data_9OR6
# 
_entry.id   9OR6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9OR6         pdb_00009or6 10.2210/pdb9or6/pdb 
WWPDB D_1000296143 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9OR6 
_pdbx_database_status.recvd_initial_deposition_date   2025-05-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mjunop@uwo.ca 
_pdbx_contact_author.name_first         Murray 
_pdbx_contact_author.name_last          Junop 
_pdbx_contact_author.name_mi            S 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6676-5717 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Szabla, R.'  1 0000-0002-6379-232X 
'Junop, M.S.' 2 0000-0001-6676-5717 
'Wood, K.'    3 0000-0002-4672-3832 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Self-assembly of PprA from D.radiodurans' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Szabla, R.'  1 0000-0002-6379-232X 
primary 'Junop, M.S.' 2 0000-0001-6676-5717 
# 
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 'DNA repair protein PprA' 29731.230 2  ? 'D180K, D184K' ? 
'1-8 deletion of PprA from D.radiodurans with D180K/D184K mutation' 
2 non-polymer syn SPERMIDINE                145.246   3  ? ?              ? ? 
3 water       nat water                     18.015    47 ? ?              ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Pleiotropic protein promoting DNA repair' 
# 
_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       
;QTDGIYAAFDTLMSTAGVDSQIAALAASEADAGTLDAALTQSLQEAQGRWGLGLHHLRHEARLTDDGDIEILTDGRPSAR
VSEGFGALAQAYAPMQALDERGLSQWAALGEGYRAPGDLPLAQLKVLIEHARDFETDWSAGRGETFQRVWRKGDTLFVEV
ARPASAEAALSKAAWKVIASIKDRAFQRELMRRSEKDGMLGALLGARHAGAKANLAQLPEAHFTVQAFVQTLSGAAARNA
EEYRAALKTAAAALEEYQGVTTRQLSEVLRHGLRES
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QTDGIYAAFDTLMSTAGVDSQIAALAASEADAGTLDAALTQSLQEAQGRWGLGLHHLRHEARLTDDGDIEILTDGRPSAR
VSEGFGALAQAYAPMQALDERGLSQWAALGEGYRAPGDLPLAQLKVLIEHARDFETDWSAGRGETFQRVWRKGDTLFVEV
ARPASAEAALSKAAWKVIASIKDRAFQRELMRRSEKDGMLGALLGARHAGAKANLAQLPEAHFTVQAFVQTLSGAAARNA
EEYRAALKTAAAALEEYQGVTTRQLSEVLRHGLRES
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 SPERMIDINE SPD 
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   THR n 
1 3   ASP n 
1 4   GLY n 
1 5   ILE n 
1 6   TYR n 
1 7   ALA n 
1 8   ALA n 
1 9   PHE n 
1 10  ASP n 
1 11  THR n 
1 12  LEU n 
1 13  MET n 
1 14  SER n 
1 15  THR n 
1 16  ALA n 
1 17  GLY n 
1 18  VAL n 
1 19  ASP n 
1 20  SER n 
1 21  GLN n 
1 22  ILE n 
1 23  ALA n 
1 24  ALA n 
1 25  LEU n 
1 26  ALA n 
1 27  ALA n 
1 28  SER n 
1 29  GLU n 
1 30  ALA n 
1 31  ASP n 
1 32  ALA n 
1 33  GLY n 
1 34  THR n 
1 35  LEU n 
1 36  ASP n 
1 37  ALA n 
1 38  ALA n 
1 39  LEU n 
1 40  THR n 
1 41  GLN n 
1 42  SER n 
1 43  LEU n 
1 44  GLN n 
1 45  GLU n 
1 46  ALA n 
1 47  GLN n 
1 48  GLY n 
1 49  ARG n 
1 50  TRP n 
1 51  GLY n 
1 52  LEU n 
1 53  GLY n 
1 54  LEU n 
1 55  HIS n 
1 56  HIS n 
1 57  LEU n 
1 58  ARG n 
1 59  HIS n 
1 60  GLU n 
1 61  ALA n 
1 62  ARG n 
1 63  LEU n 
1 64  THR n 
1 65  ASP n 
1 66  ASP n 
1 67  GLY n 
1 68  ASP n 
1 69  ILE n 
1 70  GLU n 
1 71  ILE n 
1 72  LEU n 
1 73  THR n 
1 74  ASP n 
1 75  GLY n 
1 76  ARG n 
1 77  PRO n 
1 78  SER n 
1 79  ALA n 
1 80  ARG n 
1 81  VAL n 
1 82  SER n 
1 83  GLU n 
1 84  GLY n 
1 85  PHE n 
1 86  GLY n 
1 87  ALA n 
1 88  LEU n 
1 89  ALA n 
1 90  GLN n 
1 91  ALA n 
1 92  TYR n 
1 93  ALA n 
1 94  PRO n 
1 95  MET n 
1 96  GLN n 
1 97  ALA n 
1 98  LEU n 
1 99  ASP n 
1 100 GLU n 
1 101 ARG n 
1 102 GLY n 
1 103 LEU n 
1 104 SER n 
1 105 GLN n 
1 106 TRP n 
1 107 ALA n 
1 108 ALA n 
1 109 LEU n 
1 110 GLY n 
1 111 GLU n 
1 112 GLY n 
1 113 TYR n 
1 114 ARG n 
1 115 ALA n 
1 116 PRO n 
1 117 GLY n 
1 118 ASP n 
1 119 LEU n 
1 120 PRO n 
1 121 LEU n 
1 122 ALA n 
1 123 GLN n 
1 124 LEU n 
1 125 LYS n 
1 126 VAL n 
1 127 LEU n 
1 128 ILE n 
1 129 GLU n 
1 130 HIS n 
1 131 ALA n 
1 132 ARG n 
1 133 ASP n 
1 134 PHE n 
1 135 GLU n 
1 136 THR n 
1 137 ASP n 
1 138 TRP n 
1 139 SER n 
1 140 ALA n 
1 141 GLY n 
1 142 ARG n 
1 143 GLY n 
1 144 GLU n 
1 145 THR n 
1 146 PHE n 
1 147 GLN n 
1 148 ARG n 
1 149 VAL n 
1 150 TRP n 
1 151 ARG n 
1 152 LYS n 
1 153 GLY n 
1 154 ASP n 
1 155 THR n 
1 156 LEU n 
1 157 PHE n 
1 158 VAL n 
1 159 GLU n 
1 160 VAL n 
1 161 ALA n 
1 162 ARG n 
1 163 PRO n 
1 164 ALA n 
1 165 SER n 
1 166 ALA n 
1 167 GLU n 
1 168 ALA n 
1 169 ALA n 
1 170 LEU n 
1 171 SER n 
1 172 LYS n 
1 173 ALA n 
1 174 ALA n 
1 175 TRP n 
1 176 LYS n 
1 177 VAL n 
1 178 ILE n 
1 179 ALA n 
1 180 SER n 
1 181 ILE n 
1 182 LYS n 
1 183 ASP n 
1 184 ARG n 
1 185 ALA n 
1 186 PHE n 
1 187 GLN n 
1 188 ARG n 
1 189 GLU n 
1 190 LEU n 
1 191 MET n 
1 192 ARG n 
1 193 ARG n 
1 194 SER n 
1 195 GLU n 
1 196 LYS n 
1 197 ASP n 
1 198 GLY n 
1 199 MET n 
1 200 LEU n 
1 201 GLY n 
1 202 ALA n 
1 203 LEU n 
1 204 LEU n 
1 205 GLY n 
1 206 ALA n 
1 207 ARG n 
1 208 HIS n 
1 209 ALA n 
1 210 GLY n 
1 211 ALA n 
1 212 LYS n 
1 213 ALA n 
1 214 ASN n 
1 215 LEU n 
1 216 ALA n 
1 217 GLN n 
1 218 LEU n 
1 219 PRO n 
1 220 GLU n 
1 221 ALA n 
1 222 HIS n 
1 223 PHE n 
1 224 THR n 
1 225 VAL n 
1 226 GLN n 
1 227 ALA n 
1 228 PHE n 
1 229 VAL n 
1 230 GLN n 
1 231 THR n 
1 232 LEU n 
1 233 SER n 
1 234 GLY n 
1 235 ALA n 
1 236 ALA n 
1 237 ALA n 
1 238 ARG n 
1 239 ASN n 
1 240 ALA n 
1 241 GLU n 
1 242 GLU n 
1 243 TYR n 
1 244 ARG n 
1 245 ALA n 
1 246 ALA n 
1 247 LEU n 
1 248 LYS n 
1 249 THR n 
1 250 ALA n 
1 251 ALA n 
1 252 ALA n 
1 253 ALA n 
1 254 LEU n 
1 255 GLU n 
1 256 GLU n 
1 257 TYR n 
1 258 GLN n 
1 259 GLY n 
1 260 VAL n 
1 261 THR n 
1 262 THR n 
1 263 ARG n 
1 264 GLN n 
1 265 LEU n 
1 266 SER n 
1 267 GLU n 
1 268 VAL n 
1 269 LEU n 
1 270 ARG n 
1 271 HIS n 
1 272 GLY n 
1 273 LEU n 
1 274 ARG n 
1 275 GLU n 
1 276 SER 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                   276 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'pprA, DR_A0346' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    R1 
_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      'Deinococcus radiodurans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1299 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 'ATCC 13939' 
_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               'BL21(DE3)' 
_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          'E.coli expression plasmid' 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   'pDEST-527-based expression plasmid' 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMJ5666 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                                              'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                                              'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                                              'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                                              'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ?                                              'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                                              'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                                              'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                                              'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                                              'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                                              'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                                              'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                                              'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                                              'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                                              'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                                              'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                                              'C3 H7 N O3'     105.093 
SPD non-polymer         . SPERMIDINE      'N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)' 'C7 H19 N3'      145.246 
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   GLN 1   9   ?   ?   ?   A . n 
A 1 2   THR 2   10  ?   ?   ?   A . n 
A 1 3   ASP 3   11  11  ASP ASP A . n 
A 1 4   GLY 4   12  12  GLY GLY A . n 
A 1 5   ILE 5   13  13  ILE ILE A . n 
A 1 6   TYR 6   14  14  TYR TYR A . n 
A 1 7   ALA 7   15  15  ALA ALA A . n 
A 1 8   ALA 8   16  16  ALA ALA A . n 
A 1 9   PHE 9   17  17  PHE PHE A . n 
A 1 10  ASP 10  18  18  ASP ASP A . n 
A 1 11  THR 11  19  19  THR THR A . n 
A 1 12  LEU 12  20  20  LEU LEU A . n 
A 1 13  MET 13  21  21  MET MET A . n 
A 1 14  SER 14  22  22  SER SER A . n 
A 1 15  THR 15  23  23  THR THR A . n 
A 1 16  ALA 16  24  24  ALA ALA A . n 
A 1 17  GLY 17  25  25  GLY GLY A . n 
A 1 18  VAL 18  26  26  VAL VAL A . n 
A 1 19  ASP 19  27  27  ASP ASP A . n 
A 1 20  SER 20  28  28  SER SER A . n 
A 1 21  GLN 21  29  29  GLN GLN A . n 
A 1 22  ILE 22  30  30  ILE ILE A . n 
A 1 23  ALA 23  31  31  ALA ALA A . n 
A 1 24  ALA 24  32  32  ALA ALA A . n 
A 1 25  LEU 25  33  33  LEU LEU A . n 
A 1 26  ALA 26  34  34  ALA ALA A . n 
A 1 27  ALA 27  35  35  ALA ALA A . n 
A 1 28  SER 28  36  36  SER SER A . n 
A 1 29  GLU 29  37  37  GLU GLU A . n 
A 1 30  ALA 30  38  38  ALA ALA A . n 
A 1 31  ASP 31  39  39  ASP ASP A . n 
A 1 32  ALA 32  40  40  ALA ALA A . n 
A 1 33  GLY 33  41  41  GLY GLY A . n 
A 1 34  THR 34  42  42  THR THR A . n 
A 1 35  LEU 35  43  43  LEU LEU A . n 
A 1 36  ASP 36  44  44  ASP ASP A . n 
A 1 37  ALA 37  45  45  ALA ALA A . n 
A 1 38  ALA 38  46  46  ALA ALA A . n 
A 1 39  LEU 39  47  47  LEU LEU A . n 
A 1 40  THR 40  48  48  THR THR A . n 
A 1 41  GLN 41  49  49  GLN GLN A . n 
A 1 42  SER 42  50  50  SER SER A . n 
A 1 43  LEU 43  51  51  LEU LEU A . n 
A 1 44  GLN 44  52  52  GLN GLN A . n 
A 1 45  GLU 45  53  53  GLU GLU A . n 
A 1 46  ALA 46  54  54  ALA ALA A . n 
A 1 47  GLN 47  55  55  GLN GLN A . n 
A 1 48  GLY 48  56  56  GLY GLY A . n 
A 1 49  ARG 49  57  57  ARG ARG A . n 
A 1 50  TRP 50  58  58  TRP TRP A . n 
A 1 51  GLY 51  59  59  GLY GLY A . n 
A 1 52  LEU 52  60  60  LEU LEU A . n 
A 1 53  GLY 53  61  61  GLY GLY A . n 
A 1 54  LEU 54  62  62  LEU LEU A . n 
A 1 55  HIS 55  63  63  HIS HIS A . n 
A 1 56  HIS 56  64  64  HIS HIS A . n 
A 1 57  LEU 57  65  65  LEU LEU A . n 
A 1 58  ARG 58  66  66  ARG ARG A . n 
A 1 59  HIS 59  67  67  HIS HIS A . n 
A 1 60  GLU 60  68  68  GLU GLU A . n 
A 1 61  ALA 61  69  69  ALA ALA A . n 
A 1 62  ARG 62  70  70  ARG ARG A . n 
A 1 63  LEU 63  71  71  LEU LEU A . n 
A 1 64  THR 64  72  72  THR THR A . n 
A 1 65  ASP 65  73  73  ASP ASP A . n 
A 1 66  ASP 66  74  74  ASP ASP A . n 
A 1 67  GLY 67  75  75  GLY GLY A . n 
A 1 68  ASP 68  76  76  ASP ASP A . n 
A 1 69  ILE 69  77  77  ILE ILE A . n 
A 1 70  GLU 70  78  78  GLU GLU A . n 
A 1 71  ILE 71  79  79  ILE ILE A . n 
A 1 72  LEU 72  80  80  LEU LEU A . n 
A 1 73  THR 73  81  81  THR THR A . n 
A 1 74  ASP 74  82  82  ASP ASP A . n 
A 1 75  GLY 75  83  83  GLY GLY A . n 
A 1 76  ARG 76  84  84  ARG ARG A . n 
A 1 77  PRO 77  85  85  PRO PRO A . n 
A 1 78  SER 78  86  86  SER SER A . n 
A 1 79  ALA 79  87  87  ALA ALA A . n 
A 1 80  ARG 80  88  88  ARG ARG A . n 
A 1 81  VAL 81  89  89  VAL VAL A . n 
A 1 82  SER 82  90  90  SER SER A . n 
A 1 83  GLU 83  91  91  GLU GLU A . n 
A 1 84  GLY 84  92  92  GLY GLY A . n 
A 1 85  PHE 85  93  93  PHE PHE A . n 
A 1 86  GLY 86  94  94  GLY GLY A . n 
A 1 87  ALA 87  95  95  ALA ALA A . n 
A 1 88  LEU 88  96  96  LEU LEU A . n 
A 1 89  ALA 89  97  97  ALA ALA A . n 
A 1 90  GLN 90  98  98  GLN GLN A . n 
A 1 91  ALA 91  99  99  ALA ALA A . n 
A 1 92  TYR 92  100 100 TYR TYR A . n 
A 1 93  ALA 93  101 101 ALA ALA A . n 
A 1 94  PRO 94  102 102 PRO PRO A . n 
A 1 95  MET 95  103 103 MET MET A . n 
A 1 96  GLN 96  104 104 GLN GLN A . n 
A 1 97  ALA 97  105 105 ALA ALA A . n 
A 1 98  LEU 98  106 106 LEU LEU A . n 
A 1 99  ASP 99  107 107 ASP ASP A . n 
A 1 100 GLU 100 108 108 GLU GLU A . n 
A 1 101 ARG 101 109 109 ARG ARG A . n 
A 1 102 GLY 102 110 110 GLY GLY A . n 
A 1 103 LEU 103 111 111 LEU LEU A . n 
A 1 104 SER 104 112 112 SER SER A . n 
A 1 105 GLN 105 113 113 GLN GLN A . n 
A 1 106 TRP 106 114 114 TRP TRP A . n 
A 1 107 ALA 107 115 115 ALA ALA A . n 
A 1 108 ALA 108 116 116 ALA ALA A . n 
A 1 109 LEU 109 117 117 LEU LEU A . n 
A 1 110 GLY 110 118 118 GLY GLY A . n 
A 1 111 GLU 111 119 119 GLU GLU A . n 
A 1 112 GLY 112 120 120 GLY GLY A . n 
A 1 113 TYR 113 121 121 TYR TYR A . n 
A 1 114 ARG 114 122 122 ARG ARG A . n 
A 1 115 ALA 115 123 123 ALA ALA A . n 
A 1 116 PRO 116 124 124 PRO PRO A . n 
A 1 117 GLY 117 125 125 GLY GLY A . n 
A 1 118 ASP 118 126 126 ASP ASP A . n 
A 1 119 LEU 119 127 127 LEU LEU A . n 
A 1 120 PRO 120 128 128 PRO PRO A . n 
A 1 121 LEU 121 129 129 LEU LEU A . n 
A 1 122 ALA 122 130 130 ALA ALA A . n 
A 1 123 GLN 123 131 131 GLN GLN A . n 
A 1 124 LEU 124 132 132 LEU LEU A . n 
A 1 125 LYS 125 133 133 LYS LYS A . n 
A 1 126 VAL 126 134 134 VAL VAL A . n 
A 1 127 LEU 127 135 135 LEU LEU A . n 
A 1 128 ILE 128 136 136 ILE ILE A . n 
A 1 129 GLU 129 137 137 GLU GLU A . n 
A 1 130 HIS 130 138 138 HIS HIS A . n 
A 1 131 ALA 131 139 139 ALA ALA A . n 
A 1 132 ARG 132 140 140 ARG ARG A . n 
A 1 133 ASP 133 141 141 ASP ASP A . n 
A 1 134 PHE 134 142 142 PHE PHE A . n 
A 1 135 GLU 135 143 143 GLU GLU A . n 
A 1 136 THR 136 144 144 THR THR A . n 
A 1 137 ASP 137 145 145 ASP ASP A . n 
A 1 138 TRP 138 146 146 TRP TRP A . n 
A 1 139 SER 139 147 147 SER SER A . n 
A 1 140 ALA 140 148 148 ALA ALA A . n 
A 1 141 GLY 141 149 149 GLY GLY A . n 
A 1 142 ARG 142 150 150 ARG ARG A . n 
A 1 143 GLY 143 151 151 GLY GLY A . n 
A 1 144 GLU 144 152 152 GLU GLU A . n 
A 1 145 THR 145 153 153 THR THR A . n 
A 1 146 PHE 146 154 154 PHE PHE A . n 
A 1 147 GLN 147 155 155 GLN GLN A . n 
A 1 148 ARG 148 156 156 ARG ARG A . n 
A 1 149 VAL 149 157 157 VAL VAL A . n 
A 1 150 TRP 150 158 158 TRP TRP A . n 
A 1 151 ARG 151 159 159 ARG ARG A . n 
A 1 152 LYS 152 160 160 LYS LYS A . n 
A 1 153 GLY 153 161 161 GLY GLY A . n 
A 1 154 ASP 154 162 162 ASP ASP A . n 
A 1 155 THR 155 163 163 THR THR A . n 
A 1 156 LEU 156 164 164 LEU LEU A . n 
A 1 157 PHE 157 165 165 PHE PHE A . n 
A 1 158 VAL 158 166 166 VAL VAL A . n 
A 1 159 GLU 159 167 167 GLU GLU A . n 
A 1 160 VAL 160 168 168 VAL VAL A . n 
A 1 161 ALA 161 169 169 ALA ALA A . n 
A 1 162 ARG 162 170 170 ARG ARG A . n 
A 1 163 PRO 163 171 171 PRO PRO A . n 
A 1 164 ALA 164 172 172 ALA ALA A . n 
A 1 165 SER 165 173 173 SER SER A . n 
A 1 166 ALA 166 174 174 ALA ALA A . n 
A 1 167 GLU 167 175 175 GLU GLU A . n 
A 1 168 ALA 168 176 176 ALA ALA A . n 
A 1 169 ALA 169 177 177 ALA ALA A . n 
A 1 170 LEU 170 178 178 LEU LEU A . n 
A 1 171 SER 171 179 179 SER SER A . n 
A 1 172 LYS 172 180 180 LYS LYS A . n 
A 1 173 ALA 173 181 181 ALA ALA A . n 
A 1 174 ALA 174 182 182 ALA ALA A . n 
A 1 175 TRP 175 183 183 TRP TRP A . n 
A 1 176 LYS 176 184 184 LYS LYS A . n 
A 1 177 VAL 177 185 185 VAL VAL A . n 
A 1 178 ILE 178 186 186 ILE ILE A . n 
A 1 179 ALA 179 187 187 ALA ALA A . n 
A 1 180 SER 180 188 188 SER SER A . n 
A 1 181 ILE 181 189 189 ILE ILE A . n 
A 1 182 LYS 182 190 190 LYS LYS A . n 
A 1 183 ASP 183 191 191 ASP ASP A . n 
A 1 184 ARG 184 192 192 ARG ARG A . n 
A 1 185 ALA 185 193 193 ALA ALA A . n 
A 1 186 PHE 186 194 194 PHE PHE A . n 
A 1 187 GLN 187 195 195 GLN GLN A . n 
A 1 188 ARG 188 196 196 ARG ARG A . n 
A 1 189 GLU 189 197 197 GLU GLU A . n 
A 1 190 LEU 190 198 198 LEU LEU A . n 
A 1 191 MET 191 199 199 MET MET A . n 
A 1 192 ARG 192 200 200 ARG ARG A . n 
A 1 193 ARG 193 201 201 ARG ARG A . n 
A 1 194 SER 194 202 202 SER SER A . n 
A 1 195 GLU 195 203 203 GLU GLU A . n 
A 1 196 LYS 196 204 204 LYS LYS A . n 
A 1 197 ASP 197 205 205 ASP ASP A . n 
A 1 198 GLY 198 206 206 GLY GLY A . n 
A 1 199 MET 199 207 207 MET MET A . n 
A 1 200 LEU 200 208 208 LEU LEU A . n 
A 1 201 GLY 201 209 209 GLY GLY A . n 
A 1 202 ALA 202 210 210 ALA ALA A . n 
A 1 203 LEU 203 211 211 LEU LEU A . n 
A 1 204 LEU 204 212 212 LEU LEU A . n 
A 1 205 GLY 205 213 213 GLY GLY A . n 
A 1 206 ALA 206 214 214 ALA ALA A . n 
A 1 207 ARG 207 215 215 ARG ARG A . n 
A 1 208 HIS 208 216 216 HIS HIS A . n 
A 1 209 ALA 209 217 217 ALA ALA A . n 
A 1 210 GLY 210 218 218 GLY GLY A . n 
A 1 211 ALA 211 219 219 ALA ALA A . n 
A 1 212 LYS 212 220 220 LYS LYS A . n 
A 1 213 ALA 213 221 221 ALA ALA A . n 
A 1 214 ASN 214 222 222 ASN ASN A . n 
A 1 215 LEU 215 223 223 LEU LEU A . n 
A 1 216 ALA 216 224 224 ALA ALA A . n 
A 1 217 GLN 217 225 225 GLN GLN A . n 
A 1 218 LEU 218 226 226 LEU LEU A . n 
A 1 219 PRO 219 227 227 PRO PRO A . n 
A 1 220 GLU 220 228 228 GLU GLU A . n 
A 1 221 ALA 221 229 229 ALA ALA A . n 
A 1 222 HIS 222 230 230 HIS HIS A . n 
A 1 223 PHE 223 231 231 PHE PHE A . n 
A 1 224 THR 224 232 232 THR THR A . n 
A 1 225 VAL 225 233 233 VAL VAL A . n 
A 1 226 GLN 226 234 234 GLN GLN A . n 
A 1 227 ALA 227 235 235 ALA ALA A . n 
A 1 228 PHE 228 236 236 PHE PHE A . n 
A 1 229 VAL 229 237 237 VAL VAL A . n 
A 1 230 GLN 230 238 238 GLN GLN A . n 
A 1 231 THR 231 239 239 THR THR A . n 
A 1 232 LEU 232 240 240 LEU LEU A . n 
A 1 233 SER 233 241 241 SER SER A . n 
A 1 234 GLY 234 242 242 GLY GLY A . n 
A 1 235 ALA 235 243 243 ALA ALA A . n 
A 1 236 ALA 236 244 244 ALA ALA A . n 
A 1 237 ALA 237 245 245 ALA ALA A . n 
A 1 238 ARG 238 246 246 ARG ARG A . n 
A 1 239 ASN 239 247 247 ASN ASN A . n 
A 1 240 ALA 240 248 248 ALA ALA A . n 
A 1 241 GLU 241 249 249 GLU GLU A . n 
A 1 242 GLU 242 250 250 GLU GLU A . n 
A 1 243 TYR 243 251 251 TYR TYR A . n 
A 1 244 ARG 244 252 252 ARG ARG A . n 
A 1 245 ALA 245 253 253 ALA ALA A . n 
A 1 246 ALA 246 254 254 ALA ALA A . n 
A 1 247 LEU 247 255 255 LEU LEU A . n 
A 1 248 LYS 248 256 256 LYS LYS A . n 
A 1 249 THR 249 257 257 THR THR A . n 
A 1 250 ALA 250 258 258 ALA ALA A . n 
A 1 251 ALA 251 259 259 ALA ALA A . n 
A 1 252 ALA 252 260 260 ALA ALA A . n 
A 1 253 ALA 253 261 261 ALA ALA A . n 
A 1 254 LEU 254 262 262 LEU LEU A . n 
A 1 255 GLU 255 263 263 GLU GLU A . n 
A 1 256 GLU 256 264 264 GLU GLU A . n 
A 1 257 TYR 257 265 265 TYR TYR A . n 
A 1 258 GLN 258 266 266 GLN GLN A . n 
A 1 259 GLY 259 267 267 GLY GLY A . n 
A 1 260 VAL 260 268 268 VAL VAL A . n 
A 1 261 THR 261 269 269 THR THR A . n 
A 1 262 THR 262 270 270 THR THR A . n 
A 1 263 ARG 263 271 271 ARG ARG A . n 
A 1 264 GLN 264 272 272 GLN GLN A . n 
A 1 265 LEU 265 273 273 LEU LEU A . n 
A 1 266 SER 266 274 274 SER SER A . n 
A 1 267 GLU 267 275 275 GLU GLU A . n 
A 1 268 VAL 268 276 276 VAL VAL A . n 
A 1 269 LEU 269 277 277 LEU LEU A . n 
A 1 270 ARG 270 278 278 ARG ARG A . n 
A 1 271 HIS 271 279 279 HIS HIS A . n 
A 1 272 GLY 272 280 280 GLY GLY A . n 
A 1 273 LEU 273 281 281 LEU LEU A . n 
A 1 274 ARG 274 282 ?   ?   ?   A . n 
A 1 275 GLU 275 283 ?   ?   ?   A . n 
A 1 276 SER 276 284 ?   ?   ?   A . n 
B 1 1   GLN 1   9   ?   ?   ?   B . n 
B 1 2   THR 2   10  ?   ?   ?   B . n 
B 1 3   ASP 3   11  11  ASP ASP B . n 
B 1 4   GLY 4   12  12  GLY GLY B . n 
B 1 5   ILE 5   13  13  ILE ILE B . n 
B 1 6   TYR 6   14  14  TYR TYR B . n 
B 1 7   ALA 7   15  15  ALA ALA B . n 
B 1 8   ALA 8   16  16  ALA ALA B . n 
B 1 9   PHE 9   17  17  PHE PHE B . n 
B 1 10  ASP 10  18  18  ASP ASP B . n 
B 1 11  THR 11  19  19  THR THR B . n 
B 1 12  LEU 12  20  20  LEU LEU B . n 
B 1 13  MET 13  21  21  MET MET B . n 
B 1 14  SER 14  22  22  SER SER B . n 
B 1 15  THR 15  23  23  THR THR B . n 
B 1 16  ALA 16  24  24  ALA ALA B . n 
B 1 17  GLY 17  25  25  GLY GLY B . n 
B 1 18  VAL 18  26  26  VAL VAL B . n 
B 1 19  ASP 19  27  27  ASP ASP B . n 
B 1 20  SER 20  28  28  SER SER B . n 
B 1 21  GLN 21  29  29  GLN GLN B . n 
B 1 22  ILE 22  30  30  ILE ILE B . n 
B 1 23  ALA 23  31  31  ALA ALA B . n 
B 1 24  ALA 24  32  32  ALA ALA B . n 
B 1 25  LEU 25  33  33  LEU LEU B . n 
B 1 26  ALA 26  34  34  ALA ALA B . n 
B 1 27  ALA 27  35  35  ALA ALA B . n 
B 1 28  SER 28  36  36  SER SER B . n 
B 1 29  GLU 29  37  37  GLU GLU B . n 
B 1 30  ALA 30  38  38  ALA ALA B . n 
B 1 31  ASP 31  39  39  ASP ASP B . n 
B 1 32  ALA 32  40  40  ALA ALA B . n 
B 1 33  GLY 33  41  41  GLY GLY B . n 
B 1 34  THR 34  42  42  THR THR B . n 
B 1 35  LEU 35  43  43  LEU LEU B . n 
B 1 36  ASP 36  44  44  ASP ASP B . n 
B 1 37  ALA 37  45  45  ALA ALA B . n 
B 1 38  ALA 38  46  46  ALA ALA B . n 
B 1 39  LEU 39  47  47  LEU LEU B . n 
B 1 40  THR 40  48  48  THR THR B . n 
B 1 41  GLN 41  49  49  GLN GLN B . n 
B 1 42  SER 42  50  50  SER SER B . n 
B 1 43  LEU 43  51  51  LEU LEU B . n 
B 1 44  GLN 44  52  52  GLN GLN B . n 
B 1 45  GLU 45  53  53  GLU GLU B . n 
B 1 46  ALA 46  54  54  ALA ALA B . n 
B 1 47  GLN 47  55  55  GLN GLN B . n 
B 1 48  GLY 48  56  56  GLY GLY B . n 
B 1 49  ARG 49  57  57  ARG ARG B . n 
B 1 50  TRP 50  58  58  TRP TRP B . n 
B 1 51  GLY 51  59  59  GLY GLY B . n 
B 1 52  LEU 52  60  60  LEU LEU B . n 
B 1 53  GLY 53  61  61  GLY GLY B . n 
B 1 54  LEU 54  62  62  LEU LEU B . n 
B 1 55  HIS 55  63  63  HIS HIS B . n 
B 1 56  HIS 56  64  64  HIS HIS B . n 
B 1 57  LEU 57  65  65  LEU LEU B . n 
B 1 58  ARG 58  66  66  ARG ARG B . n 
B 1 59  HIS 59  67  67  HIS HIS B . n 
B 1 60  GLU 60  68  68  GLU GLU B . n 
B 1 61  ALA 61  69  69  ALA ALA B . n 
B 1 62  ARG 62  70  70  ARG ARG B . n 
B 1 63  LEU 63  71  71  LEU LEU B . n 
B 1 64  THR 64  72  72  THR THR B . n 
B 1 65  ASP 65  73  73  ASP ASP B . n 
B 1 66  ASP 66  74  74  ASP ASP B . n 
B 1 67  GLY 67  75  75  GLY GLY B . n 
B 1 68  ASP 68  76  76  ASP ASP B . n 
B 1 69  ILE 69  77  77  ILE ILE B . n 
B 1 70  GLU 70  78  78  GLU GLU B . n 
B 1 71  ILE 71  79  79  ILE ILE B . n 
B 1 72  LEU 72  80  80  LEU LEU B . n 
B 1 73  THR 73  81  81  THR THR B . n 
B 1 74  ASP 74  82  82  ASP ASP B . n 
B 1 75  GLY 75  83  83  GLY GLY B . n 
B 1 76  ARG 76  84  84  ARG ARG B . n 
B 1 77  PRO 77  85  85  PRO PRO B . n 
B 1 78  SER 78  86  86  SER SER B . n 
B 1 79  ALA 79  87  87  ALA ALA B . n 
B 1 80  ARG 80  88  88  ARG ARG B . n 
B 1 81  VAL 81  89  89  VAL VAL B . n 
B 1 82  SER 82  90  90  SER SER B . n 
B 1 83  GLU 83  91  91  GLU GLU B . n 
B 1 84  GLY 84  92  92  GLY GLY B . n 
B 1 85  PHE 85  93  93  PHE PHE B . n 
B 1 86  GLY 86  94  94  GLY GLY B . n 
B 1 87  ALA 87  95  95  ALA ALA B . n 
B 1 88  LEU 88  96  96  LEU LEU B . n 
B 1 89  ALA 89  97  97  ALA ALA B . n 
B 1 90  GLN 90  98  98  GLN GLN B . n 
B 1 91  ALA 91  99  99  ALA ALA B . n 
B 1 92  TYR 92  100 100 TYR TYR B . n 
B 1 93  ALA 93  101 101 ALA ALA B . n 
B 1 94  PRO 94  102 102 PRO PRO B . n 
B 1 95  MET 95  103 103 MET MET B . n 
B 1 96  GLN 96  104 104 GLN GLN B . n 
B 1 97  ALA 97  105 105 ALA ALA B . n 
B 1 98  LEU 98  106 106 LEU LEU B . n 
B 1 99  ASP 99  107 107 ASP ASP B . n 
B 1 100 GLU 100 108 108 GLU GLU B . n 
B 1 101 ARG 101 109 109 ARG ARG B . n 
B 1 102 GLY 102 110 110 GLY GLY B . n 
B 1 103 LEU 103 111 111 LEU LEU B . n 
B 1 104 SER 104 112 112 SER SER B . n 
B 1 105 GLN 105 113 113 GLN GLN B . n 
B 1 106 TRP 106 114 114 TRP TRP B . n 
B 1 107 ALA 107 115 115 ALA ALA B . n 
B 1 108 ALA 108 116 116 ALA ALA B . n 
B 1 109 LEU 109 117 117 LEU LEU B . n 
B 1 110 GLY 110 118 118 GLY GLY B . n 
B 1 111 GLU 111 119 119 GLU GLU B . n 
B 1 112 GLY 112 120 120 GLY GLY B . n 
B 1 113 TYR 113 121 121 TYR TYR B . n 
B 1 114 ARG 114 122 122 ARG ARG B . n 
B 1 115 ALA 115 123 123 ALA ALA B . n 
B 1 116 PRO 116 124 124 PRO PRO B . n 
B 1 117 GLY 117 125 125 GLY GLY B . n 
B 1 118 ASP 118 126 126 ASP ASP B . n 
B 1 119 LEU 119 127 127 LEU LEU B . n 
B 1 120 PRO 120 128 128 PRO PRO B . n 
B 1 121 LEU 121 129 129 LEU LEU B . n 
B 1 122 ALA 122 130 130 ALA ALA B . n 
B 1 123 GLN 123 131 131 GLN GLN B . n 
B 1 124 LEU 124 132 132 LEU LEU B . n 
B 1 125 LYS 125 133 133 LYS LYS B . n 
B 1 126 VAL 126 134 134 VAL VAL B . n 
B 1 127 LEU 127 135 135 LEU LEU B . n 
B 1 128 ILE 128 136 136 ILE ILE B . n 
B 1 129 GLU 129 137 137 GLU GLU B . n 
B 1 130 HIS 130 138 138 HIS HIS B . n 
B 1 131 ALA 131 139 139 ALA ALA B . n 
B 1 132 ARG 132 140 140 ARG ARG B . n 
B 1 133 ASP 133 141 141 ASP ASP B . n 
B 1 134 PHE 134 142 142 PHE PHE B . n 
B 1 135 GLU 135 143 143 GLU GLU B . n 
B 1 136 THR 136 144 144 THR THR B . n 
B 1 137 ASP 137 145 145 ASP ASP B . n 
B 1 138 TRP 138 146 146 TRP TRP B . n 
B 1 139 SER 139 147 147 SER SER B . n 
B 1 140 ALA 140 148 148 ALA ALA B . n 
B 1 141 GLY 141 149 149 GLY GLY B . n 
B 1 142 ARG 142 150 150 ARG ARG B . n 
B 1 143 GLY 143 151 151 GLY GLY B . n 
B 1 144 GLU 144 152 152 GLU GLU B . n 
B 1 145 THR 145 153 153 THR THR B . n 
B 1 146 PHE 146 154 154 PHE PHE B . n 
B 1 147 GLN 147 155 155 GLN GLN B . n 
B 1 148 ARG 148 156 156 ARG ARG B . n 
B 1 149 VAL 149 157 157 VAL VAL B . n 
B 1 150 TRP 150 158 158 TRP TRP B . n 
B 1 151 ARG 151 159 159 ARG ARG B . n 
B 1 152 LYS 152 160 160 LYS LYS B . n 
B 1 153 GLY 153 161 161 GLY GLY B . n 
B 1 154 ASP 154 162 162 ASP ASP B . n 
B 1 155 THR 155 163 163 THR THR B . n 
B 1 156 LEU 156 164 164 LEU LEU B . n 
B 1 157 PHE 157 165 165 PHE PHE B . n 
B 1 158 VAL 158 166 166 VAL VAL B . n 
B 1 159 GLU 159 167 167 GLU GLU B . n 
B 1 160 VAL 160 168 168 VAL VAL B . n 
B 1 161 ALA 161 169 169 ALA ALA B . n 
B 1 162 ARG 162 170 170 ARG ARG B . n 
B 1 163 PRO 163 171 171 PRO PRO B . n 
B 1 164 ALA 164 172 172 ALA ALA B . n 
B 1 165 SER 165 173 173 SER SER B . n 
B 1 166 ALA 166 174 174 ALA ALA B . n 
B 1 167 GLU 167 175 175 GLU GLU B . n 
B 1 168 ALA 168 176 176 ALA ALA B . n 
B 1 169 ALA 169 177 177 ALA ALA B . n 
B 1 170 LEU 170 178 178 LEU LEU B . n 
B 1 171 SER 171 179 179 SER SER B . n 
B 1 172 LYS 172 180 180 LYS LYS B . n 
B 1 173 ALA 173 181 181 ALA ALA B . n 
B 1 174 ALA 174 182 182 ALA ALA B . n 
B 1 175 TRP 175 183 183 TRP TRP B . n 
B 1 176 LYS 176 184 184 LYS LYS B . n 
B 1 177 VAL 177 185 185 VAL VAL B . n 
B 1 178 ILE 178 186 186 ILE ILE B . n 
B 1 179 ALA 179 187 187 ALA ALA B . n 
B 1 180 SER 180 188 188 SER SER B . n 
B 1 181 ILE 181 189 189 ILE ILE B . n 
B 1 182 LYS 182 190 190 LYS LYS B . n 
B 1 183 ASP 183 191 191 ASP ASP B . n 
B 1 184 ARG 184 192 192 ARG ARG B . n 
B 1 185 ALA 185 193 193 ALA ALA B . n 
B 1 186 PHE 186 194 194 PHE PHE B . n 
B 1 187 GLN 187 195 195 GLN GLN B . n 
B 1 188 ARG 188 196 196 ARG ARG B . n 
B 1 189 GLU 189 197 197 GLU GLU B . n 
B 1 190 LEU 190 198 198 LEU LEU B . n 
B 1 191 MET 191 199 199 MET MET B . n 
B 1 192 ARG 192 200 200 ARG ARG B . n 
B 1 193 ARG 193 201 201 ARG ARG B . n 
B 1 194 SER 194 202 202 SER SER B . n 
B 1 195 GLU 195 203 203 GLU GLU B . n 
B 1 196 LYS 196 204 204 LYS LYS B . n 
B 1 197 ASP 197 205 205 ASP ASP B . n 
B 1 198 GLY 198 206 206 GLY GLY B . n 
B 1 199 MET 199 207 207 MET MET B . n 
B 1 200 LEU 200 208 208 LEU LEU B . n 
B 1 201 GLY 201 209 209 GLY GLY B . n 
B 1 202 ALA 202 210 210 ALA ALA B . n 
B 1 203 LEU 203 211 211 LEU LEU B . n 
B 1 204 LEU 204 212 212 LEU LEU B . n 
B 1 205 GLY 205 213 213 GLY GLY B . n 
B 1 206 ALA 206 214 214 ALA ALA B . n 
B 1 207 ARG 207 215 ?   ?   ?   B . n 
B 1 208 HIS 208 216 ?   ?   ?   B . n 
B 1 209 ALA 209 217 ?   ?   ?   B . n 
B 1 210 GLY 210 218 ?   ?   ?   B . n 
B 1 211 ALA 211 219 ?   ?   ?   B . n 
B 1 212 LYS 212 220 ?   ?   ?   B . n 
B 1 213 ALA 213 221 ?   ?   ?   B . n 
B 1 214 ASN 214 222 ?   ?   ?   B . n 
B 1 215 LEU 215 223 223 LEU LEU B . n 
B 1 216 ALA 216 224 224 ALA ALA B . n 
B 1 217 GLN 217 225 225 GLN GLN B . n 
B 1 218 LEU 218 226 226 LEU LEU B . n 
B 1 219 PRO 219 227 227 PRO PRO B . n 
B 1 220 GLU 220 228 228 GLU GLU B . n 
B 1 221 ALA 221 229 229 ALA ALA B . n 
B 1 222 HIS 222 230 230 HIS HIS B . n 
B 1 223 PHE 223 231 231 PHE PHE B . n 
B 1 224 THR 224 232 232 THR THR B . n 
B 1 225 VAL 225 233 233 VAL VAL B . n 
B 1 226 GLN 226 234 234 GLN GLN B . n 
B 1 227 ALA 227 235 235 ALA ALA B . n 
B 1 228 PHE 228 236 236 PHE PHE B . n 
B 1 229 VAL 229 237 237 VAL VAL B . n 
B 1 230 GLN 230 238 238 GLN GLN B . n 
B 1 231 THR 231 239 239 THR THR B . n 
B 1 232 LEU 232 240 240 LEU LEU B . n 
B 1 233 SER 233 241 241 SER SER B . n 
B 1 234 GLY 234 242 242 GLY GLY B . n 
B 1 235 ALA 235 243 243 ALA ALA B . n 
B 1 236 ALA 236 244 244 ALA ALA B . n 
B 1 237 ALA 237 245 245 ALA ALA B . n 
B 1 238 ARG 238 246 246 ARG ARG B . n 
B 1 239 ASN 239 247 247 ASN ASN B . n 
B 1 240 ALA 240 248 248 ALA ALA B . n 
B 1 241 GLU 241 249 249 GLU GLU B . n 
B 1 242 GLU 242 250 250 GLU GLU B . n 
B 1 243 TYR 243 251 251 TYR TYR B . n 
B 1 244 ARG 244 252 252 ARG ARG B . n 
B 1 245 ALA 245 253 253 ALA ALA B . n 
B 1 246 ALA 246 254 254 ALA ALA B . n 
B 1 247 LEU 247 255 255 LEU LEU B . n 
B 1 248 LYS 248 256 256 LYS LYS B . n 
B 1 249 THR 249 257 257 THR THR B . n 
B 1 250 ALA 250 258 258 ALA ALA B . n 
B 1 251 ALA 251 259 259 ALA ALA B . n 
B 1 252 ALA 252 260 260 ALA ALA B . n 
B 1 253 ALA 253 261 261 ALA ALA B . n 
B 1 254 LEU 254 262 262 LEU LEU B . n 
B 1 255 GLU 255 263 263 GLU GLU B . n 
B 1 256 GLU 256 264 264 GLU GLU B . n 
B 1 257 TYR 257 265 265 TYR TYR B . n 
B 1 258 GLN 258 266 266 GLN GLN B . n 
B 1 259 GLY 259 267 267 GLY GLY B . n 
B 1 260 VAL 260 268 268 VAL VAL B . n 
B 1 261 THR 261 269 269 THR THR B . n 
B 1 262 THR 262 270 270 THR THR B . n 
B 1 263 ARG 263 271 271 ARG ARG B . n 
B 1 264 GLN 264 272 272 GLN GLN B . n 
B 1 265 LEU 265 273 273 LEU LEU B . n 
B 1 266 SER 266 274 274 SER SER B . n 
B 1 267 GLU 267 275 275 GLU GLU B . n 
B 1 268 VAL 268 276 276 VAL VAL B . n 
B 1 269 LEU 269 277 277 LEU LEU B . n 
B 1 270 ARG 270 278 278 ARG ARG B . n 
B 1 271 HIS 271 279 ?   ?   ?   B . n 
B 1 272 GLY 272 280 ?   ?   ?   B . n 
B 1 273 LEU 273 281 ?   ?   ?   B . n 
B 1 274 ARG 274 282 ?   ?   ?   B . n 
B 1 275 GLU 275 283 ?   ?   ?   B . n 
B 1 276 SER 276 284 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SPD 1  301 1  SPD SPD A . 
D 2 SPD 1  302 3  SPD SPD A . 
E 2 SPD 1  301 2  SPD SPD B . 
F 3 HOH 1  401 47 HOH HOH A . 
F 3 HOH 2  402 5  HOH HOH A . 
F 3 HOH 3  403 38 HOH HOH A . 
F 3 HOH 4  404 20 HOH HOH A . 
F 3 HOH 5  405 26 HOH HOH A . 
F 3 HOH 6  406 18 HOH HOH A . 
F 3 HOH 7  407 1  HOH HOH A . 
F 3 HOH 8  408 17 HOH HOH A . 
F 3 HOH 9  409 2  HOH HOH A . 
F 3 HOH 10 410 24 HOH HOH A . 
F 3 HOH 11 411 3  HOH HOH A . 
F 3 HOH 12 412 12 HOH HOH A . 
F 3 HOH 13 413 19 HOH HOH A . 
F 3 HOH 14 414 28 HOH HOH A . 
F 3 HOH 15 415 25 HOH HOH A . 
F 3 HOH 16 416 41 HOH HOH A . 
F 3 HOH 17 417 39 HOH HOH A . 
F 3 HOH 18 418 14 HOH HOH A . 
F 3 HOH 19 419 29 HOH HOH A . 
F 3 HOH 20 420 22 HOH HOH A . 
F 3 HOH 21 421 7  HOH HOH A . 
F 3 HOH 22 422 42 HOH HOH A . 
F 3 HOH 23 423 16 HOH HOH A . 
F 3 HOH 24 424 40 HOH HOH A . 
F 3 HOH 25 425 11 HOH HOH A . 
F 3 HOH 26 426 37 HOH HOH A . 
F 3 HOH 27 427 44 HOH HOH A . 
F 3 HOH 28 428 43 HOH HOH A . 
F 3 HOH 29 429 32 HOH HOH A . 
F 3 HOH 30 430 8  HOH HOH A . 
F 3 HOH 31 431 31 HOH HOH A . 
F 3 HOH 32 432 35 HOH HOH A . 
F 3 HOH 33 433 45 HOH HOH A . 
F 3 HOH 34 434 36 HOH HOH A . 
F 3 HOH 35 435 46 HOH HOH A . 
G 3 HOH 1  401 6  HOH HOH B . 
G 3 HOH 2  402 13 HOH HOH B . 
G 3 HOH 3  403 15 HOH HOH B . 
G 3 HOH 4  404 4  HOH HOH B . 
G 3 HOH 5  405 30 HOH HOH B . 
G 3 HOH 6  406 9  HOH HOH B . 
G 3 HOH 7  407 27 HOH HOH B . 
G 3 HOH 8  408 10 HOH HOH B . 
G 3 HOH 9  409 21 HOH HOH B . 
G 3 HOH 10 410 23 HOH HOH B . 
G 3 HOH 11 411 34 HOH HOH B . 
G 3 HOH 12 412 33 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 11  ? CG  ? A ASP 3   CG  
2  1 Y 1 A ASP 11  ? OD1 ? A ASP 3   OD1 
3  1 Y 1 A ASP 11  ? OD2 ? A ASP 3   OD2 
4  1 Y 1 A LYS 220 ? CG  ? A LYS 212 CG  
5  1 Y 1 A LYS 220 ? CD  ? A LYS 212 CD  
6  1 Y 1 A LYS 220 ? CE  ? A LYS 212 CE  
7  1 Y 1 A LYS 220 ? NZ  ? A LYS 212 NZ  
8  1 Y 1 A ARG 278 ? CG  ? A ARG 270 CG  
9  1 Y 1 A ARG 278 ? CD  ? A ARG 270 CD  
10 1 Y 1 A ARG 278 ? NE  ? A ARG 270 NE  
11 1 Y 1 A ARG 278 ? CZ  ? A ARG 270 CZ  
12 1 Y 1 A ARG 278 ? NH1 ? A ARG 270 NH1 
13 1 Y 1 A ARG 278 ? NH2 ? A ARG 270 NH2 
14 1 Y 1 A HIS 279 ? CG  ? A HIS 271 CG  
15 1 Y 1 A HIS 279 ? ND1 ? A HIS 271 ND1 
16 1 Y 1 A HIS 279 ? CD2 ? A HIS 271 CD2 
17 1 Y 1 A HIS 279 ? CE1 ? A HIS 271 CE1 
18 1 Y 1 A HIS 279 ? NE2 ? A HIS 271 NE2 
19 1 Y 1 A LEU 281 ? CG  ? A LEU 273 CG  
20 1 Y 1 A LEU 281 ? CD1 ? A LEU 273 CD1 
21 1 Y 1 A LEU 281 ? CD2 ? A LEU 273 CD2 
22 1 Y 1 B ASP 11  ? CG  ? B ASP 3   CG  
23 1 Y 1 B ASP 11  ? OD1 ? B ASP 3   OD1 
24 1 Y 1 B ASP 11  ? OD2 ? B ASP 3   OD2 
25 1 Y 1 B ARG 278 ? CG  ? B ARG 270 CG  
26 1 Y 1 B ARG 278 ? CD  ? B ARG 270 CD  
27 1 Y 1 B ARG 278 ? NE  ? B ARG 270 NE  
28 1 Y 1 B ARG 278 ? CZ  ? B ARG 270 CZ  
29 1 Y 1 B ARG 278 ? NH1 ? B ARG 270 NH1 
30 1 Y 1 B ARG 278 ? NH2 ? B ARG 270 NH2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? MxDC     ? ? ? .                               ? 1 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '1.0.5 (20200206)'              ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? 'Jan 31, 2020 (BUILT 20200131)' ? 3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? 0.7.4                           ? 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419                     ? 5 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419                     ? 6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.337 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9OR6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     183.486 
_cell.length_a_esd                 ? 
_cell.length_b                     34.083 
_cell.length_b_esd                 ? 
_cell.length_c                     98.734 
_cell.length_c_esd                 ? 
_cell.volume                       610933.008 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9OR6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_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                   9OR6 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.0 
_exptl_crystal.description                  'long and thin hexagonal-based prisms' 
_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    'Temperature-controlled incubator' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.5 ul of protein solution was mixed with 1.0 uL of crystallization solution and hung upside-down in a sealed chamber containing 1mL of well solution.  
| Protein solution: 5.0 mg/mL PprA (168 uM), 43bp dsDNA (101 uM), 150mM KCl, 20mM Tris, pH 7.5, 1 mM MgCl2.  
| Crystallization solution (Molecular Dimensions - Morpheus 2 #94): 10 mM Spermine tetrahydrochloride, 10 mM Spermidine trihydrochloride, 10 mM 1,4 Diaminobutane dihydrochloride, 10 mM DL Ornithine monohydrochloride
0.1M Gly-Gly, AMPD, pH 8.5, 13% w/v PEG 4000, 21% w/v 1,2,6 Hexanetriol.  
| Well solution: 2.0 M Ammonium sulfate.
;
_exptl_crystal_grow.pdbx_pH_range   7.5-8.5 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             'Nitrogen cryo-stream' 
_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                      'CMCF-ID optics setup' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-02-13 
_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                    'CMCF-ID default optics (Feb 2019)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97934 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          51.01 
_reflns.entry_id                                       9OR6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.90 
_reflns.d_resolution_low                               90.774 
_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                                     13352 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_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                                0.130 
_reflns.pdbx_Rpim_I_all                                0.069 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.094 
_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                                    2.904 
_reflns_shell.d_res_low                                     2.954 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             633 
_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                               3.4 
_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                               0.610 
_reflns_shell.pdbx_Rpim_I_all                               0.417 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.756 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.443 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               51.11 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9OR6 
_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                            2.90 
_refine.ls_d_res_low                             90.77 
_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                     13350 
_refine.ls_number_reflns_R_free                  650 
_refine.ls_number_reflns_R_work                  12700 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.21 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2276 
_refine.ls_R_factor_R_free                       0.2479 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2266 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.2516 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4166 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.90 
_refine_hist.d_res_low                        90.77 
_refine_hist.number_atoms_solvent             47 
_refine_hist.number_atoms_total               4070 
_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        3993 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0037  ? 4086 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.6416  ? 5519 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0428  ? 611  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 729  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 17.1593 ? 1470 ? f_dihedral_angle_d ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.90 3.13  . . 141 2572 99.89 . . . . 0.2756 . . . . . . . . . . . . . . . 0.3308 
'X-RAY DIFFRACTION' 3.13 3.43  . . 127 2527 99.36 . . . . 0.2753 . . . . . . . . . . . . . . . 0.3413 
'X-RAY DIFFRACTION' 3.46 3.94  . . 112 2209 88.69 . . . . 0.2316 . . . . . . . . . . . . . . . 0.2738 
'X-RAY DIFFRACTION' 3.94 4.97  . . 137 2650 99.57 . . . . 0.2053 . . . . . . . . . . . . . . . 0.2013 
'X-RAY DIFFRACTION' 4.97 90.77 . . 133 2742 99.52 . . . . 0.2046 . . . . . . . . . . . . . . . 0.2125 
# 
_struct.entry_id                     9OR6 
_struct.title                        'Crystal structure of PprA S-F-S tetramer from Deinococcus radiodurans' 
_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        9OR6 
_struct_keywords.text            
;PprA, Deinococcus, Deinococcus radiodurans, D. radiodurans, DNA repair, DNA binding protein, Genome reassembly, self-assembly, protein filament
;
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PPRA_DEIRA 
_struct_ref.pdbx_db_accession          O32504 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QTDGIYAAFDTLMSTAGVDSQIAALAASEADAGTLDAALTQSLQEAQGRWGLGLHHLRHEARLTDDGDIEILTDGRPSAR
VSEGFGALAQAYAPMQALDERGLSQWAALGEGYRAPGDLPLAQLKVLIEHARDFETDWSAGRGETFQRVWRKGDTLFVEV
ARPASAEAALSDAAWDVIASIKDRAFQRELMRRSEKDGMLGALLGARHAGAKANLAQLPEAHFTVQAFVQTLSGAAARNA
EEYRAALKTAAAALEEYQGVTTRQLSEVLRHGLRES
;
_struct_ref.pdbx_align_begin           25 
# 
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 9OR6 A 1 ? 276 ? O32504 25 ? 300 ? 9 284 
2 1 9OR6 B 1 ? 276 ? O32504 25 ? 300 ? 9 284 
# 
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 9OR6 LYS A 172 ? UNP O32504 ASP 196 'engineered mutation' 180 1 
1 9OR6 LYS A 176 ? UNP O32504 ASP 200 'engineered mutation' 184 2 
2 9OR6 LYS B 172 ? UNP O32504 ASP 196 'engineered mutation' 180 3 
2 9OR6 LYS B 176 ? UNP O32504 ASP 200 'engineered mutation' 184 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
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_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 
# 
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 ASP A 3   ? THR A 15  ? ASP A 11  THR A 23  1 ? 13 
HELX_P HELX_P2  AA2 GLN A 21  ? SER A 28  ? GLN A 29  SER A 36  1 ? 8  
HELX_P HELX_P3  AA3 ASP A 31  ? GLY A 51  ? ASP A 39  GLY A 59  1 ? 21 
HELX_P HELX_P4  AA4 GLY A 84  ? ALA A 93  ? GLY A 92  ALA A 101 1 ? 10 
HELX_P HELX_P5  AA5 PRO A 94  ? GLN A 96  ? PRO A 102 GLN A 104 5 ? 3  
HELX_P HELX_P6  AA6 PRO A 120 ? ALA A 131 ? PRO A 128 ALA A 139 1 ? 12 
HELX_P HELX_P7  AA7 SER A 165 ? ILE A 181 ? SER A 173 ILE A 189 1 ? 17 
HELX_P HELX_P8  AA8 ASP A 183 ? GLY A 198 ? ASP A 191 GLY A 206 1 ? 16 
HELX_P HELX_P9  AA9 GLY A 198 ? ALA A 206 ? GLY A 206 ALA A 214 1 ? 9  
HELX_P HELX_P10 AB1 LEU A 218 ? HIS A 222 ? LEU A 226 HIS A 230 5 ? 5  
HELX_P HELX_P11 AB2 ALA A 235 ? ARG A 238 ? ALA A 243 ARG A 246 5 ? 4  
HELX_P HELX_P12 AB3 ASN A 239 ? LEU A 273 ? ASN A 247 LEU A 281 1 ? 35 
HELX_P HELX_P13 AB4 GLY B 4   ? THR B 15  ? GLY B 12  THR B 23  1 ? 12 
HELX_P HELX_P14 AB5 GLN B 21  ? SER B 28  ? GLN B 29  SER B 36  1 ? 8  
HELX_P HELX_P15 AB6 ASP B 31  ? GLY B 51  ? ASP B 39  GLY B 59  1 ? 21 
HELX_P HELX_P16 AB7 GLY B 84  ? ALA B 93  ? GLY B 92  ALA B 101 1 ? 10 
HELX_P HELX_P17 AB8 PRO B 94  ? GLN B 96  ? PRO B 102 GLN B 104 5 ? 3  
HELX_P HELX_P18 AB9 PRO B 120 ? ALA B 131 ? PRO B 128 ALA B 139 1 ? 12 
HELX_P HELX_P19 AC1 ARG B 142 ? GLU B 144 ? ARG B 150 GLU B 152 5 ? 3  
HELX_P HELX_P20 AC2 SER B 165 ? SER B 180 ? SER B 173 SER B 188 1 ? 16 
HELX_P HELX_P21 AC3 ASP B 183 ? ALA B 206 ? ASP B 191 ALA B 214 1 ? 24 
HELX_P HELX_P22 AC4 LEU B 218 ? HIS B 222 ? LEU B 226 HIS B 230 5 ? 5  
HELX_P HELX_P23 AC5 ALA B 235 ? ARG B 238 ? ALA B 243 ARG B 246 5 ? 4  
HELX_P HELX_P24 AC6 ASN B 239 ? ARG B 270 ? ASN B 247 ARG B 278 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
# 
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 HIS A 59  ? LEU A 63  ? HIS A 67  LEU A 71  
AA1 2 ILE A 69  ? THR A 73  ? ILE A 77  THR A 81  
AA1 3 ARG A 76  ? ARG A 80  ? ARG A 84  ARG A 88  
AA2 1 PHE A 134 ? GLU A 135 ? PHE A 142 GLU A 143 
AA2 2 PHE A 146 ? LYS A 152 ? PHE A 154 LYS A 160 
AA2 3 THR A 155 ? ALA A 161 ? THR A 163 ALA A 169 
AA2 4 ALA A 227 ? SER A 233 ? ALA A 235 SER A 241 
AA3 1 HIS B 59  ? LEU B 63  ? HIS B 67  LEU B 71  
AA3 2 ILE B 69  ? THR B 73  ? ILE B 77  THR B 81  
AA3 3 ARG B 76  ? ARG B 80  ? ARG B 84  ARG B 88  
AA4 1 PHE B 134 ? GLU B 135 ? PHE B 142 GLU B 143 
AA4 2 PHE B 146 ? LYS B 152 ? PHE B 154 LYS B 160 
AA4 3 SER B 139 ? ALA B 140 ? SER B 147 ALA B 148 
AA5 1 PHE B 134 ? GLU B 135 ? PHE B 142 GLU B 143 
AA5 2 PHE B 146 ? LYS B 152 ? PHE B 154 LYS B 160 
AA5 3 THR B 155 ? ALA B 161 ? THR B 163 ALA B 169 
AA5 4 ALA B 227 ? SER B 233 ? ALA B 235 SER B 241 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 62  ? N ARG A 70  O GLU A 70  ? O GLU A 78  
AA1 2 3 N ILE A 71  ? N ILE A 79  O SER A 78  ? O SER A 86  
AA2 1 2 N PHE A 134 ? N PHE A 142 O ARG A 151 ? O ARG A 159 
AA2 2 3 N TRP A 150 ? N TRP A 158 O PHE A 157 ? O PHE A 165 
AA2 3 4 N VAL A 160 ? N VAL A 168 O PHE A 228 ? O PHE A 236 
AA3 1 2 N ARG B 62  ? N ARG B 70  O GLU B 70  ? O GLU B 78  
AA3 2 3 N ILE B 71  ? N ILE B 79  O ALA B 79  ? O ALA B 87  
AA4 1 2 N PHE B 134 ? N PHE B 142 O ARG B 151 ? O ARG B 159 
AA4 2 3 O GLN B 147 ? O GLN B 155 N SER B 139 ? N SER B 147 
AA5 1 2 N PHE B 134 ? N PHE B 142 O ARG B 151 ? O ARG B 159 
AA5 2 3 N TRP B 150 ? N TRP B 158 O PHE B 157 ? O PHE B 165 
AA5 3 4 N LEU B 156 ? N LEU B 164 O LEU B 232 ? O LEU B 240 
# 
_pdbx_entry_details.entry_id                   9OR6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
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 GLN 9   ? A GLN 1   
2  1 Y 1 A THR 10  ? A THR 2   
3  1 Y 1 A ARG 282 ? A ARG 274 
4  1 Y 1 A GLU 283 ? A GLU 275 
5  1 Y 1 A SER 284 ? A SER 276 
6  1 Y 1 B GLN 9   ? B GLN 1   
7  1 Y 1 B THR 10  ? B THR 2   
8  1 Y 1 B ARG 215 ? B ARG 207 
9  1 Y 1 B HIS 216 ? B HIS 208 
10 1 Y 1 B ALA 217 ? B ALA 209 
11 1 Y 1 B GLY 218 ? B GLY 210 
12 1 Y 1 B ALA 219 ? B ALA 211 
13 1 Y 1 B LYS 220 ? B LYS 212 
14 1 Y 1 B ALA 221 ? B ALA 213 
15 1 Y 1 B ASN 222 ? B ASN 214 
16 1 Y 1 B HIS 279 ? B HIS 271 
17 1 Y 1 B GLY 280 ? B GLY 272 
18 1 Y 1 B LEU 281 ? B LEU 273 
19 1 Y 1 B ARG 282 ? B ARG 274 
20 1 Y 1 B GLU 283 ? B GLU 275 
21 1 Y 1 B SER 284 ? B SER 276 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
SPD N1   N N N 290 
SPD C2   C N N 291 
SPD C3   C N N 292 
SPD C4   C N N 293 
SPD C5   C N N 294 
SPD N6   N N N 295 
SPD C7   C N N 296 
SPD C8   C N N 297 
SPD C9   C N N 298 
SPD N10  N N N 299 
SPD HN11 H N N 300 
SPD HN12 H N N 301 
SPD H21  H N N 302 
SPD H22  H N N 303 
SPD H31  H N N 304 
SPD H32  H N N 305 
SPD H41  H N N 306 
SPD H42  H N N 307 
SPD H51  H N N 308 
SPD H52  H N N 309 
SPD HN6  H N N 310 
SPD H71  H N N 311 
SPD H72  H N N 312 
SPD H81  H N N 313 
SPD H82  H N N 314 
SPD H91  H N N 315 
SPD H92  H N N 316 
SPD H101 H N N 317 
SPD H102 H N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
VAL N    N N N 387 
VAL CA   C N S 388 
VAL C    C N N 389 
VAL O    O N N 390 
VAL CB   C N N 391 
VAL CG1  C N N 392 
VAL CG2  C N N 393 
VAL OXT  O N N 394 
VAL H    H N N 395 
VAL H2   H N N 396 
VAL HA   H N N 397 
VAL HB   H N N 398 
VAL HG11 H N N 399 
VAL HG12 H N N 400 
VAL HG13 H N N 401 
VAL HG21 H N N 402 
VAL HG22 H N N 403 
VAL HG23 H N N 404 
VAL HXT  H N N 405 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
SPD N1  C2   sing N N 277 
SPD N1  HN11 sing N N 278 
SPD N1  HN12 sing N N 279 
SPD C2  C3   sing N N 280 
SPD C2  H21  sing N N 281 
SPD C2  H22  sing N N 282 
SPD C3  C4   sing N N 283 
SPD C3  H31  sing N N 284 
SPD C3  H32  sing N N 285 
SPD C4  C5   sing N N 286 
SPD C4  H41  sing N N 287 
SPD C4  H42  sing N N 288 
SPD C5  N6   sing N N 289 
SPD C5  H51  sing N N 290 
SPD C5  H52  sing N N 291 
SPD N6  C7   sing N N 292 
SPD N6  HN6  sing N N 293 
SPD C7  C8   sing N N 294 
SPD C7  H71  sing N N 295 
SPD C7  H72  sing N N 296 
SPD C8  C9   sing N N 297 
SPD C8  H81  sing N N 298 
SPD C8  H82  sing N N 299 
SPD C9  N10  sing N N 300 
SPD C9  H91  sing N N 301 
SPD C9  H92  sing N N 302 
SPD N10 H101 sing N N 303 
SPD N10 H102 sing N N 304 
THR N   CA   sing N N 305 
THR N   H    sing N N 306 
THR N   H2   sing N N 307 
THR CA  C    sing N N 308 
THR CA  CB   sing N N 309 
THR CA  HA   sing N N 310 
THR C   O    doub N N 311 
THR C   OXT  sing N N 312 
THR CB  OG1  sing N N 313 
THR CB  CG2  sing N N 314 
THR CB  HB   sing N N 315 
THR OG1 HG1  sing N N 316 
THR CG2 HG21 sing N N 317 
THR CG2 HG22 sing N N 318 
THR CG2 HG23 sing N N 319 
THR OXT HXT  sing N N 320 
TRP N   CA   sing N N 321 
TRP N   H    sing N N 322 
TRP N   H2   sing N N 323 
TRP CA  C    sing N N 324 
TRP CA  CB   sing N N 325 
TRP CA  HA   sing N N 326 
TRP C   O    doub N N 327 
TRP C   OXT  sing N N 328 
TRP CB  CG   sing N N 329 
TRP CB  HB2  sing N N 330 
TRP CB  HB3  sing N N 331 
TRP CG  CD1  doub Y N 332 
TRP CG  CD2  sing Y N 333 
TRP CD1 NE1  sing Y N 334 
TRP CD1 HD1  sing N N 335 
TRP CD2 CE2  doub Y N 336 
TRP CD2 CE3  sing Y N 337 
TRP NE1 CE2  sing Y N 338 
TRP NE1 HE1  sing N N 339 
TRP CE2 CZ2  sing Y N 340 
TRP CE3 CZ3  doub Y N 341 
TRP CE3 HE3  sing N N 342 
TRP CZ2 CH2  doub Y N 343 
TRP CZ2 HZ2  sing N N 344 
TRP CZ3 CH2  sing Y N 345 
TRP CZ3 HZ3  sing N N 346 
TRP CH2 HH2  sing N N 347 
TRP OXT HXT  sing N N 348 
TYR N   CA   sing N N 349 
TYR N   H    sing N N 350 
TYR N   H2   sing N N 351 
TYR CA  C    sing N N 352 
TYR CA  CB   sing N N 353 
TYR CA  HA   sing N N 354 
TYR C   O    doub N N 355 
TYR C   OXT  sing N N 356 
TYR CB  CG   sing N N 357 
TYR CB  HB2  sing N N 358 
TYR CB  HB3  sing N N 359 
TYR CG  CD1  doub Y N 360 
TYR CG  CD2  sing Y N 361 
TYR CD1 CE1  sing Y N 362 
TYR CD1 HD1  sing N N 363 
TYR CD2 CE2  doub Y N 364 
TYR CD2 HD2  sing N N 365 
TYR CE1 CZ   doub Y N 366 
TYR CE1 HE1  sing N N 367 
TYR CE2 CZ   sing Y N 368 
TYR CE2 HE2  sing N N 369 
TYR CZ  OH   sing N N 370 
TYR OH  HH   sing N N 371 
TYR OXT HXT  sing N N 372 
VAL N   CA   sing N N 373 
VAL N   H    sing N N 374 
VAL N   H2   sing N N 375 
VAL CA  C    sing N N 376 
VAL CA  CB   sing N N 377 
VAL CA  HA   sing N N 378 
VAL C   O    doub N N 379 
VAL C   OXT  sing N N 380 
VAL CB  CG1  sing N N 381 
VAL CB  CG2  sing N N 382 
VAL CB  HB   sing N N 383 
VAL CG1 HG11 sing N N 384 
VAL CG1 HG12 sing N N 385 
VAL CG1 HG13 sing N N 386 
VAL CG2 HG21 sing N N 387 
VAL CG2 HG22 sing N N 388 
VAL CG2 HG23 sing N N 389 
VAL OXT HXT  sing N N 390 
# 
_pdbx_audit_support.funding_organization   'Natural Sciences and Engineering Research Council (NSERC, Canada)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           2008R00075 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_related_exp_data_set.ordinal              1 
_pdbx_related_exp_data_set.data_reference       10.5281/zenodo.15485035 
_pdbx_related_exp_data_set.metadata_reference   ? 
_pdbx_related_exp_data_set.data_set_type        'diffraction image data' 
_pdbx_related_exp_data_set.details              ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9OR6 
_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]   0.005450 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000799 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.029340 
_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]   0.010236 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASP A 1 3   ? 83.48600  -10.76500 40.55200  1.000 83.06540  ?  11  ASP A N   1 
ATOM   2    C CA  . ASP A 1 3   ? 82.78100  -11.30100 41.70900  1.000 87.62802  ?  11  ASP A CA  1 
ATOM   3    C C   . ASP A 1 3   ? 82.24500  -10.18100 42.59500  1.000 90.18476  ?  11  ASP A C   1 
ATOM   4    O O   . ASP A 1 3   ? 81.16300  -10.29700 43.17100  1.000 80.73921  ?  11  ASP A O   1 
ATOM   5    C CB  . ASP A 1 3   ? 83.70100  -12.21800 42.51800  1.000 78.55303  ?  11  ASP A CB  1 
ATOM   6    N N   . GLY A 1 4   ? 83.01900  -9.09900  42.70900  1.000 87.37785  ?  12  GLY A N   1 
ATOM   7    C CA  . GLY A 1 4   ? 82.60900  -7.98800  43.54800  1.000 72.26978  ?  12  GLY A CA  1 
ATOM   8    C C   . GLY A 1 4   ? 81.41800  -7.21900  43.02300  1.000 65.19219  ?  12  GLY A C   1 
ATOM   9    O O   . GLY A 1 4   ? 80.55600  -6.80500  43.80400  1.000 60.64743  ?  12  GLY A O   1 
ATOM   10   N N   . ILE A 1 5   ? 81.34700  -7.01400  41.70600  1.000 62.58291  ?  13  ILE A N   1 
ATOM   11   C CA  . ILE A 1 5   ? 80.25800  -6.22300  41.14200  1.000 60.34113  ?  13  ILE A CA  1 
ATOM   12   C C   . ILE A 1 5   ? 78.93600  -6.97000  41.26300  1.000 57.05867  ?  13  ILE A C   1 
ATOM   13   O O   . ILE A 1 5   ? 77.87500  -6.36100  41.44400  1.000 54.59513  ?  13  ILE A O   1 
ATOM   14   C CB  . ILE A 1 5   ? 80.57900  -5.83100  39.68700  1.000 52.30979  ?  13  ILE A CB  1 
ATOM   15   C CG1 . ILE A 1 5   ? 80.16600  -4.38400  39.43200  1.000 54.52951  ?  13  ILE A CG1 1 
ATOM   16   C CG2 . ILE A 1 5   ? 79.90000  -6.75200  38.68800  1.000 49.32210  ?  13  ILE A CG2 1 
ATOM   17   C CD1 . ILE A 1 5   ? 81.07600  -3.37100  40.07900  1.000 55.69217  ?  13  ILE A CD1 1 
ATOM   18   N N   . TYR A 1 6   ? 78.97800  -8.30100  41.19300  1.000 59.73328  ?  14  TYR A N   1 
ATOM   19   C CA  . TYR A 1 6   ? 77.75200  -9.08000  41.30000  1.000 56.27274  ?  14  TYR A CA  1 
ATOM   20   C C   . TYR A 1 6   ? 77.19500  -9.01600  42.71500  1.000 53.47822  ?  14  TYR A C   1 
ATOM   21   O O   . TYR A 1 6   ? 75.98600  -8.85000  42.91300  1.000 48.21386  ?  14  TYR A O   1 
ATOM   22   C CB  . TYR A 1 6   ? 78.03100  -10.52100 40.88200  1.000 51.56843  ?  14  TYR A CB  1 
ATOM   23   C CG  . TYR A 1 6   ? 78.43800  -10.64000 39.43300  1.000 60.37475  ?  14  TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 6   ? 77.55400  -10.33200 38.41000  1.000 59.96182  ?  14  TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 6   ? 79.72100  -11.04200 39.09000  1.000 58.69066  ?  14  TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 6   ? 77.93100  -10.43400 37.08600  1.000 58.76748  ?  14  TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 6   ? 80.10700  -11.14500 37.77100  1.000 57.88400  ?  14  TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 6   ? 79.20900  -10.84000 36.77400  1.000 62.81674  ?  14  TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 6   ? 79.59700  -10.94500 35.45900  1.000 73.81824  ?  14  TYR A OH  1 
ATOM   30   N N   . ALA A 1 7   ? 78.07200  -9.12000  43.71600  1.000 53.48661  ?  15  ALA A N   1 
ATOM   31   C CA  . ALA A 1 7   ? 77.64300  -8.96100  45.10000  1.000 53.32850  ?  15  ALA A CA  1 
ATOM   32   C C   . ALA A 1 7   ? 77.19200  -7.53200  45.37700  1.000 54.44106  ?  15  ALA A C   1 
ATOM   33   O O   . ALA A 1 7   ? 76.29200  -7.30600  46.19300  1.000 51.12989  ?  15  ALA A O   1 
ATOM   34   C CB  . ALA A 1 7   ? 78.77000  -9.36600  46.04900  1.000 55.95682  ?  15  ALA A CB  1 
ATOM   35   N N   . ALA A 1 8   ? 77.81400  -6.55100  44.72000  1.000 46.29687  ?  16  ALA A N   1 
ATOM   36   C CA  . ALA A 1 8   ? 77.36300  -5.17000  44.85400  1.000 46.57499  ?  16  ALA A CA  1 
ATOM   37   C C   . ALA A 1 8   ? 75.94400  -5.00700  44.32300  1.000 52.64554  ?  16  ALA A C   1 
ATOM   38   O O   . ALA A 1 8   ? 75.10800  -4.33700  44.93800  1.000 53.63169  ?  16  ALA A O   1 
ATOM   39   C CB  . ALA A 1 8   ? 78.32500  -4.23100  44.12900  1.000 43.59472  ?  16  ALA A CB  1 
ATOM   40   N N   . PHE A 1 9   ? 75.65500  -5.62100  43.17600  1.000 51.47733  ?  17  PHE A N   1 
ATOM   41   C CA  . PHE A 1 9   ? 74.29400  -5.59900  42.64900  1.000 49.55309  ?  17  PHE A CA  1 
ATOM   42   C C   . PHE A 1 9   ? 73.33400  -6.31600  43.59000  1.000 48.35407  ?  17  PHE A C   1 
ATOM   43   O O   . PHE A 1 9   ? 72.19000  -5.88700  43.77500  1.000 48.53333  ?  17  PHE A O   1 
ATOM   44   C CB  . PHE A 1 9   ? 74.26000  -6.23100  41.25900  1.000 47.22304  ?  17  PHE A CB  1 
ATOM   45   C CG  . PHE A 1 9   ? 72.95900  -6.04100  40.54100  1.000 47.42291  ?  17  PHE A CG  1 
ATOM   46   C CD1 . PHE A 1 9   ? 72.74000  -4.91500  39.77000  1.000 45.79023  ?  17  PHE A CD1 1 
ATOM   47   C CD2 . PHE A 1 9   ? 71.95400  -6.98600  40.63600  1.000 48.58930  ?  17  PHE A CD2 1 
ATOM   48   C CE1 . PHE A 1 9   ? 71.54700  -4.73700  39.10700  1.000 48.24404  ?  17  PHE A CE1 1 
ATOM   49   C CE2 . PHE A 1 9   ? 70.75800  -6.81200  39.97600  1.000 50.79000  ?  17  PHE A CE2 1 
ATOM   50   C CZ  . PHE A 1 9   ? 70.55500  -5.68600  39.20900  1.000 51.41987  ?  17  PHE A CZ  1 
ATOM   51   N N   . ASP A 1 10  ? 73.78300  -7.42200  44.18600  1.000 49.19007  ?  18  ASP A N   1 
ATOM   52   C CA  . ASP A 1 10  ? 72.94300  -8.13900  45.14100  1.000 47.88606  ?  18  ASP A CA  1 
ATOM   53   C C   . ASP A 1 10  ? 72.60700  -7.27000  46.34800  1.000 47.11762  ?  18  ASP A C   1 
ATOM   54   O O   . ASP A 1 10  ? 71.45800  -7.24300  46.80300  1.000 45.92974  ?  18  ASP A O   1 
ATOM   55   C CB  . ASP A 1 10  ? 73.63700  -9.42500  45.59000  1.000 58.75380  ?  18  ASP A CB  1 
ATOM   56   C CG  . ASP A 1 10  ? 73.70000  -10.46800 44.49500  1.000 55.39240  ?  18  ASP A CG  1 
ATOM   57   O OD1 . ASP A 1 10  ? 72.98200  -10.32100 43.48700  1.000 54.20902  ?  18  ASP A OD1 1 
ATOM   58   O OD2 . ASP A 1 10  ? 74.46800  -11.43900 44.64500  1.000 55.81107  -1 18  ASP A OD2 1 
ATOM   59   N N   . THR A 1 11  ? 73.59800  -6.55300  46.88200  1.000 49.13864  ?  19  THR A N   1 
ATOM   60   C CA  . THR A 1 11  ? 73.34300  -5.67000  48.01700  1.000 50.10111  ?  19  THR A CA  1 
ATOM   61   C C   . THR A 1 11  ? 72.47700  -4.48200  47.62000  1.000 47.82843  ?  19  THR A C   1 
ATOM   62   O O   . THR A 1 11  ? 71.70500  -3.97900  48.44400  1.000 41.52615  ?  19  THR A O   1 
ATOM   63   C CB  . THR A 1 11  ? 74.65600  -5.17900  48.62800  1.000 40.83738  ?  19  THR A CB  1 
ATOM   64   O OG1 . THR A 1 11  ? 75.62000  -4.96400  47.59400  1.000 50.80355  ?  19  THR A OG1 1 
ATOM   65   C CG2 . THR A 1 11  ? 75.19800  -6.20000  49.61200  1.000 39.77372  ?  19  THR A CG2 1 
ATOM   66   N N   . LEU A 1 12  ? 72.60200  -4.00700  46.38000  1.000 43.10943  ?  20  LEU A N   1 
ATOM   67   C CA  . LEU A 1 12  ? 71.70300  -2.96500  45.89600  1.000 42.58374  ?  20  LEU A CA  1 
ATOM   68   C C   . LEU A 1 12  ? 70.26700  -3.47100  45.83800  1.000 40.05576  ?  20  LEU A C   1 
ATOM   69   O O   . LEU A 1 12  ? 69.32700  -2.75400  46.19400  1.000 40.47062  ?  20  LEU A O   1 
ATOM   70   C CB  . LEU A 1 12  ? 72.15600  -2.47500  44.52200  1.000 37.87984  ?  20  LEU A CB  1 
ATOM   71   C CG  . LEU A 1 12  ? 71.22900  -1.47000  43.83900  1.000 35.70970  ?  20  LEU A CG  1 
ATOM   72   C CD1 . LEU A 1 12  ? 71.13400  -0.19600  44.65600  1.000 35.63948  ?  20  LEU A CD1 1 
ATOM   73   C CD2 . LEU A 1 12  ? 71.70400  -1.17200  42.43200  1.000 37.21240  ?  20  LEU A CD2 1 
ATOM   74   N N   . MET A 1 13  ? 70.08200  -4.71000  45.38200  1.000 39.57742  ?  21  MET A N   1 
ATOM   75   C CA  . MET A 1 13  ? 68.74100  -5.27900  45.31300  1.000 35.85026  ?  21  MET A CA  1 
ATOM   76   C C   . MET A 1 13  ? 68.17900  -5.54400  46.70300  1.000 34.57633  ?  21  MET A C   1 
ATOM   77   O O   . MET A 1 13  ? 66.96500  -5.46000  46.91600  1.000 37.69922  ?  21  MET A O   1 
ATOM   78   C CB  . MET A 1 13  ? 68.75700  -6.56800  44.49300  1.000 42.07616  ?  21  MET A CB  1 
ATOM   79   C CG  . MET A 1 13  ? 69.07900  -6.38300  43.02300  1.000 44.67781  ?  21  MET A CG  1 
ATOM   80   S SD  . MET A 1 13  ? 67.75700  -5.61300  42.07600  1.000 41.82863  ?  21  MET A SD  1 
ATOM   81   C CE  . MET A 1 13  ? 68.39900  -3.95400  41.90500  1.000 39.43328  ?  21  MET A CE  1 
ATOM   82   N N   . SER A 1 14  ? 69.04700  -5.88100  47.66000  1.000 32.32121  ?  22  SER A N   1 
ATOM   83   C CA  . SER A 1 14  ? 68.57500  -6.23300  48.99500  1.000 35.58722  ?  22  SER A CA  1 
ATOM   84   C C   . SER A 1 14  ? 67.91600  -5.05300  49.69700  1.000 38.39513  ?  22  SER A C   1 
ATOM   85   O O   . SER A 1 14  ? 67.07100  -5.25000  50.57700  1.000 36.85586  ?  22  SER A O   1 
ATOM   86   C CB  . SER A 1 14  ? 69.72900  -6.77200  49.83800  1.000 31.88977  ?  22  SER A CB  1 
ATOM   87   O OG  . SER A 1 14  ? 70.57300  -5.72500  50.27800  1.000 51.27932  ?  22  SER A OG  1 
ATOM   88   N N   . THR A 1 15  ? 68.28800  -3.82400  49.33300  1.000 39.39888  ?  23  THR A N   1 
ATOM   89   C CA  . THR A 1 15  ? 67.63300  -2.65400  49.90600  1.000 42.27085  ?  23  THR A CA  1 
ATOM   90   C C   . THR A 1 15  ? 66.17800  -2.54600  49.47700  1.000 38.32946  ?  23  THR A C   1 
ATOM   91   O O   . THR A 1 15  ? 65.38800  -1.89400  50.16500  1.000 33.21618  ?  23  THR A O   1 
ATOM   92   C CB  . THR A 1 15  ? 68.38000  -1.37800  49.51900  1.000 35.20185  ?  23  THR A CB  1 
ATOM   93   O OG1 . THR A 1 15  ? 68.22400  -1.13300  48.11700  1.000 31.71180  ?  23  THR A OG1 1 
ATOM   94   C CG2 . THR A 1 15  ? 69.85500  -1.51300  49.83900  1.000 41.95597  ?  23  THR A CG2 1 
ATOM   95   N N   . ALA A 1 16  ? 65.81200  -3.16500  48.35700  1.000 31.53749  ?  24  ALA A N   1 
ATOM   96   C CA  . ALA A 1 16  ? 64.43800  -3.20000  47.88100  1.000 31.30817  ?  24  ALA A CA  1 
ATOM   97   C C   . ALA A 1 16  ? 63.77500  -4.55000  48.11100  1.000 35.77135  ?  24  ALA A C   1 
ATOM   98   O O   . ALA A 1 16  ? 62.69500  -4.79800  47.56900  1.000 39.93405  ?  24  ALA A O   1 
ATOM   99   C CB  . ALA A 1 16  ? 64.38400  -2.84000  46.39800  1.000 28.47945  ?  24  ALA A CB  1 
ATOM   100  N N   . GLY A 1 17  ? 64.39800  -5.42800  48.89300  1.000 33.42994  ?  25  GLY A N   1 
ATOM   101  C CA  . GLY A 1 17  ? 63.81000  -6.71900  49.18500  1.000 33.04756  ?  25  GLY A CA  1 
ATOM   102  C C   . GLY A 1 17  ? 63.86800  -7.72000  48.05700  1.000 41.49793  ?  25  GLY A C   1 
ATOM   103  O O   . GLY A 1 17  ? 63.06600  -8.65500  48.03200  1.000 44.84743  ?  25  GLY A O   1 
ATOM   104  N N   . VAL A 1 18  ? 64.79700  -7.55500  47.12200  1.000 35.31908  ?  26  VAL A N   1 
ATOM   105  C CA  . VAL A 1 18  ? 64.92400  -8.44000  45.97100  1.000 37.38925  ?  26  VAL A CA  1 
ATOM   106  C C   . VAL A 1 18  ? 66.11600  -9.35700  46.19900  1.000 38.98203  ?  26  VAL A C   1 
ATOM   107  O O   . VAL A 1 18  ? 67.24600  -8.88800  46.38100  1.000 40.83019  ?  26  VAL A O   1 
ATOM   108  C CB  . VAL A 1 18  ? 65.08200  -7.64300  44.66700  1.000 38.77324  ?  26  VAL A CB  1 
ATOM   109  C CG1 . VAL A 1 18  ? 65.30200  -8.58200  43.50000  1.000 44.46476  ?  26  VAL A CG1 1 
ATOM   110  C CG2 . VAL A 1 18  ? 63.86300  -6.77400  44.42900  1.000 35.59621  ?  26  VAL A CG2 1 
ATOM   111  N N   . ASP A 1 19  ? 65.86900  -10.66500 46.19100  1.000 46.65005  ?  27  ASP A N   1 
ATOM   112  C CA  . ASP A 1 19  ? 66.92900  -11.66000 46.34800  1.000 44.68318  ?  27  ASP A CA  1 
ATOM   113  C C   . ASP A 1 19  ? 67.35200  -12.09300 44.95200  1.000 40.76586  ?  27  ASP A C   1 
ATOM   114  O O   . ASP A 1 19  ? 66.92000  -13.12300 44.43500  1.000 44.40232  ?  27  ASP A O   1 
ATOM   115  C CB  . ASP A 1 19  ? 66.45100  -12.83100 47.19400  1.000 40.98895  ?  27  ASP A CB  1 
ATOM   116  C CG  . ASP A 1 19  ? 67.59100  -13.67100 47.71600  1.000 41.09912  ?  27  ASP A CG  1 
ATOM   117  O OD1 . ASP A 1 19  ? 68.75500  -13.25500 47.55400  1.000 49.84325  ?  27  ASP A OD1 1 
ATOM   118  O OD2 . ASP A 1 19  ? 67.32600  -14.74200 48.29800  1.000 47.20292  -1 27  ASP A OD2 1 
ATOM   119  N N   . SER A 1 20  ? 68.21400  -11.28700 44.33400  1.000 41.77840  ?  28  SER A N   1 
ATOM   120  C CA  . SER A 1 20  ? 68.55200  -11.47000 42.92900  1.000 44.76387  ?  28  SER A CA  1 
ATOM   121  C C   . SER A 1 20  ? 69.46100  -12.66900 42.69200  1.000 45.60458  ?  28  SER A C   1 
ATOM   122  O O   . SER A 1 20  ? 69.35900  -13.31200 41.64200  1.000 43.51141  ?  28  SER A O   1 
ATOM   123  C CB  . SER A 1 20  ? 69.20200  -10.19800 42.38600  1.000 45.49468  ?  28  SER A CB  1 
ATOM   124  O OG  . SER A 1 20  ? 70.26400  -9.77600  43.22000  1.000 45.74468  ?  28  SER A OG  1 
ATOM   125  N N   . GLN A 1 21  ? 70.34800  -12.97700 43.64000  1.000 48.11565  ?  29  GLN A N   1 
ATOM   126  C CA  . GLN A 1 21  ? 71.27700  -14.10300 43.52000  1.000 48.02713  ?  29  GLN A CA  1 
ATOM   127  C C   . GLN A 1 21  ? 72.09600  -14.00900 42.23500  1.000 48.16829  ?  29  GLN A C   1 
ATOM   128  O O   . GLN A 1 21  ? 72.36300  -15.00900 41.56600  1.000 45.84878  ?  29  GLN A O   1 
ATOM   129  C CB  . GLN A 1 21  ? 70.53700  -15.44000 43.59600  1.000 39.90117  ?  29  GLN A CB  1 
ATOM   130  C CG  . GLN A 1 21  ? 69.86200  -15.71600 44.92700  1.000 32.47234  ?  29  GLN A CG  1 
ATOM   131  C CD  . GLN A 1 21  ? 70.84900  -15.94100 46.05000  1.000 35.53272  ?  29  GLN A CD  1 
ATOM   132  O OE1 . GLN A 1 21  ? 71.99100  -16.33300 45.81800  1.000 54.69776  ?  29  GLN A OE1 1 
ATOM   133  N NE2 . GLN A 1 21  ? 70.41100  -15.70400 47.27800  1.000 35.80841  ?  29  GLN A NE2 1 
ATOM   134  N N   . ILE A 1 22  ? 72.49100  -12.78600 41.88200  1.000 43.48488  ?  30  ILE A N   1 
ATOM   135  C CA  . ILE A 1 22  ? 73.25200  -12.57400 40.65500  1.000 49.03368  ?  30  ILE A CA  1 
ATOM   136  C C   . ILE A 1 22  ? 74.65000  -13.16900 40.78100  1.000 48.78558  ?  30  ILE A C   1 
ATOM   137  O O   . ILE A 1 22  ? 75.22000  -13.66100 39.80100  1.000 51.48171  ?  30  ILE A O   1 
ATOM   138  C CB  . ILE A 1 22  ? 73.29100  -11.07500 40.30800  1.000 46.27550  ?  30  ILE A CB  1 
ATOM   139  C CG1 . ILE A 1 22  ? 71.88800  -10.57100 39.98300  1.000 47.31523  ?  30  ILE A CG1 1 
ATOM   140  C CG2 . ILE A 1 22  ? 74.18700  -10.82300 39.11700  1.000 49.69891  ?  30  ILE A CG2 1 
ATOM   141  C CD1 . ILE A 1 22  ? 71.19900  -11.35600 38.89700  1.000 45.94371  ?  30  ILE A CD1 1 
ATOM   142  N N   . ALA A 1 23  ? 75.22600  -13.12800 41.98300  1.000 42.43876  ?  31  ALA A N   1 
ATOM   143  C CA  . ALA A 1 23  ? 76.55900  -13.68700 42.18800  1.000 53.32008  ?  31  ALA A CA  1 
ATOM   144  C C   . ALA A 1 23  ? 76.57400  -15.18800 41.92700  1.000 49.64362  ?  31  ALA A C   1 
ATOM   145  O O   . ALA A 1 23  ? 77.50200  -15.71300 41.30000  1.000 52.22576  ?  31  ALA A O   1 
ATOM   146  C CB  . ALA A 1 23  ? 77.04000  -13.38100 43.60600  1.000 52.82921  ?  31  ALA A CB  1 
ATOM   147  N N   . ALA A 1 24  ? 75.55200  -15.89800 42.40700  1.000 48.23764  ?  32  ALA A N   1 
ATOM   148  C CA  . ALA A 1 24  ? 75.47500  -17.33500 42.17000  1.000 49.86230  ?  32  ALA A CA  1 
ATOM   149  C C   . ALA A 1 24  ? 75.30600  -17.64200 40.68800  1.000 53.60146  ?  32  ALA A C   1 
ATOM   150  O O   . ALA A 1 24  ? 75.91100  -18.58700 40.16900  1.000 56.40693  ?  32  ALA A O   1 
ATOM   151  C CB  . ALA A 1 24  ? 74.33100  -17.94100 42.98000  1.000 43.81455  ?  32  ALA A CB  1 
ATOM   152  N N   . LEU A 1 25  ? 74.48100  -16.85800 39.99100  1.000 48.26603  ?  33  LEU A N   1 
ATOM   153  C CA  . LEU A 1 25  ? 74.29600  -17.07100 38.55900  1.000 50.37859  ?  33  LEU A CA  1 
ATOM   154  C C   . LEU A 1 25  ? 75.58400  -16.80500 37.79200  1.000 52.03015  ?  33  LEU A C   1 
ATOM   155  O O   . LEU A 1 25  ? 75.89300  -17.50400 36.82100  1.000 57.06278  ?  33  LEU A O   1 
ATOM   156  C CB  . LEU A 1 25  ? 73.16600  -16.18500 38.03700  1.000 49.35896  ?  33  LEU A CB  1 
ATOM   157  C CG  . LEU A 1 25  ? 72.39500  -16.73600 36.83700  1.000 48.83703  ?  33  LEU A CG  1 
ATOM   158  C CD1 . LEU A 1 25  ? 71.97400  -18.17400 37.08300  1.000 53.85958  ?  33  LEU A CD1 1 
ATOM   159  C CD2 . LEU A 1 25  ? 71.18900  -15.87200 36.53400  1.000 51.49499  ?  33  LEU A CD2 1 
ATOM   160  N N   . ALA A 1 26  ? 76.34000  -15.78500 38.20000  1.000 49.24154  ?  34  ALA A N   1 
ATOM   161  C CA  . ALA A 1 26  ? 77.62600  -15.52200 37.56600  1.000 53.24916  ?  34  ALA A CA  1 
ATOM   162  C C   . ALA A 1 26  ? 78.60800  -16.65600 37.82600  1.000 59.43864  ?  34  ALA A C   1 
ATOM   163  O O   . ALA A 1 26  ? 79.36200  -17.05300 36.93000  1.000 58.35309  ?  34  ALA A O   1 
ATOM   164  C CB  . ALA A 1 26  ? 78.19600  -14.19500 38.06300  1.000 50.71914  ?  34  ALA A CB  1 
ATOM   165  N N   . ALA A 1 27  ? 78.61700  -17.18700 39.05000  1.000 55.89354  ?  35  ALA A N   1 
ATOM   166  C CA  . ALA A 1 27  ? 79.51900  -18.28800 39.36800  1.000 49.12296  ?  35  ALA A CA  1 
ATOM   167  C C   . ALA A 1 27  ? 79.13700  -19.56200 38.62700  1.000 60.86109  ?  35  ALA A C   1 
ATOM   168  O O   . ALA A 1 27  ? 79.99500  -20.42100 38.39600  1.000 69.13679  ?  35  ALA A O   1 
ATOM   169  C CB  . ALA A 1 27  ? 79.54000  -18.53400 40.87500  1.000 49.87680  ?  35  ALA A CB  1 
ATOM   170  N N   . SER A 1 28  ? 77.87000  -19.70300 38.24300  1.000 62.95182  ?  36  SER A N   1 
ATOM   171  C CA  . SER A 1 28  ? 77.42200  -20.89200 37.53000  1.000 59.71088  ?  36  SER A CA  1 
ATOM   172  C C   . SER A 1 28  ? 77.78500  -20.86400 36.05300  1.000 62.41652  ?  36  SER A C   1 
ATOM   173  O O   . SER A 1 28  ? 77.42000  -21.79700 35.32800  1.000 66.04093  ?  36  SER A O   1 
ATOM   174  C CB  . SER A 1 28  ? 75.90800  -21.06600 37.68000  1.000 54.39171  ?  36  SER A CB  1 
ATOM   175  O OG  . SER A 1 28  ? 75.20100  -20.17500 36.83900  1.000 55.49278  ?  36  SER A OG  1 
ATOM   176  N N   . GLU A 1 29  ? 78.48100  -19.82100 35.59700  1.000 61.27340  ?  37  GLU A N   1 
ATOM   177  C CA  . GLU A 1 29  ? 78.94400  -19.71200 34.21400  1.000 63.57475  ?  37  GLU A CA  1 
ATOM   178  C C   . GLU A 1 29  ? 77.77700  -19.73600 33.23000  1.000 59.83787  ?  37  GLU A C   1 
ATOM   179  O O   . GLU A 1 29  ? 77.87200  -20.29800 32.13800  1.000 61.22200  ?  37  GLU A O   1 
ATOM   180  C CB  . GLU A 1 29  ? 79.95800  -20.81000 33.88500  1.000 63.09462  ?  37  GLU A CB  1 
ATOM   181  C CG  . GLU A 1 29  ? 81.23700  -20.72600 34.69900  1.000 68.81473  ?  37  GLU A CG  1 
ATOM   182  C CD  . GLU A 1 29  ? 82.20500  -21.84200 34.37700  1.000 71.08292  ?  37  GLU A CD  1 
ATOM   183  O OE1 . GLU A 1 29  ? 81.76700  -22.85800 33.80000  1.000 75.96176  ?  37  GLU A OE1 1 
ATOM   184  O OE2 . GLU A 1 29  ? 83.40200  -21.70300 34.70100  1.000 68.79991  -1 37  GLU A OE2 1 
ATOM   185  N N   . ALA A 1 30  ? 76.66400  -19.12400 33.62400  1.000 55.63672  ?  38  ALA A N   1 
ATOM   186  C CA  . ALA A 1 30  ? 75.53100  -18.99100 32.72100  1.000 56.40538  ?  38  ALA A CA  1 
ATOM   187  C C   . ALA A 1 30  ? 75.86800  -18.02100 31.59800  1.000 51.37533  ?  38  ALA A C   1 
ATOM   188  O O   . ALA A 1 30  ? 76.66100  -17.09200 31.76700  1.000 59.16241  ?  38  ALA A O   1 
ATOM   189  C CB  . ALA A 1 30  ? 74.29500  -18.50900 33.48000  1.000 62.14916  ?  38  ALA A CB  1 
ATOM   190  N N   . ASP A 1 31  ? 75.25300  -18.24200 30.43900  1.000 53.84943  ?  39  ASP A N   1 
ATOM   191  C CA  . ASP A 1 31  ? 75.53400  -17.40300 29.28700  1.000 60.25940  ?  39  ASP A CA  1 
ATOM   192  C C   . ASP A 1 31  ? 75.04600  -15.97900 29.53300  1.000 62.75796  ?  39  ASP A C   1 
ATOM   193  O O   . ASP A 1 31  ? 74.30900  -15.69900 30.48200  1.000 59.12108  ?  39  ASP A O   1 
ATOM   194  C CB  . ASP A 1 31  ? 74.89000  -17.97300 28.02200  1.000 46.23846  ?  39  ASP A CB  1 
ATOM   195  C CG  . ASP A 1 31  ? 73.38000  -17.99700 28.09300  1.000 60.04522  ?  39  ASP A CG  1 
ATOM   196  O OD1 . ASP A 1 31  ? 72.83700  -18.67900 28.98400  1.000 66.33922  ?  39  ASP A OD1 1 
ATOM   197  O OD2 . ASP A 1 31  ? 72.73400  -17.33700 27.25200  1.000 63.86995  -1 39  ASP A OD2 1 
ATOM   198  N N   . ALA A 1 32  ? 75.47900  -15.07000 28.65800  1.000 67.66260  ?  40  ALA A N   1 
ATOM   199  C CA  . ALA A 1 32  ? 75.21800  -13.65300 28.87900  1.000 65.30061  ?  40  ALA A CA  1 
ATOM   200  C C   . ALA A 1 32  ? 73.72500  -13.35600 28.90500  1.000 70.80209  ?  40  ALA A C   1 
ATOM   201  O O   . ALA A 1 32  ? 73.24900  -12.65400 29.80100  1.000 68.45259  ?  40  ALA A O   1 
ATOM   202  C CB  . ALA A 1 32  ? 75.91200  -12.82000 27.80300  1.000 59.70634  ?  40  ALA A CB  1 
ATOM   203  N N   . GLY A 1 33  ? 72.96600  -13.91700 27.96200  1.000 70.78293  ?  41  GLY A N   1 
ATOM   204  C CA  . GLY A 1 33  ? 71.55000  -13.59100 27.87500  1.000 67.06171  ?  41  GLY A CA  1 
ATOM   205  C C   . GLY A 1 33  ? 70.79300  -13.88700 29.15600  1.000 62.71684  ?  41  GLY A C   1 
ATOM   206  O O   . GLY A 1 33  ? 69.96700  -13.08500 29.59800  1.000 58.24210  ?  41  GLY A O   1 
ATOM   207  N N   . THR A 1 34  ? 71.07400  -15.03600 29.77400  1.000 60.65087  ?  42  THR A N   1 
ATOM   208  C CA  . THR A 1 34  ? 70.41800  -15.38100 31.03100  1.000 62.33886  ?  42  THR A CA  1 
ATOM   209  C C   . THR A 1 34  ? 70.75300  -14.37700 32.12500  1.000 64.88347  ?  42  THR A C   1 
ATOM   210  O O   . THR A 1 34  ? 69.87500  -13.97400 32.89800  1.000 70.22647  ?  42  THR A O   1 
ATOM   211  C CB  . THR A 1 34  ? 70.81700  -16.79300 31.46200  1.000 59.95640  ?  42  THR A CB  1 
ATOM   212  O OG1 . THR A 1 34  ? 70.64900  -17.69600 30.36300  1.000 64.71786  ?  42  THR A OG1 1 
ATOM   213  C CG2 . THR A 1 34  ? 69.96300  -17.25800 32.62700  1.000 64.43439  ?  42  THR A CG2 1 
ATOM   214  N N   . LEU A 1 35  ? 72.01700  -13.96200 32.21000  1.000 63.01714  ?  43  LEU A N   1 
ATOM   215  C CA  . LEU A 1 35  ? 72.41000  -13.01900 33.25100  1.000 61.03070  ?  43  LEU A CA  1 
ATOM   216  C C   . LEU A 1 35  ? 71.77900  -11.64800 33.03200  1.000 57.90385  ?  43  LEU A C   1 
ATOM   217  O O   . LEU A 1 35  ? 71.31200  -11.02100 33.98800  1.000 49.93347  ?  43  LEU A O   1 
ATOM   218  C CB  . LEU A 1 35  ? 73.93100  -12.91300 33.31600  1.000 51.11091  ?  43  LEU A CB  1 
ATOM   219  C CG  . LEU A 1 35  ? 74.60200  -13.68900 34.45000  1.000 48.94878  ?  43  LEU A CG  1 
ATOM   220  C CD1 . LEU A 1 35  ? 76.10700  -13.51800 34.39100  1.000 55.94768  ?  43  LEU A CD1 1 
ATOM   221  C CD2 . LEU A 1 35  ? 74.06300  -13.25500 35.80100  1.000 43.61925  ?  43  LEU A CD2 1 
ATOM   222  N N   . ASP A 1 36  ? 71.75800  -11.16100 31.78600  1.000 52.71156  ?  44  ASP A N   1 
ATOM   223  C CA  . ASP A 1 36  ? 71.06700  -9.90500  31.50300  1.000 45.85665  ?  44  ASP A CA  1 
ATOM   224  C C   . ASP A 1 36  ? 69.58400  -9.99800  31.82900  1.000 56.14594  ?  44  ASP A C   1 
ATOM   225  O O   . ASP A 1 36  ? 69.01000  -9.06000  32.39200  1.000 59.44800  ?  44  ASP A O   1 
ATOM   226  C CB  . ASP A 1 36  ? 71.25900  -9.47500  30.04400  1.000 47.91944  ?  44  ASP A CB  1 
ATOM   227  C CG  . ASP A 1 36  ? 72.71700  -9.32500  29.64600  1.000 56.71930  ?  44  ASP A CG  1 
ATOM   228  O OD1 . ASP A 1 36  ? 73.55000  -10.17400 29.99200  1.000 64.29169  ?  44  ASP A OD1 1 
ATOM   229  O OD2 . ASP A 1 36  ? 73.02900  -8.34300  28.94500  1.000 62.58857  -1 44  ASP A OD2 1 
ATOM   230  N N   . ALA A 1 37  ? 68.94200  -11.11500 31.48000  1.000 59.96546  ?  45  ALA A N   1 
ATOM   231  C CA  . ALA A 1 37  ? 67.52600  -11.26900 31.79100  1.000 51.40534  ?  45  ALA A CA  1 
ATOM   232  C C   . ALA A 1 37  ? 67.28700  -11.25000 33.29400  1.000 49.69579  ?  45  ALA A C   1 
ATOM   233  O O   . ALA A 1 37  ? 66.35400  -10.59400 33.77300  1.000 51.44764  ?  45  ALA A O   1 
ATOM   234  C CB  . ALA A 1 37  ? 66.99100  -12.56100 31.17700  1.000 51.60558  ?  45  ALA A CB  1 
ATOM   235  N N   . ALA A 1 38  ? 68.12500  -11.95700 34.05500  1.000 52.19437  ?  46  ALA A N   1 
ATOM   236  C CA  . ALA A 1 38  ? 67.96800  -11.98300 35.50600  1.000 53.98973  ?  46  ALA A CA  1 
ATOM   237  C C   . ALA A 1 38  ? 68.19900  -10.60600 36.11300  1.000 49.68945  ?  46  ALA A C   1 
ATOM   238  O O   . ALA A 1 38  ? 67.44900  -10.17600 36.99800  1.000 47.06072  ?  46  ALA A O   1 
ATOM   239  C CB  . ALA A 1 38  ? 68.92300  -13.00600 36.11700  1.000 46.20442  ?  46  ALA A CB  1 
ATOM   240  N N   . LEU A 1 39  ? 69.23200  -9.89900  35.65100  1.000 54.67880  ?  47  LEU A N   1 
ATOM   241  C CA  . LEU A 1 39  ? 69.50200  -8.55500  36.14800  1.000 50.76660  ?  47  LEU A CA  1 
ATOM   242  C C   . LEU A 1 39  ? 68.33300  -7.62600  35.85700  1.000 49.05025  ?  47  LEU A C   1 
ATOM   243  O O   . LEU A 1 39  ? 67.89800  -6.86200  36.72600  1.000 46.32570  ?  47  LEU A O   1 
ATOM   244  C CB  . LEU A 1 39  ? 70.78300  -8.01400  35.51200  1.000 43.14054  ?  47  LEU A CB  1 
ATOM   245  C CG  . LEU A 1 39  ? 72.11900  -8.62000  35.93900  1.000 46.42391  ?  47  LEU A CG  1 
ATOM   246  C CD1 . LEU A 1 39  ? 73.17400  -8.35800  34.88300  1.000 44.86883  ?  47  LEU A CD1 1 
ATOM   247  C CD2 . LEU A 1 39  ? 72.55900  -8.06000  37.27000  1.000 46.46889  ?  47  LEU A CD2 1 
ATOM   248  N N   . THR A 1 40  ? 67.80700  -7.68600  34.63100  1.000 46.49253  ?  48  THR A N   1 
ATOM   249  C CA  . THR A 1 40  ? 66.68800  -6.83200  34.25900  1.000 45.16713  ?  48  THR A CA  1 
ATOM   250  C C   . THR A 1 40  ? 65.46200  -7.13400  35.10500  1.000 47.10348  ?  48  THR A C   1 
ATOM   251  O O   . THR A 1 40  ? 64.80600  -6.21400  35.60200  1.000 48.65478  ?  48  THR A O   1 
ATOM   252  C CB  . THR A 1 40  ? 66.37000  -7.00600  32.77400  1.000 46.34935  ?  48  THR A CB  1 
ATOM   253  O OG1 . THR A 1 40  ? 67.49600  -6.59200  31.99300  1.000 55.64014  ?  48  THR A OG1 1 
ATOM   254  C CG2 . THR A 1 40  ? 65.16000  -6.17800  32.38400  1.000 36.95547  ?  48  THR A CG2 1 
ATOM   255  N N   . GLN A 1 41  ? 65.18100  -8.40800  35.32500  1.000 50.59126  ?  49  GLN A N   1 
ATOM   256  C CA  . GLN A 1 41  ? 63.96100  -8.76000  36.08600  1.000 47.71722  ?  49  GLN A CA  1 
ATOM   257  C C   . GLN A 1 41  ? 64.13800  -8.28400  37.53100  1.000 48.55929  ?  49  GLN A C   1 
ATOM   258  O O   . GLN A 1 41  ? 63.19700  -7.69000  38.07900  1.000 49.79716  ?  49  GLN A O   1 
ATOM   259  C CB  . GLN A 1 41  ? 63.68700  -10.25900 36.03500  1.000 43.59155  ?  49  GLN A CB  1 
ATOM   260  C CG  . GLN A 1 41  ? 62.22900  -10.60600 35.76300  1.000 56.46013  ?  49  GLN A CG  1 
ATOM   261  C CD  . GLN A 1 41  ? 61.43500  -10.85400 37.02500  1.000 64.92670  ?  49  GLN A CD  1 
ATOM   262  O OE1 . GLN A 1 41  ? 61.66800  -11.82600 37.75000  1.000 68.69924  ?  49  GLN A OE1 1 
ATOM   263  N NE2 . GLN A 1 41  ? 60.49000  -9.96800  37.30300  1.000 58.69842  ?  49  GLN A NE2 1 
ATOM   264  N N   . SER A 1 42  ? 65.30200  -8.53800  38.11800  1.000 45.15048  ?  50  SER A N   1 
ATOM   265  C CA  . SER A 1 42  ? 65.52100  -8.13200  39.50200  1.000 45.67047  ?  50  SER A CA  1 
ATOM   266  C C   . SER A 1 42  ? 65.42900  -6.62000  39.65700  1.000 46.02120  ?  50  SER A C   1 
ATOM   267  O O   . SER A 1 42  ? 64.82200  -6.12100  40.61100  1.000 43.74957  ?  50  SER A O   1 
ATOM   268  C CB  . SER A 1 42  ? 66.87800  -8.63900  39.98700  1.000 46.24619  ?  50  SER A CB  1 
ATOM   269  O OG  . SER A 1 42  ? 66.92300  -10.05300 39.98500  1.000 47.73704  ?  50  SER A OG  1 
ATOM   270  N N   . LEU A 1 43  ? 66.01700  -5.87200  38.72400  1.000 45.70060  ?  51  LEU A N   1 
ATOM   271  C CA  . LEU A 1 43  ? 66.02200  -4.42000  38.85100  1.000 44.75222  ?  51  LEU A CA  1 
ATOM   272  C C   . LEU A 1 43  ? 64.63100  -3.84400  38.59900  1.000 40.30713  ?  51  LEU A C   1 
ATOM   273  O O   . LEU A 1 43  ? 64.23100  -2.86800  39.24200  1.000 41.21814  ?  51  LEU A O   1 
ATOM   274  C CB  . LEU A 1 43  ? 67.07200  -3.83400  37.90200  1.000 43.34726  ?  51  LEU A CB  1 
ATOM   275  C CG  . LEU A 1 43  ? 67.28300  -2.33300  37.67500  1.000 41.18259  ?  51  LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 43  ? 66.34500  -1.78900  36.62800  1.000 40.29833  ?  51  LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 43  ? 67.16200  -1.55400  38.97600  1.000 39.33897  ?  51  LEU A CD2 1 
ATOM   278  N N   . GLN A 1 44  ? 63.86900  -4.44800  37.68300  1.000 36.21830  ?  52  GLN A N   1 
ATOM   279  C CA  . GLN A 1 44  ? 62.48500  -4.03200  37.47800  1.000 39.68110  ?  52  GLN A CA  1 
ATOM   280  C C   . GLN A 1 44  ? 61.63800  -4.32400  38.70800  1.000 40.30499  ?  52  GLN A C   1 
ATOM   281  O O   . GLN A 1 44  ? 60.73300  -3.55400  39.04900  1.000 32.75381  ?  52  GLN A O   1 
ATOM   282  C CB  . GLN A 1 44  ? 61.90600  -4.73100  36.24900  1.000 31.46342  ?  52  GLN A CB  1 
ATOM   283  C CG  . GLN A 1 44  ? 62.52900  -4.29100  34.94300  1.000 42.48893  ?  52  GLN A CG  1 
ATOM   284  C CD  . GLN A 1 44  ? 61.50900  -3.90300  33.89900  1.000 49.74072  ?  52  GLN A CD  1 
ATOM   285  O OE1 . GLN A 1 44  ? 61.08900  -4.72900  33.09100  1.000 44.90919  ?  52  GLN A OE1 1 
ATOM   286  N NE2 . GLN A 1 44  ? 61.10800  -2.63700  33.90500  1.000 44.08783  ?  52  GLN A NE2 1 
ATOM   287  N N   . GLU A 1 45  ? 61.90300  -5.45000  39.37300  1.000 40.51490  ?  53  GLU A N   1 
ATOM   288  C CA  . GLU A 1 45  ? 61.22500  -5.75300  40.62800  1.000 39.89965  ?  53  GLU A CA  1 
ATOM   289  C C   . GLU A 1 45  ? 61.57800  -4.73200  41.70400  1.000 36.37322  ?  53  GLU A C   1 
ATOM   290  O O   . GLU A 1 45  ? 60.71600  -4.31900  42.48700  1.000 34.75877  ?  53  GLU A O   1 
ATOM   291  C CB  . GLU A 1 45  ? 61.59800  -7.16500  41.07700  1.000 43.88133  ?  53  GLU A CB  1 
ATOM   292  C CG  . GLU A 1 45  ? 60.78500  -7.71700  42.22600  1.000 47.99839  ?  53  GLU A CG  1 
ATOM   293  C CD  . GLU A 1 45  ? 61.14200  -9.15600  42.53100  1.000 54.17743  ?  53  GLU A CD  1 
ATOM   294  O OE1 . GLU A 1 45  ? 61.53300  -9.88100  41.59300  1.000 48.48892  ?  53  GLU A OE1 1 
ATOM   295  O OE2 . GLU A 1 45  ? 61.04200  -9.56100  43.70700  1.000 50.68265  -1 53  GLU A OE2 1 
ATOM   296  N N   . ALA A 1 46  ? 62.84600  -4.32100  41.75800  1.000 35.71660  ?  54  ALA A N   1 
ATOM   297  C CA  . ALA A 1 46  ? 63.28500  -3.37700  42.78200  1.000 35.69410  ?  54  ALA A CA  1 
ATOM   298  C C   . ALA A 1 46  ? 62.76000  -1.97200  42.51400  1.000 33.93458  ?  54  ALA A C   1 
ATOM   299  O O   . ALA A 1 46  ? 62.57600  -1.18200  43.44700  1.000 28.65227  ?  54  ALA A O   1 
ATOM   300  C CB  . ALA A 1 46  ? 64.81000  -3.37000  42.86300  1.000 33.16902  ?  54  ALA A CB  1 
ATOM   301  N N   . GLN A 1 47  ? 62.53900  -1.63400  41.24300  1.000 33.67684  ?  55  GLN A N   1 
ATOM   302  C CA  . GLN A 1 47  ? 62.05700  -0.29900  40.90700  1.000 30.17850  ?  55  GLN A CA  1 
ATOM   303  C C   . GLN A 1 47  ? 60.66400  -0.05100  41.46900  1.000 33.05917  ?  55  GLN A C   1 
ATOM   304  O O   . GLN A 1 47  ? 60.33800  1.07200   41.86700  1.000 38.59762  ?  55  GLN A O   1 
ATOM   305  C CB  . GLN A 1 47  ? 62.07100  -0.10400  39.39200  1.000 29.43302  ?  55  GLN A CB  1 
ATOM   306  C CG  . GLN A 1 47  ? 63.43000  0.27100   38.84000  1.000 36.81875  ?  55  GLN A CG  1 
ATOM   307  C CD  . GLN A 1 47  ? 63.84400  1.67600   39.22400  1.000 40.03051  ?  55  GLN A CD  1 
ATOM   308  O OE1 . GLN A 1 47  ? 63.02800  2.59600   39.22700  1.000 40.88839  ?  55  GLN A OE1 1 
ATOM   309  N NE2 . GLN A 1 47  ? 65.11300  1.84600   39.56100  1.000 37.98835  ?  55  GLN A NE2 1 
ATOM   310  N N   . GLY A 1 48  ? 59.82700  -1.08500  41.50700  1.000 38.56106  ?  56  GLY A N   1 
ATOM   311  C CA  . GLY A 1 48  ? 58.50700  -0.94600  42.08700  1.000 32.37878  ?  56  GLY A CA  1 
ATOM   312  C C   . GLY A 1 48  ? 58.49600  -0.85100  43.59600  1.000 36.78964  ?  56  GLY A C   1 
ATOM   313  O O   . GLY A 1 48  ? 57.45700  -0.51000  44.17000  1.000 41.06453  ?  56  GLY A O   1 
ATOM   314  N N   . ARG A 1 49  ? 59.62000  -1.13800  44.24700  1.000 30.81169  ?  57  ARG A N   1 
ATOM   315  C CA  . ARG A 1 49  ? 59.73800  -1.02700  45.69300  1.000 32.79463  ?  57  ARG A CA  1 
ATOM   316  C C   . ARG A 1 49  ? 60.49900  0.20500   46.14500  1.000 34.89753  ?  57  ARG A C   1 
ATOM   317  O O   . ARG A 1 49  ? 60.27000  0.68000   47.25800  1.000 30.19069  ?  57  ARG A O   1 
ATOM   318  C CB  . ARG A 1 49  ? 60.42400  -2.27100  46.26700  1.000 38.26897  ?  57  ARG A CB  1 
ATOM   319  C CG  . ARG A 1 49  ? 59.66600  -3.55700  46.01500  1.000 41.54988  ?  57  ARG A CG  1 
ATOM   320  C CD  . ARG A 1 49  ? 59.40700  -4.31900  47.29900  1.000 35.32826  ?  57  ARG A CD  1 
ATOM   321  N NE  . ARG A 1 49  ? 58.82800  -5.63000  47.03700  1.000 40.91843  ?  57  ARG A NE  1 
ATOM   322  C CZ  . ARG A 1 49  ? 59.49800  -6.66700  46.55500  1.000 35.90953  ?  57  ARG A CZ  1 
ATOM   323  N NH1 . ARG A 1 49  ? 60.78800  -6.59100  46.28000  1.000 35.50936  ?  57  ARG A NH1 1 
ATOM   324  N NH2 . ARG A 1 49  ? 58.85700  -7.81200  46.34400  1.000 39.51568  ?  57  ARG A NH2 1 
ATOM   325  N N   . TRP A 1 50  ? 61.39800  0.73200   45.31200  1.000 37.88492  ?  58  TRP A N   1 
ATOM   326  C CA  . TRP A 1 50  ? 62.14800  1.92500   45.68500  1.000 33.03950  ?  58  TRP A CA  1 
ATOM   327  C C   . TRP A 1 50  ? 61.27500  3.17000   45.74000  1.000 39.98975  ?  58  TRP A C   1 
ATOM   328  O O   . TRP A 1 50  ? 61.66900  4.16000   46.36500  1.000 42.58317  ?  58  TRP A O   1 
ATOM   329  C CB  . TRP A 1 50  ? 63.30400  2.14700   44.71000  1.000 32.55866  ?  58  TRP A CB  1 
ATOM   330  C CG  . TRP A 1 50  ? 64.49800  1.30000   45.00100  1.000 29.69442  ?  58  TRP A CG  1 
ATOM   331  C CD1 . TRP A 1 50  ? 64.86900  0.79700   46.21000  1.000 30.39901  ?  58  TRP A CD1 1 
ATOM   332  C CD2 . TRP A 1 50  ? 65.48400  0.86100   44.06400  1.000 27.20378  ?  58  TRP A CD2 1 
ATOM   333  N NE1 . TRP A 1 50  ? 66.02300  0.06800   46.08700  1.000 26.08002  ?  58  TRP A NE1 1 
ATOM   334  C CE2 . TRP A 1 50  ? 66.42200  0.09200   44.77700  1.000 24.93909  ?  58  TRP A CE2 1 
ATOM   335  C CE3 . TRP A 1 50  ? 65.66300  1.03900   42.69100  1.000 27.53304  ?  58  TRP A CE3 1 
ATOM   336  C CZ2 . TRP A 1 50  ? 67.52100  -0.49400  44.16500  1.000 23.69800  ?  58  TRP A CZ2 1 
ATOM   337  C CZ3 . TRP A 1 50  ? 66.75400  0.45700   42.08600  1.000 27.29158  ?  58  TRP A CZ3 1 
ATOM   338  C CH2 . TRP A 1 50  ? 67.67000  -0.30000  42.82100  1.000 31.15598  ?  58  TRP A CH2 1 
ATOM   339  N N   . GLY A 1 51  ? 60.10800  3.14300   45.10700  1.000 36.06708  ?  59  GLY A N   1 
ATOM   340  C CA  . GLY A 1 51  ? 59.18900  4.26700   45.14700  1.000 29.04150  ?  59  GLY A CA  1 
ATOM   341  C C   . GLY A 1 51  ? 59.67400  5.51900   44.45100  1.000 31.95510  ?  59  GLY A C   1 
ATOM   342  O O   . GLY A 1 51  ? 59.36100  6.63000   44.89600  1.000 37.90278  ?  59  GLY A O   1 
ATOM   343  N N   . LEU A 1 52  ? 60.42300  5.37100   43.36100  1.000 37.26874  ?  60  LEU A N   1 
ATOM   344  C CA  . LEU A 1 52  ? 60.85900  6.51300   42.57100  1.000 36.48008  ?  60  LEU A CA  1 
ATOM   345  C C   . LEU A 1 52  ? 59.79000  7.00800   41.61000  1.000 34.99237  ?  60  LEU A C   1 
ATOM   346  O O   . LEU A 1 52  ? 59.93400  8.10300   41.05800  1.000 33.71752  ?  60  LEU A O   1 
ATOM   347  C CB  . LEU A 1 52  ? 62.12500  6.16500   41.78200  1.000 35.76491  ?  60  LEU A CB  1 
ATOM   348  C CG  . LEU A 1 52  ? 63.31800  5.64200   42.58000  1.000 38.50504  ?  60  LEU A CG  1 
ATOM   349  C CD1 . LEU A 1 52  ? 64.48100  5.34500   41.65600  1.000 30.35389  ?  60  LEU A CD1 1 
ATOM   350  C CD2 . LEU A 1 52  ? 63.72600  6.62600   43.66100  1.000 34.15068  ?  60  LEU A CD2 1 
ATOM   351  N N   . GLY A 1 53  ? 58.72700  6.23800   41.40600  1.000 38.21400  ?  61  GLY A N   1 
ATOM   352  C CA  . GLY A 1 53  ? 57.66800  6.62200   40.49000  1.000 35.68527  ?  61  GLY A CA  1 
ATOM   353  C C   . GLY A 1 53  ? 58.07500  6.65300   39.03500  1.000 33.64933  ?  61  GLY A C   1 
ATOM   354  O O   . GLY A 1 53  ? 57.68600  7.57300   38.30600  1.000 43.63624  ?  61  GLY A O   1 
ATOM   355  N N   . LEU A 1 54  ? 58.84400  5.66600   38.59200  1.000 35.01915  ?  62  LEU A N   1 
ATOM   356  C CA  . LEU A 1 54  ? 59.32300  5.58400   37.21800  1.000 41.80869  ?  62  LEU A CA  1 
ATOM   357  C C   . LEU A 1 54  ? 58.67400  4.41900   36.47500  1.000 41.61481  ?  62  LEU A C   1 
ATOM   358  O O   . LEU A 1 54  ? 59.31600  3.73600   35.67800  1.000 40.14322  ?  62  LEU A O   1 
ATOM   359  C CB  . LEU A 1 54  ? 60.84300  5.46500   37.18900  1.000 46.35992  ?  62  LEU A CB  1 
ATOM   360  C CG  . LEU A 1 54  ? 61.59800  6.60000   37.88400  1.000 43.44937  ?  62  LEU A CG  1 
ATOM   361  C CD1 . LEU A 1 54  ? 63.08000  6.29200   37.96200  1.000 36.44412  ?  62  LEU A CD1 1 
ATOM   362  C CD2 . LEU A 1 54  ? 61.36300  7.91300   37.16200  1.000 33.99839  ?  62  LEU A CD2 1 
ATOM   363  N N   . HIS A 1 55  ? 57.38600  4.18500   36.73700  1.000 45.04552  ?  63  HIS A N   1 
ATOM   364  C CA  . HIS A 1 55  ? 56.67800  3.08600   36.08900  1.000 36.88878  ?  63  HIS A CA  1 
ATOM   365  C C   . HIS A 1 55  ? 56.52700  3.31300   34.59200  1.000 32.73342  ?  63  HIS A C   1 
ATOM   366  O O   . HIS A 1 55  ? 56.40000  2.35000   33.82900  1.000 36.30539  ?  63  HIS A O   1 
ATOM   367  C CB  . HIS A 1 55  ? 55.30500  2.89700   36.73000  1.000 31.44705  ?  63  HIS A CB  1 
ATOM   368  C CG  . HIS A 1 55  ? 55.35500  2.63300   38.20100  1.000 29.13207  ?  63  HIS A CG  1 
ATOM   369  N ND1 . HIS A 1 55  ? 54.75400  3.45800   39.12600  1.000 30.01026  ?  63  HIS A ND1 1 
ATOM   370  C CD2 . HIS A 1 55  ? 55.93400  1.63500   38.90900  1.000 29.26940  ?  63  HIS A CD2 1 
ATOM   371  C CE1 . HIS A 1 55  ? 54.95900  2.98000   40.33900  1.000 26.47709  ?  63  HIS A CE1 1 
ATOM   372  N NE2 . HIS A 1 55  ? 55.67300  1.87500   40.23600  1.000 30.59529  ?  63  HIS A NE2 1 
ATOM   373  N N   . HIS A 1 56  ? 56.53300  4.57100   34.15800  1.000 38.12187  ?  64  HIS A N   1 
ATOM   374  C CA  . HIS A 1 56  ? 56.39500  4.91500   32.75000  1.000 40.22833  ?  64  HIS A CA  1 
ATOM   375  C C   . HIS A 1 56  ? 57.67500  4.69500   31.95300  1.000 42.28026  ?  64  HIS A C   1 
ATOM   376  O O   . HIS A 1 56  ? 57.64300  4.79500   30.72300  1.000 45.29006  ?  64  HIS A O   1 
ATOM   377  C CB  . HIS A 1 56  ? 55.94100  6.37100   32.62000  1.000 38.98431  ?  64  HIS A CB  1 
ATOM   378  C CG  . HIS A 1 56  ? 56.83600  7.34700   33.31800  1.000 42.33353  ?  64  HIS A CG  1 
ATOM   379  N ND1 . HIS A 1 56  ? 56.92500  7.42400   34.69100  1.000 42.14726  ?  64  HIS A ND1 1 
ATOM   380  C CD2 . HIS A 1 56  ? 57.67000  8.29700   32.83400  1.000 42.59603  ?  64  HIS A CD2 1 
ATOM   381  C CE1 . HIS A 1 56  ? 57.78600  8.36900   35.02200  1.000 41.70302  ?  64  HIS A CE1 1 
ATOM   382  N NE2 . HIS A 1 56  ? 58.25200  8.91400   33.91400  1.000 43.92139  ?  64  HIS A NE2 1 
ATOM   383  N N   . LEU A 1 57  ? 58.78700  4.39900   32.61500  1.000 38.23189  ?  65  LEU A N   1 
ATOM   384  C CA  . LEU A 1 57  ? 60.05400  4.13600   31.95300  1.000 42.33771  ?  65  LEU A CA  1 
ATOM   385  C C   . LEU A 1 57  ? 60.36900  2.64700   31.96700  1.000 48.28063  ?  65  LEU A C   1 
ATOM   386  O O   . LEU A 1 57  ? 60.00200  1.92200   32.89400  1.000 43.75393  ?  65  LEU A O   1 
ATOM   387  C CB  . LEU A 1 57  ? 61.19200  4.90800   32.62100  1.000 50.94922  ?  65  LEU A CB  1 
ATOM   388  C CG  . LEU A 1 57  ? 60.96100  6.38900   32.90500  1.000 49.91017  ?  65  LEU A CG  1 
ATOM   389  C CD1 . LEU A 1 57  ? 62.22300  7.01300   33.45300  1.000 51.67848  ?  65  LEU A CD1 1 
ATOM   390  C CD2 . LEU A 1 57  ? 60.54700  7.09000   31.62900  1.000 34.98274  ?  65  LEU A CD2 1 
ATOM   391  N N   . ARG A 1 58  ? 61.05900  2.19900   30.92300  1.000 51.46987  ?  66  ARG A N   1 
ATOM   392  C CA  . ARG A 1 58  ? 61.50700  0.81900   30.81900  1.000 42.16157  ?  66  ARG A CA  1 
ATOM   393  C C   . ARG A 1 58  ? 62.87500  0.68700   31.47000  1.000 44.17267  ?  66  ARG A C   1 
ATOM   394  O O   . ARG A 1 58  ? 63.81700  1.38400   31.09000  1.000 52.36794  ?  66  ARG A O   1 
ATOM   395  C CB  . ARG A 1 58  ? 61.57400  0.38400   29.35600  1.000 52.01861  ?  66  ARG A CB  1 
ATOM   396  C CG  . ARG A 1 58  ? 62.21200  -0.97800  29.13000  1.000 51.61242  ?  66  ARG A CG  1 
ATOM   397  C CD  . ARG A 1 58  ? 62.37300  -1.32500  27.64200  1.000 54.77810  ?  66  ARG A CD  1 
ATOM   398  N NE  . ARG A 1 58  ? 61.43600  -0.66800  26.73300  1.000 64.14227  ?  66  ARG A NE  1 
ATOM   399  C CZ  . ARG A 1 58  ? 60.11300  -0.78000  26.77100  1.000 61.70281  ?  66  ARG A CZ  1 
ATOM   400  N NH1 . ARG A 1 58  ? 59.50700  -1.57300  27.64000  1.000 57.41519  ?  66  ARG A NH1 1 
ATOM   401  N NH2 . ARG A 1 58  ? 59.37900  -0.08800  25.90500  1.000 56.70071  ?  66  ARG A NH2 1 
ATOM   402  N N   . HIS A 1 59  ? 62.98300  -0.21000  32.44100  1.000 46.98582  ?  67  HIS A N   1 
ATOM   403  C CA  . HIS A 1 59  ? 64.20100  -0.38100  33.21900  1.000 48.34888  ?  67  HIS A CA  1 
ATOM   404  C C   . HIS A 1 59  ? 64.88000  -1.68600  32.82900  1.000 49.33664  ?  67  HIS A C   1 
ATOM   405  O O   . HIS A 1 59  ? 64.23600  -2.73800  32.79800  1.000 51.70373  ?  67  HIS A O   1 
ATOM   406  C CB  . HIS A 1 59  ? 63.88700  -0.36000  34.71400  1.000 43.46786  ?  67  HIS A CB  1 
ATOM   407  C CG  . HIS A 1 59  ? 63.25300  0.91300   35.17900  1.000 46.69185  ?  67  HIS A CG  1 
ATOM   408  N ND1 . HIS A 1 59  ? 63.97800  2.05900   35.41800  1.000 50.91597  ?  67  HIS A ND1 1 
ATOM   409  C CD2 . HIS A 1 59  ? 61.96300  1.22200   35.44600  1.000 42.53571  ?  67  HIS A CD2 1 
ATOM   410  C CE1 . HIS A 1 59  ? 63.16300  3.01900   35.81400  1.000 48.09374  ?  67  HIS A CE1 1 
ATOM   411  N NE2 . HIS A 1 59  ? 61.93400  2.53700   35.84000  1.000 48.02868  ?  67  HIS A NE2 1 
ATOM   412  N N   . GLU A 1 60  ? 66.17400  -1.61400  32.52200  1.000 53.12937  ?  68  GLU A N   1 
ATOM   413  C CA  . GLU A 1 60  ? 66.92900  -2.78200  32.09200  1.000 51.07047  ?  68  GLU A CA  1 
ATOM   414  C C   . GLU A 1 60  ? 68.32000  -2.74500  32.70700  1.000 48.84906  ?  68  GLU A C   1 
ATOM   415  O O   . GLU A 1 60  ? 68.83000  -1.68200  33.06000  1.000 48.43478  ?  68  GLU A O   1 
ATOM   416  C CB  . GLU A 1 60  ? 67.03100  -2.85200  30.56100  1.000 44.08926  ?  68  GLU A CB  1 
ATOM   417  C CG  . GLU A 1 60  ? 65.68800  -2.96000  29.85400  1.000 50.68291  ?  68  GLU A CG  1 
ATOM   418  C CD  . GLU A 1 60  ? 65.80200  -2.83700  28.35200  1.000 56.76050  ?  68  GLU A CD  1 
ATOM   419  O OE1 . GLU A 1 60  ? 65.84700  -1.69600  27.84800  1.000 58.77945  ?  68  GLU A OE1 1 
ATOM   420  O OE2 . GLU A 1 60  ? 65.83800  -3.88300  27.67200  1.000 67.91364  -1 68  GLU A OE2 1 
ATOM   421  N N   . ALA A 1 61  ? 68.92500  -3.92300  32.84000  1.000 51.82857  ?  69  ALA A N   1 
ATOM   422  C CA  . ALA A 1 61  ? 70.29400  -4.05800  33.32300  1.000 57.79441  ?  69  ALA A CA  1 
ATOM   423  C C   . ALA A 1 61  ? 71.00800  -5.10100  32.47900  1.000 60.30348  ?  69  ALA A C   1 
ATOM   424  O O   . ALA A 1 61  ? 70.45800  -6.17800  32.22700  1.000 60.13569  ?  69  ALA A O   1 
ATOM   425  C CB  . ALA A 1 61  ? 70.33000  -4.45300  34.80200  1.000 55.81556  ?  69  ALA A CB  1 
ATOM   426  N N   . ARG A 1 62  ? 72.22500  -4.78700  32.04300  1.000 60.85762  ?  70  ARG A N   1 
ATOM   427  C CA  . ARG A 1 62  ? 72.94700  -5.67800  31.14500  1.000 54.95920  ?  70  ARG A CA  1 
ATOM   428  C C   . ARG A 1 62  ? 74.43500  -5.64300  31.45400  1.000 65.28974  ?  70  ARG A C   1 
ATOM   429  O O   . ARG A 1 62  ? 74.95400  -4.67100  32.00000  1.000 67.72969  ?  70  ARG A O   1 
ATOM   430  C CB  . ARG A 1 62  ? 72.69900  -5.30300  29.67900  1.000 53.04645  ?  70  ARG A CB  1 
ATOM   431  C CG  . ARG A 1 62  ? 73.22400  -3.93900  29.28500  1.000 54.45170  ?  70  ARG A CG  1 
ATOM   432  C CD  . ARG A 1 62  ? 73.34300  -3.82400  27.77800  1.000 62.89190  ?  70  ARG A CD  1 
ATOM   433  N NE  . ARG A 1 62  ? 73.66600  -2.47000  27.35100  1.000 66.77833  ?  70  ARG A NE  1 
ATOM   434  C CZ  . ARG A 1 62  ? 73.27200  -1.93600  26.20300  1.000 72.10558  ?  70  ARG A CZ  1 
ATOM   435  N NH1 . ARG A 1 62  ? 72.52500  -2.61400  25.34600  1.000 61.23656  ?  70  ARG A NH1 1 
ATOM   436  N NH2 . ARG A 1 62  ? 73.63600  -0.69200  25.90700  1.000 73.03811  ?  70  ARG A NH2 1 
ATOM   437  N N   . LEU A 1 63  ? 75.12900  -6.71800  31.08900  1.000 63.77550  ?  71  LEU A N   1 
ATOM   438  C CA  . LEU A 1 63  ? 76.57300  -6.76800  31.27500  1.000 60.09906  ?  71  LEU A CA  1 
ATOM   439  C C   . LEU A 1 63  ? 77.27600  -6.07600  30.11600  1.000 62.77553  ?  71  LEU A C   1 
ATOM   440  O O   . LEU A 1 63  ? 76.80500  -6.11600  28.97600  1.000 57.20264  ?  71  LEU A O   1 
ATOM   441  C CB  . LEU A 1 63  ? 77.06600  -8.20700  31.39900  1.000 59.53654  ?  71  LEU A CB  1 
ATOM   442  C CG  . LEU A 1 63  ? 76.52600  -9.04600  32.55400  1.000 59.68783  ?  71  LEU A CG  1 
ATOM   443  C CD1 . LEU A 1 63  ? 75.92200  -10.32200 32.02400  1.000 57.35919  ?  71  LEU A CD1 1 
ATOM   444  C CD2 . LEU A 1 63  ? 77.62000  -9.34800  33.55600  1.000 43.94084  ?  71  LEU A CD2 1 
ATOM   445  N N   . THR A 1 64  ? 78.40500  -5.44500  30.41400  1.000 72.94644  ?  72  THR A N   1 
ATOM   446  C CA  . THR A 1 64  ? 79.19600  -4.72700  29.42900  1.000 80.49201  ?  72  THR A CA  1 
ATOM   447  C C   . THR A 1 64  ? 80.50100  -5.47400  29.16200  1.000 80.93789  ?  72  THR A C   1 
ATOM   448  O O   . THR A 1 64  ? 80.83100  -6.46200  29.82200  1.000 72.86328  ?  72  THR A O   1 
ATOM   449  C CB  . THR A 1 64  ? 79.46800  -3.29900  29.91300  1.000 81.86983  ?  72  THR A CB  1 
ATOM   450  O OG1 . THR A 1 64  ? 80.30500  -2.60800  28.97700  1.000 88.46132  ?  72  THR A OG1 1 
ATOM   451  C CG2 . THR A 1 64  ? 80.15000  -3.33400  31.25700  1.000 71.36389  ?  72  THR A CG2 1 
ATOM   452  N N   . ASP A 1 65  ? 81.24800  -4.98200  28.17100  1.000 81.94825  ?  73  ASP A N   1 
ATOM   453  C CA  . ASP A 1 65  ? 82.47700  -5.64700  27.75500  1.000 82.38542  ?  73  ASP A CA  1 
ATOM   454  C C   . ASP A 1 65  ? 83.51500  -5.68100  28.87000  1.000 81.58017  ?  73  ASP A C   1 
ATOM   455  O O   . ASP A 1 65  ? 84.21300  -6.68800  29.03300  1.000 79.62986  ?  73  ASP A O   1 
ATOM   456  C CB  . ASP A 1 65  ? 83.05100  -4.95000  26.52300  1.000 78.95878  ?  73  ASP A CB  1 
ATOM   457  C CG  . ASP A 1 65  ? 82.13300  -5.04300  25.32200  1.000 81.44425  ?  73  ASP A CG  1 
ATOM   458  O OD1 . ASP A 1 65  ? 81.28400  -5.95700  25.29300  1.000 92.13549  ?  73  ASP A OD1 1 
ATOM   459  O OD2 . ASP A 1 65  ? 82.25800  -4.20100  24.40900  1.000 80.71336  -1 73  ASP A OD2 1 
ATOM   460  N N   . ASP A 1 66  ? 83.63100  -4.60700  29.64600  1.000 81.36674  ?  74  ASP A N   1 
ATOM   461  C CA  . ASP A 1 66  ? 84.67800  -4.49000  30.65300  1.000 78.07571  ?  74  ASP A CA  1 
ATOM   462  C C   . ASP A 1 66  ? 84.30900  -5.13200  31.98600  1.000 74.50885  ?  74  ASP A C   1 
ATOM   463  O O   . ASP A 1 66  ? 84.92700  -4.81000  33.00500  1.000 76.15475  ?  74  ASP A O   1 
ATOM   464  C CB  . ASP A 1 66  ? 85.05500  -3.01900  30.87200  1.000 76.48459  ?  74  ASP A CB  1 
ATOM   465  C CG  . ASP A 1 66  ? 83.85600  -2.13200  31.15200  1.000 80.40421  ?  74  ASP A CG  1 
ATOM   466  O OD1 . ASP A 1 66  ? 82.93600  -2.06700  30.31000  1.000 86.37991  ?  74  ASP A OD1 1 
ATOM   467  O OD2 . ASP A 1 66  ? 83.83600  -1.49100  32.22300  1.000 80.83124  -1 74  ASP A OD2 1 
ATOM   468  N N   . GLY A 1 67  ? 83.32600  -6.02700  32.00700  1.000 77.85420  ?  75  GLY A N   1 
ATOM   469  C CA  . GLY A 1 67  ? 83.02000  -6.78100  33.20600  1.000 73.99514  ?  75  GLY A CA  1 
ATOM   470  C C   . GLY A 1 67  ? 82.15000  -6.08300  34.22300  1.000 77.35096  ?  75  GLY A C   1 
ATOM   471  O O   . GLY A 1 67  ? 82.12300  -6.50600  35.38300  1.000 69.79962  ?  75  GLY A O   1 
ATOM   472  N N   . ASP A 1 68  ? 81.44300  -5.03000  33.83400  1.000 82.19529  ?  76  ASP A N   1 
ATOM   473  C CA  . ASP A 1 68  ? 80.57100  -4.28900  34.73200  1.000 77.79819  ?  76  ASP A CA  1 
ATOM   474  C C   . ASP A 1 68  ? 79.10900  -4.54500  34.37700  1.000 71.71731  ?  76  ASP A C   1 
ATOM   475  O O   . ASP A 1 68  ? 78.78600  -5.31300  33.46900  1.000 68.12701  ?  76  ASP A O   1 
ATOM   476  C CB  . ASP A 1 68  ? 80.89000  -2.79200  34.66400  1.000 80.39189  ?  76  ASP A CB  1 
ATOM   477  C CG  . ASP A 1 68  ? 80.61700  -2.07200  35.96600  1.000 73.44779  ?  76  ASP A CG  1 
ATOM   478  O OD1 . ASP A 1 68  ? 79.96900  -2.65600  36.85400  1.000 71.13999  ?  76  ASP A OD1 1 
ATOM   479  O OD2 . ASP A 1 68  ? 81.05100  -0.91200  36.09800  1.000 66.94331  -1 76  ASP A OD2 1 
ATOM   480  N N   . ILE A 1 69  ? 78.22000  -3.88700  35.11600  1.000 68.33654  ?  77  ILE A N   1 
ATOM   481  C CA  . ILE A 1 69  ? 76.78300  -3.94200  34.87600  1.000 63.89289  ?  77  ILE A CA  1 
ATOM   482  C C   . ILE A 1 69  ? 76.29500  -2.52300  34.61700  1.000 64.55649  ?  77  ILE A C   1 
ATOM   483  O O   . ILE A 1 69  ? 76.55400  -1.61400  35.41400  1.000 66.19523  ?  77  ILE A O   1 
ATOM   484  C CB  . ILE A 1 69  ? 76.03100  -4.57800  36.05400  1.000 54.43565  ?  77  ILE A CB  1 
ATOM   485  C CG1 . ILE A 1 69  ? 76.79900  -5.78500  36.59400  1.000 58.29926  ?  77  ILE A CG1 1 
ATOM   486  C CG2 . ILE A 1 69  ? 74.62400  -4.96700  35.63700  1.000 53.55861  ?  77  ILE A CG2 1 
ATOM   487  C CD1 . ILE A 1 69  ? 76.00100  -6.63900  37.55200  1.000 54.17295  ?  77  ILE A CD1 1 
ATOM   488  N N   . GLU A 1 70  ? 75.59000  -2.33800  33.50700  1.000 58.94695  ?  78  GLU A N   1 
ATOM   489  C CA  . GLU A 1 70  ? 75.06700  -1.04500  33.09600  1.000 51.50765  ?  78  GLU A CA  1 
ATOM   490  C C   . GLU A 1 70  ? 73.55100  -1.04400  33.23200  1.000 54.78436  ?  78  GLU A C   1 
ATOM   491  O O   . GLU A 1 70  ? 72.88300  -1.99700  32.80900  1.000 57.71637  ?  78  GLU A O   1 
ATOM   492  C CB  . GLU A 1 70  ? 75.47200  -0.73500  31.65500  1.000 55.02993  ?  78  GLU A CB  1 
ATOM   493  C CG  . GLU A 1 70  ? 74.65600  0.35700   30.99000  1.000 56.48836  ?  78  GLU A CG  1 
ATOM   494  C CD  . GLU A 1 70  ? 75.28700  0.84800   29.70600  1.000 65.02332  ?  78  GLU A CD  1 
ATOM   495  O OE1 . GLU A 1 70  ? 76.49300  1.16900   29.72100  1.000 77.72154  ?  78  GLU A OE1 1 
ATOM   496  O OE2 . GLU A 1 70  ? 74.58100  0.90800   28.67900  1.000 60.14142  -1 78  GLU A OE2 1 
ATOM   497  N N   . ILE A 1 71  ? 73.01800  0.02400   33.82300  1.000 55.72071  ?  79  ILE A N   1 
ATOM   498  C CA  . ILE A 1 71  ? 71.58200  0.18200   34.02000  1.000 48.98291  ?  79  ILE A CA  1 
ATOM   499  C C   . ILE A 1 71  ? 71.06100  1.19300   33.00900  1.000 46.28928  ?  79  ILE A C   1 
ATOM   500  O O   . ILE A 1 71  ? 71.66000  2.25700   32.81800  1.000 49.51587  ?  79  ILE A O   1 
ATOM   501  C CB  . ILE A 1 71  ? 71.27400  0.62500   35.45900  1.000 41.73637  ?  79  ILE A CB  1 
ATOM   502  C CG1 . ILE A 1 71  ? 71.71800  -0.45600  36.44700  1.000 45.83350  ?  79  ILE A CG1 1 
ATOM   503  C CG2 . ILE A 1 71  ? 69.79700  0.94500   35.61400  1.000 46.38663  ?  79  ILE A CG2 1 
ATOM   504  C CD1 . ILE A 1 71  ? 70.92400  -0.48900  37.73100  1.000 48.34145  ?  79  ILE A CD1 1 
ATOM   505  N N   . LEU A 1 72  ? 69.95100  0.86100   32.35500  1.000 44.27878  ?  80  LEU A N   1 
ATOM   506  C CA  . LEU A 1 72  ? 69.39500  1.66300   31.27600  1.000 48.70781  ?  80  LEU A CA  1 
ATOM   507  C C   . LEU A 1 72  ? 67.91900  1.93900   31.52200  1.000 57.22693  ?  80  LEU A C   1 
ATOM   508  O O   . LEU A 1 72  ? 67.19200  1.08100   32.03400  1.000 59.61157  ?  80  LEU A O   1 
ATOM   509  C CB  . LEU A 1 72  ? 69.56000  0.95600   29.93100  1.000 53.98796  ?  80  LEU A CB  1 
ATOM   510  C CG  . LEU A 1 72  ? 70.95700  0.44300   29.60200  1.000 57.69924  ?  80  LEU A CG  1 
ATOM   511  C CD1 . LEU A 1 72  ? 70.97900  -1.07200  29.64900  1.000 62.03415  ?  80  LEU A CD1 1 
ATOM   512  C CD2 . LEU A 1 72  ? 71.39000  0.94700   28.24000  1.000 65.57501  ?  80  LEU A CD2 1 
ATOM   513  N N   . THR A 1 73  ? 67.48400  3.14100   31.15000  1.000 51.68076  ?  81  THR A N   1 
ATOM   514  C CA  . THR A 1 73  ? 66.07500  3.51800   31.15600  1.000 51.68166  ?  81  THR A CA  1 
ATOM   515  C C   . THR A 1 73  ? 65.68700  3.96700   29.75400  1.000 57.21868  ?  81  THR A C   1 
ATOM   516  O O   . THR A 1 73  ? 66.33300  4.85100   29.18100  1.000 58.35925  ?  81  THR A O   1 
ATOM   517  C CB  . THR A 1 73  ? 65.79100  4.61800   32.18400  1.000 54.22576  ?  81  THR A CB  1 
ATOM   518  O OG1 . THR A 1 73  ? 66.08500  5.90200   31.62300  1.000 71.83586  ?  81  THR A OG1 1 
ATOM   519  C CG2 . THR A 1 73  ? 66.62500  4.41300   33.43600  1.000 49.77641  ?  81  THR A CG2 1 
ATOM   520  N N   . ASP A 1 74  ? 64.64300  3.34600   29.20300  1.000 65.22595  ?  82  ASP A N   1 
ATOM   521  C CA  . ASP A 1 74  ? 64.17400  3.61800   27.84200  1.000 64.39873  ?  82  ASP A CA  1 
ATOM   522  C C   . ASP A 1 74  ? 65.29400  3.45200   26.81900  1.000 69.60623  ?  82  ASP A C   1 
ATOM   523  O O   . ASP A 1 74  ? 65.37100  4.18200   25.83000  1.000 74.53346  ?  82  ASP A O   1 
ATOM   524  C CB  . ASP A 1 74  ? 63.54300  5.00800   27.73600  1.000 67.96422  ?  82  ASP A CB  1 
ATOM   525  C CG  . ASP A 1 74  ? 62.09100  5.02200   28.16500  1.000 69.16389  ?  82  ASP A CG  1 
ATOM   526  O OD1 . ASP A 1 74  ? 61.47900  3.93600   28.22000  1.000 61.25432  ?  82  ASP A OD1 1 
ATOM   527  O OD2 . ASP A 1 74  ? 61.55900  6.11800   28.43500  1.000 62.21087  -1 82  ASP A OD2 1 
ATOM   528  N N   . GLY A 1 75  ? 66.17200  2.48000   27.05800  1.000 68.50138  ?  83  GLY A N   1 
ATOM   529  C CA  . GLY A 1 75  ? 67.26800  2.19900   26.15800  1.000 72.08953  ?  83  GLY A CA  1 
ATOM   530  C C   . GLY A 1 75  ? 68.44500  3.14200   26.26600  1.000 73.55907  ?  83  GLY A C   1 
ATOM   531  O O   . GLY A 1 75  ? 69.44600  2.93800   25.56900  1.000 76.32437  ?  83  GLY A O   1 
ATOM   532  N N   . ARG A 1 76  ? 68.36000  4.16300   27.11100  1.000 72.30455  ?  84  ARG A N   1 
ATOM   533  C CA  . ARG A 1 76  ? 69.41400  5.13700   27.33800  1.000 61.77448  ?  84  ARG A CA  1 
ATOM   534  C C   . ARG A 1 76  ? 70.23300  4.75700   28.56100  1.000 59.56565  ?  84  ARG A C   1 
ATOM   535  O O   . ARG A 1 76  ? 69.66800  4.50500   29.63000  1.000 58.26464  ?  84  ARG A O   1 
ATOM   536  C CB  . ARG A 1 76  ? 68.83100  6.53500   27.54000  1.000 65.31901  ?  84  ARG A CB  1 
ATOM   537  C CG  . ARG A 1 76  ? 67.78600  6.93100   26.51400  1.000 71.82696  ?  84  ARG A CG  1 
ATOM   538  C CD  . ARG A 1 76  ? 67.33400  8.36600   26.72400  1.000 77.95296  ?  84  ARG A CD  1 
ATOM   539  N NE  . ARG A 1 76  ? 66.53900  8.51200   27.93700  1.000 83.72486  ?  84  ARG A NE  1 
ATOM   540  C CZ  . ARG A 1 76  ? 65.21500  8.57000   27.96100  1.000 84.21517  ?  84  ARG A CZ  1 
ATOM   541  N NH1 . ARG A 1 76  ? 64.50000  8.49800   26.85100  1.000 80.98162  ?  84  ARG A NH1 1 
ATOM   542  N NH2 . ARG A 1 76  ? 64.59300  8.70300   29.12900  1.000 72.47539  ?  84  ARG A NH2 1 
ATOM   543  N N   . PRO A 1 77  ? 71.55700  4.69800   28.42700  1.000 67.14018  ?  85  PRO A N   1 
ATOM   544  C CA  . PRO A 1 77  ? 72.39900  4.35400   29.58000  1.000 59.86117  ?  85  PRO A CA  1 
ATOM   545  C C   . PRO A 1 77  ? 72.23700  5.37400   30.69600  1.000 51.84131  ?  85  PRO A C   1 
ATOM   546  O O   . PRO A 1 77  ? 72.10200  6.57300   30.44600  1.000 58.89426  ?  85  PRO A O   1 
ATOM   547  C CB  . PRO A 1 77  ? 73.81800  4.36700   29.00100  1.000 54.64496  ?  85  PRO A CB  1 
ATOM   548  C CG  . PRO A 1 77  ? 73.72700  5.24000   27.79700  1.000 56.32965  ?  85  PRO A CG  1 
ATOM   549  C CD  . PRO A 1 77  ? 72.35400  5.03200   27.23600  1.000 66.38152  ?  85  PRO A CD  1 
ATOM   550  N N   . SER A 1 78  ? 72.24400  4.88500   31.93300  1.000 45.79244  ?  86  SER A N   1 
ATOM   551  C CA  . SER A 1 78  ? 72.09400  5.73100   33.10800  1.000 37.93813  ?  86  SER A CA  1 
ATOM   552  C C   . SER A 1 78  ? 73.31500  5.69400   34.01500  1.000 43.55975  ?  86  SER A C   1 
ATOM   553  O O   . SER A 1 78  ? 73.85100  6.74600   34.37300  1.000 46.82409  ?  86  SER A O   1 
ATOM   554  C CB  . SER A 1 78  ? 70.84400  5.32000   33.89300  1.000 44.76019  ?  86  SER A CB  1 
ATOM   555  O OG  . SER A 1 78  ? 69.67200  5.55400   33.13300  1.000 49.52032  ?  86  SER A OG  1 
ATOM   556  N N   . ALA A 1 79  ? 73.77000  4.50400   34.39500  1.000 49.37108  ?  87  ALA A N   1 
ATOM   557  C CA  . ALA A 1 79  ? 74.91200  4.40100   35.29000  1.000 51.29793  ?  87  ALA A CA  1 
ATOM   558  C C   . ALA A 1 79  ? 75.54000  3.02100   35.17400  1.000 53.64796  ?  87  ALA A C   1 
ATOM   559  O O   . ALA A 1 79  ? 74.95600  2.08800   34.61400  1.000 58.17789  ?  87  ALA A O   1 
ATOM   560  C CB  . ALA A 1 79  ? 74.51200  4.68500   36.74200  1.000 42.60521  ?  87  ALA A CB  1 
ATOM   561  N N   . ARG A 1 80  ? 76.75900  2.92200   35.69500  1.000 47.38660  ?  88  ARG A N   1 
ATOM   562  C CA  . ARG A 1 80  ? 77.44200  1.66000   35.92300  1.000 53.16926  ?  88  ARG A CA  1 
ATOM   563  C C   . ARG A 1 80  ? 77.45300  1.37700   37.41900  1.000 52.69053  ?  88  ARG A C   1 
ATOM   564  O O   . ARG A 1 80  ? 77.44100  2.29900   38.23800  1.000 53.45844  ?  88  ARG A O   1 
ATOM   565  C CB  . ARG A 1 80  ? 78.87900  1.69400   35.39300  1.000 66.67884  ?  88  ARG A CB  1 
ATOM   566  C CG  . ARG A 1 80  ? 79.03600  1.46000   33.89600  1.000 66.56004  ?  88  ARG A CG  1 
ATOM   567  C CD  . ARG A 1 80  ? 80.43200  0.92900   33.58900  1.000 65.00709  ?  88  ARG A CD  1 
ATOM   568  N NE  . ARG A 1 80  ? 80.96800  1.41300   32.32200  1.000 79.19849  ?  88  ARG A NE  1 
ATOM   569  C CZ  . ARG A 1 80  ? 80.67600  0.90000   31.13500  1.000 79.71408  ?  88  ARG A CZ  1 
ATOM   570  N NH1 . ARG A 1 80  ? 79.83500  -0.11000  31.00700  1.000 82.91885  ?  88  ARG A NH1 1 
ATOM   571  N NH2 . ARG A 1 80  ? 81.24400  1.41500   30.04900  1.000 77.40292  ?  88  ARG A NH2 1 
ATOM   572  N N   . VAL A 1 81  ? 77.47300  0.09200   37.77200  1.000 49.94306  ?  89  VAL A N   1 
ATOM   573  C CA  . VAL A 1 81  ? 77.44800  -0.27900  39.18400  1.000 52.82692  ?  89  VAL A CA  1 
ATOM   574  C C   . VAL A 1 81  ? 78.72400  0.16500   39.88700  1.000 55.13429  ?  89  VAL A C   1 
ATOM   575  O O   . VAL A 1 81  ? 78.69200  0.54900   41.06200  1.000 52.47353  ?  89  VAL A O   1 
ATOM   576  C CB  . VAL A 1 81  ? 77.20700  -1.79300  39.33400  1.000 49.60543  ?  89  VAL A CB  1 
ATOM   577  C CG1 . VAL A 1 81  ? 77.16000  -2.18300  40.79800  1.000 53.62028  ?  89  VAL A CG1 1 
ATOM   578  C CG2 . VAL A 1 81  ? 75.91000  -2.17100  38.66200  1.000 44.56021  ?  89  VAL A CG2 1 
ATOM   579  N N   . SER A 1 82  ? 79.86100  0.12900   39.18900  1.000 62.15804  ?  90  SER A N   1 
ATOM   580  C CA  . SER A 1 82  ? 81.11800  0.54300   39.80000  1.000 65.21310  ?  90  SER A CA  1 
ATOM   581  C C   . SER A 1 82  ? 81.14500  2.03000   40.13100  1.000 64.69235  ?  90  SER A C   1 
ATOM   582  O O   . SER A 1 82  ? 81.96500  2.45200   40.95400  1.000 66.05736  ?  90  SER A O   1 
ATOM   583  C CB  . SER A 1 82  ? 82.29100  0.20400   38.88200  1.000 57.73664  ?  90  SER A CB  1 
ATOM   584  O OG  . SER A 1 82  ? 82.22300  0.95000   37.68200  1.000 64.76802  ?  90  SER A OG  1 
ATOM   585  N N   . GLU A 1 83  ? 80.27500  2.83100   39.51300  1.000 60.38354  ?  91  GLU A N   1 
ATOM   586  C CA  . GLU A 1 83  ? 80.23600  4.26200   39.78600  1.000 52.77052  ?  91  GLU A CA  1 
ATOM   587  C C   . GLU A 1 83  ? 79.76400  4.58400   41.19500  1.000 54.97087  ?  91  GLU A C   1 
ATOM   588  O O   . GLU A 1 83  ? 79.95100  5.71800   41.64700  1.000 63.45135  ?  91  GLU A O   1 
ATOM   589  C CB  . GLU A 1 83  ? 79.33100  4.96700   38.77500  1.000 46.91244  ?  91  GLU A CB  1 
ATOM   590  C CG  . GLU A 1 83  ? 79.71600  4.73500   37.32700  1.000 57.59034  ?  91  GLU A CG  1 
ATOM   591  C CD  . GLU A 1 83  ? 78.99900  5.67300   36.37800  1.000 59.72454  ?  91  GLU A CD  1 
ATOM   592  O OE1 . GLU A 1 83  ? 78.50100  6.71900   36.84000  1.000 71.68838  ?  91  GLU A OE1 1 
ATOM   593  O OE2 . GLU A 1 83  ? 78.93700  5.36600   35.17000  1.000 57.20292  -1 91  GLU A OE2 1 
ATOM   594  N N   . GLY A 1 84  ? 79.16500  3.62900   41.89200  1.000 48.70640  ?  92  GLY A N   1 
ATOM   595  C CA  . GLY A 1 84  ? 78.62400  3.86400   43.21100  1.000 42.35058  ?  92  GLY A CA  1 
ATOM   596  C C   . GLY A 1 84  ? 77.10700  3.95100   43.19900  1.000 40.79258  ?  92  GLY A C   1 
ATOM   597  O O   . GLY A 1 84  ? 76.47100  4.20900   42.17500  1.000 40.55277  ?  92  GLY A O   1 
ATOM   598  N N   . PHE A 1 85  ? 76.52000  3.72200   44.37200  1.000 42.22487  ?  93  PHE A N   1 
ATOM   599  C CA  . PHE A 1 85  ? 75.06700  3.75200   44.48700  1.000 44.70557  ?  93  PHE A CA  1 
ATOM   600  C C   . PHE A 1 85  ? 74.54300  5.18200   44.49700  1.000 47.89418  ?  93  PHE A C   1 
ATOM   601  O O   . PHE A 1 85  ? 73.46200  5.45800   43.96300  1.000 45.94371  ?  93  PHE A O   1 
ATOM   602  C CB  . PHE A 1 85  ? 74.63900  2.99900   45.74300  1.000 38.39532  ?  93  PHE A CB  1 
ATOM   603  C CG  . PHE A 1 85  ? 75.24900  1.63400   45.85800  1.000 44.75253  ?  93  PHE A CG  1 
ATOM   604  C CD1 . PHE A 1 85  ? 75.03300  0.68200   44.87800  1.000 40.89059  ?  93  PHE A CD1 1 
ATOM   605  C CD2 . PHE A 1 85  ? 76.05800  1.30800   46.93200  1.000 44.90479  ?  93  PHE A CD2 1 
ATOM   606  C CE1 . PHE A 1 85  ? 75.59700  -0.57300  44.97500  1.000 36.05092  ?  93  PHE A CE1 1 
ATOM   607  C CE2 . PHE A 1 85  ? 76.62300  0.05500   47.03400  1.000 39.66875  ?  93  PHE A CE2 1 
ATOM   608  C CZ  . PHE A 1 85  ? 76.39300  -0.88600  46.05400  1.000 38.82468  ?  93  PHE A CZ  1 
ATOM   609  N N   . GLY A 1 86  ? 75.29600  6.10300   45.09800  1.000 45.54322  ?  94  GLY A N   1 
ATOM   610  C CA  . GLY A 1 86  ? 74.91300  7.50300   45.04300  1.000 38.26554  ?  94  GLY A CA  1 
ATOM   611  C C   . GLY A 1 86  ? 74.87500  8.03200   43.62400  1.000 34.79532  ?  94  GLY A C   1 
ATOM   612  O O   . GLY A 1 86  ? 74.03900  8.87100   43.28600  1.000 34.21225  ?  94  GLY A O   1 
ATOM   613  N N   . ALA A 1 87  ? 75.78100  7.54700   42.77300  1.000 34.32851  ?  95  ALA A N   1 
ATOM   614  C CA  . ALA A 1 87  ? 75.74700  7.92000   41.36400  1.000 33.24005  ?  95  ALA A CA  1 
ATOM   615  C C   . ALA A 1 87  ? 74.47100  7.43000   40.69300  1.000 35.60795  ?  95  ALA A C   1 
ATOM   616  O O   . ALA A 1 87  ? 73.88300  8.13800   39.86900  1.000 34.14167  ?  95  ALA A O   1 
ATOM   617  C CB  . ALA A 1 87  ? 76.97900  7.37200   40.64800  1.000 37.39288  ?  95  ALA A CB  1 
ATOM   618  N N   . LEU A 1 88  ? 74.03000  6.21500   41.02500  1.000 39.25377  ?  96  LEU A N   1 
ATOM   619  C CA  . LEU A 1 88  ? 72.78000  5.70400   40.47200  1.000 42.58446  ?  96  LEU A CA  1 
ATOM   620  C C   . LEU A 1 88  ? 71.59200  6.52800   40.95300  1.000 41.30800  ?  96  LEU A C   1 
ATOM   621  O O   . LEU A 1 88  ? 70.66400  6.81800   40.18600  1.000 43.20365  ?  96  LEU A O   1 
ATOM   622  C CB  . LEU A 1 88  ? 72.60500  4.23400   40.84700  1.000 43.08267  ?  96  LEU A CB  1 
ATOM   623  C CG  . LEU A 1 88  ? 71.40000  3.52500   40.23100  1.000 32.25557  ?  96  LEU A CG  1 
ATOM   624  C CD1 . LEU A 1 88  ? 71.45300  3.61500   38.71900  1.000 35.63014  ?  96  LEU A CD1 1 
ATOM   625  C CD2 . LEU A 1 88  ? 71.35000  2.07900   40.68100  1.000 26.93413  ?  96  LEU A CD2 1 
ATOM   626  N N   . ALA A 1 89  ? 71.60100  6.90800   42.23200  1.000 41.24079  ?  97  ALA A N   1 
ATOM   627  C CA  . ALA A 1 89  ? 70.54100  7.76500   42.75200  1.000 39.95089  ?  97  ALA A CA  1 
ATOM   628  C C   . ALA A 1 89  ? 70.53200  9.11400   42.04500  1.000 38.20709  ?  97  ALA A C   1 
ATOM   629  O O   . ALA A 1 89  ? 69.46500  9.65100   41.72700  1.000 39.11683  ?  97  ALA A O   1 
ATOM   630  C CB  . ALA A 1 89  ? 70.70800  7.94900   44.25900  1.000 29.17597  ?  97  ALA A CB  1 
ATOM   631  N N   . GLN A 1 90  ? 71.71500  9.67600   41.79500  1.000 38.10980  ?  98  GLN A N   1 
ATOM   632  C CA  . GLN A 1 90  ? 71.79900  10.94700  41.08400  1.000 44.83157  ?  98  GLN A CA  1 
ATOM   633  C C   . GLN A 1 90  ? 71.35500  10.80100  39.63600  1.000 36.44090  ?  98  GLN A C   1 
ATOM   634  O O   . GLN A 1 90  ? 70.86000  11.75700  39.03300  1.000 44.46816  ?  98  GLN A O   1 
ATOM   635  C CB  . GLN A 1 90  ? 73.22200  11.49800  41.15700  1.000 39.46795  ?  98  GLN A CB  1 
ATOM   636  C CG  . GLN A 1 90  ? 73.39500  12.60300  42.17900  1.000 47.98171  ?  98  GLN A CG  1 
ATOM   637  C CD  . GLN A 1 90  ? 72.60100  13.84400  41.83200  1.000 48.35587  ?  98  GLN A CD  1 
ATOM   638  O OE1 . GLN A 1 90  ? 72.32900  14.11500  40.66300  1.000 41.75159  ?  98  GLN A OE1 1 
ATOM   639  N NE2 . GLN A 1 90  ? 72.21400  14.60100  42.85000  1.000 52.24981  ?  98  GLN A NE2 1 
ATOM   640  N N   . ALA A 1 91  ? 71.56000  9.62400   39.04900  1.000 37.33833  ?  99  ALA A N   1 
ATOM   641  C CA  . ALA A 1 91  ? 71.03900  9.37500   37.71100  1.000 42.54454  ?  99  ALA A CA  1 
ATOM   642  C C   . ALA A 1 91  ? 69.51900  9.31800   37.70700  1.000 40.70871  ?  99  ALA A C   1 
ATOM   643  O O   . ALA A 1 91  ? 68.88100  9.85200   36.79400  1.000 37.42289  ?  99  ALA A O   1 
ATOM   644  C CB  . ALA A 1 91  ? 71.62000  8.07800   37.15100  1.000 28.80930  ?  99  ALA A CB  1 
ATOM   645  N N   . TYR A 1 92  ? 68.92800  8.67600   38.71400  1.000 40.55900  ?  100 TYR A N   1 
ATOM   646  C CA  . TYR A 1 92  ? 67.47600  8.54000   38.76200  1.000 35.89362  ?  100 TYR A CA  1 
ATOM   647  C C   . TYR A 1 92  ? 66.77700  9.83300   39.16800  1.000 39.01072  ?  100 TYR A C   1 
ATOM   648  O O   . TYR A 1 92  ? 65.62100  10.04700  38.79100  1.000 35.51644  ?  100 TYR A O   1 
ATOM   649  C CB  . TYR A 1 92  ? 67.08000  7.42100   39.72800  1.000 37.98490  ?  100 TYR A CB  1 
ATOM   650  C CG  . TYR A 1 92  ? 67.20900  6.02700   39.15700  1.000 38.03672  ?  100 TYR A CG  1 
ATOM   651  C CD1 . TYR A 1 92  ? 66.81200  5.74900   37.85900  1.000 32.60275  ?  100 TYR A CD1 1 
ATOM   652  C CD2 . TYR A 1 92  ? 67.70800  4.98500   39.92300  1.000 38.66523  ?  100 TYR A CD2 1 
ATOM   653  C CE1 . TYR A 1 92  ? 66.92100  4.48100   37.33400  1.000 24.39667  ?  100 TYR A CE1 1 
ATOM   654  C CE2 . TYR A 1 92  ? 67.81800  3.71000   39.40700  1.000 38.69388  ?  100 TYR A CE2 1 
ATOM   655  C CZ  . TYR A 1 92  ? 67.42300  3.46400   38.11100  1.000 38.04760  ?  100 TYR A CZ  1 
ATOM   656  O OH  . TYR A 1 92  ? 67.52900  2.19700   37.58800  1.000 38.35302  ?  100 TYR A OH  1 
ATOM   657  N N   . ALA A 1 93  ? 67.45100  10.69500  39.93000  1.000 45.29141  ?  101 ALA A N   1 
ATOM   658  C CA  . ALA A 1 93  ? 66.78300  11.85500  40.52100  1.000 39.84100  ?  101 ALA A CA  1 
ATOM   659  C C   . ALA A 1 93  ? 66.18300  12.82400  39.50600  1.000 40.03704  ?  101 ALA A C   1 
ATOM   660  O O   . ALA A 1 93  ? 65.01700  13.21500  39.68500  1.000 44.97106  ?  101 ALA A O   1 
ATOM   661  C CB  . ALA A 1 93  ? 67.75500  12.57400  41.46200  1.000 29.62708  ?  101 ALA A CB  1 
ATOM   662  N N   . PRO A 1 94  ? 66.88700  13.26700  38.45600  1.000 36.39057  ?  102 PRO A N   1 
ATOM   663  C CA  . PRO A 1 94  ? 66.28500  14.25700  37.54800  1.000 32.12872  ?  102 PRO A CA  1 
ATOM   664  C C   . PRO A 1 94  ? 65.06500  13.75200  36.80100  1.000 34.73171  ?  102 PRO A C   1 
ATOM   665  O O   . PRO A 1 94  ? 64.29600  14.57400  36.28900  1.000 40.83700  ?  102 PRO A O   1 
ATOM   666  C CB  . PRO A 1 94  ? 67.42400  14.59200  36.57900  1.000 28.53515  ?  102 PRO A CB  1 
ATOM   667  C CG  . PRO A 1 94  ? 68.34100  13.45100  36.65200  1.000 40.82654  ?  102 PRO A CG  1 
ATOM   668  C CD  . PRO A 1 94  ? 68.26100  12.93400  38.04600  1.000 38.21795  ?  102 PRO A CD  1 
ATOM   669  N N   . MET A 1 95  ? 64.86400  12.44100  36.70900  1.000 42.57332  ?  103 MET A N   1 
ATOM   670  C CA  . MET A 1 95  ? 63.67800  11.89800  36.06400  1.000 45.50927  ?  103 MET A CA  1 
ATOM   671  C C   . MET A 1 95  ? 62.49700  11.76100  37.01400  1.000 42.32620  ?  103 MET A C   1 
ATOM   672  O O   . MET A 1 95  ? 61.42100  11.33800  36.58100  1.000 33.48200  ?  103 MET A O   1 
ATOM   673  C CB  . MET A 1 95  ? 63.99500  10.54000  35.43100  1.000 41.52970  ?  103 MET A CB  1 
ATOM   674  C CG  . MET A 1 95  ? 65.47000  10.32200  35.14900  1.000 49.83823  ?  103 MET A CG  1 
ATOM   675  S SD  . MET A 1 95  ? 65.78500  8.84000   34.17500  1.000 71.05437  ?  103 MET A SD  1 
ATOM   676  C CE  . MET A 1 95  ? 65.36500  7.57000   35.35100  1.000 26.16160  ?  103 MET A CE  1 
ATOM   677  N N   . GLN A 1 96  ? 62.66900  12.11000  38.28400  1.000 42.79559  ?  104 GLN A N   1 
ATOM   678  C CA  . GLN A 1 96  ? 61.60000  12.05900  39.26600  1.000 36.64953  ?  104 GLN A CA  1 
ATOM   679  C C   . GLN A 1 96  ? 60.83100  13.37500  39.30000  1.000 34.49054  ?  104 GLN A C   1 
ATOM   680  O O   . GLN A 1 96  ? 61.32400  14.42600  38.88900  1.000 38.05789  ?  104 GLN A O   1 
ATOM   681  C CB  . GLN A 1 96  ? 62.15600  11.75900  40.65800  1.000 35.72380  ?  104 GLN A CB  1 
ATOM   682  C CG  . GLN A 1 96  ? 62.84000  10.41700  40.80000  1.000 31.44281  ?  104 GLN A CG  1 
ATOM   683  C CD  . GLN A 1 96  ? 63.31600  10.16900  42.21500  1.000 37.75822  ?  104 GLN A CD  1 
ATOM   684  O OE1 . GLN A 1 96  ? 64.50300  10.28100  42.51200  1.000 46.30117  ?  104 GLN A OE1 1 
ATOM   685  N NE2 . GLN A 1 96  ? 62.38700  9.83500   43.09900  1.000 35.88183  ?  104 GLN A NE2 1 
ATOM   686  N N   . ALA A 1 97  ? 59.60100  13.29900  39.80600  1.000 33.17161  ?  105 ALA A N   1 
ATOM   687  C CA  . ALA A 1 97  ? 58.76600  14.47700  40.05500  1.000 30.01174  ?  105 ALA A CA  1 
ATOM   688  C C   . ALA A 1 97  ? 57.88800  14.14400  41.25700  1.000 28.88229  ?  105 ALA A C   1 
ATOM   689  O O   . ALA A 1 97  ? 56.82300  13.54300  41.10900  1.000 36.35714  ?  105 ALA A O   1 
ATOM   690  C CB  . ALA A 1 97  ? 57.93900  14.84900  38.83300  1.000 23.44862  ?  105 ALA A CB  1 
ATOM   691  N N   . LEU A 1 98  ? 58.33600  14.54000  42.44300  1.000 31.54600  ?  106 LEU A N   1 
ATOM   692  C CA  . LEU A 1 98  ? 57.66000  14.20100  43.68600  1.000 29.01865  ?  106 LEU A CA  1 
ATOM   693  C C   . LEU A 1 98  ? 56.97600  15.43100  44.26500  1.000 36.52515  ?  106 LEU A C   1 
ATOM   694  O O   . LEU A 1 98  ? 57.47700  16.55100  44.13800  1.000 38.81865  ?  106 LEU A O   1 
ATOM   695  C CB  . LEU A 1 98  ? 58.64500  13.63400  44.70800  1.000 28.04291  ?  106 LEU A CB  1 
ATOM   696  C CG  . LEU A 1 98  ? 59.56900  12.50600  44.25200  1.000 30.26243  ?  106 LEU A CG  1 
ATOM   697  C CD1 . LEU A 1 98  ? 60.47200  12.07800  45.39300  1.000 23.56440  ?  106 LEU A CD1 1 
ATOM   698  C CD2 . LEU A 1 98  ? 58.77900  11.32600  43.71900  1.000 32.47688  ?  106 LEU A CD2 1 
ATOM   699  N N   . ASP A 1 99  ? 55.82900  15.21500  44.90100  1.000 33.26045  ?  107 ASP A N   1 
ATOM   700  C CA  . ASP A 1 99  ? 55.11700  16.29800  45.56300  1.000 28.80996  ?  107 ASP A CA  1 
ATOM   701  C C   . ASP A 1 99  ? 55.64800  16.45400  46.98700  1.000 30.29809  ?  107 ASP A C   1 
ATOM   702  O O   . ASP A 1 99  ? 56.65800  15.85800  47.37100  1.000 32.90154  ?  107 ASP A O   1 
ATOM   703  C CB  . ASP A 1 99  ? 53.60800  16.05800  45.50800  1.000 30.51459  ?  107 ASP A CB  1 
ATOM   704  C CG  . ASP A 1 99  ? 53.18300  14.75200  46.16200  1.000 32.22488  ?  107 ASP A CG  1 
ATOM   705  O OD1 . ASP A 1 99  ? 53.96800  14.15700  46.92400  1.000 33.62762  ?  107 ASP A OD1 1 
ATOM   706  O OD2 . ASP A 1 99  ? 52.04300  14.31600  45.90700  1.000 27.05312  -1 107 ASP A OD2 1 
ATOM   707  N N   . GLU A 1 100 ? 54.96800  17.26900  47.79300  1.000 36.10786  ?  108 GLU A N   1 
ATOM   708  C CA  . GLU A 1 100 ? 55.42100  17.51100  49.15600  1.000 36.37243  ?  108 GLU A CA  1 
ATOM   709  C C   . GLU A 1 100 ? 55.26600  16.28500  50.04500  1.000 28.68345  ?  108 GLU A C   1 
ATOM   710  O O   . GLU A 1 100 ? 55.90900  16.21200  51.09800  1.000 29.96790  ?  108 GLU A O   1 
ATOM   711  C CB  . GLU A 1 100 ? 54.66100  18.69400  49.75400  1.000 44.43899  ?  108 GLU A CB  1 
ATOM   712  C CG  . GLU A 1 100 ? 54.32400  19.78700  48.75000  1.000 43.66525  ?  108 GLU A CG  1 
ATOM   713  C CD  . GLU A 1 100 ? 55.44900  20.78500  48.56100  1.000 67.16303  ?  108 GLU A CD  1 
ATOM   714  O OE1 . GLU A 1 100 ? 56.61400  20.43900  48.84700  1.000 67.62516  ?  108 GLU A OE1 1 
ATOM   715  O OE2 . GLU A 1 100 ? 55.16800  21.92200  48.12600  1.000 80.89062  -1 108 GLU A OE2 1 
ATOM   716  N N   . ARG A 1 101 ? 54.43400  15.32500  49.65000  1.000 27.84325  ?  109 ARG A N   1 
ATOM   717  C CA  . ARG A 1 101 ? 54.23800  14.10800  50.42300  1.000 26.19747  ?  109 ARG A CA  1 
ATOM   718  C C   . ARG A 1 101 ? 55.23000  13.01000  50.07000  1.000 26.27419  ?  109 ARG A C   1 
ATOM   719  O O   . ARG A 1 101 ? 55.20700  11.95100  50.70400  1.000 26.30278  ?  109 ARG A O   1 
ATOM   720  C CB  . ARG A 1 101 ? 52.81500  13.57700  50.22400  1.000 25.63739  ?  109 ARG A CB  1 
ATOM   721  C CG  . ARG A 1 101 ? 51.71900  14.53000  50.65400  1.000 16.62612  ?  109 ARG A CG  1 
ATOM   722  C CD  . ARG A 1 101 ? 50.36300  14.02800  50.19900  1.000 15.79244  ?  109 ARG A CD  1 
ATOM   723  N NE  . ARG A 1 101 ? 50.25800  14.00600  48.74600  1.000 19.01032  ?  109 ARG A NE  1 
ATOM   724  C CZ  . ARG A 1 101 ? 49.25100  13.46500  48.07500  1.000 21.65267  ?  109 ARG A CZ  1 
ATOM   725  N NH1 . ARG A 1 101 ? 48.23700  12.88900  48.69700  1.000 28.09462  ?  109 ARG A NH1 1 
ATOM   726  N NH2 . ARG A 1 101 ? 49.26300  13.50200  46.74700  1.000 25.70622  ?  109 ARG A NH2 1 
ATOM   727  N N   . GLY A 1 102 ? 56.09700  13.23300  49.08800  1.000 22.66004  ?  110 GLY A N   1 
ATOM   728  C CA  . GLY A 1 102 ? 57.01500  12.20900  48.64100  1.000 30.48540  ?  110 GLY A CA  1 
ATOM   729  C C   . GLY A 1 102 ? 56.45400  11.24600  47.62200  1.000 31.03752  ?  110 GLY A C   1 
ATOM   730  O O   . GLY A 1 102 ? 57.09100  10.22400  47.34300  1.000 32.67157  ?  110 GLY A O   1 
ATOM   731  N N   . LEU A 1 103 ? 55.28600  11.53500  47.05900  1.000 33.69394  ?  111 LEU A N   1 
ATOM   732  C CA  . LEU A 1 103 ? 54.63900  10.67000  46.08500  1.000 28.30216  ?  111 LEU A CA  1 
ATOM   733  C C   . LEU A 1 103 ? 54.90700  11.17800  44.67800  1.000 28.58545  ?  111 LEU A C   1 
ATOM   734  O O   . LEU A 1 103 ? 54.95200  12.38800  44.44000  1.000 29.06149  ?  111 LEU A O   1 
ATOM   735  C CB  . LEU A 1 103 ? 53.13200  10.60400  46.33200  1.000 24.31639  ?  111 LEU A CB  1 
ATOM   736  C CG  . LEU A 1 103 ? 52.68400  10.08300  47.69400  1.000 25.17135  ?  111 LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 103 ? 51.22700  10.41400  47.91800  1.000 25.40943  ?  111 LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 103 ? 52.91300  8.59000   47.78500  1.000 26.22242  ?  111 LEU A CD2 1 
ATOM   739  N N   . SER A 1 104 ? 55.08700  10.24700  43.74700  1.000 27.33664  ?  112 SER A N   1 
ATOM   740  C CA  . SER A 1 104 ? 55.36000  10.62200  42.36900  1.000 26.70429  ?  112 SER A CA  1 
ATOM   741  C C   . SER A 1 104 ? 54.12700  11.24000  41.72500  1.000 26.86663  ?  112 SER A C   1 
ATOM   742  O O   . SER A 1 104 ? 53.01000  10.73700  41.86700  1.000 32.40215  ?  112 SER A O   1 
ATOM   743  C CB  . SER A 1 104 ? 55.81700  9.40500   41.57100  1.000 25.91181  ?  112 SER A CB  1 
ATOM   744  O OG  . SER A 1 104 ? 56.03000  9.73700   40.21200  1.000 28.99499  ?  112 SER A OG  1 
ATOM   745  N N   . GLN A 1 105 ? 54.33900  12.34200  41.01500  1.000 30.46982  ?  113 GLN A N   1 
ATOM   746  C CA  . GLN A 1 105 ? 53.28200  13.01200  40.27500  1.000 31.96640  ?  113 GLN A CA  1 
ATOM   747  C C   . GLN A 1 105 ? 53.12100  12.47000  38.86400  1.000 25.77227  ?  113 GLN A C   1 
ATOM   748  O O   . GLN A 1 105 ? 52.16400  12.84300  38.17900  1.000 26.66939  ?  113 GLN A O   1 
ATOM   749  C CB  . GLN A 1 105 ? 53.55500  14.51800  40.22200  1.000 33.75138  ?  113 GLN A CB  1 
ATOM   750  C CG  . GLN A 1 105 ? 53.53500  15.19700  41.58200  1.000 35.23283  ?  113 GLN A CG  1 
ATOM   751  C CD  . GLN A 1 105 ? 53.88100  16.66900  41.50800  1.000 35.41226  ?  113 GLN A CD  1 
ATOM   752  O OE1 . GLN A 1 105 ? 54.96900  17.04100  41.07400  1.000 34.80508  ?  113 GLN A OE1 1 
ATOM   753  N NE2 . GLN A 1 105 ? 52.95400  17.51500  41.93700  1.000 33.38389  ?  113 GLN A NE2 1 
ATOM   754  N N   . TRP A 1 106 ? 54.03000  11.60900  38.41500  1.000 31.02766  ?  114 TRP A N   1 
ATOM   755  C CA  . TRP A 1 106 ? 53.91500  11.01800  37.09200  1.000 35.26078  ?  114 TRP A CA  1 
ATOM   756  C C   . TRP A 1 106 ? 52.81300  9.97000   37.06400  1.000 37.73986  ?  114 TRP A C   1 
ATOM   757  O O   . TRP A 1 106 ? 52.58700  9.25500   38.04300  1.000 31.86308  ?  114 TRP A O   1 
ATOM   758  C CB  . TRP A 1 106 ? 55.23700  10.38000  36.66900  1.000 31.95632  ?  114 TRP A CB  1 
ATOM   759  C CG  . TRP A 1 106 ? 56.35900  11.34200  36.48400  1.000 35.93119  ?  114 TRP A CG  1 
ATOM   760  C CD1 . TRP A 1 106 ? 57.55400  11.33400  37.13400  1.000 40.77575  ?  114 TRP A CD1 1 
ATOM   761  C CD2 . TRP A 1 106 ? 56.39800  12.45400  35.58500  1.000 33.35656  ?  114 TRP A CD2 1 
ATOM   762  N NE1 . TRP A 1 106 ? 58.33700  12.37000  36.69900  1.000 45.28680  ?  114 TRP A NE1 1 
ATOM   763  C CE2 . TRP A 1 106 ? 57.64900  13.07600  35.74800  1.000 45.33214  ?  114 TRP A CE2 1 
ATOM   764  C CE3 . TRP A 1 106 ? 55.49700  12.98700  34.66000  1.000 34.09956  ?  114 TRP A CE3 1 
ATOM   765  C CZ2 . TRP A 1 106 ? 58.02100  14.20100  35.02200  1.000 35.94079  ?  114 TRP A CZ2 1 
ATOM   766  C CZ3 . TRP A 1 106 ? 55.86800  14.10300  33.94300  1.000 38.48687  ?  114 TRP A CZ3 1 
ATOM   767  C CH2 . TRP A 1 106 ? 57.11900  14.69800  34.12600  1.000 34.96033  ?  114 TRP A CH2 1 
ATOM   768  N N   . ALA A 1 107 ? 52.12900  9.88000   35.92900  1.000 36.22280  ?  115 ALA A N   1 
ATOM   769  C CA  . ALA A 1 107 ? 51.15400  8.82600   35.71400  1.000 32.13485  ?  115 ALA A CA  1 
ATOM   770  C C   . ALA A 1 107 ? 51.84900  7.54400   35.27500  1.000 33.80188  ?  115 ALA A C   1 
ATOM   771  O O   . ALA A 1 107 ? 52.89600  7.57000   34.62500  1.000 38.09585  ?  115 ALA A O   1 
ATOM   772  C CB  . ALA A 1 107 ? 50.12800  9.25200   34.66600  1.000 38.08590  ?  115 ALA A CB  1 
ATOM   773  N N   . ALA A 1 108 ? 51.25600  6.40900   35.64900  1.000 34.25348  ?  116 ALA A N   1 
ATOM   774  C CA  . ALA A 1 108 ? 51.82900  5.12300   35.26900  1.000 33.68782  ?  116 ALA A CA  1 
ATOM   775  C C   . ALA A 1 108 ? 51.54800  4.78700   33.81100  1.000 30.86029  ?  116 ALA A C   1 
ATOM   776  O O   . ALA A 1 108 ? 52.37700  4.14800   33.15400  1.000 32.10661  ?  116 ALA A O   1 
ATOM   777  C CB  . ALA A 1 108 ? 51.29700  4.01900   36.17900  1.000 37.45348  ?  116 ALA A CB  1 
ATOM   778  N N   . LEU A 1 109 ? 50.39600  5.20200   33.29200  1.000 35.25344  ?  117 LEU A N   1 
ATOM   779  C CA  . LEU A 1 109 ? 50.00200  4.91100   31.92200  1.000 35.38836  ?  117 LEU A CA  1 
ATOM   780  C C   . LEU A 1 109 ? 50.44800  5.98400   30.93600  1.000 47.30630  ?  117 LEU A C   1 
ATOM   781  O O   . LEU A 1 109 ? 50.17100  5.86200   29.73900  1.000 45.38741  ?  117 LEU A O   1 
ATOM   782  C CB  . LEU A 1 109 ? 48.48500  4.73500   31.83800  1.000 32.14110  ?  117 LEU A CB  1 
ATOM   783  C CG  . LEU A 1 109 ? 47.85700  3.61800   32.67100  1.000 34.26733  ?  117 LEU A CG  1 
ATOM   784  C CD1 . LEU A 1 109 ? 46.35900  3.58700   32.46200  1.000 28.48560  ?  117 LEU A CD1 1 
ATOM   785  C CD2 . LEU A 1 109 ? 48.47000  2.27600   32.33100  1.000 34.79535  ?  117 LEU A CD2 1 
ATOM   786  N N   . GLY A 1 110 ? 51.12600  7.02600   31.40700  1.000 46.31882  ?  118 GLY A N   1 
ATOM   787  C CA  . GLY A 1 110 ? 51.57000  8.07200   30.50200  1.000 54.55910  ?  118 GLY A CA  1 
ATOM   788  C C   . GLY A 1 110 ? 50.44700  9.03400   30.16600  1.000 64.60842  ?  118 GLY A C   1 
ATOM   789  O O   . GLY A 1 110 ? 49.59500  9.35100   31.00200  1.000 61.33743  ?  118 GLY A O   1 
ATOM   790  N N   . GLU A 1 111 ? 50.44900  9.51500   28.92500  1.000 66.54045  ?  119 GLU A N   1 
ATOM   791  C CA  . GLU A 1 111 ? 49.43100  10.46100  28.49100  1.000 69.08115  ?  119 GLU A CA  1 
ATOM   792  C C   . GLU A 1 111 ? 48.07200  9.78000   28.40400  1.000 50.57705  ?  119 GLU A C   1 
ATOM   793  O O   . GLU A 1 111 ? 47.95200  8.66800   27.88300  1.000 53.34714  ?  119 GLU A O   1 
ATOM   794  C CB  . GLU A 1 111 ? 49.80400  11.07300  27.14200  1.000 76.04132  ?  119 GLU A CB  1 
ATOM   795  C CG  . GLU A 1 111 ? 50.84100  12.18000  27.23000  1.000 78.52966  ?  119 GLU A CG  1 
ATOM   796  C CD  . GLU A 1 111 ? 50.93300  12.99200  25.95500  1.000 90.14284  ?  119 GLU A CD  1 
ATOM   797  O OE1 . GLU A 1 111 ? 50.12700  12.74700  25.03400  1.000 91.80750  ?  119 GLU A OE1 1 
ATOM   798  O OE2 . GLU A 1 111 ? 51.80900  13.87800  25.87500  1.000 94.25604  -1 119 GLU A OE2 1 
ATOM   799  N N   . GLY A 1 112 ? 47.05600  10.45400  28.90700  1.000 46.42312  ?  120 GLY A N   1 
ATOM   800  C CA  . GLY A 1 112 ? 45.71800  9.90300   28.95800  1.000 37.33489  ?  120 GLY A CA  1 
ATOM   801  C C   . GLY A 1 112 ? 44.99800  10.41300  30.18800  1.000 41.67765  ?  120 GLY A C   1 
ATOM   802  O O   . GLY A 1 112 ? 45.51900  11.21500  30.95600  1.000 47.79810  ?  120 GLY A O   1 
ATOM   803  N N   . TYR A 1 113 ? 43.77300  9.92700   30.35600  1.000 38.57466  ?  121 TYR A N   1 
ATOM   804  C CA  . TYR A 1 113 ? 42.96900  10.33500  31.49800  1.000 38.02620  ?  121 TYR A CA  1 
ATOM   805  C C   . TYR A 1 113 ? 43.32400  9.51100   32.72800  1.000 35.08378  ?  121 TYR A C   1 
ATOM   806  O O   . TYR A 1 113 ? 43.53200  8.29800   32.64700  1.000 27.95977  ?  121 TYR A O   1 
ATOM   807  C CB  . TYR A 1 113 ? 41.48100  10.19000  31.18400  1.000 31.30369  ?  121 TYR A CB  1 
ATOM   808  C CG  . TYR A 1 113 ? 40.57400  10.54500  32.34100  1.000 34.74920  ?  121 TYR A CG  1 
ATOM   809  C CD1 . TYR A 1 113 ? 40.19400  11.85800  32.56900  1.000 29.26280  ?  121 TYR A CD1 1 
ATOM   810  C CD2 . TYR A 1 113 ? 40.09700  9.56800   33.20400  1.000 33.10121  ?  121 TYR A CD2 1 
ATOM   811  C CE1 . TYR A 1 113 ? 39.36900  12.18800  33.62200  1.000 28.08371  ?  121 TYR A CE1 1 
ATOM   812  C CE2 . TYR A 1 113 ? 39.27400  9.89100   34.26000  1.000 30.13057  ?  121 TYR A CE2 1 
ATOM   813  C CZ  . TYR A 1 113 ? 38.91200  11.20100  34.46300  1.000 31.97184  ?  121 TYR A CZ  1 
ATOM   814  O OH  . TYR A 1 113 ? 38.09000  11.52700  35.51400  1.000 34.28321  ?  121 TYR A OH  1 
ATOM   815  N N   . ARG A 1 114 ? 43.39700  10.18300  33.87300  1.000 34.45333  ?  122 ARG A N   1 
ATOM   816  C CA  . ARG A 1 114 ? 43.57300  9.53400   35.16300  1.000 30.89192  ?  122 ARG A CA  1 
ATOM   817  C C   . ARG A 1 114 ? 42.42800  9.93900   36.07700  1.000 31.35020  ?  122 ARG A C   1 
ATOM   818  O O   . ARG A 1 114 ? 42.13000  11.12900  36.21500  1.000 36.77828  ?  122 ARG A O   1 
ATOM   819  C CB  . ARG A 1 114 ? 44.91800  9.89800   35.79800  1.000 34.18497  ?  122 ARG A CB  1 
ATOM   820  C CG  . ARG A 1 114 ? 45.13600  9.22600   37.13600  1.000 35.47953  ?  122 ARG A CG  1 
ATOM   821  C CD  . ARG A 1 114 ? 46.53100  9.42900   37.68600  1.000 33.50893  ?  122 ARG A CD  1 
ATOM   822  N NE  . ARG A 1 114 ? 47.21600  10.57500  37.10800  1.000 33.18318  ?  122 ARG A NE  1 
ATOM   823  C CZ  . ARG A 1 114 ? 48.33100  11.09400  37.60100  1.000 32.23581  ?  122 ARG A CZ  1 
ATOM   824  N NH1 . ARG A 1 114 ? 48.90400  10.59500  38.68300  1.000 26.59680  ?  122 ARG A NH1 1 
ATOM   825  N NH2 . ARG A 1 114 ? 48.88200  12.14100  36.99700  1.000 35.70357  ?  122 ARG A NH2 1 
ATOM   826  N N   . ALA A 1 115 ? 41.78900  8.95000   36.69200  1.000 30.16735  ?  123 ALA A N   1 
ATOM   827  C CA  . ALA A 1 115 ? 40.67000  9.21000   37.57800  1.000 27.46603  ?  123 ALA A CA  1 
ATOM   828  C C   . ALA A 1 115 ? 41.15700  9.81000   38.89600  1.000 26.23597  ?  123 ALA A C   1 
ATOM   829  O O   . ALA A 1 115 ? 42.33200  9.68100   39.24900  1.000 24.15799  ?  123 ALA A O   1 
ATOM   830  C CB  . ALA A 1 115 ? 39.89700  7.92200   37.84600  1.000 25.06828  ?  123 ALA A CB  1 
ATOM   831  N N   . PRO A 1 116 ? 40.27500  10.53300  39.61600  1.000 23.99923  ?  124 PRO A N   1 
ATOM   832  C CA  . PRO A 1 116 ? 40.67000  11.09600  40.87800  1.000 21.70307  ?  124 PRO A CA  1 
ATOM   833  C C   . PRO A 1 116 ? 40.90500  9.97200   41.84600  1.000 26.30459  ?  124 PRO A C   1 
ATOM   834  O O   . PRO A 1 116 ? 40.42900  8.85100   41.65000  1.000 24.11137  ?  124 PRO A O   1 
ATOM   835  C CB  . PRO A 1 116 ? 39.44700  11.91500  41.22800  1.000 20.79173  ?  124 PRO A CB  1 
ATOM   836  C CG  . PRO A 1 116 ? 38.80100  12.21800  39.91300  1.000 33.83634  ?  124 PRO A CG  1 
ATOM   837  C CD  . PRO A 1 116 ? 38.89400  10.86800  39.26900  1.000 22.80345  ?  124 PRO A CD  1 
ATOM   838  N N   . GLY A 1 117 ? 41.66300  10.25800  42.88900  1.000 21.07603  ?  125 GLY A N   1 
ATOM   839  C CA  . GLY A 1 117 ? 41.83700  9.24600   43.92900  1.000 25.59342  ?  125 GLY A CA  1 
ATOM   840  C C   . GLY A 1 117 ? 40.65800  9.29100   44.86200  1.000 26.66186  ?  125 GLY A C   1 
ATOM   841  O O   . GLY A 1 117 ? 39.86800  10.24100  44.77900  1.000 25.83304  ?  125 GLY A O   1 
ATOM   842  N N   . ASP A 1 118 ? 40.55300  8.30300   45.75800  1.000 22.94911  ?  126 ASP A N   1 
ATOM   843  C CA  . ASP A 1 118 ? 39.41700  8.23300   46.72200  1.000 24.35084  ?  126 ASP A CA  1 
ATOM   844  C C   . ASP A 1 118 ? 38.11100  8.02700   45.94900  1.000 30.98970  ?  126 ASP A C   1 
ATOM   845  O O   . ASP A 1 118 ? 37.06800  8.55600   46.39300  1.000 32.36883  ?  126 ASP A O   1 
ATOM   846  C CB  . ASP A 1 118 ? 39.36300  9.45000   47.63300  1.000 29.86109  ?  126 ASP A CB  1 
ATOM   847  C CG  . ASP A 1 118 ? 40.52000  9.59000   48.61100  1.000 34.08993  ?  126 ASP A CG  1 
ATOM   848  O OD1 . ASP A 1 118 ? 41.39500  8.70000   48.61200  1.000 32.72094  ?  126 ASP A OD1 1 
ATOM   849  O OD2 . ASP A 1 118 ? 40.53400  10.58700  49.36100  1.000 45.89849  -1 126 ASP A OD2 1 
ATOM   850  N N   . LEU A 1 119 ? 38.16600  7.28500   44.83900  1.000 25.01095  ?  127 LEU A N   1 
ATOM   851  C CA  . LEU A 1 119 ? 36.94700  7.00100   44.05500  1.000 20.54894  ?  127 LEU A CA  1 
ATOM   852  C C   . LEU A 1 119 ? 36.12600  6.01200   44.88100  1.000 24.14076  ?  127 LEU A C   1 
ATOM   853  O O   . LEU A 1 119 ? 36.70700  5.06300   45.42700  1.000 20.70803  ?  127 LEU A O   1 
ATOM   854  C CB  . LEU A 1 119 ? 37.28300  6.41900   42.68800  1.000 20.92582  ?  127 LEU A CB  1 
ATOM   855  C CG  . LEU A 1 119 ? 37.36300  7.40100   41.51700  1.000 32.95200  ?  127 LEU A CG  1 
ATOM   856  C CD1 . LEU A 1 119 ? 37.13200  6.65400   40.22200  1.000 24.85209  ?  127 LEU A CD1 1 
ATOM   857  C CD2 . LEU A 1 119 ? 36.37500  8.53900   41.65600  1.000 29.65362  ?  127 LEU A CD2 1 
ATOM   858  N N   . PRO A 1 120 ? 34.80800  6.22900   45.02300  1.000 27.29877  ?  128 PRO A N   1 
ATOM   859  C CA  . PRO A 1 120 ? 33.98200  5.32800   45.79800  1.000 21.15218  ?  128 PRO A CA  1 
ATOM   860  C C   . PRO A 1 120 ? 34.05400  3.90000   45.28900  1.000 23.31594  ?  128 PRO A C   1 
ATOM   861  O O   . PRO A 1 120 ? 34.26200  3.69400   44.08900  1.000 27.71070  ?  128 PRO A O   1 
ATOM   862  C CB  . PRO A 1 120 ? 32.63200  5.98400   45.58400  1.000 21.95703  ?  128 PRO A CB  1 
ATOM   863  C CG  . PRO A 1 120 ? 32.94900  7.44100   45.43400  1.000 21.47810  ?  128 PRO A CG  1 
ATOM   864  C CD  . PRO A 1 120 ? 34.10500  7.36800   44.47700  1.000 25.79353  ?  128 PRO A CD  1 
ATOM   865  N N   . LEU A 1 121 ? 33.85000  2.92500   46.16800  1.000 19.91175  ?  129 LEU A N   1 
ATOM   866  C CA  . LEU A 1 121 ? 33.98800  1.51900   45.80200  1.000 19.36019  ?  129 LEU A CA  1 
ATOM   867  C C   . LEU A 1 121 ? 33.10400  1.15500   44.61700  1.000 23.13779  ?  129 LEU A C   1 
ATOM   868  O O   . LEU A 1 121 ? 33.47100  0.30100   43.80600  1.000 25.43388  ?  129 LEU A O   1 
ATOM   869  C CB  . LEU A 1 121 ? 33.66700  0.62500   46.99900  1.000 23.85597  ?  129 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 121 ? 33.74300  -0.88100  46.74000  1.000 20.00159  ?  129 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 121 ? 35.13300  -1.28000  46.28300  1.000 17.19561  ?  129 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 121 ? 33.33400  -1.66300  47.97300  1.000 24.24918  ?  129 LEU A CD2 1 
ATOM   873  N N   . ALA A 1 122 ? 31.93400  1.78400   44.49800  1.000 21.43575  ?  130 ALA A N   1 
ATOM   874  C CA  . ALA A 1 122 ? 31.04300  1.46000   43.38800  1.000 22.64647  ?  130 ALA A CA  1 
ATOM   875  C C   . ALA A 1 122 ? 31.64300  1.87700   42.05100  1.000 27.46899  ?  130 ALA A C   1 
ATOM   876  O O   . ALA A 1 122 ? 31.70000  1.07700   41.11000  1.000 27.86323  ?  130 ALA A O   1 
ATOM   877  C CB  . ALA A 1 122 ? 29.68400  2.12400   43.59800  1.000 17.17978  ?  130 ALA A CB  1 
ATOM   878  N N   . GLN A 1 123 ? 32.10200  3.12500   41.95300  1.000 27.34854  ?  131 GLN A N   1 
ATOM   879  C CA  . GLN A 1 123 ? 32.68000  3.61500   40.70600  1.000 28.85668  ?  131 GLN A CA  1 
ATOM   880  C C   . GLN A 1 123 ? 33.96300  2.87100   40.35800  1.000 23.53599  ?  131 GLN A C   1 
ATOM   881  O O   . GLN A 1 123 ? 34.18800  2.50500   39.19600  1.000 25.58986  ?  131 GLN A O   1 
ATOM   882  C CB  . GLN A 1 123 ? 32.93600  5.11600   40.82500  1.000 27.69997  ?  131 GLN A CB  1 
ATOM   883  C CG  . GLN A 1 123 ? 31.68800  5.91400   41.15000  1.000 20.25620  ?  131 GLN A CG  1 
ATOM   884  C CD  . GLN A 1 123 ? 31.97400  7.37900   41.37100  1.000 27.54135  ?  131 GLN A CD  1 
ATOM   885  O OE1 . GLN A 1 123 ? 32.96900  7.90900   40.88300  1.000 37.59911  ?  131 GLN A OE1 1 
ATOM   886  N NE2 . GLN A 1 123 ? 31.10000  8.04600   42.11300  1.000 33.39823  ?  131 GLN A NE2 1 
ATOM   887  N N   . LEU A 1 124 ? 34.81500  2.63700   41.35700  1.000 22.32388  ?  132 LEU A N   1 
ATOM   888  C CA  . LEU A 1 124 ? 36.04000  1.88300   41.12700  1.000 22.09317  ?  132 LEU A CA  1 
ATOM   889  C C   . LEU A 1 124 ? 35.72900  0.45300   40.70500  1.000 25.96750  ?  132 LEU A C   1 
ATOM   890  O O   . LEU A 1 124 ? 36.44400  -0.12900  39.88500  1.000 27.05782  ?  132 LEU A O   1 
ATOM   891  C CB  . LEU A 1 124 ? 36.89900  1.90400   42.38900  1.000 18.61331  ?  132 LEU A CB  1 
ATOM   892  C CG  . LEU A 1 124 ? 38.34400  1.43300   42.26400  1.000 22.59691  ?  132 LEU A CG  1 
ATOM   893  C CD1 . LEU A 1 124 ? 39.07900  2.25600   41.22500  1.000 19.15145  ?  132 LEU A CD1 1 
ATOM   894  C CD2 . LEU A 1 124 ? 39.02700  1.53800   43.60400  1.000 26.67515  ?  132 LEU A CD2 1 
ATOM   895  N N   . LYS A 1 125 ? 34.66100  -0.12600  41.25400  1.000 18.46536  ?  133 LYS A N   1 
ATOM   896  C CA  . LYS A 1 125 ? 34.24100  -1.46400  40.85800  1.000 21.56591  ?  133 LYS A CA  1 
ATOM   897  C C   . LYS A 1 125 ? 33.79100  -1.49300  39.40500  1.000 26.48690  ?  133 LYS A C   1 
ATOM   898  O O   . LYS A 1 125 ? 34.12100  -2.42700  38.66500  1.000 26.88007  ?  133 LYS A O   1 
ATOM   899  C CB  . LYS A 1 125 ? 33.12100  -1.94600  41.77800  1.000 29.35758  ?  133 LYS A CB  1 
ATOM   900  C CG  . LYS A 1 125 ? 32.57700  -3.32000  41.44700  1.000 26.62194  ?  133 LYS A CG  1 
ATOM   901  C CD  . LYS A 1 125 ? 31.44900  -3.69400  42.38600  1.000 21.50139  ?  133 LYS A CD  1 
ATOM   902  C CE  . LYS A 1 125 ? 30.79300  -4.99200  41.96500  1.000 20.79315  ?  133 LYS A CE  1 
ATOM   903  N NZ  . LYS A 1 125 ? 29.64300  -5.33100  42.83800  1.000 23.84514  ?  133 LYS A NZ  1 
ATOM   904  N N   . VAL A 1 126 ? 33.02600  -0.48400  38.98000  1.000 25.80196  ?  134 VAL A N   1 
ATOM   905  C CA  . VAL A 1 126 ? 32.64100  -0.40200  37.57200  1.000 26.84936  ?  134 VAL A CA  1 
ATOM   906  C C   . VAL A 1 126 ? 33.87300  -0.29500  36.68800  1.000 24.13307  ?  134 VAL A C   1 
ATOM   907  O O   . VAL A 1 126 ? 33.95600  -0.93700  35.63500  1.000 23.58726  ?  134 VAL A O   1 
ATOM   908  C CB  . VAL A 1 126 ? 31.67400  0.77000   37.32300  1.000 24.15668  ?  134 VAL A CB  1 
ATOM   909  C CG1 . VAL A 1 126 ? 31.06800  0.63900   35.94600  1.000 26.93107  ?  134 VAL A CG1 1 
ATOM   910  C CG2 . VAL A 1 126 ? 30.56400  0.76700   38.33900  1.000 21.30752  ?  134 VAL A CG2 1 
ATOM   911  N N   . LEU A 1 127 ? 34.84300  0.52500   37.09200  1.000 25.71580  ?  135 LEU A N   1 
ATOM   912  C CA  . LEU A 1 127 ? 36.06800  0.64200   36.30600  1.000 25.12312  ?  135 LEU A CA  1 
ATOM   913  C C   . LEU A 1 127 ? 36.80300  -0.68900  36.22400  1.000 25.04312  ?  135 LEU A C   1 
ATOM   914  O O   . LEU A 1 127 ? 37.28100  -1.07800  35.15400  1.000 21.96373  ?  135 LEU A O   1 
ATOM   915  C CB  . LEU A 1 127 ? 36.97500  1.71700   36.89700  1.000 21.37705  ?  135 LEU A CB  1 
ATOM   916  C CG  . LEU A 1 127 ? 36.55200  3.15400   36.62000  1.000 22.00889  ?  135 LEU A CG  1 
ATOM   917  C CD1 . LEU A 1 127 ? 37.58500  4.11600   37.16400  1.000 23.30982  ?  135 LEU A CD1 1 
ATOM   918  C CD2 . LEU A 1 127 ? 36.34300  3.36200   35.13500  1.000 20.92454  ?  135 LEU A CD2 1 
ATOM   919  N N   . ILE A 1 128 ? 36.89500  -1.40600  37.34500  1.000 25.68191  ?  136 ILE A N   1 
ATOM   920  C CA  . ILE A 1 128 ? 37.62000  -2.67100  37.37200  1.000 24.08457  ?  136 ILE A CA  1 
ATOM   921  C C   . ILE A 1 128 ? 36.92000  -3.72100  36.52000  1.000 23.34985  ?  136 ILE A C   1 
ATOM   922  O O   . ILE A 1 128 ? 37.57600  -4.52700  35.85100  1.000 20.57166  ?  136 ILE A O   1 
ATOM   923  C CB  . ILE A 1 128 ? 37.79800  -3.13900  38.82900  1.000 24.76689  ?  136 ILE A CB  1 
ATOM   924  C CG1 . ILE A 1 128 ? 38.80300  -2.24600  39.55600  1.000 21.16830  ?  136 ILE A CG1 1 
ATOM   925  C CG2 . ILE A 1 128 ? 38.26100  -4.58000  38.88900  1.000 22.54085  ?  136 ILE A CG2 1 
ATOM   926  C CD1 . ILE A 1 128 ? 38.85400  -2.47600  41.04200  1.000 15.83826  ?  136 ILE A CD1 1 
ATOM   927  N N   . GLU A 1 129 ? 35.59000  -3.73000  36.51200  1.000 24.57510  ?  137 GLU A N   1 
ATOM   928  C CA  . GLU A 1 129 ? 34.85800  -4.77000  35.80300  1.000 28.71984  ?  137 GLU A CA  1 
ATOM   929  C C   . GLU A 1 129 ? 34.64700  -4.47500  34.32400  1.000 30.99031  ?  137 GLU A C   1 
ATOM   930  O O   . GLU A 1 129 ? 34.57000  -5.41600  33.52600  1.000 28.07693  ?  137 GLU A O   1 
ATOM   931  C CB  . GLU A 1 129 ? 33.49500  -4.99700  36.46100  1.000 28.95011  ?  137 GLU A CB  1 
ATOM   932  C CG  . GLU A 1 129 ? 33.56000  -5.64200  37.82900  1.000 27.32626  ?  137 GLU A CG  1 
ATOM   933  C CD  . GLU A 1 129 ? 32.19100  -5.82300  38.44400  1.000 34.17225  ?  137 GLU A CD  1 
ATOM   934  O OE1 . GLU A 1 129 ? 31.32900  -4.94500  38.24300  1.000 35.55369  ?  137 GLU A OE1 1 
ATOM   935  O OE2 . GLU A 1 129 ? 31.97700  -6.84100  39.13100  1.000 42.03375  -1 137 GLU A OE2 1 
ATOM   936  N N   . HIS A 1 130 ? 34.55400  -3.20500  33.92500  1.000 30.41446  ?  138 HIS A N   1 
ATOM   937  C CA  . HIS A 1 130 ? 34.08900  -2.87900  32.58100  1.000 26.81482  ?  138 HIS A CA  1 
ATOM   938  C C   . HIS A 1 130 ? 34.96400  -1.91000  31.79800  1.000 30.61166  ?  138 HIS A C   1 
ATOM   939  O O   . HIS A 1 130 ? 34.76700  -1.79500  30.58300  1.000 36.55374  ?  138 HIS A O   1 
ATOM   940  C CB  . HIS A 1 130 ? 32.66200  -2.31700  32.63800  1.000 26.13530  ?  138 HIS A CB  1 
ATOM   941  C CG  . HIS A 1 130 ? 31.67800  -3.25200  33.26600  1.000 28.31809  ?  138 HIS A CG  1 
ATOM   942  N ND1 . HIS A 1 130 ? 31.32400  -4.45300  32.69400  1.000 33.24622  ?  138 HIS A ND1 1 
ATOM   943  C CD2 . HIS A 1 130 ? 30.98400  -3.16900  34.42500  1.000 32.14194  ?  138 HIS A CD2 1 
ATOM   944  C CE1 . HIS A 1 130 ? 30.45000  -5.06800  33.46800  1.000 28.71702  ?  138 HIS A CE1 1 
ATOM   945  N NE2 . HIS A 1 130 ? 30.22500  -4.31000  34.52500  1.000 34.21269  ?  138 HIS A NE2 1 
ATOM   946  N N   . ALA A 1 131 ? 35.90300  -1.21300  32.42500  1.000 30.01642  ?  139 ALA A N   1 
ATOM   947  C CA  . ALA A 1 131 ? 36.81200  -0.35800  31.67700  1.000 23.91430  ?  139 ALA A CA  1 
ATOM   948  C C   . ALA A 1 131 ? 37.95200  -1.18100  31.09400  1.000 26.04846  ?  139 ALA A C   1 
ATOM   949  O O   . ALA A 1 131 ? 38.27700  -2.26400  31.58500  1.000 35.73844  ?  139 ALA A O   1 
ATOM   950  C CB  . ALA A 1 131 ? 37.36900  0.75300   32.56400  1.000 19.30922  ?  139 ALA A CB  1 
ATOM   951  N N   . ARG A 1 132 ? 38.55300  -0.66800  30.02200  1.000 26.57677  ?  140 ARG A N   1 
ATOM   952  C CA  . ARG A 1 132 ? 39.67400  -1.36500  29.40500  1.000 28.63581  ?  140 ARG A CA  1 
ATOM   953  C C   . ARG A 1 132 ? 40.97000  -1.08300  30.15600  1.000 25.89839  ?  140 ARG A C   1 
ATOM   954  O O   . ARG A 1 132 ? 41.54700  -1.98500  30.77100  1.000 34.49398  ?  140 ARG A O   1 
ATOM   955  C CB  . ARG A 1 132 ? 39.81000  -0.96200  27.93700  1.000 27.71291  ?  140 ARG A CB  1 
ATOM   956  C CG  . ARG A 1 132 ? 38.66800  -1.44500  27.06400  1.000 27.50565  ?  140 ARG A CG  1 
ATOM   957  C CD  . ARG A 1 132 ? 39.00100  -1.31300  25.59400  1.000 29.44427  ?  140 ARG A CD  1 
ATOM   958  N NE  . ARG A 1 132 ? 38.00400  -1.96700  24.75700  1.000 41.49803  ?  140 ARG A NE  1 
ATOM   959  C CZ  . ARG A 1 132 ? 38.27800  -2.61900  23.63600  1.000 44.44281  ?  140 ARG A CZ  1 
ATOM   960  N NH1 . ARG A 1 132 ? 39.51500  -2.72300  23.18300  1.000 50.35869  ?  140 ARG A NH1 1 
ATOM   961  N NH2 . ARG A 1 132 ? 37.28600  -3.18100  22.95400  1.000 40.22425  ?  140 ARG A NH2 1 
ATOM   962  N N   . ASP A 1 133 ? 41.41900  0.16500   30.12900  1.000 26.42703  ?  141 ASP A N   1 
ATOM   963  C CA  . ASP A 1 133 ? 42.59200  0.60500   30.86800  1.000 21.96459  ?  141 ASP A CA  1 
ATOM   964  C C   . ASP A 1 133 ? 42.23000  1.84500   31.66800  1.000 27.40880  ?  141 ASP A C   1 
ATOM   965  O O   . ASP A 1 133 ? 41.49100  2.70900   31.18800  1.000 31.28322  ?  141 ASP A O   1 
ATOM   966  C CB  . ASP A 1 133 ? 43.76900  0.91500   29.93900  1.000 17.33587  ?  141 ASP A CB  1 
ATOM   967  C CG  . ASP A 1 133 ? 44.44100  -0.33200  29.40000  1.000 27.57731  ?  141 ASP A CG  1 
ATOM   968  O OD1 . ASP A 1 133 ? 44.10700  -1.44400  29.85300  1.000 24.27712  ?  141 ASP A OD1 1 
ATOM   969  O OD2 . ASP A 1 133 ? 45.32300  -0.19700  28.52900  1.000 30.63351  -1 141 ASP A OD2 1 
ATOM   970  N N   . PHE A 1 134 ? 42.74400  1.92700   32.89100  1.000 24.18301  ?  142 PHE A N   1 
ATOM   971  C CA  . PHE A 1 134 ? 42.44600  3.05900   33.75000  1.000 27.09851  ?  142 PHE A CA  1 
ATOM   972  C C   . PHE A 1 134 ? 43.54100  3.19600   34.79300  1.000 24.89113  ?  142 PHE A C   1 
ATOM   973  O O   . PHE A 1 134 ? 44.33900  2.28300   35.01200  1.000 29.68636  ?  142 PHE A O   1 
ATOM   974  C CB  . PHE A 1 134 ? 41.07500  2.90900   34.42400  1.000 25.85814  ?  142 PHE A CB  1 
ATOM   975  C CG  . PHE A 1 134 ? 41.03000  1.84600   35.48400  1.000 24.71117  ?  142 PHE A CG  1 
ATOM   976  C CD1 . PHE A 1 134 ? 40.80800  0.52500   35.14700  1.000 24.77365  ?  142 PHE A CD1 1 
ATOM   977  C CD2 . PHE A 1 134 ? 41.20100  2.17100   36.81800  1.000 23.77118  ?  142 PHE A CD2 1 
ATOM   978  C CE1 . PHE A 1 134 ? 40.76600  -0.45000  36.11600  1.000 22.66451  ?  142 PHE A CE1 1 
ATOM   979  C CE2 . PHE A 1 134 ? 41.16100  1.19800   37.78900  1.000 21.58261  ?  142 PHE A CE2 1 
ATOM   980  C CZ  . PHE A 1 134 ? 40.94200  -0.11300  37.43800  1.000 22.75916  ?  142 PHE A CZ  1 
ATOM   981  N N   . GLU A 1 135 ? 43.53900  4.36700   35.42100  1.000 23.36059  ?  143 GLU A N   1 
ATOM   982  C CA  . GLU A 1 135 ? 44.51800  4.70000   36.47200  1.000 34.26399  ?  143 GLU A CA  1 
ATOM   983  C C   . GLU A 1 135 ? 43.86300  5.70300   37.42100  1.000 34.46224  ?  143 GLU A C   1 
ATOM   984  O O   . GLU A 1 135 ? 43.01900  6.47700   36.95500  1.000 25.00854  ?  143 GLU A O   1 
ATOM   985  C CB  . GLU A 1 135 ? 45.73500  5.37100   35.84500  1.000 30.34166  ?  143 GLU A CB  1 
ATOM   986  C CG  . GLU A 1 135 ? 46.91300  5.49600   36.80200  1.000 38.04102  ?  143 GLU A CG  1 
ATOM   987  C CD  . GLU A 1 135 ? 48.06300  6.24900   36.18100  1.000 42.10238  ?  143 GLU A CD  1 
ATOM   988  O OE1 . GLU A 1 135 ? 47.99700  6.54600   34.97400  1.000 37.45632  ?  143 GLU A OE1 1 
ATOM   989  O OE2 . GLU A 1 135 ? 49.01800  6.53500   36.92600  1.000 39.61884  -1 143 GLU A OE2 1 
ATOM   990  N N   . THR A 1 136 ? 44.22200  5.66800   38.70100  1.000 29.92716  ?  144 THR A N   1 
ATOM   991  C CA  . THR A 1 136 ? 43.72500  6.62700   39.67100  1.000 30.16621  ?  144 THR A CA  1 
ATOM   992  C C   . THR A 1 136 ? 44.88700  7.36900   40.31400  1.000 32.36098  ?  144 THR A C   1 
ATOM   993  O O   . THR A 1 136 ? 46.01200  6.86800   40.36900  1.000 29.31449  ?  144 THR A O   1 
ATOM   994  C CB  . THR A 1 136 ? 42.89400  5.94000   40.75800  1.000 28.73486  ?  144 THR A CB  1 
ATOM   995  O OG1 . THR A 1 136 ? 43.75800  5.18400   41.61300  1.000 30.86787  ?  144 THR A OG1 1 
ATOM   996  C CG2 . THR A 1 136 ? 41.87100  5.01000   40.13900  1.000 28.83449  ?  144 THR A CG2 1 
ATOM   997  N N   . ASP A 1 137 ? 44.60100  8.57500   40.79500  1.000 29.20954  ?  145 ASP A N   1 
ATOM   998  C CA  . ASP A 1 137 ? 45.59300  9.35900   41.50800  1.000 27.30419  ?  145 ASP A CA  1 
ATOM   999  C C   . ASP A 1 137 ? 45.81300  8.77900   42.90300  1.000 25.89469  ?  145 ASP A C   1 
ATOM   1000 O O   . ASP A 1 137 ? 45.16300  7.81900   43.32200  1.000 29.97270  ?  145 ASP A O   1 
ATOM   1001 C CB  . ASP A 1 137 ? 45.15600  10.81900  41.58700  1.000 30.96290  ?  145 ASP A CB  1 
ATOM   1002 C CG  . ASP A 1 137 ? 46.29100  11.78000  41.33100  1.000 32.33870  ?  145 ASP A CG  1 
ATOM   1003 O OD1 . ASP A 1 137 ? 47.42500  11.49100  41.75900  1.000 32.31095  ?  145 ASP A OD1 1 
ATOM   1004 O OD2 . ASP A 1 137 ? 46.04800  12.83000  40.70400  1.000 42.36119  -1 145 ASP A OD2 1 
ATOM   1005 N N   . TRP A 1 138 ? 46.75100  9.37600   43.62900  1.000 21.46519  ?  146 TRP A N   1 
ATOM   1006 C CA  . TRP A 1 138 ? 47.03700  8.93900   44.98500  1.000 22.45502  ?  146 TRP A CA  1 
ATOM   1007 C C   . TRP A 1 138 ? 45.87800  9.27800   45.91500  1.000 27.64130  ?  146 TRP A C   1 
ATOM   1008 O O   . TRP A 1 138 ? 45.18600  10.28400  45.74400  1.000 27.76372  ?  146 TRP A O   1 
ATOM   1009 C CB  . TRP A 1 138 ? 48.32000  9.58800   45.49500  1.000 23.26165  ?  146 TRP A CB  1 
ATOM   1010 C CG  . TRP A 1 138 ? 49.55900  9.04900   44.86200  1.000 22.90783  ?  146 TRP A CG  1 
ATOM   1011 C CD1 . TRP A 1 138 ? 50.30000  9.63700   43.88400  1.000 19.93034  ?  146 TRP A CD1 1 
ATOM   1012 C CD2 . TRP A 1 138 ? 50.20700  7.81200   45.16800  1.000 26.80914  ?  146 TRP A CD2 1 
ATOM   1013 N NE1 . TRP A 1 138 ? 51.37000  8.84400   43.55900  1.000 21.90266  ?  146 TRP A NE1 1 
ATOM   1014 C CE2 . TRP A 1 138 ? 51.33500  7.71600   44.33400  1.000 27.11262  ?  146 TRP A CE2 1 
ATOM   1015 C CE3 . TRP A 1 138 ? 49.94200  6.77500   46.06600  1.000 20.99638  ?  146 TRP A CE3 1 
ATOM   1016 C CZ2 . TRP A 1 138 ? 52.19800  6.62700   44.37300  1.000 20.99532  ?  146 TRP A CZ2 1 
ATOM   1017 C CZ3 . TRP A 1 138 ? 50.79800  5.69600   46.10000  1.000 22.06211  ?  146 TRP A CZ3 1 
ATOM   1018 C CH2 . TRP A 1 138 ? 51.91100  5.62900   45.26100  1.000 21.09731  ?  146 TRP A CH2 1 
ATOM   1019 N N   . SER A 1 139 ? 45.67400  8.42100   46.91000  1.000 29.42170  ?  147 SER A N   1 
ATOM   1020 C CA  . SER A 1 139 ? 44.60700  8.62500   47.87300  1.000 26.71861  ?  147 SER A CA  1 
ATOM   1021 C C   . SER A 1 139 ? 44.96300  9.77200   48.81500  1.000 30.49041  ?  147 SER A C   1 
ATOM   1022 O O   . SER A 1 139 ? 46.07300  10.31000  48.80000  1.000 26.26560  ?  147 SER A O   1 
ATOM   1023 C CB  . SER A 1 139 ? 44.34500  7.34000   48.65300  1.000 26.45076  ?  147 SER A CB  1 
ATOM   1024 O OG  . SER A 1 139 ? 45.52200  6.88400   49.29600  1.000 23.85157  ?  147 SER A OG  1 
ATOM   1025 N N   . ALA A 1 140 ? 43.99400  10.15800  49.64600  1.000 30.30357  ?  148 ALA A N   1 
ATOM   1026 C CA  . ALA A 1 140 ? 44.23500  11.20500  50.62900  1.000 27.55936  ?  148 ALA A CA  1 
ATOM   1027 C C   . ALA A 1 140 ? 45.25500  10.77600  51.67100  1.000 33.89407  ?  148 ALA A C   1 
ATOM   1028 O O   . ALA A 1 140 ? 45.94400  11.62500  52.24500  1.000 26.37214  ?  148 ALA A O   1 
ATOM   1029 C CB  . ALA A 1 140 ? 42.92500  11.60100  51.30900  1.000 22.95715  ?  148 ALA A CB  1 
ATOM   1030 N N   . GLY A 1 141 ? 45.36600  9.48500   51.92000  1.000 28.71984  ?  149 GLY A N   1 
ATOM   1031 C CA  . GLY A 1 141 ? 46.32900  8.96800   52.86400  1.000 23.38066  ?  149 GLY A CA  1 
ATOM   1032 C C   . GLY A 1 141 ? 45.66600  8.50100   54.14500  1.000 23.74064  ?  149 GLY A C   1 
ATOM   1033 O O   . GLY A 1 141 ? 44.60900  8.99900   54.55300  1.000 25.83353  ?  149 GLY A O   1 
ATOM   1034 N N   . ARG A 1 142 ? 46.23800  7.46900   54.74100  1.000 27.65465  ?  150 ARG A N   1 
ATOM   1035 C CA  . ARG A 1 142 ? 45.75100  6.99300   56.05300  1.000 30.00526  ?  150 ARG A CA  1 
ATOM   1036 C C   . ARG A 1 142 ? 46.97900  7.12200   56.93400  1.000 37.73785  ?  150 ARG A C   1 
ATOM   1037 O O   . ARG A 1 142 ? 47.50800  6.08700   57.36100  1.000 50.55353  ?  150 ARG A O   1 
ATOM   1038 C CB  . ARG A 1 142 ? 45.23900  5.55300   56.03600  1.000 21.41481  ?  150 ARG A CB  1 
ATOM   1039 C CG  . ARG A 1 142 ? 43.89300  5.33400   55.36700  1.000 29.80107  ?  150 ARG A CG  1 
ATOM   1040 C CD  . ARG A 1 142 ? 43.11300  4.30100   56.14800  1.000 34.33328  ?  150 ARG A CD  1 
ATOM   1041 N NE  . ARG A 1 142 ? 42.84900  4.78200   57.50700  1.000 34.61286  ?  150 ARG A NE  1 
ATOM   1042 C CZ  . ARG A 1 142 ? 42.17900  4.09400   58.41700  1.000 40.86266  ?  150 ARG A CZ  1 
ATOM   1043 N NH1 . ARG A 1 142 ? 41.92400  2.81500   58.21700  1.000 36.56395  ?  150 ARG A NH1 1 
ATOM   1044 N NH2 . ARG A 1 142 ? 41.76500  4.68500   59.52200  1.000 39.67653  ?  150 ARG A NH2 1 
ATOM   1045 N N   . GLY A 1 143 ? 47.42300  8.35300   57.16400  1.000 35.84106  ?  151 GLY A N   1 
ATOM   1046 C CA  . GLY A 1 143 ? 48.69300  8.56300   57.86600  1.000 30.57957  ?  151 GLY A CA  1 
ATOM   1047 C C   . GLY A 1 143 ? 49.70700  8.91800   56.81400  1.000 31.28158  ?  151 GLY A C   1 
ATOM   1048 O O   . GLY A 1 143 ? 49.38800  9.74500   55.95200  1.000 30.98693  ?  151 GLY A O   1 
ATOM   1049 N N   . GLU A 1 144 ? 50.86100  8.27500   56.83700  1.000 37.31293  ?  152 GLU A N   1 
ATOM   1050 C CA  . GLU A 1 144 ? 51.86400  8.50400   55.77600  1.000 34.67166  ?  152 GLU A CA  1 
ATOM   1051 C C   . GLU A 1 144 ? 51.78700  7.36400   54.75200  1.000 36.16201  ?  152 GLU A C   1 
ATOM   1052 O O   . GLU A 1 144 ? 52.75100  7.21700   53.99500  1.000 34.13862  ?  152 GLU A O   1 
ATOM   1053 C CB  . GLU A 1 144 ? 53.24900  8.58100   56.40900  1.000 37.66438  ?  152 GLU A CB  1 
ATOM   1054 C CG  . GLU A 1 144 ? 53.47000  9.81000   57.28300  1.000 40.67691  ?  152 GLU A CG  1 
ATOM   1055 C CD  . GLU A 1 144 ? 54.89400  9.87800   57.79900  1.000 55.33655  ?  152 GLU A CD  1 
ATOM   1056 O OE1 . GLU A 1 144 ? 55.29600  8.95900   58.53300  1.000 59.43602  ?  152 GLU A OE1 1 
ATOM   1057 O OE2 . GLU A 1 144 ? 55.60800  10.83900  57.45700  1.000 75.76973  -1 152 GLU A OE2 1 
ATOM   1058 N N   . THR A 1 145 ? 50.68300  6.60700   54.73400  1.000 34.09054  ?  153 THR A N   1 
ATOM   1059 C CA  . THR A 1 145 ? 50.50600  5.50500   53.75900  1.000 30.35687  ?  153 THR A CA  1 
ATOM   1060 C C   . THR A 1 145 ? 49.44700  5.86600   52.74300  1.000 26.36031  ?  153 THR A C   1 
ATOM   1061 O O   . THR A 1 145 ? 48.35000  6.23900   53.16600  1.000 27.45794  ?  153 THR A O   1 
ATOM   1062 C CB  . THR A 1 145 ? 50.25400  4.17300   54.46100  1.000 31.24079  ?  153 THR A CB  1 
ATOM   1063 O OG1 . THR A 1 145 ? 51.38400  3.96600   55.29800  1.000 33.69968  ?  153 THR A OG1 1 
ATOM   1064 C CG2 . THR A 1 145 ? 50.15600  3.01500   53.48800  1.000 28.65676  ?  153 THR A CG2 1 
ATOM   1065 N N   . PHE A 1 146 ? 49.76400  5.74200   51.45600  1.000 26.15485  ?  154 PHE A N   1 
ATOM   1066 C CA  . PHE A 1 146 ? 48.91900  6.11900   50.33300  1.000 25.95488  ?  154 PHE A CA  1 
ATOM   1067 C C   . PHE A 1 146 ? 48.77200  4.93800   49.38200  1.000 28.77922  ?  154 PHE A C   1 
ATOM   1068 O O   . PHE A 1 146 ? 49.54700  3.98200   49.42100  1.000 21.71785  ?  154 PHE A O   1 
ATOM   1069 C CB  . PHE A 1 146 ? 49.50300  7.32800   49.59300  1.000 22.09449  ?  154 PHE A CB  1 
ATOM   1070 C CG  . PHE A 1 146 ? 49.88600  8.46300   50.49500  1.000 26.72288  ?  154 PHE A CG  1 
ATOM   1071 C CD1 . PHE A 1 146 ? 51.12600  8.49500   51.10700  1.000 25.46708  ?  154 PHE A CD1 1 
ATOM   1072 C CD2 . PHE A 1 146 ? 49.00900  9.50300   50.72700  1.000 22.09692  ?  154 PHE A CD2 1 
ATOM   1073 C CE1 . PHE A 1 146 ? 51.47700  9.53400   51.93600  1.000 27.44325  ?  154 PHE A CE1 1 
ATOM   1074 C CE2 . PHE A 1 146 ? 49.35700  10.54400  51.55600  1.000 23.68719  ?  154 PHE A CE2 1 
ATOM   1075 C CZ  . PHE A 1 146 ? 50.59100  10.55900  52.16000  1.000 25.10124  ?  154 PHE A CZ  1 
ATOM   1076 N N   . GLN A 1 147 ? 47.76600  5.01400   48.51400  1.000 28.27715  ?  155 GLN A N   1 
ATOM   1077 C CA  . GLN A 1 147 ? 47.47500  3.91800   47.60200  1.000 22.44016  ?  155 GLN A CA  1 
ATOM   1078 C C   . GLN A 1 147 ? 47.04500  4.46300   46.24700  1.000 21.43257  ?  155 GLN A C   1 
ATOM   1079 O O   . GLN A 1 147 ? 46.53300  5.58100   46.14900  1.000 17.61120  ?  155 GLN A O   1 
ATOM   1080 C CB  . GLN A 1 147 ? 46.38100  3.00400   48.16800  1.000 20.22456  ?  155 GLN A CB  1 
ATOM   1081 C CG  . GLN A 1 147 ? 44.98300  3.34000   47.68200  1.000 19.67649  ?  155 GLN A CG  1 
ATOM   1082 C CD  . GLN A 1 147 ? 43.93300  3.17000   48.75100  1.000 29.67845  ?  155 GLN A CD  1 
ATOM   1083 O OE1 . GLN A 1 147 ? 44.24100  2.84000   49.89300  1.000 43.87393  ?  155 GLN A OE1 1 
ATOM   1084 N NE2 . GLN A 1 147 ? 42.68000  3.40100   48.38700  1.000 37.12261  ?  155 GLN A NE2 1 
ATOM   1085 N N   . ARG A 1 148 ? 47.27700  3.66600   45.20700  1.000 18.94723  ?  156 ARG A N   1 
ATOM   1086 C CA  . ARG A 1 148 ? 46.72000  3.92700   43.88700  1.000 20.81037  ?  156 ARG A CA  1 
ATOM   1087 C C   . ARG A 1 148 ? 46.67600  2.61900   43.11100  1.000 23.61881  ?  156 ARG A C   1 
ATOM   1088 O O   . ARG A 1 148 ? 47.26100  1.61400   43.52000  1.000 23.02495  ?  156 ARG A O   1 
ATOM   1089 C CB  . ARG A 1 148 ? 47.51000  4.99800   43.12300  1.000 24.12188  ?  156 ARG A CB  1 
ATOM   1090 C CG  . ARG A 1 148 ? 48.94200  4.64600   42.78000  1.000 21.13452  ?  156 ARG A CG  1 
ATOM   1091 C CD  . ARG A 1 148 ? 49.54400  5.72900   41.90300  1.000 18.47799  ?  156 ARG A CD  1 
ATOM   1092 N NE  . ARG A 1 148 ? 50.95500  5.50300   41.61900  1.000 21.11370  ?  156 ARG A NE  1 
ATOM   1093 C CZ  . ARG A 1 148 ? 51.69300  6.27700   40.83600  1.000 24.60812  ?  156 ARG A CZ  1 
ATOM   1094 N NH1 . ARG A 1 148 ? 51.17800  7.32900   40.22200  1.000 26.38627  ?  156 ARG A NH1 1 
ATOM   1095 N NH2 . ARG A 1 148 ? 52.97900  5.99000   40.66600  1.000 27.55581  ?  156 ARG A NH2 1 
ATOM   1096 N N   . VAL A 1 149 ? 45.95200  2.63100   41.99500  1.000 19.72443  ?  157 VAL A N   1 
ATOM   1097 C CA  . VAL A 1 149 ? 45.72900  1.42700   41.20300  1.000 22.11826  ?  157 VAL A CA  1 
ATOM   1098 C C   . VAL A 1 149 ? 45.68200  1.80200   39.72800  1.000 26.42280  ?  157 VAL A C   1 
ATOM   1099 O O   . VAL A 1 149 ? 45.15200  2.85400   39.35900  1.000 30.69014  ?  157 VAL A O   1 
ATOM   1100 C CB  . VAL A 1 149 ? 44.43700  0.70100   41.64000  1.000 20.56523  ?  157 VAL A CB  1 
ATOM   1101 C CG1 . VAL A 1 149 ? 43.23200  1.61400   41.51100  1.000 21.47947  ?  157 VAL A CG1 1 
ATOM   1102 C CG2 . VAL A 1 149 ? 44.23700  -0.57500  40.84800  1.000 20.36154  ?  157 VAL A CG2 1 
ATOM   1103 N N   . TRP A 1 150 ? 46.25400  0.94400   38.88500  1.000 25.62665  ?  158 TRP A N   1 
ATOM   1104 C CA  . TRP A 1 150 ? 46.19900  1.15200   37.44400  1.000 24.17598  ?  158 TRP A CA  1 
ATOM   1105 C C   . TRP A 1 150 ? 46.24900  -0.18700  36.72800  1.000 26.15027  ?  158 TRP A C   1 
ATOM   1106 O O   . TRP A 1 150 ? 46.93600  -1.10800  37.16200  1.000 24.88415  ?  158 TRP A O   1 
ATOM   1107 C CB  . TRP A 1 150 ? 47.33800  2.05300   36.95400  1.000 22.81114  ?  158 TRP A CB  1 
ATOM   1108 C CG  . TRP A 1 150 ? 48.69700  1.44500   36.99700  1.000 24.51907  ?  158 TRP A CG  1 
ATOM   1109 C CD1 . TRP A 1 150 ? 49.31900  0.75900   36.00100  1.000 24.36613  ?  158 TRP A CD1 1 
ATOM   1110 C CD2 . TRP A 1 150 ? 49.61800  1.49200   38.08800  1.000 24.50358  ?  158 TRP A CD2 1 
ATOM   1111 N NE1 . TRP A 1 150 ? 50.56700  0.36300   36.40800  1.000 28.74968  ?  158 TRP A NE1 1 
ATOM   1112 C CE2 . TRP A 1 150 ? 50.77400  0.80300   37.68800  1.000 27.58908  ?  158 TRP A CE2 1 
ATOM   1113 C CE3 . TRP A 1 150 ? 49.57300  2.04500   39.36900  1.000 27.28787  ?  158 TRP A CE3 1 
ATOM   1114 C CZ2 . TRP A 1 150 ? 51.87500  0.65100   38.52100  1.000 29.51814  ?  158 TRP A CZ2 1 
ATOM   1115 C CZ3 . TRP A 1 150 ? 50.66400  1.89400   40.19200  1.000 27.28850  ?  158 TRP A CZ3 1 
ATOM   1116 C CH2 . TRP A 1 150 ? 51.80000  1.20200   39.76800  1.000 30.91437  ?  158 TRP A CH2 1 
ATOM   1117 N N   . ARG A 1 151 ? 45.53200  -0.28200  35.61400  1.000 24.71795  ?  159 ARG A N   1 
ATOM   1118 C CA  . ARG A 1 151 ? 45.52100  -1.49500  34.81000  1.000 23.10431  ?  159 ARG A CA  1 
ATOM   1119 C C   . ARG A 1 151 ? 46.07700  -1.21600  33.42400  1.000 21.01447  ?  159 ARG A C   1 
ATOM   1120 O O   . ARG A 1 151 ? 45.69800  -0.23700  32.77600  1.000 26.86649  ?  159 ARG A O   1 
ATOM   1121 C CB  . ARG A 1 151 ? 44.11600  -2.07600  34.67900  1.000 24.45830  ?  159 ARG A CB  1 
ATOM   1122 C CG  . ARG A 1 151 ? 44.05600  -3.27700  33.75500  1.000 29.82180  ?  159 ARG A CG  1 
ATOM   1123 C CD  . ARG A 1 151 ? 42.79000  -4.06400  33.95800  1.000 28.45247  ?  159 ARG A CD  1 
ATOM   1124 N NE  . ARG A 1 151 ? 41.61000  -3.22900  33.79000  1.000 29.37745  ?  159 ARG A NE  1 
ATOM   1125 C CZ  . ARG A 1 151 ? 40.43700  -3.48600  34.34700  1.000 29.30986  ?  159 ARG A CZ  1 
ATOM   1126 N NH1 . ARG A 1 151 ? 40.25800  -4.54300  35.11800  1.000 30.08924  ?  159 ARG A NH1 1 
ATOM   1127 N NH2 . ARG A 1 151 ? 39.42200  -2.65900  34.12900  1.000 25.84865  ?  159 ARG A NH2 1 
ATOM   1128 N N   . LYS A 1 152 ? 46.97500  -2.08700  32.97600  1.000 21.46832  ?  160 LYS A N   1 
ATOM   1129 C CA  . LYS A 1 152 ? 47.48500  -2.05800  31.61100  1.000 25.13744  ?  160 LYS A CA  1 
ATOM   1130 C C   . LYS A 1 152 ? 47.26800  -3.43800  31.00800  1.000 26.71188  ?  160 LYS A C   1 
ATOM   1131 O O   . LYS A 1 152 ? 47.73000  -4.44100  31.56300  1.000 29.94649  ?  160 LYS A O   1 
ATOM   1132 C CB  . LYS A 1 152 ? 48.96000  -1.66400  31.56800  1.000 30.34727  ?  160 LYS A CB  1 
ATOM   1133 C CG  . LYS A 1 152 ? 49.36400  -0.96500  30.28100  1.000 29.82761  ?  160 LYS A CG  1 
ATOM   1134 C CD  . LYS A 1 152 ? 50.86900  -0.95100  30.09900  1.000 43.99496  ?  160 LYS A CD  1 
ATOM   1135 C CE  . LYS A 1 152 ? 51.27300  -0.03500  28.95400  1.000 60.52859  ?  160 LYS A CE  1 
ATOM   1136 N NZ  . LYS A 1 152 ? 52.73400  0.25000   28.94700  1.000 71.10194  ?  160 LYS A NZ  1 
ATOM   1137 N N   . GLY A 1 153 ? 46.55500  -3.48500  29.88700  1.000 24.97367  ?  161 GLY A N   1 
ATOM   1138 C CA  . GLY A 1 153 ? 46.28700  -4.73500  29.21100  1.000 23.46797  ?  161 GLY A CA  1 
ATOM   1139 C C   . GLY A 1 153 ? 45.57200  -5.74400  30.08200  1.000 27.37208  ?  161 GLY A C   1 
ATOM   1140 O O   . GLY A 1 153 ? 44.38900  -5.58600  30.39500  1.000 34.36382  ?  161 GLY A O   1 
ATOM   1141 N N   . ASP A 1 154 ? 46.29000  -6.78800  30.48000  1.000 30.77341  ?  162 ASP A N   1 
ATOM   1142 C CA  . ASP A 1 154 ? 45.73400  -7.86700  31.27800  1.000 25.84547  ?  162 ASP A CA  1 
ATOM   1143 C C   . ASP A 1 154 ? 46.20400  -7.83200  32.72500  1.000 29.00613  ?  162 ASP A C   1 
ATOM   1144 O O   . ASP A 1 154 ? 45.86300  -8.73300  33.49500  1.000 31.10247  ?  162 ASP A O   1 
ATOM   1145 C CB  . ASP A 1 154 ? 46.08900  -9.21500  30.64700  1.000 26.47624  ?  162 ASP A CB  1 
ATOM   1146 C CG  . ASP A 1 154 ? 45.15300  -10.32500 31.07300  1.000 43.50240  ?  162 ASP A CG  1 
ATOM   1147 O OD1 . ASP A 1 154 ? 44.01300  -10.02100 31.47800  1.000 49.80381  ?  162 ASP A OD1 1 
ATOM   1148 O OD2 . ASP A 1 154 ? 45.55700  -11.50400 31.00200  1.000 43.20376  -1 162 ASP A OD2 1 
ATOM   1149 N N   . THR A 1 155 ? 46.96900  -6.81700  33.12000  1.000 24.73185  ?  163 THR A N   1 
ATOM   1150 C CA  . THR A 1 155 ? 47.57300  -6.78500  34.44500  1.000 24.78922  ?  163 THR A CA  1 
ATOM   1151 C C   . THR A 1 155 ? 47.10600  -5.55700  35.21300  1.000 25.60724  ?  163 THR A C   1 
ATOM   1152 O O   . THR A 1 155 ? 47.16200  -4.43400  34.70100  1.000 27.01420  ?  163 THR A O   1 
ATOM   1153 C CB  . THR A 1 155 ? 49.10200  -6.80700  34.35800  1.000 25.96646  ?  163 THR A CB  1 
ATOM   1154 O OG1 . THR A 1 155 ? 49.51500  -7.86500  33.48600  1.000 28.27246  ?  163 THR A OG1 1 
ATOM   1155 C CG2 . THR A 1 155 ? 49.70100  -7.05100  35.72700  1.000 23.24853  ?  163 THR A CG2 1 
ATOM   1156 N N   . LEU A 1 156 ? 46.66000  -5.78200  36.44500  1.000 20.61542  ?  164 LEU A N   1 
ATOM   1157 C CA  . LEU A 1 156 ? 46.26500  -4.73100  37.37000  1.000 20.46257  ?  164 LEU A CA  1 
ATOM   1158 C C   . LEU A 1 156 ? 47.34500  -4.57400  38.43200  1.000 22.58544  ?  164 LEU A C   1 
ATOM   1159 O O   . LEU A 1 156 ? 47.81600  -5.56700  38.99100  1.000 22.98250  ?  164 LEU A O   1 
ATOM   1160 C CB  . LEU A 1 156 ? 44.92300  -5.06700  38.02100  1.000 21.06642  ?  164 LEU A CB  1 
ATOM   1161 C CG  . LEU A 1 156 ? 44.26700  -4.04900  38.95200  1.000 22.81656  ?  164 LEU A CG  1 
ATOM   1162 C CD1 . LEU A 1 156 ? 43.62900  -2.93000  38.16100  1.000 28.28653  ?  164 LEU A CD1 1 
ATOM   1163 C CD2 . LEU A 1 156 ? 43.23800  -4.72900  39.82800  1.000 19.69870  ?  164 LEU A CD2 1 
ATOM   1164 N N   . PHE A 1 157 ? 47.73800  -3.33500  38.70400  1.000 22.23295  ?  165 PHE A N   1 
ATOM   1165 C CA  . PHE A 1 157 ? 48.78200  -3.01700  39.66600  1.000 25.21422  ?  165 PHE A CA  1 
ATOM   1166 C C   . PHE A 1 157 ? 48.17700  -2.16900  40.77500  1.000 21.44960  ?  165 PHE A C   1 
ATOM   1167 O O   . PHE A 1 157 ? 47.58200  -1.12000  40.50100  1.000 22.36377  ?  165 PHE A O   1 
ATOM   1168 C CB  . PHE A 1 157 ? 49.93800  -2.25900  39.01000  1.000 27.04746  ?  165 PHE A CB  1 
ATOM   1169 C CG  . PHE A 1 157 ? 50.48200  -2.90900  37.76900  1.000 24.03179  ?  165 PHE A CG  1 
ATOM   1170 C CD1 . PHE A 1 157 ? 49.81100  -2.81500  36.56200  1.000 24.55565  ?  165 PHE A CD1 1 
ATOM   1171 C CD2 . PHE A 1 157 ? 51.68400  -3.58800  37.80500  1.000 20.47288  ?  165 PHE A CD2 1 
ATOM   1172 C CE1 . PHE A 1 157 ? 50.31600  -3.40300  35.42800  1.000 23.38101  ?  165 PHE A CE1 1 
ATOM   1173 C CE2 . PHE A 1 157 ? 52.19300  -4.17500  36.67200  1.000 18.86863  ?  165 PHE A CE2 1 
ATOM   1174 C CZ  . PHE A 1 157 ? 51.51000  -4.08000  35.48300  1.000 22.42595  ?  165 PHE A CZ  1 
ATOM   1175 N N   . VAL A 1 158 ? 48.33900  -2.61700  42.01600  1.000 17.27709  ?  166 VAL A N   1 
ATOM   1176 C CA  . VAL A 1 158 ? 47.92600  -1.86600  43.19300  1.000 27.07094  ?  166 VAL A CA  1 
ATOM   1177 C C   . VAL A 1 158 ? 49.19300  -1.47600  43.94000  1.000 25.58521  ?  166 VAL A C   1 
ATOM   1178 O O   . VAL A 1 158 ? 49.91700  -2.34200  44.44300  1.000 16.31319  ?  166 VAL A O   1 
ATOM   1179 C CB  . VAL A 1 158 ? 46.98100  -2.67700  44.08800  1.000 28.22133  ?  166 VAL A CB  1 
ATOM   1180 C CG1 . VAL A 1 158 ? 46.46700  -1.81900  45.22800  1.000 27.79786  ?  166 VAL A CG1 1 
ATOM   1181 C CG2 . VAL A 1 158 ? 45.82900  -3.23700  43.27300  1.000 20.38667  ?  166 VAL A CG2 1 
ATOM   1182 N N   . GLU A 1 159 ? 49.46900  -0.17900  44.01100  1.000 28.79120  ?  167 GLU A N   1 
ATOM   1183 C CA  . GLU A 1 159 ? 50.66600  0.34000   44.65300  1.000 24.75306  ?  167 GLU A CA  1 
ATOM   1184 C C   . GLU A 1 159 ? 50.29700  0.98100   45.98200  1.000 21.09525  ?  167 GLU A C   1 
ATOM   1185 O O   . GLU A 1 159 ? 49.44600  1.87600   46.03000  1.000 22.24538  ?  167 GLU A O   1 
ATOM   1186 C CB  . GLU A 1 159 ? 51.37200  1.35800   43.75500  1.000 21.59281  ?  167 GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 159 ? 52.61300  1.96800   44.37400  1.000 23.44698  ?  167 GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 159 ? 53.25600  3.00300   43.48100  1.000 24.23004  ?  167 GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 159 ? 52.69600  3.28900   42.40600  1.000 21.81067  ?  167 GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 159 ? 54.32000  3.53700   43.85500  1.000 25.23486  -1 167 GLU A OE2 1 
ATOM   1191 N N   . VAL A 1 160 ? 50.93500  0.51800   47.05300  1.000 16.00948  ?  168 VAL A N   1 
ATOM   1192 C CA  . VAL A 1 160 ? 50.79700  1.10000   48.38100  1.000 21.58736  ?  168 VAL A CA  1 
ATOM   1193 C C   . VAL A 1 160 ? 52.15600  1.64500   48.78700  1.000 24.61694  ?  168 VAL A C   1 
ATOM   1194 O O   . VAL A 1 160 ? 53.13600  0.89500   48.85000  1.000 21.25974  ?  168 VAL A O   1 
ATOM   1195 C CB  . VAL A 1 160 ? 50.28600  0.07200   49.40700  1.000 26.16702  ?  168 VAL A CB  1 
ATOM   1196 C CG1 . VAL A 1 160 ? 50.17800  0.70600   50.78100  1.000 20.97681  ?  168 VAL A CG1 1 
ATOM   1197 C CG2 . VAL A 1 160 ? 48.94500  -0.48800  48.97000  1.000 18.93967  ?  168 VAL A CG2 1 
ATOM   1198 N N   . ALA A 1 161 ? 52.21600  2.94300   49.05700  1.000 26.92826  ?  169 ALA A N   1 
ATOM   1199 C CA  . ALA A 1 161 ? 53.47800  3.62700   49.28500  1.000 25.21185  ?  169 ALA A CA  1 
ATOM   1200 C C   . ALA A 1 161 ? 53.45200  4.38100   50.60300  1.000 20.06910  ?  169 ALA A C   1 
ATOM   1201 O O   . ALA A 1 161 ? 52.51000  5.12100   50.88700  1.000 25.69802  ?  169 ALA A O   1 
ATOM   1202 C CB  . ALA A 1 161 ? 53.79000  4.60300   48.14700  1.000 21.41624  ?  169 ALA A CB  1 
ATOM   1203 N N   . ARG A 1 162 ? 54.50100  4.19600   51.40000  1.000 22.43285  ?  170 ARG A N   1 
ATOM   1204 C CA  . ARG A 1 162 ? 54.77700  5.04300   52.55700  1.000 29.75494  ?  170 ARG A CA  1 
ATOM   1205 C C   . ARG A 1 162 ? 56.09900  5.73600   52.27100  1.000 35.79041  ?  170 ARG A C   1 
ATOM   1206 O O   . ARG A 1 162 ? 57.17500  5.17100   52.51200  1.000 25.44582  ?  170 ARG A O   1 
ATOM   1207 C CB  . ARG A 1 162 ? 54.83300  4.24100   53.85400  1.000 25.50917  ?  170 ARG A CB  1 
ATOM   1208 C CG  . ARG A 1 162 ? 54.99900  5.11200   55.08300  1.000 31.37912  ?  170 ARG A CG  1 
ATOM   1209 C CD  . ARG A 1 162 ? 55.14900  4.29400   56.34600  1.000 40.92619  ?  170 ARG A CD  1 
ATOM   1210 N NE  . ARG A 1 162 ? 55.66800  5.10100   57.44300  1.000 42.26790  ?  170 ARG A NE  1 
ATOM   1211 C CZ  . ARG A 1 162 ? 55.83700  4.66100   58.68200  1.000 56.83038  ?  170 ARG A CZ  1 
ATOM   1212 N NH1 . ARG A 1 162 ? 55.53200  3.42100   59.02300  1.000 56.88394  ?  170 ARG A NH1 1 
ATOM   1213 N NH2 . ARG A 1 162 ? 56.32000  5.48900   59.60300  1.000 48.45256  ?  170 ARG A NH2 1 
ATOM   1214 N N   . PRO A 1 163 ? 56.05700  6.95500   51.73800  1.000 35.07931  ?  171 PRO A N   1 
ATOM   1215 C CA  . PRO A 1 163 ? 57.29100  7.62500   51.31600  1.000 31.81010  ?  171 PRO A CA  1 
ATOM   1216 C C   . PRO A 1 163 ? 58.27100  7.79500   52.46500  1.000 31.56653  ?  171 PRO A C   1 
ATOM   1217 O O   . PRO A 1 163 ? 57.89400  8.14200   53.58600  1.000 34.87526  ?  171 PRO A O   1 
ATOM   1218 C CB  . PRO A 1 163 ? 56.79300  8.97500   50.79400  1.000 25.66764  ?  171 PRO A CB  1 
ATOM   1219 C CG  . PRO A 1 163 ? 55.39600  8.72000   50.38900  1.000 28.04031  ?  171 PRO A CG  1 
ATOM   1220 C CD  . PRO A 1 163 ? 54.86000  7.72400   51.36400  1.000 26.91672  ?  171 PRO A CD  1 
ATOM   1221 N N   . ALA A 1 164 ? 59.54400  7.54800   52.17200  1.000 31.28256  ?  172 ALA A N   1 
ATOM   1222 C CA  . ALA A 1 164 ? 60.60900  7.66700   53.15800  1.000 38.37896  ?  172 ALA A CA  1 
ATOM   1223 C C   . ALA A 1 164 ? 61.93500  7.74700   52.42600  1.000 44.87064  ?  172 ALA A C   1 
ATOM   1224 O O   . ALA A 1 164 ? 62.27500  6.84600   51.65500  1.000 44.56392  ?  172 ALA A O   1 
ATOM   1225 C CB  . ALA A 1 164 ? 60.60300  6.48400   54.13000  1.000 34.45721  ?  172 ALA A CB  1 
ATOM   1226 N N   . SER A 1 165 ? 62.67500  8.82500   52.65600  1.000 43.96457  ?  173 SER A N   1 
ATOM   1227 C CA  . SER A 1 165 ? 64.03800  8.90200   52.15800  1.000 40.96833  ?  173 SER A CA  1 
ATOM   1228 C C   . SER A 1 165 ? 64.92700  7.94500   52.94100  1.000 44.99030  ?  173 SER A C   1 
ATOM   1229 O O   . SER A 1 165 ? 64.57700  7.49200   54.03300  1.000 45.97711  ?  173 SER A O   1 
ATOM   1230 C CB  . SER A 1 165 ? 64.56700  10.33000  52.27100  1.000 38.14748  ?  173 SER A CB  1 
ATOM   1231 O OG  . SER A 1 165 ? 64.78400  10.68500  53.62400  1.000 32.21216  ?  173 SER A OG  1 
ATOM   1232 N N   . ALA A 1 166 ? 66.08600  7.62300   52.36300  1.000 43.33162  ?  174 ALA A N   1 
ATOM   1233 C CA  . ALA A 1 166 ? 67.05500  6.80200   53.07800  1.000 32.69497  ?  174 ALA A CA  1 
ATOM   1234 C C   . ALA A 1 166 ? 67.44700  7.45700   54.39300  1.000 42.79673  ?  174 ALA A C   1 
ATOM   1235 O O   . ALA A 1 166 ? 67.64100  6.77700   55.40900  1.000 46.13763  ?  174 ALA A O   1 
ATOM   1236 C CB  . ALA A 1 166 ? 68.28500  6.56400   52.20600  1.000 33.75151  ?  174 ALA A CB  1 
ATOM   1237 N N   . GLU A 1 167 ? 67.54600  8.78600   54.39400  1.000 42.27042  ?  175 GLU A N   1 
ATOM   1238 C CA  . GLU A 1 167 ? 67.85400  9.51800   55.61500  1.000 46.47841  ?  175 GLU A CA  1 
ATOM   1239 C C   . GLU A 1 167 ? 66.75900  9.32700   56.65800  1.000 44.28767  ?  175 GLU A C   1 
ATOM   1240 O O   . GLU A 1 167 ? 67.04200  9.19200   57.85100  1.000 46.68721  ?  175 GLU A O   1 
ATOM   1241 C CB  . GLU A 1 167 ? 68.05100  10.99800  55.28600  1.000 47.56337  ?  175 GLU A CB  1 
ATOM   1242 C CG  . GLU A 1 167 ? 68.27500  11.89800  56.48300  1.000 54.21248  ?  175 GLU A CG  1 
ATOM   1243 C CD  . GLU A 1 167 ? 68.64100  13.31000  56.07500  1.000 63.24631  ?  175 GLU A CD  1 
ATOM   1244 O OE1 . GLU A 1 167 ? 68.46700  13.64700  54.88600  1.000 57.09258  ?  175 GLU A OE1 1 
ATOM   1245 O OE2 . GLU A 1 167 ? 69.10400  14.08200  56.94000  1.000 68.16373  -1 175 GLU A OE2 1 
ATOM   1246 N N   . ALA A 1 168 ? 65.49700  9.30500   56.22200  1.000 37.45652  ?  176 ALA A N   1 
ATOM   1247 C CA  . ALA A 1 168 ? 64.39200  9.11000   57.15700  1.000 38.05350  ?  176 ALA A CA  1 
ATOM   1248 C C   . ALA A 1 168 ? 64.43600  7.72700   57.79600  1.000 41.04530  ?  176 ALA A C   1 
ATOM   1249 O O   . ALA A 1 168 ? 64.23200  7.58500   59.01000  1.000 44.43346  ?  176 ALA A O   1 
ATOM   1250 C CB  . ALA A 1 168 ? 63.06100  9.32600   56.44000  1.000 36.53425  ?  176 ALA A CB  1 
ATOM   1251 N N   . ALA A 1 169 ? 64.69100  6.69200   56.99400  1.000 41.34217  ?  177 ALA A N   1 
ATOM   1252 C CA  . ALA A 1 169 ? 64.79800  5.34200   57.53900  1.000 40.22029  ?  177 ALA A CA  1 
ATOM   1253 C C   . ALA A 1 169 ? 65.97600  5.23000   58.49600  1.000 44.03659  ?  177 ALA A C   1 
ATOM   1254 O O   . ALA A 1 169 ? 65.87100  4.60100   59.55900  1.000 51.25347  ?  177 ALA A O   1 
ATOM   1255 C CB  . ALA A 1 169 ? 64.92700  4.33000   56.40300  1.000 33.52005  ?  177 ALA A CB  1 
ATOM   1256 N N   . LEU A 1 170 ? 67.10800  5.83900   58.13700  1.000 40.30495  ?  178 LEU A N   1 
ATOM   1257 C CA  . LEU A 1 170 ? 68.26200  5.83200   59.02600  1.000 38.72730  ?  178 LEU A CA  1 
ATOM   1258 C C   . LEU A 1 170 ? 67.95700  6.56000   60.32900  1.000 45.39042  ?  178 LEU A C   1 
ATOM   1259 O O   . LEU A 1 170 ? 68.41000  6.14500   61.39900  1.000 43.86261  ?  178 LEU A O   1 
ATOM   1260 C CB  . LEU A 1 170 ? 69.46400  6.45800   58.32300  1.000 38.23728  ?  178 LEU A CB  1 
ATOM   1261 C CG  . LEU A 1 170 ? 70.11400  5.60400   57.23600  1.000 40.22431  ?  178 LEU A CG  1 
ATOM   1262 C CD1 . LEU A 1 170 ? 71.05400  6.43800   56.38800  1.000 25.24595  ?  178 LEU A CD1 1 
ATOM   1263 C CD2 . LEU A 1 170 ? 70.84300  4.42700   57.85600  1.000 39.87603  ?  178 LEU A CD2 1 
ATOM   1264 N N   . SER A 1 171 ? 67.19000  7.65000   60.25900  1.000 40.88517  ?  179 SER A N   1 
ATOM   1265 C CA  . SER A 1 171 ? 66.81100  8.37800   61.46600  1.000 41.07864  ?  179 SER A CA  1 
ATOM   1266 C C   . SER A 1 171 ? 65.90800  7.53600   62.35700  1.000 41.42722  ?  179 SER A C   1 
ATOM   1267 O O   . SER A 1 171 ? 66.03700  7.55300   63.58700  1.000 54.30537  ?  179 SER A O   1 
ATOM   1268 C CB  . SER A 1 171 ? 66.12700  9.69000   61.08800  1.000 47.20543  ?  179 SER A CB  1 
ATOM   1269 O OG  . SER A 1 171 ? 65.30000  10.15400  62.13900  1.000 60.89495  ?  179 SER A OG  1 
ATOM   1270 N N   . LYS A 1 172 ? 64.97000  6.80400   61.75300  1.000 47.52236  ?  180 LYS A N   1 
ATOM   1271 C CA  . LYS A 1 172 ? 64.11600  5.91400   62.53600  1.000 53.79154  ?  180 LYS A CA  1 
ATOM   1272 C C   . LYS A 1 172 ? 64.94500  4.83500   63.22500  1.000 52.11670  ?  180 LYS A C   1 
ATOM   1273 O O   . LYS A 1 172 ? 64.74500  4.53500   64.41200  1.000 54.89121  ?  180 LYS A O   1 
ATOM   1274 C CB  . LYS A 1 172 ? 63.04800  5.28800   61.63800  1.000 44.35792  ?  180 LYS A CB  1 
ATOM   1275 C CG  . LYS A 1 172 ? 61.85700  4.73400   62.39700  1.000 50.71409  ?  180 LYS A CG  1 
ATOM   1276 C CD  . LYS A 1 172 ? 60.60100  4.72800   61.54300  1.000 60.45422  ?  180 LYS A CD  1 
ATOM   1277 C CE  . LYS A 1 172 ? 59.35200  4.72700   62.41200  1.000 58.55435  ?  180 LYS A CE  1 
ATOM   1278 N NZ  . LYS A 1 172 ? 58.31300  3.78800   61.91100  1.000 54.05443  ?  180 LYS A NZ  1 
ATOM   1279 N N   . ALA A 1 173 ? 65.90000  4.25600   62.49600  1.000 47.76992  ?  181 ALA A N   1 
ATOM   1280 C CA  . ALA A 1 173 ? 66.78400  3.25800   63.09100  1.000 49.41988  ?  181 ALA A CA  1 
ATOM   1281 C C   . ALA A 1 173 ? 67.62000  3.86300   64.21300  1.000 51.41729  ?  181 ALA A C   1 
ATOM   1282 O O   . ALA A 1 173 ? 67.88100  3.21200   65.23100  1.000 46.42705  ?  181 ALA A O   1 
ATOM   1283 C CB  . ALA A 1 173 ? 67.68200  2.65200   62.01500  1.000 48.43206  ?  181 ALA A CB  1 
ATOM   1284 N N   . ALA A 1 174 ? 68.07100  5.10700   64.02800  1.000 55.55184  ?  182 ALA A N   1 
ATOM   1285 C CA  . ALA A 1 174 ? 68.84900  5.78800   65.05700  1.000 53.69875  ?  182 ALA A CA  1 
ATOM   1286 C C   . ALA A 1 174 ? 68.02700  5.99700   66.31900  1.000 54.43582  ?  182 ALA A C   1 
ATOM   1287 O O   . ALA A 1 174 ? 68.52100  5.78800   67.43400  1.000 58.95963  ?  182 ALA A O   1 
ATOM   1288 C CB  . ALA A 1 174 ? 69.36200  7.12500   64.52400  1.000 53.03163  ?  182 ALA A CB  1 
ATOM   1289 N N   . TRP A 1 175 ? 66.77100  6.41200   66.16200  1.000 52.83445  ?  183 TRP A N   1 
ATOM   1290 C CA  . TRP A 1 175 ? 65.88100  6.51900   67.31200  1.000 66.24186  ?  183 TRP A CA  1 
ATOM   1291 C C   . TRP A 1 175 ? 65.74800  5.17600   68.01400  1.000 69.08235  ?  183 TRP A C   1 
ATOM   1292 O O   . TRP A 1 175 ? 65.80000  5.09600   69.24800  1.000 67.90606  ?  183 TRP A O   1 
ATOM   1293 C CB  . TRP A 1 175 ? 64.51100  7.03500   66.87100  1.000 63.36461  ?  183 TRP A CB  1 
ATOM   1294 C CG  . TRP A 1 175 ? 63.61200  7.40000   68.01300  1.000 76.92872  ?  183 TRP A CG  1 
ATOM   1295 C CD1 . TRP A 1 175 ? 63.76800  8.44000   68.87700  1.000 82.14328  ?  183 TRP A CD1 1 
ATOM   1296 C CD2 . TRP A 1 175 ? 62.41600  6.72100   68.41500  1.000 91.87520  ?  183 TRP A CD2 1 
ATOM   1297 N NE1 . TRP A 1 175 ? 62.74700  8.45300   69.79400  1.000 94.13987  ?  183 TRP A NE1 1 
ATOM   1298 C CE2 . TRP A 1 175 ? 61.90200  7.40800   69.53100  1.000 96.43361  ?  183 TRP A CE2 1 
ATOM   1299 C CE3 . TRP A 1 175 ? 61.73000  5.60000   67.93900  1.000 89.26579  ?  183 TRP A CE3 1 
ATOM   1300 C CZ2 . TRP A 1 175 ? 60.73400  7.01200   70.17900  1.000 99.53700  ?  183 TRP A CZ2 1 
ATOM   1301 C CZ3 . TRP A 1 175 ? 60.57200  5.20800   68.58300  1.000 87.87351  ?  183 TRP A CZ3 1 
ATOM   1302 C CH2 . TRP A 1 175 ? 60.08600  5.91200   69.69000  1.000 94.02268  ?  183 TRP A CH2 1 
ATOM   1303 N N   . LYS A 1 176 ? 65.59800  4.10200   67.23600  1.000 63.65485  ?  184 LYS A N   1 
ATOM   1304 C CA  . LYS A 1 176 ? 65.44600  2.77900   67.83500  1.000 62.40111  ?  184 LYS A CA  1 
ATOM   1305 C C   . LYS A 1 176 ? 66.68100  2.38300   68.64100  1.000 64.98291  ?  184 LYS A C   1 
ATOM   1306 O O   . LYS A 1 176 ? 66.56300  1.92000   69.78300  1.000 64.25925  ?  184 LYS A O   1 
ATOM   1307 C CB  . LYS A 1 176 ? 65.15700  1.74500   66.74900  1.000 54.07851  ?  184 LYS A CB  1 
ATOM   1308 C CG  . LYS A 1 176 ? 63.79800  1.08200   66.87700  1.000 54.55842  ?  184 LYS A CG  1 
ATOM   1309 C CD  . LYS A 1 176 ? 62.76200  1.79800   66.02500  1.000 66.13127  ?  184 LYS A CD  1 
ATOM   1310 C CE  . LYS A 1 176 ? 61.50700  0.96000   65.84600  1.000 58.26691  ?  184 LYS A CE  1 
ATOM   1311 N NZ  . LYS A 1 176 ? 60.73200  0.84300   67.11100  1.000 47.35697  ?  184 LYS A NZ  1 
ATOM   1312 N N   . VAL A 1 177 ? 67.87600  2.56600   68.07300  1.000 65.05445  ?  185 VAL A N   1 
ATOM   1313 C CA  . VAL A 1 177 ? 69.08600  2.12200   68.76400  1.000 58.92240  ?  185 VAL A CA  1 
ATOM   1314 C C   . VAL A 1 177 ? 69.35600  2.99200   69.98600  1.000 64.47060  ?  185 VAL A C   1 
ATOM   1315 O O   . VAL A 1 177 ? 69.83000  2.50300   71.01800  1.000 63.87960  ?  185 VAL A O   1 
ATOM   1316 C CB  . VAL A 1 177 ? 70.30000  2.09200   67.81600  1.000 47.75622  ?  185 VAL A CB  1 
ATOM   1317 C CG1 . VAL A 1 177 ? 70.21400  0.90200   66.88700  1.000 58.37648  ?  185 VAL A CG1 1 
ATOM   1318 C CG2 . VAL A 1 177 ? 70.43700  3.37700   67.05100  1.000 48.02541  ?  185 VAL A CG2 1 
ATOM   1319 N N   . ILE A 1 178 ? 69.07400  4.29400   69.89000  1.000 58.45728  ?  186 ILE A N   1 
ATOM   1320 C CA  . ILE A 1 178 ? 69.24700  5.16000   71.05200  1.000 52.93119  ?  186 ILE A CA  1 
ATOM   1321 C C   . ILE A 1 178 ? 68.28900  4.75300   72.16300  1.000 63.16504  ?  186 ILE A C   1 
ATOM   1322 O O   . ILE A 1 178 ? 68.65600  4.73600   73.34400  1.000 73.95192  ?  186 ILE A O   1 
ATOM   1323 C CB  . ILE A 1 178 ? 69.07400  6.63700   70.65500  1.000 59.31277  ?  186 ILE A CB  1 
ATOM   1324 C CG1 . ILE A 1 178 ? 70.31200  7.12300   69.90300  1.000 64.33239  ?  186 ILE A CG1 1 
ATOM   1325 C CG2 . ILE A 1 178 ? 68.83800  7.50000   71.87900  1.000 66.13948  ?  186 ILE A CG2 1 
ATOM   1326 C CD1 . ILE A 1 178 ? 70.19500  8.52600   69.37200  1.000 57.27213  ?  186 ILE A CD1 1 
ATOM   1327 N N   . ALA A 1 179 ? 67.05100  4.40300   71.80700  1.000 64.37824  ?  187 ALA A N   1 
ATOM   1328 C CA  . ALA A 1 179 ? 66.13000  3.88500   72.81200  1.000 68.06013  ?  187 ALA A CA  1 
ATOM   1329 C C   . ALA A 1 179 ? 66.59900  2.54500   73.36600  1.000 70.74919  ?  187 ALA A C   1 
ATOM   1330 O O   . ALA A 1 179 ? 66.24800  2.18700   74.49600  1.000 69.61803  ?  187 ALA A O   1 
ATOM   1331 C CB  . ALA A 1 179 ? 64.72600  3.75700   72.22500  1.000 60.87682  ?  187 ALA A CB  1 
ATOM   1332 N N   . SER A 1 180 ? 67.38500  1.79700   72.59500  1.000 68.12363  ?  188 SER A N   1 
ATOM   1333 C CA  . SER A 1 180 ? 67.89000  0.50100   73.03300  1.000 70.27772  ?  188 SER A CA  1 
ATOM   1334 C C   . SER A 1 180 ? 69.14900  0.59700   73.88800  1.000 76.93399  ?  188 SER A C   1 
ATOM   1335 O O   . SER A 1 180 ? 69.52800  -0.39900  74.51600  1.000 71.67243  ?  188 SER A O   1 
ATOM   1336 C CB  . SER A 1 180 ? 68.16000  -0.38600  71.81100  1.000 77.12918  ?  188 SER A CB  1 
ATOM   1337 O OG  . SER A 1 180 ? 69.26800  -1.24500  72.01300  1.000 78.10447  ?  188 SER A OG  1 
ATOM   1338 N N   . ILE A 1 181 ? 69.78700  1.76700   73.95300  1.000 78.56903  ?  189 ILE A N   1 
ATOM   1339 C CA  . ILE A 1 181 ? 71.06200  1.89500   74.65400  1.000 80.34562  ?  189 ILE A CA  1 
ATOM   1340 C C   . ILE A 1 181 ? 70.84700  1.70100   76.14800  1.000 85.63536  ?  189 ILE A C   1 
ATOM   1341 O O   . ILE A 1 181 ? 69.96400  2.32200   76.75200  1.000 84.90505  ?  189 ILE A O   1 
ATOM   1342 C CB  . ILE A 1 181 ? 71.70800  3.24900   74.35000  1.000 67.48855  ?  189 ILE A CB  1 
ATOM   1343 C CG1 . ILE A 1 181 ? 72.31700  3.24100   72.94800  1.000 59.57549  ?  189 ILE A CG1 1 
ATOM   1344 C CG2 . ILE A 1 181 ? 72.76600  3.58500   75.38700  1.000 76.85510  ?  189 ILE A CG2 1 
ATOM   1345 C CD1 . ILE A 1 181 ? 73.08000  4.49500   72.61000  1.000 60.87651  ?  189 ILE A CD1 1 
ATOM   1346 N N   . LYS A 1 182 ? 71.65900  0.83100   76.75500  1.000 88.76461  ?  190 LYS A N   1 
ATOM   1347 C CA  . LYS A 1 182 ? 71.53700  0.56100   78.18200  1.000 85.60736  ?  190 LYS A CA  1 
ATOM   1348 C C   . LYS A 1 182 ? 72.31500  1.55900   79.02900  1.000 84.55438  ?  190 LYS A C   1 
ATOM   1349 O O   . LYS A 1 182 ? 71.99600  1.74300   80.20900  1.000 80.97348  ?  190 LYS A O   1 
ATOM   1350 C CB  . LYS A 1 182 ? 72.00200  -0.86300  78.48900  1.000 88.62356  ?  190 LYS A CB  1 
ATOM   1351 C CG  . LYS A 1 182 ? 71.10000  -1.94300  77.91300  1.000 97.78171  ?  190 LYS A CG  1 
ATOM   1352 C CD  . LYS A 1 182 ? 71.54600  -3.32900  78.34500  1.000 110.75322 ?  190 LYS A CD  1 
ATOM   1353 C CE  . LYS A 1 182 ? 70.63200  -4.40100  77.77400  1.000 110.48406 ?  190 LYS A CE  1 
ATOM   1354 N NZ  . LYS A 1 182 ? 71.06000  -5.77000  78.17500  1.000 108.12834 ?  190 LYS A NZ  1 
ATOM   1355 N N   . ASP A 1 183 ? 73.33000  2.20400   78.46000  1.000 84.29068  ?  191 ASP A N   1 
ATOM   1356 C CA  . ASP A 1 183 ? 74.09500  3.22400   79.17400  1.000 88.97933  ?  191 ASP A CA  1 
ATOM   1357 C C   . ASP A 1 183 ? 73.23900  4.48100   79.24900  1.000 94.52120  ?  191 ASP A C   1 
ATOM   1358 O O   . ASP A 1 183 ? 73.17400  5.26200   78.29800  1.000 93.36175  ?  191 ASP A O   1 
ATOM   1359 C CB  . ASP A 1 183 ? 75.42200  3.49000   78.47200  1.000 84.87331  ?  191 ASP A CB  1 
ATOM   1360 C CG  . ASP A 1 183 ? 76.37000  4.33300   79.30600  1.000 87.01443  ?  191 ASP A CG  1 
ATOM   1361 O OD1 . ASP A 1 183 ? 75.94500  4.86200   80.35400  1.000 89.06434  ?  191 ASP A OD1 1 
ATOM   1362 O OD2 . ASP A 1 183 ? 77.54700  4.46800   78.91000  1.000 82.04182  -1 191 ASP A OD2 1 
ATOM   1363 N N   . ARG A 1 184 ? 72.57700  4.67900   80.39300  1.000 93.66123  ?  192 ARG A N   1 
ATOM   1364 C CA  . ARG A 1 184 ? 71.63300  5.78300   80.53100  1.000 95.31220  ?  192 ARG A CA  1 
ATOM   1365 C C   . ARG A 1 184 ? 72.31200  7.13900   80.38500  1.000 89.54417  ?  192 ARG A C   1 
ATOM   1366 O O   . ARG A 1 184 ? 71.77100  8.03300   79.72400  1.000 90.82606  ?  192 ARG A O   1 
ATOM   1367 C CB  . ARG A 1 184 ? 70.91400  5.68700   81.87600  1.000 93.61654  ?  192 ARG A CB  1 
ATOM   1368 C CG  . ARG A 1 184 ? 70.05200  4.44100   82.02800  1.000 97.59287  ?  192 ARG A CG  1 
ATOM   1369 C CD  . ARG A 1 184 ? 68.90400  4.43600   81.03000  1.000 103.33683 ?  192 ARG A CD  1 
ATOM   1370 N NE  . ARG A 1 184 ? 68.10900  3.21600   81.10500  1.000 111.07096 ?  192 ARG A NE  1 
ATOM   1371 C CZ  . ARG A 1 184 ? 67.01100  2.99200   80.39400  1.000 117.84206 ?  192 ARG A CZ  1 
ATOM   1372 N NH1 . ARG A 1 184 ? 66.53600  3.89500   79.55200  1.000 115.48478 ?  192 ARG A NH1 1 
ATOM   1373 N NH2 . ARG A 1 184 ? 66.37200  1.83400   80.53400  1.000 119.08376 ?  192 ARG A NH2 1 
ATOM   1374 N N   . ALA A 1 185 ? 73.48900  7.31400   80.98900  1.000 91.21577  ?  193 ALA A N   1 
ATOM   1375 C CA  . ALA A 1 185 ? 74.20900  8.57300   80.84000  1.000 93.53290  ?  193 ALA A CA  1 
ATOM   1376 C C   . ALA A 1 185 ? 74.59400  8.81700   79.38700  1.000 92.60254  ?  193 ALA A C   1 
ATOM   1377 O O   . ALA A 1 185 ? 74.46900  9.94100   78.88500  1.000 89.45650  ?  193 ALA A O   1 
ATOM   1378 C CB  . ALA A 1 185 ? 75.44700  8.58000   81.73400  1.000 85.29816  ?  193 ALA A CB  1 
ATOM   1379 N N   . PHE A 1 186 ? 75.05300  7.77300   78.69300  1.000 90.08897  ?  194 PHE A N   1 
ATOM   1380 C CA  . PHE A 1 186 ? 75.43000  7.92400   77.29200  1.000 86.25519  ?  194 PHE A CA  1 
ATOM   1381 C C   . PHE A 1 186 ? 74.22900  8.27600   76.42400  1.000 87.10976  ?  194 PHE A C   1 
ATOM   1382 O O   . PHE A 1 186 ? 74.32700  9.13800   75.54500  1.000 77.80959  ?  194 PHE A O   1 
ATOM   1383 C CB  . PHE A 1 186 ? 76.10000  6.64800   76.78700  1.000 83.89134  ?  194 PHE A CB  1 
ATOM   1384 C CG  . PHE A 1 186 ? 76.71600  6.78700   75.42600  1.000 77.96185  ?  194 PHE A CG  1 
ATOM   1385 C CD1 . PHE A 1 186 ? 77.47600  7.89700   75.10700  1.000 69.85263  ?  194 PHE A CD1 1 
ATOM   1386 C CD2 . PHE A 1 186 ? 76.54500  5.80100   74.47100  1.000 74.42510  ?  194 PHE A CD2 1 
ATOM   1387 C CE1 . PHE A 1 186 ? 78.04800  8.02700   73.86000  1.000 65.19106  ?  194 PHE A CE1 1 
ATOM   1388 C CE2 . PHE A 1 186 ? 77.11700  5.92300   73.22200  1.000 71.47096  ?  194 PHE A CE2 1 
ATOM   1389 C CZ  . PHE A 1 186 ? 77.86800  7.03800   72.91600  1.000 70.73911  ?  194 PHE A CZ  1 
ATOM   1390 N N   . GLN A 1 187 ? 73.08600  7.62400   76.65200  1.000 88.32250  ?  195 GLN A N   1 
ATOM   1391 C CA  . GLN A 1 187 ? 71.90900  7.91100   75.83700  1.000 84.12778  ?  195 GLN A CA  1 
ATOM   1392 C C   . GLN A 1 187 ? 71.37100  9.30600   76.12900  1.000 83.85678  ?  195 GLN A C   1 
ATOM   1393 O O   . GLN A 1 187 ? 70.89300  10.00000  75.22500  1.000 81.00077  ?  195 GLN A O   1 
ATOM   1394 C CB  . GLN A 1 187 ? 70.83200  6.84400   76.05400  1.000 84.37871  ?  195 GLN A CB  1 
ATOM   1395 C CG  . GLN A 1 187 ? 69.99100  7.01500   77.30700  1.000 90.33467  ?  195 GLN A CG  1 
ATOM   1396 C CD  . GLN A 1 187 ? 68.92600  5.95000   77.44500  1.000 87.83364  ?  195 GLN A CD  1 
ATOM   1397 O OE1 . GLN A 1 187 ? 68.07100  6.02500   78.32500  1.000 90.54610  ?  195 GLN A OE1 1 
ATOM   1398 N NE2 . GLN A 1 187 ? 68.96400  4.95800   76.56700  1.000 83.08803  ?  195 GLN A NE2 1 
ATOM   1399 N N   . ARG A 1 188 ? 71.45700  9.74600   77.38600  1.000 85.89866  ?  196 ARG A N   1 
ATOM   1400 C CA  . ARG A 1 188 ? 71.02900  11.10100  77.71500  1.000 90.88326  ?  196 ARG A CA  1 
ATOM   1401 C C   . ARG A 1 188 ? 71.94800  12.13400  77.07400  1.000 87.83021  ?  196 ARG A C   1 
ATOM   1402 O O   . ARG A 1 188 ? 71.48400  13.16700  76.57500  1.000 80.66322  ?  196 ARG A O   1 
ATOM   1403 C CB  . ARG A 1 188 ? 70.97100  11.27500  79.23300  1.000 93.72274  ?  196 ARG A CB  1 
ATOM   1404 C CG  . ARG A 1 188 ? 69.74200  10.62800  79.86200  1.000 101.77992 ?  196 ARG A CG  1 
ATOM   1405 C CD  . ARG A 1 188 ? 69.70300  10.79800  81.37400  1.000 108.16005 ?  196 ARG A CD  1 
ATOM   1406 N NE  . ARG A 1 188 ? 68.52000  10.17100  81.95400  1.000 102.96921 ?  196 ARG A NE  1 
ATOM   1407 C CZ  . ARG A 1 188 ? 68.31400  10.01000  83.25400  1.000 96.64719  ?  196 ARG A CZ  1 
ATOM   1408 N NH1 . ARG A 1 188 ? 69.20300  10.41000  84.14900  1.000 101.89913 ?  196 ARG A NH1 1 
ATOM   1409 N NH2 . ARG A 1 188 ? 67.19000  9.43200   83.66600  1.000 78.98293  ?  196 ARG A NH2 1 
ATOM   1410 N N   . GLU A 1 189 ? 73.25500  11.86400  77.06000  1.000 86.30098  ?  197 GLU A N   1 
ATOM   1411 C CA  . GLU A 1 189 ? 74.18600  12.75100  76.37200  1.000 82.42059  ?  197 GLU A CA  1 
ATOM   1412 C C   . GLU A 1 189 ? 73.89300  12.79300  74.87700  1.000 84.77946  ?  197 GLU A C   1 
ATOM   1413 O O   . GLU A 1 189 ? 73.91000  13.86300  74.25600  1.000 82.19813  ?  197 GLU A O   1 
ATOM   1414 C CB  . GLU A 1 189 ? 75.62200  12.29600  76.63400  1.000 78.16007  ?  197 GLU A CB  1 
ATOM   1415 C CG  . GLU A 1 189 ? 76.57200  13.41300  77.03600  1.000 92.00882  ?  197 GLU A CG  1 
ATOM   1416 C CD  . GLU A 1 189 ? 77.03900  14.23900  75.85500  1.000 94.83727  ?  197 GLU A CD  1 
ATOM   1417 O OE1 . GLU A 1 189 ? 77.68000  13.66700  74.95000  1.000 98.97638  ?  197 GLU A OE1 1 
ATOM   1418 O OE2 . GLU A 1 189 ? 76.76900  15.45800  75.83400  1.000 84.43512  -1 197 GLU A OE2 1 
ATOM   1419 N N   . LEU A 1 190 ? 73.60900  11.63100  74.28300  1.000 85.19017  ?  198 LEU A N   1 
ATOM   1420 C CA  . LEU A 1 190 ? 73.28900  11.58300  72.86100  1.000 78.72258  ?  198 LEU A CA  1 
ATOM   1421 C C   . LEU A 1 190 ? 72.01700  12.35900  72.55500  1.000 72.56085  ?  198 LEU A C   1 
ATOM   1422 O O   . LEU A 1 190 ? 71.93100  13.03500  71.52800  1.000 70.63670  ?  198 LEU A O   1 
ATOM   1423 C CB  . LEU A 1 190 ? 73.15400  10.13600  72.39100  1.000 74.92409  ?  198 LEU A CB  1 
ATOM   1424 C CG  . LEU A 1 190 ? 74.45200  9.40700   72.04900  1.000 73.09958  ?  198 LEU A CG  1 
ATOM   1425 C CD1 . LEU A 1 190 ? 74.38300  7.96900   72.51400  1.000 74.68754  ?  198 LEU A CD1 1 
ATOM   1426 C CD2 . LEU A 1 190 ? 74.72700  9.47700   70.55900  1.000 67.15251  ?  198 LEU A CD2 1 
ATOM   1427 N N   . MET A 1 191 ? 71.01600  12.27000  73.43200  1.000 77.72187  ?  199 MET A N   1 
ATOM   1428 C CA  . MET A 1 191 ? 69.79800  13.05300  73.24400  1.000 74.62363  ?  199 MET A CA  1 
ATOM   1429 C C   . MET A 1 191 ? 70.07700  14.54700  73.37300  1.000 75.63828  ?  199 MET A C   1 
ATOM   1430 O O   . MET A 1 191 ? 69.49500  15.36500  72.64700  1.000 72.78038  ?  199 MET A O   1 
ATOM   1431 C CB  . MET A 1 191 ? 68.73500  12.61100  74.24800  1.000 72.20618  ?  199 MET A CB  1 
ATOM   1432 C CG  . MET A 1 191 ? 67.95500  11.37500  73.82400  1.000 75.66752  ?  199 MET A CG  1 
ATOM   1433 S SD  . MET A 1 191 ? 67.36400  10.41600  75.23200  1.000 102.96902 ?  199 MET A SD  1 
ATOM   1434 C CE  . MET A 1 191 ? 66.53500  9.06300   74.40400  1.000 72.87281  ?  199 MET A CE  1 
ATOM   1435 N N   . ARG A 1 192 ? 70.96200  14.92300  74.30000  1.000 82.44909  ?  200 ARG A N   1 
ATOM   1436 C CA  . ARG A 1 192 ? 71.32400  16.33000  74.44000  1.000 79.38494  ?  200 ARG A CA  1 
ATOM   1437 C C   . ARG A 1 192 ? 71.99200  16.85300  73.17300  1.000 76.97778  ?  200 ARG A C   1 
ATOM   1438 O O   . ARG A 1 192 ? 71.71300  17.97500  72.73500  1.000 76.48131  ?  200 ARG A O   1 
ATOM   1439 C CB  . ARG A 1 192 ? 72.22800  16.52400  75.66100  1.000 86.48103  ?  200 ARG A CB  1 
ATOM   1440 C CG  . ARG A 1 192 ? 73.43900  17.41800  75.43100  1.000 89.22445  ?  200 ARG A CG  1 
ATOM   1441 C CD  . ARG A 1 192 ? 74.21300  17.66400  76.72100  1.000 81.84845  ?  200 ARG A CD  1 
ATOM   1442 N NE  . ARG A 1 192 ? 73.53200  18.61100  77.59600  1.000 101.35842 ?  200 ARG A NE  1 
ATOM   1443 C CZ  . ARG A 1 192 ? 73.91000  18.89700  78.83500  1.000 105.06629 ?  200 ARG A CZ  1 
ATOM   1444 N NH1 . ARG A 1 192 ? 74.97200  18.32800  79.38300  1.000 93.13691  ?  200 ARG A NH1 1 
ATOM   1445 N NH2 . ARG A 1 192 ? 73.20700  19.77700  79.54200  1.000 88.71099  ?  200 ARG A NH2 1 
ATOM   1446 N N   . ARG A 1 193 ? 72.87300  16.05300  72.56400  1.000 81.25776  ?  201 ARG A N   1 
ATOM   1447 C CA  . ARG A 1 193 ? 73.46300  16.46600  71.29000  1.000 76.85433  ?  201 ARG A CA  1 
ATOM   1448 C C   . ARG A 1 193 ? 72.44700  16.42300  70.15500  1.000 76.61753  ?  201 ARG A C   1 
ATOM   1449 O O   . ARG A 1 193 ? 72.53800  17.22000  69.21200  1.000 76.93127  ?  201 ARG A O   1 
ATOM   1450 C CB  . ARG A 1 193 ? 74.67700  15.60300  70.93700  1.000 73.48304  ?  201 ARG A CB  1 
ATOM   1451 C CG  . ARG A 1 193 ? 75.86100  15.75400  71.86600  1.000 85.01073  ?  201 ARG A CG  1 
ATOM   1452 C CD  . ARG A 1 193 ? 77.05300  14.91800  71.40500  1.000 81.59793  ?  201 ARG A CD  1 
ATOM   1453 N NE  . ARG A 1 193 ? 78.22400  15.00300  72.27400  1.000 85.53010  ?  201 ARG A NE  1 
ATOM   1454 C CZ  . ARG A 1 193 ? 79.14400  15.96000  72.24700  1.000 97.31989  ?  201 ARG A CZ  1 
ATOM   1455 N NH1 . ARG A 1 193 ? 79.02700  17.01900  71.46200  1.000 104.56170 ?  201 ARG A NH1 1 
ATOM   1456 N NH2 . ARG A 1 193 ? 80.19700  15.86600  73.05300  1.000 103.42815 ?  201 ARG A NH2 1 
ATOM   1457 N N   . SER A 1 194 ? 71.48800  15.49600  70.21500  1.000 77.74057  ?  202 SER A N   1 
ATOM   1458 C CA  . SER A 1 194 ? 70.47800  15.39800  69.17100  1.000 74.85205  ?  202 SER A CA  1 
ATOM   1459 C C   . SER A 1 194 ? 69.57700  16.61900  69.13700  1.000 76.51426  ?  202 SER A C   1 
ATOM   1460 O O   . SER A 1 194 ? 69.25500  17.08600  68.04400  1.000 79.00267  ?  202 SER A O   1 
ATOM   1461 C CB  . SER A 1 194 ? 69.63400  14.13400  69.34800  1.000 74.05241  ?  202 SER A CB  1 
ATOM   1462 O OG  . SER A 1 194 ? 68.63800  14.30600  70.33800  1.000 64.37079  ?  202 SER A OG  1 
ATOM   1463 N N   . GLU A 1 195 ? 69.20000  17.15300  70.30500  1.000 82.71955  ?  203 GLU A N   1 
ATOM   1464 C CA  . GLU A 1 195 ? 68.41700  18.38700  70.34900  1.000 78.85270  ?  203 GLU A CA  1 
ATOM   1465 C C   . GLU A 1 195 ? 69.03500  19.48700  69.49200  1.000 78.55217  ?  203 GLU A C   1 
ATOM   1466 O O   . GLU A 1 195 ? 68.32000  20.37200  69.01000  1.000 74.74631  ?  203 GLU A O   1 
ATOM   1467 C CB  . GLU A 1 195 ? 68.27700  18.88300  71.78800  1.000 75.66553  ?  203 GLU A CB  1 
ATOM   1468 C CG  . GLU A 1 195 ? 67.61000  17.91000  72.74000  1.000 86.34679  ?  203 GLU A CG  1 
ATOM   1469 C CD  . GLU A 1 195 ? 67.66500  18.38500  74.18000  1.000 83.22949  ?  203 GLU A CD  1 
ATOM   1470 O OE1 . GLU A 1 195 ? 68.09300  19.53500  74.41100  1.000 78.09929  ?  203 GLU A OE1 1 
ATOM   1471 O OE2 . GLU A 1 195 ? 67.28200  17.60800  75.08000  1.000 78.34694  -1 203 GLU A OE2 1 
ATOM   1472 N N   . LYS A 1 196 ? 70.35100  19.44800  69.29200  1.000 79.92563  ?  204 LYS A N   1 
ATOM   1473 C CA  . LYS A 1 196 ? 71.06400  20.42900  68.48600  1.000 85.04409  ?  204 LYS A CA  1 
ATOM   1474 C C   . LYS A 1 196 ? 71.30800  19.97000  67.05400  1.000 84.40282  ?  204 LYS A C   1 
ATOM   1475 O O   . LYS A 1 196 ? 71.19000  20.77400  66.12600  1.000 83.53601  ?  204 LYS A O   1 
ATOM   1476 C CB  . LYS A 1 196 ? 72.40700  20.76300  69.14400  1.000 89.64529  ?  204 LYS A CB  1 
ATOM   1477 C CG  . LYS A 1 196 ? 73.18100  21.88200  68.47200  1.000 89.94880  ?  204 LYS A CG  1 
ATOM   1478 C CD  . LYS A 1 196 ? 74.49400  22.13500  69.19300  1.000 99.56417  ?  204 LYS A CD  1 
ATOM   1479 C CE  . LYS A 1 196 ? 74.78300  23.62100  69.32300  1.000 117.86727 ?  204 LYS A CE  1 
ATOM   1480 N NZ  . LYS A 1 196 ? 76.04300  23.88100  70.07900  1.000 119.22771 ?  204 LYS A NZ  1 
ATOM   1481 N N   . ASP A 1 197 ? 71.63700  18.69300  66.84700  1.000 80.13296  ?  205 ASP A N   1 
ATOM   1482 C CA  . ASP A 1 197 ? 72.13900  18.24000  65.55200  1.000 85.65471  ?  205 ASP A CA  1 
ATOM   1483 C C   . ASP A 1 197 ? 71.31500  17.12800  64.91100  1.000 86.59118  ?  205 ASP A C   1 
ATOM   1484 O O   . ASP A 1 197 ? 71.84100  16.41100  64.05100  1.000 83.28326  ?  205 ASP A O   1 
ATOM   1485 C CB  . ASP A 1 197 ? 73.59000  17.77300  65.69100  1.000 87.92733  ?  205 ASP A CB  1 
ATOM   1486 C CG  . ASP A 1 197 ? 74.52300  18.89300  66.08000  1.000 96.86011  ?  205 ASP A CG  1 
ATOM   1487 O OD1 . ASP A 1 197 ? 74.30000  20.03300  65.62400  1.000 105.44338 ?  205 ASP A OD1 1 
ATOM   1488 O OD2 . ASP A 1 197 ? 75.47700  18.63200  66.84100  1.000 96.97462  -1 205 ASP A OD2 1 
ATOM   1489 N N   . GLY A 1 198 ? 70.05200  16.95400  65.28900  1.000 83.31876  ?  206 GLY A N   1 
ATOM   1490 C CA  . GLY A 1 198 ? 69.29400  15.85000  64.73400  1.000 76.08524  ?  206 GLY A CA  1 
ATOM   1491 C C   . GLY A 1 198 ? 69.71300  14.52200  65.33300  1.000 71.43489  ?  206 GLY A C   1 
ATOM   1492 O O   . GLY A 1 198 ? 70.88000  14.34300  65.69600  1.000 70.38257  ?  206 GLY A O   1 
ATOM   1493 N N   . MET A 1 199 ? 68.77500  13.58000  65.44900  1.000 69.81667  ?  207 MET A N   1 
ATOM   1494 C CA  . MET A 1 199 ? 69.09100  12.29800  66.07100  1.000 68.23680  ?  207 MET A CA  1 
ATOM   1495 C C   . MET A 1 199 ? 70.07300  11.50100  65.22000  1.000 63.58630  ?  207 MET A C   1 
ATOM   1496 O O   . MET A 1 199 ? 71.00300  10.86900  65.74100  1.000 65.58973  ?  207 MET A O   1 
ATOM   1497 C CB  . MET A 1 199 ? 67.80800  11.50600  66.31400  1.000 58.98550  ?  207 MET A CB  1 
ATOM   1498 C CG  . MET A 1 199 ? 67.93100  10.48300  67.42200  1.000 65.72996  ?  207 MET A CG  1 
ATOM   1499 S SD  . MET A 1 199 ? 67.40900  11.16600  69.00600  1.000 84.59721  ?  207 MET A SD  1 
ATOM   1500 C CE  . MET A 1 199 ? 66.71400  9.72100   69.79500  1.000 73.13794  ?  207 MET A CE  1 
ATOM   1501 N N   . LEU A 1 200 ? 69.88500  11.52700  63.89900  1.000 64.62903  ?  208 LEU A N   1 
ATOM   1502 C CA  . LEU A 1 200 ? 70.81300  10.84600  63.00300  1.000 70.25699  ?  208 LEU A CA  1 
ATOM   1503 C C   . LEU A 1 200 ? 72.21800  11.42000  63.12000  1.000 62.58513  ?  208 LEU A C   1 
ATOM   1504 O O   . LEU A 1 200 ? 73.19600  10.66900  63.21400  1.000 58.67168  ?  208 LEU A O   1 
ATOM   1505 C CB  . LEU A 1 200 ? 70.31600  10.95100  61.56300  1.000 65.41397  ?  208 LEU A CB  1 
ATOM   1506 C CG  . LEU A 1 200 ? 70.89600  9.97700   60.53800  1.000 55.95998  ?  208 LEU A CG  1 
ATOM   1507 C CD1 . LEU A 1 200 ? 71.15900  8.61500   61.15600  1.000 45.02772  ?  208 LEU A CD1 1 
ATOM   1508 C CD2 . LEU A 1 200 ? 69.97300  9.86400   59.34100  1.000 49.39634  ?  208 LEU A CD2 1 
ATOM   1509 N N   . GLY A 1 201 ? 72.33800  12.74900  63.11400  1.000 60.53504  ?  209 GLY A N   1 
ATOM   1510 C CA  . GLY A 1 201 ? 73.64900  13.36400  63.23700  1.000 58.35189  ?  209 GLY A CA  1 
ATOM   1511 C C   . GLY A 1 201 ? 74.29300  13.09400  64.58100  1.000 57.26757  ?  209 GLY A C   1 
ATOM   1512 O O   . GLY A 1 201 ? 75.50700  12.89300  64.67000  1.000 56.64241  ?  209 GLY A O   1 
ATOM   1513 N N   . ALA A 1 202 ? 73.48900  13.08200  65.64600  1.000 59.90603  ?  210 ALA A N   1 
ATOM   1514 C CA  . ALA A 1 202 ? 74.01600  12.74700  66.96300  1.000 64.91854  ?  210 ALA A CA  1 
ATOM   1515 C C   . ALA A 1 202 ? 74.55700  11.32500  66.99100  1.000 62.95923  ?  210 ALA A C   1 
ATOM   1516 O O   . ALA A 1 202 ? 75.62100  11.07000  67.56600  1.000 69.04488  ?  210 ALA A O   1 
ATOM   1517 C CB  . ALA A 1 202 ? 72.93200  12.92900  68.02500  1.000 63.13722  ?  210 ALA A CB  1 
ATOM   1518 N N   . LEU A 1 203 ? 73.83400  10.38200  66.38200  1.000 68.74598  ?  211 LEU A N   1 
ATOM   1519 C CA  . LEU A 1 203 ? 74.32800  9.01000   66.33000  1.000 67.68840  ?  211 LEU A CA  1 
ATOM   1520 C C   . LEU A 1 203 ? 75.60700  8.90700   65.51000  1.000 65.25657  ?  211 LEU A C   1 
ATOM   1521 O O   . LEU A 1 203 ? 76.55900  8.23400   65.92100  1.000 59.71499  ?  211 LEU A O   1 
ATOM   1522 C CB  . LEU A 1 203 ? 73.26100  8.07900   65.76100  1.000 65.50537  ?  211 LEU A CB  1 
ATOM   1523 C CG  . LEU A 1 203 ? 73.44100  6.62200   66.19200  1.000 74.09085  ?  211 LEU A CG  1 
ATOM   1524 C CD1 . LEU A 1 203 ? 73.12400  6.44800   67.66700  1.000 63.07594  ?  211 LEU A CD1 1 
ATOM   1525 C CD2 . LEU A 1 203 ? 72.60300  5.69400   65.33600  1.000 75.50022  ?  211 LEU A CD2 1 
ATOM   1526 N N   . LEU A 1 204 ? 75.65000  9.56500   64.34900  1.000 64.62687  ?  212 LEU A N   1 
ATOM   1527 C CA  . LEU A 1 204 ? 76.83200  9.47000   63.49600  1.000 65.87108  ?  212 LEU A CA  1 
ATOM   1528 C C   . LEU A 1 204 ? 78.04600  10.13500  64.13200  1.000 65.93036  ?  212 LEU A C   1 
ATOM   1529 O O   . LEU A 1 204 ? 79.17900  9.70000   63.89800  1.000 68.51680  ?  212 LEU A O   1 
ATOM   1530 C CB  . LEU A 1 204 ? 76.55900  10.07900  62.11900  1.000 66.78319  ?  212 LEU A CB  1 
ATOM   1531 C CG  . LEU A 1 204 ? 75.36400  9.62400   61.27600  1.000 61.75283  ?  212 LEU A CG  1 
ATOM   1532 C CD1 . LEU A 1 204 ? 75.70600  9.72900   59.80100  1.000 67.27340  ?  212 LEU A CD1 1 
ATOM   1533 C CD2 . LEU A 1 204 ? 74.94200  8.20200   61.60700  1.000 60.85241  ?  212 LEU A CD2 1 
ATOM   1534 N N   . GLY A 1 205 ? 77.83600  11.18300  64.92900  1.000 61.84123  ?  213 GLY A N   1 
ATOM   1535 C CA  . GLY A 1 205 ? 78.95600  11.82900  65.59000  1.000 61.31089  ?  213 GLY A CA  1 
ATOM   1536 C C   . GLY A 1 205 ? 79.63800  10.94100  66.61000  1.000 64.57062  ?  213 GLY A C   1 
ATOM   1537 O O   . GLY A 1 205 ? 80.81800  11.13100  66.91600  1.000 66.64102  ?  213 GLY A O   1 
ATOM   1538 N N   . ALA A 1 206 ? 78.91300  9.96300   67.14900  1.000 64.05806  ?  214 ALA A N   1 
ATOM   1539 C CA  . ALA A 1 206 ? 79.45100  9.03800   68.13500  1.000 70.18703  ?  214 ALA A CA  1 
ATOM   1540 C C   . ALA A 1 206 ? 79.90600  7.72200   67.51700  1.000 75.96936  ?  214 ALA A C   1 
ATOM   1541 O O   . ALA A 1 206 ? 80.17400  6.76300   68.25000  1.000 69.56000  ?  214 ALA A O   1 
ATOM   1542 C CB  . ALA A 1 206 ? 78.41500  8.77500   69.23000  1.000 63.73328  ?  214 ALA A CB  1 
ATOM   1543 N N   . ARG A 1 207 ? 79.99500  7.65400   66.19500  1.000 75.86719  ?  215 ARG A N   1 
ATOM   1544 C CA  . ARG A 1 207 ? 80.37800  6.44500   65.49000  1.000 73.98047  ?  215 ARG A CA  1 
ATOM   1545 C C   . ARG A 1 207 ? 81.90000  6.40600   65.31800  1.000 75.73287  ?  215 ARG A C   1 
ATOM   1546 O O   . ARG A 1 207 ? 82.62900  7.19300   65.93200  1.000 78.43367  ?  215 ARG A O   1 
ATOM   1547 C CB  . ARG A 1 207 ? 79.62600  6.37800   64.15700  1.000 71.24469  ?  215 ARG A CB  1 
ATOM   1548 C CG  . ARG A 1 207 ? 78.15100  6.04400   64.30100  1.000 71.85698  ?  215 ARG A CG  1 
ATOM   1549 C CD  . ARG A 1 207 ? 77.79900  4.73700   63.61100  1.000 76.42871  ?  215 ARG A CD  1 
ATOM   1550 N NE  . ARG A 1 207 ? 78.09900  4.77400   62.18500  1.000 71.71926  ?  215 ARG A NE  1 
ATOM   1551 C CZ  . ARG A 1 207 ? 77.97200  3.73900   61.36800  1.000 61.46872  ?  215 ARG A CZ  1 
ATOM   1552 N NH1 . ARG A 1 207 ? 77.53600  2.56800   61.79900  1.000 59.38167  ?  215 ARG A NH1 1 
ATOM   1553 N NH2 . ARG A 1 207 ? 78.29200  3.88300   60.08600  1.000 74.70004  ?  215 ARG A NH2 1 
ATOM   1554 N N   . HIS A 1 208 ? 82.38700  5.48700   64.48800  1.000 77.37190  ?  216 HIS A N   1 
ATOM   1555 C CA  . HIS A 1 208 ? 83.81400  5.36100   64.23900  1.000 78.73241  ?  216 HIS A CA  1 
ATOM   1556 C C   . HIS A 1 208 ? 84.33700  6.57500   63.47600  1.000 79.40109  ?  216 HIS A C   1 
ATOM   1557 O O   . HIS A 1 208 ? 83.58000  7.38300   62.93200  1.000 88.26355  ?  216 HIS A O   1 
ATOM   1558 C CB  . HIS A 1 208 ? 84.12200  4.02800   63.55700  1.000 84.90701  ?  216 HIS A CB  1 
ATOM   1559 C CG  . HIS A 1 208 ? 84.30100  2.88600   64.50700  1.000 76.91348  ?  216 HIS A CG  1 
ATOM   1560 N ND1 . HIS A 1 208 ? 84.23800  1.56800   64.10700  1.000 66.49783  ?  216 HIS A ND1 1 
ATOM   1561 C CD2 . HIS A 1 208 ? 84.53800  2.86400   65.83900  1.000 76.30557  ?  216 HIS A CD2 1 
ATOM   1562 C CE1 . HIS A 1 208 ? 84.43000  0.78400   65.15200  1.000 76.34705  ?  216 HIS A CE1 1 
ATOM   1563 N NE2 . HIS A 1 208 ? 84.61600  1.54500   66.21600  1.000 76.94577  ?  216 HIS A NE2 1 
ATOM   1564 N N   . ALA A 1 209 ? 85.66000  6.70000   63.44500  1.000 76.30793  ?  217 ALA A N   1 
ATOM   1565 C CA  . ALA A 1 209 ? 86.29900  7.74200   62.65700  1.000 80.23603  ?  217 ALA A CA  1 
ATOM   1566 C C   . ALA A 1 209 ? 86.11800  7.45500   61.17400  1.000 85.92499  ?  217 ALA A C   1 
ATOM   1567 O O   . ALA A 1 209 ? 86.28900  6.31900   60.72200  1.000 81.19739  ?  217 ALA A O   1 
ATOM   1568 C CB  . ALA A 1 209 ? 87.78500  7.84000   62.99900  1.000 84.18753  ?  217 ALA A CB  1 
ATOM   1569 N N   . GLY A 1 210 ? 85.76400  8.49100   60.41800  1.000 87.54921  ?  218 GLY A N   1 
ATOM   1570 C CA  . GLY A 1 210 ? 85.49900  8.31500   59.00100  1.000 80.88764  ?  218 GLY A CA  1 
ATOM   1571 C C   . GLY A 1 210 ? 84.32800  7.40500   58.71300  1.000 95.84242  ?  218 GLY A C   1 
ATOM   1572 O O   . GLY A 1 210 ? 84.28700  6.77000   57.65400  1.000 91.55976  ?  218 GLY A O   1 
ATOM   1573 N N   . ALA A 1 211 ? 83.37000  7.31900   59.63900  1.000 100.83655 ?  219 ALA A N   1 
ATOM   1574 C CA  . ALA A 1 211 ? 82.22700  6.43500   59.44400  1.000 90.65734  ?  219 ALA A CA  1 
ATOM   1575 C C   . ALA A 1 211 ? 81.31100  6.93400   58.33600  1.000 89.09990  ?  219 ALA A C   1 
ATOM   1576 O O   . ALA A 1 211 ? 80.68100  6.12500   57.64800  1.000 84.29438  ?  219 ALA A O   1 
ATOM   1577 C CB  . ALA A 1 211 ? 81.44800  6.28600   60.74900  1.000 80.54083  ?  219 ALA A CB  1 
ATOM   1578 N N   . LYS A 1 212 ? 81.21300  8.25400   58.15600  1.000 91.50690  ?  220 LYS A N   1 
ATOM   1579 C CA  . LYS A 1 212 ? 80.39500  8.79200   57.07500  1.000 87.28374  ?  220 LYS A CA  1 
ATOM   1580 C C   . LYS A 1 212 ? 80.93100  8.36700   55.71400  1.000 96.13136  ?  220 LYS A C   1 
ATOM   1581 O O   . LYS A 1 212 ? 80.15600  8.01500   54.81700  1.000 92.95169  ?  220 LYS A O   1 
ATOM   1582 C CB  . LYS A 1 212 ? 80.32700  10.31600  57.17600  1.000 81.16999  ?  220 LYS A CB  1 
ATOM   1583 N N   . ALA A 1 213 ? 82.25500  8.39700   55.54100  1.000 98.61882  ?  221 ALA A N   1 
ATOM   1584 C CA  . ALA A 1 213 ? 82.84800  7.88700   54.31000  1.000 92.25210  ?  221 ALA A CA  1 
ATOM   1585 C C   . ALA A 1 213 ? 82.72600  6.37200   54.21900  1.000 97.43487  ?  221 ALA A C   1 
ATOM   1586 O O   . ALA A 1 213 ? 82.66000  5.82100   53.11400  1.000 92.96194  ?  221 ALA A O   1 
ATOM   1587 C CB  . ALA A 1 213 ? 84.31300  8.31000   54.21700  1.000 81.65343  ?  221 ALA A CB  1 
ATOM   1588 N N   . ASN A 1 214 ? 82.69600  5.68400   55.36100  1.000 93.39129  ?  222 ASN A N   1 
ATOM   1589 C CA  . ASN A 1 214 ? 82.52100  4.23800   55.38500  1.000 88.54130  ?  222 ASN A CA  1 
ATOM   1590 C C   . ASN A 1 214 ? 81.05800  3.82300   55.31000  1.000 89.38782  ?  222 ASN A C   1 
ATOM   1591 O O   . ASN A 1 214 ? 80.77300  2.62000   55.29400  1.000 76.45491  ?  222 ASN A O   1 
ATOM   1592 C CB  . ASN A 1 214 ? 83.17000  3.64400   56.63600  1.000 79.73012  ?  222 ASN A CB  1 
ATOM   1593 C CG  . ASN A 1 214 ? 84.68500  3.69100   56.58500  1.000 90.14685  ?  222 ASN A CG  1 
ATOM   1594 O OD1 . ASN A 1 214 ? 85.28000  3.76000   55.51000  1.000 90.83131  ?  222 ASN A OD1 1 
ATOM   1595 N ND2 . ASN A 1 214 ? 85.31800  3.65200   57.75200  1.000 96.11066  ?  222 ASN A ND2 1 
ATOM   1596 N N   . LEU A 1 215 ? 80.13400  4.78100   55.27300  1.000 87.09664  ?  223 LEU A N   1 
ATOM   1597 C CA  . LEU A 1 215 ? 78.70900  4.49600   55.17200  1.000 75.97797  ?  223 LEU A CA  1 
ATOM   1598 C C   . LEU A 1 215 ? 78.13200  4.83500   53.80800  1.000 74.12802  ?  223 LEU A C   1 
ATOM   1599 O O   . LEU A 1 215 ? 77.11100  4.25900   53.42100  1.000 79.75749  ?  223 LEU A O   1 
ATOM   1600 C CB  . LEU A 1 215 ? 77.93700  5.26400   56.25000  1.000 75.51756  ?  223 LEU A CB  1 
ATOM   1601 C CG  . LEU A 1 215 ? 76.55300  4.72600   56.61200  1.000 70.68940  ?  223 LEU A CG  1 
ATOM   1602 C CD1 . LEU A 1 215 ? 76.64500  3.26100   56.99200  1.000 67.70822  ?  223 LEU A CD1 1 
ATOM   1603 C CD2 . LEU A 1 215 ? 75.94700  5.53600   57.74300  1.000 61.25604  ?  223 LEU A CD2 1 
ATOM   1604 N N   . ALA A 1 216 ? 78.75500  5.75800   53.07300  1.000 70.14494  ?  224 ALA A N   1 
ATOM   1605 C CA  . ALA A 1 216 ? 78.31200  6.04000   51.71400  1.000 68.50579  ?  224 ALA A CA  1 
ATOM   1606 C C   . ALA A 1 216 ? 78.55400  4.86200   50.78500  1.000 69.63359  ?  224 ALA A C   1 
ATOM   1607 O O   . ALA A 1 216 ? 77.94300  4.79400   49.71300  1.000 69.33023  ?  224 ALA A O   1 
ATOM   1608 C CB  . ALA A 1 216 ? 79.01300  7.28600   51.17400  1.000 68.46381  ?  224 ALA A CB  1 
ATOM   1609 N N   . GLN A 1 217 ? 79.43300  3.93600   51.17000  1.000 65.77668  ?  225 GLN A N   1 
ATOM   1610 C CA  . GLN A 1 217 ? 79.65800  2.73200   50.38300  1.000 75.00584  ?  225 GLN A CA  1 
ATOM   1611 C C   . GLN A 1 217 ? 78.50800  1.74100   50.48500  1.000 70.77933  ?  225 GLN A C   1 
ATOM   1612 O O   . GLN A 1 217 ? 78.45600  0.79500   49.69300  1.000 69.97849  ?  225 GLN A O   1 
ATOM   1613 C CB  . GLN A 1 217 ? 80.96100  2.06000   50.81700  1.000 74.83659  ?  225 GLN A CB  1 
ATOM   1614 C CG  . GLN A 1 217 ? 82.19300  2.92700   50.62800  1.000 80.60414  ?  225 GLN A CG  1 
ATOM   1615 C CD  . GLN A 1 217 ? 83.45800  2.25600   51.11700  1.000 83.88695  ?  225 GLN A CD  1 
ATOM   1616 O OE1 . GLN A 1 217 ? 83.85100  2.41400   52.27200  1.000 88.77083  ?  225 GLN A OE1 1 
ATOM   1617 N NE2 . GLN A 1 217 ? 84.10700  1.50300   50.23700  1.000 78.04420  ?  225 GLN A NE2 1 
ATOM   1618 N N   . LEU A 1 218 ? 77.59700  1.92900   51.43400  1.000 64.11162  ?  226 LEU A N   1 
ATOM   1619 C CA  . LEU A 1 218 ? 76.45600  1.03800   51.57600  1.000 55.74686  ?  226 LEU A CA  1 
ATOM   1620 C C   . LEU A 1 218 ? 75.28700  1.54100   50.73100  1.000 55.14520  ?  226 LEU A C   1 
ATOM   1621 O O   . LEU A 1 218 ? 75.02600  2.74500   50.68800  1.000 54.69108  ?  226 LEU A O   1 
ATOM   1622 C CB  . LEU A 1 218 ? 76.03200  0.93000   53.03800  1.000 56.48836  ?  226 LEU A CB  1 
ATOM   1623 C CG  . LEU A 1 218 ? 76.92000  0.10700   53.97500  1.000 54.76027  ?  226 LEU A CG  1 
ATOM   1624 C CD1 . LEU A 1 218 ? 77.27900  -1.22600  53.34100  1.000 53.39771  ?  226 LEU A CD1 1 
ATOM   1625 C CD2 . LEU A 1 218 ? 78.16900  0.86800   54.39100  1.000 67.03194  ?  226 LEU A CD2 1 
ATOM   1626 N N   . PRO A 1 219 ? 74.58000  0.64400   50.04200  1.000 57.18411  ?  227 PRO A N   1 
ATOM   1627 C CA  . PRO A 1 219 ? 73.45500  1.09100   49.20500  1.000 45.63484  ?  227 PRO A CA  1 
ATOM   1628 C C   . PRO A 1 219 ? 72.30300  1.67700   49.99800  1.000 40.77679  ?  227 PRO A C   1 
ATOM   1629 O O   . PRO A 1 219 ? 71.51800  2.45600   49.44500  1.000 40.35265  ?  227 PRO A O   1 
ATOM   1630 C CB  . PRO A 1 219 ? 73.04000  -0.18800  48.46600  1.000 45.40530  ?  227 PRO A CB  1 
ATOM   1631 C CG  . PRO A 1 219 ? 73.51400  -1.29900  49.33300  1.000 46.25318  ?  227 PRO A CG  1 
ATOM   1632 C CD  . PRO A 1 219 ? 74.75700  -0.81700  50.01300  1.000 52.93670  ?  227 PRO A CD  1 
ATOM   1633 N N   . GLU A 1 220 ? 72.17700  1.32900   51.27900  1.000 45.56431  ?  228 GLU A N   1 
ATOM   1634 C CA  . GLU A 1 220 ? 71.05900  1.79700   52.08700  1.000 47.52285  ?  228 GLU A CA  1 
ATOM   1635 C C   . GLU A 1 220 ? 71.13500  3.28400   52.40500  1.000 53.98681  ?  228 GLU A C   1 
ATOM   1636 O O   . GLU A 1 220 ? 70.15900  3.83800   52.92100  1.000 53.02022  ?  228 GLU A O   1 
ATOM   1637 C CB  . GLU A 1 220 ? 70.97400  0.99100   53.38400  1.000 44.83587  ?  228 GLU A CB  1 
ATOM   1638 C CG  . GLU A 1 220 ? 72.31500  0.65000   54.00200  1.000 47.77010  ?  228 GLU A CG  1 
ATOM   1639 C CD  . GLU A 1 220 ? 72.77700  -0.74900  53.65300  1.000 53.37753  ?  228 GLU A CD  1 
ATOM   1640 O OE1 . GLU A 1 220 ? 72.34000  -1.27800  52.61200  1.000 53.00003  ?  228 GLU A OE1 1 
ATOM   1641 O OE2 . GLU A 1 220 ? 73.57300  -1.32300  54.42300  1.000 67.35444  -1 228 GLU A OE2 1 
ATOM   1642 N N   . ALA A 1 221 ? 72.26100  3.93800   52.12000  1.000 47.55193  ?  229 ALA A N   1 
ATOM   1643 C CA  . ALA A 1 221 ? 72.35600  5.37900   52.30700  1.000 45.73269  ?  229 ALA A CA  1 
ATOM   1644 C C   . ALA A 1 221 ? 71.72100  6.16100   51.16700  1.000 45.41428  ?  229 ALA A C   1 
ATOM   1645 O O   . ALA A 1 221 ? 71.62500  7.38900   51.26200  1.000 49.26643  ?  229 ALA A O   1 
ATOM   1646 C CB  . ALA A 1 221 ? 73.82000  5.79200   52.46500  1.000 49.68714  ?  229 ALA A CB  1 
ATOM   1647 N N   . HIS A 1 222 ? 71.29100  5.48900   50.10100  1.000 41.28790  ?  230 HIS A N   1 
ATOM   1648 C CA  . HIS A 1 222 ? 70.70600  6.16600   48.95100  1.000 42.25975  ?  230 HIS A CA  1 
ATOM   1649 C C   . HIS A 1 222 ? 69.39800  5.51500   48.52100  1.000 35.70447  ?  230 HIS A C   1 
ATOM   1650 O O   . HIS A 1 222 ? 68.58000  6.14600   47.84500  1.000 27.45530  ?  230 HIS A O   1 
ATOM   1651 C CB  . HIS A 1 222 ? 71.69400  6.17400   47.78400  1.000 41.37032  ?  230 HIS A CB  1 
ATOM   1652 C CG  . HIS A 1 222 ? 72.99600  6.83700   48.10100  1.000 48.19250  ?  230 HIS A CG  1 
ATOM   1653 N ND1 . HIS A 1 222 ? 73.15000  8.20600   48.10900  1.000 47.74528  ?  230 HIS A ND1 1 
ATOM   1654 C CD2 . HIS A 1 222 ? 74.20300  6.32000   48.42800  1.000 47.95932  ?  230 HIS A CD2 1 
ATOM   1655 C CE1 . HIS A 1 222 ? 74.39800  8.50400   48.42300  1.000 54.01222  ?  230 HIS A CE1 1 
ATOM   1656 N NE2 . HIS A 1 222 ? 75.05800  7.37700   48.62200  1.000 47.45563  ?  230 HIS A NE2 1 
ATOM   1657 N N   . PHE A 1 223 ? 69.19400  4.25500   48.90000  1.000 38.13166  ?  231 PHE A N   1 
ATOM   1658 C CA  . PHE A 1 223 ? 68.01900  3.50200   48.48900  1.000 31.35969  ?  231 PHE A CA  1 
ATOM   1659 C C   . PHE A 1 223 ? 67.35900  2.85000   49.69400  1.000 33.94404  ?  231 PHE A C   1 
ATOM   1660 O O   . PHE A 1 223 ? 68.03800  2.37200   50.60600  1.000 29.13702  ?  231 PHE A O   1 
ATOM   1661 C CB  . PHE A 1 223 ? 68.38000  2.43800   47.45300  1.000 28.97259  ?  231 PHE A CB  1 
ATOM   1662 C CG  . PHE A 1 223 ? 68.81000  3.00300   46.13200  1.000 32.99351  ?  231 PHE A CG  1 
ATOM   1663 C CD1 . PHE A 1 223 ? 67.87300  3.35100   45.17600  1.000 31.71439  ?  231 PHE A CD1 1 
ATOM   1664 C CD2 . PHE A 1 223 ? 70.14900  3.18600   45.84600  1.000 31.31337  ?  231 PHE A CD2 1 
ATOM   1665 C CE1 . PHE A 1 223 ? 68.26400  3.87000   43.96200  1.000 27.87865  ?  231 PHE A CE1 1 
ATOM   1666 C CE2 . PHE A 1 223 ? 70.54400  3.70600   44.63400  1.000 31.69814  ?  231 PHE A CE2 1 
ATOM   1667 C CZ  . PHE A 1 223 ? 69.60000  4.04700   43.69100  1.000 29.42923  ?  231 PHE A CZ  1 
ATOM   1668 N N   . THR A 1 224 ? 66.02800  2.84000   49.68600  1.000 37.46109  ?  232 THR A N   1 
ATOM   1669 C CA  . THR A 1 224 ? 65.24000  2.21200   50.73600  1.000 23.54447  ?  232 THR A CA  1 
ATOM   1670 C C   . THR A 1 224 ? 63.86700  1.88000   50.17200  1.000 26.72528  ?  232 THR A C   1 
ATOM   1671 O O   . THR A 1 224 ? 63.47900  2.36500   49.10700  1.000 31.92763  ?  232 THR A O   1 
ATOM   1672 C CB  . THR A 1 224 ? 65.11100  3.11100   51.97100  1.000 25.49092  ?  232 THR A CB  1 
ATOM   1673 O OG1 . THR A 1 224 ? 64.60500  2.34700   53.07100  1.000 39.48425  ?  232 THR A OG1 1 
ATOM   1674 C CG2 . THR A 1 224 ? 64.16600  4.25800   51.69300  1.000 30.24953  ?  232 THR A CG2 1 
ATOM   1675 N N   . VAL A 1 225 ? 63.13500  1.03700   50.89800  1.000 29.77260  ?  233 VAL A N   1 
ATOM   1676 C CA  . VAL A 1 225 ? 61.80700  0.63100   50.45500  1.000 31.35148  ?  233 VAL A CA  1 
ATOM   1677 C C   . VAL A 1 225 ? 60.81200  1.74400   50.74600  1.000 28.12536  ?  233 VAL A C   1 
ATOM   1678 O O   . VAL A 1 225 ? 60.62100  2.14500   51.90100  1.000 26.01554  ?  233 VAL A O   1 
ATOM   1679 C CB  . VAL A 1 225 ? 61.38700  -0.67900  51.13800  1.000 34.81868  ?  233 VAL A CB  1 
ATOM   1680 C CG1 . VAL A 1 225 ? 59.92000  -0.96700  50.87200  1.000 32.26899  ?  233 VAL A CG1 1 
ATOM   1681 C CG2 . VAL A 1 225 ? 62.24600  -1.82900  50.65400  1.000 27.30163  ?  233 VAL A CG2 1 
ATOM   1682 N N   . GLN A 1 226 ? 60.16900  2.24800   49.69500  1.000 30.10645  ?  234 GLN A N   1 
ATOM   1683 C CA  . GLN A 1 226 ? 59.11600  3.24600   49.83200  1.000 33.44375  ?  234 GLN A CA  1 
ATOM   1684 C C   . GLN A 1 226 ? 57.74200  2.76000   49.41000  1.000 33.87085  ?  234 GLN A C   1 
ATOM   1685 O O   . GLN A 1 226 ? 56.75300  3.41700   49.75000  1.000 31.72595  ?  234 GLN A O   1 
ATOM   1686 C CB  . GLN A 1 226 ? 59.44300  4.50300   49.01400  1.000 32.03244  ?  234 GLN A CB  1 
ATOM   1687 C CG  . GLN A 1 226 ? 60.68600  5.24000   49.44300  1.000 33.89963  ?  234 GLN A CG  1 
ATOM   1688 C CD  . GLN A 1 226 ? 60.81800  6.57900   48.75400  1.000 34.63221  ?  234 GLN A CD  1 
ATOM   1689 O OE1 . GLN A 1 226 ? 59.93200  7.42500   48.84500  1.000 41.26273  ?  234 GLN A OE1 1 
ATOM   1690 N NE2 . GLN A 1 226 ? 61.92200  6.77500   48.04800  1.000 44.06995  ?  234 GLN A NE2 1 
ATOM   1691 N N   . ALA A 1 227 ? 57.63800  1.64900   48.68600  1.000 31.56298  ?  235 ALA A N   1 
ATOM   1692 C CA  . ALA A 1 227 ? 56.35900  1.23000   48.14100  1.000 34.74073  ?  235 ALA A CA  1 
ATOM   1693 C C   . ALA A 1 227 ? 56.36300  -0.27200  47.91400  1.000 30.13054  ?  235 ALA A C   1 
ATOM   1694 O O   . ALA A 1 227 ? 57.40700  -0.92600  47.94100  1.000 35.16368  ?  235 ALA A O   1 
ATOM   1695 C CB  . ALA A 1 227 ? 56.04200  1.96000   46.83200  1.000 33.31676  ?  235 ALA A CB  1 
ATOM   1696 N N   . PHE A 1 228 ? 55.16500  -0.81100  47.71200  1.000 27.88307  ?  236 PHE A N   1 
ATOM   1697 C CA  . PHE A 1 228 ? 54.97600  -2.19400  47.30100  1.000 26.55648  ?  236 PHE A CA  1 
ATOM   1698 C C   . PHE A 1 228 ? 53.86700  -2.23600  46.26400  1.000 26.62001  ?  236 PHE A C   1 
ATOM   1699 O O   . PHE A 1 228 ? 52.80600  -1.63800  46.46200  1.000 26.36859  ?  236 PHE A O   1 
ATOM   1700 C CB  . PHE A 1 228 ? 54.62700  -3.09400  48.49100  1.000 24.78474  ?  236 PHE A CB  1 
ATOM   1701 C CG  . PHE A 1 228 ? 54.67200  -4.56000  48.17300  1.000 28.37593  ?  236 PHE A CG  1 
ATOM   1702 C CD1 . PHE A 1 228 ? 53.55000  -5.21400  47.69800  1.000 30.16930  ?  236 PHE A CD1 1 
ATOM   1703 C CD2 . PHE A 1 228 ? 55.83600  -5.28200  48.34600  1.000 37.81257  ?  236 PHE A CD2 1 
ATOM   1704 C CE1 . PHE A 1 228 ? 53.58900  -6.55900  47.40300  1.000 29.40747  ?  236 PHE A CE1 1 
ATOM   1705 C CE2 . PHE A 1 228 ? 55.88100  -6.62900  48.05100  1.000 36.66015  ?  236 PHE A CE2 1 
ATOM   1706 C CZ  . PHE A 1 228 ? 54.75500  -7.26700  47.58000  1.000 29.11406  ?  236 PHE A CZ  1 
ATOM   1707 N N   . VAL A 1 229 ? 54.10900  -2.94600  45.16800  1.000 28.44478  ?  237 VAL A N   1 
ATOM   1708 C CA  . VAL A 1 229 ? 53.13200  -3.10500  44.09800  1.000 31.38288  ?  237 VAL A CA  1 
ATOM   1709 C C   . VAL A 1 229 ? 52.71100  -4.56500  44.05800  1.000 30.32938  ?  237 VAL A C   1 
ATOM   1710 O O   . VAL A 1 229 ? 53.55300  -5.46100  43.92000  1.000 31.32705  ?  237 VAL A O   1 
ATOM   1711 C CB  . VAL A 1 229 ? 53.69200  -2.65200  42.74200  1.000 26.98835  ?  237 VAL A CB  1 
ATOM   1712 C CG1 . VAL A 1 229 ? 52.65500  -2.84500  41.65300  1.000 21.14543  ?  237 VAL A CG1 1 
ATOM   1713 C CG2 . VAL A 1 229 ? 54.12400  -1.20100  42.80600  1.000 25.43905  ?  237 VAL A CG2 1 
ATOM   1714 N N   . GLN A 1 230 ? 51.41000  -4.80300  44.18800  1.000 28.73236  ?  238 GLN A N   1 
ATOM   1715 C CA  . GLN A 1 230 ? 50.83100  -6.13200  44.05700  1.000 23.94790  ?  238 GLN A CA  1 
ATOM   1716 C C   . GLN A 1 230 ? 50.11200  -6.22700  42.72000  1.000 27.42749  ?  238 GLN A C   1 
ATOM   1717 O O   . GLN A 1 230 ? 49.34600  -5.32800  42.35400  1.000 29.36036  ?  238 GLN A O   1 
ATOM   1718 C CB  . GLN A 1 230 ? 49.86700  -6.43000  45.20400  1.000 21.78152  ?  238 GLN A CB  1 
ATOM   1719 C CG  . GLN A 1 230 ? 49.29500  -7.83100  45.16600  1.000 23.21686  ?  238 GLN A CG  1 
ATOM   1720 C CD  . GLN A 1 230 ? 50.30800  -8.88200  45.55500  1.000 27.38106  ?  238 GLN A CD  1 
ATOM   1721 O OE1 . GLN A 1 230 ? 51.28300  -8.59500  46.24500  1.000 37.85037  ?  238 GLN A OE1 1 
ATOM   1722 N NE2 . GLN A 1 230 ? 50.08600  -10.10900 45.10700  1.000 33.19300  ?  238 GLN A NE2 1 
ATOM   1723 N N   . THR A 1 231 ? 50.35900  -7.31100  41.99400  1.000 27.44342  ?  239 THR A N   1 
ATOM   1724 C CA  . THR A 1 231 ? 49.87500  -7.46800  40.63200  1.000 24.94552  ?  239 THR A CA  1 
ATOM   1725 C C   . THR A 1 231 ? 48.84600  -8.58500  40.54800  1.000 24.62710  ?  239 THR A C   1 
ATOM   1726 O O   . THR A 1 231 ? 49.00800  -9.64500  41.16000  1.000 29.14230  ?  239 THR A O   1 
ATOM   1727 C CB  . THR A 1 231 ? 51.02800  -7.75800  39.67000  1.000 27.78187  ?  239 THR A CB  1 
ATOM   1728 O OG1 . THR A 1 231 ? 51.68000  -8.97200  40.05700  1.000 38.96525  ?  239 THR A OG1 1 
ATOM   1729 C CG2 . THR A 1 231 ? 52.03100  -6.62500  39.69700  1.000 26.58035  ?  239 THR A CG2 1 
ATOM   1730 N N   . LEU A 1 232 ? 47.78800  -8.33000  39.78800  1.000 22.81073  ?  240 LEU A N   1 
ATOM   1731 C CA  . LEU A 1 232 ? 46.77800  -9.31700  39.44500  1.000 23.34382  ?  240 LEU A CA  1 
ATOM   1732 C C   . LEU A 1 232 ? 46.75600  -9.49200  37.93500  1.000 22.35054  ?  240 LEU A C   1 
ATOM   1733 O O   . LEU A 1 232 ? 47.00200  -8.53900  37.19200  1.000 26.59412  ?  240 LEU A O   1 
ATOM   1734 C CB  . LEU A 1 232 ? 45.39500  -8.89200  39.94000  1.000 20.58545  ?  240 LEU A CB  1 
ATOM   1735 C CG  . LEU A 1 232 ? 45.25900  -8.55200  41.42200  1.000 22.23287  ?  240 LEU A CG  1 
ATOM   1736 C CD1 . LEU A 1 232 ? 43.92400  -7.88900  41.68100  1.000 20.60690  ?  240 LEU A CD1 1 
ATOM   1737 C CD2 . LEU A 1 232 ? 45.41100  -9.80000  42.26800  1.000 23.40504  ?  240 LEU A CD2 1 
ATOM   1738 N N   . SER A 1 233 ? 46.47100  -10.70600 37.48300  1.000 22.75396  ?  241 SER A N   1 
ATOM   1739 C CA  . SER A 1 233 ? 46.45700  -11.01300 36.06300  1.000 21.10045  ?  241 SER A CA  1 
ATOM   1740 C C   . SER A 1 233 ? 45.23000  -11.84300 35.71500  1.000 23.57480  ?  241 SER A C   1 
ATOM   1741 O O   . SER A 1 233 ? 44.68100  -12.56400 36.55000  1.000 25.20068  ?  241 SER A O   1 
ATOM   1742 C CB  . SER A 1 233 ? 47.72900  -11.75800 35.64400  1.000 27.09514  ?  241 SER A CB  1 
ATOM   1743 O OG  . SER A 1 233 ? 48.88600  -11.00200 35.95200  1.000 38.27201  ?  241 SER A OG  1 
ATOM   1744 N N   . GLY A 1 234 ? 44.80800  -11.72700 34.46200  1.000 27.46127  ?  242 GLY A N   1 
ATOM   1745 C CA  . GLY A 1 234 ? 43.68500  -12.51900 33.99100  1.000 17.44378  ?  242 GLY A CA  1 
ATOM   1746 C C   . GLY A 1 234 ? 42.38200  -12.06600 34.61500  1.000 20.20427  ?  242 GLY A C   1 
ATOM   1747 O O   . GLY A 1 234 ? 42.13400  -10.86900 34.79900  1.000 19.63184  ?  242 GLY A O   1 
ATOM   1748 N N   . ALA A 1 235 ? 41.53400  -13.04100 34.95000  1.000 23.55376  ?  243 ALA A N   1 
ATOM   1749 C CA  . ALA A 1 235 ? 40.22500  -12.73300 35.51100  1.000 20.70689  ?  243 ALA A CA  1 
ATOM   1750 C C   . ALA A 1 235 ? 40.33800  -11.99500 36.83600  1.000 23.53022  ?  243 ALA A C   1 
ATOM   1751 O O   . ALA A 1 235 ? 39.51000  -11.12600 37.13000  1.000 23.09110  ?  243 ALA A O   1 
ATOM   1752 C CB  . ALA A 1 235 ? 39.41600  -14.01700 35.68500  1.000 17.67694  ?  243 ALA A CB  1 
ATOM   1753 N N   . ALA A 1 236 ? 41.35200  -12.31900 37.64000  1.000 27.94519  ?  244 ALA A N   1 
ATOM   1754 C CA  . ALA A 1 236 ? 41.55200  -11.62000 38.90300  1.000 25.34522  ?  244 ALA A CA  1 
ATOM   1755 C C   . ALA A 1 236 ? 41.85300  -10.14400 38.68800  1.000 24.19707  ?  244 ALA A C   1 
ATOM   1756 O O   . ALA A 1 236 ? 41.66100  -9.33500  39.60200  1.000 25.95539  ?  244 ALA A O   1 
ATOM   1757 C CB  . ALA A 1 236 ? 42.67800  -12.27900 39.69800  1.000 24.68096  ?  244 ALA A CB  1 
ATOM   1758 N N   . ALA A 1 237 ? 42.32300  -9.77300  37.49700  1.000 22.50007  ?  245 ALA A N   1 
ATOM   1759 C CA  . ALA A 1 237 ? 42.54100  -8.36800  37.18700  1.000 22.60758  ?  245 ALA A CA  1 
ATOM   1760 C C   . ALA A 1 237 ? 41.24100  -7.59200  37.04700  1.000 23.91142  ?  245 ALA A C   1 
ATOM   1761 O O   . ALA A 1 237 ? 41.27300  -6.35800  37.06300  1.000 24.14185  ?  245 ALA A O   1 
ATOM   1762 C CB  . ALA A 1 237 ? 43.36500  -8.23200  35.90800  1.000 21.94345  ?  245 ALA A CB  1 
ATOM   1763 N N   . ARG A 1 238 ? 40.10500  -8.27700  36.91000  1.000 21.21502  ?  246 ARG A N   1 
ATOM   1764 C CA  . ARG A 1 238 ? 38.80400  -7.62600  36.82100  1.000 22.07209  ?  246 ARG A CA  1 
ATOM   1765 C C   . ARG A 1 238 ? 37.92000  -7.96800  38.01300  1.000 23.93504  ?  246 ARG A C   1 
ATOM   1766 O O   . ARG A 1 238 ? 36.69200  -7.96200  37.89500  1.000 28.30426  ?  246 ARG A O   1 
ATOM   1767 C CB  . ARG A 1 238 ? 38.10900  -8.00000  35.51300  1.000 27.80125  ?  246 ARG A CB  1 
ATOM   1768 C CG  . ARG A 1 238 ? 38.83100  -7.47600  34.29400  1.000 28.15940  ?  246 ARG A CG  1 
ATOM   1769 C CD  . ARG A 1 238 ? 37.96900  -7.50600  33.05100  1.000 25.76251  ?  246 ARG A CD  1 
ATOM   1770 N NE  . ARG A 1 238 ? 38.61600  -6.77000  31.97400  1.000 30.66486  ?  246 ARG A NE  1 
ATOM   1771 C CZ  . ARG A 1 238 ? 38.30500  -5.53100  31.62500  1.000 26.44429  ?  246 ARG A CZ  1 
ATOM   1772 N NH1 . ARG A 1 238 ? 37.31500  -4.87800  32.20800  1.000 25.20894  ?  246 ARG A NH1 1 
ATOM   1773 N NH2 . ARG A 1 238 ? 39.00800  -4.93000  30.67200  1.000 26.38750  ?  246 ARG A NH2 1 
ATOM   1774 N N   . ASN A 1 239 ? 38.52600  -8.26300  39.15900  1.000 24.11987  ?  247 ASN A N   1 
ATOM   1775 C CA  . ASN A 1 239 ? 37.81400  -8.65300  40.36600  1.000 23.94092  ?  247 ASN A CA  1 
ATOM   1776 C C   . ASN A 1 239 ? 38.02600  -7.57700  41.41900  1.000 27.79337  ?  247 ASN A C   1 
ATOM   1777 O O   . ASN A 1 239 ? 39.16400  -7.31000  41.81600  1.000 25.53846  ?  247 ASN A O   1 
ATOM   1778 C CB  . ASN A 1 239 ? 38.31200  -10.01000 40.86700  1.000 23.56285  ?  247 ASN A CB  1 
ATOM   1779 C CG  . ASN A 1 239 ? 37.35700  -10.66600 41.83400  1.000 28.63130  ?  247 ASN A CG  1 
ATOM   1780 O OD1 . ASN A 1 239 ? 36.69100  -9.99800  42.62000  1.000 30.56075  ?  247 ASN A OD1 1 
ATOM   1781 N ND2 . ASN A 1 239 ? 37.29500  -11.98800 41.79100  1.000 23.51988  ?  247 ASN A ND2 1 
ATOM   1782 N N   . ALA A 1 240 ? 36.93200  -6.95400  41.86200  1.000 25.41156  ?  248 ALA A N   1 
ATOM   1783 C CA  . ALA A 1 240 ? 37.03300  -5.94000  42.90500  1.000 26.80004  ?  248 ALA A CA  1 
ATOM   1784 C C   . ALA A 1 240 ? 37.45800  -6.55400  44.23100  1.000 28.52350  ?  248 ALA A C   1 
ATOM   1785 O O   . ALA A 1 240 ? 38.23500  -5.95300  44.98500  1.000 27.13159  ?  248 ALA A O   1 
ATOM   1786 C CB  . ALA A 1 240 ? 35.70200  -5.20600  43.05200  1.000 28.07904  ?  248 ALA A CB  1 
ATOM   1787 N N   . GLU A 1 241 ? 36.94900  -7.75000  44.53500  1.000 31.15058  ?  249 GLU A N   1 
ATOM   1788 C CA  . GLU A 1 241 ? 37.35300  -8.44200  45.75200  1.000 23.76590  ?  249 GLU A CA  1 
ATOM   1789 C C   . GLU A 1 241 ? 38.84300  -8.75600  45.72900  1.000 27.19159  ?  249 GLU A C   1 
ATOM   1790 O O   . GLU A 1 241 ? 39.54800  -8.54000  46.72300  1.000 34.14543  ?  249 GLU A O   1 
ATOM   1791 C CB  . GLU A 1 241 ? 36.53000  -9.71900  45.91500  1.000 25.83748  ?  249 GLU A CB  1 
ATOM   1792 C CG  . GLU A 1 241 ? 35.04500  -9.47400  46.13200  1.000 29.68993  ?  249 GLU A CG  1 
ATOM   1793 C CD  . GLU A 1 241 ? 34.22100  -10.74800 46.07000  1.000 35.90747  ?  249 GLU A CD  1 
ATOM   1794 O OE1 . GLU A 1 241 ? 34.73300  -11.76700 45.56500  1.000 34.80130  ?  249 GLU A OE1 1 
ATOM   1795 O OE2 . GLU A 1 241 ? 33.05800  -10.72900 46.52300  1.000 37.03610  -1 249 GLU A OE2 1 
ATOM   1796 N N   . GLU A 1 242 ? 39.34200  -9.25400  44.59400  1.000 23.11253  ?  250 GLU A N   1 
ATOM   1797 C CA  . GLU A 1 242 ? 40.77300  -9.49400  44.46100  1.000 24.98610  ?  250 GLU A CA  1 
ATOM   1798 C C   . GLU A 1 242 ? 41.55600  -8.19500  44.56400  1.000 25.95263  ?  250 GLU A C   1 
ATOM   1799 O O   . GLU A 1 242 ? 42.65600  -8.17500  45.12100  1.000 25.38444  ?  250 GLU A O   1 
ATOM   1800 C CB  . GLU A 1 242 ? 41.07800  -10.19300 43.13600  1.000 23.66192  ?  250 GLU A CB  1 
ATOM   1801 C CG  . GLU A 1 242 ? 40.70800  -11.66700 43.09200  1.000 30.68296  ?  250 GLU A CG  1 
ATOM   1802 C CD  . GLU A 1 242 ? 41.68300  -12.54500 43.85100  1.000 36.55736  ?  250 GLU A CD  1 
ATOM   1803 O OE1 . GLU A 1 242 ? 42.83600  -12.11800 44.06200  1.000 34.58161  ?  250 GLU A OE1 1 
ATOM   1804 O OE2 . GLU A 1 242 ? 41.29600  -13.66700 44.23200  1.000 38.30579  -1 250 GLU A OE2 1 
ATOM   1805 N N   . TYR A 1 243 ? 41.00200  -7.10000  44.04200  1.000 23.93853  ?  251 TYR A N   1 
ATOM   1806 C CA  . TYR A 1 243 ? 41.67700  -5.80900  44.12500  1.000 23.19132  ?  251 TYR A CA  1 
ATOM   1807 C C   . TYR A 1 243 ? 41.84800  -5.36500  45.57200  1.000 22.08368  ?  251 TYR A C   1 
ATOM   1808 O O   . TYR A 1 243 ? 42.93300  -4.93800  45.98000  1.000 21.73716  ?  251 TYR A O   1 
ATOM   1809 C CB  . TYR A 1 243 ? 40.89800  -4.75900  43.33300  1.000 19.01951  ?  251 TYR A CB  1 
ATOM   1810 C CG  . TYR A 1 243 ? 41.05000  -3.35800  43.87400  1.000 19.00981  ?  251 TYR A CG  1 
ATOM   1811 C CD1 . TYR A 1 243 ? 42.22500  -2.64600  43.69000  1.000 25.58732  ?  251 TYR A CD1 1 
ATOM   1812 C CD2 . TYR A 1 243 ? 40.02200  -2.75100  44.57600  1.000 20.79492  ?  251 TYR A CD2 1 
ATOM   1813 C CE1 . TYR A 1 243 ? 42.36800  -1.37000  44.18700  1.000 25.14225  ?  251 TYR A CE1 1 
ATOM   1814 C CE2 . TYR A 1 243 ? 40.16000  -1.47600  45.07800  1.000 22.90644  ?  251 TYR A CE2 1 
ATOM   1815 C CZ  . TYR A 1 243 ? 41.33400  -0.79000  44.87800  1.000 23.97221  ?  251 TYR A CZ  1 
ATOM   1816 O OH  . TYR A 1 243 ? 41.47900  0.48200   45.37300  1.000 30.00462  ?  251 TYR A OH  1 
ATOM   1817 N N   . ARG A 1 244 ? 40.80100  -5.49200  46.37200  1.000 22.89900  ?  252 ARG A N   1 
ATOM   1818 C CA  . ARG A 1 244 ? 40.85700  -5.00900  47.77000  1.000 23.05841  ?  252 ARG A CA  1 
ATOM   1819 C C   . ARG A 1 244 ? 41.74400  -5.95200  48.57700  1.000 26.50009  ?  252 ARG A C   1 
ATOM   1820 O O   . ARG A 1 244 ? 42.47900  -5.46700  49.44000  1.000 29.02798  ?  252 ARG A O   1 
ATOM   1821 C CB  . ARG A 1 244 ? 39.42300  -4.89600  48.28900  1.000 20.61995  ?  252 ARG A CB  1 
ATOM   1822 C CG  . ARG A 1 244 ? 38.59100  -3.78900  47.65900  1.000 26.45060  ?  252 ARG A CG  1 
ATOM   1823 C CD  . ARG A 1 244 ? 37.57400  -3.20400  48.62500  1.000 30.20254  ?  252 ARG A CD  1 
ATOM   1824 N NE  . ARG A 1 244 ? 36.69700  -4.22700  49.20400  1.000 40.85892  ?  252 ARG A NE  1 
ATOM   1825 C CZ  . ARG A 1 244 ? 35.74700  -3.99900  50.10000  1.000 36.47699  ?  252 ARG A CZ  1 
ATOM   1826 N NH1 . ARG A 1 244 ? 35.56600  -2.78800  50.58600  1.000 35.37340  ?  252 ARG A NH1 1 
ATOM   1827 N NH2 . ARG A 1 244 ? 34.98200  -4.99000  50.51100  1.000 27.81724  ?  252 ARG A NH2 1 
ATOM   1828 N N   . ALA A 1 245 ? 41.67300  -7.25000  48.30000  1.000 28.46204  ?  253 ALA A N   1 
ATOM   1829 C CA  . ALA A 1 245 ? 42.56900  -8.19100  48.96300  1.000 23.14271  ?  253 ALA A CA  1 
ATOM   1830 C C   . ALA A 1 245 ? 44.02400  -7.89900  48.62200  1.000 22.04891  ?  253 ALA A C   1 
ATOM   1831 O O   . ALA A 1 245 ? 44.89900  -7.97800  49.48900  1.000 27.82667  ?  253 ALA A O   1 
ATOM   1832 C CB  . ALA A 1 245 ? 42.20400  -9.62300  48.58000  1.000 25.94392  ?  253 ALA A CB  1 
ATOM   1833 N N   . ALA A 1 246 ? 44.30200  -7.56100  47.36200  1.000 22.46785  ?  254 ALA A N   1 
ATOM   1834 C CA  . ALA A 1 246 ? 45.66300  -7.22800  46.96000  1.000 21.36232  ?  254 ALA A CA  1 
ATOM   1835 C C   . ALA A 1 246 ? 46.12300  -5.92500  47.59500  1.000 21.73039  ?  254 ALA A C   1 
ATOM   1836 O O   . ALA A 1 246 ? 47.30400  -5.76500  47.91100  1.000 22.92136  ?  254 ALA A O   1 
ATOM   1837 C CB  . ALA A 1 246 ? 45.75100  -7.14200  45.43800  1.000 20.29349  ?  254 ALA A CB  1 
ATOM   1838 N N   . LEU A 1 247 ? 45.20600  -4.97500  47.77200  1.000 23.84366  ?  255 LEU A N   1 
ATOM   1839 C CA  . LEU A 1 247 ? 45.54500  -3.74000  48.47000  1.000 20.90030  ?  255 LEU A CA  1 
ATOM   1840 C C   . LEU A 1 247 ? 45.97500  -4.03400  49.90200  1.000 24.27517  ?  255 LEU A C   1 
ATOM   1841 O O   . LEU A 1 247 ? 46.99600  -3.52000  50.38100  1.000 23.17080  ?  255 LEU A O   1 
ATOM   1842 C CB  . LEU A 1 247 ? 44.34500  -2.79200  48.43800  1.000 25.09603  ?  255 LEU A CB  1 
ATOM   1843 C CG  . LEU A 1 247 ? 44.51100  -1.31800  48.80500  1.000 27.51116  ?  255 LEU A CG  1 
ATOM   1844 C CD1 . LEU A 1 247 ? 43.69700  -0.47600  47.84900  1.000 21.97854  ?  255 LEU A CD1 1 
ATOM   1845 C CD2 . LEU A 1 247 ? 44.08600  -1.05400  50.23600  1.000 35.09131  ?  255 LEU A CD2 1 
ATOM   1846 N N   . LYS A 1 248 ? 45.21700  -4.89000  50.59300  1.000 23.82032  ?  256 LYS A N   1 
ATOM   1847 C CA  . LYS A 1 248 ? 45.60300  -5.28800  51.94500  1.000 21.03204  ?  256 LYS A CA  1 
ATOM   1848 C C   . LYS A 1 248 ? 46.93300  -6.03600  51.95000  1.000 20.62706  ?  256 LYS A C   1 
ATOM   1849 O O   . LYS A 1 248 ? 47.77500  -5.82100  52.83400  1.000 24.03961  ?  256 LYS A O   1 
ATOM   1850 C CB  . LYS A 1 248 ? 44.50700  -6.14400  52.57600  1.000 23.40553  ?  256 LYS A CB  1 
ATOM   1851 C CG  . LYS A 1 248 ? 43.12000  -5.54800  52.47600  1.000 25.18614  ?  256 LYS A CG  1 
ATOM   1852 C CD  . LYS A 1 248 ? 42.36400  -5.68900  53.77800  1.000 31.49811  ?  256 LYS A CD  1 
ATOM   1853 C CE  . LYS A 1 248 ? 40.86700  -5.68100  53.54600  1.000 33.35046  ?  256 LYS A CE  1 
ATOM   1854 N NZ  . LYS A 1 248 ? 40.48000  -4.71900  52.48000  1.000 36.89376  ?  256 LYS A NZ  1 
ATOM   1855 N N   . THR A 1 249 ? 47.13300  -6.92400  50.97600  1.000 18.78024  ?  257 THR A N   1 
ATOM   1856 C CA  . THR A 1 249 ? 48.37800  -7.68100  50.89300  1.000 23.63784  ?  257 THR A CA  1 
ATOM   1857 C C   . THR A 1 249 ? 49.56900  -6.75500  50.69700  1.000 29.56188  ?  257 THR A C   1 
ATOM   1858 O O   . THR A 1 249 ? 50.61000  -6.91400  51.34200  1.000 29.83921  ?  257 THR A O   1 
ATOM   1859 C CB  . THR A 1 249 ? 48.29700  -8.69500  49.75100  1.000 22.42239  ?  257 THR A CB  1 
ATOM   1860 O OG1 . THR A 1 249 ? 47.20600  -9.59300  49.97900  1.000 25.52193  ?  257 THR A OG1 1 
ATOM   1861 C CG2 . THR A 1 249 ? 49.58300  -9.49000  49.65300  1.000 26.30294  ?  257 THR A CG2 1 
ATOM   1862 N N   . ALA A 1 250 ? 49.42800  -5.77300  49.80600  1.000 27.10421  ?  258 ALA A N   1 
ATOM   1863 C CA  . ALA A 1 250 ? 50.50800  -4.83000  49.55200  1.000 26.19607  ?  258 ALA A CA  1 
ATOM   1864 C C   . ALA A 1 250 ? 50.79000  -3.97000  50.77400  1.000 26.01438  ?  258 ALA A C   1 
ATOM   1865 O O   . ALA A 1 250 ? 51.94900  -3.67300  51.07500  1.000 28.09696  ?  258 ALA A O   1 
ATOM   1866 C CB  . ALA A 1 250 ? 50.17000  -3.95800  48.34500  1.000 24.29431  ?  258 ALA A CB  1 
ATOM   1867 N N   . ALA A 1 251 ? 49.74400  -3.55400  51.49200  1.000 28.73180  ?  259 ALA A N   1 
ATOM   1868 C CA  . ALA A 1 251 ? 49.96000  -2.76600  52.70200  1.000 30.87638  ?  259 ALA A CA  1 
ATOM   1869 C C   . ALA A 1 251 ? 50.73000  -3.56400  53.74800  1.000 31.28455  ?  259 ALA A C   1 
ATOM   1870 O O   . ALA A 1 251 ? 51.69900  -3.06900  54.34100  1.000 28.47267  ?  259 ALA A O   1 
ATOM   1871 C CB  . ALA A 1 251 ? 48.62100  -2.28900  53.26200  1.000 27.60595  ?  259 ALA A CB  1 
ATOM   1872 N N   . ALA A 1 252 ? 50.31700  -4.81300  53.98000  1.000 28.54905  ?  260 ALA A N   1 
ATOM   1873 C CA  . ALA A 1 252 ? 51.01000  -5.64700  54.95700  1.000 26.37709  ?  260 ALA A CA  1 
ATOM   1874 C C   . ALA A 1 252 ? 52.44600  -5.92100  54.53100  1.000 26.69067  ?  260 ALA A C   1 
ATOM   1875 O O   . ALA A 1 252 ? 53.36300  -5.91000  55.36200  1.000 30.96753  ?  260 ALA A O   1 
ATOM   1876 C CB  . ALA A 1 252 ? 50.25000  -6.95500  55.16300  1.000 28.21040  ?  260 ALA A CB  1 
ATOM   1877 N N   . ALA A 1 253 ? 52.66000  -6.17300  53.23800  1.000 27.79699  ?  261 ALA A N   1 
ATOM   1878 C CA  . ALA A 1 253 ? 54.00600  -6.42600  52.73800  1.000 30.58017  ?  261 ALA A CA  1 
ATOM   1879 C C   . ALA A 1 253 ? 54.89000  -5.19700  52.89200  1.000 30.02840  ?  261 ALA A C   1 
ATOM   1880 O O   . ALA A 1 253 ? 56.06200  -5.31100  53.25800  1.000 34.14957  ?  261 ALA A O   1 
ATOM   1881 C CB  . ALA A 1 253 ? 53.94600  -6.87200  51.27800  1.000 30.46896  ?  261 ALA A CB  1 
ATOM   1882 N N   . LEU A 1 254 ? 54.35000  -4.01200  52.60600  1.000 24.37713  ?  262 LEU A N   1 
ATOM   1883 C CA  . LEU A 1 254 ? 55.11900  -2.78600  52.78000  1.000 27.91659  ?  262 LEU A CA  1 
ATOM   1884 C C   . LEU A 1 254 ? 55.50000  -2.59100  54.23900  1.000 25.01420  ?  262 LEU A C   1 
ATOM   1885 O O   . LEU A 1 254 ? 56.63600  -2.21600  54.55200  1.000 24.52686  ?  262 LEU A O   1 
ATOM   1886 C CB  . LEU A 1 254 ? 54.31900  -1.58800  52.27200  1.000 24.38341  ?  262 LEU A CB  1 
ATOM   1887 C CG  . LEU A 1 254 ? 54.96100  -0.21600  52.47300  1.000 22.35808  ?  262 LEU A CG  1 
ATOM   1888 C CD1 . LEU A 1 254 ? 56.22100  -0.08200  51.64200  1.000 26.86892  ?  262 LEU A CD1 1 
ATOM   1889 C CD2 . LEU A 1 254 ? 53.98100  0.89400   52.15300  1.000 27.10138  ?  262 LEU A CD2 1 
ATOM   1890 N N   . GLU A 1 255 ? 54.55700  -2.84100  55.14800  1.000 27.30010  ?  263 GLU A N   1 
ATOM   1891 C CA  . GLU A 1 255 ? 54.85800  -2.71200  56.57000  1.000 29.07229  ?  263 GLU A CA  1 
ATOM   1892 C C   . GLU A 1 255 ? 55.96300  -3.67600  56.98600  1.000 27.13464  ?  263 GLU A C   1 
ATOM   1893 O O   . GLU A 1 255 ? 56.91100  -3.29200  57.68200  1.000 24.90785  ?  263 GLU A O   1 
ATOM   1894 C CB  . GLU A 1 255 ? 53.59100  -2.94600  57.38900  1.000 28.27912  ?  263 GLU A CB  1 
ATOM   1895 C CG  . GLU A 1 255 ? 53.74800  -2.68300  58.86900  1.000 31.48240  ?  263 GLU A CG  1 
ATOM   1896 C CD  . GLU A 1 255 ? 52.43300  -2.75800  59.60700  1.000 47.79868  ?  263 GLU A CD  1 
ATOM   1897 O OE1 . GLU A 1 255 ? 51.37600  -2.67700  58.94800  1.000 48.05333  ?  263 GLU A OE1 1 
ATOM   1898 O OE2 . GLU A 1 255 ? 52.45500  -2.89700  60.84700  1.000 56.49224  -1 263 GLU A OE2 1 
ATOM   1899 N N   . GLU A 1 256 ? 55.87000  -4.93300  56.54200  1.000 33.36039  ?  264 GLU A N   1 
ATOM   1900 C CA  . GLU A 1 256 ? 56.89300  -5.92100  56.87600  1.000 35.61699  ?  264 GLU A CA  1 
ATOM   1901 C C   . GLU A 1 256 ? 58.25200  -5.52800  56.31100  1.000 33.61794  ?  264 GLU A C   1 
ATOM   1902 O O   . GLU A 1 256 ? 59.27400  -5.61200  57.00200  1.000 35.02906  ?  264 GLU A O   1 
ATOM   1903 C CB  . GLU A 1 256 ? 56.47900  -7.29800  56.35900  1.000 38.89650  ?  264 GLU A CB  1 
ATOM   1904 C CG  . GLU A 1 256 ? 57.56700  -8.35300  56.47600  1.000 51.17438  ?  264 GLU A CG  1 
ATOM   1905 C CD  . GLU A 1 256 ? 57.40600  -9.23300  57.69700  1.000 77.69726  ?  264 GLU A CD  1 
ATOM   1906 O OE1 . GLU A 1 256 ? 56.55400  -10.14500 57.66400  1.000 91.96344  ?  264 GLU A OE1 1 
ATOM   1907 O OE2 . GLU A 1 256 ? 58.13100  -9.01300  58.68900  1.000 73.27677  -1 264 GLU A OE2 1 
ATOM   1908 N N   . TYR A 1 257 ? 58.28200  -5.09600  55.04900  1.000 34.53006  ?  265 TYR A N   1 
ATOM   1909 C CA  . TYR A 1 257 ? 59.54500  -4.72900  54.42100  1.000 31.53560  ?  265 TYR A CA  1 
ATOM   1910 C C   . TYR A 1 257 ? 60.18700  -3.54500  55.12400  1.000 35.01003  ?  265 TYR A C   1 
ATOM   1911 O O   . TYR A 1 257 ? 61.39100  -3.55800  55.39600  1.000 38.78227  ?  265 TYR A O   1 
ATOM   1912 C CB  . TYR A 1 257 ? 59.32600  -4.41400  52.94100  1.000 26.93644  ?  265 TYR A CB  1 
ATOM   1913 C CG  . TYR A 1 257 ? 59.39400  -5.61800  52.03200  1.000 28.88734  ?  265 TYR A CG  1 
ATOM   1914 C CD1 . TYR A 1 257 ? 58.52200  -6.68400  52.19000  1.000 38.69278  ?  265 TYR A CD1 1 
ATOM   1915 C CD2 . TYR A 1 257 ? 60.33300  -5.68900  51.01800  1.000 35.93309  ?  265 TYR A CD2 1 
ATOM   1916 C CE1 . TYR A 1 257 ? 58.58000  -7.78300  51.36000  1.000 41.75645  ?  265 TYR A CE1 1 
ATOM   1917 C CE2 . TYR A 1 257 ? 60.40000  -6.78700  50.18500  1.000 43.74348  ?  265 TYR A CE2 1 
ATOM   1918 C CZ  . TYR A 1 257 ? 59.52100  -7.83000  50.36100  1.000 39.88082  ?  265 TYR A CZ  1 
ATOM   1919 O OH  . TYR A 1 257 ? 59.58400  -8.92400  49.53300  1.000 38.08963  ?  265 TYR A OH  1 
ATOM   1920 N N   . GLN A 1 258 ? 59.40000  -2.51400  55.43600  1.000 34.84411  ?  266 GLN A N   1 
ATOM   1921 C CA  . GLN A 1 258 ? 59.96500  -1.33800  56.08500  1.000 28.83746  ?  266 GLN A CA  1 
ATOM   1922 C C   . GLN A 1 258 ? 60.42300  -1.65800  57.50100  1.000 35.53376  ?  266 GLN A C   1 
ATOM   1923 O O   . GLN A 1 258 ? 61.44100  -1.12800  57.96000  1.000 41.07385  ?  266 GLN A O   1 
ATOM   1924 C CB  . GLN A 1 258 ? 58.95300  -0.19400  56.07400  1.000 31.61866  ?  266 GLN A CB  1 
ATOM   1925 C CG  . GLN A 1 258 ? 58.81300  0.46700   54.71000  1.000 29.91392  ?  266 GLN A CG  1 
ATOM   1926 C CD  . GLN A 1 258 ? 57.92300  1.68700   54.73500  1.000 29.20127  ?  266 GLN A CD  1 
ATOM   1927 O OE1 . GLN A 1 258 ? 57.00500  1.78200   55.54700  1.000 33.85032  ?  266 GLN A OE1 1 
ATOM   1928 N NE2 . GLN A 1 258 ? 58.18500  2.62900   53.84000  1.000 26.36206  ?  266 GLN A NE2 1 
ATOM   1929 N N   . GLY A 1 259 ? 59.70700  -2.53900  58.20200  1.000 41.64247  ?  267 GLY A N   1 
ATOM   1930 C CA  . GLY A 1 259 ? 60.18800  -2.98400  59.50000  1.000 35.63073  ?  267 GLY A CA  1 
ATOM   1931 C C   . GLY A 1 259 ? 61.50000  -3.73700  59.39900  1.000 44.08046  ?  267 GLY A C   1 
ATOM   1932 O O   . GLY A 1 259 ? 62.39000  -3.58100  60.23900  1.000 47.70229  ?  267 GLY A O   1 
ATOM   1933 N N   . VAL A 1 260 ? 61.63800  -4.56500  58.36100  1.000 44.63893  ?  268 VAL A N   1 
ATOM   1934 C CA  . VAL A 1 260 ? 62.88000  -5.30800  58.16400  1.000 47.53988  ?  268 VAL A CA  1 
ATOM   1935 C C   . VAL A 1 260 ? 64.03500  -4.35500  57.88400  1.000 42.00269  ?  268 VAL A C   1 
ATOM   1936 O O   . VAL A 1 260 ? 65.13400  -4.51200  58.43200  1.000 45.40621  ?  268 VAL A O   1 
ATOM   1937 C CB  . VAL A 1 260 ? 62.70400  -6.34700  57.04000  1.000 45.42923  ?  268 VAL A CB  1 
ATOM   1938 C CG1 . VAL A 1 260 ? 64.02900  -6.63600  56.35700  1.000 46.28114  ?  268 VAL A CG1 1 
ATOM   1939 C CG2 . VAL A 1 260 ? 62.09900  -7.62400  57.59600  1.000 43.14317  ?  268 VAL A CG2 1 
ATOM   1940 N N   . THR A 1 261 ? 63.81000  -3.35200  57.02800  1.000 40.20009  ?  269 THR A N   1 
ATOM   1941 C CA  . THR A 1 261 ? 64.85700  -2.36200  56.78100  1.000 42.53698  ?  269 THR A CA  1 
ATOM   1942 C C   . THR A 1 261 ? 65.20200  -1.59500  58.04900  1.000 44.75737  ?  269 THR A C   1 
ATOM   1943 O O   . THR A 1 261 ? 66.37400  -1.29800  58.29600  1.000 51.92278  ?  269 THR A O   1 
ATOM   1944 C CB  . THR A 1 261 ? 64.46600  -1.38800  55.66400  1.000 35.07204  ?  269 THR A CB  1 
ATOM   1945 O OG1 . THR A 1 261 ? 63.64100  -0.33900  56.18800  1.000 43.99777  ?  269 THR A OG1 1 
ATOM   1946 C CG2 . THR A 1 261 ? 63.78200  -2.08700  54.51400  1.000 32.97183  ?  269 THR A CG2 1 
ATOM   1947 N N   . THR A 1 262 ? 64.19900  -1.25200  58.86000  1.000 43.52484  ?  270 THR A N   1 
ATOM   1948 C CA  . THR A 1 262 ? 64.48000  -0.55300  60.10900  1.000 46.44068  ?  270 THR A CA  1 
ATOM   1949 C C   . THR A 1 262 ? 65.34400  -1.40300  61.03200  1.000 51.12056  ?  270 THR A C   1 
ATOM   1950 O O   . THR A 1 262 ? 66.31300  -0.90700  61.61800  1.000 43.26066  ?  270 THR A O   1 
ATOM   1951 C CB  . THR A 1 262 ? 63.17400  -0.16300  60.80200  1.000 33.09446  ?  270 THR A CB  1 
ATOM   1952 O OG1 . THR A 1 262 ? 62.44000  0.74000   59.96800  1.000 46.17662  ?  270 THR A OG1 1 
ATOM   1953 C CG2 . THR A 1 262 ? 63.45600  0.50600   62.13400  1.000 38.51365  ?  270 THR A CG2 1 
ATOM   1954 N N   . ARG A 1 263 ? 65.02200  -2.69400  61.15400  1.000 55.22791  ?  271 ARG A N   1 
ATOM   1955 C CA  . ARG A 1 263 ? 65.82700  -3.57900  61.99200  1.000 47.01368  ?  271 ARG A CA  1 
ATOM   1956 C C   . ARG A 1 263 ? 67.25000  -3.70400  61.46400  1.000 49.87449  ?  271 ARG A C   1 
ATOM   1957 O O   . ARG A 1 263 ? 68.21100  -3.66800  62.24200  1.000 55.58228  ?  271 ARG A O   1 
ATOM   1958 C CB  . ARG A 1 263 ? 65.17500  -4.95800  62.08300  1.000 57.36456  ?  271 ARG A CB  1 
ATOM   1959 C CG  . ARG A 1 263 ? 63.81600  -4.96600  62.75500  1.000 66.61604  ?  271 ARG A CG  1 
ATOM   1960 C CD  . ARG A 1 263 ? 63.05300  -6.23700  62.42600  1.000 69.97961  ?  271 ARG A CD  1 
ATOM   1961 N NE  . ARG A 1 263 ? 63.94800  -7.35700  62.16300  1.000 73.89799  ?  271 ARG A NE  1 
ATOM   1962 C CZ  . ARG A 1 263 ? 63.56100  -8.52400  61.66700  1.000 73.41230  ?  271 ARG A CZ  1 
ATOM   1963 N NH1 . ARG A 1 263 ? 62.29500  -8.75900  61.36300  1.000 67.11611  ?  271 ARG A NH1 1 
ATOM   1964 N NH2 . ARG A 1 263 ? 64.46600  -9.47700  61.46900  1.000 62.94681  ?  271 ARG A NH2 1 
ATOM   1965 N N   . GLN A 1 264 ? 67.40500  -3.85100  60.14800  1.000 47.15992  ?  272 GLN A N   1 
ATOM   1966 C CA  . GLN A 1 264 ? 68.73700  -4.00500  59.57100  1.000 55.35909  ?  272 GLN A CA  1 
ATOM   1967 C C   . GLN A 1 264 ? 69.56900  -2.74200  59.75800  1.000 50.85917  ?  272 GLN A C   1 
ATOM   1968 O O   . GLN A 1 264 ? 70.74900  -2.80600  60.12700  1.000 49.46669  ?  272 GLN A O   1 
ATOM   1969 C CB  . GLN A 1 264 ? 68.61900  -4.37100  58.09100  1.000 49.94540  ?  272 GLN A CB  1 
ATOM   1970 C CG  . GLN A 1 264 ? 68.11700  -5.78700  57.85100  1.000 48.99048  ?  272 GLN A CG  1 
ATOM   1971 C CD  . GLN A 1 264 ? 67.67700  -6.02400  56.42100  1.000 62.30287  ?  272 GLN A CD  1 
ATOM   1972 O OE1 . GLN A 1 264 ? 67.44800  -5.08100  55.66400  1.000 54.44741  ?  272 GLN A OE1 1 
ATOM   1973 N NE2 . GLN A 1 264 ? 67.55200  -7.29100  56.04500  1.000 55.43369  ?  272 GLN A NE2 1 
ATOM   1974 N N   . LEU A 1 265 ? 68.96300  -1.57700  59.51900  1.000 55.06158  ?  273 LEU A N   1 
ATOM   1975 C CA  . LEU A 1 265 ? 69.67600  -0.31800  59.69400  1.000 51.41405  ?  273 LEU A CA  1 
ATOM   1976 C C   . LEU A 1 265 ? 70.03500  -0.08700  61.15400  1.000 48.83880  ?  273 LEU A C   1 
ATOM   1977 O O   . LEU A 1 265 ? 71.10800  0.44400   61.45900  1.000 49.02375  ?  273 LEU A O   1 
ATOM   1978 C CB  . LEU A 1 265 ? 68.83600  0.83700   59.15200  1.000 52.20528  ?  273 LEU A CB  1 
ATOM   1979 C CG  . LEU A 1 265 ? 68.64200  0.86500   57.63600  1.000 46.83064  ?  273 LEU A CG  1 
ATOM   1980 C CD1 . LEU A 1 265 ? 67.82600  2.07100   57.21700  1.000 37.92317  ?  273 LEU A CD1 1 
ATOM   1981 C CD2 . LEU A 1 265 ? 69.98600  0.85600   56.93200  1.000 50.24196  ?  273 LEU A CD2 1 
ATOM   1982 N N   . SER A 1 266 ? 69.14800  -0.47200  62.07500  1.000 48.93935  ?  274 SER A N   1 
ATOM   1983 C CA  . SER A 1 266 ? 69.47000  -0.34700  63.49100  1.000 49.32374  ?  274 SER A CA  1 
ATOM   1984 C C   . SER A 1 266 ? 70.63600  -1.25100  63.87000  1.000 58.46355  ?  274 SER A C   1 
ATOM   1985 O O   . SER A 1 266 ? 71.54500  -0.83200  64.59600  1.000 54.24908  ?  274 SER A O   1 
ATOM   1986 C CB  . SER A 1 266 ? 68.23900  -0.66400  64.33900  1.000 43.80412  ?  274 SER A CB  1 
ATOM   1987 O OG  . SER A 1 266 ? 68.07200  -2.05800  64.51400  1.000 54.13929  ?  274 SER A OG  1 
ATOM   1988 N N   . GLU A 1 267 ? 70.63300  -2.49400  63.38400  1.000 63.65091  ?  275 GLU A N   1 
ATOM   1989 C CA  . GLU A 1 267 ? 71.72900  -3.40400  63.69400  1.000 54.32221  ?  275 GLU A CA  1 
ATOM   1990 C C   . GLU A 1 267 ? 73.03400  -2.99700  63.03500  1.000 56.73966  ?  275 GLU A C   1 
ATOM   1991 O O   . GLU A 1 267 ? 74.09800  -3.39100  63.52100  1.000 59.72681  ?  275 GLU A O   1 
ATOM   1992 C CB  . GLU A 1 267 ? 71.36200  -4.83200  63.28700  1.000 53.27220  ?  275 GLU A CB  1 
ATOM   1993 C CG  . GLU A 1 267 ? 70.91400  -5.70300  64.45100  1.000 58.81876  ?  275 GLU A CG  1 
ATOM   1994 C CD  . GLU A 1 267 ? 69.69800  -6.54400  64.11900  1.000 76.70010  ?  275 GLU A CD  1 
ATOM   1995 O OE1 . GLU A 1 267 ? 69.54700  -6.93700  62.94400  1.000 77.14539  ?  275 GLU A OE1 1 
ATOM   1996 O OE2 . GLU A 1 267 ? 68.89200  -6.81200  65.03400  1.000 75.57687  -1 275 GLU A OE2 1 
ATOM   1997 N N   . VAL A 1 268 ? 72.98400  -2.23400  61.94700  1.000 63.30731  ?  276 VAL A N   1 
ATOM   1998 C CA  . VAL A 1 268 ? 74.18100  -1.66500  61.34400  1.000 57.77862  ?  276 VAL A CA  1 
ATOM   1999 C C   . VAL A 1 268 ? 74.69600  -0.47000  62.13800  1.000 63.91496  ?  276 VAL A C   1 
ATOM   2000 O O   . VAL A 1 268 ? 75.88600  -0.38900  62.44600  1.000 68.96465  ?  276 VAL A O   1 
ATOM   2001 C CB  . VAL A 1 268 ? 73.90200  -1.28200  59.87500  1.000 50.35301  ?  276 VAL A CB  1 
ATOM   2002 C CG1 . VAL A 1 268 ? 74.80100  -0.13700  59.43100  1.000 48.20275  ?  276 VAL A CG1 1 
ATOM   2003 C CG2 . VAL A 1 268 ? 74.08000  -2.48800  58.97100  1.000 55.52113  ?  276 VAL A CG2 1 
ATOM   2004 N N   . LEU A 1 269 ? 73.80300  0.45800   62.49300  1.000 62.89489  ?  277 LEU A N   1 
ATOM   2005 C CA  . LEU A 1 269 ? 74.21200  1.65000   63.22600  1.000 58.51737  ?  277 LEU A CA  1 
ATOM   2006 C C   . LEU A 1 269 ? 74.72900  1.31200   64.61800  1.000 70.50629  ?  277 LEU A C   1 
ATOM   2007 O O   . LEU A 1 269 ? 75.68900  1.93400   65.08600  1.000 71.74973  ?  277 LEU A O   1 
ATOM   2008 C CB  . LEU A 1 269 ? 73.04600  2.63700   63.32800  1.000 60.13052  ?  277 LEU A CB  1 
ATOM   2009 C CG  . LEU A 1 269 ? 72.54700  3.23400   62.01000  1.000 61.03481  ?  277 LEU A CG  1 
ATOM   2010 C CD1 . LEU A 1 269 ? 71.30100  4.07500   62.24200  1.000 40.42900  ?  277 LEU A CD1 1 
ATOM   2011 C CD2 . LEU A 1 269 ? 73.63800  4.05600   61.34400  1.000 64.91118  ?  277 LEU A CD2 1 
ATOM   2012 N N   . ARG A 1 270 ? 74.10900  0.34600   65.29800  1.000 75.33387  ?  278 ARG A N   1 
ATOM   2013 C CA  . ARG A 1 270 ? 74.59100  -0.05000  66.61700  1.000 64.22621  ?  278 ARG A CA  1 
ATOM   2014 C C   . ARG A 1 270 ? 75.94400  -0.74100  66.51700  1.000 73.50791  ?  278 ARG A C   1 
ATOM   2015 O O   . ARG A 1 270 ? 76.86600  -0.43900  67.28400  1.000 75.22592  ?  278 ARG A O   1 
ATOM   2016 C CB  . ARG A 1 270 ? 73.56900  -0.95900  67.29700  1.000 53.19764  ?  278 ARG A CB  1 
ATOM   2017 N N   . HIS A 1 271 ? 76.08500  -1.67000  65.56900  1.000 80.94236  ?  279 HIS A N   1 
ATOM   2018 C CA  . HIS A 1 271 ? 77.34800  -2.37200  65.38500  1.000 83.82628  ?  279 HIS A CA  1 
ATOM   2019 C C   . HIS A 1 271 ? 78.45700  -1.46500  64.87500  1.000 86.63426  ?  279 HIS A C   1 
ATOM   2020 O O   . HIS A 1 271 ? 79.62900  -1.84500  64.96200  1.000 96.20420  ?  279 HIS A O   1 
ATOM   2021 C CB  . HIS A 1 271 ? 77.16400  -3.55000  64.42600  1.000 76.33382  ?  279 HIS A CB  1 
ATOM   2022 N N   . GLY A 1 272 ? 78.12200  -0.29400  64.33700  1.000 78.19157  ?  280 GLY A N   1 
ATOM   2023 C CA  . GLY A 1 272 ? 79.14500  0.65000   63.93200  1.000 84.11350  ?  280 GLY A CA  1 
ATOM   2024 C C   . GLY A 1 272 ? 80.00900  1.09400   65.09400  1.000 84.67319  ?  280 GLY A C   1 
ATOM   2025 O O   . GLY A 1 272 ? 81.19000  0.74200   65.16400  1.000 81.77073  ?  280 GLY A O   1 
ATOM   2026 N N   . LEU A 1 273 ? 79.42600  1.85000   66.01800  1.000 81.97022  ?  281 LEU A N   1 
ATOM   2027 C CA  . LEU A 1 273 ? 80.12300  2.27900   67.22600  1.000 74.21989  ?  281 LEU A CA  1 
ATOM   2028 C C   . LEU A 1 273 ? 79.14500  2.85900   68.23900  1.000 65.32502  ?  281 LEU A C   1 
ATOM   2029 O O   . LEU A 1 273 ? 79.45900  3.82300   68.93600  1.000 63.08183  ?  281 LEU A O   1 
ATOM   2030 C CB  . LEU A 1 273 ? 81.20500  3.30900   66.89700  1.000 62.42331  ?  281 LEU A CB  1 
ATOM   2031 N N   . ASP B 1 3   ? 31.72800  13.63800  -15.77300 1.000 90.83444  ?  11  ASP B N   1 
ATOM   2032 C CA  . ASP B 1 3   ? 31.75300  13.42300  -14.33100 1.000 92.31502  ?  11  ASP B CA  1 
ATOM   2033 C C   . ASP B 1 3   ? 30.93900  12.19400  -13.94100 1.000 87.55885  ?  11  ASP B C   1 
ATOM   2034 O O   . ASP B 1 3   ? 30.24000  12.20100  -12.93200 1.000 84.97041  ?  11  ASP B O   1 
ATOM   2035 C CB  . ASP B 1 3   ? 31.22500  14.65800  -13.59800 1.000 80.93027  ?  11  ASP B CB  1 
ATOM   2036 N N   . GLY B 1 4   ? 31.03500  11.14000  -14.74800 1.000 84.63410  ?  12  GLY B N   1 
ATOM   2037 C CA  . GLY B 1 4   ? 30.26300  9.93500   -14.51700 1.000 72.79934  ?  12  GLY B CA  1 
ATOM   2038 C C   . GLY B 1 4   ? 30.58600  9.23500   -13.21400 1.000 77.36502  ?  12  GLY B C   1 
ATOM   2039 O O   . GLY B 1 4   ? 29.67900  8.85400   -12.46800 1.000 77.90166  ?  12  GLY B O   1 
ATOM   2040 N N   . ILE B 1 5   ? 31.87700  9.06400   -12.92500 1.000 81.29890  ?  13  ILE B N   1 
ATOM   2041 C CA  . ILE B 1 5   ? 32.27400  8.41100   -11.68100 1.000 80.41395  ?  13  ILE B CA  1 
ATOM   2042 C C   . ILE B 1 5   ? 31.93600  9.29100   -10.48500 1.000 75.04498  ?  13  ILE B C   1 
ATOM   2043 O O   . ILE B 1 5   ? 31.51000  8.79900   -9.43100  1.000 67.94208  ?  13  ILE B O   1 
ATOM   2044 C CB  . ILE B 1 5   ? 33.76800  8.03500   -11.72500 1.000 66.55747  ?  13  ILE B CB  1 
ATOM   2045 C CG1 . ILE B 1 5   ? 34.63400  9.24400   -12.08300 1.000 67.36257  ?  13  ILE B CG1 1 
ATOM   2046 C CG2 . ILE B 1 5   ? 34.00100  6.90400   -12.71000 1.000 71.32401  ?  13  ILE B CG2 1 
ATOM   2047 C CD1 . ILE B 1 5   ? 35.25100  9.94000   -10.89700 1.000 76.26552  ?  13  ILE B CD1 1 
ATOM   2048 N N   . TYR B 1 6   ? 32.10200  10.60700  -10.63200 1.000 70.76914  ?  14  TYR B N   1 
ATOM   2049 C CA  . TYR B 1 6   ? 31.72600  11.52000  -9.56000  1.000 69.34873  ?  14  TYR B CA  1 
ATOM   2050 C C   . TYR B 1 6   ? 30.23200  11.43800  -9.27700  1.000 69.99565  ?  14  TYR B C   1 
ATOM   2051 O O   . TYR B 1 6   ? 29.81400  11.38300  -8.11700  1.000 69.82056  ?  14  TYR B O   1 
ATOM   2052 C CB  . TYR B 1 6   ? 32.12800  12.95000  -9.92300  1.000 65.62297  ?  14  TYR B CB  1 
ATOM   2053 C CG  . TYR B 1 6   ? 33.60600  13.13100  -10.18300 1.000 72.47129  ?  14  TYR B CG  1 
ATOM   2054 C CD1 . TYR B 1 6   ? 34.52300  13.11600  -9.14300  1.000 74.91531  ?  14  TYR B CD1 1 
ATOM   2055 C CD2 . TYR B 1 6   ? 34.08400  13.32600  -11.47000 1.000 76.13605  ?  14  TYR B CD2 1 
ATOM   2056 C CE1 . TYR B 1 6   ? 35.87300  13.28300  -9.37800  1.000 75.50323  ?  14  TYR B CE1 1 
ATOM   2057 C CE2 . TYR B 1 6   ? 35.43300  13.49400  -11.71500 1.000 74.71909  ?  14  TYR B CE2 1 
ATOM   2058 C CZ  . TYR B 1 6   ? 36.32300  13.47200  -10.66500 1.000 75.90750  ?  14  TYR B CZ  1 
ATOM   2059 O OH  . TYR B 1 6   ? 37.66700  13.64000  -10.90400 1.000 65.11649  ?  14  TYR B OH  1 
ATOM   2060 N N   . ALA B 1 7   ? 29.41300  11.40400  -10.33000 1.000 67.55090  ?  15  ALA B N   1 
ATOM   2061 C CA  . ALA B 1 7   ? 27.96900  11.30500  -10.14400 1.000 55.45008  ?  15  ALA B CA  1 
ATOM   2062 C C   . ALA B 1 7   ? 27.57900  9.96700   -9.52900  1.000 58.91199  ?  15  ALA B C   1 
ATOM   2063 O O   . ALA B 1 7   ? 26.67000  9.90200   -8.69400  1.000 57.73022  ?  15  ALA B O   1 
ATOM   2064 C CB  . ALA B 1 7   ? 27.25300  11.51400  -11.47700 1.000 62.94775  ?  15  ALA B CB  1 
ATOM   2065 N N   . ALA B 1 8   ? 28.24400  8.88500   -9.93900  1.000 61.16440  ?  16  ALA B N   1 
ATOM   2066 C CA  . ALA B 1 8   ? 27.95900  7.58200   -9.34700  1.000 59.90509  ?  16  ALA B CA  1 
ATOM   2067 C C   . ALA B 1 8   ? 28.28300  7.57300   -7.86000  1.000 53.79869  ?  16  ALA B C   1 
ATOM   2068 O O   . ALA B 1 8   ? 27.51000  7.04700   -7.04900  1.000 56.58996  ?  16  ALA B O   1 
ATOM   2069 C CB  . ALA B 1 8   ? 28.74100  6.49000   -10.07500 1.000 61.46633  ?  16  ALA B CB  1 
ATOM   2070 N N   . PHE B 1 9   ? 29.41800  8.16100   -7.48000  1.000 52.53667  ?  17  PHE B N   1 
ATOM   2071 C CA  . PHE B 1 9   ? 29.74500  8.28700   -6.06400  1.000 54.38090  ?  17  PHE B CA  1 
ATOM   2072 C C   . PHE B 1 9   ? 28.72100  9.16000   -5.34900  1.000 51.77731  ?  17  PHE B C   1 
ATOM   2073 O O   . PHE B 1 9   ? 28.39000  8.92500   -4.18200  1.000 47.58444  ?  17  PHE B O   1 
ATOM   2074 C CB  . PHE B 1 9   ? 31.15400  8.85500   -5.90000  1.000 48.90975  ?  17  PHE B CB  1 
ATOM   2075 C CG  . PHE B 1 9   ? 31.67900  8.77700   -4.49600  1.000 50.06586  ?  17  PHE B CG  1 
ATOM   2076 C CD1 . PHE B 1 9   ? 32.34800  7.64900   -4.05600  1.000 41.25855  ?  17  PHE B CD1 1 
ATOM   2077 C CD2 . PHE B 1 9   ? 31.49900  9.82900   -3.61600  1.000 49.62617  ?  17  PHE B CD2 1 
ATOM   2078 C CE1 . PHE B 1 9   ? 32.83100  7.57400   -2.76800  1.000 37.33975  ?  17  PHE B CE1 1 
ATOM   2079 C CE2 . PHE B 1 9   ? 31.98100  9.75800   -2.32600  1.000 47.68391  ?  17  PHE B CE2 1 
ATOM   2080 C CZ  . PHE B 1 9   ? 32.64700  8.62900   -1.90200  1.000 47.04848  ?  17  PHE B CZ  1 
ATOM   2081 N N   . ASP B 1 10  ? 28.20900  10.18000  -6.04200  1.000 47.72501  ?  18  ASP B N   1 
ATOM   2082 C CA  . ASP B 1 10  ? 27.18700  11.03700  -5.45300  1.000 47.18075  ?  18  ASP B CA  1 
ATOM   2083 C C   . ASP B 1 10  ? 25.91700  10.25500  -5.13800  1.000 50.63932  ?  18  ASP B C   1 
ATOM   2084 O O   . ASP B 1 10  ? 25.33800  10.41400  -4.06100  1.000 50.52199  ?  18  ASP B O   1 
ATOM   2085 C CB  . ASP B 1 10  ? 26.88200  12.20600  -6.38900  1.000 51.74604  ?  18  ASP B CB  1 
ATOM   2086 C CG  . ASP B 1 10  ? 27.78800  13.39500  -6.15000  1.000 55.67021  ?  18  ASP B CG  1 
ATOM   2087 O OD1 . ASP B 1 10  ? 27.50800  14.17800  -5.22100  1.000 61.76827  ?  18  ASP B OD1 1 
ATOM   2088 O OD2 . ASP B 1 10  ? 28.77500  13.55700  -6.89100  1.000 57.14269  -1 18  ASP B OD2 1 
ATOM   2089 N N   . THR B 1 11  ? 25.46700  9.40500   -6.06400  1.000 49.47708  ?  19  THR B N   1 
ATOM   2090 C CA  . THR B 1 11  ? 24.29600  8.57500   -5.77800  1.000 46.17751  ?  19  THR B CA  1 
ATOM   2091 C C   . THR B 1 11  ? 24.58800  7.55900   -4.67900  1.000 50.51028  ?  19  THR B C   1 
ATOM   2092 O O   . THR B 1 11  ? 23.72200  7.26700   -3.84100  1.000 54.71615  ?  19  THR B O   1 
ATOM   2093 C CB  . THR B 1 11  ? 23.79700  7.86400   -7.03900  1.000 56.42313  ?  19  THR B CB  1 
ATOM   2094 O OG1 . THR B 1 11  ? 24.47700  6.61200   -7.19800  1.000 55.36955  ?  19  THR B OG1 1 
ATOM   2095 C CG2 . THR B 1 11  ? 23.96700  8.72100   -8.27200  1.000 52.43096  ?  19  THR B CG2 1 
ATOM   2096 N N   . LEU B 1 12  ? 25.80300  7.00900   -4.66500  1.000 53.00290  ?  20  LEU B N   1 
ATOM   2097 C CA  . LEU B 1 12  ? 26.17500  6.06800   -3.61300  1.000 47.72166  ?  20  LEU B CA  1 
ATOM   2098 C C   . LEU B 1 12  ? 26.10300  6.73100   -2.24300  1.000 47.86965  ?  20  LEU B C   1 
ATOM   2099 O O   . LEU B 1 12  ? 25.67200  6.11700   -1.26200  1.000 49.10590  ?  20  LEU B O   1 
ATOM   2100 C CB  . LEU B 1 12  ? 27.57500  5.51700   -3.87600  1.000 42.11538  ?  20  LEU B CB  1 
ATOM   2101 C CG  . LEU B 1 12  ? 28.13200  4.56700   -2.81800  1.000 44.06120  ?  20  LEU B CG  1 
ATOM   2102 C CD1 . LEU B 1 12  ? 27.31800  3.29100   -2.78400  1.000 33.92955  ?  20  LEU B CD1 1 
ATOM   2103 C CD2 . LEU B 1 12  ? 29.59700  4.27000   -3.07800  1.000 38.54238  ?  20  LEU B CD2 1 
ATOM   2104 N N   . MET B 1 13  ? 26.53100  7.99000   -2.15700  1.000 43.34483  ?  21  MET B N   1 
ATOM   2105 C CA  . MET B 1 13  ? 26.42300  8.71700   -0.89700  1.000 43.51028  ?  21  MET B CA  1 
ATOM   2106 C C   . MET B 1 13  ? 24.97900  9.10100   -0.60300  1.000 48.51581  ?  21  MET B C   1 
ATOM   2107 O O   . MET B 1 13  ? 24.56500  9.14000   0.56100   1.000 55.37932  ?  21  MET B O   1 
ATOM   2108 C CB  . MET B 1 13  ? 27.31300  9.95800   -0.92800  1.000 49.33331  ?  21  MET B CB  1 
ATOM   2109 C CG  . MET B 1 13  ? 28.79800  9.66100   -1.01400  1.000 47.43235  ?  21  MET B CG  1 
ATOM   2110 S SD  . MET B 1 13  ? 29.40100  8.60900   0.31600   1.000 43.99713  ?  21  MET B SD  1 
ATOM   2111 C CE  . MET B 1 13  ? 29.70600  7.08000   -0.55700  1.000 39.10844  ?  21  MET B CE  1 
ATOM   2112 N N   . SER B 1 14  ? 24.19800  9.39400   -1.64400  1.000 47.34947  ?  22  SER B N   1 
ATOM   2113 C CA  . SER B 1 14  ? 22.81600  9.80900   -1.43900  1.000 46.38833  ?  22  SER B CA  1 
ATOM   2114 C C   . SER B 1 14  ? 21.96300  8.67100   -0.90400  1.000 50.61281  ?  22  SER B C   1 
ATOM   2115 O O   . SER B 1 14  ? 20.95500  8.91600   -0.23300  1.000 49.80391  ?  22  SER B O   1 
ATOM   2116 C CB  . SER B 1 14  ? 22.22400  10.34100  -2.74400  1.000 50.80801  ?  22  SER B CB  1 
ATOM   2117 O OG  . SER B 1 14  ? 21.83200  9.28100   -3.59800  1.000 51.15930  ?  22  SER B OG  1 
ATOM   2118 N N   . THR B 1 15  ? 22.33300  7.42400   -1.20200  1.000 49.42462  ?  23  THR B N   1 
ATOM   2119 C CA  . THR B 1 15  ? 21.60100  6.31000   -0.60400  1.000 54.25175  ?  23  THR B CA  1 
ATOM   2120 C C   . THR B 1 15  ? 21.73600  6.28100   0.91300   1.000 52.97536  ?  23  THR B C   1 
ATOM   2121 O O   . THR B 1 15  ? 20.91000  5.65400   1.58400   1.000 56.83783  ?  23  THR B O   1 
ATOM   2122 C CB  . THR B 1 15  ? 22.05800  4.97000   -1.17900  1.000 52.03542  ?  23  THR B CB  1 
ATOM   2123 O OG1 . THR B 1 15  ? 23.43300  4.74500   -0.85300  1.000 47.52050  ?  23  THR B OG1 1 
ATOM   2124 C CG2 . THR B 1 15  ? 21.88000  4.95600   -2.67500  1.000 57.37422  ?  23  THR B CG2 1 
ATOM   2125 N N   . ALA B 1 16  ? 22.75300  6.93800   1.46500   1.000 49.46793  ?  24  ALA B N   1 
ATOM   2126 C CA  . ALA B 1 16  ? 22.90300  7.09400   2.90400   1.000 49.36484  ?  24  ALA B CA  1 
ATOM   2127 C C   . ALA B 1 16  ? 22.46500  8.46700   3.39100   1.000 45.29108  ?  24  ALA B C   1 
ATOM   2128 O O   . ALA B 1 16  ? 22.66000  8.78700   4.56500   1.000 45.17240  ?  24  ALA B O   1 
ATOM   2129 C CB  . ALA B 1 16  ? 24.35200  6.83600   3.31700   1.000 43.52367  ?  24  ALA B CB  1 
ATOM   2130 N N   . GLY B 1 17  ? 21.87800  9.28200   2.51900   1.000 44.80914  ?  25  GLY B N   1 
ATOM   2131 C CA  . GLY B 1 17  ? 21.48000  10.62000  2.90600   1.000 42.29461  ?  25  GLY B CA  1 
ATOM   2132 C C   . GLY B 1 17  ? 22.60600  11.62200  2.97700   1.000 44.64004  ?  25  GLY B C   1 
ATOM   2133 O O   . GLY B 1 17  ? 22.48400  12.62600  3.68100   1.000 53.39622  ?  25  GLY B O   1 
ATOM   2134 N N   . VAL B 1 18  ? 23.70100  11.38400  2.26400   1.000 43.93748  ?  26  VAL B N   1 
ATOM   2135 C CA  . VAL B 1 18  ? 24.86500  12.26200  2.27900   1.000 45.50428  ?  26  VAL B CA  1 
ATOM   2136 C C   . VAL B 1 18  ? 24.86500  13.08600  1.00000   1.000 45.38232  ?  26  VAL B C   1 
ATOM   2137 O O   . VAL B 1 18  ? 24.86200  12.53200  -0.10600  1.000 44.97960  ?  26  VAL B O   1 
ATOM   2138 C CB  . VAL B 1 18  ? 26.16800  11.46100  2.41800   1.000 46.12514  ?  26  VAL B CB  1 
ATOM   2139 C CG1 . VAL B 1 18  ? 27.33300  12.39000  2.69400   1.000 42.17200  ?  26  VAL B CG1 1 
ATOM   2140 C CG2 . VAL B 1 18  ? 26.03800  10.42900  3.52200   1.000 46.75171  ?  26  VAL B CG2 1 
ATOM   2141 N N   . ASP B 1 19  ? 24.87000  14.41000  1.14700   1.000 44.18920  ?  27  ASP B N   1 
ATOM   2142 C CA  . ASP B 1 19  ? 24.95700  15.32200  0.00800   1.000 53.26171  ?  27  ASP B CA  1 
ATOM   2143 C C   . ASP B 1 19  ? 26.43200  15.61600  -0.23300  1.000 51.42425  ?  27  ASP B C   1 
ATOM   2144 O O   . ASP B 1 19  ? 26.96100  16.64900  0.17800   1.000 47.38531  ?  27  ASP B O   1 
ATOM   2145 C CB  . ASP B 1 19  ? 24.15700  16.59200  0.26800   1.000 46.63560  ?  27  ASP B CB  1 
ATOM   2146 C CG  . ASP B 1 19  ? 24.01600  17.45400  -0.96800  1.000 53.28243  ?  27  ASP B CG  1 
ATOM   2147 O OD1 . ASP B 1 19  ? 24.35000  16.97500  -2.07100  1.000 49.38243  ?  27  ASP B OD1 1 
ATOM   2148 O OD2 . ASP B 1 19  ? 23.57100  18.61300  -0.83700  1.000 68.82498  -1 27  ASP B OD2 1 
ATOM   2149 N N   . SER B 1 20  ? 27.10300  14.68800  -0.91400  1.000 49.04678  ?  28  SER B N   1 
ATOM   2150 C CA  . SER B 1 20  ? 28.54600  14.78200  -1.09000  1.000 45.71688  ?  28  SER B CA  1 
ATOM   2151 C C   . SER B 1 20  ? 28.94700  15.89300  -2.05100  1.000 53.58764  ?  28  SER B C   1 
ATOM   2152 O O   . SER B 1 20  ? 29.97000  16.55000  -1.83000  1.000 55.62746  ?  28  SER B O   1 
ATOM   2153 C CB  . SER B 1 20  ? 29.09900  13.44000  -1.57000  1.000 44.51877  ?  28  SER B CB  1 
ATOM   2154 O OG  . SER B 1 20  ? 28.46200  13.02300  -2.76100  1.000 50.81041  ?  28  SER B OG  1 
ATOM   2155 N N   . GLN B 1 21  ? 28.16400  16.11600  -3.10900  1.000 54.64534  ?  29  GLN B N   1 
ATOM   2156 C CA  . GLN B 1 21  ? 28.45100  17.15200  -4.10500  1.000 54.53685  ?  29  GLN B CA  1 
ATOM   2157 C C   . GLN B 1 21  ? 29.85000  16.98500  -4.69000  1.000 56.71996  ?  29  GLN B C   1 
ATOM   2158 O O   . GLN B 1 21  ? 30.57800  17.95500  -4.90800  1.000 52.53578  ?  29  GLN B O   1 
ATOM   2159 C CB  . GLN B 1 21  ? 28.27200  18.55200  -3.51200  1.000 51.13024  ?  29  GLN B CB  1 
ATOM   2160 C CG  . GLN B 1 21  ? 26.83500  18.92900  -3.19300  1.000 45.59828  ?  29  GLN B CG  1 
ATOM   2161 C CD  . GLN B 1 21  ? 26.04200  19.32700  -4.42200  1.000 60.12348  ?  29  GLN B CD  1 
ATOM   2162 O OE1 . GLN B 1 21  ? 25.87600  18.53900  -5.35300  1.000 58.08156  ?  29  GLN B OE1 1 
ATOM   2163 N NE2 . GLN B 1 21  ? 25.54800  20.55800  -4.43100  1.000 61.90575  ?  29  GLN B NE2 1 
ATOM   2164 N N   . ILE B 1 22  ? 30.22900  15.73300  -4.94800  1.000 54.95051  ?  30  ILE B N   1 
ATOM   2165 C CA  . ILE B 1 22  ? 31.57100  15.44900  -5.44400  1.000 56.12470  ?  30  ILE B CA  1 
ATOM   2166 C C   . ILE B 1 22  ? 31.73700  15.95200  -6.87300  1.000 58.88258  ?  30  ILE B C   1 
ATOM   2167 O O   . ILE B 1 22  ? 32.79600  16.47300  -7.24200  1.000 59.34491  ?  30  ILE B O   1 
ATOM   2168 C CB  . ILE B 1 22  ? 31.86700  13.94300  -5.32900  1.000 52.46120  ?  30  ILE B CB  1 
ATOM   2169 C CG1 . ILE B 1 22  ? 31.86700  13.51800  -3.86200  1.000 56.40425  ?  30  ILE B CG1 1 
ATOM   2170 C CG2 . ILE B 1 22  ? 33.20000  13.61000  -5.96300  1.000 50.04849  ?  30  ILE B CG2 1 
ATOM   2171 C CD1 . ILE B 1 22  ? 32.92100  14.20600  -3.02800  1.000 45.62999  ?  30  ILE B CD1 1 
ATOM   2172 N N   . ALA B 1 23  ? 30.70100  15.79900  -7.70000  1.000 64.27358  ?  31  ALA B N   1 
ATOM   2173 C CA  . ALA B 1 23  ? 30.78000  16.25300  -9.08400  1.000 63.02742  ?  31  ALA B CA  1 
ATOM   2174 C C   . ALA B 1 23  ? 30.96000  17.76400  -9.15600  1.000 59.17222  ?  31  ALA B C   1 
ATOM   2175 O O   . ALA B 1 23  ? 31.73900  18.27200  -9.97100  1.000 56.30484  ?  31  ALA B O   1 
ATOM   2176 C CB  . ALA B 1 23  ? 29.53100  15.82000  -9.85000  1.000 67.44749  ?  31  ALA B CB  1 
ATOM   2177 N N   . ALA B 1 24  ? 30.24100  18.50000  -8.30700  1.000 59.07170  ?  32  ALA B N   1 
ATOM   2178 C CA  . ALA B 1 24  ? 30.40500  19.94800  -8.26600  1.000 54.49169  ?  32  ALA B CA  1 
ATOM   2179 C C   . ALA B 1 24  ? 31.81400  20.32800  -7.83300  1.000 60.03161  ?  32  ALA B C   1 
ATOM   2180 O O   . ALA B 1 24  ? 32.40400  21.27100  -8.37300  1.000 62.45984  ?  32  ALA B O   1 
ATOM   2181 C CB  . ALA B 1 24  ? 29.36700  20.56700  -7.33100  1.000 49.15595  ?  32  ALA B CB  1 
ATOM   2182 N N   . LEU B 1 25  ? 32.36800  19.60800  -6.85500  1.000 56.38963  ?  33  LEU B N   1 
ATOM   2183 C CA  . LEU B 1 25  ? 33.73100  19.88300  -6.41300  1.000 51.85571  ?  33  LEU B CA  1 
ATOM   2184 C C   . LEU B 1 25  ? 34.73600  19.62600  -7.52800  1.000 56.89560  ?  33  LEU B C   1 
ATOM   2185 O O   . LEU B 1 25  ? 35.68600  20.39600  -7.70700  1.000 63.60891  ?  33  LEU B O   1 
ATOM   2186 C CB  . LEU B 1 25  ? 34.06800  19.03600  -5.18800  1.000 54.23998  ?  33  LEU B CB  1 
ATOM   2187 C CG  . LEU B 1 25  ? 35.40500  19.36100  -4.52300  1.000 46.34913  ?  33  LEU B CG  1 
ATOM   2188 C CD1 . LEU B 1 25  ? 35.39700  20.77900  -3.97900  1.000 41.42670  ?  33  LEU B CD1 1 
ATOM   2189 C CD2 . LEU B 1 25  ? 35.71500  18.36500  -3.42600  1.000 47.54904  ?  33  LEU B CD2 1 
ATOM   2190 N N   . ALA B 1 26  ? 34.55000  18.54100  -8.28100  1.000 56.65787  ?  34  ALA B N   1 
ATOM   2191 C CA  . ALA B 1 26  ? 35.44300  18.26000  -9.39900  1.000 54.71957  ?  34  ALA B CA  1 
ATOM   2192 C C   . ALA B 1 26  ? 35.29000  19.29800  -10.50200 1.000 60.26266  ?  34  ALA B C   1 
ATOM   2193 O O   . ALA B 1 26  ? 36.25700  19.60900  -11.20700 1.000 61.80029  ?  34  ALA B O   1 
ATOM   2194 C CB  . ALA B 1 26  ? 35.18200  16.85600  -9.94200  1.000 57.27941  ?  34  ALA B CB  1 
ATOM   2195 N N   . ALA B 1 27  ? 34.08200  19.84200  -10.66800 1.000 59.82146  ?  35  ALA B N   1 
ATOM   2196 C CA  . ALA B 1 27  ? 33.86000  20.85100  -11.69800 1.000 60.29726  ?  35  ALA B CA  1 
ATOM   2197 C C   . ALA B 1 27  ? 34.61400  22.14000  -11.40100 1.000 65.68801  ?  35  ALA B C   1 
ATOM   2198 O O   . ALA B 1 27  ? 34.94100  22.89200  -12.32500 1.000 64.36159  ?  35  ALA B O   1 
ATOM   2199 C CB  . ALA B 1 27  ? 32.36500  21.13400  -11.84300 1.000 53.65332  ?  35  ALA B CB  1 
ATOM   2200 N N   . SER B 1 28  ? 34.90000  22.41300  -10.13000 1.000 61.35663  ?  36  SER B N   1 
ATOM   2201 C CA  . SER B 1 28  ? 35.62400  23.61600  -9.74300  1.000 63.08436  ?  36  SER B CA  1 
ATOM   2202 C C   . SER B 1 28  ? 37.13400  23.46200  -9.86300  1.000 59.97924  ?  36  SER B C   1 
ATOM   2203 O O   . SER B 1 28  ? 37.86800  24.25200  -9.26000  1.000 64.40544  ?  36  SER B O   1 
ATOM   2204 C CB  . SER B 1 28  ? 35.25800  24.01800  -8.31200  1.000 58.82974  ?  36  SER B CB  1 
ATOM   2205 O OG  . SER B 1 28  ? 35.84500  23.14300  -7.36700  1.000 56.92665  ?  36  SER B OG  1 
ATOM   2206 N N   . GLU B 1 29  ? 37.60200  22.46900  -10.62100 1.000 60.77677  ?  37  GLU B N   1 
ATOM   2207 C CA  . GLU B 1 29  ? 39.03100  22.22000  -10.82100 1.000 66.72381  ?  37  GLU B CA  1 
ATOM   2208 C C   . GLU B 1 29  ? 39.75200  21.99600  -9.49500  1.000 64.18903  ?  37  GLU B C   1 
ATOM   2209 O O   . GLU B 1 29  ? 40.87200  22.46800  -9.28900  1.000 65.98144  ?  37  GLU B O   1 
ATOM   2210 C CB  . GLU B 1 29  ? 39.68600  23.35300  -11.61500 1.000 71.44709  ?  37  GLU B CB  1 
ATOM   2211 C CG  . GLU B 1 29  ? 39.24700  23.42600  -13.06800 1.000 73.09975  ?  37  GLU B CG  1 
ATOM   2212 C CD  . GLU B 1 29  ? 39.98800  24.49300  -13.84800 1.000 85.56141  ?  37  GLU B CD  1 
ATOM   2213 O OE1 . GLU B 1 29  ? 41.19800  24.31600  -14.10100 1.000 89.97396  ?  37  GLU B OE1 1 
ATOM   2214 O OE2 . GLU B 1 29  ? 39.36000  25.50800  -14.21200 1.000 87.14514  -1 37  GLU B OE2 1 
ATOM   2215 N N   . ALA B 1 30  ? 39.10300  21.27600  -8.58400  1.000 61.21425  ?  38  ALA B N   1 
ATOM   2216 C CA  . ALA B 1 30  ? 39.74600  20.91100  -7.33000  1.000 56.04813  ?  38  ALA B CA  1 
ATOM   2217 C C   . ALA B 1 30  ? 40.85700  19.90000  -7.58300  1.000 55.25214  ?  38  ALA B C   1 
ATOM   2218 O O   . ALA B 1 30  ? 40.75100  19.04300  -8.46400  1.000 48.20533  ?  38  ALA B O   1 
ATOM   2219 C CB  . ALA B 1 30  ? 38.72000  20.33900  -6.35400  1.000 46.92622  ?  38  ALA B CB  1 
ATOM   2220 N N   . ASP B 1 31  ? 41.93000  20.00300  -6.80400  1.000 52.27845  ?  39  ASP B N   1 
ATOM   2221 C CA  . ASP B 1 31  ? 43.06300  19.11200  -6.99000  1.000 48.32575  ?  39  ASP B CA  1 
ATOM   2222 C C   . ASP B 1 31  ? 42.75300  17.72100  -6.44100  1.000 47.83254  ?  39  ASP B C   1 
ATOM   2223 O O   . ASP B 1 31  ? 41.69800  17.47200  -5.85300  1.000 47.52801  ?  39  ASP B O   1 
ATOM   2224 C CB  . ASP B 1 31  ? 44.31800  19.68300  -6.32600  1.000 54.14409  ?  39  ASP B CB  1 
ATOM   2225 C CG  . ASP B 1 31  ? 44.15700  19.88100  -4.83400  1.000 53.57778  ?  39  ASP B CG  1 
ATOM   2226 O OD1 . ASP B 1 31  ? 44.41700  18.92800  -4.07300  1.000 49.27198  ?  39  ASP B OD1 1 
ATOM   2227 O OD2 . ASP B 1 31  ? 43.78100  20.99600  -4.42300  1.000 56.82255  -1 39  ASP B OD2 1 
ATOM   2228 N N   . ALA B 1 32  ? 43.69800  16.80400  -6.65600  1.000 48.95423  ?  40  ALA B N   1 
ATOM   2229 C CA  . ALA B 1 32  ? 43.48400  15.41200  -6.27700  1.000 46.81451  ?  40  ALA B CA  1 
ATOM   2230 C C   . ALA B 1 32  ? 43.34600  15.25400  -4.76800  1.000 53.88362  ?  40  ALA B C   1 
ATOM   2231 O O   . ALA B 1 32  ? 42.51600  14.47200  -4.29500  1.000 47.81038  ?  40  ALA B O   1 
ATOM   2232 C CB  . ALA B 1 32  ? 44.62600  14.54400  -6.80400  1.000 39.28327  ?  40  ALA B CB  1 
ATOM   2233 N N   . GLY B 1 33  ? 44.15700  15.97900  -3.99600  1.000 50.45272  ?  41  GLY B N   1 
ATOM   2234 C CA  . GLY B 1 33  ? 44.11400  15.82500  -2.55000  1.000 42.33080  ?  41  GLY B CA  1 
ATOM   2235 C C   . GLY B 1 33  ? 42.80700  16.29000  -1.93700  1.000 44.77034  ?  41  GLY B C   1 
ATOM   2236 O O   . GLY B 1 33  ? 42.23900  15.60900  -1.08000  1.000 36.43550  ?  41  GLY B O   1 
ATOM   2237 N N   . THR B 1 34  ? 42.31500  17.45700  -2.36000  1.000 47.82964  ?  42  THR B N   1 
ATOM   2238 C CA  . THR B 1 34  ? 41.04800  17.96100  -1.83900  1.000 51.23163  ?  42  THR B CA  1 
ATOM   2239 C C   . THR B 1 34  ? 39.89600  17.03700  -2.20500  1.000 47.14778  ?  42  THR B C   1 
ATOM   2240 O O   . THR B 1 34  ? 39.02400  16.75200  -1.37200  1.000 49.76736  ?  42  THR B O   1 
ATOM   2241 C CB  . THR B 1 34  ? 40.79000  19.37000  -2.37000  1.000 42.32937  ?  42  THR B CB  1 
ATOM   2242 O OG1 . THR B 1 34  ? 42.03500  20.06700  -2.49200  1.000 42.43526  ?  42  THR B OG1 1 
ATOM   2243 C CG2 . THR B 1 34  ? 39.87700  20.13600  -1.43100  1.000 34.45532  ?  42  THR B CG2 1 
ATOM   2244 N N   . LEU B 1 35  ? 39.87800  16.55800  -3.45000  1.000 40.50284  ?  43  LEU B N   1 
ATOM   2245 C CA  . LEU B 1 35  ? 38.83700  15.63300  -3.87600  1.000 45.28670  ?  43  LEU B CA  1 
ATOM   2246 C C   . LEU B 1 35  ? 38.90100  14.33100  -3.08900  1.000 42.20602  ?  43  LEU B C   1 
ATOM   2247 O O   . LEU B 1 35  ? 37.86500  13.79700  -2.68400  1.000 41.49472  ?  43  LEU B O   1 
ATOM   2248 C CB  . LEU B 1 35  ? 38.96100  15.36700  -5.37400  1.000 53.44992  ?  43  LEU B CB  1 
ATOM   2249 C CG  . LEU B 1 35  ? 38.19500  16.30200  -6.31000  1.000 48.51742  ?  43  LEU B CG  1 
ATOM   2250 C CD1 . LEU B 1 35  ? 38.62700  16.08400  -7.74500  1.000 50.33044  ?  43  LEU B CD1 1 
ATOM   2251 C CD2 . LEU B 1 35  ? 36.70000  16.09500  -6.16900  1.000 46.34244  ?  43  LEU B CD2 1 
ATOM   2252 N N   . ASP B 1 36  ? 40.10800  13.80900  -2.85800  1.000 48.27555  ?  44  ASP B N   1 
ATOM   2253 C CA  . ASP B 1 36  ? 40.24700  12.57900  -2.08500  1.000 50.60845  ?  44  ASP B CA  1 
ATOM   2254 C C   . ASP B 1 36  ? 39.78900  12.77700  -0.64700  1.000 41.17686  ?  44  ASP B C   1 
ATOM   2255 O O   . ASP B 1 36  ? 39.15000  11.89500  -0.06700  1.000 44.65482  ?  44  ASP B O   1 
ATOM   2256 C CB  . ASP B 1 36  ? 41.69600  12.09100  -2.11700  1.000 51.17140  ?  44  ASP B CB  1 
ATOM   2257 C CG  . ASP B 1 36  ? 42.11500  11.59600  -3.48200  1.000 54.64272  ?  44  ASP B CG  1 
ATOM   2258 O OD1 . ASP B 1 36  ? 41.29500  11.66600  -4.41800  1.000 63.11312  ?  44  ASP B OD1 1 
ATOM   2259 O OD2 . ASP B 1 36  ? 43.26400  11.13000  -3.61800  1.000 54.46266  -1 44  ASP B OD2 1 
ATOM   2260 N N   . ALA B 1 37  ? 40.12200  13.92200  -0.04900  1.000 35.36895  ?  45  ALA B N   1 
ATOM   2261 C CA  . ALA B 1 37  ? 39.67900  14.19500  1.31300   1.000 38.93912  ?  45  ALA B CA  1 
ATOM   2262 C C   . ALA B 1 37  ? 38.16100  14.27600  1.39200   1.000 42.25502  ?  45  ALA B C   1 
ATOM   2263 O O   . ALA B 1 37  ? 37.55000  13.72900  2.31900   1.000 44.97774  ?  45  ALA B O   1 
ATOM   2264 C CB  . ALA B 1 37  ? 40.31600  15.48600  1.82300   1.000 41.16426  ?  45  ALA B CB  1 
ATOM   2265 N N   . ALA B 1 38  ? 37.53500  14.95200  0.42500   1.000 46.80552  ?  46  ALA B N   1 
ATOM   2266 C CA  . ALA B 1 38  ? 36.07800  15.02200  0.40100   1.000 41.89260  ?  46  ALA B CA  1 
ATOM   2267 C C   . ALA B 1 38  ? 35.46200  13.64200  0.21100   1.000 43.92841  ?  46  ALA B C   1 
ATOM   2268 O O   . ALA B 1 38  ? 34.46200  13.30400  0.85700   1.000 43.39380  ?  46  ALA B O   1 
ATOM   2269 C CB  . ALA B 1 38  ? 35.61500  15.97200  -0.70100  1.000 38.23680  ?  46  ALA B CB  1 
ATOM   2270 N N   . LEU B 1 39  ? 36.04900  12.82900  -0.67000  1.000 40.87687  ?  47  LEU B N   1 
ATOM   2271 C CA  . LEU B 1 39  ? 35.54500  11.48000  -0.89700  1.000 39.16538  ?  47  LEU B CA  1 
ATOM   2272 C C   . LEU B 1 39  ? 35.64400  10.64300  0.37000   1.000 44.38869  ?  47  LEU B C   1 
ATOM   2273 O O   . LEU B 1 39  ? 34.71600  9.90600   0.71400   1.000 43.72279  ?  47  LEU B O   1 
ATOM   2274 C CB  . LEU B 1 39  ? 36.32200  10.81500  -2.03300  1.000 45.54718  ?  47  LEU B CB  1 
ATOM   2275 C CG  . LEU B 1 39  ? 36.12600  11.30600  -3.46700  1.000 44.61324  ?  47  LEU B CG  1 
ATOM   2276 C CD1 . LEU B 1 39  ? 37.23800  10.78000  -4.35500  1.000 51.20925  ?  47  LEU B CD1 1 
ATOM   2277 C CD2 . LEU B 1 39  ? 34.78500  10.88900  -4.00400  1.000 43.58248  ?  47  LEU B CD2 1 
ATOM   2278 N N   . THR B 1 40  ? 36.77300  10.73900  1.07300   1.000 43.85729  ?  48  THR B N   1 
ATOM   2279 C CA  . THR B 1 40  ? 36.95800  9.97100   2.30000   1.000 44.48525  ?  48  THR B CA  1 
ATOM   2280 C C   . THR B 1 40  ? 35.98200  10.41400  3.38200   1.000 42.22335  ?  48  THR B C   1 
ATOM   2281 O O   . THR B 1 40  ? 35.40200  9.57900   4.08600   1.000 38.21165  ?  48  THR B O   1 
ATOM   2282 C CB  . THR B 1 40  ? 38.40300  10.10200  2.78300   1.000 38.29899  ?  48  THR B CB  1 
ATOM   2283 O OG1 . THR B 1 40  ? 39.27900  9.46500   1.84600   1.000 40.66112  ?  48  THR B OG1 1 
ATOM   2284 C CG2 . THR B 1 40  ? 38.57500  9.45000   4.14000   1.000 44.42026  ?  48  THR B CG2 1 
ATOM   2285 N N   . GLN B 1 41  ? 35.78400  11.72600  3.52500   1.000 44.83766  ?  49  GLN B N   1 
ATOM   2286 C CA  . GLN B 1 41  ? 34.82100  12.22800  4.50000   1.000 49.48202  ?  49  GLN B CA  1 
ATOM   2287 C C   . GLN B 1 41  ? 33.41400  11.73500  4.18500   1.000 47.91590  ?  49  GLN B C   1 
ATOM   2288 O O   . GLN B 1 41  ? 32.68400  11.28200  5.07600   1.000 48.63302  ?  49  GLN B O   1 
ATOM   2289 C CB  . GLN B 1 41  ? 34.86400  13.75500  4.52600   1.000 49.93930  ?  49  GLN B CB  1 
ATOM   2290 C CG  . GLN B 1 41  ? 34.51700  14.37100  5.86400   1.000 62.77827  ?  49  GLN B CG  1 
ATOM   2291 C CD  . GLN B 1 41  ? 34.51000  15.88300  5.81300   1.000 81.21543  ?  49  GLN B CD  1 
ATOM   2292 O OE1 . GLN B 1 41  ? 35.42600  16.53800  6.30900   1.000 81.42952  ?  49  GLN B OE1 1 
ATOM   2293 N NE2 . GLN B 1 41  ? 33.47400  16.44800  5.20400   1.000 75.57052  ?  49  GLN B NE2 1 
ATOM   2294 N N   . SER B 1 42  ? 33.02000  11.80600  2.91000   1.000 41.59350  ?  50  SER B N   1 
ATOM   2295 C CA  . SER B 1 42  ? 31.69700  11.33800  2.51600   1.000 45.53862  ?  50  SER B CA  1 
ATOM   2296 C C   . SER B 1 42  ? 31.54700  9.84000   2.74800   1.000 42.40081  ?  50  SER B C   1 
ATOM   2297 O O   . SER B 1 42  ? 30.49600  9.37800   3.20500   1.000 39.85363  ?  50  SER B O   1 
ATOM   2298 C CB  . SER B 1 42  ? 31.43700  11.68500  1.05100   1.000 50.19341  ?  50  SER B CB  1 
ATOM   2299 O OG  . SER B 1 42  ? 31.41200  13.08800  0.86100   1.000 48.50316  ?  50  SER B OG  1 
ATOM   2300 N N   . LEU B 1 43  ? 32.58800  9.06600   2.43600   1.000 37.98293  ?  51  LEU B N   1 
ATOM   2301 C CA  . LEU B 1 43  ? 32.52400  7.62300   2.63300   1.000 37.35241  ?  51  LEU B CA  1 
ATOM   2302 C C   . LEU B 1 43  ? 32.39700  7.27400   4.10700   1.000 37.39395  ?  51  LEU B C   1 
ATOM   2303 O O   . LEU B 1 43  ? 31.64300  6.36800   4.47200   1.000 38.78849  ?  51  LEU B O   1 
ATOM   2304 C CB  . LEU B 1 43  ? 33.75700  6.95200   2.03100   1.000 36.19454  ?  51  LEU B CB  1 
ATOM   2305 C CG  . LEU B 1 43  ? 33.84200  5.44200   2.25600   1.000 41.10243  ?  51  LEU B CG  1 
ATOM   2306 C CD1 . LEU B 1 43  ? 32.70500  4.73400   1.54200   1.000 40.57255  ?  51  LEU B CD1 1 
ATOM   2307 C CD2 . LEU B 1 43  ? 35.18100  4.90300   1.80300   1.000 41.47447  ?  51  LEU B CD2 1 
ATOM   2308 N N   . GLN B 1 44  ? 33.13500  7.97300   4.97000   1.000 35.43795  ?  52  GLN B N   1 
ATOM   2309 C CA  . GLN B 1 44  ? 33.02600  7.72400   6.40400   1.000 36.79607  ?  52  GLN B CA  1 
ATOM   2310 C C   . GLN B 1 44  ? 31.63800  8.08600   6.92000   1.000 38.80480  ?  52  GLN B C   1 
ATOM   2311 O O   . GLN B 1 44  ? 31.04800  7.34700   7.72200   1.000 38.73401  ?  52  GLN B O   1 
ATOM   2312 C CB  . GLN B 1 44  ? 34.10600  8.50600   7.14700   1.000 40.77317  ?  52  GLN B CB  1 
ATOM   2313 C CG  . GLN B 1 44  ? 35.51500  8.00500   6.87500   1.000 40.35175  ?  52  GLN B CG  1 
ATOM   2314 C CD  . GLN B 1 44  ? 36.58200  8.93800   7.40500   1.000 39.88036  ?  52  GLN B CD  1 
ATOM   2315 O OE1 . GLN B 1 44  ? 36.30300  10.08300  7.75600   1.000 39.26977  ?  52  GLN B OE1 1 
ATOM   2316 N NE2 . GLN B 1 44  ? 37.81500  8.45600   7.45300   1.000 34.20550  ?  52  GLN B NE2 1 
ATOM   2317 N N   . GLU B 1 45  ? 31.09100  9.21100   6.45200   1.000 41.07995  ?  53  GLU B N   1 
ATOM   2318 C CA  . GLU B 1 45  ? 29.74200  9.59800   6.85200   1.000 37.87036  ?  53  GLU B CA  1 
ATOM   2319 C C   . GLU B 1 45  ? 28.71800  8.56200   6.40900   1.000 38.99835  ?  53  GLU B C   1 
ATOM   2320 O O   . GLU B 1 45  ? 27.78600  8.23800   7.15400   1.000 41.55710  ?  53  GLU B O   1 
ATOM   2321 C CB  . GLU B 1 45  ? 29.39900  10.96900  6.27200   1.000 44.28156  ?  53  GLU B CB  1 
ATOM   2322 C CG  . GLU B 1 45  ? 28.52900  11.82600  7.17100   1.000 59.31468  ?  53  GLU B CG  1 
ATOM   2323 C CD  . GLU B 1 45  ? 29.34300  12.72800  8.07200   1.000 72.99652  ?  53  GLU B CD  1 
ATOM   2324 O OE1 . GLU B 1 45  ? 30.10300  13.56600  7.54500   1.000 68.35788  ?  53  GLU B OE1 1 
ATOM   2325 O OE2 . GLU B 1 45  ? 29.22000  12.60200  9.30800   1.000 74.79539  -1 53  GLU B OE2 1 
ATOM   2326 N N   . ALA B 1 46  ? 28.87200  8.03500   5.19300   1.000 43.24860  ?  54  ALA B N   1 
ATOM   2327 C CA  . ALA B 1 46  ? 27.93200  7.03900   4.68900   1.000 38.83845  ?  54  ALA B CA  1 
ATOM   2328 C C   . ALA B 1 46  ? 28.09200  5.70600   5.40800   1.000 38.42381  ?  54  ALA B C   1 
ATOM   2329 O O   . ALA B 1 46  ? 27.11300  4.98100   5.60800   1.000 39.33052  ?  54  ALA B O   1 
ATOM   2330 C CB  . ALA B 1 46  ? 28.11400  6.86100   3.18400   1.000 41.80261  ?  54  ALA B CB  1 
ATOM   2331 N N   . GLN B 1 47  ? 29.32400  5.35500   5.77900   1.000 41.48318  ?  55  GLN B N   1 
ATOM   2332 C CA  . GLN B 1 47  ? 29.55000  4.13800   6.55100   1.000 35.39906  ?  55  GLN B CA  1 
ATOM   2333 C C   . GLN B 1 47  ? 28.90100  4.23700   7.92100   1.000 33.03080  ?  55  GLN B C   1 
ATOM   2334 O O   . GLN B 1 47  ? 28.38800  3.24400   8.44800   1.000 35.54495  ?  55  GLN B O   1 
ATOM   2335 C CB  . GLN B 1 47  ? 31.04700  3.87000   6.68900   1.000 30.86953  ?  55  GLN B CB  1 
ATOM   2336 C CG  . GLN B 1 47  ? 31.66800  3.14800   5.51300   1.000 33.84680  ?  55  GLN B CG  1 
ATOM   2337 C CD  . GLN B 1 47  ? 31.20400  1.71200   5.40500   1.000 43.03071  ?  55  GLN B CD  1 
ATOM   2338 O OE1 . GLN B 1 47  ? 30.88100  1.07400   6.40500   1.000 45.79466  ?  55  GLN B OE1 1 
ATOM   2339 N NE2 . GLN B 1 47  ? 31.17800  1.19000   4.18700   1.000 52.40318  ?  55  GLN B NE2 1 
ATOM   2340 N N   . GLY B 1 48  ? 28.92300  5.42700   8.51800   1.000 39.00902  ?  56  GLY B N   1 
ATOM   2341 C CA  . GLY B 1 48  ? 28.23600  5.62000   9.78000   1.000 35.59456  ?  56  GLY B CA  1 
ATOM   2342 C C   . GLY B 1 48  ? 26.73500  5.42000   9.71700   1.000 36.51373  ?  56  GLY B C   1 
ATOM   2343 O O   . GLY B 1 48  ? 26.11100  5.22500   10.76500  1.000 36.00350  ?  56  GLY B O   1 
ATOM   2344 N N   . ARG B 1 49  ? 26.14600  5.44800   8.52200   1.000 38.11111  ?  57  ARG B N   1 
ATOM   2345 C CA  . ARG B 1 49  ? 24.70200  5.35600   8.36200   1.000 37.79913  ?  57  ARG B CA  1 
ATOM   2346 C C   . ARG B 1 49  ? 24.23400  4.07900   7.68500   1.000 40.84836  ?  57  ARG B C   1 
ATOM   2347 O O   . ARG B 1 49  ? 23.06900  3.71000   7.83500   1.000 40.77645  ?  57  ARG B O   1 
ATOM   2348 C CB  . ARG B 1 49  ? 24.18700  6.56000   7.56500   1.000 34.64938  ?  57  ARG B CB  1 
ATOM   2349 C CG  . ARG B 1 49  ? 24.46100  7.88700   8.24500   1.000 40.56566  ?  57  ARG B CG  1 
ATOM   2350 C CD  . ARG B 1 49  ? 24.07800  9.06200   7.37300   1.000 39.14384  ?  57  ARG B CD  1 
ATOM   2351 N NE  . ARG B 1 49  ? 24.59000  10.31700  7.91000   1.000 48.65843  ?  57  ARG B NE  1 
ATOM   2352 C CZ  . ARG B 1 49  ? 24.41100  11.50200  7.34400   1.000 52.53479  ?  57  ARG B CZ  1 
ATOM   2353 N NH1 . ARG B 1 49  ? 23.73300  11.63300  6.21600   1.000 51.85986  ?  57  ARG B NH1 1 
ATOM   2354 N NH2 . ARG B 1 49  ? 24.92500  12.58200  7.92300   1.000 51.33718  ?  57  ARG B NH2 1 
ATOM   2355 N N   . TRP B 1 50  ? 25.10800  3.39500   6.94500   1.000 43.93058  ?  58  TRP B N   1 
ATOM   2356 C CA  . TRP B 1 50  ? 24.71400  2.17700   6.24700   1.000 40.42909  ?  58  TRP B CA  1 
ATOM   2357 C C   . TRP B 1 50  ? 24.46900  1.01100   7.19400   1.000 43.74303  ?  58  TRP B C   1 
ATOM   2358 O O   . TRP B 1 50  ? 23.79300  0.05100   6.81000   1.000 45.15092  ?  58  TRP B O   1 
ATOM   2359 C CB  . TRP B 1 50  ? 25.77800  1.78600   5.22200   1.000 39.99316  ?  58  TRP B CB  1 
ATOM   2360 C CG  . TRP B 1 50  ? 25.71700  2.57400   3.95600   1.000 40.97419  ?  58  TRP B CG  1 
ATOM   2361 C CD1 . TRP B 1 50  ? 24.61300  3.15000   3.40100   1.000 43.37960  ?  58  TRP B CD1 1 
ATOM   2362 C CD2 . TRP B 1 50  ? 26.80600  2.86200   3.07500   1.000 47.30667  ?  58  TRP B CD2 1 
ATOM   2363 N NE1 . TRP B 1 50  ? 24.94900  3.78500   2.23200   1.000 42.47417  ?  58  TRP B NE1 1 
ATOM   2364 C CE2 . TRP B 1 50  ? 26.29000  3.62300   2.00900   1.000 43.94322  ?  58  TRP B CE2 1 
ATOM   2365 C CE3 . TRP B 1 50  ? 28.16900  2.55400   3.08600   1.000 42.01655  ?  58  TRP B CE3 1 
ATOM   2366 C CZ2 . TRP B 1 50  ? 27.08800  4.07800   0.96600   1.000 40.74529  ?  58  TRP B CZ2 1 
ATOM   2367 C CZ3 . TRP B 1 50  ? 28.95700  3.00600   2.05000   1.000 39.29370  ?  58  TRP B CZ3 1 
ATOM   2368 C CH2 . TRP B 1 50  ? 28.41600  3.76000   1.00400   1.000 45.30284  ?  58  TRP B CH2 1 
ATOM   2369 N N   . GLY B 1 51  ? 25.00100  1.06700   8.40800   1.000 41.82804  ?  59  GLY B N   1 
ATOM   2370 C CA  . GLY B 1 51  ? 24.82900  -0.01900  9.35600   1.000 38.68582  ?  59  GLY B CA  1 
ATOM   2371 C C   . GLY B 1 51  ? 25.51400  -1.30800  8.96100   1.000 39.73875  ?  59  GLY B C   1 
ATOM   2372 O O   . GLY B 1 51  ? 24.98800  -2.39400  9.23500   1.000 43.93459  ?  59  GLY B O   1 
ATOM   2373 N N   . LEU B 1 52  ? 26.67700  -1.21800  8.32300   1.000 41.50954  ?  60  LEU B N   1 
ATOM   2374 C CA  . LEU B 1 52  ? 27.45000  -2.39800  7.96800   1.000 41.37298  ?  60  LEU B CA  1 
ATOM   2375 C C   . LEU B 1 52  ? 28.30200  -2.91500  9.11700   1.000 46.61117  ?  60  LEU B C   1 
ATOM   2376 O O   . LEU B 1 52  ? 28.80300  -4.04100  9.03800   1.000 43.32455  ?  60  LEU B O   1 
ATOM   2377 C CB  . LEU B 1 52  ? 28.34800  -2.09900  6.76400   1.000 42.74040  ?  60  LEU B CB  1 
ATOM   2378 C CG  . LEU B 1 52  ? 27.63500  -1.64100  5.49200   1.000 42.67544  ?  60  LEU B CG  1 
ATOM   2379 C CD1 . LEU B 1 52  ? 28.64100  -1.28300  4.41800   1.000 41.78944  ?  60  LEU B CD1 1 
ATOM   2380 C CD2 . LEU B 1 52  ? 26.68300  -2.71200  4.99900   1.000 32.70262  ?  60  LEU B CD2 1 
ATOM   2381 N N   . GLY B 1 53  ? 28.46800  -2.12900  10.17700  1.000 54.90332  ?  61  GLY B N   1 
ATOM   2382 C CA  . GLY B 1 53  ? 29.26200  -2.55000  11.31400  1.000 41.73542  ?  61  GLY B CA  1 
ATOM   2383 C C   . GLY B 1 53  ? 30.73800  -2.70800  11.03900  1.000 38.61807  ?  61  GLY B C   1 
ATOM   2384 O O   . GLY B 1 53  ? 31.35000  -3.66900  11.51200  1.000 45.81493  ?  61  GLY B O   1 
ATOM   2385 N N   . LEU B 1 54  ? 31.33200  -1.78600  10.28900  1.000 37.05679  ?  62  LEU B N   1 
ATOM   2386 C CA  . LEU B 1 54  ? 32.75300  -1.81500  9.96800   1.000 38.75248  ?  62  LEU B CA  1 
ATOM   2387 C C   . LEU B 1 54  ? 33.48500  -0.64000  10.60700  1.000 39.54399  ?  62  LEU B C   1 
ATOM   2388 O O   . LEU B 1 54  ? 34.42100  -0.08300  10.03400  1.000 42.25720  ?  62  LEU B O   1 
ATOM   2389 C CB  . LEU B 1 54  ? 32.96200  -1.82600  8.45700   1.000 43.49769  ?  62  LEU B CB  1 
ATOM   2390 C CG  . LEU B 1 54  ? 32.22500  -2.93900  7.71100   1.000 38.39116  ?  62  LEU B CG  1 
ATOM   2391 C CD1 . LEU B 1 54  ? 32.43800  -2.82200  6.21600   1.000 35.93772  ?  62  LEU B CD1 1 
ATOM   2392 C CD2 . LEU B 1 54  ? 32.66600  -4.30000  8.20900   1.000 38.47179  ?  62  LEU B CD2 1 
ATOM   2393 N N   . HIS B 1 55  ? 33.05700  -0.25200  11.81000  1.000 40.80574  ?  63  HIS B N   1 
ATOM   2394 C CA  . HIS B 1 55  ? 33.67800  0.87400   12.49900  1.000 39.71009  ?  63  HIS B CA  1 
ATOM   2395 C C   . HIS B 1 55  ? 35.12300  0.58100   12.88000  1.000 34.63416  ?  63  HIS B C   1 
ATOM   2396 O O   . HIS B 1 55  ? 35.90200  1.51300   13.10900  1.000 40.74039  ?  63  HIS B O   1 
ATOM   2397 C CB  . HIS B 1 55  ? 32.87100  1.23500   13.74400  1.000 39.12228  ?  63  HIS B CB  1 
ATOM   2398 C CG  . HIS B 1 55  ? 31.44600  1.59300   13.45900  1.000 38.38056  ?  63  HIS B CG  1 
ATOM   2399 N ND1 . HIS B 1 55  ? 31.09000  2.69500   12.71400  1.000 40.55756  ?  63  HIS B ND1 1 
ATOM   2400 C CD2 . HIS B 1 55  ? 30.28800  0.99400   13.82100  1.000 29.90259  ?  63  HIS B CD2 1 
ATOM   2401 C CE1 . HIS B 1 55  ? 29.77400  2.76100   12.63000  1.000 39.33097  ?  63  HIS B CE1 1 
ATOM   2402 N NE2 . HIS B 1 55  ? 29.26300  1.74000   13.29300  1.000 32.50192  ?  63  HIS B NE2 1 
ATOM   2403 N N   . HIS B 1 56  ? 35.49800  -0.69300  12.95600  1.000 32.62438  ?  64  HIS B N   1 
ATOM   2404 C CA  . HIS B 1 56  ? 36.86300  -1.07000  13.29400  1.000 36.73029  ?  64  HIS B CA  1 
ATOM   2405 C C   . HIS B 1 56  ? 37.84400  -0.83200  12.15500  1.000 35.43321  ?  64  HIS B C   1 
ATOM   2406 O O   . HIS B 1 56  ? 39.05300  -0.96500  12.36500  1.000 33.91532  ?  64  HIS B O   1 
ATOM   2407 C CB  . HIS B 1 56  ? 36.91200  -2.54000  13.71400  1.000 38.13627  ?  64  HIS B CB  1 
ATOM   2408 C CG  . HIS B 1 56  ? 36.37300  -3.48200  12.68300  1.000 43.92818  ?  64  HIS B CG  1 
ATOM   2409 N ND1 . HIS B 1 56  ? 35.02700  -3.60400  12.41800  1.000 42.71910  ?  64  HIS B ND1 1 
ATOM   2410 C CD2 . HIS B 1 56  ? 37.00000  -4.35100  11.85700  1.000 39.55393  ?  64  HIS B CD2 1 
ATOM   2411 C CE1 . HIS B 1 56  ? 34.84800  -4.50400  11.46800  1.000 48.74657  ?  64  HIS B CE1 1 
ATOM   2412 N NE2 . HIS B 1 56  ? 36.02900  -4.97200  11.11000  1.000 48.88282  ?  64  HIS B NE2 1 
ATOM   2413 N N   . LEU B 1 57  ? 37.35800  -0.48400  10.96900  1.000 40.02080  ?  65  LEU B N   1 
ATOM   2414 C CA  . LEU B 1 57  ? 38.19400  -0.30900  9.79400   1.000 35.43997  ?  65  LEU B CA  1 
ATOM   2415 C C   . LEU B 1 57  ? 38.21400  1.15500   9.37600   1.000 38.14326  ?  65  LEU B C   1 
ATOM   2416 O O   . LEU B 1 57  ? 37.25700  1.89800   9.60500   1.000 40.29386  ?  65  LEU B O   1 
ATOM   2417 C CB  . LEU B 1 57  ? 37.68100  -1.16600  8.63700   1.000 40.83075  ?  65  LEU B CB  1 
ATOM   2418 C CG  . LEU B 1 57  ? 37.62000  -2.67400  8.87900   1.000 36.31249  ?  65  LEU B CG  1 
ATOM   2419 C CD1 . LEU B 1 57  ? 36.87500  -3.36000  7.75500   1.000 30.22951  ?  65  LEU B CD1 1 
ATOM   2420 C CD2 . LEU B 1 57  ? 39.00200  -3.26300  9.04000   1.000 40.51704  ?  65  LEU B CD2 1 
ATOM   2421 N N   . ARG B 1 58  ? 39.31700  1.56400   8.75800   1.000 39.49282  ?  66  ARG B N   1 
ATOM   2422 C CA  . ARG B 1 58  ? 39.45100  2.91700   8.23900   1.000 40.07529  ?  66  ARG B CA  1 
ATOM   2423 C C   . ARG B 1 58  ? 39.04000  2.94400   6.77400   1.000 42.12464  ?  66  ARG B C   1 
ATOM   2424 O O   . ARG B 1 58  ? 39.69800  2.33900   5.92600   1.000 47.99526  ?  66  ARG B O   1 
ATOM   2425 C CB  . ARG B 1 58  ? 40.88600  3.41900   8.39700   1.000 46.57684  ?  66  ARG B CB  1 
ATOM   2426 C CG  . ARG B 1 58  ? 41.04700  4.91400   8.19200   1.000 40.89596  ?  66  ARG B CG  1 
ATOM   2427 C CD  . ARG B 1 58  ? 42.35500  5.41200   8.78000   1.000 48.58683  ?  66  ARG B CD  1 
ATOM   2428 N NE  . ARG B 1 58  ? 42.14500  6.50800   9.71800   1.000 60.76191  ?  66  ARG B NE  1 
ATOM   2429 C CZ  . ARG B 1 58  ? 42.32400  6.41800   11.02900  1.000 63.74736  ?  66  ARG B CZ  1 
ATOM   2430 N NH1 . ARG B 1 58  ? 42.71400  5.28900   11.59700  1.000 65.53638  ?  66  ARG B NH1 1 
ATOM   2431 N NH2 . ARG B 1 58  ? 42.10500  7.48700   11.78900  1.000 38.13744  ?  66  ARG B NH2 1 
ATOM   2432 N N   . HIS B 1 59  ? 37.96100  3.65800   6.47900   1.000 42.52827  ?  67  HIS B N   1 
ATOM   2433 C CA  . HIS B 1 59  ? 37.39000  3.70100   5.14100   1.000 43.56118  ?  67  HIS B CA  1 
ATOM   2434 C C   . HIS B 1 59  ? 37.86200  4.95700   4.42900   1.000 43.73388  ?  67  HIS B C   1 
ATOM   2435 O O   . HIS B 1 59  ? 37.68200  6.06800   4.93700   1.000 42.94984  ?  67  HIS B O   1 
ATOM   2436 C CB  . HIS B 1 59  ? 35.86300  3.65900   5.20300   1.000 42.27682  ?  67  HIS B CB  1 
ATOM   2437 C CG  . HIS B 1 59  ? 35.32400  2.47800   5.94600   1.000 34.67474  ?  67  HIS B CG  1 
ATOM   2438 N ND1 . HIS B 1 59  ? 35.24400  1.22200   5.38700   1.000 41.53299  ?  67  HIS B ND1 1 
ATOM   2439 C CD2 . HIS B 1 59  ? 34.84100  2.36100   7.20400   1.000 26.47264  ?  67  HIS B CD2 1 
ATOM   2440 C CE1 . HIS B 1 59  ? 34.73300  0.38200   6.26800   1.000 40.08488  ?  67  HIS B CE1 1 
ATOM   2441 N NE2 . HIS B 1 59  ? 34.47900  1.04800   7.37900   1.000 34.35359  ?  67  HIS B NE2 1 
ATOM   2442 N N   . GLU B 1 60  ? 38.46500  4.77900   3.25600   1.000 49.67701  ?  68  GLU B N   1 
ATOM   2443 C CA  . GLU B 1 60  ? 39.01600  5.88900   2.49500   1.000 51.67006  ?  68  GLU B CA  1 
ATOM   2444 C C   . GLU B 1 60  ? 38.61800  5.75200   1.03400   1.000 46.48174  ?  68  GLU B C   1 
ATOM   2445 O O   . GLU B 1 60  ? 38.28900  4.66200   0.56500   1.000 41.89826  ?  68  GLU B O   1 
ATOM   2446 C CB  . GLU B 1 60  ? 40.54400  5.95600   2.62700   1.000 42.47214  ?  68  GLU B CB  1 
ATOM   2447 C CG  . GLU B 1 60  ? 41.02800  6.22200   4.04300   1.000 41.34948  ?  68  GLU B CG  1 
ATOM   2448 C CD  . GLU B 1 60  ? 42.52900  6.10800   4.18400   1.000 49.67779  ?  68  GLU B CD  1 
ATOM   2449 O OE1 . GLU B 1 60  ? 43.16700  5.50100   3.30100   1.000 63.30036  ?  68  GLU B OE1 1 
ATOM   2450 O OE2 . GLU B 1 60  ? 43.07300  6.62700   5.18000   1.000 55.52717  -1 68  GLU B OE2 1 
ATOM   2451 N N   . ALA B 1 61  ? 38.62900  6.87600   0.32400   1.000 43.17586  ?  69  ALA B N   1 
ATOM   2452 C CA  . ALA B 1 61  ? 38.34600  6.90300   -1.10400  1.000 49.92259  ?  69  ALA B CA  1 
ATOM   2453 C C   . ALA B 1 61  ? 39.33700  7.83600   -1.77800  1.000 53.84235  ?  69  ALA B C   1 
ATOM   2454 O O   . ALA B 1 61  ? 39.59800  8.93300   -1.27600  1.000 53.06504  ?  69  ALA B O   1 
ATOM   2455 C CB  . ALA B 1 61  ? 36.91000  7.35500   -1.38000  1.000 49.21537  ?  69  ALA B CB  1 
ATOM   2456 N N   . ARG B 1 62  ? 39.88600  7.40400   -2.91000  1.000 61.02699  ?  70  ARG B N   1 
ATOM   2457 C CA  . ARG B 1 62  ? 40.91700  8.18300   -3.58200  1.000 60.72037  ?  70  ARG B CA  1 
ATOM   2458 C C   . ARG B 1 62  ? 40.73700  8.11900   -5.09100  1.000 65.29958  ?  70  ARG B C   1 
ATOM   2459 O O   . ARG B 1 62  ? 40.16400  7.17400   -5.63300  1.000 64.85332  ?  70  ARG B O   1 
ATOM   2460 C CB  . ARG B 1 62  ? 42.32300  7.69900   -3.20200  1.000 57.88339  ?  70  ARG B CB  1 
ATOM   2461 C CG  . ARG B 1 62  ? 42.63700  6.28200   -3.64300  1.000 57.81752  ?  70  ARG B CG  1 
ATOM   2462 C CD  . ARG B 1 62  ? 44.12800  6.10400   -3.85800  1.000 65.35871  ?  70  ARG B CD  1 
ATOM   2463 N NE  . ARG B 1 62  ? 44.83500  5.83800   -2.61100  1.000 74.75587  ?  70  ARG B NE  1 
ATOM   2464 C CZ  . ARG B 1 62  ? 45.39800  4.67900   -2.30100  1.000 68.10900  ?  70  ARG B CZ  1 
ATOM   2465 N NH1 . ARG B 1 62  ? 45.37100  3.65300   -3.13600  1.000 64.85433  ?  70  ARG B NH1 1 
ATOM   2466 N NH2 . ARG B 1 62  ? 46.00800  4.54700   -1.12700  1.000 70.23740  ?  70  ARG B NH2 1 
ATOM   2467 N N   . LEU B 1 63  ? 41.23900  9.14400   -5.77100  1.000 55.87116  ?  71  LEU B N   1 
ATOM   2468 C CA  . LEU B 1 63  ? 41.26800  9.14400   -7.22500  1.000 56.12271  ?  71  LEU B CA  1 
ATOM   2469 C C   . LEU B 1 63  ? 42.43100  8.30100   -7.72800  1.000 63.61664  ?  71  LEU B C   1 
ATOM   2470 O O   . LEU B 1 63  ? 43.53400  8.34800   -7.17800  1.000 68.81453  ?  71  LEU B O   1 
ATOM   2471 C CB  . LEU B 1 63  ? 41.39300  10.56800  -7.76600  1.000 59.91861  ?  71  LEU B CB  1 
ATOM   2472 C CG  . LEU B 1 63  ? 40.12300  11.40800  -7.86300  1.000 63.01404  ?  71  LEU B CG  1 
ATOM   2473 C CD1 . LEU B 1 63  ? 40.41100  12.83700  -7.45100  1.000 51.81062  ?  71  LEU B CD1 1 
ATOM   2474 C CD2 . LEU B 1 63  ? 39.56100  11.36000  -9.27300  1.000 72.75597  ?  71  LEU B CD2 1 
ATOM   2475 N N   . THR B 1 64  ? 42.17900  7.52800   -8.77700  1.000 61.78277  ?  72  THR B N   1 
ATOM   2476 C CA  . THR B 1 64  ? 43.21600  6.71000   -9.38200  1.000 65.58760  ?  72  THR B CA  1 
ATOM   2477 C C   . THR B 1 64  ? 43.88900  7.46400   -10.52400 1.000 77.32629  ?  72  THR B C   1 
ATOM   2478 O O   . THR B 1 64  ? 43.50200  8.57600   -10.88800 1.000 80.80684  ?  72  THR B O   1 
ATOM   2479 C CB  . THR B 1 64  ? 42.63800  5.39200   -9.89000  1.000 66.58891  ?  72  THR B CB  1 
ATOM   2480 O OG1 . THR B 1 64  ? 41.33500  5.62300   -10.43200 1.000 76.37564  ?  72  THR B OG1 1 
ATOM   2481 C CG2 . THR B 1 64  ? 42.53400  4.38700   -8.75900  1.000 66.33735  ?  72  THR B CG2 1 
ATOM   2482 N N   . ASP B 1 65  ? 44.92000  6.83600   -11.09400 1.000 78.78011  ?  73  ASP B N   1 
ATOM   2483 C CA  . ASP B 1 65  ? 45.64200  7.45500   -12.19900 1.000 78.17322  ?  73  ASP B CA  1 
ATOM   2484 C C   . ASP B 1 65  ? 44.79100  7.52900   -13.45900 1.000 80.41520  ?  73  ASP B C   1 
ATOM   2485 O O   . ASP B 1 65  ? 45.03400  8.38100   -14.32000 1.000 82.83012  ?  73  ASP B O   1 
ATOM   2486 C CB  . ASP B 1 65  ? 46.93300  6.68700   -12.47700 1.000 83.20483  ?  73  ASP B CB  1 
ATOM   2487 C CG  . ASP B 1 65  ? 48.12100  7.60200   -12.67700 1.000 93.95525  ?  73  ASP B CG  1 
ATOM   2488 O OD1 . ASP B 1 65  ? 47.90900  8.82000   -12.84900 1.000 89.16655  ?  73  ASP B OD1 1 
ATOM   2489 O OD2 . ASP B 1 65  ? 49.26600  7.10400   -12.66300 1.000 99.86105  -1 73  ASP B OD2 1 
ATOM   2490 N N   . ASP B 1 66  ? 43.79800  6.65300   -13.58800 1.000 75.75029  ?  74  ASP B N   1 
ATOM   2491 C CA  . ASP B 1 66  ? 42.96400  6.59600   -14.78000 1.000 68.28273  ?  74  ASP B CA  1 
ATOM   2492 C C   . ASP B 1 66  ? 41.66500  7.38000   -14.63400 1.000 72.84685  ?  74  ASP B C   1 
ATOM   2493 O O   . ASP B 1 66  ? 40.79800  7.28200   -15.50700 1.000 83.82849  ?  74  ASP B O   1 
ATOM   2494 C CB  . ASP B 1 66  ? 42.65500  5.14100   -15.14300 1.000 70.84178  ?  74  ASP B CB  1 
ATOM   2495 C CG  . ASP B 1 66  ? 41.94700  4.39600   -14.03000 1.000 78.59166  ?  74  ASP B CG  1 
ATOM   2496 O OD1 . ASP B 1 66  ? 42.57400  4.14500   -12.98000 1.000 80.02641  ?  74  ASP B OD1 1 
ATOM   2497 O OD2 . ASP B 1 66  ? 40.76000  4.05500   -14.20800 1.000 80.51194  -1 74  ASP B OD2 1 
ATOM   2498 N N   . GLY B 1 67  ? 41.50900  8.14700   -13.56100 1.000 73.79625  ?  75  GLY B N   1 
ATOM   2499 C CA  . GLY B 1 67  ? 40.32500  8.96300   -13.38500 1.000 75.29823  ?  75  GLY B CA  1 
ATOM   2500 C C   . GLY B 1 67  ? 39.16400  8.28800   -12.69500 1.000 72.80416  ?  75  GLY B C   1 
ATOM   2501 O O   . GLY B 1 67  ? 38.05700  8.83800   -12.70200 1.000 74.57620  ?  75  GLY B O   1 
ATOM   2502 N N   . ASP B 1 68  ? 39.37300  7.11900   -12.10300 1.000 74.75234  ?  76  ASP B N   1 
ATOM   2503 C CA  . ASP B 1 68  ? 38.34200  6.41400   -11.36000 1.000 73.26497  ?  76  ASP B CA  1 
ATOM   2504 C C   . ASP B 1 68  ? 38.42700  6.77000   -9.87900  1.000 75.40018  ?  76  ASP B C   1 
ATOM   2505 O O   . ASP B 1 68  ? 39.29500  7.52800   -9.44200  1.000 74.25087  ?  76  ASP B O   1 
ATOM   2506 C CB  . ASP B 1 68  ? 38.48200  4.90200   -11.55700 1.000 67.56635  ?  76  ASP B CB  1 
ATOM   2507 C CG  . ASP B 1 68  ? 37.15600  4.17900   -11.50300 1.000 72.57295  ?  76  ASP B CG  1 
ATOM   2508 O OD1 . ASP B 1 68  ? 36.13200  4.82400   -11.19800 1.000 76.74146  ?  76  ASP B OD1 1 
ATOM   2509 O OD2 . ASP B 1 68  ? 37.14200  2.95900   -11.75700 1.000 70.14510  -1 76  ASP B OD2 1 
ATOM   2510 N N   . ILE B 1 69  ? 37.50200  6.21400   -9.10100  1.000 71.08763  ?  77  ILE B N   1 
ATOM   2511 C CA  . ILE B 1 69  ? 37.47800  6.39300   -7.65500  1.000 63.81702  ?  77  ILE B CA  1 
ATOM   2512 C C   . ILE B 1 69  ? 37.59800  5.01500   -7.01900  1.000 63.05488  ?  77  ILE B C   1 
ATOM   2513 O O   . ILE B 1 69  ? 36.81700  4.10700   -7.33100  1.000 59.96594  ?  77  ILE B O   1 
ATOM   2514 C CB  . ILE B 1 69  ? 36.20500  7.11400   -7.18900  1.000 59.21356  ?  77  ILE B CB  1 
ATOM   2515 C CG1 . ILE B 1 69  ? 36.38400  8.62600   -7.30000  1.000 59.79556  ?  77  ILE B CG1 1 
ATOM   2516 C CG2 . ILE B 1 69  ? 35.90800  6.77900   -5.74100  1.000 54.52310  ?  77  ILE B CG2 1 
ATOM   2517 C CD1 . ILE B 1 69  ? 35.08300  9.38900   -7.30400  1.000 52.42122  ?  77  ILE B CD1 1 
ATOM   2518 N N   . GLU B 1 70  ? 38.57700  4.85900   -6.13500  1.000 61.59447  ?  78  GLU B N   1 
ATOM   2519 C CA  . GLU B 1 70  ? 38.86000  3.59700   -5.47300  1.000 58.99266  ?  78  GLU B CA  1 
ATOM   2520 C C   . GLU B 1 70  ? 38.48700  3.69900   -4.00100  1.000 57.99560  ?  78  GLU B C   1 
ATOM   2521 O O   . GLU B 1 70  ? 38.85000  4.67300   -3.32900  1.000 56.13307  ?  78  GLU B O   1 
ATOM   2522 C CB  . GLU B 1 70  ? 40.33600  3.22900   -5.62100  1.000 59.61486  ?  78  GLU B CB  1 
ATOM   2523 C CG  . GLU B 1 70  ? 40.68100  1.82400   -5.16800  1.000 62.54333  ?  78  GLU B CG  1 
ATOM   2524 C CD  . GLU B 1 70  ? 42.10600  1.44300   -5.51000  1.000 70.26862  ?  78  GLU B CD  1 
ATOM   2525 O OE1 . GLU B 1 70  ? 43.02000  2.24200   -5.22200  1.000 63.94748  ?  78  GLU B OE1 1 
ATOM   2526 O OE2 . GLU B 1 70  ? 42.31200  0.34600   -6.07000  1.000 68.01257  -1 78  GLU B OE2 1 
ATOM   2527 N N   . ILE B 1 71  ? 37.75900  2.69700   -3.51500  1.000 54.22811  ?  79  ILE B N   1 
ATOM   2528 C CA  . ILE B 1 71  ? 37.34200  2.60900   -2.12300  1.000 51.20862  ?  79  ILE B CA  1 
ATOM   2529 C C   . ILE B 1 71  ? 38.21700  1.57900   -1.42300  1.000 51.42280  ?  79  ILE B C   1 
ATOM   2530 O O   . ILE B 1 71  ? 38.33900  0.43900   -1.89000  1.000 49.96519  ?  79  ILE B O   1 
ATOM   2531 C CB  . ILE B 1 71  ? 35.85700  2.22500   -2.02100  1.000 50.06254  ?  79  ILE B CB  1 
ATOM   2532 C CG1 . ILE B 1 71  ? 34.98200  3.27300   -2.71400  1.000 46.50430  ?  79  ILE B CG1 1 
ATOM   2533 C CG2 . ILE B 1 71  ? 35.45200  2.03300   -0.57100  1.000 55.57502  ?  79  ILE B CG2 1 
ATOM   2534 C CD1 . ILE B 1 71  ? 34.67600  4.47700   -1.86300  1.000 47.41384  ?  79  ILE B CD1 1 
ATOM   2535 N N   . LEU B 1 72  ? 38.81600  1.97800   -0.30100  1.000 55.35435  ?  80  LEU B N   1 
ATOM   2536 C CA  . LEU B 1 72  ? 39.78000  1.17100   0.43100   1.000 55.55851  ?  80  LEU B CA  1 
ATOM   2537 C C   . LEU B 1 72  ? 39.37200  1.05000   1.89200   1.000 52.67703  ?  80  LEU B C   1 
ATOM   2538 O O   . LEU B 1 72  ? 38.77700  1.97200   2.46100   1.000 50.72404  ?  80  LEU B O   1 
ATOM   2539 C CB  . LEU B 1 72  ? 41.18400  1.78100   0.36400   1.000 50.30704  ?  80  LEU B CB  1 
ATOM   2540 C CG  . LEU B 1 72  ? 41.67500  2.40500   -0.93900  1.000 53.23312  ?  80  LEU B CG  1 
ATOM   2541 C CD1 . LEU B 1 72  ? 41.38500  3.89300   -0.96000  1.000 55.11685  ?  80  LEU B CD1 1 
ATOM   2542 C CD2 . LEU B 1 72  ? 43.15800  2.15000   -1.10400  1.000 57.53793  ?  80  LEU B CD2 1 
ATOM   2543 N N   . THR B 1 73  ? 39.71500  -0.08700  2.49700   1.000 54.87105  ?  81  THR B N   1 
ATOM   2544 C CA  . THR B 1 73  ? 39.56100  -0.31500  3.93000   1.000 48.60757  ?  81  THR B CA  1 
ATOM   2545 C C   . THR B 1 73  ? 40.94200  -0.58400  4.51300   1.000 49.97934  ?  81  THR B C   1 
ATOM   2546 O O   . THR B 1 73  ? 41.65300  -1.48000  4.04700   1.000 49.04928  ?  81  THR B O   1 
ATOM   2547 C CB  . THR B 1 73  ? 38.61100  -1.47700  4.21200   1.000 45.99918  ?  81  THR B CB  1 
ATOM   2548 O OG1 . THR B 1 73  ? 39.11900  -2.67000  3.60400   1.000 50.75647  ?  81  THR B OG1 1 
ATOM   2549 C CG2 . THR B 1 73  ? 37.23500  -1.18100  3.65100   1.000 53.70110  ?  81  THR B CG2 1 
ATOM   2550 N N   . ASP B 1 74  ? 41.31400  0.19300   5.53100   1.000 47.44919  ?  82  ASP B N   1 
ATOM   2551 C CA  . ASP B 1 74  ? 42.63100  0.12600   6.16600   1.000 50.42475  ?  82  ASP B CA  1 
ATOM   2552 C C   . ASP B 1 74  ? 43.75500  0.34700   5.16000   1.000 51.33917  ?  82  ASP B C   1 
ATOM   2553 O O   . ASP B 1 74  ? 44.86500  -0.16100  5.33000   1.000 51.00499  ?  82  ASP B O   1 
ATOM   2554 C CB  . ASP B 1 74  ? 42.83400  -1.19900  6.90500   1.000 45.94187  ?  82  ASP B CB  1 
ATOM   2555 C CG  . ASP B 1 74  ? 42.13300  -1.22800  8.24400   1.000 48.57523  ?  82  ASP B CG  1 
ATOM   2556 O OD1 . ASP B 1 74  ? 41.75900  -0.15000  8.74700   1.000 49.33844  ?  82  ASP B OD1 1 
ATOM   2557 O OD2 . ASP B 1 74  ? 41.97200  -2.33100  8.80300   1.000 52.38170  -1 82  ASP B OD2 1 
ATOM   2558 N N   . GLY B 1 75  ? 43.47600  1.11300   4.10800   1.000 49.49311  ?  83  GLY B N   1 
ATOM   2559 C CA  . GLY B 1 75  ? 44.44100  1.36500   3.06300   1.000 56.52563  ?  83  GLY B CA  1 
ATOM   2560 C C   . GLY B 1 75  ? 44.55100  0.27400   2.02400   1.000 53.33015  ?  83  GLY B C   1 
ATOM   2561 O O   . GLY B 1 75  ? 45.30500  0.43600   1.05600   1.000 50.47554  ?  83  GLY B O   1 
ATOM   2562 N N   . ARG B 1 76  ? 43.82300  -0.82400  2.18700   1.000 52.14134  ?  84  ARG B N   1 
ATOM   2563 C CA  . ARG B 1 76  ? 43.79200  -1.95300  1.27500   1.000 51.27392  ?  84  ARG B CA  1 
ATOM   2564 C C   . ARG B 1 76  ? 42.71000  -1.75500  0.22500   1.000 53.78364  ?  84  ARG B C   1 
ATOM   2565 O O   . ARG B 1 76  ? 41.55100  -1.50300  0.57100   1.000 52.41835  ?  84  ARG B O   1 
ATOM   2566 C CB  . ARG B 1 76  ? 43.53100  -3.25600  2.03200   1.000 51.18467  ?  84  ARG B CB  1 
ATOM   2567 C CG  . ARG B 1 76  ? 44.53500  -3.54900  3.13300   1.000 47.92036  ?  84  ARG B CG  1 
ATOM   2568 C CD  . ARG B 1 76  ? 44.24300  -4.88400  3.79600   1.000 60.88919  ?  84  ARG B CD  1 
ATOM   2569 N NE  . ARG B 1 76  ? 45.14800  -5.16300  4.90400   1.000 64.96219  ?  84  ARG B NE  1 
ATOM   2570 C CZ  . ARG B 1 76  ? 44.75300  -5.44200  6.13900   1.000 64.77700  ?  84  ARG B CZ  1 
ATOM   2571 N NH1 . ARG B 1 76  ? 43.47100  -5.49000  6.46000   1.000 59.32855  ?  84  ARG B NH1 1 
ATOM   2572 N NH2 . ARG B 1 76  ? 45.66800  -5.68100  7.07400   1.000 55.92471  ?  84  ARG B NH2 1 
ATOM   2573 N N   . PRO B 1 77  ? 43.06600  -1.85100  -1.05600  1.000 59.43931  ?  85  PRO B N   1 
ATOM   2574 C CA  . PRO B 1 77  ? 42.08000  -1.63900  -2.12700  1.000 52.61862  ?  85  PRO B CA  1 
ATOM   2575 C C   . PRO B 1 77  ? 40.92400  -2.62000  -2.00500  1.000 54.65164  ?  85  PRO B C   1 
ATOM   2576 O O   . PRO B 1 77  ? 41.10800  -3.83400  -2.10800  1.000 54.49986  ?  85  PRO B O   1 
ATOM   2577 C CB  . PRO B 1 77  ? 42.89000  -1.87400  -3.40700  1.000 51.08138  ?  85  PRO B CB  1 
ATOM   2578 C CG  . PRO B 1 77  ? 44.30800  -1.65700  -3.00600  1.000 62.20259  ?  85  PRO B CG  1 
ATOM   2579 C CD  . PRO B 1 77  ? 44.41000  -2.12500  -1.58800  1.000 62.75359  ?  85  PRO B CD  1 
ATOM   2580 N N   . SER B 1 78  ? 39.72700  -2.08300  -1.78100  1.000 55.31030  ?  86  SER B N   1 
ATOM   2581 C CA  . SER B 1 78  ? 38.52300  -2.88500  -1.61600  1.000 49.06383  ?  86  SER B CA  1 
ATOM   2582 C C   . SER B 1 78  ? 37.70100  -2.97500  -2.89400  1.000 51.71929  ?  86  SER B C   1 
ATOM   2583 O O   . SER B 1 78  ? 37.32000  -4.07400  -3.30500  1.000 49.72752  ?  86  SER B O   1 
ATOM   2584 C CB  . SER B 1 78  ? 37.66600  -2.31400  -0.48000  1.000 54.76233  ?  86  SER B CB  1 
ATOM   2585 O OG  . SER B 1 78  ? 36.35200  -2.84000  -0.51300  1.000 56.53477  ?  86  SER B OG  1 
ATOM   2586 N N   . ALA B 1 79  ? 37.42500  -1.84300  -3.53900  1.000 52.88157  ?  87  ALA B N   1 
ATOM   2587 C CA  . ALA B 1 79  ? 36.61600  -1.86900  -4.75200  1.000 50.08026  ?  87  ALA B CA  1 
ATOM   2588 C C   . ALA B 1 79  ? 36.82100  -0.58600  -5.54100  1.000 53.42448  ?  87  ALA B C   1 
ATOM   2589 O O   . ALA B 1 79  ? 37.53800  0.32100   -5.11600  1.000 55.94795  ?  87  ALA B O   1 
ATOM   2590 C CB  . ALA B 1 79  ? 35.13000  -2.06100  -4.43300  1.000 44.33570  ?  87  ALA B CB  1 
ATOM   2591 N N   . ARG B 1 80  ? 36.18300  -0.53200  -6.70700  1.000 51.94292  ?  88  ARG B N   1 
ATOM   2592 C CA  . ARG B 1 80  ? 36.14700  0.65600   -7.54400  1.000 54.84167  ?  88  ARG B CA  1 
ATOM   2593 C C   . ARG B 1 80  ? 34.71700  0.93100   -7.99400  1.000 53.65045  ?  88  ARG B C   1 
ATOM   2594 O O   . ARG B 1 80  ? 33.91100  0.01200   -8.15600  1.000 52.25455  ?  88  ARG B O   1 
ATOM   2595 C CB  . ARG B 1 80  ? 37.06100  0.50600   -8.76400  1.000 57.37637  ?  88  ARG B CB  1 
ATOM   2596 C CG  . ARG B 1 80  ? 38.54000  0.64300   -8.44600  1.000 57.73248  ?  88  ARG B CG  1 
ATOM   2597 C CD  . ARG B 1 80  ? 39.38100  -0.31300  -9.27300  1.000 60.54184  ?  88  ARG B CD  1 
ATOM   2598 N NE  . ARG B 1 80  ? 40.80900  -0.09400  -9.07200  1.000 60.01717  ?  88  ARG B NE  1 
ATOM   2599 C CZ  . ARG B 1 80  ? 41.50400  0.88900   -9.62600  1.000 64.34764  ?  88  ARG B CZ  1 
ATOM   2600 N NH1 . ARG B 1 80  ? 40.93600  1.76600   -10.43700 1.000 66.90004  ?  88  ARG B NH1 1 
ATOM   2601 N NH2 . ARG B 1 80  ? 42.80200  0.99500   -9.36100  1.000 59.26094  ?  88  ARG B NH2 1 
ATOM   2602 N N   . VAL B 1 81  ? 34.41100  2.21600   -8.18900  1.000 47.50870  ?  89  VAL B N   1 
ATOM   2603 C CA  . VAL B 1 81  ? 33.04800  2.62100   -8.52300  1.000 55.66495  ?  89  VAL B CA  1 
ATOM   2604 C C   . VAL B 1 81  ? 32.63800  2.11900   -9.89900  1.000 63.46857  ?  89  VAL B C   1 
ATOM   2605 O O   . VAL B 1 81  ? 31.47300  1.76000   -10.11400 1.000 53.45331  ?  89  VAL B O   1 
ATOM   2606 C CB  . VAL B 1 81  ? 32.91200  4.15100   -8.41900  1.000 54.44300  ?  89  VAL B CB  1 
ATOM   2607 C CG1 . VAL B 1 81  ? 31.45600  4.55800   -8.50500  1.000 63.44316  ?  89  VAL B CG1 1 
ATOM   2608 C CG2 . VAL B 1 81  ? 33.50100  4.62600   -7.11800  1.000 47.99585  ?  89  VAL B CG2 1 
ATOM   2609 N N   . SER B 1 82  ? 33.57200  2.08700   -10.85200 1.000 56.76119  ?  90  SER B N   1 
ATOM   2610 C CA  . SER B 1 82  ? 33.24000  1.65000   -12.20300 1.000 50.23097  ?  90  SER B CA  1 
ATOM   2611 C C   . SER B 1 82  ? 32.76500  0.20400   -12.24500 1.000 52.25271  ?  90  SER B C   1 
ATOM   2612 O O   . SER B 1 82  ? 32.10900  -0.19000  -13.21500 1.000 66.09157  ?  90  SER B O   1 
ATOM   2613 C CB  . SER B 1 82  ? 34.44500  1.81900   -13.12600 1.000 36.21754  ?  90  SER B CB  1 
ATOM   2614 O OG  . SER B 1 82  ? 35.51100  0.98200   -12.72100 1.000 56.71101  ?  90  SER B OG  1 
ATOM   2615 N N   . GLU B 1 83  ? 33.08000  -0.59100  -11.22200 1.000 49.32647  ?  91  GLU B N   1 
ATOM   2616 C CA  . GLU B 1 83  ? 32.64500  -1.98000  -11.18300 1.000 51.33560  ?  91  GLU B CA  1 
ATOM   2617 C C   . GLU B 1 83  ? 31.18700  -2.13200  -10.77500 1.000 53.08107  ?  91  GLU B C   1 
ATOM   2618 O O   . GLU B 1 83  ? 30.65300  -3.24200  -10.85800 1.000 49.44120  ?  91  GLU B O   1 
ATOM   2619 C CB  . GLU B 1 83  ? 33.53600  -2.77700  -10.23000 1.000 55.74378  ?  91  GLU B CB  1 
ATOM   2620 C CG  . GLU B 1 83  ? 34.97300  -2.91400  -10.70000 1.000 58.52213  ?  91  GLU B CG  1 
ATOM   2621 C CD  . GLU B 1 83  ? 35.86900  -3.54600  -9.65600  1.000 69.76344  ?  91  GLU B CD  1 
ATOM   2622 O OE1 . GLU B 1 83  ? 35.34200  -4.23300  -8.75800  1.000 74.21796  ?  91  GLU B OE1 1 
ATOM   2623 O OE2 . GLU B 1 83  ? 37.09900  -3.35600  -9.73300  1.000 71.17578  -1 91  GLU B OE2 1 
ATOM   2624 N N   . GLY B 1 84  ? 30.53800  -1.06200  -10.33700 1.000 45.00200  ?  92  GLY B N   1 
ATOM   2625 C CA  . GLY B 1 84  ? 29.14900  -1.12200  -9.94300  1.000 50.08314  ?  92  GLY B CA  1 
ATOM   2626 C C   . GLY B 1 84  ? 28.97500  -1.10200  -8.43300  1.000 57.52788  ?  92  GLY B C   1 
ATOM   2627 O O   . GLY B 1 84  ? 29.89600  -1.37900  -7.66100  1.000 65.45115  ?  92  GLY B O   1 
ATOM   2628 N N   . PHE B 1 85  ? 27.75900  -0.76000  -8.00800  1.000 52.72015  ?  93  PHE B N   1 
ATOM   2629 C CA  . PHE B 1 85  ? 27.47300  -0.69100  -6.57900  1.000 59.49481  ?  93  PHE B CA  1 
ATOM   2630 C C   . PHE B 1 85  ? 27.29400  -2.08500  -5.98900  1.000 60.27668  ?  93  PHE B C   1 
ATOM   2631 O O   . PHE B 1 85  ? 27.68000  -2.33600  -4.84000  1.000 55.35157  ?  93  PHE B O   1 
ATOM   2632 C CB  . PHE B 1 85  ? 26.23600  0.17200   -6.31400  1.000 48.50530  ?  93  PHE B CB  1 
ATOM   2633 C CG  . PHE B 1 85  ? 26.16100  1.42700   -7.15100  1.000 60.54468  ?  93  PHE B CG  1 
ATOM   2634 C CD1 . PHE B 1 85  ? 25.85400  1.37500   -8.50300  1.000 71.20156  ?  93  PHE B CD1 1 
ATOM   2635 C CD2 . PHE B 1 85  ? 26.31200  2.66700   -6.56100  1.000 64.49745  ?  93  PHE B CD2 1 
ATOM   2636 C CE1 . PHE B 1 85  ? 25.76700  2.52800   -9.25500  1.000 66.28964  ?  93  PHE B CE1 1 
ATOM   2637 C CE2 . PHE B 1 85  ? 26.22500  3.82300   -7.30900  1.000 64.00482  ?  93  PHE B CE2 1 
ATOM   2638 C CZ  . PHE B 1 85  ? 25.95000  3.75300   -8.65600  1.000 65.08262  ?  93  PHE B CZ  1 
ATOM   2639 N N   . GLY B 1 86  ? 26.70800  -3.00200  -6.76100  1.000 62.73414  ?  94  GLY B N   1 
ATOM   2640 C CA  . GLY B 1 86  ? 26.60500  -4.37700  -6.30500  1.000 60.89584  ?  94  GLY B CA  1 
ATOM   2641 C C   . GLY B 1 86  ? 27.96200  -5.01300  -6.08300  1.000 55.83213  ?  94  GLY B C   1 
ATOM   2642 O O   . GLY B 1 86  ? 28.14100  -5.81200  -5.16400  1.000 51.59797  ?  94  GLY B O   1 
ATOM   2643 N N   . ALA B 1 87  ? 28.94000  -4.65900  -6.91900  1.000 55.30346  ?  95  ALA B N   1 
ATOM   2644 C CA  . ALA B 1 87  ? 30.29500  -5.16100  -6.72500  1.000 61.57775  ?  95  ALA B CA  1 
ATOM   2645 C C   . ALA B 1 87  ? 30.88300  -4.66900  -5.41000  1.000 65.75522  ?  95  ALA B C   1 
ATOM   2646 O O   . ALA B 1 87  ? 31.55400  -5.42500  -4.69900  1.000 65.63949  ?  95  ALA B O   1 
ATOM   2647 C CB  . ALA B 1 87  ? 31.18200  -4.74500  -7.89700  1.000 61.09172  ?  95  ALA B CB  1 
ATOM   2648 N N   . LEU B 1 88  ? 30.64700  -3.40200  -5.06900  1.000 57.91868  ?  96  LEU B N   1 
ATOM   2649 C CA  . LEU B 1 88  ? 31.18500  -2.86600  -3.82400  1.000 44.91968  ?  96  LEU B CA  1 
ATOM   2650 C C   . LEU B 1 88  ? 30.48600  -3.48600  -2.62000  1.000 44.30406  ?  96  LEU B C   1 
ATOM   2651 O O   . LEU B 1 88  ? 31.11400  -3.75400  -1.58900  1.000 47.88071  ?  96  LEU B O   1 
ATOM   2652 C CB  . LEU B 1 88  ? 31.06500  -1.34100  -3.82000  1.000 52.62738  ?  96  LEU B CB  1 
ATOM   2653 C CG  . LEU B 1 88  ? 31.48100  -0.57800  -2.56400  1.000 40.88867  ?  96  LEU B CG  1 
ATOM   2654 C CD1 . LEU B 1 88  ? 32.52300  0.46300   -2.91400  1.000 37.47327  ?  96  LEU B CD1 1 
ATOM   2655 C CD2 . LEU B 1 88  ? 30.28500  0.09200   -1.95000  1.000 35.65769  ?  96  LEU B CD2 1 
ATOM   2656 N N   . ALA B 1 89  ? 29.18200  -3.74200  -2.73900  1.000 49.66566  ?  97  ALA B N   1 
ATOM   2657 C CA  . ALA B 1 89  ? 28.48200  -4.46400  -1.68100  1.000 48.33672  ?  97  ALA B CA  1 
ATOM   2658 C C   . ALA B 1 89  ? 29.03400  -5.87600  -1.52300  1.000 52.85074  ?  97  ALA B C   1 
ATOM   2659 O O   . ALA B 1 89  ? 29.20200  -6.36700  -0.39900  1.000 52.01014  ?  97  ALA B O   1 
ATOM   2660 C CB  . ALA B 1 89  ? 26.98300  -4.50200  -1.97300  1.000 50.30789  ?  97  ALA B CB  1 
ATOM   2661 N N   . GLN B 1 90  ? 29.32400  -6.54400  -2.64200  1.000 54.17566  ?  98  GLN B N   1 
ATOM   2662 C CA  . GLN B 1 90  ? 29.91800  -7.87500  -2.59000  1.000 57.71379  ?  98  GLN B CA  1 
ATOM   2663 C C   . GLN B 1 90  ? 31.29100  -7.83900  -1.93400  1.000 53.25751  ?  98  GLN B C   1 
ATOM   2664 O O   . GLN B 1 90  ? 31.65600  -8.75700  -1.19300  1.000 57.13952  ?  98  GLN B O   1 
ATOM   2665 C CB  . GLN B 1 90  ? 30.00900  -8.45500  -4.00200  1.000 63.13320  ?  98  GLN B CB  1 
ATOM   2666 C CG  . GLN B 1 90  ? 30.34200  -9.93600  -4.05600  1.000 69.22814  ?  98  GLN B CG  1 
ATOM   2667 C CD  . GLN B 1 90  ? 31.66000  -10.20800 -4.75300  1.000 69.16508  ?  98  GLN B CD  1 
ATOM   2668 O OE1 . GLN B 1 90  ? 32.20200  -9.34300  -5.43900  1.000 67.14597  ?  98  GLN B OE1 1 
ATOM   2669 N NE2 . GLN B 1 90  ? 32.18300  -11.41500 -4.57800  1.000 68.01399  ?  98  GLN B NE2 1 
ATOM   2670 N N   . ALA B 1 91  ? 32.07300  -6.79600  -2.21200  1.000 47.45342  ?  99  ALA B N   1 
ATOM   2671 C CA  . ALA B 1 91  ? 33.37800  -6.65100  -1.57600  1.000 42.39913  ?  99  ALA B CA  1 
ATOM   2672 C C   . ALA B 1 91  ? 33.25100  -6.40200  -0.07900  1.000 48.92437  ?  99  ALA B C   1 
ATOM   2673 O O   . ALA B 1 91  ? 34.06700  -6.90100  0.70300   1.000 45.13612  ?  99  ALA B O   1 
ATOM   2674 C CB  . ALA B 1 91  ? 34.16200  -5.51800  -2.23500  1.000 39.14012  ?  99  ALA B CB  1 
ATOM   2675 N N   . TYR B 1 92  ? 32.24800  -5.62700  0.33400   1.000 50.94473  ?  100 TYR B N   1 
ATOM   2676 C CA  . TYR B 1 92  ? 32.04700  -5.35700  1.75300   1.000 48.01074  ?  100 TYR B CA  1 
ATOM   2677 C C   . TYR B 1 92  ? 31.50500  -6.56800  2.50400   1.000 53.20145  ?  100 TYR B C   1 
ATOM   2678 O O   . TYR B 1 92  ? 31.74200  -6.69700  3.70900   1.000 49.00927  ?  100 TYR B O   1 
ATOM   2679 C CB  . TYR B 1 92  ? 31.08900  -4.18000  1.93600   1.000 46.03383  ?  100 TYR B CB  1 
ATOM   2680 C CG  . TYR B 1 92  ? 31.73800  -2.81700  1.89800   1.000 44.17630  ?  100 TYR B CG  1 
ATOM   2681 C CD1 . TYR B 1 92  ? 32.90800  -2.56200  2.59500   1.000 44.93872  ?  100 TYR B CD1 1 
ATOM   2682 C CD2 . TYR B 1 92  ? 31.16300  -1.77700  1.18300   1.000 45.63254  ?  100 TYR B CD2 1 
ATOM   2683 C CE1 . TYR B 1 92  ? 33.49600  -1.31400  2.56700   1.000 46.35985  ?  100 TYR B CE1 1 
ATOM   2684 C CE2 . TYR B 1 92  ? 31.74300  -0.52700  1.15200   1.000 42.77652  ?  100 TYR B CE2 1 
ATOM   2685 C CZ  . TYR B 1 92  ? 32.90800  -0.30000  1.84400   1.000 46.77786  ?  100 TYR B CZ  1 
ATOM   2686 O OH  . TYR B 1 92  ? 33.48500  0.94700   1.80900   1.000 43.56235  ?  100 TYR B OH  1 
ATOM   2687 N N   . ALA B 1 93  ? 30.77600  -7.45000  1.81600   1.000 55.07021  ?  101 ALA B N   1 
ATOM   2688 C CA  . ALA B 1 93  ? 30.07000  -8.53500  2.49900   1.000 48.11028  ?  101 ALA B CA  1 
ATOM   2689 C C   . ALA B 1 93  ? 30.96800  -9.46300  3.31300   1.000 45.26729  ?  101 ALA B C   1 
ATOM   2690 O O   . ALA B 1 93  ? 30.63200  -9.73100  4.48000   1.000 41.63301  ?  101 ALA B O   1 
ATOM   2691 C CB  . ALA B 1 93  ? 29.24800  -9.32600  1.47600   1.000 41.55048  ?  101 ALA B CB  1 
ATOM   2692 N N   . PRO B 1 94  ? 32.08200  -10.00000 2.79300   1.000 47.79042  ?  102 PRO B N   1 
ATOM   2693 C CA  . PRO B 1 94  ? 32.87100  -10.94200 3.60500   1.000 49.04359  ?  102 PRO B CA  1 
ATOM   2694 C C   . PRO B 1 94  ? 33.49200  -10.31300 4.83700   1.000 54.24252  ?  102 PRO B C   1 
ATOM   2695 O O   . PRO B 1 94  ? 33.83600  -11.04100 5.77600   1.000 46.33338  ?  102 PRO B O   1 
ATOM   2696 C CB  . PRO B 1 94  ? 33.94900  -11.43500 2.63300   1.000 43.52972  ?  102 PRO B CB  1 
ATOM   2697 C CG  . PRO B 1 94  ? 34.07700  -10.36000 1.64200   1.000 40.90677  ?  102 PRO B CG  1 
ATOM   2698 C CD  . PRO B 1 94  ? 32.71900  -9.75700  1.48700   1.000 43.00019  ?  102 PRO B CD  1 
ATOM   2699 N N   . MET B 1 95  ? 33.64900  -8.99200  4.86100   1.000 49.66408  ?  103 MET B N   1 
ATOM   2700 C CA  . MET B 1 95  ? 34.19300  -8.29300  6.01500   1.000 44.80804  ?  103 MET B CA  1 
ATOM   2701 C C   . MET B 1 95  ? 33.16000  -8.06500  7.10700   1.000 43.61874  ?  103 MET B C   1 
ATOM   2702 O O   . MET B 1 95  ? 33.51800  -7.57400  8.18200   1.000 43.31244  ?  103 MET B O   1 
ATOM   2703 C CB  . MET B 1 95  ? 34.78400  -6.95400  5.57100   1.000 42.81591  ?  103 MET B CB  1 
ATOM   2704 C CG  . MET B 1 95  ? 35.73200  -7.07000  4.39200   1.000 46.97899  ?  103 MET B CG  1 
ATOM   2705 S SD  . MET B 1 95  ? 35.84700  -5.58200  3.38300   1.000 61.50237  ?  103 MET B SD  1 
ATOM   2706 C CE  . MET B 1 95  ? 35.48200  -4.31800  4.58500   1.000 38.43799  ?  103 MET B CE  1 
ATOM   2707 N N   . GLN B 1 96  ? 31.90100  -8.41100  6.86200   1.000 46.57898  ?  104 GLN B N   1 
ATOM   2708 C CA  . GLN B 1 96  ? 30.83600  -8.15300  7.81400   1.000 50.17854  ?  104 GLN B CA  1 
ATOM   2709 C C   . GLN B 1 96  ? 30.57900  -9.37300  8.69300   1.000 50.72561  ?  104 GLN B C   1 
ATOM   2710 O O   . GLN B 1 96  ? 31.01100  -10.49100 8.40100   1.000 57.33749  ?  104 GLN B O   1 
ATOM   2711 C CB  . GLN B 1 96  ? 29.55000  -7.75900  7.08700   1.000 45.33012  ?  104 GLN B CB  1 
ATOM   2712 C CG  . GLN B 1 96  ? 29.65200  -6.46800  6.29800   1.000 44.17054  ?  104 GLN B CG  1 
ATOM   2713 C CD  . GLN B 1 96  ? 28.37200  -6.13300  5.56300   1.000 47.67728  ?  104 GLN B CD  1 
ATOM   2714 O OE1 . GLN B 1 96  ? 28.28600  -6.27600  4.34500   1.000 54.10888  ?  104 GLN B OE1 1 
ATOM   2715 N NE2 . GLN B 1 96  ? 27.36700  -5.68800  6.30200   1.000 50.78685  ?  104 GLN B NE2 1 
ATOM   2716 N N   . ALA B 1 97  ? 29.86400  -9.13500  9.79100   1.000 49.34761  ?  105 ALA B N   1 
ATOM   2717 C CA  . ALA B 1 97  ? 29.43500  -10.18300 10.71900  1.000 43.94005  ?  105 ALA B CA  1 
ATOM   2718 C C   . ALA B 1 97  ? 28.14600  -9.68100  11.36300  1.000 51.22884  ?  105 ALA B C   1 
ATOM   2719 O O   . ALA B 1 97  ? 28.17700  -8.82000  12.24400  1.000 55.64453  ?  105 ALA B O   1 
ATOM   2720 C CB  . ALA B 1 97  ? 30.50500  -10.49200 11.75600  1.000 43.03882  ?  105 ALA B CB  1 
ATOM   2721 N N   . LEU B 1 98  ? 27.01600  -10.21400 10.91200  1.000 46.69687  ?  106 LEU B N   1 
ATOM   2722 C CA  . LEU B 1 98  ? 25.71100  -9.76200  11.36600  1.000 50.46251  ?  106 LEU B CA  1 
ATOM   2723 C C   . LEU B 1 98  ? 24.94400  -10.91200 12.00300  1.000 53.74156  ?  106 LEU B C   1 
ATOM   2724 O O   . LEU B 1 98  ? 25.03300  -12.05700 11.55100  1.000 57.11584  ?  106 LEU B O   1 
ATOM   2725 C CB  . LEU B 1 98  ? 24.90900  -9.17800  10.20200  1.000 49.64947  ?  106 LEU B CB  1 
ATOM   2726 C CG  . LEU B 1 98  ? 25.44200  -7.86400  9.63200   1.000 47.65574  ?  106 LEU B CG  1 
ATOM   2727 C CD1 . LEU B 1 98  ? 25.60600  -7.96900  8.12700   1.000 48.29192  ?  106 LEU B CD1 1 
ATOM   2728 C CD2 . LEU B 1 98  ? 24.53400  -6.70900  9.99300   1.000 48.97671  ?  106 LEU B CD2 1 
ATOM   2729 N N   . ASP B 1 99  ? 24.19500  -10.60100 13.05700  1.000 55.44645  ?  107 ASP B N   1 
ATOM   2730 C CA  . ASP B 1 99  ? 23.39000  -11.60100 13.74000  1.000 59.73578  ?  107 ASP B CA  1 
ATOM   2731 C C   . ASP B 1 99  ? 21.98300  -11.62500 13.14200  1.000 57.37692  ?  107 ASP B C   1 
ATOM   2732 O O   . ASP B 1 99  ? 21.71100  -11.01300 12.10700  1.000 59.76625  ?  107 ASP B O   1 
ATOM   2733 C CB  . ASP B 1 99  ? 23.38300  -11.34600 15.24900  1.000 57.50327  ?  107 ASP B CB  1 
ATOM   2734 C CG  . ASP B 1 99  ? 22.79000  -9.99900  15.62800  1.000 56.72667  ?  107 ASP B CG  1 
ATOM   2735 O OD1 . ASP B 1 99  ? 22.19800  -9.32000  14.76600  1.000 58.09880  ?  107 ASP B OD1 1 
ATOM   2736 O OD2 . ASP B 1 99  ? 22.91000  -9.61900  16.81100  1.000 60.86905  -1 107 ASP B OD2 1 
ATOM   2737 N N   . GLU B 1 100 ? 21.06900  -12.33800 13.80100  1.000 61.24958  ?  108 GLU B N   1 
ATOM   2738 C CA  . GLU B 1 100 ? 19.71600  -12.48700 13.28300  1.000 64.17484  ?  108 GLU B CA  1 
ATOM   2739 C C   . GLU B 1 100 ? 18.91700  -11.19200 13.34000  1.000 53.46044  ?  108 GLU B C   1 
ATOM   2740 O O   . GLU B 1 100 ? 17.93900  -11.05300 12.59900  1.000 59.44164  ?  108 GLU B O   1 
ATOM   2741 C CB  . GLU B 1 100 ? 18.98300  -13.58400 14.05300  1.000 66.93024  ?  108 GLU B CB  1 
ATOM   2742 C CG  . GLU B 1 100 ? 19.89100  -14.69200 14.55400  1.000 64.88688  ?  108 GLU B CG  1 
ATOM   2743 C CD  . GLU B 1 100 ? 20.25700  -14.52500 16.01400  1.000 76.41117  ?  108 GLU B CD  1 
ATOM   2744 O OE1 . GLU B 1 100 ? 20.38600  -13.36900 16.46700  1.000 71.09056  ?  108 GLU B OE1 1 
ATOM   2745 O OE2 . GLU B 1 100 ? 20.41900  -15.54900 16.70800  1.000 88.34844  -1 108 GLU B OE2 1 
ATOM   2746 N N   . ARG B 1 101 ? 19.30400  -10.24700 14.19300  1.000 55.29868  ?  109 ARG B N   1 
ATOM   2747 C CA  . ARG B 1 101 ? 18.59600  -8.97900  14.29800  1.000 55.14319  ?  109 ARG B CA  1 
ATOM   2748 C C   . ARG B 1 101 ? 19.08500  -7.93700  13.30300  1.000 56.29447  ?  109 ARG B C   1 
ATOM   2749 O O   . ARG B 1 101 ? 18.51100  -6.84500  13.24400  1.000 49.07637  ?  109 ARG B O   1 
ATOM   2750 C CB  . ARG B 1 101 ? 18.72100  -8.41400  15.71600  1.000 49.35656  ?  109 ARG B CB  1 
ATOM   2751 C CG  . ARG B 1 101 ? 18.10800  -9.28300  16.79300  1.000 53.22147  ?  109 ARG B CG  1 
ATOM   2752 C CD  . ARG B 1 101 ? 18.34500  -8.69700  18.17500  1.000 63.38722  ?  109 ARG B CD  1 
ATOM   2753 N NE  . ARG B 1 101 ? 19.75600  -8.70600  18.54300  1.000 70.55748  ?  109 ARG B NE  1 
ATOM   2754 C CZ  . ARG B 1 101 ? 20.24100  -8.18600  19.66200  1.000 70.26545  ?  109 ARG B CZ  1 
ATOM   2755 N NH1 . ARG B 1 101 ? 19.45400  -7.60200  20.55100  1.000 64.30674  ?  109 ARG B NH1 1 
ATOM   2756 N NH2 . ARG B 1 101 ? 21.54800  -8.25500  19.89600  1.000 60.34167  ?  109 ARG B NH2 1 
ATOM   2757 N N   . GLY B 1 102 ? 20.11300  -8.24600  12.52000  1.000 55.24078  ?  110 GLY B N   1 
ATOM   2758 C CA  . GLY B 1 102 ? 20.70000  -7.27000  11.62700  1.000 51.85265  ?  110 GLY B CA  1 
ATOM   2759 C C   . GLY B 1 102 ? 21.73000  -6.37100  12.26400  1.000 47.54654  ?  110 GLY B C   1 
ATOM   2760 O O   . GLY B 1 102 ? 22.12500  -5.37400  11.65000  1.000 48.27968  ?  110 GLY B O   1 
ATOM   2761 N N   . LEU B 1 103 ? 22.17200  -6.68300  13.47700  1.000 49.27877  ?  111 LEU B N   1 
ATOM   2762 C CA  . LEU B 1 103 ? 23.15500  -5.88400  14.19100  1.000 47.66196  ?  111 LEU B CA  1 
ATOM   2763 C C   . LEU B 1 103 ? 24.54400  -6.47900  14.00900  1.000 54.30320  ?  111 LEU B C   1 
ATOM   2764 O O   . LEU B 1 103 ? 24.70300  -7.69900  13.91900  1.000 46.25366  ?  111 LEU B O   1 
ATOM   2765 C CB  . LEU B 1 103 ? 22.81600  -5.80500  15.67900  1.000 37.97003  ?  111 LEU B CB  1 
ATOM   2766 C CG  . LEU B 1 103 ? 21.48000  -5.15900  16.03400  1.000 48.54742  ?  111 LEU B CG  1 
ATOM   2767 C CD1 . LEU B 1 103 ? 21.12800  -5.45500  17.47800  1.000 50.84358  ?  111 LEU B CD1 1 
ATOM   2768 C CD2 . LEU B 1 103 ? 21.53100  -3.66500  15.78500  1.000 44.96278  ?  111 LEU B CD2 1 
ATOM   2769 N N   . SER B 1 104 ? 25.54600  -5.60700  13.95200  1.000 53.98428  ?  112 SER B N   1 
ATOM   2770 C CA  . SER B 1 104 ? 26.91700  -6.06000  13.78400  1.000 42.92614  ?  112 SER B CA  1 
ATOM   2771 C C   . SER B 1 104 ? 27.41900  -6.73700  15.05100  1.000 44.49362  ?  112 SER B C   1 
ATOM   2772 O O   . SER B 1 104 ? 27.20700  -6.25000  16.16400  1.000 51.91140  ?  112 SER B O   1 
ATOM   2773 C CB  . SER B 1 104 ? 27.82100  -4.88500  13.42800  1.000 42.15720  ?  112 SER B CB  1 
ATOM   2774 O OG  . SER B 1 104 ? 29.17700  -5.28500  13.36400  1.000 39.19827  ?  112 SER B OG  1 
ATOM   2775 N N   . GLN B 1 105 ? 28.09300  -7.86900  14.87200  1.000 40.66158  ?  113 GLN B N   1 
ATOM   2776 C CA  . GLN B 1 105 ? 28.71300  -8.57700  15.97900  1.000 39.35246  ?  113 GLN B CA  1 
ATOM   2777 C C   . GLN B 1 105 ? 30.13200  -8.10400  16.25200  1.000 43.42340  ?  113 GLN B C   1 
ATOM   2778 O O   . GLN B 1 105 ? 30.68200  -8.41600  17.31400  1.000 43.86671  ?  113 GLN B O   1 
ATOM   2779 C CB  . GLN B 1 105 ? 28.71700  -10.08200 15.69400  1.000 46.96772  ?  113 GLN B CB  1 
ATOM   2780 C CG  . GLN B 1 105 ? 27.33100  -10.66700 15.47100  1.000 50.10036  ?  113 GLN B CG  1 
ATOM   2781 C CD  . GLN B 1 105 ? 27.35800  -12.15200 15.18300  1.000 51.55916  ?  113 GLN B CD  1 
ATOM   2782 O OE1 . GLN B 1 105 ? 26.49000  -12.89800 15.63200  1.000 61.51363  ?  113 GLN B OE1 1 
ATOM   2783 N NE2 . GLN B 1 105 ? 28.35800  -12.59100 14.43100  1.000 55.06027  ?  113 GLN B NE2 1 
ATOM   2784 N N   . TRP B 1 106 ? 30.72900  -7.36100  15.32500  1.000 45.56886  ?  114 TRP B N   1 
ATOM   2785 C CA  . TRP B 1 106 ? 32.08100  -6.85600  15.51100  1.000 39.15508  ?  114 TRP B CA  1 
ATOM   2786 C C   . TRP B 1 106 ? 32.10600  -5.73800  16.54400  1.000 38.96098  ?  114 TRP B C   1 
ATOM   2787 O O   . TRP B 1 106 ? 31.15500  -4.96400  16.67000  1.000 39.93170  ?  114 TRP B O   1 
ATOM   2788 C CB  . TRP B 1 106 ? 32.64700  -6.33700  14.19000  1.000 40.56404  ?  114 TRP B CB  1 
ATOM   2789 C CG  . TRP B 1 106 ? 32.99500  -7.39100  13.18100  1.000 47.40979  ?  114 TRP B CG  1 
ATOM   2790 C CD1 . TRP B 1 106 ? 32.66400  -7.39200  11.86000  1.000 44.39076  ?  114 TRP B CD1 1 
ATOM   2791 C CD2 . TRP B 1 106 ? 33.76400  -8.58100  13.40200  1.000 54.91680  ?  114 TRP B CD2 1 
ATOM   2792 N NE1 . TRP B 1 106 ? 33.16600  -8.51100  11.24600  1.000 48.46730  ?  114 TRP B NE1 1 
ATOM   2793 C CE2 . TRP B 1 106 ? 33.84500  -9.25700  12.17100  1.000 53.53510  ?  114 TRP B CE2 1 
ATOM   2794 C CE3 . TRP B 1 106 ? 34.38700  -9.14200  14.52100  1.000 46.86070  ?  114 TRP B CE3 1 
ATOM   2795 C CZ2 . TRP B 1 106 ? 34.52100  -10.46400 12.02700  1.000 56.85724  ?  114 TRP B CZ2 1 
ATOM   2796 C CZ3 . TRP B 1 106 ? 35.05500  -10.33900 14.37500  1.000 54.09817  ?  114 TRP B CZ3 1 
ATOM   2797 C CH2 . TRP B 1 106 ? 35.11800  -10.98700 13.13800  1.000 57.03459  ?  114 TRP B CH2 1 
ATOM   2798 N N   . ALA B 1 107 ? 33.20900  -5.65500  17.27900  1.000 40.94982  ?  115 ALA B N   1 
ATOM   2799 C CA  . ALA B 1 107 ? 33.43700  -4.54000  18.18200  1.000 34.57314  ?  115 ALA B CA  1 
ATOM   2800 C C   . ALA B 1 107 ? 34.13200  -3.40000  17.45000  1.000 35.13922  ?  115 ALA B C   1 
ATOM   2801 O O   . ALA B 1 107 ? 35.01400  -3.61500  16.61500  1.000 49.08607  ?  115 ALA B O   1 
ATOM   2802 C CB  . ALA B 1 107 ? 34.27400  -4.97900  19.38200  1.000 40.66633  ?  115 ALA B CB  1 
ATOM   2803 N N   . ALA B 1 108 ? 33.72200  -2.17400  17.77300  1.000 26.35584  ?  116 ALA B N   1 
ATOM   2804 C CA  . ALA B 1 108 ? 34.28100  -1.00800  17.09900  1.000 29.22747  ?  116 ALA B CA  1 
ATOM   2805 C C   . ALA B 1 108 ? 35.71300  -0.73000  17.53300  1.000 35.11728  ?  116 ALA B C   1 
ATOM   2806 O O   . ALA B 1 108 ? 36.48800  -0.14800  16.76600  1.000 34.55207  ?  116 ALA B O   1 
ATOM   2807 C CB  . ALA B 1 108 ? 33.40200  0.21200   17.35400  1.000 29.23579  ?  116 ALA B CB  1 
ATOM   2808 N N   . LEU B 1 109 ? 36.08400  -1.12600  18.74800  1.000 38.20447  ?  117 LEU B N   1 
ATOM   2809 C CA  . LEU B 1 109 ? 37.43400  -0.92500  19.25400  1.000 35.42798  ?  117 LEU B CA  1 
ATOM   2810 C C   . LEU B 1 109 ? 38.35900  -2.09500  18.95400  1.000 43.87883  ?  117 LEU B C   1 
ATOM   2811 O O   . LEU B 1 109 ? 39.53500  -2.04900  19.32600  1.000 54.77823  ?  117 LEU B O   1 
ATOM   2812 C CB  . LEU B 1 109 ? 37.40200  -0.67400  20.76200  1.000 35.51590  ?  117 LEU B CB  1 
ATOM   2813 C CG  . LEU B 1 109 ? 36.80000  0.64400   21.24000  1.000 36.07889  ?  117 LEU B CG  1 
ATOM   2814 C CD1 . LEU B 1 109 ? 36.80300  0.69600   22.75300  1.000 32.69405  ?  117 LEU B CD1 1 
ATOM   2815 C CD2 . LEU B 1 109 ? 37.57000  1.81200   20.66600  1.000 40.45491  ?  117 LEU B CD2 1 
ATOM   2816 N N   . GLY B 1 110 ? 37.86200  -3.13400  18.29000  1.000 44.13230  ?  118 GLY B N   1 
ATOM   2817 C CA  . GLY B 1 110 ? 38.70600  -4.27900  18.00000  1.000 58.83406  ?  118 GLY B CA  1 
ATOM   2818 C C   . GLY B 1 110 ? 38.84900  -5.18500  19.20700  1.000 54.23023  ?  118 GLY B C   1 
ATOM   2819 O O   . GLY B 1 110 ? 37.94700  -5.29500  20.04500  1.000 52.91951  ?  118 GLY B O   1 
ATOM   2820 N N   . GLU B 1 111 ? 39.99800  -5.85100  19.29500  1.000 55.42968  ?  119 GLU B N   1 
ATOM   2821 C CA  . GLU B 1 111 ? 40.25200  -6.77100  20.39500  1.000 61.31492  ?  119 GLU B CA  1 
ATOM   2822 C C   . GLU B 1 111 ? 40.29800  -6.01600  21.71600  1.000 55.11284  ?  119 GLU B C   1 
ATOM   2823 O O   . GLU B 1 111 ? 40.87200  -4.92700  21.80400  1.000 50.72506  ?  119 GLU B O   1 
ATOM   2824 C CB  . GLU B 1 111 ? 41.56100  -7.52400  20.16900  1.000 66.65811  ?  119 GLU B CB  1 
ATOM   2825 C CG  . GLU B 1 111 ? 41.47100  -8.64800  19.15200  1.000 65.40657  ?  119 GLU B CG  1 
ATOM   2826 C CD  . GLU B 1 111 ? 42.74600  -9.46500  19.07400  1.000 74.64184  ?  119 GLU B CD  1 
ATOM   2827 O OE1 . GLU B 1 111 ? 43.79000  -8.98900  19.56700  1.000 71.09357  ?  119 GLU B OE1 1 
ATOM   2828 O OE2 . GLU B 1 111 ? 42.70500  -10.58500 18.52300  1.000 86.26999  -1 119 GLU B OE2 1 
ATOM   2829 N N   . GLY B 1 112 ? 39.69300  -6.59600  22.73500  1.000 42.94395  ?  120 GLY B N   1 
ATOM   2830 C CA  . GLY B 1 112 ? 39.62000  -5.96500  24.03700  1.000 44.19365  ?  120 GLY B CA  1 
ATOM   2831 C C   . GLY B 1 112 ? 38.29400  -6.28500  24.69300  1.000 39.37955  ?  120 GLY B C   1 
ATOM   2832 O O   . GLY B 1 112 ? 37.43000  -6.93700  24.11700  1.000 44.37259  ?  120 GLY B O   1 
ATOM   2833 N N   . TYR B 1 113 ? 38.15300  -5.80200  25.92300  1.000 33.71694  ?  121 TYR B N   1 
ATOM   2834 C CA  . TYR B 1 113 ? 36.94500  -6.07800  26.68600  1.000 39.55764  ?  121 TYR B CA  1 
ATOM   2835 C C   . TYR B 1 113 ? 35.76800  -5.27700  26.14800  1.000 37.85749  ?  121 TYR B C   1 
ATOM   2836 O O   . TYR B 1 113 ? 35.91400  -4.12400  25.73400  1.000 41.45495  ?  121 TYR B O   1 
ATOM   2837 C CB  . TYR B 1 113 ? 37.15200  -5.75500  28.16300  1.000 27.85604  ?  121 TYR B CB  1 
ATOM   2838 C CG  . TYR B 1 113 ? 35.91600  -6.00000  28.99600  1.000 28.93488  ?  121 TYR B CG  1 
ATOM   2839 C CD1 . TYR B 1 113 ? 35.58000  -7.27800  29.41200  1.000 26.10300  ?  121 TYR B CD1 1 
ATOM   2840 C CD2 . TYR B 1 113 ? 35.07500  -4.95800  29.34700  1.000 29.40198  ?  121 TYR B CD2 1 
ATOM   2841 C CE1 . TYR B 1 113 ? 34.44900  -7.50700  30.16300  1.000 25.53767  ?  121 TYR B CE1 1 
ATOM   2842 C CE2 . TYR B 1 113 ? 33.94100  -5.18100  30.09200  1.000 25.34586  ?  121 TYR B CE2 1 
ATOM   2843 C CZ  . TYR B 1 113 ? 33.63400  -6.45300  30.50100  1.000 23.63192  ?  121 TYR B CZ  1 
ATOM   2844 O OH  . TYR B 1 113 ? 32.50200  -6.67000  31.24800  1.000 24.09694  ?  121 TYR B OH  1 
ATOM   2845 N N   . ARG B 1 114 ? 34.59200  -5.89600  26.16100  1.000 29.69333  ?  122 ARG B N   1 
ATOM   2846 C CA  . ARG B 1 114 ? 33.35200  -5.23900  25.78000  1.000 32.70963  ?  122 ARG B CA  1 
ATOM   2847 C C   . ARG B 1 114 ? 32.37300  -5.31800  26.94000  1.000 30.60292  ?  122 ARG B C   1 
ATOM   2848 O O   . ARG B 1 114 ? 32.10400  -6.40700  27.45600  1.000 32.83509  ?  122 ARG B O   1 
ATOM   2849 C CB  . ARG B 1 114 ? 32.74200  -5.88000  24.53500  1.000 39.27685  ?  122 ARG B CB  1 
ATOM   2850 C CG  . ARG B 1 114 ? 31.86900  -4.94100  23.73000  1.000 35.69809  ?  122 ARG B CG  1 
ATOM   2851 C CD  . ARG B 1 114 ? 30.76100  -5.70100  23.03600  1.000 48.39253  ?  122 ARG B CD  1 
ATOM   2852 N NE  . ARG B 1 114 ? 31.24600  -6.48900  21.91200  1.000 42.79110  ?  122 ARG B NE  1 
ATOM   2853 C CZ  . ARG B 1 114 ? 31.12200  -6.13200  20.64300  1.000 43.60703  ?  122 ARG B CZ  1 
ATOM   2854 N NH1 . ARG B 1 114 ? 30.53700  -4.99700  20.29900  1.000 43.88458  ?  122 ARG B NH1 1 
ATOM   2855 N NH2 . ARG B 1 114 ? 31.59300  -6.93500  19.69500  1.000 50.55824  ?  122 ARG B NH2 1 
ATOM   2856 N N   . ALA B 1 115 ? 31.84500  -4.16900  27.34300  1.000 29.92683  ?  123 ALA B N   1 
ATOM   2857 C CA  . ALA B 1 115 ? 30.87100  -4.13700  28.42000  1.000 32.32018  ?  123 ALA B CA  1 
ATOM   2858 C C   . ALA B 1 115 ? 29.54500  -4.73200  27.95000  1.000 37.76372  ?  123 ALA B C   1 
ATOM   2859 O O   . ALA B 1 115 ? 29.20200  -4.63000  26.76900  1.000 39.05290  ?  123 ALA B O   1 
ATOM   2860 C CB  . ALA B 1 115 ? 30.65900  -2.70500  28.91000  1.000 36.73599  ?  123 ALA B CB  1 
ATOM   2861 N N   . PRO B 1 116 ? 28.78700  -5.36300  28.84400  1.000 33.85306  ?  124 PRO B N   1 
ATOM   2862 C CA  . PRO B 1 116 ? 27.49900  -5.93800  28.44300  1.000 35.27475  ?  124 PRO B CA  1 
ATOM   2863 C C   . PRO B 1 116 ? 26.50600  -4.86400  28.02700  1.000 39.05351  ?  124 PRO B C   1 
ATOM   2864 O O   . PRO B 1 116 ? 26.55400  -3.72600  28.49800  1.000 39.57797  ?  124 PRO B O   1 
ATOM   2865 C CB  . PRO B 1 116 ? 27.03200  -6.67300  29.70400  1.000 31.53222  ?  124 PRO B CB  1 
ATOM   2866 C CG  . PRO B 1 116 ? 28.26000  -6.87400  30.51500  1.000 32.80910  ?  124 PRO B CG  1 
ATOM   2867 C CD  . PRO B 1 116 ? 29.14400  -5.71100  30.22700  1.000 25.97957  ?  124 PRO B CD  1 
ATOM   2868 N N   . GLY B 1 117 ? 25.59400  -5.24100  27.13000  1.000 33.07680  ?  125 GLY B N   1 
ATOM   2869 C CA  . GLY B 1 117 ? 24.57200  -4.31600  26.67700  1.000 37.86834  ?  125 GLY B CA  1 
ATOM   2870 C C   . GLY B 1 117 ? 23.51100  -4.01100  27.71300  1.000 37.71451  ?  125 GLY B C   1 
ATOM   2871 O O   . GLY B 1 117 ? 22.85900  -2.96700  27.62700  1.000 44.98875  ?  125 GLY B O   1 
ATOM   2872 N N   . ASP B 1 118 ? 23.32400  -4.89600  28.69000  1.000 33.12937  ?  126 ASP B N   1 
ATOM   2873 C CA  . ASP B 1 118 ? 22.35200  -4.69100  29.75600  1.000 42.83145  ?  126 ASP B CA  1 
ATOM   2874 C C   . ASP B 1 118 ? 22.96200  -3.97800  30.95900  1.000 48.17753  ?  126 ASP B C   1 
ATOM   2875 O O   . ASP B 1 118 ? 22.49100  -4.14700  32.08800  1.000 50.58897  ?  126 ASP B O   1 
ATOM   2876 C CB  . ASP B 1 118 ? 21.72900  -6.02400  30.17700  1.000 57.00797  ?  126 ASP B CB  1 
ATOM   2877 C CG  . ASP B 1 118 ? 22.74100  -6.99800  30.76400  1.000 57.55516  ?  126 ASP B CG  1 
ATOM   2878 O OD1 . ASP B 1 118 ? 23.96000  -6.77800  30.61900  1.000 50.20644  ?  126 ASP B OD1 1 
ATOM   2879 O OD2 . ASP B 1 118 ? 22.30900  -7.99600  31.37700  1.000 56.31163  -1 126 ASP B OD2 1 
ATOM   2880 N N   . LEU B 1 119 ? 24.00200  -3.18600  30.73300  1.000 40.87902  ?  127 LEU B N   1 
ATOM   2881 C CA  . LEU B 1 119 ? 24.67400  -2.49500  31.82100  1.000 37.25632  ?  127 LEU B CA  1 
ATOM   2882 C C   . LEU B 1 119 ? 23.76300  -1.42600  32.41600  1.000 33.86875  ?  127 LEU B C   1 
ATOM   2883 O O   . LEU B 1 119 ? 23.07300  -0.72000  31.66900  1.000 26.84021  ?  127 LEU B O   1 
ATOM   2884 C CB  . LEU B 1 119 ? 25.96900  -1.86000  31.31800  1.000 40.13724  ?  127 LEU B CB  1 
ATOM   2885 C CG  . LEU B 1 119 ? 27.01400  -1.47800  32.36400  1.000 33.08748  ?  127 LEU B CG  1 
ATOM   2886 C CD1 . LEU B 1 119 ? 27.89100  -2.66600  32.69200  1.000 35.00378  ?  127 LEU B CD1 1 
ATOM   2887 C CD2 . LEU B 1 119 ? 27.85100  -0.32000  31.86500  1.000 34.12509  ?  127 LEU B CD2 1 
ATOM   2888 N N   . PRO B 1 120 ? 23.72500  -1.27900  33.74000  1.000 35.62385  ?  128 PRO B N   1 
ATOM   2889 C CA  . PRO B 1 120 ? 22.93300  -0.20200  34.34000  1.000 26.85903  ?  128 PRO B CA  1 
ATOM   2890 C C   . PRO B 1 120 ? 23.47800  1.16600   33.96300  1.000 28.68106  ?  128 PRO B C   1 
ATOM   2891 O O   . PRO B 1 120 ? 24.66700  1.33300   33.68700  1.000 30.67778  ?  128 PRO B O   1 
ATOM   2892 C CB  . PRO B 1 120 ? 23.06100  -0.46000  35.84400  1.000 26.76906  ?  128 PRO B CB  1 
ATOM   2893 C CG  . PRO B 1 120 ? 23.43400  -1.89300  35.95700  1.000 29.12814  ?  128 PRO B CG  1 
ATOM   2894 C CD  . PRO B 1 120 ? 24.25800  -2.20600  34.75000  1.000 30.62995  ?  128 PRO B CD  1 
ATOM   2895 N N   . LEU B 1 121 ? 22.58200  2.15400   33.95900  1.000 31.55985  ?  129 LEU B N   1 
ATOM   2896 C CA  . LEU B 1 121 ? 22.93600  3.48100   33.46600  1.000 24.25229  ?  129 LEU B CA  1 
ATOM   2897 C C   . LEU B 1 121 ? 23.93900  4.17600   34.38000  1.000 26.88164  ?  129 LEU B C   1 
ATOM   2898 O O   . LEU B 1 121 ? 24.75800  4.97400   33.91400  1.000 24.98332  ?  129 LEU B O   1 
ATOM   2899 C CB  . LEU B 1 121 ? 21.67600  4.33000   33.30400  1.000 23.84022  ?  129 LEU B CB  1 
ATOM   2900 C CG  . LEU B 1 121 ? 20.65400  3.87200   32.25900  1.000 31.28596  ?  129 LEU B CG  1 
ATOM   2901 C CD1 . LEU B 1 121 ? 19.90300  5.06400   31.70100  1.000 33.35588  ?  129 LEU B CD1 1 
ATOM   2902 C CD2 . LEU B 1 121 ? 21.31700  3.09400   31.13400  1.000 24.18131  ?  129 LEU B CD2 1 
ATOM   2903 N N   . ALA B 1 122 ? 23.88200  3.90200   35.68500  1.000 27.52184  ?  130 ALA B N   1 
ATOM   2904 C CA  . ALA B 1 122 ? 24.85800  4.48600   36.60100  1.000 18.19067  ?  130 ALA B CA  1 
ATOM   2905 C C   . ALA B 1 122 ? 26.26200  3.97200   36.30900  1.000 23.78674  ?  130 ALA B C   1 
ATOM   2906 O O   . ALA B 1 122 ? 27.23700  4.73600   36.34100  1.000 33.95159  ?  130 ALA B O   1 
ATOM   2907 C CB  . ALA B 1 122 ? 24.46400  4.18400   38.04500  1.000 8.09529   ?  130 ALA B CB  1 
ATOM   2908 N N   . GLN B 1 123 ? 26.38400  2.67800   36.02100  1.000 23.02639  ?  131 GLN B N   1 
ATOM   2909 C CA  . GLN B 1 123 ? 27.67900  2.11700   35.65800  1.000 25.91810  ?  131 GLN B CA  1 
ATOM   2910 C C   . GLN B 1 123 ? 28.18100  2.70400   34.34400  1.000 24.37449  ?  131 GLN B C   1 
ATOM   2911 O O   . GLN B 1 123 ? 29.38000  2.97100   34.19300  1.000 24.59446  ?  131 GLN B O   1 
ATOM   2912 C CB  . GLN B 1 123 ? 27.57300  0.59600   35.58200  1.000 27.15539  ?  131 GLN B CB  1 
ATOM   2913 C CG  . GLN B 1 123 ? 27.17500  -0.04400  36.90100  1.000 26.04586  ?  131 GLN B CG  1 
ATOM   2914 C CD  . GLN B 1 123 ? 27.19400  -1.55300  36.85100  1.000 24.79779  ?  131 GLN B CD  1 
ATOM   2915 O OE1 . GLN B 1 123 ? 27.92300  -2.14900  36.06300  1.000 29.66221  ?  131 GLN B OE1 1 
ATOM   2916 N NE2 . GLN B 1 123 ? 26.39100  -2.18100  37.69800  1.000 22.04310  ?  131 GLN B NE2 1 
ATOM   2917 N N   . LEU B 1 124 ? 27.27700  2.91500   33.38600  1.000 23.33120  ?  132 LEU B N   1 
ATOM   2918 C CA  . LEU B 1 124 ? 27.65800  3.56700   32.13800  1.000 22.06008  ?  132 LEU B CA  1 
ATOM   2919 C C   . LEU B 1 124 ? 28.12400  4.99500   32.38300  1.000 24.68209  ?  132 LEU B C   1 
ATOM   2920 O O   . LEU B 1 124 ? 29.05600  5.46900   31.73000  1.000 19.91145  ?  132 LEU B O   1 
ATOM   2921 C CB  . LEU B 1 124 ? 26.48900  3.54400   31.15500  1.000 20.38269  ?  132 LEU B CB  1 
ATOM   2922 C CG  . LEU B 1 124 ? 26.76500  4.13400   29.77200  1.000 22.46858  ?  132 LEU B CG  1 
ATOM   2923 C CD1 . LEU B 1 124 ? 27.92500  3.42000   29.10500  1.000 23.28294  ?  132 LEU B CD1 1 
ATOM   2924 C CD2 . LEU B 1 124 ? 25.52600  4.06000   28.90700  1.000 29.15971  ?  132 LEU B CD2 1 
ATOM   2925 N N   . LYS B 1 125 ? 27.47500  5.70200   33.30900  1.000 24.38846  ?  133 LYS B N   1 
ATOM   2926 C CA  . LYS B 1 125 ? 27.91800  7.04700   33.66300  1.000 25.63419  ?  133 LYS B CA  1 
ATOM   2927 C C   . LYS B 1 125 ? 29.31900  7.02400   34.25900  1.000 26.27921  ?  133 LYS B C   1 
ATOM   2928 O O   . LYS B 1 125 ? 30.15000  7.88700   33.95000  1.000 26.78128  ?  133 LYS B O   1 
ATOM   2929 C CB  . LYS B 1 125 ? 26.93100  7.68100   34.64100  1.000 25.38575  ?  133 LYS B CB  1 
ATOM   2930 C CG  . LYS B 1 125 ? 27.34000  9.05700   35.13100  1.000 29.44889  ?  133 LYS B CG  1 
ATOM   2931 C CD  . LYS B 1 125 ? 26.36300  9.59200   36.16100  1.000 24.59268  ?  133 LYS B CD  1 
ATOM   2932 C CE  . LYS B 1 125 ? 26.90700  10.84100  36.82700  1.000 28.99801  ?  133 LYS B CE  1 
ATOM   2933 N NZ  . LYS B 1 125 ? 26.01100  11.34800  37.89700  1.000 38.98111  ?  133 LYS B NZ  1 
ATOM   2934 N N   . VAL B 1 126 ? 29.59500  6.04500   35.12200  1.000 22.96610  ?  134 VAL B N   1 
ATOM   2935 C CA  . VAL B 1 126 ? 30.93900  5.90400   35.67800  1.000 29.51308  ?  134 VAL B CA  1 
ATOM   2936 C C   . VAL B 1 126 ? 31.95300  5.66300   34.56600  1.000 29.43557  ?  134 VAL B C   1 
ATOM   2937 O O   . VAL B 1 126 ? 33.03500  6.26600   34.54600  1.000 21.57984  ?  134 VAL B O   1 
ATOM   2938 C CB  . VAL B 1 126 ? 30.97100  4.77400   36.72500  1.000 28.61122  ?  134 VAL B CB  1 
ATOM   2939 C CG1 . VAL B 1 126 ? 32.39800  4.49000   37.15300  1.000 23.83083  ?  134 VAL B CG1 1 
ATOM   2940 C CG2 . VAL B 1 126 ? 30.12000  5.13900   37.92300  1.000 23.38351  ?  134 VAL B CG2 1 
ATOM   2941 N N   . LEU B 1 127 ? 31.61700  4.78000   33.62200  1.000 32.08037  ?  135 LEU B N   1 
ATOM   2942 C CA  . LEU B 1 127 ? 32.51800  4.50700   32.50500  1.000 31.37831  ?  135 LEU B CA  1 
ATOM   2943 C C   . LEU B 1 127 ? 32.74500  5.75200   31.65800  1.000 30.77388  ?  135 LEU B C   1 
ATOM   2944 O O   . LEU B 1 127 ? 33.86600  6.01300   31.21000  1.000 22.96715  ?  135 LEU B O   1 
ATOM   2945 C CB  . LEU B 1 127 ? 31.96100  3.37500   31.64600  1.000 24.81351  ?  135 LEU B CB  1 
ATOM   2946 C CG  . LEU B 1 127 ? 32.07300  1.96600   32.22200  1.000 32.19971  ?  135 LEU B CG  1 
ATOM   2947 C CD1 . LEU B 1 127 ? 31.51100  0.94900   31.24700  1.000 24.13202  ?  135 LEU B CD1 1 
ATOM   2948 C CD2 . LEU B 1 127 ? 33.51400  1.64900   32.56400  1.000 26.37359  ?  135 LEU B CD2 1 
ATOM   2949 N N   . ILE B 1 128 ? 31.68700  6.52700   31.42200  1.000 29.16730  ?  136 ILE B N   1 
ATOM   2950 C CA  . ILE B 1 128 ? 31.80200  7.74200   30.62400  1.000 33.00357  ?  136 ILE B CA  1 
ATOM   2951 C C   . ILE B 1 128 ? 32.70400  8.75400   31.31500  1.000 30.22371  ?  136 ILE B C   1 
ATOM   2952 O O   . ILE B 1 128 ? 33.55700  9.38400   30.68100  1.000 25.40974  ?  136 ILE B O   1 
ATOM   2953 C CB  . ILE B 1 128 ? 30.40300  8.32300   30.35200  1.000 31.54285  ?  136 ILE B CB  1 
ATOM   2954 C CG1 . ILE B 1 128 ? 29.67000  7.48400   29.30600  1.000 33.05960  ?  136 ILE B CG1 1 
ATOM   2955 C CG2 . ILE B 1 128 ? 30.49700  9.76600   29.89700  1.000 27.82030  ?  136 ILE B CG2 1 
ATOM   2956 C CD1 . ILE B 1 128 ? 28.29700  8.00400   28.97100  1.000 30.91307  ?  136 ILE B CD1 1 
ATOM   2957 N N   . GLU B 1 129 ? 32.53600  8.92500   32.62200  1.000 27.44268  ?  137 GLU B N   1 
ATOM   2958 C CA  . GLU B 1 129 ? 33.27800  9.95100   33.33700  1.000 25.54413  ?  137 GLU B CA  1 
ATOM   2959 C C   . GLU B 1 129 ? 34.72600  9.57700   33.62000  1.000 25.49015  ?  137 GLU B C   1 
ATOM   2960 O O   . GLU B 1 129 ? 35.59000  10.45900  33.60100  1.000 29.77286  ?  137 GLU B O   1 
ATOM   2961 C CB  . GLU B 1 129 ? 32.57300  10.28800  34.65200  1.000 24.39133  ?  137 GLU B CB  1 
ATOM   2962 C CG  . GLU B 1 129 ? 31.28900  11.07100  34.46800  1.000 27.06311  ?  137 GLU B CG  1 
ATOM   2963 C CD  . GLU B 1 129 ? 30.58800  11.36100  35.77300  1.000 25.25092  ?  137 GLU B CD  1 
ATOM   2964 O OE1 . GLU B 1 129 ? 31.02500  10.83300  36.81400  1.000 28.19295  ?  137 GLU B OE1 1 
ATOM   2965 O OE2 . GLU B 1 129 ? 29.60400  12.12500  35.76000  1.000 26.78863  -1 137 GLU B OE2 1 
ATOM   2966 N N   . HIS B 1 130 ? 35.03000  8.30300   33.87900  1.000 30.53920  ?  138 HIS B N   1 
ATOM   2967 C CA  . HIS B 1 130 ? 36.33700  7.96400   34.43100  1.000 31.94466  ?  138 HIS B CA  1 
ATOM   2968 C C   . HIS B 1 130 ? 37.12200  6.89800   33.67700  1.000 31.74354  ?  138 HIS B C   1 
ATOM   2969 O O   . HIS B 1 130 ? 38.31400  6.74100   33.96300  1.000 37.11395  ?  138 HIS B O   1 
ATOM   2970 C CB  . HIS B 1 130 ? 36.19300  7.52800   35.89600  1.000 27.20043  ?  138 HIS B CB  1 
ATOM   2971 C CG  . HIS B 1 130 ? 35.70000  8.61700   36.79700  1.000 25.57104  ?  138 HIS B CG  1 
ATOM   2972 N ND1 . HIS B 1 130 ? 36.45000  9.73200   37.09500  1.000 15.10359  ?  138 HIS B ND1 1 
ATOM   2973 C CD2 . HIS B 1 130 ? 34.52400  8.77000   37.44900  1.000 30.24142  ?  138 HIS B CD2 1 
ATOM   2974 C CE1 . HIS B 1 130 ? 35.76200  10.52100  37.89900  1.000 18.91978  ?  138 HIS B CE1 1 
ATOM   2975 N NE2 . HIS B 1 130 ? 34.58900  9.96100   38.12900  1.000 21.33922  ?  138 HIS B NE2 1 
ATOM   2976 N N   . ALA B 1 131 ? 36.52300  6.16700   32.74500  1.000 29.22597  ?  139 ALA B N   1 
ATOM   2977 C CA  . ALA B 1 131 ? 37.29600  5.19700   31.98500  1.000 27.75427  ?  139 ALA B CA  1 
ATOM   2978 C C   . ALA B 1 131 ? 38.08000  5.89100   30.87600  1.000 30.74954  ?  139 ALA B C   1 
ATOM   2979 O O   . ALA B 1 131 ? 37.78000  7.02000   30.48400  1.000 33.23153  ?  139 ALA B O   1 
ATOM   2980 C CB  . ALA B 1 131 ? 36.38900  4.12200   31.39200  1.000 27.68364  ?  139 ALA B CB  1 
ATOM   2981 N N   . ARG B 1 132 ? 39.11200  5.21100   30.38200  1.000 26.74439  ?  140 ARG B N   1 
ATOM   2982 C CA  . ARG B 1 132 ? 39.86300  5.73800   29.24900  1.000 27.24906  ?  140 ARG B CA  1 
ATOM   2983 C C   . ARG B 1 132 ? 39.17500  5.38800   27.93600  1.000 34.96451  ?  140 ARG B C   1 
ATOM   2984 O O   . ARG B 1 132 ? 38.67800  6.26900   27.23000  1.000 46.78919  ?  140 ARG B O   1 
ATOM   2985 C CB  . ARG B 1 132 ? 41.29200  5.19800   29.24800  1.000 25.28499  ?  140 ARG B CB  1 
ATOM   2986 C CG  . ARG B 1 132 ? 42.24700  5.94600   30.15200  1.000 32.59428  ?  140 ARG B CG  1 
ATOM   2987 C CD  . ARG B 1 132 ? 43.67600  5.51100   29.90500  1.000 24.67834  ?  140 ARG B CD  1 
ATOM   2988 N NE  . ARG B 1 132 ? 44.63600  6.38900   30.56100  1.000 32.67680  ?  140 ARG B NE  1 
ATOM   2989 C CZ  . ARG B 1 132 ? 45.89900  6.52700   30.18600  1.000 38.57456  ?  140 ARG B CZ  1 
ATOM   2990 N NH1 . ARG B 1 132 ? 46.38800  5.86300   29.15300  1.000 37.41204  ?  140 ARG B NH1 1 
ATOM   2991 N NH2 . ARG B 1 132 ? 46.69200  7.35000   30.86600  1.000 44.62494  ?  140 ARG B NH2 1 
ATOM   2992 N N   . ASP B 1 133 ? 39.12800  4.10000   27.61600  1.000 31.09527  ?  141 ASP B N   1 
ATOM   2993 C CA  . ASP B 1 133 ? 38.43400  3.59600   26.44200  1.000 26.04587  ?  141 ASP B CA  1 
ATOM   2994 C C   . ASP B 1 133 ? 37.49200  2.48000   26.86400  1.000 32.28173  ?  141 ASP B C   1 
ATOM   2995 O O   . ASP B 1 133 ? 37.83900  1.64400   27.70100  1.000 32.19252  ?  141 ASP B O   1 
ATOM   2996 C CB  . ASP B 1 133 ? 39.41300  3.07200   25.38900  1.000 23.69671  ?  141 ASP B CB  1 
ATOM   2997 C CG  . ASP B 1 133 ? 40.17200  4.17900   24.68500  1.000 38.09323  ?  141 ASP B CG  1 
ATOM   2998 O OD1 . ASP B 1 133 ? 39.82200  5.36100   24.87300  1.000 45.50056  ?  141 ASP B OD1 1 
ATOM   2999 O OD2 . ASP B 1 133 ? 41.11500  3.86500   23.93200  1.000 40.88231  -1 141 ASP B OD2 1 
ATOM   3000 N N   . PHE B 1 134 ? 36.29800  2.47300   26.28200  1.000 27.40636  ?  142 PHE B N   1 
ATOM   3001 C CA  . PHE B 1 134 ? 35.31100  1.45800   26.60500  1.000 20.56714  ?  142 PHE B CA  1 
ATOM   3002 C C   . PHE B 1 134 ? 34.37600  1.29000   25.42000  1.000 28.63259  ?  142 PHE B C   1 
ATOM   3003 O O   . PHE B 1 134 ? 34.33600  2.12000   24.51100  1.000 34.41842  ?  142 PHE B O   1 
ATOM   3004 C CB  . PHE B 1 134 ? 34.52600  1.81400   27.87400  1.000 22.66762  ?  142 PHE B CB  1 
ATOM   3005 C CG  . PHE B 1 134 ? 33.57300  2.96000   27.69900  1.000 30.80856  ?  142 PHE B CG  1 
ATOM   3006 C CD1 . PHE B 1 134 ? 34.00700  4.26500   27.84300  1.000 37.17892  ?  142 PHE B CD1 1 
ATOM   3007 C CD2 . PHE B 1 134 ? 32.24100  2.73300   27.40200  1.000 29.30647  ?  142 PHE B CD2 1 
ATOM   3008 C CE1 . PHE B 1 134 ? 33.13500  5.31900   27.68500  1.000 32.32757  ?  142 PHE B CE1 1 
ATOM   3009 C CE2 . PHE B 1 134 ? 31.36600  3.78300   27.24200  1.000 32.14205  ?  142 PHE B CE2 1 
ATOM   3010 C CZ  . PHE B 1 134 ? 31.81400  5.07700   27.38400  1.000 34.10897  ?  142 PHE B CZ  1 
ATOM   3011 N N   . GLU B 1 135 ? 33.63000  0.19000   25.43800  1.000 34.50726  ?  143 GLU B N   1 
ATOM   3012 C CA  . GLU B 1 135 ? 32.63100  -0.08100  24.42000  1.000 32.71050  ?  143 GLU B CA  1 
ATOM   3013 C C   . GLU B 1 135 ? 31.56500  -0.97900  25.02500  1.000 32.64398  ?  143 GLU B C   1 
ATOM   3014 O O   . GLU B 1 135 ? 31.86200  -1.83600  25.85800  1.000 30.17691  ?  143 GLU B O   1 
ATOM   3015 C CB  . GLU B 1 135 ? 33.25200  -0.73400  23.18000  1.000 28.13499  ?  143 GLU B CB  1 
ATOM   3016 C CG  . GLU B 1 135 ? 32.23800  -1.27800  22.19800  1.000 37.17487  ?  143 GLU B CG  1 
ATOM   3017 C CD  . GLU B 1 135 ? 32.86900  -1.83000  20.94700  1.000 43.95864  ?  143 GLU B CD  1 
ATOM   3018 O OE1 . GLU B 1 135 ? 34.11200  -1.89400  20.88500  1.000 38.32918  ?  143 GLU B OE1 1 
ATOM   3019 O OE2 . GLU B 1 135 ? 32.11400  -2.20300  20.02800  1.000 45.06719  -1 143 GLU B OE2 1 
ATOM   3020 N N   . THR B 1 136 ? 30.32100  -0.76700  24.61000  1.000 35.24861  ?  144 THR B N   1 
ATOM   3021 C CA  . THR B 1 136 ? 29.19800  -1.56700  25.06700  1.000 34.69851  ?  144 THR B CA  1 
ATOM   3022 C C   . THR B 1 136 ? 28.59700  -2.34400  23.90400  1.000 37.94406  ?  144 THR B C   1 
ATOM   3023 O O   . THR B 1 136 ? 28.66200  -1.91700  22.74900  1.000 34.04980  ?  144 THR B O   1 
ATOM   3024 C CB  . THR B 1 136 ? 28.11900  -0.69400  25.71100  1.000 33.98800  ?  144 THR B CB  1 
ATOM   3025 O OG1 . THR B 1 136 ? 27.56600  0.18600   24.72600  1.000 35.54888  ?  144 THR B OG1 1 
ATOM   3026 C CG2 . THR B 1 136 ? 28.70500  0.12400   26.84300  1.000 31.58448  ?  144 THR B CG2 1 
ATOM   3027 N N   . ASP B 1 137 ? 28.01800  -3.49700  24.22400  1.000 37.54317  ?  145 ASP B N   1 
ATOM   3028 C CA  . ASP B 1 137 ? 27.30600  -4.28300  23.23300  1.000 36.76122  ?  145 ASP B CA  1 
ATOM   3029 C C   . ASP B 1 137 ? 25.95700  -3.63800  22.92300  1.000 41.34034  ?  145 ASP B C   1 
ATOM   3030 O O   . ASP B 1 137 ? 25.53800  -2.66600  23.55600  1.000 44.91167  ?  145 ASP B O   1 
ATOM   3031 C CB  . ASP B 1 137 ? 27.11200  -5.71600  23.72400  1.000 49.22657  ?  145 ASP B CB  1 
ATOM   3032 C CG  . ASP B 1 137 ? 27.30600  -6.74200  22.62700  1.000 53.15449  ?  145 ASP B CG  1 
ATOM   3033 O OD1 . ASP B 1 137 ? 26.90800  -6.47600  21.47500  1.000 45.79389  ?  145 ASP B OD1 1 
ATOM   3034 O OD2 . ASP B 1 137 ? 27.85800  -7.82200  22.92000  1.000 64.09195  -1 145 ASP B OD2 1 
ATOM   3035 N N   . TRP B 1 138 ? 25.27300  -4.19700  21.93100  1.000 39.91198  ?  146 TRP B N   1 
ATOM   3036 C CA  . TRP B 1 138 ? 23.98900  -3.65900  21.50900  1.000 46.09827  ?  146 TRP B CA  1 
ATOM   3037 C C   . TRP B 1 138 ? 22.95700  -3.79900  22.62000  1.000 49.64506  ?  146 TRP B C   1 
ATOM   3038 O O   . TRP B 1 138 ? 22.86900  -4.83900  23.27900  1.000 44.81354  ?  146 TRP B O   1 
ATOM   3039 C CB  . TRP B 1 138 ? 23.50800  -4.37300  20.24900  1.000 48.18732  ?  146 TRP B CB  1 
ATOM   3040 C CG  . TRP B 1 138 ? 24.22500  -3.94100  19.01900  1.000 39.91814  ?  146 TRP B CG  1 
ATOM   3041 C CD1 . TRP B 1 138 ? 25.13300  -4.66200  18.30800  1.000 35.19112  ?  146 TRP B CD1 1 
ATOM   3042 C CD2 . TRP B 1 138 ? 24.09800  -2.68300  18.35200  1.000 36.89978  ?  146 TRP B CD2 1 
ATOM   3043 N NE1 . TRP B 1 138 ? 25.58100  -3.93200  17.23700  1.000 41.29143  ?  146 TRP B NE1 1 
ATOM   3044 C CE2 . TRP B 1 138 ? 24.96000  -2.71200  17.24200  1.000 40.64749  ?  146 TRP B CE2 1 
ATOM   3045 C CE3 . TRP B 1 138 ? 23.33800  -1.53400  18.58600  1.000 39.88017  ?  146 TRP B CE3 1 
ATOM   3046 C CZ2 . TRP B 1 138 ? 25.08300  -1.63900  16.36700  1.000 40.28003  ?  146 TRP B CZ2 1 
ATOM   3047 C CZ3 . TRP B 1 138 ? 23.46300  -0.47100  17.71700  1.000 38.63260  ?  146 TRP B CZ3 1 
ATOM   3048 C CH2 . TRP B 1 138 ? 24.32700  -0.52900  16.62300  1.000 34.27783  ?  146 TRP B CH2 1 
ATOM   3049 N N   . SER B 1 139 ? 22.17600  -2.74300  22.82500  1.000 50.10398  ?  147 SER B N   1 
ATOM   3050 C CA  . SER B 1 139 ? 21.11200  -2.72300  23.81400  1.000 48.85930  ?  147 SER B CA  1 
ATOM   3051 C C   . SER B 1 139 ? 19.82400  -2.24700  23.16100  1.000 50.09284  ?  147 SER B C   1 
ATOM   3052 O O   . SER B 1 139 ? 19.84400  -1.42700  22.24200  1.000 48.99999  ?  147 SER B O   1 
ATOM   3053 C CB  . SER B 1 139 ? 21.46800  -1.81400  24.99300  1.000 49.93686  ?  147 SER B CB  1 
ATOM   3054 O OG  . SER B 1 139 ? 20.31400  -1.18300  25.51800  1.000 63.50300  ?  147 SER B OG  1 
ATOM   3055 N N   . ALA B 1 140 ? 18.70100  -2.77000  23.63900  1.000 55.03888  ?  148 ALA B N   1 
ATOM   3056 C CA  . ALA B 1 140 ? 17.40500  -2.39000  23.09800  1.000 50.90139  ?  148 ALA B CA  1 
ATOM   3057 C C   . ALA B 1 140 ? 17.05100  -0.96700  23.50800  1.000 57.59446  ?  148 ALA B C   1 
ATOM   3058 O O   . ALA B 1 140 ? 17.35600  -0.53000  24.62100  1.000 58.45525  ?  148 ALA B O   1 
ATOM   3059 C CB  . ALA B 1 140 ? 16.32400  -3.36000  23.57200  1.000 54.40280  ?  148 ALA B CB  1 
ATOM   3060 N N   . GLY B 1 141 ? 16.40600  -0.24400  22.59800  1.000 57.24885  ?  149 GLY B N   1 
ATOM   3061 C CA  . GLY B 1 141 ? 16.02600  1.13000   22.85000  1.000 62.78333  ?  149 GLY B CA  1 
ATOM   3062 C C   . GLY B 1 141 ? 14.59700  1.44900   22.46200  1.000 71.08730  ?  149 GLY B C   1 
ATOM   3063 O O   . GLY B 1 141 ? 13.82400  0.55300   22.11000  1.000 62.10732  ?  149 GLY B O   1 
ATOM   3064 N N   . ARG B 1 142 ? 14.23800  2.72800   22.52000  1.000 76.16452  ?  150 ARG B N   1 
ATOM   3065 C CA  . ARG B 1 142 ? 12.88900  3.16400   22.19900  1.000 70.21075  ?  150 ARG B CA  1 
ATOM   3066 C C   . ARG B 1 142 ? 12.61000  3.02700   20.70800  1.000 69.32736  ?  150 ARG B C   1 
ATOM   3067 O O   . ARG B 1 142 ? 13.49100  3.22600   19.86800  1.000 73.94396  ?  150 ARG B O   1 
ATOM   3068 C CB  . ARG B 1 142 ? 12.68100  4.61900   22.62100  1.000 65.89502  ?  150 ARG B CB  1 
ATOM   3069 C CG  . ARG B 1 142 ? 12.82600  4.87000   24.11000  1.000 68.96447  ?  150 ARG B CG  1 
ATOM   3070 C CD  . ARG B 1 142 ? 12.12900  6.16500   24.51900  1.000 63.53513  ?  150 ARG B CD  1 
ATOM   3071 N NE  . ARG B 1 142 ? 12.58100  6.71800   25.79400  1.000 74.62587  ?  150 ARG B NE  1 
ATOM   3072 C CZ  . ARG B 1 142 ? 12.66500  6.05900   26.94400  1.000 80.96427  ?  150 ARG B CZ  1 
ATOM   3073 N NH1 . ARG B 1 142 ? 12.25200  4.80700   27.06500  1.000 72.17177  ?  150 ARG B NH1 1 
ATOM   3074 N NH2 . ARG B 1 142 ? 13.15400  6.68200   28.01300  1.000 72.78530  ?  150 ARG B NH2 1 
ATOM   3075 N N   . GLY B 1 143 ? 11.36300  2.69300   20.38600  1.000 69.74073  ?  151 GLY B N   1 
ATOM   3076 C CA  . GLY B 1 143 ? 10.92800  2.65200   19.00200  1.000 67.35618  ?  151 GLY B CA  1 
ATOM   3077 C C   . GLY B 1 143 ? 11.57100  1.58100   18.15300  1.000 62.83766  ?  151 GLY B C   1 
ATOM   3078 O O   . GLY B 1 143 ? 11.91500  1.84500   16.99800  1.000 57.94041  ?  151 GLY B O   1 
ATOM   3079 N N   . GLU B 1 144 ? 11.73800  0.37400   18.69400  1.000 67.10870  ?  152 GLU B N   1 
ATOM   3080 C CA  . GLU B 1 144 ? 12.30000  -0.77000  17.97900  1.000 63.68456  ?  152 GLU B CA  1 
ATOM   3081 C C   . GLU B 1 144 ? 13.72700  -0.52000  17.50200  1.000 62.19811  ?  152 GLU B C   1 
ATOM   3082 O O   . GLU B 1 144 ? 14.20500  -1.19600  16.58600  1.000 56.53232  ?  152 GLU B O   1 
ATOM   3083 C CB  . GLU B 1 144 ? 11.41600  -1.18400  16.79400  1.000 66.23977  ?  152 GLU B CB  1 
ATOM   3084 C CG  . GLU B 1 144 ? 10.07900  -1.80400  17.18200  1.000 74.63825  ?  152 GLU B CG  1 
ATOM   3085 C CD  . GLU B 1 144 ? 9.03900   -0.77400  17.57600  1.000 67.28680  ?  152 GLU B CD  1 
ATOM   3086 O OE1 . GLU B 1 144 ? 8.62100   0.01500   16.70500  1.000 67.33008  ?  152 GLU B OE1 1 
ATOM   3087 O OE2 . GLU B 1 144 ? 8.63500   -0.75800  18.75700  1.000 65.15678  -1 152 GLU B OE2 1 
ATOM   3088 N N   . THR B 1 145 ? 14.42000  0.44000   18.10300  1.000 55.97435  ?  153 THR B N   1 
ATOM   3089 C CA  . THR B 1 145 ? 15.81100  0.70300   17.77200  1.000 52.23399  ?  153 THR B CA  1 
ATOM   3090 C C   . THR B 1 145 ? 16.73900  0.04600   18.78600  1.000 58.19415  ?  153 THR B C   1 
ATOM   3091 O O   . THR B 1 145 ? 16.30900  -0.48700  19.81000  1.000 60.18392  ?  153 THR B O   1 
ATOM   3092 C CB  . THR B 1 145 ? 16.09000  2.20600   17.71600  1.000 55.53619  ?  153 THR B CB  1 
ATOM   3093 O OG1 . THR B 1 145 ? 16.32300  2.70300   19.04000  1.000 58.10874  ?  153 THR B OG1 1 
ATOM   3094 C CG2 . THR B 1 145 ? 14.93000  2.94700   17.08900  1.000 61.60910  ?  153 THR B CG2 1 
ATOM   3095 N N   . PHE B 1 146 ? 18.03200  0.08500   18.47500  1.000 55.37835  ?  154 PHE B N   1 
ATOM   3096 C CA  . PHE B 1 146 ? 19.07700  -0.43600  19.34100  1.000 49.67227  ?  154 PHE B CA  1 
ATOM   3097 C C   . PHE B 1 146 ? 20.17700  0.60600   19.46500  1.000 48.76899  ?  154 PHE B C   1 
ATOM   3098 O O   . PHE B 1 146 ? 20.41200  1.38800   18.54500  1.000 52.18694  ?  154 PHE B O   1 
ATOM   3099 C CB  . PHE B 1 146 ? 19.64500  -1.74800  18.79900  1.000 44.93276  ?  154 PHE B CB  1 
ATOM   3100 C CG  . PHE B 1 146 ? 18.60000  -2.78300  18.51300  1.000 50.73001  ?  154 PHE B CG  1 
ATOM   3101 C CD1 . PHE B 1 146 ? 17.91000  -3.39300  19.54200  1.000 55.70091  ?  154 PHE B CD1 1 
ATOM   3102 C CD2 . PHE B 1 146 ? 18.30000  -3.13800  17.21200  1.000 56.87431  ?  154 PHE B CD2 1 
ATOM   3103 C CE1 . PHE B 1 146 ? 16.94600  -4.34100  19.28000  1.000 55.59936  ?  154 PHE B CE1 1 
ATOM   3104 C CE2 . PHE B 1 146 ? 17.33800  -4.08600  16.94400  1.000 52.14209  ?  154 PHE B CE2 1 
ATOM   3105 C CZ  . PHE B 1 146 ? 16.66100  -4.68800  17.97900  1.000 50.17412  ?  154 PHE B CZ  1 
ATOM   3106 N N   . GLN B 1 147 ? 20.84600  0.62100   20.61300  1.000 46.78219  ?  155 GLN B N   1 
ATOM   3107 C CA  . GLN B 1 147 ? 21.83100  1.65200   20.89600  1.000 42.61909  ?  155 GLN B CA  1 
ATOM   3108 C C   . GLN B 1 147 ? 23.10200  1.02700   21.45200  1.000 46.41975  ?  155 GLN B C   1 
ATOM   3109 O O   . GLN B 1 147 ? 23.06400  0.00000   22.13300  1.000 43.51261  ?  155 GLN B O   1 
ATOM   3110 C CB  . GLN B 1 147 ? 21.28500  2.69200   21.88400  1.000 39.53243  ?  155 GLN B CB  1 
ATOM   3111 C CG  . GLN B 1 147 ? 21.00000  2.14700   23.27300  1.000 46.64753  ?  155 GLN B CG  1 
ATOM   3112 C CD  . GLN B 1 147 ? 20.35000  3.17000   24.18200  1.000 59.63856  ?  155 GLN B CD  1 
ATOM   3113 O OE1 . GLN B 1 147 ? 19.48400  3.93300   23.75800  1.000 56.62365  ?  155 GLN B OE1 1 
ATOM   3114 N NE2 . GLN B 1 147 ? 20.76900  3.19300   25.44000  1.000 61.43330  ?  155 GLN B NE2 1 
ATOM   3115 N N   . ARG B 1 148 ? 24.23200  1.65800   21.13900  1.000 39.81587  ?  156 ARG B N   1 
ATOM   3116 C CA  . ARG B 1 148 ? 25.49600  1.31700   21.77400  1.000 34.84415  ?  156 ARG B CA  1 
ATOM   3117 C C   . ARG B 1 148 ? 26.39700  2.54200   21.75500  1.000 37.51719  ?  156 ARG B C   1 
ATOM   3118 O O   . ARG B 1 148 ? 26.13400  3.51800   21.05100  1.000 38.54561  ?  156 ARG B O   1 
ATOM   3119 C CB  . ARG B 1 148 ? 26.17800  0.11700   21.10300  1.000 33.96217  ?  156 ARG B CB  1 
ATOM   3120 C CG  . ARG B 1 148 ? 26.72600  0.36800   19.71500  1.000 36.26341  ?  156 ARG B CG  1 
ATOM   3121 C CD  . ARG B 1 148 ? 27.47100  -0.86100  19.22300  1.000 33.97741  ?  156 ARG B CD  1 
ATOM   3122 N NE  . ARG B 1 148 ? 27.97800  -0.70600  17.86600  1.000 35.32820  ?  156 ARG B NE  1 
ATOM   3123 C CZ  . ARG B 1 148 ? 28.65500  -1.63800  17.21200  1.000 40.55035  ?  156 ARG B CZ  1 
ATOM   3124 N NH1 . ARG B 1 148 ? 28.93400  -2.80600  17.76600  1.000 36.26420  ?  156 ARG B NH1 1 
ATOM   3125 N NH2 . ARG B 1 148 ? 29.06300  -1.39400  15.97100  1.000 41.33288  ?  156 ARG B NH2 1 
ATOM   3126 N N   . VAL B 1 149 ? 27.45100  2.49400   22.56200  1.000 30.91968  ?  157 VAL B N   1 
ATOM   3127 C CA  . VAL B 1 149 ? 28.34700  3.63000   22.73700  1.000 34.82216  ?  157 VAL B CA  1 
ATOM   3128 C C   . VAL B 1 149 ? 29.76300  3.11400   22.95300  1.000 39.52996  ?  157 VAL B C   1 
ATOM   3129 O O   . VAL B 1 149 ? 29.96600  2.07300   23.58600  1.000 37.98827  ?  157 VAL B O   1 
ATOM   3130 C CB  . VAL B 1 149 ? 27.88500  4.52700   23.90800  1.000 34.37762  ?  157 VAL B CB  1 
ATOM   3131 C CG1 . VAL B 1 149 ? 27.84400  3.74600   25.20800  1.000 26.95908  ?  157 VAL B CG1 1 
ATOM   3132 C CG2 . VAL B 1 149 ? 28.76800  5.74900   24.03800  1.000 38.02571  ?  157 VAL B CG2 1 
ATOM   3133 N N   . TRP B 1 150 ? 30.74200  3.83100   22.40500  1.000 35.53023  ?  158 TRP B N   1 
ATOM   3134 C CA  . TRP B 1 150 ? 32.13900  3.47900   22.61600  1.000 34.26441  ?  158 TRP B CA  1 
ATOM   3135 C C   . TRP B 1 150 ? 33.00200  4.72300   22.48500  1.000 35.94717  ?  158 TRP B C   1 
ATOM   3136 O O   . TRP B 1 150 ? 32.70400  5.61600   21.69600  1.000 40.30353  ?  158 TRP B O   1 
ATOM   3137 C CB  . TRP B 1 150 ? 32.61300  2.40300   21.63100  1.000 29.66830  ?  158 TRP B CB  1 
ATOM   3138 C CG  . TRP B 1 150 ? 32.92200  2.89800   20.24800  1.000 34.25262  ?  158 TRP B CG  1 
ATOM   3139 C CD1 . TRP B 1 150 ? 34.12800  3.33500   19.78500  1.000 33.71997  ?  158 TRP B CD1 1 
ATOM   3140 C CD2 . TRP B 1 150 ? 32.01700  2.97900   19.14100  1.000 36.57815  ?  158 TRP B CD2 1 
ATOM   3141 N NE1 . TRP B 1 150 ? 34.02700  3.69800   18.46700  1.000 32.94250  ?  158 TRP B NE1 1 
ATOM   3142 C CE2 . TRP B 1 150 ? 32.74000  3.48900   18.04700  1.000 31.28027  ?  158 TRP B CE2 1 
ATOM   3143 C CE3 . TRP B 1 150 ? 30.66300  2.67900   18.97100  1.000 38.80098  ?  158 TRP B CE3 1 
ATOM   3144 C CZ2 . TRP B 1 150 ? 32.15900  3.69900   16.80200  1.000 28.16663  ?  158 TRP B CZ2 1 
ATOM   3145 C CZ3 . TRP B 1 150 ? 30.08800  2.89100   17.73400  1.000 33.36359  ?  158 TRP B CZ3 1 
ATOM   3146 C CH2 . TRP B 1 150 ? 30.83400  3.39700   16.66700  1.000 29.16928  ?  158 TRP B CH2 1 
ATOM   3147 N N   . ARG B 1 151 ? 34.08900  4.76700   23.24600  1.000 33.21594  ?  159 ARG B N   1 
ATOM   3148 C CA  . ARG B 1 151 ? 35.01900  5.88400   23.18600  1.000 32.97162  ?  159 ARG B CA  1 
ATOM   3149 C C   . ARG B 1 151 ? 36.38900  5.41400   22.72700  1.000 35.18243  ?  159 ARG B C   1 
ATOM   3150 O O   . ARG B 1 151 ? 36.92900  4.43400   23.24900  1.000 35.22693  ?  159 ARG B O   1 
ATOM   3151 C CB  . ARG B 1 151 ? 35.15000  6.58300   24.53700  1.000 35.68286  ?  159 ARG B CB  1 
ATOM   3152 C CG  . ARG B 1 151 ? 36.18400  7.69300   24.53800  1.000 32.62485  ?  159 ARG B CG  1 
ATOM   3153 C CD  . ARG B 1 151 ? 35.98500  8.61900   25.70700  1.000 31.66505  ?  159 ARG B CD  1 
ATOM   3154 N NE  . ARG B 1 151 ? 35.97200  7.88800   26.96600  1.000 32.78579  ?  159 ARG B NE  1 
ATOM   3155 C CZ  . ARG B 1 151 ? 35.39200  8.32600   28.07200  1.000 32.99589  ?  159 ARG B CZ  1 
ATOM   3156 N NH1 . ARG B 1 151 ? 34.78800  9.50000   28.11400  1.000 36.61418  ?  159 ARG B NH1 1 
ATOM   3157 N NH2 . ARG B 1 151 ? 35.41000  7.56400   29.15900  1.000 30.56434  ?  159 ARG B NH2 1 
ATOM   3158 N N   . LYS B 1 152 ? 36.94700  6.12300   21.75000  1.000 35.10956  ?  160 LYS B N   1 
ATOM   3159 C CA  . LYS B 1 152 ? 38.31200  5.90000   21.28800  1.000 36.20650  ?  160 LYS B CA  1 
ATOM   3160 C C   . LYS B 1 152 ? 39.06700  7.21000   21.44400  1.000 44.31409  ?  160 LYS B C   1 
ATOM   3161 O O   . LYS B 1 152 ? 38.67000  8.23200   20.87200  1.000 49.40495  ?  160 LYS B O   1 
ATOM   3162 C CB  . LYS B 1 152 ? 38.33900  5.41700   19.83900  1.000 37.97102  ?  160 LYS B CB  1 
ATOM   3163 C CG  . LYS B 1 152 ? 39.63700  4.74400   19.43500  1.000 33.38454  ?  160 LYS B CG  1 
ATOM   3164 C CD  . LYS B 1 152 ? 39.80100  4.73300   17.92700  1.000 50.91378  ?  160 LYS B CD  1 
ATOM   3165 C CE  . LYS B 1 152 ? 41.26700  4.73800   17.53000  1.000 63.01980  ?  160 LYS B CE  1 
ATOM   3166 N NZ  . LYS B 1 152 ? 41.52100  3.86100   16.35400  1.000 65.50528  ?  160 LYS B NZ  1 
ATOM   3167 N N   . GLY B 1 153 ? 40.14300  7.18200   22.22400  1.000 40.26352  ?  161 GLY B N   1 
ATOM   3168 C CA  . GLY B 1 153 ? 40.93600  8.36700   22.47200  1.000 44.82180  ?  161 GLY B CA  1 
ATOM   3169 C C   . GLY B 1 153 ? 40.13400  9.51200   23.05000  1.000 39.06373  ?  161 GLY B C   1 
ATOM   3170 O O   . GLY B 1 153 ? 39.66700  9.44700   24.19000  1.000 42.41459  ?  161 GLY B O   1 
ATOM   3171 N N   . ASP B 1 154 ? 39.96300  10.56900  22.26200  1.000 42.71090  ?  162 ASP B N   1 
ATOM   3172 C CA  . ASP B 1 154 ? 39.23800  11.75600  22.68500  1.000 44.67136  ?  162 ASP B CA  1 
ATOM   3173 C C   . ASP B 1 154 ? 37.88300  11.88800  22.00300  1.000 46.07106  ?  162 ASP B C   1 
ATOM   3174 O O   . ASP B 1 154 ? 37.28900  12.96900  22.03400  1.000 47.29782  ?  162 ASP B O   1 
ATOM   3175 C CB  . ASP B 1 154 ? 40.08700  13.00200  22.42200  1.000 47.28858  ?  162 ASP B CB  1 
ATOM   3176 C CG  . ASP B 1 154 ? 39.70200  14.17000  23.30500  1.000 54.08250  ?  162 ASP B CG  1 
ATOM   3177 O OD1 . ASP B 1 154 ? 40.19500  14.23800  24.44900  1.000 54.66336  ?  162 ASP B OD1 1 
ATOM   3178 O OD2 . ASP B 1 154 ? 38.90900  15.02100  22.85600  1.000 55.23923  -1 162 ASP B OD2 1 
ATOM   3179 N N   . THR B 1 155 ? 37.37700  10.82100  21.38900  1.000 42.32147  ?  163 THR B N   1 
ATOM   3180 C CA  . THR B 1 155 ? 36.10600  10.88300  20.68200  1.000 43.55676  ?  163 THR B CA  1 
ATOM   3181 C C   . THR B 1 155 ? 35.16700  9.80200   21.19500  1.000 43.04793  ?  163 THR B C   1 
ATOM   3182 O O   . THR B 1 155 ? 35.54700  8.63100   21.28600  1.000 40.67410  ?  163 THR B O   1 
ATOM   3183 C CB  . THR B 1 155 ? 36.30700  10.73800  19.17100  1.000 44.77442  ?  163 THR B CB  1 
ATOM   3184 O OG1 . THR B 1 155 ? 37.46000  11.48700  18.77200  1.000 47.99346  ?  163 THR B OG1 1 
ATOM   3185 C CG2 . THR B 1 155 ? 35.09500  11.25900  18.42300  1.000 37.66705  ?  163 THR B CG2 1 
ATOM   3186 N N   . LEU B 1 156 ? 33.93800  10.19900  21.51200  1.000 40.14729  ?  164 LEU B N   1 
ATOM   3187 C CA  . LEU B 1 156 ? 32.89800  9.28400   21.95800  1.000 38.90893  ?  164 LEU B CA  1 
ATOM   3188 C C   . LEU B 1 156 ? 31.85200  9.14300   20.86000  1.000 38.65691  ?  164 LEU B C   1 
ATOM   3189 O O   . LEU B 1 156 ? 31.31100  10.14400  20.38200  1.000 41.62844  ?  164 LEU B O   1 
ATOM   3190 C CB  . LEU B 1 156 ? 32.24900  9.79000   23.24700  1.000 45.62081  ?  164 LEU B CB  1 
ATOM   3191 C CG  . LEU B 1 156 ? 31.11900  8.95600   23.85100  1.000 42.81067  ?  164 LEU B CG  1 
ATOM   3192 C CD1 . LEU B 1 156 ? 31.68700  7.74900   24.56200  1.000 43.04556  ?  164 LEU B CD1 1 
ATOM   3193 C CD2 . LEU B 1 156 ? 30.28600  9.79000   24.80200  1.000 42.80664  ?  164 LEU B CD2 1 
ATOM   3194 N N   . PHE B 1 157 ? 31.57100  7.90400   20.46800  1.000 36.59507  ?  165 PHE B N   1 
ATOM   3195 C CA  . PHE B 1 157 ? 30.63400  7.58100   19.40200  1.000 33.95933  ?  165 PHE B CA  1 
ATOM   3196 C C   . PHE B 1 157 ? 29.40600  6.93300   20.02300  1.000 37.66112  ?  165 PHE B C   1 
ATOM   3197 O O   . PHE B 1 157 ? 29.53100  5.98200   20.80500  1.000 34.00356  ?  165 PHE B O   1 
ATOM   3198 C CB  . PHE B 1 157 ? 31.25600  6.63000   18.37900  1.000 33.69136  ?  165 PHE B CB  1 
ATOM   3199 C CG  . PHE B 1 157 ? 32.60100  7.06300   17.85900  1.000 36.58223  ?  165 PHE B CG  1 
ATOM   3200 C CD1 . PHE B 1 157 ? 33.74200  6.92300   18.63100  1.000 33.02293  ?  165 PHE B CD1 1 
ATOM   3201 C CD2 . PHE B 1 157 ? 32.72800  7.57400   16.58100  1.000 35.22329  ?  165 PHE B CD2 1 
ATOM   3202 C CE1 . PHE B 1 157 ? 34.97100  7.30900   18.15100  1.000 31.00164  ?  165 PHE B CE1 1 
ATOM   3203 C CE2 . PHE B 1 157 ? 33.95700  7.95800   16.09700  1.000 36.45466  ?  165 PHE B CE2 1 
ATOM   3204 C CZ  . PHE B 1 157 ? 35.08000  7.82500   16.88300  1.000 37.51983  ?  165 PHE B CZ  1 
ATOM   3205 N N   . VAL B 1 158 ? 28.23000  7.44400   19.67400  1.000 36.19409  ?  166 VAL B N   1 
ATOM   3206 C CA  . VAL B 1 158 ? 26.95500  6.87000   20.08400  1.000 37.37308  ?  166 VAL B CA  1 
ATOM   3207 C C   . VAL B 1 158 ? 26.23200  6.44600   18.81600  1.000 33.78989  ?  166 VAL B C   1 
ATOM   3208 O O   . VAL B 1 158 ? 25.91300  7.28600   17.96700  1.000 32.88099  ?  166 VAL B O   1 
ATOM   3209 C CB  . VAL B 1 158 ? 26.11700  7.86500   20.89700  1.000 38.73168  ?  166 VAL B CB  1 
ATOM   3210 C CG1 . VAL B 1 158 ? 24.94700  7.16000   21.55000  1.000 45.58108  ?  166 VAL B CG1 1 
ATOM   3211 C CG2 . VAL B 1 158 ? 26.97700  8.55400   21.94100  1.000 37.23155  ?  166 VAL B CG2 1 
ATOM   3212 N N   . GLU B 1 159 ? 25.97300  5.15000   18.67700  1.000 39.67742  ?  167 GLU B N   1 
ATOM   3213 C CA  . GLU B 1 159 ? 25.34900  4.59600   17.48500  1.000 34.70907  ?  167 GLU B CA  1 
ATOM   3214 C C   . GLU B 1 159 ? 23.95000  4.10100   17.81600  1.000 39.30416  ?  167 GLU B C   1 
ATOM   3215 O O   . GLU B 1 159 ? 23.76400  3.33000   18.76500  1.000 41.75159  ?  167 GLU B O   1 
ATOM   3216 C CB  . GLU B 1 159 ? 26.18500  3.45400   16.90600  1.000 32.14779  ?  167 GLU B CB  1 
ATOM   3217 C CG  . GLU B 1 159 ? 25.60000  2.84600   15.64400  1.000 36.23694  ?  167 GLU B CG  1 
ATOM   3218 C CD  . GLU B 1 159 ? 26.47500  1.76200   15.05800  1.000 38.44298  ?  167 GLU B CD  1 
ATOM   3219 O OE1 . GLU B 1 159 ? 27.30700  1.20300   15.79900  1.000 38.58982  ?  167 GLU B OE1 1 
ATOM   3220 O OE2 . GLU B 1 159 ? 26.33100  1.46600   13.85500  1.000 37.33604  -1 167 GLU B OE2 1 
ATOM   3221 N N   . VAL B 1 160 ? 22.97300  4.55100   17.03200  1.000 40.03974  ?  168 VAL B N   1 
ATOM   3222 C CA  . VAL B 1 160 ? 21.59000  4.10100   17.13000  1.000 44.39771  ?  168 VAL B CA  1 
ATOM   3223 C C   . VAL B 1 160 ? 21.20900  3.47900   15.79700  1.000 42.40455  ?  168 VAL B C   1 
ATOM   3224 O O   . VAL B 1 160 ? 21.33800  4.12100   14.75100  1.000 38.57386  ?  168 VAL B O   1 
ATOM   3225 C CB  . VAL B 1 160 ? 20.63700  5.25500   17.48700  1.000 41.54035  ?  168 VAL B CB  1 
ATOM   3226 C CG1 . VAL B 1 160 ? 19.21600  4.74300   17.61500  1.000 40.17634  ?  168 VAL B CG1 1 
ATOM   3227 C CG2 . VAL B 1 160 ? 21.08100  5.92500   18.76900  1.000 38.90840  ?  168 VAL B CG2 1 
ATOM   3228 N N   . ALA B 1 161 ? 20.73500  2.23700   15.83600  1.000 41.33633  ?  169 ALA B N   1 
ATOM   3229 C CA  . ALA B 1 161 ? 20.50400  1.45000   14.63600  1.000 44.98266  ?  169 ALA B CA  1 
ATOM   3230 C C   . ALA B 1 161 ? 19.13800  0.78300   14.67300  1.000 47.74632  ?  169 ALA B C   1 
ATOM   3231 O O   . ALA B 1 161 ? 18.75300  0.18500   15.68000  1.000 43.81240  ?  169 ALA B O   1 
ATOM   3232 C CB  . ALA B 1 161 ? 21.58400  0.37600   14.46700  1.000 39.25648  ?  169 ALA B CB  1 
ATOM   3233 N N   . ARG B 1 162 ? 18.41200  0.89000   13.56100  1.000 53.48154  ?  170 ARG B N   1 
ATOM   3234 C CA  . ARG B 1 162 ? 17.24900  0.05200   13.27900  1.000 50.38760  ?  170 ARG B CA  1 
ATOM   3235 C C   . ARG B 1 162 ? 17.54900  -0.68500  11.98400  1.000 49.17973  ?  170 ARG B C   1 
ATOM   3236 O O   . ARG B 1 162 ? 17.35800  -0.13800  10.88900  1.000 52.85920  ?  170 ARG B O   1 
ATOM   3237 C CB  . ARG B 1 162 ? 15.96500  0.86600   13.16200  1.000 52.48378  ?  170 ARG B CB  1 
ATOM   3238 C CG  . ARG B 1 162 ? 14.74700  0.00600   12.86500  1.000 50.71350  ?  170 ARG B CG  1 
ATOM   3239 C CD  . ARG B 1 162 ? 13.54800  0.83800   12.45900  1.000 62.28328  ?  170 ARG B CD  1 
ATOM   3240 N NE  . ARG B 1 162 ? 13.01500  1.61700   13.56800  1.000 63.74956  ?  170 ARG B NE  1 
ATOM   3241 C CZ  . ARG B 1 162 ? 13.22100  2.91500   13.73400  1.000 63.34848  ?  170 ARG B CZ  1 
ATOM   3242 N NH1 . ARG B 1 162 ? 13.96400  3.60900   12.88800  1.000 57.05022  ?  170 ARG B NH1 1 
ATOM   3243 N NH2 . ARG B 1 162 ? 12.66700  3.53200   14.77200  1.000 64.67571  ?  170 ARG B NH2 1 
ATOM   3244 N N   . PRO B 1 163 ? 18.03700  -1.91900  12.06600  1.000 47.35584  ?  171 PRO B N   1 
ATOM   3245 C CA  . PRO B 1 163 ? 18.39500  -2.65500  10.85000  1.000 48.78918  ?  171 PRO B CA  1 
ATOM   3246 C C   . PRO B 1 163 ? 17.19900  -2.82100  9.92600   1.000 54.23100  ?  171 PRO B C   1 
ATOM   3247 O O   . PRO B 1 163 ? 16.07000  -3.03800  10.37100  1.000 57.36702  ?  171 PRO B O   1 
ATOM   3248 C CB  . PRO B 1 163 ? 18.88700  -4.00200  11.38700  1.000 51.96526  ?  171 PRO B CB  1 
ATOM   3249 C CG  . PRO B 1 163 ? 19.31100  -3.71800  12.78600  1.000 51.54387  ?  171 PRO B CG  1 
ATOM   3250 C CD  . PRO B 1 163 ? 18.36900  -2.67000  13.28600  1.000 50.12142  ?  171 PRO B CD  1 
ATOM   3251 N N   . ALA B 1 164 ? 17.45300  -2.70600  8.62600   1.000 48.84923  ?  172 ALA B N   1 
ATOM   3252 C CA  . ALA B 1 164 ? 16.41200  -2.82200  7.61400   1.000 46.31496  ?  172 ALA B CA  1 
ATOM   3253 C C   . ALA B 1 164 ? 17.05100  -3.28100  6.31500   1.000 53.80142  ?  172 ALA B C   1 
ATOM   3254 O O   . ALA B 1 164 ? 18.03000  -2.68300  5.85900   1.000 60.30629  ?  172 ALA B O   1 
ATOM   3255 C CB  . ALA B 1 164 ? 15.68000  -1.49300  7.41400   1.000 41.80414  ?  172 ALA B CB  1 
ATOM   3256 N N   . SER B 1 165 ? 16.50500  -4.34000  5.72700   1.000 59.95924  ?  173 SER B N   1 
ATOM   3257 C CA  . SER B 1 165 ? 17.00500  -4.81300  4.44700   1.000 60.08860  ?  173 SER B CA  1 
ATOM   3258 C C   . SER B 1 165 ? 16.61100  -3.84500  3.33800   1.000 57.06467  ?  173 SER B C   1 
ATOM   3259 O O   . SER B 1 165 ? 15.65700  -3.07400  3.46400   1.000 60.05478  ?  173 SER B O   1 
ATOM   3260 C CB  . SER B 1 165 ? 16.46500  -6.21100  4.14600   1.000 58.54413  ?  173 SER B CB  1 
ATOM   3261 O OG  . SER B 1 165 ? 15.07600  -6.17300  3.87400   1.000 62.03890  ?  173 SER B OG  1 
ATOM   3262 N N   . ALA B 1 166 ? 17.37000  -3.88500  2.24100   1.000 59.53023  ?  174 ALA B N   1 
ATOM   3263 C CA  . ALA B 1 166 ? 17.04300  -3.05200  1.09000   1.000 57.89162  ?  174 ALA B CA  1 
ATOM   3264 C C   . ALA B 1 166 ? 15.69800  -3.44400  0.49600   1.000 68.45277  ?  174 ALA B C   1 
ATOM   3265 O O   . ALA B 1 166 ? 14.97700  -2.59900  -0.04700  1.000 73.83115  ?  174 ALA B O   1 
ATOM   3266 C CB  . ALA B 1 166 ? 18.14600  -3.15400  0.03700   1.000 57.47420  ?  174 ALA B CB  1 
ATOM   3267 N N   . GLU B 1 167 ? 15.34400  -4.72700  0.59400   1.000 70.12890  ?  175 GLU B N   1 
ATOM   3268 C CA  . GLU B 1 167 ? 14.06500  -5.19000  0.06700   1.000 71.32105  ?  175 GLU B CA  1 
ATOM   3269 C C   . GLU B 1 167 ? 12.90100  -4.52800  0.79400   1.000 72.81967  ?  175 GLU B C   1 
ATOM   3270 O O   . GLU B 1 167 ? 11.91300  -4.12800  0.17000   1.000 71.25454  ?  175 GLU B O   1 
ATOM   3271 C CB  . GLU B 1 167 ? 13.97700  -6.71200  0.17400   1.000 69.73060  ?  175 GLU B CB  1 
ATOM   3272 C CG  . GLU B 1 167 ? 12.57400  -7.27100  0.00100   1.000 80.16020  ?  175 GLU B CG  1 
ATOM   3273 C CD  . GLU B 1 167 ? 12.54600  -8.52100  -0.85800  1.000 90.69322  ?  175 GLU B CD  1 
ATOM   3274 O OE1 . GLU B 1 167 ? 13.24000  -9.49900  -0.51000  1.000 81.28222  ?  175 GLU B OE1 1 
ATOM   3275 O OE2 . GLU B 1 167 ? 11.82800  -8.52600  -1.88000  1.000 93.74460  -1 175 GLU B OE2 1 
ATOM   3276 N N   . ALA B 1 168 ? 13.00100  -4.40300  2.11900   1.000 68.31642  ?  176 ALA B N   1 
ATOM   3277 C CA  . ALA B 1 168 ? 11.92600  -3.78100  2.88600   1.000 65.02121  ?  176 ALA B CA  1 
ATOM   3278 C C   . ALA B 1 168 ? 11.76300  -2.31000  2.52700   1.000 72.06681  ?  176 ALA B C   1 
ATOM   3279 O O   . ALA B 1 168 ? 10.63600  -1.82100  2.37600   1.000 66.24485  ?  176 ALA B O   1 
ATOM   3280 C CB  . ALA B 1 168 ? 12.18800  -3.94200  4.38200   1.000 54.72536  ?  176 ALA B CB  1 
ATOM   3281 N N   . ALA B 1 169 ? 12.87600  -1.58500  2.39500   1.000 67.50437  ?  177 ALA B N   1 
ATOM   3282 C CA  . ALA B 1 169 ? 12.79800  -0.17700  2.01800   1.000 62.82591  ?  177 ALA B CA  1 
ATOM   3283 C C   . ALA B 1 169 ? 12.22900  -0.01700  0.61600   1.000 68.93430  ?  177 ALA B C   1 
ATOM   3284 O O   . ALA B 1 169 ? 11.42200  0.88600   0.36300   1.000 68.83675  ?  177 ALA B O   1 
ATOM   3285 C CB  . ALA B 1 169 ? 14.17800  0.47000   2.11800   1.000 45.42980  ?  177 ALA B CB  1 
ATOM   3286 N N   . LEU B 1 170 ? 12.63700  -0.88800  -0.31100  1.000 69.59423  ?  178 LEU B N   1 
ATOM   3287 C CA  . LEU B 1 170 ? 12.07600  -0.85400  -1.65600  1.000 72.98149  ?  178 LEU B CA  1 
ATOM   3288 C C   . LEU B 1 170 ? 10.57800  -1.12300  -1.63200  1.000 68.34870  ?  178 LEU B C   1 
ATOM   3289 O O   . LEU B 1 170 ? 9.81000   -0.46200  -2.33900  1.000 67.28572  ?  178 LEU B O   1 
ATOM   3290 C CB  . LEU B 1 170 ? 12.78800  -1.87100  -2.54700  1.000 68.56349  ?  178 LEU B CB  1 
ATOM   3291 C CG  . LEU B 1 170 ? 14.17400  -1.48600  -3.06000  1.000 54.64340  ?  178 LEU B CG  1 
ATOM   3292 C CD1 . LEU B 1 170 ? 14.89200  -2.70300  -3.61300  1.000 55.91475  ?  178 LEU B CD1 1 
ATOM   3293 C CD2 . LEU B 1 170 ? 14.06500  -0.40200  -4.11600  1.000 58.14492  ?  178 LEU B CD2 1 
ATOM   3294 N N   . SER B 1 171 ? 10.14600  -2.09200  -0.82300  1.000 67.80254  ?  179 SER B N   1 
ATOM   3295 C CA  . SER B 1 171 ? 8.72600   -2.40300  -0.72000  1.000 65.66675  ?  179 SER B CA  1 
ATOM   3296 C C   . SER B 1 171 ? 7.94600   -1.21900  -0.16500  1.000 64.33745  ?  179 SER B C   1 
ATOM   3297 O O   . SER B 1 171 ? 6.86000   -0.89500  -0.65300  1.000 72.64531  ?  179 SER B O   1 
ATOM   3298 C CB  . SER B 1 171 ? 8.52400   -3.63800  0.15900   1.000 66.74190  ?  179 SER B CB  1 
ATOM   3299 O OG  . SER B 1 171 ? 9.04300   -4.80000  -0.46200  1.000 74.02170  ?  179 SER B OG  1 
ATOM   3300 N N   . LYS B 1 172 ? 8.51100   -0.55300  0.83900   1.000 68.24068  ?  180 LYS B N   1 
ATOM   3301 C CA  . LYS B 1 172 ? 7.82700   0.60000   1.47400   1.000 65.83775  ?  180 LYS B CA  1 
ATOM   3302 C C   . LYS B 1 172 ? 7.72300   1.74400   0.46500   1.000 66.70832  ?  180 LYS B C   1 
ATOM   3303 O O   . LYS B 1 172 ? 6.66100   2.38000   0.39400   1.000 65.40043  ?  180 LYS B O   1 
ATOM   3304 C CB  . LYS B 1 172 ? 8.62700   1.04000   2.70000   1.000 67.89110  ?  180 LYS B CB  1 
ATOM   3305 C CG  . LYS B 1 172 ? 8.07000   2.20800   3.49800   1.000 71.33532  ?  180 LYS B CG  1 
ATOM   3306 C CD  . LYS B 1 172 ? 8.99200   2.56400   4.65700   1.000 72.69471  ?  180 LYS B CD  1 
ATOM   3307 C CE  . LYS B 1 172 ? 8.48100   3.67800   5.51100   1.000 81.95002  ?  180 LYS B CE  1 
ATOM   3308 N NZ  . LYS B 1 172 ? 9.39600   3.95000   6.62100   1.000 71.69648  ?  180 LYS B NZ  1 
ATOM   3309 N N   . ALA B 1 173 ? 8.79700   1.99100   -0.28000  1.000 70.72316  ?  181 ALA B N   1 
ATOM   3310 C CA  . ALA B 1 173 ? 8.77800   3.04600   -1.28500  1.000 70.85567  ?  181 ALA B CA  1 
ATOM   3311 C C   . ALA B 1 173 ? 7.78200   2.73500   -2.39300  1.000 73.83076  ?  181 ALA B C   1 
ATOM   3312 O O   . ALA B 1 173 ? 7.06800   3.62700   -2.86400  1.000 77.50473  ?  181 ALA B O   1 
ATOM   3313 C CB  . ALA B 1 173 ? 10.17700  3.24800   -1.86100  1.000 69.09112  ?  181 ALA B CB  1 
ATOM   3314 N N   . ALA B 1 174 ? 7.72300   1.47400   -2.82700  1.000 73.81820  ?  182 ALA B N   1 
ATOM   3315 C CA  . ALA B 1 174 ? 6.76200   1.08600   -3.85300  1.000 73.66562  ?  182 ALA B CA  1 
ATOM   3316 C C   . ALA B 1 174 ? 5.33200   1.21600   -3.34500  1.000 74.21724  ?  182 ALA B C   1 
ATOM   3317 O O   . ALA B 1 174 ? 4.43800   1.62700   -4.09100  1.000 79.99240  ?  182 ALA B O   1 
ATOM   3318 C CB  . ALA B 1 174 ? 7.04600   -0.34000  -4.32100  1.000 66.15520  ?  182 ALA B CB  1 
ATOM   3319 N N   . TRP B 1 175 ? 5.10000   0.86200   -2.08000  1.000 66.72229  ?  183 TRP B N   1 
ATOM   3320 C CA  . TRP B 1 175 ? 3.79300   1.06400   -1.46300  1.000 73.42820  ?  183 TRP B CA  1 
ATOM   3321 C C   . TRP B 1 175 ? 3.38900   2.53100   -1.53200  1.000 72.96161  ?  183 TRP B C   1 
ATOM   3322 O O   . TRP B 1 175 ? 2.28100   2.86700   -1.96900  1.000 73.44938  ?  183 TRP B O   1 
ATOM   3323 C CB  . TRP B 1 175 ? 3.84100   0.58000   -0.00900  1.000 77.64622  ?  183 TRP B CB  1 
ATOM   3324 C CG  . TRP B 1 175 ? 2.55000   0.66100   0.77600   1.000 80.95633  ?  183 TRP B CG  1 
ATOM   3325 C CD1 . TRP B 1 175 ? 1.71900   1.73900   0.89600   1.000 84.63742  ?  183 TRP B CD1 1 
ATOM   3326 C CD2 . TRP B 1 175 ? 1.98500   -0.36800  1.59700   1.000 79.63984  ?  183 TRP B CD2 1 
ATOM   3327 N NE1 . TRP B 1 175 ? 0.65900   1.43400   1.71000   1.000 77.83056  ?  183 TRP B NE1 1 
ATOM   3328 C CE2 . TRP B 1 175 ? 0.80000   0.14700   2.15700   1.000 80.80389  ?  183 TRP B CE2 1 
ATOM   3329 C CE3 . TRP B 1 175 ? 2.36100   -1.67900  1.90400   1.000 79.82024  ?  183 TRP B CE3 1 
ATOM   3330 C CZ2 . TRP B 1 175 ? -0.01300  -0.60200  3.00300   1.000 79.77373  ?  183 TRP B CZ2 1 
ATOM   3331 C CZ3 . TRP B 1 175 ? 1.55200   -2.42100  2.74300   1.000 80.59685  ?  183 TRP B CZ3 1 
ATOM   3332 C CH2 . TRP B 1 175 ? 0.38000   -1.88100  3.28300   1.000 83.29744  ?  183 TRP B CH2 1 
ATOM   3333 N N   . LYS B 1 176 ? 4.28900   3.41900   -1.10600  1.000 69.91324  ?  184 LYS B N   1 
ATOM   3334 C CA  . LYS B 1 176 ? 3.98500   4.84700   -1.11800  1.000 71.01480  ?  184 LYS B CA  1 
ATOM   3335 C C   . LYS B 1 176 ? 3.73300   5.34700   -2.53500  1.000 72.55189  ?  184 LYS B C   1 
ATOM   3336 O O   . LYS B 1 176 ? 2.79200   6.11500   -2.77500  1.000 73.13902  ?  184 LYS B O   1 
ATOM   3337 C CB  . LYS B 1 176 ? 5.12800   5.62700   -0.47100  1.000 76.16264  ?  184 LYS B CB  1 
ATOM   3338 C CG  . LYS B 1 176 ? 5.17800   5.52500   1.04300   1.000 74.96694  ?  184 LYS B CG  1 
ATOM   3339 C CD  . LYS B 1 176 ? 6.19900   6.48900   1.62400   1.000 74.74058  ?  184 LYS B CD  1 
ATOM   3340 C CE  . LYS B 1 176 ? 6.14500   6.50500   3.14100   1.000 83.23531  ?  184 LYS B CE  1 
ATOM   3341 N NZ  . LYS B 1 176 ? 7.13500   7.45500   3.71700   1.000 87.24418  ?  184 LYS B NZ  1 
ATOM   3342 N N   . VAL B 1 177 ? 4.55800   4.91300   -3.48800  1.000 75.58094  ?  185 VAL B N   1 
ATOM   3343 C CA  . VAL B 1 177 ? 4.41900   5.37000   -4.86700  1.000 78.62381  ?  185 VAL B CA  1 
ATOM   3344 C C   . VAL B 1 177 ? 3.08600   4.91500   -5.44700  1.000 77.24634  ?  185 VAL B C   1 
ATOM   3345 O O   . VAL B 1 177 ? 2.37700   5.69300   -6.09600  1.000 84.42012  ?  185 VAL B O   1 
ATOM   3346 C CB  . VAL B 1 177 ? 5.60600   4.87600   -5.71200  1.000 81.15729  ?  185 VAL B CB  1 
ATOM   3347 C CG1 . VAL B 1 177 ? 5.21900   4.77500   -7.17800  1.000 81.65148  ?  185 VAL B CG1 1 
ATOM   3348 C CG2 . VAL B 1 177 ? 6.79300   5.80100   -5.53400  1.000 69.21231  ?  185 VAL B CG2 1 
ATOM   3349 N N   . ILE B 1 178 ? 2.72100   3.65400   -5.21300  1.000 75.86988  ?  186 ILE B N   1 
ATOM   3350 C CA  . ILE B 1 178 ? 1.45000   3.14000   -5.71300  1.000 77.86635  ?  186 ILE B CA  1 
ATOM   3351 C C   . ILE B 1 178 ? 0.29000   3.90400   -5.09100  1.000 79.23864  ?  186 ILE B C   1 
ATOM   3352 O O   . ILE B 1 178 ? -0.67300  4.26800   -5.77800  1.000 77.91743  ?  186 ILE B O   1 
ATOM   3353 C CB  . ILE B 1 178 ? 1.34800   1.62600   -5.44800  1.000 76.66959  ?  186 ILE B CB  1 
ATOM   3354 C CG1 . ILE B 1 178 ? 1.94100   0.84100   -6.61700  1.000 72.55102  ?  186 ILE B CG1 1 
ATOM   3355 C CG2 . ILE B 1 178 ? -0.09500  1.21000   -5.22000  1.000 78.28188  ?  186 ILE B CG2 1 
ATOM   3356 C CD1 . ILE B 1 178 ? 1.89700   -0.65600  -6.42800  1.000 70.64064  ?  186 ILE B CD1 1 
ATOM   3357 N N   . ALA B 1 179 ? 0.36700   4.17400   -3.78500  1.000 79.80140  ?  187 ALA B N   1 
ATOM   3358 C CA  . ALA B 1 179 ? -0.70800  4.90800   -3.12700  1.000 73.73926  ?  187 ALA B CA  1 
ATOM   3359 C C   . ALA B 1 179 ? -0.79300  6.35100   -3.60900  1.000 71.37550  ?  187 ALA B C   1 
ATOM   3360 O O   . ALA B 1 179 ? -1.86300  6.96500   -3.52800  1.000 71.07788  ?  187 ALA B O   1 
ATOM   3361 C CB  . ALA B 1 179 ? -0.52100  4.86500   -1.61200  1.000 70.77530  ?  187 ALA B CB  1 
ATOM   3362 N N   . SER B 1 180 ? 0.30800   6.91000   -4.11000  1.000 73.13787  ?  188 SER B N   1 
ATOM   3363 C CA  . SER B 1 180 ? 0.33600   8.31100   -4.51100  1.000 72.86317  ?  188 SER B CA  1 
ATOM   3364 C C   . SER B 1 180 ? 0.01600   8.53800   -5.98600  1.000 80.10290  ?  188 SER B C   1 
ATOM   3365 O O   . SER B 1 180 ? 0.08100   9.68400   -6.44300  1.000 79.10859  ?  188 SER B O   1 
ATOM   3366 C CB  . SER B 1 180 ? 1.70500   8.92100   -4.19100  1.000 63.56560  ?  188 SER B CB  1 
ATOM   3367 O OG  . SER B 1 180 ? 2.71000   8.39600   -5.03900  1.000 64.67853  ?  188 SER B OG  1 
ATOM   3368 N N   . ILE B 1 181 ? -0.33100  7.49300   -6.73700  1.000 79.52694  ?  189 ILE B N   1 
ATOM   3369 C CA  . ILE B 1 181 ? -0.56100  7.64100   -8.17000  1.000 79.86225  ?  189 ILE B CA  1 
ATOM   3370 C C   . ILE B 1 181 ? -1.87600  8.36800   -8.41400  1.000 81.50560  ?  189 ILE B C   1 
ATOM   3371 O O   . ILE B 1 181 ? -2.92400  7.99100   -7.87400  1.000 82.40577  ?  189 ILE B O   1 
ATOM   3372 C CB  . ILE B 1 181 ? -0.54500  6.27100   -8.86200  1.000 83.58363  ?  189 ILE B CB  1 
ATOM   3373 C CG1 . ILE B 1 181 ? 0.87400   5.70500   -8.87500  1.000 79.66036  ?  189 ILE B CG1 1 
ATOM   3374 C CG2 . ILE B 1 181 ? -1.09100  6.37800   -10.27600 1.000 77.48616  ?  189 ILE B CG2 1 
ATOM   3375 C CD1 . ILE B 1 181 ? 0.95100   4.27300   -9.31000  1.000 70.13140  ?  189 ILE B CD1 1 
ATOM   3376 N N   . LYS B 1 182 ? -1.82600  9.41500   -9.24200  1.000 78.27178  ?  190 LYS B N   1 
ATOM   3377 C CA  . LYS B 1 182 ? -3.01100  10.22200  -9.51000  1.000 79.25936  ?  190 LYS B CA  1 
ATOM   3378 C C   . LYS B 1 182 ? -3.98400  9.54200   -10.46600 1.000 85.52330  ?  190 LYS B C   1 
ATOM   3379 O O   . LYS B 1 182 ? -5.18800  9.81400   -10.40700 1.000 86.82090  ?  190 LYS B O   1 
ATOM   3380 C CB  . LYS B 1 182 ? -2.60000  11.58600  -10.06500 1.000 73.20334  ?  190 LYS B CB  1 
ATOM   3381 C CG  . LYS B 1 182 ? -1.67400  12.37200  -9.15200  1.000 69.97369  ?  190 LYS B CG  1 
ATOM   3382 C CD  . LYS B 1 182 ? -0.75300  13.28800  -9.94300  1.000 54.84101  ?  190 LYS B CD  1 
ATOM   3383 C CE  . LYS B 1 182 ? -0.13700  14.35100  -9.04600  1.000 56.53832  ?  190 LYS B CE  1 
ATOM   3384 N NZ  . LYS B 1 182 ? 0.51600   15.43400  -9.82900  1.000 54.78466  ?  190 LYS B NZ  1 
ATOM   3385 N N   . ASP B 1 183 ? -3.49700  8.67000   -11.34500 1.000 87.66082  ?  191 ASP B N   1 
ATOM   3386 C CA  . ASP B 1 183 ? -4.36100  7.97800   -12.29800 1.000 86.61135  ?  191 ASP B CA  1 
ATOM   3387 C C   . ASP B 1 183 ? -5.07600  6.84600   -11.57000 1.000 88.42324  ?  191 ASP B C   1 
ATOM   3388 O O   . ASP B 1 183 ? -4.43200  5.96300   -10.99500 1.000 96.88718  ?  191 ASP B O   1 
ATOM   3389 C CB  . ASP B 1 183 ? -3.54200  7.45700   -13.47600 1.000 85.35550  ?  191 ASP B CB  1 
ATOM   3390 C CG  . ASP B 1 183 ? -4.40500  6.88200   -14.59100 1.000 96.60646  ?  191 ASP B CG  1 
ATOM   3391 O OD1 . ASP B 1 183 ? -5.33300  6.09600   -14.30800 1.000 93.61938  ?  191 ASP B OD1 1 
ATOM   3392 O OD2 . ASP B 1 183 ? -4.15200  7.22300   -15.76500 1.000 98.92757  -1 191 ASP B OD2 1 
ATOM   3393 N N   . ARG B 1 184 ? -6.41000  6.86900   -11.59200 1.000 82.46759  ?  192 ARG B N   1 
ATOM   3394 C CA  . ARG B 1 184 ? -7.18000  5.85300   -10.88200 1.000 90.10376  ?  192 ARG B CA  1 
ATOM   3395 C C   . ARG B 1 184 ? -7.02300  4.47200   -11.50600 1.000 89.31936  ?  192 ARG B C   1 
ATOM   3396 O O   . ARG B 1 184 ? -6.72100  3.50600   -10.79600 1.000 89.45955  ?  192 ARG B O   1 
ATOM   3397 C CB  . ARG B 1 184 ? -8.65600  6.24700   -10.84200 1.000 98.40463  ?  192 ARG B CB  1 
ATOM   3398 C CG  . ARG B 1 184 ? -8.99000  7.34000   -9.83700  1.000 93.92982  ?  192 ARG B CG  1 
ATOM   3399 C CD  . ARG B 1 184 ? -8.80400  6.85800   -8.40800  1.000 96.52418  ?  192 ARG B CD  1 
ATOM   3400 N NE  . ARG B 1 184 ? -9.12600  7.89400   -7.43400  1.000 88.47029  ?  192 ARG B NE  1 
ATOM   3401 C CZ  . ARG B 1 184 ? -9.09400  7.72100   -6.11900  1.000 86.73081  ?  192 ARG B CZ  1 
ATOM   3402 N NH1 . ARG B 1 184 ? -8.75900  6.55900   -5.58200  1.000 84.00668  ?  192 ARG B NH1 1 
ATOM   3403 N NH2 . ARG B 1 184 ? -9.40600  8.74000   -5.32300  1.000 83.58901  ?  192 ARG B NH2 1 
ATOM   3404 N N   . ALA B 1 185 ? -7.22100  4.35400   -12.82100 1.000 91.62865  ?  193 ALA B N   1 
ATOM   3405 C CA  . ALA B 1 185 ? -7.17100  3.04300   -13.46100 1.000 93.96456  ?  193 ALA B CA  1 
ATOM   3406 C C   . ALA B 1 185 ? -5.76500  2.45800   -13.42000 1.000 92.35808  ?  193 ALA B C   1 
ATOM   3407 O O   . ALA B 1 185 ? -5.59300  1.25100   -13.20400 1.000 95.06037  ?  193 ALA B O   1 
ATOM   3408 C CB  . ALA B 1 185 ? -7.67100  3.14100   -14.90200 1.000 89.23918  ?  193 ALA B CB  1 
ATOM   3409 N N   . PHE B 1 186 ? -4.75000  3.29700   -13.62900 1.000 92.67497  ?  194 PHE B N   1 
ATOM   3410 C CA  . PHE B 1 186 ? -3.37200  2.82700   -13.54500 1.000 95.87531  ?  194 PHE B CA  1 
ATOM   3411 C C   . PHE B 1 186 ? -3.05500  2.32500   -12.14300 1.000 95.94534  ?  194 PHE B C   1 
ATOM   3412 O O   . PHE B 1 186 ? -2.41900  1.27700   -11.98100 1.000 88.03693  ?  194 PHE B O   1 
ATOM   3413 C CB  . PHE B 1 186 ? -2.41800  3.95100   -13.94900 1.000 93.48443  ?  194 PHE B CB  1 
ATOM   3414 C CG  . PHE B 1 186 ? -1.01300  3.49400   -14.21200 1.000 95.13051  ?  194 PHE B CG  1 
ATOM   3415 C CD1 . PHE B 1 186 ? -0.77000  2.33300   -14.92200 1.000 95.29338  ?  194 PHE B CD1 1 
ATOM   3416 C CD2 . PHE B 1 186 ? 0.06500   4.23400   -13.75800 1.000 89.12078  ?  194 PHE B CD2 1 
ATOM   3417 C CE1 . PHE B 1 186 ? 0.52100   1.91500   -15.16900 1.000 90.32450  ?  194 PHE B CE1 1 
ATOM   3418 C CE2 . PHE B 1 186 ? 1.35700   3.82100   -14.00200 1.000 80.49193  ?  194 PHE B CE2 1 
ATOM   3419 C CZ  . PHE B 1 186 ? 1.58600   2.65900   -14.70900 1.000 86.62608  ?  194 PHE B CZ  1 
ATOM   3420 N N   . GLN B 1 187 ? -3.50900  3.05200   -11.12000 1.000 95.13102  ?  195 GLN B N   1 
ATOM   3421 C CA  . GLN B 1 187 ? -3.29700  2.62000   -9.74300  1.000 87.15980  ?  195 GLN B CA  1 
ATOM   3422 C C   . GLN B 1 187 ? -4.00800  1.30100   -9.46500  1.000 89.50216  ?  195 GLN B C   1 
ATOM   3423 O O   . GLN B 1 187 ? -3.45500  0.41400   -8.80700  1.000 90.15943  ?  195 GLN B O   1 
ATOM   3424 C CB  . GLN B 1 187 ? -3.77100  3.70600   -8.77800  1.000 82.36377  ?  195 GLN B CB  1 
ATOM   3425 C CG  . GLN B 1 187 ? -3.52300  3.39300   -7.31200  1.000 88.04609  ?  195 GLN B CG  1 
ATOM   3426 C CD  . GLN B 1 187 ? -4.17100  4.40100   -6.38300  1.000 87.47923  ?  195 GLN B CD  1 
ATOM   3427 O OE1 . GLN B 1 187 ? -5.14800  4.09500   -5.70200  1.000 85.83238  ?  195 GLN B OE1 1 
ATOM   3428 N NE2 . GLN B 1 187 ? -3.63000  5.61200   -6.35300  1.000 77.75964  ?  195 GLN B NE2 1 
ATOM   3429 N N   . ARG B 1 188 ? -5.21400  1.15700   -10.00300 1.000 88.97390  ?  196 ARG B N   1 
ATOM   3430 C CA  . ARG B 1 188 ? -5.99100  -0.07700  -9.74200  1.000 89.02477  ?  196 ARG B CA  1 
ATOM   3431 C C   . ARG B 1 188 ? -5.28100  -1.26100  -10.40800 1.000 87.84934  ?  196 ARG B C   1 
ATOM   3432 O O   . ARG B 1 188 ? -5.20200  -2.32900  -9.77400  1.000 86.66650  ?  196 ARG B O   1 
ATOM   3433 C CB  . ARG B 1 188 ? -7.42800  0.11300   -10.23000 1.000 89.54635  ?  196 ARG B CB  1 
ATOM   3434 C CG  . ARG B 1 188 ? -8.23400  1.03500   -9.32700  1.000 93.17160  ?  196 ARG B CG  1 
ATOM   3435 C CD  . ARG B 1 188 ? -9.64000  1.28000   -9.85200  1.000 97.92226  ?  196 ARG B CD  1 
ATOM   3436 N NE  . ARG B 1 188 ? -9.65700  2.08300   -11.07900 1.000 89.65308  ?  196 ARG B NE  1 
ATOM   3437 C CZ  . ARG B 1 188 ? -10.25500 3.26200   -11.17800 1.000 87.51485  ?  196 ARG B CZ  1 
ATOM   3438 N NH1 . ARG B 1 188 ? -10.74100 3.84400   -10.09800 1.000 88.68444  ?  196 ARG B NH1 1 
ATOM   3439 N NH2 . ARG B 1 188 ? -10.36300 3.85400   -12.35300 1.000 78.93797  ?  196 ARG B NH2 1 
ATOM   3440 N N   . GLU B 1 189 ? -4.68900  -1.00900  -11.57300 1.000 85.86319  ?  197 GLU B N   1 
ATOM   3441 C CA  . GLU B 1 189 ? -3.94600  -2.06400  -12.29600 1.000 92.17043  ?  197 GLU B CA  1 
ATOM   3442 C C   . GLU B 1 189 ? -2.71300  -2.43300  -11.48900 1.000 90.53728  ?  197 GLU B C   1 
ATOM   3443 O O   . GLU B 1 189 ? -2.41400  -3.62300  -11.39800 1.000 93.06305  ?  197 GLU B O   1 
ATOM   3444 C CB  . GLU B 1 189 ? -3.41200  -1.56400  -13.63400 1.000 94.43886  ?  197 GLU B CB  1 
ATOM   3445 C CG  . GLU B 1 189 ? -2.75200  -2.65600  -14.47000 1.000 93.04509  ?  197 GLU B CG  1 
ATOM   3446 C CD  . GLU B 1 189 ? -3.63200  -3.86900  -14.70700 1.000 98.94137  ?  197 GLU B CD  1 
ATOM   3447 O OE1 . GLU B 1 189 ? -4.71400  -3.71100  -15.30900 1.000 104.78270 ?  197 GLU B OE1 1 
ATOM   3448 O OE2 . GLU B 1 189 ? -3.23700  -4.97300  -14.28800 1.000 94.16640  -1 197 GLU B OE2 1 
ATOM   3449 N N   . LEU B 1 190 ? -2.01100  -1.43500  -10.96100 1.000 88.50176  ?  198 LEU B N   1 
ATOM   3450 C CA  . LEU B 1 190 ? -0.75400  -1.73500  -10.23400 1.000 85.79572  ?  198 LEU B CA  1 
ATOM   3451 C C   . LEU B 1 190 ? -1.10400  -2.49100  -8.94800  1.000 85.46791  ?  198 LEU B C   1 
ATOM   3452 O O   . LEU B 1 190 ? -0.42900  -3.48400  -8.65300  1.000 92.07991  ?  198 LEU B O   1 
ATOM   3453 C CB  . LEU B 1 190 ? 0.03800   -0.45700  -9.97200  1.000 82.96637  ?  198 LEU B CB  1 
ATOM   3454 C CG  . LEU B 1 190 ? 1.21700   -0.20700  -10.91800 1.000 82.32572  ?  198 LEU B CG  1 
ATOM   3455 C CD1 . LEU B 1 190 ? 0.80800   -0.34300  -12.37200 1.000 87.14169  ?  198 LEU B CD1 1 
ATOM   3456 C CD2 . LEU B 1 190 ? 1.84900   1.14600   -10.67400 1.000 70.71286  ?  198 LEU B CD2 1 
ATOM   3457 N N   . MET B 1 191 ? -2.14000  -2.05300  -8.23900  1.000 83.73106  ?  199 MET B N   1 
ATOM   3458 C CA  . MET B 1 191 ? -2.55800  -2.72700  -6.98400  1.000 81.20154  ?  199 MET B CA  1 
ATOM   3459 C C   . MET B 1 191 ? -2.99100  -4.16000  -7.31000  1.000 84.55312  ?  199 MET B C   1 
ATOM   3460 O O   . MET B 1 191 ? -2.85700  -5.03500  -6.43600  1.000 81.14679  ?  199 MET B O   1 
ATOM   3461 C CB  . MET B 1 191 ? -3.71200  -1.96700  -6.32600  1.000 80.99760  ?  199 MET B CB  1 
ATOM   3462 C CG  . MET B 1 191 ? -3.31700  -0.63400  -5.73300  1.000 83.74728  ?  199 MET B CG  1 
ATOM   3463 S SD  . MET B 1 191 ? -4.75300  0.28300   -5.14400  1.000 83.81571  ?  199 MET B SD  1 
ATOM   3464 C CE  . MET B 1 191 ? -3.96400  1.42000   -3.99600  1.000 75.73282  ?  199 MET B CE  1 
ATOM   3465 N N   . ARG B 1 192 ? -3.51800  -4.37500  -8.51500  1.000 90.80806  ?  200 ARG B N   1 
ATOM   3466 C CA  . ARG B 1 192 ? -3.96200  -5.72300  -8.94300  1.000 87.32135  ?  200 ARG B CA  1 
ATOM   3467 C C   . ARG B 1 192 ? -2.73300  -6.59100  -9.20600  1.000 90.63260  ?  200 ARG B C   1 
ATOM   3468 O O   . ARG B 1 192 ? -2.69300  -7.72800  -8.70100  1.000 91.08874  ?  200 ARG B O   1 
ATOM   3469 C CB  . ARG B 1 192 ? -4.78600  -5.58500  -10.22100 1.000 88.29550  ?  200 ARG B CB  1 
ATOM   3470 C CG  . ARG B 1 192 ? -5.39000  -6.88600  -10.72900 1.000 103.13106 ?  200 ARG B CG  1 
ATOM   3471 C CD  . ARG B 1 192 ? -6.12300  -6.70700  -12.05200 1.000 106.93804 ?  200 ARG B CD  1 
ATOM   3472 N NE  . ARG B 1 192 ? -5.24700  -6.69100  -13.23000 1.000 99.12182  ?  200 ARG B NE  1 
ATOM   3473 C CZ  . ARG B 1 192 ? -4.51200  -7.71200  -13.64900 1.000 100.42460 ?  200 ARG B CZ  1 
ATOM   3474 N NH1 . ARG B 1 192 ? -4.55000  -8.86900  -13.01300 1.000 96.94679  ?  200 ARG B NH1 1 
ATOM   3475 N NH2 . ARG B 1 192 ? -3.74200  -7.57500  -14.71200 1.000 105.88315 ?  200 ARG B NH2 1 
ATOM   3476 N N   . ARG B 1 193 ? -1.76700  -6.06100  -9.95800  1.000 87.29547  ?  201 ARG B N   1 
ATOM   3477 C CA  . ARG B 1 193 ? -0.51900  -6.80700  -10.24200 1.000 80.64055  ?  201 ARG B CA  1 
ATOM   3478 C C   . ARG B 1 193 ? 0.20400   -7.05100  -8.91200  1.000 92.76522  ?  201 ARG B C   1 
ATOM   3479 O O   . ARG B 1 193 ? 0.71300   -8.17900  -8.71600  1.000 95.32234  ?  201 ARG B O   1 
ATOM   3480 C CB  . ARG B 1 193 ? 0.30900   -6.01800  -11.25600 1.000 69.28986  ?  201 ARG B CB  1 
ATOM   3481 C CG  . ARG B 1 193 ? -0.33800  -5.99100  -12.63200 1.000 79.42059  ?  201 ARG B CG  1 
ATOM   3482 C CD  . ARG B 1 193 ? -0.16300  -4.64600  -13.30600 1.000 79.17332  ?  201 ARG B CD  1 
ATOM   3483 N NE  . ARG B 1 193 ? 1.20200   -4.38400  -13.76800 1.000 77.33206  ?  201 ARG B NE  1 
ATOM   3484 C CZ  . ARG B 1 193 ? 1.49300   -4.11900  -15.02900 1.000 89.79850  ?  201 ARG B CZ  1 
ATOM   3485 N NH1 . ARG B 1 193 ? 0.54500   -4.18400  -15.94500 1.000 92.09472  ?  201 ARG B NH1 1 
ATOM   3486 N NH2 . ARG B 1 193 ? 2.72400   -3.78500  -15.37100 1.000 104.87850 ?  201 ARG B NH2 1 
ATOM   3487 N N   . SER B 1 194 ? 0.22900   -6.04700  -8.03000  1.000 91.06702  ?  202 SER B N   1 
ATOM   3488 C CA  . SER B 1 194 ? 0.84000   -6.24800  -6.72400  1.000 88.88956  ?  202 SER B CA  1 
ATOM   3489 C C   . SER B 1 194 ? 0.32100   -7.50200  -6.05400  1.000 90.25476  ?  202 SER B C   1 
ATOM   3490 O O   . SER B 1 194 ? 1.12400   -8.26800  -5.52000  1.000 89.57001  ?  202 SER B O   1 
ATOM   3491 C CB  . SER B 1 194 ? 0.58700   -5.05100  -5.80600  1.000 86.70165  ?  202 SER B CB  1 
ATOM   3492 O OG  . SER B 1 194 ? 0.95700   -3.82800  -6.41000  1.000 85.26715  ?  202 SER B OG  1 
ATOM   3493 N N   . GLU B 1 195 ? -0.99100  -7.73800  -6.11400  1.000 87.67753  ?  203 GLU B N   1 
ATOM   3494 C CA  . GLU B 1 195 ? -1.57000  -8.92800  -5.49600  1.000 94.04458  ?  203 GLU B CA  1 
ATOM   3495 C C   . GLU B 1 195 ? -0.83500  -10.20000 -5.91400  1.000 95.11280  ?  203 GLU B C   1 
ATOM   3496 O O   . GLU B 1 195 ? -0.78600  -11.16700 -5.14400  1.000 91.23131  ?  203 GLU B O   1 
ATOM   3497 C CB  . GLU B 1 195 ? -3.05700  -9.02200  -5.84900  1.000 95.13420  ?  203 GLU B CB  1 
ATOM   3498 C CG  . GLU B 1 195 ? -3.72300  -10.34100 -5.48400  1.000 101.46875 ?  203 GLU B CG  1 
ATOM   3499 C CD  . GLU B 1 195 ? -5.20400  -10.18900 -5.19500  1.000 104.26642 ?  203 GLU B CD  1 
ATOM   3500 O OE1 . GLU B 1 195 ? -5.75600  -9.10500  -5.47500  1.000 111.43012 ?  203 GLU B OE1 1 
ATOM   3501 O OE2 . GLU B 1 195 ? -5.81500  -11.15300 -4.68800  1.000 95.19711  -1 203 GLU B OE2 1 
ATOM   3502 N N   . LYS B 1 196 ? -0.22700  -10.20800 -7.10000  1.000 95.69675  ?  204 LYS B N   1 
ATOM   3503 C CA  . LYS B 1 196 ? 0.48100   -11.38000 -7.59900  1.000 97.83771  ?  204 LYS B CA  1 
ATOM   3504 C C   . LYS B 1 196 ? 1.99700   -11.29800 -7.45200  1.000 97.51539  ?  204 LYS B C   1 
ATOM   3505 O O   . LYS B 1 196 ? 2.62700   -12.31600 -7.15100  1.000 96.57475  ?  204 LYS B O   1 
ATOM   3506 C CB  . LYS B 1 196 ? 0.13200   -11.61400 -9.07400  1.000 96.54643  ?  204 LYS B CB  1 
ATOM   3507 C CG  . LYS B 1 196 ? 0.67800   -12.91300 -9.65000  1.000 99.27483  ?  204 LYS B CG  1 
ATOM   3508 C CD  . LYS B 1 196 ? 0.71800   -12.87000 -11.17000 1.000 94.99154  ?  204 LYS B CD  1 
ATOM   3509 C CE  . LYS B 1 196 ? 1.76200   -13.82300 -11.72600 1.000 93.20428  ?  204 LYS B CE  1 
ATOM   3510 N NZ  . LYS B 1 196 ? 1.15800   -15.10000 -12.19700 1.000 97.15566  ?  204 LYS B NZ  1 
ATOM   3511 N N   . ASP B 1 197 ? 2.60800   -10.12600 -7.65300  1.000 99.75904  ?  205 ASP B N   1 
ATOM   3512 C CA  . ASP B 1 197 ? 4.06700   -10.02600 -7.69400  1.000 102.68316 ?  205 ASP B CA  1 
ATOM   3513 C C   . ASP B 1 197 ? 4.62900   -8.99200  -6.72200  1.000 102.42936 ?  205 ASP B C   1 
ATOM   3514 O O   . ASP B 1 197 ? 5.70700   -8.43700  -6.97000  1.000 93.65896  ?  205 ASP B O   1 
ATOM   3515 C CB  . ASP B 1 197 ? 4.53800   -9.70500  -9.11400  1.000 97.96116  ?  205 ASP B CB  1 
ATOM   3516 C CG  . ASP B 1 197 ? 3.77800   -10.47600 -10.17100 1.000 98.86183  ?  205 ASP B CG  1 
ATOM   3517 O OD1 . ASP B 1 197 ? 3.60600   -11.70000 -10.00400 1.000 94.44635  ?  205 ASP B OD1 1 
ATOM   3518 O OD2 . ASP B 1 197 ? 3.36500   -9.86000  -11.17500 1.000 96.89683  -1 205 ASP B OD2 1 
ATOM   3519 N N   . GLY B 1 198 ? 3.93200   -8.70500  -5.62800  1.000 103.31527 ?  206 GLY B N   1 
ATOM   3520 C CA  . GLY B 1 198 ? 4.38000   -7.63800  -4.76100  1.000 93.68363  ?  206 GLY B CA  1 
ATOM   3521 C C   . GLY B 1 198 ? 4.35200   -6.28300  -5.44300  1.000 95.91952  ?  206 GLY B C   1 
ATOM   3522 O O   . GLY B 1 198 ? 4.28600   -6.18100  -6.67700  1.000 96.06948  ?  206 GLY B O   1 
ATOM   3523 N N   . MET B 1 199 ? 4.42300   -5.21900  -4.64600  1.000 90.14759  ?  207 MET B N   1 
ATOM   3524 C CA  . MET B 1 199 ? 4.62500   -3.90400  -5.23300  1.000 87.93630  ?  207 MET B CA  1 
ATOM   3525 C C   . MET B 1 199 ? 5.94800   -3.83700  -5.97700  1.000 91.54994  ?  207 MET B C   1 
ATOM   3526 O O   . MET B 1 199 ? 6.11100   -2.99200  -6.86400  1.000 92.06592  ?  207 MET B O   1 
ATOM   3527 C CB  . MET B 1 199 ? 4.53700   -2.83300  -4.14800  1.000 86.56080  ?  207 MET B CB  1 
ATOM   3528 C CG  . MET B 1 199 ? 3.19500   -2.82100  -3.44300  1.000 87.88473  ?  207 MET B CG  1 
ATOM   3529 S SD  . MET B 1 199 ? 3.28900   -2.68700  -1.65300  1.000 93.11301  ?  207 MET B SD  1 
ATOM   3530 C CE  . MET B 1 199 ? 1.55300   -2.82300  -1.24200  1.000 80.03687  ?  207 MET B CE  1 
ATOM   3531 N N   . LEU B 1 200 ? 6.87200   -4.74800  -5.67000  1.000 95.51725  ?  208 LEU B N   1 
ATOM   3532 C CA  . LEU B 1 200 ? 8.11700   -4.89100  -6.41100  1.000 96.40013  ?  208 LEU B CA  1 
ATOM   3533 C C   . LEU B 1 200 ? 7.85100   -5.13900  -7.89000  1.000 97.25642  ?  208 LEU B C   1 
ATOM   3534 O O   . LEU B 1 200 ? 8.20000   -4.29800  -8.72600  1.000 93.97425  ?  208 LEU B O   1 
ATOM   3535 C CB  . LEU B 1 200 ? 8.96300   -6.02700  -5.82600  1.000 98.82090  ?  208 LEU B CB  1 
ATOM   3536 C CG  . LEU B 1 200 ? 9.35800   -5.94500  -4.34700  1.000 98.57948  ?  208 LEU B CG  1 
ATOM   3537 C CD1 . LEU B 1 200 ? 9.67600   -4.51000  -3.94200  1.000 81.17005  ?  208 LEU B CD1 1 
ATOM   3538 C CD2 . LEU B 1 200 ? 8.29300   -6.55200  -3.43800  1.000 90.10102  ?  208 LEU B CD2 1 
ATOM   3539 N N   . GLY B 1 201 ? 7.23200   -6.27300  -8.24000  1.000 96.21003  ?  209 GLY B N   1 
ATOM   3540 C CA  . GLY B 1 201 ? 6.95300   -6.53300  -9.63900  1.000 92.56819  ?  209 GLY B CA  1 
ATOM   3541 C C   . GLY B 1 201 ? 5.86600   -5.63400  -10.19200 1.000 93.86667  ?  209 GLY B C   1 
ATOM   3542 O O   . GLY B 1 201 ? 5.74100   -5.47500  -11.40800 1.000 96.49883  ?  209 GLY B O   1 
ATOM   3543 N N   . ALA B 1 202 ? 5.05300   -5.04500  -9.31200  1.000 89.43889  ?  210 ALA B N   1 
ATOM   3544 C CA  . ALA B 1 202 ? 4.08000   -4.06300  -9.77600  1.000 90.53704  ?  210 ALA B CA  1 
ATOM   3545 C C   . ALA B 1 202 ? 4.76900   -2.84500  -10.37600 1.000 87.17258  ?  210 ALA B C   1 
ATOM   3546 O O   . ALA B 1 202 ? 4.46300   -2.43100  -11.49900 1.000 88.21691  ?  210 ALA B O   1 
ATOM   3547 C CB  . ALA B 1 202 ? 3.16500   -3.65100  -8.62300  1.000 95.00990  ?  210 ALA B CB  1 
ATOM   3548 N N   . LEU B 1 203 ? 5.71400   -2.26200  -9.63800  1.000 84.41344  ?  211 LEU B N   1 
ATOM   3549 C CA  . LEU B 1 203 ? 6.42600   -1.08900  -10.12900 1.000 82.87215  ?  211 LEU B CA  1 
ATOM   3550 C C   . LEU B 1 203 ? 7.41600   -1.45000  -11.22800 1.000 87.05273  ?  211 LEU B C   1 
ATOM   3551 O O   . LEU B 1 203 ? 7.51600   -0.73700  -12.23300 1.000 84.16196  ?  211 LEU B O   1 
ATOM   3552 C CB  . LEU B 1 203 ? 7.14500   -0.39000  -8.97700  1.000 78.31588  ?  211 LEU B CB  1 
ATOM   3553 C CG  . LEU B 1 203 ? 6.31000   0.57900   -8.14100  1.000 77.95302  ?  211 LEU B CG  1 
ATOM   3554 C CD1 . LEU B 1 203 ? 7.20300   1.63700   -7.52600  1.000 79.21858  ?  211 LEU B CD1 1 
ATOM   3555 C CD2 . LEU B 1 203 ? 5.22000   1.22100   -8.98200  1.000 84.19959  ?  211 LEU B CD2 1 
ATOM   3556 N N   . LEU B 1 204 ? 8.15900   -2.54400  -11.05500 1.000 94.14465  ?  212 LEU B N   1 
ATOM   3557 C CA  . LEU B 1 204 ? 9.13800   -2.93100  -12.06500 1.000 98.95052  ?  212 LEU B CA  1 
ATOM   3558 C C   . LEU B 1 204 ? 8.46100   -3.35300  -13.36200 1.000 96.11295  ?  212 LEU B C   1 
ATOM   3559 O O   . LEU B 1 204 ? 8.97200   -3.07700  -14.45300 1.000 98.70972  ?  212 LEU B O   1 
ATOM   3560 C CB  . LEU B 1 204 ? 10.02900  -4.05200  -11.53100 1.000 98.17351  ?  212 LEU B CB  1 
ATOM   3561 C CG  . LEU B 1 204 ? 10.97900  -3.66600  -10.39700 1.000 82.35314  ?  212 LEU B CG  1 
ATOM   3562 C CD1 . LEU B 1 204 ? 11.78200  -4.87000  -9.94100  1.000 80.80266  ?  212 LEU B CD1 1 
ATOM   3563 C CD2 . LEU B 1 204 ? 11.89900  -2.53700  -10.83200 1.000 83.30296  ?  212 LEU B CD2 1 
ATOM   3564 N N   . GLY B 1 205 ? 7.31000   -4.01900  -13.26400 1.000 93.53205  ?  213 GLY B N   1 
ATOM   3565 C CA  . GLY B 1 205 ? 6.60800   -4.47200  -14.45100 1.000 98.98795  ?  213 GLY B CA  1 
ATOM   3566 C C   . GLY B 1 205 ? 5.92400   -3.36400  -15.22300 1.000 99.44273  ?  213 GLY B C   1 
ATOM   3567 O O   . GLY B 1 205 ? 5.49200   -3.58700  -16.35800 1.000 93.49334  ?  213 GLY B O   1 
ATOM   3568 N N   . ALA B 1 206 ? 5.81500   -2.17600  -14.63700 1.000 96.28462  ?  214 ALA B N   1 
ATOM   3569 C CA  . ALA B 1 206 ? 5.19500   -1.04500  -15.31500 1.000 94.98126  ?  214 ALA B CA  1 
ATOM   3570 C C   . ALA B 1 206 ? 6.24900   -0.18100  -15.99800 1.000 89.05116  ?  214 ALA B C   1 
ATOM   3571 O O   . ALA B 1 206 ? 5.96100   0.50800   -16.97600 1.000 89.48979  ?  214 ALA B O   1 
ATOM   3572 C CB  . ALA B 1 206 ? 4.38500   -0.21600  -14.33500 1.000 90.13037  ?  214 ALA B CB  1 
ATOM   3573 N N   . LEU B 1 215 ? 17.49800  -3.30600  -12.07500 1.000 83.26350  ?  223 LEU B N   1 
ATOM   3574 C CA  . LEU B 1 215 ? 17.26800  -3.01000  -10.66700 1.000 84.43640  ?  223 LEU B CA  1 
ATOM   3575 C C   . LEU B 1 215 ? 18.58100  -2.95900  -9.89500  1.000 91.07931  ?  223 LEU B C   1 
ATOM   3576 O O   . LEU B 1 215 ? 18.76200  -2.11800  -9.01600  1.000 91.20373  ?  223 LEU B O   1 
ATOM   3577 C CB  . LEU B 1 215 ? 16.33400  -4.04900  -10.04400 1.000 82.51691  ?  223 LEU B CB  1 
ATOM   3578 C CG  . LEU B 1 215 ? 16.05300  -3.88800  -8.54900  1.000 74.52949  ?  223 LEU B CG  1 
ATOM   3579 C CD1 . LEU B 1 215 ? 15.34800  -2.57000  -8.28300  1.000 86.59002  ?  223 LEU B CD1 1 
ATOM   3580 C CD2 . LEU B 1 215 ? 15.23000  -5.05300  -8.02600  1.000 67.50035  ?  223 LEU B CD2 1 
ATOM   3581 N N   . ALA B 1 216 ? 19.49600  -3.87000  -10.23500 1.000 96.66714  ?  224 ALA B N   1 
ATOM   3582 C CA  . ALA B 1 216 ? 20.77700  -3.93000  -9.53900  1.000 93.41896  ?  224 ALA B CA  1 
ATOM   3583 C C   . ALA B 1 216 ? 21.63100  -2.70000  -9.81500  1.000 95.06696  ?  224 ALA B C   1 
ATOM   3584 O O   . ALA B 1 216 ? 22.53600  -2.38800  -9.03200  1.000 95.63860  ?  224 ALA B O   1 
ATOM   3585 C CB  . ALA B 1 216 ? 21.53100  -5.19900  -9.93300  1.000 82.82558  ?  224 ALA B CB  1 
ATOM   3586 N N   . GLN B 1 217 ? 21.36700  -1.99300  -10.91600 1.000 95.62722  ?  225 GLN B N   1 
ATOM   3587 C CA  . GLN B 1 217 ? 22.14700  -0.80200  -11.23000 1.000 97.92927  ?  225 GLN B CA  1 
ATOM   3588 C C   . GLN B 1 217 ? 21.91000  0.30900   -10.21700 1.000 94.03305  ?  225 GLN B C   1 
ATOM   3589 O O   . GLN B 1 217 ? 22.81600  1.10500   -9.94700  1.000 89.47792  ?  225 GLN B O   1 
ATOM   3590 C CB  . GLN B 1 217 ? 21.81600  -0.31400  -12.64100 1.000 96.79822  ?  225 GLN B CB  1 
ATOM   3591 C CG  . GLN B 1 217 ? 22.09200  -1.32900  -13.74300 1.000 95.53653  ?  225 GLN B CG  1 
ATOM   3592 C CD  . GLN B 1 217 ? 23.33500  -2.15700  -13.48700 1.000 92.34321  ?  225 GLN B CD  1 
ATOM   3593 O OE1 . GLN B 1 217 ? 24.45500  -1.70400  -13.71900 1.000 87.60962  ?  225 GLN B OE1 1 
ATOM   3594 N NE2 . GLN B 1 217 ? 23.14200  -3.38400  -13.01600 1.000 84.30992  ?  225 GLN B NE2 1 
ATOM   3595 N N   . LEU B 1 218 ? 20.71100  0.38200   -9.65300  1.000 91.57789  ?  226 LEU B N   1 
ATOM   3596 C CA  . LEU B 1 218 ? 20.39500  1.42900   -8.68700  1.000 89.65205  ?  226 LEU B CA  1 
ATOM   3597 C C   . LEU B 1 218 ? 21.02700  1.10800   -7.33700  1.000 86.45389  ?  226 LEU B C   1 
ATOM   3598 O O   . LEU B 1 218 ? 20.82700  0.00800   -6.81100  1.000 81.78790  ?  226 LEU B O   1 
ATOM   3599 C CB  . LEU B 1 218 ? 18.88400  1.59900   -8.53600  1.000 86.55768  ?  226 LEU B CB  1 
ATOM   3600 C CG  . LEU B 1 218 ? 18.04800  1.86800   -9.79400  1.000 104.14978 ?  226 LEU B CG  1 
ATOM   3601 C CD1 . LEU B 1 218 ? 18.75200  2.87000   -10.70600 1.000 100.42292 ?  226 LEU B CD1 1 
ATOM   3602 C CD2 . LEU B 1 218 ? 17.68100  0.59600   -10.55400 1.000 96.16771  ?  226 LEU B CD2 1 
ATOM   3603 N N   . PRO B 1 219 ? 21.79300  2.03300   -6.75600  1.000 79.77874  ?  227 PRO B N   1 
ATOM   3604 C CA  . PRO B 1 219 ? 22.45400  1.74200   -5.47200  1.000 78.10423  ?  227 PRO B CA  1 
ATOM   3605 C C   . PRO B 1 219 ? 21.49300  1.47000   -4.33100  1.000 71.27444  ?  227 PRO B C   1 
ATOM   3606 O O   . PRO B 1 219 ? 21.87600  0.80300   -3.36200  1.000 64.78530  ?  227 PRO B O   1 
ATOM   3607 C CB  . PRO B 1 219 ? 23.28500  3.00600   -5.21200  1.000 71.39984  ?  227 PRO B CB  1 
ATOM   3608 C CG  . PRO B 1 219 ? 22.69300  4.06000   -6.08700  1.000 70.55361  ?  227 PRO B CG  1 
ATOM   3609 C CD  . PRO B 1 219 ? 22.14800  3.35900   -7.28300  1.000 73.84760  ?  227 PRO B CD  1 
ATOM   3610 N N   . GLU B 1 220 ? 20.25900  1.97100   -4.40500  1.000 65.97930  ?  228 GLU B N   1 
ATOM   3611 C CA  . GLU B 1 220 ? 19.29200  1.74000   -3.34000  1.000 64.53361  ?  228 GLU B CA  1 
ATOM   3612 C C   . GLU B 1 220 ? 18.94500  0.26800   -3.16800  1.000 71.40038  ?  228 GLU B C   1 
ATOM   3613 O O   . GLU B 1 220 ? 18.43000  -0.10900  -2.10900  1.000 66.33642  ?  228 GLU B O   1 
ATOM   3614 C CB  . GLU B 1 220 ? 18.02000  2.54700   -3.60000  1.000 63.22913  ?  228 GLU B CB  1 
ATOM   3615 C CG  . GLU B 1 220 ? 18.11500  4.01000   -3.19600  1.000 69.12567  ?  228 GLU B CG  1 
ATOM   3616 C CD  . GLU B 1 220 ? 18.65900  4.89600   -4.30000  1.000 78.59860  ?  228 GLU B CD  1 
ATOM   3617 O OE1 . GLU B 1 220 ? 18.96500  4.37400   -5.39200  1.000 82.97767  ?  228 GLU B OE1 1 
ATOM   3618 O OE2 . GLU B 1 220 ? 18.78000  6.11800   -4.07500  1.000 73.66210  -1 228 GLU B OE2 1 
ATOM   3619 N N   . ALA B 1 221 ? 19.21200  -0.56900  -4.17200  1.000 69.02585  ?  229 ALA B N   1 
ATOM   3620 C CA  . ALA B 1 221 ? 18.95900  -1.99800  -4.05600  1.000 60.94973  ?  229 ALA B CA  1 
ATOM   3621 C C   . ALA B 1 221 ? 19.97700  -2.70600  -3.17600  1.000 67.15628  ?  229 ALA B C   1 
ATOM   3622 O O   . ALA B 1 221 ? 19.75900  -3.86800  -2.81800  1.000 69.03727  ?  229 ALA B O   1 
ATOM   3623 C CB  . ALA B 1 221 ? 18.94700  -2.64100  -5.44300  1.000 65.58767  ?  229 ALA B CB  1 
ATOM   3624 N N   . HIS B 1 222 ? 21.07200  -2.04300  -2.82000  1.000 68.39051  ?  230 HIS B N   1 
ATOM   3625 C CA  . HIS B 1 222 ? 22.13500  -2.65200  -2.03500  1.000 65.80139  ?  230 HIS B CA  1 
ATOM   3626 C C   . HIS B 1 222 ? 22.44400  -1.91300  -0.74500  1.000 56.21056  ?  230 HIS B C   1 
ATOM   3627 O O   . HIS B 1 222 ? 22.90500  -2.54000  0.21000   1.000 47.44873  ?  230 HIS B O   1 
ATOM   3628 C CB  . HIS B 1 222 ? 23.42000  -2.74800  -2.87000  1.000 61.38646  ?  230 HIS B CB  1 
ATOM   3629 C CG  . HIS B 1 222 ? 23.22100  -3.37700  -4.21300  1.000 71.88920  ?  230 HIS B CG  1 
ATOM   3630 N ND1 . HIS B 1 222 ? 23.13100  -4.74100  -4.39000  1.000 64.32101  ?  230 HIS B ND1 1 
ATOM   3631 C CD2 . HIS B 1 222 ? 23.08200  -2.82900  -5.44300  1.000 77.73593  ?  230 HIS B CD2 1 
ATOM   3632 C CE1 . HIS B 1 222 ? 22.95200  -5.00500  -5.67100  1.000 70.32791  ?  230 HIS B CE1 1 
ATOM   3633 N NE2 . HIS B 1 222 ? 22.91800  -3.86200  -6.33200  1.000 65.72198  ?  230 HIS B NE2 1 
ATOM   3634 N N   . PHE B 1 223 ? 22.20800  -0.60600  -0.68900  1.000 56.16429  ?  231 PHE B N   1 
ATOM   3635 C CA  . PHE B 1 223 ? 22.52800  0.19900   0.47800   1.000 50.91757  ?  231 PHE B CA  1 
ATOM   3636 C C   . PHE B 1 223 ? 21.31600  1.00700   0.90600   1.000 52.10590  ?  231 PHE B C   1 
ATOM   3637 O O   . PHE B 1 223 ? 20.66600  1.65800   0.08300   1.000 56.97836  ?  231 PHE B O   1 
ATOM   3638 C CB  . PHE B 1 223 ? 23.70100  1.13200   0.19000   1.000 48.33689  ?  231 PHE B CB  1 
ATOM   3639 C CG  . PHE B 1 223 ? 24.99800  0.41700   0.00800   1.000 47.57141  ?  231 PHE B CG  1 
ATOM   3640 C CD1 . PHE B 1 223 ? 25.47000  -0.43900  0.98500   1.000 51.73204  ?  231 PHE B CD1 1 
ATOM   3641 C CD2 . PHE B 1 223 ? 25.75000  0.60200   -1.13200  1.000 46.43829  ?  231 PHE B CD2 1 
ATOM   3642 C CE1 . PHE B 1 223 ? 26.66400  -1.10100  0.82300   1.000 52.68328  ?  231 PHE B CE1 1 
ATOM   3643 C CE2 . PHE B 1 223 ? 26.94100  -0.06000  -1.30000  1.000 41.82509  ?  231 PHE B CE2 1 
ATOM   3644 C CZ  . PHE B 1 223 ? 27.40100  -0.91100  -0.32100  1.000 42.72602  ?  231 PHE B CZ  1 
ATOM   3645 N N   . THR B 1 224 ? 21.02300  0.96400   2.20200   1.000 50.80465  ?  232 THR B N   1 
ATOM   3646 C CA  . THR B 1 224 ? 19.94700  1.75200   2.77700   1.000 53.47973  ?  232 THR B CA  1 
ATOM   3647 C C   . THR B 1 224 ? 20.35700  2.15800   4.18400   1.000 56.30849  ?  232 THR B C   1 
ATOM   3648 O O   . THR B 1 224 ? 21.24300  1.55200   4.79100   1.000 49.82703  ?  232 THR B O   1 
ATOM   3649 C CB  . THR B 1 224 ? 18.62100  0.98300   2.78800   1.000 49.66514  ?  232 THR B CB  1 
ATOM   3650 O OG1 . THR B 1 224 ? 17.54400  1.88600   3.06600   1.000 60.82399  ?  232 THR B OG1 1 
ATOM   3651 C CG2 . THR B 1 224 ? 18.64300  -0.11000  3.84000   1.000 37.86609  ?  232 THR B CG2 1 
ATOM   3652 N N   . VAL B 1 225 ? 19.71200  3.20400   4.69300   1.000 51.38132  ?  233 VAL B N   1 
ATOM   3653 C CA  . VAL B 1 225 ? 20.06400  3.72500   6.00700   1.000 41.43403  ?  233 VAL B CA  1 
ATOM   3654 C C   . VAL B 1 225 ? 19.57800  2.75600   7.07500   1.000 48.38981  ?  233 VAL B C   1 
ATOM   3655 O O   . VAL B 1 225 ? 18.39300  2.40800   7.12900   1.000 47.37470  ?  233 VAL B O   1 
ATOM   3656 C CB  . VAL B 1 225 ? 19.48000  5.12600   6.21900   1.000 42.63987  ?  233 VAL B CB  1 
ATOM   3657 C CG1 . VAL B 1 225 ? 19.55100  5.50700   7.68500   1.000 52.30017  ?  233 VAL B CG1 1 
ATOM   3658 C CG2 . VAL B 1 225 ? 20.23500  6.13500   5.38400   1.000 43.58748  ?  233 VAL B CG2 1 
ATOM   3659 N N   . GLN B 1 226 ? 20.49700  2.31400   7.92900   1.000 47.28985  ?  234 GLN B N   1 
ATOM   3660 C CA  . GLN B 1 226 ? 20.16800  1.44100   9.04500   1.000 48.68924  ?  234 GLN B CA  1 
ATOM   3661 C C   . GLN B 1 226 ? 20.60700  1.97900   10.39500  1.000 54.12812  ?  234 GLN B C   1 
ATOM   3662 O O   . GLN B 1 226 ? 20.19000  1.42300   11.41600  1.000 54.13622  ?  234 GLN B O   1 
ATOM   3663 C CB  . GLN B 1 226 ? 20.80000  0.05500   8.85300   1.000 43.79845  ?  234 GLN B CB  1 
ATOM   3664 C CG  . GLN B 1 226 ? 20.41900  -0.64100  7.56800   1.000 44.27823  ?  234 GLN B CG  1 
ATOM   3665 C CD  . GLN B 1 226 ? 20.98100  -2.04200  7.49100   1.000 46.71812  ?  234 GLN B CD  1 
ATOM   3666 O OE1 . GLN B 1 226 ? 20.73700  -2.86900  8.36500   1.000 47.46069  ?  234 GLN B OE1 1 
ATOM   3667 N NE2 . GLN B 1 226 ? 21.74800  -2.31300  6.44500   1.000 58.97689  ?  234 GLN B NE2 1 
ATOM   3668 N N   . ALA B 1 227 ? 21.42700  3.02500   10.44400  1.000 45.35218  ?  235 ALA B N   1 
ATOM   3669 C CA  . ALA B 1 227 ? 21.97400  3.49600   11.70500  1.000 41.73814  ?  235 ALA B CA  1 
ATOM   3670 C C   . ALA B 1 227 ? 22.40000  4.94800   11.57200  1.000 49.63163  ?  235 ALA B C   1 
ATOM   3671 O O   . ALA B 1 227 ? 22.35400  5.53800   10.49000  1.000 53.72318  ?  235 ALA B O   1 
ATOM   3672 C CB  . ALA B 1 227 ? 23.16300  2.63900   12.15200  1.000 40.08517  ?  235 ALA B CB  1 
ATOM   3673 N N   . PHE B 1 228 ? 22.79800  5.52100   12.70300  1.000 46.35698  ?  236 PHE B N   1 
ATOM   3674 C CA  . PHE B 1 228 ? 23.40000  6.84500   12.75300  1.000 46.27292  ?  236 PHE B CA  1 
ATOM   3675 C C   . PHE B 1 228 ? 24.33700  6.91100   13.94700  1.000 42.14801  ?  236 PHE B C   1 
ATOM   3676 O O   . PHE B 1 228 ? 24.00600  6.41300   15.02700  1.000 46.65342  ?  236 PHE B O   1 
ATOM   3677 C CB  . PHE B 1 228 ? 22.34100  7.94800   12.84600  1.000 43.09908  ?  236 PHE B CB  1 
ATOM   3678 C CG  . PHE B 1 228 ? 22.90600  9.33700   12.75100  1.000 43.02500  ?  236 PHE B CG  1 
ATOM   3679 C CD1 . PHE B 1 228 ? 23.08100  9.94300   11.52100  1.000 45.80489  ?  236 PHE B CD1 1 
ATOM   3680 C CD2 . PHE B 1 228 ? 23.27200  10.03000  13.89000  1.000 52.12046  ?  236 PHE B CD2 1 
ATOM   3681 C CE1 . PHE B 1 228 ? 23.60300  11.21600  11.43000  1.000 45.54881  ?  236 PHE B CE1 1 
ATOM   3682 C CE2 . PHE B 1 228 ? 23.79600  11.30400  13.80400  1.000 50.20136  ?  236 PHE B CE2 1 
ATOM   3683 C CZ  . PHE B 1 228 ? 23.96100  11.89700  12.57200  1.000 44.79790  ?  236 PHE B CZ  1 
ATOM   3684 N N   . VAL B 1 229 ? 25.49800  7.52800   13.74900  1.000 39.42540  ?  237 VAL B N   1 
ATOM   3685 C CA  . VAL B 1 229 ? 26.51400  7.67100   14.78600  1.000 38.63444  ?  237 VAL B CA  1 
ATOM   3686 C C   . VAL B 1 229 ? 26.72100  9.15500   15.05100  1.000 41.54300  ?  237 VAL B C   1 
ATOM   3687 O O   . VAL B 1 229 ? 27.02100  9.92400   14.12900  1.000 42.20862  ?  237 VAL B O   1 
ATOM   3688 C CB  . VAL B 1 229 ? 27.83300  6.99300   14.38500  1.000 36.99600  ?  237 VAL B CB  1 
ATOM   3689 C CG1 . VAL B 1 229 ? 28.67500  6.70500   15.61300  1.000 37.53991  ?  237 VAL B CG1 1 
ATOM   3690 C CG2 . VAL B 1 229 ? 27.56000  5.71300   13.62200  1.000 35.65951  ?  237 VAL B CG2 1 
ATOM   3691 N N   . GLN B 1 230 ? 26.56700  9.55300   16.30900  1.000 43.17298  ?  238 GLN B N   1 
ATOM   3692 C CA  . GLN B 1 230 ? 26.81800  10.91800  16.74900  1.000 40.83981  ?  238 GLN B CA  1 
ATOM   3693 C C   . GLN B 1 230 ? 28.09400  10.94400  17.57800  1.000 36.53370  ?  238 GLN B C   1 
ATOM   3694 O O   . GLN B 1 230 ? 28.33200  10.04100  18.38600  1.000 39.25904  ?  238 GLN B O   1 
ATOM   3695 C CB  . GLN B 1 230 ? 25.64100  11.45700  17.56200  1.000 42.81583  ?  238 GLN B CB  1 
ATOM   3696 C CG  . GLN B 1 230 ? 25.82300  12.88100  18.06700  1.000 42.21550  ?  238 GLN B CG  1 
ATOM   3697 C CD  . GLN B 1 230 ? 25.68000  13.91500  16.96900  1.000 44.42828  ?  238 GLN B CD  1 
ATOM   3698 O OE1 . GLN B 1 230 ? 26.51500  14.80700  16.83000  1.000 41.84269  ?  238 GLN B OE1 1 
ATOM   3699 N NE2 . GLN B 1 230 ? 24.61900  13.79900  16.18100  1.000 46.10451  ?  238 GLN B NE2 1 
ATOM   3700 N N   . THR B 1 231 ? 28.91000  11.97300  17.37800  1.000 35.88156  ?  239 THR B N   1 
ATOM   3701 C CA  . THR B 1 231 ? 30.22800  12.05000  17.98600  1.000 38.16346  ?  239 THR B CA  1 
ATOM   3702 C C   . THR B 1 231 ? 30.33100  13.24000  18.93100  1.000 43.20804  ?  239 THR B C   1 
ATOM   3703 O O   . THR B 1 231 ? 29.85800  14.33800  18.62300  1.000 44.63582  ?  239 THR B O   1 
ATOM   3704 C CB  . THR B 1 231 ? 31.31600  12.14900  16.91800  1.000 34.03458  ?  239 THR B CB  1 
ATOM   3705 O OG1 . THR B 1 231 ? 31.05500  13.27600  16.07400  1.000 37.61000  ?  239 THR B OG1 1 
ATOM   3706 C CG2 . THR B 1 231 ? 31.34300  10.88900  16.07800  1.000 36.71850  ?  239 THR B CG2 1 
ATOM   3707 N N   . LEU B 1 232 ? 30.95300  13.00400  20.08100  1.000 44.81103  ?  240 LEU B N   1 
ATOM   3708 C CA  . LEU B 1 232 ? 31.30500  14.04400  21.03500  1.000 43.69085  ?  240 LEU B CA  1 
ATOM   3709 C C   . LEU B 1 232 ? 32.81700  14.07200  21.21000  1.000 47.91754  ?  240 LEU B C   1 
ATOM   3710 O O   . LEU B 1 232 ? 33.47900  13.03500  21.12100  1.000 48.21958  ?  240 LEU B O   1 
ATOM   3711 C CB  . LEU B 1 232 ? 30.63100  13.81200  22.38900  1.000 39.56635  ?  240 LEU B CB  1 
ATOM   3712 C CG  . LEU B 1 232 ? 29.10600  13.75800  22.41200  1.000 37.44929  ?  240 LEU B CG  1 
ATOM   3713 C CD1 . LEU B 1 232 ? 28.62500  13.28700  23.76700  1.000 31.41671  ?  240 LEU B CD1 1 
ATOM   3714 C CD2 . LEU B 1 232 ? 28.52500  15.11800  22.08200  1.000 42.75862  ?  240 LEU B CD2 1 
ATOM   3715 N N   . SER B 1 233 ? 33.35700  15.26000  21.45700  1.000 48.70732  ?  241 SER B N   1 
ATOM   3716 C CA  . SER B 1 233 ? 34.79000  15.44900  21.60200  1.000 45.63191  ?  241 SER B CA  1 
ATOM   3717 C C   . SER B 1 233 ? 35.08900  16.31200  22.82100  1.000 45.07904  ?  241 SER B C   1 
ATOM   3718 O O   . SER B 1 233 ? 34.25900  17.10800  23.26500  1.000 49.39360  ?  241 SER B O   1 
ATOM   3719 C CB  . SER B 1 233 ? 35.39500  16.09000  20.34700  1.000 51.65963  ?  241 SER B CB  1 
ATOM   3720 O OG  . SER B 1 233 ? 35.15900  15.29000  19.20200  1.000 58.57801  ?  241 SER B OG  1 
ATOM   3721 N N   . GLY B 1 234 ? 36.29200  16.14100  23.35600  1.000 42.57152  ?  242 GLY B N   1 
ATOM   3722 C CA  . GLY B 1 234 ? 36.71600  16.95900  24.48000  1.000 40.12882  ?  242 GLY B CA  1 
ATOM   3723 C C   . GLY B 1 234 ? 35.98700  16.57600  25.75000  1.000 43.30539  ?  242 GLY B C   1 
ATOM   3724 O O   . GLY B 1 234 ? 35.64500  15.40900  25.97000  1.000 49.26285  ?  242 GLY B O   1 
ATOM   3725 N N   . ALA B 1 235 ? 35.74500  17.57400  26.60400  1.000 42.44260  ?  243 ALA B N   1 
ATOM   3726 C CA  . ALA B 1 235 ? 35.05000  17.32600  27.86200  1.000 38.05148  ?  243 ALA B CA  1 
ATOM   3727 C C   . ALA B 1 235 ? 33.63800  16.80800  27.63400  1.000 44.54759  ?  243 ALA B C   1 
ATOM   3728 O O   . ALA B 1 235 ? 33.09600  16.09600  28.48600  1.000 43.33082  ?  243 ALA B O   1 
ATOM   3729 C CB  . ALA B 1 235 ? 35.01800  18.60100  28.70300  1.000 38.29852  ?  243 ALA B CB  1 
ATOM   3730 N N   . ALA B 1 236 ? 33.03000  17.14800  26.49400  1.000 46.30770  ?  244 ALA B N   1 
ATOM   3731 C CA  . ALA B 1 236 ? 31.71000  16.62100  26.17000  1.000 43.50862  ?  244 ALA B CA  1 
ATOM   3732 C C   . ALA B 1 236 ? 31.72600  15.10400  26.05400  1.000 40.54928  ?  244 ALA B C   1 
ATOM   3733 O O   . ALA B 1 236 ? 30.69200  14.45800  26.25100  1.000 36.98218  ?  244 ALA B O   1 
ATOM   3734 C CB  . ALA B 1 236 ? 31.19700  17.24900  24.87600  1.000 34.90268  ?  244 ALA B CB  1 
ATOM   3735 N N   . ALA B 1 237 ? 32.88300  14.51900  25.73700  1.000 42.46699  ?  245 ALA B N   1 
ATOM   3736 C CA  . ALA B 1 237 ? 32.99100  13.06900  25.67900  1.000 43.34537  ?  245 ALA B CA  1 
ATOM   3737 C C   . ALA B 1 237 ? 32.93800  12.42700  27.05900  1.000 53.65710  ?  245 ALA B C   1 
ATOM   3738 O O   . ALA B 1 237 ? 32.71000  11.21700  27.15400  1.000 43.96910  ?  245 ALA B O   1 
ATOM   3739 C CB  . ALA B 1 237 ? 34.28200  12.66400  24.97100  1.000 38.05953  ?  245 ALA B CB  1 
ATOM   3740 N N   . ARG B 1 238 ? 33.13800  13.20300  28.12500  1.000 44.01681  ?  246 ARG B N   1 
ATOM   3741 C CA  . ARG B 1 238 ? 33.13300  12.68400  29.48800  1.000 33.56865  ?  246 ARG B CA  1 
ATOM   3742 C C   . ARG B 1 238 ? 31.97800  13.25200  30.30400  1.000 37.98122  ?  246 ARG B C   1 
ATOM   3743 O O   . ARG B 1 238 ? 32.06800  13.34900  31.52800  1.000 40.31946  ?  246 ARG B O   1 
ATOM   3744 C CB  . ARG B 1 238 ? 34.45900  12.97500  30.18500  1.000 27.31061  ?  246 ARG B CB  1 
ATOM   3745 C CG  . ARG B 1 238 ? 35.67700  12.57800  29.38500  1.000 32.33882  ?  246 ARG B CG  1 
ATOM   3746 C CD  . ARG B 1 238 ? 36.91600  12.55600  30.25400  1.000 27.26706  ?  246 ARG B CD  1 
ATOM   3747 N NE  . ARG B 1 238 ? 37.87400  11.56800  29.78000  1.000 34.27278  ?  246 ARG B NE  1 
ATOM   3748 C CZ  . ARG B 1 238 ? 37.87300  10.29400  30.13900  1.000 32.83512  ?  246 ARG B CZ  1 
ATOM   3749 N NH1 . ARG B 1 238 ? 36.99900  9.82200   31.01000  1.000 30.77743  ?  246 ARG B NH1 1 
ATOM   3750 N NH2 . ARG B 1 238 ? 38.77100  9.47100   29.60800  1.000 39.91200  ?  246 ARG B NH2 1 
ATOM   3751 N N   . ASN B 1 239 ? 30.88800  13.62800  29.64200  1.000 41.88973  ?  247 ASN B N   1 
ATOM   3752 C CA  . ASN B 1 239 ? 29.73800  14.23100  30.30200  1.000 47.62171  ?  247 ASN B CA  1 
ATOM   3753 C C   . ASN B 1 239 ? 28.50100  13.40000  29.99700  1.000 40.17962  ?  247 ASN B C   1 
ATOM   3754 O O   . ASN B 1 239 ? 28.20400  13.12800  28.83000  1.000 39.39902  ?  247 ASN B O   1 
ATOM   3755 C CB  . ASN B 1 239 ? 29.55200  15.68000  29.84800  1.000 41.03155  ?  247 ASN B CB  1 
ATOM   3756 C CG  . ASN B 1 239 ? 28.66500  16.47200  30.77700  1.000 40.31308  ?  247 ASN B CG  1 
ATOM   3757 O OD1 . ASN B 1 239 ? 27.58800  16.02300  31.16200  1.000 48.11719  ?  247 ASN B OD1 1 
ATOM   3758 N ND2 . ASN B 1 239 ? 29.12200  17.65600  31.15800  1.000 44.78543  ?  247 ASN B ND2 1 
ATOM   3759 N N   . ALA B 1 240 ? 27.78300  12.99800  31.04900  1.000 36.12024  ?  248 ALA B N   1 
ATOM   3760 C CA  . ALA B 1 240 ? 26.58800  12.18200  30.86400  1.000 44.10893  ?  248 ALA B CA  1 
ATOM   3761 C C   . ALA B 1 240 ? 25.46700  12.96100  30.19000  1.000 50.14193  ?  248 ALA B C   1 
ATOM   3762 O O   . ALA B 1 240 ? 24.72000  12.39700  29.38100  1.000 54.10752  ?  248 ALA B O   1 
ATOM   3763 C CB  . ALA B 1 240 ? 26.11900  11.62800  32.20900  1.000 41.94959  ?  248 ALA B CB  1 
ATOM   3764 N N   . GLU B 1 241 ? 25.32300  14.24800  30.51800  1.000 47.21126  ?  249 GLU B N   1 
ATOM   3765 C CA  . GLU B 1 241 ? 24.32000  15.07200  29.85100  1.000 52.46002  ?  249 GLU B CA  1 
ATOM   3766 C C   . GLU B 1 241 ? 24.57700  15.13000  28.35400  1.000 42.69286  ?  249 GLU B C   1 
ATOM   3767 O O   . GLU B 1 241 ? 23.64800  14.99100  27.54700  1.000 42.60241  ?  249 GLU B O   1 
ATOM   3768 C CB  . GLU B 1 241 ? 24.32100  16.48400  30.43700  1.000 55.53683  ?  249 GLU B CB  1 
ATOM   3769 C CG  . GLU B 1 241 ? 24.11500  16.56100  31.93700  1.000 60.81493  ?  249 GLU B CG  1 
ATOM   3770 C CD  . GLU B 1 241 ? 22.68900  16.27400  32.34200  1.000 72.70187  ?  249 GLU B CD  1 
ATOM   3771 O OE1 . GLU B 1 241 ? 21.85200  17.19700  32.27200  1.000 80.78888  ?  249 GLU B OE1 1 
ATOM   3772 O OE2 . GLU B 1 241 ? 22.40200  15.12500  32.72900  1.000 70.60662  -1 249 GLU B OE2 1 
ATOM   3773 N N   . GLU B 1 242 ? 25.83600  15.33200  27.96700  1.000 43.08452  ?  250 GLU B N   1 
ATOM   3774 C CA  . GLU B 1 242 ? 26.18100  15.35100  26.55400  1.000 45.81536  ?  250 GLU B CA  1 
ATOM   3775 C C   . GLU B 1 242 ? 25.92000  13.99900  25.90800  1.000 46.37254  ?  250 GLU B C   1 
ATOM   3776 O O   . GLU B 1 242 ? 25.48400  13.93500  24.75700  1.000 47.27960  ?  250 GLU B O   1 
ATOM   3777 C CB  . GLU B 1 242 ? 27.64100  15.76400  26.37400  1.000 46.09870  ?  250 GLU B CB  1 
ATOM   3778 C CG  . GLU B 1 242 ? 27.96500  17.14900  26.90300  1.000 48.20294  ?  250 GLU B CG  1 
ATOM   3779 C CD  . GLU B 1 242 ? 27.56900  18.25200  25.94200  1.000 70.60095  ?  250 GLU B CD  1 
ATOM   3780 O OE1 . GLU B 1 242 ? 27.31500  17.95100  24.75700  1.000 61.48453  ?  250 GLU B OE1 1 
ATOM   3781 O OE2 . GLU B 1 242 ? 27.51300  19.42300  26.37300  1.000 79.81702  -1 250 GLU B OE2 1 
ATOM   3782 N N   . TYR B 1 243 ? 26.18000  12.90700  26.63100  1.000 43.16434  ?  251 TYR B N   1 
ATOM   3783 C CA  . TYR B 1 243 ? 25.92600  11.58100  26.07400  1.000 42.00099  ?  251 TYR B CA  1 
ATOM   3784 C C   . TYR B 1 243 ? 24.44200  11.37300  25.80700  1.000 42.75707  ?  251 TYR B C   1 
ATOM   3785 O O   . TYR B 1 243 ? 24.05700  10.85300  24.75400  1.000 48.22188  ?  251 TYR B O   1 
ATOM   3786 C CB  . TYR B 1 243 ? 26.45300  10.49600  27.01300  1.000 41.28176  ?  251 TYR B CB  1 
ATOM   3787 C CG  . TYR B 1 243 ? 25.81300  9.14500   26.77600  1.000 43.47278  ?  251 TYR B CG  1 
ATOM   3788 C CD1 . TYR B 1 243 ? 26.27200  8.30800   25.77100  1.000 40.87922  ?  251 TYR B CD1 1 
ATOM   3789 C CD2 . TYR B 1 243 ? 24.74000  8.71300   27.54600  1.000 44.22940  ?  251 TYR B CD2 1 
ATOM   3790 C CE1 . TYR B 1 243 ? 25.68900  7.07900   25.54400  1.000 38.34984  ?  251 TYR B CE1 1 
ATOM   3791 C CE2 . TYR B 1 243 ? 24.15200  7.48600   27.32300  1.000 39.69567  ?  251 TYR B CE2 1 
ATOM   3792 C CZ  . TYR B 1 243 ? 24.63100  6.67300   26.32300  1.000 39.48223  ?  251 TYR B CZ  1 
ATOM   3793 O OH  . TYR B 1 243 ? 24.04700  5.45000   26.10200  1.000 46.62518  ?  251 TYR B OH  1 
ATOM   3794 N N   . ARG B 1 244 ? 23.59100  11.75300  26.76100  1.000 41.94798  ?  252 ARG B N   1 
ATOM   3795 C CA  . ARG B 1 244 ? 22.15500  11.59100  26.56300  1.000 45.24587  ?  252 ARG B CA  1 
ATOM   3796 C C   . ARG B 1 244 ? 21.65000  12.48100  25.43600  1.000 46.31143  ?  252 ARG B C   1 
ATOM   3797 O O   . ARG B 1 244 ? 20.81400  12.05900  24.62300  1.000 49.61503  ?  252 ARG B O   1 
ATOM   3798 C CB  . ARG B 1 244 ? 21.41000  11.88800  27.86200  1.000 49.02118  ?  252 ARG B CB  1 
ATOM   3799 C CG  . ARG B 1 244 ? 21.12300  10.65500  28.69600  1.000 57.64891  ?  252 ARG B CG  1 
ATOM   3800 C CD  . ARG B 1 244 ? 20.67300  11.02700  30.09300  1.000 64.40206  ?  252 ARG B CD  1 
ATOM   3801 N NE  . ARG B 1 244 ? 21.79400  11.29100  30.98500  1.000 69.51074  ?  252 ARG B NE  1 
ATOM   3802 C CZ  . ARG B 1 244 ? 21.77000  12.18100  31.96600  1.000 67.32790  ?  252 ARG B CZ  1 
ATOM   3803 N NH1 . ARG B 1 244 ? 20.70900  12.94000  32.18300  1.000 70.29813  ?  252 ARG B NH1 1 
ATOM   3804 N NH2 . ARG B 1 244 ? 22.83500  12.31100  32.75100  1.000 56.28642  ?  252 ARG B NH2 1 
ATOM   3805 N N   . ALA B 1 245 ? 22.14800  13.71700  25.36900  1.000 37.87395  ?  253 ALA B N   1 
ATOM   3806 C CA  . ALA B 1 245 ? 21.77600  14.59900  24.27000  1.000 45.98759  ?  253 ALA B CA  1 
ATOM   3807 C C   . ALA B 1 245 ? 22.19700  14.01000  22.93100  1.000 49.96177  ?  253 ALA B C   1 
ATOM   3808 O O   . ALA B 1 245 ? 21.43000  14.04200  21.96400  1.000 50.02390  ?  253 ALA B O   1 
ATOM   3809 C CB  . ALA B 1 245 ? 22.39700  15.97900  24.47200  1.000 44.37931  ?  253 ALA B CB  1 
ATOM   3810 N N   . ALA B 1 246 ? 23.40900  13.45400  22.86200  1.000 45.25571  ?  254 ALA B N   1 
ATOM   3811 C CA  . ALA B 1 246 ? 23.88400  12.83800  21.63000  1.000 43.52130  ?  254 ALA B CA  1 
ATOM   3812 C C   . ALA B 1 246 ? 23.04900  11.62100  21.26100  1.000 46.12844  ?  254 ALA B C   1 
ATOM   3813 O O   . ALA B 1 246 ? 22.80000  11.37400  20.08100  1.000 41.50714  ?  254 ALA B O   1 
ATOM   3814 C CB  . ALA B 1 246 ? 25.35600  12.45700  21.76800  1.000 32.04503  ?  254 ALA B CB  1 
ATOM   3815 N N   . LEU B 1 247 ? 22.62200  10.84100  22.25500  1.000 43.23304  ?  255 LEU B N   1 
ATOM   3816 C CA  . LEU B 1 247 ? 21.76000  9.69500   21.98000  1.000 42.54472  ?  255 LEU B CA  1 
ATOM   3817 C C   . LEU B 1 247 ? 20.43300  10.14400  21.38200  1.000 50.24821  ?  255 LEU B C   1 
ATOM   3818 O O   . LEU B 1 247 ? 19.94400  9.56100   20.40300  1.000 54.30051  ?  255 LEU B O   1 
ATOM   3819 C CB  . LEU B 1 247 ? 21.53200  8.90000   23.26500  1.000 39.53613  ?  255 LEU B CB  1 
ATOM   3820 C CG  . LEU B 1 247 ? 20.71900  7.61100   23.15500  1.000 37.80266  ?  255 LEU B CG  1 
ATOM   3821 C CD1 . LEU B 1 247 ? 21.45300  6.59100   22.31300  1.000 42.33784  ?  255 LEU B CD1 1 
ATOM   3822 C CD2 . LEU B 1 247 ? 20.40600  7.05000   24.52800  1.000 42.01550  ?  255 LEU B CD2 1 
ATOM   3823 N N   . LYS B 1 248 ? 19.83500  11.19000  21.95900  1.000 50.39994  ?  256 LYS B N   1 
ATOM   3824 C CA  . LYS B 1 248 ? 18.58000  11.70700  21.42000  1.000 52.56654  ?  256 LYS B CA  1 
ATOM   3825 C C   . LYS B 1 248 ? 18.76300  12.24100  20.00300  1.000 51.27702  ?  256 LYS B C   1 
ATOM   3826 O O   . LYS B 1 248 ? 17.93600  11.97700  19.11900  1.000 44.79480  ?  256 LYS B O   1 
ATOM   3827 C CB  . LYS B 1 248 ? 18.02100  12.79600  22.33600  1.000 54.29361  ?  256 LYS B CB  1 
ATOM   3828 C CG  . LYS B 1 248 ? 17.31500  12.27000  23.57500  1.000 56.09015  ?  256 LYS B CG  1 
ATOM   3829 C CD  . LYS B 1 248 ? 17.25800  13.32700  24.66800  1.000 61.94741  ?  256 LYS B CD  1 
ATOM   3830 C CE  . LYS B 1 248 ? 17.21500  12.69800  26.05100  1.000 62.15271  ?  256 LYS B CE  1 
ATOM   3831 N NZ  . LYS B 1 248 ? 17.09000  13.72300  27.12200  1.000 52.23734  ?  256 LYS B NZ  1 
ATOM   3832 N N   . THR B 1 249 ? 19.84500  12.98600  19.76600  1.000 47.83683  ?  257 THR B N   1 
ATOM   3833 C CA  . THR B 1 249 ? 20.10000  13.51000  18.42800  1.000 51.74753  ?  257 THR B CA  1 
ATOM   3834 C C   . THR B 1 249 ? 20.35900  12.38300  17.43600  1.000 50.04373  ?  257 THR B C   1 
ATOM   3835 O O   . THR B 1 249 ? 19.95900  12.46800  16.27400  1.000 54.60188  ?  257 THR B O   1 
ATOM   3836 C CB  . THR B 1 249 ? 21.27100  14.49500  18.44300  1.000 49.89473  ?  257 THR B CB  1 
ATOM   3837 O OG1 . THR B 1 249 ? 21.27000  15.23500  19.66600  1.000 47.76025  ?  257 THR B OG1 1 
ATOM   3838 C CG2 . THR B 1 249 ? 21.16300  15.46400  17.28100  1.000 58.26229  ?  257 THR B CG2 1 
ATOM   3839 N N   . ALA B 1 250 ? 21.02900  11.31700  17.87600  1.000 53.83711  ?  258 ALA B N   1 
ATOM   3840 C CA  . ALA B 1 250 ? 21.28600  10.18900  16.98900  1.000 51.28809  ?  258 ALA B CA  1 
ATOM   3841 C C   . ALA B 1 250 ? 19.99500  9.47600   16.61200  1.000 45.77526  ?  258 ALA B C   1 
ATOM   3842 O O   . ALA B 1 250 ? 19.80300  9.10100   15.45000  1.000 50.46488  ?  258 ALA B O   1 
ATOM   3843 C CB  . ALA B 1 250 ? 22.26400  9.21700   17.64500  1.000 43.24804  ?  258 ALA B CB  1 
ATOM   3844 N N   . ALA B 1 251 ? 19.09500  9.28300   17.57700  1.000 41.27990  ?  259 ALA B N   1 
ATOM   3845 C CA  . ALA B 1 251 ? 17.80600  8.67200   17.26200  1.000 49.69653  ?  259 ALA B CA  1 
ATOM   3846 C C   . ALA B 1 251 ? 17.00700  9.54500   16.29900  1.000 57.05047  ?  259 ALA B C   1 
ATOM   3847 O O   . ALA B 1 251 ? 16.43800  9.05500   15.31000  1.000 61.20252  ?  259 ALA B O   1 
ATOM   3848 C CB  . ALA B 1 251 ? 17.01900  8.42100   18.54600  1.000 37.83134  ?  259 ALA B CB  1 
ATOM   3849 N N   . ALA B 1 252 ? 16.96900  10.85300  16.56600  1.000 51.16503  ?  260 ALA B N   1 
ATOM   3850 C CA  . ALA B 1 252 ? 16.24200  11.76300  15.68800  1.000 56.72517  ?  260 ALA B CA  1 
ATOM   3851 C C   . ALA B 1 252 ? 16.84700  11.78200  14.29100  1.000 55.25845  ?  260 ALA B C   1 
ATOM   3852 O O   . ALA B 1 252 ? 16.12000  11.83900  13.29300  1.000 61.46032  ?  260 ALA B O   1 
ATOM   3853 C CB  . ALA B 1 252 ? 16.22700  13.16800  16.28800  1.000 53.20749  ?  260 ALA B CB  1 
ATOM   3854 N N   . ALA B 1 253 ? 18.17700  11.74500  14.20100  1.000 49.24233  ?  261 ALA B N   1 
ATOM   3855 C CA  . ALA B 1 253 ? 18.84000  11.74300  12.90400  1.000 56.25047  ?  261 ALA B CA  1 
ATOM   3856 C C   . ALA B 1 253 ? 18.56600  10.45300  12.15000  1.000 55.47363  ?  261 ALA B C   1 
ATOM   3857 O O   . ALA B 1 253 ? 18.38800  10.46800  10.92900  1.000 54.33438  ?  261 ALA B O   1 
ATOM   3858 C CB  . ALA B 1 253 ? 20.34200  11.95600  13.08300  1.000 40.40525  ?  261 ALA B CB  1 
ATOM   3859 N N   . LEU B 1 254 ? 18.53700  9.32200   12.85600  1.000 50.19530  ?  262 LEU B N   1 
ATOM   3860 C CA  . LEU B 1 254 ? 18.16700  8.06700   12.21400  1.000 52.45537  ?  262 LEU B CA  1 
ATOM   3861 C C   . LEU B 1 254 ? 16.77400  8.16800   11.61200  1.000 58.45553  ?  262 LEU B C   1 
ATOM   3862 O O   . LEU B 1 254 ? 16.55500  7.79500   10.45300  1.000 53.79397  ?  262 LEU B O   1 
ATOM   3863 C CB  . LEU B 1 254 ? 18.23800  6.92100   13.22300  1.000 42.27052  ?  262 LEU B CB  1 
ATOM   3864 C CG  . LEU B 1 254 ? 17.71800  5.56600   12.74600  1.000 44.53681  ?  262 LEU B CG  1 
ATOM   3865 C CD1 . LEU B 1 254 ? 18.54400  5.05300   11.58500  1.000 48.45221  ?  262 LEU B CD1 1 
ATOM   3866 C CD2 . LEU B 1 254 ? 17.71300  4.56700   13.88500  1.000 45.72402  ?  262 LEU B CD2 1 
ATOM   3867 N N   . GLU B 1 255 ? 15.82500  8.70600   12.38200  1.000 61.84455  ?  263 GLU B N   1 
ATOM   3868 C CA  . GLU B 1 255 ? 14.46900  8.88600   11.86700  1.000 65.64275  ?  263 GLU B CA  1 
ATOM   3869 C C   . GLU B 1 255 ? 14.45800  9.78300   10.63200  1.000 65.85597  ?  263 GLU B C   1 
ATOM   3870 O O   . GLU B 1 255 ? 13.87700  9.43400   9.59500   1.000 62.62431  ?  263 GLU B O   1 
ATOM   3871 C CB  . GLU B 1 255 ? 13.57000  9.47600   12.95400  1.000 65.28775  ?  263 GLU B CB  1 
ATOM   3872 C CG  . GLU B 1 255 ? 13.07200  8.47600   13.97300  1.000 57.78266  ?  263 GLU B CG  1 
ATOM   3873 C CD  . GLU B 1 255 ? 12.73000  7.14000   13.36000  1.000 63.71575  ?  263 GLU B CD  1 
ATOM   3874 O OE1 . GLU B 1 255 ? 11.93300  7.10100   12.39900  1.000 73.39380  ?  263 GLU B OE1 1 
ATOM   3875 O OE2 . GLU B 1 255 ? 13.26200  6.12500   13.84300  1.000 69.47617  -1 263 GLU B OE2 1 
ATOM   3876 N N   . GLU B 1 256 ? 15.10300  10.94600  10.73200  1.000 59.77749  ?  264 GLU B N   1 
ATOM   3877 C CA  . GLU B 1 256 ? 15.06400  11.92400  9.65100   1.000 62.38774  ?  264 GLU B CA  1 
ATOM   3878 C C   . GLU B 1 256 ? 15.70600  11.37500  8.38600   1.000 67.47852  ?  264 GLU B C   1 
ATOM   3879 O O   . GLU B 1 256 ? 15.17900  11.55300  7.28300   1.000 75.72330  ?  264 GLU B O   1 
ATOM   3880 C CB  . GLU B 1 256 ? 15.75800  13.21300  10.09100  1.000 62.82000  ?  264 GLU B CB  1 
ATOM   3881 C CG  . GLU B 1 256 ? 15.77300  14.30500  9.03500   1.000 67.10626  ?  264 GLU B CG  1 
ATOM   3882 C CD  . GLU B 1 256 ? 17.13900  14.94000  8.87600   1.000 74.23112  ?  264 GLU B CD  1 
ATOM   3883 O OE1 . GLU B 1 256 ? 17.79000  15.22000  9.90300   1.000 81.51590  ?  264 GLU B OE1 1 
ATOM   3884 O OE2 . GLU B 1 256 ? 17.56300  15.16200  7.72300   1.000 72.15724  -1 264 GLU B OE2 1 
ATOM   3885 N N   . TYR B 1 257 ? 16.84400  10.69300  8.52400   1.000 64.24529  ?  265 TYR B N   1 
ATOM   3886 C CA  . TYR B 1 257 ? 17.54900  10.20700  7.34600   1.000 61.60291  ?  265 TYR B CA  1 
ATOM   3887 C C   . TYR B 1 257 ? 16.84600  9.00500   6.73300   1.000 62.23738  ?  265 TYR B C   1 
ATOM   3888 O O   . TYR B 1 257 ? 16.83800  8.85000   5.50800   1.000 62.49275  ?  265 TYR B O   1 
ATOM   3889 C CB  . TYR B 1 257 ? 19.00100  9.88500   7.69600   1.000 56.58786  ?  265 TYR B CB  1 
ATOM   3890 C CG  . TYR B 1 257 ? 19.86100  11.12500  7.80100   1.000 57.84988  ?  265 TYR B CG  1 
ATOM   3891 C CD1 . TYR B 1 257 ? 20.02900  11.96500  6.71100   1.000 56.08887  ?  265 TYR B CD1 1 
ATOM   3892 C CD2 . TYR B 1 257 ? 20.48800  11.46400  8.99000   1.000 57.07821  ?  265 TYR B CD2 1 
ATOM   3893 C CE1 . TYR B 1 257 ? 20.80400  13.10300  6.79900   1.000 54.09979  ?  265 TYR B CE1 1 
ATOM   3894 C CE2 . TYR B 1 257 ? 21.26300  12.60100  9.08700   1.000 60.54716  ?  265 TYR B CE2 1 
ATOM   3895 C CZ  . TYR B 1 257 ? 21.41800  13.41600  7.98800   1.000 57.63349  ?  265 TYR B CZ  1 
ATOM   3896 O OH  . TYR B 1 257 ? 22.19100  14.54900  8.07700   1.000 57.57141  ?  265 TYR B OH  1 
ATOM   3897 N N   . GLN B 1 258 ? 16.22900  8.15000   7.55500   1.000 60.04606  ?  266 GLN B N   1 
ATOM   3898 C CA  . GLN B 1 258 ? 15.42000  7.08000   6.98300   1.000 59.97298  ?  266 GLN B CA  1 
ATOM   3899 C C   . GLN B 1 258 ? 14.24100  7.64400   6.20100   1.000 63.20037  ?  266 GLN B C   1 
ATOM   3900 O O   . GLN B 1 258 ? 13.93400  7.16700   5.10100   1.000 60.53127  ?  266 GLN B O   1 
ATOM   3901 C CB  . GLN B 1 258 ? 14.93900  6.12800   8.07600   1.000 54.54476  ?  266 GLN B CB  1 
ATOM   3902 C CG  . GLN B 1 258 ? 15.96100  5.08100   8.47000   1.000 45.72275  ?  266 GLN B CG  1 
ATOM   3903 C CD  . GLN B 1 258 ? 15.36600  3.97700   9.31500   1.000 47.61337  ?  266 GLN B CD  1 
ATOM   3904 O OE1 . GLN B 1 258 ? 14.41100  4.19600   10.05700  1.000 56.63780  ?  266 GLN B OE1 1 
ATOM   3905 N NE2 . GLN B 1 258 ? 15.92800  2.78200   9.20700   1.000 44.82916  ?  266 GLN B NE2 1 
ATOM   3906 N N   . GLY B 1 259 ? 13.57700  8.66800   6.74100   1.000 66.34385  ?  267 GLY B N   1 
ATOM   3907 C CA  . GLY B 1 259 ? 12.49400  9.29800   5.99900   1.000 69.10160  ?  267 GLY B CA  1 
ATOM   3908 C C   . GLY B 1 259 ? 12.97200  9.93900   4.70900   1.000 69.23651  ?  267 GLY B C   1 
ATOM   3909 O O   . GLY B 1 259 ? 12.33100  9.81500   3.66000   1.000 71.42552  ?  267 GLY B O   1 
ATOM   3910 N N   . VAL B 1 260 ? 14.11300  10.62700  4.77000   1.000 69.73364  ?  268 VAL B N   1 
ATOM   3911 C CA  . VAL B 1 260 ? 14.66500  11.27800  3.58500   1.000 70.30177  ?  268 VAL B CA  1 
ATOM   3912 C C   . VAL B 1 260 ? 14.98500  10.24500  2.51300   1.000 70.66063  ?  268 VAL B C   1 
ATOM   3913 O O   . VAL B 1 260 ? 14.66500  10.42900  1.33400   1.000 70.35757  ?  268 VAL B O   1 
ATOM   3914 C CB  . VAL B 1 260 ? 15.90600  12.10700  3.96100   1.000 64.68944  ?  268 VAL B CB  1 
ATOM   3915 C CG1 . VAL B 1 260 ? 16.80200  12.31400  2.75100   1.000 46.85143  ?  268 VAL B CG1 1 
ATOM   3916 C CG2 . VAL B 1 260 ? 15.49200  13.44000  4.55700   1.000 67.08220  ?  268 VAL B CG2 1 
ATOM   3917 N N   . THR B 1 261 ? 15.61500  9.13700   2.90800   1.000 69.69721  ?  269 THR B N   1 
ATOM   3918 C CA  . THR B 1 261 ? 15.99000  8.12000   1.93400   1.000 65.73433  ?  269 THR B CA  1 
ATOM   3919 C C   . THR B 1 261 ? 14.76600  7.42100   1.36000   1.000 68.08273  ?  269 THR B C   1 
ATOM   3920 O O   . THR B 1 261 ? 14.74100  7.08800   0.17100   1.000 76.68331  ?  269 THR B O   1 
ATOM   3921 C CB  . THR B 1 261 ? 16.94400  7.10400   2.55900   1.000 63.81175  ?  269 THR B CB  1 
ATOM   3922 O OG1 . THR B 1 261 ? 16.37400  6.58000   3.76300   1.000 65.44456  ?  269 THR B OG1 1 
ATOM   3923 C CG2 . THR B 1 261 ? 18.27900  7.75500   2.86400   1.000 57.49103  ?  269 THR B CG2 1 
ATOM   3924 N N   . THR B 1 262 ? 13.73700  7.18800   2.17900   1.000 67.22437  ?  270 THR B N   1 
ATOM   3925 C CA  . THR B 1 262 ? 12.54300  6.53500   1.65200   1.000 72.15810  ?  270 THR B CA  1 
ATOM   3926 C C   . THR B 1 262 ? 11.80400  7.45500   0.68300   1.000 71.33644  ?  270 THR B C   1 
ATOM   3927 O O   . THR B 1 262 ? 11.29800  7.00500   -0.35300  1.000 72.29418  ?  270 THR B O   1 
ATOM   3928 C CB  . THR B 1 262 ? 11.64100  6.05400   2.79900   1.000 68.81956  ?  270 THR B CB  1 
ATOM   3929 O OG1 . THR B 1 262 ? 10.87400  4.92500   2.36100   1.000 64.95872  ?  270 THR B OG1 1 
ATOM   3930 C CG2 . THR B 1 262 ? 10.69200  7.13700   3.28600   1.000 67.37740  ?  270 THR B CG2 1 
ATOM   3931 N N   . ARG B 1 263 ? 11.78500  8.76100   0.96700   1.000 68.18958  ?  271 ARG B N   1 
ATOM   3932 C CA  . ARG B 1 263 ? 11.16900  9.69800   0.03200   1.000 71.05602  ?  271 ARG B CA  1 
ATOM   3933 C C   . ARG B 1 263 ? 11.98500  9.81200   -1.25000  1.000 74.82097  ?  271 ARG B C   1 
ATOM   3934 O O   . ARG B 1 263 ? 11.42400  9.91700   -2.34700  1.000 80.58841  ?  271 ARG B O   1 
ATOM   3935 C CB  . ARG B 1 263 ? 10.99500  11.06600  0.69300   1.000 70.23687  ?  271 ARG B CB  1 
ATOM   3936 C CG  . ARG B 1 263 ? 9.62300   11.26700  1.32500   1.000 72.28136  ?  271 ARG B CG  1 
ATOM   3937 C CD  . ARG B 1 263 ? 9.47100   12.63800  1.96600   1.000 67.73207  ?  271 ARG B CD  1 
ATOM   3938 N NE  . ARG B 1 263 ? 10.34200  12.82100  3.12000   1.000 79.04202  ?  271 ARG B NE  1 
ATOM   3939 C CZ  . ARG B 1 263 ? 11.44300  13.56100  3.12100   1.000 75.70404  ?  271 ARG B CZ  1 
ATOM   3940 N NH1 . ARG B 1 263 ? 11.84600  14.20100  2.03700   1.000 66.56463  ?  271 ARG B NH1 1 
ATOM   3941 N NH2 . ARG B 1 263 ? 12.15400  13.66300  4.24000   1.000 71.66733  ?  271 ARG B NH2 1 
ATOM   3942 N N   . GLN B 1 264 ? 13.31300  9.78000   -1.13200  1.000 66.40019  ?  272 GLN B N   1 
ATOM   3943 C CA  . GLN B 1 264 ? 14.17100  9.82400   -2.31100  1.000 67.76638  ?  272 GLN B CA  1 
ATOM   3944 C C   . GLN B 1 264 ? 13.97200  8.58800   -3.17900  1.000 67.58645  ?  272 GLN B C   1 
ATOM   3945 O O   . GLN B 1 264 ? 13.92900  8.67700   -4.41100  1.000 74.40022  ?  272 GLN B O   1 
ATOM   3946 C CB  . GLN B 1 264 ? 15.63000  9.95700   -1.87400  1.000 74.97678  ?  272 GLN B CB  1 
ATOM   3947 C CG  . GLN B 1 264 ? 16.64300  9.92100   -3.00000  1.000 71.67942  ?  272 GLN B CG  1 
ATOM   3948 C CD  . GLN B 1 264 ? 18.04000  10.26400  -2.52300  1.000 64.52459  ?  272 GLN B CD  1 
ATOM   3949 O OE1 . GLN B 1 264 ? 18.87300  10.73900  -3.29400  1.000 68.62436  ?  272 GLN B OE1 1 
ATOM   3950 N NE2 . GLN B 1 264 ? 18.30200  10.02900  -1.24300  1.000 49.15997  ?  272 GLN B NE2 1 
ATOM   3951 N N   . LEU B 1 265 ? 13.85400  7.41900   -2.54800  1.000 72.05008  ?  273 LEU B N   1 
ATOM   3952 C CA  . LEU B 1 265 ? 13.62100  6.19000   -3.29700  1.000 71.05325  ?  273 LEU B CA  1 
ATOM   3953 C C   . LEU B 1 265 ? 12.25400  6.22000   -3.97100  1.000 79.08556  ?  273 LEU B C   1 
ATOM   3954 O O   . LEU B 1 265 ? 12.10700  5.77700   -5.11700  1.000 79.24359  ?  273 LEU B O   1 
ATOM   3955 C CB  . LEU B 1 265 ? 13.74900  4.98600   -2.36200  1.000 66.97444  ?  273 LEU B CB  1 
ATOM   3956 C CG  . LEU B 1 265 ? 13.59400  3.55500   -2.88300  1.000 71.88280  ?  273 LEU B CG  1 
ATOM   3957 C CD1 . LEU B 1 265 ? 14.06300  3.41400   -4.32200  1.000 68.05297  ?  273 LEU B CD1 1 
ATOM   3958 C CD2 . LEU B 1 265 ? 14.33900  2.58800   -1.97900  1.000 65.04670  ?  273 LEU B CD2 1 
ATOM   3959 N N   . SER B 1 266 ? 11.24200  6.74900   -3.27900  1.000 81.67366  ?  274 SER B N   1 
ATOM   3960 C CA  . SER B 1 266 ? 9.93300   6.90800   -3.90400  1.000 83.59265  ?  274 SER B CA  1 
ATOM   3961 C C   . SER B 1 266 ? 10.01400  7.82600   -5.11700  1.000 83.20046  ?  274 SER B C   1 
ATOM   3962 O O   . SER B 1 266 ? 9.41900   7.54100   -6.16300  1.000 80.64982  ?  274 SER B O   1 
ATOM   3963 C CB  . SER B 1 266 ? 8.92600   7.44800   -2.88900  1.000 79.90733  ?  274 SER B CB  1 
ATOM   3964 O OG  . SER B 1 266 ? 8.71000   6.52200   -1.84000  1.000 80.78991  ?  274 SER B OG  1 
ATOM   3965 N N   . GLU B 1 267 ? 10.75100  8.93200   -4.99700  1.000 86.43346  ?  275 GLU B N   1 
ATOM   3966 C CA  . GLU B 1 267 ? 10.90900  9.84100   -6.12700  1.000 85.59585  ?  275 GLU B CA  1 
ATOM   3967 C C   . GLU B 1 267 ? 11.61500  9.16000   -7.29200  1.000 82.79141  ?  275 GLU B C   1 
ATOM   3968 O O   . GLU B 1 267 ? 11.22700  9.33800   -8.45300  1.000 92.03237  ?  275 GLU B O   1 
ATOM   3969 C CB  . GLU B 1 267 ? 11.68000  11.08800  -5.69900  1.000 85.92686  ?  275 GLU B CB  1 
ATOM   3970 C CG  . GLU B 1 267 ? 10.84900  12.11700  -4.95800  1.000 91.09912  ?  275 GLU B CG  1 
ATOM   3971 C CD  . GLU B 1 267 ? 11.63500  13.37200  -4.64400  1.000 106.38796 ?  275 GLU B CD  1 
ATOM   3972 O OE1 . GLU B 1 267 ? 12.84200  13.25800  -4.34300  1.000 99.54780  ?  275 GLU B OE1 1 
ATOM   3973 O OE2 . GLU B 1 267 ? 11.04800  14.47300  -4.70200  1.000 112.76269 -1 275 GLU B OE2 1 
ATOM   3974 N N   . VAL B 1 268 ? 12.65900  8.37900   -7.00600  1.000 78.28703  ?  276 VAL B N   1 
ATOM   3975 C CA  . VAL B 1 268 ? 13.41000  7.74200   -8.08000  1.000 80.63122  ?  276 VAL B CA  1 
ATOM   3976 C C   . VAL B 1 268 ? 12.62200  6.60800   -8.72200  1.000 79.49660  ?  276 VAL B C   1 
ATOM   3977 O O   . VAL B 1 268 ? 12.86000  6.28100   -9.89000  1.000 84.40495  ?  276 VAL B O   1 
ATOM   3978 C CB  . VAL B 1 268 ? 14.78200  7.25200   -7.57600  1.000 77.25940  ?  276 VAL B CB  1 
ATOM   3979 C CG1 . VAL B 1 268 ? 14.68500  5.85800   -6.98500  1.000 76.31067  ?  276 VAL B CG1 1 
ATOM   3980 C CG2 . VAL B 1 268 ? 15.80100  7.28700   -8.70200  1.000 73.05366  ?  276 VAL B CG2 1 
ATOM   3981 N N   . LEU B 1 269 ? 11.68300  5.99700   -7.99700  1.000 80.09704  ?  277 LEU B N   1 
ATOM   3982 C CA  . LEU B 1 269 ? 10.82800  4.97700   -8.59100  1.000 78.91159  ?  277 LEU B CA  1 
ATOM   3983 C C   . LEU B 1 269 ? 9.64400   5.56000   -9.34700  1.000 81.87165  ?  277 LEU B C   1 
ATOM   3984 O O   . LEU B 1 269 ? 8.98500   4.83000   -10.09600 1.000 76.92126  ?  277 LEU B O   1 
ATOM   3985 C CB  . LEU B 1 269 ? 10.30800  4.01600   -7.51800  1.000 75.34103  ?  277 LEU B CB  1 
ATOM   3986 C CG  . LEU B 1 269 ? 11.33300  3.11800   -6.82700  1.000 72.26342  ?  277 LEU B CG  1 
ATOM   3987 C CD1 . LEU B 1 269 ? 10.63000  2.10800   -5.93700  1.000 68.45367  ?  277 LEU B CD1 1 
ATOM   3988 C CD2 . LEU B 1 269 ? 12.20800  2.42000   -7.85000  1.000 64.94020  ?  277 LEU B CD2 1 
ATOM   3989 N N   . ARG B 1 270 ? 9.36000   6.84700   -9.17500  1.000 79.19838  ?  278 ARG B N   1 
ATOM   3990 C CA  . ARG B 1 270 ? 8.24400   7.48200   -9.86300  1.000 72.69366  ?  278 ARG B CA  1 
ATOM   3991 C C   . ARG B 1 270 ? 8.64900   7.92400   -11.26400 1.000 75.02743  ?  278 ARG B C   1 
ATOM   3992 O O   . ARG B 1 270 ? 9.70100   7.53300   -11.76900 1.000 69.25217  ?  278 ARG B O   1 
ATOM   3993 C CB  . ARG B 1 270 ? 7.73000   8.67800   -9.05900  1.000 64.00041  ?  278 ARG B CB  1 
HETATM 3994 N N1  . SPD C 2 .   ? 53.26100  0.01500   32.80300  1.000 54.56277  ?  301 SPD A N1  1 
HETATM 3995 C C2  . SPD C 2 .   ? 53.02500  -0.33800  34.20400  1.000 41.85231  ?  301 SPD A C2  1 
HETATM 3996 C C3  . SPD C 2 .   ? 54.16500  -1.07600  34.88500  1.000 43.62610  ?  301 SPD A C3  1 
HETATM 3997 C C4  . SPD C 2 .   ? 54.17000  -0.87700  36.38500  1.000 39.19213  ?  301 SPD A C4  1 
HETATM 3998 C C5  . SPD C 2 .   ? 55.32600  -1.57700  37.07900  1.000 32.71053  ?  301 SPD A C5  1 
HETATM 3999 N N6  . SPD C 2 .   ? 54.86900  -2.31000  38.25800  1.000 42.47853  ?  301 SPD A N6  1 
HETATM 4000 C C7  . SPD C 2 .   ? 55.93700  -2.82400  39.11200  1.000 28.17358  ?  301 SPD A C7  1 
HETATM 4001 C C8  . SPD C 2 .   ? 55.52900  -4.11300  39.78300  1.000 37.80861  ?  301 SPD A C8  1 
HETATM 4002 C C9  . SPD C 2 .   ? 56.60400  -5.16100  39.80500  1.000 39.28313  ?  301 SPD A C9  1 
HETATM 4003 N N10 . SPD C 2 .   ? 56.18600  -6.37100  40.52300  1.000 45.90722  ?  301 SPD A N10 1 
HETATM 4004 N N1  . SPD D 2 .   ? 39.09100  -0.66600  55.17300  1.000 34.56950  ?  302 SPD A N1  1 
HETATM 4005 C C2  . SPD D 2 .   ? 40.21800  -1.60800  55.17500  1.000 48.03790  ?  302 SPD A C2  1 
HETATM 4006 C C3  . SPD D 2 .   ? 41.30200  -1.32900  54.14600  1.000 48.08525  ?  302 SPD A C3  1 
HETATM 4007 C C4  . SPD D 2 .   ? 42.68700  -1.74600  54.60700  1.000 52.27097  ?  302 SPD A C4  1 
HETATM 4008 C C5  . SPD D 2 .   ? 43.74000  -1.55200  53.52900  1.000 40.12234  ?  302 SPD A C5  1 
HETATM 4009 N N6  . SPD D 2 .   ? 44.84000  -0.69100  53.96700  1.000 52.95603  ?  302 SPD A N6  1 
HETATM 4010 C C7  . SPD D 2 .   ? 45.36700  0.13200   52.88100  1.000 37.07195  ?  302 SPD A C7  1 
HETATM 4011 C C8  . SPD D 2 .   ? 46.24600  1.24700   53.36400  1.000 36.66112  ?  302 SPD A C8  1 
HETATM 4012 C C9  . SPD D 2 .   ? 46.62300  2.18500   52.25900  1.000 34.49544  ?  302 SPD A C9  1 
HETATM 4013 N N10 . SPD D 2 .   ? 46.34900  3.58500   52.59400  1.000 28.42846  ?  302 SPD A N10 1 
HETATM 4014 N N1  . SPD E 2 .   ? 38.63300  4.23000   12.16700  1.000 32.39969  ?  301 SPD B N1  1 
HETATM 4015 C C2  . SPD E 2 .   ? 37.62900  4.56000   13.18300  1.000 54.15834  ?  301 SPD B C2  1 
HETATM 4016 C C3  . SPD E 2 .   ? 36.23400  4.82700   12.63800  1.000 55.42609  ?  301 SPD B C3  1 
HETATM 4017 C C4  . SPD E 2 .   ? 35.16700  4.91300   13.71300  1.000 42.21507  ?  301 SPD B C4  1 
HETATM 4018 C C5  . SPD E 2 .   ? 33.76200  4.88500   13.13400  1.000 49.35567  ?  301 SPD B C5  1 
HETATM 4019 N N6  . SPD E 2 .   ? 32.88700  5.86800   13.76900  1.000 47.67081  ?  301 SPD B N6  1 
HETATM 4020 C C7  . SPD E 2 .   ? 31.64200  6.10100   13.04000  1.000 43.39965  ?  301 SPD B C7  1 
HETATM 4021 C C8  . SPD E 2 .   ? 31.74700  7.31200   12.16000  1.000 43.45654  ?  301 SPD B C8  1 
HETATM 4022 C C9  . SPD E 2 .   ? 30.51300  8.15600   12.16700  1.000 46.84917  ?  301 SPD B C9  1 
HETATM 4023 N N10 . SPD E 2 .   ? 30.65400  9.33600   11.30900  1.000 34.08166  ?  301 SPD B N10 1 
HETATM 4024 O O   . HOH F 3 .   ? 37.44800  -11.83400 36.33700  1.000 26.93728  ?  401 HOH A O   1 
HETATM 4025 O O   . HOH F 3 .   ? 54.13300  7.80100   39.18400  1.000 29.31318  ?  402 HOH A O   1 
HETATM 4026 O O   . HOH F 3 .   ? 55.00700  0.86100   56.56300  1.000 31.90285  ?  403 HOH A O   1 
HETATM 4027 O O   . HOH F 3 .   ? 67.98900  -13.09800 39.63600  1.000 49.95237  ?  404 HOH A O   1 
HETATM 4028 O O   . HOH F 3 .   ? 54.91300  6.74600   35.92400  1.000 37.70302  ?  405 HOH A O   1 
HETATM 4029 O O   . HOH F 3 .   ? 69.73100  -9.13600  46.48500  1.000 41.43172  ?  406 HOH A O   1 
HETATM 4030 O O   . HOH F 3 .   ? 39.12100  1.77600   29.93600  1.000 18.34263  ?  407 HOH A O   1 
HETATM 4031 O O   . HOH F 3 .   ? 60.22000  10.55700  33.56500  1.000 33.08574  ?  408 HOH A O   1 
HETATM 4032 O O   . HOH F 3 .   ? 55.37300  5.15900   42.13000  1.000 23.60251  ?  409 HOH A O   1 
HETATM 4033 O O   . HOH F 3 .   ? 60.52800  3.15500   39.67800  1.000 33.85206  ?  410 HOH A O   1 
HETATM 4034 O O   . HOH F 3 .   ? 50.32500  11.28600  40.86300  1.000 22.80971  ?  411 HOH A O   1 
HETATM 4035 O O   . HOH F 3 .   ? 46.67900  -12.81000 39.20600  1.000 26.19842  ?  412 HOH A O   1 
HETATM 4036 O O   . HOH F 3 .   ? 50.02600  3.35300   28.59700  1.000 32.89733  ?  413 HOH A O   1 
HETATM 4037 O O   . HOH F 3 .   ? 42.58300  12.89700  43.28900  1.000 27.36736  ?  414 HOH A O   1 
HETATM 4038 O O   . HOH F 3 .   ? 38.586    -13.566   39.706    1.000 30.89511  ?  415 HOH A O   1 
HETATM 4039 O O   . HOH F 3 .   ? 63.01600  16.76100  39.40300  1.000 44.76805  ?  416 HOH A O   1 
HETATM 4040 O O   . HOH F 3 .   ? 41.65900  -0.73400  22.85200  1.000 34.60250  ?  417 HOH A O   1 
HETATM 4041 O O   . HOH F 3 .   ? 56.65900  0.45500   24.88100  1.000 41.83016  ?  418 HOH A O   1 
HETATM 4042 O O   . HOH F 3 .   ? 42.74800  7.06800   61.10000  1.000 28.09385  ?  419 HOH A O   1 
HETATM 4043 O O   . HOH F 3 .   ? 58.74700  -2.15700  37.21500  1.000 35.03084  ?  420 HOH A O   1 
HETATM 4044 O O   . HOH F 3 .   ? 41.59500  5.84100   33.59400  1.000 18.14211  ?  421 HOH A O   1 
HETATM 4045 O O   . HOH F 3 .   ? 78.13700  6.55000   46.11900  1.000 40.51616  ?  422 HOH A O   1 
HETATM 4046 O O   . HOH F 3 .   ? 61.02400  15.71100  43.40300  1.000 30.35263  ?  423 HOH A O   1 
HETATM 4047 O O   . HOH F 3 .   ? 57.90100  3.27800   41.96500  1.000 28.73554  ?  424 HOH A O   1 
HETATM 4048 O O   . HOH F 3 .   ? 57.66300  -4.43700  43.15400  1.000 29.06505  ?  425 HOH A O   1 
HETATM 4049 O O   . HOH F 3 .   ? 63.11700  -11.87300 44.06800  1.000 39.36941  ?  426 HOH A O   1 
HETATM 4050 O O   . HOH F 3 .   ? 61.83300  2.03800   25.15200  1.000 55.46179  ?  427 HOH A O   1 
HETATM 4051 O O   . HOH F 3 .   ? 72.61400  9.92900   52.87700  1.000 49.37225  ?  428 HOH A O   1 
HETATM 4052 O O   . HOH F 3 .   ? 53.74400  9.99100   32.74200  1.000 37.42137  ?  429 HOH A O   1 
HETATM 4053 O O   . HOH F 3 .   ? 68.23800  10.43000  51.72700  1.000 40.04214  ?  430 HOH A O   1 
HETATM 4054 O O   . HOH F 3 .   ? 51.25200  -9.92300  52.63900  1.000 27.34152  ?  431 HOH A O   1 
HETATM 4055 O O   . HOH F 3 .   ? 28.560    6.435     44.194    1.000 21.55596  ?  432 HOH A O   1 
HETATM 4056 O O   . HOH F 3 .   ? 42.21900  1.88000   26.91900  1.000 18.34915  ?  433 HOH A O   1 
HETATM 4057 O O   . HOH F 3 .   ? 81.44400  2.91900   72.44900  1.000 38.92639  ?  434 HOH A O   1 
HETATM 4058 O O   . HOH F 3 .   ? 60.60000  12.31800  51.33400  1.000 19.52035  ?  435 HOH A O   1 
HETATM 4059 O O   . HOH G 3 .   ? 47.40500  7.94500   32.93700  1.000 36.29685  ?  401 HOH B O   1 
HETATM 4060 O O   . HOH G 3 .   ? 37.70800  17.71700  0.25400   1.000 41.97684  ?  402 HOH B O   1 
HETATM 4061 O O   . HOH G 3 .   ? 11.22500  6.32500   -13.16900 1.000 57.22843  ?  403 HOH B O   1 
HETATM 4062 O O   . HOH G 3 .   ? 17.50300  -1.94100  -14.14600 1.000 63.57413  ?  404 HOH B O   1 
HETATM 4063 O O   . HOH G 3 .   ? 35.71400  12.94200  34.28900  1.000 25.53008  ?  405 HOH B O   1 
HETATM 4064 O O   . HOH G 3 .   ? 31.31400  8.53200   38.11900  1.000 25.14346  ?  406 HOH B O   1 
HETATM 4065 O O   . HOH G 3 .   ? 26.42100  -4.93400  38.37400  1.000 27.50911  ?  407 HOH B O   1 
HETATM 4066 O O   . HOH G 3 .   ? 24.19900  3.48200   23.31000  1.000 37.19762  ?  408 HOH B O   1 
HETATM 4067 O O   . HOH G 3 .   ? 24.70400  -7.85000  22.96600  1.000 38.26888  ?  409 HOH B O   1 
HETATM 4068 O O   . HOH G 3 .   ? 45.40900  17.71400  -9.11600  1.000 38.47409  ?  410 HOH B O   1 
HETATM 4069 O O   . HOH G 3 .   ? 20.57200  14.77900  35.25400  1.000 38.95570  ?  411 HOH B O   1 
HETATM 4070 O O   . HOH G 3 .   ? 25.11200  15.49800  4.16700   1.000 35.25265  ?  412 HOH B O   1 
# 
