data_8XC8
# 
_entry.id   8XC8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XC8         pdb_00008xc8 10.2210/pdb8xc8/pdb 
WWPDB D_1300042865 ?            ?                   
# 
_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       2024-12-11 
# 
_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                        8XC8 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-08 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              7220112092@jiangnan.edu.cn 
_pdbx_contact_author.name_first         Luo 
_pdbx_contact_author.name_last          Guocong 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0009-1691-0088 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Luo, G.'   1  ? 
'Huang, Z.' 2  ? 
'Chen, J.'  3  ? 
'Hou, X.'   4  ? 
'Zhu, Y.'   5  ? 
'Ni, D.'    6  ? 
'Xu, W.'    7  ? 
'Zhang, W.' 8  ? 
'Rao, Y.'   9  ? 
'Mu, W.'    10 ? 
# 
_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            279 
_citation.language                  ? 
_citation.page_first                135374 
_citation.page_last                 135374 
_citation.title                     
'Crystal structure and structure-guided tunnel engineering in a bacterial beta-1,4-galactosyltransferase.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.135374 
_citation.pdbx_database_id_PubMed   39265897 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Luo, G.'   1  ? 
primary 'Huang, Z.' 2  ? 
primary 'Zhu, Y.'   3  ? 
primary 'Chen, J.'  4  ? 
primary 'Hou, X.'   5  ? 
primary 'Ni, D.'    6  ? 
primary 'Xu, W.'    7  ? 
primary 'Zhang, W.' 8  ? 
primary 'Rao, Y.'   9  ? 
primary 'Mu, W.'    10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Glycosyltransferase family 25 protein' 29842.023 2 ? ? ? ? 
2 water   nat water                                   18.015    6 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(MSE)NSTENKNFVISISTAEQRRNHIIEQFTHQNIPFEFFDAFTPSDKLTDHLQRYLPNVANAAQLT(MSE)GEKGCL
(MSE)SHF(MSE)LWKKCIDENLDYITLFEDDILLGENANKFLAEGDWLKVRFNFQEIFVLRLETFL(MSE)PVQLEKQT
QIPPFQQRDIDILTSKHFGTAGYVISQGAAKYLIALFEKLTTEEIKPIDEI(MSE)FNQQINATDYRVYQLNPAICVQEL
QLNQEASLLVSNLEQERKINLKYEKRKHLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNSTENKNFVISISTAEQRRNHIIEQFTHQNIPFEFFDAFTPSDKLTDHLQRYLPNVANAAQLTMGEKGCLMSHFMLWKK
CIDENLDYITLFEDDILLGENANKFLAEGDWLKVRFNFQEIFVLRLETFLMPVQLEKQTQIPPFQQRDIDILTSKHFGTA
GYVISQGAAKYLIALFEKLTTEEIKPIDEIMFNQQINATDYRVYQLNPAICVQELQLNQEASLLVSNLEQERKINLKYEK
RKHLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MSE n 
1 2   ASN n 
1 3   SER n 
1 4   THR n 
1 5   GLU n 
1 6   ASN n 
1 7   LYS n 
1 8   ASN n 
1 9   PHE n 
1 10  VAL n 
1 11  ILE n 
1 12  SER n 
1 13  ILE n 
1 14  SER n 
1 15  THR n 
1 16  ALA n 
1 17  GLU n 
1 18  GLN n 
1 19  ARG n 
1 20  ARG n 
1 21  ASN n 
1 22  HIS n 
1 23  ILE n 
1 24  ILE n 
1 25  GLU n 
1 26  GLN n 
1 27  PHE n 
1 28  THR n 
1 29  HIS n 
1 30  GLN n 
1 31  ASN n 
1 32  ILE n 
1 33  PRO n 
1 34  PHE n 
1 35  GLU n 
1 36  PHE n 
1 37  PHE n 
1 38  ASP n 
1 39  ALA n 
1 40  PHE n 
1 41  THR n 
1 42  PRO n 
1 43  SER n 
1 44  ASP n 
1 45  LYS n 
1 46  LEU n 
1 47  THR n 
1 48  ASP n 
1 49  HIS n 
1 50  LEU n 
1 51  GLN n 
1 52  ARG n 
1 53  TYR n 
1 54  LEU n 
1 55  PRO n 
1 56  ASN n 
1 57  VAL n 
1 58  ALA n 
1 59  ASN n 
1 60  ALA n 
1 61  ALA n 
1 62  GLN n 
1 63  LEU n 
1 64  THR n 
1 65  MSE n 
1 66  GLY n 
1 67  GLU n 
1 68  LYS n 
1 69  GLY n 
1 70  CYS n 
1 71  LEU n 
1 72  MSE n 
1 73  SER n 
1 74  HIS n 
1 75  PHE n 
1 76  MSE n 
1 77  LEU n 
1 78  TRP n 
1 79  LYS n 
1 80  LYS n 
1 81  CYS n 
1 82  ILE n 
1 83  ASP n 
1 84  GLU n 
1 85  ASN n 
1 86  LEU n 
1 87  ASP n 
1 88  TYR n 
1 89  ILE n 
1 90  THR n 
1 91  LEU n 
1 92  PHE n 
1 93  GLU n 
1 94  ASP n 
1 95  ASP n 
1 96  ILE n 
1 97  LEU n 
1 98  LEU n 
1 99  GLY n 
1 100 GLU n 
1 101 ASN n 
1 102 ALA n 
1 103 ASN n 
1 104 LYS n 
1 105 PHE n 
1 106 LEU n 
1 107 ALA n 
1 108 GLU n 
1 109 GLY n 
1 110 ASP n 
1 111 TRP n 
1 112 LEU n 
1 113 LYS n 
1 114 VAL n 
1 115 ARG n 
1 116 PHE n 
1 117 ASN n 
1 118 PHE n 
1 119 GLN n 
1 120 GLU n 
1 121 ILE n 
1 122 PHE n 
1 123 VAL n 
1 124 LEU n 
1 125 ARG n 
1 126 LEU n 
1 127 GLU n 
1 128 THR n 
1 129 PHE n 
1 130 LEU n 
1 131 MSE n 
1 132 PRO n 
1 133 VAL n 
1 134 GLN n 
1 135 LEU n 
1 136 GLU n 
1 137 LYS n 
1 138 GLN n 
1 139 THR n 
1 140 GLN n 
1 141 ILE n 
1 142 PRO n 
1 143 PRO n 
1 144 PHE n 
1 145 GLN n 
1 146 GLN n 
1 147 ARG n 
1 148 ASP n 
1 149 ILE n 
1 150 ASP n 
1 151 ILE n 
1 152 LEU n 
1 153 THR n 
1 154 SER n 
1 155 LYS n 
1 156 HIS n 
1 157 PHE n 
1 158 GLY n 
1 159 THR n 
1 160 ALA n 
1 161 GLY n 
1 162 TYR n 
1 163 VAL n 
1 164 ILE n 
1 165 SER n 
1 166 GLN n 
1 167 GLY n 
1 168 ALA n 
1 169 ALA n 
1 170 LYS n 
1 171 TYR n 
1 172 LEU n 
1 173 ILE n 
1 174 ALA n 
1 175 LEU n 
1 176 PHE n 
1 177 GLU n 
1 178 LYS n 
1 179 LEU n 
1 180 THR n 
1 181 THR n 
1 182 GLU n 
1 183 GLU n 
1 184 ILE n 
1 185 LYS n 
1 186 PRO n 
1 187 ILE n 
1 188 ASP n 
1 189 GLU n 
1 190 ILE n 
1 191 MSE n 
1 192 PHE n 
1 193 ASN n 
1 194 GLN n 
1 195 GLN n 
1 196 ILE n 
1 197 ASN n 
1 198 ALA n 
1 199 THR n 
1 200 ASP n 
1 201 TYR n 
1 202 ARG n 
1 203 VAL n 
1 204 TYR n 
1 205 GLN n 
1 206 LEU n 
1 207 ASN n 
1 208 PRO n 
1 209 ALA n 
1 210 ILE n 
1 211 CYS n 
1 212 VAL n 
1 213 GLN n 
1 214 GLU n 
1 215 LEU n 
1 216 GLN n 
1 217 LEU n 
1 218 ASN n 
1 219 GLN n 
1 220 GLU n 
1 221 ALA n 
1 222 SER n 
1 223 LEU n 
1 224 LEU n 
1 225 VAL n 
1 226 SER n 
1 227 ASN n 
1 228 LEU n 
1 229 GLU n 
1 230 GLN n 
1 231 GLU n 
1 232 ARG n 
1 233 LYS n 
1 234 ILE n 
1 235 ASN n 
1 236 LEU n 
1 237 LYS n 
1 238 TYR n 
1 239 GLU n 
1 240 LYS n 
1 241 ARG n 
1 242 LYS n 
1 243 HIS n 
1 244 LEU n 
1 245 GLU n 
1 246 HIS n 
1 247 HIS n 
1 248 HIS n 
1 249 HIS n 
1 250 HIS n 
1 251 HIS 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                   251 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 FXB68_02155 
_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      'Aggregatibacter actinomycetemcomitans NUM4039' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1407647 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
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 
MSE 'L-peptide linking' n SELENOMETHIONINE ? 'C5 H11 N O2 Se' 196.106 
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   MSE 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  GLN 18  18  18  GLN GLN A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  HIS 22  22  22  HIS HIS A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  HIS 29  29  29  HIS HIS A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  MSE 65  65  65  MSE MSE A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  CYS 70  70  70  CYS CYS A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  MSE 72  72  72  MSE MSE A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  HIS 74  74  74  HIS HIS A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  MSE 76  76  76  MSE MSE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 TRP 111 111 111 TRP TRP A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 MSE 131 131 131 MSE MSE A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 GLN 134 134 134 GLN GLN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLN 145 145 145 GLN GLN A . n 
A 1 146 GLN 146 146 146 GLN GLN A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 HIS 156 156 156 HIS HIS A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 THR 159 159 159 THR THR A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 LYS 185 185 185 LYS LYS A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 MSE 191 191 191 MSE MSE A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 GLN 194 194 194 GLN GLN A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 GLN 205 205 205 GLN GLN A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 CYS 211 211 211 CYS CYS A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 GLN 213 213 213 GLN GLN A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ASN 227 227 227 ASN ASN A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 GLN 230 230 230 GLN GLN A . n 
A 1 231 GLU 231 231 231 GLU GLU A . n 
A 1 232 ARG 232 232 232 ARG ARG A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 ARG 241 241 ?   ?   ?   A . n 
A 1 242 LYS 242 242 ?   ?   ?   A . n 
A 1 243 HIS 243 243 ?   ?   ?   A . n 
A 1 244 LEU 244 244 ?   ?   ?   A . n 
A 1 245 GLU 245 245 ?   ?   ?   A . n 
A 1 246 HIS 246 246 ?   ?   ?   A . n 
A 1 247 HIS 247 247 ?   ?   ?   A . n 
A 1 248 HIS 248 248 ?   ?   ?   A . n 
A 1 249 HIS 249 249 ?   ?   ?   A . n 
A 1 250 HIS 250 250 ?   ?   ?   A . n 
A 1 251 HIS 251 251 ?   ?   ?   A . n 
B 1 1   MSE 1   1   ?   ?   ?   B . n 
B 1 2   ASN 2   2   2   ASN ASN B . n 
B 1 3   SER 3   3   3   SER SER B . n 
B 1 4   THR 4   4   4   THR THR B . n 
B 1 5   GLU 5   5   5   GLU GLU B . n 
B 1 6   ASN 6   6   6   ASN ASN B . n 
B 1 7   LYS 7   7   7   LYS LYS B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   PHE 9   9   9   PHE PHE B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  SER 12  12  12  SER SER B . n 
B 1 13  ILE 13  13  13  ILE ILE B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  THR 15  15  15  THR THR B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  GLN 18  18  18  GLN GLN B . n 
B 1 19  ARG 19  19  19  ARG ARG B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  ASN 21  21  21  ASN ASN B . n 
B 1 22  HIS 22  22  22  HIS HIS B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLN 26  26  26  GLN GLN B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  THR 28  28  28  THR THR B . n 
B 1 29  HIS 29  29  29  HIS HIS B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  ASN 31  31  31  ASN ASN B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  PHE 34  34  34  PHE PHE B . n 
B 1 35  GLU 35  35  35  GLU GLU B . n 
B 1 36  PHE 36  36  36  PHE PHE B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  THR 41  41  41  THR THR B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  THR 47  47  47  THR THR B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  HIS 49  49  49  HIS HIS B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  GLN 51  51  51  GLN GLN B . n 
B 1 52  ARG 52  52  52  ARG ARG B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  PRO 55  55  55  PRO PRO B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  LEU 63  63  63  LEU LEU B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  MSE 65  65  65  MSE MSE B . n 
B 1 66  GLY 66  66  66  GLY GLY B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  CYS 70  70  70  CYS CYS B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  MSE 72  72  72  MSE MSE B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  HIS 74  74  74  HIS HIS B . n 
B 1 75  PHE 75  75  75  PHE PHE B . n 
B 1 76  MSE 76  76  76  MSE MSE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  TRP 78  78  78  TRP TRP B . n 
B 1 79  LYS 79  79  79  LYS LYS B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  ASP 94  94  94  ASP ASP B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 LYS 104 104 104 LYS LYS B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 TRP 111 111 111 TRP TRP B . n 
B 1 112 LEU 112 112 112 LEU LEU B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 GLN 119 119 119 GLN GLN B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 PHE 122 122 122 PHE PHE B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 MSE 131 131 131 MSE MSE B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 VAL 133 133 133 VAL VAL B . n 
B 1 134 GLN 134 134 134 GLN GLN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 THR 139 139 139 THR THR B . n 
B 1 140 GLN 140 140 140 GLN GLN B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 GLN 145 145 145 GLN GLN B . n 
B 1 146 GLN 146 146 146 GLN GLN B . n 
B 1 147 ARG 147 147 147 ARG ARG B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 ASP 150 150 150 ASP ASP B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 LYS 155 155 155 LYS LYS B . n 
B 1 156 HIS 156 156 156 HIS HIS B . n 
B 1 157 PHE 157 157 157 PHE PHE B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 THR 159 159 159 THR THR B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 TYR 162 162 162 TYR TYR B . n 
B 1 163 VAL 163 163 163 VAL VAL B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 GLN 166 166 166 GLN GLN B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 TYR 171 171 171 TYR TYR B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 PHE 176 176 176 PHE PHE B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 LYS 178 178 178 LYS LYS B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 THR 181 181 181 THR THR B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 LYS 185 185 185 LYS LYS B . n 
B 1 186 PRO 186 186 186 PRO PRO B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 ILE 190 190 190 ILE ILE B . n 
B 1 191 MSE 191 191 191 MSE MSE B . n 
B 1 192 PHE 192 192 192 PHE PHE B . n 
B 1 193 ASN 193 193 193 ASN ASN B . n 
B 1 194 GLN 194 194 194 GLN GLN B . n 
B 1 195 GLN 195 195 195 GLN GLN B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 ASN 197 197 197 ASN ASN B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 TYR 201 201 201 TYR TYR B . n 
B 1 202 ARG 202 202 202 ARG ARG B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 TYR 204 204 204 TYR TYR B . n 
B 1 205 GLN 205 205 205 GLN GLN B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ASN 207 207 207 ASN ASN B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 CYS 211 211 211 CYS CYS B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 GLN 213 213 213 GLN GLN B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 ASN 218 218 218 ASN ASN B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 ASN 227 227 227 ASN ASN B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 GLN 230 230 230 GLN GLN B . n 
B 1 231 GLU 231 231 ?   ?   ?   B . n 
B 1 232 ARG 232 232 ?   ?   ?   B . n 
B 1 233 LYS 233 233 ?   ?   ?   B . n 
B 1 234 ILE 234 234 ?   ?   ?   B . n 
B 1 235 ASN 235 235 ?   ?   ?   B . n 
B 1 236 LEU 236 236 ?   ?   ?   B . n 
B 1 237 LYS 237 237 ?   ?   ?   B . n 
B 1 238 TYR 238 238 ?   ?   ?   B . n 
B 1 239 GLU 239 239 ?   ?   ?   B . n 
B 1 240 LYS 240 240 ?   ?   ?   B . n 
B 1 241 ARG 241 241 ?   ?   ?   B . n 
B 1 242 LYS 242 242 ?   ?   ?   B . n 
B 1 243 HIS 243 243 ?   ?   ?   B . n 
B 1 244 LEU 244 244 ?   ?   ?   B . n 
B 1 245 GLU 245 245 ?   ?   ?   B . n 
B 1 246 HIS 246 246 ?   ?   ?   B . n 
B 1 247 HIS 247 247 ?   ?   ?   B . n 
B 1 248 HIS 248 248 ?   ?   ?   B . n 
B 1 249 HIS 249 249 ?   ?   ?   B . n 
B 1 250 HIS 250 250 ?   ?   ?   B . n 
B 1 251 HIS 251 251 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1 301 2 HOH HOH A . 
D 2 HOH 1 301 4 HOH HOH B . 
D 2 HOH 2 302 5 HOH HOH B . 
D 2 HOH 3 303 1 HOH HOH B . 
D 2 HOH 4 304 3 HOH HOH B . 
D 2 HOH 5 305 6 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267           1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 'February 5, 2021' 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .                  4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                  5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XC8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.393 
_cell.length_a_esd                 ? 
_cell.length_b                     84.393 
_cell.length_b_esd                 ? 
_cell.length_c                     257.495 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8XC8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   8XC8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.98 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;1.26M Sodium phosphate monobasic monohydrate,
0.14M Potassium phosphate dibasic
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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         2022-11-14 
_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   0.97852 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97852 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XC8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.507 
_reflns.d_resolution_low                               80.20 
_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                                     13430 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                15.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.5 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.142 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.51 
_reflns_shell.d_res_low                                     2.87 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             672 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.731 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.67 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.67 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.34 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               73.854 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.916 
_refine.correlation_coeff_Fo_to_Fc_free          0.888 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XC8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.51 
_refine.ls_d_res_low                             80.20 
_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                     12767 
_refine.ls_number_reflns_R_free                  663 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    40.71 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.23863 
_refine.ls_R_factor_R_free                       0.27882 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23649 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.527 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             16.297 
_refine.overall_SU_ML                            0.328 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.51 
_refine_hist.d_res_low                        80.20 
_refine_hist.number_atoms_solvent             6 
_refine_hist.number_atoms_total               3848 
_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        3842 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.004  0.013  3921 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3720 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.340  1.645  5306 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.089  1.576  8556 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.488  5.000  466  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.709 24.646 226  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 19.318 15.000 681  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.405 15.000 15   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.051  0.200  521  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  4477 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  933  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.671  7.682  1870 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.672  7.680  1869 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.190  11.522 2334 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.189  11.524 2335 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.316  8.049  2051 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.316  8.051  2052 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.845  11.943 2973 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.752  91.507 4329 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.751  91.520 4330 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.16 ? 0.05 1 'interatomic distance' ? A 6672 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.16 ? 0.05 2 'interatomic distance' ? B 6672 ? ? 1 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.510 
_refine_ls_shell.d_res_low                        2.580 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             1 
_refine_ls_shell.number_reflns_R_work             34 
_refine_ls_shell.percent_reflns_obs               1.47 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.678 
_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                  0.284 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       ? 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     8XC8 
_struct.title                        beta-1,4-galacosyltransferase 
_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        8XC8 
_struct_keywords.text            TRANSFERASE 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A5D0ENI3_AGGAC 
_struct_ref.pdbx_db_accession          A0A5D0ENI3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNSTENKNFVISISTAEQRRNHIIEQFTHQNIPFEFFDAFTPSDKLTDHLQRYLPNVANAAQLTMGEKGCLMSHFMLWKK
CIDENLDYITLFEDDILLGENANKFLAEGDWLKVRFNFQEIFVLRLETFLMPVQLEKQTQIPPFQQRDIDILTSKHFGTA
GYVISQGAAKYLIALFEKLTTEEIKPIDEIMFNQQINATDYRVYQLNPAICVQELQLNQEASLLVSNLEQER
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8XC8 A 1 ? 232 ? A0A5D0ENI3 1 ? 232 ? 1 232 
2 1 8XC8 B 1 ? 232 ? A0A5D0ENI3 1 ? 232 ? 1 232 
# 
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 8XC8 LYS A 233 ? UNP A0A5D0ENI3 ? ? 'expression tag' 233 1  
1 8XC8 ILE A 234 ? UNP A0A5D0ENI3 ? ? 'expression tag' 234 2  
1 8XC8 ASN A 235 ? UNP A0A5D0ENI3 ? ? 'expression tag' 235 3  
1 8XC8 LEU A 236 ? UNP A0A5D0ENI3 ? ? 'expression tag' 236 4  
1 8XC8 LYS A 237 ? UNP A0A5D0ENI3 ? ? 'expression tag' 237 5  
1 8XC8 TYR A 238 ? UNP A0A5D0ENI3 ? ? 'expression tag' 238 6  
1 8XC8 GLU A 239 ? UNP A0A5D0ENI3 ? ? 'expression tag' 239 7  
1 8XC8 LYS A 240 ? UNP A0A5D0ENI3 ? ? 'expression tag' 240 8  
1 8XC8 ARG A 241 ? UNP A0A5D0ENI3 ? ? 'expression tag' 241 9  
1 8XC8 LYS A 242 ? UNP A0A5D0ENI3 ? ? 'expression tag' 242 10 
1 8XC8 HIS A 243 ? UNP A0A5D0ENI3 ? ? 'expression tag' 243 11 
1 8XC8 LEU A 244 ? UNP A0A5D0ENI3 ? ? 'expression tag' 244 12 
1 8XC8 GLU A 245 ? UNP A0A5D0ENI3 ? ? 'expression tag' 245 13 
1 8XC8 HIS A 246 ? UNP A0A5D0ENI3 ? ? 'expression tag' 246 14 
1 8XC8 HIS A 247 ? UNP A0A5D0ENI3 ? ? 'expression tag' 247 15 
1 8XC8 HIS A 248 ? UNP A0A5D0ENI3 ? ? 'expression tag' 248 16 
1 8XC8 HIS A 249 ? UNP A0A5D0ENI3 ? ? 'expression tag' 249 17 
1 8XC8 HIS A 250 ? UNP A0A5D0ENI3 ? ? 'expression tag' 250 18 
1 8XC8 HIS A 251 ? UNP A0A5D0ENI3 ? ? 'expression tag' 251 19 
2 8XC8 LYS B 233 ? UNP A0A5D0ENI3 ? ? 'expression tag' 233 20 
2 8XC8 ILE B 234 ? UNP A0A5D0ENI3 ? ? 'expression tag' 234 21 
2 8XC8 ASN B 235 ? UNP A0A5D0ENI3 ? ? 'expression tag' 235 22 
2 8XC8 LEU B 236 ? UNP A0A5D0ENI3 ? ? 'expression tag' 236 23 
2 8XC8 LYS B 237 ? UNP A0A5D0ENI3 ? ? 'expression tag' 237 24 
2 8XC8 TYR B 238 ? UNP A0A5D0ENI3 ? ? 'expression tag' 238 25 
2 8XC8 GLU B 239 ? UNP A0A5D0ENI3 ? ? 'expression tag' 239 26 
2 8XC8 LYS B 240 ? UNP A0A5D0ENI3 ? ? 'expression tag' 240 27 
2 8XC8 ARG B 241 ? UNP A0A5D0ENI3 ? ? 'expression tag' 241 28 
2 8XC8 LYS B 242 ? UNP A0A5D0ENI3 ? ? 'expression tag' 242 29 
2 8XC8 HIS B 243 ? UNP A0A5D0ENI3 ? ? 'expression tag' 243 30 
2 8XC8 LEU B 244 ? UNP A0A5D0ENI3 ? ? 'expression tag' 244 31 
2 8XC8 GLU B 245 ? UNP A0A5D0ENI3 ? ? 'expression tag' 245 32 
2 8XC8 HIS B 246 ? UNP A0A5D0ENI3 ? ? 'expression tag' 246 33 
2 8XC8 HIS B 247 ? UNP A0A5D0ENI3 ? ? 'expression tag' 247 34 
2 8XC8 HIS B 248 ? UNP A0A5D0ENI3 ? ? 'expression tag' 248 35 
2 8XC8 HIS B 249 ? UNP A0A5D0ENI3 ? ? 'expression tag' 249 36 
2 8XC8 HIS B 250 ? UNP A0A5D0ENI3 ? ? 'expression tag' 250 37 
2 8XC8 HIS B 251 ? UNP A0A5D0ENI3 ? ? 'expression tag' 251 38 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ALA A 16  ? GLN A 30  ? ALA A 16  GLN A 30  1 ? 15 
HELX_P HELX_P2  AA2 SER A 43  ? LEU A 54  ? SER A 43  LEU A 54  1 ? 12 
HELX_P HELX_P3  AA3 LEU A 54  ? ALA A 60  ? LEU A 54  ALA A 60  1 ? 7  
HELX_P HELX_P4  AA4 THR A 64  ? GLU A 84  ? THR A 64  GLU A 84  1 ? 21 
HELX_P HELX_P5  AA5 ASN A 101 ? ALA A 107 ? ASN A 101 ALA A 107 1 ? 7  
HELX_P HELX_P6  AA6 GLY A 109 ? VAL A 114 ? GLY A 109 VAL A 114 1 ? 6  
HELX_P HELX_P7  AA7 GLN A 166 ? LYS A 178 ? GLN A 166 LYS A 178 1 ? 13 
HELX_P HELX_P8  AA8 ILE A 187 ? PHE A 192 ? ILE A 187 PHE A 192 1 ? 6  
HELX_P HELX_P9  AA9 GLN A 213 ? GLU A 239 ? GLN A 213 GLU A 239 1 ? 27 
HELX_P HELX_P10 AB1 ALA B 16  ? GLN B 30  ? ALA B 16  GLN B 30  1 ? 15 
HELX_P HELX_P11 AB2 SER B 43  ? LEU B 54  ? SER B 43  LEU B 54  1 ? 12 
HELX_P HELX_P12 AB3 LEU B 54  ? ALA B 60  ? LEU B 54  ALA B 60  1 ? 7  
HELX_P HELX_P13 AB4 THR B 64  ? GLU B 84  ? THR B 64  GLU B 84  1 ? 21 
HELX_P HELX_P14 AB5 ASN B 101 ? ALA B 107 ? ASN B 101 ALA B 107 1 ? 7  
HELX_P HELX_P15 AB6 GLY B 109 ? VAL B 114 ? GLY B 109 VAL B 114 1 ? 6  
HELX_P HELX_P16 AB7 PRO B 143 ? ARG B 147 ? PRO B 143 ARG B 147 5 ? 5  
HELX_P HELX_P17 AB8 GLN B 166 ? LYS B 178 ? GLN B 166 LYS B 178 1 ? 13 
HELX_P HELX_P18 AB9 ILE B 187 ? PHE B 192 ? ILE B 187 PHE B 192 1 ? 6  
HELX_P HELX_P19 AC1 ASN B 193 ? ASN B 197 ? ASN B 193 ASN B 197 5 ? 5  
HELX_P HELX_P20 AC2 LEU B 215 ? SER B 226 ? LEU B 215 SER B 226 1 ? 12 
# 
_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 
covale1  covale both ? A THR 64  C ? ? ? 1_555 A MSE 65  N ? ? A THR 64  A MSE 65  1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale2  covale both ? A MSE 65  C ? ? ? 1_555 A GLY 66  N ? ? A MSE 65  A GLY 66  1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale3  covale both ? A LEU 71  C ? ? ? 1_555 A MSE 72  N ? ? A LEU 71  A MSE 72  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale4  covale both ? A MSE 72  C ? ? ? 1_555 A SER 73  N ? ? A MSE 72  A SER 73  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale5  covale both ? A PHE 75  C ? ? ? 1_555 A MSE 76  N ? ? A PHE 75  A MSE 76  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale6  covale both ? A MSE 76  C ? ? ? 1_555 A LEU 77  N ? ? A MSE 76  A LEU 77  1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale7  covale both ? A LEU 130 C ? ? ? 1_555 A MSE 131 N ? ? A LEU 130 A MSE 131 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale8  covale both ? A MSE 131 C ? ? ? 1_555 A PRO 132 N ? ? A MSE 131 A PRO 132 1_555 ? ? ? ? ? ? ? 1.346 ? ? 
covale9  covale both ? A ILE 190 C ? ? ? 1_555 A MSE 191 N ? ? A ILE 190 A MSE 191 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale10 covale both ? A MSE 191 C ? ? ? 1_555 A PHE 192 N ? ? A MSE 191 A PHE 192 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale11 covale both ? B THR 64  C ? ? ? 1_555 B MSE 65  N ? ? B THR 64  B MSE 65  1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale12 covale both ? B MSE 65  C ? ? ? 1_555 B GLY 66  N ? ? B MSE 65  B GLY 66  1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale13 covale both ? B LEU 71  C ? ? ? 1_555 B MSE 72  N ? ? B LEU 71  B MSE 72  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale14 covale both ? B MSE 72  C ? ? ? 1_555 B SER 73  N ? ? B MSE 72  B SER 73  1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale15 covale both ? B PHE 75  C ? ? ? 1_555 B MSE 76  N ? ? B PHE 75  B MSE 76  1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale16 covale both ? B MSE 76  C ? ? ? 1_555 B LEU 77  N ? ? B MSE 76  B LEU 77  1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale17 covale both ? B LEU 130 C ? ? ? 1_555 B MSE 131 N ? ? B LEU 130 B MSE 131 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale18 covale both ? B MSE 131 C ? ? ? 1_555 B PRO 132 N ? ? B MSE 131 B PRO 132 1_555 ? ? ? ? ? ? ? 1.351 ? ? 
covale19 covale both ? B ILE 190 C ? ? ? 1_555 B MSE 191 N ? ? B ILE 190 B MSE 191 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale20 covale both ? B MSE 191 C ? ? ? 1_555 B PHE 192 N ? ? B MSE 191 B PHE 192 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  MSE A 65  ? . . . . MSE A 65  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
2  MSE A 72  ? . . . . MSE A 72  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
3  MSE A 76  ? . . . . MSE A 76  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
4  MSE A 131 ? . . . . MSE A 131 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
5  MSE A 191 ? . . . . MSE A 191 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
6  MSE B 65  ? . . . . MSE B 65  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
7  MSE B 72  ? . . . . MSE B 72  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
8  MSE B 76  ? . . . . MSE B 76  ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
9  MSE B 131 ? . . . . MSE B 131 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
10 MSE B 191 ? . . . . MSE B 191 ? 1_555 . . . . . . . MET 1 MSE Selenomethionine 'Named protein modification' 
# 
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 ASN 207 A . ? ASN 207 A PRO 208 A ? PRO 208 A 1 -1.38 
2 MSE 131 B . ? MSE 131 B PRO 132 B ? PRO 132 B 1 2.90  
3 ASN 207 B . ? ASN 207 B PRO 208 B ? PRO 208 B 1 -1.36 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 35  ? ASP A 38  ? GLU A 35  ASP A 38  
AA1 2 ASN A 8   ? SER A 12  ? ASN A 8   SER A 12  
AA1 3 TYR A 88  ? GLU A 93  ? TYR A 88  GLU A 93  
AA1 4 GLY A 161 ? SER A 165 ? GLY A 161 SER A 165 
AA1 5 PHE A 122 ? ARG A 125 ? PHE A 122 ARG A 125 
AA1 6 ARG A 202 ? ASN A 207 ? ARG A 202 ASN A 207 
AA1 7 ASP B 148 ? LYS B 155 ? ASP B 148 LYS B 155 
AA1 8 GLN B 134 ? LYS B 137 ? GLN B 134 LYS B 137 
AA2 1 LEU A 97  ? LEU A 98  ? LEU A 97  LEU A 98  
AA2 2 CYS A 211 ? VAL A 212 ? CYS A 211 VAL A 212 
AA3 1 GLN A 134 ? GLU A 136 ? GLN A 134 GLU A 136 
AA3 2 ASP A 148 ? THR A 153 ? ASP A 148 THR A 153 
AA3 3 ARG B 202 ? ASN B 207 ? ARG B 202 ASN B 207 
AA3 4 PHE B 122 ? ARG B 125 ? PHE B 122 ARG B 125 
AA3 5 GLY B 161 ? SER B 165 ? GLY B 161 SER B 165 
AA3 6 TYR B 88  ? GLU B 93  ? TYR B 88  GLU B 93  
AA3 7 ASN B 8   ? SER B 12  ? ASN B 8   SER B 12  
AA3 8 GLU B 35  ? ASP B 38  ? GLU B 35  ASP B 38  
AA4 1 ILE B 96  ? LEU B 98  ? ILE B 96  LEU B 98  
AA4 2 CYS B 211 ? GLN B 213 ? CYS B 211 GLN B 213 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O PHE A 37  ? O PHE A 37  N SER A 12  ? N SER A 12  
AA1 2 3 N ILE A 11  ? N ILE A 11  O PHE A 92  ? O PHE A 92  
AA1 3 4 N ILE A 89  ? N ILE A 89  O ILE A 164 ? O ILE A 164 
AA1 4 5 O VAL A 163 ? O VAL A 163 N LEU A 124 ? N LEU A 124 
AA1 5 6 N ARG A 125 ? N ARG A 125 O TYR A 204 ? O TYR A 204 
AA1 6 7 N GLN A 205 ? N GLN A 205 O ASP B 150 ? O ASP B 150 
AA1 7 8 O THR B 153 ? O THR B 153 N LEU B 135 ? N LEU B 135 
AA2 1 2 N LEU A 97  ? N LEU A 97  O VAL A 212 ? O VAL A 212 
AA3 1 2 N GLN A 134 ? N GLN A 134 O THR A 153 ? O THR A 153 
AA3 2 3 N LEU A 152 ? N LEU A 152 O VAL B 203 ? O VAL B 203 
AA3 3 4 O TYR B 204 ? O TYR B 204 N ARG B 125 ? N ARG B 125 
AA3 4 5 N LEU B 124 ? N LEU B 124 O VAL B 163 ? O VAL B 163 
AA3 5 6 O ILE B 164 ? O ILE B 164 N ILE B 89  ? N ILE B 89  
AA3 6 7 O PHE B 92  ? O PHE B 92  N ILE B 11  ? N ILE B 11  
AA3 7 8 N SER B 12  ? N SER B 12  O PHE B 37  ? O PHE B 37  
AA4 1 2 N LEU B 97  ? N LEU B 97  O VAL B 212 ? O VAL B 212 
# 
_pdbx_entry_details.entry_id                   8XC8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   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 16  ? ? -64.02  58.12   
2  1 PRO A 42  ? ? -45.21  103.18  
3  1 ASP A 48  ? ? -43.94  -72.04  
4  1 LEU A 50  ? ? -53.99  -71.43  
5  1 ASN A 56  ? ? -20.85  -44.35  
6  1 ALA A 60  ? ? -42.79  109.79  
7  1 ASN A 85  ? ? 35.65   61.31   
8  1 ASN A 101 ? ? -99.36  34.02   
9  1 ILE A 121 ? ? -105.02 58.33   
10 1 ILE A 149 ? ? -107.03 73.28   
11 1 PHE A 157 ? ? -65.93  79.07   
12 1 ILE A 184 ? ? -58.96  96.78   
13 1 ASN A 193 ? ? -87.03  -74.73  
14 1 ILE A 196 ? ? -147.33 17.25   
15 1 ALA A 198 ? ? -164.40 -69.50  
16 1 THR A 199 ? ? -36.33  154.07  
17 1 ALA B 16  ? ? -64.64  58.19   
18 1 PRO B 42  ? ? -45.51  103.01  
19 1 ASP B 48  ? ? -44.16  -71.73  
20 1 LEU B 50  ? ? -53.80  -71.46  
21 1 ASN B 56  ? ? -20.98  -43.74  
22 1 ALA B 60  ? ? -44.42  108.97  
23 1 ASN B 85  ? ? 35.82   62.21   
24 1 THR B 128 ? ? -58.65  -178.12 
25 1 ILE B 149 ? ? -112.46 73.92   
26 1 THR B 153 ? ? -117.97 -110.14 
27 1 ILE B 184 ? ? -61.54  95.50   
28 1 GLU B 189 ? ? -68.32  0.95    
29 1 ASN B 193 ? ? -87.61  -76.83  
30 1 ASN B 197 ? ? -44.51  -76.73  
31 1 THR B 199 ? ? 87.25   25.01   
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A MSE 65  A MSE 65  ? MET 'modified residue' 
2  A MSE 72  A MSE 72  ? MET 'modified residue' 
3  A MSE 76  A MSE 76  ? MET 'modified residue' 
4  A MSE 131 A MSE 131 ? MET 'modified residue' 
5  A MSE 191 A MSE 191 ? MET 'modified residue' 
6  B MSE 65  B MSE 65  ? MET 'modified residue' 
7  B MSE 72  B MSE 72  ? MET 'modified residue' 
8  B MSE 76  B MSE 76  ? MET 'modified residue' 
9  B MSE 131 B MSE 131 ? MET 'modified residue' 
10 B MSE 191 B MSE 191 ? MET 'modified residue' 
# 
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 MSE 1   ? A MSE 1   
2  1 Y 1 A ARG 241 ? A ARG 241 
3  1 Y 1 A LYS 242 ? A LYS 242 
4  1 Y 1 A HIS 243 ? A HIS 243 
5  1 Y 1 A LEU 244 ? A LEU 244 
6  1 Y 1 A GLU 245 ? A GLU 245 
7  1 Y 1 A HIS 246 ? A HIS 246 
8  1 Y 1 A HIS 247 ? A HIS 247 
9  1 Y 1 A HIS 248 ? A HIS 248 
10 1 Y 1 A HIS 249 ? A HIS 249 
11 1 Y 1 A HIS 250 ? A HIS 250 
12 1 Y 1 A HIS 251 ? A HIS 251 
13 1 Y 1 B MSE 1   ? B MSE 1   
14 1 Y 1 B GLU 231 ? B GLU 231 
15 1 Y 1 B ARG 232 ? B ARG 232 
16 1 Y 1 B LYS 233 ? B LYS 233 
17 1 Y 1 B ILE 234 ? B ILE 234 
18 1 Y 1 B ASN 235 ? B ASN 235 
19 1 Y 1 B LEU 236 ? B LEU 236 
20 1 Y 1 B LYS 237 ? B LYS 237 
21 1 Y 1 B TYR 238 ? B TYR 238 
22 1 Y 1 B GLU 239 ? B GLU 239 
23 1 Y 1 B LYS 240 ? B LYS 240 
24 1 Y 1 B ARG 241 ? B ARG 241 
25 1 Y 1 B LYS 242 ? B LYS 242 
26 1 Y 1 B HIS 243 ? B HIS 243 
27 1 Y 1 B LEU 244 ? B LEU 244 
28 1 Y 1 B GLU 245 ? B GLU 245 
29 1 Y 1 B HIS 246 ? B HIS 246 
30 1 Y 1 B HIS 247 ? B HIS 247 
31 1 Y 1 B HIS 248 ? B HIS 248 
32 1 Y 1 B HIS 249 ? B HIS 249 
33 1 Y 1 B HIS 250 ? B HIS 250 
34 1 Y 1 B HIS 251 ? B HIS 251 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MSE N    N  N N 230 
MSE CA   C  N S 231 
MSE C    C  N N 232 
MSE O    O  N N 233 
MSE OXT  O  N N 234 
MSE CB   C  N N 235 
MSE CG   C  N N 236 
MSE SE   SE N N 237 
MSE CE   C  N N 238 
MSE H    H  N N 239 
MSE H2   H  N N 240 
MSE HA   H  N N 241 
MSE HXT  H  N N 242 
MSE HB2  H  N N 243 
MSE HB3  H  N N 244 
MSE HG2  H  N N 245 
MSE HG3  H  N N 246 
MSE HE1  H  N N 247 
MSE HE2  H  N N 248 
MSE HE3  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
VAL N    N  N N 372 
VAL CA   C  N S 373 
VAL C    C  N N 374 
VAL O    O  N N 375 
VAL CB   C  N N 376 
VAL CG1  C  N N 377 
VAL CG2  C  N N 378 
VAL OXT  O  N N 379 
VAL H    H  N N 380 
VAL H2   H  N N 381 
VAL HA   H  N N 382 
VAL HB   H  N N 383 
VAL HG11 H  N N 384 
VAL HG12 H  N N 385 
VAL HG13 H  N N 386 
VAL HG21 H  N N 387 
VAL HG22 H  N N 388 
VAL HG23 H  N N 389 
VAL HXT  H  N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MSE N   CA   sing N N 218 
MSE N   H    sing N N 219 
MSE N   H2   sing N N 220 
MSE CA  C    sing N N 221 
MSE CA  CB   sing N N 222 
MSE CA  HA   sing N N 223 
MSE C   O    doub N N 224 
MSE C   OXT  sing N N 225 
MSE OXT HXT  sing N N 226 
MSE CB  CG   sing N N 227 
MSE CB  HB2  sing N N 228 
MSE CB  HB3  sing N N 229 
MSE CG  SE   sing N N 230 
MSE CG  HG2  sing N N 231 
MSE CG  HG3  sing N N 232 
MSE SE  CE   sing N N 233 
MSE CE  HE1  sing N N 234 
MSE CE  HE2  sing N N 235 
MSE CE  HE3  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 2022YFC2104900 1 
'National Natural Science Foundation of China (NSFC)' China 32302010       2 
'Other private'                                       ?     BK20231043     3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF_AFQ03974F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XC8 
_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]   0.011849 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.011849 
_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]   0.003884 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
SE 
# 
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 2   ? 7.968   -15.828 -26.434 1.00 79.81  ? 2   ASN A N   1 
ATOM   2    C  CA  . ASN A 1 2   ? 8.738   -15.250 -27.586 1.00 73.77  ? 2   ASN A CA  1 
ATOM   3    C  C   . ASN A 1 2   ? 8.749   -16.221 -28.772 1.00 69.18  ? 2   ASN A C   1 
ATOM   4    O  O   . ASN A 1 2   ? 9.344   -15.854 -29.793 1.00 74.48  ? 2   ASN A O   1 
ATOM   5    C  CB  . ASN A 1 2   ? 10.164  -14.846 -27.189 1.00 76.17  ? 2   ASN A CB  1 
ATOM   6    C  CG  . ASN A 1 2   ? 10.967  -15.949 -26.526 1.00 77.36  ? 2   ASN A CG  1 
ATOM   7    O  OD1 . ASN A 1 2   ? 11.098  -17.048 -27.062 1.00 73.16  ? 2   ASN A OD1 1 
ATOM   8    N  ND2 . ASN A 1 2   ? 11.535  -15.656 -25.367 1.00 77.92  ? 2   ASN A ND2 1 
ATOM   9    N  N   . SER A 1 3   ? 8.116   -17.398 -28.646 1.00 64.81  ? 3   SER A N   1 
ATOM   10   C  CA  . SER A 1 3   ? 7.986   -18.446 -29.700 1.00 60.34  ? 3   SER A CA  1 
ATOM   11   C  C   . SER A 1 3   ? 6.496   -18.720 -29.973 1.00 63.59  ? 3   SER A C   1 
ATOM   12   O  O   . SER A 1 3   ? 5.650   -18.319 -29.125 1.00 71.39  ? 3   SER A O   1 
ATOM   13   C  CB  . SER A 1 3   ? 8.744   -19.701 -29.305 1.00 52.81  ? 3   SER A CB  1 
ATOM   14   O  OG  . SER A 1 3   ? 8.232   -20.856 -29.949 1.00 47.74  ? 3   SER A OG  1 
ATOM   15   N  N   . THR A 1 4   ? 6.167   -19.310 -31.130 1.00 60.47  ? 4   THR A N   1 
ATOM   16   C  CA  . THR A 1 4   ? 4.790   -19.757 -31.479 1.00 59.69  ? 4   THR A CA  1 
ATOM   17   C  C   . THR A 1 4   ? 4.755   -21.274 -31.654 1.00 56.01  ? 4   THR A C   1 
ATOM   18   O  O   . THR A 1 4   ? 3.756   -21.767 -32.191 1.00 54.53  ? 4   THR A O   1 
ATOM   19   C  CB  . THR A 1 4   ? 4.249   -19.100 -32.753 1.00 63.10  ? 4   THR A CB  1 
ATOM   20   O  OG1 . THR A 1 4   ? 5.045   -19.553 -33.847 1.00 69.68  ? 4   THR A OG1 1 
ATOM   21   C  CG2 . THR A 1 4   ? 4.249   -17.590 -32.678 1.00 65.93  ? 4   THR A CG2 1 
ATOM   22   N  N   . GLU A 1 5   ? 5.798   -21.978 -31.213 1.00 55.51  ? 5   GLU A N   1 
ATOM   23   C  CA  . GLU A 1 5   ? 5.774   -23.456 -31.103 1.00 57.58  ? 5   GLU A CA  1 
ATOM   24   C  C   . GLU A 1 5   ? 4.617   -23.832 -30.170 1.00 58.22  ? 5   GLU A C   1 
ATOM   25   O  O   . GLU A 1 5   ? 4.398   -23.094 -29.191 1.00 60.84  ? 5   GLU A O   1 
ATOM   26   C  CB  . GLU A 1 5   ? 7.120   -23.987 -30.613 1.00 58.78  ? 5   GLU A CB  1 
ATOM   27   C  CG  . GLU A 1 5   ? 7.112   -25.492 -30.428 1.00 61.18  ? 5   GLU A CG  1 
ATOM   28   C  CD  . GLU A 1 5   ? 8.442   -26.194 -30.638 1.00 62.16  ? 5   GLU A CD  1 
ATOM   29   O  OE1 . GLU A 1 5   ? 9.502   -25.578 -30.338 1.00 59.16  ? 5   GLU A OE1 1 
ATOM   30   O  OE2 . GLU A 1 5   ? 8.408   -27.359 -31.105 1.00 60.78  ? 5   GLU A OE2 1 
ATOM   31   N  N   . ASN A 1 6   ? 3.892   -24.912 -30.479 1.00 59.44  ? 6   ASN A N   1 
ATOM   32   C  CA  . ASN A 1 6   ? 2.663   -25.329 -29.752 1.00 62.04  ? 6   ASN A CA  1 
ATOM   33   C  C   . ASN A 1 6   ? 2.990   -25.510 -28.267 1.00 61.73  ? 6   ASN A C   1 
ATOM   34   O  O   . ASN A 1 6   ? 3.965   -26.238 -27.964 1.00 58.63  ? 6   ASN A O   1 
ATOM   35   C  CB  . ASN A 1 6   ? 2.041   -26.610 -30.314 1.00 65.34  ? 6   ASN A CB  1 
ATOM   36   C  CG  . ASN A 1 6   ? 0.748   -26.973 -29.615 1.00 67.54  ? 6   ASN A CG  1 
ATOM   37   O  OD1 . ASN A 1 6   ? -0.159  -26.150 -29.518 1.00 70.70  ? 6   ASN A OD1 1 
ATOM   38   N  ND2 . ASN A 1 6   ? 0.660   -28.189 -29.104 1.00 68.77  ? 6   ASN A ND2 1 
ATOM   39   N  N   . LYS A 1 7   ? 2.205   -24.844 -27.408 1.00 60.16  ? 7   LYS A N   1 
ATOM   40   C  CA  . LYS A 1 7   ? 2.308   -24.837 -25.922 1.00 55.70  ? 7   LYS A CA  1 
ATOM   41   C  C   . LYS A 1 7   ? 1.122   -25.586 -25.300 1.00 53.38  ? 7   LYS A C   1 
ATOM   42   O  O   . LYS A 1 7   ? 1.259   -26.061 -24.162 1.00 53.50  ? 7   LYS A O   1 
ATOM   43   C  CB  . LYS A 1 7   ? 2.312   -23.396 -25.407 1.00 55.92  ? 7   LYS A CB  1 
ATOM   44   C  CG  . LYS A 1 7   ? 3.508   -22.561 -25.834 1.00 58.72  ? 7   LYS A CG  1 
ATOM   45   C  CD  . LYS A 1 7   ? 3.136   -21.143 -26.192 1.00 63.60  ? 7   LYS A CD  1 
ATOM   46   C  CE  . LYS A 1 7   ? 4.321   -20.199 -26.217 1.00 67.28  ? 7   LYS A CE  1 
ATOM   47   N  NZ  . LYS A 1 7   ? 5.083   -20.296 -27.484 1.00 68.40  ? 7   LYS A NZ  1 
ATOM   48   N  N   . ASN A 1 8   ? -0.012  -25.657 -26.002 1.00 51.06  ? 8   ASN A N   1 
ATOM   49   C  CA  . ASN A 1 8   ? -1.272  -26.269 -25.508 1.00 49.85  ? 8   ASN A CA  1 
ATOM   50   C  C   . ASN A 1 8   ? -1.234  -27.772 -25.785 1.00 49.56  ? 8   ASN A C   1 
ATOM   51   O  O   . ASN A 1 8   ? -1.275  -28.147 -26.962 1.00 50.41  ? 8   ASN A O   1 
ATOM   52   C  CB  . ASN A 1 8   ? -2.488  -25.588 -26.137 1.00 51.21  ? 8   ASN A CB  1 
ATOM   53   C  CG  . ASN A 1 8   ? -2.578  -24.129 -25.740 1.00 53.59  ? 8   ASN A CG  1 
ATOM   54   O  OD1 . ASN A 1 8   ? -1.891  -23.704 -24.818 1.00 59.54  ? 8   ASN A OD1 1 
ATOM   55   N  ND2 . ASN A 1 8   ? -3.409  -23.346 -26.412 1.00 55.11  ? 8   ASN A ND2 1 
ATOM   56   N  N   . PHE A 1 9   ? -1.161  -28.589 -24.729 1.00 52.41  ? 9   PHE A N   1 
ATOM   57   C  CA  . PHE A 1 9   ? -1.105  -30.075 -24.797 1.00 54.50  ? 9   PHE A CA  1 
ATOM   58   C  C   . PHE A 1 9   ? -2.226  -30.690 -23.953 1.00 51.98  ? 9   PHE A C   1 
ATOM   59   O  O   . PHE A 1 9   ? -2.344  -30.333 -22.780 1.00 55.69  ? 9   PHE A O   1 
ATOM   60   C  CB  . PHE A 1 9   ? 0.273   -30.578 -24.366 1.00 56.12  ? 9   PHE A CB  1 
ATOM   61   C  CG  . PHE A 1 9   ? 1.354   -30.226 -25.353 1.00 60.04  ? 9   PHE A CG  1 
ATOM   62   C  CD1 . PHE A 1 9   ? 1.881   -28.947 -25.385 1.00 63.52  ? 9   PHE A CD1 1 
ATOM   63   C  CD2 . PHE A 1 9   ? 1.808   -31.152 -26.280 1.00 61.19  ? 9   PHE A CD2 1 
ATOM   64   C  CE1 . PHE A 1 9   ? 2.861   -28.608 -26.306 1.00 65.55  ? 9   PHE A CE1 1 
ATOM   65   C  CE2 . PHE A 1 9   ? 2.796   -30.815 -27.194 1.00 61.41  ? 9   PHE A CE2 1 
ATOM   66   C  CZ  . PHE A 1 9   ? 3.318   -29.542 -27.210 1.00 62.38  ? 9   PHE A CZ  1 
ATOM   67   N  N   . VAL A 1 10  ? -3.006  -31.593 -24.556 1.00 50.36  ? 10  VAL A N   1 
ATOM   68   C  CA  . VAL A 1 10  ? -4.139  -32.332 -23.926 1.00 48.62  ? 10  VAL A CA  1 
ATOM   69   C  C   . VAL A 1 10  ? -3.732  -33.795 -23.754 1.00 46.94  ? 10  VAL A C   1 
ATOM   70   O  O   . VAL A 1 10  ? -3.788  -34.540 -24.745 1.00 46.44  ? 10  VAL A O   1 
ATOM   71   C  CB  . VAL A 1 10  ? -5.421  -32.224 -24.770 1.00 49.80  ? 10  VAL A CB  1 
ATOM   72   C  CG1 . VAL A 1 10  ? -6.599  -32.925 -24.102 1.00 51.47  ? 10  VAL A CG1 1 
ATOM   73   C  CG2 . VAL A 1 10  ? -5.755  -30.774 -25.076 1.00 50.05  ? 10  VAL A CG2 1 
ATOM   74   N  N   . ILE A 1 11  ? -3.360  -34.189 -22.539 1.00 48.15  ? 11  ILE A N   1 
ATOM   75   C  CA  . ILE A 1 11  ? -3.030  -35.604 -22.204 1.00 51.71  ? 11  ILE A CA  1 
ATOM   76   C  C   . ILE A 1 11  ? -4.286  -36.445 -22.433 1.00 55.61  ? 11  ILE A C   1 
ATOM   77   O  O   . ILE A 1 11  ? -5.352  -36.077 -21.925 1.00 55.12  ? 11  ILE A O   1 
ATOM   78   C  CB  . ILE A 1 11  ? -2.501  -35.754 -20.768 1.00 53.94  ? 11  ILE A CB  1 
ATOM   79   C  CG1 . ILE A 1 11  ? -1.301  -34.842 -20.493 1.00 55.07  ? 11  ILE A CG1 1 
ATOM   80   C  CG2 . ILE A 1 11  ? -2.173  -37.215 -20.489 1.00 54.61  ? 11  ILE A CG2 1 
ATOM   81   C  CD1 . ILE A 1 11  ? -1.135  -34.475 -19.040 1.00 55.90  ? 11  ILE A CD1 1 
ATOM   82   N  N   . SER A 1 12  ? -4.161  -37.523 -23.203 1.00 65.51  ? 12  SER A N   1 
ATOM   83   C  CA  . SER A 1 12  ? -5.295  -38.362 -23.666 1.00 68.75  ? 12  SER A CA  1 
ATOM   84   C  C   . SER A 1 12  ? -4.790  -39.771 -23.980 1.00 75.40  ? 12  SER A C   1 
ATOM   85   O  O   . SER A 1 12  ? -3.705  -39.900 -24.587 1.00 78.75  ? 12  SER A O   1 
ATOM   86   C  CB  . SER A 1 12  ? -5.954  -37.745 -24.864 1.00 65.93  ? 12  SER A CB  1 
ATOM   87   O  OG  . SER A 1 12  ? -7.005  -38.571 -25.339 1.00 66.45  ? 12  SER A OG  1 
ATOM   88   N  N   . ILE A 1 13  ? -5.562  -40.785 -23.592 1.00 81.39  ? 13  ILE A N   1 
ATOM   89   C  CA  . ILE A 1 13  ? -5.269  -42.202 -23.947 1.00 87.18  ? 13  ILE A CA  1 
ATOM   90   C  C   . ILE A 1 13  ? -5.577  -42.341 -25.445 1.00 90.87  ? 13  ILE A C   1 
ATOM   91   O  O   . ILE A 1 13  ? -6.709  -42.001 -25.833 1.00 92.89  ? 13  ILE A O   1 
ATOM   92   C  CB  . ILE A 1 13  ? -6.065  -43.193 -23.071 1.00 89.97  ? 13  ILE A CB  1 
ATOM   93   C  CG1 . ILE A 1 13  ? -6.244  -42.709 -21.624 1.00 91.03  ? 13  ILE A CG1 1 
ATOM   94   C  CG2 . ILE A 1 13  ? -5.399  -44.562 -23.129 1.00 91.10  ? 13  ILE A CG2 1 
ATOM   95   C  CD1 . ILE A 1 13  ? -7.691  -42.561 -21.186 1.00 90.13  ? 13  ILE A CD1 1 
ATOM   96   N  N   . SER A 1 14  ? -4.595  -42.767 -26.252 1.00 91.20  ? 14  SER A N   1 
ATOM   97   C  CA  . SER A 1 14  ? -4.612  -42.734 -27.743 1.00 90.70  ? 14  SER A CA  1 
ATOM   98   C  C   . SER A 1 14  ? -5.992  -43.110 -28.309 1.00 92.39  ? 14  SER A C   1 
ATOM   99   O  O   . SER A 1 14  ? -6.443  -42.428 -29.250 1.00 85.06  ? 14  SER A O   1 
ATOM   100  C  CB  . SER A 1 14  ? -3.516  -43.597 -28.326 1.00 88.29  ? 14  SER A CB  1 
ATOM   101  O  OG  . SER A 1 14  ? -3.499  -44.883 -27.728 1.00 90.39  ? 14  SER A OG  1 
ATOM   102  N  N   . THR A 1 15  ? -6.648  -44.139 -27.755 1.00 96.77  ? 15  THR A N   1 
ATOM   103  C  CA  . THR A 1 15  ? -7.900  -44.744 -28.299 1.00 96.69  ? 15  THR A CA  1 
ATOM   104  C  C   . THR A 1 15  ? -9.157  -44.150 -27.640 1.00 98.00  ? 15  THR A C   1 
ATOM   105  O  O   . THR A 1 15  ? -10.275 -44.555 -28.047 1.00 96.26  ? 15  THR A O   1 
ATOM   106  C  CB  . THR A 1 15  ? -7.865  -46.269 -28.155 1.00 95.17  ? 15  THR A CB  1 
ATOM   107  O  OG1 . THR A 1 15  ? -7.509  -46.557 -26.804 1.00 87.13  ? 15  THR A OG1 1 
ATOM   108  C  CG2 . THR A 1 15  ? -6.887  -46.925 -29.106 1.00 97.12  ? 15  THR A CG2 1 
ATOM   109  N  N   . ALA A 1 16  ? -9.012  -43.212 -26.695 1.00 98.24  ? 16  ALA A N   1 
ATOM   110  C  CA  . ALA A 1 16  ? -10.130 -42.518 -26.002 1.00 96.60  ? 16  ALA A CA  1 
ATOM   111  C  C   . ALA A 1 16  ? -10.938 -41.686 -27.009 1.00 93.53  ? 16  ALA A C   1 
ATOM   112  O  O   . ALA A 1 16  ? -11.081 -40.468 -26.803 1.00 86.56  ? 16  ALA A O   1 
ATOM   113  C  CB  . ALA A 1 16  ? -9.601  -41.664 -24.873 1.00 97.49  ? 16  ALA A CB  1 
ATOM   114  N  N   . GLU A 1 17  ? -11.470 -42.352 -28.038 1.00 93.90  ? 17  GLU A N   1 
ATOM   115  C  CA  . GLU A 1 17  ? -12.160 -41.752 -29.211 1.00 97.53  ? 17  GLU A CA  1 
ATOM   116  C  C   . GLU A 1 17  ? -13.140 -40.674 -28.734 1.00 98.12  ? 17  GLU A C   1 
ATOM   117  O  O   . GLU A 1 17  ? -12.978 -39.498 -29.137 1.00 94.70  ? 17  GLU A O   1 
ATOM   118  C  CB  . GLU A 1 17  ? -12.865 -42.876 -29.976 1.00 103.12 ? 17  GLU A CB  1 
ATOM   119  C  CG  . GLU A 1 17  ? -13.915 -42.427 -30.984 1.00 107.76 ? 17  GLU A CG  1 
ATOM   120  C  CD  . GLU A 1 17  ? -14.935 -43.504 -31.331 1.00 109.67 ? 17  GLU A CD  1 
ATOM   121  O  OE1 . GLU A 1 17  ? -15.471 -43.466 -32.457 1.00 108.70 ? 17  GLU A OE1 1 
ATOM   122  O  OE2 . GLU A 1 17  ? -15.202 -44.377 -30.473 1.00 109.67 ? 17  GLU A OE2 1 
ATOM   123  N  N   . GLN A 1 18  ? -14.105 -41.083 -27.904 1.00 102.52 ? 18  GLN A N   1 
ATOM   124  C  CA  . GLN A 1 18  ? -15.249 -40.253 -27.436 1.00 103.07 ? 18  GLN A CA  1 
ATOM   125  C  C   . GLN A 1 18  ? -14.731 -38.926 -26.867 1.00 98.59  ? 18  GLN A C   1 
ATOM   126  O  O   . GLN A 1 18  ? -15.213 -37.880 -27.341 1.00 92.51  ? 18  GLN A O   1 
ATOM   127  C  CB  . GLN A 1 18  ? -16.105 -41.035 -26.439 1.00 110.37 ? 18  GLN A CB  1 
ATOM   128  C  CG  . GLN A 1 18  ? -17.045 -42.023 -27.118 1.00 114.60 ? 18  GLN A CG  1 
ATOM   129  C  CD  . GLN A 1 18  ? -17.988 -42.712 -26.160 1.00 117.90 ? 18  GLN A CD  1 
ATOM   130  O  OE1 . GLN A 1 18  ? -17.967 -42.477 -24.953 1.00 110.01 ? 18  GLN A OE1 1 
ATOM   131  N  NE2 . GLN A 1 18  ? -18.834 -43.577 -26.698 1.00 122.96 ? 18  GLN A NE2 1 
ATOM   132  N  N   . ARG A 1 19  ? -13.796 -38.972 -25.907 1.00 93.54  ? 19  ARG A N   1 
ATOM   133  C  CA  . ARG A 1 19  ? -13.215 -37.774 -25.236 1.00 87.05  ? 19  ARG A CA  1 
ATOM   134  C  C   . ARG A 1 19  ? -12.563 -36.866 -26.283 1.00 81.55  ? 19  ARG A C   1 
ATOM   135  O  O   . ARG A 1 19  ? -12.931 -35.680 -26.358 1.00 77.32  ? 19  ARG A O   1 
ATOM   136  C  CB  . ARG A 1 19  ? -12.185 -38.169 -24.173 1.00 87.88  ? 19  ARG A CB  1 
ATOM   137  C  CG  . ARG A 1 19  ? -12.801 -38.535 -22.831 1.00 89.65  ? 19  ARG A CG  1 
ATOM   138  C  CD  . ARG A 1 19  ? -11.747 -38.859 -21.790 1.00 88.95  ? 19  ARG A CD  1 
ATOM   139  N  NE  . ARG A 1 19  ? -12.339 -39.245 -20.520 1.00 87.96  ? 19  ARG A NE  1 
ATOM   140  C  CZ  . ARG A 1 19  ? -11.655 -39.649 -19.454 1.00 91.36  ? 19  ARG A CZ  1 
ATOM   141  N  NH1 . ARG A 1 19  ? -10.333 -39.725 -19.497 1.00 92.91  ? 19  ARG A NH1 1 
ATOM   142  N  NH2 . ARG A 1 19  ? -12.301 -39.977 -18.348 1.00 93.19  ? 19  ARG A NH2 1 
ATOM   143  N  N   . ARG A 1 20  ? -11.640 -37.422 -27.068 1.00 78.01  ? 20  ARG A N   1 
ATOM   144  C  CA  . ARG A 1 20  ? -10.830 -36.669 -28.060 1.00 72.60  ? 20  ARG A CA  1 
ATOM   145  C  C   . ARG A 1 20  ? -11.763 -35.809 -28.922 1.00 67.89  ? 20  ARG A C   1 
ATOM   146  O  O   . ARG A 1 20  ? -11.491 -34.605 -29.057 1.00 59.00  ? 20  ARG A O   1 
ATOM   147  C  CB  . ARG A 1 20  ? -9.974  -37.647 -28.868 1.00 72.81  ? 20  ARG A CB  1 
ATOM   148  C  CG  . ARG A 1 20  ? -8.915  -38.355 -28.035 1.00 72.86  ? 20  ARG A CG  1 
ATOM   149  C  CD  . ARG A 1 20  ? -7.665  -38.678 -28.825 1.00 76.00  ? 20  ARG A CD  1 
ATOM   150  N  NE  . ARG A 1 20  ? -6.571  -39.100 -27.962 1.00 80.12  ? 20  ARG A NE  1 
ATOM   151  C  CZ  . ARG A 1 20  ? -5.276  -39.018 -28.268 1.00 85.03  ? 20  ARG A CZ  1 
ATOM   152  N  NH1 . ARG A 1 20  ? -4.888  -38.514 -29.429 1.00 85.04  ? 20  ARG A NH1 1 
ATOM   153  N  NH2 . ARG A 1 20  ? -4.368  -39.435 -27.402 1.00 88.74  ? 20  ARG A NH2 1 
ATOM   154  N  N   . ASN A 1 21  ? -12.846 -36.394 -29.438 1.00 71.84  ? 21  ASN A N   1 
ATOM   155  C  CA  . ASN A 1 21  ? -13.872 -35.673 -30.241 1.00 80.13  ? 21  ASN A CA  1 
ATOM   156  C  C   . ASN A 1 21  ? -14.423 -34.507 -29.412 1.00 81.07  ? 21  ASN A C   1 
ATOM   157  O  O   . ASN A 1 21  ? -14.402 -33.360 -29.909 1.00 79.01  ? 21  ASN A O   1 
ATOM   158  C  CB  . ASN A 1 21  ? -15.013 -36.591 -30.691 1.00 83.10  ? 21  ASN A CB  1 
ATOM   159  C  CG  . ASN A 1 21  ? -14.526 -37.849 -31.377 1.00 83.89  ? 21  ASN A CG  1 
ATOM   160  O  OD1 . ASN A 1 21  ? -13.694 -37.785 -32.278 1.00 81.26  ? 21  ASN A OD1 1 
ATOM   161  N  ND2 . ASN A 1 21  ? -15.040 -38.996 -30.964 1.00 86.63  ? 21  ASN A ND2 1 
ATOM   162  N  N   . HIS A 1 22  ? -14.899 -34.809 -28.199 1.00 78.06  ? 22  HIS A N   1 
ATOM   163  C  CA  . HIS A 1 22  ? -15.431 -33.835 -27.205 1.00 81.58  ? 22  HIS A CA  1 
ATOM   164  C  C   . HIS A 1 22  ? -14.441 -32.666 -27.094 1.00 75.67  ? 22  HIS A C   1 
ATOM   165  O  O   . HIS A 1 22  ? -14.875 -31.508 -27.236 1.00 73.14  ? 22  HIS A O   1 
ATOM   166  C  CB  . HIS A 1 22  ? -15.801 -34.599 -25.908 1.00 88.74  ? 22  HIS A CB  1 
ATOM   167  C  CG  . HIS A 1 22  ? -15.502 -33.976 -24.580 1.00 97.21  ? 22  HIS A CG  1 
ATOM   168  N  ND1 . HIS A 1 22  ? -16.049 -32.774 -24.175 1.00 100.33 ? 22  HIS A ND1 1 
ATOM   169  C  CD2 . HIS A 1 22  ? -14.804 -34.448 -23.516 1.00 97.22  ? 22  HIS A CD2 1 
ATOM   170  C  CE1 . HIS A 1 22  ? -15.653 -32.509 -22.944 1.00 97.73  ? 22  HIS A CE1 1 
ATOM   171  N  NE2 . HIS A 1 22  ? -14.882 -33.516 -22.519 1.00 92.06  ? 22  HIS A NE2 1 
ATOM   172  N  N   . ILE A 1 23  ? -13.153 -32.972 -26.929 1.00 71.55  ? 23  ILE A N   1 
ATOM   173  C  CA  . ILE A 1 23  ? -12.050 -31.971 -26.814 1.00 71.47  ? 23  ILE A CA  1 
ATOM   174  C  C   . ILE A 1 23  ? -11.979 -31.153 -28.109 1.00 69.55  ? 23  ILE A C   1 
ATOM   175  O  O   . ILE A 1 23  ? -12.139 -29.914 -28.055 1.00 62.09  ? 23  ILE A O   1 
ATOM   176  C  CB  . ILE A 1 23  ? -10.715 -32.680 -26.510 1.00 72.56  ? 23  ILE A CB  1 
ATOM   177  C  CG1 . ILE A 1 23  ? -10.723 -33.340 -25.127 1.00 72.34  ? 23  ILE A CG1 1 
ATOM   178  C  CG2 . ILE A 1 23  ? -9.545  -31.723 -26.676 1.00 73.26  ? 23  ILE A CG2 1 
ATOM   179  C  CD1 . ILE A 1 23  ? -10.980 -32.385 -23.977 1.00 74.86  ? 23  ILE A CD1 1 
ATOM   180  N  N   . ILE A 1 24  ? -11.741 -31.832 -29.230 1.00 70.37  ? 24  ILE A N   1 
ATOM   181  C  CA  . ILE A 1 24  ? -11.551 -31.204 -30.571 1.00 70.67  ? 24  ILE A CA  1 
ATOM   182  C  C   . ILE A 1 24  ? -12.640 -30.150 -30.787 1.00 72.53  ? 24  ILE A C   1 
ATOM   183  O  O   . ILE A 1 24  ? -12.284 -28.993 -31.093 1.00 70.09  ? 24  ILE A O   1 
ATOM   184  C  CB  . ILE A 1 24  ? -11.544 -32.273 -31.676 1.00 68.92  ? 24  ILE A CB  1 
ATOM   185  C  CG1 . ILE A 1 24  ? -10.262 -33.106 -31.626 1.00 69.79  ? 24  ILE A CG1 1 
ATOM   186  C  CG2 . ILE A 1 24  ? -11.747 -31.644 -33.044 1.00 67.74  ? 24  ILE A CG2 1 
ATOM   187  C  CD1 . ILE A 1 24  ? -10.418 -34.492 -32.203 1.00 71.36  ? 24  ILE A CD1 1 
ATOM   188  N  N   . GLU A 1 25  ? -13.908 -30.532 -30.607 1.00 77.20  ? 25  GLU A N   1 
ATOM   189  C  CA  . GLU A 1 25  ? -15.079 -29.638 -30.816 1.00 85.68  ? 25  GLU A CA  1 
ATOM   190  C  C   . GLU A 1 25  ? -14.875 -28.328 -30.040 1.00 87.13  ? 25  GLU A C   1 
ATOM   191  O  O   . GLU A 1 25  ? -15.198 -27.264 -30.605 1.00 77.24  ? 25  GLU A O   1 
ATOM   192  C  CB  . GLU A 1 25  ? -16.392 -30.313 -30.398 1.00 94.07  ? 25  GLU A CB  1 
ATOM   193  C  CG  . GLU A 1 25  ? -17.600 -29.770 -31.161 1.00 102.08 ? 25  GLU A CG  1 
ATOM   194  C  CD  . GLU A 1 25  ? -18.970 -29.907 -30.504 1.00 105.81 ? 25  GLU A CD  1 
ATOM   195  O  OE1 . GLU A 1 25  ? -19.077 -29.619 -29.291 1.00 102.83 ? 25  GLU A OE1 1 
ATOM   196  O  OE2 . GLU A 1 25  ? -19.937 -30.278 -31.215 1.00 101.59 ? 25  GLU A OE2 1 
ATOM   197  N  N   . GLN A 1 26  ? -14.359 -28.409 -28.804 1.00 87.71  ? 26  GLN A N   1 
ATOM   198  C  CA  . GLN A 1 26  ? -14.237 -27.264 -27.858 1.00 86.15  ? 26  GLN A CA  1 
ATOM   199  C  C   . GLN A 1 26  ? -13.125 -26.315 -28.308 1.00 84.87  ? 26  GLN A C   1 
ATOM   200  O  O   . GLN A 1 26  ? -13.397 -25.101 -28.448 1.00 86.76  ? 26  GLN A O   1 
ATOM   201  C  CB  . GLN A 1 26  ? -13.899 -27.733 -26.443 1.00 86.91  ? 26  GLN A CB  1 
ATOM   202  C  CG  . GLN A 1 26  ? -14.962 -28.596 -25.784 1.00 89.79  ? 26  GLN A CG  1 
ATOM   203  C  CD  . GLN A 1 26  ? -14.655 -28.775 -24.318 1.00 88.87  ? 26  GLN A CD  1 
ATOM   204  O  OE1 . GLN A 1 26  ? -14.697 -27.817 -23.552 1.00 94.23  ? 26  GLN A OE1 1 
ATOM   205  N  NE2 . GLN A 1 26  ? -14.326 -29.993 -23.915 1.00 84.80  ? 26  GLN A NE2 1 
ATOM   206  N  N   . PHE A 1 27  ? -11.911 -26.844 -28.473 1.00 83.02  ? 27  PHE A N   1 
ATOM   207  C  CA  . PHE A 1 27  ? -10.694 -26.054 -28.788 1.00 86.05  ? 27  PHE A CA  1 
ATOM   208  C  C   . PHE A 1 27  ? -10.880 -25.379 -30.147 1.00 87.71  ? 27  PHE A C   1 
ATOM   209  O  O   . PHE A 1 27  ? -10.566 -24.171 -30.279 1.00 90.96  ? 27  PHE A O   1 
ATOM   210  C  CB  . PHE A 1 27  ? -9.452  -26.945 -28.736 1.00 84.85  ? 27  PHE A CB  1 
ATOM   211  C  CG  . PHE A 1 27  ? -8.858  -27.048 -27.355 1.00 78.78  ? 27  PHE A CG  1 
ATOM   212  C  CD1 . PHE A 1 27  ? -7.970  -26.086 -26.903 1.00 73.66  ? 27  PHE A CD1 1 
ATOM   213  C  CD2 . PHE A 1 27  ? -9.210  -28.080 -26.500 1.00 74.06  ? 27  PHE A CD2 1 
ATOM   214  C  CE1 . PHE A 1 27  ? -7.427  -26.166 -25.632 1.00 70.01  ? 27  PHE A CE1 1 
ATOM   215  C  CE2 . PHE A 1 27  ? -8.668  -28.156 -25.228 1.00 70.55  ? 27  PHE A CE2 1 
ATOM   216  C  CZ  . PHE A 1 27  ? -7.777  -27.199 -24.798 1.00 69.76  ? 27  PHE A CZ  1 
ATOM   217  N  N   . THR A 1 28  ? -11.391 -26.148 -31.110 1.00 85.16  ? 28  THR A N   1 
ATOM   218  C  CA  . THR A 1 28  ? -11.794 -25.670 -32.454 1.00 82.96  ? 28  THR A CA  1 
ATOM   219  C  C   . THR A 1 28  ? -12.757 -24.490 -32.284 1.00 82.96  ? 28  THR A C   1 
ATOM   220  O  O   . THR A 1 28  ? -12.377 -23.372 -32.666 1.00 79.14  ? 28  THR A O   1 
ATOM   221  C  CB  . THR A 1 28  ? -12.393 -26.818 -33.275 1.00 79.59  ? 28  THR A CB  1 
ATOM   222  O  OG1 . THR A 1 28  ? -11.467 -27.904 -33.214 1.00 73.58  ? 28  THR A OG1 1 
ATOM   223  C  CG2 . THR A 1 28  ? -12.668 -26.443 -34.713 1.00 80.82  ? 28  THR A CG2 1 
ATOM   224  N  N   . HIS A 1 29  ? -13.922 -24.730 -31.672 1.00 85.57  ? 29  HIS A N   1 
ATOM   225  C  CA  . HIS A 1 29  ? -15.047 -23.761 -31.559 1.00 85.29  ? 29  HIS A CA  1 
ATOM   226  C  C   . HIS A 1 29  ? -14.559 -22.404 -31.033 1.00 80.70  ? 29  HIS A C   1 
ATOM   227  O  O   . HIS A 1 29  ? -15.155 -21.390 -31.428 1.00 78.77  ? 29  HIS A O   1 
ATOM   228  C  CB  . HIS A 1 29  ? -16.200 -24.352 -30.731 1.00 87.29  ? 29  HIS A CB  1 
ATOM   229  C  CG  . HIS A 1 29  ? -17.221 -25.022 -31.588 1.00 91.94  ? 29  HIS A CG  1 
ATOM   230  N  ND1 . HIS A 1 29  ? -17.081 -26.325 -32.023 1.00 95.61  ? 29  HIS A ND1 1 
ATOM   231  C  CD2 . HIS A 1 29  ? -18.358 -24.555 -32.149 1.00 97.27  ? 29  HIS A CD2 1 
ATOM   232  C  CE1 . HIS A 1 29  ? -18.100 -26.642 -32.795 1.00 100.19 ? 29  HIS A CE1 1 
ATOM   233  N  NE2 . HIS A 1 29  ? -18.898 -25.572 -32.889 1.00 102.85 ? 29  HIS A NE2 1 
ATOM   234  N  N   . GLN A 1 30  ? -13.522 -22.378 -30.191 1.00 80.56  ? 30  GLN A N   1 
ATOM   235  C  CA  . GLN A 1 30  ? -12.954 -21.124 -29.620 1.00 79.79  ? 30  GLN A CA  1 
ATOM   236  C  C   . GLN A 1 30  ? -11.646 -20.766 -30.333 1.00 83.51  ? 30  GLN A C   1 
ATOM   237  O  O   . GLN A 1 30  ? -10.986 -19.814 -29.890 1.00 83.99  ? 30  GLN A O   1 
ATOM   238  C  CB  . GLN A 1 30  ? -12.744 -21.261 -28.111 1.00 76.58  ? 30  GLN A CB  1 
ATOM   239  C  CG  . GLN A 1 30  ? -13.996 -20.957 -27.304 1.00 74.68  ? 30  GLN A CG  1 
ATOM   240  C  CD  . GLN A 1 30  ? -13.697 -20.742 -25.844 1.00 71.72  ? 30  GLN A CD  1 
ATOM   241  O  OE1 . GLN A 1 30  ? -13.325 -19.650 -25.413 1.00 68.62  ? 30  GLN A OE1 1 
ATOM   242  N  NE2 . GLN A 1 30  ? -13.841 -21.804 -25.068 1.00 74.46  ? 30  GLN A NE2 1 
ATOM   243  N  N   . ASN A 1 31  ? -11.293 -21.492 -31.397 1.00 85.04  ? 31  ASN A N   1 
ATOM   244  C  CA  . ASN A 1 31  ? -10.140 -21.165 -32.276 1.00 85.49  ? 31  ASN A CA  1 
ATOM   245  C  C   . ASN A 1 31  ? -8.880  -21.138 -31.408 1.00 80.40  ? 31  ASN A C   1 
ATOM   246  O  O   . ASN A 1 31  ? -8.264  -20.054 -31.263 1.00 76.35  ? 31  ASN A O   1 
ATOM   247  C  CB  . ASN A 1 31  ? -10.364 -19.845 -33.024 1.00 93.59  ? 31  ASN A CB  1 
ATOM   248  C  CG  . ASN A 1 31  ? -11.590 -19.851 -33.917 1.00 100.84 ? 31  ASN A CG  1 
ATOM   249  O  OD1 . ASN A 1 31  ? -12.048 -20.908 -34.349 1.00 107.02 ? 31  ASN A OD1 1 
ATOM   250  N  ND2 . ASN A 1 31  ? -12.126 -18.675 -34.213 1.00 102.01 ? 31  ASN A ND2 1 
ATOM   251  N  N   . ILE A 1 32  ? -8.554  -22.285 -30.810 1.00 77.74  ? 32  ILE A N   1 
ATOM   252  C  CA  . ILE A 1 32  ? -7.390  -22.451 -29.896 1.00 76.56  ? 32  ILE A CA  1 
ATOM   253  C  C   . ILE A 1 32  ? -6.516  -23.570 -30.447 1.00 73.39  ? 32  ILE A C   1 
ATOM   254  O  O   . ILE A 1 32  ? -6.924  -24.728 -30.495 1.00 67.68  ? 32  ILE A O   1 
ATOM   255  C  CB  . ILE A 1 32  ? -7.842  -22.710 -28.445 1.00 76.62  ? 32  ILE A CB  1 
ATOM   256  C  CG1 . ILE A 1 32  ? -8.829  -21.638 -27.978 1.00 80.48  ? 32  ILE A CG1 1 
ATOM   257  C  CG2 . ILE A 1 32  ? -6.637  -22.798 -27.519 1.00 74.58  ? 32  ILE A CG2 1 
ATOM   258  C  CD1 . ILE A 1 32  ? -9.422  -21.880 -26.619 1.00 80.07  ? 32  ILE A CD1 1 
ATOM   259  N  N   . PRO A 1 33  ? -5.281  -23.248 -30.885 1.00 70.61  ? 33  PRO A N   1 
ATOM   260  C  CA  . PRO A 1 33  ? -4.372  -24.258 -31.412 1.00 66.81  ? 33  PRO A CA  1 
ATOM   261  C  C   . PRO A 1 33  ? -3.876  -25.142 -30.265 1.00 63.33  ? 33  PRO A C   1 
ATOM   262  O  O   . PRO A 1 33  ? -3.621  -24.619 -29.201 1.00 63.42  ? 33  PRO A O   1 
ATOM   263  C  CB  . PRO A 1 33  ? -3.225  -23.436 -32.008 1.00 71.19  ? 33  PRO A CB  1 
ATOM   264  C  CG  . PRO A 1 33  ? -3.221  -22.158 -31.186 1.00 72.25  ? 33  PRO A CG  1 
ATOM   265  C  CD  . PRO A 1 33  ? -4.673  -21.909 -30.833 1.00 71.70  ? 33  PRO A CD  1 
ATOM   266  N  N   . PHE A 1 34  ? -3.752  -26.444 -30.506 1.00 59.39  ? 34  PHE A N   1 
ATOM   267  C  CA  . PHE A 1 34  ? -3.312  -27.429 -29.486 1.00 58.15  ? 34  PHE A CA  1 
ATOM   268  C  C   . PHE A 1 34  ? -2.775  -28.693 -30.160 1.00 57.00  ? 34  PHE A C   1 
ATOM   269  O  O   . PHE A 1 34  ? -2.871  -28.827 -31.385 1.00 57.80  ? 34  PHE A O   1 
ATOM   270  C  CB  . PHE A 1 34  ? -4.481  -27.793 -28.570 1.00 57.69  ? 34  PHE A CB  1 
ATOM   271  C  CG  . PHE A 1 34  ? -5.421  -28.813 -29.163 1.00 58.14  ? 34  PHE A CG  1 
ATOM   272  C  CD1 . PHE A 1 34  ? -6.465  -28.426 -29.990 1.00 58.30  ? 34  PHE A CD1 1 
ATOM   273  C  CD2 . PHE A 1 34  ? -5.239  -30.168 -28.920 1.00 57.75  ? 34  PHE A CD2 1 
ATOM   274  C  CE1 . PHE A 1 34  ? -7.319  -29.371 -30.542 1.00 57.81  ? 34  PHE A CE1 1 
ATOM   275  C  CE2 . PHE A 1 34  ? -6.099  -31.112 -29.465 1.00 57.42  ? 34  PHE A CE2 1 
ATOM   276  C  CZ  . PHE A 1 34  ? -7.137  -30.712 -30.279 1.00 57.34  ? 34  PHE A CZ  1 
ATOM   277  N  N   . GLU A 1 35  ? -2.248  -29.607 -29.349 1.00 57.95  ? 35  GLU A N   1 
ATOM   278  C  CA  . GLU A 1 35  ? -1.856  -30.980 -29.752 1.00 58.79  ? 35  GLU A CA  1 
ATOM   279  C  C   . GLU A 1 35  ? -2.289  -31.939 -28.647 1.00 55.71  ? 35  GLU A C   1 
ATOM   280  O  O   . GLU A 1 35  ? -2.298  -31.507 -27.489 1.00 54.64  ? 35  GLU A O   1 
ATOM   281  C  CB  . GLU A 1 35  ? -0.345  -31.060 -29.957 1.00 63.64  ? 35  GLU A CB  1 
ATOM   282  C  CG  . GLU A 1 35  ? 0.123   -32.388 -30.530 1.00 67.18  ? 35  GLU A CG  1 
ATOM   283  C  CD  . GLU A 1 35  ? 0.512   -32.324 -31.995 1.00 69.59  ? 35  GLU A CD  1 
ATOM   284  O  OE1 . GLU A 1 35  ? 1.354   -31.460 -32.331 1.00 71.18  ? 35  GLU A OE1 1 
ATOM   285  O  OE2 . GLU A 1 35  ? -0.032  -33.128 -32.792 1.00 69.41  ? 35  GLU A OE2 1 
ATOM   286  N  N   . PHE A 1 36  ? -2.639  -33.180 -28.992 1.00 56.92  ? 36  PHE A N   1 
ATOM   287  C  CA  . PHE A 1 36  ? -2.854  -34.278 -28.014 1.00 60.38  ? 36  PHE A CA  1 
ATOM   288  C  C   . PHE A 1 36  ? -1.493  -34.770 -27.518 1.00 60.44  ? 36  PHE A C   1 
ATOM   289  O  O   . PHE A 1 36  ? -0.461  -34.286 -28.010 1.00 67.50  ? 36  PHE A O   1 
ATOM   290  C  CB  . PHE A 1 36  ? -3.671  -35.421 -28.624 1.00 60.59  ? 36  PHE A CB  1 
ATOM   291  C  CG  . PHE A 1 36  ? -5.158  -35.176 -28.634 1.00 62.29  ? 36  PHE A CG  1 
ATOM   292  C  CD1 . PHE A 1 36  ? -5.892  -35.205 -27.454 1.00 64.77  ? 36  PHE A CD1 1 
ATOM   293  C  CD2 . PHE A 1 36  ? -5.822  -34.906 -29.818 1.00 60.45  ? 36  PHE A CD2 1 
ATOM   294  C  CE1 . PHE A 1 36  ? -7.262  -34.982 -27.465 1.00 64.58  ? 36  PHE A CE1 1 
ATOM   295  C  CE2 . PHE A 1 36  ? -7.188  -34.678 -29.827 1.00 62.18  ? 36  PHE A CE2 1 
ATOM   296  C  CZ  . PHE A 1 36  ? -7.905  -34.716 -28.653 1.00 66.84  ? 36  PHE A CZ  1 
ATOM   297  N  N   . PHE A 1 37  ? -1.508  -35.694 -26.561 1.00 59.14  ? 37  PHE A N   1 
ATOM   298  C  CA  . PHE A 1 37  ? -0.327  -36.455 -26.086 1.00 61.55  ? 37  PHE A CA  1 
ATOM   299  C  C   . PHE A 1 37  ? -0.805  -37.828 -25.613 1.00 65.91  ? 37  PHE A C   1 
ATOM   300  O  O   . PHE A 1 37  ? -1.682  -37.880 -24.737 1.00 66.67  ? 37  PHE A O   1 
ATOM   301  C  CB  . PHE A 1 37  ? 0.390   -35.689 -24.977 1.00 61.77  ? 37  PHE A CB  1 
ATOM   302  C  CG  . PHE A 1 37  ? 1.575   -36.398 -24.372 1.00 63.50  ? 37  PHE A CG  1 
ATOM   303  C  CD1 . PHE A 1 37  ? 1.446   -37.617 -23.721 1.00 65.94  ? 37  PHE A CD1 1 
ATOM   304  C  CD2 . PHE A 1 37  ? 2.833   -35.818 -24.421 1.00 63.42  ? 37  PHE A CD2 1 
ATOM   305  C  CE1 . PHE A 1 37  ? 2.545   -38.246 -23.157 1.00 66.18  ? 37  PHE A CE1 1 
ATOM   306  C  CE2 . PHE A 1 37  ? 3.930   -36.443 -23.849 1.00 63.73  ? 37  PHE A CE2 1 
ATOM   307  C  CZ  . PHE A 1 37  ? 3.784   -37.656 -23.218 1.00 64.83  ? 37  PHE A CZ  1 
ATOM   308  N  N   . ASP A 1 38  ? -0.259  -38.900 -26.189 1.00 73.58  ? 38  ASP A N   1 
ATOM   309  C  CA  . ASP A 1 38  ? -0.653  -40.300 -25.879 1.00 79.55  ? 38  ASP A CA  1 
ATOM   310  C  C   . ASP A 1 38  ? -0.284  -40.587 -24.422 1.00 79.30  ? 38  ASP A C   1 
ATOM   311  O  O   . ASP A 1 38  ? 0.923   -40.661 -24.125 1.00 79.20  ? 38  ASP A O   1 
ATOM   312  C  CB  . ASP A 1 38  ? 0.001   -41.296 -26.840 1.00 84.97  ? 38  ASP A CB  1 
ATOM   313  C  CG  . ASP A 1 38  ? -0.346  -41.062 -28.300 1.00 89.77  ? 38  ASP A CG  1 
ATOM   314  O  OD1 . ASP A 1 38  ? -1.287  -40.287 -28.560 1.00 96.56  ? 38  ASP A OD1 1 
ATOM   315  O  OD2 . ASP A 1 38  ? 0.334   -41.650 -29.164 1.00 95.53  ? 38  ASP A OD2 1 
ATOM   316  N  N   . ALA A 1 39  ? -1.287  -40.713 -23.550 1.00 79.29  ? 39  ALA A N   1 
ATOM   317  C  CA  . ALA A 1 39  ? -1.113  -40.917 -22.094 1.00 81.98  ? 39  ALA A CA  1 
ATOM   318  C  C   . ALA A 1 39  ? -0.572  -42.328 -21.848 1.00 81.26  ? 39  ALA A C   1 
ATOM   319  O  O   . ALA A 1 39  ? -1.161  -43.280 -22.389 1.00 79.71  ? 39  ALA A O   1 
ATOM   320  C  CB  . ALA A 1 39  ? -2.426  -40.684 -21.389 1.00 86.19  ? 39  ALA A CB  1 
ATOM   321  N  N   . PHE A 1 40  ? 0.517   -42.441 -21.082 1.00 85.86  ? 40  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 40  ? 1.186   -43.725 -20.749 1.00 95.39  ? 40  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 40  ? 0.195   -44.648 -20.031 1.00 98.93  ? 40  PHE A C   1 
ATOM   324  O  O   . PHE A 1 40  ? -0.455  -44.185 -19.073 1.00 104.34 ? 40  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 40  ? 2.407   -43.492 -19.859 1.00 100.31 ? 40  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 40  ? 3.560   -42.780 -20.516 1.00 107.57 ? 40  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 40  ? 4.477   -43.476 -21.289 1.00 111.13 ? 40  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 40  ? 3.741   -41.417 -20.348 1.00 111.90 ? 40  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 40  ? 5.553   -42.826 -21.877 1.00 112.77 ? 40  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 40  ? 4.814   -40.766 -20.943 1.00 113.52 ? 40  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 40  ? 5.716   -41.471 -21.706 1.00 112.63 ? 40  PHE A CZ  1 
ATOM   332  N  N   . THR A 1 41  ? 0.097   -45.905 -20.480 1.00 101.93 ? 41  THR A N   1 
ATOM   333  C  CA  . THR A 1 41  ? -0.731  -46.983 -19.872 1.00 104.82 ? 41  THR A CA  1 
ATOM   334  C  C   . THR A 1 41  ? 0.186   -48.127 -19.441 1.00 117.80 ? 41  THR A C   1 
ATOM   335  O  O   . THR A 1 41  ? 1.269   -48.288 -20.003 1.00 122.41 ? 41  THR A O   1 
ATOM   336  C  CB  . THR A 1 41  ? -1.826  -47.457 -20.840 1.00 95.48  ? 41  THR A CB  1 
ATOM   337  O  OG1 . THR A 1 41  ? -1.238  -48.293 -21.839 1.00 90.37  ? 41  THR A OG1 1 
ATOM   338  C  CG2 . THR A 1 41  ? -2.562  -46.312 -21.502 1.00 91.72  ? 41  THR A CG2 1 
ATOM   339  N  N   . PRO A 1 42  ? -0.196  -48.935 -18.419 1.00 129.64 ? 42  PRO A N   1 
ATOM   340  C  CA  . PRO A 1 42  ? 0.554   -50.140 -18.064 1.00 129.37 ? 42  PRO A CA  1 
ATOM   341  C  C   . PRO A 1 42  ? 0.912   -50.931 -19.332 1.00 127.42 ? 42  PRO A C   1 
ATOM   342  O  O   . PRO A 1 42  ? 0.041   -51.565 -19.901 1.00 127.18 ? 42  PRO A O   1 
ATOM   343  C  CB  . PRO A 1 42  ? -0.371  -50.948 -17.136 1.00 131.02 ? 42  PRO A CB  1 
ATOM   344  C  CG  . PRO A 1 42  ? -1.525  -50.023 -16.783 1.00 131.92 ? 42  PRO A CG  1 
ATOM   345  C  CD  . PRO A 1 42  ? -1.344  -48.716 -17.529 1.00 132.08 ? 42  PRO A CD  1 
ATOM   346  N  N   . SER A 1 43  ? 2.172   -50.835 -19.765 1.00 120.12 ? 43  SER A N   1 
ATOM   347  C  CA  . SER A 1 43  ? 2.682   -51.424 -21.030 1.00 111.85 ? 43  SER A CA  1 
ATOM   348  C  C   . SER A 1 43  ? 4.212   -51.433 -21.021 1.00 109.18 ? 43  SER A C   1 
ATOM   349  O  O   . SER A 1 43  ? 4.801   -50.856 -20.092 1.00 99.48  ? 43  SER A O   1 
ATOM   350  C  CB  . SER A 1 43  ? 2.157   -50.667 -22.222 1.00 110.14 ? 43  SER A CB  1 
ATOM   351  O  OG  . SER A 1 43  ? 2.677   -49.344 -22.242 1.00 109.12 ? 43  SER A OG  1 
ATOM   352  N  N   . ASP A 1 44  ? 4.809   -52.075 -22.028 1.00 113.94 ? 44  ASP A N   1 
ATOM   353  C  CA  . ASP A 1 44  ? 6.273   -52.075 -22.296 1.00 116.75 ? 44  ASP A CA  1 
ATOM   354  C  C   . ASP A 1 44  ? 6.780   -50.625 -22.271 1.00 121.60 ? 44  ASP A C   1 
ATOM   355  O  O   . ASP A 1 44  ? 7.569   -50.295 -21.357 1.00 117.63 ? 44  ASP A O   1 
ATOM   356  C  CB  . ASP A 1 44  ? 6.591   -52.791 -23.616 1.00 114.17 ? 44  ASP A CB  1 
ATOM   357  C  CG  . ASP A 1 44  ? 5.492   -52.685 -24.665 1.00 113.46 ? 44  ASP A CG  1 
ATOM   358  O  OD1 . ASP A 1 44  ? 5.046   -51.554 -24.938 1.00 115.61 ? 44  ASP A OD1 1 
ATOM   359  O  OD2 . ASP A 1 44  ? 5.068   -53.737 -25.181 1.00 107.74 ? 44  ASP A OD2 1 
ATOM   360  N  N   . LYS A 1 45  ? 6.281   -49.781 -23.186 1.00 125.53 ? 45  LYS A N   1 
ATOM   361  C  CA  . LYS A 1 45  ? 6.817   -48.411 -23.429 1.00 121.48 ? 45  LYS A CA  1 
ATOM   362  C  C   . LYS A 1 45  ? 6.728   -47.572 -22.144 1.00 120.09 ? 45  LYS A C   1 
ATOM   363  O  O   . LYS A 1 45  ? 7.624   -46.727 -21.951 1.00 114.64 ? 45  LYS A O   1 
ATOM   364  C  CB  . LYS A 1 45  ? 6.159   -47.724 -24.632 1.00 119.58 ? 45  LYS A CB  1 
ATOM   365  C  CG  . LYS A 1 45  ? 6.960   -46.538 -25.164 1.00 120.76 ? 45  LYS A CG  1 
ATOM   366  C  CD  . LYS A 1 45  ? 7.216   -46.539 -26.665 1.00 119.61 ? 45  LYS A CD  1 
ATOM   367  C  CE  . LYS A 1 45  ? 8.407   -45.684 -27.052 1.00 118.80 ? 45  LYS A CE  1 
ATOM   368  N  NZ  . LYS A 1 45  ? 8.445   -45.426 -28.510 1.00 118.15 ? 45  LYS A NZ  1 
ATOM   369  N  N   . LEU A 1 46  ? 5.725   -47.799 -21.284 1.00 116.31 ? 46  LEU A N   1 
ATOM   370  C  CA  . LEU A 1 46  ? 5.636   -47.126 -19.956 1.00 111.77 ? 46  LEU A CA  1 
ATOM   371  C  C   . LEU A 1 46  ? 6.794   -47.611 -19.078 1.00 108.32 ? 46  LEU A C   1 
ATOM   372  O  O   . LEU A 1 46  ? 7.708   -46.802 -18.793 1.00 103.61 ? 46  LEU A O   1 
ATOM   373  C  CB  . LEU A 1 46  ? 4.282   -47.406 -19.291 1.00 108.92 ? 46  LEU A CB  1 
ATOM   374  C  CG  . LEU A 1 46  ? 4.206   -47.103 -17.791 1.00 105.74 ? 46  LEU A CG  1 
ATOM   375  C  CD1 . LEU A 1 46  ? 4.678   -45.690 -17.475 1.00 104.24 ? 46  LEU A CD1 1 
ATOM   376  C  CD2 . LEU A 1 46  ? 2.803   -47.316 -17.254 1.00 104.21 ? 46  LEU A CD2 1 
ATOM   377  N  N   . THR A 1 47  ? 6.738   -48.884 -18.674 1.00 109.09 ? 47  THR A N   1 
ATOM   378  C  CA  . THR A 1 47  ? 7.719   -49.551 -17.779 1.00 108.63 ? 47  THR A CA  1 
ATOM   379  C  C   . THR A 1 47  ? 9.137   -49.193 -18.242 1.00 111.17 ? 47  THR A C   1 
ATOM   380  O  O   . THR A 1 47  ? 9.981   -48.930 -17.362 1.00 102.02 ? 47  THR A O   1 
ATOM   381  C  CB  . THR A 1 47  ? 7.451   -51.063 -17.712 1.00 105.24 ? 47  THR A CB  1 
ATOM   382  O  OG1 . THR A 1 47  ? 6.779   -51.450 -18.909 1.00 104.20 ? 47  THR A OG1 1 
ATOM   383  C  CG2 . THR A 1 47  ? 6.597   -51.477 -16.537 1.00 102.50 ? 47  THR A CG2 1 
ATOM   384  N  N   . ASP A 1 48  ? 9.372   -49.156 -19.562 1.00 117.10 ? 48  ASP A N   1 
ATOM   385  C  CA  . ASP A 1 48  ? 10.627  -48.649 -20.185 1.00 121.11 ? 48  ASP A CA  1 
ATOM   386  C  C   . ASP A 1 48  ? 11.034  -47.343 -19.487 1.00 116.47 ? 48  ASP A C   1 
ATOM   387  O  O   . ASP A 1 48  ? 12.005  -47.350 -18.688 1.00 110.54 ? 48  ASP A O   1 
ATOM   388  C  CB  . ASP A 1 48  ? 10.462  -48.367 -21.685 1.00 126.57 ? 48  ASP A CB  1 
ATOM   389  C  CG  . ASP A 1 48  ? 10.404  -49.580 -22.605 1.00 126.31 ? 48  ASP A CG  1 
ATOM   390  O  OD1 . ASP A 1 48  ? 10.250  -50.709 -22.101 1.00 127.30 ? 48  ASP A OD1 1 
ATOM   391  O  OD2 . ASP A 1 48  ? 10.514  -49.379 -23.836 1.00 121.44 ? 48  ASP A OD2 1 
ATOM   392  N  N   . HIS A 1 49  ? 10.276  -46.276 -19.757 1.00 110.73 ? 49  HIS A N   1 
ATOM   393  C  CA  . HIS A 1 49  ? 10.584  -44.876 -19.365 1.00 104.70 ? 49  HIS A CA  1 
ATOM   394  C  C   . HIS A 1 49  ? 10.674  -44.778 -17.833 1.00 103.95 ? 49  HIS A C   1 
ATOM   395  O  O   . HIS A 1 49  ? 11.470  -43.945 -17.342 1.00 103.26 ? 49  HIS A O   1 
ATOM   396  C  CB  . HIS A 1 49  ? 9.534   -43.925 -19.965 1.00 100.30 ? 49  HIS A CB  1 
ATOM   397  C  CG  . HIS A 1 49  ? 9.573   -43.793 -21.454 1.00 93.82  ? 49  HIS A CG  1 
ATOM   398  N  ND1 . HIS A 1 49  ? 9.249   -44.831 -22.303 1.00 90.40  ? 49  HIS A ND1 1 
ATOM   399  C  CD2 . HIS A 1 49  ? 9.876   -42.746 -22.253 1.00 91.51  ? 49  HIS A CD2 1 
ATOM   400  C  CE1 . HIS A 1 49  ? 9.362   -44.431 -23.556 1.00 92.09  ? 49  HIS A CE1 1 
ATOM   401  N  NE2 . HIS A 1 49  ? 9.744   -43.157 -23.551 1.00 92.14  ? 49  HIS A NE2 1 
ATOM   402  N  N   . LEU A 1 50  ? 9.888   -45.594 -17.113 1.00 106.75 ? 50  LEU A N   1 
ATOM   403  C  CA  . LEU A 1 50  ? 9.827   -45.612 -15.623 1.00 113.06 ? 50  LEU A CA  1 
ATOM   404  C  C   . LEU A 1 50  ? 11.235  -45.797 -15.050 1.00 112.78 ? 50  LEU A C   1 
ATOM   405  O  O   . LEU A 1 50  ? 11.778  -44.816 -14.518 1.00 101.67 ? 50  LEU A O   1 
ATOM   406  C  CB  . LEU A 1 50  ? 8.875   -46.714 -15.139 1.00 117.88 ? 50  LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 50  ? 7.423   -46.292 -14.915 1.00 119.62 ? 50  LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 50  ? 6.545   -47.505 -14.644 1.00 119.49 ? 50  LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 50  ? 7.303   -45.295 -13.766 1.00 121.45 ? 50  LEU A CD2 1 
ATOM   410  N  N   . GLN A 1 51  ? 11.808  -46.996 -15.186 1.00 119.47 ? 51  GLN A N   1 
ATOM   411  C  CA  . GLN A 1 51  ? 13.139  -47.344 -14.615 1.00 124.09 ? 51  GLN A CA  1 
ATOM   412  C  C   . GLN A 1 51  ? 14.231  -46.550 -15.337 1.00 123.66 ? 51  GLN A C   1 
ATOM   413  O  O   . GLN A 1 51  ? 15.322  -46.405 -14.747 1.00 124.51 ? 51  GLN A O   1 
ATOM   414  C  CB  . GLN A 1 51  ? 13.455  -48.836 -14.718 1.00 127.03 ? 51  GLN A CB  1 
ATOM   415  C  CG  . GLN A 1 51  ? 12.393  -49.736 -14.111 1.00 130.38 ? 51  GLN A CG  1 
ATOM   416  C  CD  . GLN A 1 51  ? 11.392  -50.208 -15.138 1.00 135.51 ? 51  GLN A CD  1 
ATOM   417  O  OE1 . GLN A 1 51  ? 11.717  -50.406 -16.307 1.00 128.35 ? 51  GLN A OE1 1 
ATOM   418  N  NE2 . GLN A 1 51  ? 10.154  -50.379 -14.708 1.00 145.21 ? 51  GLN A NE2 1 
ATOM   419  N  N   . ARG A 1 52  ? 13.965  -46.060 -16.555 1.00 118.11 ? 52  ARG A N   1 
ATOM   420  C  CA  . ARG A 1 52  ? 14.901  -45.156 -17.273 1.00 112.39 ? 52  ARG A CA  1 
ATOM   421  C  C   . ARG A 1 52  ? 15.040  -43.854 -16.472 1.00 107.87 ? 52  ARG A C   1 
ATOM   422  O  O   . ARG A 1 52  ? 16.173  -43.547 -16.059 1.00 107.69 ? 52  ARG A O   1 
ATOM   423  C  CB  . ARG A 1 52  ? 14.462  -44.880 -18.717 1.00 113.89 ? 52  ARG A CB  1 
ATOM   424  C  CG  . ARG A 1 52  ? 14.933  -43.524 -19.231 1.00 117.15 ? 52  ARG A CG  1 
ATOM   425  C  CD  . ARG A 1 52  ? 15.775  -43.442 -20.489 1.00 117.42 ? 52  ARG A CD  1 
ATOM   426  N  NE  . ARG A 1 52  ? 16.590  -42.231 -20.413 1.00 116.46 ? 52  ARG A NE  1 
ATOM   427  C  CZ  . ARG A 1 52  ? 17.300  -41.708 -21.409 1.00 117.59 ? 52  ARG A CZ  1 
ATOM   428  N  NH1 . ARG A 1 52  ? 17.286  -42.264 -22.609 1.00 120.23 ? 52  ARG A NH1 1 
ATOM   429  N  NH2 . ARG A 1 52  ? 18.000  -40.605 -21.202 1.00 116.70 ? 52  ARG A NH2 1 
ATOM   430  N  N   . TYR A 1 53  ? 13.938  -43.127 -16.256 1.00 106.77 ? 53  TYR A N   1 
ATOM   431  C  CA  . TYR A 1 53  ? 13.937  -41.744 -15.705 1.00 109.19 ? 53  TYR A CA  1 
ATOM   432  C  C   . TYR A 1 53  ? 13.661  -41.739 -14.201 1.00 111.13 ? 53  TYR A C   1 
ATOM   433  O  O   . TYR A 1 53  ? 14.309  -40.947 -13.483 1.00 111.43 ? 53  TYR A O   1 
ATOM   434  C  CB  . TYR A 1 53  ? 12.916  -40.875 -16.440 1.00 109.86 ? 53  TYR A CB  1 
ATOM   435  C  CG  . TYR A 1 53  ? 13.363  -40.463 -17.816 1.00 108.82 ? 53  TYR A CG  1 
ATOM   436  C  CD1 . TYR A 1 53  ? 14.401  -39.559 -17.983 1.00 109.50 ? 53  TYR A CD1 1 
ATOM   437  C  CD2 . TYR A 1 53  ? 12.766  -40.984 -18.950 1.00 110.65 ? 53  TYR A CD2 1 
ATOM   438  C  CE1 . TYR A 1 53  ? 14.826  -39.174 -19.243 1.00 113.35 ? 53  TYR A CE1 1 
ATOM   439  C  CE2 . TYR A 1 53  ? 13.179  -40.611 -20.220 1.00 115.00 ? 53  TYR A CE2 1 
ATOM   440  C  CZ  . TYR A 1 53  ? 14.218  -39.707 -20.366 1.00 114.62 ? 53  TYR A CZ  1 
ATOM   441  O  OH  . TYR A 1 53  ? 14.639  -39.331 -21.609 1.00 112.43 ? 53  TYR A OH  1 
ATOM   442  N  N   . LEU A 1 54  ? 12.715  -42.566 -13.747 1.00 111.00 ? 54  LEU A N   1 
ATOM   443  C  CA  . LEU A 1 54  ? 12.265  -42.606 -12.332 1.00 111.50 ? 54  LEU A CA  1 
ATOM   444  C  C   . LEU A 1 54  ? 12.205  -44.057 -11.860 1.00 115.76 ? 54  LEU A C   1 
ATOM   445  O  O   . LEU A 1 54  ? 11.147  -44.683 -11.888 1.00 115.56 ? 54  LEU A O   1 
ATOM   446  C  CB  . LEU A 1 54  ? 10.908  -41.906 -12.234 1.00 107.40 ? 54  LEU A CB  1 
ATOM   447  C  CG  . LEU A 1 54  ? 10.944  -40.392 -12.445 1.00 103.33 ? 54  LEU A CG  1 
ATOM   448  C  CD1 . LEU A 1 54  ? 9.574   -39.858 -12.825 1.00 101.83 ? 54  LEU A CD1 1 
ATOM   449  C  CD2 . LEU A 1 54  ? 11.487  -39.682 -11.213 1.00 102.58 ? 54  LEU A CD2 1 
ATOM   450  N  N   . PRO A 1 55  ? 13.349  -44.637 -11.425 1.00 121.50 ? 55  PRO A N   1 
ATOM   451  C  CA  . PRO A 1 55  ? 13.370  -46.006 -10.908 1.00 126.52 ? 55  PRO A CA  1 
ATOM   452  C  C   . PRO A 1 55  ? 12.539  -46.131 -9.621  1.00 129.47 ? 55  PRO A C   1 
ATOM   453  O  O   . PRO A 1 55  ? 11.595  -46.913 -9.605  1.00 126.34 ? 55  PRO A O   1 
ATOM   454  C  CB  . PRO A 1 55  ? 14.860  -46.299 -10.650 1.00 125.23 ? 55  PRO A CB  1 
ATOM   455  C  CG  . PRO A 1 55  ? 15.530  -44.935 -10.580 1.00 121.22 ? 55  PRO A CG  1 
ATOM   456  C  CD  . PRO A 1 55  ? 14.681  -44.010 -11.424 1.00 118.25 ? 55  PRO A CD  1 
ATOM   457  N  N   . ASN A 1 56  ? 12.928  -45.367 -8.593  1.00 131.07 ? 56  ASN A N   1 
ATOM   458  C  CA  . ASN A 1 56  ? 12.207  -45.124 -7.313  1.00 130.33 ? 56  ASN A CA  1 
ATOM   459  C  C   . ASN A 1 56  ? 10.708  -45.427 -7.444  1.00 124.05 ? 56  ASN A C   1 
ATOM   460  O  O   . ASN A 1 56  ? 10.157  -46.067 -6.520  1.00 119.10 ? 56  ASN A O   1 
ATOM   461  C  CB  . ASN A 1 56  ? 12.425  -43.682 -6.847  1.00 131.55 ? 56  ASN A CB  1 
ATOM   462  C  CG  . ASN A 1 56  ? 12.390  -42.671 -7.977  1.00 130.33 ? 56  ASN A CG  1 
ATOM   463  O  OD1 . ASN A 1 56  ? 13.068  -42.837 -8.989  1.00 125.45 ? 56  ASN A OD1 1 
ATOM   464  N  ND2 . ASN A 1 56  ? 11.632  -41.601 -7.802  1.00 129.23 ? 56  ASN A ND2 1 
ATOM   465  N  N   . VAL A 1 57  ? 10.089  -44.975 -8.539  1.00 118.31 ? 57  VAL A N   1 
ATOM   466  C  CA  . VAL A 1 57  ? 8.621   -45.054 -8.806  1.00 117.90 ? 57  VAL A CA  1 
ATOM   467  C  C   . VAL A 1 57  ? 8.242   -46.491 -9.181  1.00 119.71 ? 57  VAL A C   1 
ATOM   468  O  O   . VAL A 1 57  ? 7.270   -47.012 -8.593  1.00 115.58 ? 57  VAL A O   1 
ATOM   469  C  CB  . VAL A 1 57  ? 8.217   -44.064 -9.917  1.00 114.72 ? 57  VAL A CB  1 
ATOM   470  C  CG1 . VAL A 1 57  ? 6.757   -44.210 -10.318 1.00 112.84 ? 57  VAL A CG1 1 
ATOM   471  C  CG2 . VAL A 1 57  ? 8.527   -42.629 -9.515  1.00 115.06 ? 57  VAL A CG2 1 
ATOM   472  N  N   . ALA A 1 58  ? 8.964   -47.084 -10.140 1.00 124.28 ? 58  ALA A N   1 
ATOM   473  C  CA  . ALA A 1 58  ? 8.718   -48.441 -10.684 1.00 124.71 ? 58  ALA A CA  1 
ATOM   474  C  C   . ALA A 1 58  ? 8.510   -49.426 -9.528  1.00 126.40 ? 58  ALA A C   1 
ATOM   475  O  O   . ALA A 1 58  ? 7.556   -50.229 -9.594  1.00 124.42 ? 58  ALA A O   1 
ATOM   476  C  CB  . ALA A 1 58  ? 9.869   -48.860 -11.565 1.00 122.64 ? 58  ALA A CB  1 
ATOM   477  N  N   . ASN A 1 59  ? 9.362   -49.337 -8.502  1.00 129.35 ? 59  ASN A N   1 
ATOM   478  C  CA  . ASN A 1 59  ? 9.348   -50.213 -7.298  1.00 132.21 ? 59  ASN A CA  1 
ATOM   479  C  C   . ASN A 1 59  ? 8.089   -49.912 -6.480  1.00 130.33 ? 59  ASN A C   1 
ATOM   480  O  O   . ASN A 1 59  ? 7.334   -50.864 -6.204  1.00 130.23 ? 59  ASN A O   1 
ATOM   481  C  CB  . ASN A 1 59  ? 10.594  -50.036 -6.425  1.00 134.85 ? 59  ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 59  ? 11.854  -49.790 -7.228  1.00 136.88 ? 59  ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 59  ? 12.598  -50.721 -7.525  1.00 140.99 ? 59  ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 59  ? 12.089  -48.545 -7.600  1.00 136.96 ? 59  ASN A ND2 1 
ATOM   485  N  N   . ALA A 1 60  ? 7.890   -48.635 -6.124  1.00 125.19 ? 60  ALA A N   1 
ATOM   486  C  CA  . ALA A 1 60  ? 6.767   -48.116 -5.301  1.00 118.54 ? 60  ALA A CA  1 
ATOM   487  C  C   . ALA A 1 60  ? 5.445   -48.762 -5.733  1.00 117.51 ? 60  ALA A C   1 
ATOM   488  O  O   . ALA A 1 60  ? 4.970   -48.456 -6.845  1.00 123.12 ? 60  ALA A O   1 
ATOM   489  C  CB  . ALA A 1 60  ? 6.698   -46.611 -5.418  1.00 116.60 ? 60  ALA A CB  1 
ATOM   490  N  N   . ALA A 1 61  ? 4.890   -49.630 -4.879  1.00 111.11 ? 61  ALA A N   1 
ATOM   491  C  CA  . ALA A 1 61  ? 3.572   -50.286 -5.051  1.00 107.63 ? 61  ALA A CA  1 
ATOM   492  C  C   . ALA A 1 61  ? 2.497   -49.510 -4.280  1.00 104.93 ? 61  ALA A C   1 
ATOM   493  O  O   . ALA A 1 61  ? 1.321   -49.921 -4.355  1.00 104.70 ? 61  ALA A O   1 
ATOM   494  C  CB  . ALA A 1 61  ? 3.650   -51.720 -4.589  1.00 105.74 ? 61  ALA A CB  1 
ATOM   495  N  N   . GLN A 1 62  ? 2.880   -48.428 -3.586  1.00 101.88 ? 62  GLN A N   1 
ATOM   496  C  CA  . GLN A 1 62  ? 1.941   -47.501 -2.893  1.00 100.18 ? 62  GLN A CA  1 
ATOM   497  C  C   . GLN A 1 62  ? 1.182   -46.663 -3.932  1.00 99.79  ? 62  GLN A C   1 
ATOM   498  O  O   . GLN A 1 62  ? 0.325   -45.865 -3.517  1.00 99.38  ? 62  GLN A O   1 
ATOM   499  C  CB  . GLN A 1 62  ? 2.662   -46.610 -1.871  1.00 99.35  ? 62  GLN A CB  1 
ATOM   500  C  CG  . GLN A 1 62  ? 3.572   -45.540 -2.466  1.00 100.43 ? 62  GLN A CG  1 
ATOM   501  C  CD  . GLN A 1 62  ? 5.038   -45.845 -2.259  1.00 101.81 ? 62  GLN A CD  1 
ATOM   502  O  OE1 . GLN A 1 62  ? 5.492   -46.964 -2.476  1.00 110.46 ? 62  GLN A OE1 1 
ATOM   503  N  NE2 . GLN A 1 62  ? 5.799   -44.850 -1.826  1.00 97.38  ? 62  GLN A NE2 1 
ATOM   504  N  N   . LEU A 1 63  ? 1.505   -46.821 -5.224  1.00 100.95 ? 63  LEU A N   1 
ATOM   505  C  CA  . LEU A 1 63  ? 0.795   -46.200 -6.376  1.00 97.08  ? 63  LEU A CA  1 
ATOM   506  C  C   . LEU A 1 63  ? 0.285   -47.304 -7.305  1.00 93.40  ? 63  LEU A C   1 
ATOM   507  O  O   . LEU A 1 63  ? 1.041   -48.262 -7.561  1.00 93.36  ? 63  LEU A O   1 
ATOM   508  C  CB  . LEU A 1 63  ? 1.751   -45.286 -7.148  1.00 97.73  ? 63  LEU A CB  1 
ATOM   509  C  CG  . LEU A 1 63  ? 2.576   -44.309 -6.315  1.00 100.96 ? 63  LEU A CG  1 
ATOM   510  C  CD1 . LEU A 1 63  ? 3.563   -43.566 -7.198  1.00 102.51 ? 63  LEU A CD1 1 
ATOM   511  C  CD2 . LEU A 1 63  ? 1.680   -43.331 -5.581  1.00 100.33 ? 63  LEU A CD2 1 
ATOM   512  N  N   . THR A 1 64  ? -0.943  -47.159 -7.808  1.00 89.17  ? 64  THR A N   1 
ATOM   513  C  CA  . THR A 1 64  ? -1.447  -47.927 -8.974  1.00 89.79  ? 64  THR A CA  1 
ATOM   514  C  C   . THR A 1 64  ? -0.597  -47.539 -10.188 1.00 90.47  ? 64  THR A C   1 
ATOM   515  O  O   . THR A 1 64  ? -0.029  -46.429 -10.187 1.00 84.87  ? 64  THR A O   1 
ATOM   516  C  CB  . THR A 1 64  ? -2.947  -47.709 -9.217  1.00 92.99  ? 64  THR A CB  1 
ATOM   517  O  OG1 . THR A 1 64  ? -3.290  -48.345 -10.450 1.00 101.14 ? 64  THR A OG1 1 
ATOM   518  C  CG2 . THR A 1 64  ? -3.360  -46.254 -9.287  1.00 91.54  ? 64  THR A CG2 1 
HETATM 519  N  N   . MSE A 1 65  ? -0.505  -48.431 -11.175 1.00 93.42  ? 65  MSE A N   1 
HETATM 520  C  CA  . MSE A 1 65  ? 0.187   -48.174 -12.463 1.00 97.85  ? 65  MSE A CA  1 
HETATM 521  C  C   . MSE A 1 65  ? -0.490  -46.988 -13.164 1.00 101.09 ? 65  MSE A C   1 
HETATM 522  O  O   . MSE A 1 65  ? 0.231   -46.148 -13.736 1.00 99.73  ? 65  MSE A O   1 
HETATM 523  C  CB  . MSE A 1 65  ? 0.165   -49.435 -13.331 1.00 101.26 ? 65  MSE A CB  1 
HETATM 524  C  CG  . MSE A 1 65  ? 1.213   -49.445 -14.417 1.00 106.60 ? 65  MSE A CG  1 
HETATM 525  SE SE  . MSE A 1 65  ? 3.040   -49.722 -13.734 1.00 103.78 ? 65  MSE A SE  1 
HETATM 526  C  CE  . MSE A 1 65  ? 4.045   -50.048 -15.382 1.00 99.82  ? 65  MSE A CE  1 
ATOM   527  N  N   . GLY A 1 66  ? -1.825  -46.922 -13.101 1.00 104.09 ? 66  GLY A N   1 
ATOM   528  C  CA  . GLY A 1 66  ? -2.633  -45.803 -13.623 1.00 104.37 ? 66  GLY A CA  1 
ATOM   529  C  C   . GLY A 1 66  ? -2.079  -44.453 -13.195 1.00 103.74 ? 66  GLY A C   1 
ATOM   530  O  O   . GLY A 1 66  ? -2.108  -43.522 -14.017 1.00 104.12 ? 66  GLY A O   1 
ATOM   531  N  N   . GLU A 1 67  ? -1.576  -44.357 -11.959 1.00 103.16 ? 67  GLU A N   1 
ATOM   532  C  CA  . GLU A 1 67  ? -1.018  -43.115 -11.357 1.00 104.34 ? 67  GLU A CA  1 
ATOM   533  C  C   . GLU A 1 67  ? 0.439   -42.933 -11.794 1.00 105.16 ? 67  GLU A C   1 
ATOM   534  O  O   . GLU A 1 67  ? 0.876   -41.770 -11.918 1.00 108.83 ? 67  GLU A O   1 
ATOM   535  C  CB  . GLU A 1 67  ? -1.109  -43.166 -9.832  1.00 104.41 ? 67  GLU A CB  1 
ATOM   536  C  CG  . GLU A 1 67  ? -2.513  -42.956 -9.302  1.00 101.92 ? 67  GLU A CG  1 
ATOM   537  C  CD  . GLU A 1 67  ? -2.642  -43.196 -7.811  1.00 99.74  ? 67  GLU A CD  1 
ATOM   538  O  OE1 . GLU A 1 67  ? -3.334  -42.403 -7.145  1.00 95.55  ? 67  GLU A OE1 1 
ATOM   539  O  OE2 . GLU A 1 67  ? -2.025  -44.158 -7.315  1.00 96.11  ? 67  GLU A OE2 1 
ATOM   540  N  N   . LYS A 1 68  ? 1.168   -44.036 -11.986 1.00 104.59 ? 68  LYS A N   1 
ATOM   541  C  CA  . LYS A 1 68  ? 2.543   -44.037 -12.555 1.00 104.68 ? 68  LYS A CA  1 
ATOM   542  C  C   . LYS A 1 68  ? 2.468   -43.500 -13.991 1.00 99.79  ? 68  LYS A C   1 
ATOM   543  O  O   . LYS A 1 68  ? 3.246   -42.580 -14.324 1.00 97.71  ? 68  LYS A O   1 
ATOM   544  C  CB  . LYS A 1 68  ? 3.150   -45.443 -12.471 1.00 111.67 ? 68  LYS A CB  1 
ATOM   545  C  CG  . LYS A 1 68  ? 3.416   -45.939 -11.053 1.00 117.51 ? 68  LYS A CG  1 
ATOM   546  C  CD  . LYS A 1 68  ? 3.760   -47.419 -10.944 1.00 120.55 ? 68  LYS A CD  1 
ATOM   547  C  CE  . LYS A 1 68  ? 4.018   -47.845 -9.512  1.00 120.09 ? 68  LYS A CE  1 
ATOM   548  N  NZ  . LYS A 1 68  ? 3.614   -49.247 -9.238  1.00 120.09 ? 68  LYS A NZ  1 
ATOM   549  N  N   . GLY A 1 69  ? 1.536   -44.031 -14.789 1.00 96.11  ? 69  GLY A N   1 
ATOM   550  C  CA  . GLY A 1 69  ? 1.293   -43.627 -16.189 1.00 95.77  ? 69  GLY A CA  1 
ATOM   551  C  C   . GLY A 1 69  ? 0.848   -42.176 -16.299 1.00 92.87  ? 69  GLY A C   1 
ATOM   552  O  O   . GLY A 1 69  ? 1.269   -41.491 -17.244 1.00 90.47  ? 69  GLY A O   1 
ATOM   553  N  N   . CYS A 1 70  ? 0.009   -41.723 -15.370 1.00 93.66  ? 70  CYS A N   1 
ATOM   554  C  CA  . CYS A 1 70  ? -0.466  -40.318 -15.284 1.00 95.10  ? 70  CYS A CA  1 
ATOM   555  C  C   . CYS A 1 70  ? 0.718   -39.395 -14.971 1.00 90.86  ? 70  CYS A C   1 
ATOM   556  O  O   . CYS A 1 70  ? 0.913   -38.409 -15.720 1.00 92.46  ? 70  CYS A O   1 
ATOM   557  C  CB  . CYS A 1 70  ? -1.549  -40.166 -14.226 1.00 98.26  ? 70  CYS A CB  1 
ATOM   558  S  SG  . CYS A 1 70  ? -1.785  -38.452 -13.698 1.00 107.84 ? 70  CYS A SG  1 
ATOM   559  N  N   . LEU A 1 71  ? 1.478   -39.707 -13.915 1.00 86.09  ? 71  LEU A N   1 
ATOM   560  C  CA  . LEU A 1 71  ? 2.645   -38.903 -13.460 1.00 82.93  ? 71  LEU A CA  1 
ATOM   561  C  C   . LEU A 1 71  ? 3.650   -38.759 -14.604 1.00 82.02  ? 71  LEU A C   1 
ATOM   562  O  O   . LEU A 1 71  ? 4.160   -37.635 -14.799 1.00 83.22  ? 71  LEU A O   1 
ATOM   563  C  CB  . LEU A 1 71  ? 3.317   -39.573 -12.260 1.00 83.34  ? 71  LEU A CB  1 
ATOM   564  C  CG  . LEU A 1 71  ? 4.715   -39.046 -11.928 1.00 82.64  ? 71  LEU A CG  1 
ATOM   565  C  CD1 . LEU A 1 71  ? 4.701   -37.552 -11.647 1.00 82.65  ? 71  LEU A CD1 1 
ATOM   566  C  CD2 . LEU A 1 71  ? 5.308   -39.786 -10.743 1.00 82.33  ? 71  LEU A CD2 1 
HETATM 567  N  N   . MSE A 1 72  ? 3.942   -39.831 -15.334 1.00 79.63  ? 72  MSE A N   1 
HETATM 568  C  CA  . MSE A 1 72  ? 4.912   -39.767 -16.415 1.00 83.19  ? 72  MSE A CA  1 
HETATM 569  C  C   . MSE A 1 72  ? 4.429   -38.808 -17.458 1.00 77.46  ? 72  MSE A C   1 
HETATM 570  O  O   . MSE A 1 72  ? 5.173   -37.870 -17.809 1.00 72.70  ? 72  MSE A O   1 
HETATM 571  C  CB  . MSE A 1 72  ? 5.057   -41.147 -17.038 1.00 90.85  ? 72  MSE A CB  1 
HETATM 572  C  CG  . MSE A 1 72  ? 6.413   -41.290 -17.716 1.00 95.36  ? 72  MSE A CG  1 
HETATM 573  SE SE  . MSE A 1 72  ? 7.781   -40.363 -16.643 1.00 104.09 ? 72  MSE A SE  1 
HETATM 574  C  CE  . MSE A 1 72  ? 8.948   -41.905 -16.265 1.00 101.65 ? 72  MSE A CE  1 
ATOM   575  N  N   . SER A 1 73  ? 3.230   -39.025 -17.980 1.00 72.03  ? 73  SER A N   1 
ATOM   576  C  CA  . SER A 1 73  ? 2.616   -38.116 -18.980 1.00 69.33  ? 73  SER A CA  1 
ATOM   577  C  C   . SER A 1 73  ? 3.052   -36.683 -18.657 1.00 67.43  ? 73  SER A C   1 
ATOM   578  O  O   . SER A 1 73  ? 3.739   -36.062 -19.499 1.00 67.85  ? 73  SER A O   1 
ATOM   579  C  CB  . SER A 1 73  ? 1.116   -38.271 -19.016 1.00 67.84  ? 73  SER A CB  1 
ATOM   580  O  OG  . SER A 1 73  ? 0.752   -39.619 -19.286 1.00 68.48  ? 73  SER A OG  1 
ATOM   581  N  N   . HIS A 1 74  ? 2.739   -36.217 -17.446 1.00 65.62  ? 74  HIS A N   1 
ATOM   582  C  CA  . HIS A 1 74  ? 3.049   -34.844 -16.965 1.00 63.91  ? 74  HIS A CA  1 
ATOM   583  C  C   . HIS A 1 74  ? 4.565   -34.618 -16.977 1.00 65.00  ? 74  HIS A C   1 
ATOM   584  O  O   . HIS A 1 74  ? 4.990   -33.567 -17.477 1.00 62.23  ? 74  HIS A O   1 
ATOM   585  C  CB  . HIS A 1 74  ? 2.412   -34.598 -15.592 1.00 61.13  ? 74  HIS A CB  1 
ATOM   586  C  CG  . HIS A 1 74  ? 0.948   -34.313 -15.664 1.00 59.28  ? 74  HIS A CG  1 
ATOM   587  N  ND1 . HIS A 1 74  ? 0.454   -33.026 -15.754 1.00 57.46  ? 74  HIS A ND1 1 
ATOM   588  C  CD2 . HIS A 1 74  ? -0.125  -35.136 -15.671 1.00 59.32  ? 74  HIS A CD2 1 
ATOM   589  C  CE1 . HIS A 1 74  ? -0.861  -33.066 -15.819 1.00 59.30  ? 74  HIS A CE1 1 
ATOM   590  N  NE2 . HIS A 1 74  ? -1.246  -34.349 -15.766 1.00 60.05  ? 74  HIS A NE2 1 
ATOM   591  N  N   . PHE A 1 75  ? 5.344   -35.574 -16.468 1.00 70.51  ? 75  PHE A N   1 
ATOM   592  C  CA  . PHE A 1 75  ? 6.824   -35.472 -16.350 1.00 75.39  ? 75  PHE A CA  1 
ATOM   593  C  C   . PHE A 1 75  ? 7.426   -35.186 -17.730 1.00 73.02  ? 75  PHE A C   1 
ATOM   594  O  O   . PHE A 1 75  ? 8.119   -34.161 -17.893 1.00 68.67  ? 75  PHE A O   1 
ATOM   595  C  CB  . PHE A 1 75  ? 7.413   -36.739 -15.721 1.00 80.23  ? 75  PHE A CB  1 
ATOM   596  C  CG  . PHE A 1 75  ? 8.883   -36.657 -15.393 1.00 83.98  ? 75  PHE A CG  1 
ATOM   597  C  CD1 . PHE A 1 75  ? 9.345   -35.804 -14.399 1.00 86.80  ? 75  PHE A CD1 1 
ATOM   598  C  CD2 . PHE A 1 75  ? 9.809   -37.428 -16.079 1.00 87.00  ? 75  PHE A CD2 1 
ATOM   599  C  CE1 . PHE A 1 75  ? 10.697  -35.733 -14.098 1.00 87.65  ? 75  PHE A CE1 1 
ATOM   600  C  CE2 . PHE A 1 75  ? 11.160  -37.347 -15.781 1.00 91.72  ? 75  PHE A CE2 1 
ATOM   601  C  CZ  . PHE A 1 75  ? 11.602  -36.499 -14.792 1.00 90.42  ? 75  PHE A CZ  1 
HETATM 602  N  N   . MSE A 1 76  ? 7.201   -36.055 -18.704 1.00 75.63  ? 76  MSE A N   1 
HETATM 603  C  CA  . MSE A 1 76  ? 7.814   -35.866 -20.010 1.00 77.23  ? 76  MSE A CA  1 
HETATM 604  C  C   . MSE A 1 76  ? 7.442   -34.526 -20.590 1.00 72.31  ? 76  MSE A C   1 
HETATM 605  O  O   . MSE A 1 76  ? 8.302   -33.858 -21.201 1.00 70.16  ? 76  MSE A O   1 
HETATM 606  C  CB  . MSE A 1 76  ? 7.348   -37.007 -20.907 1.00 81.70  ? 76  MSE A CB  1 
HETATM 607  C  CG  . MSE A 1 76  ? 7.781   -38.349 -20.318 1.00 87.85  ? 76  MSE A CG  1 
HETATM 608  SE SE  . MSE A 1 76  ? 9.470   -38.933 -21.156 1.00 93.81  ? 76  MSE A SE  1 
HETATM 609  C  CE  . MSE A 1 76  ? 10.004  -40.377 -19.920 1.00 95.97  ? 76  MSE A CE  1 
ATOM   610  N  N   . LEU A 1 77  ? 6.195   -34.110 -20.417 1.00 69.10  ? 77  LEU A N   1 
ATOM   611  C  CA  . LEU A 1 77  ? 5.710   -32.816 -20.956 1.00 69.88  ? 77  LEU A CA  1 
ATOM   612  C  C   . LEU A 1 77  ? 6.435   -31.652 -20.269 1.00 72.33  ? 77  LEU A C   1 
ATOM   613  O  O   . LEU A 1 77  ? 6.564   -30.595 -20.911 1.00 77.29  ? 77  LEU A O   1 
ATOM   614  C  CB  . LEU A 1 77  ? 4.191   -32.745 -20.779 1.00 68.77  ? 77  LEU A CB  1 
ATOM   615  C  CG  . LEU A 1 77  ? 3.396   -33.515 -21.831 1.00 69.41  ? 77  LEU A CG  1 
ATOM   616  C  CD1 . LEU A 1 77  ? 1.999   -33.845 -21.339 1.00 69.44  ? 77  LEU A CD1 1 
ATOM   617  C  CD2 . LEU A 1 77  ? 3.331   -32.735 -23.132 1.00 72.13  ? 77  LEU A CD2 1 
ATOM   618  N  N   . TRP A 1 78  ? 6.902   -31.830 -19.028 1.00 74.59  ? 78  TRP A N   1 
ATOM   619  C  CA  . TRP A 1 78  ? 7.795   -30.848 -18.352 1.00 77.53  ? 78  TRP A CA  1 
ATOM   620  C  C   . TRP A 1 78  ? 9.150   -30.878 -19.058 1.00 76.29  ? 78  TRP A C   1 
ATOM   621  O  O   . TRP A 1 78  ? 9.647   -29.798 -19.423 1.00 78.58  ? 78  TRP A O   1 
ATOM   622  C  CB  . TRP A 1 78  ? 7.942   -31.107 -16.844 1.00 80.93  ? 78  TRP A CB  1 
ATOM   623  C  CG  . TRP A 1 78  ? 6.647   -31.184 -16.092 1.00 81.16  ? 78  TRP A CG  1 
ATOM   624  C  CD1 . TRP A 1 78  ? 5.479   -30.543 -16.388 1.00 80.88  ? 78  TRP A CD1 1 
ATOM   625  C  CD2 . TRP A 1 78  ? 6.395   -31.942 -14.895 1.00 82.20  ? 78  TRP A CD2 1 
ATOM   626  N  NE1 . TRP A 1 78  ? 4.513   -30.865 -15.474 1.00 81.17  ? 78  TRP A NE1 1 
ATOM   627  C  CE2 . TRP A 1 78  ? 5.047   -31.717 -14.542 1.00 80.93  ? 78  TRP A CE2 1 
ATOM   628  C  CE3 . TRP A 1 78  ? 7.172   -32.782 -14.088 1.00 82.12  ? 78  TRP A CE3 1 
ATOM   629  C  CZ2 . TRP A 1 78  ? 4.465   -32.310 -13.425 1.00 76.74  ? 78  TRP A CZ2 1 
ATOM   630  C  CZ3 . TRP A 1 78  ? 6.593   -33.373 -12.987 1.00 77.46  ? 78  TRP A CZ3 1 
ATOM   631  C  CH2 . TRP A 1 78  ? 5.257   -33.140 -12.665 1.00 75.45  ? 78  TRP A CH2 1 
ATOM   632  N  N   . LYS A 1 79  ? 9.700   -32.079 -19.268 1.00 76.80  ? 79  LYS A N   1 
ATOM   633  C  CA  . LYS A 1 79  ? 11.005  -32.286 -19.949 1.00 79.80  ? 79  LYS A CA  1 
ATOM   634  C  C   . LYS A 1 79  ? 10.972  -31.567 -21.305 1.00 73.79  ? 79  LYS A C   1 
ATOM   635  O  O   . LYS A 1 79  ? 11.963  -30.888 -21.627 1.00 73.16  ? 79  LYS A O   1 
ATOM   636  C  CB  . LYS A 1 79  ? 11.322  -33.780 -20.080 1.00 89.26  ? 79  LYS A CB  1 
ATOM   637  C  CG  . LYS A 1 79  ? 12.788  -34.102 -20.343 1.00 99.87  ? 79  LYS A CG  1 
ATOM   638  C  CD  . LYS A 1 79  ? 13.251  -35.435 -19.798 1.00 106.02 ? 79  LYS A CD  1 
ATOM   639  C  CE  . LYS A 1 79  ? 14.762  -35.563 -19.751 1.00 108.76 ? 79  LYS A CE  1 
ATOM   640  N  NZ  . LYS A 1 79  ? 15.366  -35.650 -21.104 1.00 108.48 ? 79  LYS A NZ  1 
ATOM   641  N  N   . LYS A 1 80  ? 9.871   -31.691 -22.054 1.00 68.82  ? 80  LYS A N   1 
ATOM   642  C  CA  . LYS A 1 80  ? 9.666   -31.020 -23.366 1.00 66.22  ? 80  LYS A CA  1 
ATOM   643  C  C   . LYS A 1 80  ? 9.818   -29.501 -23.218 1.00 63.56  ? 80  LYS A C   1 
ATOM   644  O  O   . LYS A 1 80  ? 10.514  -28.909 -24.052 1.00 63.15  ? 80  LYS A O   1 
ATOM   645  C  CB  . LYS A 1 80  ? 8.300   -31.371 -23.959 1.00 68.14  ? 80  LYS A CB  1 
ATOM   646  C  CG  . LYS A 1 80  ? 8.274   -32.669 -24.757 1.00 72.44  ? 80  LYS A CG  1 
ATOM   647  C  CD  . LYS A 1 80  ? 7.254   -32.674 -25.875 1.00 73.55  ? 80  LYS A CD  1 
ATOM   648  C  CE  . LYS A 1 80  ? 7.705   -31.868 -27.072 1.00 78.90  ? 80  LYS A CE  1 
ATOM   649  N  NZ  . LYS A 1 80  ? 8.520   -32.670 -28.018 1.00 81.07  ? 80  LYS A NZ  1 
ATOM   650  N  N   . CYS A 1 81  ? 9.197   -28.892 -22.203 1.00 63.94  ? 81  CYS A N   1 
ATOM   651  C  CA  . CYS A 1 81  ? 9.299   -27.430 -21.927 1.00 66.37  ? 81  CYS A CA  1 
ATOM   652  C  C   . CYS A 1 81  ? 10.781  -27.037 -21.907 1.00 70.42  ? 81  CYS A C   1 
ATOM   653  O  O   . CYS A 1 81  ? 11.113  -25.960 -22.431 1.00 71.45  ? 81  CYS A O   1 
ATOM   654  C  CB  . CYS A 1 81  ? 8.641   -27.039 -20.606 1.00 66.97  ? 81  CYS A CB  1 
ATOM   655  S  SG  . CYS A 1 81  ? 8.413   -25.251 -20.394 1.00 65.50  ? 81  CYS A SG  1 
ATOM   656  N  N   . ILE A 1 82  ? 11.629  -27.897 -21.330 1.00 75.29  ? 82  ILE A N   1 
ATOM   657  C  CA  . ILE A 1 82  ? 13.108  -27.705 -21.242 1.00 79.52  ? 82  ILE A CA  1 
ATOM   658  C  C   . ILE A 1 82  ? 13.714  -27.933 -22.632 1.00 78.38  ? 82  ILE A C   1 
ATOM   659  O  O   . ILE A 1 82  ? 14.396  -27.015 -23.130 1.00 78.54  ? 82  ILE A O   1 
ATOM   660  C  CB  . ILE A 1 82  ? 13.736  -28.630 -20.175 1.00 82.55  ? 82  ILE A CB  1 
ATOM   661  C  CG1 . ILE A 1 82  ? 13.019  -28.523 -18.825 1.00 84.10  ? 82  ILE A CG1 1 
ATOM   662  C  CG2 . ILE A 1 82  ? 15.227  -28.358 -20.032 1.00 84.50  ? 82  ILE A CG2 1 
ATOM   663  C  CD1 . ILE A 1 82  ? 12.791  -27.098 -18.355 1.00 85.01  ? 82  ILE A CD1 1 
ATOM   664  N  N   . ASP A 1 83  ? 13.451  -29.099 -23.233 1.00 77.08  ? 83  ASP A N   1 
ATOM   665  C  CA  . ASP A 1 83  ? 14.022  -29.535 -24.537 1.00 76.56  ? 83  ASP A CA  1 
ATOM   666  C  C   . ASP A 1 83  ? 13.809  -28.434 -25.582 1.00 73.77  ? 83  ASP A C   1 
ATOM   667  O  O   . ASP A 1 83  ? 14.810  -27.943 -26.133 1.00 72.88  ? 83  ASP A O   1 
ATOM   668  C  CB  . ASP A 1 83  ? 13.411  -30.861 -25.003 1.00 81.59  ? 83  ASP A CB  1 
ATOM   669  C  CG  . ASP A 1 83  ? 13.749  -32.049 -24.117 1.00 86.06  ? 83  ASP A CG  1 
ATOM   670  O  OD1 . ASP A 1 83  ? 14.613  -31.889 -23.227 1.00 86.42  ? 83  ASP A OD1 1 
ATOM   671  O  OD2 . ASP A 1 83  ? 13.146  -33.124 -24.328 1.00 91.42  ? 83  ASP A OD2 1 
ATOM   672  N  N   . GLU A 1 84  ? 12.552  -28.037 -25.807 1.00 72.76  ? 84  GLU A N   1 
ATOM   673  C  CA  . GLU A 1 84  ? 12.152  -27.001 -26.801 1.00 70.01  ? 84  GLU A CA  1 
ATOM   674  C  C   . GLU A 1 84  ? 12.445  -25.597 -26.244 1.00 65.77  ? 84  GLU A C   1 
ATOM   675  O  O   . GLU A 1 84  ? 12.024  -24.616 -26.876 1.00 62.02  ? 84  GLU A O   1 
ATOM   676  C  CB  . GLU A 1 84  ? 10.668  -27.154 -27.161 1.00 70.02  ? 84  GLU A CB  1 
ATOM   677  C  CG  . GLU A 1 84  ? 10.293  -28.547 -27.656 1.00 69.46  ? 84  GLU A CG  1 
ATOM   678  C  CD  . GLU A 1 84  ? 8.836   -28.750 -28.045 1.00 69.52  ? 84  GLU A CD  1 
ATOM   679  O  OE1 . GLU A 1 84  ? 8.542   -29.756 -28.720 1.00 69.59  ? 84  GLU A OE1 1 
ATOM   680  O  OE2 . GLU A 1 84  ? 7.999   -27.898 -27.696 1.00 68.01  ? 84  GLU A OE2 1 
ATOM   681  N  N   . ASN A 1 85  ? 13.141  -25.511 -25.106 1.00 65.70  ? 85  ASN A N   1 
ATOM   682  C  CA  . ASN A 1 85  ? 13.432  -24.255 -24.364 1.00 68.68  ? 85  ASN A CA  1 
ATOM   683  C  C   . ASN A 1 85  ? 12.236  -23.304 -24.476 1.00 67.38  ? 85  ASN A C   1 
ATOM   684  O  O   . ASN A 1 85  ? 12.405  -22.204 -25.025 1.00 71.77  ? 85  ASN A O   1 
ATOM   685  C  CB  . ASN A 1 85  ? 14.734  -23.594 -24.828 1.00 69.96  ? 85  ASN A CB  1 
ATOM   686  C  CG  . ASN A 1 85  ? 15.204  -22.522 -23.863 1.00 71.70  ? 85  ASN A CG  1 
ATOM   687  O  OD1 . ASN A 1 85  ? 15.733  -22.827 -22.795 1.00 71.62  ? 85  ASN A OD1 1 
ATOM   688  N  ND2 . ASN A 1 85  ? 14.995  -21.263 -24.211 1.00 72.34  ? 85  ASN A ND2 1 
ATOM   689  N  N   . LEU A 1 86  ? 11.075  -23.729 -23.973 1.00 65.24  ? 86  LEU A N   1 
ATOM   690  C  CA  . LEU A 1 86  ? 9.836   -22.911 -23.906 1.00 63.63  ? 86  LEU A CA  1 
ATOM   691  C  C   . LEU A 1 86  ? 9.858   -22.094 -22.614 1.00 61.13  ? 86  LEU A C   1 
ATOM   692  O  O   . LEU A 1 86  ? 10.291  -22.640 -21.592 1.00 59.93  ? 86  LEU A O   1 
ATOM   693  C  CB  . LEU A 1 86  ? 8.617   -23.840 -23.937 1.00 65.32  ? 86  LEU A CB  1 
ATOM   694  C  CG  . LEU A 1 86  ? 8.260   -24.430 -25.301 1.00 65.41  ? 86  LEU A CG  1 
ATOM   695  C  CD1 . LEU A 1 86  ? 7.422   -25.696 -25.145 1.00 62.88  ? 86  LEU A CD1 1 
ATOM   696  C  CD2 . LEU A 1 86  ? 7.525   -23.395 -26.146 1.00 65.95  ? 86  LEU A CD2 1 
ATOM   697  N  N   . ASP A 1 87  ? 9.390   -20.847 -22.671 1.00 60.07  ? 87  ASP A N   1 
ATOM   698  C  CA  . ASP A 1 87  ? 9.123   -19.988 -21.485 1.00 60.39  ? 87  ASP A CA  1 
ATOM   699  C  C   . ASP A 1 87  ? 8.175   -20.736 -20.534 1.00 59.54  ? 87  ASP A C   1 
ATOM   700  O  O   . ASP A 1 87  ? 8.413   -20.718 -19.309 1.00 58.12  ? 87  ASP A O   1 
ATOM   701  C  CB  . ASP A 1 87  ? 8.516   -18.643 -21.896 1.00 62.10  ? 87  ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 87  ? 9.350   -17.824 -22.871 1.00 64.94  ? 87  ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 87  ? 10.244  -18.412 -23.516 1.00 69.41  ? 87  ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 87  ? 9.085   -16.609 -22.996 1.00 66.46  ? 87  ASP A OD2 1 
ATOM   705  N  N   . TYR A 1 88  ? 7.144   -21.377 -21.090 1.00 58.52  ? 88  TYR A N   1 
ATOM   706  C  CA  . TYR A 1 88  ? 6.055   -22.060 -20.350 1.00 56.00  ? 88  TYR A CA  1 
ATOM   707  C  C   . TYR A 1 88  ? 5.320   -23.027 -21.276 1.00 54.90  ? 88  TYR A C   1 
ATOM   708  O  O   . TYR A 1 88  ? 5.270   -22.779 -22.490 1.00 56.74  ? 88  TYR A O   1 
ATOM   709  C  CB  . TYR A 1 88  ? 5.043   -21.031 -19.849 1.00 57.77  ? 88  TYR A CB  1 
ATOM   710  C  CG  . TYR A 1 88  ? 4.164   -20.470 -20.939 1.00 59.72  ? 88  TYR A CG  1 
ATOM   711  C  CD1 . TYR A 1 88  ? 3.017   -21.131 -21.349 1.00 62.64  ? 88  TYR A CD1 1 
ATOM   712  C  CD2 . TYR A 1 88  ? 4.501   -19.302 -21.602 1.00 62.28  ? 88  TYR A CD2 1 
ATOM   713  C  CE1 . TYR A 1 88  ? 2.214   -20.632 -22.363 1.00 67.09  ? 88  TYR A CE1 1 
ATOM   714  C  CE2 . TYR A 1 88  ? 3.710   -18.788 -22.617 1.00 64.46  ? 88  TYR A CE2 1 
ATOM   715  C  CZ  . TYR A 1 88  ? 2.560   -19.455 -23.003 1.00 67.89  ? 88  TYR A CZ  1 
ATOM   716  O  OH  . TYR A 1 88  ? 1.768   -18.955 -24.003 1.00 71.45  ? 88  TYR A OH  1 
ATOM   717  N  N   . ILE A 1 89  ? 4.699   -24.052 -20.702 1.00 56.06  ? 89  ILE A N   1 
ATOM   718  C  CA  . ILE A 1 89  ? 3.818   -25.012 -21.430 1.00 56.80  ? 89  ILE A CA  1 
ATOM   719  C  C   . ILE A 1 89  ? 2.520   -25.186 -20.624 1.00 56.07  ? 89  ILE A C   1 
ATOM   720  O  O   . ILE A 1 89  ? 2.553   -24.977 -19.384 1.00 53.37  ? 89  ILE A O   1 
ATOM   721  C  CB  . ILE A 1 89  ? 4.567   -26.335 -21.674 1.00 58.89  ? 89  ILE A CB  1 
ATOM   722  C  CG1 . ILE A 1 89  ? 3.801   -27.253 -22.630 1.00 61.54  ? 89  ILE A CG1 1 
ATOM   723  C  CG2 . ILE A 1 89  ? 4.894   -27.026 -20.357 1.00 61.77  ? 89  ILE A CG2 1 
ATOM   724  C  CD1 . ILE A 1 89  ? 4.534   -28.525 -22.981 1.00 64.10  ? 89  ILE A CD1 1 
ATOM   725  N  N   . THR A 1 90  ? 1.421   -25.532 -21.305 1.00 53.87  ? 90  THR A N   1 
ATOM   726  C  CA  . THR A 1 90  ? 0.033   -25.492 -20.775 1.00 51.50  ? 90  THR A CA  1 
ATOM   727  C  C   . THR A 1 90  ? -0.630  -26.865 -20.947 1.00 51.47  ? 90  THR A C   1 
ATOM   728  O  O   . THR A 1 90  ? -0.950  -27.225 -22.100 1.00 50.15  ? 90  THR A O   1 
ATOM   729  C  CB  . THR A 1 90  ? -0.753  -24.387 -21.488 1.00 50.41  ? 90  THR A CB  1 
ATOM   730  O  OG1 . THR A 1 90  ? 0.111   -23.262 -21.643 1.00 48.53  ? 90  THR A OG1 1 
ATOM   731  C  CG2 . THR A 1 90  ? -2.002  -23.983 -20.739 1.00 51.33  ? 90  THR A CG2 1 
ATOM   732  N  N   . LEU A 1 91  ? -0.844  -27.595 -19.844 1.00 52.60  ? 91  LEU A N   1 
ATOM   733  C  CA  . LEU A 1 91  ? -1.251  -29.029 -19.862 1.00 52.50  ? 91  LEU A CA  1 
ATOM   734  C  C   . LEU A 1 91  ? -2.704  -29.182 -19.416 1.00 49.86  ? 91  LEU A C   1 
ATOM   735  O  O   . LEU A 1 91  ? -3.103  -28.484 -18.477 1.00 51.35  ? 91  LEU A O   1 
ATOM   736  C  CB  . LEU A 1 91  ? -0.334  -29.843 -18.946 1.00 55.40  ? 91  LEU A CB  1 
ATOM   737  C  CG  . LEU A 1 91  ? 1.167   -29.627 -19.144 1.00 59.45  ? 91  LEU A CG  1 
ATOM   738  C  CD1 . LEU A 1 91  ? 1.961   -30.761 -18.510 1.00 59.75  ? 91  LEU A CD1 1 
ATOM   739  C  CD2 . LEU A 1 91  ? 1.534   -29.493 -20.616 1.00 61.33  ? 91  LEU A CD2 1 
ATOM   740  N  N   . PHE A 1 92  ? -3.424  -30.103 -20.060 1.00 48.27  ? 92  PHE A N   1 
ATOM   741  C  CA  . PHE A 1 92  ? -4.833  -30.478 -19.776 1.00 48.61  ? 92  PHE A CA  1 
ATOM   742  C  C   . PHE A 1 92  ? -4.961  -32.003 -19.781 1.00 49.66  ? 92  PHE A C   1 
ATOM   743  O  O   . PHE A 1 92  ? -4.044  -32.664 -20.316 1.00 53.11  ? 92  PHE A O   1 
ATOM   744  C  CB  . PHE A 1 92  ? -5.769  -29.883 -20.829 1.00 47.63  ? 92  PHE A CB  1 
ATOM   745  C  CG  . PHE A 1 92  ? -5.637  -28.393 -21.018 1.00 46.61  ? 92  PHE A CG  1 
ATOM   746  C  CD1 . PHE A 1 92  ? -6.391  -27.510 -20.261 1.00 46.56  ? 92  PHE A CD1 1 
ATOM   747  C  CD2 . PHE A 1 92  ? -4.758  -27.873 -21.953 1.00 46.79  ? 92  PHE A CD2 1 
ATOM   748  C  CE1 . PHE A 1 92  ? -6.261  -26.142 -20.424 1.00 46.64  ? 92  PHE A CE1 1 
ATOM   749  C  CE2 . PHE A 1 92  ? -4.635  -26.503 -22.123 1.00 47.48  ? 92  PHE A CE2 1 
ATOM   750  C  CZ  . PHE A 1 92  ? -5.387  -25.641 -21.358 1.00 47.65  ? 92  PHE A CZ  1 
ATOM   751  N  N   . GLU A 1 93  ? -6.046  -32.537 -19.209 1.00 50.01  ? 93  GLU A N   1 
ATOM   752  C  CA  . GLU A 1 93  ? -6.481  -33.949 -19.399 1.00 52.42  ? 93  GLU A CA  1 
ATOM   753  C  C   . GLU A 1 93  ? -7.770  -33.945 -20.225 1.00 54.53  ? 93  GLU A C   1 
ATOM   754  O  O   . GLU A 1 93  ? -8.434  -32.898 -20.279 1.00 55.64  ? 93  GLU A O   1 
ATOM   755  C  CB  . GLU A 1 93  ? -6.656  -34.671 -18.065 1.00 54.64  ? 93  GLU A CB  1 
ATOM   756  C  CG  . GLU A 1 93  ? -5.353  -34.878 -17.319 1.00 57.18  ? 93  GLU A CG  1 
ATOM   757  C  CD  . GLU A 1 93  ? -5.474  -34.792 -15.809 1.00 61.14  ? 93  GLU A CD  1 
ATOM   758  O  OE1 . GLU A 1 93  ? -4.420  -34.620 -15.145 1.00 61.76  ? 93  GLU A OE1 1 
ATOM   759  O  OE2 . GLU A 1 93  ? -6.616  -34.883 -15.302 1.00 64.98  ? 93  GLU A OE2 1 
ATOM   760  N  N   . ASP A 1 94  ? -8.117  -35.087 -20.823 1.00 57.30  ? 94  ASP A N   1 
ATOM   761  C  CA  . ASP A 1 94  ? -9.074  -35.185 -21.958 1.00 59.25  ? 94  ASP A CA  1 
ATOM   762  C  C   . ASP A 1 94  ? -10.526 -35.084 -21.462 1.00 56.78  ? 94  ASP A C   1 
ATOM   763  O  O   . ASP A 1 94  ? -11.440 -35.344 -22.271 1.00 57.74  ? 94  ASP A O   1 
ATOM   764  C  CB  . ASP A 1 94  ? -8.816  -36.463 -22.765 1.00 64.29  ? 94  ASP A CB  1 
ATOM   765  C  CG  . ASP A 1 94  ? -8.621  -37.719 -21.927 1.00 72.54  ? 94  ASP A CG  1 
ATOM   766  O  OD1 . ASP A 1 94  ? -8.390  -37.584 -20.704 1.00 79.94  ? 94  ASP A OD1 1 
ATOM   767  O  OD2 . ASP A 1 94  ? -8.706  -38.831 -22.502 1.00 78.24  ? 94  ASP A OD2 1 
ATOM   768  N  N   . ASP A 1 95  ? -10.746 -34.675 -20.210 1.00 56.54  ? 95  ASP A N   1 
ATOM   769  C  CA  . ASP A 1 95  ? -12.068 -34.757 -19.533 1.00 56.55  ? 95  ASP A CA  1 
ATOM   770  C  C   . ASP A 1 95  ? -12.494 -33.378 -19.016 1.00 54.21  ? 95  ASP A C   1 
ATOM   771  O  O   . ASP A 1 95  ? -13.280 -33.331 -18.055 1.00 53.82  ? 95  ASP A O   1 
ATOM   772  C  CB  . ASP A 1 95  ? -12.029 -35.787 -18.399 1.00 57.44  ? 95  ASP A CB  1 
ATOM   773  C  CG  . ASP A 1 95  ? -11.100 -35.436 -17.247 1.00 58.11  ? 95  ASP A CG  1 
ATOM   774  O  OD1 . ASP A 1 95  ? -10.424 -34.392 -17.320 1.00 59.49  ? 95  ASP A OD1 1 
ATOM   775  O  OD2 . ASP A 1 95  ? -11.057 -36.216 -16.284 1.00 60.24  ? 95  ASP A OD2 1 
ATOM   776  N  N   . ILE A 1 96  ? -12.017 -32.297 -19.635 1.00 53.50  ? 96  ILE A N   1 
ATOM   777  C  CA  . ILE A 1 96  ? -12.284 -30.899 -19.175 1.00 54.88  ? 96  ILE A CA  1 
ATOM   778  C  C   . ILE A 1 96  ? -13.423 -30.289 -19.992 1.00 55.97  ? 96  ILE A C   1 
ATOM   779  O  O   . ILE A 1 96  ? -13.798 -30.874 -21.021 1.00 61.99  ? 96  ILE A O   1 
ATOM   780  C  CB  . ILE A 1 96  ? -11.027 -30.023 -19.288 1.00 56.03  ? 96  ILE A CB  1 
ATOM   781  C  CG1 . ILE A 1 96  ? -10.436 -30.071 -20.697 1.00 60.47  ? 96  ILE A CG1 1 
ATOM   782  C  CG2 . ILE A 1 96  ? -10.012 -30.397 -18.228 1.00 56.66  ? 96  ILE A CG2 1 
ATOM   783  C  CD1 . ILE A 1 96  ? -9.702  -28.819 -21.073 1.00 64.75  ? 96  ILE A CD1 1 
ATOM   784  N  N   . LEU A 1 97  ? -13.908 -29.128 -19.540 1.00 56.30  ? 97  LEU A N   1 
ATOM   785  C  CA  . LEU A 1 97  ? -14.761 -28.173 -20.295 1.00 55.98  ? 97  LEU A CA  1 
ATOM   786  C  C   . LEU A 1 97  ? -14.107 -26.796 -20.201 1.00 52.48  ? 97  LEU A C   1 
ATOM   787  O  O   . LEU A 1 97  ? -13.499 -26.518 -19.158 1.00 49.09  ? 97  LEU A O   1 
ATOM   788  C  CB  . LEU A 1 97  ? -16.159 -28.134 -19.673 1.00 59.84  ? 97  LEU A CB  1 
ATOM   789  C  CG  . LEU A 1 97  ? -16.860 -29.479 -19.489 1.00 64.88  ? 97  LEU A CG  1 
ATOM   790  C  CD1 . LEU A 1 97  ? -18.175 -29.278 -18.758 1.00 66.47  ? 97  LEU A CD1 1 
ATOM   791  C  CD2 . LEU A 1 97  ? -17.107 -30.167 -20.823 1.00 65.84  ? 97  LEU A CD2 1 
ATOM   792  N  N   . LEU A 1 98  ? -14.246 -25.966 -21.236 1.00 50.68  ? 98  LEU A N   1 
ATOM   793  C  CA  . LEU A 1 98  ? -13.567 -24.645 -21.309 1.00 52.58  ? 98  LEU A CA  1 
ATOM   794  C  C   . LEU A 1 98  ? -14.537 -23.519 -20.950 1.00 51.85  ? 98  LEU A C   1 
ATOM   795  O  O   . LEU A 1 98  ? -15.752 -23.699 -21.123 1.00 53.71  ? 98  LEU A O   1 
ATOM   796  C  CB  . LEU A 1 98  ? -12.994 -24.448 -22.715 1.00 55.26  ? 98  LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 98  ? -11.930 -25.459 -23.144 1.00 55.54  ? 98  LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 98  ? -11.320 -25.063 -24.477 1.00 57.65  ? 98  LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 98  ? -10.850 -25.594 -22.089 1.00 54.59  ? 98  LEU A CD2 1 
ATOM   800  N  N   . GLY A 1 99  ? -13.981 -22.403 -20.470 1.00 52.90  ? 99  GLY A N   1 
ATOM   801  C  CA  . GLY A 1 99  ? -14.705 -21.165 -20.131 1.00 56.70  ? 99  GLY A CA  1 
ATOM   802  C  C   . GLY A 1 99  ? -15.316 -20.524 -21.362 1.00 58.21  ? 99  GLY A C   1 
ATOM   803  O  O   . GLY A 1 99  ? -15.647 -21.260 -22.307 1.00 54.79  ? 99  GLY A O   1 
ATOM   804  N  N   . GLU A 1 100 ? -15.490 -19.203 -21.332 1.00 64.15  ? 100 GLU A N   1 
ATOM   805  C  CA  . GLU A 1 100 ? -16.141 -18.430 -22.417 1.00 74.12  ? 100 GLU A CA  1 
ATOM   806  C  C   . GLU A 1 100 ? -15.075 -17.666 -23.201 1.00 79.15  ? 100 GLU A C   1 
ATOM   807  O  O   . GLU A 1 100 ? -15.056 -17.771 -24.443 1.00 76.95  ? 100 GLU A O   1 
ATOM   808  C  CB  . GLU A 1 100 ? -17.181 -17.477 -21.831 1.00 80.31  ? 100 GLU A CB  1 
ATOM   809  C  CG  . GLU A 1 100 ? -18.201 -17.011 -22.851 1.00 86.25  ? 100 GLU A CG  1 
ATOM   810  C  CD  . GLU A 1 100 ? -19.633 -16.978 -22.344 1.00 91.19  ? 100 GLU A CD  1 
ATOM   811  O  OE1 . GLU A 1 100 ? -20.386 -16.091 -22.779 1.00 94.55  ? 100 GLU A OE1 1 
ATOM   812  O  OE2 . GLU A 1 100 ? -19.991 -17.848 -21.523 1.00 97.87  ? 100 GLU A OE2 1 
ATOM   813  N  N   . ASN A 1 101 ? -14.200 -16.955 -22.491 1.00 86.55  ? 101 ASN A N   1 
ATOM   814  C  CA  . ASN A 1 101 ? -13.093 -16.159 -23.084 1.00 90.77  ? 101 ASN A CA  1 
ATOM   815  C  C   . ASN A 1 101 ? -11.791 -16.959 -22.991 1.00 86.42  ? 101 ASN A C   1 
ATOM   816  O  O   . ASN A 1 101 ? -10.729 -16.333 -22.809 1.00 87.97  ? 101 ASN A O   1 
ATOM   817  C  CB  . ASN A 1 101 ? -12.944 -14.801 -22.394 1.00 95.83  ? 101 ASN A CB  1 
ATOM   818  C  CG  . ASN A 1 101 ? -14.217 -13.982 -22.423 1.00 97.36  ? 101 ASN A CG  1 
ATOM   819  O  OD1 . ASN A 1 101 ? -14.896 -13.922 -23.448 1.00 100.00 ? 101 ASN A OD1 1 
ATOM   820  N  ND2 . ASN A 1 101 ? -14.545 -13.347 -21.309 1.00 95.06  ? 101 ASN A ND2 1 
ATOM   821  N  N   . ALA A 1 102 ? -11.868 -18.287 -23.110 1.00 80.10  ? 102 ALA A N   1 
ATOM   822  C  CA  . ALA A 1 102 ? -10.704 -19.199 -23.061 1.00 78.37  ? 102 ALA A CA  1 
ATOM   823  C  C   . ALA A 1 102 ? -9.689  -18.770 -24.128 1.00 78.75  ? 102 ALA A C   1 
ATOM   824  O  O   . ALA A 1 102 ? -8.487  -18.742 -23.816 1.00 74.83  ? 102 ALA A O   1 
ATOM   825  C  CB  . ALA A 1 102 ? -11.160 -20.624 -23.243 1.00 76.45  ? 102 ALA A CB  1 
ATOM   826  N  N   . ASN A 1 103 ? -10.113 -18.348 -25.302 1.00 78.00  ? 103 ASN A N   1 
ATOM   827  C  CA  . ASN A 1 103 ? -9.170  -17.910 -26.308 1.00 77.80  ? 103 ASN A CA  1 
ATOM   828  C  C   . ASN A 1 103 ? -8.220  -16.875 -25.794 1.00 76.86  ? 103 ASN A C   1 
ATOM   829  O  O   . ASN A 1 103 ? -7.016  -17.007 -25.938 1.00 76.17  ? 103 ASN A O   1 
ATOM   830  C  CB  . ASN A 1 103 ? -9.879  -17.253 -27.489 1.00 79.20  ? 103 ASN A CB  1 
ATOM   831  C  CG  . ASN A 1 103 ? -11.194 -17.892 -27.829 1.00 81.28  ? 103 ASN A CG  1 
ATOM   832  O  OD1 . ASN A 1 103 ? -11.665 -18.761 -27.126 1.00 81.72  ? 103 ASN A OD1 1 
ATOM   833  N  ND2 . ASN A 1 103 ? -11.791 -17.463 -28.928 1.00 83.69  ? 103 ASN A ND2 1 
ATOM   834  N  N   . LYS A 1 104 ? -8.755  -15.835 -25.194 1.00 76.34  ? 104 LYS A N   1 
ATOM   835  C  CA  . LYS A 1 104 ? -7.910  -14.684 -24.773 1.00 81.10  ? 104 LYS A CA  1 
ATOM   836  C  C   . LYS A 1 104 ? -6.738  -15.174 -23.916 1.00 78.60  ? 104 LYS A C   1 
ATOM   837  O  O   . LYS A 1 104 ? -5.695  -14.496 -23.920 1.00 79.30  ? 104 LYS A O   1 
ATOM   838  C  CB  . LYS A 1 104 ? -8.742  -13.650 -24.005 1.00 89.62  ? 104 LYS A CB  1 
ATOM   839  C  CG  . LYS A 1 104 ? -9.588  -12.715 -24.863 1.00 97.63  ? 104 LYS A CG  1 
ATOM   840  C  CD  . LYS A 1 104 ? -8.787  -11.683 -25.656 1.00 100.77 ? 104 LYS A CD  1 
ATOM   841  C  CE  . LYS A 1 104 ? -9.483  -10.343 -25.822 1.00 99.64  ? 104 LYS A CE  1 
ATOM   842  N  NZ  . LYS A 1 104 ? -10.543 -10.371 -26.859 1.00 97.54  ? 104 LYS A NZ  1 
ATOM   843  N  N   . PHE A 1 105 ? -6.907  -16.300 -23.213 1.00 77.01  ? 105 PHE A N   1 
ATOM   844  C  CA  . PHE A 1 105 ? -5.911  -16.874 -22.273 1.00 71.12  ? 105 PHE A CA  1 
ATOM   845  C  C   . PHE A 1 105 ? -5.027  -17.907 -22.970 1.00 69.91  ? 105 PHE A C   1 
ATOM   846  O  O   . PHE A 1 105 ? -3.889  -18.080 -22.514 1.00 64.65  ? 105 PHE A O   1 
ATOM   847  C  CB  . PHE A 1 105 ? -6.604  -17.555 -21.092 1.00 71.37  ? 105 PHE A CB  1 
ATOM   848  C  CG  . PHE A 1 105 ? -7.430  -16.628 -20.245 1.00 69.02  ? 105 PHE A CG  1 
ATOM   849  C  CD1 . PHE A 1 105 ? -6.823  -15.786 -19.328 1.00 70.12  ? 105 PHE A CD1 1 
ATOM   850  C  CD2 . PHE A 1 105 ? -8.807  -16.592 -20.371 1.00 68.19  ? 105 PHE A CD2 1 
ATOM   851  C  CE1 . PHE A 1 105 ? -7.579  -14.924 -18.550 1.00 71.94  ? 105 PHE A CE1 1 
ATOM   852  C  CE2 . PHE A 1 105 ? -9.564  -15.735 -19.588 1.00 72.93  ? 105 PHE A CE2 1 
ATOM   853  C  CZ  . PHE A 1 105 ? -8.948  -14.903 -18.680 1.00 72.86  ? 105 PHE A CZ  1 
ATOM   854  N  N   . LEU A 1 106 ? -5.537  -18.567 -24.018 1.00 74.28  ? 106 LEU A N   1 
ATOM   855  C  CA  . LEU A 1 106 ? -4.908  -19.775 -24.624 1.00 76.31  ? 106 LEU A CA  1 
ATOM   856  C  C   . LEU A 1 106 ? -4.452  -19.503 -26.062 1.00 79.97  ? 106 LEU A C   1 
ATOM   857  O  O   . LEU A 1 106 ? -3.312  -19.904 -26.388 1.00 75.66  ? 106 LEU A O   1 
ATOM   858  C  CB  . LEU A 1 106 ? -5.915  -20.926 -24.565 1.00 74.33  ? 106 LEU A CB  1 
ATOM   859  C  CG  . LEU A 1 106 ? -6.393  -21.276 -23.157 1.00 71.63  ? 106 LEU A CG  1 
ATOM   860  C  CD1 . LEU A 1 106 ? -7.551  -22.252 -23.195 1.00 72.98  ? 106 LEU A CD1 1 
ATOM   861  C  CD2 . LEU A 1 106 ? -5.256  -21.846 -22.330 1.00 71.85  ? 106 LEU A CD2 1 
ATOM   862  N  N   . ALA A 1 107 ? -5.300  -18.873 -26.886 1.00 87.54  ? 107 ALA A N   1 
ATOM   863  C  CA  . ALA A 1 107 ? -4.987  -18.522 -28.293 1.00 90.52  ? 107 ALA A CA  1 
ATOM   864  C  C   . ALA A 1 107 ? -3.667  -17.740 -28.324 1.00 86.91  ? 107 ALA A C   1 
ATOM   865  O  O   . ALA A 1 107 ? -2.709  -18.225 -28.942 1.00 85.65  ? 107 ALA A O   1 
ATOM   866  C  CB  . ALA A 1 107 ? -6.126  -17.749 -28.921 1.00 93.15  ? 107 ALA A CB  1 
ATOM   867  N  N   . GLU A 1 108 ? -3.622  -16.598 -27.633 1.00 83.77  ? 108 GLU A N   1 
ATOM   868  C  CA  . GLU A 1 108 ? -2.416  -15.741 -27.466 1.00 87.04  ? 108 GLU A CA  1 
ATOM   869  C  C   . GLU A 1 108 ? -1.795  -16.023 -26.091 1.00 85.96  ? 108 GLU A C   1 
ATOM   870  O  O   . GLU A 1 108 ? -2.456  -16.684 -25.282 1.00 84.25  ? 108 GLU A O   1 
ATOM   871  C  CB  . GLU A 1 108 ? -2.806  -14.270 -27.622 1.00 92.07  ? 108 GLU A CB  1 
ATOM   872  C  CG  . GLU A 1 108 ? -3.676  -13.742 -26.488 1.00 97.18  ? 108 GLU A CG  1 
ATOM   873  C  CD  . GLU A 1 108 ? -2.985  -12.817 -25.498 1.00 101.30 ? 108 GLU A CD  1 
ATOM   874  O  OE1 . GLU A 1 108 ? -1.740  -12.835 -25.438 1.00 104.80 ? 108 GLU A OE1 1 
ATOM   875  O  OE2 . GLU A 1 108 ? -3.698  -12.083 -24.781 1.00 100.87 ? 108 GLU A OE2 1 
ATOM   876  N  N   . GLY A 1 109 ? -0.578  -15.528 -25.835 1.00 83.61  ? 109 GLY A N   1 
ATOM   877  C  CA  . GLY A 1 109 ? 0.160   -15.752 -24.572 1.00 81.03  ? 109 GLY A CA  1 
ATOM   878  C  C   . GLY A 1 109 ? 0.961   -14.535 -24.125 1.00 82.76  ? 109 GLY A C   1 
ATOM   879  O  O   . GLY A 1 109 ? 2.046   -14.723 -23.547 1.00 82.78  ? 109 GLY A O   1 
ATOM   880  N  N   . ASP A 1 110 ? 0.463   -13.324 -24.388 1.00 85.67  ? 110 ASP A N   1 
ATOM   881  C  CA  . ASP A 1 110 ? 1.192   -12.049 -24.149 1.00 89.34  ? 110 ASP A CA  1 
ATOM   882  C  C   . ASP A 1 110 ? 0.869   -11.551 -22.738 1.00 89.82  ? 110 ASP A C   1 
ATOM   883  O  O   . ASP A 1 110 ? 1.827   -11.256 -22.007 1.00 87.04  ? 110 ASP A O   1 
ATOM   884  C  CB  . ASP A 1 110 ? 0.886   -11.032 -25.250 1.00 93.19  ? 110 ASP A CB  1 
ATOM   885  C  CG  . ASP A 1 110 ? 1.334   -11.507 -26.625 1.00 98.16  ? 110 ASP A CG  1 
ATOM   886  O  OD1 . ASP A 1 110 ? 2.563   -11.538 -26.869 1.00 100.37 ? 110 ASP A OD1 1 
ATOM   887  O  OD2 . ASP A 1 110 ? 0.454   -11.877 -27.433 1.00 98.76  ? 110 ASP A OD2 1 
ATOM   888  N  N   . TRP A 1 111 ? -0.419  -11.491 -22.373 1.00 90.00  ? 111 TRP A N   1 
ATOM   889  C  CA  . TRP A 1 111 ? -0.927  -11.244 -20.989 1.00 86.82  ? 111 TRP A CA  1 
ATOM   890  C  C   . TRP A 1 111 ? -0.075  -12.001 -19.964 1.00 82.61  ? 111 TRP A C   1 
ATOM   891  O  O   . TRP A 1 111 ? 0.066   -11.524 -18.827 1.00 76.69  ? 111 TRP A O   1 
ATOM   892  C  CB  . TRP A 1 111 ? -2.395  -11.675 -20.862 1.00 84.31  ? 111 TRP A CB  1 
ATOM   893  C  CG  . TRP A 1 111 ? -2.581  -13.159 -20.959 1.00 81.59  ? 111 TRP A CG  1 
ATOM   894  C  CD1 . TRP A 1 111 ? -2.563  -13.913 -22.096 1.00 82.30  ? 111 TRP A CD1 1 
ATOM   895  C  CD2 . TRP A 1 111 ? -2.785  -14.084 -19.877 1.00 78.83  ? 111 TRP A CD2 1 
ATOM   896  N  NE1 . TRP A 1 111 ? -2.745  -15.235 -21.800 1.00 78.43  ? 111 TRP A NE1 1 
ATOM   897  C  CE2 . TRP A 1 111 ? -2.884  -15.373 -20.446 1.00 78.93  ? 111 TRP A CE2 1 
ATOM   898  C  CE3 . TRP A 1 111 ? -2.899  -13.953 -18.489 1.00 81.23  ? 111 TRP A CE3 1 
ATOM   899  C  CZ2 . TRP A 1 111 ? -3.104  -16.515 -19.678 1.00 77.18  ? 111 TRP A CZ2 1 
ATOM   900  C  CZ3 . TRP A 1 111 ? -3.112  -15.083 -17.728 1.00 77.11  ? 111 TRP A CZ3 1 
ATOM   901  C  CH2 . TRP A 1 111 ? -3.213  -16.345 -18.317 1.00 74.97  ? 111 TRP A CH2 1 
ATOM   902  N  N   . LEU A 1 112 ? 0.441   -13.162 -20.362 1.00 84.56  ? 112 LEU A N   1 
ATOM   903  C  CA  . LEU A 1 112 ? 1.278   -14.056 -19.525 1.00 90.81  ? 112 LEU A CA  1 
ATOM   904  C  C   . LEU A 1 112 ? 2.699   -13.491 -19.446 1.00 92.29  ? 112 LEU A C   1 
ATOM   905  O  O   . LEU A 1 112 ? 3.238   -13.421 -18.322 1.00 92.77  ? 112 LEU A O   1 
ATOM   906  C  CB  . LEU A 1 112 ? 1.252   -15.446 -20.167 1.00 96.12  ? 112 LEU A CB  1 
ATOM   907  C  CG  . LEU A 1 112 ? 1.120   -16.642 -19.228 1.00 98.82  ? 112 LEU A CG  1 
ATOM   908  C  CD1 . LEU A 1 112 ? 0.144   -16.376 -18.090 1.00 100.20 ? 112 LEU A CD1 1 
ATOM   909  C  CD2 . LEU A 1 112 ? 0.680   -17.871 -20.015 1.00 96.91  ? 112 LEU A CD2 1 
ATOM   910  N  N   . LYS A 1 113 ? 3.274   -13.105 -20.594 1.00 93.94  ? 113 LYS A N   1 
ATOM   911  C  CA  . LYS A 1 113 ? 4.639   -12.519 -20.693 1.00 94.72  ? 113 LYS A CA  1 
ATOM   912  C  C   . LYS A 1 113 ? 4.700   -11.246 -19.842 1.00 91.33  ? 113 LYS A C   1 
ATOM   913  O  O   . LYS A 1 113 ? 5.669   -11.104 -19.069 1.00 84.38  ? 113 LYS A O   1 
ATOM   914  C  CB  . LYS A 1 113 ? 5.011   -12.251 -22.157 1.00 100.12 ? 113 LYS A CB  1 
ATOM   915  C  CG  . LYS A 1 113 ? 6.490   -11.975 -22.432 1.00 105.31 ? 113 LYS A CG  1 
ATOM   916  C  CD  . LYS A 1 113 ? 7.259   -13.123 -23.078 1.00 105.88 ? 113 LYS A CD  1 
ATOM   917  C  CE  . LYS A 1 113 ? 8.722   -12.811 -23.337 1.00 102.55 ? 113 LYS A CE  1 
ATOM   918  N  NZ  . LYS A 1 113 ? 8.962   -12.359 -24.729 1.00 100.27 ? 113 LYS A NZ  1 
ATOM   919  N  N   . VAL A 1 114 ? 3.678   -10.388 -19.949 1.00 91.21  ? 114 VAL A N   1 
ATOM   920  C  CA  . VAL A 1 114 ? 3.647   -9.030  -19.324 1.00 90.73  ? 114 VAL A CA  1 
ATOM   921  C  C   . VAL A 1 114 ? 3.562   -9.164  -17.795 1.00 89.47  ? 114 VAL A C   1 
ATOM   922  O  O   . VAL A 1 114 ? 3.930   -8.186  -17.120 1.00 89.66  ? 114 VAL A O   1 
ATOM   923  C  CB  . VAL A 1 114 ? 2.510   -8.145  -19.886 1.00 90.53  ? 114 VAL A CB  1 
ATOM   924  C  CG1 . VAL A 1 114 ? 2.552   -8.051  -21.405 1.00 92.36  ? 114 VAL A CG1 1 
ATOM   925  C  CG2 . VAL A 1 114 ? 1.128   -8.585  -19.428 1.00 90.44  ? 114 VAL A CG2 1 
ATOM   926  N  N   . ARG A 1 115 ? 3.135   -10.321 -17.269 1.00 88.53  ? 115 ARG A N   1 
ATOM   927  C  CA  . ARG A 1 115 ? 2.730   -10.475 -15.843 1.00 85.64  ? 115 ARG A CA  1 
ATOM   928  C  C   . ARG A 1 115 ? 3.741   -11.305 -15.039 1.00 82.99  ? 115 ARG A C   1 
ATOM   929  O  O   . ARG A 1 115 ? 3.722   -11.182 -13.797 1.00 80.38  ? 115 ARG A O   1 
ATOM   930  C  CB  . ARG A 1 115 ? 1.329   -11.086 -15.773 1.00 84.28  ? 115 ARG A CB  1 
ATOM   931  C  CG  . ARG A 1 115 ? 0.220   -10.082 -16.046 1.00 83.48  ? 115 ARG A CG  1 
ATOM   932  C  CD  . ARG A 1 115 ? -1.161  -10.713 -16.056 1.00 85.70  ? 115 ARG A CD  1 
ATOM   933  N  NE  . ARG A 1 115 ? -2.225  -9.731  -16.226 1.00 88.87  ? 115 ARG A NE  1 
ATOM   934  C  CZ  . ARG A 1 115 ? -2.506  -9.085  -17.358 1.00 95.43  ? 115 ARG A CZ  1 
ATOM   935  N  NH1 . ARG A 1 115 ? -1.805  -9.305  -18.459 1.00 99.13  ? 115 ARG A NH1 1 
ATOM   936  N  NH2 . ARG A 1 115 ? -3.502  -8.215  -17.385 1.00 99.14  ? 115 ARG A NH2 1 
ATOM   937  N  N   . PHE A 1 116 ? 4.592   -12.105 -15.691 1.00 84.89  ? 116 PHE A N   1 
ATOM   938  C  CA  . PHE A 1 116 ? 5.475   -13.082 -15.001 1.00 86.05  ? 116 PHE A CA  1 
ATOM   939  C  C   . PHE A 1 116 ? 6.872   -13.119 -15.614 1.00 82.43  ? 116 PHE A C   1 
ATOM   940  O  O   . PHE A 1 116 ? 7.037   -12.871 -16.818 1.00 82.89  ? 116 PHE A O   1 
ATOM   941  C  CB  . PHE A 1 116 ? 4.904   -14.498 -15.074 1.00 91.67  ? 116 PHE A CB  1 
ATOM   942  C  CG  . PHE A 1 116 ? 3.547   -14.659 -14.443 1.00 95.91  ? 116 PHE A CG  1 
ATOM   943  C  CD1 . PHE A 1 116 ? 3.397   -14.677 -13.065 1.00 94.48  ? 116 PHE A CD1 1 
ATOM   944  C  CD2 . PHE A 1 116 ? 2.412   -14.751 -15.236 1.00 96.96  ? 116 PHE A CD2 1 
ATOM   945  C  CE1 . PHE A 1 116 ? 2.141   -14.804 -12.494 1.00 96.67  ? 116 PHE A CE1 1 
ATOM   946  C  CE2 . PHE A 1 116 ? 1.156   -14.876 -14.662 1.00 96.65  ? 116 PHE A CE2 1 
ATOM   947  C  CZ  . PHE A 1 116 ? 1.023   -14.904 -13.293 1.00 96.78  ? 116 PHE A CZ  1 
ATOM   948  N  N   . ASN A 1 117 ? 7.843   -13.465 -14.772 1.00 79.74  ? 117 ASN A N   1 
ATOM   949  C  CA  . ASN A 1 117 ? 9.187   -13.941 -15.178 1.00 82.21  ? 117 ASN A CA  1 
ATOM   950  C  C   . ASN A 1 117 ? 9.151   -15.473 -15.195 1.00 82.16  ? 117 ASN A C   1 
ATOM   951  O  O   . ASN A 1 117 ? 8.936   -16.056 -14.131 1.00 84.12  ? 117 ASN A O   1 
ATOM   952  C  CB  . ASN A 1 117 ? 10.268  -13.408 -14.240 1.00 83.92  ? 117 ASN A CB  1 
ATOM   953  C  CG  . ASN A 1 117 ? 11.572  -14.158 -14.396 1.00 84.64  ? 117 ASN A CG  1 
ATOM   954  O  OD1 . ASN A 1 117 ? 11.988  -14.453 -15.511 1.00 92.49  ? 117 ASN A OD1 1 
ATOM   955  N  ND2 . ASN A 1 117 ? 12.210  -14.493 -13.289 1.00 84.47  ? 117 ASN A ND2 1 
ATOM   956  N  N   . PHE A 1 118 ? 9.377   -16.089 -16.356 1.00 82.60  ? 118 PHE A N   1 
ATOM   957  C  CA  . PHE A 1 118 ? 9.094   -17.523 -16.635 1.00 84.54  ? 118 PHE A CA  1 
ATOM   958  C  C   . PHE A 1 118 ? 10.196  -18.456 -16.121 1.00 86.95  ? 118 PHE A C   1 
ATOM   959  O  O   . PHE A 1 118 ? 10.003  -19.684 -16.229 1.00 87.98  ? 118 PHE A O   1 
ATOM   960  C  CB  . PHE A 1 118 ? 8.937   -17.753 -18.136 1.00 87.65  ? 118 PHE A CB  1 
ATOM   961  C  CG  . PHE A 1 118 ? 7.787   -17.011 -18.758 1.00 90.04  ? 118 PHE A CG  1 
ATOM   962  C  CD1 . PHE A 1 118 ? 6.509   -17.541 -18.720 1.00 91.07  ? 118 PHE A CD1 1 
ATOM   963  C  CD2 . PHE A 1 118 ? 7.989   -15.795 -19.391 1.00 93.13  ? 118 PHE A CD2 1 
ATOM   964  C  CE1 . PHE A 1 118 ? 5.450   -16.868 -19.305 1.00 94.51  ? 118 PHE A CE1 1 
ATOM   965  C  CE2 . PHE A 1 118 ? 6.929   -15.123 -19.975 1.00 94.20  ? 118 PHE A CE2 1 
ATOM   966  C  CZ  . PHE A 1 118 ? 5.663   -15.664 -19.932 1.00 94.97  ? 118 PHE A CZ  1 
ATOM   967  N  N   . GLN A 1 119 ? 11.319  -17.928 -15.628 1.00 90.17  ? 119 GLN A N   1 
ATOM   968  C  CA  . GLN A 1 119 ? 12.401  -18.764 -15.038 1.00 95.35  ? 119 GLN A CA  1 
ATOM   969  C  C   . GLN A 1 119 ? 12.252  -18.768 -13.511 1.00 92.43  ? 119 GLN A C   1 
ATOM   970  O  O   . GLN A 1 119 ? 12.967  -19.550 -12.853 1.00 95.80  ? 119 GLN A O   1 
ATOM   971  C  CB  . GLN A 1 119 ? 13.793  -18.352 -15.524 1.00 103.87 ? 119 GLN A CB  1 
ATOM   972  C  CG  . GLN A 1 119 ? 14.085  -16.861 -15.469 1.00 110.07 ? 119 GLN A CG  1 
ATOM   973  C  CD  . GLN A 1 119 ? 15.389  -16.521 -16.152 1.00 114.63 ? 119 GLN A CD  1 
ATOM   974  O  OE1 . GLN A 1 119 ? 15.509  -15.506 -16.837 1.00 116.82 ? 119 GLN A OE1 1 
ATOM   975  N  NE2 . GLN A 1 119 ? 16.381  -17.383 -15.986 1.00 114.76 ? 119 GLN A NE2 1 
ATOM   976  N  N   . GLU A 1 120 ? 11.333  -17.955 -12.979 1.00 84.75  ? 120 GLU A N   1 
ATOM   977  C  CA  . GLU A 1 120 ? 10.745  -18.131 -11.624 1.00 78.93  ? 120 GLU A CA  1 
ATOM   978  C  C   . GLU A 1 120 ? 10.004  -19.467 -11.598 1.00 74.48  ? 120 GLU A C   1 
ATOM   979  O  O   . GLU A 1 120 ? 9.636   -19.962 -12.679 1.00 69.67  ? 120 GLU A O   1 
ATOM   980  C  CB  . GLU A 1 120 ? 9.775   -16.999 -11.274 1.00 81.67  ? 120 GLU A CB  1 
ATOM   981  C  CG  . GLU A 1 120 ? 10.378  -15.915 -10.403 1.00 86.25  ? 120 GLU A CG  1 
ATOM   982  C  CD  . GLU A 1 120 ? 9.688   -14.564 -10.503 1.00 88.86  ? 120 GLU A CD  1 
ATOM   983  O  OE1 . GLU A 1 120 ? 8.650   -14.475 -11.202 1.00 86.93  ? 120 GLU A OE1 1 
ATOM   984  O  OE2 . GLU A 1 120 ? 10.194  -13.602 -9.885  1.00 91.68  ? 120 GLU A OE2 1 
ATOM   985  N  N   . ILE A 1 121 ? 9.774   -20.003 -10.400 1.00 73.53  ? 121 ILE A N   1 
ATOM   986  C  CA  . ILE A 1 121 ? 9.424   -21.438 -10.164 1.00 73.11  ? 121 ILE A CA  1 
ATOM   987  C  C   . ILE A 1 121 ? 7.931   -21.536 -9.838  1.00 69.73  ? 121 ILE A C   1 
ATOM   988  O  O   . ILE A 1 121 ? 7.606   -22.074 -8.771  1.00 77.95  ? 121 ILE A O   1 
ATOM   989  C  CB  . ILE A 1 121 ? 10.272  -22.030 -9.011  1.00 73.65  ? 121 ILE A CB  1 
ATOM   990  C  CG1 . ILE A 1 121 ? 11.632  -21.344 -8.830  1.00 76.60  ? 121 ILE A CG1 1 
ATOM   991  C  CG2 . ILE A 1 121 ? 10.438  -23.532 -9.171  1.00 71.48  ? 121 ILE A CG2 1 
ATOM   992  C  CD1 . ILE A 1 121 ? 12.135  -21.382 -7.410  1.00 77.77  ? 121 ILE A CD1 1 
ATOM   993  N  N   . PHE A 1 122 ? 7.050   -21.077 -10.728 1.00 66.55  ? 122 PHE A N   1 
ATOM   994  C  CA  . PHE A 1 122 ? 5.598   -20.940 -10.448 1.00 63.86  ? 122 PHE A CA  1 
ATOM   995  C  C   . PHE A 1 122 ? 4.777   -21.860 -11.351 1.00 60.42  ? 122 PHE A C   1 
ATOM   996  O  O   . PHE A 1 122 ? 5.192   -22.153 -12.482 1.00 60.43  ? 122 PHE A O   1 
ATOM   997  C  CB  . PHE A 1 122 ? 5.132   -19.496 -10.623 1.00 66.48  ? 122 PHE A CB  1 
ATOM   998  C  CG  . PHE A 1 122 ? 5.118   -19.004 -12.048 1.00 68.91  ? 122 PHE A CG  1 
ATOM   999  C  CD1 . PHE A 1 122 ? 6.276   -18.514 -12.633 1.00 70.29  ? 122 PHE A CD1 1 
ATOM   1000 C  CD2 . PHE A 1 122 ? 3.952   -19.005 -12.797 1.00 69.76  ? 122 PHE A CD2 1 
ATOM   1001 C  CE1 . PHE A 1 122 ? 6.268   -18.042 -13.936 1.00 70.56  ? 122 PHE A CE1 1 
ATOM   1002 C  CE2 . PHE A 1 122 ? 3.947   -18.533 -14.101 1.00 70.24  ? 122 PHE A CE2 1 
ATOM   1003 C  CZ  . PHE A 1 122 ? 5.105   -18.059 -14.669 1.00 70.21  ? 122 PHE A CZ  1 
ATOM   1004 N  N   . VAL A 1 123 ? 3.645   -22.316 -10.818 1.00 58.54  ? 123 VAL A N   1 
ATOM   1005 C  CA  . VAL A 1 123 ? 2.523   -22.952 -11.567 1.00 56.74  ? 123 VAL A CA  1 
ATOM   1006 C  C   . VAL A 1 123 ? 1.340   -21.988 -11.488 1.00 58.00  ? 123 VAL A C   1 
ATOM   1007 O  O   . VAL A 1 123 ? 1.279   -21.208 -10.518 1.00 63.55  ? 123 VAL A O   1 
ATOM   1008 C  CB  . VAL A 1 123 ? 2.155   -24.329 -10.985 1.00 54.18  ? 123 VAL A CB  1 
ATOM   1009 C  CG1 . VAL A 1 123 ? 0.914   -24.914 -11.642 1.00 52.95  ? 123 VAL A CG1 1 
ATOM   1010 C  CG2 . VAL A 1 123 ? 3.316   -25.302 -11.069 1.00 55.74  ? 123 VAL A CG2 1 
ATOM   1011 N  N   . LEU A 1 124 ? 0.451   -22.035 -12.477 1.00 56.37  ? 124 LEU A N   1 
ATOM   1012 C  CA  . LEU A 1 124 ? -0.844  -21.314 -12.453 1.00 55.60  ? 124 LEU A CA  1 
ATOM   1013 C  C   . LEU A 1 124 ? -1.948  -22.301 -12.829 1.00 55.85  ? 124 LEU A C   1 
ATOM   1014 O  O   . LEU A 1 124 ? -1.999  -22.705 -13.998 1.00 56.74  ? 124 LEU A O   1 
ATOM   1015 C  CB  . LEU A 1 124 ? -0.789  -20.134 -13.424 1.00 54.64  ? 124 LEU A CB  1 
ATOM   1016 C  CG  . LEU A 1 124 ? -2.139  -19.502 -13.749 1.00 54.40  ? 124 LEU A CG  1 
ATOM   1017 C  CD1 . LEU A 1 124 ? -2.847  -19.061 -12.480 1.00 53.78  ? 124 LEU A CD1 1 
ATOM   1018 C  CD2 . LEU A 1 124 ? -1.970  -18.339 -14.709 1.00 55.32  ? 124 LEU A CD2 1 
ATOM   1019 N  N   . ARG A 1 125 ? -2.772  -22.683 -11.854 1.00 57.91  ? 125 ARG A N   1 
ATOM   1020 C  CA  . ARG A 1 125 ? -3.987  -23.502 -12.077 1.00 59.76  ? 125 ARG A CA  1 
ATOM   1021 C  C   . ARG A 1 125 ? -5.008  -22.640 -12.824 1.00 58.00  ? 125 ARG A C   1 
ATOM   1022 O  O   . ARG A 1 125 ? -5.225  -21.482 -12.410 1.00 54.45  ? 125 ARG A O   1 
ATOM   1023 C  CB  . ARG A 1 125 ? -4.569  -23.995 -10.750 1.00 64.82  ? 125 ARG A CB  1 
ATOM   1024 C  CG  . ARG A 1 125 ? -3.695  -24.996 -10.005 1.00 68.53  ? 125 ARG A CG  1 
ATOM   1025 C  CD  . ARG A 1 125 ? -4.168  -25.153 -8.576  1.00 73.82  ? 125 ARG A CD  1 
ATOM   1026 N  NE  . ARG A 1 125 ? -5.535  -25.656 -8.560  1.00 76.74  ? 125 ARG A NE  1 
ATOM   1027 C  CZ  . ARG A 1 125 ? -5.936  -26.777 -7.976  1.00 80.59  ? 125 ARG A CZ  1 
ATOM   1028 N  NH1 . ARG A 1 125 ? -5.088  -27.533 -7.296  1.00 77.55  ? 125 ARG A NH1 1 
ATOM   1029 N  NH2 . ARG A 1 125 ? -7.211  -27.125 -8.054  1.00 85.90  ? 125 ARG A NH2 1 
ATOM   1030 N  N   . LEU A 1 126 ? -5.583  -23.186 -13.895 1.00 58.64  ? 126 LEU A N   1 
ATOM   1031 C  CA  . LEU A 1 126 ? -6.612  -22.529 -14.741 1.00 57.94  ? 126 LEU A CA  1 
ATOM   1032 C  C   . LEU A 1 126 ? -7.972  -23.176 -14.481 1.00 57.26  ? 126 LEU A C   1 
ATOM   1033 O  O   . LEU A 1 126 ? -8.999  -22.502 -14.698 1.00 56.30  ? 126 LEU A O   1 
ATOM   1034 C  CB  . LEU A 1 126 ? -6.207  -22.703 -16.205 1.00 58.34  ? 126 LEU A CB  1 
ATOM   1035 C  CG  . LEU A 1 126 ? -4.781  -22.281 -16.550 1.00 55.87  ? 126 LEU A CG  1 
ATOM   1036 C  CD1 . LEU A 1 126 ? -4.293  -23.040 -17.776 1.00 56.14  ? 126 LEU A CD1 1 
ATOM   1037 C  CD2 . LEU A 1 126 ? -4.699  -20.776 -16.759 1.00 53.26  ? 126 LEU A CD2 1 
ATOM   1038 N  N   . GLU A 1 127 ? -7.951  -24.441 -14.041 1.00 59.10  ? 127 GLU A N   1 
ATOM   1039 C  CA  . GLU A 1 127 ? -9.123  -25.240 -13.591 1.00 58.15  ? 127 GLU A CA  1 
ATOM   1040 C  C   . GLU A 1 127 ? -9.713  -24.591 -12.341 1.00 56.25  ? 127 GLU A C   1 
ATOM   1041 O  O   . GLU A 1 127 ? -8.916  -24.058 -11.534 1.00 56.86  ? 127 GLU A O   1 
ATOM   1042 C  CB  . GLU A 1 127 ? -8.656  -26.665 -13.293 1.00 58.11  ? 127 GLU A CB  1 
ATOM   1043 C  CG  . GLU A 1 127 ? -9.781  -27.658 -13.069 1.00 60.50  ? 127 GLU A CG  1 
ATOM   1044 C  CD  . GLU A 1 127 ? -9.319  -29.036 -12.616 1.00 62.15  ? 127 GLU A CD  1 
ATOM   1045 O  OE1 . GLU A 1 127 ? -10.129 -29.739 -11.976 1.00 60.24  ? 127 GLU A OE1 1 
ATOM   1046 O  OE2 . GLU A 1 127 ? -8.161  -29.407 -12.899 1.00 63.65  ? 127 GLU A OE2 1 
ATOM   1047 N  N   . THR A 1 128 ? -11.042 -24.626 -12.185 1.00 57.17  ? 128 THR A N   1 
ATOM   1048 C  CA  . THR A 1 128 ? -11.706 -24.178 -10.933 1.00 60.12  ? 128 THR A CA  1 
ATOM   1049 C  C   . THR A 1 128 ? -11.031 -24.953 -9.804  1.00 60.27  ? 128 THR A C   1 
ATOM   1050 O  O   . THR A 1 128 ? -10.453 -26.054 -10.084 1.00 58.28  ? 128 THR A O   1 
ATOM   1051 C  CB  . THR A 1 128 ? -13.223 -24.411 -10.885 1.00 61.72  ? 128 THR A CB  1 
ATOM   1052 O  OG1 . THR A 1 128 ? -13.465 -25.731 -11.372 1.00 66.82  ? 128 THR A OG1 1 
ATOM   1053 C  CG2 . THR A 1 128 ? -14.042 -23.397 -11.654 1.00 60.96  ? 128 THR A CG2 1 
ATOM   1054 N  N   . PHE A 1 129 ? -11.049 -24.397 -8.595  1.00 61.28  ? 129 PHE A N   1 
ATOM   1055 C  CA  . PHE A 1 129 ? -10.542 -25.117 -7.408  1.00 58.77  ? 129 PHE A CA  1 
ATOM   1056 C  C   . PHE A 1 129 ? -11.633 -26.081 -6.945  1.00 54.89  ? 129 PHE A C   1 
ATOM   1057 O  O   . PHE A 1 129 ? -12.778 -25.654 -6.695  1.00 49.63  ? 129 PHE A O   1 
ATOM   1058 C  CB  . PHE A 1 129 ? -10.086 -24.199 -6.276  1.00 60.61  ? 129 PHE A CB  1 
ATOM   1059 C  CG  . PHE A 1 129 ? -9.410  -24.998 -5.194  1.00 63.11  ? 129 PHE A CG  1 
ATOM   1060 C  CD1 . PHE A 1 129 ? -8.147  -25.528 -5.405  1.00 66.30  ? 129 PHE A CD1 1 
ATOM   1061 C  CD2 . PHE A 1 129 ? -10.073 -25.322 -4.024  1.00 61.68  ? 129 PHE A CD2 1 
ATOM   1062 C  CE1 . PHE A 1 129 ? -7.532  -26.312 -4.443  1.00 66.20  ? 129 PHE A CE1 1 
ATOM   1063 C  CE2 . PHE A 1 129 ? -9.458  -26.109 -3.065  1.00 64.74  ? 129 PHE A CE2 1 
ATOM   1064 C  CZ  . PHE A 1 129 ? -8.187  -26.596 -3.272  1.00 65.38  ? 129 PHE A CZ  1 
ATOM   1065 N  N   . LEU A 1 130 ? -11.279 -27.361 -6.946  1.00 55.03  ? 130 LEU A N   1 
ATOM   1066 C  CA  . LEU A 1 130 ? -12.106 -28.473 -6.427  1.00 54.60  ? 130 LEU A CA  1 
ATOM   1067 C  C   . LEU A 1 130 ? -11.449 -29.001 -5.149  1.00 50.66  ? 130 LEU A C   1 
ATOM   1068 O  O   . LEU A 1 130 ? -10.208 -29.166 -5.137  1.00 48.13  ? 130 LEU A O   1 
ATOM   1069 C  CB  . LEU A 1 130 ? -12.217 -29.529 -7.528  1.00 56.34  ? 130 LEU A CB  1 
ATOM   1070 C  CG  . LEU A 1 130 ? -12.659 -28.963 -8.875  1.00 60.29  ? 130 LEU A CG  1 
ATOM   1071 C  CD1 . LEU A 1 130 ? -12.638 -30.031 -9.955  1.00 64.89  ? 130 LEU A CD1 1 
ATOM   1072 C  CD2 . LEU A 1 130 ? -14.042 -28.332 -8.775  1.00 59.83  ? 130 LEU A CD2 1 
HETATM 1073 N  N   . MSE A 1 131 ? -12.260 -29.208 -4.114  1.00 47.64  ? 131 MSE A N   1 
HETATM 1074 C  CA  . MSE A 1 131 ? -11.847 -29.745 -2.797  1.00 48.38  ? 131 MSE A CA  1 
HETATM 1075 C  C   . MSE A 1 131 ? -10.876 -30.905 -2.973  1.00 48.08  ? 131 MSE A C   1 
HETATM 1076 O  O   . MSE A 1 131 ? -11.151 -31.864 -3.685  1.00 50.72  ? 131 MSE A O   1 
HETATM 1077 C  CB  . MSE A 1 131 ? -13.080 -30.217 -2.033  1.00 49.14  ? 131 MSE A CB  1 
HETATM 1078 C  CG  . MSE A 1 131 ? -13.807 -29.104 -1.336  1.00 51.48  ? 131 MSE A CG  1 
HETATM 1079 SE SE  . MSE A 1 131 ? -15.317 -29.841 -0.343  1.00 55.08  ? 131 MSE A SE  1 
HETATM 1080 C  CE  . MSE A 1 131 ? -14.702 -31.361 0.745   1.00 56.02  ? 131 MSE A CE  1 
ATOM   1081 N  N   . PRO A 1 132 ? -9.722  -30.874 -2.281  1.00 49.01  ? 132 PRO A N   1 
ATOM   1082 C  CA  . PRO A 1 132 ? -8.771  -31.975 -2.334  1.00 54.12  ? 132 PRO A CA  1 
ATOM   1083 C  C   . PRO A 1 132 ? -9.239  -33.172 -1.501  1.00 62.54  ? 132 PRO A C   1 
ATOM   1084 O  O   . PRO A 1 132 ? -8.456  -34.060 -1.323  1.00 74.07  ? 132 PRO A O   1 
ATOM   1085 C  CB  . PRO A 1 132 ? -7.493  -31.354 -1.756  1.00 50.89  ? 132 PRO A CB  1 
ATOM   1086 C  CG  . PRO A 1 132 ? -8.016  -30.350 -0.774  1.00 50.13  ? 132 PRO A CG  1 
ATOM   1087 C  CD  . PRO A 1 132 ? -9.264  -29.786 -1.415  1.00 48.36  ? 132 PRO A CD  1 
ATOM   1088 N  N   . VAL A 1 133 ? -10.477 -33.166 -1.005  1.00 69.68  ? 133 VAL A N   1 
ATOM   1089 C  CA  . VAL A 1 133 ? -11.053 -34.311 -0.243  1.00 72.03  ? 133 VAL A CA  1 
ATOM   1090 C  C   . VAL A 1 133 ? -12.461 -34.597 -0.772  1.00 70.46  ? 133 VAL A C   1 
ATOM   1091 O  O   . VAL A 1 133 ? -13.170 -33.635 -1.132  1.00 68.24  ? 133 VAL A O   1 
ATOM   1092 C  CB  . VAL A 1 133 ? -11.043 -34.033 1.271   1.00 80.96  ? 133 VAL A CB  1 
ATOM   1093 C  CG1 . VAL A 1 133 ? -11.674 -35.165 2.064   1.00 83.90  ? 133 VAL A CG1 1 
ATOM   1094 C  CG2 . VAL A 1 133 ? -9.630  -33.762 1.768   1.00 88.57  ? 133 VAL A CG2 1 
ATOM   1095 N  N   . GLN A 1 134 ? -12.812 -35.881 -0.877  1.00 67.68  ? 134 GLN A N   1 
ATOM   1096 C  CA  . GLN A 1 134 ? -14.170 -36.374 -1.222  1.00 65.35  ? 134 GLN A CA  1 
ATOM   1097 C  C   . GLN A 1 134 ? -14.266 -37.831 -0.753  1.00 60.53  ? 134 GLN A C   1 
ATOM   1098 O  O   . GLN A 1 134 ? -13.236 -38.377 -0.301  1.00 58.96  ? 134 GLN A O   1 
ATOM   1099 C  CB  . GLN A 1 134 ? -14.438 -36.151 -2.712  1.00 68.95  ? 134 GLN A CB  1 
ATOM   1100 C  CG  . GLN A 1 134 ? -13.518 -36.921 -3.650  1.00 76.55  ? 134 GLN A CG  1 
ATOM   1101 C  CD  . GLN A 1 134 ? -12.088 -36.429 -3.687  1.00 78.99  ? 134 GLN A CD  1 
ATOM   1102 O  OE1 . GLN A 1 134 ? -11.787 -35.299 -4.074  1.00 82.17  ? 134 GLN A OE1 1 
ATOM   1103 N  NE2 . GLN A 1 134 ? -11.182 -37.303 -3.293  1.00 77.61  ? 134 GLN A NE2 1 
ATOM   1104 N  N   . LEU A 1 135 ? -15.462 -38.415 -0.782  1.00 58.26  ? 135 LEU A N   1 
ATOM   1105 C  CA  . LEU A 1 135 ? -15.749 -39.717 -0.124  1.00 60.38  ? 135 LEU A CA  1 
ATOM   1106 C  C   . LEU A 1 135 ? -16.342 -40.708 -1.131  1.00 61.69  ? 135 LEU A C   1 
ATOM   1107 O  O   . LEU A 1 135 ? -17.016 -40.262 -2.068  1.00 61.01  ? 135 LEU A O   1 
ATOM   1108 C  CB  . LEU A 1 135 ? -16.673 -39.501 1.085   1.00 61.29  ? 135 LEU A CB  1 
ATOM   1109 C  CG  . LEU A 1 135 ? -17.911 -38.622 0.894   1.00 57.87  ? 135 LEU A CG  1 
ATOM   1110 C  CD1 . LEU A 1 135 ? -18.873 -39.226 -0.122  1.00 59.22  ? 135 LEU A CD1 1 
ATOM   1111 C  CD2 . LEU A 1 135 ? -18.618 -38.404 2.223   1.00 53.78  ? 135 LEU A CD2 1 
ATOM   1112 N  N   . GLU A 1 136 ? -16.084 -42.003 -0.928  1.00 67.20  ? 136 GLU A N   1 
ATOM   1113 C  CA  . GLU A 1 136 ? -16.599 -43.128 -1.756  1.00 72.18  ? 136 GLU A CA  1 
ATOM   1114 C  C   . GLU A 1 136 ? -17.487 -44.014 -0.881  1.00 69.05  ? 136 GLU A C   1 
ATOM   1115 O  O   . GLU A 1 136 ? -17.192 -44.113 0.326   1.00 66.26  ? 136 GLU A O   1 
ATOM   1116 C  CB  . GLU A 1 136 ? -15.456 -43.974 -2.315  1.00 77.50  ? 136 GLU A CB  1 
ATOM   1117 C  CG  . GLU A 1 136 ? -14.484 -43.220 -3.202  1.00 83.63  ? 136 GLU A CG  1 
ATOM   1118 C  CD  . GLU A 1 136 ? -13.177 -43.960 -3.449  1.00 90.30  ? 136 GLU A CD  1 
ATOM   1119 O  OE1 . GLU A 1 136 ? -13.129 -45.189 -3.213  1.00 91.79  ? 136 GLU A OE1 1 
ATOM   1120 O  OE2 . GLU A 1 136 ? -12.205 -43.304 -3.872  1.00 97.67  ? 136 GLU A OE2 1 
ATOM   1121 N  N   . LYS A 1 137 ? -18.516 -44.631 -1.472  1.00 67.23  ? 137 LYS A N   1 
ATOM   1122 C  CA  . LYS A 1 137 ? -19.466 -45.523 -0.759  1.00 66.11  ? 137 LYS A CA  1 
ATOM   1123 C  C   . LYS A 1 137 ? -18.750 -46.827 -0.425  1.00 65.09  ? 137 LYS A C   1 
ATOM   1124 O  O   . LYS A 1 137 ? -17.855 -47.214 -1.184  1.00 62.04  ? 137 LYS A O   1 
ATOM   1125 C  CB  . LYS A 1 137 ? -20.738 -45.776 -1.572  1.00 67.88  ? 137 LYS A CB  1 
ATOM   1126 C  CG  . LYS A 1 137 ? -21.760 -44.651 -1.522  1.00 72.71  ? 137 LYS A CG  1 
ATOM   1127 C  CD  . LYS A 1 137 ? -23.188 -45.134 -1.479  1.00 78.06  ? 137 LYS A CD  1 
ATOM   1128 C  CE  . LYS A 1 137 ? -24.180 -44.008 -1.662  1.00 83.01  ? 137 LYS A CE  1 
ATOM   1129 N  NZ  . LYS A 1 137 ? -25.539 -44.519 -1.957  1.00 86.29  ? 137 LYS A NZ  1 
ATOM   1130 N  N   . GLN A 1 138 ? -19.118 -47.433 0.705   1.00 68.98  ? 138 GLN A N   1 
ATOM   1131 C  CA  . GLN A 1 138 ? -18.499 -48.662 1.253   1.00 74.12  ? 138 GLN A CA  1 
ATOM   1132 C  C   . GLN A 1 138 ? -19.420 -49.841 0.960   1.00 77.65  ? 138 GLN A C   1 
ATOM   1133 O  O   . GLN A 1 138 ? -20.649 -49.641 0.982   1.00 81.24  ? 138 GLN A O   1 
ATOM   1134 C  CB  . GLN A 1 138 ? -18.282 -48.524 2.764   1.00 78.11  ? 138 GLN A CB  1 
ATOM   1135 C  CG  . GLN A 1 138 ? -17.378 -49.594 3.351   1.00 78.81  ? 138 GLN A CG  1 
ATOM   1136 C  CD  . GLN A 1 138 ? -15.947 -49.462 2.887   1.00 84.43  ? 138 GLN A CD  1 
ATOM   1137 O  OE1 . GLN A 1 138 ? -15.625 -48.716 1.960   1.00 82.63  ? 138 GLN A OE1 1 
ATOM   1138 N  NE2 . GLN A 1 138 ? -15.067 -50.201 3.538   1.00 86.41  ? 138 GLN A NE2 1 
ATOM   1139 N  N   . THR A 1 139 ? -18.836 -51.016 0.718   1.00 80.60  ? 139 THR A N   1 
ATOM   1140 C  CA  . THR A 1 139 ? -19.549 -52.319 0.632   1.00 82.01  ? 139 THR A CA  1 
ATOM   1141 C  C   . THR A 1 139 ? -19.174 -53.205 1.828   1.00 82.64  ? 139 THR A C   1 
ATOM   1142 O  O   . THR A 1 139 ? -20.082 -53.883 2.364   1.00 85.49  ? 139 THR A O   1 
ATOM   1143 C  CB  . THR A 1 139 ? -19.231 -53.025 -0.689  1.00 81.12  ? 139 THR A CB  1 
ATOM   1144 O  OG1 . THR A 1 139 ? -17.845 -53.367 -0.660  1.00 81.05  ? 139 THR A OG1 1 
ATOM   1145 C  CG2 . THR A 1 139 ? -19.535 -52.175 -1.903  1.00 79.20  ? 139 THR A CG2 1 
ATOM   1146 N  N   . GLN A 1 140 ? -17.892 -53.206 2.211   1.00 81.13  ? 140 GLN A N   1 
ATOM   1147 C  CA  . GLN A 1 140 ? -17.316 -54.134 3.220   1.00 80.45  ? 140 GLN A CA  1 
ATOM   1148 C  C   . GLN A 1 140 ? -17.930 -53.818 4.587   1.00 80.08  ? 140 GLN A C   1 
ATOM   1149 O  O   . GLN A 1 140 ? -18.470 -54.757 5.204   1.00 79.43  ? 140 GLN A O   1 
ATOM   1150 C  CB  . GLN A 1 140 ? -15.789 -54.036 3.240   1.00 80.41  ? 140 GLN A CB  1 
ATOM   1151 C  CG  . GLN A 1 140 ? -15.141 -54.316 1.886   1.00 79.53  ? 140 GLN A CG  1 
ATOM   1152 C  CD  . GLN A 1 140 ? -13.888 -53.501 1.665   1.00 78.15  ? 140 GLN A CD  1 
ATOM   1153 O  OE1 . GLN A 1 140 ? -13.173 -53.163 2.608   1.00 74.54  ? 140 GLN A OE1 1 
ATOM   1154 N  NE2 . GLN A 1 140 ? -13.609 -53.177 0.410   1.00 75.73  ? 140 GLN A NE2 1 
ATOM   1155 N  N   . ILE A 1 141 ? -17.889 -52.546 5.014   1.00 78.93  ? 141 ILE A N   1 
ATOM   1156 C  CA  . ILE A 1 141 ? -18.324 -52.109 6.377   1.00 73.31  ? 141 ILE A CA  1 
ATOM   1157 C  C   . ILE A 1 141 ? -19.805 -51.720 6.373   1.00 70.59  ? 141 ILE A C   1 
ATOM   1158 O  O   . ILE A 1 141 ? -20.229 -50.756 5.735   1.00 65.99  ? 141 ILE A O   1 
ATOM   1159 C  CB  . ILE A 1 141 ? -17.444 -50.987 6.953   1.00 74.69  ? 141 ILE A CB  1 
ATOM   1160 C  CG1 . ILE A 1 141 ? -15.947 -51.286 6.832   1.00 74.44  ? 141 ILE A CG1 1 
ATOM   1161 C  CG2 . ILE A 1 141 ? -17.835 -50.722 8.396   1.00 77.23  ? 141 ILE A CG2 1 
ATOM   1162 C  CD1 . ILE A 1 141 ? -15.515 -52.535 7.558   1.00 73.31  ? 141 ILE A CD1 1 
ATOM   1163 N  N   . PRO A 1 142 ? -20.630 -52.467 7.134   1.00 73.15  ? 142 PRO A N   1 
ATOM   1164 C  CA  . PRO A 1 142 ? -22.086 -52.313 7.087   1.00 73.93  ? 142 PRO A CA  1 
ATOM   1165 C  C   . PRO A 1 142 ? -22.600 -50.999 7.673   1.00 73.84  ? 142 PRO A C   1 
ATOM   1166 O  O   . PRO A 1 142 ? -22.212 -50.610 8.771   1.00 74.48  ? 142 PRO A O   1 
ATOM   1167 C  CB  . PRO A 1 142 ? -22.598 -53.489 7.933   1.00 76.05  ? 142 PRO A CB  1 
ATOM   1168 C  CG  . PRO A 1 142 ? -21.447 -53.818 8.863   1.00 75.99  ? 142 PRO A CG  1 
ATOM   1169 C  CD  . PRO A 1 142 ? -20.193 -53.515 8.071   1.00 74.24  ? 142 PRO A CD  1 
ATOM   1170 N  N   . PRO A 1 143 ? -23.506 -50.290 6.966   1.00 72.88  ? 143 PRO A N   1 
ATOM   1171 C  CA  . PRO A 1 143 ? -24.178 -49.101 7.503   1.00 74.01  ? 143 PRO A CA  1 
ATOM   1172 C  C   . PRO A 1 143 ? -24.971 -49.305 8.805   1.00 73.50  ? 143 PRO A C   1 
ATOM   1173 O  O   . PRO A 1 143 ? -26.014 -49.933 8.763   1.00 72.28  ? 143 PRO A O   1 
ATOM   1174 C  CB  . PRO A 1 143 ? -25.172 -48.722 6.387   1.00 76.15  ? 143 PRO A CB  1 
ATOM   1175 C  CG  . PRO A 1 143 ? -24.553 -49.283 5.131   1.00 79.42  ? 143 PRO A CG  1 
ATOM   1176 C  CD  . PRO A 1 143 ? -23.904 -50.573 5.580   1.00 77.17  ? 143 PRO A CD  1 
ATOM   1177 N  N   . PHE A 1 144 ? -24.491 -48.737 9.917   1.00 74.97  ? 144 PHE A N   1 
ATOM   1178 C  CA  . PHE A 1 144 ? -25.186 -48.744 11.232  1.00 76.90  ? 144 PHE A CA  1 
ATOM   1179 C  C   . PHE A 1 144 ? -26.124 -47.539 11.348  1.00 76.57  ? 144 PHE A C   1 
ATOM   1180 O  O   . PHE A 1 144 ? -25.710 -46.433 10.985  1.00 80.11  ? 144 PHE A O   1 
ATOM   1181 C  CB  . PHE A 1 144 ? -24.192 -48.714 12.394  1.00 77.81  ? 144 PHE A CB  1 
ATOM   1182 C  CG  . PHE A 1 144 ? -24.846 -48.810 13.747  1.00 82.60  ? 144 PHE A CG  1 
ATOM   1183 C  CD1 . PHE A 1 144 ? -25.752 -49.823 14.030  1.00 86.34  ? 144 PHE A CD1 1 
ATOM   1184 C  CD2 . PHE A 1 144 ? -24.569 -47.880 14.735  1.00 83.93  ? 144 PHE A CD2 1 
ATOM   1185 C  CE1 . PHE A 1 144 ? -26.361 -49.905 15.273  1.00 85.90  ? 144 PHE A CE1 1 
ATOM   1186 C  CE2 . PHE A 1 144 ? -25.170 -47.969 15.982  1.00 83.01  ? 144 PHE A CE2 1 
ATOM   1187 C  CZ  . PHE A 1 144 ? -26.066 -48.979 16.247  1.00 84.29  ? 144 PHE A CZ  1 
ATOM   1188 N  N   . GLN A 1 145 ? -27.329 -47.761 11.882  1.00 77.36  ? 145 GLN A N   1 
ATOM   1189 C  CA  . GLN A 1 145 ? -28.364 -46.725 12.141  1.00 77.67  ? 145 GLN A CA  1 
ATOM   1190 C  C   . GLN A 1 145 ? -28.522 -45.844 10.895  1.00 78.38  ? 145 GLN A C   1 
ATOM   1191 O  O   . GLN A 1 145 ? -28.423 -44.612 11.039  1.00 80.88  ? 145 GLN A O   1 
ATOM   1192 C  CB  . GLN A 1 145 ? -27.980 -45.907 13.376  1.00 81.19  ? 145 GLN A CB  1 
ATOM   1193 C  CG  . GLN A 1 145 ? -29.169 -45.316 14.123  1.00 84.82  ? 145 GLN A CG  1 
ATOM   1194 C  CD  . GLN A 1 145 ? -29.752 -46.261 15.144  1.00 85.01  ? 145 GLN A CD  1 
ATOM   1195 O  OE1 . GLN A 1 145 ? -29.525 -47.470 15.106  1.00 83.95  ? 145 GLN A OE1 1 
ATOM   1196 N  NE2 . GLN A 1 145 ? -30.511 -45.706 16.078  1.00 85.60  ? 145 GLN A NE2 1 
ATOM   1197 N  N   . GLN A 1 146 ? -28.740 -46.466 9.728   1.00 80.24  ? 146 GLN A N   1 
ATOM   1198 C  CA  . GLN A 1 146 ? -28.984 -45.826 8.397   1.00 85.92  ? 146 GLN A CA  1 
ATOM   1199 C  C   . GLN A 1 146 ? -27.981 -44.686 8.139   1.00 78.51  ? 146 GLN A C   1 
ATOM   1200 O  O   . GLN A 1 146 ? -28.373 -43.641 7.569   1.00 74.66  ? 146 GLN A O   1 
ATOM   1201 C  CB  . GLN A 1 146 ? -30.448 -45.382 8.262   1.00 93.17  ? 146 GLN A CB  1 
ATOM   1202 C  CG  . GLN A 1 146 ? -30.880 -44.242 9.181   1.00 98.25  ? 146 GLN A CG  1 
ATOM   1203 C  CD  . GLN A 1 146 ? -31.388 -44.696 10.529  1.00 103.27 ? 146 GLN A CD  1 
ATOM   1204 O  OE1 . GLN A 1 146 ? -32.028 -45.738 10.655  1.00 105.15 ? 146 GLN A OE1 1 
ATOM   1205 N  NE2 . GLN A 1 146 ? -31.114 -43.908 11.557  1.00 105.79 ? 146 GLN A NE2 1 
ATOM   1206 N  N   . ARG A 1 147 ? -26.719 -44.911 8.507   1.00 72.05  ? 147 ARG A N   1 
ATOM   1207 C  CA  . ARG A 1 147 ? -25.580 -43.994 8.260   1.00 70.77  ? 147 ARG A CA  1 
ATOM   1208 C  C   . ARG A 1 147 ? -24.417 -44.809 7.691   1.00 68.77  ? 147 ARG A C   1 
ATOM   1209 O  O   . ARG A 1 147 ? -23.969 -45.744 8.389   1.00 69.07  ? 147 ARG A O   1 
ATOM   1210 C  CB  . ARG A 1 147 ? -25.139 -43.331 9.564   1.00 72.67  ? 147 ARG A CB  1 
ATOM   1211 C  CG  . ARG A 1 147 ? -26.074 -42.253 10.090  1.00 74.07  ? 147 ARG A CG  1 
ATOM   1212 C  CD  . ARG A 1 147 ? -25.434 -41.618 11.314  1.00 74.89  ? 147 ARG A CD  1 
ATOM   1213 N  NE  . ARG A 1 147 ? -25.927 -40.288 11.633  1.00 78.07  ? 147 ARG A NE  1 
ATOM   1214 C  CZ  . ARG A 1 147 ? -27.045 -40.021 12.303  1.00 82.03  ? 147 ARG A CZ  1 
ATOM   1215 N  NH1 . ARG A 1 147 ? -27.827 -40.999 12.736  1.00 82.38  ? 147 ARG A NH1 1 
ATOM   1216 N  NH2 . ARG A 1 147 ? -27.376 -38.762 12.536  1.00 82.39  ? 147 ARG A NH2 1 
ATOM   1217 N  N   . ASP A 1 148 ? -23.949 -44.470 6.484   1.00 65.98  ? 148 ASP A N   1 
ATOM   1218 C  CA  . ASP A 1 148 ? -22.830 -45.174 5.804   1.00 63.31  ? 148 ASP A CA  1 
ATOM   1219 C  C   . ASP A 1 148 ? -21.510 -44.806 6.480   1.00 58.30  ? 148 ASP A C   1 
ATOM   1220 O  O   . ASP A 1 148 ? -21.442 -43.740 7.127   1.00 54.87  ? 148 ASP A O   1 
ATOM   1221 C  CB  . ASP A 1 148 ? -22.754 -44.839 4.313   1.00 66.67  ? 148 ASP A CB  1 
ATOM   1222 C  CG  . ASP A 1 148 ? -23.997 -45.208 3.531   1.00 72.52  ? 148 ASP A CG  1 
ATOM   1223 O  OD1 . ASP A 1 148 ? -24.688 -46.167 3.943   1.00 72.56  ? 148 ASP A OD1 1 
ATOM   1224 O  OD2 . ASP A 1 148 ? -24.261 -44.531 2.509   1.00 80.08  ? 148 ASP A OD2 1 
ATOM   1225 N  N   . ILE A 1 149 ? -20.508 -45.666 6.307   1.00 56.80  ? 149 ILE A N   1 
ATOM   1226 C  CA  . ILE A 1 149 ? -19.083 -45.389 6.637   1.00 57.41  ? 149 ILE A CA  1 
ATOM   1227 C  C   . ILE A 1 149 ? -18.354 -45.204 5.307   1.00 55.61  ? 149 ILE A C   1 
ATOM   1228 O  O   . ILE A 1 149 ? -17.619 -46.108 4.889   1.00 59.10  ? 149 ILE A O   1 
ATOM   1229 C  CB  . ILE A 1 149 ? -18.491 -46.517 7.506   1.00 59.72  ? 149 ILE A CB  1 
ATOM   1230 C  CG1 . ILE A 1 149 ? -19.258 -46.672 8.823   1.00 60.70  ? 149 ILE A CG1 1 
ATOM   1231 C  CG2 . ILE A 1 149 ? -17.010 -46.292 7.762   1.00 60.32  ? 149 ILE A CG2 1 
ATOM   1232 C  CD1 . ILE A 1 149 ? -20.464 -47.579 8.748   1.00 62.78  ? 149 ILE A CD1 1 
ATOM   1233 N  N   . ASP A 1 150 ? -18.586 -44.069 4.650   1.00 53.13  ? 150 ASP A N   1 
ATOM   1234 C  CA  . ASP A 1 150 ? -17.911 -43.717 3.379   1.00 54.70  ? 150 ASP A CA  1 
ATOM   1235 C  C   . ASP A 1 150 ? -16.432 -43.491 3.691   1.00 54.59  ? 150 ASP A C   1 
ATOM   1236 O  O   . ASP A 1 150 ? -16.127 -43.083 4.828   1.00 51.66  ? 150 ASP A O   1 
ATOM   1237 C  CB  . ASP A 1 150 ? -18.584 -42.521 2.710   1.00 55.55  ? 150 ASP A CB  1 
ATOM   1238 C  CG  . ASP A 1 150 ? -20.076 -42.723 2.483   1.00 55.78  ? 150 ASP A CG  1 
ATOM   1239 O  OD1 . ASP A 1 150 ? -20.463 -43.752 1.898   1.00 56.29  ? 150 ASP A OD1 1 
ATOM   1240 O  OD2 . ASP A 1 150 ? -20.845 -41.859 2.912   1.00 57.13  ? 150 ASP A OD2 1 
ATOM   1241 N  N   . ILE A 1 151 ? -15.562 -43.795 2.729   1.00 56.11  ? 151 ILE A N   1 
ATOM   1242 C  CA  . ILE A 1 151 ? -14.081 -43.721 2.894   1.00 59.10  ? 151 ILE A CA  1 
ATOM   1243 C  C   . ILE A 1 151 ? -13.616 -42.408 2.269   1.00 56.59  ? 151 ILE A C   1 
ATOM   1244 O  O   . ILE A 1 151 ? -14.073 -42.095 1.166   1.00 55.83  ? 151 ILE A O   1 
ATOM   1245 C  CB  . ILE A 1 151 ? -13.367 -44.947 2.290   1.00 63.65  ? 151 ILE A CB  1 
ATOM   1246 C  CG1 . ILE A 1 151 ? -11.854 -44.724 2.166   1.00 70.72  ? 151 ILE A CG1 1 
ATOM   1247 C  CG2 . ILE A 1 151 ? -13.993 -45.341 0.963   1.00 62.59  ? 151 ILE A CG2 1 
ATOM   1248 C  CD1 . ILE A 1 151 ? -11.060 -45.983 1.889   1.00 73.87  ? 151 ILE A CD1 1 
ATOM   1249 N  N   . LEU A 1 152 ? -12.754 -41.671 2.974   1.00 59.60  ? 152 LEU A N   1 
ATOM   1250 C  CA  . LEU A 1 152 ? -12.201 -40.370 2.514   1.00 62.61  ? 152 LEU A CA  1 
ATOM   1251 C  C   . LEU A 1 152 ? -11.049 -40.635 1.555   1.00 67.49  ? 152 LEU A C   1 
ATOM   1252 O  O   . LEU A 1 152 ? -10.288 -41.581 1.817   1.00 72.67  ? 152 LEU A O   1 
ATOM   1253 C  CB  . LEU A 1 152 ? -11.714 -39.539 3.702   1.00 63.40  ? 152 LEU A CB  1 
ATOM   1254 C  CG  . LEU A 1 152 ? -12.513 -38.263 3.932   1.00 66.40  ? 152 LEU A CG  1 
ATOM   1255 C  CD1 . LEU A 1 152 ? -13.971 -38.602 4.191   1.00 67.54  ? 152 LEU A CD1 1 
ATOM   1256 C  CD2 . LEU A 1 152 ? -11.923 -37.438 5.067   1.00 68.33  ? 152 LEU A CD2 1 
ATOM   1257 N  N   . THR A 1 153 ? -10.933 -39.794 0.526   1.00 71.51  ? 153 THR A N   1 
ATOM   1258 C  CA  . THR A 1 153 ? -9.789  -39.735 -0.421  1.00 73.38  ? 153 THR A CA  1 
ATOM   1259 C  C   . THR A 1 153 ? -9.211  -38.317 -0.386  1.00 84.16  ? 153 THR A C   1 
ATOM   1260 O  O   . THR A 1 153 ? -9.946  -37.407 0.049   1.00 84.83  ? 153 THR A O   1 
ATOM   1261 C  CB  . THR A 1 153 ? -10.230 -40.128 -1.836  1.00 65.47  ? 153 THR A CB  1 
ATOM   1262 O  OG1 . THR A 1 153 ? -11.364 -40.995 -1.754  1.00 57.05  ? 153 THR A OG1 1 
ATOM   1263 C  CG2 . THR A 1 153 ? -9.105  -40.775 -2.609  1.00 66.43  ? 153 THR A CG2 1 
ATOM   1264 N  N   . SER A 1 154 ? -7.957  -38.135 -0.814  1.00 96.05  ? 154 SER A N   1 
ATOM   1265 C  CA  . SER A 1 154 ? -7.292  -36.806 -0.932  1.00 104.71 ? 154 SER A CA  1 
ATOM   1266 C  C   . SER A 1 154 ? -6.770  -36.601 -2.357  1.00 103.94 ? 154 SER A C   1 
ATOM   1267 O  O   . SER A 1 154 ? -5.563  -36.282 -2.494  1.00 108.65 ? 154 SER A O   1 
ATOM   1268 C  CB  . SER A 1 154 ? -6.178  -36.609 0.083   1.00 110.31 ? 154 SER A CB  1 
ATOM   1269 O  OG  . SER A 1 154 ? -5.482  -35.385 -0.133  1.00 116.73 ? 154 SER A OG  1 
ATOM   1270 N  N   . LYS A 1 155 ? -7.632  -36.741 -3.370  1.00 97.92  ? 155 LYS A N   1 
ATOM   1271 C  CA  . LYS A 1 155 ? -7.323  -36.336 -4.769  1.00 95.52  ? 155 LYS A CA  1 
ATOM   1272 C  C   . LYS A 1 155 ? -7.459  -34.811 -4.865  1.00 89.71  ? 155 LYS A C   1 
ATOM   1273 O  O   . LYS A 1 155 ? -8.379  -34.263 -4.243  1.00 83.05  ? 155 LYS A O   1 
ATOM   1274 C  CB  . LYS A 1 155 ? -8.212  -37.077 -5.774  1.00 94.81  ? 155 LYS A CB  1 
ATOM   1275 C  CG  . LYS A 1 155 ? -7.857  -38.544 -5.968  1.00 93.42  ? 155 LYS A CG  1 
ATOM   1276 C  CD  . LYS A 1 155 ? -9.020  -39.419 -6.382  1.00 93.46  ? 155 LYS A CD  1 
ATOM   1277 C  CE  . LYS A 1 155 ? -8.734  -40.894 -6.198  1.00 95.29  ? 155 LYS A CE  1 
ATOM   1278 N  NZ  . LYS A 1 155 ? -9.978  -41.698 -6.196  1.00 95.57  ? 155 LYS A NZ  1 
ATOM   1279 N  N   . HIS A 1 156 ? -6.528  -34.172 -5.580  1.00 86.25  ? 156 HIS A N   1 
ATOM   1280 C  CA  . HIS A 1 156 ? -6.340  -32.702 -5.676  1.00 84.69  ? 156 HIS A CA  1 
ATOM   1281 C  C   . HIS A 1 156 ? -6.491  -32.347 -7.166  1.00 84.22  ? 156 HIS A C   1 
ATOM   1282 O  O   . HIS A 1 156 ? -5.481  -32.028 -7.828  1.00 80.91  ? 156 HIS A O   1 
ATOM   1283 C  CB  . HIS A 1 156 ? -4.988  -32.359 -5.020  1.00 85.11  ? 156 HIS A CB  1 
ATOM   1284 C  CG  . HIS A 1 156 ? -4.921  -31.096 -4.225  1.00 85.35  ? 156 HIS A CG  1 
ATOM   1285 N  ND1 . HIS A 1 156 ? -5.295  -29.861 -4.735  1.00 85.41  ? 156 HIS A ND1 1 
ATOM   1286 C  CD2 . HIS A 1 156 ? -4.438  -30.862 -2.985  1.00 82.14  ? 156 HIS A CD2 1 
ATOM   1287 C  CE1 . HIS A 1 156 ? -5.076  -28.930 -3.828  1.00 81.53  ? 156 HIS A CE1 1 
ATOM   1288 N  NE2 . HIS A 1 156 ? -4.553  -29.518 -2.746  1.00 83.46  ? 156 HIS A NE2 1 
ATOM   1289 N  N   . PHE A 1 157 ? -7.713  -32.489 -7.683  1.00 84.47  ? 157 PHE A N   1 
ATOM   1290 C  CA  . PHE A 1 157 ? -8.042  -32.377 -9.127  1.00 83.68  ? 157 PHE A CA  1 
ATOM   1291 C  C   . PHE A 1 157 ? -7.797  -30.936 -9.578  1.00 81.07  ? 157 PHE A C   1 
ATOM   1292 O  O   . PHE A 1 157 ? -8.739  -30.135 -9.641  1.00 85.66  ? 157 PHE A O   1 
ATOM   1293 C  CB  . PHE A 1 157 ? -9.479  -32.818 -9.391  1.00 85.83  ? 157 PHE A CB  1 
ATOM   1294 C  CG  . PHE A 1 157 ? -9.791  -34.210 -8.913  1.00 88.12  ? 157 PHE A CG  1 
ATOM   1295 C  CD1 . PHE A 1 157 ? -9.308  -35.321 -9.589  1.00 91.25  ? 157 PHE A CD1 1 
ATOM   1296 C  CD2 . PHE A 1 157 ? -10.575 -34.406 -7.788  1.00 90.42  ? 157 PHE A CD2 1 
ATOM   1297 C  CE1 . PHE A 1 157 ? -9.598  -36.600 -9.140  1.00 95.72  ? 157 PHE A CE1 1 
ATOM   1298 C  CE2 . PHE A 1 157 ? -10.872 -35.686 -7.347  1.00 92.64  ? 157 PHE A CE2 1 
ATOM   1299 C  CZ  . PHE A 1 157 ? -10.388 -36.779 -8.027  1.00 95.76  ? 157 PHE A CZ  1 
ATOM   1300 N  N   . GLY A 1 158 ? -6.529  -30.612 -9.812  1.00 75.36  ? 158 GLY A N   1 
ATOM   1301 C  CA  . GLY A 1 158 ? -6.081  -29.345 -10.419 1.00 72.28  ? 158 GLY A CA  1 
ATOM   1302 C  C   . GLY A 1 158 ? -5.028  -29.614 -11.475 1.00 70.07  ? 158 GLY A C   1 
ATOM   1303 O  O   . GLY A 1 158 ? -4.477  -28.633 -12.030 1.00 66.11  ? 158 GLY A O   1 
ATOM   1304 N  N   . THR A 1 159 ? -4.800  -30.901 -11.763 1.00 67.57  ? 159 THR A N   1 
ATOM   1305 C  CA  . THR A 1 159 ? -3.777  -31.422 -12.704 1.00 63.20  ? 159 THR A CA  1 
ATOM   1306 C  C   . THR A 1 159 ? -4.362  -31.465 -14.115 1.00 59.16  ? 159 THR A C   1 
ATOM   1307 O  O   . THR A 1 159 ? -3.608  -31.764 -15.030 1.00 67.08  ? 159 THR A O   1 
ATOM   1308 C  CB  . THR A 1 159 ? -3.316  -32.837 -12.329 1.00 63.97  ? 159 THR A CB  1 
ATOM   1309 O  OG1 . THR A 1 159 ? -4.386  -33.751 -12.564 1.00 63.03  ? 159 THR A OG1 1 
ATOM   1310 C  CG2 . THR A 1 159 ? -2.892  -32.991 -10.886 1.00 65.77  ? 159 THR A CG2 1 
ATOM   1311 N  N   . ALA A 1 160 ? -5.654  -31.165 -14.277 1.00 54.84  ? 160 ALA A N   1 
ATOM   1312 C  CA  . ALA A 1 160 ? -6.376  -31.305 -15.558 1.00 54.58  ? 160 ALA A CA  1 
ATOM   1313 C  C   . ALA A 1 160 ? -6.363  -29.984 -16.338 1.00 55.73  ? 160 ALA A C   1 
ATOM   1314 O  O   . ALA A 1 160 ? -7.147  -29.872 -17.286 1.00 57.35  ? 160 ALA A O   1 
ATOM   1315 C  CB  . ALA A 1 160 ? -7.781  -31.768 -15.295 1.00 53.80  ? 160 ALA A CB  1 
ATOM   1316 N  N   . GLY A 1 161 ? -5.497  -29.033 -15.975 1.00 54.45  ? 161 GLY A N   1 
ATOM   1317 C  CA  . GLY A 1 161 ? -5.445  -27.705 -16.611 1.00 53.71  ? 161 GLY A CA  1 
ATOM   1318 C  C   . GLY A 1 161 ? -4.616  -26.731 -15.803 1.00 54.12  ? 161 GLY A C   1 
ATOM   1319 O  O   . GLY A 1 161 ? -5.070  -26.349 -14.702 1.00 62.62  ? 161 GLY A O   1 
ATOM   1320 N  N   . TYR A 1 162 ? -3.451  -26.341 -16.324 1.00 54.87  ? 162 TYR A N   1 
ATOM   1321 C  CA  . TYR A 1 162 ? -2.535  -25.369 -15.676 1.00 56.69  ? 162 TYR A CA  1 
ATOM   1322 C  C   . TYR A 1 162 ? -1.366  -24.999 -16.595 1.00 54.80  ? 162 TYR A C   1 
ATOM   1323 O  O   . TYR A 1 162 ? -0.959  -25.809 -17.452 1.00 49.70  ? 162 TYR A O   1 
ATOM   1324 C  CB  . TYR A 1 162 ? -1.975  -25.952 -14.379 1.00 57.00  ? 162 TYR A CB  1 
ATOM   1325 C  CG  . TYR A 1 162 ? -1.168  -27.207 -14.581 1.00 57.97  ? 162 TYR A CG  1 
ATOM   1326 C  CD1 . TYR A 1 162 ? 0.189   -27.146 -14.853 1.00 57.97  ? 162 TYR A CD1 1 
ATOM   1327 C  CD2 . TYR A 1 162 ? -1.757  -28.455 -14.514 1.00 60.45  ? 162 TYR A CD2 1 
ATOM   1328 C  CE1 . TYR A 1 162 ? 0.948   -28.289 -15.035 1.00 58.25  ? 162 TYR A CE1 1 
ATOM   1329 C  CE2 . TYR A 1 162 ? -1.008  -29.612 -14.682 1.00 61.72  ? 162 TYR A CE2 1 
ATOM   1330 C  CZ  . TYR A 1 162 ? 0.347   -29.532 -14.948 1.00 60.07  ? 162 TYR A CZ  1 
ATOM   1331 O  OH  . TYR A 1 162 ? 1.082   -30.672 -15.116 1.00 58.82  ? 162 TYR A OH  1 
ATOM   1332 N  N   . VAL A 1 163 ? -0.827  -23.800 -16.371 1.00 55.65  ? 163 VAL A N   1 
ATOM   1333 C  CA  . VAL A 1 163 ? 0.457   -23.315 -16.942 1.00 57.75  ? 163 VAL A CA  1 
ATOM   1334 C  C   . VAL A 1 163 ? 1.568   -23.655 -15.956 1.00 57.80  ? 163 VAL A C   1 
ATOM   1335 O  O   . VAL A 1 163 ? 1.363   -23.448 -14.752 1.00 59.60  ? 163 VAL A O   1 
ATOM   1336 C  CB  . VAL A 1 163 ? 0.433   -21.797 -17.181 1.00 62.31  ? 163 VAL A CB  1 
ATOM   1337 C  CG1 . VAL A 1 163 ? 1.731   -21.320 -17.817 1.00 65.23  ? 163 VAL A CG1 1 
ATOM   1338 C  CG2 . VAL A 1 163 ? -0.764  -21.372 -18.015 1.00 62.81  ? 163 VAL A CG2 1 
ATOM   1339 N  N   . ILE A 1 164 ? 2.716   -24.097 -16.463 1.00 61.55  ? 164 ILE A N   1 
ATOM   1340 C  CA  . ILE A 1 164 ? 3.949   -24.314 -15.653 1.00 63.62  ? 164 ILE A CA  1 
ATOM   1341 C  C   . ILE A 1 164 ? 5.090   -23.532 -16.311 1.00 62.74  ? 164 ILE A C   1 
ATOM   1342 O  O   . ILE A 1 164 ? 5.326   -23.729 -17.517 1.00 64.62  ? 164 ILE A O   1 
ATOM   1343 C  CB  . ILE A 1 164 ? 4.262   -25.817 -15.483 1.00 66.23  ? 164 ILE A CB  1 
ATOM   1344 C  CG1 . ILE A 1 164 ? 5.463   -26.036 -14.560 1.00 68.28  ? 164 ILE A CG1 1 
ATOM   1345 C  CG2 . ILE A 1 164 ? 4.448   -26.517 -16.825 1.00 67.10  ? 164 ILE A CG2 1 
ATOM   1346 C  CD1 . ILE A 1 164 ? 5.688   -27.481 -14.178 1.00 70.27  ? 164 ILE A CD1 1 
ATOM   1347 N  N   . SER A 1 165 ? 5.735   -22.651 -15.543 1.00 61.99  ? 165 SER A N   1 
ATOM   1348 C  CA  . SER A 1 165 ? 6.970   -21.922 -15.930 1.00 63.93  ? 165 SER A CA  1 
ATOM   1349 C  C   . SER A 1 165 ? 8.073   -22.940 -16.239 1.00 66.64  ? 165 SER A C   1 
ATOM   1350 O  O   . SER A 1 165 ? 8.018   -24.052 -15.679 1.00 68.26  ? 165 SER A O   1 
ATOM   1351 C  CB  . SER A 1 165 ? 7.386   -20.973 -14.836 1.00 63.76  ? 165 SER A CB  1 
ATOM   1352 O  OG  . SER A 1 165 ? 8.192   -21.627 -13.866 1.00 61.44  ? 165 SER A OG  1 
ATOM   1353 N  N   . GLN A 1 166 ? 9.037   -22.588 -17.095 1.00 69.26  ? 166 GLN A N   1 
ATOM   1354 C  CA  . GLN A 1 166 ? 10.199  -23.466 -17.391 1.00 72.74  ? 166 GLN A CA  1 
ATOM   1355 C  C   . GLN A 1 166 ? 10.962  -23.691 -16.084 1.00 73.07  ? 166 GLN A C   1 
ATOM   1356 O  O   . GLN A 1 166 ? 11.254  -24.859 -15.775 1.00 76.68  ? 166 GLN A O   1 
ATOM   1357 C  CB  . GLN A 1 166 ? 11.116  -22.861 -18.452 1.00 79.93  ? 166 GLN A CB  1 
ATOM   1358 C  CG  . GLN A 1 166 ? 12.126  -23.856 -19.010 1.00 87.44  ? 166 GLN A CG  1 
ATOM   1359 C  CD  . GLN A 1 166 ? 13.269  -23.190 -19.743 1.00 96.91  ? 166 GLN A CD  1 
ATOM   1360 O  OE1 . GLN A 1 166 ? 13.723  -22.107 -19.373 1.00 108.33 ? 166 GLN A OE1 1 
ATOM   1361 N  NE2 . GLN A 1 166 ? 13.757  -23.837 -20.790 1.00 98.03  ? 166 GLN A NE2 1 
ATOM   1362 N  N   . GLY A 1 167 ? 11.252  -22.607 -15.350 1.00 71.15  ? 167 GLY A N   1 
ATOM   1363 C  CA  . GLY A 1 167 ? 11.845  -22.650 -13.999 1.00 68.17  ? 167 GLY A CA  1 
ATOM   1364 C  C   . GLY A 1 167 ? 11.197  -23.741 -13.169 1.00 67.57  ? 167 GLY A C   1 
ATOM   1365 O  O   . GLY A 1 167 ? 11.935  -24.597 -12.642 1.00 68.66  ? 167 GLY A O   1 
ATOM   1366 N  N   . ALA A 1 168 ? 9.860   -23.729 -13.103 1.00 65.11  ? 168 ALA A N   1 
ATOM   1367 C  CA  . ALA A 1 168 ? 9.022   -24.710 -12.375 1.00 64.04  ? 168 ALA A CA  1 
ATOM   1368 C  C   . ALA A 1 168 ? 9.206   -26.100 -12.986 1.00 63.16  ? 168 ALA A C   1 
ATOM   1369 O  O   . ALA A 1 168 ? 9.324   -27.068 -12.215 1.00 64.27  ? 168 ALA A O   1 
ATOM   1370 C  CB  . ALA A 1 168 ? 7.576   -24.289 -12.402 1.00 62.89  ? 168 ALA A CB  1 
ATOM   1371 N  N   . ALA A 1 169 ? 9.231   -26.194 -14.316 1.00 65.13  ? 169 ALA A N   1 
ATOM   1372 C  CA  . ALA A 1 169 ? 9.464   -27.458 -15.050 1.00 71.00  ? 169 ALA A CA  1 
ATOM   1373 C  C   . ALA A 1 169 ? 10.737  -28.105 -14.498 1.00 75.75  ? 169 ALA A C   1 
ATOM   1374 O  O   . ALA A 1 169 ? 10.659  -29.258 -14.041 1.00 78.77  ? 169 ALA A O   1 
ATOM   1375 C  CB  . ALA A 1 169 ? 9.553   -27.215 -16.541 1.00 73.06  ? 169 ALA A CB  1 
ATOM   1376 N  N   . LYS A 1 170 ? 11.846  -27.357 -14.494 1.00 81.15  ? 170 LYS A N   1 
ATOM   1377 C  CA  . LYS A 1 170 ? 13.165  -27.807 -13.969 1.00 84.85  ? 170 LYS A CA  1 
ATOM   1378 C  C   . LYS A 1 170 ? 12.980  -28.292 -12.532 1.00 83.02  ? 170 LYS A C   1 
ATOM   1379 O  O   . LYS A 1 170 ? 13.242  -29.480 -12.268 1.00 78.16  ? 170 LYS A O   1 
ATOM   1380 C  CB  . LYS A 1 170 ? 14.198  -26.677 -14.034 1.00 89.43  ? 170 LYS A CB  1 
ATOM   1381 C  CG  . LYS A 1 170 ? 14.558  -26.246 -15.446 1.00 96.94  ? 170 LYS A CG  1 
ATOM   1382 C  CD  . LYS A 1 170 ? 15.759  -25.338 -15.551 1.00 100.55 ? 170 LYS A CD  1 
ATOM   1383 C  CE  . LYS A 1 170 ? 16.229  -25.191 -16.985 1.00 100.57 ? 170 LYS A CE  1 
ATOM   1384 N  NZ  . LYS A 1 170 ? 16.888  -23.885 -17.229 1.00 101.53 ? 170 LYS A NZ  1 
ATOM   1385 N  N   . TYR A 1 171 ? 12.517  -27.396 -11.659 1.00 85.71  ? 171 TYR A N   1 
ATOM   1386 C  CA  . TYR A 1 171 ? 12.290  -27.646 -10.213 1.00 88.15  ? 171 TYR A CA  1 
ATOM   1387 C  C   . TYR A 1 171 ? 11.637  -29.019 -10.045 1.00 86.57  ? 171 TYR A C   1 
ATOM   1388 O  O   . TYR A 1 171 ? 12.261  -29.904 -9.424  1.00 87.64  ? 171 TYR A O   1 
ATOM   1389 C  CB  . TYR A 1 171 ? 11.434  -26.530 -9.616  1.00 91.34  ? 171 TYR A CB  1 
ATOM   1390 C  CG  . TYR A 1 171 ? 11.158  -26.662 -8.143  1.00 98.81  ? 171 TYR A CG  1 
ATOM   1391 C  CD1 . TYR A 1 171 ? 10.155  -27.491 -7.670  1.00 101.57 ? 171 TYR A CD1 1 
ATOM   1392 C  CD2 . TYR A 1 171 ? 11.884  -25.932 -7.217  1.00 105.09 ? 171 TYR A CD2 1 
ATOM   1393 C  CE1 . TYR A 1 171 ? 9.888   -27.603 -6.314  1.00 105.55 ? 171 TYR A CE1 1 
ATOM   1394 C  CE2 . TYR A 1 171 ? 11.628  -26.025 -5.858  1.00 109.13 ? 171 TYR A CE2 1 
ATOM   1395 C  CZ  . TYR A 1 171 ? 10.629  -26.869 -5.404  1.00 110.45 ? 171 TYR A CZ  1 
ATOM   1396 O  OH  . TYR A 1 171 ? 10.373  -26.969 -4.068  1.00 116.03 ? 171 TYR A OH  1 
ATOM   1397 N  N   . LEU A 1 172 ? 10.437  -29.186 -10.612 1.00 83.28  ? 172 LEU A N   1 
ATOM   1398 C  CA  . LEU A 1 172 ? 9.617   -30.422 -10.494 1.00 80.79  ? 172 LEU A CA  1 
ATOM   1399 C  C   . LEU A 1 172 ? 10.417  -31.609 -11.026 1.00 78.03  ? 172 LEU A C   1 
ATOM   1400 O  O   . LEU A 1 172 ? 10.519  -32.608 -10.306 1.00 75.86  ? 172 LEU A O   1 
ATOM   1401 C  CB  . LEU A 1 172 ? 8.298   -30.257 -11.259 1.00 80.46  ? 172 LEU A CB  1 
ATOM   1402 C  CG  . LEU A 1 172 ? 7.075   -29.937 -10.399 1.00 82.12  ? 172 LEU A CG  1 
ATOM   1403 C  CD1 . LEU A 1 172 ? 7.380   -28.843 -9.388  1.00 84.83  ? 172 LEU A CD1 1 
ATOM   1404 C  CD2 . LEU A 1 172 ? 5.886   -29.542 -11.262 1.00 82.12  ? 172 LEU A CD2 1 
ATOM   1405 N  N   . ILE A 1 173 ? 10.978  -31.490 -12.229 1.00 82.63  ? 173 ILE A N   1 
ATOM   1406 C  CA  . ILE A 1 173 ? 11.723  -32.601 -12.890 1.00 92.05  ? 173 ILE A CA  1 
ATOM   1407 C  C   . ILE A 1 173 ? 12.713  -33.186 -11.874 1.00 96.18  ? 173 ILE A C   1 
ATOM   1408 O  O   . ILE A 1 173 ? 12.621  -34.399 -11.582 1.00 98.62  ? 173 ILE A O   1 
ATOM   1409 C  CB  . ILE A 1 173 ? 12.417  -32.132 -14.186 1.00 94.83  ? 173 ILE A CB  1 
ATOM   1410 C  CG1 . ILE A 1 173 ? 11.406  -31.843 -15.300 1.00 95.77  ? 173 ILE A CG1 1 
ATOM   1411 C  CG2 . ILE A 1 173 ? 13.457  -33.147 -14.639 1.00 97.34  ? 173 ILE A CG2 1 
ATOM   1412 C  CD1 . ILE A 1 173 ? 11.912  -30.883 -16.353 1.00 96.73  ? 173 ILE A CD1 1 
ATOM   1413 N  N   . ALA A 1 174 ? 13.605  -32.342 -11.348 1.00 98.38  ? 174 ALA A N   1 
ATOM   1414 C  CA  . ALA A 1 174 ? 14.653  -32.711 -10.367 1.00 96.55  ? 174 ALA A CA  1 
ATOM   1415 C  C   . ALA A 1 174 ? 13.991  -33.333 -9.135  1.00 92.18  ? 174 ALA A C   1 
ATOM   1416 O  O   . ALA A 1 174 ? 14.258  -34.514 -8.843  1.00 90.06  ? 174 ALA A O   1 
ATOM   1417 C  CB  . ALA A 1 174 ? 15.464  -31.493 -9.996  1.00 99.38  ? 174 ALA A CB  1 
ATOM   1418 N  N   . LEU A 1 175 ? 13.125  -32.555 -8.481  1.00 87.41  ? 175 LEU A N   1 
ATOM   1419 C  CA  . LEU A 1 175 ? 12.417  -32.898 -7.221  1.00 85.12  ? 175 LEU A CA  1 
ATOM   1420 C  C   . LEU A 1 175 ? 11.914  -34.347 -7.251  1.00 84.61  ? 175 LEU A C   1 
ATOM   1421 O  O   . LEU A 1 175 ? 12.002  -35.012 -6.205  1.00 91.73  ? 175 LEU A O   1 
ATOM   1422 C  CB  . LEU A 1 175 ? 11.258  -31.913 -7.038  1.00 84.70  ? 175 LEU A CB  1 
ATOM   1423 C  CG  . LEU A 1 175 ? 10.425  -32.105 -5.769  1.00 80.80  ? 175 LEU A CG  1 
ATOM   1424 C  CD1 . LEU A 1 175 ? 9.897   -30.771 -5.251  1.00 78.78  ? 175 LEU A CD1 1 
ATOM   1425 C  CD2 . LEU A 1 175 ? 9.281   -33.084 -6.007  1.00 77.95  ? 175 LEU A CD2 1 
ATOM   1426 N  N   . PHE A 1 176 ? 11.398  -34.808 -8.391  1.00 83.08  ? 176 PHE A N   1 
ATOM   1427 C  CA  . PHE A 1 176 ? 10.781  -36.153 -8.555  1.00 88.01  ? 176 PHE A CA  1 
ATOM   1428 C  C   . PHE A 1 176 ? 11.863  -37.232 -8.670  1.00 88.70  ? 176 PHE A C   1 
ATOM   1429 O  O   . PHE A 1 176 ? 11.623  -38.382 -8.240  1.00 84.25  ? 176 PHE A O   1 
ATOM   1430 C  CB  . PHE A 1 176 ? 9.853   -36.174 -9.770  1.00 93.94  ? 176 PHE A CB  1 
ATOM   1431 C  CG  . PHE A 1 176 ? 8.442   -35.741 -9.470  1.00 99.66  ? 176 PHE A CG  1 
ATOM   1432 C  CD1 . PHE A 1 176 ? 8.097   -34.398 -9.480  1.00 103.02 ? 176 PHE A CD1 1 
ATOM   1433 C  CD2 . PHE A 1 176 ? 7.463   -36.673 -9.168  1.00 100.97 ? 176 PHE A CD2 1 
ATOM   1434 C  CE1 . PHE A 1 176 ? 6.800   -33.996 -9.203  1.00 105.07 ? 176 PHE A CE1 1 
ATOM   1435 C  CE2 . PHE A 1 176 ? 6.165   -36.271 -8.893  1.00 103.17 ? 176 PHE A CE2 1 
ATOM   1436 C  CZ  . PHE A 1 176 ? 5.836   -34.934 -8.909  1.00 106.88 ? 176 PHE A CZ  1 
ATOM   1437 N  N   . GLU A 1 177 ? 13.017  -36.879 -9.239  1.00 95.25  ? 177 GLU A N   1 
ATOM   1438 C  CA  . GLU A 1 177 ? 14.185  -37.789 -9.367  1.00 102.68 ? 177 GLU A CA  1 
ATOM   1439 C  C   . GLU A 1 177 ? 14.914  -37.889 -8.018  1.00 108.80 ? 177 GLU A C   1 
ATOM   1440 O  O   . GLU A 1 177 ? 15.716  -38.828 -7.872  1.00 115.98 ? 177 GLU A O   1 
ATOM   1441 C  CB  . GLU A 1 177 ? 15.099  -37.314 -10.498 1.00 101.59 ? 177 GLU A CB  1 
ATOM   1442 C  CG  . GLU A 1 177 ? 14.474  -37.512 -11.869 1.00 104.68 ? 177 GLU A CG  1 
ATOM   1443 C  CD  . GLU A 1 177 ? 15.258  -36.944 -13.040 1.00 107.40 ? 177 GLU A CD  1 
ATOM   1444 O  OE1 . GLU A 1 177 ? 15.271  -37.587 -14.120 1.00 104.72 ? 177 GLU A OE1 1 
ATOM   1445 O  OE2 . GLU A 1 177 ? 15.842  -35.854 -12.872 1.00 107.14 ? 177 GLU A OE2 1 
ATOM   1446 N  N   . LYS A 1 178 ? 14.634  -36.980 -7.072  1.00 110.31 ? 178 LYS A N   1 
ATOM   1447 C  CA  . LYS A 1 178 ? 15.233  -36.953 -5.705  1.00 106.54 ? 178 LYS A CA  1 
ATOM   1448 C  C   . LYS A 1 178 ? 14.302  -37.632 -4.688  1.00 106.22 ? 178 LYS A C   1 
ATOM   1449 O  O   . LYS A 1 178 ? 14.368  -37.267 -3.499  1.00 103.97 ? 178 LYS A O   1 
ATOM   1450 C  CB  . LYS A 1 178 ? 15.518  -35.511 -5.269  1.00 103.76 ? 178 LYS A CB  1 
ATOM   1451 C  CG  . LYS A 1 178 ? 16.434  -34.719 -6.192  1.00 101.85 ? 178 LYS A CG  1 
ATOM   1452 C  CD  . LYS A 1 178 ? 16.829  -33.380 -5.617  1.00 100.10 ? 178 LYS A CD  1 
ATOM   1453 C  CE  . LYS A 1 178 ? 17.420  -32.440 -6.644  1.00 98.81  ? 178 LYS A CE  1 
ATOM   1454 N  NZ  . LYS A 1 178 ? 17.894  -31.185 -6.013  1.00 98.48  ? 178 LYS A NZ  1 
ATOM   1455 N  N   . LEU A 1 179 ? 13.472  -38.580 -5.136  1.00 111.24 ? 179 LEU A N   1 
ATOM   1456 C  CA  . LEU A 1 179 ? 12.597  -39.421 -4.274  1.00 116.53 ? 179 LEU A CA  1 
ATOM   1457 C  C   . LEU A 1 179 ? 12.929  -40.892 -4.539  1.00 121.13 ? 179 LEU A C   1 
ATOM   1458 O  O   . LEU A 1 179 ? 13.181  -41.228 -5.705  1.00 127.11 ? 179 LEU A O   1 
ATOM   1459 C  CB  . LEU A 1 179 ? 11.131  -39.123 -4.601  1.00 119.92 ? 179 LEU A CB  1 
ATOM   1460 C  CG  . LEU A 1 179 ? 10.714  -37.653 -4.560  1.00 120.00 ? 179 LEU A CG  1 
ATOM   1461 C  CD1 . LEU A 1 179 ? 9.242   -37.501 -4.909  1.00 119.25 ? 179 LEU A CD1 1 
ATOM   1462 C  CD2 . LEU A 1 179 ? 11.005  -37.031 -3.205  1.00 116.86 ? 179 LEU A CD2 1 
ATOM   1463 N  N   . THR A 1 180 ? 12.952  -41.717 -3.487  1.00 120.79 ? 180 THR A N   1 
ATOM   1464 C  CA  . THR A 1 180 ? 13.265  -43.175 -3.512  1.00 124.48 ? 180 THR A CA  1 
ATOM   1465 C  C   . THR A 1 180 ? 12.183  -43.911 -2.718  1.00 113.53 ? 180 THR A C   1 
ATOM   1466 O  O   . THR A 1 180 ? 12.491  -44.440 -1.639  1.00 114.68 ? 180 THR A O   1 
ATOM   1467 C  CB  . THR A 1 180 ? 14.682  -43.448 -2.981  1.00 134.91 ? 180 THR A CB  1 
ATOM   1468 O  OG1 . THR A 1 180 ? 15.584  -42.573 -3.658  1.00 156.25 ? 180 THR A OG1 1 
ATOM   1469 C  CG2 . THR A 1 180 ? 15.158  -44.870 -3.191  1.00 131.00 ? 180 THR A CG2 1 
ATOM   1470 N  N   . THR A 1 181 ? 10.948  -43.880 -3.224  1.00 108.85 ? 181 THR A N   1 
ATOM   1471 C  CA  . THR A 1 181 ? 9.751   -44.535 -2.633  1.00 107.25 ? 181 THR A CA  1 
ATOM   1472 C  C   . THR A 1 181 ? 9.468   -43.953 -1.240  1.00 100.81 ? 181 THR A C   1 
ATOM   1473 O  O   . THR A 1 181 ? 8.529   -44.422 -0.575  1.00 91.17  ? 181 THR A O   1 
ATOM   1474 C  CB  . THR A 1 181 ? 9.944   -46.055 -2.607  1.00 108.44 ? 181 THR A CB  1 
ATOM   1475 O  OG1 . THR A 1 181 ? 10.509  -46.470 -3.851  1.00 104.81 ? 181 THR A OG1 1 
ATOM   1476 C  CG2 . THR A 1 181 ? 8.645   -46.794 -2.398  1.00 108.62 ? 181 THR A CG2 1 
ATOM   1477 N  N   . GLU A 1 182 ? 10.225  -42.927 -0.852  1.00 97.68  ? 182 GLU A N   1 
ATOM   1478 C  CA  . GLU A 1 182 ? 10.279  -42.385 0.532   1.00 97.55  ? 182 GLU A CA  1 
ATOM   1479 C  C   . GLU A 1 182 ? 9.051   -41.496 0.739   1.00 102.25 ? 182 GLU A C   1 
ATOM   1480 O  O   . GLU A 1 182 ? 8.274   -41.789 1.669   1.00 105.21 ? 182 GLU A O   1 
ATOM   1481 C  CB  . GLU A 1 182 ? 11.594  -41.639 0.780   1.00 93.82  ? 182 GLU A CB  1 
ATOM   1482 C  CG  . GLU A 1 182 ? 12.264  -41.178 -0.501  1.00 92.14  ? 182 GLU A CG  1 
ATOM   1483 C  CD  . GLU A 1 182 ? 13.257  -40.035 -0.429  1.00 89.30  ? 182 GLU A CD  1 
ATOM   1484 O  OE1 . GLU A 1 182 ? 14.023  -39.881 -1.398  1.00 84.84  ? 182 GLU A OE1 1 
ATOM   1485 O  OE2 . GLU A 1 182 ? 13.267  -39.306 0.580   1.00 85.63  ? 182 GLU A OE2 1 
ATOM   1486 N  N   . GLU A 1 183 ? 8.883   -40.468 -0.103  1.00 103.20 ? 183 GLU A N   1 
ATOM   1487 C  CA  . GLU A 1 183 ? 7.713   -39.551 -0.077  1.00 104.89 ? 183 GLU A CA  1 
ATOM   1488 C  C   . GLU A 1 183 ? 6.927   -39.697 -1.379  1.00 100.55 ? 183 GLU A C   1 
ATOM   1489 O  O   . GLU A 1 183 ? 6.101   -38.817 -1.653  1.00 102.12 ? 183 GLU A O   1 
ATOM   1490 C  CB  . GLU A 1 183 ? 8.141   -38.097 0.125   1.00 109.71 ? 183 GLU A CB  1 
ATOM   1491 C  CG  . GLU A 1 183 ? 9.126   -37.899 1.264   1.00 113.12 ? 183 GLU A CG  1 
ATOM   1492 C  CD  . GLU A 1 183 ? 10.571  -37.703 0.838   1.00 113.63 ? 183 GLU A CD  1 
ATOM   1493 O  OE1 . GLU A 1 183 ? 10.882  -37.956 -0.347  1.00 115.66 ? 183 GLU A OE1 1 
ATOM   1494 O  OE2 . GLU A 1 183 ? 11.379  -37.292 1.691   1.00 111.74 ? 183 GLU A OE2 1 
ATOM   1495 N  N   . ILE A 1 184 ? 7.170   -40.780 -2.121  1.00 100.20 ? 184 ILE A N   1 
ATOM   1496 C  CA  . ILE A 1 184 ? 6.506   -41.066 -3.425  1.00 104.15 ? 184 ILE A CA  1 
ATOM   1497 C  C   . ILE A 1 184 ? 4.990   -41.136 -3.205  1.00 106.17 ? 184 ILE A C   1 
ATOM   1498 O  O   . ILE A 1 184 ? 4.497   -42.195 -2.747  1.00 112.73 ? 184 ILE A O   1 
ATOM   1499 C  CB  . ILE A 1 184 ? 7.093   -42.348 -4.054  1.00 107.21 ? 184 ILE A CB  1 
ATOM   1500 C  CG1 . ILE A 1 184 ? 8.511   -42.099 -4.574  1.00 108.54 ? 184 ILE A CG1 1 
ATOM   1501 C  CG2 . ILE A 1 184 ? 6.201   -42.922 -5.147  1.00 108.67 ? 184 ILE A CG2 1 
ATOM   1502 C  CD1 . ILE A 1 184 ? 8.599   -41.000 -5.606  1.00 109.10 ? 184 ILE A CD1 1 
ATOM   1503 N  N   . LYS A 1 185 ? 4.305   -40.016 -3.473  1.00 103.92 ? 185 LYS A N   1 
ATOM   1504 C  CA  . LYS A 1 185 ? 2.820   -39.893 -3.559  1.00 104.16 ? 185 LYS A CA  1 
ATOM   1505 C  C   . LYS A 1 185 ? 2.452   -39.431 -4.969  1.00 97.63  ? 185 LYS A C   1 
ATOM   1506 O  O   . LYS A 1 185 ? 3.270   -38.810 -5.635  1.00 96.16  ? 185 LYS A O   1 
ATOM   1507 C  CB  . LYS A 1 185 ? 2.312   -38.906 -2.501  1.00 110.75 ? 185 LYS A CB  1 
ATOM   1508 C  CG  . LYS A 1 185 ? 2.703   -39.247 -1.067  1.00 115.97 ? 185 LYS A CG  1 
ATOM   1509 C  CD  . LYS A 1 185 ? 2.384   -38.161 -0.062  1.00 120.62 ? 185 LYS A CD  1 
ATOM   1510 C  CE  . LYS A 1 185 ? 2.724   -38.560 1.358   1.00 122.59 ? 185 LYS A CE  1 
ATOM   1511 N  NZ  . LYS A 1 185 ? 2.177   -37.598 2.344   1.00 124.24 ? 185 LYS A NZ  1 
ATOM   1512 N  N   . PRO A 1 186 ? 1.230   -39.706 -5.490  1.00 93.51  ? 186 PRO A N   1 
ATOM   1513 C  CA  . PRO A 1 186 ? 0.863   -39.291 -6.848  1.00 89.18  ? 186 PRO A CA  1 
ATOM   1514 C  C   . PRO A 1 186 ? 1.114   -37.800 -7.131  1.00 83.40  ? 186 PRO A C   1 
ATOM   1515 O  O   . PRO A 1 186 ? 1.393   -37.048 -6.209  1.00 78.54  ? 186 PRO A O   1 
ATOM   1516 C  CB  . PRO A 1 186 ? -0.639  -39.606 -6.946  1.00 91.91  ? 186 PRO A CB  1 
ATOM   1517 C  CG  . PRO A 1 186 ? -0.840  -40.719 -5.939  1.00 93.79  ? 186 PRO A CG  1 
ATOM   1518 C  CD  . PRO A 1 186 ? 0.137   -40.427 -4.817  1.00 94.70  ? 186 PRO A CD  1 
ATOM   1519 N  N   . ILE A 1 187 ? 1.000   -37.418 -8.405  1.00 77.19  ? 187 ILE A N   1 
ATOM   1520 C  CA  . ILE A 1 187 ? 1.443   -36.094 -8.936  1.00 77.41  ? 187 ILE A CA  1 
ATOM   1521 C  C   . ILE A 1 187 ? 0.724   -34.952 -8.200  1.00 80.97  ? 187 ILE A C   1 
ATOM   1522 O  O   . ILE A 1 187 ? 1.437   -34.040 -7.704  1.00 79.40  ? 187 ILE A O   1 
ATOM   1523 C  CB  . ILE A 1 187 ? 1.262   -36.013 -10.468 1.00 77.07  ? 187 ILE A CB  1 
ATOM   1524 C  CG1 . ILE A 1 187 ? 1.488   -34.586 -10.980 1.00 74.38  ? 187 ILE A CG1 1 
ATOM   1525 C  CG2 . ILE A 1 187 ? -0.082  -36.575 -10.919 1.00 78.27  ? 187 ILE A CG2 1 
ATOM   1526 C  CD1 . ILE A 1 187 ? 1.860   -34.517 -12.427 1.00 74.46  ? 187 ILE A CD1 1 
ATOM   1527 N  N   . ASP A 1 188 ? -0.616  -34.994 -8.123  1.00 86.06  ? 188 ASP A N   1 
ATOM   1528 C  CA  . ASP A 1 188 ? -1.451  -33.924 -7.506  1.00 88.17  ? 188 ASP A CA  1 
ATOM   1529 C  C   . ASP A 1 188 ? -0.954  -33.681 -6.075  1.00 86.58  ? 188 ASP A C   1 
ATOM   1530 O  O   . ASP A 1 188 ? -0.699  -32.517 -5.711  1.00 78.19  ? 188 ASP A O   1 
ATOM   1531 C  CB  . ASP A 1 188 ? -2.958  -34.223 -7.511  1.00 92.60  ? 188 ASP A CB  1 
ATOM   1532 C  CG  . ASP A 1 188 ? -3.444  -35.624 -7.870  1.00 97.93  ? 188 ASP A CG  1 
ATOM   1533 O  OD1 . ASP A 1 188 ? -2.621  -36.567 -8.002  1.00 104.37 ? 188 ASP A OD1 1 
ATOM   1534 O  OD2 . ASP A 1 188 ? -4.673  -35.763 -8.012  1.00 100.16 ? 188 ASP A OD2 1 
ATOM   1535 N  N   . GLU A 1 189 ? -0.769  -34.764 -5.320  1.00 87.09  ? 189 GLU A N   1 
ATOM   1536 C  CA  . GLU A 1 189 ? -0.500  -34.741 -3.863  1.00 91.38  ? 189 GLU A CA  1 
ATOM   1537 C  C   . GLU A 1 189 ? 0.929   -34.269 -3.589  1.00 87.02  ? 189 GLU A C   1 
ATOM   1538 O  O   . GLU A 1 189 ? 1.337   -34.317 -2.414  1.00 90.82  ? 189 GLU A O   1 
ATOM   1539 C  CB  . GLU A 1 189 ? -0.786  -36.123 -3.281  1.00 103.56 ? 189 GLU A CB  1 
ATOM   1540 C  CG  . GLU A 1 189 ? -2.273  -36.452 -3.286  1.00 116.15 ? 189 GLU A CG  1 
ATOM   1541 C  CD  . GLU A 1 189 ? -2.778  -37.282 -4.460  1.00 125.53 ? 189 GLU A CD  1 
ATOM   1542 O  OE1 . GLU A 1 189 ? -2.471  -38.489 -4.501  1.00 131.87 ? 189 GLU A OE1 1 
ATOM   1543 O  OE2 . GLU A 1 189 ? -3.494  -36.726 -5.322  1.00 126.05 ? 189 GLU A OE2 1 
ATOM   1544 N  N   . ILE A 1 190 ? 1.645   -33.801 -4.614  1.00 86.58  ? 190 ILE A N   1 
ATOM   1545 C  CA  . ILE A 1 190 ? 3.000   -33.184 -4.481  1.00 86.94  ? 190 ILE A CA  1 
ATOM   1546 C  C   . ILE A 1 190 ? 2.936   -31.745 -4.995  1.00 83.78  ? 190 ILE A C   1 
ATOM   1547 O  O   . ILE A 1 190 ? 3.148   -30.817 -4.187  1.00 89.49  ? 190 ILE A O   1 
ATOM   1548 C  CB  . ILE A 1 190 ? 4.068   -34.017 -5.217  1.00 84.62  ? 190 ILE A CB  1 
ATOM   1549 C  CG1 . ILE A 1 190 ? 4.024   -35.475 -4.756  1.00 86.99  ? 190 ILE A CG1 1 
ATOM   1550 C  CG2 . ILE A 1 190 ? 5.448   -33.397 -5.039  1.00 82.03  ? 190 ILE A CG2 1 
ATOM   1551 C  CD1 . ILE A 1 190 ? 5.130   -36.347 -5.294  1.00 88.70  ? 190 ILE A CD1 1 
HETATM 1552 N  N   . MSE A 1 191 ? 2.653   -31.589 -6.288  1.00 74.94  ? 191 MSE A N   1 
HETATM 1553 C  CA  . MSE A 1 191 ? 2.620   -30.291 -7.004  1.00 71.29  ? 191 MSE A CA  1 
HETATM 1554 C  C   . MSE A 1 191 ? 1.924   -29.227 -6.156  1.00 72.96  ? 191 MSE A C   1 
HETATM 1555 O  O   . MSE A 1 191 ? 2.540   -28.178 -5.925  1.00 76.53  ? 191 MSE A O   1 
HETATM 1556 C  CB  . MSE A 1 191 ? 1.850   -30.438 -8.315  1.00 67.72  ? 191 MSE A CB  1 
HETATM 1557 C  CG  . MSE A 1 191 ? 2.553   -31.251 -9.360  1.00 62.01  ? 191 MSE A CG  1 
HETATM 1558 SE SE  . MSE A 1 191 ? 1.499   -31.078 -10.990 1.00 53.19  ? 191 MSE A SE  1 
HETATM 1559 C  CE  . MSE A 1 191 ? 1.907   -29.337 -11.823 1.00 54.56  ? 191 MSE A CE  1 
ATOM   1560 N  N   . PHE A 1 192 ? 0.692   -29.499 -5.726  1.00 74.79  ? 192 PHE A N   1 
ATOM   1561 C  CA  . PHE A 1 192 ? -0.238  -28.503 -5.134  1.00 80.71  ? 192 PHE A CA  1 
ATOM   1562 C  C   . PHE A 1 192 ? -0.258  -28.617 -3.607  1.00 89.87  ? 192 PHE A C   1 
ATOM   1563 O  O   . PHE A 1 192 ? -0.323  -27.579 -2.924  1.00 95.50  ? 192 PHE A O   1 
ATOM   1564 C  CB  . PHE A 1 192 ? -1.632  -28.697 -5.732  1.00 76.19  ? 192 PHE A CB  1 
ATOM   1565 C  CG  . PHE A 1 192 ? -1.623  -28.712 -7.237  1.00 70.04  ? 192 PHE A CG  1 
ATOM   1566 C  CD1 . PHE A 1 192 ? -1.330  -27.558 -7.941  1.00 64.81  ? 192 PHE A CD1 1 
ATOM   1567 C  CD2 . PHE A 1 192 ? -1.884  -29.876 -7.944  1.00 67.41  ? 192 PHE A CD2 1 
ATOM   1568 C  CE1 . PHE A 1 192 ? -1.318  -27.558 -9.324  1.00 63.97  ? 192 PHE A CE1 1 
ATOM   1569 C  CE2 . PHE A 1 192 ? -1.863  -29.876 -9.327  1.00 64.38  ? 192 PHE A CE2 1 
ATOM   1570 C  CZ  . PHE A 1 192 ? -1.563  -28.725 -10.012 1.00 65.59  ? 192 PHE A CZ  1 
ATOM   1571 N  N   . ASN A 1 193 ? -0.211  -29.850 -3.099  1.00 98.86  ? 193 ASN A N   1 
ATOM   1572 C  CA  . ASN A 1 193 ? -0.385  -30.194 -1.664  1.00 104.55 ? 193 ASN A CA  1 
ATOM   1573 C  C   . ASN A 1 193 ? 0.972   -30.097 -0.963  1.00 107.04 ? 193 ASN A C   1 
ATOM   1574 O  O   . ASN A 1 193 ? 1.187   -29.107 -0.236  1.00 99.48  ? 193 ASN A O   1 
ATOM   1575 C  CB  . ASN A 1 193 ? -1.022  -31.578 -1.525  1.00 110.40 ? 193 ASN A CB  1 
ATOM   1576 C  CG  . ASN A 1 193 ? -1.358  -31.979 -0.105  1.00 112.32 ? 193 ASN A CG  1 
ATOM   1577 O  OD1 . ASN A 1 193 ? -0.909  -31.371 0.865   1.00 117.22 ? 193 ASN A OD1 1 
ATOM   1578 N  ND2 . ASN A 1 193 ? -2.169  -33.016 0.023   1.00 110.83 ? 193 ASN A ND2 1 
ATOM   1579 N  N   . GLN A 1 194 ? 1.852   -31.077 -1.192  1.00 117.55 ? 194 GLN A N   1 
ATOM   1580 C  CA  . GLN A 1 194 ? 3.159   -31.220 -0.496  1.00 127.58 ? 194 GLN A CA  1 
ATOM   1581 C  C   . GLN A 1 194 ? 3.885   -29.874 -0.507  1.00 134.69 ? 194 GLN A C   1 
ATOM   1582 O  O   . GLN A 1 194 ? 4.267   -29.394 0.575   1.00 132.63 ? 194 GLN A O   1 
ATOM   1583 C  CB  . GLN A 1 194 ? 4.014   -32.302 -1.161  1.00 126.88 ? 194 GLN A CB  1 
ATOM   1584 C  CG  . GLN A 1 194 ? 5.066   -32.914 -0.250  1.00 126.12 ? 194 GLN A CG  1 
ATOM   1585 C  CD  . GLN A 1 194 ? 4.457   -33.761 0.842   1.00 129.62 ? 194 GLN A CD  1 
ATOM   1586 O  OE1 . GLN A 1 194 ? 3.367   -34.315 0.702   1.00 126.56 ? 194 GLN A OE1 1 
ATOM   1587 N  NE2 . GLN A 1 194 ? 5.163   -33.860 1.955   1.00 131.53 ? 194 GLN A NE2 1 
ATOM   1588 N  N   . GLN A 1 195 ? 4.076   -29.310 -1.681  1.00 146.39 ? 195 GLN A N   1 
ATOM   1589 C  CA  . GLN A 1 195 ? 4.791   -28.067 -1.745  1.00 158.70 ? 195 GLN A CA  1 
ATOM   1590 C  C   . GLN A 1 195 ? 3.792   -26.947 -1.761  1.00 171.54 ? 195 GLN A C   1 
ATOM   1591 O  O   . GLN A 1 195 ? 3.424   -26.442 -2.817  1.00 177.25 ? 195 GLN A O   1 
ATOM   1592 C  CB  . GLN A 1 195 ? 5.715   -28.013 -2.960  1.00 157.10 ? 195 GLN A CB  1 
ATOM   1593 C  CG  . GLN A 1 195 ? 6.997   -27.227 -2.708  1.00 153.93 ? 195 GLN A CG  1 
ATOM   1594 C  CD  . GLN A 1 195 ? 6.784   -26.011 -1.819  1.00 155.25 ? 195 GLN A CD  1 
ATOM   1595 O  OE1 . GLN A 1 195 ? 6.258   -24.990 -2.259  1.00 155.47 ? 195 GLN A OE1 1 
ATOM   1596 N  NE2 . GLN A 1 195 ? 7.192   -26.118 -0.559  1.00 154.23 ? 195 GLN A NE2 1 
ATOM   1597 N  N   . ILE A 1 196 ? 3.333   -26.569 -0.583  1.00 184.62 ? 196 ILE A N   1 
ATOM   1598 C  CA  . ILE A 1 196 ? 2.430   -25.435 -0.485  1.00 188.69 ? 196 ILE A CA  1 
ATOM   1599 C  C   . ILE A 1 196 ? 2.748   -24.796 0.838   1.00 184.12 ? 196 ILE A C   1 
ATOM   1600 O  O   . ILE A 1 196 ? 1.999   -23.962 1.347   1.00 181.76 ? 196 ILE A O   1 
ATOM   1601 C  CB  . ILE A 1 196 ? 0.955   -25.868 -0.573  1.00 189.01 ? 196 ILE A CB  1 
ATOM   1602 C  CG1 . ILE A 1 196 ? 0.103   -24.724 -1.130  1.00 183.01 ? 196 ILE A CG1 1 
ATOM   1603 C  CG2 . ILE A 1 196 ? 0.434   -26.342 0.780   1.00 188.97 ? 196 ILE A CG2 1 
ATOM   1604 C  CD1 . ILE A 1 196 ? 0.655   -24.127 -2.406  1.00 175.65 ? 196 ILE A CD1 1 
ATOM   1605 N  N   . ASN A 1 197 ? 3.907   -25.136 1.376   1.00 174.24 ? 197 ASN A N   1 
ATOM   1606 C  CA  . ASN A 1 197 ? 4.223   -24.661 2.707   1.00 164.31 ? 197 ASN A CA  1 
ATOM   1607 C  C   . ASN A 1 197 ? 5.413   -23.735 2.868   1.00 157.34 ? 197 ASN A C   1 
ATOM   1608 O  O   . ASN A 1 197 ? 5.488   -23.042 3.878   1.00 153.87 ? 197 ASN A O   1 
ATOM   1609 C  CB  . ASN A 1 197 ? 4.447   -25.889 3.597   1.00 160.34 ? 197 ASN A CB  1 
ATOM   1610 C  CG  . ASN A 1 197 ? 4.232   -27.190 2.849   1.00 161.55 ? 197 ASN A CG  1 
ATOM   1611 O  OD1 . ASN A 1 197 ? 3.129   -27.479 2.384   1.00 159.39 ? 197 ASN A OD1 1 
ATOM   1612 N  ND2 . ASN A 1 197 ? 5.292   -27.978 2.718   1.00 162.02 ? 197 ASN A ND2 1 
ATOM   1613 N  N   . ALA A 1 198 ? 6.338   -23.681 1.908   1.00 150.38 ? 198 ALA A N   1 
ATOM   1614 C  CA  . ALA A 1 198 ? 7.506   -22.866 2.183   1.00 139.43 ? 198 ALA A CA  1 
ATOM   1615 C  C   . ALA A 1 198 ? 8.410   -22.461 1.085   1.00 134.39 ? 198 ALA A C   1 
ATOM   1616 O  O   . ALA A 1 198 ? 8.554   -21.278 0.794   1.00 133.95 ? 198 ALA A O   1 
ATOM   1617 C  CB  . ALA A 1 198 ? 8.358   -23.598 3.225   1.00 132.90 ? 198 ALA A CB  1 
ATOM   1618 N  N   . THR A 1 199 ? 9.105   -23.429 0.569   1.00 129.75 ? 199 THR A N   1 
ATOM   1619 C  CA  . THR A 1 199 ? 10.054  -23.206 -0.564  1.00 121.53 ? 199 THR A CA  1 
ATOM   1620 C  C   . THR A 1 199 ? 9.500   -22.150 -1.541  1.00 116.75 ? 199 THR A C   1 
ATOM   1621 O  O   . THR A 1 199 ? 8.273   -21.948 -1.588  1.00 118.54 ? 199 THR A O   1 
ATOM   1622 C  CB  . THR A 1 199 ? 10.420  -24.526 -1.260  1.00 114.59 ? 199 THR A CB  1 
ATOM   1623 O  OG1 . THR A 1 199 ? 10.719  -25.482 -0.244  1.00 116.18 ? 199 THR A OG1 1 
ATOM   1624 C  CG2 . THR A 1 199 ? 11.618  -24.418 -2.176  1.00 108.06 ? 199 THR A CG2 1 
ATOM   1625 N  N   . ASP A 1 200 ? 10.409  -21.479 -2.253  1.00 107.11 ? 200 ASP A N   1 
ATOM   1626 C  CA  . ASP A 1 200 ? 10.159  -20.359 -3.203  1.00 97.32  ? 200 ASP A CA  1 
ATOM   1627 C  C   . ASP A 1 200 ? 9.146   -20.738 -4.291  1.00 93.15  ? 200 ASP A C   1 
ATOM   1628 O  O   . ASP A 1 200 ? 8.552   -19.808 -4.864  1.00 92.25  ? 200 ASP A O   1 
ATOM   1629 C  CB  . ASP A 1 200 ? 11.471  -19.927 -3.860  1.00 95.69  ? 200 ASP A CB  1 
ATOM   1630 C  CG  . ASP A 1 200 ? 12.396  -21.098 -4.145  1.00 96.88  ? 200 ASP A CG  1 
ATOM   1631 O  OD1 . ASP A 1 200 ? 11.884  -22.224 -4.318  1.00 92.30  ? 200 ASP A OD1 1 
ATOM   1632 O  OD2 . ASP A 1 200 ? 13.625  -20.884 -4.164  1.00 100.23 ? 200 ASP A OD2 1 
ATOM   1633 N  N   . TYR A 1 201 ? 8.973   -22.032 -4.585  1.00 87.05  ? 201 TYR A N   1 
ATOM   1634 C  CA  . TYR A 1 201 ? 7.982   -22.576 -5.556  1.00 78.39  ? 201 TYR A CA  1 
ATOM   1635 C  C   . TYR A 1 201 ? 6.561   -22.205 -5.110  1.00 74.01  ? 201 TYR A C   1 
ATOM   1636 O  O   . TYR A 1 201 ? 6.075   -22.768 -4.114  1.00 72.70  ? 201 TYR A O   1 
ATOM   1637 C  CB  . TYR A 1 201 ? 8.146   -24.095 -5.680  1.00 79.88  ? 201 TYR A CB  1 
ATOM   1638 C  CG  . TYR A 1 201 ? 6.965   -24.834 -6.264  1.00 81.31  ? 201 TYR A CG  1 
ATOM   1639 C  CD1 . TYR A 1 201 ? 5.912   -25.245 -5.464  1.00 81.63  ? 201 TYR A CD1 1 
ATOM   1640 C  CD2 . TYR A 1 201 ? 6.895   -25.131 -7.617  1.00 82.53  ? 201 TYR A CD2 1 
ATOM   1641 C  CE1 . TYR A 1 201 ? 4.824   -25.924 -5.989  1.00 84.04  ? 201 TYR A CE1 1 
ATOM   1642 C  CE2 . TYR A 1 201 ? 5.810   -25.801 -8.157  1.00 81.57  ? 201 TYR A CE2 1 
ATOM   1643 C  CZ  . TYR A 1 201 ? 4.766   -26.200 -7.343  1.00 81.38  ? 201 TYR A CZ  1 
ATOM   1644 O  OH  . TYR A 1 201 ? 3.704   -26.871 -7.877  1.00 78.03  ? 201 TYR A OH  1 
ATOM   1645 N  N   . ARG A 1 202 ? 5.915   -21.300 -5.842  1.00 70.98  ? 202 ARG A N   1 
ATOM   1646 C  CA  . ARG A 1 202 ? 4.561   -20.780 -5.521  1.00 73.04  ? 202 ARG A CA  1 
ATOM   1647 C  C   . ARG A 1 202 ? 3.572   -21.274 -6.581  1.00 66.16  ? 202 ARG A C   1 
ATOM   1648 O  O   . ARG A 1 202 ? 3.983   -21.524 -7.727  1.00 65.20  ? 202 ARG A O   1 
ATOM   1649 C  CB  . ARG A 1 202 ? 4.574   -19.250 -5.408  1.00 81.79  ? 202 ARG A CB  1 
ATOM   1650 C  CG  . ARG A 1 202 ? 5.091   -18.520 -6.640  1.00 93.87  ? 202 ARG A CG  1 
ATOM   1651 C  CD  . ARG A 1 202 ? 5.869   -17.251 -6.315  1.00 104.32 ? 202 ARG A CD  1 
ATOM   1652 N  NE  . ARG A 1 202 ? 7.223   -17.545 -5.853  1.00 115.41 ? 202 ARG A NE  1 
ATOM   1653 C  CZ  . ARG A 1 202 ? 8.190   -16.648 -5.678  1.00 117.99 ? 202 ARG A CZ  1 
ATOM   1654 N  NH1 . ARG A 1 202 ? 7.974   -15.366 -5.927  1.00 116.07 ? 202 ARG A NH1 1 
ATOM   1655 N  NH2 . ARG A 1 202 ? 9.379   -17.042 -5.252  1.00 119.46 ? 202 ARG A NH2 1 
ATOM   1656 N  N   . VAL A 1 203 ? 2.303   -21.409 -6.190  1.00 60.41  ? 203 VAL A N   1 
ATOM   1657 C  CA  . VAL A 1 203 ? 1.171   -21.885 -7.038  1.00 54.59  ? 203 VAL A CA  1 
ATOM   1658 C  C   . VAL A 1 203 ? 0.102   -20.800 -7.049  1.00 53.22  ? 203 VAL A C   1 
ATOM   1659 O  O   . VAL A 1 203 ? -0.280  -20.352 -5.960  1.00 56.72  ? 203 VAL A O   1 
ATOM   1660 C  CB  . VAL A 1 203 ? 0.579   -23.193 -6.491  1.00 52.27  ? 203 VAL A CB  1 
ATOM   1661 C  CG1 . VAL A 1 203 ? -0.662  -23.606 -7.261  1.00 52.43  ? 203 VAL A CG1 1 
ATOM   1662 C  CG2 . VAL A 1 203 ? 1.607   -24.309 -6.462  1.00 52.42  ? 203 VAL A CG2 1 
ATOM   1663 N  N   . TYR A 1 204 ? -0.387  -20.429 -8.227  1.00 52.99  ? 204 TYR A N   1 
ATOM   1664 C  CA  . TYR A 1 204 ? -1.458  -19.416 -8.392  1.00 55.60  ? 204 TYR A CA  1 
ATOM   1665 C  C   . TYR A 1 204 ? -2.726  -20.102 -8.889  1.00 53.15  ? 204 TYR A C   1 
ATOM   1666 O  O   . TYR A 1 204 ? -2.628  -21.199 -9.464  1.00 52.73  ? 204 TYR A O   1 
ATOM   1667 C  CB  . TYR A 1 204 ? -1.010  -18.313 -9.344  1.00 59.58  ? 204 TYR A CB  1 
ATOM   1668 C  CG  . TYR A 1 204 ? 0.242   -17.603 -8.905  1.00 65.19  ? 204 TYR A CG  1 
ATOM   1669 C  CD1 . TYR A 1 204 ? 0.187   -16.507 -8.059  1.00 69.92  ? 204 TYR A CD1 1 
ATOM   1670 C  CD2 . TYR A 1 204 ? 1.485   -18.020 -9.348  1.00 67.30  ? 204 TYR A CD2 1 
ATOM   1671 C  CE1 . TYR A 1 204 ? 1.338   -15.846 -7.660  1.00 73.00  ? 204 TYR A CE1 1 
ATOM   1672 C  CE2 . TYR A 1 204 ? 2.644   -17.366 -8.966  1.00 70.24  ? 204 TYR A CE2 1 
ATOM   1673 C  CZ  . TYR A 1 204 ? 2.571   -16.277 -8.116  1.00 73.29  ? 204 TYR A CZ  1 
ATOM   1674 O  OH  . TYR A 1 204 ? 3.710   -15.633 -7.732  1.00 77.40  ? 204 TYR A OH  1 
ATOM   1675 N  N   . GLN A 1 205 ? -3.873  -19.471 -8.641  1.00 51.67  ? 205 GLN A N   1 
ATOM   1676 C  CA  . GLN A 1 205 ? -5.198  -19.942 -9.108  1.00 53.18  ? 205 GLN A CA  1 
ATOM   1677 C  C   . GLN A 1 205 ? -5.898  -18.770 -9.787  1.00 53.25  ? 205 GLN A C   1 
ATOM   1678 O  O   . GLN A 1 205 ? -6.346  -17.852 -9.089  1.00 55.63  ? 205 GLN A O   1 
ATOM   1679 C  CB  . GLN A 1 205 ? -6.016  -20.509 -7.945  1.00 53.38  ? 205 GLN A CB  1 
ATOM   1680 C  CG  . GLN A 1 205 ? -7.474  -20.818 -8.284  1.00 54.53  ? 205 GLN A CG  1 
ATOM   1681 C  CD  . GLN A 1 205 ? -7.693  -22.100 -9.056  1.00 55.43  ? 205 GLN A CD  1 
ATOM   1682 O  OE1 . GLN A 1 205 ? -6.988  -23.094 -8.892  1.00 54.84  ? 205 GLN A OE1 1 
ATOM   1683 N  NE2 . GLN A 1 205 ? -8.718  -22.095 -9.894  1.00 57.43  ? 205 GLN A NE2 1 
ATOM   1684 N  N   . LEU A 1 206 ? -5.957  -18.810 -11.110 1.00 59.13  ? 206 LEU A N   1 
ATOM   1685 C  CA  . LEU A 1 206 ? -6.805  -17.911 -11.927 1.00 60.85  ? 206 LEU A CA  1 
ATOM   1686 C  C   . LEU A 1 206 ? -8.219  -17.966 -11.347 1.00 57.76  ? 206 LEU A C   1 
ATOM   1687 O  O   . LEU A 1 206 ? -8.739  -19.087 -11.196 1.00 57.82  ? 206 LEU A O   1 
ATOM   1688 C  CB  . LEU A 1 206 ? -6.754  -18.410 -13.376 1.00 61.33  ? 206 LEU A CB  1 
ATOM   1689 C  CG  . LEU A 1 206 ? -7.335  -17.484 -14.437 1.00 62.68  ? 206 LEU A CG  1 
ATOM   1690 C  CD1 . LEU A 1 206 ? -6.773  -16.074 -14.314 1.00 63.67  ? 206 LEU A CD1 1 
ATOM   1691 C  CD2 . LEU A 1 206 ? -7.048  -18.049 -15.821 1.00 62.86  ? 206 LEU A CD2 1 
ATOM   1692 N  N   . ASN A 1 207 ? -8.801  -16.824 -10.989 1.00 56.14  ? 207 ASN A N   1 
ATOM   1693 C  CA  . ASN A 1 207 ? -10.103 -16.804 -10.269 1.00 59.12  ? 207 ASN A CA  1 
ATOM   1694 C  C   . ASN A 1 207 ? -10.912 -15.571 -10.664 1.00 57.92  ? 207 ASN A C   1 
ATOM   1695 O  O   . ASN A 1 207 ? -10.501 -14.449 -10.371 1.00 65.13  ? 207 ASN A O   1 
ATOM   1696 C  CB  . ASN A 1 207 ? -9.901  -16.881 -8.753  1.00 61.42  ? 207 ASN A CB  1 
ATOM   1697 C  CG  . ASN A 1 207 ? -10.970 -17.730 -8.104  1.00 65.69  ? 207 ASN A CG  1 
ATOM   1698 O  OD1 . ASN A 1 207 ? -10.909 -18.955 -8.165  1.00 68.14  ? 207 ASN A OD1 1 
ATOM   1699 N  ND2 . ASN A 1 207 ? -11.981 -17.090 -7.542  1.00 70.70  ? 207 ASN A ND2 1 
ATOM   1700 N  N   . PRO A 1 208 ? -12.091 -15.727 -11.316 1.00 51.31  ? 208 PRO A N   1 
ATOM   1701 C  CA  . PRO A 1 208 ? -12.620 -17.039 -11.691 1.00 49.76  ? 208 PRO A CA  1 
ATOM   1702 C  C   . PRO A 1 208 ? -11.708 -17.837 -12.632 1.00 49.56  ? 208 PRO A C   1 
ATOM   1703 O  O   . PRO A 1 208 ? -10.881 -17.259 -13.287 1.00 49.11  ? 208 PRO A O   1 
ATOM   1704 C  CB  . PRO A 1 208 ? -13.954 -16.748 -12.395 1.00 48.83  ? 208 PRO A CB  1 
ATOM   1705 C  CG  . PRO A 1 208 ? -13.947 -15.262 -12.671 1.00 48.21  ? 208 PRO A CG  1 
ATOM   1706 C  CD  . PRO A 1 208 ? -13.016 -14.638 -11.657 1.00 48.28  ? 208 PRO A CD  1 
ATOM   1707 N  N   . ALA A 1 209 ? -11.884 -19.159 -12.645 1.00 51.77  ? 209 ALA A N   1 
ATOM   1708 C  CA  . ALA A 1 209 ? -11.162 -20.109 -13.521 1.00 51.85  ? 209 ALA A CA  1 
ATOM   1709 C  C   . ALA A 1 209 ? -11.713 -19.988 -14.944 1.00 52.63  ? 209 ALA A C   1 
ATOM   1710 O  O   . ALA A 1 209 ? -12.670 -19.215 -15.144 1.00 50.91  ? 209 ALA A O   1 
ATOM   1711 C  CB  . ALA A 1 209 ? -11.313 -21.505 -12.983 1.00 51.46  ? 209 ALA A CB  1 
ATOM   1712 N  N   . ILE A 1 210 ? -11.125 -20.724 -15.891 1.00 53.25  ? 210 ILE A N   1 
ATOM   1713 C  CA  . ILE A 1 210 ? -11.520 -20.699 -17.329 1.00 53.14  ? 210 ILE A CA  1 
ATOM   1714 C  C   . ILE A 1 210 ? -11.758 -22.122 -17.851 1.00 52.34  ? 210 ILE A C   1 
ATOM   1715 O  O   . ILE A 1 210 ? -12.013 -22.259 -19.056 1.00 49.11  ? 210 ILE A O   1 
ATOM   1716 C  CB  . ILE A 1 210 ? -10.453 -19.963 -18.158 1.00 53.31  ? 210 ILE A CB  1 
ATOM   1717 C  CG1 . ILE A 1 210 ? -9.069  -20.590 -17.975 1.00 54.99  ? 210 ILE A CG1 1 
ATOM   1718 C  CG2 . ILE A 1 210 ? -10.460 -18.476 -17.833 1.00 52.15  ? 210 ILE A CG2 1 
ATOM   1719 C  CD1 . ILE A 1 210 ? -8.062  -20.166 -19.016 1.00 56.20  ? 210 ILE A CD1 1 
ATOM   1720 N  N   . CYS A 1 211 ? -11.656 -23.147 -17.006 1.00 52.60  ? 211 CYS A N   1 
ATOM   1721 C  CA  . CYS A 1 211 ? -12.105 -24.529 -17.326 1.00 54.26  ? 211 CYS A CA  1 
ATOM   1722 C  C   . CYS A 1 211 ? -12.532 -25.238 -16.034 1.00 53.31  ? 211 CYS A C   1 
ATOM   1723 O  O   . CYS A 1 211 ? -12.482 -24.608 -14.979 1.00 54.03  ? 211 CYS A O   1 
ATOM   1724 C  CB  . CYS A 1 211 ? -11.022 -25.310 -18.063 1.00 54.26  ? 211 CYS A CB  1 
ATOM   1725 S  SG  . CYS A 1 211 ? -9.502  -25.533 -17.109 1.00 62.18  ? 211 CYS A SG  1 
ATOM   1726 N  N   . VAL A 1 212 ? -12.945 -26.505 -16.141 1.00 52.49  ? 212 VAL A N   1 
ATOM   1727 C  CA  . VAL A 1 212 ? -13.510 -27.339 -15.041 1.00 51.68  ? 212 VAL A CA  1 
ATOM   1728 C  C   . VAL A 1 212 ? -13.510 -28.801 -15.492 1.00 50.86  ? 212 VAL A C   1 
ATOM   1729 O  O   . VAL A 1 212 ? -13.694 -29.036 -16.684 1.00 51.75  ? 212 VAL A O   1 
ATOM   1730 C  CB  . VAL A 1 212 ? -14.939 -26.888 -14.683 1.00 51.84  ? 212 VAL A CB  1 
ATOM   1731 C  CG1 . VAL A 1 212 ? -15.797 -26.686 -15.921 1.00 51.72  ? 212 VAL A CG1 1 
ATOM   1732 C  CG2 . VAL A 1 212 ? -15.617 -27.850 -13.723 1.00 51.34  ? 212 VAL A CG2 1 
ATOM   1733 N  N   . GLN A 1 213 ? -13.321 -29.740 -14.565 1.00 53.68  ? 213 GLN A N   1 
ATOM   1734 C  CA  . GLN A 1 213 ? -13.653 -31.179 -14.757 1.00 55.74  ? 213 GLN A CA  1 
ATOM   1735 C  C   . GLN A 1 213 ? -15.096 -31.365 -14.270 1.00 59.08  ? 213 GLN A C   1 
ATOM   1736 O  O   . GLN A 1 213 ? -15.271 -31.571 -13.066 1.00 59.89  ? 213 GLN A O   1 
ATOM   1737 C  CB  . GLN A 1 213 ? -12.680 -32.092 -14.007 1.00 54.04  ? 213 GLN A CB  1 
ATOM   1738 C  CG  . GLN A 1 213 ? -11.219 -31.711 -14.177 1.00 53.88  ? 213 GLN A CG  1 
ATOM   1739 C  CD  . GLN A 1 213 ? -10.292 -32.784 -13.668 1.00 55.58  ? 213 GLN A CD  1 
ATOM   1740 O  OE1 . GLN A 1 213 ? -9.508  -32.573 -12.743 1.00 55.79  ? 213 GLN A OE1 1 
ATOM   1741 N  NE2 . GLN A 1 213 ? -10.363 -33.949 -14.292 1.00 57.07  ? 213 GLN A NE2 1 
ATOM   1742 N  N   . GLU A 1 214 ? -16.083 -31.257 -15.167 1.00 64.17  ? 214 GLU A N   1 
ATOM   1743 C  CA  . GLU A 1 214 ? -17.514 -31.102 -14.796 1.00 64.07  ? 214 GLU A CA  1 
ATOM   1744 C  C   . GLU A 1 214 ? -17.881 -32.169 -13.762 1.00 62.55  ? 214 GLU A C   1 
ATOM   1745 O  O   . GLU A 1 214 ? -18.368 -31.788 -12.678 1.00 61.41  ? 214 GLU A O   1 
ATOM   1746 C  CB  . GLU A 1 214 ? -18.419 -31.158 -16.028 1.00 66.92  ? 214 GLU A CB  1 
ATOM   1747 C  CG  . GLU A 1 214 ? -19.751 -30.418 -15.864 1.00 70.45  ? 214 GLU A CG  1 
ATOM   1748 C  CD  . GLU A 1 214 ? -19.727 -28.950 -15.438 1.00 72.04  ? 214 GLU A CD  1 
ATOM   1749 O  OE1 . GLU A 1 214 ? -18.839 -28.212 -15.917 1.00 68.97  ? 214 GLU A OE1 1 
ATOM   1750 O  OE2 . GLU A 1 214 ? -20.615 -28.536 -14.632 1.00 71.58  ? 214 GLU A OE2 1 
ATOM   1751 N  N   . LEU A 1 215 ? -17.625 -33.443 -14.057 1.00 62.04  ? 215 LEU A N   1 
ATOM   1752 C  CA  . LEU A 1 215 ? -18.118 -34.552 -13.202 1.00 61.16  ? 215 LEU A CA  1 
ATOM   1753 C  C   . LEU A 1 215 ? -17.770 -34.265 -11.742 1.00 59.85  ? 215 LEU A C   1 
ATOM   1754 O  O   . LEU A 1 215 ? -18.642 -34.450 -10.884 1.00 63.19  ? 215 LEU A O   1 
ATOM   1755 C  CB  . LEU A 1 215 ? -17.516 -35.888 -13.624 1.00 63.34  ? 215 LEU A CB  1 
ATOM   1756 C  CG  . LEU A 1 215 ? -18.395 -37.077 -13.246 1.00 65.15  ? 215 LEU A CG  1 
ATOM   1757 C  CD1 . LEU A 1 215 ? -19.473 -37.284 -14.303 1.00 67.83  ? 215 LEU A CD1 1 
ATOM   1758 C  CD2 . LEU A 1 215 ? -17.580 -38.348 -13.045 1.00 64.64  ? 215 LEU A CD2 1 
ATOM   1759 N  N   . GLN A 1 216 ? -16.546 -33.805 -11.485 1.00 58.46  ? 216 GLN A N   1 
ATOM   1760 C  CA  . GLN A 1 216 ? -16.024 -33.580 -10.112 1.00 57.13  ? 216 GLN A CA  1 
ATOM   1761 C  C   . GLN A 1 216 ? -16.890 -32.521 -9.433  1.00 56.28  ? 216 GLN A C   1 
ATOM   1762 O  O   . GLN A 1 216 ? -17.297 -32.743 -8.276  1.00 59.49  ? 216 GLN A O   1 
ATOM   1763 C  CB  . GLN A 1 216 ? -14.553 -33.168 -10.152 1.00 58.01  ? 216 GLN A CB  1 
ATOM   1764 C  CG  . GLN A 1 216 ? -13.603 -34.356 -10.169 1.00 59.57  ? 216 GLN A CG  1 
ATOM   1765 C  CD  . GLN A 1 216 ? -13.896 -35.284 -11.322 1.00 59.32  ? 216 GLN A CD  1 
ATOM   1766 O  OE1 . GLN A 1 216 ? -14.218 -36.456 -11.138 1.00 62.45  ? 216 GLN A OE1 1 
ATOM   1767 N  NE2 . GLN A 1 216 ? -13.816 -34.747 -12.527 1.00 55.12  ? 216 GLN A NE2 1 
ATOM   1768 N  N   . LEU A 1 217 ? -17.181 -31.436 -10.148 1.00 53.88  ? 217 LEU A N   1 
ATOM   1769 C  CA  . LEU A 1 217 ? -18.021 -30.314 -9.653  1.00 55.05  ? 217 LEU A CA  1 
ATOM   1770 C  C   . LEU A 1 217 ? -19.373 -30.861 -9.183  1.00 56.27  ? 217 LEU A C   1 
ATOM   1771 O  O   . LEU A 1 217 ? -19.693 -30.667 -8.016  1.00 58.94  ? 217 LEU A O   1 
ATOM   1772 C  CB  . LEU A 1 217 ? -18.205 -29.279 -10.764 1.00 55.51  ? 217 LEU A CB  1 
ATOM   1773 C  CG  . LEU A 1 217 ? -18.628 -27.895 -10.282 1.00 55.98  ? 217 LEU A CG  1 
ATOM   1774 C  CD1 . LEU A 1 217 ? -17.483 -27.226 -9.542  1.00 57.50  ? 217 LEU A CD1 1 
ATOM   1775 C  CD2 . LEU A 1 217 ? -19.090 -27.028 -11.445 1.00 56.64  ? 217 LEU A CD2 1 
ATOM   1776 N  N   . ASN A 1 218 ? -20.123 -31.534 -10.057 1.00 62.17  ? 218 ASN A N   1 
ATOM   1777 C  CA  . ASN A 1 218 ? -21.478 -32.074 -9.754  1.00 65.58  ? 218 ASN A CA  1 
ATOM   1778 C  C   . ASN A 1 218 ? -21.397 -32.895 -8.470  1.00 63.35  ? 218 ASN A C   1 
ATOM   1779 O  O   . ASN A 1 218 ? -22.292 -32.742 -7.630  1.00 66.99  ? 218 ASN A O   1 
ATOM   1780 C  CB  . ASN A 1 218 ? -22.044 -32.928 -10.887 1.00 73.61  ? 218 ASN A CB  1 
ATOM   1781 C  CG  . ASN A 1 218 ? -21.731 -32.359 -12.255 1.00 86.40  ? 218 ASN A CG  1 
ATOM   1782 O  OD1 . ASN A 1 218 ? -21.210 -33.060 -13.126 1.00 95.41  ? 218 ASN A OD1 1 
ATOM   1783 N  ND2 . ASN A 1 218 ? -22.028 -31.081 -12.450 1.00 87.48  ? 218 ASN A ND2 1 
ATOM   1784 N  N   . GLN A 1 219 ? -20.341 -33.699 -8.324  1.00 59.91  ? 219 GLN A N   1 
ATOM   1785 C  CA  . GLN A 1 219 ? -20.086 -34.567 -7.139  1.00 57.27  ? 219 GLN A CA  1 
ATOM   1786 C  C   . GLN A 1 219 ? -19.742 -33.695 -5.928  1.00 51.18  ? 219 GLN A C   1 
ATOM   1787 O  O   . GLN A 1 219 ? -20.394 -33.858 -4.870  1.00 49.53  ? 219 GLN A O   1 
ATOM   1788 C  CB  . GLN A 1 219 ? -18.951 -35.556 -7.415  1.00 60.30  ? 219 GLN A CB  1 
ATOM   1789 C  CG  . GLN A 1 219 ? -19.431 -36.918 -7.894  1.00 65.21  ? 219 GLN A CG  1 
ATOM   1790 C  CD  . GLN A 1 219 ? -18.593 -37.468 -9.022  1.00 69.12  ? 219 GLN A CD  1 
ATOM   1791 O  OE1 . GLN A 1 219 ? -18.184 -36.750 -9.930  1.00 74.07  ? 219 GLN A OE1 1 
ATOM   1792 N  NE2 . GLN A 1 219 ? -18.342 -38.766 -8.990  1.00 70.01  ? 219 GLN A NE2 1 
ATOM   1793 N  N   . GLU A 1 220 ? -18.749 -32.815 -6.084  1.00 47.84  ? 220 GLU A N   1 
ATOM   1794 C  CA  . GLU A 1 220 ? -18.306 -31.884 -5.015  1.00 47.98  ? 220 GLU A CA  1 
ATOM   1795 C  C   . GLU A 1 220 ? -19.530 -31.120 -4.511  1.00 47.97  ? 220 GLU A C   1 
ATOM   1796 O  O   . GLU A 1 220 ? -19.752 -31.101 -3.295  1.00 55.13  ? 220 GLU A O   1 
ATOM   1797 C  CB  . GLU A 1 220 ? -17.233 -30.915 -5.507  1.00 48.74  ? 220 GLU A CB  1 
ATOM   1798 C  CG  . GLU A 1 220 ? -17.141 -29.650 -4.665  1.00 49.36  ? 220 GLU A CG  1 
ATOM   1799 C  CD  . GLU A 1 220 ? -15.998 -28.715 -5.020  1.00 52.52  ? 220 GLU A CD  1 
ATOM   1800 O  OE1 . GLU A 1 220 ? -16.260 -27.613 -5.574  1.00 53.02  ? 220 GLU A OE1 1 
ATOM   1801 O  OE2 . GLU A 1 220 ? -14.845 -29.085 -4.737  1.00 55.22  ? 220 GLU A OE2 1 
ATOM   1802 N  N   . ALA A 1 221 ? -20.298 -30.526 -5.426  1.00 45.37  ? 221 ALA A N   1 
ATOM   1803 C  CA  . ALA A 1 221 ? -21.537 -29.768 -5.144  1.00 44.94  ? 221 ALA A CA  1 
ATOM   1804 C  C   . ALA A 1 221 ? -22.517 -30.664 -4.392  1.00 44.88  ? 221 ALA A C   1 
ATOM   1805 O  O   . ALA A 1 221 ? -23.005 -30.238 -3.348  1.00 48.55  ? 221 ALA A O   1 
ATOM   1806 C  CB  . ALA A 1 221 ? -22.148 -29.255 -6.423  1.00 45.16  ? 221 ALA A CB  1 
ATOM   1807 N  N   . SER A 1 222 ? -22.782 -31.864 -4.902  1.00 46.44  ? 222 SER A N   1 
ATOM   1808 C  CA  . SER A 1 222 ? -23.753 -32.814 -4.304  1.00 46.58  ? 222 SER A CA  1 
ATOM   1809 C  C   . SER A 1 222 ? -23.337 -33.135 -2.866  1.00 44.57  ? 222 SER A C   1 
ATOM   1810 O  O   . SER A 1 222 ? -24.236 -33.273 -2.013  1.00 43.69  ? 222 SER A O   1 
ATOM   1811 C  CB  . SER A 1 222 ? -23.888 -34.059 -5.126  1.00 49.66  ? 222 SER A CB  1 
ATOM   1812 O  OG  . SER A 1 222 ? -24.478 -35.087 -4.350  1.00 54.25  ? 222 SER A OG  1 
ATOM   1813 N  N   . LEU A 1 223 ? -22.030 -33.242 -2.614  1.00 43.04  ? 223 LEU A N   1 
ATOM   1814 C  CA  . LEU A 1 223 ? -21.471 -33.546 -1.268  1.00 42.66  ? 223 LEU A CA  1 
ATOM   1815 C  C   . LEU A 1 223 ? -21.759 -32.381 -0.322  1.00 42.93  ? 223 LEU A C   1 
ATOM   1816 O  O   . LEU A 1 223 ? -22.177 -32.638 0.827   1.00 44.44  ? 223 LEU A O   1 
ATOM   1817 C  CB  . LEU A 1 223 ? -19.962 -33.778 -1.373  1.00 41.43  ? 223 LEU A CB  1 
ATOM   1818 C  CG  . LEU A 1 223 ? -19.212 -33.853 -0.045  1.00 40.38  ? 223 LEU A CG  1 
ATOM   1819 C  CD1 . LEU A 1 223 ? -17.876 -34.559 -0.213  1.00 40.20  ? 223 LEU A CD1 1 
ATOM   1820 C  CD2 . LEU A 1 223 ? -19.004 -32.471 0.553   1.00 40.70  ? 223 LEU A CD2 1 
ATOM   1821 N  N   . LEU A 1 224 ? -21.467 -31.155 -0.767  1.00 41.56  ? 224 LEU A N   1 
ATOM   1822 C  CA  . LEU A 1 224 ? -21.338 -29.986 0.146   1.00 42.98  ? 224 LEU A CA  1 
ATOM   1823 C  C   . LEU A 1 224 ? -22.718 -29.344 0.343   1.00 41.51  ? 224 LEU A C   1 
ATOM   1824 O  O   . LEU A 1 224 ? -22.899 -28.603 1.331   1.00 43.50  ? 224 LEU A O   1 
ATOM   1825 C  CB  . LEU A 1 224 ? -20.227 -29.034 -0.329  1.00 42.88  ? 224 LEU A CB  1 
ATOM   1826 C  CG  . LEU A 1 224 ? -20.464 -28.247 -1.614  1.00 46.10  ? 224 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A 1 224 ? -21.421 -27.092 -1.372  1.00 48.19  ? 224 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A 1 224 ? -19.149 -27.732 -2.191  1.00 45.59  ? 224 LEU A CD2 1 
ATOM   1829 N  N   . VAL A 1 225 ? -23.692 -29.711 -0.488  1.00 39.29  ? 225 VAL A N   1 
ATOM   1830 C  CA  . VAL A 1 225 ? -25.135 -29.453 -0.233  1.00 40.79  ? 225 VAL A CA  1 
ATOM   1831 C  C   . VAL A 1 225 ? -25.586 -30.343 0.924   1.00 40.42  ? 225 VAL A C   1 
ATOM   1832 O  O   . VAL A 1 225 ? -26.332 -29.844 1.760   1.00 39.66  ? 225 VAL A O   1 
ATOM   1833 C  CB  . VAL A 1 225 ? -25.982 -29.697 -1.498  1.00 42.54  ? 225 VAL A CB  1 
ATOM   1834 C  CG1 . VAL A 1 225 ? -27.472 -29.781 -1.203  1.00 43.27  ? 225 VAL A CG1 1 
ATOM   1835 C  CG2 . VAL A 1 225 ? -25.724 -28.633 -2.545  1.00 42.21  ? 225 VAL A CG2 1 
ATOM   1836 N  N   . SER A 1 226 ? -25.178 -31.614 0.945   1.00 43.20  ? 226 SER A N   1 
ATOM   1837 C  CA  . SER A 1 226 ? -25.558 -32.582 2.005   1.00 45.10  ? 226 SER A CA  1 
ATOM   1838 C  C   . SER A 1 226 ? -24.950 -32.077 3.302   1.00 43.04  ? 226 SER A C   1 
ATOM   1839 O  O   . SER A 1 226 ? -25.703 -31.718 4.205   1.00 43.86  ? 226 SER A O   1 
ATOM   1840 C  CB  . SER A 1 226 ? -25.093 -33.983 1.715   1.00 48.91  ? 226 SER A CB  1 
ATOM   1841 O  OG  . SER A 1 226 ? -25.525 -34.406 0.433   1.00 58.77  ? 226 SER A OG  1 
ATOM   1842 N  N   . ASN A 1 227 ? -23.622 -32.011 3.314   1.00 43.31  ? 227 ASN A N   1 
ATOM   1843 C  CA  . ASN A 1 227 ? -22.797 -31.503 4.431   1.00 44.09  ? 227 ASN A CA  1 
ATOM   1844 C  C   . ASN A 1 227 ? -23.491 -30.278 5.035   1.00 45.23  ? 227 ASN A C   1 
ATOM   1845 O  O   . ASN A 1 227 ? -23.600 -30.210 6.271   1.00 48.21  ? 227 ASN A O   1 
ATOM   1846 C  CB  . ASN A 1 227 ? -21.383 -31.227 3.930   1.00 45.18  ? 227 ASN A CB  1 
ATOM   1847 C  CG  . ASN A 1 227 ? -20.512 -30.590 4.984   1.00 45.18  ? 227 ASN A CG  1 
ATOM   1848 O  OD1 . ASN A 1 227 ? -19.730 -31.269 5.647   1.00 44.92  ? 227 ASN A OD1 1 
ATOM   1849 N  ND2 . ASN A 1 227 ? -20.644 -29.287 5.146   1.00 46.33  ? 227 ASN A ND2 1 
ATOM   1850 N  N   . LEU A 1 228 ? -23.971 -29.361 4.197   1.00 45.93  ? 228 LEU A N   1 
ATOM   1851 C  CA  . LEU A 1 228 ? -24.608 -28.099 4.663   1.00 44.88  ? 228 LEU A CA  1 
ATOM   1852 C  C   . LEU A 1 228 ? -25.965 -28.401 5.318   1.00 43.84  ? 228 LEU A C   1 
ATOM   1853 O  O   . LEU A 1 228 ? -26.171 -27.935 6.444   1.00 44.23  ? 228 LEU A O   1 
ATOM   1854 C  CB  . LEU A 1 228 ? -24.712 -27.126 3.485   1.00 44.26  ? 228 LEU A CB  1 
ATOM   1855 C  CG  . LEU A 1 228 ? -25.527 -25.858 3.735   1.00 42.77  ? 228 LEU A CG  1 
ATOM   1856 C  CD1 . LEU A 1 228 ? -25.121 -25.184 5.026   1.00 44.67  ? 228 LEU A CD1 1 
ATOM   1857 C  CD2 . LEU A 1 228 ? -25.383 -24.890 2.577   1.00 43.92  ? 228 LEU A CD2 1 
ATOM   1858 N  N   . GLU A 1 229 ? -26.837 -29.181 4.672   1.00 46.03  ? 229 GLU A N   1 
ATOM   1859 C  CA  . GLU A 1 229 ? -28.224 -29.447 5.149   1.00 49.53  ? 229 GLU A CA  1 
ATOM   1860 C  C   . GLU A 1 229 ? -28.140 -30.172 6.498   1.00 53.42  ? 229 GLU A C   1 
ATOM   1861 O  O   . GLU A 1 229 ? -28.798 -29.729 7.458   1.00 58.68  ? 229 GLU A O   1 
ATOM   1862 C  CB  . GLU A 1 229 ? -29.018 -30.229 4.099   1.00 50.11  ? 229 GLU A CB  1 
ATOM   1863 C  CG  . GLU A 1 229 ? -30.398 -30.680 4.553   1.00 51.98  ? 229 GLU A CG  1 
ATOM   1864 C  CD  . GLU A 1 229 ? -31.386 -29.584 4.920   1.00 53.91  ? 229 GLU A CD  1 
ATOM   1865 O  OE1 . GLU A 1 229 ? -31.006 -28.661 5.658   1.00 56.11  ? 229 GLU A OE1 1 
ATOM   1866 O  OE2 . GLU A 1 229 ? -32.546 -29.667 4.481   1.00 57.19  ? 229 GLU A OE2 1 
ATOM   1867 N  N   . GLN A 1 230 ? -27.318 -31.217 6.566   1.00 56.37  ? 230 GLN A N   1 
ATOM   1868 C  CA  . GLN A 1 230 ? -26.931 -31.906 7.824   1.00 59.82  ? 230 GLN A CA  1 
ATOM   1869 C  C   . GLN A 1 230 ? -26.614 -30.859 8.905   1.00 58.47  ? 230 GLN A C   1 
ATOM   1870 O  O   . GLN A 1 230 ? -27.322 -30.851 9.938   1.00 59.60  ? 230 GLN A O   1 
ATOM   1871 C  CB  . GLN A 1 230 ? -25.750 -32.834 7.529   1.00 64.31  ? 230 GLN A CB  1 
ATOM   1872 C  CG  . GLN A 1 230 ? -25.176 -33.524 8.755   1.00 70.05  ? 230 GLN A CG  1 
ATOM   1873 C  CD  . GLN A 1 230 ? -26.154 -34.468 9.413   1.00 74.18  ? 230 GLN A CD  1 
ATOM   1874 O  OE1 . GLN A 1 230 ? -27.219 -34.776 8.880   1.00 79.51  ? 230 GLN A OE1 1 
ATOM   1875 N  NE2 . GLN A 1 230 ? -25.780 -34.952 10.584  1.00 75.71  ? 230 GLN A NE2 1 
ATOM   1876 N  N   . GLU A 1 231 ? -25.608 -30.004 8.665   1.00 56.76  ? 231 GLU A N   1 
ATOM   1877 C  CA  . GLU A 1 231 ? -25.149 -28.928 9.591   1.00 55.27  ? 231 GLU A CA  1 
ATOM   1878 C  C   . GLU A 1 231 ? -26.345 -28.103 10.071  1.00 51.68  ? 231 GLU A C   1 
ATOM   1879 O  O   . GLU A 1 231 ? -26.397 -27.813 11.275  1.00 48.62  ? 231 GLU A O   1 
ATOM   1880 C  CB  . GLU A 1 231 ? -24.162 -27.966 8.922   1.00 58.51  ? 231 GLU A CB  1 
ATOM   1881 C  CG  . GLU A 1 231 ? -22.710 -28.419 8.941   1.00 60.44  ? 231 GLU A CG  1 
ATOM   1882 C  CD  . GLU A 1 231 ? -21.717 -27.380 8.432   1.00 62.33  ? 231 GLU A CD  1 
ATOM   1883 O  OE1 . GLU A 1 231 ? -22.033 -26.174 8.512   1.00 65.00  ? 231 GLU A OE1 1 
ATOM   1884 O  OE2 . GLU A 1 231 ? -20.629 -27.775 7.951   1.00 63.73  ? 231 GLU A OE2 1 
ATOM   1885 N  N   . ARG A 1 232 ? -27.243 -27.719 9.157   1.00 49.46  ? 232 ARG A N   1 
ATOM   1886 C  CA  . ARG A 1 232 ? -28.426 -26.871 9.464   1.00 51.53  ? 232 ARG A CA  1 
ATOM   1887 C  C   . ARG A 1 232 ? -29.346 -27.596 10.450  1.00 52.14  ? 232 ARG A C   1 
ATOM   1888 O  O   . ARG A 1 232 ? -29.804 -26.950 11.427  1.00 55.62  ? 232 ARG A O   1 
ATOM   1889 C  CB  . ARG A 1 232 ? -29.228 -26.536 8.205   1.00 53.20  ? 232 ARG A CB  1 
ATOM   1890 C  CG  . ARG A 1 232 ? -30.459 -25.681 8.476   1.00 56.10  ? 232 ARG A CG  1 
ATOM   1891 C  CD  . ARG A 1 232 ? -31.275 -25.409 7.227   1.00 59.33  ? 232 ARG A CD  1 
ATOM   1892 N  NE  . ARG A 1 232 ? -32.168 -26.513 6.910   1.00 62.04  ? 232 ARG A NE  1 
ATOM   1893 C  CZ  . ARG A 1 232 ? -33.292 -26.796 7.563   1.00 67.08  ? 232 ARG A CZ  1 
ATOM   1894 N  NH1 . ARG A 1 232 ? -33.687 -26.052 8.588   1.00 68.40  ? 232 ARG A NH1 1 
ATOM   1895 N  NH2 . ARG A 1 232 ? -34.018 -27.836 7.188   1.00 68.35  ? 232 ARG A NH2 1 
ATOM   1896 N  N   . LYS A 1 233 ? -29.636 -28.869 10.178  1.00 50.17  ? 233 LYS A N   1 
ATOM   1897 C  CA  . LYS A 1 233 ? -30.615 -29.665 10.960  1.00 50.11  ? 233 LYS A CA  1 
ATOM   1898 C  C   . LYS A 1 233 ? -30.063 -29.837 12.379  1.00 49.94  ? 233 LYS A C   1 
ATOM   1899 O  O   . LYS A 1 233 ? -30.856 -29.703 13.322  1.00 52.17  ? 233 LYS A O   1 
ATOM   1900 C  CB  . LYS A 1 233 ? -30.968 -30.976 10.243  1.00 52.12  ? 233 LYS A CB  1 
ATOM   1901 C  CG  . LYS A 1 233 ? -32.207 -30.895 9.348   1.00 54.12  ? 233 LYS A CG  1 
ATOM   1902 C  CD  . LYS A 1 233 ? -32.439 -32.091 8.420   1.00 57.75  ? 233 LYS A CD  1 
ATOM   1903 C  CE  . LYS A 1 233 ? -33.365 -31.781 7.249   1.00 60.21  ? 233 LYS A CE  1 
ATOM   1904 N  NZ  . LYS A 1 233 ? -33.335 -32.812 6.175   1.00 57.53  ? 233 LYS A NZ  1 
ATOM   1905 N  N   . ILE A 1 234 ? -28.753 -30.049 12.533  1.00 48.90  ? 234 ILE A N   1 
ATOM   1906 C  CA  . ILE A 1 234 ? -28.093 -30.198 13.868  1.00 48.13  ? 234 ILE A CA  1 
ATOM   1907 C  C   . ILE A 1 234 ? -28.175 -28.878 14.649  1.00 48.63  ? 234 ILE A C   1 
ATOM   1908 O  O   . ILE A 1 234 ? -28.365 -28.941 15.873  1.00 53.94  ? 234 ILE A O   1 
ATOM   1909 C  CB  . ILE A 1 234 ? -26.634 -30.673 13.731  1.00 47.10  ? 234 ILE A CB  1 
ATOM   1910 C  CG1 . ILE A 1 234 ? -26.549 -32.089 13.159  1.00 46.47  ? 234 ILE A CG1 1 
ATOM   1911 C  CG2 . ILE A 1 234 ? -25.921 -30.562 15.070  1.00 47.83  ? 234 ILE A CG2 1 
ATOM   1912 C  CD1 . ILE A 1 234 ? -25.138 -32.608 13.002  1.00 46.14  ? 234 ILE A CD1 1 
ATOM   1913 N  N   . ASN A 1 235 ? -27.983 -27.735 13.985  1.00 50.03  ? 235 ASN A N   1 
ATOM   1914 C  CA  . ASN A 1 235 ? -28.112 -26.384 14.597  1.00 50.00  ? 235 ASN A CA  1 
ATOM   1915 C  C   . ASN A 1 235 ? -29.559 -26.209 15.058  1.00 50.37  ? 235 ASN A C   1 
ATOM   1916 O  O   . ASN A 1 235 ? -29.769 -25.713 16.181  1.00 48.39  ? 235 ASN A O   1 
ATOM   1917 C  CB  . ASN A 1 235 ? -27.689 -25.263 13.641  1.00 51.44  ? 235 ASN A CB  1 
ATOM   1918 C  CG  . ASN A 1 235 ? -26.209 -24.936 13.717  1.00 52.82  ? 235 ASN A CG  1 
ATOM   1919 O  OD1 . ASN A 1 235 ? -25.372 -25.624 13.127  1.00 51.48  ? 235 ASN A OD1 1 
ATOM   1920 N  ND2 . ASN A 1 235 ? -25.872 -23.872 14.430  1.00 53.05  ? 235 ASN A ND2 1 
ATOM   1921 N  N   . LEU A 1 236 ? -30.510 -26.630 14.222  1.00 52.42  ? 236 LEU A N   1 
ATOM   1922 C  CA  . LEU A 1 236 ? -31.965 -26.557 14.510  1.00 55.68  ? 236 LEU A CA  1 
ATOM   1923 C  C   . LEU A 1 236 ? -32.314 -27.461 15.703  1.00 58.59  ? 236 LEU A C   1 
ATOM   1924 O  O   . LEU A 1 236 ? -33.018 -26.980 16.605  1.00 60.86  ? 236 LEU A O   1 
ATOM   1925 C  CB  . LEU A 1 236 ? -32.742 -26.955 13.253  1.00 55.41  ? 236 LEU A CB  1 
ATOM   1926 C  CG  . LEU A 1 236 ? -34.235 -26.645 13.296  1.00 55.56  ? 236 LEU A CG  1 
ATOM   1927 C  CD1 . LEU A 1 236 ? -34.472 -25.144 13.226  1.00 54.24  ? 236 LEU A CD1 1 
ATOM   1928 C  CD2 . LEU A 1 236 ? -34.975 -27.366 12.175  1.00 56.71  ? 236 LEU A CD2 1 
ATOM   1929 N  N   . LYS A 1 237 ? -31.851 -28.717 15.708  1.00 63.70  ? 237 LYS A N   1 
ATOM   1930 C  CA  . LYS A 1 237 ? -31.987 -29.649 16.865  1.00 66.40  ? 237 LYS A CA  1 
ATOM   1931 C  C   . LYS A 1 237 ? -31.602 -28.901 18.141  1.00 65.24  ? 237 LYS A C   1 
ATOM   1932 O  O   . LYS A 1 237 ? -32.493 -28.651 18.966  1.00 68.30  ? 237 LYS A O   1 
ATOM   1933 C  CB  . LYS A 1 237 ? -31.095 -30.891 16.737  1.00 72.46  ? 237 LYS A CB  1 
ATOM   1934 C  CG  . LYS A 1 237 ? -31.763 -32.137 16.163  1.00 78.23  ? 237 LYS A CG  1 
ATOM   1935 C  CD  . LYS A 1 237 ? -31.272 -32.545 14.778  1.00 78.22  ? 237 LYS A CD  1 
ATOM   1936 C  CE  . LYS A 1 237 ? -31.879 -33.847 14.294  1.00 77.53  ? 237 LYS A CE  1 
ATOM   1937 N  NZ  . LYS A 1 237 ? -31.239 -34.334 13.049  1.00 77.01  ? 237 LYS A NZ  1 
ATOM   1938 N  N   . TYR A 1 238 ? -30.329 -28.517 18.258  1.00 64.08  ? 238 TYR A N   1 
ATOM   1939 C  CA  . TYR A 1 238 ? -29.722 -27.921 19.478  1.00 65.19  ? 238 TYR A CA  1 
ATOM   1940 C  C   . TYR A 1 238 ? -30.497 -26.677 19.935  1.00 66.88  ? 238 TYR A C   1 
ATOM   1941 O  O   . TYR A 1 238 ? -30.283 -26.280 21.094  1.00 77.92  ? 238 TYR A O   1 
ATOM   1942 C  CB  . TYR A 1 238 ? -28.242 -27.607 19.248  1.00 65.28  ? 238 TYR A CB  1 
ATOM   1943 C  CG  . TYR A 1 238 ? -27.569 -26.835 20.359  1.00 67.54  ? 238 TYR A CG  1 
ATOM   1944 C  CD1 . TYR A 1 238 ? -27.357 -27.396 21.610  1.00 69.88  ? 238 TYR A CD1 1 
ATOM   1945 C  CD2 . TYR A 1 238 ? -27.127 -25.537 20.159  1.00 70.32  ? 238 TYR A CD2 1 
ATOM   1946 C  CE1 . TYR A 1 238 ? -26.737 -26.687 22.631  1.00 71.15  ? 238 TYR A CE1 1 
ATOM   1947 C  CE2 . TYR A 1 238 ? -26.497 -24.817 21.165  1.00 72.42  ? 238 TYR A CE2 1 
ATOM   1948 C  CZ  . TYR A 1 238 ? -26.301 -25.390 22.410  1.00 70.78  ? 238 TYR A CZ  1 
ATOM   1949 O  OH  . TYR A 1 238 ? -25.677 -24.674 23.392  1.00 68.27  ? 238 TYR A OH  1 
ATOM   1950 N  N   . GLU A 1 239 ? -31.373 -26.094 19.106  1.00 66.53  ? 239 GLU A N   1 
ATOM   1951 C  CA  . GLU A 1 239 ? -32.223 -24.939 19.511  1.00 67.61  ? 239 GLU A CA  1 
ATOM   1952 C  C   . GLU A 1 239 ? -33.474 -25.443 20.239  1.00 66.18  ? 239 GLU A C   1 
ATOM   1953 O  O   . GLU A 1 239 ? -34.582 -25.213 19.724  1.00 64.05  ? 239 GLU A O   1 
ATOM   1954 C  CB  . GLU A 1 239 ? -32.595 -24.074 18.310  1.00 74.00  ? 239 GLU A CB  1 
ATOM   1955 C  CG  . GLU A 1 239 ? -31.422 -23.299 17.753  1.00 80.50  ? 239 GLU A CG  1 
ATOM   1956 C  CD  . GLU A 1 239 ? -31.660 -22.788 16.346  1.00 90.04  ? 239 GLU A CD  1 
ATOM   1957 O  OE1 . GLU A 1 239 ? -32.712 -22.148 16.122  1.00 95.72  ? 239 GLU A OE1 1 
ATOM   1958 O  OE2 . GLU A 1 239 ? -30.803 -23.044 15.476  1.00 106.09 ? 239 GLU A OE2 1 
ATOM   1959 N  N   . LYS A 1 240 ? -33.276 -26.106 21.387  1.00 67.53  ? 240 LYS A N   1 
ATOM   1960 C  CA  . LYS A 1 240 ? -34.314 -26.441 22.400  1.00 63.38  ? 240 LYS A CA  1 
ATOM   1961 C  C   . LYS A 1 240 ? -33.659 -26.477 23.783  1.00 59.17  ? 240 LYS A C   1 
ATOM   1962 O  O   . LYS A 1 240 ? -32.852 -25.600 24.072  1.00 54.63  ? 240 LYS A O   1 
ATOM   1963 C  CB  . LYS A 1 240 ? -34.984 -27.779 22.085  1.00 63.93  ? 240 LYS A CB  1 
ATOM   1964 C  CG  . LYS A 1 240 ? -36.019 -27.722 20.970  1.00 66.63  ? 240 LYS A CG  1 
ATOM   1965 C  CD  . LYS A 1 240 ? -35.471 -28.110 19.618  1.00 67.69  ? 240 LYS A CD  1 
ATOM   1966 C  CE  . LYS A 1 240 ? -36.336 -27.644 18.469  1.00 68.48  ? 240 LYS A CE  1 
ATOM   1967 N  NZ  . LYS A 1 240 ? -36.035 -28.409 17.238  1.00 72.27  ? 240 LYS A NZ  1 
ATOM   1968 N  N   . ASN B 1 2   ? -11.533 -55.472 24.986  1.00 62.64  ? 2   ASN B N   1 
ATOM   1969 C  CA  . ASN B 1 2   ? -12.690 -54.562 25.225  1.00 64.12  ? 2   ASN B CA  1 
ATOM   1970 C  C   . ASN B 1 2   ? -12.562 -53.968 26.630  1.00 68.18  ? 2   ASN B C   1 
ATOM   1971 O  O   . ASN B 1 2   ? -11.735 -54.494 27.395  1.00 74.28  ? 2   ASN B O   1 
ATOM   1972 C  CB  . ASN B 1 2   ? -14.033 -55.285 25.073  1.00 64.11  ? 2   ASN B CB  1 
ATOM   1973 C  CG  . ASN B 1 2   ? -15.206 -54.335 24.927  1.00 65.25  ? 2   ASN B CG  1 
ATOM   1974 O  OD1 . ASN B 1 2   ? -15.199 -53.469 24.053  1.00 68.39  ? 2   ASN B OD1 1 
ATOM   1975 N  ND2 . ASN B 1 2   ? -16.213 -54.475 25.779  1.00 63.27  ? 2   ASN B ND2 1 
ATOM   1976 N  N   . SER B 1 3   ? -13.333 -52.918 26.946  1.00 67.80  ? 3   SER B N   1 
ATOM   1977 C  CA  . SER B 1 3   ? -13.441 -52.311 28.301  1.00 65.79  ? 3   SER B CA  1 
ATOM   1978 C  C   . SER B 1 3   ? -14.568 -51.267 28.331  1.00 68.35  ? 3   SER B C   1 
ATOM   1979 O  O   . SER B 1 3   ? -15.134 -50.985 27.257  1.00 76.43  ? 3   SER B O   1 
ATOM   1980 C  CB  . SER B 1 3   ? -12.120 -51.716 28.737  1.00 64.14  ? 3   SER B CB  1 
ATOM   1981 O  OG  . SER B 1 3   ? -12.099 -50.310 28.560  1.00 62.03  ? 3   SER B OG  1 
ATOM   1982 N  N   . THR B 1 4   ? -14.876 -50.717 29.514  1.00 66.57  ? 4   THR B N   1 
ATOM   1983 C  CA  . THR B 1 4   ? -15.773 -49.542 29.697  1.00 66.38  ? 4   THR B CA  1 
ATOM   1984 C  C   . THR B 1 4   ? -14.997 -48.377 30.313  1.00 63.75  ? 4   THR B C   1 
ATOM   1985 O  O   . THR B 1 4   ? -15.655 -47.436 30.788  1.00 63.83  ? 4   THR B O   1 
ATOM   1986 C  CB  . THR B 1 4   ? -16.986 -49.851 30.580  1.00 70.89  ? 4   THR B CB  1 
ATOM   1987 O  OG1 . THR B 1 4   ? -16.504 -50.133 31.895  1.00 77.90  ? 4   THR B OG1 1 
ATOM   1988 C  CG2 . THR B 1 4   ? -17.827 -50.990 30.049  1.00 71.40  ? 4   THR B CG2 1 
ATOM   1989 N  N   . GLU B 1 5   ? -13.661 -48.436 30.312  1.00 64.01  ? 5   GLU B N   1 
ATOM   1990 C  CA  . GLU B 1 5   ? -12.786 -47.278 30.638  1.00 67.30  ? 5   GLU B CA  1 
ATOM   1991 C  C   . GLU B 1 5   ? -13.176 -46.128 29.699  1.00 73.89  ? 5   GLU B C   1 
ATOM   1992 O  O   . GLU B 1 5   ? -13.478 -46.414 28.520  1.00 81.92  ? 5   GLU B O   1 
ATOM   1993 C  CB  . GLU B 1 5   ? -11.308 -47.660 30.505  1.00 65.43  ? 5   GLU B CB  1 
ATOM   1994 C  CG  . GLU B 1 5   ? -10.350 -46.488 30.669  1.00 65.92  ? 5   GLU B CG  1 
ATOM   1995 C  CD  . GLU B 1 5   ? -8.955  -46.861 31.154  1.00 64.63  ? 5   GLU B CD  1 
ATOM   1996 O  OE1 . GLU B 1 5   ? -8.424  -47.910 30.705  1.00 58.02  ? 5   GLU B OE1 1 
ATOM   1997 O  OE2 . GLU B 1 5   ? -8.400  -46.098 31.985  1.00 62.82  ? 5   GLU B OE2 1 
ATOM   1998 N  N   . ASN B 1 6   ? -13.206 -44.888 30.199  1.00 76.09  ? 6   ASN B N   1 
ATOM   1999 C  CA  . ASN B 1 6   ? -13.755 -43.725 29.449  1.00 76.07  ? 6   ASN B CA  1 
ATOM   2000 C  C   . ASN B 1 6   ? -12.961 -43.553 28.149  1.00 78.59  ? 6   ASN B C   1 
ATOM   2001 O  O   . ASN B 1 6   ? -11.712 -43.524 28.230  1.00 80.53  ? 6   ASN B O   1 
ATOM   2002 C  CB  . ASN B 1 6   ? -13.754 -42.431 30.263  1.00 72.93  ? 6   ASN B CB  1 
ATOM   2003 C  CG  . ASN B 1 6   ? -14.361 -41.276 29.494  1.00 72.04  ? 6   ASN B CG  1 
ATOM   2004 O  OD1 . ASN B 1 6   ? -15.484 -41.370 29.001  1.00 75.33  ? 6   ASN B OD1 1 
ATOM   2005 N  ND2 . ASN B 1 6   ? -13.616 -40.192 29.361  1.00 70.79  ? 6   ASN B ND2 1 
ATOM   2006 N  N   . LYS B 1 7   ? -13.678 -43.476 27.018  1.00 76.40  ? 7   LYS B N   1 
ATOM   2007 C  CA  . LYS B 1 7   ? -13.145 -43.324 25.636  1.00 72.59  ? 7   LYS B CA  1 
ATOM   2008 C  C   . LYS B 1 7   ? -13.468 -41.928 25.085  1.00 66.51  ? 7   LYS B C   1 
ATOM   2009 O  O   . LYS B 1 7   ? -12.729 -41.464 24.199  1.00 67.11  ? 7   LYS B O   1 
ATOM   2010 C  CB  . LYS B 1 7   ? -13.772 -44.379 24.720  1.00 75.40  ? 7   LYS B CB  1 
ATOM   2011 C  CG  . LYS B 1 7   ? -13.435 -45.821 25.063  1.00 78.01  ? 7   LYS B CG  1 
ATOM   2012 C  CD  . LYS B 1 7   ? -14.629 -46.753 24.959  1.00 82.21  ? 7   LYS B CD  1 
ATOM   2013 C  CE  . LYS B 1 7   ? -14.251 -48.220 24.917  1.00 84.46  ? 7   LYS B CE  1 
ATOM   2014 N  NZ  . LYS B 1 7   ? -13.232 -48.557 25.940  1.00 85.43  ? 7   LYS B NZ  1 
ATOM   2015 N  N   . ASN B 1 8   ? -14.540 -41.297 25.571  1.00 59.18  ? 8   ASN B N   1 
ATOM   2016 C  CA  . ASN B 1 8   ? -15.018 -39.978 25.087  1.00 55.65  ? 8   ASN B CA  1 
ATOM   2017 C  C   . ASN B 1 8   ? -14.271 -38.865 25.820  1.00 55.33  ? 8   ASN B C   1 
ATOM   2018 O  O   . ASN B 1 8   ? -14.476 -38.731 27.032  1.00 57.60  ? 8   ASN B O   1 
ATOM   2019 C  CB  . ASN B 1 8   ? -16.527 -39.858 25.259  1.00 54.13  ? 8   ASN B CB  1 
ATOM   2020 C  CG  . ASN B 1 8   ? -17.262 -40.842 24.382  1.00 55.52  ? 8   ASN B CG  1 
ATOM   2021 O  OD1 . ASN B 1 8   ? -16.662 -41.475 23.518  1.00 56.76  ? 8   ASN B OD1 1 
ATOM   2022 N  ND2 . ASN B 1 8   ? -18.558 -40.971 24.598  1.00 57.07  ? 8   ASN B ND2 1 
ATOM   2023 N  N   . PHE B 1 9   ? -13.438 -38.111 25.096  1.00 55.99  ? 9   PHE B N   1 
ATOM   2024 C  CA  . PHE B 1 9   ? -12.619 -36.989 25.621  1.00 54.67  ? 9   PHE B CA  1 
ATOM   2025 C  C   . PHE B 1 9   ? -12.907 -35.715 24.824  1.00 53.39  ? 9   PHE B C   1 
ATOM   2026 O  O   . PHE B 1 9   ? -12.813 -35.739 23.585  1.00 56.86  ? 9   PHE B O   1 
ATOM   2027 C  CB  . PHE B 1 9   ? -11.137 -37.353 25.584  1.00 55.33  ? 9   PHE B CB  1 
ATOM   2028 C  CG  . PHE B 1 9   ? -10.785 -38.425 26.577  1.00 58.99  ? 9   PHE B CG  1 
ATOM   2029 C  CD1 . PHE B 1 9   ? -11.084 -39.750 26.313  1.00 61.52  ? 9   PHE B CD1 1 
ATOM   2030 C  CD2 . PHE B 1 9   ? -10.214 -38.106 27.798  1.00 64.63  ? 9   PHE B CD2 1 
ATOM   2031 C  CE1 . PHE B 1 9   ? -10.789 -40.742 27.233  1.00 64.90  ? 9   PHE B CE1 1 
ATOM   2032 C  CE2 . PHE B 1 9   ? -9.921  -39.098 28.722  1.00 65.94  ? 9   PHE B CE2 1 
ATOM   2033 C  CZ  . PHE B 1 9   ? -10.206 -40.415 28.436  1.00 67.50  ? 9   PHE B CZ  1 
ATOM   2034 N  N   . VAL B 1 10  ? -13.237 -34.639 25.542  1.00 51.47  ? 10  VAL B N   1 
ATOM   2035 C  CA  . VAL B 1 10  ? -13.534 -33.285 24.993  1.00 48.40  ? 10  VAL B CA  1 
ATOM   2036 C  C   . VAL B 1 10  ? -12.371 -32.356 25.344  1.00 48.21  ? 10  VAL B C   1 
ATOM   2037 O  O   . VAL B 1 10  ? -12.317 -31.902 26.501  1.00 45.50  ? 10  VAL B O   1 
ATOM   2038 C  CB  . VAL B 1 10  ? -14.859 -32.747 25.558  1.00 47.06  ? 10  VAL B CB  1 
ATOM   2039 C  CG1 . VAL B 1 10  ? -15.211 -31.401 24.950  1.00 47.61  ? 10  VAL B CG1 1 
ATOM   2040 C  CG2 . VAL B 1 10  ? -15.991 -33.743 25.369  1.00 47.06  ? 10  VAL B CG2 1 
ATOM   2041 N  N   . ILE B 1 11  ? -11.486 -32.084 24.378  1.00 48.67  ? 11  ILE B N   1 
ATOM   2042 C  CA  . ILE B 1 11  ? -10.360 -31.117 24.533  1.00 50.14  ? 11  ILE B CA  1 
ATOM   2043 C  C   . ILE B 1 11  ? -10.979 -29.753 24.832  1.00 51.91  ? 11  ILE B C   1 
ATOM   2044 O  O   . ILE B 1 11  ? -11.860 -29.332 24.076  1.00 57.74  ? 11  ILE B O   1 
ATOM   2045 C  CB  . ILE B 1 11  ? -9.462  -31.058 23.281  1.00 50.87  ? 11  ILE B CB  1 
ATOM   2046 C  CG1 . ILE B 1 11  ? -8.883  -32.428 22.914  1.00 51.69  ? 11  ILE B CG1 1 
ATOM   2047 C  CG2 . ILE B 1 11  ? -8.369  -30.015 23.467  1.00 51.31  ? 11  ILE B CG2 1 
ATOM   2048 C  CD1 . ILE B 1 11  ? -8.498  -32.571 21.454  1.00 50.73  ? 11  ILE B CD1 1 
ATOM   2049 N  N   . SER B 1 12  ? -10.534 -29.105 25.902  1.00 54.48  ? 12  SER B N   1 
ATOM   2050 C  CA  . SER B 1 12  ? -11.122 -27.849 26.421  1.00 57.62  ? 12  SER B CA  1 
ATOM   2051 C  C   . SER B 1 12  ? -10.069 -27.079 27.214  1.00 61.28  ? 12  SER B C   1 
ATOM   2052 O  O   . SER B 1 12  ? -9.335  -27.704 27.994  1.00 62.63  ? 12  SER B O   1 
ATOM   2053 C  CB  . SER B 1 12  ? -12.338 -28.135 27.259  1.00 56.54  ? 12  SER B CB  1 
ATOM   2054 O  OG  . SER B 1 12  ? -12.884 -26.932 27.773  1.00 55.94  ? 12  SER B OG  1 
ATOM   2055 N  N   . ILE B 1 13  ? -10.012 -25.765 27.018  1.00 67.39  ? 13  ILE B N   1 
ATOM   2056 C  CA  . ILE B 1 13  ? -9.154  -24.838 27.808  1.00 68.86  ? 13  ILE B CA  1 
ATOM   2057 C  C   . ILE B 1 13  ? -9.775  -24.792 29.207  1.00 67.28  ? 13  ILE B C   1 
ATOM   2058 O  O   . ILE B 1 13  ? -10.977 -24.465 29.291  1.00 64.52  ? 13  ILE B O   1 
ATOM   2059 C  CB  . ILE B 1 13  ? -9.076  -23.449 27.132  1.00 70.89  ? 13  ILE B CB  1 
ATOM   2060 C  CG1 . ILE B 1 13  ? -8.925  -23.541 25.608  1.00 72.30  ? 13  ILE B CG1 1 
ATOM   2061 C  CG2 . ILE B 1 13  ? -7.968  -22.610 27.743  1.00 70.95  ? 13  ILE B CG2 1 
ATOM   2062 C  CD1 . ILE B 1 13  ? -10.176 -23.177 24.824  1.00 71.43  ? 13  ILE B CD1 1 
ATOM   2063 N  N   . SER B 1 14  ? -9.008  -25.145 30.245  1.00 70.13  ? 14  SER B N   1 
ATOM   2064 C  CA  . SER B 1 14  ? -9.490  -25.376 31.640  1.00 73.97  ? 14  SER B CA  1 
ATOM   2065 C  C   . SER B 1 14  ? -10.545 -24.336 32.058  1.00 74.43  ? 14  SER B C   1 
ATOM   2066 O  O   . SER B 1 14  ? -11.557 -24.746 32.667  1.00 66.23  ? 14  SER B O   1 
ATOM   2067 C  CB  . SER B 1 14  ? -8.335  -25.418 32.621  1.00 71.54  ? 14  SER B CB  1 
ATOM   2068 O  OG  . SER B 1 14  ? -7.444  -24.330 32.418  1.00 70.21  ? 14  SER B OG  1 
ATOM   2069 N  N   . THR B 1 15  ? -10.331 -23.060 31.710  1.00 79.05  ? 15  THR B N   1 
ATOM   2070 C  CA  . THR B 1 15  ? -11.124 -21.878 32.146  1.00 78.40  ? 15  THR B CA  1 
ATOM   2071 C  C   . THR B 1 15  ? -12.313 -21.594 31.211  1.00 77.15  ? 15  THR B C   1 
ATOM   2072 O  O   . THR B 1 15  ? -13.132 -20.738 31.586  1.00 76.04  ? 15  THR B O   1 
ATOM   2073 C  CB  . THR B 1 15  ? -10.224 -20.637 32.212  1.00 79.34  ? 15  THR B CB  1 
ATOM   2074 O  OG1 . THR B 1 15  ? -9.506  -20.555 30.979  1.00 77.92  ? 15  THR B OG1 1 
ATOM   2075 C  CG2 . THR B 1 15  ? -9.246  -20.670 33.364  1.00 78.35  ? 15  THR B CG2 1 
ATOM   2076 N  N   . ALA B 1 16  ? -12.401 -22.266 30.053  1.00 75.29  ? 16  ALA B N   1 
ATOM   2077 C  CA  . ALA B 1 16  ? -13.433 -22.045 29.009  1.00 73.12  ? 16  ALA B CA  1 
ATOM   2078 C  C   . ALA B 1 16  ? -14.817 -22.409 29.564  1.00 69.65  ? 16  ALA B C   1 
ATOM   2079 O  O   . ALA B 1 16  ? -15.503 -23.260 28.967  1.00 67.70  ? 16  ALA B O   1 
ATOM   2080 C  CB  . ALA B 1 16  ? -13.096 -22.842 27.771  1.00 74.33  ? 16  ALA B CB  1 
ATOM   2081 N  N   . GLU B 1 17  ? -15.214 -21.749 30.653  1.00 69.54  ? 17  GLU B N   1 
ATOM   2082 C  CA  . GLU B 1 17  ? -16.434 -22.051 31.442  1.00 72.09  ? 17  GLU B CA  1 
ATOM   2083 C  C   . GLU B 1 17  ? -17.629 -22.182 30.499  1.00 70.19  ? 17  GLU B C   1 
ATOM   2084 O  O   . GLU B 1 17  ? -18.270 -23.237 30.523  1.00 64.69  ? 17  GLU B O   1 
ATOM   2085 C  CB  . GLU B 1 17  ? -16.671 -20.948 32.473  1.00 78.63  ? 17  GLU B CB  1 
ATOM   2086 C  CG  . GLU B 1 17  ? -17.942 -21.156 33.271  1.00 83.05  ? 17  GLU B CG  1 
ATOM   2087 C  CD  . GLU B 1 17  ? -18.286 -20.054 34.253  1.00 86.30  ? 17  GLU B CD  1 
ATOM   2088 O  OE1 . GLU B 1 17  ? -18.966 -20.354 35.255  1.00 84.74  ? 17  GLU B OE1 1 
ATOM   2089 O  OE2 . GLU B 1 17  ? -17.892 -18.898 34.001  1.00 93.38  ? 17  GLU B OE2 1 
ATOM   2090 N  N   . GLN B 1 18  ? -17.893 -21.132 29.714  1.00 76.04  ? 18  GLN B N   1 
ATOM   2091 C  CA  . GLN B 1 18  ? -19.002 -21.005 28.727  1.00 81.00  ? 18  GLN B CA  1 
ATOM   2092 C  C   . GLN B 1 18  ? -19.187 -22.304 27.931  1.00 77.99  ? 18  GLN B C   1 
ATOM   2093 O  O   . GLN B 1 18  ? -20.293 -22.897 27.974  1.00 74.33  ? 18  GLN B O   1 
ATOM   2094 C  CB  . GLN B 1 18  ? -18.665 -19.892 27.727  1.00 89.20  ? 18  GLN B CB  1 
ATOM   2095 C  CG  . GLN B 1 18  ? -18.873 -18.474 28.242  1.00 92.23  ? 18  GLN B CG  1 
ATOM   2096 C  CD  . GLN B 1 18  ? -20.068 -17.830 27.581  1.00 99.12  ? 18  GLN B CD  1 
ATOM   2097 O  OE1 . GLN B 1 18  ? -19.951 -17.147 26.562  1.00 95.53  ? 18  GLN B OE1 1 
ATOM   2098 N  NE2 . GLN B 1 18  ? -21.241 -18.084 28.139  1.00 103.77 ? 18  GLN B NE2 1 
ATOM   2099 N  N   . ARG B 1 19  ? -18.136 -22.708 27.210  1.00 74.10  ? 19  ARG B N   1 
ATOM   2100 C  CA  . ARG B 1 19  ? -18.128 -23.896 26.315  1.00 77.02  ? 19  ARG B CA  1 
ATOM   2101 C  C   . ARG B 1 19  ? -18.437 -25.149 27.141  1.00 73.27  ? 19  ARG B C   1 
ATOM   2102 O  O   . ARG B 1 19  ? -19.390 -25.871 26.800  1.00 75.34  ? 19  ARG B O   1 
ATOM   2103 C  CB  . ARG B 1 19  ? -16.772 -24.026 25.613  1.00 79.14  ? 19  ARG B CB  1 
ATOM   2104 C  CG  . ARG B 1 19  ? -16.613 -23.146 24.381  1.00 84.23  ? 19  ARG B CG  1 
ATOM   2105 C  CD  . ARG B 1 19  ? -15.273 -23.353 23.698  1.00 84.81  ? 19  ARG B CD  1 
ATOM   2106 N  NE  . ARG B 1 19  ? -14.982 -22.381 22.653  1.00 83.75  ? 19  ARG B NE  1 
ATOM   2107 C  CZ  . ARG B 1 19  ? -13.835 -22.294 21.980  1.00 85.29  ? 19  ARG B CZ  1 
ATOM   2108 N  NH1 . ARG B 1 19  ? -12.836 -23.125 22.223  1.00 87.99  ? 19  ARG B NH1 1 
ATOM   2109 N  NH2 . ARG B 1 19  ? -13.684 -21.361 21.058  1.00 85.87  ? 19  ARG B NH2 1 
ATOM   2110 N  N   . ARG B 1 20  ? -17.662 -25.378 28.201  1.00 70.59  ? 20  ARG B N   1 
ATOM   2111 C  CA  . ARG B 1 20  ? -17.752 -26.585 29.064  1.00 65.95  ? 20  ARG B CA  1 
ATOM   2112 C  C   . ARG B 1 20  ? -19.221 -26.827 29.438  1.00 60.82  ? 20  ARG B C   1 
ATOM   2113 O  O   . ARG B 1 20  ? -19.701 -27.958 29.248  1.00 55.43  ? 20  ARG B O   1 
ATOM   2114 C  CB  . ARG B 1 20  ? -16.825 -26.429 30.276  1.00 66.62  ? 20  ARG B CB  1 
ATOM   2115 C  CG  . ARG B 1 20  ? -15.344 -26.389 29.914  1.00 67.80  ? 20  ARG B CG  1 
ATOM   2116 C  CD  . ARG B 1 20  ? -14.422 -26.989 30.965  1.00 69.54  ? 20  ARG B CD  1 
ATOM   2117 N  NE  . ARG B 1 20  ? -13.055 -27.152 30.473  1.00 71.09  ? 20  ARG B NE  1 
ATOM   2118 C  CZ  . ARG B 1 20  ? -12.163 -28.029 30.939  1.00 70.92  ? 20  ARG B CZ  1 
ATOM   2119 N  NH1 . ARG B 1 20  ? -12.478 -28.855 31.924  1.00 71.28  ? 20  ARG B NH1 1 
ATOM   2120 N  NH2 . ARG B 1 20  ? -10.954 -28.094 30.405  1.00 69.35  ? 20  ARG B NH2 1 
ATOM   2121 N  N   . ASN B 1 21  ? -19.917 -25.790 29.906  1.00 61.10  ? 21  ASN B N   1 
ATOM   2122 C  CA  . ASN B 1 21  ? -21.357 -25.864 30.275  1.00 64.79  ? 21  ASN B CA  1 
ATOM   2123 C  C   . ASN B 1 21  ? -22.151 -26.321 29.051  1.00 64.61  ? 21  ASN B C   1 
ATOM   2124 O  O   . ASN B 1 21  ? -22.907 -27.305 29.182  1.00 62.80  ? 21  ASN B O   1 
ATOM   2125 C  CB  . ASN B 1 21  ? -21.913 -24.533 30.783  1.00 67.92  ? 21  ASN B CB  1 
ATOM   2126 C  CG  . ASN B 1 21  ? -21.057 -23.904 31.858  1.00 71.36  ? 21  ASN B CG  1 
ATOM   2127 O  OD1 . ASN B 1 21  ? -20.643 -24.569 32.805  1.00 70.20  ? 21  ASN B OD1 1 
ATOM   2128 N  ND2 . ASN B 1 21  ? -20.764 -22.624 31.696  1.00 76.76  ? 21  ASN B ND2 1 
ATOM   2129 N  N   . HIS B 1 22  ? -21.977 -25.622 27.922  1.00 66.56  ? 22  HIS B N   1 
ATOM   2130 C  CA  . HIS B 1 22  ? -22.615 -25.934 26.615  1.00 68.95  ? 22  HIS B CA  1 
ATOM   2131 C  C   . HIS B 1 22  ? -22.444 -27.431 26.332  1.00 64.62  ? 22  HIS B C   1 
ATOM   2132 O  O   . HIS B 1 22  ? -23.459 -28.092 26.051  1.00 60.19  ? 22  HIS B O   1 
ATOM   2133 C  CB  . HIS B 1 22  ? -22.065 -25.033 25.494  1.00 76.44  ? 22  HIS B CB  1 
ATOM   2134 C  CG  . HIS B 1 22  ? -22.705 -23.689 25.447  1.00 81.42  ? 22  HIS B CG  1 
ATOM   2135 N  ND1 . HIS B 1 22  ? -23.877 -23.401 26.123  1.00 83.87  ? 22  HIS B ND1 1 
ATOM   2136 C  CD2 . HIS B 1 22  ? -22.352 -22.562 24.797  1.00 86.57  ? 22  HIS B CD2 1 
ATOM   2137 C  CE1 . HIS B 1 22  ? -24.209 -22.145 25.907  1.00 88.04  ? 22  HIS B CE1 1 
ATOM   2138 N  NE2 . HIS B 1 22  ? -23.290 -21.609 25.093  1.00 91.24  ? 22  HIS B NE2 1 
ATOM   2139 N  N   . ILE B 1 23  ? -21.218 -27.947 26.475  1.00 61.08  ? 23  ILE B N   1 
ATOM   2140 C  CA  . ILE B 1 23  ? -20.862 -29.382 26.265  1.00 58.37  ? 23  ILE B CA  1 
ATOM   2141 C  C   . ILE B 1 23  ? -21.665 -30.243 27.246  1.00 55.71  ? 23  ILE B C   1 
ATOM   2142 O  O   . ILE B 1 23  ? -22.461 -31.089 26.790  1.00 50.38  ? 23  ILE B O   1 
ATOM   2143 C  CB  . ILE B 1 23  ? -19.342 -29.587 26.446  1.00 59.72  ? 23  ILE B CB  1 
ATOM   2144 C  CG1 . ILE B 1 23  ? -18.530 -28.871 25.360  1.00 60.74  ? 23  ILE B CG1 1 
ATOM   2145 C  CG2 . ILE B 1 23  ? -18.989 -31.064 26.544  1.00 58.78  ? 23  ILE B CG2 1 
ATOM   2146 C  CD1 . ILE B 1 23  ? -18.866 -29.283 23.951  1.00 62.50  ? 23  ILE B CD1 1 
ATOM   2147 N  N   . ILE B 1 24  ? -21.460 -30.017 28.546  1.00 57.75  ? 24  ILE B N   1 
ATOM   2148 C  CA  . ILE B 1 24  ? -22.070 -30.813 29.651  1.00 58.14  ? 24  ILE B CA  1 
ATOM   2149 C  C   . ILE B 1 24  ? -23.560 -31.013 29.357  1.00 60.63  ? 24  ILE B C   1 
ATOM   2150 O  O   . ILE B 1 24  ? -24.003 -32.173 29.357  1.00 64.52  ? 24  ILE B O   1 
ATOM   2151 C  CB  . ILE B 1 24  ? -21.827 -30.132 31.009  1.00 56.92  ? 24  ILE B CB  1 
ATOM   2152 C  CG1 . ILE B 1 24  ? -20.359 -30.238 31.429  1.00 56.03  ? 24  ILE B CG1 1 
ATOM   2153 C  CG2 . ILE B 1 24  ? -22.757 -30.690 32.076  1.00 58.06  ? 24  ILE B CG2 1 
ATOM   2154 C  CD1 . ILE B 1 24  ? -19.910 -29.140 32.357  1.00 55.86  ? 24  ILE B CD1 1 
ATOM   2155 N  N   . GLU B 1 25  ? -24.288 -29.924 29.086  1.00 62.09  ? 25  GLU B N   1 
ATOM   2156 C  CA  . GLU B 1 25  ? -25.754 -29.935 28.818  1.00 64.35  ? 25  GLU B CA  1 
ATOM   2157 C  C   . GLU B 1 25  ? -26.068 -30.979 27.740  1.00 65.64  ? 25  GLU B C   1 
ATOM   2158 O  O   . GLU B 1 25  ? -27.060 -31.706 27.906  1.00 66.98  ? 25  GLU B O   1 
ATOM   2159 C  CB  . GLU B 1 25  ? -26.256 -28.560 28.369  1.00 69.07  ? 25  GLU B CB  1 
ATOM   2160 C  CG  . GLU B 1 25  ? -26.097 -27.467 29.419  1.00 73.80  ? 25  GLU B CG  1 
ATOM   2161 C  CD  . GLU B 1 25  ? -26.341 -26.034 28.956  1.00 77.84  ? 25  GLU B CD  1 
ATOM   2162 O  OE1 . GLU B 1 25  ? -25.896 -25.666 27.836  1.00 76.56  ? 25  GLU B OE1 1 
ATOM   2163 O  OE2 . GLU B 1 25  ? -26.975 -25.273 29.725  1.00 78.06  ? 25  GLU B OE2 1 
ATOM   2164 N  N   . GLN B 1 26  ? -25.241 -31.055 26.691  1.00 67.10  ? 26  GLN B N   1 
ATOM   2165 C  CA  . GLN B 1 26  ? -25.490 -31.886 25.480  1.00 68.34  ? 26  GLN B CA  1 
ATOM   2166 C  C   . GLN B 1 26  ? -25.243 -33.364 25.785  1.00 66.35  ? 26  GLN B C   1 
ATOM   2167 O  O   . GLN B 1 26  ? -26.136 -34.177 25.504  1.00 65.73  ? 26  GLN B O   1 
ATOM   2168 C  CB  . GLN B 1 26  ? -24.585 -31.468 24.320  1.00 67.91  ? 26  GLN B CB  1 
ATOM   2169 C  CG  . GLN B 1 26  ? -24.829 -30.044 23.853  1.00 66.48  ? 26  GLN B CG  1 
ATOM   2170 C  CD  . GLN B 1 26  ? -24.163 -29.776 22.529  1.00 63.88  ? 26  GLN B CD  1 
ATOM   2171 O  OE1 . GLN B 1 26  ? -24.565 -30.305 21.497  1.00 66.60  ? 26  GLN B OE1 1 
ATOM   2172 N  NE2 . GLN B 1 26  ? -23.126 -28.956 22.556  1.00 64.29  ? 26  GLN B NE2 1 
ATOM   2173 N  N   . PHE B 1 27  ? -24.053 -33.692 26.289  1.00 64.94  ? 27  PHE B N   1 
ATOM   2174 C  CA  . PHE B 1 27  ? -23.612 -35.087 26.550  1.00 66.33  ? 27  PHE B CA  1 
ATOM   2175 C  C   . PHE B 1 27  ? -24.530 -35.708 27.601  1.00 68.36  ? 27  PHE B C   1 
ATOM   2176 O  O   . PHE B 1 27  ? -24.978 -36.858 27.415  1.00 76.07  ? 27  PHE B O   1 
ATOM   2177 C  CB  . PHE B 1 27  ? -22.144 -35.123 26.971  1.00 66.96  ? 27  PHE B CB  1 
ATOM   2178 C  CG  . PHE B 1 27  ? -21.194 -35.123 25.801  1.00 66.86  ? 27  PHE B CG  1 
ATOM   2179 C  CD1 . PHE B 1 27  ? -20.852 -33.942 25.165  1.00 65.95  ? 27  PHE B CD1 1 
ATOM   2180 C  CD2 . PHE B 1 27  ? -20.676 -36.311 25.312  1.00 68.01  ? 27  PHE B CD2 1 
ATOM   2181 C  CE1 . PHE B 1 27  ? -19.989 -33.947 24.081  1.00 66.82  ? 27  PHE B CE1 1 
ATOM   2182 C  CE2 . PHE B 1 27  ? -19.813 -36.315 24.227  1.00 67.50  ? 27  PHE B CE2 1 
ATOM   2183 C  CZ  . PHE B 1 27  ? -19.467 -35.132 23.617  1.00 67.63  ? 27  PHE B CZ  1 
ATOM   2184 N  N   . THR B 1 28  ? -24.815 -34.945 28.656  1.00 64.30  ? 28  THR B N   1 
ATOM   2185 C  CA  . THR B 1 28  ? -25.804 -35.293 29.704  1.00 62.31  ? 28  THR B CA  1 
ATOM   2186 C  C   . THR B 1 28  ? -27.144 -35.610 29.033  1.00 61.53  ? 28  THR B C   1 
ATOM   2187 O  O   . THR B 1 28  ? -27.564 -36.777 29.104  1.00 65.07  ? 28  THR B O   1 
ATOM   2188 C  CB  . THR B 1 28  ? -25.905 -34.173 30.743  1.00 63.51  ? 28  THR B CB  1 
ATOM   2189 O  OG1 . THR B 1 28  ? -24.578 -33.851 31.163  1.00 62.11  ? 28  THR B OG1 1 
ATOM   2190 C  CG2 . THR B 1 28  ? -26.747 -34.567 31.937  1.00 65.76  ? 28  THR B CG2 1 
ATOM   2191 N  N   . HIS B 1 29  ? -27.745 -34.628 28.354  1.00 60.11  ? 29  HIS B N   1 
ATOM   2192 C  CA  . HIS B 1 29  ? -29.114 -34.690 27.769  1.00 59.89  ? 29  HIS B CA  1 
ATOM   2193 C  C   . HIS B 1 29  ? -29.294 -35.972 26.945  1.00 62.41  ? 29  HIS B C   1 
ATOM   2194 O  O   . HIS B 1 29  ? -30.432 -36.465 26.909  1.00 71.58  ? 29  HIS B O   1 
ATOM   2195 C  CB  . HIS B 1 29  ? -29.408 -33.412 26.965  1.00 60.52  ? 29  HIS B CB  1 
ATOM   2196 C  CG  . HIS B 1 29  ? -30.685 -33.414 26.190  1.00 64.17  ? 29  HIS B CG  1 
ATOM   2197 N  ND1 . HIS B 1 29  ? -30.851 -34.136 25.019  1.00 66.94  ? 29  HIS B ND1 1 
ATOM   2198 C  CD2 . HIS B 1 29  ? -31.838 -32.737 26.378  1.00 65.31  ? 29  HIS B CD2 1 
ATOM   2199 C  CE1 . HIS B 1 29  ? -32.060 -33.927 24.539  1.00 66.21  ? 29  HIS B CE1 1 
ATOM   2200 N  NE2 . HIS B 1 29  ? -32.682 -33.068 25.351  1.00 66.85  ? 29  HIS B NE2 1 
ATOM   2201 N  N   . GLN B 1 30  ? -28.237 -36.488 26.303  1.00 61.71  ? 30  GLN B N   1 
ATOM   2202 C  CA  . GLN B 1 30  ? -28.301 -37.722 25.471  1.00 60.74  ? 30  GLN B CA  1 
ATOM   2203 C  C   . GLN B 1 30  ? -27.663 -38.894 26.221  1.00 61.03  ? 30  GLN B C   1 
ATOM   2204 O  O   . GLN B 1 30  ? -27.510 -39.968 25.610  1.00 63.94  ? 30  GLN B O   1 
ATOM   2205 C  CB  . GLN B 1 30  ? -27.630 -37.506 24.115  1.00 61.72  ? 30  GLN B CB  1 
ATOM   2206 C  CG  . GLN B 1 30  ? -28.567 -36.896 23.084  1.00 61.56  ? 30  GLN B CG  1 
ATOM   2207 C  CD  . GLN B 1 30  ? -27.970 -36.902 21.699  1.00 59.38  ? 30  GLN B CD  1 
ATOM   2208 O  OE1 . GLN B 1 30  ? -28.055 -37.883 20.966  1.00 56.32  ? 30  GLN B OE1 1 
ATOM   2209 N  NE2 . GLN B 1 30  ? -27.384 -35.782 21.324  1.00 58.70  ? 30  GLN B NE2 1 
ATOM   2210 N  N   . ASN B 1 31  ? -27.327 -38.705 27.497  1.00 60.83  ? 31  ASN B N   1 
ATOM   2211 C  CA  . ASN B 1 31  ? -26.850 -39.789 28.389  1.00 63.57  ? 31  ASN B CA  1 
ATOM   2212 C  C   . ASN B 1 31  ? -25.603 -40.422 27.763  1.00 60.35  ? 31  ASN B C   1 
ATOM   2213 O  O   . ASN B 1 31  ? -25.645 -41.606 27.388  1.00 62.60  ? 31  ASN B O   1 
ATOM   2214 C  CB  . ASN B 1 31  ? -27.966 -40.803 28.644  1.00 68.54  ? 31  ASN B CB  1 
ATOM   2215 C  CG  . ASN B 1 31  ? -27.633 -41.740 29.781  1.00 74.31  ? 31  ASN B CG  1 
ATOM   2216 O  OD1 . ASN B 1 31  ? -28.160 -42.848 29.855  1.00 80.37  ? 31  ASN B OD1 1 
ATOM   2217 N  ND2 . ASN B 1 31  ? -26.750 -41.303 30.664  1.00 78.42  ? 31  ASN B ND2 1 
ATOM   2218 N  N   . ILE B 1 32  ? -24.546 -39.624 27.623  1.00 56.00  ? 32  ILE B N   1 
ATOM   2219 C  CA  . ILE B 1 32  ? -23.257 -40.027 26.992  1.00 52.37  ? 32  ILE B CA  1 
ATOM   2220 C  C   . ILE B 1 32  ? -22.144 -39.769 27.999  1.00 51.27  ? 32  ILE B C   1 
ATOM   2221 O  O   . ILE B 1 32  ? -21.875 -38.631 28.372  1.00 51.25  ? 32  ILE B O   1 
ATOM   2222 C  CB  . ILE B 1 32  ? -23.035 -39.283 25.661  1.00 50.52  ? 32  ILE B CB  1 
ATOM   2223 C  CG1 . ILE B 1 32  ? -24.236 -39.442 24.727  1.00 50.59  ? 32  ILE B CG1 1 
ATOM   2224 C  CG2 . ILE B 1 32  ? -21.740 -39.729 25.002  1.00 48.85  ? 32  ILE B CG2 1 
ATOM   2225 C  CD1 . ILE B 1 32  ? -24.155 -38.594 23.481  1.00 52.28  ? 32  ILE B CD1 1 
ATOM   2226 N  N   . PRO B 1 33  ? -21.465 -40.829 28.471  1.00 53.10  ? 33  PRO B N   1 
ATOM   2227 C  CA  . PRO B 1 33  ? -20.377 -40.675 29.427  1.00 51.78  ? 33  PRO B CA  1 
ATOM   2228 C  C   . PRO B 1 33  ? -19.166 -40.058 28.726  1.00 48.19  ? 33  PRO B C   1 
ATOM   2229 O  O   . PRO B 1 33  ? -18.910 -40.433 27.607  1.00 47.72  ? 33  PRO B O   1 
ATOM   2230 C  CB  . PRO B 1 33  ? -20.035 -42.098 29.896  1.00 56.71  ? 33  PRO B CB  1 
ATOM   2231 C  CG  . PRO B 1 33  ? -20.977 -43.035 29.145  1.00 59.21  ? 33  PRO B CG  1 
ATOM   2232 C  CD  . PRO B 1 33  ? -21.675 -42.226 28.071  1.00 57.56  ? 33  PRO B CD  1 
ATOM   2233 N  N   . PHE B 1 34  ? -18.460 -39.148 29.392  1.00 48.09  ? 34  PHE B N   1 
ATOM   2234 C  CA  . PHE B 1 34  ? -17.260 -38.476 28.833  1.00 52.15  ? 34  PHE B CA  1 
ATOM   2235 C  C   . PHE B 1 34  ? -16.380 -37.913 29.951  1.00 52.84  ? 34  PHE B C   1 
ATOM   2236 O  O   . PHE B 1 34  ? -16.773 -37.938 31.119  1.00 53.14  ? 34  PHE B O   1 
ATOM   2237 C  CB  . PHE B 1 34  ? -17.676 -37.341 27.895  1.00 51.70  ? 34  PHE B CB  1 
ATOM   2238 C  CG  . PHE B 1 34  ? -18.067 -36.078 28.619  1.00 51.28  ? 34  PHE B CG  1 
ATOM   2239 C  CD1 . PHE B 1 34  ? -19.365 -35.892 29.070  1.00 50.76  ? 34  PHE B CD1 1 
ATOM   2240 C  CD2 . PHE B 1 34  ? -17.127 -35.089 28.873  1.00 50.67  ? 34  PHE B CD2 1 
ATOM   2241 C  CE1 . PHE B 1 34  ? -19.719 -34.732 29.742  1.00 50.79  ? 34  PHE B CE1 1 
ATOM   2242 C  CE2 . PHE B 1 34  ? -17.478 -33.939 29.559  1.00 50.77  ? 34  PHE B CE2 1 
ATOM   2243 C  CZ  . PHE B 1 34  ? -18.773 -33.760 29.987  1.00 51.05  ? 34  PHE B CZ  1 
ATOM   2244 N  N   . GLU B 1 35  ? -15.221 -37.384 29.563  1.00 56.94  ? 35  GLU B N   1 
ATOM   2245 C  CA  . GLU B 1 35  ? -14.298 -36.607 30.425  1.00 61.47  ? 35  GLU B CA  1 
ATOM   2246 C  C   . GLU B 1 35  ? -13.778 -35.427 29.604  1.00 59.36  ? 35  GLU B C   1 
ATOM   2247 O  O   . GLU B 1 35  ? -13.666 -35.575 28.382  1.00 58.37  ? 35  GLU B O   1 
ATOM   2248 C  CB  . GLU B 1 35  ? -13.139 -37.493 30.876  1.00 66.16  ? 35  GLU B CB  1 
ATOM   2249 C  CG  . GLU B 1 35  ? -12.207 -36.836 31.876  1.00 69.99  ? 35  GLU B CG  1 
ATOM   2250 C  CD  . GLU B 1 35  ? -12.369 -37.344 33.293  1.00 73.71  ? 35  GLU B CD  1 
ATOM   2251 O  OE1 . GLU B 1 35  ? -12.310 -38.582 33.477  1.00 75.46  ? 35  GLU B OE1 1 
ATOM   2252 O  OE2 . GLU B 1 35  ? -12.558 -36.503 34.202  1.00 78.21  ? 35  GLU B OE2 1 
ATOM   2253 N  N   . PHE B 1 36  ? -13.478 -34.302 30.250  1.00 58.85  ? 36  PHE B N   1 
ATOM   2254 C  CA  . PHE B 1 36  ? -12.750 -33.165 29.632  1.00 57.35  ? 36  PHE B CA  1 
ATOM   2255 C  C   . PHE B 1 36  ? -11.266 -33.522 29.541  1.00 58.82  ? 36  PHE B C   1 
ATOM   2256 O  O   . PHE B 1 36  ? -10.870 -34.600 30.017  1.00 59.56  ? 36  PHE B O   1 
ATOM   2257 C  CB  . PHE B 1 36  ? -12.964 -31.873 30.423  1.00 56.89  ? 36  PHE B CB  1 
ATOM   2258 C  CG  . PHE B 1 36  ? -14.272 -31.189 30.126  1.00 57.22  ? 36  PHE B CG  1 
ATOM   2259 C  CD1 . PHE B 1 36  ? -14.471 -30.552 28.912  1.00 58.90  ? 36  PHE B CD1 1 
ATOM   2260 C  CD2 . PHE B 1 36  ? -15.305 -31.189 31.050  1.00 56.39  ? 36  PHE B CD2 1 
ATOM   2261 C  CE1 . PHE B 1 36  ? -15.679 -29.936 28.626  1.00 58.88  ? 36  PHE B CE1 1 
ATOM   2262 C  CE2 . PHE B 1 36  ? -16.511 -30.567 30.767  1.00 56.39  ? 36  PHE B CE2 1 
ATOM   2263 C  CZ  . PHE B 1 36  ? -16.696 -29.942 29.555  1.00 58.47  ? 36  PHE B CZ  1 
ATOM   2264 N  N   . PHE B 1 37  ? -10.484 -32.638 28.923  1.00 60.46  ? 37  PHE B N   1 
ATOM   2265 C  CA  . PHE B 1 37  ? -9.000  -32.671 28.901  1.00 62.00  ? 37  PHE B CA  1 
ATOM   2266 C  C   . PHE B 1 37  ? -8.497  -31.229 28.799  1.00 66.57  ? 37  PHE B C   1 
ATOM   2267 O  O   . PHE B 1 37  ? -8.899  -30.535 27.854  1.00 74.25  ? 37  PHE B O   1 
ATOM   2268 C  CB  . PHE B 1 37  ? -8.509  -33.543 27.745  1.00 58.47  ? 37  PHE B CB  1 
ATOM   2269 C  CG  . PHE B 1 37  ? -7.020  -33.504 27.505  1.00 59.51  ? 37  PHE B CG  1 
ATOM   2270 C  CD1 . PHE B 1 37  ? -6.166  -34.351 28.186  1.00 61.28  ? 37  PHE B CD1 1 
ATOM   2271 C  CD2 . PHE B 1 37  ? -6.473  -32.618 26.589  1.00 61.39  ? 37  PHE B CD2 1 
ATOM   2272 C  CE1 . PHE B 1 37  ? -4.797  -34.316 27.957  1.00 63.87  ? 37  PHE B CE1 1 
ATOM   2273 C  CE2 . PHE B 1 37  ? -5.107  -32.582 26.362  1.00 61.48  ? 37  PHE B CE2 1 
ATOM   2274 C  CZ  . PHE B 1 37  ? -4.269  -33.432 27.045  1.00 63.58  ? 37  PHE B CZ  1 
ATOM   2275 N  N   . ASP B 1 38  ? -7.659  -30.793 29.742  1.00 70.92  ? 38  ASP B N   1 
ATOM   2276 C  CA  . ASP B 1 38  ? -7.099  -29.416 29.776  1.00 71.65  ? 38  ASP B CA  1 
ATOM   2277 C  C   . ASP B 1 38  ? -6.239  -29.207 28.524  1.00 71.01  ? 38  ASP B C   1 
ATOM   2278 O  O   . ASP B 1 38  ? -5.165  -29.826 28.431  1.00 70.02  ? 38  ASP B O   1 
ATOM   2279 C  CB  . ASP B 1 38  ? -6.309  -29.168 31.063  1.00 71.57  ? 38  ASP B CB  1 
ATOM   2280 C  CG  . ASP B 1 38  ? -7.144  -29.287 32.323  1.00 69.11  ? 38  ASP B CG  1 
ATOM   2281 O  OD1 . ASP B 1 38  ? -8.387  -29.391 32.209  1.00 66.64  ? 38  ASP B OD1 1 
ATOM   2282 O  OD2 . ASP B 1 38  ? -6.541  -29.277 33.407  1.00 74.09  ? 38  ASP B OD2 1 
ATOM   2283 N  N   . ALA B 1 39  ? -6.716  -28.376 27.596  1.00 71.92  ? 39  ALA B N   1 
ATOM   2284 C  CA  . ALA B 1 39  ? -6.039  -28.056 26.322  1.00 74.81  ? 39  ALA B CA  1 
ATOM   2285 C  C   . ALA B 1 39  ? -4.804  -27.208 26.623  1.00 75.59  ? 39  ALA B C   1 
ATOM   2286 O  O   . ALA B 1 39  ? -4.938  -26.214 27.352  1.00 77.12  ? 39  ALA B O   1 
ATOM   2287 C  CB  . ALA B 1 39  ? -6.980  -27.338 25.388  1.00 77.49  ? 39  ALA B CB  1 
ATOM   2288 N  N   . PHE B 1 40  ? -3.654  -27.594 26.073  1.00 80.59  ? 40  PHE B N   1 
ATOM   2289 C  CA  . PHE B 1 40  ? -2.368  -26.857 26.183  1.00 88.46  ? 40  PHE B CA  1 
ATOM   2290 C  C   . PHE B 1 40  ? -2.539  -25.440 25.628  1.00 91.23  ? 40  PHE B C   1 
ATOM   2291 O  O   . PHE B 1 40  ? -3.074  -25.300 24.509  1.00 93.04  ? 40  PHE B O   1 
ATOM   2292 C  CB  . PHE B 1 40  ? -1.251  -27.579 25.424  1.00 94.30  ? 40  PHE B CB  1 
ATOM   2293 C  CG  . PHE B 1 40  ? -0.860  -28.914 26.004  1.00 99.60  ? 40  PHE B CG  1 
ATOM   2294 C  CD1 . PHE B 1 40  ? 0.038   -28.992 27.059  1.00 105.41 ? 40  PHE B CD1 1 
ATOM   2295 C  CD2 . PHE B 1 40  ? -1.388  -30.090 25.495  1.00 101.86 ? 40  PHE B CD2 1 
ATOM   2296 C  CE1 . PHE B 1 40  ? 0.388   -30.219 27.600  1.00 108.66 ? 40  PHE B CE1 1 
ATOM   2297 C  CE2 . PHE B 1 40  ? -1.039  -31.314 26.040  1.00 106.23 ? 40  PHE B CE2 1 
ATOM   2298 C  CZ  . PHE B 1 40  ? -0.146  -31.377 27.087  1.00 108.80 ? 40  PHE B CZ  1 
ATOM   2299 N  N   . THR B 1 41  ? -2.092  -24.436 26.392  1.00 95.72  ? 41  THR B N   1 
ATOM   2300 C  CA  . THR B 1 41  ? -2.097  -22.995 26.022  1.00 98.64  ? 41  THR B CA  1 
ATOM   2301 C  C   . THR B 1 41  ? -0.659  -22.481 26.031  1.00 105.85 ? 41  THR B C   1 
ATOM   2302 O  O   . THR B 1 41  ? 0.184   -23.033 26.738  1.00 106.97 ? 41  THR B O   1 
ATOM   2303 C  CB  . THR B 1 41  ? -3.000  -22.183 26.962  1.00 97.04  ? 41  THR B CB  1 
ATOM   2304 O  OG1 . THR B 1 41  ? -2.340  -21.975 28.210  1.00 93.98  ? 41  THR B OG1 1 
ATOM   2305 C  CG2 . THR B 1 41  ? -4.332  -22.849 27.225  1.00 96.91  ? 41  THR B CG2 1 
ATOM   2306 N  N   . PRO B 1 42  ? -0.326  -21.434 25.236  1.00 115.21 ? 42  PRO B N   1 
ATOM   2307 C  CA  . PRO B 1 42  ? 0.985   -20.793 25.315  1.00 120.46 ? 42  PRO B CA  1 
ATOM   2308 C  C   . PRO B 1 42  ? 1.369   -20.551 26.783  1.00 123.45 ? 42  PRO B C   1 
ATOM   2309 O  O   . PRO B 1 42  ? 0.826   -19.650 27.399  1.00 126.55 ? 42  PRO B O   1 
ATOM   2310 C  CB  . PRO B 1 42  ? 0.850   -19.476 24.528  1.00 122.72 ? 42  PRO B CB  1 
ATOM   2311 C  CG  . PRO B 1 42  ? -0.554  -19.477 23.919  1.00 122.95 ? 42  PRO B CG  1 
ATOM   2312 C  CD  . PRO B 1 42  ? -1.173  -20.833 24.197  1.00 120.68 ? 42  PRO B CD  1 
ATOM   2313 N  N   . SER B 1 43  ? 2.259   -21.392 27.314  1.00 123.04 ? 43  SER B N   1 
ATOM   2314 C  CA  . SER B 1 43  ? 2.671   -21.396 28.741  1.00 121.03 ? 43  SER B CA  1 
ATOM   2315 C  C   . SER B 1 43  ? 3.950   -22.219 28.912  1.00 124.24 ? 43  SER B C   1 
ATOM   2316 O  O   . SER B 1 43  ? 4.371   -22.886 27.935  1.00 125.39 ? 43  SER B O   1 
ATOM   2317 C  CB  . SER B 1 43  ? 1.566   -21.924 29.619  1.00 116.40 ? 43  SER B CB  1 
ATOM   2318 O  OG  . SER B 1 43  ? 1.312   -23.292 29.340  1.00 113.81 ? 43  SER B OG  1 
ATOM   2319 N  N   . ASP B 1 44  ? 4.520   -22.178 30.119  1.00 122.46 ? 44  ASP B N   1 
ATOM   2320 C  CA  . ASP B 1 44  ? 5.657   -23.032 30.550  1.00 117.89 ? 44  ASP B CA  1 
ATOM   2321 C  C   . ASP B 1 44  ? 5.298   -24.490 30.237  1.00 114.22 ? 44  ASP B C   1 
ATOM   2322 O  O   . ASP B 1 44  ? 5.991   -25.081 29.391  1.00 108.92 ? 44  ASP B O   1 
ATOM   2323 C  CB  . ASP B 1 44  ? 6.000   -22.795 32.026  1.00 120.27 ? 44  ASP B CB  1 
ATOM   2324 C  CG  . ASP B 1 44  ? 6.658   -21.450 32.305  1.00 118.78 ? 44  ASP B CG  1 
ATOM   2325 O  OD1 . ASP B 1 44  ? 6.138   -20.423 31.822  1.00 112.99 ? 44  ASP B OD1 1 
ATOM   2326 O  OD2 . ASP B 1 44  ? 7.689   -21.438 33.007  1.00 114.67 ? 44  ASP B OD2 1 
ATOM   2327 N  N   . LYS B 1 45  ? 4.224   -25.013 30.848  1.00 110.59 ? 45  LYS B N   1 
ATOM   2328 C  CA  . LYS B 1 45  ? 3.768   -26.433 30.771  1.00 108.72 ? 45  LYS B CA  1 
ATOM   2329 C  C   . LYS B 1 45  ? 3.682   -26.910 29.311  1.00 105.51 ? 45  LYS B C   1 
ATOM   2330 O  O   . LYS B 1 45  ? 4.018   -28.084 29.059  1.00 102.52 ? 45  LYS B O   1 
ATOM   2331 C  CB  . LYS B 1 45  ? 2.413   -26.585 31.480  1.00 107.00 ? 45  LYS B CB  1 
ATOM   2332 C  CG  . LYS B 1 45  ? 1.670   -27.897 31.242  1.00 106.88 ? 45  LYS B CG  1 
ATOM   2333 C  CD  . LYS B 1 45  ? 1.175   -28.574 32.506  1.00 109.23 ? 45  LYS B CD  1 
ATOM   2334 C  CE  . LYS B 1 45  ? 0.838   -30.039 32.312  1.00 108.75 ? 45  LYS B CE  1 
ATOM   2335 N  NZ  . LYS B 1 45  ? 0.960   -30.813 33.573  1.00 110.58 ? 45  LYS B NZ  1 
ATOM   2336 N  N   . LEU B 1 46  ? 3.230   -26.055 28.389  1.00 103.30 ? 46  LEU B N   1 
ATOM   2337 C  CA  . LEU B 1 46  ? 3.162   -26.382 26.936  1.00 101.43 ? 46  LEU B CA  1 
ATOM   2338 C  C   . LEU B 1 46  ? 4.590   -26.525 26.404  1.00 98.61  ? 46  LEU B C   1 
ATOM   2339 O  O   . LEU B 1 46  ? 4.989   -27.659 26.065  1.00 93.69  ? 46  LEU B O   1 
ATOM   2340 C  CB  . LEU B 1 46  ? 2.394   -25.290 26.179  1.00 100.71 ? 46  LEU B CB  1 
ATOM   2341 C  CG  . LEU B 1 46  ? 2.583   -25.257 24.658  1.00 98.03  ? 46  LEU B CG  1 
ATOM   2342 C  CD1 . LEU B 1 46  ? 2.343   -26.625 24.025  1.00 93.43  ? 46  LEU B CD1 1 
ATOM   2343 C  CD2 . LEU B 1 46  ? 1.669   -24.209 24.034  1.00 94.86  ? 46  LEU B CD2 1 
ATOM   2344 N  N   . THR B 1 47  ? 5.318   -25.408 26.349  1.00 96.98  ? 47  THR B N   1 
ATOM   2345 C  CA  . THR B 1 47  ? 6.701   -25.303 25.814  1.00 95.68  ? 47  THR B CA  1 
ATOM   2346 C  C   . THR B 1 47  ? 7.544   -26.449 26.392  1.00 100.59 ? 47  THR B C   1 
ATOM   2347 O  O   . THR B 1 47  ? 8.335   -27.033 25.625  1.00 100.07 ? 47  THR B O   1 
ATOM   2348 C  CB  . THR B 1 47  ? 7.249   -23.892 26.062  1.00 91.58  ? 47  THR B CB  1 
ATOM   2349 O  OG1 . THR B 1 47  ? 6.603   -23.360 27.222  1.00 88.46  ? 47  THR B OG1 1 
ATOM   2350 C  CG2 . THR B 1 47  ? 7.017   -22.962 24.889  1.00 90.37  ? 47  THR B CG2 1 
ATOM   2351 N  N   . ASP B 1 48  ? 7.352   -26.776 27.679  1.00 103.36 ? 48  ASP B N   1 
ATOM   2352 C  CA  . ASP B 1 48  ? 7.926   -27.979 28.346  1.00 104.24 ? 48  ASP B CA  1 
ATOM   2353 C  C   . ASP B 1 48  ? 7.759   -29.187 27.420  1.00 98.34  ? 48  ASP B C   1 
ATOM   2354 O  O   . ASP B 1 48  ? 8.760   -29.640 26.842  1.00 88.39  ? 48  ASP B O   1 
ATOM   2355 C  CB  . ASP B 1 48  ? 7.229   -28.311 29.675  1.00 112.24 ? 48  ASP B CB  1 
ATOM   2356 C  CG  . ASP B 1 48  ? 7.563   -27.422 30.859  1.00 117.98 ? 48  ASP B CG  1 
ATOM   2357 O  OD1 . ASP B 1 48  ? 8.186   -26.358 30.647  1.00 122.28 ? 48  ASP B OD1 1 
ATOM   2358 O  OD2 . ASP B 1 48  ? 7.170   -27.795 31.989  1.00 117.04 ? 48  ASP B OD2 1 
ATOM   2359 N  N   . HIS B 1 49  ? 6.515   -29.654 27.280  1.00 96.13  ? 49  HIS B N   1 
ATOM   2360 C  CA  . HIS B 1 49  ? 6.137   -30.920 26.601  1.00 95.22  ? 49  HIS B CA  1 
ATOM   2361 C  C   . HIS B 1 49  ? 6.571   -30.866 25.135  1.00 93.08  ? 49  HIS B C   1 
ATOM   2362 O  O   . HIS B 1 49  ? 6.898   -31.934 24.595  1.00 86.36  ? 49  HIS B O   1 
ATOM   2363 C  CB  . HIS B 1 49  ? 4.635   -31.193 26.770  1.00 94.75  ? 49  HIS B CB  1 
ATOM   2364 C  CG  . HIS B 1 49  ? 4.239   -31.539 28.168  1.00 91.01  ? 49  HIS B CG  1 
ATOM   2365 N  ND1 . HIS B 1 49  ? 4.251   -30.608 29.185  1.00 93.95  ? 49  HIS B ND1 1 
ATOM   2366 C  CD2 . HIS B 1 49  ? 3.798   -32.694 28.716  1.00 91.51  ? 49  HIS B CD2 1 
ATOM   2367 C  CE1 . HIS B 1 49  ? 3.851   -31.175 30.304  1.00 97.26  ? 49  HIS B CE1 1 
ATOM   2368 N  NE2 . HIS B 1 49  ? 3.563   -32.456 30.044  1.00 96.81  ? 49  HIS B NE2 1 
ATOM   2369 N  N   . LEU B 1 50  ? 6.590   -29.673 24.529  1.00 96.98  ? 50  LEU B N   1 
ATOM   2370 C  CA  . LEU B 1 50  ? 6.993   -29.461 23.110  1.00 106.83 ? 50  LEU B CA  1 
ATOM   2371 C  C   . LEU B 1 50  ? 8.379   -30.071 22.872  1.00 108.04 ? 50  LEU B C   1 
ATOM   2372 O  O   . LEU B 1 50  ? 8.443   -31.132 22.220  1.00 98.94  ? 50  LEU B O   1 
ATOM   2373 C  CB  . LEU B 1 50  ? 6.955   -27.968 22.763  1.00 112.21 ? 50  LEU B CB  1 
ATOM   2374 C  CG  . LEU B 1 50  ? 5.619   -27.453 22.220  1.00 116.52 ? 50  LEU B CG  1 
ATOM   2375 C  CD1 . LEU B 1 50  ? 5.602   -25.934 22.129  1.00 118.81 ? 50  LEU B CD1 1 
ATOM   2376 C  CD2 . LEU B 1 50  ? 5.318   -28.057 20.860  1.00 116.66 ? 50  LEU B CD2 1 
ATOM   2377 N  N   . GLN B 1 51  ? 9.433   -29.454 23.416  1.00 117.92 ? 51  GLN B N   1 
ATOM   2378 C  CA  . GLN B 1 51  ? 10.843  -29.906 23.244  1.00 121.85 ? 51  GLN B CA  1 
ATOM   2379 C  C   . GLN B 1 51  ? 11.054  -31.270 23.909  1.00 119.17 ? 51  GLN B C   1 
ATOM   2380 O  O   . GLN B 1 51  ? 12.011  -31.959 23.515  1.00 115.90 ? 51  GLN B O   1 
ATOM   2381 C  CB  . GLN B 1 51  ? 11.828  -28.882 23.809  1.00 124.73 ? 51  GLN B CB  1 
ATOM   2382 C  CG  . GLN B 1 51  ? 12.304  -27.875 22.771  1.00 130.51 ? 51  GLN B CG  1 
ATOM   2383 C  CD  . GLN B 1 51  ? 11.962  -26.457 23.149  1.00 135.31 ? 51  GLN B CD  1 
ATOM   2384 O  OE1 . GLN B 1 51  ? 10.895  -26.181 23.697  1.00 139.60 ? 51  GLN B OE1 1 
ATOM   2385 N  NE2 . GLN B 1 51  ? 12.866  -25.543 22.837  1.00 135.42 ? 51  GLN B NE2 1 
ATOM   2386 N  N   . ARG B 1 52  ? 10.221  -31.630 24.888  1.00 118.69 ? 52  ARG B N   1 
ATOM   2387 C  CA  . ARG B 1 52  ? 10.251  -32.977 25.516  1.00 116.75 ? 52  ARG B CA  1 
ATOM   2388 C  C   . ARG B 1 52  ? 9.900   -34.028 24.454  1.00 115.77 ? 52  ARG B C   1 
ATOM   2389 O  O   . ARG B 1 52  ? 10.749  -34.901 24.207  1.00 114.17 ? 52  ARG B O   1 
ATOM   2390 C  CB  . ARG B 1 52  ? 9.319   -33.067 26.729  1.00 116.43 ? 52  ARG B CB  1 
ATOM   2391 C  CG  . ARG B 1 52  ? 8.799   -34.471 26.990  1.00 119.14 ? 52  ARG B CG  1 
ATOM   2392 C  CD  . ARG B 1 52  ? 8.796   -34.868 28.453  1.00 119.05 ? 52  ARG B CD  1 
ATOM   2393 N  NE  . ARG B 1 52  ? 8.626   -36.313 28.564  1.00 120.19 ? 52  ARG B NE  1 
ATOM   2394 C  CZ  . ARG B 1 52  ? 8.718   -37.021 29.683  1.00 117.29 ? 52  ARG B CZ  1 
ATOM   2395 N  NH1 . ARG B 1 52  ? 9.013   -36.429 30.830  1.00 118.08 ? 52  ARG B NH1 1 
ATOM   2396 N  NH2 . ARG B 1 52  ? 8.536   -38.331 29.648  1.00 113.75 ? 52  ARG B NH2 1 
ATOM   2397 N  N   . TYR B 1 53  ? 8.710   -33.941 23.847  1.00 111.89 ? 53  TYR B N   1 
ATOM   2398 C  CA  . TYR B 1 53  ? 8.135   -34.993 22.963  1.00 106.06 ? 53  TYR B CA  1 
ATOM   2399 C  C   . TYR B 1 53  ? 8.384   -34.668 21.481  1.00 102.48 ? 53  TYR B C   1 
ATOM   2400 O  O   . TYR B 1 53  ? 8.702   -35.600 20.716  1.00 93.96  ? 53  TYR B O   1 
ATOM   2401 C  CB  . TYR B 1 53  ? 6.640   -35.170 23.235  1.00 105.13 ? 53  TYR B CB  1 
ATOM   2402 C  CG  . TYR B 1 53  ? 6.303   -35.804 24.562  1.00 103.25 ? 53  TYR B CG  1 
ATOM   2403 C  CD1 . TYR B 1 53  ? 6.526   -37.151 24.797  1.00 101.71 ? 53  TYR B CD1 1 
ATOM   2404 C  CD2 . TYR B 1 53  ? 5.733   -35.056 25.581  1.00 101.98 ? 53  TYR B CD2 1 
ATOM   2405 C  CE1 . TYR B 1 53  ? 6.211   -37.732 26.018  1.00 101.97 ? 53  TYR B CE1 1 
ATOM   2406 C  CE2 . TYR B 1 53  ? 5.412   -35.619 26.805  1.00 101.85 ? 53  TYR B CE2 1 
ATOM   2407 C  CZ  . TYR B 1 53  ? 5.645   -36.966 27.024  1.00 102.16 ? 53  TYR B CZ  1 
ATOM   2408 O  OH  . TYR B 1 53  ? 5.330   -37.521 28.231  1.00 98.30  ? 53  TYR B OH  1 
ATOM   2409 N  N   . LEU B 1 54  ? 8.216   -33.406 21.078  1.00 105.18 ? 54  LEU B N   1 
ATOM   2410 C  CA  . LEU B 1 54  ? 8.313   -32.964 19.659  1.00 110.91 ? 54  LEU B CA  1 
ATOM   2411 C  C   . LEU B 1 54  ? 9.161   -31.700 19.573  1.00 113.34 ? 54  LEU B C   1 
ATOM   2412 O  O   . LEU B 1 54  ? 8.634   -30.589 19.584  1.00 109.01 ? 54  LEU B O   1 
ATOM   2413 C  CB  . LEU B 1 54  ? 6.904   -32.733 19.108  1.00 112.23 ? 54  LEU B CB  1 
ATOM   2414 C  CG  . LEU B 1 54  ? 6.090   -34.004 18.874  1.00 112.47 ? 54  LEU B CG  1 
ATOM   2415 C  CD1 . LEU B 1 54  ? 4.615   -33.672 18.747  1.00 112.92 ? 54  LEU B CD1 1 
ATOM   2416 C  CD2 . LEU B 1 54  ? 6.574   -34.754 17.640  1.00 110.10 ? 54  LEU B CD2 1 
ATOM   2417 N  N   . PRO B 1 55  ? 10.503  -31.842 19.505  1.00 121.24 ? 55  PRO B N   1 
ATOM   2418 C  CA  . PRO B 1 55  ? 11.397  -30.686 19.408  1.00 125.96 ? 55  PRO B CA  1 
ATOM   2419 C  C   . PRO B 1 55  ? 11.179  -29.907 18.100  1.00 125.62 ? 55  PRO B C   1 
ATOM   2420 O  O   . PRO B 1 55  ? 10.832  -28.745 18.163  1.00 120.13 ? 55  PRO B O   1 
ATOM   2421 C  CB  . PRO B 1 55  ? 12.810  -31.294 19.492  1.00 127.66 ? 55  PRO B CB  1 
ATOM   2422 C  CG  . PRO B 1 55  ? 12.637  -32.762 19.130  1.00 125.03 ? 55  PRO B CG  1 
ATOM   2423 C  CD  . PRO B 1 55  ? 11.223  -33.125 19.535  1.00 122.46 ? 55  PRO B CD  1 
ATOM   2424 N  N   . ASN B 1 56  ? 11.390  -30.582 16.966  1.00 127.28 ? 56  ASN B N   1 
ATOM   2425 C  CA  . ASN B 1 56  ? 11.058  -30.155 15.577  1.00 129.13 ? 56  ASN B CA  1 
ATOM   2426 C  C   . ASN B 1 56  ? 9.976   -29.064 15.556  1.00 128.02 ? 56  ASN B C   1 
ATOM   2427 O  O   . ASN B 1 56  ? 10.114  -28.104 14.767  1.00 124.99 ? 56  ASN B O   1 
ATOM   2428 C  CB  . ASN B 1 56  ? 10.602  -31.364 14.759  1.00 132.83 ? 56  ASN B CB  1 
ATOM   2429 C  CG  . ASN B 1 56  ? 9.718   -32.327 15.530  1.00 138.72 ? 56  ASN B CG  1 
ATOM   2430 O  OD1 . ASN B 1 56  ? 10.055  -32.744 16.635  1.00 139.39 ? 56  ASN B OD1 1 
ATOM   2431 N  ND2 . ASN B 1 56  ? 8.594   -32.709 14.945  1.00 139.81 ? 56  ASN B ND2 1 
ATOM   2432 N  N   . VAL B 1 57  ? 8.928   -29.232 16.368  1.00 126.57 ? 57  VAL B N   1 
ATOM   2433 C  CA  . VAL B 1 57  ? 7.719   -28.355 16.413  1.00 125.47 ? 57  VAL B CA  1 
ATOM   2434 C  C   . VAL B 1 57  ? 8.059   -27.046 17.139  1.00 124.35 ? 57  VAL B C   1 
ATOM   2435 O  O   . VAL B 1 57  ? 7.717   -25.974 16.605  1.00 129.14 ? 57  VAL B O   1 
ATOM   2436 C  CB  . VAL B 1 57  ? 6.539   -29.078 17.088  1.00 125.13 ? 57  VAL B CB  1 
ATOM   2437 C  CG1 . VAL B 1 57  ? 5.330   -28.162 17.227  1.00 127.62 ? 57  VAL B CG1 1 
ATOM   2438 C  CG2 . VAL B 1 57  ? 6.162   -30.357 16.355  1.00 119.86 ? 57  VAL B CG2 1 
ATOM   2439 N  N   . ALA B 1 58  ? 8.681   -27.134 18.319  1.00 116.19 ? 58  ALA B N   1 
ATOM   2440 C  CA  . ALA B 1 58  ? 9.091   -25.979 19.156  1.00 111.22 ? 58  ALA B CA  1 
ATOM   2441 C  C   . ALA B 1 58  ? 9.792   -24.926 18.287  1.00 108.42 ? 58  ALA B C   1 
ATOM   2442 O  O   . ALA B 1 58  ? 9.470   -23.731 18.444  1.00 102.88 ? 58  ALA B O   1 
ATOM   2443 C  CB  . ALA B 1 58  ? 9.980   -26.445 20.284  1.00 110.23 ? 58  ALA B CB  1 
ATOM   2444 N  N   . ASN B 1 59  ? 10.698  -25.368 17.402  1.00 110.02 ? 59  ASN B N   1 
ATOM   2445 C  CA  . ASN B 1 59  ? 11.470  -24.515 16.453  1.00 112.41 ? 59  ASN B CA  1 
ATOM   2446 C  C   . ASN B 1 59  ? 10.503  -23.865 15.455  1.00 114.43 ? 59  ASN B C   1 
ATOM   2447 O  O   . ASN B 1 59  ? 10.502  -22.621 15.355  1.00 118.90 ? 59  ASN B O   1 
ATOM   2448 C  CB  . ASN B 1 59  ? 12.537  -25.288 15.666  1.00 111.04 ? 59  ASN B CB  1 
ATOM   2449 C  CG  . ASN B 1 59  ? 13.128  -26.466 16.410  1.00 111.80 ? 59  ASN B CG  1 
ATOM   2450 O  OD1 . ASN B 1 59  ? 13.153  -27.577 15.886  1.00 115.20 ? 59  ASN B OD1 1 
ATOM   2451 N  ND2 . ASN B 1 59  ? 13.598  -26.241 17.626  1.00 109.67 ? 59  ASN B ND2 1 
ATOM   2452 N  N   . ALA B 1 60  ? 9.719   -24.694 14.757  1.00 112.74 ? 60  ALA B N   1 
ATOM   2453 C  CA  . ALA B 1 60  ? 8.750   -24.306 13.706  1.00 109.87 ? 60  ALA B CA  1 
ATOM   2454 C  C   . ALA B 1 60  ? 7.936   -23.087 14.156  1.00 110.26 ? 60  ALA B C   1 
ATOM   2455 O  O   . ALA B 1 60  ? 7.100   -23.230 15.070  1.00 104.23 ? 60  ALA B O   1 
ATOM   2456 C  CB  . ALA B 1 60  ? 7.850   -25.473 13.386  1.00 108.77 ? 60  ALA B CB  1 
ATOM   2457 N  N   . ALA B 1 61  ? 8.190   -21.927 13.541  1.00 111.35 ? 61  ALA B N   1 
ATOM   2458 C  CA  . ALA B 1 61  ? 7.415   -20.676 13.717  1.00 107.87 ? 61  ALA B CA  1 
ATOM   2459 C  C   . ALA B 1 61  ? 6.391   -20.552 12.580  1.00 104.81 ? 61  ALA B C   1 
ATOM   2460 O  O   . ALA B 1 61  ? 5.637   -19.555 12.577  1.00 100.14 ? 61  ALA B O   1 
ATOM   2461 C  CB  . ALA B 1 61  ? 8.339   -19.483 13.770  1.00 106.63 ? 61  ALA B CB  1 
ATOM   2462 N  N   . GLN B 1 62  ? 6.357   -21.528 11.659  1.00 99.03  ? 62  GLN B N   1 
ATOM   2463 C  CA  . GLN B 1 62  ? 5.328   -21.620 10.585  1.00 97.29  ? 62  GLN B CA  1 
ATOM   2464 C  C   . GLN B 1 62  ? 3.985   -22.055 11.192  1.00 98.67  ? 62  GLN B C   1 
ATOM   2465 O  O   . GLN B 1 62  ? 3.005   -22.128 10.421  1.00 94.97  ? 62  GLN B O   1 
ATOM   2466 C  CB  . GLN B 1 62  ? 5.767   -22.556 9.453   1.00 94.32  ? 62  GLN B CB  1 
ATOM   2467 C  CG  . GLN B 1 62  ? 5.772   -24.037 9.810   1.00 96.24  ? 62  GLN B CG  1 
ATOM   2468 C  CD  . GLN B 1 62  ? 7.166   -24.603 9.917   1.00 101.30 ? 62  GLN B CD  1 
ATOM   2469 O  OE1 . GLN B 1 62  ? 8.047   -24.010 10.540  1.00 106.91 ? 62  GLN B OE1 1 
ATOM   2470 N  NE2 . GLN B 1 62  ? 7.369   -25.766 9.319   1.00 99.85  ? 62  GLN B NE2 1 
ATOM   2471 N  N   . LEU B 1 63  ? 3.946   -22.332 12.505  1.00 96.88  ? 63  LEU B N   1 
ATOM   2472 C  CA  . LEU B 1 63  ? 2.705   -22.565 13.294  1.00 90.28  ? 63  LEU B CA  1 
ATOM   2473 C  C   . LEU B 1 63  ? 2.593   -21.521 14.403  1.00 88.16  ? 63  LEU B C   1 
ATOM   2474 O  O   . LEU B 1 63  ? 3.617   -21.259 15.071  1.00 89.76  ? 63  LEU B O   1 
ATOM   2475 C  CB  . LEU B 1 63  ? 2.751   -23.966 13.906  1.00 88.89  ? 63  LEU B CB  1 
ATOM   2476 C  CG  . LEU B 1 63  ? 2.998   -25.104 12.919  1.00 90.06  ? 63  LEU B CG  1 
ATOM   2477 C  CD1 . LEU B 1 63  ? 3.143   -26.427 13.653  1.00 89.95  ? 63  LEU B CD1 1 
ATOM   2478 C  CD2 . LEU B 1 63  ? 1.885   -25.179 11.884  1.00 89.91  ? 63  LEU B CD2 1 
ATOM   2479 N  N   . THR B 1 64  ? 1.391   -20.972 14.597  1.00 87.87  ? 64  THR B N   1 
ATOM   2480 C  CA  . THR B 1 64  ? 1.017   -20.212 15.818  1.00 92.53  ? 64  THR B CA  1 
ATOM   2481 C  C   . THR B 1 64  ? 1.113   -21.169 17.008  1.00 90.82  ? 64  THR B C   1 
ATOM   2482 O  O   . THR B 1 64  ? 0.994   -22.391 16.785  1.00 92.13  ? 64  THR B O   1 
ATOM   2483 C  CB  . THR B 1 64  ? -0.375  -19.563 15.713  1.00 95.98  ? 64  THR B CB  1 
ATOM   2484 O  OG1 . THR B 1 64  ? -0.717  -19.020 16.991  1.00 95.99  ? 64  THR B OG1 1 
ATOM   2485 C  CG2 . THR B 1 64  ? -1.472  -20.512 15.281  1.00 93.27  ? 64  THR B CG2 1 
HETATM 2486 N  N   . MSE B 1 65  ? 1.334   -20.634 18.210  1.00 90.02  ? 65  MSE B N   1 
HETATM 2487 C  CA  . MSE B 1 65  ? 1.354   -21.424 19.469  1.00 88.72  ? 65  MSE B CA  1 
HETATM 2488 C  C   . MSE B 1 65  ? -0.013  -22.090 19.658  1.00 88.92  ? 65  MSE B C   1 
HETATM 2489 O  O   . MSE B 1 65  ? -0.034  -23.263 20.074  1.00 87.53  ? 65  MSE B O   1 
HETATM 2490 C  CB  . MSE B 1 65  ? 1.711   -20.536 20.665  1.00 90.09  ? 65  MSE B CB  1 
HETATM 2491 C  CG  . MSE B 1 65  ? 3.194   -20.497 20.979  1.00 93.10  ? 65  MSE B CG  1 
HETATM 2492 SE SE  . MSE B 1 65  ? 3.883   -22.203 21.701  1.00 92.63  ? 65  MSE B SE  1 
HETATM 2493 C  CE  . MSE B 1 65  ? 5.732   -22.446 21.068  1.00 91.42  ? 65  MSE B CE  1 
ATOM   2494 N  N   . GLY B 1 66  ? -1.099  -21.374 19.339  1.00 89.41  ? 66  GLY B N   1 
ATOM   2495 C  CA  . GLY B 1 66  ? -2.482  -21.891 19.362  1.00 88.45  ? 66  GLY B CA  1 
ATOM   2496 C  C   . GLY B 1 66  ? -2.592  -23.244 18.677  1.00 88.08  ? 66  GLY B C   1 
ATOM   2497 O  O   . GLY B 1 66  ? -3.332  -24.105 19.188  1.00 91.96  ? 66  GLY B O   1 
ATOM   2498 N  N   . GLU B 1 67  ? -1.865  -23.428 17.571  1.00 89.98  ? 67  GLU B N   1 
ATOM   2499 C  CA  . GLU B 1 67  ? -1.866  -24.668 16.747  1.00 91.87  ? 67  GLU B CA  1 
ATOM   2500 C  C   . GLU B 1 67  ? -0.910  -25.701 17.352  1.00 88.78  ? 67  GLU B C   1 
ATOM   2501 O  O   . GLU B 1 67  ? -1.190  -26.902 17.208  1.00 82.38  ? 67  GLU B O   1 
ATOM   2502 C  CB  . GLU B 1 67  ? -1.448  -24.358 15.310  1.00 95.42  ? 67  GLU B CB  1 
ATOM   2503 C  CG  . GLU B 1 67  ? -2.520  -23.660 14.499  1.00 97.12  ? 67  GLU B CG  1 
ATOM   2504 C  CD  . GLU B 1 67  ? -2.029  -23.202 13.137  1.00 100.57 ? 67  GLU B CD  1 
ATOM   2505 O  OE1 . GLU B 1 67  ? -2.789  -23.340 12.160  1.00 100.62 ? 67  GLU B OE1 1 
ATOM   2506 O  OE2 . GLU B 1 67  ? -0.885  -22.705 13.063  1.00 105.22 ? 67  GLU B OE2 1 
ATOM   2507 N  N   . LYS B 1 68  ? 0.187   -25.247 17.967  1.00 92.60  ? 68  LYS B N   1 
ATOM   2508 C  CA  . LYS B 1 68  ? 1.133   -26.103 18.735  1.00 89.62  ? 68  LYS B CA  1 
ATOM   2509 C  C   . LYS B 1 68  ? 0.373   -26.707 19.922  1.00 82.29  ? 68  LYS B C   1 
ATOM   2510 O  O   . LYS B 1 68  ? 0.440   -27.940 20.102  1.00 73.46  ? 68  LYS B O   1 
ATOM   2511 C  CB  . LYS B 1 68  ? 2.363   -25.300 19.181  1.00 91.69  ? 68  LYS B CB  1 
ATOM   2512 C  CG  . LYS B 1 68  ? 3.280   -24.843 18.051  1.00 95.99  ? 68  LYS B CG  1 
ATOM   2513 C  CD  . LYS B 1 68  ? 4.346   -23.849 18.464  1.00 96.56  ? 68  LYS B CD  1 
ATOM   2514 C  CE  . LYS B 1 68  ? 5.313   -23.519 17.346  1.00 98.21  ? 68  LYS B CE  1 
ATOM   2515 N  NZ  . LYS B 1 68  ? 6.494   -22.777 17.842  1.00 97.76  ? 68  LYS B NZ  1 
ATOM   2516 N  N   . GLY B 1 69  ? -0.352  -25.864 20.667  1.00 81.86  ? 69  GLY B N   1 
ATOM   2517 C  CA  . GLY B 1 69  ? -1.167  -26.247 21.837  1.00 83.33  ? 69  GLY B CA  1 
ATOM   2518 C  C   . GLY B 1 69  ? -2.286  -27.199 21.463  1.00 81.62  ? 69  GLY B C   1 
ATOM   2519 O  O   . GLY B 1 69  ? -2.539  -28.152 22.229  1.00 78.81  ? 69  GLY B O   1 
ATOM   2520 N  N   . CYS B 1 70  ? -2.932  -26.953 20.323  1.00 85.59  ? 70  CYS B N   1 
ATOM   2521 C  CA  . CYS B 1 70  ? -4.004  -27.817 19.765  1.00 86.88  ? 70  CYS B CA  1 
ATOM   2522 C  C   . CYS B 1 70  ? -3.416  -29.184 19.396  1.00 85.43  ? 70  CYS B C   1 
ATOM   2523 O  O   . CYS B 1 70  ? -3.956  -30.192 19.860  1.00 84.31  ? 70  CYS B O   1 
ATOM   2524 C  CB  . CYS B 1 70  ? -4.663  -27.181 18.548  1.00 89.84  ? 70  CYS B CB  1 
ATOM   2525 S  SG  . CYS B 1 70  ? -6.312  -27.856 18.219  1.00 95.00  ? 70  CYS B SG  1 
ATOM   2526 N  N   . LEU B 1 71  ? -2.342  -29.201 18.600  1.00 84.44  ? 71  LEU B N   1 
ATOM   2527 C  CA  . LEU B 1 71  ? -1.673  -30.439 18.113  1.00 82.32  ? 71  LEU B CA  1 
ATOM   2528 C  C   . LEU B 1 71  ? -1.248  -31.303 19.299  1.00 80.82  ? 71  LEU B C   1 
ATOM   2529 O  O   . LEU B 1 71  ? -1.446  -32.531 19.234  1.00 81.49  ? 71  LEU B O   1 
ATOM   2530 C  CB  . LEU B 1 71  ? -0.442  -30.078 17.280  1.00 84.14  ? 71  LEU B CB  1 
ATOM   2531 C  CG  . LEU B 1 71  ? 0.516   -31.238 17.010  1.00 87.74  ? 71  LEU B CG  1 
ATOM   2532 C  CD1 . LEU B 1 71  ? -0.190  -32.388 16.298  1.00 89.05  ? 71  LEU B CD1 1 
ATOM   2533 C  CD2 . LEU B 1 71  ? 1.713   -30.765 16.202  1.00 90.42  ? 71  LEU B CD2 1 
HETATM 2534 N  N   . MSE B 1 72  ? -0.638  -30.688 20.315  1.00 76.25  ? 72  MSE B N   1 
HETATM 2535 C  CA  . MSE B 1 72  ? -0.168  -31.408 21.524  1.00 75.43  ? 72  MSE B CA  1 
HETATM 2536 C  C   . MSE B 1 72  ? -1.364  -32.132 22.141  1.00 67.99  ? 72  MSE B C   1 
HETATM 2537 O  O   . MSE B 1 72  ? -1.325  -33.374 22.231  1.00 67.21  ? 72  MSE B O   1 
HETATM 2538 C  CB  . MSE B 1 72  ? 0.472   -30.447 22.531  1.00 83.14  ? 72  MSE B CB  1 
HETATM 2539 C  CG  . MSE B 1 72  ? 1.240   -31.148 23.646  1.00 84.96  ? 72  MSE B CG  1 
HETATM 2540 SE SE  . MSE B 1 72  ? 2.693   -32.284 22.944  1.00 88.12  ? 72  MSE B SE  1 
HETATM 2541 C  CE  . MSE B 1 72  ? 4.244   -31.119 22.633  1.00 94.85  ? 72  MSE B CE  1 
ATOM   2542 N  N   . SER B 1 73  ? -2.399  -31.377 22.510  1.00 60.10  ? 73  SER B N   1 
ATOM   2543 C  CA  . SER B 1 73  ? -3.646  -31.917 23.101  1.00 58.38  ? 73  SER B CA  1 
ATOM   2544 C  C   . SER B 1 73  ? -3.961  -33.256 22.424  1.00 58.99  ? 73  SER B C   1 
ATOM   2545 O  O   . SER B 1 73  ? -4.000  -34.274 23.128  1.00 65.06  ? 73  SER B O   1 
ATOM   2546 C  CB  . SER B 1 73  ? -4.782  -30.937 22.979  1.00 56.47  ? 73  SER B CB  1 
ATOM   2547 O  OG  . SER B 1 73  ? -4.439  -29.687 23.558  1.00 54.44  ? 73  SER B OG  1 
ATOM   2548 N  N   . HIS B 1 74  ? -4.101  -33.256 21.098  1.00 58.51  ? 74  HIS B N   1 
ATOM   2549 C  CA  . HIS B 1 74  ? -4.411  -34.456 20.275  1.00 60.72  ? 74  HIS B CA  1 
ATOM   2550 C  C   . HIS B 1 74  ? -3.321  -35.517 20.475  1.00 62.59  ? 74  HIS B C   1 
ATOM   2551 O  O   . HIS B 1 74  ? -3.677  -36.684 20.707  1.00 60.72  ? 74  HIS B O   1 
ATOM   2552 C  CB  . HIS B 1 74  ? -4.618  -34.072 18.796  1.00 59.32  ? 74  HIS B CB  1 
ATOM   2553 C  CG  . HIS B 1 74  ? -5.950  -33.448 18.531  1.00 57.20  ? 74  HIS B CG  1 
ATOM   2554 N  ND1 . HIS B 1 74  ? -7.056  -34.191 18.177  1.00 55.27  ? 74  HIS B ND1 1 
ATOM   2555 C  CD2 . HIS B 1 74  ? -6.371  -32.166 18.601  1.00 56.87  ? 74  HIS B CD2 1 
ATOM   2556 C  CE1 . HIS B 1 74  ? -8.097  -33.397 18.031  1.00 55.58  ? 74  HIS B CE1 1 
ATOM   2557 N  NE2 . HIS B 1 74  ? -7.703  -32.149 18.290  1.00 56.39  ? 74  HIS B NE2 1 
ATOM   2558 N  N   . PHE B 1 75  ? -2.047  -35.126 20.402  1.00 68.78  ? 75  PHE B N   1 
ATOM   2559 C  CA  . PHE B 1 75  ? -0.883  -36.047 20.495  1.00 77.06  ? 75  PHE B CA  1 
ATOM   2560 C  C   . PHE B 1 75  ? -0.959  -36.829 21.814  1.00 75.45  ? 75  PHE B C   1 
ATOM   2561 O  O   . PHE B 1 75  ? -0.992  -38.080 21.784  1.00 73.64  ? 75  PHE B O   1 
ATOM   2562 C  CB  . PHE B 1 75  ? 0.435   -35.280 20.354  1.00 85.71  ? 75  PHE B CB  1 
ATOM   2563 C  CG  . PHE B 1 75  ? 1.662   -36.156 20.249  1.00 95.26  ? 75  PHE B CG  1 
ATOM   2564 C  CD1 . PHE B 1 75  ? 1.879   -36.961 19.139  1.00 98.89  ? 75  PHE B CD1 1 
ATOM   2565 C  CD2 . PHE B 1 75  ? 2.614   -36.168 21.257  1.00 97.26  ? 75  PHE B CD2 1 
ATOM   2566 C  CE1 . PHE B 1 75  ? 3.007   -37.763 19.044  1.00 98.86  ? 75  PHE B CE1 1 
ATOM   2567 C  CE2 . PHE B 1 75  ? 3.745   -36.968 21.160  1.00 99.77  ? 75  PHE B CE2 1 
ATOM   2568 C  CZ  . PHE B 1 75  ? 3.941   -37.763 20.052  1.00 100.49 ? 75  PHE B CZ  1 
HETATM 2569 N  N   . MSE B 1 76  ? -0.980  -36.149 22.951  1.00 73.31  ? 76  MSE B N   1 
HETATM 2570 C  CA  . MSE B 1 76  ? -0.994  -36.852 24.222  1.00 73.48  ? 76  MSE B CA  1 
HETATM 2571 C  C   . MSE B 1 76  ? -2.146  -37.810 24.286  1.00 72.60  ? 76  MSE B C   1 
HETATM 2572 O  O   . MSE B 1 76  ? -1.976  -38.952 24.758  1.00 75.08  ? 76  MSE B O   1 
HETATM 2573 C  CB  . MSE B 1 76  ? -1.153  -35.835 25.342  1.00 74.94  ? 76  MSE B CB  1 
HETATM 2574 C  CG  . MSE B 1 76  ? -0.437  -34.534 25.004  1.00 78.36  ? 76  MSE B CG  1 
HETATM 2575 SE SE  . MSE B 1 76  ? 1.286   -34.468 25.957  1.00 78.91  ? 76  MSE B SE  1 
HETATM 2576 C  CE  . MSE B 1 76  ? 2.464   -34.524 24.380  1.00 75.70  ? 76  MSE B CE  1 
ATOM   2577 N  N   . LEU B 1 77  ? -3.313  -37.386 23.826  1.00 69.78  ? 77  LEU B N   1 
ATOM   2578 C  CA  . LEU B 1 77  ? -4.538  -38.222 23.888  1.00 69.09  ? 77  LEU B CA  1 
ATOM   2579 C  C   . LEU B 1 77  ? -4.365  -39.469 23.015  1.00 68.42  ? 77  LEU B C   1 
ATOM   2580 O  O   . LEU B 1 77  ? -5.009  -40.485 23.341  1.00 65.83  ? 77  LEU B O   1 
ATOM   2581 C  CB  . LEU B 1 77  ? -5.741  -37.377 23.462  1.00 69.47  ? 77  LEU B CB  1 
ATOM   2582 C  CG  . LEU B 1 77  ? -6.311  -36.483 24.563  1.00 70.67  ? 77  LEU B CG  1 
ATOM   2583 C  CD1 . LEU B 1 77  ? -7.074  -35.300 23.980  1.00 73.26  ? 77  LEU B CD1 1 
ATOM   2584 C  CD2 . LEU B 1 77  ? -7.207  -37.288 25.494  1.00 69.58  ? 77  LEU B CD2 1 
ATOM   2585 N  N   . TRP B 1 78  ? -3.529  -39.413 21.970  1.00 68.97  ? 78  TRP B N   1 
ATOM   2586 C  CA  . TRP B 1 78  ? -3.131  -40.617 21.190  1.00 72.04  ? 78  TRP B CA  1 
ATOM   2587 C  C   . TRP B 1 78  ? -2.246  -41.484 22.087  1.00 75.26  ? 78  TRP B C   1 
ATOM   2588 O  O   . TRP B 1 78  ? -2.526  -42.692 22.206  1.00 76.39  ? 78  TRP B O   1 
ATOM   2589 C  CB  . TRP B 1 78  ? -2.418  -40.271 19.873  1.00 73.12  ? 78  TRP B CB  1 
ATOM   2590 C  CG  . TRP B 1 78  ? -3.172  -39.343 18.973  1.00 72.70  ? 78  TRP B CG  1 
ATOM   2591 C  CD1 . TRP B 1 78  ? -4.526  -39.213 18.873  1.00 73.34  ? 78  TRP B CD1 1 
ATOM   2592 C  CD2 . TRP B 1 78  ? -2.613  -38.418 18.024  1.00 73.41  ? 78  TRP B CD2 1 
ATOM   2593 N  NE1 . TRP B 1 78  ? -4.848  -38.264 17.942  1.00 71.98  ? 78  TRP B NE1 1 
ATOM   2594 C  CE2 . TRP B 1 78  ? -3.695  -37.758 17.406  1.00 72.44  ? 78  TRP B CE2 1 
ATOM   2595 C  CE3 . TRP B 1 78  ? -1.312  -38.082 17.638  1.00 74.94  ? 78  TRP B CE3 1 
ATOM   2596 C  CZ2 . TRP B 1 78  ? -3.512  -36.786 16.424  1.00 73.77  ? 78  TRP B CZ2 1 
ATOM   2597 C  CZ3 . TRP B 1 78  ? -1.131  -37.119 16.670  1.00 74.25  ? 78  TRP B CZ3 1 
ATOM   2598 C  CH2 . TRP B 1 78  ? -2.218  -36.482 16.072  1.00 74.69  ? 78  TRP B CH2 1 
ATOM   2599 N  N   . LYS B 1 79  ? -1.240  -40.873 22.720  1.00 79.13  ? 79  LYS B N   1 
ATOM   2600 C  CA  . LYS B 1 79  ? -0.290  -41.573 23.627  1.00 82.81  ? 79  LYS B CA  1 
ATOM   2601 C  C   . LYS B 1 79  ? -1.081  -42.324 24.706  1.00 77.69  ? 79  LYS B C   1 
ATOM   2602 O  O   . LYS B 1 79  ? -0.749  -43.493 24.965  1.00 79.07  ? 79  LYS B O   1 
ATOM   2603 C  CB  . LYS B 1 79  ? 0.727   -40.597 24.229  1.00 86.40  ? 79  LYS B CB  1 
ATOM   2604 C  CG  . LYS B 1 79  ? 2.021   -41.251 24.709  1.00 90.52  ? 79  LYS B CG  1 
ATOM   2605 C  CD  . LYS B 1 79  ? 3.290   -40.567 24.202  1.00 94.57  ? 79  LYS B CD  1 
ATOM   2606 C  CE  . LYS B 1 79  ? 4.530   -41.430 24.309  1.00 95.38  ? 79  LYS B CE  1 
ATOM   2607 N  NZ  . LYS B 1 79  ? 4.973   -41.572 25.716  1.00 96.07  ? 79  LYS B NZ  1 
ATOM   2608 N  N   . LYS B 1 80  ? -2.115  -41.690 25.269  1.00 70.75  ? 80  LYS B N   1 
ATOM   2609 C  CA  . LYS B 1 80  ? -3.021  -42.296 26.281  1.00 68.66  ? 80  LYS B CA  1 
ATOM   2610 C  C   . LYS B 1 80  ? -3.655  -43.578 25.725  1.00 67.86  ? 80  LYS B C   1 
ATOM   2611 O  O   . LYS B 1 80  ? -3.662  -44.580 26.455  1.00 67.86  ? 80  LYS B O   1 
ATOM   2612 C  CB  . LYS B 1 80  ? -4.095  -41.292 26.701  1.00 68.49  ? 80  LYS B CB  1 
ATOM   2613 C  CG  . LYS B 1 80  ? -5.181  -41.846 27.611  1.00 70.29  ? 80  LYS B CG  1 
ATOM   2614 C  CD  . LYS B 1 80  ? -5.834  -40.795 28.483  1.00 71.13  ? 80  LYS B CD  1 
ATOM   2615 C  CE  . LYS B 1 80  ? -4.936  -40.310 29.603  1.00 75.03  ? 80  LYS B CE  1 
ATOM   2616 N  NZ  . LYS B 1 80  ? -5.710  -39.659 30.686  1.00 76.37  ? 80  LYS B NZ  1 
ATOM   2617 N  N   . CYS B 1 81  ? -4.166  -43.557 24.490  1.00 68.45  ? 81  CYS B N   1 
ATOM   2618 C  CA  . CYS B 1 81  ? -4.780  -44.742 23.828  1.00 72.84  ? 81  CYS B CA  1 
ATOM   2619 C  C   . CYS B 1 81  ? -3.811  -45.923 23.925  1.00 74.35  ? 81  CYS B C   1 
ATOM   2620 O  O   . CYS B 1 81  ? -4.283  -47.051 24.179  1.00 74.15  ? 81  CYS B O   1 
ATOM   2621 C  CB  . CYS B 1 81  ? -5.141  -44.477 22.369  1.00 74.88  ? 81  CYS B CB  1 
ATOM   2622 S  SG  . CYS B 1 81  ? -6.252  -45.718 21.646  1.00 72.96  ? 81  CYS B SG  1 
ATOM   2623 N  N   . ILE B 1 82  ? -2.512  -45.650 23.763  1.00 76.59  ? 82  ILE B N   1 
ATOM   2624 C  CA  . ILE B 1 82  ? -1.410  -46.655 23.870  1.00 79.31  ? 82  ILE B CA  1 
ATOM   2625 C  C   . ILE B 1 82  ? -1.231  -47.024 25.347  1.00 79.56  ? 82  ILE B C   1 
ATOM   2626 O  O   . ILE B 1 82  ? -1.329  -48.225 25.672  1.00 81.34  ? 82  ILE B O   1 
ATOM   2627 C  CB  . ILE B 1 82  ? -0.100  -46.121 23.247  1.00 78.50  ? 82  ILE B CB  1 
ATOM   2628 C  CG1 . ILE B 1 82  ? -0.312  -45.586 21.828  1.00 77.13  ? 82  ILE B CG1 1 
ATOM   2629 C  CG2 . ILE B 1 82  ? 0.998   -47.174 23.288  1.00 78.78  ? 82  ILE B CG2 1 
ATOM   2630 C  CD1 . ILE B 1 82  ? -1.090  -46.516 20.936  1.00 77.98  ? 82  ILE B CD1 1 
ATOM   2631 N  N   . ASP B 1 83  ? -0.991  -46.023 26.202  1.00 79.36  ? 83  ASP B N   1 
ATOM   2632 C  CA  . ASP B 1 83  ? -0.667  -46.190 27.646  1.00 78.25  ? 83  ASP B CA  1 
ATOM   2633 C  C   . ASP B 1 83  ? -1.732  -47.071 28.307  1.00 76.81  ? 83  ASP B C   1 
ATOM   2634 O  O   . ASP B 1 83  ? -1.357  -48.125 28.853  1.00 79.85  ? 83  ASP B O   1 
ATOM   2635 C  CB  . ASP B 1 83  ? -0.537  -44.835 28.346  1.00 76.55  ? 83  ASP B CB  1 
ATOM   2636 C  CG  . ASP B 1 83  ? 0.658   -44.016 27.876  1.00 77.06  ? 83  ASP B CG  1 
ATOM   2637 O  OD1 . ASP B 1 83  ? 1.480   -44.545 27.097  1.00 75.04  ? 83  ASP B OD1 1 
ATOM   2638 O  OD2 . ASP B 1 83  ? 0.754   -42.844 28.282  1.00 79.67  ? 83  ASP B OD2 1 
ATOM   2639 N  N   . GLU B 1 84  ? -3.005  -46.680 28.212  1.00 73.38  ? 84  GLU B N   1 
ATOM   2640 C  CA  . GLU B 1 84  ? -4.153  -47.418 28.807  1.00 70.26  ? 84  GLU B CA  1 
ATOM   2641 C  C   . GLU B 1 84  ? -4.512  -48.628 27.928  1.00 68.28  ? 84  GLU B C   1 
ATOM   2642 O  O   . GLU B 1 84  ? -5.541  -49.265 28.214  1.00 68.73  ? 84  GLU B O   1 
ATOM   2643 C  CB  . GLU B 1 84  ? -5.374  -46.505 28.959  1.00 69.13  ? 84  GLU B CB  1 
ATOM   2644 C  CG  . GLU B 1 84  ? -5.118  -45.206 29.705  1.00 67.71  ? 84  GLU B CG  1 
ATOM   2645 C  CD  . GLU B 1 84  ? -6.360  -44.339 29.897  1.00 69.14  ? 84  GLU B CD  1 
ATOM   2646 O  OE1 . GLU B 1 84  ? -6.309  -43.419 30.742  1.00 73.07  ? 84  GLU B OE1 1 
ATOM   2647 O  OE2 . GLU B 1 84  ? -7.376  -44.564 29.194  1.00 66.72  ? 84  GLU B OE2 1 
ATOM   2648 N  N   . ASN B 1 85  ? -3.694  -48.947 26.918  1.00 66.37  ? 85  ASN B N   1 
ATOM   2649 C  CA  . ASN B 1 85  ? -3.952  -50.015 25.912  1.00 70.54  ? 85  ASN B CA  1 
ATOM   2650 C  C   . ASN B 1 85  ? -5.456  -50.061 25.602  1.00 70.93  ? 85  ASN B C   1 
ATOM   2651 O  O   . ASN B 1 85  ? -6.096  -51.101 25.870  1.00 71.94  ? 85  ASN B O   1 
ATOM   2652 C  CB  . ASN B 1 85  ? -3.414  -51.378 26.361  1.00 72.14  ? 85  ASN B CB  1 
ATOM   2653 C  CG  . ASN B 1 85  ? -3.432  -52.417 25.257  1.00 75.70  ? 85  ASN B CG  1 
ATOM   2654 O  OD1 . ASN B 1 85  ? -2.577  -52.409 24.374  1.00 77.69  ? 85  ASN B OD1 1 
ATOM   2655 N  ND2 . ASN B 1 85  ? -4.403  -53.316 25.288  1.00 76.37  ? 85  ASN B ND2 1 
ATOM   2656 N  N   . LEU B 1 86  ? -5.994  -48.964 25.061  1.00 70.20  ? 86  LEU B N   1 
ATOM   2657 C  CA  . LEU B 1 86  ? -7.402  -48.862 24.591  1.00 67.52  ? 86  LEU B CA  1 
ATOM   2658 C  C   . LEU B 1 86  ? -7.472  -49.371 23.150  1.00 63.44  ? 86  LEU B C   1 
ATOM   2659 O  O   . LEU B 1 86  ? -6.530  -49.072 22.389  1.00 62.71  ? 86  LEU B O   1 
ATOM   2660 C  CB  . LEU B 1 86  ? -7.876  -47.406 24.659  1.00 69.98  ? 86  LEU B CB  1 
ATOM   2661 C  CG  . LEU B 1 86  ? -7.615  -46.664 25.969  1.00 72.61  ? 86  LEU B CG  1 
ATOM   2662 C  CD1 . LEU B 1 86  ? -8.193  -45.260 25.928  1.00 73.42  ? 86  LEU B CD1 1 
ATOM   2663 C  CD2 . LEU B 1 86  ? -8.181  -47.426 27.157  1.00 74.43  ? 86  LEU B CD2 1 
ATOM   2664 N  N   . ASP B 1 87  ? -8.541  -50.097 22.798  1.00 62.94  ? 87  ASP B N   1 
ATOM   2665 C  CA  . ASP B 1 87  ? -8.882  -50.467 21.396  1.00 66.15  ? 87  ASP B CA  1 
ATOM   2666 C  C   . ASP B 1 87  ? -8.919  -49.193 20.532  1.00 65.80  ? 87  ASP B C   1 
ATOM   2667 O  O   . ASP B 1 87  ? -8.354  -49.191 19.408  1.00 63.50  ? 87  ASP B O   1 
ATOM   2668 C  CB  . ASP B 1 87  ? -10.237 -51.183 21.307  1.00 67.04  ? 87  ASP B CB  1 
ATOM   2669 C  CG  . ASP B 1 87  ? -10.323 -52.524 22.015  1.00 67.69  ? 87  ASP B CG  1 
ATOM   2670 O  OD1 . ASP B 1 87  ? -9.268  -53.126 22.272  1.00 72.68  ? 87  ASP B OD1 1 
ATOM   2671 O  OD2 . ASP B 1 87  ? -11.459 -52.963 22.286  1.00 69.10  ? 87  ASP B OD2 1 
ATOM   2672 N  N   . TYR B 1 88  ? -9.557  -48.143 21.059  1.00 60.64  ? 88  TYR B N   1 
ATOM   2673 C  CA  . TYR B 1 88  ? -9.827  -46.864 20.362  1.00 55.60  ? 88  TYR B CA  1 
ATOM   2674 C  C   . TYR B 1 88  ? -10.177 -45.785 21.382  1.00 52.77  ? 88  TYR B C   1 
ATOM   2675 O  O   . TYR B 1 88  ? -10.708 -46.109 22.445  1.00 53.66  ? 88  TYR B O   1 
ATOM   2676 C  CB  . TYR B 1 88  ? -11.010 -47.018 19.411  1.00 55.02  ? 88  TYR B CB  1 
ATOM   2677 C  CG  . TYR B 1 88  ? -12.344 -47.098 20.104  1.00 54.22  ? 88  TYR B CG  1 
ATOM   2678 C  CD1 . TYR B 1 88  ? -12.852 -48.302 20.556  1.00 52.87  ? 88  TYR B CD1 1 
ATOM   2679 C  CD2 . TYR B 1 88  ? -13.113 -45.965 20.293  1.00 57.37  ? 88  TYR B CD2 1 
ATOM   2680 C  CE1 . TYR B 1 88  ? -14.091 -48.378 21.178  1.00 54.50  ? 88  TYR B CE1 1 
ATOM   2681 C  CE2 . TYR B 1 88  ? -14.349 -46.023 20.920  1.00 58.71  ? 88  TYR B CE2 1 
ATOM   2682 C  CZ  . TYR B 1 88  ? -14.847 -47.234 21.362  1.00 54.87  ? 88  TYR B CZ  1 
ATOM   2683 O  OH  . TYR B 1 88  ? -16.075 -47.282 21.962  1.00 49.56  ? 88  TYR B OH  1 
ATOM   2684 N  N   . ILE B 1 89  ? -9.944  -44.529 21.018  1.00 53.16  ? 89  ILE B N   1 
ATOM   2685 C  CA  . ILE B 1 89  ? -10.351 -43.338 21.814  1.00 53.84  ? 89  ILE B CA  1 
ATOM   2686 C  C   . ILE B 1 89  ? -11.031 -42.333 20.874  1.00 53.11  ? 89  ILE B C   1 
ATOM   2687 O  O   . ILE B 1 89  ? -10.731 -42.347 19.669  1.00 57.32  ? 89  ILE B O   1 
ATOM   2688 C  CB  . ILE B 1 89  ? -9.131  -42.763 22.555  1.00 53.87  ? 89  ILE B CB  1 
ATOM   2689 C  CG1 . ILE B 1 89  ? -9.538  -41.700 23.574  1.00 55.41  ? 89  ILE B CG1 1 
ATOM   2690 C  CG2 . ILE B 1 89  ? -8.091  -42.245 21.574  1.00 55.70  ? 89  ILE B CG2 1 
ATOM   2691 C  CD1 . ILE B 1 89  ? -8.383  -41.172 24.397  1.00 58.17  ? 89  ILE B CD1 1 
ATOM   2692 N  N   . THR B 1 90  ? -11.931 -41.508 21.413  1.00 50.40  ? 90  THR B N   1 
ATOM   2693 C  CA  . THR B 1 90  ? -12.871 -40.641 20.653  1.00 48.10  ? 90  THR B CA  1 
ATOM   2694 C  C   . THR B 1 90  ? -12.715 -39.191 21.120  1.00 48.52  ? 90  THR B C   1 
ATOM   2695 O  O   . THR B 1 90  ? -13.130 -38.898 22.253  1.00 45.92  ? 90  THR B O   1 
ATOM   2696 C  CB  . THR B 1 90  ? -14.305 -41.148 20.834  1.00 46.64  ? 90  THR B CB  1 
ATOM   2697 O  OG1 . THR B 1 90  ? -14.264 -42.570 20.749  1.00 45.27  ? 90  THR B OG1 1 
ATOM   2698 C  CG2 . THR B 1 90  ? -15.260 -40.608 19.798  1.00 46.86  ? 90  THR B CG2 1 
ATOM   2699 N  N   . LEU B 1 91  ? -12.147 -38.329 20.270  1.00 49.26  ? 91  LEU B N   1 
ATOM   2700 C  CA  . LEU B 1 91  ? -11.694 -36.963 20.641  1.00 51.37  ? 91  LEU B CA  1 
ATOM   2701 C  C   . LEU B 1 91  ? -12.610 -35.911 20.022  1.00 54.05  ? 91  LEU B C   1 
ATOM   2702 O  O   . LEU B 1 91  ? -12.979 -36.066 18.843  1.00 58.72  ? 91  LEU B O   1 
ATOM   2703 C  CB  . LEU B 1 91  ? -10.261 -36.757 20.146  1.00 50.51  ? 91  LEU B CB  1 
ATOM   2704 C  CG  . LEU B 1 91  ? -9.265  -37.848 20.523  1.00 49.29  ? 91  LEU B CG  1 
ATOM   2705 C  CD1 . LEU B 1 91  ? -7.844  -37.338 20.365  1.00 49.25  ? 91  LEU B CD1 1 
ATOM   2706 C  CD2 . LEU B 1 91  ? -9.501  -38.335 21.942  1.00 49.83  ? 91  LEU B CD2 1 
ATOM   2707 N  N   . PHE B 1 92  ? -12.903 -34.857 20.787  1.00 54.90  ? 92  PHE B N   1 
ATOM   2708 C  CA  . PHE B 1 92  ? -13.708 -33.682 20.365  1.00 56.42  ? 92  PHE B CA  1 
ATOM   2709 C  C   . PHE B 1 92  ? -13.007 -32.402 20.824  1.00 57.43  ? 92  PHE B C   1 
ATOM   2710 O  O   . PHE B 1 92  ? -12.147 -32.498 21.713  1.00 54.95  ? 92  PHE B O   1 
ATOM   2711 C  CB  . PHE B 1 92  ? -15.104 -33.752 20.985  1.00 55.33  ? 92  PHE B CB  1 
ATOM   2712 C  CG  . PHE B 1 92  ? -15.848 -35.038 20.747  1.00 55.20  ? 92  PHE B CG  1 
ATOM   2713 C  CD1 . PHE B 1 92  ? -16.663 -35.184 19.635  1.00 57.63  ? 92  PHE B CD1 1 
ATOM   2714 C  CD2 . PHE B 1 92  ? -15.740 -36.095 21.634  1.00 55.78  ? 92  PHE B CD2 1 
ATOM   2715 C  CE1 . PHE B 1 92  ? -17.371 -36.358 19.425  1.00 57.56  ? 92  PHE B CE1 1 
ATOM   2716 C  CE2 . PHE B 1 92  ? -16.440 -37.270 21.420  1.00 57.51  ? 92  PHE B CE2 1 
ATOM   2717 C  CZ  . PHE B 1 92  ? -17.257 -37.399 20.317  1.00 57.33  ? 92  PHE B CZ  1 
ATOM   2718 N  N   . GLU B 1 93  ? -13.379 -31.255 20.243  1.00 57.98  ? 93  GLU B N   1 
ATOM   2719 C  CA  . GLU B 1 93  ? -13.054 -29.904 20.775  1.00 59.36  ? 93  GLU B CA  1 
ATOM   2720 C  C   . GLU B 1 93  ? -14.331 -29.310 21.382  1.00 58.60  ? 93  GLU B C   1 
ATOM   2721 O  O   . GLU B 1 93  ? -15.429 -29.772 21.032  1.00 59.25  ? 93  GLU B O   1 
ATOM   2722 C  CB  . GLU B 1 93  ? -12.444 -29.047 19.668  1.00 61.50  ? 93  GLU B CB  1 
ATOM   2723 C  CG  . GLU B 1 93  ? -11.047 -29.502 19.275  1.00 63.07  ? 93  GLU B CG  1 
ATOM   2724 C  CD  . GLU B 1 93  ? -10.669 -29.253 17.823  1.00 66.34  ? 93  GLU B CD  1 
ATOM   2725 O  OE1 . GLU B 1 93  ? -9.743  -29.917 17.337  1.00 71.44  ? 93  GLU B OE1 1 
ATOM   2726 O  OE2 . GLU B 1 93  ? -11.305 -28.395 17.173  1.00 66.15  ? 93  GLU B OE2 1 
ATOM   2727 N  N   . ASP B 1 94  ? -14.186 -28.316 22.253  1.00 58.36  ? 94  ASP B N   1 
ATOM   2728 C  CA  . ASP B 1 94  ? -15.236 -27.873 23.212  1.00 61.83  ? 94  ASP B CA  1 
ATOM   2729 C  C   . ASP B 1 94  ? -16.297 -27.012 22.512  1.00 61.56  ? 94  ASP B C   1 
ATOM   2730 O  O   . ASP B 1 94  ? -17.122 -26.402 23.223  1.00 68.09  ? 94  ASP B O   1 
ATOM   2731 C  CB  . ASP B 1 94  ? -14.598 -27.145 24.403  1.00 64.90  ? 94  ASP B CB  1 
ATOM   2732 C  CG  . ASP B 1 94  ? -13.518 -26.137 24.031  1.00 67.31  ? 94  ASP B CG  1 
ATOM   2733 O  OD1 . ASP B 1 94  ? -13.034 -26.181 22.871  1.00 69.02  ? 94  ASP B OD1 1 
ATOM   2734 O  OD2 . ASP B 1 94  ? -13.164 -25.315 24.901  1.00 65.52  ? 94  ASP B OD2 1 
ATOM   2735 N  N   . ASP B 1 95  ? -16.324 -27.000 21.178  1.00 60.11  ? 95  ASP B N   1 
ATOM   2736 C  CA  . ASP B 1 95  ? -17.162 -26.067 20.380  1.00 56.80  ? 95  ASP B CA  1 
ATOM   2737 C  C   . ASP B 1 95  ? -18.101 -26.851 19.455  1.00 53.92  ? 95  ASP B C   1 
ATOM   2738 O  O   . ASP B 1 95  ? -18.510 -26.272 18.440  1.00 58.44  ? 95  ASP B O   1 
ATOM   2739 C  CB  . ASP B 1 95  ? -16.271 -25.097 19.599  1.00 57.10  ? 95  ASP B CB  1 
ATOM   2740 C  CG  . ASP B 1 95  ? -15.421 -25.738 18.509  1.00 58.78  ? 95  ASP B CG  1 
ATOM   2741 O  OD1 . ASP B 1 95  ? -15.441 -26.978 18.384  1.00 54.78  ? 95  ASP B OD1 1 
ATOM   2742 O  OD2 . ASP B 1 95  ? -14.747 -24.984 17.783  1.00 64.01  ? 95  ASP B OD2 1 
ATOM   2743 N  N   . ILE B 1 96  ? -18.448 -28.096 19.797  1.00 50.77  ? 96  ILE B N   1 
ATOM   2744 C  CA  . ILE B 1 96  ? -19.266 -28.980 18.916  1.00 50.62  ? 96  ILE B CA  1 
ATOM   2745 C  C   . ILE B 1 96  ? -20.736 -28.931 19.329  1.00 47.90  ? 96  ILE B C   1 
ATOM   2746 O  O   . ILE B 1 96  ? -21.030 -28.453 20.429  1.00 49.65  ? 96  ILE B O   1 
ATOM   2747 C  CB  . ILE B 1 96  ? -18.758 -30.428 18.909  1.00 52.75  ? 96  ILE B CB  1 
ATOM   2748 C  CG1 . ILE B 1 96  ? -18.667 -30.990 20.323  1.00 56.86  ? 96  ILE B CG1 1 
ATOM   2749 C  CG2 . ILE B 1 96  ? -17.435 -30.554 18.173  1.00 55.48  ? 96  ILE B CG2 1 
ATOM   2750 C  CD1 . ILE B 1 96  ? -18.950 -32.468 20.396  1.00 61.32  ? 96  ILE B CD1 1 
ATOM   2751 N  N   . LEU B 1 97  ? -21.601 -29.388 18.420  1.00 48.82  ? 97  LEU B N   1 
ATOM   2752 C  CA  . LEU B 1 97  ? -23.065 -29.582 18.609  1.00 47.94  ? 97  LEU B CA  1 
ATOM   2753 C  C   . LEU B 1 97  ? -23.408 -31.000 18.149  1.00 47.11  ? 97  LEU B C   1 
ATOM   2754 O  O   . LEU B 1 97  ? -22.823 -31.424 17.146  1.00 44.63  ? 97  LEU B O   1 
ATOM   2755 C  CB  . LEU B 1 97  ? -23.846 -28.544 17.793  1.00 46.77  ? 97  LEU B CB  1 
ATOM   2756 C  CG  . LEU B 1 97  ? -23.436 -27.088 18.010  1.00 46.88  ? 97  LEU B CG  1 
ATOM   2757 C  CD1 . LEU B 1 97  ? -24.129 -26.172 17.013  1.00 46.83  ? 97  LEU B CD1 1 
ATOM   2758 C  CD2 . LEU B 1 97  ? -23.720 -26.645 19.437  1.00 45.27  ? 97  LEU B CD2 1 
ATOM   2759 N  N   . LEU B 1 98  ? -24.313 -31.694 18.844  1.00 47.01  ? 98  LEU B N   1 
ATOM   2760 C  CA  . LEU B 1 98  ? -24.638 -33.119 18.587  1.00 48.35  ? 98  LEU B CA  1 
ATOM   2761 C  C   . LEU B 1 98  ? -25.970 -33.245 17.833  1.00 53.96  ? 98  LEU B C   1 
ATOM   2762 O  O   . LEU B 1 98  ? -26.788 -32.305 17.900  1.00 58.55  ? 98  LEU B O   1 
ATOM   2763 C  CB  . LEU B 1 98  ? -24.698 -33.851 19.927  1.00 46.90  ? 98  LEU B CB  1 
ATOM   2764 C  CG  . LEU B 1 98  ? -23.394 -33.948 20.719  1.00 45.62  ? 98  LEU B CG  1 
ATOM   2765 C  CD1 . LEU B 1 98  ? -23.542 -34.954 21.854  1.00 45.42  ? 98  LEU B CD1 1 
ATOM   2766 C  CD2 . LEU B 1 98  ? -22.220 -34.341 19.841  1.00 44.91  ? 98  LEU B CD2 1 
ATOM   2767 N  N   . GLY B 1 99  ? -26.188 -34.393 17.179  1.00 57.72  ? 99  GLY B N   1 
ATOM   2768 C  CA  . GLY B 1 99  ? -27.416 -34.747 16.437  1.00 60.23  ? 99  GLY B CA  1 
ATOM   2769 C  C   . GLY B 1 99  ? -28.149 -35.917 17.076  1.00 63.55  ? 99  GLY B C   1 
ATOM   2770 O  O   . GLY B 1 99  ? -27.590 -36.545 17.988  1.00 64.48  ? 99  GLY B O   1 
ATOM   2771 N  N   . GLU B 1 100 ? -29.337 -36.243 16.570  1.00 69.70  ? 100 GLU B N   1 
ATOM   2772 C  CA  . GLU B 1 100 ? -30.421 -36.919 17.333  1.00 80.73  ? 100 GLU B CA  1 
ATOM   2773 C  C   . GLU B 1 100 ? -29.919 -38.187 18.040  1.00 82.20  ? 100 GLU B C   1 
ATOM   2774 O  O   . GLU B 1 100 ? -30.139 -38.282 19.265  1.00 91.19  ? 100 GLU B O   1 
ATOM   2775 C  CB  . GLU B 1 100 ? -31.604 -37.229 16.417  1.00 87.56  ? 100 GLU B CB  1 
ATOM   2776 C  CG  . GLU B 1 100 ? -32.916 -37.370 17.172  1.00 94.74  ? 100 GLU B CG  1 
ATOM   2777 C  CD  . GLU B 1 100 ? -34.156 -37.136 16.330  1.00 98.96  ? 100 GLU B CD  1 
ATOM   2778 O  OE1 . GLU B 1 100 ? -35.167 -36.670 16.893  1.00 101.86 ? 100 GLU B OE1 1 
ATOM   2779 O  OE2 . GLU B 1 100 ? -34.113 -37.421 15.113  1.00 98.34  ? 100 GLU B OE2 1 
ATOM   2780 N  N   . ASN B 1 101 ? -29.328 -39.136 17.306  1.00 75.78  ? 101 ASN B N   1 
ATOM   2781 C  CA  . ASN B 1 101 ? -28.996 -40.488 17.830  1.00 74.84  ? 101 ASN B CA  1 
ATOM   2782 C  C   . ASN B 1 101 ? -27.509 -40.572 18.177  1.00 71.82  ? 101 ASN B C   1 
ATOM   2783 O  O   . ASN B 1 101 ? -26.947 -41.664 18.019  1.00 74.93  ? 101 ASN B O   1 
ATOM   2784 C  CB  . ASN B 1 101 ? -29.383 -41.590 16.841  1.00 80.54  ? 101 ASN B CB  1 
ATOM   2785 C  CG  . ASN B 1 101 ? -30.862 -41.589 16.521  1.00 90.52  ? 101 ASN B CG  1 
ATOM   2786 O  OD1 . ASN B 1 101 ? -31.691 -41.427 17.415  1.00 97.61  ? 101 ASN B OD1 1 
ATOM   2787 N  ND2 . ASN B 1 101 ? -31.202 -41.761 15.253  1.00 94.99  ? 101 ASN B ND2 1 
ATOM   2788 N  N   . ALA B 1 102 ? -26.911 -39.481 18.665  1.00 67.58  ? 102 ALA B N   1 
ATOM   2789 C  CA  . ALA B 1 102 ? -25.488 -39.430 19.082  1.00 65.32  ? 102 ALA B CA  1 
ATOM   2790 C  C   . ALA B 1 102 ? -25.224 -40.524 20.127  1.00 68.18  ? 102 ALA B C   1 
ATOM   2791 O  O   . ALA B 1 102 ? -24.195 -41.234 20.011  1.00 71.47  ? 102 ALA B O   1 
ATOM   2792 C  CB  . ALA B 1 102 ? -25.142 -38.063 19.618  1.00 62.40  ? 102 ALA B CB  1 
ATOM   2793 N  N   . ASN B 1 103 ? -26.131 -40.661 21.097  1.00 69.95  ? 103 ASN B N   1 
ATOM   2794 C  CA  . ASN B 1 103 ? -26.073 -41.692 22.169  1.00 67.98  ? 103 ASN B CA  1 
ATOM   2795 C  C   . ASN B 1 103 ? -25.697 -43.046 21.558  1.00 68.97  ? 103 ASN B C   1 
ATOM   2796 O  O   . ASN B 1 103 ? -24.709 -43.616 22.039  1.00 62.54  ? 103 ASN B O   1 
ATOM   2797 C  CB  . ASN B 1 103 ? -27.363 -41.737 22.992  1.00 70.08  ? 103 ASN B CB  1 
ATOM   2798 C  CG  . ASN B 1 103 ? -28.624 -41.454 22.201  1.00 73.37  ? 103 ASN B CG  1 
ATOM   2799 O  OD1 . ASN B 1 103 ? -28.616 -41.475 20.971  1.00 71.75  ? 103 ASN B OD1 1 
ATOM   2800 N  ND2 . ASN B 1 103 ? -29.717 -41.186 22.901  1.00 76.20  ? 103 ASN B ND2 1 
ATOM   2801 N  N   . LYS B 1 104 ? -26.422 -43.509 20.532  1.00 76.05  ? 104 LYS B N   1 
ATOM   2802 C  CA  . LYS B 1 104 ? -26.279 -44.864 19.925  1.00 81.98  ? 104 LYS B CA  1 
ATOM   2803 C  C   . LYS B 1 104 ? -24.841 -45.100 19.434  1.00 74.45  ? 104 LYS B C   1 
ATOM   2804 O  O   . LYS B 1 104 ? -24.420 -46.270 19.388  1.00 75.63  ? 104 LYS B O   1 
ATOM   2805 C  CB  . LYS B 1 104 ? -27.282 -45.054 18.776  1.00 91.49  ? 104 LYS B CB  1 
ATOM   2806 C  CG  . LYS B 1 104 ? -28.506 -45.913 19.092  1.00 99.56  ? 104 LYS B CG  1 
ATOM   2807 C  CD  . LYS B 1 104 ? -28.179 -47.395 19.268  1.00 106.20 ? 104 LYS B CD  1 
ATOM   2808 C  CE  . LYS B 1 104 ? -29.262 -48.340 18.784  1.00 110.02 ? 104 LYS B CE  1 
ATOM   2809 N  NZ  . LYS B 1 104 ? -30.361 -48.477 19.768  1.00 111.60 ? 104 LYS B NZ  1 
ATOM   2810 N  N   . PHE B 1 105 ? -24.126 -44.036 19.065  1.00 66.74  ? 105 PHE B N   1 
ATOM   2811 C  CA  . PHE B 1 105 ? -22.749 -44.090 18.506  1.00 63.40  ? 105 PHE B CA  1 
ATOM   2812 C  C   . PHE B 1 105 ? -21.699 -43.908 19.603  1.00 59.87  ? 105 PHE B C   1 
ATOM   2813 O  O   . PHE B 1 105 ? -20.577 -44.378 19.404  1.00 53.18  ? 105 PHE B O   1 
ATOM   2814 C  CB  . PHE B 1 105 ? -22.562 -43.001 17.449  1.00 63.16  ? 105 PHE B CB  1 
ATOM   2815 C  CG  . PHE B 1 105 ? -23.454 -43.160 16.246  1.00 60.49  ? 105 PHE B CG  1 
ATOM   2816 C  CD1 . PHE B 1 105 ? -23.151 -44.090 15.265  1.00 58.61  ? 105 PHE B CD1 1 
ATOM   2817 C  CD2 . PHE B 1 105 ? -24.603 -42.397 16.109  1.00 60.03  ? 105 PHE B CD2 1 
ATOM   2818 C  CE1 . PHE B 1 105 ? -23.978 -44.248 14.166  1.00 59.85  ? 105 PHE B CE1 1 
ATOM   2819 C  CE2 . PHE B 1 105 ? -25.429 -42.557 15.008  1.00 59.58  ? 105 PHE B CE2 1 
ATOM   2820 C  CZ  . PHE B 1 105 ? -25.114 -43.481 14.040  1.00 59.34  ? 105 PHE B CZ  1 
ATOM   2821 N  N   . LEU B 1 106 ? -22.049 -43.232 20.700  1.00 65.11  ? 106 LEU B N   1 
ATOM   2822 C  CA  . LEU B 1 106 ? -21.089 -42.730 21.722  1.00 67.68  ? 106 LEU B CA  1 
ATOM   2823 C  C   . LEU B 1 106 ? -21.302 -43.419 23.076  1.00 67.53  ? 106 LEU B C   1 
ATOM   2824 O  O   . LEU B 1 106 ? -20.289 -43.795 23.704  1.00 63.61  ? 106 LEU B O   1 
ATOM   2825 C  CB  . LEU B 1 106 ? -21.271 -41.217 21.828  1.00 68.76  ? 106 LEU B CB  1 
ATOM   2826 C  CG  . LEU B 1 106 ? -20.998 -40.448 20.537  1.00 68.83  ? 106 LEU B CG  1 
ATOM   2827 C  CD1 . LEU B 1 106 ? -21.387 -38.984 20.690  1.00 70.24  ? 106 LEU B CD1 1 
ATOM   2828 C  CD2 . LEU B 1 106 ? -19.539 -40.579 20.124  1.00 67.33  ? 106 LEU B CD2 1 
ATOM   2829 N  N   . ALA B 1 107 ? -22.556 -43.560 23.521  1.00 73.06  ? 107 ALA B N   1 
ATOM   2830 C  CA  . ALA B 1 107 ? -22.931 -44.254 24.778  1.00 77.06  ? 107 ALA B CA  1 
ATOM   2831 C  C   . ALA B 1 107 ? -22.285 -45.642 24.777  1.00 80.88  ? 107 ALA B C   1 
ATOM   2832 O  O   . ALA B 1 107 ? -21.460 -45.902 25.676  1.00 84.21  ? 107 ALA B O   1 
ATOM   2833 C  CB  . ALA B 1 107 ? -24.434 -44.340 24.930  1.00 74.91  ? 107 ALA B CB  1 
ATOM   2834 N  N   . GLU B 1 108 ? -22.616 -46.461 23.771  1.00 86.84  ? 108 GLU B N   1 
ATOM   2835 C  CA  . GLU B 1 108 ? -22.072 -47.831 23.559  1.00 87.57  ? 108 GLU B CA  1 
ATOM   2836 C  C   . GLU B 1 108 ? -20.948 -47.772 22.517  1.00 85.03  ? 108 GLU B C   1 
ATOM   2837 O  O   . GLU B 1 108 ? -20.812 -46.716 21.863  1.00 82.07  ? 108 GLU B O   1 
ATOM   2838 C  CB  . GLU B 1 108 ? -23.191 -48.774 23.110  1.00 89.21  ? 108 GLU B CB  1 
ATOM   2839 C  CG  . GLU B 1 108 ? -23.685 -48.505 21.696  1.00 88.67  ? 108 GLU B CG  1 
ATOM   2840 C  CD  . GLU B 1 108 ? -24.929 -49.263 21.273  1.00 90.70  ? 108 GLU B CD  1 
ATOM   2841 O  OE1 . GLU B 1 108 ? -25.654 -49.751 22.162  1.00 90.26  ? 108 GLU B OE1 1 
ATOM   2842 O  OE2 . GLU B 1 108 ? -25.168 -49.364 20.050  1.00 86.74  ? 108 GLU B OE2 1 
ATOM   2843 N  N   . GLY B 1 109 ? -20.191 -48.865 22.372  1.00 86.43  ? 109 GLY B N   1 
ATOM   2844 C  CA  . GLY B 1 109 ? -19.161 -49.033 21.330  1.00 90.57  ? 109 GLY B CA  1 
ATOM   2845 C  C   . GLY B 1 109 ? -19.083 -50.463 20.813  1.00 94.15  ? 109 GLY B C   1 
ATOM   2846 O  O   . GLY B 1 109 ? -17.954 -50.923 20.538  1.00 94.38  ? 109 GLY B O   1 
ATOM   2847 N  N   . ASP B 1 110 ? -20.230 -51.123 20.619  1.00 94.35  ? 110 ASP B N   1 
ATOM   2848 C  CA  . ASP B 1 110 ? -20.302 -52.534 20.147  1.00 93.79  ? 110 ASP B CA  1 
ATOM   2849 C  C   . ASP B 1 110 ? -20.360 -52.541 18.614  1.00 89.08  ? 110 ASP B C   1 
ATOM   2850 O  O   . ASP B 1 110 ? -19.527 -53.241 17.998  1.00 84.81  ? 110 ASP B O   1 
ATOM   2851 C  CB  . ASP B 1 110 ? -21.480 -53.268 20.789  1.00 100.13 ? 110 ASP B CB  1 
ATOM   2852 C  CG  . ASP B 1 110 ? -21.407 -53.312 22.306  1.00 103.26 ? 110 ASP B CG  1 
ATOM   2853 O  OD1 . ASP B 1 110 ? -21.626 -52.256 22.941  1.00 101.74 ? 110 ASP B OD1 1 
ATOM   2854 O  OD2 . ASP B 1 110 ? -21.121 -54.401 22.842  1.00 105.99 ? 110 ASP B OD2 1 
ATOM   2855 N  N   . TRP B 1 111 ? -21.287 -51.764 18.037  1.00 88.38  ? 111 TRP B N   1 
ATOM   2856 C  CA  . TRP B 1 111 ? -21.391 -51.467 16.579  1.00 88.54  ? 111 TRP B CA  1 
ATOM   2857 C  C   . TRP B 1 111 ? -19.996 -51.205 15.995  1.00 89.38  ? 111 TRP B C   1 
ATOM   2858 O  O   . TRP B 1 111 ? -19.781 -51.496 14.796  1.00 88.76  ? 111 TRP B O   1 
ATOM   2859 C  CB  . TRP B 1 111 ? -22.300 -50.255 16.341  1.00 85.74  ? 111 TRP B CB  1 
ATOM   2860 C  CG  . TRP B 1 111 ? -21.709 -48.966 16.828  1.00 84.29  ? 111 TRP B CG  1 
ATOM   2861 C  CD1 . TRP B 1 111 ? -21.672 -48.520 18.116  1.00 84.79  ? 111 TRP B CD1 1 
ATOM   2862 C  CD2 . TRP B 1 111 ? -21.044 -47.958 16.041  1.00 84.19  ? 111 TRP B CD2 1 
ATOM   2863 N  NE1 . TRP B 1 111 ? -21.056 -47.298 18.181  1.00 82.40  ? 111 TRP B NE1 1 
ATOM   2864 C  CE2 . TRP B 1 111 ? -20.655 -46.930 16.927  1.00 80.03  ? 111 TRP B CE2 1 
ATOM   2865 C  CE3 . TRP B 1 111 ? -20.757 -47.809 14.678  1.00 81.72  ? 111 TRP B CE3 1 
ATOM   2866 C  CZ2 . TRP B 1 111 ? -19.983 -45.789 16.491  1.00 77.23  ? 111 TRP B CZ2 1 
ATOM   2867 C  CZ3 . TRP B 1 111 ? -20.096 -46.678 14.250  1.00 76.50  ? 111 TRP B CZ3 1 
ATOM   2868 C  CH2 . TRP B 1 111 ? -19.718 -45.681 15.146  1.00 75.45  ? 111 TRP B CH2 1 
ATOM   2869 N  N   . LEU B 1 112 ? -19.106 -50.633 16.809  1.00 88.93  ? 112 LEU B N   1 
ATOM   2870 C  CA  . LEU B 1 112 ? -17.706 -50.309 16.439  1.00 90.21  ? 112 LEU B CA  1 
ATOM   2871 C  C   . LEU B 1 112 ? -16.855 -51.586 16.427  1.00 93.02  ? 112 LEU B C   1 
ATOM   2872 O  O   . LEU B 1 112 ? -16.102 -51.782 15.452  1.00 89.79  ? 112 LEU B O   1 
ATOM   2873 C  CB  . LEU B 1 112 ? -17.165 -49.290 17.447  1.00 90.55  ? 112 LEU B CB  1 
ATOM   2874 C  CG  . LEU B 1 112 ? -16.278 -48.199 16.856  1.00 91.06  ? 112 LEU B CG  1 
ATOM   2875 C  CD1 . LEU B 1 112 ? -16.956 -47.548 15.658  1.00 93.90  ? 112 LEU B CD1 1 
ATOM   2876 C  CD2 . LEU B 1 112 ? -15.925 -47.172 17.916  1.00 90.23  ? 112 LEU B CD2 1 
ATOM   2877 N  N   . LYS B 1 113 ? -16.964 -52.412 17.473  1.00 95.51  ? 113 LYS B N   1 
ATOM   2878 C  CA  . LYS B 1 113 ? -16.216 -53.694 17.601  1.00 97.53  ? 113 LYS B CA  1 
ATOM   2879 C  C   . LYS B 1 113 ? -16.579 -54.607 16.426  1.00 94.13  ? 113 LYS B C   1 
ATOM   2880 O  O   . LYS B 1 113 ? -15.650 -55.175 15.813  1.00 93.95  ? 113 LYS B O   1 
ATOM   2881 C  CB  . LYS B 1 113 ? -16.504 -54.391 18.934  1.00 109.07 ? 113 LYS B CB  1 
ATOM   2882 C  CG  . LYS B 1 113 ? -15.429 -55.389 19.356  1.00 117.76 ? 113 LYS B CG  1 
ATOM   2883 C  CD  . LYS B 1 113 ? -15.906 -56.504 20.266  1.00 119.79 ? 113 LYS B CD  1 
ATOM   2884 C  CE  . LYS B 1 113 ? -16.355 -57.737 19.509  1.00 119.53 ? 113 LYS B CE  1 
ATOM   2885 N  NZ  . LYS B 1 113 ? -16.703 -58.844 20.431  1.00 119.69 ? 113 LYS B NZ  1 
ATOM   2886 N  N   . VAL B 1 114 ? -17.874 -54.698 16.100  1.00 90.01  ? 114 VAL B N   1 
ATOM   2887 C  CA  . VAL B 1 114 ? -18.421 -55.642 15.077  1.00 83.28  ? 114 VAL B CA  1 
ATOM   2888 C  C   . VAL B 1 114 ? -17.937 -55.231 13.677  1.00 79.91  ? 114 VAL B C   1 
ATOM   2889 O  O   . VAL B 1 114 ? -17.975 -56.096 12.788  1.00 87.77  ? 114 VAL B O   1 
ATOM   2890 C  CB  . VAL B 1 114 ? -19.963 -55.762 15.143  1.00 80.95  ? 114 VAL B CB  1 
ATOM   2891 C  CG1 . VAL B 1 114 ? -20.459 -56.101 16.541  1.00 82.67  ? 114 VAL B CG1 1 
ATOM   2892 C  CG2 . VAL B 1 114 ? -20.681 -54.530 14.626  1.00 79.99  ? 114 VAL B CG2 1 
ATOM   2893 N  N   . ARG B 1 115 ? -17.482 -53.985 13.483  1.00 72.41  ? 115 ARG B N   1 
ATOM   2894 C  CA  . ARG B 1 115 ? -17.250 -53.389 12.136  1.00 69.27  ? 115 ARG B CA  1 
ATOM   2895 C  C   . ARG B 1 115 ? -15.756 -53.208 11.830  1.00 67.98  ? 115 ARG B C   1 
ATOM   2896 O  O   . ARG B 1 115 ? -15.436 -53.080 10.633  1.00 66.75  ? 115 ARG B O   1 
ATOM   2897 C  CB  . ARG B 1 115 ? -18.021 -52.070 12.018  1.00 66.82  ? 115 ARG B CB  1 
ATOM   2898 C  CG  . ARG B 1 115 ? -19.507 -52.280 11.769  1.00 67.87  ? 115 ARG B CG  1 
ATOM   2899 C  CD  . ARG B 1 115 ? -20.331 -51.014 11.704  1.00 69.46  ? 115 ARG B CD  1 
ATOM   2900 N  NE  . ARG B 1 115 ? -21.725 -51.297 11.375  1.00 71.94  ? 115 ARG B NE  1 
ATOM   2901 C  CZ  . ARG B 1 115 ? -22.632 -51.810 12.213  1.00 73.96  ? 115 ARG B CZ  1 
ATOM   2902 N  NH1 . ARG B 1 115 ? -22.311 -52.107 13.462  1.00 73.68  ? 115 ARG B NH1 1 
ATOM   2903 N  NH2 . ARG B 1 115 ? -23.871 -52.021 11.796  1.00 72.94  ? 115 ARG B NH2 1 
ATOM   2904 N  N   . PHE B 1 116 ? -14.870 -53.203 12.832  1.00 68.22  ? 116 PHE B N   1 
ATOM   2905 C  CA  . PHE B 1 116 ? -13.435 -52.854 12.649  1.00 69.96  ? 116 PHE B CA  1 
ATOM   2906 C  C   . PHE B 1 116 ? -12.503 -53.752 13.460  1.00 69.83  ? 116 PHE B C   1 
ATOM   2907 O  O   . PHE B 1 116 ? -12.891 -54.240 14.532  1.00 69.23  ? 116 PHE B O   1 
ATOM   2908 C  CB  . PHE B 1 116 ? -13.157 -51.416 13.085  1.00 72.82  ? 116 PHE B CB  1 
ATOM   2909 C  CG  . PHE B 1 116 ? -13.866 -50.373 12.267  1.00 75.76  ? 116 PHE B CG  1 
ATOM   2910 C  CD1 . PHE B 1 116 ? -15.196 -50.065 12.500  1.00 78.77  ? 116 PHE B CD1 1 
ATOM   2911 C  CD2 . PHE B 1 116 ? -13.190 -49.686 11.271  1.00 77.90  ? 116 PHE B CD2 1 
ATOM   2912 C  CE1 . PHE B 1 116 ? -15.840 -49.098 11.743  1.00 80.15  ? 116 PHE B CE1 1 
ATOM   2913 C  CE2 . PHE B 1 116 ? -13.834 -48.720 10.516  1.00 80.46  ? 116 PHE B CE2 1 
ATOM   2914 C  CZ  . PHE B 1 116 ? -15.159 -48.429 10.752  1.00 81.35  ? 116 PHE B CZ  1 
ATOM   2915 N  N   . ASN B 1 117 ? -11.284 -53.913 12.947  1.00 72.64  ? 117 ASN B N   1 
ATOM   2916 C  CA  . ASN B 1 117 ? -10.108 -54.419 13.695  1.00 76.55  ? 117 ASN B CA  1 
ATOM   2917 C  C   . ASN B 1 117 ? -9.309  -53.204 14.176  1.00 76.89  ? 117 ASN B C   1 
ATOM   2918 O  O   . ASN B 1 117 ? -8.794  -52.461 13.315  1.00 80.08  ? 117 ASN B O   1 
ATOM   2919 C  CB  . ASN B 1 117 ? -9.254  -55.352 12.837  1.00 80.24  ? 117 ASN B CB  1 
ATOM   2920 C  CG  . ASN B 1 117 ? -7.883  -55.577 13.436  1.00 85.58  ? 117 ASN B CG  1 
ATOM   2921 O  OD1 . ASN B 1 117 ? -7.751  -55.751 14.644  1.00 95.24  ? 117 ASN B OD1 1 
ATOM   2922 N  ND2 . ASN B 1 117 ? -6.859  -55.567 12.604  1.00 88.54  ? 117 ASN B ND2 1 
ATOM   2923 N  N   . PHE B 1 118 ? -9.193  -53.030 15.495  1.00 79.47  ? 118 PHE B N   1 
ATOM   2924 C  CA  . PHE B 1 118 ? -8.748  -51.773 16.155  1.00 84.75  ? 118 PHE B CA  1 
ATOM   2925 C  C   . PHE B 1 118 ? -7.224  -51.615 16.155  1.00 85.88  ? 118 PHE B C   1 
ATOM   2926 O  O   . PHE B 1 118 ? -6.753  -50.526 16.550  1.00 85.78  ? 118 PHE B O   1 
ATOM   2927 C  CB  . PHE B 1 118 ? -9.228  -51.722 17.604  1.00 86.76  ? 118 PHE B CB  1 
ATOM   2928 C  CG  . PHE B 1 118 ? -10.723 -51.711 17.762  1.00 92.06  ? 118 PHE B CG  1 
ATOM   2929 C  CD1 . PHE B 1 118 ? -11.437 -50.529 17.652  1.00 95.47  ? 118 PHE B CD1 1 
ATOM   2930 C  CD2 . PHE B 1 118 ? -11.416 -52.883 18.021  1.00 97.84  ? 118 PHE B CD2 1 
ATOM   2931 C  CE1 . PHE B 1 118 ? -12.818 -50.524 17.781  1.00 100.08 ? 118 PHE B CE1 1 
ATOM   2932 C  CE2 . PHE B 1 118 ? -12.796 -52.875 18.156  1.00 99.77  ? 118 PHE B CE2 1 
ATOM   2933 C  CZ  . PHE B 1 118 ? -13.496 -51.696 18.033  1.00 100.63 ? 118 PHE B CZ  1 
ATOM   2934 N  N   . GLN B 1 119 ? -6.470  -52.647 15.770  1.00 85.38  ? 119 GLN B N   1 
ATOM   2935 C  CA  . GLN B 1 119 ? -4.983  -52.567 15.734  1.00 86.12  ? 119 GLN B CA  1 
ATOM   2936 C  C   . GLN B 1 119 ? -4.542  -52.309 14.293  1.00 83.25  ? 119 GLN B C   1 
ATOM   2937 O  O   . GLN B 1 119 ? -3.341  -52.051 14.093  1.00 79.87  ? 119 GLN B O   1 
ATOM   2938 C  CB  . GLN B 1 119 ? -4.331  -53.800 16.370  1.00 89.86  ? 119 GLN B CB  1 
ATOM   2939 C  CG  . GLN B 1 119 ? -4.919  -55.138 15.944  1.00 92.61  ? 119 GLN B CG  1 
ATOM   2940 C  CD  . GLN B 1 119 ? -4.386  -56.270 16.789  1.00 95.41  ? 119 GLN B CD  1 
ATOM   2941 O  OE1 . GLN B 1 119 ? -3.918  -56.072 17.909  1.00 92.72  ? 119 GLN B OE1 1 
ATOM   2942 N  NE2 . GLN B 1 119 ? -4.463  -57.479 16.256  1.00 98.30  ? 119 GLN B NE2 1 
ATOM   2943 N  N   . GLU B 1 120 ? -5.480  -52.338 13.339  1.00 82.82  ? 120 GLU B N   1 
ATOM   2944 C  CA  . GLU B 1 120 ? -5.270  -51.717 12.005  1.00 83.87  ? 120 GLU B CA  1 
ATOM   2945 C  C   . GLU B 1 120 ? -5.240  -50.200 12.198  1.00 78.88  ? 120 GLU B C   1 
ATOM   2946 O  O   . GLU B 1 120 ? -5.780  -49.726 13.211  1.00 78.45  ? 120 GLU B O   1 
ATOM   2947 C  CB  . GLU B 1 120 ? -6.330  -52.137 10.986  1.00 89.25  ? 120 GLU B CB  1 
ATOM   2948 C  CG  . GLU B 1 120 ? -5.839  -53.242 10.063  1.00 94.43  ? 120 GLU B CG  1 
ATOM   2949 C  CD  . GLU B 1 120 ? -6.908  -53.934 9.234   1.00 102.89 ? 120 GLU B CD  1 
ATOM   2950 O  OE1 . GLU B 1 120 ? -6.594  -54.352 8.096   1.00 107.57 ? 120 GLU B OE1 1 
ATOM   2951 O  OE2 . GLU B 1 120 ? -8.048  -54.068 9.729   1.00 110.30 ? 120 GLU B OE2 1 
ATOM   2952 N  N   . ILE B 1 121 ? -4.619  -49.489 11.256  1.00 77.60  ? 121 ILE B N   1 
ATOM   2953 C  CA  . ILE B 1 121 ? -4.588  -48.002 11.206  1.00 72.04  ? 121 ILE B CA  1 
ATOM   2954 C  C   . ILE B 1 121 ? -5.840  -47.529 10.466  1.00 69.17  ? 121 ILE B C   1 
ATOM   2955 O  O   . ILE B 1 121 ? -5.879  -47.655 9.226   1.00 72.37  ? 121 ILE B O   1 
ATOM   2956 C  CB  . ILE B 1 121 ? -3.304  -47.480 10.539  1.00 70.27  ? 121 ILE B CB  1 
ATOM   2957 C  CG1 . ILE B 1 121 ? -2.044  -47.954 11.262  1.00 69.27  ? 121 ILE B CG1 1 
ATOM   2958 C  CG2 . ILE B 1 121 ? -3.349  -45.966 10.433  1.00 69.34  ? 121 ILE B CG2 1 
ATOM   2959 C  CD1 . ILE B 1 121 ? -0.803  -47.919 10.395  1.00 69.28  ? 121 ILE B CD1 1 
ATOM   2960 N  N   . PHE B 1 122 ? -6.840  -47.059 11.205  1.00 65.47  ? 122 PHE B N   1 
ATOM   2961 C  CA  . PHE B 1 122 ? -7.976  -46.284 10.648  1.00 64.69  ? 122 PHE B CA  1 
ATOM   2962 C  C   . PHE B 1 122 ? -8.327  -45.135 11.596  1.00 60.94  ? 122 PHE B C   1 
ATOM   2963 O  O   . PHE B 1 122 ? -8.152  -45.271 12.824  1.00 63.43  ? 122 PHE B O   1 
ATOM   2964 C  CB  . PHE B 1 122 ? -9.199  -47.172 10.399  1.00 67.42  ? 122 PHE B CB  1 
ATOM   2965 C  CG  . PHE B 1 122 ? -9.912  -47.613 11.648  1.00 70.12  ? 122 PHE B CG  1 
ATOM   2966 C  CD1 . PHE B 1 122 ? -10.797 -46.760 12.294  1.00 71.76  ? 122 PHE B CD1 1 
ATOM   2967 C  CD2 . PHE B 1 122 ? -9.680  -48.865 12.192  1.00 73.37  ? 122 PHE B CD2 1 
ATOM   2968 C  CE1 . PHE B 1 122 ? -11.436 -47.152 13.458  1.00 71.35  ? 122 PHE B CE1 1 
ATOM   2969 C  CE2 . PHE B 1 122 ? -10.321 -49.256 13.356  1.00 74.74  ? 122 PHE B CE2 1 
ATOM   2970 C  CZ  . PHE B 1 122 ? -11.201 -48.401 13.983  1.00 72.83  ? 122 PHE B CZ  1 
ATOM   2971 N  N   . VAL B 1 123 ? -8.809  -44.038 11.012  1.00 58.43  ? 123 VAL B N   1 
ATOM   2972 C  CA  . VAL B 1 123 ? -9.557  -42.950 11.700  1.00 55.43  ? 123 VAL B CA  1 
ATOM   2973 C  C   . VAL B 1 123 ? -10.985 -42.987 11.159  1.00 51.39  ? 123 VAL B C   1 
ATOM   2974 O  O   . VAL B 1 123 ? -11.181 -43.447 10.019  1.00 49.25  ? 123 VAL B O   1 
ATOM   2975 C  CB  . VAL B 1 123 ? -8.906  -41.570 11.479  1.00 57.78  ? 123 VAL B CB  1 
ATOM   2976 C  CG1 . VAL B 1 123 ? -9.754  -40.439 12.042  1.00 57.53  ? 123 VAL B CG1 1 
ATOM   2977 C  CG2 . VAL B 1 123 ? -7.505  -41.510 12.064  1.00 59.67  ? 123 VAL B CG2 1 
ATOM   2978 N  N   . LEU B 1 124 ? -11.942 -42.538 11.966  1.00 50.88  ? 124 LEU B N   1 
ATOM   2979 C  CA  . LEU B 1 124 ? -13.344 -42.317 11.538  1.00 49.14  ? 124 LEU B CA  1 
ATOM   2980 C  C   . LEU B 1 124 ? -13.775 -40.920 11.989  1.00 49.56  ? 124 LEU B C   1 
ATOM   2981 O  O   . LEU B 1 124 ? -13.953 -40.713 13.201  1.00 48.46  ? 124 LEU B O   1 
ATOM   2982 C  CB  . LEU B 1 124 ? -14.235 -43.401 12.143  1.00 47.61  ? 124 LEU B CB  1 
ATOM   2983 C  CG  . LEU B 1 124 ? -15.735 -43.135 12.051  1.00 47.65  ? 124 LEU B CG  1 
ATOM   2984 C  CD1 . LEU B 1 124 ? -16.167 -42.864 10.622  1.00 48.10  ? 124 LEU B CD1 1 
ATOM   2985 C  CD2 . LEU B 1 124 ? -16.512 -44.308 12.613  1.00 48.99  ? 124 LEU B CD2 1 
ATOM   2986 N  N   . ARG B 1 125 ? -14.038 -40.062 11.020  1.00 48.85  ? 125 ARG B N   1 
ATOM   2987 C  CA  . ARG B 1 125 ? -14.516 -38.739 11.316  1.00 46.50  ? 125 ARG B CA  1 
ATOM   2988 C  C   . ARG B 1 125 ? -15.993 -38.752 11.564  1.00 44.21  ? 125 ARG B C   1 
ATOM   2989 O  O   . ARG B 1 125 ? -16.747 -39.357 10.830  1.00 43.49  ? 125 ARG B O   1 
ATOM   2990 C  CB  . ARG B 1 125 ? -14.168 -37.790 10.183  1.00 48.04  ? 125 ARG B CB  1 
ATOM   2991 C  CG  . ARG B 1 125 ? -12.798 -37.168 10.312  1.00 48.42  ? 125 ARG B CG  1 
ATOM   2992 C  CD  . ARG B 1 125 ? -12.556 -36.192 9.184   1.00 51.00  ? 125 ARG B CD  1 
ATOM   2993 N  NE  . ARG B 1 125 ? -13.778 -35.505 8.807   1.00 51.89  ? 125 ARG B NE  1 
ATOM   2994 C  CZ  . ARG B 1 125 ? -14.032 -34.236 9.089   1.00 53.93  ? 125 ARG B CZ  1 
ATOM   2995 N  NH1 . ARG B 1 125 ? -13.147 -33.508 9.744   1.00 55.05  ? 125 ARG B NH1 1 
ATOM   2996 N  NH2 . ARG B 1 125 ? -15.167 -33.695 8.705   1.00 54.19  ? 125 ARG B NH2 1 
ATOM   2997 N  N   . LEU B 1 126 ? -16.396 -38.072 12.601  1.00 46.29  ? 126 LEU B N   1 
ATOM   2998 C  CA  . LEU B 1 126 ? -17.814 -37.998 13.036  1.00 48.97  ? 126 LEU B CA  1 
ATOM   2999 C  C   . LEU B 1 126 ? -18.363 -36.612 12.689  1.00 50.73  ? 126 LEU B C   1 
ATOM   3000 O  O   . LEU B 1 126 ? -19.586 -36.476 12.536  1.00 48.85  ? 126 LEU B O   1 
ATOM   3001 C  CB  . LEU B 1 126 ? -17.847 -38.261 14.544  1.00 48.90  ? 126 LEU B CB  1 
ATOM   3002 C  CG  . LEU B 1 126 ? -17.118 -39.530 14.994  1.00 49.61  ? 126 LEU B CG  1 
ATOM   3003 C  CD1 . LEU B 1 126 ? -16.654 -39.434 16.436  1.00 50.33  ? 126 LEU B CD1 1 
ATOM   3004 C  CD2 . LEU B 1 126 ? -17.991 -40.756 14.806  1.00 50.20  ? 126 LEU B CD2 1 
ATOM   3005 N  N   . GLU B 1 127 ? -17.466 -35.628 12.626  1.00 54.55  ? 127 GLU B N   1 
ATOM   3006 C  CA  . GLU B 1 127 ? -17.745 -34.208 12.300  1.00 55.30  ? 127 GLU B CA  1 
ATOM   3007 C  C   . GLU B 1 127 ? -18.165 -34.092 10.831  1.00 53.61  ? 127 GLU B C   1 
ATOM   3008 O  O   . GLU B 1 127 ? -17.679 -34.875 10.018  1.00 56.48  ? 127 GLU B O   1 
ATOM   3009 C  CB  . GLU B 1 127 ? -16.496 -33.357 12.558  1.00 56.44  ? 127 GLU B CB  1 
ATOM   3010 C  CG  . GLU B 1 127 ? -16.795 -31.875 12.675  1.00 56.68  ? 127 GLU B CG  1 
ATOM   3011 C  CD  . GLU B 1 127 ? -15.588 -30.959 12.592  1.00 56.17  ? 127 GLU B CD  1 
ATOM   3012 O  OE1 . GLU B 1 127 ? -15.776 -29.775 12.233  1.00 54.51  ? 127 GLU B OE1 1 
ATOM   3013 O  OE2 . GLU B 1 127 ? -14.468 -31.427 12.907  1.00 56.62  ? 127 GLU B OE2 1 
ATOM   3014 N  N   . THR B 1 128 ? -19.012 -33.115 10.513  1.00 51.39  ? 128 THR B N   1 
ATOM   3015 C  CA  . THR B 1 128 ? -19.240 -32.579 9.147   1.00 50.91  ? 128 THR B CA  1 
ATOM   3016 C  C   . THR B 1 128 ? -17.921 -32.047 8.581   1.00 52.00  ? 128 THR B C   1 
ATOM   3017 O  O   . THR B 1 128 ? -16.921 -32.136 9.272   1.00 56.19  ? 128 THR B O   1 
ATOM   3018 C  CB  . THR B 1 128 ? -20.263 -31.443 9.197   1.00 51.14  ? 128 THR B CB  1 
ATOM   3019 O  OG1 . THR B 1 128 ? -19.646 -30.401 9.955   1.00 49.56  ? 128 THR B OG1 1 
ATOM   3020 C  CG2 . THR B 1 128 ? -21.569 -31.875 9.830   1.00 53.29  ? 128 THR B CG2 1 
ATOM   3021 N  N   . PHE B 1 129 ? -17.925 -31.487 7.373   1.00 52.27  ? 129 PHE B N   1 
ATOM   3022 C  CA  . PHE B 1 129 ? -16.737 -30.839 6.759   1.00 50.69  ? 129 PHE B CA  1 
ATOM   3023 C  C   . PHE B 1 129 ? -16.692 -29.351 7.116   1.00 50.74  ? 129 PHE B C   1 
ATOM   3024 O  O   . PHE B 1 129 ? -17.743 -28.677 7.197   1.00 48.76  ? 129 PHE B O   1 
ATOM   3025 C  CB  . PHE B 1 129 ? -16.720 -31.051 5.248   1.00 50.47  ? 129 PHE B CB  1 
ATOM   3026 C  CG  . PHE B 1 129 ? -16.538 -32.498 4.892   1.00 49.86  ? 129 PHE B CG  1 
ATOM   3027 C  CD1 . PHE B 1 129 ? -15.319 -33.121 5.094   1.00 50.99  ? 129 PHE B CD1 1 
ATOM   3028 C  CD2 . PHE B 1 129 ? -17.597 -33.251 4.423   1.00 50.18  ? 129 PHE B CD2 1 
ATOM   3029 C  CE1 . PHE B 1 129 ? -15.146 -34.459 4.777   1.00 51.82  ? 129 PHE B CE1 1 
ATOM   3030 C  CE2 . PHE B 1 129 ? -17.423 -34.589 4.108   1.00 51.66  ? 129 PHE B CE2 1 
ATOM   3031 C  CZ  . PHE B 1 129 ? -16.198 -35.190 4.281   1.00 51.44  ? 129 PHE B CZ  1 
ATOM   3032 N  N   . LEU B 1 130 ? -15.466 -28.841 7.241   1.00 52.18  ? 130 LEU B N   1 
ATOM   3033 C  CA  . LEU B 1 130 ? -15.149 -27.428 7.570   1.00 54.33  ? 130 LEU B CA  1 
ATOM   3034 C  C   . LEU B 1 130 ? -14.945 -26.655 6.258   1.00 52.71  ? 130 LEU B C   1 
ATOM   3035 O  O   . LEU B 1 130 ? -14.196 -27.149 5.384   1.00 52.80  ? 130 LEU B O   1 
ATOM   3036 C  CB  . LEU B 1 130 ? -13.896 -27.433 8.454   1.00 58.63  ? 130 LEU B CB  1 
ATOM   3037 C  CG  . LEU B 1 130 ? -13.731 -26.263 9.425   1.00 60.71  ? 130 LEU B CG  1 
ATOM   3038 C  CD1 . LEU B 1 130 ? -12.724 -26.607 10.515  1.00 61.82  ? 130 LEU B CD1 1 
ATOM   3039 C  CD2 . LEU B 1 130 ? -13.307 -25.000 8.689   1.00 65.24  ? 130 LEU B CD2 1 
HETATM 3040 N  N   . MSE B 1 131 ? -15.655 -25.530 6.104   1.00 50.29  ? 131 MSE B N   1 
HETATM 3041 C  CA  . MSE B 1 131 ? -15.505 -24.557 4.983   1.00 46.32  ? 131 MSE B CA  1 
HETATM 3042 C  C   . MSE B 1 131 ? -14.962 -23.255 5.564   1.00 44.27  ? 131 MSE B C   1 
HETATM 3043 O  O   . MSE B 1 131 ? -15.429 -22.822 6.614   1.00 45.92  ? 131 MSE B O   1 
HETATM 3044 C  CB  . MSE B 1 131 ? -16.842 -24.240 4.299   1.00 44.59  ? 131 MSE B CB  1 
HETATM 3045 C  CG  . MSE B 1 131 ? -17.510 -25.393 3.586   1.00 43.68  ? 131 MSE B CG  1 
HETATM 3046 SE SE  . MSE B 1 131 ? -16.382 -26.342 2.288   1.00 44.47  ? 131 MSE B SE  1 
HETATM 3047 C  CE  . MSE B 1 131 ? -16.624 -28.192 2.897   1.00 48.06  ? 131 MSE B CE  1 
ATOM   3048 N  N   . PRO B 1 132 ? -14.008 -22.557 4.909   1.00 42.09  ? 132 PRO B N   1 
ATOM   3049 C  CA  . PRO B 1 132 ? -13.487 -22.951 3.607   1.00 42.08  ? 132 PRO B CA  1 
ATOM   3050 C  C   . PRO B 1 132 ? -12.445 -24.056 3.767   1.00 41.37  ? 132 PRO B C   1 
ATOM   3051 O  O   . PRO B 1 132 ? -11.938 -24.194 4.834   1.00 46.13  ? 132 PRO B O   1 
ATOM   3052 C  CB  . PRO B 1 132 ? -12.797 -21.698 3.054   1.00 42.48  ? 132 PRO B CB  1 
ATOM   3053 C  CG  . PRO B 1 132 ? -12.926 -20.632 4.133   1.00 42.84  ? 132 PRO B CG  1 
ATOM   3054 C  CD  . PRO B 1 132 ? -13.369 -21.331 5.399   1.00 42.35  ? 132 PRO B CD  1 
ATOM   3055 N  N   . VAL B 1 133 ? -12.123 -24.766 2.693   1.00 43.04  ? 133 VAL B N   1 
ATOM   3056 C  CA  . VAL B 1 133 ? -11.066 -25.815 2.688   1.00 45.94  ? 133 VAL B CA  1 
ATOM   3057 C  C   . VAL B 1 133 ? -9.718  -25.163 2.357   1.00 48.96  ? 133 VAL B C   1 
ATOM   3058 O  O   . VAL B 1 133 ? -8.803  -25.294 3.186   1.00 53.76  ? 133 VAL B O   1 
ATOM   3059 C  CB  . VAL B 1 133 ? -11.435 -26.955 1.724   1.00 48.10  ? 133 VAL B CB  1 
ATOM   3060 C  CG1 . VAL B 1 133 ? -10.226 -27.766 1.283   1.00 48.74  ? 133 VAL B CG1 1 
ATOM   3061 C  CG2 . VAL B 1 133 ? -12.499 -27.849 2.340   1.00 49.54  ? 133 VAL B CG2 1 
ATOM   3062 N  N   . GLN B 1 134 ? -9.603  -24.496 1.200   1.00 49.87  ? 134 GLN B N   1 
ATOM   3063 C  CA  . GLN B 1 134 ? -8.357  -23.811 0.744   1.00 50.08  ? 134 GLN B CA  1 
ATOM   3064 C  C   . GLN B 1 134 ? -8.462  -22.308 1.006   1.00 50.10  ? 134 GLN B C   1 
ATOM   3065 O  O   . GLN B 1 134 ? -9.501  -21.736 0.654   1.00 50.47  ? 134 GLN B O   1 
ATOM   3066 C  CB  . GLN B 1 134 ? -8.128  -24.024 -0.751  1.00 48.63  ? 134 GLN B CB  1 
ATOM   3067 C  CG  . GLN B 1 134 ? -6.781  -23.513 -1.237  1.00 48.64  ? 134 GLN B CG  1 
ATOM   3068 C  CD  . GLN B 1 134 ? -5.670  -24.504 -0.993  1.00 51.61  ? 134 GLN B CD  1 
ATOM   3069 O  OE1 . GLN B 1 134 ? -5.622  -25.577 -1.603  1.00 51.03  ? 134 GLN B OE1 1 
ATOM   3070 N  NE2 . GLN B 1 134 ? -4.740  -24.136 -0.121  1.00 56.41  ? 134 GLN B NE2 1 
ATOM   3071 N  N   . LEU B 1 135 ? -7.399  -21.684 1.523   1.00 51.21  ? 135 LEU B N   1 
ATOM   3072 C  CA  . LEU B 1 135 ? -7.314  -20.205 1.634   1.00 54.83  ? 135 LEU B CA  1 
ATOM   3073 C  C   . LEU B 1 135 ? -6.495  -19.641 0.466   1.00 59.86  ? 135 LEU B C   1 
ATOM   3074 O  O   . LEU B 1 135 ? -5.488  -20.273 0.066   1.00 61.77  ? 135 LEU B O   1 
ATOM   3075 C  CB  . LEU B 1 135 ? -6.705  -19.819 2.982   1.00 54.88  ? 135 LEU B CB  1 
ATOM   3076 C  CG  . LEU B 1 135 ? -7.660  -19.870 4.174   1.00 54.02  ? 135 LEU B CG  1 
ATOM   3077 C  CD1 . LEU B 1 135 ? -6.888  -19.774 5.483   1.00 53.25  ? 135 LEU B CD1 1 
ATOM   3078 C  CD2 . LEU B 1 135 ? -8.709  -18.771 4.086   1.00 52.87  ? 135 LEU B CD2 1 
ATOM   3079 N  N   . GLU B 1 136 ? -6.952  -18.504 -0.067  1.00 62.91  ? 136 GLU B N   1 
ATOM   3080 C  CA  . GLU B 1 136 ? -6.328  -17.762 -1.191  1.00 65.28  ? 136 GLU B CA  1 
ATOM   3081 C  C   . GLU B 1 136 ? -5.905  -16.385 -0.681  1.00 69.50  ? 136 GLU B C   1 
ATOM   3082 O  O   . GLU B 1 136 ? -6.591  -15.856 0.205   1.00 71.08  ? 136 GLU B O   1 
ATOM   3083 C  CB  . GLU B 1 136 ? -7.318  -17.616 -2.346  1.00 64.39  ? 136 GLU B CB  1 
ATOM   3084 C  CG  . GLU B 1 136 ? -7.634  -18.926 -3.044  1.00 64.18  ? 136 GLU B CG  1 
ATOM   3085 C  CD  . GLU B 1 136 ? -8.647  -18.799 -4.168  1.00 65.06  ? 136 GLU B CD  1 
ATOM   3086 O  OE1 . GLU B 1 136 ? -9.464  -17.854 -4.112  1.00 63.70  ? 136 GLU B OE1 1 
ATOM   3087 O  OE2 . GLU B 1 136 ? -8.614  -19.636 -5.101  1.00 67.37  ? 136 GLU B OE2 1 
ATOM   3088 N  N   . LYS B 1 137 ? -4.825  -15.835 -1.239  1.00 75.50  ? 137 LYS B N   1 
ATOM   3089 C  CA  . LYS B 1 137 ? -4.209  -14.553 -0.811  1.00 78.25  ? 137 LYS B CA  1 
ATOM   3090 C  C   . LYS B 1 137 ? -4.108  -13.630 -2.026  1.00 77.05  ? 137 LYS B C   1 
ATOM   3091 O  O   . LYS B 1 137 ? -3.970  -14.143 -3.152  1.00 76.80  ? 137 LYS B O   1 
ATOM   3092 C  CB  . LYS B 1 137 ? -2.840  -14.837 -0.189  1.00 84.48  ? 137 LYS B CB  1 
ATOM   3093 C  CG  . LYS B 1 137 ? -2.119  -13.643 0.423   1.00 93.09  ? 137 LYS B CG  1 
ATOM   3094 C  CD  . LYS B 1 137 ? -0.726  -13.997 0.929   1.00 99.60  ? 137 LYS B CD  1 
ATOM   3095 C  CE  . LYS B 1 137 ? 0.290   -12.872 0.829   1.00 103.03 ? 137 LYS B CE  1 
ATOM   3096 N  NZ  . LYS B 1 137 ? 1.657   -13.382 0.557   1.00 102.24 ? 137 LYS B NZ  1 
ATOM   3097 N  N   . GLN B 1 138 ? -4.196  -12.322 -1.796  1.00 81.17  ? 138 GLN B N   1 
ATOM   3098 C  CA  . GLN B 1 138 ? -3.960  -11.274 -2.823  1.00 84.24  ? 138 GLN B CA  1 
ATOM   3099 C  C   . GLN B 1 138 ? -2.516  -11.401 -3.313  1.00 84.76  ? 138 GLN B C   1 
ATOM   3100 O  O   . GLN B 1 138 ? -1.656  -11.788 -2.506  1.00 85.54  ? 138 GLN B O   1 
ATOM   3101 C  CB  . GLN B 1 138 ? -4.209  -9.881  -2.246  1.00 90.37  ? 138 GLN B CB  1 
ATOM   3102 C  CG  . GLN B 1 138 ? -5.681  -9.518  -2.090  1.00 90.76  ? 138 GLN B CG  1 
ATOM   3103 C  CD  . GLN B 1 138 ? -6.383  -9.339  -3.415  1.00 91.35  ? 138 GLN B CD  1 
ATOM   3104 O  OE1 . GLN B 1 138 ? -6.297  -10.186 -4.300  1.00 90.83  ? 138 GLN B OE1 1 
ATOM   3105 N  NE2 . GLN B 1 138 ? -7.097  -8.231  -3.562  1.00 92.69  ? 138 GLN B NE2 1 
ATOM   3106 N  N   . THR B 1 139 ? -2.273  -11.075 -4.581  1.00 85.96  ? 139 THR B N   1 
ATOM   3107 C  CA  . THR B 1 139 ? -1.073  -11.494 -5.351  1.00 89.43  ? 139 THR B CA  1 
ATOM   3108 C  C   . THR B 1 139 ? -0.273  -10.279 -5.844  1.00 93.24  ? 139 THR B C   1 
ATOM   3109 O  O   . THR B 1 139 ? 0.959   -10.417 -6.015  1.00 94.36  ? 139 THR B O   1 
ATOM   3110 C  CB  . THR B 1 139 ? -1.506  -12.409 -6.502  1.00 91.36  ? 139 THR B CB  1 
ATOM   3111 O  OG1 . THR B 1 139 ? -0.348  -12.697 -7.286  1.00 97.22  ? 139 THR B OG1 1 
ATOM   3112 C  CG2 . THR B 1 139 ? -2.599  -11.802 -7.359  1.00 88.68  ? 139 THR B CG2 1 
ATOM   3113 N  N   . GLN B 1 140 ? -0.941  -9.151  -6.107  1.00 94.02  ? 140 GLN B N   1 
ATOM   3114 C  CA  . GLN B 1 140 ? -0.346  -7.923  -6.711  1.00 93.10  ? 140 GLN B CA  1 
ATOM   3115 C  C   . GLN B 1 140 ? 0.192   -8.252  -8.111  1.00 88.62  ? 140 GLN B C   1 
ATOM   3116 O  O   . GLN B 1 140 ? 1.387   -8.032  -8.380  1.00 81.94  ? 140 GLN B O   1 
ATOM   3117 C  CB  . GLN B 1 140 ? 0.731   -7.323  -5.805  1.00 96.04  ? 140 GLN B CB  1 
ATOM   3118 C  CG  . GLN B 1 140 ? 1.299   -6.014  -6.337  1.00 98.81  ? 140 GLN B CG  1 
ATOM   3119 C  CD  . GLN B 1 140 ? 1.535   -4.971  -5.271  1.00 101.14 ? 140 GLN B CD  1 
ATOM   3120 O  OE1 . GLN B 1 140 ? 1.481   -5.242  -4.071  1.00 97.60  ? 140 GLN B OE1 1 
ATOM   3121 N  NE2 . GLN B 1 140 ? 1.797   -3.753  -5.712  1.00 100.75 ? 140 GLN B NE2 1 
ATOM   3122 N  N   . ILE B 1 141 ? -0.684  -8.800  -8.950  1.00 86.39  ? 141 ILE B N   1 
ATOM   3123 C  CA  . ILE B 1 141 ? -0.481  -9.055  -10.403 1.00 84.81  ? 141 ILE B CA  1 
ATOM   3124 C  C   . ILE B 1 141 ? -1.804  -8.686  -11.054 1.00 82.50  ? 141 ILE B C   1 
ATOM   3125 O  O   . ILE B 1 141 ? -2.846  -9.106  -10.563 1.00 80.83  ? 141 ILE B O   1 
ATOM   3126 C  CB  . ILE B 1 141 ? -0.079  -10.527 -10.640 1.00 85.39  ? 141 ILE B CB  1 
ATOM   3127 C  CG1 . ILE B 1 141 ? 1.270   -10.834 -9.983  1.00 83.99  ? 141 ILE B CG1 1 
ATOM   3128 C  CG2 . ILE B 1 141 ? -0.088  -10.882 -12.123 1.00 86.27  ? 141 ILE B CG2 1 
ATOM   3129 C  CD1 . ILE B 1 141 ? 1.767   -12.246 -10.200 1.00 83.22  ? 141 ILE B CD1 1 
ATOM   3130 N  N   . PRO B 1 142 ? -1.798  -7.911  -12.160 1.00 84.86  ? 142 PRO B N   1 
ATOM   3131 C  CA  . PRO B 1 142 ? -3.012  -7.289  -12.692 1.00 87.68  ? 142 PRO B CA  1 
ATOM   3132 C  C   . PRO B 1 142 ? -4.073  -8.265  -13.189 1.00 85.06  ? 142 PRO B C   1 
ATOM   3133 O  O   . PRO B 1 142 ? -3.770  -9.165  -13.971 1.00 80.90  ? 142 PRO B O   1 
ATOM   3134 C  CB  . PRO B 1 142 ? -2.509  -6.463  -13.888 1.00 91.22  ? 142 PRO B CB  1 
ATOM   3135 C  CG  . PRO B 1 142 ? -1.208  -7.129  -14.287 1.00 91.22  ? 142 PRO B CG  1 
ATOM   3136 C  CD  . PRO B 1 142 ? -0.617  -7.617  -12.982 1.00 89.60  ? 142 PRO B CD  1 
ATOM   3137 N  N   . PRO B 1 143 ? -5.342  -8.119  -12.741 1.00 89.02  ? 143 PRO B N   1 
ATOM   3138 C  CA  . PRO B 1 143 ? -6.424  -8.999  -13.188 1.00 91.72  ? 143 PRO B CA  1 
ATOM   3139 C  C   . PRO B 1 143 ? -6.688  -8.927  -14.701 1.00 89.10  ? 143 PRO B C   1 
ATOM   3140 O  O   . PRO B 1 143 ? -7.308  -7.983  -15.142 1.00 88.47  ? 143 PRO B O   1 
ATOM   3141 C  CB  . PRO B 1 143 ? -7.653  -8.514  -12.401 1.00 94.46  ? 143 PRO B CB  1 
ATOM   3142 C  CG  . PRO B 1 143 ? -7.075  -7.762  -11.208 1.00 94.14  ? 143 PRO B CG  1 
ATOM   3143 C  CD  . PRO B 1 143 ? -5.780  -7.159  -11.714 1.00 91.93  ? 143 PRO B CD  1 
ATOM   3144 N  N   . PHE B 1 144 ? -6.217  -9.930  -15.450 1.00 84.81  ? 144 PHE B N   1 
ATOM   3145 C  CA  . PHE B 1 144 ? -6.424  -10.042 -16.915 1.00 85.49  ? 144 PHE B CA  1 
ATOM   3146 C  C   . PHE B 1 144 ? -7.821  -10.601 -17.189 1.00 87.43  ? 144 PHE B C   1 
ATOM   3147 O  O   . PHE B 1 144 ? -8.227  -11.568 -16.519 1.00 86.00  ? 144 PHE B O   1 
ATOM   3148 C  CB  . PHE B 1 144 ? -5.379  -10.935 -17.582 1.00 86.25  ? 144 PHE B CB  1 
ATOM   3149 C  CG  . PHE B 1 144 ? -5.539  -11.026 -19.079 1.00 86.07  ? 144 PHE B CG  1 
ATOM   3150 C  CD1 . PHE B 1 144 ? -5.611  -9.877  -19.853 1.00 86.65  ? 144 PHE B CD1 1 
ATOM   3151 C  CD2 . PHE B 1 144 ? -5.643  -12.255 -19.713 1.00 86.48  ? 144 PHE B CD2 1 
ATOM   3152 C  CE1 . PHE B 1 144 ? -5.779  -9.955  -21.226 1.00 88.76  ? 144 PHE B CE1 1 
ATOM   3153 C  CE2 . PHE B 1 144 ? -5.813  -12.332 -21.086 1.00 89.45  ? 144 PHE B CE2 1 
ATOM   3154 C  CZ  . PHE B 1 144 ? -5.880  -11.183 -21.840 1.00 91.55  ? 144 PHE B CZ  1 
ATOM   3155 N  N   . GLN B 1 145 ? -8.518  -10.000 -18.157 1.00 95.47  ? 145 GLN B N   1 
ATOM   3156 C  CA  . GLN B 1 145 ? -9.907  -10.345 -18.557 1.00 98.31  ? 145 GLN B CA  1 
ATOM   3157 C  C   . GLN B 1 145 ? -10.771 -10.491 -17.297 1.00 99.28  ? 145 GLN B C   1 
ATOM   3158 O  O   . GLN B 1 145 ? -11.400 -11.553 -17.129 1.00 102.81 ? 145 GLN B O   1 
ATOM   3159 C  CB  . GLN B 1 145 ? -9.902  -11.607 -19.419 1.00 100.06 ? 145 GLN B CB  1 
ATOM   3160 C  CG  . GLN B 1 145 ? -11.040 -11.652 -20.429 1.00 102.99 ? 145 GLN B CG  1 
ATOM   3161 C  CD  . GLN B 1 145 ? -10.770 -10.839 -21.678 1.00 102.92 ? 145 GLN B CD  1 
ATOM   3162 O  OE1 . GLN B 1 145 ? -9.717  -10.219 -21.838 1.00 98.02  ? 145 GLN B OE1 1 
ATOM   3163 N  NE2 . GLN B 1 145 ? -11.738 -10.830 -22.579 1.00 101.65 ? 145 GLN B NE2 1 
ATOM   3164 N  N   . GLN B 1 146 ? -10.774 -9.446  -16.460 1.00 97.64  ? 146 GLN B N   1 
ATOM   3165 C  CA  . GLN B 1 146 ? -11.568 -9.284  -15.206 1.00 94.99  ? 146 GLN B CA  1 
ATOM   3166 C  C   . GLN B 1 146 ? -11.479 -10.547 -14.333 1.00 91.11  ? 146 GLN B C   1 
ATOM   3167 O  O   . GLN B 1 146 ? -12.493 -10.897 -13.698 1.00 92.10  ? 146 GLN B O   1 
ATOM   3168 C  CB  . GLN B 1 146 ? -13.011 -8.863  -15.527 1.00 95.79  ? 146 GLN B CB  1 
ATOM   3169 C  CG  . GLN B 1 146 ? -13.864 -9.917  -16.232 1.00 98.64  ? 146 GLN B CG  1 
ATOM   3170 C  CD  . GLN B 1 146 ? -13.781 -9.867  -17.740 1.00 102.48 ? 146 GLN B CD  1 
ATOM   3171 O  OE1 . GLN B 1 146 ? -13.670 -8.800  -18.342 1.00 110.10 ? 146 GLN B OE1 1 
ATOM   3172 N  NE2 . GLN B 1 146 ? -13.843 -11.031 -18.371 1.00 98.96  ? 146 GLN B NE2 1 
ATOM   3173 N  N   . ARG B 1 147 ? -10.300 -11.175 -14.263 1.00 82.09  ? 147 ARG B N   1 
ATOM   3174 C  CA  . ARG B 1 147 ? -10.032 -12.388 -13.443 1.00 74.35  ? 147 ARG B CA  1 
ATOM   3175 C  C   . ARG B 1 147 ? -8.699  -12.209 -12.712 1.00 72.80  ? 147 ARG B C   1 
ATOM   3176 O  O   . ARG B 1 147 ? -7.677  -12.185 -13.406 1.00 71.63  ? 147 ARG B O   1 
ATOM   3177 C  CB  . ARG B 1 147 ? -9.940  -13.636 -14.328 1.00 70.08  ? 147 ARG B CB  1 
ATOM   3178 C  CG  . ARG B 1 147 ? -11.258 -14.120 -14.912 1.00 68.10  ? 147 ARG B CG  1 
ATOM   3179 C  CD  . ARG B 1 147 ? -11.003 -15.246 -15.884 1.00 69.50  ? 147 ARG B CD  1 
ATOM   3180 N  NE  . ARG B 1 147 ? -12.189 -16.016 -16.220 1.00 69.29  ? 147 ARG B NE  1 
ATOM   3181 C  CZ  . ARG B 1 147 ? -13.070 -15.692 -17.158 1.00 69.50  ? 147 ARG B CZ  1 
ATOM   3182 N  NH1 . ARG B 1 147 ? -12.931 -14.581 -17.864 1.00 69.89  ? 147 ARG B NH1 1 
ATOM   3183 N  NH2 . ARG B 1 147 ? -14.103 -16.485 -17.380 1.00 72.17  ? 147 ARG B NH2 1 
ATOM   3184 N  N   . ASP B 1 148 ? -8.700  -12.118 -11.378 1.00 77.41  ? 148 ASP B N   1 
ATOM   3185 C  CA  . ASP B 1 148 ? -7.459  -11.922 -10.574 1.00 82.96  ? 148 ASP B CA  1 
ATOM   3186 C  C   . ASP B 1 148 ? -6.716  -13.257 -10.456 1.00 79.55  ? 148 ASP B C   1 
ATOM   3187 O  O   . ASP B 1 148 ? -7.340  -14.312 -10.665 1.00 74.03  ? 148 ASP B O   1 
ATOM   3188 C  CB  . ASP B 1 148 ? -7.741  -11.306 -9.201  1.00 90.28  ? 148 ASP B CB  1 
ATOM   3189 C  CG  . ASP B 1 148 ? -6.543  -10.603 -8.567  1.00 97.28  ? 148 ASP B CG  1 
ATOM   3190 O  OD1 . ASP B 1 148 ? -5.396  -11.057 -8.793  1.00 100.54 ? 148 ASP B OD1 1 
ATOM   3191 O  OD2 . ASP B 1 148 ? -6.761  -9.596  -7.857  1.00 99.88  ? 148 ASP B OD2 1 
ATOM   3192 N  N   . ILE B 1 149 ? -5.412  -13.181 -10.175 1.00 78.67  ? 149 ILE B N   1 
ATOM   3193 C  CA  . ILE B 1 149 ? -4.472  -14.337 -10.108 1.00 79.83  ? 149 ILE B CA  1 
ATOM   3194 C  C   . ILE B 1 149 ? -4.032  -14.502 -8.650  1.00 75.82  ? 149 ILE B C   1 
ATOM   3195 O  O   . ILE B 1 149 ? -2.892  -14.149 -8.330  1.00 75.79  ? 149 ILE B O   1 
ATOM   3196 C  CB  . ILE B 1 149 ? -3.278  -14.135 -11.069 1.00 84.31  ? 149 ILE B CB  1 
ATOM   3197 C  CG1 . ILE B 1 149 ? -3.740  -13.923 -12.515 1.00 88.81  ? 149 ILE B CG1 1 
ATOM   3198 C  CG2 . ILE B 1 149 ? -2.286  -15.286 -10.963 1.00 84.60  ? 149 ILE B CG2 1 
ATOM   3199 C  CD1 . ILE B 1 149 ? -4.013  -12.478 -12.874 1.00 92.05  ? 149 ILE B CD1 1 
ATOM   3200 N  N   . ASP B 1 150 ? -4.920  -15.013 -7.803  1.00 71.11  ? 150 ASP B N   1 
ATOM   3201 C  CA  . ASP B 1 150 ? -4.659  -15.225 -6.354  1.00 65.28  ? 150 ASP B CA  1 
ATOM   3202 C  C   . ASP B 1 150 ? -3.573  -16.296 -6.203  1.00 60.16  ? 150 ASP B C   1 
ATOM   3203 O  O   . ASP B 1 150 ? -3.498  -17.195 -7.064  1.00 57.52  ? 150 ASP B O   1 
ATOM   3204 C  CB  . ASP B 1 150 ? -5.932  -15.636 -5.609  1.00 64.64  ? 150 ASP B CB  1 
ATOM   3205 C  CG  . ASP B 1 150 ? -7.130  -14.752 -5.904  1.00 65.64  ? 150 ASP B CG  1 
ATOM   3206 O  OD1 . ASP B 1 150 ? -7.023  -13.535 -5.647  1.00 64.58  ? 150 ASP B OD1 1 
ATOM   3207 O  OD2 . ASP B 1 150 ? -8.150  -15.289 -6.409  1.00 67.11  ? 150 ASP B OD2 1 
ATOM   3208 N  N   . ILE B 1 151 ? -2.774  -16.202 -5.139  1.00 57.38  ? 151 ILE B N   1 
ATOM   3209 C  CA  . ILE B 1 151 ? -1.825  -17.273 -4.716  1.00 58.75  ? 151 ILE B CA  1 
ATOM   3210 C  C   . ILE B 1 151 ? -2.520  -18.155 -3.673  1.00 60.62  ? 151 ILE B C   1 
ATOM   3211 O  O   . ILE B 1 151 ? -3.166  -17.597 -2.770  1.00 56.79  ? 151 ILE B O   1 
ATOM   3212 C  CB  . ILE B 1 151 ? -0.496  -16.706 -4.178  1.00 58.24  ? 151 ILE B CB  1 
ATOM   3213 C  CG1 . ILE B 1 151 ? 0.409   -17.833 -3.671  1.00 55.57  ? 151 ILE B CG1 1 
ATOM   3214 C  CG2 . ILE B 1 151 ? -0.720  -15.662 -3.098  1.00 60.20  ? 151 ILE B CG2 1 
ATOM   3215 C  CD1 . ILE B 1 151 ? 1.852   -17.428 -3.465  1.00 55.46  ? 151 ILE B CD1 1 
ATOM   3216 N  N   . LEU B 1 152 ? -2.369  -19.477 -3.813  1.00 64.49  ? 152 LEU B N   1 
ATOM   3217 C  CA  . LEU B 1 152 ? -2.925  -20.527 -2.915  1.00 62.97  ? 152 LEU B CA  1 
ATOM   3218 C  C   . LEU B 1 152 ? -2.109  -20.567 -1.624  1.00 65.90  ? 152 LEU B C   1 
ATOM   3219 O  O   . LEU B 1 152 ? -0.869  -20.455 -1.715  1.00 72.57  ? 152 LEU B O   1 
ATOM   3220 C  CB  . LEU B 1 152 ? -2.848  -21.887 -3.620  1.00 59.00  ? 152 LEU B CB  1 
ATOM   3221 C  CG  . LEU B 1 152 ? -4.169  -22.506 -4.072  1.00 55.60  ? 152 LEU B CG  1 
ATOM   3222 C  CD1 . LEU B 1 152 ? -5.055  -21.498 -4.786  1.00 53.86  ? 152 LEU B CD1 1 
ATOM   3223 C  CD2 . LEU B 1 152 ? -3.905  -23.711 -4.963  1.00 55.43  ? 152 LEU B CD2 1 
ATOM   3224 N  N   . THR B 1 153 ? -2.778  -20.748 -0.480  1.00 66.47  ? 153 THR B N   1 
ATOM   3225 C  CA  . THR B 1 153 ? -2.176  -20.660 0.879   1.00 66.03  ? 153 THR B CA  1 
ATOM   3226 C  C   . THR B 1 153 ? -2.299  -22.015 1.589   1.00 67.38  ? 153 THR B C   1 
ATOM   3227 O  O   . THR B 1 153 ? -1.603  -22.961 1.165   1.00 68.29  ? 153 THR B O   1 
ATOM   3228 C  CB  . THR B 1 153 ? -2.792  -19.496 1.664   1.00 64.48  ? 153 THR B CB  1 
ATOM   3229 O  OG1 . THR B 1 153 ? -3.053  -18.442 0.740   1.00 65.49  ? 153 THR B OG1 1 
ATOM   3230 C  CG2 . THR B 1 153 ? -1.894  -18.997 2.773   1.00 66.69  ? 153 THR B CG2 1 
ATOM   3231 N  N   . SER B 1 154 ? -3.145  -22.104 2.620   1.00 68.18  ? 154 SER B N   1 
ATOM   3232 C  CA  . SER B 1 154 ? -3.219  -23.238 3.573   1.00 71.27  ? 154 SER B CA  1 
ATOM   3233 C  C   . SER B 1 154 ? -4.618  -23.857 3.550   1.00 73.86  ? 154 SER B C   1 
ATOM   3234 O  O   . SER B 1 154 ? -5.600  -23.102 3.527   1.00 78.75  ? 154 SER B O   1 
ATOM   3235 C  CB  . SER B 1 154 ? -2.878  -22.775 4.954   1.00 72.26  ? 154 SER B CB  1 
ATOM   3236 O  OG  . SER B 1 154 ? -3.821  -21.807 5.402   1.00 69.18  ? 154 SER B OG  1 
ATOM   3237 N  N   . LYS B 1 155 ? -4.682  -25.187 3.532   1.00 74.91  ? 155 LYS B N   1 
ATOM   3238 C  CA  . LYS B 1 155 ? -5.939  -25.968 3.630   1.00 73.86  ? 155 LYS B CA  1 
ATOM   3239 C  C   . LYS B 1 155 ? -6.348  -26.046 5.108   1.00 70.03  ? 155 LYS B C   1 
ATOM   3240 O  O   . LYS B 1 155 ? -5.451  -26.081 5.961   1.00 69.43  ? 155 LYS B O   1 
ATOM   3241 C  CB  . LYS B 1 155 ? -5.733  -27.336 2.970   1.00 75.13  ? 155 LYS B CB  1 
ATOM   3242 C  CG  . LYS B 1 155 ? -5.569  -27.294 1.454   1.00 75.49  ? 155 LYS B CG  1 
ATOM   3243 C  CD  . LYS B 1 155 ? -4.794  -28.460 0.873   1.00 78.80  ? 155 LYS B CD  1 
ATOM   3244 C  CE  . LYS B 1 155 ? -3.290  -28.273 0.913   1.00 83.43  ? 155 LYS B CE  1 
ATOM   3245 N  NZ  . LYS B 1 155 ? -2.811  -27.317 -0.115  1.00 86.88  ? 155 LYS B NZ  1 
ATOM   3246 N  N   . HIS B 1 156 ? -7.654  -26.059 5.390   1.00 70.37  ? 156 HIS B N   1 
ATOM   3247 C  CA  . HIS B 1 156 ? -8.249  -26.234 6.744   1.00 74.67  ? 156 HIS B CA  1 
ATOM   3248 C  C   . HIS B 1 156 ? -9.275  -27.369 6.761   1.00 69.01  ? 156 HIS B C   1 
ATOM   3249 O  O   . HIS B 1 156 ? -10.234 -27.299 5.992   1.00 64.94  ? 156 HIS B O   1 
ATOM   3250 C  CB  . HIS B 1 156 ? -8.930  -24.947 7.215   1.00 83.30  ? 156 HIS B CB  1 
ATOM   3251 C  CG  . HIS B 1 156 ? -7.965  -23.896 7.642   1.00 95.51  ? 156 HIS B CG  1 
ATOM   3252 N  ND1 . HIS B 1 156 ? -8.288  -22.554 7.635   1.00 104.09 ? 156 HIS B ND1 1 
ATOM   3253 C  CD2 . HIS B 1 156 ? -6.688  -23.978 8.075   1.00 102.82 ? 156 HIS B CD2 1 
ATOM   3254 C  CE1 . HIS B 1 156 ? -7.254  -21.854 8.055   1.00 108.61 ? 156 HIS B CE1 1 
ATOM   3255 N  NE2 . HIS B 1 156 ? -6.260  -22.705 8.328   1.00 109.95 ? 156 HIS B NE2 1 
ATOM   3256 N  N   . PHE B 1 157 ? -9.122  -28.325 7.687   1.00 70.21  ? 157 PHE B N   1 
ATOM   3257 C  CA  . PHE B 1 157 ? -10.103 -29.407 7.985   1.00 68.17  ? 157 PHE B CA  1 
ATOM   3258 C  C   . PHE B 1 157 ? -10.422 -29.410 9.487   1.00 66.36  ? 157 PHE B C   1 
ATOM   3259 O  O   . PHE B 1 157 ? -9.593  -28.956 10.307  1.00 66.24  ? 157 PHE B O   1 
ATOM   3260 C  CB  . PHE B 1 157 ? -9.589  -30.768 7.500   1.00 67.59  ? 157 PHE B CB  1 
ATOM   3261 C  CG  . PHE B 1 157 ? -8.881  -30.706 6.171   1.00 68.32  ? 157 PHE B CG  1 
ATOM   3262 C  CD1 . PHE B 1 157 ? -7.577  -30.245 6.096   1.00 65.77  ? 157 PHE B CD1 1 
ATOM   3263 C  CD2 . PHE B 1 157 ? -9.530  -31.052 4.994   1.00 70.11  ? 157 PHE B CD2 1 
ATOM   3264 C  CE1 . PHE B 1 157 ? -6.926  -30.160 4.879   1.00 67.48  ? 157 PHE B CE1 1 
ATOM   3265 C  CE2 . PHE B 1 157 ? -8.880  -30.963 3.776   1.00 68.18  ? 157 PHE B CE2 1 
ATOM   3266 C  CZ  . PHE B 1 157 ? -7.579  -30.517 3.720   1.00 70.49  ? 157 PHE B CZ  1 
ATOM   3267 N  N   . GLY B 1 158 ? -11.616 -29.893 9.831   1.00 64.00  ? 158 GLY B N   1 
ATOM   3268 C  CA  . GLY B 1 158 ? -12.132 -29.909 11.211  1.00 62.19  ? 158 GLY B CA  1 
ATOM   3269 C  C   . GLY B 1 158 ? -11.638 -31.124 11.971  1.00 61.27  ? 158 GLY B C   1 
ATOM   3270 O  O   . GLY B 1 158 ? -12.005 -32.250 11.601  1.00 60.64  ? 158 GLY B O   1 
ATOM   3271 N  N   . THR B 1 159 ? -10.822 -30.890 12.997  1.00 62.42  ? 159 THR B N   1 
ATOM   3272 C  CA  . THR B 1 159 ? -10.224 -31.914 13.892  1.00 58.24  ? 159 THR B CA  1 
ATOM   3273 C  C   . THR B 1 159 ? -11.064 -32.073 15.161  1.00 53.93  ? 159 THR B C   1 
ATOM   3274 O  O   . THR B 1 159 ? -10.529 -32.595 16.151  1.00 54.13  ? 159 THR B O   1 
ATOM   3275 C  CB  . THR B 1 159 ? -8.823  -31.453 14.288  1.00 57.61  ? 159 THR B CB  1 
ATOM   3276 O  OG1 . THR B 1 159 ? -9.037  -30.105 14.714  1.00 58.30  ? 159 THR B OG1 1 
ATOM   3277 C  CG2 . THR B 1 159 ? -7.833  -31.557 13.149  1.00 56.05  ? 159 THR B CG2 1 
ATOM   3278 N  N   . ALA B 1 160 ? -12.320 -31.634 15.137  1.00 53.53  ? 160 ALA B N   1 
ATOM   3279 C  CA  . ALA B 1 160 ? -13.146 -31.379 16.344  1.00 55.51  ? 160 ALA B CA  1 
ATOM   3280 C  C   . ALA B 1 160 ? -14.037 -32.578 16.692  1.00 55.08  ? 160 ALA B C   1 
ATOM   3281 O  O   . ALA B 1 160 ? -15.019 -32.369 17.429  1.00 57.42  ? 160 ALA B O   1 
ATOM   3282 C  CB  . ALA B 1 160 ? -13.972 -30.131 16.129  1.00 55.68  ? 160 ALA B CB  1 
ATOM   3283 N  N   . GLY B 1 161 ? -13.720 -33.787 16.224  1.00 54.77  ? 161 GLY B N   1 
ATOM   3284 C  CA  . GLY B 1 161 ? -14.578 -34.967 16.457  1.00 51.87  ? 161 GLY B CA  1 
ATOM   3285 C  C   . GLY B 1 161 ? -14.240 -36.128 15.542  1.00 49.44  ? 161 GLY B C   1 
ATOM   3286 O  O   . GLY B 1 161 ? -14.459 -36.001 14.315  1.00 45.82  ? 161 GLY B O   1 
ATOM   3287 N  N   . TYR B 1 162 ? -13.727 -37.218 16.120  1.00 46.68  ? 162 TYR B N   1 
ATOM   3288 C  CA  . TYR B 1 162 ? -13.366 -38.464 15.395  1.00 48.39  ? 162 TYR B CA  1 
ATOM   3289 C  C   . TYR B 1 162 ? -12.938 -39.579 16.358  1.00 49.55  ? 162 TYR B C   1 
ATOM   3290 O  O   . TYR B 1 162 ? -12.439 -39.300 17.458  1.00 53.63  ? 162 TYR B O   1 
ATOM   3291 C  CB  . TYR B 1 162 ? -12.221 -38.200 14.420  1.00 48.79  ? 162 TYR B CB  1 
ATOM   3292 C  CG  . TYR B 1 162 ? -10.970 -37.712 15.095  1.00 48.87  ? 162 TYR B CG  1 
ATOM   3293 C  CD1 . TYR B 1 162 ? -10.034 -38.602 15.590  1.00 49.14  ? 162 TYR B CD1 1 
ATOM   3294 C  CD2 . TYR B 1 162 ? -10.737 -36.357 15.260  1.00 50.88  ? 162 TYR B CD2 1 
ATOM   3295 C  CE1 . TYR B 1 162 ? -8.888  -38.155 16.224  1.00 49.73  ? 162 TYR B CE1 1 
ATOM   3296 C  CE2 . TYR B 1 162 ? -9.604  -35.894 15.898  1.00 51.10  ? 162 TYR B CE2 1 
ATOM   3297 C  CZ  . TYR B 1 162 ? -8.675  -36.799 16.377  1.00 50.21  ? 162 TYR B CZ  1 
ATOM   3298 O  OH  . TYR B 1 162 ? -7.553  -36.357 17.005  1.00 51.78  ? 162 TYR B OH  1 
ATOM   3299 N  N   . VAL B 1 163 ? -13.109 -40.823 15.914  1.00 51.34  ? 163 VAL B N   1 
ATOM   3300 C  CA  . VAL B 1 163 ? -12.557 -42.055 16.546  1.00 51.02  ? 163 VAL B CA  1 
ATOM   3301 C  C   . VAL B 1 163 ? -11.203 -42.341 15.907  1.00 55.53  ? 163 VAL B C   1 
ATOM   3302 O  O   . VAL B 1 163 ? -11.113 -42.238 14.667  1.00 58.72  ? 163 VAL B O   1 
ATOM   3303 C  CB  . VAL B 1 163 ? -13.467 -43.274 16.327  1.00 49.83  ? 163 VAL B CB  1 
ATOM   3304 C  CG1 . VAL B 1 163 ? -12.954 -44.469 17.113  1.00 50.27  ? 163 VAL B CG1 1 
ATOM   3305 C  CG2 . VAL B 1 163 ? -14.926 -42.978 16.631  1.00 49.71  ? 163 VAL B CG2 1 
ATOM   3306 N  N   . ILE B 1 164 ? -10.222 -42.751 16.711  1.00 58.73  ? 164 ILE B N   1 
ATOM   3307 C  CA  . ILE B 1 164 ? -8.885  -43.198 16.221  1.00 62.69  ? 164 ILE B CA  1 
ATOM   3308 C  C   . ILE B 1 164 ? -8.594  -44.580 16.817  1.00 65.91  ? 164 ILE B C   1 
ATOM   3309 O  O   . ILE B 1 164 ? -8.657  -44.718 18.044  1.00 68.39  ? 164 ILE B O   1 
ATOM   3310 C  CB  . ILE B 1 164 ? -7.789  -42.157 16.542  1.00 61.44  ? 164 ILE B CB  1 
ATOM   3311 C  CG1 . ILE B 1 164 ? -6.440  -42.564 15.947  1.00 62.02  ? 164 ILE B CG1 1 
ATOM   3312 C  CG2 . ILE B 1 164 ? -7.675  -41.875 18.032  1.00 59.02  ? 164 ILE B CG2 1 
ATOM   3313 C  CD1 . ILE B 1 164 ? -5.393  -41.486 16.013  1.00 63.18  ? 164 ILE B CD1 1 
ATOM   3314 N  N   . SER B 1 165 ? -8.324  -45.567 15.960  1.00 69.83  ? 165 SER B N   1 
ATOM   3315 C  CA  . SER B 1 165 ? -7.843  -46.922 16.335  1.00 71.17  ? 165 SER B CA  1 
ATOM   3316 C  C   . SER B 1 165 ? -6.514  -46.791 17.091  1.00 73.68  ? 165 SER B C   1 
ATOM   3317 O  O   . SER B 1 165 ? -5.803  -45.797 16.859  1.00 73.11  ? 165 SER B O   1 
ATOM   3318 C  CB  . SER B 1 165 ? -7.701  -47.798 15.113  1.00 71.03  ? 165 SER B CB  1 
ATOM   3319 O  OG  . SER B 1 165 ? -6.426  -47.626 14.502  1.00 70.67  ? 165 SER B OG  1 
ATOM   3320 N  N   . GLN B 1 166 ? -6.186  -47.746 17.963  1.00 79.02  ? 166 GLN B N   1 
ATOM   3321 C  CA  . GLN B 1 166 ? -4.875  -47.768 18.664  1.00 84.19  ? 166 GLN B CA  1 
ATOM   3322 C  C   . GLN B 1 166 ? -3.764  -47.852 17.612  1.00 80.11  ? 166 GLN B C   1 
ATOM   3323 O  O   . GLN B 1 166 ? -2.813  -47.045 17.685  1.00 74.07  ? 166 GLN B O   1 
ATOM   3324 C  CB  . GLN B 1 166 ? -4.770  -48.928 19.654  1.00 92.12  ? 166 GLN B CB  1 
ATOM   3325 C  CG  . GLN B 1 166 ? -3.608  -48.753 20.622  1.00 99.59  ? 166 GLN B CG  1 
ATOM   3326 C  CD  . GLN B 1 166 ? -3.257  -50.005 21.386  1.00 107.07 ? 166 GLN B CD  1 
ATOM   3327 O  OE1 . GLN B 1 166 ? -2.220  -50.623 21.155  1.00 111.56 ? 166 GLN B OE1 1 
ATOM   3328 N  NE2 . GLN B 1 166 ? -4.107  -50.369 22.332  1.00 112.67 ? 166 GLN B NE2 1 
ATOM   3329 N  N   . GLY B 1 167 ? -3.893  -48.790 16.669  1.00 77.15  ? 167 GLY B N   1 
ATOM   3330 C  CA  . GLY B 1 167 ? -2.993  -48.913 15.508  1.00 78.21  ? 167 GLY B CA  1 
ATOM   3331 C  C   . GLY B 1 167 ? -2.709  -47.550 14.902  1.00 77.51  ? 167 GLY B C   1 
ATOM   3332 O  O   . GLY B 1 167 ? -1.515  -47.214 14.729  1.00 78.09  ? 167 GLY B O   1 
ATOM   3333 N  N   . ALA B 1 168 ? -3.770  -46.780 14.630  1.00 72.77  ? 168 ALA B N   1 
ATOM   3334 C  CA  . ALA B 1 168 ? -3.712  -45.408 14.070  1.00 70.56  ? 168 ALA B CA  1 
ATOM   3335 C  C   . ALA B 1 168 ? -2.997  -44.478 15.054  1.00 67.60  ? 168 ALA B C   1 
ATOM   3336 O  O   . ALA B 1 168 ? -2.175  -43.657 14.605  1.00 63.54  ? 168 ALA B O   1 
ATOM   3337 C  CB  . ALA B 1 168 ? -5.101  -44.912 13.742  1.00 68.67  ? 168 ALA B CB  1 
ATOM   3338 N  N   . ALA B 1 169 ? -3.301  -44.603 16.347  1.00 71.43  ? 169 ALA B N   1 
ATOM   3339 C  CA  . ALA B 1 169 ? -2.653  -43.826 17.428  1.00 74.12  ? 169 ALA B CA  1 
ATOM   3340 C  C   . ALA B 1 169 ? -1.136  -43.968 17.281  1.00 77.88  ? 169 ALA B C   1 
ATOM   3341 O  O   . ALA B 1 169 ? -0.459  -42.929 17.161  1.00 75.09  ? 169 ALA B O   1 
ATOM   3342 C  CB  . ALA B 1 169 ? -3.132  -44.286 18.780  1.00 70.27  ? 169 ALA B CB  1 
ATOM   3343 N  N   . LYS B 1 170 ? -0.647  -45.212 17.233  1.00 86.86  ? 170 LYS B N   1 
ATOM   3344 C  CA  . LYS B 1 170 ? 0.792   -45.542 17.054  1.00 93.92  ? 170 LYS B CA  1 
ATOM   3345 C  C   . LYS B 1 170 ? 1.304   -44.834 15.800  1.00 95.55  ? 170 LYS B C   1 
ATOM   3346 O  O   . LYS B 1 170 ? 2.221   -43.991 15.922  1.00 97.14  ? 170 LYS B O   1 
ATOM   3347 C  CB  . LYS B 1 170 ? 1.005   -47.056 16.943  1.00 95.70  ? 170 LYS B CB  1 
ATOM   3348 C  CG  . LYS B 1 170 ? 0.674   -47.834 18.210  1.00 100.59 ? 170 LYS B CG  1 
ATOM   3349 C  CD  . LYS B 1 170 ? 1.430   -49.136 18.378  1.00 100.88 ? 170 LYS B CD  1 
ATOM   3350 C  CE  . LYS B 1 170 ? 1.580   -49.512 19.838  1.00 101.92 ? 170 LYS B CE  1 
ATOM   3351 N  NZ  . LYS B 1 170 ? 1.830   -50.960 20.006  1.00 104.65 ? 170 LYS B NZ  1 
ATOM   3352 N  N   . TYR B 1 171 ? 0.702   -45.156 14.652  1.00 94.60  ? 171 TYR B N   1 
ATOM   3353 C  CA  . TYR B 1 171 ? 1.061   -44.607 13.321  1.00 94.85  ? 171 TYR B CA  1 
ATOM   3354 C  C   . TYR B 1 171 ? 1.323   -43.101 13.450  1.00 93.32  ? 171 TYR B C   1 
ATOM   3355 O  O   . TYR B 1 171 ? 2.461   -42.653 13.198  1.00 91.60  ? 171 TYR B O   1 
ATOM   3356 C  CB  . TYR B 1 171 ? -0.041  -44.902 12.300  1.00 94.75  ? 171 TYR B CB  1 
ATOM   3357 C  CG  . TYR B 1 171 ? 0.290   -44.425 10.910  1.00 98.75  ? 171 TYR B CG  1 
ATOM   3358 C  CD1 . TYR B 1 171 ? 1.122   -45.163 10.084  1.00 104.14 ? 171 TYR B CD1 1 
ATOM   3359 C  CD2 . TYR B 1 171 ? -0.177  -43.209 10.439  1.00 100.33 ? 171 TYR B CD2 1 
ATOM   3360 C  CE1 . TYR B 1 171 ? 1.457   -44.722 8.815   1.00 106.10 ? 171 TYR B CE1 1 
ATOM   3361 C  CE2 . TYR B 1 171 ? 0.151   -42.751 9.174   1.00 104.67 ? 171 TYR B CE2 1 
ATOM   3362 C  CZ  . TYR B 1 171 ? 0.968   -43.512 8.357   1.00 106.11 ? 171 TYR B CZ  1 
ATOM   3363 O  OH  . TYR B 1 171 ? 1.300   -43.074 7.107   1.00 107.30 ? 171 TYR B OH  1 
ATOM   3364 N  N   . LEU B 1 172 ? 0.293   -42.357 13.857  1.00 93.25  ? 172 LEU B N   1 
ATOM   3365 C  CA  . LEU B 1 172 ? 0.325   -40.874 13.969  1.00 94.98  ? 172 LEU B CA  1 
ATOM   3366 C  C   . LEU B 1 172 ? 1.439   -40.457 14.932  1.00 96.38  ? 172 LEU B C   1 
ATOM   3367 O  O   . LEU B 1 172 ? 2.250   -39.597 14.549  1.00 93.14  ? 172 LEU B O   1 
ATOM   3368 C  CB  . LEU B 1 172 ? -1.040  -40.359 14.433  1.00 95.01  ? 172 LEU B CB  1 
ATOM   3369 C  CG  . LEU B 1 172 ? -1.931  -39.796 13.326  1.00 96.07  ? 172 LEU B CG  1 
ATOM   3370 C  CD1 . LEU B 1 172 ? -1.984  -40.722 12.121  1.00 95.72  ? 172 LEU B CD1 1 
ATOM   3371 C  CD2 . LEU B 1 172 ? -3.330  -39.535 13.845  1.00 96.96  ? 172 LEU B CD2 1 
ATOM   3372 N  N   . ILE B 1 173 ? 1.490   -41.057 16.121  1.00 103.73 ? 173 ILE B N   1 
ATOM   3373 C  CA  . ILE B 1 173 ? 2.492   -40.697 17.168  1.00 108.52 ? 173 ILE B CA  1 
ATOM   3374 C  C   . ILE B 1 173 ? 3.880   -40.661 16.516  1.00 105.99 ? 173 ILE B C   1 
ATOM   3375 O  O   . ILE B 1 173 ? 4.540   -39.603 16.577  1.00 100.10 ? 173 ILE B O   1 
ATOM   3376 C  CB  . ILE B 1 173 ? 2.439   -41.664 18.369  1.00 113.82 ? 173 ILE B CB  1 
ATOM   3377 C  CG1 . ILE B 1 173 ? 1.162   -41.479 19.193  1.00 114.86 ? 173 ILE B CG1 1 
ATOM   3378 C  CG2 . ILE B 1 173 ? 3.679   -41.512 19.239  1.00 115.64 ? 173 ILE B CG2 1 
ATOM   3379 C  CD1 . ILE B 1 173 ? 0.766   -42.702 19.989  1.00 113.98 ? 173 ILE B CD1 1 
ATOM   3380 N  N   . ALA B 1 174 ? 4.289   -41.776 15.905  1.00 104.76 ? 174 ALA B N   1 
ATOM   3381 C  CA  . ALA B 1 174 ? 5.593   -41.946 15.224  1.00 106.94 ? 174 ALA B CA  1 
ATOM   3382 C  C   . ALA B 1 174 ? 5.741   -40.876 14.139  1.00 106.12 ? 174 ALA B C   1 
ATOM   3383 O  O   . ALA B 1 174 ? 6.675   -40.053 14.237  1.00 105.89 ? 174 ALA B O   1 
ATOM   3384 C  CB  . ALA B 1 174 ? 5.694   -43.334 14.641  1.00 107.75 ? 174 ALA B CB  1 
ATOM   3385 N  N   . LEU B 1 175 ? 4.816   -40.883 13.174  1.00 101.53 ? 175 LEU B N   1 
ATOM   3386 C  CA  . LEU B 1 175 ? 4.783   -39.993 11.981  1.00 97.98  ? 175 LEU B CA  1 
ATOM   3387 C  C   . LEU B 1 175 ? 5.158   -38.554 12.363  1.00 94.37  ? 175 LEU B C   1 
ATOM   3388 O  O   . LEU B 1 175 ? 5.867   -37.907 11.573  1.00 89.66  ? 175 LEU B O   1 
ATOM   3389 C  CB  . LEU B 1 175 ? 3.375   -40.068 11.381  1.00 97.94  ? 175 LEU B CB  1 
ATOM   3390 C  CG  . LEU B 1 175 ? 3.090   -39.177 10.172  1.00 96.24  ? 175 LEU B CG  1 
ATOM   3391 C  CD1 . LEU B 1 175 ? 2.017   -39.810 9.305   1.00 96.15  ? 175 LEU B CD1 1 
ATOM   3392 C  CD2 . LEU B 1 175 ? 2.661   -37.775 10.584  1.00 95.21  ? 175 LEU B CD2 1 
ATOM   3393 N  N   . PHE B 1 176 ? 4.682   -38.066 13.512  1.00 97.73  ? 176 PHE B N   1 
ATOM   3394 C  CA  . PHE B 1 176 ? 4.864   -36.664 13.973  1.00 101.38 ? 176 PHE B CA  1 
ATOM   3395 C  C   . PHE B 1 176 ? 6.270   -36.467 14.549  1.00 105.54 ? 176 PHE B C   1 
ATOM   3396 O  O   . PHE B 1 176 ? 6.803   -35.346 14.446  1.00 109.36 ? 176 PHE B O   1 
ATOM   3397 C  CB  . PHE B 1 176 ? 3.772   -36.286 14.976  1.00 100.84 ? 176 PHE B CB  1 
ATOM   3398 C  CG  . PHE B 1 176 ? 2.546   -35.703 14.322  1.00 98.62  ? 176 PHE B CG  1 
ATOM   3399 C  CD1 . PHE B 1 176 ? 2.480   -34.346 14.047  1.00 95.70  ? 176 PHE B CD1 1 
ATOM   3400 C  CD2 . PHE B 1 176 ? 1.480   -36.504 13.943  1.00 100.22 ? 176 PHE B CD2 1 
ATOM   3401 C  CE1 . PHE B 1 176 ? 1.368   -33.799 13.426  1.00 94.98  ? 176 PHE B CE1 1 
ATOM   3402 C  CE2 . PHE B 1 176 ? 0.368   -35.955 13.322  1.00 98.83  ? 176 PHE B CE2 1 
ATOM   3403 C  CZ  . PHE B 1 176 ? 0.313   -34.604 13.065  1.00 94.78  ? 176 PHE B CZ  1 
ATOM   3404 N  N   . GLU B 1 177 ? 6.846   -37.517 15.137  1.00 104.85 ? 177 GLU B N   1 
ATOM   3405 C  CA  . GLU B 1 177 ? 8.232   -37.499 15.675  1.00 104.23 ? 177 GLU B CA  1 
ATOM   3406 C  C   . GLU B 1 177 ? 9.240   -37.626 14.524  1.00 103.51 ? 177 GLU B C   1 
ATOM   3407 O  O   . GLU B 1 177 ? 10.423  -37.319 14.764  1.00 101.06 ? 177 GLU B O   1 
ATOM   3408 C  CB  . GLU B 1 177 ? 8.407   -38.600 16.721  1.00 105.67 ? 177 GLU B CB  1 
ATOM   3409 C  CG  . GLU B 1 177 ? 7.630   -38.339 17.997  1.00 104.72 ? 177 GLU B CG  1 
ATOM   3410 C  CD  . GLU B 1 177 ? 7.901   -39.315 19.129  1.00 102.60 ? 177 GLU B CD  1 
ATOM   3411 O  OE1 . GLU B 1 177 ? 7.636   -38.945 20.283  1.00 104.16 ? 177 GLU B OE1 1 
ATOM   3412 O  OE2 . GLU B 1 177 ? 8.376   -40.439 18.861  1.00 101.42 ? 177 GLU B OE2 1 
ATOM   3413 N  N   . LYS B 1 178 ? 8.788   -38.030 13.326  1.00 103.16 ? 178 LYS B N   1 
ATOM   3414 C  CA  . LYS B 1 178 ? 9.624   -38.178 12.100  1.00 101.35 ? 178 LYS B CA  1 
ATOM   3415 C  C   . LYS B 1 178 ? 9.525   -36.926 11.215  1.00 98.79  ? 178 LYS B C   1 
ATOM   3416 O  O   . LYS B 1 178 ? 9.726   -37.058 9.993   1.00 90.85  ? 178 LYS B O   1 
ATOM   3417 C  CB  . LYS B 1 178 ? 9.193   -39.413 11.300  1.00 100.56 ? 178 LYS B CB  1 
ATOM   3418 C  CG  . LYS B 1 178 ? 9.236   -40.733 12.060  1.00 101.83 ? 178 LYS B CG  1 
ATOM   3419 C  CD  . LYS B 1 178 ? 9.215   -41.949 11.160  1.00 101.18 ? 178 LYS B CD  1 
ATOM   3420 C  CE  . LYS B 1 178 ? 8.141   -41.880 10.095  1.00 102.68 ? 178 LYS B CE  1 
ATOM   3421 N  NZ  . LYS B 1 178 ? 8.147   -43.090 9.242   1.00 106.13 ? 178 LYS B NZ  1 
ATOM   3422 N  N   . LEU B 1 179 ? 9.241   -35.761 11.807  1.00 104.95 ? 179 LEU B N   1 
ATOM   3423 C  CA  . LEU B 1 179 ? 9.227   -34.439 11.121  1.00 113.00 ? 179 LEU B CA  1 
ATOM   3424 C  C   . LEU B 1 179 ? 10.208  -33.509 11.843  1.00 119.95 ? 179 LEU B C   1 
ATOM   3425 O  O   . LEU B 1 179 ? 10.242  -33.578 13.085  1.00 115.35 ? 179 LEU B O   1 
ATOM   3426 C  CB  . LEU B 1 179 ? 7.805   -33.868 11.142  1.00 114.23 ? 179 LEU B CB  1 
ATOM   3427 C  CG  . LEU B 1 179 ? 6.708   -34.785 10.598  1.00 111.35 ? 179 LEU B CG  1 
ATOM   3428 C  CD1 . LEU B 1 179 ? 5.351   -34.101 10.656  1.00 107.46 ? 179 LEU B CD1 1 
ATOM   3429 C  CD2 . LEU B 1 179 ? 7.014   -35.224 9.174   1.00 110.41 ? 179 LEU B CD2 1 
ATOM   3430 N  N   . THR B 1 180 ? 10.977  -32.704 11.095  1.00 126.91 ? 180 THR B N   1 
ATOM   3431 C  CA  . THR B 1 180 ? 11.912  -31.668 11.621  1.00 129.85 ? 180 THR B CA  1 
ATOM   3432 C  C   . THR B 1 180 ? 11.658  -30.360 10.871  1.00 120.17 ? 180 THR B C   1 
ATOM   3433 O  O   . THR B 1 180 ? 12.507  -29.969 10.047  1.00 114.37 ? 180 THR B O   1 
ATOM   3434 C  CB  . THR B 1 180 ? 13.384  -32.106 11.566  1.00 134.14 ? 180 THR B CB  1 
ATOM   3435 O  OG1 . THR B 1 180 ? 13.484  -33.419 12.116  1.00 141.76 ? 180 THR B OG1 1 
ATOM   3436 C  CG2 . THR B 1 180 ? 14.300  -31.181 12.339  1.00 131.24 ? 180 THR B CG2 1 
ATOM   3437 N  N   . THR B 1 181 ? 10.510  -29.736 11.140  1.00 115.31 ? 181 THR B N   1 
ATOM   3438 C  CA  . THR B 1 181 ? 10.089  -28.426 10.571  1.00 112.49 ? 181 THR B CA  1 
ATOM   3439 C  C   . THR B 1 181 ? 9.955   -28.555 9.047   1.00 111.65 ? 181 THR B C   1 
ATOM   3440 O  O   . THR B 1 181 ? 9.663   -27.534 8.390   1.00 111.64 ? 181 THR B O   1 
ATOM   3441 C  CB  . THR B 1 181 ? 11.074  -27.328 10.999  1.00 108.95 ? 181 THR B CB  1 
ATOM   3442 O  OG1 . THR B 1 181 ? 11.302  -27.492 12.402  1.00 99.29  ? 181 THR B OG1 1 
ATOM   3443 C  CG2 . THR B 1 181 ? 10.593  -25.926 10.688  1.00 106.06 ? 181 THR B CG2 1 
ATOM   3444 N  N   . GLU B 1 182 ? 10.122  -29.773 8.520   1.00 110.42 ? 182 GLU B N   1 
ATOM   3445 C  CA  . GLU B 1 182 ? 10.266  -30.059 7.069   1.00 113.78 ? 182 GLU B CA  1 
ATOM   3446 C  C   . GLU B 1 182 ? 8.884   -29.985 6.410   1.00 117.30 ? 182 GLU B C   1 
ATOM   3447 O  O   . GLU B 1 182 ? 8.711   -29.146 5.505   1.00 125.75 ? 182 GLU B O   1 
ATOM   3448 C  CB  . GLU B 1 182 ? 10.950  -31.416 6.871   1.00 111.20 ? 182 GLU B CB  1 
ATOM   3449 C  CG  . GLU B 1 182 ? 10.127  -32.595 7.351   1.00 108.19 ? 182 GLU B CG  1 
ATOM   3450 C  CD  . GLU B 1 182 ? 10.875  -33.838 7.788   1.00 103.55 ? 182 GLU B CD  1 
ATOM   3451 O  OE1 . GLU B 1 182 ? 10.836  -34.848 7.057   1.00 100.70 ? 182 GLU B OE1 1 
ATOM   3452 O  OE2 . GLU B 1 182 ? 11.429  -33.807 8.896   1.00 98.31  ? 182 GLU B OE2 1 
ATOM   3453 N  N   . GLU B 1 183 ? 7.939   -30.811 6.867   1.00 116.50 ? 183 GLU B N   1 
ATOM   3454 C  CA  . GLU B 1 183 ? 6.524   -30.814 6.410   1.00 117.47 ? 183 GLU B CA  1 
ATOM   3455 C  C   . GLU B 1 183 ? 5.643   -30.529 7.626   1.00 109.73 ? 183 GLU B C   1 
ATOM   3456 O  O   . GLU B 1 183 ? 4.463   -30.937 7.625   1.00 110.54 ? 183 GLU B O   1 
ATOM   3457 C  CB  . GLU B 1 183 ? 6.113   -32.147 5.776   1.00 121.55 ? 183 GLU B CB  1 
ATOM   3458 C  CG  . GLU B 1 183 ? 7.127   -32.728 4.805   1.00 121.68 ? 183 GLU B CG  1 
ATOM   3459 C  CD  . GLU B 1 183 ? 7.992   -33.841 5.371   1.00 122.30 ? 183 GLU B CD  1 
ATOM   3460 O  OE1 . GLU B 1 183 ? 7.983   -34.030 6.600   1.00 121.41 ? 183 GLU B OE1 1 
ATOM   3461 O  OE2 . GLU B 1 183 ? 8.672   -34.516 4.577   1.00 123.44 ? 183 GLU B OE2 1 
ATOM   3462 N  N   . ILE B 1 184 ? 6.197   -29.862 8.637   1.00 101.56 ? 184 ILE B N   1 
ATOM   3463 C  CA  . ILE B 1 184 ? 5.430   -29.425 9.838   1.00 106.99 ? 184 ILE B CA  1 
ATOM   3464 C  C   . ILE B 1 184 ? 4.333   -28.459 9.370   1.00 110.63 ? 184 ILE B C   1 
ATOM   3465 O  O   . ILE B 1 184 ? 4.630   -27.267 9.170   1.00 114.38 ? 184 ILE B O   1 
ATOM   3466 C  CB  . ILE B 1 184 ? 6.370   -28.833 10.906  1.00 107.88 ? 184 ILE B CB  1 
ATOM   3467 C  CG1 . ILE B 1 184 ? 7.238   -29.925 11.538  1.00 109.31 ? 184 ILE B CG1 1 
ATOM   3468 C  CG2 . ILE B 1 184 ? 5.591   -28.056 11.957  1.00 104.49 ? 184 ILE B CG2 1 
ATOM   3469 C  CD1 . ILE B 1 184 ? 6.464   -31.031 12.215  1.00 107.20 ? 184 ILE B CD1 1 
ATOM   3470 N  N   . LYS B 1 185 ? 3.128   -29.003 9.157   1.00 110.57 ? 185 LYS B N   1 
ATOM   3471 C  CA  . LYS B 1 185 ? 1.850   -28.289 8.889   1.00 105.81 ? 185 LYS B CA  1 
ATOM   3472 C  C   . LYS B 1 185 ? 0.881   -28.648 10.017  1.00 98.58  ? 185 LYS B C   1 
ATOM   3473 O  O   . LYS B 1 185 ? 1.011   -29.722 10.603  1.00 91.83  ? 185 LYS B O   1 
ATOM   3474 C  CB  . LYS B 1 185 ? 1.270   -28.714 7.534   1.00 111.23 ? 185 LYS B CB  1 
ATOM   3475 C  CG  . LYS B 1 185 ? 2.214   -28.685 6.335   1.00 111.41 ? 185 LYS B CG  1 
ATOM   3476 C  CD  . LYS B 1 185 ? 1.601   -29.267 5.062   1.00 110.02 ? 185 LYS B CD  1 
ATOM   3477 C  CE  . LYS B 1 185 ? 0.507   -28.398 4.469   1.00 108.21 ? 185 LYS B CE  1 
ATOM   3478 N  NZ  . LYS B 1 185 ? 0.121   -28.811 3.098   1.00 101.60 ? 185 LYS B NZ  1 
ATOM   3479 N  N   . PRO B 1 186 ? -0.129  -27.807 10.353  1.00 95.46  ? 186 PRO B N   1 
ATOM   3480 C  CA  . PRO B 1 186 ? -1.049  -28.115 11.451  1.00 92.06  ? 186 PRO B CA  1 
ATOM   3481 C  C   . PRO B 1 186 ? -1.665  -29.521 11.368  1.00 86.00  ? 186 PRO B C   1 
ATOM   3482 O  O   . PRO B 1 186 ? -1.545  -30.175 10.339  1.00 86.02  ? 186 PRO B O   1 
ATOM   3483 C  CB  . PRO B 1 186 ? -2.145  -27.045 11.331  1.00 96.21  ? 186 PRO B CB  1 
ATOM   3484 C  CG  . PRO B 1 186 ? -1.462  -25.881 10.640  1.00 98.27  ? 186 PRO B CG  1 
ATOM   3485 C  CD  . PRO B 1 186 ? -0.435  -26.516 9.718   1.00 97.75  ? 186 PRO B CD  1 
ATOM   3486 N  N   . ILE B 1 187 ? -2.321  -29.946 12.449  1.00 79.12  ? 187 ILE B N   1 
ATOM   3487 C  CA  . ILE B 1 187 ? -2.789  -31.351 12.653  1.00 78.62  ? 187 ILE B CA  1 
ATOM   3488 C  C   . ILE B 1 187 ? -3.757  -31.757 11.528  1.00 76.12  ? 187 ILE B C   1 
ATOM   3489 O  O   . ILE B 1 187 ? -3.519  -32.816 10.907  1.00 68.09  ? 187 ILE B O   1 
ATOM   3490 C  CB  . ILE B 1 187 ? -3.383  -31.538 14.067  1.00 79.39  ? 187 ILE B CB  1 
ATOM   3491 C  CG1 . ILE B 1 187 ? -4.066  -32.899 14.213  1.00 76.14  ? 187 ILE B CG1 1 
ATOM   3492 C  CG2 . ILE B 1 187 ? -4.314  -30.392 14.452  1.00 82.16  ? 187 ILE B CG2 1 
ATOM   3493 C  CD1 . ILE B 1 187 ? -4.187  -33.373 15.644  1.00 74.73  ? 187 ILE B CD1 1 
ATOM   3494 N  N   . ASP B 1 188 ? -4.788  -30.945 11.267  1.00 77.38  ? 188 ASP B N   1 
ATOM   3495 C  CA  . ASP B 1 188 ? -5.816  -31.182 10.210  1.00 74.41  ? 188 ASP B CA  1 
ATOM   3496 C  C   . ASP B 1 188 ? -5.125  -31.478 8.877   1.00 70.90  ? 188 ASP B C   1 
ATOM   3497 O  O   . ASP B 1 188 ? -5.447  -32.523 8.254   1.00 67.41  ? 188 ASP B O   1 
ATOM   3498 C  CB  . ASP B 1 188 ? -6.804  -30.011 10.053  1.00 70.32  ? 188 ASP B CB  1 
ATOM   3499 C  CG  . ASP B 1 188 ? -6.242  -28.621 10.316  1.00 67.43  ? 188 ASP B CG  1 
ATOM   3500 O  OD1 . ASP B 1 188 ? -5.548  -28.477 11.325  1.00 66.96  ? 188 ASP B OD1 1 
ATOM   3501 O  OD2 . ASP B 1 188 ? -6.514  -27.695 9.521   1.00 64.57  ? 188 ASP B OD2 1 
ATOM   3502 N  N   . GLU B 1 189 ? -4.181  -30.614 8.496   1.00 72.74  ? 189 GLU B N   1 
ATOM   3503 C  CA  . GLU B 1 189 ? -3.544  -30.590 7.151   1.00 84.29  ? 189 GLU B CA  1 
ATOM   3504 C  C   . GLU B 1 189 ? -2.668  -31.832 6.942   1.00 85.83  ? 189 GLU B C   1 
ATOM   3505 O  O   . GLU B 1 189 ? -2.049  -31.930 5.862   1.00 84.06  ? 189 GLU B O   1 
ATOM   3506 C  CB  . GLU B 1 189 ? -2.728  -29.306 6.958   1.00 89.97  ? 189 GLU B CB  1 
ATOM   3507 C  CG  . GLU B 1 189 ? -3.232  -28.424 5.828   1.00 98.84  ? 189 GLU B CG  1 
ATOM   3508 C  CD  . GLU B 1 189 ? -2.579  -27.054 5.742   1.00 103.80 ? 189 GLU B CD  1 
ATOM   3509 O  OE1 . GLU B 1 189 ? -2.082  -26.702 4.647   1.00 108.79 ? 189 GLU B OE1 1 
ATOM   3510 O  OE2 . GLU B 1 189 ? -2.584  -26.334 6.764   1.00 107.99 ? 189 GLU B OE2 1 
ATOM   3511 N  N   . ILE B 1 190 ? -2.610  -32.733 7.930   1.00 88.96  ? 190 ILE B N   1 
ATOM   3512 C  CA  . ILE B 1 190 ? -1.809  -33.990 7.858   1.00 90.67  ? 190 ILE B CA  1 
ATOM   3513 C  C   . ILE B 1 190 ? -2.753  -35.190 7.979   1.00 89.34  ? 190 ILE B C   1 
ATOM   3514 O  O   . ILE B 1 190 ? -2.840  -35.978 7.015   1.00 91.51  ? 190 ILE B O   1 
ATOM   3515 C  CB  . ILE B 1 190 ? -0.713  -33.989 8.941   1.00 91.30  ? 190 ILE B CB  1 
ATOM   3516 C  CG1 . ILE B 1 190 ? 0.131   -32.710 8.866   1.00 88.86  ? 190 ILE B CG1 1 
ATOM   3517 C  CG2 . ILE B 1 190 ? 0.132   -35.253 8.843   1.00 92.59  ? 190 ILE B CG2 1 
ATOM   3518 C  CD1 . ILE B 1 190 ? 1.348   -32.704 9.760   1.00 89.00  ? 190 ILE B CD1 1 
HETATM 3519 N  N   . MSE B 1 191 ? -3.427  -35.306 9.122   1.00 82.46  ? 191 MSE B N   1 
HETATM 3520 C  CA  . MSE B 1 191 ? -4.329  -36.435 9.462   1.00 76.68  ? 191 MSE B CA  1 
HETATM 3521 C  C   . MSE B 1 191 ? -5.218  -36.784 8.268   1.00 76.84  ? 191 MSE B C   1 
HETATM 3522 O  O   . MSE B 1 191 ? -5.238  -37.958 7.870   1.00 80.12  ? 191 MSE B O   1 
HETATM 3523 C  CB  . MSE B 1 191 ? -5.231  -36.036 10.625  1.00 73.63  ? 191 MSE B CB  1 
HETATM 3524 C  CG  . MSE B 1 191 ? -4.531  -35.928 11.940  1.00 69.99  ? 191 MSE B CG  1 
HETATM 3525 SE SE  . MSE B 1 191 ? -5.917  -35.731 13.294  1.00 69.22  ? 191 MSE B SE  1 
HETATM 3526 C  CE  . MSE B 1 191 ? -6.681  -37.510 13.620  1.00 67.77  ? 191 MSE B CE  1 
ATOM   3527 N  N   . PHE B 1 192 ? -5.941  -35.792 7.743   1.00 74.45  ? 192 PHE B N   1 
ATOM   3528 C  CA  . PHE B 1 192 ? -7.068  -35.986 6.798   1.00 76.58  ? 192 PHE B CA  1 
ATOM   3529 C  C   . PHE B 1 192 ? -6.615  -35.725 5.363   1.00 85.21  ? 192 PHE B C   1 
ATOM   3530 O  O   . PHE B 1 192 ? -7.075  -36.459 4.468   1.00 86.74  ? 192 PHE B O   1 
ATOM   3531 C  CB  . PHE B 1 192 ? -8.233  -35.090 7.209   1.00 72.76  ? 192 PHE B CB  1 
ATOM   3532 C  CG  . PHE B 1 192 ? -8.616  -35.258 8.655   1.00 69.20  ? 192 PHE B CG  1 
ATOM   3533 C  CD1 . PHE B 1 192 ? -9.130  -36.458 9.119   1.00 67.45  ? 192 PHE B CD1 1 
ATOM   3534 C  CD2 . PHE B 1 192 ? -8.424  -34.228 9.560   1.00 69.94  ? 192 PHE B CD2 1 
ATOM   3535 C  CE1 . PHE B 1 192 ? -9.458  -36.618 10.455  1.00 66.80  ? 192 PHE B CE1 1 
ATOM   3536 C  CE2 . PHE B 1 192 ? -8.762  -34.386 10.896  1.00 70.12  ? 192 PHE B CE2 1 
ATOM   3537 C  CZ  . PHE B 1 192 ? -9.296  -35.575 11.337  1.00 69.50  ? 192 PHE B CZ  1 
ATOM   3538 N  N   . ASN B 1 193 ? -5.751  -34.728 5.158   1.00 95.85  ? 193 ASN B N   1 
ATOM   3539 C  CA  . ASN B 1 193 ? -5.268  -34.321 3.811   1.00 102.82 ? 193 ASN B CA  1 
ATOM   3540 C  C   . ASN B 1 193 ? -4.036  -35.157 3.441   1.00 103.15 ? 193 ASN B C   1 
ATOM   3541 O  O   . ASN B 1 193 ? -4.173  -36.109 2.646   1.00 102.60 ? 193 ASN B O   1 
ATOM   3542 C  CB  . ASN B 1 193 ? -4.971  -32.817 3.755   1.00 107.67 ? 193 ASN B CB  1 
ATOM   3543 C  CG  . ASN B 1 193 ? -4.617  -32.322 2.367   1.00 109.44 ? 193 ASN B CG  1 
ATOM   3544 O  OD1 . ASN B 1 193 ? -5.174  -32.795 1.379   1.00 109.29 ? 193 ASN B OD1 1 
ATOM   3545 N  ND2 . ASN B 1 193 ? -3.683  -31.384 2.279   1.00 110.43 ? 193 ASN B ND2 1 
ATOM   3546 N  N   . GLN B 1 194 ? -2.885  -34.812 4.025   1.00 102.87 ? 194 GLN B N   1 
ATOM   3547 C  CA  . GLN B 1 194 ? -1.543  -35.299 3.614   1.00 104.86 ? 194 GLN B CA  1 
ATOM   3548 C  C   . GLN B 1 194 ? -1.583  -36.823 3.454   1.00 103.25 ? 194 GLN B C   1 
ATOM   3549 O  O   . GLN B 1 194 ? -1.226  -37.303 2.366   1.00 96.36  ? 194 GLN B O   1 
ATOM   3550 C  CB  . GLN B 1 194 ? -0.488  -34.900 4.649   1.00 108.69 ? 194 GLN B CB  1 
ATOM   3551 C  CG  . GLN B 1 194 ? 0.927   -34.810 4.090   1.00 110.71 ? 194 GLN B CG  1 
ATOM   3552 C  CD  . GLN B 1 194 ? 1.278   -33.410 3.644   1.00 116.82 ? 194 GLN B CD  1 
ATOM   3553 O  OE1 . GLN B 1 194 ? 0.430   -32.661 3.162   1.00 125.50 ? 194 GLN B OE1 1 
ATOM   3554 N  NE2 . GLN B 1 194 ? 2.538   -33.035 3.810   1.00 116.71 ? 194 GLN B NE2 1 
ATOM   3555 N  N   . GLN B 1 195 ? -2.020  -37.543 4.491   1.00 109.27 ? 195 GLN B N   1 
ATOM   3556 C  CA  . GLN B 1 195 ? -1.637  -38.966 4.688   1.00 113.38 ? 195 GLN B CA  1 
ATOM   3557 C  C   . GLN B 1 195 ? -2.795  -39.939 4.445   1.00 109.49 ? 195 GLN B C   1 
ATOM   3558 O  O   . GLN B 1 195 ? -2.526  -41.148 4.594   1.00 107.71 ? 195 GLN B O   1 
ATOM   3559 C  CB  . GLN B 1 195 ? -0.993  -39.163 6.065   1.00 120.34 ? 195 GLN B CB  1 
ATOM   3560 C  CG  . GLN B 1 195 ? 0.525   -39.198 5.990   1.00 125.73 ? 195 GLN B CG  1 
ATOM   3561 C  CD  . GLN B 1 195 ? 1.028   -40.255 5.034   1.00 135.64 ? 195 GLN B CD  1 
ATOM   3562 O  OE1 . GLN B 1 195 ? 0.411   -41.301 4.834   1.00 147.20 ? 195 GLN B OE1 1 
ATOM   3563 N  NE2 . GLN B 1 195 ? 2.163   -39.987 4.416   1.00 135.91 ? 195 GLN B NE2 1 
ATOM   3564 N  N   . ILE B 1 196 ? -3.995  -39.490 4.051   1.00 106.99 ? 196 ILE B N   1 
ATOM   3565 C  CA  . ILE B 1 196 ? -4.999  -40.421 3.446   1.00 108.08 ? 196 ILE B CA  1 
ATOM   3566 C  C   . ILE B 1 196 ? -4.385  -40.954 2.147   1.00 113.58 ? 196 ILE B C   1 
ATOM   3567 O  O   . ILE B 1 196 ? -4.786  -42.049 1.722   1.00 113.80 ? 196 ILE B O   1 
ATOM   3568 C  CB  . ILE B 1 196 ? -6.388  -39.784 3.226   1.00 103.52 ? 196 ILE B CB  1 
ATOM   3569 C  CG1 . ILE B 1 196 ? -7.428  -40.776 2.691   1.00 100.67 ? 196 ILE B CG1 1 
ATOM   3570 C  CG2 . ILE B 1 196 ? -6.295  -38.597 2.295   1.00 102.90 ? 196 ILE B CG2 1 
ATOM   3571 C  CD1 . ILE B 1 196 ? -7.577  -42.067 3.471   1.00 99.20  ? 196 ILE B CD1 1 
ATOM   3572 N  N   . ASN B 1 197 ? -3.441  -40.201 1.571   1.00 125.62 ? 197 ASN B N   1 
ATOM   3573 C  CA  . ASN B 1 197 ? -2.632  -40.568 0.379   1.00 132.73 ? 197 ASN B CA  1 
ATOM   3574 C  C   . ASN B 1 197 ? -2.135  -42.015 0.500   1.00 139.32 ? 197 ASN B C   1 
ATOM   3575 O  O   . ASN B 1 197 ? -2.738  -42.887 -0.156  1.00 144.72 ? 197 ASN B O   1 
ATOM   3576 C  CB  . ASN B 1 197 ? -1.489  -39.569 0.178   1.00 133.57 ? 197 ASN B CB  1 
ATOM   3577 C  CG  . ASN B 1 197 ? -1.978  -38.179 -0.186  1.00 136.71 ? 197 ASN B CG  1 
ATOM   3578 O  OD1 . ASN B 1 197 ? -3.113  -38.013 -0.625  1.00 139.92 ? 197 ASN B OD1 1 
ATOM   3579 N  ND2 . ASN B 1 197 ? -1.141  -37.166 -0.010  1.00 135.88 ? 197 ASN B ND2 1 
ATOM   3580 N  N   . ALA B 1 198 ? -1.105  -42.269 1.319   1.00 140.30 ? 198 ALA B N   1 
ATOM   3581 C  CA  . ALA B 1 198 ? -0.290  -43.510 1.278   1.00 139.11 ? 198 ALA B CA  1 
ATOM   3582 C  C   . ALA B 1 198 ? -0.192  -44.184 2.654   1.00 132.29 ? 198 ALA B C   1 
ATOM   3583 O  O   . ALA B 1 198 ? -0.645  -43.586 3.639   1.00 125.53 ? 198 ALA B O   1 
ATOM   3584 C  CB  . ALA B 1 198 ? 1.086   -43.181 0.751   1.00 141.69 ? 198 ALA B CB  1 
ATOM   3585 N  N   . THR B 1 199 ? 0.389   -45.392 2.678   1.00 132.07 ? 199 THR B N   1 
ATOM   3586 C  CA  . THR B 1 199 ? 0.915   -46.138 3.864   1.00 131.67 ? 199 THR B CA  1 
ATOM   3587 C  C   . THR B 1 199 ? -0.191  -46.975 4.527   1.00 124.20 ? 199 THR B C   1 
ATOM   3588 O  O   . THR B 1 199 ? -0.058  -47.280 5.737   1.00 112.72 ? 199 THR B O   1 
ATOM   3589 C  CB  . THR B 1 199 ? 1.606   -45.214 4.878   1.00 133.11 ? 199 THR B CB  1 
ATOM   3590 O  OG1 . THR B 1 199 ? 2.307   -44.178 4.186   1.00 141.69 ? 199 THR B OG1 1 
ATOM   3591 C  CG2 . THR B 1 199 ? 2.582   -45.956 5.768   1.00 127.64 ? 199 THR B CG2 1 
ATOM   3592 N  N   . ASP B 1 200 ? -1.225  -47.352 3.763   1.00 121.74 ? 200 ASP B N   1 
ATOM   3593 C  CA  . ASP B 1 200 ? -2.355  -48.225 4.194   1.00 116.91 ? 200 ASP B CA  1 
ATOM   3594 C  C   . ASP B 1 200 ? -3.098  -47.621 5.403   1.00 110.18 ? 200 ASP B C   1 
ATOM   3595 O  O   . ASP B 1 200 ? -3.782  -48.382 6.122   1.00 105.89 ? 200 ASP B O   1 
ATOM   3596 C  CB  . ASP B 1 200 ? -1.844  -49.637 4.481   1.00 116.53 ? 200 ASP B CB  1 
ATOM   3597 C  CG  . ASP B 1 200 ? -2.940  -50.685 4.532   1.00 116.88 ? 200 ASP B CG  1 
ATOM   3598 O  OD1 . ASP B 1 200 ? -4.104  -50.342 4.230   1.00 115.22 ? 200 ASP B OD1 1 
ATOM   3599 O  OD2 . ASP B 1 200 ? -2.623  -51.827 4.884   1.00 120.50 ? 200 ASP B OD2 1 
ATOM   3600 N  N   . TYR B 1 201 ? -2.971  -46.308 5.616   1.00 102.59 ? 201 TYR B N   1 
ATOM   3601 C  CA  . TYR B 1 201 ? -3.713  -45.519 6.634   1.00 92.09  ? 201 TYR B CA  1 
ATOM   3602 C  C   . TYR B 1 201 ? -5.019  -45.038 6.002   1.00 87.00  ? 201 TYR B C   1 
ATOM   3603 O  O   . TYR B 1 201 ? -4.973  -44.143 5.142   1.00 93.50  ? 201 TYR B O   1 
ATOM   3604 C  CB  . TYR B 1 201 ? -2.863  -44.347 7.131   1.00 88.71  ? 201 TYR B CB  1 
ATOM   3605 C  CG  . TYR B 1 201 ? -3.601  -43.190 7.759   1.00 86.58  ? 201 TYR B CG  1 
ATOM   3606 C  CD1 . TYR B 1 201 ? -4.685  -43.367 8.606   1.00 86.46  ? 201 TYR B CD1 1 
ATOM   3607 C  CD2 . TYR B 1 201 ? -3.157  -41.896 7.556   1.00 84.67  ? 201 TYR B CD2 1 
ATOM   3608 C  CE1 . TYR B 1 201 ? -5.329  -42.289 9.196   1.00 83.61  ? 201 TYR B CE1 1 
ATOM   3609 C  CE2 . TYR B 1 201 ? -3.778  -40.807 8.148   1.00 83.59  ? 201 TYR B CE2 1 
ATOM   3610 C  CZ  . TYR B 1 201 ? -4.866  -41.004 8.979   1.00 81.59  ? 201 TYR B CZ  1 
ATOM   3611 O  OH  . TYR B 1 201 ? -5.496  -39.937 9.555   1.00 73.14  ? 201 TYR B OH  1 
ATOM   3612 N  N   . ARG B 1 202 ? -6.147  -45.620 6.414   1.00 82.57  ? 202 ARG B N   1 
ATOM   3613 C  CA  . ARG B 1 202 ? -7.476  -45.371 5.788   1.00 85.29  ? 202 ARG B CA  1 
ATOM   3614 C  C   . ARG B 1 202 ? -8.304  -44.469 6.714   1.00 77.32  ? 202 ARG B C   1 
ATOM   3615 O  O   . ARG B 1 202 ? -8.194  -44.635 7.935   1.00 75.35  ? 202 ARG B O   1 
ATOM   3616 C  CB  . ARG B 1 202 ? -8.153  -46.707 5.478   1.00 93.08  ? 202 ARG B CB  1 
ATOM   3617 C  CG  . ARG B 1 202 ? -8.540  -47.486 6.723   1.00 103.33 ? 202 ARG B CG  1 
ATOM   3618 C  CD  . ARG B 1 202 ? -8.852  -48.935 6.451   1.00 114.75 ? 202 ARG B CD  1 
ATOM   3619 N  NE  . ARG B 1 202 ? -7.669  -49.781 6.447   1.00 124.10 ? 202 ARG B NE  1 
ATOM   3620 C  CZ  . ARG B 1 202 ? -7.672  -51.100 6.662   1.00 130.20 ? 202 ARG B CZ  1 
ATOM   3621 N  NH1 . ARG B 1 202 ? -8.802  -51.744 6.913   1.00 131.73 ? 202 ARG B NH1 1 
ATOM   3622 N  NH2 . ARG B 1 202 ? -6.535  -51.773 6.631   1.00 132.81 ? 202 ARG B NH2 1 
ATOM   3623 N  N   . VAL B 1 203 ? -9.056  -43.529 6.138   1.00 67.28  ? 203 VAL B N   1 
ATOM   3624 C  CA  . VAL B 1 203 ? -9.876  -42.522 6.871   1.00 58.34  ? 203 VAL B CA  1 
ATOM   3625 C  C   . VAL B 1 203 ? -11.319 -42.671 6.408   1.00 56.76  ? 203 VAL B C   1 
ATOM   3626 O  O   . VAL B 1 203 ? -11.546 -42.667 5.192   1.00 59.95  ? 203 VAL B O   1 
ATOM   3627 C  CB  . VAL B 1 203 ? -9.387  -41.086 6.623   1.00 55.88  ? 203 VAL B CB  1 
ATOM   3628 C  CG1 . VAL B 1 203 ? -10.321 -40.076 7.264   1.00 56.11  ? 203 VAL B CG1 1 
ATOM   3629 C  CG2 . VAL B 1 203 ? -7.964  -40.878 7.106   1.00 56.26  ? 203 VAL B CG2 1 
ATOM   3630 N  N   . TYR B 1 204 ? -12.250 -42.781 7.350   1.00 57.72  ? 204 TYR B N   1 
ATOM   3631 C  CA  . TYR B 1 204 ? -13.698 -42.929 7.067   1.00 57.62  ? 204 TYR B CA  1 
ATOM   3632 C  C   . TYR B 1 204 ? -14.431 -41.676 7.532   1.00 51.47  ? 204 TYR B C   1 
ATOM   3633 O  O   . TYR B 1 204 ? -13.899 -40.955 8.385   1.00 48.59  ? 204 TYR B O   1 
ATOM   3634 C  CB  . TYR B 1 204 ? -14.240 -44.186 7.745   1.00 62.09  ? 204 TYR B CB  1 
ATOM   3635 C  CG  . TYR B 1 204 ? -13.542 -45.452 7.321   1.00 67.05  ? 204 TYR B CG  1 
ATOM   3636 C  CD1 . TYR B 1 204 ? -13.962 -46.162 6.205   1.00 67.90  ? 204 TYR B CD1 1 
ATOM   3637 C  CD2 . TYR B 1 204 ? -12.429 -45.914 8.007   1.00 67.09  ? 204 TYR B CD2 1 
ATOM   3638 C  CE1 . TYR B 1 204 ? -13.322 -47.320 5.805   1.00 66.87  ? 204 TYR B CE1 1 
ATOM   3639 C  CE2 . TYR B 1 204 ? -11.777 -47.071 7.618   1.00 68.08  ? 204 TYR B CE2 1 
ATOM   3640 C  CZ  . TYR B 1 204 ? -12.225 -47.774 6.514   1.00 68.42  ? 204 TYR B CZ  1 
ATOM   3641 O  OH  . TYR B 1 204 ? -11.599 -48.916 6.119   1.00 73.05  ? 204 TYR B OH  1 
ATOM   3642 N  N   . GLN B 1 205 ? -15.607 -41.430 6.962   1.00 48.71  ? 205 GLN B N   1 
ATOM   3643 C  CA  . GLN B 1 205 ? -16.497 -40.307 7.343   1.00 49.40  ? 205 GLN B CA  1 
ATOM   3644 C  C   . GLN B 1 205 ? -17.899 -40.871 7.557   1.00 49.20  ? 205 GLN B C   1 
ATOM   3645 O  O   . GLN B 1 205 ? -18.551 -41.220 6.573   1.00 55.48  ? 205 GLN B O   1 
ATOM   3646 C  CB  . GLN B 1 205 ? -16.470 -39.211 6.276   1.00 50.02  ? 205 GLN B CB  1 
ATOM   3647 C  CG  . GLN B 1 205 ? -17.519 -38.119 6.459   1.00 50.82  ? 205 GLN B CG  1 
ATOM   3648 C  CD  . GLN B 1 205 ? -17.159 -37.077 7.495   1.00 52.15  ? 205 GLN B CD  1 
ATOM   3649 O  OE1 . GLN B 1 205 ? -16.002 -36.695 7.669   1.00 50.38  ? 205 GLN B OE1 1 
ATOM   3650 N  NE2 . GLN B 1 205 ? -18.165 -36.575 8.189   1.00 52.13  ? 205 GLN B NE2 1 
ATOM   3651 N  N   . LEU B 1 206 ? -18.315 -40.982 8.814   1.00 48.34  ? 206 LEU B N   1 
ATOM   3652 C  CA  . LEU B 1 206 ? -19.725 -41.231 9.198   1.00 48.58  ? 206 LEU B CA  1 
ATOM   3653 C  C   . LEU B 1 206 ? -20.585 -40.208 8.446   1.00 47.91  ? 206 LEU B C   1 
ATOM   3654 O  O   . LEU B 1 206 ? -20.291 -39.010 8.546   1.00 46.95  ? 206 LEU B O   1 
ATOM   3655 C  CB  . LEU B 1 206 ? -19.835 -41.087 10.720  1.00 48.95  ? 206 LEU B CB  1 
ATOM   3656 C  CG  . LEU B 1 206 ? -21.174 -41.466 11.356  1.00 49.81  ? 206 LEU B CG  1 
ATOM   3657 C  CD1 . LEU B 1 206 ? -21.615 -42.866 10.959  1.00 49.31  ? 206 LEU B CD1 1 
ATOM   3658 C  CD2 . LEU B 1 206 ? -21.097 -41.341 12.870  1.00 50.53  ? 206 LEU B CD2 1 
ATOM   3659 N  N   . ASN B 1 207 ? -21.575 -40.672 7.682   1.00 48.68  ? 207 ASN B N   1 
ATOM   3660 C  CA  . ASN B 1 207 ? -22.373 -39.815 6.773   1.00 50.37  ? 207 ASN B CA  1 
ATOM   3661 C  C   . ASN B 1 207 ? -23.812 -40.325 6.703   1.00 48.13  ? 207 ASN B C   1 
ATOM   3662 O  O   . ASN B 1 207 ? -24.056 -41.419 6.202   1.00 48.24  ? 207 ASN B O   1 
ATOM   3663 C  CB  . ASN B 1 207 ? -21.706 -39.737 5.403   1.00 51.54  ? 207 ASN B CB  1 
ATOM   3664 C  CG  . ASN B 1 207 ? -22.641 -39.219 4.339   1.00 54.21  ? 207 ASN B CG  1 
ATOM   3665 O  OD1 . ASN B 1 207 ? -23.169 -38.116 4.449   1.00 56.13  ? 207 ASN B OD1 1 
ATOM   3666 N  ND2 . ASN B 1 207 ? -22.847 -40.008 3.299   1.00 61.00  ? 207 ASN B ND2 1 
ATOM   3667 N  N   . PRO B 1 208 ? -24.817 -39.532 7.144   1.00 46.09  ? 208 PRO B N   1 
ATOM   3668 C  CA  . PRO B 1 208 ? -24.586 -38.205 7.718   1.00 46.59  ? 208 PRO B CA  1 
ATOM   3669 C  C   . PRO B 1 208 ? -23.692 -38.204 8.967   1.00 47.00  ? 208 PRO B C   1 
ATOM   3670 O  O   . PRO B 1 208 ? -23.582 -39.224 9.608   1.00 50.50  ? 208 PRO B O   1 
ATOM   3671 C  CB  . PRO B 1 208 ? -25.987 -37.692 8.091   1.00 46.71  ? 208 PRO B CB  1 
ATOM   3672 C  CG  . PRO B 1 208 ? -26.882 -38.915 8.047   1.00 47.86  ? 208 PRO B CG  1 
ATOM   3673 C  CD  . PRO B 1 208 ? -26.246 -39.848 7.038   1.00 46.54  ? 208 PRO B CD  1 
ATOM   3674 N  N   . ALA B 1 209 ? -23.070 -37.059 9.259   1.00 47.64  ? 209 ALA B N   1 
ATOM   3675 C  CA  . ALA B 1 209 ? -22.235 -36.813 10.458  1.00 48.93  ? 209 ALA B CA  1 
ATOM   3676 C  C   . ALA B 1 209 ? -23.144 -36.743 11.687  1.00 50.72  ? 209 ALA B C   1 
ATOM   3677 O  O   . ALA B 1 209 ? -24.377 -36.771 11.513  1.00 52.84  ? 209 ALA B O   1 
ATOM   3678 C  CB  . ALA B 1 209 ? -21.430 -35.537 10.307  1.00 49.59  ? 209 ALA B CB  1 
ATOM   3679 N  N   . ILE B 1 210 ? -22.556 -36.651 12.879  1.00 50.98  ? 210 ILE B N   1 
ATOM   3680 C  CA  . ILE B 1 210 ? -23.329 -36.563 14.151  1.00 54.10  ? 210 ILE B CA  1 
ATOM   3681 C  C   . ILE B 1 210 ? -22.917 -35.328 14.955  1.00 51.07  ? 210 ILE B C   1 
ATOM   3682 O  O   . ILE B 1 210 ? -23.600 -35.054 15.941  1.00 51.32  ? 210 ILE B O   1 
ATOM   3683 C  CB  . ILE B 1 210 ? -23.193 -37.865 14.959  1.00 57.54  ? 210 ILE B CB  1 
ATOM   3684 C  CG1 . ILE B 1 210 ? -21.729 -38.247 15.182  1.00 58.49  ? 210 ILE B CG1 1 
ATOM   3685 C  CG2 . ILE B 1 210 ? -23.967 -38.979 14.274  1.00 61.34  ? 210 ILE B CG2 1 
ATOM   3686 C  CD1 . ILE B 1 210 ? -21.533 -39.304 16.247  1.00 58.72  ? 210 ILE B CD1 1 
ATOM   3687 N  N   . CYS B 1 211 ? -21.907 -34.572 14.522  1.00 50.58  ? 211 CYS B N   1 
ATOM   3688 C  CA  . CYS B 1 211 ? -21.517 -33.310 15.196  1.00 51.93  ? 211 CYS B CA  1 
ATOM   3689 C  C   . CYS B 1 211 ? -21.041 -32.275 14.173  1.00 53.56  ? 211 CYS B C   1 
ATOM   3690 O  O   . CYS B 1 211 ? -20.960 -32.623 12.975  1.00 61.64  ? 211 CYS B O   1 
ATOM   3691 C  CB  . CYS B 1 211 ? -20.480 -33.573 16.280  1.00 51.95  ? 211 CYS B CB  1 
ATOM   3692 S  SG  . CYS B 1 211 ? -18.916 -34.241 15.662  1.00 52.45  ? 211 CYS B SG  1 
ATOM   3693 N  N   . VAL B 1 212 ? -20.791 -31.048 14.641  1.00 53.87  ? 212 VAL B N   1 
ATOM   3694 C  CA  . VAL B 1 212 ? -20.413 -29.854 13.824  1.00 51.96  ? 212 VAL B CA  1 
ATOM   3695 C  C   . VAL B 1 212 ? -19.868 -28.778 14.765  1.00 51.99  ? 212 VAL B C   1 
ATOM   3696 O  O   . VAL B 1 212 ? -20.416 -28.653 15.873  1.00 52.24  ? 212 VAL B O   1 
ATOM   3697 C  CB  . VAL B 1 212 ? -21.609 -29.299 13.027  1.00 52.40  ? 212 VAL B CB  1 
ATOM   3698 C  CG1 . VAL B 1 212 ? -22.871 -29.207 13.870  1.00 50.87  ? 212 VAL B CG1 1 
ATOM   3699 C  CG2 . VAL B 1 212 ? -21.292 -27.940 12.415  1.00 54.56  ? 212 VAL B CG2 1 
ATOM   3700 N  N   . GLN B 1 213 ? -18.872 -28.009 14.317  1.00 52.69  ? 213 GLN B N   1 
ATOM   3701 C  CA  . GLN B 1 213 ? -18.330 -26.855 15.078  1.00 53.61  ? 213 GLN B CA  1 
ATOM   3702 C  C   . GLN B 1 213 ? -19.409 -25.772 15.186  1.00 57.45  ? 213 GLN B C   1 
ATOM   3703 O  O   . GLN B 1 213 ? -20.109 -25.499 14.182  1.00 59.52  ? 213 GLN B O   1 
ATOM   3704 C  CB  . GLN B 1 213 ? -17.038 -26.344 14.443  1.00 52.46  ? 213 GLN B CB  1 
ATOM   3705 C  CG  . GLN B 1 213 ? -15.975 -27.426 14.288  1.00 52.41  ? 213 GLN B CG  1 
ATOM   3706 C  CD  . GLN B 1 213 ? -14.558 -26.928 14.471  1.00 53.64  ? 213 GLN B CD  1 
ATOM   3707 O  OE1 . GLN B 1 213 ? -14.294 -26.042 15.281  1.00 56.19  ? 213 GLN B OE1 1 
ATOM   3708 N  NE2 . GLN B 1 213 ? -13.622 -27.511 13.734  1.00 52.74  ? 213 GLN B NE2 1 
ATOM   3709 N  N   . GLU B 1 214 ? -19.527 -25.181 16.375  1.00 61.81  ? 214 GLU B N   1 
ATOM   3710 C  CA  . GLU B 1 214 ? -20.675 -24.340 16.813  1.00 68.64  ? 214 GLU B CA  1 
ATOM   3711 C  C   . GLU B 1 214 ? -21.100 -23.416 15.667  1.00 67.71  ? 214 GLU B C   1 
ATOM   3712 O  O   . GLU B 1 214 ? -22.263 -23.492 15.238  1.00 67.39  ? 214 GLU B O   1 
ATOM   3713 C  CB  . GLU B 1 214 ? -20.301 -23.525 18.058  1.00 78.39  ? 214 GLU B CB  1 
ATOM   3714 C  CG  . GLU B 1 214 ? -21.453 -23.275 19.023  1.00 85.13  ? 214 GLU B CG  1 
ATOM   3715 C  CD  . GLU B 1 214 ? -21.106 -23.508 20.492  1.00 91.70  ? 214 GLU B CD  1 
ATOM   3716 O  OE1 . GLU B 1 214 ? -22.037 -23.539 21.332  1.00 97.67  ? 214 GLU B OE1 1 
ATOM   3717 O  OE2 . GLU B 1 214 ? -19.903 -23.674 20.798  1.00 92.99  ? 214 GLU B OE2 1 
ATOM   3718 N  N   . LEU B 1 215 ? -20.170 -22.604 15.163  1.00 64.61  ? 215 LEU B N   1 
ATOM   3719 C  CA  . LEU B 1 215 ? -20.494 -21.411 14.346  1.00 64.61  ? 215 LEU B CA  1 
ATOM   3720 C  C   . LEU B 1 215 ? -20.323 -21.716 12.857  1.00 62.73  ? 215 LEU B C   1 
ATOM   3721 O  O   . LEU B 1 215 ? -20.348 -20.756 12.070  1.00 61.79  ? 215 LEU B O   1 
ATOM   3722 C  CB  . LEU B 1 215 ? -19.581 -20.262 14.786  1.00 67.99  ? 215 LEU B CB  1 
ATOM   3723 C  CG  . LEU B 1 215 ? -20.311 -18.950 15.070  1.00 72.52  ? 215 LEU B CG  1 
ATOM   3724 C  CD1 . LEU B 1 215 ? -21.007 -19.008 16.425  1.00 72.76  ? 215 LEU B CD1 1 
ATOM   3725 C  CD2 . LEU B 1 215 ? -19.359 -17.769 14.992  1.00 73.77  ? 215 LEU B CD2 1 
ATOM   3726 N  N   . GLN B 1 216 ? -20.164 -22.988 12.485  1.00 61.56  ? 216 GLN B N   1 
ATOM   3727 C  CA  . GLN B 1 216 ? -19.809 -23.398 11.104  1.00 57.98  ? 216 GLN B CA  1 
ATOM   3728 C  C   . GLN B 1 216 ? -20.928 -22.945 10.166  1.00 55.68  ? 216 GLN B C   1 
ATOM   3729 O  O   . GLN B 1 216 ? -20.611 -22.344 9.117   1.00 59.19  ? 216 GLN B O   1 
ATOM   3730 C  CB  . GLN B 1 216 ? -19.581 -24.907 11.033  1.00 60.99  ? 216 GLN B CB  1 
ATOM   3731 C  CG  . GLN B 1 216 ? -19.004 -25.395 9.710   1.00 65.16  ? 216 GLN B CG  1 
ATOM   3732 C  CD  . GLN B 1 216 ? -17.670 -24.801 9.317   1.00 66.22  ? 216 GLN B CD  1 
ATOM   3733 O  OE1 . GLN B 1 216 ? -17.317 -24.781 8.139   1.00 62.67  ? 216 GLN B OE1 1 
ATOM   3734 N  NE2 . GLN B 1 216 ? -16.900 -24.341 10.293  1.00 67.84  ? 216 GLN B NE2 1 
ATOM   3735 N  N   . LEU B 1 217 ? -22.180 -23.192 10.558  1.00 52.74  ? 217 LEU B N   1 
ATOM   3736 C  CA  . LEU B 1 217 ? -23.385 -22.821 9.773   1.00 53.31  ? 217 LEU B CA  1 
ATOM   3737 C  C   . LEU B 1 217 ? -23.349 -21.326 9.436   1.00 53.96  ? 217 LEU B C   1 
ATOM   3738 O  O   . LEU B 1 217 ? -23.352 -20.991 8.241   1.00 52.42  ? 217 LEU B O   1 
ATOM   3739 C  CB  . LEU B 1 217 ? -24.638 -23.169 10.579  1.00 53.56  ? 217 LEU B CB  1 
ATOM   3740 C  CG  . LEU B 1 217 ? -25.965 -22.758 9.944   1.00 52.99  ? 217 LEU B CG  1 
ATOM   3741 C  CD1 . LEU B 1 217 ? -26.068 -23.274 8.519   1.00 55.16  ? 217 LEU B CD1 1 
ATOM   3742 C  CD2 . LEU B 1 217 ? -27.144 -23.248 10.767  1.00 54.53  ? 217 LEU B CD2 1 
ATOM   3743 N  N   . ASN B 1 218 ? -23.307 -20.467 10.459  1.00 56.66  ? 218 ASN B N   1 
ATOM   3744 C  CA  . ASN B 1 218 ? -23.336 -18.986 10.302  1.00 58.60  ? 218 ASN B CA  1 
ATOM   3745 C  C   . ASN B 1 218 ? -22.276 -18.590 9.272   1.00 57.28  ? 218 ASN B C   1 
ATOM   3746 O  O   . ASN B 1 218 ? -22.567 -17.746 8.402   1.00 53.42  ? 218 ASN B O   1 
ATOM   3747 C  CB  . ASN B 1 218 ? -23.085 -18.238 11.615  1.00 63.36  ? 218 ASN B CB  1 
ATOM   3748 C  CG  . ASN B 1 218 ? -23.600 -18.967 12.841  1.00 70.68  ? 218 ASN B CG  1 
ATOM   3749 O  OD1 . ASN B 1 218 ? -23.401 -20.176 12.984  1.00 76.40  ? 218 ASN B OD1 1 
ATOM   3750 N  ND2 . ASN B 1 218 ? -24.237 -18.241 13.745  1.00 71.50  ? 218 ASN B ND2 1 
ATOM   3751 N  N   . GLN B 1 219 ? -21.095 -19.202 9.384   1.00 57.94  ? 219 GLN B N   1 
ATOM   3752 C  CA  . GLN B 1 219 ? -19.924 -18.932 8.522   1.00 57.85  ? 219 GLN B CA  1 
ATOM   3753 C  C   . GLN B 1 219 ? -20.173 -19.498 7.126   1.00 56.97  ? 219 GLN B C   1 
ATOM   3754 O  O   . GLN B 1 219 ? -19.944 -18.759 6.160   1.00 59.91  ? 219 GLN B O   1 
ATOM   3755 C  CB  . GLN B 1 219 ? -18.662 -19.546 9.114   1.00 62.19  ? 219 GLN B CB  1 
ATOM   3756 C  CG  . GLN B 1 219 ? -17.408 -18.842 8.626   1.00 66.62  ? 219 GLN B CG  1 
ATOM   3757 C  CD  . GLN B 1 219 ? -16.332 -19.812 8.207   1.00 70.63  ? 219 GLN B CD  1 
ATOM   3758 O  OE1 . GLN B 1 219 ? -16.112 -20.846 8.841   1.00 72.50  ? 219 GLN B OE1 1 
ATOM   3759 N  NE2 . GLN B 1 219 ? -15.658 -19.475 7.120   1.00 72.22  ? 219 GLN B NE2 1 
ATOM   3760 N  N   . GLU B 1 220 ? -20.597 -20.760 7.023   1.00 53.25  ? 220 GLU B N   1 
ATOM   3761 C  CA  . GLU B 1 220 ? -20.981 -21.402 5.733   1.00 51.16  ? 220 GLU B CA  1 
ATOM   3762 C  C   . GLU B 1 220 ? -21.937 -20.472 4.967   1.00 47.74  ? 220 GLU B C   1 
ATOM   3763 O  O   . GLU B 1 220 ? -21.639 -20.138 3.815   1.00 51.03  ? 220 GLU B O   1 
ATOM   3764 C  CB  . GLU B 1 220 ? -21.622 -22.769 5.987   1.00 51.47  ? 220 GLU B CB  1 
ATOM   3765 C  CG  . GLU B 1 220 ? -21.530 -23.730 4.815   1.00 53.35  ? 220 GLU B CG  1 
ATOM   3766 C  CD  . GLU B 1 220 ? -20.726 -25.010 5.015   1.00 55.31  ? 220 GLU B CD  1 
ATOM   3767 O  OE1 . GLU B 1 220 ? -20.739 -25.862 4.081   1.00 57.70  ? 220 GLU B OE1 1 
ATOM   3768 O  OE2 . GLU B 1 220 ? -20.085 -25.164 6.086   1.00 52.97  ? 220 GLU B OE2 1 
ATOM   3769 N  N   . ALA B 1 221 ? -23.034 -20.053 5.594   1.00 47.66  ? 221 ALA B N   1 
ATOM   3770 C  CA  . ALA B 1 221 ? -24.035 -19.119 5.021   1.00 46.48  ? 221 ALA B CA  1 
ATOM   3771 C  C   . ALA B 1 221 ? -23.350 -17.808 4.621   1.00 46.56  ? 221 ALA B C   1 
ATOM   3772 O  O   . ALA B 1 221 ? -23.545 -17.351 3.491   1.00 47.64  ? 221 ALA B O   1 
ATOM   3773 C  CB  . ALA B 1 221 ? -25.141 -18.864 6.018   1.00 47.53  ? 221 ALA B CB  1 
ATOM   3774 N  N   . SER B 1 222 ? -22.578 -17.219 5.534   1.00 48.84  ? 222 SER B N   1 
ATOM   3775 C  CA  . SER B 1 222 ? -21.879 -15.929 5.318   1.00 49.65  ? 222 SER B CA  1 
ATOM   3776 C  C   . SER B 1 222 ? -20.973 -16.022 4.083   1.00 49.20  ? 222 SER B C   1 
ATOM   3777 O  O   . SER B 1 222 ? -20.864 -15.007 3.372   1.00 52.09  ? 222 SER B O   1 
ATOM   3778 C  CB  . SER B 1 222 ? -21.110 -15.512 6.536   1.00 50.21  ? 222 SER B CB  1 
ATOM   3779 O  OG  . SER B 1 222 ? -20.115 -14.562 6.188   1.00 52.96  ? 222 SER B OG  1 
ATOM   3780 N  N   . LEU B 1 223 ? -20.362 -17.186 3.839   1.00 46.70  ? 223 LEU B N   1 
ATOM   3781 C  CA  . LEU B 1 223 ? -19.444 -17.426 2.694   1.00 44.13  ? 223 LEU B CA  1 
ATOM   3782 C  C   . LEU B 1 223 ? -20.192 -17.261 1.376   1.00 43.39  ? 223 LEU B C   1 
ATOM   3783 O  O   . LEU B 1 223 ? -19.606 -16.629 0.454   1.00 43.75  ? 223 LEU B O   1 
ATOM   3784 C  CB  . LEU B 1 223 ? -18.851 -18.834 2.766   1.00 46.19  ? 223 LEU B CB  1 
ATOM   3785 C  CG  . LEU B 1 223 ? -17.648 -19.016 3.690   1.00 48.84  ? 223 LEU B CG  1 
ATOM   3786 C  CD1 . LEU B 1 223 ? -17.266 -20.487 3.780   1.00 49.11  ? 223 LEU B CD1 1 
ATOM   3787 C  CD2 . LEU B 1 223 ? -16.461 -18.193 3.219   1.00 49.69  ? 223 LEU B CD2 1 
ATOM   3788 N  N   . LEU B 1 224 ? -21.397 -17.829 1.285   1.00 40.50  ? 224 LEU B N   1 
ATOM   3789 C  CA  . LEU B 1 224 ? -22.217 -17.835 0.043   1.00 39.26  ? 224 LEU B CA  1 
ATOM   3790 C  C   . LEU B 1 224 ? -22.872 -16.478 -0.182  1.00 39.63  ? 224 LEU B C   1 
ATOM   3791 O  O   . LEU B 1 224 ? -23.032 -16.093 -1.350  1.00 41.13  ? 224 LEU B O   1 
ATOM   3792 C  CB  . LEU B 1 224 ? -23.313 -18.891 0.164   1.00 37.22  ? 224 LEU B CB  1 
ATOM   3793 C  CG  . LEU B 1 224 ? -22.858 -20.313 -0.120  1.00 37.36  ? 224 LEU B CG  1 
ATOM   3794 C  CD1 . LEU B 1 224 ? -23.976 -21.307 0.143   1.00 37.00  ? 224 LEU B CD1 1 
ATOM   3795 C  CD2 . LEU B 1 224 ? -22.348 -20.430 -1.547  1.00 37.57  ? 224 LEU B CD2 1 
ATOM   3796 N  N   . VAL B 1 225 ? -23.307 -15.841 0.898   1.00 39.76  ? 225 VAL B N   1 
ATOM   3797 C  CA  . VAL B 1 225 ? -24.150 -14.619 0.817   1.00 41.30  ? 225 VAL B CA  1 
ATOM   3798 C  C   . VAL B 1 225 ? -23.253 -13.437 0.464   1.00 43.72  ? 225 VAL B C   1 
ATOM   3799 O  O   . VAL B 1 225 ? -23.673 -12.620 -0.357  1.00 48.69  ? 225 VAL B O   1 
ATOM   3800 C  CB  . VAL B 1 225 ? -24.936 -14.371 2.112   1.00 43.10  ? 225 VAL B CB  1 
ATOM   3801 C  CG1 . VAL B 1 225 ? -25.608 -13.009 2.093   1.00 43.74  ? 225 VAL B CG1 1 
ATOM   3802 C  CG2 . VAL B 1 225 ? -25.956 -15.472 2.359   1.00 44.19  ? 225 VAL B CG2 1 
ATOM   3803 N  N   . SER B 1 226 ? -22.065 -13.346 1.062   1.00 47.12  ? 226 SER B N   1 
ATOM   3804 C  CA  . SER B 1 226 ? -21.142 -12.191 0.900   1.00 49.48  ? 226 SER B CA  1 
ATOM   3805 C  C   . SER B 1 226 ? -19.708 -12.658 0.652   1.00 54.51  ? 226 SER B C   1 
ATOM   3806 O  O   . SER B 1 226 ? -19.225 -13.529 1.404   1.00 60.68  ? 226 SER B O   1 
ATOM   3807 C  CB  . SER B 1 226 ? -21.192 -11.317 2.106   1.00 47.79  ? 226 SER B CB  1 
ATOM   3808 O  OG  . SER B 1 226 ? -20.623 -12.000 3.203   1.00 47.02  ? 226 SER B OG  1 
ATOM   3809 N  N   . ASN B 1 227 ? -19.045 -12.034 -0.328  1.00 58.93  ? 227 ASN B N   1 
ATOM   3810 C  CA  . ASN B 1 227 ? -17.597 -12.214 -0.631  1.00 63.34  ? 227 ASN B CA  1 
ATOM   3811 C  C   . ASN B 1 227 ? -16.961 -10.825 -0.771  1.00 64.56  ? 227 ASN B C   1 
ATOM   3812 O  O   . ASN B 1 227 ? -17.690 -9.832  -0.640  1.00 62.58  ? 227 ASN B O   1 
ATOM   3813 C  CB  . ASN B 1 227 ? -17.375 -13.099 -1.864  1.00 64.90  ? 227 ASN B CB  1 
ATOM   3814 C  CG  . ASN B 1 227 ? -16.337 -14.183 -1.639  1.00 68.82  ? 227 ASN B CG  1 
ATOM   3815 O  OD1 . ASN B 1 227 ? -15.239 -14.106 -2.186  1.00 68.38  ? 227 ASN B OD1 1 
ATOM   3816 N  ND2 . ASN B 1 227 ? -16.666 -15.180 -0.826  1.00 67.98  ? 227 ASN B ND2 1 
ATOM   3817 N  N   . LEU B 1 228 ? -15.651 -10.760 -1.023  1.00 70.12  ? 228 LEU B N   1 
ATOM   3818 C  CA  . LEU B 1 228 ? -14.851 -9.506  -1.003  1.00 73.62  ? 228 LEU B CA  1 
ATOM   3819 C  C   . LEU B 1 228 ? -14.472 -9.049  -2.421  1.00 76.61  ? 228 LEU B C   1 
ATOM   3820 O  O   . LEU B 1 228 ? -14.216 -9.911  -3.285  1.00 79.31  ? 228 LEU B O   1 
ATOM   3821 C  CB  . LEU B 1 228 ? -13.601 -9.768  -0.161  1.00 74.16  ? 228 LEU B CB  1 
ATOM   3822 C  CG  . LEU B 1 228 ? -13.867 -9.867  1.337   1.00 77.68  ? 228 LEU B CG  1 
ATOM   3823 C  CD1 . LEU B 1 228 ? -13.173 -11.078 1.953   1.00 77.65  ? 228 LEU B CD1 1 
ATOM   3824 C  CD2 . LEU B 1 228 ? -13.455 -8.574  2.026   1.00 79.13  ? 228 LEU B CD2 1 
ATOM   3825 N  N   . GLU B 1 229 ? -14.426 -7.730  -2.638  1.00 78.56  ? 229 GLU B N   1 
ATOM   3826 C  CA  . GLU B 1 229 ? -13.904 -7.092  -3.879  1.00 85.02  ? 229 GLU B CA  1 
ATOM   3827 C  C   . GLU B 1 229 ? -12.371 -7.143  -3.861  1.00 90.08  ? 229 GLU B C   1 
ATOM   3828 O  O   . GLU B 1 229 ? -11.812 -7.645  -2.877  1.00 89.69  ? 229 GLU B O   1 
ATOM   3829 C  CB  . GLU B 1 229 ? -14.358 -5.633  -3.978  1.00 85.98  ? 229 GLU B CB  1 
ATOM   3830 C  CG  . GLU B 1 229 ? -15.863 -5.446  -4.099  1.00 86.14  ? 229 GLU B CG  1 
ATOM   3831 C  CD  . GLU B 1 229 ? -16.334 -3.997  -4.082  1.00 86.69  ? 229 GLU B CD  1 
ATOM   3832 O  OE1 . GLU B 1 229 ? -15.893 -3.240  -3.189  1.00 83.33  ? 229 GLU B OE1 1 
ATOM   3833 O  OE2 . GLU B 1 229 ? -17.146 -3.620  -4.962  1.00 87.27  ? 229 GLU B OE2 1 
ATOM   3834 N  N   . GLN B 1 230 ? -11.716 -6.622  -4.905  1.00 98.81  ? 230 GLN B N   1 
ATOM   3835 C  CA  . GLN B 1 230 ? -10.236 -6.488  -4.992  1.00 104.26 ? 230 GLN B CA  1 
ATOM   3836 C  C   . GLN B 1 230 ? -9.897  -5.132  -5.626  1.00 106.29 ? 230 GLN B C   1 
ATOM   3837 O  O   . GLN B 1 230 ? -9.085  -4.363  -5.109  1.00 104.13 ? 230 GLN B O   1 
ATOM   3838 C  CB  . GLN B 1 230 ? -9.639  -7.631  -5.816  1.00 111.03 ? 230 GLN B CB  1 
ATOM   3839 C  CG  . GLN B 1 230 ? -10.001 -9.028  -5.319  1.00 109.69 ? 230 GLN B CG  1 
ATOM   3840 C  CD  . GLN B 1 230 ? -9.715  -10.092 -6.352  1.00 112.93 ? 230 GLN B CD  1 
ATOM   3841 O  OE1 . GLN B 1 230 ? -9.755  -9.844  -7.557  1.00 121.96 ? 230 GLN B OE1 1 
ATOM   3842 N  NE2 . GLN B 1 230 ? -9.433  -11.299 -5.888  1.00 106.90 ? 230 GLN B NE2 1 
HETATM 3843 O  O   . HOH C 2 .   ? -16.248 -34.349 -20.404 1.00 53.14  ? 301 HOH A O   1 
HETATM 3844 O  O   . HOH D 2 .   ? -10.912 -27.458 14.040  1.00 46.71  ? 301 HOH B O   1 
HETATM 3845 O  O   . HOH D 2 .   ? -9.984  -25.969 22.487  1.00 32.49  ? 302 HOH B O   1 
HETATM 3846 O  O   . HOH D 2 .   ? -14.026 -23.555 13.471  1.00 30.58  ? 303 HOH B O   1 
HETATM 3847 O  O   . HOH D 2 .   ? -25.435 -53.407 14.215  1.00 31.79  ? 304 HOH B O   1 
HETATM 3848 O  O   . HOH D 2 .   ? -7.001  -26.116 21.964  1.00 48.81  ? 305 HOH B O   1 
# 
