data_8Z2J
# 
_entry.id   8Z2J 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z2J         pdb_00008z2j 10.2210/pdb8z2j/pdb 
WWPDB D_1300046891 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z2J 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 ito.str@tmd.ac.jp Nobutoshi Ito ? 'principal investigator/group leader' 0000-0003-0839-0384 
3 oda@kpu.ac.jp     Masayuki  Oda ? 'principal investigator/group leader' 0000-0002-8568-4223 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Numoto, N.'    1 ? 
'Kondo, F.'     2 ? 
'Bekker, G.J.'  3 ? 
'Liao, Z.'      4 ? 
'Yamashita, M.' 5 ? 
'Iida, A.'      6 ? 
'Ito, N.'       7 ? 
'Kamiya, N.'    8 ? 
'Oda, M.'       9 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            281 
_citation.language                  ? 
_citation.page_first                136597 
_citation.page_last                 136597 
_citation.title                     
'Structural dynamics of the Ca 2+ -regulated cutinase towards structure-based improvement of PET degradation activity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.136597 
_citation.pdbx_database_id_PubMed   39419144 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Numoto, N.'    1 ? 
primary 'Kondo, F.'     2 ? 
primary 'Bekker, G.J.'  3 ? 
primary 'Liao, Z.'      4 ? 
primary 'Yamashita, M.' 5 ? 
primary 'Iida, A.'      6 ? 
primary 'Ito, N.'       7 ? 
primary 'Kamiya, N.'    8 ? 
primary 'Oda, M.'       9 ? 
# 
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 'Alpha/beta hydrolase family protein'                              28533.098 2   3.1.1.74 ? ? ? 
2 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                    118.174   2   ?        ? ? ? 
3 non-polymer syn '(4-methoxycarbonylphenyl)-(2-phenylmethoxyethoxy)phosphinic acid' 350.303   2   ?        ? ? ? 
4 non-polymer syn 'CALCIUM ION'                                                      40.078    4   ?        ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                     35.453    3   ?        ? ? ? 
6 non-polymer syn 'ACETATE ION'                                                      59.044    2   ?        ? ? ? 
7 water       nat water                                                              18.015    609 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        cutinase 
# 
_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       
;GPNPYERGPDPTEDSIEAIRGPFSVATERVSSFASGFGGGTIYYPRETDEGTFGAVAVAPGFTASQGSMSWYGERVASHG
FIVFTIDTNTRLDAPGQRGRQLLAALDYLVERSDRKVRERLDPNRLAVMGHAMGGGGSLEATVMRPSLKASIPLTPWHLD
KTWGQVQVPTFIIGAELDTIAPVSTHAKPFYESLPSSLPKAYMELCGATHFAPNIPNTTIAKYVISWLKRFVDEDTRYSQ
FLCPNPTDRAICEYRSTCPY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPNPYERGPDPTEDSIEAIRGPFSVATERVSSFASGFGGGTIYYPRETDEGTFGAVAVAPGFTASQGSMSWYGERVASHG
FIVFTIDTNTRLDAPGQRGRQLLAALDYLVERSDRKVRERLDPNRLAVMGHAMGGGGSLEATVMRPSLKASIPLTPWHLD
KTWGQVQVPTFIIGAELDTIAPVSTHAKPFYESLPSSLPKAYMELCGATHFAPNIPNTTIAKYVISWLKRFVDEDTRYSQ
FLCPNPTDRAICEYRSTCPY
;
_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 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                    MPD   
3 '(4-methoxycarbonylphenyl)-(2-phenylmethoxyethoxy)phosphinic acid' A1L0M 
4 'CALCIUM ION'                                                      CA    
5 'CHLORIDE ION'                                                     CL    
6 'ACETATE ION'                                                      ACT   
7 water                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   ASN n 
1 4   PRO n 
1 5   TYR n 
1 6   GLU n 
1 7   ARG n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  PRO n 
1 12  THR n 
1 13  GLU n 
1 14  ASP n 
1 15  SER n 
1 16  ILE n 
1 17  GLU n 
1 18  ALA n 
1 19  ILE n 
1 20  ARG n 
1 21  GLY n 
1 22  PRO n 
1 23  PHE n 
1 24  SER n 
1 25  VAL n 
1 26  ALA n 
1 27  THR n 
1 28  GLU n 
1 29  ARG n 
1 30  VAL n 
1 31  SER n 
1 32  SER n 
1 33  PHE n 
1 34  ALA n 
1 35  SER n 
1 36  GLY n 
1 37  PHE n 
1 38  GLY n 
1 39  GLY n 
1 40  GLY n 
1 41  THR n 
1 42  ILE n 
1 43  TYR n 
1 44  TYR n 
1 45  PRO n 
1 46  ARG n 
1 47  GLU n 
1 48  THR n 
1 49  ASP n 
1 50  GLU n 
1 51  GLY n 
1 52  THR n 
1 53  PHE n 
1 54  GLY n 
1 55  ALA n 
1 56  VAL n 
1 57  ALA n 
1 58  VAL n 
1 59  ALA n 
1 60  PRO n 
1 61  GLY n 
1 62  PHE n 
1 63  THR n 
1 64  ALA n 
1 65  SER n 
1 66  GLN n 
1 67  GLY n 
1 68  SER n 
1 69  MET n 
1 70  SER n 
1 71  TRP n 
1 72  TYR n 
1 73  GLY n 
1 74  GLU n 
1 75  ARG n 
1 76  VAL n 
1 77  ALA n 
1 78  SER n 
1 79  HIS n 
1 80  GLY n 
1 81  PHE n 
1 82  ILE n 
1 83  VAL n 
1 84  PHE n 
1 85  THR n 
1 86  ILE n 
1 87  ASP n 
1 88  THR n 
1 89  ASN n 
1 90  THR n 
1 91  ARG n 
1 92  LEU n 
1 93  ASP n 
1 94  ALA n 
1 95  PRO n 
1 96  GLY n 
1 97  GLN n 
1 98  ARG n 
1 99  GLY n 
1 100 ARG n 
1 101 GLN n 
1 102 LEU n 
1 103 LEU n 
1 104 ALA n 
1 105 ALA n 
1 106 LEU n 
1 107 ASP n 
1 108 TYR n 
1 109 LEU n 
1 110 VAL n 
1 111 GLU n 
1 112 ARG n 
1 113 SER n 
1 114 ASP n 
1 115 ARG n 
1 116 LYS n 
1 117 VAL n 
1 118 ARG n 
1 119 GLU n 
1 120 ARG n 
1 121 LEU n 
1 122 ASP n 
1 123 PRO n 
1 124 ASN n 
1 125 ARG n 
1 126 LEU n 
1 127 ALA n 
1 128 VAL n 
1 129 MET n 
1 130 GLY n 
1 131 HIS n 
1 132 ALA n 
1 133 MET n 
1 134 GLY n 
1 135 GLY n 
1 136 GLY n 
1 137 GLY n 
1 138 SER n 
1 139 LEU n 
1 140 GLU n 
1 141 ALA n 
1 142 THR n 
1 143 VAL n 
1 144 MET n 
1 145 ARG n 
1 146 PRO n 
1 147 SER n 
1 148 LEU n 
1 149 LYS n 
1 150 ALA n 
1 151 SER n 
1 152 ILE n 
1 153 PRO n 
1 154 LEU n 
1 155 THR n 
1 156 PRO n 
1 157 TRP n 
1 158 HIS n 
1 159 LEU n 
1 160 ASP n 
1 161 LYS n 
1 162 THR n 
1 163 TRP n 
1 164 GLY n 
1 165 GLN n 
1 166 VAL n 
1 167 GLN n 
1 168 VAL n 
1 169 PRO n 
1 170 THR n 
1 171 PHE n 
1 172 ILE n 
1 173 ILE n 
1 174 GLY n 
1 175 ALA n 
1 176 GLU n 
1 177 LEU n 
1 178 ASP n 
1 179 THR n 
1 180 ILE n 
1 181 ALA n 
1 182 PRO n 
1 183 VAL n 
1 184 SER n 
1 185 THR n 
1 186 HIS n 
1 187 ALA n 
1 188 LYS n 
1 189 PRO n 
1 190 PHE n 
1 191 TYR n 
1 192 GLU n 
1 193 SER n 
1 194 LEU n 
1 195 PRO n 
1 196 SER n 
1 197 SER n 
1 198 LEU n 
1 199 PRO n 
1 200 LYS n 
1 201 ALA n 
1 202 TYR n 
1 203 MET n 
1 204 GLU n 
1 205 LEU n 
1 206 CYS n 
1 207 GLY n 
1 208 ALA n 
1 209 THR n 
1 210 HIS n 
1 211 PHE n 
1 212 ALA n 
1 213 PRO n 
1 214 ASN n 
1 215 ILE n 
1 216 PRO n 
1 217 ASN n 
1 218 THR n 
1 219 THR n 
1 220 ILE n 
1 221 ALA n 
1 222 LYS n 
1 223 TYR n 
1 224 VAL n 
1 225 ILE n 
1 226 SER n 
1 227 TRP n 
1 228 LEU n 
1 229 LYS n 
1 230 ARG n 
1 231 PHE n 
1 232 VAL n 
1 233 ASP n 
1 234 GLU n 
1 235 ASP n 
1 236 THR n 
1 237 ARG n 
1 238 TYR n 
1 239 SER n 
1 240 GLN n 
1 241 PHE n 
1 242 LEU n 
1 243 CYS n 
1 244 PRO n 
1 245 ASN n 
1 246 PRO n 
1 247 THR n 
1 248 ASP n 
1 249 ARG n 
1 250 ALA n 
1 251 ILE n 
1 252 CYS n 
1 253 GLU n 
1 254 TYR n 
1 255 ARG n 
1 256 SER n 
1 257 THR n 
1 258 CYS n 
1 259 PRO n 
1 260 TYR 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                   260 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Cut190, MINT15_00360' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Saccharomonospora viridis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1852 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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               'Rosetta-gami B(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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pQE80L 
_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 
A1L0M non-polymer         . '(4-methoxycarbonylphenyl)-(2-phenylmethoxyethoxy)phosphinic acid' ? 'C17 H19 O6 P'   350.303 
ACT   non-polymer         . 'ACETATE ION'                                                      ? 'C2 H3 O2 -1'    59.044  
ALA   'L-peptide linking' y ALANINE                                                            ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                           ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                         ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                    ? 'C4 H7 N O4'     133.103 
CA    non-polymer         . 'CALCIUM ION'                                                      ? 'Ca 2'           40.078  
CL    non-polymer         . 'CHLORIDE ION'                                                     ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                          ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                    ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                            ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                          ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                              ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                            ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                             ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                         ? 'C5 H11 N O2 S'  149.211 
MPD   non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL'                                    ? 'C6 H14 O2'      118.174 
PHE   'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                          ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                         ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                           ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   45  ?   ?   ?   A . n 
A 1 2   PRO 2   46  46  PRO PRO A . n 
A 1 3   ASN 3   47  47  ASN ASN A . n 
A 1 4   PRO 4   48  48  PRO PRO A . n 
A 1 5   TYR 5   49  49  TYR TYR A . n 
A 1 6   GLU 6   50  50  GLU GLU A . n 
A 1 7   ARG 7   51  51  ARG ARG A . n 
A 1 8   GLY 8   52  52  GLY GLY A . n 
A 1 9   PRO 9   53  53  PRO PRO A . n 
A 1 10  ASP 10  54  54  ASP ASP A . n 
A 1 11  PRO 11  55  55  PRO PRO A . n 
A 1 12  THR 12  56  56  THR THR A . n 
A 1 13  GLU 13  57  57  GLU GLU A . n 
A 1 14  ASP 14  58  58  ASP ASP A . n 
A 1 15  SER 15  59  59  SER SER A . n 
A 1 16  ILE 16  60  60  ILE ILE A . n 
A 1 17  GLU 17  61  61  GLU GLU A . n 
A 1 18  ALA 18  62  62  ALA ALA A . n 
A 1 19  ILE 19  63  63  ILE ILE A . n 
A 1 20  ARG 20  64  64  ARG ARG A . n 
A 1 21  GLY 21  65  65  GLY GLY A . n 
A 1 22  PRO 22  66  66  PRO PRO A . n 
A 1 23  PHE 23  67  67  PHE PHE A . n 
A 1 24  SER 24  68  68  SER SER A . n 
A 1 25  VAL 25  69  69  VAL VAL A . n 
A 1 26  ALA 26  70  70  ALA ALA A . n 
A 1 27  THR 27  71  71  THR THR A . n 
A 1 28  GLU 28  72  72  GLU GLU A . n 
A 1 29  ARG 29  73  73  ARG ARG A . n 
A 1 30  VAL 30  74  74  VAL VAL A . n 
A 1 31  SER 31  75  75  SER SER A . n 
A 1 32  SER 32  76  76  SER SER A . n 
A 1 33  PHE 33  77  77  PHE PHE A . n 
A 1 34  ALA 34  78  78  ALA ALA A . n 
A 1 35  SER 35  79  79  SER SER A . n 
A 1 36  GLY 36  80  80  GLY GLY A . n 
A 1 37  PHE 37  81  81  PHE PHE A . n 
A 1 38  GLY 38  82  82  GLY GLY A . n 
A 1 39  GLY 39  83  83  GLY GLY A . n 
A 1 40  GLY 40  84  84  GLY GLY A . n 
A 1 41  THR 41  85  85  THR THR A . n 
A 1 42  ILE 42  86  86  ILE ILE A . n 
A 1 43  TYR 43  87  87  TYR TYR A . n 
A 1 44  TYR 44  88  88  TYR TYR A . n 
A 1 45  PRO 45  89  89  PRO PRO A . n 
A 1 46  ARG 46  90  90  ARG ARG A . n 
A 1 47  GLU 47  91  91  GLU GLU A . n 
A 1 48  THR 48  92  92  THR THR A . n 
A 1 49  ASP 49  93  93  ASP ASP A . n 
A 1 50  GLU 50  94  94  GLU GLU A . n 
A 1 51  GLY 51  95  95  GLY GLY A . n 
A 1 52  THR 52  96  96  THR THR A . n 
A 1 53  PHE 53  97  97  PHE PHE A . n 
A 1 54  GLY 54  98  98  GLY GLY A . n 
A 1 55  ALA 55  99  99  ALA ALA A . n 
A 1 56  VAL 56  100 100 VAL VAL A . n 
A 1 57  ALA 57  101 101 ALA ALA A . n 
A 1 58  VAL 58  102 102 VAL VAL A . n 
A 1 59  ALA 59  103 103 ALA ALA A . n 
A 1 60  PRO 60  104 104 PRO PRO A . n 
A 1 61  GLY 61  105 105 GLY GLY A . n 
A 1 62  PHE 62  106 106 PHE PHE A . n 
A 1 63  THR 63  107 107 THR THR A . n 
A 1 64  ALA 64  108 108 ALA ALA A . n 
A 1 65  SER 65  109 109 SER SER A . n 
A 1 66  GLN 66  110 110 GLN GLN A . n 
A 1 67  GLY 67  111 111 GLY GLY A . n 
A 1 68  SER 68  112 112 SER SER A . n 
A 1 69  MET 69  113 113 MET MET A . n 
A 1 70  SER 70  114 114 SER SER A . n 
A 1 71  TRP 71  115 115 TRP TRP A . n 
A 1 72  TYR 72  116 116 TYR TYR A . n 
A 1 73  GLY 73  117 117 GLY GLY A . n 
A 1 74  GLU 74  118 118 GLU GLU A . n 
A 1 75  ARG 75  119 119 ARG ARG A . n 
A 1 76  VAL 76  120 120 VAL VAL A . n 
A 1 77  ALA 77  121 121 ALA ALA A . n 
A 1 78  SER 78  122 122 SER SER A . n 
A 1 79  HIS 79  123 123 HIS HIS A . n 
A 1 80  GLY 80  124 124 GLY GLY A . n 
A 1 81  PHE 81  125 125 PHE PHE A . n 
A 1 82  ILE 82  126 126 ILE ILE A . n 
A 1 83  VAL 83  127 127 VAL VAL A . n 
A 1 84  PHE 84  128 128 PHE PHE A . n 
A 1 85  THR 85  129 129 THR THR A . n 
A 1 86  ILE 86  130 130 ILE ILE A . n 
A 1 87  ASP 87  131 131 ASP ASP A . n 
A 1 88  THR 88  132 132 THR THR A . n 
A 1 89  ASN 89  133 133 ASN ASN A . n 
A 1 90  THR 90  134 134 THR THR A . n 
A 1 91  ARG 91  135 135 ARG ARG A . n 
A 1 92  LEU 92  136 136 LEU LEU A . n 
A 1 93  ASP 93  137 137 ASP ASP A . n 
A 1 94  ALA 94  138 138 ALA ALA A . n 
A 1 95  PRO 95  139 139 PRO PRO A . n 
A 1 96  GLY 96  140 140 GLY GLY A . n 
A 1 97  GLN 97  141 141 GLN GLN A . n 
A 1 98  ARG 98  142 142 ARG ARG A . n 
A 1 99  GLY 99  143 143 GLY GLY A . n 
A 1 100 ARG 100 144 144 ARG ARG A . n 
A 1 101 GLN 101 145 145 GLN GLN A . n 
A 1 102 LEU 102 146 146 LEU LEU A . n 
A 1 103 LEU 103 147 147 LEU LEU A . n 
A 1 104 ALA 104 148 148 ALA ALA A . n 
A 1 105 ALA 105 149 149 ALA ALA A . n 
A 1 106 LEU 106 150 150 LEU LEU A . n 
A 1 107 ASP 107 151 151 ASP ASP A . n 
A 1 108 TYR 108 152 152 TYR TYR A . n 
A 1 109 LEU 109 153 153 LEU LEU A . n 
A 1 110 VAL 110 154 154 VAL VAL A . n 
A 1 111 GLU 111 155 155 GLU GLU A . n 
A 1 112 ARG 112 156 156 ARG ARG A . n 
A 1 113 SER 113 157 157 SER SER A . n 
A 1 114 ASP 114 158 158 ASP ASP A . n 
A 1 115 ARG 115 159 159 ARG ARG A . n 
A 1 116 LYS 116 160 160 LYS LYS A . n 
A 1 117 VAL 117 161 161 VAL VAL A . n 
A 1 118 ARG 118 162 162 ARG ARG A . n 
A 1 119 GLU 119 163 163 GLU GLU A . n 
A 1 120 ARG 120 164 164 ARG ARG A . n 
A 1 121 LEU 121 165 165 LEU LEU A . n 
A 1 122 ASP 122 166 166 ASP ASP A . n 
A 1 123 PRO 123 167 167 PRO PRO A . n 
A 1 124 ASN 124 168 168 ASN ASN A . n 
A 1 125 ARG 125 169 169 ARG ARG A . n 
A 1 126 LEU 126 170 170 LEU LEU A . n 
A 1 127 ALA 127 171 171 ALA ALA A . n 
A 1 128 VAL 128 172 172 VAL VAL A . n 
A 1 129 MET 129 173 173 MET MET A . n 
A 1 130 GLY 130 174 174 GLY GLY A . n 
A 1 131 HIS 131 175 175 HIS HIS A . n 
A 1 132 ALA 132 176 176 ALA ALA A . n 
A 1 133 MET 133 177 177 MET MET A . n 
A 1 134 GLY 134 178 178 GLY GLY A . n 
A 1 135 GLY 135 179 179 GLY GLY A . n 
A 1 136 GLY 136 180 180 GLY GLY A . n 
A 1 137 GLY 137 181 181 GLY GLY A . n 
A 1 138 SER 138 182 182 SER SER A . n 
A 1 139 LEU 139 183 183 LEU LEU A . n 
A 1 140 GLU 140 184 184 GLU GLU A . n 
A 1 141 ALA 141 185 185 ALA ALA A . n 
A 1 142 THR 142 186 186 THR THR A . n 
A 1 143 VAL 143 187 187 VAL VAL A . n 
A 1 144 MET 144 188 188 MET MET A . n 
A 1 145 ARG 145 189 189 ARG ARG A . n 
A 1 146 PRO 146 190 190 PRO PRO A . n 
A 1 147 SER 147 191 191 SER SER A . n 
A 1 148 LEU 148 192 192 LEU LEU A . n 
A 1 149 LYS 149 193 193 LYS LYS A . n 
A 1 150 ALA 150 194 194 ALA ALA A . n 
A 1 151 SER 151 195 195 SER SER A . n 
A 1 152 ILE 152 196 196 ILE ILE A . n 
A 1 153 PRO 153 197 197 PRO PRO A . n 
A 1 154 LEU 154 198 198 LEU LEU A . n 
A 1 155 THR 155 199 199 THR THR A . n 
A 1 156 PRO 156 200 200 PRO PRO A . n 
A 1 157 TRP 157 201 201 TRP TRP A . n 
A 1 158 HIS 158 202 202 HIS HIS A . n 
A 1 159 LEU 159 203 203 LEU LEU A . n 
A 1 160 ASP 160 204 204 ASP ASP A . n 
A 1 161 LYS 161 205 205 LYS LYS A . n 
A 1 162 THR 162 206 206 THR THR A . n 
A 1 163 TRP 163 207 207 TRP TRP A . n 
A 1 164 GLY 164 208 208 GLY GLY A . n 
A 1 165 GLN 165 209 209 GLN GLN A . n 
A 1 166 VAL 166 210 210 VAL VAL A . n 
A 1 167 GLN 167 211 211 GLN GLN A . n 
A 1 168 VAL 168 212 212 VAL VAL A . n 
A 1 169 PRO 169 213 213 PRO PRO A . n 
A 1 170 THR 170 214 214 THR THR A . n 
A 1 171 PHE 171 215 215 PHE PHE A . n 
A 1 172 ILE 172 216 216 ILE ILE A . n 
A 1 173 ILE 173 217 217 ILE ILE A . n 
A 1 174 GLY 174 218 218 GLY GLY A . n 
A 1 175 ALA 175 219 219 ALA ALA A . n 
A 1 176 GLU 176 220 220 GLU GLU A . n 
A 1 177 LEU 177 221 221 LEU LEU A . n 
A 1 178 ASP 178 222 222 ASP ASP A . n 
A 1 179 THR 179 223 223 THR THR A . n 
A 1 180 ILE 180 224 224 ILE ILE A . n 
A 1 181 ALA 181 225 225 ALA ALA A . n 
A 1 182 PRO 182 226 226 PRO PRO A . n 
A 1 183 VAL 183 227 227 VAL VAL A . n 
A 1 184 SER 184 228 228 SER SER A . n 
A 1 185 THR 185 229 229 THR THR A . n 
A 1 186 HIS 186 230 230 HIS HIS A . n 
A 1 187 ALA 187 231 231 ALA ALA A . n 
A 1 188 LYS 188 232 232 LYS LYS A . n 
A 1 189 PRO 189 233 233 PRO PRO A . n 
A 1 190 PHE 190 234 234 PHE PHE A . n 
A 1 191 TYR 191 235 235 TYR TYR A . n 
A 1 192 GLU 192 236 236 GLU GLU A . n 
A 1 193 SER 193 237 237 SER SER A . n 
A 1 194 LEU 194 238 238 LEU LEU A . n 
A 1 195 PRO 195 239 239 PRO PRO A . n 
A 1 196 SER 196 240 240 SER SER A . n 
A 1 197 SER 197 241 241 SER SER A . n 
A 1 198 LEU 198 242 242 LEU LEU A . n 
A 1 199 PRO 199 243 243 PRO PRO A . n 
A 1 200 LYS 200 244 244 LYS LYS A . n 
A 1 201 ALA 201 245 245 ALA ALA A . n 
A 1 202 TYR 202 246 246 TYR TYR A . n 
A 1 203 MET 203 247 247 MET MET A . n 
A 1 204 GLU 204 248 248 GLU GLU A . n 
A 1 205 LEU 205 249 249 LEU LEU A . n 
A 1 206 CYS 206 250 250 CYS CYS A . n 
A 1 207 GLY 207 251 251 GLY GLY A . n 
A 1 208 ALA 208 252 252 ALA ALA A . n 
A 1 209 THR 209 253 253 THR THR A . n 
A 1 210 HIS 210 254 254 HIS HIS A . n 
A 1 211 PHE 211 255 255 PHE PHE A . n 
A 1 212 ALA 212 256 256 ALA ALA A . n 
A 1 213 PRO 213 257 257 PRO PRO A . n 
A 1 214 ASN 214 258 258 ASN ASN A . n 
A 1 215 ILE 215 259 259 ILE ILE A . n 
A 1 216 PRO 216 260 260 PRO PRO A . n 
A 1 217 ASN 217 261 261 ASN ASN A . n 
A 1 218 THR 218 262 262 THR THR A . n 
A 1 219 THR 219 263 263 THR THR A . n 
A 1 220 ILE 220 264 264 ILE ILE A . n 
A 1 221 ALA 221 265 265 ALA ALA A . n 
A 1 222 LYS 222 266 266 LYS LYS A . n 
A 1 223 TYR 223 267 267 TYR TYR A . n 
A 1 224 VAL 224 268 268 VAL VAL A . n 
A 1 225 ILE 225 269 269 ILE ILE A . n 
A 1 226 SER 226 270 270 SER SER A . n 
A 1 227 TRP 227 271 271 TRP TRP A . n 
A 1 228 LEU 228 272 272 LEU LEU A . n 
A 1 229 LYS 229 273 273 LYS LYS A . n 
A 1 230 ARG 230 274 274 ARG ARG A . n 
A 1 231 PHE 231 275 275 PHE PHE A . n 
A 1 232 VAL 232 276 276 VAL VAL A . n 
A 1 233 ASP 233 277 277 ASP ASP A . n 
A 1 234 GLU 234 278 278 GLU GLU A . n 
A 1 235 ASP 235 279 279 ASP ASP A . n 
A 1 236 THR 236 280 280 THR THR A . n 
A 1 237 ARG 237 281 281 ARG ARG A . n 
A 1 238 TYR 238 282 282 TYR TYR A . n 
A 1 239 SER 239 283 283 SER SER A . n 
A 1 240 GLN 240 284 284 GLN GLN A . n 
A 1 241 PHE 241 285 285 PHE PHE A . n 
A 1 242 LEU 242 286 286 LEU LEU A . n 
A 1 243 CYS 243 287 287 CYS CYS A . n 
A 1 244 PRO 244 288 288 PRO PRO A . n 
A 1 245 ASN 245 289 289 ASN ASN A . n 
A 1 246 PRO 246 290 290 PRO PRO A . n 
A 1 247 THR 247 291 291 THR THR A . n 
A 1 248 ASP 248 292 292 ASP ASP A . n 
A 1 249 ARG 249 293 293 ARG ARG A . n 
A 1 250 ALA 250 294 294 ALA ALA A . n 
A 1 251 ILE 251 295 295 ILE ILE A . n 
A 1 252 CYS 252 296 296 CYS CYS A . n 
A 1 253 GLU 253 297 297 GLU GLU A . n 
A 1 254 TYR 254 298 298 TYR TYR A . n 
A 1 255 ARG 255 299 299 ARG ARG A . n 
A 1 256 SER 256 300 300 SER SER A . n 
A 1 257 THR 257 301 301 THR THR A . n 
A 1 258 CYS 258 302 302 CYS CYS A . n 
A 1 259 PRO 259 303 303 PRO PRO A . n 
A 1 260 TYR 260 304 304 TYR TYR A . n 
B 1 1   GLY 1   45  ?   ?   ?   B . n 
B 1 2   PRO 2   46  46  PRO PRO B . n 
B 1 3   ASN 3   47  47  ASN ASN B . n 
B 1 4   PRO 4   48  48  PRO PRO B . n 
B 1 5   TYR 5   49  49  TYR TYR B . n 
B 1 6   GLU 6   50  50  GLU GLU B . n 
B 1 7   ARG 7   51  51  ARG ARG B . n 
B 1 8   GLY 8   52  52  GLY GLY B . n 
B 1 9   PRO 9   53  53  PRO PRO B . n 
B 1 10  ASP 10  54  54  ASP ASP B . n 
B 1 11  PRO 11  55  55  PRO PRO B . n 
B 1 12  THR 12  56  56  THR THR B . n 
B 1 13  GLU 13  57  57  GLU GLU B . n 
B 1 14  ASP 14  58  58  ASP ASP B . n 
B 1 15  SER 15  59  59  SER SER B . n 
B 1 16  ILE 16  60  60  ILE ILE B . n 
B 1 17  GLU 17  61  61  GLU GLU B . n 
B 1 18  ALA 18  62  62  ALA ALA B . n 
B 1 19  ILE 19  63  63  ILE ILE B . n 
B 1 20  ARG 20  64  64  ARG ARG B . n 
B 1 21  GLY 21  65  65  GLY GLY B . n 
B 1 22  PRO 22  66  66  PRO PRO B . n 
B 1 23  PHE 23  67  67  PHE PHE B . n 
B 1 24  SER 24  68  68  SER SER B . n 
B 1 25  VAL 25  69  69  VAL VAL B . n 
B 1 26  ALA 26  70  70  ALA ALA B . n 
B 1 27  THR 27  71  71  THR THR B . n 
B 1 28  GLU 28  72  72  GLU GLU B . n 
B 1 29  ARG 29  73  73  ARG ARG B . n 
B 1 30  VAL 30  74  74  VAL VAL B . n 
B 1 31  SER 31  75  75  SER SER B . n 
B 1 32  SER 32  76  76  SER SER B . n 
B 1 33  PHE 33  77  77  PHE PHE B . n 
B 1 34  ALA 34  78  78  ALA ALA B . n 
B 1 35  SER 35  79  79  SER SER B . n 
B 1 36  GLY 36  80  80  GLY GLY B . n 
B 1 37  PHE 37  81  81  PHE PHE B . n 
B 1 38  GLY 38  82  82  GLY GLY B . n 
B 1 39  GLY 39  83  83  GLY GLY B . n 
B 1 40  GLY 40  84  84  GLY GLY B . n 
B 1 41  THR 41  85  85  THR THR B . n 
B 1 42  ILE 42  86  86  ILE ILE B . n 
B 1 43  TYR 43  87  87  TYR TYR B . n 
B 1 44  TYR 44  88  88  TYR TYR B . n 
B 1 45  PRO 45  89  89  PRO PRO B . n 
B 1 46  ARG 46  90  90  ARG ARG B . n 
B 1 47  GLU 47  91  91  GLU GLU B . n 
B 1 48  THR 48  92  92  THR THR B . n 
B 1 49  ASP 49  93  93  ASP ASP B . n 
B 1 50  GLU 50  94  94  GLU GLU B . n 
B 1 51  GLY 51  95  95  GLY GLY B . n 
B 1 52  THR 52  96  96  THR THR B . n 
B 1 53  PHE 53  97  97  PHE PHE B . n 
B 1 54  GLY 54  98  98  GLY GLY B . n 
B 1 55  ALA 55  99  99  ALA ALA B . n 
B 1 56  VAL 56  100 100 VAL VAL B . n 
B 1 57  ALA 57  101 101 ALA ALA B . n 
B 1 58  VAL 58  102 102 VAL VAL B . n 
B 1 59  ALA 59  103 103 ALA ALA B . n 
B 1 60  PRO 60  104 104 PRO PRO B . n 
B 1 61  GLY 61  105 105 GLY GLY B . n 
B 1 62  PHE 62  106 106 PHE PHE B . n 
B 1 63  THR 63  107 107 THR THR B . n 
B 1 64  ALA 64  108 108 ALA ALA B . n 
B 1 65  SER 65  109 109 SER SER B . n 
B 1 66  GLN 66  110 110 GLN GLN B . n 
B 1 67  GLY 67  111 111 GLY GLY B . n 
B 1 68  SER 68  112 112 SER SER B . n 
B 1 69  MET 69  113 113 MET MET B . n 
B 1 70  SER 70  114 114 SER SER B . n 
B 1 71  TRP 71  115 115 TRP TRP B . n 
B 1 72  TYR 72  116 116 TYR TYR B . n 
B 1 73  GLY 73  117 117 GLY GLY B . n 
B 1 74  GLU 74  118 118 GLU GLU B . n 
B 1 75  ARG 75  119 119 ARG ARG B . n 
B 1 76  VAL 76  120 120 VAL VAL B . n 
B 1 77  ALA 77  121 121 ALA ALA B . n 
B 1 78  SER 78  122 122 SER SER B . n 
B 1 79  HIS 79  123 123 HIS HIS B . n 
B 1 80  GLY 80  124 124 GLY GLY B . n 
B 1 81  PHE 81  125 125 PHE PHE B . n 
B 1 82  ILE 82  126 126 ILE ILE B . n 
B 1 83  VAL 83  127 127 VAL VAL B . n 
B 1 84  PHE 84  128 128 PHE PHE B . n 
B 1 85  THR 85  129 129 THR THR B . n 
B 1 86  ILE 86  130 130 ILE ILE B . n 
B 1 87  ASP 87  131 131 ASP ASP B . n 
B 1 88  THR 88  132 132 THR THR B . n 
B 1 89  ASN 89  133 133 ASN ASN B . n 
B 1 90  THR 90  134 134 THR THR B . n 
B 1 91  ARG 91  135 135 ARG ARG B . n 
B 1 92  LEU 92  136 136 LEU LEU B . n 
B 1 93  ASP 93  137 137 ASP ASP B . n 
B 1 94  ALA 94  138 138 ALA ALA B . n 
B 1 95  PRO 95  139 139 PRO PRO B . n 
B 1 96  GLY 96  140 140 GLY GLY B . n 
B 1 97  GLN 97  141 141 GLN GLN B . n 
B 1 98  ARG 98  142 142 ARG ARG B . n 
B 1 99  GLY 99  143 143 GLY GLY B . n 
B 1 100 ARG 100 144 144 ARG ARG B . n 
B 1 101 GLN 101 145 145 GLN GLN B . n 
B 1 102 LEU 102 146 146 LEU LEU B . n 
B 1 103 LEU 103 147 147 LEU LEU B . n 
B 1 104 ALA 104 148 148 ALA ALA B . n 
B 1 105 ALA 105 149 149 ALA ALA B . n 
B 1 106 LEU 106 150 150 LEU LEU B . n 
B 1 107 ASP 107 151 151 ASP ASP B . n 
B 1 108 TYR 108 152 152 TYR TYR B . n 
B 1 109 LEU 109 153 153 LEU LEU B . n 
B 1 110 VAL 110 154 154 VAL VAL B . n 
B 1 111 GLU 111 155 155 GLU GLU B . n 
B 1 112 ARG 112 156 156 ARG ARG B . n 
B 1 113 SER 113 157 157 SER SER B . n 
B 1 114 ASP 114 158 158 ASP ASP B . n 
B 1 115 ARG 115 159 159 ARG ARG B . n 
B 1 116 LYS 116 160 160 LYS LYS B . n 
B 1 117 VAL 117 161 161 VAL VAL B . n 
B 1 118 ARG 118 162 162 ARG ARG B . n 
B 1 119 GLU 119 163 163 GLU GLU B . n 
B 1 120 ARG 120 164 164 ARG ARG B . n 
B 1 121 LEU 121 165 165 LEU LEU B . n 
B 1 122 ASP 122 166 166 ASP ASP B . n 
B 1 123 PRO 123 167 167 PRO PRO B . n 
B 1 124 ASN 124 168 168 ASN ASN B . n 
B 1 125 ARG 125 169 169 ARG ARG B . n 
B 1 126 LEU 126 170 170 LEU LEU B . n 
B 1 127 ALA 127 171 171 ALA ALA B . n 
B 1 128 VAL 128 172 172 VAL VAL B . n 
B 1 129 MET 129 173 173 MET MET B . n 
B 1 130 GLY 130 174 174 GLY GLY B . n 
B 1 131 HIS 131 175 175 HIS HIS B . n 
B 1 132 ALA 132 176 176 ALA ALA B . n 
B 1 133 MET 133 177 177 MET MET B . n 
B 1 134 GLY 134 178 178 GLY GLY B . n 
B 1 135 GLY 135 179 179 GLY GLY B . n 
B 1 136 GLY 136 180 180 GLY GLY B . n 
B 1 137 GLY 137 181 181 GLY GLY B . n 
B 1 138 SER 138 182 182 SER SER B . n 
B 1 139 LEU 139 183 183 LEU LEU B . n 
B 1 140 GLU 140 184 184 GLU GLU B . n 
B 1 141 ALA 141 185 185 ALA ALA B . n 
B 1 142 THR 142 186 186 THR THR B . n 
B 1 143 VAL 143 187 187 VAL VAL B . n 
B 1 144 MET 144 188 188 MET MET B . n 
B 1 145 ARG 145 189 189 ARG ARG B . n 
B 1 146 PRO 146 190 190 PRO PRO B . n 
B 1 147 SER 147 191 191 SER SER B . n 
B 1 148 LEU 148 192 192 LEU LEU B . n 
B 1 149 LYS 149 193 193 LYS LYS B . n 
B 1 150 ALA 150 194 194 ALA ALA B . n 
B 1 151 SER 151 195 195 SER SER B . n 
B 1 152 ILE 152 196 196 ILE ILE B . n 
B 1 153 PRO 153 197 197 PRO PRO B . n 
B 1 154 LEU 154 198 198 LEU LEU B . n 
B 1 155 THR 155 199 199 THR THR B . n 
B 1 156 PRO 156 200 200 PRO PRO B . n 
B 1 157 TRP 157 201 201 TRP TRP B . n 
B 1 158 HIS 158 202 202 HIS HIS B . n 
B 1 159 LEU 159 203 203 LEU LEU B . n 
B 1 160 ASP 160 204 204 ASP ASP B . n 
B 1 161 LYS 161 205 205 LYS LYS B . n 
B 1 162 THR 162 206 206 THR THR B . n 
B 1 163 TRP 163 207 207 TRP TRP B . n 
B 1 164 GLY 164 208 208 GLY GLY B . n 
B 1 165 GLN 165 209 209 GLN GLN B . n 
B 1 166 VAL 166 210 210 VAL VAL B . n 
B 1 167 GLN 167 211 211 GLN GLN B . n 
B 1 168 VAL 168 212 212 VAL VAL B . n 
B 1 169 PRO 169 213 213 PRO PRO B . n 
B 1 170 THR 170 214 214 THR THR B . n 
B 1 171 PHE 171 215 215 PHE PHE B . n 
B 1 172 ILE 172 216 216 ILE ILE B . n 
B 1 173 ILE 173 217 217 ILE ILE B . n 
B 1 174 GLY 174 218 218 GLY GLY B . n 
B 1 175 ALA 175 219 219 ALA ALA B . n 
B 1 176 GLU 176 220 220 GLU GLU B . n 
B 1 177 LEU 177 221 221 LEU LEU B . n 
B 1 178 ASP 178 222 222 ASP ASP B . n 
B 1 179 THR 179 223 223 THR THR B . n 
B 1 180 ILE 180 224 224 ILE ILE B . n 
B 1 181 ALA 181 225 225 ALA ALA B . n 
B 1 182 PRO 182 226 226 PRO PRO B . n 
B 1 183 VAL 183 227 227 VAL VAL B . n 
B 1 184 SER 184 228 228 SER SER B . n 
B 1 185 THR 185 229 229 THR THR B . n 
B 1 186 HIS 186 230 230 HIS HIS B . n 
B 1 187 ALA 187 231 231 ALA ALA B . n 
B 1 188 LYS 188 232 232 LYS LYS B . n 
B 1 189 PRO 189 233 233 PRO PRO B . n 
B 1 190 PHE 190 234 234 PHE PHE B . n 
B 1 191 TYR 191 235 235 TYR TYR B . n 
B 1 192 GLU 192 236 236 GLU GLU B . n 
B 1 193 SER 193 237 237 SER SER B . n 
B 1 194 LEU 194 238 238 LEU LEU B . n 
B 1 195 PRO 195 239 239 PRO PRO B . n 
B 1 196 SER 196 240 240 SER SER B . n 
B 1 197 SER 197 241 241 SER SER B . n 
B 1 198 LEU 198 242 242 LEU LEU B . n 
B 1 199 PRO 199 243 243 PRO PRO B . n 
B 1 200 LYS 200 244 244 LYS LYS B . n 
B 1 201 ALA 201 245 245 ALA ALA B . n 
B 1 202 TYR 202 246 246 TYR TYR B . n 
B 1 203 MET 203 247 247 MET MET B . n 
B 1 204 GLU 204 248 248 GLU GLU B . n 
B 1 205 LEU 205 249 249 LEU LEU B . n 
B 1 206 CYS 206 250 250 CYS CYS B . n 
B 1 207 GLY 207 251 251 GLY GLY B . n 
B 1 208 ALA 208 252 252 ALA ALA B . n 
B 1 209 THR 209 253 253 THR THR B . n 
B 1 210 HIS 210 254 254 HIS HIS B . n 
B 1 211 PHE 211 255 255 PHE PHE B . n 
B 1 212 ALA 212 256 256 ALA ALA B . n 
B 1 213 PRO 213 257 257 PRO PRO B . n 
B 1 214 ASN 214 258 258 ASN ASN B . n 
B 1 215 ILE 215 259 259 ILE ILE B . n 
B 1 216 PRO 216 260 260 PRO PRO B . n 
B 1 217 ASN 217 261 261 ASN ASN B . n 
B 1 218 THR 218 262 262 THR THR B . n 
B 1 219 THR 219 263 263 THR THR B . n 
B 1 220 ILE 220 264 264 ILE ILE B . n 
B 1 221 ALA 221 265 265 ALA ALA B . n 
B 1 222 LYS 222 266 266 LYS LYS B . n 
B 1 223 TYR 223 267 267 TYR TYR B . n 
B 1 224 VAL 224 268 268 VAL VAL B . n 
B 1 225 ILE 225 269 269 ILE ILE B . n 
B 1 226 SER 226 270 270 SER SER B . n 
B 1 227 TRP 227 271 271 TRP TRP B . n 
B 1 228 LEU 228 272 272 LEU LEU B . n 
B 1 229 LYS 229 273 273 LYS LYS B . n 
B 1 230 ARG 230 274 274 ARG ARG B . n 
B 1 231 PHE 231 275 275 PHE PHE B . n 
B 1 232 VAL 232 276 276 VAL VAL B . n 
B 1 233 ASP 233 277 277 ASP ASP B . n 
B 1 234 GLU 234 278 278 GLU GLU B . n 
B 1 235 ASP 235 279 279 ASP ASP B . n 
B 1 236 THR 236 280 280 THR THR B . n 
B 1 237 ARG 237 281 281 ARG ARG B . n 
B 1 238 TYR 238 282 282 TYR TYR B . n 
B 1 239 SER 239 283 283 SER SER B . n 
B 1 240 GLN 240 284 284 GLN GLN B . n 
B 1 241 PHE 241 285 285 PHE PHE B . n 
B 1 242 LEU 242 286 286 LEU LEU B . n 
B 1 243 CYS 243 287 287 CYS CYS B . n 
B 1 244 PRO 244 288 288 PRO PRO B . n 
B 1 245 ASN 245 289 289 ASN ASN B . n 
B 1 246 PRO 246 290 290 PRO PRO B . n 
B 1 247 THR 247 291 291 THR THR B . n 
B 1 248 ASP 248 292 292 ASP ASP B . n 
B 1 249 ARG 249 293 293 ARG ARG B . n 
B 1 250 ALA 250 294 294 ALA ALA B . n 
B 1 251 ILE 251 295 295 ILE ILE B . n 
B 1 252 CYS 252 296 296 CYS CYS B . n 
B 1 253 GLU 253 297 297 GLU GLU B . n 
B 1 254 TYR 254 298 298 TYR TYR B . n 
B 1 255 ARG 255 299 299 ARG ARG B . n 
B 1 256 SER 256 300 300 SER SER B . n 
B 1 257 THR 257 301 301 THR THR B . n 
B 1 258 CYS 258 302 302 CYS CYS B . n 
B 1 259 PRO 259 303 303 PRO PRO B . n 
B 1 260 TYR 260 304 304 TYR TYR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L0M 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L0M 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 MPD   1   401 401 MPD   MPD A . 
D 3 A1L0M 1   402 1   A1L0M DRG A . 
E 4 CA    1   403 1   CA    CA  A . 
F 4 CA    1   404 4   CA    CA  A . 
G 5 CL    1   405 1   CL    CL  A . 
H 2 MPD   1   401 401 MPD   MPD B . 
I 6 ACT   1   402 402 ACT   ACY B . 
J 6 ACT   1   403 403 ACT   ACY B . 
K 3 A1L0M 1   404 2   A1L0M DRG B . 
L 4 CA    1   405 2   CA    CA  B . 
M 4 CA    1   406 3   CA    CA  B . 
N 5 CL    1   407 2   CL    CL  B . 
O 5 CL    1   408 3   CL    CL  B . 
P 7 HOH   1   501 346 HOH   HOH A . 
P 7 HOH   2   502 187 HOH   HOH A . 
P 7 HOH   3   503 487 HOH   HOH A . 
P 7 HOH   4   504 341 HOH   HOH A . 
P 7 HOH   5   505 423 HOH   HOH A . 
P 7 HOH   6   506 245 HOH   HOH A . 
P 7 HOH   7   507 137 HOH   HOH A . 
P 7 HOH   8   508 291 HOH   HOH A . 
P 7 HOH   9   509 195 HOH   HOH A . 
P 7 HOH   10  510 242 HOH   HOH A . 
P 7 HOH   11  511 254 HOH   HOH A . 
P 7 HOH   12  512 304 HOH   HOH A . 
P 7 HOH   13  513 510 HOH   HOH A . 
P 7 HOH   14  514 456 HOH   HOH A . 
P 7 HOH   15  515 339 HOH   HOH A . 
P 7 HOH   16  516 361 HOH   HOH A . 
P 7 HOH   17  517 434 HOH   HOH A . 
P 7 HOH   18  518 142 HOH   HOH A . 
P 7 HOH   19  519 161 HOH   HOH A . 
P 7 HOH   20  520 231 HOH   HOH A . 
P 7 HOH   21  521 127 HOH   HOH A . 
P 7 HOH   22  522 465 HOH   HOH A . 
P 7 HOH   23  523 3   HOH   HOH A . 
P 7 HOH   24  524 488 HOH   HOH A . 
P 7 HOH   25  525 498 HOH   HOH A . 
P 7 HOH   26  526 140 HOH   HOH A . 
P 7 HOH   27  527 220 HOH   HOH A . 
P 7 HOH   28  528 353 HOH   HOH A . 
P 7 HOH   29  529 370 HOH   HOH A . 
P 7 HOH   30  530 263 HOH   HOH A . 
P 7 HOH   31  531 463 HOH   HOH A . 
P 7 HOH   32  532 8   HOH   HOH A . 
P 7 HOH   33  533 354 HOH   HOH A . 
P 7 HOH   34  534 223 HOH   HOH A . 
P 7 HOH   35  535 133 HOH   HOH A . 
P 7 HOH   36  536 428 HOH   HOH A . 
P 7 HOH   37  537 25  HOH   HOH A . 
P 7 HOH   38  538 491 HOH   HOH A . 
P 7 HOH   39  539 234 HOH   HOH A . 
P 7 HOH   40  540 92  HOH   HOH A . 
P 7 HOH   41  541 44  HOH   HOH A . 
P 7 HOH   42  542 521 HOH   HOH A . 
P 7 HOH   43  543 138 HOH   HOH A . 
P 7 HOH   44  544 440 HOH   HOH A . 
P 7 HOH   45  545 422 HOH   HOH A . 
P 7 HOH   46  546 112 HOH   HOH A . 
P 7 HOH   47  547 287 HOH   HOH A . 
P 7 HOH   48  548 166 HOH   HOH A . 
P 7 HOH   49  549 217 HOH   HOH A . 
P 7 HOH   50  550 279 HOH   HOH A . 
P 7 HOH   51  551 218 HOH   HOH A . 
P 7 HOH   52  552 260 HOH   HOH A . 
P 7 HOH   53  553 34  HOH   HOH A . 
P 7 HOH   54  554 414 HOH   HOH A . 
P 7 HOH   55  555 369 HOH   HOH A . 
P 7 HOH   56  556 12  HOH   HOH A . 
P 7 HOH   57  557 119 HOH   HOH A . 
P 7 HOH   58  558 55  HOH   HOH A . 
P 7 HOH   59  559 1   HOH   HOH A . 
P 7 HOH   60  560 235 HOH   HOH A . 
P 7 HOH   61  561 255 HOH   HOH A . 
P 7 HOH   62  562 376 HOH   HOH A . 
P 7 HOH   63  563 88  HOH   HOH A . 
P 7 HOH   64  564 267 HOH   HOH A . 
P 7 HOH   65  565 143 HOH   HOH A . 
P 7 HOH   66  566 97  HOH   HOH A . 
P 7 HOH   67  567 302 HOH   HOH A . 
P 7 HOH   68  568 276 HOH   HOH A . 
P 7 HOH   69  569 296 HOH   HOH A . 
P 7 HOH   70  570 151 HOH   HOH A . 
P 7 HOH   71  571 93  HOH   HOH A . 
P 7 HOH   72  572 322 HOH   HOH A . 
P 7 HOH   73  573 2   HOH   HOH A . 
P 7 HOH   74  574 379 HOH   HOH A . 
P 7 HOH   75  575 629 HOH   HOH A . 
P 7 HOH   76  576 43  HOH   HOH A . 
P 7 HOH   77  577 139 HOH   HOH A . 
P 7 HOH   78  578 389 HOH   HOH A . 
P 7 HOH   79  579 186 HOH   HOH A . 
P 7 HOH   80  580 519 HOH   HOH A . 
P 7 HOH   81  581 221 HOH   HOH A . 
P 7 HOH   82  582 11  HOH   HOH A . 
P 7 HOH   83  583 300 HOH   HOH A . 
P 7 HOH   84  584 50  HOH   HOH A . 
P 7 HOH   85  585 293 HOH   HOH A . 
P 7 HOH   86  586 71  HOH   HOH A . 
P 7 HOH   87  587 22  HOH   HOH A . 
P 7 HOH   88  588 98  HOH   HOH A . 
P 7 HOH   89  589 162 HOH   HOH A . 
P 7 HOH   90  590 124 HOH   HOH A . 
P 7 HOH   91  591 299 HOH   HOH A . 
P 7 HOH   92  592 67  HOH   HOH A . 
P 7 HOH   93  593 49  HOH   HOH A . 
P 7 HOH   94  594 135 HOH   HOH A . 
P 7 HOH   95  595 249 HOH   HOH A . 
P 7 HOH   96  596 141 HOH   HOH A . 
P 7 HOH   97  597 62  HOH   HOH A . 
P 7 HOH   98  598 149 HOH   HOH A . 
P 7 HOH   99  599 116 HOH   HOH A . 
P 7 HOH   100 600 355 HOH   HOH A . 
P 7 HOH   101 601 182 HOH   HOH A . 
P 7 HOH   102 602 323 HOH   HOH A . 
P 7 HOH   103 603 35  HOH   HOH A . 
P 7 HOH   104 604 564 HOH   HOH A . 
P 7 HOH   105 605 475 HOH   HOH A . 
P 7 HOH   106 606 390 HOH   HOH A . 
P 7 HOH   107 607 52  HOH   HOH A . 
P 7 HOH   108 608 312 HOH   HOH A . 
P 7 HOH   109 609 216 HOH   HOH A . 
P 7 HOH   110 610 144 HOH   HOH A . 
P 7 HOH   111 611 173 HOH   HOH A . 
P 7 HOH   112 612 170 HOH   HOH A . 
P 7 HOH   113 613 426 HOH   HOH A . 
P 7 HOH   114 614 61  HOH   HOH A . 
P 7 HOH   115 615 460 HOH   HOH A . 
P 7 HOH   116 616 53  HOH   HOH A . 
P 7 HOH   117 617 246 HOH   HOH A . 
P 7 HOH   118 618 31  HOH   HOH A . 
P 7 HOH   119 619 28  HOH   HOH A . 
P 7 HOH   120 620 325 HOH   HOH A . 
P 7 HOH   121 621 77  HOH   HOH A . 
P 7 HOH   122 622 533 HOH   HOH A . 
P 7 HOH   123 623 204 HOH   HOH A . 
P 7 HOH   124 624 449 HOH   HOH A . 
P 7 HOH   125 625 37  HOH   HOH A . 
P 7 HOH   126 626 232 HOH   HOH A . 
P 7 HOH   127 627 269 HOH   HOH A . 
P 7 HOH   128 628 437 HOH   HOH A . 
P 7 HOH   129 629 156 HOH   HOH A . 
P 7 HOH   130 630 407 HOH   HOH A . 
P 7 HOH   131 631 387 HOH   HOH A . 
P 7 HOH   132 632 616 HOH   HOH A . 
P 7 HOH   133 633 79  HOH   HOH A . 
P 7 HOH   134 634 76  HOH   HOH A . 
P 7 HOH   135 635 542 HOH   HOH A . 
P 7 HOH   136 636 294 HOH   HOH A . 
P 7 HOH   137 637 621 HOH   HOH A . 
P 7 HOH   138 638 117 HOH   HOH A . 
P 7 HOH   139 639 275 HOH   HOH A . 
P 7 HOH   140 640 69  HOH   HOH A . 
P 7 HOH   141 641 624 HOH   HOH A . 
P 7 HOH   142 642 525 HOH   HOH A . 
P 7 HOH   143 643 73  HOH   HOH A . 
P 7 HOH   144 644 610 HOH   HOH A . 
P 7 HOH   145 645 10  HOH   HOH A . 
P 7 HOH   146 646 74  HOH   HOH A . 
P 7 HOH   147 647 4   HOH   HOH A . 
P 7 HOH   148 648 265 HOH   HOH A . 
P 7 HOH   149 649 84  HOH   HOH A . 
P 7 HOH   150 650 66  HOH   HOH A . 
P 7 HOH   151 651 314 HOH   HOH A . 
P 7 HOH   152 652 96  HOH   HOH A . 
P 7 HOH   153 653 177 HOH   HOH A . 
P 7 HOH   154 654 562 HOH   HOH A . 
P 7 HOH   155 655 288 HOH   HOH A . 
P 7 HOH   156 656 252 HOH   HOH A . 
P 7 HOH   157 657 241 HOH   HOH A . 
P 7 HOH   158 658 174 HOH   HOH A . 
P 7 HOH   159 659 607 HOH   HOH A . 
P 7 HOH   160 660 277 HOH   HOH A . 
P 7 HOH   161 661 75  HOH   HOH A . 
P 7 HOH   162 662 424 HOH   HOH A . 
P 7 HOH   163 663 532 HOH   HOH A . 
P 7 HOH   164 664 81  HOH   HOH A . 
P 7 HOH   165 665 83  HOH   HOH A . 
P 7 HOH   166 666 326 HOH   HOH A . 
P 7 HOH   167 667 225 HOH   HOH A . 
P 7 HOH   168 668 23  HOH   HOH A . 
P 7 HOH   169 669 540 HOH   HOH A . 
P 7 HOH   170 670 64  HOH   HOH A . 
P 7 HOH   171 671 78  HOH   HOH A . 
P 7 HOH   172 672 297 HOH   HOH A . 
P 7 HOH   173 673 356 HOH   HOH A . 
P 7 HOH   174 674 251 HOH   HOH A . 
P 7 HOH   175 675 419 HOH   HOH A . 
P 7 HOH   176 676 68  HOH   HOH A . 
P 7 HOH   177 677 258 HOH   HOH A . 
P 7 HOH   178 678 175 HOH   HOH A . 
P 7 HOH   179 679 199 HOH   HOH A . 
P 7 HOH   180 680 160 HOH   HOH A . 
P 7 HOH   181 681 523 HOH   HOH A . 
P 7 HOH   182 682 617 HOH   HOH A . 
P 7 HOH   183 683 188 HOH   HOH A . 
P 7 HOH   184 684 347 HOH   HOH A . 
P 7 HOH   185 685 548 HOH   HOH A . 
P 7 HOH   186 686 51  HOH   HOH A . 
P 7 HOH   187 687 644 HOH   HOH A . 
P 7 HOH   188 688 444 HOH   HOH A . 
P 7 HOH   189 689 243 HOH   HOH A . 
P 7 HOH   190 690 222 HOH   HOH A . 
P 7 HOH   191 691 399 HOH   HOH A . 
P 7 HOH   192 692 107 HOH   HOH A . 
P 7 HOH   193 693 58  HOH   HOH A . 
P 7 HOH   194 694 171 HOH   HOH A . 
P 7 HOH   195 695 363 HOH   HOH A . 
P 7 HOH   196 696 628 HOH   HOH A . 
P 7 HOH   197 697 559 HOH   HOH A . 
P 7 HOH   198 698 122 HOH   HOH A . 
P 7 HOH   199 699 264 HOH   HOH A . 
P 7 HOH   200 700 179 HOH   HOH A . 
P 7 HOH   201 701 395 HOH   HOH A . 
P 7 HOH   202 702 494 HOH   HOH A . 
P 7 HOH   203 703 132 HOH   HOH A . 
P 7 HOH   204 704 549 HOH   HOH A . 
P 7 HOH   205 705 45  HOH   HOH A . 
P 7 HOH   206 706 567 HOH   HOH A . 
P 7 HOH   207 707 54  HOH   HOH A . 
P 7 HOH   208 708 384 HOH   HOH A . 
P 7 HOH   209 709 41  HOH   HOH A . 
P 7 HOH   210 710 240 HOH   HOH A . 
P 7 HOH   211 711 400 HOH   HOH A . 
P 7 HOH   212 712 129 HOH   HOH A . 
P 7 HOH   213 713 331 HOH   HOH A . 
P 7 HOH   214 714 511 HOH   HOH A . 
P 7 HOH   215 715 272 HOH   HOH A . 
P 7 HOH   216 716 611 HOH   HOH A . 
P 7 HOH   217 717 334 HOH   HOH A . 
P 7 HOH   218 718 190 HOH   HOH A . 
P 7 HOH   219 719 391 HOH   HOH A . 
P 7 HOH   220 720 575 HOH   HOH A . 
P 7 HOH   221 721 530 HOH   HOH A . 
P 7 HOH   222 722 206 HOH   HOH A . 
P 7 HOH   223 723 608 HOH   HOH A . 
P 7 HOH   224 724 87  HOH   HOH A . 
P 7 HOH   225 725 309 HOH   HOH A . 
P 7 HOH   226 726 430 HOH   HOH A . 
P 7 HOH   227 727 615 HOH   HOH A . 
P 7 HOH   228 728 601 HOH   HOH A . 
P 7 HOH   229 729 410 HOH   HOH A . 
P 7 HOH   230 730 626 HOH   HOH A . 
P 7 HOH   231 731 282 HOH   HOH A . 
P 7 HOH   232 732 178 HOH   HOH A . 
P 7 HOH   233 733 458 HOH   HOH A . 
P 7 HOH   234 734 596 HOH   HOH A . 
P 7 HOH   235 735 338 HOH   HOH A . 
P 7 HOH   236 736 208 HOH   HOH A . 
P 7 HOH   237 737 453 HOH   HOH A . 
P 7 HOH   238 738 499 HOH   HOH A . 
P 7 HOH   239 739 637 HOH   HOH A . 
P 7 HOH   240 740 396 HOH   HOH A . 
P 7 HOH   241 741 257 HOH   HOH A . 
P 7 HOH   242 742 278 HOH   HOH A . 
P 7 HOH   243 743 181 HOH   HOH A . 
P 7 HOH   244 744 368 HOH   HOH A . 
P 7 HOH   245 745 367 HOH   HOH A . 
P 7 HOH   246 746 320 HOH   HOH A . 
P 7 HOH   247 747 493 HOH   HOH A . 
P 7 HOH   248 748 357 HOH   HOH A . 
P 7 HOH   249 749 558 HOH   HOH A . 
P 7 HOH   250 750 495 HOH   HOH A . 
P 7 HOH   251 751 635 HOH   HOH A . 
P 7 HOH   252 752 557 HOH   HOH A . 
P 7 HOH   253 753 281 HOH   HOH A . 
P 7 HOH   254 754 350 HOH   HOH A . 
P 7 HOH   255 755 378 HOH   HOH A . 
P 7 HOH   256 756 185 HOH   HOH A . 
P 7 HOH   257 757 566 HOH   HOH A . 
P 7 HOH   258 758 348 HOH   HOH A . 
P 7 HOH   259 759 619 HOH   HOH A . 
P 7 HOH   260 760 192 HOH   HOH A . 
P 7 HOH   261 761 377 HOH   HOH A . 
P 7 HOH   262 762 382 HOH   HOH A . 
P 7 HOH   263 763 505 HOH   HOH A . 
P 7 HOH   264 764 321 HOH   HOH A . 
P 7 HOH   265 765 106 HOH   HOH A . 
P 7 HOH   266 766 214 HOH   HOH A . 
P 7 HOH   267 767 404 HOH   HOH A . 
P 7 HOH   268 768 150 HOH   HOH A . 
P 7 HOH   269 769 535 HOH   HOH A . 
P 7 HOH   270 770 413 HOH   HOH A . 
P 7 HOH   271 771 359 HOH   HOH A . 
P 7 HOH   272 772 522 HOH   HOH A . 
P 7 HOH   273 773 172 HOH   HOH A . 
P 7 HOH   274 774 569 HOH   HOH A . 
P 7 HOH   275 775 543 HOH   HOH A . 
P 7 HOH   276 776 565 HOH   HOH A . 
P 7 HOH   277 777 335 HOH   HOH A . 
P 7 HOH   278 778 445 HOH   HOH A . 
P 7 HOH   279 779 479 HOH   HOH A . 
P 7 HOH   280 780 638 HOH   HOH A . 
P 7 HOH   281 781 501 HOH   HOH A . 
P 7 HOH   282 782 365 HOH   HOH A . 
P 7 HOH   283 783 103 HOH   HOH A . 
P 7 HOH   284 784 609 HOH   HOH A . 
P 7 HOH   285 785 130 HOH   HOH A . 
P 7 HOH   286 786 136 HOH   HOH A . 
P 7 HOH   287 787 412 HOH   HOH A . 
P 7 HOH   288 788 358 HOH   HOH A . 
P 7 HOH   289 789 438 HOH   HOH A . 
P 7 HOH   290 790 496 HOH   HOH A . 
P 7 HOH   291 791 439 HOH   HOH A . 
P 7 HOH   292 792 432 HOH   HOH A . 
P 7 HOH   293 793 213 HOH   HOH A . 
P 7 HOH   294 794 572 HOH   HOH A . 
P 7 HOH   295 795 409 HOH   HOH A . 
P 7 HOH   296 796 590 HOH   HOH A . 
P 7 HOH   297 797 515 HOH   HOH A . 
P 7 HOH   298 798 167 HOH   HOH A . 
P 7 HOH   299 799 405 HOH   HOH A . 
P 7 HOH   300 800 427 HOH   HOH A . 
P 7 HOH   301 801 131 HOH   HOH A . 
P 7 HOH   302 802 589 HOH   HOH A . 
P 7 HOH   303 803 99  HOH   HOH A . 
P 7 HOH   304 804 591 HOH   HOH A . 
P 7 HOH   305 805 592 HOH   HOH A . 
P 7 HOH   306 806 527 HOH   HOH A . 
P 7 HOH   307 807 385 HOH   HOH A . 
P 7 HOH   308 808 482 HOH   HOH A . 
P 7 HOH   309 809 406 HOH   HOH A . 
P 7 HOH   310 810 595 HOH   HOH A . 
P 7 HOH   311 811 636 HOH   HOH A . 
P 7 HOH   312 812 418 HOH   HOH A . 
P 7 HOH   313 813 623 HOH   HOH A . 
P 7 HOH   314 814 600 HOH   HOH A . 
P 7 HOH   315 815 536 HOH   HOH A . 
P 7 HOH   316 816 593 HOH   HOH A . 
P 7 HOH   317 817 586 HOH   HOH A . 
P 7 HOH   318 818 598 HOH   HOH A . 
P 7 HOH   319 819 528 HOH   HOH A . 
P 7 HOH   320 820 461 HOH   HOH A . 
Q 7 HOH   1   501 313 HOH   HOH B . 
Q 7 HOH   2   502 30  HOH   HOH B . 
Q 7 HOH   3   503 622 HOH   HOH B . 
Q 7 HOH   4   504 202 HOH   HOH B . 
Q 7 HOH   5   505 228 HOH   HOH B . 
Q 7 HOH   6   506 642 HOH   HOH B . 
Q 7 HOH   7   507 633 HOH   HOH B . 
Q 7 HOH   8   508 383 HOH   HOH B . 
Q 7 HOH   9   509 580 HOH   HOH B . 
Q 7 HOH   10  510 147 HOH   HOH B . 
Q 7 HOH   11  511 415 HOH   HOH B . 
Q 7 HOH   12  512 343 HOH   HOH B . 
Q 7 HOH   13  513 82  HOH   HOH B . 
Q 7 HOH   14  514 105 HOH   HOH B . 
Q 7 HOH   15  515 193 HOH   HOH B . 
Q 7 HOH   16  516 153 HOH   HOH B . 
Q 7 HOH   17  517 15  HOH   HOH B . 
Q 7 HOH   18  518 462 HOH   HOH B . 
Q 7 HOH   19  519 473 HOH   HOH B . 
Q 7 HOH   20  520 386 HOH   HOH B . 
Q 7 HOH   21  521 123 HOH   HOH B . 
Q 7 HOH   22  522 201 HOH   HOH B . 
Q 7 HOH   23  523 295 HOH   HOH B . 
Q 7 HOH   24  524 471 HOH   HOH B . 
Q 7 HOH   25  525 306 HOH   HOH B . 
Q 7 HOH   26  526 239 HOH   HOH B . 
Q 7 HOH   27  527 109 HOH   HOH B . 
Q 7 HOH   28  528 233 HOH   HOH B . 
Q 7 HOH   29  529 210 HOH   HOH B . 
Q 7 HOH   30  530 317 HOH   HOH B . 
Q 7 HOH   31  531 344 HOH   HOH B . 
Q 7 HOH   32  532 108 HOH   HOH B . 
Q 7 HOH   33  533 578 HOH   HOH B . 
Q 7 HOH   34  534 316 HOH   HOH B . 
Q 7 HOH   35  535 468 HOH   HOH B . 
Q 7 HOH   36  536 408 HOH   HOH B . 
Q 7 HOH   37  537 65  HOH   HOH B . 
Q 7 HOH   38  538 381 HOH   HOH B . 
Q 7 HOH   39  539 27  HOH   HOH B . 
Q 7 HOH   40  540 134 HOH   HOH B . 
Q 7 HOH   41  541 366 HOH   HOH B . 
Q 7 HOH   42  542 14  HOH   HOH B . 
Q 7 HOH   43  543 394 HOH   HOH B . 
Q 7 HOH   44  544 286 HOH   HOH B . 
Q 7 HOH   45  545 219 HOH   HOH B . 
Q 7 HOH   46  546 203 HOH   HOH B . 
Q 7 HOH   47  547 194 HOH   HOH B . 
Q 7 HOH   48  548 613 HOH   HOH B . 
Q 7 HOH   49  549 72  HOH   HOH B . 
Q 7 HOH   50  550 392 HOH   HOH B . 
Q 7 HOH   51  551 145 HOH   HOH B . 
Q 7 HOH   52  552 114 HOH   HOH B . 
Q 7 HOH   53  553 17  HOH   HOH B . 
Q 7 HOH   54  554 146 HOH   HOH B . 
Q 7 HOH   55  555 441 HOH   HOH B . 
Q 7 HOH   56  556 101 HOH   HOH B . 
Q 7 HOH   57  557 163 HOH   HOH B . 
Q 7 HOH   58  558 80  HOH   HOH B . 
Q 7 HOH   59  559 301 HOH   HOH B . 
Q 7 HOH   60  560 36  HOH   HOH B . 
Q 7 HOH   61  561 244 HOH   HOH B . 
Q 7 HOH   62  562 48  HOH   HOH B . 
Q 7 HOH   63  563 349 HOH   HOH B . 
Q 7 HOH   64  564 189 HOH   HOH B . 
Q 7 HOH   65  565 520 HOH   HOH B . 
Q 7 HOH   66  566 259 HOH   HOH B . 
Q 7 HOH   67  567 271 HOH   HOH B . 
Q 7 HOH   68  568 183 HOH   HOH B . 
Q 7 HOH   69  569 310 HOH   HOH B . 
Q 7 HOH   70  570 229 HOH   HOH B . 
Q 7 HOH   71  571 113 HOH   HOH B . 
Q 7 HOH   72  572 89  HOH   HOH B . 
Q 7 HOH   73  573 7   HOH   HOH B . 
Q 7 HOH   74  574 20  HOH   HOH B . 
Q 7 HOH   75  575 18  HOH   HOH B . 
Q 7 HOH   76  576 165 HOH   HOH B . 
Q 7 HOH   77  577 524 HOH   HOH B . 
Q 7 HOH   78  578 248 HOH   HOH B . 
Q 7 HOH   79  579 207 HOH   HOH B . 
Q 7 HOH   80  580 507 HOH   HOH B . 
Q 7 HOH   81  581 464 HOH   HOH B . 
Q 7 HOH   82  582 180 HOH   HOH B . 
Q 7 HOH   83  583 435 HOH   HOH B . 
Q 7 HOH   84  584 24  HOH   HOH B . 
Q 7 HOH   85  585 466 HOH   HOH B . 
Q 7 HOH   86  586 85  HOH   HOH B . 
Q 7 HOH   87  587 451 HOH   HOH B . 
Q 7 HOH   88  588 13  HOH   HOH B . 
Q 7 HOH   89  589 237 HOH   HOH B . 
Q 7 HOH   90  590 351 HOH   HOH B . 
Q 7 HOH   91  591 285 HOH   HOH B . 
Q 7 HOH   92  592 155 HOH   HOH B . 
Q 7 HOH   93  593 38  HOH   HOH B . 
Q 7 HOH   94  594 47  HOH   HOH B . 
Q 7 HOH   95  595 86  HOH   HOH B . 
Q 7 HOH   96  596 411 HOH   HOH B . 
Q 7 HOH   97  597 469 HOH   HOH B . 
Q 7 HOH   98  598 289 HOH   HOH B . 
Q 7 HOH   99  599 9   HOH   HOH B . 
Q 7 HOH   100 600 483 HOH   HOH B . 
Q 7 HOH   101 601 380 HOH   HOH B . 
Q 7 HOH   102 602 307 HOH   HOH B . 
Q 7 HOH   103 603 125 HOH   HOH B . 
Q 7 HOH   104 604 46  HOH   HOH B . 
Q 7 HOH   105 605 94  HOH   HOH B . 
Q 7 HOH   106 606 509 HOH   HOH B . 
Q 7 HOH   107 607 324 HOH   HOH B . 
Q 7 HOH   108 608 191 HOH   HOH B . 
Q 7 HOH   109 609 266 HOH   HOH B . 
Q 7 HOH   110 610 39  HOH   HOH B . 
Q 7 HOH   111 611 311 HOH   HOH B . 
Q 7 HOH   112 612 393 HOH   HOH B . 
Q 7 HOH   113 613 606 HOH   HOH B . 
Q 7 HOH   114 614 6   HOH   HOH B . 
Q 7 HOH   115 615 118 HOH   HOH B . 
Q 7 HOH   116 616 247 HOH   HOH B . 
Q 7 HOH   117 617 476 HOH   HOH B . 
Q 7 HOH   118 618 563 HOH   HOH B . 
Q 7 HOH   119 619 425 HOH   HOH B . 
Q 7 HOH   120 620 40  HOH   HOH B . 
Q 7 HOH   121 621 481 HOH   HOH B . 
Q 7 HOH   122 622 226 HOH   HOH B . 
Q 7 HOH   123 623 280 HOH   HOH B . 
Q 7 HOH   124 624 26  HOH   HOH B . 
Q 7 HOH   125 625 197 HOH   HOH B . 
Q 7 HOH   126 626 19  HOH   HOH B . 
Q 7 HOH   127 627 364 HOH   HOH B . 
Q 7 HOH   128 628 63  HOH   HOH B . 
Q 7 HOH   129 629 200 HOH   HOH B . 
Q 7 HOH   130 630 59  HOH   HOH B . 
Q 7 HOH   131 631 184 HOH   HOH B . 
Q 7 HOH   132 632 70  HOH   HOH B . 
Q 7 HOH   133 633 227 HOH   HOH B . 
Q 7 HOH   134 634 446 HOH   HOH B . 
Q 7 HOH   135 635 337 HOH   HOH B . 
Q 7 HOH   136 636 298 HOH   HOH B . 
Q 7 HOH   137 637 250 HOH   HOH B . 
Q 7 HOH   138 638 375 HOH   HOH B . 
Q 7 HOH   139 639 327 HOH   HOH B . 
Q 7 HOH   140 640 159 HOH   HOH B . 
Q 7 HOH   141 641 352 HOH   HOH B . 
Q 7 HOH   142 642 372 HOH   HOH B . 
Q 7 HOH   143 643 336 HOH   HOH B . 
Q 7 HOH   144 644 290 HOH   HOH B . 
Q 7 HOH   145 645 196 HOH   HOH B . 
Q 7 HOH   146 646 292 HOH   HOH B . 
Q 7 HOH   147 647 545 HOH   HOH B . 
Q 7 HOH   148 648 224 HOH   HOH B . 
Q 7 HOH   149 649 104 HOH   HOH B . 
Q 7 HOH   150 650 32  HOH   HOH B . 
Q 7 HOH   151 651 5   HOH   HOH B . 
Q 7 HOH   152 652 157 HOH   HOH B . 
Q 7 HOH   153 653 198 HOH   HOH B . 
Q 7 HOH   154 654 274 HOH   HOH B . 
Q 7 HOH   155 655 158 HOH   HOH B . 
Q 7 HOH   156 656 16  HOH   HOH B . 
Q 7 HOH   157 657 115 HOH   HOH B . 
Q 7 HOH   158 658 454 HOH   HOH B . 
Q 7 HOH   159 659 328 HOH   HOH B . 
Q 7 HOH   160 660 571 HOH   HOH B . 
Q 7 HOH   161 661 500 HOH   HOH B . 
Q 7 HOH   162 662 236 HOH   HOH B . 
Q 7 HOH   163 663 42  HOH   HOH B . 
Q 7 HOH   164 664 433 HOH   HOH B . 
Q 7 HOH   165 665 614 HOH   HOH B . 
Q 7 HOH   166 666 262 HOH   HOH B . 
Q 7 HOH   167 667 148 HOH   HOH B . 
Q 7 HOH   168 668 303 HOH   HOH B . 
Q 7 HOH   169 669 56  HOH   HOH B . 
Q 7 HOH   170 670 128 HOH   HOH B . 
Q 7 HOH   171 671 168 HOH   HOH B . 
Q 7 HOH   172 672 95  HOH   HOH B . 
Q 7 HOH   173 673 284 HOH   HOH B . 
Q 7 HOH   174 674 570 HOH   HOH B . 
Q 7 HOH   175 675 643 HOH   HOH B . 
Q 7 HOH   176 676 283 HOH   HOH B . 
Q 7 HOH   177 677 230 HOH   HOH B . 
Q 7 HOH   178 678 315 HOH   HOH B . 
Q 7 HOH   179 679 253 HOH   HOH B . 
Q 7 HOH   180 680 164 HOH   HOH B . 
Q 7 HOH   181 681 329 HOH   HOH B . 
Q 7 HOH   182 682 33  HOH   HOH B . 
Q 7 HOH   183 683 29  HOH   HOH B . 
Q 7 HOH   184 684 436 HOH   HOH B . 
Q 7 HOH   185 685 176 HOH   HOH B . 
Q 7 HOH   186 686 514 HOH   HOH B . 
Q 7 HOH   187 687 126 HOH   HOH B . 
Q 7 HOH   188 688 556 HOH   HOH B . 
Q 7 HOH   189 689 452 HOH   HOH B . 
Q 7 HOH   190 690 602 HOH   HOH B . 
Q 7 HOH   191 691 111 HOH   HOH B . 
Q 7 HOH   192 692 305 HOH   HOH B . 
Q 7 HOH   193 693 333 HOH   HOH B . 
Q 7 HOH   194 694 238 HOH   HOH B . 
Q 7 HOH   195 695 152 HOH   HOH B . 
Q 7 HOH   196 696 345 HOH   HOH B . 
Q 7 HOH   197 697 212 HOH   HOH B . 
Q 7 HOH   198 698 91  HOH   HOH B . 
Q 7 HOH   199 699 420 HOH   HOH B . 
Q 7 HOH   200 700 371 HOH   HOH B . 
Q 7 HOH   201 701 100 HOH   HOH B . 
Q 7 HOH   202 702 554 HOH   HOH B . 
Q 7 HOH   203 703 261 HOH   HOH B . 
Q 7 HOH   204 704 374 HOH   HOH B . 
Q 7 HOH   205 705 205 HOH   HOH B . 
Q 7 HOH   206 706 154 HOH   HOH B . 
Q 7 HOH   207 707 490 HOH   HOH B . 
Q 7 HOH   208 708 544 HOH   HOH B . 
Q 7 HOH   209 709 518 HOH   HOH B . 
Q 7 HOH   210 710 599 HOH   HOH B . 
Q 7 HOH   211 711 489 HOH   HOH B . 
Q 7 HOH   212 712 561 HOH   HOH B . 
Q 7 HOH   213 713 268 HOH   HOH B . 
Q 7 HOH   214 714 492 HOH   HOH B . 
Q 7 HOH   215 715 169 HOH   HOH B . 
Q 7 HOH   216 716 579 HOH   HOH B . 
Q 7 HOH   217 717 497 HOH   HOH B . 
Q 7 HOH   218 718 486 HOH   HOH B . 
Q 7 HOH   219 719 576 HOH   HOH B . 
Q 7 HOH   220 720 332 HOH   HOH B . 
Q 7 HOH   221 721 470 HOH   HOH B . 
Q 7 HOH   222 722 209 HOH   HOH B . 
Q 7 HOH   223 723 517 HOH   HOH B . 
Q 7 HOH   224 724 429 HOH   HOH B . 
Q 7 HOH   225 725 256 HOH   HOH B . 
Q 7 HOH   226 726 402 HOH   HOH B . 
Q 7 HOH   227 727 506 HOH   HOH B . 
Q 7 HOH   228 728 342 HOH   HOH B . 
Q 7 HOH   229 729 416 HOH   HOH B . 
Q 7 HOH   230 730 605 HOH   HOH B . 
Q 7 HOH   231 731 397 HOH   HOH B . 
Q 7 HOH   232 732 60  HOH   HOH B . 
Q 7 HOH   233 733 632 HOH   HOH B . 
Q 7 HOH   234 734 547 HOH   HOH B . 
Q 7 HOH   235 735 431 HOH   HOH B . 
Q 7 HOH   236 736 450 HOH   HOH B . 
Q 7 HOH   237 737 448 HOH   HOH B . 
Q 7 HOH   238 738 582 HOH   HOH B . 
Q 7 HOH   239 739 508 HOH   HOH B . 
Q 7 HOH   240 740 340 HOH   HOH B . 
Q 7 HOH   241 741 502 HOH   HOH B . 
Q 7 HOH   242 742 120 HOH   HOH B . 
Q 7 HOH   243 743 630 HOH   HOH B . 
Q 7 HOH   244 744 447 HOH   HOH B . 
Q 7 HOH   245 745 550 HOH   HOH B . 
Q 7 HOH   246 746 90  HOH   HOH B . 
Q 7 HOH   247 747 215 HOH   HOH B . 
Q 7 HOH   248 748 330 HOH   HOH B . 
Q 7 HOH   249 749 319 HOH   HOH B . 
Q 7 HOH   250 750 478 HOH   HOH B . 
Q 7 HOH   251 751 211 HOH   HOH B . 
Q 7 HOH   252 752 485 HOH   HOH B . 
Q 7 HOH   253 753 121 HOH   HOH B . 
Q 7 HOH   254 754 318 HOH   HOH B . 
Q 7 HOH   255 755 583 HOH   HOH B . 
Q 7 HOH   256 756 110 HOH   HOH B . 
Q 7 HOH   257 757 421 HOH   HOH B . 
Q 7 HOH   258 758 480 HOH   HOH B . 
Q 7 HOH   259 759 627 HOH   HOH B . 
Q 7 HOH   260 760 57  HOH   HOH B . 
Q 7 HOH   261 761 442 HOH   HOH B . 
Q 7 HOH   262 762 526 HOH   HOH B . 
Q 7 HOH   263 763 555 HOH   HOH B . 
Q 7 HOH   264 764 597 HOH   HOH B . 
Q 7 HOH   265 765 537 HOH   HOH B . 
Q 7 HOH   266 766 477 HOH   HOH B . 
Q 7 HOH   267 767 529 HOH   HOH B . 
Q 7 HOH   268 768 270 HOH   HOH B . 
Q 7 HOH   269 769 585 HOH   HOH B . 
Q 7 HOH   270 770 588 HOH   HOH B . 
Q 7 HOH   271 771 398 HOH   HOH B . 
Q 7 HOH   272 772 459 HOH   HOH B . 
Q 7 HOH   273 773 618 HOH   HOH B . 
Q 7 HOH   274 774 551 HOH   HOH B . 
Q 7 HOH   275 775 474 HOH   HOH B . 
Q 7 HOH   276 776 620 HOH   HOH B . 
Q 7 HOH   277 777 584 HOH   HOH B . 
Q 7 HOH   278 778 504 HOH   HOH B . 
Q 7 HOH   279 779 401 HOH   HOH B . 
Q 7 HOH   280 780 21  HOH   HOH B . 
Q 7 HOH   281 781 403 HOH   HOH B . 
Q 7 HOH   282 782 640 HOH   HOH B . 
Q 7 HOH   283 783 388 HOH   HOH B . 
Q 7 HOH   284 784 546 HOH   HOH B . 
Q 7 HOH   285 785 577 HOH   HOH B . 
Q 7 HOH   286 786 512 HOH   HOH B . 
Q 7 HOH   287 787 443 HOH   HOH B . 
Q 7 HOH   288 788 604 HOH   HOH B . 
Q 7 HOH   289 789 634 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.122 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z2J 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.560 
_cell.length_a_esd                 ? 
_cell.length_b                     78.840 
_cell.length_b_esd                 ? 
_cell.length_c                     74.250 
_cell.length_c_esd                 ? 
_cell.volume                       233718.999 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z2J 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z2J 
_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             2.05 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.94 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.2 M NaCl, 0.1 M Sodium acetate trihydrate pH 4.6, 30% (v/v) 2-Methyl-2,4-pentanediol, and 2 mM ligand' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_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                        'SPRING-8 BEAMLINE BL32XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL32XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          13.33 
_reflns.entry_id                                       8Z2J 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.89 
_reflns.d_resolution_low                               40 
_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                                     36906 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.6 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.983 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.445 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.89 
_reflns_shell.d_res_low                                     2.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5712 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.582 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               2 
_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                               14.73 
_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                                 8Z2J 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.89 
_refine.ls_d_res_low                             39.93 
_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                     36877 
_refine.ls_number_reflns_R_free                  1853 
_refine.ls_number_reflns_R_work                  35024 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1618 
_refine.ls_R_factor_R_free                       0.2074 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1594 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_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                      7CTS 
_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             1.1100 
_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                 20.1047 
_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                            0.2123 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.89 
_refine_hist.d_res_low                        39.93 
_refine_hist.number_atoms_solvent             609 
_refine_hist.number_atoms_total               4700 
_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        4012 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         79 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0067  ? 4203 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8610  ? 5727 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0538  ? 611  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0089  ? 750  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.5123 ? 1559 ? 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.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.89 1.94  . . 143 2665 99.82  . . . . 0.2202 . . . . . . . . . . . 0.2655 
'X-RAY DIFFRACTION' 1.94 2.00  . . 139 2673 100.00 . . . . 0.2167 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 2.00 2.06  . . 139 2701 99.96  . . . . 0.2035 . . . . . . . . . . . 0.2738 
'X-RAY DIFFRACTION' 2.06 2.14  . . 143 2672 100.00 . . . . 0.1929 . . . . . . . . . . . 0.2900 
'X-RAY DIFFRACTION' 2.14 2.22  . . 139 2675 100.00 . . . . 0.1808 . . . . . . . . . . . 0.2382 
'X-RAY DIFFRACTION' 2.22 2.32  . . 142 2711 100.00 . . . . 0.1684 . . . . . . . . . . . 0.2042 
'X-RAY DIFFRACTION' 2.32 2.45  . . 141 2681 100.00 . . . . 0.1606 . . . . . . . . . . . 0.2056 
'X-RAY DIFFRACTION' 2.45 2.60  . . 140 2695 99.96  . . . . 0.1569 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.60 2.80  . . 146 2699 100.00 . . . . 0.1559 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 2.80 3.08  . . 142 2689 99.96  . . . . 0.1501 . . . . . . . . . . . 0.2175 
'X-RAY DIFFRACTION' 3.08 3.53  . . 148 2709 99.97  . . . . 0.1346 . . . . . . . . . . . 0.1613 
'X-RAY DIFFRACTION' 3.53 4.44  . . 142 2694 100.00 . . . . 0.1165 . . . . . . . . . . . 0.1525 
'X-RAY DIFFRACTION' 4.44 39.93 . . 149 2760 99.62  . . . . 0.1552 . . . . . . . . . . . 0.2043 
# 
_struct.entry_id                     8Z2J 
_struct.title                        'Substrate analog a012 bound form of PET-degrading cutinase mutant Cut190**SS_S176A' 
_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        8Z2J 
_struct_keywords.text            'PROTEIN ENGINEERING, POLYESTERASE, METAL BINDING, Aromatic ligand, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 2 ? 
I N N 6 ? 
J N N 6 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P N N 7 ? 
Q N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    W0TJ64_9PSEU 
_struct_ref.pdbx_db_accession          W0TJ64 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NPYERGPDPTEDSIEAIRGPFSVATERVSSFASGFGGGTIYYPRETDEGTFGAVAVAPGFTASQGSMSWYGERVASQGFI
VFTIDTNTRLDQPGQRGRQLLAALDYLVERSDRKVRERLDPNRLAVMGHSMGGGGSLEATVMRPSLKASIPLTPWNLDKT
WGQVQVPTFIIGAELDTIASVRTHAKPFYESLPSSLPKAYMELDGATHFAPNIPNTTIAKYVISWLKRFVDEDTRYSQFL
CPNPTDRAIEEYRSTCPY
;
_struct_ref.pdbx_align_begin           47 
# 
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 8Z2J A 3 ? 260 ? W0TJ64 47 ? 304 ? 47 304 
2 1 8Z2J B 3 ? 260 ? W0TJ64 47 ? 304 ? 47 304 
# 
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 8Z2J GLY A 1   ? UNP W0TJ64 ?   ?   'expression tag'      45  1  
1 8Z2J PRO A 2   ? UNP W0TJ64 ?   ?   'expression tag'      46  2  
1 8Z2J HIS A 79  ? UNP W0TJ64 GLN 123 'engineered mutation' 123 3  
1 8Z2J ALA A 94  ? UNP W0TJ64 GLN 138 'engineered mutation' 138 4  
1 8Z2J ALA A 132 ? UNP W0TJ64 SER 176 'engineered mutation' 176 5  
1 8Z2J HIS A 158 ? UNP W0TJ64 ASN 202 'engineered mutation' 202 6  
1 8Z2J PRO A 182 ? UNP W0TJ64 SER 226 'engineered mutation' 226 7  
1 8Z2J SER A 184 ? UNP W0TJ64 ARG 228 'engineered mutation' 228 8  
1 8Z2J CYS A 206 ? UNP W0TJ64 ASP 250 'engineered mutation' 250 9  
1 8Z2J CYS A 252 ? UNP W0TJ64 GLU 296 'engineered mutation' 296 10 
2 8Z2J GLY B 1   ? UNP W0TJ64 ?   ?   'expression tag'      45  11 
2 8Z2J PRO B 2   ? UNP W0TJ64 ?   ?   'expression tag'      46  12 
2 8Z2J HIS B 79  ? UNP W0TJ64 GLN 123 'engineered mutation' 123 13 
2 8Z2J ALA B 94  ? UNP W0TJ64 GLN 138 'engineered mutation' 138 14 
2 8Z2J ALA B 132 ? UNP W0TJ64 SER 176 'engineered mutation' 176 15 
2 8Z2J HIS B 158 ? UNP W0TJ64 ASN 202 'engineered mutation' 202 16 
2 8Z2J PRO B 182 ? UNP W0TJ64 SER 226 'engineered mutation' 226 17 
2 8Z2J SER B 184 ? UNP W0TJ64 ARG 228 'engineered mutation' 228 18 
2 8Z2J CYS B 206 ? UNP W0TJ64 ASP 250 'engineered mutation' 250 19 
2 8Z2J CYS B 252 ? UNP W0TJ64 GLU 296 'engineered mutation' 296 20 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,P       
2 1 B,H,I,J,K,L,M,N,O,Q 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 12  ? ALA A 18  ? THR A 56  ALA A 62  1 ? 7  
HELX_P HELX_P2  AA2 SER A 65  ? MET A 69  ? SER A 109 MET A 113 5 ? 5  
HELX_P HELX_P3  AA3 SER A 70  ? SER A 78  ? SER A 114 SER A 122 1 ? 9  
HELX_P HELX_P4  AA4 ALA A 94  ? ARG A 112 ? ALA A 138 ARG A 156 1 ? 19 
HELX_P HELX_P5  AA5 ASP A 114 ? GLU A 119 ? ASP A 158 GLU A 163 1 ? 6  
HELX_P HELX_P6  AA6 ALA A 132 ? ARG A 145 ? ALA A 176 ARG A 189 1 ? 14 
HELX_P HELX_P7  AA7 HIS A 186 ? LEU A 194 ? HIS A 230 LEU A 238 1 ? 9  
HELX_P HELX_P8  AA8 PHE A 211 ? ILE A 215 ? PHE A 255 ILE A 259 5 ? 5  
HELX_P HELX_P9  AA9 ASN A 217 ? ASP A 233 ? ASN A 261 ASP A 277 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 235 ? ARG A 237 ? ASP A 279 ARG A 281 5 ? 3  
HELX_P HELX_P11 AB2 TYR A 238 ? CYS A 243 ? TYR A 282 CYS A 287 1 ? 6  
HELX_P HELX_P12 AB3 THR B 12  ? ALA B 18  ? THR B 56  ALA B 62  1 ? 7  
HELX_P HELX_P13 AB4 SER B 65  ? SER B 70  ? SER B 109 SER B 114 5 ? 6  
HELX_P HELX_P14 AB5 TRP B 71  ? SER B 78  ? TRP B 115 SER B 122 1 ? 8  
HELX_P HELX_P15 AB6 ALA B 94  ? ARG B 112 ? ALA B 138 ARG B 156 1 ? 19 
HELX_P HELX_P16 AB7 ASP B 114 ? GLU B 119 ? ASP B 158 GLU B 163 1 ? 6  
HELX_P HELX_P17 AB8 ALA B 132 ? ARG B 145 ? ALA B 176 ARG B 189 1 ? 14 
HELX_P HELX_P18 AB9 HIS B 186 ? LEU B 194 ? HIS B 230 LEU B 238 1 ? 9  
HELX_P HELX_P19 AC1 PHE B 211 ? ILE B 215 ? PHE B 255 ILE B 259 5 ? 5  
HELX_P HELX_P20 AC2 ASN B 217 ? ASP B 233 ? ASN B 261 ASP B 277 1 ? 17 
HELX_P HELX_P21 AC3 ASP B 235 ? ARG B 237 ? ASP B 279 ARG B 281 5 ? 3  
HELX_P HELX_P22 AC4 TYR B 238 ? CYS B 243 ? TYR B 282 CYS B 287 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 206 SG ? ? ? 1_555 A CYS 252 SG ? ? A CYS 250 A CYS 296 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
disulf2  disulf ? ? A CYS 243 SG ? ? ? 1_555 A CYS 258 SG ? ? A CYS 287 A CYS 302 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf3  disulf ? ? B CYS 206 SG ? ? ? 1_555 B CYS 252 SG ? ? B CYS 250 B CYS 296 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf4  disulf ? ? B CYS 243 SG ? ? ? 1_555 B CYS 258 SG ? ? B CYS 287 B CYS 302 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc1  metalc ? ? A SER 32  O  ? ? ? 1_555 E CA  .   CA ? ? A SER 76  A CA  403 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc2  metalc ? ? A ALA 34  O  ? ? ? 1_555 E CA  .   CA ? ? A ALA 78  A CA  403 1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc3  metalc ? ? A PHE 37  O  ? ? ? 1_555 E CA  .   CA ? ? A PHE 81  A CA  403 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc4  metalc ? ? A TYR 254 O  ? ? ? 1_555 F CA  .   CA ? ? A TYR 298 A CA  404 1_555 ? ? ? ? ? ? ? 2.413 ? ? 
metalc5  metalc ? ? E CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  403 A HOH 594 1_555 ? ? ? ? ? ? ? 2.524 ? ? 
metalc6  metalc ? ? E CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  403 A HOH 692 1_555 ? ? ? ? ? ? ? 2.407 ? ? 
metalc7  metalc ? ? E CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  403 A HOH 746 1_555 ? ? ? ? ? ? ? 2.462 ? ? 
metalc8  metalc ? ? F CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  404 A HOH 652 1_555 ? ? ? ? ? ? ? 2.491 ? ? 
metalc9  metalc ? ? F CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  404 A HOH 677 1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc10 metalc ? ? F CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  404 A HOH 686 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc11 metalc ? ? F CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  404 A HOH 744 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc12 metalc ? ? F CA  .   CA ? ? ? 1_555 P HOH .   O  ? ? A CA  404 A HOH 805 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc13 metalc ? ? B SER 32  O  ? ? ? 1_555 L CA  .   CA ? ? B SER 76  B CA  405 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc14 metalc ? ? B ALA 34  O  ? ? ? 1_555 L CA  .   CA ? ? B ALA 78  B CA  405 1_555 ? ? ? ? ? ? ? 2.448 ? ? 
metalc15 metalc ? ? B PHE 37  O  ? ? ? 1_555 L CA  .   CA ? ? B PHE 81  B CA  405 1_555 ? ? ? ? ? ? ? 2.433 ? ? 
metalc16 metalc ? ? B TYR 254 O  ? ? ? 1_555 M CA  .   CA ? ? B TYR 298 B CA  406 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc17 metalc ? ? L CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  405 B HOH 581 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc18 metalc ? ? L CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  405 B HOH 703 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc19 metalc ? ? L CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  405 B HOH 728 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc20 metalc ? ? M CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  406 B HOH 558 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc21 metalc ? ? M CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  406 B HOH 605 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc22 metalc ? ? M CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  406 B HOH 659 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
metalc23 metalc ? ? M CA  .   CA ? ? ? 1_555 Q HOH .   O  ? ? B CA  406 B HOH 781 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? A SER 32  ? A SER 76  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A ALA 34 ? A ALA 78  ? 1_555 98.8  ? 
2  O ? A SER 32  ? A SER 76  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A PHE 37 ? A PHE 81  ? 1_555 108.7 ? 
3  O ? A ALA 34  ? A ALA 78  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A PHE 37 ? A PHE 81  ? 1_555 81.0  ? 
4  O ? A SER 32  ? A SER 76  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 594 ? 1_555 168.5 ? 
5  O ? A ALA 34  ? A ALA 78  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 594 ? 1_555 88.2  ? 
6  O ? A PHE 37  ? A PHE 81  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 594 ? 1_555 81.2  ? 
7  O ? A SER 32  ? A SER 76  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 692 ? 1_555 89.5  ? 
8  O ? A ALA 34  ? A ALA 78  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 692 ? 1_555 166.9 ? 
9  O ? A PHE 37  ? A PHE 81  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 692 ? 1_555 86.7  ? 
10 O ? P HOH .   ? A HOH 594 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 692 ? 1_555 85.4  ? 
11 O ? A SER 32  ? A SER 76  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 746 ? 1_555 91.5  ? 
12 O ? A ALA 34  ? A ALA 78  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 746 ? 1_555 99.1  ? 
13 O ? A PHE 37  ? A PHE 81  ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 746 ? 1_555 159.6 ? 
14 O ? P HOH .   ? A HOH 594 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 746 ? 1_555 78.4  ? 
15 O ? P HOH .   ? A HOH 692 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? P HOH .  ? A HOH 746 ? 1_555 90.8  ? 
16 O ? A TYR 254 ? A TYR 298 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 652 ? 1_555 86.7  ? 
17 O ? A TYR 254 ? A TYR 298 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 677 ? 1_555 87.6  ? 
18 O ? P HOH .   ? A HOH 652 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 677 ? 1_555 174.3 ? 
19 O ? A TYR 254 ? A TYR 298 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 686 ? 1_555 86.1  ? 
20 O ? P HOH .   ? A HOH 652 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 686 ? 1_555 96.6  ? 
21 O ? P HOH .   ? A HOH 677 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 686 ? 1_555 82.8  ? 
22 O ? A TYR 254 ? A TYR 298 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 744 ? 1_555 90.1  ? 
23 O ? P HOH .   ? A HOH 652 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 744 ? 1_555 91.8  ? 
24 O ? P HOH .   ? A HOH 677 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 744 ? 1_555 88.4  ? 
25 O ? P HOH .   ? A HOH 686 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 744 ? 1_555 170.5 ? 
26 O ? A TYR 254 ? A TYR 298 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 805 ? 1_555 176.5 ? 
27 O ? P HOH .   ? A HOH 652 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 805 ? 1_555 92.5  ? 
28 O ? P HOH .   ? A HOH 677 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 805 ? 1_555 93.2  ? 
29 O ? P HOH .   ? A HOH 686 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 805 ? 1_555 90.7  ? 
30 O ? P HOH .   ? A HOH 744 ? 1_555 CA ? F CA . ? A CA 404 ? 1_555 O ? P HOH .  ? A HOH 805 ? 1_555 93.3  ? 
31 O ? B SER 32  ? B SER 76  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? B ALA 34 ? B ALA 78  ? 1_555 94.2  ? 
32 O ? B SER 32  ? B SER 76  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? B PHE 37 ? B PHE 81  ? 1_555 100.9 ? 
33 O ? B ALA 34  ? B ALA 78  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? B PHE 37 ? B PHE 81  ? 1_555 77.6  ? 
34 O ? B SER 32  ? B SER 76  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 581 ? 1_555 163.8 ? 
35 O ? B ALA 34  ? B ALA 78  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 581 ? 1_555 99.7  ? 
36 O ? B PHE 37  ? B PHE 81  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 581 ? 1_555 90.1  ? 
37 O ? B SER 32  ? B SER 76  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 703 ? 1_555 92.5  ? 
38 O ? B ALA 34  ? B ALA 78  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 703 ? 1_555 164.3 ? 
39 O ? B PHE 37  ? B PHE 81  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 703 ? 1_555 87.2  ? 
40 O ? Q HOH .   ? B HOH 581 ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 703 ? 1_555 76.1  ? 
41 O ? B SER 32  ? B SER 76  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 728 ? 1_555 93.2  ? 
42 O ? B ALA 34  ? B ALA 78  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 728 ? 1_555 95.5  ? 
43 O ? B PHE 37  ? B PHE 81  ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 728 ? 1_555 164.7 ? 
44 O ? Q HOH .   ? B HOH 581 ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 728 ? 1_555 77.4  ? 
45 O ? Q HOH .   ? B HOH 703 ? 1_555 CA ? L CA . ? B CA 405 ? 1_555 O ? Q HOH .  ? B HOH 728 ? 1_555 98.2  ? 
46 O ? B TYR 254 ? B TYR 298 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 558 ? 1_555 100.4 ? 
47 O ? B TYR 254 ? B TYR 298 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 605 ? 1_555 86.1  ? 
48 O ? Q HOH .   ? B HOH 558 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 605 ? 1_555 171.1 ? 
49 O ? B TYR 254 ? B TYR 298 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 659 ? 1_555 86.8  ? 
50 O ? Q HOH .   ? B HOH 558 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 659 ? 1_555 89.1  ? 
51 O ? Q HOH .   ? B HOH 605 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 659 ? 1_555 85.2  ? 
52 O ? B TYR 254 ? B TYR 298 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 781 ? 1_555 164.0 ? 
53 O ? Q HOH .   ? B HOH 558 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 781 ? 1_555 70.2  ? 
54 O ? Q HOH .   ? B HOH 605 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 781 ? 1_555 102.0 ? 
55 O ? Q HOH .   ? B HOH 659 ? 1_555 CA ? M CA . ? B CA 406 ? 1_555 O ? Q HOH .  ? B HOH 781 ? 1_555 80.2  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 206 ? CYS A 252 ? CYS A 250 ? 1_555 CYS A 296 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 243 ? CYS A 258 ? CYS A 287 ? 1_555 CYS A 302 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 206 ? CYS B 252 ? CYS B 250 ? 1_555 CYS B 296 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 243 ? CYS B 258 ? CYS B 287 ? 1_555 CYS B 302 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 CYS 243 A . ? CYS 287 A PRO 244 A ? PRO 288 A 1 -6.65 
2 CYS 258 A . ? CYS 302 A PRO 259 A ? PRO 303 A 1 3.68  
3 CYS 243 B . ? CYS 287 B PRO 244 B ? PRO 288 B 1 -2.51 
4 CYS 258 B . ? CYS 302 B PRO 259 B ? PRO 303 B 1 1.33  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? 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 VAL A 25  ? VAL A 30  ? VAL A 69  VAL A 74  
AA1 2 GLY A 40  ? PRO A 45  ? GLY A 84  PRO A 89  
AA1 3 ILE A 82  ? ILE A 86  ? ILE A 126 ILE A 130 
AA1 4 PHE A 53  ? ALA A 59  ? PHE A 97  ALA A 103 
AA1 5 LEU A 121 ? HIS A 131 ? LEU A 165 HIS A 175 
AA1 6 ALA A 150 ? LEU A 154 ? ALA A 194 LEU A 198 
AA2 1 THR A 170 ? ALA A 175 ? THR A 214 ALA A 219 
AA2 2 LYS A 200 ? LEU A 205 ? LYS A 244 LEU A 249 
AA2 3 ILE A 251 ? SER A 256 ? ILE A 295 SER A 300 
AA3 1 VAL B 25  ? VAL B 30  ? VAL B 69  VAL B 74  
AA3 2 GLY B 40  ? PRO B 45  ? GLY B 84  PRO B 89  
AA3 3 ILE B 82  ? ILE B 86  ? ILE B 126 ILE B 130 
AA3 4 PHE B 53  ? ALA B 59  ? PHE B 97  ALA B 103 
AA3 5 LEU B 121 ? HIS B 131 ? LEU B 165 HIS B 175 
AA3 6 ALA B 150 ? LEU B 154 ? ALA B 194 LEU B 198 
AA4 1 THR B 170 ? ALA B 175 ? THR B 214 ALA B 219 
AA4 2 LYS B 200 ? LEU B 205 ? LYS B 244 LEU B 249 
AA4 3 ILE B 251 ? SER B 256 ? ILE B 295 SER B 300 
# 
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 VAL A 30  ? N VAL A 74  O GLY A 40  ? O GLY A 84  
AA1 2 3 N TYR A 43  ? N TYR A 87  O VAL A 83  ? O VAL A 127 
AA1 3 4 O PHE A 84  ? O PHE A 128 N VAL A 58  ? N VAL A 102 
AA1 4 5 N PHE A 53  ? N PHE A 97  O ASP A 122 ? O ASP A 166 
AA1 5 6 N GLY A 130 ? N GLY A 174 O LEU A 154 ? O LEU A 198 
AA2 1 2 N GLY A 174 ? N GLY A 218 O MET A 203 ? O MET A 247 
AA2 2 3 N GLU A 204 ? N GLU A 248 O CYS A 252 ? O CYS A 296 
AA3 1 2 N GLU B 28  ? N GLU B 72  O ILE B 42  ? O ILE B 86  
AA3 2 3 N TYR B 43  ? N TYR B 87  O VAL B 83  ? O VAL B 127 
AA3 3 4 O PHE B 84  ? O PHE B 128 N VAL B 58  ? N VAL B 102 
AA3 4 5 N PHE B 53  ? N PHE B 97  O ASP B 122 ? O ASP B 166 
AA3 5 6 N GLY B 130 ? N GLY B 174 O LEU B 154 ? O LEU B 198 
AA4 1 2 N GLY B 174 ? N GLY B 218 O MET B 203 ? O MET B 247 
AA4 2 3 N GLU B 204 ? N GLU B 248 O GLU B 253 ? O GLU B 297 
# 
_pdbx_entry_details.entry_id                   8Z2J 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 107 ? ? 69.23   -1.36   
2  1 ALA A 176 ? ? 66.17   -121.75 
3  1 THR A 199 ? ? 30.62   62.90   
4  1 HIS A 230 ? ? -119.38 -79.74  
5  1 THR A 301 ? ? -99.83  35.09   
6  1 THR B 107 ? ? 68.60   -2.47   
7  1 ALA B 176 ? ? 64.20   -124.03 
8  1 THR B 199 ? ? 30.74   61.80   
9  1 HIS B 230 ? ? -124.24 -82.93  
10 1 CYS B 302 ? ? -47.03  152.74  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       820 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.36 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 45 ? A GLY 1 
2 1 Y 1 B GLY 45 ? B GLY 1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1L0M CAA  C  Y N 1   
A1L0M CAB  C  Y N 2   
A1L0M CAC  C  Y N 3   
A1L0M CAD  C  Y N 4   
A1L0M CAI  C  N N 5   
A1L0M CAJ  C  N N 6   
A1L0M CAL  C  N N 7   
A1L0M CAM  C  Y N 8   
A1L0M CAN  C  Y N 9   
A1L0M CAO  C  Y N 10  
A1L0M CAP  C  Y N 11  
A1L0M CAQ  C  Y N 12  
A1L0M CAR  C  Y N 13  
A1L0M CAS  C  Y N 14  
A1L0M CAT  C  Y N 15  
A1L0M CAU  C  N N 16  
A1L0M CAX  C  N N 17  
A1L0M OAF  O  N N 18  
A1L0M OAG  O  N N 19  
A1L0M OAH  O  N N 20  
A1L0M OAK  O  N N 21  
A1L0M OAV  O  N N 22  
A1L0M OAW  O  N N 23  
A1L0M PAE  P  N N 24  
A1L0M H1   H  N N 25  
A1L0M H2   H  N N 26  
A1L0M H3   H  N N 27  
A1L0M H4   H  N N 28  
A1L0M H5   H  N N 29  
A1L0M H6   H  N N 30  
A1L0M H7   H  N N 31  
A1L0M H8   H  N N 32  
A1L0M H9   H  N N 33  
A1L0M H10  H  N N 34  
A1L0M H11  H  N N 35  
A1L0M H12  H  N N 36  
A1L0M H13  H  N N 37  
A1L0M H14  H  N N 38  
A1L0M H15  H  N N 39  
A1L0M H16  H  N N 40  
A1L0M H17  H  N N 41  
A1L0M H18  H  N N 42  
A1L0M H19  H  N N 43  
ACT   C    C  N N 44  
ACT   O    O  N N 45  
ACT   OXT  O  N N 46  
ACT   CH3  C  N N 47  
ACT   H1   H  N N 48  
ACT   H2   H  N N 49  
ACT   H3   H  N N 50  
ALA   N    N  N N 51  
ALA   CA   C  N S 52  
ALA   C    C  N N 53  
ALA   O    O  N N 54  
ALA   CB   C  N N 55  
ALA   OXT  O  N N 56  
ALA   H    H  N N 57  
ALA   H2   H  N N 58  
ALA   HA   H  N N 59  
ALA   HB1  H  N N 60  
ALA   HB2  H  N N 61  
ALA   HB3  H  N N 62  
ALA   HXT  H  N N 63  
ARG   N    N  N N 64  
ARG   CA   C  N S 65  
ARG   C    C  N N 66  
ARG   O    O  N N 67  
ARG   CB   C  N N 68  
ARG   CG   C  N N 69  
ARG   CD   C  N N 70  
ARG   NE   N  N N 71  
ARG   CZ   C  N N 72  
ARG   NH1  N  N N 73  
ARG   NH2  N  N N 74  
ARG   OXT  O  N N 75  
ARG   H    H  N N 76  
ARG   H2   H  N N 77  
ARG   HA   H  N N 78  
ARG   HB2  H  N N 79  
ARG   HB3  H  N N 80  
ARG   HG2  H  N N 81  
ARG   HG3  H  N N 82  
ARG   HD2  H  N N 83  
ARG   HD3  H  N N 84  
ARG   HE   H  N N 85  
ARG   HH11 H  N N 86  
ARG   HH12 H  N N 87  
ARG   HH21 H  N N 88  
ARG   HH22 H  N N 89  
ARG   HXT  H  N N 90  
ASN   N    N  N N 91  
ASN   CA   C  N S 92  
ASN   C    C  N N 93  
ASN   O    O  N N 94  
ASN   CB   C  N N 95  
ASN   CG   C  N N 96  
ASN   OD1  O  N N 97  
ASN   ND2  N  N N 98  
ASN   OXT  O  N N 99  
ASN   H    H  N N 100 
ASN   H2   H  N N 101 
ASN   HA   H  N N 102 
ASN   HB2  H  N N 103 
ASN   HB3  H  N N 104 
ASN   HD21 H  N N 105 
ASN   HD22 H  N N 106 
ASN   HXT  H  N N 107 
ASP   N    N  N N 108 
ASP   CA   C  N S 109 
ASP   C    C  N N 110 
ASP   O    O  N N 111 
ASP   CB   C  N N 112 
ASP   CG   C  N N 113 
ASP   OD1  O  N N 114 
ASP   OD2  O  N N 115 
ASP   OXT  O  N N 116 
ASP   H    H  N N 117 
ASP   H2   H  N N 118 
ASP   HA   H  N N 119 
ASP   HB2  H  N N 120 
ASP   HB3  H  N N 121 
ASP   HD2  H  N N 122 
ASP   HXT  H  N N 123 
CA    CA   CA N N 124 
CL    CL   CL N N 125 
CYS   N    N  N N 126 
CYS   CA   C  N R 127 
CYS   C    C  N N 128 
CYS   O    O  N N 129 
CYS   CB   C  N N 130 
CYS   SG   S  N N 131 
CYS   OXT  O  N N 132 
CYS   H    H  N N 133 
CYS   H2   H  N N 134 
CYS   HA   H  N N 135 
CYS   HB2  H  N N 136 
CYS   HB3  H  N N 137 
CYS   HG   H  N N 138 
CYS   HXT  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
MPD   C1   C  N N 302 
MPD   C2   C  N N 303 
MPD   O2   O  N N 304 
MPD   CM   C  N N 305 
MPD   C3   C  N N 306 
MPD   C4   C  N S 307 
MPD   O4   O  N N 308 
MPD   C5   C  N N 309 
MPD   H11  H  N N 310 
MPD   H12  H  N N 311 
MPD   H13  H  N N 312 
MPD   HO2  H  N N 313 
MPD   HM1  H  N N 314 
MPD   HM2  H  N N 315 
MPD   HM3  H  N N 316 
MPD   H31  H  N N 317 
MPD   H32  H  N N 318 
MPD   H4   H  N N 319 
MPD   HO4  H  N N 320 
MPD   H51  H  N N 321 
MPD   H52  H  N N 322 
MPD   H53  H  N N 323 
PHE   N    N  N N 324 
PHE   CA   C  N S 325 
PHE   C    C  N N 326 
PHE   O    O  N N 327 
PHE   CB   C  N N 328 
PHE   CG   C  Y N 329 
PHE   CD1  C  Y N 330 
PHE   CD2  C  Y N 331 
PHE   CE1  C  Y N 332 
PHE   CE2  C  Y N 333 
PHE   CZ   C  Y N 334 
PHE   OXT  O  N N 335 
PHE   H    H  N N 336 
PHE   H2   H  N N 337 
PHE   HA   H  N N 338 
PHE   HB2  H  N N 339 
PHE   HB3  H  N N 340 
PHE   HD1  H  N N 341 
PHE   HD2  H  N N 342 
PHE   HE1  H  N N 343 
PHE   HE2  H  N N 344 
PHE   HZ   H  N N 345 
PHE   HXT  H  N N 346 
PRO   N    N  N N 347 
PRO   CA   C  N S 348 
PRO   C    C  N N 349 
PRO   O    O  N N 350 
PRO   CB   C  N N 351 
PRO   CG   C  N N 352 
PRO   CD   C  N N 353 
PRO   OXT  O  N N 354 
PRO   H    H  N N 355 
PRO   HA   H  N N 356 
PRO   HB2  H  N N 357 
PRO   HB3  H  N N 358 
PRO   HG2  H  N N 359 
PRO   HG3  H  N N 360 
PRO   HD2  H  N N 361 
PRO   HD3  H  N N 362 
PRO   HXT  H  N N 363 
SER   N    N  N N 364 
SER   CA   C  N S 365 
SER   C    C  N N 366 
SER   O    O  N N 367 
SER   CB   C  N N 368 
SER   OG   O  N N 369 
SER   OXT  O  N N 370 
SER   H    H  N N 371 
SER   H2   H  N N 372 
SER   HA   H  N N 373 
SER   HB2  H  N N 374 
SER   HB3  H  N N 375 
SER   HG   H  N N 376 
SER   HXT  H  N N 377 
THR   N    N  N N 378 
THR   CA   C  N S 379 
THR   C    C  N N 380 
THR   O    O  N N 381 
THR   CB   C  N R 382 
THR   OG1  O  N N 383 
THR   CG2  C  N N 384 
THR   OXT  O  N N 385 
THR   H    H  N N 386 
THR   H2   H  N N 387 
THR   HA   H  N N 388 
THR   HB   H  N N 389 
THR   HG1  H  N N 390 
THR   HG21 H  N N 391 
THR   HG22 H  N N 392 
THR   HG23 H  N N 393 
THR   HXT  H  N N 394 
TRP   N    N  N N 395 
TRP   CA   C  N S 396 
TRP   C    C  N N 397 
TRP   O    O  N N 398 
TRP   CB   C  N N 399 
TRP   CG   C  Y N 400 
TRP   CD1  C  Y N 401 
TRP   CD2  C  Y N 402 
TRP   NE1  N  Y N 403 
TRP   CE2  C  Y N 404 
TRP   CE3  C  Y N 405 
TRP   CZ2  C  Y N 406 
TRP   CZ3  C  Y N 407 
TRP   CH2  C  Y N 408 
TRP   OXT  O  N N 409 
TRP   H    H  N N 410 
TRP   H2   H  N N 411 
TRP   HA   H  N N 412 
TRP   HB2  H  N N 413 
TRP   HB3  H  N N 414 
TRP   HD1  H  N N 415 
TRP   HE1  H  N N 416 
TRP   HE3  H  N N 417 
TRP   HZ2  H  N N 418 
TRP   HZ3  H  N N 419 
TRP   HH2  H  N N 420 
TRP   HXT  H  N N 421 
TYR   N    N  N N 422 
TYR   CA   C  N S 423 
TYR   C    C  N N 424 
TYR   O    O  N N 425 
TYR   CB   C  N N 426 
TYR   CG   C  Y N 427 
TYR   CD1  C  Y N 428 
TYR   CD2  C  Y N 429 
TYR   CE1  C  Y N 430 
TYR   CE2  C  Y N 431 
TYR   CZ   C  Y N 432 
TYR   OH   O  N N 433 
TYR   OXT  O  N N 434 
TYR   H    H  N N 435 
TYR   H2   H  N N 436 
TYR   HA   H  N N 437 
TYR   HB2  H  N N 438 
TYR   HB3  H  N N 439 
TYR   HD1  H  N N 440 
TYR   HD2  H  N N 441 
TYR   HE1  H  N N 442 
TYR   HE2  H  N N 443 
TYR   HH   H  N N 444 
TYR   HXT  H  N N 445 
VAL   N    N  N N 446 
VAL   CA   C  N S 447 
VAL   C    C  N N 448 
VAL   O    O  N N 449 
VAL   CB   C  N N 450 
VAL   CG1  C  N N 451 
VAL   CG2  C  N N 452 
VAL   OXT  O  N N 453 
VAL   H    H  N N 454 
VAL   H2   H  N N 455 
VAL   HA   H  N N 456 
VAL   HB   H  N N 457 
VAL   HG11 H  N N 458 
VAL   HG12 H  N N 459 
VAL   HG13 H  N N 460 
VAL   HG21 H  N N 461 
VAL   HG22 H  N N 462 
VAL   HG23 H  N N 463 
VAL   HXT  H  N N 464 
# 
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 
A1L0M OAG PAE  doub N N 1   
A1L0M OAF PAE  sing N N 2   
A1L0M PAE CAD  sing N N 3   
A1L0M PAE OAH  sing N N 4   
A1L0M CAC CAD  doub Y N 5   
A1L0M CAC CAB  sing Y N 6   
A1L0M CAI OAH  sing N N 7   
A1L0M CAI CAJ  sing N N 8   
A1L0M CAD CAS  sing Y N 9   
A1L0M CAB CAA  doub Y N 10  
A1L0M CAJ OAK  sing N N 11  
A1L0M CAS CAT  doub Y N 12  
A1L0M CAX OAW  sing N N 13  
A1L0M CAA CAT  sing Y N 14  
A1L0M CAA CAU  sing N N 15  
A1L0M OAW CAU  sing N N 16  
A1L0M OAK CAL  sing N N 17  
A1L0M CAU OAV  doub N N 18  
A1L0M CAL CAM  sing N N 19  
A1L0M CAM CAN  doub Y N 20  
A1L0M CAM CAR  sing Y N 21  
A1L0M CAN CAO  sing Y N 22  
A1L0M CAR CAQ  doub Y N 23  
A1L0M CAO CAP  doub Y N 24  
A1L0M CAQ CAP  sing Y N 25  
A1L0M CAB H1   sing N N 26  
A1L0M CAC H2   sing N N 27  
A1L0M CAI H3   sing N N 28  
A1L0M CAI H4   sing N N 29  
A1L0M CAJ H5   sing N N 30  
A1L0M CAJ H6   sing N N 31  
A1L0M CAL H7   sing N N 32  
A1L0M CAL H8   sing N N 33  
A1L0M CAN H9   sing N N 34  
A1L0M CAO H10  sing N N 35  
A1L0M CAP H11  sing N N 36  
A1L0M CAQ H12  sing N N 37  
A1L0M CAR H13  sing N N 38  
A1L0M CAS H14  sing N N 39  
A1L0M CAT H15  sing N N 40  
A1L0M CAX H16  sing N N 41  
A1L0M CAX H17  sing N N 42  
A1L0M CAX H18  sing N N 43  
A1L0M OAF H19  sing N N 44  
ACT   C   O    doub N N 45  
ACT   C   OXT  sing N N 46  
ACT   C   CH3  sing N N 47  
ACT   CH3 H1   sing N N 48  
ACT   CH3 H2   sing N N 49  
ACT   CH3 H3   sing N N 50  
ALA   N   CA   sing N N 51  
ALA   N   H    sing N N 52  
ALA   N   H2   sing N N 53  
ALA   CA  C    sing N N 54  
ALA   CA  CB   sing N N 55  
ALA   CA  HA   sing N N 56  
ALA   C   O    doub N N 57  
ALA   C   OXT  sing N N 58  
ALA   CB  HB1  sing N N 59  
ALA   CB  HB2  sing N N 60  
ALA   CB  HB3  sing N N 61  
ALA   OXT HXT  sing N N 62  
ARG   N   CA   sing N N 63  
ARG   N   H    sing N N 64  
ARG   N   H2   sing N N 65  
ARG   CA  C    sing N N 66  
ARG   CA  CB   sing N N 67  
ARG   CA  HA   sing N N 68  
ARG   C   O    doub N N 69  
ARG   C   OXT  sing N N 70  
ARG   CB  CG   sing N N 71  
ARG   CB  HB2  sing N N 72  
ARG   CB  HB3  sing N N 73  
ARG   CG  CD   sing N N 74  
ARG   CG  HG2  sing N N 75  
ARG   CG  HG3  sing N N 76  
ARG   CD  NE   sing N N 77  
ARG   CD  HD2  sing N N 78  
ARG   CD  HD3  sing N N 79  
ARG   NE  CZ   sing N N 80  
ARG   NE  HE   sing N N 81  
ARG   CZ  NH1  sing N N 82  
ARG   CZ  NH2  doub N N 83  
ARG   NH1 HH11 sing N N 84  
ARG   NH1 HH12 sing N N 85  
ARG   NH2 HH21 sing N N 86  
ARG   NH2 HH22 sing N N 87  
ARG   OXT HXT  sing N N 88  
ASN   N   CA   sing N N 89  
ASN   N   H    sing N N 90  
ASN   N   H2   sing N N 91  
ASN   CA  C    sing N N 92  
ASN   CA  CB   sing N N 93  
ASN   CA  HA   sing N N 94  
ASN   C   O    doub N N 95  
ASN   C   OXT  sing N N 96  
ASN   CB  CG   sing N N 97  
ASN   CB  HB2  sing N N 98  
ASN   CB  HB3  sing N N 99  
ASN   CG  OD1  doub N N 100 
ASN   CG  ND2  sing N N 101 
ASN   ND2 HD21 sing N N 102 
ASN   ND2 HD22 sing N N 103 
ASN   OXT HXT  sing N N 104 
ASP   N   CA   sing N N 105 
ASP   N   H    sing N N 106 
ASP   N   H2   sing N N 107 
ASP   CA  C    sing N N 108 
ASP   CA  CB   sing N N 109 
ASP   CA  HA   sing N N 110 
ASP   C   O    doub N N 111 
ASP   C   OXT  sing N N 112 
ASP   CB  CG   sing N N 113 
ASP   CB  HB2  sing N N 114 
ASP   CB  HB3  sing N N 115 
ASP   CG  OD1  doub N N 116 
ASP   CG  OD2  sing N N 117 
ASP   OD2 HD2  sing N N 118 
ASP   OXT HXT  sing N N 119 
CYS   N   CA   sing N N 120 
CYS   N   H    sing N N 121 
CYS   N   H2   sing N N 122 
CYS   CA  C    sing N N 123 
CYS   CA  CB   sing N N 124 
CYS   CA  HA   sing N N 125 
CYS   C   O    doub N N 126 
CYS   C   OXT  sing N N 127 
CYS   CB  SG   sing N N 128 
CYS   CB  HB2  sing N N 129 
CYS   CB  HB3  sing N N 130 
CYS   SG  HG   sing N N 131 
CYS   OXT HXT  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
MPD   C1  C2   sing N N 287 
MPD   C1  H11  sing N N 288 
MPD   C1  H12  sing N N 289 
MPD   C1  H13  sing N N 290 
MPD   C2  O2   sing N N 291 
MPD   C2  CM   sing N N 292 
MPD   C2  C3   sing N N 293 
MPD   O2  HO2  sing N N 294 
MPD   CM  HM1  sing N N 295 
MPD   CM  HM2  sing N N 296 
MPD   CM  HM3  sing N N 297 
MPD   C3  C4   sing N N 298 
MPD   C3  H31  sing N N 299 
MPD   C3  H32  sing N N 300 
MPD   C4  O4   sing N N 301 
MPD   C4  C5   sing N N 302 
MPD   C4  H4   sing N N 303 
MPD   O4  HO4  sing N N 304 
MPD   C5  H51  sing N N 305 
MPD   C5  H52  sing N N 306 
MPD   C5  H53  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           JP21H02120 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7CTS 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z2J 
_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]   0.024062 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006955 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012684 
_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]   0.014019 
_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.
;
? 
CA ? ? 16.26893 3.65395 ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 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  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135  5.44231 ? ? 1.42069  35.72801 ? ? 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   . PRO   A 1 2   ? 3.21000   -4.84500  -16.28700 1.000 29.56682 ? 46  PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 2   ? 3.73400   -6.00800  -17.01200 1.000 26.20682 ? 46  PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 2   ? 4.66300   -6.91900  -16.19800 1.000 24.40682 ? 46  PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 2   ? 4.82500   -8.06500  -16.61300 1.000 28.13682 ? 46  PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 2   ? 4.50200   -5.37500  -18.18500 1.000 23.32682 ? 46  PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 2   ? 4.61100   -3.91400  -17.87500 1.000 25.81682 ? 46  PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 2   ? 3.42100   -3.59400  -17.03200 1.000 34.37682 ? 46  PRO   A CD  1 
ATOM   8    N  N   . ASN   A 1 3   ? 5.24900   -6.43400  -15.09600 1.000 25.89682 ? 47  ASN   A N   1 
ATOM   9    C  CA  . ASN   A 1 3   ? 6.19600   -7.20500  -14.28700 1.000 20.86682 ? 47  ASN   A CA  1 
ATOM   10   C  C   . ASN   A 1 3   ? 5.64500   -8.60500  -14.00700 1.000 17.37682 ? 47  ASN   A C   1 
ATOM   11   O  O   . ASN   A 1 3   ? 4.61500   -8.73300  -13.33200 1.000 16.74682 ? 47  ASN   A O   1 
ATOM   12   C  CB  . ASN   A 1 3   ? 6.48700   -6.47000  -12.97600 1.000 19.64682 ? 47  ASN   A CB  1 
ATOM   13   C  CG  . ASN   A 1 3   ? 7.37600   -7.26500  -12.00800 1.000 17.40682 ? 47  ASN   A CG  1 
ATOM   14   O  OD1 . ASN   A 1 3   ? 7.90100   -8.33700  -12.32500 1.000 13.91682 ? 47  ASN   A OD1 1 
ATOM   15   N  ND2 . ASN   A 1 3   ? 7.54200   -6.71900  -10.80500 1.000 17.76682 ? 47  ASN   A ND2 1 
ATOM   16   N  N   . PRO   A 1 4   ? 6.29400   -9.66200  -14.50500 1.000 12.50682 ? 48  PRO   A N   1 
ATOM   17   C  CA  . PRO   A 1 4   ? 5.76100   -11.02000 -14.32900 1.000 16.11682 ? 48  PRO   A CA  1 
ATOM   18   C  C   . PRO   A 1 4   ? 5.70700   -11.50000 -12.88300 1.000 17.48682 ? 48  PRO   A C   1 
ATOM   19   O  O   . PRO   A 1 4   ? 5.03100   -12.50700 -12.61800 1.000 15.55682 ? 48  PRO   A O   1 
ATOM   20   C  CB  . PRO   A 1 4   ? 6.73000   -11.87900 -15.15600 1.000 18.08682 ? 48  PRO   A CB  1 
ATOM   21   C  CG  . PRO   A 1 4   ? 8.01300   -11.08500 -15.15700 1.000 18.69682 ? 48  PRO   A CG  1 
ATOM   22   C  CD  . PRO   A 1 4   ? 7.57600   -9.65800  -15.22900 1.000 16.38682 ? 48  PRO   A CD  1 
ATOM   23   N  N   . TYR   A 1 5   ? 6.40000   -10.83600 -11.95600 1.000 13.66682 ? 49  TYR   A N   1 
ATOM   24   C  CA  . TYR   A 1 5   ? 6.44500   -11.25000 -10.55900 1.000 16.35682 ? 49  TYR   A CA  1 
ATOM   25   C  C   . TYR   A 1 5   ? 5.47800   -10.47100 -9.66800  1.000 15.29682 ? 49  TYR   A C   1 
ATOM   26   O  O   . TYR   A 1 5   ? 5.46100   -10.69300 -8.45300  1.000 13.63682 ? 49  TYR   A O   1 
ATOM   27   C  CB  . TYR   A 1 5   ? 7.88000   -11.11500 -10.02400 1.000 10.85682 ? 49  TYR   A CB  1 
ATOM   28   C  CG  . TYR   A 1 5   ? 8.90800   -11.78200 -10.92000 1.000 13.31682 ? 49  TYR   A CG  1 
ATOM   29   C  CD1 . TYR   A 1 5   ? 8.69200   -13.05300 -11.43200 1.000 10.59682 ? 49  TYR   A CD1 1 
ATOM   30   C  CD2 . TYR   A 1 5   ? 10.07200  -11.12100 -11.28600 1.000 13.42682 ? 49  TYR   A CD2 1 
ATOM   31   C  CE1 . TYR   A 1 5   ? 9.62000   -13.66200 -12.25400 1.000 14.25682 ? 49  TYR   A CE1 1 
ATOM   32   C  CE2 . TYR   A 1 5   ? 11.00100  -11.71300 -12.11000 1.000 15.78682 ? 49  TYR   A CE2 1 
ATOM   33   C  CZ  . TYR   A 1 5   ? 10.77200  -12.98200 -12.59200 1.000 16.27682 ? 49  TYR   A CZ  1 
ATOM   34   O  OH  . TYR   A 1 5   ? 11.70100  -13.57100 -13.40800 1.000 22.83682 ? 49  TYR   A OH  1 
ATOM   35   N  N   . GLU   A 1 6   ? 4.68400   -9.56200  -10.22800 1.000 13.20682 ? 50  GLU   A N   1 
ATOM   36   C  CA  . GLU   A 1 6   ? 3.71500   -8.83100  -9.41600  1.000 18.81682 ? 50  GLU   A CA  1 
ATOM   37   C  C   . GLU   A 1 6   ? 2.58900   -9.75400  -8.97200  1.000 15.13682 ? 50  GLU   A C   1 
ATOM   38   O  O   . GLU   A 1 6   ? 1.95500   -10.42100 -9.79500  1.000 12.89682 ? 50  GLU   A O   1 
ATOM   39   C  CB  . GLU   A 1 6   ? 3.13800   -7.63800  -10.18800 1.000 18.14682 ? 50  GLU   A CB  1 
ATOM   40   C  CG  . GLU   A 1 6   ? 4.03900   -6.41700  -10.21600 1.000 20.05682 ? 50  GLU   A CG  1 
ATOM   41   C  CD  . GLU   A 1 6   ? 3.37900   -5.19700  -10.86300 1.000 25.19682 ? 50  GLU   A CD  1 
ATOM   42   O  OE1 . GLU   A 1 6   ? 2.17700   -5.26600  -11.18600 1.000 25.05682 ? 50  GLU   A OE1 1 
ATOM   43   O  OE2 . GLU   A 1 6   ? 4.07000   -4.16700  -11.04100 1.000 22.68682 ? 50  GLU   A OE2 1 
ATOM   44   N  N   . ARG   A 1 7   ? 2.33700   -9.77800  -7.67000  1.000 13.95682 ? 51  ARG   A N   1 
ATOM   45   C  CA  . ARG   A 1 7   ? 1.25500   -10.54900 -7.07900  1.000 12.61682 ? 51  ARG   A CA  1 
ATOM   46   C  C   . ARG   A 1 7   ? 0.38600   -9.61500  -6.25200  1.000 17.90682 ? 51  ARG   A C   1 
ATOM   47   O  O   . ARG   A 1 7   ? 0.90300   -8.75700  -5.53600  1.000 13.31682 ? 51  ARG   A O   1 
ATOM   48   C  CB  . ARG   A 1 7   ? 1.80500   -11.69100 -6.20400  1.000 12.37682 ? 51  ARG   A CB  1 
ATOM   49   C  CG  . ARG   A 1 7   ? 2.83800   -12.56900 -6.93400  1.000 9.36682  ? 51  ARG   A CG  1 
ATOM   50   C  CD  . ARG   A 1 7   ? 2.15900   -13.50200 -7.94000  1.000 13.14682 ? 51  ARG   A CD  1 
ATOM   51   N  NE  . ARG   A 1 7   ? 3.12400   -14.29800 -8.69200  1.000 15.93682 ? 51  ARG   A NE  1 
ATOM   52   C  CZ  . ARG   A 1 7   ? 3.62500   -13.95000 -9.86900  1.000 17.09682 ? 51  ARG   A CZ  1 
ATOM   53   N  NH1 . ARG   A 1 7   ? 3.23500   -12.84200 -10.48700 1.000 15.63682 ? 51  ARG   A NH1 1 
ATOM   54   N  NH2 . ARG   A 1 7   ? 4.53600   -14.73200 -10.44400 1.000 13.72682 ? 51  ARG   A NH2 1 
ATOM   55   N  N   . GLY   A 1 8   ? -0.93400  -9.76600  -6.36600  1.000 17.14682 ? 52  GLY   A N   1 
ATOM   56   C  CA  . GLY   A 1 8   ? -1.84600  -9.05300  -5.50400  1.000 15.57682 ? 52  GLY   A CA  1 
ATOM   57   C  C   . GLY   A 1 8   ? -2.24000  -7.68000  -6.01700  1.000 15.84682 ? 52  GLY   A C   1 
ATOM   58   O  O   . GLY   A 1 8   ? -1.62600  -7.13000  -6.93600  1.000 16.45682 ? 52  GLY   A O   1 
ATOM   59   N  N   . PRO   A 1 9   ? -3.26500  -7.08800  -5.40600  1.000 22.90682 ? 53  PRO   A N   1 
ATOM   60   C  CA  . PRO   A 1 9   ? -3.72400  -5.76300  -5.83600  1.000 19.22682 ? 53  PRO   A CA  1 
ATOM   61   C  C   . PRO   A 1 9   ? -2.72500  -4.67800  -5.45500  1.000 20.38682 ? 53  PRO   A C   1 
ATOM   62   O  O   . PRO   A 1 9   ? -1.81600  -4.88300  -4.65000  1.000 18.74682 ? 53  PRO   A O   1 
ATOM   63   C  CB  . PRO   A 1 9   ? -5.04600  -5.59600  -5.08400  1.000 27.79682 ? 53  PRO   A CB  1 
ATOM   64   C  CG  . PRO   A 1 9   ? -4.84300  -6.37700  -3.82800  1.000 27.19682 ? 53  PRO   A CG  1 
ATOM   65   C  CD  . PRO   A 1 9   ? -3.98600  -7.56000  -4.21000  1.000 21.20682 ? 53  PRO   A CD  1 
ATOM   66   N  N   . ASP   A 1 10  ? -2.91500  -3.49700  -6.04300  1.000 20.03682 ? 54  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 10  ? -2.03600  -2.36800  -5.74800  1.000 18.13682 ? 54  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 10  ? -2.06900  -2.03300  -4.25800  1.000 17.28682 ? 54  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 10  ? -3.15400  -1.95000  -3.66600  1.000 18.18682 ? 54  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 10  ? -2.42800  -1.15200  -6.58700  1.000 23.40682 ? 54  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 10  ? -2.23800  -1.40100  -8.07100  1.000 21.19682 ? 54  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 10  ? -1.63800  -2.44500  -8.40600  1.000 24.18682 ? 54  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 10  ? -2.68600  -0.57700  -8.89900  1.000 24.92682 ? 54  ASP   A OD2 1 
ATOM   74   N  N   . PRO   A 1 11  ? -0.91700  -1.85000  -3.61900  1.000 17.54682 ? 55  PRO   A N   1 
ATOM   75   C  CA  . PRO   A 1 11  ? -0.88700  -1.73200  -2.15800  1.000 15.72682 ? 55  PRO   A CA  1 
ATOM   76   C  C   . PRO   A 1 11  ? -1.28500  -0.35100  -1.66000  1.000 14.50682 ? 55  PRO   A C   1 
ATOM   77   O  O   . PRO   A 1 11  ? -1.18100  0.66200   -2.35400  1.000 15.58682 ? 55  PRO   A O   1 
ATOM   78   C  CB  . PRO   A 1 11  ? 0.57800   -2.02500  -1.81200  1.000 10.41682 ? 55  PRO   A CB  1 
ATOM   79   C  CG  . PRO   A 1 11  ? 1.33200   -1.59800  -3.01800  1.000 13.94682 ? 55  PRO   A CG  1 
ATOM   80   C  CD  . PRO   A 1 11  ? 0.43800   -1.95200  -4.19300  1.000 13.87682 ? 55  PRO   A CD  1 
ATOM   81   N  N   . THR   A 1 12  ? -1.72900  -0.33200  -0.40800  1.000 16.39682 ? 56  THR   A N   1 
ATOM   82   C  CA  . THR   A 1 12  ? -2.03100  0.89500   0.30600   1.000 15.53682 ? 56  THR   A CA  1 
ATOM   83   C  C   . THR   A 1 12  ? -1.36900  0.82000   1.67400   1.000 18.05682 ? 56  THR   A C   1 
ATOM   84   O  O   . THR   A 1 12  ? -0.89500  -0.23900  2.09600   1.000 13.46682 ? 56  THR   A O   1 
ATOM   85   C  CB  . THR   A 1 12  ? -3.54900  1.10300   0.44800   1.000 21.24682 ? 56  THR   A CB  1 
ATOM   86   O  OG1 . THR   A 1 12  ? -4.10300  0.06400   1.26700   1.000 17.31682 ? 56  THR   A OG1 1 
ATOM   87   C  CG2 . THR   A 1 12  ? -4.23100  1.08300   -0.92700  1.000 21.57682 ? 56  THR   A CG2 1 
ATOM   88   N  N   . GLU   A 1 13  ? -1.34300  1.95300   2.38100   1.000 17.10682 ? 57  GLU   A N   1 
ATOM   89   C  CA  . GLU   A 1 13  ? -0.88500  1.92200   3.76700   1.000 20.85682 ? 57  GLU   A CA  1 
ATOM   90   C  C   . GLU   A 1 13  ? -1.69100  0.92100   4.58200   1.000 20.78682 ? 57  GLU   A C   1 
ATOM   91   O  O   . GLU   A 1 13  ? -1.15300  0.24400   5.46800   1.000 16.31682 ? 57  GLU   A O   1 
ATOM   92   C  CB  . GLU   A 1 13  ? -0.98300  3.31500   4.39300   1.000 22.76682 ? 57  GLU   A CB  1 
ATOM   93   C  CG  . GLU   A 1 13  ? 0.01400   4.31100   3.85800   1.000 21.78682 ? 57  GLU   A CG  1 
ATOM   94   C  CD  . GLU   A 1 13  ? 1.43700   4.01500   4.30600   1.000 33.39682 ? 57  GLU   A CD  1 
ATOM   95   O  OE1 . GLU   A 1 13  ? 1.62200   3.19300   5.23100   1.000 37.05682 ? 57  GLU   A OE1 1 
ATOM   96   O  OE2 . GLU   A 1 13  ? 2.37500   4.60400   3.73100   1.000 39.88682 ? 57  GLU   A OE2 1 
ATOM   97   N  N   . ASP   A 1 14  ? -2.98400  0.79500   4.28000   1.000 19.95682 ? 58  ASP   A N   1 
ATOM   98   C  CA  . ASP   A 1 14  ? -3.81700  -0.14100  5.02500   1.000 18.70682 ? 58  ASP   A CA  1 
ATOM   99   C  C   . ASP   A 1 14  ? -3.47100  -1.58700  4.69000   1.000 17.29682 ? 58  ASP   A C   1 
ATOM   100  O  O   . ASP   A 1 14  ? -3.47300  -2.44900  5.57600   1.000 16.72682 ? 58  ASP   A O   1 
ATOM   101  C  CB  . ASP   A 1 14  ? -5.29000  0.14300   4.74700   1.000 23.47682 ? 58  ASP   A CB  1 
ATOM   102  C  CG  . ASP   A 1 14  ? -5.67500  1.57500   5.09200   1.000 34.42682 ? 58  ASP   A CG  1 
ATOM   103  O  OD1 . ASP   A 1 14  ? -5.46100  1.99500   6.25700   1.000 31.39682 ? 58  ASP   A OD1 1 
ATOM   104  O  OD2 . ASP   A 1 14  ? -6.17000  2.28800   4.19200   1.000 35.74682 ? 58  ASP   A OD2 1 
ATOM   105  N  N   . SER   A 1 15  ? -3.15100  -1.87500  3.42600   1.000 15.83682 ? 59  SER   A N   1 
ATOM   106  C  CA  . SER   A 1 15  ? -2.94900  -3.27400  3.06400   1.000 21.25682 ? 59  SER   A CA  1 
ATOM   107  C  C   . SER   A 1 15  ? -1.61200  -3.79500  3.56600   1.000 13.38682 ? 59  SER   A C   1 
ATOM   108  O  O   . SER   A 1 15  ? -1.50500  -4.97700  3.91000   1.000 13.06682 ? 59  SER   A O   1 
ATOM   109  C  CB  . SER   A 1 15  ? -3.06600  -3.47600  1.54700   1.000 15.23682 ? 59  SER   A CB  1 
ATOM   110  O  OG  . SER   A 1 15  ? -1.98800  -2.88900  0.84200   1.000 17.01682 ? 59  SER   A OG  1 
ATOM   111  N  N   . ILE   A 1 16  ? -0.59200  -2.93900  3.63700   1.000 14.68682 ? 60  ILE   A N   1 
ATOM   112  C  CA  . ILE   A 1 16  ? 0.69000   -3.41300  4.14700   1.000 15.38682 ? 60  ILE   A CA  1 
ATOM   113  C  C   . ILE   A 1 16  ? 0.70500   -3.47700  5.67400   1.000 11.73682 ? 60  ILE   A C   1 
ATOM   114  O  O   . ILE   A 1 16  ? 1.54400   -4.17700  6.25000   1.000 10.82682 ? 60  ILE   A O   1 
ATOM   115  C  CB  . ILE   A 1 16  ? 1.86000   -2.55800  3.61200   1.000 9.32682  ? 60  ILE   A CB  1 
ATOM   116  C  CG1 . ILE   A 1 16  ? 1.75900   -1.10200  4.05600   1.000 11.25682 ? 60  ILE   A CG1 1 
ATOM   117  C  CG2 . ILE   A 1 16  ? 1.94600   -2.62900  2.08300   1.000 13.60682 ? 60  ILE   A CG2 1 
ATOM   118  C  CD1 . ILE   A 1 16  ? 3.02300   -0.29600  3.70100   1.000 15.34682 ? 60  ILE   A CD1 1 
ATOM   119  N  N   . GLU   A 1 17  ? -0.20600  -2.79000  6.35600   1.000 12.95682 ? 61  GLU   A N   1 
ATOM   120  C  CA  . GLU   A 1 17  ? -0.30100  -2.92900  7.80000   1.000 12.72682 ? 61  GLU   A CA  1 
ATOM   121  C  C   . GLU   A 1 17  ? -1.22400  -4.06900  8.22200   1.000 12.99682 ? 61  GLU   A C   1 
ATOM   122  O  O   . GLU   A 1 17  ? -1.16300  -4.49800  9.37700   1.000 17.07682 ? 61  GLU   A O   1 
ATOM   123  C  CB  . GLU   A 1 17  ? -0.77600  -1.61100  8.43200   1.000 13.53682 ? 61  GLU   A CB  1 
ATOM   124  C  CG  . GLU   A 1 17  ? 0.21900   -0.46400  8.28100   1.000 14.98682 ? 61  GLU   A CG  1 
ATOM   125  C  CD  . GLU   A 1 17  ? -0.27600  0.83000   8.88900   1.000 20.82682 ? 61  GLU   A CD  1 
ATOM   126  O  OE1 . GLU   A 1 17  ? -1.44600  0.87800   9.32800   1.000 18.66682 ? 61  GLU   A OE1 1 
ATOM   127  O  OE2 . GLU   A 1 17  ? 0.50500   1.80700   8.92700   1.000 20.00682 ? 61  GLU   A OE2 1 
ATOM   128  N  N   . ALA   A 1 18  ? -2.03900  -4.59000  7.30800   1.000 16.37682 ? 62  ALA   A N   1 
ATOM   129  C  CA  . ALA   A 1 18  ? -3.04000  -5.59400  7.65600   1.000 14.58682 ? 62  ALA   A CA  1 
ATOM   130  C  C   . ALA   A 1 18  ? -2.39000  -6.87100  8.17000   1.000 18.83682 ? 62  ALA   A C   1 
ATOM   131  O  O   . ALA   A 1 18  ? -1.36700  -7.31800  7.64700   1.000 15.80682 ? 62  ALA   A O   1 
ATOM   132  C  CB  . ALA   A 1 18  ? -3.90300  -5.91900  6.43900   1.000 15.76682 ? 62  ALA   A CB  1 
ATOM   133  N  N   . ILE   A 1 19  ? -3.01300  -7.48400  9.18400   1.000 13.89682 ? 63  ILE   A N   1 
ATOM   134  C  CA  . ILE   A 1 19  ? -2.45600  -8.71700  9.72600   1.000 16.34682 ? 63  ILE   A CA  1 
ATOM   135  C  C   . ILE   A 1 19  ? -2.54700  -9.85400  8.72300   1.000 17.06682 ? 63  ILE   A C   1 
ATOM   136  O  O   . ILE   A 1 19  ? -1.79000  -10.82600 8.82800   1.000 18.98682 ? 63  ILE   A O   1 
ATOM   137  C  CB  . ILE   A 1 19  ? -3.12500  -9.12200  11.05700  1.000 15.59682 ? 63  ILE   A CB  1 
ATOM   138  C  CG1 . ILE   A 1 19  ? -4.59100  -9.51900  10.85400  1.000 16.15682 ? 63  ILE   A CG1 1 
ATOM   139  C  CG2 . ILE   A 1 19  ? -3.00000  -8.01500  12.09300  1.000 18.60682 ? 63  ILE   A CG2 1 
ATOM   140  C  CD1 . ILE   A 1 19  ? -5.28200  -9.92200  12.15200  1.000 20.93682 ? 63  ILE   A CD1 1 
ATOM   141  N  N   . ARG   A 1 20  ? -3.43200  -9.75300  7.73400   1.000 21.97682 ? 64  ARG   A N   1 
ATOM   142  C  CA  . ARG   A 1 20  ? -3.59800  -10.78900 6.72100   1.000 16.89682 ? 64  ARG   A CA  1 
ATOM   143  C  C   . ARG   A 1 20  ? -3.65400  -10.14000 5.34900   1.000 21.15682 ? 64  ARG   A C   1 
ATOM   144  O  O   . ARG   A 1 20  ? -4.54200  -9.32500  5.08600   1.000 18.26682 ? 64  ARG   A O   1 
ATOM   145  C  CB  . ARG   A 1 20  ? -4.86800  -11.61600 6.96200   1.000 23.40682 ? 64  ARG   A CB  1 
ATOM   146  C  CG  . ARG   A 1 20  ? -4.75900  -12.60400 8.10700   1.000 24.17682 ? 64  ARG   A CG  1 
ATOM   147  C  CD  . ARG   A 1 20  ? -5.97900  -13.51800 8.18300   1.000 30.11682 ? 64  ARG   A CD  1 
ATOM   148  N  NE  . ARG   A 1 20  ? -7.22900  -12.79200 8.38400   1.000 34.30682 ? 64  ARG   A NE  1 
ATOM   149  C  CZ  . ARG   A 1 20  ? -8.42200  -13.36500 8.48300   1.000 35.64682 ? 64  ARG   A CZ  1 
ATOM   150  N  NH1 . ARG   A 1 20  ? -8.56600  -14.67800 8.42700   1.000 35.88682 ? 64  ARG   A NH1 1 
ATOM   151  N  NH2 . ARG   A 1 20  ? -9.50000  -12.59900 8.63400   1.000 29.65682 ? 64  ARG   A NH2 1 
ATOM   152  N  N   . GLY   A 1 21  ? -2.71700  -10.52000 4.47500   1.000 16.93682 ? 65  GLY   A N   1 
ATOM   153  C  CA  . GLY   A 1 21  ? -2.73800  -10.11300 3.09000   1.000 10.58682 ? 65  GLY   A CA  1 
ATOM   154  C  C   . GLY   A 1 21  ? -3.81500  -10.84900 2.31900   1.000 13.97682 ? 65  GLY   A C   1 
ATOM   155  O  O   . GLY   A 1 21  ? -4.59400  -11.62300 2.88600   1.000 12.97682 ? 65  GLY   A O   1 
ATOM   156  N  N   . PRO   A 1 22  ? -3.86300  -10.63500 1.00300   1.000 17.37682 ? 66  PRO   A N   1 
ATOM   157  C  CA  . PRO   A 1 22  ? -4.96700  -11.16400 0.18600   1.000 21.52682 ? 66  PRO   A CA  1 
ATOM   158  C  C   . PRO   A 1 22  ? -4.88700  -12.64800 -0.13800  1.000 21.55682 ? 66  PRO   A C   1 
ATOM   159  O  O   . PRO   A 1 22  ? -5.81700  -13.17300 -0.76400  1.000 23.58682 ? 66  PRO   A O   1 
ATOM   160  C  CB  . PRO   A 1 22  ? -4.86100  -10.33200 -1.09900  1.000 18.08682 ? 66  PRO   A CB  1 
ATOM   161  C  CG  . PRO   A 1 22  ? -3.41900  -9.97700  -1.19600  1.000 20.92682 ? 66  PRO   A CG  1 
ATOM   162  C  CD  . PRO   A 1 22  ? -2.97100  -9.75300  0.22800   1.000 23.12682 ? 66  PRO   A CD  1 
ATOM   163  N  N   . PHE   A 1 23  ? -3.82600  -13.34700 0.24900   1.000 14.60682 ? 67  PHE   A N   1 
ATOM   164  C  CA  . PHE   A 1 23  ? -3.69100  -14.76600 -0.05000  1.000 16.78682 ? 67  PHE   A CA  1 
ATOM   165  C  C   . PHE   A 1 23  ? -4.00800  -15.59300 1.18900   1.000 15.55682 ? 67  PHE   A C   1 
ATOM   166  O  O   . PHE   A 1 23  ? -3.63400  -15.22300 2.30400   1.000 16.22682 ? 67  PHE   A O   1 
ATOM   167  C  CB  . PHE   A 1 23  ? -2.27500  -15.08900 -0.54700  1.000 12.78682 ? 67  PHE   A CB  1 
ATOM   168  C  CG  . PHE   A 1 23  ? -1.94800  -14.49500 -1.89000  1.000 15.51682 ? 67  PHE   A CG  1 
ATOM   169  C  CD1 . PHE   A 1 23  ? -2.27200  -15.17200 -3.06300  1.000 15.54682 ? 67  PHE   A CD1 1 
ATOM   170  C  CD2 . PHE   A 1 23  ? -1.29400  -13.27400 -1.98600  1.000 12.47682 ? 67  PHE   A CD2 1 
ATOM   171  C  CE1 . PHE   A 1 23  ? -1.97500  -14.63100 -4.30900  1.000 14.40682 ? 67  PHE   A CE1 1 
ATOM   172  C  CE2 . PHE   A 1 23  ? -0.98500  -12.73000 -3.22600  1.000 15.76682 ? 67  PHE   A CE2 1 
ATOM   173  C  CZ  . PHE   A 1 23  ? -1.33100  -13.41200 -4.39900  1.000 12.32682 ? 67  PHE   A CZ  1 
ATOM   174  N  N   . SER   A 1 24  ? -4.71400  -16.70600 0.99300   1.000 18.74682 ? 68  SER   A N   1 
ATOM   175  C  CA  . SER   A 1 24  ? -4.88900  -17.67100 2.06500   1.000 12.73682 ? 68  SER   A CA  1 
ATOM   176  C  C   . SER   A 1 24  ? -3.63600  -18.53000 2.15100   1.000 14.13682 ? 68  SER   A C   1 
ATOM   177  O  O   . SER   A 1 24  ? -2.93300  -18.72100 1.15800   1.000 16.17682 ? 68  SER   A O   1 
ATOM   178  C  CB  . SER   A 1 24  ? -6.13800  -18.53800 1.84400   1.000 15.26682 ? 68  SER   A CB  1 
ATOM   179  O  OG  . SER   A 1 24  ? -6.14600  -19.13000 0.55900   1.000 18.40682 ? 68  SER   A OG  1 
ATOM   180  N  N   . VAL   A 1 25  ? -3.33400  -19.00900 3.36000   1.000 14.62682 ? 69  VAL   A N   1 
ATOM   181  C  CA  . VAL   A 1 25  ? -2.05400  -19.64700 3.66000   1.000 16.62682 ? 69  VAL   A CA  1 
ATOM   182  C  C   . VAL   A 1 25  ? -2.28600  -21.07100 4.14700   1.000 14.66682 ? 69  VAL   A C   1 
ATOM   183  O  O   . VAL   A 1 25  ? -3.19300  -21.32400 4.94900   1.000 15.02682 ? 69  VAL   A O   1 
ATOM   184  C  CB  . VAL   A 1 25  ? -1.25900  -18.84000 4.71200   1.000 15.61682 ? 69  VAL   A CB  1 
ATOM   185  C  CG1 . VAL   A 1 25  ? 0.07300   -19.52000 5.03600   1.000 12.54682 ? 69  VAL   A CG1 1 
ATOM   186  C  CG2 . VAL   A 1 25  ? -1.01600  -17.41800 4.22200   1.000 12.63682 ? 69  VAL   A CG2 1 
ATOM   187  N  N   . ALA   A 1 26  ? -1.46100  -21.99600 3.66300   1.000 15.30682 ? 70  ALA   A N   1 
ATOM   188  C  CA  . ALA   A 1 26  ? -1.38900  -23.35600 4.17800   1.000 16.90682 ? 70  ALA   A CA  1 
ATOM   189  C  C   . ALA   A 1 26  ? 0.03400   -23.62600 4.65300   1.000 14.49682 ? 70  ALA   A C   1 
ATOM   190  O  O   . ALA   A 1 26  ? 0.97100   -22.89700 4.31000   1.000 10.66682 ? 70  ALA   A O   1 
ATOM   191  C  CB  . ALA   A 1 26  ? -1.80000  -24.38500 3.11500   1.000 17.74682 ? 70  ALA   A CB  1 
ATOM   192  N  N   . THR   A 1 27  ? 0.19800   -24.68300 5.44600   1.000 15.64682 ? 71  THR   A N   1 
ATOM   193  C  CA  . THR   A 1 27  ? 1.47100   -24.94600 6.10300   1.000 14.14682 ? 71  THR   A CA  1 
ATOM   194  C  C   . THR   A 1 27  ? 1.90400   -26.39600 5.93900   1.000 17.70682 ? 71  THR   A C   1 
ATOM   195  O  O   . THR   A 1 27  ? 1.11200   -27.28500 5.61600   1.000 16.19682 ? 71  THR   A O   1 
ATOM   196  C  CB  . THR   A 1 27  ? 1.43000   -24.61800 7.60200   1.000 19.95682 ? 71  THR   A CB  1 
ATOM   197  O  OG1 . THR   A 1 27  ? 0.49700   -25.48500 8.26100   1.000 17.45682 ? 71  THR   A OG1 1 
ATOM   198  C  CG2 . THR   A 1 27  ? 1.03500   -23.15600 7.83100   1.000 17.46682 ? 71  THR   A CG2 1 
ATOM   199  N  N   . GLU   A 1 28  ? 3.18300   -26.61800 6.22300   1.000 16.20682 ? 72  GLU   A N   1 
ATOM   200  C  CA  . GLU   A 1 28  ? 3.82400   -27.92100 6.13000   1.000 15.38682 ? 72  GLU   A CA  1 
ATOM   201  C  C   . GLU   A 1 28  ? 4.93500   -27.96900 7.16900   1.000 16.95682 ? 72  GLU   A C   1 
ATOM   202  O  O   . GLU   A 1 28  ? 5.74700   -27.04500 7.23700   1.000 13.88682 ? 72  GLU   A O   1 
ATOM   203  C  CB  . GLU   A 1 28  ? 4.40000   -28.13200 4.73300   1.000 15.69682 ? 72  GLU   A CB  1 
ATOM   204  C  CG  . GLU   A 1 28  ? 4.23500   -29.50400 4.18500   1.000 25.52682 ? 72  GLU   A CG  1 
ATOM   205  C  CD  . GLU   A 1 28  ? 4.94400   -29.66200 2.85900   1.000 30.51682 ? 72  GLU   A CD  1 
ATOM   206  O  OE1 . GLU   A 1 28  ? 6.15100   -29.98300 2.87000   1.000 40.06682 ? 72  GLU   A OE1 1 
ATOM   207  O  OE2 . GLU   A 1 28  ? 4.30200   -29.44600 1.81100   1.000 31.46682 ? 72  GLU   A OE2 1 
ATOM   208  N  N   . ARG   A 1 29  ? 4.98200   -29.02500 7.97200   1.000 13.91682 ? 73  ARG   A N   1 
ATOM   209  C  CA  . ARG   A 1 29  ? 6.03700   -29.16900 8.97000   1.000 15.41682 ? 73  ARG   A CA  1 
ATOM   210  C  C   . ARG   A 1 29  ? 7.15400   -30.02700 8.39500   1.000 17.77682 ? 73  ARG   A C   1 
ATOM   211  O  O   . ARG   A 1 29  ? 6.89300   -31.09700 7.83900   1.000 16.52682 ? 73  ARG   A O   1 
ATOM   212  C  CB  . ARG   A 1 29  ? 5.50000   -29.79200 10.26200  1.000 16.38682 ? 73  ARG   A CB  1 
ATOM   213  C  CG  . ARG   A 1 29  ? 4.18000   -29.19800 10.74200  1.000 27.91682 ? 73  ARG   A CG  1 
ATOM   214  C  CD  . ARG   A 1 29  ? 4.37000   -27.88200 11.49500  1.000 32.88682 ? 73  ARG   A CD  1 
ATOM   215  N  NE  . ARG   A 1 29  ? 3.20400   -27.00700 11.38400  1.000 43.16682 ? 73  ARG   A NE  1 
ATOM   216  C  CZ  . ARG   A 1 29  ? 2.10500   -27.10700 12.12300  1.000 49.94682 ? 73  ARG   A CZ  1 
ATOM   217  N  NH1 . ARG   A 1 29  ? 1.97100   -28.05300 13.04100  1.000 50.75682 ? 73  ARG   A NH1 1 
ATOM   218  N  NH2 . ARG   A 1 29  ? 1.11300   -26.23900 11.93100  1.000 37.23682 ? 73  ARG   A NH2 1 
ATOM   219  N  N   . VAL   A 1 30  ? 8.39500   -29.56600 8.53700   1.000 13.71682 ? 74  VAL   A N   1 
ATOM   220  C  CA  . VAL   A 1 30  ? 9.57200   -30.29000 8.06200   1.000 13.26682 ? 74  VAL   A CA  1 
ATOM   221  C  C   . VAL   A 1 30  ? 10.34300  -30.79800 9.27100   1.000 12.88682 ? 74  VAL   A C   1 
ATOM   222  O  O   . VAL   A 1 30  ? 10.76200  -30.00500 10.12700  1.000 13.32682 ? 74  VAL   A O   1 
ATOM   223  C  CB  . VAL   A 1 30  ? 10.45900  -29.40900 7.17100   1.000 13.61682 ? 74  VAL   A CB  1 
ATOM   224  C  CG1 . VAL   A 1 30  ? 11.77300  -30.12000 6.86300   1.000 13.84682 ? 74  VAL   A CG1 1 
ATOM   225  C  CG2 . VAL   A 1 30  ? 9.71400   -29.05200 5.87500   1.000 16.08682 ? 74  VAL   A CG2 1 
ATOM   226  N  N   . SER   A 1 31  ? 10.53900  -32.11500 9.33200   1.000 12.76682 ? 75  SER   A N   1 
ATOM   227  C  CA  . SER   A 1 31  ? 11.19700  -32.73700 10.47200  1.000 11.83682 ? 75  SER   A CA  1 
ATOM   228  C  C   . SER   A 1 31  ? 12.63400  -32.25100 10.62400  1.000 11.67682 ? 75  SER   A C   1 
ATOM   229  O  O   . SER   A 1 31  ? 13.31000  -31.90300 9.64900   1.000 9.77682  ? 75  SER   A O   1 
ATOM   230  C  CB  . SER   A 1 31  ? 11.19500  -34.26500 10.32800  1.000 16.74682 ? 75  SER   A CB  1 
ATOM   231  O  OG  . SER   A 1 31  ? 11.98000  -34.86500 11.35700  1.000 12.33682 ? 75  SER   A OG  1 
ATOM   232  N  N   . SER   A 1 32  ? 13.10000  -32.24400 11.87400  1.000 8.94682  ? 76  SER   A N   1 
ATOM   233  C  CA  . SER   A 1 32  ? 14.49700  -31.95900 12.16900  1.000 11.72682 ? 76  SER   A CA  1 
ATOM   234  C  C   . SER   A 1 32  ? 15.44200  -33.02300 11.62400  1.000 13.23682 ? 76  SER   A C   1 
ATOM   235  O  O   . SER   A 1 32  ? 16.65600  -32.79700 11.62100  1.000 11.20682 ? 76  SER   A O   1 
ATOM   236  C  CB  . SER   A 1 32  ? 14.69300  -31.82800 13.67900  1.000 12.79682 ? 76  SER   A CB  1 
ATOM   237  O  OG  . SER   A 1 32  ? 14.25700  -33.01300 14.31800  1.000 17.19682 ? 76  SER   A OG  1 
ATOM   238  N  N   . PHE   A 1 33  ? 14.91600  -34.17100 11.17900  1.000 11.41682 ? 77  PHE   A N   1 
ATOM   239  C  CA  . PHE   A 1 33  ? 15.73400  -35.21900 10.57400  1.000 15.95682 ? 77  PHE   A CA  1 
ATOM   240  C  C   . PHE   A 1 33  ? 16.40700  -34.75700 9.28100   1.000 16.89682 ? 77  PHE   A C   1 
ATOM   241  O  O   . PHE   A 1 33  ? 17.41900  -35.34600 8.87900   1.000 16.53682 ? 77  PHE   A O   1 
ATOM   242  C  CB  . PHE   A 1 33  ? 14.85700  -36.44800 10.31400  1.000 18.31682 ? 77  PHE   A CB  1 
ATOM   243  C  CG  . PHE   A 1 33  ? 15.62400  -37.71300 10.00900  1.000 20.73682 ? 77  PHE   A CG  1 
ATOM   244  C  CD1 . PHE   A 1 33  ? 16.05000  -38.54400 11.03300  1.000 21.46682 ? 77  PHE   A CD1 1 
ATOM   245  C  CD2 . PHE   A 1 33  ? 15.87400  -38.09100 8.70000   1.000 18.28682 ? 77  PHE   A CD2 1 
ATOM   246  C  CE1 . PHE   A 1 33  ? 16.73900  -39.72400 10.75800  1.000 22.91682 ? 77  PHE   A CE1 1 
ATOM   247  C  CE2 . PHE   A 1 33  ? 16.56200  -39.27200 8.41100   1.000 20.55682 ? 77  PHE   A CE2 1 
ATOM   248  C  CZ  . PHE   A 1 33  ? 16.99600  -40.08500 9.44200   1.000 19.09682 ? 77  PHE   A CZ  1 
ATOM   249  N  N   . ALA   A 1 34  ? 15.88000  -33.71300 8.63700   1.000 12.96682 ? 78  ALA   A N   1 
ATOM   250  C  CA  . ALA   A 1 34  ? 16.45600  -33.20100 7.39600   1.000 19.40682 ? 78  ALA   A CA  1 
ATOM   251  C  C   . ALA   A 1 34  ? 17.90100  -32.74500 7.59300   1.000 15.18682 ? 78  ALA   A C   1 
ATOM   252  O  O   . ALA   A 1 34  ? 18.25600  -32.17700 8.62800   1.000 16.78682 ? 78  ALA   A O   1 
ATOM   253  C  CB  . ALA   A 1 34  ? 15.61400  -32.03800 6.87100   1.000 20.02682 ? 78  ALA   A CB  1 
ATOM   254  N  N   . SER   A 1 35  ? 18.74600  -32.99500 6.59100   1.000 16.41682 ? 79  SER   A N   1 
ATOM   255  C  CA  . SER   A 1 35  ? 20.15600  -32.64100 6.70900   1.000 16.79682 ? 79  SER   A CA  1 
ATOM   256  C  C   . SER   A 1 35  ? 20.37400  -31.15000 6.46400   1.000 20.94682 ? 79  SER   A C   1 
ATOM   257  O  O   . SER   A 1 35  ? 19.72500  -30.53700 5.60700   1.000 20.78682 ? 79  SER   A O   1 
ATOM   258  C  CB  . SER   A 1 35  ? 21.00100  -33.45300 5.72600   1.000 16.85682 ? 79  SER   A CB  1 
ATOM   259  O  OG  . SER   A 1 35  ? 20.55600  -33.24800 4.39600   1.000 21.03682 ? 79  SER   A OG  1 
ATOM   260  N  N   . GLY   A 1 36  ? 21.30200  -30.56800 7.21800   1.000 16.79682 ? 80  GLY   A N   1 
ATOM   261  C  CA  . GLY   A 1 36  ? 21.73800  -29.21100 6.97200   1.000 20.82682 ? 80  GLY   A CA  1 
ATOM   262  C  C   . GLY   A 1 36  ? 21.09400  -28.14600 7.83700   1.000 14.79682 ? 80  GLY   A C   1 
ATOM   263  O  O   . GLY   A 1 36  ? 21.56600  -27.00200 7.82200   1.000 15.82682 ? 80  GLY   A O   1 
ATOM   264  N  N   . PHE   A 1 37  ? 20.02800  -28.47100 8.56400   1.000 13.94682 ? 81  PHE   A N   1 
ATOM   265  C  CA  . PHE   A 1 37  ? 19.36900  -27.52000 9.46300   1.000 11.83682 ? 81  PHE   A CA  1 
ATOM   266  C  C   . PHE   A 1 37  ? 18.41100  -28.31000 10.35200  1.000 12.60682 ? 81  PHE   A C   1 
ATOM   267  O  O   . PHE   A 1 37  ? 18.27700  -29.52800 10.21800  1.000 9.95682  ? 81  PHE   A O   1 
ATOM   268  C  CB  . PHE   A 1 37  ? 18.66400  -26.40000 8.68300   1.000 10.10682 ? 81  PHE   A CB  1 
ATOM   269  C  CG  . PHE   A 1 37  ? 17.50500  -26.86000 7.83800   1.000 9.72682  ? 81  PHE   A CG  1 
ATOM   270  C  CD1 . PHE   A 1 37  ? 17.70500  -27.64400 6.70500   1.000 13.46682 ? 81  PHE   A CD1 1 
ATOM   271  C  CD2 . PHE   A 1 37  ? 16.21800  -26.48000 8.15300   1.000 11.12682 ? 81  PHE   A CD2 1 
ATOM   272  C  CE1 . PHE   A 1 37  ? 16.63200  -28.05600 5.93100   1.000 11.36682 ? 81  PHE   A CE1 1 
ATOM   273  C  CE2 . PHE   A 1 37  ? 15.13800  -26.88600 7.37600   1.000 10.77682 ? 81  PHE   A CE2 1 
ATOM   274  C  CZ  . PHE   A 1 37  ? 15.34500  -27.66700 6.26900   1.000 10.23682 ? 81  PHE   A CZ  1 
ATOM   275  N  N   . GLY   A 1 38  ? 17.73100  -27.61100 11.26100  1.000 13.17682 ? 82  GLY   A N   1 
ATOM   276  C  CA  . GLY   A 1 38  ? 16.89600  -28.31600 12.21900  1.000 10.84682 ? 82  GLY   A CA  1 
ATOM   277  C  C   . GLY   A 1 38  ? 15.42900  -28.49000 11.85300  1.000 11.14682 ? 82  GLY   A C   1 
ATOM   278  O  O   . GLY   A 1 38  ? 14.60000  -28.67600 12.74700  1.000 12.09682 ? 82  GLY   A O   1 
ATOM   279  N  N   . GLY   A 1 39  ? 15.08200  -28.43100 10.56400  1.000 7.85682  ? 83  GLY   A N   1 
ATOM   280  C  CA  . GLY   A 1 39  ? 13.68800  -28.50300 10.17300  1.000 9.37682  ? 83  GLY   A CA  1 
ATOM   281  C  C   . GLY   A 1 39  ? 13.00200  -27.15800 10.37400  1.000 10.83682 ? 83  GLY   A C   1 
ATOM   282  O  O   . GLY   A 1 39  ? 13.64800  -26.14200 10.62100  1.000 9.52682  ? 83  GLY   A O   1 
ATOM   283  N  N   . GLY   A 1 40  ? 11.67700  -27.16000 10.25400  1.000 13.03682 ? 84  GLY   A N   1 
ATOM   284  C  CA  . GLY   A 1 40  ? 10.91600  -25.93200 10.41600  1.000 10.07682 ? 84  GLY   A CA  1 
ATOM   285  C  C   . GLY   A 1 40  ? 9.49300   -26.08500 9.90700   1.000 14.44682 ? 84  GLY   A C   1 
ATOM   286  O  O   . GLY   A 1 40  ? 8.98400   -27.20200 9.75200   1.000 11.28682 ? 84  GLY   A O   1 
ATOM   287  N  N   . THR   A 1 41  ? 8.86100   -24.93700 9.65500   1.000 8.82682  ? 85  THR   A N   1 
ATOM   288  C  CA  . THR   A 1 41  ? 7.48700   -24.86800 9.17100   1.000 7.29682  ? 85  THR   A CA  1 
ATOM   289  C  C   . THR   A 1 41  ? 7.47100   -24.05000 7.88800   1.000 7.68682  ? 85  THR   A C   1 
ATOM   290  O  O   . THR   A 1 41  ? 8.00700   -22.93900 7.86100   1.000 10.42682 ? 85  THR   A O   1 
ATOM   291  C  CB  . THR   A 1 41  ? 6.54800   -24.21300 10.20500  1.000 12.15682 ? 85  THR   A CB  1 
ATOM   292  O  OG1 . THR   A 1 41  ? 6.61400   -24.90100 11.46300  1.000 11.35682 ? 85  THR   A OG1 1 
ATOM   293  C  CG2 . THR   A 1 41  ? 5.11700   -24.22700 9.70100   1.000 10.00682 ? 85  THR   A CG2 1 
ATOM   294  N  N   . ILE   A 1 42  ? 6.87900   -24.59300 6.82500   1.000 8.31682  ? 86  ILE   A N   1 
ATOM   295  C  CA  . ILE   A 1 42  ? 6.71600   -23.86600 5.56600   1.000 7.78682  ? 86  ILE   A CA  1 
ATOM   296  C  C   . ILE   A 1 42  ? 5.32900   -23.24000 5.53200   1.000 8.70682  ? 86  ILE   A C   1 
ATOM   297  O  O   . ILE   A 1 42  ? 4.32900   -23.92600 5.75900   1.000 13.29682 ? 86  ILE   A O   1 
ATOM   298  C  CB  . ILE   A 1 42  ? 6.92700   -24.78600 4.35100   1.000 6.60682  ? 86  ILE   A CB  1 
ATOM   299  C  CG1 . ILE   A 1 42  ? 8.32900   -25.40200 4.38900   1.000 10.44682 ? 86  ILE   A CG1 1 
ATOM   300  C  CG2 . ILE   A 1 42  ? 6.72800   -23.99900 3.06400   1.000 6.61682  ? 86  ILE   A CG2 1 
ATOM   301  C  CD1 . ILE   A 1 42  ? 8.53700   -26.49900 3.37100   1.000 13.04682 ? 86  ILE   A CD1 1 
ATOM   302  N  N   . TYR   A 1 43  ? 5.26400   -21.94200 5.24900   1.000 9.38682  ? 87  TYR   A N   1 
ATOM   303  C  CA  . TYR   A 1 43  ? 4.00500   -21.23200 5.03100   1.000 9.25682  ? 87  TYR   A CA  1 
ATOM   304  C  C   . TYR   A 1 43  ? 3.93000   -20.82000 3.56700   1.000 12.46682 ? 87  TYR   A C   1 
ATOM   305  O  O   . TYR   A 1 43  ? 4.80000   -20.08200 3.09600   1.000 10.16682 ? 87  TYR   A O   1 
ATOM   306  C  CB  . TYR   A 1 43  ? 3.91000   -19.98600 5.91700   1.000 10.24682 ? 87  TYR   A CB  1 
ATOM   307  C  CG  . TYR   A 1 43  ? 3.99400   -20.22300 7.40500   1.000 12.27682 ? 87  TYR   A CG  1 
ATOM   308  C  CD1 . TYR   A 1 43  ? 5.22000   -20.38800 8.03900   1.000 10.79682 ? 87  TYR   A CD1 1 
ATOM   309  C  CD2 . TYR   A 1 43  ? 2.84400   -20.25300 8.18400   1.000 12.77682 ? 87  TYR   A CD2 1 
ATOM   310  C  CE1 . TYR   A 1 43  ? 5.29300   -20.59100 9.40600   1.000 7.87682  ? 87  TYR   A CE1 1 
ATOM   311  C  CE2 . TYR   A 1 43  ? 2.90800   -20.45500 9.54300   1.000 15.90682 ? 87  TYR   A CE2 1 
ATOM   312  C  CZ  . TYR   A 1 43  ? 4.13300   -20.61800 10.14900  1.000 12.91682 ? 87  TYR   A CZ  1 
ATOM   313  O  OH  . TYR   A 1 43  ? 4.19200   -20.82400 11.50100  1.000 11.24682 ? 87  TYR   A OH  1 
ATOM   314  N  N   . TYR   A 1 44  ? 2.89000   -21.26500 2.85300   1.000 10.02682 ? 88  TYR   A N   1 
ATOM   315  C  CA  . TYR   A 1 44  ? 2.81300   -20.90600 1.44000   1.000 13.14682 ? 88  TYR   A CA  1 
ATOM   316  C  C   . TYR   A 1 44  ? 1.43800   -20.37400 1.05900   1.000 13.06682 ? 88  TYR   A C   1 
ATOM   317  O  O   . TYR   A 1 44  ? 0.43100   -20.70200 1.70200   1.000 12.24682 ? 88  TYR   A O   1 
ATOM   318  C  CB  . TYR   A 1 44  ? 3.16600   -22.09500 0.53400   1.000 14.08682 ? 88  TYR   A CB  1 
ATOM   319  C  CG  . TYR   A 1 44  ? 2.32300   -23.34300 0.71700   1.000 10.09682 ? 88  TYR   A CG  1 
ATOM   320  C  CD1 . TYR   A 1 44  ? 2.61300   -24.26400 1.72000   1.000 12.10682 ? 88  TYR   A CD1 1 
ATOM   321  C  CD2 . TYR   A 1 44  ? 1.24900   -23.60400 -0.12600  1.000 14.59682 ? 88  TYR   A CD2 1 
ATOM   322  C  CE1 . TYR   A 1 44  ? 1.84000   -25.41900 1.88000   1.000 13.28682 ? 88  TYR   A CE1 1 
ATOM   323  C  CE2 . TYR   A 1 44  ? 0.47300   -24.75000 0.01600   1.000 10.20682 ? 88  TYR   A CE2 1 
ATOM   324  C  CZ  . TYR   A 1 44  ? 0.77300   -25.65200 1.01600   1.000 20.20682 ? 88  TYR   A CZ  1 
ATOM   325  O  OH  . TYR   A 1 44  ? -0.00400  -26.78100 1.15100   1.000 18.24682 ? 88  TYR   A OH  1 
ATOM   326  N  N   . PRO   A 1 45  ? 1.37200   -19.53000 0.02600   1.000 10.40682 ? 89  PRO   A N   1 
ATOM   327  C  CA  . PRO   A 1 45  ? 0.06400   -19.10500 -0.49000  1.000 12.22682 ? 89  PRO   A CA  1 
ATOM   328  C  C   . PRO   A 1 45  ? -0.61800  -20.22000 -1.27000  1.000 14.99682 ? 89  PRO   A C   1 
ATOM   329  O  O   . PRO   A 1 45  ? 0.00100   -20.90400 -2.09000  1.000 15.30682 ? 89  PRO   A O   1 
ATOM   330  C  CB  . PRO   A 1 45  ? 0.40200   -17.91400 -1.40000  1.000 10.94682 ? 89  PRO   A CB  1 
ATOM   331  C  CG  . PRO   A 1 45  ? 1.79700   -17.49300 -1.00000  1.000 14.67682 ? 89  PRO   A CG  1 
ATOM   332  C  CD  . PRO   A 1 45  ? 2.47200   -18.77000 -0.58500  1.000 12.98682 ? 89  PRO   A CD  1 
ATOM   333  N  N   . ARG   A 1 46  ? -1.92200  -20.36800 -1.03200  1.000 17.01682 ? 90  ARG   A N   1 
ATOM   334  C  CA  . ARG   A 1 46  ? -2.68800  -21.45100 -1.63700  1.000 19.23682 ? 90  ARG   A CA  1 
ATOM   335  C  C   . ARG   A 1 46  ? -3.03800  -21.17100 -3.10200  1.000 17.58682 ? 90  ARG   A C   1 
ATOM   336  O  O   . ARG   A 1 46  ? -3.02500  -22.08900 -3.92700  1.000 16.67682 ? 90  ARG   A O   1 
ATOM   337  C  CB  . ARG   A 1 46  ? -3.95000  -21.69900 -0.80000  1.000 20.28682 ? 90  ARG   A CB  1 
ATOM   338  C  CG  . ARG   A 1 46  ? -3.63000  -22.18200 0.60900   1.000 20.38682 ? 90  ARG   A CG  1 
ATOM   339  C  CD  . ARG   A 1 46  ? -4.83100  -22.16200 1.55500   1.000 24.71682 ? 90  ARG   A CD  1 
ATOM   340  N  NE  . ARG   A 1 46  ? -5.83700  -23.15400 1.20100   1.000 27.09682 ? 90  ARG   A NE  1 
ATOM   341  C  CZ  . ARG   A 1 46  ? -6.90400  -22.90000 0.45500   1.000 30.14682 ? 90  ARG   A CZ  1 
ATOM   342  N  NH1 . ARG   A 1 46  ? -7.14900  -21.68500 -0.00800  1.000 34.25682 ? 90  ARG   A NH1 1 
ATOM   343  N  NH2 . ARG   A 1 46  ? -7.74500  -23.89000 0.16600   1.000 31.58682 ? 90  ARG   A NH2 1 
ATOM   344  N  N   . GLU   A 1 47  ? -3.33100  -19.91800 -3.45000  1.000 14.86682 ? 91  GLU   A N   1 
ATOM   345  C  CA  . GLU   A 1 47  ? -3.83300  -19.57900 -4.78000  1.000 18.60682 ? 91  GLU   A CA  1 
ATOM   346  C  C   . GLU   A 1 47  ? -2.71500  -19.55800 -5.81800  1.000 17.79682 ? 91  GLU   A C   1 
ATOM   347  O  O   . GLU   A 1 47  ? -1.67100  -18.93200 -5.60600  1.000 18.91682 ? 91  GLU   A O   1 
ATOM   348  C  CB  . GLU   A 1 47  ? -4.53500  -18.21900 -4.74200  1.000 20.05682 ? 91  GLU   A CB  1 
ATOM   349  C  CG  . GLU   A 1 47  ? -5.82100  -18.18900 -3.92300  1.000 18.09682 ? 91  GLU   A CG  1 
ATOM   350  C  CD  . GLU   A 1 47  ? -5.59400  -17.85500 -2.45200  1.000 24.92682 ? 91  GLU   A CD  1 
ATOM   351  O  OE1 . GLU   A 1 47  ? -4.42100  -17.72000 -2.03000  1.000 18.87682 ? 91  GLU   A OE1 1 
ATOM   352  O  OE2 . GLU   A 1 47  ? -6.59900  -17.73100 -1.71200  1.000 23.59682 ? 91  GLU   A OE2 1 
ATOM   353  N  N   . THR   A 1 48  ? -2.95400  -20.20400 -6.96800  1.000 15.46682 ? 92  THR   A N   1 
ATOM   354  C  CA  . THR   A 1 48  ? -1.93000  -20.37500 -7.99300  1.000 16.66682 ? 92  THR   A CA  1 
ATOM   355  C  C   . THR   A 1 48  ? -2.21100  -19.62300 -9.29200  1.000 18.07682 ? 92  THR   A C   1 
ATOM   356  O  O   . THR   A 1 48  ? -1.35800  -19.63300 -10.18900 1.000 19.61682 ? 92  THR   A O   1 
ATOM   357  C  CB  . THR   A 1 48  ? -1.73000  -21.87000 -8.30300  1.000 19.56682 ? 92  THR   A CB  1 
ATOM   358  O  OG1 . THR   A 1 48  ? -2.94100  -22.41800 -8.83600  1.000 22.70682 ? 92  THR   A OG1 1 
ATOM   359  C  CG2 . THR   A 1 48  ? -1.34500  -22.64500 -7.03200  1.000 14.70682 ? 92  THR   A CG2 1 
ATOM   360  N  N   . ASP   A 1 49  ? -3.35300  -18.94000 -9.41600  1.000 19.15682 ? 93  ASP   A N   1 
ATOM   361  C  CA  . ASP   A 1 49  ? -3.72400  -18.36200 -10.71000 1.000 23.23682 ? 93  ASP   A CA  1 
ATOM   362  C  C   . ASP   A 1 49  ? -2.85200  -17.17700 -11.12800 1.000 20.19682 ? 93  ASP   A C   1 
ATOM   363  O  O   . ASP   A 1 49  ? -2.88300  -16.79600 -12.30400 1.000 20.14682 ? 93  ASP   A O   1 
ATOM   364  C  CB  . ASP   A 1 49  ? -5.20000  -17.94200 -10.71800 1.000 24.54682 ? 93  ASP   A CB  1 
ATOM   365  C  CG  . ASP   A 1 49  ? -5.72000  -17.57300 -9.33700  1.000 33.44682 ? 93  ASP   A CG  1 
ATOM   366  O  OD1 . ASP   A 1 49  ? -5.13200  -18.01100 -8.32300  1.000 34.94682 ? 93  ASP   A OD1 1 
ATOM   367  O  OD2 . ASP   A 1 49  ? -6.74300  -16.85900 -9.26700  1.000 42.67682 ? 93  ASP   A OD2 1 
ATOM   368  N  N   . GLU   A 1 50  ? -2.07600  -16.59200 -10.21600 1.000 20.06682 ? 94  GLU   A N   1 
ATOM   369  C  CA  . GLU   A 1 50  ? -1.19700  -15.47800 -10.56700 1.000 19.10682 ? 94  GLU   A CA  1 
ATOM   370  C  C   . GLU   A 1 50  ? 0.25100   -15.89600 -10.81600 1.000 21.73682 ? 94  GLU   A C   1 
ATOM   371  O  O   . GLU   A 1 50  ? 1.06300   -15.04600 -11.19700 1.000 20.18682 ? 94  GLU   A O   1 
ATOM   372  C  CB  . GLU   A 1 50  ? -1.23700  -14.39700 -9.48000  1.000 18.94682 ? 94  GLU   A CB  1 
ATOM   373  C  CG  . GLU   A 1 50  ? -2.63400  -13.85600 -9.18400  1.000 19.96682 ? 94  GLU   A CG  1 
ATOM   374  C  CD  . GLU   A 1 50  ? -2.63200  -12.66700 -8.21600  1.000 27.58682 ? 94  GLU   A CD  1 
ATOM   375  O  OE1 . GLU   A 1 50  ? -1.72100  -11.81000 -8.30700  1.000 19.99682 ? 94  GLU   A OE1 1 
ATOM   376  O  OE2 . GLU   A 1 50  ? -3.54800  -12.58900 -7.36300  1.000 28.71682 ? 94  GLU   A OE2 1 
ATOM   377  N  N   . GLY   A 1 51  ? 0.60000   -17.16400 -10.61000 1.000 13.79682 ? 95  GLY   A N   1 
ATOM   378  C  CA  . GLY   A 1 51  ? 1.93900   -17.65800 -10.88400 1.000 13.15682 ? 95  GLY   A CA  1 
ATOM   379  C  C   . GLY   A 1 51  ? 2.64900   -18.11000 -9.62000  1.000 14.44682 ? 95  GLY   A C   1 
ATOM   380  O  O   . GLY   A 1 51  ? 2.06600   -18.17400 -8.53400  1.000 15.30682 ? 95  GLY   A O   1 
ATOM   381  N  N   . THR   A 1 52  ? 3.93500   -18.44100 -9.77700  1.000 13.14682 ? 96  THR   A N   1 
ATOM   382  C  CA  . THR   A 1 52  ? 4.76300   -18.90400 -8.67000  1.000 11.64682 ? 96  THR   A CA  1 
ATOM   383  C  C   . THR   A 1 52  ? 5.22600   -17.73200 -7.79900  1.000 13.45682 ? 96  THR   A C   1 
ATOM   384  O  O   . THR   A 1 52  ? 5.06600   -16.55600 -8.14700  1.000 13.29682 ? 96  THR   A O   1 
ATOM   385  C  CB  . THR   A 1 52  ? 5.97300   -19.69300 -9.18700  1.000 11.94682 ? 96  THR   A CB  1 
ATOM   386  O  OG1 . THR   A 1 52  ? 6.67600   -18.92400 -10.18000 1.000 12.66682 ? 96  THR   A OG1 1 
ATOM   387  C  CG2 . THR   A 1 52  ? 5.52800   -21.02800 -9.76700  1.000 12.13682 ? 96  THR   A CG2 1 
ATOM   388  N  N   . PHE   A 1 53  ? 5.81900   -18.07600 -6.65100  1.000 10.48682 ? 97  PHE   A N   1 
ATOM   389  C  CA  . PHE   A 1 53  ? 6.21500   -17.11100 -5.63000  1.000 9.02682  ? 97  PHE   A CA  1 
ATOM   390  C  C   . PHE   A 1 53  ? 7.68200   -17.27800 -5.24700  1.000 12.04682 ? 97  PHE   A C   1 
ATOM   391  O  O   . PHE   A 1 53  ? 8.25600   -18.36500 -5.36900  1.000 12.69682 ? 97  PHE   A O   1 
ATOM   392  C  CB  . PHE   A 1 53  ? 5.37700   -17.26900 -4.37000  1.000 11.31682 ? 97  PHE   A CB  1 
ATOM   393  C  CG  . PHE   A 1 53  ? 3.91900   -17.01400 -4.57500  1.000 10.52682 ? 97  PHE   A CG  1 
ATOM   394  C  CD1 . PHE   A 1 53  ? 3.41700   -15.73800 -4.47900  1.000 7.64682  ? 97  PHE   A CD1 1 
ATOM   395  C  CD2 . PHE   A 1 53  ? 3.04900   -18.05400 -4.85400  1.000 13.90682 ? 97  PHE   A CD2 1 
ATOM   396  C  CE1 . PHE   A 1 53  ? 2.06600   -15.49400 -4.64800  1.000 12.74682 ? 97  PHE   A CE1 1 
ATOM   397  C  CE2 . PHE   A 1 53  ? 1.69400   -17.81500 -5.03300  1.000 12.32682 ? 97  PHE   A CE2 1 
ATOM   398  C  CZ  . PHE   A 1 53  ? 1.20600   -16.54000 -4.92900  1.000 13.71682 ? 97  PHE   A CZ  1 
ATOM   399  N  N   . GLY   A 1 54  ? 8.29700   -16.16900 -4.76900  1.000 10.51682 ? 98  GLY   A N   1 
ATOM   400  C  CA  . GLY   A 1 54  ? 9.60400   -16.26300 -4.15400  1.000 7.39682  ? 98  GLY   A CA  1 
ATOM   401  C  C   . GLY   A 1 54  ? 9.50200   -16.80400 -2.73800  1.000 10.11682 ? 98  GLY   A C   1 
ATOM   402  O  O   . GLY   A 1 54  ? 8.41000   -17.00200 -2.20200  1.000 10.06682 ? 98  GLY   A O   1 
ATOM   403  N  N   . ALA   A 1 55  ? 10.65600  -17.04900 -2.12100  1.000 8.36682  ? 99  ALA   A N   1 
ATOM   404  C  CA  . ALA   A 1 55  ? 10.69500  -17.61000 -0.77100  1.000 7.56682  ? 99  ALA   A CA  1 
ATOM   405  C  C   . ALA   A 1 55  ? 11.68800  -16.85000 0.10300   1.000 13.27682 ? 99  ALA   A C   1 
ATOM   406  O  O   . ALA   A 1 55  ? 12.66900  -16.28600 -0.39200  1.000 10.37682 ? 99  ALA   A O   1 
ATOM   407  C  CB  . ALA   A 1 55  ? 11.06400  -19.09700 -0.79900  1.000 7.63682  ? 99  ALA   A CB  1 
ATOM   408  N  N   . VAL   A 1 56  ? 11.42300  -16.84500 1.41400   1.000 8.50682  ? 100 VAL   A N   1 
ATOM   409  C  CA  . VAL   A 1 56  ? 12.33300  -16.28700 2.41200   1.000 10.19682 ? 100 VAL   A CA  1 
ATOM   410  C  C   . VAL   A 1 56  ? 12.49600  -17.30000 3.54200   1.000 7.89682  ? 100 VAL   A C   1 
ATOM   411  O  O   . VAL   A 1 56  ? 11.50200  -17.78800 4.09000   1.000 8.81682  ? 100 VAL   A O   1 
ATOM   412  C  CB  . VAL   A 1 56  ? 11.83400  -14.92500 2.95200   1.000 10.60682 ? 100 VAL   A CB  1 
ATOM   413  C  CG1 . VAL   A 1 56  ? 10.44100  -15.03100 3.57700   1.000 11.43682 ? 100 VAL   A CG1 1 
ATOM   414  C  CG2 . VAL   A 1 56  ? 12.84000  -14.31900 3.94200   1.000 10.41682 ? 100 VAL   A CG2 1 
ATOM   415  N  N   . ALA   A 1 57  ? 13.74700  -17.64900 3.86300   1.000 7.29682  ? 101 ALA   A N   1 
ATOM   416  C  CA  . ALA   A 1 57  ? 14.05200  -18.45000 5.05200   1.000 9.07682  ? 101 ALA   A CA  1 
ATOM   417  C  C   . ALA   A 1 57  ? 14.27900  -17.54100 6.26000   1.000 8.96682  ? 101 ALA   A C   1 
ATOM   418  O  O   . ALA   A 1 57  ? 14.91000  -16.48700 6.14400   1.000 10.79682 ? 101 ALA   A O   1 
ATOM   419  C  CB  . ALA   A 1 57  ? 15.29000  -19.31600 4.81400   1.000 7.25682  ? 101 ALA   A CB  1 
ATOM   420  N  N   . VAL   A 1 58  ? 13.79000  -17.96200 7.43000   1.000 9.43682  ? 102 VAL   A N   1 
ATOM   421  C  CA  . VAL   A 1 58  ? 13.71500  -17.09100 8.60500   1.000 6.84682  ? 102 VAL   A CA  1 
ATOM   422  C  C   . VAL   A 1 58  ? 14.36300  -17.79000 9.80200   1.000 9.95682  ? 102 VAL   A C   1 
ATOM   423  O  O   . VAL   A 1 58  ? 13.86200  -18.82300 10.26300  1.000 7.64682  ? 102 VAL   A O   1 
ATOM   424  C  CB  . VAL   A 1 58  ? 12.25600  -16.70600 8.90900   1.000 7.36682  ? 102 VAL   A CB  1 
ATOM   425  C  CG1 . VAL   A 1 58  ? 12.18000  -15.74300 10.08500  1.000 8.19682  ? 102 VAL   A CG1 1 
ATOM   426  C  CG2 . VAL   A 1 58  ? 11.60900  -16.09000 7.65600   1.000 8.47682  ? 102 VAL   A CG2 1 
ATOM   427  N  N   . ALA   A 1 59  ? 15.48900  -17.19300 10.34700  1.000 7.02682  ? 103 ALA   A N   1 
ATOM   428  C  CA  . ALA   A 1 59  ? 16.21700  -17.86000 11.44000  1.000 10.80682 ? 103 ALA   A CA  1 
ATOM   429  C  C   . ALA   A 1 59  ? 15.98500  -17.17600 12.78900  1.000 8.84682  ? 103 ALA   A C   1 
ATOM   430  O  O   . ALA   A 1 59  ? 15.82600  -15.95000 12.86000  1.000 9.95682  ? 103 ALA   A O   1 
ATOM   431  C  CB  . ALA   A 1 59  ? 17.73000  -17.89800 11.16700  1.000 9.50682  ? 103 ALA   A CB  1 
ATOM   432  N  N   . PRO   A 1 60  ? 15.97800  -17.94800 13.89100  1.000 8.42682  ? 104 PRO   A N   1 
ATOM   433  C  CA  . PRO   A 1 60  ? 15.86100  -17.34100 15.22500  1.000 9.44682  ? 104 PRO   A CA  1 
ATOM   434  C  C   . PRO   A 1 60  ? 17.23400  -16.99900 15.78200  1.000 11.39682 ? 104 PRO   A C   1 
ATOM   435  O  O   . PRO   A 1 60  ? 18.24200  -17.21000 15.09600  1.000 10.18682 ? 104 PRO   A O   1 
ATOM   436  C  CB  . PRO   A 1 60  ? 15.18300  -18.44700 16.04500  1.000 11.53682 ? 104 PRO   A CB  1 
ATOM   437  C  CG  . PRO   A 1 60  ? 15.77100  -19.73200 15.43300  1.000 12.18682 ? 104 PRO   A CG  1 
ATOM   438  C  CD  . PRO   A 1 60  ? 16.06900  -19.42200 13.96700  1.000 11.89682 ? 104 PRO   A CD  1 
ATOM   439  N  N   . GLY   A 1 61  ? 17.28700  -16.48900 17.01600  1.000 9.22682  ? 105 GLY   A N   1 
ATOM   440  C  CA  . GLY   A 1 61  ? 18.53000  -16.10100 17.64500  1.000 7.70682  ? 105 GLY   A CA  1 
ATOM   441  C  C   . GLY   A 1 61  ? 19.08000  -17.16200 18.58400  1.000 12.63682 ? 105 GLY   A C   1 
ATOM   442  O  O   . GLY   A 1 61  ? 18.56600  -18.28000 18.69400  1.000 11.56682 ? 105 GLY   A O   1 
ATOM   443  N  N   . PHE   A 1 62  ? 20.15300  -16.78000 19.27800  1.000 11.12682 ? 106 PHE   A N   1 
ATOM   444  C  CA  . PHE   A 1 62  ? 20.86100  -17.65700 20.20500  1.000 11.75682 ? 106 PHE   A CA  1 
ATOM   445  C  C   . PHE   A 1 62  ? 19.93300  -18.09400 21.33200  1.000 16.25682 ? 106 PHE   A C   1 
ATOM   446  O  O   . PHE   A 1 62  ? 19.22600  -17.27200 21.92000  1.000 15.13682 ? 106 PHE   A O   1 
ATOM   447  C  CB  . PHE   A 1 62  ? 22.07200  -16.90400 20.76200  1.000 11.76682 ? 106 PHE   A CB  1 
ATOM   448  C  CG  . PHE   A 1 62  ? 23.11200  -17.76300 21.44900  1.000 14.94682 ? 106 PHE   A CG  1 
ATOM   449  C  CD1 . PHE   A 1 62  ? 23.83700  -18.71600 20.74700  1.000 17.04682 ? 106 PHE   A CD1 1 
ATOM   450  C  CD2 . PHE   A 1 62  ? 23.43600  -17.53400 22.77500  1.000 16.42682 ? 106 PHE   A CD2 1 
ATOM   451  C  CE1 . PHE   A 1 62  ? 24.82900  -19.45800 21.37800  1.000 19.01682 ? 106 PHE   A CE1 1 
ATOM   452  C  CE2 . PHE   A 1 62  ? 24.42900  -18.26300 23.40800  1.000 19.31682 ? 106 PHE   A CE2 1 
ATOM   453  C  CZ  . PHE   A 1 62  ? 25.11900  -19.23000 22.71300  1.000 14.48682 ? 106 PHE   A CZ  1 
ATOM   454  N  N   . THR   A 1 63  ? 19.94700  -19.39700 21.62900  1.000 16.75682 ? 107 THR   A N   1 
ATOM   455  C  CA  . THR   A 1 63  ? 19.12000  -20.10500 22.60700  1.000 13.93682 ? 107 THR   A CA  1 
ATOM   456  C  C   . THR   A 1 63  ? 17.65100  -20.19100 22.20700  1.000 16.62682 ? 107 THR   A C   1 
ATOM   457  O  O   . THR   A 1 63  ? 16.87000  -20.81700 22.94200  1.000 18.31682 ? 107 THR   A O   1 
ATOM   458  C  CB  . THR   A 1 63  ? 19.19200  -19.50300 24.02700  1.000 14.90682 ? 107 THR   A CB  1 
ATOM   459  O  OG1 . THR   A 1 63  ? 18.36500  -18.33300 24.11200  1.000 16.29682 ? 107 THR   A OG1 1 
ATOM   460  C  CG2 . THR   A 1 63  ? 20.62600  -19.15100 24.42100  1.000 17.39682 ? 107 THR   A CG2 1 
ATOM   461  N  N   . ALA   A 1 64  ? 17.24400  -19.62200 21.07300  1.000 14.16682 ? 108 ALA   A N   1 
ATOM   462  C  CA  . ALA   A 1 64  ? 15.83800  -19.53000 20.70200  1.000 12.52682 ? 108 ALA   A CA  1 
ATOM   463  C  C   . ALA   A 1 64  ? 15.45600  -20.54300 19.62600  1.000 12.63682 ? 108 ALA   A C   1 
ATOM   464  O  O   . ALA   A 1 64  ? 16.30200  -21.17200 18.98300  1.000 13.49682 ? 108 ALA   A O   1 
ATOM   465  C  CB  . ALA   A 1 64  ? 15.50600  -18.11100 20.23400  1.000 13.14682 ? 108 ALA   A CB  1 
ATOM   466  N  N   . SER   A 1 65  ? 14.14800  -20.68800 19.42400  1.000 18.50682 ? 109 SER   A N   1 
ATOM   467  C  CA  . SER   A 1 65  ? 13.58500  -21.64800 18.47200  1.000 16.64682 ? 109 SER   A CA  1 
ATOM   468  C  C   . SER   A 1 65  ? 12.67500  -20.92400 17.47900  1.000 15.64682 ? 109 SER   A C   1 
ATOM   469  O  O   . SER   A 1 65  ? 12.46500  -19.71000 17.57200  1.000 14.72682 ? 109 SER   A O   1 
ATOM   470  C  CB  . SER   A 1 65  ? 12.84000  -22.75600 19.21800  1.000 17.91682 ? 109 SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 65  ? 11.78400  -22.20900 19.98100  1.000 24.42682 ? 109 SER   A OG  1 
ATOM   472  N  N   . GLN   A 1 66  ? 12.13600  -21.67600 16.50700  1.000 16.79682 ? 110 GLN   A N   1 
ATOM   473  C  CA  . GLN   A 1 66  ? 11.28700  -21.05500 15.49100  1.000 13.54682 ? 110 GLN   A CA  1 
ATOM   474  C  C   . GLN   A 1 66  ? 10.04100  -20.42300 16.09100  1.000 14.74682 ? 110 GLN   A C   1 
ATOM   475  O  O   . GLN   A 1 66  ? 9.48200   -19.50200 15.48500  1.000 14.29682 ? 110 GLN   A O   1 
ATOM   476  C  CB  . GLN   A 1 66  ? 10.86600  -22.06800 14.41800  1.000 15.51682 ? 110 GLN   A CB  1 
ATOM   477  C  CG  . GLN   A 1 66  ? 9.78100   -23.03200 14.85300  1.000 19.95682 ? 110 GLN   A CG  1 
ATOM   478  C  CD  . GLN   A 1 66  ? 9.32400   -23.95900 13.73400  1.000 19.50682 ? 110 GLN   A CD  1 
ATOM   479  O  OE1 . GLN   A 1 66  ? 8.80200   -23.51300 12.70900  1.000 15.01682 ? 110 GLN   A OE1 1 
ATOM   480  N  NE2 . GLN   A 1 66  ? 9.50000   -25.25700 13.94000  1.000 20.88682 ? 110 GLN   A NE2 1 
ATOM   481  N  N   . GLY   A 1 67  ? 9.59700   -20.89400 17.26600  1.000 17.40682 ? 111 GLY   A N   1 
ATOM   482  C  CA  . GLY   A 1 67  ? 8.44800   -20.28600 17.92300  1.000 15.92682 ? 111 GLY   A CA  1 
ATOM   483  C  C   . GLY   A 1 67  ? 8.61500   -18.80400 18.21100  1.000 15.39682 ? 111 GLY   A C   1 
ATOM   484  O  O   . GLY   A 1 67  ? 7.62900   -18.06100 18.25400  1.000 11.78682 ? 111 GLY   A O   1 
ATOM   485  N  N   . SER   A 1 68  ? 9.85600   -18.34500 18.39800  1.000 9.52682  ? 112 SER   A N   1 
ATOM   486  C  CA  . SER   A 1 68  ? 10.08400  -16.91100 18.56000  1.000 13.46682 ? 112 SER   A CA  1 
ATOM   487  C  C   . SER   A 1 68  ? 9.83900   -16.12400 17.27600  1.000 10.26682 ? 112 SER   A C   1 
ATOM   488  O  O   . SER   A 1 68  ? 9.76500   -14.89400 17.33200  1.000 7.42682  ? 112 SER   A O   1 
ATOM   489  C  CB  . SER   A 1 68  ? 11.50600  -16.64500 19.05000  1.000 9.64682  ? 112 SER   A CB  1 
ATOM   490  O  OG  . SER   A 1 68  ? 12.45700  -17.01600 18.06900  1.000 10.08682 ? 112 SER   A OG  1 
ATOM   491  N  N   . MET   A 1 69  ? 9.72700   -16.79600 16.12700  1.000 10.25682 ? 113 MET   A N   1 
ATOM   492  C  CA  . MET   A 1 69  ? 9.54600   -16.13000 14.83900  1.000 10.46682 ? 113 MET   A CA  1 
ATOM   493  C  C   . MET   A 1 69  ? 8.24500   -16.53000 14.15000  1.000 9.97682  ? 113 MET   A C   1 
ATOM   494  O  O   . MET   A 1 69  ? 8.03800   -16.16400 12.98800  1.000 8.16682  ? 113 MET   A O   1 
ATOM   495  C  CB  . MET   A 1 69  ? 10.72800  -16.44000 13.90800  1.000 9.48682  ? 113 MET   A CB  1 
ATOM   496  C  CG  . MET   A 1 69  ? 12.10000  -16.24800 14.53900  1.000 10.62682 ? 113 MET   A CG  1 
ATOM   497  S  SD  . MET   A 1 69  ? 12.38500  -14.50600 14.89000  1.000 10.75682 ? 113 MET   A SD  1 
ATOM   498  C  CE  . MET   A 1 69  ? 12.60300  -13.87400 13.22100  1.000 5.31682  ? 113 MET   A CE  1 
ATOM   499  N  N   . SER   A 1 70  ? 7.36300   -17.27800 14.82400  1.000 10.56682 ? 114 SER   A N   1 
ATOM   500  C  CA  . SER   A 1 70  ? 6.25500   -17.90400 14.10300  1.000 10.08682 ? 114 SER   A CA  1 
ATOM   501  C  C   . SER   A 1 70  ? 5.28900   -16.87500 13.51500  1.000 8.61682  ? 114 SER   A C   1 
ATOM   502  O  O   . SER   A 1 70  ? 4.67200   -17.14100 12.47700  1.000 10.87682 ? 114 SER   A O   1 
ATOM   503  C  CB  . SER   A 1 70  ? 5.51400   -18.89300 15.01200  1.000 12.23682 ? 114 SER   A CB  1 
ATOM   504  O  OG  . SER   A 1 70  ? 5.00800   -18.25100 16.16700  1.000 20.18682 ? 114 SER   A OG  1 
ATOM   505  N  N   . TRP   A 1 71  ? 5.17500   -15.68500 14.12000  1.000 7.13682  ? 115 TRP   A N   1 
ATOM   506  C  CA  . TRP   A 1 71  ? 4.18600   -14.72600 13.63200  1.000 10.96682 ? 115 TRP   A CA  1 
ATOM   507  C  C   . TRP   A 1 71  ? 4.51400   -14.18100 12.24400  1.000 14.35682 ? 115 TRP   A C   1 
ATOM   508  O  O   . TRP   A 1 71  ? 3.60700   -13.68000 11.56700  1.000 11.83682 ? 115 TRP   A O   1 
ATOM   509  C  CB  . TRP   A 1 71  ? 4.00600   -13.56700 14.62600  1.000 9.05682  ? 115 TRP   A CB  1 
ATOM   510  C  CG  . TRP   A 1 71  ? 5.11100   -12.54700 14.70800  1.000 7.58682  ? 115 TRP   A CG  1 
ATOM   511  C  CD1 . TRP   A 1 71  ? 6.21100   -12.59100 15.51800  1.000 9.73682  ? 115 TRP   A CD1 1 
ATOM   512  C  CD2 . TRP   A 1 71  ? 5.18200   -11.29500 14.00600  1.000 7.61682  ? 115 TRP   A CD2 1 
ATOM   513  N  NE1 . TRP   A 1 71  ? 6.97500   -11.45700 15.34300  1.000 10.19682 ? 115 TRP   A NE1 1 
ATOM   514  C  CE2 . TRP   A 1 71  ? 6.36800   -10.65100 14.41500  1.000 7.14682  ? 115 TRP   A CE2 1 
ATOM   515  C  CE3 . TRP   A 1 71  ? 4.36800   -10.66600 13.05200  1.000 8.51682  ? 115 TRP   A CE3 1 
ATOM   516  C  CZ2 . TRP   A 1 71  ? 6.76500   -9.40800  13.89800  1.000 7.17682  ? 115 TRP   A CZ2 1 
ATOM   517  C  CZ3 . TRP   A 1 71  ? 4.75900   -9.44500  12.54600  1.000 6.64682  ? 115 TRP   A CZ3 1 
ATOM   518  C  CH2 . TRP   A 1 71  ? 5.95300   -8.82500  12.97000  1.000 7.54682  ? 115 TRP   A CH2 1 
ATOM   519  N  N   . TYR   A 1 72  ? 5.77600   -14.26100 11.80700  1.000 9.33682  ? 116 TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 72  ? 6.11900   -13.81300 10.46200  1.000 8.06682  ? 116 TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 72  ? 5.51500   -14.72500 9.40400   1.000 12.03682 ? 116 TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 72  ? 5.27400   -14.28400 8.27500   1.000 12.51682 ? 116 TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 72  ? 7.64200   -13.74700 10.28200  1.000 8.01682  ? 116 TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 72  ? 8.31800   -12.67300 11.10400  1.000 10.43682 ? 116 TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 72  ? 8.36400   -11.35200 10.66500  1.000 9.72682  ? 116 TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 72  ? 8.90800   -12.97900 12.32000  1.000 8.96682  ? 116 TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 72  ? 8.98500   -10.35700 11.43400  1.000 8.45682  ? 116 TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 72  ? 9.53500   -11.99900 13.09100  1.000 6.89682  ? 116 TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 72  ? 9.56500   -10.69800 12.65100  1.000 8.99682  ? 116 TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 72  ? 10.17700  -9.75100  13.43800  1.000 7.57682  ? 116 TYR   A OH  1 
ATOM   531  N  N   . GLY   A 1 73  ? 5.27100   -15.99000 9.75400   1.000 12.10682 ? 117 GLY   A N   1 
ATOM   532  C  CA  . GLY   A 1 73  ? 4.76100   -17.00400 8.84600   1.000 12.74682 ? 117 GLY   A CA  1 
ATOM   533  C  C   . GLY   A 1 73  ? 3.47300   -16.63200 8.14200   1.000 11.43682 ? 117 GLY   A C   1 
ATOM   534  O  O   . GLY   A 1 73  ? 3.47200   -16.42900 6.92700   1.000 10.97682 ? 117 GLY   A O   1 
ATOM   535  N  N   . GLU   A 1 74  ? 2.37000   -16.54800 8.88800   1.000 13.61682 ? 118 GLU   A N   1 
ATOM   536  C  CA  . GLU   A 1 74  ? 1.09200   -16.20000 8.27100   1.000 11.74682 ? 118 GLU   A CA  1 
ATOM   537  C  C   . GLU   A 1 74  ? 1.11400   -14.77200 7.74300   1.000 14.32682 ? 118 GLU   A C   1 
ATOM   538  O  O   . GLU   A 1 74  ? 0.66600   -14.51200 6.62400   1.000 12.09682 ? 118 GLU   A O   1 
ATOM   539  C  CB  . GLU   A 1 74  ? -0.04700  -16.35800 9.27900   1.000 17.67682 ? 118 GLU   A CB  1 
ATOM   540  C  CG  . GLU   A 1 74  ? -0.31200  -17.78100 9.74600   1.000 20.28682 ? 118 GLU   A CG  1 
ATOM   541  C  CD  . GLU   A 1 74  ? -1.15600  -18.55600 8.75100   1.000 29.89682 ? 118 GLU   A CD  1 
ATOM   542  O  OE1 . GLU   A 1 74  ? -1.83200  -17.90500 7.91700   1.000 24.78682 ? 118 GLU   A OE1 1 
ATOM   543  O  OE2 . GLU   A 1 74  ? -1.13400  -19.80900 8.79700   1.000 31.27682 ? 118 GLU   A OE2 1 
ATOM   544  N  N   . ARG   A 1 75  ? 1.65300   -13.84200 8.53300   1.000 14.05682 ? 119 ARG   A N   1 
ATOM   545  C  CA  . ARG   A 1 75  ? 1.61000   -12.42900 8.17000   1.000 12.02682 ? 119 ARG   A CA  1 
ATOM   546  C  C   . ARG   A 1 75  ? 2.29100   -12.17100 6.83200   1.000 12.61682 ? 119 ARG   A C   1 
ATOM   547  O  O   . ARG   A 1 75  ? 1.74000   -11.48200 5.96800   1.000 13.52682 ? 119 ARG   A O   1 
ATOM   548  C  CB  . ARG   A 1 75  ? 2.27000   -11.59400 9.26200   1.000 13.67682 ? 119 ARG   A CB  1 
ATOM   549  C  CG  . ARG   A 1 75  ? 2.12900   -10.09300 9.05200   1.000 15.04682 ? 119 ARG   A CG  1 
ATOM   550  C  CD  . ARG   A 1 75  ? 1.32700   -9.52900  10.19000  1.000 13.12682 ? 119 ARG   A CD  1 
ATOM   551  N  NE  . ARG   A 1 75  ? 1.18500   -8.08200  10.14900  1.000 16.00682 ? 119 ARG   A NE  1 
ATOM   552  C  CZ  . ARG   A 1 75  ? 0.97300   -7.34000  11.22600  1.000 13.85682 ? 119 ARG   A CZ  1 
ATOM   553  N  NH1 . ARG   A 1 75  ? 0.90600   -7.88100  12.43000  1.000 13.43682 ? 119 ARG   A NH1 1 
ATOM   554  N  NH2 . ARG   A 1 75  ? 0.82900   -6.02500  11.09300  1.000 12.31682 ? 119 ARG   A NH2 1 
ATOM   555  N  N   . VAL   A 1 76  ? 3.50000   -12.70300 6.64600   1.000 9.99682  ? 120 VAL   A N   1 
ATOM   556  C  CA  . VAL   A 1 76  ? 4.21700   -12.44400 5.40400   1.000 11.17682 ? 120 VAL   A CA  1 
ATOM   557  C  C   . VAL   A 1 76  ? 3.71600   -13.34000 4.27100   1.000 8.55682  ? 120 VAL   A C   1 
ATOM   558  O  O   . VAL   A 1 76  ? 3.58200   -12.88800 3.13000   1.000 11.41682 ? 120 VAL   A O   1 
ATOM   559  C  CB  . VAL   A 1 76  ? 5.73400   -12.59100 5.61800   1.000 12.40682 ? 120 VAL   A CB  1 
ATOM   560  C  CG1 . VAL   A 1 76  ? 6.46200   -12.40000 4.30300   1.000 10.68682 ? 120 VAL   A CG1 1 
ATOM   561  C  CG2 . VAL   A 1 76  ? 6.22500   -11.56400 6.64300   1.000 9.24682  ? 120 VAL   A CG2 1 
ATOM   562  N  N   . ALA   A 1 77  ? 3.44900   -14.62100 4.54400   1.000 10.77682 ? 121 ALA   A N   1 
ATOM   563  C  CA  . ALA   A 1 77  ? 3.06100   -15.51000 3.45100   1.000 9.91682  ? 121 ALA   A CA  1 
ATOM   564  C  C   . ALA   A 1 77  ? 1.74100   -15.07400 2.82300   1.000 12.29682 ? 121 ALA   A C   1 
ATOM   565  O  O   . ALA   A 1 77  ? 1.54000   -15.24500 1.61000   1.000 11.40682 ? 121 ALA   A O   1 
ATOM   566  C  CB  . ALA   A 1 77  ? 2.96600   -16.96200 3.93100   1.000 11.75682 ? 121 ALA   A CB  1 
ATOM   567  N  N   . SER   A 1 78  ? 0.84200   -14.48600 3.62300   1.000 9.71682  ? 122 SER   A N   1 
ATOM   568  C  CA  . SER   A 1 78  ? -0.45100  -14.04600 3.11100   1.000 11.29682 ? 122 SER   A CA  1 
ATOM   569  C  C   . SER   A 1 78  ? -0.33800  -12.83200 2.20300   1.000 13.68682 ? 122 SER   A C   1 
ATOM   570  O  O   . SER   A 1 78  ? -1.31800  -12.49700 1.52500   1.000 9.93682  ? 122 SER   A O   1 
ATOM   571  C  CB  . SER   A 1 78  ? -1.40700  -13.72800 4.26500   1.000 9.34682  ? 122 SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 78  ? -1.02600  -12.54000 4.94400   1.000 12.26682 ? 122 SER   A OG  1 
ATOM   573  N  N   . HIS   A 1 79  ? 0.81400   -12.15500 2.18200   1.000 10.04682 ? 123 HIS   A N   1 
ATOM   574  C  CA  . HIS   A 1 79  ? 1.05800   -11.12100 1.18800   1.000 9.30682  ? 123 HIS   A CA  1 
ATOM   575  C  C   . HIS   A 1 79  ? 1.74600   -11.66200 -0.05800  1.000 12.38682 ? 123 HIS   A C   1 
ATOM   576  O  O   . HIS   A 1 79  ? 2.10400   -10.87700 -0.94300  1.000 15.23682 ? 123 HIS   A O   1 
ATOM   577  C  CB  . HIS   A 1 79  ? 1.86800   -9.97000  1.79700   1.000 10.10682 ? 123 HIS   A CB  1 
ATOM   578  C  CG  . HIS   A 1 79  ? 1.07100   -9.11600  2.73000   1.000 10.29682 ? 123 HIS   A CG  1 
ATOM   579  N  ND1 . HIS   A 1 79  ? 0.84300   -9.46400  4.04500   1.000 14.03682 ? 123 HIS   A ND1 1 
ATOM   580  C  CD2 . HIS   A 1 79  ? 0.42500   -7.94100  2.53400   1.000 9.91682  ? 123 HIS   A CD2 1 
ATOM   581  C  CE1 . HIS   A 1 79  ? 0.10800   -8.53000  4.62300   1.000 15.19682 ? 123 HIS   A CE1 1 
ATOM   582  N  NE2 . HIS   A 1 79  ? -0.15700  -7.59500  3.72900   1.000 13.80682 ? 123 HIS   A NE2 1 
ATOM   583  N  N   . GLY   A 1 80  ? 1.92700   -12.98000 -0.15300  1.000 10.91682 ? 124 GLY   A N   1 
ATOM   584  C  CA  . GLY   A 1 80  ? 2.40600   -13.59000 -1.38100  1.000 12.91682 ? 124 GLY   A CA  1 
ATOM   585  C  C   . GLY   A 1 80  ? 3.85100   -14.05900 -1.36800  1.000 11.90682 ? 124 GLY   A C   1 
ATOM   586  O  O   . GLY   A 1 80  ? 4.62100   -13.72200 -2.27600  1.000 10.36682 ? 124 GLY   A O   1 
ATOM   587  N  N   . PHE   A 1 81  ? 4.21900   -14.87300 -0.37800  1.000 9.81682  ? 125 PHE   A N   1 
ATOM   588  C  CA  . PHE   A 1 81  ? 5.56400   -15.42900 -0.30600  1.000 9.20682  ? 125 PHE   A CA  1 
ATOM   589  C  C   . PHE   A 1 81  ? 5.51200   -16.80400 0.32700   1.000 11.37682 ? 125 PHE   A C   1 
ATOM   590  O  O   . PHE   A 1 81  ? 4.63600   -17.09400 1.13700   1.000 9.27682  ? 125 PHE   A O   1 
ATOM   591  C  CB  . PHE   A 1 81  ? 6.52200   -14.55200 0.51400   1.000 8.98682  ? 125 PHE   A CB  1 
ATOM   592  C  CG  . PHE   A 1 81  ? 6.70300   -13.17500 -0.04700  1.000 11.53682 ? 125 PHE   A CG  1 
ATOM   593  C  CD1 . PHE   A 1 81  ? 7.60200   -12.94300 -1.08500  1.000 8.36682  ? 125 PHE   A CD1 1 
ATOM   594  C  CD2 . PHE   A 1 81  ? 5.95400   -12.11200 0.43800   1.000 10.40682 ? 125 PHE   A CD2 1 
ATOM   595  C  CE1 . PHE   A 1 81  ? 7.76600   -11.65000 -1.61500  1.000 11.31682 ? 125 PHE   A CE1 1 
ATOM   596  C  CE2 . PHE   A 1 81  ? 6.11600   -10.82800 -0.09200  1.000 9.61682  ? 125 PHE   A CE2 1 
ATOM   597  C  CZ  . PHE   A 1 81  ? 7.02000   -10.60000 -1.11000  1.000 6.62682  ? 125 PHE   A CZ  1 
ATOM   598  N  N   . ILE   A 1 82  ? 6.46700   -17.64700 -0.04600  1.000 9.76682  ? 126 ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 82  ? 6.72900   -18.86300 0.71100   1.000 11.18682 ? 126 ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 82  ? 7.67700   -18.50400 1.84900   1.000 10.44682 ? 126 ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 82  ? 8.74100   -17.92400 1.61700   1.000 10.10682 ? 126 ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 82  ? 7.31700   -19.95200 -0.18900  1.000 9.20682  ? 126 ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 82  ? 6.30600   -20.29400 -1.29700  1.000 9.42682  ? 126 ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 82  ? 7.68000   -21.19100 0.64900   1.000 6.85682  ? 126 ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 82  ? 6.88300   -21.09500 -2.44000  1.000 10.70682 ? 126 ILE   A CD1 1 
ATOM   606  N  N   . VAL   A 1 83  ? 7.27100   -18.80700 3.08300   1.000 10.01682 ? 127 VAL   A N   1 
ATOM   607  C  CA  . VAL   A 1 83  ? 7.99900   -18.40400 4.28500   1.000 9.05682  ? 127 VAL   A CA  1 
ATOM   608  C  C   . VAL   A 1 83  ? 8.35100   -19.66000 5.06900   1.000 11.10682 ? 127 VAL   A C   1 
ATOM   609  O  O   . VAL   A 1 83  ? 7.46300   -20.45200 5.40300   1.000 10.04682 ? 127 VAL   A O   1 
ATOM   610  C  CB  . VAL   A 1 83  ? 7.18100   -17.44000 5.16700   1.000 8.67682  ? 127 VAL   A CB  1 
ATOM   611  C  CG1 . VAL   A 1 83  ? 8.01100   -17.02000 6.39300   1.000 11.42682 ? 127 VAL   A CG1 1 
ATOM   612  C  CG2 . VAL   A 1 83  ? 6.71000   -16.20300 4.36900   1.000 9.97682  ? 127 VAL   A CG2 1 
ATOM   613  N  N   . PHE   A 1 84  ? 9.64300   -19.82700 5.37900   1.000 7.95682  ? 128 PHE   A N   1 
ATOM   614  C  CA  . PHE   A 1 84  ? 10.19000  -21.03400 6.00200   1.000 8.44682  ? 128 PHE   A CA  1 
ATOM   615  C  C   . PHE   A 1 84  ? 10.83100  -20.61200 7.33000   1.000 8.66682  ? 128 PHE   A C   1 
ATOM   616  O  O   . PHE   A 1 84  ? 11.95900  -20.10900 7.34100   1.000 7.68682  ? 128 PHE   A O   1 
ATOM   617  C  CB  . PHE   A 1 84  ? 11.20400  -21.68100 5.04700   1.000 7.58682  ? 128 PHE   A CB  1 
ATOM   618  C  CG  . PHE   A 1 84  ? 11.51600  -23.13600 5.32900   1.000 10.18682 ? 128 PHE   A CG  1 
ATOM   619  C  CD1 . PHE   A 1 84  ? 10.91700  -23.82400 6.37000   1.000 9.35682  ? 128 PHE   A CD1 1 
ATOM   620  C  CD2 . PHE   A 1 84  ? 12.41900  -23.81700 4.52100   1.000 9.05682  ? 128 PHE   A CD2 1 
ATOM   621  C  CE1 . PHE   A 1 84  ? 11.21800  -25.16900 6.60400   1.000 12.41682 ? 128 PHE   A CE1 1 
ATOM   622  C  CE2 . PHE   A 1 84  ? 12.72200  -25.15500 4.74000   1.000 9.17682  ? 128 PHE   A CE2 1 
ATOM   623  C  CZ  . PHE   A 1 84  ? 12.12000  -25.83500 5.78400   1.000 9.24682  ? 128 PHE   A CZ  1 
ATOM   624  N  N   . THR   A 1 85  ? 10.11000  -20.76500 8.44400   1.000 6.75682  ? 129 THR   A N   1 
ATOM   625  C  CA  . THR   A 1 85  ? 10.65500  -20.45300 9.76700   1.000 7.64682  ? 129 THR   A CA  1 
ATOM   626  C  C   . THR   A 1 85  ? 11.40200  -21.67600 10.28700  1.000 10.22682 ? 129 THR   A C   1 
ATOM   627  O  O   . THR   A 1 85  ? 10.78600  -22.72000 10.53200  1.000 9.79682  ? 129 THR   A O   1 
ATOM   628  C  CB  . THR   A 1 85  ? 9.55600   -20.03500 10.75100  1.000 7.98682  ? 129 THR   A CB  1 
ATOM   629  O  OG1 . THR   A 1 85  ? 8.59100   -21.09100 10.90300  1.000 9.71682  ? 129 THR   A OG1 1 
ATOM   630  C  CG2 . THR   A 1 85  ? 8.84700   -18.77800 10.26300  1.000 11.11682 ? 129 THR   A CG2 1 
ATOM   631  N  N   . ILE   A 1 86  ? 12.72000  -21.56100 10.45800  1.000 7.57682  ? 130 ILE   A N   1 
ATOM   632  C  CA  . ILE   A 1 86  ? 13.53900  -22.75000 10.68900  1.000 8.82682  ? 130 ILE   A CA  1 
ATOM   633  C  C   . ILE   A 1 86  ? 13.97600  -22.83600 12.14400  1.000 12.71682 ? 130 ILE   A C   1 
ATOM   634  O  O   . ILE   A 1 86  ? 13.97600  -21.85400 12.89200  1.000 9.40682  ? 130 ILE   A O   1 
ATOM   635  C  CB  . ILE   A 1 86  ? 14.77700  -22.80400 9.77000   1.000 8.96682  ? 130 ILE   A CB  1 
ATOM   636  C  CG1 . ILE   A 1 86  ? 15.75400  -21.68600 10.14800  1.000 9.18682  ? 130 ILE   A CG1 1 
ATOM   637  C  CG2 . ILE   A 1 86  ? 14.35400  -22.71700 8.30600   1.000 9.78682  ? 130 ILE   A CG2 1 
ATOM   638  C  CD1 . ILE   A 1 86  ? 17.12300  -21.77900 9.45600   1.000 13.79682 ? 130 ILE   A CD1 1 
ATOM   639  N  N   . ASP   A 1 87  ? 14.34500  -24.05500 12.53700  1.000 8.55682  ? 131 ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 87  ? 15.16100  -24.32400 13.70600  1.000 10.30682 ? 131 ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 87  ? 16.58900  -24.59900 13.25200  1.000 10.09682 ? 131 ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 87  ? 16.81900  -25.11400 12.15500  1.000 9.05682  ? 131 ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 87  ? 14.60500  -25.51800 14.49900  1.000 11.79682 ? 131 ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 87  ? 13.39800  -25.13400 15.35500  1.000 17.86682 ? 131 ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 87  ? 13.53100  -24.20200 16.17800  1.000 20.21682 ? 131 ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 87  ? 12.31600  -25.73800 15.19600  1.000 17.73682 ? 131 ASP   A OD2 1 
ATOM   647  N  N   . THR   A 1 88  ? 17.55100  -24.21600 14.08200  1.000 9.67682  ? 132 THR   A N   1 
ATOM   648  C  CA  . THR   A 1 88  ? 18.94700  -24.50200 13.78800  1.000 9.83682  ? 132 THR   A CA  1 
ATOM   649  C  C   . THR   A 1 88  ? 19.31000  -25.88500 14.33100  1.000 11.14682 ? 132 THR   A C   1 
ATOM   650  O  O   . THR   A 1 88  ? 18.54100  -26.50500 15.06400  1.000 9.43682  ? 132 THR   A O   1 
ATOM   651  C  CB  . THR   A 1 88  ? 19.84800  -23.41700 14.37500  1.000 12.50682 ? 132 THR   A CB  1 
ATOM   652  O  OG1 . THR   A 1 88  ? 19.50800  -23.23500 15.75300  1.000 13.55682 ? 132 THR   A OG1 1 
ATOM   653  C  CG2 . THR   A 1 88  ? 19.63700  -22.10400 13.63700  1.000 12.46682 ? 132 THR   A CG2 1 
ATOM   654  N  N   . ASN   A 1 89  ? 20.49100  -26.38500 13.94500  1.000 10.37682 ? 133 ASN   A N   1 
ATOM   655  C  CA  . ASN   A 1 89  ? 20.88600  -27.72900 14.37900  1.000 12.33682 ? 133 ASN   A CA  1 
ATOM   656  C  C   . ASN   A 1 89  ? 20.94400  -27.82200 15.90400  1.000 12.08682 ? 133 ASN   A C   1 
ATOM   657  O  O   . ASN   A 1 89  ? 20.40600  -28.76400 16.50000  1.000 10.86682 ? 133 ASN   A O   1 
ATOM   658  C  CB  . ASN   A 1 89  ? 22.22100  -28.12800 13.73800  1.000 9.04682  ? 133 ASN   A CB  1 
ATOM   659  C  CG  . ASN   A 1 89  ? 22.06400  -28.52000 12.25800  1.000 16.43682 ? 133 ASN   A CG  1 
ATOM   660  O  OD1 . ASN   A 1 89  ? 21.02500  -29.03400 11.85300  1.000 12.61682 ? 133 ASN   A OD1 1 
ATOM   661  N  ND2 . ASN   A 1 89  ? 23.09600  -28.27000 11.45700  1.000 11.48682 ? 133 ASN   A ND2 1 
ATOM   662  N  N   . THR   A 1 90  ? 21.55800  -26.83500 16.55800  1.000 11.56682 ? 134 THR   A N   1 
ATOM   663  C  CA  . THR   A 1 90  ? 21.40400  -26.63600 17.99400  1.000 11.63682 ? 134 THR   A CA  1 
ATOM   664  C  C   . THR   A 1 90  ? 21.04000  -25.18500 18.24700  1.000 13.45682 ? 134 THR   A C   1 
ATOM   665  O  O   . THR   A 1 90  ? 21.35400  -24.30000 17.44700  1.000 12.68682 ? 134 THR   A O   1 
ATOM   666  C  CB  . THR   A 1 90  ? 22.66900  -26.97500 18.81500  1.000 11.82682 ? 134 THR   A CB  1 
ATOM   667  O  OG1 . THR   A 1 90  ? 23.59100  -25.87800 18.76600  1.000 16.57682 ? 134 THR   A OG1 1 
ATOM   668  C  CG2 . THR   A 1 90  ? 23.34900  -28.23300 18.30100  1.000 14.35682 ? 134 THR   A CG2 1 
ATOM   669  N  N   . ARG   A 1 91  ? 20.39200  -24.94100 19.39000  1.000 12.29682 ? 135 ARG   A N   1 
ATOM   670  C  CA  . ARG   A 1 91  ? 20.06600  -23.57100 19.76000  1.000 13.21682 ? 135 ARG   A CA  1 
ATOM   671  C  C   . ARG   A 1 91  ? 21.30200  -22.73400 20.06200  1.000 13.69682 ? 135 ARG   A C   1 
ATOM   672  O  O   . ARG   A 1 91  ? 21.17500  -21.51500 20.20500  1.000 15.02682 ? 135 ARG   A O   1 
ATOM   673  C  CB  . ARG   A 1 91  ? 19.12000  -23.55100 20.96200  1.000 13.58682 ? 135 ARG   A CB  1 
ATOM   674  C  CG  . ARG   A 1 91  ? 17.69300  -24.02900 20.65000  1.000 24.19682 ? 135 ARG   A CG  1 
ATOM   675  C  CD  . ARG   A 1 91  ? 16.88100  -24.18600 21.93500  1.000 22.05682 ? 135 ARG   A CD  1 
ATOM   676  N  NE  . ARG   A 1 91  ? 17.54500  -25.10300 22.85400  1.000 28.51682 ? 135 ARG   A NE  1 
ATOM   677  C  CZ  . ARG   A 1 91  ? 17.12600  -26.33400 23.12400  1.000 33.98682 ? 135 ARG   A CZ  1 
ATOM   678  N  NH1 . ARG   A 1 91  ? 15.98400  -26.79600 22.64200  1.000 34.17682 ? 135 ARG   A NH1 1 
ATOM   679  N  NH2 . ARG   A 1 91  ? 17.87400  -27.12100 23.89700  1.000 30.93682 ? 135 ARG   A NH2 1 
ATOM   680  N  N   . LEU   A 1 92  ? 22.48900  -23.33900 20.13100  1.000 12.54682 ? 136 LEU   A N   1 
ATOM   681  C  CA  . LEU   A 1 92  ? 23.71400  -22.61000 20.44300  1.000 14.11682 ? 136 LEU   A CA  1 
ATOM   682  C  C   . LEU   A 1 92  ? 24.57600  -22.29700 19.21900  1.000 13.40682 ? 136 LEU   A C   1 
ATOM   683  O  O   . LEU   A 1 92  ? 25.69700  -21.80700 19.38300  1.000 12.43682 ? 136 LEU   A O   1 
ATOM   684  C  CB  . LEU   A 1 92  ? 24.54400  -23.38400 21.46900  1.000 16.23682 ? 136 LEU   A CB  1 
ATOM   685  C  CG  . LEU   A 1 92  ? 23.89200  -23.63800 22.82800  1.000 17.63682 ? 136 LEU   A CG  1 
ATOM   686  C  CD1 . LEU   A 1 92  ? 24.90100  -24.25900 23.79000  1.000 21.87682 ? 136 LEU   A CD1 1 
ATOM   687  C  CD2 . LEU   A 1 92  ? 23.30100  -22.35200 23.40200  1.000 16.43682 ? 136 LEU   A CD2 1 
ATOM   688  N  N   . ASP   A 1 93  ? 24.08100  -22.53900 18.00400  1.000 13.93682 ? 137 ASP   A N   1 
ATOM   689  C  CA  . ASP   A 1 93  ? 24.89800  -22.33200 16.80900  1.000 11.88682 ? 137 ASP   A CA  1 
ATOM   690  C  C   . ASP   A 1 93  ? 25.26400  -20.85800 16.62800  1.000 16.47682 ? 137 ASP   A C   1 
ATOM   691  O  O   . ASP   A 1 93  ? 24.49300  -19.95600 16.97100  1.000 16.02682 ? 137 ASP   A O   1 
ATOM   692  C  CB  . ASP   A 1 93  ? 24.16300  -22.84600 15.56900  1.000 11.34682 ? 137 ASP   A CB  1 
ATOM   693  C  CG  . ASP   A 1 93  ? 24.03100  -24.35600 15.55900  1.000 16.73682 ? 137 ASP   A CG  1 
ATOM   694  O  OD1 . ASP   A 1 93  ? 24.69700  -25.01200 16.39000  1.000 14.37682 ? 137 ASP   A OD1 1 
ATOM   695  O  OD2 . ASP   A 1 93  ? 23.25800  -24.88500 14.73500  1.000 14.74682 ? 137 ASP   A OD2 1 
ATOM   696  N  N   . ALA   A 1 94  ? 26.45300  -20.62500 16.06200  1.000 10.02682 ? 138 ALA   A N   1 
ATOM   697  C  CA  . ALA   A 1 94  ? 26.99200  -19.28200 15.85400  1.000 13.89682 ? 138 ALA   A CA  1 
ATOM   698  C  C   . ALA   A 1 94  ? 26.42100  -18.65800 14.57700  1.000 15.24682 ? 138 ALA   A C   1 
ATOM   699  O  O   . ALA   A 1 94  ? 25.81100  -19.34700 13.75400  1.000 11.02682 ? 138 ALA   A O   1 
ATOM   700  C  CB  . ALA   A 1 94  ? 28.52100  -19.35000 15.81100  1.000 13.58682 ? 138 ALA   A CB  1 
ATOM   701  N  N   . PRO   A 1 95  ? 26.60500  -17.33800 14.38600  1.000 12.51682 ? 139 PRO   A N   1 
ATOM   702  C  CA  . PRO   A 1 95  ? 26.07000  -16.68100 13.17200  1.000 12.32682 ? 139 PRO   A CA  1 
ATOM   703  C  C   . PRO   A 1 95  ? 26.50500  -17.31000 11.85300  1.000 11.38682 ? 139 PRO   A C   1 
ATOM   704  O  O   . PRO   A 1 95  ? 25.66400  -17.46800 10.96300  1.000 10.12682 ? 139 PRO   A O   1 
ATOM   705  C  CB  . PRO   A 1 95  ? 26.59800  -15.24200 13.29700  1.000 10.04682 ? 139 PRO   A CB  1 
ATOM   706  C  CG  . PRO   A 1 95  ? 26.73300  -15.02200 14.75000  1.000 11.18682 ? 139 PRO   A CG  1 
ATOM   707  C  CD  . PRO   A 1 95  ? 27.19100  -16.35000 15.31600  1.000 14.85682 ? 139 PRO   A CD  1 
ATOM   708  N  N   . GLY   A 1 96  ? 27.78700  -17.65400 11.68200  1.000 12.61682 ? 140 GLY   A N   1 
ATOM   709  C  CA  . GLY   A 1 96  ? 28.19600  -18.28200 10.42200  1.000 13.68682 ? 140 GLY   A CA  1 
ATOM   710  C  C   . GLY   A 1 96  ? 27.46600  -19.60600 10.20300  1.000 12.36682 ? 140 GLY   A C   1 
ATOM   711  O  O   . GLY   A 1 96  ? 27.04300  -19.91400 9.07900   1.000 9.48682  ? 140 GLY   A O   1 
ATOM   712  N  N   . GLN   A 1 97  ? 27.29900  -20.39900 11.26700  1.000 10.04682 ? 141 GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 97  ? 26.48200  -21.60600 11.17000  1.000 10.78682 ? 141 GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 97  ? 25.03700  -21.26800 10.80200  1.000 11.28682 ? 141 GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 97  ? 24.41500  -21.96500 9.99400   1.000 11.65682 ? 141 GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 97  ? 26.54500  -22.38800 12.48700  1.000 15.00682 ? 141 GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 97  ? 27.96200  -22.84800 12.86200  1.000 14.37682 ? 141 GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 97  ? 28.03900  -23.54100 14.22000  1.000 20.57682 ? 141 GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 97  ? 27.71100  -22.95600 15.24600  1.000 16.03682 ? 141 GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 97  ? 28.48400  -24.79400 14.22400  1.000 25.44682 ? 141 GLN   A NE2 1 
ATOM   721  N  N   . ARG   A 1 98  ? 24.48500  -20.19500 11.37500  1.000 8.12682  ? 142 ARG   A N   1 
ATOM   722  C  CA  . ARG   A 1 98  ? 23.10200  -19.83800 11.06200  1.000 7.67682  ? 142 ARG   A CA  1 
ATOM   723  C  C   . ARG   A 1 98  ? 22.95600  -19.42300 9.59900   1.000 7.27682  ? 142 ARG   A C   1 
ATOM   724  O  O   . ARG   A 1 98  ? 21.95900  -19.75900 8.95200   1.000 9.37682  ? 142 ARG   A O   1 
ATOM   725  C  CB  . ARG   A 1 98  ? 22.60800  -18.74600 12.01900  1.000 10.07682 ? 142 ARG   A CB  1 
ATOM   726  C  CG  . ARG   A 1 98  ? 22.39300  -19.29900 13.43800  1.000 7.97682  ? 142 ARG   A CG  1 
ATOM   727  C  CD  . ARG   A 1 98  ? 22.07900  -18.25100 14.48400  1.000 10.12682 ? 142 ARG   A CD  1 
ATOM   728  N  NE  . ARG   A 1 98  ? 22.24300  -18.84900 15.80500  1.000 12.75682 ? 142 ARG   A NE  1 
ATOM   729  C  CZ  . ARG   A 1 98  ? 21.25600  -19.37500 16.51700  1.000 11.76682 ? 142 ARG   A CZ  1 
ATOM   730  N  NH1 . ARG   A 1 98  ? 19.99300  -19.21600 16.16200  1.000 9.37682  ? 142 ARG   A NH1 1 
ATOM   731  N  NH2 . ARG   A 1 98  ? 21.54700  -20.08100 17.61200  1.000 11.51682 ? 142 ARG   A NH2 1 
ATOM   732  N  N   . GLY   A 1 99  ? 23.95500  -18.73200 9.04900   1.000 8.43682  ? 143 GLY   A N   1 
ATOM   733  C  CA  . GLY   A 1 99  ? 23.92000  -18.40900 7.62800   1.000 9.57682  ? 143 GLY   A CA  1 
ATOM   734  C  C   . GLY   A 1 99  ? 23.94300  -19.64200 6.74300   1.000 10.02682 ? 143 GLY   A C   1 
ATOM   735  O  O   . GLY   A 1 99  ? 23.16500  -19.75400 5.79100   1.000 6.04682  ? 143 GLY   A O   1 
ATOM   736  N  N   . ARG   A 1 100 ? 24.84400  -20.58400 7.04700   1.000 10.27682 ? 144 ARG   A N   1 
ATOM   737  C  CA  . ARG   A 1 100 ? 24.91700  -21.84100 6.30500   1.000 9.16682  ? 144 ARG   A CA  1 
ATOM   738  C  C   . ARG   A 1 100 ? 23.58400  -22.58500 6.33000   1.000 8.38682  ? 144 ARG   A C   1 
ATOM   739  O  O   . ARG   A 1 100 ? 23.15900  -23.14600 5.31200   1.000 7.83682  ? 144 ARG   A O   1 
ATOM   740  C  CB  . ARG   A 1 100 ? 26.02800  -22.71100 6.89200   1.000 11.63682 ? 144 ARG   A CB  1 
ATOM   741  C  CG  . ARG   A 1 100 ? 26.54500  -23.81000 5.99100   1.000 17.26682 ? 144 ARG   A CG  1 
ATOM   742  C  CD  . ARG   A 1 100 ? 27.80100  -24.46600 6.57400   1.000 23.43682 ? 144 ARG   A CD  1 
ATOM   743  N  NE  . ARG   A 1 100 ? 28.86700  -23.50400 6.85100   1.000 37.65682 ? 144 ARG   A NE  1 
ATOM   744  C  CZ  . ARG   A 1 100 ? 29.33000  -23.20900 8.06300   1.000 29.51682 ? 144 ARG   A CZ  1 
ATOM   745  N  NH1 . ARG   A 1 100 ? 28.86300  -23.80500 9.15100   1.000 25.94682 ? 144 ARG   A NH1 1 
ATOM   746  N  NH2 . ARG   A 1 100 ? 30.28700  -22.29300 8.18700   1.000 33.61682 ? 144 ARG   A NH2 1 
ATOM   747  N  N   . GLN   A 1 101 ? 22.89500  -22.58000 7.47600   1.000 7.48682  ? 145 GLN   A N   1 
ATOM   748  C  CA  . GLN   A 1 101 ? 21.65200  -23.33600 7.60000   1.000 8.24682  ? 145 GLN   A CA  1 
ATOM   749  C  C   . GLN   A 1 101 ? 20.47200  -22.62400 6.94900   1.000 8.79682  ? 145 GLN   A C   1 
ATOM   750  O  O   . GLN   A 1 101 ? 19.55100  -23.28900 6.46800   1.000 8.85682  ? 145 GLN   A O   1 
ATOM   751  C  CB  . GLN   A 1 101 ? 21.36600  -23.63700 9.07600   1.000 8.88682  ? 145 GLN   A CB  1 
ATOM   752  C  CG  . GLN   A 1 101 ? 22.40000  -24.58100 9.67400   1.000 9.40682  ? 145 GLN   A CG  1 
ATOM   753  C  CD  . GLN   A 1 101 ? 22.30500  -24.72800 11.18600  1.000 12.78682 ? 145 GLN   A CD  1 
ATOM   754  O  OE1 . GLN   A 1 101 ? 21.23300  -24.95400 11.73000  1.000 13.56682 ? 145 GLN   A OE1 1 
ATOM   755  N  NE2 . GLN   A 1 101 ? 23.44300  -24.62900 11.86500  1.000 10.06682 ? 145 GLN   A NE2 1 
ATOM   756  N  N   . LEU   A 1 102 ? 20.48000  -21.28800 6.91100   1.000 6.41682  ? 146 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 102 ? 19.50300  -20.57000 6.09400   1.000 7.75682  ? 146 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 102 ? 19.60000  -20.99900 4.63700   1.000 9.49682  ? 146 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 102 ? 18.58100  -21.26000 3.98400   1.000 6.77682  ? 146 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 102 ? 19.71200  -19.05400 6.20900   1.000 8.66682  ? 146 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 102 ? 19.19800  -18.35700 7.46900   1.000 6.74682  ? 146 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 102 ? 19.80500  -16.95900 7.58700   1.000 7.11682  ? 146 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 102 ? 17.67900  -18.28200 7.43800   1.000 8.23682  ? 146 LEU   A CD2 1 
ATOM   764  N  N   . LEU   A 1 103 ? 20.82400  -21.11800 4.12400   1.000 6.77682  ? 147 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 103 ? 21.00500  -21.55400 2.74500   1.000 9.51682  ? 147 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 103 ? 20.57200  -23.00500 2.56100   1.000 8.07682  ? 147 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 103 ? 19.99600  -23.35600 1.52400   1.000 11.13682 ? 147 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 103 ? 22.46300  -21.36300 2.32500   1.000 13.67682 ? 147 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 103 ? 22.90500  -19.90100 2.22700   1.000 8.38682  ? 147 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 103 ? 24.34700  -19.79100 1.75600   1.000 8.92682  ? 147 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 103 ? 21.97100  -19.16000 1.28800   1.000 11.81682 ? 147 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 104 ? 20.82000  -23.86200 3.55700   1.000 7.25682  ? 148 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 104 ? 20.34200  -25.24200 3.45800   1.000 10.31682 ? 148 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 104 ? 18.81800  -25.31100 3.48600   1.000 8.58682  ? 148 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 104 ? 18.22400  -26.17500 2.82900   1.000 11.47682 ? 148 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 104 ? 20.93000  -26.09900 4.57900   1.000 6.45682  ? 148 ALA   A CB  1 
ATOM   777  N  N   . ALA   A 1 105 ? 18.17000  -24.40700 4.21500   1.000 8.23682  ? 149 ALA   A N   1 
ATOM   778  C  CA  . ALA   A 1 105 ? 16.70700  -24.38600 4.23400   1.000 9.80682  ? 149 ALA   A CA  1 
ATOM   779  C  C   . ALA   A 1 105 ? 16.14500  -23.95000 2.88600   1.000 8.45682  ? 149 ALA   A C   1 
ATOM   780  O  O   . ALA   A 1 105 ? 15.19300  -24.55300 2.37000   1.000 7.50682  ? 149 ALA   A O   1 
ATOM   781  C  CB  . ALA   A 1 105 ? 16.21300  -23.46300 5.34300   1.000 6.86682  ? 149 ALA   A CB  1 
ATOM   782  N  N   . LEU   A 1 106 ? 16.72700  -22.90800 2.29500   1.000 9.42682  ? 150 LEU   A N   1 
ATOM   783  C  CA  . LEU   A 1 106 ? 16.35000  -22.52200 0.94500   1.000 7.05682  ? 150 LEU   A CA  1 
ATOM   784  C  C   . LEU   A 1 106 ? 16.59100  -23.65500 -0.04800  1.000 11.10682 ? 150 LEU   A C   1 
ATOM   785  O  O   . LEU   A 1 106 ? 15.76700  -23.88300 -0.94200  1.000 9.93682  ? 150 LEU   A O   1 
ATOM   786  C  CB  . LEU   A 1 106 ? 17.11700  -21.26600 0.53000   1.000 6.13682  ? 150 LEU   A CB  1 
ATOM   787  C  CG  . LEU   A 1 106 ? 16.67500  -19.97300 1.21900   1.000 8.63682  ? 150 LEU   A CG  1 
ATOM   788  C  CD1 . LEU   A 1 106 ? 17.56600  -18.78600 0.80300   1.000 5.30682  ? 150 LEU   A CD1 1 
ATOM   789  C  CD2 . LEU   A 1 106 ? 15.18500  -19.66800 0.96000   1.000 8.84682  ? 150 LEU   A CD2 1 
ATOM   790  N  N   . ASP   A 1 107 ? 17.72500  -24.35800 0.06900   1.000 9.49682  ? 151 ASP   A N   1 
ATOM   791  C  CA  . ASP   A 1 107 ? 17.99300  -25.46000 -0.85500  1.000 10.93682 ? 151 ASP   A CA  1 
ATOM   792  C  C   . ASP   A 1 107 ? 17.00600  -26.61100 -0.66700  1.000 9.63682  ? 151 ASP   A C   1 
ATOM   793  O  O   . ASP   A 1 107 ? 16.68600  -27.31700 -1.62900  1.000 10.22682 ? 151 ASP   A O   1 
ATOM   794  C  CB  . ASP   A 1 107 ? 19.42400  -25.97500 -0.68700  1.000 10.50682 ? 151 ASP   A CB  1 
ATOM   795  C  CG  . ASP   A 1 107 ? 20.47500  -25.00500 -1.22100  1.000 14.97682 ? 151 ASP   A CG  1 
ATOM   796  O  OD1 . ASP   A 1 107 ? 20.14200  -24.11200 -2.02700  1.000 16.47682 ? 151 ASP   A OD1 1 
ATOM   797  O  OD2 . ASP   A 1 107 ? 21.64800  -25.15600 -0.83300  1.000 21.98682 ? 151 ASP   A OD2 1 
ATOM   798  N  N   . TYR   A 1 108 ? 16.53400  -26.82900 0.55900   1.000 8.85682  ? 152 TYR   A N   1 
ATOM   799  C  CA  . TYR   A 1 108 ? 15.45900  -27.79300 0.77500   1.000 10.91682 ? 152 TYR   A CA  1 
ATOM   800  C  C   . TYR   A 1 108 ? 14.22300  -27.43900 -0.04700  1.000 11.90682 ? 152 TYR   A C   1 
ATOM   801  O  O   . TYR   A 1 108 ? 13.61600  -28.30900 -0.68600  1.000 10.82682 ? 152 TYR   A O   1 
ATOM   802  C  CB  . TYR   A 1 108 ? 15.10100  -27.86300 2.25600   1.000 9.91682  ? 152 TYR   A CB  1 
ATOM   803  C  CG  . TYR   A 1 108 ? 14.01600  -28.88900 2.55400   1.000 12.77682 ? 152 TYR   A CG  1 
ATOM   804  C  CD1 . TYR   A 1 108 ? 12.67300  -28.58200 2.37100   1.000 10.64682 ? 152 TYR   A CD1 1 
ATOM   805  C  CD2 . TYR   A 1 108 ? 14.34200  -30.16800 3.00200   1.000 12.65682 ? 152 TYR   A CD2 1 
ATOM   806  C  CE1 . TYR   A 1 108 ? 11.67600  -29.52000 2.62400   1.000 17.09682 ? 152 TYR   A CE1 1 
ATOM   807  C  CE2 . TYR   A 1 108 ? 13.34800  -31.11600 3.25300   1.000 16.67682 ? 152 TYR   A CE2 1 
ATOM   808  C  CZ  . TYR   A 1 108 ? 12.01900  -30.77900 3.06700   1.000 14.67682 ? 152 TYR   A CZ  1 
ATOM   809  O  OH  . TYR   A 1 108 ? 11.01900  -31.69400 3.32100   1.000 27.23682 ? 152 TYR   A OH  1 
ATOM   810  N  N   . LEU   A 1 109 ? 13.80800  -26.17100 -0.00400  1.000 11.56682 ? 153 LEU   A N   1 
ATOM   811  C  CA  . LEU   A 1 109 ? 12.65500  -25.74100 -0.79000  1.000 9.37682  ? 153 LEU   A CA  1 
ATOM   812  C  C   . LEU   A 1 109 ? 12.86600  -26.01700 -2.27600  1.000 10.59682 ? 153 LEU   A C   1 
ATOM   813  O  O   . LEU   A 1 109 ? 11.96700  -26.52000 -2.95800  1.000 9.65682  ? 153 LEU   A O   1 
ATOM   814  C  CB  . LEU   A 1 109 ? 12.39500  -24.25000 -0.56400  1.000 6.82682  ? 153 LEU   A CB  1 
ATOM   815  C  CG  . LEU   A 1 109 ? 12.03300  -23.75600 0.83800   1.000 8.08682  ? 153 LEU   A CG  1 
ATOM   816  C  CD1 . LEU   A 1 109 ? 11.93300  -22.22800 0.80500   1.000 6.55682  ? 153 LEU   A CD1 1 
ATOM   817  C  CD2 . LEU   A 1 109 ? 10.72100  -24.38400 1.30400   1.000 7.45682  ? 153 LEU   A CD2 1 
ATOM   818  N  N   . VAL   A 1 110 ? 14.05800  -25.70600 -2.78900  1.000 10.89682 ? 154 VAL   A N   1 
ATOM   819  C  CA  . VAL   A 1 110 ? 14.31100  -25.83300 -4.22300  1.000 10.98682 ? 154 VAL   A CA  1 
ATOM   820  C  C   . VAL   A 1 110 ? 14.39700  -27.30500 -4.63200  1.000 10.16682 ? 154 VAL   A C   1 
ATOM   821  O  O   . VAL   A 1 110 ? 13.86300  -27.70900 -5.67400  1.000 13.81682 ? 154 VAL   A O   1 
ATOM   822  C  CB  . VAL   A 1 110 ? 15.59300  -25.06000 -4.59500  1.000 9.69682  ? 154 VAL   A CB  1 
ATOM   823  C  CG1 . VAL   A 1 110 ? 16.02300  -25.37500 -6.02000  1.000 11.32682 ? 154 VAL   A CG1 1 
ATOM   824  C  CG2 . VAL   A 1 110 ? 15.38400  -23.55200 -4.41700  1.000 8.99682  ? 154 VAL   A CG2 1 
ATOM   825  N  N   . GLU   A 1 111 ? 15.04300  -28.12900 -3.80900  1.000 9.83682  ? 155 GLU   A N   1 
ATOM   826  C  CA  . GLU   A 1 111 ? 15.53100  -29.43400 -4.23400  1.000 12.06682 ? 155 GLU   A CA  1 
ATOM   827  C  C   . GLU   A 1 111 ? 14.81000  -30.61500 -3.61000  1.000 9.92682  ? 155 GLU   A C   1 
ATOM   828  O  O   . GLU   A 1 111 ? 14.85000  -31.70700 -4.18700  1.000 14.99682 ? 155 GLU   A O   1 
ATOM   829  C  CB  . GLU   A 1 111 ? 17.03000  -29.57300 -3.91500  1.000 9.15682  ? 155 GLU   A CB  1 
ATOM   830  C  CG  . GLU   A 1 111 ? 17.91500  -28.53900 -4.58400  1.000 13.31682 ? 155 GLU   A CG  1 
ATOM   831  C  CD  . GLU   A 1 111 ? 19.34900  -28.56800 -4.08100  1.000 19.28682 ? 155 GLU   A CD  1 
ATOM   832  O  OE1 . GLU   A 1 111 ? 19.71700  -29.51500 -3.34900  1.000 14.15682 ? 155 GLU   A OE1 1 
ATOM   833  O  OE2 . GLU   A 1 111 ? 20.11000  -27.63100 -4.41500  1.000 20.36682 ? 155 GLU   A OE2 1 
ATOM   834  N  N   . ARG   A 1 112 ? 14.18000  -30.44600 -2.44800  1.000 11.49682 ? 156 ARG   A N   1 
ATOM   835  C  CA  . ARG   A 1 112 ? 13.67800  -31.58400 -1.68400  1.000 10.91682 ? 156 ARG   A CA  1 
ATOM   836  C  C   . ARG   A 1 112 ? 12.19800  -31.51500 -1.35500  1.000 12.40682 ? 156 ARG   A C   1 
ATOM   837  O  O   . ARG   A 1 112 ? 11.60900  -32.56100 -1.06100  1.000 14.06682 ? 156 ARG   A O   1 
ATOM   838  C  CB  . ARG   A 1 112 ? 14.45900  -31.73500 -0.36400  1.000 11.73682 ? 156 ARG   A CB  1 
ATOM   839  C  CG  . ARG   A 1 112 ? 15.97200  -31.89100 -0.54100  1.000 14.67682 ? 156 ARG   A CG  1 
ATOM   840  C  CD  . ARG   A 1 112 ? 16.67400  -32.09800 0.79200   1.000 16.79682 ? 156 ARG   A CD  1 
ATOM   841  N  NE  . ARG   A 1 112 ? 18.11200  -31.88400 0.68600   1.000 18.94682 ? 156 ARG   A NE  1 
ATOM   842  C  CZ  . ARG   A 1 112 ? 18.95000  -31.93900 1.71300   1.000 21.96682 ? 156 ARG   A CZ  1 
ATOM   843  N  NH1 . ARG   A 1 112 ? 18.52000  -32.18400 2.94200   1.000 21.02682 ? 156 ARG   A NH1 1 
ATOM   844  N  NH2 . ARG   A 1 112 ? 20.25200  -31.73700 1.50300   1.000 17.70682 ? 156 ARG   A NH2 1 
ATOM   845  N  N   . SER   A 1 113 ? 11.58600  -30.33100 -1.39900  1.000 11.93682 ? 157 SER   A N   1 
ATOM   846  C  CA  . SER   A 1 113 ? 10.21200  -30.15800 -0.95500  1.000 12.87682 ? 157 SER   A CA  1 
ATOM   847  C  C   . SER   A 1 113 ? 9.25200   -30.99100 -1.80100  1.000 11.92682 ? 157 SER   A C   1 
ATOM   848  O  O   . SER   A 1 113 ? 9.52000   -31.32200 -2.96100  1.000 13.53682 ? 157 SER   A O   1 
ATOM   849  C  CB  . SER   A 1 113 ? 9.81200   -28.68100 -1.02700  1.000 11.74682 ? 157 SER   A CB  1 
ATOM   850  O  OG  . SER   A 1 113 ? 9.87500   -28.22000 -2.36500  1.000 8.91682  ? 157 SER   A OG  1 
ATOM   851  N  N   . ASP   A 1 114 ? 8.10300   -31.30800 -1.21100  1.000 15.33682 ? 158 ASP   A N   1 
ATOM   852  C  CA  . ASP   A 1 114 ? 7.11100   -32.08200 -1.93300  1.000 17.15682 ? 158 ASP   A CA  1 
ATOM   853  C  C   . ASP   A 1 114 ? 6.37800   -31.19500 -2.94200  1.000 17.36682 ? 158 ASP   A C   1 
ATOM   854  O  O   . ASP   A 1 114 ? 6.58000   -29.98000 -3.01300  1.000 13.46682 ? 158 ASP   A O   1 
ATOM   855  C  CB  . ASP   A 1 114 ? 6.15000   -32.76600 -0.96300  1.000 19.78682 ? 158 ASP   A CB  1 
ATOM   856  C  CG  . ASP   A 1 114 ? 5.30300   -31.78700 -0.16400  1.000 26.34682 ? 158 ASP   A CG  1 
ATOM   857  O  OD1 . ASP   A 1 114 ? 5.29600   -30.57200 -0.46600  1.000 27.70682 ? 158 ASP   A OD1 1 
ATOM   858  O  OD2 . ASP   A 1 114 ? 4.62800   -32.24800 0.78100   1.000 22.72682 ? 158 ASP   A OD2 1 
ATOM   859  N  N   . ARG   A 1 115 ? 5.48300   -31.82900 -3.70300  1.000 20.36682 ? 159 ARG   A N   1 
ATOM   860  C  CA  . ARG   A 1 115 ? 4.88800   -31.21000 -4.88400  1.000 19.98682 ? 159 ARG   A CA  1 
ATOM   861  C  C   . ARG   A 1 115 ? 4.08500   -29.96100 -4.53100  1.000 15.69682 ? 159 ARG   A C   1 
ATOM   862  O  O   . ARG   A 1 115 ? 4.12500   -28.96700 -5.26800  1.000 17.03682 ? 159 ARG   A O   1 
ATOM   863  C  CB  . ARG   A 1 115 ? 4.00300   -32.23900 -5.59000  1.000 24.88682 ? 159 ARG   A CB  1 
ATOM   864  C  CG  . ARG   A 1 115 ? 3.63700   -31.92400 -7.02600  1.000 30.48682 ? 159 ARG   A CG  1 
ATOM   865  C  CD  . ARG   A 1 115 ? 2.67900   -32.98200 -7.59200  1.000 16.42682 ? 159 ARG   A CD  1 
ATOM   866  N  NE  . ARG   A 1 115 ? 3.21400   -34.33500 -7.45300  1.000 25.41682 ? 159 ARG   A NE  1 
ATOM   867  C  CZ  . ARG   A 1 115 ? 2.57700   -35.43200 -7.84000  1.000 23.78682 ? 159 ARG   A CZ  1 
ATOM   868  N  NH1 . ARG   A 1 115 ? 1.36100   -35.37600 -8.36300  1.000 22.54682 ? 159 ARG   A NH1 1 
ATOM   869  N  NH2 . ARG   A 1 115 ? 3.17300   -36.61400 -7.69600  1.000 21.10682 ? 159 ARG   A NH2 1 
ATOM   870  N  N   . LYS   A 1 116 ? 3.33500   -30.00400 -3.42300  1.000 16.88682 ? 160 LYS   A N   1 
ATOM   871  C  CA  . LYS   A 1 116 ? 2.54400   -28.85300 -2.98200  1.000 16.87682 ? 160 LYS   A CA  1 
ATOM   872  C  C   . LYS   A 1 116 ? 3.38600   -27.58500 -2.92400  1.000 17.29682 ? 160 LYS   A C   1 
ATOM   873  O  O   . LYS   A 1 116 ? 2.94200   -26.51400 -3.35200  1.000 12.63682 ? 160 LYS   A O   1 
ATOM   874  C  CB  . LYS   A 1 116 ? 1.94500   -29.11200 -1.59400  1.000 18.23682 ? 160 LYS   A CB  1 
ATOM   875  C  CG  . LYS   A 1 116 ? 0.69800   -29.95700 -1.53700  1.000 31.59682 ? 160 LYS   A CG  1 
ATOM   876  C  CD  . LYS   A 1 116 ? 0.24200   -30.10500 -0.08100  1.000 29.88682 ? 160 LYS   A CD  1 
ATOM   877  C  CE  . LYS   A 1 116 ? 1.37900   -30.61200 0.81100   1.000 31.32682 ? 160 LYS   A CE  1 
ATOM   878  N  NZ  . LYS   A 1 116 ? 0.98600   -30.70300 2.25100   1.000 39.55682 ? 160 LYS   A NZ  1 
ATOM   879  N  N   . VAL   A 1 117 ? 4.60200   -27.69000 -2.38400  1.000 15.39682 ? 161 VAL   A N   1 
ATOM   880  C  CA  . VAL   A 1 117 ? 5.47300   -26.52700 -2.23000  1.000 10.98682 ? 161 VAL   A CA  1 
ATOM   881  C  C   . VAL   A 1 117 ? 6.27100   -26.27900 -3.49700  1.000 14.22682 ? 161 VAL   A C   1 
ATOM   882  O  O   . VAL   A 1 117 ? 6.40800   -25.14100 -3.95700  1.000 11.98682 ? 161 VAL   A O   1 
ATOM   883  C  CB  . VAL   A 1 117 ? 6.40000   -26.72100 -1.01600  1.000 14.30682 ? 161 VAL   A CB  1 
ATOM   884  C  CG1 . VAL   A 1 117 ? 7.51600   -25.67100 -1.00400  1.000 9.09682  ? 161 VAL   A CG1 1 
ATOM   885  C  CG2 . VAL   A 1 117 ? 5.59700   -26.69000 0.27200   1.000 9.33682  ? 161 VAL   A CG2 1 
ATOM   886  N  N   . ARG   A 1 118 ? 6.83200   -27.33900 -4.06800  1.000 13.59682 ? 162 ARG   A N   1 
ATOM   887  C  CA  . ARG   A 1 118 ? 7.80500   -27.16500 -5.13600  1.000 13.50682 ? 162 ARG   A CA  1 
ATOM   888  C  C   . ARG   A 1 118 ? 7.17400   -26.52300 -6.36500  1.000 14.33682 ? 162 ARG   A C   1 
ATOM   889  O  O   . ARG   A 1 118 ? 7.81900   -25.72900 -7.05200  1.000 14.24682 ? 162 ARG   A O   1 
ATOM   890  C  CB  . ARG   A 1 118 ? 8.43500   -28.51400 -5.48300  1.000 16.82682 ? 162 ARG   A CB  1 
ATOM   891  C  CG  . ARG   A 1 118 ? 9.60500   -28.44700 -6.43600  1.000 18.74682 ? 162 ARG   A CG  1 
ATOM   892  C  CD  . ARG   A 1 118 ? 10.91900  -28.62800 -5.71300  1.000 20.21682 ? 162 ARG   A CD  1 
ATOM   893  N  NE  . ARG   A 1 118 ? 11.01100  -29.87400 -4.95600  1.000 20.05682 ? 162 ARG   A NE  1 
ATOM   894  C  CZ  . ARG   A 1 118 ? 11.72500  -30.93400 -5.31600  1.000 21.04682 ? 162 ARG   A CZ  1 
ATOM   895  N  NH1 . ARG   A 1 118 ? 12.43100  -30.94700 -6.43900  1.000 20.19682 ? 162 ARG   A NH1 1 
ATOM   896  N  NH2 . ARG   A 1 118 ? 11.74400  -32.00500 -4.51900  1.000 12.53682 ? 162 ARG   A NH2 1 
ATOM   897  N  N   . GLU   A 1 119 ? 5.90600   -26.83000 -6.64600  1.000 14.17682 ? 163 GLU   A N   1 
ATOM   898  C  CA  . GLU   A 1 119 ? 5.26800   -26.28700 -7.84400  1.000 15.79682 ? 163 GLU   A CA  1 
ATOM   899  C  C   . GLU   A 1 119 ? 4.73000   -24.87400 -7.64200  1.000 16.54682 ? 163 GLU   A C   1 
ATOM   900  O  O   . GLU   A 1 119 ? 4.28100   -24.24700 -8.61000  1.000 17.73682 ? 163 GLU   A O   1 
ATOM   901  C  CB  . GLU   A 1 119 ? 4.15300   -27.23100 -8.31300  1.000 21.95682 ? 163 GLU   A CB  1 
ATOM   902  C  CG  . GLU   A 1 119 ? 4.66400   -28.67200 -8.50300  1.000 30.53682 ? 163 GLU   A CG  1 
ATOM   903  C  CD  . GLU   A 1 119 ? 3.80500   -29.53500 -9.43400  1.000 38.41682 ? 163 GLU   A CD  1 
ATOM   904  O  OE1 . GLU   A 1 119 ? 2.63200   -29.17400 -9.69600  1.000 36.81682 ? 163 GLU   A OE1 1 
ATOM   905  O  OE2 . GLU   A 1 119 ? 4.31400   -30.58700 -9.89900  1.000 33.55682 ? 163 GLU   A OE2 1 
ATOM   906  N  N   . ARG   A 1 120 ? 4.77400   -24.35300 -6.41900  1.000 17.76682 ? 164 ARG   A N   1 
ATOM   907  C  CA  . ARG   A 1 120 ? 4.40500   -22.97300 -6.14000  1.000 13.40682 ? 164 ARG   A CA  1 
ATOM   908  C  C   . ARG   A 1 120 ? 5.61100   -22.04100 -6.05000  1.000 14.46682 ? 164 ARG   A C   1 
ATOM   909  O  O   . ARG   A 1 120 ? 5.43300   -20.84800 -5.78900  1.000 12.13682 ? 164 ARG   A O   1 
ATOM   910  C  CB  . ARG   A 1 120 ? 3.60000   -22.90300 -4.83100  1.000 11.36682 ? 164 ARG   A CB  1 
ATOM   911  C  CG  . ARG   A 1 120 ? 2.18500   -23.48500 -4.90600  1.000 10.64682 ? 164 ARG   A CG  1 
ATOM   912  C  CD  . ARG   A 1 120 ? 1.50400   -23.37600 -3.55300  1.000 15.12682 ? 164 ARG   A CD  1 
ATOM   913  N  NE  . ARG   A 1 120 ? 0.05400   -23.52500 -3.62500  1.000 14.48682 ? 164 ARG   A NE  1 
ATOM   914  C  CZ  . ARG   A 1 120 ? -0.57000  -24.68800 -3.74000  1.000 15.26682 ? 164 ARG   A CZ  1 
ATOM   915  N  NH1 . ARG   A 1 120 ? 0.09900   -25.82300 -3.87300  1.000 13.80682 ? 164 ARG   A NH1 1 
ATOM   916  N  NH2 . ARG   A 1 120 ? -1.90000  -24.71300 -3.71800  1.000 17.97682 ? 164 ARG   A NH2 1 
ATOM   917  N  N   . LEU   A 1 121 ? 6.82400   -22.55200 -6.25800  1.000 12.04682 ? 165 LEU   A N   1 
ATOM   918  C  CA  . LEU   A 1 121 ? 8.06100   -21.83900 -5.95900  1.000 12.03682 ? 165 LEU   A CA  1 
ATOM   919  C  C   . LEU   A 1 121 ? 8.77700   -21.43600 -7.23800  1.000 13.96682 ? 165 LEU   A C   1 
ATOM   920  O  O   . LEU   A 1 121 ? 8.92000   -22.25500 -8.15100  1.000 12.88682 ? 165 LEU   A O   1 
ATOM   921  C  CB  . LEU   A 1 121 ? 8.99300   -22.71900 -5.12100  1.000 12.74682 ? 165 LEU   A CB  1 
ATOM   922  C  CG  . LEU   A 1 121 ? 10.41100  -22.20000 -4.89300  1.000 12.96682 ? 165 LEU   A CG  1 
ATOM   923  C  CD1 . LEU   A 1 121 ? 10.41300  -21.04900 -3.88600  1.000 10.80682 ? 165 LEU   A CD1 1 
ATOM   924  C  CD2 . LEU   A 1 121 ? 11.33200  -23.34300 -4.43600  1.000 11.52682 ? 165 LEU   A CD2 1 
ATOM   925  N  N   . ASP   A 1 122 ? 9.24000   -20.18000 -7.29100  1.000 10.09682 ? 166 ASP   A N   1 
ATOM   926  C  CA  . ASP   A 1 122 ? 10.21700  -19.72000 -8.27400  1.000 13.91682 ? 166 ASP   A CA  1 
ATOM   927  C  C   . ASP   A 1 122 ? 11.59800  -19.87700 -7.64800  1.000 15.57682 ? 166 ASP   A C   1 
ATOM   928  O  O   . ASP   A 1 122 ? 11.96800  -19.08200 -6.77900  1.000 14.38682 ? 166 ASP   A O   1 
ATOM   929  C  CB  . ASP   A 1 122 ? 9.97500   -18.26000 -8.67400  1.000 8.35682  ? 166 ASP   A CB  1 
ATOM   930  C  CG  . ASP   A 1 122 ? 10.86200  -17.81000 -9.83600  1.000 14.80682 ? 166 ASP   A CG  1 
ATOM   931  O  OD1 . ASP   A 1 122 ? 11.93000  -18.42400 -10.06400 1.000 16.01682 ? 166 ASP   A OD1 1 
ATOM   932  O  OD2 . ASP   A 1 122 ? 10.49400  -16.83100 -10.52300 1.000 11.57682 ? 166 ASP   A OD2 1 
ATOM   933  N  N   . PRO   A 1 123 ? 12.38100  -20.88600 -8.04300  1.000 13.26682 ? 167 PRO   A N   1 
ATOM   934  C  CA  . PRO   A 1 123 ? 13.67000  -21.12100 -7.37500  1.000 15.09682 ? 167 PRO   A CA  1 
ATOM   935  C  C   . PRO   A 1 123 ? 14.72200  -20.05400 -7.65800  1.000 15.59682 ? 167 PRO   A C   1 
ATOM   936  O  O   . PRO   A 1 123 ? 15.79600  -20.10300 -7.04900  1.000 20.03682 ? 167 PRO   A O   1 
ATOM   937  C  CB  . PRO   A 1 123 ? 14.10200  -22.49000 -7.92100  1.000 17.14682 ? 167 PRO   A CB  1 
ATOM   938  C  CG  . PRO   A 1 123 ? 13.44500  -22.58800 -9.26000  1.000 19.13682 ? 167 PRO   A CG  1 
ATOM   939  C  CD  . PRO   A 1 123 ? 12.13800  -21.83100 -9.14800  1.000 18.42682 ? 167 PRO   A CD  1 
ATOM   940  N  N   . ASN   A 1 124 ? 14.45400  -19.10800 -8.55800  1.000 15.21682 ? 168 ASN   A N   1 
ATOM   941  C  CA  . ASN   A 1 124 ? 15.37900  -18.02600 -8.87100  1.000 14.21682 ? 168 ASN   A CA  1 
ATOM   942  C  C   . ASN   A 1 124 ? 15.27700  -16.85400 -7.90600  1.000 15.02682 ? 168 ASN   A C   1 
ATOM   943  O  O   . ASN   A 1 124 ? 16.11200  -15.94900 -7.97700  1.000 12.63682 ? 168 ASN   A O   1 
ATOM   944  C  CB  . ASN   A 1 124 ? 15.11600  -17.49500 -10.28500 1.000 16.06682 ? 168 ASN   A CB  1 
ATOM   945  C  CG  . ASN   A 1 124 ? 15.25700  -18.55900 -11.34400 1.000 16.10682 ? 168 ASN   A CG  1 
ATOM   946  O  OD1 . ASN   A 1 124 ? 16.24000  -19.29300 -11.36900 1.000 22.91682 ? 168 ASN   A OD1 1 
ATOM   947  N  ND2 . ASN   A 1 124 ? 14.25900  -18.66200 -12.21500 1.000 22.11682 ? 168 ASN   A ND2 1 
ATOM   948  N  N   . ARG   A 1 125 ? 14.26100  -16.81700 -7.04000  1.000 13.81682 ? 169 ARG   A N   1 
ATOM   949  C  CA  . ARG   A 1 125 ? 13.94500  -15.61200 -6.26600  1.000 9.81682  ? 169 ARG   A CA  1 
ATOM   950  C  C   . ARG   A 1 125 ? 13.84900  -15.97400 -4.78800  1.000 7.19682  ? 169 ARG   A C   1 
ATOM   951  O  O   . ARG   A 1 125 ? 12.75600  -16.22400 -4.27000  1.000 10.01682 ? 169 ARG   A O   1 
ATOM   952  C  CB  . ARG   A 1 125 ? 12.66000  -14.96200 -6.78200  1.000 9.68682  ? 169 ARG   A CB  1 
ATOM   953  C  CG  . ARG   A 1 125 ? 12.69600  -14.68800 -8.29000  1.000 9.05682  ? 169 ARG   A CG  1 
ATOM   954  C  CD  . ARG   A 1 125 ? 11.50500  -13.87600 -8.79700  1.000 10.16682 ? 169 ARG   A CD  1 
ATOM   955  N  NE  . ARG   A 1 125 ? 10.22400  -14.57700 -8.76000  1.000 12.20682 ? 169 ARG   A NE  1 
ATOM   956  C  CZ  . ARG   A 1 125 ? 9.17900   -14.18900 -8.03800  1.000 12.19682 ? 169 ARG   A CZ  1 
ATOM   957  N  NH1 . ARG   A 1 125 ? 9.25400   -13.16000 -7.20600  1.000 9.35682  ? 169 ARG   A NH1 1 
ATOM   958  N  NH2 . ARG   A 1 125 ? 8.02200   -14.83600 -8.16900  1.000 11.65682 ? 169 ARG   A NH2 1 
ATOM   959  N  N   . LEU   A 1 126 ? 14.99600  -15.96000 -4.11200  1.000 5.49682  ? 170 LEU   A N   1 
ATOM   960  C  CA  . LEU   A 1 126 ? 15.13600  -16.40000 -2.73200  1.000 5.72682  ? 170 LEU   A CA  1 
ATOM   961  C  C   . LEU   A 1 126 ? 15.64500  -15.25200 -1.87200  1.000 9.59682  ? 170 LEU   A C   1 
ATOM   962  O  O   . LEU   A 1 126 ? 16.34100  -14.35300 -2.35900  1.000 10.30682 ? 170 LEU   A O   1 
ATOM   963  C  CB  . LEU   A 1 126 ? 16.11000  -17.57800 -2.62400  1.000 6.73682  ? 170 LEU   A CB  1 
ATOM   964  C  CG  . LEU   A 1 126 ? 15.79700  -18.70100 -3.61000  1.000 12.69682 ? 170 LEU   A CG  1 
ATOM   965  C  CD1 . LEU   A 1 126 ? 16.84600  -19.83700 -3.55600  1.000 10.58682 ? 170 LEU   A CD1 1 
ATOM   966  C  CD2 . LEU   A 1 126 ? 14.36700  -19.20200 -3.37500  1.000 8.73682  ? 170 LEU   A CD2 1 
ATOM   967  N  N   . ALA   A 1 127 ? 15.33600  -15.32100 -0.57600  1.000 6.37682  ? 171 ALA   A N   1 
ATOM   968  C  CA  . ALA   A 1 127 ? 15.67900  -14.25400 0.35700   1.000 8.09682  ? 171 ALA   A CA  1 
ATOM   969  C  C   . ALA   A 1 127 ? 15.91000  -14.85300 1.74000   1.000 8.72682  ? 171 ALA   A C   1 
ATOM   970  O  O   . ALA   A 1 127 ? 15.48200  -15.97500 2.02700   1.000 6.21682  ? 171 ALA   A O   1 
ATOM   971  C  CB  . ALA   A 1 127 ? 14.58100  -13.18600 0.40800   1.000 7.68682  ? 171 ALA   A CB  1 
ATOM   972  N  N   . VAL   A 1 128 ? 16.59700  -14.08600 2.59800   1.000 6.24682  ? 172 VAL   A N   1 
ATOM   973  C  CA  . VAL   A 1 128 ? 16.90400  -14.51000 3.96200   1.000 7.05682  ? 172 VAL   A CA  1 
ATOM   974  C  C   . VAL   A 1 128 ? 16.51200  -13.40400 4.93600   1.000 7.32682  ? 172 VAL   A C   1 
ATOM   975  O  O   . VAL   A 1 128 ? 16.56000  -12.21200 4.61100   1.000 7.33682  ? 172 VAL   A O   1 
ATOM   976  C  CB  . VAL   A 1 128 ? 18.39900  -14.88300 4.14800   1.000 6.08682  ? 172 VAL   A CB  1 
ATOM   977  C  CG1 . VAL   A 1 128 ? 18.76100  -16.15300 3.36800   1.000 4.40682  ? 172 VAL   A CG1 1 
ATOM   978  C  CG2 . VAL   A 1 128 ? 19.34000  -13.69500 3.74600   1.000 6.35682  ? 172 VAL   A CG2 1 
ATOM   979  N  N   . MET   A 1 129 ? 16.15000  -13.81800 6.15200   1.000 8.95682  ? 173 MET   A N   1 
ATOM   980  C  CA  . MET   A 1 129 ? 15.78200  -12.93200 7.24600   1.000 6.69682  ? 173 MET   A CA  1 
ATOM   981  C  C   . MET   A 1 129 ? 16.10500  -13.65500 8.54600   1.000 8.59682  ? 173 MET   A C   1 
ATOM   982  O  O   . MET   A 1 129 ? 16.02500  -14.88300 8.61900   1.000 10.29682 ? 173 MET   A O   1 
ATOM   983  C  CB  . MET   A 1 129 ? 14.29400  -12.54200 7.17600   1.000 4.40682  ? 173 MET   A CB  1 
ATOM   984  C  CG  . MET   A 1 129 ? 13.79000  -11.68300 8.34400   1.000 8.92682  ? 173 MET   A CG  1 
ATOM   985  S  SD  . MET   A 1 129 ? 12.19200  -10.87500 8.04500   1.000 9.37682  ? 173 MET   A SD  1 
ATOM   986  C  CE  . MET   A 1 129 ? 11.06500  -12.26600 8.21000   1.000 8.95682  ? 173 MET   A CE  1 
ATOM   987  N  N   . GLY   A 1 130 ? 16.47600  -12.90100 9.57200   1.000 5.48682  ? 174 GLY   A N   1 
ATOM   988  C  CA  . GLY   A 1 130 ? 16.78300  -13.53600 10.83700  1.000 6.53682  ? 174 GLY   A CA  1 
ATOM   989  C  C   . GLY   A 1 130 ? 16.93000  -12.54800 11.97000  1.000 6.97682  ? 174 GLY   A C   1 
ATOM   990  O  O   . GLY   A 1 130 ? 17.23900  -11.36600 11.76500  1.000 8.25682  ? 174 GLY   A O   1 
ATOM   991  N  N   . HIS   A 1 131 ? 16.73400  -13.06900 13.18000  1.000 6.77682  ? 175 HIS   A N   1 
ATOM   992  C  CA  . HIS   A 1 131 ? 16.72300  -12.29500 14.41900  1.000 8.65682  ? 175 HIS   A CA  1 
ATOM   993  C  C   . HIS   A 1 131 ? 17.99600  -12.53400 15.21600  1.000 9.57682  ? 175 HIS   A C   1 
ATOM   994  O  O   . HIS   A 1 131 ? 18.36600  -13.69200 15.47400  1.000 5.29682  ? 175 HIS   A O   1 
ATOM   995  C  CB  . HIS   A 1 131 ? 15.51700  -12.66300 15.28600  1.000 8.29682  ? 175 HIS   A CB  1 
ATOM   996  C  CG  . HIS   A 1 131 ? 15.49900  -11.97000 16.61700  1.000 9.78682  ? 175 HIS   A CG  1 
ATOM   997  N  ND1 . HIS   A 1 131 ? 15.34500  -12.65000 17.80600  1.000 8.11682  ? 175 HIS   A ND1 1 
ATOM   998  C  CD2 . HIS   A 1 131 ? 15.62100  -10.65800 16.94600  1.000 7.68682  ? 175 HIS   A CD2 1 
ATOM   999  C  CE1 . HIS   A 1 131 ? 15.36800  -11.78700 18.81100  1.000 9.33682  ? 175 HIS   A CE1 1 
ATOM   1000 N  NE2 . HIS   A 1 131 ? 15.54000  -10.57300 18.31600  1.000 7.20682  ? 175 HIS   A NE2 1 
ATOM   1001 N  N   . ALA   A 1 132 ? 18.65200  -11.43200 15.61600  1.000 6.49682  ? 176 ALA   A N   1 
ATOM   1002 C  CA  . ALA   A 1 132 ? 19.75300  -11.47400 16.57600  1.000 7.56682  ? 176 ALA   A CA  1 
ATOM   1003 C  C   . ALA   A 1 132 ? 20.95600  -12.21600 15.98200  1.000 6.64682  ? 176 ALA   A C   1 
ATOM   1004 O  O   . ALA   A 1 132 ? 21.46600  -11.79500 14.94300  1.000 7.25682  ? 176 ALA   A O   1 
ATOM   1005 C  CB  . ALA   A 1 132 ? 19.26800  -12.09300 17.88900  1.000 11.14682 ? 176 ALA   A CB  1 
ATOM   1006 N  N   . MET   A 1 133 ? 21.44600  -13.30100 16.60300  1.000 7.61682  ? 177 MET   A N   1 
ATOM   1007 C  CA  . MET   A 1 133 ? 22.47400  -14.09400 15.92200  1.000 7.24682  ? 177 MET   A CA  1 
ATOM   1008 C  C   . MET   A 1 133 ? 22.00800  -14.57700 14.54900  1.000 6.34682  ? 177 MET   A C   1 
ATOM   1009 O  O   . MET   A 1 133 ? 22.82600  -14.73200 13.63800  1.000 7.64682  ? 177 MET   A O   1 
ATOM   1010 C  CB  . MET   A 1 133 ? 22.89400  -15.30100 16.76600  1.000 7.66682  ? 177 MET   A CB  1 
ATOM   1011 C  CG  . MET   A 1 133 ? 23.96900  -15.01500 17.78400  1.000 12.39682 ? 177 MET   A CG  1 
ATOM   1012 S  SD  . MET   A 1 133 ? 24.88900  -16.52200 18.26400  1.000 14.75682 ? 177 MET   A SD  1 
ATOM   1013 C  CE  . MET   A 1 133 ? 25.79100  -15.79900 19.62900  1.000 15.39682 ? 177 MET   A CE  1 
ATOM   1014 N  N   . GLY   A 1 134 ? 20.71500  -14.87200 14.39300  1.000 9.36682  ? 178 GLY   A N   1 
ATOM   1015 C  CA  . GLY   A 1 134 ? 20.18900  -15.20300 13.07600  1.000 7.80682  ? 178 GLY   A CA  1 
ATOM   1016 C  C   . GLY   A 1 134 ? 20.17700  -14.02700 12.12000  1.000 6.87682  ? 178 GLY   A C   1 
ATOM   1017 O  O   . GLY   A 1 134 ? 20.18000  -14.23000 10.89800  1.000 8.29682  ? 178 GLY   A O   1 
ATOM   1018 N  N   . GLY   A 1 135 ? 20.17000  -12.80400 12.65100  1.000 5.95682  ? 179 GLY   A N   1 
ATOM   1019 C  CA  . GLY   A 1 135 ? 20.40300  -11.63100 11.81500  1.000 5.89682  ? 179 GLY   A CA  1 
ATOM   1020 C  C   . GLY   A 1 135 ? 21.85200  -11.50100 11.38200  1.000 7.19682  ? 179 GLY   A C   1 
ATOM   1021 O  O   . GLY   A 1 135 ? 22.13600  -11.11200 10.24400  1.000 7.33682  ? 179 GLY   A O   1 
ATOM   1022 N  N   . GLY   A 1 136 ? 22.79100  -11.82000 12.28200  1.000 6.52682  ? 180 GLY   A N   1 
ATOM   1023 C  CA  . GLY   A 1 136 ? 24.15900  -12.05400 11.84700  1.000 4.73682  ? 180 GLY   A CA  1 
ATOM   1024 C  C   . GLY   A 1 136 ? 24.24100  -13.13000 10.77600  1.000 7.58682  ? 180 GLY   A C   1 
ATOM   1025 O  O   . GLY   A 1 136 ? 25.01400  -13.01700 9.82200   1.000 8.75682  ? 180 GLY   A O   1 
ATOM   1026 N  N   . GLY   A 1 137 ? 23.42100  -14.17600 10.90300  1.000 7.66682  ? 181 GLY   A N   1 
ATOM   1027 C  CA  . GLY   A 1 137 ? 23.39700  -15.21800 9.88700   1.000 6.46682  ? 181 GLY   A CA  1 
ATOM   1028 C  C   . GLY   A 1 137 ? 22.85600  -14.73900 8.55300   1.000 7.90682  ? 181 GLY   A C   1 
ATOM   1029 O  O   . GLY   A 1 137 ? 23.32100  -15.18400 7.49500   1.000 6.29682  ? 181 GLY   A O   1 
ATOM   1030 N  N   . SER   A 1 138 ? 21.88500  -13.81900 8.58100   1.000 7.73682  ? 182 SER   A N   1 
ATOM   1031 C  CA  . SER   A 1 138 ? 21.37200  -13.24700 7.34300   1.000 8.12682  ? 182 SER   A CA  1 
ATOM   1032 C  C   . SER   A 1 138 ? 22.48900  -12.53000 6.58600   1.000 9.31682  ? 182 SER   A C   1 
ATOM   1033 O  O   . SER   A 1 138 ? 22.64800  -12.72600 5.37700   1.000 10.32682 ? 182 SER   A O   1 
ATOM   1034 C  CB  . SER   A 1 138 ? 20.19500  -12.30800 7.65700   1.000 8.50682  ? 182 SER   A CB  1 
ATOM   1035 O  OG  . SER   A 1 138 ? 19.45500  -11.94500 6.49400   1.000 8.57682  ? 182 SER   A OG  1 
ATOM   1036 N  N   . LEU   A 1 139 ? 23.29900  -11.73200 7.29400   1.000 8.29682  ? 183 LEU   A N   1 
ATOM   1037 C  CA  . LEU   A 1 139 ? 24.47900  -11.10700 6.69100   1.000 7.36682  ? 183 LEU   A CA  1 
ATOM   1038 C  C   . LEU   A 1 139 ? 25.42900  -12.16300 6.12400   1.000 11.14682 ? 183 LEU   A C   1 
ATOM   1039 O  O   . LEU   A 1 139 ? 25.84200  -12.08300 4.95500   1.000 7.51682  ? 183 LEU   A O   1 
ATOM   1040 C  CB  . LEU   A 1 139 ? 25.18900  -10.22900 7.73400   1.000 7.78682  ? 183 LEU   A CB  1 
ATOM   1041 C  CG  . LEU   A 1 139 ? 24.43400  -8.97500  8.20400   1.000 6.71682  ? 183 LEU   A CG  1 
ATOM   1042 C  CD1 . LEU   A 1 139 ? 24.92300  -8.45700  9.56700   1.000 6.01682  ? 183 LEU   A CD1 1 
ATOM   1043 C  CD2 . LEU   A 1 139 ? 24.52300  -7.87100  7.16100   1.000 6.38682  ? 183 LEU   A CD2 1 
ATOM   1044 N  N   . GLU   A 1 140 ? 25.75400  -13.18200 6.93500   1.000 7.03682  ? 184 GLU   A N   1 
ATOM   1045 C  CA  . GLU   A 1 140 ? 26.64100  -14.26000 6.49800   1.000 9.18682  ? 184 GLU   A CA  1 
ATOM   1046 C  C   . GLU   A 1 140 ? 26.13200  -14.94700 5.23400   1.000 10.41682 ? 184 GLU   A C   1 
ATOM   1047 O  O   . GLU   A 1 140 ? 26.91700  -15.23300 4.32200   1.000 11.29682 ? 184 GLU   A O   1 
ATOM   1048 C  CB  . GLU   A 1 140 ? 26.80200  -15.29600 7.61200   1.000 7.25682  ? 184 GLU   A CB  1 
ATOM   1049 C  CG  . GLU   A 1 140 ? 27.60300  -14.83600 8.81600   1.000 12.96682 ? 184 GLU   A CG  1 
ATOM   1050 C  CD  . GLU   A 1 140 ? 29.09500  -15.16300 8.70400   1.000 23.25682 ? 184 GLU   A CD  1 
ATOM   1051 O  OE1 . GLU   A 1 140 ? 29.51900  -15.67600 7.64200   1.000 18.94682 ? 184 GLU   A OE1 1 
ATOM   1052 O  OE2 . GLU   A 1 140 ? 29.83500  -14.91100 9.68900   1.000 22.04682 ? 184 GLU   A OE2 1 
ATOM   1053 N  N   . ALA   A 1 141 ? 24.82600  -15.24300 5.17500   1.000 8.12682  ? 185 ALA   A N   1 
ATOM   1054 C  CA  . ALA   A 1 141 ? 24.26600  -15.94600 4.02000   1.000 12.28682 ? 185 ALA   A CA  1 
ATOM   1055 C  C   . ALA   A 1 141 ? 24.44900  -15.15900 2.72100   1.000 7.16682  ? 185 ALA   A C   1 
ATOM   1056 O  O   . ALA   A 1 141 ? 24.68000  -15.75400 1.66000   1.000 7.78682  ? 185 ALA   A O   1 
ATOM   1057 C  CB  . ALA   A 1 141 ? 22.78800  -16.24600 4.25300   1.000 7.69682  ? 185 ALA   A CB  1 
ATOM   1058 N  N   . THR   A 1 142 ? 24.33600  -13.82400 2.76900   1.000 8.70682  ? 186 THR   A N   1 
ATOM   1059 C  CA  . THR   A 1 142 ? 24.46900  -13.07400 1.52300   1.000 7.10682  ? 186 THR   A CA  1 
ATOM   1060 C  C   . THR   A 1 142 ? 25.91300  -13.04500 1.03100   1.000 10.36682 ? 186 THR   A C   1 
ATOM   1061 O  O   . THR   A 1 142 ? 26.13900  -13.00300 -0.18600  1.000 9.88682  ? 186 THR   A O   1 
ATOM   1062 C  CB  . THR   A 1 142 ? 23.91000  -11.65300 1.65500   1.000 10.08682 ? 186 THR   A CB  1 
ATOM   1063 O  OG1 . THR   A 1 142 ? 24.64700  -10.89500 2.62600   1.000 8.89682  ? 186 THR   A OG1 1 
ATOM   1064 C  CG2 . THR   A 1 142 ? 22.44900  -11.71500 2.05500   1.000 10.20682 ? 186 THR   A CG2 1 
ATOM   1065 N  N   . VAL   A 1 143 ? 26.89200  -13.09800 1.94000   1.000 8.98682  ? 187 VAL   A N   1 
ATOM   1066 C  CA  . VAL   A 1 143 ? 28.28400  -13.22800 1.50900   1.000 9.72682  ? 187 VAL   A CA  1 
ATOM   1067 C  C   . VAL   A 1 143 ? 28.52300  -14.60400 0.89200   1.000 10.35682 ? 187 VAL   A C   1 
ATOM   1068 O  O   . VAL   A 1 143 ? 29.23000  -14.73200 -0.11500  1.000 13.06682 ? 187 VAL   A O   1 
ATOM   1069 C  CB  . VAL   A 1 143 ? 29.24100  -12.95600 2.68500   1.000 13.15682 ? 187 VAL   A CB  1 
ATOM   1070 C  CG1 . VAL   A 1 143 ? 30.69200  -13.20300 2.25700   1.000 13.17682 ? 187 VAL   A CG1 1 
ATOM   1071 C  CG2 . VAL   A 1 143 ? 29.06200  -11.51800 3.21200   1.000 10.48682 ? 187 VAL   A CG2 1 
ATOM   1072 N  N   . MET   A 1 144 ? 27.92400  -15.64900 1.47800   1.000 12.48682 ? 188 MET   A N   1 
ATOM   1073 C  CA  . MET   A 1 144 ? 28.03200  -17.00600 0.94300   1.000 11.87682 ? 188 MET   A CA  1 
ATOM   1074 C  C   . MET   A 1 144 ? 27.31900  -17.16300 -0.39500  1.000 13.21682 ? 188 MET   A C   1 
ATOM   1075 O  O   . MET   A 1 144 ? 27.71100  -18.01800 -1.19800  1.000 15.85682 ? 188 MET   A O   1 
ATOM   1076 C  CB  . MET   A 1 144 ? 27.46000  -18.02300 1.94100   1.000 11.53682 ? 188 MET   A CB  1 
ATOM   1077 C  CG  . MET   A 1 144 ? 28.17700  -18.08100 3.27500   1.000 16.07682 ? 188 MET   A CG  1 
ATOM   1078 S  SD  . MET   A 1 144 ? 27.30000  -19.05700 4.53000   1.000 16.45682 ? 188 MET   A SD  1 
ATOM   1079 C  CE  . MET   A 1 144 ? 28.45700  -18.88600 5.88800   1.000 19.30682 ? 188 MET   A CE  1 
ATOM   1080 N  N   . ARG   A 1 145 ? 26.25800  -16.39000 -0.64700  1.000 11.76682 ? 189 ARG   A N   1 
ATOM   1081 C  CA  . ARG   A 1 145 ? 25.44900  -16.55900 -1.85700  1.000 8.44682  ? 189 ARG   A CA  1 
ATOM   1082 C  C   . ARG   A 1 145 ? 24.98500  -15.21300 -2.39900  1.000 9.70682  ? 189 ARG   A C   1 
ATOM   1083 O  O   . ARG   A 1 145 ? 23.86600  -14.75600 -2.12100  1.000 10.48682 ? 189 ARG   A O   1 
ATOM   1084 C  CB  . ARG   A 1 145 ? 24.24900  -17.47300 -1.60500  1.000 10.62682 ? 189 ARG   A CB  1 
ATOM   1085 C  CG  . ARG   A 1 145 ? 23.53700  -17.84800 -2.90100  1.000 12.82682 ? 189 ARG   A CG  1 
ATOM   1086 C  CD  . ARG   A 1 145 ? 22.48400  -18.91200 -2.67700  1.000 15.11682 ? 189 ARG   A CD  1 
ATOM   1087 N  NE  . ARG   A 1 145 ? 23.08200  -20.17000 -2.24200  1.000 20.06682 ? 189 ARG   A NE  1 
ATOM   1088 C  CZ  . ARG   A 1 145 ? 22.38600  -21.26900 -1.98300  1.000 17.51682 ? 189 ARG   A CZ  1 
ATOM   1089 N  NH1 . ARG   A 1 145 ? 21.07500  -21.31200 -2.15700  1.000 18.28682 ? 189 ARG   A NH1 1 
ATOM   1090 N  NH2 . ARG   A 1 145 ? 23.01900  -22.34700 -1.54000  1.000 14.69682 ? 189 ARG   A NH2 1 
ATOM   1091 N  N   . PRO   A 1 146 ? 25.82500  -14.55500 -3.19900  1.000 10.98682 ? 190 PRO   A N   1 
ATOM   1092 C  CA  . PRO   A 1 146 ? 25.47000  -13.23100 -3.74500  1.000 12.32682 ? 190 PRO   A CA  1 
ATOM   1093 C  C   . PRO   A 1 146 ? 24.23800  -13.20200 -4.65300  1.000 13.88682 ? 190 PRO   A C   1 
ATOM   1094 O  O   . PRO   A 1 146 ? 23.78000  -12.10100 -4.99500  1.000 8.55682  ? 190 PRO   A O   1 
ATOM   1095 C  CB  . PRO   A 1 146 ? 26.73400  -12.83300 -4.52400  1.000 10.71682 ? 190 PRO   A CB  1 
ATOM   1096 C  CG  . PRO   A 1 146 ? 27.85300  -13.54800 -3.78600  1.000 12.46682 ? 190 PRO   A CG  1 
ATOM   1097 C  CD  . PRO   A 1 146 ? 27.24900  -14.88600 -3.39200  1.000 9.87682  ? 190 PRO   A CD  1 
ATOM   1098 N  N   . SER   A 1 147 ? 23.68900  -14.34400 -5.07200  1.000 10.36682 ? 191 SER   A N   1 
ATOM   1099 C  CA  . SER   A 1 147 ? 22.52200  -14.29100 -5.94700  1.000 8.25682  ? 191 SER   A CA  1 
ATOM   1100 C  C   . SER   A 1 147 ? 21.20600  -14.14300 -5.19400  1.000 9.70682  ? 191 SER   A C   1 
ATOM   1101 O  O   . SER   A 1 147 ? 20.15300  -14.12100 -5.83600  1.000 10.32682 ? 191 SER   A O   1 
ATOM   1102 C  CB  . SER   A 1 147 ? 22.45900  -15.53700 -6.83500  1.000 12.13682 ? 191 SER   A CB  1 
ATOM   1103 O  OG  . SER   A 1 147 ? 22.44000  -16.71900 -6.06000  1.000 12.06682 ? 191 SER   A OG  1 
ATOM   1104 N  N   . LEU   A 1 148 ? 21.22500  -14.06400 -3.86500  1.000 10.14682 ? 192 LEU   A N   1 
ATOM   1105 C  CA  . LEU   A 1 148 ? 19.98800  -13.87000 -3.11300  1.000 9.48682  ? 192 LEU   A CA  1 
ATOM   1106 C  C   . LEU   A 1 148 ? 19.37400  -12.50900 -3.44600  1.000 10.00682 ? 192 LEU   A C   1 
ATOM   1107 O  O   . LEU   A 1 148 ? 20.08000  -11.53700 -3.72000  1.000 8.56682  ? 192 LEU   A O   1 
ATOM   1108 C  CB  . LEU   A 1 148 ? 20.25600  -13.97200 -1.60800  1.000 7.38682  ? 192 LEU   A CB  1 
ATOM   1109 C  CG  . LEU   A 1 148 ? 20.69000  -15.32500 -1.01100  1.000 9.69682  ? 192 LEU   A CG  1 
ATOM   1110 C  CD1 . LEU   A 1 148 ? 21.23000  -15.12200 0.41200   1.000 9.46682  ? 192 LEU   A CD1 1 
ATOM   1111 C  CD2 . LEU   A 1 148 ? 19.54100  -16.32000 -0.99800  1.000 6.76682  ? 192 LEU   A CD2 1 
ATOM   1112 N  N   . LYS   A 1 149 ? 18.03900  -12.44300 -3.42200  1.000 9.92682  ? 193 LYS   A N   1 
ATOM   1113 C  CA  . LYS   A 1 149 ? 17.35000  -11.22400 -3.83900  1.000 9.35682  ? 193 LYS   A CA  1 
ATOM   1114 C  C   . LYS   A 1 149 ? 17.23400  -10.19400 -2.71500  1.000 9.62682  ? 193 LYS   A C   1 
ATOM   1115 O  O   . LYS   A 1 149 ? 17.20300  -8.98500  -2.99200  1.000 6.98682  ? 193 LYS   A O   1 
ATOM   1116 C  CB  . LYS   A 1 149 ? 15.95100  -11.56400 -4.37500  1.000 8.59682  ? 193 LYS   A CB  1 
ATOM   1117 C  CG  . LYS   A 1 149 ? 15.96000  -12.38100 -5.66600  1.000 12.66682 ? 193 LYS   A CG  1 
ATOM   1118 C  CD  . LYS   A 1 149 ? 16.64000  -11.61800 -6.78400  1.000 14.11682 ? 193 LYS   A CD  1 
ATOM   1119 C  CE  . LYS   A 1 149 ? 16.69400  -12.42600 -8.06600  1.000 23.18682 ? 193 LYS   A CE  1 
ATOM   1120 N  NZ  . LYS   A 1 149 ? 17.43600  -11.66900 -9.11100  1.000 28.85682 ? 193 LYS   A NZ  1 
ATOM   1121 N  N   . ALA   A 1 150 ? 17.17300  -10.62900 -1.45700  1.000 8.77682  ? 194 ALA   A N   1 
ATOM   1122 C  CA  . ALA   A 1 150 ? 16.97300  -9.68600  -0.36300  1.000 6.55682  ? 194 ALA   A CA  1 
ATOM   1123 C  C   . ALA   A 1 150 ? 17.45700  -10.29800 0.94700   1.000 9.78682  ? 194 ALA   A C   1 
ATOM   1124 O  O   . ALA   A 1 150 ? 17.49300  -11.52200 1.11300   1.000 7.48682  ? 194 ALA   A O   1 
ATOM   1125 C  CB  . ALA   A 1 150 ? 15.50100  -9.26800  -0.25100  1.000 6.12682  ? 194 ALA   A CB  1 
ATOM   1126 N  N   . SER   A 1 151 ? 17.81100  -9.42200  1.88700   1.000 7.85682  ? 195 SER   A N   1 
ATOM   1127 C  CA  . SER   A 1 151 ? 18.28300  -9.83800  3.20300   1.000 8.78682  ? 195 SER   A CA  1 
ATOM   1128 C  C   . SER   A 1 151 ? 17.74700  -8.87500  4.25300   1.000 6.89682  ? 195 SER   A C   1 
ATOM   1129 O  O   . SER   A 1 151 ? 17.83000  -7.66200  4.06800   1.000 6.98682  ? 195 SER   A O   1 
ATOM   1130 C  CB  . SER   A 1 151 ? 19.81900  -9.87700  3.24200   1.000 7.37682  ? 195 SER   A CB  1 
ATOM   1131 O  OG  . SER   A 1 151 ? 20.31900  -9.95700  4.56400   1.000 11.51682 ? 195 SER   A OG  1 
ATOM   1132 N  N   . ILE   A 1 152 ? 17.19000  -9.40600  5.34300   1.000 5.72682  ? 196 ILE   A N   1 
ATOM   1133 C  CA  . ILE   A 1 152 ? 16.62600  -8.55800  6.39900   1.000 6.41682  ? 196 ILE   A CA  1 
ATOM   1134 C  C   . ILE   A 1 152 ? 17.14400  -8.99100  7.76800   1.000 7.99682  ? 196 ILE   A C   1 
ATOM   1135 O  O   . ILE   A 1 152 ? 16.56600  -9.89500  8.39800   1.000 5.65682  ? 196 ILE   A O   1 
ATOM   1136 C  CB  . ILE   A 1 152 ? 15.08800  -8.56500  6.36700   1.000 6.79682  ? 196 ILE   A CB  1 
ATOM   1137 C  CG1 . ILE   A 1 152 ? 14.58400  -8.16200  4.97000   1.000 6.97682  ? 196 ILE   A CG1 1 
ATOM   1138 C  CG2 . ILE   A 1 152 ? 14.53600  -7.61200  7.46200   1.000 6.52682  ? 196 ILE   A CG2 1 
ATOM   1139 C  CD1 . ILE   A 1 152 ? 13.03800  -8.18600  4.78600   1.000 7.39682  ? 196 ILE   A CD1 1 
ATOM   1140 N  N   . PRO   A 1 153 ? 18.23000  -8.38700  8.26100   1.000 8.68682  ? 197 PRO   A N   1 
ATOM   1141 C  CA  . PRO   A 1 153 ? 18.72900  -8.69800  9.61300   1.000 5.33682  ? 197 PRO   A CA  1 
ATOM   1142 C  C   . PRO   A 1 153 ? 17.95600  -7.90200  10.65700  1.000 7.54682  ? 197 PRO   A C   1 
ATOM   1143 O  O   . PRO   A 1 153 ? 17.91200  -6.67000  10.60500  1.000 7.76682  ? 197 PRO   A O   1 
ATOM   1144 C  CB  . PRO   A 1 153 ? 20.20800  -8.27400  9.55600   1.000 5.44682  ? 197 PRO   A CB  1 
ATOM   1145 C  CG  . PRO   A 1 153 ? 20.53000  -8.11800  8.07500   1.000 6.31682  ? 197 PRO   A CG  1 
ATOM   1146 C  CD  . PRO   A 1 153 ? 19.23600  -7.67500  7.45300   1.000 7.57682  ? 197 PRO   A CD  1 
ATOM   1147 N  N   . LEU   A 1 154 ? 17.33100  -8.61400  11.59300  1.000 5.99682  ? 198 LEU   A N   1 
ATOM   1148 C  CA  . LEU   A 1 154 ? 16.48800  -8.03600  12.63500  1.000 6.03682  ? 198 LEU   A CA  1 
ATOM   1149 C  C   . LEU   A 1 154 ? 17.26200  -8.01800  13.94900  1.000 8.20682  ? 198 LEU   A C   1 
ATOM   1150 O  O   . LEU   A 1 154 ? 17.67700  -9.07600  14.44000  1.000 6.50682  ? 198 LEU   A O   1 
ATOM   1151 C  CB  . LEU   A 1 154 ? 15.20200  -8.84300  12.81100  1.000 6.78682  ? 198 LEU   A CB  1 
ATOM   1152 C  CG  . LEU   A 1 154 ? 14.36800  -9.17800  11.57700  1.000 4.45682  ? 198 LEU   A CG  1 
ATOM   1153 C  CD1 . LEU   A 1 154 ? 13.41500  -10.34400 11.86000  1.000 5.97682  ? 198 LEU   A CD1 1 
ATOM   1154 C  CD2 . LEU   A 1 154 ? 13.61000  -7.95200  11.13000  1.000 8.16682  ? 198 LEU   A CD2 1 
ATOM   1155 N  N   . THR   A 1 155 ? 17.39100  -6.82800  14.54100  1.000 5.03682  ? 199 THR   A N   1 
ATOM   1156 C  CA  . THR   A 1 155 ? 18.26300  -6.55500  15.67800  1.000 6.07682  ? 199 THR   A CA  1 
ATOM   1157 C  C   . THR   A 1 155 ? 19.48500  -7.47200  15.62200  1.000 8.39682  ? 199 THR   A C   1 
ATOM   1158 O  O   . THR   A 1 155 ? 19.66500  -8.30700  16.51600  1.000 5.72682  ? 199 THR   A O   1 
ATOM   1159 C  CB  . THR   A 1 155 ? 17.50600  -6.72000  17.00300  1.000 8.91682  ? 199 THR   A CB  1 
ATOM   1160 O  OG1 . THR   A 1 155 ? 16.99300  -8.05300  17.11400  1.000 9.94682  ? 199 THR   A OG1 1 
ATOM   1161 C  CG2 . THR   A 1 155 ? 16.35100  -5.71600  17.11600  1.000 7.69682  ? 199 THR   A CG2 1 
ATOM   1162 N  N   . PRO   A 1 156 ? 20.32300  -7.36200  14.58400  1.000 5.67682  ? 200 PRO   A N   1 
ATOM   1163 C  CA  . PRO   A 1 156 ? 21.36900  -8.37100  14.34300  1.000 7.16682  ? 200 PRO   A CA  1 
ATOM   1164 C  C   . PRO   A 1 156 ? 22.54100  -8.28500  15.30500  1.000 5.64682  ? 200 PRO   A C   1 
ATOM   1165 O  O   . PRO   A 1 156 ? 22.93600  -7.20300  15.74300  1.000 9.17682  ? 200 PRO   A O   1 
ATOM   1166 C  CB  . PRO   A 1 156 ? 21.83600  -8.04000  12.91700  1.000 7.27682  ? 200 PRO   A CB  1 
ATOM   1167 C  CG  . PRO   A 1 156 ? 21.64700  -6.53000  12.84400  1.000 4.49682  ? 200 PRO   A CG  1 
ATOM   1168 C  CD  . PRO   A 1 156 ? 20.31000  -6.33500  13.52100  1.000 6.15682  ? 200 PRO   A CD  1 
ATOM   1169 N  N   . TRP   A 1 157 ? 23.12600  -9.45200  15.59100  1.000 4.72682  ? 201 TRP   A N   1 
ATOM   1170 C  CA  . TRP   A 1 157 ? 24.31100  -9.59300  16.43600  1.000 7.00682  ? 201 TRP   A CA  1 
ATOM   1171 C  C   . TRP   A 1 157 ? 25.41700  -10.31800 15.67100  1.000 6.38682  ? 201 TRP   A C   1 
ATOM   1172 O  O   . TRP   A 1 157 ? 25.17200  -11.37400 15.07600  1.000 9.63682  ? 201 TRP   A O   1 
ATOM   1173 C  CB  . TRP   A 1 157 ? 23.98100  -10.37100 17.71900  1.000 7.81682  ? 201 TRP   A CB  1 
ATOM   1174 C  CG  . TRP   A 1 157 ? 25.07200  -10.37100 18.76400  1.000 8.94682  ? 201 TRP   A CG  1 
ATOM   1175 C  CD1 . TRP   A 1 157 ? 25.14600  -9.57700  19.87900  1.000 10.54682 ? 201 TRP   A CD1 1 
ATOM   1176 C  CD2 . TRP   A 1 157 ? 26.22500  -11.22400 18.80600  1.000 10.80682 ? 201 TRP   A CD2 1 
ATOM   1177 N  NE1 . TRP   A 1 157 ? 26.27900  -9.88100  20.61100  1.000 9.61682  ? 201 TRP   A NE1 1 
ATOM   1178 C  CE2 . TRP   A 1 157 ? 26.95400  -10.89000 19.97500  1.000 12.69682 ? 201 TRP   A CE2 1 
ATOM   1179 C  CE3 . TRP   A 1 157 ? 26.71200  -12.24200 17.97500  1.000 10.83682 ? 201 TRP   A CE3 1 
ATOM   1180 C  CZ2 . TRP   A 1 157 ? 28.14400  -11.53100 20.31900  1.000 13.42682 ? 201 TRP   A CZ2 1 
ATOM   1181 C  CZ3 . TRP   A 1 157 ? 27.88700  -12.87900 18.32500  1.000 11.35682 ? 201 TRP   A CZ3 1 
ATOM   1182 C  CH2 . TRP   A 1 157 ? 28.58700  -12.52700 19.48500  1.000 11.42682 ? 201 TRP   A CH2 1 
ATOM   1183 N  N   . HIS   A 1 158 ? 26.63400  -9.76100  15.69900  1.000 6.52682  ? 202 HIS   A N   1 
ATOM   1184 C  CA  . HIS   A 1 158 ? 27.78800  -10.33700 15.01900  1.000 6.73682  ? 202 HIS   A CA  1 
ATOM   1185 C  C   . HIS   A 1 158 ? 29.05300  -9.62300  15.48800  1.000 9.42682  ? 202 HIS   A C   1 
ATOM   1186 O  O   . HIS   A 1 158 ? 29.07300  -8.39200  15.59600  1.000 5.98682  ? 202 HIS   A O   1 
ATOM   1187 C  CB  . HIS   A 1 158 ? 27.65400  -10.21500 13.49100  1.000 9.69682  ? 202 HIS   A CB  1 
ATOM   1188 C  CG  . HIS   A 1 158 ? 28.39200  -11.27200 12.72600  1.000 9.56682  ? 202 HIS   A CG  1 
ATOM   1189 N  ND1 . HIS   A 1 158 ? 29.76300  -11.42300 12.78700  1.000 11.12682 ? 202 HIS   A ND1 1 
ATOM   1190 C  CD2 . HIS   A 1 158 ? 27.94900  -12.22500 11.87100  1.000 10.93682 ? 202 HIS   A CD2 1 
ATOM   1191 C  CE1 . HIS   A 1 158 ? 30.12900  -12.42400 12.00700  1.000 13.52682 ? 202 HIS   A CE1 1 
ATOM   1192 N  NE2 . HIS   A 1 158 ? 29.04800  -12.92700 11.44000  1.000 12.13682 ? 202 HIS   A NE2 1 
ATOM   1193 N  N   . LEU   A 1 159 ? 30.11400  -10.39500 15.73800  1.000 9.93682  ? 203 LEU   A N   1 
ATOM   1194 C  CA  . LEU   A 1 159 ? 31.38100  -9.77900  16.12800  1.000 10.09682 ? 203 LEU   A CA  1 
ATOM   1195 C  C   . LEU   A 1 159 ? 32.12000  -9.14300  14.95400  1.000 11.52682 ? 203 LEU   A C   1 
ATOM   1196 O  O   . LEU   A 1 159 ? 32.98000  -8.28800  15.18000  1.000 8.06682  ? 203 LEU   A O   1 
ATOM   1197 C  CB  . LEU   A 1 159 ? 32.29000  -10.80300 16.81000  1.000 15.64682 ? 203 LEU   A CB  1 
ATOM   1198 C  CG  . LEU   A 1 159 ? 31.77300  -11.40100 18.12700  1.000 14.94682 ? 203 LEU   A CG  1 
ATOM   1199 C  CD1 . LEU   A 1 159 ? 32.79300  -12.36200 18.72600  1.000 21.08682 ? 203 LEU   A CD1 1 
ATOM   1200 C  CD2 . LEU   A 1 159 ? 31.36500  -10.33100 19.14800  1.000 15.39682 ? 203 LEU   A CD2 1 
ATOM   1201 N  N   . ASP   A 1 160 ? 31.83200  -9.55300  13.71900  1.000 10.35682 ? 204 ASP   A N   1 
ATOM   1202 C  CA  . ASP   A 1 160 ? 32.43300  -8.93000  12.53600  1.000 13.66682 ? 204 ASP   A CA  1 
ATOM   1203 C  C   . ASP   A 1 160 ? 31.63000  -7.68700  12.15800  1.000 12.78682 ? 204 ASP   A C   1 
ATOM   1204 O  O   . ASP   A 1 160 ? 30.43700  -7.78800  11.84900  1.000 13.41682 ? 204 ASP   A O   1 
ATOM   1205 C  CB  . ASP   A 1 160 ? 32.47000  -9.92200  11.37300  1.000 12.53682 ? 204 ASP   A CB  1 
ATOM   1206 C  CG  . ASP   A 1 160 ? 33.26800  -9.40800  10.17100  1.000 14.41682 ? 204 ASP   A CG  1 
ATOM   1207 O  OD1 . ASP   A 1 160 ? 33.78400  -8.27300  10.21500  1.000 16.30682 ? 204 ASP   A OD1 1 
ATOM   1208 O  OD2 . ASP   A 1 160 ? 33.37900  -10.14500 9.16900   1.000 24.81682 ? 204 ASP   A OD2 1 
ATOM   1209 N  N   . LYS   A 1 161 ? 32.27700  -6.51700  12.17000  1.000 10.92682 ? 205 LYS   A N   1 
ATOM   1210 C  CA  . LYS   A 1 161 ? 31.57900  -5.24200  11.99600  1.000 11.51682 ? 205 LYS   A CA  1 
ATOM   1211 C  C   . LYS   A 1 161 ? 31.66700  -4.67800  10.58100  1.000 16.15682 ? 205 LYS   A C   1 
ATOM   1212 O  O   . LYS   A 1 161 ? 31.11900  -3.59400  10.33000  1.000 15.09682 ? 205 LYS   A O   1 
ATOM   1213 C  CB  . LYS   A 1 161 ? 32.12300  -4.19000  12.97000  1.000 11.14682 ? 205 LYS   A CB  1 
ATOM   1214 C  CG  . LYS   A 1 161 ? 32.26600  -4.64900  14.42200  1.000 12.49682 ? 205 LYS   A CG  1 
ATOM   1215 C  CD  . LYS   A 1 161 ? 30.90600  -4.96400  15.04000  1.000 7.05682  ? 205 LYS   A CD  1 
ATOM   1216 C  CE  . LYS   A 1 161 ? 31.06100  -5.45600  16.45900  1.000 10.18682 ? 205 LYS   A CE  1 
ATOM   1217 N  NZ  . LYS   A 1 161 ? 29.77000  -5.96000  16.97000  1.000 10.12682 ? 205 LYS   A NZ  1 
ATOM   1218 N  N   . THR   A 1 162 ? 32.32700  -5.37400  9.65200   1.000 10.52682 ? 206 THR   A N   1 
ATOM   1219 C  CA  . THR   A 1 162 ? 32.55200  -4.87400  8.29800   1.000 10.49682 ? 206 THR   A CA  1 
ATOM   1220 C  C   . THR   A 1 162 ? 31.85200  -5.79100  7.30700   1.000 12.20682 ? 206 THR   A C   1 
ATOM   1221 O  O   . THR   A 1 162 ? 32.13200  -6.99500  7.27000   1.000 13.48682 ? 206 THR   A O   1 
ATOM   1222 C  CB  . THR   A 1 162 ? 34.04900  -4.81500  7.97100   1.000 15.45682 ? 206 THR   A CB  1 
ATOM   1223 O  OG1 . THR   A 1 162 ? 34.75500  -4.18900  9.04600   1.000 17.67682 ? 206 THR   A OG1 1 
ATOM   1224 C  CG2 . THR   A 1 162 ? 34.27800  -4.02600  6.69100   1.000 14.67682 ? 206 THR   A CG2 1 
ATOM   1225 N  N   . TRP   A 1 163 ? 30.96600  -5.22700  6.49400   1.000 7.18682  ? 207 TRP   A N   1 
ATOM   1226 C  CA  . TRP   A 1 163 ? 30.22200  -6.01400  5.51200   1.000 11.94682 ? 207 TRP   A CA  1 
ATOM   1227 C  C   . TRP   A 1 163 ? 30.27900  -5.37300  4.13000   1.000 11.92682 ? 207 TRP   A C   1 
ATOM   1228 O  O   . TRP   A 1 163 ? 29.28400  -5.31700  3.40400   1.000 7.38682  ? 207 TRP   A O   1 
ATOM   1229 C  CB  . TRP   A 1 163 ? 28.78900  -6.22400  5.98700   1.000 6.82682  ? 207 TRP   A CB  1 
ATOM   1230 C  CG  . TRP   A 1 163 ? 28.80900  -7.04300  7.23100   1.000 9.22682  ? 207 TRP   A CG  1 
ATOM   1231 C  CD1 . TRP   A 1 163 ? 28.85600  -6.58800  8.51400   1.000 8.34682  ? 207 TRP   A CD1 1 
ATOM   1232 C  CD2 . TRP   A 1 163 ? 28.85000  -8.47300  7.30600   1.000 10.74682 ? 207 TRP   A CD2 1 
ATOM   1233 N  NE1 . TRP   A 1 163 ? 28.90700  -7.65300  9.39700   1.000 11.22682 ? 207 TRP   A NE1 1 
ATOM   1234 C  CE2 . TRP   A 1 163 ? 28.91400  -8.82000  8.67600   1.000 8.91682  ? 207 TRP   A CE2 1 
ATOM   1235 C  CE3 . TRP   A 1 163 ? 28.83600  -9.49600  6.34700   1.000 7.74682  ? 207 TRP   A CE3 1 
ATOM   1236 C  CZ2 . TRP   A 1 163 ? 28.94600  -10.14100 9.10900   1.000 9.88682  ? 207 TRP   A CZ2 1 
ATOM   1237 C  CZ3 . TRP   A 1 163 ? 28.87800  -10.81800 6.78300   1.000 9.78682  ? 207 TRP   A CZ3 1 
ATOM   1238 C  CH2 . TRP   A 1 163 ? 28.93900  -11.12400 8.15000   1.000 12.91682 ? 207 TRP   A CH2 1 
ATOM   1239 N  N   . GLY   A 1 164 ? 31.46400  -4.92500  3.72600   1.000 9.79682  ? 208 GLY   A N   1 
ATOM   1240 C  CA  . GLY   A 1 164 ? 31.61900  -4.20700  2.47900   1.000 11.48682 ? 208 GLY   A CA  1 
ATOM   1241 C  C   . GLY   A 1 164 ? 31.55600  -5.04300  1.21700   1.000 11.64682 ? 208 GLY   A C   1 
ATOM   1242 O  O   . GLY   A 1 164 ? 31.62800  -4.47500  0.12600   1.000 13.18682 ? 208 GLY   A O   1 
ATOM   1243 N  N   . GLN   A 1 165 ? 31.45500  -6.36900  1.32200   1.000 10.26682 ? 209 GLN   A N   1 
ATOM   1244 C  CA  . GLN   A 1 165 ? 31.34400  -7.22600  0.15100   1.000 17.53682 ? 209 GLN   A CA  1 
ATOM   1245 C  C   . GLN   A 1 165 ? 29.91300  -7.69500  -0.10300  1.000 15.66682 ? 209 GLN   A C   1 
ATOM   1246 O  O   . GLN   A 1 165 ? 29.68700  -8.47000  -1.03700  1.000 12.81682 ? 209 GLN   A O   1 
ATOM   1247 C  CB  . GLN   A 1 165 ? 32.27500  -8.43500  0.29100   1.000 20.68682 ? 209 GLN   A CB  1 
ATOM   1248 C  CG  . GLN   A 1 165 ? 33.74200  -8.06000  0.53500   1.000 31.54682 ? 209 GLN   A CG  1 
ATOM   1249 C  CD  . GLN   A 1 165 ? 34.33600  -7.20400  -0.58700  1.000 37.40682 ? 209 GLN   A CD  1 
ATOM   1250 O  OE1 . GLN   A 1 165 ? 34.83900  -6.09500  -0.35000  1.000 38.32682 ? 209 GLN   A OE1 1 
ATOM   1251 N  NE2 . GLN   A 1 165 ? 34.28400  -7.72100  -1.81400  1.000 36.53682 ? 209 GLN   A NE2 1 
ATOM   1252 N  N   . VAL   A 1 166 ? 28.95100  -7.25400  0.71200   1.000 12.75682 ? 210 VAL   A N   1 
ATOM   1253 C  CA  . VAL   A 1 166 ? 27.56500  -7.66700  0.53500   1.000 9.62682  ? 210 VAL   A CA  1 
ATOM   1254 C  C   . VAL   A 1 166 ? 27.03200  -7.08400  -0.76600  1.000 11.07682 ? 210 VAL   A C   1 
ATOM   1255 O  O   . VAL   A 1 166 ? 27.11600  -5.87400  -0.99900  1.000 6.77682  ? 210 VAL   A O   1 
ATOM   1256 C  CB  . VAL   A 1 166 ? 26.71800  -7.22500  1.74000   1.000 8.80682  ? 210 VAL   A CB  1 
ATOM   1257 C  CG1 . VAL   A 1 166 ? 25.21900  -7.45100  1.47100   1.000 10.59682 ? 210 VAL   A CG1 1 
ATOM   1258 C  CG2 . VAL   A 1 166 ? 27.14300  -7.99400  2.98600   1.000 11.56682 ? 210 VAL   A CG2 1 
ATOM   1259 N  N   . GLN   A 1 167 ? 26.46400  -7.94300  -1.61500  1.000 8.22682  ? 211 GLN   A N   1 
ATOM   1260 C  CA  . GLN   A 1 167 ? 25.86200  -7.51800  -2.87000  1.000 11.42682 ? 211 GLN   A CA  1 
ATOM   1261 C  C   . GLN   A 1 167 ? 24.34500  -7.68700  -2.90400  1.000 10.81682 ? 211 GLN   A C   1 
ATOM   1262 O  O   . GLN   A 1 167 ? 23.73200  -7.44700  -3.94600  1.000 9.10682  ? 211 GLN   A O   1 
ATOM   1263 C  CB  . GLN   A 1 167 ? 26.49400  -8.28900  -4.03300  1.000 7.47682  ? 211 GLN   A CB  1 
ATOM   1264 C  CG  . GLN   A 1 167 ? 27.96700  -7.98800  -4.19600  1.000 13.97682 ? 211 GLN   A CG  1 
ATOM   1265 C  CD  . GLN   A 1 167 ? 28.57100  -8.67800  -5.39100  1.000 23.74682 ? 211 GLN   A CD  1 
ATOM   1266 O  OE1 . GLN   A 1 167 ? 28.52200  -8.16400  -6.50900  1.000 24.94682 ? 211 GLN   A OE1 1 
ATOM   1267 N  NE2 . GLN   A 1 167 ? 29.14200  -9.85500  -5.16500  1.000 18.77682 ? 211 GLN   A NE2 1 
ATOM   1268 N  N   . VAL   A 1 168 ? 23.72800  -8.06900  -1.79800  1.000 10.44682 ? 212 VAL   A N   1 
ATOM   1269 C  CA  . VAL   A 1 168 ? 22.30200  -8.38600  -1.74700  1.000 10.19682 ? 212 VAL   A CA  1 
ATOM   1270 C  C   . VAL   A 1 168 ? 21.58300  -7.22800  -1.06500  1.000 7.40682  ? 212 VAL   A C   1 
ATOM   1271 O  O   . VAL   A 1 168 ? 22.00200  -6.82200  0.02700   1.000 9.45682  ? 212 VAL   A O   1 
ATOM   1272 C  CB  . VAL   A 1 168 ? 22.05400  -9.70200  -0.98600  1.000 7.99682  ? 212 VAL   A CB  1 
ATOM   1273 C  CG1 . VAL   A 1 168 ? 20.54700  -9.88500  -0.73100  1.000 6.07682  ? 212 VAL   A CG1 1 
ATOM   1274 C  CG2 . VAL   A 1 168 ? 22.65000  -10.89100 -1.74200  1.000 11.50682 ? 212 VAL   A CG2 1 
ATOM   1275 N  N   . PRO   A 1 169 ? 20.48800  -6.68200  -1.65400  1.000 8.16682  ? 213 PRO   A N   1 
ATOM   1276 C  CA  . PRO   A 1 169 ? 19.77500  -5.57000  -0.99200  1.000 10.78682 ? 213 PRO   A CA  1 
ATOM   1277 C  C   . PRO   A 1 169 ? 19.40100  -5.89900  0.45000   1.000 8.11682  ? 213 PRO   A C   1 
ATOM   1278 O  O   . PRO   A 1 169 ? 18.75000  -6.91600  0.72200   1.000 5.62682  ? 213 PRO   A O   1 
ATOM   1279 C  CB  . PRO   A 1 169 ? 18.53800  -5.37000  -1.87800  1.000 9.63682  ? 213 PRO   A CB  1 
ATOM   1280 C  CG  . PRO   A 1 169 ? 18.99400  -5.82100  -3.23200  1.000 10.39682 ? 213 PRO   A CG  1 
ATOM   1281 C  CD  . PRO   A 1 169 ? 19.91600  -6.99300  -2.97400  1.000 10.08682 ? 213 PRO   A CD  1 
ATOM   1282 N  N   . THR   A 1 170 ? 19.82400  -5.05900  1.39300   1.000 7.06682  ? 214 THR   A N   1 
ATOM   1283 C  CA  . THR   A 1 170 ? 19.80100  -5.42300  2.80900   1.000 6.98682  ? 214 THR   A CA  1 
ATOM   1284 C  C   . THR   A 1 170 ? 19.09300  -4.35400  3.63400   1.000 7.22682  ? 214 THR   A C   1 
ATOM   1285 O  O   . THR   A 1 170 ? 19.41200  -3.16800  3.52600   1.000 7.32682  ? 214 THR   A O   1 
ATOM   1286 C  CB  . THR   A 1 170 ? 21.22500  -5.63700  3.34400   1.000 8.34682  ? 214 THR   A CB  1 
ATOM   1287 O  OG1 . THR   A 1 170 ? 21.83800  -6.74500  2.66900   1.000 6.16682  ? 214 THR   A OG1 1 
ATOM   1288 C  CG2 . THR   A 1 170 ? 21.21500  -5.90300  4.85900   1.000 9.12682  ? 214 THR   A CG2 1 
ATOM   1289 N  N   . PHE   A 1 171 ? 18.17900  -4.79200  4.50000   1.000 7.47682  ? 215 PHE   A N   1 
ATOM   1290 C  CA  . PHE   A 1 171 ? 17.32400  -3.93900  5.32400   1.000 5.64682  ? 215 PHE   A CA  1 
ATOM   1291 C  C   . PHE   A 1 171 ? 17.57200  -4.32100  6.77600   1.000 7.61682  ? 215 PHE   A C   1 
ATOM   1292 O  O   . PHE   A 1 171 ? 17.12400  -5.38200  7.22400   1.000 6.54682  ? 215 PHE   A O   1 
ATOM   1293 C  CB  . PHE   A 1 171 ? 15.85500  -4.13900  4.95300   1.000 5.56682  ? 215 PHE   A CB  1 
ATOM   1294 C  CG  . PHE   A 1 171 ? 14.88300  -3.28700  5.73700   1.000 6.66682  ? 215 PHE   A CG  1 
ATOM   1295 C  CD1 . PHE   A 1 171 ? 15.25600  -2.05300  6.26800   1.000 5.12682  ? 215 PHE   A CD1 1 
ATOM   1296 C  CD2 . PHE   A 1 171 ? 13.57300  -3.72300  5.91600   1.000 7.14682  ? 215 PHE   A CD2 1 
ATOM   1297 C  CE1 . PHE   A 1 171 ? 14.34400  -1.27500  6.97900   1.000 5.88682  ? 215 PHE   A CE1 1 
ATOM   1298 C  CE2 . PHE   A 1 171 ? 12.64300  -2.95200  6.61500   1.000 7.03682  ? 215 PHE   A CE2 1 
ATOM   1299 C  CZ  . PHE   A 1 171 ? 13.03500  -1.71600  7.15500   1.000 7.18682  ? 215 PHE   A CZ  1 
ATOM   1300 N  N   . ILE   A 1 172 ? 18.30000  -3.48000  7.50200   1.000 7.03682  ? 216 ILE   A N   1 
ATOM   1301 C  CA  . ILE   A 1 172 ? 18.63100  -3.73700  8.90300   1.000 9.68682  ? 216 ILE   A CA  1 
ATOM   1302 C  C   . ILE   A 1 172 ? 17.64600  -2.99900  9.79300   1.000 7.28682  ? 216 ILE   A C   1 
ATOM   1303 O  O   . ILE   A 1 172 ? 17.47800  -1.77900  9.67500   1.000 7.73682  ? 216 ILE   A O   1 
ATOM   1304 C  CB  . ILE   A 1 172 ? 20.07100  -3.31600  9.22700   1.000 5.41682  ? 216 ILE   A CB  1 
ATOM   1305 C  CG1 . ILE   A 1 172 ? 21.05100  -4.21500  8.47700   1.000 5.81682  ? 216 ILE   A CG1 1 
ATOM   1306 C  CG2 . ILE   A 1 172 ? 20.29500  -3.33600  10.74000  1.000 5.89682  ? 216 ILE   A CG2 1 
ATOM   1307 C  CD1 . ILE   A 1 172 ? 22.47300  -3.75300  8.55600   1.000 7.95682  ? 216 ILE   A CD1 1 
ATOM   1308 N  N   . ILE   A 1 173 ? 17.00000  -3.73000  10.68900  1.000 5.77682  ? 217 ILE   A N   1 
ATOM   1309 C  CA  . ILE   A 1 173 ? 16.07700  -3.14600  11.65400  1.000 5.98682  ? 217 ILE   A CA  1 
ATOM   1310 C  C   . ILE   A 1 173 ? 16.75900  -3.16100  13.01500  1.000 7.88682  ? 217 ILE   A C   1 
ATOM   1311 O  O   . ILE   A 1 173 ? 17.14100  -4.22800  13.50700  1.000 7.71682  ? 217 ILE   A O   1 
ATOM   1312 C  CB  . ILE   A 1 173 ? 14.74100  -3.90200  11.68300  1.000 6.16682  ? 217 ILE   A CB  1 
ATOM   1313 C  CG1 . ILE   A 1 173 ? 14.09100  -3.85800  10.29200  1.000 6.39682  ? 217 ILE   A CG1 1 
ATOM   1314 C  CG2 . ILE   A 1 173 ? 13.81600  -3.31700  12.75000  1.000 10.70682 ? 217 ILE   A CG2 1 
ATOM   1315 C  CD1 . ILE   A 1 173 ? 12.69500  -4.50400  10.23200  1.000 7.21682  ? 217 ILE   A CD1 1 
ATOM   1316 N  N   . GLY   A 1 174 ? 16.91900  -1.97800  13.62000  1.000 7.42682  ? 218 GLY   A N   1 
ATOM   1317 C  CA  . GLY   A 1 174 ? 17.50100  -1.89400  14.95500  1.000 7.35682  ? 218 GLY   A CA  1 
ATOM   1318 C  C   . GLY   A 1 174 ? 16.49400  -1.50700  16.02400  1.000 7.91682  ? 218 GLY   A C   1 
ATOM   1319 O  O   . GLY   A 1 174 ? 15.42500  -0.97400  15.69900  1.000 6.98682  ? 218 GLY   A O   1 
ATOM   1320 N  N   . ALA   A 1 175 ? 16.81700  -1.77500  17.29600  1.000 8.10682  ? 219 ALA   A N   1 
ATOM   1321 C  CA  . ALA   A 1 175 ? 15.95900  -1.45600  18.43600  1.000 8.35682  ? 219 ALA   A CA  1 
ATOM   1322 C  C   . ALA   A 1 175 ? 16.68800  -0.47000  19.34200  1.000 6.07682  ? 219 ALA   A C   1 
ATOM   1323 O  O   . ALA   A 1 175 ? 17.75900  -0.79000  19.86600  1.000 6.61682  ? 219 ALA   A O   1 
ATOM   1324 C  CB  . ALA   A 1 175 ? 15.58800  -2.72200  19.21500  1.000 6.41682  ? 219 ALA   A CB  1 
ATOM   1325 N  N   . GLU   A 1 176 ? 16.09100  0.71100   19.54900  1.000 6.20682  ? 220 GLU   A N   1 
ATOM   1326 C  CA  . GLU   A 1 176 ? 16.82400  1.84300   20.12500  1.000 8.68682  ? 220 GLU   A CA  1 
ATOM   1327 C  C   . GLU   A 1 176 ? 17.46900  1.50300   21.46500  1.000 7.54682  ? 220 GLU   A C   1 
ATOM   1328 O  O   . GLU   A 1 176 ? 18.61800  1.88000   21.71700  1.000 7.77682  ? 220 GLU   A O   1 
ATOM   1329 C  CB  . GLU   A 1 176 ? 15.90500  3.05900   20.29800  1.000 8.42682  ? 220 GLU   A CB  1 
ATOM   1330 C  CG  . GLU   A 1 176 ? 16.62800  4.24900   20.94100  1.000 9.78682  ? 220 GLU   A CG  1 
ATOM   1331 C  CD  . GLU   A 1 176 ? 15.69700  5.40200   21.31400  1.000 18.24682 ? 220 GLU   A CD  1 
ATOM   1332 O  OE1 . GLU   A 1 176 ? 14.46500  5.19600   21.42900  1.000 13.88682 ? 220 GLU   A OE1 1 
ATOM   1333 O  OE2 . GLU   A 1 176 ? 16.20900  6.52800   21.47400  1.000 18.33682 ? 220 GLU   A OE2 1 
ATOM   1334 N  N   . LEU   A 1 177 ? 16.74100  0.82000   22.34900  1.000 9.21682  ? 221 LEU   A N   1 
ATOM   1335 C  CA  . LEU   A 1 177 ? 17.23100  0.50200   23.67900  1.000 7.65682  ? 221 LEU   A CA  1 
ATOM   1336 C  C   . LEU   A 1 177 ? 17.73800  -0.94200  23.80200  1.000 7.30682  ? 221 LEU   A C   1 
ATOM   1337 O  O   . LEU   A 1 177 ? 17.79200  -1.47200  24.91200  1.000 9.14682  ? 221 LEU   A O   1 
ATOM   1338 C  CB  . LEU   A 1 177 ? 16.13300  0.78400   24.71500  1.000 10.20682 ? 221 LEU   A CB  1 
ATOM   1339 C  CG  . LEU   A 1 177 ? 15.61200  2.23100   24.70400  1.000 10.66682 ? 221 LEU   A CG  1 
ATOM   1340 C  CD1 . LEU   A 1 177 ? 14.43800  2.45700   25.64700  1.000 11.59682 ? 221 LEU   A CD1 1 
ATOM   1341 C  CD2 . LEU   A 1 177 ? 16.73000  3.19800   25.03200  1.000 7.36682  ? 221 LEU   A CD2 1 
ATOM   1342 N  N   . ASP   A 1 178 ? 18.12000  -1.57700  22.69400  1.000 6.09682  ? 222 ASP   A N   1 
ATOM   1343 C  CA  . ASP   A 1 178 ? 18.70600  -2.91900  22.72300  1.000 7.77682  ? 222 ASP   A CA  1 
ATOM   1344 C  C   . ASP   A 1 178 ? 19.98800  -2.92900  23.56200  1.000 8.24682  ? 222 ASP   A C   1 
ATOM   1345 O  O   . ASP   A 1 178 ? 20.90100  -2.13600  23.31500  1.000 10.70682 ? 222 ASP   A O   1 
ATOM   1346 C  CB  . ASP   A 1 178 ? 18.99900  -3.37300  21.29300  1.000 9.07682  ? 222 ASP   A CB  1 
ATOM   1347 C  CG  . ASP   A 1 178 ? 19.21500  -4.87500  21.16800  1.000 8.65682  ? 222 ASP   A CG  1 
ATOM   1348 O  OD1 . ASP   A 1 178 ? 19.76900  -5.50700  22.09200  1.000 8.37682  ? 222 ASP   A OD1 1 
ATOM   1349 O  OD2 . ASP   A 1 178 ? 18.84000  -5.41600  20.11200  1.000 6.69682  ? 222 ASP   A OD2 1 
ATOM   1350 N  N   . THR   A 1 179 ? 20.04400  -3.80200  24.57700  1.000 9.04682  ? 223 THR   A N   1 
ATOM   1351 C  CA  . THR   A 1 179 ? 21.25700  -3.98200  25.37700  1.000 10.38682 ? 223 THR   A CA  1 
ATOM   1352 C  C   . THR   A 1 179 ? 22.01200  -5.25700  25.03000  1.000 8.64682  ? 223 THR   A C   1 
ATOM   1353 O  O   . THR   A 1 179 ? 23.14300  -5.43800  25.50200  1.000 8.54682  ? 223 THR   A O   1 
ATOM   1354 C  CB  . THR   A 1 179 ? 20.95700  -4.01400  26.89400  1.000 12.01682 ? 223 THR   A CB  1 
ATOM   1355 O  OG1 . THR   A 1 179 ? 20.24500  -5.21500  27.22400  1.000 17.25682 ? 223 THR   A OG1 1 
ATOM   1356 C  CG2 . THR   A 1 179 ? 20.14300  -2.80900  27.33800  1.000 12.29682 ? 223 THR   A CG2 1 
ATOM   1357 N  N   . ILE   A 1 180 ? 21.42100  -6.14400  24.23400  1.000 12.18682 ? 224 ILE   A N   1 
ATOM   1358 C  CA  . ILE   A 1 180 ? 22.07900  -7.40100  23.88700  1.000 11.64682 ? 224 ILE   A CA  1 
ATOM   1359 C  C   . ILE   A 1 180 ? 22.85800  -7.28300  22.58400  1.000 10.26682 ? 224 ILE   A C   1 
ATOM   1360 O  O   . ILE   A 1 180 ? 23.97400  -7.79900  22.46600  1.000 11.45682 ? 224 ILE   A O   1 
ATOM   1361 C  CB  . ILE   A 1 180 ? 21.03500  -8.53100  23.83200  1.000 13.44682 ? 224 ILE   A CB  1 
ATOM   1362 C  CG1 . ILE   A 1 180 ? 20.55700  -8.85400  25.24700  1.000 12.28682 ? 224 ILE   A CG1 1 
ATOM   1363 C  CG2 . ILE   A 1 180 ? 21.60900  -9.77600  23.18200  1.000 9.00682  ? 224 ILE   A CG2 1 
ATOM   1364 C  CD1 . ILE   A 1 180 ? 19.18600  -9.50500  25.25600  1.000 15.91682 ? 224 ILE   A CD1 1 
ATOM   1365 N  N   . ALA   A 1 181 ? 22.28100  -6.62100  21.58900  1.000 13.12682 ? 225 ALA   A N   1 
ATOM   1366 C  CA  . ALA   A 1 181 ? 22.98500  -6.24400  20.36600  1.000 9.30682  ? 225 ALA   A CA  1 
ATOM   1367 C  C   . ALA   A 1 181 ? 22.75300  -4.75500  20.13700  1.000 7.06682  ? 225 ALA   A C   1 
ATOM   1368 O  O   . ALA   A 1 181 ? 21.95400  -4.36100  19.27600  1.000 7.87682  ? 225 ALA   A O   1 
ATOM   1369 C  CB  . ALA   A 1 181 ? 22.51300  -7.08800  19.18000  1.000 7.12682  ? 225 ALA   A CB  1 
ATOM   1370 N  N   . PRO   A 1 182 ? 23.42300  -3.89700  20.91500  1.000 8.85682  ? 226 PRO   A N   1 
ATOM   1371 C  CA  . PRO   A 1 182 ? 23.14600  -2.45400  20.84000  1.000 6.90682  ? 226 PRO   A CA  1 
ATOM   1372 C  C   . PRO   A 1 182 ? 23.37200  -1.91400  19.43400  1.000 8.54682  ? 226 PRO   A C   1 
ATOM   1373 O  O   . PRO   A 1 182 ? 24.32900  -2.28600  18.75600  1.000 10.76682 ? 226 PRO   A O   1 
ATOM   1374 C  CB  . PRO   A 1 182 ? 24.14400  -1.84600  21.83800  1.000 7.49682  ? 226 PRO   A CB  1 
ATOM   1375 C  CG  . PRO   A 1 182 ? 24.49500  -2.96100  22.76100  1.000 11.00682 ? 226 PRO   A CG  1 
ATOM   1376 C  CD  . PRO   A 1 182 ? 24.43100  -4.21800  21.94300  1.000 9.63682  ? 226 PRO   A CD  1 
ATOM   1377 N  N   . VAL   A 1 183 ? 22.47600  -1.02200  19.00100  1.000 7.55682  ? 227 VAL   A N   1 
ATOM   1378 C  CA  . VAL   A 1 183 ? 22.56300  -0.48100  17.64500  1.000 10.08682 ? 227 VAL   A CA  1 
ATOM   1379 C  C   . VAL   A 1 183 ? 23.87400  0.27600   17.43500  1.000 9.17682  ? 227 VAL   A C   1 
ATOM   1380 O  O   . VAL   A 1 183 ? 24.37200  0.36100   16.30900  1.000 6.25682  ? 227 VAL   A O   1 
ATOM   1381 C  CB  . VAL   A 1 183 ? 21.34900  0.41800   17.32600  1.000 9.07682  ? 227 VAL   A CB  1 
ATOM   1382 C  CG1 . VAL   A 1 183 ? 20.05900  -0.39700  17.23800  1.000 7.64682  ? 227 VAL   A CG1 1 
ATOM   1383 C  CG2 . VAL   A 1 183 ? 21.21900  1.52900   18.34500  1.000 9.58682  ? 227 VAL   A CG2 1 
ATOM   1384 N  N   . SER   A 1 184 ? 24.45300  0.83500   18.49600  1.000 9.56682  ? 228 SER   A N   1 
ATOM   1385 C  CA  . SER   A 1 184 ? 25.68400  1.59700   18.30700  1.000 10.30682 ? 228 SER   A CA  1 
ATOM   1386 C  C   . SER   A 1 184 ? 26.87300  0.69500   18.00700  1.000 9.66682  ? 228 SER   A C   1 
ATOM   1387 O  O   . SER   A 1 184 ? 27.85600  1.15500   17.41400  1.000 10.88682 ? 228 SER   A O   1 
ATOM   1388 C  CB  . SER   A 1 184 ? 25.97000  2.45500   19.53500  1.000 8.54682  ? 228 SER   A CB  1 
ATOM   1389 O  OG  . SER   A 1 184 ? 26.40100  1.64400   20.61300  1.000 14.90682 ? 228 SER   A OG  1 
ATOM   1390 N  N   . THR   A 1 185 ? 26.79900  -0.58300  18.36700  1.000 7.79682  ? 229 THR   A N   1 
ATOM   1391 C  CA  . THR   A 1 185 ? 27.91800  -1.48400  18.16700  1.000 7.20682  ? 229 THR   A CA  1 
ATOM   1392 C  C   . THR   A 1 185 ? 27.61400  -2.64900  17.23400  1.000 9.26682  ? 229 THR   A C   1 
ATOM   1393 O  O   . THR   A 1 185 ? 28.55500  -3.33500  16.81800  1.000 8.01682  ? 229 THR   A O   1 
ATOM   1394 C  CB  . THR   A 1 185 ? 28.41100  -2.02500  19.52000  1.000 7.87682  ? 229 THR   A CB  1 
ATOM   1395 O  OG1 . THR   A 1 185 ? 27.31600  -2.62300  20.22600  1.000 7.33682  ? 229 THR   A OG1 1 
ATOM   1396 C  CG2 . THR   A 1 185 ? 29.00500  -0.89100  20.36400  1.000 9.23682  ? 229 THR   A CG2 1 
ATOM   1397 N  N   . HIS   A 1 186 ? 26.34400  -2.89400  16.88500  1.000 8.75682  ? 230 HIS   A N   1 
ATOM   1398 C  CA  . HIS   A 1 186 ? 26.03400  -3.91000  15.87900  1.000 7.42682  ? 230 HIS   A CA  1 
ATOM   1399 C  C   . HIS   A 1 186 ? 25.30900  -3.30900  14.66200  1.000 8.93682  ? 230 HIS   A C   1 
ATOM   1400 O  O   . HIS   A 1 186 ? 25.94700  -3.04900  13.63800  1.000 5.92682  ? 230 HIS   A O   1 
ATOM   1401 C  CB  . HIS   A 1 186 ? 25.23600  -5.06300  16.51700  1.000 4.91682  ? 230 HIS   A CB  1 
ATOM   1402 C  CG  . HIS   A 1 186 ? 25.98600  -5.77600  17.60600  1.000 7.20682  ? 230 HIS   A CG  1 
ATOM   1403 N  ND1 . HIS   A 1 186 ? 26.52800  -7.03500  17.44400  1.000 7.29682  ? 230 HIS   A ND1 1 
ATOM   1404 C  CD2 . HIS   A 1 186 ? 26.32000  -5.38400  18.86400  1.000 10.92682 ? 230 HIS   A CD2 1 
ATOM   1405 C  CE1 . HIS   A 1 186 ? 27.15700  -7.39100  18.55500  1.000 8.61682  ? 230 HIS   A CE1 1 
ATOM   1406 N  NE2 . HIS   A 1 186 ? 27.04600  -6.40600  19.43300  1.000 9.04682  ? 230 HIS   A NE2 1 
ATOM   1407 N  N   . ALA   A 1 187 ? 23.99500  -3.06700  14.76300  1.000 5.93682  ? 231 ALA   A N   1 
ATOM   1408 C  CA  . ALA   A 1 187 ? 23.19200  -2.69600  13.59100  1.000 6.97682  ? 231 ALA   A CA  1 
ATOM   1409 C  C   . ALA   A 1 187 ? 23.77800  -1.52200  12.80000  1.000 6.77682  ? 231 ALA   A C   1 
ATOM   1410 O  O   . ALA   A 1 187 ? 23.85500  -1.56900  11.56700  1.000 7.19682  ? 231 ALA   A O   1 
ATOM   1411 C  CB  . ALA   A 1 187 ? 21.76200  -2.36400  14.02400  1.000 7.74682  ? 231 ALA   A CB  1 
ATOM   1412 N  N   . LYS   A 1 188 ? 24.16400  -0.44000  13.48400  1.000 8.46682  ? 232 LYS   A N   1 
ATOM   1413 C  CA  . LYS   A 1 188 ? 24.59300  0.74900   12.74500  1.000 9.87682  ? 232 LYS   A CA  1 
ATOM   1414 C  C   . LYS   A 1 188 ? 25.94100  0.55700   12.06000  1.000 8.64682  ? 232 LYS   A C   1 
ATOM   1415 O  O   . LYS   A 1 188 ? 26.05700  0.92000   10.87500  1.000 7.30682  ? 232 LYS   A O   1 
ATOM   1416 C  CB  . LYS   A 1 188 ? 24.60300  1.97600   13.65600  1.000 9.40682  ? 232 LYS   A CB  1 
ATOM   1417 C  CG  . LYS   A 1 188 ? 23.23500  2.56600   13.96700  1.000 10.58682 ? 232 LYS   A CG  1 
ATOM   1418 C  CD  . LYS   A 1 188 ? 23.37400  3.55800   15.10500  1.000 12.61682 ? 232 LYS   A CD  1 
ATOM   1419 C  CE  . LYS   A 1 188 ? 22.10900  4.35100   15.32000  1.000 19.99682 ? 232 LYS   A CE  1 
ATOM   1420 N  NZ  . LYS   A 1 188 ? 22.30000  5.33200   16.44100  1.000 25.44682 ? 232 LYS   A NZ  1 
ATOM   1421 N  N   . PRO   A 1 189 ? 26.99500  0.05400   12.72900  1.000 6.79682  ? 233 PRO   A N   1 
ATOM   1422 C  CA  . PRO   A 1 189 ? 28.24000  -0.24300  12.00000  1.000 7.12682  ? 233 PRO   A CA  1 
ATOM   1423 C  C   . PRO   A 1 189 ? 28.03700  -1.20900  10.85700  1.000 8.90682  ? 233 PRO   A C   1 
ATOM   1424 O  O   . PRO   A 1 189 ? 28.64000  -1.02800  9.79400   1.000 10.10682 ? 233 PRO   A O   1 
ATOM   1425 C  CB  . PRO   A 1 189 ? 29.15800  -0.84000  13.08100  1.000 8.76682  ? 233 PRO   A CB  1 
ATOM   1426 C  CG  . PRO   A 1 189 ? 28.62500  -0.35400  14.37300  1.000 7.41682  ? 233 PRO   A CG  1 
ATOM   1427 C  CD  . PRO   A 1 189 ? 27.14500  -0.14900  14.18700  1.000 6.19682  ? 233 PRO   A CD  1 
ATOM   1428 N  N   . PHE   A 1 190 ? 27.19300  -2.23200  11.04000  1.000 9.51682  ? 234 PHE   A N   1 
ATOM   1429 C  CA  . PHE   A 1 190 ? 26.84800  -3.10100  9.91900   1.000 7.75682  ? 234 PHE   A CA  1 
ATOM   1430 C  C   . PHE   A 1 190 ? 26.32000  -2.27600  8.74400   1.000 9.58682  ? 234 PHE   A C   1 
ATOM   1431 O  O   . PHE   A 1 190 ? 26.82500  -2.38100  7.61900   1.000 9.85682  ? 234 PHE   A O   1 
ATOM   1432 C  CB  . PHE   A 1 190 ? 25.79600  -4.14700  10.32000  1.000 5.77682  ? 234 PHE   A CB  1 
ATOM   1433 C  CG  . PHE   A 1 190 ? 26.19700  -5.07000  11.45300  1.000 6.10682  ? 234 PHE   A CG  1 
ATOM   1434 C  CD1 . PHE   A 1 190 ? 27.52200  -5.24100  11.82500  1.000 6.98682  ? 234 PHE   A CD1 1 
ATOM   1435 C  CD2 . PHE   A 1 190 ? 25.21100  -5.77200  12.14400  1.000 6.46682  ? 234 PHE   A CD2 1 
ATOM   1436 C  CE1 . PHE   A 1 190 ? 27.86700  -6.08800  12.86400  1.000 7.07682  ? 234 PHE   A CE1 1 
ATOM   1437 C  CE2 . PHE   A 1 190 ? 25.53800  -6.62000  13.19800  1.000 6.44682  ? 234 PHE   A CE2 1 
ATOM   1438 C  CZ  . PHE   A 1 190 ? 26.86800  -6.78400  13.55500  1.000 8.07682  ? 234 PHE   A CZ  1 
ATOM   1439 N  N   . TYR   A 1 191 ? 25.30700  -1.43800  8.99400   1.000 7.92682  ? 235 TYR   A N   1 
ATOM   1440 C  CA  . TYR   A 1 191 ? 24.67200  -0.70300  7.89700   1.000 7.50682  ? 235 TYR   A CA  1 
ATOM   1441 C  C   . TYR   A 1 191 ? 25.66700  0.23700   7.21500   1.000 8.27682  ? 235 TYR   A C   1 
ATOM   1442 O  O   . TYR   A 1 191 ? 25.72300  0.32200   5.97900   1.000 8.48682  ? 235 TYR   A O   1 
ATOM   1443 C  CB  . TYR   A 1 191 ? 23.45300  0.08800   8.39400   1.000 6.96682  ? 235 TYR   A CB  1 
ATOM   1444 C  CG  . TYR   A 1 191 ? 22.94600  1.06400   7.32900   1.000 6.93682  ? 235 TYR   A CG  1 
ATOM   1445 C  CD1 . TYR   A 1 191 ? 22.02400  0.66000   6.36900   1.000 7.41682  ? 235 TYR   A CD1 1 
ATOM   1446 C  CD2 . TYR   A 1 191 ? 23.43700  2.36600   7.25800   1.000 9.63682  ? 235 TYR   A CD2 1 
ATOM   1447 C  CE1 . TYR   A 1 191 ? 21.59100  1.52600   5.36900   1.000 7.26682  ? 235 TYR   A CE1 1 
ATOM   1448 C  CE2 . TYR   A 1 191 ? 23.01400  3.24500   6.26100   1.000 10.01682 ? 235 TYR   A CE2 1 
ATOM   1449 C  CZ  . TYR   A 1 191 ? 22.08800  2.81900   5.31900   1.000 9.02682  ? 235 TYR   A CZ  1 
ATOM   1450 O  OH  . TYR   A 1 191 ? 21.67000  3.69300   4.33300   1.000 8.10682  ? 235 TYR   A OH  1 
ATOM   1451 N  N   . GLU   A 1 192 ? 26.43300  0.97900   8.01100   1.000 7.72682  ? 236 GLU   A N   1 
ATOM   1452 C  CA  . GLU   A 1 192 ? 27.41000  1.92300   7.47200   1.000 9.00682  ? 236 GLU   A CA  1 
ATOM   1453 C  C   . GLU   A 1 192 ? 28.52200  1.23400   6.69500   1.000 13.02682 ? 236 GLU   A C   1 
ATOM   1454 O  O   . GLU   A 1 192 ? 29.13600  1.86400   5.82000   1.000 10.74682 ? 236 GLU   A O   1 
ATOM   1455 C  CB  . GLU   A 1 192 ? 28.01000  2.76200   8.60700   1.000 9.25682  ? 236 GLU   A CB  1 
ATOM   1456 C  CG  . GLU   A 1 192 ? 27.01600  3.76500   9.21400   1.000 9.28682  ? 236 GLU   A CG  1 
ATOM   1457 C  CD  . GLU   A 1 192 ? 26.56200  4.81600   8.19800   1.000 13.69682 ? 236 GLU   A CD  1 
ATOM   1458 O  OE1 . GLU   A 1 192 ? 27.42500  5.31300   7.43600   1.000 13.50682 ? 236 GLU   A OE1 1 
ATOM   1459 O  OE2 . GLU   A 1 192 ? 25.34800  5.13300   8.14900   1.000 12.13682 ? 236 GLU   A OE2 1 
ATOM   1460 N  N   . SER   A 1 193 ? 28.80300  -0.03500  6.98100   1.000 8.21682  ? 237 SER   A N   1 
ATOM   1461 C  CA  . SER   A 1 193 ? 29.87600  -0.70300  6.25700   1.000 9.11682  ? 237 SER   A CA  1 
ATOM   1462 C  C   . SER   A 1 193 ? 29.40600  -1.32300  4.95500   1.000 10.65682 ? 237 SER   A C   1 
ATOM   1463 O  O   . SER   A 1 193 ? 30.24900  -1.65200  4.11700   1.000 7.76682  ? 237 SER   A O   1 
ATOM   1464 C  CB  . SER   A 1 193 ? 30.53000  -1.78100  7.12000   1.000 9.91682  ? 237 SER   A CB  1 
ATOM   1465 O  OG  . SER   A 1 193 ? 29.65000  -2.87200  7.33400   1.000 9.82682  ? 237 SER   A OG  1 
ATOM   1466 N  N   . LEU   A 1 194 ? 28.09200  -1.50200  4.77700   1.000 9.88682  ? 238 LEU   A N   1 
ATOM   1467 C  CA  . LEU   A 1 194 ? 27.56400  -1.99600  3.51400   1.000 7.92682  ? 238 LEU   A CA  1 
ATOM   1468 C  C   . LEU   A 1 194 ? 27.95300  -1.04700  2.38600   1.000 9.84682  ? 238 LEU   A C   1 
ATOM   1469 O  O   . LEU   A 1 194 ? 28.05700  0.16600   2.59900   1.000 9.68682  ? 238 LEU   A O   1 
ATOM   1470 C  CB  . LEU   A 1 194 ? 26.04100  -2.13200  3.57300   1.000 8.95682  ? 238 LEU   A CB  1 
ATOM   1471 C  CG  . LEU   A 1 194 ? 25.40000  -3.18100  4.49700   1.000 8.11682  ? 238 LEU   A CG  1 
ATOM   1472 C  CD1 . LEU   A 1 194 ? 23.88600  -2.92300  4.65600   1.000 8.20682  ? 238 LEU   A CD1 1 
ATOM   1473 C  CD2 . LEU   A 1 194 ? 25.65200  -4.60800  4.01200   1.000 8.15682  ? 238 LEU   A CD2 1 
ATOM   1474 N  N   . PRO   A 1 195 ? 28.14400  -1.56400  1.16900   1.000 11.08682 ? 239 PRO   A N   1 
ATOM   1475 C  CA  . PRO   A 1 195 ? 28.50100  -0.68600  0.04400   1.000 8.04682  ? 239 PRO   A CA  1 
ATOM   1476 C  C   . PRO   A 1 195 ? 27.51500  0.46700   -0.10200  1.000 10.26682 ? 239 PRO   A C   1 
ATOM   1477 O  O   . PRO   A 1 195 ? 26.30700  0.30400   0.06800   1.000 9.04682  ? 239 PRO   A O   1 
ATOM   1478 C  CB  . PRO   A 1 195 ? 28.45600  -1.62300  -1.16700  1.000 8.79682  ? 239 PRO   A CB  1 
ATOM   1479 C  CG  . PRO   A 1 195 ? 28.71900  -3.01000  -0.58600  1.000 12.49682 ? 239 PRO   A CG  1 
ATOM   1480 C  CD  . PRO   A 1 195 ? 28.04100  -2.98100  0.76900   1.000 7.95682  ? 239 PRO   A CD  1 
ATOM   1481 N  N   . SER   A 1 196 ? 28.04000  1.65700   -0.41000  1.000 9.60682  ? 240 SER   A N   1 
ATOM   1482 C  CA  . SER   A 1 196 ? 27.14700  2.79700   -0.59300  1.000 12.11682 ? 240 SER   A CA  1 
ATOM   1483 C  C   . SER   A 1 196 ? 26.36900  2.71100   -1.89600  1.000 14.10682 ? 240 SER   A C   1 
ATOM   1484 O  O   . SER   A 1 196 ? 25.36700  3.42000   -2.05300  1.000 13.25682 ? 240 SER   A O   1 
ATOM   1485 C  CB  . SER   A 1 196 ? 27.93500  4.11300   -0.52300  1.000 13.90682 ? 240 SER   A CB  1 
ATOM   1486 O  OG  . SER   A 1 196 ? 28.93300  4.14400   -1.51700  1.000 25.12682 ? 240 SER   A OG  1 
ATOM   1487 N  N   . SER   A 1 197 ? 26.78900  1.84600   -2.82100  1.000 11.47682 ? 241 SER   A N   1 
ATOM   1488 C  CA  . SER   A 1 197 ? 26.06700  1.61400   -4.06600  1.000 15.08682 ? 241 SER   A CA  1 
ATOM   1489 C  C   . SER   A 1 197 ? 25.01400  0.52400   -3.93900  1.000 14.33682 ? 241 SER   A C   1 
ATOM   1490 O  O   . SER   A 1 197 ? 24.31100  0.23800   -4.91500  1.000 15.80682 ? 241 SER   A O   1 
ATOM   1491 C  CB  . SER   A 1 197 ? 27.04100  1.23600   -5.17700  1.000 14.27682 ? 241 SER   A CB  1 
ATOM   1492 O  OG  . SER   A 1 197 ? 27.75100  0.06100   -4.82300  1.000 22.03682 ? 241 SER   A OG  1 
ATOM   1493 N  N   . LEU   A 1 198 ? 24.90300  -0.09000  -2.78400  1.000 11.03682 ? 242 LEU   A N   1 
ATOM   1494 C  CA  . LEU   A 1 198 ? 23.90200  -1.13100  -2.56700  1.000 11.38682 ? 242 LEU   A CA  1 
ATOM   1495 C  C   . LEU   A 1 198 ? 22.55600  -0.50700  -2.18900  1.000 9.61682  ? 242 LEU   A C   1 
ATOM   1496 O  O   . LEU   A 1 198 ? 22.50800  0.42900   -1.39000  1.000 8.00682  ? 242 LEU   A O   1 
ATOM   1497 C  CB  . LEU   A 1 198 ? 24.35700  -2.06600  -1.45100  1.000 11.29682 ? 242 LEU   A CB  1 
ATOM   1498 C  CG  . LEU   A 1 198 ? 23.48200  -3.27600  -1.14000  1.000 8.37682  ? 242 LEU   A CG  1 
ATOM   1499 C  CD1 . LEU   A 1 198 ? 23.67100  -4.34700  -2.22200  1.000 10.35682 ? 242 LEU   A CD1 1 
ATOM   1500 C  CD2 . LEU   A 1 198 ? 23.82900  -3.80200  0.23900   1.000 10.34682 ? 242 LEU   A CD2 1 
ATOM   1501 N  N   . PRO   A 1 199 ? 21.45000  -1.01100  -2.73400  1.000 12.09682 ? 243 PRO   A N   1 
ATOM   1502 C  CA  . PRO   A 1 199 ? 20.13500  -0.65900  -2.17500  1.000 8.95682  ? 243 PRO   A CA  1 
ATOM   1503 C  C   . PRO   A 1 199 ? 20.03800  -1.20100  -0.75600  1.000 8.86682  ? 243 PRO   A C   1 
ATOM   1504 O  O   . PRO   A 1 199 ? 20.10200  -2.41200  -0.52900  1.000 9.31682  ? 243 PRO   A O   1 
ATOM   1505 C  CB  . PRO   A 1 199 ? 19.14200  -1.34800  -3.12800  1.000 10.90682 ? 243 PRO   A CB  1 
ATOM   1506 C  CG  . PRO   A 1 199 ? 19.94800  -1.67400  -4.39100  1.000 13.47682 ? 243 PRO   A CG  1 
ATOM   1507 C  CD  . PRO   A 1 199 ? 21.34500  -1.94300  -3.87400  1.000 10.66682 ? 243 PRO   A CD  1 
ATOM   1508 N  N   . LYS   A 1 200 ? 19.92200  -0.29700  0.21500   1.000 5.77682  ? 244 LYS   A N   1 
ATOM   1509 C  CA  . LYS   A 1 200 ? 19.96100  -0.71000  1.61000   1.000 6.54682  ? 244 LYS   A CA  1 
ATOM   1510 C  C   . LYS   A 1 200 ? 19.15600  0.27000   2.44400   1.000 10.02682 ? 244 LYS   A C   1 
ATOM   1511 O  O   . LYS   A 1 200 ? 18.87400  1.39000   2.01200   1.000 7.25682  ? 244 LYS   A O   1 
ATOM   1512 C  CB  . LYS   A 1 200 ? 21.40500  -0.79100  2.13800   1.000 6.45682  ? 244 LYS   A CB  1 
ATOM   1513 C  CG  . LYS   A 1 200 ? 22.17900  0.52300   2.01500   1.000 6.72682  ? 244 LYS   A CG  1 
ATOM   1514 C  CD  . LYS   A 1 200 ? 23.54300  0.44200   2.71500   1.000 8.02682  ? 244 LYS   A CD  1 
ATOM   1515 C  CE  . LYS   A 1 200 ? 24.32200  1.76300   2.60500   1.000 6.64682  ? 244 LYS   A CE  1 
ATOM   1516 N  NZ  . LYS   A 1 200 ? 25.65100  1.71100   3.31000   1.000 7.03682  ? 244 LYS   A NZ  1 
ATOM   1517 N  N   . ALA   A 1 201 ? 18.78700  -0.16900  3.64600   1.000 5.48682  ? 245 ALA   A N   1 
ATOM   1518 C  CA  . ALA   A 1 201 ? 18.06700  0.69300   4.57400   1.000 6.49682  ? 245 ALA   A CA  1 
ATOM   1519 C  C   . ALA   A 1 201 ? 18.37000  0.27000   6.00100   1.000 6.95682  ? 245 ALA   A C   1 
ATOM   1520 O  O   . ALA   A 1 201 ? 18.78000  -0.86800  6.26700   1.000 7.48682  ? 245 ALA   A O   1 
ATOM   1521 C  CB  . ALA   A 1 201 ? 16.55500  0.67200   4.33600   1.000 6.04682  ? 245 ALA   A CB  1 
ATOM   1522 N  N   . TYR   A 1 202 ? 18.15400  1.21900   6.91700   1.000 9.50682  ? 246 TYR   A N   1 
ATOM   1523 C  CA  . TYR   A 1 202 ? 18.27400  1.00600   8.35400   1.000 6.62682  ? 246 TYR   A CA  1 
ATOM   1524 C  C   . TYR   A 1 202 ? 17.10200  1.70000   9.03200   1.000 9.44682  ? 246 TYR   A C   1 
ATOM   1525 O  O   . TYR   A 1 202 ? 16.92000  2.90700   8.85100   1.000 7.38682  ? 246 TYR   A O   1 
ATOM   1526 C  CB  . TYR   A 1 202 ? 19.59500  1.56700   8.89300   1.000 7.23682  ? 246 TYR   A CB  1 
ATOM   1527 C  CG  . TYR   A 1 202 ? 19.63200  1.63000   10.41000  1.000 9.92682  ? 246 TYR   A CG  1 
ATOM   1528 C  CD1 . TYR   A 1 202 ? 19.69300  0.46300   11.16500  1.000 10.91682 ? 246 TYR   A CD1 1 
ATOM   1529 C  CD2 . TYR   A 1 202 ? 19.59500  2.84700   11.09000  1.000 9.74682  ? 246 TYR   A CD2 1 
ATOM   1530 C  CE1 . TYR   A 1 202 ? 19.71100  0.49900   12.54800  1.000 9.09682  ? 246 TYR   A CE1 1 
ATOM   1531 C  CE2 . TYR   A 1 202 ? 19.62800  2.89200   12.49500  1.000 10.07682 ? 246 TYR   A CE2 1 
ATOM   1532 C  CZ  . TYR   A 1 202 ? 19.68600  1.71200   13.20800  1.000 12.00682 ? 246 TYR   A CZ  1 
ATOM   1533 O  OH  . TYR   A 1 202 ? 19.70800  1.71700   14.59100  1.000 16.89682 ? 246 TYR   A OH  1 
ATOM   1534 N  N   . MET   A 1 203 ? 16.32800  0.95000   9.82100   1.000 5.79682  ? 247 MET   A N   1 
ATOM   1535 C  CA  . MET   A 1 203 ? 15.19000  1.47800   10.56700  1.000 7.31682  ? 247 MET   A CA  1 
ATOM   1536 C  C   . MET   A 1 203 ? 15.37600  1.19600   12.05400  1.000 9.33682  ? 247 MET   A C   1 
ATOM   1537 O  O   . MET   A 1 203 ? 15.54100  0.04100   12.45300  1.000 7.57682  ? 247 MET   A O   1 
ATOM   1538 C  CB  . MET   A 1 203 ? 13.87700  0.85800   10.07100  1.000 7.35682  ? 247 MET   A CB  1 
ATOM   1539 C  CG  . MET   A 1 203 ? 12.62900  1.33700   10.82200  1.000 7.59682  ? 247 MET   A CG  1 
ATOM   1540 S  SD  . MET   A 1 203 ? 11.08900  0.73600   10.08400  1.000 9.87682  ? 247 MET   A SD  1 
ATOM   1541 C  CE  . MET   A 1 203 ? 11.02600  -0.94200  10.72600  1.000 9.24682  ? 247 MET   A CE  1 
ATOM   1542 N  N   . GLU   A 1 204 ? 15.33500  2.24400   12.87300  1.000 5.99682  ? 248 GLU   A N   1 
ATOM   1543 C  CA  . GLU   A 1 204 ? 15.49900  2.12100   14.31700  1.000 6.41682  ? 248 GLU   A CA  1 
ATOM   1544 C  C   . GLU   A 1 204 ? 14.16100  2.39200   14.99800  1.000 8.12682  ? 248 GLU   A C   1 
ATOM   1545 O  O   . GLU   A 1 204 ? 13.53500  3.43200   14.76300  1.000 7.57682  ? 248 GLU   A O   1 
ATOM   1546 C  CB  . GLU   A 1 204 ? 16.57600  3.08300   14.83800  1.000 8.51682  ? 248 GLU   A CB  1 
ATOM   1547 C  CG  . GLU   A 1 204 ? 16.90600  2.92800   16.32900  1.000 9.88682  ? 248 GLU   A CG  1 
ATOM   1548 C  CD  . GLU   A 1 204 ? 18.09700  3.77500   16.76800  1.000 15.62682 ? 248 GLU   A CD  1 
ATOM   1549 O  OE1 . GLU   A 1 204 ? 19.07400  3.88500   15.99500  1.000 13.73682 ? 248 GLU   A OE1 1 
ATOM   1550 O  OE2 . GLU   A 1 204 ? 18.06200  4.32500   17.89400  1.000 14.24682 ? 248 GLU   A OE2 1 
ATOM   1551 N  N   . LEU   A 1 205 ? 13.73400  1.46200   15.84300  1.000 8.60682  ? 249 LEU   A N   1 
ATOM   1552 C  CA  . LEU   A 1 205 ? 12.43000  1.52600   16.49000  1.000 8.38682  ? 249 LEU   A CA  1 
ATOM   1553 C  C   . LEU   A 1 205 ? 12.55900  2.21200   17.85000  1.000 8.47682  ? 249 LEU   A C   1 
ATOM   1554 O  O   . LEU   A 1 205 ? 13.31800  1.75200   18.71100  1.000 7.55682  ? 249 LEU   A O   1 
ATOM   1555 C  CB  . LEU   A 1 205 ? 11.85900  0.11900   16.65200  1.000 8.95682  ? 249 LEU   A CB  1 
ATOM   1556 C  CG  . LEU   A 1 205 ? 11.59800  -0.69200  15.37500  1.000 8.54682  ? 249 LEU   A CG  1 
ATOM   1557 C  CD1 . LEU   A 1 205 ? 11.29100  -2.13800  15.72400  1.000 7.22682  ? 249 LEU   A CD1 1 
ATOM   1558 C  CD2 . LEU   A 1 205 ? 10.45800  -0.08300  14.57400  1.000 10.38682 ? 249 LEU   A CD2 1 
ATOM   1559 N  N   . CYS   A 1 206 ? 11.80600  3.29800   18.03700  1.000 9.66682  ? 250 CYS   A N   1 
ATOM   1560 C  CA  . CYS   A 1 206 ? 11.80000  4.05600   19.28800  1.000 11.48682 ? 250 CYS   A CA  1 
ATOM   1561 C  C   . CYS   A 1 206 ? 11.51800  3.16000   20.48800  1.000 11.23682 ? 250 CYS   A C   1 
ATOM   1562 O  O   . CYS   A 1 206 ? 10.53900  2.40900   20.49800  1.000 9.27682  ? 250 CYS   A O   1 
ATOM   1563 C  CB  . CYS   A 1 206 ? 10.72900  5.15400   19.24000  1.000 11.97682 ? 250 CYS   A CB  1 
ATOM   1564 S  SG  . CYS   A 1 206 ? 10.87300  6.44400   17.96400  1.000 15.04682 ? 250 CYS   A SG  1 
ATOM   1565 N  N   . GLY   A 1 207 ? 12.34600  3.29200   21.52800  1.000 8.80682  ? 251 GLY   A N   1 
ATOM   1566 C  CA  . GLY   A 1 207 ? 12.10600  2.62700   22.79300  1.000 11.15682 ? 251 GLY   A CA  1 
ATOM   1567 C  C   . GLY   A 1 207 ? 12.13100  1.11100   22.77200  1.000 11.11682 ? 251 GLY   A C   1 
ATOM   1568 O  O   . GLY   A 1 207 ? 11.85600  0.50000   23.81000  1.000 12.82682 ? 251 GLY   A O   1 
ATOM   1569 N  N   . ALA   A 1 208 ? 12.46400  0.48400   21.64400  1.000 8.26682  ? 252 ALA   A N   1 
ATOM   1570 C  CA  . ALA   A 1 208 ? 12.35600  -0.96100  21.51100  1.000 6.95682  ? 252 ALA   A CA  1 
ATOM   1571 C  C   . ALA   A 1 208 ? 13.54600  -1.69700  22.14000  1.000 8.54682  ? 252 ALA   A C   1 
ATOM   1572 O  O   . ALA   A 1 208 ? 14.65300  -1.17100  22.28500  1.000 6.48682  ? 252 ALA   A O   1 
ATOM   1573 C  CB  . ALA   A 1 208 ? 12.23200  -1.36700  20.03700  1.000 6.71682  ? 252 ALA   A CB  1 
ATOM   1574 N  N   . THR   A 1 209 ? 13.29900  -2.95700  22.47500  1.000 6.17682  ? 253 THR   A N   1 
ATOM   1575 C  CA  . THR   A 1 209 ? 14.28000  -3.84800  23.06200  1.000 8.54682  ? 253 THR   A CA  1 
ATOM   1576 C  C   . THR   A 1 209 ? 14.67300  -4.92800  22.05900  1.000 7.86682  ? 253 THR   A C   1 
ATOM   1577 O  O   . THR   A 1 209 ? 14.14000  -5.01800  20.94600  1.000 8.31682  ? 253 THR   A O   1 
ATOM   1578 C  CB  . THR   A 1 209 ? 13.72600  -4.49300  24.33600  1.000 9.02682  ? 253 THR   A CB  1 
ATOM   1579 O  OG1 . THR   A 1 209 ? 12.67800  -5.40000  23.97600  1.000 11.07682 ? 253 THR   A OG1 1 
ATOM   1580 C  CG2 . THR   A 1 209 ? 13.15900  -3.43200  25.27100  1.000 10.66682 ? 253 THR   A CG2 1 
ATOM   1581 N  N   . HIS   A 1 210 ? 15.60300  -5.77900  22.50000  1.000 7.36682  ? 254 HIS   A N   1 
ATOM   1582 C  CA  . HIS   A 1 210 ? 16.14000  -6.84300  21.65800  1.000 11.08682 ? 254 HIS   A CA  1 
ATOM   1583 C  C   . HIS   A 1 210 ? 15.07300  -7.84200  21.21900  1.000 7.73682  ? 254 HIS   A C   1 
ATOM   1584 O  O   . HIS   A 1 210 ? 15.22500  -8.48700  20.17700  1.000 9.12682  ? 254 HIS   A O   1 
ATOM   1585 C  CB  . HIS   A 1 210 ? 17.25500  -7.56200  22.42000  1.000 7.65682  ? 254 HIS   A CB  1 
ATOM   1586 C  CG  . HIS   A 1 210 ? 18.09800  -8.45800  21.56300  1.000 9.01682  ? 254 HIS   A CG  1 
ATOM   1587 N  ND1 . HIS   A 1 210 ? 18.82300  -8.00100  20.48300  1.000 6.86682  ? 254 HIS   A ND1 1 
ATOM   1588 C  CD2 . HIS   A 1 210 ? 18.33500  -9.78900  21.64200  1.000 11.24682 ? 254 HIS   A CD2 1 
ATOM   1589 C  CE1 . HIS   A 1 210 ? 19.46800  -9.01600  19.93000  1.000 7.88682  ? 254 HIS   A CE1 1 
ATOM   1590 N  NE2 . HIS   A 1 210 ? 19.19300  -10.11000 20.61900  1.000 10.52682 ? 254 HIS   A NE2 1 
ATOM   1591 N  N   . PHE   A 1 211 ? 14.00200  -8.00600  21.99700  1.000 6.82682  ? 255 PHE   A N   1 
ATOM   1592 C  CA  . PHE   A 1 211 ? 12.97500  -8.99300  21.68200  1.000 7.17682  ? 255 PHE   A CA  1 
ATOM   1593 C  C   . PHE   A 1 211 ? 11.73300  -8.38000  21.03200  1.000 7.26682  ? 255 PHE   A C   1 
ATOM   1594 O  O   . PHE   A 1 211 ? 10.72700  -9.08300  20.83900  1.000 6.01682  ? 255 PHE   A O   1 
ATOM   1595 C  CB  . PHE   A 1 211 ? 12.62800  -9.78200  22.94700  1.000 8.89682  ? 255 PHE   A CB  1 
ATOM   1596 C  CG  . PHE   A 1 211 ? 13.82200  -10.48100 23.53800  1.000 7.21682  ? 255 PHE   A CG  1 
ATOM   1597 C  CD1 . PHE   A 1 211 ? 14.34400  -11.61000 22.92700  1.000 14.59682 ? 255 PHE   A CD1 1 
ATOM   1598 C  CD2 . PHE   A 1 211 ? 14.47500  -9.95800  24.65300  1.000 12.17682 ? 255 PHE   A CD2 1 
ATOM   1599 C  CE1 . PHE   A 1 211 ? 15.47100  -12.24100 23.44000  1.000 16.68682 ? 255 PHE   A CE1 1 
ATOM   1600 C  CE2 . PHE   A 1 211 ? 15.59800  -10.58100 25.17200  1.000 12.71682 ? 255 PHE   A CE2 1 
ATOM   1601 C  CZ  . PHE   A 1 211 ? 16.09300  -11.73000 24.56500  1.000 13.48682 ? 255 PHE   A CZ  1 
ATOM   1602 N  N   . ALA   A 1 212 ? 11.78500  -7.09900  20.66600  1.000 6.51682  ? 256 ALA   A N   1 
ATOM   1603 C  CA  . ALA   A 1 212 ? 10.70800  -6.52200  19.86300  1.000 6.07682  ? 256 ALA   A CA  1 
ATOM   1604 C  C   . ALA   A 1 212 ? 10.38300  -7.33300  18.61100  1.000 7.74682  ? 256 ALA   A C   1 
ATOM   1605 O  O   . ALA   A 1 212 ? 9.18800   -7.48200  18.30800  1.000 7.58682  ? 256 ALA   A O   1 
ATOM   1606 C  CB  . ALA   A 1 212 ? 11.03800  -5.06800  19.48700  1.000 5.68682  ? 256 ALA   A CB  1 
ATOM   1607 N  N   . PRO   A 1 213 ? 11.34600  -7.88300  17.85700  1.000 8.14682  ? 257 PRO   A N   1 
ATOM   1608 C  CA  . PRO   A 1 213 ? 10.97200  -8.67100  16.66600  1.000 9.38682  ? 257 PRO   A CA  1 
ATOM   1609 C  C   . PRO   A 1 213 ? 10.21400  -9.96100  16.97000  1.000 7.49682  ? 257 PRO   A C   1 
ATOM   1610 O  O   . PRO   A 1 213 ? 9.69300   -10.57200 16.02500  1.000 7.08682  ? 257 PRO   A O   1 
ATOM   1611 C  CB  . PRO   A 1 213 ? 12.32400  -8.99400  16.01100  1.000 4.69682  ? 257 PRO   A CB  1 
ATOM   1612 C  CG  . PRO   A 1 213 ? 13.26400  -7.96000  16.52000  1.000 5.67682  ? 257 PRO   A CG  1 
ATOM   1613 C  CD  . PRO   A 1 213 ? 12.81400  -7.71700  17.93900  1.000 7.79682  ? 257 PRO   A CD  1 
ATOM   1614 N  N   . ASN   A 1 214 ? 10.14500  -10.40300 18.22400  1.000 5.23682  ? 258 ASN   A N   1 
ATOM   1615 C  CA  . ASN   A 1 214 ? 9.51800   -11.68100 18.54200  1.000 6.60682  ? 258 ASN   A CA  1 
ATOM   1616 C  C   . ASN   A 1 214 ? 8.04400   -11.55600 18.91600  1.000 7.23682  ? 258 ASN   A C   1 
ATOM   1617 O  O   . ASN   A 1 214 ? 7.42600   -12.55900 19.28000  1.000 7.84682  ? 258 ASN   A O   1 
ATOM   1618 C  CB  . ASN   A 1 214 ? 10.27900  -12.40000 19.67900  1.000 7.61682  ? 258 ASN   A CB  1 
ATOM   1619 C  CG  . ASN   A 1 214 ? 11.75100  -12.63100 19.35200  1.000 8.21682  ? 258 ASN   A CG  1 
ATOM   1620 O  OD1 . ASN   A 1 214 ? 12.63200  -12.34800 20.16200  1.000 11.91682 ? 258 ASN   A OD1 1 
ATOM   1621 N  ND2 . ASN   A 1 214 ? 12.01900  -13.13100 18.15700  1.000 8.44682  ? 258 ASN   A ND2 1 
ATOM   1622 N  N   . ILE   A 1 215 ? 7.46400   -10.36300 18.87200  1.000 6.72682  ? 259 ILE   A N   1 
ATOM   1623 C  CA  . ILE   A 1 215 ? 6.01200   -10.26000 19.00600  1.000 5.72682  ? 259 ILE   A CA  1 
ATOM   1624 C  C   . ILE   A 1 215 ? 5.49100   -9.46200  17.81800  1.000 9.30682  ? 259 ILE   A C   1 
ATOM   1625 O  O   . ILE   A 1 215 ? 6.23100   -8.63000  17.26600  1.000 9.43682  ? 259 ILE   A O   1 
ATOM   1626 C  CB  . ILE   A 1 215 ? 5.59100   -9.60200  20.32700  1.000 8.61682  ? 259 ILE   A CB  1 
ATOM   1627 C  CG1 . ILE   A 1 215 ? 6.16700   -8.18000  20.41500  1.000 6.91682  ? 259 ILE   A CG1 1 
ATOM   1628 C  CG2 . ILE   A 1 215 ? 5.98600   -10.48700 21.52000  1.000 9.27682  ? 259 ILE   A CG2 1 
ATOM   1629 C  CD1 . ILE   A 1 215 ? 5.64900   -7.35500  21.58400  1.000 7.94682  ? 259 ILE   A CD1 1 
ATOM   1630 N  N   . PRO   A 1 216 ? 4.24100   -9.67200  17.40500  1.000 7.69682  ? 260 PRO   A N   1 
ATOM   1631 C  CA  . PRO   A 1 216 ? 3.68500   -8.90500  16.28500  1.000 8.69682  ? 260 PRO   A CA  1 
ATOM   1632 C  C   . PRO   A 1 216 ? 3.90900   -7.40800  16.44400  1.000 9.21682  ? 260 PRO   A C   1 
ATOM   1633 O  O   . PRO   A 1 216 ? 3.66600   -6.82400  17.50700  1.000 9.08682  ? 260 PRO   A O   1 
ATOM   1634 C  CB  . PRO   A 1 216 ? 2.19800   -9.27000  16.32500  1.000 10.70682 ? 260 PRO   A CB  1 
ATOM   1635 C  CG  . PRO   A 1 216 ? 2.20000   -10.70100 16.85300  1.000 10.45682 ? 260 PRO   A CG  1 
ATOM   1636 C  CD  . PRO   A 1 216 ? 3.32000   -10.73000 17.87200  1.000 11.86682 ? 260 PRO   A CD  1 
ATOM   1637 N  N   . ASN   A 1 217 ? 4.40600   -6.80100  15.37300  1.000 8.73682  ? 261 ASN   A N   1 
ATOM   1638 C  CA  . ASN   A 1 217 ? 4.83800   -5.41000  15.33700  1.000 6.43682  ? 261 ASN   A CA  1 
ATOM   1639 C  C   . ASN   A 1 217 ? 4.48100   -4.87600  13.95700  1.000 8.33682  ? 261 ASN   A C   1 
ATOM   1640 O  O   . ASN   A 1 217 ? 5.08300   -5.28800  12.96400  1.000 7.57682  ? 261 ASN   A O   1 
ATOM   1641 C  CB  . ASN   A 1 217 ? 6.34200   -5.30300  15.60000  1.000 6.76682  ? 261 ASN   A CB  1 
ATOM   1642 C  CG  . ASN   A 1 217 ? 6.82100   -3.85500  15.73200  1.000 9.96682  ? 261 ASN   A CG  1 
ATOM   1643 O  OD1 . ASN   A 1 217 ? 6.54900   -3.01300  14.86900  1.000 10.03682 ? 261 ASN   A OD1 1 
ATOM   1644 N  ND2 . ASN   A 1 217 ? 7.54400   -3.56500  16.81700  1.000 7.99682  ? 261 ASN   A ND2 1 
ATOM   1645 N  N   . THR   A 1 218 ? 3.51400   -3.95500  13.88500  1.000 7.88682  ? 262 THR   A N   1 
ATOM   1646 C  CA  . THR   A 1 218 ? 3.05500   -3.48100  12.57700  1.000 9.72682  ? 262 THR   A CA  1 
ATOM   1647 C  C   . THR   A 1 218 ? 4.16100   -2.75400  11.82500  1.000 8.20682  ? 262 THR   A C   1 
ATOM   1648 O  O   . THR   A 1 218 ? 4.23000   -2.81900  10.59100  1.000 8.92682  ? 262 THR   A O   1 
ATOM   1649 C  CB  . THR   A 1 218 ? 1.84300   -2.55500  12.74000  1.000 16.63682 ? 262 THR   A CB  1 
ATOM   1650 O  OG1 . THR   A 1 218 ? 0.79600   -3.25500  13.41000  1.000 14.24682 ? 262 THR   A OG1 1 
ATOM   1651 C  CG2 . THR   A 1 218 ? 1.31500   -2.10200  11.38900  1.000 12.12682 ? 262 THR   A CG2 1 
ATOM   1652 N  N   . THR   A 1 219 ? 5.01900   -2.02700  12.54700  1.000 5.77682  ? 263 THR   A N   1 
ATOM   1653 C  CA  . THR   A 1 219 ? 6.06300   -1.25300  11.88700  1.000 7.85682  ? 263 THR   A CA  1 
ATOM   1654 C  C   . THR   A 1 219 ? 7.07100   -2.17300  11.20400  1.000 8.14682  ? 263 THR   A C   1 
ATOM   1655 O  O   . THR   A 1 219 ? 7.45700   -1.94500  10.04600  1.000 6.43682  ? 263 THR   A O   1 
ATOM   1656 C  CB  . THR   A 1 219 ? 6.75600   -0.33700  12.90100  1.000 10.34682 ? 263 THR   A CB  1 
ATOM   1657 O  OG1 . THR   A 1 219 ? 5.76900   0.48100   13.54300  1.000 11.15682 ? 263 THR   A OG1 1 
ATOM   1658 C  CG2 . THR   A 1 219 ? 7.77100   0.56700   12.18600  1.000 8.53682  ? 263 THR   A CG2 1 
ATOM   1659 N  N   . ILE   A 1 220 ? 7.50300   -3.22000  11.90900  1.000 6.26682  ? 264 ILE   A N   1 
ATOM   1660 C  CA  . ILE   A 1 220 ? 8.34500   -4.24600  11.29700  1.000 8.05682  ? 264 ILE   A CA  1 
ATOM   1661 C  C   . ILE   A 1 220 ? 7.63300   -4.88200  10.10800  1.000 7.05682  ? 264 ILE   A C   1 
ATOM   1662 O  O   . ILE   A 1 220 ? 8.18300   -4.95500  9.00300   1.000 8.00682  ? 264 ILE   A O   1 
ATOM   1663 C  CB  . ILE   A 1 220 ? 8.74200   -5.30500  12.34100  1.000 8.24682  ? 264 ILE   A CB  1 
ATOM   1664 C  CG1 . ILE   A 1 220 ? 9.64300   -4.69200  13.41900  1.000 8.09682  ? 264 ILE   A CG1 1 
ATOM   1665 C  CG2 . ILE   A 1 220 ? 9.43600   -6.48300  11.66800  1.000 6.13682  ? 264 ILE   A CG2 1 
ATOM   1666 C  CD1 . ILE   A 1 220 ? 10.06600  -5.69200  14.50800  1.000 8.29682  ? 264 ILE   A CD1 1 
ATOM   1667 N  N   . ALA   A 1 221 ? 6.39100   -5.34000  10.31500  1.000 7.35682  ? 265 ALA   A N   1 
ATOM   1668 C  CA  . ALA   A 1 221 ? 5.69100   -6.08800  9.27300   1.000 5.52682  ? 265 ALA   A CA  1 
ATOM   1669 C  C   . ALA   A 1 221 ? 5.55200   -5.26800  7.99400   1.000 8.36682  ? 265 ALA   A C   1 
ATOM   1670 O  O   . ALA   A 1 221 ? 5.84500   -5.75800  6.89900   1.000 8.03682  ? 265 ALA   A O   1 
ATOM   1671 C  CB  . ALA   A 1 221 ? 4.31500   -6.53500  9.77300   1.000 8.31682  ? 265 ALA   A CB  1 
ATOM   1672 N  N   . LYS   A 1 222 ? 5.12400   -4.00200  8.11100   1.000 7.54682  ? 266 LYS   A N   1 
ATOM   1673 C  CA  . LYS   A 1 222 ? 4.79600   -3.26000  6.89700   1.000 9.51682  ? 266 LYS   A CA  1 
ATOM   1674 C  C   . LYS   A 1 222 ? 6.03200   -3.05500  6.01900   1.000 6.33682  ? 266 LYS   A C   1 
ATOM   1675 O  O   . LYS   A 1 222 ? 5.94800   -3.14300  4.78900   1.000 7.53682  ? 266 LYS   A O   1 
ATOM   1676 C  CB  . LYS   A 1 222 ? 4.13500   -1.92600  7.24300   1.000 6.18682  ? 266 LYS   A CB  1 
ATOM   1677 C  CG  . LYS   A 1 222 ? 5.04800   -0.92900  7.96200   1.000 7.16682  ? 266 LYS   A CG  1 
ATOM   1678 C  CD  . LYS   A 1 222 ? 4.27100   0.28100   8.48100   1.000 6.21682  ? 266 LYS   A CD  1 
ATOM   1679 C  CE  . LYS   A 1 222 ? 3.62700   1.07200   7.33800   1.000 12.35682 ? 266 LYS   A CE  1 
ATOM   1680 N  NZ  . LYS   A 1 222 ? 3.15200   2.40500   7.80200   1.000 11.30682 ? 266 LYS   A NZ  1 
ATOM   1681 N  N   . TYR   A 1 223 ? 7.19500   -2.81300  6.62300   1.000 7.13682  ? 267 TYR   A N   1 
ATOM   1682 C  CA  . TYR   A 1 223 ? 8.38100   -2.56700  5.80900   1.000 8.87682  ? 267 TYR   A CA  1 
ATOM   1683 C  C   . TYR   A 1 223 ? 9.15400   -3.84100  5.49600   1.000 5.31682  ? 267 TYR   A C   1 
ATOM   1684 O  O   . TYR   A 1 223 ? 9.83600   -3.89100  4.47600   1.000 7.60682  ? 267 TYR   A O   1 
ATOM   1685 C  CB  . TYR   A 1 223 ? 9.26900   -1.50300  6.47400   1.000 6.35682  ? 267 TYR   A CB  1 
ATOM   1686 C  CG  . TYR   A 1 223 ? 8.51500   -0.19300  6.56200   1.000 5.35682  ? 267 TYR   A CG  1 
ATOM   1687 C  CD1 . TYR   A 1 223 ? 8.04900   0.42900   5.39700   1.000 8.14682  ? 267 TYR   A CD1 1 
ATOM   1688 C  CD2 . TYR   A 1 223 ? 8.21400   0.39100   7.78500   1.000 5.77682  ? 267 TYR   A CD2 1 
ATOM   1689 C  CE1 . TYR   A 1 223 ? 7.32900   1.59300   5.44200   1.000 8.37682  ? 267 TYR   A CE1 1 
ATOM   1690 C  CE2 . TYR   A 1 223 ? 7.47500   1.58300   7.85300   1.000 7.29682  ? 267 TYR   A CE2 1 
ATOM   1691 C  CZ  . TYR   A 1 223 ? 7.03700   2.17300   6.66900   1.000 9.02682  ? 267 TYR   A CZ  1 
ATOM   1692 O  OH  . TYR   A 1 223 ? 6.31400   3.34600   6.68400   1.000 11.86682 ? 267 TYR   A OH  1 
ATOM   1693 N  N   . VAL   A 1 224 ? 9.02200   -4.89300  6.30300   1.000 6.92682  ? 268 VAL   A N   1 
ATOM   1694 C  CA  . VAL   A 1 224 ? 9.50200   -6.20400  5.86700   1.000 10.18682 ? 268 VAL   A CA  1 
ATOM   1695 C  C   . VAL   A 1 224 ? 8.77000   -6.64400  4.59500   1.000 8.01682  ? 268 VAL   A C   1 
ATOM   1696 O  O   . VAL   A 1 224 ? 9.39400   -7.06800  3.61200   1.000 7.94682  ? 268 VAL   A O   1 
ATOM   1697 C  CB  . VAL   A 1 224 ? 9.35200   -7.23700  6.99800   1.000 7.31682  ? 268 VAL   A CB  1 
ATOM   1698 C  CG1 . VAL   A 1 224 ? 9.40000   -8.65400  6.43900   1.000 5.25682  ? 268 VAL   A CG1 1 
ATOM   1699 C  CG2 . VAL   A 1 224 ? 10.47600  -7.05100  8.01000   1.000 6.02682  ? 268 VAL   A CG2 1 
ATOM   1700 N  N   . ILE   A 1 225 ? 7.43800   -6.52800  4.58800   1.000 7.25682  ? 269 ILE   A N   1 
ATOM   1701 C  CA  . ILE   A 1 225 ? 6.66400   -6.86900  3.39200   1.000 6.34682  ? 269 ILE   A CA  1 
ATOM   1702 C  C   . ILE   A 1 225 ? 7.07900   -5.99400  2.20900   1.000 7.18682  ? 269 ILE   A C   1 
ATOM   1703 O  O   . ILE   A 1 225 ? 7.26600   -6.48800  1.08600   1.000 6.81682  ? 269 ILE   A O   1 
ATOM   1704 C  CB  . ILE   A 1 225 ? 5.15400   -6.75700  3.68200   1.000 7.20682  ? 269 ILE   A CB  1 
ATOM   1705 C  CG1 . ILE   A 1 225 ? 4.71600   -7.87200  4.65400   1.000 8.65682  ? 269 ILE   A CG1 1 
ATOM   1706 C  CG2 . ILE   A 1 225 ? 4.34300   -6.84600  2.38300   1.000 7.46682  ? 269 ILE   A CG2 1 
ATOM   1707 C  CD1 . ILE   A 1 225 ? 3.39100   -7.61500  5.37500   1.000 7.49682  ? 269 ILE   A CD1 1 
ATOM   1708 N  N   . SER   A 1 226 ? 7.23500   -4.68400  2.43700   1.000 5.54682  ? 270 SER   A N   1 
ATOM   1709 C  CA  . SER   A 1 226 ? 7.58800   -3.79300  1.33100   1.000 6.45682  ? 270 SER   A CA  1 
ATOM   1710 C  C   . SER   A 1 226 ? 8.95800   -4.13500  0.75200   1.000 9.09682  ? 270 SER   A C   1 
ATOM   1711 O  O   . SER   A 1 226 ? 9.14400   -4.09600  -0.47000  1.000 7.62682  ? 270 SER   A O   1 
ATOM   1712 C  CB  . SER   A 1 226 ? 7.55300   -2.33200  1.78500   1.000 6.77682  ? 270 SER   A CB  1 
ATOM   1713 O  OG  . SER   A 1 226 ? 6.21800   -1.90100  2.02800   1.000 7.28682  ? 270 SER   A OG  1 
ATOM   1714 N  N   . TRP   A 1 227 ? 9.92400   -4.47500  1.61600   1.000 6.34682  ? 271 TRP   A N   1 
ATOM   1715 C  CA  . TRP   A 1 227 ? 11.27700  -4.80100  1.15500   1.000 6.42682  ? 271 TRP   A CA  1 
ATOM   1716 C  C   . TRP   A 1 227 ? 11.28700  -6.09100  0.34400   1.000 7.97682  ? 271 TRP   A C   1 
ATOM   1717 O  O   . TRP   A 1 227 ? 11.93800  -6.16600  -0.70700  1.000 6.47682  ? 271 TRP   A O   1 
ATOM   1718 C  CB  . TRP   A 1 227 ? 12.23600  -4.91300  2.35400   1.000 8.63682  ? 271 TRP   A CB  1 
ATOM   1719 C  CG  . TRP   A 1 227 ? 13.70600  -4.88200  1.96500   1.000 5.40682  ? 271 TRP   A CG  1 
ATOM   1720 C  CD1 . TRP   A 1 227 ? 14.53800  -5.95700  1.77400   1.000 7.43682  ? 271 TRP   A CD1 1 
ATOM   1721 C  CD2 . TRP   A 1 227 ? 14.49000  -3.71800  1.69600   1.000 6.14682  ? 271 TRP   A CD2 1 
ATOM   1722 N  NE1 . TRP   A 1 227 ? 15.79800  -5.52600  1.41600   1.000 6.72682  ? 271 TRP   A NE1 1 
ATOM   1723 C  CE2 . TRP   A 1 227 ? 15.79100  -4.15500  1.35300   1.000 6.60682  ? 271 TRP   A CE2 1 
ATOM   1724 C  CE3 . TRP   A 1 227 ? 14.22600  -2.34400  1.72500   1.000 6.41682  ? 271 TRP   A CE3 1 
ATOM   1725 C  CZ2 . TRP   A 1 227 ? 16.81500  -3.26700  1.03600   1.000 6.49682  ? 271 TRP   A CZ2 1 
ATOM   1726 C  CZ3 . TRP   A 1 227 ? 15.25700  -1.45700  1.41000   1.000 6.25682  ? 271 TRP   A CZ3 1 
ATOM   1727 C  CH2 . TRP   A 1 227 ? 16.52900  -1.92300  1.07700   1.000 6.13682  ? 271 TRP   A CH2 1 
ATOM   1728 N  N   . LEU   A 1 228 ? 10.59000  -7.12700  0.82000   1.000 5.82682  ? 272 LEU   A N   1 
ATOM   1729 C  CA  . LEU   A 1 228 ? 10.52600  -8.37200  0.05900   1.000 7.57682  ? 272 LEU   A CA  1 
ATOM   1730 C  C   . LEU   A 1 228 ? 9.80800   -8.16200  -1.26400  1.000 5.83682  ? 272 LEU   A C   1 
ATOM   1731 O  O   . LEU   A 1 228 ? 10.23600  -8.68000  -2.29800  1.000 7.81682  ? 272 LEU   A O   1 
ATOM   1732 C  CB  . LEU   A 1 228 ? 9.82500   -9.46000  0.86900   1.000 7.23682  ? 272 LEU   A CB  1 
ATOM   1733 C  CG  . LEU   A 1 228 ? 10.56700  -9.88200  2.14500   1.000 11.01682 ? 272 LEU   A CG  1 
ATOM   1734 C  CD1 . LEU   A 1 228 ? 9.75000   -10.90000 2.92100   1.000 7.94682  ? 272 LEU   A CD1 1 
ATOM   1735 C  CD2 . LEU   A 1 228 ? 11.93900  -10.43800 1.77600   1.000 8.11682  ? 272 LEU   A CD2 1 
ATOM   1736 N  N   . LYS   A 1 229 ? 8.70100   -7.41500  -1.24600  1.000 6.51682  ? 273 LYS   A N   1 
ATOM   1737 C  CA  . LYS   A 1 229 ? 8.00700   -7.11000  -2.49100  1.000 8.20682  ? 273 LYS   A CA  1 
ATOM   1738 C  C   . LYS   A 1 229 ? 8.93700   -6.40000  -3.46900  1.000 7.45682  ? 273 LYS   A C   1 
ATOM   1739 O  O   . LYS   A 1 229 ? 9.06600   -6.81000  -4.62200  1.000 8.26682  ? 273 LYS   A O   1 
ATOM   1740 C  CB  . LYS   A 1 229 ? 6.76600   -6.26500  -2.21100  1.000 7.67682  ? 273 LYS   A CB  1 
ATOM   1741 C  CG  . LYS   A 1 229 ? 5.57000   -7.04400  -1.69400  1.000 8.85682  ? 273 LYS   A CG  1 
ATOM   1742 C  CD  . LYS   A 1 229 ? 4.85100   -7.81800  -2.80100  1.000 7.88682  ? 273 LYS   A CD  1 
ATOM   1743 C  CE  . LYS   A 1 229 ? 3.51800   -8.36500  -2.28500  1.000 9.81682  ? 273 LYS   A CE  1 
ATOM   1744 N  NZ  . LYS   A 1 229 ? 2.82500   -9.26200  -3.27200  1.000 12.41682 ? 273 LYS   A NZ  1 
ATOM   1745 N  N   . ARG   A 1 230 ? 9.61400   -5.34200  -3.01700  1.000 7.72682  ? 274 ARG   A N   1 
ATOM   1746 C  CA  . ARG   A 1 230 ? 10.43500  -4.55600  -3.93700  1.000 10.14682 ? 274 ARG   A CA  1 
ATOM   1747 C  C   . ARG   A 1 230 ? 11.57500  -5.38300  -4.52900  1.000 10.24682 ? 274 ARG   A C   1 
ATOM   1748 O  O   . ARG   A 1 230 ? 11.87900  -5.27300  -5.72300  1.000 9.20682  ? 274 ARG   A O   1 
ATOM   1749 C  CB  . ARG   A 1 230 ? 10.97100  -3.31200  -3.22600  1.000 7.96682  ? 274 ARG   A CB  1 
ATOM   1750 C  CG  . ARG   A 1 230 ? 11.98900  -2.50200  -4.01100  1.000 8.16682  ? 274 ARG   A CG  1 
ATOM   1751 C  CD  . ARG   A 1 230 ? 11.49700  -2.09800  -5.40900  1.000 12.43682 ? 274 ARG   A CD  1 
ATOM   1752 N  NE  . ARG   A 1 230 ? 12.52300  -1.37400  -6.15600  1.000 11.23682 ? 274 ARG   A NE  1 
ATOM   1753 C  CZ  . ARG   A 1 230 ? 13.46200  -1.94800  -6.89900  1.000 12.44682 ? 274 ARG   A CZ  1 
ATOM   1754 N  NH1 . ARG   A 1 230 ? 13.50500  -3.26200  -7.07400  1.000 11.19682 ? 274 ARG   A NH1 1 
ATOM   1755 N  NH2 . ARG   A 1 230 ? 14.38500  -1.18700  -7.47900  1.000 9.98682  ? 274 ARG   A NH2 1 
ATOM   1756 N  N   . PHE   A 1 231 ? 12.20100  -6.24500  -3.73400  1.000 7.75682  ? 275 PHE   A N   1 
ATOM   1757 C  CA  . PHE   A 1 231 ? 13.42300  -6.87400  -4.22100  1.000 8.74682  ? 275 PHE   A CA  1 
ATOM   1758 C  C   . PHE   A 1 231 ? 13.28200  -8.34600  -4.58200  1.000 10.88682 ? 275 PHE   A C   1 
ATOM   1759 O  O   . PHE   A 1 231 ? 13.91700  -8.78400  -5.54100  1.000 10.78682 ? 275 PHE   A O   1 
ATOM   1760 C  CB  . PHE   A 1 231 ? 14.55900  -6.66800  -3.21000  1.000 8.42682  ? 275 PHE   A CB  1 
ATOM   1761 C  CG  . PHE   A 1 231 ? 14.96900  -5.23000  -3.10500  1.000 7.94682  ? 275 PHE   A CG  1 
ATOM   1762 C  CD1 . PHE   A 1 231 ? 15.59200  -4.60200  -4.17600  1.000 8.10682  ? 275 PHE   A CD1 1 
ATOM   1763 C  CD2 . PHE   A 1 231 ? 14.65100  -4.48200  -1.98300  1.000 6.03682  ? 275 PHE   A CD2 1 
ATOM   1764 C  CE1 . PHE   A 1 231 ? 15.94300  -3.24600  -4.11500  1.000 10.31682 ? 275 PHE   A CE1 1 
ATOM   1765 C  CE2 . PHE   A 1 231 ? 14.99200  -3.13500  -1.90700  1.000 8.72682  ? 275 PHE   A CE2 1 
ATOM   1766 C  CZ  . PHE   A 1 231 ? 15.64400  -2.51300  -2.99200  1.000 8.99682  ? 275 PHE   A CZ  1 
ATOM   1767 N  N   . VAL   A 1 232 ? 12.42600  -9.10600  -3.89500  1.000 6.77682  ? 276 VAL   A N   1 
ATOM   1768 C  CA  . VAL   A 1 232 ? 12.17400  -10.47500 -4.33000  1.000 9.93682  ? 276 VAL   A CA  1 
ATOM   1769 C  C   . VAL   A 1 232 ? 11.28000  -10.49400 -5.57100  1.000 9.41682  ? 276 VAL   A C   1 
ATOM   1770 O  O   . VAL   A 1 232 ? 11.50300  -11.28100 -6.49900  1.000 11.85682 ? 276 VAL   A O   1 
ATOM   1771 C  CB  . VAL   A 1 232 ? 11.56900  -11.30000 -3.17800  1.000 7.84682  ? 276 VAL   A CB  1 
ATOM   1772 C  CG1 . VAL   A 1 232 ? 11.34400  -12.74600 -3.62100  1.000 7.43682  ? 276 VAL   A CG1 1 
ATOM   1773 C  CG2 . VAL   A 1 232 ? 12.47800  -11.23100 -1.94900  1.000 7.37682  ? 276 VAL   A CG2 1 
ATOM   1774 N  N   . ASP   A 1 233 ? 10.27400  -9.62300  -5.61900  1.000 8.29682  ? 277 ASP   A N   1 
ATOM   1775 C  CA  . ASP   A 1 233 ? 9.35200   -9.55900  -6.74700  1.000 12.44682 ? 277 ASP   A CA  1 
ATOM   1776 C  C   . ASP   A 1 233 ? 9.70300   -8.47900  -7.76600  1.000 12.91682 ? 277 ASP   A C   1 
ATOM   1777 O  O   . ASP   A 1 233 ? 9.00200   -8.35800  -8.77800  1.000 12.09682 ? 277 ASP   A O   1 
ATOM   1778 C  CB  . ASP   A 1 233 ? 7.92100   -9.32100  -6.25300  1.000 11.16682 ? 277 ASP   A CB  1 
ATOM   1779 C  CG  . ASP   A 1 233 ? 7.38300   -10.47600 -5.44000  1.000 11.06682 ? 277 ASP   A CG  1 
ATOM   1780 O  OD1 . ASP   A 1 233 ? 8.08500   -11.50300 -5.29100  1.000 14.62682 ? 277 ASP   A OD1 1 
ATOM   1781 O  OD2 . ASP   A 1 233 ? 6.24200   -10.35800 -4.95000  1.000 14.07682 ? 277 ASP   A OD2 1 
ATOM   1782 N  N   . GLU   A 1 234 ? 10.75200  -7.68600  -7.52200  1.000 10.47682 ? 278 GLU   A N   1 
ATOM   1783 C  CA  . GLU   A 1 234 ? 11.07100  -6.52800  -8.36400  1.000 12.64682 ? 278 GLU   A CA  1 
ATOM   1784 C  C   . GLU   A 1 234 ? 9.86200   -5.60200  -8.51000  1.000 12.29682 ? 278 GLU   A C   1 
ATOM   1785 O  O   . GLU   A 1 234 ? 9.64300   -4.97100  -9.54500  1.000 14.84682 ? 278 GLU   A O   1 
ATOM   1786 C  CB  . GLU   A 1 234 ? 11.60800  -6.97300  -9.72600  1.000 15.99682 ? 278 GLU   A CB  1 
ATOM   1787 C  CG  . GLU   A 1 234 ? 12.90800  -7.76700  -9.61400  1.000 19.71682 ? 278 GLU   A CG  1 
ATOM   1788 C  CD  . GLU   A 1 234 ? 13.34000  -8.40300  -10.92500 1.000 30.73682 ? 278 GLU   A CD  1 
ATOM   1789 O  OE1 . GLU   A 1 234 ? 12.68500  -8.14800  -11.95600 1.000 22.67682 ? 278 GLU   A OE1 1 
ATOM   1790 O  OE2 . GLU   A 1 234 ? 14.34300  -9.15500  -10.92200 1.000 30.38682 ? 278 GLU   A OE2 1 
ATOM   1791 N  N   . ASP   A 1 235 ? 9.07100   -5.50100  -7.45200  1.000 11.09682 ? 279 ASP   A N   1 
ATOM   1792 C  CA  . ASP   A 1 235 ? 7.75900   -4.85400  -7.51900  1.000 10.64682 ? 279 ASP   A CA  1 
ATOM   1793 C  C   . ASP   A 1 235 ? 7.88700   -3.38500  -7.10800  1.000 10.67682 ? 279 ASP   A C   1 
ATOM   1794 O  O   . ASP   A 1 235 ? 7.88600   -3.05900  -5.91600  1.000 13.34682 ? 279 ASP   A O   1 
ATOM   1795 C  CB  . ASP   A 1 235 ? 6.77000   -5.60800  -6.63700  1.000 11.54682 ? 279 ASP   A CB  1 
ATOM   1796 C  CG  . ASP   A 1 235 ? 5.33900   -5.14200  -6.82200  1.000 16.50682 ? 279 ASP   A CG  1 
ATOM   1797 O  OD1 . ASP   A 1 235 ? 5.11000   -4.10500  -7.48700  1.000 14.38682 ? 279 ASP   A OD1 1 
ATOM   1798 O  OD2 . ASP   A 1 235 ? 4.43700   -5.82800  -6.30500  1.000 11.40682 ? 279 ASP   A OD2 1 
ATOM   1799 N  N   . THR   A 1 236 ? 7.95500   -2.49000  -8.10100  1.000 13.72682 ? 280 THR   A N   1 
ATOM   1800 C  CA  . THR   A 1 236 ? 8.15500   -1.07100  -7.81900  1.000 17.04682 ? 280 THR   A CA  1 
ATOM   1801 C  C   . THR   A 1 236 ? 6.89300   -0.37200  -7.33100  1.000 14.73682 ? 280 THR   A C   1 
ATOM   1802 O  O   . THR   A 1 236 ? 6.96900   0.80700   -6.96600  1.000 15.69682 ? 280 THR   A O   1 
ATOM   1803 C  CB  . THR   A 1 236 ? 8.70800   -0.34900  -9.05100  1.000 14.01682 ? 280 THR   A CB  1 
ATOM   1804 O  OG1 . THR   A 1 236 ? 7.82800   -0.56000  -10.16500 1.000 11.36682 ? 280 THR   A OG1 1 
ATOM   1805 C  CG2 . THR   A 1 236 ? 10.09200  -0.88800  -9.38600  1.000 14.70682 ? 280 THR   A CG2 1 
ATOM   1806 N  N   . ARG   A 1 237 ? 5.74700   -1.06300  -7.28500  1.000 9.58682  ? 281 ARG   A N   1 
ATOM   1807 C  CA  . ARG   A 1 237 ? 4.58600   -0.47700  -6.63300  1.000 10.65682 ? 281 ARG   A CA  1 
ATOM   1808 C  C   . ARG   A 1 237 ? 4.84700   -0.22100  -5.15300  1.000 12.06682 ? 281 ARG   A C   1 
ATOM   1809 O  O   . ARG   A 1 237 ? 4.14900   0.59600   -4.55000  1.000 11.36682 ? 281 ARG   A O   1 
ATOM   1810 C  CB  . ARG   A 1 237 ? 3.35700   -1.38400  -6.77800  1.000 12.29682 ? 281 ARG   A CB  1 
ATOM   1811 C  CG  . ARG   A 1 237 ? 2.93300   -1.71200  -8.20800  1.000 13.62682 ? 281 ARG   A CG  1 
ATOM   1812 C  CD  . ARG   A 1 237 ? 1.73700   -2.65700  -8.21500  1.000 15.90682 ? 281 ARG   A CD  1 
ATOM   1813 N  NE  . ARG   A 1 237 ? 2.04900   -3.93400  -7.58200  1.000 15.46682 ? 281 ARG   A NE  1 
ATOM   1814 C  CZ  . ARG   A 1 237 ? 1.17100   -4.90300  -7.35400  1.000 18.78682 ? 281 ARG   A CZ  1 
ATOM   1815 N  NH1 . ARG   A 1 237 ? -0.10400  -4.77900  -7.69200  1.000 19.04682 ? 281 ARG   A NH1 1 
ATOM   1816 N  NH2 . ARG   A 1 237 ? 1.58300   -6.02700  -6.77200  1.000 16.86682 ? 281 ARG   A NH2 1 
ATOM   1817 N  N   . TYR   A 1 238 ? 5.82600   -0.90900  -4.56000  1.000 11.19682 ? 282 TYR   A N   1 
ATOM   1818 C  CA  . TYR   A 1 238 ? 6.15700   -0.78300  -3.14600  1.000 9.66682  ? 282 TYR   A CA  1 
ATOM   1819 C  C   . TYR   A 1 238 ? 7.28400   0.21500   -2.88400  1.000 11.80682 ? 282 TYR   A C   1 
ATOM   1820 O  O   . TYR   A 1 238 ? 7.60100   0.48400   -1.71600  1.000 9.63682  ? 282 TYR   A O   1 
ATOM   1821 C  CB  . TYR   A 1 238 ? 6.50200   -2.17400  -2.56700  1.000 6.27682  ? 282 TYR   A CB  1 
ATOM   1822 C  CG  . TYR   A 1 238 ? 5.25900   -3.04000  -2.42200  1.000 8.72682  ? 282 TYR   A CG  1 
ATOM   1823 C  CD1 . TYR   A 1 238 ? 4.75100   -3.75300  -3.50100  1.000 12.95682 ? 282 TYR   A CD1 1 
ATOM   1824 C  CD2 . TYR   A 1 238 ? 4.55900   -3.08800  -1.22200  1.000 10.99682 ? 282 TYR   A CD2 1 
ATOM   1825 C  CE1 . TYR   A 1 238 ? 3.59200   -4.52000  -3.37600  1.000 15.08682 ? 282 TYR   A CE1 1 
ATOM   1826 C  CE2 . TYR   A 1 238 ? 3.40500   -3.84600  -1.08400  1.000 9.80682  ? 282 TYR   A CE2 1 
ATOM   1827 C  CZ  . TYR   A 1 238 ? 2.92900   -4.56300  -2.16200  1.000 11.89682 ? 282 TYR   A CZ  1 
ATOM   1828 O  OH  . TYR   A 1 238 ? 1.77800   -5.30500  -2.03200  1.000 14.11682 ? 282 TYR   A OH  1 
ATOM   1829 N  N   . SER   A 1 239 ? 7.88000   0.78500   -3.93600  1.000 10.32682 ? 283 SER   A N   1 
ATOM   1830 C  CA  . SER   A 1 239 ? 8.86200   1.85000   -3.74200  1.000 11.86682 ? 283 SER   A CA  1 
ATOM   1831 C  C   . SER   A 1 239 ? 8.26300   3.05700   -3.03500  1.000 12.57682 ? 283 SER   A C   1 
ATOM   1832 O  O   . SER   A 1 239 ? 8.98800   3.79600   -2.36000  1.000 11.13682 ? 283 SER   A O   1 
ATOM   1833 C  CB  . SER   A 1 239 ? 9.45900   2.28600   -5.08300  1.000 10.18682 ? 283 SER   A CB  1 
ATOM   1834 O  OG  . SER   A 1 239 ? 10.32300  1.28600   -5.59400  1.000 15.73682 ? 283 SER   A OG  1 
ATOM   1835 N  N   . GLN   A 1 240 ? 6.95200   3.27700   -3.17800  1.000 10.95682 ? 284 GLN   A N   1 
ATOM   1836 C  CA  . GLN   A 1 240 ? 6.32300   4.44800   -2.56400  1.000 13.46682 ? 284 GLN   A CA  1 
ATOM   1837 C  C   . GLN   A 1 240 ? 6.42800   4.43100   -1.04500  1.000 13.14682 ? 284 GLN   A C   1 
ATOM   1838 O  O   . GLN   A 1 240 ? 6.45500   5.49700   -0.41800  1.000 14.61682 ? 284 GLN   A O   1 
ATOM   1839 C  CB  . GLN   A 1 240 ? 4.85800   4.53800   -2.97900  1.000 12.91682 ? 284 GLN   A CB  1 
ATOM   1840 C  CG  . GLN   A 1 240 ? 4.02000   3.33000   -2.56800  1.000 8.33682  ? 284 GLN   A CG  1 
ATOM   1841 C  CD  . GLN   A 1 240 ? 2.58200   3.44700   -3.01800  1.000 13.56682 ? 284 GLN   A CD  1 
ATOM   1842 O  OE1 . GLN   A 1 240 ? 1.85800   4.32300   -2.56200  1.000 15.16682 ? 284 GLN   A OE1 1 
ATOM   1843 N  NE2 . GLN   A 1 240 ? 2.15800   2.55700   -3.92000  1.000 13.75682 ? 284 GLN   A NE2 1 
ATOM   1844 N  N   . PHE   A 1 241 ? 6.46900   3.24500   -0.43400  1.000 10.53682 ? 285 PHE   A N   1 
ATOM   1845 C  CA  . PHE   A 1 241 ? 6.55900   3.13800   1.02100   1.000 12.48682 ? 285 PHE   A CA  1 
ATOM   1846 C  C   . PHE   A 1 241 ? 7.98900   3.15800   1.53200   1.000 11.04682 ? 285 PHE   A C   1 
ATOM   1847 O  O   . PHE   A 1 241 ? 8.20000   3.38700   2.73300   1.000 7.87682  ? 285 PHE   A O   1 
ATOM   1848 C  CB  . PHE   A 1 241 ? 5.87500   1.85300   1.51400   1.000 9.26682  ? 285 PHE   A CB  1 
ATOM   1849 C  CG  . PHE   A 1 241 ? 4.50000   1.65700   0.95100   1.000 11.26682 ? 285 PHE   A CG  1 
ATOM   1850 C  CD1 . PHE   A 1 241 ? 3.47200   2.51900   1.29900   1.000 15.28682 ? 285 PHE   A CD1 1 
ATOM   1851 C  CD2 . PHE   A 1 241 ? 4.24100   0.62800   0.05400   1.000 9.35682  ? 285 PHE   A CD2 1 
ATOM   1852 C  CE1 . PHE   A 1 241 ? 2.20000   2.35600   0.76000   1.000 13.80682 ? 285 PHE   A CE1 1 
ATOM   1853 C  CE2 . PHE   A 1 241 ? 2.97200   0.45600   -0.48500  1.000 11.67682 ? 285 PHE   A CE2 1 
ATOM   1854 C  CZ  . PHE   A 1 241 ? 1.95700   1.32300   -0.13600  1.000 11.63682 ? 285 PHE   A CZ  1 
ATOM   1855 N  N   . LEU   A 1 242 ? 8.96400   2.91000   0.65500   1.000 8.39682  ? 286 LEU   A N   1 
ATOM   1856 C  CA  . LEU   A 1 242 ? 10.36400  2.82700   1.04800   1.000 10.41682 ? 286 LEU   A CA  1 
ATOM   1857 C  C   . LEU   A 1 242 ? 11.13300  4.11600   0.81000   1.000 9.30682  ? 286 LEU   A C   1 
ATOM   1858 O  O   . LEU   A 1 242 ? 12.11400  4.38100   1.51700   1.000 11.17682 ? 286 LEU   A O   1 
ATOM   1859 C  CB  . LEU   A 1 242 ? 11.05600  1.68000   0.28900   1.000 8.15682  ? 286 LEU   A CB  1 
ATOM   1860 C  CG  . LEU   A 1 242 ? 10.54100  0.26500   0.58400   1.000 8.99682  ? 286 LEU   A CG  1 
ATOM   1861 C  CD1 . LEU   A 1 242 ? 11.13500  -0.77100  -0.36400  1.000 8.66682  ? 286 LEU   A CD1 1 
ATOM   1862 C  CD2 . LEU   A 1 242 ? 10.82200  -0.11400  2.04300   1.000 10.60682 ? 286 LEU   A CD2 1 
ATOM   1863 N  N   . CYS   A 1 243 ? 10.71500  4.91900   -0.17200  1.000 13.94682 ? 287 CYS   A N   1 
ATOM   1864 C  CA  . CYS   A 1 243 ? 11.42700  6.11600   -0.59100  1.000 9.33682  ? 287 CYS   A CA  1 
ATOM   1865 C  C   . CYS   A 1 243 ? 10.39500  7.19900   -0.90500  1.000 9.49682  ? 287 CYS   A C   1 
ATOM   1866 O  O   . CYS   A 1 243 ? 9.41900   6.92100   -1.62100  1.000 9.89682  ? 287 CYS   A O   1 
ATOM   1867 C  CB  . CYS   A 1 243 ? 12.30400  5.84700   -1.81400  1.000 14.47682 ? 287 CYS   A CB  1 
ATOM   1868 S  SG  . CYS   A 1 243 ? 13.54600  4.54200   -1.59600  1.000 12.55682 ? 287 CYS   A SG  1 
ATOM   1869 N  N   . PRO   A 1 244 ? 10.54900  8.42600   -0.36500  1.000 11.61682 ? 288 PRO   A N   1 
ATOM   1870 C  CA  . PRO   A 1 244 ? 11.56800  8.79200   0.63000   1.000 10.23682 ? 288 PRO   A CA  1 
ATOM   1871 C  C   . PRO   A 1 244 ? 11.42700  8.00400   1.93500   1.000 12.37682 ? 288 PRO   A C   1 
ATOM   1872 O  O   . PRO   A 1 244 ? 10.44200  7.27300   2.11500   1.000 9.52682  ? 288 PRO   A O   1 
ATOM   1873 C  CB  . PRO   A 1 244 ? 11.31000  10.28400  0.89000   1.000 11.40682 ? 288 PRO   A CB  1 
ATOM   1874 C  CG  . PRO   A 1 244 ? 10.46900  10.75300  -0.26900  1.000 22.19682 ? 288 PRO   A CG  1 
ATOM   1875 C  CD  . PRO   A 1 244 ? 9.65800   9.55700   -0.68500  1.000 15.55682 ? 288 PRO   A CD  1 
ATOM   1876 N  N   . ASN   A 1 245 ? 12.40000  8.17800   2.82000   1.000 10.39682 ? 289 ASN   A N   1 
ATOM   1877 C  CA  . ASN   A 1 245 ? 12.45500  7.42400   4.06200   1.000 9.92682  ? 289 ASN   A CA  1 
ATOM   1878 C  C   . ASN   A 1 245 ? 11.13200  7.52800   4.82200   1.000 12.96682 ? 289 ASN   A C   1 
ATOM   1879 O  O   . ASN   A 1 245 ? 10.57700  8.63100   4.95500   1.000 9.97682  ? 289 ASN   A O   1 
ATOM   1880 C  CB  . ASN   A 1 245 ? 13.59100  7.94600   4.94800   1.000 7.09682  ? 289 ASN   A CB  1 
ATOM   1881 C  CG  . ASN   A 1 245 ? 14.95100  7.64900   4.38900   1.000 12.07682 ? 289 ASN   A CG  1 
ATOM   1882 O  OD1 . ASN   A 1 245 ? 15.08300  6.88200   3.43600   1.000 14.61682 ? 289 ASN   A OD1 1 
ATOM   1883 N  ND2 . ASN   A 1 245 ? 15.99100  8.23800   4.99700   1.000 10.25682 ? 289 ASN   A ND2 1 
ATOM   1884 N  N   . PRO   A 1 246 ? 10.62300  6.41500   5.35400   1.000 9.69682  ? 290 PRO   A N   1 
ATOM   1885 C  CA  . PRO   A 1 246 ? 9.42500   6.45700   6.20700   1.000 7.69682  ? 290 PRO   A CA  1 
ATOM   1886 C  C   . PRO   A 1 246 ? 9.57400   7.38100   7.41100   1.000 9.60682  ? 290 PRO   A C   1 
ATOM   1887 O  O   . PRO   A 1 246 ? 10.66800  7.58400   7.94700   1.000 12.26682 ? 290 PRO   A O   1 
ATOM   1888 C  CB  . PRO   A 1 246 ? 9.26900   5.00300   6.66200   1.000 9.84682  ? 290 PRO   A CB  1 
ATOM   1889 C  CG  . PRO   A 1 246 ? 9.98500   4.19200   5.60700   1.000 11.43682 ? 290 PRO   A CG  1 
ATOM   1890 C  CD  . PRO   A 1 246 ? 11.10400  5.04000   5.12300   1.000 11.17682 ? 290 PRO   A CD  1 
ATOM   1891 N  N   . THR   A 1 247 ? 8.43200   7.90300   7.86800   1.000 10.43682 ? 291 THR   A N   1 
ATOM   1892 C  CA  . THR   A 1 247 ? 8.38400   8.80600   9.01100   1.000 10.10682 ? 291 THR   A CA  1 
ATOM   1893 C  C   . THR   A 1 247 ? 7.44800   8.33800   10.12600  1.000 9.95682  ? 291 THR   A C   1 
ATOM   1894 O  O   . THR   A 1 247 ? 7.10100   9.15400   10.98700  1.000 9.78682  ? 291 THR   A O   1 
ATOM   1895 C  CB  . THR   A 1 247 ? 7.95200   10.21200  8.56000   1.000 11.68682 ? 291 THR   A CB  1 
ATOM   1896 O  OG1 . THR   A 1 247 ? 6.67500   10.12800  7.91400   1.000 12.98682 ? 291 THR   A OG1 1 
ATOM   1897 C  CG2 . THR   A 1 247 ? 8.96000   10.81200  7.58000   1.000 18.05682 ? 291 THR   A CG2 1 
ATOM   1898 N  N   . ASP   A 1 248 ? 7.02000   7.06600   10.12900  1.000 8.88682  ? 292 ASP   A N   1 
ATOM   1899 C  CA  . ASP   A 1 248 ? 6.13100   6.52200   11.16300  1.000 12.45682 ? 292 ASP   A CA  1 
ATOM   1900 C  C   . ASP   A 1 248 ? 6.55400   6.95700   12.56700  1.000 9.23682  ? 292 ASP   A C   1 
ATOM   1901 O  O   . ASP   A 1 248 ? 7.74500   6.99700   12.88500  1.000 8.52682  ? 292 ASP   A O   1 
ATOM   1902 C  CB  . ASP   A 1 248 ? 6.11900   4.98100   11.12600  1.000 8.75682  ? 292 ASP   A CB  1 
ATOM   1903 C  CG  . ASP   A 1 248 ? 5.68300   4.40300   9.78700   1.000 14.00682 ? 292 ASP   A CG  1 
ATOM   1904 O  OD1 . ASP   A 1 248 ? 6.21700   4.81500   8.72900   1.000 11.99682 ? 292 ASP   A OD1 1 
ATOM   1905 O  OD2 . ASP   A 1 248 ? 4.82600   3.48600   9.80300   1.000 11.34682 ? 292 ASP   A OD2 1 
ATOM   1906 N  N   . ARG   A 1 249 ? 5.56600   7.23200   13.42600  1.000 10.13682 ? 293 ARG   A N   1 
ATOM   1907 C  CA  . ARG   A 1 249 ? 5.88100   7.64700   14.79400  1.000 11.05682 ? 293 ARG   A CA  1 
ATOM   1908 C  C   . ARG   A 1 249 ? 6.77800   6.64000   15.51600  1.000 11.14682 ? 293 ARG   A C   1 
ATOM   1909 O  O   . ARG   A 1 249 ? 7.62800   7.03900   16.32000  1.000 13.34682 ? 293 ARG   A O   1 
ATOM   1910 C  CB  . ARG   A 1 249 ? 4.59600   7.87700   15.59700  1.000 16.79682 ? 293 ARG   A CB  1 
ATOM   1911 C  CG  . ARG   A 1 249 ? 3.72700   9.04700   15.09900  1.000 28.01682 ? 293 ARG   A CG  1 
ATOM   1912 C  CD  . ARG   A 1 249 ? 4.51700   10.36200  14.94100  1.000 23.85682 ? 293 ARG   A CD  1 
ATOM   1913 N  NE  . ARG   A 1 249 ? 5.16300   10.76800  16.18300  1.000 25.59682 ? 293 ARG   A NE  1 
ATOM   1914 C  CZ  . ARG   A 1 249 ? 6.01700   11.77700  16.29600  1.000 27.20682 ? 293 ARG   A CZ  1 
ATOM   1915 N  NH1 . ARG   A 1 249 ? 6.34400   12.52500  15.25300  1.000 25.65682 ? 293 ARG   A NH1 1 
ATOM   1916 N  NH2 . ARG   A 1 249 ? 6.56500   12.03500  17.48400  1.000 20.09682 ? 293 ARG   A NH2 1 
ATOM   1917 N  N   . ALA   A 1 250 ? 6.62100   5.34000   15.24000  1.000 8.81682  ? 294 ALA   A N   1 
ATOM   1918 C  CA  . ALA   A 1 250 ? 7.41700   4.31700   15.92100  1.000 8.40682  ? 294 ALA   A CA  1 
ATOM   1919 C  C   . ALA   A 1 250 ? 8.88300   4.30100   15.49700  1.000 7.01682  ? 294 ALA   A C   1 
ATOM   1920 O  O   . ALA   A 1 250 ? 9.67000   3.54200   16.08300  1.000 9.31682  ? 294 ALA   A O   1 
ATOM   1921 C  CB  . ALA   A 1 250 ? 6.80700   2.93500   15.68000  1.000 9.25682  ? 294 ALA   A CB  1 
ATOM   1922 N  N   . ILE   A 1 251 ? 9.26900   5.09500   14.50300  1.000 8.15682  ? 295 ILE   A N   1 
ATOM   1923 C  CA  . ILE   A 1 251 ? 10.63100  5.10000   13.97500  1.000 8.94682  ? 295 ILE   A CA  1 
ATOM   1924 C  C   . ILE   A 1 251 ? 11.38400  6.27600   14.58000  1.000 10.15682 ? 295 ILE   A C   1 
ATOM   1925 O  O   . ILE   A 1 251 ? 10.89100  7.41100   14.56000  1.000 9.22682  ? 295 ILE   A O   1 
ATOM   1926 C  CB  . ILE   A 1 251 ? 10.62100  5.18300   12.43900  1.000 7.51682  ? 295 ILE   A CB  1 
ATOM   1927 C  CG1 . ILE   A 1 251 ? 9.84200   4.00300   11.86700  1.000 6.71682  ? 295 ILE   A CG1 1 
ATOM   1928 C  CG2 . ILE   A 1 251 ? 12.05100  5.26900   11.89800  1.000 9.37682  ? 295 ILE   A CG2 1 
ATOM   1929 C  CD1 . ILE   A 1 251 ? 9.65700   4.01900   10.33600  1.000 6.76682  ? 295 ILE   A CD1 1 
ATOM   1930 N  N   . CYS   A 1 252 ? 12.58100  6.01600   15.11600  1.000 8.96682  ? 296 CYS   A N   1 
ATOM   1931 C  CA  . CYS   A 1 252 ? 13.39600  7.07400   15.69700  1.000 9.54682  ? 296 CYS   A CA  1 
ATOM   1932 C  C   . CYS   A 1 252 ? 14.62500  7.44200   14.87200  1.000 8.66682  ? 296 CYS   A C   1 
ATOM   1933 O  O   . CYS   A 1 252 ? 15.22000  8.49600   15.11600  1.000 7.85682  ? 296 CYS   A O   1 
ATOM   1934 C  CB  . CYS   A 1 252 ? 13.82400  6.69100   17.12200  1.000 13.62682 ? 296 CYS   A CB  1 
ATOM   1935 S  SG  . CYS   A 1 252 ? 12.66700  7.34000   18.37900  1.000 26.80682 ? 296 CYS   A SG  1 
ATOM   1936 N  N   . GLU   A 1 253 ? 15.02900  6.59700   13.92800  1.000 8.36682  ? 297 GLU   A N   1 
ATOM   1937 C  CA  . GLU   A 1 253 ? 16.01300  6.97200   12.92500  1.000 7.97682  ? 297 GLU   A CA  1 
ATOM   1938 C  C   . GLU   A 1 253 ? 15.80200  6.08200   11.70900  1.000 9.81682  ? 297 GLU   A C   1 
ATOM   1939 O  O   . GLU   A 1 253 ? 15.46300  4.90300   11.85000  1.000 7.99682  ? 297 GLU   A O   1 
ATOM   1940 C  CB  . GLU   A 1 253 ? 17.44800  6.83300   13.44500  1.000 12.58682 ? 297 GLU   A CB  1 
ATOM   1941 C  CG  . GLU   A 1 253 ? 18.48900  6.99900   12.35000  1.000 16.65682 ? 297 GLU   A CG  1 
ATOM   1942 C  CD  . GLU   A 1 253 ? 19.85300  7.36600   12.86400  1.000 25.55682 ? 297 GLU   A CD  1 
ATOM   1943 O  OE1 . GLU   A 1 253 ? 20.18300  7.00200   14.01300  1.000 33.30682 ? 297 GLU   A OE1 1 
ATOM   1944 O  OE2 . GLU   A 1 253 ? 20.59800  8.03100   12.10800  1.000 35.21682 ? 297 GLU   A OE2 1 
ATOM   1945 N  N   . TYR   A 1 254 ? 15.99900  6.64900   10.52400  1.000 8.34682  ? 298 TYR   A N   1 
ATOM   1946 C  CA  . TYR   A 1 254 ? 15.94500  5.88100   9.28400   1.000 9.73682  ? 298 TYR   A CA  1 
ATOM   1947 C  C   . TYR   A 1 254 ? 17.04700  6.36400   8.34600   1.000 8.87682  ? 298 TYR   A C   1 
ATOM   1948 O  O   . TYR   A 1 254 ? 17.21800  7.57300   8.16900   1.000 12.03682 ? 298 TYR   A O   1 
ATOM   1949 C  CB  . TYR   A 1 254 ? 14.57100  6.02200   8.62100   1.000 6.18682  ? 298 TYR   A CB  1 
ATOM   1950 C  CG  . TYR   A 1 254 ? 14.22400  4.91100   7.65500   1.000 7.41682  ? 298 TYR   A CG  1 
ATOM   1951 C  CD1 . TYR   A 1 254 ? 14.75500  4.88200   6.36400   1.000 7.39682  ? 298 TYR   A CD1 1 
ATOM   1952 C  CD2 . TYR   A 1 254 ? 13.35300  3.89600   8.02800   1.000 8.36682  ? 298 TYR   A CD2 1 
ATOM   1953 C  CE1 . TYR   A 1 254 ? 14.42500  3.85100   5.47000   1.000 8.64682  ? 298 TYR   A CE1 1 
ATOM   1954 C  CE2 . TYR   A 1 254 ? 13.01600  2.87300   7.14600   1.000 9.19682  ? 298 TYR   A CE2 1 
ATOM   1955 C  CZ  . TYR   A 1 254 ? 13.54800  2.85600   5.87100   1.000 7.35682  ? 298 TYR   A CZ  1 
ATOM   1956 O  OH  . TYR   A 1 254 ? 13.19400  1.83700   5.00000   1.000 9.84682  ? 298 TYR   A OH  1 
ATOM   1957 N  N   . ARG   A 1 255 ? 17.79300  5.42700   7.75400   1.000 4.58682  ? 299 ARG   A N   1 
ATOM   1958 C  CA  . ARG   A 1 255 ? 18.81800  5.73000   6.75700   1.000 9.59682  ? 299 ARG   A CA  1 
ATOM   1959 C  C   . ARG   A 1 255 ? 18.56800  4.86700   5.52600   1.000 8.40682  ? 299 ARG   A C   1 
ATOM   1960 O  O   . ARG   A 1 255 ? 18.07600  3.74500   5.64400   1.000 5.46682  ? 299 ARG   A O   1 
ATOM   1961 C  CB  . ARG   A 1 255 ? 20.25300  5.46000   7.28800   1.000 7.78682  ? 299 ARG   A CB  1 
ATOM   1962 C  CG  . ARG   A 1 255 ? 20.58400  6.15000   8.60600   1.000 9.76682  ? 299 ARG   A CG  1 
ATOM   1963 C  CD  . ARG   A 1 255 ? 21.95400  5.73900   9.15600   1.000 10.16682 ? 299 ARG   A CD  1 
ATOM   1964 N  NE  . ARG   A 1 255 ? 22.16500  6.33600   10.47200  1.000 12.04682 ? 299 ARG   A NE  1 
ATOM   1965 C  CZ  . ARG   A 1 255 ? 23.25700  6.20300   11.21500  1.000 17.75682 ? 299 ARG   A CZ  1 
ATOM   1966 N  NH1 . ARG   A 1 255 ? 24.31000  5.52500   10.78800  1.000 9.28682  ? 299 ARG   A NH1 1 
ATOM   1967 N  NH2 . ARG   A 1 255 ? 23.29400  6.77600   12.42000  1.000 13.05682 ? 299 ARG   A NH2 1 
ATOM   1968 N  N   . SER   A 1 256 ? 18.91600  5.38200   4.34400   1.000 7.78682  ? 300 SER   A N   1 
ATOM   1969 C  CA  . SER   A 1 256 ? 18.72200  4.60000   3.12500   1.000 8.60682  ? 300 SER   A CA  1 
ATOM   1970 C  C   . SER   A 1 256 ? 19.58500  5.15000   1.99800   1.000 10.14682 ? 300 SER   A C   1 
ATOM   1971 O  O   . SER   A 1 256 ? 20.07000  6.28200   2.05300   1.000 6.78682  ? 300 SER   A O   1 
ATOM   1972 C  CB  . SER   A 1 256 ? 17.26300  4.61500   2.66700   1.000 9.36682  ? 300 SER   A CB  1 
ATOM   1973 O  OG  . SER   A 1 256 ? 17.01500  5.76100   1.86900   1.000 7.08682  ? 300 SER   A OG  1 
ATOM   1974 N  N   . THR   A 1 257 ? 19.73600  4.33100   0.95600   1.000 8.78682  ? 301 THR   A N   1 
ATOM   1975 C  CA  . THR   A 1 257 ? 20.29000  4.75600   -0.32200  1.000 9.66682  ? 301 THR   A CA  1 
ATOM   1976 C  C   . THR   A 1 257 ? 19.19600  5.02800   -1.35200  1.000 13.17682 ? 301 THR   A C   1 
ATOM   1977 O  O   . THR   A 1 257 ? 19.38300  4.75200   -2.54600  1.000 9.33682  ? 301 THR   A O   1 
ATOM   1978 C  CB  . THR   A 1 257 ? 21.27600  3.71900   -0.86900  1.000 11.79682 ? 301 THR   A CB  1 
ATOM   1979 O  OG1 . THR   A 1 257 ? 20.67200  2.41400   -0.87300  1.000 9.62682  ? 301 THR   A OG1 1 
ATOM   1980 C  CG2 . THR   A 1 257 ? 22.55900  3.69600   -0.05500  1.000 10.22682 ? 301 THR   A CG2 1 
ATOM   1981 N  N   . CYS   A 1 258 ? 18.04900  5.55200   -0.90900  1.000 11.55682 ? 302 CYS   A N   1 
ATOM   1982 C  CA  . CYS   A 1 258 ? 17.00300  5.96700   -1.83500  1.000 13.77682 ? 302 CYS   A CA  1 
ATOM   1983 C  C   . CYS   A 1 258 ? 17.54800  7.01400   -2.81100  1.000 11.25682 ? 302 CYS   A C   1 
ATOM   1984 O  O   . CYS   A 1 258 ? 18.47900  7.75800   -2.47800  1.000 11.90682 ? 302 CYS   A O   1 
ATOM   1985 C  CB  . CYS   A 1 258 ? 15.80600  6.53600   -1.06600  1.000 9.48682  ? 302 CYS   A CB  1 
ATOM   1986 S  SG  . CYS   A 1 258 ? 14.80800  5.30500   -0.18400  1.000 12.57682 ? 302 CYS   A SG  1 
ATOM   1987 N  N   . PRO   A 1 259 ? 16.95900  7.12600   -4.02200  1.000 15.21682 ? 303 PRO   A N   1 
ATOM   1988 C  CA  . PRO   A 1 259 ? 15.78000  6.39400   -4.50100  1.000 10.60682 ? 303 PRO   A CA  1 
ATOM   1989 C  C   . PRO   A 1 259 ? 16.07800  5.00700   -5.05800  1.000 14.45682 ? 303 PRO   A C   1 
ATOM   1990 O  O   . PRO   A 1 259 ? 17.09300  4.82500   -5.72200  1.000 15.20682 ? 303 PRO   A O   1 
ATOM   1991 C  CB  . PRO   A 1 259 ? 15.25300  7.29800   -5.61600  1.000 14.75682 ? 303 PRO   A CB  1 
ATOM   1992 C  CG  . PRO   A 1 259 ? 16.48900  7.91000   -6.18600  1.000 13.30682 ? 303 PRO   A CG  1 
ATOM   1993 C  CD  . PRO   A 1 259 ? 17.37000  8.17300   -4.97900  1.000 14.30682 ? 303 PRO   A CD  1 
ATOM   1994 N  N   . TYR   A 1 260 ? 15.20100  4.04400   -4.77300  1.000 13.82682 ? 304 TYR   A N   1 
ATOM   1995 C  CA  . TYR   A 1 260 ? 15.16100  2.78500   -5.51900  1.000 12.54682 ? 304 TYR   A CA  1 
ATOM   1996 C  C   . TYR   A 1 260 ? 13.72200  2.29100   -5.59200  1.000 17.81682 ? 304 TYR   A C   1 
ATOM   1997 O  O   . TYR   A 1 260 ? 12.80500  2.93100   -5.06800  1.000 18.93682 ? 304 TYR   A O   1 
ATOM   1998 C  CB  . TYR   A 1 260 ? 16.06800  1.70900   -4.89700  1.000 12.13682 ? 304 TYR   A CB  1 
ATOM   1999 C  CG  . TYR   A 1 260 ? 16.10600  1.68000   -3.38000  1.000 11.42682 ? 304 TYR   A CG  1 
ATOM   2000 C  CD1 . TYR   A 1 260 ? 15.00100  1.28700   -2.63200  1.000 8.54682  ? 304 TYR   A CD1 1 
ATOM   2001 C  CD2 . TYR   A 1 260 ? 17.26500  2.02900   -2.69900  1.000 11.15682 ? 304 TYR   A CD2 1 
ATOM   2002 C  CE1 . TYR   A 1 260 ? 15.05300  1.26800   -1.24000  1.000 10.36682 ? 304 TYR   A CE1 1 
ATOM   2003 C  CE2 . TYR   A 1 260 ? 17.32300  2.01300   -1.31200  1.000 9.59682  ? 304 TYR   A CE2 1 
ATOM   2004 C  CZ  . TYR   A 1 260 ? 16.21600  1.63200   -0.59200  1.000 10.03682 ? 304 TYR   A CZ  1 
ATOM   2005 O  OH  . TYR   A 1 260 ? 16.29900  1.61400   0.78300   1.000 9.24682  ? 304 TYR   A OH  1 
ATOM   2006 O  OXT . TYR   A 1 260 ? 13.43800  1.25700   -6.19200  1.000 17.40682 ? 304 TYR   A OXT 1 
ATOM   2007 N  N   . PRO   B 1 2   ? 10.29200  0.19400   61.54800  1.000 24.45682 ? 46  PRO   B N   1 
ATOM   2008 C  CA  . PRO   B 1 2   ? 9.50800   -0.75200  62.35300  1.000 17.39682 ? 46  PRO   B CA  1 
ATOM   2009 C  C   . PRO   B 1 2   ? 8.64300   -1.72700  61.53800  1.000 19.23682 ? 46  PRO   B C   1 
ATOM   2010 O  O   . PRO   B 1 2   ? 8.22100   -2.73500  62.09900  1.000 22.08682 ? 46  PRO   B O   1 
ATOM   2011 C  CB  . PRO   B 1 2   ? 8.60700   0.16100   63.20200  1.000 21.69682 ? 46  PRO   B CB  1 
ATOM   2012 C  CG  . PRO   B 1 2   ? 9.18300   1.54900   63.07300  1.000 22.53682 ? 46  PRO   B CG  1 
ATOM   2013 C  CD  . PRO   B 1 2   ? 9.85400   1.58700   61.73700  1.000 23.18682 ? 46  PRO   B CD  1 
ATOM   2014 N  N   . ASN   B 1 3   ? 8.36400   -1.43400  60.26900  1.000 17.57682 ? 47  ASN   B N   1 
ATOM   2015 C  CA  . ASN   B 1 3   ? 7.51500   -2.31500  59.46600  1.000 17.49682 ? 47  ASN   B CA  1 
ATOM   2016 C  C   . ASN   B 1 3   ? 8.15900   -3.69500  59.36400  1.000 14.18682 ? 47  ASN   B C   1 
ATOM   2017 O  O   . ASN   B 1 3   ? 9.23600   -3.82900  58.76300  1.000 13.96682 ? 47  ASN   B O   1 
ATOM   2018 C  CB  . ASN   B 1 3   ? 7.27100   -1.72500  58.06400  1.000 14.85682 ? 47  ASN   B CB  1 
ATOM   2019 C  CG  . ASN   B 1 3   ? 6.51000   -2.68600  57.13000  1.000 18.62682 ? 47  ASN   B CG  1 
ATOM   2020 O  OD1 . ASN   B 1 3   ? 6.01200   -3.72500  57.55400  1.000 16.77682 ? 47  ASN   B OD1 1 
ATOM   2021 N  ND2 . ASN   B 1 3   ? 6.43100   -2.33200  55.84900  1.000 14.11682 ? 47  ASN   B ND2 1 
ATOM   2022 N  N   . PRO   B 1 4   ? 7.53400   -4.74400  59.90700  1.000 14.90682 ? 48  PRO   B N   1 
ATOM   2023 C  CA  . PRO   B 1 4   ? 8.20400   -6.05200  59.95200  1.000 17.30682 ? 48  PRO   B CA  1 
ATOM   2024 C  C   . PRO   B 1 4   ? 8.31200   -6.73900  58.60200  1.000 16.55682 ? 48  PRO   B C   1 
ATOM   2025 O  O   . PRO   B 1 4   ? 9.07700   -7.70400  58.48600  1.000 16.59682 ? 48  PRO   B O   1 
ATOM   2026 C  CB  . PRO   B 1 4   ? 7.32600   -6.85500  60.91700  1.000 14.84682 ? 48  PRO   B CB  1 
ATOM   2027 C  CG  . PRO   B 1 4   ? 5.96800   -6.24800  60.76000  1.000 15.00682 ? 48  PRO   B CG  1 
ATOM   2028 C  CD  . PRO   B 1 4   ? 6.17800   -4.78900  60.48300  1.000 17.27682 ? 48  PRO   B CD  1 
ATOM   2029 N  N   . TYR   B 1 5   ? 7.59800   -6.27600  57.57600  1.000 14.22682 ? 49  TYR   B N   1 
ATOM   2030 C  CA  . TYR   B 1 5   ? 7.64000   -6.91600  56.26500  1.000 15.28682 ? 49  TYR   B CA  1 
ATOM   2031 C  C   . TYR   B 1 5   ? 8.64200   -6.27900  55.30100  1.000 14.32682 ? 49  TYR   B C   1 
ATOM   2032 O  O   . TYR   B 1 5   ? 8.74800   -6.74000  54.16100  1.000 14.24682 ? 49  TYR   B O   1 
ATOM   2033 C  CB  . TYR   B 1 5   ? 6.23700   -6.92100  55.64500  1.000 13.92682 ? 49  TYR   B CB  1 
ATOM   2034 C  CG  . TYR   B 1 5   ? 5.18500   -7.48300  56.57700  1.000 11.44682 ? 49  TYR   B CG  1 
ATOM   2035 C  CD1 . TYR   B 1 5   ? 5.39200   -8.69200  57.24200  1.000 15.22682 ? 49  TYR   B CD1 1 
ATOM   2036 C  CD2 . TYR   B 1 5   ? 4.01000   -6.79100  56.83000  1.000 16.33682 ? 49  TYR   B CD2 1 
ATOM   2037 C  CE1 . TYR   B 1 5   ? 4.43800   -9.21000  58.11700  1.000 12.33682 ? 49  TYR   B CE1 1 
ATOM   2038 C  CE2 . TYR   B 1 5   ? 3.04900   -7.30100  57.69600  1.000 13.64682 ? 49  TYR   B CE2 1 
ATOM   2039 C  CZ  . TYR   B 1 5   ? 3.27000   -8.51100  58.33200  1.000 13.76682 ? 49  TYR   B CZ  1 
ATOM   2040 O  OH  . TYR   B 1 5   ? 2.32200   -9.00800  59.19400  1.000 17.81682 ? 49  TYR   B OH  1 
ATOM   2041 N  N   . GLU   B 1 6   ? 9.39800   -5.26100  55.72500  1.000 15.90682 ? 50  GLU   B N   1 
ATOM   2042 C  CA  . GLU   B 1 6   ? 10.40400  -4.66300  54.84500  1.000 18.53682 ? 50  GLU   B CA  1 
ATOM   2043 C  C   . GLU   B 1 6   ? 11.53400  -5.64900  54.57800  1.000 16.01682 ? 50  GLU   B C   1 
ATOM   2044 O  O   . GLU   B 1 6   ? 12.07600  -6.25200  55.51000  1.000 15.20682 ? 50  GLU   B O   1 
ATOM   2045 C  CB  . GLU   B 1 6   ? 10.99000  -3.38000  55.45200  1.000 11.55682 ? 50  GLU   B CB  1 
ATOM   2046 C  CG  . GLU   B 1 6   ? 10.06400  -2.17600  55.45800  1.000 14.42682 ? 50  GLU   B CG  1 
ATOM   2047 C  CD  . GLU   B 1 6   ? 10.71100  -0.95400  56.10000  1.000 24.34682 ? 50  GLU   B CD  1 
ATOM   2048 O  OE1 . GLU   B 1 6   ? 11.91500  -1.03100  56.43100  1.000 24.04682 ? 50  GLU   B OE1 1 
ATOM   2049 O  OE2 . GLU   B 1 6   ? 10.01700  0.07700   56.27600  1.000 27.12682 ? 50  GLU   B OE2 1 
ATOM   2050 N  N   . ARG   B 1 7   ? 11.89600  -5.79800  53.29900  1.000 13.36682 ? 51  ARG   B N   1 
ATOM   2051 C  CA  . ARG   B 1 7   ? 13.01100  -6.62800  52.86000  1.000 14.50682 ? 51  ARG   B CA  1 
ATOM   2052 C  C   . ARG   B 1 7   ? 13.86800  -5.83700  51.87600  1.000 17.36682 ? 51  ARG   B C   1 
ATOM   2053 O  O   . ARG   B 1 7   ? 13.33900  -5.06600  51.07200  1.000 11.09682 ? 51  ARG   B O   1 
ATOM   2054 C  CB  . ARG   B 1 7   ? 12.51300  -7.91800  52.19100  1.000 9.51682  ? 51  ARG   B CB  1 
ATOM   2055 C  CG  . ARG   B 1 7   ? 11.43600  -8.66200  52.97300  1.000 11.29682 ? 51  ARG   B CG  1 
ATOM   2056 C  CD  . ARG   B 1 7   ? 12.01200  -9.56100  54.04300  1.000 12.63682 ? 51  ARG   B CD  1 
ATOM   2057 N  NE  . ARG   B 1 7   ? 10.97400  -10.26000 54.79800  1.000 13.50682 ? 51  ARG   B NE  1 
ATOM   2058 C  CZ  . ARG   B 1 7   ? 10.40400  -9.78300  55.89700  1.000 15.05682 ? 51  ARG   B CZ  1 
ATOM   2059 N  NH1 . ARG   B 1 7   ? 10.70600  -8.58000  56.36600  1.000 19.55682 ? 51  ARG   B NH1 1 
ATOM   2060 N  NH2 . ARG   B 1 7   ? 9.51700   -10.53300 56.54800  1.000 9.45682  ? 51  ARG   B NH2 1 
ATOM   2061 N  N   . GLY   B 1 8   ? 15.18900  -6.02500  51.93900  1.000 15.58682 ? 52  GLY   B N   1 
ATOM   2062 C  CA  . GLY   B 1 8   ? 16.09000  -5.41000  50.98700  1.000 14.51682 ? 52  GLY   B CA  1 
ATOM   2063 C  C   . GLY   B 1 8   ? 16.40100  -3.96500  51.31900  1.000 15.28682 ? 52  GLY   B C   1 
ATOM   2064 O  O   . GLY   B 1 8   ? 15.73700  -3.34200  52.15400  1.000 13.49682 ? 52  GLY   B O   1 
ATOM   2065 N  N   . PRO   B 1 9   ? 17.41800  -3.40000  50.66500  1.000 19.77682 ? 53  PRO   B N   1 
ATOM   2066 C  CA  . PRO   B 1 9   ? 17.86000  -2.04100  51.00600  1.000 15.34682 ? 53  PRO   B CA  1 
ATOM   2067 C  C   . PRO   B 1 9   ? 16.90100  -0.98800  50.47500  1.000 16.17682 ? 53  PRO   B C   1 
ATOM   2068 O  O   . PRO   B 1 9   ? 16.04200  -1.25500  49.63200  1.000 13.96682 ? 53  PRO   B O   1 
ATOM   2069 C  CB  . PRO   B 1 9   ? 19.23100  -1.93100  50.33600  1.000 21.60682 ? 53  PRO   B CB  1 
ATOM   2070 C  CG  . PRO   B 1 9   ? 19.16200  -2.88400  49.19800  1.000 21.60682 ? 53  PRO   B CG  1 
ATOM   2071 C  CD  . PRO   B 1 9   ? 18.28800  -4.02800  49.65500  1.000 17.74682 ? 53  PRO   B CD  1 
ATOM   2072 N  N   . ASP   B 1 10  ? 17.06900  0.23300   50.99400  1.000 15.11682 ? 54  ASP   B N   1 
ATOM   2073 C  CA  . ASP   B 1 10  ? 16.22200  1.34700   50.59100  1.000 18.02682 ? 54  ASP   B CA  1 
ATOM   2074 C  C   . ASP   B 1 10  ? 16.31400  1.54000   49.07800  1.000 19.36682 ? 54  ASP   B C   1 
ATOM   2075 O  O   . ASP   B 1 10  ? 17.42200  1.53100   48.52300  1.000 16.46682 ? 54  ASP   B O   1 
ATOM   2076 C  CB  . ASP   B 1 10  ? 16.62600  2.63300   51.31800  1.000 21.14682 ? 54  ASP   B CB  1 
ATOM   2077 C  CG  . ASP   B 1 10  ? 16.29800  2.60100   52.80500  1.000 21.49682 ? 54  ASP   B CG  1 
ATOM   2078 O  OD1 . ASP   B 1 10  ? 15.60900  1.66400   53.25600  1.000 24.01682 ? 54  ASP   B OD1 1 
ATOM   2079 O  OD2 . ASP   B 1 10  ? 16.73800  3.51000   53.53200  1.000 19.11682 ? 54  ASP   B OD2 1 
ATOM   2080 N  N   . PRO   B 1 11  ? 15.18900  1.70500   48.38500  1.000 15.74682 ? 55  PRO   B N   1 
ATOM   2081 C  CA  . PRO   B 1 11  ? 15.18600  1.68400   46.91900  1.000 11.52682 ? 55  PRO   B CA  1 
ATOM   2082 C  C   . PRO   B 1 11  ? 15.48800  3.03000   46.26700  1.000 15.09682 ? 55  PRO   B C   1 
ATOM   2083 O  O   . PRO   B 1 11  ? 15.35300  4.10400   46.86000  1.000 17.43682 ? 55  PRO   B O   1 
ATOM   2084 C  CB  . PRO   B 1 11  ? 13.74500  1.25800   46.59600  1.000 11.30682 ? 55  PRO   B CB  1 
ATOM   2085 C  CG  . PRO   B 1 11  ? 12.94600  1.90100   47.72600  1.000 14.71682 ? 55  PRO   B CG  1 
ATOM   2086 C  CD  . PRO   B 1 11  ? 13.82400  1.71900   48.94600  1.000 12.66682 ? 55  PRO   B CD  1 
ATOM   2087 N  N   . THR   B 1 12  ? 15.89500  2.94100   45.00400  1.000 12.93682 ? 56  THR   B N   1 
ATOM   2088 C  CA  . THR   B 1 12  ? 16.04100  4.07600   44.10500  1.000 14.23682 ? 56  THR   B CA  1 
ATOM   2089 C  C   . THR   B 1 12  ? 15.40500  3.72200   42.76700  1.000 20.09682 ? 56  THR   B C   1 
ATOM   2090 O  O   . THR   B 1 12  ? 15.07900  2.56200   42.50000  1.000 15.29682 ? 56  THR   B O   1 
ATOM   2091 C  CB  . THR   B 1 12  ? 17.51000  4.42600   43.88500  1.000 18.80682 ? 56  THR   B CB  1 
ATOM   2092 O  OG1 . THR   B 1 12  ? 18.12900  3.34400   43.17600  1.000 17.90682 ? 56  THR   B OG1 1 
ATOM   2093 C  CG2 . THR   B 1 12  ? 18.23000  4.63700   45.22100  1.000 17.92682 ? 56  THR   B CG2 1 
ATOM   2094 N  N   . GLU   B 1 13  ? 15.25500  4.72800   41.90100  1.000 18.84682 ? 57  GLU   B N   1 
ATOM   2095 C  CA  . GLU   B 1 13  ? 14.79300  4.45000   40.54100  1.000 23.86682 ? 57  GLU   B CA  1 
ATOM   2096 C  C   . GLU   B 1 13  ? 15.64900  3.38800   39.86600  1.000 24.19682 ? 57  GLU   B C   1 
ATOM   2097 O  O   . GLU   B 1 13  ? 15.12600  2.48500   39.19900  1.000 20.36682 ? 57  GLU   B O   1 
ATOM   2098 C  CB  . GLU   B 1 13  ? 14.79400  5.72900   39.71100  1.000 27.37682 ? 57  GLU   B CB  1 
ATOM   2099 C  CG  . GLU   B 1 13  ? 13.61500  6.62100   39.98400  1.000 24.47682 ? 57  GLU   B CG  1 
ATOM   2100 C  CD  . GLU   B 1 13  ? 12.93800  7.06100   38.70300  1.000 43.06682 ? 57  GLU   B CD  1 
ATOM   2101 O  OE1 . GLU   B 1 13  ? 12.25400  6.22500   38.06400  1.000 36.52682 ? 57  GLU   B OE1 1 
ATOM   2102 O  OE2 . GLU   B 1 13  ? 13.11400  8.24000   38.32100  1.000 55.65682 ? 57  GLU   B OE2 1 
ATOM   2103 N  N   . ASP   B 1 14  ? 16.96900  3.46200   40.05100  1.000 17.74682 ? 58  ASP   B N   1 
ATOM   2104 C  CA  . ASP   B 1 14  ? 17.85700  2.49500   39.41500  1.000 22.68682 ? 58  ASP   B CA  1 
ATOM   2105 C  C   . ASP   B 1 14  ? 17.61400  1.07600   39.92300  1.000 19.43682 ? 58  ASP   B C   1 
ATOM   2106 O  O   . ASP   B 1 14  ? 17.71800  0.11000   39.15500  1.000 21.73682 ? 58  ASP   B O   1 
ATOM   2107 C  CB  . ASP   B 1 14  ? 19.31300  2.89200   39.64200  1.000 25.47682 ? 58  ASP   B CB  1 
ATOM   2108 C  CG  . ASP   B 1 14  ? 19.65600  4.23200   39.01500  1.000 29.37682 ? 58  ASP   B CG  1 
ATOM   2109 O  OD1 . ASP   B 1 14  ? 18.92300  4.68000   38.09900  1.000 31.94682 ? 58  ASP   B OD1 1 
ATOM   2110 O  OD2 . ASP   B 1 14  ? 20.66900  4.83100   39.43300  1.000 30.23682 ? 58  ASP   B OD2 1 
ATOM   2111 N  N   . SER   B 1 15  ? 17.30800  0.91800   41.21400  1.000 17.82682 ? 59  SER   B N   1 
ATOM   2112 C  CA  . SER   B 1 15  ? 17.27200  -0.43600  41.75700  1.000 18.21682 ? 59  SER   B CA  1 
ATOM   2113 C  C   . SER   B 1 15  ? 16.01300  -1.17500  41.33400  1.000 14.51682 ? 59  SER   B C   1 
ATOM   2114 O  O   . SER   B 1 15  ? 16.05800  -2.39300  41.12000  1.000 17.83682 ? 59  SER   B O   1 
ATOM   2115 C  CB  . SER   B 1 15  ? 17.40700  -0.42000  43.28500  1.000 19.26682 ? 59  SER   B CB  1 
ATOM   2116 O  OG  . SER   B 1 15  ? 16.24400  0.05600   43.93500  1.000 17.00682 ? 59  SER   B OG  1 
ATOM   2117 N  N   . ILE   B 1 16  ? 14.89200  -0.46400  41.18700  1.000 13.51682 ? 60  ILE   B N   1 
ATOM   2118 C  CA  . ILE   B 1 16  ? 13.66800  -1.10800  40.71400  1.000 16.34682 ? 60  ILE   B CA  1 
ATOM   2119 C  C   . ILE   B 1 16  ? 13.69800  -1.35700  39.21700  1.000 12.36682 ? 60  ILE   B C   1 
ATOM   2120 O  O   . ILE   B 1 16  ? 12.87000  -2.12000  38.70900  1.000 11.86682 ? 60  ILE   B O   1 
ATOM   2121 C  CB  . ILE   B 1 16  ? 12.42000  -0.28400  41.08000  1.000 13.84682 ? 60  ILE   B CB  1 
ATOM   2122 C  CG1 . ILE   B 1 16  ? 12.45800  1.09500   40.42100  1.000 10.24682 ? 60  ILE   B CG1 1 
ATOM   2123 C  CG2 . ILE   B 1 16  ? 12.32200  -0.10700  42.59800  1.000 14.42682 ? 60  ILE   B CG2 1 
ATOM   2124 C  CD1 . ILE   B 1 16  ? 11.20000  1.92800   40.70300  1.000 10.98682 ? 60  ILE   B CD1 1 
ATOM   2125 N  N   . GLU   B 1 17  ? 14.64200  -0.75100  38.50000  1.000 11.88682 ? 61  GLU   B N   1 
ATOM   2126 C  CA  . GLU   B 1 17  ? 14.83700  -1.03200  37.08400  1.000 15.00682 ? 61  GLU   B CA  1 
ATOM   2127 C  C   . GLU   B 1 17  ? 15.81000  -2.17800  36.82400  1.000 16.29682 ? 61  GLU   B C   1 
ATOM   2128 O  O   . GLU   B 1 17  ? 15.80000  -2.74900  35.72500  1.000 12.70682 ? 61  GLU   B O   1 
ATOM   2129 C  CB  . GLU   B 1 17  ? 15.34800  0.22400   36.36900  1.000 13.77682 ? 61  GLU   B CB  1 
ATOM   2130 C  CG  . GLU   B 1 17  ? 14.33500  1.35300   36.31600  1.000 13.78682 ? 61  GLU   B CG  1 
ATOM   2131 C  CD  . GLU   B 1 17  ? 14.84300  2.55700   35.55700  1.000 20.10682 ? 61  GLU   B CD  1 
ATOM   2132 O  OE1 . GLU   B 1 17  ? 16.07400  2.74400   35.48200  1.000 20.84682 ? 61  GLU   B OE1 1 
ATOM   2133 O  OE2 . GLU   B 1 17  ? 14.00800  3.32500   35.03900  1.000 22.05682 ? 61  GLU   B OE2 1 
ATOM   2134 N  N   . ALA   B 1 18  ? 16.64400  -2.52000  37.80100  1.000 13.19682 ? 62  ALA   B N   1 
ATOM   2135 C  CA  . ALA   B 1 18  ? 17.67400  -3.53300  37.60500  1.000 15.29682 ? 62  ALA   B CA  1 
ATOM   2136 C  C   . ALA   B 1 18  ? 17.04500  -4.88500  37.30600  1.000 16.61682 ? 62  ALA   B C   1 
ATOM   2137 O  O   . ALA   B 1 18  ? 15.98900  -5.23100  37.83700  1.000 15.01682 ? 62  ALA   B O   1 
ATOM   2138 C  CB  . ALA   B 1 18  ? 18.56800  -3.62700  38.84300  1.000 14.10682 ? 62  ALA   B CB  1 
ATOM   2139 N  N   . ILE   B 1 19  ? 17.69800  -5.64500  36.42900  1.000 19.49682 ? 63  ILE   B N   1 
ATOM   2140 C  CA  . ILE   B 1 19  ? 17.18600  -6.95900  36.05300  1.000 19.87682 ? 63  ILE   B CA  1 
ATOM   2141 C  C   . ILE   B 1 19  ? 17.20800  -7.90600  37.24600  1.000 22.07682 ? 63  ILE   B C   1 
ATOM   2142 O  O   . ILE   B 1 19  ? 16.28100  -8.70400  37.44100  1.000 25.45682 ? 63  ILE   B O   1 
ATOM   2143 C  CB  . ILE   B 1 19  ? 17.99400  -7.50600  34.86300  1.000 23.31682 ? 63  ILE   B CB  1 
ATOM   2144 C  CG1 . ILE   B 1 19  ? 17.62200  -6.73300  33.59200  1.000 20.87682 ? 63  ILE   B CG1 1 
ATOM   2145 C  CG2 . ILE   B 1 19  ? 17.75500  -8.99300  34.68400  1.000 20.59682 ? 63  ILE   B CG2 1 
ATOM   2146 C  CD1 . ILE   B 1 19  ? 18.57200  -6.97400  32.42700  1.000 32.05682 ? 63  ILE   B CD1 1 
ATOM   2147 N  N   . ARG   B 1 20  ? 18.24900  -7.82200  38.07000  1.000 18.22682 ? 64  ARG   B N   1 
ATOM   2148 C  CA  . ARG   B 1 20  ? 18.40200  -8.66200  39.25400  1.000 19.27682 ? 64  ARG   B CA  1 
ATOM   2149 C  C   . ARG   B 1 20  ? 18.32900  -7.79200  40.50000  1.000 18.41682 ? 64  ARG   B C   1 
ATOM   2150 O  O   . ARG   B 1 20  ? 19.17600  -6.91700  40.69700  1.000 22.97682 ? 64  ARG   B O   1 
ATOM   2151 C  CB  . ARG   B 1 20  ? 19.73100  -9.41700  39.22700  1.000 25.01682 ? 64  ARG   B CB  1 
ATOM   2152 C  CG  . ARG   B 1 20  ? 19.98400  -10.25000 37.96900  1.000 34.89682 ? 64  ARG   B CG  1 
ATOM   2153 C  CD  . ARG   B 1 20  ? 21.38500  -10.87000 38.00500  1.000 38.20682 ? 64  ARG   B CD  1 
ATOM   2154 N  NE  . ARG   B 1 20  ? 21.76300  -11.45600 36.72300  1.000 40.33682 ? 64  ARG   B NE  1 
ATOM   2155 C  CZ  . ARG   B 1 20  ? 22.94700  -11.99500 36.45900  1.000 42.63682 ? 64  ARG   B CZ  1 
ATOM   2156 N  NH1 . ARG   B 1 20  ? 23.91300  -12.03100 37.36900  1.000 31.92682 ? 64  ARG   B NH1 1 
ATOM   2157 N  NH2 . ARG   B 1 20  ? 23.17100  -12.50700 35.25100  1.000 40.68682 ? 64  ARG   B NH2 1 
ATOM   2158 N  N   . GLY   B 1 21  ? 17.33300  -8.04600  41.34500  1.000 13.50682 ? 65  GLY   B N   1 
ATOM   2159 C  CA  . GLY   B 1 21  ? 17.25900  -7.41500  42.63900  1.000 11.79682 ? 65  GLY   B CA  1 
ATOM   2160 C  C   . GLY   B 1 21  ? 18.29700  -7.96900  43.60700  1.000 13.67682 ? 65  GLY   B C   1 
ATOM   2161 O  O   . GLY   B 1 21  ? 19.19400  -8.73100  43.22500  1.000 13.99682 ? 65  GLY   B O   1 
ATOM   2162 N  N   . PRO   B 1 22  ? 18.18000  -7.60200  44.88800  1.000 18.31682 ? 66  PRO   B N   1 
ATOM   2163 C  CA  . PRO   B 1 22  ? 19.21600  -7.97500  45.86800  1.000 17.96682 ? 66  PRO   B CA  1 
ATOM   2164 C  C   . PRO   B 1 22  ? 19.20400  -9.43700  46.29000  1.000 20.67682 ? 66  PRO   B C   1 
ATOM   2165 O  O   . PRO   B 1 22  ? 20.16100  -9.87000  46.94600  1.000 17.22682 ? 66  PRO   B O   1 
ATOM   2166 C  CB  . PRO   B 1 22  ? 18.91600  -7.06300  47.06300  1.000 17.37682 ? 66  PRO   B CB  1 
ATOM   2167 C  CG  . PRO   B 1 22  ? 17.48000  -6.70100  46.92600  1.000 19.75682 ? 66  PRO   B CG  1 
ATOM   2168 C  CD  . PRO   B 1 22  ? 17.19000  -6.66100  45.45100  1.000 14.22682 ? 66  PRO   B CD  1 
ATOM   2169 N  N   . PHE   B 1 23  ? 18.18400  -10.21400 45.94700  1.000 15.31682 ? 67  PHE   B N   1 
ATOM   2170 C  CA  . PHE   B 1 23  ? 18.07900  -11.59200 46.41100  1.000 17.63682 ? 67  PHE   B CA  1 
ATOM   2171 C  C   . PHE   B 1 23  ? 18.44500  -12.56100 45.29200  1.000 16.38682 ? 67  PHE   B C   1 
ATOM   2172 O  O   . PHE   B 1 23  ? 18.14100  -12.31200 44.12400  1.000 13.67682 ? 67  PHE   B O   1 
ATOM   2173 C  CB  . PHE   B 1 23  ? 16.66600  -11.88900 46.92000  1.000 10.99682 ? 67  PHE   B CB  1 
ATOM   2174 C  CG  . PHE   B 1 23  ? 16.28000  -11.08600 48.12700  1.000 13.32682 ? 67  PHE   B CG  1 
ATOM   2175 C  CD1 . PHE   B 1 23  ? 16.73100  -11.44600 49.38600  1.000 15.69682 ? 67  PHE   B CD1 1 
ATOM   2176 C  CD2 . PHE   B 1 23  ? 15.46900  -9.97100  48.00900  1.000 12.07682 ? 67  PHE   B CD2 1 
ATOM   2177 C  CE1 . PHE   B 1 23  ? 16.37300  -10.70600 50.50800  1.000 16.34682 ? 67  PHE   B CE1 1 
ATOM   2178 C  CE2 . PHE   B 1 23  ? 15.11100  -9.23900  49.12100  1.000 18.08682 ? 67  PHE   B CE2 1 
ATOM   2179 C  CZ  . PHE   B 1 23  ? 15.57500  -9.61000  50.37500  1.000 16.21682 ? 67  PHE   B CZ  1 
ATOM   2180 N  N   . SER   B 1 24  ? 19.10400  -13.66200 45.65000  1.000 15.78682 ? 68  SER   B N   1 
ATOM   2181 C  CA  . SER   B 1 24  ? 19.33100  -14.73500 44.69300  1.000 13.41682 ? 68  SER   B CA  1 
ATOM   2182 C  C   . SER   B 1 24  ? 18.12800  -15.67200 44.70600  1.000 13.43682 ? 68  SER   B C   1 
ATOM   2183 O  O   . SER   B 1 24  ? 17.38800  -15.75000 45.68700  1.000 14.33682 ? 68  SER   B O   1 
ATOM   2184 C  CB  . SER   B 1 24  ? 20.62300  -15.49500 45.00400  1.000 22.56682 ? 68  SER   B CB  1 
ATOM   2185 O  OG  . SER   B 1 24  ? 20.56200  -16.10300 46.27600  1.000 22.60682 ? 68  SER   B OG  1 
ATOM   2186 N  N   . VAL   B 1 25  ? 17.92500  -16.37400 43.59300  1.000 12.26682 ? 69  VAL   B N   1 
ATOM   2187 C  CA  . VAL   B 1 25  ? 16.64200  -16.99800 43.28900  1.000 11.85682 ? 69  VAL   B CA  1 
ATOM   2188 C  C   . VAL   B 1 25  ? 16.83000  -18.47900 42.98100  1.000 14.77682 ? 69  VAL   B C   1 
ATOM   2189 O  O   . VAL   B 1 25  ? 17.65100  -18.84600 42.13500  1.000 17.96682 ? 69  VAL   B O   1 
ATOM   2190 C  CB  . VAL   B 1 25  ? 15.94600  -16.28600 42.10800  1.000 12.26682 ? 69  VAL   B CB  1 
ATOM   2191 C  CG1 . VAL   B 1 25  ? 14.74100  -17.08600 41.60800  1.000 14.35682 ? 69  VAL   B CG1 1 
ATOM   2192 C  CG2 . VAL   B 1 25  ? 15.53300  -14.86900 42.52300  1.000 11.95682 ? 69  VAL   B CG2 1 
ATOM   2193 N  N   . ALA   B 1 26  ? 16.04300  -19.32400 43.64600  1.000 16.10682 ? 70  ALA   B N   1 
ATOM   2194 C  CA  . ALA   B 1 26  ? 15.92400  -20.72900 43.29000  1.000 19.63682 ? 70  ALA   B CA  1 
ATOM   2195 C  C   . ALA   B 1 26  ? 14.53800  -20.98900 42.70100  1.000 20.94682 ? 70  ALA   B C   1 
ATOM   2196 O  O   . ALA   B 1 26  ? 13.62800  -20.16000 42.80400  1.000 14.85682 ? 70  ALA   B O   1 
ATOM   2197 C  CB  . ALA   B 1 26  ? 16.18400  -21.62600 44.50800  1.000 12.59682 ? 70  ALA   B CB  1 
ATOM   2198 N  N   . THR   B 1 27  ? 14.37700  -22.14600 42.05900  1.000 16.12682 ? 71  THR   B N   1 
ATOM   2199 C  CA  . THR   B 1 27  ? 13.09700  -22.49500 41.45700  1.000 16.79682 ? 71  THR   B CA  1 
ATOM   2200 C  C   . THR   B 1 27  ? 12.66700  -23.90000 41.85500  1.000 21.92682 ? 71  THR   B C   1 
ATOM   2201 O  O   . THR   B 1 27  ? 13.49000  -24.74700 42.21200  1.000 20.57682 ? 71  THR   B O   1 
ATOM   2202 C  CB  . THR   B 1 27  ? 13.12600  -22.40600 39.92900  1.000 16.68682 ? 71  THR   B CB  1 
ATOM   2203 O  OG1 . THR   B 1 27  ? 14.07000  -23.34300 39.40200  1.000 23.51682 ? 71  THR   B OG1 1 
ATOM   2204 C  CG2 . THR   B 1 27  ? 13.49100  -21.00800 39.48200  1.000 17.71682 ? 71  THR   B CG2 1 
ATOM   2205 N  N   . GLU   B 1 28  ? 11.35200  -24.13100 41.77300  1.000 21.22682 ? 72  GLU   B N   1 
ATOM   2206 C  CA  . GLU   B 1 28  ? 10.73300  -25.43800 41.97300  1.000 18.82682 ? 72  GLU   B CA  1 
ATOM   2207 C  C   . GLU   B 1 28  ? 9.68900   -25.66100 40.89000  1.000 19.10682 ? 72  GLU   B C   1 
ATOM   2208 O  O   . GLU   B 1 28  ? 8.85300   -24.78500 40.64700  1.000 17.45682 ? 72  GLU   B O   1 
ATOM   2209 C  CB  . GLU   B 1 28  ? 10.06600  -25.54100 43.35500  1.000 20.42682 ? 72  GLU   B CB  1 
ATOM   2210 C  CG  . GLU   B 1 28  ? 11.03700  -25.68800 44.50500  1.000 19.63682 ? 72  GLU   B CG  1 
ATOM   2211 C  CD  . GLU   B 1 28  ? 11.59100  -27.09000 44.60700  1.000 25.59682 ? 72  GLU   B CD  1 
ATOM   2212 O  OE1 . GLU   B 1 28  ? 10.92300  -28.02600 44.11800  1.000 24.53682 ? 72  GLU   B OE1 1 
ATOM   2213 O  OE2 . GLU   B 1 28  ? 12.69300  -27.25900 45.17000  1.000 23.91682 ? 72  GLU   B OE2 1 
ATOM   2214 N  N   . ARG   B 1 29  ? 9.72700   -26.82700 40.25600  1.000 21.31682 ? 73  ARG   B N   1 
ATOM   2215 C  CA  . ARG   B 1 29  ? 8.74500   -27.19600 39.24500  1.000 20.17682 ? 73  ARG   B CA  1 
ATOM   2216 C  C   . ARG   B 1 29  ? 7.55200   -27.88300 39.91300  1.000 20.32682 ? 73  ARG   B C   1 
ATOM   2217 O  O   . ARG   B 1 29  ? 7.72700   -28.69100 40.83400  1.000 18.10682 ? 73  ARG   B O   1 
ATOM   2218 C  CB  . ARG   B 1 29  ? 9.38700   -28.11700 38.20100  1.000 22.70682 ? 73  ARG   B CB  1 
ATOM   2219 C  CG  . ARG   B 1 29  ? 8.70400   -28.13700 36.82400  1.000 31.22682 ? 73  ARG   B CG  1 
ATOM   2220 C  CD  . ARG   B 1 29  ? 9.37700   -29.14300 35.86800  1.000 36.30682 ? 73  ARG   B CD  1 
ATOM   2221 N  NE  . ARG   B 1 29  ? 8.46700   -30.19100 35.40700  1.000 40.15682 ? 73  ARG   B NE  1 
ATOM   2222 C  CZ  . ARG   B 1 29  ? 7.98200   -31.15800 36.18000  1.000 40.83682 ? 73  ARG   B CZ  1 
ATOM   2223 N  NH1 . ARG   B 1 29  ? 8.28400   -31.23200 37.46700  1.000 40.05682 ? 73  ARG   B NH1 1 
ATOM   2224 N  NH2 . ARG   B 1 29  ? 7.16500   -32.06900 35.65200  1.000 36.24682 ? 73  ARG   B NH2 1 
ATOM   2225 N  N   . VAL   B 1 30  ? 6.33700   -27.54400 39.46900  1.000 18.92682 ? 74  VAL   B N   1 
ATOM   2226 C  CA  . VAL   B 1 30  ? 5.10600   -28.15100 39.99200  1.000 15.85682 ? 74  VAL   B CA  1 
ATOM   2227 C  C   . VAL   B 1 30  ? 4.40000   -28.88000 38.85000  1.000 17.85682 ? 74  VAL   B C   1 
ATOM   2228 O  O   . VAL   B 1 30  ? 4.07700   -28.27300 37.82100  1.000 15.34682 ? 74  VAL   B O   1 
ATOM   2229 C  CB  . VAL   B 1 30  ? 4.17000   -27.11200 40.63700  1.000 16.35682 ? 74  VAL   B CB  1 
ATOM   2230 C  CG1 . VAL   B 1 30  ? 2.88000   -27.78000 41.12900  1.000 12.32682 ? 74  VAL   B CG1 1 
ATOM   2231 C  CG2 . VAL   B 1 30  ? 4.86400   -26.37500 41.78600  1.000 16.35682 ? 74  VAL   B CG2 1 
ATOM   2232 N  N   . SER   B 1 31  ? 4.13500   -30.16900 39.04500  1.000 18.00682 ? 75  SER   B N   1 
ATOM   2233 C  CA  . SER   B 1 31  ? 3.56800   -31.00200 37.99200  1.000 14.69682 ? 75  SER   B CA  1 
ATOM   2234 C  C   . SER   B 1 31  ? 2.13500   -30.59300 37.65500  1.000 19.34682 ? 75  SER   B C   1 
ATOM   2235 O  O   . SER   B 1 31  ? 1.37400   -30.13900 38.51300  1.000 12.65682 ? 75  SER   B O   1 
ATOM   2236 C  CB  . SER   B 1 31  ? 3.59600   -32.47300 38.41600  1.000 19.78682 ? 75  SER   B CB  1 
ATOM   2237 O  OG  . SER   B 1 31  ? 2.51400   -33.17800 37.84700  1.000 21.94682 ? 75  SER   B OG  1 
ATOM   2238 N  N   . SER   B 1 32  ? 1.76400   -30.77100 36.38100  1.000 15.68682 ? 76  SER   B N   1 
ATOM   2239 C  CA  . SER   B 1 32  ? 0.39400   -30.48400 35.96900  1.000 19.25682 ? 76  SER   B CA  1 
ATOM   2240 C  C   . SER   B 1 32  ? -0.62600  -31.32800 36.72700  1.000 20.36682 ? 76  SER   B C   1 
ATOM   2241 O  O   . SER   B 1 32  ? -1.81000  -30.98000 36.74100  1.000 18.59682 ? 76  SER   B O   1 
ATOM   2242 C  CB  . SER   B 1 32  ? 0.22800   -30.70000 34.46400  1.000 18.82682 ? 76  SER   B CB  1 
ATOM   2243 O  OG  . SER   B 1 32  ? 0.35700   -32.07000 34.12500  1.000 30.26682 ? 76  SER   B OG  1 
ATOM   2244 N  N   . PHE   B 1 33  ? -0.19500  -32.41700 37.36900  1.000 18.51682 ? 77  PHE   B N   1 
ATOM   2245 C  CA  . PHE   B 1 33  ? -1.11600  -33.22900 38.15800  1.000 21.54682 ? 77  PHE   B CA  1 
ATOM   2246 C  C   . PHE   B 1 33  ? -1.57000  -32.54600 39.43600  1.000 18.28682 ? 77  PHE   B C   1 
ATOM   2247 O  O   . PHE   B 1 33  ? -2.40600  -33.11400 40.14300  1.000 18.21682 ? 77  PHE   B O   1 
ATOM   2248 C  CB  . PHE   B 1 33  ? -0.48300  -34.58300 38.48800  1.000 21.73682 ? 77  PHE   B CB  1 
ATOM   2249 C  CG  . PHE   B 1 33  ? -0.38300  -35.50400 37.29900  1.000 30.16682 ? 77  PHE   B CG  1 
ATOM   2250 C  CD1 . PHE   B 1 33  ? -1.52600  -36.03300 36.72300  1.000 32.79682 ? 77  PHE   B CD1 1 
ATOM   2251 C  CD2 . PHE   B 1 33  ? 0.85300   -35.82900 36.75200  1.000 32.73682 ? 77  PHE   B CD2 1 
ATOM   2252 C  CE1 . PHE   B 1 33  ? -1.44200  -36.87700 35.62600  1.000 30.79682 ? 77  PHE   B CE1 1 
ATOM   2253 C  CE2 . PHE   B 1 33  ? 0.94400   -36.67200 35.65600  1.000 31.98682 ? 77  PHE   B CE2 1 
ATOM   2254 C  CZ  . PHE   B 1 33  ? -0.20600  -37.19400 35.09200  1.000 26.93682 ? 77  PHE   B CZ  1 
ATOM   2255 N  N   . ALA   B 1 34  ? -1.04900  -31.36000 39.75800  1.000 16.32682 ? 78  ALA   B N   1 
ATOM   2256 C  CA  . ALA   B 1 34  ? -1.54100  -30.62900 40.91500  1.000 18.00682 ? 78  ALA   B CA  1 
ATOM   2257 C  C   . ALA   B 1 34  ? -3.03300  -30.35100 40.76900  1.000 16.95682 ? 78  ALA   B C   1 
ATOM   2258 O  O   . ALA   B 1 34  ? -3.54900  -30.13600 39.66700  1.000 20.64682 ? 78  ALA   B O   1 
ATOM   2259 C  CB  . ALA   B 1 34  ? -0.77600  -29.31700 41.09800  1.000 11.57682 ? 78  ALA   B CB  1 
ATOM   2260 N  N   . SER   B 1 35  ? -3.72800  -30.34000 41.90000  1.000 18.35682 ? 79  SER   B N   1 
ATOM   2261 C  CA  . SER   B 1 35  ? -5.17700  -30.20500 41.89600  1.000 21.06682 ? 79  SER   B CA  1 
ATOM   2262 C  C   . SER   B 1 35  ? -5.58700  -28.75400 41.65800  1.000 17.38682 ? 79  SER   B C   1 
ATOM   2263 O  O   . SER   B 1 35  ? -5.05700  -27.83700 42.29300  1.000 21.00682 ? 79  SER   B O   1 
ATOM   2264 C  CB  . SER   B 1 35  ? -5.75100  -30.71500 43.21800  1.000 18.46682 ? 79  SER   B CB  1 
ATOM   2265 O  OG  . SER   B 1 35  ? -7.12700  -30.41300 43.31900  1.000 25.06682 ? 79  SER   B OG  1 
ATOM   2266 N  N   . GLY   B 1 36  ? -6.50900  -28.54500 40.71100  1.000 14.30682 ? 80  GLY   B N   1 
ATOM   2267 C  CA  . GLY   B 1 36  ? -7.17500  -27.26700 40.54700  1.000 15.79682 ? 80  GLY   B CA  1 
ATOM   2268 C  C   . GLY   B 1 36  ? -6.52500  -26.27500 39.59900  1.000 16.81682 ? 80  GLY   B C   1 
ATOM   2269 O  O   . GLY   B 1 36  ? -7.11100  -25.20900 39.36300  1.000 16.39682 ? 80  GLY   B O   1 
ATOM   2270 N  N   . PHE   B 1 37  ? -5.33500  -26.57300 39.07600  1.000 11.27682 ? 81  PHE   B N   1 
ATOM   2271 C  CA  . PHE   B 1 37  ? -4.67600  -25.77600 38.04600  1.000 13.36682 ? 81  PHE   B CA  1 
ATOM   2272 C  C   . PHE   B 1 37  ? -3.70800  -26.69100 37.29700  1.000 15.83682 ? 81  PHE   B C   1 
ATOM   2273 O  O   . PHE   B 1 37  ? -3.58300  -27.87600 37.60800  1.000 12.93682 ? 81  PHE   B O   1 
ATOM   2274 C  CB  . PHE   B 1 37  ? -3.97000  -24.55200 38.64400  1.000 12.91682 ? 81  PHE   B CB  1 
ATOM   2275 C  CG  . PHE   B 1 37  ? -2.81800  -24.89000 39.55700  1.000 14.22682 ? 81  PHE   B CG  1 
ATOM   2276 C  CD1 . PHE   B 1 37  ? -3.04500  -25.32300 40.86200  1.000 14.29682 ? 81  PHE   B CD1 1 
ATOM   2277 C  CD2 . PHE   B 1 37  ? -1.51000  -24.74400 39.12300  1.000 14.74682 ? 81  PHE   B CD2 1 
ATOM   2278 C  CE1 . PHE   B 1 37  ? -1.98300  -25.63000 41.71200  1.000 16.29682 ? 81  PHE   B CE1 1 
ATOM   2279 C  CE2 . PHE   B 1 37  ? -0.44400  -25.04900 39.96400  1.000 14.19682 ? 81  PHE   B CE2 1 
ATOM   2280 C  CZ  . PHE   B 1 37  ? -0.68200  -25.49600 41.26100  1.000 17.09682 ? 81  PHE   B CZ  1 
ATOM   2281 N  N   . GLY   B 1 38  ? -3.00700  -26.13600 36.31300  1.000 12.91682 ? 82  GLY   B N   1 
ATOM   2282 C  CA  . GLY   B 1 38  ? -2.16000  -26.97900 35.48300  1.000 12.92682 ? 82  GLY   B CA  1 
ATOM   2283 C  C   . GLY   B 1 38  ? -0.67100  -26.98900 35.77300  1.000 14.68682 ? 82  GLY   B C   1 
ATOM   2284 O  O   . GLY   B 1 38  ? 0.13400   -27.14800 34.84900  1.000 17.42682 ? 82  GLY   B O   1 
ATOM   2285 N  N   . GLY   B 1 39  ? -0.28300  -26.84800 37.03700  1.000 12.82682 ? 83  GLY   B N   1 
ATOM   2286 C  CA  . GLY   B 1 39  ? 1.12500   -26.81900 37.39000  1.000 12.41682 ? 83  GLY   B CA  1 
ATOM   2287 C  C   . GLY   B 1 39  ? 1.76700   -25.46700 37.12500  1.000 15.58682 ? 83  GLY   B C   1 
ATOM   2288 O  O   . GLY   B 1 39  ? 1.10300   -24.46900 36.83100  1.000 13.52682 ? 83  GLY   B O   1 
ATOM   2289 N  N   . GLY   B 1 40  ? 3.09000   -25.43800 37.24600  1.000 13.30682 ? 84  GLY   B N   1 
ATOM   2290 C  CA  . GLY   B 1 40  ? 3.82100   -24.21300 36.96600  1.000 15.73682 ? 84  GLY   B CA  1 
ATOM   2291 C  C   . GLY   B 1 40  ? 5.22300   -24.25300 37.55500  1.000 14.97682 ? 84  GLY   B C   1 
ATOM   2292 O  O   . GLY   B 1 40  ? 5.76600   -25.32000 37.83300  1.000 14.50682 ? 84  GLY   B O   1 
ATOM   2293 N  N   . THR   B 1 41  ? 5.78700   -23.05800 37.72300  1.000 14.42682 ? 85  THR   B N   1 
ATOM   2294 C  CA  . THR   B 1 41  ? 7.14600   -22.87700 38.21800  1.000 12.09682 ? 85  THR   B CA  1 
ATOM   2295 C  C   . THR   B 1 41  ? 7.13100   -21.87400 39.35900  1.000 10.98682 ? 85  THR   B C   1 
ATOM   2296 O  O   . THR   B 1 41  ? 6.59300   -20.77300 39.20900  1.000 12.06682 ? 85  THR   B O   1 
ATOM   2297 C  CB  . THR   B 1 41  ? 8.08800   -22.37100 37.11100  1.000 18.71682 ? 85  THR   B CB  1 
ATOM   2298 O  OG1 . THR   B 1 41  ? 7.99500   -23.21900 35.96000  1.000 15.83682 ? 85  THR   B OG1 1 
ATOM   2299 C  CG2 . THR   B 1 41  ? 9.54200   -22.32200 37.61800  1.000 11.61682 ? 85  THR   B CG2 1 
ATOM   2300 N  N   . ILE   B 1 42  ? 7.74700   -22.24200 40.47700  1.000 9.09682  ? 86  ILE   B N   1 
ATOM   2301 C  CA  . ILE   B 1 42  ? 7.87200   -21.36800 41.63600  1.000 10.62682 ? 86  ILE   B CA  1 
ATOM   2302 C  C   . ILE   B 1 42  ? 9.27500   -20.77300 41.62900  1.000 11.62682 ? 86  ILE   B C   1 
ATOM   2303 O  O   . ILE   B 1 42  ? 10.26500  -21.51200 41.58800  1.000 13.79682 ? 86  ILE   B O   1 
ATOM   2304 C  CB  . ILE   B 1 42  ? 7.61100   -22.13600 42.94300  1.000 11.90682 ? 86  ILE   B CB  1 
ATOM   2305 C  CG1 . ILE   B 1 42  ? 6.24300   -22.81700 42.90200  1.000 12.79682 ? 86  ILE   B CG1 1 
ATOM   2306 C  CG2 . ILE   B 1 42  ? 7.70300   -21.20400 44.16100  1.000 11.65682 ? 86  ILE   B CG2 1 
ATOM   2307 C  CD1 . ILE   B 1 42  ? 6.00600   -23.78400 44.06700  1.000 14.22682 ? 86  ILE   B CD1 1 
ATOM   2308 N  N   . TYR   B 1 43  ? 9.35700   -19.44500 41.66100  1.000 8.38682  ? 87  TYR   B N   1 
ATOM   2309 C  CA  . TYR   B 1 43  ? 10.60400  -18.70600 41.83600  1.000 11.29682 ? 87  TYR   B CA  1 
ATOM   2310 C  C   . TYR   B 1 43  ? 10.60300  -18.11300 43.23900  1.000 13.99682 ? 87  TYR   B C   1 
ATOM   2311 O  O   . TYR   B 1 43  ? 9.65700   -17.40900 43.61500  1.000 12.12682 ? 87  TYR   B O   1 
ATOM   2312 C  CB  . TYR   B 1 43  ? 10.74500  -17.58300 40.79400  1.000 8.95682  ? 87  TYR   B CB  1 
ATOM   2313 C  CG  . TYR   B 1 43  ? 10.68200  -18.04200 39.34500  1.000 10.27682 ? 87  TYR   B CG  1 
ATOM   2314 C  CD1 . TYR   B 1 43  ? 9.46200   -18.35700 38.74400  1.000 9.14682  ? 87  TYR   B CD1 1 
ATOM   2315 C  CD2 . TYR   B 1 43  ? 11.83500  -18.13600 38.57700  1.000 12.77682 ? 87  TYR   B CD2 1 
ATOM   2316 C  CE1 . TYR   B 1 43  ? 9.40100   -18.76600 37.41500  1.000 10.62682 ? 87  TYR   B CE1 1 
ATOM   2317 C  CE2 . TYR   B 1 43  ? 11.79000  -18.55400 37.25000  1.000 14.53682 ? 87  TYR   B CE2 1 
ATOM   2318 C  CZ  . TYR   B 1 43  ? 10.57300  -18.87000 36.67800  1.000 11.93682 ? 87  TYR   B CZ  1 
ATOM   2319 O  OH  . TYR   B 1 43  ? 10.52100  -19.27000 35.36900  1.000 14.00682 ? 87  TYR   B OH  1 
ATOM   2320 N  N   . TYR   B 1 44  ? 11.64400  -18.39500 44.01600  1.000 13.10682 ? 88  TYR   B N   1 
ATOM   2321 C  CA  . TYR   B 1 44  ? 11.66600  -17.87500 45.37300  1.000 12.14682 ? 88  TYR   B CA  1 
ATOM   2322 C  C   . TYR   B 1 44  ? 13.04900  -17.36400 45.74900  1.000 13.44682 ? 88  TYR   B C   1 
ATOM   2323 O  O   . TYR   B 1 44  ? 14.06000  -17.79700 45.17600  1.000 9.96682  ? 88  TYR   B O   1 
ATOM   2324 C  CB  . TYR   B 1 44  ? 11.20100  -18.93200 46.38900  1.000 13.42682 ? 88  TYR   B CB  1 
ATOM   2325 C  CG  . TYR   B 1 44  ? 12.05300  -20.17200 46.49100  1.000 17.19682 ? 88  TYR   B CG  1 
ATOM   2326 C  CD1 . TYR   B 1 44  ? 11.88500  -21.22900 45.60800  1.000 11.74682 ? 88  TYR   B CD1 1 
ATOM   2327 C  CD2 . TYR   B 1 44  ? 12.99700  -20.30400 47.51000  1.000 19.23682 ? 88  TYR   B CD2 1 
ATOM   2328 C  CE1 . TYR   B 1 44  ? 12.65300  -22.37700 45.71600  1.000 17.11682 ? 88  TYR   B CE1 1 
ATOM   2329 C  CE2 . TYR   B 1 44  ? 13.77000  -21.44800 47.63200  1.000 14.30682 ? 88  TYR   B CE2 1 
ATOM   2330 C  CZ  . TYR   B 1 44  ? 13.59600  -22.47600 46.73000  1.000 18.67682 ? 88  TYR   B CZ  1 
ATOM   2331 O  OH  . TYR   B 1 44  ? 14.36200  -23.61000 46.84500  1.000 20.71682 ? 88  TYR   B OH  1 
ATOM   2332 N  N   . PRO   B 1 45  ? 13.12000  -16.42500 46.69400  1.000 10.86682 ? 89  PRO   B N   1 
ATOM   2333 C  CA  . PRO   B 1 45  ? 14.42600  -15.94500 47.16700  1.000 16.42682 ? 89  PRO   B CA  1 
ATOM   2334 C  C   . PRO   B 1 45  ? 15.06500  -16.93000 48.13400  1.000 15.12682 ? 89  PRO   B C   1 
ATOM   2335 O  O   . PRO   B 1 45  ? 14.40000  -17.50100 49.00400  1.000 17.20682 ? 89  PRO   B O   1 
ATOM   2336 C  CB  . PRO   B 1 45  ? 14.09600  -14.61800 47.87300  1.000 13.32682 ? 89  PRO   B CB  1 
ATOM   2337 C  CG  . PRO   B 1 45  ? 12.63100  -14.34700 47.61900  1.000 15.46682 ? 89  PRO   B CG  1 
ATOM   2338 C  CD  . PRO   B 1 45  ? 12.00400  -15.67600 47.29100  1.000 15.44682 ? 89  PRO   B CD  1 
ATOM   2339 N  N   . ARG   B 1 46  ? 16.38300  -17.10700 47.99200  1.000 17.44682 ? 90  ARG   B N   1 
ATOM   2340 C  CA  . ARG   B 1 46  ? 17.10300  -18.09600 48.79100  1.000 18.75682 ? 90  ARG   B CA  1 
ATOM   2341 C  C   . ARG   B 1 46  ? 17.39300  -17.61100 50.20800  1.000 21.78682 ? 90  ARG   B C   1 
ATOM   2342 O  O   . ARG   B 1 46  ? 17.37700  -18.41700 51.14500  1.000 21.91682 ? 90  ARG   B O   1 
ATOM   2343 C  CB  . ARG   B 1 46  ? 18.40700  -18.49100 48.08100  1.000 18.13682 ? 90  ARG   B CB  1 
ATOM   2344 C  CG  . ARG   B 1 46  ? 18.17500  -19.21700 46.75700  1.000 17.41682 ? 90  ARG   B CG  1 
ATOM   2345 C  CD  . ARG   B 1 46  ? 19.45300  -19.46100 45.95300  1.000 21.21682 ? 90  ARG   B CD  1 
ATOM   2346 N  NE  . ARG   B 1 46  ? 20.36700  -20.41000 46.57800  1.000 39.76682 ? 90  ARG   B NE  1 
ATOM   2347 C  CZ  . ARG   B 1 46  ? 21.51100  -20.07800 47.16600  1.000 47.64682 ? 90  ARG   B CZ  1 
ATOM   2348 N  NH1 . ARG   B 1 46  ? 21.92800  -18.82200 47.21000  1.000 41.25682 ? 90  ARG   B NH1 1 
ATOM   2349 N  NH2 . ARG   B 1 46  ? 22.25800  -21.02800 47.72300  1.000 39.34682 ? 90  ARG   B NH2 1 
ATOM   2350 N  N   . GLU   B 1 47  ? 17.63500  -16.31400 50.39000  1.000 23.56682 ? 91  GLU   B N   1 
ATOM   2351 C  CA  . GLU   B 1 47  ? 18.06400  -15.79900 51.68400  1.000 21.37682 ? 91  GLU   B CA  1 
ATOM   2352 C  C   . GLU   B 1 47  ? 16.90700  -15.76700 52.67900  1.000 24.72682 ? 91  GLU   B C   1 
ATOM   2353 O  O   . GLU   B 1 47  ? 15.81600  -15.27700 52.36800  1.000 26.12682 ? 91  GLU   B O   1 
ATOM   2354 C  CB  . GLU   B 1 47  ? 18.66400  -14.39600 51.52700  1.000 21.84682 ? 91  GLU   B CB  1 
ATOM   2355 C  CG  . GLU   B 1 47  ? 20.01100  -14.33900 50.79000  1.000 24.50682 ? 91  GLU   B CG  1 
ATOM   2356 C  CD  . GLU   B 1 47  ? 19.87900  -14.40800 49.27700  1.000 20.73682 ? 91  GLU   B CD  1 
ATOM   2357 O  OE1 . GLU   B 1 47  ? 18.75400  -14.25100 48.75300  1.000 20.93682 ? 91  GLU   B OE1 1 
ATOM   2358 O  OE2 . GLU   B 1 47  ? 20.90600  -14.62100 48.60200  1.000 23.05682 ? 91  GLU   B OE2 1 
ATOM   2359 N  N   . THR   B 1 48  ? 17.16700  -16.25400 53.89600  1.000 20.70682 ? 92  THR   B N   1 
ATOM   2360 C  CA  . THR   B 1 48  ? 16.17900  -16.31600 54.96700  1.000 19.15682 ? 92  THR   B CA  1 
ATOM   2361 C  C   . THR   B 1 48  ? 16.45900  -15.35000 56.11300  1.000 19.79682 ? 92  THR   B C   1 
ATOM   2362 O  O   . THR   B 1 48  ? 15.63200  -15.24500 57.02800  1.000 20.19682 ? 92  THR   B O   1 
ATOM   2363 C  CB  . THR   B 1 48  ? 16.09600  -17.74500 55.52200  1.000 27.24682 ? 92  THR   B CB  1 
ATOM   2364 O  OG1 . THR   B 1 48  ? 17.39300  -18.16000 55.97200  1.000 24.49682 ? 92  THR   B OG1 1 
ATOM   2365 C  CG2 . THR   B 1 48  ? 15.62400  -18.71200 54.44500  1.000 20.86682 ? 92  THR   B CG2 1 
ATOM   2366 N  N   . ASP   B 1 49  ? 17.57800  -14.62200 56.07900  1.000 21.60682 ? 93  ASP   B N   1 
ATOM   2367 C  CA  . ASP   B 1 49  ? 18.01400  -13.83600 57.23400  1.000 22.48682 ? 93  ASP   B CA  1 
ATOM   2368 C  C   . ASP   B 1 49  ? 17.16900  -12.59300 57.49500  1.000 20.94682 ? 93  ASP   B C   1 
ATOM   2369 O  O   . ASP   B 1 49  ? 17.38800  -11.92600 58.51100  1.000 27.35682 ? 93  ASP   B O   1 
ATOM   2370 C  CB  . ASP   B 1 49  ? 19.48900  -13.42200 57.08400  1.000 27.56682 ? 93  ASP   B CB  1 
ATOM   2371 C  CG  . ASP   B 1 49  ? 19.80000  -12.80000 55.72700  1.000 30.00682 ? 93  ASP   B CG  1 
ATOM   2372 O  OD1 . ASP   B 1 49  ? 19.04100  -11.92400 55.28000  1.000 36.03682 ? 93  ASP   B OD1 1 
ATOM   2373 O  OD2 . ASP   B 1 49  ? 20.81600  -13.17400 55.10700  1.000 40.31682 ? 93  ASP   B OD2 1 
ATOM   2374 N  N   . GLU   B 1 50  ? 16.22200  -12.25400 56.62200  1.000 19.58682 ? 94  GLU   B N   1 
ATOM   2375 C  CA  . GLU   B 1 50  ? 15.39600  -11.07400 56.82200  1.000 20.82682 ? 94  GLU   B CA  1 
ATOM   2376 C  C   . GLU   B 1 50  ? 13.94000  -11.40800 57.09900  1.000 20.07682 ? 94  GLU   B C   1 
ATOM   2377 O  O   . GLU   B 1 50  ? 13.15800  -10.49400 57.36800  1.000 22.09682 ? 94  GLU   B O   1 
ATOM   2378 C  CB  . GLU   B 1 50  ? 15.48600  -10.14400 55.60100  1.000 23.37682 ? 94  GLU   B CB  1 
ATOM   2379 C  CG  . GLU   B 1 50  ? 16.91300  -9.76300  55.21500  1.000 22.89682 ? 94  GLU   B CG  1 
ATOM   2380 C  CD  . GLU   B 1 50  ? 16.98000  -8.64600  54.18100  1.000 29.19682 ? 94  GLU   B CD  1 
ATOM   2381 O  OE1 . GLU   B 1 50  ? 15.99000  -7.89600  54.04200  1.000 23.04682 ? 94  GLU   B OE1 1 
ATOM   2382 O  OE2 . GLU   B 1 50  ? 18.02600  -8.51300  53.50700  1.000 27.58682 ? 94  GLU   B OE2 1 
ATOM   2383 N  N   . GLY   B 1 51  ? 13.55400  -12.67500 57.03400  1.000 17.60682 ? 95  GLY   B N   1 
ATOM   2384 C  CA  . GLY   B 1 51  ? 12.19000  -13.08400 57.29900  1.000 20.25682 ? 95  GLY   B CA  1 
ATOM   2385 C  C   . GLY   B 1 51  ? 11.51200  -13.66500 56.07000  1.000 15.79682 ? 95  GLY   B C   1 
ATOM   2386 O  O   . GLY   B 1 51  ? 12.08600  -13.75100 54.98600  1.000 19.11682 ? 95  GLY   B O   1 
ATOM   2387 N  N   . THR   B 1 52  ? 10.25800  -14.07700 56.27000  1.000 12.12682 ? 96  THR   B N   1 
ATOM   2388 C  CA  . THR   B 1 52  ? 9.46300   -14.67000 55.21000  1.000 15.20682 ? 96  THR   B CA  1 
ATOM   2389 C  C   . THR   B 1 52  ? 8.96500   -13.59700 54.24900  1.000 13.75682 ? 96  THR   B C   1 
ATOM   2390 O  O   . THR   B 1 52  ? 8.97300   -12.40000 54.55500  1.000 12.12682 ? 96  THR   B O   1 
ATOM   2391 C  CB  . THR   B 1 52  ? 8.27500   -15.44300 55.78800  1.000 12.30682 ? 96  THR   B CB  1 
ATOM   2392 O  OG1 . THR   B 1 52  ? 7.59800   -14.62600 56.75400  1.000 15.94682 ? 96  THR   B OG1 1 
ATOM   2393 C  CG2 . THR   B 1 52  ? 8.75100   -16.72600 56.46400  1.000 19.02682 ? 96  THR   B CG2 1 
ATOM   2394 N  N   . PHE   B 1 53  ? 8.50200   -14.05800 53.08100  1.000 11.25682 ? 97  PHE   B N   1 
ATOM   2395 C  CA  . PHE   B 1 53  ? 8.12500   -13.22300 51.95200  1.000 13.17682 ? 97  PHE   B CA  1 
ATOM   2396 C  C   . PHE   B 1 53  ? 6.66600   -13.45400 51.57000  1.000 12.89682 ? 97  PHE   B C   1 
ATOM   2397 O  O   . PHE   B 1 53  ? 6.11200   -14.53400 51.80100  1.000 9.67682  ? 97  PHE   B O   1 
ATOM   2398 C  CB  . PHE   B 1 53  ? 8.99200   -13.53000 50.72500  1.000 13.02682 ? 97  PHE   B CB  1 
ATOM   2399 C  CG  . PHE   B 1 53  ? 10.45800  -13.25700 50.91400  1.000 11.94682 ? 97  PHE   B CG  1 
ATOM   2400 C  CD1 . PHE   B 1 53  ? 10.97100  -11.98300 50.71800  1.000 13.92682 ? 97  PHE   B CD1 1 
ATOM   2401 C  CD2 . PHE   B 1 53  ? 11.33000  -14.27900 51.23500  1.000 17.28682 ? 97  PHE   B CD2 1 
ATOM   2402 C  CE1 . PHE   B 1 53  ? 12.32600  -11.72800 50.87200  1.000 17.95682 ? 97  PHE   B CE1 1 
ATOM   2403 C  CE2 . PHE   B 1 53  ? 12.68200  -14.03200 51.38700  1.000 18.95682 ? 97  PHE   B CE2 1 
ATOM   2404 C  CZ  . PHE   B 1 53  ? 13.17900  -12.75600 51.20600  1.000 14.66682 ? 97  PHE   B CZ  1 
ATOM   2405 N  N   . GLY   B 1 54  ? 6.05300   -12.43100 50.97400  1.000 7.43682  ? 98  GLY   B N   1 
ATOM   2406 C  CA  . GLY   B 1 54  ? 4.77400   -12.59500 50.32100  1.000 13.26682 ? 98  GLY   B CA  1 
ATOM   2407 C  C   . GLY   B 1 54  ? 4.93600   -13.31800 48.99200  1.000 12.11682 ? 98  GLY   B C   1 
ATOM   2408 O  O   . GLY   B 1 54  ? 6.03900   -13.62700 48.54000  1.000 12.06682 ? 98  GLY   B O   1 
ATOM   2409 N  N   . ALA   B 1 55  ? 3.80200   -13.59600 48.35100  1.000 11.33682 ? 99  ALA   B N   1 
ATOM   2410 C  CA  . ALA   B 1 55  ? 3.80300   -14.38100 47.12400  1.000 12.12682 ? 99  ALA   B CA  1 
ATOM   2411 C  C   . ALA   B 1 55  ? 2.80300   -13.79600 46.13800  1.000 10.32682 ? 99  ALA   B C   1 
ATOM   2412 O  O   . ALA   B 1 55  ? 1.83500   -13.14300 46.53200  1.000 11.42682 ? 99  ALA   B O   1 
ATOM   2413 C  CB  . ALA   B 1 55  ? 3.45500   -15.85300 47.39500  1.000 8.32682  ? 99  ALA   B CB  1 
ATOM   2414 N  N   . VAL   B 1 56  ? 3.04400   -14.03600 44.85100  1.000 9.98682  ? 100 VAL   B N   1 
ATOM   2415 C  CA  . VAL   B 1 56  ? 2.13400   -13.61500 43.78800  1.000 12.83682 ? 100 VAL   B CA  1 
ATOM   2416 C  C   . VAL   B 1 56  ? 2.01200   -14.75800 42.78800  1.000 10.56682 ? 100 VAL   B C   1 
ATOM   2417 O  O   . VAL   B 1 56  ? 3.02200   -15.32300 42.35900  1.000 12.75682 ? 100 VAL   B O   1 
ATOM   2418 C  CB  . VAL   B 1 56  ? 2.59600   -12.30900 43.09400  1.000 11.59682 ? 100 VAL   B CB  1 
ATOM   2419 C  CG1 . VAL   B 1 56  ? 4.03500   -12.41200 42.60500  1.000 9.16682  ? 100 VAL   B CG1 1 
ATOM   2420 C  CG2 . VAL   B 1 56  ? 1.66100   -11.94200 41.91800  1.000 6.39682  ? 100 VAL   B CG2 1 
ATOM   2421 N  N   . ALA   B 1 57  ? 0.77400   -15.12900 42.45200  1.000 9.57682  ? 101 ALA   B N   1 
ATOM   2422 C  CA  . ALA   B 1 57  ? 0.50200   -16.09600 41.39800  1.000 8.50682  ? 101 ALA   B CA  1 
ATOM   2423 C  C   . ALA   B 1 57  ? 0.22400   -15.34800 40.09500  1.000 10.65682 ? 101 ALA   B C   1 
ATOM   2424 O  O   . ALA   B 1 57  ? -0.40200  -14.28800 40.11400  1.000 10.81682 ? 101 ALA   B O   1 
ATOM   2425 C  CB  . ALA   B 1 57  ? -0.69000  -16.97800 41.78300  1.000 10.63682 ? 101 ALA   B CB  1 
ATOM   2426 N  N   . VAL   B 1 58  ? 0.69100   -15.90100 38.96900  1.000 8.80682  ? 102 VAL   B N   1 
ATOM   2427 C  CA  . VAL   B 1 58  ? 0.74600   -15.18900 37.68600  1.000 8.22682  ? 102 VAL   B CA  1 
ATOM   2428 C  C   . VAL   B 1 58  ? 0.11300   -16.04900 36.59900  1.000 8.38682  ? 102 VAL   B C   1 
ATOM   2429 O  O   . VAL   B 1 58  ? 0.63800   -17.12600 36.27300  1.000 8.96682  ? 102 VAL   B O   1 
ATOM   2430 C  CB  . VAL   B 1 58  ? 2.18700   -14.83800 37.27200  1.000 7.92682  ? 102 VAL   B CB  1 
ATOM   2431 C  CG1 . VAL   B 1 58  ? 2.17400   -14.00200 35.99800  1.000 10.68682 ? 102 VAL   B CG1 1 
ATOM   2432 C  CG2 . VAL   B 1 58  ? 2.92200   -14.12800 38.38400  1.000 5.99682  ? 102 VAL   B CG2 1 
ATOM   2433 N  N   . ALA   B 1 59  ? -0.97300  -15.53900 35.97600  1.000 7.59682  ? 103 ALA   B N   1 
ATOM   2434 C  CA  . ALA   B 1 59  ? -1.66600  -16.36300 34.98100  1.000 9.46682  ? 103 ALA   B CA  1 
ATOM   2435 C  C   . ALA   B 1 59  ? -1.40900  -15.88200 33.54700  1.000 8.64682  ? 103 ALA   B C   1 
ATOM   2436 O  O   . ALA   B 1 59  ? -1.27700  -14.67700 33.29300  1.000 7.78682  ? 103 ALA   B O   1 
ATOM   2437 C  CB  . ALA   B 1 59  ? -3.17500  -16.37800 35.24100  1.000 6.46682  ? 103 ALA   B CB  1 
ATOM   2438 N  N   . PRO   B 1 60  ? -1.37000  -16.81200 32.57800  1.000 10.87682 ? 104 PRO   B N   1 
ATOM   2439 C  CA  . PRO   B 1 60  ? -1.22900  -16.41400 31.17000  1.000 8.81682  ? 104 PRO   B CA  1 
ATOM   2440 C  C   . PRO   B 1 60  ? -2.56400  -16.09300 30.51600  1.000 11.67682 ? 104 PRO   B C   1 
ATOM   2441 O  O   . PRO   B 1 60  ? -3.60500  -16.13500 31.17800  1.000 11.02682 ? 104 PRO   B O   1 
ATOM   2442 C  CB  . PRO   B 1 60  ? -0.58700  -17.65100 30.53600  1.000 10.18682 ? 104 PRO   B CB  1 
ATOM   2443 C  CG  . PRO   B 1 60  ? -1.24900  -18.78900 31.28300  1.000 15.44682 ? 104 PRO   B CG  1 
ATOM   2444 C  CD  . PRO   B 1 60  ? -1.36700  -18.28100 32.73200  1.000 13.10682 ? 104 PRO   B CD  1 
ATOM   2445 N  N   . GLY   B 1 61  ? -2.54800  -15.78500 29.21300  1.000 10.01682 ? 105 GLY   B N   1 
ATOM   2446 C  CA  . GLY   B 1 61  ? -3.75300  -15.48800 28.47100  1.000 10.45682 ? 105 GLY   B CA  1 
ATOM   2447 C  C   . GLY   B 1 61  ? -4.25900  -16.67600 27.65500  1.000 11.56682 ? 105 GLY   B C   1 
ATOM   2448 O  O   . GLY   B 1 61  ? -3.68100  -17.76100 27.63900  1.000 12.54682 ? 105 GLY   B O   1 
ATOM   2449 N  N   . PHE   B 1 62  ? -5.37500  -16.43000 26.96700  1.000 13.32682 ? 106 PHE   B N   1 
ATOM   2450 C  CA  . PHE   B 1 62  ? -6.03500  -17.41600 26.11100  1.000 13.50682 ? 106 PHE   B CA  1 
ATOM   2451 C  C   . PHE   B 1 62  ? -5.05900  -17.99100 25.09400  1.000 15.38682 ? 106 PHE   B C   1 
ATOM   2452 O  O   . PHE   B 1 62  ? -4.30800  -17.25100 24.45300  1.000 12.63682 ? 106 PHE   B O   1 
ATOM   2453 C  CB  . PHE   B 1 62  ? -7.20700  -16.73300 25.39700  1.000 18.08682 ? 106 PHE   B CB  1 
ATOM   2454 C  CG  . PHE   B 1 62  ? -8.20600  -17.66800 24.76400  1.000 16.33682 ? 106 PHE   B CG  1 
ATOM   2455 C  CD1 . PHE   B 1 62  ? -9.00100  -18.48600 25.53900  1.000 12.92682 ? 106 PHE   B CD1 1 
ATOM   2456 C  CD2 . PHE   B 1 62  ? -8.40400  -17.66000 23.39100  1.000 20.79682 ? 106 PHE   B CD2 1 
ATOM   2457 C  CE1 . PHE   B 1 62  ? -9.95200  -19.30800 24.96000  1.000 16.09682 ? 106 PHE   B CE1 1 
ATOM   2458 C  CE2 . PHE   B 1 62  ? -9.35300  -18.47900 22.79700  1.000 20.22682 ? 106 PHE   B CE2 1 
ATOM   2459 C  CZ  . PHE   B 1 62  ? -10.12700 -19.30700 23.58300  1.000 21.18682 ? 106 PHE   B CZ  1 
ATOM   2460 N  N   . THR   B 1 63  ? -5.08500  -19.32100 24.95300  1.000 14.97682 ? 107 THR   B N   1 
ATOM   2461 C  CA  . THR   B 1 63  ? -4.21400  -20.16300 24.12800  1.000 15.92682 ? 107 THR   B CA  1 
ATOM   2462 C  C   . THR   B 1 63  ? -2.77300  -20.21600 24.63100  1.000 18.68682 ? 107 THR   B C   1 
ATOM   2463 O  O   . THR   B 1 63  ? -1.96100  -20.93900 24.03900  1.000 19.65682 ? 107 THR   B O   1 
ATOM   2464 C  CB  . THR   B 1 63  ? -4.17000  -19.75300 22.64000  1.000 18.24682 ? 107 THR   B CB  1 
ATOM   2465 O  OG1 . THR   B 1 63  ? -3.42700  -18.53600 22.48400  1.000 17.26682 ? 107 THR   B OG1 1 
ATOM   2466 C  CG2 . THR   B 1 63  ? -5.56800  -19.57200 22.05100  1.000 16.06682 ? 107 THR   B CG2 1 
ATOM   2467 N  N   . ALA   B 1 64  ? -2.41900  -19.49500 25.69000  1.000 14.12682 ? 108 ALA   B N   1 
ATOM   2468 C  CA  . ALA   B 1 64  ? -1.01600  -19.34400 26.05400  1.000 14.16682 ? 108 ALA   B CA  1 
ATOM   2469 C  C   . ALA   B 1 64  ? -0.64400  -20.19900 27.26300  1.000 16.65682 ? 108 ALA   B C   1 
ATOM   2470 O  O   . ALA   B 1 64  ? -1.49100  -20.71600 27.99000  1.000 15.87682 ? 108 ALA   B O   1 
ATOM   2471 C  CB  . ALA   B 1 64  ? -0.68700  -17.87200 26.32300  1.000 14.72682 ? 108 ALA   B CB  1 
ATOM   2472 N  N   . SER   B 1 65  ? 0.65800   -20.32900 27.48100  1.000 19.31682 ? 109 SER   B N   1 
ATOM   2473 C  CA  . SER   B 1 65  ? 1.19300   -21.11300 28.58400  1.000 21.56682 ? 109 SER   B CA  1 
ATOM   2474 C  C   . SER   B 1 65  ? 2.12600   -20.24100 29.42200  1.000 18.97682 ? 109 SER   B C   1 
ATOM   2475 O  O   . SER   B 1 65  ? 2.39700   -19.08300 29.08600  1.000 14.76682 ? 109 SER   B O   1 
ATOM   2476 C  CB  . SER   B 1 65  ? 1.91400   -22.36100 28.06000  1.000 27.50682 ? 109 SER   B CB  1 
ATOM   2477 O  OG  . SER   B 1 65  ? 3.02100   -21.99800 27.26000  1.000 27.19682 ? 109 SER   B OG  1 
ATOM   2478 N  N   . GLN   B 1 66  ? 2.62900   -20.81600 30.52300  1.000 15.66682 ? 110 GLN   B N   1 
ATOM   2479 C  CA  . GLN   B 1 66  ? 3.48900   -20.08500 31.44800  1.000 14.72682 ? 110 GLN   B CA  1 
ATOM   2480 C  C   . GLN   B 1 66  ? 4.75200   -19.55200 30.78400  1.000 15.12682 ? 110 GLN   B C   1 
ATOM   2481 O  O   . GLN   B 1 66  ? 5.38000   -18.63800 31.33100  1.000 19.14682 ? 110 GLN   B O   1 
ATOM   2482 C  CB  . GLN   B 1 66  ? 3.88800   -20.97400 32.63700  1.000 15.92682 ? 110 GLN   B CB  1 
ATOM   2483 C  CG  . GLN   B 1 66  ? 4.88900   -22.07500 32.29100  1.000 22.75682 ? 110 GLN   B CG  1 
ATOM   2484 C  CD  . GLN   B 1 66  ? 5.43400   -22.81400 33.51200  1.000 20.81682 ? 110 GLN   B CD  1 
ATOM   2485 O  OE1 . GLN   B 1 66  ? 5.89400   -22.20300 34.48600  1.000 17.90682 ? 110 GLN   B OE1 1 
ATOM   2486 N  NE2 . GLN   B 1 66  ? 5.39600   -24.13900 33.45600  1.000 25.38682 ? 110 GLN   B NE2 1 
ATOM   2487 N  N   . GLY   B 1 67  ? 5.15600   -20.11300 29.63900  1.000 14.94682 ? 111 GLY   B N   1 
ATOM   2488 C  CA  . GLY   B 1 67  ? 6.32300   -19.59500 28.94100  1.000 15.12682 ? 111 GLY   B CA  1 
ATOM   2489 C  C   . GLY   B 1 67  ? 6.15200   -18.16000 28.47000  1.000 20.94682 ? 111 GLY   B C   1 
ATOM   2490 O  O   . GLY   B 1 67  ? 7.13500   -17.41400 28.36900  1.000 12.42682 ? 111 GLY   B O   1 
ATOM   2491 N  N   . SER   B 1 68  ? 4.91000   -17.75300 28.17400  1.000 14.44682 ? 112 SER   B N   1 
ATOM   2492 C  CA  . SER   B 1 68  ? 4.63300   -16.36300 27.81000  1.000 14.51682 ? 112 SER   B CA  1 
ATOM   2493 C  C   . SER   B 1 68  ? 4.85200   -15.40200 28.97100  1.000 11.61682 ? 112 SER   B C   1 
ATOM   2494 O  O   . SER   B 1 68  ? 4.95000   -14.18800 28.74400  1.000 9.77682  ? 112 SER   B O   1 
ATOM   2495 C  CB  . SER   B 1 68  ? 3.19600   -16.21000 27.30400  1.000 9.66682  ? 112 SER   B CB  1 
ATOM   2496 O  OG  . SER   B 1 68  ? 2.24700   -16.43100 28.33800  1.000 11.12682 ? 112 SER   B OG  1 
ATOM   2497 N  N   . MET   B 1 69  ? 4.90800   -15.91400 30.20500  1.000 12.34682 ? 113 MET   B N   1 
ATOM   2498 C  CA  . MET   B 1 69  ? 5.09800   -15.09600 31.40000  1.000 12.62682 ? 113 MET   B CA  1 
ATOM   2499 C  C   . MET   B 1 69  ? 6.40300   -15.38200 32.13800  1.000 13.80682 ? 113 MET   B C   1 
ATOM   2500 O  O   . MET   B 1 69  ? 6.59700   -14.85100 33.24000  1.000 10.46682 ? 113 MET   B O   1 
ATOM   2501 C  CB  . MET   B 1 69  ? 3.93600   -15.30400 32.37800  1.000 15.53682 ? 113 MET   B CB  1 
ATOM   2502 C  CG  . MET   B 1 69  ? 2.55500   -15.13100 31.76300  1.000 10.66682 ? 113 MET   B CG  1 
ATOM   2503 S  SD  . MET   B 1 69  ? 2.32500   -13.45900 31.14500  1.000 12.06682 ? 113 MET   B SD  1 
ATOM   2504 C  CE  . MET   B 1 69  ? 1.91800   -12.53200 32.62300  1.000 11.30682 ? 113 MET   B CE  1 
ATOM   2505 N  N   . SER   B 1 70  ? 7.29600   -16.21000 31.58300  1.000 11.08682 ? 114 SER   B N   1 
ATOM   2506 C  CA  . SER   B 1 70  ? 8.41500   -16.71600 32.38200  1.000 10.71682 ? 114 SER   B CA  1 
ATOM   2507 C  C   . SER   B 1 70  ? 9.36800   -15.60900 32.83700  1.000 10.91682 ? 114 SER   B C   1 
ATOM   2508 O  O   . SER   B 1 70  ? 9.99200   -15.73400 33.89700  1.000 11.76682 ? 114 SER   B O   1 
ATOM   2509 C  CB  . SER   B 1 70  ? 9.18400   -17.79000 31.60400  1.000 11.04682 ? 114 SER   B CB  1 
ATOM   2510 O  OG  . SER   B 1 70  ? 9.84900   -17.22200 30.49200  1.000 16.73682 ? 114 SER   B OG  1 
ATOM   2511 N  N   . TRP   B 1 71  ? 9.48400   -14.51500 32.07800  1.000 9.46682  ? 115 TRP   B N   1 
ATOM   2512 C  CA  . TRP   B 1 71  ? 10.47000  -13.49500 32.42900  1.000 11.00682 ? 115 TRP   B CA  1 
ATOM   2513 C  C   . TRP   B 1 71  ? 10.15400  -12.80600 33.75100  1.000 14.29682 ? 115 TRP   B C   1 
ATOM   2514 O  O   . TRP   B 1 71  ? 11.07200  -12.26200 34.37200  1.000 10.69682 ? 115 TRP   B O   1 
ATOM   2515 C  CB  . TRP   B 1 71  ? 10.62100  -12.45400 31.30500  1.000 12.19682 ? 115 TRP   B CB  1 
ATOM   2516 C  CG  . TRP   B 1 71  ? 9.49300   -11.43500 31.12000  1.000 10.46682 ? 115 TRP   B CG  1 
ATOM   2517 C  CD1 . TRP   B 1 71  ? 8.38200   -11.57800 30.34200  1.000 12.23682 ? 115 TRP   B CD1 1 
ATOM   2518 C  CD2 . TRP   B 1 71  ? 9.41600   -10.11000 31.68500  1.000 9.40682  ? 115 TRP   B CD2 1 
ATOM   2519 N  NE1 . TRP   B 1 71  ? 7.60900   -10.44100 30.39800  1.000 10.52682 ? 115 TRP   B NE1 1 
ATOM   2520 C  CE2 . TRP   B 1 71  ? 8.21600   -9.52800  31.22000  1.000 12.10682 ? 115 TRP   B CE2 1 
ATOM   2521 C  CE3 . TRP   B 1 71  ? 10.23400  -9.37100  32.55200  1.000 12.25682 ? 115 TRP   B CE3 1 
ATOM   2522 C  CZ2 . TRP   B 1 71  ? 7.81600   -8.23700  31.58200  1.000 8.53682  ? 115 TRP   B CZ2 1 
ATOM   2523 C  CZ3 . TRP   B 1 71  ? 9.83700   -8.08800  32.91400  1.000 10.25682 ? 115 TRP   B CZ3 1 
ATOM   2524 C  CH2 . TRP   B 1 71  ? 8.63500   -7.53300  32.42800  1.000 8.54682  ? 115 TRP   B CH2 1 
ATOM   2525 N  N   . TYR   B 1 72  ? 8.88500   -12.81900 34.19200  1.000 8.85682  ? 116 TYR   B N   1 
ATOM   2526 C  CA  . TYR   B 1 72  ? 8.53600   -12.22500 35.48100  1.000 11.68682 ? 116 TYR   B CA  1 
ATOM   2527 C  C   . TYR   B 1 72  ? 9.14400   -12.99400 36.65300  1.000 12.66682 ? 116 TYR   B C   1 
ATOM   2528 O  O   . TYR   B 1 72  ? 9.40400   -12.40300 37.70700  1.000 12.07682 ? 116 TYR   B O   1 
ATOM   2529 C  CB  . TYR   B 1 72  ? 7.00700   -12.15400 35.64800  1.000 11.29682 ? 116 TYR   B CB  1 
ATOM   2530 C  CG  . TYR   B 1 72  ? 6.31200   -11.21100 34.67900  1.000 10.23682 ? 116 TYR   B CG  1 
ATOM   2531 C  CD1 . TYR   B 1 72  ? 6.20900   -9.85600  34.95100  1.000 10.16682 ? 116 TYR   B CD1 1 
ATOM   2532 C  CD2 . TYR   B 1 72  ? 5.75100   -11.68800 33.49400  1.000 11.04682 ? 116 TYR   B CD2 1 
ATOM   2533 C  CE1 . TYR   B 1 72  ? 5.59000   -8.99800  34.07000  1.000 12.06682 ? 116 TYR   B CE1 1 
ATOM   2534 C  CE2 . TYR   B 1 72  ? 5.12600   -10.83500 32.60100  1.000 12.14682 ? 116 TYR   B CE2 1 
ATOM   2535 C  CZ  . TYR   B 1 72  ? 5.04300   -9.49100  32.89500  1.000 13.69682 ? 116 TYR   B CZ  1 
ATOM   2536 O  OH  . TYR   B 1 72  ? 4.42800   -8.63900  32.00900  1.000 8.85682  ? 116 TYR   B OH  1 
ATOM   2537 N  N   . GLY   B 1 73  ? 9.37500   -14.29800 36.49700  1.000 11.05682 ? 117 GLY   B N   1 
ATOM   2538 C  CA  . GLY   B 1 73  ? 9.79800   -15.13200 37.60800  1.000 9.75682  ? 117 GLY   B CA  1 
ATOM   2539 C  C   . GLY   B 1 73  ? 11.06400  -14.67800 38.30000  1.000 10.27682 ? 117 GLY   B C   1 
ATOM   2540 O  O   . GLY   B 1 73  ? 11.01300  -14.26300 39.46100  1.000 13.39682 ? 117 GLY   B O   1 
ATOM   2541 N  N   . GLU   B 1 74  ? 12.20600  -14.74400 37.60900  1.000 8.85682  ? 118 GLU   B N   1 
ATOM   2542 C  CA  . GLU   B 1 74  ? 13.46100  -14.33300 38.23300  1.000 12.71682 ? 118 GLU   B CA  1 
ATOM   2543 C  C   . GLU   B 1 74  ? 13.44700  -12.85400 38.59400  1.000 14.19682 ? 118 GLU   B C   1 
ATOM   2544 O  O   . GLU   B 1 74  ? 13.91600  -12.46300 39.66900  1.000 14.32682 ? 118 GLU   B O   1 
ATOM   2545 C  CB  . GLU   B 1 74  ? 14.64000  -14.63000 37.30700  1.000 17.80682 ? 118 GLU   B CB  1 
ATOM   2546 C  CG  . GLU   B 1 74  ? 14.83400  -16.10000 36.98300  1.000 19.84682 ? 118 GLU   B CG  1 
ATOM   2547 C  CD  . GLU   B 1 74  ? 15.73800  -16.80300 37.97000  1.000 35.27682 ? 118 GLU   B CD  1 
ATOM   2548 O  OE1 . GLU   B 1 74  ? 16.38900  -16.10900 38.78600  1.000 36.59682 ? 118 GLU   B OE1 1 
ATOM   2549 O  OE2 . GLU   B 1 74  ? 15.79300  -18.05400 37.93100  1.000 37.97682 ? 118 GLU   B OE2 1 
ATOM   2550 N  N   . ARG   B 1 75  ? 12.90900  -12.01500 37.71000  1.000 12.46682 ? 119 ARG   B N   1 
ATOM   2551 C  CA  . ARG   B 1 75  ? 13.04500  -10.57400 37.88400  1.000 13.36682 ? 119 ARG   B CA  1 
ATOM   2552 C  C   . ARG   B 1 75  ? 12.30900  -10.08500 39.12600  1.000 11.36682 ? 119 ARG   B C   1 
ATOM   2553 O  O   . ARG   B 1 75  ? 12.86700  -9.32900  39.92800  1.000 14.41682 ? 119 ARG   B O   1 
ATOM   2554 C  CB  . ARG   B 1 75  ? 12.54000  -9.85100  36.63700  1.000 14.63682 ? 119 ARG   B CB  1 
ATOM   2555 C  CG  . ARG   B 1 75  ? 12.87600  -8.37400  36.62000  1.000 15.71682 ? 119 ARG   B CG  1 
ATOM   2556 C  CD  . ARG   B 1 75  ? 13.12500  -7.91100  35.20600  1.000 16.34682 ? 119 ARG   B CD  1 
ATOM   2557 N  NE  . ARG   B 1 75  ? 13.36400  -6.47600  35.14800  1.000 15.02682 ? 119 ARG   B NE  1 
ATOM   2558 C  CZ  . ARG   B 1 75  ? 13.59800  -5.80100  34.03300  1.000 16.63682 ? 119 ARG   B CZ  1 
ATOM   2559 N  NH1 . ARG   B 1 75  ? 13.63800  -6.40500  32.85500  1.000 15.73682 ? 119 ARG   B NH1 1 
ATOM   2560 N  NH2 . ARG   B 1 75  ? 13.79300  -4.48700  34.10300  1.000 13.98682 ? 119 ARG   B NH2 1 
ATOM   2561 N  N   . VAL   B 1 76  ? 11.04900  -10.49300 39.29400  1.000 7.99682  ? 120 VAL   B N   1 
ATOM   2562 C  CA  . VAL   B 1 76  ? 10.27900  -10.06500 40.45500  1.000 13.01682 ? 120 VAL   B CA  1 
ATOM   2563 C  C   . VAL   B 1 76  ? 10.73300  -10.81000 41.70800  1.000 9.98682  ? 120 VAL   B C   1 
ATOM   2564 O  O   . VAL   B 1 76  ? 10.85800  -10.21500 42.78000  1.000 10.17682 ? 120 VAL   B O   1 
ATOM   2565 C  CB  . VAL   B 1 76  ? 8.77100   -10.24600 40.18500  1.000 8.96682  ? 120 VAL   B CB  1 
ATOM   2566 C  CG1 . VAL   B 1 76  ? 7.94600   -9.89600  41.43000  1.000 6.90682  ? 120 VAL   B CG1 1 
ATOM   2567 C  CG2 . VAL   B 1 76  ? 8.35100   -9.38100  39.00100  1.000 10.59682 ? 120 VAL   B CG2 1 
ATOM   2568 N  N   . ALA   B 1 77  ? 11.01000  -12.11200 41.59700  1.000 9.44682  ? 121 ALA   B N   1 
ATOM   2569 C  CA  . ALA   B 1 77  ? 11.41800  -12.86500 42.78300  1.000 12.31682 ? 121 ALA   B CA  1 
ATOM   2570 C  C   . ALA   B 1 77  ? 12.71700  -12.31500 43.37200  1.000 13.32682 ? 121 ALA   B C   1 
ATOM   2571 O  O   . ALA   B 1 77  ? 12.86500  -12.22300 44.59800  1.000 10.24682 ? 121 ALA   B O   1 
ATOM   2572 C  CB  . ALA   B 1 77  ? 11.55500  -14.35400 42.45400  1.000 9.07682  ? 121 ALA   B CB  1 
ATOM   2573 N  N   . SER   B 1 78  ? 13.65200  -11.89600 42.52000  1.000 9.97682  ? 122 SER   B N   1 
ATOM   2574 C  CA  . SER   B 1 78  ? 14.90800  -11.37300 43.04100  1.000 12.65682 ? 122 SER   B CA  1 
ATOM   2575 C  C   . SER   B 1 78  ? 14.73200  -10.08700 43.84100  1.000 11.88682 ? 122 SER   B C   1 
ATOM   2576 O  O   . SER   B 1 78  ? 15.67400  -9.67600  44.52800  1.000 13.83682 ? 122 SER   B O   1 
ATOM   2577 C  CB  . SER   B 1 78  ? 15.89600  -11.14700 41.89100  1.000 11.00682 ? 122 SER   B CB  1 
ATOM   2578 O  OG  . SER   B 1 78  ? 15.48500  -10.05600 41.07900  1.000 10.78682 ? 122 SER   B OG  1 
ATOM   2579 N  N   . HIS   B 1 79  ? 13.56000  -9.44800  43.78900  1.000 11.26682 ? 123 HIS   B N   1 
ATOM   2580 C  CA  . HIS   B 1 79  ? 13.29300  -8.25800  44.59000  1.000 13.05682 ? 123 HIS   B CA  1 
ATOM   2581 C  C   . HIS   B 1 79  ? 12.54900  -8.56800  45.88600  1.000 15.81682 ? 123 HIS   B C   1 
ATOM   2582 O  O   . HIS   B 1 79  ? 12.14600  -7.64100  46.59100  1.000 14.51682 ? 123 HIS   B O   1 
ATOM   2583 C  CB  . HIS   B 1 79  ? 12.52000  -7.22300  43.76700  1.000 12.73682 ? 123 HIS   B CB  1 
ATOM   2584 C  CG  . HIS   B 1 79  ? 13.38100  -6.46700  42.80900  1.000 12.20682 ? 123 HIS   B CG  1 
ATOM   2585 N  ND1 . HIS   B 1 79  ? 13.66000  -6.92400  41.53800  1.000 14.86682 ? 123 HIS   B ND1 1 
ATOM   2586 C  CD2 . HIS   B 1 79  ? 14.05600  -5.30100  42.94600  1.000 11.10682 ? 123 HIS   B CD2 1 
ATOM   2587 C  CE1 . HIS   B 1 79  ? 14.45100  -6.06000  40.92500  1.000 12.77682 ? 123 HIS   B CE1 1 
ATOM   2588 N  NE2 . HIS   B 1 79  ? 14.70900  -5.06900  41.75900  1.000 14.87682 ? 123 HIS   B NE2 1 
ATOM   2589 N  N   . GLY   B 1 80  ? 12.36800  -9.84300  46.21500  1.000 15.14682 ? 124 GLY   B N   1 
ATOM   2590 C  CA  . GLY   B 1 80  ? 11.85300  -10.22300 47.51500  1.000 12.69682 ? 124 GLY   B CA  1 
ATOM   2591 C  C   . GLY   B 1 80  ? 10.43400  -10.74800 47.49600  1.000 13.97682 ? 124 GLY   B C   1 
ATOM   2592 O  O   . GLY   B 1 80  ? 9.63300   -10.39400 48.36700  1.000 17.38682 ? 124 GLY   B O   1 
ATOM   2593 N  N   . PHE   B 1 81  ? 10.10600  -11.59400 46.52300  1.000 9.84682  ? 125 PHE   B N   1 
ATOM   2594 C  CA  . PHE   B 1 81  ? 8.78900   -12.21900 46.46900  1.000 12.21682 ? 125 PHE   B CA  1 
ATOM   2595 C  C   . PHE   B 1 81  ? 8.90500   -13.66600 46.01200  1.000 11.40682 ? 125 PHE   B C   1 
ATOM   2596 O  O   . PHE   B 1 81  ? 9.83900   -14.04600 45.30800  1.000 10.41682 ? 125 PHE   B O   1 
ATOM   2597 C  CB  . PHE   B 1 81  ? 7.84400   -11.47100 45.51700  1.000 11.33682 ? 125 PHE   B CB  1 
ATOM   2598 C  CG  . PHE   B 1 81  ? 7.67800   -10.02900 45.84700  1.000 11.90682 ? 125 PHE   B CG  1 
ATOM   2599 C  CD1 . PHE   B 1 81  ? 6.75700   -9.62300  46.80300  1.000 10.18682 ? 125 PHE   B CD1 1 
ATOM   2600 C  CD2 . PHE   B 1 81  ? 8.44500   -9.06900  45.20900  1.000 9.23682  ? 125 PHE   B CD2 1 
ATOM   2601 C  CE1 . PHE   B 1 81  ? 6.60400   -8.29100  47.10800  1.000 7.86682  ? 125 PHE   B CE1 1 
ATOM   2602 C  CE2 . PHE   B 1 81  ? 8.30200   -7.74000  45.51900  1.000 9.92682  ? 125 PHE   B CE2 1 
ATOM   2603 C  CZ  . PHE   B 1 81  ? 7.38000   -7.34700  46.46900  1.000 10.40682 ? 125 PHE   B CZ  1 
ATOM   2604 N  N   . ILE   B 1 82  ? 7.92400   -14.46900 46.40000  1.000 9.86682  ? 126 ILE   B N   1 
ATOM   2605 C  CA  . ILE   B 1 82  ? 7.74300   -15.79400 45.82300  1.000 7.58682  ? 126 ILE   B CA  1 
ATOM   2606 C  C   . ILE   B 1 82  ? 6.80700   -15.65200 44.62700  1.000 9.65682  ? 126 ILE   B C   1 
ATOM   2607 O  O   . ILE   B 1 82  ? 5.71300   -15.09900 44.75600  1.000 10.32682 ? 126 ILE   B O   1 
ATOM   2608 C  CB  . ILE   B 1 82  ? 7.18600   -16.77900 46.86700  1.000 8.58682  ? 126 ILE   B CB  1 
ATOM   2609 C  CG1 . ILE   B 1 82  ? 8.24200   -17.04100 47.95500  1.000 10.80682 ? 126 ILE   B CG1 1 
ATOM   2610 C  CG2 . ILE   B 1 82  ? 6.72900   -18.07600 46.18300  1.000 9.08682  ? 126 ILE   B CG2 1 
ATOM   2611 C  CD1 . ILE   B 1 82  ? 7.71200   -17.70400 49.22900  1.000 12.51682 ? 126 ILE   B CD1 1 
ATOM   2612 N  N   . VAL   B 1 83  ? 7.24100   -16.11800 43.45700  1.000 10.19682 ? 127 VAL   B N   1 
ATOM   2613 C  CA  . VAL   B 1 83  ? 6.53300   -15.87400 42.19800  1.000 13.52682 ? 127 VAL   B CA  1 
ATOM   2614 C  C   . VAL   B 1 83  ? 6.18200   -17.21900 41.56000  1.000 9.88682  ? 127 VAL   B C   1 
ATOM   2615 O  O   . VAL   B 1 83  ? 7.07400   -18.02000 41.25800  1.000 13.13682 ? 127 VAL   B O   1 
ATOM   2616 C  CB  . VAL   B 1 83  ? 7.36800   -14.99900 41.24500  1.000 12.31682 ? 127 VAL   B CB  1 
ATOM   2617 C  CG1 . VAL   B 1 83  ? 6.64200   -14.76900 39.95400  1.000 9.25682  ? 127 VAL   B CG1 1 
ATOM   2618 C  CG2 . VAL   B 1 83  ? 7.69600   -13.66000 41.90800  1.000 8.68682  ? 127 VAL   B CG2 1 
ATOM   2619 N  N   . PHE   B 1 84  ? 4.88300   -17.46500 41.36600  1.000 8.16682  ? 128 PHE   B N   1 
ATOM   2620 C  CA  . PHE   B 1 84  ? 4.35700   -18.72000 40.81600  1.000 8.75682  ? 128 PHE   B CA  1 
ATOM   2621 C  C   . PHE   B 1 84  ? 3.76600   -18.45200 39.42700  1.000 10.32682 ? 128 PHE   B C   1 
ATOM   2622 O  O   . PHE   B 1 84  ? 2.67000   -17.89200 39.31000  1.000 11.31682 ? 128 PHE   B O   1 
ATOM   2623 C  CB  . PHE   B 1 84  ? 3.30200   -19.29500 41.76500  1.000 11.97682 ? 128 PHE   B CB  1 
ATOM   2624 C  CG  . PHE   B 1 84  ? 3.02900   -20.78500 41.58800  1.000 9.36682  ? 128 PHE   B CG  1 
ATOM   2625 C  CD1 . PHE   B 1 84  ? 3.75100   -21.55300 40.69300  1.000 9.28682  ? 128 PHE   B CD1 1 
ATOM   2626 C  CD2 . PHE   B 1 84  ? 2.05300   -21.40900 42.35500  1.000 12.18682 ? 128 PHE   B CD2 1 
ATOM   2627 C  CE1 . PHE   B 1 84  ? 3.48400   -22.92100 40.54800  1.000 10.78682 ? 128 PHE   B CE1 1 
ATOM   2628 C  CE2 . PHE   B 1 84  ? 1.79100   -22.77100 42.22100  1.000 10.50682 ? 128 PHE   B CE2 1 
ATOM   2629 C  CZ  . PHE   B 1 84  ? 2.50400   -23.52400 41.31700  1.000 10.36682 ? 128 PHE   B CZ  1 
ATOM   2630 N  N   . THR   B 1 85  ? 4.48300   -18.83700 38.36900  1.000 8.50682  ? 129 THR   B N   1 
ATOM   2631 C  CA  . THR   B 1 85  ? 3.93800   -18.73300 37.01500  1.000 9.94682  ? 129 THR   B CA  1 
ATOM   2632 C  C   . THR   B 1 85  ? 3.23400   -20.03900 36.68000  1.000 11.59682 ? 129 THR   B C   1 
ATOM   2633 O  O   . THR   B 1 85  ? 3.87900   -21.08600 36.60400  1.000 12.09682 ? 129 THR   B O   1 
ATOM   2634 C  CB  . THR   B 1 85  ? 5.01700   -18.44300 35.97000  1.000 12.66682 ? 129 THR   B CB  1 
ATOM   2635 O  OG1 . THR   B 1 85  ? 5.95900   -19.52200 35.93800  1.000 11.06682 ? 129 THR   B OG1 1 
ATOM   2636 C  CG2 . THR   B 1 85  ? 5.73000   -17.12400 36.27300  1.000 9.02682  ? 129 THR   B CG2 1 
ATOM   2637 N  N   . ILE   B 1 86  ? 1.92400   -19.98000 36.47100  1.000 10.89682 ? 130 ILE   B N   1 
ATOM   2638 C  CA  . ILE   B 1 86  ? 1.13100   -21.19200 36.36600  1.000 13.09682 ? 130 ILE   B CA  1 
ATOM   2639 C  C   . ILE   B 1 86  ? 0.71800   -21.44500 34.92300  1.000 15.98682 ? 130 ILE   B C   1 
ATOM   2640 O  O   . ILE   B 1 86  ? 0.71800   -20.55200 34.06700  1.000 14.49682 ? 130 ILE   B O   1 
ATOM   2641 C  CB  . ILE   B 1 86  ? -0.11400  -21.15700 37.28200  1.000 10.45682 ? 130 ILE   B CB  1 
ATOM   2642 C  CG1 . ILE   B 1 86  ? -1.18100  -20.21300 36.71400  1.000 13.70682 ? 130 ILE   B CG1 1 
ATOM   2643 C  CG2 . ILE   B 1 86  ? 0.28500   -20.75400 38.69700  1.000 11.57682 ? 130 ILE   B CG2 1 
ATOM   2644 C  CD1 . ILE   B 1 86  ? -2.57100  -20.42700 37.30100  1.000 15.49682 ? 130 ILE   B CD1 1 
ATOM   2645 N  N   . ASP   B 1 87  ? 0.39000   -22.70600 34.65900  1.000 13.65682 ? 131 ASP   B N   1 
ATOM   2646 C  CA  . ASP   B 1 87  ? -0.41200  -23.10200 33.51500  1.000 14.93682 ? 131 ASP   B CA  1 
ATOM   2647 C  C   . ASP   B 1 87  ? -1.84000  -23.34300 33.98900  1.000 16.85682 ? 131 ASP   B C   1 
ATOM   2648 O  O   . ASP   B 1 87  ? -2.06600  -23.80700 35.10800  1.000 14.62682 ? 131 ASP   B O   1 
ATOM   2649 C  CB  . ASP   B 1 87  ? 0.13000   -24.37200 32.85300  1.000 19.85682 ? 131 ASP   B CB  1 
ATOM   2650 C  CG  . ASP   B 1 87  ? 1.35400   -24.11400 32.00300  1.000 23.40682 ? 131 ASP   B CG  1 
ATOM   2651 O  OD1 . ASP   B 1 87  ? 1.27700   -23.27800 31.07300  1.000 24.61682 ? 131 ASP   B OD1 1 
ATOM   2652 O  OD2 . ASP   B 1 87  ? 2.39500   -24.75300 32.26600  1.000 22.86682 ? 131 ASP   B OD2 1 
ATOM   2653 N  N   . THR   B 1 88  ? -2.80300  -23.02000 33.12900  1.000 14.33682 ? 132 THR   B N   1 
ATOM   2654 C  CA  . THR   B 1 88  ? -4.21000  -23.24800 33.41400  1.000 15.47682 ? 132 THR   B CA  1 
ATOM   2655 C  C   . THR   B 1 88  ? -4.60200  -24.67800 33.04200  1.000 15.99682 ? 132 THR   B C   1 
ATOM   2656 O  O   . THR   B 1 88  ? -3.86700  -25.39300 32.35600  1.000 14.73682 ? 132 THR   B O   1 
ATOM   2657 C  CB  . THR   B 1 88  ? -5.07400  -22.24500 32.65200  1.000 14.81682 ? 132 THR   B CB  1 
ATOM   2658 O  OG1 . THR   B 1 88  ? -4.79800  -22.36700 31.25000  1.000 13.67682 ? 132 THR   B OG1 1 
ATOM   2659 C  CG2 . THR   B 1 88  ? -4.76000  -20.82700 33.09700  1.000 11.43682 ? 132 THR   B CG2 1 
ATOM   2660 N  N   . ASN   B 1 89  ? -5.79600  -25.08600 33.48500  1.000 11.02682 ? 133 ASN   B N   1 
ATOM   2661 C  CA  . ASN   B 1 89  ? -6.21500  -26.46900 33.27700  1.000 12.86682 ? 133 ASN   B CA  1 
ATOM   2662 C  C   . ASN   B 1 89  ? -6.25400  -26.82200 31.80100  1.000 18.51682 ? 133 ASN   B C   1 
ATOM   2663 O  O   . ASN   B 1 89  ? -5.82700  -27.91600 31.41200  1.000 16.03682 ? 133 ASN   B O   1 
ATOM   2664 C  CB  . ASN   B 1 89  ? -7.57000  -26.71700 33.91800  1.000 14.02682 ? 133 ASN   B CB  1 
ATOM   2665 C  CG  . ASN   B 1 89  ? -7.46000  -26.94600 35.41000  1.000 18.16682 ? 133 ASN   B CG  1 
ATOM   2666 O  OD1 . ASN   B 1 89  ? -6.45000  -27.46900 35.89500  1.000 13.94682 ? 133 ASN   B OD1 1 
ATOM   2667 N  ND2 . ASN   B 1 89  ? -8.49000  -26.55400 36.14600  1.000 16.05682 ? 133 ASN   B ND2 1 
ATOM   2668 N  N   . THR   B 1 90  ? -6.79800  -25.93100 30.96800  1.000 13.59682 ? 134 THR   B N   1 
ATOM   2669 C  CA  . THR   B 1 90  ? -6.59000  -26.00800 29.53100  1.000 15.44682 ? 134 THR   B CA  1 
ATOM   2670 C  C   . THR   B 1 90  ? -6.27400  -24.60500 29.02600  1.000 17.37682 ? 134 THR   B C   1 
ATOM   2671 O  O   . THR   B 1 90  ? -6.53700  -23.60300 29.69500  1.000 13.91682 ? 134 THR   B O   1 
ATOM   2672 C  CB  . THR   B 1 90  ? -7.79400  -26.61000 28.76100  1.000 16.50682 ? 134 THR   B CB  1 
ATOM   2673 O  OG1 . THR   B 1 90  ? -8.73100  -25.58200 28.41800  1.000 16.44682 ? 134 THR   B OG1 1 
ATOM   2674 C  CG2 . THR   B 1 90  ? -8.51500  -27.68200 29.58500  1.000 26.03682 ? 134 THR   B CG2 1 
ATOM   2675 N  N   . ARG   B 1 91  ? -5.68800  -24.54600 27.83500  1.000 12.62682 ? 135 ARG   B N   1 
ATOM   2676 C  CA  . ARG   B 1 91  ? -5.32500  -23.26000 27.26400  1.000 16.70682 ? 135 ARG   B CA  1 
ATOM   2677 C  C   . ARG   B 1 91  ? -6.53900  -22.45200 26.82700  1.000 17.62682 ? 135 ARG   B C   1 
ATOM   2678 O  O   . ARG   B 1 91  ? -6.38900  -21.27900 26.47100  1.000 13.63682 ? 135 ARG   B O   1 
ATOM   2679 C  CB  . ARG   B 1 91  ? -4.37700  -23.48300 26.08900  1.000 18.16682 ? 135 ARG   B CB  1 
ATOM   2680 C  CG  . ARG   B 1 91  ? -3.17500  -24.34400 26.46000  1.000 25.05682 ? 135 ARG   B CG  1 
ATOM   2681 C  CD  . ARG   B 1 91  ? -2.39700  -24.79000 25.23800  1.000 32.48682 ? 135 ARG   B CD  1 
ATOM   2682 N  NE  . ARG   B 1 91  ? -1.51500  -23.73400 24.76200  1.000 40.63682 ? 135 ARG   B NE  1 
ATOM   2683 C  CZ  . ARG   B 1 91  ? -0.23100  -23.63000 25.08000  1.000 37.38682 ? 135 ARG   B CZ  1 
ATOM   2684 N  NH1 . ARG   B 1 91  ? 0.36500   -24.52100 25.85900  1.000 40.48682 ? 135 ARG   B NH1 1 
ATOM   2685 N  NH2 . ARG   B 1 91  ? 0.47200   -22.60600 24.60400  1.000 27.09682 ? 135 ARG   B NH2 1 
ATOM   2686 N  N   . LEU   B 1 92  ? -7.73000  -23.04600 26.85800  1.000 15.39682 ? 136 LEU   B N   1 
ATOM   2687 C  CA  . LEU   B 1 92  ? -8.94800  -22.39000 26.41300  1.000 14.35682 ? 136 LEU   B CA  1 
ATOM   2688 C  C   . LEU   B 1 92  ? -9.83000  -21.94900 27.57500  1.000 14.56682 ? 136 LEU   B C   1 
ATOM   2689 O  O   . LEU   B 1 92  ? -10.97000 -21.52100 27.35200  1.000 14.80682 ? 136 LEU   B O   1 
ATOM   2690 C  CB  . LEU   B 1 92  ? -9.72400  -23.31600 25.47000  1.000 15.64682 ? 136 LEU   B CB  1 
ATOM   2691 C  CG  . LEU   B 1 92  ? -8.99700  -23.70000 24.18000  1.000 19.97682 ? 136 LEU   B CG  1 
ATOM   2692 C  CD1 . LEU   B 1 92  ? -9.93200  -24.42100 23.22000  1.000 22.43682 ? 136 LEU   B CD1 1 
ATOM   2693 C  CD2 . LEU   B 1 92  ? -8.37400  -22.47200 23.52200  1.000 17.39682 ? 136 LEU   B CD2 1 
ATOM   2694 N  N   . ASP   B 1 93  ? -9.32500  -22.01200 28.80600  1.000 15.10682 ? 137 ASP   B N   1 
ATOM   2695 C  CA  . ASP   B 1 93  ? -10.13400 -21.63900 29.95700  1.000 15.38682 ? 137 ASP   B CA  1 
ATOM   2696 C  C   . ASP   B 1 93  ? -10.52300 -20.16200 29.89500  1.000 14.09682 ? 137 ASP   B C   1 
ATOM   2697 O  O   . ASP   B 1 93  ? -9.79800  -19.33100 29.34500  1.000 13.80682 ? 137 ASP   B O   1 
ATOM   2698 C  CB  . ASP   B 1 93  ? -9.38100  -21.92500 31.25400  1.000 15.32682 ? 137 ASP   B CB  1 
ATOM   2699 C  CG  . ASP   B 1 93  ? -9.25400  -23.40800 31.54800  1.000 20.06682 ? 137 ASP   B CG  1 
ATOM   2700 O  OD1 . ASP   B 1 93  ? -9.90000  -24.23600 30.86000  1.000 23.77682 ? 137 ASP   B OD1 1 
ATOM   2701 O  OD2 . ASP   B 1 93  ? -8.50000  -23.75200 32.47900  1.000 19.61682 ? 137 ASP   B OD2 1 
ATOM   2702 N  N   . ALA   B 1 94  ? -11.67400 -19.84700 30.49100  1.000 12.20682 ? 138 ALA   B N   1 
ATOM   2703 C  CA  . ALA   B 1 94  ? -12.27000 -18.51000 30.51300  1.000 13.32682 ? 138 ALA   B CA  1 
ATOM   2704 C  C   . ALA   B 1 94  ? -11.71900 -17.68400 31.67000  1.000 14.75682 ? 138 ALA   B C   1 
ATOM   2705 O  O   . ALA   B 1 94  ? -11.09900 -18.21800 32.60100  1.000 14.49682 ? 138 ALA   B O   1 
ATOM   2706 C  CB  . ALA   B 1 94  ? -13.78900 -18.63800 30.62400  1.000 15.14682 ? 138 ALA   B CB  1 
ATOM   2707 N  N   . PRO   B 1 95  ? -11.94400 -16.35500 31.66500  1.000 13.34682 ? 139 PRO   B N   1 
ATOM   2708 C  CA  . PRO   B 1 95  ? -11.38000 -15.53100 32.75500  1.000 13.88682 ? 139 PRO   B CA  1 
ATOM   2709 C  C   . PRO   B 1 95  ? -11.82700 -15.95300 34.14800  1.000 16.70682 ? 139 PRO   B C   1 
ATOM   2710 O  O   . PRO   B 1 95  ? -11.00900 -15.93200 35.07700  1.000 13.88682 ? 139 PRO   B O   1 
ATOM   2711 C  CB  . PRO   B 1 95  ? -11.85500 -14.11400 32.40400  1.000 15.81682 ? 139 PRO   B CB  1 
ATOM   2712 C  CG  . PRO   B 1 95  ? -12.05000 -14.13500 30.94000  1.000 13.31682 ? 139 PRO   B CG  1 
ATOM   2713 C  CD  . PRO   B 1 95  ? -12.57300 -15.50800 30.63000  1.000 12.86682 ? 139 PRO   B CD  1 
ATOM   2714 N  N   . GLY   B 1 96  ? -13.09000 -16.35300 34.33000  1.000 14.37682 ? 140 GLY   B N   1 
ATOM   2715 C  CA  . GLY   B 1 96  ? -13.52700 -16.72500 35.67400  1.000 15.70682 ? 140 GLY   B CA  1 
ATOM   2716 C  C   . GLY   B 1 96  ? -12.86900 -18.02600 36.12700  1.000 16.20682 ? 140 GLY   B C   1 
ATOM   2717 O  O   . GLY   B 1 96  ? -12.53600 -18.18600 37.31000  1.000 16.18682 ? 140 GLY   B O   1 
ATOM   2718 N  N   . GLN   B 1 97  ? -12.66100 -18.96200 35.20100  1.000 13.70682 ? 141 GLN   B N   1 
ATOM   2719 C  CA  . GLN   B 1 97  ? -11.85300 -20.14200 35.49900  1.000 12.97682 ? 141 GLN   B CA  1 
ATOM   2720 C  C   . GLN   B 1 97  ? -10.42400 -19.75700 35.87400  1.000 14.31682 ? 141 GLN   B C   1 
ATOM   2721 O  O   . GLN   B 1 97  ? -9.86900  -20.26900 36.85100  1.000 14.40682 ? 141 GLN   B O   1 
ATOM   2722 C  CB  . GLN   B 1 97  ? -11.85400 -21.09000 34.29900  1.000 17.89682 ? 141 GLN   B CB  1 
ATOM   2723 C  CG  . GLN   B 1 97  ? -13.24200 -21.59700 33.92700  1.000 24.77682 ? 141 GLN   B CG  1 
ATOM   2724 C  CD  . GLN   B 1 97  ? -13.23200 -22.44700 32.67200  1.000 19.78682 ? 141 GLN   B CD  1 
ATOM   2725 O  OE1 . GLN   B 1 97  ? -13.03400 -21.93900 31.56400  1.000 17.85682 ? 141 GLN   B OE1 1 
ATOM   2726 N  NE2 . GLN   B 1 97  ? -13.43000 -23.74500 32.84000  1.000 21.07682 ? 141 GLN   B NE2 1 
ATOM   2727 N  N   . ARG   B 1 98  ? -9.79800  -18.87400 35.09100  1.000 13.06682 ? 142 ARG   B N   1 
ATOM   2728 C  CA  . ARG   B 1 98  ? -8.43500  -18.45200 35.40600  1.000 11.23682 ? 142 ARG   B CA  1 
ATOM   2729 C  C   . ARG   B 1 98  ? -8.33400  -17.84300 36.80500  1.000 13.05682 ? 142 ARG   B C   1 
ATOM   2730 O  O   . ARG   B 1 98  ? -7.32200  -18.03500 37.49300  1.000 12.06682 ? 142 ARG   B O   1 
ATOM   2731 C  CB  . ARG   B 1 98  ? -7.93700  -17.47500 34.33300  1.000 13.66682 ? 142 ARG   B CB  1 
ATOM   2732 C  CG  . ARG   B 1 98  ? -7.80200  -18.16000 32.97600  1.000 10.60682 ? 142 ARG   B CG  1 
ATOM   2733 C  CD  . ARG   B 1 98  ? -7.47600  -17.21700 31.82700  1.000 14.26682 ? 142 ARG   B CD  1 
ATOM   2734 N  NE  . ARG   B 1 98  ? -7.58500  -17.96700 30.58500  1.000 14.31682 ? 142 ARG   B NE  1 
ATOM   2735 C  CZ  . ARG   B 1 98  ? -6.57500  -18.59000 29.99200  1.000 14.45682 ? 142 ARG   B CZ  1 
ATOM   2736 N  NH1 . ARG   B 1 98  ? -5.32600  -18.40900 30.38000  1.000 13.12682 ? 142 ARG   B NH1 1 
ATOM   2737 N  NH2 . ARG   B 1 98  ? -6.82400  -19.41000 28.97700  1.000 15.41682 ? 142 ARG   B NH2 1 
ATOM   2738 N  N   . GLY   B 1 99  ? -9.38000  -17.15000 37.26100  1.000 11.33682 ? 143 GLY   B N   1 
ATOM   2739 C  CA  . GLY   B 1 99  ? -9.37000  -16.62400 38.62100  1.000 12.98682 ? 143 GLY   B CA  1 
ATOM   2740 C  C   . GLY   B 1 99  ? -9.43200  -17.70700 39.68600  1.000 13.69682 ? 143 GLY   B C   1 
ATOM   2741 O  O   . GLY   B 1 99  ? -8.73000  -17.63100 40.70000  1.000 11.38682 ? 143 GLY   B O   1 
ATOM   2742 N  N   . ARG   B 1 100 ? -10.28900 -18.71900 39.49000  1.000 9.85682  ? 144 ARG   B N   1 
ATOM   2743 C  CA  . ARG   B 1 100 ? -10.31900 -19.83500 40.43700  1.000 14.99682 ? 144 ARG   B CA  1 
ATOM   2744 C  C   . ARG   B 1 100 ? -8.97500  -20.53900 40.48800  1.000 12.29682 ? 144 ARG   B C   1 
ATOM   2745 O  O   . ARG   B 1 100 ? -8.52200  -20.95700 41.56300  1.000 10.53682 ? 144 ARG   B O   1 
ATOM   2746 C  CB  . ARG   B 1 100 ? -11.40600 -20.84800 40.07200  1.000 16.15682 ? 144 ARG   B CB  1 
ATOM   2747 C  CG  . ARG   B 1 100 ? -12.82700 -20.37600 40.29100  1.000 28.76682 ? 144 ARG   B CG  1 
ATOM   2748 C  CD  . ARG   B 1 100 ? -13.81900 -21.50400 40.00000  1.000 29.76682 ? 144 ARG   B CD  1 
ATOM   2749 N  NE  . ARG   B 1 100 ? -15.19300 -21.01600 39.98700  1.000 34.02682 ? 144 ARG   B NE  1 
ATOM   2750 C  CZ  . ARG   B 1 100 ? -15.82400 -20.58800 38.90200  1.000 34.25682 ? 144 ARG   B CZ  1 
ATOM   2751 N  NH1 . ARG   B 1 100 ? -15.24000 -20.59800 37.71200  1.000 34.51682 ? 144 ARG   B NH1 1 
ATOM   2752 N  NH2 . ARG   B 1 100 ? -17.07000 -20.13600 39.01200  1.000 44.45682 ? 144 ARG   B NH2 1 
ATOM   2753 N  N   . GLN   B 1 101 ? -8.32000  -20.67600 39.33000  1.000 7.61682  ? 145 GLN   B N   1 
ATOM   2754 C  CA  . GLN   B 1 101 ? -7.05900  -21.40900 39.26900  1.000 12.04682 ? 145 GLN   B CA  1 
ATOM   2755 C  C   . GLN   B 1 101 ? -5.90600  -20.61700 39.87100  1.000 13.24682 ? 145 GLN   B C   1 
ATOM   2756 O  O   . GLN   B 1 101 ? -4.97800  -21.21100 40.42700  1.000 9.92682  ? 145 GLN   B O   1 
ATOM   2757 C  CB  . GLN   B 1 101 ? -6.77500  -21.81000 37.82300  1.000 13.55682 ? 145 GLN   B CB  1 
ATOM   2758 C  CG  . GLN   B 1 101 ? -7.85900  -22.76700 37.30800  1.000 10.54682 ? 145 GLN   B CG  1 
ATOM   2759 C  CD  . GLN   B 1 101 ? -7.69200  -23.14900 35.85800  1.000 15.91682 ? 145 GLN   B CD  1 
ATOM   2760 O  OE1 . GLN   B 1 101 ? -6.59100  -23.45500 35.41400  1.000 16.36682 ? 145 GLN   B OE1 1 
ATOM   2761 N  NE2 . GLN   B 1 101 ? -8.79400  -23.15800 35.11600  1.000 12.17682 ? 145 GLN   B NE2 1 
ATOM   2762 N  N   . LEU   B 1 102 ? -5.94800  -19.28500 39.80200  1.000 10.16682 ? 146 LEU   B N   1 
ATOM   2763 C  CA  . LEU   B 1 102 ? -4.95800  -18.50000 40.53700  1.000 12.72682 ? 146 LEU   B CA  1 
ATOM   2764 C  C   . LEU   B 1 102 ? -5.07800  -18.75200 42.03700  1.000 12.24682 ? 146 LEU   B C   1 
ATOM   2765 O  O   . LEU   B 1 102 ? -4.06800  -18.88100 42.74000  1.000 11.54682 ? 146 LEU   B O   1 
ATOM   2766 C  CB  . LEU   B 1 102 ? -5.12700  -17.00900 40.22900  1.000 7.15682  ? 146 LEU   B CB  1 
ATOM   2767 C  CG  . LEU   B 1 102 ? -4.63700  -16.53500 38.85700  1.000 13.46682 ? 146 LEU   B CG  1 
ATOM   2768 C  CD1 . LEU   B 1 102 ? -5.29900  -15.22100 38.46000  1.000 9.39682  ? 146 LEU   B CD1 1 
ATOM   2769 C  CD2 . LEU   B 1 102 ? -3.12400  -16.36500 38.89200  1.000 13.95682 ? 146 LEU   B CD2 1 
ATOM   2770 N  N   . LEU   B 1 103 ? -6.31100  -18.84600 42.53800  1.000 9.83682  ? 147 LEU   B N   1 
ATOM   2771 C  CA  . LEU   B 1 103 ? -6.52600  -19.10400 43.95600  1.000 10.39682 ? 147 LEU   B CA  1 
ATOM   2772 C  C   . LEU   B 1 103 ? -6.15200  -20.53500 44.32100  1.000 13.29682 ? 147 LEU   B C   1 
ATOM   2773 O  O   . LEU   B 1 103 ? -5.62600  -20.78700 45.41600  1.000 11.13682 ? 147 LEU   B O   1 
ATOM   2774 C  CB  . LEU   B 1 103 ? -7.98400  -18.81200 44.32400  1.000 10.64682 ? 147 LEU   B CB  1 
ATOM   2775 C  CG  . LEU   B 1 103 ? -8.47800  -17.36900 44.15900  1.000 10.55682 ? 147 LEU   B CG  1 
ATOM   2776 C  CD1 . LEU   B 1 103 ? -9.96800  -17.24700 44.48000  1.000 10.85682 ? 147 LEU   B CD1 1 
ATOM   2777 C  CD2 . LEU   B 1 103 ? -7.66000  -16.40100 45.00800  1.000 10.54682 ? 147 LEU   B CD2 1 
ATOM   2778 N  N   . ALA   B 1 104 ? -6.42600  -21.49100 43.42300  1.000 12.43682 ? 148 ALA   B N   1 
ATOM   2779 C  CA  . ALA   B 1 104 ? -5.97500  -22.85900 43.65200  1.000 12.65682 ? 148 ALA   B CA  1 
ATOM   2780 C  C   . ALA   B 1 104 ? -4.45700  -22.91800 43.74700  1.000 17.29682 ? 148 ALA   B C   1 
ATOM   2781 O  O   . ALA   B 1 104 ? -3.91000  -23.63600 44.58900  1.000 14.56682 ? 148 ALA   B O   1 
ATOM   2782 C  CB  . ALA   B 1 104 ? -6.47400  -23.78200 42.54100  1.000 15.32682 ? 148 ALA   B CB  1 
ATOM   2783 N  N   . ALA   B 1 105 ? -3.76100  -22.14300 42.90900  1.000 11.41682 ? 149 ALA   B N   1 
ATOM   2784 C  CA  . ALA   B 1 105 ? -2.30300  -22.15400 42.92700  1.000 11.97682 ? 149 ALA   B CA  1 
ATOM   2785 C  C   . ALA   B 1 105 ? -1.75700  -21.53500 44.20500  1.000 11.72682 ? 149 ALA   B C   1 
ATOM   2786 O  O   . ALA   B 1 105 ? -0.75400  -22.01300 44.75600  1.000 10.91682 ? 149 ALA   B O   1 
ATOM   2787 C  CB  . ALA   B 1 105 ? -1.75600  -21.42000 41.70000  1.000 10.35682 ? 149 ALA   B CB  1 
ATOM   2788 N  N   . LEU   B 1 106 ? -2.39000  -20.46700 44.69000  1.000 13.50682 ? 150 LEU   B N   1 
ATOM   2789 C  CA  . LEU   B 1 106 ? -1.94100  -19.86600 45.94400  1.000 13.60682 ? 150 LEU   B CA  1 
ATOM   2790 C  C   . LEU   B 1 106 ? -2.16700  -20.81500 47.11300  1.000 12.14682 ? 150 LEU   B C   1 
ATOM   2791 O  O   . LEU   B 1 106 ? -1.30200  -20.95500 47.98800  1.000 13.19682 ? 150 LEU   B O   1 
ATOM   2792 C  CB  . LEU   B 1 106 ? -2.65700  -18.53400 46.17700  1.000 10.54682 ? 150 LEU   B CB  1 
ATOM   2793 C  CG  . LEU   B 1 106 ? -2.27100  -17.37200 45.25400  1.000 13.02682 ? 150 LEU   B CG  1 
ATOM   2794 C  CD1 . LEU   B 1 106 ? -3.18400  -16.17800 45.47900  1.000 11.20682 ? 150 LEU   B CD1 1 
ATOM   2795 C  CD2 . LEU   B 1 106 ? -0.81000  -16.97300 45.48200  1.000 10.53682 ? 150 LEU   B CD2 1 
ATOM   2796 N  N   . ASP   B 1 107 ? -3.32200  -21.48500 47.14100  1.000 15.78682 ? 151 ASP   B N   1 
ATOM   2797 C  CA  . ASP   B 1 107 ? -3.58000  -22.46800 48.18600  1.000 13.70682 ? 151 ASP   B CA  1 
ATOM   2798 C  C   . ASP   B 1 107 ? -2.61300  -23.65000 48.10800  1.000 14.68682 ? 151 ASP   B C   1 
ATOM   2799 O  O   . ASP   B 1 107 ? -2.23100  -24.20700 49.14300  1.000 17.07682 ? 151 ASP   B O   1 
ATOM   2800 C  CB  . ASP   B 1 107 ? -5.03100  -22.93200 48.09500  1.000 13.06682 ? 151 ASP   B CB  1 
ATOM   2801 C  CG  . ASP   B 1 107 ? -6.00100  -21.84800 48.53000  1.000 17.17682 ? 151 ASP   B CG  1 
ATOM   2802 O  OD1 . ASP   B 1 107 ? -5.52800  -20.82400 49.07900  1.000 23.61682 ? 151 ASP   B OD1 1 
ATOM   2803 O  OD2 . ASP   B 1 107 ? -7.22000  -22.00000 48.30800  1.000 23.04682 ? 151 ASP   B OD2 1 
ATOM   2804 N  N   . TYR   B 1 108 ? -2.21900  -24.05600 46.90000  1.000 14.24682 ? 152 TYR   B N   1 
ATOM   2805 C  CA  . TYR   B 1 108 ? -1.16400  -25.05300 46.77700  1.000 13.31682 ? 152 TYR   B CA  1 
ATOM   2806 C  C   . TYR   B 1 108 ? 0.10900   -24.57300 47.46400  1.000 15.56682 ? 152 TYR   B C   1 
ATOM   2807 O  O   . TYR   B 1 108 ? 0.70800   -25.30300 48.26400  1.000 13.09682 ? 152 TYR   B O   1 
ATOM   2808 C  CB  . TYR   B 1 108 ? -0.89600  -25.37300 45.30500  1.000 15.42682 ? 152 TYR   B CB  1 
ATOM   2809 C  CG  . TYR   B 1 108 ? 0.37100   -26.17600 45.11700  1.000 17.39682 ? 152 TYR   B CG  1 
ATOM   2810 C  CD1 . TYR   B 1 108 ? 0.34900   -27.56400 45.15600  1.000 16.12682 ? 152 TYR   B CD1 1 
ATOM   2811 C  CD2 . TYR   B 1 108 ? 1.59900   -25.54100 44.93000  1.000 14.66682 ? 152 TYR   B CD2 1 
ATOM   2812 C  CE1 . TYR   B 1 108 ? 1.51500   -28.29600 45.00400  1.000 14.22682 ? 152 TYR   B CE1 1 
ATOM   2813 C  CE2 . TYR   B 1 108 ? 2.76400   -26.26000 44.77900  1.000 13.65682 ? 152 TYR   B CE2 1 
ATOM   2814 C  CZ  . TYR   B 1 108 ? 2.72100   -27.63200 44.81600  1.000 16.69682 ? 152 TYR   B CZ  1 
ATOM   2815 O  OH  . TYR   B 1 108 ? 3.89400   -28.33900 44.66900  1.000 17.72682 ? 152 TYR   B OH  1 
ATOM   2816 N  N   . LEU   B 1 109 ? 0.53900   -23.34200 47.15200  1.000 12.14682 ? 153 LEU   B N   1 
ATOM   2817 C  CA  . LEU   B 1 109 ? 1.74000   -22.76800 47.76300  1.000 14.26682 ? 153 LEU   B CA  1 
ATOM   2818 C  C   . LEU   B 1 109 ? 1.70800   -22.85600 49.28100  1.000 11.93682 ? 153 LEU   B C   1 
ATOM   2819 O  O   . LEU   B 1 109 ? 2.71200   -23.20400 49.91300  1.000 10.67682 ? 153 LEU   B O   1 
ATOM   2820 C  CB  . LEU   B 1 109 ? 1.90100   -21.30300 47.36100  1.000 12.09682 ? 153 LEU   B CB  1 
ATOM   2821 C  CG  . LEU   B 1 109 ? 2.43500   -20.84500 46.01400  1.000 18.82682 ? 153 LEU   B CG  1 
ATOM   2822 C  CD1 . LEU   B 1 109 ? 2.53300   -19.32000 46.02900  1.000 14.84682 ? 153 LEU   B CD1 1 
ATOM   2823 C  CD2 . LEU   B 1 109 ? 3.78400   -21.45400 45.72800  1.000 11.98682 ? 153 LEU   B CD2 1 
ATOM   2824 N  N   . VAL   B 1 110 ? 0.56300   -22.53200 49.88300  1.000 12.63682 ? 154 VAL   B N   1 
ATOM   2825 C  CA  . VAL   B 1 110 ? 0.46200   -22.47900 51.34100  1.000 13.49682 ? 154 VAL   B CA  1 
ATOM   2826 C  C   . VAL   B 1 110 ? 0.46900   -23.88500 51.93500  1.000 19.16682 ? 154 VAL   B C   1 
ATOM   2827 O  O   . VAL   B 1 110 ? 1.12500   -24.14500 52.95200  1.000 14.33682 ? 154 VAL   B O   1 
ATOM   2828 C  CB  . VAL   B 1 110 ? -0.80300  -21.69600 51.75200  1.000 14.66682 ? 154 VAL   B CB  1 
ATOM   2829 C  CG1 . VAL   B 1 110 ? -1.15100  -21.94200 53.21500  1.000 17.15682 ? 154 VAL   B CG1 1 
ATOM   2830 C  CG2 . VAL   B 1 110 ? -0.63900  -20.20400 51.49400  1.000 15.50682 ? 154 VAL   B CG2 1 
ATOM   2831 N  N   . GLU   B 1 111 ? -0.24300  -24.81600 51.30300  1.000 14.50682 ? 155 GLU   B N   1 
ATOM   2832 C  CA  . GLU   B 1 111 ? -0.57700  -26.09100 51.92100  1.000 16.53682 ? 155 GLU   B CA  1 
ATOM   2833 C  C   . GLU   B 1 111 ? 0.29700   -27.25700 51.47300  1.000 17.48682 ? 155 GLU   B C   1 
ATOM   2834 O  O   . GLU   B 1 111 ? 0.57800   -28.14800 52.28200  1.000 20.46682 ? 155 GLU   B O   1 
ATOM   2835 C  CB  . GLU   B 1 111 ? -2.04400  -26.42400 51.64200  1.000 21.37682 ? 155 GLU   B CB  1 
ATOM   2836 C  CG  . GLU   B 1 111 ? -3.01200  -25.40200 52.22100  1.000 20.80682 ? 155 GLU   B CG  1 
ATOM   2837 C  CD  . GLU   B 1 111 ? -4.45700  -25.75700 51.96000  1.000 39.30682 ? 155 GLU   B CD  1 
ATOM   2838 O  OE1 . GLU   B 1 111 ? -4.75300  -26.28300 50.86300  1.000 42.42682 ? 155 GLU   B OE1 1 
ATOM   2839 O  OE2 . GLU   B 1 111 ? -5.29800  -25.51700 52.85500  1.000 52.03682 ? 155 GLU   B OE2 1 
ATOM   2840 N  N   . ARG   B 1 112 ? 0.72800   -27.29400 50.20600  1.000 15.49682 ? 156 ARG   B N   1 
ATOM   2841 C  CA  . ARG   B 1 112 ? 1.28900   -28.51500 49.64400  1.000 15.25682 ? 156 ARG   B CA  1 
ATOM   2842 C  C   . ARG   B 1 112 ? 2.64400   -28.37400 48.95700  1.000 16.88682 ? 156 ARG   B C   1 
ATOM   2843 O  O   . ARG   B 1 112 ? 3.19300   -29.39500 48.53100  1.000 13.79682 ? 156 ARG   B O   1 
ATOM   2844 C  CB  . ARG   B 1 112 ? 0.29500   -29.13500 48.64600  1.000 11.68682 ? 156 ARG   B CB  1 
ATOM   2845 C  CG  . ARG   B 1 112 ? -0.93900  -29.73900 49.30600  1.000 16.95682 ? 156 ARG   B CG  1 
ATOM   2846 C  CD  . ARG   B 1 112 ? -1.91800  -30.29700 48.27500  1.000 24.59682 ? 156 ARG   B CD  1 
ATOM   2847 N  NE  . ARG   B 1 112 ? -2.51200  -29.24100 47.46300  1.000 23.00682 ? 156 ARG   B NE  1 
ATOM   2848 C  CZ  . ARG   B 1 112 ? -3.49200  -28.45200 47.88100  1.000 22.69682 ? 156 ARG   B CZ  1 
ATOM   2849 N  NH1 . ARG   B 1 112 ? -4.00700  -28.58000 49.09100  1.000 27.37682 ? 156 ARG   B NH1 1 
ATOM   2850 N  NH2 . ARG   B 1 112 ? -3.96700  -27.51300 47.06300  1.000 22.92682 ? 156 ARG   B NH2 1 
ATOM   2851 N  N   . SER   B 1 113 ? 3.19200   -27.16300 48.81700  1.000 12.85682 ? 157 SER   B N   1 
ATOM   2852 C  CA  . SER   B 1 113 ? 4.45100   -26.98500 48.10200  1.000 11.63682 ? 157 SER   B CA  1 
ATOM   2853 C  C   . SER   B 1 113 ? 5.63100   -27.53400 48.91000  1.000 15.39682 ? 157 SER   B C   1 
ATOM   2854 O  O   . SER   B 1 113 ? 5.51800   -27.86600 50.09300  1.000 12.02682 ? 157 SER   B O   1 
ATOM   2855 C  CB  . SER   B 1 113 ? 4.70500   -25.50400 47.79800  1.000 12.83682 ? 157 SER   B CB  1 
ATOM   2856 O  OG  . SER   B 1 113 ? 4.84100   -24.76000 49.00700  1.000 14.67682 ? 157 SER   B OG  1 
ATOM   2857 N  N   . ASP   B 1 114 ? 6.78800   -27.59400 48.24700  1.000 17.28682 ? 158 ASP   B N   1 
ATOM   2858 C  CA  . ASP   B 1 114 ? 8.01800   -28.08100 48.86600  1.000 17.41682 ? 158 ASP   B CA  1 
ATOM   2859 C  C   . ASP   B 1 114 ? 8.33700   -27.30600 50.15000  1.000 18.90682 ? 158 ASP   B C   1 
ATOM   2860 O  O   . ASP   B 1 114 ? 8.02000   -26.11800 50.28800  1.000 14.87682 ? 158 ASP   B O   1 
ATOM   2861 C  CB  . ASP   B 1 114 ? 9.17600   -27.97300 47.86000  1.000 18.06682 ? 158 ASP   B CB  1 
ATOM   2862 C  CG  . ASP   B 1 114 ? 10.49100  -28.53000 48.39900  1.000 20.08682 ? 158 ASP   B CG  1 
ATOM   2863 O  OD1 . ASP   B 1 114 ? 10.71900  -29.75900 48.32000  1.000 19.33682 ? 158 ASP   B OD1 1 
ATOM   2864 O  OD2 . ASP   B 1 114 ? 11.30500  -27.73600 48.90400  1.000 21.67682 ? 158 ASP   B OD2 1 
ATOM   2865 N  N   . ARG   B 1 115 ? 8.97500   -27.99700 51.10700  1.000 15.65682 ? 159 ARG   B N   1 
ATOM   2866 C  CA  . ARG   B 1 115 ? 9.26800   -27.37000 52.39500  1.000 15.71682 ? 159 ARG   B CA  1 
ATOM   2867 C  C   . ARG   B 1 115 ? 10.12700  -26.12000 52.24600  1.000 14.18682 ? 159 ARG   B C   1 
ATOM   2868 O  O   . ARG   B 1 115 ? 9.97900   -25.17800 53.02800  1.000 12.20682 ? 159 ARG   B O   1 
ATOM   2869 C  CB  . ARG   B 1 115 ? 9.95600   -28.35700 53.33300  1.000 16.77682 ? 159 ARG   B CB  1 
ATOM   2870 C  CG  . ARG   B 1 115 ? 10.20400  -27.78000 54.71700  1.000 16.77682 ? 159 ARG   B CG  1 
ATOM   2871 C  CD  . ARG   B 1 115 ? 10.72200  -28.81900 55.67400  1.000 19.49682 ? 159 ARG   B CD  1 
ATOM   2872 N  NE  . ARG   B 1 115 ? 11.39400  -28.18200 56.79800  1.000 12.70682 ? 159 ARG   B NE  1 
ATOM   2873 C  CZ  . ARG   B 1 115 ? 12.06600  -28.83600 57.73000  1.000 13.46682 ? 159 ARG   B CZ  1 
ATOM   2874 N  NH1 . ARG   B 1 115 ? 12.10600  -30.16000 57.74800  1.000 14.01682 ? 159 ARG   B NH1 1 
ATOM   2875 N  NH2 . ARG   B 1 115 ? 12.73300  -28.14400 58.65400  1.000 12.87682 ? 159 ARG   B NH2 1 
ATOM   2876 N  N   . LYS   B 1 116 ? 11.02500  -26.09200 51.26100  1.000 10.57682 ? 160 LYS   B N   1 
ATOM   2877 C  CA  . LYS   B 1 116 ? 11.84200  -24.90100 51.03700  1.000 16.48682 ? 160 LYS   B CA  1 
ATOM   2878 C  C   . LYS   B 1 116 ? 10.97800  -23.68600 50.70000  1.000 13.27682 ? 160 LYS   B C   1 
ATOM   2879 O  O   . LYS   B 1 116 ? 11.27200  -22.57100 51.14600  1.000 13.49682 ? 160 LYS   B O   1 
ATOM   2880 C  CB  . LYS   B 1 116 ? 12.86400  -25.16900 49.93300  1.000 15.06682 ? 160 LYS   B CB  1 
ATOM   2881 C  CG  . LYS   B 1 116 ? 13.93000  -26.19700 50.31800  1.000 16.45682 ? 160 LYS   B CG  1 
ATOM   2882 C  CD  . LYS   B 1 116 ? 14.97700  -26.36100 49.23100  1.000 17.28682 ? 160 LYS   B CD  1 
ATOM   2883 C  CE  . LYS   B 1 116 ? 14.38600  -26.99800 47.97900  1.000 19.00682 ? 160 LYS   B CE  1 
ATOM   2884 N  NZ  . LYS   B 1 116 ? 13.83700  -28.35700 48.27300  1.000 22.67682 ? 160 LYS   B NZ  1 
ATOM   2885 N  N   . VAL   B 1 117 ? 9.89100   -23.88600 49.94300  1.000 13.59682 ? 161 VAL   B N   1 
ATOM   2886 C  CA  . VAL   B 1 117 ? 8.99000   -22.77600 49.62200  1.000 9.23682  ? 161 VAL   B CA  1 
ATOM   2887 C  C   . VAL   B 1 117 ? 8.17100   -22.38300 50.84700  1.000 12.02682 ? 161 VAL   B C   1 
ATOM   2888 O  O   . VAL   B 1 117 ? 8.10300   -21.20300 51.21700  1.000 13.14682 ? 161 VAL   B O   1 
ATOM   2889 C  CB  . VAL   B 1 117 ? 8.07500   -23.13500 48.44000  1.000 9.66682  ? 161 VAL   B CB  1 
ATOM   2890 C  CG1 . VAL   B 1 117 ? 7.11400   -21.97900 48.16300  1.000 8.94682  ? 161 VAL   B CG1 1 
ATOM   2891 C  CG2 . VAL   B 1 117 ? 8.90000   -23.47200 47.20100  1.000 13.79682 ? 161 VAL   B CG2 1 
ATOM   2892 N  N   . ARG   B 1 118 ? 7.55700   -23.37100 51.50700  1.000 11.28682 ? 162 ARG   B N   1 
ATOM   2893 C  CA  . ARG   B 1 118 ? 6.63500   -23.07900 52.60300  1.000 13.11682 ? 162 ARG   B CA  1 
ATOM   2894 C  C   . ARG   B 1 118 ? 7.33600   -22.38300 53.76600  1.000 16.49682 ? 162 ARG   B C   1 
ATOM   2895 O  O   . ARG   B 1 118 ? 6.74700   -21.50900 54.41400  1.000 17.50682 ? 162 ARG   B O   1 
ATOM   2896 C  CB  . ARG   B 1 118 ? 5.94800   -24.36800 53.07700  1.000 15.47682 ? 162 ARG   B CB  1 
ATOM   2897 C  CG  . ARG   B 1 118 ? 4.64100   -24.67400 52.34100  1.000 20.74682 ? 162 ARG   B CG  1 
ATOM   2898 C  CD  . ARG   B 1 118 ? 3.92000   -25.92900 52.86900  1.000 16.96682 ? 162 ARG   B CD  1 
ATOM   2899 N  NE  . ARG   B 1 118 ? 4.77000   -27.11400 52.81900  1.000 19.18682 ? 162 ARG   B NE  1 
ATOM   2900 C  CZ  . ARG   B 1 118 ? 5.20800   -27.77100 53.88600  1.000 22.06682 ? 162 ARG   B CZ  1 
ATOM   2901 N  NH1 . ARG   B 1 118 ? 4.82100   -27.43900 55.10700  1.000 20.20682 ? 162 ARG   B NH1 1 
ATOM   2902 N  NH2 . ARG   B 1 118 ? 6.05200   -28.79000 53.72400  1.000 20.77682 ? 162 ARG   B NH2 1 
ATOM   2903 N  N   . GLU   B 1 119 ? 8.59200   -22.75400 54.04800  1.000 13.54682 ? 163 GLU   B N   1 
ATOM   2904 C  CA  A GLU   B 1 119 ? 9.31600   -22.15700 55.16300  0.500 14.91682 ? 163 GLU   B CA  1 
ATOM   2905 C  CA  B GLU   B 1 119 ? 9.33500   -22.16400 55.15700  0.500 14.90682 ? 163 GLU   B CA  1 
ATOM   2906 C  C   . GLU   B 1 119 ? 9.78000   -20.73500 54.87500  1.000 18.39682 ? 163 GLU   B C   1 
ATOM   2907 O  O   . GLU   B 1 119 ? 10.20900  -20.04400 55.80700  1.000 14.35682 ? 163 GLU   B O   1 
ATOM   2908 C  CB  A GLU   B 1 119 ? 10.51500  -23.03300 55.54200  0.500 14.40682 ? 163 GLU   B CB  1 
ATOM   2909 C  CB  B GLU   B 1 119 ? 10.55600  -23.03000 55.49800  0.500 14.43682 ? 163 GLU   B CB  1 
ATOM   2910 C  CG  A GLU   B 1 119 ? 10.53900  -23.40800 57.01800  0.500 14.12682 ? 163 GLU   B CG  1 
ATOM   2911 C  CG  B GLU   B 1 119 ? 11.68500  -22.96800 54.47900  0.500 15.21682 ? 163 GLU   B CG  1 
ATOM   2912 C  CD  A GLU   B 1 119 ? 11.40900  -24.62400 57.31600  0.500 17.42682 ? 163 GLU   B CD  1 
ATOM   2913 C  CD  B GLU   B 1 119 ? 12.76600  -24.01700 54.71900  0.500 16.14682 ? 163 GLU   B CD  1 
ATOM   2914 O  OE1 A GLU   B 1 119 ? 12.42300  -24.84000 56.61800  0.500 20.44682 ? 163 GLU   B OE1 1 
ATOM   2915 O  OE1 B GLU   B 1 119 ? 12.81600  -24.59700 55.82100  0.500 19.93682 ? 163 GLU   B OE1 1 
ATOM   2916 O  OE2 A GLU   B 1 119 ? 11.06800  -25.37000 58.24800  0.500 12.70682 ? 163 GLU   B OE2 1 
ATOM   2917 O  OE2 B GLU   B 1 119 ? 13.56800  -24.26000 53.80200  0.500 11.87682 ? 163 GLU   B OE2 1 
ATOM   2918 N  N   . ARG   B 1 120 ? 9.69300   -20.28700 53.62300  1.000 14.88682 ? 164 ARG   B N   1 
ATOM   2919 C  CA  . ARG   B 1 120 ? 10.02100  -18.92300 53.22200  1.000 17.45682 ? 164 ARG   B CA  1 
ATOM   2920 C  C   . ARG   B 1 120 ? 8.78200   -18.07500 52.96500  1.000 16.58682 ? 164 ARG   B C   1 
ATOM   2921 O  O   . ARG   B 1 120 ? 8.91200   -16.90400 52.58600  1.000 16.72682 ? 164 ARG   B O   1 
ATOM   2922 C  CB  . ARG   B 1 120 ? 10.89300  -18.94500 51.96300  1.000 15.61682 ? 164 ARG   B CB  1 
ATOM   2923 C  CG  . ARG   B 1 120 ? 12.29600  -19.49100 52.19900  1.000 14.08682 ? 164 ARG   B CG  1 
ATOM   2924 C  CD  . ARG   B 1 120 ? 13.01400  -19.75900 50.89700  1.000 17.57682 ? 164 ARG   B CD  1 
ATOM   2925 N  NE  . ARG   B 1 120 ? 14.44300  -19.96700 51.10800  1.000 17.10682 ? 164 ARG   B NE  1 
ATOM   2926 C  CZ  . ARG   B 1 120 ? 14.97200  -21.10800 51.52500  1.000 20.89682 ? 164 ARG   B CZ  1 
ATOM   2927 N  NH1 . ARG   B 1 120 ? 14.21300  -22.15800 51.81400  1.000 16.50682 ? 164 ARG   B NH1 1 
ATOM   2928 N  NH2 . ARG   B 1 120 ? 16.29000  -21.19800 51.66000  1.000 19.96682 ? 164 ARG   B NH2 1 
ATOM   2929 N  N   . LEU   B 1 121 ? 7.58900   -18.63800 53.15900  1.000 15.66682 ? 165 LEU   B N   1 
ATOM   2930 C  CA  . LEU   B 1 121 ? 6.33400   -18.02600 52.73800  1.000 17.00682 ? 165 LEU   B CA  1 
ATOM   2931 C  C   . LEU   B 1 121 ? 5.55700   -17.51200 53.94400  1.000 16.50682 ? 165 LEU   B C   1 
ATOM   2932 O  O   . LEU   B 1 121 ? 5.39100   -18.22700 54.93700  1.000 17.28682 ? 165 LEU   B O   1 
ATOM   2933 C  CB  . LEU   B 1 121 ? 5.47900   -19.02900 51.95600  1.000 12.63682 ? 165 LEU   B CB  1 
ATOM   2934 C  CG  . LEU   B 1 121 ? 4.04400   -18.63000 51.60100  1.000 11.00682 ? 165 LEU   B CG  1 
ATOM   2935 C  CD1 . LEU   B 1 121 ? 4.03500   -17.49300 50.59100  1.000 13.03682 ? 165 LEU   B CD1 1 
ATOM   2936 C  CD2 . LEU   B 1 121 ? 3.24400   -19.83800 51.08700  1.000 14.21682 ? 165 LEU   B CD2 1 
ATOM   2937 N  N   . ASP   B 1 122 ? 5.07400   -16.27500 53.84500  1.000 13.79682 ? 166 ASP   B N   1 
ATOM   2938 C  CA  . ASP   B 1 122 ? 4.09300   -15.75300 54.78500  1.000 14.91682 ? 166 ASP   B CA  1 
ATOM   2939 C  C   . ASP   B 1 122 ? 2.72200   -16.00600 54.17200  1.000 18.51682 ? 166 ASP   B C   1 
ATOM   2940 O  O   . ASP   B 1 122 ? 2.35700   -15.32600 53.19900  1.000 15.03682 ? 166 ASP   B O   1 
ATOM   2941 C  CB  . ASP   B 1 122 ? 4.31500   -14.26400 55.03100  1.000 14.11682 ? 166 ASP   B CB  1 
ATOM   2942 C  CG  . ASP   B 1 122 ? 3.37300   -13.67800 56.08000  1.000 12.80682 ? 166 ASP   B CG  1 
ATOM   2943 O  OD1 . ASP   B 1 122 ? 2.29600   -14.25400 56.36600  1.000 15.16682 ? 166 ASP   B OD1 1 
ATOM   2944 O  OD2 . ASP   B 1 122 ? 3.69900   -12.60000 56.60300  1.000 11.96682 ? 166 ASP   B OD2 1 
ATOM   2945 N  N   . PRO   B 1 123 ? 1.93700   -16.95900 54.68300  1.000 17.26682 ? 167 PRO   B N   1 
ATOM   2946 C  CA  . PRO   B 1 123 ? 0.65800   -17.28500 54.03400  1.000 15.12682 ? 167 PRO   B CA  1 
ATOM   2947 C  C   . PRO   B 1 123 ? -0.39500  -16.18700 54.14300  1.000 12.77682 ? 167 PRO   B C   1 
ATOM   2948 O  O   . PRO   B 1 123 ? -1.44700  -16.30700 53.50900  1.000 17.51682 ? 167 PRO   B O   1 
ATOM   2949 C  CB  . PRO   B 1 123 ? 0.21600   -18.55800 54.76500  1.000 22.32682 ? 167 PRO   B CB  1 
ATOM   2950 C  CG  . PRO   B 1 123 ? 0.80100   -18.42000 56.12600  1.000 19.91682 ? 167 PRO   B CG  1 
ATOM   2951 C  CD  . PRO   B 1 123 ? 2.10900   -17.66600 55.96500  1.000 17.33682 ? 167 PRO   B CD  1 
ATOM   2952 N  N   . ASN   B 1 124 ? -0.15100  -15.12300 54.90400  1.000 15.94682 ? 168 ASN   B N   1 
ATOM   2953 C  CA  . ASN   B 1 124 ? -1.12000  -14.03800 55.02700  1.000 16.79682 ? 168 ASN   B CA  1 
ATOM   2954 C  C   . ASN   B 1 124 ? -0.96300  -12.96000 53.96000  1.000 12.47682 ? 168 ASN   B C   1 
ATOM   2955 O  O   . ASN   B 1 124 ? -1.81400  -12.07100 53.87500  1.000 15.82682 ? 168 ASN   B O   1 
ATOM   2956 C  CB  . ASN   B 1 124 ? -1.01000  -13.36500 56.40200  1.000 19.66682 ? 168 ASN   B CB  1 
ATOM   2957 C  CG  . ASN   B 1 124 ? -1.21800  -14.33200 57.55000  1.000 27.21682 ? 168 ASN   B CG  1 
ATOM   2958 O  OD1 . ASN   B 1 124 ? -2.09000  -15.19900 57.49900  1.000 28.66682 ? 168 ASN   B OD1 1 
ATOM   2959 N  ND2 . ASN   B 1 124 ? -0.41200  -14.18500 58.59800  1.000 32.93682 ? 168 ASN   B ND2 1 
ATOM   2960 N  N   . ARG   B 1 125 ? 0.09400   -12.99700 53.15400  1.000 12.16682 ? 169 ARG   B N   1 
ATOM   2961 C  CA  . ARG   B 1 125 ? 0.40500   -11.88800 52.24900  1.000 12.68682 ? 169 ARG   B CA  1 
ATOM   2962 C  C   . ARG   B 1 125 ? 0.50500   -12.40000 50.80800  1.000 12.13682 ? 169 ARG   B C   1 
ATOM   2963 O  O   . ARG   B 1 125 ? 1.59400   -12.71200 50.31500  1.000 10.27682 ? 169 ARG   B O   1 
ATOM   2964 C  CB  . ARG   B 1 125 ? 1.67300   -11.19700 52.71800  1.000 11.99682 ? 169 ARG   B CB  1 
ATOM   2965 C  CG  . ARG   B 1 125 ? 1.55800   -10.74300 54.17100  1.000 11.33682 ? 169 ARG   B CG  1 
ATOM   2966 C  CD  . ARG   B 1 125 ? 2.66500   -9.77200  54.58800  1.000 12.15682 ? 169 ARG   B CD  1 
ATOM   2967 N  NE  . ARG   B 1 125 ? 3.94900   -10.43800 54.74800  1.000 9.14682  ? 169 ARG   B NE  1 
ATOM   2968 C  CZ  . ARG   B 1 125 ? 5.02800   -10.17400 54.02600  1.000 12.04682 ? 169 ARG   B CZ  1 
ATOM   2969 N  NH1 . ARG   B 1 125 ? 5.01100   -9.26400  53.06200  1.000 10.66682 ? 169 ARG   B NH1 1 
ATOM   2970 N  NH2 . ARG   B 1 125 ? 6.15500   -10.83800 54.27900  1.000 11.85682 ? 169 ARG   B NH2 1 
ATOM   2971 N  N   . LEU   B 1 126 ? -0.64300  -12.45700 50.12600  1.000 8.89682  ? 170 LEU   B N   1 
ATOM   2972 C  CA  . LEU   B 1 126 ? -0.76000  -13.07900 48.81200  1.000 10.15682 ? 170 LEU   B CA  1 
ATOM   2973 C  C   . LEU   B 1 126 ? -1.32400  -12.10100 47.79000  1.000 9.16682  ? 170 LEU   B C   1 
ATOM   2974 O  O   . LEU   B 1 126 ? -2.05500  -11.16800 48.13600  1.000 13.60682 ? 170 LEU   B O   1 
ATOM   2975 C  CB  . LEU   B 1 126 ? -1.64800  -14.33100 48.87400  1.000 10.29682 ? 170 LEU   B CB  1 
ATOM   2976 C  CG  . LEU   B 1 126 ? -1.26900  -15.34600 49.95900  1.000 13.50682 ? 170 LEU   B CG  1 
ATOM   2977 C  CD1 . LEU   B 1 126 ? -2.31400  -16.46500 50.06100  1.000 14.80682 ? 170 LEU   B CD1 1 
ATOM   2978 C  CD2 . LEU   B 1 126 ? 0.09800   -15.91800 49.70800  1.000 13.36682 ? 170 LEU   B CD2 1 
ATOM   2979 N  N   . ALA   B 1 127 ? -0.99400  -12.33500 46.51800  1.000 8.96682  ? 171 ALA   B N   1 
ATOM   2980 C  CA  . ALA   B 1 127 ? -1.40600  -11.43900 45.44500  1.000 9.22682  ? 171 ALA   B CA  1 
ATOM   2981 C  C   . ALA   B 1 127 ? -1.55100  -12.22300 44.14700  1.000 9.19682  ? 171 ALA   B C   1 
ATOM   2982 O  O   . ALA   B 1 127 ? -1.07600  -13.35700 44.02400  1.000 8.12682  ? 171 ALA   B O   1 
ATOM   2983 C  CB  . ALA   B 1 127 ? -0.40800  -10.28400 45.26700  1.000 9.26682  ? 171 ALA   B CB  1 
ATOM   2984 N  N   . VAL   B 1 128 ? -2.19300  -11.58300 43.16300  1.000 9.08682  ? 172 VAL   B N   1 
ATOM   2985 C  CA  . VAL   B 1 128 ? -2.43000  -12.16800 41.85100  1.000 7.77682  ? 172 VAL   B CA  1 
ATOM   2986 C  C   . VAL   B 1 128 ? -2.04000  -11.17300 40.77000  1.000 7.93682  ? 172 VAL   B C   1 
ATOM   2987 O  O   . VAL   B 1 128 ? -2.11400  -9.95500  40.95700  1.000 9.62682  ? 172 VAL   B O   1 
ATOM   2988 C  CB  . VAL   B 1 128 ? -3.90200  -12.60300 41.65600  1.000 9.28682  ? 172 VAL   B CB  1 
ATOM   2989 C  CG1 . VAL   B 1 128 ? -4.23500  -13.78000 42.58000  1.000 10.11682 ? 172 VAL   B CG1 1 
ATOM   2990 C  CG2 . VAL   B 1 128 ? -4.84600  -11.41500 41.93600  1.000 8.62682  ? 172 VAL   B CG2 1 
ATOM   2991 N  N   . MET   B 1 129 ? -1.66200  -11.71600 39.61800  1.000 9.87682  ? 173 MET   B N   1 
ATOM   2992 C  CA  . MET   B 1 129 ? -1.25800  -10.98200 38.43000  1.000 5.61682  ? 173 MET   B CA  1 
ATOM   2993 C  C   . MET   B 1 129 ? -1.58700  -11.86000 37.23100  1.000 8.55682  ? 173 MET   B C   1 
ATOM   2994 O  O   . MET   B 1 129 ? -1.58700  -13.08400 37.33800  1.000 11.16682 ? 173 MET   B O   1 
ATOM   2995 C  CB  . MET   B 1 129 ? 0.24500   -10.64300 38.46300  1.000 10.86682 ? 173 MET   B CB  1 
ATOM   2996 C  CG  . MET   B 1 129 ? 0.77600   -9.89500  37.23300  1.000 7.15682  ? 173 MET   B CG  1 
ATOM   2997 S  SD  . MET   B 1 129 ? 2.34800   -9.05200  37.56100  1.000 12.99682 ? 173 MET   B SD  1 
ATOM   2998 C  CE  . MET   B 1 129 ? 3.47600   -10.44200 37.66900  1.000 12.05682 ? 173 MET   B CE  1 
ATOM   2999 N  N   . GLY   B 1 130 ? -1.87700  -11.23700 36.09000  1.000 7.60682  ? 174 GLY   B N   1 
ATOM   3000 C  CA  . GLY   B 1 130 ? -2.22400  -12.01900 34.91600  1.000 8.68682  ? 174 GLY   B CA  1 
ATOM   3001 C  C   . GLY   B 1 130 ? -2.32100  -11.22100 33.63300  1.000 9.62682  ? 174 GLY   B C   1 
ATOM   3002 O  O   . GLY   B 1 130 ? -2.59700  -10.01400 33.65100  1.000 7.01682  ? 174 GLY   B O   1 
ATOM   3003 N  N   . HIS   B 1 131 ? -2.06500  -11.89200 32.51000  1.000 10.45682 ? 175 HIS   B N   1 
ATOM   3004 C  CA  . HIS   B 1 131 ? -2.05700  -11.27600 31.19100  1.000 10.30682 ? 175 HIS   B CA  1 
ATOM   3005 C  C   . HIS   B 1 131 ? -3.33400  -11.63000 30.44200  1.000 9.33682  ? 175 HIS   B C   1 
ATOM   3006 O  O   . HIS   B 1 131 ? -3.72100  -12.80800 30.39600  1.000 10.27682 ? 175 HIS   B O   1 
ATOM   3007 C  CB  . HIS   B 1 131 ? -0.84100  -11.74600 30.38400  1.000 9.45682  ? 175 HIS   B CB  1 
ATOM   3008 C  CG  . HIS   B 1 131 ? -0.80800  -11.21900 28.98400  1.000 11.74682 ? 175 HIS   B CG  1 
ATOM   3009 N  ND1 . HIS   B 1 131 ? -0.62700  -12.02900 27.88600  1.000 11.19682 ? 175 HIS   B ND1 1 
ATOM   3010 C  CD2 . HIS   B 1 131 ? -0.94600  -9.96100  28.50300  1.000 11.01682 ? 175 HIS   B CD2 1 
ATOM   3011 C  CE1 . HIS   B 1 131 ? -0.64200  -11.29300 26.79000  1.000 12.79682 ? 175 HIS   B CE1 1 
ATOM   3012 N  NE2 . HIS   B 1 131 ? -0.83400  -10.03200 27.13700  1.000 9.16682  ? 175 HIS   B NE2 1 
ATOM   3013 N  N   . ALA   B 1 132 ? -3.96500  -10.61500 29.84100  1.000 8.75682  ? 176 ALA   B N   1 
ATOM   3014 C  CA  . ALA   B 1 132 ? -5.06400  -10.80800 28.89600  1.000 9.99682  ? 176 ALA   B CA  1 
ATOM   3015 C  C   . ALA   B 1 132 ? -6.26500  -11.44600 29.59700  1.000 8.25682  ? 176 ALA   B C   1 
ATOM   3016 O  O   . ALA   B 1 132 ? -6.75000  -10.89300 30.58500  1.000 9.30682  ? 176 ALA   B O   1 
ATOM   3017 C  CB  . ALA   B 1 132 ? -4.58600  -11.63200 27.70200  1.000 11.69682 ? 176 ALA   B CB  1 
ATOM   3018 N  N   . MET   B 1 133 ? -6.76900  -12.59100 29.11400  1.000 9.10682  ? 177 MET   B N   1 
ATOM   3019 C  CA  . MET   B 1 133 ? -7.80600  -13.29800 29.87300  1.000 9.84682  ? 177 MET   B CA  1 
ATOM   3020 C  C   . MET   B 1 133 ? -7.34800  -13.60100 31.28900  1.000 10.81682 ? 177 MET   B C   1 
ATOM   3021 O  O   . MET   B 1 133 ? -8.16800  -13.61300 32.22000  1.000 10.70682 ? 177 MET   B O   1 
ATOM   3022 C  CB  . MET   B 1 133 ? -8.20100  -14.59400 29.18300  1.000 11.04682 ? 177 MET   B CB  1 
ATOM   3023 C  CG  . MET   B 1 133 ? -9.34000  -14.42700 28.21400  1.000 14.67682 ? 177 MET   B CG  1 
ATOM   3024 S  SD  . MET   B 1 133 ? -10.08600 -16.00900 27.76900  1.000 15.39682 ? 177 MET   B SD  1 
ATOM   3025 C  CE  . MET   B 1 133 ? -10.88600 -15.48500 26.25100  1.000 14.48682 ? 177 MET   B CE  1 
ATOM   3026 N  N   . GLY   B 1 134 ? -6.04400  -13.83800 31.46900  1.000 6.77682  ? 178 GLY   B N   1 
ATOM   3027 C  CA  . GLY   B 1 134 ? -5.50500  -13.99900 32.80700  1.000 10.11682 ? 178 GLY   B CA  1 
ATOM   3028 C  C   . GLY   B 1 134 ? -5.58000  -12.73000 33.62800  1.000 10.01682 ? 178 GLY   B C   1 
ATOM   3029 O  O   . GLY   B 1 134 ? -5.61000  -12.78800 34.86000  1.000 10.24682 ? 178 GLY   B O   1 
ATOM   3030 N  N   . GLY   B 1 135 ? -5.59400  -11.57100 32.96400  1.000 8.53682  ? 179 GLY   B N   1 
ATOM   3031 C  CA  . GLY   B 1 135 ? -5.81500  -10.31800 33.67100  1.000 10.51682 ? 179 GLY   B CA  1 
ATOM   3032 C  C   . GLY   B 1 135 ? -7.26100  -10.15800 34.10900  1.000 9.87682  ? 179 GLY   B C   1 
ATOM   3033 O  O   . GLY   B 1 135 ? -7.54000  -9.67100  35.20800  1.000 10.19682 ? 179 GLY   B O   1 
ATOM   3034 N  N   . GLY   B 1 136 ? -8.20200  -10.57200 33.25800  1.000 7.84682  ? 180 GLY   B N   1 
ATOM   3035 C  CA  . GLY   B 1 136 ? -9.56500  -10.74300 33.72600  1.000 11.51682 ? 180 GLY   B CA  1 
ATOM   3036 C  C   . GLY   B 1 136 ? -9.63400  -11.71200 34.88800  1.000 10.45682 ? 180 GLY   B C   1 
ATOM   3037 O  O   . GLY   B 1 136 ? -10.39800 -11.50800 35.84000  1.000 9.95682  ? 180 GLY   B O   1 
ATOM   3038 N  N   . GLY   B 1 137 ? -8.81500  -12.77100 34.83300  1.000 9.80682  ? 181 GLY   B N   1 
ATOM   3039 C  CA  . GLY   B 1 137 ? -8.72500  -13.70500 35.95000  1.000 8.78682  ? 181 GLY   B CA  1 
ATOM   3040 C  C   . GLY   B 1 137 ? -8.22300  -13.06000 37.23000  1.000 11.29682 ? 181 GLY   B C   1 
ATOM   3041 O  O   . GLY   B 1 137 ? -8.67200  -13.40800 38.32900  1.000 9.92682  ? 181 GLY   B O   1 
ATOM   3042 N  N   . SER   B 1 138 ? -7.27700  -12.11500 37.11000  1.000 8.36682  ? 182 SER   B N   1 
ATOM   3043 C  CA  . SER   B 1 138 ? -6.79400  -11.39200 38.28700  1.000 6.43682  ? 182 SER   B CA  1 
ATOM   3044 C  C   . SER   B 1 138 ? -7.92400  -10.58800 38.92800  1.000 11.28682 ? 182 SER   B C   1 
ATOM   3045 O  O   . SER   B 1 138 ? -8.09900  -10.60100 40.15800  1.000 8.46682  ? 182 SER   B O   1 
ATOM   3046 C  CB  . SER   B 1 138 ? -5.62100  -10.48500 37.88200  1.000 12.47682 ? 182 SER   B CB  1 
ATOM   3047 O  OG  . SER   B 1 138 ? -4.86000  -10.04100 38.99800  1.000 13.42682 ? 182 SER   B OG  1 
ATOM   3048 N  N   . LEU   B 1 139 ? -8.71500  -9.89700  38.10000  1.000 8.10682  ? 183 LEU   B N   1 
ATOM   3049 C  CA  . LEU   B 1 139 ? -9.89800  -9.19200  38.58300  1.000 8.19682  ? 183 LEU   B CA  1 
ATOM   3050 C  C   . LEU   B 1 139 ? -10.86000 -10.14900 39.28100  1.000 8.73682  ? 183 LEU   B C   1 
ATOM   3051 O  O   . LEU   B 1 139 ? -11.32000 -9.88100  40.40200  1.000 8.56682  ? 183 LEU   B O   1 
ATOM   3052 C  CB  . LEU   B 1 139 ? -10.59500 -8.49200  37.40600  1.000 6.55682  ? 183 LEU   B CB  1 
ATOM   3053 C  CG  . LEU   B 1 139 ? -9.90500  -7.29500  36.73100  1.000 9.43682  ? 183 LEU   B CG  1 
ATOM   3054 C  CD1 . LEU   B 1 139 ? -10.52400 -6.95100  35.36700  1.000 6.57682  ? 183 LEU   B CD1 1 
ATOM   3055 C  CD2 . LEU   B 1 139 ? -9.93600  -6.08000  37.65400  1.000 8.91682  ? 183 LEU   B CD2 1 
ATOM   3056 N  N   . GLU   B 1 140 ? -11.15700 -11.28200 38.63600  1.000 7.67682  ? 184 GLU   B N   1 
ATOM   3057 C  CA  . GLU   B 1 140 ? -12.08700 -12.26500 39.20000  1.000 10.10682 ? 184 GLU   B CA  1 
ATOM   3058 C  C   . GLU   B 1 140 ? -11.60900 -12.78500 40.55300  1.000 11.49682 ? 184 GLU   B C   1 
ATOM   3059 O  O   . GLU   B 1 140 ? -12.41500 -12.97900 41.47100  1.000 7.48682  ? 184 GLU   B O   1 
ATOM   3060 C  CB  . GLU   B 1 140 ? -12.26000 -13.44200 38.24500  1.000 11.23682 ? 184 GLU   B CB  1 
ATOM   3061 C  CG  . GLU   B 1 140 ? -13.03000 -13.15100 36.97800  1.000 16.78682 ? 184 GLU   B CG  1 
ATOM   3062 C  CD  . GLU   B 1 140 ? -14.49100 -13.55900 37.09300  1.000 20.82682 ? 184 GLU   B CD  1 
ATOM   3063 O  OE1 . GLU   B 1 140 ? -14.91500 -13.95200 38.19900  1.000 23.20682 ? 184 GLU   B OE1 1 
ATOM   3064 O  OE2 . GLU   B 1 140 ? -15.20900 -13.48700 36.07800  1.000 21.93682 ? 184 GLU   B OE2 1 
ATOM   3065 N  N   . ALA   B 1 141 ? -10.30600 -13.05000 40.68000  1.000 9.63682  ? 185 ALA   B N   1 
ATOM   3066 C  CA  . ALA   B 1 141 ? -9.77500  -13.61900 41.91400  1.000 12.30682 ? 185 ALA   B CA  1 
ATOM   3067 C  C   . ALA   B 1 141 ? -9.97300  -12.67700 43.09600  1.000 10.02682 ? 185 ALA   B C   1 
ATOM   3068 O  O   . ALA   B 1 141 ? -10.23600 -13.12700 44.21500  1.000 9.99682  ? 185 ALA   B O   1 
ATOM   3069 C  CB  . ALA   B 1 141 ? -8.29300  -13.97000 41.74100  1.000 9.90682  ? 185 ALA   B CB  1 
ATOM   3070 N  N   . THR   B 1 142 ? -9.85200  -11.36400 42.87300  1.000 9.80682  ? 186 THR   B N   1 
ATOM   3071 C  CA  . THR   B 1 142 ? -10.01800 -10.43700 43.98600  1.000 8.73682  ? 186 THR   B CA  1 
ATOM   3072 C  C   . THR   B 1 142 ? -11.46600 -10.34500 44.43600  1.000 10.12682 ? 186 THR   B C   1 
ATOM   3073 O  O   . THR   B 1 142 ? -11.72100 -10.12400 45.62600  1.000 14.91682 ? 186 THR   B O   1 
ATOM   3074 C  CB  . THR   B 1 142 ? -9.46500  -9.05500  43.63200  1.000 10.14682 ? 186 THR   B CB  1 
ATOM   3075 O  OG1 . THR   B 1 142 ? -10.20700 -8.47200  42.55500  1.000 9.92682  ? 186 THR   B OG1 1 
ATOM   3076 C  CG2 . THR   B 1 142 ? -8.00300  -9.18800  43.22600  1.000 9.89682  ? 186 THR   B CG2 1 
ATOM   3077 N  N   . VAL   B 1 143 ? -12.42600 -10.52300 43.52200  1.000 9.35682  ? 187 VAL   B N   1 
ATOM   3078 C  CA  . VAL   B 1 143 ? -13.82000 -10.62700 43.94900  1.000 10.52682 ? 187 VAL   B CA  1 
ATOM   3079 C  C   . VAL   B 1 143 ? -14.04300 -11.94400 44.69600  1.000 12.12682 ? 187 VAL   B C   1 
ATOM   3080 O  O   . VAL   B 1 143 ? -14.77000 -11.99200 45.69100  1.000 10.31682 ? 187 VAL   B O   1 
ATOM   3081 C  CB  . VAL   B 1 143 ? -14.76500 -10.48000 42.73800  1.000 11.31682 ? 187 VAL   B CB  1 
ATOM   3082 C  CG1 . VAL   B 1 143 ? -16.22200 -10.49200 43.17200  1.000 10.92682 ? 187 VAL   B CG1 1 
ATOM   3083 C  CG2 . VAL   B 1 143 ? -14.44700 -9.19900  41.96700  1.000 10.51682 ? 187 VAL   B CG2 1 
ATOM   3084 N  N   . MET   B 1 144 ? -13.39800 -13.02300 44.24400  1.000 12.50682 ? 188 MET   B N   1 
ATOM   3085 C  CA  . MET   B 1 144 ? -13.53100 -14.31800 44.91000  1.000 12.02682 ? 188 MET   B CA  1 
ATOM   3086 C  C   . MET   B 1 144 ? -12.83700 -14.34500 46.27200  1.000 14.78682 ? 188 MET   B C   1 
ATOM   3087 O  O   . MET   B 1 144 ? -13.25800 -15.09200 47.16100  1.000 11.97682 ? 188 MET   B O   1 
ATOM   3088 C  CB  . MET   B 1 144 ? -12.97000 -15.43200 44.02200  1.000 12.83682 ? 188 MET   B CB  1 
ATOM   3089 C  CG  . MET   B 1 144 ? -13.72100 -15.67000 42.71900  1.000 13.37682 ? 188 MET   B CG  1 
ATOM   3090 S  SD  . MET   B 1 144 ? -12.87200 -16.83600 41.61800  1.000 20.97682 ? 188 MET   B SD  1 
ATOM   3091 C  CE  . MET   B 1 144 ? -13.88700 -16.69900 40.13900  1.000 18.19682 ? 188 MET   B CE  1 
ATOM   3092 N  N   . ARG   B 1 145 ? -11.77000 -13.56700 46.45900  1.000 11.88682 ? 189 ARG   B N   1 
ATOM   3093 C  CA  . ARG   B 1 145 ? -11.01300 -13.58700 47.71200  1.000 11.25682 ? 189 ARG   B CA  1 
ATOM   3094 C  C   . ARG   B 1 145 ? -10.55500 -12.17800 48.05800  1.000 12.65682 ? 189 ARG   B C   1 
ATOM   3095 O  O   . ARG   B 1 145 ? -9.43400  -11.76800 47.72200  1.000 9.49682  ? 189 ARG   B O   1 
ATOM   3096 C  CB  . ARG   B 1 145 ? -9.82000  -14.54000 47.63300  1.000 12.60682 ? 189 ARG   B CB  1 
ATOM   3097 C  CG  . ARG   B 1 145 ? -9.08400  -14.68000 48.96000  1.000 15.95682 ? 189 ARG   B CG  1 
ATOM   3098 C  CD  . ARG   B 1 145 ? -8.09600  -15.84300 48.96200  1.000 21.13682 ? 189 ARG   B CD  1 
ATOM   3099 N  NE  . ARG   B 1 145 ? -8.73400  -17.13600 48.72800  1.000 18.60682 ? 189 ARG   B NE  1 
ATOM   3100 C  CZ  . ARG   B 1 145 ? -8.06100  -18.26000 48.52200  1.000 21.39682 ? 189 ARG   B CZ  1 
ATOM   3101 N  NH1 . ARG   B 1 145 ? -6.73800  -18.28100 48.52500  1.000 19.64682 ? 189 ARG   B NH1 1 
ATOM   3102 N  NH2 . ARG   B 1 145 ? -8.72900  -19.38500 48.28400  1.000 20.98682 ? 189 ARG   B NH2 1 
ATOM   3103 N  N   . PRO   B 1 146 ? -11.40200 -11.40300 48.74000  1.000 10.17682 ? 190 PRO   B N   1 
ATOM   3104 C  CA  . PRO   B 1 146 ? -11.06200 -9.99900  49.02200  1.000 13.38682 ? 190 PRO   B CA  1 
ATOM   3105 C  C   . PRO   B 1 146 ? -9.88400  -9.80800  49.96900  1.000 14.98682 ? 190 PRO   B C   1 
ATOM   3106 O  O   . PRO   B 1 146 ? -9.42900  -8.66600  50.12300  1.000 13.99682 ? 190 PRO   B O   1 
ATOM   3107 C  CB  . PRO   B 1 146 ? -12.35200 -9.44200  49.63900  1.000 11.45682 ? 190 PRO   B CB  1 
ATOM   3108 C  CG  . PRO   B 1 146 ? -13.43400 -10.34700 49.14700  1.000 10.89682 ? 190 PRO   B CG  1 
ATOM   3109 C  CD  . PRO   B 1 146 ? -12.80500 -11.71300 49.05600  1.000 13.33682 ? 190 PRO   B CD  1 
ATOM   3110 N  N   . SER   B 1 147 ? -9.38700  -10.86600 50.61100  1.000 14.13682 ? 191 SER   B N   1 
ATOM   3111 C  CA  . SER   B 1 147 ? -8.26500  -10.76000 51.53900  1.000 15.89682 ? 191 SER   B CA  1 
ATOM   3112 C  C   . SER   B 1 147 ? -6.91300  -10.70700 50.83500  1.000 15.53682 ? 191 SER   B C   1 
ATOM   3113 O  O   . SER   B 1 147 ? -5.89000  -10.50400 51.50600  1.000 9.40682  ? 191 SER   B O   1 
ATOM   3114 C  CB  . SER   B 1 147 ? -8.28100  -11.94000 52.51700  1.000 14.99682 ? 191 SER   B CB  1 
ATOM   3115 O  OG  . SER   B 1 147 ? -8.18100  -13.17900 51.83000  1.000 13.15682 ? 191 SER   B OG  1 
ATOM   3116 N  N   . LEU   B 1 148 ? -6.88700  -10.89500 49.51100  1.000 12.28682 ? 192 LEU   B N   1 
ATOM   3117 C  CA  . LEU   B 1 148 ? -5.67000  -10.69900 48.73100  1.000 10.51682 ? 192 LEU   B CA  1 
ATOM   3118 C  C   . LEU   B 1 148 ? -5.10500  -9.30000  48.95800  1.000 12.39682 ? 192 LEU   B C   1 
ATOM   3119 O  O   . LEU   B 1 148 ? -5.84300  -8.33500  49.18900  1.000 13.79682 ? 192 LEU   B O   1 
ATOM   3120 C  CB  . LEU   B 1 148 ? -5.96100  -10.91000 47.23700  1.000 10.02682 ? 192 LEU   B CB  1 
ATOM   3121 C  CG  . LEU   B 1 148 ? -6.32500  -12.34200 46.81800  1.000 11.24682 ? 192 LEU   B CG  1 
ATOM   3122 C  CD1 . LEU   B 1 148 ? -6.89100  -12.41800 45.39100  1.000 8.68682  ? 192 LEU   B CD1 1 
ATOM   3123 C  CD2 . LEU   B 1 148 ? -5.11700  -13.25400 46.96400  1.000 11.78682 ? 192 LEU   B CD2 1 
ATOM   3124 N  N   . LYS   B 1 149 ? -3.78000  -9.18600  48.88600  1.000 11.41682 ? 193 LYS   B N   1 
ATOM   3125 C  CA  . LYS   B 1 149 ? -3.12900  -7.90900  49.15000  1.000 10.24682 ? 193 LYS   B CA  1 
ATOM   3126 C  C   . LYS   B 1 149 ? -2.99700  -7.01500  47.91900  1.000 10.61682 ? 193 LYS   B C   1 
ATOM   3127 O  O   . LYS   B 1 149 ? -2.88500  -5.79000  48.06600  1.000 7.35682  ? 193 LYS   B O   1 
ATOM   3128 C  CB  . LYS   B 1 149 ? -1.73500  -8.14200  49.74600  1.000 9.44682  ? 193 LYS   B CB  1 
ATOM   3129 C  CG  . LYS   B 1 149 ? -1.74900  -8.80300  51.13500  1.000 11.97682 ? 193 LYS   B CG  1 
ATOM   3130 C  CD  . LYS   B 1 149 ? -2.52700  -7.97200  52.14600  1.000 14.38682 ? 193 LYS   B CD  1 
ATOM   3131 C  CE  . LYS   B 1 149 ? -2.50500  -8.63000  53.52200  1.000 21.45682 ? 193 LYS   B CE  1 
ATOM   3132 N  NZ  . LYS   B 1 149 ? -3.27500  -7.86100  54.53200  1.000 16.71682 ? 193 LYS   B NZ  1 
ATOM   3133 N  N   . ALA   B 1 150 ? -2.97400  -7.58600  46.71500  1.000 7.91682  ? 194 ALA   B N   1 
ATOM   3134 C  CA  . ALA   B 1 150 ? -2.73400  -6.78900  45.51800  1.000 8.00682  ? 194 ALA   B CA  1 
ATOM   3135 C  C   . ALA   B 1 150 ? -3.13200  -7.58800  44.28400  1.000 8.39682  ? 194 ALA   B C   1 
ATOM   3136 O  O   . ALA   B 1 150 ? -3.14300  -8.82100  44.29700  1.000 7.90682  ? 194 ALA   B O   1 
ATOM   3137 C  CB  . ALA   B 1 150 ? -1.26300  -6.36100  45.40100  1.000 7.32682  ? 194 ALA   B CB  1 
ATOM   3138 N  N   . SER   B 1 151 ? -3.40700  -6.85800  43.20100  1.000 9.10682  ? 195 SER   B N   1 
ATOM   3139 C  CA  . SER   B 1 151 ? -3.85300  -7.43200  41.93700  1.000 10.09682 ? 195 SER   B CA  1 
ATOM   3140 C  C   . SER   B 1 151 ? -3.29500  -6.59900  40.78900  1.000 8.54682  ? 195 SER   B C   1 
ATOM   3141 O  O   . SER   B 1 151 ? -3.36600  -5.36600  40.83900  1.000 7.80682  ? 195 SER   B O   1 
ATOM   3142 C  CB  . SER   B 1 151 ? -5.38000  -7.45600  41.87500  1.000 9.97682  ? 195 SER   B CB  1 
ATOM   3143 O  OG  . SER   B 1 151 ? -5.85800  -7.71700  40.56300  1.000 11.01682 ? 195 SER   B OG  1 
ATOM   3144 N  N   . ILE   B 1 152 ? -2.75500  -7.25600  39.76400  1.000 9.76682  ? 196 ILE   B N   1 
ATOM   3145 C  CA  . ILE   B 1 152 ? -2.15500  -6.53900  38.63300  1.000 7.53682  ? 196 ILE   B CA  1 
ATOM   3146 C  C   . ILE   B 1 152 ? -2.65300  -7.12200  37.31200  1.000 8.49682  ? 196 ILE   B C   1 
ATOM   3147 O  O   . ILE   B 1 152 ? -2.03500  -8.04900  36.76800  1.000 8.58682  ? 196 ILE   B O   1 
ATOM   3148 C  CB  . ILE   B 1 152 ? -0.61600  -6.56600  38.68900  1.000 8.17682  ? 196 ILE   B CB  1 
ATOM   3149 C  CG1 . ILE   B 1 152 ? -0.11200  -6.08000  40.06700  1.000 9.49682  ? 196 ILE   B CG1 1 
ATOM   3150 C  CG2 . ILE   B 1 152 ? -0.03400  -5.67800  37.56500  1.000 7.07682  ? 196 ILE   B CG2 1 
ATOM   3151 C  CD1 . ILE   B 1 152 ? 1.43100   -5.92300  40.17900  1.000 11.18682 ? 196 ILE   B CD1 1 
ATOM   3152 N  N   . PRO   B 1 153 ? -3.75900  -6.61600  36.76100  1.000 8.12682  ? 197 PRO   B N   1 
ATOM   3153 C  CA  . PRO   B 1 153 ? -4.21900  -7.06000  35.43300  1.000 7.94682  ? 197 PRO   B CA  1 
ATOM   3154 C  C   . PRO   B 1 153 ? -3.40100  -6.41200  34.31900  1.000 10.05682 ? 197 PRO   B C   1 
ATOM   3155 O  O   . PRO   B 1 153 ? -3.36500  -5.18700  34.19100  1.000 7.97682  ? 197 PRO   B O   1 
ATOM   3156 C  CB  . PRO   B 1 153 ? -5.68700  -6.60200  35.39800  1.000 7.92682  ? 197 PRO   B CB  1 
ATOM   3157 C  CG  . PRO   B 1 153 ? -6.05800  -6.34100  36.84900  1.000 7.48682  ? 197 PRO   B CG  1 
ATOM   3158 C  CD  . PRO   B 1 153 ? -4.78500  -5.81300  37.45400  1.000 9.62682  ? 197 PRO   B CD  1 
ATOM   3159 N  N   . LEU   B 1 154 ? -2.76400  -7.24000  33.49200  1.000 11.48682 ? 198 LEU   B N   1 
ATOM   3160 C  CA  . LEU   B 1 154 ? -1.89200  -6.77500  32.41500  1.000 7.99682  ? 198 LEU   B CA  1 
ATOM   3161 C  C   . LEU   B 1 154 ? -2.63200  -6.91900  31.08800  1.000 7.81682  ? 198 LEU   B C   1 
ATOM   3162 O  O   . LEU   B 1 154 ? -3.03900  -8.02700  30.72800  1.000 8.17682  ? 198 LEU   B O   1 
ATOM   3163 C  CB  . LEU   B 1 154 ? -0.58300  -7.57300  32.39500  1.000 7.29682  ? 198 LEU   B CB  1 
ATOM   3164 C  CG  . LEU   B 1 154 ? 0.21900   -7.66600  33.69800  1.000 10.84682 ? 198 LEU   B CG  1 
ATOM   3165 C  CD1 . LEU   B 1 154 ? 1.26700   -8.78500  33.59400  1.000 12.34682 ? 198 LEU   B CD1 1 
ATOM   3166 C  CD2 . LEU   B 1 154 ? 0.89500   -6.32300  34.05300  1.000 8.11682  ? 198 LEU   B CD2 1 
ATOM   3167 N  N   . THR   B 1 155 ? -2.77200  -5.80600  30.34900  1.000 9.13682  ? 199 THR   B N   1 
ATOM   3168 C  CA  . THR   B 1 155 ? -3.64500  -5.71400  29.16900  1.000 7.56682  ? 199 THR   B CA  1 
ATOM   3169 C  C   . THR   B 1 155 ? -4.85200  -6.63900  29.31600  1.000 10.67682 ? 199 THR   B C   1 
ATOM   3170 O  O   . THR   B 1 155 ? -5.02900  -7.56500  28.51600  1.000 9.93682  ? 199 THR   B O   1 
ATOM   3171 C  CB  . THR   B 1 155 ? -2.89800  -6.06100  27.88200  1.000 8.35682  ? 199 THR   B CB  1 
ATOM   3172 O  OG1 . THR   B 1 155 ? -2.41000  -7.40100  27.97600  1.000 10.49682 ? 199 THR   B OG1 1 
ATOM   3173 C  CG2 . THR   B 1 155 ? -1.72800  -5.07900  27.62300  1.000 9.53682  ? 199 THR   B CG2 1 
ATOM   3174 N  N   . PRO   B 1 156 ? -5.69200  -6.42100  30.32200  1.000 10.08682 ? 200 PRO   B N   1 
ATOM   3175 C  CA  . PRO   B 1 156 ? -6.71100  -7.41800  30.66900  1.000 8.70682  ? 200 PRO   B CA  1 
ATOM   3176 C  C   . PRO   B 1 156 ? -7.85600  -7.47600  29.66600  1.000 8.16682  ? 200 PRO   B C   1 
ATOM   3177 O  O   . PRO   B 1 156 ? -8.23500  -6.47100  29.05800  1.000 6.67682  ? 200 PRO   B O   1 
ATOM   3178 C  CB  . PRO   B 1 156 ? -7.21100  -6.93400  32.03000  1.000 8.81682  ? 200 PRO   B CB  1 
ATOM   3179 C  CG  . PRO   B 1 156 ? -7.08500  -5.42800  31.91300  1.000 6.25682  ? 200 PRO   B CG  1 
ATOM   3180 C  CD  . PRO   B 1 156 ? -5.77200  -5.22400  31.18000  1.000 9.83682  ? 200 PRO   B CD  1 
ATOM   3181 N  N   . TRP   B 1 157 ? -8.43000  -8.67500  29.53500  1.000 7.86682  ? 201 TRP   B N   1 
ATOM   3182 C  CA  . TRP   B 1 157 ? -9.61000  -8.92900  28.71300  1.000 11.49682 ? 201 TRP   B CA  1 
ATOM   3183 C  C   . TRP   B 1 157 ? -10.71700 -9.51600  29.58200  1.000 10.31682 ? 201 TRP   B C   1 
ATOM   3184 O  O   . TRP   B 1 157 ? -10.49300 -10.50100 30.29900  1.000 9.72682  ? 201 TRP   B O   1 
ATOM   3185 C  CB  . TRP   B 1 157 ? -9.27100  -9.88200  27.55300  1.000 12.18682 ? 201 TRP   B CB  1 
ATOM   3186 C  CG  . TRP   B 1 157 ? -10.35700 -10.05800 26.50800  1.000 9.83682  ? 201 TRP   B CG  1 
ATOM   3187 C  CD1 . TRP   B 1 157 ? -10.43300 -9.44200  25.29600  1.000 10.46682 ? 201 TRP   B CD1 1 
ATOM   3188 C  CD2 . TRP   B 1 157 ? -11.51200 -10.91600 26.59300  1.000 11.60682 ? 201 TRP   B CD2 1 
ATOM   3189 N  NE1 . TRP   B 1 157 ? -11.55500 -9.86400  24.61600  1.000 11.35682 ? 201 TRP   B NE1 1 
ATOM   3190 C  CE2 . TRP   B 1 157 ? -12.23300 -10.76800 25.39000  1.000 13.51682 ? 201 TRP   B CE2 1 
ATOM   3191 C  CE3 . TRP   B 1 157 ? -12.00000 -11.79300 27.56700  1.000 11.95682 ? 201 TRP   B CE3 1 
ATOM   3192 C  CZ2 . TRP   B 1 157 ? -13.42300 -11.45800 25.13600  1.000 15.01682 ? 201 TRP   B CZ2 1 
ATOM   3193 C  CZ3 . TRP   B 1 157 ? -13.17900 -12.48600 27.31100  1.000 14.24682 ? 201 TRP   B CZ3 1 
ATOM   3194 C  CH2 . TRP   B 1 157 ? -13.87800 -12.30900 26.09800  1.000 13.77682 ? 201 TRP   B CH2 1 
ATOM   3195 N  N   . HIS   B 1 158 ? -11.91100 -8.91900  29.51300  1.000 10.70682 ? 202 HIS   B N   1 
ATOM   3196 C  CA  . HIS   B 1 158 ? -13.07700 -9.43600  30.22100  1.000 8.67682  ? 202 HIS   B CA  1 
ATOM   3197 C  C   . HIS   B 1 158 ? -14.33300 -8.81700  29.61500  1.000 12.35682 ? 202 HIS   B C   1 
ATOM   3198 O  O   . HIS   B 1 158 ? -14.33600 -7.63400  29.26700  1.000 10.00682 ? 202 HIS   B O   1 
ATOM   3199 C  CB  . HIS   B 1 158 ? -13.00100 -9.13000  31.72700  1.000 10.76682 ? 202 HIS   B CB  1 
ATOM   3200 C  CG  . HIS   B 1 158 ? -13.77400 -10.08700 32.58100  1.000 12.89682 ? 202 HIS   B CG  1 
ATOM   3201 N  ND1 . HIS   B 1 158 ? -15.14100 -10.22600 32.49200  1.000 13.99682 ? 202 HIS   B ND1 1 
ATOM   3202 C  CD2 . HIS   B 1 158 ? -13.37300 -10.94400 33.55100  1.000 11.93682 ? 202 HIS   B CD2 1 
ATOM   3203 C  CE1 . HIS   B 1 158 ? -15.55000 -11.13500 33.36100  1.000 15.38682 ? 202 HIS   B CE1 1 
ATOM   3204 N  NE2 . HIS   B 1 158 ? -14.49500 -11.59100 34.01100  1.000 10.68682 ? 202 HIS   B NE2 1 
ATOM   3205 N  N   . LEU   B 1 159 ? -15.40500 -9.61100  29.49800  1.000 9.64682  ? 203 LEU   B N   1 
ATOM   3206 C  CA  . LEU   B 1 159 ? -16.64700 -9.05100  28.95500  1.000 10.87682 ? 203 LEU   B CA  1 
ATOM   3207 C  C   . LEU   B 1 159 ? -17.41600 -8.22300  29.98500  1.000 8.66682  ? 203 LEU   B C   1 
ATOM   3208 O  O   . LEU   B 1 159 ? -18.20500 -7.35400  29.60300  1.000 9.76682  ? 203 LEU   B O   1 
ATOM   3209 C  CB  . LEU   B 1 159 ? -17.53600 -10.17100 28.39900  1.000 11.99682 ? 203 LEU   B CB  1 
ATOM   3210 C  CG  . LEU   B 1 159 ? -17.05200 -10.80700 27.08800  1.000 16.66682 ? 203 LEU   B CG  1 
ATOM   3211 C  CD1 . LEU   B 1 159 ? -18.07600 -11.77000 26.50800  1.000 18.91682 ? 203 LEU   B CD1 1 
ATOM   3212 C  CD2 . LEU   B 1 159 ? -16.67500 -9.73000  26.06400  1.000 13.50682 ? 203 LEU   B CD2 1 
ATOM   3213 N  N   . ASP   B 1 160 ? -17.23200 -8.48800  31.27800  1.000 13.71682 ? 204 ASP   B N   1 
ATOM   3214 C  CA  . ASP   B 1 160 ? -17.85700 -7.69300  32.33400  1.000 13.61682 ? 204 ASP   B CA  1 
ATOM   3215 C  C   . ASP   B 1 160 ? -17.05200 -6.41200  32.52300  1.000 12.77682 ? 204 ASP   B C   1 
ATOM   3216 O  O   . ASP   B 1 160 ? -15.84100 -6.47100  32.75900  1.000 12.69682 ? 204 ASP   B O   1 
ATOM   3217 C  CB  . ASP   B 1 160 ? -17.91500 -8.50400  33.63100  1.000 19.37682 ? 204 ASP   B CB  1 
ATOM   3218 C  CG  . ASP   B 1 160 ? -18.69700 -7.80900  34.74300  1.000 25.56682 ? 204 ASP   B CG  1 
ATOM   3219 O  OD1 . ASP   B 1 160 ? -19.15900 -6.65700  34.56300  1.000 23.04682 ? 204 ASP   B OD1 1 
ATOM   3220 O  OD2 . ASP   B 1 160 ? -18.86000 -8.43700  35.81500  1.000 31.53682 ? 204 ASP   B OD2 1 
ATOM   3221 N  N   . LYS   B 1 161 ? -17.71300 -5.25400  32.41900  1.000 11.03682 ? 205 LYS   B N   1 
ATOM   3222 C  CA  . LYS   B 1 161 ? -17.00700 -3.97500  32.36900  1.000 13.80682 ? 205 LYS   B CA  1 
ATOM   3223 C  C   . LYS   B 1 161 ? -17.02400 -3.19900  33.68000  1.000 15.06682 ? 205 LYS   B C   1 
ATOM   3224 O  O   . LYS   B 1 161 ? -16.45400 -2.10100  33.72500  1.000 15.65682 ? 205 LYS   B O   1 
ATOM   3225 C  CB  . LYS   B 1 161 ? -17.58500 -3.07800  31.26400  1.000 10.77682 ? 205 LYS   B CB  1 
ATOM   3226 C  CG  . LYS   B 1 161 ? -17.61500 -3.72400  29.88900  1.000 9.91682  ? 205 LYS   B CG  1 
ATOM   3227 C  CD  . LYS   B 1 161 ? -16.25900 -4.31500  29.49600  1.000 9.65682  ? 205 LYS   B CD  1 
ATOM   3228 C  CE  . LYS   B 1 161 ? -16.32500 -4.89800  28.07400  1.000 13.17682 ? 205 LYS   B CE  1 
ATOM   3229 N  NZ  . LYS   B 1 161 ? -14.97300 -5.35300  27.60500  1.000 10.23682 ? 205 LYS   B NZ  1 
ATOM   3230 N  N   . THR   B 1 162 ? -17.65500 -3.72100  34.73600  1.000 14.35682 ? 206 THR   B N   1 
ATOM   3231 C  CA  . THR   B 1 162 ? -17.77700 -2.99700  35.99600  1.000 13.93682 ? 206 THR   B CA  1 
ATOM   3232 C  C   . THR   B 1 162 ? -17.26400 -3.85900  37.13900  1.000 13.69682 ? 206 THR   B C   1 
ATOM   3233 O  O   . THR   B 1 162 ? -17.61900 -5.03600  37.25400  1.000 16.86682 ? 206 THR   B O   1 
ATOM   3234 C  CB  . THR   B 1 162 ? -19.22100 -2.56000  36.27800  1.000 17.92682 ? 206 THR   B CB  1 
ATOM   3235 O  OG1 . THR   B 1 162 ? -20.06400 -3.71100  36.39100  1.000 18.62682 ? 206 THR   B OG1 1 
ATOM   3236 C  CG2 . THR   B 1 162 ? -19.72700 -1.64200  35.16400  1.000 19.12682 ? 206 THR   B CG2 1 
ATOM   3237 N  N   . TRP   B 1 163 ? -16.44000 -3.26100  37.98400  1.000 11.86682 ? 207 TRP   B N   1 
ATOM   3238 C  CA  . TRP   B 1 163 ? -15.71400 -3.96900  39.02200  1.000 12.67682 ? 207 TRP   B CA  1 
ATOM   3239 C  C   . TRP   B 1 163 ? -15.76600 -3.17400  40.31900  1.000 13.49682 ? 207 TRP   B C   1 
ATOM   3240 O  O   . TRP   B 1 163 ? -14.76200 -3.02200  41.01600  1.000 10.27682 ? 207 TRP   B O   1 
ATOM   3241 C  CB  . TRP   B 1 163 ? -14.27500 -4.23700  38.56500  1.000 15.08682 ? 207 TRP   B CB  1 
ATOM   3242 C  CG  . TRP   B 1 163 ? -14.27500 -5.20500  37.43200  1.000 11.81682 ? 207 TRP   B CG  1 
ATOM   3243 C  CD1 . TRP   B 1 163 ? -14.34600 -4.91700  36.09800  1.000 12.13682 ? 207 TRP   B CD1 1 
ATOM   3244 C  CD2 . TRP   B 1 163 ? -14.29200 -6.62600  37.53900  1.000 11.76682 ? 207 TRP   B CD2 1 
ATOM   3245 N  NE1 . TRP   B 1 163 ? -14.37400 -6.08100  35.36600  1.000 14.29682 ? 207 TRP   B NE1 1 
ATOM   3246 C  CE2 . TRP   B 1 163 ? -14.34800 -7.14500  36.22900  1.000 15.02682 ? 207 TRP   B CE2 1 
ATOM   3247 C  CE3 . TRP   B 1 163 ? -14.26200 -7.51400  38.61700  1.000 9.76682  ? 207 TRP   B CE3 1 
ATOM   3248 C  CZ2 . TRP   B 1 163 ? -14.36100 -8.51600  35.96800  1.000 12.71682 ? 207 TRP   B CZ2 1 
ATOM   3249 C  CZ3 . TRP   B 1 163 ? -14.27000 -8.87300  38.35800  1.000 11.81682 ? 207 TRP   B CZ3 1 
ATOM   3250 C  CH2 . TRP   B 1 163 ? -14.32400 -9.36000  37.04500  1.000 14.16682 ? 207 TRP   B CH2 1 
ATOM   3251 N  N   . GLY   B 1 164 ? -16.95000 -2.65900  40.65500  1.000 13.60682 ? 208 GLY   B N   1 
ATOM   3252 C  CA  . GLY   B 1 164 ? -17.13200 -1.80700  41.81800  1.000 13.53682 ? 208 GLY   B CA  1 
ATOM   3253 C  C   . GLY   B 1 164 ? -17.12100 -2.52600  43.15500  1.000 12.92682 ? 208 GLY   B C   1 
ATOM   3254 O  O   . GLY   B 1 164 ? -17.19800 -1.85700  44.19300  1.000 16.01682 ? 208 GLY   B O   1 
ATOM   3255 N  N   . GLN   B 1 165 ? -17.03100 -3.85700  43.15800  1.000 11.42682 ? 209 GLN   B N   1 
ATOM   3256 C  CA  . GLN   B 1 165 ? -16.95400 -4.63100  44.39200  1.000 15.04682 ? 209 GLN   B CA  1 
ATOM   3257 C  C   . GLN   B 1 165 ? -15.52600 -4.97000  44.80500  1.000 12.75682 ? 209 GLN   B C   1 
ATOM   3258 O  O   . GLN   B 1 165 ? -15.32400 -5.46100  45.92100  1.000 13.63682 ? 209 GLN   B O   1 
ATOM   3259 C  CB  . GLN   B 1 165 ? -17.75700 -5.93200  44.26100  1.000 15.28682 ? 209 GLN   B CB  1 
ATOM   3260 C  CG  . GLN   B 1 165 ? -19.25800 -5.70500  44.09900  1.000 20.90682 ? 209 GLN   B CG  1 
ATOM   3261 C  CD  . GLN   B 1 165 ? -19.84200 -4.92300  45.26500  1.000 28.01682 ? 209 GLN   B CD  1 
ATOM   3262 O  OE1 . GLN   B 1 165 ? -20.43900 -3.85900  45.08400  1.000 35.38682 ? 209 GLN   B OE1 1 
ATOM   3263 N  NE2 . GLN   B 1 165 ? -19.66200 -5.44700  46.47500  1.000 30.33682 ? 209 GLN   B NE2 1 
ATOM   3264 N  N   . VAL   B 1 166 ? -14.53900 -4.70900  43.94300  1.000 10.45682 ? 210 VAL   B N   1 
ATOM   3265 C  CA  . VAL   B 1 166 ? -13.14900 -5.03400  44.25500  1.000 10.50682 ? 210 VAL   B CA  1 
ATOM   3266 C  C   . VAL   B 1 166 ? -12.67600 -4.22500  45.45400  1.000 10.46682 ? 210 VAL   B C   1 
ATOM   3267 O  O   . VAL   B 1 166 ? -12.82500 -2.99700  45.50200  1.000 10.60682 ? 210 VAL   B O   1 
ATOM   3268 C  CB  . VAL   B 1 166 ? -12.25500 -4.79000  43.02700  1.000 11.20682 ? 210 VAL   B CB  1 
ATOM   3269 C  CG1 . VAL   B 1 166 ? -10.78600 -4.97900  43.38200  1.000 10.58682 ? 210 VAL   B CG1 1 
ATOM   3270 C  CG2 . VAL   B 1 166 ? -12.64100 -5.73100  41.89600  1.000 8.69682  ? 210 VAL   B CG2 1 
ATOM   3271 N  N   . GLN   B 1 167 ? -12.09500 -4.91700  46.43100  1.000 9.81682  ? 211 GLN   B N   1 
ATOM   3272 C  CA  . GLN   B 1 167 ? -11.55200 -4.29900  47.63000  1.000 12.16682 ? 211 GLN   B CA  1 
ATOM   3273 C  C   . GLN   B 1 167 ? -10.03600 -4.38800  47.70300  1.000 14.74682 ? 211 GLN   B C   1 
ATOM   3274 O  O   . GLN   B 1 167 ? -9.44500  -3.95500  48.69700  1.000 13.90682 ? 211 GLN   B O   1 
ATOM   3275 C  CB  . GLN   B 1 167 ? -12.13900 -4.95900  48.87900  1.000 12.99682 ? 211 GLN   B CB  1 
ATOM   3276 C  CG  . GLN   B 1 167 ? -13.64700 -5.09000  48.90800  1.000 15.57682 ? 211 GLN   B CG  1 
ATOM   3277 C  CD  . GLN   B 1 167 ? -14.09900 -5.91300  50.10500  1.000 24.77682 ? 211 GLN   B CD  1 
ATOM   3278 O  OE1 . GLN   B 1 167 ? -14.99400 -6.76200  50.00300  1.000 29.94682 ? 211 GLN   B OE1 1 
ATOM   3279 N  NE2 . GLN   B 1 167 ? -13.46400 -5.67600  51.24900  1.000 26.23682 ? 211 GLN   B NE2 1 
ATOM   3280 N  N   . VAL   B 1 168 ? -9.39900  -4.94000  46.68300  1.000 9.73682  ? 212 VAL   B N   1 
ATOM   3281 C  CA  . VAL   B 1 168 ? -7.98000  -5.28100  46.69800  1.000 10.55682 ? 212 VAL   B CA  1 
ATOM   3282 C  C   . VAL   B 1 168 ? -7.24600  -4.27000  45.82500  1.000 12.23682 ? 212 VAL   B C   1 
ATOM   3283 O  O   . VAL   B 1 168 ? -7.65400  -4.06400  44.67700  1.000 9.89682  ? 212 VAL   B O   1 
ATOM   3284 C  CB  . VAL   B 1 168 ? -7.75900  -6.71300  46.18100  1.000 10.70682 ? 212 VAL   B CB  1 
ATOM   3285 C  CG1 . VAL   B 1 168 ? -6.26700  -7.03700  46.06200  1.000 12.98682 ? 212 VAL   B CG1 1 
ATOM   3286 C  CG2 . VAL   B 1 168 ? -8.46500  -7.69800  47.10400  1.000 9.53682  ? 212 VAL   B CG2 1 
ATOM   3287 N  N   . PRO   B 1 169 ? -6.18000  -3.62600  46.32100  1.000 12.55682 ? 213 PRO   B N   1 
ATOM   3288 C  CA  . PRO   B 1 169 ? -5.45400  -2.64000  45.50100  1.000 9.93682  ? 213 PRO   B CA  1 
ATOM   3289 C  C   . PRO   B 1 169 ? -5.06100  -3.20700  44.14500  1.000 11.39682 ? 213 PRO   B C   1 
ATOM   3290 O  O   . PRO   B 1 169 ? -4.40500  -4.24800  44.04800  1.000 9.70682  ? 213 PRO   B O   1 
ATOM   3291 C  CB  . PRO   B 1 169 ? -4.22100  -2.31000  46.35100  1.000 11.68682 ? 213 PRO   B CB  1 
ATOM   3292 C  CG  . PRO   B 1 169 ? -4.66000  -2.55000  47.76200  1.000 7.60682  ? 213 PRO   B CG  1 
ATOM   3293 C  CD  . PRO   B 1 169 ? -5.60000  -3.74600  47.67300  1.000 10.60682 ? 213 PRO   B CD  1 
ATOM   3294 N  N   . THR   B 1 170 ? -5.44300  -2.49000  43.09100  1.000 9.40682  ? 214 THR   B N   1 
ATOM   3295 C  CA  . THR   B 1 170 ? -5.39600  -3.00900  41.73200  1.000 9.69682  ? 214 THR   B CA  1 
ATOM   3296 C  C   . THR   B 1 170 ? -4.65200  -2.02700  40.83700  1.000 10.45682 ? 214 THR   B C   1 
ATOM   3297 O  O   . THR   B 1 170 ? -4.95600  -0.83100  40.84100  1.000 6.99682  ? 214 THR   B O   1 
ATOM   3298 C  CB  . THR   B 1 170 ? -6.81900  -3.27400  41.22100  1.000 8.62682  ? 214 THR   B CB  1 
ATOM   3299 O  OG1 . THR   B 1 170 ? -7.42200  -4.27600  42.05400  1.000 7.79682  ? 214 THR   B OG1 1 
ATOM   3300 C  CG2 . THR   B 1 170 ? -6.81500  -3.78100  39.76600  1.000 4.96682  ? 214 THR   B CG2 1 
ATOM   3301 N  N   . PHE   B 1 171 ? -3.65500  -2.54100  40.10400  1.000 9.29682  ? 215 PHE   B N   1 
ATOM   3302 C  CA  . PHE   B 1 171 ? -2.80400  -1.77700  39.19600  1.000 9.00682  ? 215 PHE   B CA  1 
ATOM   3303 C  C   . PHE   B 1 171 ? -3.01000  -2.34000  37.79700  1.000 8.25682  ? 215 PHE   B C   1 
ATOM   3304 O  O   . PHE   B 1 171 ? -2.54100  -3.44200  37.50300  1.000 8.32682  ? 215 PHE   B O   1 
ATOM   3305 C  CB  . PHE   B 1 171 ? -1.33000  -1.88900  39.60600  1.000 6.27682  ? 215 PHE   B CB  1 
ATOM   3306 C  CG  . PHE   B 1 171 ? -0.37200  -1.15400  38.69200  1.000 7.81682  ? 215 PHE   B CG  1 
ATOM   3307 C  CD1 . PHE   B 1 171 ? -0.76600  -0.01600  38.00700  1.000 8.24682  ? 215 PHE   B CD1 1 
ATOM   3308 C  CD2 . PHE   B 1 171 ? 0.92500   -1.61500  38.52100  1.000 10.60682 ? 215 PHE   B CD2 1 
ATOM   3309 C  CE1 . PHE   B 1 171 ? 0.12500   0.66300   37.18900  1.000 9.51682  ? 215 PHE   B CE1 1 
ATOM   3310 C  CE2 . PHE   B 1 171 ? 1.83200   -0.94100  37.70000  1.000 6.56682  ? 215 PHE   B CE2 1 
ATOM   3311 C  CZ  . PHE   B 1 171 ? 1.42700   0.20200   37.03900  1.000 6.90682  ? 215 PHE   B CZ  1 
ATOM   3312 N  N   . ILE   B 1 172 ? -3.68700  -1.58800  36.93200  1.000 8.73682  ? 216 ILE   B N   1 
ATOM   3313 C  CA  . ILE   B 1 172 ? -4.01400  -2.04600  35.58300  1.000 8.20682  ? 216 ILE   B CA  1 
ATOM   3314 C  C   . ILE   B 1 172 ? -3.03300  -1.43800  34.58800  1.000 10.44682 ? 216 ILE   B C   1 
ATOM   3315 O  O   . ILE   B 1 172 ? -2.81100  -0.22100  34.58700  1.000 9.38682  ? 216 ILE   B O   1 
ATOM   3316 C  CB  . ILE   B 1 172 ? -5.46400  -1.68700  35.21400  1.000 9.68682  ? 216 ILE   B CB  1 
ATOM   3317 C  CG1 . ILE   B 1 172 ? -6.44000  -2.53100  36.04100  1.000 7.92682  ? 216 ILE   B CG1 1 
ATOM   3318 C  CG2 . ILE   B 1 172 ? -5.69600  -1.86000  33.69600  1.000 7.86682  ? 216 ILE   B CG2 1 
ATOM   3319 C  CD1 . ILE   B 1 172 ? -7.87900  -1.98200  36.07600  1.000 8.15682  ? 216 ILE   B CD1 1 
ATOM   3320 N  N   . ILE   B 1 173 ? -2.45400  -2.28000  33.73300  1.000 10.09682 ? 217 ILE   B N   1 
ATOM   3321 C  CA  . ILE   B 1 173 ? -1.49500  -1.85700  32.71700  1.000 7.46682  ? 217 ILE   B CA  1 
ATOM   3322 C  C   . ILE   B 1 173 ? -2.13200  -2.04600  31.34100  1.000 7.46682  ? 217 ILE   B C   1 
ATOM   3323 O  O   . ILE   B 1 173 ? -2.47900  -3.17100  30.95000  1.000 9.13682  ? 217 ILE   B O   1 
ATOM   3324 C  CB  . ILE   B 1 173 ? -0.16800  -2.62600  32.83300  1.000 9.31682  ? 217 ILE   B CB  1 
ATOM   3325 C  CG1 . ILE   B 1 173 ? 0.48100   -2.33700  34.18600  1.000 8.56682  ? 217 ILE   B CG1 1 
ATOM   3326 C  CG2 . ILE   B 1 173 ? 0.78200   -2.23200  31.70400  1.000 10.44682 ? 217 ILE   B CG2 1 
ATOM   3327 C  CD1 . ILE   B 1 173 ? 1.87600   -2.90200  34.35800  1.000 13.34682 ? 217 ILE   B CD1 1 
ATOM   3328 N  N   . GLY   B 1 174 ? -2.27600  -0.94800  30.60400  1.000 7.76682  ? 218 GLY   B N   1 
ATOM   3329 C  CA  . GLY   B 1 174 ? -2.81100  -1.01800  29.25400  1.000 6.34682  ? 218 GLY   B CA  1 
ATOM   3330 C  C   . GLY   B 1 174 ? -1.78000  -0.77800  28.16900  1.000 9.91682  ? 218 GLY   B C   1 
ATOM   3331 O  O   . GLY   B 1 174 ? -0.72100  -0.19800  28.42400  1.000 9.54682  ? 218 GLY   B O   1 
ATOM   3332 N  N   . ALA   B 1 175 ? -2.08100  -1.21200  26.94700  1.000 5.01682  ? 219 ALA   B N   1 
ATOM   3333 C  CA  . ALA   B 1 175 ? -1.21800  -0.99600  25.79100  1.000 8.92682  ? 219 ALA   B CA  1 
ATOM   3334 C  C   . ALA   B 1 175 ? -1.97500  -0.12000  24.80700  1.000 11.21682 ? 219 ALA   B C   1 
ATOM   3335 O  O   . ALA   B 1 175 ? -3.04900  -0.50700  24.33400  1.000 10.16682 ? 219 ALA   B O   1 
ATOM   3336 C  CB  . ALA   B 1 175 ? -0.81300  -2.32000  25.13100  1.000 9.10682  ? 219 ALA   B CB  1 
ATOM   3337 N  N   . GLU   B 1 176 ? -1.40100  1.04200   24.48300  1.000 10.41682 ? 220 GLU   B N   1 
ATOM   3338 C  CA  . GLU   B 1 176 ? -2.13200  2.06300   23.73300  1.000 9.87682  ? 220 GLU   B CA  1 
ATOM   3339 C  C   . GLU   B 1 176 ? -2.75200  1.52200   22.44500  1.000 9.22682  ? 220 GLU   B C   1 
ATOM   3340 O  O   . GLU   B 1 176 ? -3.90500  1.83900   22.12500  1.000 9.05682  ? 220 GLU   B O   1 
ATOM   3341 C  CB  . GLU   B 1 176 ? -1.20400  3.23700   23.41300  1.000 11.36682 ? 220 GLU   B CB  1 
ATOM   3342 C  CG  . GLU   B 1 176 ? -1.86300  4.30200   22.55300  1.000 10.60682 ? 220 GLU   B CG  1 
ATOM   3343 C  CD  . GLU   B 1 176 ? -0.88700  5.34800   22.03400  1.000 20.55682 ? 220 GLU   B CD  1 
ATOM   3344 O  OE1 . GLU   B 1 176 ? 0.33900   5.16600   22.19400  1.000 16.51682 ? 220 GLU   B OE1 1 
ATOM   3345 O  OE2 . GLU   B 1 176 ? -1.35600  6.35800   21.46000  1.000 23.46682 ? 220 GLU   B OE2 1 
ATOM   3346 N  N   . LEU   B 1 177 ? -2.01500  0.70900   21.68600  1.000 7.02682  ? 221 LEU   B N   1 
ATOM   3347 C  CA  . LEU   B 1 177 ? -2.50600  0.27000   20.38400  1.000 10.75682 ? 221 LEU   B CA  1 
ATOM   3348 C  C   . LEU   B 1 177 ? -3.04500  -1.15700  20.39900  1.000 7.87682  ? 221 LEU   B C   1 
ATOM   3349 O  O   . LEU   B 1 177 ? -3.12100  -1.79100  19.34200  1.000 10.23682 ? 221 LEU   B O   1 
ATOM   3350 C  CB  . LEU   B 1 177 ? -1.41000  0.42100   19.32100  1.000 9.44682  ? 221 LEU   B CB  1 
ATOM   3351 C  CG  . LEU   B 1 177 ? -0.81500  1.83000   19.20200  1.000 9.45682  ? 221 LEU   B CG  1 
ATOM   3352 C  CD1 . LEU   B 1 177 ? 0.30300   1.87100   18.16300  1.000 8.86682  ? 221 LEU   B CD1 1 
ATOM   3353 C  CD2 . LEU   B 1 177 ? -1.89600  2.86200   18.89600  1.000 14.96682 ? 221 LEU   B CD2 1 
ATOM   3354 N  N   . ASP   B 1 178 ? -3.42900  -1.66400  21.56800  1.000 7.52682  ? 222 ASP   B N   1 
ATOM   3355 C  CA  . ASP   B 1 178 ? -3.98700  -3.00800  21.70100  1.000 7.08682  ? 222 ASP   B CA  1 
ATOM   3356 C  C   . ASP   B 1 178 ? -5.25900  -3.15000  20.85300  1.000 8.33682  ? 222 ASP   B C   1 
ATOM   3357 O  O   . ASP   B 1 178 ? -6.19300  -2.35900  20.99400  1.000 8.81682  ? 222 ASP   B O   1 
ATOM   3358 C  CB  . ASP   B 1 178 ? -4.28400  -3.25300  23.18400  1.000 8.77682  ? 222 ASP   B CB  1 
ATOM   3359 C  CG  . ASP   B 1 178 ? -4.43600  -4.72200  23.54000  1.000 8.86682  ? 222 ASP   B CG  1 
ATOM   3360 O  OD1 . ASP   B 1 178 ? -4.90400  -5.51000  22.69000  1.000 9.57682  ? 222 ASP   B OD1 1 
ATOM   3361 O  OD2 . ASP   B 1 178 ? -4.09200  -5.08700  24.68900  1.000 9.00682  ? 222 ASP   B OD2 1 
ATOM   3362 N  N   . THR   B 1 179 ? -5.29200  -4.14100  19.95800  1.000 8.52682  ? 223 THR   B N   1 
ATOM   3363 C  CA  . THR   B 1 179 ? -6.48800  -4.41400  19.15700  1.000 9.61682  ? 223 THR   B CA  1 
ATOM   3364 C  C   . THR   B 1 179 ? -7.27300  -5.61900  19.65800  1.000 14.31682 ? 223 THR   B C   1 
ATOM   3365 O  O   . THR   B 1 179 ? -8.40500  -5.84700  19.20400  1.000 10.38682 ? 223 THR   B O   1 
ATOM   3366 C  CB  . THR   B 1 179 ? -6.12500  -4.65600  17.68000  1.000 11.63682 ? 223 THR   B CB  1 
ATOM   3367 O  OG1 . THR   B 1 179 ? -5.37700  -5.87200  17.55900  1.000 16.29682 ? 223 THR   B OG1 1 
ATOM   3368 C  CG2 . THR   B 1 179 ? -5.29700  -3.51000  17.12900  1.000 14.97682 ? 223 THR   B CG2 1 
ATOM   3369 N  N   . ILE   B 1 180 ? -6.69200  -6.40800  20.55200  1.000 10.84682 ? 224 ILE   B N   1 
ATOM   3370 C  CA  . ILE   B 1 180 ? -7.35400  -7.60500  21.04800  1.000 12.14682 ? 224 ILE   B CA  1 
ATOM   3371 C  C   . ILE   B 1 180 ? -8.14600  -7.30400  22.31300  1.000 10.82682 ? 224 ILE   B C   1 
ATOM   3372 O  O   . ILE   B 1 180 ? -9.30000  -7.71700  22.43900  1.000 10.29682 ? 224 ILE   B O   1 
ATOM   3373 C  CB  . ILE   B 1 180 ? -6.31000  -8.72000  21.26000  1.000 12.49682 ? 224 ILE   B CB  1 
ATOM   3374 C  CG1 . ILE   B 1 180 ? -5.63300  -9.05000  19.92900  1.000 13.88682 ? 224 ILE   B CG1 1 
ATOM   3375 C  CG2 . ILE   B 1 180 ? -6.95100  -9.95900  21.86500  1.000 9.13682  ? 224 ILE   B CG2 1 
ATOM   3376 C  CD1 . ILE   B 1 180 ? -4.42600  -9.96900  20.06400  1.000 17.41682 ? 224 ILE   B CD1 1 
ATOM   3377 N  N   . ALA   B 1 181 ? -7.55900  -6.55300  23.25500  1.000 10.50682 ? 225 ALA   B N   1 
ATOM   3378 C  CA  . ALA   B 1 181 ? -8.27600  -5.99900  24.41200  1.000 10.84682 ? 225 ALA   B CA  1 
ATOM   3379 C  C   . ALA   B 1 181 ? -8.04500  -4.49000  24.43600  1.000 9.66682  ? 225 ALA   B C   1 
ATOM   3380 O  O   . ALA   B 1 181 ? -7.24900  -3.97900  25.24800  1.000 8.74682  ? 225 ALA   B O   1 
ATOM   3381 C  CB  . ALA   B 1 181 ? -7.83600  -6.64800  25.72300  1.000 9.66682  ? 225 ALA   B CB  1 
ATOM   3382 N  N   . PRO   B 1 182 ? -8.72300  -3.74400  23.56200  1.000 9.31682  ? 226 PRO   B N   1 
ATOM   3383 C  CA  . PRO   B 1 182 ? -8.45300  -2.30300  23.45200  1.000 7.86682  ? 226 PRO   B CA  1 
ATOM   3384 C  C   . PRO   B 1 182 ? -8.68000  -1.58900  24.77500  1.000 8.41682  ? 226 PRO   B C   1 
ATOM   3385 O  O   . PRO   B 1 182 ? -9.63900  -1.86300  25.50100  1.000 8.07682  ? 226 PRO   B O   1 
ATOM   3386 C  CB  . PRO   B 1 182 ? -9.44500  -1.83800  22.37500  1.000 7.43682  ? 226 PRO   B CB  1 
ATOM   3387 C  CG  . PRO   B 1 182 ? -9.74300  -3.07900  21.58200  1.000 6.15682  ? 226 PRO   B CG  1 
ATOM   3388 C  CD  . PRO   B 1 182 ? -9.73800  -4.19100  22.59700  1.000 7.87682  ? 226 PRO   B CD  1 
ATOM   3389 N  N   . VAL   B 1 183 ? -7.77500  -0.66000  25.09100  1.000 9.54682  ? 227 VAL   B N   1 
ATOM   3390 C  CA  . VAL   B 1 183 ? -7.86400  0.02000   26.37800  1.000 9.51682  ? 227 VAL   B CA  1 
ATOM   3391 C  C   . VAL   B 1 183 ? -9.17300  0.79000   26.49800  1.000 8.68682  ? 227 VAL   B C   1 
ATOM   3392 O  O   . VAL   B 1 183 ? -9.67100  1.00600   27.60700  1.000 7.55682  ? 227 VAL   B O   1 
ATOM   3393 C  CB  . VAL   B 1 183 ? -6.63600  0.92900   26.59000  1.000 7.38682  ? 227 VAL   B CB  1 
ATOM   3394 C  CG1 . VAL   B 1 183 ? -5.35000  0.06000   26.72000  1.000 7.49682  ? 227 VAL   B CG1 1 
ATOM   3395 C  CG2 . VAL   B 1 183 ? -6.49800  1.93100   25.46100  1.000 13.59682 ? 227 VAL   B CG2 1 
ATOM   3396 N  N   . SER   B 1 184 ? -9.76300  1.19300   25.36700  1.000 9.69682  ? 228 SER   B N   1 
ATOM   3397 C  CA  . SER   B 1 184 ? -10.99700 1.96900   25.41500  1.000 10.16682 ? 228 SER   B CA  1 
ATOM   3398 C  C   . SER   B 1 184 ? -12.18800 1.12700   25.86100  1.000 7.95682  ? 228 SER   B C   1 
ATOM   3399 O  O   . SER   B 1 184 ? -13.14700 1.66400   26.42600  1.000 9.50682  ? 228 SER   B O   1 
ATOM   3400 C  CB  . SER   B 1 184 ? -11.26800 2.60500   24.04700  1.000 8.87682  ? 228 SER   B CB  1 
ATOM   3401 O  OG  . SER   B 1 184 ? -11.43700 1.60500   23.05500  1.000 12.73682 ? 228 SER   B OG  1 
ATOM   3402 N  N   . THR   B 1 185 ? -12.14500 -0.18700  25.64800  1.000 8.53682  ? 229 THR   B N   1 
ATOM   3403 C  CA  . THR   B 1 185 ? -13.27300 -1.03900  25.98200  1.000 9.78682  ? 229 THR   B CA  1 
ATOM   3404 C  C   . THR   B 1 185 ? -12.97600 -2.08200  27.05500  1.000 7.84682  ? 229 THR   B C   1 
ATOM   3405 O  O   . THR   B 1 185 ? -13.90900 -2.75400  27.50300  1.000 9.64682  ? 229 THR   B O   1 
ATOM   3406 C  CB  . THR   B 1 185 ? -13.79200 -1.73900  24.72100  1.000 11.02682 ? 229 THR   B CB  1 
ATOM   3407 O  OG1 . THR   B 1 185 ? -12.69400 -2.34700  24.03300  1.000 8.20682  ? 229 THR   B OG1 1 
ATOM   3408 C  CG2 . THR   B 1 185 ? -14.44700 -0.71300  23.80300  1.000 11.03682 ? 229 THR   B CG2 1 
ATOM   3409 N  N   . HIS   B 1 186 ? -11.72300 -2.22000  27.49500  1.000 6.21682  ? 230 HIS   B N   1 
ATOM   3410 C  CA  . HIS   B 1 186 ? -11.38200 -3.13600  28.57800  1.000 8.84682  ? 230 HIS   B CA  1 
ATOM   3411 C  C   . HIS   B 1 186 ? -10.66300 -2.39400  29.70900  1.000 9.29682  ? 230 HIS   B C   1 
ATOM   3412 O  O   . HIS   B 1 186 ? -11.30400 -1.96700  30.67900  1.000 7.75682  ? 230 HIS   B O   1 
ATOM   3413 C  CB  . HIS   B 1 186 ? -10.54100 -4.30200  28.02900  1.000 9.60682  ? 230 HIS   B CB  1 
ATOM   3414 C  CG  . HIS   B 1 186 ? -11.28700 -5.16900  27.06000  1.000 9.43682  ? 230 HIS   B CG  1 
ATOM   3415 N  ND1 . HIS   B 1 186 ? -11.86700 -6.36500  27.42300  1.000 8.62682  ? 230 HIS   B ND1 1 
ATOM   3416 C  CD2 . HIS   B 1 186 ? -11.59700 -4.98100  25.75500  1.000 11.54682 ? 230 HIS   B CD2 1 
ATOM   3417 C  CE1 . HIS   B 1 186 ? -12.48300 -6.88800  26.37900  1.000 10.02682 ? 230 HIS   B CE1 1 
ATOM   3418 N  NE2 . HIS   B 1 186 ? -12.33500 -6.06900  25.35300  1.000 11.10682 ? 230 HIS   B NE2 1 
ATOM   3419 N  N   . ALA   B 1 187 ? -9.34800  -2.19600  29.56800  1.000 6.43682  ? 231 ALA   B N   1 
ATOM   3420 C  CA  . ALA   B 1 187 ? -8.52500  -1.63400  30.64000  1.000 6.80682  ? 231 ALA   B CA  1 
ATOM   3421 C  C   . ALA   B 1 187 ? -9.13600  -0.37700  31.26600  1.000 8.73682  ? 231 ALA   B C   1 
ATOM   3422 O  O   . ALA   B 1 187 ? -9.26100  -0.27400  32.49100  1.000 7.52682  ? 231 ALA   B O   1 
ATOM   3423 C  CB  . ALA   B 1 187 ? -7.13100  -1.30800  30.10300  1.000 6.68682  ? 231 ALA   B CB  1 
ATOM   3424 N  N   . LYS   B 1 188 ? -9.47800  0.61500   30.44700  1.000 8.14682  ? 232 LYS   B N   1 
ATOM   3425 C  CA  . LYS   B 1 188 ? -9.94300  1.87600   31.02800  1.000 9.72682  ? 232 LYS   B CA  1 
ATOM   3426 C  C   . LYS   B 1 188 ? -11.29700 1.74100   31.71800  1.000 7.30682  ? 232 LYS   B C   1 
ATOM   3427 O  O   . LYS   B 1 188 ? -11.44300 2.24600   32.84500  1.000 9.70682  ? 232 LYS   B O   1 
ATOM   3428 C  CB  . LYS   B 1 188 ? -9.95700  2.97400   29.96100  1.000 10.09682 ? 232 LYS   B CB  1 
ATOM   3429 C  CG  . LYS   B 1 188 ? -8.59000  3.47300   29.53700  1.000 11.69682 ? 232 LYS   B CG  1 
ATOM   3430 C  CD  . LYS   B 1 188 ? -8.75300  4.45300   28.38700  1.000 9.97682  ? 232 LYS   B CD  1 
ATOM   3431 C  CE  . LYS   B 1 188 ? -7.49400  5.25900   28.15900  1.000 19.79682 ? 232 LYS   B CE  1 
ATOM   3432 N  NZ  . LYS   B 1 188 ? -7.50200  5.92500   26.82100  1.000 23.38682 ? 232 LYS   B NZ  1 
ATOM   3433 N  N   . PRO   B 1 189 ? -12.32600 1.13100   31.12100  1.000 5.85682  ? 233 PRO   B N   1 
ATOM   3434 C  CA  . PRO   B 1 189 ? -13.57900 0.98800   31.88100  1.000 7.80682  ? 233 PRO   B CA  1 
ATOM   3435 C  C   . PRO   B 1 189 ? -13.41800 0.13500   33.14000  1.000 8.85682  ? 233 PRO   B C   1 
ATOM   3436 O  O   . PRO   B 1 189 ? -14.04500 0.44200   34.15800  1.000 9.78682  ? 233 PRO   B O   1 
ATOM   3437 C  CB  . PRO   B 1 189 ? -14.56000 0.36900   30.86400  1.000 10.81682 ? 233 PRO   B CB  1 
ATOM   3438 C  CG  . PRO   B 1 189 ? -13.78900 0.04500   29.66400  1.000 9.70682  ? 233 PRO   B CG  1 
ATOM   3439 C  CD  . PRO   B 1 189 ? -12.50800 0.81700   29.68900  1.000 7.14682  ? 233 PRO   B CD  1 
ATOM   3440 N  N   . PHE   B 1 190 ? -12.57400 -0.90900  33.11300  1.000 6.43682  ? 234 PHE   B N   1 
ATOM   3441 C  CA  . PHE   B 1 190 ? -12.27100 -1.63600  34.34300  1.000 9.35682  ? 234 PHE   B CA  1 
ATOM   3442 C  C   . PHE   B 1 190 ? -11.74600 -0.68400  35.40300  1.000 8.65682  ? 234 PHE   B C   1 
ATOM   3443 O  O   . PHE   B 1 190 ? -12.21700 -0.68300  36.54200  1.000 9.68682  ? 234 PHE   B O   1 
ATOM   3444 C  CB  . PHE   B 1 190 ? -11.22400 -2.73300  34.11000  1.000 6.91682  ? 234 PHE   B CB  1 
ATOM   3445 C  CG  . PHE   B 1 190 ? -11.60700 -3.76600  33.09600  1.000 8.09682  ? 234 PHE   B CG  1 
ATOM   3446 C  CD1 . PHE   B 1 190 ? -12.93700 -4.01700  32.78500  1.000 9.37682  ? 234 PHE   B CD1 1 
ATOM   3447 C  CD2 . PHE   B 1 190 ? -10.61800 -4.50900  32.45900  1.000 6.75682  ? 234 PHE   B CD2 1 
ATOM   3448 C  CE1 . PHE   B 1 190 ? -13.27200 -4.98100  31.85000  1.000 9.58682  ? 234 PHE   B CE1 1 
ATOM   3449 C  CE2 . PHE   B 1 190 ? -10.95000 -5.47100  31.52300  1.000 12.63682 ? 234 PHE   B CE2 1 
ATOM   3450 C  CZ  . PHE   B 1 190 ? -12.28000 -5.71600  31.22300  1.000 8.76682  ? 234 PHE   B CZ  1 
ATOM   3451 N  N   . TYR   B 1 191 ? -10.75700 0.13700   35.03600  1.000 7.77682  ? 235 TYR   B N   1 
ATOM   3452 C  CA  . TYR   B 1 191 ? -10.09900 0.98500   36.02200  1.000 6.57682  ? 235 TYR   B CA  1 
ATOM   3453 C  C   . TYR   B 1 191 ? -11.07800 1.98300   36.61900  1.000 6.95682  ? 235 TYR   B C   1 
ATOM   3454 O  O   . TYR   B 1 191 ? -11.13800 2.16600   37.84100  1.000 9.46682  ? 235 TYR   B O   1 
ATOM   3455 C  CB  . TYR   B 1 191 ? -8.91000  1.72400   35.39400  1.000 5.75682  ? 235 TYR   B CB  1 
ATOM   3456 C  CG  . TYR   B 1 191 ? -8.37600  2.77900   36.33500  1.000 10.53682 ? 235 TYR   B CG  1 
ATOM   3457 C  CD1 . TYR   B 1 191 ? -7.59800  2.42300   37.43100  1.000 8.71682  ? 235 TYR   B CD1 1 
ATOM   3458 C  CD2 . TYR   B 1 191 ? -8.70000  4.13400   36.16600  1.000 9.13682  ? 235 TYR   B CD2 1 
ATOM   3459 C  CE1 . TYR   B 1 191 ? -7.12900  3.38300   38.31400  1.000 7.73682  ? 235 TYR   B CE1 1 
ATOM   3460 C  CE2 . TYR   B 1 191 ? -8.23900  5.09200   37.04400  1.000 8.80682  ? 235 TYR   B CE2 1 
ATOM   3461 C  CZ  . TYR   B 1 191 ? -7.45200  4.71300   38.11700  1.000 8.14682  ? 235 TYR   B CZ  1 
ATOM   3462 O  OH  . TYR   B 1 191 ? -6.99500  5.66500   39.00800  1.000 8.59682  ? 235 TYR   B OH  1 
ATOM   3463 N  N   . GLU   B 1 192 ? -11.84800 2.65100   35.76000  1.000 7.94682  ? 236 GLU   B N   1 
ATOM   3464 C  CA  . GLU   B 1 192 ? -12.76800 3.67300   36.22200  1.000 7.66682  ? 236 GLU   B CA  1 
ATOM   3465 C  C   . GLU   B 1 192 ? -13.92100 3.08700   37.02900  1.000 12.65682 ? 236 GLU   B C   1 
ATOM   3466 O  O   . GLU   B 1 192 ? -14.52000 3.80500   37.83100  1.000 14.91682 ? 236 GLU   B O   1 
ATOM   3467 C  CB  . GLU   B 1 192 ? -13.28500 4.47200   35.01500  1.000 11.03682 ? 236 GLU   B CB  1 
ATOM   3468 C  CG  . GLU   B 1 192 ? -12.20300 5.32000   34.36500  1.000 11.06682 ? 236 GLU   B CG  1 
ATOM   3469 C  CD  . GLU   B 1 192 ? -11.68400 6.41200   35.30100  1.000 14.17682 ? 236 GLU   B CD  1 
ATOM   3470 O  OE1 . GLU   B 1 192 ? -12.40700 6.77400   36.25900  1.000 16.81682 ? 236 GLU   B OE1 1 
ATOM   3471 O  OE2 . GLU   B 1 192 ? -10.55700 6.91000   35.08200  1.000 17.73682 ? 236 GLU   B OE2 1 
ATOM   3472 N  N   . SER   B 1 193 ? -14.23900 1.80100   36.84500  1.000 11.36682 ? 237 SER   B N   1 
ATOM   3473 C  CA  . SER   B 1 193 ? -15.30900 1.18000   37.61400  1.000 10.69682 ? 237 SER   B CA  1 
ATOM   3474 C  C   . SER   B 1 193 ? -14.85700 0.70800   38.99300  1.000 13.24682 ? 237 SER   B C   1 
ATOM   3475 O  O   . SER   B 1 193 ? -15.70900 0.43200   39.84500  1.000 10.99682 ? 237 SER   B O   1 
ATOM   3476 C  CB  . SER   B 1 193 ? -15.91200 0.00000   36.84300  1.000 11.48682 ? 237 SER   B CB  1 
ATOM   3477 O  OG  . SER   B 1 193 ? -15.06600 -1.14000  36.89900  1.000 12.33682 ? 237 SER   B OG  1 
ATOM   3478 N  N   . LEU   B 1 194 ? -13.55200 0.60700   39.23800  1.000 11.06682 ? 238 LEU   B N   1 
ATOM   3479 C  CA  . LEU   B 1 194 ? -13.08000 0.29000   40.57900  1.000 9.05682  ? 238 LEU   B CA  1 
ATOM   3480 C  C   . LEU   B 1 194 ? -13.46900 1.41400   41.53600  1.000 12.62682 ? 238 LEU   B C   1 
ATOM   3481 O  O   . LEU   B 1 194 ? -13.52800 2.58200   41.13200  1.000 11.68682 ? 238 LEU   B O   1 
ATOM   3482 C  CB  . LEU   B 1 194 ? -11.56000 0.09000   40.59500  1.000 6.50682  ? 238 LEU   B CB  1 
ATOM   3483 C  CG  . LEU   B 1 194 ? -10.99700 -1.04500  39.73300  1.000 11.17682 ? 238 LEU   B CG  1 
ATOM   3484 C  CD1 . LEU   B 1 194 ? -9.48700  -0.85100  39.50500  1.000 7.14682  ? 238 LEU   B CD1 1 
ATOM   3485 C  CD2 . LEU   B 1 194 ? -11.28700 -2.44200  40.31900  1.000 9.99682  ? 238 LEU   B CD2 1 
ATOM   3486 N  N   . PRO   B 1 195 ? -13.73500 1.09000   42.80700  1.000 10.00682 ? 239 PRO   B N   1 
ATOM   3487 C  CA  . PRO   B 1 195 ? -14.16500 2.11800   43.77000  1.000 11.80682 ? 239 PRO   B CA  1 
ATOM   3488 C  C   . PRO   B 1 195 ? -13.20200 3.29800   43.81600  1.000 13.58682 ? 239 PRO   B C   1 
ATOM   3489 O  O   . PRO   B 1 195 ? -11.98000 3.14500   43.72300  1.000 10.31682 ? 239 PRO   B O   1 
ATOM   3490 C  CB  . PRO   B 1 195 ? -14.18900 1.36900   45.11100  1.000 11.33682 ? 239 PRO   B CB  1 
ATOM   3491 C  CG  . PRO   B 1 195 ? -14.33700 -0.06700  44.78100  1.000 12.32682 ? 239 PRO   B CG  1 
ATOM   3492 C  CD  . PRO   B 1 195 ? -13.71200 -0.26100  43.39700  1.000 11.39682 ? 239 PRO   B CD  1 
ATOM   3493 N  N   . SER   B 1 196 ? -13.76500 4.49300   43.96500  1.000 15.48682 ? 240 SER   B N   1 
ATOM   3494 C  CA  . SER   B 1 196 ? -12.92300 5.67800   44.02400  1.000 16.19682 ? 240 SER   B CA  1 
ATOM   3495 C  C   . SER   B 1 196 ? -12.07000 5.71500   45.28500  1.000 14.71682 ? 240 SER   B C   1 
ATOM   3496 O  O   . SER   B 1 196 ? -11.04700 6.40800   45.30600  1.000 15.74682 ? 240 SER   B O   1 
ATOM   3497 C  CB  . SER   B 1 196 ? -13.78900 6.93600   43.92400  1.000 25.34682 ? 240 SER   B CB  1 
ATOM   3498 O  OG  . SER   B 1 196 ? -14.91500 6.83900   44.77500  1.000 36.58682 ? 240 SER   B OG  1 
ATOM   3499 N  N   . SER   B 1 197 ? -12.45100 4.97800   46.32600  1.000 13.65682 ? 241 SER   B N   1 
ATOM   3500 C  CA  . SER   B 1 197 ? -11.65900 4.92700   47.54700  1.000 19.84682 ? 241 SER   B CA  1 
ATOM   3501 C  C   . SER   B 1 197 ? -10.64000 3.79400   47.54200  1.000 17.00682 ? 241 SER   B C   1 
ATOM   3502 O  O   . SER   B 1 197 ? -9.85100  3.68700   48.48100  1.000 18.07682 ? 241 SER   B O   1 
ATOM   3503 C  CB  . SER   B 1 197 ? -12.57100 4.79700   48.76900  1.000 15.26682 ? 241 SER   B CB  1 
ATOM   3504 O  OG  . SER   B 1 197 ? -13.22400 3.54100   48.78000  1.000 21.16682 ? 241 SER   B OG  1 
ATOM   3505 N  N   . LEU   B 1 198 ? -10.63000 2.95600   46.51300  1.000 12.25682 ? 242 LEU   B N   1 
ATOM   3506 C  CA  . LEU   B 1 198 ? -9.62400  1.90800   46.41900  1.000 11.54682 ? 242 LEU   B CA  1 
ATOM   3507 C  C   . LEU   B 1 198 ? -8.26700  2.50700   46.04900  1.000 11.56682 ? 242 LEU   B C   1 
ATOM   3508 O  O   . LEU   B 1 198 ? -8.18800  3.36000   45.16100  1.000 10.78682 ? 242 LEU   B O   1 
ATOM   3509 C  CB  . LEU   B 1 198 ? -10.02200 0.88500   45.35600  1.000 8.26682  ? 242 LEU   B CB  1 
ATOM   3510 C  CG  . LEU   B 1 198 ? -9.17600  -0.38800  45.34300  1.000 10.84682 ? 242 LEU   B CG  1 
ATOM   3511 C  CD1 . LEU   B 1 198 ? -9.49300  -1.17600  46.59100  1.000 8.73682  ? 242 LEU   B CD1 1 
ATOM   3512 C  CD2 . LEU   B 1 198 ? -9.41200  -1.22100  44.09900  1.000 7.80682  ? 242 LEU   B CD2 1 
ATOM   3513 N  N   . PRO   B 1 199 ? -7.17700  2.07600   46.70200  1.000 10.53682 ? 243 PRO   B N   1 
ATOM   3514 C  CA  . PRO   B 1 199 ? -5.84500  2.36500   46.15000  1.000 12.84682 ? 243 PRO   B CA  1 
ATOM   3515 C  C   . PRO   B 1 199 ? -5.71000  1.69700   44.78900  1.000 9.73682  ? 243 PRO   B C   1 
ATOM   3516 O  O   . PRO   B 1 199 ? -5.73300  0.46500   44.70100  1.000 7.91682  ? 243 PRO   B O   1 
ATOM   3517 C  CB  . PRO   B 1 199 ? -4.88100  1.77000   47.19000  1.000 10.87682 ? 243 PRO   B CB  1 
ATOM   3518 C  CG  . PRO   B 1 199 ? -5.71400  1.60500   48.45000  1.000 13.62682 ? 243 PRO   B CG  1 
ATOM   3519 C  CD  . PRO   B 1 199 ? -7.09900  1.29000   47.94600  1.000 13.40682 ? 243 PRO   B CD  1 
ATOM   3520 N  N   . LYS   B 1 200 ? -5.60700  2.48400   43.71900  1.000 8.38682  ? 244 LYS   B N   1 
ATOM   3521 C  CA  . LYS   B 1 200 ? -5.58100  1.90900   42.37900  1.000 12.62682 ? 244 LYS   B CA  1 
ATOM   3522 C  C   . LYS   B 1 200 ? -4.73900  2.78800   41.46200  1.000 9.00682  ? 244 LYS   B C   1 
ATOM   3523 O  O   . LYS   B 1 200 ? -4.39900  3.92600   41.79900  1.000 6.19682  ? 244 LYS   B O   1 
ATOM   3524 C  CB  . LYS   B 1 200 ? -7.00900  1.72000   41.82600  1.000 7.10682  ? 244 LYS   B CB  1 
ATOM   3525 C  CG  . LYS   B 1 200 ? -7.84400  3.01000   41.76600  1.000 7.19682  ? 244 LYS   B CG  1 
ATOM   3526 C  CD  . LYS   B 1 200 ? -9.22900  2.75900   41.19100  1.000 12.05682 ? 244 LYS   B CD  1 
ATOM   3527 C  CE  . LYS   B 1 200 ? -9.89700  4.06100   40.71600  1.000 11.08682 ? 244 LYS   B CE  1 
ATOM   3528 N  NZ  . LYS   B 1 200 ? -11.25800 3.79100   40.14400  1.000 11.23682 ? 244 LYS   B NZ  1 
ATOM   3529 N  N   . ALA   B 1 201 ? -4.39200  2.23600   40.29600  1.000 7.72682  ? 245 ALA   B N   1 
ATOM   3530 C  CA  . ALA   B 1 201 ? -3.65200  2.97900   39.28500  1.000 7.35682  ? 245 ALA   B CA  1 
ATOM   3531 C  C   . ALA   B 1 201 ? -3.85200  2.34700   37.91300  1.000 7.30682  ? 245 ALA   B C   1 
ATOM   3532 O  O   . ALA   B 1 201 ? -4.08900  1.14400   37.79100  1.000 8.18682  ? 245 ALA   B O   1 
ATOM   3533 C  CB  . ALA   B 1 201 ? -2.15500  3.04500   39.60700  1.000 8.23682  ? 245 ALA   B CB  1 
ATOM   3534 N  N   . TYR   B 1 202 ? -3.75600  3.19200   36.88700  1.000 9.62682  ? 246 TYR   B N   1 
ATOM   3535 C  CA  . TYR   B 1 202 ? -3.80200  2.79300   35.48900  1.000 9.59682  ? 246 TYR   B CA  1 
ATOM   3536 C  C   . TYR   B 1 202 ? -2.57700  3.36500   34.78400  1.000 10.30682 ? 246 TYR   B C   1 
ATOM   3537 O  O   . TYR   B 1 202 ? -2.31100  4.56300   34.89200  1.000 10.94682 ? 246 TYR   B O   1 
ATOM   3538 C  CB  . TYR   B 1 202 ? -5.08300  3.29900   34.82100  1.000 8.49682  ? 246 TYR   B CB  1 
ATOM   3539 C  CG  . TYR   B 1 202 ? -5.07400  3.14000   33.32300  1.000 8.91682  ? 246 TYR   B CG  1 
ATOM   3540 C  CD1 . TYR   B 1 202 ? -5.15000  1.87800   32.75400  1.000 10.12682 ? 246 TYR   B CD1 1 
ATOM   3541 C  CD2 . TYR   B 1 202 ? -4.96800  4.23900   32.47800  1.000 11.68682 ? 246 TYR   B CD2 1 
ATOM   3542 C  CE1 . TYR   B 1 202 ? -5.13400  1.70800   31.39200  1.000 12.40682 ? 246 TYR   B CE1 1 
ATOM   3543 C  CE2 . TYR   B 1 202 ? -4.96600  4.07600   31.09100  1.000 11.51682 ? 246 TYR   B CE2 1 
ATOM   3544 C  CZ  . TYR   B 1 202 ? -5.04600  2.79700   30.56400  1.000 11.46682 ? 246 TYR   B CZ  1 
ATOM   3545 O  OH  . TYR   B 1 202 ? -5.03400  2.57200   29.20200  1.000 11.88682 ? 246 TYR   B OH  1 
ATOM   3546 N  N   . MET   B 1 203 ? -1.83500  2.51200   34.06700  1.000 8.26682  ? 247 MET   B N   1 
ATOM   3547 C  CA  . MET   B 1 203 ? -0.64300  2.91900   33.31900  1.000 9.72682  ? 247 MET   B CA  1 
ATOM   3548 C  C   . MET   B 1 203 ? -0.76800  2.45500   31.87100  1.000 7.85682  ? 247 MET   B C   1 
ATOM   3549 O  O   . MET   B 1 203 ? -0.86800  1.25100   31.61000  1.000 10.77682 ? 247 MET   B O   1 
ATOM   3550 C  CB  . MET   B 1 203 ? 0.63400   2.33200   33.94000  1.000 6.44682  ? 247 MET   B CB  1 
ATOM   3551 C  CG  . MET   B 1 203 ? 1.88300   2.52700   33.07000  1.000 9.15682  ? 247 MET   B CG  1 
ATOM   3552 S  SD  . MET   B 1 203 ? 3.43500   2.15800   33.92800  1.000 9.19682  ? 247 MET   B SD  1 
ATOM   3553 C  CE  . MET   B 1 203 ? 3.42300   0.37600   33.86500  1.000 5.44682  ? 247 MET   B CE  1 
ATOM   3554 N  N   . GLU   B 1 204 ? -0.73200  3.39100   30.93400  1.000 8.27682  ? 248 GLU   B N   1 
ATOM   3555 C  CA  . GLU   B 1 204 ? -0.88800  3.07300   29.52000  1.000 7.42682  ? 248 GLU   B CA  1 
ATOM   3556 C  C   . GLU   B 1 204 ? 0.46800   3.21700   28.84500  1.000 8.92682  ? 248 GLU   B C   1 
ATOM   3557 O  O   . GLU   B 1 204 ? 1.10300   4.27100   28.94300  1.000 7.68682  ? 248 GLU   B O   1 
ATOM   3558 C  CB  . GLU   B 1 204 ? -1.93600  3.97700   28.87200  1.000 9.87682  ? 248 GLU   B CB  1 
ATOM   3559 C  CG  . GLU   B 1 204 ? -2.28700  3.59800   27.44300  1.000 12.80682 ? 248 GLU   B CG  1 
ATOM   3560 C  CD  . GLU   B 1 204 ? -3.46900  4.38000   26.90300  1.000 15.68682 ? 248 GLU   B CD  1 
ATOM   3561 O  OE1 . GLU   B 1 204 ? -4.48400  4.51000   27.62000  1.000 14.36682 ? 248 GLU   B OE1 1 
ATOM   3562 O  OE2 . GLU   B 1 204 ? -3.38300  4.85700   25.75400  1.000 17.59682 ? 248 GLU   B OE2 1 
ATOM   3563 N  N   . LEU   B 1 205 ? 0.91300   2.16000   28.17700  1.000 6.98682  ? 249 LEU   B N   1 
ATOM   3564 C  CA  . LEU   B 1 205 ? 2.21000   2.14600   27.50500  1.000 9.27682  ? 249 LEU   B CA  1 
ATOM   3565 C  C   . LEU   B 1 205 ? 2.08900   2.68000   26.07200  1.000 9.23682  ? 249 LEU   B C   1 
ATOM   3566 O  O   . LEU   B 1 205 ? 1.31600   2.14300   25.27200  1.000 6.50682  ? 249 LEU   B O   1 
ATOM   3567 C  CB  . LEU   B 1 205 ? 2.76600   0.72400   27.50300  1.000 7.22682  ? 249 LEU   B CB  1 
ATOM   3568 C  CG  . LEU   B 1 205 ? 3.03700   0.09900   28.87900  1.000 10.59682 ? 249 LEU   B CG  1 
ATOM   3569 C  CD1 . LEU   B 1 205 ? 3.47300   -1.35900  28.72700  1.000 10.43682 ? 249 LEU   B CD1 1 
ATOM   3570 C  CD2 . LEU   B 1 205 ? 4.04800   0.89900   29.66600  1.000 9.55682  ? 249 LEU   B CD2 1 
ATOM   3571 N  N   . CYS   B 1 206 ? 2.87800   3.71500   25.74500  1.000 7.29682  ? 250 CYS   B N   1 
ATOM   3572 C  CA  . CYS   B 1 206 ? 2.86500   4.31600   24.40500  1.000 12.24682 ? 250 CYS   B CA  1 
ATOM   3573 C  C   . CYS   B 1 206 ? 3.16400   3.30100   23.30900  1.000 10.35682 ? 250 CYS   B C   1 
ATOM   3574 O  O   . CYS   B 1 206 ? 4.16400   2.58000   23.38400  1.000 12.39682 ? 250 CYS   B O   1 
ATOM   3575 C  CB  . CYS   B 1 206 ? 3.92100   5.42000   24.29200  1.000 15.94682 ? 250 CYS   B CB  1 
ATOM   3576 S  SG  . CYS   B 1 206 ? 3.74100   6.81000   25.34200  1.000 25.19682 ? 250 CYS   B SG  1 
ATOM   3577 N  N   . GLY   B 1 207 ? 2.35800   3.33000   22.23900  1.000 8.59682  ? 251 GLY   B N   1 
ATOM   3578 C  CA  . GLY   B 1 207 ? 2.61800   2.56700   21.02200  1.000 8.11682  ? 251 GLY   B CA  1 
ATOM   3579 C  C   . GLY   B 1 207 ? 2.61600   1.05300   21.14000  1.000 11.00682 ? 251 GLY   B C   1 
ATOM   3580 O  O   . GLY   B 1 207 ? 2.97000   0.34700   20.18500  1.000 10.41682 ? 251 GLY   B O   1 
ATOM   3581 N  N   . ALA   B 1 208 ? 2.17500   0.53600   22.28000  1.000 7.05682  ? 252 ALA   B N   1 
ATOM   3582 C  CA  . ALA   B 1 208 ? 2.34500   -0.87500  22.59600  1.000 11.81682 ? 252 ALA   B CA  1 
ATOM   3583 C  C   . ALA   B 1 208 ? 1.14100   -1.70900  22.15300  1.000 6.95682  ? 252 ALA   B C   1 
ATOM   3584 O  O   . ALA   B 1 208 ? 0.01500   -1.21700  22.02300  1.000 9.05682  ? 252 ALA   B O   1 
ATOM   3585 C  CB  . ALA   B 1 208 ? 2.57600   -1.05300  24.09600  1.000 6.52682  ? 252 ALA   B CB  1 
ATOM   3586 N  N   . THR   B 1 209 ? 1.39200   -2.99900  21.95400  1.000 6.42682  ? 253 THR   B N   1 
ATOM   3587 C  CA  . THR   B 1 209 ? 0.39300   -3.96100  21.50400  1.000 11.04682 ? 253 THR   B CA  1 
ATOM   3588 C  C   . THR   B 1 209 ? -0.01600  -4.90100  22.64100  1.000 9.11682  ? 253 THR   B C   1 
ATOM   3589 O  O   . THR   B 1 209 ? 0.54000   -4.88100  23.74500  1.000 9.63682  ? 253 THR   B O   1 
ATOM   3590 C  CB  . THR   B 1 209 ? 0.92600   -4.80200  20.34100  1.000 12.30682 ? 253 THR   B CB  1 
ATOM   3591 O  OG1 . THR   B 1 209 ? 1.92700   -5.68700  20.85200  1.000 15.02682 ? 253 THR   B OG1 1 
ATOM   3592 C  CG2 . THR   B 1 209 ? 1.54000   -3.93700  19.26200  1.000 10.50682 ? 253 THR   B CG2 1 
ATOM   3593 N  N   . HIS   B 1 210 ? -0.95000  -5.80000  22.31100  1.000 9.00682  ? 254 HIS   B N   1 
ATOM   3594 C  CA  . HIS   B 1 210 ? -1.47800  -6.75200  23.28500  1.000 8.22682  ? 254 HIS   B CA  1 
ATOM   3595 C  C   . HIS   B 1 210 ? -0.39700  -7.67100  23.85500  1.000 8.14682  ? 254 HIS   B C   1 
ATOM   3596 O  O   . HIS   B 1 210 ? -0.53900  -8.17700  24.97500  1.000 11.14682 ? 254 HIS   B O   1 
ATOM   3597 C  CB  . HIS   B 1 210 ? -2.57700  -7.57500  22.61600  1.000 10.75682 ? 254 HIS   B CB  1 
ATOM   3598 C  CG  . HIS   B 1 210 ? -3.41500  -8.36900  23.56600  1.000 11.95682 ? 254 HIS   B CG  1 
ATOM   3599 N  ND1 . HIS   B 1 210 ? -4.14900  -7.78900  24.57900  1.000 12.64682 ? 254 HIS   B ND1 1 
ATOM   3600 C  CD2 . HIS   B 1 210 ? -3.65900  -9.69800  23.63800  1.000 16.16682 ? 254 HIS   B CD2 1 
ATOM   3601 C  CE1 . HIS   B 1 210 ? -4.80400  -8.72700  25.23600  1.000 11.98682 ? 254 HIS   B CE1 1 
ATOM   3602 N  NE2 . HIS   B 1 210 ? -4.52400  -9.89500  24.68500  1.000 13.06682 ? 254 HIS   B NE2 1 
ATOM   3603 N  N   . PHE   B 1 211 ? 0.68600   -7.90700  23.11500  1.000 8.94682  ? 255 PHE   B N   1 
ATOM   3604 C  CA  . PHE   B 1 211 ? 1.69200   -8.87300  23.54600  1.000 9.61682  ? 255 PHE   B CA  1 
ATOM   3605 C  C   . PHE   B 1 211 ? 2.91800   -8.23200  24.18000  1.000 8.44682  ? 255 PHE   B C   1 
ATOM   3606 O  O   . PHE   B 1 211 ? 3.85800   -8.94900  24.55000  1.000 8.26682  ? 255 PHE   B O   1 
ATOM   3607 C  CB  . PHE   B 1 211 ? 2.07100   -9.77000  22.36100  1.000 10.23682 ? 255 PHE   B CB  1 
ATOM   3608 C  CG  . PHE   B 1 211 ? 0.90700   -10.56400 21.84900  1.000 14.46682 ? 255 PHE   B CG  1 
ATOM   3609 C  CD1 . PHE   B 1 211 ? 0.46100   -11.67800 22.54400  1.000 17.42682 ? 255 PHE   B CD1 1 
ATOM   3610 C  CD2 . PHE   B 1 211 ? 0.21000   -10.15900 20.72000  1.000 16.21682 ? 255 PHE   B CD2 1 
ATOM   3611 C  CE1 . PHE   B 1 211 ? -0.63700  -12.40500 22.09200  1.000 17.06682 ? 255 PHE   B CE1 1 
ATOM   3612 C  CE2 . PHE   B 1 211 ? -0.89400  -10.87700 20.26600  1.000 14.39682 ? 255 PHE   B CE2 1 
ATOM   3613 C  CZ  . PHE   B 1 211 ? -1.31400  -12.00000 20.95200  1.000 17.96682 ? 255 PHE   B CZ  1 
ATOM   3614 N  N   . ALA   B 1 212 ? 2.90900   -6.91700  24.36600  1.000 7.89682  ? 256 ALA   B N   1 
ATOM   3615 C  CA  . ALA   B 1 212 ? 3.97800   -6.26600  25.11900  1.000 9.71682  ? 256 ALA   B CA  1 
ATOM   3616 C  C   . ALA   B 1 212 ? 4.26600   -6.92600  26.46600  1.000 9.91682  ? 256 ALA   B C   1 
ATOM   3617 O  O   . ALA   B 1 212 ? 5.45500   -7.06300  26.80900  1.000 8.96682  ? 256 ALA   B O   1 
ATOM   3618 C  CB  . ALA   B 1 212 ? 3.64900   -4.77300  25.29200  1.000 7.32682  ? 256 ALA   B CB  1 
ATOM   3619 N  N   . PRO   B 1 213 ? 3.28100   -7.37600  27.25300  1.000 9.17682  ? 257 PRO   B N   1 
ATOM   3620 C  CA  . PRO   B 1 213 ? 3.61900   -7.95100  28.56600  1.000 8.25682  ? 257 PRO   B CA  1 
ATOM   3621 C  C   . PRO   B 1 213 ? 4.40800   -9.24900  28.49700  1.000 7.58682  ? 257 PRO   B C   1 
ATOM   3622 O  O   . PRO   B 1 213 ? 4.91300   -9.68600  29.54000  1.000 9.33682  ? 257 PRO   B O   1 
ATOM   3623 C  CB  . PRO   B 1 213 ? 2.24800   -8.17600  29.21600  1.000 7.67682  ? 257 PRO   B CB  1 
ATOM   3624 C  CG  . PRO   B 1 213 ? 1.36700   -7.16900  28.57300  1.000 9.60682  ? 257 PRO   B CG  1 
ATOM   3625 C  CD  . PRO   B 1 213 ? 1.82500   -7.14500  27.14000  1.000 8.86682  ? 257 PRO   B CD  1 
ATOM   3626 N  N   . ASN   B 1 214 ? 4.55200   -9.85400  27.31800  1.000 5.41682  ? 258 ASN   B N   1 
ATOM   3627 C  CA  . ASN   B 1 214 ? 5.20000   -11.14900 27.16400  1.000 7.73682  ? 258 ASN   B CA  1 
ATOM   3628 C  C   . ASN   B 1 214 ? 6.69000   -11.05800 26.84000  1.000 10.96682 ? 258 ASN   B C   1 
ATOM   3629 O  O   . ASN   B 1 214 ? 7.33400   -12.09900 26.70600  1.000 14.23682 ? 258 ASN   B O   1 
ATOM   3630 C  CB  . ASN   B 1 214 ? 4.50500   -11.96700 26.07600  1.000 10.11682 ? 258 ASN   B CB  1 
ATOM   3631 C  CG  . ASN   B 1 214 ? 3.01600   -12.13000 26.32200  1.000 13.80682 ? 258 ASN   B CG  1 
ATOM   3632 O  OD1 . ASN   B 1 214 ? 2.19500   -11.77500 25.47400  1.000 12.69682 ? 258 ASN   B OD1 1 
ATOM   3633 N  ND2 . ASN   B 1 214 ? 2.66200   -12.68000 27.47100  1.000 7.70682  ? 258 ASN   B ND2 1 
ATOM   3634 N  N   . ILE   B 1 215 ? 7.25800   -9.86500  26.72200  1.000 9.64682  ? 259 ILE   B N   1 
ATOM   3635 C  CA  . ILE   B 1 215 ? 8.71300   -9.75100  26.59200  1.000 8.62682  ? 259 ILE   B CA  1 
ATOM   3636 C  C   . ILE   B 1 215 ? 9.23100   -8.83200  27.69000  1.000 7.83682  ? 259 ILE   B C   1 
ATOM   3637 O  O   . ILE   B 1 215 ? 8.47900   -7.97000  28.17100  1.000 8.65682  ? 259 ILE   B O   1 
ATOM   3638 C  CB  . ILE   B 1 215 ? 9.12600   -9.21800  25.21100  1.000 11.88682 ? 259 ILE   B CB  1 
ATOM   3639 C  CG1 . ILE   B 1 215 ? 8.46800   -7.85400  24.96100  1.000 13.38682 ? 259 ILE   B CG1 1 
ATOM   3640 C  CG2 . ILE   B 1 215 ? 8.81000   -10.23200 24.10900  1.000 11.45682 ? 259 ILE   B CG2 1 
ATOM   3641 C  CD1 . ILE   B 1 215 ? 9.01500   -7.14300  23.73500  1.000 10.39682 ? 259 ILE   B CD1 1 
ATOM   3642 N  N   . PRO   B 1 216 ? 10.49400  -8.96500  28.10400  1.000 11.56682 ? 260 PRO   B N   1 
ATOM   3643 C  CA  . PRO   B 1 216 ? 11.03000  -8.09000  29.15200  1.000 10.21682 ? 260 PRO   B CA  1 
ATOM   3644 C  C   . PRO   B 1 216 ? 10.77800  -6.62300  28.84000  1.000 9.82682  ? 260 PRO   B C   1 
ATOM   3645 O  O   . PRO   B 1 216 ? 11.04600  -6.14100  27.73300  1.000 9.64682  ? 260 PRO   B O   1 
ATOM   3646 C  CB  . PRO   B 1 216 ? 12.52600  -8.42700  29.15700  1.000 9.68682  ? 260 PRO   B CB  1 
ATOM   3647 C  CG  . PRO   B 1 216 ? 12.55300  -9.88000  28.74400  1.000 12.05682 ? 260 PRO   B CG  1 
ATOM   3648 C  CD  . PRO   B 1 216 ? 11.49100  -9.96700  27.66600  1.000 9.21682  ? 260 PRO   B CD  1 
ATOM   3649 N  N   . ASN   B 1 217 ? 10.23800  -5.92500  29.83300  1.000 8.20682  ? 261 ASN   B N   1 
ATOM   3650 C  CA  . ASN   B 1 217 ? 9.81600   -4.53300  29.70300  1.000 8.56682  ? 261 ASN   B CA  1 
ATOM   3651 C  C   . ASN   B 1 217 ? 10.08900  -3.87200  31.05000  1.000 6.93682  ? 261 ASN   B C   1 
ATOM   3652 O  O   . ASN   B 1 217 ? 9.41800   -4.18300  32.04300  1.000 7.13682  ? 261 ASN   B O   1 
ATOM   3653 C  CB  . ASN   B 1 217 ? 8.33900   -4.45200  29.31400  1.000 8.12682  ? 261 ASN   B CB  1 
ATOM   3654 C  CG  . ASN   B 1 217 ? 7.86600   -3.02800  29.07200  1.000 11.24682 ? 261 ASN   B CG  1 
ATOM   3655 O  OD1 . ASN   B 1 217 ? 8.14200   -2.13500  29.86400  1.000 8.63682  ? 261 ASN   B OD1 1 
ATOM   3656 N  ND2 . ASN   B 1 217 ? 7.15900   -2.81200  27.96500  1.000 5.94682  ? 261 ASN   B ND2 1 
ATOM   3657 N  N   . THR   B 1 218 ? 11.07900  -2.97200  31.08500  1.000 6.59682  ? 262 THR   B N   1 
ATOM   3658 C  CA  . THR   B 1 218 ? 11.49700  -2.36700  32.35500  1.000 8.61682  ? 262 THR   B CA  1 
ATOM   3659 C  C   . THR   B 1 218 ? 10.43300  -1.44100  32.93000  1.000 8.81682  ? 262 THR   B C   1 
ATOM   3660 O  O   . THR   B 1 218 ? 10.32500  -1.31400  34.15700  1.000 6.84682  ? 262 THR   B O   1 
ATOM   3661 C  CB  . THR   B 1 218 ? 12.81100  -1.60100  32.17500  1.000 11.19682 ? 262 THR   B CB  1 
ATOM   3662 O  OG1 . THR   B 1 218 ? 13.83800  -2.52200  31.79300  1.000 15.01682 ? 262 THR   B OG1 1 
ATOM   3663 C  CG2 . THR   B 1 218 ? 13.21400  -0.88800  33.47700  1.000 12.65682 ? 262 THR   B CG2 1 
ATOM   3664 N  N   . THR   B 1 219 ? 9.64100   -0.79000  32.07300  1.000 6.63682  ? 263 THR   B N   1 
ATOM   3665 C  CA  . THR   B 1 219 ? 8.54800   0.03300   32.58200  1.000 7.62682  ? 263 THR   B CA  1 
ATOM   3666 C  C   . THR   B 1 219 ? 7.53000   -0.82100  33.33800  1.000 7.15682  ? 263 THR   B C   1 
ATOM   3667 O  O   . THR   B 1 219 ? 7.09200   -0.45300  34.43400  1.000 9.67682  ? 263 THR   B O   1 
ATOM   3668 C  CB  . THR   B 1 219 ? 7.88300   0.79600   31.43400  1.000 7.31682  ? 263 THR   B CB  1 
ATOM   3669 O  OG1 . THR   B 1 219 ? 8.89300   1.41000   30.62300  1.000 7.90682  ? 263 THR   B OG1 1 
ATOM   3670 C  CG2 . THR   B 1 219 ? 6.94200   1.91700   31.98500  1.000 5.13682  ? 263 THR   B CG2 1 
ATOM   3671 N  N   . ILE   B 1 220 ? 7.15600   -1.97700  32.77800  1.000 6.76682  ? 264 ILE   B N   1 
ATOM   3672 C  CA  . ILE   B 1 220 ? 6.26400   -2.89100  33.49100  1.000 9.78682  ? 264 ILE   B CA  1 
ATOM   3673 C  C   . ILE   B 1 220 ? 6.92700   -3.39000  34.77500  1.000 7.94682  ? 264 ILE   B C   1 
ATOM   3674 O  O   . ILE   B 1 220 ? 6.34400   -3.32100  35.85900  1.000 8.07682  ? 264 ILE   B O   1 
ATOM   3675 C  CB  . ILE   B 1 220 ? 5.84800   -4.06500  32.58400  1.000 7.97682  ? 264 ILE   B CB  1 
ATOM   3676 C  CG1 . ILE   B 1 220 ? 4.98000   -3.56900  31.41900  1.000 9.64682  ? 264 ILE   B CG1 1 
ATOM   3677 C  CG2 . ILE   B 1 220 ? 5.10600   -5.12900  33.39900  1.000 8.64682  ? 264 ILE   B CG2 1 
ATOM   3678 C  CD1 . ILE   B 1 220 ? 4.55600   -4.67200  30.42300  1.000 8.89682  ? 264 ILE   B CD1 1 
ATOM   3679 N  N   . ALA   B 1 221 ? 8.16600   -3.88200  34.67200  1.000 6.70682  ? 265 ALA   B N   1 
ATOM   3680 C  CA  . ALA   B 1 221 ? 8.81800   -4.49900  35.82300  1.000 5.62682  ? 265 ALA   B CA  1 
ATOM   3681 C  C   . ALA   B 1 221 ? 8.94700   -3.53300  36.99900  1.000 8.84682  ? 265 ALA   B C   1 
ATOM   3682 O  O   . ALA   B 1 221 ? 8.69500   -3.90600  38.15500  1.000 8.71682  ? 265 ALA   B O   1 
ATOM   3683 C  CB  . ALA   B 1 221 ? 10.19400  -5.02800  35.42200  1.000 6.65682  ? 265 ALA   B CB  1 
ATOM   3684 N  N   . LYS   B 1 222 ? 9.33600   -2.28300  36.73500  1.000 6.86682  ? 266 LYS   B N   1 
ATOM   3685 C  CA  . LYS   B 1 222 ? 9.65100   -1.39900  37.85600  1.000 9.80682  ? 266 LYS   B CA  1 
ATOM   3686 C  C   . LYS   B 1 222 ? 8.40200   -1.02300  38.64900  1.000 10.87682 ? 266 LYS   B C   1 
ATOM   3687 O  O   . LYS   B 1 222 ? 8.46300   -0.90800  39.88300  1.000 7.18682  ? 266 LYS   B O   1 
ATOM   3688 C  CB  . LYS   B 1 222 ? 10.38700  -0.15200  37.36900  1.000 10.79682 ? 266 LYS   B CB  1 
ATOM   3689 C  CG  . LYS   B 1 222 ? 9.55400   0.80000   36.55200  1.000 8.87682  ? 266 LYS   B CG  1 
ATOM   3690 C  CD  . LYS   B 1 222 ? 10.41400  1.87300   35.90000  1.000 12.55682 ? 266 LYS   B CD  1 
ATOM   3691 C  CE  . LYS   B 1 222 ? 10.85500  2.93300   36.89100  1.000 11.61682 ? 266 LYS   B CE  1 
ATOM   3692 N  NZ  . LYS   B 1 222 ? 11.33800  4.15600   36.18400  1.000 12.27682 ? 266 LYS   B NZ  1 
ATOM   3693 N  N   . TYR   B 1 223 ? 7.25700   -0.87200  37.98200  1.000 8.87682  ? 267 TYR   B N   1 
ATOM   3694 C  CA  . TYR   B 1 223 ? 6.04800   -0.51200  38.70700  1.000 9.07682  ? 267 TYR   B CA  1 
ATOM   3695 C  C   . TYR   B 1 223 ? 5.26800   -1.72300  39.19600  1.000 7.04682  ? 267 TYR   B C   1 
ATOM   3696 O  O   . TYR   B 1 223 ? 4.53000   -1.60100  40.17900  1.000 8.09682  ? 267 TYR   B O   1 
ATOM   3697 C  CB  . TYR   B 1 223 ? 5.18500   0.41700   37.84700  1.000 5.25682  ? 267 TYR   B CB  1 
ATOM   3698 C  CG  . TYR   B 1 223 ? 5.94500   1.69700   37.62500  1.000 7.98682  ? 267 TYR   B CG  1 
ATOM   3699 C  CD1 . TYR   B 1 223 ? 6.37800   2.44800   38.70800  1.000 9.61682  ? 267 TYR   B CD1 1 
ATOM   3700 C  CD2 . TYR   B 1 223 ? 6.30300   2.11400   36.35300  1.000 10.48682 ? 267 TYR   B CD2 1 
ATOM   3701 C  CE1 . TYR   B 1 223 ? 7.12600   3.59700   38.53200  1.000 11.23682 ? 267 TYR   B CE1 1 
ATOM   3702 C  CE2 . TYR   B 1 223 ? 7.03900   3.26900   36.16200  1.000 7.42682  ? 267 TYR   B CE2 1 
ATOM   3703 C  CZ  . TYR   B 1 223 ? 7.44900   4.00200   37.25800  1.000 10.96682 ? 267 TYR   B CZ  1 
ATOM   3704 O  OH  . TYR   B 1 223 ? 8.18600   5.14900   37.08600  1.000 9.73682  ? 267 TYR   B OH  1 
ATOM   3705 N  N   . VAL   B 1 224 ? 5.45500   -2.88800  38.57400  1.000 8.24682  ? 268 VAL   B N   1 
ATOM   3706 C  CA  . VAL   B 1 224 ? 4.97000   -4.13700  39.16300  1.000 7.71682  ? 268 VAL   B CA  1 
ATOM   3707 C  C   . VAL   B 1 224 ? 5.66600   -4.38700  40.49800  1.000 7.03682  ? 268 VAL   B C   1 
ATOM   3708 O  O   . VAL   B 1 224 ? 5.02700   -4.70100  41.50900  1.000 9.45682  ? 268 VAL   B O   1 
ATOM   3709 C  CB  . VAL   B 1 224 ? 5.17400   -5.30600  38.17900  1.000 8.35682  ? 268 VAL   B CB  1 
ATOM   3710 C  CG1 . VAL   B 1 224 ? 5.03300   -6.65100  38.89300  1.000 6.87682  ? 268 VAL   B CG1 1 
ATOM   3711 C  CG2 . VAL   B 1 224 ? 4.14300   -5.22700  37.04400  1.000 5.92682  ? 268 VAL   B CG2 1 
ATOM   3712 N  N   . ILE   B 1 225 ? 6.98600   -4.21700  40.52600  1.000 5.85682  ? 269 ILE   B N   1 
ATOM   3713 C  CA  . ILE   B 1 225 ? 7.74400   -4.39800  41.76100  1.000 9.07682  ? 269 ILE   B CA  1 
ATOM   3714 C  C   . ILE   B 1 225 ? 7.30900   -3.37900  42.81600  1.000 9.45682  ? 269 ILE   B C   1 
ATOM   3715 O  O   . ILE   B 1 225 ? 7.11400   -3.71900  43.99300  1.000 7.88682  ? 269 ILE   B O   1 
ATOM   3716 C  CB  . ILE   B 1 225 ? 9.25700   -4.30900  41.46800  1.000 9.94682  ? 269 ILE   B CB  1 
ATOM   3717 C  CG1 . ILE   B 1 225 ? 9.73400   -5.56100  40.72200  1.000 9.04682  ? 269 ILE   B CG1 1 
ATOM   3718 C  CG2 . ILE   B 1 225 ? 10.05500  -4.12700  42.77200  1.000 9.77682  ? 269 ILE   B CG2 1 
ATOM   3719 C  CD1 . ILE   B 1 225 ? 11.06700  -5.37100  39.98500  1.000 10.81682 ? 269 ILE   B CD1 1 
ATOM   3720 N  N   . SER   B 1 226 ? 7.16700   -2.10700  42.41500  1.000 7.50682  ? 270 SER   B N   1 
ATOM   3721 C  CA  . SER   B 1 226 ? 6.76700   -1.07700  43.37400  1.000 9.44682  ? 270 SER   B CA  1 
ATOM   3722 C  C   . SER   B 1 226 ? 5.36800   -1.35000  43.91900  1.000 9.26682  ? 270 SER   B C   1 
ATOM   3723 O  O   . SER   B 1 226 ? 5.10600   -1.13500  45.10600  1.000 8.48682  ? 270 SER   B O   1 
ATOM   3724 C  CB  . SER   B 1 226 ? 6.82700   0.31500   42.73500  1.000 12.05682 ? 270 SER   B CB  1 
ATOM   3725 O  OG  . SER   B 1 226 ? 8.15100   0.66800   42.34100  1.000 12.65682 ? 270 SER   B OG  1 
ATOM   3726 N  N   . TRP   B 1 227 ? 4.46000   -1.83500  43.06900  1.000 8.53682  ? 271 TRP   B N   1 
ATOM   3727 C  CA  . TRP   B 1 227 ? 3.09600   -2.09000  43.51700  1.000 8.24682  ? 271 TRP   B CA  1 
ATOM   3728 C  C   . TRP   B 1 227 ? 3.05600   -3.24500  44.51100  1.000 8.92682  ? 271 TRP   B C   1 
ATOM   3729 O  O   . TRP   B 1 227 ? 2.37600   -3.16300  45.53900  1.000 8.52682  ? 271 TRP   B O   1 
ATOM   3730 C  CB  . TRP   B 1 227 ? 2.18200   -2.37500  42.32600  1.000 6.13682  ? 271 TRP   B CB  1 
ATOM   3731 C  CG  . TRP   B 1 227 ? 0.71500   -2.29400  42.67500  1.000 6.85682  ? 271 TRP   B CG  1 
ATOM   3732 C  CD1 . TRP   B 1 227 ? -0.13400  -3.33300  42.99500  1.000 7.82682  ? 271 TRP   B CD1 1 
ATOM   3733 C  CD2 . TRP   B 1 227 ? -0.05800  -1.09700  42.78400  1.000 6.75682  ? 271 TRP   B CD2 1 
ATOM   3734 N  NE1 . TRP   B 1 227 ? -1.40100  -2.84200  43.26500  1.000 8.38682  ? 271 TRP   B NE1 1 
ATOM   3735 C  CE2 . TRP   B 1 227 ? -1.37200  -1.47200  43.16000  1.000 8.61682  ? 271 TRP   B CE2 1 
ATOM   3736 C  CE3 . TRP   B 1 227 ? 0.23600   0.26100   42.61700  1.000 5.51682  ? 271 TRP   B CE3 1 
ATOM   3737 C  CZ2 . TRP   B 1 227 ? -2.38800  -0.53400  43.34800  1.000 8.15682  ? 271 TRP   B CZ2 1 
ATOM   3738 C  CZ3 . TRP   B 1 227 ? -0.77000  1.18800   42.80400  1.000 7.84682  ? 271 TRP   B CZ3 1 
ATOM   3739 C  CH2 . TRP   B 1 227 ? -2.06600  0.78900   43.15500  1.000 8.50682  ? 271 TRP   B CH2 1 
ATOM   3740 N  N   . LEU   B 1 228 ? 3.79900   -4.32100  44.23700  1.000 8.63682  ? 272 LEU   B N   1 
ATOM   3741 C  CA  . LEU   B 1 228 ? 3.81500   -5.44600  45.17100  1.000 8.68682  ? 272 LEU   B CA  1 
ATOM   3742 C  C   . LEU   B 1 228 ? 4.48500   -5.06000  46.48800  1.000 11.14682 ? 272 LEU   B C   1 
ATOM   3743 O  O   . LEU   B 1 228 ? 4.02000   -5.45400  47.56700  1.000 9.53682  ? 272 LEU   B O   1 
ATOM   3744 C  CB  . LEU   B 1 228 ? 4.52000   -6.64500  44.53700  1.000 7.39682  ? 272 LEU   B CB  1 
ATOM   3745 C  CG  . LEU   B 1 228 ? 3.88800   -7.26300  43.28600  1.000 6.54682  ? 272 LEU   B CG  1 
ATOM   3746 C  CD1 . LEU   B 1 228 ? 4.84800   -8.27100  42.64900  1.000 9.99682  ? 272 LEU   B CD1 1 
ATOM   3747 C  CD2 . LEU   B 1 228 ? 2.55800   -7.93300  43.59900  1.000 7.14682  ? 272 LEU   B CD2 1 
ATOM   3748 N  N   . LYS   B 1 229 ? 5.58000   -4.29300  46.42600  1.000 7.13682  ? 273 LYS   B N   1 
ATOM   3749 C  CA  . LYS   B 1 229 ? 6.23600   -3.84800  47.65400  1.000 9.01682  ? 273 LYS   B CA  1 
ATOM   3750 C  C   . LYS   B 1 229 ? 5.27600   -3.04200  48.51400  1.000 7.38682  ? 273 LYS   B C   1 
ATOM   3751 O  O   . LYS   B 1 229 ? 5.12900   -3.29800  49.71400  1.000 7.72682  ? 273 LYS   B O   1 
ATOM   3752 C  CB  . LYS   B 1 229 ? 7.48000   -3.01400  47.32500  1.000 6.67682  ? 273 LYS   B CB  1 
ATOM   3753 C  CG  . LYS   B 1 229 ? 8.68200   -3.82000  46.83700  1.000 7.64682  ? 273 LYS   B CG  1 
ATOM   3754 C  CD  . LYS   B 1 229 ? 9.39900   -4.51300  47.98700  1.000 8.08682  ? 273 LYS   B CD  1 
ATOM   3755 C  CE  . LYS   B 1 229 ? 10.76300  -5.04500  47.56200  1.000 14.79682 ? 273 LYS   B CE  1 
ATOM   3756 N  NZ  . LYS   B 1 229 ? 11.45100  -5.74600  48.69600  1.000 12.52682 ? 273 LYS   B NZ  1 
ATOM   3757 N  N   . ARG   B 1 230 ? 4.59000   -2.07500  47.90500  1.000 5.76682  ? 274 ARG   B N   1 
ATOM   3758 C  CA  . ARG   B 1 230 ? 3.74200   -1.17500  48.68100  1.000 6.90682  ? 274 ARG   B CA  1 
ATOM   3759 C  C   . ARG   B 1 230 ? 2.57900   -1.91400  49.33500  1.000 8.81682  ? 274 ARG   B C   1 
ATOM   3760 O  O   . ARG   B 1 230 ? 2.20200   -1.60000  50.47100  1.000 8.76682  ? 274 ARG   B O   1 
ATOM   3761 C  CB  . ARG   B 1 230 ? 3.22900   -0.04100  47.78500  1.000 8.32682  ? 274 ARG   B CB  1 
ATOM   3762 C  CG  . ARG   B 1 230 ? 2.15100   0.81300   48.41600  1.000 6.64682  ? 274 ARG   B CG  1 
ATOM   3763 C  CD  . ARG   B 1 230 ? 2.65300   1.58300   49.62300  1.000 9.68682  ? 274 ARG   B CD  1 
ATOM   3764 N  NE  . ARG   B 1 230 ? 1.56500   2.34000   50.22400  1.000 13.20682 ? 274 ARG   B NE  1 
ATOM   3765 C  CZ  . ARG   B 1 230 ? 0.65300   1.81400   51.03000  1.000 12.39682 ? 274 ARG   B CZ  1 
ATOM   3766 N  NH1 . ARG   B 1 230 ? 0.69300   0.53700   51.38000  1.000 13.18682 ? 274 ARG   B NH1 1 
ATOM   3767 N  NH2 . ARG   B 1 230 ? -0.33600  2.57900   51.47600  1.000 13.56682 ? 274 ARG   B NH2 1 
ATOM   3768 N  N   . PHE   B 1 231 ? 1.99100   -2.89200  48.64800  1.000 8.44682  ? 275 PHE   B N   1 
ATOM   3769 C  CA  . PHE   B 1 231 ? 0.77900   -3.50700  49.18300  1.000 10.76682 ? 275 PHE   B CA  1 
ATOM   3770 C  C   . PHE   B 1 231 ? 0.95600   -4.93300  49.67900  1.000 9.98682  ? 275 PHE   B C   1 
ATOM   3771 O  O   . PHE   B 1 231 ? 0.29600   -5.30600  50.65100  1.000 12.13682 ? 275 PHE   B O   1 
ATOM   3772 C  CB  . PHE   B 1 231 ? -0.35200  -3.44400  48.15200  1.000 7.25682  ? 275 PHE   B CB  1 
ATOM   3773 C  CG  . PHE   B 1 231 ? -0.71800  -2.02700  47.77800  1.000 9.42682  ? 275 PHE   B CG  1 
ATOM   3774 C  CD1 . PHE   B 1 231 ? -1.44200  -1.23100  48.65000  1.000 9.68682  ? 275 PHE   B CD1 1 
ATOM   3775 C  CD2 . PHE   B 1 231 ? -0.28800  -1.47700  46.58200  1.000 9.49682  ? 275 PHE   B CD2 1 
ATOM   3776 C  CE1 . PHE   B 1 231 ? -1.76300  0.09000   48.32300  1.000 10.88682 ? 275 PHE   B CE1 1 
ATOM   3777 C  CE2 . PHE   B 1 231 ? -0.59400  -0.15900  46.24900  1.000 7.60682  ? 275 PHE   B CE2 1 
ATOM   3778 C  CZ  . PHE   B 1 231 ? -1.32400  0.62600   47.12000  1.000 8.81682  ? 275 PHE   B CZ  1 
ATOM   3779 N  N   . VAL   B 1 232 ? 1.85000   -5.73400  49.09100  1.000 9.83682  ? 276 VAL   B N   1 
ATOM   3780 C  CA  . VAL   B 1 232 ? 2.12300   -7.04200  49.69100  1.000 10.39682 ? 276 VAL   B CA  1 
ATOM   3781 C  C   . VAL   B 1 232 ? 2.94200   -6.88500  50.97100  1.000 13.67682 ? 276 VAL   B C   1 
ATOM   3782 O  O   . VAL   B 1 232 ? 2.66000   -7.53900  51.98300  1.000 7.95682  ? 276 VAL   B O   1 
ATOM   3783 C  CB  . VAL   B 1 232 ? 2.81500   -7.98200  48.68900  1.000 11.62682 ? 276 VAL   B CB  1 
ATOM   3784 C  CG1 . VAL   B 1 232 ? 3.23000   -9.29000  49.36600  1.000 13.80682 ? 276 VAL   B CG1 1 
ATOM   3785 C  CG2 . VAL   B 1 232 ? 1.89300   -8.27800  47.54800  1.000 5.65682  ? 276 VAL   B CG2 1 
ATOM   3786 N  N   . ASP   B 1 233 ? 3.96000   -6.01600  50.94500  1.000 11.41682 ? 277 ASP   B N   1 
ATOM   3787 C  CA  . ASP   B 1 233 ? 4.86800   -5.76900  52.06700  1.000 10.86682 ? 277 ASP   B CA  1 
ATOM   3788 C  C   . ASP   B 1 233 ? 4.48300   -4.55500  52.90400  1.000 13.16682 ? 277 ASP   B C   1 
ATOM   3789 O  O   . ASP   B 1 233 ? 5.18500   -4.24500  53.87600  1.000 12.57682 ? 277 ASP   B O   1 
ATOM   3790 C  CB  . ASP   B 1 233 ? 6.30600   -5.55800  51.56100  1.000 10.14682 ? 277 ASP   B CB  1 
ATOM   3791 C  CG  . ASP   B 1 233 ? 6.91500   -6.81000  50.94000  1.000 15.07682 ? 277 ASP   B CG  1 
ATOM   3792 O  OD1 . ASP   B 1 233 ? 6.20500   -7.83600  50.84800  1.000 14.95682 ? 277 ASP   B OD1 1 
ATOM   3793 O  OD2 . ASP   B 1 233 ? 8.11200   -6.76300  50.54800  1.000 12.28682 ? 277 ASP   B OD2 1 
ATOM   3794 N  N   . GLU   B 1 234 ? 3.42300   -3.83400  52.53100  1.000 10.87682 ? 278 GLU   B N   1 
ATOM   3795 C  CA  . GLU   B 1 234 ? 3.05600   -2.58000  53.19000  1.000 11.62682 ? 278 GLU   B CA  1 
ATOM   3796 C  C   . GLU   B 1 234 ? 4.22100   -1.59400  53.20400  1.000 11.41682 ? 278 GLU   B C   1 
ATOM   3797 O  O   . GLU   B 1 234 ? 4.33200   -0.76400  54.11000  1.000 12.63682 ? 278 GLU   B O   1 
ATOM   3798 C  CB  . GLU   B 1 234 ? 2.54200   -2.82500  54.61200  1.000 12.15682 ? 278 GLU   B CB  1 
ATOM   3799 C  CG  . GLU   B 1 234 ? 1.25300   -3.62600  54.66000  1.000 17.39682 ? 278 GLU   B CG  1 
ATOM   3800 C  CD  . GLU   B 1 234 ? 0.83200   -3.97300  56.08200  1.000 30.41682 ? 278 GLU   B CD  1 
ATOM   3801 O  OE1 . GLU   B 1 234 ? 1.38500   -3.37900  57.03000  1.000 28.15682 ? 278 GLU   B OE1 1 
ATOM   3802 O  OE2 . GLU   B 1 234 ? -0.04600  -4.84700  56.25100  1.000 31.89682 ? 278 GLU   B OE2 1 
ATOM   3803 N  N   . ASP   B 1 235 ? 5.09400   -1.67600  52.20000  1.000 9.38682  ? 279 ASP   B N   1 
ATOM   3804 C  CA  . ASP   B 1 235 ? 6.39700   -1.00500  52.24000  1.000 11.40682 ? 279 ASP   B CA  1 
ATOM   3805 C  C   . ASP   B 1 235 ? 6.25400   0.39300   51.64200  1.000 12.02682 ? 279 ASP   B C   1 
ATOM   3806 O  O   . ASP   B 1 235 ? 6.34400   0.58100   50.42500  1.000 11.65682 ? 279 ASP   B O   1 
ATOM   3807 C  CB  . ASP   B 1 235 ? 7.43700   -1.84500  51.50500  1.000 12.49682 ? 279 ASP   B CB  1 
ATOM   3808 C  CG  . ASP   B 1 235 ? 8.87300   -1.40400  51.76900  1.000 10.71682 ? 279 ASP   B CG  1 
ATOM   3809 O  OD1 . ASP   B 1 235 ? 9.11400   -0.24600  52.16000  1.000 12.92682 ? 279 ASP   B OD1 1 
ATOM   3810 O  OD2 . ASP   B 1 235 ? 9.77400   -2.23200  51.54800  1.000 10.76682 ? 279 ASP   B OD2 1 
ATOM   3811 N  N   . THR   B 1 236 ? 6.05100   1.38800   52.50700  1.000 9.54682  ? 280 THR   B N   1 
ATOM   3812 C  CA  . THR   B 1 236 ? 5.88800   2.75400   52.03300  1.000 12.19682 ? 280 THR   B CA  1 
ATOM   3813 C  C   . THR   B 1 236 ? 7.18600   3.37000   51.51000  1.000 15.25682 ? 280 THR   B C   1 
ATOM   3814 O  O   . THR   B 1 236 ? 7.15000   4.50800   51.02300  1.000 11.23682 ? 280 THR   B O   1 
ATOM   3815 C  CB  . THR   B 1 236 ? 5.30400   3.61100   53.15100  1.000 17.24682 ? 280 THR   B CB  1 
ATOM   3816 O  OG1 . THR   B 1 236 ? 6.08400   3.42500   54.33800  1.000 13.38682 ? 280 THR   B OG1 1 
ATOM   3817 C  CG2 . THR   B 1 236 ? 3.85000   3.19500   53.41900  1.000 11.54682 ? 280 THR   B CG2 1 
ATOM   3818 N  N   . ARG   B 1 237 ? 8.32400   2.66700   51.58500  1.000 12.72682 ? 281 ARG   B N   1 
ATOM   3819 C  CA  . ARG   B 1 237 ? 9.51700   3.17400   50.91000  1.000 11.10682 ? 281 ARG   B CA  1 
ATOM   3820 C  C   . ARG   B 1 237 ? 9.32800   3.22900   49.40200  1.000 13.75682 ? 281 ARG   B C   1 
ATOM   3821 O  O   . ARG   B 1 237 ? 10.09100  3.92200   48.72000  1.000 14.03682 ? 281 ARG   B O   1 
ATOM   3822 C  CB  . ARG   B 1 237 ? 10.74300  2.31600   51.21900  1.000 14.06682 ? 281 ARG   B CB  1 
ATOM   3823 C  CG  . ARG   B 1 237 ? 11.09300  2.19700   52.69800  1.000 12.53682 ? 281 ARG   B CG  1 
ATOM   3824 C  CD  . ARG   B 1 237 ? 12.31400  1.33700   52.87300  1.000 11.71682 ? 281 ARG   B CD  1 
ATOM   3825 N  NE  . ARG   B 1 237 ? 12.04900  -0.04100  52.48500  1.000 12.92682 ? 281 ARG   B NE  1 
ATOM   3826 C  CZ  . ARG   B 1 237 ? 12.96900  -0.99400  52.42300  1.000 13.80682 ? 281 ARG   B CZ  1 
ATOM   3827 N  NH1 . ARG   B 1 237 ? 14.23400  -0.75200  52.72200  1.000 13.06682 ? 281 ARG   B NH1 1 
ATOM   3828 N  NH2 . ARG   B 1 237 ? 12.60800  -2.22300  52.05800  1.000 10.84682 ? 281 ARG   B NH2 1 
ATOM   3829 N  N   . TYR   B 1 238 ? 8.33800   2.50500   48.86700  1.000 9.65682  ? 282 TYR   B N   1 
ATOM   3830 C  CA  . TYR   B 1 238 ? 8.08300   2.47000   47.43200  1.000 12.94682 ? 282 TYR   B CA  1 
ATOM   3831 C  C   . TYR   B 1 238 ? 6.96900   3.41800   46.99200  1.000 12.05682 ? 282 TYR   B C   1 
ATOM   3832 O  O   . TYR   B 1 238 ? 6.75100   3.57400   45.78400  1.000 13.28682 ? 282 TYR   B O   1 
ATOM   3833 C  CB  . TYR   B 1 238 ? 7.78700   1.02300   46.99700  1.000 10.13682 ? 282 TYR   B CB  1 
ATOM   3834 C  CG  . TYR   B 1 238 ? 9.02700   0.16000   47.06200  1.000 7.89682  ? 282 TYR   B CG  1 
ATOM   3835 C  CD1 . TYR   B 1 238 ? 9.48600   -0.35800  48.27900  1.000 8.93682  ? 282 TYR   B CD1 1 
ATOM   3836 C  CD2 . TYR   B 1 238 ? 9.77900   -0.09200  45.91700  1.000 10.51682 ? 282 TYR   B CD2 1 
ATOM   3837 C  CE1 . TYR   B 1 238 ? 10.64600  -1.12500  48.34400  1.000 10.80682 ? 282 TYR   B CE1 1 
ATOM   3838 C  CE2 . TYR   B 1 238 ? 10.93700  -0.86500  45.97100  1.000 13.23682 ? 282 TYR   B CE2 1 
ATOM   3839 C  CZ  . TYR   B 1 238 ? 11.36800  -1.37100  47.18400  1.000 10.91682 ? 282 TYR   B CZ  1 
ATOM   3840 O  OH  . TYR   B 1 238 ? 12.51700  -2.13000  47.22700  1.000 11.00682 ? 282 TYR   B OH  1 
ATOM   3841 N  N   . SER   B 1 239 ? 6.29400   4.08700   47.93800  1.000 12.06682 ? 283 SER   B N   1 
ATOM   3842 C  CA  . SER   B 1 239 ? 5.32000   5.12600   47.59200  1.000 11.69682 ? 283 SER   B CA  1 
ATOM   3843 C  C   . SER   B 1 239 ? 5.92700   6.23900   46.73800  1.000 14.49682 ? 283 SER   B C   1 
ATOM   3844 O  O   . SER   B 1 239 ? 5.22200   6.84600   45.92000  1.000 13.70682 ? 283 SER   B O   1 
ATOM   3845 C  CB  . SER   B 1 239 ? 4.72600   5.73700   48.86500  1.000 10.96682 ? 283 SER   B CB  1 
ATOM   3846 O  OG  . SER   B 1 239 ? 3.92500   4.80400   49.56100  1.000 17.02682 ? 283 SER   B OG  1 
ATOM   3847 N  N   . GLN   B 1 240 ? 7.22000   6.53100   46.91800  1.000 13.92682 ? 284 GLN   B N   1 
ATOM   3848 C  CA  . GLN   B 1 240 ? 7.85100   7.61700   46.17300  1.000 13.61682 ? 284 GLN   B CA  1 
ATOM   3849 C  C   . GLN   B 1 240 ? 7.82400   7.37000   44.66900  1.000 14.33682 ? 284 GLN   B C   1 
ATOM   3850 O  O   . GLN   B 1 240 ? 7.87600   8.32600   43.88300  1.000 13.44682 ? 284 GLN   B O   1 
ATOM   3851 C  CB  . GLN   B 1 240 ? 9.29400   7.80200   46.63600  1.000 13.55682 ? 284 GLN   B CB  1 
ATOM   3852 C  CG  . GLN   B 1 240 ? 10.17200  6.55700   46.42600  1.000 13.87682 ? 284 GLN   B CG  1 
ATOM   3853 C  CD  . GLN   B 1 240 ? 11.56900  6.72800   46.99800  1.000 21.71682 ? 284 GLN   B CD  1 
ATOM   3854 O  OE1 . GLN   B 1 240 ? 12.29900  7.64100   46.61600  1.000 18.32682 ? 284 GLN   B OE1 1 
ATOM   3855 N  NE2 . GLN   B 1 240 ? 11.94600  5.84900   47.91700  1.000 14.86682 ? 284 GLN   B NE2 1 
ATOM   3856 N  N   . PHE   B 1 241 ? 7.75000   6.10200   44.25200  1.000 11.33682 ? 285 PHE   B N   1 
ATOM   3857 C  CA  . PHE   B 1 241 ? 7.73500   5.75100   42.84000  1.000 12.11682 ? 285 PHE   B CA  1 
ATOM   3858 C  C   . PHE   B 1 241 ? 6.34000   5.74300   42.23800  1.000 12.64682 ? 285 PHE   B C   1 
ATOM   3859 O  O   . PHE   B 1 241 ? 6.20900   5.88300   41.01800  1.000 10.75682 ? 285 PHE   B O   1 
ATOM   3860 C  CB  . PHE   B 1 241 ? 8.38800   4.38200   42.63600  1.000 10.10682 ? 285 PHE   B CB  1 
ATOM   3861 C  CG  . PHE   B 1 241 ? 9.71700   4.26200   43.30000  1.000 15.13682 ? 285 PHE   B CG  1 
ATOM   3862 C  CD1 . PHE   B 1 241 ? 10.77200  5.06500   42.89400  1.000 13.27682 ? 285 PHE   B CD1 1 
ATOM   3863 C  CD2 . PHE   B 1 241 ? 9.91000   3.37700   44.35800  1.000 12.06682 ? 285 PHE   B CD2 1 
ATOM   3864 C  CE1 . PHE   B 1 241 ? 11.99600  4.97000   43.50500  1.000 15.20682 ? 285 PHE   B CE1 1 
ATOM   3865 C  CE2 . PHE   B 1 241 ? 11.13100  3.27900   44.97600  1.000 12.71682 ? 285 PHE   B CE2 1 
ATOM   3866 C  CZ  . PHE   B 1 241 ? 12.18200  4.07400   44.55000  1.000 18.82682 ? 285 PHE   B CZ  1 
ATOM   3867 N  N   . LEU   B 1 242 ? 5.30400   5.60700   43.06000  1.000 13.38682 ? 286 LEU   B N   1 
ATOM   3868 C  CA  . LEU   B 1 242 ? 3.92400   5.53700   42.59900  1.000 9.92682  ? 286 LEU   B CA  1 
ATOM   3869 C  C   . LEU   B 1 242 ? 3.17600   6.85600   42.69400  1.000 10.91682 ? 286 LEU   B C   1 
ATOM   3870 O  O   . LEU   B 1 242 ? 2.27500   7.10700   41.88300  1.000 15.08682 ? 286 LEU   B O   1 
ATOM   3871 C  CB  . LEU   B 1 242 ? 3.17000   4.48100   43.41000  1.000 9.28682  ? 286 LEU   B CB  1 
ATOM   3872 C  CG  . LEU   B 1 242 ? 3.81600   3.09500   43.36300  1.000 10.69682 ? 286 LEU   B CG  1 
ATOM   3873 C  CD1 . LEU   B 1 242 ? 3.15400   2.19700   44.37800  1.000 10.18682 ? 286 LEU   B CD1 1 
ATOM   3874 C  CD2 . LEU   B 1 242 ? 3.69600   2.50700   41.96500  1.000 11.08682 ? 286 LEU   B CD2 1 
ATOM   3875 N  N   . CYS   B 1 243 ? 3.52200   7.69700   43.66000  1.000 10.63682 ? 287 CYS   B N   1 
ATOM   3876 C  CA  . CYS   B 1 243 ? 2.84400   8.96200   43.91600  1.000 14.46682 ? 287 CYS   B CA  1 
ATOM   3877 C  C   . CYS   B 1 243 ? 3.89700   10.04900  44.12300  1.000 17.16682 ? 287 CYS   B C   1 
ATOM   3878 O  O   . CYS   B 1 243 ? 4.77300   9.89200   44.98200  1.000 19.29682 ? 287 CYS   B O   1 
ATOM   3879 C  CB  . CYS   B 1 243 ? 1.94700   8.85600   45.14900  1.000 15.85682 ? 287 CYS   B CB  1 
ATOM   3880 S  SG  . CYS   B 1 243 ? 0.75900   7.50100   45.11000  1.000 17.03682 ? 287 CYS   B SG  1 
ATOM   3881 N  N   . PRO   B 1 244 ? 3.86800   11.15400  43.35700  1.000 16.34682 ? 288 PRO   B N   1 
ATOM   3882 C  CA  . PRO   B 1 244 ? 2.91500   11.40600  42.26300  1.000 16.35682 ? 288 PRO   B CA  1 
ATOM   3883 C  C   . PRO   B 1 244 ? 3.09800   10.46900  41.06300  1.000 14.06682 ? 288 PRO   B C   1 
ATOM   3884 O  O   . PRO   B 1 244 ? 4.05700   9.70400   41.04200  1.000 13.73682 ? 288 PRO   B O   1 
ATOM   3885 C  CB  . PRO   B 1 244 ? 3.20900   12.85800  41.87100  1.000 16.48682 ? 288 PRO   B CB  1 
ATOM   3886 C  CG  . PRO   B 1 244 ? 4.60500   13.09500  42.32100  1.000 18.07682 ? 288 PRO   B CG  1 
ATOM   3887 C  CD  . PRO   B 1 244 ? 4.75500   12.30800  43.58500  1.000 19.28682 ? 288 PRO   B CD  1 
ATOM   3888 N  N   . ASN   B 1 245 ? 2.16900   10.53000  40.11100  1.000 15.25682 ? 289 ASN   B N   1 
ATOM   3889 C  CA  . ASN   B 1 245 ? 2.14300   9.61400   38.97700  1.000 15.03682 ? 289 ASN   B CA  1 
ATOM   3890 C  C   . ASN   B 1 245 ? 3.50400   9.55000   38.27600  1.000 17.60682 ? 289 ASN   B C   1 
ATOM   3891 O  O   . ASN   B 1 245 ? 4.11500   10.59600  38.01500  1.000 15.53682 ? 289 ASN   B O   1 
ATOM   3892 C  CB  . ASN   B 1 245 ? 1.07200   10.05200  37.97400  1.000 19.12682 ? 289 ASN   B CB  1 
ATOM   3893 C  CG  . ASN   B 1 245 ? -0.34200  9.89000   38.51100  1.000 15.87682 ? 289 ASN   B CG  1 
ATOM   3894 O  OD1 . ASN   B 1 245 ? -0.56300  9.23900   39.53000  1.000 21.35682 ? 289 ASN   B OD1 1 
ATOM   3895 N  ND2 . ASN   B 1 245 ? -1.31000  10.46000  37.80600  1.000 17.27682 ? 289 ASN   B ND2 1 
ATOM   3896 N  N   . PRO   B 1 246 ? 4.00300   8.35300   37.95700  1.000 16.65682 ? 290 PRO   B N   1 
ATOM   3897 C  CA  . PRO   B 1 246 ? 5.20100   8.23500   37.11500  1.000 18.87682 ? 290 PRO   B CA  1 
ATOM   3898 C  C   . PRO   B 1 246 ? 5.05400   8.99100   35.80000  1.000 18.24682 ? 290 PRO   B C   1 
ATOM   3899 O  O   . PRO   B 1 246 ? 3.95600   9.11400   35.25800  1.000 15.09682 ? 290 PRO   B O   1 
ATOM   3900 C  CB  . PRO   B 1 246 ? 5.30400   6.72500   36.87000  1.000 18.48682 ? 290 PRO   B CB  1 
ATOM   3901 C  CG  . PRO   B 1 246 ? 4.62800   6.11400   38.07100  1.000 16.34682 ? 290 PRO   B CG  1 
ATOM   3902 C  CD  . PRO   B 1 246 ? 3.50500   7.04200   38.40900  1.000 14.13682 ? 290 PRO   B CD  1 
ATOM   3903 N  N   . THR   B 1 247 ? 6.18700   9.48500   35.27700  1.000 15.85682 ? 291 THR   B N   1 
ATOM   3904 C  CA  . THR   B 1 247 ? 6.19900   10.22500  34.01700  1.000 20.85682 ? 291 THR   B CA  1 
ATOM   3905 C  C   . THR   B 1 247 ? 7.22400   9.66000   33.03300  1.000 22.59682 ? 291 THR   B C   1 
ATOM   3906 O  O   . THR   B 1 247 ? 7.72400   10.39000  32.17500  1.000 18.59682 ? 291 THR   B O   1 
ATOM   3907 C  CB  . THR   B 1 247 ? 6.45800   11.72000  34.24800  1.000 23.30682 ? 291 THR   B CB  1 
ATOM   3908 O  OG1 . THR   B 1 247 ? 7.67600   11.89900  34.98200  1.000 25.81682 ? 291 THR   B OG1 1 
ATOM   3909 C  CG2 . THR   B 1 247 ? 5.31000   12.35800  35.01900  1.000 21.34682 ? 291 THR   B CG2 1 
ATOM   3910 N  N   . ASP   B 1 248 ? 7.53500   8.36200   33.14400  1.000 16.74682 ? 292 ASP   B N   1 
ATOM   3911 C  CA  . ASP   B 1 248 ? 8.46100   7.68700   32.23600  1.000 14.23682 ? 292 ASP   B CA  1 
ATOM   3912 C  C   . ASP   B 1 248 ? 8.12600   7.97600   30.78000  1.000 13.51682 ? 292 ASP   B C   1 
ATOM   3913 O  O   . ASP   B 1 248 ? 6.95600   8.09600   30.40200  1.000 9.84682  ? 292 ASP   B O   1 
ATOM   3914 C  CB  . ASP   B 1 248 ? 8.41000   6.17100   32.43900  1.000 11.27682 ? 292 ASP   B CB  1 
ATOM   3915 C  CG  . ASP   B 1 248 ? 8.88200   5.74400   33.79800  1.000 17.08682 ? 292 ASP   B CG  1 
ATOM   3916 O  OD1 . ASP   B 1 248 ? 8.37100   6.28800   34.80200  1.000 16.42682 ? 292 ASP   B OD1 1 
ATOM   3917 O  OD2 . ASP   B 1 248 ? 9.74900   4.84500   33.85200  1.000 14.69682 ? 292 ASP   B OD2 1 
ATOM   3918 N  N   . ARG   B 1 249 ? 9.18200   8.04200   29.95700  1.000 16.68682 ? 293 ARG   B N   1 
ATOM   3919 C  CA  . ARG   B 1 249 ? 9.03000   8.19600   28.51000  1.000 15.14682 ? 293 ARG   B CA  1 
ATOM   3920 C  C   . ARG   B 1 249 ? 8.03700   7.19600   27.92000  1.000 8.20682  ? 293 ARG   B C   1 
ATOM   3921 O  O   . ARG   B 1 249 ? 7.22500   7.54800   27.05800  1.000 13.91682 ? 293 ARG   B O   1 
ATOM   3922 C  CB  . ARG   B 1 249 ? 10.39700  8.03500   27.83300  1.000 15.49682 ? 293 ARG   B CB  1 
ATOM   3923 C  CG  . ARG   B 1 249 ? 10.37600  8.17200   26.31800  1.000 15.41682 ? 293 ARG   B CG  1 
ATOM   3924 C  CD  . ARG   B 1 249 ? 11.74600  7.84600   25.73200  1.000 18.33682 ? 293 ARG   B CD  1 
ATOM   3925 N  NE  . ARG   B 1 249 ? 11.74500  7.84600   24.27300  1.000 20.80682 ? 293 ARG   B NE  1 
ATOM   3926 C  CZ  . ARG   B 1 249 ? 12.59900  7.15400   23.52800  1.000 18.20682 ? 293 ARG   B CZ  1 
ATOM   3927 N  NH1 . ARG   B 1 249 ? 13.50500  6.36100   24.07300  1.000 18.56682 ? 293 ARG   B NH1 1 
ATOM   3928 N  NH2 . ARG   B 1 249 ? 12.52800  7.24400   22.20400  1.000 16.96682 ? 293 ARG   B NH2 1 
ATOM   3929 N  N   . ALA   B 1 250 ? 8.09900   5.94200   28.35600  1.000 8.69682  ? 294 ALA   B N   1 
ATOM   3930 C  CA  . ALA   B 1 250 ? 7.26600   4.90500   27.74900  1.000 8.45682  ? 294 ALA   B CA  1 
ATOM   3931 C  C   . ALA   B 1 250 ? 5.79300   4.99000   28.13800  1.000 10.82682 ? 294 ALA   B C   1 
ATOM   3932 O  O   . ALA   B 1 250 ? 5.00300   4.16600   27.64800  1.000 12.25682 ? 294 ALA   B O   1 
ATOM   3933 C  CB  . ALA   B 1 250 ? 7.80000   3.51600   28.11000  1.000 8.71682  ? 294 ALA   B CB  1 
ATOM   3934 N  N   . ILE   B 1 251 ? 5.40100   5.93700   28.98500  1.000 9.32682  ? 295 ILE   B N   1 
ATOM   3935 C  CA  . ILE   B 1 251 ? 4.05300   6.00500   29.54400  1.000 10.06682 ? 295 ILE   B CA  1 
ATOM   3936 C  C   . ILE   B 1 251 ? 3.29000   7.10900   28.81500  1.000 12.03682 ? 295 ILE   B C   1 
ATOM   3937 O  O   . ILE   B 1 251 ? 3.71900   8.26700   28.81800  1.000 13.24682 ? 295 ILE   B O   1 
ATOM   3938 C  CB  . ILE   B 1 251 ? 4.10100   6.26200   31.06500  1.000 10.28682 ? 295 ILE   B CB  1 
ATOM   3939 C  CG1 . ILE   B 1 251 ? 4.83300   5.12100   31.78500  1.000 8.90682  ? 295 ILE   B CG1 1 
ATOM   3940 C  CG2 . ILE   B 1 251 ? 2.70200   6.46500   31.66200  1.000 8.84682  ? 295 ILE   B CG2 1 
ATOM   3941 C  CD1 . ILE   B 1 251 ? 4.83300   5.26100   33.34200  1.000 10.25682 ? 295 ILE   B CD1 1 
ATOM   3942 N  N   . CYS   B 1 252 ? 2.14400   6.77000   28.21200  1.000 9.33682  ? 296 CYS   B N   1 
ATOM   3943 C  CA  . CYS   B 1 252 ? 1.33100   7.77700   27.52600  1.000 11.61682 ? 296 CYS   B CA  1 
ATOM   3944 C  C   . CYS   B 1 252 ? 0.14200   8.27800   28.33900  1.000 13.74682 ? 296 CYS   B C   1 
ATOM   3945 O  O   . CYS   B 1 252 ? -0.41000  9.33400   28.01300  1.000 12.05682 ? 296 CYS   B O   1 
ATOM   3946 C  CB  . CYS   B 1 252 ? 0.82900   7.23000   26.18100  1.000 19.77682 ? 296 CYS   B CB  1 
ATOM   3947 S  SG  . CYS   B 1 252 ? 1.95100   7.61900   24.79900  1.000 34.11682 ? 296 CYS   B SG  1 
ATOM   3948 N  N   . GLU   B 1 253 ? -0.27300  7.55200   29.37300  1.000 9.99682  ? 297 GLU   B N   1 
ATOM   3949 C  CA  . GLU   B 1 253 ? -1.30000  8.02700   30.28800  1.000 10.44682 ? 297 GLU   B CA  1 
ATOM   3950 C  C   . GLU   B 1 253 ? -1.11700  7.29900   31.61000  1.000 10.31682 ? 297 GLU   B C   1 
ATOM   3951 O  O   . GLU   B 1 253 ? -0.75200  6.12300   31.62000  1.000 8.49682  ? 297 GLU   B O   1 
ATOM   3952 C  CB  . GLU   B 1 253 ? -2.72500  7.79400   29.75500  1.000 12.34682 ? 297 GLU   B CB  1 
ATOM   3953 C  CG  . GLU   B 1 253 ? -3.78200  7.88700   30.85500  1.000 16.71682 ? 297 GLU   B CG  1 
ATOM   3954 C  CD  . GLU   B 1 253 ? -5.03000  8.64500   30.45400  1.000 27.79682 ? 297 GLU   B CD  1 
ATOM   3955 O  OE1 . GLU   B 1 253 ? -5.63800  8.29200   29.42300  1.000 30.30682 ? 297 GLU   B OE1 1 
ATOM   3956 O  OE2 . GLU   B 1 253 ? -5.41000  9.59000   31.18500  1.000 25.38682 ? 297 GLU   B OE2 1 
ATOM   3957 N  N   . TYR   B 1 254 ? -1.35800  8.00800   32.71700  1.000 9.51682  ? 298 TYR   B N   1 
ATOM   3958 C  CA  . TYR   B 1 254 ? -1.33500  7.39900   34.04000  1.000 12.00682 ? 298 TYR   B CA  1 
ATOM   3959 C  C   . TYR   B 1 254 ? -2.42600  8.03200   34.88800  1.000 14.19682 ? 298 TYR   B C   1 
ATOM   3960 O  O   . TYR   B 1 254 ? -2.57000  9.25800   34.90300  1.000 15.04682 ? 298 TYR   B O   1 
ATOM   3961 C  CB  . TYR   B 1 254 ? 0.02900   7.57700   34.71600  1.000 12.41682 ? 298 TYR   B CB  1 
ATOM   3962 C  CG  . TYR   B 1 254 ? 0.32000   6.60300   35.84500  1.000 11.57682 ? 298 TYR   B CG  1 
ATOM   3963 C  CD1 . TYR   B 1 254 ? -0.26000  6.76300   37.09900  1.000 14.03682 ? 298 TYR   B CD1 1 
ATOM   3964 C  CD2 . TYR   B 1 254 ? 1.21300   5.55400   35.67000  1.000 9.76682  ? 298 TYR   B CD2 1 
ATOM   3965 C  CE1 . TYR   B 1 254 ? 0.02600   5.89400   38.14600  1.000 11.54682 ? 298 TYR   B CE1 1 
ATOM   3966 C  CE2 . TYR   B 1 254 ? 1.49600   4.67700   36.70600  1.000 11.20682 ? 298 TYR   B CE2 1 
ATOM   3967 C  CZ  . TYR   B 1 254 ? 0.89800   4.85400   37.94200  1.000 12.27682 ? 298 TYR   B CZ  1 
ATOM   3968 O  OH  . TYR   B 1 254 ? 1.18300   4.00200   38.98700  1.000 11.44682 ? 298 TYR   B OH  1 
ATOM   3969 N  N   . ARG   B 1 255 ? -3.19600  7.19600   35.57600  1.000 9.02682  ? 299 ARG   B N   1 
ATOM   3970 C  CA  . ARG   B 1 255 ? -4.25300  7.64300   36.46500  1.000 9.06682  ? 299 ARG   B CA  1 
ATOM   3971 C  C   . ARG   B 1 255 ? -4.07000  6.91500   37.79000  1.000 10.97682 ? 299 ARG   B C   1 
ATOM   3972 O  O   . ARG   B 1 255 ? -3.54300  5.80000   37.82400  1.000 10.07682 ? 299 ARG   B O   1 
ATOM   3973 C  CB  . ARG   B 1 255 ? -5.64500  7.35600   35.88500  1.000 8.66682  ? 299 ARG   B CB  1 
ATOM   3974 C  CG  . ARG   B 1 255 ? -5.92800  7.98200   34.52700  1.000 13.20682 ? 299 ARG   B CG  1 
ATOM   3975 C  CD  . ARG   B 1 255 ? -7.30800  7.55100   34.02500  1.000 14.67682 ? 299 ARG   B CD  1 
ATOM   3976 N  NE  . ARG   B 1 255 ? -7.48800  7.75200   32.59200  1.000 13.33682 ? 299 ARG   B NE  1 
ATOM   3977 C  CZ  . ARG   B 1 255 ? -8.60500  7.47700   31.93000  1.000 17.18682 ? 299 ARG   B CZ  1 
ATOM   3978 N  NH1 . ARG   B 1 255 ? -9.67600  7.00000   32.54700  1.000 16.00682 ? 299 ARG   B NH1 1 
ATOM   3979 N  NH2 . ARG   B 1 255 ? -8.64900  7.68300   30.61500  1.000 18.23682 ? 299 ARG   B NH2 1 
ATOM   3980 N  N   . SER   B 1 256 ? -4.47700  7.55600   38.88500  1.000 10.83682 ? 300 SER   B N   1 
ATOM   3981 C  CA  . SER   B 1 256 ? -4.28700  6.95300   40.20000  1.000 10.13682 ? 300 SER   B CA  1 
ATOM   3982 C  C   . SER   B 1 256 ? -5.21400  7.61500   41.20900  1.000 11.60682 ? 300 SER   B C   1 
ATOM   3983 O  O   . SER   B 1 256 ? -5.76100  8.69100   40.97100  1.000 10.49682 ? 300 SER   B O   1 
ATOM   3984 C  CB  . SER   B 1 256 ? -2.84200  7.07800   40.67500  1.000 6.79682  ? 300 SER   B CB  1 
ATOM   3985 O  OG  . SER   B 1 256 ? -2.60000  8.39800   41.11300  1.000 15.13682 ? 300 SER   B OG  1 
ATOM   3986 N  N   . THR   B 1 257 ? -5.35700  6.96300   42.36100  1.000 9.39682  ? 301 THR   B N   1 
ATOM   3987 C  CA  . THR   B 1 257 ? -5.99900  7.57400   43.51800  1.000 12.03682 ? 301 THR   B CA  1 
ATOM   3988 C  C   . THR   B 1 257 ? -4.97700  7.96600   44.58000  1.000 13.80682 ? 301 THR   B C   1 
ATOM   3989 O  O   . THR   B 1 257 ? -5.29500  7.99400   45.77100  1.000 13.18682 ? 301 THR   B O   1 
ATOM   3990 C  CB  . THR   B 1 257 ? -7.06200  6.65100   44.11600  1.000 13.26682 ? 301 THR   B CB  1 
ATOM   3991 O  OG1 . THR   B 1 257 ? -6.47500  5.38300   44.44300  1.000 12.99682 ? 301 THR   B OG1 1 
ATOM   3992 C  CG2 . THR   B 1 257 ? -8.22300  6.45900   43.12700  1.000 8.69682  ? 301 THR   B CG2 1 
ATOM   3993 N  N   . CYS   B 1 258 ? -3.74100  8.26500   44.15500  1.000 10.77682 ? 302 CYS   B N   1 
ATOM   3994 C  CA  . CYS   B 1 258 ? -2.72200  8.86100   45.00800  1.000 13.46682 ? 302 CYS   B CA  1 
ATOM   3995 C  C   . CYS   B 1 258 ? -3.29500  10.03900  45.79400  1.000 16.90682 ? 302 CYS   B C   1 
ATOM   3996 O  O   . CYS   B 1 258 ? -4.23200  10.70400  45.32800  1.000 13.30682 ? 302 CYS   B O   1 
ATOM   3997 C  CB  . CYS   B 1 258 ? -1.52700  9.32500   44.16800  1.000 15.76682 ? 302 CYS   B CB  1 
ATOM   3998 S  SG  . CYS   B 1 258 ? -0.47400  7.99200   43.54700  1.000 19.13682 ? 302 CYS   B SG  1 
ATOM   3999 N  N   . PRO   B 1 259 ? -2.74400  10.35200  46.97400  1.000 14.49682 ? 303 PRO   B N   1 
ATOM   4000 C  CA  . PRO   B 1 259 ? -1.59500  9.67400   47.59300  1.000 16.21682 ? 303 PRO   B CA  1 
ATOM   4001 C  C   . PRO   B 1 259 ? -1.93100  8.37000   48.32100  1.000 16.05682 ? 303 PRO   B C   1 
ATOM   4002 O  O   . PRO   B 1 259 ? -3.01700  8.21900   48.87800  1.000 14.16682 ? 303 PRO   B O   1 
ATOM   4003 C  CB  . PRO   B 1 259 ? -1.07900  10.71400  48.59100  1.000 15.13682 ? 303 PRO   B CB  1 
ATOM   4004 C  CG  . PRO   B 1 259 ? -2.31800  11.45900  49.00200  1.000 16.93682 ? 303 PRO   B CG  1 
ATOM   4005 C  CD  . PRO   B 1 259 ? -3.16600  11.53900  47.74200  1.000 19.53682 ? 303 PRO   B CD  1 
ATOM   4006 N  N   . TYR   B 1 260 ? -0.99000  7.43100   48.27900  1.000 14.83682 ? 304 TYR   B N   1 
ATOM   4007 C  CA  . TYR   B 1 260 ? -0.98000  6.27900   49.17600  1.000 17.78682 ? 304 TYR   B CA  1 
ATOM   4008 C  C   . TYR   B 1 260 ? 0.46900   5.80500   49.29100  1.000 22.55682 ? 304 TYR   B C   1 
ATOM   4009 O  O   . TYR   B 1 260 ? 1.37200   6.42800   48.71100  1.000 19.54682 ? 304 TYR   B O   1 
ATOM   4010 C  CB  . TYR   B 1 260 ? -1.90100  5.15700   48.68700  1.000 16.24682 ? 304 TYR   B CB  1 
ATOM   4011 C  CG  . TYR   B 1 260 ? -1.88600  4.92900   47.18700  1.000 12.55682 ? 304 TYR   B CG  1 
ATOM   4012 C  CD1 . TYR   B 1 260 ? -0.74100  4.48100   46.54100  1.000 13.36682 ? 304 TYR   B CD1 1 
ATOM   4013 C  CD2 . TYR   B 1 260 ? -3.03000  5.14000   46.42200  1.000 15.55682 ? 304 TYR   B CD2 1 
ATOM   4014 C  CE1 . TYR   B 1 260 ? -0.72900  4.26700   45.15500  1.000 14.89682 ? 304 TYR   B CE1 1 
ATOM   4015 C  CE2 . TYR   B 1 260 ? -3.03200  4.92200   45.04200  1.000 12.58682 ? 304 TYR   B CE2 1 
ATOM   4016 C  CZ  . TYR   B 1 260 ? -1.87700  4.48600   44.41800  1.000 14.20682 ? 304 TYR   B CZ  1 
ATOM   4017 O  OH  . TYR   B 1 260 ? -1.87200  4.27900   43.05400  1.000 14.32682 ? 304 TYR   B OH  1 
ATOM   4018 O  OXT . TYR   B 1 260 ? 0.78000   4.82500   49.97200  1.000 19.73682 ? 304 TYR   B OXT 1 
HETATM 4019 C  C1  . MPD   C 2 .   ? 25.08900  10.39800  11.57300  1.000 36.60682 ? 401 MPD   A C1  1 
HETATM 4020 C  C2  . MPD   C 2 .   ? 25.42700  10.23800  10.09400  1.000 33.81682 ? 401 MPD   A C2  1 
HETATM 4021 O  O2  . MPD   C 2 .   ? 24.72400  11.27100  9.35400   1.000 45.48682 ? 401 MPD   A O2  1 
HETATM 4022 C  CM  . MPD   C 2 .   ? 24.95100  8.88600   9.57700   1.000 26.92682 ? 401 MPD   A CM  1 
HETATM 4023 C  C3  . MPD   C 2 .   ? 26.92200  10.45700  9.88800   1.000 34.92682 ? 401 MPD   A C3  1 
HETATM 4024 C  C4  . MPD   C 2 .   ? 27.77300  9.23900   9.55000   1.000 36.58682 ? 401 MPD   A C4  1 
HETATM 4025 O  O4  . MPD   C 2 .   ? 28.94100  9.70200   8.89300   1.000 33.02682 ? 401 MPD   A O4  1 
HETATM 4026 C  C5  . MPD   C 2 .   ? 28.18200  8.44900   10.79700  1.000 43.20682 ? 401 MPD   A C5  1 
HETATM 4027 C  CAA . A1L0M D 3 .   ? 24.95200  -14.05000 23.24500  1.000 26.87682 ? 402 A1L0M A CAA 1 
HETATM 4028 C  CAB . A1L0M D 3 .   ? 25.20600  -13.27700 22.11600  1.000 26.01682 ? 402 A1L0M A CAB 1 
HETATM 4029 C  CAC . A1L0M D 3 .   ? 24.16200  -12.91900 21.26000  1.000 25.24682 ? 402 A1L0M A CAC 1 
HETATM 4030 C  CAD . A1L0M D 3 .   ? 22.88000  -13.36900 21.53300  1.000 17.19682 ? 402 A1L0M A CAD 1 
HETATM 4031 C  CAI . A1L0M D 3 .   ? 19.00300  -13.67600 21.26200  1.000 22.72682 ? 402 A1L0M A CAI 1 
HETATM 4032 C  CAJ . A1L0M D 3 .   ? 18.37300  -14.41400 22.46200  1.000 28.54682 ? 402 A1L0M A CAJ 1 
HETATM 4033 C  CAL . A1L0M D 3 .   ? 19.80700  -14.35700 24.37100  1.000 30.74682 ? 402 A1L0M A CAL 1 
HETATM 4034 C  CAM . A1L0M D 3 .   ? 19.48300  -14.99400 25.57000  1.000 43.14682 ? 402 A1L0M A CAM 1 
HETATM 4035 C  CAN . A1L0M D 3 .   ? 18.18800  -15.44200 25.82300  1.000 30.93682 ? 402 A1L0M A CAN 1 
HETATM 4036 C  CAO . A1L0M D 3 .   ? 17.91100  -16.08000 27.03200  1.000 44.54682 ? 402 A1L0M A CAO 1 
HETATM 4037 C  CAP . A1L0M D 3 .   ? 18.91300  -16.26900 27.98200  1.000 38.87682 ? 402 A1L0M A CAP 1 
HETATM 4038 C  CAQ . A1L0M D 3 .   ? 20.20700  -15.82500 27.72700  1.000 44.58682 ? 402 A1L0M A CAQ 1 
HETATM 4039 C  CAR . A1L0M D 3 .   ? 20.48700  -15.18800 26.52000  1.000 43.56682 ? 402 A1L0M A CAR 1 
HETATM 4040 C  CAS . A1L0M D 3 .   ? 22.63200  -14.12400 22.66700  1.000 35.01682 ? 402 A1L0M A CAS 1 
HETATM 4041 C  CAT . A1L0M D 3 .   ? 23.66400  -14.47200 23.52200  1.000 35.00682 ? 402 A1L0M A CAT 1 
HETATM 4042 C  CAU . A1L0M D 3 .   ? 25.96400  -14.44000 24.10800  1.000 39.84682 ? 402 A1L0M A CAU 1 
HETATM 4043 C  CAX . A1L0M D 3 .   ? 27.20800  -16.11100 23.22300  1.000 33.25682 ? 402 A1L0M A CAX 1 
HETATM 4044 O  OAF . A1L0M D 3 .   ? 21.47900  -11.62600 19.97700  1.000 19.80682 ? 402 A1L0M A OAF 1 
HETATM 4045 O  OAG . A1L0M D 3 .   ? 21.23900  -14.08200 19.43800  1.000 7.75682  ? 402 A1L0M A OAG 1 
HETATM 4046 O  OAH . A1L0M D 3 .   ? 20.30000  -13.18800 21.61300  1.000 36.56682 ? 402 A1L0M A OAH 1 
HETATM 4047 O  OAK . A1L0M D 3 .   ? 18.65800  -13.78600 23.72800  1.000 41.06682 ? 402 A1L0M A OAK 1 
HETATM 4048 O  OAV . A1L0M D 3 .   ? 25.73200  -14.65300 25.30000  1.000 49.31682 ? 402 A1L0M A OAV 1 
HETATM 4049 O  OAW . A1L0M D 3 .   ? 27.15400  -14.70400 23.49900  1.000 35.57682 ? 402 A1L0M A OAW 1 
HETATM 4050 P  PAE . A1L0M D 3 .   ? 21.53700  -12.98200 20.57100  1.000 19.87682 ? 402 A1L0M A PAE 1 
HETATM 4051 CA CA  . CA    E 4 .   ? 18.63500  -31.93300 10.82400  1.000 26.89682 ? 403 CA    A CA  1 
HETATM 4052 CA CA  . CA    F 4 .   ? 17.42200  9.96300   8.42900   1.000 43.81682 ? 404 CA    A CA  1 
HETATM 4053 CL CL  . CL    G 5 .   ? 17.32500  -5.54300  25.37000  1.000 10.35682 ? 405 CL    A CL  1 
HETATM 4054 C  C1  . MPD   H 2 .   ? 7.40600   7.09900   23.29900  1.000 22.44682 ? 401 MPD   B C1  1 
HETATM 4055 C  C2  . MPD   H 2 .   ? 7.86100   5.71300   22.84500  1.000 23.44682 ? 401 MPD   B C2  1 
HETATM 4056 O  O2  . MPD   H 2 .   ? 7.06800   4.74900   23.59100  1.000 24.22682 ? 401 MPD   B O2  1 
HETATM 4057 C  CM  . MPD   H 2 .   ? 9.33400   5.48400   23.18200  1.000 23.04682 ? 401 MPD   B CM  1 
HETATM 4058 C  C3  . MPD   H 2 .   ? 7.67100   5.50300   21.34000  1.000 19.06682 ? 401 MPD   B C3  1 
HETATM 4059 C  C4  . MPD   H 2 .   ? 6.23400   5.66200   20.85200  1.000 20.48682 ? 401 MPD   B C4  1 
HETATM 4060 O  O4  . MPD   H 2 .   ? 6.16100   5.85800   19.45300  1.000 27.83682 ? 401 MPD   B O4  1 
HETATM 4061 C  C5  . MPD   H 2 .   ? 5.44200   4.40400   21.13300  1.000 17.96682 ? 401 MPD   B C5  1 
HETATM 4062 C  C   . ACT   I 6 .   ? -13.82000 -20.77100 26.46200  1.000 30.82682 ? 402 ACT   B C   1 
HETATM 4063 O  O   . ACT   I 6 .   ? -13.98100 -21.19400 27.66600  1.000 31.99682 ? 402 ACT   B O   1 
HETATM 4064 O  OXT . ACT   I 6 .   ? -13.96400 -21.44800 25.45600  1.000 31.28682 ? 402 ACT   B OXT 1 
HETATM 4065 C  CH3 . ACT   I 6 .   ? -13.41500 -19.29200 26.38200  1.000 22.41682 ? 402 ACT   B CH3 1 
HETATM 4066 C  C   . ACT   J 6 .   ? -7.12100  6.10800   49.25900  1.000 38.64682 ? 403 ACT   B C   1 
HETATM 4067 O  O   . ACT   J 6 .   ? -6.63500  5.77800   48.11300  1.000 29.25682 ? 403 ACT   B O   1 
HETATM 4068 O  OXT . ACT   J 6 .   ? -7.49500  7.23200   49.57100  1.000 34.08682 ? 403 ACT   B OXT 1 
HETATM 4069 C  CH3 . ACT   J 6 .   ? -7.20000  4.92400   50.24500  1.000 28.70682 ? 403 ACT   B CH3 1 
HETATM 4070 C  CAA . A1L0M K 3 .   ? -10.12600 -14.16600 22.41500  1.000 28.37682 ? 404 A1L0M B CAA 1 
HETATM 4071 C  CAB . A1L0M K 3 .   ? -10.33500 -13.19700 23.38900  1.000 21.15682 ? 404 A1L0M B CAB 1 
HETATM 4072 C  CAC . A1L0M K 3 .   ? -9.27400  -12.79000 24.20300  1.000 23.39682 ? 404 A1L0M B CAC 1 
HETATM 4073 C  CAD . A1L0M K 3 .   ? -8.01700  -13.36900 24.06400  1.000 24.25682 ? 404 A1L0M B CAD 1 
HETATM 4074 C  CAI . A1L0M K 3 .   ? -4.64600  -14.15400 23.75900  1.000 32.59682 ? 404 A1L0M B CAI 1 
HETATM 4075 C  CAJ . A1L0M K 3 .   ? -4.45100  -13.91400 22.25000  1.000 38.75682 ? 404 A1L0M B CAJ 1 
HETATM 4076 C  CAL . A1L0M K 3 .   ? -4.67600  -14.96200 20.08200  1.000 42.24682 ? 404 A1L0M B CAL 1 
HETATM 4077 C  CAM . A1L0M K 3 .   ? -3.36300  -15.31200 19.73500  1.000 42.68682 ? 404 A1L0M B CAM 1 
HETATM 4078 C  CAN . A1L0M K 3 .   ? -2.85800  -14.93800 18.49300  1.000 52.40682 ? 404 A1L0M B CAN 1 
HETATM 4079 C  CAO . A1L0M K 3 .   ? -1.55400  -15.27100 18.12800  1.000 54.19682 ? 404 A1L0M B CAO 1 
HETATM 4080 C  CAP . A1L0M K 3 .   ? -0.74500  -15.98400 19.00700  1.000 55.29682 ? 404 A1L0M B CAP 1 
HETATM 4081 C  CAQ . A1L0M K 3 .   ? -1.24200  -16.36200 20.25000  1.000 49.37682 ? 404 A1L0M B CAQ 1 
HETATM 4082 C  CAR . A1L0M K 3 .   ? -2.54600  -16.03000 20.60800  1.000 42.45682 ? 404 A1L0M B CAR 1 
HETATM 4083 C  CAS . A1L0M K 3 .   ? -7.81400  -14.31900 23.07300  1.000 33.16682 ? 404 A1L0M B CAS 1 
HETATM 4084 C  CAT . A1L0M K 3 .   ? -8.86500  -14.71700 22.26100  1.000 36.01682 ? 404 A1L0M B CAT 1 
HETATM 4085 C  CAU . A1L0M K 3 .   ? -11.15800 -14.61100 21.58900  1.000 38.45682 ? 404 A1L0M B CAU 1 
HETATM 4086 C  CAX . A1L0M K 3 .   ? -11.88100 -16.16100 19.97800  1.000 30.92682 ? 404 A1L0M B CAX 1 
HETATM 4087 O  OAF . A1L0M K 3 .   ? -6.47000  -13.69400 26.40900  1.000 10.98682 ? 404 A1L0M B OAF 1 
HETATM 4088 O  OAG . A1L0M K 3 .   ? -6.73200  -11.38200 25.45600  1.000 19.20682 ? 404 A1L0M B OAG 1 
HETATM 4089 O  OAH . A1L0M K 3 .   ? -5.22500  -12.97300 24.33400  1.000 33.12682 ? 404 A1L0M B OAH 1 
HETATM 4090 O  OAK . A1L0M K 3 .   ? -4.89600  -15.05900 21.50500  1.000 39.69682 ? 404 A1L0M B OAK 1 
HETATM 4091 O  OAV . A1L0M K 3 .   ? -12.32200 -14.30300 21.83300  1.000 47.24682 ? 404 A1L0M B OAV 1 
HETATM 4092 O  OAW . A1L0M K 3 .   ? -10.78200 -15.42200 20.54500  1.000 39.41682 ? 404 A1L0M B OAW 1 
HETATM 4093 P  PAE . A1L0M K 3 .   ? -6.70500  -12.82400 25.07200  1.000 19.31682 ? 404 A1L0M B PAE 1 
HETATM 4094 CA CA  . CA    L 4 .   ? -3.97000  -30.25200 37.25800  1.000 30.86682 ? 405 CA    B CA  1 
HETATM 4095 CA CA  . CA    M 4 .   ? -2.70900  11.48900  34.35600  1.000 52.14682 ? 406 CA    B CA  1 
HETATM 4096 CL CL  . CL    N 5 .   ? -13.39000 -4.97800  22.27100  1.000 11.42682 ? 407 CL    B CL  1 
HETATM 4097 CL CL  . CL    O 5 .   ? -2.63900  -5.94000  19.38000  1.000 11.12682 ? 408 CL    B CL  1 
HETATM 4098 O  O   . HOH   P 7 .   ? 6.19000   -4.14300  -10.44600 1.000 21.24682 ? 501 HOH   A O   1 
HETATM 4099 O  O   . HOH   P 7 .   ? 22.89300  -25.28600 0.98100   1.000 19.14682 ? 502 HOH   A O   1 
HETATM 4100 O  O   . HOH   P 7 .   ? 19.70300  6.68000   16.19500  1.000 27.82682 ? 503 HOH   A O   1 
HETATM 4101 O  O   . HOH   P 7 .   ? 30.15100  3.62200   4.58800   1.000 19.98682 ? 504 HOH   A O   1 
HETATM 4102 O  O   . HOH   P 7 .   ? -8.40800  -15.14900 -9.42300  1.000 38.49682 ? 505 HOH   A O   1 
HETATM 4103 O  O   . HOH   P 7 .   ? 8.16700   -30.43600 1.63700   1.000 23.03682 ? 506 HOH   A O   1 
HETATM 4104 O  O   . HOH   P 7 .   ? 19.84600  -25.85100 -6.03900  1.000 29.16682 ? 507 HOH   A O   1 
HETATM 4105 O  O   . HOH   P 7 .   ? 16.15900  -9.25500  -9.31800  1.000 22.81682 ? 508 HOH   A O   1 
HETATM 4106 O  O   . HOH   P 7 .   ? 18.49200  7.27500   21.81800  1.000 18.96682 ? 509 HOH   A O   1 
HETATM 4107 O  O   . HOH   P 7 .   ? 0.60100   -10.03000 -11.78600 1.000 22.64682 ? 510 HOH   A O   1 
HETATM 4108 O  O   . HOH   P 7 .   ? -2.65000  -21.27400 7.56100   1.000 27.14682 ? 511 HOH   A O   1 
HETATM 4109 O  O   . HOH   P 7 .   ? 5.00100   4.03800   4.70200   1.000 25.33682 ? 512 HOH   A O   1 
HETATM 4110 O  O   . HOH   P 7 .   ? 1.41200   -28.61500 -7.59200  1.000 30.82682 ? 513 HOH   A O   1 
HETATM 4111 O  O   . HOH   P 7 .   ? 29.98600  -15.51200 5.18000   1.000 29.32682 ? 514 HOH   A O   1 
HETATM 4112 O  O   . HOH   P 7 .   ? 29.56300  -10.69700 -2.19600  1.000 15.41682 ? 515 HOH   A O   1 
HETATM 4113 O  O   . HOH   P 7 .   ? 0.30300   -6.51900  -3.67600  1.000 20.37682 ? 516 HOH   A O   1 
HETATM 4114 O  O   . HOH   P 7 .   ? 1.13000   -23.73700 12.26700  1.000 34.91682 ? 517 HOH   A O   1 
HETATM 4115 O  O   . HOH   P 7 .   ? -7.21000  4.57500   3.91200   1.000 32.08682 ? 518 HOH   A O   1 
HETATM 4116 O  O   . HOH   P 7 .   ? 21.82100  -10.84300 -5.99400  1.000 22.98682 ? 519 HOH   A O   1 
HETATM 4117 O  O   . HOH   P 7 .   ? 20.26200  5.16000   18.87300  1.000 20.64682 ? 520 HOH   A O   1 
HETATM 4118 O  O   . HOH   P 7 .   ? 33.36500  -9.67000  -3.18700  1.000 32.35682 ? 521 HOH   A O   1 
HETATM 4119 O  O   . HOH   P 7 .   ? 10.12200  -4.41100  -12.00100 1.000 29.02682 ? 522 HOH   A O   1 
HETATM 4120 O  O   . HOH   P 7 .   ? 4.17900   -11.40200 -3.83900  1.000 11.06682 ? 523 HOH   A O   1 
HETATM 4121 O  O   . HOH   P 7 .   ? 2.97900   -9.79400  -17.08000 1.000 38.05682 ? 524 HOH   A O   1 
HETATM 4122 O  O   . HOH   P 7 .   ? 2.04600   -20.20100 12.78100  1.000 25.07682 ? 525 HOH   A O   1 
HETATM 4123 O  O   . HOH   P 7 .   ? 12.19200  -28.24800 13.62000  1.000 17.59682 ? 526 HOH   A O   1 
HETATM 4124 O  O   . HOH   P 7 .   ? 15.68800  -7.60300  -7.03100  1.000 14.20682 ? 527 HOH   A O   1 
HETATM 4125 O  O   . HOH   P 7 .   ? -1.29500  -10.62900 -10.58900 1.000 22.69682 ? 528 HOH   A O   1 
HETATM 4126 O  O   . HOH   P 7 .   ? 16.45900  -2.38300  26.97300  1.000 22.79682 ? 529 HOH   A O   1 
HETATM 4127 O  O   . HOH   P 7 .   ? 28.37300  3.26300   15.94800  1.000 18.65682 ? 530 HOH   A O   1 
HETATM 4128 O  O   . HOH   P 7 .   ? 28.666    2.813     21.228    1.000 22.90682 ? 531 HOH   A O   1 
HETATM 4129 O  O   . HOH   P 7 .   ? 13.82300  2.55500   2.33400   1.000 12.50682 ? 532 HOH   A O   1 
HETATM 4130 O  O   . HOH   P 7 .   ? 11.98200  -16.29200 -12.62600 1.000 18.44682 ? 533 HOH   A O   1 
HETATM 4131 O  O   . HOH   P 7 .   ? 11.94400  5.40400   -5.35300  1.000 21.52682 ? 534 HOH   A O   1 
HETATM 4132 O  O   . HOH   P 7 .   ? 4.18000   2.16000   12.27700  1.000 14.29682 ? 535 HOH   A O   1 
HETATM 4133 O  O   . HOH   P 7 .   ? 22.668    12.600    8.377     1.000 32.18682 ? 536 HOH   A O   1 
HETATM 4134 O  O   . HOH   P 7 .   ? 19.04100  -31.83500 -2.29300  1.000 11.75682 ? 537 HOH   A O   1 
HETATM 4135 O  O   . HOH   P 7 .   ? 2.12300   -17.37200 11.81700  1.000 11.48682 ? 538 HOH   A O   1 
HETATM 4136 O  O   . HOH   P 7 .   ? 20.77600  -6.47100  29.49100  1.000 15.64682 ? 539 HOH   A O   1 
HETATM 4137 O  O   . HOH   P 7 .   ? 1.00900   -13.74700 12.07200  1.000 18.79682 ? 540 HOH   A O   1 
HETATM 4138 O  O   . HOH   P 7 .   ? 11.62400  11.05800  4.79700   1.000 19.47682 ? 541 HOH   A O   1 
HETATM 4139 O  O   . HOH   P 7 .   ? 2.00000   -22.95700 -8.99300  1.000 22.73682 ? 542 HOH   A O   1 
HETATM 4140 O  O   . HOH   P 7 .   ? 10.50100  -8.31200  -13.44700 1.000 21.28682 ? 543 HOH   A O   1 
HETATM 4141 O  O   . HOH   P 7 .   ? 23.60400  4.97000   18.71900  1.000 23.67682 ? 544 HOH   A O   1 
HETATM 4142 O  O   . HOH   P 7 .   ? 11.03000  -34.61800 13.81900  1.000 26.67682 ? 545 HOH   A O   1 
HETATM 4143 O  O   . HOH   P 7 .   ? 24.00600  -26.62300 6.85700   1.000 15.27682 ? 546 HOH   A O   1 
HETATM 4144 O  O   . HOH   P 7 .   ? 2.28900   -3.00700  16.04000  1.000 22.31682 ? 547 HOH   A O   1 
HETATM 4145 O  O   . HOH   P 7 .   ? 25.69300  -27.19700 15.24600  1.000 22.37682 ? 548 HOH   A O   1 
HETATM 4146 O  O   . HOH   P 7 .   ? 0.37300   -20.74600 -4.72000  1.000 18.96682 ? 549 HOH   A O   1 
HETATM 4147 O  O   . HOH   P 7 .   ? 32.892    -1.354    4.223     1.000 16.91682 ? 550 HOH   A O   1 
HETATM 4148 O  O   . HOH   P 7 .   ? 28.10500  4.96500   4.87600   1.000 15.06682 ? 551 HOH   A O   1 
HETATM 4149 O  O   . HOH   P 7 .   ? 8.33800   -20.47600 -11.58800 1.000 21.58682 ? 552 HOH   A O   1 
HETATM 4150 O  O   . HOH   P 7 .   ? 7.62400   -16.45900 -10.62900 1.000 13.45682 ? 553 HOH   A O   1 
HETATM 4151 O  O   . HOH   P 7 .   ? -4.41500  -2.27500  8.08100   1.000 24.49682 ? 554 HOH   A O   1 
HETATM 4152 O  O   . HOH   P 7 .   ? 10.68600  -25.78500 17.33900  1.000 21.40682 ? 555 HOH   A O   1 
HETATM 4153 O  O   . HOH   P 7 .   ? 1.12600   -6.36000  8.00900   1.000 14.09682 ? 556 HOH   A O   1 
HETATM 4154 O  O   . HOH   P 7 .   ? -0.62900  1.43500   -4.87700  1.000 20.06682 ? 557 HOH   A O   1 
HETATM 4155 O  O   . HOH   P 7 .   ? 5.66700   2.97900   -6.04000  1.000 11.98682 ? 558 HOH   A O   1 
HETATM 4156 O  O   . HOH   P 7 .   ? 6.25102   -13.10829 -7.09523  1.000 12.09757 ? 559 HOH   A O   1 
HETATM 4157 O  O   . HOH   P 7 .   ? -1.01700  -8.25100  -9.31900  1.000 24.36682 ? 560 HOH   A O   1 
HETATM 4158 O  O   . HOH   P 7 .   ? 32.60200  -1.96700  -0.17900  1.000 22.47682 ? 561 HOH   A O   1 
HETATM 4159 O  O   . HOH   P 7 .   ? 7.76600   7.06900   1.69900   1.000 16.00682 ? 562 HOH   A O   1 
HETATM 4160 O  O   . HOH   P 7 .   ? 18.55800  -21.26100 17.47100  1.000 13.11682 ? 563 HOH   A O   1 
HETATM 4161 O  O   . HOH   P 7 .   ? -4.98200  -3.33800  -7.80300  1.000 25.51682 ? 564 HOH   A O   1 
HETATM 4162 O  O   . HOH   P 7 .   ? 24.73700  6.69400   6.00600   1.000 13.69682 ? 565 HOH   A O   1 
HETATM 4163 O  O   . HOH   P 7 .   ? 36.066    -6.213    10.327    1.000 13.51682 ? 566 HOH   A O   1 
HETATM 4164 O  O   . HOH   P 7 .   ? -7.73600  -15.58600 -0.45900  1.000 28.75682 ? 567 HOH   A O   1 
HETATM 4165 O  O   . HOH   P 7 .   ? 17.55100  -25.74500 17.49600  1.000 20.50682 ? 568 HOH   A O   1 
HETATM 4166 O  O   . HOH   P 7 .   ? -4.66700  -14.94800 4.82100   1.000 19.20682 ? 569 HOH   A O   1 
HETATM 4167 O  O   . HOH   P 7 .   ? -8.289    -12.039   -0.471    1.000 23.17682 ? 570 HOH   A O   1 
HETATM 4168 O  O   . HOH   P 7 .   ? 30.84200  -13.02200 -1.52300  1.000 17.06682 ? 571 HOH   A O   1 
HETATM 4169 O  O   . HOH   P 7 .   ? 2.01800   -9.59300  -13.50600 1.000 25.18682 ? 572 HOH   A O   1 
HETATM 4170 O  O   . HOH   P 7 .   ? 21.76800  -4.75200  16.56900  1.000 5.18682  ? 573 HOH   A O   1 
HETATM 4171 O  O   . HOH   P 7 .   ? 9.80400   -23.50500 18.59200  1.000 20.99682 ? 574 HOH   A O   1 
HETATM 4172 O  O   . HOH   P 7 .   ? 30.68400  -7.08900  -7.81400  1.000 33.89682 ? 575 HOH   A O   1 
HETATM 4173 O  O   . HOH   P 7 .   ? 20.83500  -0.07900  21.49800  1.000 7.59682  ? 576 HOH   A O   1 
HETATM 4174 O  O   . HOH   P 7 .   ? 5.57100   -24.32700 -11.03600 1.000 23.70682 ? 577 HOH   A O   1 
HETATM 4175 O  O   . HOH   P 7 .   ? 4.02300   -34.92900 0.84000   1.000 22.98682 ? 578 HOH   A O   1 
HETATM 4176 O  O   . HOH   P 7 .   ? 19.18600  10.36600  -3.01300  1.000 20.87682 ? 579 HOH   A O   1 
HETATM 4177 O  O   . HOH   P 7 .   ? 18.05100  -18.52000 -6.87100  1.000 26.74682 ? 580 HOH   A O   1 
HETATM 4178 O  O   . HOH   P 7 .   ? 8.91300   1.96600   18.31000  1.000 14.11682 ? 581 HOH   A O   1 
HETATM 4179 O  O   . HOH   P 7 .   ? 22.85900  -8.95500  4.14400   1.000 5.95682  ? 582 HOH   A O   1 
HETATM 4180 O  O   . HOH   P 7 .   ? 19.22900  -28.67900 2.22800   1.000 24.77682 ? 583 HOH   A O   1 
HETATM 4181 O  O   . HOH   P 7 .   ? 26.67900  -10.70200 -1.62100  1.000 10.09682 ? 584 HOH   A O   1 
HETATM 4182 O  O   . HOH   P 7 .   ? 25.69700  -22.33700 -0.84600  1.000 22.82682 ? 585 HOH   A O   1 
HETATM 4183 O  O   . HOH   P 7 .   ? 14.88300  -15.35100 18.22000  1.000 9.48682  ? 586 HOH   A O   1 
HETATM 4184 O  O   . HOH   P 7 .   ? 7.58200   -5.29700  18.98600  1.000 6.75682  ? 587 HOH   A O   1 
HETATM 4185 O  O   . HOH   P 7 .   ? 1.87500   -20.60500 -7.20600  1.000 14.64682 ? 588 HOH   A O   1 
HETATM 4186 O  O   . HOH   P 7 .   ? 20.41500  3.90500   21.10000  1.000 22.98682 ? 589 HOH   A O   1 
HETATM 4187 O  O   . HOH   P 7 .   ? -0.34600  -28.35500 3.41500   1.000 22.95682 ? 590 HOH   A O   1 
HETATM 4188 O  O   . HOH   P 7 .   ? 8.11300   9.45400   3.96700   1.000 21.85682 ? 591 HOH   A O   1 
HETATM 4189 O  O   . HOH   P 7 .   ? 17.77600  -8.24100  -5.60900  1.000 12.26682 ? 592 HOH   A O   1 
HETATM 4190 O  O   . HOH   P 7 .   ? 26.28600  4.40100   3.00200   1.000 11.72682 ? 593 HOH   A O   1 
HETATM 4191 O  O   . HOH   P 7 .   ? 21.01800  -31.31800 10.26300  1.000 20.42682 ? 594 HOH   A O   1 
HETATM 4192 O  O   . HOH   P 7 .   ? 25.77600  -6.25100  25.08300  1.000 15.26682 ? 595 HOH   A O   1 
HETATM 4193 O  O   . HOH   P 7 .   ? 6.45000   -21.32200 13.06000  1.000 20.34682 ? 596 HOH   A O   1 
HETATM 4194 O  O   . HOH   P 7 .   ? 4.26400   -8.61800  -6.01700  1.000 10.94682 ? 597 HOH   A O   1 
HETATM 4195 O  O   . HOH   P 7 .   ? 4.92500   -19.25300 18.77100  1.000 27.99682 ? 598 HOH   A O   1 
HETATM 4196 O  O   . HOH   P 7 .   ? 19.61600  -27.08100 21.01700  1.000 16.67682 ? 599 HOH   A O   1 
HETATM 4197 O  O   . HOH   P 7 .   ? 16.48700  -33.76600 4.03700   1.000 20.47682 ? 600 HOH   A O   1 
HETATM 4198 O  O   . HOH   P 7 .   ? 32.20700  -1.05300  10.78100  1.000 20.06682 ? 601 HOH   A O   1 
HETATM 4199 O  O   . HOH   P 7 .   ? 6.66400   5.44500   3.85500   1.000 22.30682 ? 602 HOH   A O   1 
HETATM 4200 O  O   . HOH   P 7 .   ? 9.72900   -1.27800  24.22300  1.000 7.87682  ? 603 HOH   A O   1 
HETATM 4201 O  O   . HOH   P 7 .   ? 20.08300  -12.71200 -8.26000  1.000 25.65682 ? 604 HOH   A O   1 
HETATM 4202 O  O   . HOH   P 7 .   ? -3.26900  -21.79000 -11.55100 1.000 30.68682 ? 605 HOH   A O   1 
HETATM 4203 O  O   . HOH   P 7 .   ? 32.420    -9.774    6.558     1.000 26.10682 ? 606 HOH   A O   1 
HETATM 4204 O  O   . HOH   P 7 .   ? 8.96900   0.71500   22.09200  1.000 8.86682  ? 607 HOH   A O   1 
HETATM 4205 O  O   . HOH   P 7 .   ? 19.37500  -36.52200 10.51900  1.000 28.31682 ? 608 HOH   A O   1 
HETATM 4206 O  O   . HOH   P 7 .   ? 6.71600   -13.89400 -4.28600  1.000 9.93682  ? 609 HOH   A O   1 
HETATM 4207 O  O   . HOH   P 7 .   ? 11.18200  -32.40600 13.93800  1.000 23.15682 ? 610 HOH   A O   1 
HETATM 4208 O  O   . HOH   P 7 .   ? 24.24500  -24.68500 3.20300   1.000 15.13682 ? 611 HOH   A O   1 
HETATM 4209 O  O   . HOH   P 7 .   ? 10.32400  -24.83700 -8.03400  1.000 22.80682 ? 612 HOH   A O   1 
HETATM 4210 O  O   . HOH   P 7 .   ? -3.64500  -6.68500  3.16700   1.000 29.02682 ? 613 HOH   A O   1 
HETATM 4211 O  O   . HOH   P 7 .   ? 9.25400   5.97400   -4.29900  1.000 18.11682 ? 614 HOH   A O   1 
HETATM 4212 O  O   . HOH   P 7 .   ? 22.46300  -27.53700 -2.81200  1.000 32.61682 ? 615 HOH   A O   1 
HETATM 4213 O  O   . HOH   P 7 .   ? -0.71100  -17.28000 -7.81200  1.000 15.76682 ? 616 HOH   A O   1 
HETATM 4214 O  O   . HOH   P 7 .   ? 31.91500  -17.20600 7.45300   1.000 26.52682 ? 617 HOH   A O   1 
HETATM 4215 O  O   . HOH   P 7 .   ? 23.63600  5.68100   3.77500   1.000 10.72682 ? 618 HOH   A O   1 
HETATM 4216 O  O   . HOH   P 7 .   ? 4.91800   -4.79200  19.06700  1.000 5.92682  ? 619 HOH   A O   1 
HETATM 4217 O  O   . HOH   P 7 .   ? 29.36200  2.68800   2.31500   1.000 23.51682 ? 620 HOH   A O   1 
HETATM 4218 O  O   . HOH   P 7 .   ? 17.66900  -15.58900 -5.61200  1.000 11.20682 ? 621 HOH   A O   1 
HETATM 4219 O  O   . HOH   P 7 .   ? 1.00500   -21.21600 -10.43000 1.000 27.85682 ? 622 HOH   A O   1 
HETATM 4220 O  O   . HOH   P 7 .   ? -3.09600  -3.78200  11.36200  1.000 30.16682 ? 623 HOH   A O   1 
HETATM 4221 O  O   . HOH   P 7 .   ? 13.58600  -11.11600 -8.45700  1.000 23.42682 ? 624 HOH   A O   1 
HETATM 4222 O  O   . HOH   P 7 .   ? 10.54900  -3.79600  22.91200  1.000 10.00682 ? 625 HOH   A O   1 
HETATM 4223 O  O   . HOH   P 7 .   ? 4.58900   -3.87200  -13.96400 1.000 24.18682 ? 626 HOH   A O   1 
HETATM 4224 O  O   . HOH   P 7 .   ? 8.20700   -23.33000 -10.71700 1.000 25.25682 ? 627 HOH   A O   1 
HETATM 4225 O  O   . HOH   P 7 .   ? 30.52800  -11.82500 -6.73000  1.000 28.22682 ? 628 HOH   A O   1 
HETATM 4226 O  O   . HOH   P 7 .   ? 12.63900  9.67600   7.93800   1.000 19.55682 ? 629 HOH   A O   1 
HETATM 4227 O  O   . HOH   P 7 .   ? 21.83500  0.92000   -6.20700  1.000 28.61682 ? 630 HOH   A O   1 
HETATM 4228 O  O   . HOH   P 7 .   ? 3.76400   -14.34600 -14.43300 1.000 30.93682 ? 631 HOH   A O   1 
HETATM 4229 O  O   . HOH   P 7 .   ? 15.83300  -22.00300 -12.27500 1.000 30.88682 ? 632 HOH   A O   1 
HETATM 4230 O  O   . HOH   P 7 .   ? 15.52200  -5.02800  -8.15100  1.000 12.47682 ? 633 HOH   A O   1 
HETATM 4231 O  O   . HOH   P 7 .   ? 5.49500   -0.28900  16.32000  1.000 18.55682 ? 634 HOH   A O   1 
HETATM 4232 O  O   . HOH   P 7 .   ? 28.77100  -26.96500 16.12000  1.000 38.64682 ? 635 HOH   A O   1 
HETATM 4233 O  O   . HOH   P 7 .   ? 30.00500  -17.03700 13.44300  1.000 25.40682 ? 636 HOH   A O   1 
HETATM 4234 O  O   . HOH   P 7 .   ? 1.45700   -28.02700 9.27100   1.000 33.18682 ? 637 HOH   A O   1 
HETATM 4235 O  O   . HOH   P 7 .   ? 9.91100   -33.92600 7.15700   1.000 20.59682 ? 638 HOH   A O   1 
HETATM 4236 O  O   . HOH   P 7 .   ? -8.96700  -16.82100 -11.12900 1.000 32.96682 ? 639 HOH   A O   1 
HETATM 4237 O  O   . HOH   P 7 .   ? 12.95600  -26.03500 -7.86700  1.000 13.75682 ? 640 HOH   A O   1 
HETATM 4238 O  O   . HOH   P 7 .   ? 1.20500   -12.51800 -12.62300 1.000 32.03682 ? 641 HOH   A O   1 
HETATM 4239 O  O   . HOH   P 7 .   ? -5.96400  -1.68800  -4.36300  1.000 32.04682 ? 642 HOH   A O   1 
HETATM 4240 O  O   . HOH   P 7 .   ? 8.06300   -0.84600  17.71100  1.000 15.18682 ? 643 HOH   A O   1 
HETATM 4241 O  O   . HOH   P 7 .   ? -7.26000  2.64700   1.51900   1.000 28.61682 ? 644 HOH   A O   1 
HETATM 4242 O  O   . HOH   P 7 .   ? 12.61000  -19.25000 12.85500  1.000 11.63682 ? 645 HOH   A O   1 
HETATM 4243 O  O   . HOH   P 7 .   ? 30.84600  0.85300   10.07000  1.000 13.44682 ? 646 HOH   A O   1 
HETATM 4244 O  O   . HOH   P 7 .   ? 18.97500  -3.69100  17.68800  1.000 6.23682  ? 647 HOH   A O   1 
HETATM 4245 O  O   . HOH   P 7 .   ? 18.00300  -30.04700 15.46300  1.000 19.96682 ? 648 HOH   A O   1 
HETATM 4246 O  O   . HOH   P 7 .   ? 21.642    -31.194   -4.764    1.000 16.10682 ? 649 HOH   A O   1 
HETATM 4247 O  O   . HOH   P 7 .   ? 10.53400  1.99700   25.95000  1.000 12.56682 ? 650 HOH   A O   1 
HETATM 4248 O  O   . HOH   P 7 .   ? -5.75700  -21.01200 -7.29400  1.000 26.85682 ? 651 HOH   A O   1 
HETATM 4249 O  O   . HOH   P 7 .   ? 15.30300  10.13900  7.13100   1.000 16.88682 ? 652 HOH   A O   1 
HETATM 4250 O  O   . HOH   P 7 .   ? 26.83600  -8.13400  23.06500  1.000 15.62682 ? 653 HOH   A O   1 
HETATM 4251 O  O   . HOH   P 7 .   ? 35.23600  -8.35200  7.65200   1.000 19.76682 ? 654 HOH   A O   1 
HETATM 4252 O  O   . HOH   P 7 .   ? -0.17200  -5.17200  0.42300   1.000 16.74682 ? 655 HOH   A O   1 
HETATM 4253 O  O   . HOH   P 7 .   ? 26.01300  -20.47300 -2.07000  1.000 23.74682 ? 656 HOH   A O   1 
HETATM 4254 O  O   . HOH   P 7 .   ? -3.91100  -0.66900  9.83100   1.000 28.75682 ? 657 HOH   A O   1 
HETATM 4255 O  O   . HOH   P 7 .   ? 6.72200   8.02600   -2.12800  1.000 25.49682 ? 658 HOH   A O   1 
HETATM 4256 O  O   . HOH   P 7 .   ? -0.15100  0.89400   -9.31100  1.000 29.15682 ? 659 HOH   A O   1 
HETATM 4257 O  O   . HOH   P 7 .   ? -6.35700  -1.61500  0.32300   1.000 29.56682 ? 660 HOH   A O   1 
HETATM 4258 O  O   . HOH   P 7 .   ? 12.34100  -19.45400 21.42900  1.000 15.11682 ? 661 HOH   A O   1 
HETATM 4259 O  O   . HOH   P 7 .   ? -1.39900  -13.22700 10.53100  1.000 23.87682 ? 662 HOH   A O   1 
HETATM 4260 O  O   . HOH   P 7 .   ? -10.47800 -24.57600 1.10800   1.000 35.61682 ? 663 HOH   A O   1 
HETATM 4261 O  O   . HOH   P 7 .   ? 2.81800   6.71600   12.41600  1.000 15.46682 ? 664 HOH   A O   1 
HETATM 4262 O  O   . HOH   P 7 .   ? 9.71300   -29.13100 12.77400  1.000 18.62682 ? 665 HOH   A O   1 
HETATM 4263 O  O   . HOH   P 7 .   ? 5.15300   0.72900   -10.42800 1.000 26.96682 ? 666 HOH   A O   1 
HETATM 4264 O  O   . HOH   P 7 .   ? -5.35000  -23.36900 5.22500   1.000 32.44682 ? 667 HOH   A O   1 
HETATM 4265 O  O   . HOH   P 7 .   ? 16.31100  -23.27200 16.85300  1.000 13.22682 ? 668 HOH   A O   1 
HETATM 4266 O  O   . HOH   P 7 .   ? -4.832    -11.616   -4.841    1.000 28.60682 ? 669 HOH   A O   1 
HETATM 4267 O  O   . HOH   P 7 .   ? 14.78200  9.72800   1.87500   1.000 15.50682 ? 670 HOH   A O   1 
HETATM 4268 O  O   . HOH   P 7 .   ? 6.17200   6.94100   6.15300   1.000 17.39682 ? 671 HOH   A O   1 
HETATM 4269 O  O   . HOH   P 7 .   ? -2.64900  -27.12200 -0.21700  1.000 28.44682 ? 672 HOH   A O   1 
HETATM 4270 O  O   . HOH   P 7 .   ? 8.09800   -27.62900 12.75700  1.000 19.88682 ? 673 HOH   A O   1 
HETATM 4271 O  O   . HOH   P 7 .   ? 8.33600   -32.32800 -5.53600  1.000 24.50682 ? 674 HOH   A O   1 
HETATM 4272 O  O   . HOH   P 7 .   ? 18.26400  -21.75200 -6.53700  1.000 30.55682 ? 675 HOH   A O   1 
HETATM 4273 O  O   . HOH   P 7 .   ? 26.61200  5.62000   12.73300  1.000 14.50682 ? 676 HOH   A O   1 
HETATM 4274 O  O   . HOH   P 7 .   ? 19.53200  9.53700   9.71700   1.000 24.02682 ? 677 HOH   A O   1 
HETATM 4275 O  O   . HOH   P 7 .   ? -5.28200  -18.36700 5.58700   1.000 18.85682 ? 678 HOH   A O   1 
HETATM 4276 O  O   . HOH   P 7 .   ? 8.396     8.692     18.740    1.000 23.52682 ? 679 HOH   A O   1 
HETATM 4277 O  O   . HOH   P 7 .   ? 31.84500  -8.41300  3.52500   1.000 18.37682 ? 680 HOH   A O   1 
HETATM 4278 O  O   . HOH   P 7 .   ? 30.34400  5.72400   8.14200   1.000 30.03682 ? 681 HOH   A O   1 
HETATM 4279 O  O   . HOH   P 7 .   ? 2.54600   5.48500   9.80600   1.000 29.34682 ? 682 HOH   A O   1 
HETATM 4280 O  O   . HOH   P 7 .   ? 13.06000  -11.19000 -14.72200 1.000 35.39682 ? 683 HOH   A O   1 
HETATM 4281 O  O   . HOH   P 7 .   ? 6.28800   -15.47400 17.38500  1.000 18.47682 ? 684 HOH   A O   1 
HETATM 4282 O  O   . HOH   P 7 .   ? 4.33700   10.63700  9.79300   1.000 32.27682 ? 685 HOH   A O   1 
HETATM 4283 O  O   . HOH   P 7 .   ? 16.44100  9.66300   10.49900  1.000 16.14682 ? 686 HOH   A O   1 
HETATM 4284 O  O   . HOH   P 7 .   ? 26.54500  -25.29100 10.47300  1.000 15.58682 ? 687 HOH   A O   1 
HETATM 4285 O  O   . HOH   P 7 .   ? -3.46900  4.14100   2.20600   1.000 27.04682 ? 688 HOH   A O   1 
HETATM 4286 O  O   . HOH   P 7 .   ? 23.04600  -32.40200 8.93100   1.000 30.59682 ? 689 HOH   A O   1 
HETATM 4287 O  O   . HOH   P 7 .   ? 25.76700  -27.44500 12.69900  1.000 15.50682 ? 690 HOH   A O   1 
HETATM 4288 O  O   . HOH   P 7 .   ? 14.48200  -14.64800 20.97100  1.000 17.46682 ? 691 HOH   A O   1 
HETATM 4289 O  O   . HOH   P 7 .   ? 19.16100  -31.15300 13.03900  1.000 15.99682 ? 692 HOH   A O   1 
HETATM 4290 O  O   . HOH   P 7 .   ? 25.48700  -16.83500 -5.75100  1.000 12.31682 ? 693 HOH   A O   1 
HETATM 4291 O  O   . HOH   P 7 .   ? -0.63200  -33.06500 -8.03200  1.000 37.82682 ? 694 HOH   A O   1 
HETATM 4292 O  O   . HOH   P 7 .   ? 6.27400   -15.57800 -12.82900 1.000 23.19682 ? 695 HOH   A O   1 
HETATM 4293 O  O   . HOH   P 7 .   ? -4.39100  -25.86800 1.07000   1.000 36.18682 ? 696 HOH   A O   1 
HETATM 4294 O  O   . HOH   P 7 .   ? -2.43000  -26.12500 6.14600   1.000 21.45682 ? 697 HOH   A O   1 
HETATM 4295 O  O   . HOH   P 7 .   ? 3.98900   4.18900   14.13300  1.000 9.19682  ? 698 HOH   A O   1 
HETATM 4296 O  O   . HOH   P 7 .   ? 15.18700  -10.67800 -13.46500 1.000 33.69682 ? 699 HOH   A O   1 
HETATM 4297 O  O   . HOH   P 7 .   ? 20.02300  -20.16300 -4.82500  1.000 16.33682 ? 700 HOH   A O   1 
HETATM 4298 O  O   . HOH   P 7 .   ? 29.24700  -26.19900 11.07800  1.000 30.60682 ? 701 HOH   A O   1 
HETATM 4299 O  O   . HOH   P 7 .   ? 31.07900  2.13100   -0.03500  1.000 20.83682 ? 702 HOH   A O   1 
HETATM 4300 O  O   . HOH   P 7 .   ? 2.37700   -32.76200 -2.37700  1.000 20.70682 ? 703 HOH   A O   1 
HETATM 4301 O  O   . HOH   P 7 .   ? 17.31800  10.46000  -1.49300  1.000 33.98682 ? 704 HOH   A O   1 
HETATM 4302 O  O   . HOH   P 7 .   ? 23.20700  1.61200   21.23200  1.000 11.50682 ? 705 HOH   A O   1 
HETATM 4303 O  O   . HOH   P 7 .   ? 28.80000  -21.68700 19.50800  1.000 32.30682 ? 706 HOH   A O   1 
HETATM 4304 O  O   . HOH   P 7 .   ? 30.12400  -13.49400 15.49400  1.000 12.71682 ? 707 HOH   A O   1 
HETATM 4305 O  O   . HOH   P 7 .   ? 30.79400  -0.52700  -4.57500  1.000 21.48682 ? 708 HOH   A O   1 
HETATM 4306 O  O   . HOH   P 7 .   ? 35.23400  -5.95800  13.01500  1.000 16.16682 ? 709 HOH   A O   1 
HETATM 4307 O  O   . HOH   P 7 .   ? 17.95500  8.71400   2.33500   1.000 18.91682 ? 710 HOH   A O   1 
HETATM 4308 O  O   . HOH   P 7 .   ? 31.56500  0.02300   1.80900   1.000 25.28682 ? 711 HOH   A O   1 
HETATM 4309 O  O   . HOH   P 7 .   ? 26.892    13.509    9.782     1.000 20.74682 ? 712 HOH   A O   1 
HETATM 4310 O  O   . HOH   P 7 .   ? 10.135    -34.664   -2.882    1.000 20.12682 ? 713 HOH   A O   1 
HETATM 4311 O  O   . HOH   P 7 .   ? 19.62800  -17.63000 -4.97300  1.000 20.18682 ? 714 HOH   A O   1 
HETATM 4312 O  O   . HOH   P 7 .   ? -7.95000  0.06300   6.29400   1.000 27.11682 ? 715 HOH   A O   1 
HETATM 4313 O  O   . HOH   P 7 .   ? 2.64800   -31.12400 7.62100   1.000 24.11682 ? 716 HOH   A O   1 
HETATM 4314 O  O   . HOH   P 7 .   ? -0.12500  -8.86700  -1.98100  1.000 10.66682 ? 717 HOH   A O   1 
HETATM 4315 O  O   . HOH   P 7 .   ? 15.92400  -29.18100 15.59100  1.000 21.42682 ? 718 HOH   A O   1 
HETATM 4316 O  O   . HOH   P 7 .   ? 0.51900   -1.16300  15.79300  1.000 24.52682 ? 719 HOH   A O   1 
HETATM 4317 O  O   . HOH   P 7 .   ? -4.55600  -9.56800  -7.38800  1.000 30.23682 ? 720 HOH   A O   1 
HETATM 4318 O  O   . HOH   P 7 .   ? 22.62500  -28.00200 0.22000   1.000 32.46682 ? 721 HOH   A O   1 
HETATM 4319 O  O   . HOH   P 7 .   ? 0.37600   -10.84700 13.47300  1.000 16.20682 ? 722 HOH   A O   1 
HETATM 4320 O  O   . HOH   P 7 .   ? -5.01100  -3.43000  -1.53300  1.000 28.83682 ? 723 HOH   A O   1 
HETATM 4321 O  O   . HOH   P 7 .   ? -2.27700  -27.66600 -2.55000  1.000 26.09682 ? 724 HOH   A O   1 
HETATM 4322 O  O   . HOH   P 7 .   ? 27.79100  -24.91300 17.77900  1.000 27.76682 ? 725 HOH   A O   1 
HETATM 4323 O  O   . HOH   P 7 .   ? 3.61600   6.07700   7.32500   1.000 27.47682 ? 726 HOH   A O   1 
HETATM 4324 O  O   . HOH   P 7 .   ? 34.447    -6.123    3.835     1.000 23.79682 ? 727 HOH   A O   1 
HETATM 4325 O  O   . HOH   P 7 .   ? 17.15000  -2.62300  -8.38500  1.000 31.92682 ? 728 HOH   A O   1 
HETATM 4326 O  O   . HOH   P 7 .   ? 7.59900   -32.88500 5.19200   1.000 28.74682 ? 729 HOH   A O   1 
HETATM 4327 O  O   . HOH   P 7 .   ? 31.781    -16.459   0.999     1.000 30.20682 ? 730 HOH   A O   1 
HETATM 4328 O  O   . HOH   P 7 .   ? 4.77100   -18.02600 -12.91800 1.000 16.82682 ? 731 HOH   A O   1 
HETATM 4329 O  O   . HOH   P 7 .   ? 3.43800   3.25600   -6.86000  1.000 19.45682 ? 732 HOH   A O   1 
HETATM 4330 O  O   . HOH   P 7 .   ? 4.81200   -21.22100 17.55900  1.000 29.00682 ? 733 HOH   A O   1 
HETATM 4331 O  O   . HOH   P 7 .   ? -2.53700  -24.17300 8.38000   1.000 32.04682 ? 734 HOH   A O   1 
HETATM 4332 O  O   . HOH   P 7 .   ? 20.90800  2.42700   -4.35400  1.000 21.48682 ? 735 HOH   A O   1 
HETATM 4333 O  O   . HOH   P 7 .   ? 27.96300  3.23700   12.98700  1.000 12.12682 ? 736 HOH   A O   1 
HETATM 4334 O  O   . HOH   P 7 .   ? 12.80300  -34.13500 7.21600   1.000 24.67682 ? 737 HOH   A O   1 
HETATM 4335 O  O   . HOH   P 7 .   ? 31.664    -16.503   -1.572    1.000 34.95682 ? 738 HOH   A O   1 
HETATM 4336 O  O   . HOH   P 7 .   ? 7.06100   -26.14000 16.12100  1.000 38.78682 ? 739 HOH   A O   1 
HETATM 4337 O  O   . HOH   P 7 .   ? 25.56200  7.13000   14.92200  1.000 24.68682 ? 740 HOH   A O   1 
HETATM 4338 O  O   . HOH   P 7 .   ? -0.76000  -6.99300  15.26100  1.000 31.77682 ? 741 HOH   A O   1 
HETATM 4339 O  O   . HOH   P 7 .   ? -6.39900  -2.79500  2.99300   1.000 20.97682 ? 742 HOH   A O   1 
HETATM 4340 O  O   . HOH   P 7 .   ? 1.53300   1.57600   12.16500  1.000 34.63682 ? 743 HOH   A O   1 
HETATM 4341 O  O   . HOH   P 7 .   ? 18.74900  10.07200  6.42500   1.000 20.46682 ? 744 HOH   A O   1 
HETATM 4342 O  O   . HOH   P 7 .   ? 31.54800  4.20300   6.43000   1.000 22.30682 ? 745 HOH   A O   1 
HETATM 4343 O  O   . HOH   P 7 .   ? 19.81000  -34.05400 11.25300  1.000 22.29682 ? 746 HOH   A O   1 
HETATM 4344 O  O   . HOH   P 7 .   ? 27.897    4.798     -4.705    1.000 15.20682 ? 747 HOH   A O   1 
HETATM 4345 O  O   . HOH   P 7 .   ? -9.566    1.918     3.782     1.000 32.18682 ? 748 HOH   A O   1 
HETATM 4346 O  O   . HOH   P 7 .   ? 5.790     9.741     19.953    1.000 16.64682 ? 749 HOH   A O   1 
HETATM 4347 O  O   . HOH   P 7 .   ? 18.97400  8.97000   16.58700  1.000 30.95682 ? 750 HOH   A O   1 
HETATM 4348 O  O   . HOH   P 7 .   ? 28.25800  -19.53000 19.89600  1.000 29.39682 ? 751 HOH   A O   1 
HETATM 4349 O  O   . HOH   P 7 .   ? 20.59400  -27.22100 26.05000  1.000 15.67682 ? 752 HOH   A O   1 
HETATM 4350 O  O   . HOH   P 7 .   ? 6.20000   -20.22300 -13.42100 1.000 25.23682 ? 753 HOH   A O   1 
HETATM 4351 O  O   . HOH   P 7 .   ? 26.79200  -3.31500  -5.24000  1.000 27.78682 ? 754 HOH   A O   1 
HETATM 4352 O  O   . HOH   P 7 .   ? 24.20400  -3.06500  -6.17800  1.000 21.79682 ? 755 HOH   A O   1 
HETATM 4353 O  O   . HOH   P 7 .   ? 32.09600  1.98200   7.78900   1.000 23.36682 ? 756 HOH   A O   1 
HETATM 4354 O  O   . HOH   P 7 .   ? 10.14100  -5.93900  -13.78200 1.000 32.04682 ? 757 HOH   A O   1 
HETATM 4355 O  O   . HOH   P 7 .   ? 19.172    -31.254   -6.470    1.000 19.84682 ? 758 HOH   A O   1 
HETATM 4356 O  O   . HOH   P 7 .   ? 0.086     7.307     4.475     1.000 32.22682 ? 759 HOH   A O   1 
HETATM 4357 O  O   . HOH   P 7 .   ? 7.03800   5.45300   -6.07400  1.000 23.62682 ? 760 HOH   A O   1 
HETATM 4358 O  O   . HOH   P 7 .   ? 22.41500  -21.58500 -5.55500  1.000 30.80682 ? 761 HOH   A O   1 
HETATM 4359 O  O   . HOH   P 7 .   ? -8.068    -10.834   2.030     1.000 28.17682 ? 762 HOH   A O   1 
HETATM 4360 O  O   . HOH   P 7 .   ? 0.057     -17.216   -14.508   1.000 23.29682 ? 763 HOH   A O   1 
HETATM 4361 O  O   . HOH   P 7 .   ? 18.75500  -34.88500 13.84700  1.000 31.02682 ? 764 HOH   A O   1 
HETATM 4362 O  O   . HOH   P 7 .   ? 4.19400   -2.36900  17.89900  1.000 18.33682 ? 765 HOH   A O   1 
HETATM 4363 O  O   . HOH   P 7 .   ? 6.13800   -22.76700 15.21700  1.000 29.57682 ? 766 HOH   A O   1 
HETATM 4364 O  O   . HOH   P 7 .   ? 20.311    -29.038   -7.892    1.000 24.39682 ? 767 HOH   A O   1 
HETATM 4365 O  O   . HOH   P 7 .   ? 1.02100   1.11100   -7.21200  1.000 21.63682 ? 768 HOH   A O   1 
HETATM 4366 O  O   . HOH   P 7 .   ? 30.91200  -21.78800 13.60700  1.000 30.61682 ? 769 HOH   A O   1 
HETATM 4367 O  O   . HOH   P 7 .   ? 25.98300  5.64700   17.25000  1.000 28.10682 ? 770 HOH   A O   1 
HETATM 4368 O  O   . HOH   P 7 .   ? 7.13200   -23.82300 17.07500  1.000 30.39682 ? 771 HOH   A O   1 
HETATM 4369 O  O   . HOH   P 7 .   ? 10.88500  -17.20800 -14.40000 1.000 34.59682 ? 772 HOH   A O   1 
HETATM 4370 O  O   . HOH   P 7 .   ? 14.30000  11.53700  3.82700   1.000 25.35682 ? 773 HOH   A O   1 
HETATM 4371 O  O   . HOH   P 7 .   ? -6.14700  0.79500   9.91100   1.000 31.08682 ? 774 HOH   A O   1 
HETATM 4372 O  O   . HOH   P 7 .   ? 21.46600  -32.57600 13.46400  1.000 31.67682 ? 775 HOH   A O   1 
HETATM 4373 O  O   . HOH   P 7 .   ? 2.279     -16.503   -14.626   1.000 30.99682 ? 776 HOH   A O   1 
HETATM 4374 O  O   . HOH   P 7 .   ? 13.60200  9.19700   -2.71200  1.000 10.23682 ? 777 HOH   A O   1 
HETATM 4375 O  O   . HOH   P 7 .   ? 19.66400  1.93300   -6.54700  1.000 30.51682 ? 778 HOH   A O   1 
HETATM 4376 O  O   . HOH   P 7 .   ? 14.783    -14.402   -15.833   1.000 33.69682 ? 779 HOH   A O   1 
HETATM 4377 O  O   . HOH   P 7 .   ? 22.05000  -1.99400  -7.40700  1.000 33.13682 ? 780 HOH   A O   1 
HETATM 4378 O  O   . HOH   P 7 .   ? -0.01400  -29.96500 -5.69600  1.000 34.49682 ? 781 HOH   A O   1 
HETATM 4379 O  O   . HOH   P 7 .   ? 25.71500  -27.17100 8.49000   1.000 23.78682 ? 782 HOH   A O   1 
HETATM 4380 O  O   . HOH   P 7 .   ? 15.09800  -7.05800  26.87600  1.000 14.88682 ? 783 HOH   A O   1 
HETATM 4381 O  O   . HOH   P 7 .   ? 32.162    -1.240    17.243    1.000 27.86682 ? 784 HOH   A O   1 
HETATM 4382 O  O   . HOH   P 7 .   ? 7.80700   -1.41900  20.47500  1.000 9.80682  ? 785 HOH   A O   1 
HETATM 4383 O  O   . HOH   P 7 .   ? 2.96200   3.40900   16.55500  1.000 17.80682 ? 786 HOH   A O   1 
HETATM 4384 O  O   . HOH   P 7 .   ? 27.77400  -16.11700 -6.83200  1.000 33.37682 ? 787 HOH   A O   1 
HETATM 4385 O  O   . HOH   P 7 .   ? 11.27100  -9.88700  -15.80700 1.000 25.12682 ? 788 HOH   A O   1 
HETATM 4386 O  O   . HOH   P 7 .   ? 20.33500  6.38600   23.06400  1.000 26.33682 ? 789 HOH   A O   1 
HETATM 4387 O  O   . HOH   P 7 .   ? 6.84800   -36.04000 1.39700   1.000 26.37682 ? 790 HOH   A O   1 
HETATM 4388 O  O   . HOH   P 7 .   ? 22.75700  4.17800   21.08800  1.000 25.93682 ? 791 HOH   A O   1 
HETATM 4389 O  O   . HOH   P 7 .   ? 0.28800   -15.94600 13.52800  1.000 35.85682 ? 792 HOH   A O   1 
HETATM 4390 O  O   . HOH   P 7 .   ? 24.598    -27.201   4.035     1.000 18.71682 ? 793 HOH   A O   1 
HETATM 4391 O  O   . HOH   P 7 .   ? 30.68700  5.33700   10.53500  1.000 31.21682 ? 794 HOH   A O   1 
HETATM 4392 O  O   . HOH   P 7 .   ? 0.21100   -8.15900  -14.09800 1.000 32.38682 ? 795 HOH   A O   1 
HETATM 4393 O  O   . HOH   P 7 .   ? 5.799     -11.868   -18.837   1.000 26.95682 ? 796 HOH   A O   1 
HETATM 4394 O  O   . HOH   P 7 .   ? 35.78900  -3.00500  13.31600  1.000 27.91682 ? 797 HOH   A O   1 
HETATM 4395 O  O   . HOH   P 7 .   ? 12.01900  12.44500  7.04500   1.000 27.97682 ? 798 HOH   A O   1 
HETATM 4396 O  O   . HOH   P 7 .   ? 14.60600  11.07400  -4.62100  1.000 21.87682 ? 799 HOH   A O   1 
HETATM 4397 O  O   . HOH   P 7 .   ? 31.92900  -0.27900  -2.07100  1.000 22.22682 ? 800 HOH   A O   1 
HETATM 4398 O  O   . HOH   P 7 .   ? 30.49400  2.92000   11.63100  1.000 20.62682 ? 801 HOH   A O   1 
HETATM 4399 O  O   . HOH   P 7 .   ? 7.74400   -15.08800 -15.44500 1.000 32.73682 ? 802 HOH   A O   1 
HETATM 4400 O  O   . HOH   P 7 .   ? 8.26200   -3.85800  21.45100  1.000 9.90682  ? 803 HOH   A O   1 
HETATM 4401 O  O   . HOH   P 7 .   ? 0.078     -1.750    -17.928   1.000 33.79682 ? 804 HOH   A O   1 
HETATM 4402 O  O   . HOH   P 7 .   ? 17.51800  12.28300  8.78000   1.000 34.61682 ? 805 HOH   A O   1 
HETATM 4403 O  O   . HOH   P 7 .   ? 15.19700  10.59100  -0.50800  1.000 21.64682 ? 806 HOH   A O   1 
HETATM 4404 O  O   . HOH   P 7 .   ? 13.49200  10.72300  10.85900  1.000 32.61682 ? 807 HOH   A O   1 
HETATM 4405 O  O   . HOH   P 7 .   ? 20.01100  -6.53300  -6.91700  1.000 25.82682 ? 808 HOH   A O   1 
HETATM 4406 O  O   . HOH   P 7 .   ? -1.36300  -9.27200  16.48700  1.000 27.03682 ? 809 HOH   A O   1 
HETATM 4407 O  O   . HOH   P 7 .   ? 0.82900   6.96900   14.82600  1.000 35.26682 ? 810 HOH   A O   1 
HETATM 4408 O  O   . HOH   P 7 .   ? 14.00000  -16.22700 23.09900  1.000 33.06682 ? 811 HOH   A O   1 
HETATM 4409 O  O   . HOH   P 7 .   ? 25.37700  -29.89500 15.65200  1.000 24.60682 ? 812 HOH   A O   1 
HETATM 4410 O  O   . HOH   P 7 .   ? 20.12200  -38.82300 11.22100  1.000 35.67682 ? 813 HOH   A O   1 
HETATM 4411 O  O   . HOH   P 7 .   ? -8.528    -18.412   4.913     1.000 32.41682 ? 814 HOH   A O   1 
HETATM 4412 O  O   . HOH   P 7 .   ? -5.06400  -26.02800 5.60300   1.000 42.53682 ? 815 HOH   A O   1 
HETATM 4413 O  O   . HOH   P 7 .   ? 30.90300  -21.00300 19.24600  1.000 40.74682 ? 816 HOH   A O   1 
HETATM 4414 O  O   . HOH   P 7 .   ? 13.79400  10.47100  -7.00800  1.000 31.32682 ? 817 HOH   A O   1 
HETATM 4415 O  O   . HOH   P 7 .   ? 19.32100  -3.61700  -7.20900  1.000 31.21682 ? 818 HOH   A O   1 
HETATM 4416 O  O   . HOH   P 7 .   ? 32.24700  2.17100   13.98300  1.000 28.40682 ? 819 HOH   A O   1 
HETATM 4417 O  O   . HOH   P 7 .   ? 13.85400  14.19100  5.63700   1.000 42.36682 ? 820 HOH   A O   1 
HETATM 4418 O  O   . HOH   Q 7 .   ? -4.86200  -26.18800 45.39900  1.000 25.70682 ? 501 HOH   B O   1 
HETATM 4419 O  O   . HOH   Q 7 .   ? 2.17300   -7.59100  19.56300  1.000 12.19682 ? 502 HOH   B O   1 
HETATM 4420 O  O   . HOH   Q 7 .   ? -19.12700 -7.30400  47.78400  1.000 30.11682 ? 503 HOH   B O   1 
HETATM 4421 O  O   . HOH   Q 7 .   ? -8.25400  7.67500   38.99600  1.000 16.17682 ? 504 HOH   B O   1 
HETATM 4422 O  O   . HOH   Q 7 .   ? 3.40300   -2.98600  58.27100  1.000 21.35682 ? 505 HOH   B O   1 
HETATM 4423 O  O   . HOH   Q 7 .   ? 24.32300  -14.12900 33.89400  1.000 32.91682 ? 506 HOH   B O   1 
HETATM 4424 O  O   . HOH   Q 7 .   ? -7.12700  -6.83300  50.58200  1.000 28.16682 ? 507 HOH   B O   1 
HETATM 4425 O  O   . HOH   Q 7 .   ? 14.13200  -1.97600  56.68400  1.000 28.77682 ? 508 HOH   B O   1 
HETATM 4426 O  O   . HOH   Q 7 .   ? 14.03700  -16.81500 51.72900  1.000 27.61682 ? 509 HOH   B O   1 
HETATM 4427 O  O   . HOH   Q 7 .   ? 4.43600   -20.82300 54.80600  1.000 23.70682 ? 510 HOH   B O   1 
HETATM 4428 O  O   . HOH   Q 7 .   ? 8.89100   11.22300  30.19500  1.000 25.43682 ? 511 HOH   B O   1 
HETATM 4429 O  O   . HOH   Q 7 .   ? -5.28900  5.72700   24.46100  1.000 17.84682 ? 512 HOH   B O   1 
HETATM 4430 O  O   . HOH   Q 7 .   ? 13.898    -29.314   45.806    1.000 17.67682 ? 513 HOH   B O   1 
HETATM 4431 O  O   . HOH   Q 7 .   ? 13.51900  -12.36600 34.08200  1.000 22.21682 ? 514 HOH   B O   1 
HETATM 4432 O  O   . HOH   Q 7 .   ? 14.79800  5.17800   49.04500  1.000 23.74682 ? 515 HOH   B O   1 
HETATM 4433 O  O   . HOH   Q 7 .   ? 14.35000  -25.39900 44.98600  1.000 21.33682 ? 516 HOH   B O   1 
HETATM 4434 O  O   . HOH   Q 7 .   ? 10.05900  -7.91000  49.47800  1.000 12.08682 ? 517 HOH   B O   1 
HETATM 4435 O  O   . HOH   Q 7 .   ? 19.73600  -10.97000 53.07000  1.000 30.07682 ? 518 HOH   B O   1 
HETATM 4436 O  O   . HOH   Q 7 .   ? -5.28300  7.42600   27.08900  1.000 32.02682 ? 519 HOH   B O   1 
HETATM 4437 O  O   . HOH   Q 7 .   ? -11.55100 6.84600   38.62800  1.000 22.83682 ? 520 HOH   B O   1 
HETATM 4438 O  O   . HOH   Q 7 .   ? -11.26400 -17.33100 48.58600  1.000 23.09682 ? 521 HOH   B O   1 
HETATM 4439 O  O   . HOH   Q 7 .   ? 19.31500  -12.20500 41.86400  1.000 21.69682 ? 522 HOH   B O   1 
HETATM 4440 O  O   . HOH   Q 7 .   ? 17.26100  -19.57900 39.35800  1.000 32.39682 ? 523 HOH   B O   1 
HETATM 4441 O  O   . HOH   Q 7 .   ? 16.77100  5.19000   35.72000  1.000 31.08682 ? 524 HOH   B O   1 
HETATM 4442 O  O   . HOH   Q 7 .   ? 16.19100  -1.90400  30.99900  1.000 29.56682 ? 525 HOH   B O   1 
HETATM 4443 O  O   . HOH   Q 7 .   ? 2.32500   8.80500   48.81900  1.000 18.70682 ? 526 HOH   B O   1 
HETATM 4444 O  O   . HOH   Q 7 .   ? 12.45400  -15.86000 34.59900  1.000 13.14682 ? 527 HOH   B O   1 
HETATM 4445 O  O   . HOH   Q 7 .   ? 13.92100  -2.76000  49.28400  1.000 15.31682 ? 528 HOH   B O   1 
HETATM 4446 O  O   . HOH   Q 7 .   ? -16.53400 -21.01200 27.35300  1.000 33.12682 ? 529 HOH   B O   1 
HETATM 4447 O  O   . HOH   Q 7 .   ? 17.47100  -2.54200  33.76400  1.000 25.28682 ? 530 HOH   B O   1 
HETATM 4448 O  O   . HOH   Q 7 .   ? 10.51300  3.23000   31.98400  1.000 12.66682 ? 531 HOH   B O   1 
HETATM 4449 O  O   . HOH   Q 7 .   ? -9.05600  5.25400   24.85400  1.000 27.93682 ? 532 HOH   B O   1 
HETATM 4450 O  O   . HOH   Q 7 .   ? 19.52400  2.97400   49.01000  1.000 34.81682 ? 533 HOH   B O   1 
HETATM 4451 O  O   . HOH   Q 7 .   ? -5.54800  9.00200   48.15600  1.000 28.57682 ? 534 HOH   B O   1 
HETATM 4452 O  O   . HOH   Q 7 .   ? -2.14300  -1.85000  16.92900  1.000 25.29682 ? 535 HOH   B O   1 
HETATM 4453 O  O   . HOH   Q 7 .   ? -9.82800  9.00600   36.45000  1.000 28.07682 ? 536 HOH   B O   1 
HETATM 4454 O  O   . HOH   Q 7 .   ? 4.10100   1.38200   18.07400  1.000 11.61682 ? 537 HOH   B O   1 
HETATM 4455 O  O   . HOH   Q 7 .   ? 19.15000  -0.35000  37.02300  1.000 22.28682 ? 538 HOH   B O   1 
HETATM 4456 O  O   . HOH   Q 7 .   ? -12.49800 -7.85000  46.65200  1.000 9.93682  ? 539 HOH   B O   1 
HETATM 4457 O  O   . HOH   Q 7 .   ? -21.973   -4.240    34.687    1.000 20.34682 ? 540 HOH   B O   1 
HETATM 4458 O  O   . HOH   Q 7 .   ? -1.94500  -5.11400  54.47300  1.000 21.99682 ? 541 HOH   B O   1 
HETATM 4459 O  O   . HOH   Q 7 .   ? 7.48700   -10.03500 50.24100  1.000 11.73682 ? 542 HOH   B O   1 
HETATM 4460 O  O   . HOH   Q 7 .   ? 19.10700  -7.39500  51.40000  1.000 27.51682 ? 543 HOH   B O   1 
HETATM 4461 O  O   . HOH   Q 7 .   ? 6.61200   9.58600   41.63400  1.000 12.08682 ? 544 HOH   B O   1 
HETATM 4462 O  O   . HOH   Q 7 .   ? 7.63500   0.44800   55.20300  1.000 21.61682 ? 545 HOH   B O   1 
HETATM 4463 O  O   . HOH   Q 7 .   ? 4.13600   -25.10700 30.30700  1.000 24.15682 ? 546 HOH   B O   1 
HETATM 4464 O  O   . HOH   Q 7 .   ? -1.88600  -33.47400 34.13400  1.000 34.96682 ? 547 HOH   B O   1 
HETATM 4465 O  O   . HOH   Q 7 .   ? 2.31500   10.41600  33.63500  1.000 28.91682 ? 548 HOH   B O   1 
HETATM 4466 O  O   . HOH   Q 7 .   ? -15.07300 -7.69200  47.32900  1.000 17.58682 ? 549 HOH   B O   1 
HETATM 4467 O  O   . HOH   Q 7 .   ? 5.09900   -22.85400 28.67700  1.000 26.52682 ? 550 HOH   B O   1 
HETATM 4468 O  O   . HOH   Q 7 .   ? -1.65800  -3.98300  51.89000  1.000 12.65682 ? 551 HOH   B O   1 
HETATM 4469 O  O   . HOH   Q 7 .   ? 10.67400  -30.75900 50.79700  1.000 21.74682 ? 552 HOH   B O   1 
HETATM 4470 O  O   . HOH   Q 7 .   ? 0.49600   5.14800   41.49300  1.000 10.73682 ? 553 HOH   B O   1 
HETATM 4471 O  O   . HOH   Q 7 .   ? -5.917    -7.328    15.377    1.000 17.53682 ? 554 HOH   B O   1 
HETATM 4472 O  O   . HOH   Q 7 .   ? 21.74400  -9.57200  43.18000  1.000 27.68682 ? 555 HOH   B O   1 
HETATM 4473 O  O   . HOH   Q 7 .   ? -11.015   -6.373    19.580    1.000 14.87682 ? 556 HOH   B O   1 
HETATM 4474 O  O   . HOH   Q 7 .   ? -4.03500  -20.42100 29.14300  1.000 13.03682 ? 557 HOH   B O   1 
HETATM 4475 O  O   . HOH   Q 7 .   ? -4.80100  11.49000  32.99300  1.000 34.03682 ? 558 HOH   B O   1 
HETATM 4476 O  O   . HOH   Q 7 .   ? -15.74100 3.75000   47.84500  1.000 28.99682 ? 559 HOH   B O   1 
HETATM 4477 O  O   . HOH   Q 7 .   ? 12.65600  -7.36900  25.94700  1.000 10.10682 ? 560 HOH   B O   1 
HETATM 4478 O  O   . HOH   Q 7 .   ? 10.04900  -4.90400  51.26700  1.000 13.80682 ? 561 HOH   B O   1 
HETATM 4479 O  O   . HOH   Q 7 .   ? 5.01000   -1.42400  20.13800  1.000 17.50682 ? 562 HOH   B O   1 
HETATM 4480 O  O   . HOH   Q 7 .   ? 2.65900   -27.03000 33.88700  1.000 17.74682 ? 563 HOH   B O   1 
HETATM 4481 O  O   . HOH   Q 7 .   ? -18.27200 1.28400   39.70000  1.000 23.70682 ? 564 HOH   B O   1 
HETATM 4482 O  O   . HOH   Q 7 .   ? -8.43700  -4.37900  51.17600  1.000 38.01682 ? 565 HOH   B O   1 
HETATM 4483 O  O   . HOH   Q 7 .   ? 8.29700   -28.62800 43.79100  1.000 30.07682 ? 566 HOH   B O   1 
HETATM 4484 O  O   . HOH   Q 7 .   ? 4.98900   -28.02200 35.26800  1.000 25.23682 ? 567 HOH   B O   1 
HETATM 4485 O  O   . HOH   Q 7 .   ? 6.37300   -12.17400 56.93300  1.000 13.10682 ? 568 HOH   B O   1 
HETATM 4486 O  O   . HOH   Q 7 .   ? 22.51700  -9.01000  45.86500  1.000 26.68682 ? 569 HOH   B O   1 
HETATM 4487 O  O   . HOH   Q 7 .   ? -11.08300 8.52700   43.58000  1.000 29.31682 ? 570 HOH   B O   1 
HETATM 4488 O  O   . HOH   Q 7 .   ? 7.18200   11.08400  45.48800  1.000 29.30682 ? 571 HOH   B O   1 
HETATM 4489 O  O   . HOH   Q 7 .   ? -16.46600 -10.21300 46.89200  1.000 16.00682 ? 572 HOH   B O   1 
HETATM 4490 O  O   . HOH   Q 7 .   ? -8.36400  -6.68000  40.92700  1.000 11.39682 ? 573 HOH   B O   1 
HETATM 4491 O  O   . HOH   Q 7 .   ? 1.80900   -18.08000 33.62900  1.000 14.74682 ? 574 HOH   B O   1 
HETATM 4492 O  O   . HOH   Q 7 .   ? 8.45800   6.43500   49.58300  1.000 11.53682 ? 575 HOH   B O   1 
HETATM 4493 O  O   . HOH   Q 7 .   ? -4.51800  -34.42400 38.99300  1.000 21.60682 ? 576 HOH   B O   1 
HETATM 4494 O  O   . HOH   Q 7 .   ? -10.46900 2.03800   20.52900  1.000 31.11682 ? 577 HOH   B O   1 
HETATM 4495 O  O   . HOH   Q 7 .   ? 1.65500   -11.57100 58.11600  1.000 20.99682 ? 578 HOH   B O   1 
HETATM 4496 O  O   . HOH   Q 7 .   ? 8.17900   2.32000   24.22300  1.000 14.29682 ? 579 HOH   B O   1 
HETATM 4497 O  O   . HOH   Q 7 .   ? 11.78700  -3.43200  59.69700  1.000 28.70682 ? 580 HOH   B O   1 
HETATM 4498 O  O   . HOH   Q 7 .   ? -6.37600  -29.86300 37.24100  1.000 21.44682 ? 581 HOH   B O   1 
HETATM 4499 O  O   . HOH   Q 7 .   ? 8.10600   -19.72600 34.13500  1.000 17.14682 ? 582 HOH   B O   1 
HETATM 4500 O  O   . HOH   Q 7 .   ? 2.15600   -22.57500 54.96100  1.000 23.58682 ? 583 HOH   B O   1 
HETATM 4501 O  O   . HOH   Q 7 .   ? -3.63300  -4.67500  50.47000  1.000 13.51682 ? 584 HOH   B O   1 
HETATM 4502 O  O   . HOH   Q 7 .   ? -9.78100  -31.12200 43.11800  1.000 25.80682 ? 585 HOH   B O   1 
HETATM 4503 O  O   . HOH   Q 7 .   ? -0.81400  -28.10900 32.44200  1.000 21.59682 ? 586 HOH   B O   1 
HETATM 4504 O  O   . HOH   Q 7 .   ? -2.72000  -25.52800 29.84600  1.000 23.15682 ? 587 HOH   B O   1 
HETATM 4505 O  O   . HOH   Q 7 .   ? 13.36600  -4.56000  37.27800  1.000 13.21682 ? 588 HOH   B O   1 
HETATM 4506 O  O   . HOH   Q 7 .   ? 5.82100   -15.88100 58.46000  1.000 22.11682 ? 589 HOH   B O   1 
HETATM 4507 O  O   . HOH   Q 7 .   ? 14.74700  -5.28300  30.58400  1.000 20.90682 ? 590 HOH   B O   1 
HETATM 4508 O  O   . HOH   Q 7 .   ? -5.55000  4.06300   22.09900  1.000 17.54682 ? 591 HOH   B O   1 
HETATM 4509 O  O   . HOH   Q 7 .   ? -10.83400 -26.46800 32.20300  1.000 22.12682 ? 592 HOH   B O   1 
HETATM 4510 O  O   . HOH   Q 7 .   ? 9.73700   -4.46600  25.95500  1.000 6.78682  ? 593 HOH   B O   1 
HETATM 4511 O  O   . HOH   Q 7 .   ? 5.67600   2.28800   25.72400  1.000 8.06682  ? 594 HOH   B O   1 
HETATM 4512 O  O   . HOH   Q 7 .   ? 9.64600   -18.55200 28.06700  1.000 30.83682 ? 595 HOH   B O   1 
HETATM 4513 O  O   . HOH   Q 7 .   ? 14.92100  7.11500   45.87700  1.000 23.42682 ? 596 HOH   B O   1 
HETATM 4514 O  O   . HOH   Q 7 .   ? -5.58300  -29.59000 29.19900  1.000 34.35682 ? 597 HOH   B O   1 
HETATM 4515 O  O   . HOH   Q 7 .   ? 3.02600   13.14000  37.68700  1.000 24.13682 ? 598 HOH   B O   1 
HETATM 4516 O  O   . HOH   Q 7 .   ? 8.08600   -9.14400  52.90400  1.000 11.21682 ? 599 HOH   B O   1 
HETATM 4517 O  O   . HOH   Q 7 .   ? -15.24400 -15.51400 32.76100  1.000 25.42682 ? 600 HOH   B O   1 
HETATM 4518 O  O   . HOH   Q 7 .   ? 8.99900   -14.90700 29.17500  1.000 22.41682 ? 601 HOH   B O   1 
HETATM 4519 O  O   . HOH   Q 7 .   ? 23.55800  -15.40700 49.04900  1.000 35.06682 ? 602 HOH   B O   1 
HETATM 4520 O  O   . HOH   Q 7 .   ? -19.54000 -2.95700  39.62800  1.000 17.59682 ? 603 HOH   B O   1 
HETATM 4521 O  O   . HOH   Q 7 .   ? -0.31100  -14.97500 27.73200  1.000 11.49682 ? 604 HOH   B O   1 
HETATM 4522 O  O   . HOH   Q 7 .   ? -0.51400  11.71600  35.42500  1.000 21.25682 ? 605 HOH   B O   1 
HETATM 4523 O  O   . HOH   Q 7 .   ? -3.21200  -28.44000 44.32600  1.000 24.71682 ? 606 HOH   B O   1 
HETATM 4524 O  O   . HOH   Q 7 .   ? 4.11700   0.04600   56.79300  1.000 24.21682 ? 607 HOH   B O   1 
HETATM 4525 O  O   . HOH   Q 7 .   ? -13.63300 4.18400   27.58000  1.000 19.68682 ? 608 HOH   B O   1 
HETATM 4526 O  O   . HOH   Q 7 .   ? -5.71700  -9.19900  54.12300  1.000 27.88682 ? 609 HOH   B O   1 
HETATM 4527 O  O   . HOH   Q 7 .   ? -3.27500  -11.99300 51.46900  1.000 14.08682 ? 610 HOH   B O   1 
HETATM 4528 O  O   . HOH   Q 7 .   ? 5.28300   -30.99000 47.52200  1.000 27.67682 ? 611 HOH   B O   1 
HETATM 4529 O  O   . HOH   Q 7 .   ? 19.79700  -15.80800 41.56000  1.000 24.10682 ? 612 HOH   B O   1 
HETATM 4530 O  O   . HOH   Q 7 .   ? 10.63000  -8.99000  60.45900  1.000 26.24682 ? 613 HOH   B O   1 
HETATM 4531 O  O   . HOH   Q 7 .   ? -4.42200  -3.19900  26.76600  1.000 8.33682  ? 614 HOH   B O   1 
HETATM 4532 O  O   . HOH   Q 7 .   ? 0.45600   -6.80600  53.59500  1.000 21.40682 ? 615 HOH   B O   1 
HETATM 4533 O  O   . HOH   Q 7 .   ? 12.67800  -2.39900  28.82300  1.000 14.04682 ? 616 HOH   B O   1 
HETATM 4534 O  O   . HOH   Q 7 .   ? 6.06500   -18.95000 57.58800  1.000 26.31682 ? 617 HOH   B O   1 
HETATM 4535 O  O   . HOH   Q 7 .   ? 8.09900   7.24300   39.40600  1.000 20.19682 ? 618 HOH   B O   1 
HETATM 4536 O  O   . HOH   Q 7 .   ? 21.496    -5.472    39.945    1.000 26.95682 ? 619 HOH   B O   1 
HETATM 4537 O  O   . HOH   Q 7 .   ? 5.66500   0.50200   22.16300  1.000 11.04682 ? 620 HOH   B O   1 
HETATM 4538 O  O   . HOH   Q 7 .   ? 3.06100   -15.82800 58.60500  1.000 29.32682 ? 621 HOH   B O   1 
HETATM 4539 O  O   . HOH   Q 7 .   ? -1.40700  -22.60900 30.10800  1.000 19.32682 ? 622 HOH   B O   1 
HETATM 4540 O  O   . HOH   Q 7 .   ? -7.992    -30.558   39.359    1.000 19.75682 ? 623 HOH   B O   1 
HETATM 4541 O  O   . HOH   Q 7 .   ? 4.10900   -3.80300  21.70700  1.000 13.99682 ? 624 HOH   B O   1 
HETATM 4542 O  O   . HOH   Q 7 .   ? 14.86000  -13.30400 54.18000  1.000 19.57682 ? 625 HOH   B O   1 
HETATM 4543 O  O   . HOH   Q 7 .   ? -6.16600  0.01000   22.56900  1.000 7.32682  ? 626 HOH   B O   1 
HETATM 4544 O  O   . HOH   Q 7 .   ? -9.77000  -24.49700 40.09300  1.000 21.00682 ? 627 HOH   B O   1 
HETATM 4545 O  O   . HOH   Q 7 .   ? 4.76000   -31.45100 41.51300  1.000 22.53682 ? 628 HOH   B O   1 
HETATM 4546 O  O   . HOH   Q 7 .   ? -17.39800 -15.31900 38.50700  1.000 26.16682 ? 629 HOH   B O   1 
HETATM 4547 O  O   . HOH   Q 7 .   ? -18.00800 -7.57600  38.51400  1.000 29.37682 ? 630 HOH   B O   1 
HETATM 4548 O  O   . HOH   Q 7 .   ? 14.99400  -3.93000  54.85800  1.000 21.87682 ? 631 HOH   B O   1 
HETATM 4549 O  O   . HOH   Q 7 .   ? 12.88600  0.70600   58.49500  1.000 24.54682 ? 632 HOH   B O   1 
HETATM 4550 O  O   . HOH   Q 7 .   ? 4.78000   9.43400   47.81400  1.000 19.19682 ? 633 HOH   B O   1 
HETATM 4551 O  O   . HOH   Q 7 .   ? 6.84700   -25.94800 35.15000  1.000 27.05682 ? 634 HOH   B O   1 
HETATM 4552 O  O   . HOH   Q 7 .   ? -20.783   -6.329    37.339    1.000 19.40682 ? 635 HOH   B O   1 
HETATM 4553 O  O   . HOH   Q 7 .   ? -3.49400  -29.25700 32.44300  1.000 23.65682 ? 636 HOH   B O   1 
HETATM 4554 O  O   . HOH   Q 7 .   ? 16.77500  -23.73200 41.81700  1.000 20.37682 ? 637 HOH   B O   1 
HETATM 4555 O  O   . HOH   Q 7 .   ? -8.30700  -23.38200 46.01600  1.000 28.06682 ? 638 HOH   B O   1 
HETATM 4556 O  O   . HOH   Q 7 .   ? -15.52000 4.58900   40.52600  1.000 20.61682 ? 639 HOH   B O   1 
HETATM 4557 O  O   . HOH   Q 7 .   ? 13.11600  -16.39300 57.90000  1.000 27.37682 ? 640 HOH   B O   1 
HETATM 4558 O  O   . HOH   Q 7 .   ? -17.65200 0.43100   32.96900  1.000 18.99682 ? 641 HOH   B O   1 
HETATM 4559 O  O   . HOH   Q 7 .   ? 5.66400   -30.50300 51.29700  1.000 22.59682 ? 642 HOH   B O   1 
HETATM 4560 O  O   . HOH   Q 7 .   ? 9.04300   -31.27200 40.27700  1.000 19.70682 ? 643 HOH   B O   1 
HETATM 4561 O  O   . HOH   Q 7 .   ? 15.61100  0.12600   55.73100  1.000 28.08682 ? 644 HOH   B O   1 
HETATM 4562 O  O   . HOH   Q 7 .   ? 11.15900  2.75300   56.09300  1.000 23.69682 ? 645 HOH   B O   1 
HETATM 4563 O  O   . HOH   Q 7 .   ? -4.79400  11.08900  42.49100  1.000 17.79682 ? 646 HOH   B O   1 
HETATM 4564 O  O   . HOH   Q 7 .   ? -7.12400  -25.01700 55.08100  1.000 41.23682 ? 647 HOH   B O   1 
HETATM 4565 O  O   . HOH   Q 7 .   ? -12.18800 6.44700   40.93600  1.000 27.52682 ? 648 HOH   B O   1 
HETATM 4566 O  O   . HOH   Q 7 .   ? 6.58200   -0.24400  26.68700  1.000 11.85682 ? 649 HOH   B O   1 
HETATM 4567 O  O   . HOH   Q 7 .   ? -8.53900  1.59000   22.63300  1.000 9.49682  ? 650 HOH   B O   1 
HETATM 4568 O  O   . HOH   Q 7 .   ? -7.00000  -3.95500  28.16700  1.000 11.03682 ? 651 HOH   B O   1 
HETATM 4569 O  O   . HOH   Q 7 .   ? -16.22500 2.39400   33.89700  1.000 16.48682 ? 652 HOH   B O   1 
HETATM 4570 O  O   . HOH   Q 7 .   ? -4.36100  -11.88300 55.33200  1.000 32.17682 ? 653 HOH   B O   1 
HETATM 4571 O  O   . HOH   Q 7 .   ? 17.86500  -3.82000  42.94900  1.000 27.09682 ? 654 HOH   B O   1 
HETATM 4572 O  O   . HOH   Q 7 .   ? -4.05200  5.91900   20.36700  1.000 29.59682 ? 655 HOH   B O   1 
HETATM 4573 O  O   . HOH   Q 7 .   ? 7.09500   -4.82000  25.80900  1.000 7.75682  ? 656 HOH   B O   1 
HETATM 4574 O  O   . HOH   Q 7 .   ? 6.66000   -27.52100 45.28900  1.000 15.97682 ? 657 HOH   B O   1 
HETATM 4575 O  O   . HOH   Q 7 .   ? 13.73700  -7.96700  58.78100  1.000 23.73682 ? 658 HOH   B O   1 
HETATM 4576 O  O   . HOH   Q 7 .   ? -1.45100  10.93700  32.35200  1.000 29.29682 ? 659 HOH   B O   1 
HETATM 4577 O  O   . HOH   Q 7 .   ? -11.54300 -19.43600 47.38600  1.000 31.49682 ? 660 HOH   B O   1 
HETATM 4578 O  O   . HOH   Q 7 .   ? -4.80500  -27.00100 26.44400  1.000 23.96682 ? 661 HOH   B O   1 
HETATM 4579 O  O   . HOH   Q 7 .   ? -3.57300  -18.23500 52.77800  1.000 21.62682 ? 662 HOH   B O   1 
HETATM 4580 O  O   . HOH   Q 7 .   ? 9.00700   0.26500   27.88800  1.000 14.48682 ? 663 HOH   B O   1 
HETATM 4581 O  O   . HOH   Q 7 .   ? -11.08800 -13.61800 51.40900  1.000 23.03682 ? 664 HOH   B O   1 
HETATM 4582 O  O   . HOH   Q 7 .   ? 19.803    -10.202   57.578    1.000 31.05682 ? 665 HOH   B O   1 
HETATM 4583 O  O   . HOH   Q 7 .   ? -9.78900  -22.28400 43.90200  1.000 20.90682 ? 666 HOH   B O   1 
HETATM 4584 O  O   . HOH   Q 7 .   ? 12.48500  -18.16600 56.18200  1.000 25.02682 ? 667 HOH   B O   1 
HETATM 4585 O  O   . HOH   Q 7 .   ? 4.61100   10.03600  26.59900  1.000 28.93682 ? 668 HOH   B O   1 
HETATM 4586 O  O   . HOH   Q 7 .   ? 7.91500   -10.97400 59.02500  1.000 19.15682 ? 669 HOH   B O   1 
HETATM 4587 O  O   . HOH   Q 7 .   ? 10.55100  4.79400   29.61200  1.000 8.50682  ? 670 HOH   B O   1 
HETATM 4588 O  O   . HOH   Q 7 .   ? 13.87400  5.63800   26.95000  1.000 24.77682 ? 671 HOH   B O   1 
HETATM 4589 O  O   . HOH   Q 7 .   ? -12.32000 0.74800   49.35700  1.000 27.18682 ? 672 HOH   B O   1 
HETATM 4590 O  O   . HOH   Q 7 .   ? 12.64200  -16.55300 54.06200  1.000 20.57682 ? 673 HOH   B O   1 
HETATM 4591 O  O   . HOH   Q 7 .   ? 5.39100   -20.67300 25.97400  1.000 32.32682 ? 674 HOH   B O   1 
HETATM 4592 O  O   . HOH   Q 7 .   ? 8.62600   9.01800   36.99100  1.000 23.51682 ? 675 HOH   B O   1 
HETATM 4593 O  O   . HOH   Q 7 .   ? -12.13000 -8.56100  21.81600  1.000 22.16682 ? 676 HOH   B O   1 
HETATM 4594 O  O   . HOH   Q 7 .   ? 4.71700   10.29500  30.82000  1.000 23.75682 ? 677 HOH   B O   1 
HETATM 4595 O  O   . HOH   Q 7 .   ? 8.79100   -20.14000 58.47500  1.000 21.95682 ? 678 HOH   B O   1 
HETATM 4596 O  O   . HOH   Q 7 .   ? -3.49800  11.09700  39.79800  1.000 25.93682 ? 679 HOH   B O   1 
HETATM 4597 O  O   . HOH   Q 7 .   ? -1.53700  -0.98400  52.76800  1.000 20.24682 ? 680 HOH   B O   1 
HETATM 4598 O  O   . HOH   Q 7 .   ? -5.59800  -14.41700 50.82200  1.000 25.22682 ? 681 HOH   B O   1 
HETATM 4599 O  O   . HOH   Q 7 .   ? 9.54400   -13.44700 59.15600  1.000 20.81682 ? 682 HOH   B O   1 
HETATM 4600 O  O   . HOH   Q 7 .   ? -11.79900 6.67300   30.37500  1.000 12.22682 ? 683 HOH   B O   1 
HETATM 4601 O  O   . HOH   Q 7 .   ? 20.14000  -16.66700 54.46700  1.000 28.78682 ? 684 HOH   B O   1 
HETATM 4602 O  O   . HOH   Q 7 .   ? 4.21400   -31.25400 45.52800  1.000 25.61682 ? 685 HOH   B O   1 
HETATM 4603 O  O   . HOH   Q 7 .   ? 8.49200   1.50300   58.50900  1.000 26.16682 ? 686 HOH   B O   1 
HETATM 4604 O  O   . HOH   Q 7 .   ? -15.61200 -12.59300 30.14300  1.000 16.59682 ? 687 HOH   B O   1 
HETATM 4605 O  O   . HOH   Q 7 .   ? 8.912     4.508     54.774    1.000 24.12682 ? 688 HOH   B O   1 
HETATM 4606 O  O   . HOH   Q 7 .   ? -2.78300  7.76400   25.00200  1.000 31.38682 ? 689 HOH   B O   1 
HETATM 4607 O  O   . HOH   Q 7 .   ? -17.53000 -6.08200  41.10600  1.000 19.00682 ? 690 HOH   B O   1 
HETATM 4608 O  O   . HOH   Q 7 .   ? 14.62300  -2.46000  44.71600  1.000 18.31682 ? 691 HOH   B O   1 
HETATM 4609 O  O   . HOH   Q 7 .   ? 0.09900   -25.48800 29.24700  1.000 36.27682 ? 692 HOH   B O   1 
HETATM 4610 O  O   . HOH   Q 7 .   ? -16.80500 4.60900   43.36500  1.000 29.00682 ? 693 HOH   B O   1 
HETATM 4611 O  O   . HOH   Q 7 .   ? 19.46900  0.70500   52.92100  1.000 23.22682 ? 694 HOH   B O   1 
HETATM 4612 O  O   . HOH   Q 7 .   ? 15.76800  7.59200   43.01800  1.000 27.82682 ? 695 HOH   B O   1 
HETATM 4613 O  O   . HOH   Q 7 .   ? 14.568    -27.648   41.787    1.000 27.35682 ? 696 HOH   B O   1 
HETATM 4614 O  O   . HOH   Q 7 .   ? -20.703   -4.638    31.749    1.000 21.37682 ? 697 HOH   B O   1 
HETATM 4615 O  O   . HOH   Q 7 .   ? 2.28800   7.02500   20.59600  1.000 23.08682 ? 698 HOH   B O   1 
HETATM 4616 O  O   . HOH   Q 7 .   ? 15.23000  -6.08600  56.48400  1.000 31.25682 ? 699 HOH   B O   1 
HETATM 4617 O  O   . HOH   Q 7 .   ? -5.13800  10.56800  38.28000  1.000 20.04682 ? 700 HOH   B O   1 
HETATM 4618 O  O   . HOH   Q 7 .   ? 14.44300  -5.63500  47.35500  1.000 15.71682 ? 701 HOH   B O   1 
HETATM 4619 O  O   . HOH   Q 7 .   ? 2.64100   -19.15300 25.34100  1.000 18.04682 ? 702 HOH   B O   1 
HETATM 4620 O  O   . HOH   Q 7 .   ? -4.45700  -29.71200 34.94500  1.000 16.70682 ? 703 HOH   B O   1 
HETATM 4621 O  O   . HOH   Q 7 .   ? -6.961    -30.312   33.122    1.000 26.27682 ? 704 HOH   B O   1 
HETATM 4622 O  O   . HOH   Q 7 .   ? -0.27600  12.36400  40.91500  1.000 24.47682 ? 705 HOH   B O   1 
HETATM 4623 O  O   . HOH   Q 7 .   ? -11.34400 -25.88800 34.87100  1.000 30.17682 ? 706 HOH   B O   1 
HETATM 4624 O  O   . HOH   Q 7 .   ? 14.14100  -9.53300  32.40400  1.000 15.13682 ? 707 HOH   B O   1 
HETATM 4625 O  O   . HOH   Q 7 .   ? -10.239   10.237    29.518    1.000 26.66682 ? 708 HOH   B O   1 
HETATM 4626 O  O   . HOH   Q 7 .   ? -3.05700  0.99100   52.06900  1.000 30.20682 ? 709 HOH   B O   1 
HETATM 4627 O  O   . HOH   Q 7 .   ? -3.54400  -24.19900 55.22000  1.000 39.38682 ? 710 HOH   B O   1 
HETATM 4628 O  O   . HOH   Q 7 .   ? -1.95900  -30.79500 44.56300  1.000 11.66682 ? 711 HOH   B O   1 
HETATM 4629 O  O   . HOH   Q 7 .   ? -14.51900 -24.41600 35.81700  1.000 27.07682 ? 712 HOH   B O   1 
HETATM 4630 O  O   . HOH   Q 7 .   ? 11.88500  -5.69800  58.81900  1.000 30.02682 ? 713 HOH   B O   1 
HETATM 4631 O  O   . HOH   Q 7 .   ? 3.859     -31.660   34.054    1.000 24.25682 ? 714 HOH   B O   1 
HETATM 4632 O  O   . HOH   Q 7 .   ? 7.61200   -15.46100 59.90400  1.000 23.99682 ? 715 HOH   B O   1 
HETATM 4633 O  O   . HOH   Q 7 .   ? -20.95200 -1.97500  42.44300  1.000 31.01682 ? 716 HOH   B O   1 
HETATM 4634 O  O   . HOH   Q 7 .   ? 23.941    4.646     39.069    1.000 27.62682 ? 717 HOH   B O   1 
HETATM 4635 O  O   . HOH   Q 7 .   ? 5.98300   1.79200   57.23400  1.000 27.79682 ? 718 HOH   B O   1 
HETATM 4636 O  O   . HOH   Q 7 .   ? 12.59600  2.47900   32.13900  1.000 25.24682 ? 719 HOH   B O   1 
HETATM 4637 O  O   . HOH   Q 7 .   ? 0.37700   -14.56000 25.03300  1.000 21.31682 ? 720 HOH   B O   1 
HETATM 4638 O  O   . HOH   Q 7 .   ? -3.27200  -4.13200  56.87400  1.000 31.53682 ? 721 HOH   B O   1 
HETATM 4639 O  O   . HOH   Q 7 .   ? -11.70600 -23.77600 36.68900  1.000 17.72682 ? 722 HOH   B O   1 
HETATM 4640 O  O   . HOH   Q 7 .   ? -1.83700  -4.07900  17.23100  1.000 29.17682 ? 723 HOH   B O   1 
HETATM 4641 O  O   . HOH   Q 7 .   ? 0.730     -31.528   52.145    1.000 28.09682 ? 724 HOH   B O   1 
HETATM 4642 O  O   . HOH   Q 7 .   ? 14.03300  -4.71000  28.45400  1.000 21.86682 ? 725 HOH   B O   1 
HETATM 4643 O  O   . HOH   Q 7 .   ? 6.54700   -31.11000 42.90300  1.000 26.96682 ? 726 HOH   B O   1 
HETATM 4644 O  O   . HOH   Q 7 .   ? -10.745   -9.423    53.369    1.000 23.30682 ? 727 HOH   B O   1 
HETATM 4645 O  O   . HOH   Q 7 .   ? -4.84300  -32.44000 37.28500  1.000 23.25682 ? 728 HOH   B O   1 
HETATM 4646 O  O   . HOH   Q 7 .   ? -5.81700  -16.80800 51.46500  1.000 26.07682 ? 729 HOH   B O   1 
HETATM 4647 O  O   . HOH   Q 7 .   ? 11.01600  6.58800   51.17200  1.000 21.36682 ? 730 HOH   B O   1 
HETATM 4648 O  O   . HOH   Q 7 .   ? -3.534    -8.585    16.345    1.000 31.58682 ? 731 HOH   B O   1 
HETATM 4649 O  O   . HOH   Q 7 .   ? 10.42200  -1.96300  26.90700  1.000 13.44682 ? 732 HOH   B O   1 
HETATM 4650 O  O   . HOH   Q 7 .   ? 22.39200  -15.59800 53.06900  1.000 34.94682 ? 733 HOH   B O   1 
HETATM 4651 O  O   . HOH   Q 7 .   ? -13.21900 -27.03900 31.48900  1.000 29.99682 ? 734 HOH   B O   1 
HETATM 4652 O  O   . HOH   Q 7 .   ? 6.69700   8.91900   49.54300  1.000 26.15682 ? 735 HOH   B O   1 
HETATM 4653 O  O   . HOH   Q 7 .   ? 14.64700  -1.18900  28.54900  1.000 31.02682 ? 736 HOH   B O   1 
HETATM 4654 O  O   . HOH   Q 7 .   ? -8.522    -33.428   44.711    1.000 30.49682 ? 737 HOH   B O   1 
HETATM 4655 O  O   . HOH   Q 7 .   ? 23.587    -9.455    39.878    1.000 35.23682 ? 738 HOH   B O   1 
HETATM 4656 O  O   . HOH   Q 7 .   ? -12.22200 -11.93900 52.62900  1.000 29.24682 ? 739 HOH   B O   1 
HETATM 4657 O  O   . HOH   Q 7 .   ? -10.049   -28.826   38.565    1.000 25.56682 ? 740 HOH   B O   1 
HETATM 4658 O  O   . HOH   Q 7 .   ? 18.40500  0.01100   34.68400  1.000 23.82682 ? 741 HOH   B O   1 
HETATM 4659 O  O   . HOH   Q 7 .   ? -13.59700 4.49500   30.31100  1.000 18.46682 ? 742 HOH   B O   1 
HETATM 4660 O  O   . HOH   Q 7 .   ? 2.28800   -3.72100  60.59700  1.000 34.81682 ? 743 HOH   B O   1 
HETATM 4661 O  O   . HOH   Q 7 .   ? 20.893    0.017     41.333    1.000 28.49682 ? 744 HOH   B O   1 
HETATM 4662 O  O   . HOH   Q 7 .   ? -13.867   10.424    44.571    1.000 35.34682 ? 745 HOH   B O   1 
HETATM 4663 O  O   . HOH   Q 7 .   ? 6.39400   1.81500   19.60900  1.000 13.02682 ? 746 HOH   B O   1 
HETATM 4664 O  O   . HOH   Q 7 .   ? 0.58800   13.89000  39.37100  1.000 31.53682 ? 747 HOH   B O   1 
HETATM 4665 O  O   . HOH   Q 7 .   ? 2.04700   10.97900  30.87100  1.000 35.44682 ? 748 HOH   B O   1 
HETATM 4666 O  O   . HOH   Q 7 .   ? 12.89300  4.89400   51.46800  1.000 19.92682 ? 749 HOH   B O   1 
HETATM 4667 O  O   . HOH   Q 7 .   ? 21.455    -0.758    39.083    1.000 28.26682 ? 750 HOH   B O   1 
HETATM 4668 O  O   . HOH   Q 7 .   ? 8.65000   -21.57500 31.81200  1.000 26.14682 ? 751 HOH   B O   1 
HETATM 4669 O  O   . HOH   Q 7 .   ? -10.290   -15.491   16.606    1.000 40.18682 ? 752 HOH   B O   1 
HETATM 4670 O  O   . HOH   Q 7 .   ? -0.44600  -7.60100  18.18100  1.000 16.34682 ? 753 HOH   B O   1 
HETATM 4671 O  O   . HOH   Q 7 .   ? -7.58500  -25.70400 46.58000  1.000 32.24682 ? 754 HOH   B O   1 
HETATM 4672 O  O   . HOH   Q 7 .   ? 2.58100   7.17500   17.97700  1.000 34.98682 ? 755 HOH   B O   1 
HETATM 4673 O  O   . HOH   Q 7 .   ? 11.62500  4.10300   27.38000  1.000 16.69682 ? 756 HOH   B O   1 
HETATM 4674 O  O   . HOH   Q 7 .   ? 0.17400   -22.41100 56.57100  1.000 27.25682 ? 757 HOH   B O   1 
HETATM 4675 O  O   . HOH   Q 7 .   ? -5.52000  8.48500   24.22500  1.000 32.51682 ? 758 HOH   B O   1 
HETATM 4676 O  O   . HOH   Q 7 .   ? 17.68800  6.20800   49.59700  1.000 37.87682 ? 759 HOH   B O   1 
HETATM 4677 O  O   . HOH   Q 7 .   ? 7.09500   -1.21300  24.08900  1.000 11.31682 ? 760 HOH   B O   1 
HETATM 4678 O  O   . HOH   Q 7 .   ? -8.00200  3.76000   21.93100  1.000 26.41682 ? 761 HOH   B O   1 
HETATM 4679 O  O   . HOH   Q 7 .   ? 11.499    -2.161    64.833    1.000 28.35682 ? 762 HOH   B O   1 
HETATM 4680 O  O   . HOH   Q 7 .   ? 12.91100  1.72200   29.33100  1.000 22.21682 ? 763 HOH   B O   1 
HETATM 4681 O  O   . HOH   Q 7 .   ? 19.147    -6.222    56.895    1.000 40.51682 ? 764 HOH   B O   1 
HETATM 4682 O  O   . HOH   Q 7 .   ? -8.33800  10.92100  35.30400  1.000 29.56682 ? 765 HOH   B O   1 
HETATM 4683 O  O   . HOH   Q 7 .   ? 3.032     -29.332   32.159    1.000 29.88682 ? 766 HOH   B O   1 
HETATM 4684 O  O   . HOH   Q 7 .   ? 16.98400  8.15000   47.19300  1.000 38.67682 ? 767 HOH   B O   1 
HETATM 4685 O  O   . HOH   Q 7 .   ? -10.60300 -24.68800 42.59500  1.000 27.21682 ? 768 HOH   B O   1 
HETATM 4686 O  O   . HOH   Q 7 .   ? -6.77500  2.22700   18.81900  1.000 32.91682 ? 769 HOH   B O   1 
HETATM 4687 O  O   . HOH   Q 7 .   ? -6.95500  -22.31600 55.43900  1.000 39.11682 ? 770 HOH   B O   1 
HETATM 4688 O  O   . HOH   Q 7 .   ? -9.98200  -28.95900 32.63400  1.000 26.35682 ? 771 HOH   B O   1 
HETATM 4689 O  O   . HOH   Q 7 .   ? -17.47100 2.82500   45.82000  1.000 29.16682 ? 772 HOH   B O   1 
HETATM 4690 O  O   . HOH   Q 7 .   ? -3.40000  -31.69100 31.69000  1.000 31.63682 ? 773 HOH   B O   1 
HETATM 4691 O  O   . HOH   Q 7 .   ? -12.46000 5.47400   20.94000  1.000 31.88682 ? 774 HOH   B O   1 
HETATM 4692 O  O   . HOH   Q 7 .   ? 21.91200  -12.10600 41.53600  1.000 34.01682 ? 775 HOH   B O   1 
HETATM 4693 O  O   . HOH   Q 7 .   ? 11.82700  -21.31900 31.28200  1.000 41.23682 ? 776 HOH   B O   1 
HETATM 4694 O  O   . HOH   Q 7 .   ? 9.09300   -17.53500 60.02800  1.000 28.45682 ? 777 HOH   B O   1 
HETATM 4695 O  O   . HOH   Q 7 .   ? 21.384    3.384     46.950    1.000 27.01682 ? 778 HOH   B O   1 
HETATM 4696 O  O   . HOH   Q 7 .   ? 16.16500  -8.08400  29.33300  1.000 32.94682 ? 779 HOH   B O   1 
HETATM 4697 O  O   . HOH   Q 7 .   ? 6.42800   -3.79400  23.44400  1.000 6.11682  ? 780 HOH   B O   1 
HETATM 4698 O  O   . HOH   Q 7 .   ? -2.91000  13.64300  33.12500  1.000 37.91682 ? 781 HOH   B O   1 
HETATM 4699 O  O   . HOH   Q 7 .   ? 3.79400   -27.08800 28.32900  1.000 34.45682 ? 782 HOH   B O   1 
HETATM 4700 O  O   . HOH   Q 7 .   ? 1.39900   -16.32400 23.57800  1.000 25.84682 ? 783 HOH   B O   1 
HETATM 4701 O  O   . HOH   Q 7 .   ? -20.86500 -0.07200  32.66400  1.000 34.72682 ? 784 HOH   B O   1 
HETATM 4702 O  O   . HOH   Q 7 .   ? 15.94300  -10.23000 30.63800  1.000 29.02682 ? 785 HOH   B O   1 
HETATM 4703 O  O   . HOH   Q 7 .   ? -20.959   -1.690    30.886    1.000 24.74682 ? 786 HOH   B O   1 
HETATM 4704 O  O   . HOH   Q 7 .   ? 0.83500   5.33400   16.57100  1.000 25.61682 ? 787 HOH   B O   1 
HETATM 4705 O  O   . HOH   Q 7 .   ? -0.640    1.556     58.199    1.000 32.66682 ? 788 HOH   B O   1 
HETATM 4706 O  O   . HOH   Q 7 .   ? -5.54100  2.97400   16.79600  1.000 40.19682 ? 789 HOH   B O   1 
# 
