data_8Z2H
# 
_entry.id   8Z2H 
# 
_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   8Z2H         pdb_00008z2h 10.2210/pdb8z2h/pdb 
WWPDB D_1300046824 ?            ?                   
# 
_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                        8Z2H 
_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 
Q123H/Q138A/S176A/N202H/S226P/R228S/D250C/E296C ? ? 
2 non-polymer syn '4-[2-hydroxyethyloxy(oxidanyl)phosphoryl]benzoic acid' 246.154   2   ?        ? ? ? 
3 non-polymer syn 'CALCIUM ION'                                           40.078    2   ?        ? ? ? 
4 water       nat water                                                   18.015    199 ?        ? ? ? 
# 
_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 '4-[2-hydroxyethyloxy(oxidanyl)phosphoryl]benzoic acid' A1L0N 
3 'CALCIUM ION'                                           CA    
4 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 
A1L0N non-polymer         . '4-[2-hydroxyethyloxy(oxidanyl)phosphoryl]benzoic acid' ? 'C9 H11 O6 P'    246.154 
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  
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 
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  ?   ?   ?   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  ?   ?   ?   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        A1L0N 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L0N 
_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 A1L0N 1   401 1   A1L0N DRG A . 
D 3 CA    1   402 1   CA    CA  A . 
E 2 A1L0N 1   401 2   A1L0N DRG B . 
F 3 CA    1   402 2   CA    CA  B . 
G 4 HOH   1   501 165 HOH   HOH A . 
G 4 HOH   2   502 103 HOH   HOH A . 
G 4 HOH   3   503 72  HOH   HOH A . 
G 4 HOH   4   504 171 HOH   HOH A . 
G 4 HOH   5   505 70  HOH   HOH A . 
G 4 HOH   6   506 178 HOH   HOH A . 
G 4 HOH   7   507 105 HOH   HOH A . 
G 4 HOH   8   508 213 HOH   HOH A . 
G 4 HOH   9   509 9   HOH   HOH A . 
G 4 HOH   10  510 117 HOH   HOH A . 
G 4 HOH   11  511 163 HOH   HOH A . 
G 4 HOH   12  512 195 HOH   HOH A . 
G 4 HOH   13  513 157 HOH   HOH A . 
G 4 HOH   14  514 11  HOH   HOH A . 
G 4 HOH   15  515 183 HOH   HOH A . 
G 4 HOH   16  516 21  HOH   HOH A . 
G 4 HOH   17  517 110 HOH   HOH A . 
G 4 HOH   18  518 190 HOH   HOH A . 
G 4 HOH   19  519 77  HOH   HOH A . 
G 4 HOH   20  520 189 HOH   HOH A . 
G 4 HOH   21  521 160 HOH   HOH A . 
G 4 HOH   22  522 61  HOH   HOH A . 
G 4 HOH   23  523 24  HOH   HOH A . 
G 4 HOH   24  524 120 HOH   HOH A . 
G 4 HOH   25  525 3   HOH   HOH A . 
G 4 HOH   26  526 69  HOH   HOH A . 
G 4 HOH   27  527 200 HOH   HOH A . 
G 4 HOH   28  528 132 HOH   HOH A . 
G 4 HOH   29  529 65  HOH   HOH A . 
G 4 HOH   30  530 182 HOH   HOH A . 
G 4 HOH   31  531 91  HOH   HOH A . 
G 4 HOH   32  532 87  HOH   HOH A . 
G 4 HOH   33  533 149 HOH   HOH A . 
G 4 HOH   34  534 169 HOH   HOH A . 
G 4 HOH   35  535 50  HOH   HOH A . 
G 4 HOH   36  536 80  HOH   HOH A . 
G 4 HOH   37  537 37  HOH   HOH A . 
G 4 HOH   38  538 95  HOH   HOH A . 
G 4 HOH   39  539 173 HOH   HOH A . 
G 4 HOH   40  540 22  HOH   HOH A . 
G 4 HOH   41  541 172 HOH   HOH A . 
G 4 HOH   42  542 8   HOH   HOH A . 
G 4 HOH   43  543 140 HOH   HOH A . 
G 4 HOH   44  544 122 HOH   HOH A . 
G 4 HOH   45  545 25  HOH   HOH A . 
G 4 HOH   46  546 54  HOH   HOH A . 
G 4 HOH   47  547 214 HOH   HOH A . 
G 4 HOH   48  548 78  HOH   HOH A . 
G 4 HOH   49  549 71  HOH   HOH A . 
G 4 HOH   50  550 58  HOH   HOH A . 
G 4 HOH   51  551 63  HOH   HOH A . 
G 4 HOH   52  552 90  HOH   HOH A . 
G 4 HOH   53  553 57  HOH   HOH A . 
G 4 HOH   54  554 123 HOH   HOH A . 
G 4 HOH   55  555 124 HOH   HOH A . 
G 4 HOH   56  556 29  HOH   HOH A . 
G 4 HOH   57  557 13  HOH   HOH A . 
G 4 HOH   58  558 152 HOH   HOH A . 
G 4 HOH   59  559 55  HOH   HOH A . 
G 4 HOH   60  560 16  HOH   HOH A . 
G 4 HOH   61  561 17  HOH   HOH A . 
G 4 HOH   62  562 34  HOH   HOH A . 
G 4 HOH   63  563 194 HOH   HOH A . 
G 4 HOH   64  564 52  HOH   HOH A . 
G 4 HOH   65  565 129 HOH   HOH A . 
G 4 HOH   66  566 30  HOH   HOH A . 
G 4 HOH   67  567 32  HOH   HOH A . 
G 4 HOH   68  568 2   HOH   HOH A . 
G 4 HOH   69  569 150 HOH   HOH A . 
G 4 HOH   70  570 193 HOH   HOH A . 
G 4 HOH   71  571 135 HOH   HOH A . 
G 4 HOH   72  572 39  HOH   HOH A . 
G 4 HOH   73  573 56  HOH   HOH A . 
G 4 HOH   74  574 33  HOH   HOH A . 
G 4 HOH   75  575 48  HOH   HOH A . 
G 4 HOH   76  576 151 HOH   HOH A . 
G 4 HOH   77  577 109 HOH   HOH A . 
G 4 HOH   78  578 118 HOH   HOH A . 
G 4 HOH   79  579 28  HOH   HOH A . 
G 4 HOH   80  580 142 HOH   HOH A . 
G 4 HOH   81  581 97  HOH   HOH A . 
G 4 HOH   82  582 38  HOH   HOH A . 
G 4 HOH   83  583 18  HOH   HOH A . 
G 4 HOH   84  584 102 HOH   HOH A . 
G 4 HOH   85  585 82  HOH   HOH A . 
G 4 HOH   86  586 45  HOH   HOH A . 
G 4 HOH   87  587 203 HOH   HOH A . 
G 4 HOH   88  588 164 HOH   HOH A . 
G 4 HOH   89  589 212 HOH   HOH A . 
G 4 HOH   90  590 119 HOH   HOH A . 
G 4 HOH   91  591 125 HOH   HOH A . 
G 4 HOH   92  592 60  HOH   HOH A . 
G 4 HOH   93  593 175 HOH   HOH A . 
G 4 HOH   94  594 192 HOH   HOH A . 
G 4 HOH   95  595 99  HOH   HOH A . 
G 4 HOH   96  596 167 HOH   HOH A . 
G 4 HOH   97  597 73  HOH   HOH A . 
G 4 HOH   98  598 108 HOH   HOH A . 
H 4 HOH   1   501 100 HOH   HOH B . 
H 4 HOH   2   502 159 HOH   HOH B . 
H 4 HOH   3   503 209 HOH   HOH B . 
H 4 HOH   4   504 201 HOH   HOH B . 
H 4 HOH   5   505 136 HOH   HOH B . 
H 4 HOH   6   506 205 HOH   HOH B . 
H 4 HOH   7   507 146 HOH   HOH B . 
H 4 HOH   8   508 116 HOH   HOH B . 
H 4 HOH   9   509 211 HOH   HOH B . 
H 4 HOH   10  510 86  HOH   HOH B . 
H 4 HOH   11  511 188 HOH   HOH B . 
H 4 HOH   12  512 42  HOH   HOH B . 
H 4 HOH   13  513 31  HOH   HOH B . 
H 4 HOH   14  514 148 HOH   HOH B . 
H 4 HOH   15  515 4   HOH   HOH B . 
H 4 HOH   16  516 162 HOH   HOH B . 
H 4 HOH   17  517 27  HOH   HOH B . 
H 4 HOH   18  518 43  HOH   HOH B . 
H 4 HOH   19  519 7   HOH   HOH B . 
H 4 HOH   20  520 144 HOH   HOH B . 
H 4 HOH   21  521 133 HOH   HOH B . 
H 4 HOH   22  522 88  HOH   HOH B . 
H 4 HOH   23  523 15  HOH   HOH B . 
H 4 HOH   24  524 156 HOH   HOH B . 
H 4 HOH   25  525 64  HOH   HOH B . 
H 4 HOH   26  526 51  HOH   HOH B . 
H 4 HOH   27  527 134 HOH   HOH B . 
H 4 HOH   28  528 145 HOH   HOH B . 
H 4 HOH   29  529 94  HOH   HOH B . 
H 4 HOH   30  530 121 HOH   HOH B . 
H 4 HOH   31  531 210 HOH   HOH B . 
H 4 HOH   32  532 75  HOH   HOH B . 
H 4 HOH   33  533 23  HOH   HOH B . 
H 4 HOH   34  534 139 HOH   HOH B . 
H 4 HOH   35  535 6   HOH   HOH B . 
H 4 HOH   36  536 93  HOH   HOH B . 
H 4 HOH   37  537 40  HOH   HOH B . 
H 4 HOH   38  538 85  HOH   HOH B . 
H 4 HOH   39  539 143 HOH   HOH B . 
H 4 HOH   40  540 96  HOH   HOH B . 
H 4 HOH   41  541 126 HOH   HOH B . 
H 4 HOH   42  542 74  HOH   HOH B . 
H 4 HOH   43  543 10  HOH   HOH B . 
H 4 HOH   44  544 130 HOH   HOH B . 
H 4 HOH   45  545 53  HOH   HOH B . 
H 4 HOH   46  546 84  HOH   HOH B . 
H 4 HOH   47  547 114 HOH   HOH B . 
H 4 HOH   48  548 36  HOH   HOH B . 
H 4 HOH   49  549 59  HOH   HOH B . 
H 4 HOH   50  550 104 HOH   HOH B . 
H 4 HOH   51  551 1   HOH   HOH B . 
H 4 HOH   52  552 161 HOH   HOH B . 
H 4 HOH   53  553 66  HOH   HOH B . 
H 4 HOH   54  554 98  HOH   HOH B . 
H 4 HOH   55  555 44  HOH   HOH B . 
H 4 HOH   56  556 46  HOH   HOH B . 
H 4 HOH   57  557 154 HOH   HOH B . 
H 4 HOH   58  558 83  HOH   HOH B . 
H 4 HOH   59  559 68  HOH   HOH B . 
H 4 HOH   60  560 41  HOH   HOH B . 
H 4 HOH   61  561 5   HOH   HOH B . 
H 4 HOH   62  562 12  HOH   HOH B . 
H 4 HOH   63  563 187 HOH   HOH B . 
H 4 HOH   64  564 47  HOH   HOH B . 
H 4 HOH   65  565 19  HOH   HOH B . 
H 4 HOH   66  566 20  HOH   HOH B . 
H 4 HOH   67  567 67  HOH   HOH B . 
H 4 HOH   68  568 179 HOH   HOH B . 
H 4 HOH   69  569 170 HOH   HOH B . 
H 4 HOH   70  570 181 HOH   HOH B . 
H 4 HOH   71  571 155 HOH   HOH B . 
H 4 HOH   72  572 185 HOH   HOH B . 
H 4 HOH   73  573 26  HOH   HOH B . 
H 4 HOH   74  574 197 HOH   HOH B . 
H 4 HOH   75  575 81  HOH   HOH B . 
H 4 HOH   76  576 49  HOH   HOH B . 
H 4 HOH   77  577 115 HOH   HOH B . 
H 4 HOH   78  578 35  HOH   HOH B . 
H 4 HOH   79  579 174 HOH   HOH B . 
H 4 HOH   80  580 186 HOH   HOH B . 
H 4 HOH   81  581 207 HOH   HOH B . 
H 4 HOH   82  582 76  HOH   HOH B . 
H 4 HOH   83  583 92  HOH   HOH B . 
H 4 HOH   84  584 147 HOH   HOH B . 
H 4 HOH   85  585 166 HOH   HOH B . 
H 4 HOH   86  586 14  HOH   HOH B . 
H 4 HOH   87  587 184 HOH   HOH B . 
H 4 HOH   88  588 177 HOH   HOH B . 
H 4 HOH   89  589 131 HOH   HOH B . 
H 4 HOH   90  590 206 HOH   HOH B . 
H 4 HOH   91  591 89  HOH   HOH B . 
H 4 HOH   92  592 204 HOH   HOH B . 
H 4 HOH   93  593 79  HOH   HOH B . 
H 4 HOH   94  594 128 HOH   HOH B . 
H 4 HOH   95  595 62  HOH   HOH B . 
H 4 HOH   96  596 158 HOH   HOH B . 
H 4 HOH   97  597 168 HOH   HOH B . 
H 4 HOH   98  598 141 HOH   HOH B . 
H 4 HOH   99  599 202 HOH   HOH B . 
H 4 HOH   100 600 101 HOH   HOH B . 
H 4 HOH   101 601 198 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                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z2H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.110 
_cell.length_a_esd                 ? 
_cell.length_b                     82.110 
_cell.length_b_esd                 ? 
_cell.length_c                     64.700 
_cell.length_c_esd                 ? 
_cell.volume                       377769.609 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z2H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                143 
_symmetry.space_group_name_Hall            'P 3' 
_symmetry.space_group_name_H-M             'P 3' 
_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                   8Z2H 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.26 
_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              6.8 
_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    
'50 mM Ammonium sulfate, 0.1 M PIPES pH 6.8, 12-18% (w/v) PEG 3,350, 0.5 mM CaCl2, and 2 mM ligands' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9000 
_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 BL45XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL45XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z2H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               48 
_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                                     44206 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.108 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4092 
_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                               2.6 
_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                                  0.361 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               0.788 
_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                               20.00 
_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                                 8Z2H 
_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                            1.80 
_refine.ls_d_res_low                             47.86 
_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                     44206 
_refine.ls_number_reflns_R_free                  2271 
_refine.ls_number_reflns_R_work                  41935 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.75 
_refine.ls_percent_reflns_R_free                 5.14 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1919 
_refine.ls_R_factor_R_free                       0.1960 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1643 
_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                          2.52 
_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                 22.5509 
_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                            ? 
_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                       1.80 
_refine_hist.d_res_low                        47.86 
_refine_hist.number_atoms_solvent             199 
_refine_hist.number_atoms_total               4231 
_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        3998 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_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' ? 0.0037  ? 4142 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6590  ? 5646 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0455  ? 606  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0071  ? 742  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.8873 ? 1530 ? 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' 1.80 1.84  . . 147 2561 91.24 . . . . 0.2822 . . . . . . . . . . . 0.2688 
'X-RAY DIFFRACTION' 1.84 1.88  . . 134 2614 92.14 . . . . 0.2747 . . . . . . . . . . . 0.3189 
'X-RAY DIFFRACTION' 1.88 1.93  . . 133 2576 91.41 . . . . 0.2564 . . . . . . . . . . . 0.2884 
'X-RAY DIFFRACTION' 1.93 1.98  . . 138 2586 91.93 . . . . 0.2595 . . . . . . . . . . . 0.2856 
'X-RAY DIFFRACTION' 1.98 2.04  . . 131 2614 92.24 . . . . 0.2534 . . . . . . . . . . . 0.2799 
'X-RAY DIFFRACTION' 2.04 2.11  . . 140 2610 91.74 . . . . 0.2419 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 2.11 2.18  . . 139 2602 91.85 . . . . 0.2313 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 2.18 2.27  . . 136 2605 92.38 . . . . 0.2211 . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 2.27 2.37  . . 143 2596 92.25 . . . . 0.2147 . . . . . . . . . . . 0.2424 
'X-RAY DIFFRACTION' 2.37 2.50  . . 135 2649 93.08 . . . . 0.2005 . . . . . . . . . . . 0.2386 
'X-RAY DIFFRACTION' 2.50 2.65  . . 142 2625 93.75 . . . . 0.1960 . . . . . . . . . . . 0.2325 
'X-RAY DIFFRACTION' 2.65 2.86  . . 146 2653 93.91 . . . . 0.1780 . . . . . . . . . . . 0.1986 
'X-RAY DIFFRACTION' 2.86 3.14  . . 129 2679 94.56 . . . . 0.1659 . . . . . . . . . . . 0.2098 
'X-RAY DIFFRACTION' 3.15 3.60  . . 147 2696 94.66 . . . . 0.1591 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 3.60 4.53  . . 141 2671 94.62 . . . . 0.1519 . . . . . . . . . . . 0.2062 
'X-RAY DIFFRACTION' 4.54 47.86 . . 141 2647 93.67 . . . . 0.1551 . . . . . . . . . . . 0.1800 
# 
_struct.entry_id                     8Z2H 
_struct.title                        'Substrate analog a010 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        8Z2H 
_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 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_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 8Z2H A 3 ? 260 ? W0TJ64 47 ? 304 ? 47 304 
2 1 8Z2H 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 8Z2H GLY A 1   ? UNP W0TJ64 ?   ?   'expression tag'      45  1  
1 8Z2H PRO A 2   ? UNP W0TJ64 ?   ?   'expression tag'      46  2  
1 8Z2H HIS A 79  ? UNP W0TJ64 GLN 123 'engineered mutation' 123 3  
1 8Z2H ALA A 94  ? UNP W0TJ64 GLN 138 'engineered mutation' 138 4  
1 8Z2H ALA A 132 ? UNP W0TJ64 SER 176 'engineered mutation' 176 5  
1 8Z2H HIS A 158 ? UNP W0TJ64 ASN 202 'engineered mutation' 202 6  
1 8Z2H PRO A 182 ? UNP W0TJ64 SER 226 'engineered mutation' 226 7  
1 8Z2H SER A 184 ? UNP W0TJ64 ARG 228 'engineered mutation' 228 8  
1 8Z2H CYS A 206 ? UNP W0TJ64 ASP 250 'engineered mutation' 250 9  
1 8Z2H CYS A 252 ? UNP W0TJ64 GLU 296 'engineered mutation' 296 10 
2 8Z2H GLY B 1   ? UNP W0TJ64 ?   ?   'expression tag'      45  11 
2 8Z2H PRO B 2   ? UNP W0TJ64 ?   ?   'expression tag'      46  12 
2 8Z2H HIS B 79  ? UNP W0TJ64 GLN 123 'engineered mutation' 123 13 
2 8Z2H ALA B 94  ? UNP W0TJ64 GLN 138 'engineered mutation' 138 14 
2 8Z2H ALA B 132 ? UNP W0TJ64 SER 176 'engineered mutation' 176 15 
2 8Z2H HIS B 158 ? UNP W0TJ64 ASN 202 'engineered mutation' 202 16 
2 8Z2H PRO B 182 ? UNP W0TJ64 SER 226 'engineered mutation' 226 17 
2 8Z2H SER B 184 ? UNP W0TJ64 ARG 228 'engineered mutation' 228 18 
2 8Z2H CYS B 206 ? UNP W0TJ64 ASP 250 'engineered mutation' 250 19 
2 8Z2H 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,G 
2 1 B,E,F,H 
# 
_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  ? SER A 70  ? SER A 109 SER A 114 5 ? 6  
HELX_P HELX_P3  AA3 TRP A 71  ? SER A 78  ? TRP A 115 SER A 122 1 ? 8  
HELX_P HELX_P4  AA4 ALA A 94  ? SER A 113 ? ALA A 138 SER A 157 1 ? 20 
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  ? MET B 69  ? SER B 109 MET B 113 5 ? 5  
HELX_P HELX_P14 AB5 SER B 70  ? SER B 78  ? SER B 114 SER B 122 1 ? 9  
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 ? ? ? ? ? ? ? 2.029 ? ? 
disulf2 disulf ? ? A CYS 243 SG ? ? ? 1_555 A CYS 258 SG ? ? A CYS 287 A CYS 302 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf3 disulf ? ? B CYS 206 SG ? ? ? 1_555 B CYS 252 SG ? ? B CYS 250 B CYS 296 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf4 disulf ? ? B CYS 243 SG ? ? ? 1_555 B CYS 258 SG ? ? B CYS 287 B CYS 302 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc1 metalc ? ? A SER 32  O  ? ? ? 1_555 D CA  .   CA ? ? A SER 76  A CA  402 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc2 metalc ? ? A ALA 34  O  ? ? ? 1_555 D CA  .   CA ? ? A ALA 78  A CA  402 1_555 ? ? ? ? ? ? ? 2.454 ? ? 
metalc3 metalc ? ? A PHE 37  O  ? ? ? 1_555 D CA  .   CA ? ? A PHE 81  A CA  402 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc4 metalc ? ? B SER 32  O  ? ? ? 1_555 F CA  .   CA ? ? B SER 76  B CA  402 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc5 metalc ? ? B ALA 34  O  ? ? ? 1_555 F CA  .   CA ? ? B ALA 78  B CA  402 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc6 metalc ? ? B PHE 37  O  ? ? ? 1_555 F CA  .   CA ? ? B PHE 81  B CA  402 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
# 
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 ? D CA . ? A CA 402 ? 1_555 O ? A ALA 34 ? A ALA 78 ? 1_555 110.7 ? 
2 O ? A SER 32 ? A SER 76 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? A PHE 37 ? A PHE 81 ? 1_555 94.9  ? 
3 O ? A ALA 34 ? A ALA 78 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? A PHE 37 ? A PHE 81 ? 1_555 79.6  ? 
4 O ? B SER 32 ? B SER 76 ? 1_555 CA ? F CA . ? B CA 402 ? 1_555 O ? B ALA 34 ? B ALA 78 ? 1_555 101.9 ? 
5 O ? B SER 32 ? B SER 76 ? 1_555 CA ? F CA . ? B CA 402 ? 1_555 O ? B PHE 37 ? B PHE 81 ? 1_555 96.9  ? 
6 O ? B ALA 34 ? B ALA 78 ? 1_555 CA ? F CA . ? B CA 402 ? 1_555 O ? B PHE 37 ? B PHE 81 ? 1_555 77.2  ? 
# 
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 -3.50 
2 CYS 258 A . ? CYS 302 A PRO 259 A ? PRO 303 A 1 3.88  
3 CYS 243 B . ? CYS 287 B PRO 244 B ? PRO 288 B 1 -3.77 
4 CYS 258 B . ? CYS 302 B PRO 259 B ? PRO 303 B 1 1.74  
# 
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 VAL B 30  ? N VAL B 74  O GLY B 40  ? O GLY B 84  
AA3 2 3 N TYR B 43  ? N TYR B 87  O VAL B 83  ? O VAL B 127 
AA3 3 4 O ILE B 82  ? O ILE B 126 N VAL B 56  ? N VAL B 100 
AA3 4 5 N ALA B 57  ? N ALA B 101 O MET B 129 ? O MET B 173 
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 CYS B 252 ? O CYS B 296 
# 
_pdbx_entry_details.entry_id                   8Z2H 
_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 ALA A 176 ? ? 60.93   -114.02 
2  1 PRO A 190 ? ? -68.67  0.32    
3  1 THR A 199 ? ? 34.16   58.88   
4  1 HIS A 230 ? ? -127.14 -82.97  
5  1 ALA B 176 ? ? 62.28   -122.84 
6  1 ARG B 189 ? ? -150.89 86.66   
7  1 THR B 199 ? ? 35.25   61.64   
8  1 HIS B 230 ? ? -122.35 -77.42  
9  1 PRO B 288 ? ? -69.71  -176.88 
10 1 THR B 301 ? ? -99.84  38.75   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z     
2 -y,x-y,z  
3 -x+y,-x,z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 45 ? A GLY 1 
2 1 Y 1 A PRO 46 ? A PRO 2 
3 1 Y 1 B GLY 45 ? B GLY 1 
4 1 Y 1 B PRO 46 ? B PRO 2 
# 
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 
A1L0N CAA  C  Y N 1   
A1L0N CAB  C  Y N 2   
A1L0N CAC  C  Y N 3   
A1L0N CAD  C  Y N 4   
A1L0N CAG  C  N N 5   
A1L0N CAH  C  N N 6   
A1L0N CAL  C  Y N 7   
A1L0N CAM  C  Y N 8   
A1L0N CAN  C  N N 9   
A1L0N OAF  O  N N 10  
A1L0N OAI  O  N N 11  
A1L0N OAJ  O  N N 12  
A1L0N OAK  O  N N 13  
A1L0N OAO  O  N N 14  
A1L0N OAP  O  N N 15  
A1L0N PAE  P  N N 16  
A1L0N H1   H  N N 17  
A1L0N H2   H  N N 18  
A1L0N H3   H  N N 19  
A1L0N H4   H  N N 20  
A1L0N H5   H  N N 21  
A1L0N H6   H  N N 22  
A1L0N H7   H  N N 23  
A1L0N H8   H  N N 24  
A1L0N H9   H  N N 25  
A1L0N H10  H  N N 26  
A1L0N H11  H  N N 27  
ALA   N    N  N N 28  
ALA   CA   C  N S 29  
ALA   C    C  N N 30  
ALA   O    O  N N 31  
ALA   CB   C  N N 32  
ALA   OXT  O  N N 33  
ALA   H    H  N N 34  
ALA   H2   H  N N 35  
ALA   HA   H  N N 36  
ALA   HB1  H  N N 37  
ALA   HB2  H  N N 38  
ALA   HB3  H  N N 39  
ALA   HXT  H  N N 40  
ARG   N    N  N N 41  
ARG   CA   C  N S 42  
ARG   C    C  N N 43  
ARG   O    O  N N 44  
ARG   CB   C  N N 45  
ARG   CG   C  N N 46  
ARG   CD   C  N N 47  
ARG   NE   N  N N 48  
ARG   CZ   C  N N 49  
ARG   NH1  N  N N 50  
ARG   NH2  N  N N 51  
ARG   OXT  O  N N 52  
ARG   H    H  N N 53  
ARG   H2   H  N N 54  
ARG   HA   H  N N 55  
ARG   HB2  H  N N 56  
ARG   HB3  H  N N 57  
ARG   HG2  H  N N 58  
ARG   HG3  H  N N 59  
ARG   HD2  H  N N 60  
ARG   HD3  H  N N 61  
ARG   HE   H  N N 62  
ARG   HH11 H  N N 63  
ARG   HH12 H  N N 64  
ARG   HH21 H  N N 65  
ARG   HH22 H  N N 66  
ARG   HXT  H  N N 67  
ASN   N    N  N N 68  
ASN   CA   C  N S 69  
ASN   C    C  N N 70  
ASN   O    O  N N 71  
ASN   CB   C  N N 72  
ASN   CG   C  N N 73  
ASN   OD1  O  N N 74  
ASN   ND2  N  N N 75  
ASN   OXT  O  N N 76  
ASN   H    H  N N 77  
ASN   H2   H  N N 78  
ASN   HA   H  N N 79  
ASN   HB2  H  N N 80  
ASN   HB3  H  N N 81  
ASN   HD21 H  N N 82  
ASN   HD22 H  N N 83  
ASN   HXT  H  N N 84  
ASP   N    N  N N 85  
ASP   CA   C  N S 86  
ASP   C    C  N N 87  
ASP   O    O  N N 88  
ASP   CB   C  N N 89  
ASP   CG   C  N N 90  
ASP   OD1  O  N N 91  
ASP   OD2  O  N N 92  
ASP   OXT  O  N N 93  
ASP   H    H  N N 94  
ASP   H2   H  N N 95  
ASP   HA   H  N N 96  
ASP   HB2  H  N N 97  
ASP   HB3  H  N N 98  
ASP   HD2  H  N N 99  
ASP   HXT  H  N N 100 
CA    CA   CA N N 101 
CYS   N    N  N N 102 
CYS   CA   C  N R 103 
CYS   C    C  N N 104 
CYS   O    O  N N 105 
CYS   CB   C  N N 106 
CYS   SG   S  N N 107 
CYS   OXT  O  N N 108 
CYS   H    H  N N 109 
CYS   H2   H  N N 110 
CYS   HA   H  N N 111 
CYS   HB2  H  N N 112 
CYS   HB3  H  N N 113 
CYS   HG   H  N N 114 
CYS   HXT  H  N N 115 
GLN   N    N  N N 116 
GLN   CA   C  N S 117 
GLN   C    C  N N 118 
GLN   O    O  N N 119 
GLN   CB   C  N N 120 
GLN   CG   C  N N 121 
GLN   CD   C  N N 122 
GLN   OE1  O  N N 123 
GLN   NE2  N  N N 124 
GLN   OXT  O  N N 125 
GLN   H    H  N N 126 
GLN   H2   H  N N 127 
GLN   HA   H  N N 128 
GLN   HB2  H  N N 129 
GLN   HB3  H  N N 130 
GLN   HG2  H  N N 131 
GLN   HG3  H  N N 132 
GLN   HE21 H  N N 133 
GLN   HE22 H  N N 134 
GLN   HXT  H  N N 135 
GLU   N    N  N N 136 
GLU   CA   C  N S 137 
GLU   C    C  N N 138 
GLU   O    O  N N 139 
GLU   CB   C  N N 140 
GLU   CG   C  N N 141 
GLU   CD   C  N N 142 
GLU   OE1  O  N N 143 
GLU   OE2  O  N N 144 
GLU   OXT  O  N N 145 
GLU   H    H  N N 146 
GLU   H2   H  N N 147 
GLU   HA   H  N N 148 
GLU   HB2  H  N N 149 
GLU   HB3  H  N N 150 
GLU   HG2  H  N N 151 
GLU   HG3  H  N N 152 
GLU   HE2  H  N N 153 
GLU   HXT  H  N N 154 
GLY   N    N  N N 155 
GLY   CA   C  N N 156 
GLY   C    C  N N 157 
GLY   O    O  N N 158 
GLY   OXT  O  N N 159 
GLY   H    H  N N 160 
GLY   H2   H  N N 161 
GLY   HA2  H  N N 162 
GLY   HA3  H  N N 163 
GLY   HXT  H  N N 164 
HIS   N    N  N N 165 
HIS   CA   C  N S 166 
HIS   C    C  N N 167 
HIS   O    O  N N 168 
HIS   CB   C  N N 169 
HIS   CG   C  Y N 170 
HIS   ND1  N  Y N 171 
HIS   CD2  C  Y N 172 
HIS   CE1  C  Y N 173 
HIS   NE2  N  Y N 174 
HIS   OXT  O  N N 175 
HIS   H    H  N N 176 
HIS   H2   H  N N 177 
HIS   HA   H  N N 178 
HIS   HB2  H  N N 179 
HIS   HB3  H  N N 180 
HIS   HD1  H  N N 181 
HIS   HD2  H  N N 182 
HIS   HE1  H  N N 183 
HIS   HE2  H  N N 184 
HIS   HXT  H  N N 185 
HOH   O    O  N N 186 
HOH   H1   H  N N 187 
HOH   H2   H  N N 188 
ILE   N    N  N N 189 
ILE   CA   C  N S 190 
ILE   C    C  N N 191 
ILE   O    O  N N 192 
ILE   CB   C  N S 193 
ILE   CG1  C  N N 194 
ILE   CG2  C  N N 195 
ILE   CD1  C  N N 196 
ILE   OXT  O  N N 197 
ILE   H    H  N N 198 
ILE   H2   H  N N 199 
ILE   HA   H  N N 200 
ILE   HB   H  N N 201 
ILE   HG12 H  N N 202 
ILE   HG13 H  N N 203 
ILE   HG21 H  N N 204 
ILE   HG22 H  N N 205 
ILE   HG23 H  N N 206 
ILE   HD11 H  N N 207 
ILE   HD12 H  N N 208 
ILE   HD13 H  N N 209 
ILE   HXT  H  N N 210 
LEU   N    N  N N 211 
LEU   CA   C  N S 212 
LEU   C    C  N N 213 
LEU   O    O  N N 214 
LEU   CB   C  N N 215 
LEU   CG   C  N N 216 
LEU   CD1  C  N N 217 
LEU   CD2  C  N N 218 
LEU   OXT  O  N N 219 
LEU   H    H  N N 220 
LEU   H2   H  N N 221 
LEU   HA   H  N N 222 
LEU   HB2  H  N N 223 
LEU   HB3  H  N N 224 
LEU   HG   H  N N 225 
LEU   HD11 H  N N 226 
LEU   HD12 H  N N 227 
LEU   HD13 H  N N 228 
LEU   HD21 H  N N 229 
LEU   HD22 H  N N 230 
LEU   HD23 H  N N 231 
LEU   HXT  H  N N 232 
LYS   N    N  N N 233 
LYS   CA   C  N S 234 
LYS   C    C  N N 235 
LYS   O    O  N N 236 
LYS   CB   C  N N 237 
LYS   CG   C  N N 238 
LYS   CD   C  N N 239 
LYS   CE   C  N N 240 
LYS   NZ   N  N N 241 
LYS   OXT  O  N N 242 
LYS   H    H  N N 243 
LYS   H2   H  N N 244 
LYS   HA   H  N N 245 
LYS   HB2  H  N N 246 
LYS   HB3  H  N N 247 
LYS   HG2  H  N N 248 
LYS   HG3  H  N N 249 
LYS   HD2  H  N N 250 
LYS   HD3  H  N N 251 
LYS   HE2  H  N N 252 
LYS   HE3  H  N N 253 
LYS   HZ1  H  N N 254 
LYS   HZ2  H  N N 255 
LYS   HZ3  H  N N 256 
LYS   HXT  H  N N 257 
MET   N    N  N N 258 
MET   CA   C  N S 259 
MET   C    C  N N 260 
MET   O    O  N N 261 
MET   CB   C  N N 262 
MET   CG   C  N N 263 
MET   SD   S  N N 264 
MET   CE   C  N N 265 
MET   OXT  O  N N 266 
MET   H    H  N N 267 
MET   H2   H  N N 268 
MET   HA   H  N N 269 
MET   HB2  H  N N 270 
MET   HB3  H  N N 271 
MET   HG2  H  N N 272 
MET   HG3  H  N N 273 
MET   HE1  H  N N 274 
MET   HE2  H  N N 275 
MET   HE3  H  N N 276 
MET   HXT  H  N N 277 
PHE   N    N  N N 278 
PHE   CA   C  N S 279 
PHE   C    C  N N 280 
PHE   O    O  N N 281 
PHE   CB   C  N N 282 
PHE   CG   C  Y N 283 
PHE   CD1  C  Y N 284 
PHE   CD2  C  Y N 285 
PHE   CE1  C  Y N 286 
PHE   CE2  C  Y N 287 
PHE   CZ   C  Y N 288 
PHE   OXT  O  N N 289 
PHE   H    H  N N 290 
PHE   H2   H  N N 291 
PHE   HA   H  N N 292 
PHE   HB2  H  N N 293 
PHE   HB3  H  N N 294 
PHE   HD1  H  N N 295 
PHE   HD2  H  N N 296 
PHE   HE1  H  N N 297 
PHE   HE2  H  N N 298 
PHE   HZ   H  N N 299 
PHE   HXT  H  N N 300 
PRO   N    N  N N 301 
PRO   CA   C  N S 302 
PRO   C    C  N N 303 
PRO   O    O  N N 304 
PRO   CB   C  N N 305 
PRO   CG   C  N N 306 
PRO   CD   C  N N 307 
PRO   OXT  O  N N 308 
PRO   H    H  N N 309 
PRO   HA   H  N N 310 
PRO   HB2  H  N N 311 
PRO   HB3  H  N N 312 
PRO   HG2  H  N N 313 
PRO   HG3  H  N N 314 
PRO   HD2  H  N N 315 
PRO   HD3  H  N N 316 
PRO   HXT  H  N N 317 
SER   N    N  N N 318 
SER   CA   C  N S 319 
SER   C    C  N N 320 
SER   O    O  N N 321 
SER   CB   C  N N 322 
SER   OG   O  N N 323 
SER   OXT  O  N N 324 
SER   H    H  N N 325 
SER   H2   H  N N 326 
SER   HA   H  N N 327 
SER   HB2  H  N N 328 
SER   HB3  H  N N 329 
SER   HG   H  N N 330 
SER   HXT  H  N N 331 
THR   N    N  N N 332 
THR   CA   C  N S 333 
THR   C    C  N N 334 
THR   O    O  N N 335 
THR   CB   C  N R 336 
THR   OG1  O  N N 337 
THR   CG2  C  N N 338 
THR   OXT  O  N N 339 
THR   H    H  N N 340 
THR   H2   H  N N 341 
THR   HA   H  N N 342 
THR   HB   H  N N 343 
THR   HG1  H  N N 344 
THR   HG21 H  N N 345 
THR   HG22 H  N N 346 
THR   HG23 H  N N 347 
THR   HXT  H  N N 348 
TRP   N    N  N N 349 
TRP   CA   C  N S 350 
TRP   C    C  N N 351 
TRP   O    O  N N 352 
TRP   CB   C  N N 353 
TRP   CG   C  Y N 354 
TRP   CD1  C  Y N 355 
TRP   CD2  C  Y N 356 
TRP   NE1  N  Y N 357 
TRP   CE2  C  Y N 358 
TRP   CE3  C  Y N 359 
TRP   CZ2  C  Y N 360 
TRP   CZ3  C  Y N 361 
TRP   CH2  C  Y N 362 
TRP   OXT  O  N N 363 
TRP   H    H  N N 364 
TRP   H2   H  N N 365 
TRP   HA   H  N N 366 
TRP   HB2  H  N N 367 
TRP   HB3  H  N N 368 
TRP   HD1  H  N N 369 
TRP   HE1  H  N N 370 
TRP   HE3  H  N N 371 
TRP   HZ2  H  N N 372 
TRP   HZ3  H  N N 373 
TRP   HH2  H  N N 374 
TRP   HXT  H  N N 375 
TYR   N    N  N N 376 
TYR   CA   C  N S 377 
TYR   C    C  N N 378 
TYR   O    O  N N 379 
TYR   CB   C  N N 380 
TYR   CG   C  Y N 381 
TYR   CD1  C  Y N 382 
TYR   CD2  C  Y N 383 
TYR   CE1  C  Y N 384 
TYR   CE2  C  Y N 385 
TYR   CZ   C  Y N 386 
TYR   OH   O  N N 387 
TYR   OXT  O  N N 388 
TYR   H    H  N N 389 
TYR   H2   H  N N 390 
TYR   HA   H  N N 391 
TYR   HB2  H  N N 392 
TYR   HB3  H  N N 393 
TYR   HD1  H  N N 394 
TYR   HD2  H  N N 395 
TYR   HE1  H  N N 396 
TYR   HE2  H  N N 397 
TYR   HH   H  N N 398 
TYR   HXT  H  N N 399 
VAL   N    N  N N 400 
VAL   CA   C  N S 401 
VAL   C    C  N N 402 
VAL   O    O  N N 403 
VAL   CB   C  N N 404 
VAL   CG1  C  N N 405 
VAL   CG2  C  N N 406 
VAL   OXT  O  N N 407 
VAL   H    H  N N 408 
VAL   H2   H  N N 409 
VAL   HA   H  N N 410 
VAL   HB   H  N N 411 
VAL   HG11 H  N N 412 
VAL   HG12 H  N N 413 
VAL   HG13 H  N N 414 
VAL   HG21 H  N N 415 
VAL   HG22 H  N N 416 
VAL   HG23 H  N N 417 
VAL   HXT  H  N N 418 
# 
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 
A1L0N OAK PAE  doub N N 1   
A1L0N OAJ PAE  sing N N 2   
A1L0N PAE CAD  sing N N 3   
A1L0N PAE OAF  sing N N 4   
A1L0N CAC CAD  doub Y N 5   
A1L0N CAC CAB  sing Y N 6   
A1L0N CAD CAL  sing Y N 7   
A1L0N CAB CAA  doub Y N 8   
A1L0N CAL CAM  doub Y N 9   
A1L0N CAA CAM  sing Y N 10  
A1L0N CAA CAN  sing N N 11  
A1L0N CAG OAF  sing N N 12  
A1L0N CAG CAH  sing N N 13  
A1L0N CAN OAP  doub N N 14  
A1L0N CAN OAO  sing N N 15  
A1L0N CAH OAI  sing N N 16  
A1L0N CAB H1   sing N N 17  
A1L0N CAC H2   sing N N 18  
A1L0N CAG H3   sing N N 19  
A1L0N CAG H4   sing N N 20  
A1L0N CAH H5   sing N N 21  
A1L0N CAH H6   sing N N 22  
A1L0N CAL H7   sing N N 23  
A1L0N CAM H8   sing N N 24  
A1L0N OAI H9   sing N N 25  
A1L0N OAJ H10  sing N N 26  
A1L0N OAO H11  sing N N 27  
ALA   N   CA   sing N N 28  
ALA   N   H    sing N N 29  
ALA   N   H2   sing N N 30  
ALA   CA  C    sing N N 31  
ALA   CA  CB   sing N N 32  
ALA   CA  HA   sing N N 33  
ALA   C   O    doub N N 34  
ALA   C   OXT  sing N N 35  
ALA   CB  HB1  sing N N 36  
ALA   CB  HB2  sing N N 37  
ALA   CB  HB3  sing N N 38  
ALA   OXT HXT  sing N N 39  
ARG   N   CA   sing N N 40  
ARG   N   H    sing N N 41  
ARG   N   H2   sing N N 42  
ARG   CA  C    sing N N 43  
ARG   CA  CB   sing N N 44  
ARG   CA  HA   sing N N 45  
ARG   C   O    doub N N 46  
ARG   C   OXT  sing N N 47  
ARG   CB  CG   sing N N 48  
ARG   CB  HB2  sing N N 49  
ARG   CB  HB3  sing N N 50  
ARG   CG  CD   sing N N 51  
ARG   CG  HG2  sing N N 52  
ARG   CG  HG3  sing N N 53  
ARG   CD  NE   sing N N 54  
ARG   CD  HD2  sing N N 55  
ARG   CD  HD3  sing N N 56  
ARG   NE  CZ   sing N N 57  
ARG   NE  HE   sing N N 58  
ARG   CZ  NH1  sing N N 59  
ARG   CZ  NH2  doub N N 60  
ARG   NH1 HH11 sing N N 61  
ARG   NH1 HH12 sing N N 62  
ARG   NH2 HH21 sing N N 63  
ARG   NH2 HH22 sing N N 64  
ARG   OXT HXT  sing N N 65  
ASN   N   CA   sing N N 66  
ASN   N   H    sing N N 67  
ASN   N   H2   sing N N 68  
ASN   CA  C    sing N N 69  
ASN   CA  CB   sing N N 70  
ASN   CA  HA   sing N N 71  
ASN   C   O    doub N N 72  
ASN   C   OXT  sing N N 73  
ASN   CB  CG   sing N N 74  
ASN   CB  HB2  sing N N 75  
ASN   CB  HB3  sing N N 76  
ASN   CG  OD1  doub N N 77  
ASN   CG  ND2  sing N N 78  
ASN   ND2 HD21 sing N N 79  
ASN   ND2 HD22 sing N N 80  
ASN   OXT HXT  sing N N 81  
ASP   N   CA   sing N N 82  
ASP   N   H    sing N N 83  
ASP   N   H2   sing N N 84  
ASP   CA  C    sing N N 85  
ASP   CA  CB   sing N N 86  
ASP   CA  HA   sing N N 87  
ASP   C   O    doub N N 88  
ASP   C   OXT  sing N N 89  
ASP   CB  CG   sing N N 90  
ASP   CB  HB2  sing N N 91  
ASP   CB  HB3  sing N N 92  
ASP   CG  OD1  doub N N 93  
ASP   CG  OD2  sing N N 94  
ASP   OD2 HD2  sing N N 95  
ASP   OXT HXT  sing N N 96  
CYS   N   CA   sing N N 97  
CYS   N   H    sing N N 98  
CYS   N   H2   sing N N 99  
CYS   CA  C    sing N N 100 
CYS   CA  CB   sing N N 101 
CYS   CA  HA   sing N N 102 
CYS   C   O    doub N N 103 
CYS   C   OXT  sing N N 104 
CYS   CB  SG   sing N N 105 
CYS   CB  HB2  sing N N 106 
CYS   CB  HB3  sing N N 107 
CYS   SG  HG   sing N N 108 
CYS   OXT HXT  sing N N 109 
GLN   N   CA   sing N N 110 
GLN   N   H    sing N N 111 
GLN   N   H2   sing N N 112 
GLN   CA  C    sing N N 113 
GLN   CA  CB   sing N N 114 
GLN   CA  HA   sing N N 115 
GLN   C   O    doub N N 116 
GLN   C   OXT  sing N N 117 
GLN   CB  CG   sing N N 118 
GLN   CB  HB2  sing N N 119 
GLN   CB  HB3  sing N N 120 
GLN   CG  CD   sing N N 121 
GLN   CG  HG2  sing N N 122 
GLN   CG  HG3  sing N N 123 
GLN   CD  OE1  doub N N 124 
GLN   CD  NE2  sing N N 125 
GLN   NE2 HE21 sing N N 126 
GLN   NE2 HE22 sing N N 127 
GLN   OXT HXT  sing N N 128 
GLU   N   CA   sing N N 129 
GLU   N   H    sing N N 130 
GLU   N   H2   sing N N 131 
GLU   CA  C    sing N N 132 
GLU   CA  CB   sing N N 133 
GLU   CA  HA   sing N N 134 
GLU   C   O    doub N N 135 
GLU   C   OXT  sing N N 136 
GLU   CB  CG   sing N N 137 
GLU   CB  HB2  sing N N 138 
GLU   CB  HB3  sing N N 139 
GLU   CG  CD   sing N N 140 
GLU   CG  HG2  sing N N 141 
GLU   CG  HG3  sing N N 142 
GLU   CD  OE1  doub N N 143 
GLU   CD  OE2  sing N N 144 
GLU   OE2 HE2  sing N N 145 
GLU   OXT HXT  sing N N 146 
GLY   N   CA   sing N N 147 
GLY   N   H    sing N N 148 
GLY   N   H2   sing N N 149 
GLY   CA  C    sing N N 150 
GLY   CA  HA2  sing N N 151 
GLY   CA  HA3  sing N N 152 
GLY   C   O    doub N N 153 
GLY   C   OXT  sing N N 154 
GLY   OXT HXT  sing N N 155 
HIS   N   CA   sing N N 156 
HIS   N   H    sing N N 157 
HIS   N   H2   sing N N 158 
HIS   CA  C    sing N N 159 
HIS   CA  CB   sing N N 160 
HIS   CA  HA   sing N N 161 
HIS   C   O    doub N N 162 
HIS   C   OXT  sing N N 163 
HIS   CB  CG   sing N N 164 
HIS   CB  HB2  sing N N 165 
HIS   CB  HB3  sing N N 166 
HIS   CG  ND1  sing Y N 167 
HIS   CG  CD2  doub Y N 168 
HIS   ND1 CE1  doub Y N 169 
HIS   ND1 HD1  sing N N 170 
HIS   CD2 NE2  sing Y N 171 
HIS   CD2 HD2  sing N N 172 
HIS   CE1 NE2  sing Y N 173 
HIS   CE1 HE1  sing N N 174 
HIS   NE2 HE2  sing N N 175 
HIS   OXT HXT  sing N N 176 
HOH   O   H1   sing N N 177 
HOH   O   H2   sing N N 178 
ILE   N   CA   sing N N 179 
ILE   N   H    sing N N 180 
ILE   N   H2   sing N N 181 
ILE   CA  C    sing N N 182 
ILE   CA  CB   sing N N 183 
ILE   CA  HA   sing N N 184 
ILE   C   O    doub N N 185 
ILE   C   OXT  sing N N 186 
ILE   CB  CG1  sing N N 187 
ILE   CB  CG2  sing N N 188 
ILE   CB  HB   sing N N 189 
ILE   CG1 CD1  sing N N 190 
ILE   CG1 HG12 sing N N 191 
ILE   CG1 HG13 sing N N 192 
ILE   CG2 HG21 sing N N 193 
ILE   CG2 HG22 sing N N 194 
ILE   CG2 HG23 sing N N 195 
ILE   CD1 HD11 sing N N 196 
ILE   CD1 HD12 sing N N 197 
ILE   CD1 HD13 sing N N 198 
ILE   OXT HXT  sing N N 199 
LEU   N   CA   sing N N 200 
LEU   N   H    sing N N 201 
LEU   N   H2   sing N N 202 
LEU   CA  C    sing N N 203 
LEU   CA  CB   sing N N 204 
LEU   CA  HA   sing N N 205 
LEU   C   O    doub N N 206 
LEU   C   OXT  sing N N 207 
LEU   CB  CG   sing N N 208 
LEU   CB  HB2  sing N N 209 
LEU   CB  HB3  sing N N 210 
LEU   CG  CD1  sing N N 211 
LEU   CG  CD2  sing N N 212 
LEU   CG  HG   sing N N 213 
LEU   CD1 HD11 sing N N 214 
LEU   CD1 HD12 sing N N 215 
LEU   CD1 HD13 sing N N 216 
LEU   CD2 HD21 sing N N 217 
LEU   CD2 HD22 sing N N 218 
LEU   CD2 HD23 sing N N 219 
LEU   OXT HXT  sing N N 220 
LYS   N   CA   sing N N 221 
LYS   N   H    sing N N 222 
LYS   N   H2   sing N N 223 
LYS   CA  C    sing N N 224 
LYS   CA  CB   sing N N 225 
LYS   CA  HA   sing N N 226 
LYS   C   O    doub N N 227 
LYS   C   OXT  sing N N 228 
LYS   CB  CG   sing N N 229 
LYS   CB  HB2  sing N N 230 
LYS   CB  HB3  sing N N 231 
LYS   CG  CD   sing N N 232 
LYS   CG  HG2  sing N N 233 
LYS   CG  HG3  sing N N 234 
LYS   CD  CE   sing N N 235 
LYS   CD  HD2  sing N N 236 
LYS   CD  HD3  sing N N 237 
LYS   CE  NZ   sing N N 238 
LYS   CE  HE2  sing N N 239 
LYS   CE  HE3  sing N N 240 
LYS   NZ  HZ1  sing N N 241 
LYS   NZ  HZ2  sing N N 242 
LYS   NZ  HZ3  sing N N 243 
LYS   OXT HXT  sing N N 244 
MET   N   CA   sing N N 245 
MET   N   H    sing N N 246 
MET   N   H2   sing N N 247 
MET   CA  C    sing N N 248 
MET   CA  CB   sing N N 249 
MET   CA  HA   sing N N 250 
MET   C   O    doub N N 251 
MET   C   OXT  sing N N 252 
MET   CB  CG   sing N N 253 
MET   CB  HB2  sing N N 254 
MET   CB  HB3  sing N N 255 
MET   CG  SD   sing N N 256 
MET   CG  HG2  sing N N 257 
MET   CG  HG3  sing N N 258 
MET   SD  CE   sing N N 259 
MET   CE  HE1  sing N N 260 
MET   CE  HE2  sing N N 261 
MET   CE  HE3  sing N N 262 
MET   OXT HXT  sing N N 263 
PHE   N   CA   sing N N 264 
PHE   N   H    sing N N 265 
PHE   N   H2   sing N N 266 
PHE   CA  C    sing N N 267 
PHE   CA  CB   sing N N 268 
PHE   CA  HA   sing N N 269 
PHE   C   O    doub N N 270 
PHE   C   OXT  sing N N 271 
PHE   CB  CG   sing N N 272 
PHE   CB  HB2  sing N N 273 
PHE   CB  HB3  sing N N 274 
PHE   CG  CD1  doub Y N 275 
PHE   CG  CD2  sing Y N 276 
PHE   CD1 CE1  sing Y N 277 
PHE   CD1 HD1  sing N N 278 
PHE   CD2 CE2  doub Y N 279 
PHE   CD2 HD2  sing N N 280 
PHE   CE1 CZ   doub Y N 281 
PHE   CE1 HE1  sing N N 282 
PHE   CE2 CZ   sing Y N 283 
PHE   CE2 HE2  sing N N 284 
PHE   CZ  HZ   sing N N 285 
PHE   OXT HXT  sing N N 286 
PRO   N   CA   sing N N 287 
PRO   N   CD   sing N N 288 
PRO   N   H    sing N N 289 
PRO   CA  C    sing N N 290 
PRO   CA  CB   sing N N 291 
PRO   CA  HA   sing N N 292 
PRO   C   O    doub N N 293 
PRO   C   OXT  sing N N 294 
PRO   CB  CG   sing N N 295 
PRO   CB  HB2  sing N N 296 
PRO   CB  HB3  sing N N 297 
PRO   CG  CD   sing N N 298 
PRO   CG  HG2  sing N N 299 
PRO   CG  HG3  sing N N 300 
PRO   CD  HD2  sing N N 301 
PRO   CD  HD3  sing N N 302 
PRO   OXT HXT  sing N N 303 
SER   N   CA   sing N N 304 
SER   N   H    sing N N 305 
SER   N   H2   sing N N 306 
SER   CA  C    sing N N 307 
SER   CA  CB   sing N N 308 
SER   CA  HA   sing N N 309 
SER   C   O    doub N N 310 
SER   C   OXT  sing N N 311 
SER   CB  OG   sing N N 312 
SER   CB  HB2  sing N N 313 
SER   CB  HB3  sing N N 314 
SER   OG  HG   sing N N 315 
SER   OXT HXT  sing N N 316 
THR   N   CA   sing N N 317 
THR   N   H    sing N N 318 
THR   N   H2   sing N N 319 
THR   CA  C    sing N N 320 
THR   CA  CB   sing N N 321 
THR   CA  HA   sing N N 322 
THR   C   O    doub N N 323 
THR   C   OXT  sing N N 324 
THR   CB  OG1  sing N N 325 
THR   CB  CG2  sing N N 326 
THR   CB  HB   sing N N 327 
THR   OG1 HG1  sing N N 328 
THR   CG2 HG21 sing N N 329 
THR   CG2 HG22 sing N N 330 
THR   CG2 HG23 sing N N 331 
THR   OXT HXT  sing N N 332 
TRP   N   CA   sing N N 333 
TRP   N   H    sing N N 334 
TRP   N   H2   sing N N 335 
TRP   CA  C    sing N N 336 
TRP   CA  CB   sing N N 337 
TRP   CA  HA   sing N N 338 
TRP   C   O    doub N N 339 
TRP   C   OXT  sing N N 340 
TRP   CB  CG   sing N N 341 
TRP   CB  HB2  sing N N 342 
TRP   CB  HB3  sing N N 343 
TRP   CG  CD1  doub Y N 344 
TRP   CG  CD2  sing Y N 345 
TRP   CD1 NE1  sing Y N 346 
TRP   CD1 HD1  sing N N 347 
TRP   CD2 CE2  doub Y N 348 
TRP   CD2 CE3  sing Y N 349 
TRP   NE1 CE2  sing Y N 350 
TRP   NE1 HE1  sing N N 351 
TRP   CE2 CZ2  sing Y N 352 
TRP   CE3 CZ3  doub Y N 353 
TRP   CE3 HE3  sing N N 354 
TRP   CZ2 CH2  doub Y N 355 
TRP   CZ2 HZ2  sing N N 356 
TRP   CZ3 CH2  sing Y N 357 
TRP   CZ3 HZ3  sing N N 358 
TRP   CH2 HH2  sing N N 359 
TRP   OXT HXT  sing N N 360 
TYR   N   CA   sing N N 361 
TYR   N   H    sing N N 362 
TYR   N   H2   sing N N 363 
TYR   CA  C    sing N N 364 
TYR   CA  CB   sing N N 365 
TYR   CA  HA   sing N N 366 
TYR   C   O    doub N N 367 
TYR   C   OXT  sing N N 368 
TYR   CB  CG   sing N N 369 
TYR   CB  HB2  sing N N 370 
TYR   CB  HB3  sing N N 371 
TYR   CG  CD1  doub Y N 372 
TYR   CG  CD2  sing Y N 373 
TYR   CD1 CE1  sing Y N 374 
TYR   CD1 HD1  sing N N 375 
TYR   CD2 CE2  doub Y N 376 
TYR   CD2 HD2  sing N N 377 
TYR   CE1 CZ   doub Y N 378 
TYR   CE1 HE1  sing N N 379 
TYR   CE2 CZ   sing Y N 380 
TYR   CE2 HE2  sing N N 381 
TYR   CZ  OH   sing N N 382 
TYR   OH  HH   sing N N 383 
TYR   OXT HXT  sing N N 384 
VAL   N   CA   sing N N 385 
VAL   N   H    sing N N 386 
VAL   N   H2   sing N N 387 
VAL   CA  C    sing N N 388 
VAL   CA  CB   sing N N 389 
VAL   CA  HA   sing N N 390 
VAL   C   O    doub N N 391 
VAL   C   OXT  sing N N 392 
VAL   CB  CG1  sing N N 393 
VAL   CB  CG2  sing N N 394 
VAL   CB  HB   sing N N 395 
VAL   CG1 HG11 sing N N 396 
VAL   CG1 HG12 sing N N 397 
VAL   CG1 HG13 sing N N 398 
VAL   CG2 HG21 sing N N 399 
VAL   CG2 HG22 sing N N 400 
VAL   CG2 HG23 sing N N 401 
VAL   OXT HXT  sing N N 402 
# 
_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 3' 
_space_group.name_Hall        'P 3' 
_space_group.IT_number        143 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z2H 
_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]   0.012179 
_atom_sites.fract_transf_matrix[1][2]   0.007031 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014063 
_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]   0.015456 
_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.
;
? 
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   . ASN   A 1 3   ? 66.84000 13.01500 -20.46600 1.000 30.57000 ? 47  ASN   A N   1 
ATOM   2    C  CA  . ASN   A 1 3   ? 67.35700 14.04100 -19.56800 1.000 25.61000 ? 47  ASN   A CA  1 
ATOM   3    C  C   . ASN   A 1 3   ? 68.61600 13.54100 -18.87400 1.000 23.76000 ? 47  ASN   A C   1 
ATOM   4    O  O   . ASN   A 1 3   ? 68.54800 12.64400 -18.04000 1.000 23.75000 ? 47  ASN   A O   1 
ATOM   5    C  CB  . ASN   A 1 3   ? 66.29500 14.44100 -18.53900 1.000 24.18000 ? 47  ASN   A CB  1 
ATOM   6    C  CG  . ASN   A 1 3   ? 66.70900 15.64200 -17.70100 1.000 23.39000 ? 47  ASN   A CG  1 
ATOM   7    O  OD1 . ASN   A 1 3   ? 67.77400 16.22100 -17.90300 1.000 23.30000 ? 47  ASN   A OD1 1 
ATOM   8    N  ND2 . ASN   A 1 3   ? 65.85600 16.02600 -16.76100 1.000 22.56000 ? 47  ASN   A ND2 1 
ATOM   9    N  N   . PRO   A 1 4   ? 69.76700 14.12600 -19.22400 1.000 23.26000 ? 48  PRO   A N   1 
ATOM   10   C  CA  . PRO   A 1 4   ? 71.03600 13.67600 -18.63900 1.000 22.98000 ? 48  PRO   A CA  1 
ATOM   11   C  C   . PRO   A 1 4   ? 71.25900 14.14500 -17.21300 1.000 22.23000 ? 48  PRO   A C   1 
ATOM   12   O  O   . PRO   A 1 4   ? 72.17600 13.63900 -16.55100 1.000 21.73000 ? 48  PRO   A O   1 
ATOM   13   C  CB  . PRO   A 1 4   ? 72.07800 14.29000 -19.57800 1.000 23.13000 ? 48  PRO   A CB  1 
ATOM   14   C  CG  . PRO   A 1 4   ? 71.44300 15.55200 -20.02200 1.000 23.12000 ? 48  PRO   A CG  1 
ATOM   15   C  CD  . PRO   A 1 4   ? 69.96500 15.24800 -20.15700 1.000 22.85000 ? 48  PRO   A CD  1 
ATOM   16   N  N   . TYR   A 1 5   ? 70.45800 15.08500 -16.72500 1.000 22.28000 ? 49  TYR   A N   1 
ATOM   17   C  CA  . TYR   A 1 5   ? 70.59600 15.63200 -15.38400 1.000 22.22000 ? 49  TYR   A CA  1 
ATOM   18   C  C   . TYR   A 1 5   ? 69.75700 14.89200 -14.35100 1.000 21.75000 ? 49  TYR   A C   1 
ATOM   19   O  O   . TYR   A 1 5   ? 69.77500 15.27000 -13.17600 1.000 21.22000 ? 49  TYR   A O   1 
ATOM   20   C  CB  . TYR   A 1 5   ? 70.21900 17.11400 -15.39700 1.000 21.91000 ? 49  TYR   A CB  1 
ATOM   21   C  CG  . TYR   A 1 5   ? 70.96900 17.90500 -16.44100 1.000 21.89000 ? 49  TYR   A CG  1 
ATOM   22   C  CD1 . TYR   A 1 5   ? 72.33900 17.75100 -16.60500 1.000 21.62000 ? 49  TYR   A CD1 1 
ATOM   23   C  CD2 . TYR   A 1 5   ? 70.30500 18.79200 -17.27600 1.000 22.06000 ? 49  TYR   A CD2 1 
ATOM   24   C  CE1 . TYR   A 1 5   ? 73.03300 18.47200 -17.56400 1.000 21.38000 ? 49  TYR   A CE1 1 
ATOM   25   C  CE2 . TYR   A 1 5   ? 70.98500 19.51200 -18.23600 1.000 21.90000 ? 49  TYR   A CE2 1 
ATOM   26   C  CZ  . TYR   A 1 5   ? 72.34600 19.35000 -18.37800 1.000 21.10000 ? 49  TYR   A CZ  1 
ATOM   27   O  OH  . TYR   A 1 5   ? 73.01500 20.07600 -19.33800 1.000 19.78000 ? 49  TYR   A OH  1 
ATOM   28   N  N   . GLU   A 1 6   ? 69.02700 13.85300 -14.75300 1.000 21.94000 ? 50  GLU   A N   1 
ATOM   29   C  CA  . GLU   A 1 6   ? 68.23000 13.08500 -13.80600 1.000 21.68000 ? 50  GLU   A CA  1 
ATOM   30   C  C   . GLU   A 1 6   ? 69.13400 12.25900 -12.90000 1.000 21.31000 ? 50  GLU   A C   1 
ATOM   31   O  O   . GLU   A 1 6   ? 69.99400 11.50900 -13.37300 1.000 21.17000 ? 50  GLU   A O   1 
ATOM   32   C  CB  . GLU   A 1 6   ? 67.25100 12.17100 -14.54200 1.000 21.89000 ? 50  GLU   A CB  1 
ATOM   33   C  CG  . GLU   A 1 6   ? 66.04700 12.87200 -15.13700 1.000 22.00000 ? 50  GLU   A CG  1 
ATOM   34   C  CD  . GLU   A 1 6   ? 65.00200 11.89200 -15.63800 1.000 21.92000 ? 50  GLU   A CD  1 
ATOM   35   O  OE1 . GLU   A 1 6   ? 65.30900 10.68400 -15.70900 1.000 21.22000 ? 50  GLU   A OE1 1 
ATOM   36   O  OE2 . GLU   A 1 6   ? 63.87400 12.32400 -15.95200 1.000 21.72000 ? 50  GLU   A OE2 1 
ATOM   37   N  N   . ARG   A 1 7   ? 68.93200 12.39800 -11.59100 1.000 21.22000 ? 51  ARG   A N   1 
ATOM   38   C  CA  . ARG   A 1 7   ? 69.70300 11.68300 -10.58500 1.000 21.78000 ? 51  ARG   A CA  1 
ATOM   39   C  C   . ARG   A 1 7   ? 68.74700 10.97100 -9.64200  1.000 22.50000 ? 51  ARG   A C   1 
ATOM   40   O  O   . ARG   A 1 7   ? 67.72000 11.53100 -9.24800  1.000 22.41000 ? 51  ARG   A O   1 
ATOM   41   C  CB  . ARG   A 1 7   ? 70.60300 12.63400 -9.78800  1.000 22.10000 ? 51  ARG   A CB  1 
ATOM   42   C  CG  . ARG   A 1 7   ? 71.49100 13.52100 -10.63900 1.000 21.99000 ? 51  ARG   A CG  1 
ATOM   43   C  CD  . ARG   A 1 7   ? 72.63200 12.73400 -11.26400 1.000 22.45000 ? 51  ARG   A CD  1 
ATOM   44   N  NE  . ARG   A 1 7   ? 73.50000 13.58600 -12.07000 1.000 22.06000 ? 51  ARG   A NE  1 
ATOM   45   C  CZ  . ARG   A 1 7   ? 73.41600 13.70700 -13.38800 1.000 21.85000 ? 51  ARG   A CZ  1 
ATOM   46   N  NH1 . ARG   A 1 7   ? 72.53000 13.02000 -14.09000 1.000 22.03000 ? 51  ARG   A NH1 1 
ATOM   47   N  NH2 . ARG   A 1 7   ? 74.24100 14.53700 -14.01700 1.000 21.75000 ? 51  ARG   A NH2 1 
ATOM   48   N  N   . GLY   A 1 8   ? 69.08100 9.73400  -9.29300  1.000 23.04000 ? 52  GLY   A N   1 
ATOM   49   C  CA  . GLY   A 1 8   ? 68.32000 8.99300  -8.31900  1.000 22.97000 ? 52  GLY   A CA  1 
ATOM   50   C  C   . GLY   A 1 8   ? 67.10500 8.31600  -8.91300  1.000 22.75000 ? 52  GLY   A C   1 
ATOM   51   O  O   . GLY   A 1 8   ? 66.70500 8.58800  -10.04900 1.000 24.44000 ? 52  GLY   A O   1 
ATOM   52   N  N   . PRO   A 1 9   ? 66.49200 7.41700  -8.14800  1.000 22.79000 ? 53  PRO   A N   1 
ATOM   53   C  CA  . PRO   A 1 9   ? 65.35500 6.65000  -8.66500  1.000 22.87000 ? 53  PRO   A CA  1 
ATOM   54   C  C   . PRO   A 1 9   ? 64.09900 7.50200  -8.75100  1.000 22.93000 ? 53  PRO   A C   1 
ATOM   55   O  O   . PRO   A 1 9   ? 64.03600 8.63500  -8.26900  1.000 22.30000 ? 53  PRO   A O   1 
ATOM   56   C  CB  . PRO   A 1 9   ? 65.19800 5.52300  -7.64300  1.000 23.44000 ? 53  PRO   A CB  1 
ATOM   57   C  CG  . PRO   A 1 9   ? 65.72200 6.10000  -6.38300  1.000 24.11000 ? 53  PRO   A CG  1 
ATOM   58   C  CD  . PRO   A 1 9   ? 66.85700 7.00600  -6.78000  1.000 22.73000 ? 53  PRO   A CD  1 
ATOM   59   N  N   . ASP   A 1 10  ? 63.08100 6.92000  -9.38000  1.000 22.69000 ? 54  ASP   A N   1 
ATOM   60   C  CA  . ASP   A 1 10  ? 61.81700 7.61700  -9.56700  1.000 22.75000 ? 54  ASP   A CA  1 
ATOM   61   C  C   . ASP   A 1 10  ? 61.20800 7.95700  -8.21300  1.000 22.48000 ? 54  ASP   A C   1 
ATOM   62   O  O   . ASP   A 1 10  ? 61.13000 7.08600  -7.33600  1.000 22.59000 ? 54  ASP   A O   1 
ATOM   63   C  CB  . ASP   A 1 10  ? 60.84300 6.77000  -10.38200 1.000 23.46000 ? 54  ASP   A CB  1 
ATOM   64   C  CG  . ASP   A 1 10  ? 61.22600 6.68900  -11.84500 1.000 22.29000 ? 54  ASP   A CG  1 
ATOM   65   O  OD1 . ASP   A 1 10  ? 62.16000 7.41100  -12.25700 1.000 21.68000 ? 54  ASP   A OD1 1 
ATOM   66   O  OD2 . ASP   A 1 10  ? 60.59700 5.90200  -12.58100 1.000 22.20000 ? 54  ASP   A OD2 1 
ATOM   67   N  N   . PRO   A 1 11  ? 60.76300 9.19000  -8.00700  1.000 22.04000 ? 55  PRO   A N   1 
ATOM   68   C  CA  . PRO   A 1 11  ? 60.34400 9.61600  -6.67200  1.000 22.16000 ? 55  PRO   A CA  1 
ATOM   69   C  C   . PRO   A 1 11  ? 58.90200 9.25100  -6.36100  1.000 22.46000 ? 55  PRO   A C   1 
ATOM   70   O  O   . PRO   A 1 11  ? 58.07100 9.03100  -7.24200  1.000 22.08000 ? 55  PRO   A O   1 
ATOM   71   C  CB  . PRO   A 1 11  ? 60.51400 11.13400 -6.73500  1.000 21.91000 ? 55  PRO   A CB  1 
ATOM   72   C  CG  . PRO   A 1 11  ? 60.20500 11.45300 -8.16500  1.000 21.26000 ? 55  PRO   A CG  1 
ATOM   73   C  CD  . PRO   A 1 11  ? 60.74600 10.30100 -8.97300  1.000 21.77000 ? 55  PRO   A CD  1 
ATOM   74   N  N   . THR   A 1 12  ? 58.62800 9.18700  -5.06000  1.000 22.66000 ? 56  THR   A N   1 
ATOM   75   C  CA  . THR   A 1 12  ? 57.29400 9.04300  -4.49900  1.000 23.23000 ? 56  THR   A CA  1 
ATOM   76   C  C   . THR   A 1 12  ? 57.11900 10.11700 -3.43400  1.000 23.79000 ? 56  THR   A C   1 
ATOM   77   O  O   . THR   A 1 12  ? 58.07800 10.78200 -3.03500  1.000 23.53000 ? 56  THR   A O   1 
ATOM   78   C  CB  . THR   A 1 12  ? 57.07400 7.64300  -3.89800  1.000 23.71000 ? 56  THR   A CB  1 
ATOM   79   O  OG1 . THR   A 1 12  ? 57.96500 7.44200  -2.79300  1.000 23.49000 ? 56  THR   A OG1 1 
ATOM   80   C  CG2 . THR   A 1 12  ? 57.32700 6.56200  -4.94000  1.000 22.56000 ? 56  THR   A CG2 1 
ATOM   81   N  N   . GLU   A 1 13  ? 55.88000 10.29100 -2.97000  1.000 24.06000 ? 57  GLU   A N   1 
ATOM   82   C  CA  . GLU   A 1 13  ? 55.63100 11.28900 -1.93300  1.000 24.05000 ? 57  GLU   A CA  1 
ATOM   83   C  C   . GLU   A 1 13  ? 56.41800 10.98800 -0.66200  1.000 23.90000 ? 57  GLU   A C   1 
ATOM   84   O  O   . GLU   A 1 13  ? 56.84900 11.91800 0.03100   1.000 23.68000 ? 57  GLU   A O   1 
ATOM   85   C  CB  . GLU   A 1 13  ? 54.13500 11.38400 -1.63200  1.000 24.37000 ? 57  GLU   A CB  1 
ATOM   86   C  CG  . GLU   A 1 13  ? 53.78900 12.47400 -0.62700  1.000 24.78000 ? 57  GLU   A CG  1 
ATOM   87   C  CD  . GLU   A 1 13  ? 52.35100 12.94200 -0.73300  1.000 25.83000 ? 57  GLU   A CD  1 
ATOM   88   O  OE1 . GLU   A 1 13  ? 51.50800 12.18400 -1.25900  1.000 23.73000 ? 57  GLU   A OE1 1 
ATOM   89   O  OE2 . GLU   A 1 13  ? 52.06800 14.07900 -0.29700  1.000 23.14000 ? 57  GLU   A OE2 1 
ATOM   90   N  N   . ASP   A 1 14  ? 56.64100 9.70600  -0.35200  1.000 24.09000 ? 58  ASP   A N   1 
ATOM   91   C  CA  . ASP   A 1 14  ? 57.43600 9.34500  0.82000   1.000 24.45000 ? 58  ASP   A CA  1 
ATOM   92   C  C   . ASP   A 1 14  ? 58.92800 9.57800  0.59500   1.000 24.09000 ? 58  ASP   A C   1 
ATOM   93   O  O   . ASP   A 1 14  ? 59.64400 9.96000  1.52600   1.000 25.81000 ? 58  ASP   A O   1 
ATOM   94   C  CB  . ASP   A 1 14  ? 57.17900 7.88300  1.20200   1.000 24.91000 ? 58  ASP   A CB  1 
ATOM   95   C  CG  . ASP   A 1 14  ? 56.34100 7.73900  2.46700   1.000 25.19000 ? 58  ASP   A CG  1 
ATOM   96   O  OD1 . ASP   A 1 14  ? 55.95400 8.77300  3.05500   1.000 26.11000 ? 58  ASP   A OD1 1 
ATOM   97   O  OD2 . ASP   A 1 14  ? 56.06700 6.59100  2.87700   1.000 24.33000 ? 58  ASP   A OD2 1 
ATOM   98   N  N   . SER   A 1 15  ? 59.41700 9.35400  -0.62800  1.000 23.70000 ? 59  SER   A N   1 
ATOM   99   C  CA  . SER   A 1 15  ? 60.84600 9.49100  -0.89300  1.000 23.77000 ? 59  SER   A CA  1 
ATOM   100  C  C   . SER   A 1 15  ? 61.31300 10.94200 -0.89500  1.000 24.00000 ? 59  SER   A C   1 
ATOM   101  O  O   . SER   A 1 15  ? 62.50900 11.19000 -0.71200  1.000 23.75000 ? 59  SER   A O   1 
ATOM   102  C  CB  . SER   A 1 15  ? 61.20200 8.83700  -2.22800  1.000 22.90000 ? 59  SER   A CB  1 
ATOM   103  O  OG  . SER   A 1 15  ? 60.43800 9.40300  -3.27400  1.000 23.47000 ? 59  SER   A OG  1 
ATOM   104  N  N   . ILE   A 1 16  ? 60.41300 11.90200 -1.11500  1.000 23.99000 ? 60  ILE   A N   1 
ATOM   105  C  CA  . ILE   A 1 16  ? 60.79900 13.30200 -0.96600  1.000 23.84000 ? 60  ILE   A CA  1 
ATOM   106  C  C   . ILE   A 1 16  ? 60.68400 13.77000 0.47900   1.000 23.81000 ? 60  ILE   A C   1 
ATOM   107  O  O   . ILE   A 1 16  ? 61.28800 14.78700 0.84300   1.000 23.39000 ? 60  ILE   A O   1 
ATOM   108  C  CB  . ILE   A 1 16  ? 59.96900 14.22600 -1.87400  1.000 23.24000 ? 60  ILE   A CB  1 
ATOM   109  C  CG1 . ILE   A 1 16  ? 58.47300 13.97500 -1.68800  1.000 23.22000 ? 60  ILE   A CG1 1 
ATOM   110  C  CG2 . ILE   A 1 16  ? 60.37400 14.04800 -3.31700  1.000 23.70000 ? 60  ILE   A CG2 1 
ATOM   111  C  CD1 . ILE   A 1 16  ? 57.59600 14.94700 -2.44500  1.000 22.71000 ? 60  ILE   A CD1 1 
ATOM   112  N  N   . GLU   A 1 17  ? 59.91500 13.06200 1.30700   1.000 24.20000 ? 61  GLU   A N   1 
ATOM   113  C  CA  . GLU   A 1 17  ? 59.87400 13.33200 2.73700   1.000 24.93000 ? 61  GLU   A CA  1 
ATOM   114  C  C   . GLU   A 1 17  ? 60.99800 12.64200 3.49500   1.000 25.22000 ? 61  GLU   A C   1 
ATOM   115  O  O   . GLU   A 1 17  ? 61.20200 12.95000 4.67300   1.000 27.27000 ? 61  GLU   A O   1 
ATOM   116  C  CB  . GLU   A 1 17  ? 58.53100 12.89100 3.32200   1.000 25.33000 ? 61  GLU   A CB  1 
ATOM   117  C  CG  . GLU   A 1 17  ? 57.33300 13.60300 2.74000   1.000 23.97000 ? 61  GLU   A CG  1 
ATOM   118  C  CD  . GLU   A 1 17  ? 56.02100 13.11600 3.32600   1.000 23.37000 ? 61  GLU   A CD  1 
ATOM   119  O  OE1 . GLU   A 1 17  ? 56.03700 12.16100 4.13000   1.000 24.79000 ? 61  GLU   A OE1 1 
ATOM   120  O  OE2 . GLU   A 1 17  ? 54.96900 13.68900 2.98100   1.000 23.16000 ? 61  GLU   A OE2 1 
ATOM   121  N  N   . ALA   A 1 18  ? 61.71700 11.72000 2.85500   1.000 25.17000 ? 62  ALA   A N   1 
ATOM   122  C  CA  . ALA   A 1 18  ? 62.77100 10.97700 3.53000   1.000 25.97000 ? 62  ALA   A CA  1 
ATOM   123  C  C   . ALA   A 1 18  ? 63.83600 11.92000 4.06700   1.000 25.81000 ? 62  ALA   A C   1 
ATOM   124  O  O   . ALA   A 1 18  ? 64.34200 12.78600 3.34700   1.000 25.09000 ? 62  ALA   A O   1 
ATOM   125  C  CB  . ALA   A 1 18  ? 63.40100 9.96400  2.57500   1.000 25.59000 ? 62  ALA   A CB  1 
ATOM   126  N  N   . ILE   A 1 19  ? 64.17800 11.74500 5.34400   1.000 25.85000 ? 63  ILE   A N   1 
ATOM   127  C  CA  . ILE   A 1 19  ? 65.18900 12.58900 5.96800   1.000 26.54000 ? 63  ILE   A CA  1 
ATOM   128  C  C   . ILE   A 1 19  ? 66.52500 12.44000 5.26000   1.000 27.76000 ? 63  ILE   A C   1 
ATOM   129  O  O   . ILE   A 1 19  ? 67.30400 13.39600 5.17400   1.000 26.74000 ? 63  ILE   A O   1 
ATOM   130  C  CB  . ILE   A 1 19  ? 65.28300 12.25400 7.46900   1.000 26.96000 ? 63  ILE   A CB  1 
ATOM   131  C  CG1 . ILE   A 1 19  ? 63.94100 12.54400 8.14400   1.000 27.42000 ? 63  ILE   A CG1 1 
ATOM   132  C  CG2 . ILE   A 1 19  ? 66.40500 13.03600 8.13000   1.000 28.67000 ? 63  ILE   A CG2 1 
ATOM   133  C  CD1 . ILE   A 1 19  ? 63.90900 12.22200 9.61700   1.000 35.53000 ? 63  ILE   A CD1 1 
ATOM   134  N  N   . ARG   A 1 20  ? 66.80600 11.25700 4.72400   1.000 27.83000 ? 64  ARG   A N   1 
ATOM   135  C  CA  . ARG   A 1 20  ? 68.01600 11.00900 3.95600   1.000 27.92000 ? 64  ARG   A CA  1 
ATOM   136  C  C   . ARG   A 1 20  ? 67.63200 10.49200 2.57800   1.000 26.29000 ? 64  ARG   A C   1 
ATOM   137  O  O   . ARG   A 1 20  ? 66.88100 9.51800  2.46200   1.000 26.87000 ? 64  ARG   A O   1 
ATOM   138  C  CB  . ARG   A 1 20  ? 68.92500 10.01100 4.67700   1.000 29.95000 ? 64  ARG   A CB  1 
ATOM   139  C  CG  . ARG   A 1 20  ? 69.26900 10.43500 6.09800   1.000 33.74000 ? 64  ARG   A CG  1 
ATOM   140  C  CD  . ARG   A 1 20  ? 69.82400 9.28600  6.92400   1.000 39.23000 ? 64  ARG   A CD  1 
ATOM   141  N  NE  . ARG   A 1 20  ? 69.94500 9.65200  8.33000   1.000 43.66000 ? 64  ARG   A NE  1 
ATOM   142  C  CZ  . ARG   A 1 20  ? 70.95200 10.34900 8.83900   1.000 48.06000 ? 64  ARG   A CZ  1 
ATOM   143  N  NH1 . ARG   A 1 20  ? 71.95500 10.76700 8.08300   1.000 47.73000 ? 64  ARG   A NH1 1 
ATOM   144  N  NH2 . ARG   A 1 20  ? 70.95200 10.63600 10.13700  1.000 50.42000 ? 64  ARG   A NH2 1 
ATOM   145  N  N   . GLY   A 1 21  ? 68.13600 11.15700 1.54200   1.000 24.64000 ? 65  GLY   A N   1 
ATOM   146  C  CA  . GLY   A 1 21  ? 67.92500 10.73100 0.17900   1.000 24.04000 ? 65  GLY   A CA  1 
ATOM   147  C  C   . GLY   A 1 21  ? 68.81400 9.56300  -0.20000  1.000 24.16000 ? 65  GLY   A C   1 
ATOM   148  O  O   . GLY   A 1 21  ? 69.45000 8.93300  0.65100   1.000 23.95000 ? 65  GLY   A O   1 
ATOM   149  N  N   . PRO   A 1 22  ? 68.87400 9.24400  -1.49600  1.000 23.84000 ? 66  PRO   A N   1 
ATOM   150  C  CA  . PRO   A 1 22  ? 69.64300 8.06900  -1.92800  1.000 24.25000 ? 66  PRO   A CA  1 
ATOM   151  C  C   . PRO   A 1 22  ? 71.14800 8.27500  -1.96900  1.000 24.79000 ? 66  PRO   A C   1 
ATOM   152  O  O   . PRO   A 1 22  ? 71.87500 7.29000  -2.15400  1.000 24.52000 ? 66  PRO   A O   1 
ATOM   153  C  CB  . PRO   A 1 22  ? 69.08800 7.79300  -3.33200  1.000 23.49000 ? 66  PRO   A CB  1 
ATOM   154  C  CG  . PRO   A 1 22  ? 68.61200 9.11200  -3.80800  1.000 23.99000 ? 66  PRO   A CG  1 
ATOM   155  C  CD  . PRO   A 1 22  ? 68.09600 9.83300  -2.60000  1.000 23.66000 ? 66  PRO   A CD  1 
ATOM   156  N  N   . PHE   A 1 23  ? 71.64400 9.49900  -1.80200  1.000 24.47000 ? 67  PHE   A N   1 
ATOM   157  C  CA  . PHE   A 1 23  ? 73.07000 9.78500  -1.87900  1.000 24.32000 ? 67  PHE   A CA  1 
ATOM   158  C  C   . PHE   A 1 23  ? 73.63300 10.09000 -0.49600  1.000 23.70000 ? 67  PHE   A C   1 
ATOM   159  O  O   . PHE   A 1 23  ? 72.98200 10.75100 0.31700   1.000 23.35000 ? 67  PHE   A O   1 
ATOM   160  C  CB  . PHE   A 1 23  ? 73.35000 10.97000 -2.80900  1.000 23.88000 ? 67  PHE   A CB  1 
ATOM   161  C  CG  . PHE   A 1 23  ? 72.85600 10.77300 -4.21700  1.000 23.26000 ? 67  PHE   A CG  1 
ATOM   162  C  CD1 . PHE   A 1 23  ? 73.62300 10.09100 -5.14600  1.000 23.17000 ? 67  PHE   A CD1 1 
ATOM   163  C  CD2 . PHE   A 1 23  ? 71.62900 11.28000 -4.61400  1.000 22.86000 ? 67  PHE   A CD2 1 
ATOM   164  C  CE1 . PHE   A 1 23  ? 73.17100 9.91100  -6.44200  1.000 23.66000 ? 67  PHE   A CE1 1 
ATOM   165  C  CE2 . PHE   A 1 23  ? 71.17400 11.10200 -5.90700  1.000 22.58000 ? 67  PHE   A CE2 1 
ATOM   166  C  CZ  . PHE   A 1 23  ? 71.94800 10.41700 -6.82100  1.000 22.65000 ? 67  PHE   A CZ  1 
ATOM   167  N  N   . SER   A 1 24  ? 74.84800 9.60900  -0.23900  1.000 24.00000 ? 68  SER   A N   1 
ATOM   168  C  CA  . SER   A 1 24  ? 75.56500 9.94100  0.98100   1.000 24.46000 ? 68  SER   A CA  1 
ATOM   169  C  C   . SER   A 1 24  ? 76.25900 11.29300 0.83400   1.000 23.26000 ? 68  SER   A C   1 
ATOM   170  O  O   . SER   A 1 24  ? 76.52300 11.76600 -0.27500  1.000 22.82000 ? 68  SER   A O   1 
ATOM   171  C  CB  . SER   A 1 24  ? 76.58300 8.85600  1.31900   1.000 25.20000 ? 68  SER   A CB  1 
ATOM   172  O  OG  . SER   A 1 24  ? 77.49800 8.67300  0.25400   1.000 26.23000 ? 68  SER   A OG  1 
ATOM   173  N  N   . VAL   A 1 25  ? 76.56500 11.91500 1.97200   1.000 23.28000 ? 69  VAL   A N   1 
ATOM   174  C  CA  . VAL   A 1 25  ? 77.00600 13.30600 2.01700   1.000 22.91000 ? 69  VAL   A CA  1 
ATOM   175  C  C   . VAL   A 1 25  ? 78.39500 13.38500 2.63700   1.000 22.16000 ? 69  VAL   A C   1 
ATOM   176  O  O   . VAL   A 1 25  ? 78.64800 12.79600 3.69300   1.000 21.96000 ? 69  VAL   A O   1 
ATOM   177  C  CB  . VAL   A 1 25  ? 76.01400 14.18600 2.80200   1.000 23.43000 ? 69  VAL   A CB  1 
ATOM   178  C  CG1 . VAL   A 1 25  ? 76.40500 15.64000 2.70100   1.000 22.06000 ? 69  VAL   A CG1 1 
ATOM   179  C  CG2 . VAL   A 1 25  ? 74.60100 13.98200 2.29900   1.000 22.73000 ? 69  VAL   A CG2 1 
ATOM   180  N  N   . ALA   A 1 26  ? 79.28900 14.11100 1.97300   1.000 21.93000 ? 70  ALA   A N   1 
ATOM   181  C  CA  . ALA   A 1 26  ? 80.55800 14.55200 2.53100   1.000 21.80000 ? 70  ALA   A CA  1 
ATOM   182  C  C   . ALA   A 1 26  ? 80.54700 16.07200 2.61700   1.000 21.32000 ? 70  ALA   A C   1 
ATOM   183  O  O   . ALA   A 1 26  ? 79.76900 16.74100 1.93400   1.000 20.91000 ? 70  ALA   A O   1 
ATOM   184  C  CB  . ALA   A 1 26  ? 81.74400 14.08200 1.68400   1.000 21.85000 ? 70  ALA   A CB  1 
ATOM   185  N  N   . THR   A 1 27  ? 81.41500 16.62600 3.46000   1.000 21.38000 ? 71  THR   A N   1 
ATOM   186  C  CA  . THR   A 1 27  ? 81.42600 18.06500 3.67600   1.000 21.33000 ? 71  THR   A CA  1 
ATOM   187  C  C   . THR   A 1 27  ? 82.83100 18.63400 3.53300   1.000 21.73000 ? 71  THR   A C   1 
ATOM   188  O  O   . THR   A 1 27  ? 83.83900 17.93500 3.67800   1.000 21.62000 ? 71  THR   A O   1 
ATOM   189  C  CB  . THR   A 1 27  ? 80.86500 18.44100 5.05500   1.000 20.50000 ? 71  THR   A CB  1 
ATOM   190  O  OG1 . THR   A 1 27  ? 81.74700 17.96200 6.07700   1.000 19.57000 ? 71  THR   A OG1 1 
ATOM   191  C  CG2 . THR   A 1 27  ? 79.48900 17.83500 5.25200   1.000 20.61000 ? 71  THR   A CG2 1 
ATOM   192  N  N   . GLU   A 1 28  ? 82.87200 19.93100 3.24400   1.000 21.50000 ? 72  GLU   A N   1 
ATOM   193  C  CA  . GLU   A 1 28  ? 84.10600 20.70100 3.18700   1.000 21.84000 ? 72  GLU   A CA  1 
ATOM   194  C  C   . GLU   A 1 28  ? 83.82300 22.05300 3.82000   1.000 21.65000 ? 72  GLU   A C   1 
ATOM   195  O  O   . GLU   A 1 28  ? 82.79400 22.66500 3.52800   1.000 20.55000 ? 72  GLU   A O   1 
ATOM   196  C  CB  . GLU   A 1 28  ? 84.59400 20.86400 1.73900   1.000 22.04000 ? 72  GLU   A CB  1 
ATOM   197  C  CG  . GLU   A 1 28  ? 86.02000 21.37200 1.59400   1.000 23.02000 ? 72  GLU   A CG  1 
ATOM   198  C  CD  . GLU   A 1 28  ? 87.04900 20.27300 1.76400   1.000 24.79000 ? 72  GLU   A CD  1 
ATOM   199  O  OE1 . GLU   A 1 28  ? 86.68500 19.08600 1.59900   1.000 24.59000 ? 72  GLU   A OE1 1 
ATOM   200  O  OE2 . GLU   A 1 28  ? 88.21900 20.59600 2.06200   1.000 31.48000 ? 72  GLU   A OE2 1 
ATOM   201  N  N   . ARG   A 1 29  ? 84.71000 22.50200 4.70100   1.000 22.18000 ? 73  ARG   A N   1 
ATOM   202  C  CA  . ARG   A 1 29  ? 84.56000 23.79600 5.35100   1.000 21.42000 ? 73  ARG   A CA  1 
ATOM   203  C  C   . ARG   A 1 29  ? 85.34400 24.85000 4.58300   1.000 20.47000 ? 73  ARG   A C   1 
ATOM   204  O  O   . ARG   A 1 29  ? 86.47000 24.59900 4.15000   1.000 20.22000 ? 73  ARG   A O   1 
ATOM   205  C  CB  . ARG   A 1 29  ? 85.04600 23.73200 6.80100   1.000 21.78000 ? 73  ARG   A CB  1 
ATOM   206  C  CG  . ARG   A 1 29  ? 84.23600 22.81700 7.70400   1.000 22.85000 ? 73  ARG   A CG  1 
ATOM   207  C  CD  . ARG   A 1 29  ? 82.76700 23.19100 7.67100   1.000 25.21000 ? 73  ARG   A CD  1 
ATOM   208  N  NE  . ARG   A 1 29  ? 81.98700 22.50800 8.69600   1.000 30.20000 ? 73  ARG   A NE  1 
ATOM   209  C  CZ  . ARG   A 1 29  ? 81.50700 23.09400 9.78600   1.000 30.22000 ? 73  ARG   A CZ  1 
ATOM   210  N  NH1 . ARG   A 1 29  ? 81.71100 24.37800 10.02800  1.000 26.65000 ? 73  ARG   A NH1 1 
ATOM   211  N  NH2 . ARG   A 1 29  ? 80.80100 22.37300 10.65200  1.000 29.42000 ? 73  ARG   A NH2 1 
ATOM   212  N  N   . VAL   A 1 30  ? 84.75300 26.03600 4.43000   1.000 19.91000 ? 74  VAL   A N   1 
ATOM   213  C  CA  . VAL   A 1 30  ? 85.34800 27.11700 3.64500   1.000 19.37000 ? 74  VAL   A CA  1 
ATOM   214  C  C   . VAL   A 1 30  ? 85.58800 28.31600 4.55000   1.000 18.96000 ? 74  VAL   A C   1 
ATOM   215  O  O   . VAL   A 1 30  ? 84.64700 28.84100 5.15400   1.000 18.47000 ? 74  VAL   A O   1 
ATOM   216  C  CB  . VAL   A 1 30  ? 84.46400 27.50400 2.44700   1.000 19.14000 ? 74  VAL   A CB  1 
ATOM   217  C  CG1 . VAL   A 1 30  ? 84.94500 28.80400 1.81100   1.000 19.16000 ? 74  VAL   A CG1 1 
ATOM   218  C  CG2 . VAL   A 1 30  ? 84.44800 26.37800 1.42300   1.000 19.02000 ? 74  VAL   A CG2 1 
ATOM   219  N  N   . SER   A 1 31  ? 86.84000 28.76600 4.60900   1.000 18.43000 ? 75  SER   A N   1 
ATOM   220  C  CA  . SER   A 1 31  ? 87.23100 29.88100 5.46600   1.000 18.24000 ? 75  SER   A CA  1 
ATOM   221  C  C   . SER   A 1 31  ? 86.36100 31.10800 5.22300   1.000 18.24000 ? 75  SER   A C   1 
ATOM   222  O  O   . SER   A 1 31  ? 85.91300 31.36900 4.10400   1.000 18.27000 ? 75  SER   A O   1 
ATOM   223  C  CB  . SER   A 1 31  ? 88.70300 30.23100 5.22900   1.000 18.11000 ? 75  SER   A CB  1 
ATOM   224  O  OG  . SER   A 1 31  ? 89.02100 31.51300 5.75000   1.000 17.85000 ? 75  SER   A OG  1 
ATOM   225  N  N   . SER   A 1 32  ? 86.13300 31.87500 6.29600   1.000 18.06000 ? 76  SER   A N   1 
ATOM   226  C  CA  . SER   A 1 32  ? 85.35600 33.10300 6.19400   1.000 18.20000 ? 76  SER   A CA  1 
ATOM   227  C  C   . SER   A 1 32  ? 86.07400 34.18600 5.40800   1.000 18.58000 ? 76  SER   A C   1 
ATOM   228  O  O   . SER   A 1 32  ? 85.44600 35.18300 5.04400   1.000 18.77000 ? 76  SER   A O   1 
ATOM   229  C  CB  . SER   A 1 32  ? 85.02000 33.63600 7.58200   1.000 17.94000 ? 76  SER   A CB  1 
ATOM   230  O  OG  . SER   A 1 32  ? 86.12700 34.32500 8.13300   1.000 18.00000 ? 76  SER   A OG  1 
ATOM   231  N  N   . PHE   A 1 33  ? 87.36400 34.02500 5.14700   1.000 18.71000 ? 77  PHE   A N   1 
ATOM   232  C  CA  . PHE   A 1 33  ? 88.11700 35.00600 4.38700   1.000 18.73000 ? 77  PHE   A CA  1 
ATOM   233  C  C   . PHE   A 1 33  ? 88.08000 34.72700 2.89500   1.000 18.73000 ? 77  PHE   A C   1 
ATOM   234  O  O   . PHE   A 1 33  ? 88.88200 35.29400 2.14600   1.000 18.60000 ? 77  PHE   A O   1 
ATOM   235  C  CB  . PHE   A 1 33  ? 89.55500 35.05900 4.89200   1.000 18.45000 ? 77  PHE   A CB  1 
ATOM   236  C  CG  . PHE   A 1 33  ? 89.66900 35.52000 6.31800   1.000 18.39000 ? 77  PHE   A CG  1 
ATOM   237  C  CD1 . PHE   A 1 33  ? 89.56100 36.86400 6.63100   1.000 18.83000 ? 77  PHE   A CD1 1 
ATOM   238  C  CD2 . PHE   A 1 33  ? 89.87000 34.61100 7.34100   1.000 18.14000 ? 77  PHE   A CD2 1 
ATOM   239  C  CE1 . PHE   A 1 33  ? 89.66000 37.29400 7.93500   1.000 18.93000 ? 77  PHE   A CE1 1 
ATOM   240  C  CE2 . PHE   A 1 33  ? 89.97000 35.03500 8.64600   1.000 18.60000 ? 77  PHE   A CE2 1 
ATOM   241  C  CZ  . PHE   A 1 33  ? 89.86300 36.37800 8.94400   1.000 18.87000 ? 77  PHE   A CZ  1 
ATOM   242  N  N   . ALA   A 1 34  ? 87.18700 33.84200 2.45700   1.000 18.95000 ? 78  ALA   A N   1 
ATOM   243  C  CA  . ALA   A 1 34  ? 86.93500 33.67700 1.03500   1.000 19.18000 ? 78  ALA   A CA  1 
ATOM   244  C  C   . ALA   A 1 34  ? 86.40200 34.98200 0.45400   1.000 19.40000 ? 78  ALA   A C   1 
ATOM   245  O  O   . ALA   A 1 34  ? 85.71500 35.75500 1.12900   1.000 19.27000 ? 78  ALA   A O   1 
ATOM   246  C  CB  . ALA   A 1 34  ? 85.94600 32.53300 0.80000   1.000 19.33000 ? 78  ALA   A CB  1 
ATOM   247  N  N   . SER   A 1 35  ? 86.74100 35.24100 -0.80400  1.000 19.69000 ? 79  SER   A N   1 
ATOM   248  C  CA  . SER   A 1 35  ? 86.40900 36.52600 -1.40600  1.000 19.86000 ? 79  SER   A CA  1 
ATOM   249  C  C   . SER   A 1 35  ? 84.91300 36.63000 -1.67800  1.000 19.71000 ? 79  SER   A C   1 
ATOM   250  O  O   . SER   A 1 35  ? 84.32600 35.76000 -2.32600  1.000 19.17000 ? 79  SER   A O   1 
ATOM   251  C  CB  . SER   A 1 35  ? 87.19400 36.72400 -2.70300  1.000 20.02000 ? 79  SER   A CB  1 
ATOM   252  O  OG  . SER   A 1 35  ? 86.79000 37.91400 -3.36200  1.000 24.60000 ? 79  SER   A OG  1 
ATOM   253  N  N   . GLY   A 1 36  ? 84.29200 37.69200 -1.17300  1.000 19.61000 ? 80  GLY   A N   1 
ATOM   254  C  CA  . GLY   A 1 36  ? 82.92300 38.00000 -1.51600  1.000 19.30000 ? 80  GLY   A CA  1 
ATOM   255  C  C   . GLY   A 1 36  ? 81.86400 37.45200 -0.58600  1.000 18.96000 ? 80  GLY   A C   1 
ATOM   256  O  O   . GLY   A 1 36  ? 80.69100 37.79500 -0.75100  1.000 18.23000 ? 80  GLY   A O   1 
ATOM   257  N  N   . PHE   A 1 37  ? 82.22500 36.61300 0.37900   1.000 18.70000 ? 81  PHE   A N   1 
ATOM   258  C  CA  . PHE   A 1 37  ? 81.24600 36.11500 1.33800   1.000 18.55000 ? 81  PHE   A CA  1 
ATOM   259  C  C   . PHE   A 1 37  ? 81.97900 35.67100 2.59700   1.000 18.56000 ? 81  PHE   A C   1 
ATOM   260  O  O   . PHE   A 1 37  ? 83.20900 35.68800 2.66100   1.000 18.88000 ? 81  PHE   A O   1 
ATOM   261  C  CB  . PHE   A 1 37  ? 80.39100 34.98500 0.74200   1.000 18.06000 ? 81  PHE   A CB  1 
ATOM   262  C  CG  . PHE   A 1 37  ? 81.16300 33.74200 0.39900   1.000 18.15000 ? 81  PHE   A CG  1 
ATOM   263  C  CD1 . PHE   A 1 37  ? 82.10700 33.74400 -0.61800  1.000 18.46000 ? 81  PHE   A CD1 1 
ATOM   264  C  CD2 . PHE   A 1 37  ? 80.92200 32.56300 1.07600   1.000 18.02000 ? 81  PHE   A CD2 1 
ATOM   265  C  CE1 . PHE   A 1 37  ? 82.81000 32.59600 -0.93200  1.000 18.63000 ? 81  PHE   A CE1 1 
ATOM   266  C  CE2 . PHE   A 1 37  ? 81.61800 31.41600 0.76400   1.000 17.93000 ? 81  PHE   A CE2 1 
ATOM   267  C  CZ  . PHE   A 1 37  ? 82.56500 31.43100 -0.23800  1.000 18.45000 ? 81  PHE   A CZ  1 
ATOM   268  N  N   . GLY   A 1 38  ? 81.20400 35.28500 3.60700   1.000 18.05000 ? 82  GLY   A N   1 
ATOM   269  C  CA  . GLY   A 1 38  ? 81.78300 34.90800 4.88300   1.000 17.82000 ? 82  GLY   A CA  1 
ATOM   270  C  C   . GLY   A 1 38  ? 82.04700 33.42700 5.06900   1.000 17.65000 ? 82  GLY   A C   1 
ATOM   271  O  O   . GLY   A 1 38  ? 81.88600 32.90300 6.17300   1.000 17.24000 ? 82  GLY   A O   1 
ATOM   272  N  N   . GLY   A 1 39  ? 82.47000 32.74200 4.01400   1.000 17.96000 ? 83  GLY   A N   1 
ATOM   273  C  CA  . GLY   A 1 39  ? 82.71900 31.32100 4.11300   1.000 18.36000 ? 83  GLY   A CA  1 
ATOM   274  C  C   . GLY   A 1 39  ? 81.43500 30.51800 4.24500   1.000 18.28000 ? 83  GLY   A C   1 
ATOM   275  O  O   . GLY   A 1 39  ? 80.32300 31.02000 4.10100   1.000 17.37000 ? 83  GLY   A O   1 
ATOM   276  N  N   . GLY   A 1 40  ? 81.61500 29.23600 4.52400   1.000 18.18000 ? 84  GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 40  ? 80.48700 28.36500 4.76700   1.000 18.28000 ? 84  GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 40  ? 80.88800 26.90400 4.70500   1.000 18.87000 ? 84  GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 40  ? 82.06800 26.55600 4.71000   1.000 19.04000 ? 84  GLY   A O   1 
ATOM   280  N  N   . THR   A 1 41  ? 79.86400 26.06000 4.64500   1.000 18.62000 ? 85  THR   A N   1 
ATOM   281  C  CA  . THR   A 1 41  ? 80.01000 24.61300 4.66000   1.000 19.19000 ? 85  THR   A CA  1 
ATOM   282  C  C   . THR   A 1 41  ? 79.35300 24.04200 3.41600   1.000 18.81000 ? 85  THR   A C   1 
ATOM   283  O  O   . THR   A 1 41  ? 78.16800 24.28500 3.16800   1.000 18.11000 ? 85  THR   A O   1 
ATOM   284  C  CB  . THR   A 1 41  ? 79.37500 24.00300 5.90800   1.000 19.73000 ? 85  THR   A CB  1 
ATOM   285  O  OG1 . THR   A 1 41  ? 79.95600 24.59200 7.07500   1.000 19.91000 ? 85  THR   A OG1 1 
ATOM   286  C  CG2 . THR   A 1 41  ? 79.59600 22.50100 5.92600   1.000 20.25000 ? 85  THR   A CG2 1 
ATOM   287  N  N   . ILE   A 1 42  ? 80.11800 23.27600 2.65000   1.000 18.85000 ? 86  ILE   A N   1 
ATOM   288  C  CA  . ILE   A 1 42  ? 79.64300 22.66200 1.42000   1.000 18.83000 ? 86  ILE   A CA  1 
ATOM   289  C  C   . ILE   A 1 42  ? 79.27700 21.21900 1.71900   1.000 19.39000 ? 86  ILE   A C   1 
ATOM   290  O  O   . ILE   A 1 42  ? 80.09000 20.46400 2.26200   1.000 19.66000 ? 86  ILE   A O   1 
ATOM   291  C  CB  . ILE   A 1 42  ? 80.70600 22.73500 0.31100   1.000 18.89000 ? 86  ILE   A CB  1 
ATOM   292  C  CG1 . ILE   A 1 42  ? 81.14700 24.17700 0.06300   1.000 17.98000 ? 86  ILE   A CG1 1 
ATOM   293  C  CG2 . ILE   A 1 42  ? 80.18100 22.08700 -0.96300  1.000 19.22000 ? 86  ILE   A CG2 1 
ATOM   294  C  CD1 . ILE   A 1 42  ? 82.41200 24.28700 -0.75600  1.000 17.73000 ? 86  ILE   A CD1 1 
ATOM   295  N  N   . TYR   A 1 43  ? 78.05700 20.83900 1.37000   1.000 19.10000 ? 87  TYR   A N   1 
ATOM   296  C  CA  . TYR   A 1 43  ? 77.59800 19.46200 1.44700   1.000 19.45000 ? 87  TYR   A CA  1 
ATOM   297  C  C   . TYR   A 1 43  ? 77.44800 18.93900 0.02700   1.000 19.36000 ? 87  TYR   A C   1 
ATOM   298  O  O   . TYR   A 1 43  ? 76.77400 19.56600 -0.79400  1.000 19.03000 ? 87  TYR   A O   1 
ATOM   299  C  CB  . TYR   A 1 43  ? 76.26200 19.36000 2.18500   1.000 19.38000 ? 87  TYR   A CB  1 
ATOM   300  C  CG  . TYR   A 1 43  ? 76.23900 19.96300 3.57400   1.000 19.55000 ? 87  TYR   A CG  1 
ATOM   301  C  CD1 . TYR   A 1 43  ? 76.19200 21.33600 3.75800   1.000 19.24000 ? 87  TYR   A CD1 1 
ATOM   302  C  CD2 . TYR   A 1 43  ? 76.23300 19.15100 4.69900   1.000 19.88000 ? 87  TYR   A CD2 1 
ATOM   303  C  CE1 . TYR   A 1 43  ? 76.15500 21.88400 5.02100   1.000 19.19000 ? 87  TYR   A CE1 1 
ATOM   304  C  CE2 . TYR   A 1 43  ? 76.20000 19.69000 5.96500   1.000 20.14000 ? 87  TYR   A CE2 1 
ATOM   305  C  CZ  . TYR   A 1 43  ? 76.16000 21.05400 6.12000   1.000 19.42000 ? 87  TYR   A CZ  1 
ATOM   306  O  OH  . TYR   A 1 43  ? 76.12500 21.59700 7.37800   1.000 18.86000 ? 87  TYR   A OH  1 
ATOM   307  N  N   . TYR   A 1 44  ? 78.07200 17.80400 -0.26400  1.000 19.91000 ? 88  TYR   A N   1 
ATOM   308  C  CA  . TYR   A 1 44  ? 78.01800 17.27500 -1.61600  1.000 20.41000 ? 88  TYR   A CA  1 
ATOM   309  C  C   . TYR   A 1 44  ? 77.80400 15.77100 -1.59400  1.000 20.94000 ? 88  TYR   A C   1 
ATOM   310  O  O   . TYR   A 1 44  ? 78.22400 15.09500 -0.64900  1.000 21.30000 ? 88  TYR   A O   1 
ATOM   311  C  CB  . TYR   A 1 44  ? 79.29200 17.61200 -2.40700  1.000 20.59000 ? 88  TYR   A CB  1 
ATOM   312  C  CG  . TYR   A 1 44  ? 80.60500 17.15600 -1.80400  1.000 21.37000 ? 88  TYR   A CG  1 
ATOM   313  C  CD1 . TYR   A 1 44  ? 81.33500 17.98700 -0.96400  1.000 21.46000 ? 88  TYR   A CD1 1 
ATOM   314  C  CD2 . TYR   A 1 44  ? 81.13900 15.91600 -2.11800  1.000 22.13000 ? 88  TYR   A CD2 1 
ATOM   315  C  CE1 . TYR   A 1 44  ? 82.54300 17.58300 -0.43500  1.000 21.82000 ? 88  TYR   A CE1 1 
ATOM   316  C  CE2 . TYR   A 1 44  ? 82.34300 15.50400 -1.59700  1.000 22.51000 ? 88  TYR   A CE2 1 
ATOM   317  C  CZ  . TYR   A 1 44  ? 83.04200 16.33800 -0.75600  1.000 22.25000 ? 88  TYR   A CZ  1 
ATOM   318  O  OH  . TYR   A 1 44  ? 84.24700 15.91500 -0.23800  1.000 23.04000 ? 88  TYR   A OH  1 
ATOM   319  N  N   . PRO   A 1 45  ? 77.13400 15.22400 -2.61000  1.000 21.19000 ? 89  PRO   A N   1 
ATOM   320  C  CA  . PRO   A 1 45  ? 77.00400 13.76700 -2.70600  1.000 22.35000 ? 89  PRO   A CA  1 
ATOM   321  C  C   . PRO   A 1 45  ? 78.33500 13.12000 -3.04300  1.000 23.00000 ? 89  PRO   A C   1 
ATOM   322  O  O   . PRO   A 1 45  ? 79.13700 13.66500 -3.80400  1.000 22.81000 ? 89  PRO   A O   1 
ATOM   323  C  CB  . PRO   A 1 45  ? 75.98800 13.57000 -3.83900  1.000 22.30000 ? 89  PRO   A CB  1 
ATOM   324  C  CG  . PRO   A 1 45  ? 75.28700 14.88400 -3.96500  1.000 21.15000 ? 89  PRO   A CG  1 
ATOM   325  C  CD  . PRO   A 1 45  ? 76.32900 15.91100 -3.63100  1.000 20.58000 ? 89  PRO   A CD  1 
ATOM   326  N  N   . ARG   A 1 46  ? 78.56300 11.94200 -2.46900  1.000 23.84000 ? 90  ARG   A N   1 
ATOM   327  C  CA  . ARG   A 1 46  ? 79.82900 11.24200 -2.63700  1.000 24.96000 ? 90  ARG   A CA  1 
ATOM   328  C  C   . ARG   A 1 46  ? 79.84300 10.32400 -3.85200  1.000 25.36000 ? 90  ARG   A C   1 
ATOM   329  O  O   . ARG   A 1 46  ? 80.91300 10.08900 -4.42600  1.000 24.97000 ? 90  ARG   A O   1 
ATOM   330  C  CB  . ARG   A 1 46  ? 80.14600 10.43300 -1.37600  1.000 25.60000 ? 90  ARG   A CB  1 
ATOM   331  C  CG  . ARG   A 1 46  ? 80.16500 11.26700 -0.10300  1.000 24.52000 ? 90  ARG   A CG  1 
ATOM   332  C  CD  . ARG   A 1 46  ? 80.28700 10.40400 1.14200   1.000 25.72000 ? 90  ARG   A CD  1 
ATOM   333  N  NE  . ARG   A 1 46  ? 81.43800 9.51200  1.08600   1.000 27.54000 ? 90  ARG   A NE  1 
ATOM   334  C  CZ  . ARG   A 1 46  ? 81.35600 8.19200  0.98400   1.000 28.21000 ? 90  ARG   A CZ  1 
ATOM   335  N  NH1 . ARG   A 1 46  ? 80.18700 7.57400  0.93700   1.000 29.61000 ? 90  ARG   A NH1 1 
ATOM   336  N  NH2 . ARG   A 1 46  ? 82.47300 7.47400  0.93400   1.000 29.03000 ? 90  ARG   A NH2 1 
ATOM   337  N  N   . GLU   A 1 47  ? 78.68700 9.80500  -4.25900  1.000 25.17000 ? 91  GLU   A N   1 
ATOM   338  C  CA  . GLU   A 1 47  ? 78.60500 8.88900  -5.39100  1.000 25.87000 ? 91  GLU   A CA  1 
ATOM   339  C  C   . GLU   A 1 47  ? 78.70300 9.67400  -6.69400  1.000 26.21000 ? 91  GLU   A C   1 
ATOM   340  O  O   . GLU   A 1 47  ? 77.90300 10.58200 -6.93800  1.000 24.89000 ? 91  GLU   A O   1 
ATOM   341  C  CB  . GLU   A 1 47  ? 77.30300 8.09100  -5.34100  1.000 26.09000 ? 91  GLU   A CB  1 
ATOM   342  C  CG  . GLU   A 1 47  ? 77.16600 7.15400  -4.13900  1.000 26.89000 ? 91  GLU   A CG  1 
ATOM   343  C  CD  . GLU   A 1 47  ? 76.65600 7.84600  -2.88000  1.000 25.12000 ? 91  GLU   A CD  1 
ATOM   344  O  OE1 . GLU   A 1 47  ? 76.24700 9.02400  -2.95700  1.000 25.20000 ? 91  GLU   A OE1 1 
ATOM   345  O  OE2 . GLU   A 1 47  ? 76.66100 7.20200  -1.80900  1.000 25.25000 ? 91  GLU   A OE2 1 
ATOM   346  N  N   . THR   A 1 48  ? 79.67700 9.32100  -7.53300  1.000 26.65000 ? 92  THR   A N   1 
ATOM   347  C  CA  . THR   A 1 48  ? 79.93200 10.04100 -8.77500  1.000 26.38000 ? 92  THR   A CA  1 
ATOM   348  C  C   . THR   A 1 48  ? 79.40700 9.32700  -10.01200 1.000 27.32000 ? 92  THR   A C   1 
ATOM   349  O  O   . THR   A 1 48  ? 79.43700 9.90800  -11.10100 1.000 29.10000 ? 92  THR   A O   1 
ATOM   350  C  CB  . THR   A 1 48  ? 81.43400 10.27400 -8.95500  1.000 27.31000 ? 92  THR   A CB  1 
ATOM   351  O  OG1 . THR   A 1 48  ? 82.09300 9.01000  -9.09100  1.000 27.57000 ? 92  THR   A OG1 1 
ATOM   352  C  CG2 . THR   A 1 48  ? 82.00300 11.00200 -7.75900  1.000 25.81000 ? 92  THR   A CG2 1 
ATOM   353  N  N   . ASP   A 1 49  ? 78.92800 8.09600  -9.87500  1.000 28.28000 ? 93  ASP   A N   1 
ATOM   354  C  CA  . ASP   A 1 49  ? 78.64900 7.25600  -11.03000 1.000 28.25000 ? 93  ASP   A CA  1 
ATOM   355  C  C   . ASP   A 1 49  ? 77.34500 7.59600  -11.74300 1.000 27.41000 ? 93  ASP   A C   1 
ATOM   356  O  O   . ASP   A 1 49  ? 77.04800 6.97600  -12.76900 1.000 26.93000 ? 93  ASP   A O   1 
ATOM   357  C  CB  . ASP   A 1 49  ? 78.65000 5.78800  -10.60000 1.000 30.21000 ? 93  ASP   A CB  1 
ATOM   358  C  CG  . ASP   A 1 49  ? 80.01600 5.32800  -10.12800 1.000 32.09000 ? 93  ASP   A CG  1 
ATOM   359  O  OD1 . ASP   A 1 49  ? 80.96700 6.13900  -10.17800 1.000 29.89000 ? 93  ASP   A OD1 1 
ATOM   360  O  OD2 . ASP   A 1 49  ? 80.14200 4.15900  -9.71100  1.000 37.34000 ? 93  ASP   A OD2 1 
ATOM   361  N  N   . GLU   A 1 50  ? 76.56600 8.55600  -11.24800 1.000 26.23000 ? 94  GLU   A N   1 
ATOM   362  C  CA  . GLU   A 1 50  ? 75.36000 8.99900  -11.93700 1.000 25.14000 ? 94  GLU   A CA  1 
ATOM   363  C  C   . GLU   A 1 50  ? 75.53600 10.32900 -12.65300 1.000 24.63000 ? 94  GLU   A C   1 
ATOM   364  O  O   . GLU   A 1 50  ? 74.60600 10.77900 -13.32800 1.000 23.13000 ? 94  GLU   A O   1 
ATOM   365  C  CB  . GLU   A 1 50  ? 74.18400 9.10400  -10.95700 1.000 25.80000 ? 94  GLU   A CB  1 
ATOM   366  C  CG  . GLU   A 1 50  ? 73.63800 7.77100  -10.50300 1.000 25.89000 ? 94  GLU   A CG  1 
ATOM   367  C  CD  . GLU   A 1 50  ? 72.24300 7.87500  -9.92300  1.000 24.57000 ? 94  GLU   A CD  1 
ATOM   368  O  OE1 . GLU   A 1 50  ? 71.54500 8.87300  -10.20300 1.000 23.26000 ? 94  GLU   A OE1 1 
ATOM   369  O  OE2 . GLU   A 1 50  ? 71.84300 6.95100  -9.18600  1.000 23.38000 ? 94  GLU   A OE2 1 
ATOM   370  N  N   . GLY   A 1 51  ? 76.69000 10.96600 -12.51900 1.000 24.15000 ? 95  GLY   A N   1 
ATOM   371  C  CA  . GLY   A 1 51  ? 76.95400 12.25600 -13.12200 1.000 22.98000 ? 95  GLY   A CA  1 
ATOM   372  C  C   . GLY   A 1 51  ? 77.16100 13.34300 -12.07800 1.000 21.97000 ? 95  GLY   A C   1 
ATOM   373  O  O   . GLY   A 1 51  ? 76.97600 13.14800 -10.87600 1.000 22.08000 ? 95  GLY   A O   1 
ATOM   374  N  N   . THR   A 1 52  ? 77.56000 14.51100 -12.57200 1.000 21.54000 ? 96  THR   A N   1 
ATOM   375  C  CA  . THR   A 1 52  ? 77.76300 15.66900 -11.71900 1.000 21.73000 ? 96  THR   A CA  1 
ATOM   376  C  C   . THR   A 1 52  ? 76.42100 16.29300 -11.34300 1.000 21.40000 ? 96  THR   A C   1 
ATOM   377  O  O   . THR   A 1 52  ? 75.36900 15.94200 -11.88000 1.000 21.28000 ? 96  THR   A O   1 
ATOM   378  C  CB  . THR   A 1 52  ? 78.65000 16.69500 -12.41200 1.000 21.31000 ? 96  THR   A CB  1 
ATOM   379  O  OG1 . THR   A 1 52  ? 78.03100 17.11200 -13.63300 1.000 20.10000 ? 96  THR   A OG1 1 
ATOM   380  C  CG2 . THR   A 1 52  ? 80.00500 16.08600 -12.72300 1.000 21.23000 ? 96  THR   A CG2 1 
ATOM   381  N  N   . PHE   A 1 53  ? 76.46400 17.24000 -10.40800 1.000 21.14000 ? 97  PHE   A N   1 
ATOM   382  C  CA  . PHE   A 1 53  ? 75.25300 17.78100 -9.81300  1.000 21.03000 ? 97  PHE   A CA  1 
ATOM   383  C  C   . PHE   A 1 53  ? 75.24500 19.29900 -9.88800  1.000 20.63000 ? 97  PHE   A C   1 
ATOM   384  O  O   . PHE   A 1 53  ? 76.29600 19.94400 -9.93700  1.000 20.32000 ? 97  PHE   A O   1 
ATOM   385  C  CB  . PHE   A 1 53  ? 75.10800 17.35000 -8.35000  1.000 21.02000 ? 97  PHE   A CB  1 
ATOM   386  C  CG  . PHE   A 1 53  ? 75.19300 15.87200 -8.14100  1.000 21.55000 ? 97  PHE   A CG  1 
ATOM   387  C  CD1 . PHE   A 1 53  ? 74.06900 15.07700 -8.26000  1.000 21.64000 ? 97  PHE   A CD1 1 
ATOM   388  C  CD2 . PHE   A 1 53  ? 76.39600 15.27800 -7.80900  1.000 21.97000 ? 97  PHE   A CD2 1 
ATOM   389  C  CE1 . PHE   A 1 53  ? 74.14600 13.71400 -8.06400  1.000 22.09000 ? 97  PHE   A CE1 1 
ATOM   390  C  CE2 . PHE   A 1 53  ? 76.47800 13.91400 -7.61000  1.000 22.37000 ? 97  PHE   A CE2 1 
ATOM   391  C  CZ  . PHE   A 1 53  ? 75.35100 13.13200 -7.73800  1.000 22.55000 ? 97  PHE   A CZ  1 
ATOM   392  N  N   . GLY   A 1 54  ? 74.04000 19.86000 -9.89900  1.000 19.84000 ? 98  GLY   A N   1 
ATOM   393  C  CA  . GLY   A 1 54  ? 73.88200 21.28100 -9.69500  1.000 19.07000 ? 98  GLY   A CA  1 
ATOM   394  C  C   . GLY   A 1 54  ? 74.09100 21.65600 -8.23900  1.000 18.22000 ? 98  GLY   A C   1 
ATOM   395  O  O   . GLY   A 1 54  ? 74.23400 20.79700 -7.37000  1.000 18.38000 ? 98  GLY   A O   1 
ATOM   396  N  N   . ALA   A 1 55  ? 74.10000 22.96300 -7.97700  1.000 17.42000 ? 99  ALA   A N   1 
ATOM   397  C  CA  . ALA   A 1 55  ? 74.43400 23.47100 -6.65500  1.000 16.98000 ? 99  ALA   A CA  1 
ATOM   398  C  C   . ALA   A 1 55  ? 73.48900 24.59600 -6.26200  1.000 16.31000 ? 99  ALA   A C   1 
ATOM   399  O  O   . ALA   A 1 55  ? 73.01600 25.35600 -7.10900  1.000 16.43000 ? 99  ALA   A O   1 
ATOM   400  C  CB  . ALA   A 1 55  ? 75.88300 23.97400 -6.59400  1.000 17.16000 ? 99  ALA   A CB  1 
ATOM   401  N  N   . VAL   A 1 56  ? 73.22800 24.70600 -4.96000  1.000 15.92000 ? 100 VAL   A N   1 
ATOM   402  C  CA  . VAL   A 1 56  ? 72.41600 25.78400 -4.40800  1.000 15.73000 ? 100 VAL   A CA  1 
ATOM   403  C  C   . VAL   A 1 56  ? 73.17200 26.41000 -3.24400  1.000 15.61000 ? 100 VAL   A C   1 
ATOM   404  O  O   . VAL   A 1 56  ? 73.68200 25.69600 -2.37400  1.000 15.70000 ? 100 VAL   A O   1 
ATOM   405  C  CB  . VAL   A 1 56  ? 71.02400 25.29100 -3.95800  1.000 16.04000 ? 100 VAL   A CB  1 
ATOM   406  C  CG1 . VAL   A 1 56  ? 71.13900 24.08300 -3.04300  1.000 16.60000 ? 100 VAL   A CG1 1 
ATOM   407  C  CG2 . VAL   A 1 56  ? 70.26600 26.41300 -3.26900  1.000 15.83000 ? 100 VAL   A CG2 1 
ATOM   408  N  N   . ALA   A 1 57  ? 73.26700 27.73400 -3.24200  1.000 15.40000 ? 101 ALA   A N   1 
ATOM   409  C  CA  . ALA   A 1 57  ? 73.83500 28.45700 -2.11500  1.000 15.21000 ? 101 ALA   A CA  1 
ATOM   410  C  C   . ALA   A 1 57  ? 72.71300 28.88600 -1.18100  1.000 15.26000 ? 101 ALA   A C   1 
ATOM   411  O  O   . ALA   A 1 57  ? 71.65700 29.33800 -1.63100  1.000 15.25000 ? 101 ALA   A O   1 
ATOM   412  C  CB  . ALA   A 1 57  ? 74.63500 29.67000 -2.58900  1.000 15.34000 ? 101 ALA   A CB  1 
ATOM   413  N  N   . VAL   A 1 58  ? 72.94200 28.72900 0.12300   1.000 15.41000 ? 102 VAL   A N   1 
ATOM   414  C  CA  . VAL   A 1 58  ? 71.92100 28.95000 1.14300   1.000 15.46000 ? 102 VAL   A CA  1 
ATOM   415  C  C   . VAL   A 1 58  ? 72.37800 30.08200 2.05500   1.000 15.80000 ? 102 VAL   A C   1 
ATOM   416  O  O   . VAL   A 1 58  ? 73.38600 29.94800 2.75900   1.000 15.83000 ? 102 VAL   A O   1 
ATOM   417  C  CB  . VAL   A 1 58  ? 71.64900 27.67800 1.95800   1.000 15.69000 ? 102 VAL   A CB  1 
ATOM   418  C  CG1 . VAL   A 1 58  ? 70.51200 27.91600 2.93400   1.000 15.88000 ? 102 VAL   A CG1 1 
ATOM   419  C  CG2 . VAL   A 1 58  ? 71.33900 26.51700 1.03900   1.000 15.71000 ? 102 VAL   A CG2 1 
ATOM   420  N  N   . ALA   A 1 59  ? 71.61700 31.19300 2.06100   1.000 15.60000 ? 103 ALA   A N   1 
ATOM   421  C  CA  . ALA   A 1 59  ? 71.99900 32.33800 2.86800   1.000 16.05000 ? 103 ALA   A CA  1 
ATOM   422  C  C   . ALA   A 1 59  ? 71.13600 32.43900 4.12100   1.000 16.31000 ? 103 ALA   A C   1 
ATOM   423  O  O   . ALA   A 1 59  ? 69.99800 31.96100 4.14500   1.000 15.81000 ? 103 ALA   A O   1 
ATOM   424  C  CB  . ALA   A 1 59  ? 71.88200 33.63700 2.06600   1.000 15.95000 ? 103 ALA   A CB  1 
ATOM   425  N  N   . PRO   A 1 60  ? 71.67100 33.04900 5.18300   1.000 16.31000 ? 104 PRO   A N   1 
ATOM   426  C  CA  . PRO   A 1 60  ? 70.88300 33.23500 6.40200   1.000 16.92000 ? 104 PRO   A CA  1 
ATOM   427  C  C   . PRO   A 1 60  ? 70.25800 34.61600 6.48400   1.000 16.80000 ? 104 PRO   A C   1 
ATOM   428  O  O   . PRO   A 1 60  ? 70.44500 35.44700 5.59000   1.000 16.77000 ? 104 PRO   A O   1 
ATOM   429  C  CB  . PRO   A 1 60  ? 71.92500 33.03500 7.50100   1.000 17.26000 ? 104 PRO   A CB  1 
ATOM   430  C  CG  . PRO   A 1 60  ? 73.15500 33.64100 6.90300   1.000 17.19000 ? 104 PRO   A CG  1 
ATOM   431  C  CD  . PRO   A 1 60  ? 73.09100 33.36500 5.41100   1.000 16.97000 ? 104 PRO   A CD  1 
ATOM   432  N  N   . GLY   A 1 61  ? 69.54300 34.87600 7.57800   1.000 17.24000 ? 105 GLY   A N   1 
ATOM   433  C  CA  . GLY   A 1 61  ? 68.85700 36.13300 7.77700   1.000 17.94000 ? 105 GLY   A CA  1 
ATOM   434  C  C   . GLY   A 1 61  ? 69.69300 37.14200 8.54100   1.000 18.83000 ? 105 GLY   A C   1 
ATOM   435  O  O   . GLY   A 1 61  ? 70.88500 36.95700 8.78800   1.000 18.56000 ? 105 GLY   A O   1 
ATOM   436  N  N   . PHE   A 1 62  ? 69.03900 38.23900 8.90900   1.000 18.73000 ? 106 PHE   A N   1 
ATOM   437  C  CA  . PHE   A 1 62  ? 69.69800 39.33300 9.61200   1.000 19.25000 ? 106 PHE   A CA  1 
ATOM   438  C  C   . PHE   A 1 62  ? 70.26200 38.85800 10.94300  1.000 20.26000 ? 106 PHE   A C   1 
ATOM   439  O  O   . PHE   A 1 62  ? 69.55000 38.25800 11.74800  1.000 20.03000 ? 106 PHE   A O   1 
ATOM   440  C  CB  . PHE   A 1 62  ? 68.68900 40.45800 9.82600   1.000 19.21000 ? 106 PHE   A CB  1 
ATOM   441  C  CG  . PHE   A 1 62  ? 69.26500 41.71600 10.39800  1.000 19.59000 ? 106 PHE   A CG  1 
ATOM   442  C  CD1 . PHE   A 1 62  ? 70.30000 42.38200 9.76600   1.000 19.62000 ? 106 PHE   A CD1 1 
ATOM   443  C  CD2 . PHE   A 1 62  ? 68.72700 42.26400 11.54600  1.000 19.69000 ? 106 PHE   A CD2 1 
ATOM   444  C  CE1 . PHE   A 1 62  ? 70.80600 43.55700 10.29100  1.000 19.74000 ? 106 PHE   A CE1 1 
ATOM   445  C  CE2 . PHE   A 1 62  ? 69.22700 43.43600 12.07600  1.000 19.53000 ? 106 PHE   A CE2 1 
ATOM   446  C  CZ  . PHE   A 1 62  ? 70.26800 44.08300 11.45100  1.000 19.56000 ? 106 PHE   A CZ  1 
ATOM   447  N  N   . THR   A 1 63  ? 71.55200 39.13000 11.16200  1.000 20.21000 ? 107 THR   A N   1 
ATOM   448  C  CA  . THR   A 1 63  ? 72.30100 38.74700 12.35900  1.000 21.05000 ? 107 THR   A CA  1 
ATOM   449  C  C   . THR   A 1 63  ? 72.41600 37.23700 12.53100  1.000 20.70000 ? 107 THR   A C   1 
ATOM   450  O  O   . THR   A 1 63  ? 73.02300 36.78300 13.50500  1.000 21.06000 ? 107 THR   A O   1 
ATOM   451  C  CB  . THR   A 1 63  ? 71.68800 39.35300 13.63200  1.000 21.64000 ? 107 THR   A CB  1 
ATOM   452  O  OG1 . THR   A 1 63  ? 70.49300 38.64800 13.97400  1.000 21.08000 ? 107 THR   A OG1 1 
ATOM   453  C  CG2 . THR   A 1 63  ? 71.36500 40.82300 13.42900  1.000 21.53000 ? 107 THR   A CG2 1 
ATOM   454  N  N   . ALA   A 1 64  ? 71.89400 36.44600 11.59800  1.000 20.15000 ? 108 ALA   A N   1 
ATOM   455  C  CA  . ALA   A 1 64  ? 71.99600 35.00200 11.73900  1.000 19.82000 ? 108 ALA   A CA  1 
ATOM   456  C  C   . ALA   A 1 64  ? 73.24300 34.47900 11.03000  1.000 19.28000 ? 108 ALA   A C   1 
ATOM   457  O  O   . ALA   A 1 64  ? 73.95100 35.21300 10.33900  1.000 18.91000 ? 108 ALA   A O   1 
ATOM   458  C  CB  . ALA   A 1 64  ? 70.74400 34.31000 11.20500  1.000 18.95000 ? 108 ALA   A CB  1 
ATOM   459  N  N   . SER   A 1 65  ? 73.50500 33.18600 11.20500  1.000 18.81000 ? 109 SER   A N   1 
ATOM   460  C  CA  . SER   A 1 65  ? 74.66500 32.53500 10.61900  1.000 18.28000 ? 109 SER   A CA  1 
ATOM   461  C  C   . SER   A 1 65  ? 74.24000 31.22400 9.97100   1.000 17.99000 ? 109 SER   A C   1 
ATOM   462  O  O   . SER   A 1 65  ? 73.07100 30.83000 10.01700  1.000 17.61000 ? 109 SER   A O   1 
ATOM   463  C  CB  . SER   A 1 65  ? 75.75500 32.29900 11.67200  1.000 17.82000 ? 109 SER   A CB  1 
ATOM   464  O  OG  . SER   A 1 65  ? 75.53900 31.08900 12.37000  1.000 18.00000 ? 109 SER   A OG  1 
ATOM   465  N  N   . GLN   A 1 66  ? 75.21600 30.53500 9.37200   1.000 17.41000 ? 110 GLN   A N   1 
ATOM   466  C  CA  . GLN   A 1 66  ? 74.93100 29.27600 8.69500   1.000 17.43000 ? 110 GLN   A CA  1 
ATOM   467  C  C   . GLN   A 1 66  ? 74.33600 28.23000 9.62900   1.000 17.34000 ? 110 GLN   A C   1 
ATOM   468  O  O   . GLN   A 1 66  ? 73.71200 27.27800 9.14900   1.000 17.13000 ? 110 GLN   A O   1 
ATOM   469  C  CB  . GLN   A 1 66  ? 76.19800 28.71800 8.03700   1.000 17.39000 ? 110 GLN   A CB  1 
ATOM   470  C  CG  . GLN   A 1 66  ? 77.41800 28.66700 8.94100   1.000 17.65000 ? 110 GLN   A CG  1 
ATOM   471  C  CD  . GLN   A 1 66  ? 78.49800 27.74700 8.41500   1.000 18.11000 ? 110 GLN   A CD  1 
ATOM   472  O  OE1 . GLN   A 1 66  ? 78.22300 26.80700 7.66500   1.000 18.13000 ? 110 GLN   A OE1 1 
ATOM   473  N  NE2 . GLN   A 1 66  ? 79.73600 28.00600 8.81200   1.000 18.36000 ? 110 GLN   A NE2 1 
ATOM   474  N  N   . GLY   A 1 67  ? 74.51400 28.37500 10.94500  1.000 17.42000 ? 111 GLY   A N   1 
ATOM   475  C  CA  . GLY   A 1 67  ? 73.91800 27.42000 11.86100  1.000 17.52000 ? 111 GLY   A CA  1 
ATOM   476  C  C   . GLY   A 1 67  ? 72.40900 27.36000 11.73400  1.000 17.50000 ? 111 GLY   A C   1 
ATOM   477  O  O   . GLY   A 1 67  ? 71.81100 26.28800 11.83600  1.000 16.96000 ? 111 GLY   A O   1 
ATOM   478  N  N   . SER   A 1 68  ? 71.77500 28.50700 11.49000  1.000 17.37000 ? 112 SER   A N   1 
ATOM   479  C  CA  . SER   A 1 68  ? 70.32500 28.54600 11.35900  1.000 17.50000 ? 112 SER   A CA  1 
ATOM   480  C  C   . SER   A 1 68  ? 69.83500 27.83500 10.10600  1.000 17.06000 ? 112 SER   A C   1 
ATOM   481  O  O   . SER   A 1 68  ? 68.65200 27.48700 10.03500  1.000 17.20000 ? 112 SER   A O   1 
ATOM   482  C  CB  . SER   A 1 68  ? 69.83200 29.99000 11.36000  1.000 17.39000 ? 112 SER   A CB  1 
ATOM   483  O  OG  . SER   A 1 68  ? 70.42200 30.74000 10.31400  1.000 17.21000 ? 112 SER   A OG  1 
ATOM   484  N  N   . MET   A 1 69  ? 70.71300 27.60900 9.12700   1.000 16.97000 ? 113 MET   A N   1 
ATOM   485  C  CA  . MET   A 1 69  ? 70.36500 26.93400 7.88300   1.000 16.83000 ? 113 MET   A CA  1 
ATOM   486  C  C   . MET   A 1 69  ? 71.03700 25.57500 7.75700   1.000 17.18000 ? 113 MET   A C   1 
ATOM   487  O  O   . MET   A 1 69  ? 70.99000 24.96500 6.68400   1.000 17.35000 ? 113 MET   A O   1 
ATOM   488  C  CB  . MET   A 1 69  ? 70.73900 27.81000 6.68100   1.000 16.57000 ? 113 MET   A CB  1 
ATOM   489  C  CG  . MET   A 1 69  ? 70.22400 29.23100 6.75700   1.000 16.52000 ? 113 MET   A CG  1 
ATOM   490  S  SD  . MET   A 1 69  ? 68.43100 29.31400 6.86400   1.000 16.02000 ? 113 MET   A SD  1 
ATOM   491  C  CE  . MET   A 1 69  ? 67.97000 28.91400 5.18100   1.000 15.74000 ? 113 MET   A CE  1 
ATOM   492  N  N   . SER   A 1 70  ? 71.65100 25.08100 8.83300   1.000 17.16000 ? 114 SER   A N   1 
ATOM   493  C  CA  . SER   A 1 70  ? 72.50400 23.90400 8.73300   1.000 17.54000 ? 114 SER   A CA  1 
ATOM   494  C  C   . SER   A 1 70  ? 71.72900 22.65700 8.33000   1.000 18.20000 ? 114 SER   A C   1 
ATOM   495  O  O   . SER   A 1 70  ? 72.27900 21.79000 7.64300   1.000 18.27000 ? 114 SER   A O   1 
ATOM   496  C  CB  . SER   A 1 70  ? 73.22000 23.67000 10.06100  1.000 17.19000 ? 114 SER   A CB  1 
ATOM   497  O  OG  . SER   A 1 70  ? 72.28600 23.39300 11.09000  1.000 18.66000 ? 114 SER   A OG  1 
ATOM   498  N  N   . TRP   A 1 71  ? 70.46400 22.54100 8.73600   1.000 18.05000 ? 115 TRP   A N   1 
ATOM   499  C  CA  . TRP   A 1 71  ? 69.74300 21.29400 8.50500   1.000 18.44000 ? 115 TRP   A CA  1 
ATOM   500  C  C   . TRP   A 1 71  ? 69.43300 21.06000 7.03300   1.000 18.86000 ? 115 TRP   A C   1 
ATOM   501  O  O   . TRP   A 1 71  ? 69.18100 19.91600 6.64100   1.000 19.18000 ? 115 TRP   A O   1 
ATOM   502  C  CB  . TRP   A 1 71  ? 68.45500 21.26300 9.32900   1.000 18.78000 ? 115 TRP   A CB  1 
ATOM   503  C  CG  . TRP   A 1 71  ? 67.34900 22.12900 8.82200   1.000 19.03000 ? 115 TRP   A CG  1 
ATOM   504  C  CD1 . TRP   A 1 71  ? 67.16800 23.45300 9.07100   1.000 18.74000 ? 115 TRP   A CD1 1 
ATOM   505  C  CD2 . TRP   A 1 71  ? 66.24700 21.71700 8.00700   1.000 19.00000 ? 115 TRP   A CD2 1 
ATOM   506  N  NE1 . TRP   A 1 71  ? 66.02400 23.90100 8.45100   1.000 18.58000 ? 115 TRP   A NE1 1 
ATOM   507  C  CE2 . TRP   A 1 71  ? 65.44000 22.85200 7.79100   1.000 19.05000 ? 115 TRP   A CE2 1 
ATOM   508  C  CE3 . TRP   A 1 71  ? 65.86700 20.50100 7.43300   1.000 19.23000 ? 115 TRP   A CE3 1 
ATOM   509  C  CZ2 . TRP   A 1 71  ? 64.27800 22.80700 7.02600   1.000 18.97000 ? 115 TRP   A CZ2 1 
ATOM   510  C  CZ3 . TRP   A 1 71  ? 64.71300 20.45800 6.67400   1.000 19.43000 ? 115 TRP   A CZ3 1 
ATOM   511  C  CH2 . TRP   A 1 71  ? 63.93100 21.60500 6.47700   1.000 19.21000 ? 115 TRP   A CH2 1 
ATOM   512  N  N   . TYR   A 1 72  ? 69.45100 22.10900 6.21100   1.000 18.59000 ? 116 TYR   A N   1 
ATOM   513  C  CA  . TYR   A 1 72  ? 69.30500 21.91600 4.77600   1.000 18.91000 ? 116 TYR   A CA  1 
ATOM   514  C  C   . TYR   A 1 72  ? 70.48400 21.15100 4.19700   1.000 19.45000 ? 116 TYR   A C   1 
ATOM   515  O  O   . TYR   A 1 72  ? 70.32900 20.45200 3.19100   1.000 19.53000 ? 116 TYR   A O   1 
ATOM   516  C  CB  . TYR   A 1 72  ? 69.15900 23.26200 4.07400   1.000 18.60000 ? 116 TYR   A CB  1 
ATOM   517  C  CG  . TYR   A 1 72  ? 67.89200 23.98500 4.42600   1.000 18.45000 ? 116 TYR   A CG  1 
ATOM   518  C  CD1 . TYR   A 1 72  ? 66.67800 23.58500 3.89800   1.000 18.28000 ? 116 TYR   A CD1 1 
ATOM   519  C  CD2 . TYR   A 1 72  ? 67.90600 25.06400 5.29200   1.000 17.98000 ? 116 TYR   A CD2 1 
ATOM   520  C  CE1 . TYR   A 1 72  ? 65.51200 24.24300 4.21800   1.000 17.68000 ? 116 TYR   A CE1 1 
ATOM   521  C  CE2 . TYR   A 1 72  ? 66.74600 25.72600 5.62100   1.000 17.70000 ? 116 TYR   A CE2 1 
ATOM   522  C  CZ  . TYR   A 1 72  ? 65.55200 25.31300 5.08200   1.000 17.52000 ? 116 TYR   A CZ  1 
ATOM   523  O  OH  . TYR   A 1 72  ? 64.39300 25.97200 5.40800   1.000 17.03000 ? 116 TYR   A OH  1 
ATOM   524  N  N   . GLY   A 1 73  ? 71.65200 21.26100 4.82200   1.000 19.28000 ? 117 GLY   A N   1 
ATOM   525  C  CA  . GLY   A 1 73  ? 72.88000 20.69900 4.30100   1.000 19.74000 ? 117 GLY   A CA  1 
ATOM   526  C  C   . GLY   A 1 73  ? 72.81000 19.23400 3.93600   1.000 20.36000 ? 117 GLY   A C   1 
ATOM   527  O  O   . GLY   A 1 73  ? 72.89900 18.88600 2.75600   1.000 20.39000 ? 117 GLY   A O   1 
ATOM   528  N  N   . GLU   A 1 74  ? 72.64900 18.36100 4.93100   1.000 21.30000 ? 118 GLU   A N   1 
ATOM   529  C  CA  . GLU   A 1 74  ? 72.54900 16.93900 4.63200   1.000 22.65000 ? 118 GLU   A CA  1 
ATOM   530  C  C   . GLU   A 1 74  ? 71.20700 16.58800 4.01300   1.000 21.88000 ? 118 GLU   A C   1 
ATOM   531  O  O   . GLU   A 1 74  ? 71.13000 15.67100 3.19100   1.000 21.90000 ? 118 GLU   A O   1 
ATOM   532  C  CB  . GLU   A 1 74  ? 72.75900 16.11000 5.89700   1.000 24.48000 ? 118 GLU   A CB  1 
ATOM   533  C  CG  . GLU   A 1 74  ? 74.06100 16.38800 6.61900   1.000 29.75000 ? 118 GLU   A CG  1 
ATOM   534  C  CD  . GLU   A 1 74  ? 74.21400 15.55100 7.87300   1.000 32.80000 ? 118 GLU   A CD  1 
ATOM   535  O  OE1 . GLU   A 1 74  ? 73.21100 15.35600 8.59200   1.000 36.61000 ? 118 GLU   A OE1 1 
ATOM   536  O  OE2 . GLU   A 1 74  ? 75.33900 15.08000 8.13200   1.000 34.97000 ? 118 GLU   A OE2 1 
ATOM   537  N  N   . ARG   A 1 75  ? 70.14400 17.29200 4.40500   1.000 21.33000 ? 119 ARG   A N   1 
ATOM   538  C  CA  . ARG   A 1 75  ? 68.80400 16.94200 3.94200   1.000 21.12000 ? 119 ARG   A CA  1 
ATOM   539  C  C   . ARG   A 1 75  ? 68.70900 17.04200 2.42400   1.000 20.84000 ? 119 ARG   A C   1 
ATOM   540  O  O   . ARG   A 1 75  ? 68.29700 16.08900 1.75000   1.000 21.24000 ? 119 ARG   A O   1 
ATOM   541  C  CB  . ARG   A 1 75  ? 67.77400 17.85100 4.62100   1.000 20.63000 ? 119 ARG   A CB  1 
ATOM   542  C  CG  . ARG   A 1 75  ? 66.30900 17.52800 4.34300   1.000 21.23000 ? 119 ARG   A CG  1 
ATOM   543  C  CD  . ARG   A 1 75  ? 65.84000 16.30200 5.10800   1.000 23.24000 ? 119 ARG   A CD  1 
ATOM   544  N  NE  . ARG   A 1 75  ? 64.41200 16.05100 4.93600   1.000 23.97000 ? 119 ARG   A NE  1 
ATOM   545  C  CZ  . ARG   A 1 75  ? 63.49400 16.23900 5.87500   1.000 23.75000 ? 119 ARG   A CZ  1 
ATOM   546  N  NH1 . ARG   A 1 75  ? 63.81300 16.70500 7.07200   1.000 21.95000 ? 119 ARG   A NH1 1 
ATOM   547  N  NH2 . ARG   A 1 75  ? 62.22500 15.94300 5.61000   1.000 23.34000 ? 119 ARG   A NH2 1 
ATOM   548  N  N   . VAL   A 1 76  ? 69.12100 18.18000 1.86400   1.000 20.32000 ? 120 VAL   A N   1 
ATOM   549  C  CA  . VAL   A 1 76  ? 68.98100 18.40600 0.42900   1.000 20.25000 ? 120 VAL   A CA  1 
ATOM   550  C  C   . VAL   A 1 76  ? 70.09100 17.71400 -0.35400  1.000 20.67000 ? 120 VAL   A C   1 
ATOM   551  O  O   . VAL   A 1 76  ? 69.83700 17.11000 -1.40100  1.000 20.66000 ? 120 VAL   A O   1 
ATOM   552  C  CB  . VAL   A 1 76  ? 68.94200 19.91500 0.13400   1.000 19.84000 ? 120 VAL   A CB  1 
ATOM   553  C  CG1 . VAL   A 1 76  ? 68.82600 20.15600 -1.35700  1.000 19.17000 ? 120 VAL   A CG1 1 
ATOM   554  C  CG2 . VAL   A 1 76  ? 67.78700 20.56600 0.86700   1.000 19.59000 ? 120 VAL   A CG2 1 
ATOM   555  N  N   . ALA   A 1 77  ? 71.33400 17.79600 0.12600   1.000 20.80000 ? 121 ALA   A N   1 
ATOM   556  C  CA  . ALA   A 1 77  ? 72.44600 17.21400 -0.61500  1.000 21.30000 ? 121 ALA   A CA  1 
ATOM   557  C  C   . ALA   A 1 77  ? 72.31200 15.70400 -0.75200  1.000 21.57000 ? 121 ALA   A C   1 
ATOM   558  O  O   . ALA   A 1 77  ? 72.80400 15.13100 -1.73000  1.000 21.49000 ? 121 ALA   A O   1 
ATOM   559  C  CB  . ALA   A 1 77  ? 73.77300 17.56900 0.05200   1.000 21.01000 ? 121 ALA   A CB  1 
ATOM   560  N  N   . SER   A 1 78  ? 71.65400 15.04000 0.20400   1.000 21.90000 ? 122 SER   A N   1 
ATOM   561  C  CA  . SER   A 1 78  ? 71.44800 13.60000 0.09600   1.000 22.73000 ? 122 SER   A CA  1 
ATOM   562  C  C   . SER   A 1 78  ? 70.47200 13.23000 -1.01300  1.000 22.74000 ? 122 SER   A C   1 
ATOM   563  O  O   . SER   A 1 78  ? 70.36500 12.04800 -1.35100  1.000 23.18000 ? 122 SER   A O   1 
ATOM   564  C  CB  . SER   A 1 78  ? 70.96300 13.01800 1.42900   1.000 23.92000 ? 122 SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 78  ? 69.64300 13.42200 1.73900   1.000 23.84000 ? 122 SER   A OG  1 
ATOM   566  N  N   . HIS   A 1 79  ? 69.77000 14.20400 -1.58600  1.000 22.01000 ? 123 HIS   A N   1 
ATOM   567  C  CA  . HIS   A 1 79  ? 68.87600 13.97700 -2.71000  1.000 21.73000 ? 123 HIS   A CA  1 
ATOM   568  C  C   . HIS   A 1 79  ? 69.51400 14.33600 -4.04900  1.000 21.16000 ? 123 HIS   A C   1 
ATOM   569  O  O   . HIS   A 1 79  ? 68.82900 14.30900 -5.07500  1.000 20.41000 ? 123 HIS   A O   1 
ATOM   570  C  CB  . HIS   A 1 79  ? 67.57700 14.76200 -2.51700  1.000 21.77000 ? 123 HIS   A CB  1 
ATOM   571  C  CG  . HIS   A 1 79  ? 66.62500 14.13200 -1.54700  1.000 21.79000 ? 123 HIS   A CG  1 
ATOM   572  N  ND1 . HIS   A 1 79  ? 66.71100 14.32200 -0.18400  1.000 22.18000 ? 123 HIS   A ND1 1 
ATOM   573  C  CD2 . HIS   A 1 79  ? 65.56500 13.31300 -1.74500  1.000 22.28000 ? 123 HIS   A CD2 1 
ATOM   574  C  CE1 . HIS   A 1 79  ? 65.74600 13.64800 0.41500   1.000 23.39000 ? 123 HIS   A CE1 1 
ATOM   575  N  NE2 . HIS   A 1 79  ? 65.03700 13.02600 -0.50900  1.000 23.15000 ? 123 HIS   A NE2 1 
ATOM   576  N  N   . GLY   A 1 80  ? 70.80000 14.68000 -4.06300  1.000 21.09000 ? 124 GLY   A N   1 
ATOM   577  C  CA  . GLY   A 1 80  ? 71.50900 14.89300 -5.31100  1.000 20.84000 ? 124 GLY   A CA  1 
ATOM   578  C  C   . GLY   A 1 80  ? 71.79800 16.33800 -5.66500  1.000 20.12000 ? 124 GLY   A C   1 
ATOM   579  O  O   . GLY   A 1 80  ? 71.55600 16.76000 -6.80000  1.000 19.74000 ? 124 GLY   A O   1 
ATOM   580  N  N   . PHE   A 1 81  ? 72.32200 17.10600 -4.71000  1.000 20.10000 ? 125 PHE   A N   1 
ATOM   581  C  CA  . PHE   A 1 81  ? 72.68400 18.49700 -4.94600  1.000 19.85000 ? 125 PHE   A CA  1 
ATOM   582  C  C   . PHE   A 1 81  ? 73.89500 18.84200 -4.09500  1.000 19.36000 ? 125 PHE   A C   1 
ATOM   583  O  O   . PHE   A 1 81  ? 74.19800 18.16400 -3.11300  1.000 19.58000 ? 125 PHE   A O   1 
ATOM   584  C  CB  . PHE   A 1 81  ? 71.53000 19.45600 -4.62500  1.000 19.66000 ? 125 PHE   A CB  1 
ATOM   585  C  CG  . PHE   A 1 81  ? 70.27900 19.19900 -5.41300  1.000 19.66000 ? 125 PHE   A CG  1 
ATOM   586  C  CD1 . PHE   A 1 81  ? 70.10700 19.76500 -6.66500  1.000 19.19000 ? 125 PHE   A CD1 1 
ATOM   587  C  CD2 . PHE   A 1 81  ? 69.27000 18.40500 -4.89800  1.000 19.85000 ? 125 PHE   A CD2 1 
ATOM   588  C  CE1 . PHE   A 1 81  ? 68.95900 19.53500 -7.39000  1.000 19.18000 ? 125 PHE   A CE1 1 
ATOM   589  C  CE2 . PHE   A 1 81  ? 68.11400 18.17000 -5.62000  1.000 19.80000 ? 125 PHE   A CE2 1 
ATOM   590  C  CZ  . PHE   A 1 81  ? 67.95900 18.73700 -6.86700  1.000 19.34000 ? 125 PHE   A CZ  1 
ATOM   591  N  N   . ILE   A 1 82  ? 74.58800 19.90600 -4.48500  1.000 18.70000 ? 126 ILE   A N   1 
ATOM   592  C  CA  . ILE   A 1 82  ? 75.70200 20.45200 -3.71800  1.000 18.39000 ? 126 ILE   A CA  1 
ATOM   593  C  C   . ILE   A 1 82  ? 75.17800 21.66600 -2.96500  1.000 17.69000 ? 126 ILE   A C   1 
ATOM   594  O  O   . ILE   A 1 82  ? 74.80100 22.67100 -3.57800  1.000 17.97000 ? 126 ILE   A O   1 
ATOM   595  C  CB  . ILE   A 1 82  ? 76.88800 20.81600 -4.62100  1.000 18.51000 ? 126 ILE   A CB  1 
ATOM   596  C  CG1 . ILE   A 1 82  ? 77.60500 19.55000 -5.08800  1.000 18.94000 ? 126 ILE   A CG1 1 
ATOM   597  C  CG2 . ILE   A 1 82  ? 77.85600 21.74400 -3.90800  1.000 18.77000 ? 126 ILE   A CG2 1 
ATOM   598  C  CD1 . ILE   A 1 82  ? 78.79800 19.83100 -5.94600  1.000 20.29000 ? 126 ILE   A CD1 1 
ATOM   599  N  N   . VAL   A 1 83  ? 75.14000 21.58200 -1.63800  1.000 17.80000 ? 127 VAL   A N   1 
ATOM   600  C  CA  . VAL   A 1 83  ? 74.53400 22.61200 -0.79900  1.000 17.55000 ? 127 VAL   A CA  1 
ATOM   601  C  C   . VAL   A 1 83  ? 75.63700 23.41000 -0.12500  1.000 17.50000 ? 127 VAL   A C   1 
ATOM   602  O  O   . VAL   A 1 83  ? 76.52700 22.83600 0.51200   1.000 17.74000 ? 127 VAL   A O   1 
ATOM   603  C  CB  . VAL   A 1 83  ? 73.58300 22.00900 0.24800   1.000 18.28000 ? 127 VAL   A CB  1 
ATOM   604  C  CG1 . VAL   A 1 83  ? 72.94000 23.12200 1.06600   1.000 17.98000 ? 127 VAL   A CG1 1 
ATOM   605  C  CG2 . VAL   A 1 83  ? 72.52600 21.13800 -0.41900  1.000 18.98000 ? 127 VAL   A CG2 1 
ATOM   606  N  N   . PHE   A 1 84  ? 75.57000 24.73000 -0.25500  1.000 16.85000 ? 128 PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 84  ? 76.56200 25.64200 0.30300   1.000 16.67000 ? 128 PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 84  ? 75.84000 26.55800 1.28900   1.000 16.46000 ? 128 PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 84  ? 75.24800 27.56600 0.89200   1.000 16.14000 ? 128 PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 84  ? 77.25000 26.43700 -0.80500  1.000 16.35000 ? 128 PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 84  ? 78.58300 27.02000 -0.41200  1.000 16.69000 ? 128 PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 84  ? 79.09300 26.83600 0.86100   1.000 17.05000 ? 128 PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 84  ? 79.32800 27.75600 -1.32300  1.000 16.65000 ? 128 PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 84  ? 80.31700 27.36800 1.22000   1.000 17.47000 ? 128 PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 84  ? 80.55100 28.29500 -0.96800  1.000 17.21000 ? 128 PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 84  ? 81.04800 28.09600 0.30400   1.000 17.41000 ? 128 PHE   A CZ  1 
ATOM   617  N  N   . THR   A 1 85  ? 75.87100 26.19900 2.56900   1.000 16.85000 ? 129 THR   A N   1 
ATOM   618  C  CA  . THR   A 1 85  ? 75.36900 27.07300 3.62200   1.000 16.62000 ? 129 THR   A CA  1 
ATOM   619  C  C   . THR   A 1 85  ? 76.45100 28.08700 3.96000   1.000 17.51000 ? 129 THR   A C   1 
ATOM   620  O  O   . THR   A 1 85  ? 77.55300 27.70400 4.35800   1.000 16.95000 ? 129 THR   A O   1 
ATOM   621  C  CB  . THR   A 1 85  ? 74.98500 26.25500 4.85100   1.000 17.37000 ? 129 THR   A CB  1 
ATOM   622  O  OG1 . THR   A 1 85  ? 76.11700 25.48800 5.27700   1.000 17.56000 ? 129 THR   A OG1 1 
ATOM   623  C  CG2 . THR   A 1 85  ? 73.86200 25.30300 4.51900   1.000 17.19000 ? 129 THR   A CG2 1 
ATOM   624  N  N   . ILE   A 1 86  ? 76.15600 29.37500 3.78800   1.000 16.65000 ? 130 ILE   A N   1 
ATOM   625  C  CA  . ILE   A 1 86  ? 77.18300 30.40300 3.87700   1.000 16.84000 ? 130 ILE   A CA  1 
ATOM   626  C  C   . ILE   A 1 86  ? 76.88700 31.34700 5.03500   1.000 16.86000 ? 130 ILE   A C   1 
ATOM   627  O  O   . ILE   A 1 86  ? 75.75100 31.48100 5.49000   1.000 16.62000 ? 130 ILE   A O   1 
ATOM   628  C  CB  . ILE   A 1 86  ? 77.32000 31.20700 2.56600   1.000 16.62000 ? 130 ILE   A CB  1 
ATOM   629  C  CG1 . ILE   A 1 86  ? 76.07300 32.06200 2.33200   1.000 16.24000 ? 130 ILE   A CG1 1 
ATOM   630  C  CG2 . ILE   A 1 86  ? 77.54000 30.27400 1.39700   1.000 16.52000 ? 130 ILE   A CG2 1 
ATOM   631  C  CD1 . ILE   A 1 86  ? 76.29400 33.23400 1.39600   1.000 16.18000 ? 130 ILE   A CD1 1 
ATOM   632  N  N   . ASP   A 1 87  ? 77.94600 32.00000 5.50500   1.000 16.93000 ? 131 ASP   A N   1 
ATOM   633  C  CA  . ASP   A 1 87  ? 77.87600 33.15200 6.39100   1.000 16.75000 ? 131 ASP   A CA  1 
ATOM   634  C  C   . ASP   A 1 87  ? 78.01700 34.42400 5.56400   1.000 16.87000 ? 131 ASP   A C   1 
ATOM   635  O  O   . ASP   A 1 87  ? 78.66500 34.43000 4.51600   1.000 17.08000 ? 131 ASP   A O   1 
ATOM   636  C  CB  . ASP   A 1 87  ? 78.98600 33.11300 7.44900   1.000 16.52000 ? 131 ASP   A CB  1 
ATOM   637  C  CG  . ASP   A 1 87  ? 78.71500 32.11800 8.56600   1.000 16.32000 ? 131 ASP   A CG  1 
ATOM   638  O  OD1 . ASP   A 1 87  ? 77.60100 32.12300 9.12600   1.000 16.66000 ? 131 ASP   A OD1 1 
ATOM   639  O  OD2 . ASP   A 1 87  ? 79.63000 31.33300 8.89300   1.000 16.23000 ? 131 ASP   A OD2 1 
ATOM   640  N  N   . THR   A 1 88  ? 77.41700 35.50400 6.04100   1.000 17.07000 ? 132 THR   A N   1 
ATOM   641  C  CA  . THR   A 1 88  ? 77.55500 36.77300 5.34800   1.000 17.43000 ? 132 THR   A CA  1 
ATOM   642  C  C   . THR   A 1 88  ? 78.82500 37.49200 5.79200   1.000 17.82000 ? 132 THR   A C   1 
ATOM   643  O  O   . THR   A 1 88  ? 79.48600 37.10200 6.75400   1.000 17.65000 ? 132 THR   A O   1 
ATOM   644  C  CB  . THR   A 1 88  ? 76.33100 37.65700 5.58100   1.000 17.58000 ? 132 THR   A CB  1 
ATOM   645  O  OG1 . THR   A 1 88  ? 76.07700 37.77200 6.98600   1.000 17.88000 ? 132 THR   A OG1 1 
ATOM   646  C  CG2 . THR   A 1 88  ? 75.12000 37.06000 4.90000   1.000 17.14000 ? 132 THR   A CG2 1 
ATOM   647  N  N   . ASN   A 1 89  ? 79.16500 38.55800 5.06400   1.000 17.91000 ? 133 ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 89  ? 80.36100 39.33200 5.38900   1.000 18.15000 ? 133 ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 89  ? 80.27300 39.91400 6.79200   1.000 18.38000 ? 133 ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 89  ? 81.21600 39.80400 7.58200   1.000 18.16000 ? 133 ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 89  ? 80.56300 40.44800 4.36700   1.000 18.03000 ? 133 ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 89  ? 81.18700 39.95900 3.08300   1.000 18.02000 ? 133 ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 89  ? 81.83100 38.91400 3.05000   1.000 18.29000 ? 133 ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 89  ? 81.00900 40.72400 2.01600   1.000 17.47000 ? 133 ASN   A ND2 1 
ATOM   655  N  N   . THR   A 1 90  ? 79.16200 40.57500 7.10200   1.000 18.61000 ? 134 THR   A N   1 
ATOM   656  C  CA  . THR   A 1 90  ? 78.83700 40.98300 8.45800   1.000 19.13000 ? 134 THR   A CA  1 
ATOM   657  C  C   . THR   A 1 90  ? 77.42000 40.52600 8.76400   1.000 19.20000 ? 134 THR   A C   1 
ATOM   658  O  O   . THR   A 1 90  ? 76.61300 40.29400 7.86100   1.000 18.90000 ? 134 THR   A O   1 
ATOM   659  C  CB  . THR   A 1 90  ? 78.94700 42.50200 8.66200   1.000 19.66000 ? 134 THR   A CB  1 
ATOM   660  O  OG1 . THR   A 1 90  ? 77.79400 43.14500 8.11200   1.000 19.19000 ? 134 THR   A OG1 1 
ATOM   661  C  CG2 . THR   A 1 90  ? 80.19600 43.05600 7.99500   1.000 19.32000 ? 134 THR   A CG2 1 
ATOM   662  N  N   . ARG   A 1 91  ? 77.11900 40.40100 10.05500  1.000 19.77000 ? 135 ARG   A N   1 
ATOM   663  C  CA  . ARG   A 1 91  ? 75.78800 39.98000 10.47100  1.000 20.65000 ? 135 ARG   A CA  1 
ATOM   664  C  C   . ARG   A 1 91  ? 74.71700 41.01600 10.16200  1.000 20.78000 ? 135 ARG   A C   1 
ATOM   665  O  O   . ARG   A 1 91  ? 73.53000 40.69700 10.25800  1.000 20.26000 ? 135 ARG   A O   1 
ATOM   666  C  CB  . ARG   A 1 91  ? 75.79000 39.66000 11.96800  1.000 21.96000 ? 135 ARG   A CB  1 
ATOM   667  C  CG  . ARG   A 1 91  ? 76.38000 40.76300 12.83000  1.000 23.78000 ? 135 ARG   A CG  1 
ATOM   668  C  CD  . ARG   A 1 91  ? 76.75200 40.25700 14.22200  1.000 28.78000 ? 135 ARG   A CD  1 
ATOM   669  N  NE  . ARG   A 1 91  ? 75.58200 39.95000 15.03700  1.000 32.68000 ? 135 ARG   A NE  1 
ATOM   670  C  CZ  . ARG   A 1 91  ? 74.98100 40.82000 15.83800  1.000 29.02000 ? 135 ARG   A CZ  1 
ATOM   671  N  NH1 . ARG   A 1 91  ? 75.41400 42.06500 15.95600  1.000 28.89000 ? 135 ARG   A NH1 1 
ATOM   672  N  NH2 . ARG   A 1 91  ? 73.92000 40.42900 16.53900  1.000 28.59000 ? 135 ARG   A NH2 1 
ATOM   673  N  N   . LEU   A 1 92  ? 75.10000 42.23200 9.78200   1.000 20.29000 ? 136 LEU   A N   1 
ATOM   674  C  CA  . LEU   A 1 92  ? 74.15200 43.30300 9.51600   1.000 20.21000 ? 136 LEU   A CA  1 
ATOM   675  C  C   . LEU   A 1 92  ? 73.91100 43.52800 8.02600   1.000 19.68000 ? 136 LEU   A C   1 
ATOM   676  O  O   . LEU   A 1 92  ? 73.33700 44.55500 7.65300   1.000 19.66000 ? 136 LEU   A O   1 
ATOM   677  C  CB  . LEU   A 1 92  ? 74.63800 44.60200 10.16300  1.000 19.88000 ? 136 LEU   A CB  1 
ATOM   678  C  CG  . LEU   A 1 92  ? 75.01400 44.52700 11.64800  1.000 20.98000 ? 136 LEU   A CG  1 
ATOM   679  C  CD1 . LEU   A 1 92  ? 75.54200 45.86400 12.13800  1.000 22.21000 ? 136 LEU   A CD1 1 
ATOM   680  C  CD2 . LEU   A 1 92  ? 73.83300 44.08400 12.48800  1.000 21.73000 ? 136 LEU   A CD2 1 
ATOM   681  N  N   . ASP   A 1 93  ? 74.31700 42.59000 7.17400   1.000 19.32000 ? 137 ASP   A N   1 
ATOM   682  C  CA  . ASP   A 1 93  ? 74.28800 42.82100 5.73500   1.000 18.79000 ? 137 ASP   A CA  1 
ATOM   683  C  C   . ASP   A 1 93  ? 72.86100 42.90600 5.20300   1.000 18.68000 ? 137 ASP   A C   1 
ATOM   684  O  O   . ASP   A 1 93  ? 71.99000 42.11400 5.56800   1.000 18.30000 ? 137 ASP   A O   1 
ATOM   685  C  CB  . ASP   A 1 93  ? 75.05800 41.72100 5.00800   1.000 18.49000 ? 137 ASP   A CB  1 
ATOM   686  C  CG  . ASP   A 1 93  ? 76.54400 41.80800 5.24400   1.000 18.80000 ? 137 ASP   A CG  1 
ATOM   687  O  OD1 . ASP   A 1 93  ? 77.01800 42.89800 5.61600   1.000 18.73000 ? 137 ASP   A OD1 1 
ATOM   688  O  OD2 . ASP   A 1 93  ? 77.24200 40.79200 5.06200   1.000 18.33000 ? 137 ASP   A OD2 1 
ATOM   689  N  N   . ALA   A 1 94  ? 72.64100 43.87200 4.31500   1.000 18.57000 ? 138 ALA   A N   1 
ATOM   690  C  CA  . ALA   A 1 94  ? 71.33400 44.16300 3.75400   1.000 18.25000 ? 138 ALA   A CA  1 
ATOM   691  C  C   . ALA   A 1 94  ? 70.96400 43.11500 2.70900   1.000 17.64000 ? 138 ALA   A C   1 
ATOM   692  O  O   . ALA   A 1 94  ? 71.80300 42.31100 2.30100   1.000 17.40000 ? 138 ALA   A O   1 
ATOM   693  C  CB  . ALA   A 1 94  ? 71.34500 45.57200 3.16300   1.000 18.46000 ? 138 ALA   A CB  1 
ATOM   694  N  N   . PRO   A 1 95  ? 69.69600 43.07400 2.27400   1.000 17.59000 ? 139 PRO   A N   1 
ATOM   695  C  CA  . PRO   A 1 95  ? 69.31200 42.05900 1.27800   1.000 17.15000 ? 139 PRO   A CA  1 
ATOM   696  C  C   . PRO   A 1 95  ? 70.08800 42.14800 -0.02400  1.000 16.90000 ? 139 PRO   A C   1 
ATOM   697  O  O   . PRO   A 1 95  ? 70.42500 41.11300 -0.60800  1.000 17.22000 ? 139 PRO   A O   1 
ATOM   698  C  CB  . PRO   A 1 95  ? 67.82000 42.33400 1.06900   1.000 17.10000 ? 139 PRO   A CB  1 
ATOM   699  C  CG  . PRO   A 1 95  ? 67.37800 42.89300 2.36600   1.000 17.35000 ? 139 PRO   A CG  1 
ATOM   700  C  CD  . PRO   A 1 95  ? 68.51400 43.75300 2.83000   1.000 17.76000 ? 139 PRO   A CD  1 
ATOM   701  N  N   . GLY   A 1 96  ? 70.38500 43.35900 -0.49300  1.000 17.21000 ? 140 GLY   A N   1 
ATOM   702  C  CA  . GLY   A 1 96  ? 71.21200 43.49100 -1.67800  1.000 17.37000 ? 140 GLY   A CA  1 
ATOM   703  C  C   . GLY   A 1 96  ? 72.60600 42.93800 -1.46900  1.000 17.20000 ? 140 GLY   A C   1 
ATOM   704  O  O   . GLY   A 1 96  ? 73.18100 42.31800 -2.36700  1.000 17.34000 ? 140 GLY   A O   1 
ATOM   705  N  N   . GLN   A 1 97  ? 73.16800 43.14400 -0.27400  1.000 17.09000 ? 141 GLN   A N   1 
ATOM   706  C  CA  . GLN   A 1 97  ? 74.48900 42.60100 0.01900   1.000 17.20000 ? 141 GLN   A CA  1 
ATOM   707  C  C   . GLN   A 1 97  ? 74.47500 41.08300 0.07100   1.000 17.45000 ? 141 GLN   A C   1 
ATOM   708  O  O   . GLN   A 1 97  ? 75.45600 40.44200 -0.31700  1.000 16.94000 ? 141 GLN   A O   1 
ATOM   709  C  CB  . GLN   A 1 97  ? 75.00900 43.16800 1.34200   1.000 17.32000 ? 141 GLN   A CB  1 
ATOM   710  C  CG  . GLN   A 1 97  ? 75.51900 44.59300 1.25700   1.000 17.34000 ? 141 GLN   A CG  1 
ATOM   711  C  CD  . GLN   A 1 97  ? 75.79500 45.19600 2.61700   1.000 17.96000 ? 141 GLN   A CD  1 
ATOM   712  O  OE1 . GLN   A 1 97  ? 74.93500 45.19400 3.49900   1.000 17.83000 ? 141 GLN   A OE1 1 
ATOM   713  N  NE2 . GLN   A 1 97  ? 76.99800 45.72300 2.79300   1.000 18.71000 ? 141 GLN   A NE2 1 
ATOM   714  N  N   . ARG   A 1 98  ? 73.37800 40.49200 0.54100   1.000 16.78000 ? 142 ARG   A N   1 
ATOM   715  C  CA  . ARG   A 1 98  ? 73.30900 39.03900 0.63600   1.000 16.84000 ? 142 ARG   A CA  1 
ATOM   716  C  C   . ARG   A 1 98  ? 73.10700 38.39900 -0.73100  1.000 16.96000 ? 142 ARG   A C   1 
ATOM   717  O  O   . ARG   A 1 98  ? 73.50700 37.24800 -0.93700  1.000 16.74000 ? 142 ARG   A O   1 
ATOM   718  C  CB  . ARG   A 1 98  ? 72.19200 38.63800 1.59800   1.000 16.65000 ? 142 ARG   A CB  1 
ATOM   719  C  CG  . ARG   A 1 98  ? 72.40500 39.19000 2.99800   1.000 17.00000 ? 142 ARG   A CG  1 
ATOM   720  C  CD  . ARG   A 1 98  ? 71.19200 39.03700 3.88700   1.000 16.89000 ? 142 ARG   A CD  1 
ATOM   721  N  NE  . ARG   A 1 98  ? 71.43100 39.70400 5.16000   1.000 17.40000 ? 142 ARG   A NE  1 
ATOM   722  C  CZ  . ARG   A 1 98  ? 71.94000 39.10900 6.22800   1.000 17.77000 ? 142 ARG   A CZ  1 
ATOM   723  N  NH1 . ARG   A 1 98  ? 72.18700 37.81000 6.24400   1.000 17.36000 ? 142 ARG   A NH1 1 
ATOM   724  N  NH2 . ARG   A 1 98  ? 72.21100 39.83700 7.30600   1.000 18.52000 ? 142 ARG   A NH2 1 
ATOM   725  N  N   . GLY   A 1 99  ? 72.49100 39.12100 -1.66800  1.000 16.94000 ? 143 GLY   A N   1 
ATOM   726  C  CA  . GLY   A 1 99  ? 72.40400 38.62200 -3.03100  1.000 16.93000 ? 143 GLY   A CA  1 
ATOM   727  C  C   . GLY   A 1 99  ? 73.75700 38.57100 -3.71600  1.000 17.49000 ? 143 GLY   A C   1 
ATOM   728  O  O   . GLY   A 1 99  ? 74.08900 37.58400 -4.37700  1.000 17.28000 ? 143 GLY   A O   1 
ATOM   729  N  N   . ARG   A 1 100 ? 74.55900 39.62800 -3.55800  1.000 17.71000 ? 144 ARG   A N   1 
ATOM   730  C  CA  . ARG   A 1 100 ? 75.91000 39.63100 -4.10800  1.000 18.02000 ? 144 ARG   A CA  1 
ATOM   731  C  C   . ARG   A 1 100 ? 76.75100 38.51300 -3.51000  1.000 17.41000 ? 144 ARG   A C   1 
ATOM   732  O  O   . ARG   A 1 100 ? 77.59300 37.92200 -4.19400  1.000 17.49000 ? 144 ARG   A O   1 
ATOM   733  C  CB  . ARG   A 1 100 ? 76.57800 40.98400 -3.85700  1.000 18.68000 ? 144 ARG   A CB  1 
ATOM   734  C  CG  . ARG   A 1 100 ? 75.92200 42.16700 -4.55800  1.000 19.26000 ? 144 ARG   A CG  1 
ATOM   735  C  CD  . ARG   A 1 100 ? 76.22300 42.16100 -6.05300  1.000 22.84000 ? 144 ARG   A CD  1 
ATOM   736  N  NE  . ARG   A 1 100 ? 75.62500 43.29800 -6.74700  1.000 24.61000 ? 144 ARG   A NE  1 
ATOM   737  C  CZ  . ARG   A 1 100 ? 75.57600 43.42800 -8.06700  1.000 26.14000 ? 144 ARG   A CZ  1 
ATOM   738  N  NH1 . ARG   A 1 100 ? 76.07800 42.50400 -8.87100  1.000 24.46000 ? 144 ARG   A NH1 1 
ATOM   739  N  NH2 . ARG   A 1 100 ? 75.00100 44.50600 -8.59200  1.000 26.62000 ? 144 ARG   A NH2 1 
ATOM   740  N  N   . GLN   A 1 101 ? 76.54300 38.21100 -2.23000  1.000 17.24000 ? 145 GLN   A N   1 
ATOM   741  C  CA  . GLN   A 1 101 ? 77.35100 37.18900 -1.57900  1.000 17.27000 ? 145 GLN   A CA  1 
ATOM   742  C  C   . GLN   A 1 101 ? 76.91200 35.78300 -1.96800  1.000 18.17000 ? 145 GLN   A C   1 
ATOM   743  O  O   . GLN   A 1 101 ? 77.74500 34.87400 -2.01300  1.000 17.01000 ? 145 GLN   A O   1 
ATOM   744  C  CB  . GLN   A 1 101 ? 77.31200 37.39300 -0.06200  1.000 17.20000 ? 145 GLN   A CB  1 
ATOM   745  C  CG  . GLN   A 1 101 ? 77.97100 38.70800 0.35500   1.000 17.18000 ? 145 GLN   A CG  1 
ATOM   746  C  CD  . GLN   A 1 101 ? 77.71300 39.08900 1.79700   1.000 17.12000 ? 145 GLN   A CD  1 
ATOM   747  O  OE1 . GLN   A 1 101 ? 77.32800 38.26000 2.61000   1.000 17.20000 ? 145 GLN   A OE1 1 
ATOM   748  N  NE2 . GLN   A 1 101 ? 77.92000 40.35700 2.11500   1.000 17.12000 ? 145 GLN   A NE2 1 
ATOM   749  N  N   . LEU   A 1 102 ? 75.62800 35.58800 -2.27700  1.000 16.94000 ? 146 LEU   A N   1 
ATOM   750  C  CA  . LEU   A 1 102 ? 75.19000 34.29800 -2.80400  1.000 16.87000 ? 146 LEU   A CA  1 
ATOM   751  C  C   . LEU   A 1 102 ? 75.85900 33.99800 -4.14000  1.000 17.53000 ? 146 LEU   A C   1 
ATOM   752  O  O   . LEU   A 1 102 ? 76.28500 32.86500 -4.38900  1.000 16.93000 ? 146 LEU   A O   1 
ATOM   753  C  CB  . LEU   A 1 102 ? 73.66800 34.27500 -2.94900  1.000 17.08000 ? 146 LEU   A CB  1 
ATOM   754  C  CG  . LEU   A 1 102 ? 72.85800 34.00700 -1.68300  1.000 16.76000 ? 146 LEU   A CG  1 
ATOM   755  C  CD1 . LEU   A 1 102 ? 71.38900 34.29600 -1.90300  1.000 16.26000 ? 146 LEU   A CD1 1 
ATOM   756  C  CD2 . LEU   A 1 102 ? 73.05600 32.57100 -1.26700  1.000 16.08000 ? 146 LEU   A CD2 1 
ATOM   757  N  N   . LEU   A 1 103 ? 75.96100 35.00300 -5.01200  1.000 16.99000 ? 147 LEU   A N   1 
ATOM   758  C  CA  . LEU   A 1 103 ? 76.66600 34.81400 -6.27500  1.000 17.21000 ? 147 LEU   A CA  1 
ATOM   759  C  C   . LEU   A 1 103 ? 78.15200 34.59400 -6.04900  1.000 17.30000 ? 147 LEU   A C   1 
ATOM   760  O  O   . LEU   A 1 103 ? 78.77500 33.80000 -6.76300  1.000 17.70000 ? 147 LEU   A O   1 
ATOM   761  C  CB  . LEU   A 1 103 ? 76.44200 36.01400 -7.19100  1.000 17.16000 ? 147 LEU   A CB  1 
ATOM   762  C  CG  . LEU   A 1 103 ? 74.99000 36.38300 -7.49900  1.000 17.21000 ? 147 LEU   A CG  1 
ATOM   763  C  CD1 . LEU   A 1 103 ? 74.93900 37.60800 -8.38900  1.000 17.25000 ? 147 LEU   A CD1 1 
ATOM   764  C  CD2 . LEU   A 1 103 ? 74.26900 35.21700 -8.14700  1.000 16.83000 ? 147 LEU   A CD2 1 
ATOM   765  N  N   . ALA   A 1 104 ? 78.73000 35.27900 -5.05900  1.000 17.61000 ? 148 ALA   A N   1 
ATOM   766  C  CA  . ALA   A 1 104 ? 80.12900 35.05900 -4.71000  1.000 17.51000 ? 148 ALA   A CA  1 
ATOM   767  C  C   . ALA   A 1 104 ? 80.38000 33.63900 -4.20700  1.000 18.15000 ? 148 ALA   A C   1 
ATOM   768  O  O   . ALA   A 1 104 ? 81.43800 33.06900 -4.49000  1.000 18.17000 ? 148 ALA   A O   1 
ATOM   769  C  CB  . ALA   A 1 104 ? 80.56700 36.08500 -3.66500  1.000 17.80000 ? 148 ALA   A CB  1 
ATOM   770  N  N   . ALA   A 1 105 ? 79.43500 33.05200 -3.46800  1.000 17.63000 ? 149 ALA   A N   1 
ATOM   771  C  CA  . ALA   A 1 105 ? 79.59400 31.66100 -3.04800  1.000 17.69000 ? 149 ALA   A CA  1 
ATOM   772  C  C   . ALA   A 1 105 ? 79.53400 30.71400 -4.23800  1.000 18.04000 ? 149 ALA   A C   1 
ATOM   773  O  O   . ALA   A 1 105 ? 80.34200 29.78500 -4.33700  1.000 18.40000 ? 149 ALA   A O   1 
ATOM   774  C  CB  . ALA   A 1 105 ? 78.52300 31.28500 -2.02700  1.000 17.30000 ? 149 ALA   A CB  1 
ATOM   775  N  N   . LEU   A 1 106 ? 78.57000 30.92400 -5.14000  1.000 17.88000 ? 150 LEU   A N   1 
ATOM   776  C  CA  . LEU   A 1 106 ? 78.45600 30.08900 -6.33200  1.000 18.11000 ? 150 LEU   A CA  1 
ATOM   777  C  C   . LEU   A 1 106 ? 79.69000 30.21200 -7.21500  1.000 19.15000 ? 150 LEU   A C   1 
ATOM   778  O  O   . LEU   A 1 106 ? 80.15700 29.21800 -7.78100  1.000 19.20000 ? 150 LEU   A O   1 
ATOM   779  C  CB  . LEU   A 1 106 ? 77.20000 30.47100 -7.11200  1.000 17.73000 ? 150 LEU   A CB  1 
ATOM   780  C  CG  . LEU   A 1 106 ? 75.88800 30.21400 -6.37600  1.000 17.17000 ? 150 LEU   A CG  1 
ATOM   781  C  CD1 . LEU   A 1 106 ? 74.70900 30.77300 -7.15000  1.000 16.91000 ? 150 LEU   A CD1 1 
ATOM   782  C  CD2 . LEU   A 1 106 ? 75.71300 28.73200 -6.13200  1.000 16.83000 ? 150 LEU   A CD2 1 
ATOM   783  N  N   . ASP   A 1 107 ? 80.22900 31.42500 -7.34800  1.000 18.78000 ? 151 ASP   A N   1 
ATOM   784  C  CA  . ASP   A 1 107 ? 81.45200 31.60200 -8.12400  1.000 19.46000 ? 151 ASP   A CA  1 
ATOM   785  C  C   . ASP   A 1 107 ? 82.63800 30.89800 -7.48200  1.000 20.62000 ? 151 ASP   A C   1 
ATOM   786  O  O   . ASP   A 1 107 ? 83.50900 30.38700 -8.19400  1.000 21.89000 ? 151 ASP   A O   1 
ATOM   787  C  CB  . ASP   A 1 107 ? 81.74900 33.08600 -8.30200  1.000 19.42000 ? 151 ASP   A CB  1 
ATOM   788  C  CG  . ASP   A 1 107 ? 80.75500 33.76400 -9.20600  1.000 18.15000 ? 151 ASP   A CG  1 
ATOM   789  O  OD1 . ASP   A 1 107 ? 80.09500 33.05200 -9.98500  1.000 17.37000 ? 151 ASP   A OD1 1 
ATOM   790  O  OD2 . ASP   A 1 107 ? 80.62600 35.00000 -9.14100  1.000 17.15000 ? 151 ASP   A OD2 1 
ATOM   791  N  N   . TYR   A 1 108 ? 82.69000 30.85800 -6.14800  1.000 20.31000 ? 152 TYR   A N   1 
ATOM   792  C  CA  . TYR   A 1 108 ? 83.77100 30.14600 -5.47500  1.000 21.07000 ? 152 TYR   A CA  1 
ATOM   793  C  C   . TYR   A 1 108 ? 83.70000 28.65100 -5.75200  1.000 21.83000 ? 152 TYR   A C   1 
ATOM   794  O  O   . TYR   A 1 108 ? 84.73500 28.00500 -5.95100  1.000 22.31000 ? 152 TYR   A O   1 
ATOM   795  C  CB  . TYR   A 1 108 ? 83.73300 30.41500 -3.96800  1.000 20.34000 ? 152 TYR   A CB  1 
ATOM   796  C  CG  . TYR   A 1 108 ? 84.74000 29.59700 -3.17900  1.000 20.92000 ? 152 TYR   A CG  1 
ATOM   797  C  CD1 . TYR   A 1 108 ? 86.05000 30.02700 -3.03200  1.000 21.65000 ? 152 TYR   A CD1 1 
ATOM   798  C  CD2 . TYR   A 1 108 ? 84.37700 28.39500 -2.58700  1.000 20.50000 ? 152 TYR   A CD2 1 
ATOM   799  C  CE1 . TYR   A 1 108 ? 86.96900 29.28400 -2.32300  1.000 21.30000 ? 152 TYR   A CE1 1 
ATOM   800  C  CE2 . TYR   A 1 108 ? 85.29200 27.64400 -1.87400  1.000 20.55000 ? 152 TYR   A CE2 1 
ATOM   801  C  CZ  . TYR   A 1 108 ? 86.58400 28.09400 -1.74500  1.000 21.20000 ? 152 TYR   A CZ  1 
ATOM   802  O  OH  . TYR   A 1 108 ? 87.50000 27.35000 -1.03800  1.000 24.56000 ? 152 TYR   A OH  1 
ATOM   803  N  N   . LEU   A 1 109 ? 82.49000 28.08300 -5.75200  1.000 20.84000 ? 153 LEU   A N   1 
ATOM   804  C  CA  . LEU   A 1 109 ? 82.32300 26.67500 -6.10500  1.000 21.26000 ? 153 LEU   A CA  1 
ATOM   805  C  C   . LEU   A 1 109 ? 82.88300 26.39300 -7.49200  1.000 21.86000 ? 153 LEU   A C   1 
ATOM   806  O  O   . LEU   A 1 109 ? 83.63200 25.43000 -7.69300  1.000 22.57000 ? 153 LEU   A O   1 
ATOM   807  C  CB  . LEU   A 1 109 ? 80.84300 26.28900 -6.05400  1.000 20.30000 ? 153 LEU   A CB  1 
ATOM   808  C  CG  . LEU   A 1 109 ? 80.09000 26.22700 -4.72600  1.000 18.80000 ? 153 LEU   A CG  1 
ATOM   809  C  CD1 . LEU   A 1 109 ? 78.62100 25.90600 -4.97500  1.000 17.75000 ? 153 LEU   A CD1 1 
ATOM   810  C  CD2 . LEU   A 1 109 ? 80.71000 25.19400 -3.81500  1.000 19.27000 ? 153 LEU   A CD2 1 
ATOM   811  N  N   . VAL   A 1 110 ? 82.53200 27.23800 -8.46000  1.000 21.62000 ? 154 VAL   A N   1 
ATOM   812  C  CA  . VAL   A 1 110 ? 82.91900 27.00800 -9.84700  1.000 22.14000 ? 154 VAL   A CA  1 
ATOM   813  C  C   . VAL   A 1 110 ? 84.41900 27.21500 -10.02900 1.000 22.75000 ? 154 VAL   A C   1 
ATOM   814  O  O   . VAL   A 1 110 ? 85.11300 26.36100 -10.58700 1.000 22.66000 ? 154 VAL   A O   1 
ATOM   815  C  CB  . VAL   A 1 110 ? 82.10400 27.92300 -10.77800 1.000 21.61000 ? 154 VAL   A CB  1 
ATOM   816  C  CG1 . VAL   A 1 110 ? 82.55900 27.75800 -12.22400 1.000 21.55000 ? 154 VAL   A CG1 1 
ATOM   817  C  CG2 . VAL   A 1 110 ? 80.62000 27.63600 -10.63700 1.000 20.91000 ? 154 VAL   A CG2 1 
ATOM   818  N  N   . GLU   A 1 111 ? 84.94400 28.34200 -9.54900  1.000 23.06000 ? 155 GLU   A N   1 
ATOM   819  C  CA  . GLU   A 1 111 ? 86.30000 28.74500 -9.89900  1.000 24.43000 ? 155 GLU   A CA  1 
ATOM   820  C  C   . GLU   A 1 111 ? 87.37000 28.25400 -8.93200  1.000 23.99000 ? 155 GLU   A C   1 
ATOM   821  O  O   . GLU   A 1 111 ? 88.50100 27.99900 -9.36100  1.000 24.37000 ? 155 GLU   A O   1 
ATOM   822  C  CB  . GLU   A 1 111 ? 86.38800 30.26900 -9.98800  1.000 25.33000 ? 155 GLU   A CB  1 
ATOM   823  C  CG  . GLU   A 1 111 ? 85.49800 30.88500 -11.05300 1.000 25.34000 ? 155 GLU   A CG  1 
ATOM   824  C  CD  . GLU   A 1 111 ? 85.69300 32.37900 -11.16900 1.000 28.18000 ? 155 GLU   A CD  1 
ATOM   825  O  OE1 . GLU   A 1 111 ? 86.75200 32.87200 -10.72800 1.000 29.81000 ? 155 GLU   A OE1 1 
ATOM   826  O  OE2 . GLU   A 1 111 ? 84.78900 33.06200 -11.69300 1.000 31.64000 ? 155 GLU   A OE2 1 
ATOM   827  N  N   . ARG   A 1 112 ? 87.05700 28.12200 -7.64200  1.000 23.86000 ? 156 ARG   A N   1 
ATOM   828  C  CA  . ARG   A 1 112 ? 88.09400 27.95200 -6.63600  1.000 24.60000 ? 156 ARG   A CA  1 
ATOM   829  C  C   . ARG   A 1 112 ? 87.85400 26.81900 -5.64700  1.000 24.17000 ? 156 ARG   A C   1 
ATOM   830  O  O   . ARG   A 1 112 ? 88.68600 26.62100 -4.75500  1.000 23.65000 ? 156 ARG   A O   1 
ATOM   831  C  CB  . ARG   A 1 112 ? 88.28600 29.26400 -5.86100  1.000 24.29000 ? 156 ARG   A CB  1 
ATOM   832  C  CG  . ARG   A 1 112 ? 89.09300 30.30000 -6.62300  1.000 24.26000 ? 156 ARG   A CG  1 
ATOM   833  C  CD  . ARG   A 1 112 ? 88.96400 31.69900 -6.03700  1.000 24.72000 ? 156 ARG   A CD  1 
ATOM   834  N  NE  . ARG   A 1 112 ? 88.08700 32.55000 -6.83400  1.000 32.16000 ? 156 ARG   A NE  1 
ATOM   835  C  CZ  . ARG   A 1 112 ? 86.95100 33.07800 -6.39900  1.000 27.29000 ? 156 ARG   A CZ  1 
ATOM   836  N  NH1 . ARG   A 1 112 ? 86.53700 32.89700 -5.15600  1.000 26.41000 ? 156 ARG   A NH1 1 
ATOM   837  N  NH2 . ARG   A 1 112 ? 86.21700 33.81200 -7.23100  1.000 26.43000 ? 156 ARG   A NH2 1 
ATOM   838  N  N   . SER   A 1 113 ? 86.77000 26.06100 -5.78200  1.000 24.02000 ? 157 SER   A N   1 
ATOM   839  C  CA  . SER   A 1 113 ? 86.47800 25.03600 -4.79400  1.000 24.61000 ? 157 SER   A CA  1 
ATOM   840  C  C   . SER   A 1 113 ? 87.47200 23.87800 -4.90000  1.000 25.28000 ? 157 SER   A C   1 
ATOM   841  O  O   . SER   A 1 113 ? 88.23000 23.74600 -5.86400  1.000 24.97000 ? 157 SER   A O   1 
ATOM   842  C  CB  . SER   A 1 113 ? 85.04600 24.53000 -4.94900  1.000 23.92000 ? 157 SER   A CB  1 
ATOM   843  O  OG  . SER   A 1 113 ? 84.85800 23.87700 -6.18800  1.000 23.73000 ? 157 SER   A OG  1 
ATOM   844  N  N   . ASP   A 1 114 ? 87.47000 23.04500 -3.86300  1.000 25.25000 ? 158 ASP   A N   1 
ATOM   845  C  CA  . ASP   A 1 114 ? 88.30400 21.85300 -3.83000  1.000 25.76000 ? 158 ASP   A CA  1 
ATOM   846  C  C   . ASP   A 1 114 ? 87.94200 20.91900 -4.98100  1.000 26.27000 ? 158 ASP   A C   1 
ATOM   847  O  O   . ASP   A 1 114 ? 86.78700 20.84300 -5.40900  1.000 25.84000 ? 158 ASP   A O   1 
ATOM   848  C  CB  . ASP   A 1 114 ? 88.13000 21.14600 -2.48200  1.000 27.38000 ? 158 ASP   A CB  1 
ATOM   849  C  CG  . ASP   A 1 114 ? 89.14000 20.04500 -2.25800  1.000 28.52000 ? 158 ASP   A CG  1 
ATOM   850  O  OD1 . ASP   A 1 114 ? 90.34700 20.35000 -2.18400  1.000 28.72000 ? 158 ASP   A OD1 1 
ATOM   851  O  OD2 . ASP   A 1 114 ? 88.72000 18.87500 -2.13700  1.000 27.71000 ? 158 ASP   A OD2 1 
ATOM   852  N  N   . ARG   A 1 115 ? 88.95200 20.20600 -5.49000  1.000 27.52000 ? 159 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 115 ? 88.73800 19.33800 -6.64500  1.000 28.65000 ? 159 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 115 ? 87.67800 18.28200 -6.36200  1.000 27.85000 ? 159 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 115 ? 86.90400 17.91800 -7.25400  1.000 27.12000 ? 159 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 115 ? 90.04900 18.67700 -7.06500  1.000 30.36000 ? 159 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 115 ? 90.77100 17.95600 -5.94300  1.000 31.20000 ? 159 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 115 ? 91.73700 16.90900 -6.47900  1.000 33.12000 ? 159 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 115 ? 91.03300 15.80200 -7.11300  1.000 33.56000 ? 159 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 115 ? 90.47600 14.79400 -6.45500  1.000 35.41000 ? 159 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 115 ? 90.50900 14.72900 -5.13400  1.000 38.37000 ? 159 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 115 ? 89.86800 13.82900 -7.13800  1.000 39.25000 ? 159 ARG   A NH2 1 
ATOM   863  N  N   . LYS   A 1 116 ? 87.62300 17.77600 -5.12600  1.000 28.61000 ? 160 LYS   A N   1 
ATOM   864  C  CA  . LYS   A 1 116 ? 86.57200 16.83000 -4.76900  1.000 27.79000 ? 160 LYS   A CA  1 
ATOM   865  C  C   . LYS   A 1 116 ? 85.19100 17.41900 -5.01500  1.000 26.48000 ? 160 LYS   A C   1 
ATOM   866  O  O   . LYS   A 1 116 ? 84.25400 16.68900 -5.35500  1.000 25.81000 ? 160 LYS   A O   1 
ATOM   867  C  CB  . LYS   A 1 116 ? 86.71000 16.40500 -3.30700  1.000 28.24000 ? 160 LYS   A CB  1 
ATOM   868  C  CG  . LYS   A 1 116 ? 87.98700 15.64300 -2.98700  1.000 29.24000 ? 160 LYS   A CG  1 
ATOM   869  C  CD  . LYS   A 1 116 ? 87.96400 15.10200 -1.56200  1.000 29.65000 ? 160 LYS   A CD  1 
ATOM   870  C  CE  . LYS   A 1 116 ? 87.96100 16.22400 -0.53100  1.000 29.55000 ? 160 LYS   A CE  1 
ATOM   871  N  NZ  . LYS   A 1 116 ? 89.25700 16.95900 -0.51600  1.000 31.59000 ? 160 LYS   A NZ  1 
ATOM   872  N  N   . VAL   A 1 117 ? 85.04900 18.73100 -4.86200  1.000 26.29000 ? 161 VAL   A N   1 
ATOM   873  C  CA  . VAL   A 1 117 ? 83.78400 19.39600 -5.14200  1.000 25.28000 ? 161 VAL   A CA  1 
ATOM   874  C  C   . VAL   A 1 117 ? 83.68400 19.79500 -6.61000  1.000 24.33000 ? 161 VAL   A C   1 
ATOM   875  O  O   . VAL   A 1 117 ? 82.64800 19.58200 -7.24400  1.000 23.61000 ? 161 VAL   A O   1 
ATOM   876  C  CB  . VAL   A 1 117 ? 83.62300 20.61500 -4.21600  1.000 24.92000 ? 161 VAL   A CB  1 
ATOM   877  C  CG1 . VAL   A 1 117 ? 82.26600 21.26000 -4.42500  1.000 23.72000 ? 161 VAL   A CG1 1 
ATOM   878  C  CG2 . VAL   A 1 117 ? 83.81500 20.20700 -2.75900  1.000 23.27000 ? 161 VAL   A CG2 1 
ATOM   879  N  N   . ARG   A 1 118 ? 84.75800 20.37000 -7.15600  1.000 24.71000 ? 162 ARG   A N   1 
ATOM   880  C  CA  . ARG   A 1 118 ? 84.76500 20.82700 -8.54500  1.000 24.64000 ? 162 ARG   A CA  1 
ATOM   881  C  C   . ARG   A 1 118 ? 84.34000 19.71600 -9.49600  1.000 23.83000 ? 162 ARG   A C   1 
ATOM   882  O  O   . ARG   A 1 118 ? 83.45500 19.90300 -10.33800 1.000 22.90000 ? 162 ARG   A O   1 
ATOM   883  C  CB  . ARG   A 1 118 ? 86.16200 21.33200 -8.90600  1.000 25.15000 ? 162 ARG   A CB  1 
ATOM   884  C  CG  . ARG   A 1 118 ? 86.21300 22.36600 -10.01700 1.000 24.16000 ? 162 ARG   A CG  1 
ATOM   885  C  CD  . ARG   A 1 118 ? 86.35800 23.75900 -9.43800  1.000 23.84000 ? 162 ARG   A CD  1 
ATOM   886  N  NE  . ARG   A 1 118 ? 87.54900 23.88000 -8.60600  1.000 24.07000 ? 162 ARG   A NE  1 
ATOM   887  C  CZ  . ARG   A 1 118 ? 88.61100 24.61500 -8.90900  1.000 24.55000 ? 162 ARG   A CZ  1 
ATOM   888  N  NH1 . ARG   A 1 118 ? 88.66100 25.33700 -10.01600 1.000 25.13000 ? 162 ARG   A NH1 1 
ATOM   889  N  NH2 . ARG   A 1 118 ? 89.64800 24.63100 -8.07500  1.000 29.20000 ? 162 ARG   A NH2 1 
ATOM   890  N  N   . GLU   A 1 119 ? 84.95100 18.53900 -9.35700  1.000 24.55000 ? 163 GLU   A N   1 
ATOM   891  C  CA  . GLU   A 1 119 ? 84.71100 17.43100 -10.26900 1.000 24.78000 ? 163 GLU   A CA  1 
ATOM   892  C  C   . GLU   A 1 119 ? 83.32200 16.82300 -10.12200 1.000 23.41000 ? 163 GLU   A C   1 
ATOM   893  O  O   . GLU   A 1 119 ? 82.94800 15.97700 -10.94100 1.000 23.47000 ? 163 GLU   A O   1 
ATOM   894  C  CB  . GLU   A 1 119 ? 85.77500 16.35600 -10.05800 1.000 26.45000 ? 163 GLU   A CB  1 
ATOM   895  C  CG  . GLU   A 1 119 ? 87.19400 16.85600 -10.27300 1.000 26.52000 ? 163 GLU   A CG  1 
ATOM   896  C  CD  . GLU   A 1 119 ? 88.23500 15.77300 -10.06300 1.000 28.85000 ? 163 GLU   A CD  1 
ATOM   897  O  OE1 . GLU   A 1 119 ? 87.84900 14.58800 -9.97400  1.000 28.49000 ? 163 GLU   A OE1 1 
ATOM   898  O  OE2 . GLU   A 1 119 ? 89.43700 16.10900 -9.98400  1.000 30.24000 ? 163 GLU   A OE2 1 
ATOM   899  N  N   . ARG   A 1 120 ? 82.55700 17.21900 -9.11100  1.000 23.27000 ? 164 ARG   A N   1 
ATOM   900  C  CA  . ARG   A 1 120 ? 81.18700 16.75800 -8.95200  1.000 22.80000 ? 164 ARG   A CA  1 
ATOM   901  C  C   . ARG   A 1 120 ? 80.16900 17.81600 -9.34300  1.000 22.39000 ? 164 ARG   A C   1 
ATOM   902  O  O   . ARG   A 1 120 ? 78.96200 17.57100 -9.23900  1.000 21.94000 ? 164 ARG   A O   1 
ATOM   903  C  CB  . ARG   A 1 120 ? 80.94100 16.32700 -7.50600  1.000 22.26000 ? 164 ARG   A CB  1 
ATOM   904  C  CG  . ARG   A 1 120 ? 81.67900 15.07500 -7.08100  1.000 22.62000 ? 164 ARG   A CG  1 
ATOM   905  C  CD  . ARG   A 1 120 ? 81.50600 14.84800 -5.58800  1.000 23.76000 ? 164 ARG   A CD  1 
ATOM   906  N  NE  . ARG   A 1 120 ? 81.77700 13.46900 -5.20600  1.000 24.64000 ? 164 ARG   A NE  1 
ATOM   907  C  CZ  . ARG   A 1 120 ? 82.98900 12.98200 -4.98400  1.000 25.00000 ? 164 ARG   A CZ  1 
ATOM   908  N  NH1 . ARG   A 1 120 ? 84.06900 13.73500 -5.11200  1.000 25.33000 ? 164 ARG   A NH1 1 
ATOM   909  N  NH2 . ARG   A 1 120 ? 83.12100 11.70800 -4.62600  1.000 24.60000 ? 164 ARG   A NH2 1 
ATOM   910  N  N   . LEU   A 1 121 ? 80.62500 18.97300 -9.80400  1.000 22.19000 ? 165 LEU   A N   1 
ATOM   911  C  CA  . LEU   A 1 121 ? 79.78100 20.13800 -10.00100 1.000 21.46000 ? 165 LEU   A CA  1 
ATOM   912  C  C   . LEU   A 1 121 ? 79.51800 20.36400 -11.48100 1.000 20.67000 ? 165 LEU   A C   1 
ATOM   913  O  O   . LEU   A 1 121 ? 80.43800 20.28600 -12.30500 1.000 20.54000 ? 165 LEU   A O   1 
ATOM   914  C  CB  . LEU   A 1 121 ? 80.44200 21.38000 -9.39300  1.000 21.53000 ? 165 LEU   A CB  1 
ATOM   915  C  CG  . LEU   A 1 121 ? 79.89400 22.76600 -9.72400  1.000 21.11000 ? 165 LEU   A CG  1 
ATOM   916  C  CD1 . LEU   A 1 121 ? 78.51400 22.97800 -9.10700  1.000 20.01000 ? 165 LEU   A CD1 1 
ATOM   917  C  CD2 . LEU   A 1 121 ? 80.88000 23.84100 -9.28100  1.000 21.41000 ? 165 LEU   A CD2 1 
ATOM   918  N  N   . ASP   A 1 122 ? 78.25500 20.63000 -11.80900 1.000 20.31000 ? 166 ASP   A N   1 
ATOM   919  C  CA  . ASP   A 1 122 ? 77.89300 21.18200 -13.10600 1.000 20.13000 ? 166 ASP   A CA  1 
ATOM   920  C  C   . ASP   A 1 122 ? 77.84000 22.69600 -12.95800 1.000 20.12000 ? 166 ASP   A C   1 
ATOM   921  O  O   . ASP   A 1 122 ? 76.85100 23.22600 -12.43000 1.000 19.75000 ? 166 ASP   A O   1 
ATOM   922  C  CB  . ASP   A 1 122 ? 76.54300 20.63900 -13.57700 1.000 20.01000 ? 166 ASP   A CB  1 
ATOM   923  C  CG  . ASP   A 1 122 ? 76.27200 20.93100 -15.03800 1.000 19.71000 ? 166 ASP   A CG  1 
ATOM   924  O  OD1 . ASP   A 1 122 ? 76.81200 21.92600 -15.57600 1.000 19.55000 ? 166 ASP   A OD1 1 
ATOM   925  O  OD2 . ASP   A 1 122 ? 75.52000 20.16000 -15.65400 1.000 19.24000 ? 166 ASP   A OD2 1 
ATOM   926  N  N   . PRO   A 1 123 ? 78.86100 23.43900 -13.38800 1.000 20.34000 ? 167 PRO   A N   1 
ATOM   927  C  CA  . PRO   A 1 123 ? 78.87100 24.88400 -13.13300 1.000 20.48000 ? 167 PRO   A CA  1 
ATOM   928  C  C   . PRO   A 1 123 ? 77.81900 25.66600 -13.90100 1.000 19.96000 ? 167 PRO   A C   1 
ATOM   929  O  O   . PRO   A 1 123 ? 77.73900 26.88700 -13.72800 1.000 19.32000 ? 167 PRO   A O   1 
ATOM   930  C  CB  . PRO   A 1 123 ? 80.28700 25.30300 -13.55500 1.000 20.64000 ? 167 PRO   A CB  1 
ATOM   931  C  CG  . PRO   A 1 123 ? 80.70100 24.28200 -14.54100 1.000 20.10000 ? 167 PRO   A CG  1 
ATOM   932  C  CD  . PRO   A 1 123 ? 80.09300 22.99400 -14.06100 1.000 20.20000 ? 167 PRO   A CD  1 
ATOM   933  N  N   . ASN   A 1 124 ? 77.01200 25.02000 -14.73700 1.000 19.98000 ? 168 ASN   A N   1 
ATOM   934  C  CA  . ASN   A 1 124 ? 75.95500 25.69500 -15.47300 1.000 20.09000 ? 168 ASN   A CA  1 
ATOM   935  C  C   . ASN   A 1 124 ? 74.59100 25.55800 -14.81200 1.000 19.44000 ? 168 ASN   A C   1 
ATOM   936  O  O   . ASN   A 1 124 ? 73.62200 26.15300 -15.29400 1.000 18.95000 ? 168 ASN   A O   1 
ATOM   937  C  CB  . ASN   A 1 124 ? 75.89300 25.15700 -16.90900 1.000 20.26000 ? 168 ASN   A CB  1 
ATOM   938  C  CG  . ASN   A 1 124 ? 77.19000 25.37400 -17.66900 1.000 21.58000 ? 168 ASN   A CG  1 
ATOM   939  O  OD1 . ASN   A 1 124 ? 77.79500 24.42900 -18.17200 1.000 23.37000 ? 168 ASN   A OD1 1 
ATOM   940  N  ND2 . ASN   A 1 124 ? 77.62500 26.62500 -17.74900 1.000 21.56000 ? 168 ASN   A ND2 1 
ATOM   941  N  N   . ARG   A 1 125 ? 74.49000 24.80800 -13.71800 1.000 19.15000 ? 169 ARG   A N   1 
ATOM   942  C  CA  . ARG   A 1 125 ? 73.21500 24.54600 -13.05100 1.000 18.72000 ? 169 ARG   A CA  1 
ATOM   943  C  C   . ARG   A 1 125 ? 73.33300 24.96700 -11.58800 1.000 18.07000 ? 169 ARG   A C   1 
ATOM   944  O  O   . ARG   A 1 125 ? 73.69700 24.16500 -10.72700 1.000 17.88000 ? 169 ARG   A O   1 
ATOM   945  C  CB  . ARG   A 1 125 ? 72.83100 23.07600 -13.19500 1.000 19.18000 ? 169 ARG   A CB  1 
ATOM   946  C  CG  . ARG   A 1 125 ? 72.72500 22.63500 -14.64200 1.000 19.54000 ? 169 ARG   A CG  1 
ATOM   947  C  CD  . ARG   A 1 125 ? 72.08700 21.26600 -14.79200 1.000 20.57000 ? 169 ARG   A CD  1 
ATOM   948  N  NE  . ARG   A 1 125 ? 72.91200 20.18300 -14.27100 1.000 20.34000 ? 169 ARG   A NE  1 
ATOM   949  C  CZ  . ARG   A 1 125 ? 72.53600 19.35600 -13.30600 1.000 20.38000 ? 169 ARG   A CZ  1 
ATOM   950  N  NH1 . ARG   A 1 125 ? 71.35700 19.46900 -12.72000 1.000 20.10000 ? 169 ARG   A NH1 1 
ATOM   951  N  NH2 . ARG   A 1 125 ? 73.35800 18.38300 -12.92700 1.000 20.34000 ? 169 ARG   A NH2 1 
ATOM   952  N  N   . LEU   A 1 126 ? 73.00700 26.22900 -11.31200 1.000 17.66000 ? 170 LEU   A N   1 
ATOM   953  C  CA  . LEU   A 1 126 ? 73.18700 26.83300 -10.00200 1.000 17.44000 ? 170 LEU   A CA  1 
ATOM   954  C  C   . LEU   A 1 126 ? 71.88500 27.47000 -9.53500  1.000 16.82000 ? 170 LEU   A C   1 
ATOM   955  O  O   . LEU   A 1 126 ? 71.09600 27.97100 -10.34100 1.000 17.12000 ? 170 LEU   A O   1 
ATOM   956  C  CB  . LEU   A 1 126 ? 74.29800 27.88800 -10.03200 1.000 17.38000 ? 170 LEU   A CB  1 
ATOM   957  C  CG  . LEU   A 1 126 ? 75.64200 27.43700 -10.60600 1.000 18.06000 ? 170 LEU   A CG  1 
ATOM   958  C  CD1 . LEU   A 1 126 ? 76.63200 28.58300 -10.57900 1.000 17.88000 ? 170 LEU   A CD1 1 
ATOM   959  C  CD2 . LEU   A 1 126 ? 76.19300 26.23300 -9.86100  1.000 18.10000 ? 170 LEU   A CD2 1 
ATOM   960  N  N   . ALA   A 1 127 ? 71.66800 27.45100 -8.21900  1.000 16.80000 ? 171 ALA   A N   1 
ATOM   961  C  CA  . ALA   A 1 127 ? 70.45700 28.00400 -7.62800  1.000 16.49000 ? 171 ALA   A CA  1 
ATOM   962  C  C   . ALA   A 1 127 ? 70.82400 28.82400 -6.40000  1.000 16.60000 ? 171 ALA   A C   1 
ATOM   963  O  O   . ALA   A 1 127 ? 71.96700 28.80700 -5.93600  1.000 16.05000 ? 171 ALA   A O   1 
ATOM   964  C  CB  . ALA   A 1 127 ? 69.45700 26.90200 -7.25600  1.000 16.67000 ? 171 ALA   A CB  1 
ATOM   965  N  N   . VAL   A 1 128 ? 69.83800 29.55700 -5.88000  1.000 15.82000 ? 172 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 128 ? 70.00100 30.33900 -4.66000  1.000 15.64000 ? 172 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 128 ? 68.82100 30.08300 -3.73000  1.000 15.37000 ? 172 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 128 ? 67.69600 29.82400 -4.16900  1.000 15.24000 ? 172 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 128 ? 70.15100 31.85200 -4.94100  1.000 15.94000 ? 172 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 128 ? 71.50600 32.15500 -5.56000  1.000 16.13000 ? 172 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 128 ? 69.02400 32.36000 -5.82800  1.000 15.53000 ? 172 VAL   A CG2 1 
ATOM   972  N  N   . MET   A 1 129 ? 69.09400 30.15000 -2.42800  1.000 15.20000 ? 173 MET   A N   1 
ATOM   973  C  CA  . MET   A 1 129 ? 68.07300 30.01600 -1.40000  1.000 14.92000 ? 173 MET   A CA  1 
ATOM   974  C  C   . MET   A 1 129 ? 68.51100 30.84600 -0.20200  1.000 15.56000 ? 173 MET   A C   1 
ATOM   975  O  O   . MET   A 1 129 ? 69.70700 30.99400 0.05600   1.000 14.94000 ? 173 MET   A O   1 
ATOM   976  C  CB  . MET   A 1 129 ? 67.85700 28.54300 -1.02000  1.000 15.04000 ? 173 MET   A CB  1 
ATOM   977  C  CG  . MET   A 1 129 ? 66.74600 28.29500 -0.00700  1.000 15.05000 ? 173 MET   A CG  1 
ATOM   978  S  SD  . MET   A 1 129 ? 66.24300 26.56500 0.08200   1.000 14.95000 ? 173 MET   A SD  1 
ATOM   979  C  CE  . MET   A 1 129 ? 67.83800 25.75800 0.12800   1.000 15.29000 ? 173 MET   A CE  1 
ATOM   980  N  N   . GLY   A 1 130 ? 67.54600 31.41800 0.50900   1.000 14.91000 ? 174 GLY   A N   1 
ATOM   981  C  CA  . GLY   A 1 130 ? 67.87800 32.26300 1.64000   1.000 15.20000 ? 174 GLY   A CA  1 
ATOM   982  C  C   . GLY   A 1 130 ? 66.69700 32.46800 2.55700   1.000 15.38000 ? 174 GLY   A C   1 
ATOM   983  O  O   . GLY   A 1 130 ? 65.54100 32.43300 2.12400   1.000 15.20000 ? 174 GLY   A O   1 
ATOM   984  N  N   . HIS   A 1 131 ? 66.99200 32.71000 3.83300   1.000 15.56000 ? 175 HIS   A N   1 
ATOM   985  C  CA  . HIS   A 1 131 ? 65.97800 32.91300 4.85800   1.000 15.86000 ? 175 HIS   A CA  1 
ATOM   986  C  C   . HIS   A 1 131 ? 65.87900 34.39300 5.20700   1.000 16.60000 ? 175 HIS   A C   1 
ATOM   987  O  O   . HIS   A 1 131 ? 66.90100 35.05100 5.42500   1.000 15.60000 ? 175 HIS   A O   1 
ATOM   988  C  CB  . HIS   A 1 131 ? 66.30700 32.09300 6.10800   1.000 16.10000 ? 175 HIS   A CB  1 
ATOM   989  C  CG  . HIS   A 1 131 ? 65.38300 32.34900 7.25500   1.000 16.37000 ? 175 HIS   A CG  1 
ATOM   990  N  ND1 . HIS   A 1 131 ? 65.83400 32.67600 8.51600   1.000 16.69000 ? 175 HIS   A ND1 1 
ATOM   991  C  CD2 . HIS   A 1 131 ? 64.03200 32.33700 7.32900   1.000 16.46000 ? 175 HIS   A CD2 1 
ATOM   992  C  CE1 . HIS   A 1 131 ? 64.79900 32.85100 9.31800   1.000 17.00000 ? 175 HIS   A CE1 1 
ATOM   993  N  NE2 . HIS   A 1 131 ? 63.69300 32.65300 8.62200   1.000 16.76000 ? 175 HIS   A NE2 1 
ATOM   994  N  N   . ALA   A 1 132 ? 64.64800 34.91100 5.23700   1.000 16.39000 ? 176 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 132 ? 64.36200 36.26000 5.71300   1.000 16.14000 ? 176 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 132 ? 65.06900 37.32600 4.88900   1.000 16.12000 ? 176 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 132 ? 64.75100 37.51300 3.71100   1.000 15.68000 ? 176 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 132 ? 64.74900 36.38700 7.18600   1.000 16.52000 ? 176 ALA   A CB  1 
ATOM   999  N  N   . MET   A 1 133 ? 66.01400 38.05000 5.49000   1.000 16.61000 ? 177 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 133 ? 66.82100 38.95400 4.67900   1.000 16.31000 ? 177 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 133 ? 67.63700 38.19100 3.65000   1.000 16.05000 ? 177 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 133 ? 67.93300 38.72700 2.57800   1.000 15.99000 ? 177 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 133 ? 67.74500 39.80200 5.54600   1.000 17.05000 ? 177 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 133 ? 67.12500 41.10300 5.95600   1.000 17.31000 ? 177 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 133 ? 68.31600 42.34600 6.47500   1.000 17.91000 ? 177 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 133 ? 67.16300 43.52400 7.15200   1.000 18.37000 ? 177 MET   A CE  1 
ATOM   1007 N  N   . GLY   A 1 134 ? 68.01300 36.94900 3.95500   1.000 16.12000 ? 178 GLY   A N   1 
ATOM   1008 C  CA  . GLY   A 1 134 ? 68.64100 36.12000 2.94500   1.000 15.71000 ? 178 GLY   A CA  1 
ATOM   1009 C  C   . GLY   A 1 134 ? 67.67900 35.74800 1.83900   1.000 15.40000 ? 178 GLY   A C   1 
ATOM   1010 O  O   . GLY   A 1 134 ? 68.10000 35.49200 0.70800   1.000 15.26000 ? 178 GLY   A O   1 
ATOM   1011 N  N   . GLY   A 1 135 ? 66.38100 35.70300 2.15100   1.000 15.34000 ? 179 GLY   A N   1 
ATOM   1012 C  CA  . GLY   A 1 135 ? 65.38100 35.48900 1.11800   1.000 15.22000 ? 179 GLY   A CA  1 
ATOM   1013 C  C   . GLY   A 1 135 ? 65.19500 36.70600 0.23500   1.000 15.23000 ? 179 GLY   A C   1 
ATOM   1014 O  O   . GLY   A 1 135 ? 65.02600 36.58200 -0.98000  1.000 15.11000 ? 179 GLY   A O   1 
ATOM   1015 N  N   . GLY   A 1 136 ? 65.21500 37.89800 0.83000   1.000 15.44000 ? 180 GLY   A N   1 
ATOM   1016 C  CA  . GLY   A 1 136 ? 65.30200 39.10300 0.02800   1.000 15.80000 ? 180 GLY   A CA  1 
ATOM   1017 C  C   . GLY   A 1 136 ? 66.57800 39.16100 -0.78700  1.000 15.73000 ? 180 GLY   A C   1 
ATOM   1018 O  O   . GLY   A 1 136 ? 66.60600 39.76100 -1.86300  1.000 16.05000 ? 180 GLY   A O   1 
ATOM   1019 N  N   . GLY   A 1 137 ? 67.64800 38.53600 -0.29200  1.000 15.62000 ? 181 GLY   A N   1 
ATOM   1020 C  CA  . GLY   A 1 137 ? 68.85800 38.42200 -1.08400  1.000 15.70000 ? 181 GLY   A CA  1 
ATOM   1021 C  C   . GLY   A 1 137 ? 68.72400 37.43500 -2.22500  1.000 15.78000 ? 181 GLY   A C   1 
ATOM   1022 O  O   . GLY   A 1 137 ? 69.35900 37.59800 -3.26800  1.000 15.72000 ? 181 GLY   A O   1 
ATOM   1023 N  N   . SER   A 1 138 ? 67.89600 36.40400 -2.04700  1.000 15.20000 ? 182 SER   A N   1 
ATOM   1024 C  CA  . SER   A 1 138 ? 67.68300 35.43200 -3.11300  1.000 15.21000 ? 182 SER   A CA  1 
ATOM   1025 C  C   . SER   A 1 138 ? 66.98600 36.07500 -4.30900  1.000 15.54000 ? 182 SER   A C   1 
ATOM   1026 O  O   . SER   A 1 138 ? 67.33900 35.79800 -5.46200  1.000 15.55000 ? 182 SER   A O   1 
ATOM   1027 C  CB  . SER   A 1 138 ? 66.88000 34.24900 -2.57500  1.000 14.81000 ? 182 SER   A CB  1 
ATOM   1028 O  OG  . SER   A 1 138 ? 66.95200 33.12900 -3.43600  1.000 14.80000 ? 182 SER   A OG  1 
ATOM   1029 N  N   . LEU   A 1 139 ? 66.00500 36.95000 -4.05300  1.000 15.51000 ? 183 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 139 ? 65.38000 37.72200 -5.12500  1.000 16.00000 ? 183 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 139 ? 66.37500 38.67700 -5.77400  1.000 16.05000 ? 183 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 139 ? 66.38200 38.83300 -6.99900  1.000 16.25000 ? 183 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 139 ? 64.18100 38.50300 -4.58400  1.000 16.30000 ? 183 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 139 ? 63.01200 37.74500 -3.95800  1.000 16.46000 ? 183 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 139 ? 62.10500 38.70100 -3.18500  1.000 16.82000 ? 183 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 139 ? 62.22800 37.00400 -5.01700  1.000 15.90000 ? 183 LEU   A CD2 1 
ATOM   1037 N  N   . GLU   A 1 140 ? 67.21000 39.34100 -4.96800  1.000 16.19000 ? 184 GLU   A N   1 
ATOM   1038 C  CA  . GLU   A 1 140 ? 68.22700 40.22700 -5.52300  1.000 16.49000 ? 184 GLU   A CA  1 
ATOM   1039 C  C   . GLU   A 1 140 ? 69.25100 39.45700 -6.34700  1.000 16.50000 ? 184 GLU   A C   1 
ATOM   1040 O  O   . GLU   A 1 140 ? 69.80300 39.99600 -7.31200  1.000 16.66000 ? 184 GLU   A O   1 
ATOM   1041 C  CB  . GLU   A 1 140 ? 68.92800 40.99500 -4.40000  1.000 16.70000 ? 184 GLU   A CB  1 
ATOM   1042 C  CG  . GLU   A 1 140 ? 68.05700 42.01200 -3.67700  1.000 16.96000 ? 184 GLU   A CG  1 
ATOM   1043 C  CD  . GLU   A 1 140 ? 68.22000 43.41000 -4.23300  1.000 17.27000 ? 184 GLU   A CD  1 
ATOM   1044 O  OE1 . GLU   A 1 140 ? 69.06200 43.58300 -5.13300  1.000 17.44000 ? 184 GLU   A OE1 1 
ATOM   1045 O  OE2 . GLU   A 1 140 ? 67.51700 44.33500 -3.77300  1.000 17.28000 ? 184 GLU   A OE2 1 
ATOM   1046 N  N   . ALA   A 1 141 ? 69.52300 38.20400 -5.98200  1.000 16.31000 ? 185 ALA   A N   1 
ATOM   1047 C  CA  . ALA   A 1 141 ? 70.49300 37.40800 -6.72500  1.000 16.49000 ? 185 ALA   A CA  1 
ATOM   1048 C  C   . ALA   A 1 141 ? 69.98800 37.07400 -8.12300  1.000 16.33000 ? 185 ALA   A C   1 
ATOM   1049 O  O   . ALA   A 1 141 ? 70.77300 37.04600 -9.07800  1.000 16.43000 ? 185 ALA   A O   1 
ATOM   1050 C  CB  . ALA   A 1 141 ? 70.82000 36.12700 -5.95800  1.000 16.32000 ? 185 ALA   A CB  1 
ATOM   1051 N  N   . THR   A 1 142 ? 68.68600 36.80400 -8.26300  1.000 16.16000 ? 186 THR   A N   1 
ATOM   1052 C  CA  . THR   A 1 142 ? 68.14200 36.46600 -9.57600  1.000 16.20000 ? 186 THR   A CA  1 
ATOM   1053 C  C   . THR   A 1 142 ? 68.09000 37.67700 -10.49400 1.000 16.33000 ? 186 THR   A C   1 
ATOM   1054 O  O   . THR   A 1 142 ? 68.24000 37.53300 -11.71300 1.000 16.42000 ? 186 THR   A O   1 
ATOM   1055 C  CB  . THR   A 1 142 ? 66.74800 35.85500 -9.44400  1.000 16.09000 ? 186 THR   A CB  1 
ATOM   1056 O  OG1 . THR   A 1 142 ? 65.84900 36.79900 -8.85100  1.000 16.12000 ? 186 THR   A OG1 1 
ATOM   1057 C  CG2 . THR   A 1 142 ? 66.80800 34.60800 -8.60000  1.000 15.92000 ? 186 THR   A CG2 1 
ATOM   1058 N  N   . VAL   A 1 143 ? 67.86400 38.86600 -9.93800  1.000 16.39000 ? 187 VAL   A N   1 
ATOM   1059 C  CA  . VAL   A 1 143 ? 67.96200 40.08300 -10.73400 1.000 16.53000 ? 187 VAL   A CA  1 
ATOM   1060 C  C   . VAL   A 1 143 ? 69.40500 40.31000 -11.16800 1.000 16.61000 ? 187 VAL   A C   1 
ATOM   1061 O  O   . VAL   A 1 143 ? 69.66900 40.76000 -12.29100 1.000 16.61000 ? 187 VAL   A O   1 
ATOM   1062 C  CB  . VAL   A 1 143 ? 67.39500 41.27500 -9.93800  1.000 16.87000 ? 187 VAL   A CB  1 
ATOM   1063 C  CG1 . VAL   A 1 143 ? 67.72800 42.58900 -10.61100 1.000 16.27000 ? 187 VAL   A CG1 1 
ATOM   1064 C  CG2 . VAL   A 1 143 ? 65.89300 41.13500 -9.78300  1.000 17.29000 ? 187 VAL   A CG2 1 
ATOM   1065 N  N   . MET   A 1 144 ? 70.36300 39.96300 -10.30400 1.000 16.78000 ? 188 MET   A N   1 
ATOM   1066 C  CA  . MET   A 1 144 ? 71.77400 40.17400 -10.60800 1.000 16.89000 ? 188 MET   A CA  1 
ATOM   1067 C  C   . MET   A 1 144 ? 72.34000 39.09800 -11.52400 1.000 16.74000 ? 188 MET   A C   1 
ATOM   1068 O  O   . MET   A 1 144 ? 73.34400 39.33500 -12.20400 1.000 16.66000 ? 188 MET   A O   1 
ATOM   1069 C  CB  . MET   A 1 144 ? 72.59100 40.22100 -9.31600  1.000 17.63000 ? 188 MET   A CB  1 
ATOM   1070 C  CG  . MET   A 1 144 ? 72.30300 41.41700 -8.43200  1.000 18.27000 ? 188 MET   A CG  1 
ATOM   1071 S  SD  . MET   A 1 144 ? 72.94200 41.19800 -6.76000  1.000 18.43000 ? 188 MET   A SD  1 
ATOM   1072 C  CE  . MET   A 1 144 ? 72.32000 42.68900 -5.99300  1.000 19.91000 ? 188 MET   A CE  1 
ATOM   1073 N  N   . ARG   A 1 145 ? 71.74100 37.91200 -11.54300 1.000 16.87000 ? 189 ARG   A N   1 
ATOM   1074 C  CA  . ARG   A 1 145 ? 72.20900 36.81600 -12.38900 1.000 16.82000 ? 189 ARG   A CA  1 
ATOM   1075 C  C   . ARG   A 1 145 ? 71.01500 36.01600 -12.87600 1.000 16.40000 ? 189 ARG   A C   1 
ATOM   1076 O  O   . ARG   A 1 145 ? 70.67000 34.96800 -12.31500 1.000 16.59000 ? 189 ARG   A O   1 
ATOM   1077 C  CB  . ARG   A 1 145 ? 73.20600 35.92400 -11.65100 1.000 16.86000 ? 189 ARG   A CB  1 
ATOM   1078 C  CG  . ARG   A 1 145 ? 73.81400 34.86600 -12.55100 1.000 16.87000 ? 189 ARG   A CG  1 
ATOM   1079 C  CD  . ARG   A 1 145 ? 75.01400 34.21000 -11.92200 1.000 16.84000 ? 189 ARG   A CD  1 
ATOM   1080 N  NE  . ARG   A 1 145 ? 76.05500 35.18500 -11.63200 1.000 16.87000 ? 189 ARG   A NE  1 
ATOM   1081 C  CZ  . ARG   A 1 145 ? 77.22200 34.88400 -11.08500 1.000 16.80000 ? 189 ARG   A CZ  1 
ATOM   1082 N  NH1 . ARG   A 1 145 ? 77.54700 33.63500 -10.80000 1.000 16.67000 ? 189 ARG   A NH1 1 
ATOM   1083 N  NH2 . ARG   A 1 145 ? 78.08200 35.86100 -10.81700 1.000 16.59000 ? 189 ARG   A NH2 1 
ATOM   1084 N  N   . PRO   A 1 146 ? 70.36400 36.47500 -13.94900 1.000 16.63000 ? 190 PRO   A N   1 
ATOM   1085 C  CA  . PRO   A 1 146 ? 69.17200 35.77900 -14.45300 1.000 16.65000 ? 190 PRO   A CA  1 
ATOM   1086 C  C   . PRO   A 1 146 ? 69.45900 34.41800 -15.06100 1.000 16.69000 ? 190 PRO   A C   1 
ATOM   1087 O  O   . PRO   A 1 146 ? 68.51800 33.76500 -15.52300 1.000 16.54000 ? 190 PRO   A O   1 
ATOM   1088 C  CB  . PRO   A 1 146 ? 68.62700 36.74600 -15.51700 1.000 16.84000 ? 190 PRO   A CB  1 
ATOM   1089 C  CG  . PRO   A 1 146 ? 69.30700 38.05300 -15.26000 1.000 16.69000 ? 190 PRO   A CG  1 
ATOM   1090 C  CD  . PRO   A 1 146 ? 70.64900 37.69900 -14.71600 1.000 16.64000 ? 190 PRO   A CD  1 
ATOM   1091 N  N   . SER   A 1 147 ? 70.71700 33.97200 -15.08500 1.000 16.58000 ? 191 SER   A N   1 
ATOM   1092 C  CA  . SER   A 1 147 ? 71.04300 32.64400 -15.58200 1.000 16.57000 ? 191 SER   A CA  1 
ATOM   1093 C  C   . SER   A 1 147 ? 70.88500 31.55600 -14.53100 1.000 16.71000 ? 191 SER   A C   1 
ATOM   1094 O  O   . SER   A 1 147 ? 71.03200 30.37700 -14.86200 1.000 16.87000 ? 191 SER   A O   1 
ATOM   1095 C  CB  . SER   A 1 147 ? 72.47400 32.61300 -16.13200 1.000 16.27000 ? 191 SER   A CB  1 
ATOM   1096 O  OG  . SER   A 1 147 ? 73.36500 33.36900 -15.33700 1.000 15.75000 ? 191 SER   A OG  1 
ATOM   1097 N  N   . LEU   A 1 148 ? 70.60000 31.91400 -13.28300 1.000 16.55000 ? 192 LEU   A N   1 
ATOM   1098 C  CA  . LEU   A 1 148 ? 70.37500 30.91300 -12.25000 1.000 16.68000 ? 192 LEU   A CA  1 
ATOM   1099 C  C   . LEU   A 1 148 ? 69.12200 30.10300 -12.55600 1.000 16.92000 ? 192 LEU   A C   1 
ATOM   1100 O  O   . LEU   A 1 148 ? 68.17300 30.59400 -13.17100 1.000 16.53000 ? 192 LEU   A O   1 
ATOM   1101 C  CB  . LEU   A 1 148 ? 70.24500 31.58100 -10.88100 1.000 16.54000 ? 192 LEU   A CB  1 
ATOM   1102 C  CG  . LEU   A 1 148 ? 71.48100 32.34000 -10.40000 1.000 16.63000 ? 192 LEU   A CG  1 
ATOM   1103 C  CD1 . LEU   A 1 148 ? 71.16900 33.11600 -9.13000  1.000 15.54000 ? 192 LEU   A CD1 1 
ATOM   1104 C  CD2 . LEU   A 1 148 ? 72.62800 31.37100 -10.18000 1.000 16.92000 ? 192 LEU   A CD2 1 
ATOM   1105 N  N   . LYS   A 1 149 ? 69.12100 28.85000 -12.10200 1.000 16.90000 ? 193 LYS   A N   1 
ATOM   1106 C  CA  . LYS   A 1 149 ? 68.06000 27.90800 -12.44600 1.000 17.15000 ? 193 LYS   A CA  1 
ATOM   1107 C  C   . LYS   A 1 149 ? 66.85900 27.95900 -11.51200 1.000 16.83000 ? 193 LYS   A C   1 
ATOM   1108 O  O   . LYS   A 1 149 ? 65.74000 27.66600 -11.94900 1.000 16.83000 ? 193 LYS   A O   1 
ATOM   1109 C  CB  . LYS   A 1 149 ? 68.61500 26.48300 -12.47200 1.000 17.65000 ? 193 LYS   A CB  1 
ATOM   1110 C  CG  . LYS   A 1 149 ? 69.67400 26.26100 -13.53600 1.000 18.04000 ? 193 LYS   A CG  1 
ATOM   1111 C  CD  . LYS   A 1 149 ? 69.10800 26.51500 -14.91900 1.000 18.67000 ? 193 LYS   A CD  1 
ATOM   1112 C  CE  . LYS   A 1 149 ? 70.18100 26.42200 -15.98800 1.000 18.75000 ? 193 LYS   A CE  1 
ATOM   1113 N  NZ  . LYS   A 1 149 ? 69.64600 26.73200 -17.34600 1.000 20.60000 ? 193 LYS   A NZ  1 
ATOM   1114 N  N   . ALA   A 1 150 ? 67.05000 28.30600 -10.24100 1.000 16.46000 ? 194 ALA   A N   1 
ATOM   1115 C  CA  . ALA   A 1 150 ? 65.93700 28.33800 -9.30300  1.000 16.47000 ? 194 ALA   A CA  1 
ATOM   1116 C  C   . ALA   A 1 150 ? 66.28900 29.25200 -8.14100  1.000 16.22000 ? 194 ALA   A C   1 
ATOM   1117 O  O   . ALA   A 1 150 ? 67.46000 29.51000 -7.86000  1.000 15.93000 ? 194 ALA   A O   1 
ATOM   1118 C  CB  . ALA   A 1 150 ? 65.58000 26.93600 -8.79400  1.000 16.58000 ? 194 ALA   A CB  1 
ATOM   1119 N  N   . SER   A 1 151 ? 65.24800 29.73600 -7.47200  1.000 15.37000 ? 195 SER   A N   1 
ATOM   1120 C  CA  . SER   A 1 151 ? 65.38500 30.66900 -6.36400  1.000 15.45000 ? 195 SER   A CA  1 
ATOM   1121 C  C   . SER   A 1 151 ? 64.31200 30.33200 -5.34000  1.000 14.77000 ? 195 SER   A C   1 
ATOM   1122 O  O   . SER   A 1 151 ? 63.15500 30.12300 -5.71100  1.000 15.45000 ? 195 SER   A O   1 
ATOM   1123 C  CB  . SER   A 1 151 ? 65.24100 32.11100 -6.84900  1.000 15.16000 ? 195 SER   A CB  1 
ATOM   1124 O  OG  . SER   A 1 151 ? 65.45200 33.05700 -5.81600  1.000 15.06000 ? 195 SER   A OG  1 
ATOM   1125 N  N   . ILE   A 1 152 ? 64.69700 30.24600 -4.06800  1.000 14.95000 ? 196 ILE   A N   1 
ATOM   1126 C  CA  . ILE   A 1 152 ? 63.75100 29.88500 -3.01100  1.000 14.99000 ? 196 ILE   A CA  1 
ATOM   1127 C  C   . ILE   A 1 152 ? 63.87200 30.86200 -1.84700  1.000 14.64000 ? 196 ILE   A C   1 
ATOM   1128 O  O   . ILE   A 1 152 ? 64.69600 30.64800 -0.94400  1.000 14.96000 ? 196 ILE   A O   1 
ATOM   1129 C  CB  . ILE   A 1 152 ? 63.96600 28.44600 -2.51700  1.000 14.97000 ? 196 ILE   A CB  1 
ATOM   1130 C  CG1 . ILE   A 1 152 ? 64.06100 27.46300 -3.68500  1.000 15.27000 ? 196 ILE   A CG1 1 
ATOM   1131 C  CG2 . ILE   A 1 152 ? 62.83400 28.04400 -1.59300  1.000 15.13000 ? 196 ILE   A CG2 1 
ATOM   1132 C  CD1 . ILE   A 1 152 ? 64.17300 26.01400 -3.26500  1.000 16.22000 ? 196 ILE   A CD1 1 
ATOM   1133 N  N   . PRO   A 1 153 ? 63.09100 31.94400 -1.82600  1.000 14.80000 ? 197 PRO   A N   1 
ATOM   1134 C  CA  . PRO   A 1 153 ? 63.06300 32.83000 -0.65100  1.000 14.78000 ? 197 PRO   A CA  1 
ATOM   1135 C  C   . PRO   A 1 153 ? 62.17700 32.24800 0.44300   1.000 15.62000 ? 197 PRO   A C   1 
ATOM   1136 O  O   . PRO   A 1 153 ? 60.97300 32.06300 0.25200   1.000 14.72000 ? 197 PRO   A O   1 
ATOM   1137 C  CB  . PRO   A 1 153 ? 62.48500 34.13800 -1.20700  1.000 14.88000 ? 197 PRO   A CB  1 
ATOM   1138 C  CG  . PRO   A 1 153 ? 62.60100 34.01500 -2.70500  1.000 14.90000 ? 197 PRO   A CG  1 
ATOM   1139 C  CD  . PRO   A 1 153 ? 62.43400 32.56400 -2.98600  1.000 14.85000 ? 197 PRO   A CD  1 
ATOM   1140 N  N   . LEU   A 1 154 ? 62.77700 31.96600 1.59800   1.000 14.99000 ? 198 LEU   A N   1 
ATOM   1141 C  CA  . LEU   A 1 154 ? 62.08100 31.39800 2.74800   1.000 15.40000 ? 198 LEU   A CA  1 
ATOM   1142 C  C   . LEU   A 1 154 ? 61.73300 32.51600 3.72000   1.000 16.20000 ? 198 LEU   A C   1 
ATOM   1143 O  O   . LEU   A 1 154 ? 62.62500 33.22700 4.18700   1.000 15.39000 ? 198 LEU   A O   1 
ATOM   1144 C  CB  . LEU   A 1 154 ? 62.94700 30.34800 3.44000   1.000 15.69000 ? 198 LEU   A CB  1 
ATOM   1145 C  CG  . LEU   A 1 154 ? 63.54100 29.26200 2.55700   1.000 15.68000 ? 198 LEU   A CG  1 
ATOM   1146 C  CD1 . LEU   A 1 154 ? 64.84400 28.76500 3.14100   1.000 15.70000 ? 198 LEU   A CD1 1 
ATOM   1147 C  CD2 . LEU   A 1 154 ? 62.55800 28.13000 2.42000   1.000 15.82000 ? 198 LEU   A CD2 1 
ATOM   1148 N  N   . THR   A 1 155 ? 60.44400 32.64100 4.03800   1.000 15.31000 ? 199 THR   A N   1 
ATOM   1149 C  CA  . THR   A 1 155 ? 59.87600 33.73500 4.82200   1.000 15.66000 ? 199 THR   A CA  1 
ATOM   1150 C  C   . THR   A 1 155 ? 60.62000 35.04800 4.53500   1.000 15.59000 ? 199 THR   A C   1 
ATOM   1151 O  O   . THR   A 1 155 ? 61.17900 35.66100 5.44800   1.000 15.70000 ? 199 THR   A O   1 
ATOM   1152 C  CB  . THR   A 1 155 ? 59.87500 33.41300 6.31300   1.000 16.21000 ? 199 THR   A CB  1 
ATOM   1153 O  OG1 . THR   A 1 155 ? 61.21400 33.19500 6.77100   1.000 16.06000 ? 199 THR   A OG1 1 
ATOM   1154 C  CG2 . THR   A 1 155 ? 59.05800 32.15300 6.56300   1.000 16.30000 ? 199 THR   A CG2 1 
ATOM   1155 N  N   . PRO   A 1 156 ? 60.64200 35.49300 3.27900   1.000 15.49000 ? 200 PRO   A N   1 
ATOM   1156 C  CA  . PRO   A 1 156 ? 61.56000 36.56900 2.89600   1.000 15.40000 ? 200 PRO   A CA  1 
ATOM   1157 C  C   . PRO   A 1 156 ? 61.17500 37.90100 3.51000   1.000 16.32000 ? 200 PRO   A C   1 
ATOM   1158 O  O   . PRO   A 1 156 ? 60.00700 38.17400 3.78900   1.000 15.88000 ? 200 PRO   A O   1 
ATOM   1159 C  CB  . PRO   A 1 156 ? 61.43600 36.61200 1.36700   1.000 15.29000 ? 200 PRO   A CB  1 
ATOM   1160 C  CG  . PRO   A 1 156 ? 60.07400 36.10500 1.09000   1.000 15.20000 ? 200 PRO   A CG  1 
ATOM   1161 C  CD  . PRO   A 1 156 ? 59.79200 35.06500 2.15100   1.000 15.28000 ? 200 PRO   A CD  1 
ATOM   1162 N  N   . TRP   A 1 157 ? 62.19000 38.73100 3.71800   1.000 16.16000 ? 201 TRP   A N   1 
ATOM   1163 C  CA  . TRP   A 1 157 ? 62.00900 40.11300 4.12500   1.000 16.58000 ? 201 TRP   A CA  1 
ATOM   1164 C  C   . TRP   A 1 157 ? 62.72600 41.00200 3.12600   1.000 17.32000 ? 201 TRP   A C   1 
ATOM   1165 O  O   . TRP   A 1 157 ? 63.91200 40.80000 2.85500   1.000 16.65000 ? 201 TRP   A O   1 
ATOM   1166 C  CB  . TRP   A 1 157 ? 62.55500 40.37600 5.53600   1.000 17.13000 ? 201 TRP   A CB  1 
ATOM   1167 C  CG  . TRP   A 1 157 ? 62.29600 41.77600 6.00600   1.000 17.55000 ? 201 TRP   A CG  1 
ATOM   1168 C  CD1 . TRP   A 1 157 ? 61.27000 42.19000 6.79600   1.000 17.74000 ? 201 TRP   A CD1 1 
ATOM   1169 C  CD2 . TRP   A 1 157 ? 63.06500 42.94700 5.70000   1.000 17.80000 ? 201 TRP   A CD2 1 
ATOM   1170 N  NE1 . TRP   A 1 157 ? 61.35000 43.54300 7.00600   1.000 17.96000 ? 201 TRP   A NE1 1 
ATOM   1171 C  CE2 . TRP   A 1 157 ? 62.44500 44.03200 6.34600   1.000 18.10000 ? 201 TRP   A CE2 1 
ATOM   1172 C  CE3 . TRP   A 1 157 ? 64.21900 43.18200 4.94800   1.000 17.83000 ? 201 TRP   A CE3 1 
ATOM   1173 C  CZ2 . TRP   A 1 157 ? 62.93800 45.33000 6.26300   1.000 18.31000 ? 201 TRP   A CZ2 1 
ATOM   1174 C  CZ3 . TRP   A 1 157 ? 64.70300 44.47000 4.86300   1.000 17.99000 ? 201 TRP   A CZ3 1 
ATOM   1175 C  CH2 . TRP   A 1 157 ? 64.06500 45.52900 5.51800   1.000 18.21000 ? 201 TRP   A CH2 1 
ATOM   1176 N  N   . HIS   A 1 158 ? 62.00800 41.98200 2.58500   1.000 16.86000 ? 202 HIS   A N   1 
ATOM   1177 C  CA  . HIS   A 1 158 ? 62.60400 43.00100 1.73400   1.000 17.23000 ? 202 HIS   A CA  1 
ATOM   1178 C  C   . HIS   A 1 158 ? 61.74300 44.25200 1.81300   1.000 17.92000 ? 202 HIS   A C   1 
ATOM   1179 O  O   . HIS   A 1 158 ? 60.52300 44.16400 1.95300   1.000 16.87000 ? 202 HIS   A O   1 
ATOM   1180 C  CB  . HIS   A 1 158 ? 62.72600 42.52000 0.28000   1.000 17.19000 ? 202 HIS   A CB  1 
ATOM   1181 C  CG  . HIS   A 1 158 ? 63.90400 43.08800 -0.44500  1.000 17.59000 ? 202 HIS   A CG  1 
ATOM   1182 N  ND1 . HIS   A 1 158 ? 64.16300 44.43900 -0.50100  1.000 17.50000 ? 202 HIS   A ND1 1 
ATOM   1183 C  CD2 . HIS   A 1 158 ? 64.90100 42.48700 -1.13400  1.000 17.23000 ? 202 HIS   A CD2 1 
ATOM   1184 C  CE1 . HIS   A 1 158 ? 65.27000 44.64600 -1.19100  1.000 18.04000 ? 202 HIS   A CE1 1 
ATOM   1185 N  NE2 . HIS   A 1 158 ? 65.73600 43.47800 -1.58900  1.000 17.74000 ? 202 HIS   A NE2 1 
ATOM   1186 N  N   . LEU   A 1 159 ? 62.39000 45.41900 1.72800   1.000 17.53000 ? 203 LEU   A N   1 
ATOM   1187 C  CA  . LEU   A 1 159 ? 61.66200 46.68300 1.68200   1.000 17.67000 ? 203 LEU   A CA  1 
ATOM   1188 C  C   . LEU   A 1 159 ? 61.05900 46.97300 0.31300   1.000 17.49000 ? 203 LEU   A C   1 
ATOM   1189 O  O   . LEU   A 1 159 ? 60.10700 47.75400 0.22400   1.000 17.30000 ? 203 LEU   A O   1 
ATOM   1190 C  CB  . LEU   A 1 159 ? 62.57300 47.85100 2.06600   1.000 17.86000 ? 203 LEU   A CB  1 
ATOM   1191 C  CG  . LEU   A 1 159 ? 63.76000 48.16500 1.15600   1.000 18.10000 ? 203 LEU   A CG  1 
ATOM   1192 C  CD1 . LEU   A 1 159 ? 64.07200 49.64900 1.20200   1.000 18.56000 ? 203 LEU   A CD1 1 
ATOM   1193 C  CD2 . LEU   A 1 159 ? 64.98600 47.33600 1.54000   1.000 18.08000 ? 203 LEU   A CD2 1 
ATOM   1194 N  N   . ASP   A 1 160 ? 61.60000 46.38500 -0.75100  1.000 17.63000 ? 204 ASP   A N   1 
ATOM   1195 C  CA  . ASP   A 1 160 ? 61.11500 46.60200 -2.10800  1.000 17.74000 ? 204 ASP   A CA  1 
ATOM   1196 C  C   . ASP   A 1 160 ? 60.18400 45.46100 -2.49000  1.000 18.09000 ? 204 ASP   A C   1 
ATOM   1197 O  O   . ASP   A 1 160 ? 60.56100 44.28800 -2.39400  1.000 17.45000 ? 204 ASP   A O   1 
ATOM   1198 C  CB  . ASP   A 1 160 ? 62.28000 46.70500 -3.09400  1.000 18.22000 ? 204 ASP   A CB  1 
ATOM   1199 C  CG  . ASP   A 1 160 ? 63.24300 47.82700 -2.74000  1.000 18.68000 ? 204 ASP   A CG  1 
ATOM   1200 O  OD1 . ASP   A 1 160 ? 62.77200 48.90400 -2.31700  1.000 18.70000 ? 204 ASP   A OD1 1 
ATOM   1201 O  OD2 . ASP   A 1 160 ? 64.47000 47.63000 -2.87300  1.000 19.17000 ? 204 ASP   A OD2 1 
ATOM   1202 N  N   . LYS   A 1 161 ? 58.97500 45.80500 -2.92500  1.000 17.77000 ? 205 LYS   A N   1 
ATOM   1203 C  CA  . LYS   A 1 161 ? 57.90200 44.82400 -3.03800  1.000 17.67000 ? 205 LYS   A CA  1 
ATOM   1204 C  C   . LYS   A 1 161 ? 57.64900 44.33400 -4.46100  1.000 17.61000 ? 205 LYS   A C   1 
ATOM   1205 O  O   . LYS   A 1 161 ? 56.83600 43.42300 -4.64100  1.000 17.26000 ? 205 LYS   A O   1 
ATOM   1206 C  CB  . LYS   A 1 161 ? 56.59500 45.40800 -2.47700  1.000 17.63000 ? 205 LYS   A CB  1 
ATOM   1207 C  CG  . LYS   A 1 161 ? 56.74600 46.16600 -1.15500  1.000 17.09000 ? 205 LYS   A CG  1 
ATOM   1208 C  CD  . LYS   A 1 161 ? 57.27900 45.26900 -0.04900  1.000 17.02000 ? 205 LYS   A CD  1 
ATOM   1209 C  CE  . LYS   A 1 161 ? 57.47900 46.04300 1.24300   1.000 16.64000 ? 205 LYS   A CE  1 
ATOM   1210 N  NZ  . LYS   A 1 161 ? 57.98000 45.16900 2.33900   1.000 16.49000 ? 205 LYS   A NZ  1 
ATOM   1211 N  N   . THR   A 1 162 ? 58.31700 44.89800 -5.46500  1.000 17.66000 ? 206 THR   A N   1 
ATOM   1212 C  CA  . THR   A 1 162 ? 58.01900 44.62400 -6.86900  1.000 17.65000 ? 206 THR   A CA  1 
ATOM   1213 C  C   . THR   A 1 162 ? 59.20000 43.92500 -7.53000  1.000 17.61000 ? 206 THR   A C   1 
ATOM   1214 O  O   . THR   A 1 162 ? 60.31500 44.45600 -7.54100  1.000 17.53000 ? 206 THR   A O   1 
ATOM   1215 C  CB  . THR   A 1 162 ? 57.68100 45.91400 -7.61700  1.000 18.10000 ? 206 THR   A CB  1 
ATOM   1216 O  OG1 . THR   A 1 162 ? 56.44200 46.43700 -7.12700  1.000 17.87000 ? 206 THR   A OG1 1 
ATOM   1217 C  CG2 . THR   A 1 162 ? 57.54500 45.63800 -9.10600  1.000 19.18000 ? 206 THR   A CG2 1 
ATOM   1218 N  N   . TRP   A 1 163 ? 58.94200 42.75300 -8.10600  1.000 17.40000 ? 207 TRP   A N   1 
ATOM   1219 C  CA  . TRP   A 1 163 ? 59.95500 41.91100 -8.73400  1.000 17.59000 ? 207 TRP   A CA  1 
ATOM   1220 C  C   . TRP   A 1 163 ? 59.48200 41.44000 -10.10600 1.000 17.76000 ? 207 TRP   A C   1 
ATOM   1221 O  O   . TRP   A 1 163 ? 59.56100 40.26000 -10.45000 1.000 17.75000 ? 207 TRP   A O   1 
ATOM   1222 C  CB  . TRP   A 1 163 ? 60.28800 40.74200 -7.81300  1.000 17.51000 ? 207 TRP   A CB  1 
ATOM   1223 C  CG  . TRP   A 1 163 ? 60.78700 41.24900 -6.51400  1.000 17.31000 ? 207 TRP   A CG  1 
ATOM   1224 C  CD1 . TRP   A 1 163 ? 60.04700 41.53800 -5.41000  1.000 17.28000 ? 207 TRP   A CD1 1 
ATOM   1225 C  CD2 . TRP   A 1 163 ? 62.13700 41.60200 -6.19900  1.000 17.42000 ? 207 TRP   A CD2 1 
ATOM   1226 N  NE1 . TRP   A 1 163 ? 60.85400 42.03100 -4.41500  1.000 17.26000 ? 207 TRP   A NE1 1 
ATOM   1227 C  CE2 . TRP   A 1 163 ? 62.14400 42.07900 -4.87400  1.000 17.39000 ? 207 TRP   A CE2 1 
ATOM   1228 C  CE3 . TRP   A 1 163 ? 63.34200 41.55200 -6.90500  1.000 17.42000 ? 207 TRP   A CE3 1 
ATOM   1229 C  CZ2 . TRP   A 1 163 ? 63.30700 42.50000 -4.24200  1.000 17.47000 ? 207 TRP   A CZ2 1 
ATOM   1230 C  CZ3 . TRP   A 1 163 ? 64.49700 41.96900 -6.27500  1.000 17.28000 ? 207 TRP   A CZ3 1 
ATOM   1231 C  CH2 . TRP   A 1 163 ? 64.47200 42.43700 -4.95700  1.000 17.33000 ? 207 TRP   A CH2 1 
ATOM   1232 N  N   . GLY   A 1 164 ? 58.99100 42.38200 -10.91200 1.000 17.93000 ? 208 GLY   A N   1 
ATOM   1233 C  CA  . GLY   A 1 164 ? 58.39700 42.11400 -12.20400 1.000 18.16000 ? 208 GLY   A CA  1 
ATOM   1234 C  C   . GLY   A 1 164 ? 59.35500 41.77700 -13.32300 1.000 18.42000 ? 208 GLY   A C   1 
ATOM   1235 O  O   . GLY   A 1 164 ? 58.90700 41.50600 -14.44000 1.000 18.31000 ? 208 GLY   A O   1 
ATOM   1236 N  N   . GLN   A 1 165 ? 60.66200 41.78200 -13.06100 1.000 18.42000 ? 209 GLN   A N   1 
ATOM   1237 C  CA  . GLN   A 1 165 ? 61.67200 41.46700 -14.06400 1.000 18.69000 ? 209 GLN   A CA  1 
ATOM   1238 C  C   . GLN   A 1 165 ? 62.43200 40.18600 -13.74100 1.000 17.97000 ? 209 GLN   A C   1 
ATOM   1239 O  O   . GLN   A 1 165 ? 63.51700 39.96000 -14.28100 1.000 17.75000 ? 209 GLN   A O   1 
ATOM   1240 C  CB  . GLN   A 1 165 ? 62.64600 42.63400 -14.20900 1.000 18.98000 ? 209 GLN   A CB  1 
ATOM   1241 C  CG  . GLN   A 1 165 ? 61.97700 43.98000 -14.42200 1.000 21.23000 ? 209 GLN   A CG  1 
ATOM   1242 C  CD  . GLN   A 1 165 ? 61.58900 44.21600 -15.86600 1.000 21.27000 ? 209 GLN   A CD  1 
ATOM   1243 O  OE1 . GLN   A 1 165 ? 62.44400 44.48900 -16.71300 1.000 20.67000 ? 209 GLN   A OE1 1 
ATOM   1244 N  NE2 . GLN   A 1 165 ? 60.29600 44.10900 -16.15700 1.000 22.92000 ? 209 GLN   A NE2 1 
ATOM   1245 N  N   . VAL   A 1 166 ? 61.88900 39.34700 -12.86800 1.000 17.74000 ? 210 VAL   A N   1 
ATOM   1246 C  CA  . VAL   A 1 166 ? 62.56600 38.11700 -12.47100 1.000 17.43000 ? 210 VAL   A CA  1 
ATOM   1247 C  C   . VAL   A 1 166 ? 62.36600 37.06500 -13.55300 1.000 17.35000 ? 210 VAL   A C   1 
ATOM   1248 O  O   . VAL   A 1 166 ? 61.24200 36.83300 -14.01000 1.000 17.25000 ? 210 VAL   A O   1 
ATOM   1249 C  CB  . VAL   A 1 166 ? 62.04900 37.62700 -11.10700 1.000 17.44000 ? 210 VAL   A CB  1 
ATOM   1250 C  CG1 . VAL   A 1 166 ? 62.61700 36.25500 -10.77500 1.000 16.93000 ? 210 VAL   A CG1 1 
ATOM   1251 C  CG2 . VAL   A 1 166 ? 62.40900 38.63100 -10.01600 1.000 17.51000 ? 210 VAL   A CG2 1 
ATOM   1252 N  N   . GLN   A 1 167 ? 63.45900 36.42100 -13.96300 1.000 16.72000 ? 211 GLN   A N   1 
ATOM   1253 C  CA  . GLN   A 1 167 ? 63.41400 35.39000 -14.99100 1.000 16.53000 ? 211 GLN   A CA  1 
ATOM   1254 C  C   . GLN   A 1 167 ? 63.76000 34.01000 -14.45900 1.000 16.10000 ? 211 GLN   A C   1 
ATOM   1255 O  O   . GLN   A 1 167 ? 63.83100 33.05700 -15.24100 1.000 15.78000 ? 211 GLN   A O   1 
ATOM   1256 C  CB  . GLN   A 1 167 ? 64.37100 35.74300 -16.13900 1.000 16.87000 ? 211 GLN   A CB  1 
ATOM   1257 C  CG  . GLN   A 1 167 ? 64.46200 37.22400 -16.40900 1.000 16.91000 ? 211 GLN   A CG  1 
ATOM   1258 C  CD  . GLN   A 1 167 ? 65.26900 37.55700 -17.64600 1.000 17.42000 ? 211 GLN   A CD  1 
ATOM   1259 O  OE1 . GLN   A 1 167 ? 64.89900 38.43600 -18.41000 1.000 20.17000 ? 211 GLN   A OE1 1 
ATOM   1260 N  NE2 . GLN   A 1 167 ? 66.37800 36.86500 -17.84300 1.000 16.96000 ? 211 GLN   A NE2 1 
ATOM   1261 N  N   . VAL   A 1 168 ? 63.97200 33.87400 -13.16000 1.000 15.96000 ? 212 VAL   A N   1 
ATOM   1262 C  CA  . VAL   A 1 168 ? 64.39100 32.61500 -12.55300 1.000 15.65000 ? 212 VAL   A CA  1 
ATOM   1263 C  C   . VAL   A 1 168 ? 63.19200 32.00600 -11.83500 1.000 15.55000 ? 212 VAL   A C   1 
ATOM   1264 O  O   . VAL   A 1 168 ? 62.51700 32.71600 -11.07700 1.000 15.56000 ? 212 VAL   A O   1 
ATOM   1265 C  CB  . VAL   A 1 168 ? 65.56600 32.82800 -11.58400 1.000 15.79000 ? 212 VAL   A CB  1 
ATOM   1266 C  CG1 . VAL   A 1 168 ? 66.04700 31.51000 -11.02300 1.000 15.97000 ? 212 VAL   A CG1 1 
ATOM   1267 C  CG2 . VAL   A 1 168 ? 66.69100 33.53000 -12.30000 1.000 16.04000 ? 212 VAL   A CG2 1 
ATOM   1268 N  N   . PRO   A 1 169 ? 62.87200 30.72600 -12.06900 1.000 15.92000 ? 213 PRO   A N   1 
ATOM   1269 C  CA  . PRO   A 1 169 ? 61.75900 30.09700 -11.34900 1.000 15.57000 ? 213 PRO   A CA  1 
ATOM   1270 C  C   . PRO   A 1 169 ? 61.90600 30.24300 -9.84200  1.000 15.84000 ? 213 PRO   A C   1 
ATOM   1271 O  O   . PRO   A 1 169 ? 62.87300 29.75300 -9.25200  1.000 15.32000 ? 213 PRO   A O   1 
ATOM   1272 C  CB  . PRO   A 1 169 ? 61.84100 28.63200 -11.79300 1.000 16.31000 ? 213 PRO   A CB  1 
ATOM   1273 C  CG  . PRO   A 1 169 ? 62.48800 28.69400 -13.13200 1.000 16.31000 ? 213 PRO   A CG  1 
ATOM   1274 C  CD  . PRO   A 1 169 ? 63.48000 29.81600 -13.05200 1.000 15.83000 ? 213 PRO   A CD  1 
ATOM   1275 N  N   . THR   A 1 170 ? 60.95500 30.93100 -9.21800  1.000 15.46000 ? 214 THR   A N   1 
ATOM   1276 C  CA  . THR   A 1 170 ? 61.05000 31.32000 -7.81700  1.000 15.32000 ? 214 THR   A CA  1 
ATOM   1277 C  C   . THR   A 1 170 ? 59.94900 30.63500 -7.01600  1.000 15.57000 ? 214 THR   A C   1 
ATOM   1278 O  O   . THR   A 1 170 ? 58.78700 30.61800 -7.43500  1.000 15.65000 ? 214 THR   A O   1 
ATOM   1279 C  CB  . THR   A 1 170 ? 60.96600 32.84500 -7.67700  1.000 15.24000 ? 214 THR   A CB  1 
ATOM   1280 O  OG1 . THR   A 1 170 ? 62.17200 33.43800 -8.17800  1.000 15.19000 ? 214 THR   A OG1 1 
ATOM   1281 C  CG2 . THR   A 1 170 ? 60.78800 33.25300 -6.22800  1.000 15.23000 ? 214 THR   A CG2 1 
ATOM   1282 N  N   . PHE   A 1 171 ? 60.32600 30.06200 -5.87100  1.000 15.25000 ? 215 PHE   A N   1 
ATOM   1283 C  CA  . PHE   A 1 171 ? 59.41400 29.39200 -4.94700  1.000 15.97000 ? 215 PHE   A CA  1 
ATOM   1284 C  C   . PHE   A 1 171 ? 59.50600 30.08900 -3.59400  1.000 15.22000 ? 215 PHE   A C   1 
ATOM   1285 O  O   . PHE   A 1 171 ? 60.49200 29.91800 -2.87100  1.000 15.14000 ? 215 PHE   A O   1 
ATOM   1286 C  CB  . PHE   A 1 171 ? 59.76500 27.91200 -4.81900  1.000 15.71000 ? 215 PHE   A CB  1 
ATOM   1287 C  CG  . PHE   A 1 171 ? 58.85700 27.13600 -3.89600  1.000 16.05000 ? 215 PHE   A CG  1 
ATOM   1288 C  CD1 . PHE   A 1 171 ? 57.54600 27.52100 -3.68500  1.000 16.23000 ? 215 PHE   A CD1 1 
ATOM   1289 C  CD2 . PHE   A 1 171 ? 59.33000 26.01000 -3.24400  1.000 16.46000 ? 215 PHE   A CD2 1 
ATOM   1290 C  CE1 . PHE   A 1 171 ? 56.72900 26.79800 -2.84500  1.000 16.28000 ? 215 PHE   A CE1 1 
ATOM   1291 C  CE2 . PHE   A 1 171 ? 58.51600 25.28500 -2.40400  1.000 16.90000 ? 215 PHE   A CE2 1 
ATOM   1292 C  CZ  . PHE   A 1 171 ? 57.21500 25.67800 -2.20700  1.000 16.89000 ? 215 PHE   A CZ  1 
ATOM   1293 N  N   . ILE   A 1 172 ? 58.47600 30.85300 -3.24700  1.000 15.54000 ? 216 ILE   A N   1 
ATOM   1294 C  CA  . ILE   A 1 172 ? 58.43500 31.62100 -2.00800  1.000 15.12000 ? 216 ILE   A CA  1 
ATOM   1295 C  C   . ILE   A 1 172 ? 57.69100 30.81100 -0.95600  1.000 15.88000 ? 216 ILE   A C   1 
ATOM   1296 O  O   . ILE   A 1 172 ? 56.61300 30.27300 -1.22800  1.000 15.40000 ? 216 ILE   A O   1 
ATOM   1297 C  CB  . ILE   A 1 172 ? 57.76300 32.98500 -2.23600  1.000 15.35000 ? 216 ILE   A CB  1 
ATOM   1298 C  CG1 . ILE   A 1 172 ? 58.61800 33.83700 -3.17300  1.000 15.36000 ? 216 ILE   A CG1 1 
ATOM   1299 C  CG2 . ILE   A 1 172 ? 57.50400 33.70500 -0.91800  1.000 15.29000 ? 216 ILE   A CG2 1 
ATOM   1300 C  CD1 . ILE   A 1 172 ? 57.99400 35.15700 -3.51400  1.000 16.16000 ? 216 ILE   A CD1 1 
ATOM   1301 N  N   . ILE   A 1 173 ? 58.26200 30.71300 0.24200   1.000 15.28000 ? 217 ILE   A N   1 
ATOM   1302 C  CA  . ILE   A 1 173 ? 57.60500 30.05000 1.36700   1.000 15.47000 ? 217 ILE   A CA  1 
ATOM   1303 C  C   . ILE   A 1 173 ? 57.33600 31.09400 2.44200   1.000 16.27000 ? 217 ILE   A C   1 
ATOM   1304 O  O   . ILE   A 1 173 ? 58.26300 31.76000 2.91400   1.000 15.42000 ? 217 ILE   A O   1 
ATOM   1305 C  CB  . ILE   A 1 173 ? 58.43800 28.88600 1.92900   1.000 15.57000 ? 217 ILE   A CB  1 
ATOM   1306 C  CG1 . ILE   A 1 173 ? 58.67500 27.83200 0.84700   1.000 15.58000 ? 217 ILE   A CG1 1 
ATOM   1307 C  CG2 . ILE   A 1 173 ? 57.73000 28.26900 3.13900   1.000 16.13000 ? 217 ILE   A CG2 1 
ATOM   1308 C  CD1 . ILE   A 1 173 ? 59.45400 26.62400 1.31800   1.000 15.66000 ? 217 ILE   A CD1 1 
ATOM   1309 N  N   . GLY   A 1 174 ? 56.07000 31.24200 2.81400   1.000 15.78000 ? 218 GLY   A N   1 
ATOM   1310 C  CA  . GLY   A 1 174 ? 55.68000 32.18400 3.83700   1.000 16.37000 ? 218 GLY   A CA  1 
ATOM   1311 C  C   . GLY   A 1 174 ? 55.16000 31.47400 5.06700   1.000 16.83000 ? 218 GLY   A C   1 
ATOM   1312 O  O   . GLY   A 1 174 ? 54.83900 30.28300 5.01300   1.000 16.90000 ? 218 GLY   A O   1 
ATOM   1313 N  N   . ALA   A 1 175 ? 55.07100 32.19000 6.18200   1.000 17.04000 ? 219 ALA   A N   1 
ATOM   1314 C  CA  . ALA   A 1 175 ? 54.62400 31.63100 7.45100   1.000 17.65000 ? 219 ALA   A CA  1 
ATOM   1315 C  C   . ALA   A 1 175 ? 53.36400 32.35700 7.89500   1.000 18.50000 ? 219 ALA   A C   1 
ATOM   1316 O  O   . ALA   A 1 175 ? 53.34700 33.59100 7.95000   1.000 17.35000 ? 219 ALA   A O   1 
ATOM   1317 C  CB  . ALA   A 1 175 ? 55.71700 31.75400 8.51400   1.000 17.54000 ? 219 ALA   A CB  1 
ATOM   1318 N  N   . GLU   A 1 176 ? 52.31600 31.59100 8.21500   1.000 18.27000 ? 220 GLU   A N   1 
ATOM   1319 C  CA  . GLU   A 1 176 ? 51.02800 32.19200 8.55800   1.000 18.65000 ? 220 GLU   A CA  1 
ATOM   1320 C  C   . GLU   A 1 176 ? 51.15300 33.18300 9.71000   1.000 18.40000 ? 220 GLU   A C   1 
ATOM   1321 O  O   . GLU   A 1 176 ? 50.54200 34.25800 9.68400   1.000 18.22000 ? 220 GLU   A O   1 
ATOM   1322 C  CB  . GLU   A 1 176 ? 50.01500 31.10200 8.91000   1.000 19.01000 ? 220 GLU   A CB  1 
ATOM   1323 C  CG  . GLU   A 1 176 ? 48.62900 31.63400 9.20600   1.000 19.60000 ? 220 GLU   A CG  1 
ATOM   1324 C  CD  . GLU   A 1 176 ? 47.69400 30.58400 9.77100   1.000 19.89000 ? 220 GLU   A CD  1 
ATOM   1325 O  OE1 . GLU   A 1 176 ? 48.17500 29.53500 10.25200  1.000 19.51000 ? 220 GLU   A OE1 1 
ATOM   1326 O  OE2 . GLU   A 1 176 ? 46.46900 30.81100 9.72900   1.000 20.11000 ? 220 GLU   A OE2 1 
ATOM   1327 N  N   . LEU   A 1 177 ? 51.93600 32.83900 10.73100  1.000 18.15000 ? 221 LEU   A N   1 
ATOM   1328 C  CA  . LEU   A 1 177 ? 52.06800 33.66100 11.92900  1.000 17.97000 ? 221 LEU   A CA  1 
ATOM   1329 C  C   . LEU   A 1 177 ? 53.37200 34.44600 11.94500  1.000 17.48000 ? 221 LEU   A C   1 
ATOM   1330 O  O   . LEU   A 1 177 ? 53.89600 34.76800 13.01600  1.000 17.44000 ? 221 LEU   A O   1 
ATOM   1331 C  CB  . LEU   A 1 177 ? 51.94600 32.78800 13.17600  1.000 18.14000 ? 221 LEU   A CB  1 
ATOM   1332 C  CG  . LEU   A 1 177 ? 50.65100 31.98000 13.26800  1.000 18.40000 ? 221 LEU   A CG  1 
ATOM   1333 C  CD1 . LEU   A 1 177 ? 50.59300 31.20000 14.56800  1.000 18.07000 ? 221 LEU   A CD1 1 
ATOM   1334 C  CD2 . LEU   A 1 177 ? 49.44200 32.88600 13.13000  1.000 18.84000 ? 221 LEU   A CD2 1 
ATOM   1335 N  N   . ASP   A 1 178 ? 53.91400 34.74900 10.77000  1.000 17.41000 ? 222 ASP   A N   1 
ATOM   1336 C  CA  . ASP   A 1 178 ? 55.08900 35.59900 10.66700  1.000 17.14000 ? 222 ASP   A CA  1 
ATOM   1337 C  C   . ASP   A 1 178 ? 54.66900 37.04000 10.91600  1.000 16.80000 ? 222 ASP   A C   1 
ATOM   1338 O  O   . ASP   A 1 178 ? 53.84700 37.58800 10.17700  1.000 16.79000 ? 222 ASP   A O   1 
ATOM   1339 C  CB  . ASP   A 1 178 ? 55.73100 35.44300 9.28900   1.000 16.82000 ? 222 ASP   A CB  1 
ATOM   1340 C  CG  . ASP   A 1 178 ? 57.14300 35.99000 9.23300   1.000 16.71000 ? 222 ASP   A CG  1 
ATOM   1341 O  OD1 . ASP   A 1 178 ? 57.44400 36.96600 9.94800   1.000 16.71000 ? 222 ASP   A OD1 1 
ATOM   1342 O  OD2 . ASP   A 1 178 ? 57.96300 35.43500 8.47400   1.000 16.60000 ? 222 ASP   A OD2 1 
ATOM   1343 N  N   . THR   A 1 179 ? 55.20600 37.64900 11.97200  1.000 16.72000 ? 223 THR   A N   1 
ATOM   1344 C  CA  . THR   A 1 179 ? 54.95700 39.05600 12.24700  1.000 16.90000 ? 223 THR   A CA  1 
ATOM   1345 C  C   . THR   A 1 179 ? 56.21200 39.90000 12.10400  1.000 17.04000 ? 223 THR   A C   1 
ATOM   1346 O  O   . THR   A 1 179 ? 56.14900 41.11600 12.30300  1.000 16.63000 ? 223 THR   A O   1 
ATOM   1347 C  CB  . THR   A 1 179 ? 54.34700 39.24400 13.64700  1.000 16.92000 ? 223 THR   A CB  1 
ATOM   1348 O  OG1 . THR   A 1 179 ? 55.24000 38.74200 14.65200  1.000 16.83000 ? 223 THR   A OG1 1 
ATOM   1349 C  CG2 . THR   A 1 179 ? 53.00900 38.52600 13.74900  1.000 17.24000 ? 223 THR   A CG2 1 
ATOM   1350 N  N   . ILE   A 1 180 ? 57.33900 39.28900 11.75200  1.000 16.94000 ? 224 ILE   A N   1 
ATOM   1351 C  CA  . ILE   A 1 180 ? 58.56700 40.01900 11.45000  1.000 16.97000 ? 224 ILE   A CA  1 
ATOM   1352 C  C   . ILE   A 1 180 ? 58.65800 40.35300 9.96500   1.000 17.00000 ? 224 ILE   A C   1 
ATOM   1353 O  O   . ILE   A 1 180 ? 59.09500 41.44400 9.58800   1.000 17.05000 ? 224 ILE   A O   1 
ATOM   1354 C  CB  . ILE   A 1 180 ? 59.77900 39.19400 11.92500  1.000 17.15000 ? 224 ILE   A CB  1 
ATOM   1355 C  CG1 . ILE   A 1 180 ? 59.74700 39.06300 13.45100  1.000 17.24000 ? 224 ILE   A CG1 1 
ATOM   1356 C  CG2 . ILE   A 1 180 ? 61.08500 39.82100 11.45700  1.000 17.32000 ? 224 ILE   A CG2 1 
ATOM   1357 C  CD1 . ILE   A 1 180 ? 60.86300 38.24700 14.02400  1.000 17.83000 ? 224 ILE   A CD1 1 
ATOM   1358 N  N   . ALA   A 1 181 ? 58.26000 39.41600 9.11300   1.000 16.84000 ? 225 ALA   A N   1 
ATOM   1359 C  CA  . ALA   A 1 181 ? 58.08700 39.64700 7.68000   1.000 16.88000 ? 225 ALA   A CA  1 
ATOM   1360 C  C   . ALA   A 1 181 ? 56.71000 39.12500 7.30400   1.000 16.75000 ? 225 ALA   A C   1 
ATOM   1361 O  O   . ALA   A 1 181 ? 56.58500 38.06900 6.67400   1.000 16.69000 ? 225 ALA   A O   1 
ATOM   1362 C  CB  . ALA   A 1 181 ? 59.18100 38.95800 6.86400   1.000 16.77000 ? 225 ALA   A CB  1 
ATOM   1363 N  N   . PRO   A 1 182 ? 55.65100 39.82500 7.70900   1.000 17.32000 ? 226 PRO   A N   1 
ATOM   1364 C  CA  . PRO   A 1 182 ? 54.30000 39.30400 7.48700   1.000 17.12000 ? 226 PRO   A CA  1 
ATOM   1365 C  C   . PRO   A 1 182 ? 54.02000 39.12000 6.00200   1.000 17.02000 ? 226 PRO   A C   1 
ATOM   1366 O  O   . PRO   A 1 182 ? 54.36300 39.96800 5.17700   1.000 16.91000 ? 226 PRO   A O   1 
ATOM   1367 C  CB  . PRO   A 1 182 ? 53.39900 40.37100 8.11300   1.000 17.17000 ? 226 PRO   A CB  1 
ATOM   1368 C  CG  . PRO   A 1 182 ? 54.22700 41.60100 8.14400   1.000 17.17000 ? 226 PRO   A CG  1 
ATOM   1369 C  CD  . PRO   A 1 182 ? 55.63900 41.16200 8.32000   1.000 17.04000 ? 226 PRO   A CD  1 
ATOM   1370 N  N   . VAL   A 1 183 ? 53.40400 37.98200 5.67100   1.000 16.98000 ? 227 VAL   A N   1 
ATOM   1371 C  CA  . VAL   A 1 183 ? 53.16700 37.62000 4.27900   1.000 17.02000 ? 227 VAL   A CA  1 
ATOM   1372 C  C   . VAL   A 1 183 ? 52.29700 38.64500 3.57000   1.000 17.22000 ? 227 VAL   A C   1 
ATOM   1373 O  O   . VAL   A 1 183 ? 52.39600 38.79300 2.34800   1.000 17.31000 ? 227 VAL   A O   1 
ATOM   1374 C  CB  . VAL   A 1 183 ? 52.54500 36.21100 4.18700   1.000 17.07000 ? 227 VAL   A CB  1 
ATOM   1375 C  CG1 . VAL   A 1 183 ? 53.45900 35.18800 4.82000   1.000 16.86000 ? 227 VAL   A CG1 1 
ATOM   1376 C  CG2 . VAL   A 1 183 ? 51.18600 36.17800 4.84800   1.000 17.14000 ? 227 VAL   A CG2 1 
ATOM   1377 N  N   . SER   A 1 184 ? 51.45900 39.37800 4.31100   1.000 17.40000 ? 228 SER   A N   1 
ATOM   1378 C  CA  . SER   A 1 184 ? 50.56900 40.34900 3.68600   1.000 17.54000 ? 228 SER   A CA  1 
ATOM   1379 C  C   . SER   A 1 184 ? 51.33300 41.54400 3.12700   1.000 17.57000 ? 228 SER   A C   1 
ATOM   1380 O  O   . SER   A 1 184 ? 50.87700 42.17000 2.16300   1.000 17.89000 ? 228 SER   A O   1 
ATOM   1381 C  CB  . SER   A 1 184 ? 49.49700 40.80500 4.68300   1.000 18.20000 ? 228 SER   A CB  1 
ATOM   1382 O  OG  . SER   A 1 184 ? 50.05300 41.48800 5.79300   1.000 17.08000 ? 228 SER   A OG  1 
ATOM   1383 N  N   . THR   A 1 185 ? 52.49500 41.87100 3.69400   1.000 17.41000 ? 229 THR   A N   1 
ATOM   1384 C  CA  . THR   A 1 185 ? 53.30800 42.96600 3.18400   1.000 17.26000 ? 229 THR   A CA  1 
ATOM   1385 C  C   . THR   A 1 185 ? 54.64900 42.51800 2.62300   1.000 17.11000 ? 229 THR   A C   1 
ATOM   1386 O  O   . THR   A 1 185 ? 55.40300 43.36400 2.13400   1.000 17.04000 ? 229 THR   A O   1 
ATOM   1387 C  CB  . THR   A 1 185 ? 53.55600 44.01200 4.27700   1.000 17.11000 ? 229 THR   A CB  1 
ATOM   1388 O  OG1 . THR   A 1 185 ? 54.20700 43.39000 5.38900   1.000 16.97000 ? 229 THR   A OG1 1 
ATOM   1389 C  CG2 . THR   A 1 185 ? 52.25100 44.62800 4.73600   1.000 17.20000 ? 229 THR   A CG2 1 
ATOM   1390 N  N   . HIS   A 1 186 ? 54.97500 41.22600 2.68300   1.000 17.20000 ? 230 HIS   A N   1 
ATOM   1391 C  CA  . HIS   A 1 186 ? 56.26300 40.74500 2.19800   1.000 16.86000 ? 230 HIS   A CA  1 
ATOM   1392 C  C   . HIS   A 1 186 ? 56.10600 39.60000 1.20300   1.000 16.78000 ? 230 HIS   A C   1 
ATOM   1393 O  O   . HIS   A 1 186 ? 56.11300 39.83400 -0.00700  1.000 16.72000 ? 230 HIS   A O   1 
ATOM   1394 C  CB  . HIS   A 1 186 ? 57.15200 40.32400 3.37400   1.000 16.88000 ? 230 HIS   A CB  1 
ATOM   1395 C  CG  . HIS   A 1 186 ? 57.74200 41.48100 4.11500   1.000 17.26000 ? 230 HIS   A CG  1 
ATOM   1396 N  ND1 . HIS   A 1 186 ? 56.98300 42.33200 4.88700   1.000 16.95000 ? 230 HIS   A ND1 1 
ATOM   1397 C  CD2 . HIS   A 1 186 ? 59.00900 41.95200 4.17100   1.000 17.23000 ? 230 HIS   A CD2 1 
ATOM   1398 C  CE1 . HIS   A 1 186 ? 57.75800 43.27000 5.39800   1.000 17.29000 ? 230 HIS   A CE1 1 
ATOM   1399 N  NE2 . HIS   A 1 186 ? 58.99300 43.06200 4.97900   1.000 17.15000 ? 230 HIS   A NE2 1 
ATOM   1400 N  N   . ALA   A 1 187 ? 55.94200 38.36900 1.69800   1.000 16.75000 ? 231 ALA   A N   1 
ATOM   1401 C  CA  . ALA   A 1 187 ? 55.97700 37.19000 0.83300   1.000 16.63000 ? 231 ALA   A CA  1 
ATOM   1402 C  C   . ALA   A 1 187 ? 54.91200 37.24500 -0.26100  1.000 16.73000 ? 231 ALA   A C   1 
ATOM   1403 O  O   . ALA   A 1 187 ? 55.19800 36.96100 -1.43000  1.000 16.61000 ? 231 ALA   A O   1 
ATOM   1404 C  CB  . ALA   A 1 187 ? 55.81700 35.92300 1.67300   1.000 16.36000 ? 231 ALA   A CB  1 
ATOM   1405 N  N   . LYS   A 1 188 ? 53.66500 37.58400 0.09700   1.000 16.99000 ? 232 LYS   A N   1 
ATOM   1406 C  CA  . LYS   A 1 188 ? 52.61800 37.63900 -0.92500  1.000 17.08000 ? 232 LYS   A CA  1 
ATOM   1407 C  C   . LYS   A 1 188 ? 52.85000 38.76000 -1.93300  1.000 16.91000 ? 232 LYS   A C   1 
ATOM   1408 O  O   . LYS   A 1 188 ? 52.73700 38.49900 -3.14400  1.000 16.97000 ? 232 LYS   A O   1 
ATOM   1409 C  CB  . LYS   A 1 188 ? 51.23600 37.75100 -0.27400  1.000 18.17000 ? 232 LYS   A CB  1 
ATOM   1410 C  CG  . LYS   A 1 188 ? 50.67500 36.48000 0.32500   1.000 18.27000 ? 232 LYS   A CG  1 
ATOM   1411 C  CD  . LYS   A 1 188 ? 49.25400 36.75200 0.79800   1.000 19.23000 ? 232 LYS   A CD  1 
ATOM   1412 C  CE  . LYS   A 1 188 ? 48.59300 35.54300 1.41200   1.000 18.54000 ? 232 LYS   A CE  1 
ATOM   1413 N  NZ  . LYS   A 1 188 ? 47.21200 35.89200 1.85000   1.000 20.47000 ? 232 LYS   A NZ  1 
ATOM   1414 N  N   . PRO   A 1 189 ? 53.14600 40.00700 -1.53400  1.000 16.71000 ? 233 PRO   A N   1 
ATOM   1415 C  CA  . PRO   A 1 189 ? 53.43300 41.03000 -2.55400  1.000 16.52000 ? 233 PRO   A CA  1 
ATOM   1416 C  C   . PRO   A 1 189 ? 54.58100 40.66700 -3.47600  1.000 16.64000 ? 233 PRO   A C   1 
ATOM   1417 O  O   . PRO   A 1 189 ? 54.52300 40.98000 -4.67200  1.000 16.68000 ? 233 PRO   A O   1 
ATOM   1418 C  CB  . PRO   A 1 189 ? 53.75000 42.27600 -1.71600  1.000 16.53000 ? 233 PRO   A CB  1 
ATOM   1419 C  CG  . PRO   A 1 189 ? 52.98100 42.08400 -0.48100  1.000 16.78000 ? 233 PRO   A CG  1 
ATOM   1420 C  CD  . PRO   A 1 189 ? 53.04200 40.61200 -0.19300  1.000 16.90000 ? 233 PRO   A CD  1 
ATOM   1421 N  N   . PHE   A 1 190 ? 55.62700 40.01800 -2.95800  1.000 16.71000 ? 234 PHE   A N   1 
ATOM   1422 C  CA  . PHE   A 1 190 ? 56.72800 39.59900 -3.81900  1.000 16.65000 ? 234 PHE   A CA  1 
ATOM   1423 C  C   . PHE   A 1 190 ? 56.23600 38.63200 -4.88800  1.000 16.81000 ? 234 PHE   A C   1 
ATOM   1424 O  O   . PHE   A 1 190 ? 56.52500 38.80300 -6.07700  1.000 16.87000 ? 234 PHE   A O   1 
ATOM   1425 C  CB  . PHE   A 1 190 ? 57.84300 38.94700 -2.99800  1.000 16.59000 ? 234 PHE   A CB  1 
ATOM   1426 C  CG  . PHE   A 1 190 ? 58.35400 39.79100 -1.86200  1.000 16.61000 ? 234 PHE   A CG  1 
ATOM   1427 C  CD1 . PHE   A 1 190 ? 58.19200 41.16700 -1.85700  1.000 16.74000 ? 234 PHE   A CD1 1 
ATOM   1428 C  CD2 . PHE   A 1 190 ? 59.00500 39.19600 -0.79400  1.000 16.39000 ? 234 PHE   A CD2 1 
ATOM   1429 C  CE1 . PHE   A 1 190 ? 58.66200 41.92900 -0.80600  1.000 16.85000 ? 234 PHE   A CE1 1 
ATOM   1430 C  CE2 . PHE   A 1 190 ? 59.48100 39.95300 0.25400   1.000 16.48000 ? 234 PHE   A CE2 1 
ATOM   1431 C  CZ  . PHE   A 1 190 ? 59.30800 41.32100 0.24800   1.000 16.80000 ? 234 PHE   A CZ  1 
ATOM   1432 N  N   . TYR   A 1 191 ? 55.46800 37.61800 -4.47900  1.000 16.94000 ? 235 TYR   A N   1 
ATOM   1433 C  CA  . TYR   A 1 191 ? 55.05200 36.56900 -5.40700  1.000 17.14000 ? 235 TYR   A CA  1 
ATOM   1434 C  C   . TYR   A 1 191 ? 54.10700 37.10400 -6.47300  1.000 17.22000 ? 235 TYR   A C   1 
ATOM   1435 O  O   . TYR   A 1 191 ? 54.24900 36.78500 -7.65900  1.000 17.37000 ? 235 TYR   A O   1 
ATOM   1436 C  CB  . TYR   A 1 191 ? 54.38300 35.42400 -4.64900  1.000 17.23000 ? 235 TYR   A CB  1 
ATOM   1437 C  CG  . TYR   A 1 191 ? 53.64600 34.48100 -5.56300  1.000 17.43000 ? 235 TYR   A CG  1 
ATOM   1438 C  CD1 . TYR   A 1 191 ? 54.31400 33.45300 -6.20600  1.000 17.23000 ? 235 TYR   A CD1 1 
ATOM   1439 C  CD2 . TYR   A 1 191 ? 52.28400 34.62800 -5.80100  1.000 18.01000 ? 235 TYR   A CD2 1 
ATOM   1440 C  CE1 . TYR   A 1 191 ? 53.65100 32.59800 -7.04700  1.000 17.32000 ? 235 TYR   A CE1 1 
ATOM   1441 C  CE2 . TYR   A 1 191 ? 51.61700 33.77700 -6.64600  1.000 17.80000 ? 235 TYR   A CE2 1 
ATOM   1442 C  CZ  . TYR   A 1 191 ? 52.30500 32.76500 -7.26600  1.000 17.49000 ? 235 TYR   A CZ  1 
ATOM   1443 O  OH  . TYR   A 1 191 ? 51.64600 31.91100 -8.11000  1.000 17.30000 ? 235 TYR   A OH  1 
ATOM   1444 N  N   . GLU   A 1 192 ? 53.10000 37.87400 -6.06000  1.000 17.43000 ? 236 GLU   A N   1 
ATOM   1445 C  CA  . GLU   A 1 192 ? 52.15200 38.42100 -7.01800  1.000 17.56000 ? 236 GLU   A CA  1 
ATOM   1446 C  C   . GLU   A 1 192 ? 52.81200 39.40000 -7.97500  1.000 17.23000 ? 236 GLU   A C   1 
ATOM   1447 O  O   . GLU   A 1 192 ? 52.29700 39.61300 -9.07600  1.000 17.15000 ? 236 GLU   A O   1 
ATOM   1448 C  CB  . GLU   A 1 192 ? 50.99700 39.09900 -6.27900  1.000 18.01000 ? 236 GLU   A CB  1 
ATOM   1449 C  CG  . GLU   A 1 192 ? 50.12600 38.13900 -5.48900  1.000 19.63000 ? 236 GLU   A CG  1 
ATOM   1450 C  CD  . GLU   A 1 192 ? 49.45000 37.11100 -6.37300  1.000 19.61000 ? 236 GLU   A CD  1 
ATOM   1451 O  OE1 . GLU   A 1 192 ? 49.19800 37.42400 -7.55100  1.000 19.22000 ? 236 GLU   A OE1 1 
ATOM   1452 O  OE2 . GLU   A 1 192 ? 49.17700 35.98900 -5.89600  1.000 19.53000 ? 236 GLU   A OE2 1 
ATOM   1453 N  N   . SER   A 1 193 ? 53.93700 39.99800 -7.58000  1.000 16.95000 ? 237 SER   A N   1 
ATOM   1454 C  CA  . SER   A 1 193 ? 54.65400 40.91500 -8.45300  1.000 16.87000 ? 237 SER   A CA  1 
ATOM   1455 C  C   . SER   A 1 193 ? 55.53900 40.18700 -9.45300  1.000 17.01000 ? 237 SER   A C   1 
ATOM   1456 O  O   . SER   A 1 193 ? 55.94300 40.78800 -10.45300 1.000 16.99000 ? 237 SER   A O   1 
ATOM   1457 C  CB  . SER   A 1 193 ? 55.50500 41.88100 -7.62500  1.000 17.16000 ? 237 SER   A CB  1 
ATOM   1458 O  OG  . SER   A 1 193 ? 56.67800 41.24900 -7.14600  1.000 17.05000 ? 237 SER   A OG  1 
ATOM   1459 N  N   . LEU   A 1 194 ? 55.85300 38.92000 -9.19800  1.000 17.20000 ? 238 LEU   A N   1 
ATOM   1460 C  CA  . LEU   A 1 194 ? 56.63300 38.13900 -10.13800 1.000 17.19000 ? 238 LEU   A CA  1 
ATOM   1461 C  C   . LEU   A 1 194 ? 55.88800 38.04800 -11.46900 1.000 17.39000 ? 238 LEU   A C   1 
ATOM   1462 O  O   . LEU   A 1 194 ? 54.65600 38.07500 -11.49900 1.000 17.28000 ? 238 LEU   A O   1 
ATOM   1463 C  CB  . LEU   A 1 194 ? 56.89300 36.74200 -9.58300  1.000 17.27000 ? 238 LEU   A CB  1 
ATOM   1464 C  CG  . LEU   A 1 194 ? 57.89600 36.61700 -8.43800  1.000 17.11000 ? 238 LEU   A CG  1 
ATOM   1465 C  CD1 . LEU   A 1 194 ? 57.98500 35.17800 -7.96400  1.000 16.78000 ? 238 LEU   A CD1 1 
ATOM   1466 C  CD2 . LEU   A 1 194 ? 59.25700 37.11300 -8.87700  1.000 17.14000 ? 238 LEU   A CD2 1 
ATOM   1467 N  N   . PRO   A 1 195 ? 56.60600 37.95700 -12.58500 1.000 17.44000 ? 239 PRO   A N   1 
ATOM   1468 C  CA  . PRO   A 1 195 ? 55.92900 37.85800 -13.88400 1.000 17.67000 ? 239 PRO   A CA  1 
ATOM   1469 C  C   . PRO   A 1 195 ? 54.95500 36.68800 -13.91800 1.000 18.05000 ? 239 PRO   A C   1 
ATOM   1470 O  O   . PRO   A 1 195 ? 55.26600 35.58200 -13.47000 1.000 17.65000 ? 239 PRO   A O   1 
ATOM   1471 C  CB  . PRO   A 1 195 ? 57.08700 37.67100 -14.86900 1.000 17.81000 ? 239 PRO   A CB  1 
ATOM   1472 C  CG  . PRO   A 1 195 ? 58.24700 38.31000 -14.20000 1.000 17.84000 ? 239 PRO   A CG  1 
ATOM   1473 C  CD  . PRO   A 1 195 ? 58.07000 38.02600 -12.73400 1.000 17.63000 ? 239 PRO   A CD  1 
ATOM   1474 N  N   . SER   A 1 196 ? 53.76000 36.95600 -14.44900 1.000 18.28000 ? 240 SER   A N   1 
ATOM   1475 C  CA  . SER   A 1 196 ? 52.72000 35.93900 -14.54800 1.000 18.60000 ? 240 SER   A CA  1 
ATOM   1476 C  C   . SER   A 1 196 ? 53.18400 34.72600 -15.34000 1.000 18.10000 ? 240 SER   A C   1 
ATOM   1477 O  O   . SER   A 1 196 ? 52.69900 33.61300 -15.10900 1.000 17.81000 ? 240 SER   A O   1 
ATOM   1478 C  CB  . SER   A 1 196 ? 51.47400 36.54000 -15.19600 1.000 18.27000 ? 240 SER   A CB  1 
ATOM   1479 O  OG  . SER   A 1 196 ? 51.72700 36.90700 -16.54800 1.000 18.46000 ? 240 SER   A OG  1 
ATOM   1480 N  N   . SER   A 1 197 ? 54.11600 34.92200 -16.27300 1.000 17.94000 ? 241 SER   A N   1 
ATOM   1481 C  CA  . SER   A 1 197 ? 54.61400 33.86000 -17.13500 1.000 17.96000 ? 241 SER   A CA  1 
ATOM   1482 C  C   . SER   A 1 197 ? 55.73500 33.05100 -16.50200 1.000 17.56000 ? 241 SER   A C   1 
ATOM   1483 O  O   . SER   A 1 197 ? 56.04600 31.96300 -16.99400 1.000 17.26000 ? 241 SER   A O   1 
ATOM   1484 C  CB  . SER   A 1 197 ? 55.10500 34.44500 -18.45600 1.000 17.98000 ? 241 SER   A CB  1 
ATOM   1485 O  OG  . SER   A 1 197 ? 56.24500 35.26200 -18.24500 1.000 17.79000 ? 241 SER   A OG  1 
ATOM   1486 N  N   . LEU   A 1 198 ? 56.34900 33.55300 -15.44000 1.000 17.51000 ? 242 LEU   A N   1 
ATOM   1487 C  CA  . LEU   A 1 198 ? 57.43600 32.83300 -14.79900 1.000 17.26000 ? 242 LEU   A CA  1 
ATOM   1488 C  C   . LEU   A 1 198 ? 56.90200 31.57400 -14.12200 1.000 17.58000 ? 242 LEU   A C   1 
ATOM   1489 O  O   . LEU   A 1 198 ? 55.78300 31.58100 -13.60300 1.000 17.07000 ? 242 LEU   A O   1 
ATOM   1490 C  CB  . LEU   A 1 198 ? 58.11700 33.73100 -13.77000 1.000 17.07000 ? 242 LEU   A CB  1 
ATOM   1491 C  CG  . LEU   A 1 198 ? 59.33300 33.20200 -13.01400 1.000 16.60000 ? 242 LEU   A CG  1 
ATOM   1492 C  CD1 . LEU   A 1 198 ? 60.51900 33.07300 -13.95600 1.000 16.41000 ? 242 LEU   A CD1 1 
ATOM   1493 C  CD2 . LEU   A 1 198 ? 59.66100 34.12500 -11.85500 1.000 16.46000 ? 242 LEU   A CD2 1 
ATOM   1494 N  N   . PRO   A 1 199 ? 57.65500 30.47600 -14.13400 1.000 17.01000 ? 243 PRO   A N   1 
ATOM   1495 C  CA  . PRO   A 1 199 ? 57.29400 29.34100 -13.27600 1.000 17.10000 ? 243 PRO   A CA  1 
ATOM   1496 C  C   . PRO   A 1 199 ? 57.50600 29.71800 -11.82000 1.000 16.88000 ? 243 PRO   A C   1 
ATOM   1497 O  O   . PRO   A 1 199 ? 58.63800 29.98500 -11.41400 1.000 16.44000 ? 243 PRO   A O   1 
ATOM   1498 C  CB  . PRO   A 1 199 ? 58.25700 28.23300 -13.71400 1.000 17.20000 ? 243 PRO   A CB  1 
ATOM   1499 C  CG  . PRO   A 1 199 ? 58.77100 28.67500 -15.04800 1.000 17.31000 ? 243 PRO   A CG  1 
ATOM   1500 C  CD  . PRO   A 1 199 ? 58.79800 30.16400 -14.99800 1.000 17.32000 ? 243 PRO   A CD  1 
ATOM   1501 N  N   . LYS   A 1 200 ? 56.43600 29.76700 -11.03100 1.000 16.92000 ? 244 LYS   A N   1 
ATOM   1502 C  CA  . LYS   A 1 200 ? 56.56800 30.25500 -9.66800  1.000 16.88000 ? 244 LYS   A CA  1 
ATOM   1503 C  C   . LYS   A 1 200 ? 55.54700 29.55600 -8.78500  1.000 17.03000 ? 244 LYS   A C   1 
ATOM   1504 O  O   . LYS   A 1 200 ? 54.60100 28.93000 -9.26700  1.000 17.01000 ? 244 LYS   A O   1 
ATOM   1505 C  CB  . LYS   A 1 200 ? 56.40500 31.77900 -9.60700  1.000 17.06000 ? 244 LYS   A CB  1 
ATOM   1506 C  CG  . LYS   A 1 200 ? 55.09300 32.28400 -10.16600 1.000 17.38000 ? 244 LYS   A CG  1 
ATOM   1507 C  CD  . LYS   A 1 200 ? 55.00700 33.78800 -10.10100 1.000 17.62000 ? 244 LYS   A CD  1 
ATOM   1508 C  CE  . LYS   A 1 200 ? 53.58600 34.23200 -10.36000 1.000 17.81000 ? 244 LYS   A CE  1 
ATOM   1509 N  NZ  . LYS   A 1 200 ? 53.36700 35.66300 -10.02300 1.000 17.59000 ? 244 LYS   A NZ  1 
ATOM   1510 N  N   . ALA   A 1 201 ? 55.76300 29.65800 -7.47800  1.000 16.38000 ? 245 ALA   A N   1 
ATOM   1511 C  CA  . ALA   A 1 201 ? 54.84700 29.07600 -6.51200  1.000 17.26000 ? 245 ALA   A CA  1 
ATOM   1512 C  C   . ALA   A 1 201 ? 54.99800 29.82500 -5.19700  1.000 16.57000 ? 245 ALA   A C   1 
ATOM   1513 O  O   . ALA   A 1 201 ? 56.03500 30.43800 -4.93400  1.000 16.12000 ? 245 ALA   A O   1 
ATOM   1514 C  CB  . ALA   A 1 201 ? 55.09800 27.57900 -6.31700  1.000 16.84000 ? 245 ALA   A CB  1 
ATOM   1515 N  N   . TYR   A 1 202 ? 53.93600 29.79200 -4.39600  1.000 16.57000 ? 246 TYR   A N   1 
ATOM   1516 C  CA  . TYR   A 1 202 ? 53.91300 30.38700 -3.06400  1.000 16.61000 ? 246 TYR   A CA  1 
ATOM   1517 C  C   . TYR   A 1 202 ? 53.27500 29.38500 -2.11800  1.000 16.64000 ? 246 TYR   A C   1 
ATOM   1518 O  O   . TYR   A 1 202 ? 52.15000 28.93800 -2.35600  1.000 16.72000 ? 246 TYR   A O   1 
ATOM   1519 C  CB  . TYR   A 1 202 ? 53.12800 31.70000 -3.04700  1.000 16.74000 ? 246 TYR   A CB  1 
ATOM   1520 C  CG  . TYR   A 1 202 ? 52.77600 32.17900 -1.65300  1.000 16.65000 ? 246 TYR   A CG  1 
ATOM   1521 C  CD1 . TYR   A 1 202 ? 53.71700 32.83100 -0.86300  1.000 16.26000 ? 246 TYR   A CD1 1 
ATOM   1522 C  CD2 . TYR   A 1 202 ? 51.50600 31.97300 -1.12400  1.000 16.92000 ? 246 TYR   A CD2 1 
ATOM   1523 C  CE1 . TYR   A 1 202 ? 53.39900 33.26400 0.41900   1.000 16.25000 ? 246 TYR   A CE1 1 
ATOM   1524 C  CE2 . TYR   A 1 202 ? 51.18100 32.40400 0.15200   1.000 16.89000 ? 246 TYR   A CE2 1 
ATOM   1525 C  CZ  . TYR   A 1 202 ? 52.12900 33.04700 0.91800   1.000 16.65000 ? 246 TYR   A CZ  1 
ATOM   1526 O  OH  . TYR   A 1 202 ? 51.80100 33.47600 2.18300   1.000 16.72000 ? 246 TYR   A OH  1 
ATOM   1527 N  N   . MET   A 1 203 ? 53.98700 29.02800 -1.05500  1.000 16.48000 ? 247 MET   A N   1 
ATOM   1528 C  CA  . MET   A 1 203 ? 53.48200 28.08400 -0.06800  1.000 16.52000 ? 247 MET   A CA  1 
ATOM   1529 C  C   . MET   A 1 203 ? 53.46900 28.75400 1.29700   1.000 16.93000 ? 247 MET   A C   1 
ATOM   1530 O  O   . MET   A 1 203 ? 54.49900 29.25500 1.75500   1.000 16.46000 ? 247 MET   A O   1 
ATOM   1531 C  CB  . MET   A 1 203 ? 54.32600 26.81200 -0.03600  1.000 16.50000 ? 247 MET   A CB  1 
ATOM   1532 C  CG  . MET   A 1 203 ? 53.79100 25.76400 0.92100   1.000 16.70000 ? 247 MET   A CG  1 
ATOM   1533 S  SD  . MET   A 1 203 ? 54.69100 24.21500 0.84600   1.000 16.90000 ? 247 MET   A SD  1 
ATOM   1534 C  CE  . MET   A 1 203 ? 56.35200 24.75600 1.18600   1.000 17.45000 ? 247 MET   A CE  1 
ATOM   1535 N  N   . GLU   A 1 204 ? 52.30700 28.76300 1.94300   1.000 16.83000 ? 248 GLU   A N   1 
ATOM   1536 C  CA  . GLU   A 1 204 ? 52.14800 29.36700 3.26100   1.000 17.25000 ? 248 GLU   A CA  1 
ATOM   1537 C  C   . GLU   A 1 204 ? 51.89800 28.26200 4.27600   1.000 17.64000 ? 248 GLU   A C   1 
ATOM   1538 O  O   . GLU   A 1 204 ? 50.91100 27.52700 4.17000   1.000 17.68000 ? 248 GLU   A O   1 
ATOM   1539 C  CB  . GLU   A 1 204 ? 51.00900 30.38400 3.26400   1.000 17.35000 ? 248 GLU   A CB  1 
ATOM   1540 C  CG  . GLU   A 1 204 ? 50.83200 31.12300 4.57700   1.000 17.48000 ? 248 GLU   A CG  1 
ATOM   1541 C  CD  . GLU   A 1 204 ? 49.77600 32.21100 4.49600   1.000 17.41000 ? 248 GLU   A CD  1 
ATOM   1542 O  OE1 . GLU   A 1 204 ? 49.65300 32.85500 3.43400   1.000 17.25000 ? 248 GLU   A OE1 1 
ATOM   1543 O  OE2 . GLU   A 1 204 ? 49.06200 32.42300 5.49500   1.000 18.44000 ? 248 GLU   A OE2 1 
ATOM   1544 N  N   . LEU   A 1 205 ? 52.79600 28.14000 5.24800   1.000 17.57000 ? 249 LEU   A N   1 
ATOM   1545 C  CA  . LEU   A 1 205 ? 52.70000 27.08000 6.24100   1.000 18.00000 ? 249 LEU   A CA  1 
ATOM   1546 C  C   . LEU   A 1 205 ? 51.75400 27.49300 7.36400   1.000 18.26000 ? 249 LEU   A C   1 
ATOM   1547 O  O   . LEU   A 1 205 ? 51.85000 28.60600 7.88900   1.000 18.32000 ? 249 LEU   A O   1 
ATOM   1548 C  CB  . LEU   A 1 205 ? 54.08300 26.76200 6.80100   1.000 17.76000 ? 249 LEU   A CB  1 
ATOM   1549 C  CG  . LEU   A 1 205 ? 55.15100 26.38500 5.77500   1.000 17.45000 ? 249 LEU   A CG  1 
ATOM   1550 C  CD1 . LEU   A 1 205 ? 56.52300 26.46700 6.40600   1.000 17.55000 ? 249 LEU   A CD1 1 
ATOM   1551 C  CD2 . LEU   A 1 205 ? 54.89400 24.99200 5.22600   1.000 18.03000 ? 249 LEU   A CD2 1 
ATOM   1552 N  N   . CYS   A 1 206 ? 50.84300 26.59400 7.72800   1.000 18.38000 ? 250 CYS   A N   1 
ATOM   1553 C  CA  . CYS   A 1 206 ? 49.86300 26.90100 8.76200   1.000 18.64000 ? 250 CYS   A CA  1 
ATOM   1554 C  C   . CYS   A 1 206 ? 50.54300 27.13400 10.10300  1.000 18.66000 ? 250 CYS   A C   1 
ATOM   1555 O  O   . CYS   A 1 206 ? 51.40100 26.35500 10.52500  1.000 18.54000 ? 250 CYS   A O   1 
ATOM   1556 C  CB  . CYS   A 1 206 ? 48.85100 25.76700 8.89600   1.000 18.38000 ? 250 CYS   A CB  1 
ATOM   1557 S  SG  . CYS   A 1 206 ? 47.72300 25.55900 7.52000   1.000 18.14000 ? 250 CYS   A SG  1 
ATOM   1558 N  N   . GLY   A 1 207 ? 50.14800 28.21000 10.77300  1.000 18.61000 ? 251 GLY   A N   1 
ATOM   1559 C  CA  . GLY   A 1 207 ? 50.59900 28.48300 12.12300  1.000 18.11000 ? 251 GLY   A CA  1 
ATOM   1560 C  C   . GLY   A 1 207 ? 52.09400 28.64500 12.29700  1.000 18.75000 ? 251 GLY   A C   1 
ATOM   1561 O  O   . GLY   A 1 207 ? 52.58000 28.66100 13.43200  1.000 20.46000 ? 251 GLY   A O   1 
ATOM   1562 N  N   . ALA   A 1 208 ? 52.83400 28.77700 11.19900  1.000 18.14000 ? 252 ALA   A N   1 
ATOM   1563 C  CA  . ALA   A 1 208 ? 54.28500 28.86300 11.27400  1.000 18.04000 ? 252 ALA   A CA  1 
ATOM   1564 C  C   . ALA   A 1 208 ? 54.73200 30.27800 11.62400  1.000 17.97000 ? 252 ALA   A C   1 
ATOM   1565 O  O   . ALA   A 1 208 ? 54.05500 31.25900 11.31600  1.000 17.86000 ? 252 ALA   A O   1 
ATOM   1566 C  CB  . ALA   A 1 208 ? 54.91600 28.42700 9.95200   1.000 18.11000 ? 252 ALA   A CB  1 
ATOM   1567 N  N   . THR   A 1 209 ? 55.88800 30.37300 12.28100  1.000 17.73000 ? 253 THR   A N   1 
ATOM   1568 C  CA  . THR   A 1 209 ? 56.48400 31.64800 12.64800  1.000 17.63000 ? 253 THR   A CA  1 
ATOM   1569 C  C   . THR   A 1 209 ? 57.60000 31.99800 11.67000  1.000 17.53000 ? 253 THR   A C   1 
ATOM   1570 O  O   . THR   A 1 209 ? 57.97200 31.21500 10.79400  1.000 17.55000 ? 253 THR   A O   1 
ATOM   1571 C  CB  . THR   A 1 209 ? 57.03200 31.61900 14.08200  1.000 17.67000 ? 253 THR   A CB  1 
ATOM   1572 O  OG1 . THR   A 1 209 ? 58.14800 30.72400 14.15600  1.000 18.36000 ? 253 THR   A OG1 1 
ATOM   1573 C  CG2 . THR   A 1 209 ? 55.97000 31.17400 15.07400  1.000 17.62000 ? 253 THR   A CG2 1 
ATOM   1574 N  N   . HIS   A 1 210 ? 58.16400 33.18900 11.85100  1.000 17.35000 ? 254 HIS   A N   1 
ATOM   1575 C  CA  . HIS   A 1 210 ? 59.24400 33.67900 11.00400  1.000 17.51000 ? 254 HIS   A CA  1 
ATOM   1576 C  C   . HIS   A 1 210 ? 60.48700 32.80300 11.05200  1.000 17.64000 ? 254 HIS   A C   1 
ATOM   1577 O  O   . HIS   A 1 210 ? 61.38200 32.97400 10.21700  1.000 17.49000 ? 254 HIS   A O   1 
ATOM   1578 C  CB  . HIS   A 1 210 ? 59.59400 35.09700 11.43600  1.000 17.33000 ? 254 HIS   A CB  1 
ATOM   1579 C  CG  . HIS   A 1 210 ? 60.61000 35.76700 10.57000  1.000 17.10000 ? 254 HIS   A CG  1 
ATOM   1580 N  ND1 . HIS   A 1 210 ? 60.35100 36.13200 9.26700   1.000 16.74000 ? 254 HIS   A ND1 1 
ATOM   1581 C  CD2 . HIS   A 1 210 ? 61.88000 36.15900 10.82700  1.000 17.32000 ? 254 HIS   A CD2 1 
ATOM   1582 C  CE1 . HIS   A 1 210 ? 61.42100 36.71500 8.75700   1.000 16.68000 ? 254 HIS   A CE1 1 
ATOM   1583 N  NE2 . HIS   A 1 210 ? 62.36200 36.74300 9.68300   1.000 16.94000 ? 254 HIS   A NE2 1 
ATOM   1584 N  N   . PHE   A 1 211 ? 60.57500 31.88000 12.00300  1.000 18.03000 ? 255 PHE   A N   1 
ATOM   1585 C  CA  . PHE   A 1 211 ? 61.77400 31.08100 12.18400  1.000 18.57000 ? 255 PHE   A CA  1 
ATOM   1586 C  C   . PHE   A 1 211 ? 61.54000 29.61500 11.86000  1.000 19.00000 ? 255 PHE   A C   1 
ATOM   1587 O  O   . PHE   A 1 211 ? 62.44400 28.79400 12.04700  1.000 18.78000 ? 255 PHE   A O   1 
ATOM   1588 C  CB  . PHE   A 1 211 ? 62.30000 31.25600 13.61000  1.000 19.19000 ? 255 PHE   A CB  1 
ATOM   1589 C  CG  . PHE   A 1 211 ? 62.59800 32.69200 13.96800  1.000 19.01000 ? 255 PHE   A CG  1 
ATOM   1590 C  CD1 . PHE   A 1 211 ? 63.76500 33.29800 13.53700  1.000 19.25000 ? 255 PHE   A CD1 1 
ATOM   1591 C  CD2 . PHE   A 1 211 ? 61.70400 33.43800 14.72100  1.000 19.05000 ? 255 PHE   A CD2 1 
ATOM   1592 C  CE1 . PHE   A 1 211 ? 64.04000 34.61400 13.85500  1.000 19.12000 ? 255 PHE   A CE1 1 
ATOM   1593 C  CE2 . PHE   A 1 211 ? 61.97600 34.75900 15.04100  1.000 19.14000 ? 255 PHE   A CE2 1 
ATOM   1594 C  CZ  . PHE   A 1 211 ? 63.14200 35.34600 14.61000  1.000 19.41000 ? 255 PHE   A CZ  1 
ATOM   1595 N  N   . ALA   A 1 212 ? 60.35100 29.27100 11.37400  1.000 18.25000 ? 256 ALA   A N   1 
ATOM   1596 C  CA  . ALA   A 1 212 ? 60.08300 27.90800 10.92500  1.000 18.30000 ? 256 ALA   A CA  1 
ATOM   1597 C  C   . ALA   A 1 212 ? 61.12300 27.36700 9.94800   1.000 18.19000 ? 256 ALA   A C   1 
ATOM   1598 O  O   . ALA   A 1 212 ? 61.45900 26.17500 10.05300  1.000 18.36000 ? 256 ALA   A O   1 
ATOM   1599 C  CB  . ALA   A 1 212 ? 58.67300 27.84700 10.31800  1.000 18.10000 ? 256 ALA   A CB  1 
ATOM   1600 N  N   . PRO   A 1 213 ? 61.66900 28.14500 9.00400   1.000 18.07000 ? 257 PRO   A N   1 
ATOM   1601 C  CA  . PRO   A 1 213 ? 62.73400 27.60800 8.13900   1.000 17.91000 ? 257 PRO   A CA  1 
ATOM   1602 C  C   . PRO   A 1 213 ? 64.00500 27.20700 8.87600   1.000 18.02000 ? 257 PRO   A C   1 
ATOM   1603 O  O   . PRO   A 1 213 ? 64.85500 26.53200 8.28200   1.000 17.90000 ? 257 PRO   A O   1 
ATOM   1604 C  CB  . PRO   A 1 213 ? 63.00800 28.76200 7.16500   1.000 17.41000 ? 257 PRO   A CB  1 
ATOM   1605 C  CG  . PRO   A 1 213 ? 61.73100 29.50700 7.10700   1.000 17.29000 ? 257 PRO   A CG  1 
ATOM   1606 C  CD  . PRO   A 1 213 ? 61.16000 29.43300 8.48900   1.000 17.81000 ? 257 PRO   A CD  1 
ATOM   1607 N  N   . ASN   A 1 214 ? 64.17300 27.61000 10.13300  1.000 18.16000 ? 258 ASN   A N   1 
ATOM   1608 C  CA  . ASN   A 1 214 ? 65.38900 27.32100 10.87500  1.000 18.30000 ? 258 ASN   A CA  1 
ATOM   1609 C  C   . ASN   A 1 214 ? 65.35300 25.96600 11.57500  1.000 18.51000 ? 258 ASN   A C   1 
ATOM   1610 O  O   . ASN   A 1 214 ? 66.38400 25.52300 12.08700  1.000 18.37000 ? 258 ASN   A O   1 
ATOM   1611 C  CB  . ASN   A 1 214 ? 65.65900 28.42500 11.90700  1.000 18.21000 ? 258 ASN   A CB  1 
ATOM   1612 C  CG  . ASN   A 1 214 ? 65.70700 29.81800 11.28400  1.000 17.73000 ? 258 ASN   A CG  1 
ATOM   1613 O  OD1 . ASN   A 1 214 ? 65.08800 30.75800 11.78300  1.000 17.73000 ? 258 ASN   A OD1 1 
ATOM   1614 N  ND2 . ASN   A 1 214 ? 66.46300 29.95800 10.20100  1.000 17.22000 ? 258 ASN   A ND2 1 
ATOM   1615 N  N   . ILE   A 1 215 ? 64.21100 25.28800 11.61000  1.000 18.83000 ? 259 ILE   A N   1 
ATOM   1616 C  CA  . ILE   A 1 215 ? 64.15200 23.97300 12.24300  1.000 19.19000 ? 259 ILE   A CA  1 
ATOM   1617 C  C   . ILE   A 1 215 ? 63.60900 22.95400 11.25000  1.000 19.37000 ? 259 ILE   A C   1 
ATOM   1618 O  O   . ILE   A 1 215 ? 62.76800 23.30500 10.41200  1.000 19.28000 ? 259 ILE   A O   1 
ATOM   1619 C  CB  . ILE   A 1 215 ? 63.32200 24.00900 13.53600  1.000 19.74000 ? 259 ILE   A CB  1 
ATOM   1620 C  CG1 . ILE   A 1 215 ? 61.94500 24.60500 13.28800  1.000 20.30000 ? 259 ILE   A CG1 1 
ATOM   1621 C  CG2 . ILE   A 1 215 ? 64.03800 24.81800 14.59900  1.000 24.76000 ? 259 ILE   A CG2 1 
ATOM   1622 C  CD1 . ILE   A 1 215 ? 61.13300 24.73600 14.56000  1.000 23.09000 ? 259 ILE   A CD1 1 
ATOM   1623 N  N   . PRO   A 1 216 ? 64.07900 21.70500 11.30200  1.000 19.43000 ? 260 PRO   A N   1 
ATOM   1624 C  CA  . PRO   A 1 216 ? 63.68300 20.69500 10.31200  1.000 19.50000 ? 260 PRO   A CA  1 
ATOM   1625 C  C   . PRO   A 1 216 ? 62.17700 20.64200 10.11000  1.000 19.59000 ? 260 PRO   A C   1 
ATOM   1626 O  O   . PRO   A 1 216 ? 61.39600 20.59900 11.06300  1.000 19.43000 ? 260 PRO   A O   1 
ATOM   1627 C  CB  . PRO   A 1 216 ? 64.22700 19.39200 10.90900  1.000 19.63000 ? 260 PRO   A CB  1 
ATOM   1628 C  CG  . PRO   A 1 216 ? 65.45700 19.82700 11.64600  1.000 19.71000 ? 260 PRO   A CG  1 
ATOM   1629 C  CD  . PRO   A 1 216 ? 65.14300 21.20800 12.19200  1.000 19.21000 ? 260 PRO   A CD  1 
ATOM   1630 N  N   . ASN   A 1 217 ? 61.77700 20.68700 8.84300   1.000 19.73000 ? 261 ASN   A N   1 
ATOM   1631 C  CA  . ASN   A 1 217 ? 60.38000 20.82200 8.44700   1.000 20.20000 ? 261 ASN   A CA  1 
ATOM   1632 C  C   . ASN   A 1 217 ? 60.18500 19.98000 7.19500   1.000 20.19000 ? 261 ASN   A C   1 
ATOM   1633 O  O   . ASN   A 1 217 ? 60.71300 20.31600 6.13200   1.000 19.92000 ? 261 ASN   A O   1 
ATOM   1634 C  CB  . ASN   A 1 217 ? 60.02500 22.28900 8.20000   1.000 19.98000 ? 261 ASN   A CB  1 
ATOM   1635 C  CG  . ASN   A 1 217 ? 58.54200 22.51000 8.01600   1.000 19.77000 ? 261 ASN   A CG  1 
ATOM   1636 O  OD1 . ASN   A 1 217 ? 57.87700 21.79000 7.26900   1.000 19.73000 ? 261 ASN   A OD1 1 
ATOM   1637 N  ND2 . ASN   A 1 217 ? 58.00800 23.51400 8.70100   1.000 18.50000 ? 261 ASN   A ND2 1 
ATOM   1638 N  N   . THR   A 1 218 ? 59.43500 18.88400 7.32600   1.000 20.56000 ? 262 THR   A N   1 
ATOM   1639 C  CA  . THR   A 1 218 ? 59.22000 17.98400 6.19800   1.000 20.97000 ? 262 THR   A CA  1 
ATOM   1640 C  C   . THR   A 1 218 ? 58.48200 18.67900 5.05900   1.000 20.31000 ? 262 THR   A C   1 
ATOM   1641 O  O   . THR   A 1 218 ? 58.83000 18.50300 3.88600   1.000 20.04000 ? 262 THR   A O   1 
ATOM   1642 C  CB  . THR   A 1 218 ? 58.45000 16.75100 6.66700   1.000 21.42000 ? 262 THR   A CB  1 
ATOM   1643 O  OG1 . THR   A 1 218 ? 59.26600 16.00000 7.57500   1.000 21.72000 ? 262 THR   A OG1 1 
ATOM   1644 C  CG2 . THR   A 1 218 ? 58.06500 15.87300 5.49000   1.000 21.54000 ? 262 THR   A CG2 1 
ATOM   1645 N  N   . THR   A 1 219 ? 57.46000 19.47300 5.38700   1.000 20.22000 ? 263 THR   A N   1 
ATOM   1646 C  CA  . THR   A 1 219 ? 56.71300 20.19300 4.36200   1.000 20.10000 ? 263 THR   A CA  1 
ATOM   1647 C  C   . THR   A 1 219 ? 57.61300 21.15500 3.60000   1.000 19.42000 ? 263 THR   A C   1 
ATOM   1648 O  O   . THR   A 1 219 ? 57.47700 21.31000 2.38100   1.000 19.09000 ? 263 THR   A O   1 
ATOM   1649 C  CB  . THR   A 1 219 ? 55.53800 20.93200 5.00200   1.000 20.18000 ? 263 THR   A CB  1 
ATOM   1650 O  OG1 . THR   A 1 219 ? 54.78500 20.01200 5.79700   1.000 19.19000 ? 263 THR   A OG1 1 
ATOM   1651 C  CG2 . THR   A 1 219 ? 54.62200 21.52700 3.94500   1.000 19.61000 ? 263 THR   A CG2 1 
ATOM   1652 N  N   . ILE   A 1 220 ? 58.54600 21.80700 4.29500   1.000 19.35000 ? 264 ILE   A N   1 
ATOM   1653 C  CA  . ILE   A 1 220 ? 59.52400 22.64400 3.60800   1.000 19.11000 ? 264 ILE   A CA  1 
ATOM   1654 C  C   . ILE   A 1 220 ? 60.47200 21.77800 2.78900   1.000 18.92000 ? 264 ILE   A C   1 
ATOM   1655 O  O   . ILE   A 1 220 ? 60.70900 22.03700 1.60400   1.000 18.61000 ? 264 ILE   A O   1 
ATOM   1656 C  CB  . ILE   A 1 220 ? 60.29600 23.51200 4.61600   1.000 19.06000 ? 264 ILE   A CB  1 
ATOM   1657 C  CG1 . ILE   A 1 220 ? 59.37200 24.54900 5.25100   1.000 18.68000 ? 264 ILE   A CG1 1 
ATOM   1658 C  CG2 . ILE   A 1 220 ? 61.50100 24.16800 3.94800   1.000 18.60000 ? 264 ILE   A CG2 1 
ATOM   1659 C  CD1 . ILE   A 1 220 ? 60.06500 25.46200 6.22500   1.000 18.84000 ? 264 ILE   A CD1 1 
ATOM   1660 N  N   . ALA   A 1 221 ? 61.00500 20.72300 3.40900   1.000 19.05000 ? 265 ALA   A N   1 
ATOM   1661 C  CA  . ALA   A 1 221 ? 62.03100 19.90500 2.76900   1.000 19.20000 ? 265 ALA   A CA  1 
ATOM   1662 C  C   . ALA   A 1 221 ? 61.51900 19.24600 1.49000   1.000 19.31000 ? 265 ALA   A C   1 
ATOM   1663 O  O   . ALA   A 1 221 ? 62.19500 19.27000 0.45600   1.000 19.24000 ? 265 ALA   A O   1 
ATOM   1664 C  CB  . ALA   A 1 221 ? 62.53700 18.85100 3.75200   1.000 19.78000 ? 265 ALA   A CB  1 
ATOM   1665 N  N   . LYS   A 1 222 ? 60.32100 18.65400 1.53600   1.000 19.49000 ? 266 LYS   A N   1 
ATOM   1666 C  CA  . LYS   A 1 222 ? 59.84000 17.87900 0.39400   1.000 20.11000 ? 266 LYS   A CA  1 
ATOM   1667 C  C   . LYS   A 1 222 ? 59.65900 18.74100 -0.85100  1.000 19.66000 ? 266 LYS   A C   1 
ATOM   1668 O  O   . LYS   A 1 222 ? 59.86800 18.26200 -1.97200  1.000 20.25000 ? 266 LYS   A O   1 
ATOM   1669 C  CB  . LYS   A 1 222 ? 58.52700 17.17800 0.74800   1.000 20.82000 ? 266 LYS   A CB  1 
ATOM   1670 C  CG  . LYS   A 1 222 ? 57.36600 18.12500 0.98500   1.000 20.38000 ? 266 LYS   A CG  1 
ATOM   1671 C  CD  . LYS   A 1 222 ? 56.14300 17.40700 1.51100   1.000 20.67000 ? 266 LYS   A CD  1 
ATOM   1672 C  CE  . LYS   A 1 222 ? 55.70800 16.29600 0.57500   1.000 21.36000 ? 266 LYS   A CE  1 
ATOM   1673 N  NZ  . LYS   A 1 222 ? 54.49500 15.60000 1.08000   1.000 22.35000 ? 266 LYS   A NZ  1 
ATOM   1674 N  N   . TYR   A 1 223 ? 59.28400 20.01000 -0.68300  1.000 19.18000 ? 267 TYR   A N   1 
ATOM   1675 C  CA  . TYR   A 1 223 ? 59.00400 20.87500 -1.81800  1.000 19.30000 ? 267 TYR   A CA  1 
ATOM   1676 C  C   . TYR   A 1 223 ? 60.17000 21.77700 -2.19300  1.000 18.77000 ? 267 TYR   A C   1 
ATOM   1677 O  O   . TYR   A 1 223 ? 60.22600 22.24700 -3.33200  1.000 18.63000 ? 267 TYR   A O   1 
ATOM   1678 C  CB  . TYR   A 1 223 ? 57.75000 21.71200 -1.53900  1.000 18.82000 ? 267 TYR   A CB  1 
ATOM   1679 C  CG  . TYR   A 1 223 ? 56.50300 20.85500 -1.49700  1.000 18.87000 ? 267 TYR   A CG  1 
ATOM   1680 C  CD1 . TYR   A 1 223 ? 56.23300 19.94900 -2.51600  1.000 19.07000 ? 267 TYR   A CD1 1 
ATOM   1681 C  CD2 . TYR   A 1 223 ? 55.61500 20.92000 -0.42700  1.000 18.95000 ? 267 TYR   A CD2 1 
ATOM   1682 C  CE1 . TYR   A 1 223 ? 55.11200 19.15300 -2.49100  1.000 19.15000 ? 267 TYR   A CE1 1 
ATOM   1683 C  CE2 . TYR   A 1 223 ? 54.47900 20.12000 -0.39300  1.000 19.17000 ? 267 TYR   A CE2 1 
ATOM   1684 C  CZ  . TYR   A 1 223 ? 54.23800 19.23600 -1.43300  1.000 19.07000 ? 267 TYR   A CZ  1 
ATOM   1685 O  OH  . TYR   A 1 223 ? 53.12700 18.42300 -1.43300  1.000 18.88000 ? 267 TYR   A OH  1 
ATOM   1686 N  N   . VAL   A 1 224 ? 61.10100 22.02800 -1.27300  1.000 18.74000 ? 268 VAL   A N   1 
ATOM   1687 C  CA  . VAL   A 1 224 ? 62.38400 22.59300 -1.67300  1.000 18.67000 ? 268 VAL   A CA  1 
ATOM   1688 C  C   . VAL   A 1 224 ? 63.12200 21.61500 -2.57800  1.000 18.90000 ? 268 VAL   A C   1 
ATOM   1689 O  O   . VAL   A 1 224 ? 63.71500 22.00400 -3.59100  1.000 18.77000 ? 268 VAL   A O   1 
ATOM   1690 C  CB  . VAL   A 1 224 ? 63.21500 22.96100 -0.43000  1.000 18.35000 ? 268 VAL   A CB  1 
ATOM   1691 C  CG1 . VAL   A 1 224 ? 64.67000 23.20900 -0.80900  1.000 17.83000 ? 268 VAL   A CG1 1 
ATOM   1692 C  CG2 . VAL   A 1 224 ? 62.63400 24.19100 0.24100   1.000 17.50000 ? 268 VAL   A CG2 1 
ATOM   1693 N  N   . ILE   A 1 225 ? 63.08600 20.32800 -2.23300  1.000 19.41000 ? 269 ILE   A N   1 
ATOM   1694 C  CA  . ILE   A 1 225 ? 63.74200 19.31700 -3.05400  1.000 20.26000 ? 269 ILE   A CA  1 
ATOM   1695 C  C   . ILE   A 1 225 ? 63.02800 19.17100 -4.39600  1.000 20.56000 ? 269 ILE   A C   1 
ATOM   1696 O  O   . ILE   A 1 225 ? 63.66800 18.95600 -5.43200  1.000 20.75000 ? 269 ILE   A O   1 
ATOM   1697 C  CB  . ILE   A 1 225 ? 63.81400 17.98300 -2.28500  1.000 21.26000 ? 269 ILE   A CB  1 
ATOM   1698 C  CG1 . ILE   A 1 225 ? 64.63900 18.14700 -1.01000  1.000 20.32000 ? 269 ILE   A CG1 1 
ATOM   1699 C  CG2 . ILE   A 1 225 ? 64.44600 16.89200 -3.12000  1.000 22.68000 ? 269 ILE   A CG2 1 
ATOM   1700 C  CD1 . ILE   A 1 225 ? 64.60200 16.93400 -0.11600  1.000 21.32000 ? 269 ILE   A CD1 1 
ATOM   1701 N  N   . SER   A 1 226 ? 61.69600 19.27700 -4.40300  1.000 20.32000 ? 270 SER   A N   1 
ATOM   1702 C  CA  . SER   A 1 226 ? 60.96000 19.15700 -5.66000  1.000 20.48000 ? 270 SER   A CA  1 
ATOM   1703 C  C   . SER   A 1 226 ? 61.26300 20.32100 -6.59200  1.000 19.71000 ? 270 SER   A C   1 
ATOM   1704 O  O   . SER   A 1 226 ? 61.48500 20.11900 -7.79100  1.000 19.67000 ? 270 SER   A O   1 
ATOM   1705 C  CB  . SER   A 1 226 ? 59.45800 19.06600 -5.39000  1.000 20.57000 ? 270 SER   A CB  1 
ATOM   1706 O  OG  . SER   A 1 226 ? 59.10400 17.79300 -4.88400  1.000 20.84000 ? 270 SER   A OG  1 
ATOM   1707 N  N   . TRP   A 1 227 ? 61.28100 21.54200 -6.05700  1.000 18.67000 ? 271 TRP   A N   1 
ATOM   1708 C  CA  . TRP   A 1 227 ? 61.58100 22.71400 -6.87100  1.000 18.14000 ? 271 TRP   A CA  1 
ATOM   1709 C  C   . TRP   A 1 227 ? 62.99100 22.64800 -7.43500  1.000 18.28000 ? 271 TRP   A C   1 
ATOM   1710 O  O   . TRP   A 1 227 ? 63.22400 23.02400 -8.58900  1.000 18.21000 ? 271 TRP   A O   1 
ATOM   1711 C  CB  . TRP   A 1 227 ? 61.40300 23.98200 -6.03900  1.000 17.34000 ? 271 TRP   A CB  1 
ATOM   1712 C  CG  . TRP   A 1 227 ? 61.25400 25.22400 -6.85000  1.000 16.71000 ? 271 TRP   A CG  1 
ATOM   1713 C  CD1 . TRP   A 1 227 ? 62.21900 26.14900 -7.12800  1.000 16.38000 ? 271 TRP   A CD1 1 
ATOM   1714 C  CD2 . TRP   A 1 227 ? 60.06200 25.68100 -7.49500  1.000 16.45000 ? 271 TRP   A CD2 1 
ATOM   1715 N  NE1 . TRP   A 1 227 ? 61.69700 27.15600 -7.90200  1.000 16.04000 ? 271 TRP   A NE1 1 
ATOM   1716 C  CE2 . TRP   A 1 227 ? 60.37400 26.89000 -8.14100  1.000 16.39000 ? 271 TRP   A CE2 1 
ATOM   1717 C  CE3 . TRP   A 1 227 ? 58.75600 25.18200 -7.58600  1.000 16.92000 ? 271 TRP   A CE3 1 
ATOM   1718 C  CZ2 . TRP   A 1 227 ? 59.43000 27.60900 -8.87000  1.000 16.20000 ? 271 TRP   A CZ2 1 
ATOM   1719 C  CZ3 . TRP   A 1 227 ? 57.82500 25.89500 -8.30900  1.000 16.67000 ? 271 TRP   A CZ3 1 
ATOM   1720 C  CH2 . TRP   A 1 227 ? 58.16500 27.09400 -8.94300  1.000 16.58000 ? 271 TRP   A CH2 1 
ATOM   1721 N  N   . LEU   A 1 228 ? 63.94800 22.17800 -6.63200  1.000 18.60000 ? 272 LEU   A N   1 
ATOM   1722 C  CA  . LEU   A 1 228 ? 65.33200 22.11900 -7.08700  1.000 18.75000 ? 272 LEU   A CA  1 
ATOM   1723 C  C   . LEU   A 1 228 ? 65.51900 21.04300 -8.14700  1.000 18.96000 ? 272 LEU   A C   1 
ATOM   1724 O  O   . LEU   A 1 228 ? 66.20300 21.26600 -9.15000  1.000 18.93000 ? 272 LEU   A O   1 
ATOM   1725 C  CB  . LEU   A 1 228 ? 66.26400 21.88000 -5.90100  1.000 18.84000 ? 272 LEU   A CB  1 
ATOM   1726 C  CG  . LEU   A 1 228 ? 66.41400 23.05800 -4.93700  1.000 18.72000 ? 272 LEU   A CG  1 
ATOM   1727 C  CD1 . LEU   A 1 228 ? 67.37400 22.71100 -3.80800  1.000 18.45000 ? 272 LEU   A CD1 1 
ATOM   1728 C  CD2 . LEU   A 1 228 ? 66.87400 24.30200 -5.67500  1.000 18.31000 ? 272 LEU   A CD2 1 
ATOM   1729 N  N   . LYS   A 1 229 ? 64.91900 19.86900 -7.94700  1.000 19.57000 ? 273 LYS   A N   1 
ATOM   1730 C  CA  . LYS   A 1 229 ? 64.98400 18.83900 -8.97700  1.000 20.03000 ? 273 LYS   A CA  1 
ATOM   1731 C  C   . LYS   A 1 229 ? 64.31900 19.31000 -10.26300 1.000 19.56000 ? 273 LYS   A C   1 
ATOM   1732 O  O   . LYS   A 1 229 ? 64.87300 19.13700 -11.35600 1.000 19.69000 ? 273 LYS   A O   1 
ATOM   1733 C  CB  . LYS   A 1 229 ? 64.33500 17.55100 -8.47900  1.000 21.07000 ? 273 LYS   A CB  1 
ATOM   1734 C  CG  . LYS   A 1 229 ? 65.17500 16.75300 -7.49500  1.000 21.42000 ? 273 LYS   A CG  1 
ATOM   1735 C  CD  . LYS   A 1 229 ? 66.18100 15.87600 -8.20800  1.000 21.44000 ? 273 LYS   A CD  1 
ATOM   1736 C  CE  . LYS   A 1 229 ? 66.54900 14.66400 -7.37000  1.000 22.32000 ? 273 LYS   A CE  1 
ATOM   1737 N  NZ  . LYS   A 1 229 ? 67.66300 13.87900 -7.97100  1.000 21.25000 ? 273 LYS   A NZ  1 
ATOM   1738 N  N   . ARG   A 1 230 ? 63.14400 19.93700 -10.15000 1.000 19.36000 ? 274 ARG   A N   1 
ATOM   1739 C  CA  . ARG   A 1 230 ? 62.38000 20.32000 -11.33400 1.000 19.42000 ? 274 ARG   A CA  1 
ATOM   1740 C  C   . ARG   A 1 230 ? 63.09000 21.38100 -12.16900 1.000 19.19000 ? 274 ARG   A C   1 
ATOM   1741 O  O   . ARG   A 1 230 ? 62.99800 21.35200 -13.39800 1.000 19.38000 ? 274 ARG   A O   1 
ATOM   1742 C  CB  . ARG   A 1 230 ? 60.98900 20.80800 -10.92100 1.000 19.33000 ? 274 ARG   A CB  1 
ATOM   1743 C  CG  . ARG   A 1 230 ? 60.12700 21.30600 -12.07200 1.000 19.61000 ? 274 ARG   A CG  1 
ATOM   1744 C  CD  . ARG   A 1 230 ? 60.00300 20.26300 -13.17500 1.000 19.88000 ? 274 ARG   A CD  1 
ATOM   1745 N  NE  . ARG   A 1 230 ? 59.47600 20.84300 -14.40500 1.000 19.78000 ? 274 ARG   A NE  1 
ATOM   1746 C  CZ  . ARG   A 1 230 ? 60.20400 21.50900 -15.29200 1.000 19.49000 ? 274 ARG   A CZ  1 
ATOM   1747 N  NH1 . ARG   A 1 230 ? 61.50200 21.69500 -15.12100 1.000 19.55000 ? 274 ARG   A NH1 1 
ATOM   1748 N  NH2 . ARG   A 1 230 ? 59.61500 22.00000 -16.37800 1.000 21.03000 ? 274 ARG   A NH2 1 
ATOM   1749 N  N   . PHE   A 1 231 ? 63.80700 22.31400 -11.54300 1.000 18.92000 ? 275 PHE   A N   1 
ATOM   1750 C  CA  . PHE   A 1 231 ? 64.38100 23.42700 -12.29100 1.000 18.68000 ? 275 PHE   A CA  1 
ATOM   1751 C  C   . PHE   A 1 231 ? 65.89900 23.42300 -12.36800 1.000 18.69000 ? 275 PHE   A C   1 
ATOM   1752 O  O   . PHE   A 1 231 ? 66.44500 23.87500 -13.37400 1.000 18.61000 ? 275 PHE   A O   1 
ATOM   1753 C  CB  . PHE   A 1 231 ? 63.90000 24.76100 -11.70600 1.000 18.26000 ? 275 PHE   A CB  1 
ATOM   1754 C  CG  . PHE   A 1 231 ? 62.42500 24.97200 -11.86400 1.000 18.02000 ? 275 PHE   A CG  1 
ATOM   1755 C  CD1 . PHE   A 1 231 ? 61.89100 25.30300 -13.09900 1.000 18.15000 ? 275 PHE   A CD1 1 
ATOM   1756 C  CD2 . PHE   A 1 231 ? 61.56400 24.80200 -10.79400 1.000 17.83000 ? 275 PHE   A CD2 1 
ATOM   1757 C  CE1 . PHE   A 1 231 ? 60.53500 25.48200 -13.26000 1.000 18.18000 ? 275 PHE   A CE1 1 
ATOM   1758 C  CE2 . PHE   A 1 231 ? 60.20300 24.97600 -10.94900 1.000 17.59000 ? 275 PHE   A CE2 1 
ATOM   1759 C  CZ  . PHE   A 1 231 ? 59.68600 25.31600 -12.18400 1.000 17.68000 ? 275 PHE   A CZ  1 
ATOM   1760 N  N   . VAL   A 1 232 ? 66.60100 22.92900 -11.34800 1.000 18.75000 ? 276 VAL   A N   1 
ATOM   1761 C  CA  . VAL   A 1 232 ? 68.05300 22.81300 -11.45600 1.000 18.97000 ? 276 VAL   A CA  1 
ATOM   1762 C  C   . VAL   A 1 232 ? 68.43800 21.58000 -12.26900 1.000 19.19000 ? 276 VAL   A C   1 
ATOM   1763 O  O   . VAL   A 1 232 ? 69.40500 21.60600 -13.03900 1.000 19.12000 ? 276 VAL   A O   1 
ATOM   1764 C  CB  . VAL   A 1 232 ? 68.68900 22.80900 -10.05200 1.000 19.10000 ? 276 VAL   A CB  1 
ATOM   1765 C  CG1 . VAL   A 1 232 ? 70.12300 22.34000 -10.09700 1.000 18.96000 ? 276 VAL   A CG1 1 
ATOM   1766 C  CG2 . VAL   A 1 232 ? 68.61700 24.19400 -9.46600  1.000 18.43000 ? 276 VAL   A CG2 1 
ATOM   1767 N  N   . ASP   A 1 233 ? 67.68400 20.49400 -12.12800 1.000 19.34000 ? 277 ASP   A N   1 
ATOM   1768 C  CA  . ASP   A 1 233 ? 67.92700 19.26900 -12.87500 1.000 19.93000 ? 277 ASP   A CA  1 
ATOM   1769 C  C   . ASP   A 1 233 ? 66.96700 19.09400 -14.04100 1.000 20.30000 ? 277 ASP   A C   1 
ATOM   1770 O  O   . ASP   A 1 233 ? 67.06300 18.09100 -14.75800 1.000 20.89000 ? 277 ASP   A O   1 
ATOM   1771 C  CB  . ASP   A 1 233 ? 67.82500 18.05000 -11.95400 1.000 19.98000 ? 277 ASP   A CB  1 
ATOM   1772 C  CG  . ASP   A 1 233 ? 68.90000 18.02800 -10.87900 1.000 19.39000 ? 277 ASP   A CG  1 
ATOM   1773 O  OD1 . ASP   A 1 233 ? 69.71600 18.97000 -10.80200 1.000 19.20000 ? 277 ASP   A OD1 1 
ATOM   1774 O  OD2 . ASP   A 1 233 ? 68.93200 17.05100 -10.10700 1.000 19.43000 ? 277 ASP   A OD2 1 
ATOM   1775 N  N   . GLU   A 1 234 ? 66.03900 20.03300 -14.23700 1.000 20.15000 ? 278 GLU   A N   1 
ATOM   1776 C  CA  . GLU   A 1 234 ? 65.04200 19.94100 -15.30400 1.000 20.48000 ? 278 GLU   A CA  1 
ATOM   1777 C  C   . GLU   A 1 234 ? 64.26800 18.62900 -15.21600 1.000 20.32000 ? 278 GLU   A C   1 
ATOM   1778 O  O   . GLU   A 1 234 ? 63.80600 18.08800 -16.22400 1.000 20.49000 ? 278 GLU   A O   1 
ATOM   1779 C  CB  . GLU   A 1 234 ? 65.69300 20.10600 -16.68200 1.000 21.23000 ? 278 GLU   A CB  1 
ATOM   1780 C  CG  . GLU   A 1 234 ? 66.38500 21.45400 -16.88900 1.000 21.39000 ? 278 GLU   A CG  1 
ATOM   1781 C  CD  . GLU   A 1 234 ? 67.29300 21.47800 -18.10800 1.000 22.94000 ? 278 GLU   A CD  1 
ATOM   1782 O  OE1 . GLU   A 1 234 ? 67.11200 20.63200 -19.01200 1.000 25.05000 ? 278 GLU   A OE1 1 
ATOM   1783 O  OE2 . GLU   A 1 234 ? 68.19400 22.34000 -18.16200 1.000 23.20000 ? 278 GLU   A OE2 1 
ATOM   1784 N  N   . ASP   A 1 235 ? 64.11600 18.11700 -13.99700 1.000 20.28000 ? 279 ASP   A N   1 
ATOM   1785 C  CA  . ASP   A 1 235 ? 63.61400 16.76600 -13.76000 1.000 20.62000 ? 279 ASP   A CA  1 
ATOM   1786 C  C   . ASP   A 1 235 ? 62.09500 16.82400 -13.66100 1.000 20.50000 ? 279 ASP   A C   1 
ATOM   1787 O  O   . ASP   A 1 235 ? 61.54100 17.21200 -12.63200 1.000 20.37000 ? 279 ASP   A O   1 
ATOM   1788 C  CB  . ASP   A 1 235 ? 64.25200 16.19200 -12.50000 1.000 20.85000 ? 279 ASP   A CB  1 
ATOM   1789 C  CG  . ASP   A 1 235 ? 64.13200 14.69500 -12.41700 1.000 21.38000 ? 279 ASP   A CG  1 
ATOM   1790 O  OD1 . ASP   A 1 235 ? 63.09000 14.16200 -12.82600 1.000 21.19000 ? 279 ASP   A OD1 1 
ATOM   1791 O  OD2 . ASP   A 1 235 ? 65.08700 14.05000 -11.94000 1.000 21.34000 ? 279 ASP   A OD2 1 
ATOM   1792 N  N   . THR   A 1 236 ? 61.41200 16.43000 -14.73200 1.000 20.54000 ? 280 THR   A N   1 
ATOM   1793 C  CA  . THR   A 1 236 ? 59.95600 16.48500 -14.75400 1.000 20.51000 ? 280 THR   A CA  1 
ATOM   1794 C  C   . THR   A 1 236 ? 59.30200 15.33200 -13.99900 1.000 20.24000 ? 280 THR   A C   1 
ATOM   1795 O  O   . THR   A 1 236 ? 58.06900 15.29800 -13.89700 1.000 20.01000 ? 280 THR   A O   1 
ATOM   1796 C  CB  . THR   A 1 236 ? 59.45600 16.51900 -16.20100 1.000 20.71000 ? 280 THR   A CB  1 
ATOM   1797 O  OG1 . THR   A 1 236 ? 60.07300 15.46300 -16.94600 1.000 20.10000 ? 280 THR   A OG1 1 
ATOM   1798 C  CG2 . THR   A 1 236 ? 59.80100 17.85600 -16.84800 1.000 20.80000 ? 280 THR   A CG2 1 
ATOM   1799 N  N   . ARG   A 1 237 ? 60.08700 14.39000 -13.46900 1.000 20.34000 ? 281 ARG   A N   1 
ATOM   1800 C  CA  . ARG   A 1 237 ? 59.54200 13.39500 -12.55300 1.000 20.42000 ? 281 ARG   A CA  1 
ATOM   1801 C  C   . ARG   A 1 237 ? 59.04500 14.02000 -11.26100 1.000 20.10000 ? 281 ARG   A C   1 
ATOM   1802 O  O   . ARG   A 1 237 ? 58.34200 13.35200 -10.49700 1.000 19.80000 ? 281 ARG   A O   1 
ATOM   1803 C  CB  . ARG   A 1 237 ? 60.59400 12.34200 -12.21500 1.000 20.55000 ? 281 ARG   A CB  1 
ATOM   1804 C  CG  . ARG   A 1 237 ? 61.15400 11.60500 -13.40400 1.000 21.00000 ? 281 ARG   A CG  1 
ATOM   1805 C  CD  . ARG   A 1 237 ? 62.24100 10.65500 -12.96200 1.000 21.52000 ? 281 ARG   A CD  1 
ATOM   1806 N  NE  . ARG   A 1 237 ? 63.40800 11.35700 -12.43900 1.000 22.06000 ? 281 ARG   A NE  1 
ATOM   1807 C  CZ  . ARG   A 1 237 ? 64.41800 10.76100 -11.82100 1.000 22.60000 ? 281 ARG   A CZ  1 
ATOM   1808 N  NH1 . ARG   A 1 237 ? 64.41700 9.45700  -11.59800 1.000 22.94000 ? 281 ARG   A NH1 1 
ATOM   1809 N  NH2 . ARG   A 1 237 ? 65.45300 11.49000 -11.41600 1.000 22.35000 ? 281 ARG   A NH2 1 
ATOM   1810 N  N   . TYR   A 1 238 ? 59.40100 15.27700 -10.99900 1.000 20.21000 ? 282 TYR   A N   1 
ATOM   1811 C  CA  . TYR   A 1 238 ? 59.01100 15.98300 -9.78900  1.000 20.42000 ? 282 TYR   A CA  1 
ATOM   1812 C  C   . TYR   A 1 238 ? 57.94300 17.03600 -10.04600 1.000 19.80000 ? 282 TYR   A C   1 
ATOM   1813 O  O   . TYR   A 1 238 ? 57.62400 17.81500 -9.14300  1.000 19.59000 ? 282 TYR   A O   1 
ATOM   1814 C  CB  . TYR   A 1 238 ? 60.24400 16.60900 -9.14500  1.000 21.46000 ? 282 TYR   A CB  1 
ATOM   1815 C  CG  . TYR   A 1 238 ? 61.19600 15.57000 -8.61800  1.000 22.03000 ? 282 TYR   A CG  1 
ATOM   1816 C  CD1 . TYR   A 1 238 ? 62.18900 15.02800 -9.42200  1.000 21.94000 ? 282 TYR   A CD1 1 
ATOM   1817 C  CD2 . TYR   A 1 238 ? 61.08200 15.10300 -7.31800  1.000 22.38000 ? 282 TYR   A CD2 1 
ATOM   1818 C  CE1 . TYR   A 1 238 ? 63.05700 14.06600 -8.93500  1.000 22.50000 ? 282 TYR   A CE1 1 
ATOM   1819 C  CE2 . TYR   A 1 238 ? 61.94400 14.14900 -6.82300  1.000 23.25000 ? 282 TYR   A CE2 1 
ATOM   1820 C  CZ  . TYR   A 1 238 ? 62.92400 13.63000 -7.63200  1.000 23.06000 ? 282 TYR   A CZ  1 
ATOM   1821 O  OH  . TYR   A 1 238 ? 63.77000 12.67600 -7.12600  1.000 22.76000 ? 282 TYR   A OH  1 
ATOM   1822 N  N   . SER   A 1 239 ? 57.38600 17.08400 -11.25800 1.000 19.68000 ? 283 SER   A N   1 
ATOM   1823 C  CA  . SER   A 1 239 ? 56.24200 17.95300 -11.51300 1.000 19.44000 ? 283 SER   A CA  1 
ATOM   1824 C  C   . SER   A 1 239 ? 54.98600 17.44700 -10.81900 1.000 19.25000 ? 283 SER   A C   1 
ATOM   1825 O  O   . SER   A 1 239 ? 54.13600 18.25100 -10.42100 1.000 18.81000 ? 283 SER   A O   1 
ATOM   1826 C  CB  . SER   A 1 239 ? 55.99800 18.07200 -13.01400 1.000 19.38000 ? 283 SER   A CB  1 
ATOM   1827 O  OG  . SER   A 1 239 ? 56.97100 18.90300 -13.61800 1.000 19.32000 ? 283 SER   A OG  1 
ATOM   1828 N  N   . GLN   A 1 240 ? 54.85500 16.12600 -10.67400 1.000 19.22000 ? 284 GLN   A N   1 
ATOM   1829 C  CA  . GLN   A 1 240 ? 53.68300 15.53700 -10.03400 1.000 19.11000 ? 284 GLN   A CA  1 
ATOM   1830 C  C   . GLN   A 1 240 ? 53.48500 16.07600 -8.62500  1.000 18.98000 ? 284 GLN   A C   1 
ATOM   1831 O  O   . GLN   A 1 240 ? 52.34900 16.22200 -8.15800  1.000 18.63000 ? 284 GLN   A O   1 
ATOM   1832 C  CB  . GLN   A 1 240 ? 53.83400 14.02000 -9.99500  1.000 19.65000 ? 284 GLN   A CB  1 
ATOM   1833 C  CG  . GLN   A 1 240 ? 55.18500 13.56900 -9.46400  1.000 19.84000 ? 284 GLN   A CG  1 
ATOM   1834 C  CD  . GLN   A 1 240 ? 55.28900 12.07100 -9.30700  1.000 19.86000 ? 284 GLN   A CD  1 
ATOM   1835 O  OE1 . GLN   A 1 240 ? 54.30700 11.39800 -9.00000  1.000 18.55000 ? 284 GLN   A OE1 1 
ATOM   1836 N  NE2 . GLN   A 1 240 ? 56.48500 11.53800 -9.51300  1.000 20.26000 ? 284 GLN   A NE2 1 
ATOM   1837 N  N   . PHE   A 1 241 ? 54.58300 16.35600 -7.92600  1.000 19.19000 ? 285 PHE   A N   1 
ATOM   1838 C  CA  . PHE   A 1 241 ? 54.49900 16.87100 -6.56900  1.000 19.13000 ? 285 PHE   A CA  1 
ATOM   1839 C  C   . PHE   A 1 241 ? 54.14700 18.34800 -6.54900  1.000 18.47000 ? 285 PHE   A C   1 
ATOM   1840 O  O   . PHE   A 1 241 ? 53.52600 18.82200 -5.59200  1.000 17.89000 ? 285 PHE   A O   1 
ATOM   1841 C  CB  . PHE   A 1 241 ? 55.82500 16.65100 -5.84900  1.000 19.94000 ? 285 PHE   A CB  1 
ATOM   1842 C  CG  . PHE   A 1 241 ? 56.33400 15.24500 -5.93000  1.000 20.88000 ? 285 PHE   A CG  1 
ATOM   1843 C  CD1 . PHE   A 1 241 ? 55.52600 14.17600 -5.58500  1.000 21.54000 ? 285 PHE   A CD1 1 
ATOM   1844 C  CD2 . PHE   A 1 241 ? 57.62500 14.99300 -6.35200  1.000 21.22000 ? 285 PHE   A CD2 1 
ATOM   1845 C  CE1 . PHE   A 1 241 ? 56.00300 12.88900 -5.65800  1.000 22.14000 ? 285 PHE   A CE1 1 
ATOM   1846 C  CE2 . PHE   A 1 241 ? 58.10300 13.71000 -6.42700  1.000 21.74000 ? 285 PHE   A CE2 1 
ATOM   1847 C  CZ  . PHE   A 1 241 ? 57.29300 12.65600 -6.07900  1.000 22.08000 ? 285 PHE   A CZ  1 
ATOM   1848 N  N   . LEU   A 1 242 ? 54.53200 19.08400 -7.58600  1.000 18.51000 ? 286 LEU   A N   1 
ATOM   1849 C  CA  . LEU   A 1 242 ? 54.33500 20.52500 -7.62000  1.000 18.42000 ? 286 LEU   A CA  1 
ATOM   1850 C  C   . LEU   A 1 242 ? 53.05300 20.93500 -8.32500  1.000 18.26000 ? 286 LEU   A C   1 
ATOM   1851 O  O   . LEU   A 1 242 ? 52.48500 21.98100 -7.99400  1.000 17.99000 ? 286 LEU   A O   1 
ATOM   1852 C  CB  . LEU   A 1 242 ? 55.52500 21.19100 -8.30600  1.000 18.77000 ? 286 LEU   A CB  1 
ATOM   1853 C  CG  . LEU   A 1 242 ? 56.85900 20.93800 -7.61200  1.000 19.04000 ? 286 LEU   A CG  1 
ATOM   1854 C  CD1 . LEU   A 1 242 ? 58.02400 21.39200 -8.47300  1.000 18.97000 ? 286 LEU   A CD1 1 
ATOM   1855 C  CD2 . LEU   A 1 242 ? 56.86200 21.65400 -6.27600  1.000 18.94000 ? 286 LEU   A CD2 1 
ATOM   1856 N  N   . CYS   A 1 243 ? 52.58900 20.14600 -9.29400  1.000 18.33000 ? 287 CYS   A N   1 
ATOM   1857 C  CA  . CYS   A 1 243 ? 51.38900 20.46900 -10.04100 1.000 18.35000 ? 287 CYS   A CA  1 
ATOM   1858 C  C   . CYS   A 1 243 ? 50.50500 19.23300 -10.13100 1.000 18.42000 ? 287 CYS   A C   1 
ATOM   1859 O  O   . CYS   A 1 243 ? 50.99700 18.14200 -10.46200 1.000 18.37000 ? 287 CYS   A O   1 
ATOM   1860 C  CB  . CYS   A 1 243 ? 51.71600 20.98600 -11.44200 1.000 18.19000 ? 287 CYS   A CB  1 
ATOM   1861 S  SG  . CYS   A 1 243 ? 52.66500 22.49400 -11.43800 1.000 18.30000 ? 287 CYS   A SG  1 
ATOM   1862 N  N   . PRO   A 1 244 ? 49.20800 19.35000 -9.83200  1.000 18.44000 ? 288 PRO   A N   1 
ATOM   1863 C  CA  . PRO   A 1 244 ? 48.58800 20.58600 -9.34800  1.000 18.45000 ? 288 PRO   A CA  1 
ATOM   1864 C  C   . PRO   A 1 244 ? 49.01000 20.94800 -7.91900  1.000 18.20000 ? 288 PRO   A C   1 
ATOM   1865 O  O   . PRO   A 1 244 ? 49.78700 20.22100 -7.29800  1.000 18.10000 ? 288 PRO   A O   1 
ATOM   1866 C  CB  . PRO   A 1 244 ? 47.09300 20.27600 -9.41300  1.000 18.84000 ? 288 PRO   A CB  1 
ATOM   1867 C  CG  . PRO   A 1 244 ? 47.00900 18.79700 -9.34200  1.000 19.34000 ? 288 PRO   A CG  1 
ATOM   1868 C  CD  . PRO   A 1 244 ? 48.22900 18.26700 -10.01000 1.000 18.50000 ? 288 PRO   A CD  1 
ATOM   1869 N  N   . ASN   A 1 245 ? 48.48300 22.06600 -7.43100  1.000 18.08000 ? 289 ASN   A N   1 
ATOM   1870 C  CA  . ASN   A 1 245 ? 48.95600 22.65700 -6.18800  1.000 17.93000 ? 289 ASN   A CA  1 
ATOM   1871 C  C   . ASN   A 1 245 ? 48.84800 21.66600 -5.03100  1.000 17.90000 ? 289 ASN   A C   1 
ATOM   1872 O  O   . ASN   A 1 245 ? 47.80500 21.01600 -4.87100  1.000 18.14000 ? 289 ASN   A O   1 
ATOM   1873 C  CB  . ASN   A 1 245 ? 48.15900 23.92400 -5.88200  1.000 18.11000 ? 289 ASN   A CB  1 
ATOM   1874 C  CG  . ASN   A 1 245 ? 48.45600 25.04700 -6.85800  1.000 17.60000 ? 289 ASN   A CG  1 
ATOM   1875 O  OD1 . ASN   A 1 245 ? 49.48400 25.03700 -7.53000  1.000 17.37000 ? 289 ASN   A OD1 1 
ATOM   1876 N  ND2 . ASN   A 1 245 ? 47.56400 26.02300 -6.93300  1.000 17.38000 ? 289 ASN   A ND2 1 
ATOM   1877 N  N   . PRO   A 1 246 ? 49.89900 21.50600 -4.22600  1.000 17.78000 ? 290 PRO   A N   1 
ATOM   1878 C  CA  . PRO   A 1 246 ? 49.83200 20.58800 -3.08300  1.000 18.21000 ? 290 PRO   A CA  1 
ATOM   1879 C  C   . PRO   A 1 246 ? 48.74300 20.97700 -2.09500  1.000 18.95000 ? 290 PRO   A C   1 
ATOM   1880 O  O   . PRO   A 1 246 ? 48.37100 22.14500 -1.96600  1.000 18.95000 ? 290 PRO   A O   1 
ATOM   1881 C  CB  . PRO   A 1 246 ? 51.22200 20.71200 -2.45200  1.000 17.93000 ? 290 PRO   A CB  1 
ATOM   1882 C  CG  . PRO   A 1 246 ? 52.10600 21.13600 -3.57800  1.000 17.72000 ? 290 PRO   A CG  1 
ATOM   1883 C  CD  . PRO   A 1 246 ? 51.26100 22.01800 -4.44900  1.000 17.71000 ? 290 PRO   A CD  1 
ATOM   1884 N  N   . THR   A 1 247 ? 48.23300 19.96800 -1.38900  1.000 18.79000 ? 291 THR   A N   1 
ATOM   1885 C  CA  . THR   A 1 247 ? 47.16600 20.15500 -0.41400  1.000 18.83000 ? 291 THR   A CA  1 
ATOM   1886 C  C   . THR   A 1 247 ? 47.53800 19.55400 0.93700   1.000 18.90000 ? 291 THR   A C   1 
ATOM   1887 O  O   . THR   A 1 247 ? 46.66100 19.09100 1.67100   1.000 18.62000 ? 291 THR   A O   1 
ATOM   1888 C  CB  . THR   A 1 247 ? 45.85100 19.55800 -0.91600  1.000 19.29000 ? 291 THR   A CB  1 
ATOM   1889 O  OG1 . THR   A 1 247 ? 46.06100 18.19700 -1.30800  1.000 18.65000 ? 291 THR   A OG1 1 
ATOM   1890 C  CG2 . THR   A 1 247 ? 45.32400 20.34900 -2.10200  1.000 18.96000 ? 291 THR   A CG2 1 
ATOM   1891 N  N   . ASP   A 1 248 ? 48.83100 19.55000 1.27000   1.000 18.97000 ? 292 ASP   A N   1 
ATOM   1892 C  CA  . ASP   A 1 248 ? 49.27800 19.06700 2.57200   1.000 19.28000 ? 292 ASP   A CA  1 
ATOM   1893 C  C   . ASP   A 1 248 ? 48.55500 19.80100 3.69000   1.000 19.34000 ? 292 ASP   A C   1 
ATOM   1894 O  O   . ASP   A 1 248 ? 48.26900 20.99500 3.58600   1.000 19.12000 ? 292 ASP   A O   1 
ATOM   1895 C  CB  . ASP   A 1 248 ? 50.78400 19.26300 2.73700   1.000 19.18000 ? 292 ASP   A CB  1 
ATOM   1896 C  CG  . ASP   A 1 248 ? 51.58600 18.51200 1.70900   1.000 19.14000 ? 292 ASP   A CG  1 
ATOM   1897 O  OD1 . ASP   A 1 248 ? 51.27000 18.63800 0.51100   1.000 18.71000 ? 292 ASP   A OD1 1 
ATOM   1898 O  OD2 . ASP   A 1 248 ? 52.54200 17.81000 2.09600   1.000 19.36000 ? 292 ASP   A OD2 1 
ATOM   1899 N  N   . ARG   A 1 249 ? 48.26800 19.07700 4.77200   1.000 19.40000 ? 293 ARG   A N   1 
ATOM   1900 C  CA  . ARG   A 1 249 ? 47.58100 19.69100 5.90200   1.000 19.54000 ? 293 ARG   A CA  1 
ATOM   1901 C  C   . ARG   A 1 249 ? 48.37900 20.85400 6.47500   1.000 19.29000 ? 293 ARG   A C   1 
ATOM   1902 O  O   . ARG   A 1 249 ? 47.79300 21.80400 7.00500   1.000 18.68000 ? 293 ARG   A O   1 
ATOM   1903 C  CB  . ARG   A 1 249 ? 47.30900 18.64400 6.98300   1.000 19.80000 ? 293 ARG   A CB  1 
ATOM   1904 C  CG  . ARG   A 1 249 ? 45.84100 18.49800 7.36800   1.000 20.93000 ? 293 ARG   A CG  1 
ATOM   1905 C  CD  . ARG   A 1 249 ? 45.69600 18.26800 8.87000   1.000 24.72000 ? 293 ARG   A CD  1 
ATOM   1906 N  NE  . ARG   A 1 249 ? 44.32900 17.93900 9.26100   1.000 22.84000 ? 293 ARG   A NE  1 
ATOM   1907 C  CZ  . ARG   A 1 249 ? 43.38300 18.83400 9.50900   1.000 23.30000 ? 293 ARG   A CZ  1 
ATOM   1908 N  NH1 . ARG   A 1 249 ? 43.61100 20.13200 9.39300   1.000 23.98000 ? 293 ARG   A NH1 1 
ATOM   1909 N  NH2 . ARG   A 1 249 ? 42.17800 18.41700 9.88100   1.000 23.88000 ? 293 ARG   A NH2 1 
ATOM   1910 N  N   . ALA   A 1 250 ? 49.70900 20.81100 6.35900   1.000 19.29000 ? 294 ALA   A N   1 
ATOM   1911 C  CA  . ALA   A 1 250 ? 50.55400 21.87600 6.88900   1.000 18.94000 ? 294 ALA   A CA  1 
ATOM   1912 C  C   . ALA   A 1 250 ? 50.44300 23.16700 6.08800   1.000 18.64000 ? 294 ALA   A C   1 
ATOM   1913 O  O   . ALA   A 1 250 ? 50.83700 24.22900 6.58700   1.000 18.31000 ? 294 ALA   A O   1 
ATOM   1914 C  CB  . ALA   A 1 250 ? 52.01200 21.41700 6.93000   1.000 19.21000 ? 294 ALA   A CB  1 
ATOM   1915 N  N   . ILE   A 1 251 ? 49.90800 23.10100 4.87200   1.000 18.62000 ? 295 ILE   A N   1 
ATOM   1916 C  CA  . ILE   A 1 251 ? 49.83300 24.25200 3.98100   1.000 18.71000 ? 295 ILE   A CA  1 
ATOM   1917 C  C   . ILE   A 1 251 ? 48.50000 24.95700 4.17200   1.000 18.85000 ? 295 ILE   A C   1 
ATOM   1918 O  O   . ILE   A 1 251 ? 47.43500 24.33300 4.09500   1.000 18.53000 ? 295 ILE   A O   1 
ATOM   1919 C  CB  . ILE   A 1 251 ? 50.01800 23.82200 2.51700   1.000 18.68000 ? 295 ILE   A CB  1 
ATOM   1920 C  CG1 . ILE   A 1 251 ? 51.39700 23.19400 2.31400   1.000 18.47000 ? 295 ILE   A CG1 1 
ATOM   1921 C  CG2 . ILE   A 1 251 ? 49.82800 25.01000 1.60000   1.000 18.08000 ? 295 ILE   A CG2 1 
ATOM   1922 C  CD1 . ILE   A 1 251 ? 51.57700 22.51800 0.97400   1.000 18.34000 ? 295 ILE   A CD1 1 
ATOM   1923 N  N   . CYS   A 1 252 ? 48.55700 26.26600 4.40400   1.000 18.30000 ? 296 CYS   A N   1 
ATOM   1924 C  CA  . CYS   A 1 252 ? 47.36400 27.08100 4.56200   1.000 18.45000 ? 296 CYS   A CA  1 
ATOM   1925 C  C   . CYS   A 1 252 ? 47.02300 27.89800 3.32600   1.000 17.87000 ? 296 CYS   A C   1 
ATOM   1926 O  O   . CYS   A 1 252 ? 45.88600 28.36300 3.20800   1.000 17.46000 ? 296 CYS   A O   1 
ATOM   1927 C  CB  . CYS   A 1 252 ? 47.52200 28.02600 5.76100   1.000 18.51000 ? 296 CYS   A CB  1 
ATOM   1928 S  SG  . CYS   A 1 252 ? 46.81500 27.35700 7.27500   1.000 18.88000 ? 296 CYS   A SG  1 
ATOM   1929 N  N   . GLU   A 1 253 ? 47.97400 28.08700 2.41500   1.000 17.82000 ? 297 GLU   A N   1 
ATOM   1930 C  CA  . GLU   A 1 253 ? 47.72400 28.82900 1.18600   1.000 17.84000 ? 297 GLU   A CA  1 
ATOM   1931 C  C   . GLU   A 1 253 ? 48.77700 28.43100 0.16600   1.000 17.71000 ? 297 GLU   A C   1 
ATOM   1932 O  O   . GLU   A 1 253 ? 49.97400 28.48400 0.46100   1.000 17.48000 ? 297 GLU   A O   1 
ATOM   1933 C  CB  . GLU   A 1 253 ? 47.75900 30.34000 1.43600   1.000 17.87000 ? 297 GLU   A CB  1 
ATOM   1934 C  CG  . GLU   A 1 253 ? 47.62000 31.19200 0.19100   1.000 18.22000 ? 297 GLU   A CG  1 
ATOM   1935 C  CD  . GLU   A 1 253 ? 46.18400 31.34800 -0.26300  1.000 18.49000 ? 297 GLU   A CD  1 
ATOM   1936 O  OE1 . GLU   A 1 253 ? 45.29200 30.70000 0.32100   1.000 18.05000 ? 297 GLU   A OE1 1 
ATOM   1937 O  OE2 . GLU   A 1 253 ? 45.94600 32.12600 -1.20800  1.000 20.46000 ? 297 GLU   A OE2 1 
ATOM   1938 N  N   . TYR   A 1 254 ? 48.33200 28.02500 -1.02100  1.000 17.69000 ? 298 TYR   A N   1 
ATOM   1939 C  CA  . TYR   A 1 254 ? 49.23800 27.69100 -2.11100  1.000 17.57000 ? 298 TYR   A CA  1 
ATOM   1940 C  C   . TYR   A 1 254 ? 48.79400 28.41600 -3.37000  1.000 17.56000 ? 298 TYR   A C   1 
ATOM   1941 O  O   . TYR   A 1 254 ? 47.60500 28.42400 -3.70000  1.000 17.39000 ? 298 TYR   A O   1 
ATOM   1942 C  CB  . TYR   A 1 254 ? 49.29700 26.18500 -2.36700  1.000 17.86000 ? 298 TYR   A CB  1 
ATOM   1943 C  CG  . TYR   A 1 254 ? 50.58800 25.75100 -3.01700  1.000 17.35000 ? 298 TYR   A CG  1 
ATOM   1944 C  CD1 . TYR   A 1 254 ? 50.74800 25.80400 -4.39500  1.000 17.15000 ? 298 TYR   A CD1 1 
ATOM   1945 C  CD2 . TYR   A 1 254 ? 51.65100 25.29900 -2.25500  1.000 17.15000 ? 298 TYR   A CD2 1 
ATOM   1946 C  CE1 . TYR   A 1 254 ? 51.93300 25.40800 -4.99200  1.000 16.97000 ? 298 TYR   A CE1 1 
ATOM   1947 C  CE2 . TYR   A 1 254 ? 52.83600 24.90300 -2.83800  1.000 16.81000 ? 298 TYR   A CE2 1 
ATOM   1948 C  CZ  . TYR   A 1 254 ? 52.97300 24.95900 -4.20700  1.000 16.71000 ? 298 TYR   A CZ  1 
ATOM   1949 O  OH  . TYR   A 1 254 ? 54.15200 24.56300 -4.79000  1.000 16.65000 ? 298 TYR   A OH  1 
ATOM   1950 N  N   . ARG   A 1 255 ? 49.75300 29.02400 -4.06000  1.000 17.32000 ? 299 ARG   A N   1 
ATOM   1951 C  CA  . ARG   A 1 255 ? 49.52500 29.74800 -5.30100  1.000 17.24000 ? 299 ARG   A CA  1 
ATOM   1952 C  C   . ARG   A 1 255 ? 50.63200 29.37500 -6.27300  1.000 16.93000 ? 299 ARG   A C   1 
ATOM   1953 O  O   . ARG   A 1 255 ? 51.77900 29.18700 -5.86200  1.000 17.04000 ? 299 ARG   A O   1 
ATOM   1954 C  CB  . ARG   A 1 255 ? 49.50400 31.26400 -5.06800  1.000 17.66000 ? 299 ARG   A CB  1 
ATOM   1955 C  CG  . ARG   A 1 255 ? 48.47800 31.72400 -4.04200  1.000 18.21000 ? 299 ARG   A CG  1 
ATOM   1956 C  CD  . ARG   A 1 255 ? 48.63700 33.19900 -3.70900  1.000 19.19000 ? 299 ARG   A CD  1 
ATOM   1957 N  NE  . ARG   A 1 255 ? 47.59900 33.66700 -2.79900  1.000 19.67000 ? 299 ARG   A NE  1 
ATOM   1958 C  CZ  . ARG   A 1 255 ? 47.42700 34.93300 -2.44700  1.000 20.17000 ? 299 ARG   A CZ  1 
ATOM   1959 N  NH1 . ARG   A 1 255 ? 48.20200 35.89500 -2.92200  1.000 20.00000 ? 299 ARG   A NH1 1 
ATOM   1960 N  NH2 . ARG   A 1 255 ? 46.45200 35.24200 -1.59700  1.000 20.50000 ? 299 ARG   A NH2 1 
ATOM   1961 N  N   . SER   A 1 256 ? 50.29700 29.25500 -7.55600  1.000 16.99000 ? 300 SER   A N   1 
ATOM   1962 C  CA  . SER   A 1 256 ? 51.29800 28.82500 -8.52500  1.000 17.15000 ? 300 SER   A CA  1 
ATOM   1963 C  C   . SER   A 1 256 ? 50.87100 29.22900 -9.92800  1.000 17.38000 ? 300 SER   A C   1 
ATOM   1964 O  O   . SER   A 1 256 ? 49.76600 29.72800 -10.15600 1.000 17.22000 ? 300 SER   A O   1 
ATOM   1965 C  CB  . SER   A 1 256 ? 51.53000 27.31700 -8.46000  1.000 17.14000 ? 300 SER   A CB  1 
ATOM   1966 O  OG  . SER   A 1 256 ? 50.37300 26.61400 -8.87800  1.000 17.01000 ? 300 SER   A OG  1 
ATOM   1967 N  N   . THR   A 1 257 ? 51.78300 29.00600 -10.86800 1.000 17.63000 ? 301 THR   A N   1 
ATOM   1968 C  CA  . THR   A 1 257 ? 51.51500 29.13600 -12.29300 1.000 18.33000 ? 301 THR   A CA  1 
ATOM   1969 C  C   . THR   A 1 257 ? 51.61800 27.77600 -12.97800 1.000 18.53000 ? 301 THR   A C   1 
ATOM   1970 O  O   . THR   A 1 257 ? 52.17800 27.64600 -14.06700 1.000 18.66000 ? 301 THR   A O   1 
ATOM   1971 C  CB  . THR   A 1 257 ? 52.45800 30.15200 -12.93500 1.000 18.48000 ? 301 THR   A CB  1 
ATOM   1972 O  OG1 . THR   A 1 257 ? 53.82000 29.77600 -12.70200 1.000 17.74000 ? 301 THR   A OG1 1 
ATOM   1973 C  CG2 . THR   A 1 257 ? 52.21000 31.54900 -12.36700 1.000 18.45000 ? 301 THR   A CG2 1 
ATOM   1974 N  N   . CYS   A 1 258 ? 51.09200 26.74100 -12.32000 1.000 18.74000 ? 302 CYS   A N   1 
ATOM   1975 C  CA  . CYS   A 1 258 ? 51.00900 25.42300 -12.91800 1.000 19.21000 ? 302 CYS   A CA  1 
ATOM   1976 C  C   . CYS   A 1 258 ? 50.19700 25.49700 -14.21100 1.000 20.02000 ? 302 CYS   A C   1 
ATOM   1977 O  O   . CYS   A 1 258 ? 49.37200 26.39500 -14.38500 1.000 20.26000 ? 302 CYS   A O   1 
ATOM   1978 C  CB  . CYS   A 1 258 ? 50.36900 24.43600 -11.93800 1.000 18.64000 ? 302 CYS   A CB  1 
ATOM   1979 S  SG  . CYS   A 1 258 ? 51.44200 23.87300 -10.58900 1.000 17.90000 ? 302 CYS   A SG  1 
ATOM   1980 N  N   . PRO   A 1 259 ? 50.40800 24.55500 -15.14200 1.000 20.03000 ? 303 PRO   A N   1 
ATOM   1981 C  CA  . PRO   A 1 259 ? 51.27900 23.38100 -15.07100 1.000 19.79000 ? 303 PRO   A CA  1 
ATOM   1982 C  C   . PRO   A 1 259 ? 52.72000 23.63100 -15.48600 1.000 19.54000 ? 303 PRO   A C   1 
ATOM   1983 O  O   . PRO   A 1 259 ? 53.00000 24.42200 -16.39000 1.000 19.38000 ? 303 PRO   A O   1 
ATOM   1984 C  CB  . PRO   A 1 259 ? 50.61200 22.41200 -16.03900 1.000 20.05000 ? 303 PRO   A CB  1 
ATOM   1985 C  CG  . PRO   A 1 259 ? 50.05100 23.30300 -17.07800 1.000 19.56000 ? 303 PRO   A CG  1 
ATOM   1986 C  CD  . PRO   A 1 259 ? 49.61100 24.55800 -16.37900 1.000 20.55000 ? 303 PRO   A CD  1 
ATOM   1987 N  N   . TYR   A 1 260 ? 53.62500 22.95400 -14.79000 1.000 19.60000 ? 304 TYR   A N   1 
ATOM   1988 C  CA  . TYR   A 1 260 ? 55.01400 22.84100 -15.19400 1.000 19.81000 ? 304 TYR   A CA  1 
ATOM   1989 C  C   . TYR   A 1 260 ? 55.61700 21.62400 -14.50700 1.000 19.69000 ? 304 TYR   A C   1 
ATOM   1990 O  O   . TYR   A 1 260 ? 56.82000 21.38300 -14.55600 1.000 21.52000 ? 304 TYR   A O   1 
ATOM   1991 C  CB  . TYR   A 1 260 ? 55.80700 24.11100 -14.86900 1.000 18.77000 ? 304 TYR   A CB  1 
ATOM   1992 C  CG  . TYR   A 1 260 ? 55.53500 24.71700 -13.51200 1.000 18.50000 ? 304 TYR   A CG  1 
ATOM   1993 C  CD1 . TYR   A 1 260 ? 55.96200 24.09000 -12.35000 1.000 18.14000 ? 304 TYR   A CD1 1 
ATOM   1994 C  CD2 . TYR   A 1 260 ? 54.87500 25.93100 -13.39700 1.000 18.29000 ? 304 TYR   A CD2 1 
ATOM   1995 C  CE1 . TYR   A 1 260 ? 55.72100 24.64500 -11.11100 1.000 17.94000 ? 304 TYR   A CE1 1 
ATOM   1996 C  CE2 . TYR   A 1 260 ? 54.63400 26.49500 -12.16600 1.000 17.87000 ? 304 TYR   A CE2 1 
ATOM   1997 C  CZ  . TYR   A 1 260 ? 55.05800 25.84700 -11.02700 1.000 17.60000 ? 304 TYR   A CZ  1 
ATOM   1998 O  OH  . TYR   A 1 260 ? 54.81300 26.41700 -9.80300  1.000 17.24000 ? 304 TYR   A OH  1 
ATOM   1999 O  OXT . TYR   A 1 260 ? 54.89700 20.83900 -13.89100 1.000 20.36000 ? 304 TYR   A OXT 1 
ATOM   2000 N  N   . ASN   B 1 3   ? 53.42600 59.67100 -52.36800 1.000 22.84000 ? 47  ASN   B N   1 
ATOM   2001 C  CA  . ASN   B 1 3   ? 52.97200 58.63800 -51.44300 1.000 22.55000 ? 47  ASN   B CA  1 
ATOM   2002 C  C   . ASN   B 1 3   ? 51.68300 59.06300 -50.75900 1.000 22.64000 ? 47  ASN   B C   1 
ATOM   2003 O  O   . ASN   B 1 3   ? 51.69600 59.93900 -49.90500 1.000 22.06000 ? 47  ASN   B O   1 
ATOM   2004 C  CB  . ASN   B 1 3   ? 54.05100 58.33400 -50.39800 1.000 22.47000 ? 47  ASN   B CB  1 
ATOM   2005 C  CG  . ASN   B 1 3   ? 53.70500 57.13500 -49.52900 1.000 22.30000 ? 47  ASN   B CG  1 
ATOM   2006 O  OD1 . ASN   B 1 3   ? 52.74600 56.41400 -49.79800 1.000 22.16000 ? 47  ASN   B OD1 1 
ATOM   2007 N  ND2 . ASN   B 1 3   ? 54.49500 56.91200 -48.48500 1.000 21.89000 ? 47  ASN   B ND2 1 
ATOM   2008 N  N   . PRO   B 1 4   ? 50.56600 58.43600 -51.13200 1.000 22.68000 ? 48  PRO   B N   1 
ATOM   2009 C  CA  . PRO   B 1 4   ? 49.27500 58.78500 -50.52800 1.000 22.39000 ? 48  PRO   B CA  1 
ATOM   2010 C  C   . PRO   B 1 4   ? 49.08300 58.25700 -49.11600 1.000 22.32000 ? 48  PRO   B C   1 
ATOM   2011 O  O   . PRO   B 1 4   ? 48.03200 58.51400 -48.52000 1.000 22.34000 ? 48  PRO   B O   1 
ATOM   2012 C  CB  . PRO   B 1 4   ? 48.27300 58.13300 -51.48900 1.000 21.51000 ? 48  PRO   B CB  1 
ATOM   2013 C  CG  . PRO   B 1 4   ? 48.99400 56.93000 -51.98400 1.000 22.49000 ? 48  PRO   B CG  1 
ATOM   2014 C  CD  . PRO   B 1 4   ? 50.44000 57.34100 -52.11100 1.000 22.92000 ? 48  PRO   B CD  1 
ATOM   2015 N  N   . TYR   B 1 5   ? 50.04600 57.51600 -48.57600 1.000 22.29000 ? 49  TYR   B N   1 
ATOM   2016 C  CA  . TYR   B 1 5   ? 49.92800 56.91100 -47.25700 1.000 22.19000 ? 49  TYR   B CA  1 
ATOM   2017 C  C   . TYR   B 1 5   ? 50.66100 57.69500 -46.18000 1.000 22.17000 ? 49  TYR   B C   1 
ATOM   2018 O  O   . TYR   B 1 5   ? 50.63200 57.29300 -45.01500 1.000 21.83000 ? 49  TYR   B O   1 
ATOM   2019 C  CB  . TYR   B 1 5   ? 50.45100 55.47100 -47.28600 1.000 22.25000 ? 49  TYR   B CB  1 
ATOM   2020 C  CG  . TYR   B 1 5   ? 49.79200 54.59700 -48.32300 1.000 22.37000 ? 49  TYR   B CG  1 
ATOM   2021 C  CD1 . TYR   B 1 5   ? 48.41900 54.62600 -48.51400 1.000 22.26000 ? 49  TYR   B CD1 1 
ATOM   2022 C  CD2 . TYR   B 1 5   ? 50.54700 53.75100 -49.12200 1.000 22.67000 ? 49  TYR   B CD2 1 
ATOM   2023 C  CE1 . TYR   B 1 5   ? 47.81600 53.83300 -49.46800 1.000 21.91000 ? 49  TYR   B CE1 1 
ATOM   2024 C  CE2 . TYR   B 1 5   ? 49.95600 52.95400 -50.07500 1.000 22.62000 ? 49  TYR   B CE2 1 
ATOM   2025 C  CZ  . TYR   B 1 5   ? 48.59100 52.99800 -50.24500 1.000 21.23000 ? 49  TYR   B CZ  1 
ATOM   2026 O  OH  . TYR   B 1 5   ? 47.99900 52.20000 -51.19600 1.000 21.24000 ? 49  TYR   B OH  1 
ATOM   2027 N  N   . GLU   B 1 6   ? 51.32100 58.79100 -46.54000 1.000 22.30000 ? 50  GLU   B N   1 
ATOM   2028 C  CA  . GLU   B 1 6   ? 52.01700 59.60700 -45.55400 1.000 22.68000 ? 50  GLU   B CA  1 
ATOM   2029 C  C   . GLU   B 1 6   ? 51.02000 60.30000 -44.63700 1.000 22.96000 ? 50  GLU   B C   1 
ATOM   2030 O  O   . GLU   B 1 6   ? 50.08200 60.95800 -45.09900 1.000 22.83000 ? 50  GLU   B O   1 
ATOM   2031 C  CB  . GLU   B 1 6   ? 52.89000 60.64800 -46.24700 1.000 22.66000 ? 50  GLU   B CB  1 
ATOM   2032 C  CG  . GLU   B 1 6   ? 54.20100 60.12700 -46.78600 1.000 23.13000 ? 50  GLU   B CG  1 
ATOM   2033 C  CD  . GLU   B 1 6   ? 54.97500 61.21400 -47.48300 1.000 23.00000 ? 50  GLU   B CD  1 
ATOM   2034 O  OE1 . GLU   B 1 6   ? 54.33800 62.19200 -47.92700 1.000 22.02000 ? 50  GLU   B OE1 1 
ATOM   2035 O  OE2 . GLU   B 1 6   ? 56.21200 61.10500 -47.57600 1.000 23.95000 ? 50  GLU   B OE2 1 
ATOM   2036 N  N   . ARG   B 1 7   ? 51.22500 60.15100 -43.33400 1.000 23.03000 ? 51  ARG   B N   1 
ATOM   2037 C  CA  . ARG   B 1 7   ? 50.43100 60.83700 -42.33200 1.000 23.66000 ? 51  ARG   B CA  1 
ATOM   2038 C  C   . ARG   B 1 7   ? 51.36000 61.62100 -41.42000 1.000 24.05000 ? 51  ARG   B C   1 
ATOM   2039 O  O   . ARG   B 1 7   ? 52.50900 61.23200 -41.19500 1.000 23.57000 ? 51  ARG   B O   1 
ATOM   2040 C  CB  . ARG   B 1 7   ? 49.59200 59.85100 -41.51400 1.000 23.05000 ? 51  ARG   B CB  1 
ATOM   2041 C  CG  . ARG   B 1 7   ? 48.72200 58.92600 -42.34600 1.000 23.25000 ? 51  ARG   B CG  1 
ATOM   2042 C  CD  . ARG   B 1 7   ? 47.53800 59.65500 -42.95600 1.000 24.45000 ? 51  ARG   B CD  1 
ATOM   2043 N  NE  . ARG   B 1 7   ? 46.70300 58.75600 -43.74300 1.000 23.90000 ? 51  ARG   B NE  1 
ATOM   2044 C  CZ  . ARG   B 1 7   ? 46.79800 58.60500 -45.05600 1.000 23.50000 ? 51  ARG   B CZ  1 
ATOM   2045 N  NH1 . ARG   B 1 7   ? 47.65200 59.31800 -45.77200 1.000 23.64000 ? 51  ARG   B NH1 1 
ATOM   2046 N  NH2 . ARG   B 1 7   ? 46.01000 57.72700 -45.66800 1.000 23.01000 ? 51  ARG   B NH2 1 
ATOM   2047 N  N   . GLY   B 1 8   ? 50.86600 62.74000 -40.90900 1.000 24.55000 ? 52  GLY   B N   1 
ATOM   2048 C  CA  . GLY   B 1 8   ? 51.61500 63.52000 -39.95700 1.000 24.60000 ? 52  GLY   B CA  1 
ATOM   2049 C  C   . GLY   B 1 8   ? 52.76200 64.28400 -40.58300 1.000 24.04000 ? 52  GLY   B C   1 
ATOM   2050 O  O   . GLY   B 1 8   ? 53.21200 63.99200 -41.69600 1.000 24.04000 ? 52  GLY   B O   1 
ATOM   2051 N  N   . PRO   B 1 9   ? 53.25900 65.28600 -39.86700 1.000 24.05000 ? 53  PRO   B N   1 
ATOM   2052 C  CA  . PRO   B 1 9   ? 54.32400 66.12900 -40.41300 1.000 24.40000 ? 53  PRO   B CA  1 
ATOM   2053 C  C   . PRO   B 1 9   ? 55.62500 65.36000 -40.55700 1.000 24.38000 ? 53  PRO   B C   1 
ATOM   2054 O  O   . PRO   B 1 9   ? 55.75800 64.20200 -40.15300 1.000 23.99000 ? 53  PRO   B O   1 
ATOM   2055 C  CB  . PRO   B 1 9   ? 54.45000 67.25600 -39.38400 1.000 24.39000 ? 53  PRO   B CB  1 
ATOM   2056 C  CG  . PRO   B 1 9   ? 53.93600 66.66500 -38.12300 1.000 24.40000 ? 53  PRO   B CG  1 
ATOM   2057 C  CD  . PRO   B 1 9   ? 52.83400 65.72900 -38.53000 1.000 24.00000 ? 53  PRO   B CD  1 
ATOM   2058 N  N   . ASP   B 1 10  ? 56.59400 66.03900 -41.16000 1.000 24.24000 ? 54  ASP   B N   1 
ATOM   2059 C  CA  . ASP   B 1 10  ? 57.89800 65.44000 -41.38100 1.000 24.63000 ? 54  ASP   B CA  1 
ATOM   2060 C  C   . ASP   B 1 10  ? 58.51400 65.04800 -40.04300 1.000 24.93000 ? 54  ASP   B C   1 
ATOM   2061 O  O   . ASP   B 1 10  ? 58.38800 65.78800 -39.06100 1.000 26.12000 ? 54  ASP   B O   1 
ATOM   2062 C  CB  . ASP   B 1 10  ? 58.81500 66.41400 -42.11900 1.000 25.77000 ? 54  ASP   B CB  1 
ATOM   2063 C  CG  . ASP   B 1 10  ? 58.36300 66.67600 -43.53800 1.000 25.75000 ? 54  ASP   B CG  1 
ATOM   2064 O  OD1 . ASP   B 1 10  ? 57.44400 65.97700 -44.01800 1.000 25.51000 ? 54  ASP   B OD1 1 
ATOM   2065 O  OD2 . ASP   B 1 10  ? 58.93100 67.58900 -44.17100 1.000 27.60000 ? 54  ASP   B OD2 1 
ATOM   2066 N  N   . PRO   B 1 11  ? 59.17400 63.89900 -39.96300 1.000 24.27000 ? 55  PRO   B N   1 
ATOM   2067 C  CA  . PRO   B 1 11  ? 59.66700 63.42500 -38.67100 1.000 24.52000 ? 55  PRO   B CA  1 
ATOM   2068 C  C   . PRO   B 1 11  ? 61.02000 64.00500 -38.30100 1.000 25.29000 ? 55  PRO   B C   1 
ATOM   2069 O  O   . PRO   B 1 11  ? 61.81500 64.41200 -39.15200 1.000 25.03000 ? 55  PRO   B O   1 
ATOM   2070 C  CB  . PRO   B 1 11  ? 59.76300 61.91100 -38.87800 1.000 23.75000 ? 55  PRO   B CB  1 
ATOM   2071 C  CG  . PRO   B 1 11  ? 60.10400 61.78000 -40.31700 1.000 23.08000 ? 55  PRO   B CG  1 
ATOM   2072 C  CD  . PRO   B 1 11  ? 59.37000 62.89700 -41.02400 1.000 23.36000 ? 55  PRO   B CD  1 
ATOM   2073 N  N   . THR   B 1 12  ? 61.25800 64.04500 -36.99200 1.000 25.84000 ? 56  THR   B N   1 
ATOM   2074 C  CA  . THR   B 1 12  ? 62.56400 64.29200 -36.40200 1.000 26.75000 ? 56  THR   B CA  1 
ATOM   2075 C  C   . THR   B 1 12  ? 62.82900 63.21800 -35.35800 1.000 27.30000 ? 56  THR   B C   1 
ATOM   2076 O  O   . THR   B 1 12  ? 61.94300 62.44000 -34.99600 1.000 26.64000 ? 56  THR   B O   1 
ATOM   2077 C  CB  . THR   B 1 12  ? 62.65600 65.68300 -35.75800 1.000 27.69000 ? 56  THR   B CB  1 
ATOM   2078 O  OG1 . THR   B 1 12  ? 61.62000 65.83800 -34.78000 1.000 27.10000 ? 56  THR   B OG1 1 
ATOM   2079 C  CG2 . THR   B 1 12  ? 62.51500 66.75200 -36.80900 1.000 28.67000 ? 56  THR   B CG2 1 
ATOM   2080 N  N   . GLU   B 1 13  ? 64.06900 63.18000 -34.87100 1.000 28.07000 ? 57  GLU   B N   1 
ATOM   2081 C  CA  . GLU   B 1 13  ? 64.42000 62.19800 -33.85300 1.000 28.03000 ? 57  GLU   B CA  1 
ATOM   2082 C  C   . GLU   B 1 13  ? 63.64900 62.43400 -32.55800 1.000 27.14000 ? 57  GLU   B C   1 
ATOM   2083 O  O   . GLU   B 1 13  ? 63.35100 61.47900 -31.83500 1.000 26.78000 ? 57  GLU   B O   1 
ATOM   2084 C  CB  . GLU   B 1 13  ? 65.92600 62.22700 -33.59900 1.000 29.62000 ? 57  GLU   B CB  1 
ATOM   2085 C  CG  . GLU   B 1 13  ? 66.48600 60.91600 -33.09700 1.000 30.95000 ? 57  GLU   B CG  1 
ATOM   2086 C  CD  . GLU   B 1 13  ? 67.98100 60.81100 -33.30600 1.000 33.28000 ? 57  GLU   B CD  1 
ATOM   2087 O  OE1 . GLU   B 1 13  ? 68.62400 61.85200 -33.56500 1.000 38.63000 ? 57  GLU   B OE1 1 
ATOM   2088 O  OE2 . GLU   B 1 13  ? 68.51300 59.68400 -33.21700 1.000 36.11000 ? 57  GLU   B OE2 1 
ATOM   2089 N  N   . ASP   B 1 14  ? 63.30500 63.68900 -32.26000 1.000 27.76000 ? 58  ASP   B N   1 
ATOM   2090 C  CA  . ASP   B 1 14  ? 62.50900 63.99000 -31.07700 1.000 28.91000 ? 58  ASP   B CA  1 
ATOM   2091 C  C   . ASP   B 1 14  ? 61.03400 63.66400 -31.27000 1.000 27.70000 ? 58  ASP   B C   1 
ATOM   2092 O  O   . ASP   B 1 14  ? 60.35000 63.32400 -30.29900 1.000 26.93000 ? 58  ASP   B O   1 
ATOM   2093 C  CB  . ASP   B 1 14  ? 62.67100 65.46200 -30.69800 1.000 29.32000 ? 58  ASP   B CB  1 
ATOM   2094 C  CG  . ASP   B 1 14  ? 63.99300 65.74300 -30.01700 1.000 30.25000 ? 58  ASP   B CG  1 
ATOM   2095 O  OD1 . ASP   B 1 14  ? 64.45400 64.87900 -29.24200 1.000 29.55000 ? 58  ASP   B OD1 1 
ATOM   2096 O  OD2 . ASP   B 1 14  ? 64.57300 66.82300 -30.25700 1.000 31.44000 ? 58  ASP   B OD2 1 
ATOM   2097 N  N   . SER   B 1 15  ? 60.52600 63.76100 -32.50200 1.000 27.35000 ? 59  SER   B N   1 
ATOM   2098 C  CA  . SER   B 1 15  ? 59.11300 63.47800 -32.74400 1.000 26.89000 ? 59  SER   B CA  1 
ATOM   2099 C  C   . SER   B 1 15  ? 58.80700 61.99400 -32.58500 1.000 27.38000 ? 59  SER   B C   1 
ATOM   2100 O  O   . SER   B 1 15  ? 57.74100 61.62500 -32.07800 1.000 27.50000 ? 59  SER   B O   1 
ATOM   2101 C  CB  . SER   B 1 15  ? 58.70900 63.96100 -34.13800 1.000 26.59000 ? 59  SER   B CB  1 
ATOM   2102 O  OG  . SER   B 1 15  ? 59.34700 63.19800 -35.14500 1.000 26.66000 ? 59  SER   B OG  1 
ATOM   2103 N  N   . ILE   B 1 16  ? 59.72300 61.12700 -33.01800 1.000 26.50000 ? 60  ILE   B N   1 
ATOM   2104 C  CA  . ILE   B 1 16  ? 59.47900 59.69500 -32.88700 1.000 26.00000 ? 60  ILE   B CA  1 
ATOM   2105 C  C   . ILE   B 1 16  ? 59.67600 59.24000 -31.44700 1.000 25.84000 ? 60  ILE   B C   1 
ATOM   2106 O  O   . ILE   B 1 16  ? 59.08800 58.23700 -31.02600 1.000 24.98000 ? 60  ILE   B O   1 
ATOM   2107 C  CB  . ILE   B 1 16  ? 60.37100 58.89700 -33.85700 1.000 25.01000 ? 60  ILE   B CB  1 
ATOM   2108 C  CG1 . ILE   B 1 16  ? 61.84700 59.18800 -33.60500 1.000 25.60000 ? 60  ILE   B CG1 1 
ATOM   2109 C  CG2 . ILE   B 1 16  ? 60.02700 59.22500 -35.29700 1.000 24.13000 ? 60  ILE   B CG2 1 
ATOM   2110 C  CD1 . ILE   B 1 16  ? 62.76200 58.21300 -34.29400 1.000 23.83000 ? 60  ILE   B CD1 1 
ATOM   2111 N  N   . GLU   B 1 17  ? 60.49000 59.96200 -30.67100 1.000 26.33000 ? 61  GLU   B N   1 
ATOM   2112 C  CA  . GLU   B 1 17  ? 60.69700 59.65500 -29.26100 1.000 26.97000 ? 61  GLU   B CA  1 
ATOM   2113 C  C   . GLU   B 1 17  ? 59.56200 60.14100 -28.36900 1.000 27.21000 ? 61  GLU   B C   1 
ATOM   2114 O  O   . GLU   B 1 17  ? 59.52800 59.77400 -27.19100 1.000 26.16000 ? 61  GLU   B O   1 
ATOM   2115 C  CB  . GLU   B 1 17  ? 62.01100 60.27000 -28.76700 1.000 27.73000 ? 61  GLU   B CB  1 
ATOM   2116 C  CG  . GLU   B 1 17  ? 63.27100 59.58300 -29.26100 1.000 27.68000 ? 61  GLU   B CG  1 
ATOM   2117 C  CD  . GLU   B 1 17  ? 64.52700 60.14100 -28.61700 1.000 28.08000 ? 61  GLU   B CD  1 
ATOM   2118 O  OE1 . GLU   B 1 17  ? 64.48200 61.27700 -28.10300 1.000 27.58000 ? 61  GLU   B OE1 1 
ATOM   2119 O  OE2 . GLU   B 1 17  ? 65.56000 59.44200 -28.61800 1.000 26.80000 ? 61  GLU   B OE2 1 
ATOM   2120 N  N   . ALA   B 1 18  ? 58.64300 60.95000 -28.89000 1.000 27.68000 ? 62  ALA   B N   1 
ATOM   2121 C  CA  . ALA   B 1 18  ? 57.59300 61.52700 -28.06300 1.000 28.32000 ? 62  ALA   B CA  1 
ATOM   2122 C  C   . ALA   B 1 18  ? 56.61200 60.46000 -27.59100 1.000 27.77000 ? 62  ALA   B C   1 
ATOM   2123 O  O   . ALA   B 1 18  ? 56.32700 59.48700 -28.29200 1.000 27.19000 ? 62  ALA   B O   1 
ATOM   2124 C  CB  . ALA   B 1 18  ? 56.84300 62.61400 -28.83200 1.000 28.66000 ? 62  ALA   B CB  1 
ATOM   2125 N  N   . ILE   B 1 19  ? 56.08400 60.66100 -26.38200 1.000 28.66000 ? 63  ILE   B N   1 
ATOM   2126 C  CA  . ILE   B 1 19  ? 55.14500 59.70000 -25.81500 1.000 28.64000 ? 63  ILE   B CA  1 
ATOM   2127 C  C   . ILE   B 1 19  ? 53.80900 59.75300 -26.54400 1.000 29.23000 ? 63  ILE   B C   1 
ATOM   2128 O  O   . ILE   B 1 19  ? 53.11700 58.73700 -26.66900 1.000 27.24000 ? 63  ILE   B O   1 
ATOM   2129 C  CB  . ILE   B 1 19  ? 54.97900 59.95700 -24.30800 1.000 29.31000 ? 63  ILE   B CB  1 
ATOM   2130 C  CG1 . ILE   B 1 19  ? 56.34400 60.02200 -23.62700 1.000 29.78000 ? 63  ILE   B CG1 1 
ATOM   2131 C  CG2 . ILE   B 1 19  ? 54.14600 58.86800 -23.66900 1.000 28.89000 ? 63  ILE   B CG2 1 
ATOM   2132 C  CD1 . ILE   B 1 19  ? 56.25800 60.23600 -22.14200 1.000 30.59000 ? 63  ILE   B CD1 1 
ATOM   2133 N  N   . ARG   B 1 20  ? 53.41500 60.92500 -27.02400 1.000 31.05000 ? 64  ARG   B N   1 
ATOM   2134 C  CA  . ARG   B 1 20  ? 52.18600 61.08800 -27.78000 1.000 31.78000 ? 64  ARG   B CA  1 
ATOM   2135 C  C   . ARG   B 1 20  ? 52.54100 61.61800 -29.15700 1.000 28.72000 ? 64  ARG   B C   1 
ATOM   2136 O  O   . ARG   B 1 20  ? 53.28800 62.59500 -29.27700 1.000 29.14000 ? 64  ARG   B O   1 
ATOM   2137 C  CB  . ARG   B 1 20  ? 51.22100 62.03600 -27.06600 1.000 33.76000 ? 64  ARG   B CB  1 
ATOM   2138 C  CG  . ARG   B 1 20  ? 50.81000 61.56900 -25.67700 1.000 38.73000 ? 64  ARG   B CG  1 
ATOM   2139 C  CD  . ARG   B 1 20  ? 50.30700 62.72900 -24.83100 1.000 44.83000 ? 64  ARG   B CD  1 
ATOM   2140 N  NE  . ARG   B 1 20  ? 49.87700 62.28700 -23.51100 1.000 51.45000 ? 64  ARG   B NE  1 
ATOM   2141 C  CZ  . ARG   B 1 20  ? 48.61600 62.04900 -23.17700 1.000 54.75000 ? 64  ARG   B CZ  1 
ATOM   2142 N  NH1 . ARG   B 1 20  ? 47.62700 62.22600 -24.03700 1.000 54.75000 ? 64  ARG   B NH1 1 
ATOM   2143 N  NH2 . ARG   B 1 20  ? 48.34000 61.62400 -21.94700 1.000 57.99000 ? 64  ARG   B NH2 1 
ATOM   2144 N  N   . GLY   B 1 21  ? 52.02400 60.96300 -30.19000 1.000 27.85000 ? 65  GLY   B N   1 
ATOM   2145 C  CA  . GLY   B 1 21  ? 52.24900 61.39400 -31.54400 1.000 27.89000 ? 65  GLY   B CA  1 
ATOM   2146 C  C   . GLY   B 1 21  ? 51.34000 62.54400 -31.90600 1.000 27.38000 ? 65  GLY   B C   1 
ATOM   2147 O  O   . GLY   B 1 21  ? 50.68200 63.13900 -31.04700 1.000 29.54000 ? 65  GLY   B O   1 
ATOM   2148 N  N   . PRO   B 1 22  ? 51.28200 62.88000 -33.19600 1.000 26.58000 ? 66  PRO   B N   1 
ATOM   2149 C  CA  . PRO   B 1 22  ? 50.45600 64.01900 -33.62400 1.000 27.42000 ? 66  PRO   B CA  1 
ATOM   2150 C  C   . PRO   B 1 22  ? 48.96000 63.74200 -33.63400 1.000 27.53000 ? 66  PRO   B C   1 
ATOM   2151 O  O   . PRO   B 1 22  ? 48.18400 64.69300 -33.78400 1.000 27.19000 ? 66  PRO   B O   1 
ATOM   2152 C  CB  . PRO   B 1 22  ? 50.97300 64.31200 -35.03800 1.000 26.57000 ? 66  PRO   B CB  1 
ATOM   2153 C  CG  . PRO   B 1 22  ? 51.54300 63.01000 -35.50100 1.000 27.28000 ? 66  PRO   B CG  1 
ATOM   2154 C  CD  . PRO   B 1 22  ? 52.12900 62.36500 -34.28500 1.000 25.96000 ? 66  PRO   B CD  1 
ATOM   2155 N  N   . PHE   B 1 23  ? 48.52600 62.49400 -33.47600 1.000 26.70000 ? 67  PHE   B N   1 
ATOM   2156 C  CA  . PHE   B 1 23  ? 47.11300 62.14400 -33.52900 1.000 26.28000 ? 67  PHE   B CA  1 
ATOM   2157 C  C   . PHE   B 1 23  ? 46.57100 61.85200 -32.13400 1.000 26.35000 ? 67  PHE   B C   1 
ATOM   2158 O  O   . PHE   B 1 23  ? 47.27900 61.33500 -31.26800 1.000 25.45000 ? 67  PHE   B O   1 
ATOM   2159 C  CB  . PHE   B 1 23  ? 46.87800 60.92500 -34.43100 1.000 25.36000 ? 67  PHE   B CB  1 
ATOM   2160 C  CG  . PHE   B 1 23  ? 47.24000 61.15600 -35.86900 1.000 25.54000 ? 67  PHE   B CG  1 
ATOM   2161 C  CD1 . PHE   B 1 23  ? 48.52500 60.90300 -36.32400 1.000 25.12000 ? 67  PHE   B CD1 1 
ATOM   2162 C  CD2 . PHE   B 1 23  ? 46.29600 61.63000 -36.76600 1.000 26.27000 ? 67  PHE   B CD2 1 
ATOM   2163 C  CE1 . PHE   B 1 23  ? 48.86400 61.11900 -37.65200 1.000 25.00000 ? 67  PHE   B CE1 1 
ATOM   2164 C  CE2 . PHE   B 1 23  ? 46.62600 61.84800 -38.09500 1.000 25.09000 ? 67  PHE   B CE2 1 
ATOM   2165 C  CZ  . PHE   B 1 23  ? 47.91300 61.59200 -38.53800 1.000 25.53000 ? 67  PHE   B CZ  1 
ATOM   2166 N  N   . SER   B 1 24  ? 45.30300 62.18800 -31.92600 1.000 26.42000 ? 68  SER   B N   1 
ATOM   2167 C  CA  . SER   B 1 24  ? 44.60900 61.81500 -30.70500 1.000 25.86000 ? 68  SER   B CA  1 
ATOM   2168 C  C   . SER   B 1 24  ? 43.91500 60.47500 -30.90400 1.000 24.61000 ? 68  SER   B C   1 
ATOM   2169 O  O   . SER   B 1 24  ? 43.47700 60.14100 -32.00700 1.000 24.54000 ? 68  SER   B O   1 
ATOM   2170 C  CB  . SER   B 1 24  ? 43.59300 62.88100 -30.30000 1.000 27.89000 ? 68  SER   B CB  1 
ATOM   2171 O  OG  . SER   B 1 24  ? 42.50700 62.90900 -31.20300 1.000 26.89000 ? 68  SER   B OG  1 
ATOM   2172 N  N   . VAL   B 1 25  ? 43.81300 59.70800 -29.82000 1.000 24.05000 ? 69  VAL   B N   1 
ATOM   2173 C  CA  . VAL   B 1 25  ? 43.44000 58.30100 -29.87600 1.000 24.74000 ? 69  VAL   B CA  1 
ATOM   2174 C  C   . VAL   B 1 25  ? 42.15000 58.08600 -29.10200 1.000 24.37000 ? 69  VAL   B C   1 
ATOM   2175 O  O   . VAL   B 1 25  ? 42.00000 58.59100 -27.98500 1.000 23.53000 ? 69  VAL   B O   1 
ATOM   2176 C  CB  . VAL   B 1 25  ? 44.55600 57.40800 -29.30900 1.000 24.54000 ? 69  VAL   B CB  1 
ATOM   2177 C  CG1 . VAL   B 1 25  ? 44.22600 55.94000 -29.52200 1.000 23.43000 ? 69  VAL   B CG1 1 
ATOM   2178 C  CG2 . VAL   B 1 25  ? 45.88900 57.77300 -29.92700 1.000 24.73000 ? 69  VAL   B CG2 1 
ATOM   2179 N  N   . ALA   B 1 26  ? 41.23100 57.33300 -29.69600 1.000 24.21000 ? 70  ALA   B N   1 
ATOM   2180 C  CA  . ALA   B 1 26  ? 40.08900 56.75000 -29.00900 1.000 23.93000 ? 70  ALA   B CA  1 
ATOM   2181 C  C   . ALA   B 1 26  ? 40.22800 55.23400 -29.01800 1.000 23.27000 ? 70  ALA   B C   1 
ATOM   2182 O  O   . ALA   B 1 26  ? 41.08900 54.67000 -29.69700 1.000 22.75000 ? 70  ALA   B O   1 
ATOM   2183 C  CB  . ALA   B 1 26  ? 38.77100 57.17500 -29.66300 1.000 23.88000 ? 70  ALA   B CB  1 
ATOM   2184 N  N   . THR   B 1 27  ? 39.37400 54.56400 -28.25000 1.000 22.69000 ? 71  THR   B N   1 
ATOM   2185 C  CA  . THR   B 1 27  ? 39.46200 53.12000 -28.11400 1.000 23.03000 ? 71  THR   B CA  1 
ATOM   2186 C  C   . THR   B 1 27  ? 38.10900 52.48000 -28.37200 1.000 23.42000 ? 71  THR   B C   1 
ATOM   2187 O  O   . THR   B 1 27  ? 37.07900 53.15000 -28.47700 1.000 23.14000 ? 71  THR   B O   1 
ATOM   2188 C  CB  . THR   B 1 27  ? 39.96100 52.69800 -26.72800 1.000 22.50000 ? 71  THR   B CB  1 
ATOM   2189 O  OG1 . THR   B 1 27  ? 39.04000 53.16000 -25.73400 1.000 22.22000 ? 71  THR   B OG1 1 
ATOM   2190 C  CG2 . THR   B 1 27  ? 41.35000 53.26200 -26.45700 1.000 22.49000 ? 71  THR   B CG2 1 
ATOM   2191 N  N   . GLU   B 1 28  ? 38.13900 51.15500 -28.45800 1.000 23.18000 ? 72  GLU   B N   1 
ATOM   2192 C  CA  . GLU   B 1 28  ? 36.94500 50.36000 -28.71300 1.000 23.34000 ? 72  GLU   B CA  1 
ATOM   2193 C  C   . GLU   B 1 28  ? 37.24100 48.94500 -28.24900 1.000 22.79000 ? 72  GLU   B C   1 
ATOM   2194 O  O   . GLU   B 1 28  ? 38.17900 48.32000 -28.75300 1.000 21.55000 ? 72  GLU   B O   1 
ATOM   2195 C  CB  . GLU   B 1 28  ? 36.58200 50.39100 -30.19900 1.000 22.69000 ? 72  GLU   B CB  1 
ATOM   2196 C  CG  . GLU   B 1 28  ? 35.17600 49.92600 -30.51900 1.000 24.31000 ? 72  GLU   B CG  1 
ATOM   2197 C  CD  . GLU   B 1 28  ? 34.12300 50.96400 -30.18600 1.000 26.91000 ? 72  GLU   B CD  1 
ATOM   2198 O  OE1 . GLU   B 1 28  ? 34.48000 52.14600 -29.99600 1.000 28.33000 ? 72  GLU   B OE1 1 
ATOM   2199 O  OE2 . GLU   B 1 28  ? 32.93200 50.59400 -30.11600 1.000 28.75000 ? 72  GLU   B OE2 1 
ATOM   2200 N  N   . ARG   B 1 29  ? 36.45700 48.44500 -27.29500 1.000 23.14000 ? 73  ARG   B N   1 
ATOM   2201 C  CA  . ARG   B 1 29  ? 36.71100 47.14300 -26.68900 1.000 22.90000 ? 73  ARG   B CA  1 
ATOM   2202 C  C   . ARG   B 1 29  ? 36.09200 46.02200 -27.51500 1.000 21.80000 ? 73  ARG   B C   1 
ATOM   2203 O  O   . ARG   B 1 29  ? 34.94300 46.11600 -27.95100 1.000 21.64000 ? 73  ARG   B O   1 
ATOM   2204 C  CB  . ARG   B 1 29  ? 36.14000 47.09600 -25.26800 1.000 24.87000 ? 73  ARG   B CB  1 
ATOM   2205 C  CG  . ARG   B 1 29  ? 36.68500 48.14700 -24.31500 1.000 27.44000 ? 73  ARG   B CG  1 
ATOM   2206 C  CD  . ARG   B 1 29  ? 38.09600 47.81400 -23.86400 1.000 29.00000 ? 73  ARG   B CD  1 
ATOM   2207 N  NE  . ARG   B 1 29  ? 38.33200 48.20800 -22.48000 1.000 40.26000 ? 73  ARG   B NE  1 
ATOM   2208 C  CZ  . ARG   B 1 29  ? 38.26100 47.38500 -21.44100 1.000 42.30000 ? 73  ARG   B CZ  1 
ATOM   2209 N  NH1 . ARG   B 1 29  ? 37.98400 46.09900 -21.59200 1.000 40.81000 ? 73  ARG   B NH1 1 
ATOM   2210 N  NH2 . ARG   B 1 29  ? 38.47400 47.86300 -20.21800 1.000 39.87000 ? 73  ARG   B NH2 1 
ATOM   2211 N  N   . VAL   B 1 30  ? 36.84800 44.94200 -27.69800 1.000 20.81000 ? 74  VAL   B N   1 
ATOM   2212 C  CA  . VAL   B 1 30  ? 36.41200 43.78900 -28.47800 1.000 19.88000 ? 74  VAL   B CA  1 
ATOM   2213 C  C   . VAL   B 1 30  ? 36.25800 42.60000 -27.54600 1.000 19.45000 ? 74  VAL   B C   1 
ATOM   2214 O  O   . VAL   B 1 30  ? 37.20600 42.22100 -26.85000 1.000 19.15000 ? 74  VAL   B O   1 
ATOM   2215 C  CB  . VAL   B 1 30  ? 37.39300 43.47200 -29.61600 1.000 19.32000 ? 74  VAL   B CB  1 
ATOM   2216 C  CG1 . VAL   B 1 30  ? 37.01200 42.16500 -30.30000 1.000 19.02000 ? 74  VAL   B CG1 1 
ATOM   2217 C  CG2 . VAL   B 1 30  ? 37.40700 44.61300 -30.60600 1.000 19.40000 ? 74  VAL   B CG2 1 
ATOM   2218 N  N   . SER   B 1 31  ? 35.07500 41.99700 -27.55400 1.000 19.23000 ? 75  SER   B N   1 
ATOM   2219 C  CA  . SER   B 1 31  ? 34.77700 40.91200 -26.63700 1.000 19.19000 ? 75  SER   B CA  1 
ATOM   2220 C  C   . SER   B 1 31  ? 35.59400 39.66800 -26.96500 1.000 18.68000 ? 75  SER   B C   1 
ATOM   2221 O  O   . SER   B 1 31  ? 35.95600 39.41600 -28.11700 1.000 18.44000 ? 75  SER   B O   1 
ATOM   2222 C  CB  . SER   B 1 31  ? 33.28600 40.58900 -26.67400 1.000 19.96000 ? 75  SER   B CB  1 
ATOM   2223 O  OG  . SER   B 1 31  ? 33.06100 39.20300 -26.47500 1.000 19.10000 ? 75  SER   B OG  1 
ATOM   2224 N  N   . SER   B 1 32  ? 35.87900 38.88300 -25.92400 1.000 18.51000 ? 76  SER   B N   1 
ATOM   2225 C  CA  . SER   B 1 32  ? 36.70100 37.69000 -26.06900 1.000 18.44000 ? 76  SER   B CA  1 
ATOM   2226 C  C   . SER   B 1 32  ? 36.01300 36.58600 -26.85900 1.000 18.47000 ? 76  SER   B C   1 
ATOM   2227 O  O   . SER   B 1 32  ? 36.67800 35.62000 -27.24200 1.000 18.49000 ? 76  SER   B O   1 
ATOM   2228 C  CB  . SER   B 1 32  ? 37.11700 37.16400 -24.69000 1.000 18.07000 ? 76  SER   B CB  1 
ATOM   2229 O  OG  . SER   B 1 32  ? 35.99500 36.77100 -23.91500 1.000 17.82000 ? 76  SER   B OG  1 
ATOM   2230 N  N   . PHE   B 1 33  ? 34.71600 36.70300 -27.11900 1.000 18.69000 ? 77  PHE   B N   1 
ATOM   2231 C  CA  . PHE   B 1 33  ? 33.99800 35.70300 -27.88900 1.000 18.63000 ? 77  PHE   B CA  1 
ATOM   2232 C  C   . PHE   B 1 33  ? 34.00900 35.99300 -29.38300 1.000 18.35000 ? 77  PHE   B C   1 
ATOM   2233 O  O   . PHE   B 1 33  ? 33.28900 35.33000 -30.13500 1.000 18.21000 ? 77  PHE   B O   1 
ATOM   2234 C  CB  . PHE   B 1 33  ? 32.56800 35.58800 -27.37900 1.000 18.71000 ? 77  PHE   B CB  1 
ATOM   2235 C  CG  . PHE   B 1 33  ? 32.48300 35.11500 -25.96000 1.000 18.49000 ? 77  PHE   B CG  1 
ATOM   2236 C  CD1 . PHE   B 1 33  ? 32.61200 33.77200 -25.65700 1.000 18.22000 ? 77  PHE   B CD1 1 
ATOM   2237 C  CD2 . PHE   B 1 33  ? 32.28900 36.01200 -24.92900 1.000 18.89000 ? 77  PHE   B CD2 1 
ATOM   2238 C  CE1 . PHE   B 1 33  ? 32.53400 33.33300 -24.35300 1.000 18.55000 ? 77  PHE   B CE1 1 
ATOM   2239 C  CE2 . PHE   B 1 33  ? 32.21600 35.57700 -23.62800 1.000 19.04000 ? 77  PHE   B CE2 1 
ATOM   2240 C  CZ  . PHE   B 1 33  ? 32.33800 34.23900 -23.34000 1.000 18.94000 ? 77  PHE   B CZ  1 
ATOM   2241 N  N   . ALA   B 1 34  ? 34.79600 36.97200 -29.82400 1.000 18.27000 ? 78  ALA   B N   1 
ATOM   2242 C  CA  . ALA   B 1 34  ? 35.06800 37.12800 -31.24400 1.000 18.25000 ? 78  ALA   B CA  1 
ATOM   2243 C  C   . ALA   B 1 34  ? 35.78000 35.88800 -31.77700 1.000 18.05000 ? 78  ALA   B C   1 
ATOM   2244 O  O   . ALA   B 1 34  ? 36.43400 35.14500 -31.04000 1.000 18.15000 ? 78  ALA   B O   1 
ATOM   2245 C  CB  . ALA   B 1 34  ? 35.91300 38.37300 -31.50200 1.000 18.76000 ? 78  ALA   B CB  1 
ATOM   2246 N  N   . SER   B 1 35  ? 35.65200 35.67100 -33.08300 1.000 18.15000 ? 79  SER   B N   1 
ATOM   2247 C  CA  . SER   B 1 35  ? 36.12000 34.43400 -33.69000 1.000 18.47000 ? 79  SER   B CA  1 
ATOM   2248 C  C   . SER   B 1 35  ? 37.63100 34.46200 -33.88800 1.000 18.56000 ? 79  SER   B C   1 
ATOM   2249 O  O   . SER   B 1 35  ? 38.18500 35.44200 -34.39400 1.000 18.47000 ? 79  SER   B O   1 
ATOM   2250 C  CB  . SER   B 1 35  ? 35.41400 34.20300 -35.02500 1.000 18.68000 ? 79  SER   B CB  1 
ATOM   2251 O  OG  . SER   B 1 35  ? 35.80800 32.97100 -35.59900 1.000 17.75000 ? 79  SER   B OG  1 
ATOM   2252 N  N   . GLY   B 1 36  ? 38.29500 33.38500 -33.47900 1.000 18.39000 ? 80  GLY   B N   1 
ATOM   2253 C  CA  . GLY   B 1 36  ? 39.68500 33.17100 -33.80900 1.000 17.95000 ? 80  GLY   B CA  1 
ATOM   2254 C  C   . GLY   B 1 36  ? 40.69600 33.76600 -32.85500 1.000 17.88000 ? 80  GLY   B C   1 
ATOM   2255 O  O   . GLY   B 1 36  ? 41.88900 33.48400 -32.99800 1.000 17.62000 ? 80  GLY   B O   1 
ATOM   2256 N  N   . PHE   B 1 37  ? 40.26900 34.57500 -31.89400 1.000 17.86000 ? 81  PHE   B N   1 
ATOM   2257 C  CA  . PHE   B 1 37  ? 41.18100 35.13400 -30.90400 1.000 17.76000 ? 81  PHE   B CA  1 
ATOM   2258 C  C   . PHE   B 1 37  ? 40.36300 35.52400 -29.67900 1.000 17.85000 ? 81  PHE   B C   1 
ATOM   2259 O  O   . PHE   B 1 37  ? 39.13700 35.39500 -29.66300 1.000 18.06000 ? 81  PHE   B O   1 
ATOM   2260 C  CB  . PHE   B 1 37  ? 41.97000 36.31500 -31.48100 1.000 17.56000 ? 81  PHE   B CB  1 
ATOM   2261 C  CG  . PHE   B 1 37  ? 41.13100 37.52500 -31.77400 1.000 17.76000 ? 81  PHE   B CG  1 
ATOM   2262 C  CD1 . PHE   B 1 37  ? 40.15800 37.49600 -32.75900 1.000 17.99000 ? 81  PHE   B CD1 1 
ATOM   2263 C  CD2 . PHE   B 1 37  ? 41.33100 38.70000 -31.07800 1.000 17.92000 ? 81  PHE   B CD2 1 
ATOM   2264 C  CE1 . PHE   B 1 37  ? 39.39100 38.60800 -33.02500 1.000 18.34000 ? 81  PHE   B CE1 1 
ATOM   2265 C  CE2 . PHE   B 1 37  ? 40.57200 39.81700 -31.34300 1.000 18.17000 ? 81  PHE   B CE2 1 
ATOM   2266 C  CZ  . PHE   B 1 37  ? 39.59900 39.77200 -32.31600 1.000 18.51000 ? 81  PHE   B CZ  1 
ATOM   2267 N  N   . GLY   B 1 38  ? 41.05100 36.00500 -28.64600 1.000 17.78000 ? 82  GLY   B N   1 
ATOM   2268 C  CA  . GLY   B 1 38  ? 40.39300 36.27000 -27.38200 1.000 17.69000 ? 82  GLY   B CA  1 
ATOM   2269 C  C   . GLY   B 1 38  ? 40.02300 37.71800 -27.13400 1.000 17.85000 ? 82  GLY   B C   1 
ATOM   2270 O  O   . GLY   B 1 38  ? 40.13800 38.20400 -26.00300 1.000 17.64000 ? 82  GLY   B O   1 
ATOM   2271 N  N   . GLY   B 1 39  ? 39.55900 38.41200 -28.17100 1.000 17.96000 ? 83  GLY   B N   1 
ATOM   2272 C  CA  . GLY   B 1 39  ? 39.15300 39.79300 -28.02500 1.000 18.54000 ? 83  GLY   B CA  1 
ATOM   2273 C  C   . GLY   B 1 39  ? 40.35200 40.70000 -27.83600 1.000 18.68000 ? 83  GLY   B C   1 
ATOM   2274 O  O   . GLY   B 1 39  ? 41.50300 40.29800 -27.96900 1.000 17.81000 ? 83  GLY   B O   1 
ATOM   2275 N  N   . GLY   B 1 40  ? 40.06100 41.95300 -27.51900 1.000 18.83000 ? 84  GLY   B N   1 
ATOM   2276 C  CA  . GLY   B 1 40  ? 41.12000 42.90600 -27.26600 1.000 18.65000 ? 84  GLY   B CA  1 
ATOM   2277 C  C   . GLY   B 1 40  ? 40.59600 44.32800 -27.27100 1.000 19.33000 ? 84  GLY   B C   1 
ATOM   2278 O  O   . GLY   B 1 40  ? 39.39100 44.56900 -27.19500 1.000 19.65000 ? 84  GLY   B O   1 
ATOM   2279 N  N   . THR   B 1 41  ? 41.53800 45.26200 -27.35400 1.000 19.11000 ? 85  THR   B N   1 
ATOM   2280 C  CA  . THR   B 1 41  ? 41.25400 46.68900 -27.34900 1.000 19.66000 ? 85  THR   B CA  1 
ATOM   2281 C  C   . THR   B 1 41  ? 41.83400 47.31600 -28.60500 1.000 19.48000 ? 85  THR   B C   1 
ATOM   2282 O  O   . THR   B 1 41  ? 43.01800 47.13300 -28.90100 1.000 18.84000 ? 85  THR   B O   1 
ATOM   2283 C  CB  . THR   B 1 41  ? 41.84600 47.37000 -26.11400 1.000 19.74000 ? 85  THR   B CB  1 
ATOM   2284 O  OG1 . THR   B 1 41  ? 41.29700 46.77900 -24.93100 1.000 20.85000 ? 85  THR   B OG1 1 
ATOM   2285 C  CG2 . THR   B 1 41  ? 41.53600 48.85200 -26.13300 1.000 20.58000 ? 85  THR   B CG2 1 
ATOM   2286 N  N   . ILE   B 1 42  ? 41.00000 48.05300 -29.33400 1.000 19.91000 ? 86  ILE   B N   1 
ATOM   2287 C  CA  . ILE   B 1 42  ? 41.39700 48.73300 -30.56000 1.000 19.96000 ? 86  ILE   B CA  1 
ATOM   2288 C  C   . ILE   B 1 42  ? 41.67300 50.19200 -30.23300 1.000 20.76000 ? 86  ILE   B C   1 
ATOM   2289 O  O   . ILE   B 1 42  ? 40.76700 50.92300 -29.81900 1.000 21.12000 ? 86  ILE   B O   1 
ATOM   2290 C  CB  . ILE   B 1 42  ? 40.31300 48.61800 -31.64400 1.000 19.83000 ? 86  ILE   B CB  1 
ATOM   2291 C  CG1 . ILE   B 1 42  ? 39.97100 47.15600 -31.93100 1.000 19.46000 ? 86  ILE   B CG1 1 
ATOM   2292 C  CG2 . ILE   B 1 42  ? 40.75800 49.31600 -32.91600 1.000 20.10000 ? 86  ILE   B CG2 1 
ATOM   2293 C  CD1 . ILE   B 1 42  ? 38.76100 46.99600 -32.82900 1.000 20.59000 ? 86  ILE   B CD1 1 
ATOM   2294 N  N   . TYR   B 1 43  ? 42.91800 50.61700 -30.41600 1.000 20.47000 ? 87  TYR   B N   1 
ATOM   2295 C  CA  . TYR   B 1 43  ? 43.29700 52.02100 -30.32900 1.000 21.08000 ? 87  TYR   B CA  1 
ATOM   2296 C  C   . TYR   B 1 43  ? 43.39100 52.56400 -31.74900 1.000 21.13000 ? 87  TYR   B C   1 
ATOM   2297 O  O   . TYR   B 1 43  ? 44.09400 51.98700 -32.58500 1.000 20.43000 ? 87  TYR   B O   1 
ATOM   2298 C  CB  . TYR   B 1 43  ? 44.63700 52.19400 -29.60900 1.000 20.68000 ? 87  TYR   B CB  1 
ATOM   2299 C  CG  . TYR   B 1 43  ? 44.71800 51.56200 -28.23600 1.000 20.51000 ? 87  TYR   B CG  1 
ATOM   2300 C  CD1 . TYR   B 1 43  ? 44.88800 50.18700 -28.08900 1.000 19.97000 ? 87  TYR   B CD1 1 
ATOM   2301 C  CD2 . TYR   B 1 43  ? 44.65300 52.34100 -27.08800 1.000 21.19000 ? 87  TYR   B CD2 1 
ATOM   2302 C  CE1 . TYR   B 1 43  ? 44.97100 49.60500 -26.83700 1.000 19.62000 ? 87  TYR   B CE1 1 
ATOM   2303 C  CE2 . TYR   B 1 43  ? 44.73500 51.76900 -25.83000 1.000 20.90000 ? 87  TYR   B CE2 1 
ATOM   2304 C  CZ  . TYR   B 1 43  ? 44.89500 50.40000 -25.71100 1.000 19.62000 ? 87  TYR   B CZ  1 
ATOM   2305 O  OH  . TYR   B 1 43  ? 44.97900 49.82200 -24.46500 1.000 21.66000 ? 87  TYR   B OH  1 
ATOM   2306 N  N   . TYR   B 1 44  ? 42.68900 53.65800 -32.02400 1.000 22.04000 ? 88  TYR   B N   1 
ATOM   2307 C  CA  . TYR   B 1 44  ? 42.68700 54.20900 -33.36900 1.000 22.41000 ? 88  TYR   B CA  1 
ATOM   2308 C  C   . TYR   B 1 44  ? 42.75100 55.72500 -33.31400 1.000 22.81000 ? 88  TYR   B C   1 
ATOM   2309 O  O   . TYR   B 1 44  ? 42.18300 56.34200 -32.40600 1.000 23.13000 ? 88  TYR   B O   1 
ATOM   2310 C  CB  . TYR   B 1 44  ? 41.45200 53.76600 -34.17100 1.000 22.68000 ? 88  TYR   B CB  1 
ATOM   2311 C  CG  . TYR   B 1 44  ? 40.11000 54.21300 -33.63000 1.000 23.16000 ? 88  TYR   B CG  1 
ATOM   2312 C  CD1 . TYR   B 1 44  ? 39.60800 55.47800 -33.90800 1.000 23.79000 ? 88  TYR   B CD1 1 
ATOM   2313 C  CD2 . TYR   B 1 44  ? 39.32500 53.35200 -32.87400 1.000 22.81000 ? 88  TYR   B CD2 1 
ATOM   2314 C  CE1 . TYR   B 1 44  ? 38.38200 55.88200 -33.43000 1.000 24.40000 ? 88  TYR   B CE1 1 
ATOM   2315 C  CE2 . TYR   B 1 44  ? 38.09400 53.74800 -32.39300 1.000 23.80000 ? 88  TYR   B CE2 1 
ATOM   2316 C  CZ  . TYR   B 1 44  ? 37.62900 55.01400 -32.67300 1.000 24.23000 ? 88  TYR   B CZ  1 
ATOM   2317 O  OH  . TYR   B 1 44  ? 36.40500 55.42000 -32.19900 1.000 24.54000 ? 88  TYR   B OH  1 
ATOM   2318 N  N   . PRO   B 1 45  ? 43.43900 56.35000 -34.26800 1.000 22.78000 ? 89  PRO   B N   1 
ATOM   2319 C  CA  . PRO   B 1 45  ? 43.46200 57.81600 -34.31700 1.000 23.90000 ? 89  PRO   B CA  1 
ATOM   2320 C  C   . PRO   B 1 45  ? 42.07100 58.37500 -34.57600 1.000 24.35000 ? 89  PRO   B C   1 
ATOM   2321 O  O   . PRO   B 1 45  ? 41.25100 57.76800 -35.26800 1.000 24.19000 ? 89  PRO   B O   1 
ATOM   2322 C  CB  . PRO   B 1 45  ? 44.41400 58.12100 -35.48100 1.000 23.93000 ? 89  PRO   B CB  1 
ATOM   2323 C  CG  . PRO   B 1 45  ? 45.19400 56.85100 -35.69800 1.000 22.83000 ? 89  PRO   B CG  1 
ATOM   2324 C  CD  . PRO   B 1 45  ? 44.27500 55.73900 -35.31500 1.000 22.28000 ? 89  PRO   B CD  1 
ATOM   2325 N  N   . ARG   B 1 46  ? 41.80900 59.55100 -34.00800 1.000 25.22000 ? 90  ARG   B N   1 
ATOM   2326 C  CA  . ARG   B 1 46  ? 40.48100 60.14600 -34.08700 1.000 25.69000 ? 90  ARG   B CA  1 
ATOM   2327 C  C   . ARG   B 1 46  ? 40.28800 61.03900 -35.30800 1.000 26.45000 ? 90  ARG   B C   1 
ATOM   2328 O  O   . ARG   B 1 46  ? 39.16400 61.14600 -35.81000 1.000 26.33000 ? 90  ARG   B O   1 
ATOM   2329 C  CB  . ARG   B 1 46  ? 40.19000 60.94500 -32.81300 1.000 26.98000 ? 90  ARG   B CB  1 
ATOM   2330 C  CG  . ARG   B 1 46  ? 40.04000 60.08200 -31.56900 1.000 27.05000 ? 90  ARG   B CG  1 
ATOM   2331 C  CD  . ARG   B 1 46  ? 39.88600 60.93600 -30.31900 1.000 28.28000 ? 90  ARG   B CD  1 
ATOM   2332 N  NE  . ARG   B 1 46  ? 38.76400 61.86000 -30.42600 1.000 32.40000 ? 90  ARG   B NE  1 
ATOM   2333 C  CZ  . ARG   B 1 46  ? 38.47400 62.79400 -29.53100 1.000 36.02000 ? 90  ARG   B CZ  1 
ATOM   2334 N  NH1 . ARG   B 1 46  ? 39.20200 62.95300 -28.43600 1.000 40.17000 ? 90  ARG   B NH1 1 
ATOM   2335 N  NH2 . ARG   B 1 46  ? 37.42900 63.59100 -29.73900 1.000 36.30000 ? 90  ARG   B NH2 1 
ATOM   2336 N  N   . GLU   B 1 47  ? 41.34800 61.67600 -35.80500 1.000 26.53000 ? 91  GLU   B N   1 
ATOM   2337 C  CA  . GLU   B 1 47  ? 41.22800 62.58700 -36.93700 1.000 27.39000 ? 91  GLU   B CA  1 
ATOM   2338 C  C   . GLU   B 1 47  ? 41.25700 61.81500 -38.25300 1.000 28.28000 ? 91  GLU   B C   1 
ATOM   2339 O  O   . GLU   B 1 47  ? 42.15600 61.00400 -38.48800 1.000 27.42000 ? 91  GLU   B O   1 
ATOM   2340 C  CB  . GLU   B 1 47  ? 42.34600 63.62800 -36.90200 1.000 26.36000 ? 91  GLU   B CB  1 
ATOM   2341 C  CG  . GLU   B 1 47  ? 42.30600 64.56100 -35.68700 1.000 28.51000 ? 91  GLU   B CG  1 
ATOM   2342 C  CD  . GLU   B 1 47  ? 42.86700 63.93100 -34.41800 1.000 26.71000 ? 91  GLU   B CD  1 
ATOM   2343 O  OE1 . GLU   B 1 47  ? 43.29300 62.75500 -34.45900 1.000 26.26000 ? 91  GLU   B OE1 1 
ATOM   2344 O  OE2 . GLU   B 1 47  ? 42.88400 64.61700 -33.37500 1.000 27.24000 ? 91  GLU   B OE2 1 
ATOM   2345 N  N   . THR   B 1 48  ? 40.27100 62.07600 -39.11200 1.000 29.47000 ? 92  THR   B N   1 
ATOM   2346 C  CA  . THR   B 1 48  ? 40.07400 61.32400 -40.34400 1.000 29.29000 ? 92  THR   B CA  1 
ATOM   2347 C  C   . THR   B 1 48  ? 40.48300 62.09000 -41.59400 1.000 29.01000 ? 92  THR   B C   1 
ATOM   2348 O  O   . THR   B 1 48  ? 40.39900 61.53900 -42.69600 1.000 28.60000 ? 92  THR   B O   1 
ATOM   2349 C  CB  . THR   B 1 48  ? 38.60300 60.90600 -40.47900 1.000 29.26000 ? 92  THR   B CB  1 
ATOM   2350 O  OG1 . THR   B 1 48  ? 37.77000 62.07300 -40.48800 1.000 29.70000 ? 92  THR   B OG1 1 
ATOM   2351 C  CG2 . THR   B 1 48  ? 38.19300 60.01600 -39.32700 1.000 26.84000 ? 92  THR   B CG2 1 
ATOM   2352 N  N   . ASP   B 1 49  ? 40.92800 63.33300 -41.45600 1.000 30.86000 ? 93  ASP   B N   1 
ATOM   2353 C  CA  . ASP   B 1 49  ? 41.08900 64.22800 -42.59000 1.000 31.90000 ? 93  ASP   B CA  1 
ATOM   2354 C  C   . ASP   B 1 49  ? 42.45000 64.12100 -43.26300 1.000 30.12000 ? 93  ASP   B C   1 
ATOM   2355 O  O   . ASP   B 1 49  ? 42.77200 64.96100 -44.10900 1.000 30.98000 ? 93  ASP   B O   1 
ATOM   2356 C  CB  . ASP   B 1 49  ? 40.83200 65.66400 -42.14200 1.000 34.79000 ? 93  ASP   B CB  1 
ATOM   2357 C  CG  . ASP   B 1 49  ? 39.40900 65.87100 -41.67200 1.000 35.48000 ? 93  ASP   B CG  1 
ATOM   2358 O  OD1 . ASP   B 1 49  ? 38.49100 65.83800 -42.52000 1.000 38.31000 ? 93  ASP   B OD1 1 
ATOM   2359 O  OD2 . ASP   B 1 49  ? 39.20300 66.03800 -40.45000 1.000 44.60000 ? 93  ASP   B OD2 1 
ATOM   2360 N  N   . GLU   B 1 50  ? 43.25500 63.11900 -42.91900 1.000 28.72000 ? 94  GLU   B N   1 
ATOM   2361 C  CA  . GLU   B 1 50  ? 44.48800 62.84400 -43.64300 1.000 27.81000 ? 94  GLU   B CA  1 
ATOM   2362 C  C   . GLU   B 1 50  ? 44.43300 61.52900 -44.40500 1.000 27.03000 ? 94  GLU   B C   1 
ATOM   2363 O  O   . GLU   B 1 50  ? 45.43300 61.14300 -45.01500 1.000 27.83000 ? 94  GLU   B O   1 
ATOM   2364 C  CB  . GLU   B 1 50  ? 45.69200 62.84200 -42.69000 1.000 28.10000 ? 94  GLU   B CB  1 
ATOM   2365 C  CG  . GLU   B 1 50  ? 45.99600 64.19300 -42.05600 1.000 28.12000 ? 94  GLU   B CG  1 
ATOM   2366 C  CD  . GLU   B 1 50  ? 47.40600 64.28300 -41.49400 1.000 26.69000 ? 94  GLU   B CD  1 
ATOM   2367 O  OE1 . GLU   B 1 50  ? 48.29700 63.56700 -41.99400 1.000 25.19000 ? 94  GLU   B OE1 1 
ATOM   2368 O  OE2 . GLU   B 1 50  ? 47.62500 65.07300 -40.55200 1.000 28.16000 ? 94  GLU   B OE2 1 
ATOM   2369 N  N   . GLY   B 1 51  ? 43.29800 60.84200 -44.39200 1.000 27.35000 ? 95  GLY   B N   1 
ATOM   2370 C  CA  . GLY   B 1 51  ? 43.15300 59.54600 -45.02600 1.000 25.37000 ? 95  GLY   B CA  1 
ATOM   2371 C  C   . GLY   B 1 51  ? 42.96700 58.44000 -44.00100 1.000 23.96000 ? 95  GLY   B C   1 
ATOM   2372 O  O   . GLY   B 1 51  ? 42.91600 58.66900 -42.79200 1.000 24.05000 ? 95  GLY   B O   1 
ATOM   2373 N  N   . THR   B 1 52  ? 42.85400 57.22100 -44.52100 1.000 23.08000 ? 96  THR   B N   1 
ATOM   2374 C  CA  . THR   B 1 52  ? 42.75700 56.04000 -43.68100 1.000 22.96000 ? 96  THR   B CA  1 
ATOM   2375 C  C   . THR   B 1 52  ? 44.15000 55.58600 -43.24800 1.000 22.56000 ? 96  THR   B C   1 
ATOM   2376 O  O   . THR   B 1 52  ? 45.17200 56.03900 -43.76700 1.000 22.27000 ? 96  THR   B O   1 
ATOM   2377 C  CB  . THR   B 1 52  ? 42.02600 54.91700 -44.41400 1.000 22.77000 ? 96  THR   B CB  1 
ATOM   2378 O  OG1 . THR   B 1 52  ? 42.71200 54.61800 -45.63400 1.000 22.55000 ? 96  THR   B OG1 1 
ATOM   2379 C  CG2 . THR   B 1 52  ? 40.60500 55.33600 -44.73100 1.000 23.84000 ? 96  THR   B CG2 1 
ATOM   2380 N  N   . PHE   B 1 53  ? 44.18700 54.68200 -42.27500 1.000 22.06000 ? 97  PHE   B N   1 
ATOM   2381 C  CA  . PHE   B 1 53  ? 45.43600 54.26800 -41.66000 1.000 21.76000 ? 97  PHE   B CA  1 
ATOM   2382 C  C   . PHE   B 1 53  ? 45.61300 52.76100 -41.74700 1.000 21.35000 ? 97  PHE   B C   1 
ATOM   2383 O  O   . PHE   B 1 53  ? 44.64500 52.00300 -41.84500 1.000 21.24000 ? 97  PHE   B O   1 
ATOM   2384 C  CB  . PHE   B 1 53  ? 45.50300 54.68500 -40.18900 1.000 21.54000 ? 97  PHE   B CB  1 
ATOM   2385 C  CG  . PHE   B 1 53  ? 45.27800 56.14500 -39.95700 1.000 22.30000 ? 97  PHE   B CG  1 
ATOM   2386 C  CD1 . PHE   B 1 53  ? 46.32600 57.04200 -40.05400 1.000 22.21000 ? 97  PHE   B CD1 1 
ATOM   2387 C  CD2 . PHE   B 1 53  ? 44.02300 56.61900 -39.62200 1.000 22.96000 ? 97  PHE   B CD2 1 
ATOM   2388 C  CE1 . PHE   B 1 53  ? 46.12400 58.38400 -39.83500 1.000 23.30000 ? 97  PHE   B CE1 1 
ATOM   2389 C  CE2 . PHE   B 1 53  ? 43.81700 57.96100 -39.40200 1.000 23.50000 ? 97  PHE   B CE2 1 
ATOM   2390 C  CZ  . PHE   B 1 53  ? 44.87100 58.84400 -39.50800 1.000 24.15000 ? 97  PHE   B CZ  1 
ATOM   2391 N  N   . GLY   B 1 54  ? 46.87900 52.34100 -41.68900 1.000 20.46000 ? 98  GLY   B N   1 
ATOM   2392 C  CA  . GLY   B 1 54  ? 47.20600 50.93900 -41.55800 1.000 19.37000 ? 98  GLY   B CA  1 
ATOM   2393 C  C   . GLY   B 1 54  ? 46.95400 50.42500 -40.15100 1.000 18.87000 ? 98  GLY   B C   1 
ATOM   2394 O  O   . GLY   B 1 54  ? 46.64700 51.18100 -39.23400 1.000 19.06000 ? 98  GLY   B O   1 
ATOM   2395 N  N   . ALA   B 1 55  ? 47.10100 49.11200 -39.98700 1.000 18.05000 ? 99  ALA   B N   1 
ATOM   2396 C  CA  . ALA   B 1 55  ? 46.74400 48.44700 -38.74200 1.000 17.57000 ? 99  ALA   B CA  1 
ATOM   2397 C  C   . ALA   B 1 55  ? 47.81100 47.43900 -38.34600 1.000 16.93000 ? 99  ALA   B C   1 
ATOM   2398 O  O   . ALA   B 1 55  ? 48.38000 46.75500 -39.20100 1.000 16.84000 ? 99  ALA   B O   1 
ATOM   2399 C  CB  . ALA   B 1 55  ? 45.39400 47.73500 -38.86000 1.000 18.21000 ? 99  ALA   B CB  1 
ATOM   2400 N  N   . VAL   B 1 56  ? 48.06200 47.34000 -37.04000 1.000 16.73000 ? 100 VAL   B N   1 
ATOM   2401 C  CA  . VAL   B 1 56  ? 48.98000 46.35700 -36.47900 1.000 16.60000 ? 100 VAL   B CA  1 
ATOM   2402 C  C   . VAL   B 1 56  ? 48.26800 45.62300 -35.34800 1.000 16.38000 ? 100 VAL   B C   1 
ATOM   2403 O  O   . VAL   B 1 56  ? 47.61600 46.25100 -34.50800 1.000 16.65000 ? 100 VAL   B O   1 
ATOM   2404 C  CB  . VAL   B 1 56  ? 50.29200 47.00900 -35.99000 1.000 17.01000 ? 100 VAL   B CB  1 
ATOM   2405 C  CG1 . VAL   B 1 56  ? 50.01500 48.20800 -35.08600 1.000 17.81000 ? 100 VAL   B CG1 1 
ATOM   2406 C  CG2 . VAL   B 1 56  ? 51.18100 45.99200 -35.29500 1.000 16.76000 ? 100 VAL   B CG2 1 
ATOM   2407 N  N   . ALA   B 1 57  ? 48.36000 44.29600 -35.35300 1.000 16.13000 ? 101 ALA   B N   1 
ATOM   2408 C  CA  . ALA   B 1 57  ? 47.82700 43.45900 -34.28400 1.000 16.07000 ? 101 ALA   B CA  1 
ATOM   2409 C  C   . ALA   B 1 57  ? 48.97100 43.03600 -33.37300 1.000 15.93000 ? 101 ALA   B C   1 
ATOM   2410 O  O   . ALA   B 1 57  ? 50.00300 42.55400 -33.85300 1.000 15.92000 ? 101 ALA   B O   1 
ATOM   2411 C  CB  . ALA   B 1 57  ? 47.11200 42.23300 -34.85200 1.000 15.94000 ? 101 ALA   B CB  1 
ATOM   2412 N  N   . VAL   B 1 58  ? 48.79100 43.22000 -32.06400 1.000 16.11000 ? 102 VAL   B N   1 
ATOM   2413 C  CA  . VAL   B 1 58  ? 49.85900 43.03800 -31.08400 1.000 16.10000 ? 102 VAL   B CA  1 
ATOM   2414 C  C   . VAL   B 1 58  ? 49.50100 41.86700 -30.17400 1.000 16.24000 ? 102 VAL   B C   1 
ATOM   2415 O  O   . VAL   B 1 58  ? 48.44400 41.86700 -29.53200 1.000 16.45000 ? 102 VAL   B O   1 
ATOM   2416 C  CB  . VAL   B 1 58  ? 50.10200 44.32100 -30.27600 1.000 16.48000 ? 102 VAL   B CB  1 
ATOM   2417 C  CG1 . VAL   B 1 58  ? 51.41400 44.23200 -29.51900 1.000 16.86000 ? 102 VAL   B CG1 1 
ATOM   2418 C  CG2 . VAL   B 1 58  ? 50.09700 45.52400 -31.20200 1.000 16.60000 ? 102 VAL   B CG2 1 
ATOM   2419 N  N   . ALA   B 1 59  ? 50.39300 40.87400 -30.10700 1.000 16.33000 ? 103 ALA   B N   1 
ATOM   2420 C  CA  . ALA   B 1 59  ? 50.12900 39.65600 -29.36400 1.000 16.38000 ? 103 ALA   B CA  1 
ATOM   2421 C  C   . ALA   B 1 59  ? 50.96100 39.59400 -28.09000 1.000 16.44000 ? 103 ALA   B C   1 
ATOM   2422 O  O   . ALA   B 1 59  ? 52.11700 40.02700 -28.08200 1.000 16.52000 ? 103 ALA   B O   1 
ATOM   2423 C  CB  . ALA   B 1 59  ? 50.42800 38.41400 -30.21000 1.000 16.35000 ? 103 ALA   B CB  1 
ATOM   2424 N  N   . PRO   B 1 60  ? 50.41000 39.05300 -27.01000 1.000 16.72000 ? 104 PRO   B N   1 
ATOM   2425 C  CA  . PRO   B 1 60  ? 51.19400 38.91400 -25.78200 1.000 16.92000 ? 104 PRO   B CA  1 
ATOM   2426 C  C   . PRO   B 1 60  ? 51.96900 37.61000 -25.74200 1.000 17.01000 ? 104 PRO   B C   1 
ATOM   2427 O  O   . PRO   B 1 60  ? 51.88200 36.79100 -26.66200 1.000 16.83000 ? 104 PRO   B O   1 
ATOM   2428 C  CB  . PRO   B 1 60  ? 50.12300 38.96600 -24.69200 1.000 17.32000 ? 104 PRO   B CB  1 
ATOM   2429 C  CG  . PRO   B 1 60  ? 48.95200 38.30800 -25.33100 1.000 17.34000 ? 104 PRO   B CG  1 
ATOM   2430 C  CD  . PRO   B 1 60  ? 49.00400 38.67300 -26.80200 1.000 16.82000 ? 104 PRO   B CD  1 
ATOM   2431 N  N   . GLY   B 1 61  ? 52.73300 37.40600 -24.67100 1.000 17.05000 ? 105 GLY   B N   1 
ATOM   2432 C  CA  . GLY   B 1 61  ? 53.50100 36.19300 -24.50800 1.000 17.45000 ? 105 GLY   B CA  1 
ATOM   2433 C  C   . GLY   B 1 61  ? 52.71100 35.07400 -23.84800 1.000 18.04000 ? 105 GLY   B C   1 
ATOM   2434 O  O   . GLY   B 1 61  ? 51.52300 35.18700 -23.55200 1.000 18.03000 ? 105 GLY   B O   1 
ATOM   2435 N  N   . PHE   B 1 62  ? 53.41300 33.97200 -23.61600 1.000 18.08000 ? 106 PHE   B N   1 
ATOM   2436 C  CA  . PHE   B 1 62  ? 52.83200 32.79600 -22.98600 1.000 18.29000 ? 106 PHE   B CA  1 
ATOM   2437 C  C   . PHE   B 1 62  ? 52.34600 33.12500 -21.57900 1.000 18.68000 ? 106 PHE   B C   1 
ATOM   2438 O  O   . PHE   B 1 62  ? 53.05600 33.77100 -20.80400 1.000 18.57000 ? 106 PHE   B O   1 
ATOM   2439 C  CB  . PHE   B 1 62  ? 53.88600 31.69600 -22.97300 1.000 18.37000 ? 106 PHE   B CB  1 
ATOM   2440 C  CG  . PHE   B 1 62  ? 53.55000 30.51300 -22.12700 1.000 18.62000 ? 106 PHE   B CG  1 
ATOM   2441 C  CD1 . PHE   B 1 62  ? 52.71400 29.52500 -22.60100 1.000 18.88000 ? 106 PHE   B CD1 1 
ATOM   2442 C  CD2 . PHE   B 1 62  ? 54.11400 30.36500 -20.87000 1.000 18.68000 ? 106 PHE   B CD2 1 
ATOM   2443 C  CE1 . PHE   B 1 62  ? 52.41800 28.42600 -21.83000 1.000 19.24000 ? 106 PHE   B CE1 1 
ATOM   2444 C  CE2 . PHE   B 1 62  ? 53.82200 29.26400 -20.09400 1.000 19.61000 ? 106 PHE   B CE2 1 
ATOM   2445 C  CZ  . PHE   B 1 62  ? 52.97200 28.29500 -20.57500 1.000 19.81000 ? 106 PHE   B CZ  1 
ATOM   2446 N  N   . THR   B 1 63  ? 51.13300 32.68300 -21.25900 1.000 18.89000 ? 107 THR   B N   1 
ATOM   2447 C  CA  . THR   B 1 63  ? 50.41800 33.07100 -20.03900 1.000 19.09000 ? 107 THR   B CA  1 
ATOM   2448 C  C   . THR   B 1 63  ? 50.59500 34.56300 -19.75800 1.000 19.09000 ? 107 THR   B C   1 
ATOM   2449 O  O   . THR   B 1 63  ? 51.18700 34.98200 -18.76300 1.000 22.85000 ? 107 THR   B O   1 
ATOM   2450 C  CB  . THR   B 1 63  ? 50.84900 32.23100 -18.83500 1.000 19.30000 ? 107 THR   B CB  1 
ATOM   2451 O  OG1 . THR   B 1 63  ? 52.22000 32.48200 -18.52600 1.000 18.53000 ? 107 THR   B OG1 1 
ATOM   2452 C  CG2 . THR   B 1 63  ? 50.67900 30.75800 -19.12100 1.000 19.50000 ? 107 THR   B CG2 1 
ATOM   2453 N  N   . ALA   B 1 64  ? 50.08200 35.36400 -20.68500 1.000 18.94000 ? 108 ALA   B N   1 
ATOM   2454 C  CA  . ALA   B 1 64  ? 50.06300 36.81000 -20.54000 1.000 18.82000 ? 108 ALA   B CA  1 
ATOM   2455 C  C   . ALA   B 1 64  ? 48.84600 37.34100 -21.27800 1.000 18.49000 ? 108 ALA   B C   1 
ATOM   2456 O  O   . ALA   B 1 64  ? 48.21100 36.63000 -22.05900 1.000 17.99000 ? 108 ALA   B O   1 
ATOM   2457 C  CB  . ALA   B 1 64  ? 51.35200 37.45000 -21.06100 1.000 18.36000 ? 108 ALA   B CB  1 
ATOM   2458 N  N   . SER   B 1 65  ? 48.51300 38.59800 -21.01700 1.000 18.41000 ? 109 SER   B N   1 
ATOM   2459 C  CA  . SER   B 1 65  ? 47.33000 39.20200 -21.60600 1.000 18.18000 ? 109 SER   B CA  1 
ATOM   2460 C  C   . SER   B 1 65  ? 47.70500 40.54300 -22.21900 1.000 17.95000 ? 109 SER   B C   1 
ATOM   2461 O  O   . SER   B 1 65  ? 48.84100 41.01100 -22.09900 1.000 17.83000 ? 109 SER   B O   1 
ATOM   2462 C  CB  . SER   B 1 65  ? 46.21500 39.37100 -20.56800 1.000 17.81000 ? 109 SER   B CB  1 
ATOM   2463 O  OG  . SER   B 1 65  ? 46.44700 40.52100 -19.77600 1.000 17.69000 ? 109 SER   B OG  1 
ATOM   2464 N  N   . GLN   B 1 66  ? 46.72700 41.17100 -22.87600 1.000 17.76000 ? 110 GLN   B N   1 
ATOM   2465 C  CA  . GLN   B 1 66  ? 46.97700 42.44900 -23.53200 1.000 17.74000 ? 110 GLN   B CA  1 
ATOM   2466 C  C   . GLN   B 1 66  ? 47.47800 43.50700 -22.56100 1.000 17.76000 ? 110 GLN   B C   1 
ATOM   2467 O  O   . GLN   B 1 66  ? 48.12100 44.46900 -22.99100 1.000 17.69000 ? 110 GLN   B O   1 
ATOM   2468 C  CB  . GLN   B 1 66  ? 45.71300 42.94200 -24.23400 1.000 17.88000 ? 110 GLN   B CB  1 
ATOM   2469 C  CG  . GLN   B 1 66  ? 44.54400 43.17400 -23.30900 1.000 17.93000 ? 110 GLN   B CG  1 
ATOM   2470 C  CD  . GLN   B 1 66  ? 43.34800 43.77100 -24.01200 1.000 18.46000 ? 110 GLN   B CD  1 
ATOM   2471 O  OE1 . GLN   B 1 66  ? 43.42100 44.86700 -24.55800 1.000 18.45000 ? 110 GLN   B OE1 1 
ATOM   2472 N  NE2 . GLN   B 1 66  ? 42.23800 43.05000 -24.00300 1.000 18.50000 ? 110 GLN   B NE2 1 
ATOM   2473 N  N   . GLY   B 1 67  ? 47.20200 43.35000 -21.26400 1.000 17.89000 ? 111 GLY   B N   1 
ATOM   2474 C  CA  . GLY   B 1 67  ? 47.71600 44.29300 -20.28700 1.000 18.26000 ? 111 GLY   B CA  1 
ATOM   2475 C  C   . GLY   B 1 67  ? 49.22100 44.45200 -20.34900 1.000 18.47000 ? 111 GLY   B C   1 
ATOM   2476 O  O   . GLY   B 1 67  ? 49.73800 45.55800 -20.18000 1.000 18.12000 ? 111 GLY   B O   1 
ATOM   2477 N  N   . SER   B 1 68  ? 49.94500 43.36100 -20.61500 1.000 17.98000 ? 112 SER   B N   1 
ATOM   2478 C  CA  . SER   B 1 68  ? 51.39300 43.43500 -20.76300 1.000 17.98000 ? 112 SER   B CA  1 
ATOM   2479 C  C   . SER   B 1 68  ? 51.83100 44.20500 -22.00300 1.000 17.85000 ? 112 SER   B C   1 
ATOM   2480 O  O   . SER   B 1 68  ? 53.02400 44.49600 -22.12800 1.000 17.81000 ? 112 SER   B O   1 
ATOM   2481 C  CB  . SER   B 1 68  ? 51.99600 42.02900 -20.79700 1.000 18.13000 ? 112 SER   B CB  1 
ATOM   2482 O  OG  . SER   B 1 68  ? 51.48100 41.25900 -21.87000 1.000 17.77000 ? 112 SER   B OG  1 
ATOM   2483 N  N   . MET   B 1 69  ? 50.91000 44.53900 -22.91100 1.000 17.71000 ? 113 MET   B N   1 
ATOM   2484 C  CA  . MET   B 1 69  ? 51.24600 45.22100 -24.15700 1.000 17.68000 ? 113 MET   B CA  1 
ATOM   2485 C  C   . MET   B 1 69  ? 50.51200 46.54500 -24.31400 1.000 17.83000 ? 113 MET   B C   1 
ATOM   2486 O  O   . MET   B 1 69  ? 50.63600 47.19200 -25.36200 1.000 17.95000 ? 113 MET   B O   1 
ATOM   2487 C  CB  . MET   B 1 69  ? 50.93500 44.32200 -25.35900 1.000 17.46000 ? 113 MET   B CB  1 
ATOM   2488 C  CG  . MET   B 1 69  ? 51.52300 42.92900 -25.27600 1.000 17.62000 ? 113 MET   B CG  1 
ATOM   2489 S  SD  . MET   B 1 69  ? 53.31700 42.91500 -25.26100 1.000 16.61000 ? 113 MET   B SD  1 
ATOM   2490 C  CE  . MET   B 1 69  ? 53.69800 43.40200 -26.94400 1.000 17.22000 ? 113 MET   B CE  1 
ATOM   2491 N  N   . SER   B 1 70  ? 49.76000 46.96900 -23.29800 1.000 17.88000 ? 114 SER   B N   1 
ATOM   2492 C  CA  . SER   B 1 70  ? 48.84600 48.09500 -23.44500 1.000 18.14000 ? 114 SER   B CA  1 
ATOM   2493 C  C   . SER   B 1 70  ? 49.55700 49.42000 -23.68600 1.000 18.90000 ? 114 SER   B C   1 
ATOM   2494 O  O   . SER   B 1 70  ? 48.92500 50.36000 -24.17600 1.000 19.01000 ? 114 SER   B O   1 
ATOM   2495 C  CB  . SER   B 1 70  ? 47.96300 48.21300 -22.20200 1.000 17.74000 ? 114 SER   B CB  1 
ATOM   2496 O  OG  . SER   B 1 70  ? 48.73400 48.60100 -21.07500 1.000 17.41000 ? 114 SER   B OG  1 
ATOM   2497 N  N   . TRP   B 1 71  ? 50.84000 49.53600 -23.34600 1.000 18.95000 ? 115 TRP   B N   1 
ATOM   2498 C  CA  . TRP   B 1 71  ? 51.49600 50.82100 -23.54400 1.000 19.08000 ? 115 TRP   B CA  1 
ATOM   2499 C  C   . TRP   B 1 71  ? 51.81000 51.07500 -25.00500 1.000 19.22000 ? 115 TRP   B C   1 
ATOM   2500 O  O   . TRP   B 1 71  ? 52.06500 52.22400 -25.38200 1.000 19.70000 ? 115 TRP   B O   1 
ATOM   2501 C  CB  . TRP   B 1 71  ? 52.76800 50.92500 -22.71200 1.000 19.17000 ? 115 TRP   B CB  1 
ATOM   2502 C  CG  . TRP   B 1 71  ? 53.92500 50.12200 -23.19700 1.000 19.20000 ? 115 TRP   B CG  1 
ATOM   2503 C  CD1 . TRP   B 1 71  ? 54.18200 48.81600 -22.92100 1.000 18.88000 ? 115 TRP   B CD1 1 
ATOM   2504 C  CD2 . TRP   B 1 71  ? 55.01500 50.58500 -24.00300 1.000 19.38000 ? 115 TRP   B CD2 1 
ATOM   2505 N  NE1 . TRP   B 1 71  ? 55.35800 48.42800 -23.51600 1.000 18.92000 ? 115 TRP   B NE1 1 
ATOM   2506 C  CE2 . TRP   B 1 71  ? 55.88900 49.49700 -24.18700 1.000 19.41000 ? 115 TRP   B CE2 1 
ATOM   2507 C  CE3 . TRP   B 1 71  ? 55.33200 51.81100 -24.59400 1.000 19.79000 ? 115 TRP   B CE3 1 
ATOM   2508 C  CZ2 . TRP   B 1 71  ? 57.05700 49.59500 -24.93700 1.000 19.56000 ? 115 TRP   B CZ2 1 
ATOM   2509 C  CZ3 . TRP   B 1 71  ? 56.49300 51.90700 -25.33900 1.000 20.21000 ? 115 TRP   B CZ3 1 
ATOM   2510 C  CH2 . TRP   B 1 71  ? 57.34100 50.80600 -25.50200 1.000 19.86000 ? 115 TRP   B CH2 1 
ATOM   2511 N  N   . TYR   B 1 72  ? 51.79600 50.03100 -25.83200 1.000 19.05000 ? 116 TYR   B N   1 
ATOM   2512 C  CA  . TYR   B 1 72  ? 51.87100 50.22600 -27.27000 1.000 19.21000 ? 116 TYR   B CA  1 
ATOM   2513 C  C   . TYR   B 1 72  ? 50.60800 50.86500 -27.82700 1.000 19.80000 ? 116 TYR   B C   1 
ATOM   2514 O  O   . TYR   B 1 72  ? 50.66900 51.52200 -28.87000 1.000 20.08000 ? 116 TYR   B O   1 
ATOM   2515 C  CB  . TYR   B 1 72  ? 52.12200 48.88700 -27.95600 1.000 18.85000 ? 116 TYR   B CB  1 
ATOM   2516 C  CG  . TYR   B 1 72  ? 53.45000 48.27300 -27.60100 1.000 18.67000 ? 116 TYR   B CG  1 
ATOM   2517 C  CD1 . TYR   B 1 72  ? 54.62400 48.72700 -28.18600 1.000 18.68000 ? 116 TYR   B CD1 1 
ATOM   2518 C  CD2 . TYR   B 1 72  ? 53.53300 47.23800 -26.68400 1.000 18.38000 ? 116 TYR   B CD2 1 
ATOM   2519 C  CE1 . TYR   B 1 72  ? 55.84300 48.16400 -27.86700 1.000 18.45000 ? 116 TYR   B CE1 1 
ATOM   2520 C  CE2 . TYR   B 1 72  ? 54.74300 46.67200 -26.35400 1.000 18.35000 ? 116 TYR   B CE2 1 
ATOM   2521 C  CZ  . TYR   B 1 72  ? 55.89500 47.13500 -26.94600 1.000 18.37000 ? 116 TYR   B CZ  1 
ATOM   2522 O  OH  . TYR   B 1 72  ? 57.09800 46.56200 -26.61000 1.000 18.09000 ? 116 TYR   B OH  1 
ATOM   2523 N  N   . GLY   B 1 73  ? 49.47400 50.69500 -27.15400 1.000 19.67000 ? 117 GLY   B N   1 
ATOM   2524 C  CA  . GLY   B 1 73  ? 48.19600 51.17800 -27.64000 1.000 20.30000 ? 117 GLY   B CA  1 
ATOM   2525 C  C   . GLY   B 1 73  ? 48.16000 52.63900 -28.04100 1.000 20.77000 ? 117 GLY   B C   1 
ATOM   2526 O  O   . GLY   B 1 73  ? 48.07000 52.95500 -29.22900 1.000 20.93000 ? 117 GLY   B O   1 
ATOM   2527 N  N   . GLU   B 1 74  ? 48.21700 53.54600 -27.07000 1.000 21.35000 ? 118 GLU   B N   1 
ATOM   2528 C  CA  . GLU   B 1 74  ? 48.14900 54.96100 -27.40200 1.000 22.95000 ? 118 GLU   B CA  1 
ATOM   2529 C  C   . GLU   B 1 74  ? 49.48500 55.51700 -27.86700 1.000 22.71000 ? 118 GLU   B C   1 
ATOM   2530 O  O   . GLU   B 1 74  ? 49.51000 56.56200 -28.52200 1.000 22.67000 ? 118 GLU   B O   1 
ATOM   2531 C  CB  . GLU   B 1 74  ? 47.64500 55.76400 -26.20300 1.000 24.43000 ? 118 GLU   B CB  1 
ATOM   2532 C  CG  . GLU   B 1 74  ? 46.26000 55.36000 -25.74200 1.000 25.75000 ? 118 GLU   B CG  1 
ATOM   2533 C  CD  . GLU   B 1 74  ? 45.67200 56.32300 -24.72800 1.000 29.53000 ? 118 GLU   B CD  1 
ATOM   2534 O  OE1 . GLU   B 1 74  ? 46.21200 57.44000 -24.57500 1.000 29.50000 ? 118 GLU   B OE1 1 
ATOM   2535 O  OE2 . GLU   B 1 74  ? 44.66300 55.96200 -24.08600 1.000 32.37000 ? 118 GLU   B OE2 1 
ATOM   2536 N  N   . ARG   B 1 75  ? 50.59000 54.85100 -27.54300 1.000 22.46000 ? 119 ARG   B N   1 
ATOM   2537 C  CA  . ARG   B 1 75  ? 51.89200 55.30900 -28.00900 1.000 22.66000 ? 119 ARG   B CA  1 
ATOM   2538 C  C   . ARG   B 1 75  ? 51.96100 55.27100 -29.53000 1.000 22.23000 ? 119 ARG   B C   1 
ATOM   2539 O  O   . ARG   B 1 75  ? 52.17100 56.29800 -30.18300 1.000 22.85000 ? 119 ARG   B O   1 
ATOM   2540 C  CB  . ARG   B 1 75  ? 52.99700 54.44700 -27.39600 1.000 22.55000 ? 119 ARG   B CB  1 
ATOM   2541 C  CG  . ARG   B 1 75  ? 54.41000 54.85900 -27.77200 1.000 23.88000 ? 119 ARG   B CG  1 
ATOM   2542 C  CD  . ARG   B 1 75  ? 54.73700 56.23300 -27.23900 1.000 25.94000 ? 119 ARG   B CD  1 
ATOM   2543 N  NE  . ARG   B 1 75  ? 56.16100 56.53700 -27.29900 1.000 25.77000 ? 119 ARG   B NE  1 
ATOM   2544 C  CZ  . ARG   B 1 75  ? 56.99800 56.42200 -26.27600 1.000 24.86000 ? 119 ARG   B CZ  1 
ATOM   2545 N  NH1 . ARG   B 1 75  ? 56.59000 55.99000 -25.09300 1.000 25.20000 ? 119 ARG   B NH1 1 
ATOM   2546 N  NH2 . ARG   B 1 75  ? 58.27400 56.75500 -26.44100 1.000 25.22000 ? 119 ARG   B NH2 1 
ATOM   2547 N  N   . VAL   B 1 76  ? 51.75500 54.08900 -30.11100 1.000 21.47000 ? 120 VAL   B N   1 
ATOM   2548 C  CA  . VAL   B 1 76  ? 51.91900 53.92000 -31.55100 1.000 21.52000 ? 120 VAL   B CA  1 
ATOM   2549 C  C   . VAL   B 1 76  ? 50.73000 54.49100 -32.31100 1.000 21.96000 ? 120 VAL   B C   1 
ATOM   2550 O  O   . VAL   B 1 76  ? 50.90200 55.13500 -33.35100 1.000 21.87000 ? 120 VAL   B O   1 
ATOM   2551 C  CB  . VAL   B 1 76  ? 52.14800 52.43500 -31.88800 1.000 21.06000 ? 120 VAL   B CB  1 
ATOM   2552 C  CG1 . VAL   B 1 76  ? 52.28100 52.24900 -33.38600 1.000 20.88000 ? 120 VAL   B CG1 1 
ATOM   2553 C  CG2 . VAL   B 1 76  ? 53.39000 51.91600 -31.18300 1.000 21.13000 ? 120 VAL   B CG2 1 
ATOM   2554 N  N   . ALA   B 1 77  ? 49.50900 54.27900 -31.80900 1.000 21.98000 ? 121 ALA   B N   1 
ATOM   2555 C  CA  . ALA   B 1 77  ? 48.32500 54.73700 -32.53200 1.000 22.36000 ? 121 ALA   B CA  1 
ATOM   2556 C  C   . ALA   B 1 77  ? 48.26800 56.25600 -32.63900 1.000 22.81000 ? 121 ALA   B C   1 
ATOM   2557 O  O   . ALA   B 1 77  ? 47.64800 56.78500 -33.56800 1.000 22.79000 ? 121 ALA   B O   1 
ATOM   2558 C  CB  . ALA   B 1 77  ? 47.05300 54.20900 -31.87200 1.000 22.16000 ? 121 ALA   B CB  1 
ATOM   2559 N  N   . SER   B 1 78  ? 48.89700 56.97600 -31.70700 1.000 23.24000 ? 122 SER   B N   1 
ATOM   2560 C  CA  . SER   B 1 78  ? 48.92100 58.43100 -31.79700 1.000 24.58000 ? 122 SER   B CA  1 
ATOM   2561 C  C   . SER   B 1 78  ? 49.80500 58.93000 -32.92700 1.000 24.86000 ? 122 SER   B C   1 
ATOM   2562 O  O   . SER   B 1 78  ? 49.74900 60.11800 -33.25700 1.000 25.47000 ? 122 SER   B O   1 
ATOM   2563 C  CB  . SER   B 1 78  ? 49.39100 59.04400 -30.47500 1.000 25.79000 ? 122 SER   B CB  1 
ATOM   2564 O  OG  . SER   B 1 78  ? 50.74800 58.73500 -30.21300 1.000 25.42000 ? 122 SER   B OG  1 
ATOM   2565 N  N   . HIS   B 1 79  ? 50.61800 58.06100 -33.51900 1.000 24.07000 ? 123 HIS   B N   1 
ATOM   2566 C  CA  . HIS   B 1 79  ? 51.48300 58.43700 -34.62500 1.000 23.81000 ? 123 HIS   B CA  1 
ATOM   2567 C  C   . HIS   B 1 79  ? 50.87800 58.11600 -35.98500 1.000 22.92000 ? 123 HIS   B C   1 
ATOM   2568 O  O   . HIS   B 1 79  ? 51.50300 58.40800 -37.00900 1.000 22.36000 ? 123 HIS   B O   1 
ATOM   2569 C  CB  . HIS   B 1 79  ? 52.84800 57.75900 -34.48100 1.000 23.76000 ? 123 HIS   B CB  1 
ATOM   2570 C  CG  . HIS   B 1 79  ? 53.78700 58.48100 -33.56300 1.000 24.02000 ? 123 HIS   B CG  1 
ATOM   2571 N  ND1 . HIS   B 1 79  ? 53.78700 58.29600 -32.19700 1.000 24.71000 ? 123 HIS   B ND1 1 
ATOM   2572 C  CD2 . HIS   B 1 79  ? 54.75700 59.39300 -33.81800 1.000 24.11000 ? 123 HIS   B CD2 1 
ATOM   2573 C  CE1 . HIS   B 1 79  ? 54.71800 59.05800 -31.65100 1.000 25.69000 ? 123 HIS   B CE1 1 
ATOM   2574 N  NE2 . HIS   B 1 79  ? 55.31900 59.73500 -32.61200 1.000 26.07000 ? 123 HIS   B NE2 1 
ATOM   2575 N  N   . GLY   B 1 80  ? 49.68200 57.53200 -36.02500 1.000 22.86000 ? 124 GLY   B N   1 
ATOM   2576 C  CA  . GLY   B 1 80  ? 48.98800 57.33000 -37.28300 1.000 22.30000 ? 124 GLY   B CA  1 
ATOM   2577 C  C   . GLY   B 1 80  ? 48.72700 55.88400 -37.64900 1.000 20.98000 ? 124 GLY   B C   1 
ATOM   2578 O  O   . GLY   B 1 80  ? 48.71100 55.53500 -38.83200 1.000 21.19000 ? 124 GLY   B O   1 
ATOM   2579 N  N   . PHE   B 1 81  ? 48.50700 55.03200 -36.65200 1.000 21.13000 ? 125 PHE   B N   1 
ATOM   2580 C  CA  . PHE   B 1 81  ? 48.27200 53.61600 -36.88100 1.000 20.94000 ? 125 PHE   B CA  1 
ATOM   2581 C  C   . PHE   B 1 81  ? 47.08800 53.15100 -36.05100 1.000 20.17000 ? 125 PHE   B C   1 
ATOM   2582 O  O   . PHE   B 1 81  ? 46.70700 53.78300 -35.06500 1.000 20.44000 ? 125 PHE   B O   1 
ATOM   2583 C  CB  . PHE   B 1 81  ? 49.50500 52.77600 -36.53700 1.000 20.80000 ? 125 PHE   B CB  1 
ATOM   2584 C  CG  . PHE   B 1 81  ? 50.72700 53.14000 -37.32500 1.000 20.62000 ? 125 PHE   B CG  1 
ATOM   2585 C  CD1 . PHE   B 1 81  ? 50.94600 52.58900 -38.57700 1.000 20.34000 ? 125 PHE   B CD1 1 
ATOM   2586 C  CD2 . PHE   B 1 81  ? 51.65900 54.02800 -36.81500 1.000 21.12000 ? 125 PHE   B CD2 1 
ATOM   2587 C  CE1 . PHE   B 1 81  ? 52.06900 52.92000 -39.30500 1.000 20.44000 ? 125 PHE   B CE1 1 
ATOM   2588 C  CE2 . PHE   B 1 81  ? 52.78600 54.36200 -37.54100 1.000 21.01000 ? 125 PHE   B CE2 1 
ATOM   2589 C  CZ  . PHE   B 1 81  ? 52.98900 53.80500 -38.78800 1.000 20.63000 ? 125 PHE   B CZ  1 
ATOM   2590 N  N   . ILE   B 1 82  ? 46.50200 52.03400 -36.46600 1.000 19.28000 ? 126 ILE   B N   1 
ATOM   2591 C  CA  . ILE   B 1 82  ? 45.46600 51.35500 -35.69800 1.000 19.03000 ? 126 ILE   B CA  1 
ATOM   2592 C  C   . ILE   B 1 82  ? 46.11900 50.16800 -35.00100 1.000 18.33000 ? 126 ILE   B C   1 
ATOM   2593 O  O   . ILE   B 1 82  ? 46.69300 49.29200 -35.65800 1.000 17.93000 ? 126 ILE   B O   1 
ATOM   2594 C  CB  . ILE   B 1 82  ? 44.29900 50.91300 -36.59300 1.000 19.40000 ? 126 ILE   B CB  1 
ATOM   2595 C  CG1 . ILE   B 1 82  ? 43.50800 52.13500 -37.06500 1.000 20.59000 ? 126 ILE   B CG1 1 
ATOM   2596 C  CG2 . ILE   B 1 82  ? 43.40200 49.92700 -35.86400 1.000 18.78000 ? 126 ILE   B CG2 1 
ATOM   2597 C  CD1 . ILE   B 1 82  ? 42.32700 51.79100 -37.93000 1.000 21.09000 ? 126 ILE   B CD1 1 
ATOM   2598 N  N   . VAL   B 1 83  ? 46.05700 50.14900 -33.67100 1.000 18.54000 ? 127 VAL   B N   1 
ATOM   2599 C  CA  . VAL   B 1 83  ? 46.77600 49.17600 -32.85300 1.000 18.31000 ? 127 VAL   B CA  1 
ATOM   2600 C  C   . VAL   B 1 83  ? 45.76000 48.30000 -32.13800 1.000 18.29000 ? 127 VAL   B C   1 
ATOM   2601 O  O   . VAL   B 1 83  ? 44.81900 48.81100 -31.51900 1.000 18.58000 ? 127 VAL   B O   1 
ATOM   2602 C  CB  . VAL   B 1 83  ? 47.71600 49.87000 -31.85100 1.000 19.01000 ? 127 VAL   B CB  1 
ATOM   2603 C  CG1 . VAL   B 1 83  ? 48.56700 48.84900 -31.11700 1.000 18.78000 ? 127 VAL   B CG1 1 
ATOM   2604 C  CG2 . VAL   B 1 83  ? 48.59900 50.87700 -32.56400 1.000 19.67000 ? 127 VAL   B CG2 1 
ATOM   2605 N  N   . PHE   B 1 84  ? 45.94600 46.98600 -32.22500 1.000 17.35000 ? 128 PHE   B N   1 
ATOM   2606 C  CA  . PHE   B 1 84  ? 45.01200 46.00300 -31.67800 1.000 17.31000 ? 128 PHE   B CA  1 
ATOM   2607 C  C   . PHE   B 1 84  ? 45.76800 45.08100 -30.72200 1.000 17.17000 ? 128 PHE   B C   1 
ATOM   2608 O  O   . PHE   B 1 84  ? 46.31600 44.05600 -31.13500 1.000 16.83000 ? 128 PHE   B O   1 
ATOM   2609 C  CB  . PHE   B 1 84  ? 44.34800 45.21300 -32.80900 1.000 17.19000 ? 128 PHE   B CB  1 
ATOM   2610 C  CG  . PHE   B 1 84  ? 43.06800 44.53700 -32.41500 1.000 17.52000 ? 128 PHE   B CG  1 
ATOM   2611 C  CD1 . PHE   B 1 84  ? 42.51500 44.74000 -31.16200 1.000 17.84000 ? 128 PHE   B CD1 1 
ATOM   2612 C  CD2 . PHE   B 1 84  ? 42.41600 43.69700 -33.29900 1.000 17.31000 ? 128 PHE   B CD2 1 
ATOM   2613 C  CE1 . PHE   B 1 84  ? 41.34200 44.12400 -30.80000 1.000 18.27000 ? 128 PHE   B CE1 1 
ATOM   2614 C  CE2 . PHE   B 1 84  ? 41.23800 43.07600 -32.94000 1.000 17.86000 ? 128 PHE   B CE2 1 
ATOM   2615 C  CZ  . PHE   B 1 84  ? 40.70100 43.29100 -31.68600 1.000 18.19000 ? 128 PHE   B CZ  1 
ATOM   2616 N  N   . THR   B 1 85  ? 45.79600 45.44300 -29.43900 1.000 17.49000 ? 129 THR   B N   1 
ATOM   2617 C  CA  . THR   B 1 85  ? 46.35200 44.56800 -28.41200 1.000 17.40000 ? 129 THR   B CA  1 
ATOM   2618 C  C   . THR   B 1 85  ? 45.32900 43.48800 -28.09200 1.000 18.15000 ? 129 THR   B C   1 
ATOM   2619 O  O   . THR   B 1 85  ? 44.21500 43.79100 -27.65300 1.000 17.71000 ? 129 THR   B O   1 
ATOM   2620 C  CB  . THR   B 1 85  ? 46.70800 45.35900 -27.15600 1.000 18.00000 ? 129 THR   B CB  1 
ATOM   2621 O  OG1 . THR   B 1 85  ? 45.53400 46.01100 -26.66500 1.000 18.21000 ? 129 THR   B OG1 1 
ATOM   2622 C  CG2 . THR   B 1 85  ? 47.75600 46.40400 -27.46200 1.000 17.89000 ? 129 THR   B CG2 1 
ATOM   2623 N  N   . ILE   B 1 86  ? 45.69000 42.23500 -28.32800 1.000 17.40000 ? 130 ILE   B N   1 
ATOM   2624 C  CA  . ILE   B 1 86  ? 44.73400 41.14500 -28.25100 1.000 17.50000 ? 130 ILE   B CA  1 
ATOM   2625 C  C   . ILE   B 1 86  ? 45.10800 40.21700 -27.10600 1.000 17.90000 ? 130 ILE   B C   1 
ATOM   2626 O  O   . ILE   B 1 86  ? 46.26100 40.13200 -26.68000 1.000 17.23000 ? 130 ILE   B O   1 
ATOM   2627 C  CB  . ILE   B 1 86  ? 44.64400 40.35200 -29.57200 1.000 17.26000 ? 130 ILE   B CB  1 
ATOM   2628 C  CG1 . ILE   B 1 86  ? 45.95100 39.60100 -29.82700 1.000 16.75000 ? 130 ILE   B CG1 1 
ATOM   2629 C  CG2 . ILE   B 1 86  ? 44.30700 41.27500 -30.74000 1.000 17.25000 ? 130 ILE   B CG2 1 
ATOM   2630 C  CD1 . ILE   B 1 86  ? 45.84600 38.55500 -30.90100 1.000 16.14000 ? 130 ILE   B CD1 1 
ATOM   2631 N  N   . ASP   B 1 87  ? 44.09900 39.51500 -26.60600 1.000 17.53000 ? 131 ASP   B N   1 
ATOM   2632 C  CA  . ASP   B 1 87  ? 44.28700 38.36600 -25.73900 1.000 17.58000 ? 131 ASP   B CA  1 
ATOM   2633 C  C   . ASP   B 1 87  ? 44.14300 37.09400 -26.56300 1.000 17.63000 ? 131 ASP   B C   1 
ATOM   2634 O  O   . ASP   B 1 87  ? 43.45800 37.07600 -27.58800 1.000 17.50000 ? 131 ASP   B O   1 
ATOM   2635 C  CB  . ASP   B 1 87  ? 43.27100 38.37000 -24.59400 1.000 17.60000 ? 131 ASP   B CB  1 
ATOM   2636 C  CG  . ASP   B 1 87  ? 43.42400 39.57200 -23.68300 1.000 17.44000 ? 131 ASP   B CG  1 
ATOM   2637 O  OD1 . ASP   B 1 87  ? 44.56700 39.88900 -23.29700 1.000 17.38000 ? 131 ASP   B OD1 1 
ATOM   2638 O  OD2 . ASP   B 1 87  ? 42.40000 40.20800 -23.36100 1.000 17.41000 ? 131 ASP   B OD2 1 
ATOM   2639 N  N   . THR   B 1 88  ? 44.80300 36.03100 -26.11800 1.000 17.85000 ? 132 THR   B N   1 
ATOM   2640 C  CA  . THR   B 1 88  ? 44.71500 34.77200 -26.83800 1.000 17.93000 ? 132 THR   B CA  1 
ATOM   2641 C  C   . THR   B 1 88  ? 43.53900 33.94500 -26.32900 1.000 17.82000 ? 132 THR   B C   1 
ATOM   2642 O  O   . THR   B 1 88  ? 42.87300 34.29500 -25.35300 1.000 17.78000 ? 132 THR   B O   1 
ATOM   2643 C  CB  . THR   B 1 88  ? 46.02300 33.98000 -26.73400 1.000 17.88000 ? 132 THR   B CB  1 
ATOM   2644 O  OG1 . THR   B 1 88  ? 46.40700 33.83800 -25.36100 1.000 17.76000 ? 132 THR   B OG1 1 
ATOM   2645 C  CG2 . THR   B 1 88  ? 47.13300 34.68200 -27.48700 1.000 17.63000 ? 132 THR   B CG2 1 
ATOM   2646 N  N   . ASN   B 1 89  ? 43.27300 32.83900 -27.02300 1.000 17.70000 ? 133 ASN   B N   1 
ATOM   2647 C  CA  . ASN   B 1 89  ? 42.19500 31.94800 -26.60800 1.000 17.69000 ? 133 ASN   B CA  1 
ATOM   2648 C  C   . ASN   B 1 89  ? 42.47300 31.35400 -25.23300 1.000 17.54000 ? 133 ASN   B C   1 
ATOM   2649 O  O   . ASN   B 1 89  ? 41.62500 31.41200 -24.33500 1.000 17.14000 ? 133 ASN   B O   1 
ATOM   2650 C  CB  . ASN   B 1 89  ? 42.00300 30.84000 -27.63900 1.000 17.73000 ? 133 ASN   B CB  1 
ATOM   2651 C  CG  . ASN   B 1 89  ? 41.49800 31.36000 -28.95900 1.000 17.97000 ? 133 ASN   B CG  1 
ATOM   2652 O  OD1 . ASN   B 1 89  ? 40.84100 32.39600 -29.02300 1.000 18.11000 ? 133 ASN   B OD1 1 
ATOM   2653 N  ND2 . ASN   B 1 89  ? 41.79800 30.63800 -30.02300 1.000 17.50000 ? 133 ASN   B ND2 1 
ATOM   2654 N  N   . THR   B 1 90  ? 43.64800 30.75400 -25.05900 1.000 17.72000 ? 134 THR   B N   1 
ATOM   2655 C  CA  . THR   B 1 90  ? 44.08900 30.25300 -23.76800 1.000 17.92000 ? 134 THR   B CA  1 
ATOM   2656 C  C   . THR   B 1 90  ? 45.46500 30.82600 -23.45900 1.000 18.19000 ? 134 THR   B C   1 
ATOM   2657 O  O   . THR   B 1 90  ? 46.15700 31.34500 -24.33800 1.000 18.11000 ? 134 THR   B O   1 
ATOM   2658 C  CB  . THR   B 1 90  ? 44.14200 28.71300 -23.71500 1.000 18.05000 ? 134 THR   B CB  1 
ATOM   2659 O  OG1 . THR   B 1 90  ? 45.41500 28.24800 -24.17800 1.000 18.06000 ? 134 THR   B OG1 1 
ATOM   2660 C  CG2 . THR   B 1 90  ? 43.04700 28.09900 -24.56500 1.000 17.73000 ? 134 THR   B CG2 1 
ATOM   2661 N  N   . ARG   B 1 91  ? 45.85600 30.72700 -22.18700 1.000 18.34000 ? 135 ARG   B N   1 
ATOM   2662 C  CA  . ARG   B 1 91  ? 47.15200 31.24200 -21.76100 1.000 19.05000 ? 135 ARG   B CA  1 
ATOM   2663 C  C   . ARG   B 1 91  ? 48.30700 30.38200 -22.24800 1.000 19.27000 ? 135 ARG   B C   1 
ATOM   2664 O  O   . ARG   B 1 91  ? 49.44200 30.86200 -22.30300 1.000 19.05000 ? 135 ARG   B O   1 
ATOM   2665 C  CB  . ARG   B 1 91  ? 47.19600 31.34900 -20.23300 1.000 19.58000 ? 135 ARG   B CB  1 
ATOM   2666 C  CG  . ARG   B 1 91  ? 46.93700 30.03200 -19.50400 1.000 20.51000 ? 135 ARG   B CG  1 
ATOM   2667 C  CD  . ARG   B 1 91  ? 46.63100 30.24000 -18.01400 1.000 21.60000 ? 135 ARG   B CD  1 
ATOM   2668 N  NE  . ARG   B 1 91  ? 47.83100 30.30100 -17.18500 1.000 23.60000 ? 135 ARG   B NE  1 
ATOM   2669 C  CZ  . ARG   B 1 91  ? 48.29900 29.29100 -16.46100 1.000 24.18000 ? 135 ARG   B CZ  1 
ATOM   2670 N  NH1 . ARG   B 1 91  ? 47.68500 28.12000 -16.42700 1.000 23.15000 ? 135 ARG   B NH1 1 
ATOM   2671 N  NH2 . ARG   B 1 91  ? 49.41000 29.46200 -15.74800 1.000 21.09000 ? 135 ARG   B NH2 1 
ATOM   2672 N  N   . LEU   B 1 92  ? 48.04800 29.12800 -22.59900 1.000 19.36000 ? 136 LEU   B N   1 
ATOM   2673 C  CA  . LEU   B 1 92  ? 49.09500 28.19600 -22.98700 1.000 19.18000 ? 136 LEU   B CA  1 
ATOM   2674 C  C   . LEU   B 1 92  ? 49.30000 28.13000 -24.49800 1.000 18.73000 ? 136 LEU   B C   1 
ATOM   2675 O  O   . LEU   B 1 92  ? 50.08300 27.30200 -24.96800 1.000 18.62000 ? 136 LEU   B O   1 
ATOM   2676 C  CB  . LEU   B 1 92  ? 48.77800 26.80500 -22.43800 1.000 18.93000 ? 136 LEU   B CB  1 
ATOM   2677 C  CG  . LEU   B 1 92  ? 48.40300 26.74100 -20.95400 1.000 19.36000 ? 136 LEU   B CG  1 
ATOM   2678 C  CD1 . LEU   B 1 92  ? 47.98500 25.33700 -20.56100 1.000 19.25000 ? 136 LEU   B CD1 1 
ATOM   2679 C  CD2 . LEU   B 1 92  ? 49.56600 27.20800 -20.10400 1.000 20.21000 ? 136 LEU   B CD2 1 
ATOM   2680 N  N   . ASP   B 1 93  ? 48.62600 28.99400 -25.26000 1.000 18.39000 ? 137 ASP   B N   1 
ATOM   2681 C  CA  . ASP   B 1 93  ? 48.65000 28.90900 -26.71700 1.000 18.02000 ? 137 ASP   B CA  1 
ATOM   2682 C  C   . ASP   B 1 93  ? 50.07600 29.01300 -27.25300 1.000 17.89000 ? 137 ASP   B C   1 
ATOM   2683 O  O   . ASP   B 1 93  ? 50.84100 29.89800 -26.86300 1.000 17.61000 ? 137 ASP   B O   1 
ATOM   2684 C  CB  . ASP   B 1 93  ? 47.77100 30.00600 -27.32000 1.000 17.88000 ? 137 ASP   B CB  1 
ATOM   2685 C  CG  . ASP   B 1 93  ? 46.28900 29.73400 -27.14500 1.000 18.18000 ? 137 ASP   B CG  1 
ATOM   2686 O  OD1 . ASP   B 1 93  ? 45.92100 28.57300 -26.88900 1.000 17.65000 ? 137 ASP   B OD1 1 
ATOM   2687 O  OD2 . ASP   B 1 93  ? 45.48700 30.67900 -27.27500 1.000 17.74000 ? 137 ASP   B OD2 1 
ATOM   2688 N  N   . ALA   B 1 94  ? 50.42600 28.09200 -28.14900 1.000 17.61000 ? 138 ALA   B N   1 
ATOM   2689 C  CA  . ALA   B 1 94  ? 51.75300 28.01400 -28.73200 1.000 17.72000 ? 138 ALA   B CA  1 
ATOM   2690 C  C   . ALA   B 1 94  ? 51.95000 29.12100 -29.76600 1.000 16.75000 ? 138 ALA   B C   1 
ATOM   2691 O  O   . ALA   B 1 94  ? 50.98900 29.77400 -30.17700 1.000 17.23000 ? 138 ALA   B O   1 
ATOM   2692 C  CB  . ALA   B 1 94  ? 51.95600 26.63400 -29.35600 1.000 18.02000 ? 138 ALA   B CB  1 
ATOM   2693 N  N   . PRO   B 1 95  ? 53.19700 29.36200 -30.20300 1.000 17.13000 ? 139 PRO   B N   1 
ATOM   2694 C  CA  . PRO   B 1 95  ? 53.42600 30.41300 -31.21500 1.000 16.62000 ? 139 PRO   B CA  1 
ATOM   2695 C  C   . PRO   B 1 95  ? 52.65400 30.20800 -32.50700 1.000 16.87000 ? 139 PRO   B C   1 
ATOM   2696 O  O   . PRO   B 1 95  ? 52.24000 31.19000 -33.13400 1.000 16.29000 ? 139 PRO   B O   1 
ATOM   2697 C  CB  . PRO   B 1 95  ? 54.93700 30.33600 -31.44900 1.000 16.78000 ? 139 PRO   B CB  1 
ATOM   2698 C  CG  . PRO   B 1 95  ? 55.48000 29.81800 -30.17000 1.000 17.14000 ? 139 PRO   B CG  1 
ATOM   2699 C  CD  . PRO   B 1 95  ? 54.47000 28.83100 -29.67900 1.000 17.19000 ? 139 PRO   B CD  1 
ATOM   2700 N  N   . GLY   B 1 96  ? 52.47300 28.96100 -32.93800 1.000 16.61000 ? 140 GLY   B N   1 
ATOM   2701 C  CA  . GLY   B 1 96  ? 51.66900 28.71500 -34.12000 1.000 16.69000 ? 140 GLY   B CA  1 
ATOM   2702 C  C   . GLY   B 1 96  ? 50.24100 29.18500 -33.94200 1.000 16.74000 ? 140 GLY   B C   1 
ATOM   2703 O  O   . GLY   B 1 96  ? 49.64700 29.76100 -34.85600 1.000 16.90000 ? 140 GLY   B O   1 
ATOM   2704 N  N   . GLN   B 1 97  ? 49.67600 28.96600 -32.75400 1.000 16.70000 ? 141 GLN   B N   1 
ATOM   2705 C  CA  . GLN   B 1 97  ? 48.31000 29.40600 -32.49900 1.000 16.92000 ? 141 GLN   B CA  1 
ATOM   2706 C  C   . GLN   B 1 97  ? 48.23700 30.92200 -32.37800 1.000 16.79000 ? 141 GLN   B C   1 
ATOM   2707 O  O   . GLN   B 1 97  ? 47.30200 31.54900 -32.89400 1.000 16.76000 ? 141 GLN   B O   1 
ATOM   2708 C  CB  . GLN   B 1 97  ? 47.77100 28.72400 -31.24100 1.000 17.09000 ? 141 GLN   B CB  1 
ATOM   2709 C  CG  . GLN   B 1 97  ? 47.83500 27.20600 -31.29600 1.000 17.07000 ? 141 GLN   B CG  1 
ATOM   2710 C  CD  . GLN   B 1 97  ? 47.49400 26.55500 -29.97000 1.000 16.79000 ? 141 GLN   B CD  1 
ATOM   2711 O  OE1 . GLN   B 1 97  ? 48.28600 26.58200 -29.03000 1.000 17.20000 ? 141 GLN   B OE1 1 
ATOM   2712 N  NE2 . GLN   B 1 97  ? 46.30800 25.96800 -29.88800 1.000 16.12000 ? 141 GLN   B NE2 1 
ATOM   2713 N  N   . ARG   B 1 98  ? 49.21600 31.53300 -31.70900 1.000 16.51000 ? 142 ARG   B N   1 
ATOM   2714 C  CA  . ARG   B 1 98  ? 49.27100 32.98700 -31.65400 1.000 16.67000 ? 142 ARG   B CA  1 
ATOM   2715 C  C   . ARG   B 1 98  ? 49.41200 33.59300 -33.04500 1.000 16.33000 ? 142 ARG   B C   1 
ATOM   2716 O  O   . ARG   B 1 98  ? 48.88900 34.68300 -33.30200 1.000 16.47000 ? 142 ARG   B O   1 
ATOM   2717 C  CB  . ARG   B 1 98  ? 50.41800 33.42800 -30.74800 1.000 16.38000 ? 142 ARG   B CB  1 
ATOM   2718 C  CG  . ARG   B 1 98  ? 50.27500 32.90200 -29.34100 1.000 16.65000 ? 142 ARG   B CG  1 
ATOM   2719 C  CD  . ARG   B 1 98  ? 51.51900 33.11200 -28.50100 1.000 16.74000 ? 142 ARG   B CD  1 
ATOM   2720 N  NE  . ARG   B 1 98  ? 51.32400 32.47200 -27.21000 1.000 17.12000 ? 142 ARG   B NE  1 
ATOM   2721 C  CZ  . ARG   B 1 98  ? 50.72600 33.04700 -26.17800 1.000 17.42000 ? 142 ARG   B CZ  1 
ATOM   2722 N  NH1 . ARG   B 1 98  ? 50.39200 34.32700 -26.19900 1.000 17.17000 ? 142 ARG   B NH1 1 
ATOM   2723 N  NH2 . ARG   B 1 98  ? 50.43600 32.31400 -25.10800 1.000 17.81000 ? 142 ARG   B NH2 1 
ATOM   2724 N  N   . GLY   B 1 99  ? 50.10000 32.90000 -33.95600 1.000 16.40000 ? 143 GLY   B N   1 
ATOM   2725 C  CA  . GLY   B 1 99  ? 50.14900 33.36200 -35.33500 1.000 16.48000 ? 143 GLY   B CA  1 
ATOM   2726 C  C   . GLY   B 1 99  ? 48.77500 33.41500 -35.97500 1.000 17.08000 ? 143 GLY   B C   1 
ATOM   2727 O  O   . GLY   B 1 99  ? 48.39600 34.41800 -36.58500 1.000 16.73000 ? 143 GLY   B O   1 
ATOM   2728 N  N   . ARG   B 1 100 ? 48.00300 32.33600 -35.82800 1.000 17.14000 ? 144 ARG   B N   1 
ATOM   2729 C  CA  . ARG   B 1 100 ? 46.65300 32.30200 -36.38000 1.000 17.60000 ? 144 ARG   B CA  1 
ATOM   2730 C  C   . ARG   B 1 100 ? 45.76200 33.35300 -35.73400 1.000 17.22000 ? 144 ARG   B C   1 
ATOM   2731 O  O   . ARG   B 1 100 ? 44.95700 33.99700 -36.41400 1.000 17.45000 ? 144 ARG   B O   1 
ATOM   2732 C  CB  . ARG   B 1 100 ? 46.04500 30.91100 -36.19500 1.000 18.86000 ? 144 ARG   B CB  1 
ATOM   2733 C  CG  . ARG   B 1 100 ? 46.73400 29.80900 -36.98300 1.000 19.50000 ? 144 ARG   B CG  1 
ATOM   2734 C  CD  . ARG   B 1 100 ? 46.48500 29.97500 -38.47100 1.000 22.97000 ? 144 ARG   B CD  1 
ATOM   2735 N  NE  . ARG   B 1 100 ? 47.07200 28.89700 -39.25900 1.000 24.26000 ? 144 ARG   B NE  1 
ATOM   2736 C  CZ  . ARG   B 1 100 ? 47.11700 28.88500 -40.58400 1.000 25.04000 ? 144 ARG   B CZ  1 
ATOM   2737 N  NH1 . ARG   B 1 100 ? 46.63100 29.88600 -41.30000 1.000 23.51000 ? 144 ARG   B NH1 1 
ATOM   2738 N  NH2 . ARG   B 1 100 ? 47.66800 27.84600 -41.20600 1.000 26.44000 ? 144 ARG   B NH2 1 
ATOM   2739 N  N   . GLN   B 1 101 ? 45.88800 33.53700 -34.41800 1.000 17.04000 ? 145 GLN   B N   1 
ATOM   2740 C  CA  . GLN   B 1 101 ? 45.02400 34.48300 -33.72200 1.000 17.01000 ? 145 GLN   B CA  1 
ATOM   2741 C  C   . GLN   B 1 101 ? 45.37900 35.92400 -34.05900 1.000 17.24000 ? 145 GLN   B C   1 
ATOM   2742 O  O   . GLN   B 1 101 ? 44.51200 36.80000 -34.00000 1.000 17.02000 ? 145 GLN   B O   1 
ATOM   2743 C  CB  . GLN   B 1 101 ? 45.09200 34.23600 -32.21300 1.000 16.83000 ? 145 GLN   B CB  1 
ATOM   2744 C  CG  . GLN   B 1 101 ? 44.70900 32.81600 -31.82500 1.000 17.07000 ? 145 GLN   B CG  1 
ATOM   2745 C  CD  . GLN   B 1 101 ? 44.73100 32.58200 -30.33400 1.000 17.34000 ? 145 GLN   B CD  1 
ATOM   2746 O  OE1 . GLN   B 1 101 ? 44.36300 33.45700 -29.55900 1.000 17.43000 ? 145 GLN   B OE1 1 
ATOM   2747 N  NE2 . GLN   B 1 101 ? 45.16200 31.39600 -29.92500 1.000 17.36000 ? 145 GLN   B NE2 1 
ATOM   2748 N  N   . LEU   B 1 102 ? 46.63700 36.19300 -34.41500 1.000 16.65000 ? 146 LEU   B N   1 
ATOM   2749 C  CA  . LEU   B 1 102 ? 46.97700 37.51300 -34.93300 1.000 16.90000 ? 146 LEU   B CA  1 
ATOM   2750 C  C   . LEU   B 1 102 ? 46.24800 37.78400 -36.24300 1.000 17.18000 ? 146 LEU   B C   1 
ATOM   2751 O  O   . LEU   B 1 102 ? 45.70700 38.87600 -36.44700 1.000 17.08000 ? 146 LEU   B O   1 
ATOM   2752 C  CB  . LEU   B 1 102 ? 48.49000 37.63200 -35.11800 1.000 16.76000 ? 146 LEU   B CB  1 
ATOM   2753 C  CG  . LEU   B 1 102 ? 49.29600 37.99300 -33.86800 1.000 16.65000 ? 146 LEU   B CG  1 
ATOM   2754 C  CD1 . LEU   B 1 102 ? 50.77700 37.74000 -34.05800 1.000 16.46000 ? 146 LEU   B CD1 1 
ATOM   2755 C  CD2 . LEU   B 1 102 ? 49.05500 39.44600 -33.52300 1.000 16.28000 ? 146 LEU   B CD2 1 
ATOM   2756 N  N   . LEU   B 1 103 ? 46.20200 36.79000 -37.13300 1.000 17.02000 ? 147 LEU   B N   1 
ATOM   2757 C  CA  . LEU   B 1 103 ? 45.51600 36.96300 -38.41000 1.000 17.33000 ? 147 LEU   B CA  1 
ATOM   2758 C  C   . LEU   B 1 103 ? 44.01300 37.12100 -38.21700 1.000 17.53000 ? 147 LEU   B C   1 
ATOM   2759 O  O   . LEU   B 1 103 ? 43.37500 37.92700 -38.90400 1.000 17.89000 ? 147 LEU   B O   1 
ATOM   2760 C  CB  . LEU   B 1 103 ? 45.82100 35.78100 -39.32800 1.000 17.17000 ? 147 LEU   B CB  1 
ATOM   2761 C  CG  . LEU   B 1 103 ? 47.28600 35.64900 -39.74700 1.000 16.92000 ? 147 LEU   B CG  1 
ATOM   2762 C  CD1 . LEU   B 1 103 ? 47.51200 34.37600 -40.54000 1.000 17.29000 ? 147 LEU   B CD1 1 
ATOM   2763 C  CD2 . LEU   B 1 103 ? 47.71300 36.86300 -40.54900 1.000 16.81000 ? 147 LEU   B CD2 1 
ATOM   2764 N  N   . ALA   B 1 104 ? 43.43000 36.36300 -37.28600 1.000 17.57000 ? 148 ALA   B N   1 
ATOM   2765 C  CA  . ALA   B 1 104 ? 41.99800 36.47900 -37.03900 1.000 17.93000 ? 148 ALA   B CA  1 
ATOM   2766 C  C   . ALA   B 1 104 ? 41.64200 37.82700 -36.42700 1.000 18.44000 ? 148 ALA   B C   1 
ATOM   2767 O  O   . ALA   B 1 104 ? 40.51000 38.29800 -36.58000 1.000 18.60000 ? 148 ALA   B O   1 
ATOM   2768 C  CB  . ALA   B 1 104 ? 41.52900 35.34000 -36.13600 1.000 17.91000 ? 148 ALA   B CB  1 
ATOM   2769 N  N   . ALA   B 1 105 ? 42.58800 38.46000 -35.73200 1.000 17.80000 ? 149 ALA   B N   1 
ATOM   2770 C  CA  . ALA   B 1 105 ? 42.33100 39.79400 -35.20200 1.000 17.92000 ? 149 ALA   B CA  1 
ATOM   2771 C  C   . ALA   B 1 105 ? 42.34900 40.83400 -36.31500 1.000 18.28000 ? 149 ALA   B C   1 
ATOM   2772 O  O   . ALA   B 1 105 ? 41.51400 41.74600 -36.33500 1.000 18.70000 ? 149 ALA   B O   1 
ATOM   2773 C  CB  . ALA   B 1 105 ? 43.35400 40.13800 -34.12000 1.000 17.43000 ? 149 ALA   B CB  1 
ATOM   2774 N  N   . LEU   B 1 106 ? 43.29600 40.71100 -37.24900 1.000 18.01000 ? 150 LEU   B N   1 
ATOM   2775 C  CA  . LEU   B 1 106 ? 43.30500 41.57300 -38.42800 1.000 18.33000 ? 150 LEU   B CA  1 
ATOM   2776 C  C   . LEU   B 1 106 ? 42.04600 41.37300 -39.26300 1.000 19.14000 ? 150 LEU   B C   1 
ATOM   2777 O  O   . LEU   B 1 106 ? 41.41900 42.34500 -39.70100 1.000 19.54000 ? 150 LEU   B O   1 
ATOM   2778 C  CB  . LEU   B 1 106 ? 44.55600 41.29200 -39.26300 1.000 17.85000 ? 150 LEU   B CB  1 
ATOM   2779 C  CG  . LEU   B 1 106 ? 45.90100 41.52600 -38.57400 1.000 17.41000 ? 150 LEU   B CG  1 
ATOM   2780 C  CD1 . LEU   B 1 106 ? 47.03400 40.87200 -39.34300 1.000 17.24000 ? 150 LEU   B CD1 1 
ATOM   2781 C  CD2 . LEU   B 1 106 ? 46.15500 43.01500 -38.39300 1.000 17.14000 ? 150 LEU   B CD2 1 
ATOM   2782 N  N   . ASP   B 1 107 ? 41.65400 40.11700 -39.48500 1.000 19.11000 ? 151 ASP   B N   1 
ATOM   2783 C  CA  . ASP   B 1 107 ? 40.43900 39.84700 -40.24500 1.000 20.01000 ? 151 ASP   B CA  1 
ATOM   2784 C  C   . ASP   B 1 107 ? 39.21000 40.41800 -39.55800 1.000 20.89000 ? 151 ASP   B C   1 
ATOM   2785 O  O   . ASP   B 1 107 ? 38.26300 40.83300 -40.23400 1.000 21.87000 ? 151 ASP   B O   1 
ATOM   2786 C  CB  . ASP   B 1 107 ? 40.28000 38.34500 -40.46400 1.000 20.03000 ? 151 ASP   B CB  1 
ATOM   2787 C  CG  . ASP   B 1 107 ? 41.28900 37.79600 -41.45000 1.000 19.09000 ? 151 ASP   B CG  1 
ATOM   2788 O  OD1 . ASP   B 1 107 ? 42.01100 38.60500 -42.06700 1.000 18.51000 ? 151 ASP   B OD1 1 
ATOM   2789 O  OD2 . ASP   B 1 107 ? 41.36100 36.56000 -41.60600 1.000 18.02000 ? 151 ASP   B OD2 1 
ATOM   2790 N  N   . TYR   B 1 108 ? 39.20500 40.45600 -38.22200 1.000 20.46000 ? 152 TYR   B N   1 
ATOM   2791 C  CA  . TYR   B 1 108 ? 38.11200 41.10900 -37.50700 1.000 21.15000 ? 152 TYR   B CA  1 
ATOM   2792 C  C   . TYR   B 1 108 ? 38.08600 42.60400 -37.79600 1.000 22.02000 ? 152 TYR   B C   1 
ATOM   2793 O  O   . TYR   B 1 108 ? 37.02300 43.18100 -38.04300 1.000 21.98000 ? 152 TYR   B O   1 
ATOM   2794 C  CB  . TYR   B 1 108 ? 38.22900 40.86400 -35.99800 1.000 20.68000 ? 152 TYR   B CB  1 
ATOM   2795 C  CG  . TYR   B 1 108 ? 37.19500 41.63000 -35.19600 1.000 21.36000 ? 152 TYR   B CG  1 
ATOM   2796 C  CD1 . TYR   B 1 108 ? 37.45500 42.91500 -34.73600 1.000 20.99000 ? 152 TYR   B CD1 1 
ATOM   2797 C  CD2 . TYR   B 1 108 ? 35.95200 41.07800 -34.91900 1.000 21.97000 ? 152 TYR   B CD2 1 
ATOM   2798 C  CE1 . TYR   B 1 108 ? 36.51200 43.62800 -34.02300 1.000 21.13000 ? 152 TYR   B CE1 1 
ATOM   2799 C  CE2 . TYR   B 1 108 ? 35.00000 41.78400 -34.19800 1.000 21.74000 ? 152 TYR   B CE2 1 
ATOM   2800 C  CZ  . TYR   B 1 108 ? 35.28900 43.05800 -33.75300 1.000 21.19000 ? 152 TYR   B CZ  1 
ATOM   2801 O  OH  . TYR   B 1 108 ? 34.35800 43.77400 -33.03800 1.000 20.34000 ? 152 TYR   B OH  1 
ATOM   2802 N  N   . LEU   B 1 109 ? 39.24900 43.25500 -37.73000 1.000 20.70000 ? 153 LEU   B N   1 
ATOM   2803 C  CA  . LEU   B 1 109 ? 39.32200 44.67900 -38.04000 1.000 21.03000 ? 153 LEU   B CA  1 
ATOM   2804 C  C   . LEU   B 1 109 ? 38.76800 44.96800 -39.42800 1.000 21.52000 ? 153 LEU   B C   1 
ATOM   2805 O  O   . LEU   B 1 109 ? 38.07700 45.97300 -39.63400 1.000 21.88000 ? 153 LEU   B O   1 
ATOM   2806 C  CB  . LEU   B 1 109 ? 40.76800 45.16300 -37.93600 1.000 20.23000 ? 153 LEU   B CB  1 
ATOM   2807 C  CG  . LEU   B 1 109 ? 41.35900 45.34800 -36.54000 1.000 19.23000 ? 153 LEU   B CG  1 
ATOM   2808 C  CD1 . LEU   B 1 109 ? 42.85400 45.57400 -36.62000 1.000 18.44000 ? 153 LEU   B CD1 1 
ATOM   2809 C  CD2 . LEU   B 1 109 ? 40.69000 46.52000 -35.86500 1.000 18.60000 ? 153 LEU   B CD2 1 
ATOM   2810 N  N   . VAL   B 1 110 ? 39.03700 44.07900 -40.38300 1.000 21.37000 ? 154 VAL   B N   1 
ATOM   2811 C  CA  . VAL   B 1 110 ? 38.67800 44.31800 -41.77700 1.000 21.94000 ? 154 VAL   B CA  1 
ATOM   2812 C  C   . VAL   B 1 110 ? 37.20400 44.02600 -42.02100 1.000 22.86000 ? 154 VAL   B C   1 
ATOM   2813 O  O   . VAL   B 1 110 ? 36.49400 44.82300 -42.64400 1.000 23.39000 ? 154 VAL   B O   1 
ATOM   2814 C  CB  . VAL   B 1 110 ? 39.58100 43.47400 -42.69600 1.000 21.61000 ? 154 VAL   B CB  1 
ATOM   2815 C  CG1 . VAL   B 1 110 ? 39.06900 43.50100 -44.13400 1.000 20.69000 ? 154 VAL   B CG1 1 
ATOM   2816 C  CG2 . VAL   B 1 110 ? 41.01500 43.96400 -42.62100 1.000 21.27000 ? 154 VAL   B CG2 1 
ATOM   2817 N  N   . GLU   B 1 111 ? 36.71900 42.88600 -41.53300 1.000 23.25000 ? 155 GLU   B N   1 
ATOM   2818 C  CA  . GLU   B 1 111 ? 35.39400 42.40000 -41.89100 1.000 24.39000 ? 155 GLU   B CA  1 
ATOM   2819 C  C   . GLU   B 1 111 ? 34.30400 42.77500 -40.90200 1.000 24.48000 ? 155 GLU   B C   1 
ATOM   2820 O  O   . GLU   B 1 111 ? 33.15400 42.94700 -41.31600 1.000 23.64000 ? 155 GLU   B O   1 
ATOM   2821 C  CB  . GLU   B 1 111 ? 35.40900 40.87600 -42.02900 1.000 24.81000 ? 155 GLU   B CB  1 
ATOM   2822 C  CG  . GLU   B 1 111 ? 36.51600 40.34000 -42.91400 1.000 24.35000 ? 155 GLU   B CG  1 
ATOM   2823 C  CD  . GLU   B 1 111 ? 36.70400 38.84500 -42.76100 1.000 24.93000 ? 155 GLU   B CD  1 
ATOM   2824 O  OE1 . GLU   B 1 111 ? 35.90600 38.21800 -42.03400 1.000 31.91000 ? 155 GLU   B OE1 1 
ATOM   2825 O  OE2 . GLU   B 1 111 ? 37.64900 38.29500 -43.36200 1.000 25.98000 ? 155 GLU   B OE2 1 
ATOM   2826 N  N   . ARG   B 1 112 ? 34.61700 42.90400 -39.61100 1.000 24.23000 ? 156 ARG   B N   1 
ATOM   2827 C  CA  . ARG   B 1 112 ? 33.57700 42.88800 -38.59000 1.000 24.41000 ? 156 ARG   B CA  1 
ATOM   2828 C  C   . ARG   B 1 112 ? 33.74600 43.95800 -37.51900 1.000 24.01000 ? 156 ARG   B C   1 
ATOM   2829 O  O   . ARG   B 1 112 ? 32.96200 43.98100 -36.56200 1.000 23.66000 ? 156 ARG   B O   1 
ATOM   2830 C  CB  . ARG   B 1 112 ? 33.51800 41.50300 -37.93200 1.000 23.91000 ? 156 ARG   B CB  1 
ATOM   2831 C  CG  . ARG   B 1 112 ? 32.90400 40.43100 -38.81800 1.000 24.85000 ? 156 ARG   B CG  1 
ATOM   2832 C  CD  . ARG   B 1 112 ? 33.20100 39.03000 -38.31900 1.000 23.56000 ? 156 ARG   B CD  1 
ATOM   2833 N  NE  . ARG   B 1 112 ? 34.24500 38.37300 -39.09800 1.000 24.26000 ? 156 ARG   B NE  1 
ATOM   2834 C  CZ  . ARG   B 1 112 ? 35.42900 38.01700 -38.62000 1.000 24.80000 ? 156 ARG   B CZ  1 
ATOM   2835 N  NH1 . ARG   B 1 112 ? 35.75600 38.22700 -37.35600 1.000 27.23000 ? 156 ARG   B NH1 1 
ATOM   2836 N  NH2 . ARG   B 1 112 ? 36.30300 37.42300 -39.42800 1.000 24.56000 ? 156 ARG   B NH2 1 
ATOM   2837 N  N   . SER   B 1 113 ? 34.72700 44.84400 -37.65200 1.000 23.96000 ? 157 SER   B N   1 
ATOM   2838 C  CA  . SER   B 1 113 ? 34.94500 45.86700 -36.64400 1.000 24.73000 ? 157 SER   B CA  1 
ATOM   2839 C  C   . SER   B 1 113 ? 33.81600 46.89700 -36.65200 1.000 25.70000 ? 157 SER   B C   1 
ATOM   2840 O  O   . SER   B 1 113 ? 33.01600 46.97900 -37.58800 1.000 25.72000 ? 157 SER   B O   1 
ATOM   2841 C  CB  . SER   B 1 113 ? 36.28500 46.56600 -36.87100 1.000 23.89000 ? 157 SER   B CB  1 
ATOM   2842 O  OG  . SER   B 1 113 ? 36.30600 47.21900 -38.12400 1.000 23.88000 ? 157 SER   B OG  1 
ATOM   2843 N  N   . ASP   B 1 114 ? 33.74800 47.67400 -35.57200 1.000 26.42000 ? 158 ASP   B N   1 
ATOM   2844 C  CA  . ASP   B 1 114 ? 32.84300 48.81400 -35.52500 1.000 27.17000 ? 158 ASP   B CA  1 
ATOM   2845 C  C   . ASP   B 1 114 ? 33.17400 49.77400 -36.65900 1.000 28.63000 ? 158 ASP   B C   1 
ATOM   2846 O  O   . ASP   B 1 114 ? 34.34300 49.97400 -36.99300 1.000 27.96000 ? 158 ASP   B O   1 
ATOM   2847 C  CB  . ASP   B 1 114 ? 32.96500 49.52900 -34.17700 1.000 28.84000 ? 158 ASP   B CB  1 
ATOM   2848 C  CG  . ASP   B 1 114 ? 31.84100 50.50700 -33.93200 1.000 29.74000 ? 158 ASP   B CG  1 
ATOM   2849 O  OD1 . ASP   B 1 114 ? 30.71300 50.05000 -33.66800 1.000 29.31000 ? 158 ASP   B OD1 1 
ATOM   2850 O  OD2 . ASP   B 1 114 ? 32.08300 51.73000 -34.00100 1.000 29.50000 ? 158 ASP   B OD2 1 
ATOM   2851 N  N   . ARG   B 1 115 ? 32.13900 50.37300 -37.25500 1.000 29.68000 ? 159 ARG   B N   1 
ATOM   2852 C  CA  . ARG   B 1 115 ? 32.36700 51.24000 -38.40600 1.000 30.35000 ? 159 ARG   B CA  1 
ATOM   2853 C  C   . ARG   B 1 115 ? 33.23600 52.44800 -38.07900 1.000 30.32000 ? 159 ARG   B C   1 
ATOM   2854 O  O   . ARG   B 1 115 ? 33.87300 52.99100 -38.98700 1.000 30.19000 ? 159 ARG   B O   1 
ATOM   2855 C  CB  . ARG   B 1 115 ? 31.03700 51.70900 -38.99300 1.000 32.51000 ? 159 ARG   B CB  1 
ATOM   2856 C  CG  . ARG   B 1 115 ? 30.06500 52.24300 -37.97500 1.000 32.97000 ? 159 ARG   B CG  1 
ATOM   2857 C  CD  . ARG   B 1 115 ? 29.29300 53.41000 -38.54500 1.000 35.29000 ? 159 ARG   B CD  1 
ATOM   2858 N  NE  . ARG   B 1 115 ? 30.11700 54.61000 -38.61100 1.000 36.49000 ? 159 ARG   B NE  1 
ATOM   2859 C  CZ  . ARG   B 1 115 ? 30.34600 55.41300 -37.58100 1.000 37.19000 ? 159 ARG   B CZ  1 
ATOM   2860 N  NH1 . ARG   B 1 115 ? 29.83000 55.17100 -36.38800 1.000 39.31000 ? 159 ARG   B NH1 1 
ATOM   2861 N  NH2 . ARG   B 1 115 ? 31.11500 56.48500 -37.75200 1.000 39.90000 ? 159 ARG   B NH2 1 
ATOM   2862 N  N   . LYS   B 1 116 ? 33.27700 52.88900 -36.81800 1.000 30.52000 ? 160 LYS   B N   1 
ATOM   2863 C  CA  . LYS   B 1 116 ? 34.23200 53.93100 -36.44700 1.000 30.55000 ? 160 LYS   B CA  1 
ATOM   2864 C  C   . LYS   B 1 116 ? 35.66000 53.48300 -36.71400 1.000 28.35000 ? 160 LYS   B C   1 
ATOM   2865 O  O   . LYS   B 1 116 ? 36.52300 54.30700 -37.03200 1.000 27.36000 ? 160 LYS   B O   1 
ATOM   2866 C  CB  . LYS   B 1 116 ? 34.07000 54.31500 -34.97400 1.000 30.10000 ? 160 LYS   B CB  1 
ATOM   2867 C  CG  . LYS   B 1 116 ? 32.78300 55.05800 -34.66700 1.000 30.42000 ? 160 LYS   B CG  1 
ATOM   2868 C  CD  . LYS   B 1 116 ? 32.85500 55.77800 -33.33100 1.000 30.87000 ? 160 LYS   B CD  1 
ATOM   2869 C  CE  . LYS   B 1 116 ? 33.20400 54.82200 -32.20700 1.000 30.16000 ? 160 LYS   B CE  1 
ATOM   2870 N  NZ  . LYS   B 1 116 ? 32.19100 53.74300 -32.05300 1.000 30.28000 ? 160 LYS   B NZ  1 
ATOM   2871 N  N   . VAL   B 1 117 ? 35.92400 52.18400 -36.58800 1.000 28.10000 ? 161 VAL   B N   1 
ATOM   2872 C  CA  . VAL   B 1 117 ? 37.23400 51.64400 -36.92400 1.000 26.62000 ? 161 VAL   B CA  1 
ATOM   2873 C  C   . VAL   B 1 117 ? 37.32400 51.34200 -38.41500 1.000 26.39000 ? 161 VAL   B C   1 
ATOM   2874 O  O   . VAL   B 1 117 ? 38.35700 51.58500 -39.04800 1.000 25.18000 ? 161 VAL   B O   1 
ATOM   2875 C  CB  . VAL   B 1 117 ? 37.51500 50.39200 -36.07400 1.000 25.73000 ? 161 VAL   B CB  1 
ATOM   2876 C  CG1 . VAL   B 1 117 ? 38.77600 49.69700 -36.54800 1.000 25.63000 ? 161 VAL   B CG1 1 
ATOM   2877 C  CG2 . VAL   B 1 117 ? 37.61400 50.76000 -34.59400 1.000 24.52000 ? 161 VAL   B CG2 1 
ATOM   2878 N  N   . ARG   B 1 118 ? 36.24000 50.82200 -38.99600 1.000 26.70000 ? 162 ARG   B N   1 
ATOM   2879 C  CA  . ARG   B 1 118 ? 36.26200 50.40900 -40.39600 1.000 26.42000 ? 162 ARG   B CA  1 
ATOM   2880 C  C   . ARG   B 1 118 ? 36.47700 51.59700 -41.32900 1.000 26.73000 ? 162 ARG   B C   1 
ATOM   2881 O  O   . ARG   B 1 118 ? 37.21900 51.49600 -42.31200 1.000 26.44000 ? 162 ARG   B O   1 
ATOM   2882 C  CB  . ARG   B 1 118 ? 34.95900 49.69100 -40.74200 1.000 26.37000 ? 162 ARG   B CB  1 
ATOM   2883 C  CG  . ARG   B 1 118 ? 35.10200 48.60600 -41.78600 1.000 25.58000 ? 162 ARG   B CG  1 
ATOM   2884 C  CD  . ARG   B 1 118 ? 35.18300 47.24500 -41.13100 1.000 25.11000 ? 162 ARG   B CD  1 
ATOM   2885 N  NE  . ARG   B 1 118 ? 33.91400 46.84800 -40.53500 1.000 25.58000 ? 162 ARG   B NE  1 
ATOM   2886 C  CZ  . ARG   B 1 118 ? 32.98500 46.13800 -41.16300 1.000 28.00000 ? 162 ARG   B CZ  1 
ATOM   2887 N  NH1 . ARG   B 1 118 ? 33.14400 45.74900 -42.41700 1.000 28.10000 ? 162 ARG   B NH1 1 
ATOM   2888 N  NH2 . ARG   B 1 118 ? 31.87000 45.80800 -40.51700 1.000 25.35000 ? 162 ARG   B NH2 1 
ATOM   2889 N  N   . GLU   B 1 119 ? 35.83400 52.73000 -41.03700 1.000 27.33000 ? 163 GLU   B N   1 
ATOM   2890 C  CA  . GLU   B 1 119 ? 35.94800 53.92000 -41.87400 1.000 28.64000 ? 163 GLU   B CA  1 
ATOM   2891 C  C   . GLU   B 1 119 ? 37.32100 54.56900 -41.80000 1.000 26.57000 ? 163 GLU   B C   1 
ATOM   2892 O  O   . GLU   B 1 119 ? 37.59800 55.48500 -42.58200 1.000 26.28000 ? 163 GLU   B O   1 
ATOM   2893 C  CB  . GLU   B 1 119 ? 34.88300 54.94500 -41.48200 1.000 29.84000 ? 163 GLU   B CB  1 
ATOM   2894 C  CG  . GLU   B 1 119 ? 33.45700 54.49800 -41.75100 1.000 31.47000 ? 163 GLU   B CG  1 
ATOM   2895 C  CD  . GLU   B 1 119 ? 32.43700 55.52300 -41.30300 1.000 35.78000 ? 163 GLU   B CD  1 
ATOM   2896 O  OE1 . GLU   B 1 119 ? 32.79800 56.41700 -40.50900 1.000 35.67000 ? 163 GLU   B OE1 1 
ATOM   2897 O  OE2 . GLU   B 1 119 ? 31.27300 55.43700 -41.75100 1.000 42.24000 ? 163 GLU   B OE2 1 
ATOM   2898 N  N   . ARG   B 1 120 ? 38.17600 54.13500 -40.88000 1.000 25.56000 ? 164 ARG   B N   1 
ATOM   2899 C  CA  . ARG   B 1 120 ? 39.52400 54.66100 -40.74800 1.000 24.46000 ? 164 ARG   B CA  1 
ATOM   2900 C  C   . ARG   B 1 120 ? 40.57900 53.67500 -41.22200 1.000 23.87000 ? 164 ARG   B C   1 
ATOM   2901 O  O   . ARG   B 1 120 ? 41.76200 54.02400 -41.26700 1.000 22.86000 ? 164 ARG   B O   1 
ATOM   2902 C  CB  . ARG   B 1 120 ? 39.79600 55.04800 -39.28700 1.000 24.02000 ? 164 ARG   B CB  1 
ATOM   2903 C  CG  . ARG   B 1 120 ? 38.95600 56.21400 -38.77800 1.000 23.75000 ? 164 ARG   B CG  1 
ATOM   2904 C  CD  . ARG   B 1 120 ? 39.07400 56.36600 -37.26300 1.000 24.58000 ? 164 ARG   B CD  1 
ATOM   2905 N  NE  . ARG   B 1 120 ? 38.66800 57.69000 -36.80500 1.000 25.51000 ? 164 ARG   B NE  1 
ATOM   2906 C  CZ  . ARG   B 1 120 ? 37.41400 58.06000 -36.58400 1.000 26.16000 ? 164 ARG   B CZ  1 
ATOM   2907 N  NH1 . ARG   B 1 120 ? 36.40200 57.22700 -36.76500 1.000 25.86000 ? 164 ARG   B NH1 1 
ATOM   2908 N  NH2 . ARG   B 1 120 ? 37.16700 59.30300 -36.17900 1.000 25.88000 ? 164 ARG   B NH2 1 
ATOM   2909 N  N   . LEU   B 1 121 ? 40.18200 52.45900 -41.58000 1.000 23.79000 ? 165 LEU   B N   1 
ATOM   2910 C  CA  . LEU   B 1 121 ? 41.10800 51.38000 -41.87600 1.000 22.77000 ? 165 LEU   B CA  1 
ATOM   2911 C  C   . LEU   B 1 121 ? 41.38300 51.28600 -43.37000 1.000 22.00000 ? 165 LEU   B C   1 
ATOM   2912 O  O   . LEU   B 1 121 ? 40.46900 51.39300 -44.19400 1.000 21.98000 ? 165 LEU   B O   1 
ATOM   2913 C  CB  . LEU   B 1 121 ? 40.55700 50.04400 -41.37800 1.000 22.85000 ? 165 LEU   B CB  1 
ATOM   2914 C  CG  . LEU   B 1 121 ? 41.36800 48.80600 -41.76100 1.000 21.90000 ? 165 LEU   B CG  1 
ATOM   2915 C  CD1 . LEU   B 1 121 ? 42.70300 48.80400 -41.04700 1.000 21.22000 ? 165 LEU   B CD1 1 
ATOM   2916 C  CD2 . LEU   B 1 121 ? 40.59400 47.53500 -41.46600 1.000 21.26000 ? 165 LEU   B CD2 1 
ATOM   2917 N  N   . ASP   B 1 122 ? 42.65600 51.09700 -43.70700 1.000 21.49000 ? 166 ASP   B N   1 
ATOM   2918 C  CA  . ASP   B 1 122 ? 43.07600 50.67000 -45.03200 1.000 21.02000 ? 166 ASP   B CA  1 
ATOM   2919 C  C   . ASP   B 1 122 ? 43.28600 49.16800 -44.96300 1.000 20.70000 ? 166 ASP   B C   1 
ATOM   2920 O  O   . ASP   B 1 122 ? 44.33900 48.71800 -44.49100 1.000 20.11000 ? 166 ASP   B O   1 
ATOM   2921 C  CB  . ASP   B 1 122 ? 44.36600 51.37900 -45.45200 1.000 21.01000 ? 166 ASP   B CB  1 
ATOM   2922 C  CG  . ASP   B 1 122 ? 44.72600 51.13300 -46.90200 1.000 20.69000 ? 166 ASP   B CG  1 
ATOM   2923 O  OD1 . ASP   B 1 122 ? 44.39200 50.05800 -47.44000 1.000 20.39000 ? 166 ASP   B OD1 1 
ATOM   2924 O  OD2 . ASP   B 1 122 ? 45.35000 52.02600 -47.50500 1.000 20.90000 ? 166 ASP   B OD2 1 
ATOM   2925 N  N   . PRO   B 1 123 ? 42.33200 48.34900 -45.41200 1.000 20.64000 ? 167 PRO   B N   1 
ATOM   2926 C  CA  . PRO   B 1 123 ? 42.45600 46.89700 -45.21100 1.000 20.55000 ? 167 PRO   B CA  1 
ATOM   2927 C  C   . PRO   B 1 123 ? 43.58700 46.25100 -45.99400 1.000 20.27000 ? 167 PRO   B C   1 
ATOM   2928 O  O   . PRO   B 1 123 ? 43.82900 45.05300 -45.80400 1.000 20.04000 ? 167 PRO   B O   1 
ATOM   2929 C  CB  . PRO   B 1 123 ? 41.09100 46.36100 -45.66400 1.000 20.30000 ? 167 PRO   B CB  1 
ATOM   2930 C  CG  . PRO   B 1 123 ? 40.56500 47.40200 -46.59200 1.000 20.20000 ? 167 PRO   B CG  1 
ATOM   2931 C  CD  . PRO   B 1 123 ? 41.07300 48.71500 -46.08000 1.000 20.67000 ? 167 PRO   B CD  1 
ATOM   2932 N  N   . ASN   B 1 124 ? 44.28900 46.98900 -46.84800 1.000 20.07000 ? 168 ASN   B N   1 
ATOM   2933 C  CA  . ASN   B 1 124 ? 45.39800 46.43200 -47.61100 1.000 19.94000 ? 168 ASN   B CA  1 
ATOM   2934 C  C   . ASN   B 1 124 ? 46.75000 46.66900 -46.95300 1.000 19.38000 ? 168 ASN   B C   1 
ATOM   2935 O  O   . ASN   B 1 124 ? 47.76600 46.19500 -47.47000 1.000 19.16000 ? 168 ASN   B O   1 
ATOM   2936 C  CB  . ASN   B 1 124 ? 45.41400 47.01900 -49.02700 1.000 20.69000 ? 168 ASN   B CB  1 
ATOM   2937 C  CG  . ASN   B 1 124 ? 44.04100 47.03300 -49.66700 1.000 20.60000 ? 168 ASN   B CG  1 
ATOM   2938 O  OD1 . ASN   B 1 124 ? 43.50400 45.98900 -50.04300 1.000 21.14000 ? 168 ASN   B OD1 1 
ATOM   2939 N  ND2 . ASN   B 1 124 ? 43.46700 48.22000 -49.79600 1.000 22.46000 ? 168 ASN   B ND2 1 
ATOM   2940 N  N   . ARG   B 1 125 ? 46.79100 47.38800 -45.83600 1.000 18.98000 ? 169 ARG   B N   1 
ATOM   2941 C  CA  . ARG   B 1 125 ? 48.03800 47.74900 -45.16600 1.000 18.42000 ? 169 ARG   B CA  1 
ATOM   2942 C  C   . ARG   B 1 125 ? 47.95000 47.28200 -43.71500 1.000 17.82000 ? 169 ARG   B C   1 
ATOM   2943 O  O   . ARG   B 1 125 ? 47.51800 48.03300 -42.83900 1.000 17.75000 ? 169 ARG   B O   1 
ATOM   2944 C  CB  . ARG   B 1 125 ? 48.28700 49.24800 -45.27600 1.000 18.97000 ? 169 ARG   B CB  1 
ATOM   2945 C  CG  . ARG   B 1 125 ? 48.41400 49.71600 -46.71500 1.000 19.45000 ? 169 ARG   B CG  1 
ATOM   2946 C  CD  . ARG   B 1 125 ? 48.83700 51.16300 -46.81700 1.000 21.20000 ? 169 ARG   B CD  1 
ATOM   2947 N  NE  . ARG   B 1 125 ? 47.81700 52.07600 -46.32300 1.000 21.08000 ? 169 ARG   B NE  1 
ATOM   2948 C  CZ  . ARG   B 1 125 ? 48.02700 53.01000 -45.40500 1.000 21.40000 ? 169 ARG   B CZ  1 
ATOM   2949 N  NH1 . ARG   B 1 125 ? 49.21600 53.17900 -44.85100 1.000 21.22000 ? 169 ARG   B NH1 1 
ATOM   2950 N  NH2 . ARG   B 1 125 ? 47.02300 53.80600 -45.04800 1.000 21.54000 ? 169 ARG   B NH2 1 
ATOM   2951 N  N   . LEU   B 1 126 ? 48.36300 46.03900 -43.47600 1.000 17.60000 ? 170 LEU   B N   1 
ATOM   2952 C  CA  . LEU   B 1 126 ? 48.26600 45.38800 -42.18000 1.000 17.35000 ? 170 LEU   B CA  1 
ATOM   2953 C  C   . LEU   B 1 126 ? 49.63500 44.87700 -41.75400 1.000 17.06000 ? 170 LEU   B C   1 
ATOM   2954 O  O   . LEU   B 1 126 ? 50.49700 44.57800 -42.58400 1.000 16.97000 ? 170 LEU   B O   1 
ATOM   2955 C  CB  . LEU   B 1 126 ? 47.26600 44.22600 -42.21700 1.000 17.73000 ? 170 LEU   B CB  1 
ATOM   2956 C  CG  . LEU   B 1 126 ? 45.85200 44.52200 -42.71600 1.000 18.76000 ? 170 LEU   B CG  1 
ATOM   2957 C  CD1 . LEU   B 1 126 ? 45.02900 43.26000 -42.67100 1.000 18.80000 ? 170 LEU   B CD1 1 
ATOM   2958 C  CD2 . LEU   B 1 126 ? 45.19000 45.61500 -41.89600 1.000 18.95000 ? 170 LEU   B CD2 1 
ATOM   2959 N  N   . ALA   B 1 127 ? 49.82500 44.77000 -40.43800 1.000 16.87000 ? 171 ALA   B N   1 
ATOM   2960 C  CA  . ALA   B 1 127 ? 51.08000 44.29000 -39.87500 1.000 16.82000 ? 171 ALA   B CA  1 
ATOM   2961 C  C   . ALA   B 1 127 ? 50.79100 43.48300 -38.61800 1.000 16.53000 ? 171 ALA   B C   1 
ATOM   2962 O  O   . ALA   B 1 127 ? 49.65400 43.41400 -38.14600 1.000 16.45000 ? 171 ALA   B O   1 
ATOM   2963 C  CB  . ALA   B 1 127 ? 52.03500 45.44400 -39.56000 1.000 17.24000 ? 171 ALA   B CB  1 
ATOM   2964 N  N   . VAL   B 1 128 ? 51.84400 42.87000 -38.07600 1.000 16.31000 ? 172 VAL   B N   1 
ATOM   2965 C  CA  . VAL   B 1 128 ? 51.75500 42.08200 -36.85300 1.000 16.16000 ? 172 VAL   B CA  1 
ATOM   2966 C  C   . VAL   B 1 128 ? 52.92200 42.43900 -35.93900 1.000 15.83000 ? 172 VAL   B C   1 
ATOM   2967 O  O   . VAL   B 1 128 ? 54.01400 42.79000 -36.39400 1.000 15.77000 ? 172 VAL   B O   1 
ATOM   2968 C  CB  . VAL   B 1 128 ? 51.74000 40.55800 -37.12800 1.000 16.59000 ? 172 VAL   B CB  1 
ATOM   2969 C  CG1 . VAL   B 1 128 ? 50.43200 40.14300 -37.76600 1.000 16.82000 ? 172 VAL   B CG1 1 
ATOM   2970 C  CG2 . VAL   B 1 128 ? 52.93100 40.14700 -37.99100 1.000 16.56000 ? 172 VAL   B CG2 1 
ATOM   2971 N  N   . MET   B 1 129 ? 52.67900 42.33700 -34.63400 1.000 15.66000 ? 173 MET   B N   1 
ATOM   2972 C  CA  . MET   B 1 129 ? 53.70700 42.54600 -33.62500 1.000 15.43000 ? 173 MET   B CA  1 
ATOM   2973 C  C   . MET   B 1 129 ? 53.39400 41.63300 -32.44600 1.000 15.90000 ? 173 MET   B C   1 
ATOM   2974 O  O   . MET   B 1 129 ? 52.23000 41.33500 -32.17300 1.000 15.58000 ? 173 MET   B O   1 
ATOM   2975 C  CB  . MET   B 1 129 ? 53.77500 44.02400 -33.20600 1.000 15.43000 ? 173 MET   B CB  1 
ATOM   2976 C  CG  . MET   B 1 129 ? 54.82400 44.35300 -32.14800 1.000 15.43000 ? 173 MET   B CG  1 
ATOM   2977 S  SD  . MET   B 1 129 ? 55.23500 46.10900 -32.00800 1.000 16.18000 ? 173 MET   B SD  1 
ATOM   2978 C  CE  . MET   B 1 129 ? 53.65800 46.82900 -31.59000 1.000 16.85000 ? 173 MET   B CE  1 
ATOM   2979 N  N   . GLY   B 1 130 ? 54.43500 41.15800 -31.76900 1.000 15.47000 ? 174 GLY   B N   1 
ATOM   2980 C  CA  . GLY   B 1 130 ? 54.23300 40.23400 -30.66900 1.000 15.70000 ? 174 GLY   B CA  1 
ATOM   2981 C  C   . GLY   B 1 130 ? 55.40700 40.21000 -29.72000 1.000 15.82000 ? 174 GLY   B C   1 
ATOM   2982 O  O   . GLY   B 1 130 ? 56.55000 40.45600 -30.11200 1.000 15.65000 ? 174 GLY   B O   1 
ATOM   2983 N  N   . HIS   B 1 131 ? 55.12000 39.90400 -28.46000 1.000 15.89000 ? 175 HIS   B N   1 
ATOM   2984 C  CA  . HIS   B 1 131 ? 56.15000 39.74000 -27.44500 1.000 15.93000 ? 175 HIS   B CA  1 
ATOM   2985 C  C   . HIS   B 1 131 ? 56.32000 38.26400 -27.12300 1.000 16.23000 ? 175 HIS   B C   1 
ATOM   2986 O  O   . HIS   B 1 131 ? 55.33000 37.54500 -26.95700 1.000 15.99000 ? 175 HIS   B O   1 
ATOM   2987 C  CB  . HIS   B 1 131 ? 55.80100 40.52100 -26.17600 1.000 16.10000 ? 175 HIS   B CB  1 
ATOM   2988 C  CG  . HIS   B 1 131 ? 56.73100 40.25100 -25.03800 1.000 16.14000 ? 175 HIS   B CG  1 
ATOM   2989 N  ND1 . HIS   B 1 131 ? 56.34100 39.57500 -23.90300 1.000 16.04000 ? 175 HIS   B ND1 1 
ATOM   2990 C  CD2 . HIS   B 1 131 ? 58.04100 40.54400 -24.87100 1.000 16.29000 ? 175 HIS   B CD2 1 
ATOM   2991 C  CE1 . HIS   B 1 131 ? 57.36900 39.47300 -23.07900 1.000 16.16000 ? 175 HIS   B CE1 1 
ATOM   2992 N  NE2 . HIS   B 1 131 ? 58.41400 40.05100 -23.64400 1.000 16.33000 ? 175 HIS   B NE2 1 
ATOM   2993 N  N   . ALA   B 1 132 ? 57.57200 37.81600 -27.05100 1.000 16.17000 ? 176 ALA   B N   1 
ATOM   2994 C  CA  . ALA   B 1 132 ? 57.92600 36.48900 -26.53800 1.000 16.08000 ? 176 ALA   B CA  1 
ATOM   2995 C  C   . ALA   B 1 132 ? 57.29200 35.43100 -27.43000 1.000 16.44000 ? 176 ALA   B C   1 
ATOM   2996 O  O   . ALA   B 1 132 ? 57.57700 35.42900 -28.63900 1.000 16.24000 ? 176 ALA   B O   1 
ATOM   2997 C  CB  . ALA   B 1 132 ? 57.54100 36.43000 -25.06000 1.000 16.26000 ? 176 ALA   B CB  1 
ATOM   2998 N  N   . MET   B 1 133 ? 56.46800 34.51800 -26.90900 1.000 16.55000 ? 177 MET   B N   1 
ATOM   2999 C  CA  . MET   B 1 133 ? 55.79100 33.57000 -27.78700 1.000 16.63000 ? 177 MET   B CA  1 
ATOM   3000 C  C   . MET   B 1 133 ? 54.89500 34.28200 -28.78400 1.000 16.42000 ? 177 MET   B C   1 
ATOM   3001 O  O   . MET   B 1 133 ? 54.64600 33.76000 -29.87700 1.000 16.18000 ? 177 MET   B O   1 
ATOM   3002 C  CB  . MET   B 1 133 ? 54.97400 32.57200 -26.98000 1.000 17.16000 ? 177 MET   B CB  1 
ATOM   3003 C  CG  . MET   B 1 133 ? 55.74000 31.34400 -26.62300 1.000 17.50000 ? 177 MET   B CG  1 
ATOM   3004 S  SD  . MET   B 1 133 ? 54.65600 30.07000 -26.01900 1.000 17.39000 ? 177 MET   B SD  1 
ATOM   3005 C  CE  . MET   B 1 133 ? 55.84200 28.79100 -25.70200 1.000 18.10000 ? 177 MET   B CE  1 
ATOM   3006 N  N   . GLY   B 1 134 ? 54.38800 35.46100 -28.42300 1.000 16.46000 ? 178 GLY   B N   1 
ATOM   3007 C  CA  . GLY   B 1 134 ? 53.71800 36.29100 -29.40600 1.000 16.01000 ? 178 GLY   B CA  1 
ATOM   3008 C  C   . GLY   B 1 134 ? 54.65400 36.75900 -30.50300 1.000 15.87000 ? 178 GLY   B C   1 
ATOM   3009 O  O   . GLY   B 1 134 ? 54.22800 36.95800 -31.64200 1.000 15.70000 ? 178 GLY   B O   1 
ATOM   3010 N  N   . GLY   B 1 135 ? 55.93200 36.95600 -30.17300 1.000 15.80000 ? 179 GLY   B N   1 
ATOM   3011 C  CA  . GLY   B 1 135 ? 56.91700 37.26600 -31.19700 1.000 15.72000 ? 179 GLY   B CA  1 
ATOM   3012 C  C   . GLY   B 1 135 ? 57.19400 36.08500 -32.10600 1.000 15.73000 ? 179 GLY   B C   1 
ATOM   3013 O  O   . GLY   B 1 135 ? 57.44100 36.25400 -33.30200 1.000 15.67000 ? 179 GLY   B O   1 
ATOM   3014 N  N   . GLY   B 1 136 ? 57.17400 34.87500 -31.55100 1.000 15.93000 ? 180 GLY   B N   1 
ATOM   3015 C  CA  . GLY   B 1 136 ? 57.15100 33.69300 -32.39400 1.000 16.14000 ? 180 GLY   B CA  1 
ATOM   3016 C  C   . GLY   B 1 136 ? 55.89600 33.62600 -33.24000 1.000 15.93000 ? 180 GLY   B C   1 
ATOM   3017 O  O   . GLY   B 1 136 ? 55.92900 33.17400 -34.38800 1.000 16.17000 ? 180 GLY   B O   1 
ATOM   3018 N  N   . GLY   B 1 137 ? 54.77400 34.09200 -32.69100 1.000 16.00000 ? 181 GLY   B N   1 
ATOM   3019 C  CA  . GLY   B 1 137 ? 53.54800 34.14500 -33.46500 1.000 15.81000 ? 181 GLY   B CA  1 
ATOM   3020 C  C   . GLY   B 1 137 ? 53.58500 35.20300 -34.54400 1.000 15.91000 ? 181 GLY   B C   1 
ATOM   3021 O  O   . GLY   B 1 137 ? 52.89600 35.08300 -35.55900 1.000 15.86000 ? 181 GLY   B O   1 
ATOM   3022 N  N   . SER   B 1 138 ? 54.38300 36.25200 -34.34100 1.000 15.73000 ? 182 SER   B N   1 
ATOM   3023 C  CA  . SER   B 1 138 ? 54.55500 37.26700 -35.37100 1.000 15.71000 ? 182 SER   B CA  1 
ATOM   3024 C  C   . SER   B 1 138 ? 55.29700 36.70000 -36.57500 1.000 15.88000 ? 182 SER   B C   1 
ATOM   3025 O  O   . SER   B 1 138 ? 54.93600 36.98000 -37.72500 1.000 15.91000 ? 182 SER   B O   1 
ATOM   3026 C  CB  . SER   B 1 138 ? 55.29500 38.46800 -34.78800 1.000 15.72000 ? 182 SER   B CB  1 
ATOM   3027 O  OG  . SER   B 1 138 ? 55.36700 39.53000 -35.71500 1.000 15.57000 ? 182 SER   B OG  1 
ATOM   3028 N  N   . LEU   B 1 139 ? 56.33600 35.90000 -36.32400 1.000 15.92000 ? 183 LEU   B N   1 
ATOM   3029 C  CA  . LEU   B 1 139 ? 57.02600 35.20300 -37.40100 1.000 16.25000 ? 183 LEU   B CA  1 
ATOM   3030 C  C   . LEU   B 1 139 ? 56.10900 34.19300 -38.07300 1.000 16.11000 ? 183 LEU   B C   1 
ATOM   3031 O  O   . LEU   B 1 139 ? 56.11800 34.06000 -39.30100 1.000 16.23000 ? 183 LEU   B O   1 
ATOM   3032 C  CB  . LEU   B 1 139 ? 58.27200 34.51100 -36.85900 1.000 16.48000 ? 183 LEU   B CB  1 
ATOM   3033 C  CG  . LEU   B 1 139 ? 59.42900 35.39900 -36.40500 1.000 16.52000 ? 183 LEU   B CG  1 
ATOM   3034 C  CD1 . LEU   B 1 139 ? 60.45100 34.56500 -35.65600 1.000 16.81000 ? 183 LEU   B CD1 1 
ATOM   3035 C  CD2 . LEU   B 1 139 ? 60.08500 36.09600 -37.58300 1.000 16.40000 ? 183 LEU   B CD2 1 
ATOM   3036 N  N   . GLU   B 1 140 ? 55.31000 33.47400 -37.28100 1.000 16.11000 ? 184 GLU   B N   1 
ATOM   3037 C  CA  . GLU   B 1 140 ? 54.38500 32.49600 -37.84200 1.000 16.26000 ? 184 GLU   B CA  1 
ATOM   3038 C  C   . GLU   B 1 140 ? 53.34600 33.16500 -38.72900 1.000 16.02000 ? 184 GLU   B C   1 
ATOM   3039 O  O   . GLU   B 1 140 ? 53.01100 32.64800 -39.80000 1.000 16.42000 ? 184 GLU   B O   1 
ATOM   3040 C  CB  . GLU   B 1 140 ? 53.70000 31.71600 -36.72000 1.000 16.50000 ? 184 GLU   B CB  1 
ATOM   3041 C  CG  . GLU   B 1 140 ? 54.59100 30.71300 -36.00500 1.000 16.70000 ? 184 GLU   B CG  1 
ATOM   3042 C  CD  . GLU   B 1 140 ? 54.62400 29.36700 -36.69400 1.000 17.08000 ? 184 GLU   B CD  1 
ATOM   3043 O  OE1 . GLU   B 1 140 ? 54.09600 29.26400 -37.81800 1.000 16.69000 ? 184 GLU   B OE1 1 
ATOM   3044 O  OE2 . GLU   B 1 140 ? 55.17300 28.40900 -36.11100 1.000 17.45000 ? 184 GLU   B OE2 1 
ATOM   3045 N  N   . ALA   B 1 141 ? 52.83000 34.32000 -38.29900 1.000 16.90000 ? 185 ALA   B N   1 
ATOM   3046 C  CA  . ALA   B 1 141 ? 51.78400 35.00200 -39.05300 1.000 16.18000 ? 185 ALA   B CA  1 
ATOM   3047 C  C   . ALA   B 1 141 ? 52.26800 35.45100 -40.42600 1.000 16.44000 ? 185 ALA   B C   1 
ATOM   3048 O  O   . ALA   B 1 141 ? 51.47300 35.51700 -41.36800 1.000 16.41000 ? 185 ALA   B O   1 
ATOM   3049 C  CB  . ALA   B 1 141 ? 51.26200 36.20400 -38.26500 1.000 16.59000 ? 185 ALA   B CB  1 
ATOM   3050 N  N   . THR   B 1 142 ? 53.55500 35.76900 -40.56200 1.000 16.21000 ? 186 THR   B N   1 
ATOM   3051 C  CA  . THR   B 1 142 ? 54.05900 36.21000 -41.85700 1.000 16.19000 ? 186 THR   B CA  1 
ATOM   3052 C  C   . THR   B 1 142 ? 54.25200 35.05100 -42.81700 1.000 16.31000 ? 186 THR   B C   1 
ATOM   3053 O  O   . THR   B 1 142 ? 54.16600 35.24200 -44.03500 1.000 16.48000 ? 186 THR   B O   1 
ATOM   3054 C  CB  . THR   B 1 142 ? 55.36700 36.97500 -41.69400 1.000 16.41000 ? 186 THR   B CB  1 
ATOM   3055 O  OG1 . THR   B 1 142 ? 56.36100 36.12100 -41.12200 1.000 16.21000 ? 186 THR   B OG1 1 
ATOM   3056 C  CG2 . THR   B 1 142 ? 55.15000 38.16500 -40.79900 1.000 16.28000 ? 186 THR   B CG2 1 
ATOM   3057 N  N   . VAL   B 1 143 ? 54.51500 33.85100 -42.29600 1.000 16.18000 ? 187 VAL   B N   1 
ATOM   3058 C  CA  . VAL   B 1 143 ? 54.55400 32.67300 -43.15200 1.000 16.27000 ? 187 VAL   B CA  1 
ATOM   3059 C  C   . VAL   B 1 143 ? 53.14500 32.29700 -43.58700 1.000 16.46000 ? 187 VAL   B C   1 
ATOM   3060 O  O   . VAL   B 1 143 ? 52.93800 31.82400 -44.71100 1.000 16.41000 ? 187 VAL   B O   1 
ATOM   3061 C  CB  . VAL   B 1 143 ? 55.26600 31.51700 -42.42500 1.000 16.17000 ? 187 VAL   B CB  1 
ATOM   3062 C  CG1 . VAL   B 1 143 ? 55.31200 30.27500 -43.29400 1.000 16.38000 ? 187 VAL   B CG1 1 
ATOM   3063 C  CG2 . VAL   B 1 143 ? 56.67200 31.93100 -42.03000 1.000 16.19000 ? 187 VAL   B CG2 1 
ATOM   3064 N  N   . MET   B 1 144 ? 52.15300 32.52400 -42.72700 1.000 16.55000 ? 188 MET   B N   1 
ATOM   3065 C  CA  . MET   B 1 144 ? 50.77600 32.17700 -43.05200 1.000 16.94000 ? 188 MET   B CA  1 
ATOM   3066 C  C   . MET   B 1 144 ? 50.09400 33.21300 -43.93100 1.000 16.81000 ? 188 MET   B C   1 
ATOM   3067 O  O   . MET   B 1 144 ? 49.05800 32.90600 -44.52800 1.000 16.54000 ? 188 MET   B O   1 
ATOM   3068 C  CB  . MET   B 1 144 ? 49.96300 32.00200 -41.77200 1.000 17.86000 ? 188 MET   B CB  1 
ATOM   3069 C  CG  . MET   B 1 144 ? 50.51600 30.97500 -40.82400 1.000 18.25000 ? 188 MET   B CG  1 
ATOM   3070 S  SD  . MET   B 1 144 ? 49.78500 31.13600 -39.18800 1.000 18.18000 ? 188 MET   B SD  1 
ATOM   3071 C  CE  . MET   B 1 144 ? 50.41000 29.64000 -38.42900 1.000 19.24000 ? 188 MET   B CE  1 
ATOM   3072 N  N   . ARG   B 1 145 ? 50.63400 34.42900 -44.00200 1.000 16.84000 ? 189 ARG   B N   1 
ATOM   3073 C  CA  . ARG   B 1 145 ? 50.03500 35.50400 -44.79200 1.000 17.31000 ? 189 ARG   B CA  1 
ATOM   3074 C  C   . ARG   B 1 145 ? 51.14300 36.43300 -45.25900 1.000 17.23000 ? 189 ARG   B C   1 
ATOM   3075 O  O   . ARG   B 1 145 ? 51.43800 37.44800 -44.61500 1.000 17.05000 ? 189 ARG   B O   1 
ATOM   3076 C  CB  . ARG   B 1 145 ? 48.97900 36.27400 -44.00000 1.000 16.97000 ? 189 ARG   B CB  1 
ATOM   3077 C  CG  . ARG   B 1 145 ? 48.15800 37.22800 -44.86000 1.000 16.86000 ? 189 ARG   B CG  1 
ATOM   3078 C  CD  . ARG   B 1 145 ? 46.96600 37.81900 -44.12200 1.000 16.79000 ? 189 ARG   B CD  1 
ATOM   3079 N  NE  . ARG   B 1 145 ? 45.94700 36.82600 -43.80100 1.000 17.01000 ? 189 ARG   B NE  1 
ATOM   3080 C  CZ  . ARG   B 1 145 ? 44.82000 37.09100 -43.15400 1.000 17.07000 ? 189 ARG   B CZ  1 
ATOM   3081 N  NH1 . ARG   B 1 145 ? 44.54100 38.30900 -42.72300 1.000 17.06000 ? 189 ARG   B NH1 1 
ATOM   3082 N  NH2 . ARG   B 1 145 ? 43.95000 36.11000 -42.93600 1.000 17.27000 ? 189 ARG   B NH2 1 
ATOM   3083 N  N   . PRO   B 1 146 ? 51.77300 36.12600 -46.39800 1.000 17.07000 ? 190 PRO   B N   1 
ATOM   3084 C  CA  . PRO   B 1 146 ? 52.90900 36.94000 -46.85900 1.000 17.67000 ? 190 PRO   B CA  1 
ATOM   3085 C  C   . PRO   B 1 146 ? 52.53000 38.33100 -47.32800 1.000 17.67000 ? 190 PRO   B C   1 
ATOM   3086 O  O   . PRO   B 1 146 ? 53.43200 39.13000 -47.59900 1.000 17.16000 ? 190 PRO   B O   1 
ATOM   3087 C  CB  . PRO   B 1 146 ? 53.49000 36.11200 -48.01400 1.000 17.65000 ? 190 PRO   B CB  1 
ATOM   3088 C  CG  . PRO   B 1 146 ? 52.94100 34.73900 -47.82900 1.000 17.77000 ? 190 PRO   B CG  1 
ATOM   3089 C  CD  . PRO   B 1 146 ? 51.59200 34.91900 -47.22200 1.000 17.54000 ? 190 PRO   B CD  1 
ATOM   3090 N  N   . SER   B 1 147 ? 51.24300 38.64800 -47.43800 1.000 17.58000 ? 191 SER   B N   1 
ATOM   3091 C  CA  . SER   B 1 147 ? 50.81400 39.97800 -47.84100 1.000 17.45000 ? 191 SER   B CA  1 
ATOM   3092 C  C   . SER   B 1 147 ? 50.88900 40.99400 -46.71000 1.000 17.17000 ? 191 SER   B C   1 
ATOM   3093 O  O   . SER   B 1 147 ? 50.56900 42.16600 -46.93300 1.000 17.33000 ? 191 SER   B O   1 
ATOM   3094 C  CB  . SER   B 1 147 ? 49.38800 39.93100 -48.39600 1.000 17.30000 ? 191 SER   B CB  1 
ATOM   3095 O  OG  . SER   B 1 147 ? 48.44000 39.64700 -47.38400 1.000 16.91000 ? 191 SER   B OG  1 
ATOM   3096 N  N   . LEU   B 1 148 ? 51.29700 40.58300 -45.51200 1.000 17.08000 ? 192 LEU   B N   1 
ATOM   3097 C  CA  . LEU   B 1 148 ? 51.51100 41.53700 -44.43100 1.000 17.07000 ? 192 LEU   B CA  1 
ATOM   3098 C  C   . LEU   B 1 148 ? 52.64100 42.49500 -44.78700 1.000 17.06000 ? 192 LEU   B C   1 
ATOM   3099 O  O   . LEU   B 1 148 ? 53.63200 42.11000 -45.41400 1.000 17.01000 ? 192 LEU   B O   1 
ATOM   3100 C  CB  . LEU   B 1 148 ? 51.83200 40.80300 -43.12700 1.000 16.91000 ? 192 LEU   B CB  1 
ATOM   3101 C  CG  . LEU   B 1 148 ? 50.73000 39.90400 -42.56600 1.000 16.88000 ? 192 LEU   B CG  1 
ATOM   3102 C  CD1 . LEU   B 1 148 ? 51.27000 39.05400 -41.42700 1.000 17.03000 ? 192 LEU   B CD1 1 
ATOM   3103 C  CD2 . LEU   B 1 148 ? 49.53000 40.73200 -42.12300 1.000 16.70000 ? 192 LEU   B CD2 1 
ATOM   3104 N  N   . LYS   B 1 149 ? 52.49000 43.75300 -44.36700 1.000 17.08000 ? 193 LYS   B N   1 
ATOM   3105 C  CA  . LYS   B 1 149 ? 53.44000 44.79300 -44.73800 1.000 17.49000 ? 193 LYS   B CA  1 
ATOM   3106 C  C   . LYS   B 1 149 ? 54.65800 44.83500 -43.82200 1.000 17.41000 ? 193 LYS   B C   1 
ATOM   3107 O  O   . LYS   B 1 149 ? 55.74400 45.22100 -44.27000 1.000 17.55000 ? 193 LYS   B O   1 
ATOM   3108 C  CB  . LYS   B 1 149 ? 52.74700 46.15600 -44.73800 1.000 17.89000 ? 193 LYS   B CB  1 
ATOM   3109 C  CG  . LYS   B 1 149 ? 51.67600 46.31200 -45.80100 1.000 18.09000 ? 193 LYS   B CG  1 
ATOM   3110 C  CD  . LYS   B 1 149 ? 52.27500 46.14400 -47.18300 1.000 18.48000 ? 193 LYS   B CD  1 
ATOM   3111 C  CE  . LYS   B 1 149 ? 51.22900 46.35500 -48.26000 1.000 19.35000 ? 193 LYS   B CE  1 
ATOM   3112 N  NZ  . LYS   B 1 149 ? 51.73200 45.94900 -49.60200 1.000 20.41000 ? 193 LYS   B NZ  1 
ATOM   3113 N  N   . ALA   B 1 150 ? 54.50700 44.45900 -42.55100 1.000 17.14000 ? 194 ALA   B N   1 
ATOM   3114 C  CA  . ALA   B 1 150 ? 55.61100 44.53700 -41.60400 1.000 17.29000 ? 194 ALA   B CA  1 
ATOM   3115 C  C   . ALA   B 1 150 ? 55.39300 43.53300 -40.47900 1.000 16.69000 ? 194 ALA   B C   1 
ATOM   3116 O  O   . ALA   B 1 150 ? 54.28800 43.02400 -40.27700 1.000 16.49000 ? 194 ALA   B O   1 
ATOM   3117 C  CB  . ALA   B 1 150 ? 55.77200 45.95500 -41.04300 1.000 17.65000 ? 194 ALA   B CB  1 
ATOM   3118 N  N   . SER   B 1 151 ? 56.47100 43.25300 -39.74700 1.000 16.43000 ? 195 SER   B N   1 
ATOM   3119 C  CA  . SER   B 1 151 ? 56.45400 42.25000 -38.69200 1.000 16.20000 ? 195 SER   B CA  1 
ATOM   3120 C  C   . SER   B 1 151 ? 57.51300 42.61400 -37.66200 1.000 15.88000 ? 195 SER   B C   1 
ATOM   3121 O  O   . SER   B 1 151 ? 58.65500 42.91100 -38.02900 1.000 16.19000 ? 195 SER   B O   1 
ATOM   3122 C  CB  . SER   B 1 151 ? 56.71000 40.85800 -39.26800 1.000 16.26000 ? 195 SER   B CB  1 
ATOM   3123 O  OG  . SER   B 1 151 ? 56.79500 39.86800 -38.26200 1.000 15.95000 ? 195 SER   B OG  1 
ATOM   3124 N  N   . ILE   B 1 152 ? 57.13000 42.61200 -36.38400 1.000 15.61000 ? 196 ILE   B N   1 
ATOM   3125 C  CA  . ILE   B 1 152 ? 58.03800 42.99900 -35.30200 1.000 15.53000 ? 196 ILE   B CA  1 
ATOM   3126 C  C   . ILE   B 1 152 ? 57.95700 42.00000 -34.15000 1.000 15.39000 ? 196 ILE   B C   1 
ATOM   3127 O  O   . ILE   B 1 152 ? 57.05900 42.10600 -33.30200 1.000 15.41000 ? 196 ILE   B O   1 
ATOM   3128 C  CB  . ILE   B 1 152 ? 57.73700 44.42400 -34.80900 1.000 15.46000 ? 196 ILE   B CB  1 
ATOM   3129 C  CG1 . ILE   B 1 152 ? 57.76300 45.40800 -35.98400 1.000 15.98000 ? 196 ILE   B CG1 1 
ATOM   3130 C  CG2 . ILE   B 1 152 ? 58.74500 44.84200 -33.74500 1.000 15.88000 ? 196 ILE   B CG2 1 
ATOM   3131 C  CD1 . ILE   B 1 152 ? 57.34100 46.80700 -35.64000 1.000 17.61000 ? 196 ILE   B CD1 1 
ATOM   3132 N  N   . PRO   B 1 153 ? 58.85800 41.01700 -34.08200 1.000 15.46000 ? 197 PRO   B N   1 
ATOM   3133 C  CA  . PRO   B 1 153 ? 58.91200 40.11300 -32.92100 1.000 15.50000 ? 197 PRO   B CA  1 
ATOM   3134 C  C   . PRO   B 1 153 ? 59.73000 40.72300 -31.79000 1.000 15.63000 ? 197 PRO   B C   1 
ATOM   3135 O  O   . PRO   B 1 153 ? 60.93100 40.96300 -31.93200 1.000 15.91000 ? 197 PRO   B O   1 
ATOM   3136 C  CB  . PRO   B 1 153 ? 59.58500 38.85500 -33.48400 1.000 15.57000 ? 197 PRO   B CB  1 
ATOM   3137 C  CG  . PRO   B 1 153 ? 59.50600 39.00000 -34.98000 1.000 15.66000 ? 197 PRO   B CG  1 
ATOM   3138 C  CD  . PRO   B 1 153 ? 59.60600 40.46500 -35.21900 1.000 15.61000 ? 197 PRO   B CD  1 
ATOM   3139 N  N   . LEU   B 1 154 ? 59.07300 40.96300 -30.65800 1.000 15.85000 ? 198 LEU   B N   1 
ATOM   3140 C  CA  . LEU   B 1 154 ? 59.69900 41.54400 -29.47600 1.000 16.05000 ? 198 LEU   B CA  1 
ATOM   3141 C  C   . LEU   B 1 154 ? 60.16700 40.42300 -28.56000 1.000 16.33000 ? 198 LEU   B C   1 
ATOM   3142 O  O   . LEU   B 1 154 ? 59.34700 39.63500 -28.07900 1.000 15.85000 ? 198 LEU   B O   1 
ATOM   3143 C  CB  . LEU   B 1 154 ? 58.71600 42.45500 -28.74400 1.000 16.23000 ? 198 LEU   B CB  1 
ATOM   3144 C  CG  . LEU   B 1 154 ? 58.06000 43.52400 -29.61000 1.000 16.43000 ? 198 LEU   B CG  1 
ATOM   3145 C  CD1 . LEU   B 1 154 ? 56.88900 44.17600 -28.89800 1.000 16.89000 ? 198 LEU   B CD1 1 
ATOM   3146 C  CD2 . LEU   B 1 154 ? 59.10300 44.55300 -29.97800 1.000 16.55000 ? 198 LEU   B CD2 1 
ATOM   3147 N  N   . THR   B 1 155 ? 61.47400 40.37400 -28.30500 1.000 16.12000 ? 199 THR   B N   1 
ATOM   3148 C  CA  . THR   B 1 155 ? 62.13700 39.30700 -27.55900 1.000 16.20000 ? 199 THR   B CA  1 
ATOM   3149 C  C   . THR   B 1 155 ? 61.46800 37.95800 -27.85200 1.000 16.11000 ? 199 THR   B C   1 
ATOM   3150 O  O   . THR   B 1 155 ? 60.92200 37.32300 -26.94400 1.000 16.04000 ? 199 THR   B O   1 
ATOM   3151 C  CB  . THR   B 1 155 ? 62.15300 39.60000 -26.06300 1.000 16.47000 ? 199 THR   B CB  1 
ATOM   3152 O  OG1 . THR   B 1 155 ? 60.81000 39.59900 -25.56200 1.000 16.26000 ? 199 THR   B OG1 1 
ATOM   3153 C  CG2 . THR   B 1 155 ? 62.78100 40.95800 -25.80500 1.000 16.89000 ? 199 THR   B CG2 1 
ATOM   3154 N  N   . PRO   B 1 156 ? 61.48200 37.50800 -29.10500 1.000 15.98000 ? 200 PRO   B N   1 
ATOM   3155 C  CA  . PRO   B 1 156 ? 60.64700 36.37000 -29.49200 1.000 16.18000 ? 200 PRO   B CA  1 
ATOM   3156 C  C   . PRO   B 1 156 ? 61.16400 35.05300 -28.93900 1.000 16.94000 ? 200 PRO   B C   1 
ATOM   3157 O  O   . PRO   B 1 156 ? 62.35100 34.87400 -28.65800 1.000 16.41000 ? 200 PRO   B O   1 
ATOM   3158 C  CB  . PRO   B 1 156 ? 60.71400 36.38600 -31.02200 1.000 15.93000 ? 200 PRO   B CB  1 
ATOM   3159 C  CG  . PRO   B 1 156 ? 62.04300 36.98300 -31.32000 1.000 16.02000 ? 200 PRO   B CG  1 
ATOM   3160 C  CD  . PRO   B 1 156 ? 62.30800 37.99400 -30.22800 1.000 16.04000 ? 200 PRO   B CD  1 
ATOM   3161 N  N   . TRP   B 1 157 ? 60.22800 34.12000 -28.79800 1.000 16.45000 ? 201 TRP   B N   1 
ATOM   3162 C  CA  . TRP   B 1 157 ? 60.49900 32.75400 -28.38100 1.000 17.10000 ? 201 TRP   B CA  1 
ATOM   3163 C  C   . TRP   B 1 157 ? 59.90400 31.81200 -29.41400 1.000 17.52000 ? 201 TRP   B C   1 
ATOM   3164 O  O   . TRP   B 1 157 ? 58.71000 31.89900 -29.71500 1.000 16.98000 ? 201 TRP   B O   1 
ATOM   3165 C  CB  . TRP   B 1 157 ? 59.89400 32.46900 -27.00000 1.000 17.41000 ? 201 TRP   B CB  1 
ATOM   3166 C  CG  . TRP   B 1 157 ? 60.25900 31.13100 -26.44000 1.000 17.83000 ? 201 TRP   B CG  1 
ATOM   3167 C  CD1 . TRP   B 1 157 ? 61.20700 30.87700 -25.49900 1.000 18.13000 ? 201 TRP   B CD1 1 
ATOM   3168 C  CD2 . TRP   B 1 157 ? 59.68700 29.86300 -26.78700 1.000 18.12000 ? 201 TRP   B CD2 1 
ATOM   3169 N  NE1 . TRP   B 1 157 ? 61.26500 29.53100 -25.23800 1.000 18.43000 ? 201 TRP   B NE1 1 
ATOM   3170 C  CE2 . TRP   B 1 157 ? 60.33900 28.88800 -26.01300 1.000 18.76000 ? 201 TRP   B CE2 1 
ATOM   3171 C  CE3 . TRP   B 1 157 ? 58.68500 29.45900 -27.67200 1.000 18.16000 ? 201 TRP   B CE3 1 
ATOM   3172 C  CZ2 . TRP   B 1 157 ? 60.02300 27.53900 -26.09700 1.000 19.42000 ? 201 TRP   B CZ2 1 
ATOM   3173 C  CZ3 . TRP   B 1 157 ? 58.38000 28.11800 -27.75900 1.000 18.55000 ? 201 TRP   B CZ3 1 
ATOM   3174 C  CH2 . TRP   B 1 157 ? 59.03700 27.17700 -26.97100 1.000 18.86000 ? 201 TRP   B CH2 1 
ATOM   3175 N  N   . HIS   B 1 158 ? 60.72800 30.91200 -29.94700 1.000 17.45000 ? 202 HIS   B N   1 
ATOM   3176 C  CA  . HIS   B 1 158 ? 60.24500 29.89700 -30.87400 1.000 17.75000 ? 202 HIS   B CA  1 
ATOM   3177 C  C   . HIS   B 1 158 ? 61.22900 28.73500 -30.90100 1.000 18.10000 ? 202 HIS   B C   1 
ATOM   3178 O  O   . HIS   B 1 158 ? 62.44400 28.93900 -30.93700 1.000 17.65000 ? 202 HIS   B O   1 
ATOM   3179 C  CB  . HIS   B 1 158 ? 60.04700 30.46600 -32.28800 1.000 17.79000 ? 202 HIS   B CB  1 
ATOM   3180 C  CG  . HIS   B 1 158 ? 58.94900 29.80000 -33.05800 1.000 18.09000 ? 202 HIS   B CG  1 
ATOM   3181 N  ND1 . HIS   B 1 158 ? 58.94300 28.45100 -33.33000 1.000 18.17000 ? 202 HIS   B ND1 1 
ATOM   3182 C  CD2 . HIS   B 1 158 ? 57.81400 30.29700 -33.60100 1.000 17.79000 ? 202 HIS   B CD2 1 
ATOM   3183 C  CE1 . HIS   B 1 158 ? 57.85200 28.14400 -34.00600 1.000 18.36000 ? 202 HIS   B CE1 1 
ATOM   3184 N  NE2 . HIS   B 1 158 ? 57.15300 29.24800 -34.18900 1.000 17.75000 ? 202 HIS   B NE2 1 
ATOM   3185 N  N   . LEU   B 1 159 ? 60.68500 27.51700 -30.87800 1.000 18.11000 ? 203 LEU   B N   1 
ATOM   3186 C  CA  . LEU   B 1 159 ? 61.51000 26.32000 -31.00000 1.000 18.27000 ? 203 LEU   B CA  1 
ATOM   3187 C  C   . LEU   B 1 159 ? 62.19900 26.24800 -32.35400 1.000 18.29000 ? 203 LEU   B C   1 
ATOM   3188 O  O   . LEU   B 1 159 ? 63.33400 25.76900 -32.45500 1.000 18.26000 ? 203 LEU   B O   1 
ATOM   3189 C  CB  . LEU   B 1 159 ? 60.65200 25.07900 -30.80100 1.000 18.27000 ? 203 LEU   B CB  1 
ATOM   3190 C  CG  . LEU   B 1 159 ? 59.95100 24.99700 -29.46200 1.000 18.44000 ? 203 LEU   B CG  1 
ATOM   3191 C  CD1 . LEU   B 1 159 ? 58.86300 23.95500 -29.53900 1.000 17.99000 ? 203 LEU   B CD1 1 
ATOM   3192 C  CD2 . LEU   B 1 159 ? 60.98400 24.65300 -28.40100 1.000 21.91000 ? 203 LEU   B CD2 1 
ATOM   3193 N  N   . ASP   B 1 160 ? 61.52400 26.69500 -33.40700 1.000 18.48000 ? 204 ASP   B N   1 
ATOM   3194 C  CA  . ASP   B 1 160 ? 62.02700 26.54800 -34.76500 1.000 18.73000 ? 204 ASP   B CA  1 
ATOM   3195 C  C   . ASP   B 1 160 ? 62.86700 27.76200 -35.13900 1.000 18.68000 ? 204 ASP   B C   1 
ATOM   3196 O  O   . ASP   B 1 160 ? 62.40900 28.90200 -35.01400 1.000 18.33000 ? 204 ASP   B O   1 
ATOM   3197 C  CB  . ASP   B 1 160 ? 60.85900 26.35900 -35.73200 1.000 18.99000 ? 204 ASP   B CB  1 
ATOM   3198 C  CG  . ASP   B 1 160 ? 59.98200 25.17800 -35.35200 1.000 18.73000 ? 204 ASP   B CG  1 
ATOM   3199 O  OD1 . ASP   B 1 160 ? 60.53400 24.13800 -34.93400 1.000 19.23000 ? 204 ASP   B OD1 1 
ATOM   3200 O  OD2 . ASP   B 1 160 ? 58.74100 25.28800 -35.46000 1.000 18.62000 ? 204 ASP   B OD2 1 
ATOM   3201 N  N   . LYS   B 1 161 ? 64.09400 27.51400 -35.59600 1.000 18.56000 ? 205 LYS   B N   1 
ATOM   3202 C  CA  . LYS   B 1 161 ? 65.09600 28.56300 -35.74500 1.000 18.38000 ? 205 LYS   B CA  1 
ATOM   3203 C  C   . LYS   B 1 161 ? 65.32000 29.01300 -37.18500 1.000 18.23000 ? 205 LYS   B C   1 
ATOM   3204 O  O   . LYS   B 1 161 ? 66.07500 29.96600 -37.40300 1.000 17.84000 ? 205 LYS   B O   1 
ATOM   3205 C  CB  . LYS   B 1 161 ? 66.43700 28.09600 -35.16000 1.000 17.57000 ? 205 LYS   B CB  1 
ATOM   3206 C  CG  . LYS   B 1 161 ? 66.33400 27.35800 -33.82900 1.000 17.61000 ? 205 LYS   B CG  1 
ATOM   3207 C  CD  . LYS   B 1 161 ? 65.78600 28.24700 -32.72300 1.000 17.65000 ? 205 LYS   B CD  1 
ATOM   3208 C  CE  . LYS   B 1 161 ? 65.69500 27.49100 -31.40900 1.000 17.47000 ? 205 LYS   B CE  1 
ATOM   3209 N  NZ  . LYS   B 1 161 ? 65.00600 28.29500 -30.36600 1.000 17.09000 ? 205 LYS   B NZ  1 
ATOM   3210 N  N   . THR   B 1 162 ? 64.69900 28.36400 -38.16700 1.000 18.33000 ? 206 THR   B N   1 
ATOM   3211 C  CA  . THR   B 1 162 ? 64.91300 28.67000 -39.57600 1.000 18.55000 ? 206 THR   B CA  1 
ATOM   3212 C  C   . THR   B 1 162 ? 63.67700 29.36100 -40.13400 1.000 18.19000 ? 206 THR   B C   1 
ATOM   3213 O  O   . THR   B 1 162 ? 62.57600 28.80300 -40.08500 1.000 17.85000 ? 206 THR   B O   1 
ATOM   3214 C  CB  . THR   B 1 162 ? 65.21900 27.40300 -40.37400 1.000 19.14000 ? 206 THR   B CB  1 
ATOM   3215 O  OG1 . THR   B 1 162 ? 66.43700 26.81500 -39.89600 1.000 21.28000 ? 206 THR   B OG1 1 
ATOM   3216 C  CG2 . THR   B 1 162 ? 65.36300 27.72600 -41.86000 1.000 22.22000 ? 206 THR   B CG2 1 
ATOM   3217 N  N   . TRP   B 1 163 ? 63.86500 30.56100 -40.68200 1.000 18.08000 ? 207 TRP   B N   1 
ATOM   3218 C  CA  . TRP   B 1 163 ? 62.77400 31.37200 -41.21600 1.000 18.06000 ? 207 TRP   B CA  1 
ATOM   3219 C  C   . TRP   B 1 163 ? 63.14100 31.93700 -42.58200 1.000 18.14000 ? 207 TRP   B C   1 
ATOM   3220 O  O   . TRP   B 1 163 ? 62.90000 33.10600 -42.88800 1.000 18.12000 ? 207 TRP   B O   1 
ATOM   3221 C  CB  . TRP   B 1 163 ? 62.42200 32.47800 -40.22800 1.000 18.04000 ? 207 TRP   B CB  1 
ATOM   3222 C  CG  . TRP   B 1 163 ? 61.86300 31.92600 -38.95600 1.000 17.79000 ? 207 TRP   B CG  1 
ATOM   3223 C  CD1 . TRP   B 1 163 ? 62.55100 31.63600 -37.81400 1.000 17.91000 ? 207 TRP   B CD1 1 
ATOM   3224 C  CD2 . TRP   B 1 163 ? 60.50300 31.55200 -38.71100 1.000 17.66000 ? 207 TRP   B CD2 1 
ATOM   3225 N  NE1 . TRP   B 1 163 ? 61.69900 31.12400 -36.86800 1.000 17.84000 ? 207 TRP   B NE1 1 
ATOM   3226 C  CE2 . TRP   B 1 163 ? 60.43600 31.06200 -37.39400 1.000 17.97000 ? 207 TRP   B CE2 1 
ATOM   3227 C  CE3 . TRP   B 1 163 ? 59.33300 31.59700 -39.47400 1.000 17.54000 ? 207 TRP   B CE3 1 
ATOM   3228 C  CZ2 . TRP   B 1 163 ? 59.24600 30.61800 -36.82400 1.000 17.64000 ? 207 TRP   B CZ2 1 
ATOM   3229 C  CZ3 . TRP   B 1 163 ? 58.15500 31.15900 -38.90700 1.000 17.11000 ? 207 TRP   B CZ3 1 
ATOM   3230 C  CH2 . TRP   B 1 163 ? 58.11900 30.67300 -37.59500 1.000 17.26000 ? 207 TRP   B CH2 1 
ATOM   3231 N  N   . GLY   B 1 164 ? 63.71800 31.09000 -43.43100 1.000 18.18000 ? 208 GLY   B N   1 
ATOM   3232 C  CA  . GLY   B 1 164 ? 64.18100 31.48000 -44.74700 1.000 18.21000 ? 208 GLY   B CA  1 
ATOM   3233 C  C   . GLY   B 1 164 ? 63.12000 31.65600 -45.80900 1.000 19.01000 ? 208 GLY   B C   1 
ATOM   3234 O  O   . GLY   B 1 164 ? 63.46400 31.93100 -46.96100 1.000 19.16000 ? 208 GLY   B O   1 
ATOM   3235 N  N   . GLN   B 1 165 ? 61.84100 31.50500 -45.46700 1.000 19.47000 ? 209 GLN   B N   1 
ATOM   3236 C  CA  . GLN   B 1 165 ? 60.74700 31.71700 -46.40700 1.000 20.08000 ? 209 GLN   B CA  1 
ATOM   3237 C  C   . GLN   B 1 165 ? 59.95100 32.97500 -46.09500 1.000 19.13000 ? 209 GLN   B C   1 
ATOM   3238 O  O   . GLN   B 1 165 ? 58.93000 33.23200 -46.74200 1.000 18.76000 ? 209 GLN   B O   1 
ATOM   3239 C  CB  . GLN   B 1 165 ? 59.81700 30.50700 -46.42000 1.000 21.16000 ? 209 GLN   B CB  1 
ATOM   3240 C  CG  . GLN   B 1 165 ? 60.53700 29.18500 -46.57800 1.000 23.34000 ? 209 GLN   B CG  1 
ATOM   3241 C  CD  . GLN   B 1 165 ? 60.64800 28.75600 -48.02100 1.000 24.12000 ? 209 GLN   B CD  1 
ATOM   3242 O  OE1 . GLN   B 1 165 ? 59.68300 28.84700 -48.78000 1.000 26.72000 ? 209 GLN   B OE1 1 
ATOM   3243 N  NE2 . GLN   B 1 165 ? 61.83000 28.28900 -48.41300 1.000 28.37000 ? 209 GLN   B NE2 1 
ATOM   3244 N  N   . VAL   B 1 166 ? 60.39400 33.76200 -45.11800 1.000 18.50000 ? 210 VAL   B N   1 
ATOM   3245 C  CA  . VAL   B 1 166 ? 59.67100 34.96200 -44.72500 1.000 18.03000 ? 210 VAL   B CA  1 
ATOM   3246 C  C   . VAL   B 1 166 ? 59.85600 36.03300 -45.79200 1.000 17.69000 ? 210 VAL   B C   1 
ATOM   3247 O  O   . VAL   B 1 166 ? 60.97800 36.29000 -46.24700 1.000 17.92000 ? 210 VAL   B O   1 
ATOM   3248 C  CB  . VAL   B 1 166 ? 60.15400 35.44400 -43.34700 1.000 18.24000 ? 210 VAL   B CB  1 
ATOM   3249 C  CG1 . VAL   B 1 166 ? 59.60800 36.82900 -43.04000 1.000 17.68000 ? 210 VAL   B CG1 1 
ATOM   3250 C  CG2 . VAL   B 1 166 ? 59.75400 34.44000 -42.26400 1.000 18.30000 ? 210 VAL   B CG2 1 
ATOM   3251 N  N   . GLN   B 1 167 ? 58.74900 36.65700 -46.20000 1.000 17.23000 ? 211 GLN   B N   1 
ATOM   3252 C  CA  . GLN   B 1 167 ? 58.76900 37.70700 -47.20900 1.000 17.00000 ? 211 GLN   B CA  1 
ATOM   3253 C  C   . GLN   B 1 167 ? 58.30500 39.05500 -46.68000 1.000 16.78000 ? 211 GLN   B C   1 
ATOM   3254 O  O   . GLN   B 1 167 ? 58.18300 40.00400 -47.46600 1.000 16.55000 ? 211 GLN   B O   1 
ATOM   3255 C  CB  . GLN   B 1 167 ? 57.89300 37.31900 -48.40600 1.000 16.81000 ? 211 GLN   B CB  1 
ATOM   3256 C  CG  . GLN   B 1 167 ? 58.00300 35.87500 -48.85500 1.000 17.01000 ? 211 GLN   B CG  1 
ATOM   3257 C  CD  . GLN   B 1 167 ? 57.08400 35.59000 -50.02200 1.000 17.11000 ? 211 GLN   B CD  1 
ATOM   3258 O  OE1 . GLN   B 1 167 ? 57.26900 36.12600 -51.10900 1.000 16.98000 ? 211 GLN   B OE1 1 
ATOM   3259 N  NE2 . GLN   B 1 167 ? 56.07000 34.76800 -49.79300 1.000 17.27000 ? 211 GLN   B NE2 1 
ATOM   3260 N  N   . VAL   B 1 168 ? 58.03400 39.16400 -45.38800 1.000 16.85000 ? 212 VAL   B N   1 
ATOM   3261 C  CA  . VAL   B 1 168 ? 57.53300 40.39200 -44.77600 1.000 16.86000 ? 212 VAL   B CA  1 
ATOM   3262 C  C   . VAL   B 1 168 ? 58.70400 41.08700 -44.09000 1.000 16.94000 ? 212 VAL   B C   1 
ATOM   3263 O  O   . VAL   B 1 168 ? 59.48800 40.41500 -43.40500 1.000 16.83000 ? 212 VAL   B O   1 
ATOM   3264 C  CB  . VAL   B 1 168 ? 56.40500 40.08900 -43.77100 1.000 16.99000 ? 212 VAL   B CB  1 
ATOM   3265 C  CG1 . VAL   B 1 168 ? 55.87600 41.35800 -43.15300 1.000 16.93000 ? 212 VAL   B CG1 1 
ATOM   3266 C  CG2 . VAL   B 1 168 ? 55.27800 39.32700 -44.45700 1.000 16.81000 ? 212 VAL   B CG2 1 
ATOM   3267 N  N   . PRO   B 1 169 ? 58.88000 42.39700 -44.26800 1.000 17.02000 ? 213 PRO   B N   1 
ATOM   3268 C  CA  . PRO   B 1 169 ? 59.95900 43.10000 -43.55700 1.000 17.14000 ? 213 PRO   B CA  1 
ATOM   3269 C  C   . PRO   B 1 169 ? 59.83700 42.90000 -42.05400 1.000 16.94000 ? 213 PRO   B C   1 
ATOM   3270 O  O   . PRO   B 1 169 ? 58.79900 43.18100 -41.45000 1.000 16.76000 ? 213 PRO   B O   1 
ATOM   3271 C  CB  . PRO   B 1 169 ? 59.75500 44.56200 -43.95900 1.000 17.59000 ? 213 PRO   B CB  1 
ATOM   3272 C  CG  . PRO   B 1 169 ? 59.02000 44.49800 -45.25900 1.000 17.56000 ? 213 PRO   B CG  1 
ATOM   3273 C  CD  . PRO   B 1 169 ? 58.15900 43.27500 -45.20100 1.000 17.20000 ? 213 PRO   B CD  1 
ATOM   3274 N  N   . THR   B 1 170 ? 60.90800 42.39400 -41.45100 1.000 16.85000 ? 214 THR   B N   1 
ATOM   3275 C  CA  . THR   B 1 170 ? 60.87300 41.92000 -40.07500 1.000 16.65000 ? 214 THR   B CA  1 
ATOM   3276 C  C   . THR   B 1 170 ? 61.90900 42.64700 -39.22200 1.000 16.83000 ? 214 THR   B C   1 
ATOM   3277 O  O   . THR   B 1 170 ? 63.10100 42.65600 -39.55000 1.000 16.99000 ? 214 THR   B O   1 
ATOM   3278 C  CB  . THR   B 1 170 ? 61.10300 40.40500 -40.02000 1.000 16.66000 ? 214 THR   B CB  1 
ATOM   3279 O  OG1 . THR   B 1 170 ? 60.09000 39.73300 -40.78400 1.000 16.54000 ? 214 THR   B OG1 1 
ATOM   3280 C  CG2 . THR   B 1 170 ? 61.03400 39.90300 -38.58500 1.000 16.51000 ? 214 THR   B CG2 1 
ATOM   3281 N  N   . PHE   B 1 171 ? 61.44800 43.22400 -38.11300 1.000 16.66000 ? 215 PHE   B N   1 
ATOM   3282 C  CA  . PHE   B 1 171 ? 62.29100 43.90700 -37.13400 1.000 16.75000 ? 215 PHE   B CA  1 
ATOM   3283 C  C   . PHE   B 1 171 ? 62.27100 43.10100 -35.83700 1.000 16.54000 ? 215 PHE   B C   1 
ATOM   3284 O  O   . PHE   B 1 171 ? 61.26000 43.08300 -35.13100 1.000 16.15000 ? 215 PHE   B O   1 
ATOM   3285 C  CB  . PHE   B 1 171 ? 61.79000 45.33200 -36.90500 1.000 17.07000 ? 215 PHE   B CB  1 
ATOM   3286 C  CG  . PHE   B 1 171 ? 62.65800 46.15900 -35.98900 1.000 17.47000 ? 215 PHE   B CG  1 
ATOM   3287 C  CD1 . PHE   B 1 171 ? 63.98300 45.83300 -35.76600 1.000 17.52000 ? 215 PHE   B CD1 1 
ATOM   3288 C  CD2 . PHE   B 1 171 ? 62.13000 47.27000 -35.35100 1.000 17.84000 ? 215 PHE   B CD2 1 
ATOM   3289 C  CE1 . PHE   B 1 171 ? 64.76300 46.59800 -34.92600 1.000 17.73000 ? 215 PHE   B CE1 1 
ATOM   3290 C  CE2 . PHE   B 1 171 ? 62.90300 48.03900 -34.51800 1.000 18.44000 ? 215 PHE   B CE2 1 
ATOM   3291 C  CZ  . PHE   B 1 171 ? 64.22000 47.70400 -34.30400 1.000 18.23000 ? 215 PHE   B CZ  1 
ATOM   3292 N  N   . ILE   B 1 172 ? 63.38700 42.44000 -35.52600 1.000 16.57000 ? 216 ILE   B N   1 
ATOM   3293 C  CA  . ILE   B 1 172 ? 63.52100 41.61800 -34.32700 1.000 16.51000 ? 216 ILE   B CA  1 
ATOM   3294 C  C   . ILE   B 1 172 ? 64.24000 42.42000 -33.25500 1.000 16.70000 ? 216 ILE   B C   1 
ATOM   3295 O  O   . ILE   B 1 172 ? 65.34400 42.92700 -33.48500 1.000 17.19000 ? 216 ILE   B O   1 
ATOM   3296 C  CB  . ILE   B 1 172 ? 64.28200 40.31500 -34.62300 1.000 16.53000 ? 216 ILE   B CB  1 
ATOM   3297 C  CG1 . ILE   B 1 172 ? 63.41500 39.35400 -35.43300 1.000 16.32000 ? 216 ILE   B CG1 1 
ATOM   3298 C  CG2 . ILE   B 1 172 ? 64.72000 39.64600 -33.32900 1.000 16.42000 ? 216 ILE   B CG2 1 
ATOM   3299 C  CD1 . ILE   B 1 172 ? 64.16200 38.13300 -35.90400 1.000 16.77000 ? 216 ILE   B CD1 1 
ATOM   3300 N  N   . ILE   B 1 173 ? 63.63400 42.51600 -32.07600 1.000 16.81000 ? 217 ILE   B N   1 
ATOM   3301 C  CA  . ILE   B 1 173 ? 64.22300 43.22500 -30.94700 1.000 17.07000 ? 217 ILE   B CA  1 
ATOM   3302 C  C   . ILE   B 1 173 ? 64.60300 42.20000 -29.88900 1.000 17.09000 ? 217 ILE   B C   1 
ATOM   3303 O  O   . ILE   B 1 173 ? 63.76800 41.39200 -29.46500 1.000 16.74000 ? 217 ILE   B O   1 
ATOM   3304 C  CB  . ILE   B 1 173 ? 63.27100 44.28900 -30.38500 1.000 17.09000 ? 217 ILE   B CB  1 
ATOM   3305 C  CG1 . ILE   B 1 173 ? 63.02900 45.36500 -31.44100 1.000 17.23000 ? 217 ILE   B CG1 1 
ATOM   3306 C  CG2 . ILE   B 1 173 ? 63.85400 44.89500 -29.12500 1.000 17.18000 ? 217 ILE   B CG2 1 
ATOM   3307 C  CD1 . ILE   B 1 173 ? 62.06900 46.45000 -31.02100 1.000 17.31000 ? 217 ILE   B CD1 1 
ATOM   3308 N  N   . GLY   B 1 174 ? 65.86700 42.22000 -29.48100 1.000 17.61000 ? 218 GLY   B N   1 
ATOM   3309 C  CA  . GLY   B 1 174 ? 66.35900 41.30300 -28.47700 1.000 17.54000 ? 218 GLY   B CA  1 
ATOM   3310 C  C   . GLY   B 1 174 ? 66.80900 42.02500 -27.22600 1.000 17.79000 ? 218 GLY   B C   1 
ATOM   3311 O  O   . GLY   B 1 174 ? 67.06800 43.23100 -27.25300 1.000 18.03000 ? 218 GLY   B O   1 
ATOM   3312 N  N   . ALA   B 1 175 ? 66.90000 41.29600 -26.11900 1.000 17.69000 ? 219 ALA   B N   1 
ATOM   3313 C  CA  . ALA   B 1 175 ? 67.32500 41.84300 -24.83800 1.000 18.23000 ? 219 ALA   B CA  1 
ATOM   3314 C  C   . ALA   B 1 175 ? 68.60100 41.14100 -24.40600 1.000 18.41000 ? 219 ALA   B C   1 
ATOM   3315 O  O   . ALA   B 1 175 ? 68.64800 39.90800 -24.37100 1.000 17.90000 ? 219 ALA   B O   1 
ATOM   3316 C  CB  . ALA   B 1 175 ? 66.23900 41.67300 -23.77800 1.000 18.46000 ? 219 ALA   B CB  1 
ATOM   3317 N  N   . GLU   B 1 176 ? 69.62600 41.93400 -24.07800 1.000 18.75000 ? 220 GLU   B N   1 
ATOM   3318 C  CA  . GLU   B 1 176 ? 70.94600 41.38600 -23.78600 1.000 19.15000 ? 220 GLU   B CA  1 
ATOM   3319 C  C   . GLU   B 1 176 ? 70.87800 40.30200 -22.71900 1.000 18.67000 ? 220 GLU   B C   1 
ATOM   3320 O  O   . GLU   B 1 176 ? 71.41500 39.20200 -22.89700 1.000 18.71000 ? 220 GLU   B O   1 
ATOM   3321 C  CB  . GLU   B 1 176 ? 71.89200 42.50900 -23.35200 1.000 19.79000 ? 220 GLU   B CB  1 
ATOM   3322 C  CG  . GLU   B 1 176 ? 73.30700 42.04500 -23.01400 1.000 20.92000 ? 220 GLU   B CG  1 
ATOM   3323 C  CD  . GLU   B 1 176 ? 74.22500 43.18300 -22.59700 1.000 22.39000 ? 220 GLU   B CD  1 
ATOM   3324 O  OE1 . GLU   B 1 176 ? 73.72300 44.23500 -22.15700 1.000 20.97000 ? 220 GLU   B OE1 1 
ATOM   3325 O  OE2 . GLU   B 1 176 ? 75.45600 43.02800 -22.71200 1.000 26.70000 ? 220 GLU   B OE2 1 
ATOM   3326 N  N   . LEU   B 1 177 ? 70.19300 40.58600 -21.61000 1.000 18.64000 ? 221 LEU   B N   1 
ATOM   3327 C  CA  . LEU   B 1 177 ? 70.16800 39.70400 -20.45200 1.000 18.42000 ? 221 LEU   B CA  1 
ATOM   3328 C  C   . LEU   B 1 177 ? 68.95300 38.78400 -20.44000 1.000 17.83000 ? 221 LEU   B C   1 
ATOM   3329 O  O   . LEU   B 1 177 ? 68.59400 38.25500 -19.38400 1.000 17.61000 ? 221 LEU   B O   1 
ATOM   3330 C  CB  . LEU   B 1 177 ? 70.23100 40.53000 -19.16900 1.000 18.95000 ? 221 LEU   B CB  1 
ATOM   3331 C  CG  . LEU   B 1 177 ? 71.43500 41.47100 -19.08700 1.000 19.66000 ? 221 LEU   B CG  1 
ATOM   3332 C  CD1 . LEU   B 1 177 ? 71.47200 42.18000 -17.74500 1.000 21.72000 ? 221 LEU   B CD1 1 
ATOM   3333 C  CD2 . LEU   B 1 177 ? 72.73700 40.72700 -19.33500 1.000 20.45000 ? 221 LEU   B CD2 1 
ATOM   3334 N  N   . ASP   B 1 178 ? 68.32700 38.57400 -21.59200 1.000 17.72000 ? 222 ASP   B N   1 
ATOM   3335 C  CA  . ASP   B 1 178 ? 67.20100 37.65700 -21.69800 1.000 17.45000 ? 222 ASP   B CA  1 
ATOM   3336 C  C   . ASP   B 1 178 ? 67.68900 36.22400 -21.52600 1.000 17.35000 ? 222 ASP   B C   1 
ATOM   3337 O  O   . ASP   B 1 178 ? 68.54700 35.76000 -22.28100 1.000 17.06000 ? 222 ASP   B O   1 
ATOM   3338 C  CB  . ASP   B 1 178 ? 66.51900 37.84000 -23.05200 1.000 17.22000 ? 222 ASP   B CB  1 
ATOM   3339 C  CG  . ASP   B 1 178 ? 65.14500 37.22200 -23.10400 1.000 16.91000 ? 222 ASP   B CG  1 
ATOM   3340 O  OD1 . ASP   B 1 178 ? 64.89900 36.24200 -22.37100 1.000 16.99000 ? 222 ASP   B OD1 1 
ATOM   3341 O  OD2 . ASP   B 1 178 ? 64.30000 37.71800 -23.87800 1.000 16.76000 ? 222 ASP   B OD2 1 
ATOM   3342 N  N   . THR   B 1 179 ? 67.15600 35.52200 -20.52500 1.000 17.23000 ? 223 THR   B N   1 
ATOM   3343 C  CA  . THR   B 1 179 ? 67.47900 34.11600 -20.32100 1.000 17.19000 ? 223 THR   B CA  1 
ATOM   3344 C  C   . THR   B 1 179 ? 66.27400 33.21000 -20.48700 1.000 17.96000 ? 223 THR   B C   1 
ATOM   3345 O  O   . THR   B 1 179 ? 66.42800 31.98400 -20.47200 1.000 17.28000 ? 223 THR   B O   1 
ATOM   3346 C  CB  . THR   B 1 179 ? 68.09800 33.89500 -18.93100 1.000 17.43000 ? 223 THR   B CB  1 
ATOM   3347 O  OG1 . THR   B 1 179 ? 67.23300 34.43400 -17.92400 1.000 17.07000 ? 223 THR   B OG1 1 
ATOM   3348 C  CG2 . THR   B 1 179 ? 69.44600 34.57300 -18.85000 1.000 17.27000 ? 223 THR   B CG2 1 
ATOM   3349 N  N   . ILE   B 1 180 ? 65.08500 33.77800 -20.63800 1.000 17.20000 ? 224 ILE   B N   1 
ATOM   3350 C  CA  . ILE   B 1 180 ? 63.91900 32.98200 -20.98100 1.000 17.60000 ? 224 ILE   B CA  1 
ATOM   3351 C  C   . ILE   B 1 180 ? 63.92400 32.65300 -22.46900 1.000 17.22000 ? 224 ILE   B C   1 
ATOM   3352 O  O   . ILE   B 1 180 ? 63.78500 31.49200 -22.86700 1.000 17.75000 ? 224 ILE   B O   1 
ATOM   3353 C  CB  . ILE   B 1 180 ? 62.64600 33.73200 -20.55900 1.000 17.31000 ? 224 ILE   B CB  1 
ATOM   3354 C  CG1 . ILE   B 1 180 ? 62.54200 33.77400 -19.03200 1.000 17.28000 ? 224 ILE   B CG1 1 
ATOM   3355 C  CG2 . ILE   B 1 180 ? 61.44200 33.08100 -21.15800 1.000 17.22000 ? 224 ILE   B CG2 1 
ATOM   3356 C  CD1 . ILE   B 1 180 ? 61.51600 34.75200 -18.51800 1.000 17.08000 ? 224 ILE   B CD1 1 
ATOM   3357 N  N   . ALA   B 1 181 ? 64.10600 33.67300 -23.31000 1.000 17.07000 ? 225 ALA   B N   1 
ATOM   3358 C  CA  . ALA   B 1 181 ? 64.33300 33.51500 -24.74600 1.000 16.98000 ? 225 ALA   B CA  1 
ATOM   3359 C  C   . ALA   B 1 181 ? 65.68200 34.14800 -25.06100 1.000 17.54000 ? 225 ALA   B C   1 
ATOM   3360 O  O   . ALA   B 1 181 ? 65.74500 35.30000 -25.51500 1.000 16.75000 ? 225 ALA   B O   1 
ATOM   3361 C  CB  . ALA   B 1 181 ? 63.21300 34.15200 -25.56700 1.000 17.00000 ? 225 ALA   B CB  1 
ATOM   3362 N  N   . PRO   B 1 182 ? 66.78200 33.43900 -24.80800 1.000 17.21000 ? 226 PRO   B N   1 
ATOM   3363 C  CA  . PRO   B 1 182 ? 68.10200 34.05400 -24.98100 1.000 17.09000 ? 226 PRO   B CA  1 
ATOM   3364 C  C   . PRO   B 1 182 ? 68.37600 34.38400 -26.44100 1.000 16.92000 ? 226 PRO   B C   1 
ATOM   3365 O  O   . PRO   B 1 182 ? 68.00300 33.63900 -27.35200 1.000 17.43000 ? 226 PRO   B O   1 
ATOM   3366 C  CB  . PRO   B 1 182 ? 69.06600 32.99100 -24.44100 1.000 17.01000 ? 226 PRO   B CB  1 
ATOM   3367 C  CG  . PRO   B 1 182 ? 68.30600 31.72000 -24.47200 1.000 17.32000 ? 226 PRO   B CG  1 
ATOM   3368 C  CD  . PRO   B 1 182 ? 66.86900 32.06600 -24.28700 1.000 17.37000 ? 226 PRO   B CD  1 
ATOM   3369 N  N   . VAL   B 1 183 ? 69.02900 35.52800 -26.65400 1.000 17.18000 ? 227 VAL   B N   1 
ATOM   3370 C  CA  . VAL   B 1 183 ? 69.21600 36.02300 -28.01200 1.000 17.25000 ? 227 VAL   B CA  1 
ATOM   3371 C  C   . VAL   B 1 183 ? 70.13100 35.10100 -28.80200 1.000 17.20000 ? 227 VAL   B C   1 
ATOM   3372 O  O   . VAL   B 1 183 ? 69.98200 34.96800 -30.02100 1.000 17.20000 ? 227 VAL   B O   1 
ATOM   3373 C  CB  . VAL   B 1 183 ? 69.73900 37.47100 -27.98700 1.000 17.83000 ? 227 VAL   B CB  1 
ATOM   3374 C  CG1 . VAL   B 1 183 ? 68.68300 38.39900 -27.41200 1.000 17.93000 ? 227 VAL   B CG1 1 
ATOM   3375 C  CG2 . VAL   B 1 183 ? 71.03600 37.56700 -27.19800 1.000 18.25000 ? 227 VAL   B CG2 1 
ATOM   3376 N  N   . SER   B 1 184 ? 71.06700 34.43000 -28.13200 1.000 17.09000 ? 228 SER   B N   1 
ATOM   3377 C  CA  . SER   B 1 184 ? 71.98200 33.53900 -28.83200 1.000 16.91000 ? 228 SER   B CA  1 
ATOM   3378 C  C   . SER   B 1 184 ? 71.28800 32.29800 -29.37000 1.000 16.74000 ? 228 SER   B C   1 
ATOM   3379 O  O   . SER   B 1 184 ? 71.81900 31.65600 -30.28000 1.000 16.26000 ? 228 SER   B O   1 
ATOM   3380 C  CB  . SER   B 1 184 ? 73.12000 33.12100 -27.90700 1.000 16.25000 ? 228 SER   B CB  1 
ATOM   3381 O  OG  . SER   B 1 184 ? 72.65000 32.20400 -26.93500 1.000 16.37000 ? 228 SER   B OG  1 
ATOM   3382 N  N   . THR   B 1 185 ? 70.12900 31.92800 -28.82500 1.000 16.95000 ? 229 THR   B N   1 
ATOM   3383 C  CA  . THR   B 1 185 ? 69.40300 30.76700 -29.31600 1.000 17.19000 ? 229 THR   B CA  1 
ATOM   3384 C  C   . THR   B 1 185 ? 68.02000 31.09500 -29.85500 1.000 17.45000 ? 229 THR   B C   1 
ATOM   3385 O  O   . THR   B 1 185 ? 67.38000 30.21100 -30.43400 1.000 17.28000 ? 229 THR   B O   1 
ATOM   3386 C  CB  . THR   B 1 185 ? 69.26300 29.69800 -28.21900 1.000 17.45000 ? 229 THR   B CB  1 
ATOM   3387 O  OG1 . THR   B 1 185 ? 68.33500 30.14900 -27.22900 1.000 17.32000 ? 229 THR   B OG1 1 
ATOM   3388 C  CG2 . THR   B 1 185 ? 70.60600 29.41700 -27.56800 1.000 17.39000 ? 229 THR   B CG2 1 
ATOM   3389 N  N   . HIS   B 1 186 ? 67.53900 32.32400 -29.68800 1.000 17.27000 ? 230 HIS   B N   1 
ATOM   3390 C  CA  . HIS   B 1 186 ? 66.24100 32.68700 -30.23200 1.000 17.34000 ? 230 HIS   B CA  1 
ATOM   3391 C  C   . HIS   B 1 186 ? 66.37000 33.87200 -31.18000 1.000 17.05000 ? 230 HIS   B C   1 
ATOM   3392 O  O   . HIS   B 1 186 ? 66.37700 33.67900 -32.39900 1.000 17.09000 ? 230 HIS   B O   1 
ATOM   3393 C  CB  . HIS   B 1 186 ? 65.24400 32.97100 -29.10300 1.000 17.30000 ? 230 HIS   B CB  1 
ATOM   3394 C  CG  . HIS   B 1 186 ? 64.80700 31.73800 -28.37400 1.000 18.00000 ? 230 HIS   B CG  1 
ATOM   3395 N  ND1 . HIS   B 1 186 ? 63.57700 31.15200 -28.56800 1.000 17.61000 ? 230 HIS   B ND1 1 
ATOM   3396 C  CD2 . HIS   B 1 186 ? 65.44900 30.96600 -27.46600 1.000 17.70000 ? 230 HIS   B CD2 1 
ATOM   3397 C  CE1 . HIS   B 1 186 ? 63.47600 30.07700 -27.80800 1.000 18.11000 ? 230 HIS   B CE1 1 
ATOM   3398 N  NE2 . HIS   B 1 186 ? 64.60000 29.94000 -27.12900 1.000 18.19000 ? 230 HIS   B NE2 1 
ATOM   3399 N  N   . ALA   B 1 187 ? 66.50900 35.08500 -30.63700 1.000 17.15000 ? 231 ALA   B N   1 
ATOM   3400 C  CA  . ALA   B 1 187 ? 66.40100 36.29500 -31.45300 1.000 17.09000 ? 231 ALA   B CA  1 
ATOM   3401 C  C   . ALA   B 1 187 ? 67.43800 36.33000 -32.57200 1.000 16.91000 ? 231 ALA   B C   1 
ATOM   3402 O  O   . ALA   B 1 187 ? 67.11900 36.67500 -33.71500 1.000 16.89000 ? 231 ALA   B O   1 
ATOM   3403 C  CB  . ALA   B 1 187 ? 66.53500 37.53500 -30.57200 1.000 16.86000 ? 231 ALA   B CB  1 
ATOM   3404 N  N   . LYS   B 1 188 ? 68.68400 35.99800 -32.26600 1.000 17.14000 ? 232 LYS   B N   1 
ATOM   3405 C  CA  . LYS   B 1 188 ? 69.72600 36.10700 -33.28300 1.000 17.17000 ? 232 LYS   B CA  1 
ATOM   3406 C  C   . LYS   B 1 188 ? 69.61900 35.01400 -34.34400 1.000 16.94000 ? 232 LYS   B C   1 
ATOM   3407 O  O   . LYS   B 1 188 ? 69.77200 35.31800 -35.53700 1.000 16.97000 ? 232 LYS   B O   1 
ATOM   3408 C  CB  . LYS   B 1 188 ? 71.11900 36.09000 -32.64300 1.000 18.21000 ? 232 LYS   B CB  1 
ATOM   3409 C  CG  . LYS   B 1 188 ? 71.45500 37.34600 -31.86900 1.000 19.03000 ? 232 LYS   B CG  1 
ATOM   3410 C  CD  . LYS   B 1 188 ? 72.86500 37.28100 -31.32500 1.000 20.61000 ? 232 LYS   B CD  1 
ATOM   3411 C  CE  . LYS   B 1 188 ? 73.28200 38.61100 -30.73400 1.000 21.34000 ? 232 LYS   B CE  1 
ATOM   3412 N  NZ  . LYS   B 1 188 ? 74.67000 38.59100 -30.19000 1.000 23.45000 ? 232 LYS   B NZ  1 
ATOM   3413 N  N   . PRO   B 1 189 ? 69.38500 33.74600 -33.98100 1.000 16.70000 ? 233 PRO   B N   1 
ATOM   3414 C  CA  . PRO   B 1 189 ? 69.14600 32.74700 -35.04000 1.000 16.53000 ? 233 PRO   B CA  1 
ATOM   3415 C  C   . PRO   B 1 189 ? 67.96600 33.08900 -35.92900 1.000 16.68000 ? 233 PRO   B C   1 
ATOM   3416 O  O   . PRO   B 1 189 ? 68.02600 32.84700 -37.14100 1.000 16.75000 ? 233 PRO   B O   1 
ATOM   3417 C  CB  . PRO   B 1 189 ? 68.91000 31.45600 -34.24500 1.000 16.68000 ? 233 PRO   B CB  1 
ATOM   3418 C  CG  . PRO   B 1 189 ? 69.68400 31.65500 -33.00200 1.000 16.99000 ? 233 PRO   B CG  1 
ATOM   3419 C  CD  . PRO   B 1 189 ? 69.53900 33.10200 -32.66400 1.000 16.93000 ? 233 PRO   B CD  1 
ATOM   3420 N  N   . PHE   B 1 190 ? 66.89100 33.64600 -35.36100 1.000 16.87000 ? 234 PHE   B N   1 
ATOM   3421 C  CA  . PHE   B 1 190 ? 65.74000 34.02500 -36.17700 1.000 16.95000 ? 234 PHE   B CA  1 
ATOM   3422 C  C   . PHE   B 1 190 ? 66.13600 35.05600 -37.22500 1.000 16.96000 ? 234 PHE   B C   1 
ATOM   3423 O  O   . PHE   B 1 190 ? 65.75500 34.94800 -38.39500 1.000 17.19000 ? 234 PHE   B O   1 
ATOM   3424 C  CB  . PHE   B 1 190 ? 64.61000 34.58400 -35.30500 1.000 17.16000 ? 234 PHE   B CB  1 
ATOM   3425 C  CG  . PHE   B 1 190 ? 64.09500 33.63200 -34.25900 1.000 17.25000 ? 234 PHE   B CG  1 
ATOM   3426 C  CD1 . PHE   B 1 190 ? 64.31300 32.27300 -34.35800 1.000 17.44000 ? 234 PHE   B CD1 1 
ATOM   3427 C  CD2 . PHE   B 1 190 ? 63.38400 34.11600 -33.17000 1.000 17.08000 ? 234 PHE   B CD2 1 
ATOM   3428 C  CE1 . PHE   B 1 190 ? 63.83900 31.41200 -33.38400 1.000 17.52000 ? 234 PHE   B CE1 1 
ATOM   3429 C  CE2 . PHE   B 1 190 ? 62.90800 33.26400 -32.20300 1.000 17.14000 ? 234 PHE   B CE2 1 
ATOM   3430 C  CZ  . PHE   B 1 190 ? 63.13600 31.91100 -32.30600 1.000 17.49000 ? 234 PHE   B CZ  1 
ATOM   3431 N  N   . TYR   B 1 191 ? 66.89400 36.07500 -36.81300 1.000 16.91000 ? 235 TYR   B N   1 
ATOM   3432 C  CA  . TYR   B 1 191 ? 67.24500 37.15300 -37.72900 1.000 17.04000 ? 235 TYR   B CA  1 
ATOM   3433 C  C   . TYR   B 1 191 ? 68.19200 36.67100 -38.81900 1.000 17.26000 ? 235 TYR   B C   1 
ATOM   3434 O  O   . TYR   B 1 191 ? 68.04000 37.04400 -39.98600 1.000 17.54000 ? 235 TYR   B O   1 
ATOM   3435 C  CB  . TYR   B 1 191 ? 67.86800 38.31700 -36.96100 1.000 17.19000 ? 235 TYR   B CB  1 
ATOM   3436 C  CG  . TYR   B 1 191 ? 68.45100 39.38100 -37.86400 1.000 17.58000 ? 235 TYR   B CG  1 
ATOM   3437 C  CD1 . TYR   B 1 191 ? 67.65800 40.39500 -38.37400 1.000 17.67000 ? 235 TYR   B CD1 1 
ATOM   3438 C  CD2 . TYR   B 1 191 ? 69.79500 39.36400 -38.21100 1.000 17.97000 ? 235 TYR   B CD2 1 
ATOM   3439 C  CE1 . TYR   B 1 191 ? 68.18800 41.36100 -39.20200 1.000 17.66000 ? 235 TYR   B CE1 1 
ATOM   3440 C  CE2 . TYR   B 1 191 ? 70.33000 40.32200 -39.03900 1.000 18.02000 ? 235 TYR   B CE2 1 
ATOM   3441 C  CZ  . TYR   B 1 191 ? 69.52500 41.31500 -39.53200 1.000 18.01000 ? 235 TYR   B CZ  1 
ATOM   3442 O  OH  . TYR   B 1 191 ? 70.06800 42.26800 -40.35300 1.000 17.80000 ? 235 TYR   B OH  1 
ATOM   3443 N  N   . GLU   B 1 192 ? 69.18400 35.85700 -38.45700 1.000 17.41000 ? 236 GLU   B N   1 
ATOM   3444 C  CA  . GLU   B 1 192 ? 70.17200 35.41400 -39.43000 1.000 17.65000 ? 236 GLU   B CA  1 
ATOM   3445 C  C   . GLU   B 1 192 ? 69.60400 34.41300 -40.42700 1.000 17.70000 ? 236 GLU   B C   1 
ATOM   3446 O  O   . GLU   B 1 192 ? 70.16900 34.25900 -41.51400 1.000 17.78000 ? 236 GLU   B O   1 
ATOM   3447 C  CB  . GLU   B 1 192 ? 71.38200 34.81100 -38.71400 1.000 17.73000 ? 236 GLU   B CB  1 
ATOM   3448 C  CG  . GLU   B 1 192 ? 72.19600 35.82100 -37.92400 1.000 18.87000 ? 236 GLU   B CG  1 
ATOM   3449 C  CD  . GLU   B 1 192 ? 72.89700 36.80900 -38.81800 1.000 19.80000 ? 236 GLU   B CD  1 
ATOM   3450 O  OE1 . GLU   B 1 192 ? 73.29500 36.40900 -39.92900 1.000 23.00000 ? 236 GLU   B OE1 1 
ATOM   3451 O  OE2 . GLU   B 1 192 ? 73.04700 37.98300 -38.42100 1.000 19.64000 ? 236 GLU   B OE2 1 
ATOM   3452 N  N   . SER   B 1 193 ? 68.51300 33.72600 -40.08400 1.000 17.51000 ? 237 SER   B N   1 
ATOM   3453 C  CA  . SER   B 1 193 ? 67.87300 32.80200 -41.00800 1.000 18.08000 ? 237 SER   B CA  1 
ATOM   3454 C  C   . SER   B 1 193 ? 66.84100 33.48700 -41.89100 1.000 17.84000 ? 237 SER   B C   1 
ATOM   3455 O  O   . SER   B 1 193 ? 66.40200 32.89000 -42.87800 1.000 17.93000 ? 237 SER   B O   1 
ATOM   3456 C  CB  . SER   B 1 193 ? 67.21500 31.64400 -40.24900 1.000 18.34000 ? 237 SER   B CB  1 
ATOM   3457 O  OG  . SER   B 1 193 ? 65.92300 31.99200 -39.79400 1.000 17.96000 ? 237 SER   B OG  1 
ATOM   3458 N  N   . LEU   B 1 194 ? 66.43900 34.70900 -41.55400 1.000 17.80000 ? 238 LEU   B N   1 
ATOM   3459 C  CA  . LEU   B 1 194 ? 65.64800 35.50500 -42.47100 1.000 17.80000 ? 238 LEU   B CA  1 
ATOM   3460 C  C   . LEU   B 1 194 ? 66.43200 35.69900 -43.76700 1.000 18.07000 ? 238 LEU   B C   1 
ATOM   3461 O  O   . LEU   B 1 194 ? 67.66200 35.78500 -43.74200 1.000 18.09000 ? 238 LEU   B O   1 
ATOM   3462 C  CB  . LEU   B 1 194 ? 65.30700 36.85800 -41.85500 1.000 17.96000 ? 238 LEU   B CB  1 
ATOM   3463 C  CG  . LEU   B 1 194 ? 64.30600 36.90900 -40.69800 1.000 17.52000 ? 238 LEU   B CG  1 
ATOM   3464 C  CD1 . LEU   B 1 194 ? 64.15000 38.33900 -40.20000 1.000 17.33000 ? 238 LEU   B CD1 1 
ATOM   3465 C  CD2 . LEU   B 1 194 ? 62.96200 36.33900 -41.11500 1.000 17.76000 ? 238 LEU   B CD2 1 
ATOM   3466 N  N   . PRO   B 1 195 ? 65.75000 35.75400 -44.91100 1.000 18.05000 ? 239 PRO   B N   1 
ATOM   3467 C  CA  . PRO   B 1 195 ? 66.46500 35.90800 -46.18500 1.000 18.52000 ? 239 PRO   B CA  1 
ATOM   3468 C  C   . PRO   B 1 195 ? 67.30300 37.17700 -46.19300 1.000 19.40000 ? 239 PRO   B C   1 
ATOM   3469 O  O   . PRO   B 1 195 ? 66.85900 38.23900 -45.75400 1.000 19.01000 ? 239 PRO   B O   1 
ATOM   3470 C  CB  . PRO   B 1 195 ? 65.33400 35.97200 -47.22100 1.000 18.24000 ? 239 PRO   B CB  1 
ATOM   3471 C  CG  . PRO   B 1 195 ? 64.17300 35.30500 -46.56000 1.000 18.05000 ? 239 PRO   B CG  1 
ATOM   3472 C  CD  . PRO   B 1 195 ? 64.29400 35.64200 -45.10400 1.000 17.93000 ? 239 PRO   B CD  1 
ATOM   3473 N  N   . SER   B 1 196 ? 68.53200 37.05200 -46.69000 1.000 20.02000 ? 240 SER   B N   1 
ATOM   3474 C  CA  . SER   B 1 196 ? 69.42800 38.20000 -46.74200 1.000 20.91000 ? 240 SER   B CA  1 
ATOM   3475 C  C   . SER   B 1 196 ? 68.92300 39.28300 -47.68400 1.000 20.54000 ? 240 SER   B C   1 
ATOM   3476 O  O   . SER   B 1 196 ? 69.39300 40.42500 -47.61200 1.000 20.76000 ? 240 SER   B O   1 
ATOM   3477 C  CB  . SER   B 1 196 ? 70.82600 37.74600 -47.15600 1.000 21.70000 ? 240 SER   B CB  1 
ATOM   3478 O  OG  . SER   B 1 196 ? 70.76100 36.85500 -48.25500 1.000 24.79000 ? 240 SER   B OG  1 
ATOM   3479 N  N   . SER   B 1 197 ? 67.97600 38.95500 -48.56000 1.000 20.20000 ? 241 SER   B N   1 
ATOM   3480 C  CA  . SER   B 1 197 ? 67.37700 39.91400 -49.47400 1.000 20.00000 ? 241 SER   B CA  1 
ATOM   3481 C  C   . SER   B 1 197 ? 66.18500 40.64100 -48.86700 1.000 18.99000 ? 241 SER   B C   1 
ATOM   3482 O  O   . SER   B 1 197 ? 65.62300 41.53000 -49.51400 1.000 19.38000 ? 241 SER   B O   1 
ATOM   3483 C  CB  . SER   B 1 197 ? 66.94700 39.20500 -50.75900 1.000 19.96000 ? 241 SER   B CB  1 
ATOM   3484 O  OG  . SER   B 1 197 ? 66.06600 38.13500 -50.47000 1.000 19.57000 ? 241 SER   B OG  1 
ATOM   3485 N  N   . LEU   B 1 198 ? 65.79000 40.28600 -47.65000 1.000 18.78000 ? 242 LEU   B N   1 
ATOM   3486 C  CA  . LEU   B 1 198 ? 64.62200 40.85500 -46.99500 1.000 18.39000 ? 242 LEU   B CA  1 
ATOM   3487 C  C   . LEU   B 1 198 ? 64.99500 42.15800 -46.28900 1.000 18.48000 ? 242 LEU   B C   1 
ATOM   3488 O  O   . LEU   B 1 198 ? 66.08000 42.26300 -45.71400 1.000 18.48000 ? 242 LEU   B O   1 
ATOM   3489 C  CB  . LEU   B 1 198 ? 64.04400 39.85700 -45.98900 1.000 18.13000 ? 242 LEU   B CB  1 
ATOM   3490 C  CG  . LEU   B 1 198 ? 62.67500 40.12900 -45.36600 1.000 17.65000 ? 242 LEU   B CG  1 
ATOM   3491 C  CD1 . LEU   B 1 198 ? 61.58700 40.01700 -46.40900 1.000 17.36000 ? 242 LEU   B CD1 1 
ATOM   3492 C  CD2 . LEU   B 1 198 ? 62.40500 39.16900 -44.21600 1.000 17.63000 ? 242 LEU   B CD2 1 
ATOM   3493 N  N   . PRO   B 1 199 ? 64.13700 43.17600 -46.34500 1.000 18.11000 ? 243 PRO   B N   1 
ATOM   3494 C  CA  . PRO   B 1 199 ? 64.34100 44.34300 -45.48200 1.000 18.20000 ? 243 PRO   B CA  1 
ATOM   3495 C  C   . PRO   B 1 199 ? 64.17400 43.92200 -44.03400 1.000 17.95000 ? 243 PRO   B C   1 
ATOM   3496 O  O   . PRO   B 1 199 ? 63.06200 43.59000 -43.61300 1.000 17.76000 ? 243 PRO   B O   1 
ATOM   3497 C  CB  . PRO   B 1 199 ? 63.24200 45.32000 -45.92200 1.000 18.14000 ? 243 PRO   B CB  1 
ATOM   3498 C  CG  . PRO   B 1 199 ? 62.76000 44.81500 -47.23600 1.000 17.34000 ? 243 PRO   B CG  1 
ATOM   3499 C  CD  . PRO   B 1 199 ? 62.95500 43.33100 -47.20600 1.000 17.52000 ? 243 PRO   B CD  1 
ATOM   3500 N  N   . LYS   B 1 200 ? 65.26600 43.89800 -43.27400 1.000 18.12000 ? 244 LYS   B N   1 
ATOM   3501 C  CA  . LYS   B 1 200 ? 65.22800 43.34100 -41.93300 1.000 17.92000 ? 244 LYS   B CA  1 
ATOM   3502 C  C   . LYS   B 1 200 ? 66.22300 44.08400 -41.05500 1.000 17.88000 ? 244 LYS   B C   1 
ATOM   3503 O  O   . LYS   B 1 200 ? 67.13600 44.75500 -41.54400 1.000 17.85000 ? 244 LYS   B O   1 
ATOM   3504 C  CB  . LYS   B 1 200 ? 65.51900 41.83200 -41.94200 1.000 18.27000 ? 244 LYS   B CB  1 
ATOM   3505 C  CG  . LYS   B 1 200 ? 66.90300 41.45400 -42.42000 1.000 18.40000 ? 244 LYS   B CG  1 
ATOM   3506 C  CD  . LYS   B 1 200 ? 67.13000 39.96400 -42.33300 1.000 18.46000 ? 244 LYS   B CD  1 
ATOM   3507 C  CE  . LYS   B 1 200 ? 68.57800 39.62200 -42.61000 1.000 18.68000 ? 244 LYS   B CE  1 
ATOM   3508 N  NZ  . LYS   B 1 200 ? 68.86700 38.17800 -42.45300 1.000 18.22000 ? 244 LYS   B NZ  1 
ATOM   3509 N  N   . ALA   B 1 201 ? 66.02300 43.96200 -39.74400 1.000 17.51000 ? 245 ALA   B N   1 
ATOM   3510 C  CA  . ALA   B 1 201 ? 66.86400 44.64100 -38.77100 1.000 17.67000 ? 245 ALA   B CA  1 
ATOM   3511 C  C   . ALA   B 1 201 ? 66.78800 43.89500 -37.44900 1.000 17.47000 ? 245 ALA   B C   1 
ATOM   3512 O  O   . ALA   B 1 201 ? 65.78500 43.24500 -37.14600 1.000 17.13000 ? 245 ALA   B O   1 
ATOM   3513 C  CB  . ALA   B 1 201 ? 66.44800 46.10200 -38.58500 1.000 17.64000 ? 245 ALA   B CB  1 
ATOM   3514 N  N   . TYR   B 1 202 ? 67.86900 43.98600 -36.67800 1.000 17.49000 ? 246 TYR   B N   1 
ATOM   3515 C  CA  . TYR   B 1 202 ? 67.96000 43.39300 -35.34900 1.000 17.47000 ? 246 TYR   B CA  1 
ATOM   3516 C  C   . TYR   B 1 202 ? 68.52900 44.42900 -34.39600 1.000 17.71000 ? 246 TYR   B C   1 
ATOM   3517 O  O   . TYR   B 1 202 ? 69.57200 45.02400 -34.67400 1.000 18.16000 ? 246 TYR   B O   1 
ATOM   3518 C  CB  . TYR   B 1 202 ? 68.83800 42.13500 -35.34300 1.000 17.51000 ? 246 TYR   B CB  1 
ATOM   3519 C  CG  . TYR   B 1 202 ? 69.14600 41.61700 -33.95400 1.000 17.46000 ? 246 TYR   B CG  1 
ATOM   3520 C  CD1 . TYR   B 1 202 ? 68.21000 40.87400 -33.24500 1.000 17.20000 ? 246 TYR   B CD1 1 
ATOM   3521 C  CD2 . TYR   B 1 202 ? 70.37100 41.86900 -33.35200 1.000 18.04000 ? 246 TYR   B CD2 1 
ATOM   3522 C  CE1 . TYR   B 1 202 ? 68.48200 40.40200 -31.97300 1.000 17.34000 ? 246 TYR   B CE1 1 
ATOM   3523 C  CE2 . TYR   B 1 202 ? 70.65100 41.40100 -32.07900 1.000 18.35000 ? 246 TYR   B CE2 1 
ATOM   3524 C  CZ  . TYR   B 1 202 ? 69.70300 40.66700 -31.39600 1.000 17.87000 ? 246 TYR   B CZ  1 
ATOM   3525 O  OH  . TYR   B 1 202 ? 69.97300 40.19500 -30.13000 1.000 18.10000 ? 246 TYR   B OH  1 
ATOM   3526 N  N   . MET   B 1 203 ? 67.84000 44.64600 -33.28000 1.000 17.82000 ? 247 MET   B N   1 
ATOM   3527 C  CA  . MET   B 1 203 ? 68.26900 45.60500 -32.27100 1.000 18.14000 ? 247 MET   B CA  1 
ATOM   3528 C  C   . MET   B 1 203 ? 68.30800 44.90800 -30.92300 1.000 18.14000 ? 247 MET   B C   1 
ATOM   3529 O  O   . MET   B 1 203 ? 67.29000 44.37300 -30.47300 1.000 17.81000 ? 247 MET   B O   1 
ATOM   3530 C  CB  . MET   B 1 203 ? 67.33300 46.80900 -32.22100 1.000 18.26000 ? 247 MET   B CB  1 
ATOM   3531 C  CG  . MET   B 1 203 ? 67.76200 47.87200 -31.23300 1.000 18.63000 ? 247 MET   B CG  1 
ATOM   3532 S  SD  . MET   B 1 203 ? 66.63000 49.26100 -31.23300 1.000 18.31000 ? 247 MET   B SD  1 
ATOM   3533 C  CE  . MET   B 1 203 ? 65.15100 48.50000 -30.56900 1.000 18.42000 ? 247 MET   B CE  1 
ATOM   3534 N  N   . GLU   B 1 204 ? 69.47700 44.91000 -30.28600 1.000 18.49000 ? 248 GLU   B N   1 
ATOM   3535 C  CA  . GLU   B 1 204 ? 69.67100 44.31100 -28.97000 1.000 18.62000 ? 248 GLU   B CA  1 
ATOM   3536 C  C   . GLU   B 1 204 ? 69.79900 45.42600 -27.94100 1.000 19.20000 ? 248 GLU   B C   1 
ATOM   3537 O  O   . GLU   B 1 204 ? 70.65400 46.30600 -28.07400 1.000 19.52000 ? 248 GLU   B O   1 
ATOM   3538 C  CB  . GLU   B 1 204 ? 70.90900 43.41400 -28.95400 1.000 18.88000 ? 248 GLU   B CB  1 
ATOM   3539 C  CG  . GLU   B 1 204 ? 71.14100 42.65900 -27.65400 1.000 18.96000 ? 248 GLU   B CG  1 
ATOM   3540 C  CD  . GLU   B 1 204 ? 72.18000 41.56700 -27.80800 1.000 19.13000 ? 248 GLU   B CD  1 
ATOM   3541 O  OE1 . GLU   B 1 204 ? 72.22600 40.95200 -28.89100 1.000 19.35000 ? 248 GLU   B OE1 1 
ATOM   3542 O  OE2 . GLU   B 1 204 ? 72.95700 41.32100 -26.86200 1.000 19.27000 ? 248 GLU   B OE2 1 
ATOM   3543 N  N   . LEU   B 1 205 ? 68.95400 45.38400 -26.91800 1.000 18.95000 ? 249 LEU   B N   1 
ATOM   3544 C  CA  . LEU   B 1 205 ? 68.94300 46.40600 -25.88400 1.000 19.34000 ? 249 LEU   B CA  1 
ATOM   3545 C  C   . LEU   B 1 205 ? 69.89500 46.01700 -24.75700 1.000 19.60000 ? 249 LEU   B C   1 
ATOM   3546 O  O   . LEU   B 1 205 ? 69.80700 44.90800 -24.21900 1.000 19.24000 ? 249 LEU   B O   1 
ATOM   3547 C  CB  . LEU   B 1 205 ? 67.52300 46.59700 -25.35200 1.000 19.39000 ? 249 LEU   B CB  1 
ATOM   3548 C  CG  . LEU   B 1 205 ? 66.47500 47.00700 -26.38800 1.000 18.70000 ? 249 LEU   B CG  1 
ATOM   3549 C  CD1 . LEU   B 1 205 ? 65.09400 46.97100 -25.77100 1.000 18.49000 ? 249 LEU   B CD1 1 
ATOM   3550 C  CD2 . LEU   B 1 205 ? 66.77900 48.39100 -26.94800 1.000 19.48000 ? 249 LEU   B CD2 1 
ATOM   3551 N  N   . CYS   B 1 206 ? 70.80400 46.92800 -24.41000 1.000 19.93000 ? 250 CYS   B N   1 
ATOM   3552 C  CA  . CYS   B 1 206 ? 71.77400 46.66700 -23.35300 1.000 20.09000 ? 250 CYS   B CA  1 
ATOM   3553 C  C   . CYS   B 1 206 ? 71.07400 46.41000 -22.02600 1.000 19.85000 ? 250 CYS   B C   1 
ATOM   3554 O  O   . CYS   B 1 206 ? 70.15600 47.14300 -21.64400 1.000 19.36000 ? 250 CYS   B O   1 
ATOM   3555 C  CB  . CYS   B 1 206 ? 72.72700 47.85000 -23.19100 1.000 20.41000 ? 250 CYS   B CB  1 
ATOM   3556 S  SG  . CYS   B 1 206 ? 73.73900 48.28000 -24.60200 1.000 20.11000 ? 250 CYS   B SG  1 
ATOM   3557 N  N   . GLY   B 1 207 ? 71.51900 45.37100 -21.32100 1.000 19.80000 ? 251 GLY   B N   1 
ATOM   3558 C  CA  . GLY   B 1 207 ? 71.05800 45.08100 -19.97600 1.000 19.49000 ? 251 GLY   B CA  1 
ATOM   3559 C  C   . GLY   B 1 207 ? 69.57500 44.80600 -19.81900 1.000 19.38000 ? 251 GLY   B C   1 
ATOM   3560 O  O   . GLY   B 1 207 ? 69.10000 44.59800 -18.69900 1.000 18.70000 ? 251 GLY   B O   1 
ATOM   3561 N  N   . ALA   B 1 208 ? 68.82700 44.79900 -20.91700 1.000 19.04000 ? 252 ALA   B N   1 
ATOM   3562 C  CA  . ALA   B 1 208 ? 67.39500 44.58500 -20.81800 1.000 19.00000 ? 252 ALA   B CA  1 
ATOM   3563 C  C   . ALA   B 1 208 ? 67.09100 43.12500 -20.50100 1.000 18.92000 ? 252 ALA   B C   1 
ATOM   3564 O  O   . ALA   B 1 208 ? 67.89700 42.22300 -20.74200 1.000 18.66000 ? 252 ALA   B O   1 
ATOM   3565 C  CB  . ALA   B 1 208 ? 66.69500 45.00000 -22.11200 1.000 19.12000 ? 252 ALA   B CB  1 
ATOM   3566 N  N   . THR   B 1 209 ? 65.91000 42.90500 -19.94100 1.000 18.88000 ? 253 THR   B N   1 
ATOM   3567 C  CA  . THR   B 1 209 ? 65.43300 41.57600 -19.61500 1.000 18.53000 ? 253 THR   B CA  1 
ATOM   3568 C  C   . THR   B 1 209 ? 64.39700 41.13900 -20.64400 1.000 18.18000 ? 253 THR   B C   1 
ATOM   3569 O  O   . THR   B 1 209 ? 64.01200 41.89100 -21.54100 1.000 18.30000 ? 253 THR   B O   1 
ATOM   3570 C  CB  . THR   B 1 209 ? 64.83100 41.55600 -18.21200 1.000 18.71000 ? 253 THR   B CB  1 
ATOM   3571 O  OG1 . THR   B 1 209 ? 63.58700 42.25600 -18.23700 1.000 18.87000 ? 253 THR   B OG1 1 
ATOM   3572 C  CG2 . THR   B 1 209 ? 65.76500 42.23500 -17.21800 1.000 18.36000 ? 253 THR   B CG2 1 
ATOM   3573 N  N   . HIS   B 1 210 ? 63.92100 39.90500 -20.48700 1.000 17.89000 ? 254 HIS   B N   1 
ATOM   3574 C  CA  . HIS   B 1 210 ? 62.87100 39.38000 -21.34900 1.000 17.49000 ? 254 HIS   B CA  1 
ATOM   3575 C  C   . HIS   B 1 210 ? 61.60000 40.21600 -21.29000 1.000 17.68000 ? 254 HIS   B C   1 
ATOM   3576 O  O   . HIS   B 1 210 ? 60.77000 40.12400 -22.19800 1.000 17.33000 ? 254 HIS   B O   1 
ATOM   3577 C  CB  . HIS   B 1 210 ? 62.57000 37.93700 -20.95000 1.000 17.16000 ? 254 HIS   B CB  1 
ATOM   3578 C  CG  . HIS   B 1 210 ? 61.70000 37.19900 -21.91900 1.000 16.63000 ? 254 HIS   B CG  1 
ATOM   3579 N  ND1 . HIS   B 1 210 ? 62.11500 36.86300 -23.18900 1.000 16.38000 ? 254 HIS   B ND1 1 
ATOM   3580 C  CD2 . HIS   B 1 210 ? 60.44500 36.70800 -21.79200 1.000 16.58000 ? 254 HIS   B CD2 1 
ATOM   3581 C  CE1 . HIS   B 1 210 ? 61.15100 36.20400 -23.80500 1.000 16.20000 ? 254 HIS   B CE1 1 
ATOM   3582 N  NE2 . HIS   B 1 210 ? 60.12700 36.09600 -22.97900 1.000 16.09000 ? 254 HIS   B NE2 1 
ATOM   3583 N  N   . PHE   B 1 211 ? 61.43200 41.03100 -20.25100 1.000 18.24000 ? 255 PHE   B N   1 
ATOM   3584 C  CA  . PHE   B 1 211 ? 60.19600 41.75700 -20.00900 1.000 18.59000 ? 255 PHE   B CA  1 
ATOM   3585 C  C   . PHE   B 1 211 ? 60.33400 43.24700 -20.28400 1.000 19.09000 ? 255 PHE   B C   1 
ATOM   3586 O  O   . PHE   B 1 211 ? 59.39400 44.00700 -20.02900 1.000 18.71000 ? 255 PHE   B O   1 
ATOM   3587 C  CB  . PHE   B 1 211 ? 59.72800 41.51200 -18.57100 1.000 19.06000 ? 255 PHE   B CB  1 
ATOM   3588 C  CG  . PHE   B 1 211 ? 59.53500 40.05800 -18.24100 1.000 18.76000 ? 255 PHE   B CG  1 
ATOM   3589 C  CD1 . PHE   B 1 211 ? 58.36900 39.40000 -18.59200 1.000 18.74000 ? 255 PHE   B CD1 1 
ATOM   3590 C  CD2 . PHE   B 1 211 ? 60.52600 39.34500 -17.59200 1.000 18.51000 ? 255 PHE   B CD2 1 
ATOM   3591 C  CE1 . PHE   B 1 211 ? 58.19500 38.06400 -18.29800 1.000 18.64000 ? 255 PHE   B CE1 1 
ATOM   3592 C  CE2 . PHE   B 1 211 ? 60.35900 38.01200 -17.29600 1.000 18.28000 ? 255 PHE   B CE2 1 
ATOM   3593 C  CZ  . PHE   B 1 211 ? 59.19200 37.36900 -17.65100 1.000 18.60000 ? 255 PHE   B CZ  1 
ATOM   3594 N  N   . ALA   B 1 212 ? 61.48700 43.68200 -20.78500 1.000 18.77000 ? 256 ALA   B N   1 
ATOM   3595 C  CA  . ALA   B 1 212 ? 61.62000 45.06800 -21.22500 1.000 18.90000 ? 256 ALA   B CA  1 
ATOM   3596 C  C   . ALA   B 1 212 ? 60.56200 45.50400 -22.24000 1.000 18.63000 ? 256 ALA   B C   1 
ATOM   3597 O  O   . ALA   B 1 212 ? 60.14500 46.67300 -22.17700 1.000 18.83000 ? 256 ALA   B O   1 
ATOM   3598 C  CB  . ALA   B 1 212 ? 63.03000 45.30000 -21.77700 1.000 19.08000 ? 256 ALA   B CB  1 
ATOM   3599 N  N   . PRO   B 1 213 ? 60.10200 44.67100 -23.18300 1.000 18.24000 ? 257 PRO   B N   1 
ATOM   3600 C  CA  . PRO   B 1 213 ? 59.00700 45.11100 -24.06800 1.000 18.28000 ? 257 PRO   B CA  1 
ATOM   3601 C  C   . PRO   B 1 213 ? 57.71900 45.42700 -23.34100 1.000 18.34000 ? 257 PRO   B C   1 
ATOM   3602 O  O   . PRO   B 1 213 ? 56.83900 46.06500 -23.93000 1.000 18.35000 ? 257 PRO   B O   1 
ATOM   3603 C  CB  . PRO   B 1 213 ? 58.82600 43.91900 -25.01500 1.000 17.88000 ? 257 PRO   B CB  1 
ATOM   3604 C  CG  . PRO   B 1 213 ? 60.16000 43.30200 -25.06100 1.000 17.62000 ? 257 PRO   B CG  1 
ATOM   3605 C  CD  . PRO   B 1 213 ? 60.73500 43.43800 -23.68800 1.000 18.09000 ? 257 PRO   B CD  1 
ATOM   3606 N  N   . ASN   B 1 214 ? 57.57500 45.00800 -22.08700 1.000 18.46000 ? 258 ASN   B N   1 
ATOM   3607 C  CA  . ASN   B 1 214 ? 56.32800 45.21100 -21.36600 1.000 18.64000 ? 258 ASN   B CA  1 
ATOM   3608 C  C   . ASN   B 1 214 ? 56.25100 46.54500 -20.63400 1.000 18.81000 ? 258 ASN   B C   1 
ATOM   3609 O  O   . ASN   B 1 214 ? 55.18800 46.86900 -20.10100 1.000 18.44000 ? 258 ASN   B O   1 
ATOM   3610 C  CB  . ASN   B 1 214 ? 56.10600 44.07400 -20.36500 1.000 18.83000 ? 258 ASN   B CB  1 
ATOM   3611 C  CG  . ASN   B 1 214 ? 56.02900 42.71800 -21.02900 1.000 18.21000 ? 258 ASN   B CG  1 
ATOM   3612 O  OD1 . ASN   B 1 214 ? 56.79800 41.81900 -20.71100 1.000 18.07000 ? 258 ASN   B OD1 1 
ATOM   3613 N  ND2 . ASN   B 1 214 ? 55.08500 42.55900 -21.94400 1.000 17.66000 ? 258 ASN   B ND2 1 
ATOM   3614 N  N   . ILE   B 1 215 ? 57.32300 47.32900 -20.59800 1.000 19.13000 ? 259 ILE   B N   1 
ATOM   3615 C  CA  . ILE   B 1 215 ? 57.26900 48.63900 -19.94800 1.000 19.14000 ? 259 ILE   B CA  1 
ATOM   3616 C  C   . ILE   B 1 215 ? 57.65900 49.73400 -20.93100 1.000 19.36000 ? 259 ILE   B C   1 
ATOM   3617 O  O   . ILE   B 1 215 ? 58.50600 49.50200 -21.80800 1.000 19.34000 ? 259 ILE   B O   1 
ATOM   3618 C  CB  . ILE   B 1 215 ? 58.17200 48.68900 -18.71000 1.000 19.15000 ? 259 ILE   B CB  1 
ATOM   3619 C  CG1 . ILE   B 1 215 ? 59.57100 48.20200 -19.06400 1.000 20.07000 ? 259 ILE   B CG1 1 
ATOM   3620 C  CG2 . ILE   B 1 215 ? 57.57200 47.85900 -17.59300 1.000 20.55000 ? 259 ILE   B CG2 1 
ATOM   3621 C  CD1 . ILE   B 1 215 ? 60.62300 48.58400 -18.04600 1.000 26.66000 ? 259 ILE   B CD1 1 
ATOM   3622 N  N   . PRO   B 1 216 ? 57.07500 50.94400 -20.81000 1.000 19.41000 ? 260 PRO   B N   1 
ATOM   3623 C  CA  . PRO   B 1 216 ? 57.37900 52.03200 -21.75000 1.000 19.67000 ? 260 PRO   B CA  1 
ATOM   3624 C  C   . PRO   B 1 216 ? 58.86300 52.26800 -21.99200 1.000 19.76000 ? 260 PRO   B C   1 
ATOM   3625 O  O   . PRO   B 1 216 ? 59.59800 52.70200 -21.10000 1.000 19.82000 ? 260 PRO   B O   1 
ATOM   3626 C  CB  . PRO   B 1 216 ? 56.72100 53.24300 -21.08100 1.000 19.93000 ? 260 PRO   B CB  1 
ATOM   3627 C  CG  . PRO   B 1 216 ? 55.53300 52.66100 -20.39000 1.000 19.67000 ? 260 PRO   B CG  1 
ATOM   3628 C  CD  . PRO   B 1 216 ? 55.99600 51.31800 -19.87500 1.000 19.30000 ? 260 PRO   B CD  1 
ATOM   3629 N  N   . ASN   B 1 217 ? 59.30200 51.98700 -23.21600 1.000 20.19000 ? 261 ASN   B N   1 
ATOM   3630 C  CA  . ASN   B 1 217 ? 60.69500 52.12600 -23.61700 1.000 20.98000 ? 261 ASN   B CA  1 
ATOM   3631 C  C   . ASN   B 1 217 ? 60.73900 53.03100 -24.83900 1.000 21.28000 ? 261 ASN   B C   1 
ATOM   3632 O  O   . ASN   B 1 217 ? 60.08900 52.74500 -25.84800 1.000 21.18000 ? 261 ASN   B O   1 
ATOM   3633 C  CB  . ASN   B 1 217 ? 61.31400 50.75600 -23.91800 1.000 20.84000 ? 261 ASN   B CB  1 
ATOM   3634 C  CG  . ASN   B 1 217 ? 62.81200 50.81800 -24.10800 1.000 21.01000 ? 261 ASN   B CG  1 
ATOM   3635 O  OD1 . ASN   B 1 217 ? 63.32900 51.72000 -24.75800 1.000 20.59000 ? 261 ASN   B OD1 1 
ATOM   3636 N  ND2 . ASN   B 1 217 ? 63.52200 49.85800 -23.53300 1.000 20.75000 ? 261 ASN   B ND2 1 
ATOM   3637 N  N   . THR   B 1 218 ? 61.48900 54.13000 -24.73900 1.000 21.65000 ? 262 THR   B N   1 
ATOM   3638 C  CA  . THR   B 1 218 ? 61.59000 55.06000 -25.85800 1.000 22.20000 ? 262 THR   B CA  1 
ATOM   3639 C  C   . THR   B 1 218 ? 62.42000 54.47200 -26.99200 1.000 21.44000 ? 262 THR   B C   1 
ATOM   3640 O  O   . THR   B 1 218 ? 62.12100 54.70000 -28.17000 1.000 21.28000 ? 262 THR   B O   1 
ATOM   3641 C  CB  . THR   B 1 218 ? 62.18700 56.38500 -25.38400 1.000 23.94000 ? 262 THR   B CB  1 
ATOM   3642 O  OG1 . THR   B 1 218 ? 61.30700 56.98800 -24.43200 1.000 26.39000 ? 262 THR   B OG1 1 
ATOM   3643 C  CG2 . THR   B 1 218 ? 62.38300 57.33700 -26.55200 1.000 23.91000 ? 262 THR   B CG2 1 
ATOM   3644 N  N   . THR   B 1 219 ? 63.46500 53.71100 -26.65900 1.000 21.16000 ? 263 THR   B N   1 
ATOM   3645 C  CA  . THR   B 1 219 ? 64.26400 53.06600 -27.69400 1.000 21.05000 ? 263 THR   B CA  1 
ATOM   3646 C  C   . THR   B 1 219 ? 63.43200 52.05700 -28.46900 1.000 20.59000 ? 263 THR   B C   1 
ATOM   3647 O  O   . THR   B 1 219 ? 63.57000 51.93400 -29.69100 1.000 20.31000 ? 263 THR   B O   1 
ATOM   3648 C  CB  . THR   B 1 219 ? 65.48600 52.39100 -27.07300 1.000 20.81000 ? 263 THR   B CB  1 
ATOM   3649 O  OG1 . THR   B 1 219 ? 66.19100 53.33600 -26.26200 1.000 20.29000 ? 263 THR   B OG1 1 
ATOM   3650 C  CG2 . THR   B 1 219 ? 66.42100 51.87400 -28.15100 1.000 20.89000 ? 263 THR   B CG2 1 
ATOM   3651 N  N   . ILE   B 1 220 ? 62.55400 51.33300 -27.77900 1.000 20.43000 ? 264 ILE   B N   1 
ATOM   3652 C  CA  . ILE   B 1 220 ? 61.64600 50.42400 -28.46700 1.000 20.35000 ? 264 ILE   B CA  1 
ATOM   3653 C  C   . ILE   B 1 220 ? 60.62300 51.20700 -29.28100 1.000 20.38000 ? 264 ILE   B C   1 
ATOM   3654 O  O   . ILE   B 1 220 ? 60.44100 50.96200 -30.47900 1.000 20.08000 ? 264 ILE   B O   1 
ATOM   3655 C  CB  . ILE   B 1 220 ? 60.96400 49.48700 -27.45800 1.000 20.11000 ? 264 ILE   B CB  1 
ATOM   3656 C  CG1 . ILE   B 1 220 ? 61.97800 48.51400 -26.87000 1.000 20.11000 ? 264 ILE   B CG1 1 
ATOM   3657 C  CG2 . ILE   B 1 220 ? 59.81200 48.75000 -28.11700 1.000 19.42000 ? 264 ILE   B CG2 1 
ATOM   3658 C  CD1 . ILE   B 1 220 ? 61.36500 47.49200 -25.95600 1.000 18.84000 ? 264 ILE   B CD1 1 
ATOM   3659 N  N   . ALA   B 1 221 ? 59.95600 52.17200 -28.64500 1.000 20.72000 ? 265 ALA   B N   1 
ATOM   3660 C  CA  . ALA   B 1 221 ? 58.85700 52.88000 -29.29500 1.000 21.37000 ? 265 ALA   B CA  1 
ATOM   3661 C  C   . ALA   B 1 221 ? 59.31700 53.64300 -30.53200 1.000 21.09000 ? 265 ALA   B C   1 
ATOM   3662 O  O   . ALA   B 1 221 ? 58.59300 53.70800 -31.53200 1.000 21.07000 ? 265 ALA   B O   1 
ATOM   3663 C  CB  . ALA   B 1 221 ? 58.19300 53.83400 -28.30400 1.000 22.35000 ? 265 ALA   B CB  1 
ATOM   3664 N  N   . LYS   B 1 222 ? 60.51300 54.23300 -30.48700 1.000 21.16000 ? 266 LYS   B N   1 
ATOM   3665 C  CA  . LYS   B 1 222 ? 60.91700 55.12700 -31.56700 1.000 21.68000 ? 266 LYS   B CA  1 
ATOM   3666 C  C   . LYS   B 1 222 ? 61.14500 54.36500 -32.86900 1.000 21.03000 ? 266 LYS   B C   1 
ATOM   3667 O  O   . LYS   B 1 222 ? 60.83000 54.87300 -33.95100 1.000 20.90000 ? 266 LYS   B O   1 
ATOM   3668 C  CB  . LYS   B 1 222 ? 62.16900 55.91000 -31.17100 1.000 22.86000 ? 266 LYS   B CB  1 
ATOM   3669 C  CG  . LYS   B 1 222 ? 63.42700 55.07800 -31.05000 1.000 22.44000 ? 266 LYS   B CG  1 
ATOM   3670 C  CD  . LYS   B 1 222 ? 64.61400 55.92900 -30.64300 1.000 22.92000 ? 266 LYS   B CD  1 
ATOM   3671 C  CE  . LYS   B 1 222 ? 64.92200 56.98600 -31.68900 1.000 23.86000 ? 266 LYS   B CE  1 
ATOM   3672 N  NZ  . LYS   B 1 222 ? 66.07900 57.84800 -31.31100 1.000 25.48000 ? 266 LYS   B NZ  1 
ATOM   3673 N  N   . TYR   B 1 223 ? 61.67900 53.14700 -32.79100 1.000 20.76000 ? 267 TYR   B N   1 
ATOM   3674 C  CA  . TYR   B 1 223 ? 61.98800 52.39000 -33.99500 1.000 20.51000 ? 267 TYR   B CA  1 
ATOM   3675 C  C   . TYR   B 1 223 ? 60.87300 51.43400 -34.39200 1.000 19.88000 ? 267 TYR   B C   1 
ATOM   3676 O  O   . TYR   B 1 223 ? 60.81400 51.02600 -35.55700 1.000 19.53000 ? 267 TYR   B O   1 
ATOM   3677 C  CB  . TYR   B 1 223 ? 63.31100 51.63800 -33.81400 1.000 20.83000 ? 267 TYR   B CB  1 
ATOM   3678 C  CG  . TYR   B 1 223 ? 64.48900 52.57200 -33.61400 1.000 21.13000 ? 267 TYR   B CG  1 
ATOM   3679 C  CD1 . TYR   B 1 223 ? 64.69100 53.65500 -34.45900 1.000 21.28000 ? 267 TYR   B CD1 1 
ATOM   3680 C  CD2 . TYR   B 1 223 ? 65.37700 52.39100 -32.56200 1.000 21.18000 ? 267 TYR   B CD2 1 
ATOM   3681 C  CE1 . TYR   B 1 223 ? 65.75400 54.52200 -34.27400 1.000 21.32000 ? 267 TYR   B CE1 1 
ATOM   3682 C  CE2 . TYR   B 1 223 ? 66.44500 53.25300 -32.36700 1.000 20.99000 ? 267 TYR   B CE2 1 
ATOM   3683 C  CZ  . TYR   B 1 223 ? 66.62800 54.31600 -33.22600 1.000 21.11000 ? 267 TYR   B CZ  1 
ATOM   3684 O  OH  . TYR   B 1 223 ? 67.68800 55.17500 -33.03700 1.000 21.39000 ? 267 TYR   B OH  1 
ATOM   3685 N  N   . VAL   B 1 224 ? 59.98800 51.07300 -33.46000 1.000 19.82000 ? 268 VAL   B N   1 
ATOM   3686 C  CA  . VAL   B 1 224 ? 58.73900 50.42300 -33.84500 1.000 19.61000 ? 268 VAL   B CA  1 
ATOM   3687 C  C   . VAL   B 1 224 ? 57.88300 51.37700 -34.67000 1.000 19.71000 ? 268 VAL   B C   1 
ATOM   3688 O  O   . VAL   B 1 224 ? 57.22200 50.96900 -35.63300 1.000 19.38000 ? 268 VAL   B O   1 
ATOM   3689 C  CB  . VAL   B 1 224 ? 57.99200 49.91700 -32.59700 1.000 19.74000 ? 268 VAL   B CB  1 
ATOM   3690 C  CG1 . VAL   B 1 224 ? 56.53300 49.64600 -32.92000 1.000 19.85000 ? 268 VAL   B CG1 1 
ATOM   3691 C  CG2 . VAL   B 1 224 ? 58.65000 48.65900 -32.05800 1.000 18.51000 ? 268 VAL   B CG2 1 
ATOM   3692 N  N   . ILE   B 1 225 ? 57.88800 52.66400 -34.31300 1.000 20.10000 ? 269 ILE   B N   1 
ATOM   3693 C  CA  . ILE   B 1 225 ? 57.17900 53.66500 -35.10600 1.000 20.00000 ? 269 ILE   B CA  1 
ATOM   3694 C  C   . ILE   B 1 225 ? 57.80900 53.78600 -36.48700 1.000 19.76000 ? 269 ILE   B C   1 
ATOM   3695 O  O   . ILE   B 1 225 ? 57.11400 53.77000 -37.51000 1.000 19.77000 ? 269 ILE   B O   1 
ATOM   3696 C  CB  . ILE   B 1 225 ? 57.16500 55.02000 -34.37400 1.000 21.14000 ? 269 ILE   B CB  1 
ATOM   3697 C  CG1 . ILE   B 1 225 ? 56.21100 54.96900 -33.17700 1.000 21.73000 ? 269 ILE   B CG1 1 
ATOM   3698 C  CG2 . ILE   B 1 225 ? 56.78800 56.14500 -35.32900 1.000 22.04000 ? 269 ILE   B CG2 1 
ATOM   3699 C  CD1 . ILE   B 1 225 ? 56.44600 56.06300 -32.15700 1.000 22.18000 ? 269 ILE   B CD1 1 
ATOM   3700 N  N   . SER   B 1 226 ? 59.13900 53.89000 -36.53400 1.000 19.75000 ? 270 SER   B N   1 
ATOM   3701 C  CA  . SER   B 1 226 ? 59.83500 54.05600 -37.80800 1.000 19.67000 ? 270 SER   B CA  1 
ATOM   3702 C  C   . SER   B 1 226 ? 59.62100 52.85900 -38.72300 1.000 19.26000 ? 270 SER   B C   1 
ATOM   3703 O  O   . SER   B 1 226 ? 59.43300 53.02200 -39.93300 1.000 19.30000 ? 270 SER   B O   1 
ATOM   3704 C  CB  . SER   B 1 226 ? 61.32700 54.28100 -37.56300 1.000 19.95000 ? 270 SER   B CB  1 
ATOM   3705 O  OG  . SER   B 1 226 ? 61.56200 55.55700 -36.99200 1.000 20.15000 ? 270 SER   B OG  1 
ATOM   3706 N  N   . TRP   B 1 227 ? 59.64100 51.64800 -38.16300 1.000 19.00000 ? 271 TRP   B N   1 
ATOM   3707 C  CA  . TRP   B 1 227 ? 59.47900 50.44800 -38.97700 1.000 18.71000 ? 271 TRP   B CA  1 
ATOM   3708 C  C   . TRP   B 1 227 ? 58.06300 50.33400 -39.53100 1.000 18.94000 ? 271 TRP   B C   1 
ATOM   3709 O  O   . TRP   B 1 227 ? 57.87700 49.99000 -40.70400 1.000 18.85000 ? 271 TRP   B O   1 
ATOM   3710 C  CB  . TRP   B 1 227 ? 59.83200 49.21500 -38.15400 1.000 18.32000 ? 271 TRP   B CB  1 
ATOM   3711 C  CG  . TRP   B 1 227 ? 60.04900 47.97900 -38.96200 1.000 17.88000 ? 271 TRP   B CG  1 
ATOM   3712 C  CD1 . TRP   B 1 227 ? 59.13300 47.01000 -39.24100 1.000 17.65000 ? 271 TRP   B CD1 1 
ATOM   3713 C  CD2 . TRP   B 1 227 ? 61.27000 47.57000 -39.58400 1.000 17.86000 ? 271 TRP   B CD2 1 
ATOM   3714 N  NE1 . TRP   B 1 227 ? 59.70800 46.02000 -40.00000 1.000 17.36000 ? 271 TRP   B NE1 1 
ATOM   3715 C  CE2 . TRP   B 1 227 ? 61.02000 46.34200 -40.22500 1.000 17.51000 ? 271 TRP   B CE2 1 
ATOM   3716 C  CE3 . TRP   B 1 227 ? 62.55200 48.12500 -39.66200 1.000 17.93000 ? 271 TRP   B CE3 1 
ATOM   3717 C  CZ2 . TRP   B 1 227 ? 62.00400 45.65800 -40.93700 1.000 17.56000 ? 271 TRP   B CZ2 1 
ATOM   3718 C  CZ3 . TRP   B 1 227 ? 63.52500 47.44700 -40.36600 1.000 17.82000 ? 271 TRP   B CZ3 1 
ATOM   3719 C  CH2 . TRP   B 1 227 ? 63.24600 46.22500 -40.99600 1.000 17.78000 ? 271 TRP   B CH2 1 
ATOM   3720 N  N   . LEU   B 1 228 ? 57.05200 50.60000 -38.70200 1.000 19.04000 ? 272 LEU   B N   1 
ATOM   3721 C  CA  . LEU   B 1 228 ? 55.68400 50.61900 -39.20700 1.000 19.29000 ? 272 LEU   B CA  1 
ATOM   3722 C  C   . LEU   B 1 228 ? 55.47800 51.76000 -40.19700 1.000 19.60000 ? 272 LEU   B C   1 
ATOM   3723 O  O   . LEU   B 1 228 ? 54.80100 51.58600 -41.21300 1.000 19.66000 ? 272 LEU   B O   1 
ATOM   3724 C  CB  . LEU   B 1 228 ? 54.68900 50.72000 -38.04900 1.000 19.73000 ? 272 LEU   B CB  1 
ATOM   3725 C  CG  . LEU   B 1 228 ? 54.51900 49.50600 -37.12900 1.000 19.76000 ? 272 LEU   B CG  1 
ATOM   3726 C  CD1 . LEU   B 1 228 ? 53.50600 49.80200 -36.02900 1.000 19.85000 ? 272 LEU   B CD1 1 
ATOM   3727 C  CD2 . LEU   B 1 228 ? 54.11400 48.25500 -37.90100 1.000 18.99000 ? 272 LEU   B CD2 1 
ATOM   3728 N  N   . LYS   B 1 229 ? 56.05600 52.93100 -39.92300 1.000 19.65000 ? 273 LYS   B N   1 
ATOM   3729 C  CA  . LYS   B 1 229 ? 55.95600 54.04100 -40.86800 1.000 20.08000 ? 273 LYS   B CA  1 
ATOM   3730 C  C   . LYS   B 1 229 ? 56.58500 53.68900 -42.20800 1.000 20.00000 ? 273 LYS   B C   1 
ATOM   3731 O  O   . LYS   B 1 229 ? 56.01100 53.97200 -43.26400 1.000 20.27000 ? 273 LYS   B O   1 
ATOM   3732 C  CB  . LYS   B 1 229 ? 56.62400 55.28900 -40.29700 1.000 20.79000 ? 273 LYS   B CB  1 
ATOM   3733 C  CG  . LYS   B 1 229 ? 55.77900 56.08000 -39.32500 1.000 21.21000 ? 273 LYS   B CG  1 
ATOM   3734 C  CD  . LYS   B 1 229 ? 54.60100 56.74300 -39.99900 1.000 21.46000 ? 273 LYS   B CD  1 
ATOM   3735 C  CE  . LYS   B 1 229 ? 53.96400 57.75300 -39.06300 1.000 21.79000 ? 273 LYS   B CE  1 
ATOM   3736 N  NZ  . LYS   B 1 229 ? 52.79400 58.44400 -39.65400 1.000 22.39000 ? 273 LYS   B NZ  1 
ATOM   3737 N  N   . ARG   B 1 230 ? 57.76400 53.06700 -42.18700 1.000 19.83000 ? 274 ARG   B N   1 
ATOM   3738 C  CA  . ARG   B 1 230 ? 58.49100 52.82000 -43.42800 1.000 20.07000 ? 274 ARG   B CA  1 
ATOM   3739 C  C   . ARG   B 1 230 ? 57.79500 51.77800 -44.29500 1.000 19.89000 ? 274 ARG   B C   1 
ATOM   3740 O  O   . ARG   B 1 230 ? 57.78900 51.89300 -45.52300 1.000 20.16000 ? 274 ARG   B O   1 
ATOM   3741 C  CB  . ARG   B 1 230 ? 59.92300 52.38900 -43.11800 1.000 19.92000 ? 274 ARG   B CB  1 
ATOM   3742 C  CG  . ARG   B 1 230 ? 60.71100 51.88800 -44.32000 1.000 19.67000 ? 274 ARG   B CG  1 
ATOM   3743 C  CD  . ARG   B 1 230 ? 60.79800 52.92600 -45.42700 1.000 20.74000 ? 274 ARG   B CD  1 
ATOM   3744 N  NE  . ARG   B 1 230 ? 61.44800 52.36700 -46.60600 1.000 20.45000 ? 274 ARG   B NE  1 
ATOM   3745 C  CZ  . ARG   B 1 230 ? 60.83400 51.62400 -47.51700 1.000 20.78000 ? 274 ARG   B CZ  1 
ATOM   3746 N  NH1 . ARG   B 1 230 ? 59.53800 51.37000 -47.44400 1.000 20.62000 ? 274 ARG   B NH1 1 
ATOM   3747 N  NH2 . ARG   B 1 230 ? 61.54000 51.11100 -48.52000 1.000 19.41000 ? 274 ARG   B NH2 1 
ATOM   3748 N  N   . PHE   B 1 231 ? 57.20100 50.75700 -43.68500 1.000 19.62000 ? 275 PHE   B N   1 
ATOM   3749 C  CA  . PHE   B 1 231 ? 56.70000 49.62700 -44.45200 1.000 19.54000 ? 275 PHE   B CA  1 
ATOM   3750 C  C   . PHE   B 1 231 ? 55.18500 49.52300 -44.49600 1.000 19.58000 ? 275 PHE   B C   1 
ATOM   3751 O  O   . PHE   B 1 231 ? 54.64600 49.08600 -45.51300 1.000 19.36000 ? 275 PHE   B O   1 
ATOM   3752 C  CB  . PHE   B 1 231 ? 57.29500 48.32400 -43.90700 1.000 19.17000 ? 275 PHE   B CB  1 
ATOM   3753 C  CG  . PHE   B 1 231 ? 58.78400 48.24800 -44.06000 1.000 19.05000 ? 275 PHE   B CG  1 
ATOM   3754 C  CD1 . PHE   B 1 231 ? 59.34800 47.93200 -45.28400 1.000 19.07000 ? 275 PHE   B CD1 1 
ATOM   3755 C  CD2 . PHE   B 1 231 ? 59.62500 48.52200 -42.99400 1.000 18.91000 ? 275 PHE   B CD2 1 
ATOM   3756 C  CE1 . PHE   B 1 231 ? 60.71400 47.87200 -45.44000 1.000 19.12000 ? 275 PHE   B CE1 1 
ATOM   3757 C  CE2 . PHE   B 1 231 ? 60.99400 48.46700 -43.14600 1.000 18.81000 ? 275 PHE   B CE2 1 
ATOM   3758 C  CZ  . PHE   B 1 231 ? 61.53900 48.14100 -44.37200 1.000 18.88000 ? 275 PHE   B CZ  1 
ATOM   3759 N  N   . VAL   B 1 232 ? 54.48200 49.91700 -43.43500 1.000 19.73000 ? 276 VAL   B N   1 
ATOM   3760 C  CA  . VAL   B 1 232 ? 53.02500 49.94400 -43.50500 1.000 20.05000 ? 276 VAL   B CA  1 
ATOM   3761 C  C   . VAL   B 1 232 ? 52.54900 51.14900 -44.30500 1.000 20.36000 ? 276 VAL   B C   1 
ATOM   3762 O  O   . VAL   B 1 232 ? 51.56900 51.06500 -45.05200 1.000 20.50000 ? 276 VAL   B O   1 
ATOM   3763 C  CB  . VAL   B 1 232 ? 52.41800 49.92100 -42.09000 1.000 20.27000 ? 276 VAL   B CB  1 
ATOM   3764 C  CG1 . VAL   B 1 232 ? 50.91500 50.04500 -42.15300 1.000 20.23000 ? 276 VAL   B CG1 1 
ATOM   3765 C  CG2 . VAL   B 1 232 ? 52.81000 48.65100 -41.38100 1.000 19.40000 ? 276 VAL   B CG2 1 
ATOM   3766 N  N   . ASP   B 1 233 ? 53.23300 52.28300 -44.17000 1.000 20.28000 ? 277 ASP   B N   1 
ATOM   3767 C  CA  . ASP   B 1 233 ? 52.88300 53.49500 -44.89600 1.000 20.67000 ? 277 ASP   B CA  1 
ATOM   3768 C  C   . ASP   B 1 233 ? 53.75200 53.72800 -46.12000 1.000 20.92000 ? 277 ASP   B C   1 
ATOM   3769 O  O   . ASP   B 1 233 ? 53.54400 54.72000 -46.82300 1.000 21.07000 ? 277 ASP   B O   1 
ATOM   3770 C  CB  . ASP   B 1 233 ? 52.98500 54.71800 -43.98100 1.000 20.52000 ? 277 ASP   B CB  1 
ATOM   3771 C  CG  . ASP   B 1 233 ? 51.98800 54.68500 -42.85300 1.000 20.54000 ? 277 ASP   B CG  1 
ATOM   3772 O  OD1 . ASP   B 1 233 ? 51.40200 53.61100 -42.62000 1.000 20.37000 ? 277 ASP   B OD1 1 
ATOM   3773 O  OD2 . ASP   B 1 233 ? 51.78300 55.73800 -42.21400 1.000 20.74000 ? 277 ASP   B OD2 1 
ATOM   3774 N  N   . GLU   B 1 234 ? 54.72800 52.85600 -46.37900 1.000 20.71000 ? 278 GLU   B N   1 
ATOM   3775 C  CA  . GLU   B 1 234 ? 55.69200 53.05500 -47.46400 1.000 21.17000 ? 278 GLU   B CA  1 
ATOM   3776 C  C   . GLU   B 1 234 ? 56.34600 54.43000 -47.36400 1.000 21.03000 ? 278 GLU   B C   1 
ATOM   3777 O  O   . GLU   B 1 234 ? 56.72100 55.03600 -48.37100 1.000 22.63000 ? 278 GLU   B O   1 
ATOM   3778 C  CB  . GLU   B 1 234 ? 55.03400 52.85200 -48.83400 1.000 22.56000 ? 278 GLU   B CB  1 
ATOM   3779 C  CG  . GLU   B 1 234 ? 54.49400 51.44100 -49.05100 1.000 23.55000 ? 278 GLU   B CG  1 
ATOM   3780 C  CD  . GLU   B 1 234 ? 53.63200 51.31200 -50.29600 1.000 25.03000 ? 278 GLU   B CD  1 
ATOM   3781 O  OE1 . GLU   B 1 234 ? 53.68500 52.20700 -51.16300 1.000 27.14000 ? 278 GLU   B OE1 1 
ATOM   3782 O  OE2 . GLU   B 1 234 ? 52.89100 50.31300 -50.40400 1.000 26.90000 ? 278 GLU   B OE2 1 
ATOM   3783 N  N   . ASP   B 1 235 ? 56.49100 54.92000 -46.13500 1.000 21.04000 ? 279 ASP   B N   1 
ATOM   3784 C  CA  . ASP   B 1 235 ? 56.92300 56.29000 -45.86600 1.000 21.41000 ? 279 ASP   B CA  1 
ATOM   3785 C  C   . ASP   B 1 235 ? 58.44100 56.29800 -45.75300 1.000 21.22000 ? 279 ASP   B C   1 
ATOM   3786 O  O   . ASP   B 1 235 ? 59.00300 55.86000 -44.74900 1.000 20.91000 ? 279 ASP   B O   1 
ATOM   3787 C  CB  . ASP   B 1 235 ? 56.25300 56.80900 -44.59800 1.000 21.31000 ? 279 ASP   B CB  1 
ATOM   3788 C  CG  . ASP   B 1 235 ? 56.37100 58.30600 -44.43800 1.000 21.52000 ? 279 ASP   B CG  1 
ATOM   3789 O  OD1 . ASP   B 1 235 ? 57.16100 58.93300 -45.17300 1.000 21.38000 ? 279 ASP   B OD1 1 
ATOM   3790 O  OD2 . ASP   B 1 235 ? 55.66100 58.85800 -43.57100 1.000 21.61000 ? 279 ASP   B OD2 1 
ATOM   3791 N  N   . THR   B 1 236 ? 59.11100 56.79300 -46.79000 1.000 21.38000 ? 280 THR   B N   1 
ATOM   3792 C  CA  . THR   B 1 236 ? 60.56400 56.87500 -46.78000 1.000 21.49000 ? 280 THR   B CA  1 
ATOM   3793 C  C   . THR   B 1 236 ? 61.08200 58.07900 -46.01000 1.000 21.54000 ? 280 THR   B C   1 
ATOM   3794 O  O   . THR   B 1 236 ? 62.30100 58.24700 -45.90600 1.000 21.40000 ? 280 THR   B O   1 
ATOM   3795 C  CB  . THR   B 1 236 ? 61.10700 56.90700 -48.21100 1.000 21.28000 ? 280 THR   B CB  1 
ATOM   3796 O  OG1 . THR   B 1 236 ? 60.62900 58.08000 -48.88200 1.000 22.11000 ? 280 THR   B OG1 1 
ATOM   3797 C  CG2 . THR   B 1 236 ? 60.65100 55.67200 -48.97000 1.000 22.52000 ? 280 THR   B CG2 1 
ATOM   3798 N  N   . ARG   B 1 237 ? 60.19500 58.92000 -45.47300 1.000 21.43000 ? 281 ARG   B N   1 
ATOM   3799 C  CA  . ARG   B 1 237 ? 60.64400 59.93600 -44.53000 1.000 21.48000 ? 281 ARG   B CA  1 
ATOM   3800 C  C   . ARG   B 1 237 ? 61.21000 59.30800 -43.26800 1.000 21.44000 ? 281 ARG   B C   1 
ATOM   3801 O  O   . ARG   B 1 237 ? 61.95800 59.96800 -42.54100 1.000 21.37000 ? 281 ARG   B O   1 
ATOM   3802 C  CB  . ARG   B 1 237 ? 59.49800 60.87500 -44.15500 1.000 21.82000 ? 281 ARG   B CB  1 
ATOM   3803 C  CG  . ARG   B 1 237 ? 58.97700 61.74100 -45.27600 1.000 23.01000 ? 281 ARG   B CG  1 
ATOM   3804 C  CD  . ARG   B 1 237 ? 57.81000 62.56800 -44.78100 1.000 23.91000 ? 281 ARG   B CD  1 
ATOM   3805 N  NE  . ARG   B 1 237 ? 56.75600 61.72900 -44.22400 1.000 23.13000 ? 281 ARG   B NE  1 
ATOM   3806 C  CZ  . ARG   B 1 237 ? 55.65300 62.19400 -43.65300 1.000 23.80000 ? 281 ARG   B CZ  1 
ATOM   3807 N  NH1 . ARG   B 1 237 ? 55.43200 63.49100 -43.53500 1.000 24.37000 ? 281 ARG   B NH1 1 
ATOM   3808 N  NH2 . ARG   B 1 237 ? 54.75000 61.33500 -43.18700 1.000 23.45000 ? 281 ARG   B NH2 1 
ATOM   3809 N  N   . TYR   B 1 238 ? 60.87000 58.05100 -42.99900 1.000 21.20000 ? 282 TYR   B N   1 
ATOM   3810 C  CA  . TYR   B 1 238 ? 61.33300 57.32900 -41.82700 1.000 21.26000 ? 282 TYR   B CA  1 
ATOM   3811 C  C   . TYR   B 1 238 ? 62.44400 56.34100 -42.15000 1.000 20.59000 ? 282 TYR   B C   1 
ATOM   3812 O  O   . TYR   B 1 238 ? 62.73800 55.46500 -41.33400 1.000 20.08000 ? 282 TYR   B O   1 
ATOM   3813 C  CB  . TYR   B 1 238 ? 60.15600 56.61800 -41.16300 1.000 21.12000 ? 282 TYR   B CB  1 
ATOM   3814 C  CG  . TYR   B 1 238 ? 59.16100 57.58300 -40.56000 1.000 21.20000 ? 282 TYR   B CG  1 
ATOM   3815 C  CD1 . TYR   B 1 238 ? 58.22100 58.23000 -41.35000 1.000 21.36000 ? 282 TYR   B CD1 1 
ATOM   3816 C  CD2 . TYR   B 1 238 ? 59.17200 57.86000 -39.20200 1.000 21.37000 ? 282 TYR   B CD2 1 
ATOM   3817 C  CE1 . TYR   B 1 238 ? 57.31500 59.11800 -40.80000 1.000 21.77000 ? 282 TYR   B CE1 1 
ATOM   3818 C  CE2 . TYR   B 1 238 ? 58.27100 58.74100 -38.64600 1.000 21.80000 ? 282 TYR   B CE2 1 
ATOM   3819 C  CZ  . TYR   B 1 238 ? 57.34600 59.36900 -39.44500 1.000 21.79000 ? 282 TYR   B CZ  1 
ATOM   3820 O  OH  . TYR   B 1 238 ? 56.44800 60.24900 -38.88000 1.000 21.42000 ? 282 TYR   B OH  1 
ATOM   3821 N  N   . SER   B 1 239 ? 63.06100 56.45500 -43.32400 1.000 20.66000 ? 283 SER   B N   1 
ATOM   3822 C  CA  . SER   B 1 239 ? 64.24200 55.65300 -43.60900 1.000 20.53000 ? 283 SER   B CA  1 
ATOM   3823 C  C   . SER   B 1 239 ? 65.48300 56.23100 -42.94400 1.000 20.17000 ? 283 SER   B C   1 
ATOM   3824 O  O   . SER   B 1 239 ? 66.41700 55.48500 -42.62600 1.000 19.75000 ? 283 SER   B O   1 
ATOM   3825 C  CB  . SER   B 1 239 ? 64.45900 55.54300 -45.12000 1.000 20.39000 ? 283 SER   B CB  1 
ATOM   3826 O  OG  . SER   B 1 239 ? 63.51000 54.67600 -45.71700 1.000 19.81000 ? 283 SER   B OG  1 
ATOM   3827 N  N   . GLN   B 1 240 ? 65.50500 57.54800 -42.72400 1.000 20.44000 ? 284 GLN   B N   1 
ATOM   3828 C  CA  . GLN   B 1 240 ? 66.66500 58.19600 -42.12900 1.000 20.43000 ? 284 GLN   B CA  1 
ATOM   3829 C  C   . GLN   B 1 240 ? 66.94900 57.69200 -40.72400 1.000 20.19000 ? 284 GLN   B C   1 
ATOM   3830 O  O   . GLN   B 1 240 ? 68.09100 57.77600 -40.26500 1.000 19.82000 ? 284 GLN   B O   1 
ATOM   3831 C  CB  . GLN   B 1 240 ? 66.45300 59.70500 -42.10800 1.000 20.79000 ? 284 GLN   B CB  1 
ATOM   3832 C  CG  . GLN   B 1 240 ? 65.05600 60.10600 -41.69700 1.000 21.01000 ? 284 GLN   B CG  1 
ATOM   3833 C  CD  . GLN   B 1 240 ? 64.89200 61.60300 -41.59600 1.000 21.25000 ? 284 GLN   B CD  1 
ATOM   3834 O  OE1 . GLN   B 1 240 ? 65.82500 62.31600 -41.23300 1.000 19.28000 ? 284 GLN   B OE1 1 
ATOM   3835 N  NE2 . GLN   B 1 240 ? 63.70800 62.08900 -41.91900 1.000 21.94000 ? 284 GLN   B NE2 1 
ATOM   3836 N  N   . PHE   B 1 241 ? 65.94000 57.16200 -40.04000 1.000 20.14000 ? 285 PHE   B N   1 
ATOM   3837 C  CA  . PHE   B 1 241 ? 66.09700 56.66400 -38.68100 1.000 19.86000 ? 285 PHE   B CA  1 
ATOM   3838 C  C   . PHE   B 1 241 ? 66.53200 55.21200 -38.63500 1.000 19.47000 ? 285 PHE   B C   1 
ATOM   3839 O  O   . PHE   B 1 241 ? 67.16500 54.79000 -37.66100 1.000 19.30000 ? 285 PHE   B O   1 
ATOM   3840 C  CB  . PHE   B 1 241 ? 64.78000 56.82300 -37.92700 1.000 20.49000 ? 285 PHE   B CB  1 
ATOM   3841 C  CG  . PHE   B 1 241 ? 64.24000 58.20900 -37.96700 1.000 21.47000 ? 285 PHE   B CG  1 
ATOM   3842 C  CD1 . PHE   B 1 241 ? 65.03200 59.27700 -37.59700 1.000 22.12000 ? 285 PHE   B CD1 1 
ATOM   3843 C  CD2 . PHE   B 1 241 ? 62.95600 58.44800 -38.40200 1.000 22.03000 ? 285 PHE   B CD2 1 
ATOM   3844 C  CE1 . PHE   B 1 241 ? 64.54500 60.55500 -37.63300 1.000 23.51000 ? 285 PHE   B CE1 1 
ATOM   3845 C  CE2 . PHE   B 1 241 ? 62.46200 59.72600 -38.44600 1.000 22.83000 ? 285 PHE   B CE2 1 
ATOM   3846 C  CZ  . PHE   B 1 241 ? 63.25700 60.78400 -38.05900 1.000 23.65000 ? 285 PHE   B CZ  1 
ATOM   3847 N  N   . LEU   B 1 242 ? 66.19800 54.43900 -39.66300 1.000 19.48000 ? 286 LEU   B N   1 
ATOM   3848 C  CA  . LEU   B 1 242 ? 66.53900 53.02900 -39.71100 1.000 19.49000 ? 286 LEU   B CA  1 
ATOM   3849 C  C   . LEU   B 1 242 ? 67.85800 52.76200 -40.41100 1.000 19.19000 ? 286 LEU   B C   1 
ATOM   3850 O  O   . LEU   B 1 242 ? 68.47000 51.71800 -40.16400 1.000 18.99000 ? 286 LEU   B O   1 
ATOM   3851 C  CB  . LEU   B 1 242 ? 65.43000 52.24900 -40.41900 1.000 19.41000 ? 286 LEU   B CB  1 
ATOM   3852 C  CG  . LEU   B 1 242 ? 64.04000 52.37800 -39.80400 1.000 18.89000 ? 286 LEU   B CG  1 
ATOM   3853 C  CD1 . LEU   B 1 242 ? 62.95700 51.83900 -40.73600 1.000 18.76000 ? 286 LEU   B CD1 1 
ATOM   3854 C  CD2 . LEU   B 1 242 ? 64.01900 51.65700 -38.46800 1.000 19.05000 ? 286 LEU   B CD2 1 
ATOM   3855 N  N   . CYS   B 1 243 ? 68.30500 53.66800 -41.28600 1.000 19.17000 ? 287 CYS   B N   1 
ATOM   3856 C  CA  . CYS   B 1 243 ? 69.51100 53.43900 -42.06300 1.000 19.17000 ? 287 CYS   B CA  1 
ATOM   3857 C  C   . CYS   B 1 243 ? 70.32100 54.72700 -42.18000 1.000 19.47000 ? 287 CYS   B C   1 
ATOM   3858 O  O   . CYS   B 1 243 ? 69.75800 55.78500 -42.50900 1.000 19.56000 ? 287 CYS   B O   1 
ATOM   3859 C  CB  . CYS   B 1 243 ? 69.18300 52.88700 -43.44900 1.000 19.17000 ? 287 CYS   B CB  1 
ATOM   3860 S  SG  . CYS   B 1 243 ? 68.36700 51.28100 -43.41400 1.000 18.82000 ? 287 CYS   B SG  1 
ATOM   3861 N  N   . PRO   B 1 244 ? 71.63100 54.68100 -41.90900 1.000 19.40000 ? 288 PRO   B N   1 
ATOM   3862 C  CA  . PRO   B 1 244 ? 72.34100 53.49300 -41.42800 1.000 19.27000 ? 288 PRO   B CA  1 
ATOM   3863 C  C   . PRO   B 1 244 ? 71.95700 53.12600 -39.99200 1.000 19.07000 ? 288 PRO   B C   1 
ATOM   3864 O  O   . PRO   B 1 244 ? 71.09700 53.78500 -39.41000 1.000 18.96000 ? 288 PRO   B O   1 
ATOM   3865 C  CB  . PRO   B 1 244 ? 73.81400 53.90000 -41.52200 1.000 19.61000 ? 288 PRO   B CB  1 
ATOM   3866 C  CG  . PRO   B 1 244 ? 73.80500 55.37400 -41.50200 1.000 19.59000 ? 288 PRO   B CG  1 
ATOM   3867 C  CD  . PRO   B 1 244 ? 72.54600 55.80100 -42.17600 1.000 19.20000 ? 288 PRO   B CD  1 
ATOM   3868 N  N   . ASN   B 1 245 ? 72.60300 52.09600 -39.45200 1.000 18.97000 ? 289 ASN   B N   1 
ATOM   3869 C  CA  . ASN   B 1 245 ? 72.15100 51.46800 -38.21800 1.000 19.00000 ? 289 ASN   B CA  1 
ATOM   3870 C  C   . ASN   B 1 245 ? 72.07600 52.47900 -37.07600 1.000 19.02000 ? 289 ASN   B C   1 
ATOM   3871 O  O   . ASN   B 1 245 ? 72.98200 53.30600 -36.91700 1.000 19.00000 ? 289 ASN   B O   1 
ATOM   3872 C  CB  . ASN   B 1 245 ? 73.09000 50.32500 -37.83900 1.000 19.13000 ? 289 ASN   B CB  1 
ATOM   3873 C  CG  . ASN   B 1 245 ? 73.03600 49.18000 -38.82500 1.000 19.07000 ? 289 ASN   B CG  1 
ATOM   3874 O  OD1 . ASN   B 1 245 ? 72.16100 49.13400 -39.68500 1.000 18.71000 ? 289 ASN   B OD1 1 
ATOM   3875 N  ND2 . ASN   B 1 245 ? 73.95900 48.24200 -38.69500 1.000 19.23000 ? 289 ASN   B ND2 1 
ATOM   3876 N  N   . PRO   B 1 246 ? 71.01100 52.45000 -36.27400 1.000 19.19000 ? 290 PRO   B N   1 
ATOM   3877 C  CA  . PRO   B 1 246 ? 70.94400 53.32300 -35.09700 1.000 19.66000 ? 290 PRO   B CA  1 
ATOM   3878 C  C   . PRO   B 1 246 ? 72.08600 53.05700 -34.13000 1.000 20.05000 ? 290 PRO   B C   1 
ATOM   3879 O  O   . PRO   B 1 246 ? 72.57200 51.93300 -33.99800 1.000 20.00000 ? 290 PRO   B O   1 
ATOM   3880 C  CB  . PRO   B 1 246 ? 69.59300 52.96800 -34.47100 1.000 19.85000 ? 290 PRO   B CB  1 
ATOM   3881 C  CG  . PRO   B 1 246 ? 68.77600 52.48200 -35.60500 1.000 19.66000 ? 290 PRO   B CG  1 
ATOM   3882 C  CD  . PRO   B 1 246 ? 69.72700 51.78000 -36.53500 1.000 19.16000 ? 290 PRO   B CD  1 
ATOM   3883 N  N   . THR   B 1 247 ? 72.50600 54.12000 -33.43900 1.000 20.41000 ? 291 THR   B N   1 
ATOM   3884 C  CA  . THR   B 1 247 ? 73.65600 54.07100 -32.54600 1.000 20.94000 ? 291 THR   B CA  1 
ATOM   3885 C  C   . THR   B 1 247 ? 73.30600 54.51600 -31.13000 1.000 20.73000 ? 291 THR   B C   1 
ATOM   3886 O  O   . THR   B 1 247 ? 74.20100 54.90200 -30.37100 1.000 20.22000 ? 291 THR   B O   1 
ATOM   3887 C  CB  . THR   B 1 247 ? 74.79800 54.92500 -33.10000 1.000 21.45000 ? 291 THR   B CB  1 
ATOM   3888 O  OG1 . THR   B 1 247 ? 74.31900 56.24900 -33.36900 1.000 21.43000 ? 291 THR   B OG1 1 
ATOM   3889 C  CG2 . THR   B 1 247 ? 75.34400 54.32000 -34.38500 1.000 19.82000 ? 291 THR   B CG2 1 
ATOM   3890 N  N   . ASP   B 1 248 ? 72.02200 54.47100 -30.76300 1.000 20.82000 ? 292 ASP   B N   1 
ATOM   3891 C  CA  . ASP   B 1 248 ? 71.59600 54.82700 -29.41400 1.000 21.33000 ? 292 ASP   B CA  1 
ATOM   3892 C  C   . ASP   B 1 248 ? 72.43200 54.09400 -28.37100 1.000 21.56000 ? 292 ASP   B C   1 
ATOM   3893 O  O   . ASP   B 1 248 ? 72.80300 52.93200 -28.55500 1.000 21.48000 ? 292 ASP   B O   1 
ATOM   3894 C  CB  . ASP   B 1 248 ? 70.11700 54.48000 -29.21300 1.000 21.46000 ? 292 ASP   B CB  1 
ATOM   3895 C  CG  . ASP   B 1 248 ? 69.19500 55.24900 -30.13800 1.000 21.25000 ? 292 ASP   B CG  1 
ATOM   3896 O  OD1 . ASP   B 1 248 ? 69.45300 55.28000 -31.35900 1.000 20.91000 ? 292 ASP   B OD1 1 
ATOM   3897 O  OD2 . ASP   B 1 248 ? 68.19000 55.80200 -29.64300 1.000 21.84000 ? 292 ASP   B OD2 1 
ATOM   3898 N  N   . ARG   B 1 249 ? 72.73500 54.78900 -27.27000 1.000 22.08000 ? 293 ARG   B N   1 
ATOM   3899 C  CA  . ARG   B 1 249 ? 73.48900 54.16300 -26.18700 1.000 23.26000 ? 293 ARG   B CA  1 
ATOM   3900 C  C   . ARG   B 1 249 ? 72.74400 52.96700 -25.60600 1.000 22.83000 ? 293 ARG   B C   1 
ATOM   3901 O  O   . ARG   B 1 249 ? 73.37100 52.01800 -25.12300 1.000 22.76000 ? 293 ARG   B O   1 
ATOM   3902 C  CB  . ARG   B 1 249 ? 73.78800 55.19200 -25.09300 1.000 24.54000 ? 293 ARG   B CB  1 
ATOM   3903 C  CG  . ARG   B 1 249 ? 74.65300 54.66200 -23.95300 1.000 26.21000 ? 293 ARG   B CG  1 
ATOM   3904 C  CD  . ARG   B 1 249 ? 74.85600 55.70000 -22.85100 1.000 28.34000 ? 293 ARG   B CD  1 
ATOM   3905 N  NE  . ARG   B 1 249 ? 75.71000 56.80600 -23.26700 1.000 31.06000 ? 293 ARG   B NE  1 
ATOM   3906 C  CZ  . ARG   B 1 249 ? 75.26600 58.00500 -23.61900 1.000 32.26000 ? 293 ARG   B CZ  1 
ATOM   3907 N  NH1 . ARG   B 1 249 ? 73.97400 58.29300 -23.61100 1.000 31.71000 ? 293 ARG   B NH1 1 
ATOM   3908 N  NH2 . ARG   B 1 249 ? 76.13900 58.93900 -23.98500 1.000 30.56000 ? 293 ARG   B NH2 1 
ATOM   3909 N  N   . ALA   B 1 250 ? 71.41100 52.98700 -25.66200 1.000 22.31000 ? 294 ALA   B N   1 
ATOM   3910 C  CA  . ALA   B 1 250 ? 70.59900 51.87200 -25.19700 1.000 21.81000 ? 294 ALA   B CA  1 
ATOM   3911 C  C   . ALA   B 1 250 ? 70.75500 50.62800 -26.05500 1.000 21.02000 ? 294 ALA   B C   1 
ATOM   3912 O  O   . ALA   B 1 250 ? 70.30000 49.55600 -25.64400 1.000 20.35000 ? 294 ALA   B O   1 
ATOM   3913 C  CB  . ALA   B 1 250 ? 69.12600 52.27400 -25.15700 1.000 21.61000 ? 294 ALA   B CB  1 
ATOM   3914 N  N   . ILE   B 1 251 ? 71.38100 50.74100 -27.22300 1.000 21.22000 ? 295 ILE   B N   1 
ATOM   3915 C  CA  . ILE   B 1 251 ? 71.51700 49.63800 -28.16600 1.000 21.09000 ? 295 ILE   B CA  1 
ATOM   3916 C  C   . ILE   B 1 251 ? 72.90200 49.03000 -28.00700 1.000 21.25000 ? 295 ILE   B C   1 
ATOM   3917 O  O   . ILE   B 1 251 ? 73.91000 49.74500 -28.04900 1.000 21.26000 ? 295 ILE   B O   1 
ATOM   3918 C  CB  . ILE   B 1 251 ? 71.28700 50.11900 -29.61000 1.000 20.88000 ? 295 ILE   B CB  1 
ATOM   3919 C  CG1 . ILE   B 1 251 ? 69.88400 50.70600 -29.75800 1.000 20.57000 ? 295 ILE   B CG1 1 
ATOM   3920 C  CG2 . ILE   B 1 251 ? 71.49600 48.98800 -30.59700 1.000 20.36000 ? 295 ILE   B CG2 1 
ATOM   3921 C  CD1 . ILE   B 1 251 ? 69.63300 51.32100 -31.11200 1.000 20.31000 ? 295 ILE   B CD1 1 
ATOM   3922 N  N   . CYS   B 1 252 ? 72.95500 47.71000 -27.82100 1.000 20.90000 ? 296 CYS   B N   1 
ATOM   3923 C  CA  . CYS   B 1 252 ? 74.22300 47.00500 -27.68800 1.000 21.01000 ? 296 CYS   B CA  1 
ATOM   3924 C  C   . CYS   B 1 252 ? 74.65400 46.29100 -28.96000 1.000 20.22000 ? 296 CYS   B C   1 
ATOM   3925 O  O   . CYS   B 1 252 ? 75.84800 46.01900 -29.12400 1.000 19.73000 ? 296 CYS   B O   1 
ATOM   3926 C  CB  . CYS   B 1 252 ? 74.15300 45.98600 -26.54300 1.000 20.89000 ? 296 CYS   B CB  1 
ATOM   3927 S  SG  . CYS   B 1 252 ? 74.82400 46.61100 -24.98600 1.000 26.35000 ? 296 CYS   B SG  1 
ATOM   3928 N  N   . GLU   B 1 253 ? 73.71900 45.98300 -29.85400 1.000 20.18000 ? 297 GLU   B N   1 
ATOM   3929 C  CA  . GLU   B 1 253 ? 74.05500 45.38500 -31.14000 1.000 20.55000 ? 297 GLU   B CA  1 
ATOM   3930 C  C   . GLU   B 1 253 ? 72.94000 45.70700 -32.11900 1.000 19.82000 ? 297 GLU   B C   1 
ATOM   3931 O  O   . GLU   B 1 253 ? 71.76200 45.55800 -31.78400 1.000 19.31000 ? 297 GLU   B O   1 
ATOM   3932 C  CB  . GLU   B 1 253 ? 74.24100 43.87000 -31.02100 1.000 20.96000 ? 297 GLU   B CB  1 
ATOM   3933 C  CG  . GLU   B 1 253 ? 74.00800 43.12200 -32.32200 1.000 21.12000 ? 297 GLU   B CG  1 
ATOM   3934 C  CD  . GLU   B 1 253 ? 75.09900 42.12500 -32.62200 1.000 22.98000 ? 297 GLU   B CD  1 
ATOM   3935 O  OE1 . GLU   B 1 253 ? 75.18900 41.10400 -31.90800 1.000 31.36000 ? 297 GLU   B OE1 1 
ATOM   3936 O  OE2 . GLU   B 1 253 ? 75.87900 42.37000 -33.56700 1.000 26.24000 ? 297 GLU   B OE2 1 
ATOM   3937 N  N   . TYR   B 1 254 ? 73.30900 46.15700 -33.31500 1.000 19.76000 ? 298 TYR   B N   1 
ATOM   3938 C  CA  . TYR   B 1 254 ? 72.34100 46.38500 -34.37800 1.000 19.23000 ? 298 TYR   B CA  1 
ATOM   3939 C  C   . TYR   B 1 254 ? 72.82700 45.70700 -35.65100 1.000 19.08000 ? 298 TYR   B C   1 
ATOM   3940 O  O   . TYR   B 1 254 ? 74.00600 45.81000 -35.99900 1.000 19.01000 ? 298 TYR   B O   1 
ATOM   3941 C  CB  . TYR   B 1 254 ? 72.11300 47.88000 -34.61400 1.000 19.36000 ? 298 TYR   B CB  1 
ATOM   3942 C  CG  . TYR   B 1 254 ? 70.76600 48.19800 -35.21800 1.000 18.99000 ? 298 TYR   B CG  1 
ATOM   3943 C  CD1 . TYR   B 1 254 ? 70.55600 48.08800 -36.58400 1.000 18.67000 ? 298 TYR   B CD1 1 
ATOM   3944 C  CD2 . TYR   B 1 254 ? 69.70400 48.60700 -34.42600 1.000 19.18000 ? 298 TYR   B CD2 1 
ATOM   3945 C  CE1 . TYR   B 1 254 ? 69.33000 48.37800 -37.14400 1.000 18.58000 ? 298 TYR   B CE1 1 
ATOM   3946 C  CE2 . TYR   B 1 254 ? 68.47500 48.89500 -34.97500 1.000 18.73000 ? 298 TYR   B CE2 1 
ATOM   3947 C  CZ  . TYR   B 1 254 ? 68.29600 48.78100 -36.33800 1.000 18.54000 ? 298 TYR   B CZ  1 
ATOM   3948 O  OH  . TYR   B 1 254 ? 67.07800 49.07400 -36.89500 1.000 18.23000 ? 298 TYR   B OH  1 
ATOM   3949 N  N   . ARG   B 1 255 ? 71.92200 44.99600 -36.32500 1.000 18.52000 ? 299 ARG   B N   1 
ATOM   3950 C  CA  . ARG   B 1 255 ? 72.17700 44.38100 -37.62400 1.000 18.20000 ? 299 ARG   B CA  1 
ATOM   3951 C  C   . ARG   B 1 255 ? 71.02800 44.72100 -38.55900 1.000 17.93000 ? 299 ARG   B C   1 
ATOM   3952 O  O   . ARG   B 1 255 ? 69.87100 44.73800 -38.13900 1.000 17.76000 ? 299 ARG   B O   1 
ATOM   3953 C  CB  . ARG   B 1 255 ? 72.31500 42.85800 -37.51500 1.000 18.37000 ? 299 ARG   B CB  1 
ATOM   3954 C  CG  . ARG   B 1 255 ? 73.33800 42.39800 -36.50200 1.000 19.21000 ? 299 ARG   B CG  1 
ATOM   3955 C  CD  . ARG   B 1 255 ? 73.24200 40.90900 -36.24200 1.000 19.81000 ? 299 ARG   B CD  1 
ATOM   3956 N  NE  . ARG   B 1 255 ? 74.31300 40.45700 -35.36100 1.000 20.93000 ? 299 ARG   B NE  1 
ATOM   3957 C  CZ  . ARG   B 1 255 ? 74.54400 39.19100 -35.04300 1.000 21.80000 ? 299 ARG   B CZ  1 
ATOM   3958 N  NH1 . ARG   B 1 255 ? 73.77300 38.21400 -35.49100 1.000 21.21000 ? 299 ARG   B NH1 1 
ATOM   3959 N  NH2 . ARG   B 1 255 ? 75.57800 38.89800 -34.26200 1.000 21.63000 ? 299 ARG   B NH2 1 
ATOM   3960 N  N   . SER   B 1 256 ? 71.34200 44.98800 -39.82600 1.000 17.70000 ? 300 SER   B N   1 
ATOM   3961 C  CA  . SER   B 1 256 ? 70.29900 45.33000 -40.78500 1.000 17.64000 ? 300 SER   B CA  1 
ATOM   3962 C  C   . SER   B 1 256 ? 70.75400 44.97000 -42.18900 1.000 17.79000 ? 300 SER   B C   1 
ATOM   3963 O  O   . SER   B 1 256 ? 71.93800 44.73800 -42.44200 1.000 17.83000 ? 300 SER   B O   1 
ATOM   3964 C  CB  . SER   B 1 256 ? 69.93700 46.81800 -40.73700 1.000 17.69000 ? 300 SER   B CB  1 
ATOM   3965 O  OG  . SER   B 1 256 ? 70.86100 47.58000 -41.49200 1.000 17.75000 ? 300 SER   B OG  1 
ATOM   3966 N  N   . THR   B 1 257 ? 69.78400 44.92000 -43.10100 1.000 18.01000 ? 301 THR   B N   1 
ATOM   3967 C  CA  . THR   B 1 257 ? 70.05600 44.84900 -44.53400 1.000 18.39000 ? 301 THR   B CA  1 
ATOM   3968 C  C   . THR   B 1 257 ? 69.91200 46.21700 -45.17800 1.000 18.55000 ? 301 THR   B C   1 
ATOM   3969 O  O   . THR   B 1 257 ? 69.38400 46.34900 -46.28500 1.000 18.64000 ? 301 THR   B O   1 
ATOM   3970 C  CB  . THR   B 1 257 ? 69.14500 43.83400 -45.21500 1.000 19.42000 ? 301 THR   B CB  1 
ATOM   3971 O  OG1 . THR   B 1 257 ? 67.77900 44.12800 -44.91000 1.000 18.75000 ? 301 THR   B OG1 1 
ATOM   3972 C  CG2 . THR   B 1 257 ? 69.47900 42.43100 -44.75300 1.000 19.78000 ? 301 THR   B CG2 1 
ATOM   3973 N  N   . CYS   B 1 258 ? 70.35900 47.25100 -44.47200 1.000 18.52000 ? 302 CYS   B N   1 
ATOM   3974 C  CA  . CYS   B 1 258 ? 70.31900 48.60300 -44.99800 1.000 18.77000 ? 302 CYS   B CA  1 
ATOM   3975 C  C   . CYS   B 1 258 ? 71.13500 48.68700 -46.28800 1.000 19.56000 ? 302 CYS   B C   1 
ATOM   3976 O  O   . CYS   B 1 258 ? 72.07200 47.90900 -46.48900 1.000 19.06000 ? 302 CYS   B O   1 
ATOM   3977 C  CB  . CYS   B 1 258 ? 70.86400 49.59300 -43.96600 1.000 18.87000 ? 302 CYS   B CB  1 
ATOM   3978 S  SG  . CYS   B 1 258 ? 69.73400 50.00000 -42.61300 1.000 18.31000 ? 302 CYS   B SG  1 
ATOM   3979 N  N   . PRO   B 1 259 ? 70.81200 49.63900 -47.17800 1.000 20.02000 ? 303 PRO   B N   1 
ATOM   3980 C  CA  . PRO   B 1 259 ? 69.76100 50.64600 -47.02100 1.000 20.35000 ? 303 PRO   B CA  1 
ATOM   3981 C  C   . PRO   B 1 259 ? 68.38600 50.20200 -47.49500 1.000 19.94000 ? 303 PRO   B C   1 
ATOM   3982 O  O   . PRO   B 1 259 ? 68.27700 49.33500 -48.35800 1.000 19.84000 ? 303 PRO   B O   1 
ATOM   3983 C  CB  . PRO   B 1 259 ? 70.26700 51.79500 -47.88400 1.000 20.35000 ? 303 PRO   B CB  1 
ATOM   3984 C  CG  . PRO   B 1 259 ? 70.99200 51.11100 -48.98100 1.000 20.96000 ? 303 PRO   B CG  1 
ATOM   3985 C  CD  . PRO   B 1 259 ? 71.64400 49.90700 -48.36400 1.000 19.86000 ? 303 PRO   B CD  1 
ATOM   3986 N  N   . TYR   B 1 260 ? 67.35300 50.79700 -46.90500 1.000 19.70000 ? 304 TYR   B N   1 
ATOM   3987 C  CA  . TYR   B 1 260 ? 65.98900 50.72400 -47.41200 1.000 19.89000 ? 304 TYR   B CA  1 
ATOM   3988 C  C   . TYR   B 1 260 ? 65.21400 51.92600 -46.89300 1.000 19.83000 ? 304 TYR   B C   1 
ATOM   3989 O  O   . TYR   B 1 260 ? 65.79100 52.78500 -46.23000 1.000 19.55000 ? 304 TYR   B O   1 
ATOM   3990 C  CB  . TYR   B 1 260 ? 65.29200 49.41400 -47.02400 1.000 19.78000 ? 304 TYR   B CB  1 
ATOM   3991 C  CG  . TYR   B 1 260 ? 65.64700 48.85000 -45.66700 1.000 19.34000 ? 304 TYR   B CG  1 
ATOM   3992 C  CD1 . TYR   B 1 260 ? 65.16300 49.42600 -44.50300 1.000 19.14000 ? 304 TYR   B CD1 1 
ATOM   3993 C  CD2 . TYR   B 1 260 ? 66.43900 47.71800 -45.55700 1.000 19.35000 ? 304 TYR   B CD2 1 
ATOM   3994 C  CE1 . TYR   B 1 260 ? 65.48000 48.90100 -43.26500 1.000 18.93000 ? 304 TYR   B CE1 1 
ATOM   3995 C  CE2 . TYR   B 1 260 ? 66.76000 47.19100 -44.33100 1.000 18.72000 ? 304 TYR   B CE2 1 
ATOM   3996 C  CZ  . TYR   B 1 260 ? 66.27700 47.78500 -43.18900 1.000 18.56000 ? 304 TYR   B CZ  1 
ATOM   3997 O  OH  . TYR   B 1 260 ? 66.59600 47.25400 -41.96700 1.000 18.03000 ? 304 TYR   B OH  1 
ATOM   3998 O  OXT . TYR   B 1 260 ? 64.02000 52.09000 -47.13300 1.000 19.42000 ? 304 TYR   B OXT 1 
HETATM 3999 C  CAA . A1L0N C 2 .   ? 64.17600 43.73100 10.38400  1.000 18.99000 ? 401 A1L0N A CAA 1 
HETATM 4000 C  CAB . A1L0N C 2 .   ? 63.19300 43.00400 9.72800   1.000 18.23000 ? 401 A1L0N A CAB 1 
HETATM 4001 C  CAC . A1L0N C 2 .   ? 63.42300 41.67800 9.37700   1.000 18.00000 ? 401 A1L0N A CAC 1 
HETATM 4002 C  CAD . A1L0N C 2 .   ? 64.64100 41.08500 9.67800   1.000 18.19000 ? 401 A1L0N A CAD 1 
HETATM 4003 C  CAG . A1L0N C 2 .   ? 65.35500 37.20000 10.57200  1.000 19.12000 ? 401 A1L0N A CAG 1 
HETATM 4004 C  CAH . A1L0N C 2 .   ? 66.80900 36.87200 10.93100  1.000 18.60000 ? 401 A1L0N A CAH 1 
HETATM 4005 C  CAL . A1L0N C 2 .   ? 65.61600 41.81300 10.33500  1.000 20.03000 ? 401 A1L0N A CAL 1 
HETATM 4006 C  CAM . A1L0N C 2 .   ? 65.38800 43.13500 10.68500  1.000 18.64000 ? 401 A1L0N A CAM 1 
HETATM 4007 C  CAN . A1L0N C 2 .   ? 63.96400 45.05900 10.73600  1.000 19.40000 ? 401 A1L0N A CAN 1 
HETATM 4008 O  OAF . A1L0N C 2 .   ? 65.13800 38.61700 10.60400  1.000 18.28000 ? 401 A1L0N A OAF 1 
HETATM 4009 O  OAI . A1L0N C 2 .   ? 66.85900 35.66800 11.70900  1.000 26.07000 ? 401 A1L0N A OAI 1 
HETATM 4010 O  OAJ . A1L0N C 2 .   ? 63.58000 38.89000 8.65100   1.000 17.21000 ? 401 A1L0N A OAJ 1 
HETATM 4011 O  OAK . A1L0N C 2 .   ? 66.08900 39.13700 8.38400   1.000 17.77000 ? 401 A1L0N A OAK 1 
HETATM 4012 O  OAO . A1L0N C 2 .   ? 64.94500 45.80700 10.93800  1.000 19.87000 ? 401 A1L0N A OAO 1 
HETATM 4013 O  OAP . A1L0N C 2 .   ? 62.80500 45.51500 10.83000  1.000 21.37000 ? 401 A1L0N A OAP 1 
HETATM 4014 P  PAE . A1L0N C 2 .   ? 64.94000 39.46200 9.25400   1.000 17.62000 ? 401 A1L0N A PAE 1 
HETATM 4015 CA CA  . CA    D 3 .   ? 84.97500 36.68400 3.27700   1.000 24.26000 ? 402 CA    A CA  1 
HETATM 4016 C  CAA . A1L0N E 2 .   ? 58.23200 28.73700 -21.96700 1.000 18.82000 ? 401 A1L0N B CAA 1 
HETATM 4017 C  CAB . A1L0N E 2 .   ? 57.02800 29.12200 -22.53100 1.000 18.52000 ? 401 A1L0N B CAB 1 
HETATM 4018 C  CAC . A1L0N E 2 .   ? 56.84700 30.44200 -22.91300 1.000 17.98000 ? 401 A1L0N B CAC 1 
HETATM 4019 C  CAD . A1L0N E 2 .   ? 57.83600 31.39100 -22.73800 1.000 17.91000 ? 401 A1L0N B CAD 1 
HETATM 4020 C  CAG . A1L0N E 2 .   ? 57.36600 35.28100 -21.81700 1.000 16.80000 ? 401 A1L0N B CAG 1 
HETATM 4021 C  CAH . A1L0N E 2 .   ? 56.02400 35.97700 -21.59100 1.000 17.19000 ? 401 A1L0N B CAH 1 
HETATM 4022 C  CAL . A1L0N E 2 .   ? 59.03400 30.99800 -22.16700 1.000 17.85000 ? 401 A1L0N B CAL 1 
HETATM 4023 C  CAM . A1L0N E 2 .   ? 59.23900 29.67400 -21.78400 1.000 18.36000 ? 401 A1L0N B CAM 1 
HETATM 4024 C  CAN . A1L0N E 2 .   ? 58.41700 27.41300 -21.60000 1.000 20.33000 ? 401 A1L0N B CAN 1 
HETATM 4025 O  OAF . A1L0N E 2 .   ? 57.20000 33.87400 -21.89000 1.000 17.19000 ? 401 A1L0N B OAF 1 
HETATM 4026 O  OAI . A1L0N E 2 .   ? 54.95200 35.07500 -21.83100 1.000 17.64000 ? 401 A1L0N B OAI 1 
HETATM 4027 O  OAJ . A1L0N E 2 .   ? 58.95500 33.71300 -23.65700 1.000 17.01000 ? 401 A1L0N B OAJ 1 
HETATM 4028 O  OAK . A1L0N E 2 .   ? 56.49800 33.39800 -24.19600 1.000 17.42000 ? 401 A1L0N B OAK 1 
HETATM 4029 O  OAO . A1L0N E 2 .   ? 59.56600 26.96600 -21.41300 1.000 20.04000 ? 401 A1L0N B OAO 1 
HETATM 4030 O  OAP . A1L0N E 2 .   ? 57.43100 26.66400 -21.47900 1.000 21.42000 ? 401 A1L0N B OAP 1 
HETATM 4031 P  PAE . A1L0N E 2 .   ? 57.56100 33.07100 -23.22500 1.000 17.22000 ? 401 A1L0N B PAE 1 
HETATM 4032 CA CA  . CA    F 3 .   ? 37.42800 34.11700 -28.88200 1.000 22.18000 ? 402 CA    B CA  1 
HETATM 4033 O  O   . HOH   G 4 .   ? 76.80050 11.10221 -9.76243  1.000 23.94859 ? 501 HOH   A O   1 
HETATM 4034 O  O   . HOH   G 4 .   ? 63.11062 14.53824 -16.27507 1.000 20.77674 ? 502 HOH   A O   1 
HETATM 4035 O  O   . HOH   G 4 .   ? 63.71067 35.05658 -7.37797  1.000 14.76365 ? 503 HOH   A O   1 
HETATM 4036 O  O   . HOH   G 4 .   ? 50.43543 10.45116 -2.47957  1.000 22.28101 ? 504 HOH   A O   1 
HETATM 4037 O  O   . HOH   G 4 .   ? 65.22730 10.91992 -7.80097  1.000 19.88172 ? 505 HOH   A O   1 
HETATM 4038 O  O   . HOH   G 4 .   ? 64.39571 9.73654  -0.88509  1.000 23.96072 ? 506 HOH   A O   1 
HETATM 4039 O  O   . HOH   G 4 .   ? 49.20619 41.39091 0.61306   1.000 19.74711 ? 507 HOH   A O   1 
HETATM 4040 O  O   . HOH   G 4 .   ? 74.81432 35.17414 13.74351  1.000 29.77344 ? 508 HOH   A O   1 
HETATM 4041 O  O   . HOH   G 4 .   ? 56.00291 14.41797 -12.91249 1.000 18.72567 ? 509 HOH   A O   1 
HETATM 4042 O  O   . HOH   G 4 .   ? 69.68058 15.56615 -8.29448  1.000 19.52592 ? 510 HOH   A O   1 
HETATM 4043 O  O   . HOH   G 4 .   ? 65.39602 24.61905 -15.47679 1.000 19.36170 ? 511 HOH   A O   1 
HETATM 4044 O  O   . HOH   G 4 .   ? 71.867   41.005   17.787    1.000 35.61789 ? 512 HOH   A O   1 
HETATM 4045 O  O   . HOH   G 4 .   ? 86.50968 13.36267 -5.22121  1.000 28.94760 ? 513 HOH   A O   1 
HETATM 4046 O  O   . HOH   G 4 .   ? 66.21929 37.59976 -13.14004 1.000 15.54735 ? 514 HOH   A O   1 
HETATM 4047 O  O   . HOH   G 4 .   ? 57.89581 44.73992 -16.25576 1.000 26.22755 ? 515 HOH   A O   1 
HETATM 4048 O  O   . HOH   G 4 .   ? 69.96503 24.00896 11.74465  1.000 17.33339 ? 516 HOH   A O   1 
HETATM 4049 O  O   . HOH   G 4 .   ? 71.95102 16.66277 -11.72821 1.000 20.41238 ? 517 HOH   A O   1 
HETATM 4050 O  O   . HOH   G 4 .   ? 46.99469 27.89233 11.77337  1.000 20.86804 ? 518 HOH   A O   1 
HETATM 4051 O  O   . HOH   G 4 .   ? 67.89277 14.55231 -10.74591 1.000 20.92071 ? 519 HOH   A O   1 
HETATM 4052 O  O   . HOH   G 4 .   ? 66.60224 49.06636 -2.43603  1.000 20.56342 ? 520 HOH   A O   1 
HETATM 4053 O  O   . HOH   G 4 .   ? 48.01579 34.78504 5.94237   1.000 18.77560 ? 521 HOH   A O   1 
HETATM 4054 O  O   . HOH   G 4 .   ? 72.85898 47.03934 6.96231   1.000 21.83727 ? 522 HOH   A O   1 
HETATM 4055 O  O   . HOH   G 4 .   ? 53.50256 17.90576 4.89576   1.000 18.31058 ? 523 HOH   A O   1 
HETATM 4056 O  O   . HOH   G 4 .   ? 49.34575 32.63703 -9.15437  1.000 17.86974 ? 524 HOH   A O   1 
HETATM 4057 O  O   . HOH   G 4 .   ? 85.13423 15.93753 2.23955   1.000 24.15112 ? 525 HOH   A O   1 
HETATM 4058 O  O   . HOH   G 4 .   ? 57.48551 37.10360 4.39557   1.000 14.18592 ? 526 HOH   A O   1 
HETATM 4059 O  O   . HOH   G 4 .   ? 66.33793 46.52724 -4.63362  1.000 26.92590 ? 527 HOH   A O   1 
HETATM 4060 O  O   . HOH   G 4 .   ? 75.41716 17.63964 -14.89590 1.000 19.62227 ? 528 HOH   A O   1 
HETATM 4061 O  O   . HOH   G 4 .   ? 54.01031 24.54532 -7.42575  1.000 14.16007 ? 529 HOH   A O   1 
HETATM 4062 O  O   . HOH   G 4 .   ? 67.41336 18.04666 -19.77634 1.000 22.54762 ? 530 HOH   A O   1 
HETATM 4063 O  O   . HOH   G 4 .   ? 62.99491 15.30696 2.82383   1.000 22.46945 ? 531 HOH   A O   1 
HETATM 4064 O  O   . HOH   G 4 .   ? 71.70140 18.14890 -9.24511  1.000 19.55304 ? 532 HOH   A O   1 
HETATM 4065 O  O   . HOH   G 4 .   ? 68.13531 41.27475 -14.39711 1.000 16.52282 ? 533 HOH   A O   1 
HETATM 4066 O  O   . HOH   G 4 .   ? 67.44771 24.80181 -17.40181 1.000 24.31930 ? 534 HOH   A O   1 
HETATM 4067 O  O   . HOH   G 4 .   ? 73.95357 37.44764 8.82855   1.000 17.05865 ? 535 HOH   A O   1 
HETATM 4068 O  O   A HOH   G 4 .   ? 84.48453 38.89545 2.52179   0.600 17.98037 ? 536 HOH   A O   1 
HETATM 4069 O  O   B HOH   G 4 .   ? 85.78805 38.80520 4.02098   0.400 18.01469 ? 536 HOH   A O   1 
HETATM 4070 O  O   . HOH   G 4 .   ? 53.87904 10.71956 3.34773   1.000 24.78017 ? 537 HOH   A O   1 
HETATM 4071 O  O   . HOH   G 4 .   ? 68.62839 32.48369 9.26484   1.000 16.11515 ? 538 HOH   A O   1 
HETATM 4072 O  O   . HOH   G 4 .   ? 78.59499 21.17843 9.59245   1.000 21.33214 ? 539 HOH   A O   1 
HETATM 4073 O  O   . HOH   G 4 .   ? 48.11154 34.39913 -7.86272  1.000 25.76269 ? 540 HOH   A O   1 
HETATM 4074 O  O   . HOH   G 4 .   ? 58.34020 33.64658 -18.98901 1.000 21.99784 ? 541 HOH   A O   1 
HETATM 4075 O  O   . HOH   G 4 .   ? 65.49725 27.56034 -14.68636 1.000 16.39349 ? 542 HOH   A O   1 
HETATM 4076 O  O   . HOH   G 4 .   ? 73.35187 35.98767 -16.19010 1.000 18.16576 ? 543 HOH   A O   1 
HETATM 4077 O  O   . HOH   G 4 .   ? 50.75268 17.85909 -6.25728  1.000 18.05796 ? 544 HOH   A O   1 
HETATM 4078 O  O   . HOH   G 4 .   ? 55.27182 19.79266 8.50676   1.000 21.01446 ? 545 HOH   A O   1 
HETATM 4079 O  O   . HOH   G 4 .   ? 90.032   36.710   0.053     1.000 16.25733 ? 546 HOH   A O   1 
HETATM 4080 O  O   . HOH   G 4 .   ? 76.04989 24.33776 7.83287   1.000 17.42133 ? 547 HOH   A O   1 
HETATM 4081 O  O   . HOH   G 4 .   ? 66.24381 39.48406 -14.63151 1.000 16.16599 ? 548 HOH   A O   1 
HETATM 4082 O  O   . HOH   G 4 .   ? 73.54659 29.62614 5.52851   1.000 12.49362 ? 549 HOH   A O   1 
HETATM 4083 O  O   . HOH   G 4 .   ? 84.06126 34.09379 -4.65984  1.000 20.29283 ? 550 HOH   A O   1 
HETATM 4084 O  O   . HOH   G 4 .   ? 56.73193 34.72402 6.03600   1.000 15.09512 ? 551 HOH   A O   1 
HETATM 4085 O  O   . HOH   G 4 .   ? 81.27239 37.34794 -7.70741  1.000 20.59180 ? 552 HOH   A O   1 
HETATM 4086 O  O   . HOH   G 4 .   ? 79.07331 44.20184 4.00737   1.000 20.69042 ? 553 HOH   A O   1 
HETATM 4087 O  O   . HOH   G 4 .   ? 52.49303 42.63452 -5.79494  1.000 16.54066 ? 554 HOH   A O   1 
HETATM 4088 O  O   . HOH   G 4 .   ? 59.30676 24.55933 11.01777  1.000 18.41450 ? 555 HOH   A O   1 
HETATM 4089 O  O   . HOH   G 4 .   ? 52.04113 36.81197 8.07435   1.000 17.23536 ? 556 HOH   A O   1 
HETATM 4090 O  O   . HOH   G 4 .   ? 72.97757 28.47042 -13.71276 1.000 17.26183 ? 557 HOH   A O   1 
HETATM 4091 O  O   . HOH   G 4 .   ? 62.36597 46.40249 -6.89750  1.000 23.52706 ? 558 HOH   A O   1 
HETATM 4092 O  O   . HOH   G 4 .   ? 79.86373 40.23608 -2.07999  1.000 17.34317 ? 559 HOH   A O   1 
HETATM 4093 O  O   . HOH   G 4 .   ? 76.49100 35.00187 8.95316   1.000 16.26786 ? 560 HOH   A O   1 
HETATM 4094 O  O   . HOH   G 4 .   ? 52.51304 24.13081 8.95801   1.000 17.49314 ? 561 HOH   A O   1 
HETATM 4095 O  O   . HOH   G 4 .   ? 75.44957 21.64282 -18.15730 1.000 19.96578 ? 562 HOH   A O   1 
HETATM 4096 O  O   . HOH   G 4 .   ? 78.34267 42.10754 -0.17861  1.000 17.12229 ? 563 HOH   A O   1 
HETATM 4097 O  O   . HOH   G 4 .   ? 79.14960 38.46892 -6.63784  1.000 16.84944 ? 564 HOH   A O   1 
HETATM 4098 O  O   . HOH   G 4 .   ? 70.18681 10.50610 -16.15108 1.000 22.86962 ? 565 HOH   A O   1 
HETATM 4099 O  O   . HOH   G 4 .   ? 49.26764 17.23328 -1.93588  1.000 18.53352 ? 566 HOH   A O   1 
HETATM 4100 O  O   . HOH   G 4 .   ? 62.27854 16.41317 9.63404   1.000 24.50364 ? 567 HOH   A O   1 
HETATM 4101 O  O   . HOH   G 4 .   ? 46.29233 31.31672 5.95004   1.000 20.18794 ? 568 HOH   A O   1 
HETATM 4102 O  O   . HOH   G 4 .   ? 79.38238 13.52034 -9.07014  1.000 23.10176 ? 569 HOH   A O   1 
HETATM 4103 O  O   . HOH   G 4 .   ? 71.21016 13.17053 6.37971   1.000 31.63273 ? 570 HOH   A O   1 
HETATM 4104 O  O   . HOH   G 4 .   ? 91.72946 16.30922 -2.83726  1.000 33.20168 ? 571 HOH   A O   1 
HETATM 4105 O  O   . HOH   G 4 .   ? 58.36213 48.77725 -2.57729  1.000 15.34331 ? 572 HOH   A O   1 
HETATM 4106 O  O   . HOH   G 4 .   ? 49.70609 33.06868 -14.74564 1.000 21.46733 ? 573 HOH   A O   1 
HETATM 4107 O  O   . HOH   G 4 .   ? 58.71564 46.75226 4.86066   1.000 18.25183 ? 574 HOH   A O   1 
HETATM 4108 O  O   . HOH   G 4 .   ? 65.28969 8.63584  5.35629   1.000 26.97354 ? 575 HOH   A O   1 
HETATM 4109 O  O   . HOH   G 4 .   ? 80.95520 6.10394  -13.29898 1.000 30.60690 ? 576 HOH   A O   1 
HETATM 4110 O  O   . HOH   G 4 .   ? 62.29881 43.29596 -10.87055 1.000 17.74115 ? 577 HOH   A O   1 
HETATM 4111 O  O   . HOH   G 4 .   ? 65.65601 7.16489  0.80609   1.000 25.22906 ? 578 HOH   A O   1 
HETATM 4112 O  O   . HOH   G 4 .   ? 47.22636 29.04723 -8.16071  1.000 16.05239 ? 579 HOH   A O   1 
HETATM 4113 O  O   . HOH   G 4 .   ? 86.73769 30.67661 9.13352   1.000 18.50698 ? 580 HOH   A O   1 
HETATM 4114 O  O   . HOH   G 4 .   ? 57.14952 27.77199 13.62118  1.000 18.25782 ? 581 HOH   A O   1 
HETATM 4115 O  O   . HOH   G 4 .   ? 60.22997 45.78202 8.94363   1.000 18.80181 ? 582 HOH   A O   1 
HETATM 4116 O  O   . HOH   G 4 .   ? 54.76632 38.03483 -17.80620 1.000 18.16176 ? 583 HOH   A O   1 
HETATM 4117 O  O   . HOH   G 4 .   ? 50.60001 38.59441 7.28485   1.000 16.35382 ? 584 HOH   A O   1 
HETATM 4118 O  O   . HOH   G 4 .   ? 85.91108 39.70204 0.77245   1.000 18.21477 ? 585 HOH   A O   1 
HETATM 4119 O  O   . HOH   G 4 .   ? 58.62843 31.15591 -18.82184 1.000 21.75534 ? 586 HOH   A O   1 
HETATM 4120 O  O   . HOH   G 4 .   ? 72.43394 28.46649 -17.51545 1.000 23.07063 ? 587 HOH   A O   1 
HETATM 4121 O  O   . HOH   G 4 .   ? 77.61927 24.00080 -21.44208 1.000 26.80932 ? 588 HOH   A O   1 
HETATM 4122 O  O   . HOH   G 4 .   ? 56.98939 18.47020 9.53589   1.000 27.78707 ? 589 HOH   A O   1 
HETATM 4123 O  O   . HOH   G 4 .   ? 77.34480 24.84833 10.20701  1.000 18.53781 ? 590 HOH   A O   1 
HETATM 4124 O  O   . HOH   G 4 .   ? 85.463   37.706   8.280     1.000 23.81294 ? 591 HOH   A O   1 
HETATM 4125 O  O   . HOH   G 4 .   ? 46.313   16.318   4.059     1.000 18.30655 ? 592 HOH   A O   1 
HETATM 4126 O  O   . HOH   G 4 .   ? 51.45497 12.06312 -4.74744  1.000 31.77952 ? 593 HOH   A O   1 
HETATM 4127 O  O   . HOH   G 4 .   ? 68.42783 9.90944  -20.84180 1.000 32.88439 ? 594 HOH   A O   1 
HETATM 4128 O  O   . HOH   G 4 .   ? 63.67151 23.73442 -17.01460 1.000 22.58354 ? 595 HOH   A O   1 
HETATM 4129 O  O   . HOH   G 4 .   ? 65.71773 10.13436 -22.19728 1.000 32.01227 ? 596 HOH   A O   1 
HETATM 4130 O  O   . HOH   G 4 .   ? 89.62914 30.28839 9.27078   1.000 19.88511 ? 597 HOH   A O   1 
HETATM 4131 O  O   . HOH   G 4 .   ? 55.76950 43.26167 -15.65992 1.000 27.48263 ? 598 HOH   A O   1 
HETATM 4132 O  O   . HOH   H 4 .   ? 58.16820 57.33106 -29.06278 1.000 25.48138 ? 501 HOH   B O   1 
HETATM 4133 O  O   . HOH   H 4 .   ? 50.92477 56.96114 -40.36766 1.000 22.73387 ? 502 HOH   B O   1 
HETATM 4134 O  O   . HOH   H 4 .   ? 40.10914 39.98845 -23.95403 1.000 21.99642 ? 503 HOH   B O   1 
HETATM 4135 O  O   . HOH   H 4 .   ? 54.98019 26.05850 -36.48251 1.000 22.24515 ? 504 HOH   B O   1 
HETATM 4136 O  O   . HOH   H 4 .   ? 53.56618 29.68685 -40.10822 1.000 17.39278 ? 505 HOH   B O   1 
HETATM 4137 O  O   . HOH   H 4 .   ? 75.71330 51.44059 -24.95759 1.000 21.99503 ? 506 HOH   B O   1 
HETATM 4138 O  O   . HOH   H 4 .   ? 54.90286 61.54100 -40.21898 1.000 22.40700 ? 507 HOH   B O   1 
HETATM 4139 O  O   . HOH   H 4 .   ? 75.696   58.199   -32.854   1.000 20.14408 ? 508 HOH   B O   1 
HETATM 4140 O  O   . HOH   H 4 .   ? 30.68752 51.47962 -29.70375 1.000 29.14156 ? 509 HOH   B O   1 
HETATM 4141 O  O   . HOH   H 4 .   ? 54.46151 31.25664 -46.55232 1.000 17.73193 ? 510 HOH   B O   1 
HETATM 4142 O  O   . HOH   H 4 .   ? 53.47092 54.44972 -52.17035 1.000 23.62610 ? 511 HOH   B O   1 
HETATM 4143 O  O   . HOH   H 4 .   ? 65.73933 31.46308 -47.82793 1.000 18.36795 ? 512 HOH   B O   1 
HETATM 4144 O  O   . HOH   H 4 .   ? 67.92661 60.04033 -28.17626 1.000 30.03454 ? 513 HOH   B O   1 
HETATM 4145 O  O   . HOH   H 4 .   ? 45.41904 27.10486 -16.44060 1.000 29.79518 ? 514 HOH   B O   1 
HETATM 4146 O  O   . HOH   H 4 .   ? 64.26394 59.42625 -44.91904 1.000 19.86774 ? 515 HOH   B O   1 
HETATM 4147 O  O   . HOH   H 4 .   ? 74.46795 39.35507 -26.53605 1.000 22.11367 ? 516 HOH   B O   1 
HETATM 4148 O  O   . HOH   H 4 .   ? 74.01368 39.76548 -39.88770 1.000 17.38346 ? 517 HOH   B O   1 
HETATM 4149 O  O   . HOH   H 4 .   ? 36.86278 53.07519 -24.50287 1.000 25.25816 ? 518 HOH   B O   1 
HETATM 4150 O  O   . HOH   H 4 .   ? 45.22664 54.40939 -46.72113 1.000 20.96543 ? 519 HOH   B O   1 
HETATM 4151 O  O   . HOH   H 4 .   ? 69.41112 59.27516 -30.88681 1.000 30.70393 ? 520 HOH   B O   1 
HETATM 4152 O  O   . HOH   H 4 .   ? 69.94338 36.99681 -24.02921 1.000 16.44788 ? 521 HOH   B O   1 
HETATM 4153 O  O   . HOH   H 4 .   ? 52.87025 58.02247 -42.63286 1.000 20.70859 ? 522 HOH   B O   1 
HETATM 4154 O  O   . HOH   H 4 .   ? 75.31177 53.36533 -37.99907 1.000 18.43745 ? 523 HOH   B O   1 
HETATM 4155 O  O   . HOH   H 4 .   ? 43.42668 61.43473 -40.71416 1.000 27.21866 ? 524 HOH   B O   1 
HETATM 4156 O  O   . HOH   H 4 .   ? 58.37443 37.99931 -39.81998 1.000 16.14074 ? 525 HOH   B O   1 
HETATM 4157 O  O   . HOH   H 4 .   ? 53.18130 39.59048 -22.99523 1.000 17.01020 ? 526 HOH   B O   1 
HETATM 4158 O  O   . HOH   H 4 .   ? 56.11827 48.32448 -47.57359 1.000 19.31510 ? 527 HOH   B O   1 
HETATM 4159 O  O   . HOH   H 4 .   ? 48.24262 52.90078 -24.48627 1.000 21.85082 ? 528 HOH   B O   1 
HETATM 4160 O  O   . HOH   H 4 .   ? 63.87722 38.93578 -51.73696 1.000 21.15971 ? 529 HOH   B O   1 
HETATM 4161 O  O   . HOH   H 4 .   ? 72.62076 41.95006 -41.07235 1.000 16.88731 ? 530 HOH   B O   1 
HETATM 4162 O  O   . HOH   H 4 .   ? 59.23458 42.12999 -48.72404 1.000 20.74113 ? 531 HOH   B O   1 
HETATM 4163 O  O   . HOH   H 4 .   ? 56.21861 35.85066 -45.74049 1.000 15.09932 ? 532 HOH   B O   1 
HETATM 4164 O  O   . HOH   H 4 .   ? 61.65273 51.24615 -20.12240 1.000 20.36839 ? 533 HOH   B O   1 
HETATM 4165 O  O   . HOH   H 4 .   ? 47.12006 62.97024 -46.11770 1.000 25.19615 ? 534 HOH   B O   1 
HETATM 4166 O  O   . HOH   H 4 .   ? 48.73353 43.84180 -45.82140 1.000 17.20885 ? 535 HOH   B O   1 
HETATM 4167 O  O   . HOH   H 4 .   ? 48.82936 55.64343 -43.75037 1.000 21.47520 ? 536 HOH   B O   1 
HETATM 4168 O  O   . HOH   H 4 .   ? 48.59751 34.39967 -23.58066 1.000 16.06255 ? 537 HOH   B O   1 
HETATM 4169 O  O   . HOH   H 4 .   ? 64.68459 36.15698 -28.06800 1.000 13.61410 ? 538 HOH   B O   1 
HETATM 4170 O  O   . HOH   H 4 .   ? 47.48131 41.54896 -45.67130 1.000 20.32371 ? 539 HOH   B O   1 
HETATM 4171 O  O   . HOH   H 4 .   ? 56.72555 41.58126 -49.18510 1.000 18.79392 ? 540 HOH   B O   1 
HETATM 4172 O  O   . HOH   H 4 .   ? 44.40752 53.87873 -22.27863 1.000 26.97214 ? 541 HOH   B O   1 
HETATM 4173 O  O   . HOH   H 4 .   ? 67.16952 49.30823 -39.68411 1.000 15.32174 ? 542 HOH   B O   1 
HETATM 4174 O  O   . HOH   H 4 .   ? 45.71167 36.37837 -23.31173 1.000 17.78618 ? 543 HOH   B O   1 
HETATM 4175 O  O   . HOH   H 4 .   ? 45.23673 47.08310 -23.89588 1.000 17.64721 ? 544 HOH   B O   1 
HETATM 4176 O  O   . HOH   H 4 .   ? 32.48367 33.64681 -32.23732 1.000 16.60583 ? 545 HOH   B O   1 
HETATM 4177 O  O   . HOH   H 4 .   ? 48.86039 54.31453 -41.37005 1.000 19.92236 ? 546 HOH   B O   1 
HETATM 4178 O  O   . HOH   H 4 .   ? 62.82502 29.47495 -21.14144 1.000 18.36348 ? 547 HOH   B O   1 
HETATM 4179 O  O   . HOH   H 4 .   ? 66.31569 49.77781 -23.05244 1.000 19.06084 ? 548 HOH   B O   1 
HETATM 4180 O  O   . HOH   H 4 .   ? 63.14331 41.14914 -50.86364 1.000 18.05078 ? 549 HOH   B O   1 
HETATM 4181 O  O   . HOH   H 4 .   ? 50.72582 43.27934 -49.59877 1.000 18.27618 ? 550 HOH   B O   1 
HETATM 4182 O  O   . HOH   H 4 .   ? 56.09333 33.44141 -47.08133 1.000 16.08226 ? 551 HOH   B O   1 
HETATM 4183 O  O   . HOH   H 4 .   ? 45.68933 50.79986 -50.08174 1.000 22.80563 ? 552 HOH   B O   1 
HETATM 4184 O  O   . HOH   H 4 .   ? 29.20669 55.32158 -33.56741 1.000 31.83527 ? 553 HOH   B O   1 
HETATM 4185 O  O   . HOH   H 4 .   ? 62.13003 48.55863 -21.23474 1.000 19.51709 ? 554 HOH   B O   1 
HETATM 4186 O  O   . HOH   H 4 .   ? 40.90471 53.14856 -47.35443 1.000 26.51500 ? 555 HOH   B O   1 
HETATM 4187 O  O   . HOH   H 4 .   ? 42.72669 41.22257 -20.66581 1.000 19.15161 ? 556 HOH   B O   1 
HETATM 4188 O  O   . HOH   H 4 .   ? 36.63220 68.06932 -42.65440 1.000 34.24295 ? 557 HOH   B O   1 
HETATM 4189 O  O   . HOH   H 4 .   ? 52.28742 47.22153 -20.20161 1.000 19.58026 ? 558 HOH   B O   1 
HETATM 4190 O  O   . HOH   H 4 .   ? 48.44727 42.17896 -26.62299 1.000 14.89718 ? 559 HOH   B O   1 
HETATM 4191 O  O   . HOH   H 4 .   ? 33.08934 43.09928 -29.40710 1.000 18.69434 ? 560 HOH   B O   1 
HETATM 4192 O  O   . HOH   H 4 .   ? 41.24420 34.24041 -39.81285 1.000 19.12494 ? 561 HOH   B O   1 
HETATM 4193 O  O   . HOH   H 4 .   ? 54.67220 55.43033 -22.93008 1.000 22.07143 ? 562 HOH   B O   1 
HETATM 4194 O  O   . HOH   H 4 .   ? 50.522   24.519   -25.825   1.000 19.68739 ? 563 HOH   B O   1 
HETATM 4195 O  O   . HOH   H 4 .   ? 74.96669 50.20822 -34.20983 1.000 19.19043 ? 564 HOH   B O   1 
HETATM 4196 O  O   . HOH   H 4 .   ? 64.65431 23.11550 -32.29411 1.000 29.55843 ? 565 HOH   B O   1 
HETATM 4197 O  O   . HOH   H 4 .   ? 62.69714 54.84458 -22.11951 1.000 21.27032 ? 566 HOH   B O   1 
HETATM 4198 O  O   . HOH   H 4 .   ? 65.41702 38.64497 -26.47397 1.000 13.71926 ? 567 HOH   B O   1 
HETATM 4199 O  O   . HOH   H 4 .   ? 54.43583 26.56592 -39.05297 1.000 21.51971 ? 568 HOH   B O   1 
HETATM 4200 O  O   . HOH   H 4 .   ? 43.24634 32.71301 -38.50597 1.000 21.28144 ? 569 HOH   B O   1 
HETATM 4201 O  O   . HOH   H 4 .   ? 68.09295 56.41648 -44.92950 1.000 19.60185 ? 570 HOH   B O   1 
HETATM 4202 O  O   . HOH   H 4 .   ? 68.66695 49.31414 -23.08416 1.000 20.22700 ? 571 HOH   B O   1 
HETATM 4203 O  O   . HOH   H 4 .   ? 69.84945 55.54688 -25.82165 1.000 21.21929 ? 572 HOH   B O   1 
HETATM 4204 O  O   . HOH   H 4 .   ? 57.53271 57.92466 -49.12471 1.000 22.45028 ? 573 HOH   B O   1 
HETATM 4205 O  O   . HOH   H 4 .   ? 56.72589 63.40906 -25.25994 1.000 29.24489 ? 574 HOH   B O   1 
HETATM 4206 O  O   . HOH   H 4 .   ? 64.78427 45.36052 -18.52144 1.000 18.14852 ? 575 HOH   B O   1 
HETATM 4207 O  O   . HOH   H 4 .   ? 68.92460 56.42403 -35.77414 1.000 20.00073 ? 576 HOH   B O   1 
HETATM 4208 O  O   . HOH   H 4 .   ? 44.29419 31.81734 -40.84214 1.000 23.17717 ? 577 HOH   B O   1 
HETATM 4209 O  O   . HOH   H 4 .   ? 36.50600 55.49434 -45.47466 1.000 31.83465 ? 578 HOH   B O   1 
HETATM 4210 O  O   . HOH   H 4 .   ? 54.57863 42.29083 -48.36023 1.000 17.17306 ? 579 HOH   B O   1 
HETATM 4211 O  O   . HOH   H 4 .   ? 54.44684 63.77232 -26.19204 1.000 30.77479 ? 580 HOH   B O   1 
HETATM 4212 O  O   . HOH   H 4 .   ? 48.73109 47.22762 -17.71749 1.000 22.87649 ? 581 HOH   B O   1 
HETATM 4213 O  O   . HOH   H 4 .   ? 36.53031 31.21587 -31.87142 1.000 17.11760 ? 582 HOH   B O   1 
HETATM 4214 O  O   . HOH   H 4 .   ? 72.14097 34.96318 -25.11006 1.000 17.93276 ? 583 HOH   B O   1 
HETATM 4215 O  O   . HOH   H 4 .   ? 44.45398 34.51926 -22.43515 1.000 21.25315 ? 584 HOH   B O   1 
HETATM 4216 O  O   . HOH   H 4 .   ? 48.75960 36.46296 -48.33650 1.000 17.41134 ? 585 HOH   B O   1 
HETATM 4217 O  O   . HOH   H 4 .   ? 75.01709 35.16448 -34.62284 1.000 20.11491 ? 586 HOH   B O   1 
HETATM 4218 O  O   . HOH   H 4 .   ? 53.35176 62.09988 -54.80179 1.000 29.15820 ? 587 HOH   B O   1 
HETATM 4219 O  O   . HOH   H 4 .   ? 63.91224 27.15986 -24.89672 1.000 27.23357 ? 588 HOH   B O   1 
HETATM 4220 O  O   . HOH   H 4 .   ? 52.15798 55.46044 -23.85863 1.000 23.03562 ? 589 HOH   B O   1 
HETATM 4221 O  O   . HOH   H 4 .   ? 66.41224 28.05795 -24.66740 1.000 23.30028 ? 590 HOH   B O   1 
HETATM 4222 O  O   . HOH   H 4 .   ? 49.41402 40.02416 -17.81022 1.000 18.09897 ? 591 HOH   B O   1 
HETATM 4223 O  O   . HOH   H 4 .   ? 55.70860 61.54031 -54.63862 1.000 30.05354 ? 592 HOH   B O   1 
HETATM 4224 O  O   . HOH   H 4 .   ? 32.279   40.308   -22.982   1.000 22.39561 ? 593 HOH   B O   1 
HETATM 4225 O  O   . HOH   H 4 .   ? 61.75233 24.60031 -23.48875 1.000 28.09743 ? 594 HOH   B O   1 
HETATM 4226 O  O   A HOH   H 4 .   ? 50.204   23.281   -28.450   0.600 17.60640 ? 595 HOH   B O   1 
HETATM 4227 O  O   B HOH   H 4 .   ? 49.762   22.369   -29.699   0.400 18.11072 ? 595 HOH   B O   1 
HETATM 4228 O  O   . HOH   H 4 .   ? 71.21799 57.08118 -35.55979 1.000 21.28845 ? 596 HOH   B O   1 
HETATM 4229 O  O   . HOH   H 4 .   ? 54.52754 38.62882 -20.09574 1.000 18.37138 ? 597 HOH   B O   1 
HETATM 4230 O  O   . HOH   H 4 .   ? 76.06852 48.99235 -32.45660 1.000 22.06443 ? 598 HOH   B O   1 
HETATM 4231 O  O   . HOH   H 4 .   ? 64.04282 47.97725 -19.91613 1.000 19.27106 ? 599 HOH   B O   1 
HETATM 4232 O  O   . HOH   H 4 .   ? 54.38178 41.28049 -17.39862 1.000 24.43988 ? 600 HOH   B O   1 
HETATM 4233 O  O   . HOH   H 4 .   ? 48.52959 37.07040 -50.69083 1.000 23.85454 ? 601 HOH   B O   1 
# 
