C  1 25  ? -37.104 -8.057  9.157   1.00 29.09  ? 11  LYS C O   1 
ATOM   4638 C  CB  . LYS C  1 25  ? -39.193 -7.627  7.018   1.00 28.72  ? 11  LYS C CB  1 
ATOM   4639 C  CG  . LYS C  1 25  ? -40.343 -7.730  6.017   1.00 30.40  ? 11  LYS C CG  1 
ATOM   4640 C  CD  . LYS C  1 25  ? -40.830 -6.383  5.488   1.00 32.74  ? 11  LYS C CD  1 
ATOM   4641 C  CE  . LYS C  1 25  ? -42.007 -6.494  4.562   1.00 29.33  ? 11  LYS C CE  1 
ATOM   4642 N  NZ  . LYS C  1 25  ? -43.215 -6.970  5.244   1.00 29.67  ? 11  LYS C NZ  1 
ATOM   4643 N  N   . LEU C  1 26  ? -36.339 -9.531  7.623   1.00 25.42  ? 12  LEU C N   1 
ATOM   4644 C  CA  . LEU C  1 26  ? -34.953 -9.497  8.076   1.00 25.72  ? 12  LEU C CA  1 
ATOM   4645 C  C   . LEU C  1 26  ? -34.133 -8.608  7.140   1.00 22.25  ? 12  LEU C C   1 
ATOM   4646 O  O   . LEU C  1 26  ? -34.158 -8.795  5.926   1.00 21.41  ? 12  LEU C O   1 
ATOM   4647 C  CB  . LEU C  1 26  ? -34.399 -10.923 8.148   1.00 26.53  ? 12  LEU C CB  1 
ATOM   4648 C  CG  . LEU C  1 26  ? -32.986 -11.078 8.723   1.00 26.70  ? 12  LEU C CG  1 
ATOM   4649 C  CD1 . LEU C  1 26  ? -32.841 -12.402 9.462   1.00 27.48  ? 12  LEU C CD1 1 
ATOM   4650 C  CD2 . LEU C  1 26  ? -31.925 -10.968 7.634   1.00 27.26  ? 12  LEU C CD2 1 
ATOM   4651 N  N   . TYR C  1 27  ? -33.410 -7.636  7.720   1.00 24.49  ? 13  TYR C N   1 
ATOM   4652 C  CA  . TYR C  1 27  ? -32.628 -6.671  6.957   1.00 22.96  ? 13  TYR C CA  1 
ATOM   4653 C  C   . TYR C  1 27  ? -31.139 -6.846  7.258   1.00 24.58  ? 13  TYR C C   1 
ATOM   4654 O  O   . TYR C  1 27  ? -30.753 -7.059  8.406   1.00 25.82  ? 13  TYR C O   1 
ATOM   4655 C  CB  . TYR C  1 27  ? -33.011 -5.220  7.281   1.00 24.39  ? 13  TYR C CB  1 
ATOM   4656 C  CG  . TYR C  1 27  ? -34.448 -4.804  6.985   1.00 25.74  ? 13  TYR C CG  1 
ATOM   4657 C  CD1 . TYR C  1 27  ? -35.491 -5.157  7.835   1.00 28.52  ? 13  TYR C CD1 1 
ATOM   4658 C  CD2 . TYR C  1 27  ? -34.757 -4.025  5.874   1.00 25.46  ? 13  TYR C CD2 1 
ATOM   4659 C  CE1 . TYR C  1 27  ? -36.797 -4.771  7.577   1.00 28.50  ? 13  TYR C CE1 1 
ATOM   4660 C  CE2 . TYR C  1 27  ? -36.059 -3.632  5.606   1.00 27.14  ? 13  TYR C CE2 1 
ATOM   4661 C  CZ  . TYR C  1 27  ? -37.082 -4.004  6.461   1.00 29.13  ? 13  TYR C CZ  1 
ATOM   4662 O  OH  . TYR C  1 27  ? -38.369 -3.625  6.213   1.00 31.15  ? 13  TYR C OH  1 
ATOM   4663 N  N   . VAL C  1 28  ? -30.312 -6.733  6.208   1.00 23.33  ? 14  VAL C N   1 
ATOM   4664 C  CA  . VAL C  1 28  ? -28.862 -6.677  6.334   1.00 22.92  ? 14  VAL C CA  1 
ATOM   4665 C  C   . VAL C  1 28  ? -28.423 -5.229  6.118   1.00 25.50  ? 14  VAL C C   1 
ATOM   4666 O  O   . VAL C  1 28  ? -28.710 -4.643  5.076   1.00 23.83  ? 14  VAL C O   1 
ATOM   4667 C  CB  . VAL C  1 28  ? -28.159 -7.622  5.336   1.00 24.53  ? 14  VAL C CB  1 
ATOM   4668 C  CG1 . VAL C  1 28  ? -26.647 -7.418  5.320   1.00 24.01  ? 14  VAL C CG1 1 
ATOM   4669 C  CG2 . VAL C  1 28  ? -28.501 -9.084  5.596   1.00 27.64  ? 14  VAL C CG2 1 
ATOM   4670 N  N   . MET C  1 29  ? -27.720 -4.664  7.109   1.00 22.88  ? 15  MET C N   1 
ATOM   4671 C  CA  . MET C  1 29  ? -27.330 -3.263  7.085   1.00 25.01  ? 15  MET C CA  1 
ATOM   4672 C  C   . MET C  1 29  ? -25.811 -3.149  6.945   1.00 28.22  ? 15  MET C C   1 
ATOM   4673 O  O   . MET C  1 29  ? -25.064 -3.702  7.750   1.00 28.08  ? 15  MET C O   1 
ATOM   4674 C  CB  . MET C  1 29  ? -27.814 -2.548  8.355   1.00 27.27  ? 15  MET C CB  1 
ATOM   4675 C  CG  . MET C  1 29  ? -29.311 -2.265  8.364   1.00 26.62  ? 15  MET C CG  1 
ATOM   4676 S  SD  . MET C  1 29  ? -29.927 -1.563  9.909   1.00 28.96  ? 15  MET C SD  1 
ATOM   4677 C  CE  . MET C  1 29  ? -29.627 -2.920  11.052  1.00 29.57  ? 15  MET C CE  1 
ATOM   4678 N  N   . ASP C  1 30  ? -25.373 -2.416  5.912   1.00 24.17  ? 16  ASP C N   1 
ATOM   4679 C  CA  . ASP C  1 30  ? -23.962 -2.227  5.607   1.00 28.23  ? 16  ASP C CA  1 
ATOM   4680 C  C   . ASP C  1 30  ? -23.393 -1.121  6.497   1.00 27.22  ? 16  ASP C C   1 
ATOM   4681 O  O   . ASP C  1 30  ? -23.781 0.038   6.372   1.00 27.82  ? 16  ASP C O   1 
ATOM   4682 C  CB  . ASP C  1 30  ? -23.769 -1.930  4.126   1.00 30.12  ? 16  ASP C CB  1 
ATOM   4683 C  CG  . ASP C  1 30  ? -22.328 -1.761  3.666   1.00 32.34  ? 16  ASP C CG  1 
ATOM   4684 O  OD1 . ASP C  1 30  ? -21.441 -1.657  4.538   1.00 30.05  ? 16  ASP C OD1 1 
ATOM   4685 O  OD2 . ASP C  1 30  ? -22.105 -1.750  2.437   1.00 32.32  ? 16  ASP C OD2 1 
ATOM   4686 N  N   . ASN C  1 31  ? -22.460 -1.490  7.386   1.00 25.89  ? 17  ASN C N   1 
ATOM   4687 C  CA  . ASN C  1 31  ? -21.911 -0.559  8.360   1.00 26.23  ? 17  ASN C CA  1 
ATOM   4688 C  C   . ASN C  1 31  ? -20.424 -0.322  8.089   1.00 27.33  ? 17  ASN C C   1 
ATOM   4689 O  O   . ASN C  1 31  ? -19.659 -0.067  9.015   1.00 30.82  ? 17  ASN C O   1 
ATOM   4690 C  CB  . ASN C  1 31  ? -22.127 -1.040  9.794   1.00 26.34  ? 17  ASN C CB  1 
ATOM   4691 C  CG  . ASN C  1 31  ? -23.582 -1.282  10.125  1.00 28.14  ? 17  ASN C CG  1 
ATOM   4692 O  OD1 . ASN C  1 31  ? -23.949 -2.387  10.542  1.00 30.56  ? 17  ASN C OD1 1 
ATOM   4693 N  ND2 . ASN C  1 31  ? -24.419 -0.266  9.966   1.00 28.32  ? 17  ASN C ND2 1 
ATOM   4694 N  N   . GLY C  1 32  ? -20.016 -0.411  6.817   1.00 27.42  ? 18  GLY C N   1 
ATOM   4695 C  CA  . GLY C  1 32  ? -18.676 -0.005  6.413   1.00 28.02  ? 18  GLY C CA  1 
ATOM   4696 C  C   . GLY C  1 32  ? -17.711 -1.183  6.277   1.00 26.29  ? 18  GLY C C   1 
ATOM   4697 O  O   . GLY C  1 32  ? -18.130 -2.338  6.217   1.00 25.58  ? 18  GLY C O   1 
ATOM   4698 N  N   . ARG C  1 33  ? -16.410 -0.863  6.226   1.00 29.74  ? 19  ARG C N   1 
ATOM   4699 C  CA  . ARG C  1 33  ? -15.361 -1.838  5.967   1.00 32.00  ? 19  ARG C CA  1 
ATOM   4700 C  C   . ARG C  1 33  ? -14.262 -1.714  7.020   1.00 30.16  ? 19  ARG C C   1 
ATOM   4701 O  O   . ARG C  1 33  ? -14.038 -0.636  7.565   1.00 31.81  ? 19  ARG C O   1 
ATOM   4702 C  CB  . ARG C  1 33  ? -14.745 -1.609  4.580   1.00 32.43  ? 19  ARG C CB  1 
ATOM   4703 C  CG  . ARG C  1 33  ? -15.746 -1.641  3.434   1.00 32.72  ? 19  ARG C CG  1 
ATOM   4704 C  CD  . ARG C  1 33  ? -16.376 -3.008  3.254   1.00 33.56  ? 19  ARG C CD  1 
ATOM   4705 N  NE  . ARG C  1 33  ? -17.416 -2.958  2.221   1.00 40.43  ? 19  ARG C NE  1 
ATOM   4706 C  CZ  . ARG C  1 33  ? -18.721 -2.911  2.467   1.00 40.66  ? 19  ARG C CZ  1 
ATOM   4707 N  NH1 . ARG C  1 33  ? -19.164 -2.913  3.713   1.00 36.21  ? 19  ARG C NH1 1 
ATOM   4708 N  NH2 . ARG C  1 33  ? -19.579 -2.853  1.464   1.00 38.28  ? 19  ARG C NH2 1 
ATOM   4709 N  N   . MET C  1 34  ? -13.576 -2.832  7.291   1.00 29.55  ? 20  MET C N   1 
ATOM   4710 C  CA  . MET C  1 34  ? -12.409 -2.832  8.159   1.00 31.39  ? 20  MET C CA  1 
ATOM   4711 C  C   . MET C  1 34  ? -11.258 -3.533  7.437   1.00 28.05  ? 20  MET C C   1 
ATOM   4712 O  O   . MET C  1 34  ? -11.489 -4.331  6.532   1.00 29.55  ? 20  MET C O   1 
ATOM   4713 C  CB  . MET C  1 34  ? -12.724 -3.527  9.490   1.00 37.23  ? 20  MET C CB  1 
ATOM   4714 C  CG  . MET C  1 34  ? -11.646 -3.374  10.546  1.00 47.07  ? 20  MET C CG  1 
ATOM   4715 S  SD  . MET C  1 34  ? -12.279 -3.663  12.213  1.00 50.40  ? 20  MET C SD  1 
ATOM   4716 C  CE  . MET C  1 34  ? -13.816 -2.732  12.150  1.00 37.83  ? 20  MET C CE  1 
ATOM   4717 N  N   . ARG C  1 35  ? -10.021 -3.203  7.828   1.00 27.48  ? 21  ARG C N   1 
ATOM   4718 C  CA  . ARG C  1 35  ? -8.831  -3.854  7.299   1.00 30.00  ? 21  ARG C CA  1 
ATOM   4719 C  C   . ARG C  1 35  ? -8.014  -4.419  8.460   1.00 27.48  ? 21  ARG C C   1 
ATOM   4720 O  O   . ARG C  1 35  ? -7.936  -3.792  9.513   1.00 29.23  ? 21  ARG C O   1 
ATOM   4721 C  CB  . ARG C  1 35  ? -7.972  -2.863  6.501   1.00 30.32  ? 21  ARG C CB  1 
ATOM   4722 C  CG  . ARG C  1 35  ? -8.490  -2.525  5.109   1.00 36.10  ? 21  ARG C CG  1 
ATOM   4723 C  CD  . ARG C  1 35  ? -7.735  -1.370  4.457   1.00 39.01  ? 21  ARG C CD  1 
ATOM   4724 N  NE  . ARG C  1 35  ? -8.224  -0.078  4.951   1.00 48.16  ? 21  ARG C NE  1 
ATOM   4725 C  CZ  . ARG C  1 35  ? -7.472  0.960   5.299   1.00 49.10  ? 21  ARG C CZ  1 
ATOM   4726 N  NH1 . ARG C  1 35  ? -6.172  0.957   5.060   1.00 53.82  ? 21  ARG C NH1 1 
ATOM   4727 N  NH2 . ARG C  1 35  ? -8.039  2.016   5.856   1.00 45.55  ? 21  ARG C NH2 1 
ATOM   4728 N  N   . MET C  1 36  ? -7.404  -5.597  8.262   1.00 30.60  ? 22  MET C N   1 
ATOM   4729 C  CA  . MET C  1 36  ? -6.471  -6.136  9.241   1.00 30.37  ? 22  MET C CA  1 
ATOM   4730 C  C   . MET C  1 36  ? -5.610  -7.236  8.622   1.00 27.55  ? 22  MET C C   1 
ATOM   4731 O  O   . MET C  1 36  ? -5.937  -7.775  7.567   1.00 27.31  ? 22  MET C O   1 
ATOM   4732 C  CB  . MET C  1 36  ? -7.206  -6.690  10.469  1.00 27.24  ? 22  MET C CB  1 
ATOM   4733 C  CG  . MET C  1 36  ? -7.945  -7.996  10.237  1.00 29.56  ? 22  MET C CG  1 
ATOM   4734 S  SD  . MET C  1 36  ? -8.902  -8.494  11.687  1.00 31.69  ? 22  MET C SD  1 
ATOM   4735 C  CE  . MET C  1 36  ? -9.540  -10.096 11.174  1.00 29.62  ? 22  MET C CE  1 
ATOM   4736 N  N   . ASP C  1 37  ? -4.506  -7.552  9.313   1.00 31.41  ? 23  ASP C N   1 
ATOM   4737 C  CA  . ASP C  1 37  ? -3.589  -8.617  8.935   1.00 29.71  ? 23  ASP C CA  1 
ATOM   4738 C  C   . ASP C  1 37  ? -4.382  -9.910  8.761   1.00 32.83  ? 23  ASP C C   1 
ATOM   4739 O  O   . ASP C  1 37  ? -5.185  -10.263 9.623   1.00 32.25  ? 23  ASP C O   1 
ATOM   4740 C  CB  . ASP C  1 37  ? -2.476  -8.736  9.970   1.00 27.72  ? 23  ASP C CB  1 
ATOM   4741 C  CG  . ASP C  1 37  ? -1.357  -9.716  9.650   1.00 28.34  ? 23  ASP C CG  1 
ATOM   4742 O  OD1 . ASP C  1 37  ? -1.572  -10.597 8.792   1.00 32.97  ? 23  ASP C OD1 1 
ATOM   4743 O  OD2 . ASP C  1 37  ? -0.268  -9.572  10.251  1.00 31.29  ? 23  ASP C OD2 1 
ATOM   4744 N  N   . LYS C  1 38  ? -4.153  -10.610 7.644   1.00 30.05  ? 24  LYS C N   1 
ATOM   4745 C  CA  . LYS C  1 38  ? -4.932  -11.795 7.324   1.00 35.05  ? 24  LYS C CA  1 
ATOM   4746 C  C   . LYS C  1 38  ? -4.640  -12.889 8.350   1.00 30.48  ? 24  LYS C C   1 
ATOM   4747 O  O   . LYS C  1 38  ? -5.420  -13.827 8.497   1.00 32.93  ? 24  LYS C O   1 
ATOM   4748 C  CB  . LYS C  1 38  ? -4.648  -12.314 5.909   1.00 37.23  ? 24  LYS C CB  1 
ATOM   4749 C  CG  . LYS C  1 38  ? -5.810  -13.097 5.300   1.00 40.46  ? 24  LYS C CG  1 
ATOM   4750 C  CD  . LYS C  1 38  ? -5.449  -14.049 4.167   1.00 43.40  ? 24  LYS C CD  1 
ATOM   4751 C  CE  . LYS C  1 38  ? -6.574  -14.995 3.852   1.00 47.32  ? 24  LYS C CE  1 
ATOM   4752 N  NZ  . LYS C  1 38  ? -6.419  -15.633 2.542   1.00 50.10  ? 24  LYS C NZ  1 
ATOM   4753 N  N   . ASN C  1 39  ? -3.506  -12.764 9.051   1.00 33.65  ? 25  ASN C N   1 
ATOM   4754 C  CA  . ASN C  1 39  ? -3.115  -13.741 10.056  1.00 35.08  ? 25  ASN C CA  1 
ATOM   4755 C  C   . ASN C  1 39  ? -4.082  -13.683 11.241  1.00 31.97  ? 25  ASN C C   1 
ATOM   4756 O  O   . ASN C  1 39  ? -4.284  -14.691 11.913  1.00 34.41  ? 25  ASN C O   1 
ATOM   4757 C  CB  . ASN C  1 39  ? -1.659  -13.579 10.488  1.00 34.13  ? 25  ASN C CB  1 
ATOM   4758 C  CG  . ASN C  1 39  ? -0.684  -14.183 9.505   1.00 35.76  ? 25  ASN C CG  1 
ATOM   4759 O  OD1 . ASN C  1 39  ? -0.873  -15.322 9.061   1.00 34.73  ? 25  ASN C OD1 1 
ATOM   4760 N  ND2 . ASN C  1 39  ? 0.360   -13.443 9.155   1.00 40.73  ? 25  ASN C ND2 1 
ATOM   4761 N  N   . TRP C  1 40  ? -4.671  -12.506 11.502  1.00 28.78  ? 26  TRP C N   1 
ATOM   4762 C  CA  . TRP C  1 40  ? -5.730  -12.396 12.497  1.00 32.27  ? 26  TRP C CA  1 
ATOM   4763 C  C   . TRP C  1 40  ? -6.909  -13.272 12.072  1.00 32.31  ? 26  TRP C C   1 
ATOM   4764 O  O   . TRP C  1 40  ? -7.511  -13.957 12.896  1.00 31.84  ? 26  TRP C O   1 
ATOM   4765 C  CB  . TRP C  1 40  ? -6.213  -10.947 12.679  1.00 30.21  ? 26  TRP C CB  1 
ATOM   4766 C  CG  . TRP C  1 40  ? -5.241  -9.958  13.275  1.00 29.82  ? 26  TRP C CG  1 
ATOM   4767 C  CD1 . TRP C  1 40  ? -4.875  -8.771  12.707  1.00 31.10  ? 26  TRP C CD1 1 
ATOM   4768 C  CD2 . TRP C  1 40  ? -4.585  -10.000 14.564  1.00 34.19  ? 26  TRP C CD2 1 
ATOM   4769 N  NE1 . TRP C  1 40  ? -4.008  -8.095  13.522  1.00 31.98  ? 26  TRP C NE1 1 
ATOM   4770 C  CE2 . TRP C  1 40  ? -3.817  -8.817  14.670  1.00 32.62  ? 26  TRP C CE2 1 
ATOM   4771 C  CE3 . TRP C  1 40  ? -4.557  -10.914 15.625  1.00 33.55  ? 26  TRP C CE3 1 
ATOM   4772 C  CZ2 . TRP C  1 40  ? -3.037  -8.531  15.789  1.00 35.05  ? 26  TRP C CZ2 1 
ATOM   4773 C  CZ3 . TRP C  1 40  ? -3.789  -10.626 16.733  1.00 32.30  ? 26  TRP C CZ3 1 
ATOM   4774 C  CH2 . TRP C  1 40  ? -3.044  -9.450  16.813  1.00 36.04  ? 26  TRP C CH2 1 
ATOM   4775 N  N   . MET C  1 41  ? -7.236  -13.218 10.774  1.00 33.61  ? 27  MET C N   1 
ATOM   4776 C  CA  . MET C  1 41  ? -8.433  -13.841 10.232  1.00 32.05  ? 27  MET C CA  1 
ATOM   4777 C  C   . MET C  1 41  ? -8.209  -15.341 10.059  1.00 29.63  ? 27  MET C C   1 
ATOM   4778 O  O   . MET C  1 41  ? -9.047  -16.145 10.460  1.00 28.96  ? 27  MET C O   1 
ATOM   4779 C  CB  . MET C  1 41  ? -8.786  -13.236 8.868   1.00 37.42  ? 27  MET C CB  1 
ATOM   4780 C  CG  . MET C  1 41  ? -10.114 -13.705 8.300   1.00 45.00  ? 27  MET C CG  1 
ATOM   4781 S  SD  . MET C  1 41  ? -11.422 -12.488 8.554   1.00 61.23  ? 27  MET C SD  1 
ATOM   4782 C  CE  . MET C  1 41  ? -10.739 -11.113 7.616   1.00 58.18  ? 27  MET C CE  1 
ATOM   4783 N  N   . ILE C  1 42  ? -7.082  -15.697 9.428   1.00 26.73  ? 28  ILE C N   1 
ATOM   4784 C  CA  . ILE C  1 42  ? -6.710  -17.087 9.210   1.00 27.97  ? 28  ILE C CA  1 
ATOM   4785 C  C   . ILE C  1 42  ? -5.311  -17.313 9.786   1.00 32.74  ? 28  ILE C C   1 
ATOM   4786 O  O   . ILE C  1 42  ? -4.321  -16.815 9.251   1.00 32.79  ? 28  ILE C O   1 
ATOM   4787 C  CB  . ILE C  1 42  ? -6.781  -17.457 7.714   1.00 30.27  ? 28  ILE C CB  1 
ATOM   4788 C  CG1 . ILE C  1 42  ? -8.180  -17.234 7.128   1.00 29.19  ? 28  ILE C CG1 1 
ATOM   4789 C  CG2 . ILE C  1 42  ? -6.304  -18.891 7.487   1.00 33.45  ? 28  ILE C CG2 1 
ATOM   4790 C  CD1 . ILE C  1 42  ? -9.228  -18.218 7.618   1.00 30.80  ? 28  ILE C CD1 1 
ATOM   4791 N  N   . ALA C  1 43  ? -5.246  -18.074 10.884  1.00 31.36  ? 29  ALA C N   1 
ATOM   4792 C  CA  . ALA C  1 43  ? -3.998  -18.332 11.586  1.00 33.57  ? 29  ALA C CA  1 
ATOM   4793 C  C   . ALA C  1 43  ? -2.953  -18.921 10.638  1.00 30.98  ? 29  ALA C C   1 
ATOM   4794 O  O   . ALA C  1 43  ? -3.235  -19.873 9.914   1.00 28.18  ? 29  ALA C O   1 
ATOM   4795 C  CB  . ALA C  1 43  ? -4.257  -19.257 12.758  1.00 34.58  ? 29  ALA C CB  1 
ATOM   4796 N  N   . MET C  1 44  ? -1.746  -18.338 10.658  1.00 33.69  ? 30  MET C N   1 
ATOM   4797 C  CA  . MET C  1 44  ? -0.597  -18.875 9.941   1.00 34.15  ? 30  MET C CA  1 
ATOM   4798 C  C   . MET C  1 44  ? -0.995  -19.251 8.515   1.00 31.30  ? 30  MET C C   1 
ATOM   4799 O  O   . MET C  1 44  ? -0.726  -20.365 8.072   1.00 32.09  ? 30  MET C O   1 
ATOM   4800 C  CB  . MET C  1 44  ? -0.051  -20.126 10.642  1.00 35.12  ? 30  MET C CB  1 
ATOM   4801 C  CG  . MET C  1 44  ? 0.388   -19.898 12.078  1.00 37.59  ? 30  MET C CG  1 
ATOM   4802 S  SD  . MET C  1 44  ? 1.811   -18.801 12.232  1.00 37.28  ? 30  MET C SD  1 
ATOM   4803 C  CE  . MET C  1 44  ? 2.919   -19.491 10.994  1.00 36.08  ? 30  MET C CE  1 
ATOM   4804 N  N   . HIS C  1 45  ? -1.620  -18.311 7.797   1.00 33.15  ? 31  HIS C N   1 
ATOM   4805 C  CA  . HIS C  1 45  ? -2.167  -18.599 6.480   1.00 34.63  ? 31  HIS C CA  1 
ATOM   4806 C  C   . HIS C  1 45  ? -1.037  -18.824 5.473   1.00 37.75  ? 31  HIS C C   1 
ATOM   4807 O  O   . HIS C  1 45  ? -1.189  -19.617 4.546   1.00 38.72  ? 31  HIS C O   1 
ATOM   4808 C  CB  . HIS C  1 45  ? -3.135  -17.496 6.032   1.00 36.29  ? 31  HIS C CB  1 
ATOM   4809 C  CG  . HIS C  1 45  ? -2.477  -16.240 5.559   1.00 34.74  ? 31  HIS C CG  1 
ATOM   4810 N  ND1 . HIS C  1 45  ? -1.786  -15.389 6.395   1.00 35.47  ? 31  HIS C ND1 1 
ATOM   4811 C  CD2 . HIS C  1 45  ? -2.398  -15.698 4.335   1.00 32.43  ? 31  HIS C CD2 1 
ATOM   4812 C  CE1 . HIS C  1 45  ? -1.318  -14.367 5.692   1.00 33.94  ? 31  HIS C CE1 1 
ATOM   4813 N  NE2 . HIS C  1 45  ? -1.680  -14.533 4.439   1.00 31.70  ? 31  HIS C NE2 1 
ATOM   4814 N  N   . ASN C  1 46  ? 0.094   -18.130 5.662   1.00 38.60  ? 32  ASN C N   1 
ATOM   4815 C  CA  . ASN C  1 46  ? 1.201   -18.182 4.715   1.00 41.48  ? 32  ASN C CA  1 
ATOM   4816 C  C   . ASN C  1 46  ? 2.529   -18.289 5.468   1.00 37.41  ? 32  ASN C C   1 
ATOM   4817 O  O   . ASN C  1 46  ? 3.259   -17.306 5.586   1.00 37.05  ? 32  ASN C O   1 
ATOM   4818 C  CB  . ASN C  1 46  ? 1.171   -16.980 3.772   1.00 39.92  ? 32  ASN C CB  1 
ATOM   4819 C  CG  . ASN C  1 46  ? 2.321   -16.969 2.791   1.00 40.97  ? 32  ASN C CG  1 
ATOM   4820 O  OD1 . ASN C  1 46  ? 2.634   -18.001 2.187   1.00 40.31  ? 32  ASN C OD1 1 
ATOM   4821 N  ND2 . ASN C  1 46  ? 2.962   -15.821 2.621   1.00 42.91  ? 32  ASN C ND2 1 
ATOM   4822 N  N   . PRO C  1 47  ? 2.886   -19.483 6.000   1.00 33.74  ? 33  PRO C N   1 
ATOM   4823 C  CA  . PRO C  1 47  ? 4.128   -19.658 6.759   1.00 35.11  ? 33  PRO C CA  1 
ATOM   4824 C  C   . PRO C  1 47  ? 5.397   -19.538 5.915   1.00 36.09  ? 33  PRO C C   1 
ATOM   4825 O  O   . PRO C  1 47  ? 5.435   -20.003 4.779   1.00 31.53  ? 33  PRO C O   1 
ATOM   4826 C  CB  . PRO C  1 47  ? 4.001   -21.076 7.361   1.00 37.32  ? 33  PRO C CB  1 
ATOM   4827 C  CG  . PRO C  1 47  ? 2.547   -21.465 7.169   1.00 37.81  ? 33  PRO C CG  1 
ATOM   4828 C  CD  . PRO C  1 47  ? 2.091   -20.719 5.929   1.00 36.41  ? 33  PRO C CD  1 
ATOM   4829 N  N   . ALA C  1 48  ? 6.437   -18.932 6.501   1.00 37.30  ? 34  ALA C N   1 
ATOM   4830 C  CA  . ALA C  1 48  ? 7.748   -18.835 5.875   1.00 33.81  ? 34  ALA C CA  1 
ATOM   4831 C  C   . ALA C  1 48  ? 8.370   -20.225 5.741   1.00 39.43  ? 34  ALA C C   1 
ATOM   4832 O  O   . ALA C  1 48  ? 8.081   -21.115 6.542   1.00 30.86  ? 34  ALA C O   1 
ATOM   4833 C  CB  . ALA C  1 48  ? 8.631   -17.911 6.687   1.00 34.88  ? 34  ALA C CB  1 
ATOM   4834 N  N   . THR C  1 49  ? 9.220   -20.395 4.717   1.00 33.02  ? 35  THR C N   1 
ATOM   4835 C  CA  . THR C  1 49  ? 9.932   -21.643 4.477   1.00 32.34  ? 35  THR C CA  1 
ATOM   4836 C  C   . THR C  1 49  ? 11.392  -21.317 4.132   1.00 34.98  ? 35  THR C C   1 
ATOM   4837 O  O   . THR C  1 49  ? 11.760  -20.145 4.058   1.00 33.97  ? 35  THR C O   1 
ATOM   4838 C  CB  . THR C  1 49  ? 9.213   -22.453 3.394   1.00 39.25  ? 35  THR C CB  1 
ATOM   4839 O  OG1 . THR C  1 49  ? 9.268   -21.692 2.190   1.00 43.38  ? 35  THR C OG1 1 
ATOM   4840 C  CG2 . THR C  1 49  ? 7.767   -22.757 3.753   1.00 40.38  ? 35  THR C CG2 1 
ATOM   4841 N  N   A ILE C  1 50  ? 12.214  -22.362 3.957   0.70 33.99  ? 36  ILE C N   1 
ATOM   4842 N  N   B ILE C  1 50  ? 12.211  -22.352 3.902   0.30 31.76  ? 36  ILE C N   1 
ATOM   4843 C  CA  A ILE C  1 50  ? 13.650  -22.203 3.766   0.70 38.17  ? 36  ILE C CA  1 
ATOM   4844 C  CA  B ILE C  1 50  ? 13.655  -22.181 3.797   0.30 31.97  ? 36  ILE C CA  1 
ATOM   4845 C  C   A ILE C  1 50  ? 13.904  -21.263 2.591   0.70 33.82  ? 36  ILE C C   1 
ATOM   4846 C  C   B ILE C  1 50  ? 14.006  -21.420 2.517   0.30 31.78  ? 36  ILE C C   1 
ATOM   4847 O  O   A ILE C  1 50  ? 14.798  -20.422 2.649   0.70 33.01  ? 36  ILE C O   1 
ATOM   4848 O  O   B ILE C  1 50  ? 15.099  -20.868 2.415   0.30 32.26  ? 36  ILE C O   1 
ATOM   4849 C  CB  A ILE C  1 50  ? 14.349  -23.564 3.563   0.70 42.45  ? 36  ILE C CB  1 
ATOM   4850 C  CB  B ILE C  1 50  ? 14.388  -23.537 3.890   0.30 30.60  ? 36  ILE C CB  1 
ATOM   4851 C  CG1 A ILE C  1 50  ? 15.844  -23.398 3.259   0.70 47.94  ? 36  ILE C CG1 1 
ATOM   4852 C  CG1 B ILE C  1 50  ? 15.912  -23.359 3.975   0.30 29.23  ? 36  ILE C CG1 1 
ATOM   4853 C  CG2 A ILE C  1 50  ? 13.649  -24.382 2.477   0.70 41.74  ? 36  ILE C CG2 1 
ATOM   4854 C  CG2 B ILE C  1 50  ? 13.991  -24.463 2.741   0.30 30.20  ? 36  ILE C CG2 1 
ATOM   4855 C  CD1 A ILE C  1 50  ? 16.584  -22.495 4.230   0.70 53.25  ? 36  ILE C CD1 1 
ATOM   4856 C  CD1 B ILE C  1 50  ? 16.692  -24.661 4.047   0.30 28.07  ? 36  ILE C CD1 1 
ATOM   4857 N  N   . HIS C  1 51  ? 13.085  -21.391 1.544   1.00 33.96  ? 37  HIS C N   1 
ATOM   4858 C  CA  . HIS C  1 51  ? 13.309  -20.664 0.301   1.00 35.52  ? 37  HIS C CA  1 
ATOM   4859 C  C   . HIS C  1 51  ? 12.346  -19.482 0.197   1.00 39.89  ? 37  HIS C C   1 
ATOM   4860 O  O   . HIS C  1 51  ? 12.196  -18.893 -0.871  1.00 42.26  ? 37  HIS C O   1 
ATOM   4861 C  CB  . HIS C  1 51  ? 13.223  -21.603 -0.909  1.00 28.88  ? 37  HIS C CB  1 
ATOM   4862 C  CG  . HIS C  1 51  ? 14.255  -22.684 -0.884  1.00 31.15  ? 37  HIS C CG  1 
ATOM   4863 N  ND1 . HIS C  1 51  ? 14.006  -23.991 -1.246  1.00 34.23  ? 37  HIS C ND1 1 
ATOM   4864 C  CD2 . HIS C  1 51  ? 15.541  -22.643 -0.509  1.00 32.32  ? 37  HIS C CD2 1 
ATOM   4865 C  CE1 . HIS C  1 51  ? 15.116  -24.704 -1.100  1.00 32.62  ? 37  HIS C CE1 1 
ATOM   4866 N  NE2 . HIS C  1 51  ? 16.060  -23.905 -0.653  1.00 33.61  ? 37  HIS C NE2 1 
ATOM   4867 N  N   . ASN C  1 52  ? 11.700  -19.141 1.318   1.00 40.33  ? 38  ASN C N   1 
ATOM   4868 C  CA  . ASN C  1 52  ? 10.872  -17.948 1.412   1.00 39.43  ? 38  ASN C CA  1 
ATOM   4869 C  C   . ASN C  1 52  ? 10.827  -17.527 2.879   1.00 43.16  ? 38  ASN C C   1 
ATOM   4870 O  O   . ASN C  1 52  ? 9.757   -17.462 3.481   1.00 49.49  ? 38  ASN C O   1 
ATOM   4871 C  CB  . ASN C  1 52  ? 9.492   -18.171 0.794   1.00 41.18  ? 38  ASN C CB  1 
ATOM   4872 C  CG  . ASN C  1 52  ? 8.652   -16.913 0.748   1.00 41.60  ? 38  ASN C CG  1 
ATOM   4873 O  OD1 . ASN C  1 52  ? 9.164   -15.834 0.431   1.00 47.66  ? 38  ASN C OD1 1 
ATOM   4874 N  ND2 . ASN C  1 52  ? 7.369   -17.027 1.063   1.00 40.46  ? 38  ASN C ND2 1 
ATOM   4875 N  N   . PRO C  1 53  ? 11.997  -17.218 3.488   1.00 46.74  ? 39  PRO C N   1 
ATOM   4876 C  CA  . PRO C  1 53  ? 12.103  -17.045 4.939   1.00 47.85  ? 39  PRO C CA  1 
ATOM   4877 C  C   . PRO C  1 53  ? 11.397  -15.805 5.479   1.00 43.91  ? 39  PRO C C   1 
ATOM   4878 O  O   . PRO C  1 53  ? 11.084  -15.731 6.666   1.00 42.58  ? 39  PRO C O   1 
ATOM   4879 C  CB  . PRO C  1 53  ? 13.626  -16.947 5.148   1.00 44.15  ? 39  PRO C CB  1 
ATOM   4880 C  CG  . PRO C  1 53  ? 14.125  -16.319 3.867   1.00 42.24  ? 39  PRO C CG  1 
ATOM   4881 C  CD  . PRO C  1 53  ? 13.277  -16.985 2.797   1.00 44.74  ? 39  PRO C CD  1 
ATOM   4882 N  N   . ASN C  1 54  ? 11.179  -14.826 4.596   1.00 40.83  ? 40  ASN C N   1 
ATOM   4883 C  CA  . ASN C  1 54  ? 10.664  -13.527 4.995   1.00 43.25  ? 40  ASN C CA  1 
ATOM   4884 C  C   . ASN C  1 54  ? 9.249   -13.342 4.445   1.00 41.14  ? 40  ASN C C   1 
ATOM   4885 O  O   . ASN C  1 54  ? 8.865   -12.232 4.084   1.00 44.11  ? 40  ASN C O   1 
ATOM   4886 C  CB  . ASN C  1 54  ? 11.606  -12.404 4.567   1.00 50.74  ? 40  ASN C CB  1 
ATOM   4887 C  CG  . ASN C  1 54  ? 12.838  -12.311 5.438   1.00 52.36  ? 40  ASN C CG  1 
ATOM   4888 O  OD1 . ASN C  1 54  ? 12.724  -12.164 6.661   1.00 51.65  ? 40  ASN C OD1 1 
ATOM   4889 N  ND2 . ASN C  1 54  ? 14.018  -12.382 4.838   1.00 53.13  ? 40  ASN C ND2 1 
ATOM   4890 N  N   . ALA C  1 55  ? 8.478   -14.438 4.399   1.00 39.58  ? 41  ALA C N   1 
ATOM   4891 C  CA  . ALA C  1 55  ? 7.109   -14.417 3.901   1.00 39.50  ? 41  ALA C CA  1 
ATOM   4892 C  C   . ALA C  1 55  ? 6.374   -13.190 4.442   1.00 35.16  ? 41  ALA C C   1 
ATOM   4893 O  O   . ALA C  1 55  ? 6.540   -12.834 5.605   1.00 31.95  ? 41  ALA C O   1 
ATOM   4894 C  CB  . ALA C  1 55  ? 6.401   -15.702 4.287   1.00 44.10  ? 41  ALA C CB  1 
ATOM   4895 N  N   . GLN C  1 56  ? 5.559   -12.549 3.592   1.00 37.81  ? 42  GLN C N   1 
ATOM   4896 C  CA  . GLN C  1 56  ? 4.865   -11.327 3.979   1.00 42.86  ? 42  GLN C CA  1 
ATOM   4897 C  C   . GLN C  1 56  ? 3.363   -11.599 4.089   1.00 36.07  ? 42  GLN C C   1 
ATOM   4898 O  O   . GLN C  1 56  ? 2.851   -12.533 3.476   1.00 37.46  ? 42  GLN C O   1 
ATOM   4899 C  CB  . GLN C  1 56  ? 5.203   -10.187 3.012   1.00 44.48  ? 42  GLN C CB  1 
ATOM   4900 C  CG  . GLN C  1 56  ? 4.508   -10.254 1.656   1.00 44.81  ? 42  GLN C CG  1 
ATOM   4901 C  CD  . GLN C  1 56  ? 5.052   -9.228  0.684   1.00 47.28  ? 42  GLN C CD  1 
ATOM   4902 O  OE1 . GLN C  1 56  ? 6.263   -9.144  0.448   1.00 48.69  ? 42  GLN C OE1 1 
ATOM   4903 N  NE2 . GLN C  1 56  ? 4.166   -8.418  0.123   1.00 43.41  ? 42  GLN C NE2 1 
ATOM   4904 N  N   . THR C  1 57  ? 2.668   -10.786 4.897   1.00 39.47  ? 43  THR C N   1 
ATOM   4905 C  CA  . THR C  1 57  ? 1.225   -10.907 5.067   1.00 43.56  ? 43  THR C CA  1 
ATOM   4906 C  C   . THR C  1 57  ? 0.528   -9.883  4.172   1.00 43.50  ? 43  THR C C   1 
ATOM   4907 O  O   . THR C  1 57  ? 1.174   -9.216  3.366   1.00 47.34  ? 43  THR C O   1 
ATOM   4908 C  CB  . THR C  1 57  ? 0.828   -10.728 6.535   1.00 38.05  ? 43  THR C CB  1 
ATOM   4909 O  OG1 . THR C  1 57  ? -0.499  -11.238 6.648   1.00 37.03  ? 43  THR C OG1 1 
ATOM   4910 C  CG2 . THR C  1 57  ? 0.873   -9.279  6.989   1.00 39.31  ? 43  THR C CG2 1 
ATOM   4911 N  N   . GLU C  1 58  ? -0.797  -9.773  4.330   1.00 41.22  ? 44  GLU C N   1 
ATOM   4912 C  CA  . GLU C  1 58  ? -1.615  -8.850  3.557   1.00 44.19  ? 44  GLU C CA  1 
ATOM   4913 C  C   . GLU C  1 58  ? -2.609  -8.155  4.486   1.00 42.93  ? 44  GLU C C   1 
ATOM   4914 O  O   . GLU C  1 58  ? -3.068  -8.752  5.458   1.00 43.06  ? 44  GLU C O   1 
ATOM   4915 C  CB  . GLU C  1 58  ? -2.301  -9.622  2.428   1.00 48.69  ? 44  GLU C CB  1 
ATOM   4916 C  CG  . GLU C  1 58  ? -2.705  -11.041 2.823   1.00 57.58  ? 44  GLU C CG  1 
ATOM   4917 C  CD  . GLU C  1 58  ? -2.455  -12.078 1.741   1.00 67.83  ? 44  GLU C CD  1 
ATOM   4918 O  OE1 . GLU C  1 58  ? -1.273  -12.270 1.381   1.00 65.24  ? 44  GLU C OE1 1 
ATOM   4919 O  OE2 . GLU C  1 58  ? -3.432  -12.691 1.261   1.00 78.26  ? 44  GLU C OE2 1 
ATOM   4920 N  N   . PHE C  1 59  ? -2.914  -6.884  4.186   1.00 38.45  ? 45  PHE C N   1 
ATOM   4921 C  CA  . PHE C  1 59  ? -3.914  -6.124  4.922   1.00 41.94  ? 45  PHE C CA  1 
ATOM   4922 C  C   . PHE C  1 59  ? -5.250  -6.268  4.192   1.00 44.33  ? 45  PHE C C   1 
ATOM   4923 O  O   . PHE C  1 59  ? -5.483  -5.587  3.196   1.00 47.57  ? 45  PHE C O   1 
ATOM   4924 C  CB  . PHE C  1 59  ? -3.465  -4.661  5.033   1.00 42.59  ? 45  PHE C CB  1 
ATOM   4925 C  CG  . PHE C  1 59  ? -3.788  -3.964  6.349   1.00 46.28  ? 45  PHE C CG  1 
ATOM   4926 C  CD1 . PHE C  1 59  ? -3.536  -4.589  7.565   1.00 41.49  ? 45  PHE C CD1 1 
ATOM   4927 C  CD2 . PHE C  1 59  ? -4.327  -2.682  6.368   1.00 46.29  ? 45  PHE C CD2 1 
ATOM   4928 C  CE1 . PHE C  1 59  ? -3.820  -3.952  8.762   1.00 43.86  ? 45  PHE C CE1 1 
ATOM   4929 C  CE2 . PHE C  1 59  ? -4.612  -2.050  7.569   1.00 52.04  ? 45  PHE C CE2 1 
ATOM   4930 C  CZ  . PHE C  1 59  ? -4.359  -2.687  8.762   1.00 50.95  ? 45  PHE C CZ  1 
ATOM   4931 N  N   . VAL C  1 60  ? -6.120  -7.162  4.686   1.00 40.20  ? 46  VAL C N   1 
ATOM   4932 C  CA  . VAL C  1 60  ? -7.307  -7.572  3.947   1.00 38.87  ? 46  VAL C CA  1 
ATOM   4933 C  C   . VAL C  1 60  ? -8.521  -6.779  4.432   1.00 36.50  ? 46  VAL C C   1 
ATOM   4934 O  O   . VAL C  1 60  ? -8.713  -6.606  5.633   1.00 30.98  ? 46  VAL C O   1 
ATOM   4935 C  CB  . VAL C  1 60  ? -7.548  -9.093  4.051   1.00 44.71  ? 46  VAL C CB  1 
ATOM   4936 C  CG1 . VAL C  1 60  ? -6.414  -9.888  3.413   1.00 48.48  ? 46  VAL C CG1 1 
ATOM   4937 C  CG2 . VAL C  1 60  ? -7.777  -9.552  5.488   1.00 48.94  ? 46  VAL C CG2 1 
ATOM   4938 N  N   . GLU C  1 61  ? -9.333  -6.301  3.478   1.00 33.25  ? 47  GLU C N   1 
ATOM   4939 C  CA  . GLU C  1 61  ? -10.549 -5.561  3.781   1.00 30.86  ? 47  GLU C CA  1 
ATOM   4940 C  C   . GLU C  1 61  ? -11.708 -6.545  3.937   1.00 28.40  ? 47  GLU C C   1 
ATOM   4941 O  O   . GLU C  1 61  ? -11.747 -7.570  3.260   1.00 29.81  ? 47  GLU C O   1 
ATOM   4942 C  CB  . GLU C  1 61  ? -10.854 -4.537  2.685   1.00 31.73  ? 47  GLU C CB  1 
ATOM   4943 C  CG  . GLU C  1 61  ? -11.884 -3.487  3.096   1.00 35.78  ? 47  GLU C CG  1 
ATOM   4944 C  CD  . GLU C  1 61  ? -12.136 -2.404  2.060   1.00 40.77  ? 47  GLU C CD  1 
ATOM   4945 O  OE1 . GLU C  1 61  ? -12.572 -2.748  0.942   1.00 39.55  ? 47  GLU C OE1 1 
ATOM   4946 O  OE2 . GLU C  1 61  ? -11.899 -1.217  2.373   1.00 44.91  ? 47  GLU C OE2 1 
ATOM   4947 N  N   . PHE C  1 62  ? -12.651 -6.224  4.833   1.00 28.20  ? 48  PHE C N   1 
ATOM   4948 C  CA  . PHE C  1 62  ? -13.798 -7.086  5.082   1.00 28.69  ? 48  PHE C CA  1 
ATOM   4949 C  C   . PHE C  1 62  ? -14.989 -6.237  5.531   1.00 27.72  ? 48  PHE C C   1 
ATOM   4950 O  O   . PHE C  1 62  ? -14.814 -5.177  6.127   1.00 28.79  ? 48  PHE C O   1 
ATOM   4951 C  CB  . PHE C  1 62  ? -13.436 -8.183  6.092   1.00 30.21  ? 48  PHE C CB  1 
ATOM   4952 C  CG  . PHE C  1 62  ? -13.010 -7.698  7.470   1.00 29.29  ? 48  PHE C CG  1 
ATOM   4953 C  CD1 . PHE C  1 62  ? -13.956 -7.421  8.451   1.00 29.33  ? 48  PHE C CD1 1 
ATOM   4954 C  CD2 . PHE C  1 62  ? -11.665 -7.537  7.785   1.00 32.35  ? 48  PHE C CD2 1 
ATOM   4955 C  CE1 . PHE C  1 62  ? -13.565 -6.990  9.708   1.00 32.37  ? 48  PHE C CE1 1 
ATOM   4956 C  CE2 . PHE C  1 62  ? -11.279 -7.103  9.044   1.00 32.95  ? 48  PHE C CE2 1 
ATOM   4957 C  CZ  . PHE C  1 62  ? -12.229 -6.831  10.002  1.00 30.41  ? 48  PHE C CZ  1 
ATOM   4958 N  N   . PRO C  1 63  ? -16.236 -6.681  5.241   1.00 27.33  ? 49  PRO C N   1 
ATOM   4959 C  CA  . PRO C  1 63  ? -17.441 -5.929  5.599   1.00 28.96  ? 49  PRO C CA  1 
ATOM   4960 C  C   . PRO C  1 63  ? -17.828 -6.006  7.073   1.00 31.11  ? 49  PRO C C   1 
ATOM   4961 O  O   . PRO C  1 63  ? -17.669 -7.045  7.711   1.00 30.53  ? 49  PRO C O   1 
ATOM   4962 C  CB  . PRO C  1 63  ? -18.512 -6.590  4.713   1.00 29.92  ? 49  PRO C CB  1 
ATOM   4963 C  CG  . PRO C  1 63  ? -18.056 -8.028  4.613   1.00 29.48  ? 49  PRO C CG  1 
ATOM   4964 C  CD  . PRO C  1 63  ? -16.542 -7.932  4.528   1.00 27.97  ? 49  PRO C CD  1 
ATOM   4965 N  N   . ILE C  1 64  ? -18.341 -4.886  7.592   1.00 28.52  ? 50  ILE C N   1 
ATOM   4966 C  CA  . ILE C  1 64  ? -19.004 -4.843  8.884   1.00 29.76  ? 50  ILE C CA  1 
ATOM   4967 C  C   . ILE C  1 64  ? -20.505 -4.705  8.638   1.00 28.44  ? 50  ILE C C   1 
ATOM   4968 O  O   . ILE C  1 64  ? -20.928 -3.763  7.972   1.00 28.47  ? 50  ILE C O   1 
ATOM   4969 C  CB  . ILE C  1 64  ? -18.465 -3.671  9.729   1.00 28.67  ? 50  ILE C CB  1 
ATOM   4970 C  CG1 . ILE C  1 64  ? -16.936 -3.666  9.797   1.00 29.82  ? 50  ILE C CG1 1 
ATOM   4971 C  CG2 . ILE C  1 64  ? -19.099 -3.667  11.120  1.00 31.21  ? 50  ILE C CG2 1 
ATOM   4972 C  CD1 . ILE C  1 64  ? -16.336 -4.944  10.352  1.00 30.11  ? 50  ILE C CD1 1 
ATOM   4973 N  N   . TYR C  1 65  ? -21.311 -5.637  9.165   1.00 25.09  ? 51  TYR C N   1 
ATOM   4974 C  CA  . TYR C  1 65  ? -22.752 -5.555  8.973   1.00 25.68  ? 51  TYR C CA  1 
ATOM   4975 C  C   . TYR C  1 65  ? -23.489 -5.920  10.260  1.00 27.05  ? 51  TYR C C   1 
ATOM   4976 O  O   . TYR C  1 65  ? -22.936 -6.558  11.155  1.00 27.82  ? 51  TYR C O   1 
ATOM   4977 C  CB  . TYR C  1 65  ? -23.236 -6.418  7.800   1.00 25.15  ? 51  TYR C CB  1 
ATOM   4978 C  CG  . TYR C  1 65  ? -23.261 -7.926  8.015   1.00 23.63  ? 51  TYR C CG  1 
ATOM   4979 C  CD1 . TYR C  1 65  ? -22.131 -8.706  7.787   1.00 27.01  ? 51  TYR C CD1 1 
ATOM   4980 C  CD2 . TYR C  1 65  ? -24.428 -8.578  8.402   1.00 27.03  ? 51  TYR C CD2 1 
ATOM   4981 C  CE1 . TYR C  1 65  ? -22.155 -10.081 7.963   1.00 24.25  ? 51  TYR C CE1 1 
ATOM   4982 C  CE2 . TYR C  1 65  ? -24.465 -9.951  8.583   1.00 27.33  ? 51  TYR C CE2 1 
ATOM   4983 C  CZ  . TYR C  1 65  ? -23.326 -10.705 8.360   1.00 26.37  ? 51  TYR C CZ  1 
ATOM   4984 O  OH  . TYR C  1 65  ? -23.366 -12.059 8.536   1.00 26.33  ? 51  TYR C OH  1 
ATOM   4985 N  N   . THR C  1 66  ? -24.747 -5.471  10.327  1.00 23.96  ? 52  THR C N   1 
ATOM   4986 C  CA  . THR C  1 66  ? -25.664 -5.792  11.407  1.00 24.42  ? 52  THR C CA  1 
ATOM   4987 C  C   . THR C  1 66  ? -26.962 -6.303  10.785  1.00 24.69  ? 52  THR C C   1 
ATOM   4988 O  O   . THR C  1 66  ? -27.211 -6.086  9.600   1.00 23.45  ? 52  THR C O   1 
ATOM   4989 C  CB  . THR C  1 66  ? -25.891 -4.557  12.283  1.00 25.07  ? 52  THR C CB  1 
ATOM   4990 O  OG1 . THR C  1 66  ? -26.282 -3.508  11.403  1.00 24.79  ? 52  THR C OG1 1 
ATOM   4991 C  CG2 . THR C  1 66  ? -24.645 -4.134  13.040  1.00 25.18  ? 52  THR C CG2 1 
ATOM   4992 N  N   . VAL C  1 67  ? -27.784 -6.990  11.587  1.00 23.98  ? 53  VAL C N   1 
ATOM   4993 C  CA  . VAL C  1 67  ? -29.032 -7.548  11.092  1.00 23.04  ? 53  VAL C CA  1 
ATOM   4994 C  C   . VAL C  1 67  ? -30.181 -7.044  11.964  1.00 24.38  ? 53  VAL C C   1 
ATOM   4995 O  O   . VAL C  1 67  ? -30.135 -7.170  13.186  1.00 24.77  ? 53  VAL C O   1 
ATOM   4996 C  CB  . VAL C  1 67  ? -28.977 -9.089  11.052  1.00 22.81  ? 53  VAL C CB  1 
ATOM   4997 C  CG1 . VAL C  1 67  ? -30.323 -9.706  10.688  1.00 22.02  ? 53  VAL C CG1 1 
ATOM   4998 C  CG2 . VAL C  1 67  ? -27.886 -9.584  10.108  1.00 23.30  ? 53  VAL C CG2 1 
ATOM   4999 N  N   . LEU C  1 68  ? -31.192 -6.452  11.316  1.00 21.62  ? 54  LEU C N   1 
ATOM   5000 C  CA  . LEU C  1 68  ? -32.440 -6.086  11.971  1.00 24.03  ? 54  LEU C CA  1 
ATOM   5001 C  C   . LEU C  1 68  ? -33.512 -7.109  11.604  1.00 23.27  ? 54  LEU C C   1 
ATOM   5002 O  O   . LEU C  1 68  ? -33.777 -7.338  10.426  1.00 26.51  ? 54  LEU C O   1 
ATOM   5003 C  CB  . LEU C  1 68  ? -32.888 -4.680  11.564  1.00 23.95  ? 54  LEU C CB  1 
ATOM   5004 C  CG  . LEU C  1 68  ? -34.298 -4.283  12.019  1.00 26.68  ? 54  LEU C CG  1 
ATOM   5005 C  CD1 . LEU C  1 68  ? -34.323 -4.006  13.514  1.00 28.09  ? 54  LEU C CD1 1 
ATOM   5006 C  CD2 . LEU C  1 68  ? -34.833 -3.085  11.248  1.00 26.42  ? 54  LEU C CD2 1 
ATOM   5007 N  N   . ILE C  1 69  ? -34.134 -7.710  12.623  1.00 24.13  ? 55  ILE C N   1 
ATOM   5008 C  CA  . ILE C  1 69  ? -35.313 -8.533  12.414  1.00 25.23  ? 55  ILE C CA  1 
ATOM   5009 C  C   . ILE C  1 69  ? -36.537 -7.749  12.885  1.00 29.55  ? 55  ILE C C   1 
ATOM   5010 O  O   . ILE C  1 69  ? -36.788 -7.645  14.084  1.00 27.83  ? 55  ILE C O   1 
ATOM   5011 C  CB  . ILE C  1 69  ? -35.178 -9.893  13.126  1.00 25.90  ? 55  ILE C CB  1 
ATOM   5012 C  CG1 . ILE C  1 69  ? -33.844 -10.574 12.782  1.00 27.80  ? 55  ILE C CG1 1 
ATOM   5013 C  CG2 . ILE C  1 69  ? -36.376 -10.791 12.811  1.00 25.11  ? 55  ILE C CG2 1 
ATOM   5014 C  CD1 . ILE C  1 69  ? -33.468 -11.718 13.704  1.00 31.35  ? 55  ILE C CD1 1 
ATOM   5015 N  N   . ASP C  1 70  ? -37.275 -7.179  11.924  1.00 30.33  ? 56  ASP C N   1 
ATOM   5016 C  CA  . ASP C  1 70  ? -38.537 -6.513  12.208  1.00 31.93  ? 56  ASP C CA  1 
ATOM   5017 C  C   . ASP C  1 70  ? -39.615 -7.574  12.426  1.00 30.34  ? 56  ASP C C   1 
ATOM   5018 O  O   . ASP C  1 70  ? -40.214 -8.061  11.470  1.00 30.34  ? 56  ASP C O   1 
ATOM   5019 C  CB  . ASP C  1 70  ? -38.926 -5.535  11.108  1.00 32.74  ? 56  ASP C CB  1 
ATOM   5020 C  CG  . ASP C  1 70  ? -40.140 -4.674  11.429  1.00 33.06  ? 56  ASP C CG  1 
ATOM   5021 O  OD1 . ASP C  1 70  ? -40.642 -4.778  12.568  1.00 30.97  ? 56  ASP C OD1 1 
ATOM   5022 O  OD2 . ASP C  1 70  ? -40.575 -3.914  10.539  1.00 41.18  ? 56  ASP C OD2 1 
ATOM   5023 N  N   . HIS C  1 71  ? -39.851 -7.911  13.700  1.00 29.40  ? 57  HIS C N   1 
ATOM   5024 C  CA  . HIS C  1 71  ? -40.727 -9.006  14.090  1.00 28.36  ? 57  HIS C CA  1 
ATOM   5025 C  C   . HIS C  1 71  ? -41.995 -8.430  14.724  1.00 27.59  ? 57  HIS C C   1 
ATOM   5026 O  O   . HIS C  1 71  ? -41.923 -7.435  15.442  1.00 28.36  ? 57  HIS C O   1 
ATOM   5027 C  CB  . HIS C  1 71  ? -39.971 -9.934  15.053  1.00 26.68  ? 57  HIS C CB  1 
ATOM   5028 C  CG  . HIS C  1 71  ? -40.572 -11.288 15.253  1.00 25.37  ? 57  HIS C CG  1 
ATOM   5029 N  ND1 . HIS C  1 71  ? -41.744 -11.509 15.945  1.00 24.81  ? 57  HIS C ND1 1 
ATOM   5030 C  CD2 . HIS C  1 71  ? -40.146 -12.494 14.853  1.00 24.51  ? 57  HIS C CD2 1 
ATOM   5031 C  CE1 . HIS C  1 71  ? -42.012 -12.808 15.950  1.00 24.89  ? 57  HIS C CE1 1 
ATOM   5032 N  NE2 . HIS C  1 71  ? -41.053 -13.426 15.293  1.00 25.19  ? 57  HIS C NE2 1 
ATOM   5033 N  N   . PRO C  1 72  ? -43.196 -9.012  14.483  1.00 32.19  ? 58  PRO C N   1 
ATOM   5034 C  CA  . PRO C  1 72  ? -44.432 -8.517  15.100  1.00 35.36  ? 58  PRO C CA  1 
ATOM   5035 C  C   . PRO C  1 72  ? -44.365 -8.400  16.622  1.00 37.09  ? 58  PRO C C   1 
ATOM   5036 O  O   . PRO C  1 72  ? -45.030 -7.551  17.211  1.00 36.85  ? 58  PRO C O   1 
ATOM   5037 C  CB  . PRO C  1 72  ? -45.514 -9.532  14.666  1.00 35.39  ? 58  PRO C CB  1 
ATOM   5038 C  CG  . PRO C  1 72  ? -44.741 -10.723 14.130  1.00 34.70  ? 58  PRO C CG  1 
ATOM   5039 C  CD  . PRO C  1 72  ? -43.435 -10.157 13.592  1.00 32.97  ? 58  PRO C CD  1 
ATOM   5040 N  N   . GLU C  1 73  ? -43.565 -9.269  17.251  1.00 36.80  ? 59  GLU C N   1 
ATOM   5041 C  CA  . GLU C  1 73  ? -43.466 -9.310  18.702  1.00 33.98  ? 59  GLU C CA  1 
ATOM   5042 C  C   . GLU C  1 73  ? -42.553 -8.188  19.197  1.00 31.95  ? 59  GLU C C   1 
ATOM   5043 O  O   . GLU C  1 73  ? -42.559 -7.857  20.380  1.00 38.09  ? 59  GLU C O   1 
ATOM   5044 C  CB  . GLU C  1 73  ? -42.944 -10.668 19.173  1.00 31.40  ? 59  GLU C CB  1 
ATOM   5045 C  CG  . GLU C  1 73  ? -43.880 -11.833 18.862  1.00 32.72  ? 59  GLU C CG  1 
ATOM   5046 C  CD  . GLU C  1 73  ? -43.353 -13.181 19.320  1.00 31.31  ? 59  GLU C CD  1 
ATOM   5047 O  OE1 . GLU C  1 73  ? -42.839 -13.252 20.457  1.00 35.38  ? 59  GLU C OE1 1 
ATOM   5048 O  OE2 . GLU C  1 73  ? -43.467 -14.159 18.553  1.00 30.57  ? 59  GLU C OE2 1 
ATOM   5049 N  N   . GLY C  1 74  ? -41.763 -7.613  18.283  1.00 28.40  ? 60  GLY C N   1 
ATOM   5050 C  CA  . GLY C  1 74  ? -40.823 -6.556  18.624  1.00 24.58  ? 60  GLY C CA  1 
ATOM   5051 C  C   . GLY C  1 74  ? -39.537 -6.672  17.807  1.00 27.52  ? 60  GLY C C   1 
ATOM   5052 O  O   . GLY C  1 74  ? -39.142 -7.771  17.427  1.00 32.93  ? 60  GLY C O   1 
ATOM   5053 N  N   . LYS C  1 75  ? -38.892 -5.526  17.545  1.00 25.38  ? 61  LYS C N   1 
ATOM   5054 C  CA  . LYS C  1 75  ? -37.717 -5.468  16.685  1.00 24.69  ? 61  LYS C CA  1 
ATOM   5055 C  C   . LYS C  1 75  ? -36.495 -6.022  17.420  1.00 27.36  ? 61  LYS C C   1 
ATOM   5056 O  O   . LYS C  1 75  ? -36.251 -5.684  18.578  1.00 25.51  ? 61  LYS C O   1 
ATOM   5057 C  CB  . LYS C  1 75  ? -37.488 -4.032  16.198  1.00 25.71  ? 61  LYS C CB  1 
ATOM   5058 C  CG  . LYS C  1 75  ? -38.553 -3.505  15.239  1.00 27.54  ? 61  LYS C CG  1 
ATOM   5059 C  CD  . LYS C  1 75  ? -38.388 -2.041  14.843  1.00 28.84  ? 61  LYS C CD  1 
ATOM   5060 C  CE  . LYS C  1 75  ? -39.291 -1.646  13.709  1.00 32.72  ? 61  LYS C CE  1 
ATOM   5061 N  NZ  . LYS C  1 75  ? -40.692 -2.005  13.957  1.00 32.11  ? 61  LYS C NZ  1 
ATOM   5062 N  N   . ILE C  1 76  ? -35.730 -6.869  16.716  1.00 27.74  ? 62  ILE C N   1 
ATOM   5063 C  CA  . ILE C  1 76  ? -34.541 -7.511  17.256  1.00 26.45  ? 62  ILE C CA  1 
ATOM   5064 C  C   . ILE C  1 76  ? -33.334 -7.130  16.395  1.00 24.89  ? 62  ILE C C   1 
ATOM   5065 O  O   . ILE C  1 76  ? -33.365 -7.284  15.177  1.00 24.63  ? 62  ILE C O   1 
ATOM   5066 C  CB  . ILE C  1 76  ? -34.736 -9.040  17.319  1.00 25.42  ? 62  ILE C CB  1 
ATOM   5067 C  CG1 . ILE C  1 76  ? -35.942 -9.430  18.187  1.00 25.48  ? 62  ILE C CG1 1 
ATOM   5068 C  CG2 . ILE C  1 76  ? -33.455 -9.734  17.783  1.00 25.76  ? 62  ILE C CG2 1 
ATOM   5069 C  CD1 . ILE C  1 76  ? -36.469 -10.831 17.932  1.00 23.14  ? 62  ILE C CD1 1 
ATOM   5070 N  N   . LEU C  1 77  ? -32.273 -6.628  17.043  1.00 23.59  ? 63  LEU C N   1 
ATOM   5071 C  CA  . LEU C  1 77  ? -31.045 -6.239  16.362  1.00 23.36  ? 63  LEU C CA  1 
ATOM   5072 C  C   . LEU C  1 77  ? -29.917 -7.181  16.776  1.00 25.91  ? 63  LEU C C   1 
ATOM   5073 O  O   . LEU C  1 77  ? -29.690 -7.390  17.967  1.00 27.99  ? 63  LEU C O   1 
ATOM   5074 C  CB  . LEU C  1 77  ? -30.699 -4.786  16.695  1.00 23.00  ? 63  LEU C CB  1 
ATOM   5075 C  CG  . LEU C  1 77  ? -29.517 -4.177  15.930  1.00 26.09  ? 63  LEU C CG  1 
ATOM   5076 C  CD1 . LEU C  1 77  ? -29.851 -4.007  14.458  1.00 28.23  ? 63  LEU C CD1 1 
ATOM   5077 C  CD2 . LEU C  1 77  ? -29.089 -2.847  16.530  1.00 30.16  ? 63  LEU C CD2 1 
ATOM   5078 N  N   . PHE C  1 78  ? -29.218 -7.743  15.781  1.00 24.52  ? 64  PHE C N   1 
ATOM   5079 C  CA  . PHE C  1 78  ? -28.050 -8.579  16.014  1.00 22.66  ? 64  PHE C CA  1 
ATOM   5080 C  C   . PHE C  1 78  ? -26.794 -7.763  15.703  1.00 22.49  ? 64  PHE C C   1 
ATOM   5081 O  O   . PHE C  1 78  ? -26.574 -7.392  14.553  1.00 21.29  ? 64  PHE C O   1 
ATOM   5082 C  CB  . PHE C  1 78  ? -28.156 -9.853  15.165  1.00 25.18  ? 64  PHE C CB  1 
ATOM   5083 C  CG  . PHE C  1 78  ? -27.050 -10.874 15.396  1.00 22.45  ? 64  PHE C CG  1 
ATOM   5084 C  CD1 . PHE C  1 78  ? -27.122 -11.778 16.451  1.00 24.43  ? 64  PHE C CD1 1 
ATOM   5085 C  CD2 . PHE C  1 78  ? -25.945 -10.934 14.554  1.00 22.81  ? 64  PHE C CD2 1 
ATOM   5086 C  CE1 . PHE C  1 78  ? -26.113 -12.707 16.658  1.00 23.76  ? 64  PHE C CE1 1 
ATOM   5087 C  CE2 . PHE C  1 78  ? -24.940 -11.865 14.767  1.00 23.06  ? 64  PHE C CE2 1 
ATOM   5088 C  CZ  . PHE C  1 78  ? -25.026 -12.749 15.817  1.00 22.51  ? 64  PHE C CZ  1 
ATOM   5089 N  N   . ASP C  1 79  ? -26.000 -7.469  16.745  1.00 21.36  ? 65  ASP C N   1 
ATOM   5090 C  CA  . ASP C  1 79  ? -24.765 -6.699  16.631  1.00 24.76  ? 65  ASP C CA  1 
ATOM   5091 C  C   . ASP C  1 79  ? -25.087 -5.228  16.356  1.00 23.75  ? 65  ASP C C   1 
ATOM   5092 O  O   . ASP C  1 79  ? -26.218 -4.904  15.996  1.00 27.50  ? 65  ASP C O   1 
ATOM   5093 C  CB  . ASP C  1 79  ? -23.812 -7.319  15.618  1.00 25.98  ? 65  ASP C CB  1 
ATOM   5094 C  CG  . ASP C  1 79  ? -23.015 -8.511  16.133  1.00 28.78  ? 65  ASP C CG  1 
ATOM   5095 O  OD1 . ASP C  1 79  ? -23.052 -8.755  17.357  1.00 29.17  ? 65  ASP C OD1 1 
ATOM   5096 O  OD2 . ASP C  1 79  ? -22.366 -9.188  15.308  1.00 36.46  ? 65  ASP C OD2 1 
ATOM   5097 N  N   . THR C  1 80  ? -24.089 -4.342  16.534  1.00 22.82  ? 66  THR C N   1 
ATOM   5098 C  CA  . THR C  1 80  ? -24.319 -2.902  16.475  1.00 22.54  ? 66  THR C CA  1 
ATOM   5099 C  C   . THR C  1 80  ? -23.194 -2.170  15.737  1.00 23.14  ? 66  THR C C   1 
ATOM   5100 O  O   . THR C  1 80  ? -23.189 -0.942  15.705  1.00 31.35  ? 66  THR C O   1 
ATOM   5101 C  CB  . THR C  1 80  ? -24.493 -2.327  17.885  1.00 22.50  ? 66  THR C CB  1 
ATOM   5102 O  OG1 . THR C  1 80  ? -23.252 -2.462  18.572  1.00 24.77  ? 66  THR C OG1 1 
ATOM   5103 C  CG2 . THR C  1 80  ? -25.587 -3.018  18.678  1.00 21.32  ? 66  THR C CG2 1 
ATOM   5104 N  N   . SER C  1 81  ? -22.243 -2.908  15.150  1.00 23.86  ? 67  SER C N   1 
ATOM   5105 C  CA  . SER C  1 81  ? -21.166 -2.315  14.362  1.00 26.71  ? 67  SER C CA  1 
ATOM   5106 C  C   . SER C  1 81  ? -20.219 -1.502  15.247  1.00 29.49  ? 67  SER C C   1 
ATOM   5107 O  O   . SER C  1 81  ? -20.015 -1.838  16.413  1.00 30.14  ? 67  SER C O   1 
ATOM   5108 C  CB  . SER C  1 81  ? -21.706 -1.476  13.217  1.00 32.19  ? 67  SER C CB  1 
ATOM   5109 O  OG  . SER C  1 81  ? -22.376 -0.311  13.680  1.00 31.60  ? 67  SER C OG  1 
ATOM   5110 N  N   . CYS C  1 82  ? -19.617 -0.451  14.668  1.00 29.47  ? 68  CYS C N   1 
ATOM   5111 C  CA  . CYS C  1 82  ? -18.651 0.389   15.363  1.00 26.60  ? 68  CYS C CA  1 
ATOM   5112 C  C   . CYS C  1 82  ? -19.298 1.716   15.754  1.00 27.27  ? 68  CYS C C   1 
ATOM   5113 O  O   . CYS C  1 82  ? -20.232 2.169   15.097  1.00 30.54  ? 68  CYS C O   1 
ATOM   5114 C  CB  . CYS C  1 82  ? -17.430 0.678   14.493  1.00 25.04  ? 68  CYS C CB  1 
ATOM   5115 S  SG  . CYS C  1 82  ? -16.740 -0.791  13.688  1.00 28.01  ? 68  CYS C SG  1 
ATOM   5116 N  N   . ASN C  1 83  ? -18.787 2.336   16.825  1.00 29.35  ? 69  ASN C N   1 
ATOM   5117 C  CA  . ASN C  1 83  ? -19.266 3.642   17.251  1.00 28.31  ? 69  ASN C CA  1 
ATOM   5118 C  C   . ASN C  1 83  ? -18.864 4.686   16.211  1.00 28.40  ? 69  ASN C C   1 
ATOM   5119 O  O   . ASN C  1 83  ? -17.750 4.652   15.690  1.00 28.25  ? 69  ASN C O   1 
ATOM   5120 C  CB  . ASN C  1 83  ? -18.729 4.036   18.624  1.00 30.19  ? 69  ASN C CB  1 
ATOM   5121 C  CG  . ASN C  1 83  ? -19.462 5.226   19.199  1.00 31.62  ? 69  ASN C CG  1 
ATOM   5122 O  OD1 . ASN C  1 83  ? -18.964 6.355   19.134  1.00 33.03  ? 69  ASN C OD1 1 
ATOM   5123 N  ND2 . ASN C  1 83  ? -20.649 5.000   19.744  1.00 32.06  ? 69  ASN C ND2 1 
ATOM   5124 N  N   . PRO C  1 84  ? -19.755 5.648   15.877  1.00 30.67  ? 70  PRO C N   1 
ATOM   5125 C  CA  . PRO C  1 84  ? -19.417 6.714   14.928  1.00 36.06  ? 70  PRO C CA  1 
ATOM   5126 C  C   . PRO C  1 84  ? -18.169 7.522   15.288  1.00 40.61  ? 70  PRO C C   1 
ATOM   5127 O  O   . PRO C  1 84  ? -17.518 8.073   14.404  1.00 42.74  ? 70  PRO C O   1 
ATOM   5128 C  CB  . PRO C  1 84  ? -20.681 7.598   14.917  1.00 35.15  ? 70  PRO C CB  1 
ATOM   5129 C  CG  . PRO C  1 84  ? -21.797 6.680   15.374  1.00 36.16  ? 70  PRO C CG  1 
ATOM   5130 C  CD  . PRO C  1 84  ? -21.143 5.731   16.363  1.00 30.84  ? 70  PRO C CD  1 
ATOM   5131 N  N   . ASN C  1 85  ? -17.840 7.592   16.585  1.00 39.81  ? 71  ASN C N   1 
ATOM   5132 C  CA  . ASN C  1 85  ? -16.688 8.361   17.036  1.00 37.11  ? 71  ASN C CA  1 
ATOM   5133 C  C   . ASN C  1 85  ? -15.544 7.414   17.399  1.00 33.22  ? 71  ASN C C   1 
ATOM   5134 O  O   . ASN C  1 85  ? -14.872 7.608   18.410  1.00 32.95  ? 71  ASN C O   1 
ATOM   5135 C  CB  . ASN C  1 85  ? -17.040 9.286   18.199  1.00 38.98  ? 71  ASN C CB  1 
ATOM   5136 C  CG  . ASN C  1 85  ? -15.970 10.323  18.455  1.00 45.04  ? 71  ASN C CG  1 
ATOM   5137 O  OD1 . ASN C  1 85  ? -15.436 10.913  17.509  1.00 40.71  ? 71  ASN C OD1 1 
ATOM   5138 N  ND2 . ASN C  1 85  ? -15.633 10.553  19.716  1.00 44.25  ? 71  ASN C ND2 1 
ATOM   5139 N  N   . SER C  1 86  ? -15.319 6.401   16.554  1.00 31.18  ? 72  SER C N   1 
ATOM   5140 C  CA  . SER C  1 86  ? -14.282 5.407   16.789  1.00 31.28  ? 72  SER C CA  1 
ATOM   5141 C  C   . SER C  1 86  ? -12.929 5.909   16.287  1.00 33.89  ? 72  SER C C   1 
ATOM   5142 O  O   . SER C  1 86  ? -11.932 5.845   17.004  1.00 29.64  ? 72  SER C O   1 
ATOM   5143 C  CB  . SER C  1 86  ? -14.634 4.087   16.141  1.00 26.94  ? 72  SER C CB  1 
ATOM   5144 O  OG  . SER C  1 86  ? -15.795 3.513   16.726  1.00 27.84  ? 72  SER C OG  1 
ATOM   5145 N  N   . MET C  1 87  ? -12.911 6.398   15.042  1.00 32.82  ? 73  MET C N   1 
ATOM   5146 C  CA  . MET C  1 87  ? -11.674 6.682   14.329  1.00 35.59  ? 73  MET C CA  1 
ATOM   5147 C  C   . MET C  1 87  ? -11.344 8.172   14.421  1.00 36.25  ? 73  MET C C   1 
ATOM   5148 O  O   . MET C  1 87  ? -12.211 8.981   14.745  1.00 32.30  ? 73  MET C O   1 
ATOM   5149 C  CB  . MET C  1 87  ? -11.802 6.263   12.858  1.00 38.72  ? 73  MET C CB  1 
ATOM   5150 C  CG  . MET C  1 87  ? -11.947 4.762   12.650  1.00 34.48  ? 73  MET C CG  1 
ATOM   5151 S  SD  . MET C  1 87  ? -10.413 3.847   12.901  1.00 35.04  ? 73  MET C SD  1 
ATOM   5152 C  CE  . MET C  1 87  ? -9.325  4.621   11.695  1.00 37.33  ? 73  MET C CE  1 
ATOM   5153 N  N   . GLY C  1 88  ? -10.080 8.519   14.140  1.00 38.75  ? 74  GLY C N   1 
ATOM   5154 C  CA  . GLY C  1 88  ? -9.631  9.905   14.115  1.00 46.01  ? 74  GLY C CA  1 
ATOM   5155 C  C   . GLY C  1 88  ? -8.782  10.255  15.337  1.00 49.42  ? 74  GLY C C   1 
ATOM   5156 O  O   . GLY C  1 88  ? -8.812  9.545   16.340  1.00 46.72  ? 74  GLY C O   1 
ATOM   5157 N  N   . PRO C  1 89  ? -7.999  11.361  15.291  1.00 53.54  ? 75  PRO C N   1 
ATOM   5158 C  CA  . PRO C  1 89  ? -7.165  11.773  16.425  1.00 54.47  ? 75  PRO C CA  1 
ATOM   5159 C  C   . PRO C  1 89  ? -7.946  11.929  17.729  1.00 47.79  ? 75  PRO C C   1 
ATOM   5160 O  O   . PRO C  1 89  ? -7.402  11.711  18.809  1.00 49.21  ? 75  PRO C O   1 
ATOM   5161 C  CB  . PRO C  1 89  ? -6.542  13.110  15.963  1.00 59.62  ? 75  PRO C CB  1 
ATOM   5162 C  CG  . PRO C  1 89  ? -7.407  13.558  14.800  1.00 59.26  ? 75  PRO C CG  1 
ATOM   5163 C  CD  . PRO C  1 89  ? -7.874  12.271  14.142  1.00 57.02  ? 75  PRO C CD  1 
ATOM   5164 N  N   A GLN C  1 90  ? -9.234  12.259  17.563  0.50 48.92  ? 76  GLN C N   1 
ATOM   5165 N  N   B GLN C  1 90  ? -9.212  12.353  17.656  0.50 46.67  ? 76  GLN C N   1 
ATOM   5166 C  CA  A GLN C  1 90  ? -10.166 12.518  18.649  0.50 47.87  ? 76  GLN C CA  1 
ATOM   5167 C  CA  B GLN C  1 90  ? -10.030 12.441  18.858  0.50 44.95  ? 76  GLN C CA  1 
ATOM   5168 C  C   A GLN C  1 90  ? -11.009 11.271  18.922  0.50 43.77  ? 76  GLN C C   1 
ATOM   5169 C  C   B GLN C  1 90  ? -11.027 11.284  18.877  0.50 42.36  ? 76  GLN C C   1 
ATOM   5170 O  O   A GLN C  1 90  ? -11.992 11.335  19.656  0.50 38.82  ? 76  GLN C O   1 
ATOM   5171 O  O   B GLN C  1 90  ? -12.145 11.429  19.369  0.50 37.70  ? 76  GLN C O   1 
ATOM   5172 C  CB  A GLN C  1 90  ? -11.053 13.701  18.248  0.50 48.54  ? 76  GLN C CB  1 
ATOM   5173 C  CB  B GLN C  1 90  ? -10.743 13.788  18.991  0.50 43.83  ? 76  GLN C CB  1 
ATOM   5174 C  CG  A GLN C  1 90  ? -12.029 14.163  19.326  0.50 51.12  ? 76  GLN C CG  1 
ATOM   5175 C  CG  B GLN C  1 90  ? -9.860  14.912  19.525  0.50 43.55  ? 76  GLN C CG  1 
ATOM   5176 C  CD  A GLN C  1 90  ? -12.413 15.620  19.183  0.50 53.37  ? 76  GLN C CD  1 
ATOM   5177 C  CD  B GLN C  1 90  ? -8.879  15.428  18.496  0.50 44.23  ? 76  GLN C CD  1 
ATOM   5178 O  OE1 A GLN C  1 90  ? -12.879 16.066  18.129  0.50 56.63  ? 76  GLN C OE1 1 
ATOM   5179 O  OE1 B GLN C  1 90  ? -7.666  15.484  18.727  0.50 42.15  ? 76  GLN C OE1 1 
ATOM   5180 N  NE2 A GLN C  1 90  ? -12.204 16.382  20.247  0.50 54.79  ? 76  GLN C NE2 1 
ATOM   5181 N  NE2 B GLN C  1 90  ? -9.404  15.817  17.343  0.50 43.80  ? 76  GLN C NE2 1 
ATOM   5182 N  N   . GLY C  1 91  ? -10.604 10.136  18.338  1.00 41.47  ? 77  GLY C N   1 
ATOM   5183 C  CA  . GLY C  1 91  ? -11.424 8.932   18.327  1.00 40.34  ? 77  GLY C CA  1 
ATOM   5184 C  C   . GLY C  1 91  ? -11.378 8.174   19.655  1.00 35.00  ? 77  GLY C C   1 
ATOM   5185 O  O   . GLY C  1 91  ? -10.463 8.362   20.453  1.00 37.29  ? 77  GLY C O   1 
ATOM   5186 N  N   . ARG C  1 92  ? -12.382 7.311   19.871  1.00 31.92  ? 78  ARG C N   1 
ATOM   5187 C  CA  . ARG C  1 92  ? -12.463 6.476   21.060  1.00 30.63  ? 78  ARG C CA  1 
ATOM   5188 C  C   . ARG C  1 92  ? -11.431 5.352   20.985  1.00 32.45  ? 78  ARG C C   1 
ATOM   5189 O  O   . ARG C  1 92  ? -10.864 4.959   22.002  1.00 34.48  ? 78  ARG C O   1 
ATOM   5190 C  CB  . ARG C  1 92  ? -13.862 5.868   21.228  1.00 31.76  ? 78  ARG C CB  1 
ATOM   5191 C  CG  . ARG C  1 92  ? -14.970 6.851   21.580  1.00 31.02  ? 78  ARG C CG  1 
ATOM   5192 C  CD  . ARG C  1 92  ? -16.281 6.117   21.828  1.00 28.59  ? 78  ARG C CD  1 
ATOM   5193 N  NE  . ARG C  1 92  ? -17.370 6.984   22.290  1.00 28.48  ? 78  ARG C NE  1 
ATOM   5194 C  CZ  . ARG C  1 92  ? -18.574 6.544   22.635  1.00 30.49  ? 78  ARG C CZ  1 
ATOM   5195 N  NH1 . ARG C  1 92  ? -18.847 5.251   22.584  1.00 31.67  ? 78  ARG C NH1 1 
ATOM   5196 N  NH2 . ARG C  1 92  ? -19.502 7.396   23.033  1.00 32.08  ? 78  ARG C NH2 1 
ATOM   5197 N  N   . TRP C  1 93  ? -11.206 4.820   19.779  1.00 32.90  ? 79  TRP C N   1 
ATOM   5198 C  CA  . TRP C  1 93  ? -10.219 3.769   19.585  1.00 34.84  ? 79  TRP C CA  1 
ATOM   5199 C  C   . TRP C  1 93  ? -8.816  4.345   19.776  1.00 38.24  ? 79  TRP C C   1 
ATOM   5200 O  O   . TRP C  1 93  ? -8.538  5.459   19.340  1.00 40.93  ? 79  TRP C O   1 
ATOM   5201 C  CB  . TRP C  1 93  ? -10.365 3.133   18.194  1.00 30.30  ? 79  TRP C CB  1 
ATOM   5202 C  CG  . TRP C  1 93  ? -11.672 2.420   17.949  1.00 30.40  ? 79  TRP C CG  1 
ATOM   5203 C  CD1 . TRP C  1 93  ? -12.785 2.407   18.740  1.00 28.82  ? 79  TRP C CD1 1 
ATOM   5204 C  CD2 . TRP C  1 93  ? -11.999 1.621   16.790  1.00 27.11  ? 79  TRP C CD2 1 
ATOM   5205 N  NE1 . TRP C  1 93  ? -13.772 1.648   18.165  1.00 27.19  ? 79  TRP C NE1 1 
ATOM   5206 C  CE2 . TRP C  1 93  ? -13.322 1.156   16.968  1.00 27.11  ? 79  TRP C CE2 1 
ATOM   5207 C  CE3 . TRP C  1 93  ? -11.305 1.256   15.631  1.00 29.04  ? 79  TRP C CE3 1 
ATOM   5208 C  CZ2 . TRP C  1 93  ? -13.957 0.347   16.028  1.00 30.47  ? 79  TRP C CZ2 1 
ATOM   5209 C  CZ3 . TRP C  1 93  ? -11.935 0.456   14.703  1.00 27.92  ? 79  TRP C CZ3 1 
ATOM   5210 C  CH2 . TRP C  1 93  ? -13.243 0.011   14.900  1.00 29.06  ? 79  TRP C CH2 1 
ATOM   5211 N  N   . ALA C  1 94  ? -7.945  3.577   20.441  1.00 36.22  ? 80  ALA C N   1 
ATOM   5212 C  CA  . ALA C  1 94  ? -6.547  3.945   20.609  1.00 36.47  ? 80  ALA C CA  1 
ATOM   5213 C  C   . ALA C  1 94  ? -5.861  3.973   19.244  1.00 40.34  ? 80  ALA C C   1 
ATOM   5214 O  O   . ALA C  1 94  ? -6.318  3.316   18.312  1.00 38.01  ? 80  ALA C O   1 
ATOM   5215 C  CB  . ALA C  1 94  ? -5.868  2.970   21.549  1.00 32.58  ? 80  ALA C CB  1 
ATOM   5216 N  N   . GLU C  1 95  ? -4.765  4.737   19.136  1.00 42.79  ? 81  GLU C N   1 
ATOM   5217 C  CA  . GLU C  1 95  ? -4.032  4.859   17.884  1.00 46.37  ? 81  GLU C CA  1 
ATOM   5218 C  C   . GLU C  1 95  ? -3.657  3.472   17.369  1.00 40.50  ? 81  GLU C C   1 
ATOM   5219 O  O   . GLU C  1 95  ? -3.948  3.133   16.224  1.00 41.71  ? 81  GLU C O   1 
ATOM   5220 C  CB  . GLU C  1 95  ? -2.770  5.714   18.026  1.00 56.80  ? 81  GLU C CB  1 
ATOM   5221 C  CG  . GLU C  1 95  ? -2.962  7.170   17.607  1.00 62.36  ? 81  GLU C CG  1 
ATOM   5222 C  CD  . GLU C  1 95  ? -3.617  7.339   16.247  1.00 62.22  ? 81  GLU C CD  1 
ATOM   5223 O  OE1 . GLU C  1 95  ? -3.099  6.764   15.266  1.00 67.84  ? 81  GLU C OE1 1 
ATOM   5224 O  OE2 . GLU C  1 95  ? -4.645  8.046   16.170  1.00 58.33  ? 81  GLU C OE2 1 
ATOM   5225 N  N   . SER C  1 96  ? -3.005  2.682   18.230  1.00 39.46  ? 82  SER C N   1 
ATOM   5226 C  CA  . SER C  1 96  ? -2.485  1.379   17.846  1.00 37.51  ? 82  SER C CA  1 
ATOM   5227 C  C   . SER C  1 96  ? -3.604  0.513   17.268  1.00 35.60  ? 82  SER C C   1 
ATOM   5228 O  O   . SER C  1 96  ? -3.375  -0.262  16.342  1.00 35.94  ? 82  SER C O   1 
ATOM   5229 C  CB  . SER C  1 96  ? -1.810  0.697   19.012  1.00 40.67  ? 82  SER C CB  1 
ATOM   5230 O  OG  . SER C  1 96  ? -2.733  0.445   20.063  1.00 39.81  ? 82  SER C OG  1 
ATOM   5231 N  N   . THR C  1 97  ? -4.816  0.654   17.823  1.00 34.83  ? 83  THR C N   1 
ATOM   5232 C  CA  . THR C  1 97  ? -5.962  -0.127  17.379  1.00 37.42  ? 83  THR C CA  1 
ATOM   5233 C  C   . THR C  1 97  ? -6.396  0.372   16.001  1.00 34.18  ? 83  THR C C   1 
ATOM   5234 O  O   . THR C  1 97  ? -6.677  -0.425  15.109  1.00 32.57  ? 83  THR C O   1 
ATOM   5235 C  CB  . THR C  1 97  ? -7.105  -0.044  18.395  1.00 36.52  ? 83  THR C CB  1 
ATOM   5236 O  OG1 . THR C  1 97  ? -6.573  -0.437  19.658  1.00 36.03  ? 83  THR C OG1 1 
ATOM   5237 C  CG2 . THR C  1 97  ? -8.281  -0.936  18.033  1.00 36.59  ? 83  THR C CG2 1 
ATOM   5238 N  N   . GLN C  1 98  ? -6.440  1.700   15.840  1.00 34.22  ? 84  GLN C N   1 
ATOM   5239 C  CA  . GLN C  1 98  ? -6.862  2.317   14.592  1.00 37.59  ? 84  GLN C CA  1 
ATOM   5240 C  C   . GLN C  1 98  ? -5.929  1.893   13.457  1.00 37.15  ? 84  GLN C C   1 
ATOM   5241 O  O   . GLN C  1 98  ? -6.358  1.778   12.311  1.00 40.14  ? 84  GLN C O   1 
ATOM   5242 C  CB  . GLN C  1 98  ? -6.906  3.840   14.728  1.00 35.10  ? 84  GLN C CB  1 
ATOM   5243 C  CG  . GLN C  1 98  ? -8.026  4.355   15.625  1.00 33.00  ? 84  GLN C CG  1 
ATOM   5244 C  CD  . GLN C  1 98  ? -8.201  5.855   15.531  1.00 32.24  ? 84  GLN C CD  1 
ATOM   5245 O  OE1 . GLN C  1 98  ? -8.159  6.436   14.441  1.00 38.75  ? 84  GLN C OE1 1 
ATOM   5246 N  NE2 . GLN C  1 98  ? -8.382  6.502   16.672  1.00 33.47  ? 84  GLN C NE2 1 
ATOM   5247 N  N   . GLN C  1 99  ? -4.655  1.646   13.789  1.00 37.92  ? 85  GLN C N   1 
ATOM   5248 C  CA  . GLN C  1 99  ? -3.643  1.336   12.790  1.00 40.33  ? 85  GLN C CA  1 
ATOM   5249 C  C   . GLN C  1 99  ? -3.754  -0.129  12.367  1.00 41.32  ? 85  GLN C C   1 
ATOM   5250 O  O   . GLN C  1 99  ? -3.488  -0.463  11.214  1.00 38.31  ? 85  GLN C O   1 
ATOM   5251 C  CB  . GLN C  1 99  ? -2.236  1.646   13.307  1.00 45.65  ? 85  GLN C CB  1 
ATOM   5252 C  CG  . GLN C  1 99  ? -2.018  3.108   13.686  1.00 56.88  ? 85  GLN C CG  1 
ATOM   5253 C  CD  . GLN C  1 99  ? -2.386  4.072   12.579  1.00 70.63  ? 85  GLN C CD  1 
ATOM   5254 O  OE1 . GLN C  1 99  ? -3.286  4.907   12.724  1.00 75.51  ? 85  GLN C OE1 1 
ATOM   5255 N  NE2 . GLN C  1 99  ? -1.689  3.965   11.457  1.00 72.01  ? 85  GLN C NE2 1 
ATOM   5256 N  N   . MET C  1 100 ? -4.151  -0.998  13.306  1.00 35.10  ? 86  MET C N   1 
ATOM   5257 C  CA  . MET C  1 100 ? -4.195  -2.431  13.056  1.00 34.30  ? 86  MET C CA  1 
ATOM   5258 C  C   . MET C  1 100 ? -5.572  -2.842  12.537  1.00 30.44  ? 86  MET C C   1 
ATOM   5259 O  O   . MET C  1 100 ? -5.681  -3.814  11.792  1.00 33.44  ? 86  MET C O   1 
ATOM   5260 C  CB  . MET C  1 100 ? -3.858  -3.231  14.322  1.00 35.42  ? 86  MET C CB  1 
ATOM   5261 C  CG  . MET C  1 100 ? -2.388  -3.604  14.444  1.00 41.88  ? 86  MET C CG  1 
ATOM   5262 S  SD  . MET C  1 100 ? -2.010  -4.563  15.926  1.00 41.48  ? 86  MET C SD  1 
ATOM   5263 C  CE  . MET C  1 100 ? -2.963  -3.664  17.158  1.00 34.48  ? 86  MET C CE  1 
ATOM   5264 N  N   . PHE C  1 101 ? -6.613  -2.094  12.929  1.00 30.24  ? 87  PHE C N   1 
ATOM   5265 C  CA  . PHE C  1 101 ? -7.989  -2.461  12.625  1.00 31.51  ? 87  PHE C CA  1 
ATOM   5266 C  C   . PHE C  1 101 ? -8.768  -1.245  12.124  1.00 31.82  ? 87  PHE C C   1 
ATOM   5267 O  O   . PHE C  1 101 ? -9.853  -0.956  12.624  1.00 29.52  ? 87  PHE C O   1 
ATOM   5268 C  CB  . PHE C  1 101 ? -8.656  -3.058  13.871  1.00 30.58  ? 87  PHE C CB  1 
ATOM   5269 C  CG  . PHE C  1 101 ? -7.880  -4.215  14.484  1.00 30.44  ? 87  PHE C CG  1 
ATOM   5270 C  CD1 . PHE C  1 101 ? -7.863  -5.463  13.870  1.00 34.72  ? 87  PHE C CD1 1 
ATOM   5271 C  CD2 . PHE C  1 101 ? -7.163  -4.051  15.662  1.00 34.87  ? 87  PHE C CD2 1 
ATOM   5272 C  CE1 . PHE C  1 101 ? -7.149  -6.514  14.423  1.00 35.82  ? 87  PHE C CE1 1 
ATOM   5273 C  CE2 . PHE C  1 101 ? -6.451  -5.107  16.212  1.00 36.32  ? 87  PHE C CE2 1 
ATOM   5274 C  CZ  . PHE C  1 101 ? -6.445  -6.335  15.591  1.00 34.19  ? 87  PHE C CZ  1 
ATOM   5275 N  N   . PRO C  1 102 ? -8.266  -0.512  11.103  1.00 30.72  ? 88  PRO C N   1 
ATOM   5276 C  CA  . PRO C  1 102 ? -8.932  0.707   10.638  1.00 30.86  ? 88  PRO C CA  1 
ATOM   5277 C  C   . PRO C  1 102 ? -10.339 0.449   10.102  1.00 28.47  ? 88  PRO C C   1 
ATOM   5278 O  O   . PRO C  1 102 ? -10.550 -0.464  9.307   1.00 28.23  ? 88  PRO C O   1 
ATOM   5279 C  CB  . PRO C  1 102 ? -7.986  1.247   9.545   1.00 32.87  ? 88  PRO C CB  1 
ATOM   5280 C  CG  . PRO C  1 102 ? -7.209  0.030   9.087   1.00 33.28  ? 88  PRO C CG  1 
ATOM   5281 C  CD  . PRO C  1 102 ? -7.052  -0.828  10.333  1.00 31.74  ? 88  PRO C CD  1 
ATOM   5282 N  N   . TRP C  1 103 ? -11.293 1.270   10.559  1.00 26.96  ? 89  TRP C N   1 
ATOM   5283 C  CA  . TRP C  1 103 ? -12.667 1.239   10.079  1.00 31.19  ? 89  TRP C CA  1 
ATOM   5284 C  C   . TRP C  1 103 ? -12.901 2.433   9.155   1.00 35.85  ? 89  TRP C C   1 
ATOM   5285 O  O   . TRP C  1 103 ? -12.631 3.572   9.529   1.00 34.30  ? 89  TRP C O   1 
ATOM   5286 C  CB  . TRP C  1 103 ? -13.641 1.256   11.269  1.00 28.44  ? 89  TRP C CB  1 
ATOM   5287 C  CG  . TRP C  1 103 ? -15.108 1.270   10.913  1.00 28.43  ? 89  TRP C CG  1 
ATOM   5288 C  CD1 . TRP C  1 103 ? -15.760 0.441   10.047  1.00 27.60  ? 89  TRP C CD1 1 
ATOM   5289 C  CD2 . TRP C  1 103 ? -16.116 2.165   11.438  1.00 31.24  ? 89  TRP C CD2 1 
ATOM   5290 N  NE1 . TRP C  1 103 ? -17.093 0.755   9.997   1.00 30.16  ? 89  TRP C NE1 1 
ATOM   5291 C  CE2 . TRP C  1 103 ? -17.344 1.808   10.836  1.00 29.46  ? 89  TRP C CE2 1 
ATOM   5292 C  CE3 . TRP C  1 103 ? -16.102 3.228   12.348  1.00 29.14  ? 89  TRP C CE3 1 
ATOM   5293 C  CZ2 . TRP C  1 103 ? -18.536 2.475   11.119  1.00 31.08  ? 89  TRP C CZ2 1 
ATOM   5294 C  CZ3 . TRP C  1 103 ? -17.281 3.883   12.629  1.00 28.72  ? 89  TRP C CZ3 1 
ATOM   5295 C  CH2 . TRP C  1 103 ? -18.481 3.511   12.022  1.00 30.09  ? 89  TRP C CH2 1 
ATOM   5296 N  N   . THR C  1 104 ? -13.390 2.157   7.941   1.00 37.08  ? 90  THR C N   1 
ATOM   5297 C  CA  . THR C  1 104 ? -13.764 3.209   7.008   1.00 37.20  ? 90  THR C CA  1 
ATOM   5298 C  C   . THR C  1 104 ? -15.262 3.094   6.727   1.00 36.82  ? 90  THR C C   1 
ATOM   5299 O  O   . THR C  1 104 ? -15.750 2.023   6.370   1.00 35.06  ? 90  THR C O   1 
ATOM   5300 C  CB  . THR C  1 104 ? -12.929 3.120   5.728   1.00 37.26  ? 90  THR C CB  1 
ATOM   5301 O  OG1 . THR C  1 104 ? -13.248 1.864   5.138   1.00 42.55  ? 90  THR C OG1 1 
ATOM   5302 C  CG2 . THR C  1 104 ? -11.434 3.219   5.982   1.00 33.55  ? 90  THR C CG2 1 
ATOM   5303 N  N   . ALA C  1 105 ? -15.987 4.205   6.912   1.00 35.12  ? 91  ALA C N   1 
ATOM   5304 C  CA  . ALA C  1 105 ? -17.430 4.222   6.733   1.00 35.62  ? 91  ALA C CA  1 
ATOM   5305 C  C   . ALA C  1 105 ? -17.902 5.632   6.385   1.00 37.36  ? 91  ALA C C   1 
ATOM   5306 O  O   . ALA C  1 105 ? -17.552 6.594   7.066   1.00 34.91  ? 91  ALA C O   1 
ATOM   5307 C  CB  . ALA C  1 105 ? -18.111 3.711   7.986   1.00 35.25  ? 91  ALA C CB  1 
ATOM   5308 N  N   . THR C  1 106 ? -18.705 5.734   5.319   1.00 37.49  ? 92  THR C N   1 
ATOM   5309 C  CA  . THR C  1 106 ? -19.393 6.973   4.990   1.00 39.47  ? 92  THR C CA  1 
ATOM   5310 C  C   . THR C  1 106 ? -20.586 7.115   5.937   1.00 41.91  ? 92  THR C C   1 
ATOM   5311 O  O   . THR C  1 106 ? -21.068 6.121   6.478   1.00 37.06  ? 92  THR C O   1 
ATOM   5312 C  CB  . THR C  1 106 ? -19.805 6.970   3.517   1.00 41.45  ? 92  THR C CB  1 
ATOM   5313 O  OG1 . THR C  1 106 ? -20.775 5.935   3.381   1.00 43.95  ? 92  THR C OG1 1 
ATOM   5314 C  CG2 . THR C  1 106 ? -18.630 6.731   2.582   1.00 43.24  ? 92  THR C CG2 1 
ATOM   5315 N  N   . GLU C  1 107 ? -21.045 8.355   6.145   1.00 38.94  ? 93  GLU C N   1 
ATOM   5316 C  CA  . GLU C  1 107 ? -22.076 8.641   7.131   1.00 41.54  ? 93  GLU C CA  1 
ATOM   5317 C  C   . GLU C  1 107 ? -23.272 7.714   6.916   1.00 37.31  ? 93  GLU C C   1 
ATOM   5318 O  O   . GLU C  1 107 ? -23.943 7.327   7.871   1.00 36.47  ? 93  GLU C O   1 
ATOM   5319 C  CB  . GLU C  1 107 ? -22.475 10.118  7.078   1.00 51.53  ? 93  GLU C CB  1 
ATOM   5320 C  CG  . GLU C  1 107 ? -23.505 10.511  8.134   1.00 58.94  ? 93  GLU C CG  1 
ATOM   5321 C  CD  . GLU C  1 107 ? -23.611 12.005  8.387   1.00 65.60  ? 93  GLU C CD  1 
ATOM   5322 O  OE1 . GLU C  1 107 ? -22.603 12.605  8.817   1.00 71.83  ? 93  GLU C OE1 1 
ATOM   5323 O  OE2 . GLU C  1 107 ? -24.702 12.568  8.158   1.00 67.03  ? 93  GLU C OE2 1 
ATOM   5324 N  N   . GLU C  1 108 ? -23.523 7.358   5.652   1.00 41.05  ? 94  GLU C N   1 
ATOM   5325 C  CA  . GLU C  1 108 ? -24.628 6.486   5.284   1.00 39.36  ? 94  GLU C CA  1 
ATOM   5326 C  C   . GLU C  1 108 ? -24.538 5.163   6.045   1.00 36.80  ? 94  GLU C C   1 
ATOM   5327 O  O   . GLU C  1 108 ? -25.556 4.513   6.285   1.00 29.31  ? 94  GLU C O   1 
ATOM   5328 C  CB  . GLU C  1 108 ? -24.602 6.216   3.778   1.00 43.44  ? 94  GLU C CB  1 
ATOM   5329 C  CG  . GLU C  1 108 ? -25.011 7.413   2.923   1.00 54.51  ? 94  GLU C CG  1 
ATOM   5330 C  CD  . GLU C  1 108 ? -24.286 8.710   3.241   1.00 57.36  ? 94  GLU C CD  1 
ATOM   5331 O  OE1 . GLU C  1 108 ? -23.036 8.717   3.216   1.00 46.59  ? 94  GLU C OE1 1 
ATOM   5332 O  OE2 . GLU C  1 108 ? -24.975 9.717   3.510   1.00 64.76  ? 94  GLU C OE2 1 
ATOM   5333 N  N   . CYS C  1 109 ? -23.310 4.781   6.422   1.00 34.97  ? 95  CYS C N   1 
ATOM   5334 C  CA  . CYS C  1 109 ? -23.023 3.445   6.924   1.00 33.46  ? 95  CYS C CA  1 
ATOM   5335 C  C   . CYS C  1 109 ? -23.256 3.349   8.432   1.00 33.31  ? 95  CYS C C   1 
ATOM   5336 O  O   . CYS C  1 109 ? -23.470 2.255   8.952   1.00 32.56  ? 95  CYS C O   1 
ATOM   5337 C  CB  . CYS C  1 109 ? -21.599 3.020   6.577   1.00 31.71  ? 95  CYS C CB  1 
ATOM   5338 S  SG  . CYS C  1 109 ? -21.398 2.486   4.857   1.00 33.11  ? 95  CYS C SG  1 
ATOM   5339 N  N   . TYR C  1 110 ? -23.209 4.490   9.130   1.00 33.34  ? 96  TYR C N   1 
ATOM   5340 C  CA  . TYR C  1 110 ? -23.457 4.513   10.564  1.00 31.08  ? 96  TYR C CA  1 
ATOM   5341 C  C   . TYR C  1 110 ? -24.807 3.847   10.835  1.00 31.56  ? 96  TYR C C   1 
ATOM   5342 O  O   . TYR C  1 110 ? -25.762 4.054   10.090  1.00 32.71  ? 96  TYR C O   1 
ATOM   5343 C  CB  . TYR C  1 110 ? -23.424 5.945   11.114  1.00 35.55  ? 96  TYR C CB  1 
ATOM   5344 C  CG  . TYR C  1 110 ? -22.115 6.707   10.927  1.00 35.62  ? 96  TYR C CG  1 
ATOM   5345 C  CD1 . TYR C  1 110 ? -20.922 6.048   10.647  1.00 37.43  ? 96  TYR C CD1 1 
ATOM   5346 C  CD2 . TYR C  1 110 ? -22.070 8.093   11.048  1.00 40.09  ? 96  TYR C CD2 1 
ATOM   5347 C  CE1 . TYR C  1 110 ? -19.733 6.742   10.481  1.00 38.86  ? 96  TYR C CE1 1 
ATOM   5348 C  CE2 . TYR C  1 110 ? -20.888 8.798   10.887  1.00 39.02  ? 96  TYR C CE2 1 
ATOM   5349 C  CZ  . TYR C  1 110 ? -19.715 8.120   10.601  1.00 38.59  ? 96  TYR C CZ  1 
ATOM   5350 O  OH  . TYR C  1 110 ? -18.543 8.800   10.438  1.00 42.04  ? 96  TYR C OH  1 
ATOM   5351 N  N   . LEU C  1 111 ? -24.882 3.056   11.914  1.00 28.25  ? 97  LEU C N   1 
ATOM   5352 C  CA  . LEU C  1 111 ? -26.054 2.237   12.195  1.00 29.11  ? 97  LEU C CA  1 
ATOM   5353 C  C   . LEU C  1 111 ? -27.283 3.119   12.417  1.00 29.31  ? 97  LEU C C   1 
ATOM   5354 O  O   . LEU C  1 111 ? -28.388 2.745   12.027  1.00 27.94  ? 97  LEU C O   1 
ATOM   5355 C  CB  . LEU C  1 111 ? -25.798 1.333   13.402  1.00 30.57  ? 97  LEU C CB  1 
ATOM   5356 C  CG  . LEU C  1 111 ? -26.988 0.486   13.869  1.00 29.91  ? 97  LEU C CG  1 
ATOM   5357 C  CD1 . LEU C  1 111 ? -27.342 -0.582  12.846  1.00 31.95  ? 97  LEU C CD1 1 
ATOM   5358 C  CD2 . LEU C  1 111 ? -26.721 -0.148  15.226  1.00 29.26  ? 97  LEU C CD2 1 
ATOM   5359 N  N   . HIS C  1 112 ? -27.093 4.281   13.055  1.00 31.09  ? 98  HIS C N   1 
ATOM   5360 C  CA  . HIS C  1 112 ? -28.215 5.152   13.374  1.00 29.25  ? 98  HIS C CA  1 
ATOM   5361 C  C   . HIS C  1 112 ? -28.853 5.638   12.073  1.00 29.02  ? 98  HIS C C   1 
ATOM   5362 O  O   . HIS C  1 112 ? -30.071 5.792   11.995  1.00 28.85  ? 98  HIS C O   1 
ATOM   5363 C  CB  . HIS C  1 112 ? -27.811 6.257   14.366  1.00 32.32  ? 98  HIS C CB  1 
ATOM   5364 C  CG  . HIS C  1 112 ? -26.925 7.349   13.850  1.00 37.90  ? 98  HIS C CG  1 
ATOM   5365 N  ND1 . HIS C  1 112 ? -27.401 8.460   13.185  1.00 41.89  ? 98  HIS C ND1 1 
ATOM   5366 C  CD2 . HIS C  1 112 ? -25.598 7.526   13.952  1.00 43.18  ? 98  HIS C CD2 1 
ATOM   5367 C  CE1 . HIS C  1 112 ? -26.387 9.258   12.876  1.00 44.95  ? 98  HIS C CE1 1 
ATOM   5368 N  NE2 . HIS C  1 112 ? -25.281 8.709   13.332  1.00 44.93  ? 98  HIS C NE2 1 
ATOM   5369 N  N   . ASN C  1 113 ? -28.023 5.836   11.043  1.00 30.40  ? 99  ASN C N   1 
ATOM   5370 C  CA  . ASN C  1 113 ? -28.494 6.327   9.757   1.00 32.64  ? 99  ASN C CA  1 
ATOM   5371 C  C   . ASN C  1 113 ? -29.187 5.187   9.007   1.00 33.15  ? 99  ASN C C   1 
ATOM   5372 O  O   . ASN C  1 113 ? -30.255 5.383   8.430   1.00 28.70  ? 99  ASN C O   1 
ATOM   5373 C  CB  . ASN C  1 113 ? -27.362 6.977   8.963   1.00 30.78  ? 99  ASN C CB  1 
ATOM   5374 C  CG  . ASN C  1 113 ? -26.917 8.294   9.558   1.00 31.37  ? 99  ASN C CG  1 
ATOM   5375 O  OD1 . ASN C  1 113 ? -27.673 8.929   10.303  1.00 32.45  ? 99  ASN C OD1 1 
ATOM   5376 N  ND2 . ASN C  1 113 ? -25.708 8.729   9.233   1.00 35.12  ? 99  ASN C ND2 1 
ATOM   5377 N  N   . ARG C  1 114 ? -28.575 3.995   9.026   1.00 31.19  ? 100 ARG C N   1 
ATOM   5378 C  CA  . ARG C  1 114 ? -29.154 2.827   8.378   1.00 27.97  ? 100 ARG C CA  1 
ATOM   5379 C  C   . ARG C  1 114 ? -30.561 2.589   8.923   1.00 29.69  ? 100 ARG C C   1 
ATOM   5380 O  O   . ARG C  1 114 ? -31.490 2.321   8.163   1.00 29.74  ? 100 ARG C O   1 
ATOM   5381 C  CB  . ARG C  1 114 ? -28.287 1.576   8.578   1.00 27.08  ? 100 ARG C CB  1 
ATOM   5382 C  CG  . ARG C  1 114 ? -27.016 1.528   7.741   1.00 28.94  ? 100 ARG C CG  1 
ATOM   5383 C  CD  . ARG C  1 114 ? -27.282 1.583   6.241   1.00 30.74  ? 100 ARG C CD  1 
ATOM   5384 N  NE  . ARG C  1 114 ? -26.031 1.489   5.481   1.00 29.73  ? 100 ARG C NE  1 
ATOM   5385 C  CZ  . ARG C  1 114 ? -25.878 1.852   4.214   1.00 30.80  ? 100 ARG C CZ  1 
ATOM   5386 N  NH1 . ARG C  1 114 ? -26.898 2.354   3.541   1.00 32.48  ? 100 ARG C NH1 1 
ATOM   5387 N  NH2 . ARG C  1 114 ? -24.698 1.724   3.632   1.00 29.58  ? 100 ARG C NH2 1 
ATOM   5388 N  N   . LEU C  1 115 ? -30.701 2.686   10.249  1.00 28.81  ? 101 LEU C N   1 
ATOM   5389 C  CA  . LEU C  1 115 ? -31.980 2.462   10.906  1.00 33.32  ? 101 LEU C CA  1 
ATOM   5390 C  C   . LEU C  1 115 ? -32.966 3.557   10.500  1.00 30.78  ? 101 LEU C C   1 
ATOM   5391 O  O   . LEU C  1 115 ? -34.137 3.277   10.249  1.00 28.97  ? 101 LEU C O   1 
ATOM   5392 C  CB  . LEU C  1 115 ? -31.771 2.403   12.421  1.00 31.23  ? 101 LEU C CB  1 
ATOM   5393 C  CG  . LEU C  1 115 ? -31.084 1.138   12.949  1.00 28.30  ? 101 LEU C CG  1 
ATOM   5394 C  CD1 . LEU C  1 115 ? -30.854 1.210   14.449  1.00 27.67  ? 101 LEU C CD1 1 
ATOM   5395 C  CD2 . LEU C  1 115 ? -31.892 -0.102  12.598  1.00 26.81  ? 101 LEU C CD2 1 
ATOM   5396 N  N   . GLU C  1 116 ? -32.475 4.801   10.423  1.00 36.42  ? 102 GLU C N   1 
ATOM   5397 C  CA  . GLU C  1 116 ? -33.308 5.944   10.082  1.00 36.87  ? 102 GLU C CA  1 
ATOM   5398 C  C   . GLU C  1 116 ? -33.922 5.734   8.699   1.00 34.10  ? 102 GLU C C   1 
ATOM   5399 O  O   . GLU C  1 116 ? -35.112 5.971   8.503   1.00 31.02  ? 102 GLU C O   1 
ATOM   5400 C  CB  . GLU C  1 116 ? -32.501 7.244   10.130  1.00 39.92  ? 102 GLU C CB  1 
ATOM   5401 C  CG  . GLU C  1 116 ? -33.347 8.498   9.919   1.00 41.62  ? 102 GLU C CG  1 
ATOM   5402 C  CD  . GLU C  1 116 ? -32.561 9.798   9.890   1.00 50.76  ? 102 GLU C CD  1 
ATOM   5403 O  OE1 . GLU C  1 116 ? -31.325 9.749   10.061  1.00 57.33  ? 102 GLU C OE1 1 
ATOM   5404 O  OE2 . GLU C  1 116 ? -33.188 10.861  9.692   1.00 58.66  ? 102 GLU C OE2 1 
ATOM   5405 N  N   . GLN C  1 117 ? -33.098 5.274   7.750   1.00 31.36  ? 103 GLN C N   1 
ATOM   5406 C  CA  . GLN C  1 117 ? -33.530 5.098   6.372   1.00 33.37  ? 103 GLN C CA  1 
ATOM   5407 C  C   . GLN C  1 117 ? -34.546 3.961   6.278   1.00 34.03  ? 103 GLN C C   1 
ATOM   5408 O  O   . GLN C  1 117 ? -35.125 3.733   5.219   1.00 36.04  ? 103 GLN C O   1 
ATOM   5409 C  CB  . GLN C  1 117 ? -32.328 4.874   5.452   1.00 36.78  ? 103 GLN C CB  1 
ATOM   5410 C  CG  . GLN C  1 117 ? -31.652 6.168   5.014   1.00 41.65  ? 103 GLN C CG  1 
ATOM   5411 C  CD  . GLN C  1 117 ? -32.653 7.211   4.565   1.00 43.40  ? 103 GLN C CD  1 
ATOM   5412 O  OE1 . GLN C  1 117 ? -33.326 7.062   3.540   1.00 50.02  ? 103 GLN C OE1 1 
ATOM   5413 N  NE2 . GLN C  1 117 ? -32.771 8.277   5.342   1.00 51.24  ? 103 GLN C NE2 1 
ATOM   5414 N  N   . LEU C  1 118 ? -34.755 3.256   7.396   1.00 32.04  ? 104 LEU C N   1 
ATOM   5415 C  CA  . LEU C  1 118 ? -35.767 2.214   7.485   1.00 30.13  ? 104 LEU C CA  1 
ATOM   5416 C  C   . LEU C  1 118 ? -36.927 2.698   8.356   1.00 25.75  ? 104 LEU C C   1 
ATOM   5417 O  O   . LEU C  1 118 ? -37.869 1.950   8.604   1.00 27.81  ? 104 LEU C O   1 
ATOM   5418 C  CB  . LEU C  1 118 ? -35.143 0.937   8.050   1.00 31.83  ? 104 LEU C CB  1 
ATOM   5419 C  CG  . LEU C  1 118 ? -34.177 0.187   7.127   1.00 33.63  ? 104 LEU C CG  1 
ATOM   5420 C  CD1 . LEU C  1 118 ? -33.485 -0.950  7.866   1.00 33.34  ? 104 LEU C CD1 1 
ATOM   5421 C  CD2 . LEU C  1 118 ? -34.905 -0.343  5.903   1.00 35.68  ? 104 LEU C CD2 1 
ATOM   5422 N  N   . LYS C  1 119 ? -36.834 3.948   8.828   1.00 30.67  ? 105 LYS C N   1 
ATOM   5423 C  CA  . LYS C  1 119 ? -37.862 4.540   9.673   1.00 34.27  ? 105 LYS C CA  1 
ATOM   5424 C  C   . LYS C  1 119 ? -37.949 3.760   10.985  1.00 33.54  ? 105 LYS C C   1 
ATOM   5425 O  O   . LYS C  1 119 ? -39.034 3.523   11.512  1.00 31.86  ? 105 LYS C O   1 
ATOM   5426 C  CB  . LYS C  1 119 ? -39.202 4.600   8.926   1.00 40.90  ? 105 LYS C CB  1 
ATOM   5427 C  CG  . LYS C  1 119 ? -39.283 5.682   7.853   1.00 44.97  ? 105 LYS C CG  1 
ATOM   5428 C  CD  . LYS C  1 119 ? -40.256 5.381   6.718   1.00 55.88  ? 105 LYS C CD  1 
ATOM   5429 C  CE  . LYS C  1 119 ? -41.705 5.472   7.102   1.00 60.36  ? 105 LYS C CE  1 
ATOM   5430 N  NZ  . LYS C  1 119 ? -42.586 5.092   5.992   1.00 65.23  ? 105 LYS C NZ  1 
ATOM   5431 N  N   . VAL C  1 120 ? -36.779 3.372   11.502  1.00 33.04  ? 106 VAL C N   1 
ATOM   5432 C  CA  . VAL C  1 120 ? -36.675 2.683   12.779  1.00 30.85  ? 106 VAL C CA  1 
ATOM   5433 C  C   . VAL C  1 120 ? -35.834 3.550   13.711  1.00 28.47  ? 106 VAL C C   1 
ATOM   5434 O  O   . VAL C  1 120 ? -34.707 3.908   13.375  1.00 30.44  ? 106 VAL C O   1 
ATOM   5435 C  CB  . VAL C  1 120 ? -36.059 1.277   12.615  1.00 28.79  ? 106 VAL C CB  1 
ATOM   5436 C  CG1 . VAL C  1 120 ? -35.817 0.594   13.956  1.00 28.77  ? 106 VAL C CG1 1 
ATOM   5437 C  CG2 . VAL C  1 120 ? -36.904 0.388   11.710  1.00 31.71  ? 106 VAL C CG2 1 
ATOM   5438 N  N   . ARG C  1 121 ? -36.400 3.900   14.872  0.99 30.24  ? 107 ARG C N   1 
ATOM   5439 C  CA  . ARG C  1 121 ? -35.669 4.658   15.875  0.99 38.02  ? 107 ARG C CA  1 
ATOM   5440 C  C   . ARG C  1 121 ? -34.990 3.679   16.829  0.99 32.78  ? 107 ARG C C   1 
ATOM   5441 O  O   . ARG C  1 121 ? -35.516 2.597   17.083  0.99 31.99  ? 107 ARG C O   1 
ATOM   5442 C  CB  . ARG C  1 121 ? -36.598 5.577   16.678  0.99 48.37  ? 107 ARG C CB  1 
ATOM   5443 C  CG  . ARG C  1 121 ? -37.693 6.266   15.876  0.99 56.73  ? 107 ARG C CG  1 
ATOM   5444 C  CD  . ARG C  1 121 ? -38.636 7.062   16.771  0.99 64.15  ? 107 ARG C CD  1 
ATOM   5445 N  NE  . ARG C  1 121 ? -39.442 8.022   16.010  0.99 76.84  ? 107 ARG C NE  1 
ATOM   5446 C  CZ  . ARG C  1 121 ? -39.748 9.248   16.419  0.99 83.69  ? 107 ARG C CZ  1 
ATOM   5447 N  NH1 . ARG C  1 121 ? -39.469 9.623   17.656  0.99 83.90  ? 107 ARG C NH1 1 
ATOM   5448 N  NH2 . ARG C  1 121 ? -40.366 10.083  15.601  0.99 77.89  ? 107 ARG C NH2 1 
ATOM   5449 N  N   . PRO C  1 122 ? -33.805 4.017   17.387  1.00 33.37  ? 108 PRO C N   1 
ATOM   5450 C  CA  . PRO C  1 122 ? -33.180 3.179   18.412  1.00 33.79  ? 108 PRO C CA  1 
ATOM   5451 C  C   . PRO C  1 122 ? -34.160 2.746   19.502  1.00 32.55  ? 108 PRO C C   1 
ATOM   5452 O  O   . PRO C  1 122 ? -34.051 1.643   20.032  1.00 35.84  ? 108 PRO C O   1 
ATOM   5453 C  CB  . PRO C  1 122 ? -32.057 4.086   18.949  1.00 33.44  ? 108 PRO C CB  1 
ATOM   5454 C  CG  . PRO C  1 122 ? -31.680 4.949   17.761  1.00 36.94  ? 108 PRO C CG  1 
ATOM   5455 C  CD  . PRO C  1 122 ? -32.997 5.200   17.042  1.00 34.94  ? 108 PRO C CD  1 
ATOM   5456 N  N   . GLU C  1 123 ? -35.132 3.615   19.813  1.00 34.76  ? 109 GLU C N   1 
ATOM   5457 C  CA  . GLU C  1 123 ? -36.061 3.383   20.911  1.00 34.78  ? 109 GLU C CA  1 
ATOM   5458 C  C   . GLU C  1 123 ? -37.065 2.287   20.556  1.00 30.81  ? 109 GLU C C   1 
ATOM   5459 O  O   . GLU C  1 123 ? -37.750 1.771   21.436  1.00 35.66  ? 109 GLU C O   1 
ATOM   5460 C  CB  . GLU C  1 123 ? -36.806 4.666   21.288  1.00 43.61  ? 109 GLU C CB  1 
ATOM   5461 C  CG  . GLU C  1 123 ? -37.718 5.197   20.185  1.00 49.57  ? 109 GLU C CG  1 
ATOM   5462 C  CD  . GLU C  1 123 ? -38.533 6.417   20.578  1.00 58.26  ? 109 GLU C CD  1 
ATOM   5463 O  OE1 . GLU C  1 123 ? -38.260 7.507   20.032  1.00 64.96  ? 109 GLU C OE1 1 
ATOM   5464 O  OE2 . GLU C  1 123 ? -39.444 6.277   21.422  1.00 65.17  ? 109 GLU C OE2 1 
ATOM   5465 N  N   . ASP C  1 124 ? -37.159 1.940   19.267  1.00 32.87  ? 110 ASP C N   1 
ATOM   5466 C  CA  . ASP C  1 124 ? -38.125 0.952   18.810  1.00 35.30  ? 110 ASP C CA  1 
ATOM   5467 C  C   . ASP C  1 124 ? -37.565 -0.460  18.986  1.00 32.96  ? 110 ASP C C   1 
ATOM   5468 O  O   . ASP C  1 124 ? -38.306 -1.438  18.894  1.00 32.46  ? 110 ASP C O   1 
ATOM   5469 C  CB  . ASP C  1 124 ? -38.543 1.201   17.367  1.00 41.16  ? 110 ASP C CB  1 
ATOM   5470 C  CG  . ASP C  1 124 ? -39.137 2.574   17.082  1.00 44.50  ? 110 ASP C CG  1 
ATOM   5471 O  OD1 . ASP C  1 124 ? -40.019 3.001   17.857  1.00 42.06  ? 110 ASP C OD1 1 
ATOM   5472 O  OD2 . ASP C  1 124 ? -38.724 3.196   16.081  1.00 43.75  ? 110 ASP C OD2 1 
ATOM   5473 N  N   . ILE C  1 125 ? -36.254 -0.563  19.237  1.00 30.85  ? 111 ILE C N   1 
ATOM   5474 C  CA  . ILE C  1 125 ? -35.592 -1.856  19.340  1.00 28.67  ? 111 ILE C CA  1 
ATOM   5475 C  C   . ILE C  1 125 ? -35.888 -2.472  20.709  1.00 25.47  ? 111 ILE C C   1 
ATOM   5476 O  O   . ILE C  1 125 ? -35.551 -1.891  21.739  1.00 29.36  ? 111 ILE C O   1 
ATOM   5477 C  CB  . ILE C  1 125 ? -34.076 -1.724  19.087  1.00 25.77  ? 111 ILE C CB  1 
ATOM   5478 C  CG1 . ILE C  1 125 ? -33.770 -1.056  17.740  1.00 28.24  ? 111 ILE C CG1 1 
ATOM   5479 C  CG2 . ILE C  1 125 ? -33.387 -3.084  19.207  1.00 26.65  ? 111 ILE C CG2 1 
ATOM   5480 C  CD1 . ILE C  1 125 ? -34.153 -1.890  16.530  1.00 29.33  ? 111 ILE C CD1 1 
ATOM   5481 N  N   . ARG C  1 126 ? -36.508 -3.662  20.706  1.00 28.51  ? 112 ARG C N   1 
ATOM   5482 C  CA  . ARG C  1 126 ? -36.879 -4.358  21.930  1.00 29.88  ? 112 ARG C CA  1 
ATOM   5483 C  C   . ARG C  1 126 ? -35.680 -5.132  22.481  1.00 29.39  ? 112 ARG C C   1 
ATOM   5484 O  O   . ARG C  1 126 ? -35.426 -5.109  23.685  1.00 28.25  ? 112 ARG C O   1 
ATOM   5485 C  CB  . ARG C  1 126 ? -38.053 -5.319  21.693  1.00 30.65  ? 112 ARG C CB  1 
ATOM   5486 C  CG  . ARG C  1 126 ? -38.742 -5.803  22.963  1.00 34.15  ? 112 ARG C CG  1 
ATOM   5487 C  CD  . ARG C  1 126 ? -39.764 -6.907  22.719  1.00 35.56  ? 112 ARG C CD  1 
ATOM   5488 N  NE  . ARG C  1 126 ? -40.366 -7.388  23.969  1.00 37.60  ? 112 ARG C NE  1 
ATOM   5489 C  CZ  . ARG C  1 126 ? -41.234 -8.390  24.063  1.00 42.42  ? 112 ARG C CZ  1 
ATOM   5490 N  NH1 . ARG C  1 126 ? -41.606 -9.050  22.980  1.00 42.55  ? 112 ARG C NH1 1 
ATOM   5491 N  NH2 . ARG C  1 126 ? -41.726 -8.732  25.241  1.00 48.86  ? 112 ARG C NH2 1 
ATOM   5492 N  N   . TYR C  1 127 ? -34.959 -5.829  21.592  1.00 26.96  ? 113 TYR C N   1 
ATOM   5493 C  CA  . TYR C  1 127 ? -33.829 -6.660  21.985  1.00 28.54  ? 113 TYR C CA  1 
ATOM   5494 C  C   . TYR C  1 127 ? -32.627 -6.377  21.086  1.00 23.99  ? 113 TYR C C   1 
ATOM   5495 O  O   . TYR C  1 127 ? -32.767 -6.303  19.868  1.00 25.03  ? 113 TYR C O   1 
ATOM   5496 C  CB  . TYR C  1 127 ? -34.155 -8.157  21.894  1.00 28.95  ? 113 TYR C CB  1 
ATOM   5497 C  CG  . TYR C  1 127 ? -35.263 -8.655  22.815  1.00 29.35  ? 113 TYR C CG  1 
ATOM   5498 C  CD1 . TYR C  1 127 ? -35.081 -8.710  24.192  1.00 32.52  ? 113 TYR C CD1 1 
ATOM   5499 C  CD2 . TYR C  1 127 ? -36.476 -9.107  22.307  1.00 29.78  ? 113 TYR C CD2 1 
ATOM   5500 C  CE1 . TYR C  1 127 ? -36.080 -9.170  25.036  1.00 29.31  ? 113 TYR C CE1 1 
ATOM   5501 C  CE2 . TYR C  1 127 ? -37.482 -9.573  23.139  1.00 30.20  ? 113 TYR C CE2 1 
ATOM   5502 C  CZ  . TYR C  1 127 ? -37.283 -9.606  24.508  1.00 32.93  ? 113 TYR C CZ  1 
ATOM   5503 O  OH  . TYR C  1 127 ? -38.267 -10.065 25.337  1.00 36.30  ? 113 TYR C OH  1 
ATOM   5504 N  N   . VAL C  1 128 ? -31.452 -6.219  21.712  1.00 23.70  ? 114 VAL C N   1 
ATOM   5505 C  CA  . VAL C  1 128 ? -30.170 -6.237  21.024  1.00 21.74  ? 114 VAL C CA  1 
ATOM   5506 C  C   . VAL C  1 128 ? -29.440 -7.511  21.448  1.00 21.97  ? 114 VAL C C   1 
ATOM   5507 O  O   . VAL C  1 128 ? -29.260 -7.747  22.641  1.00 21.61  ? 114 VAL C O   1 
ATOM   5508 C  CB  . VAL C  1 128 ? -29.320 -4.985  21.330  1.00 24.36  ? 114 VAL C CB  1 
ATOM   5509 C  CG1 . VAL C  1 128 ? -27.983 -4.995  20.593  1.00 25.74  ? 114 VAL C CG1 1 
ATOM   5510 C  CG2 . VAL C  1 128 ? -30.076 -3.691  21.041  1.00 24.66  ? 114 VAL C CG2 1 
ATOM   5511 N  N   . VAL C  1 129 ? -29.045 -8.338  20.470  1.00 21.74  ? 115 VAL C N   1 
ATOM   5512 C  CA  . VAL C  1 129 ? -28.202 -9.495  20.732  1.00 21.04  ? 115 VAL C CA  1 
ATOM   5513 C  C   . VAL C  1 129 ? -26.758 -9.128  20.388  1.00 21.10  ? 115 VAL C C   1 
ATOM   5514 O  O   . VAL C  1 129 ? -26.442 -8.883  19.228  1.00 17.97  ? 115 VAL C O   1 
ATOM   5515 C  CB  . VAL C  1 129 ? -28.649 -10.749 19.953  1.00 22.61  ? 115 VAL C CB  1 
ATOM   5516 C  CG1 . VAL C  1 129 ? -27.702 -11.922 20.184  1.00 22.16  ? 115 VAL C CG1 1 
ATOM   5517 C  CG2 . VAL C  1 129 ? -30.086 -11.148 20.274  1.00 23.11  ? 115 VAL C CG2 1 
ATOM   5518 N  N   . ALA C  1 130 ? -25.894 -9.084  21.410  1.00 21.05  ? 116 ALA C N   1 
ATOM   5519 C  CA  . ALA C  1 130 ? -24.473 -8.835  21.222  1.00 23.14  ? 116 ALA C CA  1 
ATOM   5520 C  C   . ALA C  1 130 ? -23.741 -10.165 21.060  1.00 22.34  ? 116 ALA C C   1 
ATOM   5521 O  O   . ALA C  1 130 ? -23.521 -10.879 22.036  1.00 23.13  ? 116 ALA C O   1 
ATOM   5522 C  CB  . ALA C  1 130 ? -23.920 -8.047  22.394  1.00 26.16  ? 116 ALA C CB  1 
ATOM   5523 N  N   . SER C  1 131 ? -23.368 -10.493 19.819  1.00 23.02  ? 117 SER C N   1 
ATOM   5524 C  CA  . SER C  1 131 ? -22.651 -11.729 19.547  1.00 22.90  ? 117 SER C CA  1 
ATOM   5525 C  C   . SER C  1 131 ? -21.448 -11.833 20.482  1.00 20.85  ? 117 SER C C   1 
ATOM   5526 O  O   . SER C  1 131 ? -21.176 -12.897 21.036  1.00 20.82  ? 117 SER C O   1 
ATOM   5527 C  CB  . SER C  1 131 ? -22.236 -11.812 18.102  1.00 21.60  ? 117 SER C CB  1 
ATOM   5528 O  OG  . SER C  1 131 ? -21.347 -10.758 17.762  1.00 22.02  ? 117 SER C OG  1 
ATOM   5529 N  N   . HIS C  1 132 ? -20.738 -10.707 20.621  1.00 18.88  ? 118 HIS C N   1 
ATOM   5530 C  CA  . HIS C  1 132 ? -19.669 -10.524 21.591  1.00 19.89  ? 118 HIS C CA  1 
ATOM   5531 C  C   . HIS C  1 132 ? -19.418 -9.019  21.704  1.00 20.44  ? 118 HIS C C   1 
ATOM   5532 O  O   . HIS C  1 132 ? -20.105 -8.236  21.053  1.00 21.21  ? 118 HIS C O   1 
ATOM   5533 C  CB  . HIS C  1 132 ? -18.439 -11.372 21.234  1.00 20.11  ? 118 HIS C CB  1 
ATOM   5534 C  CG  . HIS C  1 132 ? -17.797 -11.043 19.924  1.00 20.58  ? 118 HIS C CG  1 
ATOM   5535 N  ND1 . HIS C  1 132 ? -18.485 -10.963 18.733  1.00 20.61  ? 118 HIS C ND1 1 
ATOM   5536 C  CD2 . HIS C  1 132 ? -16.508 -10.819 19.623  1.00 20.30  ? 118 HIS C CD2 1 
ATOM   5537 C  CE1 . HIS C  1 132 ? -17.633 -10.674 17.756  1.00 20.84  ? 118 HIS C CE1 1 
ATOM   5538 N  NE2 . HIS C  1 132 ? -16.428 -10.580 18.277  1.00 17.65  ? 118 HIS C NE2 1 
ATOM   5539 N  N   . LEU C  1 133 ? -18.445 -8.607  22.525  1.00 19.88  ? 119 LEU C N   1 
ATOM   5540 C  CA  . LEU C  1 133 ? -18.311 -7.200  22.876  1.00 20.29  ? 119 LEU C CA  1 
ATOM   5541 C  C   . LEU C  1 133 ? -17.051 -6.585  22.261  1.00 20.21  ? 119 LEU C C   1 
ATOM   5542 O  O   . LEU C  1 133 ? -16.521 -5.608  22.786  1.00 24.92  ? 119 LEU C O   1 
ATOM   5543 C  CB  . LEU C  1 133 ? -18.337 -7.075  24.400  1.00 20.76  ? 119 LEU C CB  1 
ATOM   5544 C  CG  . LEU C  1 133 ? -19.678 -7.404  25.070  1.00 20.71  ? 119 LEU C CG  1 
ATOM   5545 C  CD1 . LEU C  1 133 ? -19.601 -7.245  26.581  1.00 22.98  ? 119 LEU C CD1 1 
ATOM   5546 C  CD2 . LEU C  1 133 ? -20.796 -6.542  24.506  1.00 20.50  ? 119 LEU C CD2 1 
ATOM   5547 N  N   . HIS C  1 134 ? -16.601 -7.134  21.125  1.00 19.05  ? 120 HIS C N   1 
ATOM   5548 C  CA  . HIS C  1 134 ? -15.488 -6.571  20.368  1.00 20.71  ? 120 HIS C CA  1 
ATOM   5549 C  C   . HIS C  1 134 ? -15.898 -5.240  19.731  1.00 22.71  ? 120 HIS C C   1 
ATOM   5550 O  O   . HIS C  1 134 ? -17.085 -4.954  19.587  1.00 21.60  ? 120 HIS C O   1 
ATOM   5551 C  CB  . HIS C  1 134 ? -14.979 -7.563  19.313  1.00 21.58  ? 120 HIS C CB  1 
ATOM   5552 C  CG  . HIS C  1 134 ? -13.958 -8.540  19.806  1.00 20.32  ? 120 HIS C CG  1 
ATOM   5553 N  ND1 . HIS C  1 134 ? -13.566 -9.643  19.077  1.00 23.84  ? 120 HIS C ND1 1 
ATOM   5554 C  CD2 . HIS C  1 134 ? -13.225 -8.564  20.929  1.00 21.67  ? 120 HIS C CD2 1 
ATOM   5555 C  CE1 . HIS C  1 134 ? -12.639 -10.311 19.753  1.00 23.30  ? 120 HIS C CE1 1 
ATOM   5556 N  NE2 . HIS C  1 134 ? -12.416 -9.672  20.881  1.00 22.88  ? 120 HIS C NE2 1 
ATOM   5557 N  N   . LEU C  1 135 ? -14.888 -4.456  19.324  1.00 24.80  ? 121 LEU C N   1 
ATOM   5558 C  CA  . LEU C  1 135 ? -15.053 -3.065  18.920  1.00 26.26  ? 121 LEU C CA  1 
ATOM   5559 C  C   . LEU C  1 135 ? -16.037 -2.935  17.758  1.00 25.98  ? 121 LEU C C   1 
ATOM   5560 O  O   . LEU C  1 135 ? -16.772 -1.952  17.688  1.00 27.68  ? 121 LEU C O   1 
ATOM   5561 C  CB  . LEU C  1 135 ? -13.692 -2.458  18.564  1.00 26.21  ? 121 LEU C CB  1 
ATOM   5562 C  CG  . LEU C  1 135 ? -12.973 -3.042  17.342  1.00 29.51  ? 121 LEU C CG  1 
ATOM   5563 C  CD1 . LEU C  1 135 ? -11.659 -2.310  17.083  1.00 28.20  ? 121 LEU C CD1 1 
ATOM   5564 C  CD2 . LEU C  1 135 ? -12.726 -4.534  17.498  1.00 28.22  ? 121 LEU C CD2 1 
ATOM   5565 N  N   . ASN C  1 136 ? -16.046 -3.916  16.845  1.00 26.60  ? 122 ASN C N   1 
ATOM   5566 C  CA  . ASN C  1 136 ? -16.824 -3.794  15.621  1.00 27.13  ? 122 ASN C CA  1 
ATOM   5567 C  C   . ASN C  1 136 ? -18.174 -4.500  15.759  1.00 26.16  ? 122 ASN C C   1 
ATOM   5568 O  O   . ASN C  1 136 ? -18.860 -4.698  14.758  1.00 26.60  ? 122 ASN C O   1 
ATOM   5569 C  CB  . ASN C  1 136 ? -16.043 -4.263  14.394  1.00 28.90  ? 122 ASN C CB  1 
ATOM   5570 C  CG  . ASN C  1 136 ? -15.420 -5.629  14.560  1.00 33.48  ? 122 ASN C CG  1 
ATOM   5571 O  OD1 . ASN C  1 136 ? -15.562 -6.261  15.613  1.00 34.92  ? 122 ASN C OD1 1 
ATOM   5572 N  ND2 . ASN C  1 136 ? -14.725 -6.098  13.534  1.00 38.99  ? 122 ASN C ND2 1 
ATOM   5573 N  N   . HIS C  1 137 ? -18.572 -4.844  16.994  1.00 25.69  ? 123 HIS C N   1 
ATOM   5574 C  CA  . HIS C  1 137 ? -19.852 -5.504  17.220  1.00 22.73  ? 123 HIS C CA  1 
ATOM   5575 C  C   . HIS C  1 137 ? -20.688 -4.778  18.275  1.00 20.25  ? 123 HIS C C   1 
ATOM   5576 O  O   . HIS C  1 137 ? -21.915 -4.802  18.201  1.00 23.03  ? 123 HIS C O   1 
ATOM   5577 C  CB  . HIS C  1 137 ? -19.649 -6.988  17.560  1.00 23.39  ? 123 HIS C CB  1 
ATOM   5578 C  CG  . HIS C  1 137 ? -19.039 -7.761  16.439  1.00 24.34  ? 123 HIS C CG  1 
ATOM   5579 N  ND1 . HIS C  1 137 ? -19.762 -8.581  15.598  1.00 26.21  ? 123 HIS C ND1 1 
ATOM   5580 C  CD2 . HIS C  1 137 ? -17.768 -7.824  16.017  1.00 26.78  ? 123 HIS C CD2 1 
ATOM   5581 C  CE1 . HIS C  1 137 ? -18.943 -9.120  14.705  1.00 26.93  ? 123 HIS C CE1 1 
ATOM   5582 N  NE2 . HIS C  1 137 ? -17.728 -8.671  14.939  1.00 26.39  ? 123 HIS C NE2 1 
ATOM   5583 N  N   . ALA C  1 138 ? -20.031 -4.136  19.251  1.00 21.11  ? 124 ALA C N   1 
ATOM   5584 C  CA  . ALA C  1 138 ? -20.728 -3.568  20.396  1.00 23.39  ? 124 ALA C CA  1 
ATOM   5585 C  C   . ALA C  1 138 ? -20.623 -2.042  20.414  1.00 24.02  ? 124 ALA C C   1 
ATOM   5586 O  O   . ALA C  1 138 ? -20.988 -1.410  21.402  1.00 24.49  ? 124 ALA C O   1 
ATOM   5587 C  CB  . ALA C  1 138 ? -20.171 -4.165  21.675  1.00 25.12  ? 124 ALA C CB  1 
ATOM   5588 N  N   . GLY C  1 139 ? -20.151 -1.457  19.308  1.00 24.84  ? 125 GLY C N   1 
ATOM   5589 C  CA  . GLY C  1 139 ? -19.807 -0.043  19.250  1.00 25.27  ? 125 GLY C CA  1 
ATOM   5590 C  C   . GLY C  1 139 ? -20.991 0.895   19.502  1.00 26.58  ? 125 GLY C C   1 
ATOM   5591 O  O   . GLY C  1 139 ? -20.788 2.028   19.937  1.00 29.05  ? 125 GLY C O   1 
ATOM   5592 N  N   . CYS C  1 140 ? -22.221 0.435   19.231  1.00 25.52  ? 126 CYS C N   1 
ATOM   5593 C  CA  . CYS C  1 140 ? -23.389 1.307   19.279  1.00 26.00  ? 126 CYS C CA  1 
ATOM   5594 C  C   . CYS C  1 140 ? -24.438 0.808   20.274  1.00 27.39  ? 126 CYS C C   1 
ATOM   5595 O  O   . CYS C  1 140 ? -25.594 1.228   20.215  1.00 27.12  ? 126 CYS C O   1 
ATOM   5596 C  CB  . CYS C  1 140 ? -24.028 1.455   17.900  1.00 27.25  ? 126 CYS C CB  1 
ATOM   5597 S  SG  . CYS C  1 140 ? -23.007 2.362   16.708  1.00 29.26  ? 126 CYS C SG  1 
ATOM   5598 N  N   . LEU C  1 141 ? -24.033 -0.068  21.203  1.00 26.47  ? 127 LEU C N   1 
ATOM   5599 C  CA  . LEU C  1 141 ? -24.935 -0.579  22.226  1.00 23.73  ? 127 LEU C CA  1 
ATOM   5600 C  C   . LEU C  1 141 ? -25.622 0.577   22.953  1.00 23.98  ? 127 LEU C C   1 
ATOM   5601 O  O   . LEU C  1 141 ? -26.780 0.464   23.351  1.00 25.42  ? 127 LEU C O   1 
ATOM   5602 C  CB  . LEU C  1 141 ? -24.159 -1.448  23.218  1.00 23.91  ? 127 LEU C CB  1 
ATOM   5603 C  CG  . LEU C  1 141 ? -23.830 -2.875  22.770  1.00 27.28  ? 127 LEU C CG  1 
ATOM   5604 C  CD1 . LEU C  1 141 ? -23.101 -3.625  23.876  1.00 28.74  ? 127 LEU C CD1 1 
ATOM   5605 C  CD2 . LEU C  1 141 ? -25.084 -3.626  22.355  1.00 24.43  ? 127 LEU C CD2 1 
ATOM   5606 N  N   . GLU C  1 142 ? -24.889 1.682   23.135  1.00 27.49  ? 128 GLU C N   1 
ATOM   5607 C  CA  . GLU C  1 142 ? -25.309 2.759   24.019  1.00 32.25  ? 128 GLU C CA  1 
ATOM   5608 C  C   . GLU C  1 142 ? -26.549 3.463   23.467  1.00 33.09  ? 128 GLU C C   1 
ATOM   5609 O  O   . GLU C  1 142 ? -27.223 4.189   24.193  1.00 32.91  ? 128 GLU C O   1 
ATOM   5610 C  CB  . GLU C  1 142 ? -24.151 3.739   24.224  1.00 35.52  ? 128 GLU C CB  1 
ATOM   5611 C  CG  . GLU C  1 142 ? -23.763 4.507   22.964  1.00 35.15  ? 128 GLU C CG  1 
ATOM   5612 C  CD  . GLU C  1 142 ? -22.434 5.235   23.063  1.00 34.87  ? 128 GLU C CD  1 
ATOM   5613 O  OE1 . GLU C  1 142 ? -22.452 6.476   23.211  1.00 39.91  ? 128 GLU C OE1 1 
ATOM   5614 O  OE2 . GLU C  1 142 ? -21.382 4.567   22.976  1.00 29.71  ? 128 GLU C OE2 1 
ATOM   5615 N  N   . MET C  1 143 ? -26.849 3.232   22.184  1.00 35.67  ? 129 MET C N   1 
ATOM   5616 C  CA  . MET C  1 143 ? -27.974 3.869   21.516  1.00 34.71  ? 129 MET C CA  1 
ATOM   5617 C  C   . MET C  1 143 ? -29.299 3.284   22.003  1.00 28.88  ? 129 MET C C   1 
ATOM   5618 O  O   . MET C  1 143 ? -30.323 3.963   21.995  1.00 29.29  ? 129 MET C O   1 
ATOM   5619 C  CB  . MET C  1 143 ? -27.894 3.657   20.000  1.00 40.59  ? 129 MET C CB  1 
ATOM   5620 C  CG  . MET C  1 143 ? -27.056 4.682   19.259  1.00 44.01  ? 129 MET C CG  1 
ATOM   5621 S  SD  . MET C  1 143 ? -26.706 4.158   17.569  1.00 46.06  ? 129 MET C SD  1 
ATOM   5622 C  CE  . MET C  1 143 ? -28.366 3.763   17.003  1.00 46.65  ? 129 MET C CE  1 
ATOM   5623 N  N   . PHE C  1 144 ? -29.270 2.012   22.415  1.00 27.27  ? 130 PHE C N   1 
ATOM   5624 C  CA  . PHE C  1 144 ? -30.489 1.238   22.598  1.00 30.11  ? 130 PHE C CA  1 
ATOM   5625 C  C   . PHE C  1 144 ? -30.868 1.224   24.075  1.00 31.94  ? 130 PHE C C   1 
ATOM   5626 O  O   . PHE C  1 144 ? -30.821 0.187   24.735  1.00 32.30  ? 130 PHE C O   1 
ATOM   5627 C  CB  . PHE C  1 144 ? -30.268 -0.137  21.959  1.00 29.24  ? 130 PHE C CB  1 
ATOM   5628 C  CG  . PHE C  1 144 ? -29.826 0.000   20.510  1.00 30.55  ? 130 PHE C CG  1 
ATOM   5629 C  CD1 . PHE C  1 144 ? -30.717 0.442   19.540  1.00 35.27  ? 130 PHE C CD1 1 
ATOM   5630 C  CD2 . PHE C  1 144 ? -28.515 -0.267  20.131  1.00 32.93  ? 130 PHE C CD2 1 
ATOM   5631 C  CE1 . PHE C  1 144 ? -30.312 0.594   18.224  1.00 33.66  ? 130 PHE C CE1 1 
ATOM   5632 C  CE2 . PHE C  1 144 ? -28.117 -0.117  18.812  1.00 33.76  ? 130 PHE C CE2 1 
ATOM   5633 C  CZ  . PHE C  1 144 ? -29.016 0.313   17.863  1.00 32.07  ? 130 PHE C CZ  1 
ATOM   5634 N  N   . THR C  1 145 ? -31.274 2.400   24.563  1.00 30.86  ? 131 THR C N   1 
ATOM   5635 C  CA  . THR C  1 145 ? -31.549 2.612   25.974  1.00 33.47  ? 131 THR C CA  1 
ATOM   5636 C  C   . THR C  1 145 ? -32.931 2.057   26.325  1.00 31.28  ? 131 THR C C   1 
ATOM   5637 O  O   . THR C  1 145 ? -33.310 2.043   27.492  1.00 31.08  ? 131 THR C O   1 
ATOM   5638 C  CB  . THR C  1 145 ? -31.433 4.101   26.308  1.00 34.92  ? 131 THR C CB  1 
ATOM   5639 O  OG1 . THR C  1 145 ? -32.349 4.776   25.450  1.00 35.43  ? 131 THR C OG1 1 
ATOM   5640 C  CG2 . THR C  1 145 ? -30.032 4.651   26.098  1.00 35.56  ? 131 THR C CG2 1 
ATOM   5641 N  N   . ASN C  1 146 ? -33.675 1.580   25.318  1.00 30.63  ? 132 ASN C N   1 
ATOM   5642 C  CA  . ASN C  1 146 ? -35.032 1.099   25.539  1.00 31.79  ? 132 ASN C CA  1 
ATOM   5643 C  C   . ASN C  1 146 ? -35.087 -0.420  25.375  1.00 31.77  ? 132 ASN C C   1 
ATOM   5644 O  O   . ASN C  1 146 ? -36.131 -1.032  25.592  1.00 33.09  ? 132 ASN C O   1 
ATOM   5645 C  CB  . ASN C  1 146 ? -36.032 1.786   24.611  1.00 36.36  ? 132 ASN C CB  1 
ATOM   5646 C  CG  . ASN C  1 146 ? -37.431 1.798   25.183  1.00 47.02  ? 132 ASN C CG  1 
ATOM   5647 O  OD1 . ASN C  1 146 ? -37.636 2.289   26.298  1.00 44.02  ? 132 ASN C OD1 1 
ATOM   5648 N  ND2 . ASN C  1 146 ? -38.399 1.268   24.448  1.00 52.65  ? 132 ASN C ND2 1 
ATOM   5649 N  N   . ALA C  1 147 ? -33.955 -1.021  24.992  1.00 28.17  ? 133 ALA C N   1 
ATOM   5650 C  CA  . ALA C  1 147 ? -33.905 -2.441  24.679  1.00 27.34  ? 133 ALA C CA  1 
ATOM   5651 C  C   . ALA C  1 147 ? -33.384 -3.238  25.875  1.00 26.20  ? 133 ALA C C   1 
ATOM   5652 O  O   . ALA C  1 147 ? -32.814 -2.672  26.804  1.00 25.82  ? 133 ALA C O   1 
ATOM   5653 C  CB  . ALA C  1 147 ? -33.033 -2.660  23.459  1.00 28.21  ? 133 ALA C CB  1 
ATOM   5654 N  N   . THR C  1 148 ? -33.614 -4.557  25.843  1.00 25.92  ? 134 THR C N   1 
ATOM   5655 C  CA  . THR C  1 148 ? -32.868 -5.496  26.669  1.00 26.42  ? 134 THR C CA  1 
ATOM   5656 C  C   . THR C  1 148 ? -31.640 -5.937  25.873  1.00 24.43  ? 134 THR C C   1 
ATOM   5657 O  O   . THR C  1 148 ? -31.774 -6.413  24.749  1.00 24.92  ? 134 THR C O   1 
ATOM   5658 C  CB  . THR C  1 148 ? -33.741 -6.690  27.066  1.00 26.84  ? 134 THR C CB  1 
ATOM   5659 O  OG1 . THR C  1 148 ? -34.857 -6.170  27.785  1.00 27.20  ? 134 THR C OG1 1 
ATOM   5660 C  CG2 . THR C  1 148 ? -32.993 -7.703  27.916  1.00 27.84  ? 134 THR C CG2 1 
ATOM   5661 N  N   . ILE C  1 149 ? -30.447 -5.750  26.451  1.00 23.97  ? 135 ILE C N   1 
ATOM   5662 C  CA  . ILE C  1 149 ? -29.199 -6.112  25.792  1.00 22.23  ? 135 ILE C CA  1 
ATOM   5663 C  C   . ILE C  1 149 ? -28.814 -7.527  26.223  1.00 21.52  ? 135 ILE C C   1 
ATOM   5664 O  O   . ILE C  1 149 ? -28.453 -7.755  27.375  1.00 21.24  ? 135 ILE C O   1 
ATOM   5665 C  CB  . ILE C  1 149 ? -28.077 -5.101  26.104  1.00 23.10  ? 135 ILE C CB  1 
ATOM   5666 C  CG1 . ILE C  1 149 ? -28.532 -3.647  25.920  1.00 25.43  ? 135 ILE C CG1 1 
ATOM   5667 C  CG2 . ILE C  1 149 ? -26.822 -5.407  25.283  1.00 23.58  ? 135 ILE C CG2 1 
ATOM   5668 C  CD1 . ILE C  1 149 ? -29.118 -3.342  24.554  1.00 24.60  ? 135 ILE C CD1 1 
ATOM   5669 N  N   . ILE C  1 150 ? -28.888 -8.469  25.277  1.00 20.37  ? 136 ILE C N   1 
ATOM   5670 C  CA  . ILE C  1 150 ? -28.560 -9.861  25.539  1.00 19.69  ? 136 ILE C CA  1 
ATOM   5671 C  C   . ILE C  1 150 ? -27.093 -10.089 25.171  1.00 20.59  ? 136 ILE C C   1 
ATOM   5672 O  O   . ILE C  1 150 ? -26.678 -9.817  24.048  1.00 21.57  ? 136 ILE C O   1 
ATOM   5673 C  CB  . ILE C  1 150 ? -29.537 -10.784 24.783  1.00 22.60  ? 136 ILE C CB  1 
ATOM   5674 C  CG1 . ILE C  1 150 ? -30.997 -10.407 25.085  1.00 22.44  ? 136 ILE C CG1 1 
ATOM   5675 C  CG2 . ILE C  1 150 ? -29.258 -12.258 25.083  1.00 21.29  ? 136 ILE C CG2 1 
ATOM   5676 C  CD1 . ILE C  1 150 ? -32.031 -11.216 24.322  1.00 23.37  ? 136 ILE C CD1 1 
ATOM   5677 N  N   . VAL C  1 151 ? -26.309 -10.557 26.153  1.00 18.74  ? 137 VAL C N   1 
ATOM   5678 C  CA  . VAL C  1 151 ? -24.878 -10.776 25.999  1.00 19.10  ? 137 VAL C CA  1 
ATOM   5679 C  C   . VAL C  1 151 ? -24.497 -12.001 26.832  1.00 18.52  ? 137 VAL C C   1 
ATOM   5680 O  O   . VAL C  1 151 ? -25.167 -12.315 27.814  1.00 18.35  ? 137 VAL C O   1 
ATOM   5681 C  CB  . VAL C  1 151 ? -24.079 -9.522  26.415  1.00 20.52  ? 137 VAL C CB  1 
ATOM   5682 C  CG1 . VAL C  1 151 ? -24.275 -9.182  27.887  1.00 20.60  ? 137 VAL C CG1 1 
ATOM   5683 C  CG2 . VAL C  1 151 ? -22.592 -9.643  26.092  1.00 20.16  ? 137 VAL C CG2 1 
ATOM   5684 N  N   . HIS C  1 152 ? -23.443 -12.716 26.415  1.00 16.37  ? 138 HIS C N   1 
ATOM   5685 C  CA  . HIS C  1 152 ? -22.955 -13.856 27.177  1.00 16.12  ? 138 HIS C CA  1 
ATOM   5686 C  C   . HIS C  1 152 ? -22.296 -13.327 28.450  1.00 17.40  ? 138 HIS C C   1 
ATOM   5687 O  O   . HIS C  1 152 ? -21.555 -12.349 28.394  1.00 15.76  ? 138 HIS C O   1 
ATOM   5688 C  CB  . HIS C  1 152 ? -21.982 -14.704 26.348  1.00 16.15  ? 138 HIS C CB  1 
ATOM   5689 C  CG  . HIS C  1 152 ? -21.732 -16.063 26.918  1.00 17.35  ? 138 HIS C CG  1 
ATOM   5690 N  ND1 . HIS C  1 152 ? -21.071 -16.268 28.110  1.00 16.60  ? 138 HIS C ND1 1 
ATOM   5691 C  CD2 . HIS C  1 152 ? -22.086 -17.278 26.476  1.00 16.88  ? 138 HIS C CD2 1 
ATOM   5692 C  CE1 . HIS C  1 152 ? -21.018 -17.569 28.361  1.00 16.19  ? 138 HIS C CE1 1 
ATOM   5693 N  NE2 . HIS C  1 152 ? -21.631 -18.202 27.381  1.00 15.36  ? 138 HIS C NE2 1 
ATOM   5694 N  N   . GLU C  1 153 ? -22.557 -13.985 29.587  1.00 19.05  ? 139 GLU C N   1 
ATOM   5695 C  CA  . GLU C  1 153 ? -22.124 -13.473 30.879  1.00 21.31  ? 139 GLU C CA  1 
ATOM   5696 C  C   . GLU C  1 153 ? -20.596 -13.445 30.959  1.00 18.61  ? 139 GLU C C   1 
ATOM   5697 O  O   . GLU C  1 153 ? -20.024 -12.558 31.588  1.00 16.58  ? 139 GLU C O   1 
ATOM   5698 C  CB  . GLU C  1 153 ? -22.766 -14.231 32.044  1.00 25.54  ? 139 GLU C CB  1 
ATOM   5699 C  CG  . GLU C  1 153 ? -22.244 -15.648 32.264  1.00 26.45  ? 139 GLU C CG  1 
ATOM   5700 C  CD  . GLU C  1 153 ? -22.788 -16.301 33.528  1.00 29.28  ? 139 GLU C CD  1 
ATOM   5701 O  OE1 . GLU C  1 153 ? -23.411 -15.577 34.340  1.00 27.25  ? 139 GLU C OE1 1 
ATOM   5702 O  OE2 . GLU C  1 153 ? -22.608 -17.528 33.701  1.00 25.56  ? 139 GLU C OE2 1 
ATOM   5703 N  N   . ASP C  1 154 ? -19.930 -14.410 30.314  1.00 17.66  ? 140 ASP C N   1 
ATOM   5704 C  CA  . ASP C  1 154 ? -18.479 -14.490 30.374  1.00 17.63  ? 140 ASP C CA  1 
ATOM   5705 C  C   . ASP C  1 154 ? -17.862 -13.364 29.545  1.00 18.15  ? 140 ASP C C   1 
ATOM   5706 O  O   . ASP C  1 154 ? -16.793 -12.856 29.881  1.00 19.12  ? 140 ASP C O   1 
ATOM   5707 C  CB  . ASP C  1 154 ? -17.972 -15.866 29.966  1.00 19.22  ? 140 ASP C CB  1 
ATOM   5708 C  CG  . ASP C  1 154 ? -18.342 -16.999 30.914  1.00 17.52  ? 140 ASP C CG  1 
ATOM   5709 O  OD1 . ASP C  1 154 ? -18.167 -16.823 32.139  1.00 18.22  ? 140 ASP C OD1 1 
ATOM   5710 O  OD2 . ASP C  1 154 ? -18.780 -18.055 30.419  1.00 18.29  ? 140 ASP C OD2 1 
ATOM   5711 N  N   . GLU C  1 155 ? -18.543 -12.985 28.457  1.00 17.30  ? 141 GLU C N   1 
ATOM   5712 C  CA  . GLU C  1 155 ? -18.089 -11.898 27.604  1.00 16.28  ? 141 GLU C CA  1 
ATOM   5713 C  C   . GLU C  1 155 ? -18.264 -10.573 28.343  1.00 17.07  ? 141 GLU C C   1 
ATOM   5714 O  O   . GLU C  1 155 ? -17.385 -9.714  28.308  1.00 17.87  ? 141 GLU C O   1 
ATOM   5715 C  CB  . GLU C  1 155 ? -18.864 -11.903 26.285  1.00 16.79  ? 141 GLU C CB  1 
ATOM   5716 C  CG  . GLU C  1 155 ? -18.330 -10.911 25.254  1.00 17.04  ? 141 GLU C CG  1 
ATOM   5717 C  CD  . GLU C  1 155 ? -16.998 -11.290 24.632  1.00 19.23  ? 141 GLU C CD  1 
ATOM   5718 O  OE1 . GLU C  1 155 ? -16.489 -12.390 24.932  1.00 20.97  ? 141 GLU C OE1 1 
ATOM   5719 O  OE2 . GLU C  1 155 ? -16.468 -10.476 23.846  1.00 19.82  ? 141 GLU C OE2 1 
ATOM   5720 N  N   . PHE C  1 156 ? -19.415 -10.433 29.015  1.00 16.22  ? 142 PHE C N   1 
ATOM   5721 C  CA  . PHE C  1 156 ? -19.752 -9.239  29.775  1.00 17.41  ? 142 PHE C CA  1 
ATOM   5722 C  C   . PHE C  1 156 ? -18.753 -9.071  30.918  1.00 18.62  ? 142 PHE C C   1 
ATOM   5723 O  O   . PHE C  1 156 ? -18.275 -7.966  31.170  1.00 20.53  ? 142 PHE C O   1 
ATOM   5724 C  CB  . PHE C  1 156 ? -21.201 -9.374  30.262  1.00 19.18  ? 142 PHE C CB  1 
ATOM   5725 C  CG  . PHE C  1 156 ? -21.823 -8.145  30.913  1.00 20.57  ? 142 PHE C CG  1 
ATOM   5726 C  CD1 . PHE C  1 156 ? -21.672 -6.877  30.361  1.00 24.55  ? 142 PHE C CD1 1 
ATOM   5727 C  CD2 . PHE C  1 156 ? -22.585 -8.272  32.069  1.00 21.16  ? 142 PHE C CD2 1 
ATOM   5728 C  CE1 . PHE C  1 156 ? -22.258 -5.769  30.958  1.00 22.89  ? 142 PHE C CE1 1 
ATOM   5729 C  CE2 . PHE C  1 156 ? -23.169 -7.163  32.662  1.00 22.34  ? 142 PHE C CE2 1 
ATOM   5730 C  CZ  . PHE C  1 156 ? -23.006 -5.914  32.104  1.00 22.47  ? 142 PHE C CZ  1 
ATOM   5731 N  N   . ASN C  1 157 ? -18.440 -10.182 31.598  1.00 18.14  ? 143 ASN C N   1 
ATOM   5732 C  CA  . ASN C  1 157 ? -17.504 -10.180 32.712  1.00 18.45  ? 143 ASN C CA  1 
ATOM   5733 C  C   . ASN C  1 157 ? -16.122 -9.737  32.228  1.00 18.72  ? 143 ASN C C   1 
ATOM   5734 O  O   . ASN C  1 157 ? -15.500 -8.869  32.840  1.00 20.46  ? 143 ASN C O   1 
ATOM   5735 C  CB  . ASN C  1 157 ? -17.453 -11.540 33.409  1.00 17.24  ? 143 ASN C CB  1 
ATOM   5736 C  CG  . ASN C  1 157 ? -18.679 -11.827 34.248  1.00 19.29  ? 143 ASN C CG  1 
ATOM   5737 O  OD1 . ASN C  1 157 ? -19.476 -10.924 34.525  1.00 18.59  ? 143 ASN C OD1 1 
ATOM   5738 N  ND2 . ASN C  1 157 ? -18.836 -13.069 34.684  1.00 19.37  ? 143 ASN C ND2 1 
ATOM   5739 N  N   . GLY C  1 158 ? -15.644 -10.351 31.138  1.00 18.08  ? 144 GLY C N   1 
ATOM   5740 C  CA  . GLY C  1 158 ? -14.327 -10.064 30.585  1.00 19.09  ? 144 GLY C CA  1 
ATOM   5741 C  C   . GLY C  1 158 ? -14.182 -8.608  30.142  1.00 22.00  ? 144 GLY C C   1 
ATOM   5742 O  O   . GLY C  1 158 ? -13.137 -7.991  30.344  1.00 23.85  ? 144 GLY C O   1 
ATOM   5743 N  N   . ALA C  1 159 ? -15.235 -8.071  29.518  1.00 22.77  ? 145 ALA C N   1 
ATOM   5744 C  CA  . ALA C  1 159 ? -15.233 -6.688  29.068  1.00 22.73  ? 145 ALA C CA  1 
ATOM   5745 C  C   . ALA C  1 159 ? -15.173 -5.749  30.272  1.00 22.85  ? 145 ALA C C   1 
ATOM   5746 O  O   . ALA C  1 159 ? -14.433 -4.768  30.265  1.00 21.15  ? 145 ALA C O   1 
ATOM   5747 C  CB  . ALA C  1 159 ? -16.453 -6.421  28.214  1.00 20.94  ? 145 ALA C CB  1 
ATOM   5748 N  N   . LEU C  1 160 ? -15.962 -6.062  31.305  1.00 22.66  ? 146 LEU C N   1 
ATOM   5749 C  CA  . LEU C  1 160 ? -16.034 -5.230  32.495  1.00 23.53  ? 146 LEU C CA  1 
ATOM   5750 C  C   . LEU C  1 160 ? -14.674 -5.213  33.197  1.00 23.11  ? 146 LEU C C   1 
ATOM   5751 O  O   . LEU C  1 160 ? -14.290 -4.199  33.776  1.00 23.16  ? 146 LEU C O   1 
ATOM   5752 C  CB  . LEU C  1 160 ? -17.159 -5.719  33.411  1.00 22.73  ? 146 LEU C CB  1 
ATOM   5753 C  CG  . LEU C  1 160 ? -18.588 -5.471  32.914  1.00 24.35  ? 146 LEU C CG  1 
ATOM   5754 C  CD1 . LEU C  1 160 ? -19.624 -5.941  33.926  1.00 25.12  ? 146 LEU C CD1 1 
ATOM   5755 C  CD2 . LEU C  1 160 ? -18.805 -4.001  32.583  1.00 26.46  ? 146 LEU C CD2 1 
ATOM   5756 N  N   . GLN C  1 161 ? -13.938 -6.330  33.128  1.00 22.75  ? 147 GLN C N   1 
ATOM   5757 C  CA  . GLN C  1 161 ? -12.608 -6.404  33.715  1.00 23.29  ? 147 GLN C CA  1 
ATOM   5758 C  C   . GLN C  1 161 ? -11.653 -5.478  32.959  1.00 23.84  ? 147 GLN C C   1 
ATOM   5759 O  O   . GLN C  1 161 ? -10.845 -4.785  33.573  1.00 20.74  ? 147 GLN C O   1 
ATOM   5760 C  CB  . GLN C  1 161 ? -12.071 -7.837  33.755  1.00 22.65  ? 147 GLN C CB  1 
ATOM   5761 C  CG  . GLN C  1 161 ? -12.593 -8.657  34.930  1.00 24.53  ? 147 GLN C CG  1 
ATOM   5762 C  CD  . GLN C  1 161 ? -11.660 -9.785  35.314  1.00 23.39  ? 147 GLN C CD  1 
ATOM   5763 O  OE1 . GLN C  1 161 ? -10.434 -9.651  35.245  1.00 22.47  ? 147 GLN C OE1 1 
ATOM   5764 N  NE2 . GLN C  1 161 ? -12.230 -10.917 35.699  1.00 22.96  ? 147 GLN C NE2 1 
ATOM   5765 N  N   . CYS C  1 162 ? -11.753 -5.475  31.625  1.00 23.61  ? 148 CYS C N   1 
ATOM   5766 C  CA  . CYS C  1 162 ? -10.943 -4.594  30.794  1.00 25.20  ? 148 CYS C CA  1 
ATOM   5767 C  C   . CYS C  1 162 ? -11.163 -3.145  31.225  1.00 23.08  ? 148 CYS C C   1 
ATOM   5768 O  O   . CYS C  1 162 ? -10.221 -2.360  31.305  1.00 28.27  ? 148 CYS C O   1 
ATOM   5769 C  CB  . CYS C  1 162 ? -11.279 -4.761  29.315  1.00 26.70  ? 148 CYS C CB  1 
ATOM   5770 S  SG  . CYS C  1 162 ? -10.768 -6.354  28.618  1.00 27.71  ? 148 CYS C SG  1 
ATOM   5771 N  N   . TYR C  1 163 ? -12.427 -2.816  31.510  1.00 23.12  ? 149 TYR C N   1 
ATOM   5772 C  CA  . TYR C  1 163 ? -12.822 -1.481  31.926  1.00 25.09  ? 149 TYR C CA  1 
ATOM   5773 C  C   . TYR C  1 163 ? -12.196 -1.163  33.281  1.00 26.29  ? 149 TYR C C   1 
ATOM   5774 O  O   . TYR C  1 163 ? -11.495 -0.163  33.432  1.00 25.07  ? 149 TYR C O   1 
ATOM   5775 C  CB  . TYR C  1 163 ? -14.351 -1.394  31.987  1.00 26.90  ? 149 TYR C CB  1 
ATOM   5776 C  CG  . TYR C  1 163 ? -14.885 -0.018  32.366  1.00 28.75  ? 149 TYR C CG  1 
ATOM   5777 C  CD1 . TYR C  1 163 ? -14.787 1.054   31.487  1.00 34.49  ? 149 TYR C CD1 1 
ATOM   5778 C  CD2 . TYR C  1 163 ? -15.501 0.207   33.592  1.00 29.02  ? 149 TYR C CD2 1 
ATOM   5779 C  CE1 . TYR C  1 163 ? -15.273 2.309   31.818  1.00 34.48  ? 149 TYR C CE1 1 
ATOM   5780 C  CE2 . TYR C  1 163 ? -15.992 1.457   33.935  1.00 33.61  ? 149 TYR C CE2 1 
ATOM   5781 C  CZ  . TYR C  1 163 ? -15.878 2.511   33.045  1.00 32.22  ? 149 TYR C CZ  1 
ATOM   5782 O  OH  . TYR C  1 163 ? -16.357 3.747   33.370  1.00 32.43  ? 149 TYR C OH  1 
ATOM   5783 N  N   . ALA C  1 164 ? -12.466 -2.036  34.257  1.00 23.00  ? 150 ALA C N   1 
ATOM   5784 C  CA  . ALA C  1 164 ? -12.030 -1.843  35.630  1.00 24.06  ? 150 ALA C CA  1 
ATOM   5785 C  C   . ALA C  1 164 ? -10.504 -1.804  35.710  1.00 24.16  ? 150 ALA C C   1 
ATOM   5786 O  O   . ALA C  1 164 ? -9.951  -1.154  36.595  1.00 27.36  ? 150 ALA C O   1 
ATOM   5787 C  CB  . ALA C  1 164 ? -12.608 -2.938  36.505  1.00 25.16  ? 150 ALA C CB  1 
ATOM   5788 N  N   . ARG C  1 165 ? -9.833  -2.501  34.783  1.00 24.12  ? 151 ARG C N   1 
ATOM   5789 C  CA  . ARG C  1 165 ? -8.377  -2.564  34.758  1.00 25.31  ? 151 ARG C CA  1 
ATOM   5790 C  C   . ARG C  1 165 ? -7.802  -1.407  33.939  1.00 27.03  ? 151 ARG C C   1 
ATOM   5791 O  O   . ARG C  1 165 ? -6.589  -1.322  33.750  1.00 27.44  ? 151 ARG C O   1 
ATOM   5792 C  CB  . ARG C  1 165 ? -7.894  -3.903  34.183  1.00 25.76  ? 151 ARG C CB  1 
ATOM   5793 C  CG  . ARG C  1 165 ? -8.176  -5.127  35.046  1.00 27.14  ? 151 ARG C CG  1 
ATOM   5794 C  CD  . ARG C  1 165 ? -7.941  -6.416  34.265  1.00 26.61  ? 151 ARG C CD  1 
ATOM   5795 N  NE  . ARG C  1 165 ? -8.164  -7.643  35.039  1.00 27.39  ? 151 ARG C NE  1 
ATOM   5796 C  CZ  . ARG C  1 165 ? -7.264  -8.233  35.818  1.00 27.99  ? 151 ARG C CZ  1 
ATOM   5797 N  NH1 . ARG C  1 165 ? -6.046  -7.731  35.930  1.00 27.73  ? 151 ARG C NH1 1 
ATOM   5798 N  NH2 . ARG C  1 165 ? -7.583  -9.341  36.467  1.00 27.72  ? 151 ARG C NH2 1 
ATOM   5799 N  N   . ASN C  1 166 ? -8.679  -0.524  33.448  1.00 30.36  ? 152 ASN C N   1 
ATOM   5800 C  CA  . ASN C  1 166 ? -8.262  0.635   32.672  1.00 31.33  ? 152 ASN C CA  1 
ATOM   5801 C  C   . ASN C  1 166 ? -7.341  0.195   31.534  1.00 30.65  ? 152 ASN C C   1 
ATOM   5802 O  O   . ASN C  1 166 ? -6.286  0.790   31.317  1.00 35.12  ? 152 ASN C O   1 
ATOM   5803 C  CB  . ASN C  1 166 ? -7.612  1.697   33.556  1.00 31.01  ? 152 ASN C CB  1 
ATOM   5804 C  CG  . ASN C  1 166 ? -8.621  2.418   34.419  1.00 32.07  ? 152 ASN C CG  1 
ATOM   5805 O  OD1 . ASN C  1 166 ? -9.475  3.147   33.902  1.00 34.47  ? 152 ASN C OD1 1 
ATOM   5806 N  ND2 . ASN C  1 166 ? -8.543  2.233   35.729  1.00 32.22  ? 152 ASN C ND2 1 
ATOM   5807 N  N   . GLN C  1 167 ? -7.755  -0.849  30.807  1.00 33.69  ? 153 GLN C N   1 
ATOM   5808 C  CA  . GLN C  1 167 ? -7.047  -1.289  29.615  1.00 37.94  ? 153 GLN C CA  1 
ATOM   5809 C  C   . GLN C  1 167 ? -7.531  -0.455  28.429  1.00 36.47  ? 153 GLN C C   1 
ATOM   5810 O  O   . GLN C  1 167 ? -8.714  -0.468  28.094  1.00 35.23  ? 153 GLN C O   1 
ATOM   5811 C  CB  . GLN C  1 167 ? -7.222  -2.798  29.426  1.00 40.66  ? 153 GLN C CB  1 
ATOM   5812 C  CG  . GLN C  1 167 ? -6.345  -3.630  30.358  1.00 47.64  ? 153 GLN C CG  1 
ATOM   5813 C  CD  . GLN C  1 167 ? -6.731  -5.093  30.411  1.00 44.68  ? 153 GLN C CD  1 
ATOM   5814 O  OE1 . GLN C  1 167 ? -7.512  -5.585  29.589  1.00 48.55  ? 153 GLN C OE1 1 
ATOM   5815 N  NE2 . GLN C  1 167 ? -6.176  -5.806  31.381  1.00 46.64  ? 153 GLN C NE2 1 
ATOM   5816 N  N   . LYS C  1 168 ? -6.599  0.281   27.811  1.00 37.54  ? 154 LYS C N   1 
ATOM   5817 C  CA  . LYS C  1 168 ? -6.934  1.287   26.813  1.00 48.87  ? 154 LYS C CA  1 
ATOM   5818 C  C   . LYS C  1 168 ? -6.666  0.769   25.401  1.00 45.61  ? 154 LYS C C   1 
ATOM   5819 O  O   . LYS C  1 168 ? -7.174  1.332   24.434  1.00 53.36  ? 154 LYS C O   1 
ATOM   5820 C  CB  . LYS C  1 168 ? -6.149  2.581   27.065  1.00 50.85  ? 154 LYS C CB  1 
ATOM   5821 C  CG  . LYS C  1 168 ? -6.958  3.752   27.618  1.00 52.89  ? 154 LYS C CG  1 
ATOM   5822 C  CD  . LYS C  1 168 ? -7.739  3.466   28.894  1.00 49.38  ? 154 LYS C CD  1 
ATOM   5823 C  CE  . LYS C  1 168 ? -8.120  4.726   29.617  1.00 52.85  ? 154 LYS C CE  1 
ATOM   5824 N  NZ  . LYS C  1 168 ? -9.098  4.486   30.684  1.00 54.75  ? 154 LYS C NZ  1 
ATOM   5825 N  N   . GLU C  1 169 ? -5.866  -0.297  25.290  1.00 47.09  ? 155 GLU C N   1 
ATOM   5826 C  CA  . GLU C  1 169 ? -5.543  -0.879  23.996  1.00 48.84  ? 155 GLU C CA  1 
ATOM   5827 C  C   . GLU C  1 169 ? -6.147  -2.282  23.922  1.00 47.94  ? 155 GLU C C   1 
ATOM   5828 O  O   . GLU C  1 169 ? -6.465  -2.881  24.947  1.00 51.01  ? 155 GLU C O   1 
ATOM   5829 C  CB  . GLU C  1 169 ? -4.030  -0.854  23.765  1.00 51.41  ? 155 GLU C CB  1 
ATOM   5830 C  CG  . GLU C  1 169 ? -3.420  0.538   23.913  1.00 57.50  ? 155 GLU C CG  1 
ATOM   5831 C  CD  . GLU C  1 169 ? -2.063  0.729   23.255  1.00 61.81  ? 155 GLU C CD  1 
ATOM   5832 O  OE1 . GLU C  1 169 ? -1.510  -0.260  22.730  1.00 65.29  ? 155 GLU C OE1 1 
ATOM   5833 O  OE2 . GLU C  1 169 ? -1.567  1.876   23.256  1.00 69.51  ? 155 GLU C OE2 1 
ATOM   5834 N  N   . GLY C  1 170 ? -6.317  -2.789  22.696  1.00 45.91  ? 156 GLY C N   1 
ATOM   5835 C  CA  . GLY C  1 170 ? -6.976  -4.067  22.475  1.00 41.55  ? 156 GLY C CA  1 
ATOM   5836 C  C   . GLY C  1 170 ? -8.354  -3.883  21.838  1.00 42.41  ? 156 GLY C C   1 
ATOM   5837 O  O   . GLY C  1 170 ? -8.702  -2.784  21.409  1.00 37.90  ? 156 GLY C O   1 
ATOM   5838 N  N   . ALA C  1 171 ? -9.140  -4.968  21.810  1.00 38.11  ? 157 ALA C N   1 
ATOM   5839 C  CA  . ALA C  1 171 ? -10.339 -5.042  20.988  1.00 36.20  ? 157 ALA C CA  1 
ATOM   5840 C  C   . ALA C  1 171 ? -11.588 -4.681  21.791  1.00 29.45  ? 157 ALA C C   1 
ATOM   5841 O  O   . ALA C  1 171 ? -12.691 -4.684  21.248  1.00 28.95  ? 157 ALA C O   1 
ATOM   5842 C  CB  . ALA C  1 171 ? -10.457 -6.427  20.387  1.00 35.74  ? 157 ALA C CB  1 
ATOM   5843 N  N   . TYR C  1 172 ? -11.406 -4.377  23.080  1.00 26.64  ? 158 TYR C N   1 
ATOM   5844 C  CA  . TYR C  1 172 ? -12.502 -3.952  23.939  1.00 26.10  ? 158 TYR C CA  1 
ATOM   5845 C  C   . TYR C  1 172 ? -12.320 -2.468  24.253  1.00 28.87  ? 158 TYR C C   1 
ATOM   5846 O  O   . TYR C  1 172 ? -11.349 -2.088  24.901  1.00 31.86  ? 158 TYR C O   1 
ATOM   5847 C  CB  . TYR C  1 172 ? -12.544 -4.863  25.173  1.00 26.46  ? 158 TYR C CB  1 
ATOM   5848 C  CG  . TYR C  1 172 ? -12.924 -6.303  24.847  1.00 23.11  ? 158 TYR C CG  1 
ATOM   5849 C  CD1 . TYR C  1 172 ? -14.255 -6.679  24.698  1.00 23.73  ? 158 TYR C CD1 1 
ATOM   5850 C  CD2 . TYR C  1 172 ? -11.951 -7.280  24.662  1.00 25.97  ? 158 TYR C CD2 1 
ATOM   5851 C  CE1 . TYR C  1 172 ? -14.608 -7.982  24.387  1.00 24.78  ? 158 TYR C CE1 1 
ATOM   5852 C  CE2 . TYR C  1 172 ? -12.291 -8.587  24.351  1.00 26.01  ? 158 TYR C CE2 1 
ATOM   5853 C  CZ  . TYR C  1 172 ? -13.623 -8.939  24.214  1.00 25.38  ? 158 TYR C CZ  1 
ATOM   5854 O  OH  . TYR C  1 172 ? -13.958 -10.226 23.905  1.00 25.91  ? 158 TYR C OH  1 
ATOM   5855 N  N   . ILE C  1 173 ? -13.267 -1.641  23.786  1.00 30.58  ? 159 ILE C N   1 
ATOM   5856 C  CA  . ILE C  1 173 ? -13.099 -0.195  23.765  1.00 25.84  ? 159 ILE C CA  1 
ATOM   5857 C  C   . ILE C  1 173 ? -13.578 0.404   25.085  1.00 24.10  ? 159 ILE C C   1 
ATOM   5858 O  O   . ILE C  1 173 ? -14.775 0.427   25.379  1.00 25.97  ? 159 ILE C O   1 
ATOM   5859 C  CB  . ILE C  1 173 ? -13.828 0.431   22.560  1.00 26.57  ? 159 ILE C CB  1 
ATOM   5860 C  CG1 . ILE C  1 173 ? -13.460 -0.271  21.251  1.00 26.62  ? 159 ILE C CG1 1 
ATOM   5861 C  CG2 . ILE C  1 173 ? -13.567 1.937   22.487  1.00 26.88  ? 159 ILE C CG2 1 
ATOM   5862 C  CD1 . ILE C  1 173 ? -11.968 -0.312  20.964  1.00 25.85  ? 159 ILE C CD1 1 
ATOM   5863 N  N   . TRP C  1 174 ? -12.618 0.927   25.853  1.00 25.84  ? 160 TRP C N   1 
ATOM   5864 C  CA  . TRP C  1 174 ? -12.879 1.449   27.183  1.00 27.65  ? 160 TRP C CA  1 
ATOM   5865 C  C   . TRP C  1 174 ? -13.983 2.507   27.137  1.00 28.63  ? 160 TRP C C   1 
ATOM   5866 O  O   . TRP C  1 174 ? -14.893 2.492   27.965  1.00 24.80  ? 160 TRP C O   1 
ATOM   5867 C  CB  . TRP C  1 174 ? -11.577 2.000   27.787  1.00 28.64  ? 160 TRP C CB  1 
ATOM   5868 C  CG  . TRP C  1 174 ? -11.655 2.262   29.268  1.00 28.74  ? 160 TRP C CG  1 
ATOM   5869 C  CD1 . TRP C  1 174 ? -11.229 1.439   30.269  1.00 30.24  ? 160 TRP C CD1 1 
ATOM   5870 C  CD2 . TRP C  1 174 ? -12.202 3.433   29.916  1.00 32.62  ? 160 TRP C CD2 1 
ATOM   5871 N  NE1 . TRP C  1 174 ? -11.468 2.011   31.489  1.00 31.04  ? 160 TRP C NE1 1 
ATOM   5872 C  CE2 . TRP C  1 174 ? -12.064 3.232   31.306  1.00 30.56  ? 160 TRP C CE2 1 
ATOM   5873 C  CE3 . TRP C  1 174 ? -12.787 4.620   29.460  1.00 31.78  ? 160 TRP C CE3 1 
ATOM   5874 C  CZ2 . TRP C  1 174 ? -12.490 4.176   32.238  1.00 32.40  ? 160 TRP C CZ2 1 
ATOM   5875 C  CZ3 . TRP C  1 174 ? -13.206 5.553   30.383  1.00 31.53  ? 160 TRP C CZ3 1 
ATOM   5876 C  CH2 . TRP C  1 174 ? -13.060 5.331   31.752  1.00 33.97  ? 160 TRP C CH2 1 
ATOM   5877 N  N   . ALA C  1 175 ? -13.916 3.408   26.147  1.00 30.42  ? 161 ALA C N   1 
ATOM   5878 C  CA  . ALA C  1 175 ? -14.842 4.529   26.062  1.00 30.07  ? 161 ALA C CA  1 
ATOM   5879 C  C   . ALA C  1 175 ? -16.254 4.048   25.725  1.00 26.93  ? 161 ALA C C   1 
ATOM   5880 O  O   . ALA C  1 175 ? -17.234 4.660   26.144  1.00 29.64  ? 161 ALA C O   1 
ATOM   5881 C  CB  . ALA C  1 175 ? -14.343 5.542   25.048  1.00 36.52  ? 161 ALA C CB  1 
ATOM   5882 N  N   . ASP C  1 176 ? -16.353 2.957   24.956  1.00 26.43  ? 162 ASP C N   1 
ATOM   5883 C  CA  . ASP C  1 176 ? -17.643 2.365   24.631  1.00 26.32  ? 162 ASP C CA  1 
ATOM   5884 C  C   . ASP C  1 176 ? -18.283 1.809   25.901  1.00 24.57  ? 162 ASP C C   1 
ATOM   5885 O  O   . ASP C  1 176 ? -19.446 2.090   26.190  1.00 24.54  ? 162 ASP C O   1 
ATOM   5886 C  CB  . ASP C  1 176 ? -17.521 1.286   23.564  1.00 29.52  ? 162 ASP C CB  1 
ATOM   5887 C  CG  . ASP C  1 176 ? -17.258 1.781   22.147  1.00 33.77  ? 162 ASP C CG  1 
ATOM   5888 O  OD1 . ASP C  1 176 ? -17.275 3.014   21.940  1.00 32.57  ? 162 ASP C OD1 1 
ATOM   5889 O  OD2 . ASP C  1 176 ? -17.037 0.927   21.260  1.00 29.03  ? 162 ASP C OD2 1 
ATOM   5890 N  N   . ILE C  1 177 ? -17.515 1.003   26.644  1.00 27.15  ? 163 ILE C N   1 
ATOM   5891 C  CA  . ILE C  1 177 ? -18.007 0.372   27.859  1.00 27.20  ? 163 ILE C CA  1 
ATOM   5892 C  C   . ILE C  1 177 ? -18.450 1.465   28.829  1.00 27.75  ? 163 ILE C C   1 
ATOM   5893 O  O   . ILE C  1 177 ? -19.508 1.364   29.448  1.00 26.21  ? 163 ILE C O   1 
ATOM   5894 C  CB  . ILE C  1 177 ? -16.940 -0.555  28.474  1.00 28.23  ? 163 ILE C CB  1 
ATOM   5895 C  CG1 . ILE C  1 177 ? -16.475 -1.625  27.479  1.00 28.33  ? 163 ILE C CG1 1 
ATOM   5896 C  CG2 . ILE C  1 177 ? -17.451 -1.182  29.772  1.00 30.62  ? 163 ILE C CG2 1 
ATOM   5897 C  CD1 . ILE C  1 177 ? -15.191 -2.332  27.875  1.00 29.19  ? 163 ILE C CD1 1 
ATOM   5898 N  N   . ASP C  1 178 ? -17.630 2.516   28.937  1.00 30.24  ? 164 ASP C N   1 
ATOM   5899 C  CA  . ASP C  1 178 ? -17.944 3.668   29.768  1.00 33.03  ? 164 ASP C CA  1 
ATOM   5900 C  C   . ASP C  1 178 ? -19.355 4.156   29.440  1.00 28.70  ? 164 ASP C C   1 
ATOM   5901 O  O   . ASP C  1 178 ? -20.149 4.431   30.338  1.00 28.62  ? 164 ASP C O   1 
ATOM   5902 C  CB  . ASP C  1 178 ? -16.899 4.761   29.591  1.00 35.39  ? 164 ASP C CB  1 
ATOM   5903 C  CG  . ASP C  1 178 ? -16.946 5.886   30.615  1.00 38.43  ? 164 ASP C CG  1 
ATOM   5904 O  OD1 . ASP C  1 178 ? -16.857 5.584   31.823  1.00 33.12  ? 164 ASP C OD1 1 
ATOM   5905 O  OD2 . ASP C  1 178 ? -17.057 7.055   30.194  1.00 37.37  ? 164 ASP C OD2 1 
ATOM   5906 N  N   . ALA C  1 179 ? -19.660 4.245   28.140  1.00 31.72  ? 165 ALA C N   1 
ATOM   5907 C  CA  . ALA C  1 179 ? -20.920 4.804   27.672  1.00 29.18  ? 165 ALA C CA  1 
ATOM   5908 C  C   . ALA C  1 179 ? -22.082 3.863   27.987  1.00 30.27  ? 165 ALA C C   1 
ATOM   5909 O  O   . ALA C  1 179 ? -23.177 4.315   28.320  1.00 27.74  ? 165 ALA C O   1 
ATOM   5910 C  CB  . ALA C  1 179 ? -20.829 5.099   26.190  1.00 34.19  ? 165 ALA C CB  1 
ATOM   5911 N  N   . TRP C  1 180 ? -21.844 2.550   27.872  1.00 28.84  ? 166 TRP C N   1 
ATOM   5912 C  CA  . TRP C  1 180 ? -22.873 1.567   28.178  1.00 27.91  ? 166 TRP C CA  1 
ATOM   5913 C  C   . TRP C  1 180 ? -23.357 1.773   29.611  1.00 28.69  ? 166 TRP C C   1 
ATOM   5914 O  O   . TRP C  1 180 ? -24.557 1.752   29.881  1.00 27.00  ? 166 TRP C O   1 
ATOM   5915 C  CB  . TRP C  1 180 ? -22.360 0.130   27.990  1.00 27.07  ? 166 TRP C CB  1 
ATOM   5916 C  CG  . TRP C  1 180 ? -21.700 -0.150  26.665  1.00 29.96  ? 166 TRP C CG  1 
ATOM   5917 C  CD1 . TRP C  1 180 ? -21.787 0.578   25.513  1.00 32.15  ? 166 TRP C CD1 1 
ATOM   5918 C  CD2 . TRP C  1 180 ? -20.837 -1.271  26.366  1.00 30.87  ? 166 TRP C CD2 1 
ATOM   5919 N  NE1 . TRP C  1 180 ? -21.038 -0.005  24.524  1.00 28.75  ? 166 TRP C NE1 1 
ATOM   5920 C  CE2 . TRP C  1 180 ? -20.444 -1.139  25.016  1.00 30.43  ? 166 TRP C CE2 1 
ATOM   5921 C  CE3 . TRP C  1 180 ? -20.361 -2.362  27.104  1.00 29.23  ? 166 TRP C CE3 1 
ATOM   5922 C  CZ2 . TRP C  1 180 ? -19.599 -2.059  24.397  1.00 28.66  ? 166 TRP C CZ2 1 
ATOM   5923 C  CZ3 . TRP C  1 180 ? -19.523 -3.267  26.491  1.00 29.05  ? 166 TRP C CZ3 1 
ATOM   5924 C  CH2 . TRP C  1 180 ? -19.148 -3.115  25.157  1.00 28.89  ? 166 TRP C CH2 1 
ATOM   5925 N  N   . ILE C  1 181 ? -22.397 1.970   30.522  1.00 30.24  ? 167 ILE C N   1 
ATOM   5926 C  CA  . ILE C  1 181 ? -22.693 2.081   31.941  1.00 32.63  ? 167 ILE C CA  1 
ATOM   5927 C  C   . ILE C  1 181 ? -23.399 3.412   32.204  1.00 33.62  ? 167 ILE C C   1 
ATOM   5928 O  O   . ILE C  1 181 ? -24.402 3.453   32.913  1.00 34.12  ? 167 ILE C O   1 
ATOM   5929 C  CB  . ILE C  1 181 ? -21.408 1.904   32.775  1.00 32.72  ? 167 ILE C CB  1 
ATOM   5930 C  CG1 . ILE C  1 181 ? -20.816 0.497   32.601  1.00 29.15  ? 167 ILE C CG1 1 
ATOM   5931 C  CG2 . ILE C  1 181 ? -21.660 2.229   34.247  1.00 33.29  ? 167 ILE C CG2 1 
ATOM   5932 C  CD1 . ILE C  1 181 ? -19.491 0.280   33.309  1.00 29.41  ? 167 ILE C CD1 1 
ATOM   5933 N  N   . LYS C  1 182 ? -22.889 4.494   31.603  1.00 32.70  ? 168 LYS C N   1 
ATOM   5934 C  CA  . LYS C  1 182 ? -23.440 5.825   31.816  1.00 36.65  ? 168 LYS C CA  1 
ATOM   5935 C  C   . LYS C  1 182 ? -24.873 5.903   31.283  1.00 36.92  ? 168 LYS C C   1 
ATOM   5936 O  O   . LYS C  1 182 ? -25.694 6.631   31.836  1.00 33.62  ? 168 LYS C O   1 
ATOM   5937 C  CB  . LYS C  1 182 ? -22.528 6.894   31.199  1.00 39.45  ? 168 LYS C CB  1 
ATOM   5938 C  CG  . LYS C  1 182 ? -21.298 7.252   32.034  1.00 44.07  ? 168 LYS C CG  1 
ATOM   5939 C  CD  . LYS C  1 182 ? -20.286 8.164   31.346  1.00 48.19  ? 168 LYS C CD  1 
ATOM   5940 C  CE  . LYS C  1 182 ? -19.094 8.468   32.209  1.00 50.55  ? 168 LYS C CE  1 
ATOM   5941 N  NZ  . LYS C  1 182 ? -18.028 9.162   31.478  1.00 47.91  ? 168 LYS C NZ  1 
ATOM   5942 N  N   . ASN C  1 183 ? -25.176 5.149   30.217  1.00 37.73  ? 169 ASN C N   1 
ATOM   5943 C  CA  . ASN C  1 183 ? -26.485 5.220   29.582  1.00 36.94  ? 169 ASN C CA  1 
ATOM   5944 C  C   . ASN C  1 183 ? -27.457 4.237   30.240  1.00 32.60  ? 169 ASN C C   1 
ATOM   5945 O  O   . ASN C  1 183 ? -28.612 4.139   29.829  1.00 33.28  ? 169 ASN C O   1 
ATOM   5946 C  CB  . ASN C  1 183 ? -26.402 5.007   28.071  1.00 40.74  ? 169 ASN C CB  1 
ATOM   5947 C  CG  . ASN C  1 183 ? -25.792 6.188   27.350  1.00 44.65  ? 169 ASN C CG  1 
ATOM   5948 O  OD1 . ASN C  1 183 ? -25.263 7.104   27.989  1.00 47.95  ? 169 ASN C OD1 1 
ATOM   5949 N  ND2 . ASN C  1 183 ? -25.850 6.186   26.026  1.00 53.75  ? 169 ASN C ND2 1 
ATOM   5950 N  N   . ASN C  1 184 ? -26.988 3.514   31.264  1.00 28.75  ? 170 ASN C N   1 
ATOM   5951 C  CA  . ASN C  1 184 ? -27.865 2.692   32.087  1.00 31.00  ? 170 ASN C CA  1 
ATOM   5952 C  C   . ASN C  1 184 ? -28.605 1.678   31.213  1.00 27.12  ? 170 ASN C C   1 
ATOM   5953 O  O   . ASN C  1 184 ? -29.820 1.532   31.317  1.00 25.66  ? 170 ASN C O   1 
ATOM   5954 C  CB  . ASN C  1 184 ? -28.828 3.561   32.896  1.00 33.20  ? 170 ASN C CB  1 
ATOM   5955 C  CG  . ASN C  1 184 ? -29.665 2.769   33.875  1.00 37.06  ? 170 ASN C CG  1 
ATOM   5956 O  OD1 . ASN C  1 184 ? -29.142 1.899   34.580  1.00 45.51  ? 170 ASN C OD1 1 
ATOM   5957 N  ND2 . ASN C  1 184 ? -30.959 3.054   33.937  1.00 39.36  ? 170 ASN C ND2 1 
ATOM   5958 N  N   . LEU C  1 185 ? -27.855 0.966   30.363  1.00 28.11  ? 171 LEU C N   1 
ATOM   5959 C  CA  . LEU C  1 185 ? -28.413 -0.079  29.515  1.00 26.44  ? 171 LEU C CA  1 
ATOM   5960 C  C   . LEU C  1 185 ? -29.017 -1.191  30.376  1.00 28.10  ? 171 LEU C C   1 
ATOM   5961 O  O   . LEU C  1 185 ? -28.569 -1.421  31.499  1.00 28.00  ? 171 LEU C O   1 
ATOM   5962 C  CB  . LEU C  1 185 ? -27.309 -0.616  28.603  1.00 25.90  ? 171 LEU C CB  1 
ATOM   5963 C  CG  . LEU C  1 185 ? -26.738 0.368   27.576  1.00 27.68  ? 171 LEU C CG  1 
ATOM   5964 C  CD1 . LEU C  1 185 ? -25.814 -0.344  26.597  1.00 28.15  ? 171 LEU C CD1 1 
ATOM   5965 C  CD2 . LEU C  1 185 ? -27.854 1.091   26.836  1.00 27.43  ? 171 LEU C CD2 1 
ATOM   5966 N  N   A GLN C  1 186 ? -30.024 -1.888  29.831  0.60 30.45  ? 172 GLN C N   1 
ATOM   5967 N  N   B GLN C  1 186 ? -30.039 -1.866  29.835  0.40 27.47  ? 172 GLN C N   1 
ATOM   5968 C  CA  A GLN C  1 186 ? -30.701 -2.965  30.541  0.60 31.09  ? 172 GLN C CA  1 
ATOM   5969 C  CA  B GLN C  1 186 ? -30.702 -2.967  30.518  0.40 26.19  ? 172 GLN C CA  1 
ATOM   5970 C  C   A GLN C  1 186 ? -30.174 -4.310  30.038  0.60 29.89  ? 172 GLN C C   1 
ATOM   5971 C  C   B GLN C  1 186 ? -30.124 -4.289  30.015  0.40 26.90  ? 172 GLN C C   1 
ATOM   5972 O  O   A GLN C  1 186 ? -30.444 -4.703  28.905  0.60 30.93  ? 172 GLN C O   1 
ATOM   5973 O  O   B GLN C  1 186 ? -30.298 -4.641  28.850  0.40 28.33  ? 172 GLN C O   1 
ATOM   5974 C  CB  A GLN C  1 186 ? -32.218 -2.830  30.378  0.60 36.20  ? 172 GLN C CB  1 
ATOM   5975 C  CB  B GLN C  1 186 ? -32.215 -2.896  30.297  0.40 25.98  ? 172 GLN C CB  1 
ATOM   5976 C  CG  A GLN C  1 186 ? -33.032 -3.905  31.094  0.60 41.28  ? 172 GLN C CG  1 
ATOM   5977 C  CG  B GLN C  1 186 ? -32.854 -1.623  30.841  0.40 25.49  ? 172 GLN C CG  1 
ATOM   5978 C  CD  A GLN C  1 186 ? -34.492 -3.536  31.254  0.60 49.13  ? 172 GLN C CD  1 
ATOM   5979 C  CD  B GLN C  1 186 ? -32.540 -1.401  32.305  0.40 25.38  ? 172 GLN C CD  1 
ATOM   5980 O  OE1 A GLN C  1 186 ? -35.134 -3.028  30.327  0.60 56.06  ? 172 GLN C OE1 1 
ATOM   5981 O  OE1 B GLN C  1 186 ? -32.851 -2.235  33.163  0.40 27.09  ? 172 GLN C OE1 1 
ATOM   5982 N  NE2 A GLN C  1 186 ? -35.031 -3.769  32.442  0.60 48.95  ? 172 GLN C NE2 1 
ATOM   5983 N  NE2 B GLN C  1 186 ? -31.903 -0.278  32.601  0.40 22.93  ? 172 GLN C NE2 1 
ATOM   5984 N  N   . TRP C  1 187 ? -29.441 -5.017  30.908  1.00 25.42  ? 173 TRP C N   1 
ATOM   5985 C  CA  . TRP C  1 187 ? -28.706 -6.218  30.529  1.00 25.23  ? 173 TRP C CA  1 
ATOM   5986 C  C   . TRP C  1 187 ? -29.456 -7.500  30.907  1.00 24.33  ? 173 TRP C C   1 
ATOM   5987 O  O   . TRP C  1 187 ? -30.090 -7.571  31.957  1.00 23.90  ? 173 TRP C O   1 
ATOM   5988 C  CB  . TRP C  1 187 ? -27.315 -6.221  31.188  1.00 25.52  ? 173 TRP C CB  1 
ATOM   5989 C  CG  . TRP C  1 187 ? -26.436 -5.035  30.874  1.00 25.17  ? 173 TRP C CG  1 
ATOM   5990 C  CD1 . TRP C  1 187 ? -26.309 -3.897  31.616  1.00 25.62  ? 173 TRP C CD1 1 
ATOM   5991 C  CD2 . TRP C  1 187 ? -25.522 -4.886  29.761  1.00 25.85  ? 173 TRP C CD2 1 
ATOM   5992 N  NE1 . TRP C  1 187 ? -25.402 -3.047  31.039  1.00 27.12  ? 173 TRP C NE1 1 
ATOM   5993 C  CE2 . TRP C  1 187 ? -24.901 -3.625  29.902  1.00 26.45  ? 173 TRP C CE2 1 
ATOM   5994 C  CE3 . TRP C  1 187 ? -25.174 -5.684  28.664  1.00 25.13  ? 173 TRP C CE3 1 
ATOM   5995 C  CZ2 . TRP C  1 187 ? -23.958 -3.150  28.991  1.00 28.56  ? 173 TRP C CZ2 1 
ATOM   5996 C  CZ3 . TRP C  1 187 ? -24.238 -5.214  27.767  1.00 25.25  ? 173 TRP C CZ3 1 
ATOM   5997 C  CH2 . TRP C  1 187 ? -23.639 -3.965  27.930  1.00 25.03  ? 173 TRP C CH2 1 
ATOM   5998 N  N   A ARG C  1 188 ? -29.387 -8.473  29.993  0.72 24.25  ? 174 ARG C N   1 
ATOM   5999 N  N   B ARG C  1 188 ? -29.332 -8.521  30.048  0.08 23.90  ? 174 ARG C N   1 
ATOM   6000 N  N   C ARG C  1 188 ? -29.392 -8.510  30.030  0.20 24.47  ? 174 ARG C N   1 
ATOM   6001 C  CA  A ARG C  1 188 ? -29.813 -9.844  30.218  0.72 24.49  ? 174 ARG C CA  1 
ATOM   6002 C  CA  B ARG C  1 188 ? -29.845 -9.858  30.315  0.08 23.54  ? 174 ARG C CA  1 
ATOM   6003 C  CA  C ARG C  1 188 ? -29.838 -9.856  30.363  0.20 24.53  ? 174 ARG C CA  1 
ATOM   6004 C  C   A ARG C  1 188 ? -28.653 -10.756 29.828  0.72 25.09  ? 174 ARG C C   1 
ATOM   6005 C  C   B ARG C  1 188 ? -28.787 -10.877 29.889  0.08 24.01  ? 174 ARG C C   1 
ATOM   6006 C  C   C ARG C  1 188 ? -28.775 -10.848 29.892  0.20 25.08  ? 174 ARG C C   1 
ATOM   6007 O  O   A ARG C  1 188 ? -28.424 -10.984 28.642  0.72 24.67  ? 174 ARG C O   1 
ATOM   6008 O  O   B ARG C  1 188 ? -28.792 -11.338 28.750  0.08 24.69  ? 174 ARG C O   1 
ATOM   6009 O  O   C ARG C  1 188 ? -28.764 -11.253 28.732  0.20 26.72  ? 174 ARG C O   1 
ATOM   6010 C  CB  A ARG C  1 188 ? -31.058 -10.157 29.377  0.72 25.58  ? 174 ARG C CB  1 
ATOM   6011 C  CB  B ARG C  1 188 ? -31.176 -10.077 29.580  0.08 22.99  ? 174 ARG C CB  1 
ATOM   6012 C  CB  C ARG C  1 188 ? -31.232 -10.171 29.801  0.20 24.58  ? 174 ARG C CB  1 
ATOM   6013 C  CG  A ARG C  1 188 ? -31.235 -11.614 28.971  0.72 28.59  ? 174 ARG C CG  1 
ATOM   6014 C  CG  B ARG C  1 188 ? -31.848 -11.426 29.802  0.08 22.50  ? 174 ARG C CG  1 
ATOM   6015 C  CG  C ARG C  1 188 ? -31.636 -11.635 29.939  0.20 24.81  ? 174 ARG C CG  1 
ATOM   6016 C  CD  A ARG C  1 188 ? -31.454 -12.557 30.141  0.72 27.93  ? 174 ARG C CD  1 
ATOM   6017 C  CD  B ARG C  1 188 ? -33.065 -11.602 28.896  0.08 22.28  ? 174 ARG C CD  1 
ATOM   6018 C  CD  C ARG C  1 188 ? -33.074 -11.843 30.409  0.20 25.92  ? 174 ARG C CD  1 
ATOM   6019 N  NE  A ARG C  1 188 ? -32.216 -13.747 29.743  0.72 28.10  ? 174 ARG C NE  1 
ATOM   6020 N  NE  B ARG C  1 188 ? -33.745 -12.894 29.046  0.08 22.06  ? 174 ARG C NE  1 
ATOM   6021 N  NE  C ARG C  1 188 ? -34.101 -11.488 29.423  0.20 26.37  ? 174 ARG C NE  1 
ATOM   6022 C  CZ  A ARG C  1 188 ? -31.780 -14.999 29.814  0.72 27.54  ? 174 ARG C CZ  1 
ATOM   6023 C  CZ  B ARG C  1 188 ? -34.711 -13.329 28.242  0.08 21.46  ? 174 ARG C CZ  1 
ATOM   6024 C  CZ  C ARG C  1 188 ? -35.007 -10.533 29.593  0.20 25.80  ? 174 ARG C CZ  1 
ATOM   6025 N  NH1 A ARG C  1 188 ? -30.544 -15.253 30.206  0.72 27.42  ? 174 ARG C NH1 1 
ATOM   6026 N  NH1 B ARG C  1 188 ? -35.088 -12.598 27.208  0.08 20.98  ? 174 ARG C NH1 1 
ATOM   6027 N  NH1 C ARG C  1 188 ? -34.968 -9.770  30.671  0.20 25.56  ? 174 ARG C NH1 1 
ATOM   6028 N  NH2 A ARG C  1 188 ? -32.584 -15.993 29.484  0.72 28.62  ? 174 ARG C NH2 1 
ATOM   6029 N  NH2 B ARG C  1 188 ? -35.288 -14.497 28.467  0.08 21.30  ? 174 ARG C NH2 1 
ATOM   6030 N  NH2 C ARG C  1 188 ? -35.939 -10.333 28.678  0.20 25.66  ? 174 ARG C NH2 1 
ATOM   6031 N  N   . THR C  1 189 ? -27.885 -11.225 30.818  1.00 23.74  ? 175 THR C N   1 
ATOM   6032 C  CA  . THR C  1 189 ? -26.745 -12.085 30.522  1.00 23.28  ? 175 THR C CA  1 
ATOM   6033 C  C   . THR C  1 189 ? -27.217 -13.514 30.271  1.00 22.00  ? 175 THR C C   1 
ATOM   6034 O  O   . THR C  1 189 ? -28.087 -14.030 30.971  1.00 22.41  ? 175 THR C O   1 
ATOM   6035 C  CB  . THR C  1 189 ? -25.688 -12.051 31.631  1.00 24.04  ? 175 THR C CB  1 
ATOM   6036 O  OG1 . THR C  1 189 ? -26.346 -12.337 32.862  1.00 24.07  ? 175 THR C OG1 1 
ATOM   6037 C  CG2 . THR C  1 189 ? -24.962 -10.720 31.715  1.00 23.62  ? 175 THR C CG2 1 
ATOM   6038 N  N   . VAL C  1 190 ? -26.620 -14.136 29.249  1.00 22.02  ? 176 VAL C N   1 
ATOM   6039 C  CA  . VAL C  1 190 ? -26.803 -15.552 28.983  1.00 22.11  ? 176 VAL C CA  1 
ATOM   6040 C  C   . VAL C  1 190 ? -25.781 -16.319 29.823  1.00 20.49  ? 176 VAL C C   1 
ATOM   6041 O  O   . VAL C  1 190 ? -24.577 -16.110 29.692  1.00 19.29  ? 176 VAL C O   1 
ATOM   6042 C  CB  . VAL C  1 190 ? -26.665 -15.856 27.478  1.00 22.50  ? 176 VAL C CB  1 
ATOM   6043 C  CG1 . VAL C  1 190 ? -26.845 -17.339 27.179  1.00 21.85  ? 176 VAL C CG1 1 
ATOM   6044 C  CG2 . VAL C  1 190 ? -27.626 -15.016 26.642  1.00 23.20  ? 176 VAL C CG2 1 
ATOM   6045 N  N   . LYS C  1 191 ? -26.276 -17.188 30.710  1.00 20.61  ? 177 LYS C N   1 
ATOM   6046 C  CA  . LYS C  1 191 ? -25.419 -17.890 31.654  1.00 21.84  ? 177 LYS C CA  1 
ATOM   6047 C  C   . LYS C  1 191 ? -24.596 -18.939 30.906  1.00 22.14  ? 177 LYS C C   1 
ATOM   6048 O  O   . LYS C  1 191 ? -24.991 -19.394 29.836  1.00 20.70  ? 177 LYS C O   1 
ATOM   6049 C  CB  . LYS C  1 191 ? -26.267 -18.505 32.774  1.00 24.86  ? 177 LYS C CB  1 
ATOM   6050 C  CG  . LYS C  1 191 ? -27.289 -17.563 33.407  1.00 27.73  ? 177 LYS C CG  1 
ATOM   6051 C  CD  . LYS C  1 191 ? -26.681 -16.293 33.993  1.00 28.82  ? 177 LYS C CD  1 
ATOM   6052 C  CE  . LYS C  1 191 ? -27.678 -15.416 34.704  1.00 30.30  ? 177 LYS C CE  1 
ATOM   6053 N  NZ  . LYS C  1 191 ? -28.235 -14.366 33.844  1.00 29.27  ? 177 LYS C NZ  1 
ATOM   6054 N  N   . ARG C  1 192 ? -23.452 -19.318 31.489  1.00 21.69  ? 178 ARG C N   1 
ATOM   6055 C  CA  . ARG C  1 192 ? -22.480 -20.173 30.820  1.00 23.25  ? 178 ARG C CA  1 
ATOM   6056 C  C   . ARG C  1 192 ? -23.137 -21.473 30.354  1.00 27.42  ? 178 ARG C C   1 
ATOM   6057 O  O   . ARG C  1 192 ? -22.865 -21.944 29.251  1.00 28.69  ? 178 ARG C O   1 
ATOM   6058 C  CB  . ARG C  1 192 ? -21.279 -20.465 31.730  1.00 23.11  ? 178 ARG C CB  1 
ATOM   6059 C  CG  . ARG C  1 192 ? -20.230 -21.383 31.113  1.00 23.04  ? 178 ARG C CG  1 
ATOM   6060 C  CD  . ARG C  1 192 ? -19.020 -21.582 32.012  1.00 22.79  ? 178 ARG C CD  1 
ATOM   6061 N  NE  . ARG C  1 192 ? -18.258 -20.344 32.201  1.00 21.96  ? 178 ARG C NE  1 
ATOM   6062 C  CZ  . ARG C  1 192 ? -17.261 -20.201 33.063  1.00 21.87  ? 178 ARG C CZ  1 
ATOM   6063 N  NH1 . ARG C  1 192 ? -16.891 -21.222 33.816  1.00 23.44  ? 178 ARG C NH1 1 
ATOM   6064 N  NH2 . ARG C  1 192 ? -16.642 -19.040 33.170  1.00 23.17  ? 178 ARG C NH2 1 
ATOM   6065 N  N   . HIS C  1 193 ? -23.997 -22.059 31.196  1.00 27.76  ? 179 HIS C N   1 
ATOM   6066 C  CA  . HIS C  1 193 ? -24.587 -23.351 30.881  1.00 34.07  ? 179 HIS C CA  1 
ATOM   6067 C  C   . HIS C  1 193 ? -26.057 -23.190 30.494  1.00 34.03  ? 179 HIS C C   1 
ATOM   6068 O  O   . HIS C  1 193 ? -26.834 -24.135 30.601  1.00 36.03  ? 179 HIS C O   1 
ATOM   6069 C  CB  . HIS C  1 193 ? -24.391 -24.336 32.042  1.00 34.86  ? 179 HIS C CB  1 
ATOM   6070 C  CG  . HIS C  1 193 ? -22.953 -24.590 32.363  1.00 38.15  ? 179 HIS C CG  1 
ATOM   6071 N  ND1 . HIS C  1 193 ? -22.074 -25.108 31.434  1.00 40.80  ? 179 HIS C ND1 1 
ATOM   6072 C  CD2 . HIS C  1 193 ? -22.230 -24.359 33.468  1.00 37.16  ? 179 HIS C CD2 1 
ATOM   6073 C  CE1 . HIS C  1 193 ? -20.869 -25.204 31.977  1.00 37.50  ? 179 HIS C CE1 1 
ATOM   6074 N  NE2 . HIS C  1 193 ? -20.941 -24.759 33.213  1.00 40.50  ? 179 HIS C NE2 1 
ATOM   6075 N  N   . GLU C  1 194 ? -26.426 -21.995 30.019  1.00 27.74  ? 180 GLU C N   1 
ATOM   6076 C  CA  . GLU C  1 194 ? -27.814 -21.706 29.697  1.00 27.30  ? 180 GLU C CA  1 
ATOM   6077 C  C   . GLU C  1 194 ? -28.155 -22.271 28.320  1.00 25.74  ? 180 GLU C C   1 
ATOM   6078 O  O   . GLU C  1 194 ? -27.361 -22.173 27.386  1.00 26.59  ? 180 GLU C O   1 
ATOM   6079 C  CB  . GLU C  1 194 ? -28.102 -20.204 29.754  1.00 26.16  ? 180 GLU C CB  1 
ATOM   6080 C  CG  . GLU C  1 194 ? -29.592 -19.882 29.672  1.00 25.90  ? 180 GLU C CG  1 
ATOM   6081 C  CD  . GLU C  1 194 ? -29.953 -18.442 29.983  1.00 25.62  ? 180 GLU C CD  1 
ATOM   6082 O  OE1 . GLU C  1 194 ? -29.060 -17.679 30.408  1.00 25.15  ? 180 GLU C OE1 1 
ATOM   6083 O  OE2 . GLU C  1 194 ? -31.137 -18.092 29.791  1.00 29.39  ? 180 GLU C OE2 1 
ATOM   6084 N  N   . ASP C  1 195 ? -29.352 -22.862 28.224  1.00 22.32  ? 181 ASP C N   1 
ATOM   6085 C  CA  . ASP C  1 195 ? -29.896 -23.360 26.971  1.00 24.16  ? 181 ASP C CA  1 
ATOM   6086 C  C   . ASP C  1 195 ? -30.212 -22.184 26.050  1.00 22.64  ? 181 ASP C C   1 
ATOM   6087 O  O   . ASP C  1 195 ? -30.214 -21.033 26.482  1.00 25.32  ? 181 ASP C O   1 
ATOM   6088 C  CB  . ASP C  1 195 ? -31.150 -24.195 27.200  1.00 25.14  ? 181 ASP C CB  1 
ATOM   6089 C  CG  . ASP C  1 195 ? -30.925 -25.562 27.831  1.00 30.43  ? 181 ASP C CG  1 
ATOM   6090 O  OD1 . ASP C  1 195 ? -29.748 -25.925 28.034  1.00 35.17  ? 181 ASP C OD1 1 
ATOM   6091 O  OD2 . ASP C  1 195 ? -31.930 -26.250 28.112  1.00 33.60  ? 181 ASP C OD2 1 
ATOM   6092 N  N   . ASN C  1 196 ? -30.501 -22.501 24.783  0.60 19.34  ? 182 ASN C N   1 
ATOM   6093 C  CA  . ASN C  1 196 ? -30.893 -21.511 23.794  0.60 19.90  ? 182 ASN C CA  1 
ATOM   6094 C  C   . ASN C  1 196 ? -32.102 -20.730 24.308  0.60 20.30  ? 182 ASN C C   1 
ATOM   6095 O  O   . ASN C  1 196 ? -32.890 -21.246 25.097  0.60 18.23  ? 182 ASN C O   1 
ATOM   6096 C  CB  . ASN C  1 196 ? -31.186 -22.170 22.449  0.60 20.81  ? 182 ASN C CB  1 
ATOM   6097 C  CG  . ASN C  1 196 ? -29.990 -22.901 21.882  0.60 22.53  ? 182 ASN C CG  1 
ATOM   6098 O  OD1 . ASN C  1 196 ? -30.147 -23.749 20.999  0.60 28.88  ? 182 ASN C OD1 1 
ATOM   6099 N  ND2 . ASN C  1 196 ? -28.797 -22.610 22.383  0.60 24.25  ? 182 ASN C ND2 1 
ATOM   6100 N  N   . ILE C  1 197 ? -32.244 -19.482 23.843  1.00 22.08  ? 183 ILE C N   1 
ATOM   6101 C  CA  . ILE C  1 197 ? -33.341 -18.618 24.257  1.00 23.60  ? 183 ILE C CA  1 
ATOM   6102 C  C   . ILE C  1 197 ? -34.263 -18.352 23.068  1.00 25.95  ? 183 ILE C C   1 
ATOM   6103 O  O   . ILE C  1 197 ? -33.816 -17.869 22.031  1.00 27.85  ? 183 ILE C O   1 
ATOM   6104 C  CB  . ILE C  1 197 ? -32.807 -17.298 24.845  1.00 24.93  ? 183 ILE C CB  1 
ATOM   6105 C  CG1 . ILE C  1 197 ? -31.913 -17.535 26.066  1.00 27.53  ? 183 ILE C CG1 1 
ATOM   6106 C  CG2 . ILE C  1 197 ? -33.961 -16.344 25.161  1.00 25.93  ? 183 ILE C CG2 1 
ATOM   6107 C  CD1 . ILE C  1 197 ? -31.057 -16.340 26.446  1.00 27.71  ? 183 ILE C CD1 1 
ATOM   6108 N  N   . LEU C  1 198 ? -35.557 -18.655 23.239  1.00 29.34  ? 184 LEU C N   1 
ATOM   6109 C  CA  . LEU C  1 198 ? -36.574 -18.291 22.265  1.00 31.50  ? 184 LEU C CA  1 
ATOM   6110 C  C   . LEU C  1 198 ? -36.994 -16.843 22.512  1.00 32.75  ? 184 LEU C C   1 
ATOM   6111 O  O   . LEU C  1 198 ? -37.844 -16.580 23.360  1.00 32.06  ? 184 LEU C O   1 
ATOM   6112 C  CB  . LEU C  1 198 ? -37.763 -19.249 22.367  1.00 36.47  ? 184 LEU C CB  1 
ATOM   6113 C  CG  . LEU C  1 198 ? -38.866 -19.073 21.316  1.00 39.69  ? 184 LEU C CG  1 
ATOM   6114 C  CD1 . LEU C  1 198 ? -38.363 -19.487 19.942  1.00 36.39  ? 184 LEU C CD1 1 
ATOM   6115 C  CD2 . LEU C  1 198 ? -40.126 -19.848 21.682  1.00 39.13  ? 184 LEU C CD2 1 
ATOM   6116 N  N   . LEU C  1 199 ? -36.377 -15.911 21.772  1.00 30.95  ? 185 LEU C N   1 
ATOM   6117 C  CA  . LEU C  1 199 ? -36.679 -14.490 21.881  1.00 35.76  ? 185 LEU C CA  1 
ATOM   6118 C  C   . LEU C  1 199 ? -38.075 -14.205 21.333  1.00 31.11  ? 185 LEU C C   1 
ATOM   6119 O  O   . LEU C  1 199 ? -38.780 -13.340 21.846  1.00 34.96  ? 185 LEU C O   1 
ATOM   6120 C  CB  . LEU C  1 199 ? -35.626 -13.663 21.139  1.00 35.53  ? 185 LEU C CB  1 
ATOM   6121 C  CG  . LEU C  1 199 ? -34.551 -12.992 22.000  1.00 40.53  ? 185 LEU C CG  1 
ATOM   6122 C  CD1 . LEU C  1 199 ? -33.859 -11.876 21.228  1.00 38.81  ? 185 LEU C CD1 1 
ATOM   6123 C  CD2 . LEU C  1 199 ? -35.152 -12.462 23.293  1.00 39.41  ? 185 LEU C CD2 1 
ATOM   6124 N  N   . ALA C  1 200 ? -38.447 -14.927 20.272  1.00 31.30  ? 186 ALA C N   1 
ATOM   6125 C  CA  . ALA C  1 200 ? -39.700 -14.705 19.568  1.00 31.20  ? 186 ALA C CA  1 
ATOM   6126 C  C   . ALA C  1 200 ? -39.960 -15.880 18.630  1.00 30.91  ? 186 ALA C C   1 
ATOM   6127 O  O   . ALA C  1 200 ? -39.071 -16.695 18.393  1.00 27.81  ? 186 ALA C O   1 
ATOM   6128 C  CB  . ALA C  1 200 ? -39.641 -13.395 18.809  1.00 31.86  ? 186 ALA C CB  1 
ATOM   6129 N  N   . GLU C  1 201 ? -41.181 -15.957 18.090  1.00 32.52  ? 187 GLU C N   1 
ATOM   6130 C  CA  . GLU C  1 201 ? -41.528 -17.019 17.159  1.00 31.09  ? 187 GLU C CA  1 
ATOM   6131 C  C   . GLU C  1 201 ? -40.440 -17.112 16.089  1.00 27.98  ? 187 GLU C C   1 
ATOM   6132 O  O   . GLU C  1 201 ? -40.219 -16.160 15.343  1.00 25.30  ? 187 GLU C O   1 
ATOM   6133 C  CB  . GLU C  1 201 ? -42.910 -16.761 16.553  1.00 36.34  ? 187 GLU C CB  1 
ATOM   6134 C  CG  . GLU C  1 201 ? -43.379 -17.863 15.608  1.00 35.60  ? 187 GLU C CG  1 
ATOM   6135 C  CD  . GLU C  1 201 ? -44.751 -17.624 15.000  1.00 38.57  ? 187 GLU C CD  1 
ATOM   6136 O  OE1 . GLU C  1 201 ? -45.440 -16.679 15.439  1.00 42.17  ? 187 GLU C OE1 1 
ATOM   6137 O  OE2 . GLU C  1 201 ? -45.126 -18.379 14.079  1.00 41.29  ? 187 GLU C OE2 1 
ATOM   6138 N  N   . GLY C  1 202 ? -39.748 -18.259 16.049  1.00 26.26  ? 188 GLY C N   1 
ATOM   6139 C  CA  . GLY C  1 202 ? -38.762 -18.553 15.018  1.00 25.32  ? 188 GLY C CA  1 
ATOM   6140 C  C   . GLY C  1 202 ? -37.448 -17.788 15.194  1.00 23.38  ? 188 GLY C C   1 
ATOM   6141 O  O   . GLY C  1 202 ? -36.670 -17.678 14.249  1.00 27.82  ? 188 GLY C O   1 
ATOM   6142 N  N   . VAL C  1 203 ? -37.193 -17.271 16.402  1.00 23.59  ? 189 VAL C N   1 
ATOM   6143 C  CA  . VAL C  1 203 ? -35.956 -16.555 16.679  1.00 24.28  ? 189 VAL C CA  1 
ATOM   6144 C  C   . VAL C  1 203 ? -35.358 -17.080 17.984  1.00 24.54  ? 189 VAL C C   1 
ATOM   6145 O  O   . VAL C  1 203 ? -35.921 -16.867 19.055  1.00 23.45  ? 189 VAL C O   1 
ATOM   6146 C  CB  . VAL C  1 203 ? -36.174 -15.029 16.736  1.00 23.15  ? 189 VAL C CB  1 
ATOM   6147 C  CG1 . VAL C  1 203 ? -34.868 -14.275 16.957  1.00 21.37  ? 189 VAL C CG1 1 
ATOM   6148 C  CG2 . VAL C  1 203 ? -36.883 -14.507 15.490  1.00 22.58  ? 189 VAL C CG2 1 
ATOM   6149 N  N   . LYS C  1 204 ? -34.205 -17.757 17.879  1.00 24.17  ? 190 LYS C N   1 
ATOM   6150 C  CA  . LYS C  1 204 ? -33.545 -18.368 19.025  1.00 26.90  ? 190 LYS C CA  1 
ATOM   6151 C  C   . LYS C  1 204 ? -32.128 -17.812 19.171  1.00 25.33  ? 190 LYS C C   1 
ATOM   6152 O  O   . LYS C  1 204 ? -31.376 -17.761 18.201  1.00 30.71  ? 190 LYS C O   1 
ATOM   6153 C  CB  . LYS C  1 204 ? -33.487 -19.894 18.876  1.00 29.62  ? 190 LYS C CB  1 
ATOM   6154 C  CG  . LYS C  1 204 ? -34.834 -20.609 18.849  1.00 38.09  ? 190 LYS C CG  1 
ATOM   6155 C  CD  . LYS C  1 204 ? -34.756 -22.129 18.967  1.00 45.83  ? 190 LYS C CD  1 
ATOM   6156 C  CE  . LYS C  1 204 ? -34.148 -22.589 20.261  1.00 48.98  ? 190 LYS C CE  1 
ATOM   6157 N  NZ  . LYS C  1 204 ? -34.558 -23.953 20.617  1.00 51.73  ? 190 LYS C NZ  1 
ATOM   6158 N  N   . VAL C  1 205 ? -31.770 -17.407 20.396  1.00 22.66  ? 191 VAL C N   1 
ATOM   6159 C  CA  . VAL C  1 205 ? -30.403 -17.020 20.712  1.00 23.08  ? 191 VAL C CA  1 
ATOM   6160 C  C   . VAL C  1 205 ? -29.607 -18.294 20.991  1.00 22.31  ? 191 VAL C C   1 
ATOM   6161 O  O   . VAL C  1 205 ? -29.968 -19.069 21.874  1.00 21.84  ? 191 VAL C O   1 
ATOM   6162 C  CB  . VAL C  1 205 ? -30.337 -16.045 21.906  1.00 23.98  ? 191 VAL C CB  1 
ATOM   6163 C  CG1 . VAL C  1 205 ? -28.908 -15.612 22.216  1.00 25.08  ? 191 VAL C CG1 1 
ATOM   6164 C  CG2 . VAL C  1 205 ? -31.228 -14.826 21.695  1.00 24.99  ? 191 VAL C CG2 1 
ATOM   6165 N  N   . LEU C  1 206 ? -28.534 -18.509 20.219  1.00 22.80  ? 192 LEU C N   1 
ATOM   6166 C  CA  . LEU C  1 206 ? -27.681 -19.678 20.386  1.00 20.04  ? 192 LEU C CA  1 
ATOM   6167 C  C   . LEU C  1 206 ? -26.523 -19.332 21.319  1.00 18.00  ? 192 LEU C C   1 
ATOM   6168 O  O   . LEU C  1 206 ? -25.824 -18.345 21.107  1.00 17.89  ? 192 LEU C O   1 
ATOM   6169 C  CB  . LEU C  1 206 ? -27.167 -20.145 19.025  1.00 19.72  ? 192 LEU C CB  1 
ATOM   6170 C  CG  . LEU C  1 206 ? -28.237 -20.435 17.967  1.00 21.26  ? 192 LEU C CG  1 
ATOM   6171 C  CD1 . LEU C  1 206 ? -27.590 -20.836 16.653  1.00 20.49  ? 192 LEU C CD1 1 
ATOM   6172 C  CD2 . LEU C  1 206 ? -29.207 -21.507 18.442  1.00 22.19  ? 192 LEU C CD2 1 
ATOM   6173 N  N   . ASN C  1 207 ? -26.327 -20.164 22.346  1.00 16.87  ? 193 ASN C N   1 
ATOM   6174 C  CA  . ASN C  1 207 ? -25.254 -19.974 23.311  1.00 15.89  ? 193 ASN C CA  1 
ATOM   6175 C  C   . ASN C  1 207 ? -24.037 -20.789 22.873  1.00 15.98  ? 193 ASN C C   1 
ATOM   6176 O  O   . ASN C  1 207 ? -23.963 -21.986 23.137  1.00 18.54  ? 193 ASN C O   1 
ATOM   6177 C  CB  . ASN C  1 207 ? -25.720 -20.346 24.716  1.00 16.75  ? 193 ASN C CB  1 
ATOM   6178 C  CG  . ASN C  1 207 ? -24.645 -20.158 25.760  1.00 15.54  ? 193 ASN C CG  1 
ATOM   6179 O  OD1 . ASN C  1 207 ? -23.549 -19.673 25.453  1.00 18.26  ? 193 ASN C OD1 1 
ATOM   6180 N  ND2 . ASN C  1 207 ? -24.936 -20.544 26.993  1.00 18.34  ? 193 ASN C ND2 1 
ATOM   6181 N  N   . PHE C  1 208 ? -23.080 -20.132 22.206  1.00 16.58  ? 194 PHE C N   1 
ATOM   6182 C  CA  . PHE C  1 208 ? -21.926 -20.815 21.638  1.00 17.69  ? 194 PHE C CA  1 
ATOM   6183 C  C   . PHE C  1 208 ? -20.814 -20.953 22.678  1.00 19.20  ? 194 PHE C C   1 
ATOM   6184 O  O   . PHE C  1 208 ? -19.898 -21.752 22.502  1.00 22.28  ? 194 PHE C O   1 
ATOM   6185 C  CB  . PHE C  1 208 ? -21.359 -20.074 20.422  1.00 18.52  ? 194 PHE C CB  1 
ATOM   6186 C  CG  . PHE C  1 208 ? -22.228 -20.064 19.171  1.00 19.34  ? 194 PHE C CG  1 
ATOM   6187 C  CD1 . PHE C  1 208 ? -23.013 -21.160 18.826  1.00 20.71  ? 194 PHE C CD1 1 
ATOM   6188 C  CD2 . PHE C  1 208 ? -22.230 -18.961 18.326  1.00 19.68  ? 194 PHE C CD2 1 
ATOM   6189 C  CE1 . PHE C  1 208 ? -23.789 -21.141 17.677  1.00 20.08  ? 194 PHE C CE1 1 
ATOM   6190 C  CE2 . PHE C  1 208 ? -23.006 -18.949 17.177  1.00 21.16  ? 194 PHE C CE2 1 
ATOM   6191 C  CZ  . PHE C  1 208 ? -23.785 -20.037 16.857  1.00 19.98  ? 194 PHE C CZ  1 
ATOM   6192 N  N   . GLY C  1 209 ? -20.881 -20.148 23.744  1.00 19.38  ? 195 GLY C N   1 
ATOM   6193 C  CA  . GLY C  1 209 ? -19.867 -20.171 24.787  1.00 19.36  ? 195 GLY C CA  1 
ATOM   6194 C  C   . GLY C  1 209 ? -18.521 -19.634 24.293  1.00 19.03  ? 195 GLY C C   1 
ATOM   6195 O  O   . GLY C  1 209 ? -18.473 -18.792 23.398  1.00 18.97  ? 195 GLY C O   1 
ATOM   6196 N  N   . SER C  1 210 ? -17.431 -20.144 24.883  1.00 20.21  ? 196 SER C N   1 
ATOM   6197 C  CA  . SER C  1 210 ? -16.097 -19.596 24.674  1.00 20.63  ? 196 SER C CA  1 
ATOM   6198 C  C   . SER C  1 210 ? -15.467 -20.157 23.400  1.00 19.24  ? 196 SER C C   1 
ATOM   6199 O  O   . SER C  1 210 ? -15.660 -21.321 23.055  1.00 19.01  ? 196 SER C O   1 
ATOM   6200 C  CB  . SER C  1 210 ? -15.209 -19.840 25.876  1.00 21.29  ? 196 SER C CB  1 
ATOM   6201 O  OG  . SER C  1 210 ? -15.053 -21.228 26.142  1.00 20.22  ? 196 SER C OG  1 
ATOM   6202 N  N   . GLY C  1 211 ? -14.707 -19.298 22.706  1.00 19.50  ? 197 GLY C N   1 
ATOM   6203 C  CA  . GLY C  1 211 ? -14.011 -19.676 21.487  1.00 21.33  ? 197 GLY C CA  1 
ATOM   6204 C  C   . GLY C  1 211 ? -13.184 -18.511 20.948  1.00 18.15  ? 197 GLY C C   1 
ATOM   6205 O  O   . GLY C  1 211 ? -12.127 -18.198 21.485  1.00 18.93  ? 197 GLY C O   1 
ATOM   6206 N  N   . HIS C  1 212 ? -13.691 -17.871 19.888  1.00 18.03  ? 198 HIS C N   1 
ATOM   6207 C  CA  . HIS C  1 212 ? -13.114 -16.641 19.371  1.00 18.87  ? 198 HIS C CA  1 
ATOM   6208 C  C   . HIS C  1 212 ? -12.907 -15.661 20.524  1.00 19.28  ? 198 HIS C C   1 
ATOM   6209 O  O   . HIS C  1 212 ? -11.841 -15.062 20.647  1.00 21.02  ? 198 HIS C O   1 
ATOM   6210 C  CB  . HIS C  1 212 ? -14.005 -16.063 18.263  1.00 18.36  ? 198 HIS C CB  1 
ATOM   6211 C  CG  . HIS C  1 212 ? -13.692 -14.654 17.875  1.00 19.48  ? 198 HIS C CG  1 
ATOM   6212 N  ND1 . HIS C  1 212 ? -12.532 -14.290 17.226  1.00 20.59  ? 198 HIS C ND1 1 
ATOM   6213 C  CD2 . HIS C  1 212 ? -14.387 -13.521 18.056  1.00 22.19  ? 198 HIS C CD2 1 
ATOM   6214 C  CE1 . HIS C  1 212 ? -12.539 -12.979 17.019  1.00 22.77  ? 198 HIS C CE1 1 
ATOM   6215 N  NE2 . HIS C  1 212 ? -13.658 -12.492 17.514  1.00 21.63  ? 198 HIS C NE2 1 
ATOM   6216 N  N   . ALA C  1 213 ? -13.946 -15.519 21.356  1.00 19.45  ? 199 ALA C N   1 
ATOM   6217 C  CA  . ALA C  1 213 ? -13.927 -14.629 22.507  1.00 23.48  ? 199 ALA C CA  1 
ATOM   6218 C  C   . ALA C  1 213 ? -14.419 -15.378 23.747  1.00 23.94  ? 199 ALA C C   1 
ATOM   6219 O  O   . ALA C  1 213 ? -14.620 -16.591 23.703  1.00 21.49  ? 199 ALA C O   1 
ATOM   6220 C  CB  . ALA C  1 213 ? -14.772 -13.405 22.219  1.00 21.96  ? 199 ALA C CB  1 
ATOM   6221 N  N   . TRP C  1 214 ? -14.620 -14.645 24.849  1.00 24.68  ? 200 TRP C N   1 
ATOM   6222 C  CA  . TRP C  1 214 ? -14.964 -15.246 26.131  1.00 23.20  ? 200 TRP C CA  1 
ATOM   6223 C  C   . TRP C  1 214 ? -16.336 -15.918 26.071  1.00 20.61  ? 200 TRP C C   1 
ATOM   6224 O  O   . TRP C  1 214 ? -16.527 -16.989 26.646  1.00 20.66  ? 200 TRP C O   1 
ATOM   6225 C  CB  . TRP C  1 214 ? -14.930 -14.194 27.250  1.00 24.68  ? 200 TRP C CB  1 
ATOM   6226 C  CG  . TRP C  1 214 ? -13.556 -13.675 27.590  1.00 27.85  ? 200 TRP C CG  1 
ATOM   6227 C  CD1 . TRP C  1 214 ? -12.471 -14.399 27.990  1.00 29.90  ? 200 TRP C CD1 1 
ATOM   6228 C  CD2 . TRP C  1 214 ? -13.121 -12.296 27.549  1.00 28.75  ? 200 TRP C CD2 1 
ATOM   6229 N  NE1 . TRP C  1 214 ? -11.399 -13.574 28.207  1.00 32.00  ? 200 TRP C NE1 1 
ATOM   6230 C  CE2 . TRP C  1 214 ? -11.764 -12.279 27.944  1.00 30.82  ? 200 TRP C CE2 1 
ATOM   6231 C  CE3 . TRP C  1 214 ? -13.741 -11.085 27.221  1.00 26.18  ? 200 TRP C CE3 1 
ATOM   6232 C  CZ2 . TRP C  1 214 ? -11.025 -11.099 28.017  1.00 28.33  ? 200 TRP C CZ2 1 
ATOM   6233 C  CZ3 . TRP C  1 214 ? -13.010 -9.919  27.296  1.00 27.11  ? 200 TRP C CZ3 1 
ATOM   6234 C  CH2 . TRP C  1 214 ? -11.670 -9.929  27.688  1.00 28.17  ? 200 TRP C CH2 1 
ATOM   6235 N  N   . GLY C  1 215 ? -17.293 -15.266 25.400  1.00 18.57  ? 201 GLY C N   1 
ATOM   6236 C  CA  . GLY C  1 215 ? -18.659 -15.763 25.322  1.00 19.03  ? 201 GLY C CA  1 
ATOM   6237 C  C   . GLY C  1 215 ? -19.338 -15.317 24.029  1.00 18.17  ? 201 GLY C C   1 
ATOM   6238 O  O   . GLY C  1 215 ? -19.613 -14.135 23.851  1.00 21.25  ? 201 GLY C O   1 
ATOM   6239 N  N   . MET C  1 216 ? -19.597 -16.282 23.137  1.00 18.66  ? 202 MET C N   1 
ATOM   6240 C  CA  . MET C  1 216 ? -20.151 -16.005 21.820  1.00 18.98  ? 202 MET C CA  1 
ATOM   6241 C  C   . MET C  1 216 ? -21.641 -16.348 21.797  1.00 19.39  ? 202 MET C C   1 
ATOM   6242 O  O   . MET C  1 216 ? -22.049 -17.390 22.304  1.00 19.32  ? 202 MET C O   1 
ATOM   6243 C  CB  . MET C  1 216 ? -19.431 -16.826 20.742  1.00 18.38  ? 202 MET C CB  1 
ATOM   6244 C  CG  . MET C  1 216 ? -17.926 -16.587 20.678  1.00 19.75  ? 202 MET C CG  1 
ATOM   6245 S  SD  . MET C  1 216 ? -17.480 -14.881 20.293  1.00 22.12  ? 202 MET C SD  1 
ATOM   6246 C  CE  . MET C  1 216 ? -18.104 -14.715 18.616  1.00 21.12  ? 202 MET C CE  1 
ATOM   6247 N  N   . LEU C  1 217 ? -22.440 -15.461 21.189  1.00 20.08  ? 203 LEU C N   1 
ATOM   6248 C  CA  . LEU C  1 217 ? -23.854 -15.713 20.956  1.00 19.61  ? 203 LEU C CA  1 
ATOM   6249 C  C   . LEU C  1 217 ? -24.117 -15.728 19.452  1.00 20.95  ? 203 LEU C C   1 
ATOM   6250 O  O   . LEU C  1 217 ? -23.591 -14.895 18.716  1.00 17.78  ? 203 LEU C O   1 
ATOM   6251 C  CB  . LEU C  1 217 ? -24.716 -14.650 21.642  1.00 19.14  ? 203 LEU C CB  1 
ATOM   6252 C  CG  . LEU C  1 217 ? -24.689 -14.628 23.174  1.00 20.29  ? 203 LEU C CG  1 
ATOM   6253 C  CD1 . LEU C  1 217 ? -25.717 -13.638 23.713  1.00 19.21  ? 203 LEU C CD1 1 
ATOM   6254 C  CD2 . LEU C  1 217 ? -24.931 -16.018 23.755  1.00 19.35  ? 203 LEU C CD2 1 
ATOM   6255 N  N   . GLY C  1 218 ? -24.943 -16.681 19.009  1.00 19.65  ? 204 GLY C N   1 
ATOM   6256 C  CA  . GLY C  1 218 ? -25.449 -16.688 17.647  1.00 18.72  ? 204 GLY C CA  1 
ATOM   6257 C  C   . GLY C  1 218 ? -26.970 -16.548 17.624  1.00 19.78  ? 204 GLY C C   1 
ATOM   6258 O  O   . GLY C  1 218 ? -27.602 -16.420 18.669  1.00 20.72  ? 204 GLY C O   1 
ATOM   6259 N  N   . LEU C  1 219 ? -27.545 -16.578 16.416  1.00 19.57  ? 205 LEU C N   1 
ATOM   6260 C  CA  . LEU C  1 219 ? -28.987 -16.507 16.242  1.00 21.85  ? 205 LEU C CA  1 
ATOM   6261 C  C   . LEU C  1 219 ? -29.398 -17.525 15.181  1.00 22.11  ? 205 LEU C C   1 
ATOM   6262 O  O   . LEU C  1 219 ? -28.753 -17.631 14.139  1.00 21.99  ? 205 LEU C O   1 
ATOM   6263 C  CB  . LEU C  1 219 ? -29.374 -15.081 15.839  1.00 23.77  ? 205 LEU C CB  1 
ATOM   6264 C  CG  . LEU C  1 219 ? -30.713 -14.557 16.371  1.00 26.41  ? 205 LEU C CG  1 
ATOM   6265 C  CD1 . LEU C  1 219 ? -30.664 -14.396 17.883  1.00 26.96  ? 205 LEU C CD1 1 
ATOM   6266 C  CD2 . LEU C  1 219 ? -31.090 -13.240 15.709  1.00 27.01  ? 205 LEU C CD2 1 
ATOM   6267 N  N   . HIS C  1 220 ? -30.447 -18.303 15.472  1.00 22.02  ? 206 HIS C N   1 
ATOM   6268 C  CA  . HIS C  1 220 ? -31.146 -19.049 14.438  1.00 24.37  ? 206 HIS C CA  1 
ATOM   6269 C  C   . HIS C  1 220 ? -32.474 -18.352 14.153  1.00 25.52  ? 206 HIS C C   1 
ATOM   6270 O  O   . HIS C  1 220 ? -33.290 -18.170 15.054  1.00 23.88  ? 206 HIS C O   1 
ATOM   6271 C  CB  . HIS C  1 220 ? -31.370 -20.516 14.825  1.00 23.75  ? 206 HIS C CB  1 
ATOM   6272 C  CG  . HIS C  1 220 ? -32.143 -21.264 13.788  1.00 27.33  ? 206 HIS C CG  1 
ATOM   6273 N  ND1 . HIS C  1 220 ? -31.582 -21.661 12.592  1.00 30.03  ? 206 HIS C ND1 1 
ATOM   6274 C  CD2 . HIS C  1 220 ? -33.427 -21.649 13.738  1.00 28.84  ? 206 HIS C CD2 1 
ATOM   6275 C  CE1 . HIS C  1 220 ? -32.497 -22.281 11.862  1.00 26.09  ? 206 HIS C CE1 1 
ATOM   6276 N  NE2 . HIS C  1 220 ? -33.626 -22.284 12.537  1.00 30.86  ? 206 HIS C NE2 1 
ATOM   6277 N  N   . VAL C  1 221 ? -32.669 -17.950 12.893  1.00 26.45  ? 207 VAL C N   1 
ATOM   6278 C  CA  . VAL C  1 221 ? -33.913 -17.326 12.474  1.00 26.39  ? 207 VAL C CA  1 
ATOM   6279 C  C   . VAL C  1 221 ? -34.605 -18.252 11.474  1.00 24.38  ? 207 VAL C C   1 
ATOM   6280 O  O   . VAL C  1 221 ? -33.993 -18.677 10.497  1.00 20.27  ? 207 VAL C O   1 
ATOM   6281 C  CB  . VAL C  1 221 ? -33.663 -15.925 11.879  1.00 27.52  ? 207 VAL C CB  1 
ATOM   6282 C  CG1 . VAL C  1 221 ? -34.968 -15.207 11.551  1.00 29.08  ? 207 VAL C CG1 1 
ATOM   6283 C  CG2 . VAL C  1 221 ? -32.797 -15.068 12.797  1.00 27.16  ? 207 VAL C CG2 1 
ATOM   6284 N  N   . GLU C  1 222 ? -35.875 -18.582 11.749  1.00 22.40  ? 208 GLU C N   1 
ATOM   6285 C  CA  . GLU C  1 222 ? -36.700 -19.351 10.829  1.00 25.60  ? 208 GLU C CA  1 
ATOM   6286 C  C   . GLU C  1 222 ? -37.710 -18.413 10.166  1.00 25.73  ? 208 GLU C C   1 
ATOM   6287 O  O   . GLU C  1 222 ? -38.698 -18.023 10.785  1.00 27.87  ? 208 GLU C O   1 
ATOM   6288 C  CB  . GLU C  1 222 ? -37.425 -20.489 11.553  1.00 28.90  ? 208 GLU C CB  1 
ATOM   6289 C  CG  . GLU C  1 222 ? -38.273 -21.359 10.628  1.00 33.44  ? 208 GLU C CG  1 
ATOM   6290 C  CD  . GLU C  1 222 ? -37.460 -22.210 9.669   1.00 34.92  ? 208 GLU C CD  1 
ATOM   6291 O  OE1 . GLU C  1 222 ? -36.239 -22.335 9.893   1.00 39.17  ? 208 GLU C OE1 1 
ATOM   6292 O  OE2 . GLU C  1 222 ? -38.041 -22.734 8.696   1.00 36.58  ? 208 GLU C OE2 1 
ATOM   6293 N  N   . LEU C  1 223 ? -37.445 -18.053 8.905   1.00 26.95  ? 209 LEU C N   1 
ATOM   6294 C  CA  . LEU C  1 223 ? -38.309 -17.156 8.152   1.00 27.43  ? 209 LEU C CA  1 
ATOM   6295 C  C   . LEU C  1 223 ? -39.263 -17.974 7.280   1.00 28.10  ? 209 LEU C C   1 
ATOM   6296 O  O   . LEU C  1 223 ? -38.857 -18.956 6.660   1.00 29.20  ? 209 LEU C O   1 
ATOM   6297 C  CB  . LEU C  1 223 ? -37.446 -16.208 7.316   1.00 26.40  ? 209 LEU C CB  1 
ATOM   6298 C  CG  . LEU C  1 223 ? -36.615 -15.182 8.093   1.00 26.93  ? 209 LEU C CG  1 
ATOM   6299 C  CD1 . LEU C  1 223 ? -35.678 -14.417 7.168   1.00 26.50  ? 209 LEU C CD1 1 
ATOM   6300 C  CD2 . LEU C  1 223 ? -37.514 -14.218 8.848   1.00 30.25  ? 209 LEU C CD2 1 
ATOM   6301 N  N   . PRO C  1 224 ? -40.561 -17.598 7.206   1.00 31.00  ? 210 PRO C N   1 
ATOM   6302 C  CA  . PRO C  1 224 ? -41.544 -18.354 6.425   1.00 34.62  ? 210 PRO C CA  1 
ATOM   6303 C  C   . PRO C  1 224 ? -41.097 -18.668 4.998   1.00 32.69  ? 210 PRO C C   1 
ATOM   6304 O  O   . PRO C  1 224 ? -41.284 -19.789 4.531   1.00 34.06  ? 210 PRO C O   1 
ATOM   6305 C  CB  . PRO C  1 224 ? -42.789 -17.443 6.469   1.00 33.09  ? 210 PRO C CB  1 
ATOM   6306 C  CG  . PRO C  1 224 ? -42.648 -16.701 7.781   1.00 32.94  ? 210 PRO C CG  1 
ATOM   6307 C  CD  . PRO C  1 224 ? -41.153 -16.436 7.890   1.00 34.32  ? 210 PRO C CD  1 
ATOM   6308 N  N   . GLU C  1 225 ? -40.496 -17.685 4.312   1.00 35.24  ? 211 GLU C N   1 
ATOM   6309 C  CA  . GLU C  1 225 ? -40.129 -17.852 2.913   1.00 35.84  ? 211 GLU C CA  1 
ATOM   6310 C  C   . GLU C  1 225 ? -38.666 -18.279 2.765   1.00 32.61  ? 211 GLU C C   1 
ATOM   6311 O  O   . GLU C  1 225 ? -38.385 -19.247 2.061   1.00 31.79  ? 211 GLU C O   1 
ATOM   6312 C  CB  . GLU C  1 225 ? -40.413 -16.585 2.104   1.00 37.57  ? 211 GLU C CB  1 
ATOM   6313 C  CG  . GLU C  1 225 ? -41.881 -16.165 2.132   1.00 49.29  ? 211 GLU C CG  1 
ATOM   6314 C  CD  . GLU C  1 225 ? -42.875 -17.307 2.000   1.00 51.61  ? 211 GLU C CD  1 
ATOM   6315 O  OE1 . GLU C  1 225 ? -42.856 -17.990 0.954   1.00 54.84  ? 211 GLU C OE1 1 
ATOM   6316 O  OE2 . GLU C  1 225 ? -43.669 -17.513 2.944   1.00 50.64  ? 211 GLU C OE2 1 
ATOM   6317 N  N   . THR C  1 226 ? -37.737 -17.552 3.403   1.00 28.57  ? 212 THR C N   1 
ATOM   6318 C  CA  . THR C  1 226 ? -36.311 -17.770 3.183   1.00 29.52  ? 212 THR C CA  1 
ATOM   6319 C  C   . THR C  1 226 ? -35.877 -19.069 3.868   1.00 27.77  ? 212 THR C C   1 
ATOM   6320 O  O   . THR C  1 226 ? -34.908 -19.697 3.447   1.00 29.72  ? 212 THR C O   1 
ATOM   6321 C  CB  . THR C  1 226 ? -35.488 -16.568 3.662   1.00 32.42  ? 212 THR C CB  1 
ATOM   6322 O  OG1 . THR C  1 226 ? -36.044 -15.409 3.047   1.00 29.65  ? 212 THR C OG1 1 
ATOM   6323 C  CG2 . THR C  1 226 ? -34.014 -16.671 3.304   1.00 33.53  ? 212 THR C CG2 1 
ATOM   6324 N  N   . GLY C  1 227 ? -36.610 -19.477 4.911   1.00 26.25  ? 213 GLY C N   1 
ATOM   6325 C  CA  . GLY C  1 227 ? -36.254 -20.660 5.680   1.00 26.89  ? 213 GLY C CA  1 
ATOM   6326 C  C   . GLY C  1 227 ? -35.287 -20.317 6.812   1.00 26.96  ? 213 GLY C C   1 
ATOM   6327 O  O   . GLY C  1 227 ? -35.381 -19.244 7.406   1.00 24.44  ? 213 GLY C O   1 
ATOM   6328 N  N   . GLY C  1 228 ? -34.338 -21.224 7.081   1.00 27.55  ? 214 GLY C N   1 
ATOM   6329 C  CA  . GLY C  1 228 ? -33.472 -21.119 8.247   1.00 24.54  ? 214 GLY C CA  1 
ATOM   6330 C  C   . GLY C  1 228 ? -32.192 -20.334 7.963   1.00 22.88  ? 214 GLY C C   1 
ATOM   6331 O  O   . GLY C  1 228 ? -31.530 -20.558 6.949   1.00 21.64  ? 214 GLY C O   1 
ATOM   6332 N  N   . ILE C  1 229 ? -31.852 -19.422 8.887   1.00 20.65  ? 215 ILE C N   1 
ATOM   6333 C  CA  . ILE C  1 229 ? -30.609 -18.665 8.837   1.00 21.75  ? 215 ILE C CA  1 
ATOM   6334 C  C   . ILE C  1 229 ? -29.905 -18.772 10.189  1.00 22.26  ? 215 ILE C C   1 
ATOM   6335 O  O   . ILE C  1 229 ? -30.539 -18.603 11.229  1.00 21.32  ? 215 ILE C O   1 
ATOM   6336 C  CB  . ILE C  1 229 ? -30.867 -17.185 8.490   1.00 22.54  ? 215 ILE C CB  1 
ATOM   6337 C  CG1 . ILE C  1 229 ? -31.679 -17.015 7.205   1.00 24.88  ? 215 ILE C CG1 1 
ATOM   6338 C  CG2 . ILE C  1 229 ? -29.549 -16.410 8.436   1.00 23.46  ? 215 ILE C CG2 1 
ATOM   6339 C  CD1 . ILE C  1 229 ? -32.353 -15.660 7.083   1.00 27.39  ? 215 ILE C CD1 1 
ATOM   6340 N  N   . ILE C  1 230 ? -28.589 -19.021 10.159  1.00 20.10  ? 216 ILE C N   1 
ATOM   6341 C  CA  . ILE C  1 230 ? -27.759 -18.946 11.352  1.00 20.45  ? 216 ILE C CA  1 
ATOM   6342 C  C   . ILE C  1 230 ? -26.807 -17.759 11.214  1.00 23.14  ? 216 ILE C C   1 
ATOM   6343 O  O   . ILE C  1 230 ? -25.983 -17.726 10.301  1.00 22.76  ? 216 ILE C O   1 
ATOM   6344 C  CB  . ILE C  1 230 ? -26.988 -20.260 11.588  1.00 21.98  ? 216 ILE C CB  1 
ATOM   6345 C  CG1 . ILE C  1 230 ? -27.930 -21.449 11.795  1.00 22.48  ? 216 ILE C CG1 1 
ATOM   6346 C  CG2 . ILE C  1 230 ? -26.009 -20.107 12.754  1.00 22.86  ? 216 ILE C CG2 1 
ATOM   6347 C  CD1 . ILE C  1 230 ? -27.264 -22.804 11.625  1.00 26.28  ? 216 ILE C CD1 1 
ATOM   6348 N  N   . LEU C  1 231 ? -26.948 -16.781 12.119  1.00 21.88  ? 217 LEU C N   1 
ATOM   6349 C  CA  . LEU C  1 231 ? -25.990 -15.693 12.246  1.00 21.27  ? 217 LEU C CA  1 
ATOM   6350 C  C   . LEU C  1 231 ? -24.860 -16.153 13.166  1.00 21.74  ? 217 LEU C C   1 
ATOM   6351 O  O   . LEU C  1 231 ? -25.065 -16.307 14.367  1.00 20.47  ? 217 LEU C O   1 
ATOM   6352 C  CB  . LEU C  1 231 ? -26.695 -14.446 12.784  1.00 21.78  ? 217 LEU C CB  1 
ATOM   6353 C  CG  . LEU C  1 231 ? -27.931 -13.980 12.006  1.00 24.02  ? 217 LEU C CG  1 
ATOM   6354 C  CD1 . LEU C  1 231 ? -28.528 -12.717 12.611  1.00 24.70  ? 217 LEU C CD1 1 
ATOM   6355 C  CD2 . LEU C  1 231 ? -27.597 -13.762 10.540  1.00 23.25  ? 217 LEU C CD2 1 
ATOM   6356 N  N   . ALA C  1 232 ? -23.675 -16.388 12.584  1.00 20.84  ? 218 ALA C N   1 
ATOM   6357 C  CA  . ALA C  1 232 ? -22.553 -16.977 13.299  1.00 20.94  ? 218 ALA C CA  1 
ATOM   6358 C  C   . ALA C  1 232 ? -21.684 -15.893 13.935  1.00 19.28  ? 218 ALA C C   1 
ATOM   6359 O  O   . ALA C  1 232 ? -21.004 -16.148 14.925  1.00 19.87  ? 218 ALA C O   1 
ATOM   6360 C  CB  . ALA C  1 232 ? -21.736 -17.835 12.354  1.00 23.07  ? 218 ALA C CB  1 
ATOM   6361 N  N   . SER C  1 233 ? -21.713 -14.687 13.357  1.00 19.21  ? 219 SER C N   1 
ATOM   6362 C  CA  . SER C  1 233 ? -20.774 -13.634 13.712  1.00 20.56  ? 219 SER C CA  1 
ATOM   6363 C  C   . SER C  1 233 ? -19.346 -14.176 13.642  1.00 20.39  ? 219 SER C C   1 
ATOM   6364 O  O   . SER C  1 233 ? -19.016 -14.938 12.736  1.00 20.73  ? 219 SER C O   1 
ATOM   6365 C  CB  . SER C  1 233 ? -21.090 -13.045 15.067  1.00 25.16  ? 219 SER C CB  1 
ATOM   6366 O  OG  . SER C  1 233 ? -20.258 -11.927 15.348  1.00 21.17  ? 219 SER C OG  1 
ATOM   6367 N  N   . ASP C  1 234 ? -18.508 -13.798 14.618  1.00 21.27  ? 220 ASP C N   1 
ATOM   6368 C  CA  . ASP C  1 234 ? -17.084 -14.101 14.580  1.00 21.87  ? 220 ASP C CA  1 
ATOM   6369 C  C   . ASP C  1 234 ? -16.799 -15.523 15.065  1.00 20.74  ? 220 ASP C C   1 
ATOM   6370 O  O   . ASP C  1 234 ? -15.638 -15.889 15.234  1.00 21.55  ? 220 ASP C O   1 
ATOM   6371 C  CB  . ASP C  1 234 ? -16.272 -13.071 15.353  1.00 23.69  ? 220 ASP C CB  1 
ATOM   6372 C  CG  . ASP C  1 234 ? -16.157 -11.712 14.678  1.00 26.25  ? 220 ASP C CG  1 
ATOM   6373 O  OD1 . ASP C  1 234 ? -16.683 -11.577 13.553  1.00 24.42  ? 220 ASP C OD1 1 
ATOM   6374 O  OD2 . ASP C  1 234 ? -15.549 -10.803 15.283  1.00 28.07  ? 220 ASP C OD2 1 
ATOM   6375 N  N   . ALA C  1 235 ? -17.850 -16.324 15.284  1.00 20.58  ? 221 ALA C N   1 
ATOM   6376 C  CA  . ALA C  1 235 ? -17.671 -17.754 15.483  1.00 20.89  ? 221 ALA C CA  1 
ATOM   6377 C  C   . ALA C  1 235 ? -17.108 -18.363 14.200  1.00 22.57  ? 221 ALA C C   1 
ATOM   6378 O  O   . ALA C  1 235 ? -16.344 -19.326 14.248  1.00 23.48  ? 221 ALA C O   1 
ATOM   6379 C  CB  . ALA C  1 235 ? -18.976 -18.409 15.892  1.00 19.96  ? 221 ALA C CB  1 
ATOM   6380 N  N   . ILE C  1 236 ? -17.502 -17.783 13.058  1.00 23.11  ? 222 ILE C N   1 
ATOM   6381 C  CA  . ILE C  1 236 ? -16.948 -18.142 11.759  1.00 24.11  ? 222 ILE C CA  1 
ATOM   6382 C  C   . ILE C  1 236 ? -16.776 -16.869 10.926  1.00 25.45  ? 222 ILE C C   1 
ATOM   6383 O  O   . ILE C  1 236 ? -17.751 -16.332 10.406  1.00 25.68  ? 222 ILE C O   1 
ATOM   6384 C  CB  . ILE C  1 236 ? -17.840 -19.168 11.030  1.00 25.99  ? 222 ILE C CB  1 
ATOM   6385 C  CG1 . ILE C  1 236 ? -18.427 -20.229 11.975  1.00 25.09  ? 222 ILE C CG1 1 
ATOM   6386 C  CG2 . ILE C  1 236 ? -17.076 -19.807 9.869   1.00 23.69  ? 222 ILE C CG2 1 
ATOM   6387 C  CD1 . ILE C  1 236 ? -19.464 -21.128 11.322  1.00 23.50  ? 222 ILE C CD1 1 
ATOM   6388 N  N   . TYR C  1 237 ? -15.524 -16.405 10.790  1.00 24.38  ? 223 TYR C N   1 
ATOM   6389 C  CA  . TYR C  1 237 ? -15.200 -15.180 10.070  1.00 24.24  ? 223 TYR C CA  1 
ATOM   6390 C  C   . TYR C  1 237 ? -15.637 -15.268 8.605   1.00 23.84  ? 223 TYR C C   1 
ATOM   6391 O  O   . TYR C  1 237 ? -16.397 -14.420 8.136   1.00 25.65  ? 223 TYR C O   1 
ATOM   6392 C  CB  . TYR C  1 237 ? -13.692 -14.902 10.116  1.00 25.95  ? 223 TYR C CB  1 
ATOM   6393 C  CG  . TYR C  1 237 ? -13.121 -14.094 11.277  1.00 24.65  ? 223 TYR C CG  1 
ATOM   6394 C  CD1 . TYR C  1 237 ? -13.884 -13.172 11.988  1.00 24.90  ? 223 TYR C CD1 1 
ATOM   6395 C  CD2 . TYR C  1 237 ? -11.783 -14.231 11.631  1.00 24.48  ? 223 TYR C CD2 1 
ATOM   6396 C  CE1 . TYR C  1 237 ? -13.336 -12.431 13.025  1.00 23.86  ? 223 TYR C CE1 1 
ATOM   6397 C  CE2 . TYR C  1 237 ? -11.224 -13.497 12.663  1.00 24.54  ? 223 TYR C CE2 1 
ATOM   6398 C  CZ  . TYR C  1 237 ? -12.002 -12.592 13.361  1.00 24.69  ? 223 TYR C CZ  1 
ATOM   6399 O  OH  . TYR C  1 237 ? -11.437 -11.874 14.375  1.00 26.12  ? 223 TYR C OH  1 
ATOM   6400 N  N   . THR C  1 238 ? -15.116 -16.268 7.876   1.00 23.96  ? 224 THR C N   1 
ATOM   6401 C  CA  . THR C  1 238 ? -15.337 -16.384 6.439   1.00 24.21  ? 224 THR C CA  1 
ATOM   6402 C  C   . THR C  1 238 ? -15.603 -17.839 6.060   1.00 24.81  ? 224 THR C C   1 
ATOM   6403 O  O   . THR C  1 238 ? -15.468 -18.743 6.880   1.00 25.49  ? 224 THR C O   1 
ATOM   6404 C  CB  . THR C  1 238 ? -14.137 -15.861 5.642   1.00 24.14  ? 224 THR C CB  1 
ATOM   6405 O  OG1 . THR C  1 238 ? -13.074 -16.790 5.829   1.00 25.51  ? 224 THR C OG1 1 
ATOM   6406 C  CG2 . THR C  1 238 ? -13.694 -14.470 6.058   1.00 25.33  ? 224 THR C CG2 1 
ATOM   6407 N  N   . ALA C  1 239 ? -15.958 -18.047 4.785   1.00 22.49  ? 225 ALA C N   1 
ATOM   6408 C  CA  . ALA C  1 239 ? -16.110 -19.380 4.228   1.00 22.88  ? 225 ALA C CA  1 
ATOM   6409 C  C   . ALA C  1 239 ? -14.781 -20.131 4.313   1.00 22.85  ? 225 ALA C C   1 
ATOM   6410 O  O   . ALA C  1 239 ? -14.763 -21.359 4.380   1.00 26.35  ? 225 ALA C O   1 
ATOM   6411 C  CB  . ALA C  1 239 ? -16.611 -19.286 2.799   1.00 22.86  ? 225 ALA C CB  1 
ATOM   6412 N  N   . GLU C  1 240 ? -13.674 -19.377 4.321   1.00 26.25  ? 226 GLU C N   1 
ATOM   6413 C  CA  . GLU C  1 240 ? -12.336 -19.947 4.412   1.00 28.82  ? 226 GLU C CA  1 
ATOM   6414 C  C   . GLU C  1 240 ? -12.149 -20.550 5.804   1.00 28.31  ? 226 GLU C C   1 
ATOM   6415 O  O   . GLU C  1 240 ? -11.576 -21.630 5.950   1.00 24.09  ? 226 GLU C O   1 
ATOM   6416 C  CB  . GLU C  1 240 ? -11.274 -18.885 4.108   1.00 28.83  ? 226 GLU C CB  1 
ATOM   6417 C  CG  . GLU C  1 240 ? -9.884  -19.457 3.835   1.00 31.79  ? 226 GLU C CG  1 
ATOM   6418 C  CD  . GLU C  1 240 ? -8.826  -18.431 3.458   1.00 35.92  ? 226 GLU C CD  1 
ATOM   6419 O  OE1 . GLU C  1 240 ? -9.097  -17.215 3.551   1.00 34.12  ? 226 GLU C OE1 1 
ATOM   6420 O  OE2 . GLU C  1 240 ? -7.723  -18.856 3.056   1.00 39.33  ? 226 GLU C OE2 1 
ATOM   6421 N  N   . SER C  1 241 ? -12.646 -19.835 6.820   1.00 27.80  ? 227 SER C N   1 
ATOM   6422 C  CA  . SER C  1 241 ? -12.652 -20.323 8.189   1.00 24.13  ? 227 SER C CA  1 
ATOM   6423 C  C   . SER C  1 241 ? -13.408 -21.648 8.261   1.00 21.91  ? 227 SER C C   1 
ATOM   6424 O  O   . SER C  1 241 ? -12.963 -22.590 8.913   1.00 23.04  ? 227 SER C O   1 
ATOM   6425 C  CB  . SER C  1 241 ? -13.272 -19.304 9.122   1.00 22.26  ? 227 SER C CB  1 
ATOM   6426 O  OG  . SER C  1 241 ? -12.692 -18.019 8.944   1.00 24.55  ? 227 SER C OG  1 
ATOM   6427 N  N   . TYR C  1 242 ? -14.549 -21.696 7.565   1.00 23.07  ? 228 TYR C N   1 
ATOM   6428 C  CA  . TYR C  1 242 ? -15.544 -22.748 7.725   1.00 21.88  ? 228 TYR C CA  1 
ATOM   6429 C  C   . TYR C  1 242 ? -15.070 -24.040 7.062   1.00 24.99  ? 228 TYR C C   1 
ATOM   6430 O  O   . TYR C  1 242 ? -15.357 -25.132 7.550   1.00 24.40  ? 228 TYR C O   1 
ATOM   6431 C  CB  . TYR C  1 242 ? -16.856 -22.236 7.118   1.00 21.24  ? 228 TYR C CB  1 
ATOM   6432 C  CG  . TYR C  1 242 ? -18.121 -23.020 7.454   1.00 21.83  ? 228 TYR C CG  1 
ATOM   6433 C  CD1 . TYR C  1 242 ? -18.416 -23.401 8.760   1.00 23.02  ? 228 TYR C CD1 1 
ATOM   6434 C  CD2 . TYR C  1 242 ? -19.033 -23.368 6.463   1.00 23.50  ? 228 TYR C CD2 1 
ATOM   6435 C  CE1 . TYR C  1 242 ? -19.571 -24.104 9.067   1.00 21.21  ? 228 TYR C CE1 1 
ATOM   6436 C  CE2 . TYR C  1 242 ? -20.192 -24.068 6.758   1.00 22.98  ? 228 TYR C CE2 1 
ATOM   6437 C  CZ  . TYR C  1 242 ? -20.464 -24.436 8.064   1.00 22.40  ? 228 TYR C CZ  1 
ATOM   6438 O  OH  . TYR C  1 242 ? -21.608 -25.125 8.348   1.00 25.05  ? 228 TYR C OH  1 
ATOM   6439 N  N   . GLY C  1 243 ? -14.351 -23.910 5.942   1.00 27.27  ? 229 GLY C N   1 
ATOM   6440 C  CA  . GLY C  1 243 ? -13.895 -25.075 5.199   1.00 31.08  ? 229 GLY C CA  1 
ATOM   6441 C  C   . GLY C  1 243 ? -15.067 -25.991 4.851   1.00 28.99  ? 229 GLY C C   1 
ATOM   6442 O  O   . GLY C  1 243 ? -16.109 -25.518 4.402   1.00 34.99  ? 229 GLY C O   1 
ATOM   6443 N  N   . PRO C  1 244 ? -14.949 -27.325 5.055   1.00 33.32  ? 230 PRO C N   1 
ATOM   6444 C  CA  . PRO C  1 244 ? -13.728 -27.936 5.588   1.00 35.32  ? 230 PRO C CA  1 
ATOM   6445 C  C   . PRO C  1 244 ? -12.538 -27.813 4.638   1.00 41.41  ? 230 PRO C C   1 
ATOM   6446 O  O   . PRO C  1 244 ? -12.720 -27.696 3.428   1.00 40.02  ? 230 PRO C O   1 
ATOM   6447 C  CB  . PRO C  1 244 ? -14.119 -29.415 5.811   1.00 35.97  ? 230 PRO C CB  1 
ATOM   6448 C  CG  . PRO C  1 244 ? -15.636 -29.444 5.736   1.00 36.33  ? 230 PRO C CG  1 
ATOM   6449 C  CD  . PRO C  1 244 ? -16.010 -28.312 4.798   1.00 33.31  ? 230 PRO C CD  1 
ATOM   6450 N  N   . PRO C  1 245 ? -11.284 -27.843 5.153   1.00 42.65  ? 231 PRO C N   1 
ATOM   6451 C  CA  . PRO C  1 245 ? -11.036 -27.957 6.591   1.00 39.31  ? 231 PRO C CA  1 
ATOM   6452 C  C   . PRO C  1 245 ? -11.247 -26.631 7.312   1.00 33.59  ? 231 PRO C C   1 
ATOM   6453 O  O   . PRO C  1 245 ? -11.164 -25.568 6.700   1.00 32.06  ? 231 PRO C O   1 
ATOM   6454 C  CB  . PRO C  1 245 ? -9.562  -28.389 6.628   1.00 39.69  ? 231 PRO C CB  1 
ATOM   6455 C  CG  . PRO C  1 245 ? -8.956  -27.660 5.447   1.00 40.01  ? 231 PRO C CG  1 
ATOM   6456 C  CD  . PRO C  1 245 ? -10.035 -27.758 4.374   1.00 39.73  ? 231 PRO C CD  1 
ATOM   6457 N  N   . ILE C  1 246 ? -11.494 -26.707 8.623   1.00 30.37  ? 232 ILE C N   1 
ATOM   6458 C  CA  . ILE C  1 246 ? -11.600 -25.511 9.441   1.00 29.06  ? 232 ILE C CA  1 
ATOM   6459 C  C   . ILE C  1 246 ? -10.231 -24.836 9.508   1.00 26.93  ? 232 ILE C C   1 
ATOM   6460 O  O   . ILE C  1 246 ? -9.217  -25.489 9.740   1.00 28.45  ? 232 ILE C O   1 
ATOM   6461 C  CB  . ILE C  1 246 ? -12.139 -25.838 10.847  1.00 26.07  ? 232 ILE C CB  1 
ATOM   6462 C  CG1 . ILE C  1 246 ? -13.544 -26.451 10.798  1.00 27.27  ? 232 ILE C CG1 1 
ATOM   6463 C  CG2 . ILE C  1 246 ? -12.099 -24.593 11.732  1.00 23.89  ? 232 ILE C CG2 1 
ATOM   6464 C  CD1 . ILE C  1 246 ? -14.004 -27.058 12.111  1.00 27.70  ? 232 ILE C CD1 1 
ATOM   6465 N  N   . LYS C  1 247 ? -10.225 -23.515 9.299   1.00 27.29  ? 233 LYS C N   1 
ATOM   6466 C  CA  . LYS C  1 247 ? -9.028  -22.704 9.432   1.00 28.73  ? 233 LYS C CA  1 
ATOM   6467 C  C   . LYS C  1 247 ? -9.255  -21.676 10.537  1.00 26.40  ? 233 LYS C C   1 
ATOM   6468 O  O   . LYS C  1 247 ? -9.861  -20.633 10.297  1.00 28.27  ? 233 LYS C O   1 
ATOM   6469 C  CB  . LYS C  1 247 ? -8.701  -22.000 8.109   1.00 31.08  ? 233 LYS C CB  1 
ATOM   6470 C  CG  . LYS C  1 247 ? -8.198  -22.891 6.978   1.00 35.11  ? 233 LYS C CG  1 
ATOM   6471 C  CD  . LYS C  1 247 ? -7.821  -22.077 5.744   1.00 39.78  ? 233 LYS C CD  1 
ATOM   6472 C  CE  . LYS C  1 247 ? -6.529  -22.491 5.103   1.00 44.89  ? 233 LYS C CE  1 
ATOM   6473 N  NZ  . LYS C  1 247 ? -6.715  -23.305 3.899   1.00 48.33  ? 233 LYS C NZ  1 
ATOM   6474 N  N   . PRO C  1 248 ? -8.779  -21.932 11.778  1.00 25.17  ? 234 PRO C N   1 
ATOM   6475 C  CA  . PRO C  1 248 ? -9.073  -21.047 12.904  1.00 25.21  ? 234 PRO C CA  1 
ATOM   6476 C  C   . PRO C  1 248 ? -8.402  -19.684 12.768  1.00 25.79  ? 234 PRO C C   1 
ATOM   6477 O  O   . PRO C  1 248 ? -7.410  -19.540 12.056  1.00 27.03  ? 234 PRO C O   1 
ATOM   6478 C  CB  . PRO C  1 248 ? -8.545  -21.835 14.114  1.00 25.67  ? 234 PRO C CB  1 
ATOM   6479 C  CG  . PRO C  1 248 ? -7.426  -22.674 13.537  1.00 26.69  ? 234 PRO C CG  1 
ATOM   6480 C  CD  . PRO C  1 248 ? -7.924  -23.070 12.157  1.00 26.27  ? 234 PRO C CD  1 
ATOM   6481 N  N   . PRO C  1 249 ? -8.936  -18.645 13.448  1.00 23.42  ? 235 PRO C N   1 
ATOM   6482 C  CA  . PRO C  1 249 ? -8.332  -17.310 13.432  1.00 23.74  ? 235 PRO C CA  1 
ATOM   6483 C  C   . PRO C  1 249 ? -7.114  -17.132 14.336  1.00 29.27  ? 235 PRO C C   1 
ATOM   6484 O  O   . PRO C  1 249 ? -6.837  -17.975 15.189  1.00 25.64  ? 235 PRO C O   1 
ATOM   6485 C  CB  . PRO C  1 249 ? -9.508  -16.440 13.907  1.00 23.90  ? 235 PRO C CB  1 
ATOM   6486 C  CG  . PRO C  1 249 ? -10.252 -17.335 14.875  1.00 22.53  ? 235 PRO C CG  1 
ATOM   6487 C  CD  . PRO C  1 249 ? -10.174 -18.710 14.241  1.00 22.91  ? 235 PRO C CD  1 
ATOM   6488 N  N   . GLY C  1 250 ? -6.400  -16.017 14.127  1.00 27.65  ? 236 GLY C N   1 
ATOM   6489 C  CA  . GLY C  1 250 ? -5.346  -15.575 15.027  1.00 31.84  ? 236 GLY C CA  1 
ATOM   6490 C  C   . GLY C  1 250 ? -5.922  -14.904 16.274  1.00 32.54  ? 236 GLY C C   1 
ATOM   6491 O  O   . GLY C  1 250 ? -5.377  -15.052 17.365  1.00 40.00  ? 236 GLY C O   1 
ATOM   6492 N  N   . ILE C  1 251 ? -7.024  -14.159 16.101  1.00 35.24  ? 237 ILE C N   1 
ATOM   6493 C  CA  . ILE C  1 251 ? -7.763  -13.604 17.227  1.00 35.07  ? 237 ILE C CA  1 
ATOM   6494 C  C   . ILE C  1 251 ? -8.622  -14.718 17.828  1.00 35.08  ? 237 ILE C C   1 
ATOM   6495 O  O   . ILE C  1 251 ? -9.690  -15.029 17.301  1.00 29.81  ? 237 ILE C O   1 
ATOM   6496 C  CB  . ILE C  1 251 ? -8.621  -12.390 16.807  1.00 38.13  ? 237 ILE C CB  1 
ATOM   6497 C  CG1 . ILE C  1 251 ? -7.788  -11.274 16.163  1.00 35.80  ? 237 ILE C CG1 1 
ATOM   6498 C  CG2 . ILE C  1 251 ? -9.429  -11.864 17.995  1.00 37.75  ? 237 ILE C CG2 1 
ATOM   6499 C  CD1 . ILE C  1 251 ? -8.592  -10.040 15.789  1.00 35.25  ? 237 ILE C CD1 1 
ATOM   6500 N  N   . ILE C  1 252 ? -8.145  -15.310 18.934  1.00 35.75  ? 238 ILE C N   1 
ATOM   6501 C  CA  . ILE C  1 252 ? -8.773  -16.490 19.514  1.00 32.86  ? 238 ILE C CA  1 
ATOM   6502 C  C   . ILE C  1 252 ? -8.489  -16.544 21.016  1.00 30.60  ? 238 ILE C C   1 
ATOM   6503 O  O   . ILE C  1 252 ? -7.403  -16.175 21.459  1.00 33.76  ? 238 ILE C O   1 
ATOM   6504 C  CB  . ILE C  1 252 ? -8.278  -17.759 18.793  1.00 34.23  ? 238 ILE C CB  1 
ATOM   6505 C  CG1 . ILE C  1 252 ? -9.262  -18.927 18.933  1.00 32.96  ? 238 ILE C CG1 1 
ATOM   6506 C  CG2 . ILE C  1 252 ? -6.872  -18.138 19.261  1.00 33.61  ? 238 ILE C CG2 1 
ATOM   6507 C  CD1 . ILE C  1 252 ? -8.943  -20.107 18.032  1.00 32.87  ? 238 ILE C CD1 1 
ATOM   6508 N  N   . TYR C  1 253 ? -9.479  -17.016 21.789  1.00 24.49  ? 239 TYR C N   1 
ATOM   6509 C  CA  . TYR C  1 253 ? -9.368  -17.134 23.236  1.00 24.35  ? 239 TYR C CA  1 
ATOM   6510 C  C   . TYR C  1 253 ? -9.279  -18.609 23.629  1.00 20.52  ? 239 TYR C C   1 
ATOM   6511 O  O   . TYR C  1 253 ? -8.383  -19.005 24.372  1.00 20.71  ? 239 TYR C O   1 
ATOM   6512 C  CB  . TYR C  1 253 ? -10.557 -16.466 23.940  1.00 21.87  ? 239 TYR C CB  1 
ATOM   6513 C  CG  . TYR C  1 253 ? -10.718 -16.858 25.404  1.00 22.09  ? 239 TYR C CG  1 
ATOM   6514 C  CD1 . TYR C  1 253 ? -9.737  -16.542 26.337  1.00 22.62  ? 239 TYR C CD1 1 
ATOM   6515 C  CD2 . TYR C  1 253 ? -11.852 -17.526 25.857  1.00 21.36  ? 239 TYR C CD2 1 
ATOM   6516 C  CE1 . TYR C  1 253 ? -9.866  -16.897 27.669  1.00 21.68  ? 239 TYR C CE1 1 
ATOM   6517 C  CE2 . TYR C  1 253 ? -11.994 -17.885 27.189  1.00 22.03  ? 239 TYR C CE2 1 
ATOM   6518 C  CZ  . TYR C  1 253 ? -11.000 -17.563 28.096  1.00 21.43  ? 239 TYR C CZ  1 
ATOM   6519 O  OH  . TYR C  1 253 ? -11.120 -17.908 29.408  1.00 22.07  ? 239 TYR C OH  1 
ATOM   6520 N  N   . ASP C  1 254 ? -10.225 -19.407 23.118  1.00 19.42  ? 240 ASP C N   1 
ATOM   6521 C  CA  . ASP C  1 254 ? -10.371 -20.810 23.482  1.00 18.07  ? 240 ASP C CA  1 
ATOM   6522 C  C   . ASP C  1 254 ? -10.391 -21.649 22.204  1.00 17.96  ? 240 ASP C C   1 
ATOM   6523 O  O   . ASP C  1 254 ? -11.441 -21.812 21.588  1.00 18.44  ? 240 ASP C O   1 
ATOM   6524 C  CB  . ASP C  1 254 ? -11.627 -21.012 24.322  1.00 18.71  ? 240 ASP C CB  1 
ATOM   6525 C  CG  . ASP C  1 254 ? -11.993 -22.451 24.663  1.00 18.16  ? 240 ASP C CG  1 
ATOM   6526 O  OD1 . ASP C  1 254 ? -11.161 -23.347 24.412  1.00 17.11  ? 240 ASP C OD1 1 
ATOM   6527 O  OD2 . ASP C  1 254 ? -13.119 -22.666 25.166  1.00 19.02  ? 240 ASP C OD2 1 
ATOM   6528 N  N   . SER C  1 255 ? -9.221  -22.174 21.809  1.00 18.49  ? 241 SER C N   1 
ATOM   6529 C  CA  . SER C  1 255 ? -9.075  -22.858 20.532  1.00 17.97  ? 241 SER C CA  1 
ATOM   6530 C  C   . SER C  1 255 ? -10.004 -24.071 20.451  1.00 17.56  ? 241 SER C C   1 
ATOM   6531 O  O   . SER C  1 255 ? -10.648 -24.288 19.427  1.00 19.23  ? 241 SER C O   1 
ATOM   6532 C  CB  . SER C  1 255 ? -7.631  -23.241 20.266  1.00 18.99  ? 241 SER C CB  1 
ATOM   6533 O  OG  . SER C  1 255 ? -7.087  -24.016 21.325  1.00 18.83  ? 241 SER C OG  1 
ATOM   6534 N  N   . LEU C  1 256 ? -10.063 -24.863 21.528  1.00 17.35  ? 242 LEU C N   1 
ATOM   6535 C  CA  . LEU C  1 256 ? -10.876 -26.071 21.556  1.00 18.58  ? 242 LEU C CA  1 
ATOM   6536 C  C   . LEU C  1 256 ? -12.354 -25.702 21.408  1.00 18.19  ? 242 LEU C C   1 
ATOM   6537 O  O   . LEU C  1 256 ? -13.076 -26.300 20.608  1.00 15.23  ? 242 LEU C O   1 
ATOM   6538 C  CB  . LEU C  1 256 ? -10.617 -26.850 22.847  1.00 18.36  ? 242 LEU C CB  1 
ATOM   6539 C  CG  . LEU C  1 256 ? -9.260  -27.555 22.956  1.00 21.93  ? 242 LEU C CG  1 
ATOM   6540 C  CD1 . LEU C  1 256 ? -9.204  -28.427 24.204  1.00 21.42  ? 242 LEU C CD1 1 
ATOM   6541 C  CD2 . LEU C  1 256 ? -8.962  -28.386 21.716  1.00 23.74  ? 242 LEU C CD2 1 
ATOM   6542 N  N   . GLY C  1 257 ? -12.792 -24.708 22.189  1.00 18.32  ? 243 GLY C N   1 
ATOM   6543 C  CA  . GLY C  1 257 ? -14.166 -24.232 22.140  1.00 17.58  ? 243 GLY C CA  1 
ATOM   6544 C  C   . GLY C  1 257 ? -14.525 -23.669 20.766  1.00 19.67  ? 243 GLY C C   1 
ATOM   6545 O  O   . GLY C  1 257 ? -15.642 -23.858 20.290  1.00 18.69  ? 243 GLY C O   1 
ATOM   6546 N  N   . TYR C  1 258 ? -13.564 -22.972 20.142  1.00 20.83  ? 244 TYR C N   1 
ATOM   6547 C  CA  . TYR C  1 258 ? -13.756 -22.393 18.822  1.00 19.98  ? 244 TYR C CA  1 
ATOM   6548 C  C   . TYR C  1 258 ? -14.072 -23.503 17.821  1.00 19.51  ? 244 TYR C C   1 
ATOM   6549 O  O   . TYR C  1 258 ? -15.005 -23.382 17.031  1.00 18.57  ? 244 TYR C O   1 
ATOM   6550 C  CB  . TYR C  1 258 ? -12.533 -21.603 18.336  1.00 20.89  ? 244 TYR C CB  1 
ATOM   6551 C  CG  . TYR C  1 258 ? -12.645 -21.219 16.866  1.00 20.43  ? 244 TYR C CG  1 
ATOM   6552 C  CD1 . TYR C  1 258 ? -12.310 -22.122 15.865  1.00 21.90  ? 244 TYR C CD1 1 
ATOM   6553 C  CD2 . TYR C  1 258 ? -13.128 -19.974 16.477  1.00 21.33  ? 244 TYR C CD2 1 
ATOM   6554 C  CE1 . TYR C  1 258 ? -12.433 -21.795 14.524  1.00 22.21  ? 244 TYR C CE1 1 
ATOM   6555 C  CE2 . TYR C  1 258 ? -13.252 -19.633 15.139  1.00 22.75  ? 244 TYR C CE2 1 
ATOM   6556 C  CZ  . TYR C  1 258 ? -12.905 -20.547 14.160  1.00 22.36  ? 244 TYR C CZ  1 
ATOM   6557 O  OH  . TYR C  1 258 ? -13.027 -20.222 12.839  1.00 21.01  ? 244 TYR C OH  1 
ATOM   6558 N  N   . MET C  1 259 ? -13.272 -24.577 17.855  1.00 19.88  ? 245 MET C N   1 
ATOM   6559 C  CA  . MET C  1 259 ? -13.431 -25.693 16.934  1.00 20.44  ? 245 MET C CA  1 
ATOM   6560 C  C   . MET C  1 259 ? -14.776 -26.378 17.185  1.00 18.51  ? 245 MET C C   1 
ATOM   6561 O  O   . MET C  1 259 ? -15.507 -26.681 16.245  1.00 19.51  ? 245 MET C O   1 
ATOM   6562 C  CB  . MET C  1 259 ? -12.289 -26.706 17.095  1.00 21.26  ? 245 MET C CB  1 
ATOM   6563 C  CG  . MET C  1 259 ? -10.907 -26.144 16.797  1.00 24.16  ? 245 MET C CG  1 
ATOM   6564 S  SD  . MET C  1 259 ? -10.712 -25.546 15.105  1.00 29.76  ? 245 MET C SD  1 
ATOM   6565 C  CE  . MET C  1 259 ? -10.907 -27.071 14.175  1.00 32.24  ? 245 MET C CE  1 
ATOM   6566 N  N   . ASN C  1 260 ? -15.085 -26.627 18.463  1.00 19.79  ? 246 ASN C N   1 
ATOM   6567 C  CA  . ASN C  1 260 ? -16.354 -27.223 18.864  1.00 20.41  ? 246 ASN C CA  1 
ATOM   6568 C  C   . ASN C  1 260 ? -17.521 -26.432 18.271  1.00 19.50  ? 246 ASN C C   1 
ATOM   6569 O  O   . ASN C  1 260 ? -18.448 -27.015 17.714  1.00 20.76  ? 246 ASN C O   1 
ATOM   6570 C  CB  . ASN C  1 260 ? -16.485 -27.314 20.382  1.00 22.67  ? 246 ASN C CB  1 
ATOM   6571 C  CG  . ASN C  1 260 ? -15.570 -28.350 20.994  1.00 26.85  ? 246 ASN C CG  1 
ATOM   6572 O  OD1 . ASN C  1 260 ? -15.314 -28.314 22.203  1.00 32.75  ? 246 ASN C OD1 1 
ATOM   6573 N  ND2 . ASN C  1 260 ? -15.055 -29.264 20.185  1.00 26.31  ? 246 ASN C ND2 1 
ATOM   6574 N  N   . THR C  1 261 ? -17.472 -25.100 18.399  1.00 21.24  ? 247 THR C N   1 
ATOM   6575 C  CA  . THR C  1 261 ? -18.576 -24.243 17.986  1.00 18.68  ? 247 THR C CA  1 
ATOM   6576 C  C   . THR C  1 261 ? -18.778 -24.331 16.473  1.00 18.87  ? 247 THR C C   1 
ATOM   6577 O  O   . THR C  1 261 ? -19.912 -24.402 16.006  1.00 19.20  ? 247 THR C O   1 
ATOM   6578 C  CB  . THR C  1 261 ? -18.336 -22.801 18.437  1.00 20.45  ? 247 THR C CB  1 
ATOM   6579 O  OG1 . THR C  1 261 ? -18.472 -22.802 19.855  1.00 19.34  ? 247 THR C OG1 1 
ATOM   6580 C  CG2 . THR C  1 261 ? -19.334 -21.824 17.838  1.00 21.17  ? 247 THR C CG2 1 
ATOM   6581 N  N   . VAL C  1 262 ? -17.682 -24.320 15.703  1.00 20.37  ? 248 VAL C N   1 
ATOM   6582 C  CA  . VAL C  1 262 ? -17.787 -24.351 14.253  1.00 21.58  ? 248 VAL C CA  1 
ATOM   6583 C  C   . VAL C  1 262 ? -18.481 -25.650 13.838  1.00 20.72  ? 248 VAL C C   1 
ATOM   6584 O  O   . VAL C  1 262 ? -19.373 -25.639 12.993  1.00 22.75  ? 248 VAL C O   1 
ATOM   6585 C  CB  . VAL C  1 262 ? -16.426 -24.197 13.541  1.00 22.00  ? 248 VAL C CB  1 
ATOM   6586 C  CG1 . VAL C  1 262 ? -16.579 -24.274 12.027  1.00 23.58  ? 248 VAL C CG1 1 
ATOM   6587 C  CG2 . VAL C  1 262 ? -15.706 -22.910 13.932  1.00 19.27  ? 248 VAL C CG2 1 
ATOM   6588 N  N   . GLU C  1 263 ? -18.067 -26.773 14.437  1.00 20.83  ? 249 GLU C N   1 
ATOM   6589 C  CA  . GLU C  1 263 ? -18.619 -28.074 14.091  1.00 22.29  ? 249 GLU C CA  1 
ATOM   6590 C  C   . GLU C  1 263 ? -20.078 -28.155 14.539  1.00 22.39  ? 249 GLU C C   1 
ATOM   6591 O  O   . GLU C  1 263 ? -20.898 -28.799 13.887  1.00 21.85  ? 249 GLU C O   1 
ATOM   6592 C  CB  . GLU C  1 263 ? -17.764 -29.199 14.678  1.00 26.62  ? 249 GLU C CB  1 
ATOM   6593 C  CG  . GLU C  1 263 ? -16.493 -29.463 13.875  1.00 29.17  ? 249 GLU C CG  1 
ATOM   6594 C  CD  . GLU C  1 263 ? -16.761 -29.781 12.413  1.00 36.06  ? 249 GLU C CD  1 
ATOM   6595 O  OE1 . GLU C  1 263 ? -17.366 -30.839 12.134  1.00 48.84  ? 249 GLU C OE1 1 
ATOM   6596 O  OE2 . GLU C  1 263 ? -16.381 -28.959 11.555  1.00 38.06  ? 249 GLU C OE2 1 
ATOM   6597 N  N   . ARG C  1 264 ? -20.398 -27.486 15.651  1.00 20.47  ? 250 ARG C N   1 
ATOM   6598 C  CA  . ARG C  1 264 ? -21.764 -27.450 16.152  1.00 20.10  ? 250 ARG C CA  1 
ATOM   6599 C  C   . ARG C  1 264 ? -22.655 -26.709 15.157  1.00 20.01  ? 250 ARG C C   1 
ATOM   6600 O  O   . ARG C  1 264 ? -23.744 -27.177 14.828  1.00 20.79  ? 250 ARG C O   1 
ATOM   6601 C  CB  . ARG C  1 264 ? -21.816 -26.793 17.534  1.00 19.13  ? 250 ARG C CB  1 
ATOM   6602 C  CG  . ARG C  1 264 ? -23.226 -26.550 18.054  1.00 22.03  ? 250 ARG C CG  1 
ATOM   6603 C  CD  . ARG C  1 264 ? -23.215 -25.877 19.414  1.00 22.51  ? 250 ARG C CD  1 
ATOM   6604 N  NE  . ARG C  1 264 ? -24.569 -25.583 19.891  1.00 25.49  ? 250 ARG C NE  1 
ATOM   6605 C  CZ  . ARG C  1 264 ? -24.845 -24.749 20.884  1.00 27.65  ? 250 ARG C CZ  1 
ATOM   6606 N  NH1 . ARG C  1 264 ? -23.862 -24.131 21.516  1.00 28.90  ? 250 ARG C NH1 1 
ATOM   6607 N  NH2 . ARG C  1 264 ? -26.101 -24.533 21.235  1.00 29.39  ? 250 ARG C NH2 1 
ATOM   6608 N  N   . ILE C  1 265 ? -22.184 -25.546 14.690  1.00 18.37  ? 251 ILE C N   1 
ATOM   6609 C  CA  . ILE C  1 265 ? -22.915 -24.754 13.713  1.00 19.15  ? 251 ILE C CA  1 
ATOM   6610 C  C   . ILE C  1 265 ? -23.150 -25.595 12.459  1.00 21.35  ? 251 ILE C C   1 
ATOM   6611 O  O   . ILE C  1 265 ? -24.241 -25.569 11.894  1.00 21.12  ? 251 ILE C O   1 
ATOM   6612 C  CB  . ILE C  1 265 ? -22.176 -23.439 13.392  1.00 20.92  ? 251 ILE C CB  1 
ATOM   6613 C  CG1 . ILE C  1 265 ? -22.138 -22.498 14.599  1.00 21.63  ? 251 ILE C CG1 1 
ATOM   6614 C  CG2 . ILE C  1 265 ? -22.790 -22.750 12.172  1.00 21.25  ? 251 ILE C CG2 1 
ATOM   6615 C  CD1 . ILE C  1 265 ? -21.166 -21.342 14.451  1.00 22.90  ? 251 ILE C CD1 1 
ATOM   6616 N  N   . ARG C  1 266 ? -22.121 -26.336 12.026  1.00 23.12  ? 252 ARG C N   1 
ATOM   6617 C  CA  . ARG C  1 266 ? -22.227 -27.149 10.824  1.00 24.23  ? 252 ARG C CA  1 
ATOM   6618 C  C   . ARG C  1 266 ? -23.368 -28.153 10.994  1.00 22.51  ? 252 ARG C C   1 
ATOM   6619 O  O   . ARG C  1 266 ? -24.167 -28.346 10.080  1.00 22.75  ? 252 ARG C O   1 
ATOM   6620 C  CB  . ARG C  1 266 ? -20.911 -27.866 10.490  1.00 25.39  ? 252 ARG C CB  1 
ATOM   6621 C  CG  . ARG C  1 266 ? -20.828 -28.365 9.052   1.00 31.29  ? 252 ARG C CG  1 
ATOM   6622 C  CD  . ARG C  1 266 ? -19.599 -29.224 8.766   1.00 28.60  ? 252 ARG C CD  1 
ATOM   6623 N  NE  . ARG C  1 266 ? -18.343 -28.629 9.237   1.00 26.86  ? 252 ARG C NE  1 
ATOM   6624 C  CZ  . ARG C  1 266 ? -17.710 -27.607 8.672   1.00 29.72  ? 252 ARG C CZ  1 
ATOM   6625 N  NH1 . ARG C  1 266 ? -18.178 -27.057 7.566   1.00 28.42  ? 252 ARG C NH1 1 
ATOM   6626 N  NH2 . ARG C  1 266 ? -16.595 -27.146 9.211   1.00 31.16  ? 252 ARG C NH2 1 
ATOM   6627 N  N   . ARG C  1 267 ? -23.437 -28.793 12.168  1.00 21.59  ? 253 ARG C N   1 
ATOM   6628 C  CA  . ARG C  1 267 ? -24.453 -29.802 12.433  1.00 23.84  ? 253 ARG C CA  1 
ATOM   6629 C  C   . ARG C  1 267 ? -25.842 -29.163 12.431  1.00 24.00  ? 253 ARG C C   1 
ATOM   6630 O  O   . ARG C  1 267 ? -26.770 -29.693 11.825  1.00 22.38  ? 253 ARG C O   1 
ATOM   6631 C  CB  . ARG C  1 267 ? -24.219 -30.535 13.761  1.00 26.12  ? 253 ARG C CB  1 
ATOM   6632 C  CG  . ARG C  1 267 ? -25.400 -31.406 14.175  1.00 29.76  ? 253 ARG C CG  1 
ATOM   6633 C  CD  . ARG C  1 267 ? -25.207 -32.146 15.488  1.00 31.84  ? 253 ARG C CD  1 
ATOM   6634 N  NE  . ARG C  1 267 ? -24.741 -31.284 16.579  1.00 34.27  ? 253 ARG C NE  1 
ATOM   6635 C  CZ  . ARG C  1 267 ? -25.480 -30.392 17.227  1.00 35.43  ? 253 ARG C CZ  1 
ATOM   6636 N  NH1 . ARG C  1 267 ? -26.749 -30.208 16.903  1.00 36.75  ? 253 ARG C NH1 1 
ATOM   6637 N  NH2 . ARG C  1 267 ? -24.942 -29.689 18.208  1.00 31.50  ? 253 ARG C NH2 1 
ATOM   6638 N  N   . ILE C  1 268 ? -25.980 -28.022 13.117  1.00 23.10  ? 254 ILE C N   1 
ATOM   6639 C  CA  . ILE C  1 268 ? -27.261 -27.336 13.201  1.00 25.52  ? 254 ILE C CA  1 
ATOM   6640 C  C   . ILE C  1 268 ? -27.714 -26.955 11.793  1.00 23.40  ? 254 ILE C C   1 
ATOM   6641 O  O   . ILE C  1 268 ? -28.881 -27.126 11.446  1.00 27.42  ? 254 ILE C O   1 
ATOM   6642 C  CB  . ILE C  1 268 ? -27.183 -26.106 14.126  1.00 23.89  ? 254 ILE C CB  1 
ATOM   6643 C  CG1 . ILE C  1 268 ? -26.876 -26.504 15.572  1.00 24.78  ? 254 ILE C CG1 1 
ATOM   6644 C  CG2 . ILE C  1 268 ? -28.467 -25.279 14.033  1.00 24.65  ? 254 ILE C CG2 1 
ATOM   6645 C  CD1 . ILE C  1 268 ? -26.518 -25.338 16.476  1.00 25.48  ? 254 ILE C CD1 1 
ATOM   6646 N  N   . ALA C  1 269 ? -26.778 -26.438 10.991  1.00 23.57  ? 255 ALA C N   1 
ATOM   6647 C  CA  . ALA C  1 269 ? -27.071 -26.026 9.628   1.00 24.36  ? 255 ALA C CA  1 
ATOM   6648 C  C   . ALA C  1 269 ? -27.592 -27.218 8.828   1.00 26.18  ? 255 ALA C C   1 
ATOM   6649 O  O   . ALA C  1 269 ? -28.556 -27.090 8.076   1.00 26.01  ? 255 ALA C O   1 
ATOM   6650 C  CB  . ALA C  1 269 ? -25.835 -25.425 8.990   1.00 23.62  ? 255 ALA C CB  1 
ATOM   6651 N  N   . GLN C  1 270 ? -26.941 -28.375 9.003   1.00 27.03  ? 256 GLN C N   1 
ATOM   6652 C  CA  . GLN C  1 270 ? -27.308 -29.586 8.286   1.00 30.97  ? 256 GLN C CA  1 
ATOM   6653 C  C   . GLN C  1 270 ? -28.714 -30.028 8.693   1.00 29.10  ? 256 GLN C C   1 
ATOM   6654 O  O   . GLN C  1 270 ? -29.554 -30.301 7.839   1.00 30.66  ? 256 GLN C O   1 
ATOM   6655 C  CB  . GLN C  1 270 ? -26.319 -30.722 8.554   1.00 31.95  ? 256 GLN C CB  1 
ATOM   6656 C  CG  . GLN C  1 270 ? -26.676 -32.022 7.839   1.00 40.71  ? 256 GLN C CG  1 
ATOM   6657 C  CD  . GLN C  1 270 ? -26.304 -33.261 8.625   1.00 45.91  ? 256 GLN C CD  1 
ATOM   6658 O  OE1 . GLN C  1 270 ? -25.794 -33.185 9.748   1.00 43.28  ? 256 GLN C OE1 1 
ATOM   6659 N  NE2 . GLN C  1 270 ? -26.575 -34.422 8.045   1.00 48.56  ? 256 GLN C NE2 1 
ATOM   6660 N  N   . GLU C  1 271 ? -28.962 -30.090 10.006  1.00 28.77  ? 257 GLU C N   1 
ATOM   6661 C  CA  . GLU C  1 271 ? -30.167 -30.710 10.540  1.00 29.61  ? 257 GLU C CA  1 
ATOM   6662 C  C   . GLU C  1 271 ? -31.383 -29.794 10.383  1.00 33.10  ? 257 GLU C C   1 
ATOM   6663 O  O   . GLU C  1 271 ? -32.513 -30.278 10.369  1.00 34.01  ? 257 GLU C O   1 
ATOM   6664 C  CB  . GLU C  1 271 ? -29.960 -31.113 12.003  1.00 33.02  ? 257 GLU C CB  1 
ATOM   6665 C  CG  . GLU C  1 271 ? -29.025 -32.307 12.182  1.00 31.97  ? 257 GLU C CG  1 
ATOM   6666 C  CD  . GLU C  1 271 ? -28.715 -32.682 13.622  1.00 35.01  ? 257 GLU C CD  1 
ATOM   6667 O  OE1 . GLU C  1 271 ? -29.128 -31.943 14.541  1.00 35.31  ? 257 GLU C OE1 1 
ATOM   6668 O  OE2 . GLU C  1 271 ? -28.057 -33.726 13.824  1.00 33.06  ? 257 GLU C OE2 1 
ATOM   6669 N  N   . THR C  1 272 ? -31.160 -28.476 10.272  1.00 32.00  ? 258 THR C N   1 
ATOM   6670 C  CA  . THR C  1 272 ? -32.263 -27.527 10.170  1.00 30.18  ? 258 THR C CA  1 
ATOM   6671 C  C   . THR C  1 272 ? -32.333 -26.938 8.762   1.00 29.54  ? 258 THR C C   1 
ATOM   6672 O  O   . THR C  1 272 ? -33.197 -26.110 8.484   1.00 30.65  ? 258 THR C O   1 
ATOM   6673 C  CB  . THR C  1 272 ? -32.136 -26.413 11.213  1.00 27.20  ? 258 THR C CB  1 
ATOM   6674 O  OG1 . THR C  1 272 ? -30.973 -25.658 10.887  1.00 25.34  ? 258 THR C OG1 1 
ATOM   6675 C  CG2 . THR C  1 272 ? -32.052 -26.947 12.632  1.00 29.09  ? 258 THR C CG2 1 
ATOM   6676 N  N   A LYS C  1 273 ? -31.410 -27.361 7.891   0.80 30.72  ? 259 LYS C N   1 
ATOM   6677 N  N   B LYS C  1 273 ? -31.422 -27.380 7.886   0.20 28.85  ? 259 LYS C N   1 
ATOM   6678 C  CA  A LYS C  1 273 ? -31.370 -26.885 6.518   0.80 32.89  ? 259 LYS C CA  1 
ATOM   6679 C  CA  B LYS C  1 273 ? -31.349 -26.890 6.517   0.20 28.20  ? 259 LYS C CA  1 
ATOM   6680 C  C   A LYS C  1 273 ? -31.241 -25.363 6.502   0.80 29.24  ? 259 LYS C C   1 
ATOM   6681 C  C   B LYS C  1 273 ? -31.259 -25.365 6.523   0.20 27.34  ? 259 LYS C C   1 
ATOM   6682 O  O   A LYS C  1 273 ? -31.918 -24.689 5.730   0.80 27.69  ? 259 LYS C O   1 
ATOM   6683 O  O   B LYS C  1 273 ? -31.986 -24.693 5.795   0.20 27.42  ? 259 LYS C O   1 
ATOM   6684 C  CB  A LYS C  1 273 ? -32.633 -27.338 5.775   0.80 39.66  ? 259 LYS C CB  1 
ATOM   6685 C  CB  B LYS C  1 273 ? -32.559 -27.375 5.709   0.20 28.39  ? 259 LYS C CB  1 
ATOM   6686 C  CG  A LYS C  1 273 ? -32.891 -28.842 5.768   0.80 46.93  ? 259 LYS C CG  1 
ATOM   6687 C  CG  B LYS C  1 273 ? -32.764 -28.888 5.701   0.20 28.58  ? 259 LYS C CG  1 
ATOM   6688 C  CD  A LYS C  1 273 ? -31.837 -29.636 5.006   0.80 54.37  ? 259 LYS C CD  1 
ATOM   6689 C  CD  B LYS C  1 273 ? -34.021 -29.358 4.978   0.20 28.23  ? 259 LYS C CD  1 
ATOM   6690 C  CE  A LYS C  1 273 ? -32.359 -30.939 4.474   0.80 59.11  ? 259 LYS C CE  1 
ATOM   6691 C  CE  B LYS C  1 273 ? -34.442 -30.741 5.385   0.20 28.55  ? 259 LYS C CE  1 
ATOM   6692 N  NZ  A LYS C  1 273 ? -31.676 -31.326 3.234   0.80 63.19  ? 259 LYS C NZ  1 
ATOM   6693 N  NZ  B LYS C  1 273 ? -35.502 -31.281 4.528   0.20 29.39  ? 259 LYS C NZ  1 
ATOM   6694 N  N   . SER C  1 274 ? -30.351 -24.834 7.350   1.00 26.95  ? 260 SER C N   1 
ATOM   6695 C  CA  . SER C  1 274 ? -30.158 -23.397 7.476   1.00 23.79  ? 260 SER C CA  1 
ATOM   6696 C  C   . SER C  1 274 ? -28.928 -22.947 6.689   1.00 26.52  ? 260 SER C C   1 
ATOM   6697 O  O   . SER C  1 274 ? -27.951 -23.685 6.582   1.00 25.01  ? 260 SER C O   1 
ATOM   6698 C  CB  . SER C  1 274 ? -30.037 -22.992 8.925   1.00 22.53  ? 260 SER C CB  1 
ATOM   6699 O  OG  . SER C  1 274 ? -31.200 -23.350 9.657   1.00 24.32  ? 260 SER C OG  1 
ATOM   6700 N  N   . GLN C  1 275 ? -29.005 -21.730 6.136   1.00 26.01  ? 261 GLN C N   1 
ATOM   6701 C  CA  . GLN C  1 275 ? -27.837 -21.022 5.634   1.00 26.86  ? 261 GLN C CA  1 
ATOM   6702 C  C   . GLN C  1 275 ? -26.993 -20.559 6.818   1.00 24.86  ? 261 GLN C C   1 
ATOM   6703 O  O   . GLN C  1 275 ? -27.536 -20.235 7.872   1.00 21.65  ? 261 GLN C O   1 
ATOM   6704 C  CB  . GLN C  1 275 ? -28.219 -19.756 4.865   1.00 28.85  ? 261 GLN C CB  1 
ATOM   6705 C  CG  . GLN C  1 275 ? -29.051 -19.978 3.609   1.00 34.02  ? 261 GLN C CG  1 
ATOM   6706 C  CD  . GLN C  1 275 ? -29.579 -18.671 3.056   1.00 35.33  ? 261 GLN C CD  1 
ATOM   6707 O  OE1 . GLN C  1 275 ? -28.823 -17.723 2.813   1.00 32.84  ? 261 GLN C OE1 1 
ATOM   6708 N  NE2 . GLN C  1 275 ? -30.891 -18.593 2.889   1.00 35.32  ? 261 GLN C NE2 1 
ATOM   6709 N  N   . VAL C  1 276 ? -25.670 -20.508 6.630   1.00 21.95  ? 262 VAL C N   1 
ATOM   6710 C  CA  . VAL C  1 276 ? -24.775 -19.977 7.644   1.00 23.56  ? 262 VAL C CA  1 
ATOM   6711 C  C   . VAL C  1 276 ? -24.228 -18.640 7.150   1.00 24.31  ? 262 VAL C C   1 
ATOM   6712 O  O   . VAL C  1 276 ? -23.528 -18.588 6.140   1.00 23.09  ? 262 VAL C O   1 
ATOM   6713 C  CB  . VAL C  1 276 ? -23.639 -20.962 7.985   1.00 23.71  ? 262 VAL C CB  1 
ATOM   6714 C  CG1 . VAL C  1 276 ? -22.707 -20.402 9.054   1.00 23.92  ? 262 VAL C CG1 1 
ATOM   6715 C  CG2 . VAL C  1 276 ? -24.180 -22.325 8.403   1.00 23.75  ? 262 VAL C CG2 1 
ATOM   6716 N  N   . TRP C  1 277 ? -24.572 -17.564 7.868   1.00 22.18  ? 263 TRP C N   1 
ATOM   6717 C  CA  . TRP C  1 277 ? -24.093 -16.227 7.554   1.00 22.46  ? 263 TRP C CA  1 
ATOM   6718 C  C   . TRP C  1 277 ? -22.866 -15.911 8.411   1.00 24.97  ? 263 TRP C C   1 
ATOM   6719 O  O   . TRP C  1 277 ? -22.975 -15.726 9.621   1.00 25.66  ? 263 TRP C O   1 
ATOM   6720 C  CB  . TRP C  1 277 ? -25.220 -15.199 7.751   1.00 21.48  ? 263 TRP C CB  1 
ATOM   6721 C  CG  . TRP C  1 277 ? -26.321 -15.301 6.723   1.00 24.03  ? 263 TRP C CG  1 
ATOM   6722 C  CD1 . TRP C  1 277 ? -26.508 -16.318 5.833   1.00 25.28  ? 263 TRP C CD1 1 
ATOM   6723 C  CD2 . TRP C  1 277 ? -27.395 -14.361 6.483   1.00 24.11  ? 263 TRP C CD2 1 
ATOM   6724 N  NE1 . TRP C  1 277 ? -27.607 -16.075 5.053   1.00 25.34  ? 263 TRP C NE1 1 
ATOM   6725 C  CE2 . TRP C  1 277 ? -28.174 -14.886 5.429   1.00 22.44  ? 263 TRP C CE2 1 
ATOM   6726 C  CE3 . TRP C  1 277 ? -27.771 -13.136 7.047   1.00 25.76  ? 263 TRP C CE3 1 
ATOM   6727 C  CZ2 . TRP C  1 277 ? -29.299 -14.229 4.935   1.00 23.74  ? 263 TRP C CZ2 1 
ATOM   6728 C  CZ3 . TRP C  1 277 ? -28.883 -12.487 6.555   1.00 25.00  ? 263 TRP C CZ3 1 
ATOM   6729 C  CH2 . TRP C  1 277 ? -29.633 -13.025 5.513   1.00 23.98  ? 263 TRP C CH2 1 
ATOM   6730 N  N   . PHE C  1 278 ? -21.696 -15.856 7.761   1.00 22.53  ? 264 PHE C N   1 
ATOM   6731 C  CA  . PHE C  1 278 ? -20.425 -15.682 8.446   1.00 22.59  ? 264 PHE C CA  1 
ATOM   6732 C  C   . PHE C  1 278 ? -20.294 -14.240 8.927   1.00 21.66  ? 264 PHE C C   1 
ATOM   6733 O  O   . PHE C  1 278 ? -21.048 -13.367 8.503   1.00 22.97  ? 264 PHE C O   1 
ATOM   6734 C  CB  . PHE C  1 278 ? -19.271 -16.071 7.517   1.00 21.51  ? 264 PHE C CB  1 
ATOM   6735 C  CG  . PHE C  1 278 ? -19.477 -17.410 6.825   1.00 21.75  ? 264 PHE C CG  1 
ATOM   6736 C  CD1 . PHE C  1 278 ? -19.453 -18.597 7.550   1.00 21.99  ? 264 PHE C CD1 1 
ATOM   6737 C  CD2 . PHE C  1 278 ? -19.686 -17.478 5.453   1.00 22.56  ? 264 PHE C CD2 1 
ATOM   6738 C  CE1 . PHE C  1 278 ? -19.640 -19.816 6.918   1.00 23.64  ? 264 PHE C CE1 1 
ATOM   6739 C  CE2 . PHE C  1 278 ? -19.871 -18.700 4.826   1.00 23.72  ? 264 PHE C CE2 1 
ATOM   6740 C  CZ  . PHE C  1 278 ? -19.847 -19.866 5.558   1.00 23.70  ? 264 PHE C CZ  1 
ATOM   6741 N  N   . GLY C  1 279 ? -19.320 -14.015 9.815   1.00 22.81  ? 265 GLY C N   1 
ATOM   6742 C  CA  . GLY C  1 279 ? -19.085 -12.714 10.420  1.00 24.57  ? 265 GLY C CA  1 
ATOM   6743 C  C   . GLY C  1 279 ? -18.759 -11.626 9.396   1.00 26.98  ? 265 GLY C C   1 
ATOM   6744 O  O   . GLY C  1 279 ? -19.348 -10.549 9.441   1.00 25.80  ? 265 GLY C O   1 
ATOM   6745 N  N   A HIS C  1 280 ? -17.845 -11.936 8.463   0.80 28.16  ? 266 HIS C N   1 
ATOM   6746 N  N   B HIS C  1 280 ? -17.784 -11.885 8.517   0.20 26.57  ? 266 HIS C N   1 
ATOM   6747 C  CA  A HIS C  1 280 ? -17.345 -10.948 7.518   0.80 30.59  ? 266 HIS C CA  1 
ATOM   6748 C  CA  B HIS C  1 280 ? -17.427 -10.925 7.483   0.20 26.67  ? 266 HIS C CA  1 
ATOM   6749 C  C   A HIS C  1 280 ? -16.857 -11.596 6.222   0.80 29.27  ? 266 HIS C C   1 
ATOM   6750 C  C   B HIS C  1 280 ? -16.849 -11.646 6.267   0.20 27.23  ? 266 HIS C C   1 
ATOM   6751 O  O   A HIS C  1 280 ? -15.721 -11.365 5.814   0.80 30.31  ? 266 HIS C O   1 
ATOM   6752 O  O   B HIS C  1 280 ? -15.659 -11.536 5.980   0.20 28.23  ? 266 HIS C O   1 
ATOM   6753 C  CB  A HIS C  1 280 ? -16.158 -10.175 8.105   0.80 32.62  ? 266 HIS C CB  1 
ATOM   6754 C  CB  B HIS C  1 280 ? -16.503 -9.823  8.022   0.20 26.04  ? 266 HIS C CB  1 
ATOM   6755 C  CG  A HIS C  1 280 ? -16.354 -9.681  9.500   0.80 38.08  ? 266 HIS C CG  1 
ATOM   6756 C  CG  B HIS C  1 280 ? -15.405 -10.263 8.938   0.20 25.26  ? 266 HIS C CG  1 
ATOM   6757 N  ND1 A HIS C  1 280 ? -15.637 -10.185 10.564  0.80 42.68  ? 266 HIS C ND1 1 
ATOM   6758 N  ND1 B HIS C  1 280 ? -15.343 -9.826  10.244  0.20 25.99  ? 266 HIS C ND1 1 
ATOM   6759 C  CD2 A HIS C  1 280 ? -17.138 -8.718  10.005  0.80 39.06  ? 266 HIS C CD2 1 
ATOM   6760 C  CD2 B HIS C  1 280 ? -14.311 -11.015 8.751   0.20 24.11  ? 266 HIS C CD2 1 
ATOM   6761 C  CE1 A HIS C  1 280 ? -15.999 -9.556  11.673  0.80 33.73  ? 266 HIS C CE1 1 
ATOM   6762 C  CE1 B HIS C  1 280 ? -14.265 -10.332 10.826  0.20 24.77  ? 266 HIS C CE1 1 
ATOM   6763 N  NE2 A HIS C  1 280 ? -16.912 -8.662  11.358  0.80 38.76  ? 266 HIS C NE2 1 
ATOM   6764 N  NE2 B HIS C  1 280 ? -13.625 -11.060 9.939   0.20 23.16  ? 266 HIS C NE2 1 
ATOM   6765 N  N   . ASP C  1 281 ? -17.717 -12.374 5.556   1.00 26.97  ? 267 ASP C N   1 
ATOM   6766 C  CA  . ASP C  1 281 ? -17.359 -12.971 4.277   1.00 27.15  ? 267 ASP C CA  1 
ATOM   6767 C  C   . ASP C  1 281 ? -17.732 -11.998 3.158   1.00 26.06  ? 267 ASP C C   1 
ATOM   6768 O  O   . ASP C  1 281 ? -18.908 -11.717 2.945   1.00 27.57  ? 267 ASP C O   1 
ATOM   6769 C  CB  . ASP C  1 281 ? -17.994 -14.339 4.082   1.00 29.42  ? 267 ASP C CB  1 
ATOM   6770 C  CG  . ASP C  1 281 ? -17.533 -15.080 2.834   1.00 30.81  ? 267 ASP C CG  1 
ATOM   6771 O  OD1 . ASP C  1 281 ? -17.983 -14.710 1.729   1.00 33.22  ? 267 ASP C OD1 1 
ATOM   6772 O  OD2 . ASP C  1 281 ? -16.706 -16.003 2.974   1.00 31.16  ? 267 ASP C OD2 1 
ATOM   6773 N  N   . ALA C  1 282 ? -16.718 -11.498 2.442   1.00 29.28  ? 268 ALA C N   1 
ATOM   6774 C  CA  . ALA C  1 282 ? -16.898 -10.428 1.472   1.00 30.39  ? 268 ALA C CA  1 
ATOM   6775 C  C   . ALA C  1 282 ? -17.789 -10.890 0.319   1.00 29.84  ? 268 ALA C C   1 
ATOM   6776 O  O   . ALA C  1 282 ? -18.625 -10.129 -0.162  1.00 27.72  ? 268 ALA C O   1 
ATOM   6777 C  CB  . ALA C  1 282 ? -15.548 -9.947  0.973   1.00 29.75  ? 268 ALA C CB  1 
ATOM   6778 N  N   . GLU C  1 283 ? -17.597 -12.138 -0.123  1.00 30.01  ? 269 GLU C N   1 
ATOM   6779 C  CA  . GLU C  1 283 ? -18.334 -12.673 -1.258  1.00 32.80  ? 269 GLU C CA  1 
ATOM   6780 C  C   . GLU C  1 283 ? -19.803 -12.859 -0.874  1.00 30.42  ? 269 GLU C C   1 
ATOM   6781 O  O   . GLU C  1 283 ? -20.700 -12.493 -1.630  1.00 27.85  ? 269 GLU C O   1 
ATOM   6782 C  CB  . GLU C  1 283 ? -17.708 -13.983 -1.741  1.00 36.25  ? 269 GLU C CB  1 
ATOM   6783 C  CG  . GLU C  1 283 ? -16.316 -13.825 -2.350  1.00 42.56  ? 269 GLU C CG  1 
ATOM   6784 C  CD  . GLU C  1 283 ? -15.232 -13.332 -1.406  1.00 56.68  ? 269 GLU C CD  1 
ATOM   6785 O  OE1 . GLU C  1 283 ? -15.133 -13.872 -0.280  1.00 48.42  ? 269 GLU C OE1 1 
ATOM   6786 O  OE2 . GLU C  1 283 ? -14.469 -12.422 -1.805  1.00 54.83  ? 269 GLU C OE2 1 
ATOM   6787 N  N   . GLN C  1 284 ? -20.037 -13.434 0.311   1.00 30.71  ? 270 GLN C N   1 
ATOM   6788 C  CA  . GLN C  1 284 ? -21.385 -13.655 0.814   1.00 28.06  ? 270 GLN C CA  1 
ATOM   6789 C  C   . GLN C  1 284 ? -22.081 -12.307 0.998   1.00 26.08  ? 270 GLN C C   1 
ATOM   6790 O  O   . GLN C  1 284 ? -23.250 -12.154 0.648   1.00 26.76  ? 270 GLN C O   1 
ATOM   6791 C  CB  . GLN C  1 284 ? -21.331 -14.456 2.117   1.00 26.25  ? 270 GLN C CB  1 
ATOM   6792 C  CG  . GLN C  1 284 ? -22.677 -15.009 2.579   1.00 25.66  ? 270 GLN C CG  1 
ATOM   6793 C  CD  . GLN C  1 284 ? -22.575 -15.779 3.879   1.00 24.07  ? 270 GLN C CD  1 
ATOM   6794 O  OE1 . GLN C  1 284 ? -22.037 -15.285 4.877   1.00 23.46  ? 270 GLN C OE1 1 
ATOM   6795 N  NE2 . GLN C  1 284 ? -23.080 -17.004 3.880   1.00 22.88  ? 270 GLN C NE2 1 
ATOM   6796 N  N   . PHE C  1 285 ? -21.345 -11.328 1.539   1.00 26.15  ? 271 PHE C N   1 
ATOM   6797 C  CA  . PHE C  1 285 ? -21.898 -10.010 1.812   1.00 28.31  ? 271 PHE C CA  1 
ATOM   6798 C  C   . PHE C  1 285 ? -22.357 -9.362  0.507   1.00 29.09  ? 271 PHE C C   1 
ATOM   6799 O  O   . PHE C  1 285 ? -23.396 -8.703  0.468   1.00 24.92  ? 271 PHE C O   1 
ATOM   6800 C  CB  . PHE C  1 285 ? -20.882 -9.113  2.524   1.00 27.67  ? 271 PHE C CB  1 
ATOM   6801 C  CG  . PHE C  1 285 ? -21.452 -7.757  2.916   1.00 30.79  ? 271 PHE C CG  1 
ATOM   6802 C  CD1 . PHE C  1 285 ? -22.434 -7.661  3.897   1.00 29.22  ? 271 PHE C CD1 1 
ATOM   6803 C  CD2 . PHE C  1 285 ? -21.014 -6.587  2.303   1.00 30.18  ? 271 PHE C CD2 1 
ATOM   6804 C  CE1 . PHE C  1 285 ? -22.961 -6.430  4.253   1.00 30.19  ? 271 PHE C CE1 1 
ATOM   6805 C  CE2 . PHE C  1 285 ? -21.544 -5.359  2.666   1.00 31.22  ? 271 PHE C CE2 1 
ATOM   6806 C  CZ  . PHE C  1 285 ? -22.513 -5.283  3.640   1.00 30.32  ? 271 PHE C CZ  1 
ATOM   6807 N  N   . LYS C  1 286 ? -21.561 -9.542  -0.551  1.00 32.07  ? 272 LYS C N   1 
ATOM   6808 C  CA  . LYS C  1 286 ? -21.896 -9.028  -1.870  1.00 34.85  ? 272 LYS C CA  1 
ATOM   6809 C  C   . LYS C  1 286 ? -23.252 -9.578  -2.311  1.00 30.70  ? 272 LYS C C   1 
ATOM   6810 O  O   . LYS C  1 286 ? -24.070 -8.845  -2.864  1.00 31.84  ? 272 LYS C O   1 
ATOM   6811 C  CB  . LYS C  1 286 ? -20.816 -9.396  -2.896  1.00 40.69  ? 272 LYS C CB  1 
ATOM   6812 C  CG  . LYS C  1 286 ? -19.511 -8.607  -2.815  1.00 48.56  ? 272 LYS C CG  1 
ATOM   6813 C  CD  . LYS C  1 286 ? -18.382 -9.244  -3.621  1.00 60.07  ? 272 LYS C CD  1 
ATOM   6814 C  CE  . LYS C  1 286 ? -17.024 -9.044  -3.011  1.00 60.28  ? 272 LYS C CE  1 
ATOM   6815 N  NZ  . LYS C  1 286 ? -16.141 -10.187 -3.274  1.00 60.36  ? 272 LYS C NZ  1 
ATOM   6816 N  N   . LYS C  1 287 ? -23.478 -10.875 -2.064  1.00 27.70  ? 273 LYS C N   1 
ATOM   6817 C  CA  . LYS C  1 287 ? -24.661 -11.568 -2.555  1.00 31.50  ? 273 LYS C CA  1 
ATOM   6818 C  C   . LYS C  1 287 ? -25.898 -11.163 -1.753  1.00 32.17  ? 273 LYS C C   1 
ATOM   6819 O  O   . LYS C  1 287 ? -27.019 -11.300 -2.236  1.00 36.27  ? 273 LYS C O   1 
ATOM   6820 C  CB  . LYS C  1 287 ? -24.437 -13.085 -2.521  1.00 36.15  ? 273 LYS C CB  1 
ATOM   6821 C  CG  . LYS C  1 287 ? -23.562 -13.618 -3.652  1.00 42.80  ? 273 LYS C CG  1 
ATOM   6822 C  CD  . LYS C  1 287 ? -22.646 -14.772 -3.260  1.00 50.13  ? 273 LYS C CD  1 
ATOM   6823 C  CE  . LYS C  1 287 ? -21.556 -15.013 -4.265  1.00 56.64  ? 273 LYS C CE  1 
ATOM   6824 N  NZ  . LYS C  1 287 ? -20.804 -16.240 -3.984  1.00 63.80  ? 273 LYS C NZ  1 
ATOM   6825 N  N   . PHE C  1 288 ? -25.690 -10.664 -0.530  1.00 27.81  ? 274 PHE C N   1 
ATOM   6826 C  CA  . PHE C  1 288 ? -26.793 -10.287 0.342   1.00 28.53  ? 274 PHE C CA  1 
ATOM   6827 C  C   . PHE C  1 288 ? -27.626 -9.174  -0.289  1.00 26.82  ? 274 PHE C C   1 
ATOM   6828 O  O   . PHE C  1 288 ? -27.088 -8.270  -0.924  1.00 29.80  ? 274 PHE C O   1 
ATOM   6829 C  CB  . PHE C  1 288 ? -26.298 -9.772  1.696   1.00 29.05  ? 274 PHE C CB  1 
ATOM   6830 C  CG  . PHE C  1 288 ? -25.802 -10.829 2.673   1.00 29.47  ? 274 PHE C CG  1 
ATOM   6831 C  CD1 . PHE C  1 288 ? -26.262 -12.140 2.615   1.00 28.19  ? 274 PHE C CD1 1 
ATOM   6832 C  CD2 . PHE C  1 288 ? -24.885 -10.495 3.662   1.00 28.77  ? 274 PHE C CD2 1 
ATOM   6833 C  CE1 . PHE C  1 288 ? -25.807 -13.091 3.517   1.00 30.97  ? 274 PHE C CE1 1 
ATOM   6834 C  CE2 . PHE C  1 288 ? -24.435 -11.448 4.562   1.00 28.75  ? 274 PHE C CE2 1 
ATOM   6835 C  CZ  . PHE C  1 288 ? -24.895 -12.742 4.488   1.00 27.70  ? 274 PHE C CZ  1 
ATOM   6836 N  N   . ARG C  1 289 ? -28.944 -9.243  -0.071  1.00 29.46  ? 275 ARG C N   1 
ATOM   6837 C  CA  . ARG C  1 289 ? -29.839 -8.120  -0.301  1.00 30.65  ? 275 ARG C CA  1 
ATOM   6838 C  C   . ARG C  1 289 ? -29.736 -7.190  0.908   1.00 27.08  ? 275 ARG C C   1 
ATOM   6839 O  O   . ARG C  1 289 ? -30.124 -7.572  2.009   1.00 25.85  ? 275 ARG C O   1 
ATOM   6840 C  CB  . ARG C  1 289 ? -31.258 -8.664  -0.526  1.00 34.34  ? 275 ARG C CB  1 
ATOM   6841 C  CG  . ARG C  1 289 ? -32.217 -7.751  -1.279  1.00 34.58  ? 275 ARG C CG  1 
ATOM   6842 C  CD  . ARG C  1 289 ? -33.385 -8.524  -1.891  1.00 33.38  ? 275 ARG C CD  1 
ATOM   6843 N  NE  . ARG C  1 289 ? -34.067 -9.426  -0.955  1.00 33.41  ? 275 ARG C NE  1 
ATOM   6844 C  CZ  . ARG C  1 289 ? -34.120 -10.749 -1.080  1.00 34.94  ? 275 ARG C CZ  1 
ATOM   6845 N  NH1 . ARG C  1 289 ? -33.434 -11.352 -2.034  1.00 41.79  ? 275 ARG C NH1 1 
ATOM   6846 N  NH2 . ARG C  1 289 ? -34.844 -11.469 -0.239  1.00 35.59  ? 275 ARG C NH2 1 
ATOM   6847 N  N   . LYS C  1 290 ? -29.177 -5.987  0.707   1.00 25.85  ? 276 LYS C N   1 
ATOM   6848 C  CA  . LYS C  1 290 ? -28.952 -5.049  1.797   1.00 26.79  ? 276 LYS C CA  1 
ATOM   6849 C  C   . LYS C  1 290 ? -30.207 -4.204  2.004   1.00 25.77  ? 276 LYS C C   1 
ATOM   6850 O  O   . LYS C  1 290 ? -31.158 -4.298  1.230   1.00 26.91  ? 276 LYS C O   1 
ATOM   6851 C  CB  . LYS C  1 290 ? -27.775 -4.098  1.541   1.00 29.55  ? 276 LYS C CB  1 
ATOM   6852 C  CG  . LYS C  1 290 ? -26.616 -4.645  0.715   1.00 38.46  ? 276 LYS C CG  1 
ATOM   6853 C  CD  . LYS C  1 290 ? -25.732 -5.665  1.421   1.00 35.03  ? 276 LYS C CD  1 
ATOM   6854 C  CE  . LYS C  1 290 ? -24.502 -5.985  0.623   1.00 33.64  ? 276 LYS C CE  1 
ATOM   6855 N  NZ  . LYS C  1 290 ? -24.815 -6.683  -0.628  1.00 33.65  ? 276 LYS C NZ  1 
ATOM   6856 N  N   . SER C  1 291 ? -30.164 -3.348  3.033   1.00 25.21  ? 277 SER C N   1 
ATOM   6857 C  CA  . SER C  1 291 ? -31.321 -2.598  3.496   1.00 24.51  ? 277 SER C CA  1 
ATOM   6858 C  C   . SER C  1 291 ? -31.719 -1.507  2.499   1.00 27.54  ? 277 SER C C   1 
ATOM   6859 O  O   . SER C  1 291 ? -32.793 -0.922  2.626   1.00 26.81  ? 277 SER C O   1 
ATOM   6860 C  CB  . SER C  1 291 ? -31.053 -2.005  4.856   1.00 21.67  ? 277 SER C CB  1 
ATOM   6861 O  OG  . SER C  1 291 ? -29.926 -1.140  4.813   1.00 24.31  ? 277 SER C OG  1 
ATOM   6862 N  N   . THR C  1 292 ? -30.846 -1.221  1.523   1.00 28.31  ? 278 THR C N   1 
ATOM   6863 C  CA  . THR C  1 292 ? -31.135 -0.208  0.516   1.00 27.56  ? 278 THR C CA  1 
ATOM   6864 C  C   . THR C  1 292 ? -31.898 -0.845  -0.646  1.00 27.36  ? 278 THR C C   1 
ATOM   6865 O  O   . THR C  1 292 ? -32.349 -0.143  -1.550  1.00 27.15  ? 278 THR C O   1 
ATOM   6866 C  CB  . THR C  1 292 ? -29.851 0.478   0.035   1.00 28.21  ? 278 THR C CB  1 
ATOM   6867 O  OG1 . THR C  1 292 ? -28.889 -0.546  -0.199  1.00 32.82  ? 278 THR C OG1 1 
ATOM   6868 C  CG2 . THR C  1 292 ? -29.291 1.470   1.039   1.00 27.20  ? 278 THR C CG2 1 
ATOM   6869 N  N   . GLU C  1 293 ? -32.052 -2.175  -0.606  1.00 29.28  ? 279 GLU C N   1 
ATOM   6870 C  CA  . GLU C  1 293 ? -32.646 -2.922  -1.705  1.00 29.48  ? 279 GLU C CA  1 
ATOM   6871 C  C   . GLU C  1 293 ? -33.863 -3.719  -1.232  1.00 29.04  ? 279 GLU C C   1 
ATOM   6872 O  O   . GLU C  1 293 ? -34.777 -3.969  -2.015  1.00 24.31  ? 279 GLU C O   1 
ATOM   6873 C  CB  . GLU C  1 293 ? -31.636 -3.895  -2.315  1.00 35.12  ? 279 GLU C CB  1 
ATOM   6874 C  CG  . GLU C  1 293 ? -30.363 -3.232  -2.837  1.00 40.76  ? 279 GLU C CG  1 
ATOM   6875 C  CD  . GLU C  1 293 ? -29.245 -4.222  -3.117  1.00 49.52  ? 279 GLU C CD  1 
ATOM   6876 O  OE1 . GLU C  1 293 ? -28.867 -4.361  -4.299  1.00 57.16  ? 279 GLU C OE1 1 
ATOM   6877 O  OE2 . GLU C  1 293 ? -28.758 -4.859  -2.155  1.00 41.26  ? 279 GLU C OE2 1 
ATOM   6878 N  N   . GLY C  1 294 ? -33.857 -4.159  0.033   1.00 25.73  ? 280 GLY C N   1 
ATOM   6879 C  CA  . GLY C  1 294 ? -34.967 -4.943  0.554   1.00 23.60  ? 280 GLY C CA  1 
ATOM   6880 C  C   . GLY C  1 294 ? -34.605 -5.738  1.807   1.00 23.31  ? 280 GLY C C   1 
ATOM   6881 O  O   . GLY C  1 294 ? -33.860 -5.260  2.660   1.00 23.62  ? 280 GLY C O   1 
ATOM   6882 N  N   . TYR C  1 295 ? -35.153 -6.958  1.890   1.00 24.48  ? 281 TYR C N   1 
ATOM   6883 C  CA  . TYR C  1 295 ? -35.185 -7.738  3.119   1.00 24.85  ? 281 TYR C CA  1 
ATOM   6884 C  C   . TYR C  1 295 ? -35.452 -9.208  2.799   1.00 26.06  ? 281 TYR C C   1 
ATOM   6885 O  O   . TYR C  1 295 ? -35.714 -9.558  1.650   1.00 25.03  ? 281 TYR C O   1 
ATOM   6886 C  CB  . TYR C  1 295 ? -36.301 -7.182  4.008   1.00 27.74  ? 281 TYR C CB  1 
ATOM   6887 C  CG  . TYR C  1 295 ? -37.531 -6.757  3.214   1.00 29.51  ? 281 TYR C CG  1 
ATOM   6888 C  CD1 . TYR C  1 295 ? -38.377 -7.698  2.634   1.00 29.83  ? 281 TYR C CD1 1 
ATOM   6889 C  CD2 . TYR C  1 295 ? -37.836 -5.413  3.029   1.00 30.62  ? 281 TYR C CD2 1 
ATOM   6890 C  CE1 . TYR C  1 295 ? -39.487 -7.314  1.898   1.00 27.21  ? 281 TYR C CE1 1 
ATOM   6891 C  CE2 . TYR C  1 295 ? -38.947 -5.017  2.301   1.00 31.45  ? 281 TYR C CE2 1 
ATOM   6892 C  CZ  . TYR C  1 295 ? -39.774 -5.971  1.733   1.00 30.04  ? 281 TYR C CZ  1 
ATOM   6893 O  OH  . TYR C  1 295 ? -40.867 -5.586  1.010   1.00 32.10  ? 281 TYR C OH  1 
ATOM   6894 N  N   . TYR C  1 296 ? -35.408 -10.052 3.839   1.00 25.01  ? 282 TYR C N   1 
ATOM   6895 C  CA  . TYR C  1 296 ? -35.744 -11.463 3.719   1.00 25.26  ? 282 TYR C CA  1 
ATOM   6896 C  C   . TYR C  1 296 ? -37.022 -11.740 4.515   1.00 25.25  ? 282 TYR C C   1 
ATOM   6897 O  O   . TYR C  1 296 ? -37.127 -11.349 5.674   1.00 29.92  ? 282 TYR C O   1 
ATOM   6898 C  CB  . TYR C  1 296 ? -34.564 -12.323 4.193   1.00 22.86  ? 282 TYR C CB  1 
ATOM   6899 C  CG  . TYR C  1 296 ? -33.285 -12.182 3.370   1.00 23.12  ? 282 TYR C CG  1 
ATOM   6900 C  CD1 . TYR C  1 296 ? -32.456 -11.075 3.508   1.00 23.56  ? 282 TYR C CD1 1 
ATOM   6901 C  CD2 . TYR C  1 296 ? -32.900 -13.164 2.462   1.00 24.73  ? 282 TYR C CD2 1 
ATOM   6902 C  CE1 . TYR C  1 296 ? -31.295 -10.940 2.761   1.00 24.62  ? 282 TYR C CE1 1 
ATOM   6903 C  CE2 . TYR C  1 296 ? -31.741 -13.042 1.712   1.00 24.30  ? 282 TYR C CE2 1 
ATOM   6904 C  CZ  . TYR C  1 296 ? -30.935 -11.927 1.862   1.00 25.68  ? 282 TYR C CZ  1 
ATOM   6905 O  OH  . TYR C  1 296 ? -29.790 -11.803 1.127   1.00 27.88  ? 282 TYR C OH  1 
ATOM   6906 N  N   A GLU C  1 297 ? -37.981 -12.429 3.884   0.50 25.86  ? 283 GLU C N   1 
ATOM   6907 N  N   B GLU C  1 297 ? -37.990 -12.397 3.861   0.50 26.89  ? 283 GLU C N   1 
ATOM   6908 C  CA  A GLU C  1 297 ? -39.205 -12.848 4.551   0.50 23.56  ? 283 GLU C CA  1 
ATOM   6909 C  CA  B GLU C  1 297 ? -39.251 -12.785 4.478   0.50 25.35  ? 283 GLU C CA  1 
ATOM   6910 C  C   A GLU C  1 297 ? -39.200 -14.380 4.694   0.50 20.32  ? 283 GLU C C   1 
ATOM   6911 C  C   B GLU C  1 297 ? -39.198 -14.273 4.864   0.50 22.78  ? 283 GLU C C   1 
ATOM   6912 O  O   A GLU C  1 297 ? -38.309 -15.008 4.080   0.50 15.43  ? 283 GLU C O   1 
ATOM   6913 O  O   B GLU C  1 297 ? -40.275 -14.814 5.211   0.50 18.19  ? 283 GLU C O   1 
ATOM   6914 C  CB  A GLU C  1 297 ? -40.446 -12.395 3.780   0.50 25.85  ? 283 GLU C CB  1 
ATOM   6915 C  CB  B GLU C  1 297 ? -40.430 -12.537 3.532   0.50 27.99  ? 283 GLU C CB  1 
ATOM   6916 C  CG  A GLU C  1 297 ? -40.528 -10.883 3.586   0.50 27.12  ? 283 GLU C CG  1 
ATOM   6917 C  CG  B GLU C  1 297 ? -41.152 -11.214 3.772   0.50 29.41  ? 283 GLU C CG  1 
ATOM   6918 C  CD  A GLU C  1 297 ? -41.773 -10.413 2.852   0.50 27.51  ? 283 GLU C CD  1 
ATOM   6919 C  CD  B GLU C  1 297 ? -42.156 -10.842 2.694   0.50 30.03  ? 283 GLU C CD  1 
ATOM   6920 O  OE1 A GLU C  1 297 ? -42.601 -11.271 2.477   0.50 30.14  ? 283 GLU C OE1 1 
ATOM   6921 O  OE1 B GLU C  1 297 ? -42.170 -11.518 1.643   0.50 33.48  ? 283 GLU C OE1 1 
ATOM   6922 O  OE2 A GLU C  1 297 ? -41.915 -9.187  2.661   0.50 28.86  ? 283 GLU C OE2 1 
ATOM   6923 O  OE2 B GLU C  1 297 ? -42.931 -9.885  2.908   0.50 29.14  ? 283 GLU C OE2 1 
HETATM 6924 CO CO  . CO  D  2 .   ? 32.309  25.400  50.947  0.75 24.21  ? 301 CO  A CO  1 
HETATM 6925 S  S   . SO4 E  3 .   ? 37.434  25.088  29.886  0.80 40.72  ? 302 SO4 A S   1 
HETATM 6926 O  O1  . SO4 E  3 .   ? 38.430  24.316  29.195  0.80 40.23  ? 302 SO4 A O1  1 
HETATM 6927 O  O2  . SO4 E  3 .   ? 36.613  25.781  28.929  0.80 36.46  ? 302 SO4 A O2  1 
HETATM 6928 O  O3  . SO4 E  3 .   ? 36.612  24.211  30.679  0.80 38.86  ? 302 SO4 A O3  1 
HETATM 6929 O  O4  . SO4 E  3 .   ? 38.083  26.045  30.743  0.80 39.97  ? 302 SO4 A O4  1 
HETATM 6930 S  S   . SO4 F  3 .   ? 38.128  5.993   40.137  0.70 28.74  ? 303 SO4 A S   1 
HETATM 6931 O  O1  . SO4 F  3 .   ? 39.423  6.227   39.554  0.70 27.79  ? 303 SO4 A O1  1 
HETATM 6932 O  O2  . SO4 F  3 .   ? 37.108  6.265   39.161  0.70 31.19  ? 303 SO4 A O2  1 
HETATM 6933 O  O3  . SO4 F  3 .   ? 38.033  4.622   40.556  0.70 29.19  ? 303 SO4 A O3  1 
HETATM 6934 O  O4  . SO4 F  3 .   ? 37.948  6.855   41.273  0.70 23.94  ? 303 SO4 A O4  1 
HETATM 6935 S  S   . SO4 G  3 .   ? 23.686  35.243  36.031  1.00 69.14  ? 304 SO4 A S   1 
HETATM 6936 O  O1  . SO4 G  3 .   ? 24.340  34.604  34.921  1.00 61.77  ? 304 SO4 A O1  1 
HETATM 6937 O  O2  . SO4 G  3 .   ? 22.993  36.416  35.570  1.00 79.23  ? 304 SO4 A O2  1 
HETATM 6938 O  O3  . SO4 G  3 .   ? 22.744  34.330  36.621  1.00 73.29  ? 304 SO4 A O3  1 
HETATM 6939 O  O4  . SO4 G  3 .   ? 24.667  35.620  37.014  1.00 65.94  ? 304 SO4 A O4  1 
HETATM 6940 C  C1  . GOL H  4 .   ? 38.500  24.502  53.058  0.70 33.18  ? 305 GOL A C1  1 
HETATM 6941 O  O1  . GOL H  4 .   ? 38.463  25.825  52.530  0.70 32.76  ? 305 GOL A O1  1 
HETATM 6942 C  C2  . GOL H  4 .   ? 39.752  23.763  52.634  0.70 31.49  ? 305 GOL A C2  1 
HETATM 6943 O  O2  . GOL H  4 .   ? 39.386  22.533  52.013  0.70 27.23  ? 305 GOL A O2  1 
HETATM 6944 C  C3  . GOL H  4 .   ? 40.707  23.493  53.779  0.70 30.70  ? 305 GOL A C3  1 
HETATM 6945 O  O3  . GOL H  4 .   ? 41.994  24.059  53.540  0.70 32.98  ? 305 GOL A O3  1 
HETATM 6946 CO CO  . CO  I  2 .   ? 55.505  -2.290  21.365  0.75 22.80  ? 301 CO  B CO  1 
HETATM 6947 S  S   . SO4 J  3 .   ? 42.625  15.167  23.498  0.90 37.22  ? 302 SO4 B S   1 
HETATM 6948 O  O1  . SO4 J  3 .   ? 43.148  14.610  22.282  0.90 33.10  ? 302 SO4 B O1  1 
HETATM 6949 O  O2  . SO4 J  3 .   ? 41.189  15.095  23.485  0.90 34.41  ? 302 SO4 B O2  1 
HETATM 6950 O  O3  . SO4 J  3 .   ? 43.035  16.540  23.611  0.90 36.35  ? 302 SO4 B O3  1 
HETATM 6951 O  O4  . SO4 J  3 .   ? 43.133  14.422  24.621  0.90 39.13  ? 302 SO4 B O4  1 
HETATM 6952 S  S   . SO4 K  3 .   ? 60.773  17.891  11.641  1.00 42.94  ? 303 SO4 B S   1 
HETATM 6953 O  O1  . SO4 K  3 .   ? 61.821  18.255  10.723  1.00 48.37  ? 303 SO4 B O1  1 
HETATM 6954 O  O2  . SO4 K  3 .   ? 59.496  18.026  10.990  1.00 45.40  ? 303 SO4 B O2  1 
HETATM 6955 O  O3  . SO4 K  3 .   ? 60.820  18.761  12.785  1.00 45.75  ? 303 SO4 B O3  1 
HETATM 6956 O  O4  . SO4 K  3 .   ? 60.958  16.528  12.060  1.00 28.10  ? 303 SO4 B O4  1 
HETATM 6957 S  S   . SO4 L  3 .   ? 51.504  22.855  17.942  1.00 36.04  ? 304 SO4 B S   1 
HETATM 6958 O  O1  . SO4 L  3 .   ? 50.635  22.144  17.041  1.00 39.65  ? 304 SO4 B O1  1 
HETATM 6959 O  O2  . SO4 L  3 .   ? 52.742  23.164  17.270  1.00 35.09  ? 304 SO4 B O2  1 
HETATM 6960 O  O3  . SO4 L  3 .   ? 51.773  22.033  19.095  1.00 31.30  ? 304 SO4 B O3  1 
HETATM 6961 O  O4  . SO4 L  3 .   ? 50.867  24.077  18.357  1.00 38.56  ? 304 SO4 B O4  1 
HETATM 6962 S  S   . SO4 M  3 .   ? 41.657  12.711  30.491  0.70 36.31  ? 305 SO4 B S   1 
HETATM 6963 O  O1  . SO4 M  3 .   ? 42.300  12.644  29.206  0.70 36.87  ? 305 SO4 B O1  1 
HETATM 6964 O  O2  . SO4 M  3 .   ? 40.242  12.888  30.309  0.70 34.34  ? 305 SO4 B O2  1 
HETATM 6965 O  O3  . SO4 M  3 .   ? 41.898  11.489  31.211  0.70 33.12  ? 305 SO4 B O3  1 
HETATM 6966 O  O4  . SO4 M  3 .   ? 42.187  13.823  31.236  0.70 26.01  ? 305 SO4 B O4  1 
HETATM 6967 S  S   . SO4 N  3 .   ? 77.574  -7.743  -4.605  0.70 48.86  ? 306 SO4 B S   1 
HETATM 6968 O  O1  . SO4 N  3 .   ? 77.276  -7.922  -5.999  0.70 43.94  ? 306 SO4 B O1  1 
HETATM 6969 O  O2  . SO4 N  3 .   ? 78.981  -7.949  -4.385  0.70 50.12  ? 306 SO4 B O2  1 
HETATM 6970 O  O3  . SO4 N  3 .   ? 76.823  -8.692  -3.828  0.70 57.42  ? 306 SO4 B O3  1 
HETATM 6971 O  O4  . SO4 N  3 .   ? 77.217  -6.408  -4.206  0.70 45.71  ? 306 SO4 B O4  1 
HETATM 6972 S  S   . SO4 O  3 .   ? 49.820  -23.043 36.606  1.00 56.91  ? 307 SO4 B S   1 
HETATM 6973 O  O1  . SO4 O  3 .   ? 50.799  -24.015 36.201  1.00 48.06  ? 307 SO4 B O1  1 
HETATM 6974 O  O2  . SO4 O  3 .   ? 49.024  -22.662 35.470  1.00 51.65  ? 307 SO4 B O2  1 
HETATM 6975 O  O3  . SO4 O  3 .   ? 48.968  -23.611 37.616  1.00 51.54  ? 307 SO4 B O3  1 
HETATM 6976 O  O4  . SO4 O  3 .   ? 50.489  -21.885 37.137  1.00 55.81  ? 307 SO4 B O4  1 
HETATM 6977 S  S   . SO4 P  3 .   ? 35.692  -1.073  20.826  1.00 57.04  ? 308 SO4 B S   1 
HETATM 6978 O  O1  . SO4 P  3 .   ? 35.929  -1.619  19.517  1.00 63.41  ? 308 SO4 B O1  1 
HETATM 6979 O  O2  . SO4 P  3 .   ? 35.735  0.364   20.758  1.00 53.19  ? 308 SO4 B O2  1 
HETATM 6980 O  O3  . SO4 P  3 .   ? 36.706  -1.545  21.731  1.00 58.12  ? 308 SO4 B O3  1 
HETATM 6981 O  O4  . SO4 P  3 .   ? 34.398  -1.493  21.294  1.00 72.27  ? 308 SO4 B O4  1 
HETATM 6982 C  C1  . GOL Q  4 .   ? 61.132  20.461  31.005  1.00 49.18  ? 309 GOL B C1  1 
HETATM 6983 O  O1  . GOL Q  4 .   ? 62.301  21.000  30.393  1.00 54.54  ? 309 GOL B O1  1 
HETATM 6984 C  C2  . GOL Q  4 .   ? 60.715  19.157  30.358  1.00 43.89  ? 309 GOL B C2  1 
HETATM 6985 O  O2  . GOL Q  4 .   ? 61.296  18.064  31.066  1.00 50.87  ? 309 GOL B O2  1 
HETATM 6986 C  C3  . GOL Q  4 .   ? 59.213  18.976  30.289  1.00 46.61  ? 309 GOL B C3  1 
HETATM 6987 O  O3  . GOL Q  4 .   ? 58.860  17.713  29.733  1.00 44.32  ? 309 GOL B O3  1 
HETATM 6988 C  C1  . GOL R  4 .   ? 62.411  1.122   26.343  0.70 37.97  ? 310 GOL B C1  1 
HETATM 6989 O  O1  . GOL R  4 .   ? 62.253  1.474   27.715  0.70 36.73  ? 310 GOL B O1  1 
HETATM 6990 C  C2  . GOL R  4 .   ? 61.090  1.138   25.603  0.70 39.11  ? 310 GOL B C2  1 
HETATM 6991 O  O2  . GOL R  4 .   ? 60.809  2.460   25.146  0.70 31.66  ? 310 GOL B O2  1 
HETATM 6992 C  C3  . GOL R  4 .   ? 59.933  0.621   26.434  0.70 41.61  ? 310 GOL B C3  1 
HETATM 6993 O  O3  . GOL R  4 .   ? 59.234  -0.428  25.768  0.70 36.72  ? 310 GOL B O3  1 
HETATM 6994 C  C1  . GOL S  4 .   ? 45.195  -17.268 12.233  1.00 54.34  ? 311 GOL B C1  1 
HETATM 6995 O  O1  . GOL S  4 .   ? 43.902  -17.749 12.590  1.00 50.96  ? 311 GOL B O1  1 
HETATM 6996 C  C2  . GOL S  4 .   ? 46.233  -18.372 12.266  1.00 59.33  ? 311 GOL B C2  1 
HETATM 6997 O  O2  . GOL S  4 .   ? 47.194  -18.161 11.232  1.00 55.13  ? 311 GOL B O2  1 
HETATM 6998 C  C3  . GOL S  4 .   ? 46.940  -18.487 13.600  1.00 59.54  ? 311 GOL B C3  1 
HETATM 6999 O  O3  . GOL S  4 .   ? 48.193  -19.156 13.476  1.00 59.54  ? 311 GOL B O3  1 
HETATM 7000 C  C   . ACT T  5 .   ? 59.124  11.552  29.317  0.70 42.97  ? 312 ACT B C   1 
HETATM 7001 O  O   . ACT T  5 .   ? 58.717  12.574  28.728  0.70 43.44  ? 312 ACT B O   1 
HETATM 7002 O  OXT . ACT T  5 .   ? 60.177  10.951  29.022  0.70 42.70  ? 312 ACT B OXT 1 
HETATM 7003 C  CH3 . ACT T  5 .   ? 58.283  11.003  30.470  0.70 38.77  ? 312 ACT B CH3 1 
HETATM 7004 CO CO  . CO  U  2 .   ? -14.521 -10.479 17.187  0.78 23.88  ? 301 CO  C CO  1 
HETATM 7005 S  S   . SO4 V  3 .   ? -4.278  -11.255 36.606  0.70 27.89  ? 302 SO4 C S   1 
HETATM 7006 O  O1  . SO4 V  3 .   ? -3.866  -10.239 35.675  0.70 29.59  ? 302 SO4 C O1  1 
HETATM 7007 O  O2  . SO4 V  3 .   ? -4.612  -12.456 35.888  0.70 27.92  ? 302 SO4 C O2  1 
HETATM 7008 O  O3  . SO4 V  3 .   ? -3.202  -11.528 37.521  0.70 29.77  ? 302 SO4 C O3  1 
HETATM 7009 O  O4  . SO4 V  3 .   ? -5.430  -10.797 37.337  0.70 20.07  ? 302 SO4 C O4  1 
HETATM 7010 S  S   . SO4 W  3 .   ? -27.756 -27.718 19.889  0.70 29.81  ? 303 SO4 C S   1 
HETATM 7011 O  O1  . SO4 W  3 .   ? -26.330 -27.861 19.759  0.70 27.84  ? 303 SO4 C O1  1 
HETATM 7012 O  O2  . SO4 W  3 .   ? -28.399 -28.188 18.691  0.70 26.39  ? 303 SO4 C O2  1 
HETATM 7013 O  O3  . SO4 W  3 .   ? -28.211 -28.488 21.013  0.70 27.70  ? 303 SO4 C O3  1 
HETATM 7014 O  O4  . SO4 W  3 .   ? -28.084 -26.335 20.092  0.70 27.28  ? 303 SO4 C O4  1 
HETATM 7015 C  C   . ACT X  5 .   ? -31.337 -25.017 17.467  1.00 55.51  ? 304 ACT C C   1 
HETATM 7016 O  O   . ACT X  5 .   ? -31.468 -24.202 16.531  1.00 54.15  ? 304 ACT C O   1 
HETATM 7017 O  OXT . ACT X  5 .   ? -30.240 -25.485 17.836  1.00 53.88  ? 304 ACT C OXT 1 
HETATM 7018 C  CH3 . ACT X  5 .   ? -32.598 -25.469 18.208  1.00 48.35  ? 304 ACT C CH3 1 
HETATM 7019 O  O   . HOH Y  6 .   ? 25.199  17.225  58.125  0.60 87.21  ? 401 HOH A O   1 
HETATM 7020 O  O   . HOH Y  6 .   ? 38.269  45.218  52.442  1.00 41.84  ? 402 HOH A O   1 
HETATM 7021 O  O   . HOH Y  6 .   ? 42.315  19.920  39.278  1.00 21.94  ? 403 HOH A O   1 
HETATM 7022 O  O   . HOH Y  6 .   ? 36.811  19.630  59.762  1.00 35.12  ? 404 HOH A O   1 
HETATM 7023 O  O   . HOH Y  6 .   ? 12.902  23.573  40.351  1.00 34.15  ? 405 HOH A O   1 
HETATM 7024 O  O   . HOH Y  6 .   ? 20.049  24.450  24.390  1.00 45.67  ? 406 HOH A O   1 
HETATM 7025 O  O   . HOH Y  6 .   ? 48.353  22.284  50.888  1.00 37.68  ? 407 HOH A O   1 
HETATM 7026 O  O   . HOH Y  6 .   ? 31.453  42.565  43.639  1.00 45.79  ? 408 HOH A O   1 
HETATM 7027 O  O   . HOH Y  6 .   ? 28.939  35.900  33.518  1.00 37.38  ? 409 HOH A O   1 
HETATM 7028 O  O   . HOH Y  6 .   ? 33.275  33.119  46.771  1.00 28.40  ? 410 HOH A O   1 
HETATM 7029 O  O   . HOH Y  6 .   ? 22.695  29.344  26.599  1.00 37.13  ? 411 HOH A O   1 
HETATM 7030 O  O   . HOH Y  6 .   ? 31.966  27.182  52.271  1.00 34.78  ? 412 HOH A O   1 
HETATM 7031 O  O   . HOH Y  6 .   ? 30.429  25.332  52.496  1.00 32.61  ? 413 HOH A O   1 
HETATM 7032 O  O   . HOH Y  6 .   ? 28.269  40.317  39.891  1.00 32.72  ? 414 HOH A O   1 
HETATM 7033 O  O   . HOH Y  6 .   ? 33.652  30.686  48.048  1.00 24.60  ? 415 HOH A O   1 
HETATM 7034 O  O   . HOH Y  6 .   ? 33.110  20.356  62.639  1.00 51.31  ? 416 HOH A O   1 
HETATM 7035 O  O   . HOH Y  6 .   ? 29.202  16.586  55.104  1.00 23.94  ? 417 HOH A O   1 
HETATM 7036 O  O   . HOH Y  6 .   ? 42.058  9.827   43.163  1.00 22.51  ? 418 HOH A O   1 
HETATM 7037 O  O   . HOH Y  6 .   ? 25.654  26.703  27.175  1.00 32.74  ? 419 HOH A O   1 
HETATM 7038 O  O   . HOH Y  6 .   ? 28.022  31.436  70.305  1.00 31.82  ? 420 HOH A O   1 
HETATM 7039 O  O   . HOH Y  6 .   ? 31.061  14.625  63.563  1.00 30.62  ? 421 HOH A O   1 
HETATM 7040 O  O   . HOH Y  6 .   ? 24.654  23.384  45.681  0.60 25.07  ? 422 HOH A O   1 
HETATM 7041 O  O   . HOH Y  6 .   ? 19.144  5.681   50.825  1.00 37.72  ? 423 HOH A O   1 
HETATM 7042 O  O   . HOH Y  6 .   ? 26.342  17.607  57.041  1.00 24.97  ? 424 HOH A O   1 
HETATM 7043 O  O   . HOH Y  6 .   ? 42.984  20.312  43.317  1.00 25.52  ? 425 HOH A O   1 
HETATM 7044 O  O   . HOH Y  6 .   ? 23.487  35.983  52.302  1.00 45.25  ? 426 HOH A O   1 
HETATM 7045 O  O   . HOH Y  6 .   ? 40.312  30.209  55.404  1.00 35.58  ? 427 HOH A O   1 
HETATM 7046 O  O   . HOH Y  6 .   ? 39.376  41.297  42.905  1.00 48.26  ? 428 HOH A O   1 
HETATM 7047 O  O   . HOH Y  6 .   ? 26.138  5.105   38.522  1.00 42.84  ? 429 HOH A O   1 
HETATM 7048 O  O   . HOH Y  6 .   ? 20.594  29.909  30.156  1.00 37.38  ? 430 HOH A O   1 
HETATM 7049 O  O   . HOH Y  6 .   ? 26.958  0.919   47.622  1.00 49.73  ? 431 HOH A O   1 
HETATM 7050 O  O   . HOH Y  6 .   ? 30.444  32.248  61.735  1.00 28.47  ? 432 HOH A O   1 
HETATM 7051 O  O   . HOH Y  6 .   ? 37.666  38.803  56.368  1.00 41.01  ? 433 HOH A O   1 
HETATM 7052 O  O   . HOH Y  6 .   ? 16.817  31.628  34.850  1.00 46.35  ? 434 HOH A O   1 
HETATM 7053 O  O   . HOH Y  6 .   ? 34.994  38.543  62.009  1.00 39.70  ? 435 HOH A O   1 
HETATM 7054 O  O   . HOH Y  6 .   ? 42.324  48.742  59.168  1.00 28.71  ? 436 HOH A O   1 
HETATM 7055 O  O   . HOH Y  6 .   ? 44.967  8.085   63.007  1.00 50.92  ? 437 HOH A O   1 
HETATM 7056 O  O   . HOH Y  6 .   ? 24.123  26.769  67.043  1.00 41.63  ? 438 HOH A O   1 
HETATM 7057 O  O   . HOH Y  6 .   ? 28.202  8.375   61.240  1.00 37.31  ? 439 HOH A O   1 
HETATM 7058 O  O   . HOH Y  6 .   ? 46.080  14.705  42.999  1.00 18.67  ? 440 HOH A O   1 
HETATM 7059 O  O   . HOH Y  6 .   ? 37.772  35.659  32.210  1.00 36.54  ? 441 HOH A O   1 
HETATM 7060 O  O   . HOH Y  6 .   ? 26.295  11.657  54.289  1.00 30.20  ? 442 HOH A O   1 
HETATM 7061 O  O   . HOH Y  6 .   ? 23.773  24.381  68.444  1.00 48.75  ? 443 HOH A O   1 
HETATM 7062 O  O   . HOH Y  6 .   ? 10.565  18.740  46.074  1.00 35.75  ? 444 HOH A O   1 
HETATM 7063 O  O   . HOH Y  6 .   ? 45.539  26.324  41.484  1.00 32.18  ? 445 HOH A O   1 
HETATM 7064 O  O   . HOH Y  6 .   ? 12.225  22.984  47.006  1.00 31.07  ? 446 HOH A O   1 
HETATM 7065 O  O   . HOH Y  6 .   ? 33.723  35.895  26.327  1.00 45.29  ? 447 HOH A O   1 
HETATM 7066 O  O   . HOH Y  6 .   ? 36.586  29.986  42.629  1.00 21.22  ? 448 HOH A O   1 
HETATM 7067 O  O   . HOH Y  6 .   ? 46.913  23.619  43.924  1.00 37.75  ? 449 HOH A O   1 
HETATM 7068 O  O   . HOH Y  6 .   ? 27.377  4.816   46.037  1.00 36.57  ? 450 HOH A O   1 
HETATM 7069 O  O   . HOH Y  6 .   ? 26.034  16.048  59.822  1.00 31.93  ? 451 HOH A O   1 
HETATM 7070 O  O   . HOH Y  6 .   ? 29.106  27.303  52.324  1.00 42.79  ? 452 HOH A O   1 
HETATM 7071 O  O   . HOH Y  6 .   ? 31.634  18.691  63.447  1.00 40.07  ? 453 HOH A O   1 
HETATM 7072 O  O   . HOH Y  6 .   ? 45.403  15.297  47.308  1.00 22.36  ? 454 HOH A O   1 
HETATM 7073 O  O   . HOH Y  6 .   ? 19.841  18.999  61.897  1.00 34.63  ? 455 HOH A O   1 
HETATM 7074 O  O   . HOH Y  6 .   ? 36.723  34.681  25.715  1.00 31.41  ? 456 HOH A O   1 
HETATM 7075 O  O   . HOH Y  6 .   ? 44.178  10.293  64.475  1.00 38.48  ? 457 HOH A O   1 
HETATM 7076 O  O   . HOH Y  6 .   ? 41.813  26.409  40.305  1.00 24.06  ? 458 HOH A O   1 
HETATM 7077 O  O   . HOH Y  6 .   ? 45.264  34.070  40.154  1.00 35.55  ? 459 HOH A O   1 
HETATM 7078 O  O   . HOH Y  6 .   ? 33.303  35.449  48.039  1.00 25.09  ? 460 HOH A O   1 
HETATM 7079 O  O   . HOH Y  6 .   ? 16.714  33.866  49.529  1.00 48.83  ? 461 HOH A O   1 
HETATM 7080 O  O   . HOH Y  6 .   ? 13.662  10.032  48.994  1.00 40.53  ? 462 HOH A O   1 
HETATM 7081 O  O   . HOH Y  6 .   ? 20.945  29.465  61.146  1.00 32.63  ? 463 HOH A O   1 
HETATM 7082 O  O   . HOH Y  6 .   ? 31.843  17.208  55.705  1.00 24.61  ? 464 HOH A O   1 
HETATM 7083 O  O   . HOH Y  6 .   ? 22.713  31.311  44.240  1.00 35.75  ? 465 HOH A O   1 
HETATM 7084 O  O   . HOH Y  6 .   ? 21.961  5.918   44.692  1.00 37.21  ? 466 HOH A O   1 
HETATM 7085 O  O   . HOH Y  6 .   ? 38.694  41.037  40.176  1.00 43.74  ? 467 HOH A O   1 
HETATM 7086 O  O   . HOH Y  6 .   ? 7.903   19.555  40.484  1.00 44.39  ? 468 HOH A O   1 
HETATM 7087 O  O   . HOH Y  6 .   ? 25.675  26.400  42.088  1.00 30.08  ? 469 HOH A O   1 
HETATM 7088 O  O   . HOH Y  6 .   ? 30.912  39.229  34.433  1.00 39.13  ? 470 HOH A O   1 
HETATM 7089 O  O   . HOH Y  6 .   ? 29.459  40.657  35.928  1.00 41.38  ? 471 HOH A O   1 
HETATM 7090 O  O   . HOH Y  6 .   ? 36.676  40.148  49.810  1.00 39.82  ? 472 HOH A O   1 
HETATM 7091 O  O   . HOH Y  6 .   ? 37.271  27.893  44.060  1.00 18.30  ? 473 HOH A O   1 
HETATM 7092 O  O   . HOH Y  6 .   ? 45.983  27.484  52.491  1.00 30.86  ? 474 HOH A O   1 
HETATM 7093 O  O   . HOH Y  6 .   ? 37.789  13.405  31.831  1.00 30.05  ? 475 HOH A O   1 
HETATM 7094 O  O   . HOH Y  6 .   ? 8.210   23.438  51.361  1.00 50.35  ? 476 HOH A O   1 
HETATM 7095 O  O   . HOH Y  6 .   ? 10.375  24.384  47.928  1.00 39.13  ? 477 HOH A O   1 
HETATM 7096 O  O   . HOH Y  6 .   ? 26.599  44.580  69.548  1.00 46.56  ? 478 HOH A O   1 
HETATM 7097 O  O   . HOH Y  6 .   ? 38.586  26.076  42.201  1.00 19.48  ? 479 HOH A O   1 
HETATM 7098 O  O   . HOH Y  6 .   ? 32.557  24.266  42.660  1.00 22.81  ? 480 HOH A O   1 
HETATM 7099 O  O   . HOH Y  6 .   ? 48.090  28.394  43.450  1.00 24.11  ? 481 HOH A O   1 
HETATM 7100 O  O   . HOH Y  6 .   ? 37.553  23.390  58.252  1.00 44.85  ? 482 HOH A O   1 
HETATM 7101 O  O   . HOH Y  6 .   ? 18.955  17.882  53.778  1.00 33.08  ? 483 HOH A O   1 
HETATM 7102 O  O   . HOH Y  6 .   ? 34.953  17.788  44.747  1.00 20.47  ? 484 HOH A O   1 
HETATM 7103 O  O   . HOH Y  6 .   ? 41.504  31.897  34.665  1.00 28.64  ? 485 HOH A O   1 
HETATM 7104 O  O   . HOH Y  6 .   ? 44.330  20.627  46.698  1.00 39.71  ? 486 HOH A O   1 
HETATM 7105 O  O   . HOH Y  6 .   ? 24.351  40.565  62.401  1.00 35.96  ? 487 HOH A O   1 
HETATM 7106 O  O   . HOH Y  6 .   ? 41.466  21.877  37.430  1.00 20.62  ? 488 HOH A O   1 
HETATM 7107 O  O   . HOH Y  6 .   ? 7.881   16.453  52.409  1.00 42.35  ? 489 HOH A O   1 
HETATM 7108 O  O   . HOH Y  6 .   ? 45.581  21.433  53.506  1.00 38.00  ? 490 HOH A O   1 
HETATM 7109 O  O   . HOH Y  6 .   ? 44.509  16.932  49.243  1.00 36.48  ? 491 HOH A O   1 
HETATM 7110 O  O   . HOH Y  6 .   ? 20.991  18.258  29.043  1.00 45.54  ? 492 HOH A O   1 
HETATM 7111 O  O   . HOH Y  6 .   ? 35.944  43.051  57.974  1.00 36.33  ? 493 HOH A O   1 
HETATM 7112 O  O   . HOH Y  6 .   ? 23.797  25.683  48.165  1.00 45.27  ? 494 HOH A O   1 
HETATM 7113 O  O   . HOH Y  6 .   ? 21.795  32.338  29.097  1.00 48.94  ? 495 HOH A O   1 
HETATM 7114 O  O   . HOH Y  6 .   ? 20.773  4.335   40.122  1.00 52.17  ? 496 HOH A O   1 
HETATM 7115 O  O   . HOH Y  6 .   ? 50.449  17.604  45.452  1.00 21.26  ? 497 HOH A O   1 
HETATM 7116 O  O   . HOH Y  6 .   ? 23.366  10.480  63.051  1.00 44.80  ? 498 HOH A O   1 
HETATM 7117 O  O   . HOH Y  6 .   ? 38.452  20.015  29.797  1.00 36.18  ? 499 HOH A O   1 
HETATM 7118 O  O   . HOH Y  6 .   ? 46.357  14.285  37.377  1.00 36.49  ? 500 HOH A O   1 
HETATM 7119 O  O   . HOH Y  6 .   ? 39.542  26.409  37.238  1.00 22.69  ? 501 HOH A O   1 
HETATM 7120 O  O   . HOH Y  6 .   ? 42.149  24.597  37.706  1.00 40.01  ? 502 HOH A O   1 
HETATM 7121 O  O   . HOH Y  6 .   ? 20.773  19.896  25.059  1.00 48.38  ? 503 HOH A O   1 
HETATM 7122 O  O   . HOH Y  6 .   ? 36.656  36.627  29.622  1.00 39.94  ? 504 HOH A O   1 
HETATM 7123 O  O   . HOH Y  6 .   ? 35.731  19.933  27.152  1.00 52.77  ? 505 HOH A O   1 
HETATM 7124 O  O   . HOH Y  6 .   ? 24.081  21.597  48.986  1.00 28.86  ? 506 HOH A O   1 
HETATM 7125 O  O   . HOH Y  6 .   ? 26.723  16.593  25.011  1.00 39.67  ? 507 HOH A O   1 
HETATM 7126 O  O   . HOH Y  6 .   ? 26.515  4.252   35.911  1.00 48.33  ? 508 HOH A O   1 
HETATM 7127 O  O   . HOH Y  6 .   ? 27.971  17.364  69.004  1.00 47.89  ? 509 HOH A O   1 
HETATM 7128 O  O   . HOH Y  6 .   ? 11.929  13.456  57.859  1.00 47.99  ? 510 HOH A O   1 
HETATM 7129 O  O   . HOH Y  6 .   ? 39.550  20.320  33.279  1.00 45.99  ? 511 HOH A O   1 
HETATM 7130 O  O   . HOH Y  6 .   ? 33.976  27.781  26.783  1.00 47.10  ? 512 HOH A O   1 
HETATM 7131 O  O   . HOH Y  6 .   ? 20.204  16.490  68.261  1.00 43.77  ? 513 HOH A O   1 
HETATM 7132 O  O   . HOH Y  6 .   ? 44.041  24.144  40.632  1.00 30.73  ? 514 HOH A O   1 
HETATM 7133 O  O   . HOH Y  6 .   ? 43.659  17.279  55.486  1.00 54.06  ? 515 HOH A O   1 
HETATM 7134 O  O   . HOH Y  6 .   ? 18.165  14.034  53.794  0.70 30.69  ? 516 HOH A O   1 
HETATM 7135 O  O   . HOH Y  6 .   ? 23.393  35.963  49.950  1.00 40.49  ? 517 HOH A O   1 
HETATM 7136 O  O   . HOH Y  6 .   ? 25.321  25.244  46.232  0.60 45.49  ? 518 HOH A O   1 
HETATM 7137 O  O   . HOH Y  6 .   ? 7.801   24.356  35.385  1.00 45.40  ? 519 HOH A O   1 
HETATM 7138 O  O   . HOH Y  6 .   ? 44.304  27.563  38.975  1.00 27.01  ? 520 HOH A O   1 
HETATM 7139 O  O   . HOH Y  6 .   ? 46.633  16.021  62.822  1.00 37.64  ? 521 HOH A O   1 
HETATM 7140 O  O   . HOH Y  6 .   ? 7.543   20.490  56.439  1.00 45.49  ? 522 HOH A O   1 
HETATM 7141 O  O   . HOH Y  6 .   ? 37.693  4.604   62.186  1.00 50.79  ? 523 HOH A O   1 
HETATM 7142 O  O   . HOH Y  6 .   ? 30.099  48.984  62.254  1.00 39.31  ? 524 HOH A O   1 
HETATM 7143 O  O   . HOH Y  6 .   ? 44.168  21.660  41.213  1.00 27.68  ? 525 HOH A O   1 
HETATM 7144 O  O   . HOH Y  6 .   ? 47.931  17.932  54.956  1.00 42.37  ? 526 HOH A O   1 
HETATM 7145 O  O   . HOH Y  6 .   ? 24.202  24.367  43.093  0.60 51.50  ? 527 HOH A O   1 
HETATM 7146 O  O   . HOH Y  6 .   ? 44.519  17.992  50.454  1.00 56.13  ? 528 HOH A O   1 
HETATM 7147 O  O   . HOH Y  6 .   ? 41.271  54.670  67.496  1.00 44.90  ? 529 HOH A O   1 
HETATM 7148 O  O   . HOH Y  6 .   ? 45.376  16.344  51.308  1.00 23.90  ? 530 HOH A O   1 
HETATM 7149 O  O   . HOH Y  6 .   ? 47.984  16.533  48.000  1.00 25.36  ? 531 HOH A O   1 
HETATM 7150 O  O   . HOH Y  6 .   ? 41.544  28.055  36.283  1.00 30.20  ? 532 HOH A O   1 
HETATM 7151 O  O   . HOH Y  6 .   ? 44.015  17.563  57.136  1.00 52.44  ? 533 HOH A O   1 
HETATM 7152 O  O   . HOH Y  6 .   ? 27.478  9.729   26.920  1.00 66.06  ? 534 HOH A O   1 
HETATM 7153 O  O   . HOH Y  6 .   ? 14.453  35.480  54.554  1.00 55.20  ? 535 HOH A O   1 
HETATM 7154 O  O   . HOH Y  6 .   ? 48.188  19.147  48.008  1.00 31.47  ? 536 HOH A O   1 
HETATM 7155 O  O   . HOH Y  6 .   ? 35.571  12.039  30.569  1.00 31.82  ? 537 HOH A O   1 
HETATM 7156 O  O   . HOH Y  6 .   ? 48.680  25.124  52.401  1.00 39.20  ? 538 HOH A O   1 
HETATM 7157 O  O   . HOH Y  6 .   ? 40.066  43.826  50.543  1.00 45.27  ? 539 HOH A O   1 
HETATM 7158 O  O   . HOH Z  6 .   ? 43.974  15.301  30.851  1.00 52.48  ? 401 HOH B O   1 
HETATM 7159 O  O   . HOH Z  6 .   ? 41.627  1.640   -2.625  1.00 41.51  ? 402 HOH B O   1 
HETATM 7160 O  O   . HOH Z  6 .   ? 34.798  9.870   15.482  1.00 27.64  ? 403 HOH B O   1 
HETATM 7161 O  O   . HOH Z  6 .   ? 54.346  13.705  24.186  1.00 21.62  ? 404 HOH B O   1 
HETATM 7162 O  O   . HOH Z  6 .   ? 31.749  9.843   9.665   1.00 38.48  ? 405 HOH B O   1 
HETATM 7163 O  O   . HOH Z  6 .   ? 35.858  12.042  7.167   1.00 45.55  ? 406 HOH B O   1 
HETATM 7164 O  O   . HOH Z  6 .   ? 53.179  22.043  15.117  1.00 35.00  ? 407 HOH B O   1 
HETATM 7165 O  O   . HOH Z  6 .   ? 45.404  -8.980  4.780   1.00 25.15  ? 408 HOH B O   1 
HETATM 7166 O  O   . HOH Z  6 .   ? 64.056  -4.602  3.835   1.00 39.94  ? 409 HOH B O   1 
HETATM 7167 O  O   . HOH Z  6 .   ? 57.165  -15.144 32.904  1.00 37.35  ? 410 HOH B O   1 
HETATM 7168 O  O   . HOH Z  6 .   ? 67.147  -3.096  21.284  1.00 38.81  ? 411 HOH B O   1 
HETATM 7169 O  O   . HOH Z  6 .   ? 44.175  10.482  30.986  1.00 27.26  ? 412 HOH B O   1 
HETATM 7170 O  O   . HOH Z  6 .   ? 40.666  -4.377  5.128   1.00 21.87  ? 413 HOH B O   1 
HETATM 7171 O  O   . HOH Z  6 .   ? 54.057  10.678  30.911  1.00 27.98  ? 414 HOH B O   1 
HETATM 7172 O  O   . HOH Z  6 .   ? 44.710  13.344  28.938  1.00 42.59  ? 415 HOH B O   1 
HETATM 7173 O  O   . HOH Z  6 .   ? 36.008  12.349  4.424   1.00 39.59  ? 416 HOH B O   1 
HETATM 7174 O  O   . HOH Z  6 .   ? 31.506  9.797   13.920  1.00 41.61  ? 417 HOH B O   1 
HETATM 7175 O  O   . HOH Z  6 .   ? 31.719  4.151   16.491  1.00 47.64  ? 418 HOH B O   1 
HETATM 7176 O  O   . HOH Z  6 .   ? 39.853  10.341  32.199  1.00 36.62  ? 419 HOH B O   1 
HETATM 7177 O  O   . HOH Z  6 .   ? 49.389  -1.684  14.235  1.00 37.14  ? 420 HOH B O   1 
HETATM 7178 O  O   . HOH Z  6 .   ? 38.654  8.290   30.536  1.00 35.33  ? 421 HOH B O   1 
HETATM 7179 O  O   . HOH Z  6 .   ? 61.320  -1.618  24.874  1.00 38.22  ? 422 HOH B O   1 
HETATM 7180 O  O   . HOH Z  6 .   ? 37.858  -4.085  27.511  1.00 28.52  ? 423 HOH B O   1 
HETATM 7181 O  O   . HOH Z  6 .   ? 49.216  -19.003 40.673  1.00 39.42  ? 424 HOH B O   1 
HETATM 7182 O  O   . HOH Z  6 .   ? 57.354  11.119  25.219  1.00 22.51  ? 425 HOH B O   1 
HETATM 7183 O  O   . HOH Z  6 .   ? 57.535  -5.490  33.533  1.00 40.80  ? 426 HOH B O   1 
HETATM 7184 O  O   . HOH Z  6 .   ? 48.685  -2.680  26.891  1.00 19.69  ? 427 HOH B O   1 
HETATM 7185 O  O   . HOH Z  6 .   ? 59.733  12.562  0.686   1.00 52.12  ? 428 HOH B O   1 
HETATM 7186 O  O   . HOH Z  6 .   ? 43.003  -13.562 15.522  1.00 42.18  ? 429 HOH B O   1 
HETATM 7187 O  O   . HOH Z  6 .   ? 48.401  -4.850  28.843  1.00 21.70  ? 430 HOH B O   1 
HETATM 7188 O  O   . HOH Z  6 .   ? 48.498  -9.571  39.351  1.00 40.42  ? 431 HOH B O   1 
HETATM 7189 O  O   . HOH Z  6 .   ? 62.900  -1.140  7.990   1.00 24.48  ? 432 HOH B O   1 
HETATM 7190 O  O   . HOH Z  6 .   ? 61.128  8.535   3.288   1.00 21.83  ? 433 HOH B O   1 
HETATM 7191 O  O   . HOH Z  6 .   ? 51.133  -2.207  25.770  1.00 20.52  ? 434 HOH B O   1 
HETATM 7192 O  O   . HOH Z  6 .   ? 43.879  -12.695 7.506   1.00 44.79  ? 435 HOH B O   1 
HETATM 7193 O  O   . HOH Z  6 .   ? 51.540  9.604   28.047  1.00 24.32  ? 436 HOH B O   1 
HETATM 7194 O  O   . HOH Z  6 .   ? 62.741  15.980  17.279  1.00 26.93  ? 437 HOH B O   1 
HETATM 7195 O  O   . HOH Z  6 .   ? 36.274  -12.943 17.246  1.00 43.96  ? 438 HOH B O   1 
HETATM 7196 O  O   . HOH Z  6 .   ? 51.380  25.598  20.461  1.00 41.19  ? 439 HOH B O   1 
HETATM 7197 O  O   . HOH Z  6 .   ? 43.260  -5.600  17.853  1.00 25.76  ? 440 HOH B O   1 
HETATM 7198 O  O   . HOH Z  6 .   ? 32.998  1.680   -3.315  1.00 29.65  ? 441 HOH B O   1 
HETATM 7199 O  O   . HOH Z  6 .   ? 54.224  24.978  18.523  1.00 26.98  ? 442 HOH B O   1 
HETATM 7200 O  O   . HOH Z  6 .   ? 54.629  -3.538  -2.691  1.00 41.49  ? 443 HOH B O   1 
HETATM 7201 O  O   . HOH Z  6 .   ? 57.087  5.959   0.128   1.00 24.43  ? 444 HOH B O   1 
HETATM 7202 O  O   . HOH Z  6 .   ? 34.130  12.746  28.790  1.00 26.76  ? 445 HOH B O   1 
HETATM 7203 O  O   . HOH Z  6 .   ? 60.633  0.300   -1.557  1.00 43.43  ? 446 HOH B O   1 
HETATM 7204 O  O   . HOH Z  6 .   ? 57.440  -12.515 -1.440  1.00 52.09  ? 447 HOH B O   1 
HETATM 7205 O  O   . HOH Z  6 .   ? 62.578  19.158  19.700  1.00 49.36  ? 448 HOH B O   1 
HETATM 7206 O  O   . HOH Z  6 .   ? 34.864  6.729   2.414   1.00 34.55  ? 449 HOH B O   1 
HETATM 7207 O  O   . HOH Z  6 .   ? 49.706  8.620   -2.361  1.00 26.07  ? 450 HOH B O   1 
HETATM 7208 O  O   . HOH Z  6 .   ? 31.665  7.468   14.912  1.00 26.38  ? 451 HOH B O   1 
HETATM 7209 O  O   . HOH Z  6 .   ? 61.826  -2.488  13.537  1.00 23.54  ? 452 HOH B O   1 
HETATM 7210 O  O   . HOH Z  6 .   ? 40.001  15.890  1.269   1.00 36.58  ? 453 HOH B O   1 
HETATM 7211 O  O   . HOH Z  6 .   ? 43.885  -11.339 4.850   1.00 30.62  ? 454 HOH B O   1 
HETATM 7212 O  O   . HOH Z  6 .   ? 48.037  7.191   -4.259  1.00 50.41  ? 455 HOH B O   1 
HETATM 7213 O  O   . HOH Z  6 .   ? 61.648  -6.051  12.134  1.00 23.15  ? 456 HOH B O   1 
HETATM 7214 O  O   . HOH Z  6 .   ? 64.204  7.651   31.215  1.00 43.88  ? 457 HOH B O   1 
HETATM 7215 O  O   . HOH Z  6 .   ? 45.341  -10.072 27.003  1.00 41.42  ? 458 HOH B O   1 
HETATM 7216 O  O   . HOH Z  6 .   ? 35.415  5.064   -1.262  1.00 31.44  ? 459 HOH B O   1 
HETATM 7217 O  O   . HOH Z  6 .   ? 46.405  -7.306  0.447   1.00 27.54  ? 460 HOH B O   1 
HETATM 7218 O  O   . HOH Z  6 .   ? 55.950  6.120   35.400  0.50 23.28  ? 461 HOH B O   1 
HETATM 7219 O  O   . HOH Z  6 .   ? 34.321  -2.637  12.872  1.00 47.21  ? 462 HOH B O   1 
HETATM 7220 O  O   . HOH Z  6 .   ? 69.985  -6.323  14.230  1.00 29.72  ? 463 HOH B O   1 
HETATM 7221 O  O   . HOH Z  6 .   ? 58.748  -14.119 25.634  1.00 29.67  ? 464 HOH B O   1 
HETATM 7222 O  O   . HOH Z  6 .   ? 35.597  2.673   24.826  1.00 32.30  ? 465 HOH B O   1 
HETATM 7223 O  O   . HOH Z  6 .   ? 32.632  0.249   4.296   1.00 27.75  ? 466 HOH B O   1 
HETATM 7224 O  O   . HOH Z  6 .   ? 51.161  -22.709 31.206  1.00 48.35  ? 467 HOH B O   1 
HETATM 7225 O  O   . HOH Z  6 .   ? 60.378  19.490  21.747  1.00 34.58  ? 468 HOH B O   1 
HETATM 7226 O  O   . HOH Z  6 .   ? 59.823  16.708  8.355   1.00 45.06  ? 469 HOH B O   1 
HETATM 7227 O  O   . HOH Z  6 .   ? 35.609  1.448   28.219  1.00 31.11  ? 470 HOH B O   1 
HETATM 7228 O  O   . HOH Z  6 .   ? 67.194  -7.514  19.331  1.00 41.05  ? 471 HOH B O   1 
HETATM 7229 O  O   . HOH Z  6 .   ? 36.578  16.289  27.987  1.00 33.30  ? 472 HOH B O   1 
HETATM 7230 O  O   . HOH Z  6 .   ? 59.922  9.466   26.718  1.00 40.83  ? 473 HOH B O   1 
HETATM 7231 O  O   . HOH Z  6 .   ? 45.668  8.205   -2.810  1.00 43.95  ? 474 HOH B O   1 
HETATM 7232 O  O   . HOH Z  6 .   ? 55.559  -17.241 16.490  1.00 31.25  ? 475 HOH B O   1 
HETATM 7233 O  O   . HOH Z  6 .   ? 33.065  3.623   14.004  1.00 25.60  ? 476 HOH B O   1 
HETATM 7234 O  O   . HOH Z  6 .   ? 70.545  -3.567  7.886   1.00 35.90  ? 477 HOH B O   1 
HETATM 7235 O  O   . HOH Z  6 .   ? 52.871  -3.332  12.541  1.00 24.12  ? 478 HOH B O   1 
HETATM 7236 O  O   . HOH Z  6 .   ? 59.551  -3.436  30.706  1.00 32.78  ? 479 HOH B O   1 
HETATM 7237 O  O   . HOH Z  6 .   ? 64.028  12.280  23.894  1.00 20.05  ? 480 HOH B O   1 
HETATM 7238 O  O   . HOH Z  6 .   ? 61.605  15.773  23.661  1.00 18.74  ? 481 HOH B O   1 
HETATM 7239 O  O   . HOH Z  6 .   ? 55.304  9.787   34.268  1.00 23.03  ? 482 HOH B O   1 
HETATM 7240 O  O   . HOH Z  6 .   ? 66.524  12.512  5.392   1.00 49.62  ? 483 HOH B O   1 
HETATM 7241 O  O   . HOH Z  6 .   ? 41.822  0.776   35.853  1.00 40.96  ? 484 HOH B O   1 
HETATM 7242 O  O   . HOH Z  6 .   ? 35.396  -1.061  28.094  1.00 38.97  ? 485 HOH B O   1 
HETATM 7243 O  O   . HOH Z  6 .   ? 62.986  -1.913  15.933  1.00 23.86  ? 486 HOH B O   1 
HETATM 7244 O  O   . HOH Z  6 .   ? 48.518  7.666   35.896  1.00 42.01  ? 487 HOH B O   1 
HETATM 7245 O  O   . HOH Z  6 .   ? 61.339  2.841   32.959  1.00 29.08  ? 488 HOH B O   1 
HETATM 7246 O  O   . HOH Z  6 .   ? 48.907  3.448   26.939  1.00 18.12  ? 489 HOH B O   1 
HETATM 7247 O  O   . HOH Z  6 .   ? 61.453  -13.493 8.685   1.00 41.26  ? 490 HOH B O   1 
HETATM 7248 O  O   . HOH Z  6 .   ? 54.694  -25.494 37.786  1.00 39.71  ? 491 HOH B O   1 
HETATM 7249 O  O   . HOH Z  6 .   ? 65.164  5.148   28.571  1.00 40.75  ? 492 HOH B O   1 
HETATM 7250 O  O   . HOH Z  6 .   ? 64.339  -7.132  11.286  1.00 27.96  ? 493 HOH B O   1 
HETATM 7251 O  O   . HOH Z  6 .   ? 50.810  12.276  26.904  1.00 41.52  ? 494 HOH B O   1 
HETATM 7252 O  O   . HOH Z  6 .   ? 38.801  10.408  6.292   1.00 36.87  ? 495 HOH B O   1 
HETATM 7253 O  O   . HOH Z  6 .   ? 57.424  -6.330  3.354   1.00 35.99  ? 496 HOH B O   1 
HETATM 7254 O  O   . HOH Z  6 .   ? 55.629  -4.285  22.298  1.00 31.51  ? 497 HOH B O   1 
HETATM 7255 O  O   . HOH Z  6 .   ? 41.209  -11.656 22.008  1.00 41.95  ? 498 HOH B O   1 
HETATM 7256 O  O   . HOH Z  6 .   ? 56.162  -3.975  20.145  1.00 29.09  ? 499 HOH B O   1 
HETATM 7257 O  O   . HOH Z  6 .   ? 50.243  4.058   20.125  1.00 21.84  ? 500 HOH B O   1 
HETATM 7258 O  O   . HOH Z  6 .   ? 52.343  -14.000 36.702  1.00 32.92  ? 501 HOH B O   1 
HETATM 7259 O  O   . HOH Z  6 .   ? 61.991  9.728   27.192  1.00 51.97  ? 502 HOH B O   1 
HETATM 7260 O  O   . HOH Z  6 .   ? 51.535  6.734   25.725  1.00 20.35  ? 503 HOH B O   1 
HETATM 7261 O  O   . HOH Z  6 .   ? 64.590  13.547  7.400   1.00 29.65  ? 504 HOH B O   1 
HETATM 7262 O  O   . HOH Z  6 .   ? 45.805  -0.176  16.489  1.00 25.06  ? 505 HOH B O   1 
HETATM 7263 O  O   . HOH Z  6 .   ? 56.369  7.099   17.650  1.00 18.66  ? 506 HOH B O   1 
HETATM 7264 O  O   . HOH Z  6 .   ? 44.347  -0.708  37.053  1.00 47.69  ? 507 HOH B O   1 
HETATM 7265 O  O   . HOH Z  6 .   ? 55.886  -7.774  6.813   1.00 27.54  ? 508 HOH B O   1 
HETATM 7266 O  O   . HOH Z  6 .   ? 54.819  -9.521  34.541  1.00 31.91  ? 509 HOH B O   1 
HETATM 7267 O  O   . HOH Z  6 .   ? 57.140  -18.091 9.207   1.00 41.10  ? 510 HOH B O   1 
HETATM 7268 O  O   . HOH Z  6 .   ? 47.862  -18.317 22.185  1.00 37.59  ? 511 HOH B O   1 
HETATM 7269 O  O   . HOH Z  6 .   ? 54.135  16.908  4.442   1.00 42.21  ? 512 HOH B O   1 
HETATM 7270 O  O   . HOH Z  6 .   ? 50.557  19.642  15.547  1.00 25.24  ? 513 HOH B O   1 
HETATM 7271 O  O   . HOH Z  6 .   ? 51.645  13.492  24.600  1.00 23.79  ? 514 HOH B O   1 
HETATM 7272 O  O   . HOH Z  6 .   ? 48.193  10.491  26.260  1.00 24.28  ? 515 HOH B O   1 
HETATM 7273 O  O   . HOH Z  6 .   ? 34.848  4.648   25.881  1.00 33.77  ? 516 HOH B O   1 
HETATM 7274 O  O   . HOH Z  6 .   ? 64.020  9.308   24.593  1.00 29.13  ? 517 HOH B O   1 
HETATM 7275 O  O   . HOH Z  6 .   ? 52.556  19.075  10.190  1.00 51.74  ? 518 HOH B O   1 
HETATM 7276 O  O   . HOH Z  6 .   ? 51.223  -12.240 -2.240  1.00 35.87  ? 519 HOH B O   1 
HETATM 7277 O  O   . HOH Z  6 .   ? 48.902  16.232  22.060  1.00 41.35  ? 520 HOH B O   1 
HETATM 7278 O  O   . HOH Z  6 .   ? 59.839  -21.974 44.323  1.00 38.49  ? 521 HOH B O   1 
HETATM 7279 O  O   . HOH Z  6 .   ? 54.246  -5.597  20.343  1.00 46.80  ? 522 HOH B O   1 
HETATM 7280 O  O   . HOH Z  6 .   ? 59.300  -1.204  33.388  1.00 46.32  ? 523 HOH B O   1 
HETATM 7281 O  O   . HOH Z  6 .   ? 51.269  3.920   26.074  1.00 16.21  ? 524 HOH B O   1 
HETATM 7282 O  O   . HOH Z  6 .   ? 48.506  -6.255  34.782  1.00 32.21  ? 525 HOH B O   1 
HETATM 7283 O  O   . HOH Z  6 .   ? 55.341  -18.580 2.127   1.00 48.86  ? 526 HOH B O   1 
HETATM 7284 O  O   . HOH Z  6 .   ? 41.110  -2.496  -3.666  1.00 46.65  ? 527 HOH B O   1 
HETATM 7285 O  O   . HOH Z  6 .   ? 43.531  18.192  5.071   1.00 53.54  ? 528 HOH B O   1 
HETATM 7286 O  O   . HOH Z  6 .   ? 28.835  7.859   -5.662  1.00 40.26  ? 529 HOH B O   1 
HETATM 7287 O  O   . HOH Z  6 .   ? 64.198  -3.196  24.393  1.00 43.49  ? 530 HOH B O   1 
HETATM 7288 O  O   . HOH Z  6 .   ? 63.685  15.029  28.923  1.00 20.21  ? 531 HOH B O   1 
HETATM 7289 O  O   . HOH Z  6 .   ? 53.760  17.419  8.874   1.00 44.79  ? 532 HOH B O   1 
HETATM 7290 O  O   . HOH Z  6 .   ? 51.853  -17.031 0.922   1.00 44.54  ? 533 HOH B O   1 
HETATM 7291 O  O   . HOH Z  6 .   ? 71.104  -13.256 21.188  1.00 38.45  ? 534 HOH B O   1 
HETATM 7292 O  O   . HOH Z  6 .   ? 43.087  -2.882  -5.061  1.00 40.16  ? 535 HOH B O   1 
HETATM 7293 O  O   . HOH Z  6 .   ? 53.792  11.741  28.378  1.00 28.95  ? 536 HOH B O   1 
HETATM 7294 O  O   . HOH Z  6 .   ? 41.069  -13.649 10.668  1.00 39.26  ? 537 HOH B O   1 
HETATM 7295 O  O   . HOH Z  6 .   ? 50.493  -5.158  14.983  1.00 46.08  ? 538 HOH B O   1 
HETATM 7296 O  O   . HOH Z  6 .   ? 45.770  18.196  20.512  1.00 33.69  ? 539 HOH B O   1 
HETATM 7297 O  O   . HOH Z  6 .   ? 33.691  15.878  0.187   1.00 45.08  ? 540 HOH B O   1 
HETATM 7298 O  O   . HOH Z  6 .   ? 44.611  -11.360 22.157  1.00 40.46  ? 541 HOH B O   1 
HETATM 7299 O  O   . HOH Z  6 .   ? 59.734  -5.481  2.407   1.00 39.28  ? 542 HOH B O   1 
HETATM 7300 O  O   . HOH Z  6 .   ? 48.794  2.943   -5.963  1.00 40.22  ? 543 HOH B O   1 
HETATM 7301 O  O   . HOH Z  6 .   ? 58.097  20.011  22.751  1.00 36.71  ? 544 HOH B O   1 
HETATM 7302 O  O   . HOH Z  6 .   ? 55.631  12.563  26.606  1.00 23.79  ? 545 HOH B O   1 
HETATM 7303 O  O   . HOH Z  6 .   ? 66.412  9.101   24.874  1.00 30.41  ? 546 HOH B O   1 
HETATM 7304 O  O   . HOH Z  6 .   ? 63.577  11.066  28.439  1.00 38.30  ? 547 HOH B O   1 
HETATM 7305 O  O   . HOH Z  6 .   ? 69.122  6.984   28.032  1.00 44.73  ? 548 HOH B O   1 
HETATM 7306 O  O   . HOH Z  6 .   ? 47.388  11.351  28.867  1.00 30.48  ? 549 HOH B O   1 
HETATM 7307 O  O   . HOH Z  6 .   ? 36.827  -3.486  24.781  1.00 34.23  ? 550 HOH B O   1 
HETATM 7308 O  O   . HOH Z  6 .   ? 65.000  12.530  26.439  1.00 25.28  ? 551 HOH B O   1 
HETATM 7309 O  O   . HOH Z  6 .   ? 67.833  5.575   25.801  1.00 55.51  ? 552 HOH B O   1 
HETATM 7310 O  O   . HOH Z  6 .   ? 36.111  9.096   30.789  1.00 36.18  ? 553 HOH B O   1 
HETATM 7311 O  O   . HOH Z  6 .   ? 49.566  20.035  13.002  1.00 24.85  ? 554 HOH B O   1 
HETATM 7312 O  O   . HOH Z  6 .   ? 35.063  -2.035  25.551  1.00 41.11  ? 555 HOH B O   1 
HETATM 7313 O  O   . HOH Z  6 .   ? 51.402  21.688  11.278  1.00 42.19  ? 556 HOH B O   1 
HETATM 7314 O  O   . HOH Z  6 .   ? 59.962  -3.656  34.068  1.00 46.08  ? 557 HOH B O   1 
HETATM 7315 O  O   . HOH Z  6 .   ? 48.035  -22.593 30.789  1.00 50.56  ? 558 HOH B O   1 
HETATM 7316 O  O   . HOH Z  6 .   ? 51.155  17.571  8.462   1.00 40.85  ? 559 HOH B O   1 
HETATM 7317 O  O   . HOH Z  6 .   ? 34.901  -13.763 15.051  1.00 49.03  ? 560 HOH B O   1 
HETATM 7318 O  O   . HOH Z  6 .   ? 63.847  5.646   33.193  1.00 39.54  ? 561 HOH B O   1 
HETATM 7319 O  O   . HOH Z  6 .   ? 55.950  -7.046  35.400  0.50 35.16  ? 562 HOH B O   1 
HETATM 7320 O  O   . HOH Z  6 .   ? 49.142  -6.832  39.762  1.00 42.17  ? 563 HOH B O   1 
HETATM 7321 O  O   . HOH AA 6 .   ? -28.948 -13.557 -0.165  1.00 48.28  ? 401 HOH C O   1 
HETATM 7322 O  O   . HOH AA 6 .   ? -21.498 -21.125 27.523  1.00 17.91  ? 402 HOH C O   1 
HETATM 7323 O  O   . HOH AA 6 .   ? -42.322 -15.398 21.415  0.60 31.05  ? 403 HOH C O   1 
HETATM 7324 O  O   . HOH AA 6 .   ? -40.062 -3.497  7.927   1.00 36.75  ? 404 HOH C O   1 
HETATM 7325 O  O   . HOH AA 6 .   ? -40.021 -3.138  18.626  0.60 16.79  ? 405 HOH C O   1 
HETATM 7326 O  O   . HOH AA 6 .   ? -11.173 -23.576 4.523   1.00 31.47  ? 406 HOH C O   1 
HETATM 7327 O  O   . HOH AA 6 .   ? -42.088 -2.059  11.165  1.00 41.48  ? 407 HOH C O   1 
HETATM 7328 O  O   . HOH AA 6 .   ? -36.621 -24.327 7.440   1.00 31.99  ? 408 HOH C O   1 
HETATM 7329 O  O   . HOH AA 6 .   ? -13.309 -15.951 14.391  1.00 19.84  ? 409 HOH C O   1 
HETATM 7330 O  O   . HOH AA 6 .   ? -8.779  -27.695 10.805  1.00 38.74  ? 410 HOH C O   1 
HETATM 7331 O  O   . HOH AA 6 .   ? 1.617   -11.202 10.346  1.00 37.38  ? 411 HOH C O   1 
HETATM 7332 O  O   . HOH AA 6 .   ? -18.066 -7.696  -0.164  1.00 36.28  ? 412 HOH C O   1 
HETATM 7333 O  O   . HOH AA 6 .   ? -31.234 -0.885  27.544  1.00 29.46  ? 413 HOH C O   1 
HETATM 7334 O  O   . HOH AA 6 .   ? -45.070 -11.077 4.309   1.00 38.11  ? 414 HOH C O   1 
HETATM 7335 O  O   . HOH AA 6 .   ? -23.064 -25.958 6.468   1.00 31.13  ? 415 HOH C O   1 
HETATM 7336 O  O   . HOH AA 6 .   ? -14.674 -27.343 1.867   1.00 49.62  ? 416 HOH C O   1 
HETATM 7337 O  O   . HOH AA 6 .   ? -35.146 -26.231 21.552  1.00 57.30  ? 417 HOH C O   1 
HETATM 7338 O  O   . HOH AA 6 .   ? -34.140 -23.442 25.305  0.60 19.24  ? 418 HOH C O   1 
HETATM 7339 O  O   . HOH AA 6 .   ? -6.598  14.725  20.911  1.00 56.72  ? 419 HOH C O   1 
HETATM 7340 O  O   . HOH AA 6 .   ? -31.692 -6.582  3.764   1.00 22.10  ? 420 HOH C O   1 
HETATM 7341 O  O   . HOH AA 6 .   ? -35.238 -13.608 30.999  1.00 58.69  ? 421 HOH C O   1 
HETATM 7342 O  O   . HOH AA 6 .   ? -0.395  -22.883 8.413   1.00 46.42  ? 422 HOH C O   1 
HETATM 7343 O  O   . HOH AA 6 .   ? -33.954 0.634   22.398  1.00 28.21  ? 423 HOH C O   1 
HETATM 7344 O  O   . HOH AA 6 .   ? -17.406 -1.626  21.177  1.00 24.65  ? 424 HOH C O   1 
HETATM 7345 O  O   . HOH AA 6 .   ? -2.898  -15.767 17.257  1.00 38.84  ? 425 HOH C O   1 
HETATM 7346 O  O   . HOH AA 6 .   ? -45.494 -14.302 16.958  1.00 46.45  ? 426 HOH C O   1 
HETATM 7347 O  O   . HOH AA 6 .   ? -39.632 -21.381 7.126   1.00 37.17  ? 427 HOH C O   1 
HETATM 7348 O  O   . HOH AA 6 .   ? -23.491 -19.234 35.449  1.00 32.65  ? 428 HOH C O   1 
HETATM 7349 O  O   . HOH AA 6 .   ? -30.834 -9.570  13.910  0.60 110.47 ? 429 HOH C O   1 
HETATM 7350 O  O   . HOH AA 6 .   ? -27.391 -34.338 16.270  1.00 36.92  ? 430 HOH C O   1 
HETATM 7351 O  O   . HOH AA 6 .   ? -28.940 -0.704  34.600  1.00 44.47  ? 431 HOH C O   1 
HETATM 7352 O  O   . HOH AA 6 .   ? -34.495 -23.967 5.880   1.00 28.30  ? 432 HOH C O   1 
HETATM 7353 O  O   . HOH AA 6 .   ? -15.398 -16.393 0.370   1.00 37.52  ? 433 HOH C O   1 
HETATM 7354 O  O   . HOH AA 6 .   ? -28.131 -11.575 -4.590  1.00 51.99  ? 434 HOH C O   1 
HETATM 7355 O  O   . HOH AA 6 .   ? -20.033 -17.827 34.067  1.00 19.50  ? 435 HOH C O   1 
HETATM 7356 O  O   . HOH AA 6 .   ? -5.336  -19.943 16.051  1.00 44.70  ? 436 HOH C O   1 
HETATM 7357 O  O   . HOH AA 6 .   ? -10.947 -18.049 10.901  1.00 21.47  ? 437 HOH C O   1 
HETATM 7358 O  O   . HOH AA 6 .   ? -24.215 -13.094 34.629  1.00 22.75  ? 438 HOH C O   1 
HETATM 7359 O  O   . HOH AA 6 .   ? -13.170 -17.657 12.290  1.00 17.24  ? 439 HOH C O   1 
HETATM 7360 O  O   . HOH AA 6 .   ? -8.881  -17.710 30.786  1.00 41.41  ? 440 HOH C O   1 
HETATM 7361 O  O   . HOH AA 6 .   ? -30.509 -16.362 32.609  1.00 44.28  ? 441 HOH C O   1 
HETATM 7362 O  O   . HOH AA 6 .   ? -34.085 -23.872 9.979   1.00 26.28  ? 442 HOH C O   1 
HETATM 7363 O  O   . HOH AA 6 .   ? -17.720 -23.241 22.750  1.00 27.37  ? 443 HOH C O   1 
HETATM 7364 O  O   . HOH AA 6 .   ? -14.814 -30.059 9.719   1.00 34.67  ? 444 HOH C O   1 
HETATM 7365 O  O   . HOH AA 6 .   ? -20.383 -31.153 12.766  1.00 32.45  ? 445 HOH C O   1 
HETATM 7366 O  O   . HOH AA 6 .   ? -42.004 -13.444 6.696   1.00 30.54  ? 446 HOH C O   1 
HETATM 7367 O  O   . HOH AA 6 .   ? -16.633 -23.043 3.505   1.00 26.67  ? 447 HOH C O   1 
HETATM 7368 O  O   . HOH AA 6 .   ? -30.905 1.231   5.541   1.00 26.38  ? 448 HOH C O   1 
HETATM 7369 O  O   . HOH AA 6 .   ? -15.651 6.919   12.888  1.00 46.79  ? 449 HOH C O   1 
HETATM 7370 O  O   . HOH AA 6 .   ? -12.755 -10.226 16.009  0.60 16.55  ? 450 HOH C O   1 
HETATM 7371 O  O   . HOH AA 6 .   ? -8.595  -24.069 24.264  1.00 16.99  ? 451 HOH C O   1 
HETATM 7372 O  O   . HOH AA 6 .   ? -16.842 -14.920 33.490  1.00 19.66  ? 452 HOH C O   1 
HETATM 7373 O  O   . HOH AA 6 .   ? -26.006 -34.615 12.337  1.00 29.07  ? 453 HOH C O   1 
HETATM 7374 O  O   . HOH AA 6 .   ? -2.300  -14.058 37.735  1.00 45.28  ? 454 HOH C O   1 
HETATM 7375 O  O   . HOH AA 6 .   ? -16.781 0.905   18.564  1.00 24.07  ? 455 HOH C O   1 
HETATM 7376 O  O   . HOH AA 6 .   ? -32.478 -20.578 4.412   1.00 23.63  ? 456 HOH C O   1 
HETATM 7377 O  O   . HOH AA 6 .   ? -18.198 -18.838 27.890  1.00 27.12  ? 457 HOH C O   1 
HETATM 7378 O  O   . HOH AA 6 .   ? -17.456 7.338   26.676  1.00 38.54  ? 458 HOH C O   1 
HETATM 7379 O  O   . HOH AA 6 .   ? -7.509  -0.145  37.330  1.00 35.65  ? 459 HOH C O   1 
HETATM 7380 O  O   . HOH AA 6 .   ? -21.146 -15.652 17.620  1.00 23.63  ? 460 HOH C O   1 
HETATM 7381 O  O   . HOH AA 6 .   ? -20.530 -12.904 5.845   1.00 29.96  ? 461 HOH C O   1 
HETATM 7382 O  O   . HOH AA 6 .   ? -14.950 -17.552 28.826  1.00 34.55  ? 462 HOH C O   1 
HETATM 7383 O  O   . HOH AA 6 .   ? -11.606 4.040   24.487  1.00 29.74  ? 463 HOH C O   1 
HETATM 7384 O  O   . HOH AA 6 .   ? -10.678 5.382   34.965  1.00 43.65  ? 464 HOH C O   1 
HETATM 7385 O  O   . HOH AA 6 .   ? -18.600 -26.342 3.569   1.00 39.39  ? 465 HOH C O   1 
HETATM 7386 O  O   . HOH AA 6 .   ? -27.277 -1.329  4.080   1.00 29.19  ? 466 HOH C O   1 
HETATM 7387 O  O   . HOH AA 6 .   ? -40.568 -20.527 17.382  1.00 31.57  ? 467 HOH C O   1 
HETATM 7388 O  O   . HOH AA 6 .   ? -15.031 -24.605 25.605  1.00 33.43  ? 468 HOH C O   1 
HETATM 7389 O  O   . HOH AA 6 .   ? -26.637 -0.820  1.373   1.00 29.68  ? 469 HOH C O   1 
HETATM 7390 O  O   . HOH AA 6 .   ? 11.162  -14.261 1.883   1.00 39.23  ? 470 HOH C O   1 
HETATM 7391 O  O   . HOH AA 6 .   ? -15.462 -2.908  22.663  1.00 25.94  ? 471 HOH C O   1 
HETATM 7392 O  O   . HOH AA 6 .   ? -22.026 1.907   22.493  1.00 31.38  ? 472 HOH C O   1 
HETATM 7393 O  O   . HOH AA 6 .   ? -18.904 -17.096 0.635   1.00 37.10  ? 473 HOH C O   1 
HETATM 7394 O  O   . HOH AA 6 .   ? -22.235 2.347   12.870  1.00 32.73  ? 474 HOH C O   1 
HETATM 7395 O  O   . HOH AA 6 .   ? -22.537 -9.459  12.542  1.00 54.93  ? 475 HOH C O   1 
HETATM 7396 O  O   . HOH AA 6 .   ? -37.824 -12.439 1.080   1.00 34.98  ? 476 HOH C O   1 
HETATM 7397 O  O   . HOH AA 6 .   ? -29.975 -29.358 15.154  1.00 41.84  ? 477 HOH C O   1 
HETATM 7398 O  O   . HOH AA 6 .   ? -22.442 7.095   20.492  1.00 36.92  ? 478 HOH C O   1 
HETATM 7399 O  O   . HOH AA 6 .   ? -16.373 -20.795 16.624  1.00 18.71  ? 479 HOH C O   1 
HETATM 7400 O  O   . HOH AA 6 .   ? -41.928 -4.641  15.507  1.00 43.91  ? 480 HOH C O   1 
HETATM 7401 O  O   . HOH AA 6 .   ? -44.409 -7.913  1.583   1.00 33.12  ? 481 HOH C O   1 
HETATM 7402 O  O   . HOH AA 6 .   ? 1.421   -17.179 7.937   1.00 35.60  ? 482 HOH C O   1 
HETATM 7403 O  O   . HOH AA 6 .   ? -12.268 -28.976 20.124  1.00 40.04  ? 483 HOH C O   1 
HETATM 7404 O  O   . HOH AA 6 .   ? -9.192  -13.875 29.923  1.00 35.59  ? 484 HOH C O   1 
HETATM 7405 O  O   . HOH AA 6 .   ? -5.691  -21.134 10.450  1.00 29.86  ? 485 HOH C O   1 
HETATM 7406 O  O   . HOH AA 6 .   ? -39.115 -6.837  26.429  1.00 50.66  ? 486 HOH C O   1 
HETATM 7407 O  O   . HOH AA 6 .   ? -15.303 3.456   19.685  1.00 31.12  ? 487 HOH C O   1 
HETATM 7408 O  O   . HOH AA 6 .   ? -30.515 6.188   29.505  1.00 54.45  ? 488 HOH C O   1 
HETATM 7409 O  O   . HOH AA 6 .   ? -28.961 -19.289 24.661  0.60 39.41  ? 489 HOH C O   1 
HETATM 7410 O  O   . HOH AA 6 .   ? -21.454 -5.485  13.994  1.00 27.85  ? 490 HOH C O   1 
HETATM 7411 O  O   . HOH AA 6 .   ? -33.993 -20.432 0.881   1.00 43.26  ? 491 HOH C O   1 
HETATM 7412 O  O   . HOH AA 6 .   ? -36.970 -5.464  26.038  1.00 39.67  ? 492 HOH C O   1 
HETATM 7413 O  O   . HOH AA 6 .   ? -23.910 -28.266 7.261   1.00 33.78  ? 493 HOH C O   1 
HETATM 7414 O  O   . HOH AA 6 .   ? -31.344 -23.084 3.457   1.00 38.46  ? 494 HOH C O   1 
HETATM 7415 O  O   . HOH AA 6 .   ? -11.599 -25.431 26.298  1.00 21.25  ? 495 HOH C O   1 
HETATM 7416 O  O   . HOH AA 6 .   ? -31.433 -16.794 0.746   1.00 50.79  ? 496 HOH C O   1 
HETATM 7417 O  O   . HOH AA 6 .   ? -6.187  -17.823 25.769  1.00 30.98  ? 497 HOH C O   1 
HETATM 7418 O  O   . HOH AA 6 .   ? -9.303  -4.094  24.999  1.00 49.02  ? 498 HOH C O   1 
HETATM 7419 O  O   . HOH AA 6 .   ? -13.986 -8.856  13.801  0.60 29.24  ? 499 HOH C O   1 
HETATM 7420 O  O   . HOH AA 6 .   ? -24.688 8.125   23.929  1.00 42.44  ? 500 HOH C O   1 
HETATM 7421 O  O   . HOH AA 6 .   ? -20.781 -24.143 20.917  1.00 22.52  ? 501 HOH C O   1 
HETATM 7422 O  O   . HOH AA 6 .   ? -14.223 6.420   7.429   1.00 45.37  ? 502 HOH C O   1 
HETATM 7423 O  O   . HOH AA 6 .   ? -20.182 -7.894  10.554  0.60 35.15  ? 503 HOH C O   1 
HETATM 7424 O  O   . HOH AA 6 .   ? -13.900 -8.544  16.213  1.00 32.54  ? 504 HOH C O   1 
HETATM 7425 O  O   . HOH AA 6 .   ? -21.805 -12.259 23.954  1.00 18.27  ? 505 HOH C O   1 
HETATM 7426 O  O   . HOH AA 6 .   ? -2.283  3.585   20.876  1.00 43.96  ? 506 HOH C O   1 
HETATM 7427 O  O   . HOH AA 6 .   ? -24.361 -2.233  0.699   1.00 36.47  ? 507 HOH C O   1 
HETATM 7428 O  O   . HOH AA 6 .   ? -20.083 -27.460 5.432   1.00 35.90  ? 508 HOH C O   1 
HETATM 7429 O  O   . HOH AA 6 .   ? -23.427 -13.431 11.328  1.00 25.20  ? 509 HOH C O   1 
HETATM 7430 O  O   . HOH AA 6 .   ? -14.720 -14.009 31.550  1.00 28.29  ? 510 HOH C O   1 
HETATM 7431 O  O   . HOH AA 6 .   ? -1.489  -16.145 12.539  1.00 34.28  ? 511 HOH C O   1 
HETATM 7432 O  O   . HOH AA 6 .   ? -4.466  -5.687  34.606  1.00 44.20  ? 512 HOH C O   1 
HETATM 7433 O  O   . HOH AA 6 .   ? -22.313 -22.793 25.392  1.00 23.57  ? 513 HOH C O   1 
HETATM 7434 O  O   . HOH AA 6 .   ? -14.805 -20.007 35.444  1.00 20.06  ? 514 HOH C O   1 
HETATM 7435 O  O   . HOH AA 6 .   ? -26.814 -23.747 24.981  1.00 40.72  ? 515 HOH C O   1 
HETATM 7436 O  O   . HOH AA 6 .   ? -12.121 -29.469 9.370   1.00 40.47  ? 516 HOH C O   1 
HETATM 7437 O  O   . HOH AA 6 .   ? -4.759  3.216   31.965  1.00 48.68  ? 517 HOH C O   1 
HETATM 7438 O  O   . HOH AA 6 .   ? -17.857 -20.045 20.712  1.00 20.04  ? 518 HOH C O   1 
HETATM 7439 O  O   . HOH AA 6 .   ? -5.370  -14.057 20.151  1.00 34.12  ? 519 HOH C O   1 
HETATM 7440 O  O   . HOH AA 6 .   ? -20.378 -24.103 24.233  1.00 35.91  ? 520 HOH C O   1 
HETATM 7441 O  O   . HOH AA 6 .   ? -39.051 -9.340  19.946  1.00 38.96  ? 521 HOH C O   1 
HETATM 7442 O  O   . HOH AA 6 .   ? -32.993 -19.417 31.703  1.00 34.07  ? 522 HOH C O   1 
HETATM 7443 O  O   . HOH AA 6 .   ? -38.664 -1.321  22.996  1.00 59.24  ? 523 HOH C O   1 
HETATM 7444 O  O   . HOH AA 6 .   ? -31.556 3.669   29.856  1.00 43.30  ? 524 HOH C O   1 
HETATM 7445 O  O   . HOH AA 6 .   ? -32.604 -20.333 28.130  1.00 27.81  ? 525 HOH C O   1 
HETATM 7446 O  O   . HOH AA 6 .   ? -16.157 -19.126 18.731  1.00 17.90  ? 526 HOH C O   1 
HETATM 7447 O  O   . HOH AA 6 .   ? -30.256 -25.408 24.076  1.00 35.52  ? 527 HOH C O   1 
HETATM 7448 O  O   . HOH AA 6 .   ? -8.581  0.381   21.743  1.00 45.32  ? 528 HOH C O   1 
HETATM 7449 O  O   . HOH AA 6 .   ? -6.822  -14.754 24.048  1.00 46.53  ? 529 HOH C O   1 
HETATM 7450 O  O   . HOH AA 6 .   ? -3.683  -0.204  28.387  1.00 52.96  ? 530 HOH C O   1 
HETATM 7451 O  O   . HOH AA 6 .   ? -8.813  -11.918 34.083  1.00 47.19  ? 531 HOH C O   1 
HETATM 7452 O  O   . HOH AA 6 .   ? -30.286 8.821   7.374   1.00 47.39  ? 532 HOH C O   1 
HETATM 7453 O  O   . HOH AA 6 .   ? -7.745  -7.309  23.161  1.00 42.43  ? 533 HOH C O   1 
HETATM 7454 O  O   . HOH AA 6 .   ? -29.211 -4.144  33.814  1.00 29.42  ? 534 HOH C O   1 
HETATM 7455 O  O   . HOH AA 6 .   ? -28.472 5.105   5.639   1.00 32.06  ? 535 HOH C O   1 
HETATM 7456 O  O   . HOH AA 6 .   ? 6.640   -21.203 0.728   1.00 41.60  ? 536 HOH C O   1 
HETATM 7457 O  O   . HOH AA 6 .   ? -24.411 -21.384 34.143  1.00 34.63  ? 537 HOH C O   1 
HETATM 7458 O  O   . HOH AA 6 .   ? -39.258 -15.416 12.541  1.00 39.07  ? 538 HOH C O   1 
HETATM 7459 O  O   . HOH AA 6 .   ? -29.620 3.283   4.577   1.00 33.55  ? 539 HOH C O   1 
HETATM 7460 O  O   . HOH AA 6 .   ? -8.579  -7.166  0.620   1.00 34.71  ? 540 HOH C O   1 
HETATM 7461 O  O   . HOH AA 6 .   ? -15.041 8.160   32.339  1.00 51.58  ? 541 HOH C O   1 
HETATM 7462 O  O   . HOH AA 6 .   ? -24.359 4.894   14.561  1.00 37.49  ? 542 HOH C O   1 
HETATM 7463 O  O   . HOH AA 6 .   ? -16.806 -25.961 23.758  1.00 27.30  ? 543 HOH C O   1 
HETATM 7464 O  O   . HOH AA 6 .   ? -14.600 -17.613 31.096  1.00 52.64  ? 544 HOH C O   1 
HETATM 7465 O  O   . HOH AA 6 .   ? -46.768 -11.051 11.172  1.00 44.99  ? 545 HOH C O   1 
HETATM 7466 O  O   . HOH AA 6 .   ? -52.200 -10.184 3.900   1.00 43.53  ? 546 HOH C O   1 
HETATM 7467 O  O   . HOH AA 6 .   ? -38.566 0.696   5.650   1.00 39.48  ? 547 HOH C O   1 
HETATM 7468 O  O   . HOH AA 6 .   ? -17.615 -23.293 26.124  1.00 29.24  ? 548 HOH C O   1 
HETATM 7469 O  O   . HOH AA 6 .   ? -17.785 10.545  22.209  1.00 33.86  ? 549 HOH C O   1 
HETATM 7470 O  O   . HOH AA 6 .   ? -36.461 7.549   4.468   1.00 49.56  ? 550 HOH C O   1 
HETATM 7471 O  O   . HOH AA 6 .   ? -17.762 -24.481 34.227  1.00 45.38  ? 551 HOH C O   1 
HETATM 7472 O  O   . HOH AA 6 .   ? -43.767 -13.426 4.787   1.00 41.35  ? 552 HOH C O   1 
HETATM 7473 O  O   . HOH AA 6 .   ? -13.358 -12.635 33.014  1.00 23.40  ? 553 HOH C O   1 
HETATM 7474 O  O   . HOH AA 6 .   ? -18.620 -21.537 27.793  1.00 26.65  ? 554 HOH C O   1 
HETATM 7475 O  O   . HOH AA 6 .   ? -25.627 4.577   1.225   1.00 54.33  ? 555 HOH C O   1 
HETATM 7476 O  O   . HOH AA 6 .   ? -14.854 -16.384 34.570  1.00 25.30  ? 556 HOH C O   1 
HETATM 7477 O  O   . HOH AA 6 .   ? -12.471 -8.554  15.113  1.00 45.26  ? 557 HOH C O   1 
HETATM 7478 O  O   . HOH AA 6 .   ? -19.743 -26.775 21.109  1.00 29.43  ? 558 HOH C O   1 
HETATM 7479 O  O   . HOH AA 6 .   ? -12.477 -30.508 22.959  1.00 45.20  ? 559 HOH C O   1 
HETATM 7480 O  O   . HOH AA 6 .   ? -13.120 -24.791 28.189  1.00 42.12  ? 560 HOH C O   1 
HETATM 7481 O  O   . HOH AA 6 .   ? -13.113 -17.895 32.860  1.00 34.54  ? 561 HOH C O   1 
HETATM 7482 O  O   . HOH AA 6 .   ? -9.097  -8.650  31.227  1.00 43.98  ? 562 HOH C O   1 
HETATM 7483 O  O   . HOH AA 6 .   ? -15.254 6.301   10.568  1.00 39.99  ? 563 HOH C O   1 
HETATM 7484 O  O   . HOH AA 6 .   ? -35.068 -19.086 27.694  1.00 33.06  ? 564 HOH C O   1 
HETATM 7485 O  O   . HOH AA 6 .   ? 19.209  -22.092 -2.889  1.00 31.25  ? 565 HOH C O   1 
HETATM 7486 O  O   . HOH AA 6 .   ? -6.723  -18.037 29.344  1.00 49.28  ? 566 HOH C O   1 
HETATM 7487 O  O   . HOH AA 6 .   ? -47.157 -11.776 16.407  1.00 50.93  ? 567 HOH C O   1 
HETATM 7488 O  O   . HOH AA 6 .   ? -12.634 -33.216 19.772  1.00 48.23  ? 568 HOH C O   1 
HETATM 7489 O  O   . HOH AA 6 .   ? -12.566 -30.301 15.792  1.00 63.62  ? 569 HOH C O   1 
HETATM 7490 O  O   . HOH AA 6 .   ? -33.234 9.085   17.656  1.00 47.94  ? 570 HOH C O   1 
# 
