data_9IXF
# 
_entry.id   9IXF 
# 
_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   9IXF         pdb_00009ixf 10.2210/pdb9ixf/pdb 
WWPDB D_1300049874 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2024-11-27 
3 'Structure model' 1 2 2025-01-01 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 3 'Structure model' '_citation.journal_volume'          
3 3 'Structure model' '_citation.page_first'              
4 3 'Structure model' '_citation.page_last'               
5 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2024-11-20 
_pdbx_database_PDB_obs_spr.pdb_id           9IXF 
_pdbx_database_PDB_obs_spr.replace_pdb_id   8IUV 
_pdbx_database_PDB_obs_spr.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                        9IXF 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-27 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9IXC unspecified 
PDB . 9IXD unspecified 
PDB . 9IXE unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              matoba@yasuda-u.ac.jp 
_pdbx_contact_author.name_first         Yasuyuki 
_pdbx_contact_author.name_last          Matoba 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0366-0851 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Oda, K.'    1 0000-0002-1095-548X 
'Matoba, Y.' 2 0000-0002-0366-0851 
# 
_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            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            291 
_citation.language                  ? 
_citation.page_first                5486 
_citation.page_last                 5505 
_citation.title                     'Copper inactivates DcsB by oxidizing the metal ligand Cys86 to sulfinic acid.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.17325 
_citation.pdbx_database_id_PubMed   39563074 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Oda, K.'       1 ? 
primary 'Komaguchi, K.' 2 ? 
primary 'Matoba, Y.'    3 ? 
# 
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 'N(omega)-hydroxy-L-arginine amidinohydrolase' 30016.701 2   3.5.3.25 ? 
'N(omega)-hydroxy-L-arginine amidinohydrolase' ? 
2 non-polymer syn 'MANGANESE (II) ION'                           54.938    1   ?        ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                24.305    4   ?        ? ? ? 
4 water       nat water                                          18.015    451 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        hydroxyarginase 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDDWSVALPQARETLVAVREAATESIKGDNLTV
LVNNTCSVSLATLPVVAREHPDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQAVLVGSRDIDE
GERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWDVLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELA
ELNAPADSERAEQAVAVILDMVAPAFDAAAARPLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDDWSVALPQARETLVAVREAATESIKGDNLTV
LVNNTCSVSLATLPVVAREHPDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQAVLVGSRDIDE
GERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWDVLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELA
ELNAPADSERAEQAVAVILDMVAPAFDAAAARPLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN  
3 'MAGNESIUM ION'      MG  
4 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ILE n 
1 3   ASP n 
1 4   LEU n 
1 5   ILE n 
1 6   VAL n 
1 7   SER n 
1 8   GLN n 
1 9   GLY n 
1 10  ARG n 
1 11  VAL n 
1 12  ALA n 
1 13  ASP n 
1 14  ARG n 
1 15  ALA n 
1 16  ALA n 
1 17  TRP n 
1 18  MET n 
1 19  ILE n 
1 20  GLU n 
1 21  GLY n 
1 22  ALA n 
1 23  ALA n 
1 24  ARG n 
1 25  THR n 
1 26  ALA n 
1 27  ARG n 
1 28  ALA n 
1 29  LEU n 
1 30  GLU n 
1 31  GLU n 
1 32  ARG n 
1 33  TYR n 
1 34  GLY n 
1 35  LEU n 
1 36  LYS n 
1 37  GLY n 
1 38  HIS n 
1 39  TYR n 
1 40  VAL n 
1 41  GLY n 
1 42  GLU n 
1 43  PRO n 
1 44  ALA n 
1 45  PRO n 
1 46  HIS n 
1 47  ALA n 
1 48  ASP n 
1 49  ASP n 
1 50  ASP n 
1 51  TRP n 
1 52  SER n 
1 53  VAL n 
1 54  ALA n 
1 55  LEU n 
1 56  PRO n 
1 57  GLN n 
1 58  ALA n 
1 59  ARG n 
1 60  GLU n 
1 61  THR n 
1 62  LEU n 
1 63  VAL n 
1 64  ALA n 
1 65  VAL n 
1 66  ARG n 
1 67  GLU n 
1 68  ALA n 
1 69  ALA n 
1 70  THR n 
1 71  GLU n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  GLY n 
1 76  ASP n 
1 77  ASN n 
1 78  LEU n 
1 79  THR n 
1 80  VAL n 
1 81  LEU n 
1 82  VAL n 
1 83  ASN n 
1 84  ASN n 
1 85  THR n 
1 86  CYS y 
1 86  CSO y 
1 87  SER n 
1 88  VAL n 
1 89  SER n 
1 90  LEU n 
1 91  ALA n 
1 92  THR n 
1 93  LEU n 
1 94  PRO n 
1 95  VAL n 
1 96  VAL n 
1 97  ALA n 
1 98  ARG n 
1 99  GLU n 
1 100 HIS n 
1 101 PRO n 
1 102 ASP n 
1 103 ALA n 
1 104 VAL n 
1 105 VAL n 
1 106 LEU n 
1 107 TYR n 
1 108 ILE n 
1 109 ASP n 
1 110 GLY n 
1 111 HIS n 
1 112 GLY n 
1 113 ASP n 
1 114 PHE n 
1 115 ASN n 
1 116 THR n 
1 117 PRO n 
1 118 GLU n 
1 119 THR n 
1 120 THR n 
1 121 ASP n 
1 122 THR n 
1 123 GLY n 
1 124 TYR n 
1 125 LEU n 
1 126 GLY n 
1 127 GLY n 
1 128 MET n 
1 129 VAL n 
1 130 LEU n 
1 131 SER n 
1 132 GLY n 
1 133 ALA n 
1 134 CYS n 
1 135 GLY n 
1 136 LEU n 
1 137 TRP n 
1 138 ASP n 
1 139 SER n 
1 140 GLY n 
1 141 HIS n 
1 142 GLY n 
1 143 ALA n 
1 144 GLY n 
1 145 LEU n 
1 146 ARG n 
1 147 PRO n 
1 148 GLU n 
1 149 GLN n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 VAL n 
1 154 GLY n 
1 155 SER n 
1 156 ARG n 
1 157 ASP n 
1 158 ILE n 
1 159 ASP n 
1 160 GLU n 
1 161 GLY n 
1 162 GLU n 
1 163 ARG n 
1 164 GLU n 
1 165 LEU n 
1 166 ILE n 
1 167 ARG n 
1 168 LYS n 
1 169 ALA n 
1 170 GLY n 
1 171 VAL n 
1 172 ARG n 
1 173 VAL n 
1 174 ILE n 
1 175 PRO n 
1 176 PRO n 
1 177 GLY n 
1 178 GLU n 
1 179 ALA n 
1 180 THR n 
1 181 ALA n 
1 182 GLN n 
1 183 ALA n 
1 184 VAL n 
1 185 LEU n 
1 186 ASP n 
1 187 ALA n 
1 188 VAL n 
1 189 LYS n 
1 190 ASP n 
1 191 ALA n 
1 192 PRO n 
1 193 VAL n 
1 194 TRP n 
1 195 ILE n 
1 196 HIS n 
1 197 ILE n 
1 198 ASP n 
1 199 TRP n 
1 200 ASP n 
1 201 VAL n 
1 202 LEU n 
1 203 GLU n 
1 204 PRO n 
1 205 GLY n 
1 206 SER n 
1 207 ILE n 
1 208 PRO n 
1 209 ALA n 
1 210 ASP n 
1 211 TYR n 
1 212 THR n 
1 213 VAL n 
1 214 PRO n 
1 215 ASP n 
1 216 GLY n 
1 217 MET n 
1 218 LEU n 
1 219 PRO n 
1 220 ALA n 
1 221 GLN n 
1 222 ILE n 
1 223 ARG n 
1 224 ALA n 
1 225 VAL n 
1 226 PHE n 
1 227 GLU n 
1 228 ALA n 
1 229 ILE n 
1 230 PRO n 
1 231 ALA n 
1 232 GLU n 
1 233 ARG n 
1 234 LEU n 
1 235 ILE n 
1 236 GLY n 
1 237 VAL n 
1 238 GLU n 
1 239 LEU n 
1 240 ALA n 
1 241 GLU n 
1 242 LEU n 
1 243 ASN n 
1 244 ALA n 
1 245 PRO n 
1 246 ALA n 
1 247 ASP n 
1 248 SER n 
1 249 GLU n 
1 250 ARG n 
1 251 ALA n 
1 252 GLU n 
1 253 GLN n 
1 254 ALA n 
1 255 VAL n 
1 256 ALA n 
1 257 VAL n 
1 258 ILE n 
1 259 LEU n 
1 260 ASP n 
1 261 MET n 
1 262 VAL n 
1 263 ALA n 
1 264 PRO n 
1 265 ALA n 
1 266 PHE n 
1 267 ASP n 
1 268 ALA n 
1 269 ALA n 
1 270 ALA n 
1 271 ALA n 
1 272 ARG n 
1 273 PRO n 
1 274 LEU n 
1 275 GLU n 
1 276 HIS n 
1 277 HIS n 
1 278 HIS n 
1 279 HIS n 
1 280 HIS n 
1 281 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                   281 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 dcsB 
_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      'Streptomyces lavendulae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1914 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 11924 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21 
_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 
CSO 'L-peptide linking' n S-HYDROXYCYSTEINE    ? 'C3 H7 N O3 S'   137.158 
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'      ? 'Mg 2'           24.305  
MN  non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'           54.938  
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   MET 1   1   1   MET MET A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  TRP 17  17  17  TRP TRP A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  HIS 38  38  38  HIS HIS A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  TRP 51  51  51  TRP TRP A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  CYS 86  86  86  CYS CYS A . y 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 MET 128 128 128 MET MET A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 CYS 134 134 134 CYS CYS A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 TRP 137 137 137 TRP TRP A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 HIS 141 141 141 HIS HIS A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 PRO 176 176 176 PRO PRO A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 LYS 189 189 189 LYS LYS A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 PRO 192 192 192 PRO PRO A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 TRP 199 199 199 TRP TRP A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ILE 207 207 207 ILE ILE 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 ASP 210 210 210 ASP ASP A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 MET 217 217 217 MET MET A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 PRO 245 245 245 PRO PRO A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 SER 248 248 248 SER SER A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 GLN 253 253 253 GLN GLN A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 MET 261 261 261 MET MET A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 ARG 272 272 272 ARG ARG A . n 
A 1 273 PRO 273 273 ?   ?   ?   A . n 
A 1 274 LEU 274 274 ?   ?   ?   A . n 
A 1 275 GLU 275 275 ?   ?   ?   A . n 
A 1 276 HIS 276 276 ?   ?   ?   A . n 
A 1 277 HIS 277 277 ?   ?   ?   A . n 
A 1 278 HIS 278 278 ?   ?   ?   A . n 
A 1 279 HIS 279 279 ?   ?   ?   A . n 
A 1 280 HIS 280 280 ?   ?   ?   A . n 
A 1 281 HIS 281 281 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ILE 2   2   2   ILE ILE B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLN 8   8   8   GLN GLN B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  ASP 13  13  13  ASP ASP B . n 
B 1 14  ARG 14  14  14  ARG ARG B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  TRP 17  17  17  TRP TRP B . n 
B 1 18  MET 18  18  18  MET MET B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  GLY 21  21  21  GLY GLY B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  ARG 24  24  24  ARG ARG B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  ARG 32  32  32  ARG ARG B . n 
B 1 33  TYR 33  33  33  TYR TYR B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  HIS 38  38  38  HIS HIS B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  ASP 49  49  49  ASP ASP B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  TRP 51  51  51  TRP TRP B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  ARG 59  59  59  ARG ARG B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  THR 61  61  61  THR THR B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  CYS 86  86  86  CYS CYS B . y 
B 1 86  CSO 86  86  86  CSO CSO B . y 
B 1 87  SER 87  87  87  SER SER B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  THR 92  92  92  THR THR B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  ARG 98  98  98  ARG ARG B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 PRO 101 101 101 PRO PRO B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 ASP 113 113 113 ASP ASP B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 PRO 117 117 117 PRO PRO B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 TYR 124 124 124 TYR TYR B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 GLY 126 126 126 GLY GLY B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 MET 128 128 128 MET MET B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 SER 131 131 131 SER SER B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 CYS 134 134 134 CYS CYS B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 TRP 137 137 137 TRP TRP B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 HIS 141 141 141 HIS HIS B . n 
B 1 142 GLY 142 142 142 GLY GLY B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ARG 146 146 146 ARG ARG B . n 
B 1 147 PRO 147 147 147 PRO PRO B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 GLN 149 149 149 GLN GLN B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 VAL 153 153 153 VAL VAL B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 ASP 159 159 159 ASP ASP B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 LEU 165 165 165 LEU LEU B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 PRO 176 176 176 PRO PRO B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 ALA 179 179 179 ALA ALA B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 GLN 182 182 182 GLN GLN B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ASP 186 186 186 ASP ASP B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 LYS 189 189 189 LYS LYS B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 PRO 192 192 192 PRO PRO B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 TRP 194 194 194 TRP TRP B . n 
B 1 195 ILE 195 195 195 ILE ILE B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 ILE 197 197 197 ILE ILE B . n 
B 1 198 ASP 198 198 198 ASP ASP B . n 
B 1 199 TRP 199 199 199 TRP TRP B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 GLU 203 203 203 GLU GLU B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 ILE 207 207 207 ILE ILE 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 ASP 210 210 210 ASP ASP B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 THR 212 212 212 THR THR B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 GLY 216 216 216 GLY GLY B . n 
B 1 217 MET 217 217 217 MET MET B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 PRO 219 219 219 PRO PRO B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 ARG 223 223 223 ARG ARG B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 PRO 230 230 230 PRO PRO B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 GLU 232 232 232 GLU GLU B . n 
B 1 233 ARG 233 233 233 ARG ARG B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 ILE 235 235 235 ILE ILE B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 VAL 237 237 237 VAL VAL B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 PRO 245 245 245 PRO PRO B . n 
B 1 246 ALA 246 246 246 ALA ALA B . n 
B 1 247 ASP 247 247 247 ASP ASP B . n 
B 1 248 SER 248 248 248 SER SER B . n 
B 1 249 GLU 249 249 249 GLU GLU B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 ALA 251 251 251 ALA ALA B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 GLN 253 253 253 GLN GLN B . n 
B 1 254 ALA 254 254 254 ALA ALA B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 MET 261 261 261 MET MET B . n 
B 1 262 VAL 262 262 262 VAL VAL B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 PRO 264 264 264 PRO PRO B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 ASP 267 267 267 ASP ASP B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 ALA 270 270 270 ALA ALA B . n 
B 1 271 ALA 271 271 271 ALA ALA B . n 
B 1 272 ARG 272 272 272 ARG ARG B . n 
B 1 273 PRO 273 273 273 PRO PRO B . n 
B 1 274 LEU 274 274 274 LEU LEU B . n 
B 1 275 GLU 275 275 ?   ?   ?   B . n 
B 1 276 HIS 276 276 ?   ?   ?   B . n 
B 1 277 HIS 277 277 ?   ?   ?   B . n 
B 1 278 HIS 278 278 ?   ?   ?   B . n 
B 1 279 HIS 279 279 ?   ?   ?   B . n 
B 1 280 HIS 280 280 ?   ?   ?   B . n 
B 1 281 HIS 281 281 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CSO ? ? CSO ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 MN  1   401 401  MN  MN  A . 
D 3 MG  1   402 402  MG  MG  A . 
E 3 MG  1   401 401  MG  MG  B . 
F 3 MG  1   402 402  MG  MG  B . 
G 3 MG  1   403 405  MG  MG  B . 
H 4 HOH 1   501 1198 HOH HOH A . 
H 4 HOH 2   502 1114 HOH HOH A . 
H 4 HOH 3   503 1381 HOH HOH A . 
H 4 HOH 4   504 1212 HOH HOH A . 
H 4 HOH 5   505 1187 HOH HOH A . 
H 4 HOH 6   506 1213 HOH HOH A . 
H 4 HOH 7   507 1093 HOH HOH A . 
H 4 HOH 8   508 1181 HOH HOH A . 
H 4 HOH 9   509 1115 HOH HOH A . 
H 4 HOH 10  510 1012 HOH HOH A . 
H 4 HOH 11  511 1070 HOH HOH A . 
H 4 HOH 12  512 1142 HOH HOH A . 
H 4 HOH 13  513 1152 HOH HOH A . 
H 4 HOH 14  514 1096 HOH HOH A . 
H 4 HOH 15  515 1119 HOH HOH A . 
H 4 HOH 16  516 1231 HOH HOH A . 
H 4 HOH 17  517 1076 HOH HOH A . 
H 4 HOH 18  518 1010 HOH HOH A . 
H 4 HOH 19  519 1145 HOH HOH A . 
H 4 HOH 20  520 1101 HOH HOH A . 
H 4 HOH 21  521 1128 HOH HOH A . 
H 4 HOH 22  522 1177 HOH HOH A . 
H 4 HOH 23  523 1102 HOH HOH A . 
H 4 HOH 24  524 1079 HOH HOH A . 
H 4 HOH 25  525 1095 HOH HOH A . 
H 4 HOH 26  526 1166 HOH HOH A . 
H 4 HOH 27  527 1057 HOH HOH A . 
H 4 HOH 28  528 1027 HOH HOH A . 
H 4 HOH 29  529 1112 HOH HOH A . 
H 4 HOH 30  530 1026 HOH HOH A . 
H 4 HOH 31  531 1073 HOH HOH A . 
H 4 HOH 32  532 1039 HOH HOH A . 
H 4 HOH 33  533 1109 HOH HOH A . 
H 4 HOH 34  534 1170 HOH HOH A . 
H 4 HOH 35  535 1097 HOH HOH A . 
H 4 HOH 36  536 1126 HOH HOH A . 
H 4 HOH 37  537 1005 HOH HOH A . 
H 4 HOH 38  538 1100 HOH HOH A . 
H 4 HOH 39  539 1071 HOH HOH A . 
H 4 HOH 40  540 1007 HOH HOH A . 
H 4 HOH 41  541 1044 HOH HOH A . 
H 4 HOH 42  542 1048 HOH HOH A . 
H 4 HOH 43  543 1029 HOH HOH A . 
H 4 HOH 44  544 1214 HOH HOH A . 
H 4 HOH 45  545 1034 HOH HOH A . 
H 4 HOH 46  546 1091 HOH HOH A . 
H 4 HOH 47  547 1184 HOH HOH A . 
H 4 HOH 48  548 1098 HOH HOH A . 
H 4 HOH 49  549 1191 HOH HOH A . 
H 4 HOH 50  550 1023 HOH HOH A . 
H 4 HOH 51  551 1062 HOH HOH A . 
H 4 HOH 52  552 1035 HOH HOH A . 
H 4 HOH 53  553 1075 HOH HOH A . 
H 4 HOH 54  554 1014 HOH HOH A . 
H 4 HOH 55  555 1047 HOH HOH A . 
H 4 HOH 56  556 1031 HOH HOH A . 
H 4 HOH 57  557 1103 HOH HOH A . 
H 4 HOH 58  558 1049 HOH HOH A . 
H 4 HOH 59  559 1135 HOH HOH A . 
H 4 HOH 60  560 1068 HOH HOH A . 
H 4 HOH 61  561 1055 HOH HOH A . 
H 4 HOH 62  562 1065 HOH HOH A . 
H 4 HOH 63  563 1195 HOH HOH A . 
H 4 HOH 64  564 1018 HOH HOH A . 
H 4 HOH 65  565 1032 HOH HOH A . 
H 4 HOH 66  566 1021 HOH HOH A . 
H 4 HOH 67  567 1087 HOH HOH A . 
H 4 HOH 68  568 1013 HOH HOH A . 
H 4 HOH 69  569 1156 HOH HOH A . 
H 4 HOH 70  570 1127 HOH HOH A . 
H 4 HOH 71  571 1105 HOH HOH A . 
H 4 HOH 72  572 1072 HOH HOH A . 
H 4 HOH 73  573 1016 HOH HOH A . 
H 4 HOH 74  574 1186 HOH HOH A . 
H 4 HOH 75  575 1082 HOH HOH A . 
H 4 HOH 76  576 1099 HOH HOH A . 
H 4 HOH 77  577 1022 HOH HOH A . 
H 4 HOH 78  578 1028 HOH HOH A . 
H 4 HOH 79  579 1024 HOH HOH A . 
H 4 HOH 80  580 1129 HOH HOH A . 
H 4 HOH 81  581 1113 HOH HOH A . 
H 4 HOH 82  582 1169 HOH HOH A . 
H 4 HOH 83  583 1059 HOH HOH A . 
H 4 HOH 84  584 1004 HOH HOH A . 
H 4 HOH 85  585 1060 HOH HOH A . 
H 4 HOH 86  586 1172 HOH HOH A . 
H 4 HOH 87  587 1001 HOH HOH A . 
H 4 HOH 88  588 1030 HOH HOH A . 
H 4 HOH 89  589 1002 HOH HOH A . 
H 4 HOH 90  590 1064 HOH HOH A . 
H 4 HOH 91  591 1151 HOH HOH A . 
H 4 HOH 92  592 1066 HOH HOH A . 
H 4 HOH 93  593 1116 HOH HOH A . 
H 4 HOH 94  594 1089 HOH HOH A . 
H 4 HOH 95  595 1063 HOH HOH A . 
H 4 HOH 96  596 1155 HOH HOH A . 
H 4 HOH 97  597 1019 HOH HOH A . 
H 4 HOH 98  598 1020 HOH HOH A . 
H 4 HOH 99  599 1199 HOH HOH A . 
H 4 HOH 100 600 1003 HOH HOH A . 
H 4 HOH 101 601 1193 HOH HOH A . 
H 4 HOH 102 602 1090 HOH HOH A . 
H 4 HOH 103 603 1148 HOH HOH A . 
H 4 HOH 104 604 1244 HOH HOH A . 
H 4 HOH 105 605 1052 HOH HOH A . 
H 4 HOH 106 606 1033 HOH HOH A . 
H 4 HOH 107 607 1180 HOH HOH A . 
H 4 HOH 108 608 1134 HOH HOH A . 
H 4 HOH 109 609 1123 HOH HOH A . 
H 4 HOH 110 610 1058 HOH HOH A . 
H 4 HOH 111 611 1054 HOH HOH A . 
H 4 HOH 112 612 1088 HOH HOH A . 
H 4 HOH 113 613 1008 HOH HOH A . 
H 4 HOH 114 614 1084 HOH HOH A . 
H 4 HOH 115 615 1448 HOH HOH A . 
H 4 HOH 116 616 1302 HOH HOH A . 
H 4 HOH 117 617 1443 HOH HOH A . 
H 4 HOH 118 618 1171 HOH HOH A . 
H 4 HOH 119 619 1159 HOH HOH A . 
H 4 HOH 120 620 1006 HOH HOH A . 
H 4 HOH 121 621 1133 HOH HOH A . 
H 4 HOH 122 622 1043 HOH HOH A . 
H 4 HOH 123 623 1179 HOH HOH A . 
H 4 HOH 124 624 1036 HOH HOH A . 
H 4 HOH 125 625 1053 HOH HOH A . 
H 4 HOH 126 626 1290 HOH HOH A . 
H 4 HOH 127 627 1106 HOH HOH A . 
H 4 HOH 128 628 1111 HOH HOH A . 
H 4 HOH 129 629 1138 HOH HOH A . 
H 4 HOH 130 630 1067 HOH HOH A . 
H 4 HOH 131 631 1011 HOH HOH A . 
H 4 HOH 132 632 1157 HOH HOH A . 
H 4 HOH 133 633 1025 HOH HOH A . 
H 4 HOH 134 634 1041 HOH HOH A . 
H 4 HOH 135 635 1141 HOH HOH A . 
H 4 HOH 136 636 1204 HOH HOH A . 
H 4 HOH 137 637 1162 HOH HOH A . 
H 4 HOH 138 638 1086 HOH HOH A . 
H 4 HOH 139 639 1396 HOH HOH A . 
H 4 HOH 140 640 1201 HOH HOH A . 
H 4 HOH 141 641 1038 HOH HOH A . 
H 4 HOH 142 642 1080 HOH HOH A . 
H 4 HOH 143 643 1042 HOH HOH A . 
H 4 HOH 144 644 1092 HOH HOH A . 
H 4 HOH 145 645 1185 HOH HOH A . 
H 4 HOH 146 646 1051 HOH HOH A . 
H 4 HOH 147 647 1301 HOH HOH A . 
H 4 HOH 148 648 1015 HOH HOH A . 
H 4 HOH 149 649 1017 HOH HOH A . 
H 4 HOH 150 650 1373 HOH HOH A . 
H 4 HOH 151 651 1056 HOH HOH A . 
H 4 HOH 152 652 1118 HOH HOH A . 
H 4 HOH 153 653 1283 HOH HOH A . 
H 4 HOH 154 654 1371 HOH HOH A . 
H 4 HOH 155 655 1287 HOH HOH A . 
H 4 HOH 156 656 1197 HOH HOH A . 
H 4 HOH 157 657 1104 HOH HOH A . 
H 4 HOH 158 658 1411 HOH HOH A . 
H 4 HOH 159 659 1164 HOH HOH A . 
H 4 HOH 160 660 1120 HOH HOH A . 
H 4 HOH 161 661 1150 HOH HOH A . 
H 4 HOH 162 662 1140 HOH HOH A . 
H 4 HOH 163 663 1061 HOH HOH A . 
H 4 HOH 164 664 1209 HOH HOH A . 
H 4 HOH 165 665 1147 HOH HOH A . 
H 4 HOH 166 666 1132 HOH HOH A . 
H 4 HOH 167 667 1194 HOH HOH A . 
H 4 HOH 168 668 1372 HOH HOH A . 
H 4 HOH 169 669 1143 HOH HOH A . 
H 4 HOH 170 670 1447 HOH HOH A . 
H 4 HOH 171 671 1160 HOH HOH A . 
H 4 HOH 172 672 1085 HOH HOH A . 
H 4 HOH 173 673 1139 HOH HOH A . 
H 4 HOH 174 674 1174 HOH HOH A . 
H 4 HOH 175 675 1165 HOH HOH A . 
H 4 HOH 176 676 1205 HOH HOH A . 
H 4 HOH 177 677 1273 HOH HOH A . 
H 4 HOH 178 678 1196 HOH HOH A . 
H 4 HOH 179 679 1050 HOH HOH A . 
H 4 HOH 180 680 1415 HOH HOH A . 
H 4 HOH 181 681 1117 HOH HOH A . 
H 4 HOH 182 682 1121 HOH HOH A . 
H 4 HOH 183 683 1338 HOH HOH A . 
H 4 HOH 184 684 1176 HOH HOH A . 
H 4 HOH 185 685 1268 HOH HOH A . 
H 4 HOH 186 686 1078 HOH HOH A . 
H 4 HOH 187 687 1083 HOH HOH A . 
H 4 HOH 188 688 1200 HOH HOH A . 
H 4 HOH 189 689 1074 HOH HOH A . 
H 4 HOH 190 690 1094 HOH HOH A . 
H 4 HOH 191 691 1136 HOH HOH A . 
H 4 HOH 192 692 1108 HOH HOH A . 
H 4 HOH 193 693 1161 HOH HOH A . 
H 4 HOH 194 694 1364 HOH HOH A . 
H 4 HOH 195 695 1314 HOH HOH A . 
H 4 HOH 196 696 1081 HOH HOH A . 
H 4 HOH 197 697 1405 HOH HOH A . 
H 4 HOH 198 698 1386 HOH HOH A . 
H 4 HOH 199 699 1077 HOH HOH A . 
H 4 HOH 200 700 1144 HOH HOH A . 
H 4 HOH 201 701 1131 HOH HOH A . 
H 4 HOH 202 702 1173 HOH HOH A . 
H 4 HOH 203 703 1122 HOH HOH A . 
H 4 HOH 204 704 1107 HOH HOH A . 
H 4 HOH 205 705 1409 HOH HOH A . 
H 4 HOH 206 706 1168 HOH HOH A . 
H 4 HOH 207 707 1206 HOH HOH A . 
H 4 HOH 208 708 1009 HOH HOH A . 
H 4 HOH 209 709 1167 HOH HOH A . 
H 4 HOH 210 710 1069 HOH HOH A . 
H 4 HOH 211 711 1137 HOH HOH A . 
H 4 HOH 212 712 1037 HOH HOH A . 
H 4 HOH 213 713 1124 HOH HOH A . 
H 4 HOH 214 714 1130 HOH HOH A . 
H 4 HOH 215 715 1175 HOH HOH A . 
H 4 HOH 216 716 1178 HOH HOH A . 
H 4 HOH 217 717 1348 HOH HOH A . 
H 4 HOH 218 718 1398 HOH HOH A . 
H 4 HOH 219 719 1202 HOH HOH A . 
H 4 HOH 220 720 1210 HOH HOH A . 
H 4 HOH 221 721 1125 HOH HOH A . 
H 4 HOH 222 722 1110 HOH HOH A . 
H 4 HOH 223 723 1207 HOH HOH A . 
I 4 HOH 1   501 1418 HOH HOH B . 
I 4 HOH 2   502 1203 HOH HOH B . 
I 4 HOH 3   503 1215 HOH HOH B . 
I 4 HOH 4   504 1243 HOH HOH B . 
I 4 HOH 5   505 1369 HOH HOH B . 
I 4 HOH 6   506 1357 HOH HOH B . 
I 4 HOH 7   507 1318 HOH HOH B . 
I 4 HOH 8   508 1266 HOH HOH B . 
I 4 HOH 9   509 1382 HOH HOH B . 
I 4 HOH 10  510 1222 HOH HOH B . 
I 4 HOH 11  511 1330 HOH HOH B . 
I 4 HOH 12  512 1333 HOH HOH B . 
I 4 HOH 13  513 1251 HOH HOH B . 
I 4 HOH 14  514 1248 HOH HOH B . 
I 4 HOH 15  515 1340 HOH HOH B . 
I 4 HOH 16  516 1320 HOH HOH B . 
I 4 HOH 17  517 1277 HOH HOH B . 
I 4 HOH 18  518 1293 HOH HOH B . 
I 4 HOH 19  519 1217 HOH HOH B . 
I 4 HOH 20  520 1304 HOH HOH B . 
I 4 HOH 21  521 1270 HOH HOH B . 
I 4 HOH 22  522 1234 HOH HOH B . 
I 4 HOH 23  523 1154 HOH HOH B . 
I 4 HOH 24  524 1247 HOH HOH B . 
I 4 HOH 25  525 1229 HOH HOH B . 
I 4 HOH 26  526 1245 HOH HOH B . 
I 4 HOH 27  527 1284 HOH HOH B . 
I 4 HOH 28  528 1218 HOH HOH B . 
I 4 HOH 29  529 1428 HOH HOH B . 
I 4 HOH 30  530 1282 HOH HOH B . 
I 4 HOH 31  531 1324 HOH HOH B . 
I 4 HOH 32  532 1444 HOH HOH B . 
I 4 HOH 33  533 1336 HOH HOH B . 
I 4 HOH 34  534 1365 HOH HOH B . 
I 4 HOH 35  535 1233 HOH HOH B . 
I 4 HOH 36  536 1294 HOH HOH B . 
I 4 HOH 37  537 1254 HOH HOH B . 
I 4 HOH 38  538 1446 HOH HOH B . 
I 4 HOH 39  539 1260 HOH HOH B . 
I 4 HOH 40  540 1327 HOH HOH B . 
I 4 HOH 41  541 1220 HOH HOH B . 
I 4 HOH 42  542 1259 HOH HOH B . 
I 4 HOH 43  543 1315 HOH HOH B . 
I 4 HOH 44  544 1319 HOH HOH B . 
I 4 HOH 45  545 1153 HOH HOH B . 
I 4 HOH 46  546 1299 HOH HOH B . 
I 4 HOH 47  547 1311 HOH HOH B . 
I 4 HOH 48  548 1240 HOH HOH B . 
I 4 HOH 49  549 1375 HOH HOH B . 
I 4 HOH 50  550 1407 HOH HOH B . 
I 4 HOH 51  551 1190 HOH HOH B . 
I 4 HOH 52  552 1230 HOH HOH B . 
I 4 HOH 53  553 1241 HOH HOH B . 
I 4 HOH 54  554 1192 HOH HOH B . 
I 4 HOH 55  555 1309 HOH HOH B . 
I 4 HOH 56  556 1298 HOH HOH B . 
I 4 HOH 57  557 1341 HOH HOH B . 
I 4 HOH 58  558 1295 HOH HOH B . 
I 4 HOH 59  559 1235 HOH HOH B . 
I 4 HOH 60  560 1276 HOH HOH B . 
I 4 HOH 61  561 1370 HOH HOH B . 
I 4 HOH 62  562 1316 HOH HOH B . 
I 4 HOH 63  563 1379 HOH HOH B . 
I 4 HOH 64  564 1332 HOH HOH B . 
I 4 HOH 65  565 1227 HOH HOH B . 
I 4 HOH 66  566 1275 HOH HOH B . 
I 4 HOH 67  567 1239 HOH HOH B . 
I 4 HOH 68  568 1285 HOH HOH B . 
I 4 HOH 69  569 1310 HOH HOH B . 
I 4 HOH 70  570 1289 HOH HOH B . 
I 4 HOH 71  571 1269 HOH HOH B . 
I 4 HOH 72  572 1258 HOH HOH B . 
I 4 HOH 73  573 1389 HOH HOH B . 
I 4 HOH 74  574 1339 HOH HOH B . 
I 4 HOH 75  575 1323 HOH HOH B . 
I 4 HOH 76  576 1308 HOH HOH B . 
I 4 HOH 77  577 1250 HOH HOH B . 
I 4 HOH 78  578 1400 HOH HOH B . 
I 4 HOH 79  579 1237 HOH HOH B . 
I 4 HOH 80  580 1219 HOH HOH B . 
I 4 HOH 81  581 1263 HOH HOH B . 
I 4 HOH 82  582 1303 HOH HOH B . 
I 4 HOH 83  583 1288 HOH HOH B . 
I 4 HOH 84  584 1225 HOH HOH B . 
I 4 HOH 85  585 1264 HOH HOH B . 
I 4 HOH 86  586 1188 HOH HOH B . 
I 4 HOH 87  587 1228 HOH HOH B . 
I 4 HOH 88  588 1388 HOH HOH B . 
I 4 HOH 89  589 1226 HOH HOH B . 
I 4 HOH 90  590 1236 HOH HOH B . 
I 4 HOH 91  591 1300 HOH HOH B . 
I 4 HOH 92  592 1385 HOH HOH B . 
I 4 HOH 93  593 1329 HOH HOH B . 
I 4 HOH 94  594 1353 HOH HOH B . 
I 4 HOH 95  595 1420 HOH HOH B . 
I 4 HOH 96  596 1346 HOH HOH B . 
I 4 HOH 97  597 1306 HOH HOH B . 
I 4 HOH 98  598 1352 HOH HOH B . 
I 4 HOH 99  599 1182 HOH HOH B . 
I 4 HOH 100 600 1335 HOH HOH B . 
I 4 HOH 101 601 1406 HOH HOH B . 
I 4 HOH 102 602 1363 HOH HOH B . 
I 4 HOH 103 603 1216 HOH HOH B . 
I 4 HOH 104 604 1249 HOH HOH B . 
I 4 HOH 105 605 1383 HOH HOH B . 
I 4 HOH 106 606 1421 HOH HOH B . 
I 4 HOH 107 607 1367 HOH HOH B . 
I 4 HOH 108 608 1246 HOH HOH B . 
I 4 HOH 109 609 1297 HOH HOH B . 
I 4 HOH 110 610 1397 HOH HOH B . 
I 4 HOH 111 611 1392 HOH HOH B . 
I 4 HOH 112 612 1334 HOH HOH B . 
I 4 HOH 113 613 1313 HOH HOH B . 
I 4 HOH 114 614 1429 HOH HOH B . 
I 4 HOH 115 615 1426 HOH HOH B . 
I 4 HOH 116 616 1238 HOH HOH B . 
I 4 HOH 117 617 1331 HOH HOH B . 
I 4 HOH 118 618 1242 HOH HOH B . 
I 4 HOH 119 619 1344 HOH HOH B . 
I 4 HOH 120 620 1221 HOH HOH B . 
I 4 HOH 121 621 1232 HOH HOH B . 
I 4 HOH 122 622 1425 HOH HOH B . 
I 4 HOH 123 623 1377 HOH HOH B . 
I 4 HOH 124 624 1281 HOH HOH B . 
I 4 HOH 125 625 1189 HOH HOH B . 
I 4 HOH 126 626 1351 HOH HOH B . 
I 4 HOH 127 627 1279 HOH HOH B . 
I 4 HOH 128 628 1360 HOH HOH B . 
I 4 HOH 129 629 1399 HOH HOH B . 
I 4 HOH 130 630 1296 HOH HOH B . 
I 4 HOH 131 631 1291 HOH HOH B . 
I 4 HOH 132 632 1450 HOH HOH B . 
I 4 HOH 133 633 1255 HOH HOH B . 
I 4 HOH 134 634 1359 HOH HOH B . 
I 4 HOH 135 635 1312 HOH HOH B . 
I 4 HOH 136 636 1417 HOH HOH B . 
I 4 HOH 137 637 1253 HOH HOH B . 
I 4 HOH 138 638 1257 HOH HOH B . 
I 4 HOH 139 639 1040 HOH HOH B . 
I 4 HOH 140 640 1412 HOH HOH B . 
I 4 HOH 141 641 1394 HOH HOH B . 
I 4 HOH 142 642 1267 HOH HOH B . 
I 4 HOH 143 643 1423 HOH HOH B . 
I 4 HOH 144 644 1224 HOH HOH B . 
I 4 HOH 145 645 1395 HOH HOH B . 
I 4 HOH 146 646 1350 HOH HOH B . 
I 4 HOH 147 647 1223 HOH HOH B . 
I 4 HOH 148 648 1380 HOH HOH B . 
I 4 HOH 149 649 1252 HOH HOH B . 
I 4 HOH 150 650 1445 HOH HOH B . 
I 4 HOH 151 651 1307 HOH HOH B . 
I 4 HOH 152 652 1328 HOH HOH B . 
I 4 HOH 153 653 1393 HOH HOH B . 
I 4 HOH 154 654 1442 HOH HOH B . 
I 4 HOH 155 655 1326 HOH HOH B . 
I 4 HOH 156 656 1434 HOH HOH B . 
I 4 HOH 157 657 1321 HOH HOH B . 
I 4 HOH 158 658 1356 HOH HOH B . 
I 4 HOH 159 659 1292 HOH HOH B . 
I 4 HOH 160 660 1349 HOH HOH B . 
I 4 HOH 161 661 1378 HOH HOH B . 
I 4 HOH 162 662 1342 HOH HOH B . 
I 4 HOH 163 663 1280 HOH HOH B . 
I 4 HOH 164 664 1317 HOH HOH B . 
I 4 HOH 165 665 1272 HOH HOH B . 
I 4 HOH 166 666 1262 HOH HOH B . 
I 4 HOH 167 667 1286 HOH HOH B . 
I 4 HOH 168 668 1278 HOH HOH B . 
I 4 HOH 169 669 1433 HOH HOH B . 
I 4 HOH 170 670 1376 HOH HOH B . 
I 4 HOH 171 671 1374 HOH HOH B . 
I 4 HOH 172 672 1430 HOH HOH B . 
I 4 HOH 173 673 1305 HOH HOH B . 
I 4 HOH 174 674 1387 HOH HOH B . 
I 4 HOH 175 675 1384 HOH HOH B . 
I 4 HOH 176 676 1256 HOH HOH B . 
I 4 HOH 177 677 1408 HOH HOH B . 
I 4 HOH 178 678 1403 HOH HOH B . 
I 4 HOH 179 679 1158 HOH HOH B . 
I 4 HOH 180 680 1347 HOH HOH B . 
I 4 HOH 181 681 1046 HOH HOH B . 
I 4 HOH 182 682 1208 HOH HOH B . 
I 4 HOH 183 683 1146 HOH HOH B . 
I 4 HOH 184 684 1431 HOH HOH B . 
I 4 HOH 185 685 1449 HOH HOH B . 
I 4 HOH 186 686 1435 HOH HOH B . 
I 4 HOH 187 687 1404 HOH HOH B . 
I 4 HOH 188 688 1361 HOH HOH B . 
I 4 HOH 189 689 1149 HOH HOH B . 
I 4 HOH 190 690 1322 HOH HOH B . 
I 4 HOH 191 691 1419 HOH HOH B . 
I 4 HOH 192 692 1401 HOH HOH B . 
I 4 HOH 193 693 1427 HOH HOH B . 
I 4 HOH 194 694 1413 HOH HOH B . 
I 4 HOH 195 695 1358 HOH HOH B . 
I 4 HOH 196 696 1391 HOH HOH B . 
I 4 HOH 197 697 1441 HOH HOH B . 
I 4 HOH 198 698 1410 HOH HOH B . 
I 4 HOH 199 699 1183 HOH HOH B . 
I 4 HOH 200 700 1402 HOH HOH B . 
I 4 HOH 201 701 1343 HOH HOH B . 
I 4 HOH 202 702 1211 HOH HOH B . 
I 4 HOH 203 703 1416 HOH HOH B . 
I 4 HOH 204 704 1432 HOH HOH B . 
I 4 HOH 205 705 1274 HOH HOH B . 
I 4 HOH 206 706 1354 HOH HOH B . 
I 4 HOH 207 707 1368 HOH HOH B . 
I 4 HOH 208 708 1390 HOH HOH B . 
I 4 HOH 209 709 1422 HOH HOH B . 
I 4 HOH 210 710 1345 HOH HOH B . 
I 4 HOH 211 711 1355 HOH HOH B . 
I 4 HOH 212 712 1436 HOH HOH B . 
I 4 HOH 213 713 1414 HOH HOH B . 
I 4 HOH 214 714 1045 HOH HOH B . 
I 4 HOH 215 715 1439 HOH HOH B . 
I 4 HOH 216 716 1163 HOH HOH B . 
I 4 HOH 217 717 1362 HOH HOH B . 
I 4 HOH 218 718 1261 HOH HOH B . 
I 4 HOH 219 719 1451 HOH HOH B . 
I 4 HOH 220 720 1437 HOH HOH B . 
I 4 HOH 221 721 1325 HOH HOH B . 
I 4 HOH 222 722 1271 HOH HOH B . 
I 4 HOH 223 723 1265 HOH HOH B . 
I 4 HOH 224 724 1337 HOH HOH B . 
I 4 HOH 225 725 1366 HOH HOH B . 
I 4 HOH 226 726 1424 HOH HOH B . 
I 4 HOH 227 727 1440 HOH HOH B . 
I 4 HOH 228 728 1438 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.17.1_3660: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                    4 
# 
_cell.angle_alpha                  85.39 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   86.78 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  70.54 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IXF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.876 
_cell.length_a_esd                 ? 
_cell.length_b                     46.683 
_cell.length_b_esd                 ? 
_cell.length_c                     58.222 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9IXF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IXF 
_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             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.96 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.3 
_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    'PEG 4000, MgCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-02-14 
_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   0.90000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL44XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.90000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL44XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IXF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               43.92 
_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                                     44308 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.91 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.092 
_reflns.pdbx_Rpim_I_all                                0.048 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       158923 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           8413 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2372 
_reflns_shell.percent_possible_obs                          95.4 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.5 
_reflns_shell.pdbx_chi_squared                              0.57 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     3.1 
_reflns_shell.pdbx_Rrim_I_all                               0.413 
_reflns_shell.pdbx_Rpim_I_all                               0.217 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.884 
_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                                  0.351 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IXF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.75 
_refine.ls_d_res_low                             43.92 
_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                     44301 
_refine.ls_number_reflns_R_free                  2175 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.80 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1600 
_refine.ls_R_factor_R_free                       0.2010 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1580 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.99 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 19.02 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        43.92 
_refine_hist.number_atoms_solvent             451 
_refine_hist.number_atoms_total               4532 
_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        4076 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_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' ? 0.007  ? 4158 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.885  ? 5689 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.376 ? 592  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060  ? 658  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 761  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.75 1.79  . . 138 2573 95.00 . . . . 0.2000 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 1.79 1.83  . . 143 2612 96.00 . . . . 0.1811 . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 1.83 1.88  . . 156 2576 96.00 . . . . 0.1683 . . . . . . . . . . . 0.2344 
'X-RAY DIFFRACTION' 1.88 1.93  . . 158 2590 96.00 . . . . 0.1640 . . . . . . . . . . . 0.2216 
'X-RAY DIFFRACTION' 1.93 1.98  . . 125 2627 96.00 . . . . 0.1593 . . . . . . . . . . . 0.2000 
'X-RAY DIFFRACTION' 1.98 2.05  . . 141 2615 96.00 . . . . 0.1597 . . . . . . . . . . . 0.1760 
'X-RAY DIFFRACTION' 2.05 2.12  . . 137 2608 96.00 . . . . 0.1588 . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 2.12 2.20  . . 130 2590 96.00 . . . . 0.1619 . . . . . . . . . . . 0.2076 
'X-RAY DIFFRACTION' 2.20 2.31  . . 113 2665 96.00 . . . . 0.1591 . . . . . . . . . . . 0.2421 
'X-RAY DIFFRACTION' 2.31 2.43  . . 137 2635 96.00 . . . . 0.1626 . . . . . . . . . . . 0.1993 
'X-RAY DIFFRACTION' 2.43 2.58  . . 125 2645 98.00 . . . . 0.1647 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 2.58 2.78  . . 88  2728 98.00 . . . . 0.1661 . . . . . . . . . . . 0.2066 
'X-RAY DIFFRACTION' 2.78 3.06  . . 156 2647 98.00 . . . . 0.1728 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 3.06 3.50  . . 145 2674 98.00 . . . . 0.1571 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 3.50 4.41  . . 159 2643 98.00 . . . . 0.1321 . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 4.41 43.92 . . 124 2698 98.00 . . . . 0.1527 . . . . . . . . . . . 0.1677 
# 
_struct.entry_id                     9IXF 
_struct.title                        
'Crystal structure of Manganese-free N(omega)-hydroxy-L-arginine hydrolase with oxidized Cys86.' 
_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        9IXF 
_struct_keywords.text            HYDROLASE 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DCSB_STRLA 
_struct_ref.pdbx_db_accession          D2Z025 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDDWSVALPQARETLVAVREAATESIKGDNLTV
LVNNTCSVSLATLPVVAREHPDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQAVLVGSRDIDE
GERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWDVLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELA
ELNAPADSERAEQAVAVILDMVAPAFDAAAARP
;
_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 9IXF A 1 ? 273 ? D2Z025 1 ? 273 ? 1 273 
2 1 9IXF B 1 ? 273 ? D2Z025 1 ? 273 ? 1 273 
# 
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 9IXF LEU A 274 ? UNP D2Z025 ? ? 'expression tag' 274 1  
1 9IXF GLU A 275 ? UNP D2Z025 ? ? 'expression tag' 275 2  
1 9IXF HIS A 276 ? UNP D2Z025 ? ? 'expression tag' 276 3  
1 9IXF HIS A 277 ? UNP D2Z025 ? ? 'expression tag' 277 4  
1 9IXF HIS A 278 ? UNP D2Z025 ? ? 'expression tag' 278 5  
1 9IXF HIS A 279 ? UNP D2Z025 ? ? 'expression tag' 279 6  
1 9IXF HIS A 280 ? UNP D2Z025 ? ? 'expression tag' 280 7  
1 9IXF HIS A 281 ? UNP D2Z025 ? ? 'expression tag' 281 8  
2 9IXF LEU B 274 ? UNP D2Z025 ? ? 'expression tag' 274 9  
2 9IXF GLU B 275 ? UNP D2Z025 ? ? 'expression tag' 275 10 
2 9IXF HIS B 276 ? UNP D2Z025 ? ? 'expression tag' 276 11 
2 9IXF HIS B 277 ? UNP D2Z025 ? ? 'expression tag' 277 12 
2 9IXF HIS B 278 ? UNP D2Z025 ? ? 'expression tag' 278 13 
2 9IXF HIS B 279 ? UNP D2Z025 ? ? 'expression tag' 279 14 
2 9IXF HIS B 280 ? UNP D2Z025 ? ? 'expression tag' 280 15 
2 9IXF HIS B 281 ? UNP D2Z025 ? ? 'expression tag' 281 16 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 80    ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  11590 ? 
2 'ABSA (A^2)' 210   ? 
2 MORE         -20   ? 
2 'SSA (A^2)'  10800 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,H   
2 1 B,E,F,G,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TRP A 17  ? GLY A 34  ? TRP A 17  GLY A 34  1 ? 18 
HELX_P HELX_P2  AA2 ASP A 50  ? ALA A 58  ? ASP A 50  ALA A 58  1 ? 9  
HELX_P HELX_P3  AA3 ALA A 58  ? GLY A 75  ? ALA A 58  GLY A 75  1 ? 18 
HELX_P HELX_P4  AA4 THR A 85  ? SER A 87  ? THR A 85  SER A 87  5 ? 3  
HELX_P HELX_P5  AA5 VAL A 88  ? HIS A 100 ? VAL A 88  HIS A 100 1 ? 13 
HELX_P HELX_P6  AA6 TYR A 124 ? GLY A 127 ? TYR A 124 GLY A 127 5 ? 4  
HELX_P HELX_P7  AA7 MET A 128 ? CYS A 134 ? MET A 128 CYS A 134 1 ? 7  
HELX_P HELX_P8  AA8 ARG A 146 ? GLU A 148 ? ARG A 146 GLU A 148 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 159 ? GLY A 170 ? ASP A 159 GLY A 170 1 ? 12 
HELX_P HELX_P10 AB1 PRO A 175 ? ALA A 179 ? PRO A 175 ALA A 179 5 ? 5  
HELX_P HELX_P11 AB2 THR A 180 ? LYS A 189 ? THR A 180 LYS A 189 1 ? 10 
HELX_P HELX_P12 AB3 ASP A 200 ? LEU A 202 ? ASP A 200 LEU A 202 5 ? 3  
HELX_P HELX_P13 AB4 LEU A 218 ? ILE A 229 ? LEU A 218 ILE A 229 1 ? 12 
HELX_P HELX_P14 AB5 PRO A 230 ? GLU A 232 ? PRO A 230 GLU A 232 5 ? 3  
HELX_P HELX_P15 AB6 SER A 248 ? ARG A 272 ? SER A 248 ARG A 272 1 ? 25 
HELX_P HELX_P16 AB7 TRP B 17  ? GLY B 34  ? TRP B 17  GLY B 34  1 ? 18 
HELX_P HELX_P17 AB8 ASP B 50  ? ALA B 58  ? ASP B 50  ALA B 58  1 ? 9  
HELX_P HELX_P18 AB9 ALA B 58  ? GLY B 75  ? ALA B 58  GLY B 75  1 ? 18 
HELX_P HELX_P19 AC1 THR B 85  ? SER B 87  ? THR B 85  SER B 87  5 ? 3  
HELX_P HELX_P20 AC2 VAL B 88  ? HIS B 100 ? VAL B 88  HIS B 100 1 ? 13 
HELX_P HELX_P21 AC3 TYR B 124 ? GLY B 127 ? TYR B 124 GLY B 127 5 ? 4  
HELX_P HELX_P22 AC4 MET B 128 ? CYS B 134 ? MET B 128 CYS B 134 1 ? 7  
HELX_P HELX_P23 AC5 ARG B 146 ? GLU B 148 ? ARG B 146 GLU B 148 5 ? 3  
HELX_P HELX_P24 AC6 ASP B 159 ? GLY B 170 ? ASP B 159 GLY B 170 1 ? 12 
HELX_P HELX_P25 AC7 PRO B 175 ? ALA B 179 ? PRO B 175 ALA B 179 5 ? 5  
HELX_P HELX_P26 AC8 THR B 180 ? LYS B 189 ? THR B 180 LYS B 189 1 ? 10 
HELX_P HELX_P27 AC9 ASP B 200 ? LEU B 202 ? ASP B 200 LEU B 202 5 ? 3  
HELX_P HELX_P28 AD1 LEU B 218 ? ILE B 229 ? LEU B 218 ILE B 229 1 ? 12 
HELX_P HELX_P29 AD2 PRO B 230 ? GLU B 232 ? PRO B 230 GLU B 232 5 ? 3  
HELX_P HELX_P30 AD3 SER B 248 ? ARG B 272 ? SER B 248 ARG B 272 1 ? 25 
# 
_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 ? B THR 85  C   ? ? ? 1_555 B CSO 86 N  B ? B THR 85  B CSO 86  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2  covale both ? B CSO 86  C   B ? ? 1_555 B SER 87 N  ? ? B CSO 86  B SER 87  1_555 ? ? ? ? ? ? ? 1.330 ? ? 
metalc1  metalc ?    ? A CYS 86  SG  ? ? ? 1_555 C MN  .  MN ? ? A CYS 86  A MN  401 1_555 ? ? ? ? ? ? ? 2.517 ? ? 
metalc2  metalc ?    ? A ASP 109 OD2 ? ? ? 1_555 C MN  .  MN ? ? A ASP 109 A MN  401 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc3  metalc ?    ? A ASP 109 OD1 ? ? ? 1_555 D MG  .  MG ? ? A ASP 109 A MG  402 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc4  metalc ?    ? A ASP 113 OD2 ? ? ? 1_555 C MN  .  MN ? ? A ASP 113 A MN  401 1_555 ? ? ? ? ? ? ? 2.178 ? ? 
metalc5  metalc ?    ? A ASP 198 OD2 ? ? ? 1_555 C MN  .  MN ? ? A ASP 198 A MN  401 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc6  metalc ?    ? A ASP 198 OD2 ? ? ? 1_555 D MG  .  MG ? ? A ASP 198 A MG  402 1_555 ? ? ? ? ? ? ? 2.211 ? ? 
metalc7  metalc ?    ? A ASP 200 OD1 ? ? ? 1_555 D MG  .  MG ? ? A ASP 200 A MG  402 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc8  metalc ?    ? A ASP 200 OD2 ? ? ? 1_555 D MG  .  MG ? ? A ASP 200 A MG  402 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc9  metalc ?    ? C MN  .   MN  ? ? ? 1_555 H HOH .  O  ? ? A MN  401 A HOH 551 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc10 metalc ?    ? C MN  .   MN  ? ? ? 1_555 H HOH .  O  ? ? A MN  401 A HOH 608 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc11 metalc ?    ? D MG  .   MG  ? ? ? 1_555 H HOH .  O  ? ? A MG  402 A HOH 551 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc12 metalc ?    ? B CSO 86  OD  B ? ? 1_555 E MG  .  MG ? ? B CSO 86  B MG  401 1_555 ? ? ? ? ? ? ? 1.819 ? ? 
metalc13 metalc ?    ? B ASP 109 OD2 ? ? ? 1_555 E MG  .  MG ? ? B ASP 109 B MG  401 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc14 metalc ?    ? B ASP 113 OD2 ? ? ? 1_555 E MG  .  MG ? ? B ASP 113 B MG  401 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc15 metalc ?    ? B GLU 162 OE2 ? ? ? 1_555 G MG  .  MG ? ? B GLU 162 B MG  403 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc16 metalc ?    ? B ASP 198 OD2 ? ? ? 1_555 E MG  .  MG ? ? B ASP 198 B MG  401 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc17 metalc ?    ? B ASP 198 OD1 ? ? ? 1_555 F MG  .  MG ? ? B ASP 198 B MG  402 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc18 metalc ?    ? B ASP 198 OD2 ? ? ? 1_555 F MG  .  MG ? ? B ASP 198 B MG  402 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc19 metalc ?    ? B ASP 200 OD2 ? ? ? 1_555 F MG  .  MG ? ? B ASP 200 B MG  402 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc20 metalc ?    ? B GLU 241 OE2 ? ? ? 1_555 F MG  .  MG ? ? B GLU 241 B MG  402 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc21 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  401 B HOH 560 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc22 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  401 B HOH 630 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc23 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  402 B HOH 504 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc24 metalc ?    ? F MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  402 B HOH 582 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc25 metalc ?    ? G MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  403 B HOH 547 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc26 metalc ?    ? G MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  403 B HOH 549 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc27 metalc ?    ? G MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  403 B HOH 615 1_555 ? ? ? ? ? ? ? 1.905 ? ? 
metalc28 metalc ?    ? G MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  403 B HOH 670 1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc29 metalc ?    ? G MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? B MG  403 B HOH 671 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 104.7 ? 
2  SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD2 ? A ASP 113 ? A ASP 113 ? 1_555 104.8 ? 
3  OD2 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD2 ? A ASP 113 ? A ASP 113 ? 1_555 81.2  ? 
4  SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 93.8  ? 
5  OD2 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 83.3  ? 
6  OD2 ? A ASP 113 ? A ASP 113 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 158.3 ? 
7  SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 155.8 ? 
8  OD2 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 94.4  ? 
9  OD2 ? A ASP 113 ? A ASP 113 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 92.4  ? 
10 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 73.6  ? 
11 SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 608 ? 1_555 87.0  ? 
12 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 608 ? 1_555 167.8 ? 
13 OD2 ? A ASP 113 ? A ASP 113 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 608 ? 1_555 92.5  ? 
14 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 608 ? 1_555 99.6  ? 
15 O   ? H HOH .   ? A HOH 551 ? 1_555 MN ? C MN . ? A MN 401 ? 1_555 O   ? H HOH .   ? A HOH 608 ? 1_555 75.3  ? 
16 OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 91.4  ? 
17 OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 86.4  ? 
18 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 93.6  ? 
19 OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 146.4 ? 
20 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 87.6  ? 
21 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 60.1  ? 
22 OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 95.5  ? 
23 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 78.6  ? 
24 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 171.9 ? 
25 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 MG ? D MG . ? A MG 402 ? 1_555 O   ? H HOH .   ? A HOH 551 ? 1_555 117.2 ? 
26 OD  B B CSO 86  ? B CSO 86  ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 OD2 ? B ASP 109 ? B ASP 109 ? 1_555 79.6  ? 
27 OD  B B CSO 86  ? B CSO 86  ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 92.8  ? 
28 OD2 ? B ASP 109 ? B ASP 109 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 87.4  ? 
29 OD  B B CSO 86  ? B CSO 86  ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 92.1  ? 
30 OD2 ? B ASP 109 ? B ASP 109 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 89.8  ? 
31 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 174.0 ? 
32 OD  B B CSO 86  ? B CSO 86  ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 560 ? 1_555 164.9 ? 
33 OD2 ? B ASP 109 ? B ASP 109 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 560 ? 1_555 87.8  ? 
34 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 560 ? 1_555 95.0  ? 
35 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 560 ? 1_555 79.5  ? 
36 OD  B B CSO 86  ? B CSO 86  ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 630 ? 1_555 106.9 ? 
37 OD2 ? B ASP 109 ? B ASP 109 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 630 ? 1_555 172.3 ? 
38 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 630 ? 1_555 88.1  ? 
39 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 630 ? 1_555 94.0  ? 
40 O   ? I HOH .   ? B HOH 560 ? 1_555 MG ? E MG . ? B MG 401 ? 1_555 O   ? I HOH .   ? B HOH 630 ? 1_555 86.3  ? 
41 OE2 ? B GLU 162 ? B GLU 162 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 547 ? 1_555 90.1  ? 
42 OE2 ? B GLU 162 ? B GLU 162 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 549 ? 1_555 88.9  ? 
43 O   ? I HOH .   ? B HOH 547 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 549 ? 1_555 84.8  ? 
44 OE2 ? B GLU 162 ? B GLU 162 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 615 ? 1_555 90.2  ? 
45 O   ? I HOH .   ? B HOH 547 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 615 ? 1_555 176.5 ? 
46 O   ? I HOH .   ? B HOH 549 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 615 ? 1_555 98.7  ? 
47 OE2 ? B GLU 162 ? B GLU 162 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 670 ? 1_555 95.6  ? 
48 O   ? I HOH .   ? B HOH 547 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 670 ? 1_555 83.5  ? 
49 O   ? I HOH .   ? B HOH 549 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 670 ? 1_555 167.5 ? 
50 O   ? I HOH .   ? B HOH 615 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 670 ? 1_555 93.0  ? 
51 OE2 ? B GLU 162 ? B GLU 162 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 671 ? 1_555 174.4 ? 
52 O   ? I HOH .   ? B HOH 547 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 671 ? 1_555 86.8  ? 
53 O   ? I HOH .   ? B HOH 549 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 671 ? 1_555 95.4  ? 
54 O   ? I HOH .   ? B HOH 615 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 671 ? 1_555 92.6  ? 
55 O   ? I HOH .   ? B HOH 670 ? 1_555 MG ? G MG . ? B MG 403 ? 1_555 O   ? I HOH .   ? B HOH 671 ? 1_555 79.5  ? 
56 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 58.3  ? 
57 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 86.4  ? 
58 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 83.0  ? 
59 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 96.0  ? 
60 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 94.8  ? 
61 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 175.3 ? 
62 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 504 ? 1_555 100.1 ? 
63 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 504 ? 1_555 158.4 ? 
64 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 504 ? 1_555 98.7  ? 
65 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 504 ? 1_555 84.9  ? 
66 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 582 ? 1_555 160.1 ? 
67 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 582 ? 1_555 101.8 ? 
68 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 582 ? 1_555 90.2  ? 
69 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 582 ? 1_555 86.2  ? 
70 O   ? I HOH .   ? B HOH 504 ? 1_555 MG ? F MG . ? B MG 402 ? 1_555 O   ? I HOH .   ? B HOH 582 ? 1_555 99.8  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CSO 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       86 
_pdbx_modification_feature.label_alt_id                       B 
_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                       CSO 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        86 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_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                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        CSO 
_pdbx_modification_feature.type                               Hydroxylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
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 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA2 7 8 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 38  ? VAL A 40  ? HIS A 38  VAL A 40  
AA1 2 ILE A 2   ? SER A 7   ? ILE A 2   SER A 7   
AA1 3 LEU A 78  ? ASN A 83  ? LEU A 78  ASN A 83  
AA1 4 LEU A 234 ? ALA A 240 ? LEU A 234 ALA A 240 
AA1 5 VAL A 193 ? ASP A 198 ? VAL A 193 ASP A 198 
AA1 6 VAL A 104 ? ILE A 108 ? VAL A 104 ILE A 108 
AA1 7 ALA A 150 ? VAL A 153 ? ALA A 150 VAL A 153 
AA1 8 ARG A 172 ? ILE A 174 ? ARG A 172 ILE A 174 
AA2 1 HIS B 38  ? VAL B 40  ? HIS B 38  VAL B 40  
AA2 2 ILE B 2   ? SER B 7   ? ILE B 2   SER B 7   
AA2 3 LEU B 78  ? ASN B 83  ? LEU B 78  ASN B 83  
AA2 4 LEU B 234 ? ALA B 240 ? LEU B 234 ALA B 240 
AA2 5 VAL B 193 ? ASP B 198 ? VAL B 193 ASP B 198 
AA2 6 VAL B 104 ? ILE B 108 ? VAL B 104 ILE B 108 
AA2 7 ALA B 150 ? VAL B 153 ? ALA B 150 VAL B 153 
AA2 8 ARG B 172 ? ILE B 174 ? ARG B 172 ILE B 174 
# 
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 HIS A 38  ? O HIS A 38  N VAL A 6   ? N VAL A 6   
AA1 2 3 N ILE A 5   ? N ILE A 5   O VAL A 82  ? O VAL A 82  
AA1 3 4 N LEU A 81  ? N LEU A 81  O VAL A 237 ? O VAL A 237 
AA1 4 5 O ILE A 235 ? O ILE A 235 N VAL A 193 ? N VAL A 193 
AA1 5 6 O HIS A 196 ? O HIS A 196 N ILE A 108 ? N ILE A 108 
AA1 6 7 N VAL A 105 ? N VAL A 105 O VAL A 151 ? O VAL A 151 
AA1 7 8 N LEU A 152 ? N LEU A 152 O ILE A 174 ? O ILE A 174 
AA2 1 2 O HIS B 38  ? O HIS B 38  N VAL B 6   ? N VAL B 6   
AA2 2 3 N ASP B 3   ? N ASP B 3   O LEU B 78  ? O LEU B 78  
AA2 3 4 N ASN B 83  ? N ASN B 83  O LEU B 239 ? O LEU B 239 
AA2 4 5 O GLU B 238 ? O GLU B 238 N ILE B 195 ? N ILE B 195 
AA2 5 6 O HIS B 196 ? O HIS B 196 N ILE B 108 ? N ILE B 108 
AA2 6 7 N TYR B 107 ? N TYR B 107 O VAL B 151 ? O VAL B 151 
AA2 7 8 N LEU B 152 ? N LEU B 152 O ILE B 174 ? O ILE B 174 
# 
_pdbx_entry_details.entry_id                   9IXF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 48  ? ? -95.05  55.89   
2  1 ALA A 143 ? ? -145.61 -121.32 
3  1 LYS A 189 ? ? 47.76   -121.93 
4  1 PRO A 208 ? ? -46.06  77.35   
5  1 ALA A 209 ? ? -158.08 46.05   
6  1 GLU A 241 ? ? 74.92   48.12   
7  1 ASP A 247 ? ? 73.59   -3.80   
8  1 ASP B 48  ? ? -100.60 64.10   
9  1 ALA B 143 ? ? -140.22 -128.13 
10 1 LYS B 189 ? ? 57.41   -125.82 
11 1 GLU B 241 ? ? 85.86   32.09   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 723 ? 6.78 . 
2 1 O ? B HOH 728 ? 6.32 . 
# 
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 PRO 273 ? A PRO 273 
2  1 Y 1 A LEU 274 ? A LEU 274 
3  1 Y 1 A GLU 275 ? A GLU 275 
4  1 Y 1 A HIS 276 ? A HIS 276 
5  1 Y 1 A HIS 277 ? A HIS 277 
6  1 Y 1 A HIS 278 ? A HIS 278 
7  1 Y 1 A HIS 279 ? A HIS 279 
8  1 Y 1 A HIS 280 ? A HIS 280 
9  1 Y 1 A HIS 281 ? A HIS 281 
10 1 Y 1 B GLU 275 ? B GLU 275 
11 1 Y 1 B HIS 276 ? B HIS 276 
12 1 Y 1 B HIS 277 ? B HIS 277 
13 1 Y 1 B HIS 278 ? B HIS 278 
14 1 Y 1 B HIS 279 ? B HIS 279 
15 1 Y 1 B HIS 280 ? B HIS 280 
16 1 Y 1 B HIS 281 ? B HIS 281 
# 
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  
CSO N    N  N N 74  
CSO CA   C  N R 75  
CSO CB   C  N N 76  
CSO SG   S  N N 77  
CSO C    C  N N 78  
CSO O    O  N N 79  
CSO OXT  O  N N 80  
CSO OD   O  N N 81  
CSO H    H  N N 82  
CSO H2   H  N N 83  
CSO HA   H  N N 84  
CSO HB2  H  N N 85  
CSO HB3  H  N N 86  
CSO HXT  H  N N 87  
CSO HD   H  N N 88  
CYS N    N  N N 89  
CYS CA   C  N R 90  
CYS C    C  N N 91  
CYS O    O  N N 92  
CYS CB   C  N N 93  
CYS SG   S  N N 94  
CYS OXT  O  N N 95  
CYS H    H  N N 96  
CYS H2   H  N N 97  
CYS HA   H  N N 98  
CYS HB2  H  N N 99  
CYS HB3  H  N N 100 
CYS HG   H  N N 101 
CYS HXT  H  N N 102 
GLN N    N  N N 103 
GLN CA   C  N S 104 
GLN C    C  N N 105 
GLN O    O  N N 106 
GLN CB   C  N N 107 
GLN CG   C  N N 108 
GLN CD   C  N N 109 
GLN OE1  O  N N 110 
GLN NE2  N  N N 111 
GLN OXT  O  N N 112 
GLN H    H  N N 113 
GLN H2   H  N N 114 
GLN HA   H  N N 115 
GLN HB2  H  N N 116 
GLN HB3  H  N N 117 
GLN HG2  H  N N 118 
GLN HG3  H  N N 119 
GLN HE21 H  N N 120 
GLN HE22 H  N N 121 
GLN HXT  H  N N 122 
GLU N    N  N N 123 
GLU CA   C  N S 124 
GLU C    C  N N 125 
GLU O    O  N N 126 
GLU CB   C  N N 127 
GLU CG   C  N N 128 
GLU CD   C  N N 129 
GLU OE1  O  N N 130 
GLU OE2  O  N N 131 
GLU OXT  O  N N 132 
GLU H    H  N N 133 
GLU H2   H  N N 134 
GLU HA   H  N N 135 
GLU HB2  H  N N 136 
GLU HB3  H  N N 137 
GLU HG2  H  N N 138 
GLU HG3  H  N N 139 
GLU HE2  H  N N 140 
GLU HXT  H  N N 141 
GLY N    N  N N 142 
GLY CA   C  N N 143 
GLY C    C  N N 144 
GLY O    O  N N 145 
GLY OXT  O  N N 146 
GLY H    H  N N 147 
GLY H2   H  N N 148 
GLY HA2  H  N N 149 
GLY HA3  H  N N 150 
GLY HXT  H  N N 151 
HIS N    N  N N 152 
HIS CA   C  N S 153 
HIS C    C  N N 154 
HIS O    O  N N 155 
HIS CB   C  N N 156 
HIS CG   C  Y N 157 
HIS ND1  N  Y N 158 
HIS CD2  C  Y N 159 
HIS CE1  C  Y N 160 
HIS NE2  N  Y N 161 
HIS OXT  O  N N 162 
HIS H    H  N N 163 
HIS H2   H  N N 164 
HIS HA   H  N N 165 
HIS HB2  H  N N 166 
HIS HB3  H  N N 167 
HIS HD1  H  N N 168 
HIS HD2  H  N N 169 
HIS HE1  H  N N 170 
HIS HE2  H  N N 171 
HIS HXT  H  N N 172 
HOH O    O  N N 173 
HOH H1   H  N N 174 
HOH H2   H  N N 175 
ILE N    N  N N 176 
ILE CA   C  N S 177 
ILE C    C  N N 178 
ILE O    O  N N 179 
ILE CB   C  N S 180 
ILE CG1  C  N N 181 
ILE CG2  C  N N 182 
ILE CD1  C  N N 183 
ILE OXT  O  N N 184 
ILE H    H  N N 185 
ILE H2   H  N N 186 
ILE HA   H  N N 187 
ILE HB   H  N N 188 
ILE HG12 H  N N 189 
ILE HG13 H  N N 190 
ILE HG21 H  N N 191 
ILE HG22 H  N N 192 
ILE HG23 H  N N 193 
ILE HD11 H  N N 194 
ILE HD12 H  N N 195 
ILE HD13 H  N N 196 
ILE HXT  H  N N 197 
LEU N    N  N N 198 
LEU CA   C  N S 199 
LEU C    C  N N 200 
LEU O    O  N N 201 
LEU CB   C  N N 202 
LEU CG   C  N N 203 
LEU CD1  C  N N 204 
LEU CD2  C  N N 205 
LEU OXT  O  N N 206 
LEU H    H  N N 207 
LEU H2   H  N N 208 
LEU HA   H  N N 209 
LEU HB2  H  N N 210 
LEU HB3  H  N N 211 
LEU HG   H  N N 212 
LEU HD11 H  N N 213 
LEU HD12 H  N N 214 
LEU HD13 H  N N 215 
LEU HD21 H  N N 216 
LEU HD22 H  N N 217 
LEU HD23 H  N N 218 
LEU HXT  H  N N 219 
LYS N    N  N N 220 
LYS CA   C  N S 221 
LYS C    C  N N 222 
LYS O    O  N N 223 
LYS CB   C  N N 224 
LYS CG   C  N N 225 
LYS CD   C  N N 226 
LYS CE   C  N N 227 
LYS NZ   N  N N 228 
LYS OXT  O  N N 229 
LYS H    H  N N 230 
LYS H2   H  N N 231 
LYS HA   H  N N 232 
LYS HB2  H  N N 233 
LYS HB3  H  N N 234 
LYS HG2  H  N N 235 
LYS HG3  H  N N 236 
LYS HD2  H  N N 237 
LYS HD3  H  N N 238 
LYS HE2  H  N N 239 
LYS HE3  H  N N 240 
LYS HZ1  H  N N 241 
LYS HZ2  H  N N 242 
LYS HZ3  H  N N 243 
LYS HXT  H  N N 244 
MET N    N  N N 245 
MET CA   C  N S 246 
MET C    C  N N 247 
MET O    O  N N 248 
MET CB   C  N N 249 
MET CG   C  N N 250 
MET SD   S  N N 251 
MET CE   C  N N 252 
MET OXT  O  N N 253 
MET H    H  N N 254 
MET H2   H  N N 255 
MET HA   H  N N 256 
MET HB2  H  N N 257 
MET HB3  H  N N 258 
MET HG2  H  N N 259 
MET HG3  H  N N 260 
MET HE1  H  N N 261 
MET HE2  H  N N 262 
MET HE3  H  N N 263 
MET HXT  H  N N 264 
MG  MG   MG N N 265 
MN  MN   MN N N 266 
PHE N    N  N N 267 
PHE CA   C  N S 268 
PHE C    C  N N 269 
PHE O    O  N N 270 
PHE CB   C  N N 271 
PHE CG   C  Y N 272 
PHE CD1  C  Y N 273 
PHE CD2  C  Y N 274 
PHE CE1  C  Y N 275 
PHE CE2  C  Y N 276 
PHE CZ   C  Y N 277 
PHE OXT  O  N N 278 
PHE H    H  N N 279 
PHE H2   H  N N 280 
PHE HA   H  N N 281 
PHE HB2  H  N N 282 
PHE HB3  H  N N 283 
PHE HD1  H  N N 284 
PHE HD2  H  N N 285 
PHE HE1  H  N N 286 
PHE HE2  H  N N 287 
PHE HZ   H  N N 288 
PHE HXT  H  N N 289 
PRO N    N  N N 290 
PRO CA   C  N S 291 
PRO C    C  N N 292 
PRO O    O  N N 293 
PRO CB   C  N N 294 
PRO CG   C  N N 295 
PRO CD   C  N N 296 
PRO OXT  O  N N 297 
PRO H    H  N N 298 
PRO HA   H  N N 299 
PRO HB2  H  N N 300 
PRO HB3  H  N N 301 
PRO HG2  H  N N 302 
PRO HG3  H  N N 303 
PRO HD2  H  N N 304 
PRO HD3  H  N N 305 
PRO HXT  H  N N 306 
SER N    N  N N 307 
SER CA   C  N S 308 
SER C    C  N N 309 
SER O    O  N N 310 
SER CB   C  N N 311 
SER OG   O  N N 312 
SER OXT  O  N N 313 
SER H    H  N N 314 
SER H2   H  N N 315 
SER HA   H  N N 316 
SER HB2  H  N N 317 
SER HB3  H  N N 318 
SER HG   H  N N 319 
SER HXT  H  N N 320 
THR N    N  N N 321 
THR CA   C  N S 322 
THR C    C  N N 323 
THR O    O  N N 324 
THR CB   C  N R 325 
THR OG1  O  N N 326 
THR CG2  C  N N 327 
THR OXT  O  N N 328 
THR H    H  N N 329 
THR H2   H  N N 330 
THR HA   H  N N 331 
THR HB   H  N N 332 
THR HG1  H  N N 333 
THR HG21 H  N N 334 
THR HG22 H  N N 335 
THR HG23 H  N N 336 
THR HXT  H  N N 337 
TRP N    N  N N 338 
TRP CA   C  N S 339 
TRP C    C  N N 340 
TRP O    O  N N 341 
TRP CB   C  N N 342 
TRP CG   C  Y N 343 
TRP CD1  C  Y N 344 
TRP CD2  C  Y N 345 
TRP NE1  N  Y N 346 
TRP CE2  C  Y N 347 
TRP CE3  C  Y N 348 
TRP CZ2  C  Y N 349 
TRP CZ3  C  Y N 350 
TRP CH2  C  Y N 351 
TRP OXT  O  N N 352 
TRP H    H  N N 353 
TRP H2   H  N N 354 
TRP HA   H  N N 355 
TRP HB2  H  N N 356 
TRP HB3  H  N N 357 
TRP HD1  H  N N 358 
TRP HE1  H  N N 359 
TRP HE3  H  N N 360 
TRP HZ2  H  N N 361 
TRP HZ3  H  N N 362 
TRP HH2  H  N N 363 
TRP HXT  H  N N 364 
TYR N    N  N N 365 
TYR CA   C  N S 366 
TYR C    C  N N 367 
TYR O    O  N N 368 
TYR CB   C  N N 369 
TYR CG   C  Y N 370 
TYR CD1  C  Y N 371 
TYR CD2  C  Y N 372 
TYR CE1  C  Y N 373 
TYR CE2  C  Y N 374 
TYR CZ   C  Y N 375 
TYR OH   O  N N 376 
TYR OXT  O  N N 377 
TYR H    H  N N 378 
TYR H2   H  N N 379 
TYR HA   H  N N 380 
TYR HB2  H  N N 381 
TYR HB3  H  N N 382 
TYR HD1  H  N N 383 
TYR HD2  H  N N 384 
TYR HE1  H  N N 385 
TYR HE2  H  N N 386 
TYR HH   H  N N 387 
TYR HXT  H  N N 388 
VAL N    N  N N 389 
VAL CA   C  N S 390 
VAL C    C  N N 391 
VAL O    O  N N 392 
VAL CB   C  N N 393 
VAL CG1  C  N N 394 
VAL CG2  C  N N 395 
VAL OXT  O  N N 396 
VAL H    H  N N 397 
VAL H2   H  N N 398 
VAL HA   H  N N 399 
VAL HB   H  N N 400 
VAL HG11 H  N N 401 
VAL HG12 H  N N 402 
VAL HG13 H  N N 403 
VAL HG21 H  N N 404 
VAL HG22 H  N N 405 
VAL HG23 H  N N 406 
VAL HXT  H  N N 407 
# 
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  
CSO N   CA   sing N N 70  
CSO N   H    sing N N 71  
CSO N   H2   sing N N 72  
CSO CA  CB   sing N N 73  
CSO CA  C    sing N N 74  
CSO CA  HA   sing N N 75  
CSO CB  SG   sing N N 76  
CSO CB  HB2  sing N N 77  
CSO CB  HB3  sing N N 78  
CSO SG  OD   sing N N 79  
CSO C   O    doub N N 80  
CSO C   OXT  sing N N 81  
CSO OXT HXT  sing N N 82  
CSO OD  HD   sing N N 83  
CYS N   CA   sing N N 84  
CYS N   H    sing N N 85  
CYS N   H2   sing N N 86  
CYS CA  C    sing N N 87  
CYS CA  CB   sing N N 88  
CYS CA  HA   sing N N 89  
CYS C   O    doub N N 90  
CYS C   OXT  sing N N 91  
CYS CB  SG   sing N N 92  
CYS CB  HB2  sing N N 93  
CYS CB  HB3  sing N N 94  
CYS SG  HG   sing N N 95  
CYS OXT HXT  sing N N 96  
GLN N   CA   sing N N 97  
GLN N   H    sing N N 98  
GLN N   H2   sing N N 99  
GLN CA  C    sing N N 100 
GLN CA  CB   sing N N 101 
GLN CA  HA   sing N N 102 
GLN C   O    doub N N 103 
GLN C   OXT  sing N N 104 
GLN CB  CG   sing N N 105 
GLN CB  HB2  sing N N 106 
GLN CB  HB3  sing N N 107 
GLN CG  CD   sing N N 108 
GLN CG  HG2  sing N N 109 
GLN CG  HG3  sing N N 110 
GLN CD  OE1  doub N N 111 
GLN CD  NE2  sing N N 112 
GLN NE2 HE21 sing N N 113 
GLN NE2 HE22 sing N N 114 
GLN OXT HXT  sing N N 115 
GLU N   CA   sing N N 116 
GLU N   H    sing N N 117 
GLU N   H2   sing N N 118 
GLU CA  C    sing N N 119 
GLU CA  CB   sing N N 120 
GLU CA  HA   sing N N 121 
GLU C   O    doub N N 122 
GLU C   OXT  sing N N 123 
GLU CB  CG   sing N N 124 
GLU CB  HB2  sing N N 125 
GLU CB  HB3  sing N N 126 
GLU CG  CD   sing N N 127 
GLU CG  HG2  sing N N 128 
GLU CG  HG3  sing N N 129 
GLU CD  OE1  doub N N 130 
GLU CD  OE2  sing N N 131 
GLU OE2 HE2  sing N N 132 
GLU OXT HXT  sing N N 133 
GLY N   CA   sing N N 134 
GLY N   H    sing N N 135 
GLY N   H2   sing N N 136 
GLY CA  C    sing N N 137 
GLY CA  HA2  sing N N 138 
GLY CA  HA3  sing N N 139 
GLY C   O    doub N N 140 
GLY C   OXT  sing N N 141 
GLY OXT HXT  sing N N 142 
HIS N   CA   sing N N 143 
HIS N   H    sing N N 144 
HIS N   H2   sing N N 145 
HIS CA  C    sing N N 146 
HIS CA  CB   sing N N 147 
HIS CA  HA   sing N N 148 
HIS C   O    doub N N 149 
HIS C   OXT  sing N N 150 
HIS CB  CG   sing N N 151 
HIS CB  HB2  sing N N 152 
HIS CB  HB3  sing N N 153 
HIS CG  ND1  sing Y N 154 
HIS CG  CD2  doub Y N 155 
HIS ND1 CE1  doub Y N 156 
HIS ND1 HD1  sing N N 157 
HIS CD2 NE2  sing Y N 158 
HIS CD2 HD2  sing N N 159 
HIS CE1 NE2  sing Y N 160 
HIS CE1 HE1  sing N N 161 
HIS NE2 HE2  sing N N 162 
HIS OXT HXT  sing N N 163 
HOH O   H1   sing N N 164 
HOH O   H2   sing N N 165 
ILE N   CA   sing N N 166 
ILE N   H    sing N N 167 
ILE N   H2   sing N N 168 
ILE CA  C    sing N N 169 
ILE CA  CB   sing N N 170 
ILE CA  HA   sing N N 171 
ILE C   O    doub N N 172 
ILE C   OXT  sing N N 173 
ILE CB  CG1  sing N N 174 
ILE CB  CG2  sing N N 175 
ILE CB  HB   sing N N 176 
ILE CG1 CD1  sing N N 177 
ILE CG1 HG12 sing N N 178 
ILE CG1 HG13 sing N N 179 
ILE CG2 HG21 sing N N 180 
ILE CG2 HG22 sing N N 181 
ILE CG2 HG23 sing N N 182 
ILE CD1 HD11 sing N N 183 
ILE CD1 HD12 sing N N 184 
ILE CD1 HD13 sing N N 185 
ILE OXT HXT  sing N N 186 
LEU N   CA   sing N N 187 
LEU N   H    sing N N 188 
LEU N   H2   sing N N 189 
LEU CA  C    sing N N 190 
LEU CA  CB   sing N N 191 
LEU CA  HA   sing N N 192 
LEU C   O    doub N N 193 
LEU C   OXT  sing N N 194 
LEU CB  CG   sing N N 195 
LEU CB  HB2  sing N N 196 
LEU CB  HB3  sing N N 197 
LEU CG  CD1  sing N N 198 
LEU CG  CD2  sing N N 199 
LEU CG  HG   sing N N 200 
LEU CD1 HD11 sing N N 201 
LEU CD1 HD12 sing N N 202 
LEU CD1 HD13 sing N N 203 
LEU CD2 HD21 sing N N 204 
LEU CD2 HD22 sing N N 205 
LEU CD2 HD23 sing N N 206 
LEU OXT HXT  sing N N 207 
LYS N   CA   sing N N 208 
LYS N   H    sing N N 209 
LYS N   H2   sing N N 210 
LYS CA  C    sing N N 211 
LYS CA  CB   sing N N 212 
LYS CA  HA   sing N N 213 
LYS C   O    doub N N 214 
LYS C   OXT  sing N N 215 
LYS CB  CG   sing N N 216 
LYS CB  HB2  sing N N 217 
LYS CB  HB3  sing N N 218 
LYS CG  CD   sing N N 219 
LYS CG  HG2  sing N N 220 
LYS CG  HG3  sing N N 221 
LYS CD  CE   sing N N 222 
LYS CD  HD2  sing N N 223 
LYS CD  HD3  sing N N 224 
LYS CE  NZ   sing N N 225 
LYS CE  HE2  sing N N 226 
LYS CE  HE3  sing N N 227 
LYS NZ  HZ1  sing N N 228 
LYS NZ  HZ2  sing N N 229 
LYS NZ  HZ3  sing N N 230 
LYS OXT HXT  sing N N 231 
MET N   CA   sing N N 232 
MET N   H    sing N N 233 
MET N   H2   sing N N 234 
MET CA  C    sing N N 235 
MET CA  CB   sing N N 236 
MET CA  HA   sing N N 237 
MET C   O    doub N N 238 
MET C   OXT  sing N N 239 
MET CB  CG   sing N N 240 
MET CB  HB2  sing N N 241 
MET CB  HB3  sing N N 242 
MET CG  SD   sing N N 243 
MET CG  HG2  sing N N 244 
MET CG  HG3  sing N N 245 
MET SD  CE   sing N N 246 
MET CE  HE1  sing N N 247 
MET CE  HE2  sing N N 248 
MET CE  HE3  sing N N 249 
MET OXT HXT  sing N N 250 
PHE N   CA   sing N N 251 
PHE N   H    sing N N 252 
PHE N   H2   sing N N 253 
PHE CA  C    sing N N 254 
PHE CA  CB   sing N N 255 
PHE CA  HA   sing N N 256 
PHE C   O    doub N N 257 
PHE C   OXT  sing N N 258 
PHE CB  CG   sing N N 259 
PHE CB  HB2  sing N N 260 
PHE CB  HB3  sing N N 261 
PHE CG  CD1  doub Y N 262 
PHE CG  CD2  sing Y N 263 
PHE CD1 CE1  sing Y N 264 
PHE CD1 HD1  sing N N 265 
PHE CD2 CE2  doub Y N 266 
PHE CD2 HD2  sing N N 267 
PHE CE1 CZ   doub Y N 268 
PHE CE1 HE1  sing N N 269 
PHE CE2 CZ   sing Y N 270 
PHE CE2 HE2  sing N N 271 
PHE CZ  HZ   sing N N 272 
PHE OXT HXT  sing N N 273 
PRO N   CA   sing N N 274 
PRO N   CD   sing N N 275 
PRO N   H    sing N N 276 
PRO CA  C    sing N N 277 
PRO CA  CB   sing N N 278 
PRO CA  HA   sing N N 279 
PRO C   O    doub N N 280 
PRO C   OXT  sing N N 281 
PRO CB  CG   sing N N 282 
PRO CB  HB2  sing N N 283 
PRO CB  HB3  sing N N 284 
PRO CG  CD   sing N N 285 
PRO CG  HG2  sing N N 286 
PRO CG  HG3  sing N N 287 
PRO CD  HD2  sing N N 288 
PRO CD  HD3  sing N N 289 
PRO OXT HXT  sing N N 290 
SER N   CA   sing N N 291 
SER N   H    sing N N 292 
SER N   H2   sing N N 293 
SER CA  C    sing N N 294 
SER CA  CB   sing N N 295 
SER CA  HA   sing N N 296 
SER C   O    doub N N 297 
SER C   OXT  sing N N 298 
SER CB  OG   sing N N 299 
SER CB  HB2  sing N N 300 
SER CB  HB3  sing N N 301 
SER OG  HG   sing N N 302 
SER OXT HXT  sing N N 303 
THR N   CA   sing N N 304 
THR N   H    sing N N 305 
THR N   H2   sing N N 306 
THR CA  C    sing N N 307 
THR CA  CB   sing N N 308 
THR CA  HA   sing N N 309 
THR C   O    doub N N 310 
THR C   OXT  sing N N 311 
THR CB  OG1  sing N N 312 
THR CB  CG2  sing N N 313 
THR CB  HB   sing N N 314 
THR OG1 HG1  sing N N 315 
THR CG2 HG21 sing N N 316 
THR CG2 HG22 sing N N 317 
THR CG2 HG23 sing N N 318 
THR OXT HXT  sing N N 319 
TRP N   CA   sing N N 320 
TRP N   H    sing N N 321 
TRP N   H2   sing N N 322 
TRP CA  C    sing N N 323 
TRP CA  CB   sing N N 324 
TRP CA  HA   sing N N 325 
TRP C   O    doub N N 326 
TRP C   OXT  sing N N 327 
TRP CB  CG   sing N N 328 
TRP CB  HB2  sing N N 329 
TRP CB  HB3  sing N N 330 
TRP CG  CD1  doub Y N 331 
TRP CG  CD2  sing Y N 332 
TRP CD1 NE1  sing Y N 333 
TRP CD1 HD1  sing N N 334 
TRP CD2 CE2  doub Y N 335 
TRP CD2 CE3  sing Y N 336 
TRP NE1 CE2  sing Y N 337 
TRP NE1 HE1  sing N N 338 
TRP CE2 CZ2  sing Y N 339 
TRP CE3 CZ3  doub Y N 340 
TRP CE3 HE3  sing N N 341 
TRP CZ2 CH2  doub Y N 342 
TRP CZ2 HZ2  sing N N 343 
TRP CZ3 CH2  sing Y N 344 
TRP CZ3 HZ3  sing N N 345 
TRP CH2 HH2  sing N N 346 
TRP OXT HXT  sing N N 347 
TYR N   CA   sing N N 348 
TYR N   H    sing N N 349 
TYR N   H2   sing N N 350 
TYR CA  C    sing N N 351 
TYR CA  CB   sing N N 352 
TYR CA  HA   sing N N 353 
TYR C   O    doub N N 354 
TYR C   OXT  sing N N 355 
TYR CB  CG   sing N N 356 
TYR CB  HB2  sing N N 357 
TYR CB  HB3  sing N N 358 
TYR CG  CD1  doub Y N 359 
TYR CG  CD2  sing Y N 360 
TYR CD1 CE1  sing Y N 361 
TYR CD1 HD1  sing N N 362 
TYR CD2 CE2  doub Y N 363 
TYR CD2 HD2  sing N N 364 
TYR CE1 CZ   doub Y N 365 
TYR CE1 HE1  sing N N 366 
TYR CE2 CZ   sing Y N 367 
TYR CE2 HE2  sing N N 368 
TYR CZ  OH   sing N N 369 
TYR OH  HH   sing N N 370 
TYR OXT HXT  sing N N 371 
VAL N   CA   sing N N 372 
VAL N   H    sing N N 373 
VAL N   H2   sing N N 374 
VAL CA  C    sing N N 375 
VAL CA  CB   sing N N 376 
VAL CA  HA   sing N N 377 
VAL C   O    doub N N 378 
VAL C   OXT  sing N N 379 
VAL CB  CG1  sing N N 380 
VAL CB  CG2  sing N N 381 
VAL CB  HB   sing N N 382 
VAL CG1 HG11 sing N N 383 
VAL CG1 HG12 sing N N 384 
VAL CG1 HG13 sing N N 385 
VAL CG2 HG21 sing N N 386 
VAL CG2 HG22 sing N N 387 
VAL CG2 HG23 sing N N 388 
VAL OXT HXT  sing N N 389 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6LUH 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IXF 
_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]   0.021798 
_atom_sites.fract_transf_matrix[1][2]   -0.007700 
_atom_sites.fract_transf_matrix[1][3]   -0.000722 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022718 
_atom_sites.fract_transf_matrix[2][3]   -0.001493 
_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]   0.017240 
_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  
MG 
MN 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 1   ? 35.881 25.462  45.883  1.00 37.54 ?  1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 35.118 24.225  45.811  1.00 35.02 ?  1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 35.988 23.022  46.214  1.00 31.33 ?  1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 37.191 22.995  45.944  1.00 31.12 ?  1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 34.553 24.030  44.399  1.00 40.59 ?  1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 33.913 22.663  44.141  1.00 47.45 ?  1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 32.400 22.718  43.149  1.00 72.56 ?  1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 31.873 21.004  43.251  1.00 45.79 ?  1   MET A CE  1 
ATOM   9    N  N   . ILE A 1 2   ? 35.362 22.053  46.879  1.00 29.30 ?  2   ILE A N   1 
ATOM   10   C  CA  . ILE A 1 2   ? 35.982 20.780  47.236  1.00 24.20 ?  2   ILE A CA  1 
ATOM   11   C  C   . ILE A 1 2   ? 35.359 19.682  46.376  1.00 30.88 ?  2   ILE A C   1 
ATOM   12   O  O   . ILE A 1 2   ? 34.129 19.602  46.264  1.00 29.64 ?  2   ILE A O   1 
ATOM   13   C  CB  . ILE A 1 2   ? 35.790 20.479  48.733  1.00 25.19 ?  2   ILE A CB  1 
ATOM   14   C  CG1 . ILE A 1 2   ? 36.431 21.575  49.590  1.00 24.53 ?  2   ILE A CG1 1 
ATOM   15   C  CG2 . ILE A 1 2   ? 36.336 19.108  49.071  1.00 24.78 ?  2   ILE A CG2 1 
ATOM   16   C  CD1 . ILE A 1 2   ? 36.026 21.526  51.050  1.00 23.68 ?  2   ILE A CD1 1 
ATOM   17   N  N   . ASP A 1 3   ? 36.205 18.850  45.754  1.00 23.21 ?  3   ASP A N   1 
ATOM   18   C  CA  . ASP A 1 3   ? 35.786 17.600  45.120  1.00 21.37 ?  3   ASP A CA  1 
ATOM   19   C  C   . ASP A 1 3   ? 36.128 16.457  46.070  1.00 24.28 ?  3   ASP A C   1 
ATOM   20   O  O   . ASP A 1 3   ? 37.303 16.259  46.379  1.00 24.09 ?  3   ASP A O   1 
ATOM   21   C  CB  . ASP A 1 3   ? 36.510 17.352  43.794  1.00 24.09 ?  3   ASP A CB  1 
ATOM   22   C  CG  . ASP A 1 3   ? 36.107 18.308  42.689  1.00 35.49 ?  3   ASP A CG  1 
ATOM   23   O  OD1 . ASP A 1 3   ? 34.922 18.695  42.614  1.00 41.34 ?  3   ASP A OD1 1 
ATOM   24   O  OD2 . ASP A 1 3   ? 36.990 18.634  41.865  1.00 35.58 -1 3   ASP A OD2 1 
ATOM   25   N  N   . LEU A 1 4   ? 35.124 15.688  46.497  1.00 22.17 ?  4   LEU A N   1 
ATOM   26   C  CA  . LEU A 1 4   ? 35.325 14.577  47.423  1.00 20.34 ?  4   LEU A CA  1 
ATOM   27   C  C   . LEU A 1 4   ? 35.233 13.255  46.669  1.00 22.84 ?  4   LEU A C   1 
ATOM   28   O  O   . LEU A 1 4   ? 34.243 13.004  45.969  1.00 19.55 ?  4   LEU A O   1 
ATOM   29   C  CB  . LEU A 1 4   ? 34.300 14.613  48.558  1.00 19.46 ?  4   LEU A CB  1 
ATOM   30   C  CG  . LEU A 1 4   ? 34.265 13.424  49.517  1.00 20.22 ?  4   LEU A CG  1 
ATOM   31   C  CD1 . LEU A 1 4   ? 35.629 13.300  50.208  1.00 18.66 ?  4   LEU A CD1 1 
ATOM   32   C  CD2 . LEU A 1 4   ? 33.166 13.600  50.552  1.00 21.72 ?  4   LEU A CD2 1 
ATOM   33   N  N   . ILE A 1 5   ? 36.281 12.434  46.789  1.00 14.35 ?  5   ILE A N   1 
ATOM   34   C  CA  . ILE A 1 5   ? 36.359 11.112  46.171  1.00 14.81 ?  5   ILE A CA  1 
ATOM   35   C  C   . ILE A 1 5   ? 36.613 10.114  47.292  1.00 18.95 ?  5   ILE A C   1 
ATOM   36   O  O   . ILE A 1 5   ? 37.450 10.370  48.165  1.00 16.19 ?  5   ILE A O   1 
ATOM   37   C  CB  . ILE A 1 5   ? 37.484 11.037  45.121  1.00 17.28 ?  5   ILE A CB  1 
ATOM   38   C  CG1 . ILE A 1 5   ? 37.249 12.040  43.977  1.00 22.21 ?  5   ILE A CG1 1 
ATOM   39   C  CG2 . ILE A 1 5   ? 37.636 9.604   44.607  1.00 17.78 ?  5   ILE A CG2 1 
ATOM   40   C  CD1 . ILE A 1 5   ? 38.510 12.392  43.219  1.00 17.93 ?  5   ILE A CD1 1 
ATOM   41   N  N   . VAL A 1 6   ? 35.877 9.000   47.296  1.00 14.15 ?  6   VAL A N   1 
ATOM   42   C  CA  . VAL A 1 6   ? 35.936 8.047   48.406  1.00 14.00 ?  6   VAL A CA  1 
ATOM   43   C  C   . VAL A 1 6   ? 36.186 6.653   47.857  1.00 16.49 ?  6   VAL A C   1 
ATOM   44   O  O   . VAL A 1 6   ? 35.409 6.163   47.025  1.00 14.81 ?  6   VAL A O   1 
ATOM   45   C  CB  . VAL A 1 6   ? 34.642 8.051   49.236  1.00 16.35 ?  6   VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 6   ? 34.841 7.259   50.528  1.00 16.88 ?  6   VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 6   ? 34.195 9.501   49.518  1.00 15.95 ?  6   VAL A CG2 1 
ATOM   48   N  N   . SER A 1 7   ? 37.238 5.994   48.345  1.00 14.61 ?  7   SER A N   1 
ATOM   49   C  CA  . SER A 1 7   ? 37.486 4.616   47.943  1.00 14.49 ?  7   SER A CA  1 
ATOM   50   C  C   . SER A 1 7   ? 36.704 3.674   48.844  1.00 17.89 ?  7   SER A C   1 
ATOM   51   O  O   . SER A 1 7   ? 36.765 3.782   50.072  1.00 19.18 ?  7   SER A O   1 
ATOM   52   C  CB  . SER A 1 7   ? 38.983 4.281   47.996  1.00 15.81 ?  7   SER A CB  1 
ATOM   53   O  OG  . SER A 1 7   ? 39.180 2.903   47.674  1.00 18.15 ?  7   SER A OG  1 
ATOM   54   N  N   . GLN A 1 8   ? 35.958 2.750   48.230  1.00 16.33 ?  8   GLN A N   1 
ATOM   55   C  CA  . GLN A 1 8   ? 35.268 1.712   48.977  1.00 16.85 ?  8   GLN A CA  1 
ATOM   56   C  C   . GLN A 1 8   ? 35.614 0.320   48.459  1.00 18.11 ?  8   GLN A C   1 
ATOM   57   O  O   . GLN A 1 8   ? 35.030 -0.674  48.916  1.00 21.87 ?  8   GLN A O   1 
ATOM   58   C  CB  . GLN A 1 8   ? 33.757 1.949   48.940  1.00 18.13 ?  8   GLN A CB  1 
ATOM   59   C  CG  . GLN A 1 8   ? 33.337 3.169   49.738  1.00 17.88 ?  8   GLN A CG  1 
ATOM   60   C  CD  . GLN A 1 8   ? 33.406 2.914   51.223  1.00 20.99 ?  8   GLN A CD  1 
ATOM   61   O  OE1 . GLN A 1 8   ? 32.473 2.370   51.816  1.00 21.65 ?  8   GLN A OE1 1 
ATOM   62   N  NE2 . GLN A 1 8   ? 34.532 3.295   51.841  1.00 19.86 ?  8   GLN A NE2 1 
ATOM   63   N  N   . GLY A 1 9   ? 36.560 0.216   47.542  1.00 15.90 ?  9   GLY A N   1 
ATOM   64   C  CA  . GLY A 1 9   ? 37.035 -1.077  47.109  1.00 16.33 ?  9   GLY A CA  1 
ATOM   65   C  C   . GLY A 1 9   ? 38.246 -1.483  47.926  1.00 16.13 ?  9   GLY A C   1 
ATOM   66   O  O   . GLY A 1 9   ? 39.030 -0.639  48.355  1.00 16.52 ?  9   GLY A O   1 
ATOM   67   N  N   . ARG A 1 10  ? 38.382 -2.789  48.149  1.00 16.72 ?  10  ARG A N   1 
ATOM   68   C  CA  . ARG A 1 10  ? 39.574 -3.287  48.818  1.00 15.14 ?  10  ARG A CA  1 
ATOM   69   C  C   . ARG A 1 10  ? 40.811 -2.965  47.994  1.00 16.43 ?  10  ARG A C   1 
ATOM   70   O  O   . ARG A 1 10  ? 40.854 -3.223  46.782  1.00 12.65 ?  10  ARG A O   1 
ATOM   71   C  CB  . ARG A 1 10  ? 39.485 -4.794  49.050  1.00 16.59 ?  10  ARG A CB  1 
ATOM   72   C  CG  . ARG A 1 10  ? 40.721 -5.310  49.757  1.00 16.65 ?  10  ARG A CG  1 
ATOM   73   C  CD  . ARG A 1 10  ? 40.585 -6.711  50.277  1.00 17.47 ?  10  ARG A CD  1 
ATOM   74   N  NE  . ARG A 1 10  ? 41.788 -7.039  51.039  1.00 17.44 ?  10  ARG A NE  1 
ATOM   75   C  CZ  . ARG A 1 10  ? 42.806 -7.757  50.574  1.00 17.87 ?  10  ARG A CZ  1 
ATOM   76   N  NH1 . ARG A 1 10  ? 42.777 -8.259  49.347  1.00 15.85 ?  10  ARG A NH1 1 
ATOM   77   N  NH2 . ARG A 1 10  ? 43.862 -7.985  51.350  1.00 19.08 ?  10  ARG A NH2 1 
ATOM   78   N  N   . VAL A 1 11  ? 41.810 -2.370  48.660  1.00 11.83 ?  11  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 11  ? 43.145 -2.214  48.099  1.00 12.09 ?  11  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 11  ? 44.136 -2.749  49.122  1.00 15.09 ?  11  VAL A C   1 
ATOM   81   O  O   . VAL A 1 11  ? 44.733 -1.987  49.891  1.00 15.94 ?  11  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 11  ? 43.453 -0.753  47.705  1.00 12.11 ?  11  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 11  ? 44.772 -0.709  46.921  1.00 14.59 ?  11  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 11  ? 42.322 -0.204  46.822  1.00 15.77 ?  11  VAL A CG2 1 
ATOM   85   N  N   . ALA A 1 12  ? 44.271 -4.079  49.155  1.00 12.81 ?  12  ALA A N   1 
ATOM   86   C  CA  . ALA A 1 12  ? 45.215 -4.843  49.963  1.00 13.01 ?  12  ALA A CA  1 
ATOM   87   C  C   . ALA A 1 12  ? 44.918 -4.803  51.462  1.00 14.95 ?  12  ALA A C   1 
ATOM   88   O  O   . ALA A 1 12  ? 45.764 -5.264  52.254  1.00 14.98 ?  12  ALA A O   1 
ATOM   89   C  CB  . ALA A 1 12  ? 46.662 -4.401  49.695  1.00 13.08 ?  12  ALA A CB  1 
ATOM   90   N  N   . ASP A 1 13  ? 43.739 -4.303  51.874  1.00 14.10 ?  13  ASP A N   1 
ATOM   91   C  CA  . ASP A 1 13  ? 43.410 -4.124  53.294  1.00 14.62 ?  13  ASP A CA  1 
ATOM   92   C  C   . ASP A 1 13  ? 43.742 -5.353  54.128  1.00 15.28 ?  13  ASP A C   1 
ATOM   93   O  O   . ASP A 1 13  ? 43.228 -6.440  53.866  1.00 15.08 ?  13  ASP A O   1 
ATOM   94   C  CB  . ASP A 1 13  ? 41.914 -3.847  53.469  1.00 15.50 ?  13  ASP A CB  1 
ATOM   95   C  CG  . ASP A 1 13  ? 41.430 -2.622  52.716  1.00 16.89 ?  13  ASP A CG  1 
ATOM   96   O  OD1 . ASP A 1 13  ? 41.768 -2.468  51.533  1.00 17.94 ?  13  ASP A OD1 1 
ATOM   97   O  OD2 . ASP A 1 13  ? 40.673 -1.838  53.320  1.00 20.25 -1 13  ASP A OD2 1 
ATOM   98   N  N   . ARG A 1 14  ? 44.555 -5.158  55.169  1.00 13.32 ?  14  ARG A N   1 
ATOM   99   C  CA  . ARG A 1 14  ? 44.778 -6.178  56.192  1.00 13.36 ?  14  ARG A CA  1 
ATOM   100  C  C   . ARG A 1 14  ? 44.012 -5.905  57.473  1.00 15.99 ?  14  ARG A C   1 
ATOM   101  O  O   . ARG A 1 14  ? 43.960 -6.781  58.343  1.00 18.94 ?  14  ARG A O   1 
ATOM   102  C  CB  . ARG A 1 14  ? 46.276 -6.297  56.506  1.00 15.68 ?  14  ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 14  ? 47.038 -6.831  55.305  1.00 16.27 ?  14  ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 14  ? 48.470 -7.276  55.597  1.00 14.47 ?  14  ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 14  ? 49.033 -7.888  54.378  1.00 15.62 ?  14  ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 14  ? 50.232 -8.455  54.309  1.00 18.42 ?  14  ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 14  ? 51.001 -8.518  55.394  1.00 17.39 ?  14  ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 14  ? 50.650 -8.988  53.167  1.00 16.45 ?  14  ARG A NH2 1 
ATOM   109  N  N   . ALA A 1 15  ? 43.440 -4.717  57.617  1.00 13.33 ?  15  ALA A N   1 
ATOM   110  C  CA  . ALA A 1 15  ? 42.617 -4.364  58.760  1.00 12.43 ?  15  ALA A CA  1 
ATOM   111  C  C   . ALA A 1 15  ? 41.142 -4.479  58.406  1.00 15.42 ?  15  ALA A C   1 
ATOM   112  O  O   . ALA A 1 15  ? 40.744 -4.308  57.245  1.00 16.51 ?  15  ALA A O   1 
ATOM   113  C  CB  . ALA A 1 15  ? 42.920 -2.936  59.231  1.00 13.79 ?  15  ALA A CB  1 
ATOM   114  N  N   . ALA A 1 16  ? 40.326 -4.725  59.433  1.00 16.54 ?  16  ALA A N   1 
ATOM   115  C  CA  . ALA A 1 16  ? 38.927 -5.081  59.224  1.00 17.91 ?  16  ALA A CA  1 
ATOM   116  C  C   . ALA A 1 16  ? 38.027 -3.894  58.912  1.00 17.84 ?  16  ALA A C   1 
ATOM   117  O  O   . ALA A 1 16  ? 37.006 -4.070  58.238  1.00 16.17 ?  16  ALA A O   1 
ATOM   118  C  CB  . ALA A 1 16  ? 38.381 -5.804  60.462  1.00 19.15 ?  16  ALA A CB  1 
ATOM   119  N  N   . TRP A 1 17  ? 38.345 -2.695  59.403  1.00 14.24 ?  17  TRP A N   1 
ATOM   120  C  CA  . TRP A 1 17  ? 37.351 -1.628  59.428  1.00 14.26 ?  17  TRP A CA  1 
ATOM   121  C  C   . TRP A 1 17  ? 37.793 -0.373  58.692  1.00 14.20 ?  17  TRP A C   1 
ATOM   122  O  O   . TRP A 1 17  ? 37.194 0.692   58.900  1.00 16.42 ?  17  TRP A O   1 
ATOM   123  C  CB  . TRP A 1 17  ? 36.983 -1.277  60.872  1.00 16.36 ?  17  TRP A CB  1 
ATOM   124  C  CG  . TRP A 1 17  ? 36.479 -2.468  61.677  1.00 18.76 ?  17  TRP A CG  1 
ATOM   125  C  CD1 . TRP A 1 17  ? 35.452 -3.309  61.343  1.00 21.09 ?  17  TRP A CD1 1 
ATOM   126  C  CD2 . TRP A 1 17  ? 36.994 -2.945  62.931  1.00 16.95 ?  17  TRP A CD2 1 
ATOM   127  N  NE1 . TRP A 1 17  ? 35.302 -4.280  62.310  1.00 23.61 ?  17  TRP A NE1 1 
ATOM   128  C  CE2 . TRP A 1 17  ? 36.227 -4.072  63.298  1.00 19.72 ?  17  TRP A CE2 1 
ATOM   129  C  CE3 . TRP A 1 17  ? 38.015 -2.514  63.789  1.00 24.79 ?  17  TRP A CE3 1 
ATOM   130  C  CZ2 . TRP A 1 17  ? 36.457 -4.785  64.481  1.00 27.18 ?  17  TRP A CZ2 1 
ATOM   131  C  CZ3 . TRP A 1 17  ? 38.237 -3.217  64.967  1.00 28.52 ?  17  TRP A CZ3 1 
ATOM   132  C  CH2 . TRP A 1 17  ? 37.458 -4.342  65.301  1.00 24.36 ?  17  TRP A CH2 1 
ATOM   133  N  N   . MET A 1 18  ? 38.792 -0.472  57.805  1.00 12.82 ?  18  MET A N   1 
ATOM   134  C  CA  . MET A 1 18  ? 39.267 0.741   57.136  1.00 10.28 ?  18  MET A CA  1 
ATOM   135  C  C   . MET A 1 18  ? 38.364 1.172   55.978  1.00 15.24 ?  18  MET A C   1 
ATOM   136  O  O   . MET A 1 18  ? 38.288 2.372   55.672  1.00 12.67 ?  18  MET A O   1 
ATOM   137  C  CB  . MET A 1 18  ? 40.706 0.548   56.677  1.00 12.12 ?  18  MET A CB  1 
ATOM   138  C  CG  . MET A 1 18  ? 41.727 0.772   57.831  1.00 13.36 ?  18  MET A CG  1 
ATOM   139  S  SD  . MET A 1 18  ? 43.408 0.497   57.248  1.00 15.70 ?  18  MET A SD  1 
ATOM   140  C  CE  . MET A 1 18  ? 44.244 0.454   58.843  1.00 13.37 ?  18  MET A CE  1 
ATOM   141  N  N   . ILE A 1 19  ? 37.659 0.236   55.332  1.00 12.09 ?  19  ILE A N   1 
ATOM   142  C  CA  . ILE A 1 19  ? 36.640 0.667   54.372  1.00 13.49 ?  19  ILE A CA  1 
ATOM   143  C  C   . ILE A 1 19  ? 35.505 1.376   55.105  1.00 14.38 ?  19  ILE A C   1 
ATOM   144  O  O   . ILE A 1 19  ? 35.066 2.455   54.696  1.00 14.42 ?  19  ILE A O   1 
ATOM   145  C  CB  . ILE A 1 19  ? 36.141 -0.524  53.533  1.00 16.17 ?  19  ILE A CB  1 
ATOM   146  C  CG1 . ILE A 1 19  ? 37.222 -0.914  52.528  1.00 14.75 ?  19  ILE A CG1 1 
ATOM   147  C  CG2 . ILE A 1 19  ? 34.843 -0.144  52.781  1.00 15.44 ?  19  ILE A CG2 1 
ATOM   148  C  CD1 . ILE A 1 19  ? 37.007 -2.282  51.854  1.00 16.69 ?  19  ILE A CD1 1 
ATOM   149  N  N   . GLU A 1 20  ? 35.074 0.825   56.246  1.00 14.57 ?  20  GLU A N   1 
ATOM   150  C  CA  . GLU A 1 20  ? 34.056 1.483   57.070  1.00 18.34 ?  20  GLU A CA  1 
ATOM   151  C  C   . GLU A 1 20  ? 34.533 2.823   57.609  1.00 17.95 ?  20  GLU A C   1 
ATOM   152  O  O   . GLU A 1 20  ? 33.749 3.780   57.674  1.00 14.79 ?  20  GLU A O   1 
ATOM   153  C  CB  . GLU A 1 20  ? 33.633 0.575   58.228  1.00 17.98 ?  20  GLU A CB  1 
ATOM   154  C  CG  . GLU A 1 20  ? 32.791 -0.584  57.722  1.00 21.88 ?  20  GLU A CG  1 
ATOM   155  C  CD  . GLU A 1 20  ? 32.317 -1.536  58.802  1.00 34.11 ?  20  GLU A CD  1 
ATOM   156  O  OE1 . GLU A 1 20  ? 32.391 -1.201  60.002  1.00 32.39 ?  20  GLU A OE1 1 
ATOM   157  O  OE2 . GLU A 1 20  ? 31.856 -2.634  58.428  1.00 39.96 -1 20  GLU A OE2 1 
ATOM   158  N  N   . GLY A 1 21  ? 35.796 2.902   58.043  1.00 15.53 ?  21  GLY A N   1 
ATOM   159  C  CA  . GLY A 1 21  ? 36.312 4.169   58.534  1.00 14.04 ?  21  GLY A CA  1 
ATOM   160  C  C   . GLY A 1 21  ? 36.307 5.244   57.459  1.00 14.53 ?  21  GLY A C   1 
ATOM   161  O  O   . GLY A 1 21  ? 36.003 6.406   57.731  1.00 15.17 ?  21  GLY A O   1 
ATOM   162  N  N   . ALA A 1 22  ? 36.664 4.870   56.225  1.00 13.43 ?  22  ALA A N   1 
ATOM   163  C  CA  . ALA A 1 22  ? 36.623 5.818   55.121  1.00 13.61 ?  22  ALA A CA  1 
ATOM   164  C  C   . ALA A 1 22  ? 35.199 6.300   54.870  1.00 16.02 ?  22  ALA A C   1 
ATOM   165  O  O   . ALA A 1 22  ? 34.962 7.496   54.673  1.00 15.59 ?  22  ALA A O   1 
ATOM   166  C  CB  . ALA A 1 22  ? 37.214 5.175   53.858  1.00 13.89 ?  22  ALA A CB  1 
ATOM   167  N  N   . ALA A 1 23  ? 34.231 5.379   54.892  1.00 17.22 ?  23  ALA A N   1 
ATOM   168  C  CA  . ALA A 1 23  ? 32.846 5.777   54.666  1.00 20.23 ?  23  ALA A CA  1 
ATOM   169  C  C   . ALA A 1 23  ? 32.358 6.739   55.747  1.00 18.65 ?  23  ALA A C   1 
ATOM   170  O  O   . ALA A 1 23  ? 31.675 7.722   55.444  1.00 19.22 ?  23  ALA A O   1 
ATOM   171  C  CB  . ALA A 1 23  ? 31.953 4.541   54.588  1.00 17.85 ?  23  ALA A CB  1 
ATOM   172  N  N   . ARG A 1 24  ? 32.725 6.492   57.007  1.00 13.02 ?  24  ARG A N   1 
ATOM   173  C  CA  . ARG A 1 24  ? 32.300 7.374   58.091  1.00 16.19 ?  24  ARG A CA  1 
ATOM   174  C  C   . ARG A 1 24  ? 32.960 8.751   57.984  1.00 18.70 ?  24  ARG A C   1 
ATOM   175  O  O   . ARG A 1 24  ? 32.316 9.786   58.218  1.00 18.79 ?  24  ARG A O   1 
ATOM   176  C  CB  . ARG A 1 24  ? 32.613 6.710   59.440  1.00 17.84 ?  24  ARG A CB  1 
ATOM   177  C  CG  . ARG A 1 24  ? 32.085 7.457   60.663  1.00 25.41 ?  24  ARG A CG  1 
ATOM   178  C  CD  . ARG A 1 24  ? 30.564 7.583   60.612  1.00 30.96 ?  24  ARG A CD  1 
ATOM   179  N  NE  . ARG A 1 24  ? 30.059 8.474   61.651  1.00 32.18 ?  24  ARG A NE  1 
ATOM   180  C  CZ  . ARG A 1 24  ? 29.849 9.774   61.481  1.00 34.92 ?  24  ARG A CZ  1 
ATOM   181  N  NH1 . ARG A 1 24  ? 30.091 10.346  60.310  1.00 30.94 ?  24  ARG A NH1 1 
ATOM   182  N  NH2 . ARG A 1 24  ? 29.392 10.505  62.488  1.00 41.97 ?  24  ARG A NH2 1 
ATOM   183  N  N   . THR A 1 25  ? 34.236 8.793   57.605  1.00 15.86 ?  25  THR A N   1 
ATOM   184  C  CA  . THR A 1 25  ? 34.909 10.081  57.428  1.00 15.51 ?  25  THR A CA  1 
ATOM   185  C  C   . THR A 1 25  ? 34.257 10.887  56.314  1.00 14.77 ?  25  THR A C   1 
ATOM   186  O  O   . THR A 1 25  ? 34.025 12.098  56.450  1.00 17.14 ?  25  THR A O   1 
ATOM   187  C  CB  . THR A 1 25  ? 36.388 9.852   57.113  1.00 16.56 ?  25  THR A CB  1 
ATOM   188  O  OG1 . THR A 1 25  ? 36.996 9.180   58.212  1.00 14.91 ?  25  THR A OG1 1 
ATOM   189  C  CG2 . THR A 1 25  ? 37.119 11.180  56.840  1.00 14.28 ?  25  THR A CG2 1 
ATOM   190  N  N   . ALA A 1 26  ? 33.985 10.221  55.190  1.00 15.26 ?  26  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 26  ? 33.368 10.863  54.042  1.00 16.34 ?  26  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 26  ? 32.008 11.426  54.407  1.00 18.48 ?  26  ALA A C   1 
ATOM   193  O  O   . ALA A 1 26  ? 31.662 12.545  54.005  1.00 18.18 ?  26  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 26  ? 33.234 9.851   52.906  1.00 17.80 ?  26  ALA A CB  1 
ATOM   195  N  N   . ARG A 1 27  ? 31.227 10.664  55.168  1.00 19.65 ?  27  ARG A N   1 
ATOM   196  C  CA  . ARG A 1 27  ? 29.901 11.137  55.556  1.00 21.38 ?  27  ARG A CA  1 
ATOM   197  C  C   . ARG A 1 27  ? 29.996 12.398  56.404  1.00 23.43 ?  27  ARG A C   1 
ATOM   198  O  O   . ARG A 1 27  ? 29.229 13.346  56.198  1.00 22.33 ?  27  ARG A O   1 
ATOM   199  C  CB  . ARG A 1 27  ? 29.145 10.040  56.302  1.00 26.35 ?  27  ARG A CB  1 
ATOM   200  C  CG  . ARG A 1 27  ? 27.677 10.381  56.571  1.00 34.00 ?  27  ARG A CG  1 
ATOM   201  C  CD  . ARG A 1 27  ? 27.222 9.921   57.962  1.00 39.07 ?  27  ARG A CD  1 
ATOM   202  N  NE  . ARG A 1 27  ? 27.428 8.489   58.172  1.00 40.56 ?  27  ARG A NE  1 
ATOM   203  C  CZ  . ARG A 1 27  ? 27.162 7.849   59.309  1.00 45.05 ?  27  ARG A CZ  1 
ATOM   204  N  NH1 . ARG A 1 27  ? 26.667 8.514   60.349  1.00 39.66 ?  27  ARG A NH1 1 
ATOM   205  N  NH2 . ARG A 1 27  ? 27.387 6.542   59.405  1.00 40.93 ?  27  ARG A NH2 1 
ATOM   206  N  N   . ALA A 1 28  ? 30.952 12.442  57.342  1.00 20.21 ?  28  ALA A N   1 
ATOM   207  C  CA  . ALA A 1 28  ? 31.132 13.631  58.174  1.00 21.27 ?  28  ALA A CA  1 
ATOM   208  C  C   . ALA A 1 28  ? 31.510 14.848  57.333  1.00 20.70 ?  28  ALA A C   1 
ATOM   209  O  O   . ALA A 1 28  ? 31.040 15.966  57.593  1.00 20.29 ?  28  ALA A O   1 
ATOM   210  C  CB  . ALA A 1 28  ? 32.191 13.370  59.253  1.00 21.47 ?  28  ALA A CB  1 
ATOM   211  N  N   . LEU A 1 29  ? 32.364 14.657  56.327  1.00 16.86 ?  29  LEU A N   1 
ATOM   212  C  CA  . LEU A 1 29  ? 32.745 15.771  55.461  1.00 15.57 ?  29  LEU A CA  1 
ATOM   213  C  C   . LEU A 1 29  ? 31.577 16.219  54.593  1.00 18.93 ?  29  LEU A C   1 
ATOM   214  O  O   . LEU A 1 29  ? 31.407 17.416  54.347  1.00 20.43 ?  29  LEU A O   1 
ATOM   215  C  CB  . LEU A 1 29  ? 33.923 15.379  54.566  1.00 17.57 ?  29  LEU A CB  1 
ATOM   216  C  CG  . LEU A 1 29  ? 35.244 15.127  55.288  1.00 15.94 ?  29  LEU A CG  1 
ATOM   217  C  CD1 . LEU A 1 29  ? 36.285 14.548  54.317  1.00 18.69 ?  29  LEU A CD1 1 
ATOM   218  C  CD2 . LEU A 1 29  ? 35.763 16.432  55.929  1.00 16.10 ?  29  LEU A CD2 1 
ATOM   219  N  N   . GLU A 1 30  ? 30.791 15.266  54.087  1.00 19.39 ?  30  GLU A N   1 
ATOM   220  C  CA  . GLU A 1 30  ? 29.601 15.610  53.312  1.00 19.55 ?  30  GLU A CA  1 
ATOM   221  C  C   . GLU A 1 30  ? 28.636 16.451  54.142  1.00 22.82 ?  30  GLU A C   1 
ATOM   222  O  O   . GLU A 1 30  ? 28.125 17.474  53.674  1.00 25.97 ?  30  GLU A O   1 
ATOM   223  C  CB  . GLU A 1 30  ? 28.913 14.338  52.822  1.00 25.34 ?  30  GLU A CB  1 
ATOM   224  C  CG  . GLU A 1 30  ? 29.680 13.585  51.740  1.00 24.73 ?  30  GLU A CG  1 
ATOM   225  C  CD  . GLU A 1 30  ? 28.948 12.340  51.277  1.00 24.73 ?  30  GLU A CD  1 
ATOM   226  O  OE1 . GLU A 1 30  ? 28.315 11.683  52.125  1.00 28.50 ?  30  GLU A OE1 1 
ATOM   227  O  OE2 . GLU A 1 30  ? 29.001 12.023  50.066  1.00 32.39 -1 30  GLU A OE2 1 
ATOM   228  N  N   . GLU A 1 31  ? 28.373 16.031  55.379  1.00 21.03 ?  31  GLU A N   1 
ATOM   229  C  CA  . GLU A 1 31  ? 27.436 16.773  56.226  1.00 24.10 ?  31  GLU A CA  1 
ATOM   230  C  C   . GLU A 1 31  ? 27.990 18.139  56.608  1.00 25.72 ?  31  GLU A C   1 
ATOM   231  O  O   . GLU A 1 31  ? 27.243 19.123  56.659  1.00 28.20 ?  31  GLU A O   1 
ATOM   232  C  CB  . GLU A 1 31  ? 27.096 15.970  57.477  1.00 23.28 ?  31  GLU A CB  1 
ATOM   233  C  CG  . GLU A 1 31  ? 26.164 14.809  57.189  1.00 30.52 ?  31  GLU A CG  1 
ATOM   234  C  CD  . GLU A 1 31  ? 26.224 13.731  58.252  1.00 40.76 ?  31  GLU A CD  1 
ATOM   235  O  OE1 . GLU A 1 31  ? 26.832 13.974  59.318  1.00 46.34 ?  31  GLU A OE1 1 
ATOM   236  O  OE2 . GLU A 1 31  ? 25.666 12.636  58.019  1.00 44.05 -1 31  GLU A OE2 1 
ATOM   237  N  N   . ARG A 1 32  ? 29.296 18.226  56.868  1.00 21.07 ?  32  ARG A N   1 
ATOM   238  C  CA  . ARG A 1 32  ? 29.862 19.494  57.322  1.00 22.48 ?  32  ARG A CA  1 
ATOM   239  C  C   . ARG A 1 32  ? 29.962 20.503  56.183  1.00 19.87 ?  32  ARG A C   1 
ATOM   240  O  O   . ARG A 1 32  ? 29.707 21.701  56.378  1.00 19.64 ?  32  ARG A O   1 
ATOM   241  C  CB  . ARG A 1 32  ? 31.239 19.275  57.956  1.00 19.56 ?  32  ARG A CB  1 
ATOM   242  C  CG  . ARG A 1 32  ? 32.036 20.581  58.151  1.00 20.22 ?  32  ARG A CG  1 
ATOM   243  C  CD  . ARG A 1 32  ? 33.187 20.436  59.148  1.00 18.36 ?  32  ARG A CD  1 
ATOM   244  N  NE  . ARG A 1 32  ? 32.714 20.364  60.531  1.00 21.57 ?  32  ARG A NE  1 
ATOM   245  C  CZ  . ARG A 1 32  ? 33.465 20.612  61.609  1.00 18.99 ?  32  ARG A CZ  1 
ATOM   246  N  NH1 . ARG A 1 32  ? 34.746 20.929  61.490  1.00 18.61 ?  32  ARG A NH1 1 
ATOM   247  N  NH2 . ARG A 1 32  ? 32.920 20.548  62.814  1.00 21.88 ?  32  ARG A NH2 1 
ATOM   248  N  N   . TYR A 1 33  ? 30.355 20.054  54.995  1.00 17.65 ?  33  TYR A N   1 
ATOM   249  C  CA  . TYR A 1 33  ? 30.652 20.962  53.895  1.00 20.46 ?  33  TYR A CA  1 
ATOM   250  C  C   . TYR A 1 33  ? 29.564 21.004  52.827  1.00 22.15 ?  33  TYR A C   1 
ATOM   251  O  O   . TYR A 1 33  ? 29.703 21.751  51.852  1.00 25.35 ?  33  TYR A O   1 
ATOM   252  C  CB  . TYR A 1 33  ? 32.014 20.594  53.281  1.00 19.13 ?  33  TYR A CB  1 
ATOM   253  C  CG  . TYR A 1 33  ? 33.124 20.930  54.249  1.00 18.06 ?  33  TYR A CG  1 
ATOM   254  C  CD1 . TYR A 1 33  ? 33.480 22.259  54.485  1.00 16.40 ?  33  TYR A CD1 1 
ATOM   255  C  CD2 . TYR A 1 33  ? 33.751 19.941  55.004  1.00 18.89 ?  33  TYR A CD2 1 
ATOM   256  C  CE1 . TYR A 1 33  ? 34.450 22.597  55.404  1.00 17.52 ?  33  TYR A CE1 1 
ATOM   257  C  CE2 . TYR A 1 33  ? 34.738 20.269  55.922  1.00 15.59 ?  33  TYR A CE2 1 
ATOM   258  C  CZ  . TYR A 1 33  ? 35.086 21.601  56.113  1.00 18.36 ?  33  TYR A CZ  1 
ATOM   259  O  OH  . TYR A 1 33  ? 36.050 21.948  57.020  1.00 18.42 ?  33  TYR A OH  1 
ATOM   260  N  N   . GLY A 1 34  ? 28.484 20.248  52.991  1.00 22.44 ?  34  GLY A N   1 
ATOM   261  C  CA  . GLY A 1 34  ? 27.430 20.227  51.985  1.00 25.45 ?  34  GLY A CA  1 
ATOM   262  C  C   . GLY A 1 34  ? 27.861 19.616  50.670  1.00 26.16 ?  34  GLY A C   1 
ATOM   263  O  O   . GLY A 1 34  ? 27.486 20.121  49.603  1.00 32.17 ?  34  GLY A O   1 
ATOM   264  N  N   . LEU A 1 35  ? 28.650 18.546  50.720  1.00 24.73 ?  35  LEU A N   1 
ATOM   265  C  CA  . LEU A 1 35  ? 29.214 17.899  49.545  1.00 28.12 ?  35  LEU A CA  1 
ATOM   266  C  C   . LEU A 1 35  ? 28.546 16.551  49.331  1.00 23.08 ?  35  LEU A C   1 
ATOM   267  O  O   . LEU A 1 35  ? 27.957 15.976  50.250  1.00 26.22 ?  35  LEU A O   1 
ATOM   268  C  CB  . LEU A 1 35  ? 30.729 17.684  49.700  1.00 28.56 ?  35  LEU A CB  1 
ATOM   269  C  CG  . LEU A 1 35  ? 31.622 18.869  50.061  1.00 25.48 ?  35  LEU A CG  1 
ATOM   270  C  CD1 . LEU A 1 35  ? 33.038 18.379  50.380  1.00 32.50 ?  35  LEU A CD1 1 
ATOM   271  C  CD2 . LEU A 1 35  ? 31.632 19.879  48.932  1.00 31.10 ?  35  LEU A CD2 1 
ATOM   272  N  N   . LYS A 1 36  ? 28.666 16.038  48.109  1.00 27.72 ?  36  LYS A N   1 
ATOM   273  C  CA  . LYS A 1 36  ? 28.334 14.649  47.808  1.00 28.85 ?  36  LYS A CA  1 
ATOM   274  C  C   . LYS A 1 36  ? 29.573 13.972  47.240  1.00 27.17 ?  36  LYS A C   1 
ATOM   275  O  O   . LYS A 1 36  ? 30.149 14.442  46.250  1.00 29.46 ?  36  LYS A O   1 
ATOM   276  C  CB  . LYS A 1 36  ? 27.166 14.540  46.827  1.00 33.57 ?  36  LYS A CB  1 
ATOM   277  C  CG  . LYS A 1 36  ? 26.509 13.167  46.828  1.00 34.28 ?  36  LYS A CG  1 
ATOM   278  C  CD  . LYS A 1 36  ? 26.082 12.751  45.431  1.00 47.10 ?  36  LYS A CD  1 
ATOM   279  C  CE  . LYS A 1 36  ? 25.480 11.350  45.432  1.00 45.10 ?  36  LYS A CE  1 
ATOM   280  N  NZ  . LYS A 1 36  ? 25.147 10.909  44.055  1.00 42.17 ?  36  LYS A NZ  1 
ATOM   281  N  N   . GLY A 1 37  ? 29.980 12.876  47.866  1.00 25.15 ?  37  GLY A N   1 
ATOM   282  C  CA  . GLY A 1 37  ? 31.193 12.210  47.451  1.00 25.60 ?  37  GLY A CA  1 
ATOM   283  C  C   . GLY A 1 37  ? 30.991 11.378  46.202  1.00 25.84 ?  37  GLY A C   1 
ATOM   284  O  O   . GLY A 1 37  ? 29.890 10.929  45.888  1.00 24.78 ?  37  GLY A O   1 
ATOM   285  N  N   . HIS A 1 38  ? 32.075 11.205  45.459  1.00 23.19 ?  38  HIS A N   1 
ATOM   286  C  CA  . HIS A 1 38  ? 32.118 10.234  44.378  1.00 19.48 ?  38  HIS A CA  1 
ATOM   287  C  C   . HIS A 1 38  ? 32.720 8.956   44.958  1.00 26.20 ?  38  HIS A C   1 
ATOM   288  O  O   . HIS A 1 38  ? 33.901 8.934   45.313  1.00 23.29 ?  38  HIS A O   1 
ATOM   289  C  CB  . HIS A 1 38  ? 32.935 10.779  43.207  1.00 20.91 ?  38  HIS A CB  1 
ATOM   290  C  CG  . HIS A 1 38  ? 33.109 9.804   42.087  1.00 28.88 ?  38  HIS A CG  1 
ATOM   291  N  ND1 . HIS A 1 38  ? 32.211 8.789   41.837  1.00 40.04 ?  38  HIS A ND1 1 
ATOM   292  C  CD2 . HIS A 1 38  ? 34.090 9.676   41.162  1.00 32.69 ?  38  HIS A CD2 1 
ATOM   293  C  CE1 . HIS A 1 38  ? 32.626 8.082   40.801  1.00 31.11 ?  38  HIS A CE1 1 
ATOM   294  N  NE2 . HIS A 1 38  ? 33.767 8.596   40.376  1.00 31.66 ?  38  HIS A NE2 1 
ATOM   295  N  N   . TYR A 1 39  ? 31.901 7.910   45.100  1.00 23.95 ?  39  TYR A N   1 
ATOM   296  C  CA  . TYR A 1 39  ? 32.311 6.661   45.736  1.00 21.90 ?  39  TYR A CA  1 
ATOM   297  C  C   . TYR A 1 39  ? 32.739 5.657   44.676  1.00 24.66 ?  39  TYR A C   1 
ATOM   298  O  O   . TYR A 1 39  ? 32.024 5.448   43.688  1.00 22.63 ?  39  TYR A O   1 
ATOM   299  C  CB  . TYR A 1 39  ? 31.178 6.080   46.575  1.00 21.39 ?  39  TYR A CB  1 
ATOM   300  C  CG  . TYR A 1 39  ? 30.886 6.884   47.810  1.00 20.64 ?  39  TYR A CG  1 
ATOM   301  C  CD1 . TYR A 1 39  ? 30.180 8.081   47.735  1.00 26.79 ?  39  TYR A CD1 1 
ATOM   302  C  CD2 . TYR A 1 39  ? 31.327 6.458   49.054  1.00 21.51 ?  39  TYR A CD2 1 
ATOM   303  C  CE1 . TYR A 1 39  ? 29.922 8.828   48.874  1.00 24.14 ?  39  TYR A CE1 1 
ATOM   304  C  CE2 . TYR A 1 39  ? 31.076 7.194   50.181  1.00 21.00 ?  39  TYR A CE2 1 
ATOM   305  C  CZ  . TYR A 1 39  ? 30.368 8.375   50.090  1.00 22.76 ?  39  TYR A CZ  1 
ATOM   306  O  OH  . TYR A 1 39  ? 30.126 9.093   51.239  1.00 26.41 ?  39  TYR A OH  1 
ATOM   307  N  N   . VAL A 1 40  ? 33.889 5.021   44.895  1.00 20.24 ?  40  VAL A N   1 
ATOM   308  C  CA  . VAL A 1 40  ? 34.526 4.160   43.903  1.00 20.94 ?  40  VAL A CA  1 
ATOM   309  C  C   . VAL A 1 40  ? 34.846 2.804   44.534  1.00 22.20 ?  40  VAL A C   1 
ATOM   310  O  O   . VAL A 1 40  ? 35.447 2.739   45.612  1.00 21.68 ?  40  VAL A O   1 
ATOM   311  C  CB  . VAL A 1 40  ? 35.811 4.812   43.349  1.00 22.99 ?  40  VAL A CB  1 
ATOM   312  C  CG1 . VAL A 1 40  ? 36.639 3.792   42.614  1.00 28.17 ?  40  VAL A CG1 1 
ATOM   313  C  CG2 . VAL A 1 40  ? 35.466 5.997   42.444  1.00 27.24 ?  40  VAL A CG2 1 
ATOM   314  N  N   . GLY A 1 41  ? 34.436 1.724   43.873  1.00 22.78 ?  41  GLY A N   1 
ATOM   315  C  CA  . GLY A 1 41  ? 34.843 0.394   44.281  1.00 19.74 ?  41  GLY A CA  1 
ATOM   316  C  C   . GLY A 1 41  ? 33.802 -0.311  45.138  1.00 24.76 ?  41  GLY A C   1 
ATOM   317  O  O   . GLY A 1 41  ? 32.903 0.303   45.724  1.00 26.86 ?  41  GLY A O   1 
ATOM   318  N  N   . GLU A 1 42  ? 33.946 -1.638  45.222  1.00 26.64 ?  42  GLU A N   1 
ATOM   319  C  CA  . GLU A 1 42  ? 33.040 -2.495  45.973  1.00 29.58 ?  42  GLU A CA  1 
ATOM   320  C  C   . GLU A 1 42  ? 33.777 -3.152  47.135  1.00 22.58 ?  42  GLU A C   1 
ATOM   321  O  O   . GLU A 1 42  ? 34.878 -3.681  46.934  1.00 26.55 ?  42  GLU A O   1 
ATOM   322  C  CB  . GLU A 1 42  ? 32.444 -3.583  45.065  1.00 34.18 ?  42  GLU A CB  1 
ATOM   323  C  CG  . GLU A 1 42  ? 31.802 -3.037  43.798  1.00 39.83 ?  42  GLU A CG  1 
ATOM   324  C  CD  . GLU A 1 42  ? 30.579 -2.190  44.092  1.00 45.71 ?  42  GLU A CD  1 
ATOM   325  O  OE1 . GLU A 1 42  ? 29.844 -2.523  45.050  1.00 47.23 ?  42  GLU A OE1 1 
ATOM   326  O  OE2 . GLU A 1 42  ? 30.355 -1.191  43.370  1.00 47.83 -1 42  GLU A OE2 1 
ATOM   327  N  N   . PRO A 1 43  ? 33.211 -3.146  48.344  1.00 25.23 ?  43  PRO A N   1 
ATOM   328  C  CA  . PRO A 1 43  ? 33.920 -3.711  49.504  1.00 24.24 ?  43  PRO A CA  1 
ATOM   329  C  C   . PRO A 1 43  ? 34.163 -5.211  49.366  1.00 29.08 ?  43  PRO A C   1 
ATOM   330  O  O   . PRO A 1 43  ? 33.395 -5.937  48.730  1.00 29.71 ?  43  PRO A O   1 
ATOM   331  C  CB  . PRO A 1 43  ? 32.979 -3.406  50.677  1.00 26.00 ?  43  PRO A CB  1 
ATOM   332  C  CG  . PRO A 1 43  ? 32.166 -2.250  50.225  1.00 30.68 ?  43  PRO A CG  1 
ATOM   333  C  CD  . PRO A 1 43  ? 31.992 -2.424  48.742  1.00 26.67 ?  43  PRO A CD  1 
ATOM   334  N  N   . ALA A 1 44  ? 35.266 -5.663  49.961  1.00 25.70 ?  44  ALA A N   1 
ATOM   335  C  CA  . ALA A 1 44  ? 35.672 -7.063  49.992  1.00 23.93 ?  44  ALA A CA  1 
ATOM   336  C  C   . ALA A 1 44  ? 36.403 -7.282  51.304  1.00 24.84 ?  44  ALA A C   1 
ATOM   337  O  O   . ALA A 1 44  ? 36.985 -6.332  51.843  1.00 22.57 ?  44  ALA A O   1 
ATOM   338  C  CB  . ALA A 1 44  ? 36.572 -7.436  48.804  1.00 23.12 ?  44  ALA A CB  1 
ATOM   339  N  N   . PRO A 1 45  ? 36.381 -8.499  51.851  1.00 23.49 ?  45  PRO A N   1 
ATOM   340  C  CA  . PRO A 1 45  ? 36.954 -8.727  53.187  1.00 25.14 ?  45  PRO A CA  1 
ATOM   341  C  C   . PRO A 1 45  ? 38.467 -8.561  53.216  1.00 22.22 ?  45  PRO A C   1 
ATOM   342  O  O   . PRO A 1 45  ? 39.173 -8.741  52.221  1.00 20.48 ?  45  PRO A O   1 
ATOM   343  C  CB  . PRO A 1 45  ? 36.563 -10.178 53.505  1.00 30.35 ?  45  PRO A CB  1 
ATOM   344  C  CG  . PRO A 1 45  ? 35.468 -10.510 52.544  1.00 32.01 ?  45  PRO A CG  1 
ATOM   345  C  CD  . PRO A 1 45  ? 35.740 -9.713  51.313  1.00 24.70 ?  45  PRO A CD  1 
ATOM   346  N  N   . HIS A 1 46  ? 38.970 -8.234  54.404  1.00 22.66 ?  46  HIS A N   1 
ATOM   347  C  CA  . HIS A 1 46  ? 40.407 -8.093  54.551  1.00 20.02 ?  46  HIS A CA  1 
ATOM   348  C  C   . HIS A 1 46  ? 41.082 -9.466  54.497  1.00 24.24 ?  46  HIS A C   1 
ATOM   349  O  O   . HIS A 1 46  ? 40.457 -10.508 54.725  1.00 22.67 ?  46  HIS A O   1 
ATOM   350  C  CB  . HIS A 1 46  ? 40.746 -7.351  55.849  1.00 19.78 ?  46  HIS A CB  1 
ATOM   351  C  CG  . HIS A 1 46  ? 40.376 -8.087  57.102  1.00 24.83 ?  46  HIS A CG  1 
ATOM   352  N  ND1 . HIS A 1 46  ? 39.069 -8.285  57.490  1.00 23.69 ?  46  HIS A ND1 1 
ATOM   353  C  CD2 . HIS A 1 46  ? 41.143 -8.670  58.054  1.00 26.69 ?  46  HIS A CD2 1 
ATOM   354  C  CE1 . HIS A 1 46  ? 39.046 -8.949  58.633  1.00 26.25 ?  46  HIS A CE1 1 
ATOM   355  N  NE2 . HIS A 1 46  ? 40.290 -9.197  58.996  1.00 31.56 ?  46  HIS A NE2 1 
ATOM   356  N  N   . ALA A 1 47  ? 42.375 -9.456  54.175  1.00 19.27 ?  47  ALA A N   1 
ATOM   357  C  CA  . ALA A 1 47  ? 43.146 -10.680 54.009  1.00 22.26 ?  47  ALA A CA  1 
ATOM   358  C  C   . ALA A 1 47  ? 44.630 -10.358 54.117  1.00 23.85 ?  47  ALA A C   1 
ATOM   359  O  O   . ALA A 1 47  ? 45.062 -9.249  53.791  1.00 21.16 ?  47  ALA A O   1 
ATOM   360  C  CB  . ALA A 1 47  ? 42.837 -11.332 52.657  1.00 22.26 ?  47  ALA A CB  1 
ATOM   361  N  N   . ASP A 1 48  ? 45.411 -11.342 54.551  1.00 20.64 ?  48  ASP A N   1 
ATOM   362  C  CA  . ASP A 1 48  ? 46.863 -11.185 54.645  1.00 22.41 ?  48  ASP A CA  1 
ATOM   363  C  C   . ASP A 1 48  ? 47.548 -11.722 53.392  1.00 23.44 ?  48  ASP A C   1 
ATOM   364  O  O   . ASP A 1 48  ? 48.430 -12.580 53.463  1.00 26.20 ?  48  ASP A O   1 
ATOM   365  C  CB  . ASP A 1 48  ? 47.390 -11.897 55.880  1.00 28.03 ?  48  ASP A CB  1 
ATOM   366  C  CG  . ASP A 1 48  ? 46.949 -11.239 57.153  1.00 36.42 ?  48  ASP A CG  1 
ATOM   367  O  OD1 . ASP A 1 48  ? 46.933 -9.990  57.185  1.00 27.27 ?  48  ASP A OD1 1 
ATOM   368  O  OD2 . ASP A 1 48  ? 46.631 -11.971 58.119  1.00 42.18 -1 48  ASP A OD2 1 
ATOM   369  N  N   . ASP A 1 49  ? 47.146 -11.203 52.236  1.00 20.72 ?  49  ASP A N   1 
ATOM   370  C  CA  . ASP A 1 49  ? 47.693 -11.680 50.979  1.00 17.61 ?  49  ASP A CA  1 
ATOM   371  C  C   . ASP A 1 49  ? 48.940 -10.895 50.576  1.00 20.37 ?  49  ASP A C   1 
ATOM   372  O  O   . ASP A 1 49  ? 49.142 -9.744  50.976  1.00 17.68 ?  49  ASP A O   1 
ATOM   373  C  CB  . ASP A 1 49  ? 46.651 -11.631 49.856  1.00 20.33 ?  49  ASP A CB  1 
ATOM   374  C  CG  . ASP A 1 49  ? 45.849 -10.325 49.809  1.00 21.34 ?  49  ASP A CG  1 
ATOM   375  O  OD1 . ASP A 1 49  ? 46.102 -9.382  50.597  1.00 21.46 ?  49  ASP A OD1 1 
ATOM   376  O  OD2 . ASP A 1 49  ? 44.944 -10.249 48.942  1.00 19.65 -1 49  ASP A OD2 1 
ATOM   377  N  N   . ASP A 1 50  ? 49.797 -11.552 49.801  1.00 18.37 ?  50  ASP A N   1 
ATOM   378  C  CA  . ASP A 1 50  ? 50.993 -10.899 49.291  1.00 16.41 ?  50  ASP A CA  1 
ATOM   379  C  C   . ASP A 1 50  ? 50.620 -9.765  48.339  1.00 15.91 ?  50  ASP A C   1 
ATOM   380  O  O   . ASP A 1 50  ? 49.583 -9.805  47.673  1.00 17.00 ?  50  ASP A O   1 
ATOM   381  C  CB  . ASP A 1 50  ? 51.889 -11.907 48.563  1.00 20.82 ?  50  ASP A CB  1 
ATOM   382  C  CG  . ASP A 1 50  ? 53.240 -11.331 48.219  1.00 20.76 ?  50  ASP A CG  1 
ATOM   383  O  OD1 . ASP A 1 50  ? 54.023 -11.092 49.159  1.00 19.43 ?  50  ASP A OD1 1 
ATOM   384  O  OD2 . ASP A 1 50  ? 53.528 -11.118 47.015  1.00 19.84 -1 50  ASP A OD2 1 
ATOM   385  N  N   . TRP A 1 51  ? 51.481 -8.736  48.295  1.00 14.14 ?  51  TRP A N   1 
ATOM   386  C  CA  . TRP A 1 51  ? 51.243 -7.607  47.394  1.00 16.16 ?  51  TRP A CA  1 
ATOM   387  C  C   . TRP A 1 51  ? 51.036 -8.073  45.958  1.00 15.62 ?  51  TRP A C   1 
ATOM   388  O  O   . TRP A 1 51  ? 50.281 -7.452  45.204  1.00 14.29 ?  51  TRP A O   1 
ATOM   389  C  CB  . TRP A 1 51  ? 52.408 -6.602  47.468  1.00 16.42 ?  51  TRP A CB  1 
ATOM   390  C  CG  . TRP A 1 51  ? 53.685 -7.131  46.904  1.00 20.02 ?  51  TRP A CG  1 
ATOM   391  C  CD1 . TRP A 1 51  ? 54.699 -7.748  47.585  1.00 18.37 ?  51  TRP A CD1 1 
ATOM   392  C  CD2 . TRP A 1 51  ? 54.085 -7.094  45.532  1.00 16.44 ?  51  TRP A CD2 1 
ATOM   393  N  NE1 . TRP A 1 51  ? 55.700 -8.108  46.712  1.00 22.26 ?  51  TRP A NE1 1 
ATOM   394  C  CE2 . TRP A 1 51  ? 55.343 -7.715  45.445  1.00 19.82 ?  51  TRP A CE2 1 
ATOM   395  C  CE3 . TRP A 1 51  ? 53.486 -6.615  44.363  1.00 16.20 ?  51  TRP A CE3 1 
ATOM   396  C  CZ2 . TRP A 1 51  ? 56.013 -7.876  44.231  1.00 17.90 ?  51  TRP A CZ2 1 
ATOM   397  C  CZ3 . TRP A 1 51  ? 54.157 -6.759  43.165  1.00 19.79 ?  51  TRP A CZ3 1 
ATOM   398  C  CH2 . TRP A 1 51  ? 55.407 -7.381  43.109  1.00 21.48 ?  51  TRP A CH2 1 
ATOM   399  N  N   . SER A 1 52  ? 51.682 -9.176  45.566  1.00 18.34 ?  52  SER A N   1 
ATOM   400  C  CA  . SER A 1 52  ? 51.614 -9.605  44.174  1.00 17.36 ?  52  SER A CA  1 
ATOM   401  C  C   . SER A 1 52  ? 50.250 -10.184 43.837  1.00 16.85 ?  52  SER A C   1 
ATOM   402  O  O   . SER A 1 52  ? 49.899 -10.287 42.654  1.00 19.33 ?  52  SER A O   1 
ATOM   403  C  CB  . SER A 1 52  ? 52.723 -10.621 43.897  1.00 18.51 ?  52  SER A CB  1 
ATOM   404  O  OG  . SER A 1 52  ? 52.488 -11.843 44.596  1.00 20.31 ?  52  SER A OG  1 
ATOM   405  N  N   . VAL A 1 53  ? 49.481 -10.545 44.860  1.00 17.11 ?  53  VAL A N   1 
ATOM   406  C  CA  . VAL A 1 53  ? 48.100 -10.990 44.720  1.00 19.28 ?  53  VAL A CA  1 
ATOM   407  C  C   . VAL A 1 53  ? 47.124 -9.838  44.924  1.00 21.63 ?  53  VAL A C   1 
ATOM   408  O  O   . VAL A 1 53  ? 46.192 -9.659  44.142  1.00 18.21 ?  53  VAL A O   1 
ATOM   409  C  CB  . VAL A 1 53  ? 47.831 -12.142 45.722  1.00 20.94 ?  53  VAL A CB  1 
ATOM   410  C  CG1 . VAL A 1 53  ? 46.364 -12.548 45.733  1.00 21.27 ?  53  VAL A CG1 1 
ATOM   411  C  CG2 . VAL A 1 53  ? 48.710 -13.341 45.392  1.00 20.99 ?  53  VAL A CG2 1 
ATOM   412  N  N   . ALA A 1 54  ? 47.353 -9.024  45.958  1.00 17.73 ?  54  ALA A N   1 
ATOM   413  C  CA  . ALA A 1 54  ? 46.423 -7.945  46.295  1.00 15.18 ?  54  ALA A CA  1 
ATOM   414  C  C   . ALA A 1 54  ? 46.395 -6.855  45.223  1.00 13.95 ?  54  ALA A C   1 
ATOM   415  O  O   . ALA A 1 54  ? 45.332 -6.304  44.922  1.00 16.99 ?  54  ALA A O   1 
ATOM   416  C  CB  . ALA A 1 54  ? 46.813 -7.341  47.646  1.00 15.86 ?  54  ALA A CB  1 
ATOM   417  N  N   . LEU A 1 55  ? 47.553 -6.508  44.667  1.00 13.33 ?  55  LEU A N   1 
ATOM   418  C  CA  . LEU A 1 55  ? 47.624 -5.445  43.664  1.00 14.89 ?  55  LEU A CA  1 
ATOM   419  C  C   . LEU A 1 55  ? 46.751 -5.729  42.445  1.00 17.88 ?  55  LEU A C   1 
ATOM   420  O  O   . LEU A 1 55  ? 45.927 -4.866  42.090  1.00 14.09 ?  55  LEU A O   1 
ATOM   421  C  CB  . LEU A 1 55  ? 49.095 -5.210  43.293  1.00 18.41 ?  55  LEU A CB  1 
ATOM   422  C  CG  . LEU A 1 55  ? 49.460 -4.122  42.290  1.00 19.58 ?  55  LEU A CG  1 
ATOM   423  C  CD1 . LEU A 1 55  ? 48.919 -2.804  42.777  1.00 16.76 ?  55  LEU A CD1 1 
ATOM   424  C  CD2 . LEU A 1 55  ? 50.979 -4.050  42.128  1.00 22.32 ?  55  LEU A CD2 1 
ATOM   425  N  N   . PRO A 1 56  ? 46.836 -6.893  41.787  1.00 17.31 ?  56  PRO A N   1 
ATOM   426  C  CA  . PRO A 1 56  ? 45.910 -7.148  40.665  1.00 16.37 ?  56  PRO A CA  1 
ATOM   427  C  C   . PRO A 1 56  ? 44.451 -7.195  41.079  1.00 14.15 ?  56  PRO A C   1 
ATOM   428  O  O   . PRO A 1 56  ? 43.576 -6.760  40.316  1.00 15.23 ?  56  PRO A O   1 
ATOM   429  C  CB  . PRO A 1 56  ? 46.374 -8.507  40.112  1.00 19.59 ?  56  PRO A CB  1 
ATOM   430  C  CG  . PRO A 1 56  ? 47.703 -8.780  40.719  1.00 20.98 ?  56  PRO A CG  1 
ATOM   431  C  CD  . PRO A 1 56  ? 47.807 -7.991  41.973  1.00 19.33 ?  56  PRO A CD  1 
ATOM   432  N  N   . GLN A 1 57  ? 44.156 -7.709  42.276  1.00 18.60 ?  57  GLN A N   1 
ATOM   433  C  CA  . GLN A 1 57  ? 42.778 -7.702  42.748  1.00 17.11 ?  57  GLN A CA  1 
ATOM   434  C  C   . GLN A 1 57  ? 42.216 -6.292  42.806  1.00 17.85 ?  57  GLN A C   1 
ATOM   435  O  O   . GLN A 1 57  ? 41.024 -6.096  42.554  1.00 16.40 ?  57  GLN A O   1 
ATOM   436  C  CB  . GLN A 1 57  ? 42.687 -8.362  44.126  1.00 18.59 ?  57  GLN A CB  1 
ATOM   437  C  CG  . GLN A 1 57  ? 42.916 -9.872  44.071  1.00 20.14 ?  57  GLN A CG  1 
ATOM   438  C  CD  . GLN A 1 57  ? 42.728 -10.566 45.421  1.00 30.33 ?  57  GLN A CD  1 
ATOM   439  O  OE1 . GLN A 1 57  ? 42.355 -9.941  46.419  1.00 32.36 ?  57  GLN A OE1 1 
ATOM   440  N  NE2 . GLN A 1 57  ? 43.005 -11.864 45.452  1.00 27.51 ?  57  GLN A NE2 1 
ATOM   441  N  N   . ALA A 1 58  ? 43.056 -5.303  43.140  1.00 14.58 ?  58  ALA A N   1 
ATOM   442  C  CA  . ALA A 1 58  ? 42.624 -3.922  43.317  1.00 14.77 ?  58  ALA A CA  1 
ATOM   443  C  C   . ALA A 1 58  ? 42.624 -3.116  42.021  1.00 15.35 ?  58  ALA A C   1 
ATOM   444  O  O   . ALA A 1 58  ? 42.347 -1.913  42.055  1.00 16.76 ?  58  ALA A O   1 
ATOM   445  C  CB  . ALA A 1 58  ? 43.534 -3.222  44.340  1.00 14.41 ?  58  ALA A CB  1 
ATOM   446  N  N   . ARG A 1 59  ? 42.931 -3.742  40.882  1.00 16.37 ?  59  ARG A N   1 
ATOM   447  C  CA  . ARG A 1 59  ? 43.154 -2.984  39.651  1.00 18.38 ?  59  ARG A CA  1 
ATOM   448  C  C   . ARG A 1 59  ? 41.938 -2.156  39.257  1.00 16.64 ?  59  ARG A C   1 
ATOM   449  O  O   . ARG A 1 59  ? 42.072 -0.988  38.870  1.00 16.17 ?  59  ARG A O   1 
ATOM   450  C  CB  . ARG A 1 59  ? 43.528 -3.945  38.520  1.00 16.78 ?  59  ARG A CB  1 
ATOM   451  C  CG  . ARG A 1 59  ? 43.792 -3.282  37.173  1.00 18.27 ?  59  ARG A CG  1 
ATOM   452  C  CD  . ARG A 1 59  ? 45.247 -2.865  37.019  1.00 24.50 ?  59  ARG A CD  1 
ATOM   453  N  NE  . ARG A 1 59  ? 45.427 -2.040  35.826  1.00 21.43 ?  59  ARG A NE  1 
ATOM   454  C  CZ  . ARG A 1 59  ? 46.541 -1.386  35.536  1.00 21.87 ?  59  ARG A CZ  1 
ATOM   455  N  NH1 . ARG A 1 59  ? 47.593 -1.475  36.340  1.00 20.02 ?  59  ARG A NH1 1 
ATOM   456  N  NH2 . ARG A 1 59  ? 46.608 -0.660  34.432  1.00 28.17 ?  59  ARG A NH2 1 
ATOM   457  N  N   . GLU A 1 60  ? 40.741 -2.743  39.324  1.00 15.18 ?  60  GLU A N   1 
ATOM   458  C  CA  . GLU A 1 60  ? 39.567 -2.000  38.877  1.00 20.82 ?  60  GLU A CA  1 
ATOM   459  C  C   . GLU A 1 60  ? 39.318 -0.786  39.770  1.00 18.98 ?  60  GLU A C   1 
ATOM   460  O  O   . GLU A 1 60  ? 39.067 0.322   39.275  1.00 18.39 ?  60  GLU A O   1 
ATOM   461  C  CB  . GLU A 1 60  ? 38.344 -2.933  38.821  1.00 22.86 ?  60  GLU A CB  1 
ATOM   462  C  CG  . GLU A 1 60  ? 37.034 -2.245  38.455  1.00 31.77 ?  60  GLU A CG  1 
ATOM   463  C  CD  . GLU A 1 60  ? 35.857 -3.209  38.338  1.00 43.78 ?  60  GLU A CD  1 
ATOM   464  O  OE1 . GLU A 1 60  ? 34.838 -2.843  37.704  1.00 47.66 ?  60  GLU A OE1 1 
ATOM   465  O  OE2 . GLU A 1 60  ? 35.954 -4.343  38.867  1.00 46.49 -1 60  GLU A OE2 1 
ATOM   466  N  N   . THR A 1 61  ? 39.444 -0.958  41.086  1.00 15.96 ?  61  THR A N   1 
ATOM   467  C  CA  . THR A 1 61  ? 39.286 0.171   42.002  1.00 13.41 ?  61  THR A CA  1 
ATOM   468  C  C   . THR A 1 61  ? 40.353 1.230   41.760  1.00 12.77 ?  61  THR A C   1 
ATOM   469  O  O   . THR A 1 61  ? 40.053 2.433   41.736  1.00 17.42 ?  61  THR A O   1 
ATOM   470  C  CB  . THR A 1 61  ? 39.320 -0.319  43.449  1.00 18.03 ?  61  THR A CB  1 
ATOM   471  O  OG1 . THR A 1 61  ? 38.197 -1.186  43.656  1.00 17.02 ?  61  THR A OG1 1 
ATOM   472  C  CG2 . THR A 1 61  ? 39.216 0.861   44.431  1.00 16.63 ?  61  THR A CG2 1 
ATOM   473  N  N   . LEU A 1 62  ? 41.602 0.809   41.576  1.00 13.62 ?  62  LEU A N   1 
ATOM   474  C  CA  . LEU A 1 62  ? 42.692 1.769   41.411  1.00 15.56 ?  62  LEU A CA  1 
ATOM   475  C  C   . LEU A 1 62  ? 42.556 2.565   40.122  1.00 15.94 ?  62  LEU A C   1 
ATOM   476  O  O   . LEU A 1 62  ? 42.880 3.761   40.085  1.00 15.07 ?  62  LEU A O   1 
ATOM   477  C  CB  . LEU A 1 62  ? 44.037 1.048   41.435  1.00 14.71 ?  62  LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 62  ? 44.417 0.573   42.839  1.00 12.66 ?  62  LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 62  ? 45.696 -0.311  42.857  1.00 13.86 ?  62  LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 62  ? 44.569 1.794   43.802  1.00 12.95 ?  62  LEU A CD2 1 
ATOM   481  N  N   . VAL A 1 63  ? 42.140 1.908   39.037  1.00 13.87 ?  63  VAL A N   1 
ATOM   482  C  CA  . VAL A 1 63  ? 41.951 2.631   37.783  1.00 15.21 ?  63  VAL A CA  1 
ATOM   483  C  C   . VAL A 1 63  ? 40.810 3.634   37.912  1.00 16.86 ?  63  VAL A C   1 
ATOM   484  O  O   . VAL A 1 63  ? 40.892 4.760   37.402  1.00 21.17 ?  63  VAL A O   1 
ATOM   485  C  CB  . VAL A 1 63  ? 41.720 1.634   36.629  1.00 18.79 ?  63  VAL A CB  1 
ATOM   486  C  CG1 . VAL A 1 63  ? 41.154 2.350   35.409  1.00 25.03 ?  63  VAL A CG1 1 
ATOM   487  C  CG2 . VAL A 1 63  ? 43.026 0.922   36.299  1.00 17.74 ?  63  VAL A CG2 1 
ATOM   488  N  N   . ALA A 1 64  ? 39.743 3.251   38.607  1.00 16.20 ?  64  ALA A N   1 
ATOM   489  C  CA  . ALA A 1 64  ? 38.612 4.148   38.790  1.00 19.16 ?  64  ALA A CA  1 
ATOM   490  C  C   . ALA A 1 64  ? 38.966 5.342   39.673  1.00 19.21 ?  64  ALA A C   1 
ATOM   491  O  O   . ALA A 1 64  ? 38.487 6.452   39.434  1.00 17.34 ?  64  ALA A O   1 
ATOM   492  C  CB  . ALA A 1 64  ? 37.438 3.371   39.366  1.00 21.47 ?  64  ALA A CB  1 
ATOM   493  N  N   . VAL A 1 65  ? 39.779 5.137   40.713  1.00 16.44 ?  65  VAL A N   1 
ATOM   494  C  CA  . VAL A 1 65  ? 40.241 6.275   41.508  1.00 17.67 ?  65  VAL A CA  1 
ATOM   495  C  C   . VAL A 1 65  ? 41.146 7.180   40.679  1.00 18.40 ?  65  VAL A C   1 
ATOM   496  O  O   . VAL A 1 65  ? 41.074 8.413   40.777  1.00 18.85 ?  65  VAL A O   1 
ATOM   497  C  CB  . VAL A 1 65  ? 40.964 5.802   42.781  1.00 15.77 ?  65  VAL A CB  1 
ATOM   498  C  CG1 . VAL A 1 65  ? 41.616 7.008   43.457  1.00 16.42 ?  65  VAL A CG1 1 
ATOM   499  C  CG2 . VAL A 1 65  ? 40.010 5.149   43.734  1.00 16.87 ?  65  VAL A CG2 1 
ATOM   500  N  N   . ARG A 1 66  ? 42.017 6.588   39.859  1.00 16.98 ?  66  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 66  ? 42.904 7.389   39.028  1.00 17.74 ?  66  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 66  ? 42.111 8.292   38.095  1.00 19.91 ?  66  ARG A C   1 
ATOM   503  O  O   . ARG A 1 66  ? 42.417 9.485   37.954  1.00 18.84 ?  66  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 66  ? 43.838 6.479   38.232  1.00 21.23 ?  66  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 66  ? 44.761 7.246   37.309  1.00 25.41 ?  66  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 66  ? 45.304 6.335   36.240  1.00 30.68 ?  66  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 66  ? 44.301 6.074   35.214  1.00 37.67 ?  66  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 66  ? 44.166 4.911   34.585  1.00 40.42 ?  66  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 66  ? 44.975 3.905   34.887  1.00 33.33 ?  66  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 66  ? 43.225 4.758   33.655  1.00 39.04 ?  66  ARG A NH2 1 
ATOM   511  N  N   . GLU A 1 67  ? 41.062 7.752   37.483  1.00 19.88 ?  67  GLU A N   1 
ATOM   512  C  CA  . GLU A 1 67  ? 40.297 8.562   36.546  1.00 22.10 ?  67  GLU A CA  1 
ATOM   513  C  C   . GLU A 1 67  ? 39.538 9.674   37.270  1.00 22.70 ?  67  GLU A C   1 
ATOM   514  O  O   . GLU A 1 67  ? 39.497 10.812  36.784  1.00 21.21 ?  67  GLU A O   1 
ATOM   515  C  CB  . GLU A 1 67  ? 39.365 7.662   35.733  1.00 27.77 ?  67  GLU A CB  1 
ATOM   516  C  CG  . GLU A 1 67  ? 40.124 6.930   34.601  1.00 28.69 ?  67  GLU A CG  1 
ATOM   517  C  CD  . GLU A 1 67  ? 41.233 7.801   33.987  1.00 43.11 ?  67  GLU A CD  1 
ATOM   518  O  OE1 . GLU A 1 67  ? 42.425 7.591   34.322  1.00 45.51 ?  67  GLU A OE1 1 
ATOM   519  O  OE2 . GLU A 1 67  ? 40.910 8.714   33.185  1.00 46.00 -1 67  GLU A OE2 1 
ATOM   520  N  N   . ALA A 1 68  ? 38.975 9.389   38.453  1.00 18.59 ?  68  ALA A N   1 
ATOM   521  C  CA  . ALA A 1 68  ? 38.280 10.437  39.201  1.00 17.65 ?  68  ALA A CA  1 
ATOM   522  C  C   . ALA A 1 68  ? 39.250 11.505  39.694  1.00 21.84 ?  68  ALA A C   1 
ATOM   523  O  O   . ALA A 1 68  ? 38.943 12.705  39.652  1.00 18.35 ?  68  ALA A O   1 
ATOM   524  C  CB  . ALA A 1 68  ? 37.508 9.834   40.370  1.00 21.98 ?  68  ALA A CB  1 
ATOM   525  N  N   . ALA A 1 69  ? 40.416 11.090  40.193  1.00 18.98 ?  69  ALA A N   1 
ATOM   526  C  CA  . ALA A 1 69  ? 41.390 12.063  40.669  1.00 19.43 ?  69  ALA A CA  1 
ATOM   527  C  C   . ALA A 1 69  ? 41.930 12.909  39.522  1.00 20.93 ?  69  ALA A C   1 
ATOM   528  O  O   . ALA A 1 69  ? 42.190 14.103  39.699  1.00 23.37 ?  69  ALA A O   1 
ATOM   529  C  CB  . ALA A 1 69  ? 42.535 11.345  41.404  1.00 18.06 ?  69  ALA A CB  1 
ATOM   530  N  N   . THR A 1 70  ? 42.098 12.309  38.335  1.00 19.02 ?  70  THR A N   1 
ATOM   531  C  CA  . THR A 1 70  ? 42.568 13.063  37.182  1.00 23.47 ?  70  THR A CA  1 
ATOM   532  C  C   . THR A 1 70  ? 41.592 14.172  36.817  1.00 21.23 ?  70  THR A C   1 
ATOM   533  O  O   . THR A 1 70  ? 42.005 15.297  36.544  1.00 23.21 ?  70  THR A O   1 
ATOM   534  C  CB  . THR A 1 70  ? 42.778 12.136  35.986  1.00 22.69 ?  70  THR A CB  1 
ATOM   535  O  OG1 . THR A 1 70  ? 43.750 11.141  36.325  1.00 22.89 ?  70  THR A OG1 1 
ATOM   536  C  CG2 . THR A 1 70  ? 43.282 12.944  34.787  1.00 26.73 ?  70  THR A CG2 1 
ATOM   537  N  N   . GLU A 1 71  ? 40.294 13.878  36.828  1.00 21.42 ?  71  GLU A N   1 
ATOM   538  C  CA  . GLU A 1 71  ? 39.305 14.905  36.514  1.00 21.24 ?  71  GLU A CA  1 
ATOM   539  C  C   . GLU A 1 71  ? 39.338 16.028  37.539  1.00 24.66 ?  71  GLU A C   1 
ATOM   540  O  O   . GLU A 1 71  ? 39.311 17.215  37.183  1.00 22.52 ?  71  GLU A O   1 
ATOM   541  C  CB  . GLU A 1 71  ? 37.912 14.285  36.443  1.00 24.28 ?  71  GLU A CB  1 
ATOM   542  C  CG  . GLU A 1 71  ? 37.773 13.327  35.268  1.00 25.38 ?  71  GLU A CG  1 
ATOM   543  C  CD  . GLU A 1 71  ? 36.340 13.056  34.888  1.00 33.36 ?  71  GLU A CD  1 
ATOM   544  O  OE1 . GLU A 1 71  ? 35.434 13.356  35.703  1.00 37.23 ?  71  GLU A OE1 1 
ATOM   545  O  OE2 . GLU A 1 71  ? 36.120 12.555  33.760  1.00 40.12 -1 71  GLU A OE2 1 
ATOM   546  N  N   . SER A 1 72  ? 39.392 15.669  38.822  1.00 19.74 ?  72  SER A N   1 
ATOM   547  C  CA  . SER A 1 72  ? 39.423 16.690  39.869  1.00 22.91 ?  72  SER A CA  1 
ATOM   548  C  C   . SER A 1 72  ? 40.673 17.556  39.755  1.00 24.16 ?  72  SER A C   1 
ATOM   549  O  O   . SER A 1 72  ? 40.598 18.790  39.812  1.00 23.39 ?  72  SER A O   1 
ATOM   550  C  CB  . SER A 1 72  ? 39.351 16.023  41.243  1.00 23.52 ?  72  SER A CB  1 
ATOM   551  O  OG  . SER A 1 72  ? 39.326 16.994  42.275  1.00 21.84 ?  72  SER A OG  1 
ATOM   552  N  N   . ILE A 1 73  ? 41.835 16.921  39.584  1.00 21.27 ?  73  ILE A N   1 
ATOM   553  C  CA  . ILE A 1 73  ? 43.111 17.634  39.600  1.00 25.33 ?  73  ILE A CA  1 
ATOM   554  C  C   . ILE A 1 73  ? 43.223 18.580  38.409  1.00 30.24 ?  73  ILE A C   1 
ATOM   555  O  O   . ILE A 1 73  ? 43.817 19.663  38.513  1.00 29.70 ?  73  ILE A O   1 
ATOM   556  C  CB  . ILE A 1 73  ? 44.268 16.610  39.645  1.00 25.49 ?  73  ILE A CB  1 
ATOM   557  C  CG1 . ILE A 1 73  ? 44.419 16.046  41.061  1.00 24.44 ?  73  ILE A CG1 1 
ATOM   558  C  CG2 . ILE A 1 73  ? 45.585 17.241  39.233  1.00 29.31 ?  73  ILE A CG2 1 
ATOM   559  C  CD1 . ILE A 1 73  ? 45.196 14.747  41.148  1.00 27.56 ?  73  ILE A CD1 1 
ATOM   560  N  N   . LYS A 1 74  ? 42.624 18.221  37.274  1.00 29.22 ?  74  LYS A N   1 
ATOM   561  C  CA  . LYS A 1 74  ? 42.696 19.074  36.099  1.00 32.69 ?  74  LYS A CA  1 
ATOM   562  C  C   . LYS A 1 74  ? 41.788 20.296  36.198  1.00 28.96 ?  74  LYS A C   1 
ATOM   563  O  O   . LYS A 1 74  ? 42.053 21.295  35.520  1.00 34.53 ?  74  LYS A O   1 
ATOM   564  C  CB  . LYS A 1 74  ? 42.395 18.248  34.843  1.00 36.53 ?  74  LYS A CB  1 
ATOM   565  C  CG  . LYS A 1 74  ? 43.365 17.078  34.674  1.00 39.11 ?  74  LYS A CG  1 
ATOM   566  C  CD  . LYS A 1 74  ? 43.791 16.924  33.223  1.00 48.03 ?  74  LYS A CD  1 
ATOM   567  C  CE  . LYS A 1 74  ? 45.030 17.759  32.930  1.00 44.99 ?  74  LYS A CE  1 
ATOM   568  N  NZ  . LYS A 1 74  ? 45.002 18.371  31.574  1.00 48.46 ?  74  LYS A NZ  1 
ATOM   569  N  N   . GLY A 1 75  ? 40.767 20.263  37.056  1.00 27.94 ?  75  GLY A N   1 
ATOM   570  C  CA  . GLY A 1 75  ? 39.957 21.428  37.357  1.00 30.83 ?  75  GLY A CA  1 
ATOM   571  C  C   . GLY A 1 75  ? 40.628 22.354  38.356  1.00 35.74 ?  75  GLY A C   1 
ATOM   572  O  O   . GLY A 1 75  ? 41.846 22.335  38.544  1.00 33.64 ?  75  GLY A O   1 
ATOM   573  N  N   . ASP A 1 76  ? 39.821 23.178  39.015  1.00 31.82 ?  76  ASP A N   1 
ATOM   574  C  CA  . ASP A 1 76  ? 40.393 24.170  39.918  1.00 40.14 ?  76  ASP A CA  1 
ATOM   575  C  C   . ASP A 1 76  ? 39.797 24.069  41.314  1.00 39.78 ?  76  ASP A C   1 
ATOM   576  O  O   . ASP A 1 76  ? 39.616 25.071  42.011  1.00 41.48 ?  76  ASP A O   1 
ATOM   577  C  CB  . ASP A 1 76  ? 40.228 25.579  39.358  1.00 48.61 ?  76  ASP A CB  1 
ATOM   578  C  CG  . ASP A 1 76  ? 41.549 26.185  38.926  1.00 54.26 ?  76  ASP A CG  1 
ATOM   579  O  OD1 . ASP A 1 76  ? 41.544 27.318  38.400  1.00 63.57 -1 76  ASP A OD1 1 
ATOM   580  O  OD2 . ASP A 1 76  ? 42.595 25.525  39.117  1.00 59.74 -1 76  ASP A OD2 1 
ATOM   581  N  N   . ASN A 1 77  ? 39.503 22.859  41.764  1.00 33.97 ?  77  ASN A N   1 
ATOM   582  C  CA  . ASN A 1 77  ? 39.008 22.659  43.116  1.00 30.81 ?  77  ASN A CA  1 
ATOM   583  C  C   . ASN A 1 77  ? 40.077 21.972  43.957  1.00 28.92 ?  77  ASN A C   1 
ATOM   584  O  O   . ASN A 1 77  ? 41.103 21.509  43.452  1.00 29.51 ?  77  ASN A O   1 
ATOM   585  C  CB  . ASN A 1 77  ? 37.705 21.852  43.095  1.00 36.22 ?  77  ASN A CB  1 
ATOM   586  C  CG  . ASN A 1 77  ? 36.665 22.460  42.170  1.00 39.68 ?  77  ASN A CG  1 
ATOM   587  O  OD1 . ASN A 1 77  ? 36.577 23.683  42.040  1.00 39.04 ?  77  ASN A OD1 1 
ATOM   588  N  ND2 . ASN A 1 77  ? 35.876 21.611  41.517  1.00 43.36 ?  77  ASN A ND2 1 
ATOM   589  N  N   . LEU A 1 78  ? 39.853 21.956  45.269  1.00 20.78 ?  78  LEU A N   1 
ATOM   590  C  CA  . LEU A 1 78  ? 40.685 21.158  46.161  1.00 21.11 ?  78  LEU A CA  1 
ATOM   591  C  C   . LEU A 1 78  ? 40.261 19.702  46.032  1.00 23.02 ?  78  LEU A C   1 
ATOM   592  O  O   . LEU A 1 78  ? 39.103 19.368  46.303  1.00 21.89 ?  78  LEU A O   1 
ATOM   593  C  CB  . LEU A 1 78  ? 40.544 21.627  47.608  1.00 23.71 ?  78  LEU A CB  1 
ATOM   594  C  CG  . LEU A 1 78  ? 41.323 20.801  48.644  1.00 17.12 ?  78  LEU A CG  1 
ATOM   595  C  CD1 . LEU A 1 78  ? 42.793 21.092  48.450  1.00 18.26 ?  78  LEU A CD1 1 
ATOM   596  C  CD2 . LEU A 1 78  ? 40.860 21.120  50.040  1.00 19.75 ?  78  LEU A CD2 1 
ATOM   597  N  N   . THR A 1 79  ? 41.195 18.838  45.628  1.00 17.27 ?  79  THR A N   1 
ATOM   598  C  CA  . THR A 1 79  ? 40.914 17.413  45.500  1.00 16.54 ?  79  THR A CA  1 
ATOM   599  C  C   . THR A 1 79  ? 41.084 16.764  46.867  1.00 18.37 ?  79  THR A C   1 
ATOM   600  O  O   . THR A 1 79  ? 42.164 16.843  47.451  1.00 16.13 ?  79  THR A O   1 
ATOM   601  C  CB  . THR A 1 79  ? 41.871 16.780  44.493  1.00 18.69 ?  79  THR A CB  1 
ATOM   602  O  OG1 . THR A 1 79  ? 41.748 17.445  43.234  1.00 21.13 ?  79  THR A OG1 1 
ATOM   603  C  CG2 . THR A 1 79  ? 41.599 15.275  44.330  1.00 18.88 ?  79  THR A CG2 1 
ATOM   604  N  N   . VAL A 1 80  ? 40.027 16.148  47.388  1.00 16.02 ?  80  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 80  ? 40.075 15.467  48.679  1.00 14.26 ?  80  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 80  ? 39.725 14.008  48.441  1.00 17.52 ?  80  VAL A C   1 
ATOM   607  O  O   . VAL A 1 80  ? 38.638 13.698  47.948  1.00 15.80 ?  80  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 80  ? 39.118 16.100  49.700  1.00 15.60 ?  80  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 80  ? 39.070 15.263  50.997  1.00 17.81 ?  80  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 80  ? 39.568 17.513  50.004  1.00 17.13 ?  80  VAL A CG2 1 
ATOM   611  N  N   . LEU A 1 81  ? 40.654 13.119  48.760  1.00 13.00 ?  81  LEU A N   1 
ATOM   612  C  CA  . LEU A 1 81  ? 40.413 11.687  48.686  1.00 13.54 ?  81  LEU A CA  1 
ATOM   613  C  C   . LEU A 1 81  ? 40.322 11.130  50.099  1.00 14.21 ?  81  LEU A C   1 
ATOM   614  O  O   . LEU A 1 81  ? 41.221 11.347  50.914  1.00 15.64 ?  81  LEU A O   1 
ATOM   615  C  CB  . LEU A 1 81  ? 41.532 10.981  47.910  1.00 14.04 ?  81  LEU A CB  1 
ATOM   616  C  CG  . LEU A 1 81  ? 41.513 11.307  46.420  1.00 16.52 ?  81  LEU A CG  1 
ATOM   617  C  CD1 . LEU A 1 81  ? 42.784 11.989  46.014  1.00 19.11 ?  81  LEU A CD1 1 
ATOM   618  C  CD2 . LEU A 1 81  ? 41.273 10.055  45.567  1.00 19.71 ?  81  LEU A CD2 1 
ATOM   619  N  N   . VAL A 1 82  ? 39.246 10.404  50.382  1.00 13.97 ?  82  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 82  ? 39.108 9.677   51.635  1.00 11.61 ?  82  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 82  ? 39.289 8.210   51.286  1.00 14.23 ?  82  VAL A C   1 
ATOM   622  O  O   . VAL A 1 82  ? 38.429 7.620   50.622  1.00 13.20 ?  82  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 82  ? 37.755 9.936   52.308  1.00 14.27 ?  82  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 82  ? 37.663 9.138   53.614  1.00 15.44 ?  82  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 82  ? 37.585 11.442  52.598  1.00 17.23 ?  82  VAL A CG2 1 
ATOM   626  N  N   . ASN A 1 83  ? 40.404 7.618   51.720  1.00 13.40 ?  83  ASN A N   1 
ATOM   627  C  CA  . ASN A 1 83  ? 40.844 6.333   51.187  1.00 12.15 ?  83  ASN A CA  1 
ATOM   628  C  C   . ASN A 1 83  ? 40.856 5.289   52.289  1.00 12.49 ?  83  ASN A C   1 
ATOM   629  O  O   . ASN A 1 83  ? 41.236 5.583   53.422  1.00 14.71 ?  83  ASN A O   1 
ATOM   630  C  CB  . ASN A 1 83  ? 42.240 6.453   50.560  1.00 14.81 ?  83  ASN A CB  1 
ATOM   631  C  CG  . ASN A 1 83  ? 42.247 7.334   49.319  1.00 13.22 ?  83  ASN A CG  1 
ATOM   632  O  OD1 . ASN A 1 83  ? 41.255 7.418   48.607  1.00 16.71 ?  83  ASN A OD1 1 
ATOM   633  N  ND2 . ASN A 1 83  ? 43.380 7.961   49.046  1.00 16.50 ?  83  ASN A ND2 1 
ATOM   634  N  N   . ASN A 1 84  ? 40.491 4.049   51.955  1.00 11.82 ?  84  ASN A N   1 
ATOM   635  C  CA  . ASN A 1 84  ? 40.550 3.020   52.983  1.00 12.83 ?  84  ASN A CA  1 
ATOM   636  C  C   . ASN A 1 84  ? 41.997 2.759   53.387  1.00 12.89 ?  84  ASN A C   1 
ATOM   637  O  O   . ASN A 1 84  ? 42.313 2.741   54.580  1.00 15.64 ?  84  ASN A O   1 
ATOM   638  C  CB  . ASN A 1 84  ? 39.823 1.731   52.531  1.00 14.80 ?  84  ASN A CB  1 
ATOM   639  C  CG  . ASN A 1 84  ? 40.143 1.320   51.097  1.00 16.85 ?  84  ASN A CG  1 
ATOM   640  O  OD1 . ASN A 1 84  ? 40.118 2.136   50.174  1.00 18.02 ?  84  ASN A OD1 1 
ATOM   641  N  ND2 . ASN A 1 84  ? 40.421 0.019   50.903  1.00 15.97 ?  84  ASN A ND2 1 
ATOM   642  N  N   . THR A 1 85  ? 42.903 2.603   52.409  1.00 12.98 ?  85  THR A N   1 
ATOM   643  C  CA  . THR A 1 85  ? 44.310 2.334   52.691  1.00 12.82 ?  85  THR A CA  1 
ATOM   644  C  C   . THR A 1 85  ? 45.229 3.311   51.971  1.00 10.13 ?  85  THR A C   1 
ATOM   645  O  O   . THR A 1 85  ? 44.862 3.949   50.982  1.00 12.05 ?  85  THR A O   1 
ATOM   646  C  CB  . THR A 1 85  ? 44.748 0.918   52.265  1.00 15.14 ?  85  THR A CB  1 
ATOM   647  O  OG1 . THR A 1 85  ? 44.545 0.756   50.857  1.00 15.41 ?  85  THR A OG1 1 
ATOM   648  C  CG2 . THR A 1 85  ? 43.965 -0.159  53.005  1.00 15.05 ?  85  THR A CG2 1 
ATOM   649  N  N   . CYS A 1 86  ? 46.461 3.391   52.478  1.00 11.34 ?  86  CYS A N   1 
ATOM   650  C  CA  . CYS A 1 86  ? 47.484 4.193   51.811  1.00 12.11 ?  86  CYS A CA  1 
ATOM   651  C  C   . CYS A 1 86  ? 47.729 3.707   50.384  1.00 10.11 ?  86  CYS A C   1 
ATOM   652  O  O   . CYS A 1 86  ? 48.145 4.494   49.520  1.00 10.99 ?  86  CYS A O   1 
ATOM   653  C  CB  . CYS A 1 86  ? 48.796 4.133   52.605  1.00 11.14 ?  86  CYS A CB  1 
ATOM   654  S  SG  . CYS A 1 86  ? 48.781 5.191   54.118  1.00 11.89 ?  86  CYS A SG  1 
ATOM   655  N  N   . SER A 1 87  ? 47.469 2.419   50.119  1.00 12.82 ?  87  SER A N   1 
ATOM   656  C  CA  . SER A 1 87  ? 47.763 1.842   48.815  1.00 12.60 ?  87  SER A CA  1 
ATOM   657  C  C   . SER A 1 87  ? 46.966 2.492   47.701  1.00 12.25 ?  87  SER A C   1 
ATOM   658  O  O   . SER A 1 87  ? 47.372 2.403   46.543  1.00 11.91 ?  87  SER A O   1 
ATOM   659  C  CB  . SER A 1 87  ? 47.469 0.346   48.830  1.00 13.27 ?  87  SER A CB  1 
ATOM   660  O  OG  . SER A 1 87  ? 48.347 -0.286  49.742  1.00 16.81 ?  87  SER A OG  1 
ATOM   661  N  N   . VAL A 1 88  ? 45.845 3.141   48.015  1.00 11.02 ?  88  VAL A N   1 
ATOM   662  C  CA  . VAL A 1 88  ? 45.098 3.846   46.972  1.00 11.17 ?  88  VAL A CA  1 
ATOM   663  C  C   . VAL A 1 88  ? 45.981 4.892   46.322  1.00 13.03 ?  88  VAL A C   1 
ATOM   664  O  O   . VAL A 1 88  ? 45.827 5.210   45.140  1.00 16.17 ?  88  VAL A O   1 
ATOM   665  C  CB  . VAL A 1 88  ? 43.827 4.470   47.581  1.00 12.68 ?  88  VAL A CB  1 
ATOM   666  C  CG1 . VAL A 1 88  ? 43.093 5.348   46.555  1.00 14.93 ?  88  VAL A CG1 1 
ATOM   667  C  CG2 . VAL A 1 88  ? 42.903 3.377   48.082  1.00 12.31 ?  88  VAL A CG2 1 
ATOM   668  N  N   . SER A 1 89  ? 46.946 5.414   47.067  1.00 13.42 ?  89  SER A N   1 
ATOM   669  C  CA  . SER A 1 89  ? 47.798 6.466   46.564  1.00 10.79 ?  89  SER A CA  1 
ATOM   670  C  C   . SER A 1 89  ? 48.798 5.966   45.525  1.00 13.72 ?  89  SER A C   1 
ATOM   671  O  O   . SER A 1 89  ? 49.452 6.790   44.885  1.00 14.47 ?  89  SER A O   1 
ATOM   672  C  CB  . SER A 1 89  ? 48.513 7.133   47.742  1.00 12.74 ?  89  SER A CB  1 
ATOM   673  O  OG  . SER A 1 89  ? 47.544 7.792   48.539  1.00 14.80 ?  89  SER A OG  1 
ATOM   674  N  N   . LEU A 1 90  ? 48.934 4.643   45.331  1.00 10.97 ?  90  LEU A N   1 
ATOM   675  C  CA  . LEU A 1 90  ? 49.668 4.160   44.164  1.00 12.38 ?  90  LEU A CA  1 
ATOM   676  C  C   . LEU A 1 90  ? 49.040 4.673   42.874  1.00 15.02 ?  90  LEU A C   1 
ATOM   677  O  O   . LEU A 1 90  ? 49.737 4.842   41.868  1.00 15.32 ?  90  LEU A O   1 
ATOM   678  C  CB  . LEU A 1 90  ? 49.699 2.626   44.140  1.00 10.41 ?  90  LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 90  ? 50.670 2.045   45.180  1.00 12.16 ?  90  LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 90  ? 50.377 0.571   45.449  1.00 17.79 ?  90  LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 90  ? 52.119 2.240   44.788  1.00 16.90 ?  90  LEU A CD2 1 
ATOM   682  N  N   . ALA A 1 91  ? 47.735 4.914   42.885  1.00 13.74 ?  91  ALA A N   1 
ATOM   683  C  CA  . ALA A 1 91  ? 47.059 5.433   41.696  1.00 16.54 ?  91  ALA A CA  1 
ATOM   684  C  C   . ALA A 1 91  ? 47.025 6.949   41.661  1.00 18.35 ?  91  ALA A C   1 
ATOM   685  O  O   . ALA A 1 91  ? 47.068 7.543   40.574  1.00 22.35 ?  91  ALA A O   1 
ATOM   686  C  CB  . ALA A 1 91  ? 45.628 4.902   41.613  1.00 17.21 ?  91  ALA A CB  1 
ATOM   687  N  N   . THR A 1 92  ? 46.946 7.591   42.820  1.00 14.85 ?  92  THR A N   1 
ATOM   688  C  CA  . THR A 1 92  ? 46.798 9.039   42.814  1.00 14.84 ?  92  THR A CA  1 
ATOM   689  C  C   . THR A 1 92  ? 48.118 9.790   42.712  1.00 14.69 ?  92  THR A C   1 
ATOM   690  O  O   . THR A 1 92  ? 48.179 10.829  42.038  1.00 16.09 ?  92  THR A O   1 
ATOM   691  C  CB  . THR A 1 92  ? 46.066 9.513   44.071  1.00 15.24 ?  92  THR A CB  1 
ATOM   692  O  OG1 . THR A 1 92  ? 46.826 9.143   45.221  1.00 17.94 ?  92  THR A OG1 1 
ATOM   693  C  CG2 . THR A 1 92  ? 44.678 8.916   44.149  1.00 16.50 ?  92  THR A CG2 1 
ATOM   694  N  N   . LEU A 1 93  ? 49.169 9.328   43.383  1.00 14.34 ?  93  LEU A N   1 
ATOM   695  C  CA  . LEU A 1 93  ? 50.398 10.115  43.395  1.00 12.99 ?  93  LEU A CA  1 
ATOM   696  C  C   . LEU A 1 93  ? 51.012 10.279  42.004  1.00 16.44 ?  93  LEU A C   1 
ATOM   697  O  O   . LEU A 1 93  ? 51.513 11.377  41.711  1.00 16.40 ?  93  LEU A O   1 
ATOM   698  C  CB  . LEU A 1 93  ? 51.398 9.522   44.402  1.00 12.49 ?  93  LEU A CB  1 
ATOM   699  C  CG  . LEU A 1 93  ? 50.964 9.743   45.869  1.00 13.33 ?  93  LEU A CG  1 
ATOM   700  C  CD1 . LEU A 1 93  ? 51.847 8.963   46.847  1.00 11.85 ?  93  LEU A CD1 1 
ATOM   701  C  CD2 . LEU A 1 93  ? 50.982 11.220  46.243  1.00 16.13 ?  93  LEU A CD2 1 
ATOM   702  N  N   . PRO A 1 94  ? 50.993 9.286   41.111  1.00 16.20 ?  94  PRO A N   1 
ATOM   703  C  CA  . PRO A 1 94  ? 51.501 9.541   39.755  1.00 18.44 ?  94  PRO A CA  1 
ATOM   704  C  C   . PRO A 1 94  ? 50.687 10.587  39.003  1.00 17.60 ?  94  PRO A C   1 
ATOM   705  O  O   . PRO A 1 94  ? 51.255 11.329  38.190  1.00 21.37 ?  94  PRO A O   1 
ATOM   706  C  CB  . PRO A 1 94  ? 51.426 8.155   39.094  1.00 19.21 ?  94  PRO A CB  1 
ATOM   707  C  CG  . PRO A 1 94  ? 51.570 7.194   40.244  1.00 19.17 ?  94  PRO A CG  1 
ATOM   708  C  CD  . PRO A 1 94  ? 50.726 7.852   41.322  1.00 16.19 ?  94  PRO A CD  1 
ATOM   709  N  N   . VAL A 1 95  ? 49.376 10.677  39.254  1.00 15.28 ?  95  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 95  ? 48.582 11.737  38.639  1.00 18.82 ?  95  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 95  ? 49.013 13.103  39.160  1.00 21.37 ?  95  VAL A C   1 
ATOM   712  O  O   . VAL A 1 95  ? 49.167 14.055  38.387  1.00 19.62 ?  95  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 95  ? 47.085 11.491  38.875  1.00 22.53 ?  95  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 95  ? 46.264 12.625  38.258  1.00 21.04 ?  95  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 95  ? 46.683 10.146  38.276  1.00 24.19 ?  95  VAL A CG2 1 
ATOM   716  N  N   . VAL A 1 96  ? 49.217 13.222  40.477  1.00 17.68 ?  96  VAL A N   1 
ATOM   717  C  CA  . VAL A 1 96  ? 49.692 14.484  41.050  1.00 16.73 ?  96  VAL A CA  1 
ATOM   718  C  C   . VAL A 1 96  ? 51.044 14.867  40.459  1.00 20.80 ?  96  VAL A C   1 
ATOM   719  O  O   . VAL A 1 96  ? 51.274 16.024  40.082  1.00 22.51 ?  96  VAL A O   1 
ATOM   720  C  CB  . VAL A 1 96  ? 49.772 14.382  42.588  1.00 17.03 ?  96  VAL A CB  1 
ATOM   721  C  CG1 . VAL A 1 96  ? 50.320 15.691  43.172  1.00 19.44 ?  96  VAL A CG1 1 
ATOM   722  C  CG2 . VAL A 1 96  ? 48.414 14.053  43.165  1.00 19.71 ?  96  VAL A CG2 1 
ATOM   723  N  N   . ALA A 1 97  ? 51.973 13.905  40.393  1.00 19.71 ?  97  ALA A N   1 
ATOM   724  C  CA  . ALA A 1 97  ? 53.306 14.203  39.873  1.00 20.07 ?  97  ALA A CA  1 
ATOM   725  C  C   . ALA A 1 97  ? 53.269 14.548  38.391  1.00 22.89 ?  97  ALA A C   1 
ATOM   726  O  O   . ALA A 1 97  ? 54.069 15.368  37.927  1.00 25.52 ?  97  ALA A O   1 
ATOM   727  C  CB  . ALA A 1 97  ? 54.245 13.023  40.103  1.00 23.25 ?  97  ALA A CB  1 
ATOM   728  N  N   . ARG A 1 98  ? 52.376 13.909  37.637  1.00 19.54 ?  98  ARG A N   1 
ATOM   729  C  CA  . ARG A 1 98  ? 52.177 14.262  36.234  1.00 24.61 ?  98  ARG A CA  1 
ATOM   730  C  C   . ARG A 1 98  ? 51.696 15.700  36.092  1.00 24.21 ?  98  ARG A C   1 
ATOM   731  O  O   . ARG A 1 98  ? 52.292 16.508  35.365  1.00 28.32 ?  98  ARG A O   1 
ATOM   732  C  CB  . ARG A 1 98  ? 51.162 13.307  35.613  1.00 23.52 ?  98  ARG A CB  1 
ATOM   733  C  CG  . ARG A 1 98  ? 50.900 13.513  34.129  1.00 32.27 ?  98  ARG A CG  1 
ATOM   734  C  CD  . ARG A 1 98  ? 50.820 12.170  33.403  1.00 35.54 ?  98  ARG A CD  1 
ATOM   735  N  NE  . ARG A 1 98  ? 49.797 11.263  33.943  1.00 43.70 ?  98  ARG A NE  1 
ATOM   736  C  CZ  . ARG A 1 98  ? 50.063 10.230  34.748  1.00 42.32 ?  98  ARG A CZ  1 
ATOM   737  N  NH1 . ARG A 1 98  ? 51.315 9.981   35.116  1.00 42.88 ?  98  ARG A NH1 1 
ATOM   738  N  NH2 . ARG A 1 98  ? 49.087 9.445   35.196  1.00 41.12 ?  98  ARG A NH2 1 
ATOM   739  N  N   . GLU A 1 99  ? 50.603 16.032  36.778  1.00 22.34 ?  99  GLU A N   1 
ATOM   740  C  CA  . GLU A 1 99  ? 49.940 17.320  36.611  1.00 23.65 ?  99  GLU A CA  1 
ATOM   741  C  C   . GLU A 1 99  ? 50.682 18.472  37.275  1.00 27.72 ?  99  GLU A C   1 
ATOM   742  O  O   . GLU A 1 99  ? 50.563 19.622  36.823  1.00 28.34 ?  99  GLU A O   1 
ATOM   743  C  CB  . GLU A 1 99  ? 48.526 17.238  37.166  1.00 25.30 ?  99  GLU A CB  1 
ATOM   744  C  CG  . GLU A 1 99  ? 47.663 16.300  36.367  1.00 33.89 ?  99  GLU A CG  1 
ATOM   745  C  CD  . GLU A 1 99  ? 47.448 16.819  34.962  1.00 41.08 ?  99  GLU A CD  1 
ATOM   746  O  OE1 . GLU A 1 99  ? 47.383 18.061  34.798  1.00 40.73 ?  99  GLU A OE1 1 
ATOM   747  O  OE2 . GLU A 1 99  ? 47.342 15.990  34.028  1.00 48.63 -1 99  GLU A OE2 1 
ATOM   748  N  N   . HIS A 1 100 ? 51.418 18.195  38.349  1.00 23.34 ?  100 HIS A N   1 
ATOM   749  C  CA  . HIS A 1 100 ? 52.139 19.210  39.116  1.00 26.24 ?  100 HIS A CA  1 
ATOM   750  C  C   . HIS A 1 100 ? 53.547 18.695  39.364  1.00 27.19 ?  100 HIS A C   1 
ATOM   751  O  O   . HIS A 1 100 ? 53.883 18.271  40.480  1.00 23.06 ?  100 HIS A O   1 
ATOM   752  C  CB  . HIS A 1 100 ? 51.438 19.519  40.439  1.00 25.16 ?  100 HIS A CB  1 
ATOM   753  C  CG  . HIS A 1 100 ? 50.083 20.128  40.279  1.00 26.59 ?  100 HIS A CG  1 
ATOM   754  N  ND1 . HIS A 1 100 ? 49.900 21.458  39.961  1.00 28.80 ?  100 HIS A ND1 1 
ATOM   755  C  CD2 . HIS A 1 100 ? 48.846 19.595  40.404  1.00 27.00 ?  100 HIS A CD2 1 
ATOM   756  C  CE1 . HIS A 1 100 ? 48.607 21.714  39.892  1.00 27.32 ?  100 HIS A CE1 1 
ATOM   757  N  NE2 . HIS A 1 100 ? 47.945 20.602  40.155  1.00 29.89 ?  100 HIS A NE2 1 
ATOM   758  N  N   . PRO A 1 101 ? 54.405 18.734  38.347  1.00 24.98 ?  101 PRO A N   1 
ATOM   759  C  CA  . PRO A 1 101 ? 55.746 18.160  38.496  1.00 25.04 ?  101 PRO A CA  1 
ATOM   760  C  C   . PRO A 1 101 ? 56.593 18.873  39.534  1.00 24.61 ?  101 PRO A C   1 
ATOM   761  O  O   . PRO A 1 101 ? 57.615 18.328  39.972  1.00 26.12 ?  101 PRO A O   1 
ATOM   762  C  CB  . PRO A 1 101 ? 56.347 18.299  37.087  1.00 27.01 ?  101 PRO A CB  1 
ATOM   763  C  CG  . PRO A 1 101 ? 55.222 18.686  36.203  1.00 31.76 ?  101 PRO A CG  1 
ATOM   764  C  CD  . PRO A 1 101 ? 54.232 19.396  37.048  1.00 29.63 ?  101 PRO A CD  1 
ATOM   765  N  N   . ASP A 1 102 ? 56.196 20.067  39.957  1.00 23.42 ?  102 ASP A N   1 
ATOM   766  C  CA  . ASP A 1 102 ? 56.935 20.794  40.973  1.00 25.02 ?  102 ASP A CA  1 
ATOM   767  C  C   . ASP A 1 102 ? 56.354 20.593  42.368  1.00 25.02 ?  102 ASP A C   1 
ATOM   768  O  O   . ASP A 1 102 ? 56.892 21.141  43.334  1.00 20.65 ?  102 ASP A O   1 
ATOM   769  C  CB  . ASP A 1 102 ? 56.980 22.290  40.621  1.00 27.40 ?  102 ASP A CB  1 
ATOM   770  C  CG  . ASP A 1 102 ? 55.594 22.923  40.499  1.00 27.73 ?  102 ASP A CG  1 
ATOM   771  O  OD1 . ASP A 1 102 ? 54.602 22.223  40.183  1.00 30.82 ?  102 ASP A OD1 1 
ATOM   772  O  OD2 . ASP A 1 102 ? 55.503 24.154  40.700  1.00 32.76 -1 102 ASP A OD2 1 
ATOM   773  N  N   . ALA A 1 103 ? 55.296 19.793  42.500  1.00 20.18 ?  103 ALA A N   1 
ATOM   774  C  CA  . ALA A 1 103 ? 54.638 19.651  43.792  1.00 17.97 ?  103 ALA A CA  1 
ATOM   775  C  C   . ALA A 1 103 ? 55.506 18.876  44.781  1.00 16.39 ?  103 ALA A C   1 
ATOM   776  O  O   . ALA A 1 103 ? 56.196 17.917  44.417  1.00 17.34 ?  103 ALA A O   1 
ATOM   777  C  CB  . ALA A 1 103 ? 53.301 18.935  43.633  1.00 16.54 ?  103 ALA A CB  1 
ATOM   778  N  N   . VAL A 1 104 ? 55.427 19.273  46.048  1.00 13.99 ?  104 VAL A N   1 
ATOM   779  C  CA  . VAL A 1 104 ? 56.029 18.515  47.139  1.00 15.00 ?  104 VAL A CA  1 
ATOM   780  C  C   . VAL A 1 104 ? 54.927 17.691  47.772  1.00 14.71 ?  104 VAL A C   1 
ATOM   781  O  O   . VAL A 1 104 ? 53.823 18.200  47.990  1.00 14.24 ?  104 VAL A O   1 
ATOM   782  C  CB  . VAL A 1 104 ? 56.692 19.442  48.165  1.00 15.49 ?  104 VAL A CB  1 
ATOM   783  C  CG1 . VAL A 1 104 ? 57.071 18.657  49.429  1.00 13.45 ?  104 VAL A CG1 1 
ATOM   784  C  CG2 . VAL A 1 104 ? 57.925 20.075  47.542  1.00 16.51 ?  104 VAL A CG2 1 
ATOM   785  N  N   . VAL A 1 105 ? 55.199 16.411  48.014  1.00 13.24 ?  105 VAL A N   1 
ATOM   786  C  CA  . VAL A 1 105 ? 54.244 15.534  48.682  1.00 12.47 ?  105 VAL A CA  1 
ATOM   787  C  C   . VAL A 1 105 ? 54.676 15.402  50.129  1.00 9.00  ?  105 VAL A C   1 
ATOM   788  O  O   . VAL A 1 105 ? 55.787 14.939  50.398  1.00 12.55 ?  105 VAL A O   1 
ATOM   789  C  CB  . VAL A 1 105 ? 54.164 14.160  48.012  1.00 12.57 ?  105 VAL A CB  1 
ATOM   790  C  CG1 . VAL A 1 105 ? 53.317 13.219  48.879  1.00 12.95 ?  105 VAL A CG1 1 
ATOM   791  C  CG2 . VAL A 1 105 ? 53.533 14.307  46.611  1.00 14.75 ?  105 VAL A CG2 1 
ATOM   792  N  N   . LEU A 1 106 ? 53.812 15.852  51.046  1.00 9.30  ?  106 LEU A N   1 
ATOM   793  C  CA  . LEU A 1 106 ? 53.986 15.611  52.473  1.00 8.91  ?  106 LEU A CA  1 
ATOM   794  C  C   . LEU A 1 106 ? 53.274 14.305  52.771  1.00 10.37 ?  106 LEU A C   1 
ATOM   795  O  O   . LEU A 1 106 ? 52.044 14.231  52.707  1.00 11.91 ?  106 LEU A O   1 
ATOM   796  C  CB  . LEU A 1 106 ? 53.416 16.755  53.308  1.00 9.85  ?  106 LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 106 ? 53.990 18.150  53.054  1.00 12.79 ?  106 LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 106 ? 53.149 19.166  53.837  1.00 14.45 ?  106 LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 106 ? 55.445 18.207  53.446  1.00 12.19 ?  106 LEU A CD2 1 
ATOM   800  N  N   . TYR A 1 107 ? 54.052 13.279  53.075  1.00 10.68 ?  107 TYR A N   1 
ATOM   801  C  CA  . TYR A 1 107 ? 53.536 11.935  53.309  1.00 10.63 ?  107 TYR A CA  1 
ATOM   802  C  C   . TYR A 1 107 ? 53.607 11.741  54.824  1.00 9.59  ?  107 TYR A C   1 
ATOM   803  O  O   . TYR A 1 107 ? 54.667 11.424  55.375  1.00 11.77 ?  107 TYR A O   1 
ATOM   804  C  CB  . TYR A 1 107 ? 54.355 10.926  52.501  1.00 11.76 ?  107 TYR A CB  1 
ATOM   805  C  CG  . TYR A 1 107 ? 53.705 9.564   52.348  1.00 9.98  ?  107 TYR A CG  1 
ATOM   806  C  CD1 . TYR A 1 107 ? 53.726 8.653   53.392  1.00 9.94  ?  107 TYR A CD1 1 
ATOM   807  C  CD2 . TYR A 1 107 ? 53.077 9.197   51.177  1.00 11.45 ?  107 TYR A CD2 1 
ATOM   808  C  CE1 . TYR A 1 107 ? 53.130 7.388   53.272  1.00 11.04 ?  107 TYR A CE1 1 
ATOM   809  C  CE2 . TYR A 1 107 ? 52.463 7.929   51.045  1.00 11.92 ?  107 TYR A CE2 1 
ATOM   810  C  CZ  . TYR A 1 107 ? 52.501 7.036   52.094  1.00 11.80 ?  107 TYR A CZ  1 
ATOM   811  O  OH  . TYR A 1 107 ? 51.902 5.776   51.982  1.00 11.16 ?  107 TYR A OH  1 
ATOM   812  N  N   . ILE A 1 108 ? 52.474 11.976  55.497  1.00 8.59  ?  108 ILE A N   1 
ATOM   813  C  CA  . ILE A 1 108 ? 52.410 12.029  56.954  1.00 9.55  ?  108 ILE A CA  1 
ATOM   814  C  C   . ILE A 1 108 ? 51.974 10.660  57.440  1.00 11.26 ?  108 ILE A C   1 
ATOM   815  O  O   . ILE A 1 108 ? 50.849 10.244  57.165  1.00 11.29 ?  108 ILE A O   1 
ATOM   816  C  CB  . ILE A 1 108 ? 51.428 13.116  57.423  1.00 12.22 ?  108 ILE A CB  1 
ATOM   817  C  CG1 . ILE A 1 108 ? 51.714 14.424  56.671  1.00 12.92 ?  108 ILE A CG1 1 
ATOM   818  C  CG2 . ILE A 1 108 ? 51.492 13.279  58.941  1.00 12.17 ?  108 ILE A CG2 1 
ATOM   819  C  CD1 . ILE A 1 108 ? 50.906 15.598  57.163  1.00 14.95 ?  108 ILE A CD1 1 
ATOM   820  N  N   . ASP A 1 109 ? 52.856 9.966   58.152  1.00 9.00  ?  109 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 109 ? 52.671 8.534   58.366  1.00 8.97  ?  109 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 109 ? 53.590 8.127   59.504  1.00 10.66 ?  109 ASP A C   1 
ATOM   823  O  O   . ASP A 1 109 ? 54.691 8.665   59.611  1.00 11.38 ?  109 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 109 ? 53.025 7.759   57.080  1.00 7.81  ?  109 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 109 ? 52.432 6.358   57.045  1.00 9.47  ?  109 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 109 ? 52.541 5.623   58.044  1.00 8.47  ?  109 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 109 ? 51.887 6.012   55.988  1.00 8.53  -1 109 ASP A OD2 1 
ATOM   828  N  N   . GLY A 1 110 ? 53.113 7.240   60.384  1.00 8.98  ?  110 GLY A N   1 
ATOM   829  C  CA  . GLY A 1 110 ? 54.018 6.675   61.383  1.00 9.15  ?  110 GLY A CA  1 
ATOM   830  C  C   . GLY A 1 110 ? 55.124 5.840   60.769  1.00 11.82 ?  110 GLY A C   1 
ATOM   831  O  O   . GLY A 1 110 ? 56.171 5.632   61.404  1.00 12.41 ?  110 GLY A O   1 
ATOM   832  N  N   . HIS A 1 111 ? 54.897 5.334   59.560  1.00 10.06 ?  111 HIS A N   1 
ATOM   833  C  CA  . HIS A 1 111 ? 55.800 4.490   58.795  1.00 10.24 ?  111 HIS A CA  1 
ATOM   834  C  C   . HIS A 1 111 ? 56.412 5.250   57.628  1.00 12.74 ?  111 HIS A C   1 
ATOM   835  O  O   . HIS A 1 111 ? 56.005 6.362   57.294  1.00 14.56 ?  111 HIS A O   1 
ATOM   836  C  CB  . HIS A 1 111 ? 55.029 3.276   58.277  1.00 10.70 ?  111 HIS A CB  1 
ATOM   837  C  CG  . HIS A 1 111 ? 54.333 2.506   59.357  1.00 9.91  ?  111 HIS A CG  1 
ATOM   838  N  ND1 . HIS A 1 111 ? 53.032 2.757   59.736  1.00 10.18 ?  111 HIS A ND1 1 
ATOM   839  C  CD2 . HIS A 1 111 ? 54.754 1.459   60.109  1.00 13.58 ?  111 HIS A CD2 1 
ATOM   840  C  CE1 . HIS A 1 111 ? 52.683 1.899   60.685  1.00 12.43 ?  111 HIS A CE1 1 
ATOM   841  N  NE2 . HIS A 1 111 ? 53.714 1.111   60.938  1.00 12.59 ?  111 HIS A NE2 1 
ATOM   842  N  N   . GLY A 1 112 ? 57.414 4.631   57.004  1.00 13.63 ?  112 GLY A N   1 
ATOM   843  C  CA  . GLY A 1 112 ? 57.984 5.199   55.796  1.00 13.75 ?  112 GLY A CA  1 
ATOM   844  C  C   . GLY A 1 112 ? 57.274 4.780   54.519  1.00 12.11 ?  112 GLY A C   1 
ATOM   845  O  O   . GLY A 1 112 ? 57.375 5.477   53.501  1.00 12.44 ?  112 GLY A O   1 
ATOM   846  N  N   . ASP A 1 113 ? 56.586 3.626   54.546  1.00 12.04 ?  113 ASP A N   1 
ATOM   847  C  CA  . ASP A 1 113 ? 55.877 3.095   53.356  1.00 11.33 ?  113 ASP A CA  1 
ATOM   848  C  C   . ASP A 1 113 ? 56.794 3.103   52.128  1.00 12.94 ?  113 ASP A C   1 
ATOM   849  O  O   . ASP A 1 113 ? 56.378 3.380   51.000  1.00 12.82 ?  113 ASP A O   1 
ATOM   850  C  CB  . ASP A 1 113 ? 54.565 3.853   53.082  1.00 12.09 ?  113 ASP A CB  1 
ATOM   851  C  CG  . ASP A 1 113 ? 53.487 3.574   54.136  1.00 12.34 ?  113 ASP A CG  1 
ATOM   852  O  OD1 . ASP A 1 113 ? 53.796 2.872   55.140  1.00 10.35 ?  113 ASP A OD1 1 
ATOM   853  O  OD2 . ASP A 1 113 ? 52.331 4.067   53.981  1.00 11.49 -1 113 ASP A OD2 1 
ATOM   854  N  N   . PHE A 1 114 ? 58.052 2.719   52.339  1.00 15.09 ?  114 PHE A N   1 
ATOM   855  C  CA  . PHE A 1 114 ? 59.078 2.856   51.312  1.00 13.41 ?  114 PHE A CA  1 
ATOM   856  C  C   . PHE A 1 114 ? 59.755 1.519   51.010  1.00 18.02 ?  114 PHE A C   1 
ATOM   857  O  O   . PHE A 1 114 ? 60.896 1.486   50.547  1.00 20.64 ?  114 PHE A O   1 
ATOM   858  C  CB  . PHE A 1 114 ? 60.107 3.914   51.726  1.00 15.03 ?  114 PHE A CB  1 
ATOM   859  C  CG  . PHE A 1 114 ? 60.724 4.662   50.569  1.00 14.83 ?  114 PHE A CG  1 
ATOM   860  C  CD1 . PHE A 1 114 ? 60.012 5.646   49.888  1.00 16.10 ?  114 PHE A CD1 1 
ATOM   861  C  CD2 . PHE A 1 114 ? 62.031 4.399   50.178  1.00 16.37 ?  114 PHE A CD2 1 
ATOM   862  C  CE1 . PHE A 1 114 ? 60.585 6.340   48.824  1.00 17.26 ?  114 PHE A CE1 1 
ATOM   863  C  CE2 . PHE A 1 114 ? 62.608 5.092   49.131  1.00 15.80 ?  114 PHE A CE2 1 
ATOM   864  C  CZ  . PHE A 1 114 ? 61.891 6.060   48.449  1.00 18.49 ?  114 PHE A CZ  1 
ATOM   865  N  N   . ASN A 1 115 ? 59.059 0.408   51.257  1.00 16.78 ?  115 ASN A N   1 
ATOM   866  C  CA  . ASN A 1 115 ? 59.594 -0.908  50.924  1.00 17.06 ?  115 ASN A CA  1 
ATOM   867  C  C   . ASN A 1 115 ? 59.422 -1.215  49.437  1.00 18.67 ?  115 ASN A C   1 
ATOM   868  O  O   . ASN A 1 115 ? 58.539 -0.692  48.762  1.00 17.31 ?  115 ASN A O   1 
ATOM   869  C  CB  . ASN A 1 115 ? 58.897 -1.999  51.747  1.00 18.54 ?  115 ASN A CB  1 
ATOM   870  C  CG  . ASN A 1 115 ? 59.238 -1.924  53.218  1.00 23.92 ?  115 ASN A CG  1 
ATOM   871  O  OD1 . ASN A 1 115 ? 60.325 -2.331  53.632  1.00 24.96 ?  115 ASN A OD1 1 
ATOM   872  N  ND2 . ASN A 1 115 ? 58.315 -1.385  54.022  1.00 25.17 ?  115 ASN A ND2 1 
ATOM   873  N  N   . THR A 1 116 ? 60.286 -2.089  48.930  1.00 19.83 ?  116 THR A N   1 
ATOM   874  C  CA  . THR A 1 116 ? 60.174 -2.655  47.593  1.00 18.38 ?  116 THR A CA  1 
ATOM   875  C  C   . THR A 1 116 ? 59.886 -4.146  47.695  1.00 19.53 ?  116 THR A C   1 
ATOM   876  O  O   . THR A 1 116 ? 59.994 -4.734  48.776  1.00 22.47 ?  116 THR A O   1 
ATOM   877  C  CB  . THR A 1 116 ? 61.476 -2.437  46.814  1.00 21.43 ?  116 THR A CB  1 
ATOM   878  O  OG1 . THR A 1 116 ? 62.542 -3.111  47.488  1.00 23.81 ?  116 THR A OG1 1 
ATOM   879  C  CG2 . THR A 1 116 ? 61.795 -0.956  46.698  1.00 22.60 ?  116 THR A CG2 1 
ATOM   880  N  N   . PRO A 1 117 ? 59.534 -4.803  46.582  1.00 18.61 ?  117 PRO A N   1 
ATOM   881  C  CA  . PRO A 1 117 ? 59.343 -6.261  46.638  1.00 23.62 ?  117 PRO A CA  1 
ATOM   882  C  C   . PRO A 1 117 ? 60.535 -6.988  47.240  1.00 23.91 ?  117 PRO A C   1 
ATOM   883  O  O   . PRO A 1 117 ? 60.363 -8.040  47.874  1.00 23.85 ?  117 PRO A O   1 
ATOM   884  C  CB  . PRO A 1 117 ? 59.121 -6.630  45.166  1.00 22.78 ?  117 PRO A CB  1 
ATOM   885  C  CG  . PRO A 1 117 ? 58.426 -5.424  44.601  1.00 22.62 ?  117 PRO A CG  1 
ATOM   886  C  CD  . PRO A 1 117 ? 59.099 -4.247  45.281  1.00 18.43 ?  117 PRO A CD  1 
ATOM   887  N  N   . GLU A 1 118 ? 61.736 -6.419  47.096  1.00 24.05 ?  118 GLU A N   1 
ATOM   888  C  CA  . GLU A 1 118 ? 62.952 -7.049  47.595  1.00 30.05 ?  118 GLU A CA  1 
ATOM   889  C  C   . GLU A 1 118 ? 63.179 -6.791  49.080  1.00 31.79 ?  118 GLU A C   1 
ATOM   890  O  O   . GLU A 1 118 ? 63.815 -7.611  49.749  1.00 34.91 ?  118 GLU A O   1 
ATOM   891  C  CB  . GLU A 1 118 ? 64.160 -6.555  46.793  1.00 30.31 ?  118 GLU A CB  1 
ATOM   892  C  CG  . GLU A 1 118 ? 64.212 -7.078  45.372  1.00 43.25 ?  118 GLU A CG  1 
ATOM   893  C  CD  . GLU A 1 118 ? 63.201 -6.409  44.454  1.00 43.96 ?  118 GLU A CD  1 
ATOM   894  O  OE1 . GLU A 1 118 ? 62.860 -5.218  44.686  1.00 39.65 ?  118 GLU A OE1 1 
ATOM   895  O  OE2 . GLU A 1 118 ? 62.741 -7.085  43.503  1.00 48.63 -1 118 GLU A OE2 1 
ATOM   896  N  N   . THR A 1 119 ? 62.674 -5.681  49.625  1.00 23.86 ?  119 THR A N   1 
ATOM   897  C  CA  . THR A 1 119 ? 62.944 -5.349  51.021  1.00 23.98 ?  119 THR A CA  1 
ATOM   898  C  C   . THR A 1 119 ? 61.787 -5.641  51.968  1.00 24.59 ?  119 THR A C   1 
ATOM   899  O  O   . THR A 1 119 ? 62.015 -5.721  53.180  1.00 27.47 ?  119 THR A O   1 
ATOM   900  C  CB  . THR A 1 119 ? 63.328 -3.869  51.174  1.00 30.49 ?  119 THR A CB  1 
ATOM   901  O  OG1 . THR A 1 119 ? 62.188 -3.022  50.912  1.00 23.72 ?  119 THR A OG1 1 
ATOM   902  C  CG2 . THR A 1 119 ? 64.488 -3.520  50.246  1.00 30.70 ?  119 THR A CG2 1 
ATOM   903  N  N   . THR A 1 120 ? 60.560 -5.789  51.471  1.00 21.06 ?  120 THR A N   1 
ATOM   904  C  CA  . THR A 1 120 ? 59.433 -5.983  52.374  1.00 18.99 ?  120 THR A CA  1 
ATOM   905  C  C   . THR A 1 120 ? 59.605 -7.248  53.221  1.00 24.82 ?  120 THR A C   1 
ATOM   906  O  O   . THR A 1 120 ? 59.929 -8.321  52.707  1.00 22.91 ?  120 THR A O   1 
ATOM   907  C  CB  . THR A 1 120 ? 58.120 -6.041  51.586  1.00 18.90 ?  120 THR A CB  1 
ATOM   908  O  OG1 . THR A 1 120 ? 57.018 -6.174  52.490  1.00 18.17 ?  120 THR A OG1 1 
ATOM   909  C  CG2 . THR A 1 120 ? 58.090 -7.201  50.577  1.00 22.06 ?  120 THR A CG2 1 
ATOM   910  N  N   . ASP A 1 121 ? 59.415 -7.105  54.532  1.00 19.14 ?  121 ASP A N   1 
ATOM   911  C  CA  . ASP A 1 121 ? 59.372 -8.267  55.421  1.00 23.94 ?  121 ASP A CA  1 
ATOM   912  C  C   . ASP A 1 121 ? 57.992 -8.902  55.500  1.00 23.61 ?  121 ASP A C   1 
ATOM   913  O  O   . ASP A 1 121 ? 57.891 -10.085 55.848  1.00 26.67 ?  121 ASP A O   1 
ATOM   914  C  CB  . ASP A 1 121 ? 59.776 -7.892  56.847  1.00 22.16 ?  121 ASP A CB  1 
ATOM   915  C  CG  . ASP A 1 121 ? 61.227 -7.491  56.973  1.00 30.11 ?  121 ASP A CG  1 
ATOM   916  O  OD1 . ASP A 1 121 ? 62.066 -8.029  56.221  1.00 30.39 ?  121 ASP A OD1 1 
ATOM   917  O  OD2 . ASP A 1 121 ? 61.521 -6.636  57.845  1.00 30.87 -1 121 ASP A OD2 1 
ATOM   918  N  N   . THR A 1 122 ? 56.923 -8.142  55.226  1.00 18.43 ?  122 THR A N   1 
ATOM   919  C  CA  . THR A 1 122 ? 55.564 -8.627  55.423  1.00 18.70 ?  122 THR A CA  1 
ATOM   920  C  C   . THR A 1 122 ? 54.791 -8.838  54.133  1.00 19.96 ?  122 THR A C   1 
ATOM   921  O  O   . THR A 1 122 ? 53.703 -9.420  54.184  1.00 20.88 ?  122 THR A O   1 
ATOM   922  C  CB  . THR A 1 122 ? 54.764 -7.655  56.302  1.00 17.68 ?  122 THR A CB  1 
ATOM   923  O  OG1 . THR A 1 122 ? 54.425 -6.501  55.529  1.00 18.57 ?  122 THR A OG1 1 
ATOM   924  C  CG2 . THR A 1 122 ? 55.575 -7.228  57.507  1.00 16.29 ?  122 THR A CG2 1 
ATOM   925  N  N   . GLY A 1 123 ? 55.320 -8.393  52.990  1.00 17.43 ?  123 GLY A N   1 
ATOM   926  C  CA  . GLY A 1 123 ? 54.595 -8.451  51.731  1.00 19.69 ?  123 GLY A CA  1 
ATOM   927  C  C   . GLY A 1 123 ? 53.409 -7.518  51.610  1.00 16.58 ?  123 GLY A C   1 
ATOM   928  O  O   . GLY A 1 123 ? 52.616 -7.653  50.667  1.00 13.73 ?  123 GLY A O   1 
ATOM   929  N  N   . TYR A 1 124 ? 53.255 -6.564  52.525  1.00 16.99 ?  124 TYR A N   1 
ATOM   930  C  CA  . TYR A 1 124 ? 52.061 -5.726  52.556  1.00 15.18 ?  124 TYR A CA  1 
ATOM   931  C  C   . TYR A 1 124 ? 52.195 -4.586  51.552  1.00 15.10 ?  124 TYR A C   1 
ATOM   932  O  O   . TYR A 1 124 ? 53.142 -3.795  51.629  1.00 15.22 ?  124 TYR A O   1 
ATOM   933  C  CB  . TYR A 1 124 ? 51.841 -5.180  53.966  1.00 14.71 ?  124 TYR A CB  1 
ATOM   934  C  CG  . TYR A 1 124 ? 50.648 -4.279  54.096  1.00 14.15 ?  124 TYR A CG  1 
ATOM   935  C  CD1 . TYR A 1 124 ? 49.445 -4.571  53.449  1.00 15.38 ?  124 TYR A CD1 1 
ATOM   936  C  CD2 . TYR A 1 124 ? 50.721 -3.118  54.858  1.00 19.11 ?  124 TYR A CD2 1 
ATOM   937  C  CE1 . TYR A 1 124 ? 48.349 -3.750  53.581  1.00 15.36 ?  124 TYR A CE1 1 
ATOM   938  C  CE2 . TYR A 1 124 ? 49.634 -2.274  54.982  1.00 18.97 ?  124 TYR A CE2 1 
ATOM   939  C  CZ  . TYR A 1 124 ? 48.456 -2.585  54.351  1.00 22.46 ?  124 TYR A CZ  1 
ATOM   940  O  OH  . TYR A 1 124 ? 47.407 -1.707  54.494  1.00 27.70 ?  124 TYR A OH  1 
ATOM   941  N  N   . LEU A 1 125 ? 51.236 -4.489  50.620  1.00 12.45 ?  125 LEU A N   1 
ATOM   942  C  CA  . LEU A 1 125 ? 51.289 -3.429  49.615  1.00 9.78  ?  125 LEU A CA  1 
ATOM   943  C  C   . LEU A 1 125 ? 51.311 -2.043  50.261  1.00 13.94 ?  125 LEU A C   1 
ATOM   944  O  O   . LEU A 1 125 ? 51.944 -1.116  49.742  1.00 13.84 ?  125 LEU A O   1 
ATOM   945  C  CB  . LEU A 1 125 ? 50.087 -3.560  48.679  1.00 12.60 ?  125 LEU A CB  1 
ATOM   946  C  CG  . LEU A 1 125 ? 50.028 -2.608  47.495  1.00 11.70 ?  125 LEU A CG  1 
ATOM   947  C  CD1 . LEU A 1 125 ? 51.134 -2.966  46.523  1.00 10.94 ?  125 LEU A CD1 1 
ATOM   948  C  CD2 . LEU A 1 125 ? 48.659 -2.742  46.831  1.00 12.44 ?  125 LEU A CD2 1 
ATOM   949  N  N   . GLY A 1 126 ? 50.598 -1.882  51.375  1.00 14.21 ?  126 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 126 ? 50.529 -0.599  52.055  1.00 12.84 ?  126 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 126 ? 51.853 -0.101  52.594  1.00 14.98 ?  126 GLY A C   1 
ATOM   952  O  O   . GLY A 1 126 ? 51.973 1.091   52.898  1.00 18.13 ?  126 GLY A O   1 
ATOM   953  N  N   . GLY A 1 127 ? 52.838 -0.980  52.758  1.00 16.35 ?  127 GLY A N   1 
ATOM   954  C  CA  . GLY A 1 127 ? 54.175 -0.548  53.114  1.00 13.72 ?  127 GLY A CA  1 
ATOM   955  C  C   . GLY A 1 127 ? 55.079 -0.271  51.926  1.00 13.36 ?  127 GLY A C   1 
ATOM   956  O  O   . GLY A 1 127 ? 56.279 -0.072  52.134  1.00 14.55 ?  127 GLY A O   1 
ATOM   957  N  N   . MET A 1 128 ? 54.532 -0.232  50.697  1.00 11.64 ?  128 MET A N   1 
ATOM   958  C  CA  . MET A 1 128 ? 55.288 -0.073  49.453  1.00 12.98 ?  128 MET A CA  1 
ATOM   959  C  C   . MET A 1 128 ? 54.806 1.125   48.625  1.00 14.66 ?  128 MET A C   1 
ATOM   960  O  O   . MET A 1 128 ? 55.137 1.228   47.431  1.00 13.73 ?  128 MET A O   1 
ATOM   961  C  CB  . MET A 1 128 ? 55.201 -1.373  48.627  1.00 14.69 ?  128 MET A CB  1 
ATOM   962  C  CG  . MET A 1 128 ? 55.566 -2.619  49.430  1.00 15.79 ?  128 MET A CG  1 
ATOM   963  S  SD  . MET A 1 128 ? 55.058 -4.205  48.648  1.00 19.19 ?  128 MET A SD  1 
ATOM   964  C  CE  . MET A 1 128 ? 55.987 -4.105  47.132  1.00 18.48 ?  128 MET A CE  1 
ATOM   965  N  N   . VAL A 1 129 ? 54.059 2.050   49.244  1.00 11.40 ?  129 VAL A N   1 
ATOM   966  C  CA  . VAL A 1 129 ? 53.302 3.069   48.505  1.00 12.27 ?  129 VAL A CA  1 
ATOM   967  C  C   . VAL A 1 129 ? 54.196 4.198   48.011  1.00 16.42 ?  129 VAL A C   1 
ATOM   968  O  O   . VAL A 1 129 ? 54.164 4.553   46.829  1.00 12.19 ?  129 VAL A O   1 
ATOM   969  C  CB  . VAL A 1 129 ? 52.161 3.626   49.377  1.00 11.05 ?  129 VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 129 ? 51.453 4.779   48.663  1.00 14.50 ?  129 VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 129 ? 51.184 2.526   49.706  1.00 10.67 ?  129 VAL A CG2 1 
ATOM   972  N  N   . LEU A 1 130 ? 54.962 4.826   48.917  1.00 13.01 ?  130 LEU A N   1 
ATOM   973  C  CA  . LEU A 1 130 ? 55.768 5.974   48.507  1.00 11.57 ?  130 LEU A CA  1 
ATOM   974  C  C   . LEU A 1 130 ? 56.904 5.544   47.588  1.00 15.68 ?  130 LEU A C   1 
ATOM   975  O  O   . LEU A 1 130 ? 57.242 6.258   46.637  1.00 15.48 ?  130 LEU A O   1 
ATOM   976  C  CB  . LEU A 1 130 ? 56.308 6.710   49.743  1.00 12.09 ?  130 LEU A CB  1 
ATOM   977  C  CG  . LEU A 1 130 ? 57.051 8.030   49.511  1.00 12.64 ?  130 LEU A CG  1 
ATOM   978  C  CD1 . LEU A 1 130 ? 56.153 9.010   48.740  1.00 13.84 ?  130 LEU A CD1 1 
ATOM   979  C  CD2 . LEU A 1 130 ? 57.473 8.619   50.868  1.00 12.54 ?  130 LEU A CD2 1 
ATOM   980  N  N   . SER A 1 131 ? 57.486 4.369   47.844  1.00 14.15 ?  131 SER A N   1 
ATOM   981  C  CA  . SER A 1 131 ? 58.514 3.837   46.949  1.00 15.93 ?  131 SER A CA  1 
ATOM   982  C  C   . SER A 1 131 ? 57.967 3.502   45.566  1.00 18.44 ?  131 SER A C   1 
ATOM   983  O  O   . SER A 1 131 ? 58.685 3.655   44.570  1.00 15.75 ?  131 SER A O   1 
ATOM   984  C  CB  . SER A 1 131 ? 59.155 2.619   47.604  1.00 16.07 ?  131 SER A CB  1 
ATOM   985  O  OG  . SER A 1 131 ? 58.129 1.693   47.957  1.00 16.56 ?  131 SER A OG  1 
ATOM   986  N  N   . GLY A 1 132 ? 56.708 3.061   45.472  1.00 14.07 ?  132 GLY A N   1 
ATOM   987  C  CA  . GLY A 1 132 ? 56.134 2.797   44.164  1.00 14.71 ?  132 GLY A CA  1 
ATOM   988  C  C   . GLY A 1 132 ? 55.875 4.075   43.387  1.00 17.03 ?  132 GLY A C   1 
ATOM   989  O  O   . GLY A 1 132 ? 56.147 4.147   42.185  1.00 17.60 ?  132 GLY A O   1 
ATOM   990  N  N   . ALA A 1 133 ? 55.369 5.111   44.068  1.00 16.23 ?  133 ALA A N   1 
ATOM   991  C  CA  . ALA A 1 133 ? 55.122 6.380   43.390  1.00 13.83 ?  133 ALA A CA  1 
ATOM   992  C  C   . ALA A 1 133 ? 56.415 7.027   42.920  1.00 16.21 ?  133 ALA A C   1 
ATOM   993  O  O   . ALA A 1 133 ? 56.422 7.714   41.896  1.00 18.82 ?  133 ALA A O   1 
ATOM   994  C  CB  . ALA A 1 133 ? 54.364 7.341   44.310  1.00 13.65 ?  133 ALA A CB  1 
ATOM   995  N  N   . CYS A 1 134 ? 57.503 6.812   43.646  1.00 14.96 ?  134 CYS A N   1 
ATOM   996  C  CA  . CYS A 1 134 ? 58.818 7.349   43.320  1.00 18.54 ?  134 CYS A CA  1 
ATOM   997  C  C   . CYS A 1 134 ? 59.582 6.484   42.330  1.00 18.89 ?  134 CYS A C   1 
ATOM   998  O  O   . CYS A 1 134 ? 60.722 6.821   42.007  1.00 23.02 ?  134 CYS A O   1 
ATOM   999  C  CB  . CYS A 1 134 ? 59.657 7.493   44.586  1.00 19.18 ?  134 CYS A CB  1 
ATOM   1000 S  SG  . CYS A 1 134 ? 59.102 8.837   45.686  1.00 21.23 ?  134 CYS A SG  1 
ATOM   1001 N  N   . GLY A 1 135 ? 59.037 5.344   41.919  1.00 20.14 ?  135 GLY A N   1 
ATOM   1002 C  CA  . GLY A 1 135 ? 59.659 4.521   40.894  1.00 19.27 ?  135 GLY A CA  1 
ATOM   1003 C  C   . GLY A 1 135 ? 60.694 3.512   41.345  1.00 21.97 ?  135 GLY A C   1 
ATOM   1004 O  O   . GLY A 1 135 ? 61.363 2.927   40.481  1.00 21.59 ?  135 GLY A O   1 
ATOM   1005 N  N   . LEU A 1 136 ? 60.855 3.272   42.653  1.00 18.32 ?  136 LEU A N   1 
ATOM   1006 C  CA  . LEU A 1 136 ? 61.817 2.258   43.084  1.00 17.20 ?  136 LEU A CA  1 
ATOM   1007 C  C   . LEU A 1 136 ? 61.359 0.855   42.714  1.00 20.77 ?  136 LEU A C   1 
ATOM   1008 O  O   . LEU A 1 136 ? 62.185 -0.069  42.647  1.00 22.29 ?  136 LEU A O   1 
ATOM   1009 C  CB  . LEU A 1 136 ? 62.070 2.342   44.594  1.00 18.40 ?  136 LEU A CB  1 
ATOM   1010 C  CG  . LEU A 1 136 ? 63.098 3.377   45.074  1.00 21.83 ?  136 LEU A CG  1 
ATOM   1011 C  CD1 . LEU A 1 136 ? 62.532 4.779   45.034  1.00 22.61 ?  136 LEU A CD1 1 
ATOM   1012 C  CD2 . LEU A 1 136 ? 63.571 3.024   46.487  1.00 22.89 ?  136 LEU A CD2 1 
ATOM   1013 N  N   . TRP A 1 137 ? 60.061 0.674   42.497  1.00 17.72 ?  137 TRP A N   1 
ATOM   1014 C  CA  . TRP A 1 137 ? 59.521 -0.550  41.928  1.00 17.28 ?  137 TRP A CA  1 
ATOM   1015 C  C   . TRP A 1 137 ? 58.310 -0.159  41.090  1.00 18.42 ?  137 TRP A C   1 
ATOM   1016 O  O   . TRP A 1 137 ? 57.835 0.978   41.155  1.00 18.45 ?  137 TRP A O   1 
ATOM   1017 C  CB  . TRP A 1 137 ? 59.170 -1.572  43.021  1.00 17.00 ?  137 TRP A CB  1 
ATOM   1018 C  CG  . TRP A 1 137 ? 58.010 -1.156  43.889  1.00 15.34 ?  137 TRP A CG  1 
ATOM   1019 C  CD1 . TRP A 1 137 ? 58.021 -0.228  44.901  1.00 15.49 ?  137 TRP A CD1 1 
ATOM   1020 C  CD2 . TRP A 1 137 ? 56.675 -1.671  43.823  1.00 15.95 ?  137 TRP A CD2 1 
ATOM   1021 N  NE1 . TRP A 1 137 ? 56.763 -0.143  45.467  1.00 14.22 ?  137 TRP A NE1 1 
ATOM   1022 C  CE2 . TRP A 1 137 ? 55.921 -1.012  44.816  1.00 15.21 ?  137 TRP A CE2 1 
ATOM   1023 C  CE3 . TRP A 1 137 ? 56.047 -2.640  43.025  1.00 15.81 ?  137 TRP A CE3 1 
ATOM   1024 C  CZ2 . TRP A 1 137 ? 54.568 -1.273  45.018  1.00 13.65 ?  137 TRP A CZ2 1 
ATOM   1025 C  CZ3 . TRP A 1 137 ? 54.711 -2.900  43.227  1.00 17.36 ?  137 TRP A CZ3 1 
ATOM   1026 C  CH2 . TRP A 1 137 ? 53.979 -2.224  44.216  1.00 16.45 ?  137 TRP A CH2 1 
ATOM   1027 N  N   . ASP A 1 138 ? 57.809 -1.111  40.294  1.00 19.26 ?  138 ASP A N   1 
ATOM   1028 C  CA  . ASP A 1 138 ? 56.764 -0.828  39.305  1.00 20.16 ?  138 ASP A CA  1 
ATOM   1029 C  C   . ASP A 1 138 ? 55.427 -1.380  39.786  1.00 19.18 ?  138 ASP A C   1 
ATOM   1030 O  O   . ASP A 1 138 ? 55.184 -2.589  39.719  1.00 21.68 ?  138 ASP A O   1 
ATOM   1031 C  CB  . ASP A 1 138 ? 57.134 -1.423  37.949  1.00 24.94 ?  138 ASP A CB  1 
ATOM   1032 C  CG  . ASP A 1 138 ? 56.219 -0.950  36.836  1.00 27.99 ?  138 ASP A CG  1 
ATOM   1033 O  OD1 . ASP A 1 138 ? 55.182 -0.291  37.113  1.00 24.51 ?  138 ASP A OD1 1 
ATOM   1034 O  OD2 . ASP A 1 138 ? 56.539 -1.252  35.666  1.00 34.66 -1 138 ASP A OD2 1 
ATOM   1035 N  N   . SER A 1 139 ? 54.541 -0.482  40.225  1.00 17.57 ?  139 SER A N   1 
ATOM   1036 C  CA  . SER A 1 139 ? 53.203 -0.862  40.669  1.00 16.62 ?  139 SER A CA  1 
ATOM   1037 C  C   . SER A 1 139 ? 52.235 -1.111  39.523  1.00 17.53 ?  139 SER A C   1 
ATOM   1038 O  O   . SER A 1 139 ? 51.113 -1.561  39.766  1.00 16.31 ?  139 SER A O   1 
ATOM   1039 C  CB  . SER A 1 139 ? 52.613 0.234   41.542  1.00 17.15 ?  139 SER A CB  1 
ATOM   1040 O  OG  . SER A 1 139 ? 52.272 1.329   40.710  1.00 18.41 ?  139 SER A OG  1 
ATOM   1041 N  N   . GLY A 1 140 ? 52.616 -0.797  38.290  1.00 17.52 ?  140 GLY A N   1 
ATOM   1042 C  CA  . GLY A 1 140 ? 51.669 -0.867  37.206  1.00 17.82 ?  140 GLY A CA  1 
ATOM   1043 C  C   . GLY A 1 140 ? 50.801 0.362   37.064  1.00 18.25 ?  140 GLY A C   1 
ATOM   1044 O  O   . GLY A 1 140 ? 50.005 0.433   36.124  1.00 19.89 ?  140 GLY A O   1 
ATOM   1045 N  N   . HIS A 1 141 ? 50.939 1.346   37.960  1.00 16.39 ?  141 HIS A N   1 
ATOM   1046 C  CA  . HIS A 1 141 ? 50.118 2.547   37.907  1.00 16.00 ?  141 HIS A CA  1 
ATOM   1047 C  C   . HIS A 1 141 ? 50.953 3.800   37.703  1.00 16.64 ?  141 HIS A C   1 
ATOM   1048 O  O   . HIS A 1 141 ? 50.478 4.902   37.969  1.00 19.76 ?  141 HIS A O   1 
ATOM   1049 C  CB  . HIS A 1 141 ? 49.268 2.661   39.170  1.00 18.28 ?  141 HIS A CB  1 
ATOM   1050 C  CG  . HIS A 1 141 ? 48.257 1.566   39.286  1.00 15.38 ?  141 HIS A CG  1 
ATOM   1051 N  ND1 . HIS A 1 141 ? 47.023 1.631   38.676  1.00 15.51 ?  141 HIS A ND1 1 
ATOM   1052 C  CD2 . HIS A 1 141 ? 48.316 0.358   39.894  1.00 18.67 ?  141 HIS A CD2 1 
ATOM   1053 C  CE1 . HIS A 1 141 ? 46.353 0.519   38.927  1.00 17.52 ?  141 HIS A CE1 1 
ATOM   1054 N  NE2 . HIS A 1 141 ? 47.120 -0.273  39.656  1.00 16.74 ?  141 HIS A NE2 1 
ATOM   1055 N  N   . GLY A 1 142 ? 52.169 3.651   37.211  1.00 18.03 ?  142 GLY A N   1 
ATOM   1056 C  CA  . GLY A 1 142 ? 53.014 4.790   36.958  1.00 19.82 ?  142 GLY A CA  1 
ATOM   1057 C  C   . GLY A 1 142 ? 53.816 5.191   38.175  1.00 21.41 ?  142 GLY A C   1 
ATOM   1058 O  O   . GLY A 1 142 ? 53.687 4.646   39.273  1.00 19.08 ?  142 GLY A O   1 
ATOM   1059 N  N   . ALA A 1 143 ? 54.682 6.171   37.961  1.00 20.43 ?  143 ALA A N   1 
ATOM   1060 C  CA  . ALA A 1 143 ? 55.510 6.674   39.049  1.00 19.55 ?  143 ALA A CA  1 
ATOM   1061 C  C   . ALA A 1 143 ? 55.694 8.168   38.817  1.00 21.50 ?  143 ALA A C   1 
ATOM   1062 O  O   . ALA A 1 143 ? 54.710 8.904   38.721  1.00 21.38 ?  143 ALA A O   1 
ATOM   1063 C  CB  . ALA A 1 143 ? 56.841 5.923   39.113  1.00 20.65 ?  143 ALA A CB  1 
ATOM   1064 N  N   . GLY A 1 144 ? 56.928 8.627   38.687  1.00 20.33 ?  144 GLY A N   1 
ATOM   1065 C  CA  . GLY A 1 144 ? 57.162 10.002  38.309  1.00 20.80 ?  144 GLY A CA  1 
ATOM   1066 C  C   . GLY A 1 144 ? 57.299 10.987  39.453  1.00 24.98 ?  144 GLY A C   1 
ATOM   1067 O  O   . GLY A 1 144 ? 57.629 12.154  39.206  1.00 21.49 ?  144 GLY A O   1 
ATOM   1068 N  N   . LEU A 1 145 ? 57.041 10.578  40.695  1.00 20.18 ?  145 LEU A N   1 
ATOM   1069 C  CA  . LEU A 1 145 ? 57.292 11.463  41.824  1.00 17.44 ?  145 LEU A CA  1 
ATOM   1070 C  C   . LEU A 1 145 ? 58.784 11.470  42.107  1.00 18.29 ?  145 LEU A C   1 
ATOM   1071 O  O   . LEU A 1 145 ? 59.375 10.415  42.330  1.00 17.47 ?  145 LEU A O   1 
ATOM   1072 C  CB  . LEU A 1 145 ? 56.515 11.019  43.061  1.00 16.14 ?  145 LEU A CB  1 
ATOM   1073 C  CG  . LEU A 1 145 ? 56.696 11.875  44.325  1.00 18.72 ?  145 LEU A CG  1 
ATOM   1074 C  CD1 . LEU A 1 145 ? 56.253 13.311  44.064  1.00 22.07 ?  145 LEU A CD1 1 
ATOM   1075 C  CD2 . LEU A 1 145 ? 55.922 11.251  45.487  1.00 20.58 ?  145 LEU A CD2 1 
ATOM   1076 N  N   . ARG A 1 146 ? 59.404 12.646  42.060  1.00 17.87 ?  146 ARG A N   1 
ATOM   1077 C  CA  . ARG A 1 146 ? 60.815 12.736  42.408  1.00 17.09 ?  146 ARG A CA  1 
ATOM   1078 C  C   . ARG A 1 146 ? 61.003 12.522  43.908  1.00 18.37 ?  146 ARG A C   1 
ATOM   1079 O  O   . ARG A 1 146 ? 60.330 13.181  44.712  1.00 17.77 ?  146 ARG A O   1 
ATOM   1080 C  CB  . ARG A 1 146 ? 61.384 14.091  41.998  1.00 19.64 ?  146 ARG A CB  1 
ATOM   1081 C  CG  . ARG A 1 146 ? 61.200 14.414  40.520  1.00 23.17 ?  146 ARG A CG  1 
ATOM   1082 C  CD  . ARG A 1 146 ? 61.837 15.774  40.196  1.00 30.32 ?  146 ARG A CD  1 
ATOM   1083 N  NE  . ARG A 1 146 ? 63.206 15.841  40.699  1.00 32.52 ?  146 ARG A NE  1 
ATOM   1084 C  CZ  . ARG A 1 146 ? 63.700 16.816  41.460  1.00 32.75 ?  146 ARG A CZ  1 
ATOM   1085 N  NH1 . ARG A 1 146 ? 62.947 17.849  41.829  1.00 32.85 ?  146 ARG A NH1 1 
ATOM   1086 N  NH2 . ARG A 1 146 ? 64.966 16.757  41.852  1.00 35.57 ?  146 ARG A NH2 1 
ATOM   1087 N  N   . PRO A 1 147 ? 61.895 11.623  44.328  1.00 18.85 ?  147 PRO A N   1 
ATOM   1088 C  CA  . PRO A 1 147 ? 62.104 11.443  45.774  1.00 19.59 ?  147 PRO A CA  1 
ATOM   1089 C  C   . PRO A 1 147 ? 62.561 12.714  46.458  1.00 19.33 ?  147 PRO A C   1 
ATOM   1090 O  O   . PRO A 1 147 ? 62.279 12.908  47.644  1.00 16.28 ?  147 PRO A O   1 
ATOM   1091 C  CB  . PRO A 1 147 ? 63.173 10.342  45.850  1.00 24.88 ?  147 PRO A CB  1 
ATOM   1092 C  CG  . PRO A 1 147 ? 63.138 9.661   44.525  1.00 26.69 ?  147 PRO A CG  1 
ATOM   1093 C  CD  . PRO A 1 147 ? 62.661 10.659  43.518  1.00 20.70 ?  147 PRO A CD  1 
ATOM   1094 N  N   . GLU A 1 148 ? 63.252 13.597  45.730  1.00 17.25 ?  148 GLU A N   1 
ATOM   1095 C  CA  . GLU A 1 148 ? 63.624 14.908  46.253  1.00 20.33 ?  148 GLU A CA  1 
ATOM   1096 C  C   . GLU A 1 148 ? 62.423 15.791  46.547  1.00 18.84 ?  148 GLU A C   1 
ATOM   1097 O  O   . GLU A 1 148 ? 62.586 16.840  47.193  1.00 19.58 ?  148 GLU A O   1 
ATOM   1098 C  CB  . GLU A 1 148 ? 64.530 15.622  45.247  1.00 22.71 ?  148 GLU A CB  1 
ATOM   1099 C  CG  . GLU A 1 148 ? 65.897 14.970  45.068  1.00 27.37 ?  148 GLU A CG  1 
ATOM   1100 C  CD  . GLU A 1 148 ? 65.907 13.816  44.062  1.00 31.66 ?  148 GLU A CD  1 
ATOM   1101 O  OE1 . GLU A 1 148 ? 64.847 13.487  43.481  1.00 26.04 ?  148 GLU A OE1 1 
ATOM   1102 O  OE2 . GLU A 1 148 ? 66.995 13.233  43.856  1.00 36.19 -1 148 GLU A OE2 1 
ATOM   1103 N  N   . GLN A 1 149 ? 61.236 15.426  46.054  1.00 17.01 ?  149 GLN A N   1 
ATOM   1104 C  CA  . GLN A 1 149 ? 60.021 16.181  46.314  1.00 14.83 ?  149 GLN A CA  1 
ATOM   1105 C  C   . GLN A 1 149 ? 59.071 15.442  47.249  1.00 16.21 ?  149 GLN A C   1 
ATOM   1106 O  O   . GLN A 1 149 ? 57.910 15.830  47.364  1.00 17.25 ?  149 GLN A O   1 
ATOM   1107 C  CB  . GLN A 1 149 ? 59.324 16.527  44.992  1.00 16.91 ?  149 GLN A CB  1 
ATOM   1108 C  CG  . GLN A 1 149 ? 60.166 17.514  44.175  1.00 22.01 ?  149 GLN A CG  1 
ATOM   1109 C  CD  . GLN A 1 149 ? 59.638 17.817  42.782  1.00 31.77 ?  149 GLN A CD  1 
ATOM   1110 O  OE1 . GLN A 1 149 ? 60.428 17.980  41.847  1.00 34.22 ?  149 GLN A OE1 1 
ATOM   1111 N  NE2 . GLN A 1 149 ? 58.317 17.937  42.638  1.00 29.57 ?  149 GLN A NE2 1 
ATOM   1112 N  N   . ALA A 1 150 ? 59.536 14.391  47.918  1.00 14.22 ?  150 ALA A N   1 
ATOM   1113 C  CA  . ALA A 1 150 ? 58.726 13.657  48.888  1.00 15.95 ?  150 ALA A CA  1 
ATOM   1114 C  C   . ALA A 1 150 ? 59.296 13.890  50.279  1.00 17.41 ?  150 ALA A C   1 
ATOM   1115 O  O   . ALA A 1 150 ? 60.515 13.767  50.480  1.00 19.26 ?  150 ALA A O   1 
ATOM   1116 C  CB  . ALA A 1 150 ? 58.702 12.160  48.554  1.00 14.80 ?  150 ALA A CB  1 
ATOM   1117 N  N   . VAL A 1 151 ? 58.434 14.232  51.238  1.00 12.23 ?  151 VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 151 ? 58.877 14.466  52.616  1.00 12.41 ?  151 VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 151 ? 58.045 13.599  53.546  1.00 12.58 ?  151 VAL A C   1 
ATOM   1120 O  O   . VAL A 1 151 ? 56.824 13.768  53.626  1.00 12.28 ?  151 VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 151 ? 58.766 15.944  53.028  1.00 16.83 ?  151 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 151 ? 59.246 16.111  54.463  1.00 13.12 ?  151 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 151 ? 59.589 16.818  52.092  1.00 16.64 ?  151 VAL A CG2 1 
ATOM   1124 N  N   . LEU A 1 152 ? 58.706 12.689  54.260  1.00 12.65 ?  152 LEU A N   1 
ATOM   1125 C  CA  . LEU A 1 152 ? 58.024 11.878  55.257  1.00 13.14 ?  152 LEU A CA  1 
ATOM   1126 C  C   . LEU A 1 152 ? 57.900 12.704  56.525  1.00 14.31 ?  152 LEU A C   1 
ATOM   1127 O  O   . LEU A 1 152 ? 58.890 13.267  57.000  1.00 15.60 ?  152 LEU A O   1 
ATOM   1128 C  CB  . LEU A 1 152 ? 58.803 10.596  55.534  1.00 11.30 ?  152 LEU A CB  1 
ATOM   1129 C  CG  . LEU A 1 152 ? 58.588 9.479   54.505  1.00 13.21 ?  152 LEU A CG  1 
ATOM   1130 C  CD1 . LEU A 1 152 ? 59.629 8.395   54.666  1.00 13.16 ?  152 LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A 1 152 ? 57.134 8.919   54.623  1.00 13.09 ?  152 LEU A CD2 1 
ATOM   1132 N  N   . VAL A 1 153 ? 56.689 12.788  57.067  1.00 9.83  ?  153 VAL A N   1 
ATOM   1133 C  CA  . VAL A 1 153 ? 56.425 13.640  58.219  1.00 13.44 ?  153 VAL A CA  1 
ATOM   1134 C  C   . VAL A 1 153 ? 55.837 12.768  59.305  1.00 11.70 ?  153 VAL A C   1 
ATOM   1135 O  O   . VAL A 1 153 ? 54.797 12.132  59.100  1.00 11.68 ?  153 VAL A O   1 
ATOM   1136 C  CB  . VAL A 1 153 ? 55.490 14.812  57.876  1.00 13.61 ?  153 VAL A CB  1 
ATOM   1137 C  CG1 . VAL A 1 153 ? 55.168 15.654  59.142  1.00 14.60 ?  153 VAL A CG1 1 
ATOM   1138 C  CG2 . VAL A 1 153 ? 56.090 15.691  56.726  1.00 10.94 ?  153 VAL A CG2 1 
ATOM   1139 N  N   . GLY A 1 154 ? 56.520 12.716  60.453  1.00 11.40 ?  154 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 154 ? 56.045 11.972  61.592  1.00 14.61 ?  154 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 154 ? 56.495 10.533  61.651  1.00 12.20 ?  154 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 154 ? 56.109 9.829   62.587  1.00 12.46 ?  154 GLY A O   1 
ATOM   1143 N  N   . SER A 1 155 ? 57.269 10.071  60.672  1.00 10.65 ?  155 SER A N   1 
ATOM   1144 C  CA  . SER A 1 155 ? 57.704 8.679   60.633  1.00 10.96 ?  155 SER A CA  1 
ATOM   1145 C  C   . SER A 1 155 ? 58.756 8.431   61.704  1.00 17.06 ?  155 SER A C   1 
ATOM   1146 O  O   . SER A 1 155 ? 59.569 9.305   62.007  1.00 18.31 ?  155 SER A O   1 
ATOM   1147 C  CB  . SER A 1 155 ? 58.270 8.354   59.256  1.00 13.34 ?  155 SER A CB  1 
ATOM   1148 O  OG  . SER A 1 155 ? 57.417 8.877   58.259  1.00 13.88 ?  155 SER A OG  1 
ATOM   1149 N  N   . ARG A 1 156 ? 58.740 7.240   62.290  1.00 13.08 ?  156 ARG A N   1 
ATOM   1150 C  CA  . ARG A 1 156 ? 59.669 6.962   63.381  1.00 14.90 ?  156 ARG A CA  1 
ATOM   1151 C  C   . ARG A 1 156 ? 59.878 5.462   63.464  1.00 18.10 ?  156 ARG A C   1 
ATOM   1152 O  O   . ARG A 1 156 ? 59.100 4.677   62.910  1.00 15.92 ?  156 ARG A O   1 
ATOM   1153 C  CB  . ARG A 1 156 ? 59.162 7.516   64.724  1.00 19.65 ?  156 ARG A CB  1 
ATOM   1154 C  CG  . ARG A 1 156 ? 57.937 6.796   65.293  1.00 21.83 ?  156 ARG A CG  1 
ATOM   1155 C  CD  . ARG A 1 156 ? 56.723 7.713   65.239  1.00 22.42 ?  156 ARG A CD  1 
ATOM   1156 N  NE  . ARG A 1 156 ? 55.480 7.190   65.812  1.00 21.71 ?  156 ARG A NE  1 
ATOM   1157 C  CZ  . ARG A 1 156 ? 54.284 7.668   65.461  1.00 22.08 ?  156 ARG A CZ  1 
ATOM   1158 N  NH1 . ARG A 1 156 ? 54.226 8.672   64.565  1.00 13.32 ?  156 ARG A NH1 1 
ATOM   1159 N  NH2 . ARG A 1 156 ? 53.157 7.180   66.008  1.00 18.97 ?  156 ARG A NH2 1 
ATOM   1160 N  N   . ASP A 1 157 ? 60.947 5.076   64.158  1.00 18.93 ?  157 ASP A N   1 
ATOM   1161 C  CA  . ASP A 1 157 ? 61.273 3.664   64.373  1.00 22.96 ?  157 ASP A CA  1 
ATOM   1162 C  C   . ASP A 1 157 ? 61.250 2.896   63.054  1.00 23.40 ?  157 ASP A C   1 
ATOM   1163 O  O   . ASP A 1 157 ? 60.563 1.881   62.909  1.00 20.98 ?  157 ASP A O   1 
ATOM   1164 C  CB  . ASP A 1 157 ? 60.324 3.024   65.392  1.00 17.76 ?  157 ASP A CB  1 
ATOM   1165 C  CG  . ASP A 1 157 ? 60.398 3.675   66.755  1.00 24.31 ?  157 ASP A CG  1 
ATOM   1166 O  OD1 . ASP A 1 157 ? 61.492 4.099   67.154  1.00 25.25 ?  157 ASP A OD1 1 
ATOM   1167 O  OD2 . ASP A 1 157 ? 59.359 3.764   67.446  1.00 26.62 -1 157 ASP A OD2 1 
ATOM   1168 N  N   . ILE A 1 158 ? 62.005 3.398   62.074  1.00 19.42 ?  158 ILE A N   1 
ATOM   1169 C  CA  . ILE A 1 158 ? 62.022 2.818   60.739  1.00 21.96 ?  158 ILE A CA  1 
ATOM   1170 C  C   . ILE A 1 158 ? 63.110 1.753   60.680  1.00 25.33 ?  158 ILE A C   1 
ATOM   1171 O  O   . ILE A 1 158 ? 64.235 1.977   61.141  1.00 27.43 ?  158 ILE A O   1 
ATOM   1172 C  CB  . ILE A 1 158 ? 62.252 3.898   59.666  1.00 20.88 ?  158 ILE A CB  1 
ATOM   1173 C  CG1 . ILE A 1 158 ? 61.132 4.945   59.690  1.00 23.45 ?  158 ILE A CG1 1 
ATOM   1174 C  CG2 . ILE A 1 158 ? 62.330 3.272   58.285  1.00 21.36 ?  158 ILE A CG2 1 
ATOM   1175 C  CD1 . ILE A 1 158 ? 61.332 6.073   58.671  1.00 24.29 ?  158 ILE A CD1 1 
ATOM   1176 N  N   . ASP A 1 159 ? 62.771 0.597   60.110  1.00 25.68 ?  159 ASP A N   1 
ATOM   1177 C  CA  . ASP A 1 159 ? 63.743 -0.474  59.916  1.00 33.06 ?  159 ASP A CA  1 
ATOM   1178 C  C   . ASP A 1 159 ? 65.004 0.057   59.244  1.00 34.21 ?  159 ASP A C   1 
ATOM   1179 O  O   . ASP A 1 159 ? 64.940 0.874   58.324  1.00 29.48 ?  159 ASP A O   1 
ATOM   1180 C  CB  . ASP A 1 159 ? 63.130 -1.591  59.070  1.00 29.98 ?  159 ASP A CB  1 
ATOM   1181 C  CG  . ASP A 1 159 ? 64.162 -2.608  58.606  1.00 42.82 ?  159 ASP A CG  1 
ATOM   1182 O  OD1 . ASP A 1 159 ? 64.903 -2.314  57.642  1.00 41.48 -1 159 ASP A OD1 1 
ATOM   1183 O  OD2 . ASP A 1 159 ? 64.231 -3.702  59.209  1.00 44.41 -1 159 ASP A OD2 1 
ATOM   1184 N  N   . GLU A 1 160 ? 66.158 -0.421  59.712  1.00 36.38 ?  160 GLU A N   1 
ATOM   1185 C  CA  . GLU A 1 160 ? 67.425 0.086   59.193  1.00 39.15 ?  160 GLU A CA  1 
ATOM   1186 C  C   . GLU A 1 160 ? 67.521 -0.093  57.680  1.00 31.97 ?  160 GLU A C   1 
ATOM   1187 O  O   . GLU A 1 160 ? 67.992 0.804   56.972  1.00 33.99 ?  160 GLU A O   1 
ATOM   1188 C  CB  . GLU A 1 160 ? 68.589 -0.606  59.906  1.00 38.94 ?  160 GLU A CB  1 
ATOM   1189 C  CG  . GLU A 1 160 ? 68.879 -0.050  61.295  1.00 51.12 ?  160 GLU A CG  1 
ATOM   1190 C  CD  . GLU A 1 160 ? 67.784 -0.364  62.315  1.00 56.13 ?  160 GLU A CD  1 
ATOM   1191 O  OE1 . GLU A 1 160 ? 67.564 0.472   63.221  1.00 57.89 ?  160 GLU A OE1 1 
ATOM   1192 O  OE2 . GLU A 1 160 ? 67.145 -1.439  62.211  1.00 54.20 -1 160 GLU A OE2 1 
ATOM   1193 N  N   . GLY A 1 161 ? 67.044 -1.226  57.163  1.00 33.82 ?  161 GLY A N   1 
ATOM   1194 C  CA  . GLY A 1 161 ? 67.127 -1.473  55.730  1.00 30.24 ?  161 GLY A CA  1 
ATOM   1195 C  C   . GLY A 1 161 ? 66.218 -0.570  54.912  1.00 34.38 ?  161 GLY A C   1 
ATOM   1196 O  O   . GLY A 1 161 ? 66.581 -0.136  53.814  1.00 29.01 ?  161 GLY A O   1 
ATOM   1197 N  N   . GLU A 1 162 ? 65.018 -0.293  55.418  1.00 28.33 ?  162 GLU A N   1 
ATOM   1198 C  CA  . GLU A 1 162 ? 64.145 0.653   54.733  1.00 28.43 ?  162 GLU A CA  1 
ATOM   1199 C  C   . GLU A 1 162 ? 64.671 2.072   54.880  1.00 21.85 ?  162 GLU A C   1 
ATOM   1200 O  O   . GLU A 1 162 ? 64.624 2.861   53.926  1.00 22.25 ?  162 GLU A O   1 
ATOM   1201 C  CB  . GLU A 1 162 ? 62.720 0.533   55.278  1.00 22.93 ?  162 GLU A CB  1 
ATOM   1202 C  CG  . GLU A 1 162 ? 61.729 1.536   54.713  1.00 23.24 ?  162 GLU A CG  1 
ATOM   1203 C  CD  . GLU A 1 162 ? 60.323 1.302   55.246  1.00 23.60 ?  162 GLU A CD  1 
ATOM   1204 O  OE1 . GLU A 1 162 ? 60.156 0.404   56.098  1.00 25.84 ?  162 GLU A OE1 1 
ATOM   1205 O  OE2 . GLU A 1 162 ? 59.390 2.002   54.804  1.00 19.11 -1 162 GLU A OE2 1 
ATOM   1206 N  N   . ARG A 1 163 ? 65.194 2.412   56.065  1.00 21.53 ?  163 ARG A N   1 
ATOM   1207 C  CA  . ARG A 1 163 ? 65.729 3.753   56.274  1.00 24.78 ?  163 ARG A CA  1 
ATOM   1208 C  C   . ARG A 1 163 ? 66.897 4.023   55.341  1.00 30.06 ?  163 ARG A C   1 
ATOM   1209 O  O   . ARG A 1 163 ? 67.162 5.178   54.998  1.00 29.64 ?  163 ARG A O   1 
ATOM   1210 C  CB  . ARG A 1 163 ? 66.158 3.932   57.734  1.00 27.31 ?  163 ARG A CB  1 
ATOM   1211 C  CG  . ARG A 1 163 ? 66.556 5.345   58.120  1.00 27.76 ?  163 ARG A CG  1 
ATOM   1212 C  CD  . ARG A 1 163 ? 65.327 6.233   58.348  1.00 33.88 ?  163 ARG A CD  1 
ATOM   1213 N  NE  . ARG A 1 163 ? 65.656 7.642   58.575  1.00 35.62 ?  163 ARG A NE  1 
ATOM   1214 C  CZ  . ARG A 1 163 ? 66.014 8.501   57.621  1.00 37.10 ?  163 ARG A CZ  1 
ATOM   1215 N  NH1 . ARG A 1 163 ? 66.105 8.102   56.356  1.00 32.24 ?  163 ARG A NH1 1 
ATOM   1216 N  NH2 . ARG A 1 163 ? 66.286 9.765   57.933  1.00 33.14 ?  163 ARG A NH2 1 
ATOM   1217 N  N   . GLU A 1 164 ? 67.590 2.967   54.909  1.00 29.04 ?  164 GLU A N   1 
ATOM   1218 C  CA  . GLU A 1 164 ? 68.695 3.139   53.974  1.00 34.46 ?  164 GLU A CA  1 
ATOM   1219 C  C   . GLU A 1 164 ? 68.188 3.487   52.584  1.00 31.63 ?  164 GLU A C   1 
ATOM   1220 O  O   . GLU A 1 164 ? 68.732 4.384   51.925  1.00 28.78 ?  164 GLU A O   1 
ATOM   1221 C  CB  . GLU A 1 164 ? 69.548 1.873   53.928  1.00 41.33 ?  164 GLU A CB  1 
ATOM   1222 C  CG  . GLU A 1 164 ? 70.757 2.004   53.027  1.00 45.69 ?  164 GLU A CG  1 
ATOM   1223 C  CD  . GLU A 1 164 ? 71.583 3.231   53.370  1.00 51.41 ?  164 GLU A CD  1 
ATOM   1224 O  OE1 . GLU A 1 164 ? 72.307 3.718   52.480  1.00 52.21 ?  164 GLU A OE1 1 
ATOM   1225 O  OE2 . GLU A 1 164 ? 71.517 3.712   54.524  1.00 55.61 -1 164 GLU A OE2 1 
ATOM   1226 N  N   . LEU A 1 165 ? 67.152 2.778   52.115  1.00 27.23 ?  165 LEU A N   1 
ATOM   1227 C  CA  . LEU A 1 165 ? 66.527 3.121   50.842  1.00 23.34 ?  165 LEU A CA  1 
ATOM   1228 C  C   . LEU A 1 165 ? 66.034 4.561   50.849  1.00 22.83 ?  165 LEU A C   1 
ATOM   1229 O  O   . LEU A 1 165 ? 66.188 5.283   49.855  1.00 21.91 ?  165 LEU A O   1 
ATOM   1230 C  CB  . LEU A 1 165 ? 65.360 2.179   50.554  1.00 27.45 ?  165 LEU A CB  1 
ATOM   1231 C  CG  . LEU A 1 165 ? 65.576 0.782   49.985  1.00 33.66 ?  165 LEU A CG  1 
ATOM   1232 C  CD1 . LEU A 1 165 ? 64.219 0.189   49.662  1.00 29.54 ?  165 LEU A CD1 1 
ATOM   1233 C  CD2 . LEU A 1 165 ? 66.461 0.833   48.752  1.00 35.29 ?  165 LEU A CD2 1 
ATOM   1234 N  N   . ILE A 1 166 ? 65.424 4.986   51.961  1.00 20.30 ?  166 ILE A N   1 
ATOM   1235 C  CA  . ILE A 1 166 ? 64.908 6.353   52.070  1.00 18.44 ?  166 ILE A CA  1 
ATOM   1236 C  C   . ILE A 1 166 ? 66.041 7.361   51.904  1.00 23.89 ?  166 ILE A C   1 
ATOM   1237 O  O   . ILE A 1 166 ? 65.931 8.322   51.134  1.00 20.61 ?  166 ILE A O   1 
ATOM   1238 C  CB  . ILE A 1 166 ? 64.165 6.540   53.409  1.00 16.36 ?  166 ILE A CB  1 
ATOM   1239 C  CG1 . ILE A 1 166 ? 62.839 5.776   53.387  1.00 15.87 ?  166 ILE A CG1 1 
ATOM   1240 C  CG2 . ILE A 1 166 ? 63.916 8.012   53.732  1.00 17.21 ?  166 ILE A CG2 1 
ATOM   1241 C  CD1 . ILE A 1 166 ? 62.193 5.606   54.753  1.00 17.02 ?  166 ILE A CD1 1 
ATOM   1242 N  N   . ARG A 1 167 ? 67.157 7.152   52.607  1.00 22.72 ?  167 ARG A N   1 
ATOM   1243 C  CA  . ARG A 1 167 ? 68.222 8.150   52.515  1.00 25.92 ?  167 ARG A CA  1 
ATOM   1244 C  C   . ARG A 1 167 ? 68.913 8.093   51.155  1.00 27.37 ?  167 ARG A C   1 
ATOM   1245 O  O   . ARG A 1 167 ? 69.237 9.140   50.579  1.00 28.47 ?  167 ARG A O   1 
ATOM   1246 C  CB  . ARG A 1 167 ? 69.222 7.999   53.666  1.00 28.63 ?  167 ARG A CB  1 
ATOM   1247 C  CG  . ARG A 1 167 ? 69.688 6.604   53.972  1.00 37.97 ?  167 ARG A CG  1 
ATOM   1248 C  CD  . ARG A 1 167 ? 70.669 6.613   55.148  1.00 43.37 ?  167 ARG A CD  1 
ATOM   1249 N  NE  . ARG A 1 167 ? 70.186 7.426   56.265  1.00 41.92 ?  167 ARG A NE  1 
ATOM   1250 C  CZ  . ARG A 1 167 ? 70.037 6.975   57.507  1.00 40.99 ?  167 ARG A CZ  1 
ATOM   1251 N  NH1 . ARG A 1 167 ? 70.344 5.718   57.797  1.00 45.72 ?  167 ARG A NH1 1 
ATOM   1252 N  NH2 . ARG A 1 167 ? 69.600 7.786   58.461  1.00 39.42 ?  167 ARG A NH2 1 
ATOM   1253 N  N   . LYS A 1 168 ? 69.100 6.891   50.606  1.00 27.15 ?  168 LYS A N   1 
ATOM   1254 C  CA  . LYS A 1 168 ? 69.706 6.754   49.281  1.00 29.57 ?  168 LYS A CA  1 
ATOM   1255 C  C   . LYS A 1 168 ? 68.878 7.455   48.208  1.00 27.52 ?  168 LYS A C   1 
ATOM   1256 O  O   . LYS A 1 168 ? 69.422 8.110   47.308  1.00 27.04 ?  168 LYS A O   1 
ATOM   1257 C  CB  . LYS A 1 168 ? 69.883 5.274   48.941  1.00 28.11 ?  168 LYS A CB  1 
ATOM   1258 C  CG  . LYS A 1 168 ? 71.085 4.614   49.606  1.00 41.10 ?  168 LYS A CG  1 
ATOM   1259 C  CD  . LYS A 1 168 ? 72.394 5.278   49.176  1.00 46.36 ?  168 LYS A CD  1 
ATOM   1260 C  CE  . LYS A 1 168 ? 73.585 4.815   50.018  1.00 43.16 ?  168 LYS A CE  1 
ATOM   1261 N  NZ  . LYS A 1 168 ? 74.427 3.785   49.341  1.00 45.31 ?  168 LYS A NZ  1 
ATOM   1262 N  N   . ALA A 1 169 ? 67.556 7.333   48.283  1.00 24.15 ?  169 ALA A N   1 
ATOM   1263 C  CA  . ALA A 1 169 ? 66.704 7.991   47.306  1.00 18.72 ?  169 ALA A CA  1 
ATOM   1264 C  C   . ALA A 1 169 ? 66.645 9.505   47.490  1.00 21.95 ?  169 ALA A C   1 
ATOM   1265 O  O   . ALA A 1 169 ? 66.261 10.209  46.552  1.00 23.57 ?  169 ALA A O   1 
ATOM   1266 C  CB  . ALA A 1 169 ? 65.291 7.409   47.382  1.00 21.27 ?  169 ALA A CB  1 
ATOM   1267 N  N   . GLY A 1 170 ? 66.991 10.021  48.665  1.00 21.05 ?  170 GLY A N   1 
ATOM   1268 C  CA  . GLY A 1 170 ? 66.880 11.447  48.906  1.00 25.85 ?  170 GLY A CA  1 
ATOM   1269 C  C   . GLY A 1 170 ? 65.555 11.899  49.475  1.00 22.97 ?  170 GLY A C   1 
ATOM   1270 O  O   . GLY A 1 170 ? 65.226 13.089  49.392  1.00 19.75 ?  170 GLY A O   1 
ATOM   1271 N  N   . VAL A 1 171 ? 64.776 10.983  50.035  1.00 23.80 ?  171 VAL A N   1 
ATOM   1272 C  CA  . VAL A 1 171 ? 63.554 11.336  50.746  1.00 19.43 ?  171 VAL A CA  1 
ATOM   1273 C  C   . VAL A 1 171 ? 63.928 11.878  52.118  1.00 19.98 ?  171 VAL A C   1 
ATOM   1274 O  O   . VAL A 1 171 ? 64.658 11.230  52.876  1.00 23.41 ?  171 VAL A O   1 
ATOM   1275 C  CB  . VAL A 1 171 ? 62.636 10.111  50.861  1.00 17.75 ?  171 VAL A CB  1 
ATOM   1276 C  CG1 . VAL A 1 171 ? 61.394 10.425  51.697  1.00 16.42 ?  171 VAL A CG1 1 
ATOM   1277 C  CG2 . VAL A 1 171 ? 62.265 9.606   49.471  1.00 20.13 ?  171 VAL A CG2 1 
ATOM   1278 N  N   . ARG A 1 172 ? 63.410 13.058  52.453  1.00 17.59 ?  172 ARG A N   1 
ATOM   1279 C  CA  . ARG A 1 172 ? 63.647 13.660  53.754  1.00 14.72 ?  172 ARG A CA  1 
ATOM   1280 C  C   . ARG A 1 172 ? 62.657 13.104  54.773  1.00 18.79 ?  172 ARG A C   1 
ATOM   1281 O  O   . ARG A 1 172 ? 61.522 12.755  54.441  1.00 18.23 ?  172 ARG A O   1 
ATOM   1282 C  CB  . ARG A 1 172 ? 63.511 15.180  53.662  1.00 20.25 ?  172 ARG A CB  1 
ATOM   1283 C  CG  . ARG A 1 172 ? 64.638 15.834  52.849  1.00 23.63 ?  172 ARG A CG  1 
ATOM   1284 C  CD  . ARG A 1 172 ? 64.279 17.262  52.433  1.00 24.33 ?  172 ARG A CD  1 
ATOM   1285 N  NE  . ARG A 1 172 ? 63.382 17.269  51.281  1.00 21.63 ?  172 ARG A NE  1 
ATOM   1286 C  CZ  . ARG A 1 172 ? 62.667 18.320  50.902  1.00 20.78 ?  172 ARG A CZ  1 
ATOM   1287 N  NH1 . ARG A 1 172 ? 62.764 19.455  51.583  1.00 26.80 ?  172 ARG A NH1 1 
ATOM   1288 N  NH2 . ARG A 1 172 ? 61.867 18.247  49.848  1.00 19.14 ?  172 ARG A NH2 1 
ATOM   1289 N  N   . VAL A 1 173 ? 63.093 13.016  56.023  1.00 17.11 ?  173 VAL A N   1 
ATOM   1290 C  CA  . VAL A 1 173 ? 62.226 12.544  57.097  1.00 15.64 ?  173 VAL A CA  1 
ATOM   1291 C  C   . VAL A 1 173 ? 62.205 13.594  58.195  1.00 22.76 ?  173 VAL A C   1 
ATOM   1292 O  O   . VAL A 1 173 ? 63.266 14.020  58.663  1.00 19.50 ?  173 VAL A O   1 
ATOM   1293 C  CB  . VAL A 1 173 ? 62.703 11.189  57.658  1.00 17.63 ?  173 VAL A CB  1 
ATOM   1294 C  CG1 . VAL A 1 173 ? 61.805 10.757  58.812  1.00 17.97 ?  173 VAL A CG1 1 
ATOM   1295 C  CG2 . VAL A 1 173 ? 62.719 10.134  56.544  1.00 20.57 ?  173 VAL A CG2 1 
ATOM   1296 N  N   . ILE A 1 174 ? 61.008 13.998  58.611  1.00 16.08 ?  174 ILE A N   1 
ATOM   1297 C  CA  . ILE A 1 174 ? 60.804 14.909  59.729  1.00 15.25 ?  174 ILE A CA  1 
ATOM   1298 C  C   . ILE A 1 174 ? 60.062 14.157  60.831  1.00 17.65 ?  174 ILE A C   1 
ATOM   1299 O  O   . ILE A 1 174 ? 58.835 14.026  60.789  1.00 15.73 ?  174 ILE A O   1 
ATOM   1300 C  CB  . ILE A 1 174 ? 60.018 16.161  59.286  1.00 14.62 ?  174 ILE A CB  1 
ATOM   1301 C  CG1 . ILE A 1 174 ? 60.747 16.877  58.146  1.00 18.12 ?  174 ILE A CG1 1 
ATOM   1302 C  CG2 . ILE A 1 174 ? 59.778 17.118  60.459  1.00 14.27 ?  174 ILE A CG2 1 
ATOM   1303 C  CD1 . ILE A 1 174 ? 60.009 18.063  57.586  1.00 21.15 ?  174 ILE A CD1 1 
ATOM   1304 N  N   . PRO A 1 175 ? 60.761 13.681  61.867  1.00 18.06 ?  175 PRO A N   1 
ATOM   1305 C  CA  . PRO A 1 175 ? 60.103 12.871  62.920  1.00 14.04 ?  175 PRO A CA  1 
ATOM   1306 C  C   . PRO A 1 175 ? 59.147 13.719  63.740  1.00 17.29 ?  175 PRO A C   1 
ATOM   1307 O  O   . PRO A 1 175 ? 59.209 14.953  63.675  1.00 15.63 ?  175 PRO A O   1 
ATOM   1308 C  CB  . PRO A 1 175 ? 61.282 12.373  63.778  1.00 19.31 ?  175 PRO A CB  1 
ATOM   1309 C  CG  . PRO A 1 175 ? 62.374 13.382  63.533  1.00 23.65 ?  175 PRO A CG  1 
ATOM   1310 C  CD  . PRO A 1 175 ? 62.215 13.772  62.078  1.00 21.03 ?  175 PRO A CD  1 
ATOM   1311 N  N   . PRO A 1 176 ? 58.258 13.090  64.529  1.00 16.73 ?  176 PRO A N   1 
ATOM   1312 C  CA  . PRO A 1 176 ? 57.210 13.852  65.239  1.00 14.93 ?  176 PRO A CA  1 
ATOM   1313 C  C   . PRO A 1 176 ? 57.706 15.026  66.064  1.00 18.05 ?  176 PRO A C   1 
ATOM   1314 O  O   . PRO A 1 176 ? 57.076 16.092  66.055  1.00 18.33 ?  176 PRO A O   1 
ATOM   1315 C  CB  . PRO A 1 176 ? 56.571 12.789  66.145  1.00 19.62 ?  176 PRO A CB  1 
ATOM   1316 C  CG  . PRO A 1 176 ? 56.794 11.508  65.422  1.00 15.31 ?  176 PRO A CG  1 
ATOM   1317 C  CD  . PRO A 1 176 ? 58.113 11.630  64.720  1.00 15.63 ?  176 PRO A CD  1 
ATOM   1318 N  N   . GLY A 1 177 ? 58.810 14.860  66.791  1.00 16.15 ?  177 GLY A N   1 
ATOM   1319 C  CA  . GLY A 1 177 ? 59.278 15.938  67.651  1.00 20.79 ?  177 GLY A CA  1 
ATOM   1320 C  C   . GLY A 1 177 ? 59.871 17.108  66.904  1.00 17.87 ?  177 GLY A C   1 
ATOM   1321 O  O   . GLY A 1 177 ? 60.057 18.176  67.500  1.00 17.85 ?  177 GLY A O   1 
ATOM   1322 N  N   . GLU A 1 178 ? 60.140 16.938  65.611  1.00 16.48 ?  178 GLU A N   1 
ATOM   1323 C  CA  . GLU A 1 178 ? 60.618 18.004  64.753  1.00 14.24 ?  178 GLU A CA  1 
ATOM   1324 C  C   . GLU A 1 178 ? 59.537 18.547  63.828  1.00 21.16 ?  178 GLU A C   1 
ATOM   1325 O  O   . GLU A 1 178 ? 59.766 19.567  63.174  1.00 16.89 ?  178 GLU A O   1 
ATOM   1326 C  CB  . GLU A 1 178 ? 61.806 17.503  63.925  1.00 18.03 ?  178 GLU A CB  1 
ATOM   1327 C  CG  . GLU A 1 178 ? 63.029 17.154  64.770  1.00 20.60 ?  178 GLU A CG  1 
ATOM   1328 C  CD  . GLU A 1 178 ? 64.188 16.606  63.948  1.00 32.07 ?  178 GLU A CD  1 
ATOM   1329 O  OE1 . GLU A 1 178 ? 64.235 16.854  62.728  1.00 36.28 ?  178 GLU A OE1 1 
ATOM   1330 O  OE2 . GLU A 1 178 ? 65.057 15.930  64.535  1.00 40.74 -1 178 GLU A OE2 1 
ATOM   1331 N  N   . ALA A 1 179 ? 58.359 17.917  63.801  1.00 14.36 ?  179 ALA A N   1 
ATOM   1332 C  CA  . ALA A 1 179 ? 57.315 18.212  62.815  1.00 18.20 ?  179 ALA A CA  1 
ATOM   1333 C  C   . ALA A 1 179 ? 56.415 19.368  63.265  1.00 18.30 ?  179 ALA A C   1 
ATOM   1334 O  O   . ALA A 1 179 ? 55.206 19.231  63.450  1.00 19.92 ?  179 ALA A O   1 
ATOM   1335 C  CB  . ALA A 1 179 ? 56.495 16.952  62.539  1.00 17.29 ?  179 ALA A CB  1 
ATOM   1336 N  N   . THR A 1 180 ? 57.031 20.533  63.443  1.00 17.35 ?  180 THR A N   1 
ATOM   1337 C  CA  . THR A 1 180 ? 56.284 21.760  63.647  1.00 19.93 ?  180 THR A CA  1 
ATOM   1338 C  C   . THR A 1 180 ? 55.783 22.281  62.306  1.00 21.62 ?  180 THR A C   1 
ATOM   1339 O  O   . THR A 1 180 ? 56.279 21.898  61.244  1.00 21.05 ?  180 THR A O   1 
ATOM   1340 C  CB  . THR A 1 180 ? 57.162 22.827  64.286  1.00 20.86 ?  180 THR A CB  1 
ATOM   1341 O  OG1 . THR A 1 180 ? 58.213 23.166  63.363  1.00 20.91 ?  180 THR A OG1 1 
ATOM   1342 C  CG2 . THR A 1 180 ? 57.773 22.288  65.558  1.00 20.48 ?  180 THR A CG2 1 
ATOM   1343 N  N   . ALA A 1 181 ? 54.813 23.198  62.366  1.00 21.62 ?  181 ALA A N   1 
ATOM   1344 C  CA  . ALA A 1 181 ? 54.300 23.789  61.133  1.00 22.05 ?  181 ALA A CA  1 
ATOM   1345 C  C   . ALA A 1 181 ? 55.413 24.489  60.364  1.00 22.34 ?  181 ALA A C   1 
ATOM   1346 O  O   . ALA A 1 181 ? 55.478 24.411  59.128  1.00 23.21 ?  181 ALA A O   1 
ATOM   1347 C  CB  . ALA A 1 181 ? 53.160 24.761  61.449  1.00 25.27 ?  181 ALA A CB  1 
ATOM   1348 N  N   . GLN A 1 182 ? 56.313 25.175  61.073  1.00 24.32 ?  182 GLN A N   1 
ATOM   1349 C  CA  . GLN A 1 182 ? 57.383 25.871  60.370  1.00 24.53 ?  182 GLN A CA  1 
ATOM   1350 C  C   . GLN A 1 182 ? 58.397 24.902  59.779  1.00 24.62 ?  182 GLN A C   1 
ATOM   1351 O  O   . GLN A 1 182 ? 58.966 25.170  58.713  1.00 21.98 ?  182 GLN A O   1 
ATOM   1352 C  CB  . GLN A 1 182 ? 58.085 26.862  61.299  1.00 26.78 ?  182 GLN A CB  1 
ATOM   1353 C  CG  . GLN A 1 182 ? 59.046 27.779  60.572  1.00 28.74 ?  182 GLN A CG  1 
ATOM   1354 C  CD  . GLN A 1 182 ? 58.328 28.824  59.722  1.00 39.32 ?  182 GLN A CD  1 
ATOM   1355 O  OE1 . GLN A 1 182 ? 57.719 29.759  60.251  1.00 41.00 ?  182 GLN A OE1 1 
ATOM   1356 N  NE2 . GLN A 1 182 ? 58.403 28.671  58.402  1.00 32.69 ?  182 GLN A NE2 1 
ATOM   1357 N  N   . ALA A 1 183 ? 58.649 23.774  60.443  1.00 18.98 ?  183 ALA A N   1 
ATOM   1358 C  CA  . ALA A 1 183 ? 59.561 22.810  59.853  1.00 20.36 ?  183 ALA A CA  1 
ATOM   1359 C  C   . ALA A 1 183 ? 58.983 22.252  58.563  1.00 19.25 ?  183 ALA A C   1 
ATOM   1360 O  O   . ALA A 1 183 ? 59.694 22.079  57.567  1.00 18.93 ?  183 ALA A O   1 
ATOM   1361 C  CB  . ALA A 1 183 ? 59.851 21.682  60.848  1.00 21.52 ?  183 ALA A CB  1 
ATOM   1362 N  N   . VAL A 1 184 ? 57.683 21.975  58.558  1.00 16.66 ?  184 VAL A N   1 
ATOM   1363 C  CA  . VAL A 1 184 ? 57.062 21.442  57.352  1.00 20.09 ?  184 VAL A CA  1 
ATOM   1364 C  C   . VAL A 1 184 ? 57.026 22.507  56.262  1.00 22.16 ?  184 VAL A C   1 
ATOM   1365 O  O   . VAL A 1 184 ? 57.373 22.237  55.110  1.00 21.45 ?  184 VAL A O   1 
ATOM   1366 C  CB  . VAL A 1 184 ? 55.667 20.893  57.697  1.00 20.87 ?  184 VAL A CB  1 
ATOM   1367 C  CG1 . VAL A 1 184 ? 54.929 20.497  56.444  1.00 23.16 ?  184 VAL A CG1 1 
ATOM   1368 C  CG2 . VAL A 1 184 ? 55.817 19.708  58.658  1.00 19.64 ?  184 VAL A CG2 1 
ATOM   1369 N  N   . LEU A 1 185 ? 56.673 23.745  56.626  1.00 21.53 ?  185 LEU A N   1 
ATOM   1370 C  CA  . LEU A 1 185 ? 56.687 24.857  55.673  1.00 23.47 ?  185 LEU A CA  1 
ATOM   1371 C  C   . LEU A 1 185 ? 58.064 25.041  55.042  1.00 26.38 ?  185 LEU A C   1 
ATOM   1372 O  O   . LEU A 1 185 ? 58.184 25.233  53.826  1.00 26.80 ?  185 LEU A O   1 
ATOM   1373 C  CB  . LEU A 1 185 ? 56.268 26.151  56.379  1.00 26.85 ?  185 LEU A CB  1 
ATOM   1374 C  CG  . LEU A 1 185 ? 54.889 26.732  56.086  1.00 35.67 ?  185 LEU A CG  1 
ATOM   1375 C  CD1 . LEU A 1 185 ? 54.809 28.168  56.611  1.00 33.57 ?  185 LEU A CD1 1 
ATOM   1376 C  CD2 . LEU A 1 185 ? 54.550 26.658  54.596  1.00 29.12 ?  185 LEU A CD2 1 
ATOM   1377 N  N   . ASP A 1 186 ? 59.122 25.006  55.854  1.00 25.49 ?  186 ASP A N   1 
ATOM   1378 C  CA  . ASP A 1 186 ? 60.462 25.185  55.299  1.00 28.11 ?  186 ASP A CA  1 
ATOM   1379 C  C   . ASP A 1 186 ? 60.846 24.045  54.367  1.00 30.02 ?  186 ASP A C   1 
ATOM   1380 O  O   . ASP A 1 186 ? 61.664 24.234  53.458  1.00 27.90 ?  186 ASP A O   1 
ATOM   1381 C  CB  . ASP A 1 186 ? 61.485 25.320  56.422  1.00 26.86 ?  186 ASP A CB  1 
ATOM   1382 C  CG  . ASP A 1 186 ? 61.519 26.726  56.999  1.00 32.88 ?  186 ASP A CG  1 
ATOM   1383 O  OD1 . ASP A 1 186 ? 61.094 27.661  56.290  1.00 42.22 ?  186 ASP A OD1 1 
ATOM   1384 O  OD2 . ASP A 1 186 ? 61.955 26.896  58.155  1.00 35.71 -1 186 ASP A OD2 1 
ATOM   1385 N  N   . ALA A 1 187 ? 60.273 22.862  54.573  1.00 22.87 ?  187 ALA A N   1 
ATOM   1386 C  CA  . ALA A 1 187 ? 60.583 21.744  53.698  1.00 21.17 ?  187 ALA A CA  1 
ATOM   1387 C  C   . ALA A 1 187 ? 59.962 21.926  52.317  1.00 21.77 ?  187 ALA A C   1 
ATOM   1388 O  O   . ALA A 1 187 ? 60.557 21.527  51.306  1.00 24.76 ?  187 ALA A O   1 
ATOM   1389 C  CB  . ALA A 1 187 ? 60.097 20.440  54.334  1.00 23.67 ?  187 ALA A CB  1 
ATOM   1390 N  N   . VAL A 1 188 ? 58.756 22.495  52.249  1.00 20.47 ?  188 VAL A N   1 
ATOM   1391 C  CA  . VAL A 1 188 ? 58.098 22.622  50.946  1.00 17.55 ?  188 VAL A CA  1 
ATOM   1392 C  C   . VAL A 1 188 ? 58.631 23.801  50.135  1.00 24.26 ?  188 VAL A C   1 
ATOM   1393 O  O   . VAL A 1 188 ? 58.427 23.840  48.917  1.00 22.39 ?  188 VAL A O   1 
ATOM   1394 C  CB  . VAL A 1 188 ? 56.565 22.724  51.086  1.00 24.42 ?  188 VAL A CB  1 
ATOM   1395 C  CG1 . VAL A 1 188 ? 56.025 21.614  51.999  1.00 18.21 ?  188 VAL A CG1 1 
ATOM   1396 C  CG2 . VAL A 1 188 ? 56.138 24.061  51.621  1.00 24.95 ?  188 VAL A CG2 1 
ATOM   1397 N  N   . LYS A 1 189 ? 59.336 24.736  50.769  1.00 19.60 ?  189 LYS A N   1 
ATOM   1398 C  CA  . LYS A 1 189 ? 59.844 25.937  50.107  1.00 26.68 ?  189 LYS A CA  1 
ATOM   1399 C  C   . LYS A 1 189 ? 58.753 26.610  49.270  1.00 24.03 ?  189 LYS A C   1 
ATOM   1400 O  O   . LYS A 1 189 ? 57.714 26.971  49.830  1.00 24.05 ?  189 LYS A O   1 
ATOM   1401 C  CB  . LYS A 1 189 ? 61.100 25.589  49.309  1.00 28.56 ?  189 LYS A CB  1 
ATOM   1402 C  CG  . LYS A 1 189 ? 62.351 25.694  50.221  1.00 35.76 ?  189 LYS A CG  1 
ATOM   1403 C  CD  . LYS A 1 189 ? 63.236 24.462  50.193  1.00 41.20 ?  189 LYS A CD  1 
ATOM   1404 C  CE  . LYS A 1 189 ? 64.095 24.365  51.465  1.00 43.32 ?  189 LYS A CE  1 
ATOM   1405 N  NZ  . LYS A 1 189 ? 64.282 22.955  51.945  1.00 39.61 ?  189 LYS A NZ  1 
ATOM   1406 N  N   . ASP A 1 190 ? 58.945 26.796  47.956  1.00 25.82 ?  190 ASP A N   1 
ATOM   1407 C  CA  . ASP A 1 190 ? 57.995 27.564  47.146  1.00 23.58 ?  190 ASP A CA  1 
ATOM   1408 C  C   . ASP A 1 190 ? 57.014 26.695  46.348  1.00 27.12 ?  190 ASP A C   1 
ATOM   1409 O  O   . ASP A 1 190 ? 56.277 27.217  45.498  1.00 25.16 ?  190 ASP A O   1 
ATOM   1410 C  CB  . ASP A 1 190 ? 58.746 28.514  46.199  1.00 28.48 ?  190 ASP A CB  1 
ATOM   1411 C  CG  . ASP A 1 190 ? 59.696 27.794  45.237  1.00 35.52 ?  190 ASP A CG  1 
ATOM   1412 O  OD1 . ASP A 1 190 ? 59.956 26.586  45.419  1.00 36.28 ?  190 ASP A OD1 1 
ATOM   1413 O  OD2 . ASP A 1 190 ? 60.181 28.452  44.281  1.00 29.85 -1 190 ASP A OD2 1 
ATOM   1414 N  N   . ALA A 1 191 ? 56.944 25.411  46.640  1.00 19.98 ?  191 ALA A N   1 
ATOM   1415 C  CA  . ALA A 1 191 ? 56.212 24.465  45.817  1.00 20.75 ?  191 ALA A CA  1 
ATOM   1416 C  C   . ALA A 1 191 ? 54.727 24.425  46.183  1.00 20.09 ?  191 ALA A C   1 
ATOM   1417 O  O   . ALA A 1 191 ? 54.348 24.737  47.317  1.00 21.55 ?  191 ALA A O   1 
ATOM   1418 C  CB  . ALA A 1 191 ? 56.809 23.073  45.982  1.00 20.36 ?  191 ALA A CB  1 
ATOM   1419 N  N   . PRO A 1 192 ? 53.873 24.037  45.237  1.00 18.39 ?  192 PRO A N   1 
ATOM   1420 C  CA  . PRO A 1 192 ? 52.531 23.581  45.601  1.00 17.11 ?  192 PRO A CA  1 
ATOM   1421 C  C   . PRO A 1 192 ? 52.644 22.254  46.337  1.00 15.74 ?  192 PRO A C   1 
ATOM   1422 O  O   . PRO A 1 192 ? 53.663 21.569  46.260  1.00 17.95 ?  192 PRO A O   1 
ATOM   1423 C  CB  . PRO A 1 192 ? 51.831 23.419  44.249  1.00 19.22 ?  192 PRO A CB  1 
ATOM   1424 C  CG  . PRO A 1 192 ? 52.933 23.063  43.318  1.00 23.68 ?  192 PRO A CG  1 
ATOM   1425 C  CD  . PRO A 1 192 ? 54.148 23.842  43.802  1.00 21.40 ?  192 PRO A CD  1 
ATOM   1426 N  N   . VAL A 1 193 ? 51.591 21.901  47.074  1.00 16.01 ?  193 VAL A N   1 
ATOM   1427 C  CA  . VAL A 1 193 ? 51.699 20.866  48.102  1.00 16.84 ?  193 VAL A CA  1 
ATOM   1428 C  C   . VAL A 1 193 ? 50.537 19.889  47.980  1.00 15.36 ?  193 VAL A C   1 
ATOM   1429 O  O   . VAL A 1 193 ? 49.381 20.295  47.801  1.00 15.31 ?  193 VAL A O   1 
ATOM   1430 C  CB  . VAL A 1 193 ? 51.726 21.484  49.519  1.00 17.72 ?  193 VAL A CB  1 
ATOM   1431 C  CG1 . VAL A 1 193 ? 51.711 20.391  50.603  1.00 18.84 ?  193 VAL A CG1 1 
ATOM   1432 C  CG2 . VAL A 1 193 ? 52.950 22.395  49.698  1.00 19.94 ?  193 VAL A CG2 1 
ATOM   1433 N  N   . TRP A 1 194 ? 50.852 18.597  48.094  1.00 12.85 ?  194 TRP A N   1 
ATOM   1434 C  CA  . TRP A 1 194 ? 49.871 17.525  48.232  1.00 13.08 ?  194 TRP A CA  1 
ATOM   1435 C  C   . TRP A 1 194 ? 50.101 16.862  49.581  1.00 13.15 ?  194 TRP A C   1 
ATOM   1436 O  O   . TRP A 1 194 ? 51.234 16.506  49.894  1.00 13.16 ?  194 TRP A O   1 
ATOM   1437 C  CB  . TRP A 1 194 ? 50.045 16.488  47.118  1.00 13.70 ?  194 TRP A CB  1 
ATOM   1438 C  CG  . TRP A 1 194 ? 49.074 15.326  47.175  1.00 12.94 ?  194 TRP A CG  1 
ATOM   1439 C  CD1 . TRP A 1 194 ? 49.256 14.127  47.826  1.00 14.84 ?  194 TRP A CD1 1 
ATOM   1440 C  CD2 . TRP A 1 194 ? 47.805 15.237  46.512  1.00 12.62 ?  194 TRP A CD2 1 
ATOM   1441 N  NE1 . TRP A 1 194 ? 48.165 13.305  47.608  1.00 16.14 ?  194 TRP A NE1 1 
ATOM   1442 C  CE2 . TRP A 1 194 ? 47.267 13.966  46.802  1.00 13.85 ?  194 TRP A CE2 1 
ATOM   1443 C  CE3 . TRP A 1 194 ? 47.076 16.107  45.690  1.00 15.10 ?  194 TRP A CE3 1 
ATOM   1444 C  CZ2 . TRP A 1 194 ? 46.024 13.548  46.308  1.00 18.62 ?  194 TRP A CZ2 1 
ATOM   1445 C  CZ3 . TRP A 1 194 ? 45.840 15.689  45.204  1.00 18.38 ?  194 TRP A CZ3 1 
ATOM   1446 C  CH2 . TRP A 1 194 ? 45.330 14.426  45.510  1.00 18.53 ?  194 TRP A CH2 1 
ATOM   1447 N  N   . ILE A 1 195 ? 49.045 16.712  50.381  1.00 11.06 ?  195 ILE A N   1 
ATOM   1448 C  CA  . ILE A 1 195 ? 49.152 16.145  51.717  1.00 11.18 ?  195 ILE A CA  1 
ATOM   1449 C  C   . ILE A 1 195 ? 48.512 14.766  51.716  1.00 12.30 ?  195 ILE A C   1 
ATOM   1450 O  O   . ILE A 1 195 ? 47.354 14.612  51.322  1.00 13.21 ?  195 ILE A O   1 
ATOM   1451 C  CB  . ILE A 1 195 ? 48.476 17.049  52.760  1.00 11.81 ?  195 ILE A CB  1 
ATOM   1452 C  CG1 . ILE A 1 195 ? 49.173 18.409  52.792  1.00 14.74 ?  195 ILE A CG1 1 
ATOM   1453 C  CG2 . ILE A 1 195 ? 48.508 16.380  54.137  1.00 17.09 ?  195 ILE A CG2 1 
ATOM   1454 C  CD1 . ILE A 1 195 ? 48.527 19.419  53.749  1.00 15.96 ?  195 ILE A CD1 1 
ATOM   1455 N  N   . HIS A 1 196 ? 49.265 13.768  52.159  1.00 9.37  ?  196 HIS A N   1 
ATOM   1456 C  CA  . HIS A 1 196 ? 48.767 12.410  52.318  1.00 9.30  ?  196 HIS A CA  1 
ATOM   1457 C  C   . HIS A 1 196 ? 48.903 12.070  53.796  1.00 10.39 ?  196 HIS A C   1 
ATOM   1458 O  O   . HIS A 1 196 ? 49.999 12.194  54.333  1.00 11.13 ?  196 HIS A O   1 
ATOM   1459 C  CB  . HIS A 1 196 ? 49.600 11.462  51.441  1.00 12.90 ?  196 HIS A CB  1 
ATOM   1460 C  CG  . HIS A 1 196 ? 49.388 10.008  51.737  1.00 13.99 ?  196 HIS A CG  1 
ATOM   1461 N  ND1 . HIS A 1 196 ? 48.748 9.157   50.856  1.00 15.59 ?  196 HIS A ND1 1 
ATOM   1462 C  CD2 . HIS A 1 196 ? 49.743 9.254   52.805  1.00 12.08 ?  196 HIS A CD2 1 
ATOM   1463 C  CE1 . HIS A 1 196 ? 48.705 7.944   51.377  1.00 17.17 ?  196 HIS A CE1 1 
ATOM   1464 N  NE2 . HIS A 1 196 ? 49.299 7.976   52.560  1.00 16.44 ?  196 HIS A NE2 1 
ATOM   1465 N  N   . ILE A 1 197 ? 47.810 11.674  54.468  1.00 8.58  ?  197 ILE A N   1 
ATOM   1466 C  CA  . ILE A 1 197 ? 47.871 11.330  55.896  1.00 11.22 ?  197 ILE A CA  1 
ATOM   1467 C  C   . ILE A 1 197 ? 47.413 9.899   56.132  1.00 11.96 ?  197 ILE A C   1 
ATOM   1468 O  O   . ILE A 1 197 ? 46.307 9.520   55.723  1.00 12.33 ?  197 ILE A O   1 
ATOM   1469 C  CB  . ILE A 1 197 ? 47.015 12.269  56.765  1.00 12.46 ?  197 ILE A CB  1 
ATOM   1470 C  CG1 . ILE A 1 197 ? 47.284 13.727  56.394  1.00 20.13 ?  197 ILE A CG1 1 
ATOM   1471 C  CG2 . ILE A 1 197 ? 47.329 11.994  58.237  1.00 13.82 ?  197 ILE A CG2 1 
ATOM   1472 C  CD1 . ILE A 1 197 ? 46.407 14.700  57.164  1.00 21.63 ?  197 ILE A CD1 1 
ATOM   1473 N  N   . ASP A 1 198 ? 48.248 9.135   56.839  1.00 10.40 ?  198 ASP A N   1 
ATOM   1474 C  CA  . ASP A 1 198 ? 47.912 7.838   57.422  1.00 10.50 ?  198 ASP A CA  1 
ATOM   1475 C  C   . ASP A 1 198 ? 47.711 8.055   58.921  1.00 12.29 ?  198 ASP A C   1 
ATOM   1476 O  O   . ASP A 1 198 ? 48.629 8.527   59.606  1.00 11.46 ?  198 ASP A O   1 
ATOM   1477 C  CB  . ASP A 1 198 ? 49.060 6.868   57.130  1.00 10.74 ?  198 ASP A CB  1 
ATOM   1478 C  CG  . ASP A 1 198 ? 48.918 5.507   57.804  1.00 10.21 ?  198 ASP A CG  1 
ATOM   1479 O  OD1 . ASP A 1 198 ? 48.047 5.312   58.669  1.00 9.74  ?  198 ASP A OD1 1 
ATOM   1480 O  OD2 . ASP A 1 198 ? 49.729 4.622   57.426  1.00 12.67 -1 198 ASP A OD2 1 
ATOM   1481 N  N   . TRP A 1 199 ? 46.515 7.744   59.432  1.00 10.97 ?  199 TRP A N   1 
ATOM   1482 C  CA  . TRP A 1 199 ? 46.237 8.121   60.817  1.00 9.59  ?  199 TRP A CA  1 
ATOM   1483 C  C   . TRP A 1 199 ? 47.106 7.388   61.837  1.00 11.44 ?  199 TRP A C   1 
ATOM   1484 O  O   . TRP A 1 199 ? 47.144 7.820   62.997  1.00 11.85 ?  199 TRP A O   1 
ATOM   1485 C  CB  . TRP A 1 199 ? 44.741 7.941   61.141  1.00 12.55 ?  199 TRP A CB  1 
ATOM   1486 C  CG  . TRP A 1 199 ? 43.859 8.854   60.295  1.00 12.74 ?  199 TRP A CG  1 
ATOM   1487 C  CD1 . TRP A 1 199 ? 42.892 8.462   59.424  1.00 14.85 ?  199 TRP A CD1 1 
ATOM   1488 C  CD2 . TRP A 1 199 ? 43.903 10.297  60.222  1.00 14.16 ?  199 TRP A CD2 1 
ATOM   1489 N  NE1 . TRP A 1 199 ? 42.319 9.549   58.821  1.00 13.74 ?  199 TRP A NE1 1 
ATOM   1490 C  CE2 . TRP A 1 199 ? 42.926 10.691  59.283  1.00 16.42 ?  199 TRP A CE2 1 
ATOM   1491 C  CE3 . TRP A 1 199 ? 44.671 11.290  60.855  1.00 15.53 ?  199 TRP A CE3 1 
ATOM   1492 C  CZ2 . TRP A 1 199 ? 42.693 12.031  58.958  1.00 15.28 ?  199 TRP A CZ2 1 
ATOM   1493 C  CZ3 . TRP A 1 199 ? 44.440 12.623  60.534  1.00 17.53 ?  199 TRP A CZ3 1 
ATOM   1494 C  CH2 . TRP A 1 199 ? 43.446 12.984  59.594  1.00 15.69 ?  199 TRP A CH2 1 
ATOM   1495 N  N   . ASP A 1 200 ? 47.848 6.338   61.449  1.00 8.57  ?  200 ASP A N   1 
ATOM   1496 C  CA  . ASP A 1 200 ? 48.750 5.760   62.451  1.00 8.86  ?  200 ASP A CA  1 
ATOM   1497 C  C   . ASP A 1 200 ? 49.918 6.680   62.792  1.00 11.42 ?  200 ASP A C   1 
ATOM   1498 O  O   . ASP A 1 200 ? 50.701 6.346   63.682  1.00 13.20 ?  200 ASP A O   1 
ATOM   1499 C  CB  . ASP A 1 200 ? 49.255 4.355   62.032  1.00 12.56 ?  200 ASP A CB  1 
ATOM   1500 C  CG  . ASP A 1 200 ? 50.103 4.333   60.743  1.00 14.26 ?  200 ASP A CG  1 
ATOM   1501 O  OD1 . ASP A 1 200 ? 50.817 5.305   60.436  1.00 10.11 ?  200 ASP A OD1 1 
ATOM   1502 O  OD2 . ASP A 1 200 ? 50.082 3.277   60.052  1.00 12.35 -1 200 ASP A OD2 1 
ATOM   1503 N  N   . VAL A 1 201 ? 50.026 7.849   62.157  1.00 12.02 ?  201 VAL A N   1 
ATOM   1504 C  CA  . VAL A 1 201 ? 51.007 8.835   62.609  1.00 9.42  ?  201 VAL A CA  1 
ATOM   1505 C  C   . VAL A 1 201 ? 50.673 9.371   64.000  1.00 13.99 ?  201 VAL A C   1 
ATOM   1506 O  O   . VAL A 1 201 ? 51.573 9.848   64.711  1.00 12.96 ?  201 VAL A O   1 
ATOM   1507 C  CB  . VAL A 1 201 ? 51.101 9.990   61.589  1.00 12.98 ?  201 VAL A CB  1 
ATOM   1508 C  CG1 . VAL A 1 201 ? 49.876 10.910  61.667  1.00 12.17 ?  201 VAL A CG1 1 
ATOM   1509 C  CG2 . VAL A 1 201 ? 52.416 10.778  61.785  1.00 12.30 ?  201 VAL A CG2 1 
ATOM   1510 N  N   . LEU A 1 202 ? 49.408 9.297   64.421  1.00 13.73 ?  202 LEU A N   1 
ATOM   1511 C  CA  . LEU A 1 202 ? 48.974 9.972   65.647  1.00 11.06 ?  202 LEU A CA  1 
ATOM   1512 C  C   . LEU A 1 202 ? 49.370 9.213   66.909  1.00 17.16 ?  202 LEU A C   1 
ATOM   1513 O  O   . LEU A 1 202 ? 49.276 7.986   66.976  1.00 18.63 ?  202 LEU A O   1 
ATOM   1514 C  CB  . LEU A 1 202 ? 47.459 10.147  65.655  1.00 11.73 ?  202 LEU A CB  1 
ATOM   1515 C  CG  . LEU A 1 202 ? 46.853 11.077  64.606  1.00 16.14 ?  202 LEU A CG  1 
ATOM   1516 C  CD1 . LEU A 1 202 ? 45.337 11.027  64.728  1.00 19.89 ?  202 LEU A CD1 1 
ATOM   1517 C  CD2 . LEU A 1 202 ? 47.383 12.482  64.858  1.00 18.73 ?  202 LEU A CD2 1 
ATOM   1518 N  N   . GLU A 1 203 ? 49.753 9.957   67.930  1.00 16.20 ?  203 GLU A N   1 
ATOM   1519 C  CA  . GLU A 1 203 ? 49.952 9.349   69.245  1.00 20.01 ?  203 GLU A CA  1 
ATOM   1520 C  C   . GLU A 1 203 ? 48.675 8.632   69.686  1.00 21.74 ?  203 GLU A C   1 
ATOM   1521 O  O   . GLU A 1 203 ? 47.584 9.208   69.581  1.00 25.55 ?  203 GLU A O   1 
ATOM   1522 C  CB  . GLU A 1 203 ? 50.336 10.436  70.253  1.00 24.31 ?  203 GLU A CB  1 
ATOM   1523 C  CG  . GLU A 1 203 ? 50.423 9.947   71.683  1.00 26.86 ?  203 GLU A CG  1 
ATOM   1524 C  CD  . GLU A 1 203 ? 51.724 9.219   71.982  1.00 31.85 ?  203 GLU A CD  1 
ATOM   1525 O  OE1 . GLU A 1 203 ? 52.493 8.923   71.041  1.00 28.10 ?  203 GLU A OE1 1 
ATOM   1526 O  OE2 . GLU A 1 203 ? 51.987 8.946   73.172  1.00 36.79 -1 203 GLU A OE2 1 
ATOM   1527 N  N   . PRO A 1 204 ? 48.756 7.378   70.144  1.00 27.94 ?  204 PRO A N   1 
ATOM   1528 C  CA  . PRO A 1 204 ? 47.554 6.689   70.640  1.00 32.33 ?  204 PRO A CA  1 
ATOM   1529 C  C   . PRO A 1 204 ? 46.753 7.565   71.598  1.00 43.91 ?  204 PRO A C   1 
ATOM   1530 O  O   . PRO A 1 204 ? 47.290 8.133   72.557  1.00 41.57 ?  204 PRO A O   1 
ATOM   1531 C  CB  . PRO A 1 204 ? 48.122 5.450   71.336  1.00 34.78 ?  204 PRO A CB  1 
ATOM   1532 C  CG  . PRO A 1 204 ? 49.382 5.165   70.605  1.00 32.83 ?  204 PRO A CG  1 
ATOM   1533 C  CD  . PRO A 1 204 ? 49.942 6.501   70.167  1.00 26.12 ?  204 PRO A CD  1 
ATOM   1534 N  N   . GLY A 1 205 ? 45.452 7.667   71.326  1.00 48.16 ?  205 GLY A N   1 
ATOM   1535 C  CA  . GLY A 1 205 ? 44.648 8.803   71.730  1.00 52.94 ?  205 GLY A CA  1 
ATOM   1536 C  C   . GLY A 1 205 ? 43.949 8.749   73.070  1.00 60.52 ?  205 GLY A C   1 
ATOM   1537 O  O   . GLY A 1 205 ? 42.758 9.066   73.161  1.00 64.01 ?  205 GLY A O   1 
ATOM   1538 N  N   . SER A 1 206 ? 44.668 8.354   74.117  1.00 61.01 ?  206 SER A N   1 
ATOM   1539 C  CA  . SER A 1 206 ? 44.266 8.682   75.483  1.00 65.06 ?  206 SER A CA  1 
ATOM   1540 C  C   . SER A 1 206 ? 44.997 9.956   75.905  1.00 70.82 ?  206 SER A C   1 
ATOM   1541 O  O   . SER A 1 206 ? 45.923 9.949   76.719  1.00 72.74 ?  206 SER A O   1 
ATOM   1542 C  CB  . SER A 1 206 ? 44.547 7.515   76.425  1.00 61.17 ?  206 SER A CB  1 
ATOM   1543 O  OG  . SER A 1 206 ? 43.560 6.505   76.292  1.00 57.40 ?  206 SER A OG  1 
ATOM   1544 N  N   . ILE A 1 207 ? 44.544 11.068  75.322  1.00 73.62 ?  207 ILE A N   1 
ATOM   1545 C  CA  . ILE A 1 207 ? 45.206 12.370  75.434  1.00 71.70 ?  207 ILE A CA  1 
ATOM   1546 C  C   . ILE A 1 207 ? 45.303 12.842  76.884  1.00 75.33 ?  207 ILE A C   1 
ATOM   1547 O  O   . ILE A 1 207 ? 46.044 13.802  77.155  1.00 71.29 ?  207 ILE A O   1 
ATOM   1548 C  CB  . ILE A 1 207 ? 44.519 13.425  74.542  1.00 70.01 ?  207 ILE A CB  1 
ATOM   1549 C  CG1 . ILE A 1 207 ? 45.465 14.605  74.275  1.00 68.31 ?  207 ILE A CG1 1 
ATOM   1550 C  CG2 . ILE A 1 207 ? 43.218 13.918  75.156  1.00 69.65 ?  207 ILE A CG2 1 
ATOM   1551 C  CD1 . ILE A 1 207 ? 45.393 15.168  72.864  1.00 55.37 ?  207 ILE A CD1 1 
ATOM   1552 N  N   . PRO A 1 208 ? 44.590 12.224  77.867  1.00 77.07 ?  208 PRO A N   1 
ATOM   1553 C  CA  . PRO A 1 208 ? 45.104 12.277  79.242  1.00 75.17 ?  208 PRO A CA  1 
ATOM   1554 C  C   . PRO A 1 208 ? 46.594 11.960  79.276  1.00 73.32 ?  208 PRO A C   1 
ATOM   1555 O  O   . PRO A 1 208 ? 46.999 10.846  79.628  1.00 74.79 ?  208 PRO A O   1 
ATOM   1556 C  CB  . PRO A 1 208 ? 44.268 11.216  79.975  1.00 75.73 ?  208 PRO A CB  1 
ATOM   1557 C  CG  . PRO A 1 208 ? 43.131 10.833  79.012  1.00 75.28 ?  208 PRO A CG  1 
ATOM   1558 C  CD  . PRO A 1 208 ? 43.174 11.814  77.877  1.00 75.42 ?  208 PRO A CD  1 
ATOM   1559 N  N   . ALA A 1 209 ? 47.414 12.943  78.893  1.00 67.60 ?  209 ALA A N   1 
ATOM   1560 C  CA  . ALA A 1 209 ? 48.849 12.752  78.720  1.00 56.79 ?  209 ALA A CA  1 
ATOM   1561 C  C   . ALA A 1 209 ? 49.588 14.082  78.815  1.00 46.77 ?  209 ALA A C   1 
ATOM   1562 O  O   . ALA A 1 209 ? 50.463 14.373  77.993  1.00 43.29 ?  209 ALA A O   1 
ATOM   1563 C  CB  . ALA A 1 209 ? 49.140 12.076  77.379  1.00 57.30 ?  209 ALA A CB  1 
ATOM   1564 N  N   . ASP A 1 210 ? 49.249 14.888  79.823  1.00 39.60 ?  210 ASP A N   1 
ATOM   1565 C  CA  . ASP A 1 210 ? 49.883 16.191  80.003  1.00 38.79 ?  210 ASP A CA  1 
ATOM   1566 C  C   . ASP A 1 210 ? 51.320 16.089  80.503  1.00 33.73 ?  210 ASP A C   1 
ATOM   1567 O  O   . ASP A 1 210 ? 52.086 17.047  80.349  1.00 30.93 ?  210 ASP A O   1 
ATOM   1568 C  CB  . ASP A 1 210 ? 49.063 17.038  80.980  1.00 38.52 ?  210 ASP A CB  1 
ATOM   1569 C  CG  . ASP A 1 210 ? 47.894 17.735  80.310  1.00 45.61 ?  210 ASP A CG  1 
ATOM   1570 O  OD1 . ASP A 1 210 ? 47.767 17.635  79.071  1.00 49.81 -1 210 ASP A OD1 1 
ATOM   1571 O  OD2 . ASP A 1 210 ? 47.100 18.386  81.026  1.00 51.57 -1 210 ASP A OD2 1 
ATOM   1572 N  N   . TYR A 1 211 ? 51.709 14.959  81.096  1.00 31.45 ?  211 TYR A N   1 
ATOM   1573 C  CA  . TYR A 1 211 ? 53.026 14.824  81.706  1.00 27.82 ?  211 TYR A CA  1 
ATOM   1574 C  C   . TYR A 1 211 ? 53.903 13.799  80.994  1.00 26.71 ?  211 TYR A C   1 
ATOM   1575 O  O   . TYR A 1 211 ? 54.979 13.449  81.501  1.00 26.95 ?  211 TYR A O   1 
ATOM   1576 C  CB  . TYR A 1 211 ? 52.871 14.478  83.190  1.00 30.37 ?  211 TYR A CB  1 
ATOM   1577 C  CG  . TYR A 1 211 ? 52.081 15.535  83.929  1.00 29.19 ?  211 TYR A CG  1 
ATOM   1578 C  CD1 . TYR A 1 211 ? 52.676 16.737  84.300  1.00 25.00 ?  211 TYR A CD1 1 
ATOM   1579 C  CD2 . TYR A 1 211 ? 50.737 15.347  84.229  1.00 33.24 ?  211 TYR A CD2 1 
ATOM   1580 C  CE1 . TYR A 1 211 ? 51.959 17.715  84.975  1.00 26.10 ?  211 TYR A CE1 1 
ATOM   1581 C  CE2 . TYR A 1 211 ? 50.008 16.317  84.897  1.00 31.32 ?  211 TYR A CE2 1 
ATOM   1582 C  CZ  . TYR A 1 211 ? 50.622 17.499  85.265  1.00 32.59 ?  211 TYR A CZ  1 
ATOM   1583 O  OH  . TYR A 1 211 ? 49.895 18.461  85.929  1.00 31.26 ?  211 TYR A OH  1 
ATOM   1584 N  N   . THR A 1 212 ? 53.478 13.348  79.816  1.00 30.31 ?  212 THR A N   1 
ATOM   1585 C  CA  . THR A 1 212 ? 54.176 12.376  78.991  1.00 27.85 ?  212 THR A CA  1 
ATOM   1586 C  C   . THR A 1 212 ? 54.589 13.040  77.689  1.00 22.52 ?  212 THR A C   1 
ATOM   1587 O  O   . THR A 1 212 ? 53.795 13.761  77.078  1.00 25.47 ?  212 THR A O   1 
ATOM   1588 C  CB  . THR A 1 212 ? 53.262 11.185  78.664  1.00 31.32 ?  212 THR A CB  1 
ATOM   1589 O  OG1 . THR A 1 212 ? 52.949 10.468  79.864  1.00 44.29 ?  212 THR A OG1 1 
ATOM   1590 C  CG2 . THR A 1 212 ? 53.928 10.259  77.675  1.00 35.15 ?  212 THR A CG2 1 
ATOM   1591 N  N   . VAL A 1 213 ? 55.816 12.800  77.258  1.00 22.71 ?  213 VAL A N   1 
ATOM   1592 C  CA  . VAL A 1 213 ? 56.228 13.291  75.942  1.00 21.41 ?  213 VAL A CA  1 
ATOM   1593 C  C   . VAL A 1 213 ? 55.747 12.301  74.885  1.00 17.99 ?  213 VAL A C   1 
ATOM   1594 O  O   . VAL A 1 213 ? 56.071 11.112  74.977  1.00 21.03 ?  213 VAL A O   1 
ATOM   1595 C  CB  . VAL A 1 213 ? 57.736 13.466  75.883  1.00 23.84 ?  213 VAL A CB  1 
ATOM   1596 C  CG1 . VAL A 1 213 ? 58.167 13.787  74.470  1.00 24.88 ?  213 VAL A CG1 1 
ATOM   1597 C  CG2 . VAL A 1 213 ? 58.152 14.568  76.840  1.00 25.17 ?  213 VAL A CG2 1 
ATOM   1598 N  N   . PRO A 1 214 ? 55.003 12.742  73.885  1.00 19.36 ?  214 PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 214 ? 54.420 11.793  72.935  1.00 19.60 ?  214 PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 214 ? 55.456 11.223  71.986  1.00 22.34 ?  214 PRO A C   1 
ATOM   1601 O  O   . PRO A 1 214 ? 56.432 11.877  71.613  1.00 21.53 ?  214 PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 214 ? 53.393 12.639  72.173  1.00 19.92 ?  214 PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 214 ? 53.932 14.010  72.213  1.00 19.38 ?  214 PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 214 ? 54.652 14.135  73.572  1.00 18.62 ?  214 PRO A CD  1 
ATOM   1605 N  N   . ASP A 1 215 ? 55.213 9.983   71.576  1.00 19.46 ?  215 ASP A N   1 
ATOM   1606 C  CA  . ASP A 1 215 ? 56.020 9.361   70.535  1.00 19.10 ?  215 ASP A CA  1 
ATOM   1607 C  C   . ASP A 1 215 ? 55.468 9.624   69.140  1.00 17.69 ?  215 ASP A C   1 
ATOM   1608 O  O   . ASP A 1 215 ? 56.241 9.728   68.185  1.00 23.23 ?  215 ASP A O   1 
ATOM   1609 C  CB  . ASP A 1 215 ? 56.113 7.854   70.795  1.00 22.61 ?  215 ASP A CB  1 
ATOM   1610 C  CG  . ASP A 1 215 ? 56.756 7.546   72.139  1.00 31.16 ?  215 ASP A CG  1 
ATOM   1611 O  OD1 . ASP A 1 215 ? 57.947 7.892   72.306  1.00 34.95 ?  215 ASP A OD1 1 
ATOM   1612 O  OD2 . ASP A 1 215 ? 56.068 6.982   73.024  1.00 39.27 -1 215 ASP A OD2 1 
ATOM   1613 N  N   . GLY A 1 216 ? 54.153 9.758   69.003  1.00 15.19 ?  216 GLY A N   1 
ATOM   1614 C  CA  . GLY A 1 216 ? 53.548 10.098  67.734  1.00 16.27 ?  216 GLY A CA  1 
ATOM   1615 C  C   . GLY A 1 216 ? 53.277 11.587  67.622  1.00 14.54 ?  216 GLY A C   1 
ATOM   1616 O  O   . GLY A 1 216 ? 53.599 12.378  68.506  1.00 19.29 ?  216 GLY A O   1 
ATOM   1617 N  N   . MET A 1 217 ? 52.671 11.969  66.496  1.00 13.40 ?  217 MET A N   1 
ATOM   1618 C  CA  . MET A 1 217 ? 52.230 13.357  66.372  1.00 13.40 ?  217 MET A CA  1 
ATOM   1619 C  C   . MET A 1 217 ? 50.909 13.566  67.100  1.00 16.62 ?  217 MET A C   1 
ATOM   1620 O  O   . MET A 1 217 ? 50.072 12.665  67.184  1.00 16.83 ?  217 MET A O   1 
ATOM   1621 C  CB  . MET A 1 217 ? 52.074 13.749  64.900  1.00 13.17 ?  217 MET A CB  1 
ATOM   1622 C  CG  . MET A 1 217 ? 53.402 13.832  64.147  1.00 15.89 ?  217 MET A CG  1 
ATOM   1623 S  SD  . MET A 1 217 ? 53.210 14.385  62.434  1.00 18.05 ?  217 MET A SD  1 
ATOM   1624 C  CE  . MET A 1 217 ? 52.847 16.145  62.666  1.00 18.31 ?  217 MET A CE  1 
ATOM   1625 N  N   . LEU A 1 218 ? 50.729 14.781  67.648  1.00 13.91 ?  218 LEU A N   1 
ATOM   1626 C  CA  . LEU A 1 218 ? 49.466 15.145  68.271  1.00 18.70 ?  218 LEU A CA  1 
ATOM   1627 C  C   . LEU A 1 218 ? 48.526 15.763  67.242  1.00 16.13 ?  218 LEU A C   1 
ATOM   1628 O  O   . LEU A 1 218 ? 48.979 16.390  66.279  1.00 18.84 ?  218 LEU A O   1 
ATOM   1629 C  CB  . LEU A 1 218 ? 49.692 16.152  69.404  1.00 17.56 ?  218 LEU A CB  1 
ATOM   1630 C  CG  . LEU A 1 218 ? 50.620 15.659  70.520  1.00 20.40 ?  218 LEU A CG  1 
ATOM   1631 C  CD1 . LEU A 1 218 ? 50.868 16.778  71.516  1.00 25.48 ?  218 LEU A CD1 1 
ATOM   1632 C  CD2 . LEU A 1 218 ? 49.984 14.464  71.193  1.00 22.21 ?  218 LEU A CD2 1 
ATOM   1633 N  N   . PRO A 1 219 ? 47.214 15.610  67.427  1.00 15.54 ?  219 PRO A N   1 
ATOM   1634 C  CA  . PRO A 1 219 ? 46.273 16.277  66.504  1.00 17.01 ?  219 PRO A CA  1 
ATOM   1635 C  C   . PRO A 1 219 ? 46.584 17.754  66.309  1.00 17.42 ?  219 PRO A C   1 
ATOM   1636 O  O   . PRO A 1 219 ? 46.496 18.260  65.184  1.00 17.09 ?  219 PRO A O   1 
ATOM   1637 C  CB  . PRO A 1 219 ? 44.911 16.051  67.173  1.00 21.93 ?  219 PRO A CB  1 
ATOM   1638 C  CG  . PRO A 1 219 ? 45.087 14.738  67.894  1.00 20.32 ?  219 PRO A CG  1 
ATOM   1639 C  CD  . PRO A 1 219 ? 46.517 14.767  68.415  1.00 19.01 ?  219 PRO A CD  1 
ATOM   1640 N  N   . ALA A 1 220 ? 46.995 18.450  67.369  1.00 18.24 ?  220 ALA A N   1 
ATOM   1641 C  CA  . ALA A 1 220 ? 47.289 19.869  67.234  1.00 16.85 ?  220 ALA A CA  1 
ATOM   1642 C  C   . ALA A 1 220 ? 48.422 20.121  66.254  1.00 16.48 ?  220 ALA A C   1 
ATOM   1643 O  O   . ALA A 1 220 ? 48.438 21.161  65.586  1.00 19.28 ?  220 ALA A O   1 
ATOM   1644 C  CB  . ALA A 1 220 ? 47.625 20.481  68.602  1.00 18.95 ?  220 ALA A CB  1 
ATOM   1645 N  N   . GLN A 1 221 ? 49.384 19.192  66.152  1.00 16.04 ?  221 GLN A N   1 
ATOM   1646 C  CA  . GLN A 1 221 ? 50.452 19.360  65.176  1.00 15.75 ?  221 GLN A CA  1 
ATOM   1647 C  C   . GLN A 1 221 ? 49.947 19.162  63.754  1.00 14.89 ?  221 GLN A C   1 
ATOM   1648 O  O   . GLN A 1 221 ? 50.424 19.828  62.834  1.00 16.21 ?  221 GLN A O   1 
ATOM   1649 C  CB  . GLN A 1 221 ? 51.592 18.383  65.441  1.00 17.29 ?  221 GLN A CB  1 
ATOM   1650 C  CG  . GLN A 1 221 ? 52.300 18.563  66.742  1.00 18.68 ?  221 GLN A CG  1 
ATOM   1651 C  CD  . GLN A 1 221 ? 53.406 17.535  66.902  1.00 19.73 ?  221 GLN A CD  1 
ATOM   1652 O  OE1 . GLN A 1 221 ? 53.155 16.385  67.272  1.00 20.58 ?  221 GLN A OE1 1 
ATOM   1653 N  NE2 . GLN A 1 221 ? 54.634 17.937  66.607  1.00 21.50 ?  221 GLN A NE2 1 
ATOM   1654 N  N   . ILE A 1 222 ? 49.027 18.212  63.542  1.00 16.55 ?  222 ILE A N   1 
ATOM   1655 C  CA  . ILE A 1 222 ? 48.440 18.041  62.211  1.00 14.52 ?  222 ILE A CA  1 
ATOM   1656 C  C   . ILE A 1 222 ? 47.634 19.275  61.831  1.00 16.91 ?  222 ILE A C   1 
ATOM   1657 O  O   . ILE A 1 222 ? 47.780 19.816  60.734  1.00 18.56 ?  222 ILE A O   1 
ATOM   1658 C  CB  . ILE A 1 222 ? 47.566 16.775  62.150  1.00 15.10 ?  222 ILE A CB  1 
ATOM   1659 C  CG1 . ILE A 1 222 ? 48.387 15.542  62.523  1.00 18.61 ?  222 ILE A CG1 1 
ATOM   1660 C  CG2 . ILE A 1 222 ? 46.853 16.669  60.764  1.00 15.87 ?  222 ILE A CG2 1 
ATOM   1661 C  CD1 . ILE A 1 222 ? 49.440 15.194  61.502  1.00 21.31 ?  222 ILE A CD1 1 
ATOM   1662 N  N   . ARG A 1 223 ? 46.787 19.748  62.744  1.00 18.45 ?  223 ARG A N   1 
ATOM   1663 C  CA  . ARG A 1 223 ? 46.017 20.957  62.463  1.00 17.74 ?  223 ARG A CA  1 
ATOM   1664 C  C   . ARG A 1 223 ? 46.935 22.122  62.113  1.00 18.10 ?  223 ARG A C   1 
ATOM   1665 O  O   . ARG A 1 223 ? 46.670 22.870  61.164  1.00 19.57 ?  223 ARG A O   1 
ATOM   1666 C  CB  . ARG A 1 223 ? 45.141 21.301  63.669  1.00 20.78 ?  223 ARG A CB  1 
ATOM   1667 C  CG  . ARG A 1 223 ? 44.113 22.376  63.386  1.00 22.55 ?  223 ARG A CG  1 
ATOM   1668 C  CD  . ARG A 1 223 ? 43.398 22.780  64.645  1.00 29.21 ?  223 ARG A CD  1 
ATOM   1669 N  NE  . ARG A 1 223 ? 42.818 24.117  64.523  1.00 30.97 ?  223 ARG A NE  1 
ATOM   1670 C  CZ  . ARG A 1 223 ? 41.550 24.357  64.211  1.00 39.73 ?  223 ARG A CZ  1 
ATOM   1671 N  NH1 . ARG A 1 223 ? 40.712 23.350  63.976  1.00 34.98 ?  223 ARG A NH1 1 
ATOM   1672 N  NH2 . ARG A 1 223 ? 41.123 25.612  64.125  1.00 32.73 ?  223 ARG A NH2 1 
ATOM   1673 N  N   . ALA A 1 224 ? 48.038 22.276  62.856  1.00 18.85 ?  224 ALA A N   1 
ATOM   1674 C  CA  . ALA A 1 224 ? 48.942 23.395  62.620  1.00 18.28 ?  224 ALA A CA  1 
ATOM   1675 C  C   . ALA A 1 224 ? 49.552 23.341  61.225  1.00 20.06 ?  224 ALA A C   1 
ATOM   1676 O  O   . ALA A 1 224 ? 49.804 24.388  60.622  1.00 21.18 ?  224 ALA A O   1 
ATOM   1677 C  CB  . ALA A 1 224 ? 50.043 23.412  63.681  1.00 21.63 ?  224 ALA A CB  1 
ATOM   1678 N  N   . VAL A 1 225 ? 49.799 22.134  60.703  1.00 20.30 ?  225 VAL A N   1 
ATOM   1679 C  CA  . VAL A 1 225 ? 50.265 21.997  59.320  1.00 19.01 ?  225 VAL A CA  1 
ATOM   1680 C  C   . VAL A 1 225 ? 49.201 22.494  58.349  1.00 17.33 ?  225 VAL A C   1 
ATOM   1681 O  O   . VAL A 1 225 ? 49.491 23.269  57.429  1.00 20.99 ?  225 VAL A O   1 
ATOM   1682 C  CB  . VAL A 1 225 ? 50.655 20.535  59.022  1.00 19.12 ?  225 VAL A CB  1 
ATOM   1683 C  CG1 . VAL A 1 225 ? 50.873 20.345  57.517  1.00 17.91 ?  225 VAL A CG1 1 
ATOM   1684 C  CG2 . VAL A 1 225 ? 51.904 20.136  59.811  1.00 19.77 ?  225 VAL A CG2 1 
ATOM   1685 N  N   . PHE A 1 226 ? 47.954 22.039  58.522  1.00 20.41 ?  226 PHE A N   1 
ATOM   1686 C  CA  . PHE A 1 226 ? 46.880 22.490  57.638  1.00 20.03 ?  226 PHE A CA  1 
ATOM   1687 C  C   . PHE A 1 226 ? 46.674 24.001  57.730  1.00 21.74 ?  226 PHE A C   1 
ATOM   1688 O  O   . PHE A 1 226 ? 46.366 24.650  56.723  1.00 24.05 ?  226 PHE A O   1 
ATOM   1689 C  CB  . PHE A 1 226 ? 45.581 21.753  57.958  1.00 18.84 ?  226 PHE A CB  1 
ATOM   1690 C  CG  . PHE A 1 226 ? 45.505 20.378  57.363  1.00 19.43 ?  226 PHE A CG  1 
ATOM   1691 C  CD1 . PHE A 1 226 ? 45.517 20.202  55.985  1.00 27.69 ?  226 PHE A CD1 1 
ATOM   1692 C  CD2 . PHE A 1 226 ? 45.420 19.266  58.173  1.00 21.92 ?  226 PHE A CD2 1 
ATOM   1693 C  CE1 . PHE A 1 226 ? 45.443 18.925  55.432  1.00 20.67 ?  226 PHE A CE1 1 
ATOM   1694 C  CE2 . PHE A 1 226 ? 45.340 17.993  57.630  1.00 25.17 ?  226 PHE A CE2 1 
ATOM   1695 C  CZ  . PHE A 1 226 ? 45.360 17.826  56.253  1.00 19.09 ?  226 PHE A CZ  1 
ATOM   1696 N  N   . GLU A 1 227 ? 46.835 24.580  58.927  1.00 19.67 ?  227 GLU A N   1 
ATOM   1697 C  CA  . GLU A 1 227 ? 46.730 26.033  59.079  1.00 22.40 ?  227 GLU A CA  1 
ATOM   1698 C  C   . GLU A 1 227 ? 47.847 26.765  58.337  1.00 26.48 ?  227 GLU A C   1 
ATOM   1699 O  O   . GLU A 1 227 ? 47.641 27.890  57.872  1.00 27.68 ?  227 GLU A O   1 
ATOM   1700 C  CB  . GLU A 1 227 ? 46.742 26.425  60.568  1.00 26.49 ?  227 GLU A CB  1 
ATOM   1701 C  CG  . GLU A 1 227 ? 45.667 25.729  61.395  1.00 32.28 ?  227 GLU A CG  1 
ATOM   1702 C  CD  . GLU A 1 227 ? 45.616 26.114  62.885  1.00 42.50 ?  227 GLU A CD  1 
ATOM   1703 O  OE1 . GLU A 1 227 ? 46.646 25.991  63.597  1.00 40.39 ?  227 GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A 1 227 ? 44.519 26.508  63.351  1.00 40.76 -1 227 GLU A OE2 1 
ATOM   1705 N  N   . ALA A 1 228 ? 49.025 26.150  58.209  1.00 21.18 ?  228 ALA A N   1 
ATOM   1706 C  CA  . ALA A 1 228 ? 50.203 26.833  57.676  1.00 24.74 ?  228 ALA A CA  1 
ATOM   1707 C  C   . ALA A 1 228 ? 50.325 26.786  56.154  1.00 25.38 ?  228 ALA A C   1 
ATOM   1708 O  O   . ALA A 1 228 ? 50.990 27.650  55.570  1.00 24.07 ?  228 ALA A O   1 
ATOM   1709 C  CB  . ALA A 1 228 ? 51.480 26.239  58.282  1.00 24.80 ?  228 ALA A CB  1 
ATOM   1710 N  N   . ILE A 1 229 ? 49.756 25.785  55.491  1.00 22.52 ?  229 ILE A N   1 
ATOM   1711 C  CA  . ILE A 1 229 ? 49.895 25.697  54.037  1.00 22.69 ?  229 ILE A CA  1 
ATOM   1712 C  C   . ILE A 1 229 ? 48.939 26.698  53.396  1.00 21.27 ?  229 ILE A C   1 
ATOM   1713 O  O   . ILE A 1 229 ? 47.726 26.588  53.599  1.00 23.15 ?  229 ILE A O   1 
ATOM   1714 C  CB  . ILE A 1 229 ? 49.612 24.274  53.530  1.00 26.38 ?  229 ILE A CB  1 
ATOM   1715 C  CG1 . ILE A 1 229 ? 50.513 23.246  54.235  1.00 24.34 ?  229 ILE A CG1 1 
ATOM   1716 C  CG2 . ILE A 1 229 ? 49.781 24.212  52.010  1.00 24.99 ?  229 ILE A CG2 1 
ATOM   1717 C  CD1 . ILE A 1 229 ? 52.001 23.469  54.019  1.00 24.41 ?  229 ILE A CD1 1 
ATOM   1718 N  N   . PRO A 1 230 ? 49.419 27.679  52.629  1.00 25.09 ?  230 PRO A N   1 
ATOM   1719 C  CA  . PRO A 1 230 ? 48.493 28.652  52.033  1.00 26.35 ?  230 PRO A CA  1 
ATOM   1720 C  C   . PRO A 1 230 ? 47.494 27.969  51.108  1.00 26.68 ?  230 PRO A C   1 
ATOM   1721 O  O   . PRO A 1 230 ? 47.837 27.046  50.367  1.00 21.88 ?  230 PRO A O   1 
ATOM   1722 C  CB  . PRO A 1 230 ? 49.423 29.610  51.271  1.00 27.86 ?  230 PRO A CB  1 
ATOM   1723 C  CG  . PRO A 1 230 ? 50.748 29.476  51.958  1.00 27.95 ?  230 PRO A CG  1 
ATOM   1724 C  CD  . PRO A 1 230 ? 50.826 28.014  52.347  1.00 26.70 ?  230 PRO A CD  1 
ATOM   1725 N  N   . ALA A 1 231 ? 46.237 28.425  51.174  1.00 27.98 ?  231 ALA A N   1 
ATOM   1726 C  CA  . ALA A 1 231 ? 45.173 27.800  50.390  1.00 27.98 ?  231 ALA A CA  1 
ATOM   1727 C  C   . ALA A 1 231 ? 45.508 27.770  48.903  1.00 25.35 ?  231 ALA A C   1 
ATOM   1728 O  O   . ALA A 1 231 ? 45.215 26.783  48.215  1.00 23.58 ?  231 ALA A O   1 
ATOM   1729 C  CB  . ALA A 1 231 ? 43.846 28.527  50.622  1.00 28.05 ?  231 ALA A CB  1 
ATOM   1730 N  N   . GLU A 1 232 ? 46.145 28.827  48.385  1.00 23.31 ?  232 GLU A N   1 
ATOM   1731 C  CA  . GLU A 1 232 ? 46.435 28.839  46.955  1.00 25.18 ?  232 GLU A CA  1 
ATOM   1732 C  C   . GLU A 1 232 ? 47.493 27.810  46.568  1.00 26.19 ?  232 GLU A C   1 
ATOM   1733 O  O   . GLU A 1 232 ? 47.602 27.470  45.385  1.00 29.28 ?  232 GLU A O   1 
ATOM   1734 C  CB  . GLU A 1 232 ? 46.867 30.248  46.508  1.00 32.13 ?  232 GLU A CB  1 
ATOM   1735 C  CG  . GLU A 1 232 ? 47.066 30.404  44.992  1.00 39.98 ?  232 GLU A CG  1 
ATOM   1736 C  CD  . GLU A 1 232 ? 48.478 30.034  44.538  1.00 45.11 ?  232 GLU A CD  1 
ATOM   1737 O  OE1 . GLU A 1 232 ? 49.426 30.245  45.329  1.00 48.49 ?  232 GLU A OE1 1 
ATOM   1738 O  OE2 . GLU A 1 232 ? 48.640 29.514  43.408  1.00 52.40 -1 232 GLU A OE2 1 
ATOM   1739 N  N   . ARG A 1 233 ? 48.247 27.273  47.527  1.00 23.48 ?  233 ARG A N   1 
ATOM   1740 C  CA  . ARG A 1 233 ? 49.292 26.322  47.194  1.00 20.05 ?  233 ARG A CA  1 
ATOM   1741 C  C   . ARG A 1 233 ? 48.867 24.875  47.414  1.00 21.18 ?  233 ARG A C   1 
ATOM   1742 O  O   . ARG A 1 233 ? 49.586 23.972  46.989  1.00 18.17 ?  233 ARG A O   1 
ATOM   1743 C  CB  . ARG A 1 233 ? 50.561 26.602  48.017  1.00 24.79 ?  233 ARG A CB  1 
ATOM   1744 C  CG  . ARG A 1 233 ? 50.973 28.078  48.051  1.00 32.11 ?  233 ARG A CG  1 
ATOM   1745 C  CD  . ARG A 1 233 ? 52.393 28.279  47.566  1.00 33.23 ?  233 ARG A CD  1 
ATOM   1746 N  NE  . ARG A 1 233 ? 53.321 27.279  48.086  1.00 31.85 ?  233 ARG A NE  1 
ATOM   1747 C  CZ  . ARG A 1 233 ? 54.300 27.535  48.946  1.00 30.86 ?  233 ARG A CZ  1 
ATOM   1748 N  NH1 . ARG A 1 233 ? 55.099 26.560  49.341  1.00 23.75 ?  233 ARG A NH1 1 
ATOM   1749 N  NH2 . ARG A 1 233 ? 54.478 28.772  49.410  1.00 37.07 ?  233 ARG A NH2 1 
ATOM   1750 N  N   . LEU A 1 234 ? 47.734 24.642  48.065  1.00 17.96 ?  234 LEU A N   1 
ATOM   1751 C  CA  . LEU A 1 234 ? 47.306 23.282  48.393  1.00 19.00 ?  234 LEU A CA  1 
ATOM   1752 C  C   . LEU A 1 234 ? 46.581 22.652  47.205  1.00 18.56 ?  234 LEU A C   1 
ATOM   1753 O  O   . LEU A 1 234 ? 45.521 23.131  46.791  1.00 21.39 ?  234 LEU A O   1 
ATOM   1754 C  CB  . LEU A 1 234 ? 46.412 23.297  49.628  1.00 16.37 ?  234 LEU A CB  1 
ATOM   1755 C  CG  . LEU A 1 234 ? 46.052 21.903  50.161  1.00 17.92 ?  234 LEU A CG  1 
ATOM   1756 C  CD1 . LEU A 1 234 ? 47.299 21.082  50.457  1.00 14.48 ?  234 LEU A CD1 1 
ATOM   1757 C  CD2 . LEU A 1 234 ? 45.176 22.012  51.388  1.00 17.65 ?  234 LEU A CD2 1 
ATOM   1758 N  N   . ILE A 1 235 ? 47.167 21.586  46.656  1.00 15.36 ?  235 ILE A N   1 
ATOM   1759 C  CA  . ILE A 1 235 ? 46.582 20.867  45.532  1.00 15.00 ?  235 ILE A CA  1 
ATOM   1760 C  C   . ILE A 1 235 ? 45.478 19.935  46.010  1.00 18.26 ?  235 ILE A C   1 
ATOM   1761 O  O   . ILE A 1 235 ? 44.380 19.891  45.451  1.00 17.72 ?  235 ILE A O   1 
ATOM   1762 C  CB  . ILE A 1 235 ? 47.668 20.060  44.798  1.00 15.63 ?  235 ILE A CB  1 
ATOM   1763 C  CG1 . ILE A 1 235 ? 48.818 20.948  44.332  1.00 21.20 ?  235 ILE A CG1 1 
ATOM   1764 C  CG2 . ILE A 1 235 ? 47.060 19.252  43.649  1.00 19.68 ?  235 ILE A CG2 1 
ATOM   1765 C  CD1 . ILE A 1 235 ? 50.054 20.141  43.996  1.00 16.89 ?  235 ILE A CD1 1 
ATOM   1766 N  N   . GLY A 1 236 ? 45.760 19.151  47.036  1.00 14.57 ?  236 GLY A N   1 
ATOM   1767 C  CA  . GLY A 1 236 ? 44.780 18.171  47.452  1.00 14.97 ?  236 GLY A CA  1 
ATOM   1768 C  C   . GLY A 1 236 ? 45.238 17.500  48.719  1.00 12.26 ?  236 GLY A C   1 
ATOM   1769 O  O   . GLY A 1 236 ? 46.351 17.728  49.190  1.00 12.02 ?  236 GLY A O   1 
ATOM   1770 N  N   . VAL A 1 237 ? 44.344 16.679  49.268  1.00 12.77 ?  237 VAL A N   1 
ATOM   1771 C  CA  . VAL A 1 237 ? 44.540 16.038  50.570  1.00 10.73 ?  237 VAL A CA  1 
ATOM   1772 C  C   . VAL A 1 237 ? 43.990 14.623  50.492  1.00 13.54 ?  237 VAL A C   1 
ATOM   1773 O  O   . VAL A 1 237 ? 42.866 14.419  50.023  1.00 13.22 ?  237 VAL A O   1 
ATOM   1774 C  CB  . VAL A 1 237 ? 43.830 16.794  51.710  1.00 14.50 ?  237 VAL A CB  1 
ATOM   1775 C  CG1 . VAL A 1 237 ? 44.027 16.062  53.028  1.00 14.55 ?  237 VAL A CG1 1 
ATOM   1776 C  CG2 . VAL A 1 237 ? 44.363 18.221  51.828  1.00 13.63 ?  237 VAL A CG2 1 
ATOM   1777 N  N   . GLU A 1 238 ? 44.759 13.654  50.993  1.00 12.14 ?  238 GLU A N   1 
ATOM   1778 C  CA  . GLU A 1 238 ? 44.303 12.278  51.126  1.00 12.82 ?  238 GLU A CA  1 
ATOM   1779 C  C   . GLU A 1 238 ? 44.266 11.908  52.597  1.00 13.05 ?  238 GLU A C   1 
ATOM   1780 O  O   . GLU A 1 238 ? 45.251 12.121  53.317  1.00 11.49 ?  238 GLU A O   1 
ATOM   1781 C  CB  . GLU A 1 238 ? 45.220 11.289  50.406  1.00 16.29 ?  238 GLU A CB  1 
ATOM   1782 C  CG  . GLU A 1 238 ? 45.521 11.679  49.021  1.00 15.89 ?  238 GLU A CG  1 
ATOM   1783 C  CD  . GLU A 1 238 ? 46.380 10.642  48.340  1.00 20.28 ?  238 GLU A CD  1 
ATOM   1784 O  OE1 . GLU A 1 238 ? 47.609 10.733  48.490  1.00 20.86 ?  238 GLU A OE1 1 
ATOM   1785 O  OE2 . GLU A 1 238 ? 45.811 9.747   47.673  1.00 22.19 -1 238 GLU A OE2 1 
ATOM   1786 N  N   . LEU A 1 239 ? 43.143 11.333  53.028  1.00 12.85 ?  239 LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 239 ? 42.958 10.870  54.400  1.00 10.99 ?  239 LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 239 ? 42.781 9.359   54.381  1.00 12.20 ?  239 LEU A C   1 
ATOM   1789 O  O   . LEU A 1 239 ? 41.786 8.870   53.846  1.00 14.03 ?  239 LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 239 ? 41.738 11.529  55.041  1.00 13.60 ?  239 LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 239 ? 41.626 13.039  54.868  1.00 11.49 ?  239 LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 239 ? 40.357 13.568  55.532  1.00 13.74 ?  239 LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 239 ? 42.871 13.704  55.475  1.00 14.54 ?  239 LEU A CD2 1 
ATOM   1794 N  N   . ALA A 1 240 ? 43.706 8.626   55.000  1.00 10.71 ?  240 ALA A N   1 
ATOM   1795 C  CA  . ALA A 1 240 ? 43.720 7.169   54.866  1.00 10.72 ?  240 ALA A CA  1 
ATOM   1796 C  C   . ALA A 1 240 ? 43.868 6.473   56.211  1.00 13.17 ?  240 ALA A C   1 
ATOM   1797 O  O   . ALA A 1 240 ? 44.491 6.999   57.128  1.00 12.35 ?  240 ALA A O   1 
ATOM   1798 C  CB  . ALA A 1 240 ? 44.876 6.727   53.948  1.00 12.09 ?  240 ALA A CB  1 
ATOM   1799 N  N   . GLU A 1 241 ? 43.308 5.256   56.296  1.00 11.98 ?  241 GLU A N   1 
ATOM   1800 C  CA  . GLU A 1 241 ? 43.620 4.264   57.323  1.00 12.09 ?  241 GLU A CA  1 
ATOM   1801 C  C   . GLU A 1 241 ? 43.004 4.597   58.686  1.00 14.74 ?  241 GLU A C   1 
ATOM   1802 O  O   . GLU A 1 241 ? 43.672 4.512   59.724  1.00 15.25 ?  241 GLU A O   1 
ATOM   1803 C  CB  . GLU A 1 241 ? 45.148 4.067   57.413  1.00 12.88 ?  241 GLU A CB  1 
ATOM   1804 C  CG  . GLU A 1 241 ? 45.739 3.708   56.006  1.00 14.34 ?  241 GLU A CG  1 
ATOM   1805 C  CD  . GLU A 1 241 ? 46.681 2.493   55.969  1.00 17.28 ?  241 GLU A CD  1 
ATOM   1806 O  OE1 . GLU A 1 241 ? 47.049 1.949   57.036  1.00 15.47 ?  241 GLU A OE1 1 
ATOM   1807 O  OE2 . GLU A 1 241 ? 47.086 2.096   54.845  1.00 16.97 -1 241 GLU A OE2 1 
ATOM   1808 N  N   . LEU A 1 242 ? 41.718 4.932   58.703  1.00 12.09 ?  242 LEU A N   1 
ATOM   1809 C  CA  . LEU A 1 242 ? 40.957 5.000   59.947  1.00 11.79 ?  242 LEU A CA  1 
ATOM   1810 C  C   . LEU A 1 242 ? 40.350 3.621   60.152  1.00 15.28 ?  242 LEU A C   1 
ATOM   1811 O  O   . LEU A 1 242 ? 39.469 3.209   59.391  1.00 17.10 ?  242 LEU A O   1 
ATOM   1812 C  CB  . LEU A 1 242 ? 39.867 6.071   59.882  1.00 17.17 ?  242 LEU A CB  1 
ATOM   1813 C  CG  . LEU A 1 242 ? 38.926 6.130   61.101  1.00 15.67 ?  242 LEU A CG  1 
ATOM   1814 C  CD1 . LEU A 1 242 ? 39.705 6.419   62.380  1.00 18.83 ?  242 LEU A CD1 1 
ATOM   1815 C  CD2 . LEU A 1 242 ? 37.822 7.170   60.917  1.00 13.95 ?  242 LEU A CD2 1 
ATOM   1816 N  N   . ASN A 1 243 ? 40.809 2.896   61.166  1.00 16.01 ?  243 ASN A N   1 
ATOM   1817 C  CA  . ASN A 1 243 ? 40.304 1.541   61.410  1.00 14.26 ?  243 ASN A CA  1 
ATOM   1818 C  C   . ASN A 1 243 ? 39.262 1.622   62.523  1.00 19.54 ?  243 ASN A C   1 
ATOM   1819 O  O   . ASN A 1 243 ? 39.574 1.439   63.704  1.00 23.24 ?  243 ASN A O   1 
ATOM   1820 C  CB  . ASN A 1 243 ? 41.436 0.588   61.786  1.00 16.72 ?  243 ASN A CB  1 
ATOM   1821 C  CG  . ASN A 1 243 ? 41.007 -0.865  61.731  1.00 14.43 ?  243 ASN A CG  1 
ATOM   1822 O  OD1 . ASN A 1 243 ? 40.252 -1.248  60.842  1.00 15.12 ?  243 ASN A OD1 1 
ATOM   1823 N  ND2 . ASN A 1 243 ? 41.489 -1.686  62.668  1.00 15.00 ?  243 ASN A ND2 1 
ATOM   1824 N  N   . ALA A 1 244 ? 38.010 1.872   62.147  1.00 17.22 ?  244 ALA A N   1 
ATOM   1825 C  CA  . ALA A 1 244 ? 36.937 2.097   63.119  1.00 17.98 ?  244 ALA A CA  1 
ATOM   1826 C  C   . ALA A 1 244 ? 35.638 1.521   62.563  1.00 19.01 ?  244 ALA A C   1 
ATOM   1827 O  O   . ALA A 1 244 ? 35.262 1.836   61.417  1.00 19.78 ?  244 ALA A O   1 
ATOM   1828 C  CB  . ALA A 1 244 ? 36.778 3.586   63.432  1.00 19.77 ?  244 ALA A CB  1 
ATOM   1829 N  N   . PRO A 1 245 ? 34.963 0.651   63.315  1.00 20.96 ?  245 PRO A N   1 
ATOM   1830 C  CA  . PRO A 1 245 ? 33.763 -0.001  62.792  1.00 22.44 ?  245 PRO A CA  1 
ATOM   1831 C  C   . PRO A 1 245 ? 32.650 0.995   62.538  1.00 25.48 ?  245 PRO A C   1 
ATOM   1832 O  O   . PRO A 1 245 ? 32.491 1.982   63.265  1.00 24.14 ?  245 PRO A O   1 
ATOM   1833 C  CB  . PRO A 1 245 ? 33.375 -0.988  63.905  1.00 23.69 ?  245 PRO A CB  1 
ATOM   1834 C  CG  . PRO A 1 245 ? 34.572 -1.152  64.728  1.00 24.05 ?  245 PRO A CG  1 
ATOM   1835 C  CD  . PRO A 1 245 ? 35.350 0.131   64.633  1.00 20.73 ?  245 PRO A CD  1 
ATOM   1836 N  N   . ALA A 1 246 ? 31.898 0.733   61.470  1.00 31.71 ?  246 ALA A N   1 
ATOM   1837 C  CA  . ALA A 1 246 ? 30.694 1.496   61.186  1.00 35.72 ?  246 ALA A CA  1 
ATOM   1838 C  C   . ALA A 1 246 ? 29.726 1.392   62.357  1.00 36.88 ?  246 ALA A C   1 
ATOM   1839 O  O   . ALA A 1 246 ? 29.573 0.326   62.967  1.00 38.37 ?  246 ALA A O   1 
ATOM   1840 C  CB  . ALA A 1 246 ? 30.032 0.989   59.903  1.00 35.22 ?  246 ALA A CB  1 
ATOM   1841 N  N   . ASP A 1 247 ? 29.083 2.516   62.677  1.00 40.12 ?  247 ASP A N   1 
ATOM   1842 C  CA  . ASP A 1 247 ? 28.112 2.668   63.762  1.00 40.61 ?  247 ASP A CA  1 
ATOM   1843 C  C   . ASP A 1 247 ? 28.754 2.677   65.144  1.00 39.71 ?  247 ASP A C   1 
ATOM   1844 O  O   . ASP A 1 247 ? 28.037 2.861   66.138  1.00 43.35 ?  247 ASP A O   1 
ATOM   1845 C  CB  . ASP A 1 247 ? 27.027 1.579   63.752  1.00 42.83 ?  247 ASP A CB  1 
ATOM   1846 C  CG  . ASP A 1 247 ? 25.916 1.865   62.767  1.00 52.95 ?  247 ASP A CG  1 
ATOM   1847 O  OD1 . ASP A 1 247 ? 26.188 2.504   61.724  1.00 55.93 -1 247 ASP A OD1 1 
ATOM   1848 O  OD2 . ASP A 1 247 ? 24.768 1.447   63.039  1.00 52.12 -1 247 ASP A OD2 1 
ATOM   1849 N  N   . SER A 1 248 ? 30.063 2.477   65.255  1.00 34.84 ?  248 SER A N   1 
ATOM   1850 C  CA  . SER A 1 248 ? 30.679 2.482   66.572  1.00 31.01 ?  248 SER A CA  1 
ATOM   1851 C  C   . SER A 1 248 ? 30.747 3.902   67.122  1.00 31.70 ?  248 SER A C   1 
ATOM   1852 O  O   . SER A 1 248 ? 30.817 4.879   66.373  1.00 29.03 ?  248 SER A O   1 
ATOM   1853 C  CB  . SER A 1 248 ? 32.083 1.877   66.524  1.00 26.78 ?  248 SER A CB  1 
ATOM   1854 O  OG  . SER A 1 248 ? 32.991 2.696   65.793  1.00 29.82 ?  248 SER A OG  1 
ATOM   1855 N  N   . GLU A 1 249 ? 30.686 4.002   68.452  1.00 30.58 ?  249 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 249 ? 31.041 5.242   69.140  1.00 31.87 ?  249 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 249 ? 32.483 5.644   68.851  1.00 31.88 ?  249 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 249 ? 32.801 6.840   68.779  1.00 27.91 ?  249 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 249 ? 30.834 5.061   70.645  1.00 34.14 ?  249 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 249 ? 31.259 6.233   71.503  1.00 39.71 ?  249 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 249 ? 30.720 6.132   72.925  1.00 51.52 ?  249 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 249 ? 30.260 5.031   73.312  1.00 49.16 ?  249 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 249 ? 30.748 7.155   73.646  1.00 47.98 -1 249 GLU A OE2 1 
ATOM   1864 N  N   . ARG A 1 250 ? 33.366 4.659   68.682  1.00 28.92 ?  250 ARG A N   1 
ATOM   1865 C  CA  . ARG A 1 250 ? 34.766 4.950   68.402  1.00 29.71 ?  250 ARG A CA  1 
ATOM   1866 C  C   . ARG A 1 250 ? 34.923 5.727   67.099  1.00 23.57 ?  250 ARG A C   1 
ATOM   1867 O  O   . ARG A 1 250 ? 35.713 6.676   67.022  1.00 25.58 ?  250 ARG A O   1 
ATOM   1868 C  CB  . ARG A 1 250 ? 35.553 3.646   68.345  1.00 29.14 ?  250 ARG A CB  1 
ATOM   1869 C  CG  . ARG A 1 250 ? 37.027 3.844   68.152  1.00 30.39 ?  250 ARG A CG  1 
ATOM   1870 C  CD  . ARG A 1 250 ? 37.665 2.608   67.554  1.00 32.68 ?  250 ARG A CD  1 
ATOM   1871 N  NE  . ARG A 1 250 ? 39.082 2.832   67.311  1.00 37.55 ?  250 ARG A NE  1 
ATOM   1872 C  CZ  . ARG A 1 250 ? 40.028 2.644   68.224  1.00 43.05 ?  250 ARG A CZ  1 
ATOM   1873 N  NH1 . ARG A 1 250 ? 39.701 2.214   69.443  1.00 38.92 ?  250 ARG A NH1 1 
ATOM   1874 N  NH2 . ARG A 1 250 ? 41.295 2.879   67.914  1.00 44.04 ?  250 ARG A NH2 1 
ATOM   1875 N  N   . ALA A 1 251 ? 34.180 5.332   66.065  1.00 21.71 ?  251 ALA A N   1 
ATOM   1876 C  CA  . ALA A 1 251 ? 34.237 6.038   64.786  1.00 23.68 ?  251 ALA A CA  1 
ATOM   1877 C  C   . ALA A 1 251 ? 33.729 7.469   64.918  1.00 26.89 ?  251 ALA A C   1 
ATOM   1878 O  O   . ALA A 1 251 ? 34.327 8.397   64.358  1.00 20.92 ?  251 ALA A O   1 
ATOM   1879 C  CB  . ALA A 1 251 ? 33.425 5.283   63.736  1.00 20.84 ?  251 ALA A CB  1 
ATOM   1880 N  N   . GLU A 1 252 ? 32.619 7.672   65.637  1.00 23.36 ?  252 GLU A N   1 
ATOM   1881 C  CA  . GLU A 1 252 ? 32.106 9.031   65.794  1.00 25.65 ?  252 GLU A CA  1 
ATOM   1882 C  C   . GLU A 1 252 ? 33.120 9.917   66.511  1.00 24.66 ?  252 GLU A C   1 
ATOM   1883 O  O   . GLU A 1 252 ? 33.308 11.084  66.145  1.00 25.00 ?  252 GLU A O   1 
ATOM   1884 C  CB  . GLU A 1 252 ? 30.761 9.021   66.538  1.00 29.44 ?  252 GLU A CB  1 
ATOM   1885 C  CG  . GLU A 1 252 ? 29.786 7.914   66.100  1.00 36.99 ?  252 GLU A CG  1 
ATOM   1886 C  CD  . GLU A 1 252 ? 29.424 7.954   64.612  1.00 41.17 ?  252 GLU A CD  1 
ATOM   1887 O  OE1 . GLU A 1 252 ? 28.901 8.993   64.157  1.00 43.08 ?  252 GLU A OE1 1 
ATOM   1888 O  OE2 . GLU A 1 252 ? 29.654 6.939   63.900  1.00 45.70 -1 252 GLU A OE2 1 
ATOM   1889 N  N   . GLN A 1 253 ? 33.799 9.375   67.521  1.00 21.13 ?  253 GLN A N   1 
ATOM   1890 C  CA  . GLN A 1 253 ? 34.824 10.142  68.225  1.00 22.70 ?  253 GLN A CA  1 
ATOM   1891 C  C   . GLN A 1 253 ? 36.024 10.430  67.331  1.00 25.95 ?  253 GLN A C   1 
ATOM   1892 O  O   . GLN A 1 253 ? 36.577 11.539  67.358  1.00 22.03 ?  253 GLN A O   1 
ATOM   1893 C  CB  . GLN A 1 253 ? 35.262 9.387   69.482  1.00 29.49 ?  253 GLN A CB  1 
ATOM   1894 C  CG  . GLN A 1 253 ? 34.148 9.230   70.512  1.00 33.56 ?  253 GLN A CG  1 
ATOM   1895 C  CD  . GLN A 1 253 ? 34.547 8.339   71.666  1.00 42.68 ?  253 GLN A CD  1 
ATOM   1896 O  OE1 . GLN A 1 253 ? 35.495 7.561   71.562  1.00 39.42 ?  253 GLN A OE1 1 
ATOM   1897 N  NE2 . GLN A 1 253 ? 33.821 8.441   72.773  1.00 43.92 ?  253 GLN A NE2 1 
ATOM   1898 N  N   . ALA A 1 254 ? 36.453 9.438   66.545  1.00 23.13 ?  254 ALA A N   1 
ATOM   1899 C  CA  . ALA A 1 254 ? 37.602 9.629   65.663  1.00 22.42 ?  254 ALA A CA  1 
ATOM   1900 C  C   . ALA A 1 254 ? 37.317 10.666  64.582  1.00 19.28 ?  254 ALA A C   1 
ATOM   1901 O  O   . ALA A 1 254 ? 38.176 11.510  64.289  1.00 18.21 ?  254 ALA A O   1 
ATOM   1902 C  CB  . ALA A 1 254 ? 37.995 8.301   65.015  1.00 20.53 ?  254 ALA A CB  1 
ATOM   1903 N  N   . VAL A 1 255 ? 36.139 10.608  63.957  1.00 18.07 ?  255 VAL A N   1 
ATOM   1904 C  CA  . VAL A 1 255 ? 35.887 11.535  62.851  1.00 16.43 ?  255 VAL A CA  1 
ATOM   1905 C  C   . VAL A 1 255 ? 35.754 12.968  63.373  1.00 19.22 ?  255 VAL A C   1 
ATOM   1906 O  O   . VAL A 1 255 ? 36.103 13.922  62.668  1.00 19.01 ?  255 VAL A O   1 
ATOM   1907 C  CB  . VAL A 1 255 ? 34.668 11.114  62.003  1.00 22.47 ?  255 VAL A CB  1 
ATOM   1908 C  CG1 . VAL A 1 255 ? 34.874 9.713   61.405  1.00 25.78 ?  255 VAL A CG1 1 
ATOM   1909 C  CG2 . VAL A 1 255 ? 33.353 11.220  62.779  1.00 24.31 ?  255 VAL A CG2 1 
ATOM   1910 N  N   . ALA A 1 256 ? 35.311 13.155  64.624  1.00 24.15 ?  256 ALA A N   1 
ATOM   1911 C  CA  . ALA A 1 256 ? 35.249 14.518  65.150  1.00 22.42 ?  256 ALA A CA  1 
ATOM   1912 C  C   . ALA A 1 256 ? 36.645 15.103  65.310  1.00 19.67 ?  256 ALA A C   1 
ATOM   1913 O  O   . ALA A 1 256 ? 36.868 16.289  65.026  1.00 19.43 ?  256 ALA A O   1 
ATOM   1914 C  CB  . ALA A 1 256 ? 34.488 14.560  66.477  1.00 23.21 ?  256 ALA A CB  1 
ATOM   1915 N  N   . VAL A 1 257 ? 37.600 14.286  65.751  1.00 18.70 ?  257 VAL A N   1 
ATOM   1916 C  CA  . VAL A 1 257 ? 38.986 14.741  65.825  1.00 17.98 ?  257 VAL A CA  1 
ATOM   1917 C  C   . VAL A 1 257 ? 39.526 15.039  64.432  1.00 17.32 ?  257 VAL A C   1 
ATOM   1918 O  O   . VAL A 1 257 ? 40.250 16.021  64.227  1.00 15.81 ?  257 VAL A O   1 
ATOM   1919 C  CB  . VAL A 1 257 ? 39.857 13.699  66.555  1.00 24.05 ?  257 VAL A CB  1 
ATOM   1920 C  CG1 . VAL A 1 257 ? 41.302 14.140  66.556  1.00 20.75 ?  257 VAL A CG1 1 
ATOM   1921 C  CG2 . VAL A 1 257 ? 39.361 13.488  67.979  1.00 25.88 ?  257 VAL A CG2 1 
ATOM   1922 N  N   . ILE A 1 258 ? 39.182 14.195  63.451  1.00 15.93 ?  258 ILE A N   1 
ATOM   1923 C  CA  . ILE A 1 258 ? 39.658 14.405  62.083  1.00 17.29 ?  258 ILE A CA  1 
ATOM   1924 C  C   . ILE A 1 258 ? 39.129 15.726  61.534  1.00 16.89 ?  258 ILE A C   1 
ATOM   1925 O  O   . ILE A 1 258 ? 39.868 16.504  60.920  1.00 18.06 ?  258 ILE A O   1 
ATOM   1926 C  CB  . ILE A 1 258 ? 39.248 13.221  61.186  1.00 15.01 ?  258 ILE A CB  1 
ATOM   1927 C  CG1 . ILE A 1 258 ? 40.081 11.984  61.513  1.00 13.62 ?  258 ILE A CG1 1 
ATOM   1928 C  CG2 . ILE A 1 258 ? 39.385 13.580  59.702  1.00 15.32 ?  258 ILE A CG2 1 
ATOM   1929 C  CD1 . ILE A 1 258 ? 39.538 10.716  60.829  1.00 17.35 ?  258 ILE A CD1 1 
ATOM   1930 N  N   . LEU A 1 259 ? 37.841 16.004  61.755  1.00 19.17 ?  259 LEU A N   1 
ATOM   1931 C  CA  . LEU A 1 259 ? 37.268 17.249  61.246  1.00 17.17 ?  259 LEU A CA  1 
ATOM   1932 C  C   . LEU A 1 259 ? 38.005 18.451  61.827  1.00 17.97 ?  259 LEU A C   1 
ATOM   1933 O  O   . LEU A 1 259 ? 38.266 19.436  61.128  1.00 18.30 ?  259 LEU A O   1 
ATOM   1934 C  CB  . LEU A 1 259 ? 35.775 17.321  61.588  1.00 18.78 ?  259 LEU A CB  1 
ATOM   1935 C  CG  . LEU A 1 259 ? 34.796 16.464  60.788  1.00 22.64 ?  259 LEU A CG  1 
ATOM   1936 C  CD1 . LEU A 1 259 ? 33.374 16.654  61.264  1.00 24.48 ?  259 LEU A CD1 1 
ATOM   1937 C  CD2 . LEU A 1 259 ? 34.895 16.746  59.328  1.00 23.90 ?  259 LEU A CD2 1 
ATOM   1938 N  N   . ASP A 1 260 ? 38.376 18.368  63.103  1.00 18.64 ?  260 ASP A N   1 
ATOM   1939 C  CA  . ASP A 1 260 ? 39.082 19.470  63.752  1.00 20.32 ?  260 ASP A CA  1 
ATOM   1940 C  C   . ASP A 1 260 ? 40.446 19.703  63.116  1.00 17.24 ?  260 ASP A C   1 
ATOM   1941 O  O   . ASP A 1 260 ? 40.889 20.849  62.968  1.00 20.25 ?  260 ASP A O   1 
ATOM   1942 C  CB  . ASP A 1 260 ? 39.220 19.164  65.248  1.00 24.00 ?  260 ASP A CB  1 
ATOM   1943 C  CG  . ASP A 1 260 ? 40.195 20.097  65.960  1.00 35.22 ?  260 ASP A CG  1 
ATOM   1944 O  OD1 . ASP A 1 260 ? 39.760 21.182  66.396  1.00 39.28 ?  260 ASP A OD1 1 
ATOM   1945 O  OD2 . ASP A 1 260 ? 41.393 19.744  66.100  1.00 39.94 -1 260 ASP A OD2 1 
ATOM   1946 N  N   . MET A 1 261 ? 41.127 18.626  62.734  1.00 16.52 ?  261 MET A N   1 
ATOM   1947 C  CA  . MET A 1 261 ? 42.468 18.741  62.178  1.00 14.99 ?  261 MET A CA  1 
ATOM   1948 C  C   . MET A 1 261 ? 42.447 19.337  60.777  1.00 17.94 ?  261 MET A C   1 
ATOM   1949 O  O   . MET A 1 261 ? 43.307 20.154  60.435  1.00 18.15 ?  261 MET A O   1 
ATOM   1950 C  CB  . MET A 1 261 ? 43.145 17.361  62.163  1.00 16.18 ?  261 MET A CB  1 
ATOM   1951 C  CG  . MET A 1 261 ? 43.622 16.872  63.552  1.00 16.51 ?  261 MET A CG  1 
ATOM   1952 S  SD  . MET A 1 261 ? 44.413 15.233  63.516  1.00 18.55 ?  261 MET A SD  1 
ATOM   1953 C  CE  . MET A 1 261 ? 43.031 14.110  63.373  1.00 17.94 ?  261 MET A CE  1 
ATOM   1954 N  N   . VAL A 1 262 ? 41.506 18.903  59.933  1.00 15.35 ?  262 VAL A N   1 
ATOM   1955 C  CA  . VAL A 1 262 ? 41.501 19.333  58.532  1.00 14.77 ?  262 VAL A CA  1 
ATOM   1956 C  C   . VAL A 1 262 ? 40.765 20.646  58.324  1.00 17.98 ?  262 VAL A C   1 
ATOM   1957 O  O   . VAL A 1 262 ? 40.917 21.262  57.257  1.00 16.96 ?  262 VAL A O   1 
ATOM   1958 C  CB  . VAL A 1 262 ? 40.889 18.255  57.614  1.00 17.83 ?  262 VAL A CB  1 
ATOM   1959 C  CG1 . VAL A 1 262 ? 41.629 16.912  57.821  1.00 19.30 ?  262 VAL A CG1 1 
ATOM   1960 C  CG2 . VAL A 1 262 ? 39.384 18.094  57.868  1.00 17.60 ?  262 VAL A CG2 1 
ATOM   1961 N  N   . ALA A 1 263 ? 40.002 21.110  59.316  1.00 18.19 ?  263 ALA A N   1 
ATOM   1962 C  CA  . ALA A 1 263 ? 39.148 22.280  59.117  1.00 20.37 ?  263 ALA A CA  1 
ATOM   1963 C  C   . ALA A 1 263 ? 39.865 23.492  58.532  1.00 19.22 ?  263 ALA A C   1 
ATOM   1964 O  O   . ALA A 1 263 ? 39.293 24.128  57.635  1.00 20.32 ?  263 ALA A O   1 
ATOM   1965 C  CB  . ALA A 1 263 ? 38.472 22.644  60.448  1.00 18.97 ?  263 ALA A CB  1 
ATOM   1966 N  N   . PRO A 1 264 ? 41.075 23.871  58.965  1.00 21.98 ?  264 PRO A N   1 
ATOM   1967 C  CA  . PRO A 1 264 ? 41.700 25.079  58.386  1.00 23.50 ?  264 PRO A CA  1 
ATOM   1968 C  C   . PRO A 1 264 ? 41.828 25.044  56.869  1.00 23.94 ?  264 PRO A C   1 
ATOM   1969 O  O   . PRO A 1 264 ? 41.497 26.025  56.186  1.00 22.63 ?  264 PRO A O   1 
ATOM   1970 C  CB  . PRO A 1 264 ? 43.063 25.110  59.082  1.00 24.27 ?  264 PRO A CB  1 
ATOM   1971 C  CG  . PRO A 1 264 ? 42.814 24.446  60.384  1.00 24.61 ?  264 PRO A CG  1 
ATOM   1972 C  CD  . PRO A 1 264 ? 41.877 23.333  60.083  1.00 19.79 ?  264 PRO A CD  1 
ATOM   1973 N  N   . ALA A 1 265 ? 42.297 23.920  56.324  1.00 19.69 ?  265 ALA A N   1 
ATOM   1974 C  CA  . ALA A 1 265 ? 42.464 23.793  54.880  1.00 19.70 ?  265 ALA A CA  1 
ATOM   1975 C  C   . ALA A 1 265 ? 41.121 23.645  54.173  1.00 19.57 ?  265 ALA A C   1 
ATOM   1976 O  O   . ALA A 1 265 ? 40.901 24.235  53.107  1.00 21.94 ?  265 ALA A O   1 
ATOM   1977 C  CB  . ALA A 1 265 ? 43.365 22.593  54.571  1.00 22.14 ?  265 ALA A CB  1 
ATOM   1978 N  N   . PHE A 1 266 ? 40.208 22.855  54.740  1.00 16.81 ?  266 PHE A N   1 
ATOM   1979 C  CA  . PHE A 1 266 ? 38.956 22.601  54.042  1.00 17.02 ?  266 PHE A CA  1 
ATOM   1980 C  C   . PHE A 1 266 ? 38.043 23.826  54.096  1.00 19.11 ?  266 PHE A C   1 
ATOM   1981 O  O   . PHE A 1 266 ? 37.362 24.142  53.111  1.00 20.00 ?  266 PHE A O   1 
ATOM   1982 C  CB  . PHE A 1 266 ? 38.263 21.372  54.626  1.00 20.47 ?  266 PHE A CB  1 
ATOM   1983 C  CG  . PHE A 1 266 ? 38.941 20.056  54.287  1.00 17.36 ?  266 PHE A CG  1 
ATOM   1984 C  CD1 . PHE A 1 266 ? 40.190 20.023  53.688  1.00 21.77 ?  266 PHE A CD1 1 
ATOM   1985 C  CD2 . PHE A 1 266 ? 38.319 18.857  54.584  1.00 17.76 ?  266 PHE A CD2 1 
ATOM   1986 C  CE1 . PHE A 1 266 ? 40.800 18.804  53.379  1.00 19.32 ?  266 PHE A CE1 1 
ATOM   1987 C  CE2 . PHE A 1 266 ? 38.912 17.652  54.270  1.00 18.46 ?  266 PHE A CE2 1 
ATOM   1988 C  CZ  . PHE A 1 266 ? 40.152 17.630  53.665  1.00 18.94 ?  266 PHE A CZ  1 
ATOM   1989 N  N   . ASP A 1 267 ? 38.030 24.533  55.230  1.00 19.61 ?  267 ASP A N   1 
ATOM   1990 C  CA  . ASP A 1 267 ? 37.253 25.769  55.312  1.00 23.44 ?  267 ASP A CA  1 
ATOM   1991 C  C   . ASP A 1 267 ? 37.722 26.778  54.273  1.00 24.81 ?  267 ASP A C   1 
ATOM   1992 O  O   . ASP A 1 267 ? 36.905 27.440  53.617  1.00 25.20 ?  267 ASP A O   1 
ATOM   1993 C  CB  . ASP A 1 267 ? 37.367 26.384  56.709  1.00 22.16 ?  267 ASP A CB  1 
ATOM   1994 C  CG  . ASP A 1 267 ? 36.643 25.581  57.784  1.00 19.95 ?  267 ASP A CG  1 
ATOM   1995 O  OD1 . ASP A 1 267 ? 35.836 24.686  57.462  1.00 21.34 ?  267 ASP A OD1 1 
ATOM   1996 O  OD2 . ASP A 1 267 ? 36.900 25.855  58.986  1.00 21.44 -1 267 ASP A OD2 1 
ATOM   1997 N  N   . ALA A 1 268 ? 39.039 26.925  54.127  1.00 21.83 ?  268 ALA A N   1 
ATOM   1998 C  CA  . ALA A 1 268 ? 39.580 27.898  53.182  1.00 27.17 ?  268 ALA A CA  1 
ATOM   1999 C  C   . ALA A 1 268 ? 39.252 27.528  51.741  1.00 31.29 ?  268 ALA A C   1 
ATOM   2000 O  O   . ALA A 1 268 ? 39.020 28.412  50.909  1.00 28.32 ?  268 ALA A O   1 
ATOM   2001 C  CB  . ALA A 1 268 ? 41.090 28.029  53.368  1.00 24.48 ?  268 ALA A CB  1 
ATOM   2002 N  N   . ALA A 1 269 ? 39.235 26.230  51.416  1.00 24.18 ?  269 ALA A N   1 
ATOM   2003 C  CA  . ALA A 1 269 ? 38.896 25.839  50.050  1.00 25.53 ?  269 ALA A CA  1 
ATOM   2004 C  C   . ALA A 1 269 ? 37.408 26.020  49.784  1.00 31.72 ?  269 ALA A C   1 
ATOM   2005 O  O   . ALA A 1 269 ? 37.011 26.402  48.678  1.00 33.73 ?  269 ALA A O   1 
ATOM   2006 C  CB  . ALA A 1 269 ? 39.316 24.389  49.784  1.00 24.22 ?  269 ALA A CB  1 
ATOM   2007 N  N   . ALA A 1 270 ? 36.566 25.743  50.782  1.00 29.46 ?  270 ALA A N   1 
ATOM   2008 C  CA  . ALA A 1 270 ? 35.136 25.964  50.611  1.00 35.01 ?  270 ALA A CA  1 
ATOM   2009 C  C   . ALA A 1 270 ? 34.801 27.443  50.457  1.00 36.33 ?  270 ALA A C   1 
ATOM   2010 O  O   . ALA A 1 270 ? 33.769 27.773  49.864  1.00 42.92 ?  270 ALA A O   1 
ATOM   2011 C  CB  . ALA A 1 270 ? 34.365 25.363  51.788  1.00 31.72 ?  270 ALA A CB  1 
ATOM   2012 N  N   . ALA A 1 271 ? 35.658 28.332  50.956  1.00 35.56 ?  271 ALA A N   1 
ATOM   2013 C  CA  . ALA A 1 271 ? 35.424 29.767  50.898  1.00 39.19 ?  271 ALA A CA  1 
ATOM   2014 C  C   . ALA A 1 271 ? 35.876 30.404  49.589  1.00 47.34 ?  271 ALA A C   1 
ATOM   2015 O  O   . ALA A 1 271 ? 35.485 31.544  49.314  1.00 50.38 ?  271 ALA A O   1 
ATOM   2016 C  CB  . ALA A 1 271 ? 36.126 30.463  52.071  1.00 42.05 ?  271 ALA A CB  1 
ATOM   2017 N  N   . ARG A 1 272 ? 36.679 29.714  48.779  1.00 46.51 ?  272 ARG A N   1 
ATOM   2018 C  CA  . ARG A 1 272 ? 37.088 30.252  47.477  1.00 51.22 ?  272 ARG A CA  1 
ATOM   2019 C  C   . ARG A 1 272 ? 35.896 30.343  46.527  1.00 50.78 ?  272 ARG A C   1 
ATOM   2020 O  O   . ARG A 1 272 ? 35.784 31.287  45.743  1.00 62.11 ?  272 ARG A O   1 
ATOM   2021 C  CB  . ARG A 1 272 ? 38.191 29.395  46.842  1.00 45.71 ?  272 ARG A CB  1 
ATOM   2022 C  CG  . ARG A 1 272 ? 39.301 28.971  47.796  1.00 46.74 ?  272 ARG A CG  1 
ATOM   2023 C  CD  . ARG A 1 272 ? 40.542 28.513  47.030  1.00 46.27 ?  272 ARG A CD  1 
ATOM   2024 N  NE  . ARG A 1 272 ? 41.395 27.617  47.815  1.00 44.43 ?  272 ARG A NE  1 
ATOM   2025 C  CZ  . ARG A 1 272 ? 41.527 26.307  47.594  1.00 42.56 ?  272 ARG A CZ  1 
ATOM   2026 N  NH1 . ARG A 1 272 ? 40.858 25.724  46.602  1.00 44.82 ?  272 ARG A NH1 1 
ATOM   2027 N  NH2 . ARG A 1 272 ? 42.337 25.576  48.364  1.00 39.48 ?  272 ARG A NH2 1 
ATOM   2028 N  N   . MET B 1 1   ? 41.414 1.803   73.133  1.00 37.20 ?  1   MET B N   1 
ATOM   2029 C  CA  . MET B 1 1   ? 42.276 1.393   72.029  1.00 33.95 ?  1   MET B CA  1 
ATOM   2030 C  C   . MET B 1 1   ? 43.363 0.448   72.494  1.00 25.65 ?  1   MET B C   1 
ATOM   2031 O  O   . MET B 1 1   ? 43.379 0.000   73.637  1.00 26.77 ?  1   MET B O   1 
ATOM   2032 C  CB  . MET B 1 1   ? 42.964 2.587   71.369  1.00 38.25 ?  1   MET B CB  1 
ATOM   2033 C  CG  . MET B 1 1   ? 42.072 3.667   70.850  1.00 46.83 ?  1   MET B CG  1 
ATOM   2034 S  SD  . MET B 1 1   ? 42.898 5.264   70.932  1.00 66.62 ?  1   MET B SD  1 
ATOM   2035 C  CE  . MET B 1 1   ? 44.594 4.721   70.772  1.00 46.70 ?  1   MET B CE  1 
ATOM   2036 N  N   . ILE B 1 2   ? 44.309 0.202   71.595  1.00 26.79 ?  2   ILE B N   1 
ATOM   2037 C  CA  . ILE B 1 2   ? 45.474 -0.627  71.868  1.00 19.46 ?  2   ILE B CA  1 
ATOM   2038 C  C   . ILE B 1 2   ? 46.704 0.264   71.967  1.00 21.33 ?  2   ILE B C   1 
ATOM   2039 O  O   . ILE B 1 2   ? 46.923 1.131   71.112  1.00 22.79 ?  2   ILE B O   1 
ATOM   2040 C  CB  . ILE B 1 2   ? 45.651 -1.695  70.779  1.00 20.87 ?  2   ILE B CB  1 
ATOM   2041 C  CG1 . ILE B 1 2   ? 44.443 -2.644  70.778  1.00 23.78 ?  2   ILE B CG1 1 
ATOM   2042 C  CG2 . ILE B 1 2   ? 46.986 -2.435  70.973  1.00 20.06 ?  2   ILE B CG2 1 
ATOM   2043 C  CD1 . ILE B 1 2   ? 44.445 -3.627  69.624  1.00 21.83 ?  2   ILE B CD1 1 
ATOM   2044 N  N   . ASP B 1 3   ? 47.509 0.036   73.003  1.00 20.06 ?  3   ASP B N   1 
ATOM   2045 C  CA  . ASP B 1 3   ? 48.781 0.714   73.256  1.00 20.42 ?  3   ASP B CA  1 
ATOM   2046 C  C   . ASP B 1 3   ? 49.891 -0.293  72.982  1.00 17.96 ?  3   ASP B C   1 
ATOM   2047 O  O   . ASP B 1 3   ? 50.174 -1.127  73.839  1.00 21.04 ?  3   ASP B O   1 
ATOM   2048 C  CB  . ASP B 1 3   ? 48.871 1.145   74.712  1.00 25.80 ?  3   ASP B CB  1 
ATOM   2049 C  CG  . ASP B 1 3   ? 48.700 2.612   74.909  1.00 33.28 ?  3   ASP B CG  1 
ATOM   2050 O  OD1 . ASP B 1 3   ? 48.274 3.307   73.959  1.00 34.23 ?  3   ASP B OD1 1 
ATOM   2051 O  OD2 . ASP B 1 3   ? 48.983 3.051   76.049  1.00 31.20 -1 3   ASP B OD2 1 
ATOM   2052 N  N   . LEU B 1 4   ? 50.552 -0.195  71.825  1.00 16.09 ?  4   LEU B N   1 
ATOM   2053 C  CA  . LEU B 1 4   ? 51.549 -1.182  71.413  1.00 14.17 ?  4   LEU B CA  1 
ATOM   2054 C  C   . LEU B 1 4   ? 52.966 -0.717  71.760  1.00 17.35 ?  4   LEU B C   1 
ATOM   2055 O  O   . LEU B 1 4   ? 53.444 0.295   71.225  1.00 16.02 ?  4   LEU B O   1 
ATOM   2056 C  CB  . LEU B 1 4   ? 51.424 -1.447  69.910  1.00 14.44 ?  4   LEU B CB  1 
ATOM   2057 C  CG  . LEU B 1 4   ? 52.419 -2.448  69.313  1.00 15.49 ?  4   LEU B CG  1 
ATOM   2058 C  CD1 . LEU B 1 4   ? 52.299 -3.828  69.955  1.00 15.24 ?  4   LEU B CD1 1 
ATOM   2059 C  CD2 . LEU B 1 4   ? 52.186 -2.521  67.808  1.00 15.00 ?  4   LEU B CD2 1 
ATOM   2060 N  N   . ILE B 1 5   ? 53.638 -1.470  72.633  1.00 14.35 ?  5   ILE B N   1 
ATOM   2061 C  CA  . ILE B 1 5   ? 55.006 -1.195  73.061  1.00 14.75 ?  5   ILE B CA  1 
ATOM   2062 C  C   . ILE B 1 5   ? 55.855 -2.404  72.682  1.00 15.61 ?  5   ILE B C   1 
ATOM   2063 O  O   . ILE B 1 5   ? 55.456 -3.540  72.941  1.00 16.58 ?  5   ILE B O   1 
ATOM   2064 C  CB  . ILE B 1 5   ? 55.068 -0.931  74.577  1.00 15.54 ?  5   ILE B CB  1 
ATOM   2065 C  CG1 . ILE B 1 5   ? 54.144 0.236   74.948  1.00 19.37 ?  5   ILE B CG1 1 
ATOM   2066 C  CG2 . ILE B 1 5   ? 56.506 -0.679  75.028  1.00 16.25 ?  5   ILE B CG2 1 
ATOM   2067 C  CD1 . ILE B 1 5   ? 53.840 0.314   76.438  1.00 21.93 ?  5   ILE B CD1 1 
ATOM   2068 N  N   . VAL B 1 6   ? 57.015 -2.167  72.075  1.00 10.77 ?  6   VAL B N   1 
ATOM   2069 C  CA  . VAL B 1 6   ? 57.828 -3.240  71.504  1.00 11.11 ?  6   VAL B CA  1 
ATOM   2070 C  C   . VAL B 1 6   ? 59.248 -3.134  72.042  1.00 12.42 ?  6   VAL B C   1 
ATOM   2071 O  O   . VAL B 1 6   ? 59.919 -2.124  71.821  1.00 14.72 ?  6   VAL B O   1 
ATOM   2072 C  CB  . VAL B 1 6   ? 57.855 -3.176  69.970  1.00 12.76 ?  6   VAL B CB  1 
ATOM   2073 C  CG1 . VAL B 1 6   ? 58.527 -4.438  69.389  1.00 12.82 ?  6   VAL B CG1 1 
ATOM   2074 C  CG2 . VAL B 1 6   ? 56.455 -2.980  69.430  1.00 13.34 ?  6   VAL B CG2 1 
ATOM   2075 N  N   . SER B 1 7   ? 59.717 -4.180  72.719  1.00 11.76 ?  7   SER B N   1 
ATOM   2076 C  CA  . SER B 1 7   ? 61.097 -4.188  73.199  1.00 12.41 ?  7   SER B CA  1 
ATOM   2077 C  C   . SER B 1 7   ? 62.045 -4.592  72.076  1.00 16.84 ?  7   SER B C   1 
ATOM   2078 O  O   . SER B 1 7   ? 61.815 -5.597  71.392  1.00 15.76 ?  7   SER B O   1 
ATOM   2079 C  CB  . SER B 1 7   ? 61.251 -5.148  74.375  1.00 18.13 ?  7   SER B CB  1 
ATOM   2080 O  OG  . SER B 1 7   ? 62.625 -5.261  74.715  1.00 21.47 ?  7   SER B OG  1 
ATOM   2081 N  N   . GLN B 1 8   ? 63.117 -3.806  71.886  1.00 13.77 ?  8   GLN B N   1 
ATOM   2082 C  CA  . GLN B 1 8   ? 64.125 -4.078  70.866  1.00 16.90 ?  8   GLN B CA  1 
ATOM   2083 C  C   . GLN B 1 8   ? 65.534 -4.109  71.453  1.00 20.18 ?  8   GLN B C   1 
ATOM   2084 O  O   . GLN B 1 8   ? 66.510 -4.184  70.696  1.00 21.00 ?  8   GLN B O   1 
ATOM   2085 C  CB  . GLN B 1 8   ? 64.040 -3.041  69.732  1.00 16.69 ?  8   GLN B CB  1 
ATOM   2086 C  CG  . GLN B 1 8   ? 62.762 -3.213  68.847  1.00 14.71 ?  8   GLN B CG  1 
ATOM   2087 C  CD  . GLN B 1 8   ? 62.852 -4.427  67.933  1.00 11.67 ?  8   GLN B CD  1 
ATOM   2088 O  OE1 . GLN B 1 8   ? 63.443 -4.353  66.851  1.00 16.35 ?  8   GLN B OE1 1 
ATOM   2089 N  NE2 . GLN B 1 8   ? 62.278 -5.560  68.363  1.00 14.34 ?  8   GLN B NE2 1 
ATOM   2090 N  N   . GLY B 1 9   ? 65.664 -4.053  72.773  1.00 17.17 ?  9   GLY B N   1 
ATOM   2091 C  CA  . GLY B 1 9   ? 66.957 -4.151  73.425  1.00 16.76 ?  9   GLY B CA  1 
ATOM   2092 C  C   . GLY B 1 9   ? 67.171 -5.568  73.917  1.00 17.89 ?  9   GLY B C   1 
ATOM   2093 O  O   . GLY B 1 9   ? 66.218 -6.264  74.263  1.00 19.44 ?  9   GLY B O   1 
ATOM   2094 N  N   . ARG B 1 10  ? 68.432 -5.997  73.955  1.00 15.30 ?  10  ARG B N   1 
ATOM   2095 C  CA  . ARG B 1 10  ? 68.718 -7.339  74.446  1.00 16.61 ?  10  ARG B CA  1 
ATOM   2096 C  C   . ARG B 1 10  ? 68.394 -7.432  75.933  1.00 14.91 ?  10  ARG B C   1 
ATOM   2097 O  O   . ARG B 1 10  ? 68.809 -6.580  76.725  1.00 17.05 ?  10  ARG B O   1 
ATOM   2098 C  CB  . ARG B 1 10  ? 70.182 -7.710  74.216  1.00 20.91 ?  10  ARG B CB  1 
ATOM   2099 C  CG  . ARG B 1 10  ? 70.519 -9.036  74.873  1.00 19.22 ?  10  ARG B CG  1 
ATOM   2100 C  CD  . ARG B 1 10  ? 71.859 -9.605  74.455  1.00 21.02 ?  10  ARG B CD  1 
ATOM   2101 N  NE  . ARG B 1 10  ? 71.967 -10.984 74.924  1.00 18.67 ?  10  ARG B NE  1 
ATOM   2102 C  CZ  . ARG B 1 10  ? 72.673 -11.375 75.988  1.00 21.04 ?  10  ARG B CZ  1 
ATOM   2103 N  NH1 . ARG B 1 10  ? 73.362 -10.494 76.709  1.00 22.71 ?  10  ARG B NH1 1 
ATOM   2104 N  NH2 . ARG B 1 10  ? 72.686 -12.652 76.330  1.00 20.26 ?  10  ARG B NH2 1 
ATOM   2105 N  N   . VAL B 1 11  ? 67.644 -8.470  76.313  1.00 15.40 ?  11  VAL B N   1 
ATOM   2106 C  CA  . VAL B 1 11  ? 67.490 -8.823  77.719  1.00 15.34 ?  11  VAL B CA  1 
ATOM   2107 C  C   . VAL B 1 11  ? 67.756 -10.314 77.826  1.00 18.33 ?  11  VAL B C   1 
ATOM   2108 O  O   . VAL B 1 11  ? 66.824 -11.128 77.812  1.00 16.42 ?  11  VAL B O   1 
ATOM   2109 C  CB  . VAL B 1 11  ? 66.105 -8.442  78.289  1.00 15.75 ?  11  VAL B CB  1 
ATOM   2110 C  CG1 . VAL B 1 11  ? 66.083 -8.651  79.805  1.00 15.88 ?  11  VAL B CG1 1 
ATOM   2111 C  CG2 . VAL B 1 11  ? 65.791 -6.987  77.971  1.00 19.64 ?  11  VAL B CG2 1 
ATOM   2112 N  N   . ALA B 1 12  ? 69.043 -10.673 77.894  1.00 16.88 ?  12  ALA B N   1 
ATOM   2113 C  CA  . ALA B 1 12  ? 69.549 -12.032 78.060  1.00 16.17 ?  12  ALA B CA  1 
ATOM   2114 C  C   . ALA B 1 12  ? 69.333 -12.941 76.850  1.00 20.43 ?  12  ALA B C   1 
ATOM   2115 O  O   . ALA B 1 12  ? 69.537 -14.160 76.976  1.00 17.88 ?  12  ALA B O   1 
ATOM   2116 C  CB  . ALA B 1 12  ? 68.956 -12.709 79.312  1.00 17.28 ?  12  ALA B CB  1 
ATOM   2117 N  N   . ASP B 1 13  ? 68.943 -12.403 75.679  1.00 16.26 ?  13  ASP B N   1 
ATOM   2118 C  CA  . ASP B 1 13  ? 68.679 -13.249 74.513  1.00 16.58 ?  13  ASP B CA  1 
ATOM   2119 C  C   . ASP B 1 13  ? 69.821 -14.221 74.242  1.00 15.25 ?  13  ASP B C   1 
ATOM   2120 O  O   . ASP B 1 13  ? 70.973 -13.811 74.087  1.00 17.51 ?  13  ASP B O   1 
ATOM   2121 C  CB  . ASP B 1 13  ? 68.488 -12.415 73.239  1.00 16.01 ?  13  ASP B CB  1 
ATOM   2122 C  CG  . ASP B 1 13  ? 67.500 -11.263 73.386  1.00 21.04 ?  13  ASP B CG  1 
ATOM   2123 O  OD1 . ASP B 1 13  ? 67.429 -10.621 74.463  1.00 16.90 ?  13  ASP B OD1 1 
ATOM   2124 O  OD2 . ASP B 1 13  ? 66.818 -10.975 72.364  1.00 20.91 -1 13  ASP B OD2 1 
ATOM   2125 N  N   . ARG B 1 14  ? 69.487 -15.506 74.134  1.00 16.52 ?  14  ARG B N   1 
ATOM   2126 C  CA  . ARG B 1 14  ? 70.448 -16.504 73.694  1.00 20.71 ?  14  ARG B CA  1 
ATOM   2127 C  C   . ARG B 1 14  ? 70.200 -16.981 72.272  1.00 23.46 ?  14  ARG B C   1 
ATOM   2128 O  O   . ARG B 1 14  ? 71.117 -17.544 71.663  1.00 23.67 ?  14  ARG B O   1 
ATOM   2129 C  CB  . ARG B 1 14  ? 70.451 -17.714 74.648  1.00 18.85 ?  14  ARG B CB  1 
ATOM   2130 C  CG  . ARG B 1 14  ? 70.787 -17.344 76.104  1.00 19.18 ?  14  ARG B CG  1 
ATOM   2131 C  CD  . ARG B 1 14  ? 71.104 -18.557 76.956  1.00 20.47 ?  14  ARG B CD  1 
ATOM   2132 N  NE  . ARG B 1 14  ? 71.697 -18.179 78.236  1.00 19.51 ?  14  ARG B NE  1 
ATOM   2133 C  CZ  . ARG B 1 14  ? 71.966 -19.049 79.205  1.00 22.55 ?  14  ARG B CZ  1 
ATOM   2134 N  NH1 . ARG B 1 14  ? 71.674 -20.331 79.030  1.00 21.91 ?  14  ARG B NH1 1 
ATOM   2135 N  NH2 . ARG B 1 14  ? 72.503 -18.632 80.343  1.00 20.60 ?  14  ARG B NH2 1 
ATOM   2136 N  N   . ALA B 1 15  ? 69.014 -16.740 71.714  1.00 21.20 ?  15  ALA B N   1 
ATOM   2137 C  CA  . ALA B 1 15  ? 68.728 -17.050 70.317  1.00 23.46 ?  15  ALA B CA  1 
ATOM   2138 C  C   . ALA B 1 15  ? 68.908 -15.805 69.449  1.00 22.19 ?  15  ALA B C   1 
ATOM   2139 O  O   . ALA B 1 15  ? 68.791 -14.672 69.914  1.00 23.42 ?  15  ALA B O   1 
ATOM   2140 C  CB  . ALA B 1 15  ? 67.310 -17.618 70.149  1.00 23.97 ?  15  ALA B CB  1 
ATOM   2141 N  N   . ALA B 1 16  ? 69.192 -16.036 68.162  1.00 20.93 ?  16  ALA B N   1 
ATOM   2142 C  CA  . ALA B 1 16  ? 69.620 -14.951 67.283  1.00 21.68 ?  16  ALA B CA  1 
ATOM   2143 C  C   . ALA B 1 16  ? 68.488 -14.030 66.845  1.00 18.75 ?  16  ALA B C   1 
ATOM   2144 O  O   . ALA B 1 16  ? 68.749 -12.865 66.523  1.00 18.15 ?  16  ALA B O   1 
ATOM   2145 C  CB  . ALA B 1 16  ? 70.295 -15.519 66.032  1.00 20.78 ?  16  ALA B CB  1 
ATOM   2146 N  N   . TRP B 1 17  ? 67.248 -14.517 66.784  1.00 15.92 ?  17  TRP B N   1 
ATOM   2147 C  CA  . TRP B 1 17  ? 66.205 -13.784 66.060  1.00 16.70 ?  17  TRP B CA  1 
ATOM   2148 C  C   . TRP B 1 17  ? 65.006 -13.446 66.941  1.00 18.69 ?  17  TRP B C   1 
ATOM   2149 O  O   . TRP B 1 17  ? 63.891 -13.311 66.445  1.00 15.33 ?  17  TRP B O   1 
ATOM   2150 C  CB  . TRP B 1 17  ? 65.731 -14.564 64.836  1.00 17.63 ?  17  TRP B CB  1 
ATOM   2151 C  CG  . TRP B 1 17  ? 66.821 -15.127 63.991  1.00 19.08 ?  17  TRP B CG  1 
ATOM   2152 C  CD1 . TRP B 1 17  ? 67.760 -14.435 63.276  1.00 23.63 ?  17  TRP B CD1 1 
ATOM   2153 C  CD2 . TRP B 1 17  ? 67.087 -16.517 63.772  1.00 22.66 ?  17  TRP B CD2 1 
ATOM   2154 N  NE1 . TRP B 1 17  ? 68.597 -15.323 62.628  1.00 22.95 ?  17  TRP B NE1 1 
ATOM   2155 C  CE2 . TRP B 1 17  ? 68.198 -16.602 62.915  1.00 24.84 ?  17  TRP B CE2 1 
ATOM   2156 C  CE3 . TRP B 1 17  ? 66.478 -17.698 64.208  1.00 23.86 ?  17  TRP B CE3 1 
ATOM   2157 C  CZ2 . TRP B 1 17  ? 68.725 -17.830 62.493  1.00 31.21 ?  17  TRP B CZ2 1 
ATOM   2158 C  CZ3 . TRP B 1 17  ? 67.002 -18.918 63.791  1.00 29.27 ?  17  TRP B CZ3 1 
ATOM   2159 C  CH2 . TRP B 1 17  ? 68.112 -18.972 62.942  1.00 28.21 ?  17  TRP B CH2 1 
ATOM   2160 N  N   . MET B 1 18  ? 65.209 -13.278 68.242  1.00 13.69 ?  18  MET B N   1 
ATOM   2161 C  CA  . MET B 1 18  ? 64.060 -12.910 69.065  1.00 14.17 ?  18  MET B CA  1 
ATOM   2162 C  C   . MET B 1 18  ? 63.769 -11.407 69.012  1.00 13.12 ?  18  MET B C   1 
ATOM   2163 O  O   . MET B 1 18  ? 62.611 -11.001 69.179  1.00 12.46 ?  18  MET B O   1 
ATOM   2164 C  CB  . MET B 1 18  ? 64.263 -13.416 70.495  1.00 17.91 ?  18  MET B CB  1 
ATOM   2165 C  CG  . MET B 1 18  ? 63.790 -14.896 70.652  1.00 20.41 ?  18  MET B CG  1 
ATOM   2166 S  SD  . MET B 1 18  ? 64.186 -15.628 72.238  1.00 37.05 ?  18  MET B SD  1 
ATOM   2167 C  CE  . MET B 1 18  ? 65.865 -15.066 72.338  1.00 18.15 ?  18  MET B CE  1 
ATOM   2168 N  N   . ILE B 1 19  ? 64.774 -10.569 68.746  1.00 12.06 ?  19  ILE B N   1 
ATOM   2169 C  CA  . ILE B 1 19  ? 64.483 -9.151  68.563  1.00 14.96 ?  19  ILE B CA  1 
ATOM   2170 C  C   . ILE B 1 19  ? 63.790 -8.939  67.221  1.00 13.60 ?  19  ILE B C   1 
ATOM   2171 O  O   . ILE B 1 19  ? 62.787 -8.219  67.134  1.00 13.41 ?  19  ILE B O   1 
ATOM   2172 C  CB  . ILE B 1 19  ? 65.762 -8.301  68.699  1.00 14.74 ?  19  ILE B CB  1 
ATOM   2173 C  CG1 . ILE B 1 19  ? 66.221 -8.292  70.170  1.00 16.16 ?  19  ILE B CG1 1 
ATOM   2174 C  CG2 . ILE B 1 19  ? 65.525 -6.898  68.174  1.00 15.01 ?  19  ILE B CG2 1 
ATOM   2175 C  CD1 . ILE B 1 19  ? 67.530 -7.539  70.430  1.00 20.70 ?  19  ILE B CD1 1 
ATOM   2176 N  N   . GLU B 1 20  ? 64.265 -9.613  66.167  1.00 12.35 ?  20  GLU B N   1 
ATOM   2177 C  CA  . GLU B 1 20  ? 63.539 -9.566  64.893  1.00 16.42 ?  20  GLU B CA  1 
ATOM   2178 C  C   . GLU B 1 20  ? 62.147 -10.164 65.017  1.00 16.77 ?  20  GLU B C   1 
ATOM   2179 O  O   . GLU B 1 20  ? 61.196 -9.679  64.385  1.00 15.17 ?  20  GLU B O   1 
ATOM   2180 C  CB  . GLU B 1 20  ? 64.318 -10.300 63.793  1.00 18.72 ?  20  GLU B CB  1 
ATOM   2181 C  CG  . GLU B 1 20  ? 65.491 -9.484  63.289  1.00 20.13 ?  20  GLU B CG  1 
ATOM   2182 C  CD  . GLU B 1 20  ? 66.125 -10.053 62.024  1.00 30.08 ?  20  GLU B CD  1 
ATOM   2183 O  OE1 . GLU B 1 20  ? 65.391 -10.552 61.139  1.00 22.11 ?  20  GLU B OE1 1 
ATOM   2184 O  OE2 . GLU B 1 20  ? 67.372 -9.990  61.923  1.00 38.50 -1 20  GLU B OE2 1 
ATOM   2185 N  N   . GLY B 1 21  ? 62.007 -11.243 65.791  1.00 11.31 ?  21  GLY B N   1 
ATOM   2186 C  CA  . GLY B 1 21  ? 60.694 -11.856 65.940  1.00 13.40 ?  21  GLY B CA  1 
ATOM   2187 C  C   . GLY B 1 21  ? 59.694 -10.911 66.579  1.00 14.79 ?  21  GLY B C   1 
ATOM   2188 O  O   . GLY B 1 21  ? 58.521 -10.862 66.188  1.00 12.48 ?  21  GLY B O   1 
ATOM   2189 N  N   . ALA B 1 22  ? 60.143 -10.156 67.578  1.00 14.05 ?  22  ALA B N   1 
ATOM   2190 C  CA  . ALA B 1 22  ? 59.272 -9.177  68.208  1.00 13.10 ?  22  ALA B CA  1 
ATOM   2191 C  C   . ALA B 1 22  ? 58.903 -8.080  67.227  1.00 12.65 ?  22  ALA B C   1 
ATOM   2192 O  O   . ALA B 1 22  ? 57.741 -7.669  67.158  1.00 12.75 ?  22  ALA B O   1 
ATOM   2193 C  CB  . ALA B 1 22  ? 59.951 -8.593  69.447  1.00 12.51 ?  22  ALA B CB  1 
ATOM   2194 N  N   . ALA B 1 23  ? 59.873 -7.615  66.430  1.00 12.47 ?  23  ALA B N   1 
ATOM   2195 C  CA  . ALA B 1 23  ? 59.563 -6.571  65.456  1.00 12.99 ?  23  ALA B CA  1 
ATOM   2196 C  C   . ALA B 1 23  ? 58.569 -7.076  64.412  1.00 13.87 ?  23  ALA B C   1 
ATOM   2197 O  O   . ALA B 1 23  ? 57.667 -6.338  63.995  1.00 13.78 ?  23  ALA B O   1 
ATOM   2198 C  CB  . ALA B 1 23  ? 60.848 -6.071  64.787  1.00 13.43 ?  23  ALA B CB  1 
ATOM   2199 N  N   . ARG B 1 24  ? 58.717 -8.330  63.980  1.00 12.64 ?  24  ARG B N   1 
ATOM   2200 C  CA  . ARG B 1 24  ? 57.827 -8.884  62.960  1.00 12.27 ?  24  ARG B CA  1 
ATOM   2201 C  C   . ARG B 1 24  ? 56.421 -9.097  63.513  1.00 14.02 ?  24  ARG B C   1 
ATOM   2202 O  O   . ARG B 1 24  ? 55.423 -8.871  62.807  1.00 12.81 ?  24  ARG B O   1 
ATOM   2203 C  CB  . ARG B 1 24  ? 58.409 -10.195 62.432  1.00 12.86 ?  24  ARG B CB  1 
ATOM   2204 C  CG  . ARG B 1 24  ? 57.581 -10.843 61.343  1.00 15.20 ?  24  ARG B CG  1 
ATOM   2205 C  CD  . ARG B 1 24  ? 57.404 -9.870  60.171  1.00 16.49 ?  24  ARG B CD  1 
ATOM   2206 N  NE  . ARG B 1 24  ? 56.710 -10.563 59.094  1.00 20.75 ?  24  ARG B NE  1 
ATOM   2207 C  CZ  . ARG B 1 24  ? 55.395 -10.591 58.956  1.00 21.78 ?  24  ARG B CZ  1 
ATOM   2208 N  NH1 . ARG B 1 24  ? 54.616 -9.931  59.817  1.00 17.57 ?  24  ARG B NH1 1 
ATOM   2209 N  NH2 . ARG B 1 24  ? 54.861 -11.265 57.947  1.00 24.84 ?  24  ARG B NH2 1 
ATOM   2210 N  N   . THR B 1 25  ? 56.323 -9.529  64.773  1.00 10.07 ?  25  THR B N   1 
ATOM   2211 C  CA  . THR B 1 25  ? 55.016 -9.635  65.417  1.00 11.66 ?  25  THR B CA  1 
ATOM   2212 C  C   . THR B 1 25  ? 54.362 -8.264  65.534  1.00 11.87 ?  25  THR B C   1 
ATOM   2213 O  O   . THR B 1 25  ? 53.168 -8.106  65.257  1.00 10.83 ?  25  THR B O   1 
ATOM   2214 C  CB  . THR B 1 25  ? 55.153 -10.271 66.806  1.00 12.74 ?  25  THR B CB  1 
ATOM   2215 O  OG1 . THR B 1 25  ? 55.764 -11.560 66.687  1.00 13.06 ?  25  THR B OG1 1 
ATOM   2216 C  CG2 . THR B 1 25  ? 53.770 -10.420 67.469  1.00 14.70 ?  25  THR B CG2 1 
ATOM   2217 N  N   . ALA B 1 26  ? 55.136 -7.259  65.950  1.00 11.32 ?  26  ALA B N   1 
ATOM   2218 C  CA  . ALA B 1 26  ? 54.584 -5.921  66.102  1.00 11.09 ?  26  ALA B CA  1 
ATOM   2219 C  C   . ALA B 1 26  ? 54.102 -5.382  64.762  1.00 9.88  ?  26  ALA B C   1 
ATOM   2220 O  O   . ALA B 1 26  ? 53.026 -4.788  64.679  1.00 11.67 ?  26  ALA B O   1 
ATOM   2221 C  CB  . ALA B 1 26  ? 55.625 -4.981  66.700  1.00 12.60 ?  26  ALA B CB  1 
ATOM   2222 N  N   . ARG B 1 27  ? 54.868 -5.607  63.695  1.00 12.31 ?  27  ARG B N   1 
ATOM   2223 C  CA  . ARG B 1 27  ? 54.428 -5.120  62.390  1.00 13.98 ?  27  ARG B CA  1 
ATOM   2224 C  C   . ARG B 1 27  ? 53.145 -5.819  61.946  1.00 12.90 ?  27  ARG B C   1 
ATOM   2225 O  O   . ARG B 1 27  ? 52.267 -5.198  61.337  1.00 13.62 ?  27  ARG B O   1 
ATOM   2226 C  CB  . ARG B 1 27  ? 55.533 -5.305  61.344  1.00 16.25 ?  27  ARG B CB  1 
ATOM   2227 C  CG  . ARG B 1 27  ? 55.182 -4.710  59.944  1.00 19.87 ?  27  ARG B CG  1 
ATOM   2228 C  CD  . ARG B 1 27  ? 55.062 -3.165  59.940  1.00 31.57 ?  27  ARG B CD  1 
ATOM   2229 N  NE  . ARG B 1 27  ? 56.320 -2.524  60.312  1.00 36.18 ?  27  ARG B NE  1 
ATOM   2230 C  CZ  . ARG B 1 27  ? 57.164 -1.952  59.455  1.00 33.46 ?  27  ARG B CZ  1 
ATOM   2231 N  NH1 . ARG B 1 27  ? 56.887 -1.918  58.158  1.00 38.27 ?  27  ARG B NH1 1 
ATOM   2232 N  NH2 . ARG B 1 27  ? 58.289 -1.410  59.906  1.00 39.35 ?  27  ARG B NH2 1 
ATOM   2233 N  N   . ALA B 1 28  ? 53.018 -7.114  62.238  1.00 13.25 ?  28  ALA B N   1 
ATOM   2234 C  CA  . ALA B 1 28  ? 51.769 -7.806  61.925  1.00 15.13 ?  28  ALA B CA  1 
ATOM   2235 C  C   . ALA B 1 28  ? 50.589 -7.168  62.654  1.00 14.41 ?  28  ALA B C   1 
ATOM   2236 O  O   . ALA B 1 28  ? 49.503 -7.013  62.082  1.00 12.22 ?  28  ALA B O   1 
ATOM   2237 C  CB  . ALA B 1 28  ? 51.887 -9.277  62.296  1.00 14.01 ?  28  ALA B CB  1 
ATOM   2238 N  N   . LEU B 1 29  ? 50.786 -6.803  63.916  1.00 9.49  ?  29  LEU B N   1 
ATOM   2239 C  CA  . LEU B 1 29  ? 49.729 -6.132  64.677  1.00 9.41  ?  29  LEU B CA  1 
ATOM   2240 C  C   . LEU B 1 29  ? 49.466 -4.734  64.151  1.00 11.84 ?  29  LEU B C   1 
ATOM   2241 O  O   . LEU B 1 29  ? 48.320 -4.269  64.154  1.00 10.86 ?  29  LEU B O   1 
ATOM   2242 C  CB  . LEU B 1 29  ? 50.113 -6.050  66.153  1.00 10.99 ?  29  LEU B CB  1 
ATOM   2243 C  CG  . LEU B 1 29  ? 50.042 -7.367  66.889  1.00 11.89 ?  29  LEU B CG  1 
ATOM   2244 C  CD1 . LEU B 1 29  ? 50.740 -7.210  68.236  1.00 12.26 ?  29  LEU B CD1 1 
ATOM   2245 C  CD2 . LEU B 1 29  ? 48.602 -7.795  67.081  1.00 11.21 ?  29  LEU B CD2 1 
ATOM   2246 N  N   . GLU B 1 30  ? 50.522 -4.028  63.738  1.00 12.95 ?  30  GLU B N   1 
ATOM   2247 C  CA  . GLU B 1 30  ? 50.327 -2.713  63.142  1.00 10.55 ?  30  GLU B CA  1 
ATOM   2248 C  C   . GLU B 1 30  ? 49.446 -2.802  61.905  1.00 12.56 ?  30  GLU B C   1 
ATOM   2249 O  O   . GLU B 1 30  ? 48.552 -1.972  61.705  1.00 14.04 ?  30  GLU B O   1 
ATOM   2250 C  CB  . GLU B 1 30  ? 51.681 -2.090  62.799  1.00 12.30 ?  30  GLU B CB  1 
ATOM   2251 C  CG  . GLU B 1 30  ? 52.471 -1.668  64.039  1.00 11.40 ?  30  GLU B CG  1 
ATOM   2252 C  CD  . GLU B 1 30  ? 53.880 -1.163  63.726  1.00 11.87 ?  30  GLU B CD  1 
ATOM   2253 O  OE1 . GLU B 1 30  ? 54.258 -1.113  62.539  1.00 17.10 ?  30  GLU B OE1 1 
ATOM   2254 O  OE2 . GLU B 1 30  ? 54.605 -0.829  64.695  1.00 18.63 -1 30  GLU B OE2 1 
ATOM   2255 N  N   . GLU B 1 31  ? 49.679 -3.812  61.069  1.00 12.29 ?  31  GLU B N   1 
ATOM   2256 C  CA  . GLU B 1 31  ? 48.927 -3.924  59.816  1.00 12.62 ?  31  GLU B CA  1 
ATOM   2257 C  C   . GLU B 1 31  ? 47.491 -4.366  60.071  1.00 13.94 ?  31  GLU B C   1 
ATOM   2258 O  O   . GLU B 1 31  ? 46.561 -3.897  59.400  1.00 13.65 ?  31  GLU B O   1 
ATOM   2259 C  CB  . GLU B 1 31  ? 49.642 -4.894  58.870  1.00 13.99 ?  31  GLU B CB  1 
ATOM   2260 C  CG  . GLU B 1 31  ? 50.982 -4.360  58.371  1.00 15.37 ?  31  GLU B CG  1 
ATOM   2261 C  CD  . GLU B 1 31  ? 51.827 -5.387  57.608  1.00 17.30 ?  31  GLU B CD  1 
ATOM   2262 O  OE1 . GLU B 1 31  ? 51.442 -6.572  57.503  1.00 19.79 ?  31  GLU B OE1 1 
ATOM   2263 O  OE2 . GLU B 1 31  ? 52.899 -4.986  57.117  1.00 19.52 -1 31  GLU B OE2 1 
ATOM   2264 N  N   . ARG B 1 32  ? 47.292 -5.252  61.042  1.00 13.33 ?  32  ARG B N   1 
ATOM   2265 C  CA  . ARG B 1 32  ? 45.952 -5.764  61.322  1.00 15.04 ?  32  ARG B CA  1 
ATOM   2266 C  C   . ARG B 1 32  ? 45.072 -4.723  62.013  1.00 14.08 ?  32  ARG B C   1 
ATOM   2267 O  O   . ARG B 1 32  ? 43.850 -4.707  61.800  1.00 14.64 ?  32  ARG B O   1 
ATOM   2268 C  CB  . ARG B 1 32  ? 46.062 -7.036  62.178  1.00 15.96 ?  32  ARG B CB  1 
ATOM   2269 C  CG  . ARG B 1 32  ? 44.742 -7.573  62.695  1.00 15.50 ?  32  ARG B CG  1 
ATOM   2270 C  CD  . ARG B 1 32  ? 43.918 -8.175  61.588  1.00 26.41 ?  32  ARG B CD  1 
ATOM   2271 N  NE  . ARG B 1 32  ? 44.360 -9.547  61.349  1.00 23.80 ?  32  ARG B NE  1 
ATOM   2272 C  CZ  . ARG B 1 32  ? 45.077 -9.935  60.305  1.00 30.67 ?  32  ARG B CZ  1 
ATOM   2273 N  NH1 . ARG B 1 32  ? 45.420 -9.054  59.366  1.00 29.01 ?  32  ARG B NH1 1 
ATOM   2274 N  NH2 . ARG B 1 32  ? 45.435 -11.213 60.191  1.00 27.23 ?  32  ARG B NH2 1 
ATOM   2275 N  N   . TYR B 1 33  ? 45.658 -3.830  62.813  1.00 10.71 ?  33  TYR B N   1 
ATOM   2276 C  CA  . TYR B 1 33  ? 44.864 -2.937  63.649  1.00 12.12 ?  33  TYR B CA  1 
ATOM   2277 C  C   . TYR B 1 33  ? 45.050 -1.461  63.326  1.00 13.46 ?  33  TYR B C   1 
ATOM   2278 O  O   . TYR B 1 33  ? 44.400 -0.626  63.958  1.00 14.75 ?  33  TYR B O   1 
ATOM   2279 C  CB  . TYR B 1 33  ? 45.144 -3.207  65.145  1.00 11.00 ?  33  TYR B CB  1 
ATOM   2280 C  CG  . TYR B 1 33  ? 44.581 -4.568  65.526  1.00 14.83 ?  33  TYR B CG  1 
ATOM   2281 C  CD1 . TYR B 1 33  ? 43.202 -4.768  65.554  1.00 14.53 ?  33  TYR B CD1 1 
ATOM   2282 C  CD2 . TYR B 1 33  ? 45.407 -5.660  65.765  1.00 12.46 ?  33  TYR B CD2 1 
ATOM   2283 C  CE1 . TYR B 1 33  ? 42.654 -6.018  65.847  1.00 15.76 ?  33  TYR B CE1 1 
ATOM   2284 C  CE2 . TYR B 1 33  ? 44.862 -6.922  66.060  1.00 13.59 ?  33  TYR B CE2 1 
ATOM   2285 C  CZ  . TYR B 1 33  ? 43.490 -7.080  66.104  1.00 13.83 ?  33  TYR B CZ  1 
ATOM   2286 O  OH  . TYR B 1 33  ? 42.950 -8.322  66.377  1.00 15.46 ?  33  TYR B OH  1 
ATOM   2287 N  N   . GLY B 1 34  ? 45.898 -1.117  62.365  1.00 14.17 ?  34  GLY B N   1 
ATOM   2288 C  CA  . GLY B 1 34  ? 46.079 0.277   61.998  1.00 14.52 ?  34  GLY B CA  1 
ATOM   2289 C  C   . GLY B 1 34  ? 46.884 1.055   63.013  1.00 17.36 ?  34  GLY B C   1 
ATOM   2290 O  O   . GLY B 1 34  ? 46.599 2.241   63.251  1.00 16.45 ?  34  GLY B O   1 
ATOM   2291 N  N   . LEU B 1 35  ? 47.889 0.419   63.613  1.00 13.70 ?  35  LEU B N   1 
ATOM   2292 C  CA  . LEU B 1 35  ? 48.678 0.990   64.698  1.00 14.27 ?  35  LEU B CA  1 
ATOM   2293 C  C   . LEU B 1 35  ? 50.083 1.349   64.229  1.00 12.57 ?  35  LEU B C   1 
ATOM   2294 O  O   . LEU B 1 35  ? 50.553 0.906   63.183  1.00 11.70 ?  35  LEU B O   1 
ATOM   2295 C  CB  . LEU B 1 35  ? 48.797 -0.011  65.861  1.00 13.40 ?  35  LEU B CB  1 
ATOM   2296 C  CG  . LEU B 1 35  ? 47.530 -0.742  66.294  1.00 14.22 ?  35  LEU B CG  1 
ATOM   2297 C  CD1 . LEU B 1 35  ? 47.848 -1.830  67.322  1.00 16.85 ?  35  LEU B CD1 1 
ATOM   2298 C  CD2 . LEU B 1 35  ? 46.572 0.263   66.860  1.00 18.61 ?  35  LEU B CD2 1 
ATOM   2299 N  N   . LYS B 1 36  ? 50.779 2.110   65.073  1.00 14.32 ?  36  LYS B N   1 
ATOM   2300 C  CA  . LYS B 1 36  ? 52.232 2.225   65.007  1.00 12.35 ?  36  LYS B CA  1 
ATOM   2301 C  C   . LYS B 1 36  ? 52.783 1.992   66.404  1.00 12.65 ?  36  LYS B C   1 
ATOM   2302 O  O   . LYS B 1 36  ? 52.434 2.718   67.341  1.00 15.48 ?  36  LYS B O   1 
ATOM   2303 C  CB  . LYS B 1 36  ? 52.676 3.591   64.473  1.00 12.96 ?  36  LYS B CB  1 
ATOM   2304 C  CG  . LYS B 1 36  ? 54.190 3.833   64.544  1.00 13.48 ?  36  LYS B CG  1 
ATOM   2305 C  CD  . LYS B 1 36  ? 54.959 3.072   63.460  1.00 14.17 ?  36  LYS B CD  1 
ATOM   2306 C  CE  . LYS B 1 36  ? 56.458 3.282   63.637  1.00 13.71 ?  36  LYS B CE  1 
ATOM   2307 N  NZ  . LYS B 1 36  ? 57.268 2.644   62.527  1.00 16.72 ?  36  LYS B NZ  1 
ATOM   2308 N  N   . GLY B 1 37  ? 53.631 0.982   66.547  1.00 11.94 ?  37  GLY B N   1 
ATOM   2309 C  CA  . GLY B 1 37  ? 54.168 0.667   67.857  1.00 15.90 ?  37  GLY B CA  1 
ATOM   2310 C  C   . GLY B 1 37  ? 55.163 1.701   68.356  1.00 18.73 ?  37  GLY B C   1 
ATOM   2311 O  O   . GLY B 1 37  ? 55.732 2.481   67.600  1.00 17.16 ?  37  GLY B O   1 
ATOM   2312 N  N   . HIS B 1 38  ? 55.372 1.684   69.671  1.00 16.05 ?  38  HIS B N   1 
ATOM   2313 C  CA  . HIS B 1 38  ? 56.405 2.466   70.350  1.00 18.93 ?  38  HIS B CA  1 
ATOM   2314 C  C   . HIS B 1 38  ? 57.561 1.517   70.666  1.00 20.79 ?  38  HIS B C   1 
ATOM   2315 O  O   . HIS B 1 38  ? 57.385 0.561   71.422  1.00 15.62 ?  38  HIS B O   1 
ATOM   2316 C  CB  . HIS B 1 38  ? 55.820 3.089   71.623  1.00 19.14 ?  38  HIS B CB  1 
ATOM   2317 C  CG  . HIS B 1 38  ? 56.818 3.792   72.496  1.00 27.91 ?  38  HIS B CG  1 
ATOM   2318 N  ND1 . HIS B 1 38  ? 58.057 4.202   72.050  1.00 32.13 ?  38  HIS B ND1 1 
ATOM   2319 C  CD2 . HIS B 1 38  ? 56.744 4.171   73.795  1.00 33.66 ?  38  HIS B CD2 1 
ATOM   2320 C  CE1 . HIS B 1 38  ? 58.710 4.787   73.040  1.00 29.32 ?  38  HIS B CE1 1 
ATOM   2321 N  NE2 . HIS B 1 38  ? 57.932 4.788   74.108  1.00 36.38 ?  38  HIS B NE2 1 
ATOM   2322 N  N   . TYR B 1 39  ? 58.721 1.752   70.060  1.00 15.93 ?  39  TYR B N   1 
ATOM   2323 C  CA  . TYR B 1 39  ? 59.825 0.802   70.099  1.00 17.02 ?  39  TYR B CA  1 
ATOM   2324 C  C   . TYR B 1 39  ? 60.874 1.277   71.092  1.00 19.61 ?  39  TYR B C   1 
ATOM   2325 O  O   . TYR B 1 39  ? 61.319 2.427   71.031  1.00 21.79 ?  39  TYR B O   1 
ATOM   2326 C  CB  . TYR B 1 39  ? 60.430 0.620   68.706  1.00 19.73 ?  39  TYR B CB  1 
ATOM   2327 C  CG  . TYR B 1 39  ? 59.497 -0.084  67.729  1.00 15.64 ?  39  TYR B CG  1 
ATOM   2328 C  CD1 . TYR B 1 39  ? 58.412 0.580   67.176  1.00 18.84 ?  39  TYR B CD1 1 
ATOM   2329 C  CD2 . TYR B 1 39  ? 59.705 -1.403  67.368  1.00 16.49 ?  39  TYR B CD2 1 
ATOM   2330 C  CE1 . TYR B 1 39  ? 57.552 -0.065  66.281  1.00 17.38 ?  39  TYR B CE1 1 
ATOM   2331 C  CE2 . TYR B 1 39  ? 58.859 -2.051  66.493  1.00 18.99 ?  39  TYR B CE2 1 
ATOM   2332 C  CZ  . TYR B 1 39  ? 57.785 -1.367  65.944  1.00 18.14 ?  39  TYR B CZ  1 
ATOM   2333 O  OH  . TYR B 1 39  ? 56.939 -2.009  65.079  1.00 19.10 ?  39  TYR B OH  1 
ATOM   2334 N  N   . VAL B 1 40  ? 61.263 0.392   72.007  1.00 17.46 ?  40  VAL B N   1 
ATOM   2335 C  CA  . VAL B 1 40  ? 62.100 0.748   73.146  1.00 19.84 ?  40  VAL B CA  1 
ATOM   2336 C  C   . VAL B 1 40  ? 63.337 -0.147  73.149  1.00 20.00 ?  40  VAL B C   1 
ATOM   2337 O  O   . VAL B 1 40  ? 63.219 -1.373  73.078  1.00 19.82 ?  40  VAL B O   1 
ATOM   2338 C  CB  . VAL B 1 40  ? 61.319 0.598   74.462  1.00 19.55 ?  40  VAL B CB  1 
ATOM   2339 C  CG1 . VAL B 1 40  ? 62.198 0.930   75.630  1.00 25.47 ?  40  VAL B CG1 1 
ATOM   2340 C  CG2 . VAL B 1 40  ? 60.076 1.483   74.445  1.00 25.93 ?  40  VAL B CG2 1 
ATOM   2341 N  N   . GLY B 1 41  ? 64.514 0.457   73.251  1.00 21.62 ?  41  GLY B N   1 
ATOM   2342 C  CA  . GLY B 1 41  ? 65.713 -0.347  73.386  1.00 23.66 ?  41  GLY B CA  1 
ATOM   2343 C  C   . GLY B 1 41  ? 66.507 -0.453  72.094  1.00 25.52 ?  41  GLY B C   1 
ATOM   2344 O  O   . GLY B 1 41  ? 65.966 -0.378  70.984  1.00 26.78 ?  41  GLY B O   1 
ATOM   2345 N  N   . GLU B 1 42  ? 67.822 -0.663  72.243  1.00 28.73 ?  42  GLU B N   1 
ATOM   2346 C  CA  . GLU B 1 42  ? 68.749 -0.788  71.130  1.00 30.68 ?  42  GLU B CA  1 
ATOM   2347 C  C   . GLU B 1 42  ? 69.190 -2.234  70.992  1.00 22.63 ?  42  GLU B C   1 
ATOM   2348 O  O   . GLU B 1 42  ? 69.576 -2.845  71.996  1.00 24.81 ?  42  GLU B O   1 
ATOM   2349 C  CB  . GLU B 1 42  ? 69.983 0.106   71.348  1.00 35.69 ?  42  GLU B CB  1 
ATOM   2350 C  CG  . GLU B 1 42  ? 69.674 1.583   71.503  1.00 42.41 ?  42  GLU B CG  1 
ATOM   2351 C  CD  . GLU B 1 42  ? 69.544 2.286   70.165  1.00 55.53 ?  42  GLU B CD  1 
ATOM   2352 O  OE1 . GLU B 1 42  ? 70.028 3.433   70.047  1.00 63.20 ?  42  GLU B OE1 1 
ATOM   2353 O  OE2 . GLU B 1 42  ? 68.963 1.686   69.230  1.00 54.02 -1 42  GLU B OE2 1 
ATOM   2354 N  N   . PRO B 1 43  ? 69.162 -2.813  69.795  1.00 25.82 ?  43  PRO B N   1 
ATOM   2355 C  CA  . PRO B 1 43  ? 69.547 -4.221  69.660  1.00 24.54 ?  43  PRO B CA  1 
ATOM   2356 C  C   . PRO B 1 43  ? 71.023 -4.435  69.943  1.00 29.45 ?  43  PRO B C   1 
ATOM   2357 O  O   . PRO B 1 43  ? 71.861 -3.561  69.711  1.00 26.75 ?  43  PRO B O   1 
ATOM   2358 C  CB  . PRO B 1 43  ? 69.206 -4.550  68.202  1.00 28.36 ?  43  PRO B CB  1 
ATOM   2359 C  CG  . PRO B 1 43  ? 68.172 -3.540  67.819  1.00 30.32 ?  43  PRO B CG  1 
ATOM   2360 C  CD  . PRO B 1 43  ? 68.533 -2.294  68.568  1.00 26.39 ?  43  PRO B CD  1 
ATOM   2361 N  N   . ALA B 1 44  ? 71.326 -5.614  70.471  1.00 25.78 ?  44  ALA B N   1 
ATOM   2362 C  CA  . ALA B 1 44  ? 72.684 -6.066  70.737  1.00 27.69 ?  44  ALA B CA  1 
ATOM   2363 C  C   . ALA B 1 44  ? 72.741 -7.558  70.449  1.00 26.61 ?  44  ALA B C   1 
ATOM   2364 O  O   . ALA B 1 44  ? 71.714 -8.243  70.540  1.00 23.88 ?  44  ALA B O   1 
ATOM   2365 C  CB  . ALA B 1 44  ? 73.098 -5.781  72.189  1.00 24.46 ?  44  ALA B CB  1 
ATOM   2366 N  N   . PRO B 1 45  ? 73.907 -8.088  70.074  1.00 26.97 ?  45  PRO B N   1 
ATOM   2367 C  CA  . PRO B 1 45  ? 73.972 -9.503  69.683  1.00 25.97 ?  45  PRO B CA  1 
ATOM   2368 C  C   . PRO B 1 45  ? 73.648 -10.440 70.844  1.00 22.70 ?  45  PRO B C   1 
ATOM   2369 O  O   . PRO B 1 45  ? 73.867 -10.123 72.016  1.00 25.67 ?  45  PRO B O   1 
ATOM   2370 C  CB  . PRO B 1 45  ? 75.425 -9.690  69.215  1.00 26.47 ?  45  PRO B CB  1 
ATOM   2371 C  CG  . PRO B 1 45  ? 75.974 -8.312  69.030  1.00 30.95 ?  45  PRO B CG  1 
ATOM   2372 C  CD  . PRO B 1 45  ? 75.214 -7.414  69.952  1.00 30.53 ?  45  PRO B CD  1 
ATOM   2373 N  N   . HIS B 1 46  ? 73.140 -11.618 70.493  1.00 20.93 ?  46  HIS B N   1 
ATOM   2374 C  CA  . HIS B 1 46  ? 72.849 -12.618 71.505  1.00 20.99 ?  46  HIS B CA  1 
ATOM   2375 C  C   . HIS B 1 46  ? 74.147 -13.213 72.044  1.00 22.62 ?  46  HIS B C   1 
ATOM   2376 O  O   . HIS B 1 46  ? 75.199 -13.189 71.389  1.00 23.41 ?  46  HIS B O   1 
ATOM   2377 C  CB  . HIS B 1 46  ? 71.956 -13.721 70.940  1.00 20.17 ?  46  HIS B CB  1 
ATOM   2378 C  CG  . HIS B 1 46  ? 72.554 -14.457 69.782  1.00 26.69 ?  46  HIS B CG  1 
ATOM   2379 N  ND1 . HIS B 1 46  ? 72.788 -13.861 68.560  1.00 27.27 ?  46  HIS B ND1 1 
ATOM   2380 C  CD2 . HIS B 1 46  ? 72.934 -15.750 69.650  1.00 28.03 ?  46  HIS B CD2 1 
ATOM   2381 C  CE1 . HIS B 1 46  ? 73.308 -14.751 67.732  1.00 28.59 ?  46  HIS B CE1 1 
ATOM   2382 N  NE2 . HIS B 1 46  ? 73.405 -15.905 68.368  1.00 31.21 ?  46  HIS B NE2 1 
ATOM   2383 N  N   . ALA B 1 47  ? 74.056 -13.759 73.253  1.00 21.50 ?  47  ALA B N   1 
ATOM   2384 C  CA  . ALA B 1 47  ? 75.200 -14.350 73.934  1.00 22.73 ?  47  ALA B CA  1 
ATOM   2385 C  C   . ALA B 1 47  ? 74.700 -15.444 74.865  1.00 27.39 ?  47  ALA B C   1 
ATOM   2386 O  O   . ALA B 1 47  ? 73.551 -15.430 75.306  1.00 24.59 ?  47  ALA B O   1 
ATOM   2387 C  CB  . ALA B 1 47  ? 75.992 -13.295 74.723  1.00 26.94 ?  47  ALA B CB  1 
ATOM   2388 N  N   . ASP B 1 48  ? 75.581 -16.385 75.182  1.00 29.59 ?  48  ASP B N   1 
ATOM   2389 C  CA  . ASP B 1 48  ? 75.238 -17.478 76.088  1.00 24.82 ?  48  ASP B CA  1 
ATOM   2390 C  C   . ASP B 1 48  ? 75.792 -17.193 77.487  1.00 31.00 ?  48  ASP B C   1 
ATOM   2391 O  O   . ASP B 1 48  ? 76.654 -17.905 78.011  1.00 32.99 ?  48  ASP B O   1 
ATOM   2392 C  CB  . ASP B 1 48  ? 75.754 -18.797 75.518  1.00 34.76 ?  48  ASP B CB  1 
ATOM   2393 C  CG  . ASP B 1 48  ? 75.411 -19.989 76.383  1.00 39.59 ?  48  ASP B CG  1 
ATOM   2394 O  OD1 . ASP B 1 48  ? 74.626 -19.822 77.341  1.00 40.82 -1 48  ASP B OD1 1 
ATOM   2395 O  OD2 . ASP B 1 48  ? 75.939 -21.092 76.112  1.00 48.24 -1 48  ASP B OD2 1 
ATOM   2396 N  N   . ASP B 1 49  ? 75.281 -16.127 78.102  1.00 24.66 ?  49  ASP B N   1 
ATOM   2397 C  CA  . ASP B 1 49  ? 75.857 -15.606 79.333  1.00 22.48 ?  49  ASP B CA  1 
ATOM   2398 C  C   . ASP B 1 49  ? 74.992 -15.936 80.547  1.00 25.96 ?  49  ASP B C   1 
ATOM   2399 O  O   . ASP B 1 49  ? 73.830 -16.341 80.434  1.00 20.95 ?  49  ASP B O   1 
ATOM   2400 C  CB  . ASP B 1 49  ? 76.124 -14.091 79.236  1.00 26.07 ?  49  ASP B CB  1 
ATOM   2401 C  CG  . ASP B 1 49  ? 74.922 -13.282 78.731  1.00 25.22 ?  49  ASP B CG  1 
ATOM   2402 O  OD1 . ASP B 1 49  ? 73.894 -13.873 78.339  1.00 26.26 ?  49  ASP B OD1 1 
ATOM   2403 O  OD2 . ASP B 1 49  ? 75.037 -12.036 78.716  1.00 26.41 -1 49  ASP B OD2 1 
ATOM   2404 N  N   . ASP B 1 50  ? 75.613 -15.822 81.720  1.00 22.77 ?  50  ASP B N   1 
ATOM   2405 C  CA  . ASP B 1 50  ? 74.925 -16.065 82.979  1.00 20.75 ?  50  ASP B CA  1 
ATOM   2406 C  C   . ASP B 1 50  ? 73.993 -14.904 83.293  1.00 18.67 ?  50  ASP B C   1 
ATOM   2407 O  O   . ASP B 1 50  ? 74.231 -13.773 82.877  1.00 19.59 ?  50  ASP B O   1 
ATOM   2408 C  CB  . ASP B 1 50  ? 75.941 -16.228 84.113  1.00 20.42 ?  50  ASP B CB  1 
ATOM   2409 C  CG  . ASP B 1 50  ? 75.299 -16.666 85.419  1.00 19.89 ?  50  ASP B CG  1 
ATOM   2410 O  OD1 . ASP B 1 50  ? 74.803 -17.808 85.463  1.00 21.90 ?  50  ASP B OD1 1 
ATOM   2411 O  OD2 . ASP B 1 50  ? 75.311 -15.881 86.393  1.00 22.26 -1 50  ASP B OD2 1 
ATOM   2412 N  N   . TRP B 1 51  ? 72.926 -15.191 84.052  1.00 18.83 ?  51  TRP B N   1 
ATOM   2413 C  CA  . TRP B 1 51  ? 71.995 -14.136 84.437  1.00 17.61 ?  51  TRP B CA  1 
ATOM   2414 C  C   . TRP B 1 51  ? 72.708 -12.991 85.156  1.00 19.90 ?  51  TRP B C   1 
ATOM   2415 O  O   . TRP B 1 51  ? 72.347 -11.828 84.974  1.00 20.42 ?  51  TRP B O   1 
ATOM   2416 C  CB  . TRP B 1 51  ? 70.871 -14.717 85.308  1.00 17.17 ?  51  TRP B CB  1 
ATOM   2417 C  CG  . TRP B 1 51  ? 71.367 -15.168 86.654  1.00 20.46 ?  51  TRP B CG  1 
ATOM   2418 C  CD1 . TRP B 1 51  ? 71.798 -16.411 86.991  1.00 20.31 ?  51  TRP B CD1 1 
ATOM   2419 C  CD2 . TRP B 1 51  ? 71.504 -14.359 87.823  1.00 20.14 ?  51  TRP B CD2 1 
ATOM   2420 N  NE1 . TRP B 1 51  ? 72.198 -16.434 88.314  1.00 18.29 ?  51  TRP B NE1 1 
ATOM   2421 C  CE2 . TRP B 1 51  ? 72.027 -15.185 88.847  1.00 19.16 ?  51  TRP B CE2 1 
ATOM   2422 C  CE3 . TRP B 1 51  ? 71.234 -13.018 88.109  1.00 19.96 ?  51  TRP B CE3 1 
ATOM   2423 C  CZ2 . TRP B 1 51  ? 72.284 -14.710 90.131  1.00 25.01 ?  51  TRP B CZ2 1 
ATOM   2424 C  CZ3 . TRP B 1 51  ? 71.484 -12.546 89.383  1.00 21.40 ?  51  TRP B CZ3 1 
ATOM   2425 C  CH2 . TRP B 1 51  ? 72.007 -13.391 90.381  1.00 22.58 ?  51  TRP B CH2 1 
ATOM   2426 N  N   . SER B 1 52  ? 73.738 -13.298 85.962  1.00 19.15 ?  52  SER B N   1 
ATOM   2427 C  CA  . SER B 1 52  ? 74.462 -12.264 86.695  1.00 20.66 ?  52  SER B CA  1 
ATOM   2428 C  C   . SER B 1 52  ? 75.196 -11.303 85.777  1.00 21.01 ?  52  SER B C   1 
ATOM   2429 O  O   . SER B 1 52  ? 75.640 -10.246 86.241  1.00 23.15 ?  52  SER B O   1 
ATOM   2430 C  CB  . SER B 1 52  ? 75.463 -12.902 87.670  1.00 21.60 ?  52  SER B CB  1 
ATOM   2431 O  OG  . SER B 1 52  ? 76.364 -13.751 86.981  1.00 22.24 ?  52  SER B OG  1 
ATOM   2432 N  N   . VAL B 1 53  ? 75.342 -11.657 84.506  1.00 19.62 ?  53  VAL B N   1 
ATOM   2433 C  CA  . VAL B 1 53  ? 75.984 -10.814 83.514  1.00 19.30 ?  53  VAL B CA  1 
ATOM   2434 C  C   . VAL B 1 53  ? 74.950 -10.136 82.626  1.00 17.90 ?  53  VAL B C   1 
ATOM   2435 O  O   . VAL B 1 53  ? 75.003 -8.924  82.416  1.00 22.51 ?  53  VAL B O   1 
ATOM   2436 C  CB  . VAL B 1 53  ? 76.965 -11.670 82.683  1.00 20.22 ?  53  VAL B CB  1 
ATOM   2437 C  CG1 . VAL B 1 53  ? 77.527 -10.895 81.509  1.00 26.53 ?  53  VAL B CG1 1 
ATOM   2438 C  CG2 . VAL B 1 53  ? 78.100 -12.213 83.584  1.00 24.05 ?  53  VAL B CG2 1 
ATOM   2439 N  N   . ALA B 1 54  ? 73.955 -10.910 82.181  1.00 19.47 ?  54  ALA B N   1 
ATOM   2440 C  CA  . ALA B 1 54  ? 72.935 -10.372 81.286  1.00 18.22 ?  54  ALA B CA  1 
ATOM   2441 C  C   . ALA B 1 54  ? 72.013 -9.387  81.996  1.00 18.13 ?  54  ALA B C   1 
ATOM   2442 O  O   . ALA B 1 54  ? 71.562 -8.410  81.383  1.00 16.74 ?  54  ALA B O   1 
ATOM   2443 C  CB  . ALA B 1 54  ? 72.125 -11.520 80.682  1.00 17.60 ?  54  ALA B CB  1 
ATOM   2444 N  N   . LEU B 1 55  ? 71.706 -9.624  83.275  1.00 19.05 ?  55  LEU B N   1 
ATOM   2445 C  CA  . LEU B 1 55  ? 70.787 -8.735  83.982  1.00 21.76 ?  55  LEU B CA  1 
ATOM   2446 C  C   . LEU B 1 55  ? 71.334 -7.319  84.107  1.00 21.18 ?  55  LEU B C   1 
ATOM   2447 O  O   . LEU B 1 55  ? 70.629 -6.372  83.712  1.00 19.87 ?  55  LEU B O   1 
ATOM   2448 C  CB  . LEU B 1 55  ? 70.428 -9.341  85.347  1.00 19.41 ?  55  LEU B CB  1 
ATOM   2449 C  CG  . LEU B 1 55  ? 69.554 -8.499  86.277  1.00 20.73 ?  55  LEU B CG  1 
ATOM   2450 C  CD1 . LEU B 1 55  ? 68.208 -8.228  85.637  1.00 23.67 ?  55  LEU B CD1 1 
ATOM   2451 C  CD2 . LEU B 1 55  ? 69.387 -9.228  87.598  1.00 24.86 ?  55  LEU B CD2 1 
ATOM   2452 N  N   . PRO B 1 56  ? 72.563 -7.090  84.585  1.00 20.73 ?  56  PRO B N   1 
ATOM   2453 C  CA  . PRO B 1 56  ? 73.069 -5.707  84.599  1.00 23.07 ?  56  PRO B CA  1 
ATOM   2454 C  C   . PRO B 1 56  ? 73.192 -5.082  83.215  1.00 20.45 ?  56  PRO B C   1 
ATOM   2455 O  O   . PRO B 1 56  ? 72.944 -3.879  83.080  1.00 20.45 ?  56  PRO B O   1 
ATOM   2456 C  CB  . PRO B 1 56  ? 74.438 -5.837  85.292  1.00 22.19 ?  56  PRO B CB  1 
ATOM   2457 C  CG  . PRO B 1 56  ? 74.804 -7.272  85.195  1.00 27.22 ?  56  PRO B CG  1 
ATOM   2458 C  CD  . PRO B 1 56  ? 73.493 -8.012  85.271  1.00 22.95 ?  56  PRO B CD  1 
ATOM   2459 N  N   . GLN B 1 57  ? 73.554 -5.857  82.183  1.00 20.47 ?  57  GLN B N   1 
ATOM   2460 C  CA  . GLN B 1 57  ? 73.708 -5.273  80.851  1.00 22.35 ?  57  GLN B CA  1 
ATOM   2461 C  C   . GLN B 1 57  ? 72.377 -4.761  80.313  1.00 22.19 ?  57  GLN B C   1 
ATOM   2462 O  O   . GLN B 1 57  ? 72.339 -3.795  79.538  1.00 23.09 ?  57  GLN B O   1 
ATOM   2463 C  CB  . GLN B 1 57  ? 74.305 -6.293  79.878  1.00 28.93 ?  57  GLN B CB  1 
ATOM   2464 C  CG  . GLN B 1 57  ? 75.746 -6.674  80.198  1.00 38.43 ?  57  GLN B CG  1 
ATOM   2465 C  CD  . GLN B 1 57  ? 76.296 -7.750  79.271  1.00 41.83 ?  57  GLN B CD  1 
ATOM   2466 O  OE1 . GLN B 1 57  ? 77.273 -8.432  79.592  1.00 42.70 ?  57  GLN B OE1 1 
ATOM   2467 N  NE2 . GLN B 1 57  ? 75.673 -7.898  78.104  1.00 41.24 ?  57  GLN B NE2 1 
ATOM   2468 N  N   . ALA B 1 58  ? 71.277 -5.371  80.738  1.00 18.36 ?  58  ALA B N   1 
ATOM   2469 C  CA  . ALA B 1 58  ? 69.945 -5.016  80.258  1.00 20.84 ?  58  ALA B CA  1 
ATOM   2470 C  C   . ALA B 1 58  ? 69.292 -3.886  81.042  1.00 22.04 ?  58  ALA B C   1 
ATOM   2471 O  O   . ALA B 1 58  ? 68.151 -3.528  80.737  1.00 19.27 ?  58  ALA B O   1 
ATOM   2472 C  CB  . ALA B 1 58  ? 69.044 -6.247  80.296  1.00 20.08 ?  58  ALA B CB  1 
ATOM   2473 N  N   . ARG B 1 59  ? 69.982 -3.310  82.035  1.00 21.63 ?  59  ARG B N   1 
ATOM   2474 C  CA  . ARG B 1 59  ? 69.336 -2.348  82.925  1.00 22.55 ?  59  ARG B CA  1 
ATOM   2475 C  C   . ARG B 1 59  ? 68.680 -1.208  82.160  1.00 21.76 ?  59  ARG B C   1 
ATOM   2476 O  O   . ARG B 1 59  ? 67.540 -0.834  82.446  1.00 22.58 ?  59  ARG B O   1 
ATOM   2477 C  CB  . ARG B 1 59  ? 70.345 -1.789  83.929  1.00 24.29 ?  59  ARG B CB  1 
ATOM   2478 C  CG  . ARG B 1 59  ? 69.691 -0.858  84.947  1.00 28.06 ?  59  ARG B CG  1 
ATOM   2479 C  CD  . ARG B 1 59  ? 70.437 -0.842  86.285  1.00 38.63 ?  59  ARG B CD  1 
ATOM   2480 N  NE  . ARG B 1 59  ? 69.796 -1.702  87.282  1.00 43.67 ?  59  ARG B NE  1 
ATOM   2481 C  CZ  . ARG B 1 59  ? 68.709 -1.373  87.981  1.00 36.16 ?  59  ARG B CZ  1 
ATOM   2482 N  NH1 . ARG B 1 59  ? 68.117 -0.194  87.805  1.00 37.36 ?  59  ARG B NH1 1 
ATOM   2483 N  NH2 . ARG B 1 59  ? 68.210 -2.230  88.858  1.00 36.99 ?  59  ARG B NH2 1 
ATOM   2484 N  N   . GLU B 1 60  ? 69.387 -0.650  81.175  1.00 24.11 ?  60  GLU B N   1 
ATOM   2485 C  CA  . GLU B 1 60  ? 68.872 0.516   80.463  1.00 23.27 ?  60  GLU B CA  1 
ATOM   2486 C  C   . GLU B 1 60  ? 67.592 0.177   79.710  1.00 21.99 ?  60  GLU B C   1 
ATOM   2487 O  O   . GLU B 1 60  ? 66.628 0.954   79.722  1.00 23.50 ?  60  GLU B O   1 
ATOM   2488 C  CB  . GLU B 1 60  ? 69.943 1.049   79.504  1.00 31.46 ?  60  GLU B CB  1 
ATOM   2489 C  CG  . GLU B 1 60  ? 71.244 1.540   80.188  1.00 36.36 ?  60  GLU B CG  1 
ATOM   2490 C  CD  . GLU B 1 60  ? 72.089 0.422   80.839  1.00 38.79 ?  60  GLU B CD  1 
ATOM   2491 O  OE1 . GLU B 1 60  ? 72.053 -0.746  80.372  1.00 31.46 ?  60  GLU B OE1 1 
ATOM   2492 O  OE2 . GLU B 1 60  ? 72.803 0.720   81.829  1.00 50.09 -1 60  GLU B OE2 1 
ATOM   2493 N  N   . THR B 1 61  ? 67.561 -0.983  79.060  1.00 21.60 ?  61  THR B N   1 
ATOM   2494 C  CA  . THR B 1 61  ? 66.345 -1.420  78.374  1.00 20.87 ?  61  THR B CA  1 
ATOM   2495 C  C   . THR B 1 61  ? 65.220 -1.699  79.364  1.00 18.58 ?  61  THR B C   1 
ATOM   2496 O  O   . THR B 1 61  ? 64.080 -1.276  79.156  1.00 20.76 ?  61  THR B O   1 
ATOM   2497 C  CB  . THR B 1 61  ? 66.650 -2.652  77.524  1.00 23.22 ?  61  THR B CB  1 
ATOM   2498 O  OG1 . THR B 1 61  ? 67.526 -2.276  76.460  1.00 25.10 ?  61  THR B OG1 1 
ATOM   2499 C  CG2 . THR B 1 61  ? 65.365 -3.240  76.919  1.00 23.19 ?  61  THR B CG2 1 
ATOM   2500 N  N   . LEU B 1 62  ? 65.522 -2.396  80.463  1.00 19.60 ?  62  LEU B N   1 
ATOM   2501 C  CA  . LEU B 1 62  ? 64.474 -2.717  81.432  1.00 18.39 ?  62  LEU B CA  1 
ATOM   2502 C  C   . LEU B 1 62  ? 63.880 -1.454  82.056  1.00 22.35 ?  62  LEU B C   1 
ATOM   2503 O  O   . LEU B 1 62  ? 62.662 -1.364  82.265  1.00 20.72 ?  62  LEU B O   1 
ATOM   2504 C  CB  . LEU B 1 62  ? 65.028 -3.650  82.507  1.00 14.07 ?  62  LEU B CB  1 
ATOM   2505 C  CG  . LEU B 1 62  ? 65.262 -5.088  82.062  1.00 17.63 ?  62  LEU B CG  1 
ATOM   2506 C  CD1 . LEU B 1 62  ? 66.110 -5.856  83.093  1.00 15.79 ?  62  LEU B CD1 1 
ATOM   2507 C  CD2 . LEU B 1 62  ? 63.908 -5.799  81.848  1.00 16.58 ?  62  LEU B CD2 1 
ATOM   2508 N  N   . VAL B 1 63  ? 64.717 -0.452  82.342  1.00 21.01 ?  63  VAL B N   1 
ATOM   2509 C  CA  . VAL B 1 63  ? 64.193 0.798   82.891  1.00 21.76 ?  63  VAL B CA  1 
ATOM   2510 C  C   . VAL B 1 63  ? 63.299 1.495   81.869  1.00 20.52 ?  63  VAL B C   1 
ATOM   2511 O  O   . VAL B 1 63  ? 62.223 2.004   82.204  1.00 20.63 ?  63  VAL B O   1 
ATOM   2512 C  CB  . VAL B 1 63  ? 65.360 1.702   83.345  1.00 24.86 ?  63  VAL B CB  1 
ATOM   2513 C  CG1 . VAL B 1 63  ? 64.862 3.107   83.666  1.00 26.87 ?  63  VAL B CG1 1 
ATOM   2514 C  CG2 . VAL B 1 63  ? 66.078 1.086   84.550  1.00 22.35 ?  63  VAL B CG2 1 
ATOM   2515 N  N   . ALA B 1 64  ? 63.708 1.491   80.604  1.00 22.19 ?  64  ALA B N   1 
ATOM   2516 C  CA  . ALA B 1 64  ? 62.933 2.162   79.566  1.00 20.69 ?  64  ALA B CA  1 
ATOM   2517 C  C   . ALA B 1 64  ? 61.602 1.455   79.315  1.00 20.37 ?  64  ALA B C   1 
ATOM   2518 O  O   . ALA B 1 64  ? 60.576 2.111   79.094  1.00 20.73 ?  64  ALA B O   1 
ATOM   2519 C  CB  . ALA B 1 64  ? 63.762 2.249   78.289  1.00 21.88 ?  64  ALA B CB  1 
ATOM   2520 N  N   . VAL B 1 65  ? 61.597 0.122   79.344  1.00 18.02 ?  65  VAL B N   1 
ATOM   2521 C  CA  . VAL B 1 65  ? 60.339 -0.614  79.230  1.00 19.52 ?  65  VAL B CA  1 
ATOM   2522 C  C   . VAL B 1 65  ? 59.444 -0.350  80.434  1.00 17.30 ?  65  VAL B C   1 
ATOM   2523 O  O   . VAL B 1 65  ? 58.229 -0.156  80.293  1.00 17.79 ?  65  VAL B O   1 
ATOM   2524 C  CB  . VAL B 1 65  ? 60.613 -2.117  79.053  1.00 19.05 ?  65  VAL B CB  1 
ATOM   2525 C  CG1 . VAL B 1 65  ? 59.301 -2.907  79.151  1.00 23.62 ?  65  VAL B CG1 1 
ATOM   2526 C  CG2 . VAL B 1 65  ? 61.322 -2.383  77.720  1.00 19.89 ?  65  VAL B CG2 1 
ATOM   2527 N  N   . ARG B 1 66  ? 60.023 -0.329  81.638  1.00 18.22 ?  66  ARG B N   1 
ATOM   2528 C  CA  . ARG B 1 66  ? 59.228 -0.024  82.822  1.00 19.28 ?  66  ARG B CA  1 
ATOM   2529 C  C   . ARG B 1 66  ? 58.541 1.332   82.701  1.00 19.78 ?  66  ARG B C   1 
ATOM   2530 O  O   . ARG B 1 66  ? 57.374 1.473   83.070  1.00 22.50 ?  66  ARG B O   1 
ATOM   2531 C  CB  . ARG B 1 66  ? 60.100 -0.067  84.081  1.00 22.24 ?  66  ARG B CB  1 
ATOM   2532 C  CG  . ARG B 1 66  ? 59.315 0.183   85.357  1.00 22.41 ?  66  ARG B CG  1 
ATOM   2533 C  CD  . ARG B 1 66  ? 60.250 0.573   86.489  1.00 30.84 ?  66  ARG B CD  1 
ATOM   2534 N  NE  . ARG B 1 66  ? 60.728 1.942   86.333  1.00 37.06 ?  66  ARG B NE  1 
ATOM   2535 C  CZ  . ARG B 1 66  ? 61.967 2.348   86.606  1.00 44.12 ?  66  ARG B CZ  1 
ATOM   2536 N  NH1 . ARG B 1 66  ? 62.881 1.482   87.041  1.00 39.15 ?  66  ARG B NH1 1 
ATOM   2537 N  NH2 . ARG B 1 66  ? 62.291 3.629   86.439  1.00 39.94 ?  66  ARG B NH2 1 
ATOM   2538 N  N   . GLU B 1 67  ? 59.247 2.339   82.181  1.00 21.58 ?  67  GLU B N   1 
ATOM   2539 C  CA  . GLU B 1 67  ? 58.650 3.665   82.041  1.00 19.80 ?  67  GLU B CA  1 
ATOM   2540 C  C   . GLU B 1 67  ? 57.528 3.664   81.010  1.00 21.74 ?  67  GLU B C   1 
ATOM   2541 O  O   . GLU B 1 67  ? 56.465 4.253   81.238  1.00 20.95 ?  67  GLU B O   1 
ATOM   2542 C  CB  . GLU B 1 67  ? 59.727 4.678   81.659  1.00 26.87 ?  67  GLU B CB  1 
ATOM   2543 C  CG  . GLU B 1 67  ? 60.939 4.649   82.570  1.00 33.87 ?  67  GLU B CG  1 
ATOM   2544 C  CD  . GLU B 1 67  ? 61.865 5.844   82.379  1.00 47.88 ?  67  GLU B CD  1 
ATOM   2545 O  OE1 . GLU B 1 67  ? 62.168 6.190   81.210  1.00 45.32 ?  67  GLU B OE1 1 
ATOM   2546 O  OE2 . GLU B 1 67  ? 62.316 6.412   83.401  1.00 51.64 -1 67  GLU B OE2 1 
ATOM   2547 N  N   . ALA B 1 68  ? 57.739 3.000   79.877  1.00 18.86 ?  68  ALA B N   1 
ATOM   2548 C  CA  . ALA B 1 68  ? 56.705 2.970   78.847  1.00 20.65 ?  68  ALA B CA  1 
ATOM   2549 C  C   . ALA B 1 68  ? 55.484 2.178   79.311  1.00 22.59 ?  68  ALA B C   1 
ATOM   2550 O  O   . ALA B 1 68  ? 54.337 2.596   79.084  1.00 20.29 ?  68  ALA B O   1 
ATOM   2551 C  CB  . ALA B 1 68  ? 57.289 2.391   77.556  1.00 21.95 ?  68  ALA B CB  1 
ATOM   2552 N  N   . ALA B 1 69  ? 55.707 1.038   79.973  1.00 18.44 ?  69  ALA B N   1 
ATOM   2553 C  CA  . ALA B 1 69  ? 54.587 0.233   80.444  1.00 17.95 ?  69  ALA B CA  1 
ATOM   2554 C  C   . ALA B 1 69  ? 53.812 0.943   81.544  1.00 21.50 ?  69  ALA B C   1 
ATOM   2555 O  O   . ALA B 1 69  ? 52.587 0.807   81.617  1.00 19.88 ?  69  ALA B O   1 
ATOM   2556 C  CB  . ALA B 1 69  ? 55.078 -1.135  80.935  1.00 22.72 ?  69  ALA B CB  1 
ATOM   2557 N  N   . THR B 1 70  ? 54.505 1.710   82.398  1.00 19.58 ?  70  THR B N   1 
ATOM   2558 C  CA  . THR B 1 70  ? 53.833 2.411   83.489  1.00 21.92 ?  70  THR B CA  1 
ATOM   2559 C  C   . THR B 1 70  ? 52.873 3.464   82.953  1.00 18.95 ?  70  THR B C   1 
ATOM   2560 O  O   . THR B 1 70  ? 51.716 3.532   83.385  1.00 22.16 ?  70  THR B O   1 
ATOM   2561 C  CB  . THR B 1 70  ? 54.863 3.046   84.431  1.00 23.19 ?  70  THR B CB  1 
ATOM   2562 O  OG1 . THR B 1 70  ? 55.700 2.020   84.980  1.00 22.45 ?  70  THR B OG1 1 
ATOM   2563 C  CG2 . THR B 1 70  ? 54.156 3.769   85.580  1.00 24.68 ?  70  THR B CG2 1 
ATOM   2564 N  N   . GLU B 1 71  ? 53.332 4.283   81.998  1.00 23.28 ?  71  GLU B N   1 
ATOM   2565 C  CA  . GLU B 1 71  ? 52.452 5.270   81.376  1.00 24.86 ?  71  GLU B CA  1 
ATOM   2566 C  C   . GLU B 1 71  ? 51.226 4.610   80.750  1.00 25.55 ?  71  GLU B C   1 
ATOM   2567 O  O   . GLU B 1 71  ? 50.104 5.127   80.860  1.00 23.20 ?  71  GLU B O   1 
ATOM   2568 C  CB  . GLU B 1 71  ? 53.213 6.080   80.321  1.00 27.40 ?  71  GLU B CB  1 
ATOM   2569 C  CG  . GLU B 1 71  ? 54.498 6.734   80.804  1.00 34.66 ?  71  GLU B CG  1 
ATOM   2570 C  CD  . GLU B 1 71  ? 55.258 7.421   79.676  1.00 46.90 ?  71  GLU B CD  1 
ATOM   2571 O  OE1 . GLU B 1 71  ? 54.779 7.370   78.516  1.00 47.83 ?  71  GLU B OE1 1 
ATOM   2572 O  OE2 . GLU B 1 71  ? 56.329 8.016   79.945  1.00 48.85 -1 71  GLU B OE2 1 
ATOM   2573 N  N   . SER B 1 72  ? 51.417 3.464   80.088  1.00 17.61 ?  72  SER B N   1 
ATOM   2574 C  CA  . SER B 1 72  ? 50.284 2.787   79.459  1.00 20.51 ?  72  SER B CA  1 
ATOM   2575 C  C   . SER B 1 72  ? 49.305 2.268   80.499  1.00 16.66 ?  72  SER B C   1 
ATOM   2576 O  O   . SER B 1 72  ? 48.086 2.450   80.368  1.00 21.00 ?  72  SER B O   1 
ATOM   2577 C  CB  . SER B 1 72  ? 50.767 1.639   78.570  1.00 20.38 ?  72  SER B CB  1 
ATOM   2578 O  OG  . SER B 1 72  ? 49.670 1.072   77.869  1.00 19.83 ?  72  SER B OG  1 
ATOM   2579 N  N   . ILE B 1 73  ? 49.818 1.590   81.531  1.00 16.57 ?  73  ILE B N   1 
ATOM   2580 C  CA  . ILE B 1 73  ? 48.930 0.977   82.507  1.00 19.81 ?  73  ILE B CA  1 
ATOM   2581 C  C   . ILE B 1 73  ? 48.164 2.050   83.277  1.00 28.80 ?  73  ILE B C   1 
ATOM   2582 O  O   . ILE B 1 73  ? 46.987 1.871   83.612  1.00 27.31 ?  73  ILE B O   1 
ATOM   2583 C  CB  . ILE B 1 73  ? 49.732 0.044   83.429  1.00 22.53 ?  73  ILE B CB  1 
ATOM   2584 C  CG1 . ILE B 1 73  ? 50.181 -1.182  82.631  1.00 18.04 ?  73  ILE B CG1 1 
ATOM   2585 C  CG2 . ILE B 1 73  ? 48.898 -0.388  84.640  1.00 21.11 ?  73  ILE B CG2 1 
ATOM   2586 C  CD1 . ILE B 1 73  ? 51.404 -1.870  83.198  1.00 25.76 ?  73  ILE B CD1 1 
ATOM   2587 N  N   . LYS B 1 74  ? 48.797 3.202   83.517  1.00 23.18 ?  74  LYS B N   1 
ATOM   2588 C  CA  . LYS B 1 74  ? 48.095 4.292   84.184  1.00 30.95 ?  74  LYS B CA  1 
ATOM   2589 C  C   . LYS B 1 74  ? 47.070 4.965   83.280  1.00 31.84 ?  74  LYS B C   1 
ATOM   2590 O  O   . LYS B 1 74  ? 46.220 5.703   83.790  1.00 36.68 ?  74  LYS B O   1 
ATOM   2591 C  CB  . LYS B 1 74  ? 49.099 5.320   84.708  1.00 31.19 ?  74  LYS B CB  1 
ATOM   2592 C  CG  . LYS B 1 74  ? 49.949 4.827   85.876  1.00 32.69 ?  74  LYS B CG  1 
ATOM   2593 C  CD  . LYS B 1 74  ? 50.861 5.947   86.372  1.00 35.37 ?  74  LYS B CD  1 
ATOM   2594 C  CE  . LYS B 1 74  ? 51.556 5.597   87.673  1.00 41.87 ?  74  LYS B CE  1 
ATOM   2595 N  NZ  . LYS B 1 74  ? 52.433 6.723   88.115  1.00 47.26 ?  74  LYS B NZ  1 
ATOM   2596 N  N   . GLY B 1 75  ? 47.109 4.705   81.968  1.00 27.52 ?  75  GLY B N   1 
ATOM   2597 C  CA  . GLY B 1 75  ? 46.151 5.246   81.025  1.00 30.20 ?  75  GLY B CA  1 
ATOM   2598 C  C   . GLY B 1 75  ? 44.918 4.376   80.865  1.00 30.47 ?  75  GLY B C   1 
ATOM   2599 O  O   . GLY B 1 75  ? 44.621 3.513   81.695  1.00 33.13 ?  75  GLY B O   1 
ATOM   2600 N  N   . ASP B 1 76  ? 44.201 4.598   79.759  1.00 32.58 ?  76  ASP B N   1 
ATOM   2601 C  CA  . ASP B 1 76  ? 42.907 3.963   79.509  1.00 37.14 ?  76  ASP B CA  1 
ATOM   2602 C  C   . ASP B 1 76  ? 42.941 2.847   78.468  1.00 35.58 ?  76  ASP B C   1 
ATOM   2603 O  O   . ASP B 1 76  ? 41.907 2.216   78.233  1.00 42.84 ?  76  ASP B O   1 
ATOM   2604 C  CB  . ASP B 1 76  ? 41.877 5.011   79.057  1.00 42.02 ?  76  ASP B CB  1 
ATOM   2605 C  CG  . ASP B 1 76  ? 41.547 6.024   80.139  1.00 51.04 ?  76  ASP B CG  1 
ATOM   2606 O  OD1 . ASP B 1 76  ? 41.017 5.615   81.194  1.00 54.09 -1 76  ASP B OD1 1 
ATOM   2607 O  OD2 . ASP B 1 76  ? 41.815 7.230   79.928  1.00 52.87 -1 76  ASP B OD2 1 
ATOM   2608 N  N   . ASN B 1 77  ? 44.076 2.591   77.827  1.00 34.88 ?  77  ASN B N   1 
ATOM   2609 C  CA  . ASN B 1 77  ? 44.110 1.658   76.709  1.00 31.11 ?  77  ASN B CA  1 
ATOM   2610 C  C   . ASN B 1 77  ? 44.491 0.248   77.175  1.00 26.69 ?  77  ASN B C   1 
ATOM   2611 O  O   . ASN B 1 77  ? 44.976 0.039   78.289  1.00 30.85 ?  77  ASN B O   1 
ATOM   2612 C  CB  . ASN B 1 77  ? 45.095 2.143   75.637  1.00 29.45 ?  77  ASN B CB  1 
ATOM   2613 C  CG  . ASN B 1 77  ? 44.498 3.206   74.714  1.00 39.54 ?  77  ASN B CG  1 
ATOM   2614 O  OD1 . ASN B 1 77  ? 43.297 3.471   74.741  1.00 45.91 ?  77  ASN B OD1 1 
ATOM   2615 N  ND2 . ASN B 1 77  ? 45.343 3.802   73.876  1.00 40.59 ?  77  ASN B ND2 1 
ATOM   2616 N  N   . LEU B 1 78  ? 44.242 -0.730  76.301  1.00 18.72 ?  78  LEU B N   1 
ATOM   2617 C  CA  . LEU B 1 78  ? 44.799 -2.067  76.481  1.00 17.43 ?  78  LEU B CA  1 
ATOM   2618 C  C   . LEU B 1 78  ? 46.300 -2.015  76.229  1.00 17.42 ?  78  LEU B C   1 
ATOM   2619 O  O   . LEU B 1 78  ? 46.734 -1.609  75.149  1.00 17.02 ?  78  LEU B O   1 
ATOM   2620 C  CB  . LEU B 1 78  ? 44.128 -3.060  75.531  1.00 15.75 ?  78  LEU B CB  1 
ATOM   2621 C  CG  . LEU B 1 78  ? 44.666 -4.495  75.572  1.00 17.67 ?  78  LEU B CG  1 
ATOM   2622 C  CD1 . LEU B 1 78  ? 44.257 -5.210  76.859  1.00 18.01 ?  78  LEU B CD1 1 
ATOM   2623 C  CD2 . LEU B 1 78  ? 44.200 -5.273  74.358  1.00 20.33 ?  78  LEU B CD2 1 
ATOM   2624 N  N   . THR B 1 79  ? 47.098 -2.412  77.229  1.00 17.10 ?  79  THR B N   1 
ATOM   2625 C  CA  . THR B 1 79  ? 48.551 -2.390  77.105  1.00 15.12 ?  79  THR B CA  1 
ATOM   2626 C  C   . THR B 1 79  ? 48.998 -3.676  76.413  1.00 16.37 ?  79  THR B C   1 
ATOM   2627 O  O   . THR B 1 79  ? 48.714 -4.769  76.903  1.00 15.46 ?  79  THR B O   1 
ATOM   2628 C  CB  . THR B 1 79  ? 49.198 -2.254  78.489  1.00 19.43 ?  79  THR B CB  1 
ATOM   2629 O  OG1 . THR B 1 79  ? 48.737 -1.044  79.103  1.00 18.88 ?  79  THR B OG1 1 
ATOM   2630 C  CG2 . THR B 1 79  ? 50.728 -2.225  78.399  1.00 17.12 ?  79  THR B CG2 1 
ATOM   2631 N  N   . VAL B 1 80  ? 49.662 -3.562  75.267  1.00 11.35 ?  80  VAL B N   1 
ATOM   2632 C  CA  . VAL B 1 80  ? 50.159 -4.737  74.554  1.00 14.59 ?  80  VAL B CA  1 
ATOM   2633 C  C   . VAL B 1 80  ? 51.664 -4.597  74.411  1.00 13.83 ?  80  VAL B C   1 
ATOM   2634 O  O   . VAL B 1 80  ? 52.139 -3.708  73.700  1.00 14.69 ?  80  VAL B O   1 
ATOM   2635 C  CB  . VAL B 1 80  ? 49.484 -4.909  73.186  1.00 14.13 ?  80  VAL B CB  1 
ATOM   2636 C  CG1 . VAL B 1 80  ? 50.069 -6.134  72.470  1.00 15.29 ?  80  VAL B CG1 1 
ATOM   2637 C  CG2 . VAL B 1 80  ? 47.976 -5.037  73.382  1.00 13.36 ?  80  VAL B CG2 1 
ATOM   2638 N  N   . LEU B 1 81  ? 52.414 -5.452  75.110  1.00 12.06 ?  81  LEU B N   1 
ATOM   2639 C  CA  . LEU B 1 81  ? 53.871 -5.492  75.004  1.00 13.78 ?  81  LEU B CA  1 
ATOM   2640 C  C   . LEU B 1 81  ? 54.285 -6.654  74.118  1.00 14.11 ?  81  LEU B C   1 
ATOM   2641 O  O   . LEU B 1 81  ? 53.915 -7.807  74.382  1.00 14.86 ?  81  LEU B O   1 
ATOM   2642 C  CB  . LEU B 1 81  ? 54.522 -5.626  76.383  1.00 14.32 ?  81  LEU B CB  1 
ATOM   2643 C  CG  . LEU B 1 81  ? 54.318 -4.371  77.229  1.00 22.95 ?  81  LEU B CG  1 
ATOM   2644 C  CD1 . LEU B 1 81  ? 53.690 -4.737  78.552  1.00 25.47 ?  81  LEU B CD1 1 
ATOM   2645 C  CD2 . LEU B 1 81  ? 55.659 -3.668  77.448  1.00 24.08 ?  81  LEU B CD2 1 
ATOM   2646 N  N   . VAL B 1 82  ? 55.040 -6.360  73.068  1.00 11.47 ?  82  VAL B N   1 
ATOM   2647 C  CA  . VAL B 1 82  ? 55.630 -7.405  72.241  1.00 10.23 ?  82  VAL B CA  1 
ATOM   2648 C  C   . VAL B 1 82  ? 57.093 -7.446  72.632  1.00 11.28 ?  82  VAL B C   1 
ATOM   2649 O  O   . VAL B 1 82  ? 57.847 -6.512  72.349  1.00 13.05 ?  82  VAL B O   1 
ATOM   2650 C  CB  . VAL B 1 82  ? 55.433 -7.143  70.745  1.00 12.65 ?  82  VAL B CB  1 
ATOM   2651 C  CG1 . VAL B 1 82  ? 56.051 -8.249  69.913  1.00 14.77 ?  82  VAL B CG1 1 
ATOM   2652 C  CG2 . VAL B 1 82  ? 53.945 -7.030  70.450  1.00 12.45 ?  82  VAL B CG2 1 
ATOM   2653 N  N   . ASN B 1 83  ? 57.483 -8.496  73.333  1.00 10.29 ?  83  ASN B N   1 
ATOM   2654 C  CA  . ASN B 1 83  ? 58.796 -8.551  73.966  1.00 12.99 ?  83  ASN B CA  1 
ATOM   2655 C  C   . ASN B 1 83  ? 59.685 -9.562  73.256  1.00 13.59 ?  83  ASN B C   1 
ATOM   2656 O  O   . ASN B 1 83  ? 59.222 -10.629 72.837  1.00 14.98 ?  83  ASN B O   1 
ATOM   2657 C  CB  . ASN B 1 83  ? 58.649 -8.917  75.434  1.00 13.12 ?  83  ASN B CB  1 
ATOM   2658 C  CG  . ASN B 1 83  ? 57.990 -7.790  76.239  1.00 17.30 ?  83  ASN B CG  1 
ATOM   2659 O  OD1 . ASN B 1 83  ? 58.070 -6.612  75.863  1.00 18.81 ?  83  ASN B OD1 1 
ATOM   2660 N  ND2 . ASN B 1 83  ? 57.328 -8.151  77.322  1.00 16.60 ?  83  ASN B ND2 1 
ATOM   2661 N  N   . ASN B 1 84  ? 60.971 -9.236  73.131  1.00 10.44 ?  84  ASN B N   1 
ATOM   2662 C  CA  . ASN B 1 84  ? 61.879 -10.228 72.559  1.00 13.33 ?  84  ASN B CA  1 
ATOM   2663 C  C   . ASN B 1 84  ? 62.044 -11.440 73.478  1.00 15.54 ?  84  ASN B C   1 
ATOM   2664 O  O   . ASN B 1 84  ? 62.022 -12.586 73.009  1.00 16.91 ?  84  ASN B O   1 
ATOM   2665 C  CB  . ASN B 1 84  ? 63.240 -9.587  72.239  1.00 12.99 ?  84  ASN B CB  1 
ATOM   2666 C  CG  . ASN B 1 84  ? 63.802 -8.761  73.391  1.00 16.87 ?  84  ASN B CG  1 
ATOM   2667 O  OD1 . ASN B 1 84  ? 63.093 -7.967  74.018  1.00 16.34 ?  84  ASN B OD1 1 
ATOM   2668 N  ND2 . ASN B 1 84  ? 65.101 -8.915  73.643  1.00 15.69 ?  84  ASN B ND2 1 
ATOM   2669 N  N   . THR B 1 85  ? 62.186 -11.225 74.788  1.00 14.97 ?  85  THR B N   1 
ATOM   2670 C  CA  . THR B 1 85  ? 62.346 -12.332 75.726  1.00 15.70 ?  85  THR B CA  1 
ATOM   2671 C  C   . THR B 1 85  ? 61.388 -12.187 76.900  1.00 14.81 ?  85  THR B C   1 
ATOM   2672 O  O   . THR B 1 85  ? 60.936 -11.091 77.210  1.00 15.41 ?  85  THR B O   1 
ATOM   2673 C  CB  . THR B 1 85  ? 63.776 -12.404 76.284  1.00 16.04 ?  85  THR B CB  1 
ATOM   2674 O  OG1 . THR B 1 85  ? 64.037 -11.238 77.081  1.00 17.46 ?  85  THR B OG1 1 
ATOM   2675 C  CG2 . THR B 1 85  ? 64.803 -12.475 75.156  1.00 19.60 ?  85  THR B CG2 1 
ATOM   2676 N  N   A CYS B 1 86  ? 61.115 -13.320 77.564  0.50 14.78 ?  86  CYS B N   1 
ATOM   2677 C  CA  A CYS B 1 86  ? 60.354 -13.298 78.809  0.50 15.08 ?  86  CYS B CA  1 
ATOM   2678 C  C   A CYS B 1 86  ? 61.003 -12.406 79.858  0.50 13.89 ?  86  CYS B C   1 
ATOM   2679 O  O   A CYS B 1 86  ? 60.307 -11.868 80.721  0.50 14.20 ?  86  CYS B O   1 
ATOM   2680 C  CB  A CYS B 1 86  ? 60.218 -14.709 79.382  0.50 15.95 ?  86  CYS B CB  1 
ATOM   2681 S  SG  A CYS B 1 86  ? 58.907 -15.723 78.674  0.50 17.10 ?  86  CYS B SG  1 
HETATM 2682 N  N   B CSO B 1 86  ? 61.089 -13.285 77.584  0.50 14.78 ?  86  CSO B N   1 
HETATM 2683 C  CA  B CSO B 1 86  ? 60.311 -13.157 78.803  0.50 15.09 ?  86  CSO B CA  1 
HETATM 2684 C  CB  B CSO B 1 86  ? 59.976 -14.502 79.401  0.50 15.88 ?  86  CSO B CB  1 
HETATM 2685 S  SG  B CSO B 1 86  ? 58.872 -15.385 78.318  0.50 17.06 ?  86  CSO B SG  1 
HETATM 2686 C  C   B CSO B 1 86  ? 61.006 -12.347 79.873  0.50 13.88 ?  86  CSO B C   1 
HETATM 2687 O  O   B CSO B 1 86  ? 60.346 -11.830 80.760  0.50 14.22 ?  86  CSO B O   1 
HETATM 2688 O  OD  B CSO B 1 86  ? 58.229 -16.694 79.317  0.50 17.60 ?  86  CSO B OD  1 
ATOM   2689 N  N   . SER B 1 87  ? 62.332 -12.261 79.822  1.00 16.36 ?  87  SER B N   1 
ATOM   2690 C  CA  . SER B 1 87  ? 63.032 -11.504 80.860  1.00 17.37 ?  87  SER B CA  1 
ATOM   2691 C  C   . SER B 1 87  ? 62.619 -10.042 80.885  1.00 15.06 ?  87  SER B C   1 
ATOM   2692 O  O   . SER B 1 87  ? 62.818 -9.376  81.901  1.00 14.33 ?  87  SER B O   1 
ATOM   2693 C  CB  . SER B 1 87  ? 64.538 -11.589 80.677  1.00 16.94 ?  87  SER B CB  1 
ATOM   2694 O  OG  . SER B 1 87  ? 64.967 -12.932 80.771  1.00 18.36 ?  87  SER B OG  1 
ATOM   2695 N  N   . VAL B 1 88  ? 62.040 -9.527  79.797  1.00 12.85 ?  88  VAL B N   1 
ATOM   2696 C  CA  . VAL B 1 88  ? 61.523 -8.165  79.822  1.00 14.86 ?  88  VAL B CA  1 
ATOM   2697 C  C   . VAL B 1 88  ? 60.491 -8.011  80.934  1.00 14.74 ?  88  VAL B C   1 
ATOM   2698 O  O   . VAL B 1 88  ? 60.373 -6.940  81.547  1.00 17.71 ?  88  VAL B O   1 
ATOM   2699 C  CB  . VAL B 1 88  ? 60.940 -7.792  78.434  1.00 14.24 ?  88  VAL B CB  1 
ATOM   2700 C  CG1 . VAL B 1 88  ? 60.341 -6.405  78.464  1.00 16.25 ?  88  VAL B CG1 1 
ATOM   2701 C  CG2 . VAL B 1 88  ? 62.030 -7.892  77.335  1.00 14.51 ?  88  VAL B CG2 1 
ATOM   2702 N  N   . SER B 1 89  ? 59.746 -9.079  81.233  1.00 14.58 ?  89  SER B N   1 
ATOM   2703 C  CA  . SER B 1 89  ? 58.692 -9.009  82.242  1.00 14.23 ?  89  SER B CA  1 
ATOM   2704 C  C   . SER B 1 89  ? 59.224 -8.834  83.662  1.00 14.78 ?  89  SER B C   1 
ATOM   2705 O  O   . SER B 1 89  ? 58.428 -8.566  84.574  1.00 15.49 ?  89  SER B O   1 
ATOM   2706 C  CB  . SER B 1 89  ? 57.820 -10.256 82.163  1.00 15.01 ?  89  SER B CB  1 
ATOM   2707 O  OG  . SER B 1 89  ? 57.294 -10.343 80.844  1.00 20.40 ?  89  SER B OG  1 
ATOM   2708 N  N   . LEU B 1 90  ? 60.533 -8.977  83.879  1.00 15.80 ?  90  LEU B N   1 
ATOM   2709 C  CA  . LEU B 1 90  ? 61.088 -8.567  85.170  1.00 16.71 ?  90  LEU B CA  1 
ATOM   2710 C  C   . LEU B 1 90  ? 60.832 -7.086  85.441  1.00 15.93 ?  90  LEU B C   1 
ATOM   2711 O  O   . LEU B 1 90  ? 60.733 -6.674  86.599  1.00 18.34 ?  90  LEU B O   1 
ATOM   2712 C  CB  . LEU B 1 90  ? 62.589 -8.854  85.229  1.00 16.79 ?  90  LEU B CB  1 
ATOM   2713 C  CG  . LEU B 1 90  ? 62.961 -10.323 85.329  1.00 16.54 ?  90  LEU B CG  1 
ATOM   2714 C  CD1 . LEU B 1 90  ? 64.477 -10.469 85.079  1.00 16.56 ?  90  LEU B CD1 1 
ATOM   2715 C  CD2 . LEU B 1 90  ? 62.553 -10.891 86.678  1.00 19.66 ?  90  LEU B CD2 1 
ATOM   2716 N  N   . ALA B 1 91  ? 60.725 -6.273  84.401  1.00 16.34 ?  91  ALA B N   1 
ATOM   2717 C  CA  . ALA B 1 91  ? 60.410 -4.859  84.588  1.00 18.03 ?  91  ALA B CA  1 
ATOM   2718 C  C   . ALA B 1 91  ? 58.910 -4.589  84.626  1.00 19.81 ?  91  ALA B C   1 
ATOM   2719 O  O   . ALA B 1 91  ? 58.460 -3.717  85.384  1.00 19.01 ?  91  ALA B O   1 
ATOM   2720 C  CB  . ALA B 1 91  ? 61.048 -4.016  83.475  1.00 22.03 ?  91  ALA B CB  1 
ATOM   2721 N  N   . THR B 1 92  ? 58.118 -5.336  83.851  1.00 15.40 ?  92  THR B N   1 
ATOM   2722 C  CA  . THR B 1 92  ? 56.702 -5.021  83.710  1.00 15.26 ?  92  THR B CA  1 
ATOM   2723 C  C   . THR B 1 92  ? 55.830 -5.622  84.810  1.00 16.84 ?  92  THR B C   1 
ATOM   2724 O  O   . THR B 1 92  ? 54.902 -4.953  85.281  1.00 15.89 ?  92  THR B O   1 
ATOM   2725 C  CB  . THR B 1 92  ? 56.193 -5.482  82.338  1.00 17.70 ?  92  THR B CB  1 
ATOM   2726 O  OG1 . THR B 1 92  ? 56.330 -6.906  82.231  1.00 20.31 ?  92  THR B OG1 1 
ATOM   2727 C  CG2 . THR B 1 92  ? 57.006 -4.842  81.251  1.00 17.98 ?  92  THR B CG2 1 
ATOM   2728 N  N   . LEU B 1 93  ? 56.086 -6.865  85.229  1.00 14.80 ?  93  LEU B N   1 
ATOM   2729 C  CA  . LEU B 1 93  ? 55.173 -7.499  86.180  1.00 12.11 ?  93  LEU B CA  1 
ATOM   2730 C  C   . LEU B 1 93  ? 55.122 -6.766  87.518  1.00 17.95 ?  93  LEU B C   1 
ATOM   2731 O  O   . LEU B 1 93  ? 54.029 -6.694  88.109  1.00 13.62 ?  93  LEU B O   1 
ATOM   2732 C  CB  . LEU B 1 93  ? 55.544 -8.977  86.361  1.00 14.91 ?  93  LEU B CB  1 
ATOM   2733 C  CG  . LEU B 1 93  ? 55.221 -9.859  85.150  1.00 16.39 ?  93  LEU B CG  1 
ATOM   2734 C  CD1 . LEU B 1 93  ? 55.772 -11.255 85.316  1.00 14.31 ?  93  LEU B CD1 1 
ATOM   2735 C  CD2 . LEU B 1 93  ? 53.706 -9.899  84.906  1.00 15.55 ?  93  LEU B CD2 1 
ATOM   2736 N  N   . PRO B 1 94  ? 56.214 -6.187  88.031  1.00 15.49 ?  94  PRO B N   1 
ATOM   2737 C  CA  . PRO B 1 94  ? 56.088 -5.395  89.262  1.00 17.31 ?  94  PRO B CA  1 
ATOM   2738 C  C   . PRO B 1 94  ? 55.215 -4.168  89.092  1.00 16.69 ?  94  PRO B C   1 
ATOM   2739 O  O   . PRO B 1 94  ? 54.546 -3.755  90.052  1.00 17.47 ?  94  PRO B O   1 
ATOM   2740 C  CB  . PRO B 1 94  ? 57.542 -5.011  89.579  1.00 16.78 ?  94  PRO B CB  1 
ATOM   2741 C  CG  . PRO B 1 94  ? 58.359 -6.125  88.986  1.00 19.42 ?  94  PRO B CG  1 
ATOM   2742 C  CD  . PRO B 1 94  ? 57.629 -6.472  87.704  1.00 16.19 ?  94  PRO B CD  1 
ATOM   2743 N  N   . VAL B 1 95  ? 55.207 -3.564  87.897  1.00 16.50 ?  95  VAL B N   1 
ATOM   2744 C  CA  . VAL B 1 95  ? 54.308 -2.444  87.635  1.00 16.91 ?  95  VAL B CA  1 
ATOM   2745 C  C   . VAL B 1 95  ? 52.861 -2.911  87.669  1.00 16.04 ?  95  VAL B C   1 
ATOM   2746 O  O   . VAL B 1 95  ? 51.992 -2.254  88.253  1.00 15.36 ?  95  VAL B O   1 
ATOM   2747 C  CB  . VAL B 1 95  ? 54.645 -1.785  86.285  1.00 16.51 ?  95  VAL B CB  1 
ATOM   2748 C  CG1 . VAL B 1 95  ? 53.668 -0.635  85.977  1.00 22.06 ?  95  VAL B CG1 1 
ATOM   2749 C  CG2 . VAL B 1 95  ? 56.098 -1.313  86.255  1.00 20.84 ?  95  VAL B CG2 1 
ATOM   2750 N  N   . VAL B 1 96  ? 52.566 -4.023  86.989  1.00 15.81 ?  96  VAL B N   1 
ATOM   2751 C  CA  . VAL B 1 96  ? 51.205 -4.571  87.010  1.00 14.35 ?  96  VAL B CA  1 
ATOM   2752 C  C   . VAL B 1 96  ? 50.750 -4.802  88.443  1.00 16.61 ?  96  VAL B C   1 
ATOM   2753 O  O   . VAL B 1 96  ? 49.635 -4.433  88.841  1.00 18.46 ?  96  VAL B O   1 
ATOM   2754 C  CB  . VAL B 1 96  ? 51.143 -5.886  86.210  1.00 14.25 ?  96  VAL B CB  1 
ATOM   2755 C  CG1 . VAL B 1 96  ? 49.744 -6.479  86.302  1.00 19.05 ?  96  VAL B CG1 1 
ATOM   2756 C  CG2 . VAL B 1 96  ? 51.546 -5.658  84.763  1.00 17.34 ?  96  VAL B CG2 1 
ATOM   2757 N  N   . ALA B 1 97  ? 51.610 -5.436  89.236  1.00 15.66 ?  97  ALA B N   1 
ATOM   2758 C  CA  . ALA B 1 97  ? 51.204 -5.824  90.581  1.00 16.79 ?  97  ALA B CA  1 
ATOM   2759 C  C   . ALA B 1 97  ? 51.011 -4.598  91.462  1.00 21.28 ?  97  ALA B C   1 
ATOM   2760 O  O   . ALA B 1 97  ? 50.120 -4.574  92.319  1.00 21.01 ?  97  ALA B O   1 
ATOM   2761 C  CB  . ALA B 1 97  ? 52.238 -6.775  91.184  1.00 15.73 ?  97  ALA B CB  1 
ATOM   2762 N  N   . ARG B 1 98  ? 51.848 -3.576  91.271  1.00 17.41 ?  98  ARG B N   1 
ATOM   2763 C  CA  . ARG B 1 98  ? 51.708 -2.351  92.050  1.00 17.71 ?  98  ARG B CA  1 
ATOM   2764 C  C   . ARG B 1 98  ? 50.424 -1.621  91.695  1.00 17.37 ?  98  ARG B C   1 
ATOM   2765 O  O   . ARG B 1 98  ? 49.662 -1.215  92.579  1.00 17.02 ?  98  ARG B O   1 
ATOM   2766 C  CB  . ARG B 1 98  ? 52.914 -1.444  91.826  1.00 18.90 ?  98  ARG B CB  1 
ATOM   2767 C  CG  . ARG B 1 98  ? 52.871 -0.172  92.675  1.00 21.42 ?  98  ARG B CG  1 
ATOM   2768 C  CD  . ARG B 1 98  ? 53.958 0.806   92.266  1.00 26.19 ?  98  ARG B CD  1 
ATOM   2769 N  NE  . ARG B 1 98  ? 53.604 1.503   91.033  1.00 31.89 ?  98  ARG B NE  1 
ATOM   2770 C  CZ  . ARG B 1 98  ? 54.405 1.603   89.974  1.00 42.03 ?  98  ARG B CZ  1 
ATOM   2771 N  NH1 . ARG B 1 98  ? 55.615 1.050   89.997  1.00 39.65 ?  98  ARG B NH1 1 
ATOM   2772 N  NH2 . ARG B 1 98  ? 53.998 2.261   88.895  1.00 34.23 ?  98  ARG B NH2 1 
ATOM   2773 N  N   . GLU B 1 99  ? 50.156 -1.459  90.395  1.00 15.73 ?  99  GLU B N   1 
ATOM   2774 C  CA  . GLU B 1 99  ? 49.007 -0.670  89.972  1.00 16.85 ?  99  GLU B CA  1 
ATOM   2775 C  C   . GLU B 1 99  ? 47.704 -1.437  90.126  1.00 16.58 ?  99  GLU B C   1 
ATOM   2776 O  O   . GLU B 1 99  ? 46.655 -0.826  90.367  1.00 16.77 ?  99  GLU B O   1 
ATOM   2777 C  CB  . GLU B 1 99  ? 49.182 -0.227  88.516  1.00 18.23 ?  99  GLU B CB  1 
ATOM   2778 C  CG  . GLU B 1 99  ? 50.364 0.714   88.292  1.00 23.31 ?  99  GLU B CG  1 
ATOM   2779 C  CD  . GLU B 1 99  ? 50.130 2.087   88.909  1.00 28.67 ?  99  GLU B CD  1 
ATOM   2780 O  OE1 . GLU B 1 99  ? 51.116 2.726   89.328  1.00 37.12 ?  99  GLU B OE1 1 
ATOM   2781 O  OE2 . GLU B 1 99  ? 48.957 2.522   88.964  1.00 30.88 -1 99  GLU B OE2 1 
ATOM   2782 N  N   . HIS B 1 100 ? 47.760 -2.763  90.032  1.00 16.17 ?  100 HIS B N   1 
ATOM   2783 C  CA  . HIS B 1 100 ? 46.586 -3.628  90.128  1.00 20.07 ?  100 HIS B CA  1 
ATOM   2784 C  C   . HIS B 1 100 ? 46.846 -4.741  91.137  1.00 18.51 ?  100 HIS B C   1 
ATOM   2785 O  O   . HIS B 1 100 ? 47.051 -5.905  90.767  1.00 17.42 ?  100 HIS B O   1 
ATOM   2786 C  CB  . HIS B 1 100 ? 46.233 -4.191  88.749  1.00 14.80 ?  100 HIS B CB  1 
ATOM   2787 C  CG  . HIS B 1 100 ? 45.845 -3.137  87.758  1.00 18.01 ?  100 HIS B CG  1 
ATOM   2788 N  ND1 . HIS B 1 100 ? 44.577 -2.602  87.703  1.00 22.84 ?  100 HIS B ND1 1 
ATOM   2789 C  CD2 . HIS B 1 100 ? 46.559 -2.514  86.791  1.00 17.86 ?  100 HIS B CD2 1 
ATOM   2790 C  CE1 . HIS B 1 100 ? 44.525 -1.696  86.741  1.00 20.58 ?  100 HIS B CE1 1 
ATOM   2791 N  NE2 . HIS B 1 100 ? 45.711 -1.633  86.164  1.00 21.03 ?  100 HIS B NE2 1 
ATOM   2792 N  N   . PRO B 1 101 ? 46.820 -4.426  92.439  1.00 16.70 ?  101 PRO B N   1 
ATOM   2793 C  CA  . PRO B 1 101 ? 47.159 -5.448  93.439  1.00 18.26 ?  101 PRO B CA  1 
ATOM   2794 C  C   . PRO B 1 101 ? 46.184 -6.614  93.480  1.00 16.16 ?  101 PRO B C   1 
ATOM   2795 O  O   . PRO B 1 101 ? 46.518 -7.632  94.091  1.00 19.27 ?  101 PRO B O   1 
ATOM   2796 C  CB  . PRO B 1 101 ? 47.158 -4.668  94.767  1.00 21.16 ?  101 PRO B CB  1 
ATOM   2797 C  CG  . PRO B 1 101 ? 46.360 -3.450  94.487  1.00 21.87 ?  101 PRO B CG  1 
ATOM   2798 C  CD  . PRO B 1 101 ? 46.588 -3.105  93.055  1.00 20.23 ?  101 PRO B CD  1 
ATOM   2799 N  N   . ASP B 1 102 ? 45.027 -6.514  92.831  1.00 17.64 ?  102 ASP B N   1 
ATOM   2800 C  CA  . ASP B 1 102 ? 44.101 -7.634  92.750  1.00 22.86 ?  102 ASP B CA  1 
ATOM   2801 C  C   . ASP B 1 102 ? 44.203 -8.392  91.432  1.00 21.08 ?  102 ASP B C   1 
ATOM   2802 O  O   . ASP B 1 102 ? 43.500 -9.396  91.251  1.00 18.16 ?  102 ASP B O   1 
ATOM   2803 C  CB  . ASP B 1 102 ? 42.661 -7.153  92.981  1.00 25.79 ?  102 ASP B CB  1 
ATOM   2804 C  CG  . ASP B 1 102 ? 42.222 -6.038  92.023  1.00 31.02 ?  102 ASP B CG  1 
ATOM   2805 O  OD1 . ASP B 1 102 ? 43.055 -5.422  91.308  1.00 31.34 ?  102 ASP B OD1 1 
ATOM   2806 O  OD2 . ASP B 1 102 ? 41.001 -5.759  92.013  1.00 42.26 -1 102 ASP B OD2 1 
ATOM   2807 N  N   . ALA B 1 103 ? 45.065 -7.954  90.519  1.00 17.12 ?  103 ALA B N   1 
ATOM   2808 C  CA  . ALA B 1 103 ? 45.191 -8.647  89.237  1.00 15.27 ?  103 ALA B CA  1 
ATOM   2809 C  C   . ALA B 1 103 ? 45.721 -10.060 89.411  1.00 18.14 ?  103 ALA B C   1 
ATOM   2810 O  O   . ALA B 1 103 ? 46.593 -10.326 90.243  1.00 16.15 ?  103 ALA B O   1 
ATOM   2811 C  CB  . ALA B 1 103 ? 46.125 -7.881  88.299  1.00 18.77 ?  103 ALA B CB  1 
ATOM   2812 N  N   . VAL B 1 104 ? 45.216 -10.962 88.574  1.00 14.30 ?  104 VAL B N   1 
ATOM   2813 C  CA  . VAL B 1 104 ? 45.745 -12.305 88.427  1.00 14.12 ?  104 VAL B CA  1 
ATOM   2814 C  C   . VAL B 1 104 ? 46.576 -12.320 87.156  1.00 14.30 ?  104 VAL B C   1 
ATOM   2815 O  O   . VAL B 1 104 ? 46.116 -11.838 86.112  1.00 14.60 ?  104 VAL B O   1 
ATOM   2816 C  CB  . VAL B 1 104 ? 44.606 -13.337 88.360  1.00 15.89 ?  104 VAL B CB  1 
ATOM   2817 C  CG1 . VAL B 1 104 ? 45.121 -14.705 87.902  1.00 14.74 ?  104 VAL B CG1 1 
ATOM   2818 C  CG2 . VAL B 1 104 ? 43.922 -13.450 89.720  1.00 18.95 ?  104 VAL B CG2 1 
ATOM   2819 N  N   . VAL B 1 105 ? 47.795 -12.848 87.244  1.00 15.83 ?  105 VAL B N   1 
ATOM   2820 C  CA  . VAL B 1 105 ? 48.692 -12.964 86.101  1.00 10.98 ?  105 VAL B CA  1 
ATOM   2821 C  C   . VAL B 1 105 ? 48.567 -14.374 85.566  1.00 13.22 ?  105 VAL B C   1 
ATOM   2822 O  O   . VAL B 1 105 ? 48.830 -15.337 86.287  1.00 15.99 ?  105 VAL B O   1 
ATOM   2823 C  CB  . VAL B 1 105 ? 50.149 -12.661 86.468  1.00 13.17 ?  105 VAL B CB  1 
ATOM   2824 C  CG1 . VAL B 1 105 ? 51.083 -13.074 85.299  1.00 13.81 ?  105 VAL B CG1 1 
ATOM   2825 C  CG2 . VAL B 1 105 ? 50.310 -11.185 86.814  1.00 14.90 ?  105 VAL B CG2 1 
ATOM   2826 N  N   . LEU B 1 106 ? 48.127 -14.498 84.310  1.00 11.83 ?  106 LEU B N   1 
ATOM   2827 C  CA  . LEU B 1 106 ? 48.158 -15.781 83.623  1.00 11.96 ?  106 LEU B CA  1 
ATOM   2828 C  C   . LEU B 1 106 ? 49.505 -15.884 82.926  1.00 12.21 ?  106 LEU B C   1 
ATOM   2829 O  O   . LEU B 1 106 ? 49.761 -15.182 81.941  1.00 14.31 ?  106 LEU B O   1 
ATOM   2830 C  CB  . LEU B 1 106 ? 47.002 -15.890 82.633  1.00 9.48  ?  106 LEU B CB  1 
ATOM   2831 C  CG  . LEU B 1 106 ? 45.598 -15.868 83.226  1.00 13.09 ?  106 LEU B CG  1 
ATOM   2832 C  CD1 . LEU B 1 106 ? 44.579 -15.974 82.090  1.00 16.59 ?  106 LEU B CD1 1 
ATOM   2833 C  CD2 . LEU B 1 106 ? 45.395 -17.019 84.231  1.00 14.65 ?  106 LEU B CD2 1 
ATOM   2834 N  N   . TYR B 1 107 ? 50.391 -16.716 83.469  1.00 10.77 ?  107 TYR B N   1 
ATOM   2835 C  CA  . TYR B 1 107 ? 51.744 -16.861 82.943  1.00 10.90 ?  107 TYR B CA  1 
ATOM   2836 C  C   . TYR B 1 107 ? 51.695 -18.097 82.059  1.00 12.62 ?  107 TYR B C   1 
ATOM   2837 O  O   . TYR B 1 107 ? 51.816 -19.224 82.528  1.00 15.59 ?  107 TYR B O   1 
ATOM   2838 C  CB  . TYR B 1 107 ? 52.770 -16.982 84.070  1.00 12.27 ?  107 TYR B CB  1 
ATOM   2839 C  CG  . TYR B 1 107 ? 54.177 -16.670 83.631  1.00 12.30 ?  107 TYR B CG  1 
ATOM   2840 C  CD1 . TYR B 1 107 ? 54.979 -17.657 83.059  1.00 12.56 ?  107 TYR B CD1 1 
ATOM   2841 C  CD2 . TYR B 1 107 ? 54.710 -15.397 83.787  1.00 16.18 ?  107 TYR B CD2 1 
ATOM   2842 C  CE1 . TYR B 1 107 ? 56.274 -17.390 82.647  1.00 12.50 ?  107 TYR B CE1 1 
ATOM   2843 C  CE2 . TYR B 1 107 ? 56.020 -15.114 83.383  1.00 14.43 ?  107 TYR B CE2 1 
ATOM   2844 C  CZ  . TYR B 1 107 ? 56.787 -16.115 82.812  1.00 15.57 ?  107 TYR B CZ  1 
ATOM   2845 O  OH  . TYR B 1 107 ? 58.071 -15.842 82.401  1.00 15.11 ?  107 TYR B OH  1 
ATOM   2846 N  N   . ILE B 1 108 ? 51.453 -17.880 80.766  1.00 14.12 ?  108 ILE B N   1 
ATOM   2847 C  CA  . ILE B 1 108 ? 51.209 -18.980 79.837  1.00 11.59 ?  108 ILE B CA  1 
ATOM   2848 C  C   . ILE B 1 108 ? 52.541 -19.347 79.196  1.00 13.77 ?  108 ILE B C   1 
ATOM   2849 O  O   . ILE B 1 108 ? 53.092 -18.587 78.395  1.00 14.02 ?  108 ILE B O   1 
ATOM   2850 C  CB  . ILE B 1 108 ? 50.157 -18.605 78.791  1.00 12.29 ?  108 ILE B CB  1 
ATOM   2851 C  CG1 . ILE B 1 108 ? 48.895 -18.046 79.492  1.00 12.76 ?  108 ILE B CG1 1 
ATOM   2852 C  CG2 . ILE B 1 108 ? 49.840 -19.845 77.951  1.00 11.78 ?  108 ILE B CG2 1 
ATOM   2853 C  CD1 . ILE B 1 108 ? 47.734 -17.688 78.547  1.00 14.87 ?  108 ILE B CD1 1 
ATOM   2854 N  N   . ASP B 1 109 ? 53.076 -20.509 79.566  1.00 10.88 ?  109 ASP B N   1 
ATOM   2855 C  CA  . ASP B 1 109 ? 54.491 -20.786 79.371  1.00 12.79 ?  109 ASP B CA  1 
ATOM   2856 C  C   . ASP B 1 109 ? 54.709 -22.295 79.422  1.00 14.33 ?  109 ASP B C   1 
ATOM   2857 O  O   . ASP B 1 109 ? 54.081 -22.990 80.226  1.00 15.39 ?  109 ASP B O   1 
ATOM   2858 C  CB  . ASP B 1 109 ? 55.297 -20.071 80.478  1.00 14.90 ?  109 ASP B CB  1 
ATOM   2859 C  CG  . ASP B 1 109 ? 56.788 -20.025 80.213  1.00 16.88 ?  109 ASP B CG  1 
ATOM   2860 O  OD1 . ASP B 1 109 ? 57.491 -21.020 80.535  1.00 20.38 ?  109 ASP B OD1 1 
ATOM   2861 O  OD2 . ASP B 1 109 ? 57.265 -18.965 79.731  1.00 14.22 -1 109 ASP B OD2 1 
ATOM   2862 N  N   . GLY B 1 110 ? 55.606 -22.795 78.577  1.00 12.86 ?  110 GLY B N   1 
ATOM   2863 C  CA  . GLY B 1 110 ? 55.895 -24.219 78.599  1.00 14.64 ?  110 GLY B CA  1 
ATOM   2864 C  C   . GLY B 1 110 ? 56.729 -24.686 79.779  1.00 15.63 ?  110 GLY B C   1 
ATOM   2865 O  O   . GLY B 1 110 ? 56.776 -25.890 80.050  1.00 17.33 ?  110 GLY B O   1 
ATOM   2866 N  N   . HIS B 1 111 ? 57.356 -23.769 80.509  1.00 15.45 ?  111 HIS B N   1 
ATOM   2867 C  CA  . HIS B 1 111 ? 58.360 -24.145 81.506  1.00 14.89 ?  111 HIS B CA  1 
ATOM   2868 C  C   . HIS B 1 111 ? 58.019 -23.772 82.941  1.00 22.87 ?  111 HIS B C   1 
ATOM   2869 O  O   . HIS B 1 111 ? 58.281 -24.565 83.851  1.00 24.51 ?  111 HIS B O   1 
ATOM   2870 C  CB  . HIS B 1 111 ? 59.699 -23.510 81.149  1.00 16.42 ?  111 HIS B CB  1 
ATOM   2871 C  CG  . HIS B 1 111 ? 60.294 -24.060 79.900  1.00 20.21 ?  111 HIS B CG  1 
ATOM   2872 N  ND1 . HIS B 1 111 ? 61.128 -25.156 79.894  1.00 25.19 ?  111 HIS B ND1 1 
ATOM   2873 C  CD2 . HIS B 1 111 ? 60.147 -23.687 78.606  1.00 20.93 ?  111 HIS B CD2 1 
ATOM   2874 C  CE1 . HIS B 1 111 ? 61.487 -25.424 78.651  1.00 28.39 ?  111 HIS B CE1 1 
ATOM   2875 N  NE2 . HIS B 1 111 ? 60.910 -24.545 77.850  1.00 22.51 ?  111 HIS B NE2 1 
ATOM   2876 N  N   . GLY B 1 112 ? 57.486 -22.578 83.187  1.00 19.89 ?  112 GLY B N   1 
ATOM   2877 C  CA  . GLY B 1 112 ? 57.238 -22.096 84.531  1.00 17.81 ?  112 GLY B CA  1 
ATOM   2878 C  C   . GLY B 1 112 ? 58.111 -20.922 84.939  1.00 15.50 ?  112 GLY B C   1 
ATOM   2879 O  O   . GLY B 1 112 ? 57.656 -20.069 85.707  1.00 14.62 ?  112 GLY B O   1 
ATOM   2880 N  N   . ASP B 1 113 ? 59.350 -20.863 84.445  1.00 15.66 ?  113 ASP B N   1 
ATOM   2881 C  CA  . ASP B 1 113 ? 60.249 -19.717 84.650  1.00 12.56 ?  113 ASP B CA  1 
ATOM   2882 C  C   . ASP B 1 113 ? 60.293 -19.290 86.114  1.00 14.98 ?  113 ASP B C   1 
ATOM   2883 O  O   . ASP B 1 113 ? 60.235 -18.102 86.448  1.00 13.87 ?  113 ASP B O   1 
ATOM   2884 C  CB  . ASP B 1 113 ? 59.849 -18.546 83.747  1.00 12.16 ?  113 ASP B CB  1 
ATOM   2885 C  CG  . ASP B 1 113 ? 59.944 -18.906 82.278  1.00 14.82 ?  113 ASP B CG  1 
ATOM   2886 O  OD1 . ASP B 1 113 ? 60.556 -19.956 81.971  1.00 15.83 ?  113 ASP B OD1 1 
ATOM   2887 O  OD2 . ASP B 1 113 ? 59.416 -18.133 81.449  1.00 15.44 -1 113 ASP B OD2 1 
ATOM   2888 N  N   . PHE B 1 114 ? 60.439 -20.284 87.002  1.00 15.25 ?  114 PHE B N   1 
ATOM   2889 C  CA  . PHE B 1 114 ? 60.365 -20.045 88.443  1.00 14.56 ?  114 PHE B CA  1 
ATOM   2890 C  C   . PHE B 1 114 ? 61.661 -20.420 89.147  1.00 19.10 ?  114 PHE B C   1 
ATOM   2891 O  O   . PHE B 1 114 ? 61.646 -20.700 90.350  1.00 17.71 ?  114 PHE B O   1 
ATOM   2892 C  CB  . PHE B 1 114 ? 59.187 -20.809 89.073  1.00 17.13 ?  114 PHE B CB  1 
ATOM   2893 C  CG  . PHE B 1 114 ? 58.545 -20.088 90.230  1.00 18.86 ?  114 PHE B CG  1 
ATOM   2894 C  CD1 . PHE B 1 114 ? 57.760 -18.963 90.016  1.00 18.67 ?  114 PHE B CD1 1 
ATOM   2895 C  CD2 . PHE B 1 114 ? 58.735 -20.533 91.536  1.00 19.46 ?  114 PHE B CD2 1 
ATOM   2896 C  CE1 . PHE B 1 114 ? 57.158 -18.283 91.071  1.00 18.45 ?  114 PHE B CE1 1 
ATOM   2897 C  CE2 . PHE B 1 114 ? 58.142 -19.864 92.605  1.00 20.75 ?  114 PHE B CE2 1 
ATOM   2898 C  CZ  . PHE B 1 114 ? 57.364 -18.735 92.382  1.00 20.31 ?  114 PHE B CZ  1 
ATOM   2899 N  N   . ASN B 1 115 ? 62.777 -20.413 88.427  1.00 17.80 ?  115 ASN B N   1 
ATOM   2900 C  CA  . ASN B 1 115 ? 64.072 -20.712 89.030  1.00 19.64 ?  115 ASN B CA  1 
ATOM   2901 C  C   . ASN B 1 115 ? 64.616 -19.537 89.835  1.00 19.18 ?  115 ASN B C   1 
ATOM   2902 O  O   . ASN B 1 115 ? 64.296 -18.366 89.596  1.00 17.74 ?  115 ASN B O   1 
ATOM   2903 C  CB  . ASN B 1 115 ? 65.085 -21.104 87.949  1.00 18.71 ?  115 ASN B CB  1 
ATOM   2904 C  CG  . ASN B 1 115 ? 64.776 -22.450 87.332  1.00 23.31 ?  115 ASN B CG  1 
ATOM   2905 O  OD1 . ASN B 1 115 ? 64.893 -23.480 87.999  1.00 23.21 ?  115 ASN B OD1 1 
ATOM   2906 N  ND2 . ASN B 1 115 ? 64.350 -22.453 86.067  1.00 21.15 ?  115 ASN B ND2 1 
ATOM   2907 N  N   . THR B 1 116 ? 65.467 -19.863 90.796  1.00 16.88 ?  116 THR B N   1 
ATOM   2908 C  CA  . THR B 1 116 ? 66.253 -18.899 91.541  1.00 20.09 ?  116 THR B CA  1 
ATOM   2909 C  C   . THR B 1 116 ? 67.718 -19.049 91.159  1.00 19.36 ?  116 THR B C   1 
ATOM   2910 O  O   . THR B 1 116 ? 68.093 -19.980 90.436  1.00 19.78 ?  116 THR B O   1 
ATOM   2911 C  CB  . THR B 1 116 ? 66.087 -19.130 93.046  1.00 19.51 ?  116 THR B CB  1 
ATOM   2912 O  OG1 . THR B 1 116 ? 66.462 -20.478 93.336  1.00 20.92 ?  116 THR B OG1 1 
ATOM   2913 C  CG2 . THR B 1 116 ? 64.631 -18.859 93.477  1.00 21.91 ?  116 THR B CG2 1 
ATOM   2914 N  N   . PRO B 1 117 ? 68.581 -18.141 91.625  1.00 16.75 ?  117 PRO B N   1 
ATOM   2915 C  CA  . PRO B 1 117 ? 70.020 -18.354 91.428  1.00 22.58 ?  117 PRO B CA  1 
ATOM   2916 C  C   . PRO B 1 117 ? 70.484 -19.705 91.941  1.00 24.86 ?  117 PRO B C   1 
ATOM   2917 O  O   . PRO B 1 117 ? 71.443 -20.265 91.400  1.00 24.39 ?  117 PRO B O   1 
ATOM   2918 C  CB  . PRO B 1 117 ? 70.639 -17.189 92.204  1.00 23.67 ?  117 PRO B CB  1 
ATOM   2919 C  CG  . PRO B 1 117 ? 69.638 -16.104 92.105  1.00 20.75 ?  117 PRO B CG  1 
ATOM   2920 C  CD  . PRO B 1 117 ? 68.300 -16.787 92.147  1.00 19.27 ?  117 PRO B CD  1 
ATOM   2921 N  N   . GLU B 1 118 ? 69.796 -20.252 92.949  1.00 22.88 ?  118 GLU B N   1 
ATOM   2922 C  CA  . GLU B 1 118 ? 70.137 -21.570 93.487  1.00 21.76 ?  118 GLU B CA  1 
ATOM   2923 C  C   . GLU B 1 118 ? 69.746 -22.695 92.538  1.00 26.62 ?  118 GLU B C   1 
ATOM   2924 O  O   . GLU B 1 118 ? 70.525 -23.639 92.336  1.00 26.78 ?  118 GLU B O   1 
ATOM   2925 C  CB  . GLU B 1 118 ? 69.452 -21.786 94.836  1.00 26.63 ?  118 GLU B CB  1 
ATOM   2926 C  CG  . GLU B 1 118 ? 70.009 -20.946 95.976  1.00 27.74 ?  118 GLU B CG  1 
ATOM   2927 C  CD  . GLU B 1 118 ? 69.618 -19.486 95.877  1.00 32.73 ?  118 GLU B CD  1 
ATOM   2928 O  OE1 . GLU B 1 118 ? 68.577 -19.180 95.247  1.00 29.46 ?  118 GLU B OE1 1 
ATOM   2929 O  OE2 . GLU B 1 118 ? 70.352 -18.644 96.440  1.00 38.72 -1 118 GLU B OE2 1 
ATOM   2930 N  N   . THR B 1 119 ? 68.546 -22.627 91.940  1.00 21.73 ?  119 THR B N   1 
ATOM   2931 C  CA  . THR B 1 119 ? 68.028 -23.783 91.210  1.00 21.68 ?  119 THR B CA  1 
ATOM   2932 C  C   . THR B 1 119 ? 68.295 -23.754 89.712  1.00 25.91 ?  119 THR B C   1 
ATOM   2933 O  O   . THR B 1 119 ? 68.147 -24.797 89.058  1.00 27.33 ?  119 THR B O   1 
ATOM   2934 C  CB  . THR B 1 119 ? 66.510 -23.943 91.413  1.00 24.49 ?  119 THR B CB  1 
ATOM   2935 O  OG1 . THR B 1 119 ? 65.802 -22.849 90.800  1.00 21.66 ?  119 THR B OG1 1 
ATOM   2936 C  CG2 . THR B 1 119 ? 66.163 -24.057 92.900  1.00 26.19 ?  119 THR B CG2 1 
ATOM   2937 N  N   . THR B 1 120 ? 68.674 -22.613 89.144  1.00 22.08 ?  120 THR B N   1 
ATOM   2938 C  CA  . THR B 1 120 ? 68.906 -22.572 87.704  1.00 22.98 ?  120 THR B CA  1 
ATOM   2939 C  C   . THR B 1 120 ? 70.053 -23.505 87.330  1.00 30.47 ?  120 THR B C   1 
ATOM   2940 O  O   . THR B 1 120 ? 71.122 -23.485 87.949  1.00 25.21 ?  120 THR B O   1 
ATOM   2941 C  CB  . THR B 1 120 ? 69.187 -21.137 87.229  1.00 21.72 ?  120 THR B CB  1 
ATOM   2942 O  OG1 . THR B 1 120 ? 69.327 -21.114 85.795  1.00 21.40 ?  120 THR B OG1 1 
ATOM   2943 C  CG2 . THR B 1 120 ? 70.446 -20.548 87.899  1.00 24.10 ?  120 THR B CG2 1 
ATOM   2944 N  N   . ASP B 1 121 ? 69.809 -24.357 86.333  1.00 30.77 ?  121 ASP B N   1 
ATOM   2945 C  CA  . ASP B 1 121 ? 70.857 -25.219 85.798  1.00 31.54 ?  121 ASP B CA  1 
ATOM   2946 C  C   . ASP B 1 121 ? 71.572 -24.574 84.624  1.00 35.31 ?  121 ASP B C   1 
ATOM   2947 O  O   . ASP B 1 121 ? 72.755 -24.851 84.393  1.00 36.40 ?  121 ASP B O   1 
ATOM   2948 C  CB  . ASP B 1 121 ? 70.265 -26.561 85.350  1.00 36.56 ?  121 ASP B CB  1 
ATOM   2949 C  CG  . ASP B 1 121 ? 69.479 -27.253 86.456  1.00 45.46 ?  121 ASP B CG  1 
ATOM   2950 O  OD1 . ASP B 1 121 ? 70.093 -27.629 87.481  1.00 46.92 -1 121 ASP B OD1 1 
ATOM   2951 O  OD2 . ASP B 1 121 ? 68.246 -27.408 86.300  1.00 47.40 -1 121 ASP B OD2 1 
ATOM   2952 N  N   . THR B 1 122 ? 70.859 -23.712 83.897  1.00 26.93 ?  122 THR B N   1 
ATOM   2953 C  CA  . THR B 1 122 ? 71.324 -23.039 82.699  1.00 30.42 ?  122 THR B CA  1 
ATOM   2954 C  C   . THR B 1 122 ? 71.941 -21.678 82.981  1.00 28.42 ?  122 THR B C   1 
ATOM   2955 O  O   . THR B 1 122 ? 72.678 -21.157 82.135  1.00 27.97 ?  122 THR B O   1 
ATOM   2956 C  CB  . THR B 1 122 ? 70.144 -22.851 81.739  1.00 28.18 ?  122 THR B CB  1 
ATOM   2957 O  OG1 . THR B 1 122 ? 69.061 -22.208 82.448  1.00 24.81 ?  122 THR B OG1 1 
ATOM   2958 C  CG2 . THR B 1 122 ? 69.665 -24.203 81.225  1.00 31.95 ?  122 THR B CG2 1 
ATOM   2959 N  N   . GLY B 1 123 ? 71.648 -21.086 84.137  1.00 20.05 ?  123 GLY B N   1 
ATOM   2960 C  CA  . GLY B 1 123 ? 71.966 -19.694 84.358  1.00 20.56 ?  123 GLY B CA  1 
ATOM   2961 C  C   . GLY B 1 123 ? 71.147 -18.728 83.526  1.00 17.86 ?  123 GLY B C   1 
ATOM   2962 O  O   . GLY B 1 123 ? 71.480 -17.543 83.476  1.00 18.92 ?  123 GLY B O   1 
ATOM   2963 N  N   . TYR B 1 124 ? 70.075 -19.196 82.892  1.00 21.43 ?  124 TYR B N   1 
ATOM   2964 C  CA  . TYR B 1 124 ? 69.301 -18.374 81.957  1.00 16.37 ?  124 TYR B CA  1 
ATOM   2965 C  C   . TYR B 1 124 ? 68.315 -17.476 82.702  1.00 16.72 ?  124 TYR B C   1 
ATOM   2966 O  O   . TYR B 1 124 ? 67.405 -17.977 83.382  1.00 18.41 ?  124 TYR B O   1 
ATOM   2967 C  CB  . TYR B 1 124 ? 68.548 -19.265 80.976  1.00 16.83 ?  124 TYR B CB  1 
ATOM   2968 C  CG  . TYR B 1 124 ? 67.758 -18.482 79.952  1.00 18.15 ?  124 TYR B CG  1 
ATOM   2969 C  CD1 . TYR B 1 124 ? 68.308 -17.372 79.318  1.00 19.04 ?  124 TYR B CD1 1 
ATOM   2970 C  CD2 . TYR B 1 124 ? 66.473 -18.875 79.587  1.00 19.65 ?  124 TYR B CD2 1 
ATOM   2971 C  CE1 . TYR B 1 124 ? 67.587 -16.661 78.358  1.00 19.37 ?  124 TYR B CE1 1 
ATOM   2972 C  CE2 . TYR B 1 124 ? 65.748 -18.165 78.632  1.00 18.77 ?  124 TYR B CE2 1 
ATOM   2973 C  CZ  . TYR B 1 124 ? 66.307 -17.066 78.025  1.00 20.67 ?  124 TYR B CZ  1 
ATOM   2974 O  OH  . TYR B 1 124 ? 65.579 -16.370 77.079  1.00 22.91 ?  124 TYR B OH  1 
ATOM   2975 N  N   . LEU B 1 125 ? 68.469 -16.156 82.538  1.00 14.04 ?  125 LEU B N   1 
ATOM   2976 C  CA  . LEU B 1 125 ? 67.576 -15.195 83.183  1.00 14.63 ?  125 LEU B CA  1 
ATOM   2977 C  C   . LEU B 1 125 ? 66.121 -15.446 82.796  1.00 14.74 ?  125 LEU B C   1 
ATOM   2978 O  O   . LEU B 1 125 ? 65.211 -15.227 83.609  1.00 13.31 ?  125 LEU B O   1 
ATOM   2979 C  CB  . LEU B 1 125 ? 67.995 -13.757 82.809  1.00 12.28 ?  125 LEU B CB  1 
ATOM   2980 C  CG  . LEU B 1 125 ? 67.264 -12.579 83.480  1.00 14.18 ?  125 LEU B CG  1 
ATOM   2981 C  CD1 . LEU B 1 125 ? 67.547 -12.535 84.979  1.00 15.99 ?  125 LEU B CD1 1 
ATOM   2982 C  CD2 . LEU B 1 125 ? 67.639 -11.241 82.839  1.00 17.71 ?  125 LEU B CD2 1 
ATOM   2983 N  N   . GLY B 1 126 ? 65.885 -15.886 81.554  1.00 16.15 ?  126 GLY B N   1 
ATOM   2984 C  CA  . GLY B 1 126 ? 64.532 -16.099 81.079  1.00 14.80 ?  126 GLY B CA  1 
ATOM   2985 C  C   . GLY B 1 126 ? 63.789 -17.192 81.812  1.00 19.08 ?  126 GLY B C   1 
ATOM   2986 O  O   . GLY B 1 126 ? 62.559 -17.264 81.717  1.00 19.96 ?  126 GLY B O   1 
ATOM   2987 N  N   . GLY B 1 127 ? 64.501 -18.048 82.537  1.00 14.69 ?  127 GLY B N   1 
ATOM   2988 C  CA  . GLY B 1 127 ? 63.892 -19.058 83.376  1.00 15.04 ?  127 GLY B CA  1 
ATOM   2989 C  C   . GLY B 1 127 ? 63.741 -18.650 84.826  1.00 16.14 ?  127 GLY B C   1 
ATOM   2990 O  O   . GLY B 1 127 ? 63.403 -19.497 85.659  1.00 16.74 ?  127 GLY B O   1 
ATOM   2991 N  N   . MET B 1 128 ? 63.992 -17.378 85.154  1.00 13.96 ?  128 MET B N   1 
ATOM   2992 C  CA  . MET B 1 128 ? 63.888 -16.851 86.510  1.00 13.11 ?  128 MET B CA  1 
ATOM   2993 C  C   . MET B 1 128 ? 62.893 -15.696 86.617  1.00 14.80 ?  128 MET B C   1 
ATOM   2994 O  O   . MET B 1 128 ? 62.949 -14.920 87.579  1.00 16.72 ?  128 MET B O   1 
ATOM   2995 C  CB  . MET B 1 128 ? 65.283 -16.412 86.977  1.00 15.10 ?  128 MET B CB  1 
ATOM   2996 C  CG  . MET B 1 128 ? 66.372 -17.504 86.779  1.00 15.34 ?  128 MET B CG  1 
ATOM   2997 S  SD  . MET B 1 128 ? 68.104 -16.851 86.787  1.00 17.77 ?  128 MET B SD  1 
ATOM   2998 C  CE  . MET B 1 128 ? 68.178 -16.163 88.427  1.00 18.93 ?  128 MET B CE  1 
ATOM   2999 N  N   . VAL B 1 129 ? 61.992 -15.545 85.635  1.00 15.01 ?  129 VAL B N   1 
ATOM   3000 C  CA  . VAL B 1 129 ? 61.178 -14.330 85.528  1.00 11.73 ?  129 VAL B CA  1 
ATOM   3001 C  C   . VAL B 1 129 ? 60.044 -14.316 86.546  1.00 13.59 ?  129 VAL B C   1 
ATOM   3002 O  O   . VAL B 1 129 ? 59.838 -13.330 87.259  1.00 13.67 ?  129 VAL B O   1 
ATOM   3003 C  CB  . VAL B 1 129 ? 60.617 -14.197 84.102  1.00 11.92 ?  129 VAL B CB  1 
ATOM   3004 C  CG1 . VAL B 1 129 ? 59.656 -12.993 84.024  1.00 12.32 ?  129 VAL B CG1 1 
ATOM   3005 C  CG2 . VAL B 1 129 ? 61.759 -14.056 83.119  1.00 16.47 ?  129 VAL B CG2 1 
ATOM   3006 N  N   . LEU B 1 130 ? 59.241 -15.382 86.591  1.00 12.50 ?  130 LEU B N   1 
ATOM   3007 C  CA  . LEU B 1 130 ? 58.078 -15.336 87.471  1.00 12.41 ?  130 LEU B CA  1 
ATOM   3008 C  C   . LEU B 1 130 ? 58.509 -15.374 88.930  1.00 16.16 ?  130 LEU B C   1 
ATOM   3009 O  O   . LEU B 1 130 ? 57.912 -14.699 89.777  1.00 15.27 ?  130 LEU B O   1 
ATOM   3010 C  CB  . LEU B 1 130 ? 57.108 -16.475 87.132  1.00 12.85 ?  130 LEU B CB  1 
ATOM   3011 C  CG  . LEU B 1 130 ? 55.791 -16.525 87.926  1.00 15.43 ?  130 LEU B CG  1 
ATOM   3012 C  CD1 . LEU B 1 130 ? 54.978 -15.267 87.793  1.00 16.36 ?  130 LEU B CD1 1 
ATOM   3013 C  CD2 . LEU B 1 130 ? 54.966 -17.760 87.511  1.00 16.26 ?  130 LEU B CD2 1 
ATOM   3014 N  N   . SER B 1 131 ? 59.585 -16.107 89.228  1.00 15.13 ?  131 SER B N   1 
ATOM   3015 C  CA  . SER B 1 131 ? 60.117 -16.117 90.589  1.00 15.87 ?  131 SER B CA  1 
ATOM   3016 C  C   . SER B 1 131 ? 60.654 -14.748 90.978  1.00 17.26 ?  131 SER B C   1 
ATOM   3017 O  O   . SER B 1 131 ? 60.517 -14.321 92.133  1.00 18.68 ?  131 SER B O   1 
ATOM   3018 C  CB  . SER B 1 131 ? 61.207 -17.177 90.696  1.00 15.91 ?  131 SER B CB  1 
ATOM   3019 O  OG  . SER B 1 131 ? 62.132 -17.029 89.625  1.00 17.54 ?  131 SER B OG  1 
ATOM   3020 N  N   . GLY B 1 132 ? 61.273 -14.044 90.031  1.00 15.95 ?  132 GLY B N   1 
ATOM   3021 C  CA  . GLY B 1 132 ? 61.755 -12.706 90.329  1.00 14.14 ?  132 GLY B CA  1 
ATOM   3022 C  C   . GLY B 1 132 ? 60.614 -11.756 90.628  1.00 18.38 ?  132 GLY B C   1 
ATOM   3023 O  O   . GLY B 1 132 ? 60.665 -10.978 91.584  1.00 18.94 ?  132 GLY B O   1 
ATOM   3024 N  N   . ALA B 1 133 ? 59.560 -11.813 89.813  1.00 15.80 ?  133 ALA B N   1 
ATOM   3025 C  CA  . ALA B 1 133 ? 58.424 -10.923 90.020  1.00 16.51 ?  133 ALA B CA  1 
ATOM   3026 C  C   . ALA B 1 133 ? 57.711 -11.221 91.329  1.00 16.54 ?  133 ALA B C   1 
ATOM   3027 O  O   . ALA B 1 133 ? 57.118 -10.317 91.923  1.00 16.79 ?  133 ALA B O   1 
ATOM   3028 C  CB  . ALA B 1 133 ? 57.437 -11.045 88.846  1.00 16.53 ?  133 ALA B CB  1 
ATOM   3029 N  N   . CYS B 1 134 ? 57.737 -12.479 91.778  1.00 16.19 ?  134 CYS B N   1 
ATOM   3030 C  CA  . CYS B 1 134 ? 57.117 -12.883 93.034  1.00 15.34 ?  134 CYS B CA  1 
ATOM   3031 C  C   . CYS B 1 134 ? 58.048 -12.708 94.224  1.00 17.55 ?  134 CYS B C   1 
ATOM   3032 O  O   . CYS B 1 134 ? 57.657 -13.039 95.348  1.00 23.70 ?  134 CYS B O   1 
ATOM   3033 C  CB  . CYS B 1 134 ? 56.661 -14.346 92.968  1.00 15.35 ?  134 CYS B CB  1 
ATOM   3034 S  SG  . CYS B 1 134 ? 55.240 -14.601 91.854  1.00 20.63 ?  134 CYS B SG  1 
ATOM   3035 N  N   . GLY B 1 135 ? 59.268 -12.217 94.005  1.00 16.49 ?  135 GLY B N   1 
ATOM   3036 C  CA  . GLY B 1 135 ? 60.146 -11.882 95.113  1.00 19.63 ?  135 GLY B CA  1 
ATOM   3037 C  C   . GLY B 1 135 ? 60.940 -13.027 95.710  1.00 23.40 ?  135 GLY B C   1 
ATOM   3038 O  O   . GLY B 1 135 ? 61.468 -12.879 96.820  1.00 21.35 ?  135 GLY B O   1 
ATOM   3039 N  N   . LEU B 1 136 ? 61.062 -14.163 95.015  1.00 17.90 ?  136 LEU B N   1 
ATOM   3040 C  CA  . LEU B 1 136 ? 61.911 -15.243 95.525  1.00 20.65 ?  136 LEU B CA  1 
ATOM   3041 C  C   . LEU B 1 136 ? 63.395 -14.928 95.387  1.00 21.14 ?  136 LEU B C   1 
ATOM   3042 O  O   . LEU B 1 136 ? 64.219 -15.510 96.104  1.00 21.12 ?  136 LEU B O   1 
ATOM   3043 C  CB  . LEU B 1 136 ? 61.599 -16.559 94.814  1.00 21.60 ?  136 LEU B CB  1 
ATOM   3044 C  CG  . LEU B 1 136 ? 60.401 -17.339 95.366  1.00 26.85 ?  136 LEU B CG  1 
ATOM   3045 C  CD1 . LEU B 1 136 ? 59.059 -16.744 94.922  1.00 25.43 ?  136 LEU B CD1 1 
ATOM   3046 C  CD2 . LEU B 1 136 ? 60.503 -18.811 95.018  1.00 25.26 ?  136 LEU B CD2 1 
ATOM   3047 N  N   . TRP B 1 137 ? 63.755 -14.051 94.465  1.00 20.73 ?  137 TRP B N   1 
ATOM   3048 C  CA  . TRP B 1 137 ? 65.097 -13.500 94.374  1.00 18.32 ?  137 TRP B CA  1 
ATOM   3049 C  C   . TRP B 1 137 ? 64.939 -12.067 93.891  1.00 22.42 ?  137 TRP B C   1 
ATOM   3050 O  O   . TRP B 1 137 ? 63.873 -11.672 93.412  1.00 21.52 ?  137 TRP B O   1 
ATOM   3051 C  CB  . TRP B 1 137 ? 66.004 -14.355 93.452  1.00 19.02 ?  137 TRP B CB  1 
ATOM   3052 C  CG  . TRP B 1 137 ? 65.588 -14.294 91.995  1.00 18.62 ?  137 TRP B CG  1 
ATOM   3053 C  CD1 . TRP B 1 137 ? 64.544 -14.959 91.406  1.00 20.70 ?  137 TRP B CD1 1 
ATOM   3054 C  CD2 . TRP B 1 137 ? 66.208 -13.524 90.964  1.00 17.75 ?  137 TRP B CD2 1 
ATOM   3055 N  NE1 . TRP B 1 137 ? 64.464 -14.625 90.061  1.00 17.50 ?  137 TRP B NE1 1 
ATOM   3056 C  CE2 . TRP B 1 137 ? 65.479 -13.751 89.769  1.00 16.11 ?  137 TRP B CE2 1 
ATOM   3057 C  CE3 . TRP B 1 137 ? 67.306 -12.658 90.927  1.00 17.37 ?  137 TRP B CE3 1 
ATOM   3058 C  CZ2 . TRP B 1 137 ? 65.821 -13.149 88.561  1.00 19.06 ?  137 TRP B CZ2 1 
ATOM   3059 C  CZ3 . TRP B 1 137 ? 67.642 -12.059 89.721  1.00 20.22 ?  137 TRP B CZ3 1 
ATOM   3060 C  CH2 . TRP B 1 137 ? 66.898 -12.301 88.558  1.00 19.33 ?  137 TRP B CH2 1 
ATOM   3061 N  N   . ASP B 1 138 ? 65.992 -11.271 94.040  1.00 19.62 ?  138 ASP B N   1 
ATOM   3062 C  CA  . ASP B 1 138 ? 65.899 -9.828  93.831  1.00 18.95 ?  138 ASP B CA  1 
ATOM   3063 C  C   . ASP B 1 138 ? 66.531 -9.471  92.491  1.00 25.33 ?  138 ASP B C   1 
ATOM   3064 O  O   . ASP B 1 138 ? 67.760 -9.463  92.358  1.00 21.42 ?  138 ASP B O   1 
ATOM   3065 C  CB  . ASP B 1 138 ? 66.583 -9.068  94.966  1.00 24.01 ?  138 ASP B CB  1 
ATOM   3066 C  CG  . ASP B 1 138 ? 66.423 -7.565  94.845  1.00 29.94 ?  138 ASP B CG  1 
ATOM   3067 O  OD1 . ASP B 1 138 ? 65.795 -7.093  93.869  1.00 29.38 ?  138 ASP B OD1 1 
ATOM   3068 O  OD2 . ASP B 1 138 ? 66.918 -6.843  95.738  1.00 34.14 -1 138 ASP B OD2 1 
ATOM   3069 N  N   . SER B 1 139 ? 65.686 -9.131  91.513  1.00 21.47 ?  139 SER B N   1 
ATOM   3070 C  CA  . SER B 1 139 ? 66.159 -8.747  90.192  1.00 20.65 ?  139 SER B CA  1 
ATOM   3071 C  C   . SER B 1 139 ? 66.702 -7.331  90.138  1.00 21.78 ?  139 SER B C   1 
ATOM   3072 O  O   . SER B 1 139 ? 67.385 -6.986  89.167  1.00 22.72 ?  139 SER B O   1 
ATOM   3073 C  CB  . SER B 1 139 ? 65.021 -8.881  89.183  1.00 19.83 ?  139 SER B CB  1 
ATOM   3074 O  OG  . SER B 1 139 ? 64.077 -7.850  89.411  1.00 20.74 ?  139 SER B OG  1 
ATOM   3075 N  N   . GLY B 1 140 ? 66.419 -6.511  91.148  1.00 20.10 ?  140 GLY B N   1 
ATOM   3076 C  CA  . GLY B 1 140 ? 66.739 -5.105  91.114  1.00 18.73 ?  140 GLY B CA  1 
ATOM   3077 C  C   . GLY B 1 140 ? 65.704 -4.252  90.425  1.00 25.97 ?  140 GLY B C   1 
ATOM   3078 O  O   . GLY B 1 140 ? 65.858 -3.024  90.382  1.00 24.06 ?  140 GLY B O   1 
ATOM   3079 N  N   . HIS B 1 141 ? 64.655 -4.869  89.880  1.00 19.88 ?  141 HIS B N   1 
ATOM   3080 C  CA  . HIS B 1 141 ? 63.593 -4.164  89.177  1.00 17.24 ?  141 HIS B CA  1 
ATOM   3081 C  C   . HIS B 1 141 ? 62.251 -4.336  89.872  1.00 22.27 ?  141 HIS B C   1 
ATOM   3082 O  O   . HIS B 1 141 ? 61.206 -4.019  89.289  1.00 22.82 ?  141 HIS B O   1 
ATOM   3083 C  CB  . HIS B 1 141 ? 63.543 -4.644  87.716  1.00 19.92 ?  141 HIS B CB  1 
ATOM   3084 C  CG  . HIS B 1 141 ? 64.765 -4.262  86.938  1.00 17.99 ?  141 HIS B CG  1 
ATOM   3085 N  ND1 . HIS B 1 141 ? 64.932 -3.009  86.396  1.00 23.60 ?  141 HIS B ND1 1 
ATOM   3086 C  CD2 . HIS B 1 141 ? 65.904 -4.944  86.668  1.00 21.70 ?  141 HIS B CD2 1 
ATOM   3087 C  CE1 . HIS B 1 141 ? 66.113 -2.940  85.806  1.00 22.14 ?  141 HIS B CE1 1 
ATOM   3088 N  NE2 . HIS B 1 141 ? 66.722 -4.102  85.955  1.00 21.71 ?  141 HIS B NE2 1 
ATOM   3089 N  N   . GLY B 1 142 ? 62.255 -4.815  91.110  1.00 21.16 ?  142 GLY B N   1 
ATOM   3090 C  CA  . GLY B 1 142 ? 61.052 -4.859  91.910  1.00 22.18 ?  142 GLY B CA  1 
ATOM   3091 C  C   . GLY B 1 142 ? 60.436 -6.245  91.945  1.00 21.26 ?  142 GLY B C   1 
ATOM   3092 O  O   . GLY B 1 142 ? 60.814 -7.161  91.209  1.00 19.71 ?  142 GLY B O   1 
ATOM   3093 N  N   . ALA B 1 143 ? 59.472 -6.391  92.849  1.00 20.18 ?  143 ALA B N   1 
ATOM   3094 C  CA  . ALA B 1 143 ? 58.714 -7.630  92.964  1.00 16.19 ?  143 ALA B CA  1 
ATOM   3095 C  C   . ALA B 1 143 ? 57.257 -7.284  93.227  1.00 17.34 ?  143 ALA B C   1 
ATOM   3096 O  O   . ALA B 1 143 ? 56.654 -6.500  92.481  1.00 20.08 ?  143 ALA B O   1 
ATOM   3097 C  CB  . ALA B 1 143 ? 59.279 -8.517  94.073  1.00 18.71 ?  143 ALA B CB  1 
ATOM   3098 N  N   . GLY B 1 144 ? 56.672 -7.873  94.269  1.00 18.69 ?  144 GLY B N   1 
ATOM   3099 C  CA  . GLY B 1 144 ? 55.343 -7.505  94.693  1.00 19.80 ?  144 GLY B CA  1 
ATOM   3100 C  C   . GLY B 1 144 ? 54.203 -8.290  94.071  1.00 17.73 ?  144 GLY B C   1 
ATOM   3101 O  O   . GLY B 1 144 ? 53.051 -8.074  94.454  1.00 18.04 ?  144 GLY B O   1 
ATOM   3102 N  N   . LEU B 1 145 ? 54.462 -9.162  93.104  1.00 14.78 ?  145 LEU B N   1 
ATOM   3103 C  CA  . LEU B 1 145 ? 53.399 -10.041 92.622  1.00 17.25 ?  145 LEU B CA  1 
ATOM   3104 C  C   . LEU B 1 145 ? 53.177 -11.168 93.636  1.00 17.30 ?  145 LEU B C   1 
ATOM   3105 O  O   . LEU B 1 145 ? 54.115 -11.897 93.975  1.00 17.55 ?  145 LEU B O   1 
ATOM   3106 C  CB  . LEU B 1 145 ? 53.758 -10.602 91.246  1.00 16.08 ?  145 LEU B CB  1 
ATOM   3107 C  CG  . LEU B 1 145 ? 52.780 -11.617 90.640  1.00 16.01 ?  145 LEU B CG  1 
ATOM   3108 C  CD1 . LEU B 1 145 ? 51.390 -11.019 90.423  1.00 17.47 ?  145 LEU B CD1 1 
ATOM   3109 C  CD2 . LEU B 1 145 ? 53.353 -12.214 89.334  1.00 17.43 ?  145 LEU B CD2 1 
ATOM   3110 N  N   . ARG B 1 146 ? 51.946 -11.307 94.137  1.00 16.38 ?  146 ARG B N   1 
ATOM   3111 C  CA  . ARG B 1 146 ? 51.648 -12.391 95.072  1.00 17.59 ?  146 ARG B CA  1 
ATOM   3112 C  C   . ARG B 1 146 ? 51.612 -13.720 94.328  1.00 19.58 ?  146 ARG B C   1 
ATOM   3113 O  O   . ARG B 1 146 ? 50.877 -13.846 93.346  1.00 17.20 ?  146 ARG B O   1 
ATOM   3114 C  CB  . ARG B 1 146 ? 50.301 -12.162 95.777  1.00 18.74 ?  146 ARG B CB  1 
ATOM   3115 C  CG  . ARG B 1 146 ? 50.232 -10.864 96.589  1.00 22.08 ?  146 ARG B CG  1 
ATOM   3116 C  CD  . ARG B 1 146 ? 48.862 -10.678 97.247  1.00 28.99 ?  146 ARG B CD  1 
ATOM   3117 N  NE  . ARG B 1 146 ? 48.624 -11.672 98.295  1.00 30.29 ?  146 ARG B NE  1 
ATOM   3118 C  CZ  . ARG B 1 146 ? 47.649 -12.584 98.278  1.00 32.48 ?  146 ARG B CZ  1 
ATOM   3119 N  NH1 . ARG B 1 146 ? 46.794 -12.646 97.264  1.00 30.02 ?  146 ARG B NH1 1 
ATOM   3120 N  NH2 . ARG B 1 146 ? 47.526 -13.437 99.287  1.00 30.70 ?  146 ARG B NH2 1 
ATOM   3121 N  N   . PRO B 1 147 ? 52.378 -14.728 94.759  1.00 16.67 ?  147 PRO B N   1 
ATOM   3122 C  CA  . PRO B 1 147 ? 52.295 -16.048 94.100  1.00 17.46 ?  147 PRO B CA  1 
ATOM   3123 C  C   . PRO B 1 147 ? 50.884 -16.615 94.079  1.00 18.20 ?  147 PRO B C   1 
ATOM   3124 O  O   . PRO B 1 147 ? 50.532 -17.380 93.169  1.00 18.88 ?  147 PRO B O   1 
ATOM   3125 C  CB  . PRO B 1 147 ? 53.226 -16.934 94.942  1.00 22.42 ?  147 PRO B CB  1 
ATOM   3126 C  CG  . PRO B 1 147 ? 54.046 -16.011 95.764  1.00 22.67 ?  147 PRO B CG  1 
ATOM   3127 C  CD  . PRO B 1 147 ? 53.336 -14.699 95.880  1.00 20.14 ?  147 PRO B CD  1 
ATOM   3128 N  N   . GLU B 1 148 ? 50.067 -16.268 95.078  1.00 17.92 ?  148 GLU B N   1 
ATOM   3129 C  CA  . GLU B 1 148 ? 48.674 -16.707 95.093  1.00 22.51 ?  148 GLU B CA  1 
ATOM   3130 C  C   . GLU B 1 148 ? 47.882 -16.138 93.929  1.00 21.52 ?  148 GLU B C   1 
ATOM   3131 O  O   . GLU B 1 148 ? 46.802 -16.657 93.613  1.00 20.19 ?  148 GLU B O   1 
ATOM   3132 C  CB  . GLU B 1 148 ? 48.017 -16.298 96.411  1.00 24.03 ?  148 GLU B CB  1 
ATOM   3133 C  CG  . GLU B 1 148 ? 48.661 -16.970 97.611  1.00 26.81 ?  148 GLU B CG  1 
ATOM   3134 C  CD  . GLU B 1 148 ? 49.707 -16.111 98.311  1.00 34.70 ?  148 GLU B CD  1 
ATOM   3135 O  OE1 . GLU B 1 148 ? 50.233 -15.137 97.711  1.00 26.94 ?  148 GLU B OE1 1 
ATOM   3136 O  OE2 . GLU B 1 148 ? 50.011 -16.433 99.479  1.00 33.68 -1 148 GLU B OE2 1 
ATOM   3137 N  N   . GLN B 1 149 ? 48.390 -15.081 93.294  1.00 16.97 ?  149 GLN B N   1 
ATOM   3138 C  CA  . GLN B 1 149 ? 47.720 -14.458 92.162  1.00 15.02 ?  149 GLN B CA  1 
ATOM   3139 C  C   . GLN B 1 149 ? 48.455 -14.692 90.844  1.00 14.11 ?  149 GLN B C   1 
ATOM   3140 O  O   . GLN B 1 149 ? 48.168 -14.004 89.863  1.00 18.01 ?  149 GLN B O   1 
ATOM   3141 C  CB  . GLN B 1 149 ? 47.533 -12.961 92.433  1.00 19.31 ?  149 GLN B CB  1 
ATOM   3142 C  CG  . GLN B 1 149 ? 46.576 -12.729 93.612  1.00 18.19 ?  149 GLN B CG  1 
ATOM   3143 C  CD  . GLN B 1 149 ? 46.495 -11.301 94.072  1.00 20.66 ?  149 GLN B CD  1 
ATOM   3144 O  OE1 . GLN B 1 149 ? 46.364 -11.048 95.269  1.00 22.47 ?  149 GLN B OE1 1 
ATOM   3145 N  NE2 . GLN B 1 149 ? 46.501 -10.350 93.127  1.00 18.31 ?  149 GLN B NE2 1 
ATOM   3146 N  N   . ALA B 1 150 ? 49.394 -15.642 90.811  1.00 14.56 ?  150 ALA B N   1 
ATOM   3147 C  CA  . ALA B 1 150 ? 50.053 -16.091 89.590  1.00 14.95 ?  150 ALA B CA  1 
ATOM   3148 C  C   . ALA B 1 150 ? 49.556 -17.489 89.248  1.00 16.42 ?  150 ALA B C   1 
ATOM   3149 O  O   . ALA B 1 150 ? 49.478 -18.358 90.124  1.00 16.34 ?  150 ALA B O   1 
ATOM   3150 C  CB  . ALA B 1 150 ? 51.578 -16.092 89.747  1.00 18.39 ?  150 ALA B CB  1 
ATOM   3151 N  N   . VAL B 1 151 ? 49.199 -17.700 87.983  1.00 13.08 ?  151 VAL B N   1 
ATOM   3152 C  CA  . VAL B 1 151 ? 48.738 -19.000 87.497  1.00 12.02 ?  151 VAL B CA  1 
ATOM   3153 C  C   . VAL B 1 151 ? 49.607 -19.395 86.312  1.00 14.43 ?  151 VAL B C   1 
ATOM   3154 O  O   . VAL B 1 151 ? 49.592 -18.710 85.284  1.00 15.10 ?  151 VAL B O   1 
ATOM   3155 C  CB  . VAL B 1 151 ? 47.261 -18.968 87.065  1.00 14.66 ?  151 VAL B CB  1 
ATOM   3156 C  CG1 . VAL B 1 151 ? 46.824 -20.350 86.529  1.00 16.88 ?  151 VAL B CG1 1 
ATOM   3157 C  CG2 . VAL B 1 151 ? 46.339 -18.519 88.200  1.00 20.21 ?  151 VAL B CG2 1 
ATOM   3158 N  N   . LEU B 1 152 ? 50.337 -20.504 86.438  1.00 13.24 ?  152 LEU B N   1 
ATOM   3159 C  CA  . LEU B 1 152 ? 51.056 -21.073 85.304  1.00 11.76 ?  152 LEU B CA  1 
ATOM   3160 C  C   . LEU B 1 152 ? 50.094 -21.871 84.440  1.00 15.36 ?  152 LEU B C   1 
ATOM   3161 O  O   . LEU B 1 152 ? 49.408 -22.769 84.939  1.00 16.12 ?  152 LEU B O   1 
ATOM   3162 C  CB  . LEU B 1 152 ? 52.190 -21.975 85.788  1.00 15.84 ?  152 LEU B CB  1 
ATOM   3163 C  CG  . LEU B 1 152 ? 53.370 -21.137 86.279  1.00 12.70 ?  152 LEU B CG  1 
ATOM   3164 C  CD1 . LEU B 1 152 ? 54.292 -21.985 87.160  1.00 16.37 ?  152 LEU B CD1 1 
ATOM   3165 C  CD2 . LEU B 1 152 ? 54.117 -20.537 85.098  1.00 15.02 ?  152 LEU B CD2 1 
ATOM   3166 N  N   . VAL B 1 153 ? 50.050 -21.563 83.144  1.00 13.63 ?  153 VAL B N   1 
ATOM   3167 C  CA  . VAL B 1 153 ? 49.141 -22.243 82.222  1.00 13.50 ?  153 VAL B CA  1 
ATOM   3168 C  C   . VAL B 1 153 ? 49.971 -22.919 81.138  1.00 13.80 ?  153 VAL B C   1 
ATOM   3169 O  O   . VAL B 1 153 ? 50.737 -22.259 80.429  1.00 14.26 ?  153 VAL B O   1 
ATOM   3170 C  CB  . VAL B 1 153 ? 48.120 -21.273 81.612  1.00 13.70 ?  153 VAL B CB  1 
ATOM   3171 C  CG1 . VAL B 1 153 ? 47.159 -22.028 80.703  1.00 15.87 ?  153 VAL B CG1 1 
ATOM   3172 C  CG2 . VAL B 1 153 ? 47.332 -20.538 82.725  1.00 15.30 ?  153 VAL B CG2 1 
ATOM   3173 N  N   . GLY B 1 154 ? 49.823 -24.228 81.013  1.00 14.04 ?  154 GLY B N   1 
ATOM   3174 C  CA  . GLY B 1 154 ? 50.504 -24.962 79.973  1.00 14.69 ?  154 GLY B CA  1 
ATOM   3175 C  C   . GLY B 1 154 ? 51.868 -25.502 80.325  1.00 15.35 ?  154 GLY B C   1 
ATOM   3176 O  O   . GLY B 1 154 ? 52.487 -26.167 79.481  1.00 16.38 ?  154 GLY B O   1 
ATOM   3177 N  N   . SER B 1 155 ? 52.367 -25.238 81.532  1.00 13.62 ?  155 SER B N   1 
ATOM   3178 C  CA  . SER B 1 155 ? 53.720 -25.631 81.878  1.00 14.39 ?  155 SER B CA  1 
ATOM   3179 C  C   . SER B 1 155 ? 53.832 -27.137 82.093  1.00 20.77 ?  155 SER B C   1 
ATOM   3180 O  O   . SER B 1 155 ? 52.918 -27.788 82.614  1.00 20.40 ?  155 SER B O   1 
ATOM   3181 C  CB  . SER B 1 155 ? 54.185 -24.875 83.124  1.00 17.95 ?  155 SER B CB  1 
ATOM   3182 O  OG  . SER B 1 155 ? 53.823 -23.504 83.047  1.00 18.12 ?  155 SER B OG  1 
ATOM   3183 N  N   . ARG B 1 156 ? 54.967 -27.693 81.683  1.00 17.56 ?  156 ARG B N   1 
ATOM   3184 C  CA  . ARG B 1 156 ? 55.103 -29.142 81.679  1.00 17.43 ?  156 ARG B CA  1 
ATOM   3185 C  C   . ARG B 1 156 ? 56.572 -29.512 81.814  1.00 22.50 ?  156 ARG B C   1 
ATOM   3186 O  O   . ARG B 1 156 ? 57.467 -28.704 81.538  1.00 20.97 ?  156 ARG B O   1 
ATOM   3187 C  CB  . ARG B 1 156 ? 54.525 -29.732 80.393  1.00 20.31 ?  156 ARG B CB  1 
ATOM   3188 C  CG  . ARG B 1 156 ? 55.202 -29.170 79.141  1.00 20.94 ?  156 ARG B CG  1 
ATOM   3189 C  CD  . ARG B 1 156 ? 54.274 -29.245 77.960  1.00 20.79 ?  156 ARG B CD  1 
ATOM   3190 N  NE  . ARG B 1 156 ? 54.858 -28.732 76.718  1.00 21.07 ?  156 ARG B NE  1 
ATOM   3191 C  CZ  . ARG B 1 156 ? 54.621 -27.519 76.222  1.00 22.22 ?  156 ARG B CZ  1 
ATOM   3192 N  NH1 . ARG B 1 156 ? 53.817 -26.664 76.861  1.00 15.70 ?  156 ARG B NH1 1 
ATOM   3193 N  NH2 . ARG B 1 156 ? 55.180 -27.170 75.075  1.00 18.95 ?  156 ARG B NH2 1 
ATOM   3194 N  N   . ASP B 1 157 ? 56.809 -30.761 82.239  1.00 24.55 ?  157 ASP B N   1 
ATOM   3195 C  CA  . ASP B 1 157 ? 58.166 -31.313 82.320  1.00 23.24 ?  157 ASP B CA  1 
ATOM   3196 C  C   . ASP B 1 157 ? 59.035 -30.473 83.255  1.00 27.09 ?  157 ASP B C   1 
ATOM   3197 O  O   . ASP B 1 157 ? 60.226 -30.270 83.018  1.00 30.25 ?  157 ASP B O   1 
ATOM   3198 C  CB  . ASP B 1 157 ? 58.778 -31.420 80.915  1.00 30.78 ?  157 ASP B CB  1 
ATOM   3199 C  CG  . ASP B 1 157 ? 60.043 -32.258 80.869  1.00 44.47 ?  157 ASP B CG  1 
ATOM   3200 O  OD1 . ASP B 1 157 ? 59.935 -33.501 80.917  1.00 50.45 -1 157 ASP B OD1 1 
ATOM   3201 O  OD2 . ASP B 1 157 ? 61.140 -31.674 80.735  1.00 46.13 ?  157 ASP B OD2 1 
ATOM   3202 N  N   . ILE B 1 158 ? 58.426 -29.955 84.318  1.00 22.09 ?  158 ILE B N   1 
ATOM   3203 C  CA  . ILE B 1 158 ? 59.110 -29.042 85.230  1.00 22.59 ?  158 ILE B CA  1 
ATOM   3204 C  C   . ILE B 1 158 ? 60.052 -29.839 86.122  1.00 23.97 ?  158 ILE B C   1 
ATOM   3205 O  O   . ILE B 1 158 ? 59.671 -30.886 86.651  1.00 26.83 ?  158 ILE B O   1 
ATOM   3206 C  CB  . ILE B 1 158 ? 58.084 -28.260 86.069  1.00 25.47 ?  158 ILE B CB  1 
ATOM   3207 C  CG1 . ILE B 1 158 ? 57.089 -27.531 85.151  1.00 26.18 ?  158 ILE B CG1 1 
ATOM   3208 C  CG2 . ILE B 1 158 ? 58.786 -27.281 86.986  1.00 24.96 ?  158 ILE B CG2 1 
ATOM   3209 C  CD1 . ILE B 1 158 ? 55.917 -26.904 85.911  1.00 23.69 ?  158 ILE B CD1 1 
ATOM   3210 N  N   . ASP B 1 159 ? 61.273 -29.341 86.317  1.00 25.89 ?  159 ASP B N   1 
ATOM   3211 C  CA  . ASP B 1 159 ? 62.231 -30.120 87.092  1.00 34.35 ?  159 ASP B CA  1 
ATOM   3212 C  C   . ASP B 1 159 ? 61.876 -30.098 88.576  1.00 34.10 ?  159 ASP B C   1 
ATOM   3213 O  O   . ASP B 1 159 ? 61.123 -29.241 89.062  1.00 29.08 ?  159 ASP B O   1 
ATOM   3214 C  CB  . ASP B 1 159 ? 63.665 -29.621 86.887  1.00 37.74 ?  159 ASP B CB  1 
ATOM   3215 C  CG  . ASP B 1 159 ? 63.964 -28.351 87.658  1.00 40.58 ?  159 ASP B CG  1 
ATOM   3216 O  OD1 . ASP B 1 159 ? 63.559 -27.272 87.185  1.00 43.49 -1 159 ASP B OD1 1 
ATOM   3217 O  OD2 . ASP B 1 159 ? 64.604 -28.430 88.739  1.00 40.23 -1 159 ASP B OD2 1 
ATOM   3218 N  N   . GLU B 1 160 ? 62.459 -31.058 89.296  1.00 32.52 ?  160 GLU B N   1 
ATOM   3219 C  CA  . GLU B 1 160 ? 62.067 -31.341 90.676  1.00 35.61 ?  160 GLU B CA  1 
ATOM   3220 C  C   . GLU B 1 160 ? 62.197 -30.110 91.572  1.00 31.09 ?  160 GLU B C   1 
ATOM   3221 O  O   . GLU B 1 160 ? 61.259 -29.758 92.297  1.00 31.62 ?  160 GLU B O   1 
ATOM   3222 C  CB  . GLU B 1 160 ? 62.891 -32.531 91.203  1.00 31.96 ?  160 GLU B CB  1 
ATOM   3223 C  CG  . GLU B 1 160 ? 64.210 -32.224 91.948  1.00 45.71 ?  160 GLU B CG  1 
ATOM   3224 C  CD  . GLU B 1 160 ? 65.337 -31.702 91.043  1.00 50.60 ?  160 GLU B CD  1 
ATOM   3225 O  OE1 . GLU B 1 160 ? 66.517 -31.802 91.452  1.00 57.04 ?  160 GLU B OE1 1 
ATOM   3226 O  OE2 . GLU B 1 160 ? 65.048 -31.173 89.940  1.00 46.23 -1 160 GLU B OE2 1 
ATOM   3227 N  N   . GLY B 1 161 ? 63.336 -29.419 91.512  1.00 28.09 ?  161 GLY B N   1 
ATOM   3228 C  CA  . GLY B 1 161 ? 63.559 -28.312 92.424  1.00 32.34 ?  161 GLY B CA  1 
ATOM   3229 C  C   . GLY B 1 161 ? 62.694 -27.115 92.096  1.00 29.91 ?  161 GLY B C   1 
ATOM   3230 O  O   . GLY B 1 161 ? 62.166 -26.451 92.995  1.00 23.43 ?  161 GLY B O   1 
ATOM   3231 N  N   . GLU B 1 162 ? 62.524 -26.832 90.803  1.00 23.89 ?  162 GLU B N   1 
ATOM   3232 C  CA  . GLU B 1 162 ? 61.671 -25.726 90.385  1.00 26.53 ?  162 GLU B CA  1 
ATOM   3233 C  C   . GLU B 1 162 ? 60.215 -25.998 90.748  1.00 22.42 ?  162 GLU B C   1 
ATOM   3234 O  O   . GLU B 1 162 ? 59.516 -25.108 91.248  1.00 22.45 ?  162 GLU B O   1 
ATOM   3235 C  CB  . GLU B 1 162 ? 61.837 -25.495 88.881  1.00 24.88 ?  162 GLU B CB  1 
ATOM   3236 C  CG  . GLU B 1 162 ? 61.077 -24.300 88.316  1.00 22.33 ?  162 GLU B CG  1 
ATOM   3237 C  CD  . GLU B 1 162 ? 61.261 -24.144 86.804  1.00 22.82 ?  162 GLU B CD  1 
ATOM   3238 O  OE1 . GLU B 1 162 ? 60.893 -23.080 86.271  1.00 24.18 ?  162 GLU B OE1 1 
ATOM   3239 O  OE2 . GLU B 1 162 ? 61.764 -25.078 86.142  1.00 24.22 -1 162 GLU B OE2 1 
ATOM   3240 N  N   . ARG B 1 163 ? 59.752 -27.232 90.533  1.00 19.33 ?  163 ARG B N   1 
ATOM   3241 C  CA  . ARG B 1 163 ? 58.364 -27.571 90.836  1.00 21.56 ?  163 ARG B CA  1 
ATOM   3242 C  C   . ARG B 1 163 ? 58.074 -27.418 92.321  1.00 22.26 ?  163 ARG B C   1 
ATOM   3243 O  O   . ARG B 1 163 ? 56.980 -26.995 92.706  1.00 21.53 ?  163 ARG B O   1 
ATOM   3244 C  CB  . ARG B 1 163 ? 58.053 -28.996 90.370  1.00 24.74 ?  163 ARG B CB  1 
ATOM   3245 C  CG  . ARG B 1 163 ? 56.573 -29.386 90.449  1.00 27.07 ?  163 ARG B CG  1 
ATOM   3246 C  CD  . ARG B 1 163 ? 55.721 -28.627 89.428  1.00 27.09 ?  163 ARG B CD  1 
ATOM   3247 N  NE  . ARG B 1 163 ? 54.283 -28.863 89.599  1.00 33.10 ?  163 ARG B NE  1 
ATOM   3248 C  CZ  . ARG B 1 163 ? 53.532 -28.306 90.554  1.00 34.75 ?  163 ARG B CZ  1 
ATOM   3249 N  NH1 . ARG B 1 163 ? 54.073 -27.475 91.434  1.00 29.72 ?  163 ARG B NH1 1 
ATOM   3250 N  NH2 . ARG B 1 163 ? 52.233 -28.582 90.635  1.00 39.47 ?  163 ARG B NH2 1 
ATOM   3251 N  N   . GLU B 1 164 ? 59.048 -27.743 93.169  1.00 24.10 ?  164 GLU B N   1 
ATOM   3252 C  CA  . GLU B 1 164 ? 58.848 -27.588 94.607  1.00 24.89 ?  164 GLU B CA  1 
ATOM   3253 C  C   . GLU B 1 164 ? 58.818 -26.120 95.015  1.00 22.79 ?  164 GLU B C   1 
ATOM   3254 O  O   . GLU B 1 164 ? 58.016 -25.734 95.875  1.00 22.55 ?  164 GLU B O   1 
ATOM   3255 C  CB  . GLU B 1 164 ? 59.932 -28.347 95.371  1.00 26.87 ?  164 GLU B CB  1 
ATOM   3256 C  CG  . GLU B 1 164 ? 59.839 -28.201 96.882  1.00 27.85 ?  164 GLU B CG  1 
ATOM   3257 C  CD  . GLU B 1 164 ? 58.484 -28.591 97.448  1.00 30.36 ?  164 GLU B CD  1 
ATOM   3258 O  OE1 . GLU B 1 164 ? 58.191 -28.165 98.588  1.00 37.70 ?  164 GLU B OE1 1 
ATOM   3259 O  OE2 . GLU B 1 164 ? 57.719 -29.322 96.777  1.00 32.52 -1 164 GLU B OE2 1 
ATOM   3260 N  N   . LEU B 1 165 ? 59.667 -25.280 94.402  1.00 19.90 ?  165 LEU B N   1 
ATOM   3261 C  CA  . LEU B 1 165 ? 59.563 -23.840 94.630  1.00 21.23 ?  165 LEU B CA  1 
ATOM   3262 C  C   . LEU B 1 165 ? 58.183 -23.338 94.257  1.00 20.55 ?  165 LEU B C   1 
ATOM   3263 O  O   . LEU B 1 165 ? 57.591 -22.525 94.975  1.00 19.08 ?  165 LEU B O   1 
ATOM   3264 C  CB  . LEU B 1 165 ? 60.610 -23.078 93.815  1.00 21.92 ?  165 LEU B CB  1 
ATOM   3265 C  CG  . LEU B 1 165 ? 62.073 -23.211 94.232  1.00 28.50 ?  165 LEU B CG  1 
ATOM   3266 C  CD1 . LEU B 1 165 ? 62.961 -22.302 93.377  1.00 24.46 ?  165 LEU B CD1 1 
ATOM   3267 C  CD2 . LEU B 1 165 ? 62.216 -22.894 95.710  1.00 25.73 ?  165 LEU B CD2 1 
ATOM   3268 N  N   . ILE B 1 166 ? 57.671 -23.804 93.116  1.00 18.64 ?  166 ILE B N   1 
ATOM   3269 C  CA  . ILE B 1 166 ? 56.336 -23.420 92.666  1.00 17.36 ?  166 ILE B CA  1 
ATOM   3270 C  C   . ILE B 1 166 ? 55.288 -23.867 93.682  1.00 20.39 ?  166 ILE B C   1 
ATOM   3271 O  O   . ILE B 1 166 ? 54.434 -23.080 94.105  1.00 19.69 ?  166 ILE B O   1 
ATOM   3272 C  CB  . ILE B 1 166 ? 56.049 -24.013 91.272  1.00 19.61 ?  166 ILE B CB  1 
ATOM   3273 C  CG1 . ILE B 1 166 ? 56.861 -23.324 90.164  1.00 19.84 ?  166 ILE B CG1 1 
ATOM   3274 C  CG2 . ILE B 1 166 ? 54.568 -23.936 90.944  1.00 19.21 ?  166 ILE B CG2 1 
ATOM   3275 C  CD1 . ILE B 1 166 ? 56.807 -24.079 88.820  1.00 17.24 ?  166 ILE B CD1 1 
ATOM   3276 N  N   . ARG B 1 167 ? 55.329 -25.147 94.073  1.00 20.56 ?  167 ARG B N   1 
ATOM   3277 C  CA  . ARG B 1 167 ? 54.359 -25.670 95.034  1.00 22.78 ?  167 ARG B CA  1 
ATOM   3278 C  C   . ARG B 1 167 ? 54.394 -24.894 96.344  1.00 25.12 ?  167 ARG B C   1 
ATOM   3279 O  O   . ARG B 1 167 ? 53.350 -24.466 96.852  1.00 26.29 ?  167 ARG B O   1 
ATOM   3280 C  CB  . ARG B 1 167 ? 54.623 -27.157 95.291  1.00 26.33 ?  167 ARG B CB  1 
ATOM   3281 C  CG  . ARG B 1 167 ? 53.415 -27.927 95.840  1.00 28.94 ?  167 ARG B CG  1 
ATOM   3282 C  CD  . ARG B 1 167 ? 53.859 -29.197 96.562  1.00 25.21 ?  167 ARG B CD  1 
ATOM   3283 N  NE  . ARG B 1 167 ? 54.825 -28.858 97.600  1.00 30.60 ?  167 ARG B NE  1 
ATOM   3284 C  CZ  . ARG B 1 167 ? 54.502 -28.347 98.787  1.00 29.38 ?  167 ARG B CZ  1 
ATOM   3285 N  NH1 . ARG B 1 167 ? 53.227 -28.142 99.107  1.00 26.73 ?  167 ARG B NH1 1 
ATOM   3286 N  NH2 . ARG B 1 167 ? 55.457 -28.048 99.655  1.00 31.26 ?  167 ARG B NH2 1 
ATOM   3287 N  N   . LYS B 1 168 ? 55.592 -24.692 96.907  1.00 25.79 ?  168 LYS B N   1 
ATOM   3288 C  CA  . LYS B 1 168 ? 55.693 -24.054 98.219  1.00 29.39 ?  168 LYS B CA  1 
ATOM   3289 C  C   . LYS B 1 168 ? 55.279 -22.589 98.178  1.00 26.05 ?  168 LYS B C   1 
ATOM   3290 O  O   . LYS B 1 168 ? 54.751 -22.067 99.171  1.00 26.67 ?  168 LYS B O   1 
ATOM   3291 C  CB  . LYS B 1 168 ? 57.116 -24.193 98.758  1.00 30.15 ?  168 LYS B CB  1 
ATOM   3292 C  CG  . LYS B 1 168 ? 57.299 -23.647 100.168 1.00 40.31 ?  168 LYS B CG  1 
ATOM   3293 C  CD  . LYS B 1 168 ? 58.525 -24.245 100.834 1.00 38.38 ?  168 LYS B CD  1 
ATOM   3294 C  CE  . LYS B 1 168 ? 59.611 -24.569 99.817  1.00 45.94 ?  168 LYS B CE  1 
ATOM   3295 N  NZ  . LYS B 1 168 ? 60.262 -23.317 99.314  1.00 45.56 ?  168 LYS B NZ  1 
ATOM   3296 N  N   . ALA B 1 169 ? 55.489 -21.910 97.042  1.00 20.13 ?  169 ALA B N   1 
ATOM   3297 C  CA  . ALA B 1 169 ? 55.057 -20.522 96.906  1.00 24.60 ?  169 ALA B CA  1 
ATOM   3298 C  C   . ALA B 1 169 ? 53.549 -20.395 96.768  1.00 24.67 ?  169 ALA B C   1 
ATOM   3299 O  O   . ALA B 1 169 ? 53.005 -19.329 97.051  1.00 24.07 ?  169 ALA B O   1 
ATOM   3300 C  CB  . ALA B 1 169 ? 55.732 -19.866 95.696  1.00 20.58 ?  169 ALA B CB  1 
ATOM   3301 N  N   . GLY B 1 170 ? 52.861 -21.455 96.345  1.00 22.99 ?  170 GLY B N   1 
ATOM   3302 C  CA  . GLY B 1 170 ? 51.430 -21.386 96.138  1.00 22.64 ?  170 GLY B CA  1 
ATOM   3303 C  C   . GLY B 1 170 ? 51.027 -21.005 94.735  1.00 22.16 ?  170 GLY B C   1 
ATOM   3304 O  O   . GLY B 1 170 ? 49.884 -20.581 94.527  1.00 21.44 ?  170 GLY B O   1 
ATOM   3305 N  N   . VAL B 1 171 ? 51.940 -21.119 93.773  1.00 20.20 ?  171 VAL B N   1 
ATOM   3306 C  CA  . VAL B 1 171 ? 51.627 -20.862 92.370  1.00 18.18 ?  171 VAL B CA  1 
ATOM   3307 C  C   . VAL B 1 171 ? 50.889 -22.067 91.807  1.00 18.68 ?  171 VAL B C   1 
ATOM   3308 O  O   . VAL B 1 171 ? 51.402 -23.191 91.837  1.00 20.35 ?  171 VAL B O   1 
ATOM   3309 C  CB  . VAL B 1 171 ? 52.900 -20.577 91.562  1.00 16.48 ?  171 VAL B CB  1 
ATOM   3310 C  CG1 . VAL B 1 171 ? 52.538 -20.331 90.075  1.00 15.61 ?  171 VAL B CG1 1 
ATOM   3311 C  CG2 . VAL B 1 171 ? 53.629 -19.387 92.147  1.00 18.96 ?  171 VAL B CG2 1 
ATOM   3312 N  N   . ARG B 1 172 ? 49.705 -21.830 91.260  1.00 19.06 ?  172 ARG B N   1 
ATOM   3313 C  CA  . ARG B 1 172 ? 48.910 -22.897 90.674  1.00 16.54 ?  172 ARG B CA  1 
ATOM   3314 C  C   . ARG B 1 172 ? 49.443 -23.241 89.298  1.00 17.44 ?  172 ARG B C   1 
ATOM   3315 O  O   . ARG B 1 172 ? 49.935 -22.373 88.572  1.00 18.32 ?  172 ARG B O   1 
ATOM   3316 C  CB  . ARG B 1 172 ? 47.453 -22.478 90.558  1.00 21.10 ?  172 ARG B CB  1 
ATOM   3317 C  CG  . ARG B 1 172 ? 46.761 -22.325 91.887  1.00 25.83 ?  172 ARG B CG  1 
ATOM   3318 C  CD  . ARG B 1 172 ? 45.481 -21.558 91.691  1.00 26.65 ?  172 ARG B CD  1 
ATOM   3319 N  NE  . ARG B 1 172 ? 45.681 -20.113 91.767  1.00 23.99 ?  172 ARG B NE  1 
ATOM   3320 C  CZ  . ARG B 1 172 ? 44.770 -19.215 91.408  1.00 22.50 ?  172 ARG B CZ  1 
ATOM   3321 N  NH1 . ARG B 1 172 ? 43.586 -19.611 90.939  1.00 23.64 ?  172 ARG B NH1 1 
ATOM   3322 N  NH2 . ARG B 1 172 ? 45.036 -17.923 91.531  1.00 21.51 ?  172 ARG B NH2 1 
ATOM   3323 N  N   . VAL B 1 173 ? 49.353 -24.522 88.940  1.00 15.40 ?  173 VAL B N   1 
ATOM   3324 C  CA  . VAL B 1 173 ? 49.792 -24.980 87.629  1.00 17.61 ?  173 VAL B CA  1 
ATOM   3325 C  C   . VAL B 1 173 ? 48.616 -25.655 86.936  1.00 19.59 ?  173 VAL B C   1 
ATOM   3326 O  O   . VAL B 1 173 ? 48.038 -26.616 87.464  1.00 16.20 ?  173 VAL B O   1 
ATOM   3327 C  CB  . VAL B 1 173 ? 50.996 -25.928 87.728  1.00 17.02 ?  173 VAL B CB  1 
ATOM   3328 C  CG1 . VAL B 1 173 ? 51.412 -26.434 86.327  1.00 20.17 ?  173 VAL B CG1 1 
ATOM   3329 C  CG2 . VAL B 1 173 ? 52.151 -25.243 88.432  1.00 19.27 ?  173 VAL B CG2 1 
ATOM   3330 N  N   . ILE B 1 174 ? 48.254 -25.156 85.757  1.00 16.07 ?  174 ILE B N   1 
ATOM   3331 C  CA  . ILE B 1 174 ? 47.258 -25.821 84.930  1.00 16.15 ?  174 ILE B CA  1 
ATOM   3332 C  C   . ILE B 1 174 ? 47.990 -26.462 83.753  1.00 16.60 ?  174 ILE B C   1 
ATOM   3333 O  O   . ILE B 1 174 ? 48.404 -25.753 82.823  1.00 19.19 ?  174 ILE B O   1 
ATOM   3334 C  CB  . ILE B 1 174 ? 46.172 -24.853 84.434  1.00 16.57 ?  174 ILE B CB  1 
ATOM   3335 C  CG1 . ILE B 1 174 ? 45.561 -24.055 85.601  1.00 15.81 ?  174 ILE B CG1 1 
ATOM   3336 C  CG2 . ILE B 1 174 ? 45.098 -25.637 83.666  1.00 16.62 ?  174 ILE B CG2 1 
ATOM   3337 C  CD1 . ILE B 1 174 ? 44.561 -22.993 85.154  1.00 19.89 ?  174 ILE B CD1 1 
ATOM   3338 N  N   . PRO B 1 175 ? 48.175 -27.775 83.740  1.00 16.64 ?  175 PRO B N   1 
ATOM   3339 C  CA  . PRO B 1 175 ? 48.964 -28.402 82.672  1.00 18.01 ?  175 PRO B CA  1 
ATOM   3340 C  C   . PRO B 1 175 ? 48.185 -28.421 81.368  1.00 15.54 ?  175 PRO B C   1 
ATOM   3341 O  O   . PRO B 1 175 ? 46.961 -28.235 81.367  1.00 19.34 ?  175 PRO B O   1 
ATOM   3342 C  CB  . PRO B 1 175 ? 49.216 -29.824 83.209  1.00 21.40 ?  175 PRO B CB  1 
ATOM   3343 C  CG  . PRO B 1 175 ? 48.075 -30.076 84.137  1.00 23.68 ?  175 PRO B CG  1 
ATOM   3344 C  CD  . PRO B 1 175 ? 47.766 -28.743 84.776  1.00 21.37 ?  175 PRO B CD  1 
ATOM   3345 N  N   . PRO B 1 176 ? 48.855 -28.649 80.234  1.00 15.99 ?  176 PRO B N   1 
ATOM   3346 C  CA  . PRO B 1 176 ? 48.151 -28.546 78.940  1.00 17.97 ?  176 PRO B CA  1 
ATOM   3347 C  C   . PRO B 1 176 ? 46.877 -29.380 78.862  1.00 23.96 ?  176 PRO B C   1 
ATOM   3348 O  O   . PRO B 1 176 ? 45.859 -28.899 78.347  1.00 22.38 ?  176 PRO B O   1 
ATOM   3349 C  CB  . PRO B 1 176 ? 49.212 -29.021 77.934  1.00 20.11 ?  176 PRO B CB  1 
ATOM   3350 C  CG  . PRO B 1 176 ? 50.519 -28.739 78.601  1.00 19.96 ?  176 PRO B CG  1 
ATOM   3351 C  CD  . PRO B 1 176 ? 50.283 -28.978 80.071  1.00 16.92 ?  176 PRO B CD  1 
ATOM   3352 N  N   . GLY B 1 177 ? 46.893 -30.601 79.399  1.00 21.44 ?  177 GLY B N   1 
ATOM   3353 C  CA  . GLY B 1 177 ? 45.724 -31.470 79.338  1.00 24.32 ?  177 GLY B CA  1 
ATOM   3354 C  C   . GLY B 1 177 ? 44.533 -30.983 80.133  1.00 23.72 ?  177 GLY B C   1 
ATOM   3355 O  O   . GLY B 1 177 ? 43.428 -31.505 79.943  1.00 29.20 ?  177 GLY B O   1 
ATOM   3356 N  N   . GLU B 1 178 ? 44.729 -30.002 81.013  1.00 22.58 ?  178 GLU B N   1 
ATOM   3357 C  CA  . GLU B 1 178 ? 43.667 -29.404 81.807  1.00 22.19 ?  178 GLU B CA  1 
ATOM   3358 C  C   . GLU B 1 178 ? 43.392 -27.961 81.414  1.00 20.82 ?  178 GLU B C   1 
ATOM   3359 O  O   . GLU B 1 178 ? 42.491 -27.333 81.980  1.00 20.44 ?  178 GLU B O   1 
ATOM   3360 C  CB  . GLU B 1 178 ? 44.035 -29.458 83.299  1.00 29.09 ?  178 GLU B CB  1 
ATOM   3361 C  CG  . GLU B 1 178 ? 44.089 -30.869 83.901  1.00 29.07 ?  178 GLU B CG  1 
ATOM   3362 C  CD  . GLU B 1 178 ? 44.686 -30.882 85.301  1.00 40.59 ?  178 GLU B CD  1 
ATOM   3363 O  OE1 . GLU B 1 178 ? 45.467 -31.808 85.610  1.00 47.25 ?  178 GLU B OE1 1 
ATOM   3364 O  OE2 . GLU B 1 178 ? 44.399 -29.951 86.086  1.00 41.22 -1 178 GLU B OE2 1 
ATOM   3365 N  N   . ALA B 1 179 ? 44.156 -27.411 80.475  1.00 16.82 ?  179 ALA B N   1 
ATOM   3366 C  CA  . ALA B 1 179 ? 44.123 -25.970 80.219  1.00 18.03 ?  179 ALA B CA  1 
ATOM   3367 C  C   . ALA B 1 179 ? 43.031 -25.650 79.198  1.00 20.70 ?  179 ALA B C   1 
ATOM   3368 O  O   . ALA B 1 179 ? 43.281 -25.418 78.009  1.00 21.00 ?  179 ALA B O   1 
ATOM   3369 C  CB  . ALA B 1 179 ? 45.493 -25.496 79.757  1.00 20.94 ?  179 ALA B CB  1 
ATOM   3370 N  N   . THR B 1 180 ? 41.795 -25.628 79.687  1.00 19.17 ?  180 THR B N   1 
ATOM   3371 C  CA  . THR B 1 180 ? 40.635 -25.175 78.935  1.00 20.17 ?  180 THR B CA  1 
ATOM   3372 C  C   . THR B 1 180 ? 40.268 -23.752 79.331  1.00 18.90 ?  180 THR B C   1 
ATOM   3373 O  O   . THR B 1 180 ? 40.740 -23.214 80.336  1.00 16.83 ?  180 THR B O   1 
ATOM   3374 C  CB  . THR B 1 180 ? 39.434 -26.094 79.178  1.00 19.65 ?  180 THR B CB  1 
ATOM   3375 O  OG1 . THR B 1 180 ? 38.963 -25.904 80.521  1.00 17.96 ?  180 THR B OG1 1 
ATOM   3376 C  CG2 . THR B 1 180 ? 39.828 -27.560 78.966  1.00 22.49 ?  180 THR B CG2 1 
ATOM   3377 N  N   . ALA B 1 181 ? 39.402 -23.144 78.514  1.00 17.63 ?  181 ALA B N   1 
ATOM   3378 C  CA  . ALA B 1 181 ? 38.886 -21.807 78.812  1.00 17.95 ?  181 ALA B CA  1 
ATOM   3379 C  C   . ALA B 1 181 ? 38.221 -21.762 80.181  1.00 19.14 ?  181 ALA B C   1 
ATOM   3380 O  O   . ALA B 1 181 ? 38.460 -20.836 80.968  1.00 19.53 ?  181 ALA B O   1 
ATOM   3381 C  CB  . ALA B 1 181 ? 37.900 -21.374 77.722  1.00 19.45 ?  181 ALA B CB  1 
ATOM   3382 N  N   . GLN B 1 182 ? 37.383 -22.761 80.492  1.00 16.51 ?  182 GLN B N   1 
ATOM   3383 C  CA  . GLN B 1 182 ? 36.678 -22.744 81.771  1.00 20.74 ?  182 GLN B CA  1 
ATOM   3384 C  C   . GLN B 1 182 ? 37.638 -22.922 82.939  1.00 16.01 ?  182 GLN B C   1 
ATOM   3385 O  O   . GLN B 1 182 ? 37.453 -22.304 83.993  1.00 20.38 ?  182 GLN B O   1 
ATOM   3386 C  CB  . GLN B 1 182 ? 35.599 -23.825 81.813  1.00 22.11 ?  182 GLN B CB  1 
ATOM   3387 C  CG  . GLN B 1 182 ? 34.591 -23.628 82.949  1.00 24.04 ?  182 GLN B CG  1 
ATOM   3388 C  CD  . GLN B 1 182 ? 33.941 -22.241 82.949  1.00 28.90 ?  182 GLN B CD  1 
ATOM   3389 O  OE1 . GLN B 1 182 ? 33.333 -21.821 81.959  1.00 28.02 ?  182 GLN B OE1 1 
ATOM   3390 N  NE2 . GLN B 1 182 ? 34.084 -21.519 84.060  1.00 26.06 ?  182 GLN B NE2 1 
ATOM   3391 N  N   . ALA B 1 183 ? 38.663 -23.759 82.772  1.00 15.51 ?  183 ALA B N   1 
ATOM   3392 C  CA  . ALA B 1 183 ? 39.618 -23.973 83.858  1.00 15.30 ?  183 ALA B CA  1 
ATOM   3393 C  C   . ALA B 1 183 ? 40.339 -22.677 84.210  1.00 21.25 ?  183 ALA B C   1 
ATOM   3394 O  O   . ALA B 1 183 ? 40.575 -22.373 85.392  1.00 18.88 ?  183 ALA B O   1 
ATOM   3395 C  CB  . ALA B 1 183 ? 40.615 -25.059 83.461  1.00 15.10 ?  183 ALA B CB  1 
ATOM   3396 N  N   . VAL B 1 184 ? 40.697 -21.907 83.184  1.00 16.34 ?  184 VAL B N   1 
ATOM   3397 C  CA  . VAL B 1 184 ? 41.354 -20.622 83.370  1.00 16.61 ?  184 VAL B CA  1 
ATOM   3398 C  C   . VAL B 1 184 ? 40.397 -19.611 83.983  1.00 18.42 ?  184 VAL B C   1 
ATOM   3399 O  O   . VAL B 1 184 ? 40.770 -18.853 84.885  1.00 16.85 ?  184 VAL B O   1 
ATOM   3400 C  CB  . VAL B 1 184 ? 41.896 -20.136 82.016  1.00 17.31 ?  184 VAL B CB  1 
ATOM   3401 C  CG1 . VAL B 1 184 ? 42.316 -18.676 82.112  1.00 18.46 ?  184 VAL B CG1 1 
ATOM   3402 C  CG2 . VAL B 1 184 ? 43.050 -21.020 81.592  1.00 19.04 ?  184 VAL B CG2 1 
ATOM   3403 N  N   . LEU B 1 185 ? 39.161 -19.551 83.473  1.00 16.53 ?  185 LEU B N   1 
ATOM   3404 C  CA  . LEU B 1 185 ? 38.151 -18.676 84.060  1.00 17.36 ?  185 LEU B CA  1 
ATOM   3405 C  C   . LEU B 1 185 ? 37.928 -18.987 85.532  1.00 19.06 ?  185 LEU B C   1 
ATOM   3406 O  O   . LEU B 1 185 ? 37.762 -18.068 86.342  1.00 19.45 ?  185 LEU B O   1 
ATOM   3407 C  CB  . LEU B 1 185 ? 36.828 -18.799 83.290  1.00 18.73 ?  185 LEU B CB  1 
ATOM   3408 C  CG  . LEU B 1 185 ? 36.652 -17.996 82.004  1.00 23.30 ?  185 LEU B CG  1 
ATOM   3409 C  CD1 . LEU B 1 185 ? 35.241 -18.189 81.443  1.00 23.82 ?  185 LEU B CD1 1 
ATOM   3410 C  CD2 . LEU B 1 185 ? 36.957 -16.515 82.228  1.00 23.94 ?  185 LEU B CD2 1 
ATOM   3411 N  N   . ASP B 1 186 ? 37.883 -20.275 85.896  1.00 17.53 ?  186 ASP B N   1 
ATOM   3412 C  CA  . ASP B 1 186 ? 37.722 -20.631 87.304  1.00 21.03 ?  186 ASP B CA  1 
ATOM   3413 C  C   . ASP B 1 186 ? 38.895 -20.143 88.140  1.00 24.41 ?  186 ASP B C   1 
ATOM   3414 O  O   . ASP B 1 186 ? 38.719 -19.791 89.312  1.00 23.04 ?  186 ASP B O   1 
ATOM   3415 C  CB  . ASP B 1 186 ? 37.589 -22.140 87.472  1.00 23.54 ?  186 ASP B CB  1 
ATOM   3416 C  CG  . ASP B 1 186 ? 36.253 -22.671 87.000  1.00 25.67 ?  186 ASP B CG  1 
ATOM   3417 O  OD1 . ASP B 1 186 ? 35.325 -21.879 86.712  1.00 23.60 ?  186 ASP B OD1 1 
ATOM   3418 O  OD2 . ASP B 1 186 ? 36.142 -23.909 86.930  1.00 29.49 -1 186 ASP B OD2 1 
ATOM   3419 N  N   . ALA B 1 187 ? 40.092 -20.116 87.557  1.00 21.29 ?  187 ALA B N   1 
ATOM   3420 C  CA  . ALA B 1 187 ? 41.280 -19.672 88.285  1.00 16.32 ?  187 ALA B CA  1 
ATOM   3421 C  C   . ALA B 1 187 ? 41.296 -18.161 88.488  1.00 19.34 ?  187 ALA B C   1 
ATOM   3422 O  O   . ALA B 1 187 ? 41.816 -17.681 89.502  1.00 22.53 ?  187 ALA B O   1 
ATOM   3423 C  CB  . ALA B 1 187 ? 42.536 -20.116 87.540  1.00 19.76 ?  187 ALA B CB  1 
ATOM   3424 N  N   . VAL B 1 188 ? 40.737 -17.398 87.545  1.00 17.42 ?  188 VAL B N   1 
ATOM   3425 C  CA  . VAL B 1 188 ? 40.782 -15.940 87.640  1.00 16.32 ?  188 VAL B CA  1 
ATOM   3426 C  C   . VAL B 1 188 ? 39.651 -15.392 88.516  1.00 21.39 ?  188 VAL B C   1 
ATOM   3427 O  O   . VAL B 1 188 ? 39.804 -14.335 89.135  1.00 21.19 ?  188 VAL B O   1 
ATOM   3428 C  CB  . VAL B 1 188 ? 40.731 -15.328 86.230  1.00 22.81 ?  188 VAL B CB  1 
ATOM   3429 C  CG1 . VAL B 1 188 ? 40.423 -13.871 86.314  1.00 27.94 ?  188 VAL B CG1 1 
ATOM   3430 C  CG2 . VAL B 1 188 ? 42.056 -15.562 85.486  1.00 20.35 ?  188 VAL B CG2 1 
ATOM   3431 N  N   . LYS B 1 189 ? 38.506 -16.067 88.564  1.00 21.54 ?  189 LYS B N   1 
ATOM   3432 C  CA  . LYS B 1 189 ? 37.342 -15.626 89.354  1.00 23.46 ?  189 LYS B CA  1 
ATOM   3433 C  C   . LYS B 1 189 ? 36.959 -14.223 88.882  1.00 19.73 ?  189 LYS B C   1 
ATOM   3434 O  O   . LYS B 1 189 ? 36.761 -14.026 87.672  1.00 23.64 ?  189 LYS B O   1 
ATOM   3435 C  CB  . LYS B 1 189 ? 37.659 -15.765 90.846  1.00 24.55 ?  189 LYS B CB  1 
ATOM   3436 C  CG  . LYS B 1 189 ? 37.822 -17.217 91.330  1.00 29.25 ?  189 LYS B CG  1 
ATOM   3437 C  CD  . LYS B 1 189 ? 38.432 -17.278 92.745  1.00 37.36 ?  189 LYS B CD  1 
ATOM   3438 C  CE  . LYS B 1 189 ? 39.876 -17.801 92.707  1.00 36.74 ?  189 LYS B CE  1 
ATOM   3439 N  NZ  . LYS B 1 189 ? 40.682 -17.505 93.930  1.00 40.36 ?  189 LYS B NZ  1 
ATOM   3440 N  N   . ASP B 1 190 ? 36.863 -13.231 89.774  1.00 22.61 ?  190 ASP B N   1 
ATOM   3441 C  CA  . ASP B 1 190 ? 36.378 -11.893 89.455  1.00 24.70 ?  190 ASP B CA  1 
ATOM   3442 C  C   . ASP B 1 190 ? 37.502 -10.892 89.224  1.00 24.70 ?  190 ASP B C   1 
ATOM   3443 O  O   . ASP B 1 190 ? 37.227 -9.699  89.049  1.00 26.04 ?  190 ASP B O   1 
ATOM   3444 C  CB  . ASP B 1 190 ? 35.491 -11.361 90.593  1.00 31.85 ?  190 ASP B CB  1 
ATOM   3445 C  CG  . ASP B 1 190 ? 34.332 -12.276 90.918  1.00 40.02 ?  190 ASP B CG  1 
ATOM   3446 O  OD1 . ASP B 1 190 ? 33.962 -12.338 92.110  1.00 48.35 -1 190 ASP B OD1 1 
ATOM   3447 O  OD2 . ASP B 1 190 ? 33.782 -12.915 89.993  1.00 43.59 -1 190 ASP B OD2 1 
ATOM   3448 N  N   . ALA B 1 191 ? 38.745 -11.341 89.235  1.00 21.33 ?  191 ALA B N   1 
ATOM   3449 C  CA  . ALA B 1 191 ? 39.900 -10.460 89.229  1.00 20.64 ?  191 ALA B CA  1 
ATOM   3450 C  C   . ALA B 1 191 ? 40.121 -9.863  87.844  1.00 20.19 ?  191 ALA B C   1 
ATOM   3451 O  O   . ALA B 1 191 ? 39.752 -10.472 86.834  1.00 19.16 ?  191 ALA B O   1 
ATOM   3452 C  CB  . ALA B 1 191 ? 41.152 -11.232 89.651  1.00 20.08 ?  191 ALA B CB  1 
ATOM   3453 N  N   . PRO B 1 192 ? 40.720 -8.675  87.768  1.00 17.30 ?  192 PRO B N   1 
ATOM   3454 C  CA  . PRO B 1 192 ? 41.302 -8.228  86.500  1.00 16.49 ?  192 PRO B CA  1 
ATOM   3455 C  C   . PRO B 1 192 ? 42.487 -9.114  86.146  1.00 14.79 ?  192 PRO B C   1 
ATOM   3456 O  O   . PRO B 1 192 ? 43.078 -9.768  87.005  1.00 14.87 ?  192 PRO B O   1 
ATOM   3457 C  CB  . PRO B 1 192 ? 41.748 -6.797  86.789  1.00 21.71 ?  192 PRO B CB  1 
ATOM   3458 C  CG  . PRO B 1 192 ? 41.989 -6.784  88.252  1.00 24.06 ?  192 PRO B CG  1 
ATOM   3459 C  CD  . PRO B 1 192 ? 41.002 -7.737  88.868  1.00 19.82 ?  192 PRO B CD  1 
ATOM   3460 N  N   . VAL B 1 193 ? 42.817 -9.149  84.852  1.00 15.46 ?  193 VAL B N   1 
ATOM   3461 C  CA  . VAL B 1 193 ? 43.718 -10.173 84.327  1.00 13.51 ?  193 VAL B CA  1 
ATOM   3462 C  C   . VAL B 1 193 ? 44.847 -9.529  83.536  1.00 13.35 ?  193 VAL B C   1 
ATOM   3463 O  O   . VAL B 1 193 ? 44.611 -8.641  82.710  1.00 13.71 ?  193 VAL B O   1 
ATOM   3464 C  CB  . VAL B 1 193 ? 42.965 -11.169 83.418  1.00 18.12 ?  193 VAL B CB  1 
ATOM   3465 C  CG1 . VAL B 1 193 ? 43.914 -12.239 82.912  1.00 18.69 ?  193 VAL B CG1 1 
ATOM   3466 C  CG2 . VAL B 1 193 ? 41.847 -11.788 84.159  1.00 18.68 ?  193 VAL B CG2 1 
ATOM   3467 N  N   . TRP B 1 194 ? 46.063 -10.033 83.739  1.00 12.07 ?  194 TRP B N   1 
ATOM   3468 C  CA  . TRP B 1 194 ? 47.217 -9.713  82.904  1.00 13.47 ?  194 TRP B CA  1 
ATOM   3469 C  C   . TRP B 1 194 ? 47.692 -11.011 82.272  1.00 13.61 ?  194 TRP B C   1 
ATOM   3470 O  O   . TRP B 1 194 ? 47.940 -11.979 82.995  1.00 13.54 ?  194 TRP B O   1 
ATOM   3471 C  CB  . TRP B 1 194 ? 48.339 -9.091  83.742  1.00 14.88 ?  194 TRP B CB  1 
ATOM   3472 C  CG  . TRP B 1 194 ? 49.578 -8.775  82.941  1.00 13.65 ?  194 TRP B CG  1 
ATOM   3473 C  CD1 . TRP B 1 194 ? 50.643 -9.603  82.705  1.00 17.29 ?  194 TRP B CD1 1 
ATOM   3474 C  CD2 . TRP B 1 194 ? 49.876 -7.539  82.288  1.00 14.05 ?  194 TRP B CD2 1 
ATOM   3475 N  NE1 . TRP B 1 194 ? 51.593 -8.944  81.952  1.00 16.14 ?  194 TRP B NE1 1 
ATOM   3476 C  CE2 . TRP B 1 194 ? 51.139 -7.681  81.677  1.00 14.92 ?  194 TRP B CE2 1 
ATOM   3477 C  CE3 . TRP B 1 194 ? 49.194 -6.325  82.159  1.00 14.44 ?  194 TRP B CE3 1 
ATOM   3478 C  CZ2 . TRP B 1 194 ? 51.733 -6.647  80.949  1.00 17.68 ?  194 TRP B CZ2 1 
ATOM   3479 C  CZ3 . TRP B 1 194 ? 49.782 -5.306  81.432  1.00 17.48 ?  194 TRP B CZ3 1 
ATOM   3480 C  CH2 . TRP B 1 194 ? 51.035 -5.467  80.848  1.00 15.59 ?  194 TRP B CH2 1 
ATOM   3481 N  N   . ILE B 1 195 ? 47.792 -11.052 80.936  1.00 11.76 ?  195 ILE B N   1 
ATOM   3482 C  CA  . ILE B 1 195 ? 48.210 -12.267 80.230  1.00 12.66 ?  195 ILE B CA  1 
ATOM   3483 C  C   . ILE B 1 195 ? 49.651 -12.128 79.766  1.00 14.33 ?  195 ILE B C   1 
ATOM   3484 O  O   . ILE B 1 195 ? 49.990 -11.193 79.029  1.00 13.76 ?  195 ILE B O   1 
ATOM   3485 C  CB  . ILE B 1 195 ? 47.303 -12.572 79.031  1.00 11.36 ?  195 ILE B CB  1 
ATOM   3486 C  CG1 . ILE B 1 195 ? 45.890 -12.900 79.506  1.00 15.74 ?  195 ILE B CG1 1 
ATOM   3487 C  CG2 . ILE B 1 195 ? 47.871 -13.780 78.251  1.00 14.98 ?  195 ILE B CG2 1 
ATOM   3488 C  CD1 . ILE B 1 195 ? 44.902 -13.128 78.364  1.00 22.03 ?  195 ILE B CD1 1 
ATOM   3489 N  N   . HIS B 1 196 ? 50.486 -13.086 80.156  1.00 12.48 ?  196 HIS B N   1 
ATOM   3490 C  CA  . HIS B 1 196 ? 51.860 -13.186 79.685  1.00 11.82 ?  196 HIS B CA  1 
ATOM   3491 C  C   . HIS B 1 196 ? 51.959 -14.472 78.886  1.00 14.11 ?  196 HIS B C   1 
ATOM   3492 O  O   . HIS B 1 196 ? 51.655 -15.540 79.419  1.00 14.76 ?  196 HIS B O   1 
ATOM   3493 C  CB  . HIS B 1 196 ? 52.824 -13.201 80.878  1.00 14.65 ?  196 HIS B CB  1 
ATOM   3494 C  CG  . HIS B 1 196 ? 54.248 -13.473 80.513  1.00 16.60 ?  196 HIS B CG  1 
ATOM   3495 N  ND1 . HIS B 1 196 ? 55.222 -12.498 80.546  1.00 17.77 ?  196 HIS B ND1 1 
ATOM   3496 C  CD2 . HIS B 1 196 ? 54.873 -14.619 80.149  1.00 19.57 ?  196 HIS B CD2 1 
ATOM   3497 C  CE1 . HIS B 1 196 ? 56.380 -13.025 80.188  1.00 20.13 ?  196 HIS B CE1 1 
ATOM   3498 N  NE2 . HIS B 1 196 ? 56.196 -14.310 79.938  1.00 19.81 ?  196 HIS B NE2 1 
ATOM   3499 N  N   . ILE B 1 197 ? 52.344 -14.402 77.610  1.00 12.74 ?  197 ILE B N   1 
ATOM   3500 C  CA  . ILE B 1 197 ? 52.473 -15.652 76.863  1.00 13.12 ?  197 ILE B CA  1 
ATOM   3501 C  C   . ILE B 1 197 ? 53.853 -15.781 76.214  1.00 14.34 ?  197 ILE B C   1 
ATOM   3502 O  O   . ILE B 1 197 ? 54.329 -14.861 75.532  1.00 14.25 ?  197 ILE B O   1 
ATOM   3503 C  CB  . ILE B 1 197 ? 51.336 -15.826 75.832  1.00 14.49 ?  197 ILE B CB  1 
ATOM   3504 C  CG1 . ILE B 1 197 ? 51.407 -17.226 75.200  1.00 12.31 ?  197 ILE B CG1 1 
ATOM   3505 C  CG2 . ILE B 1 197 ? 51.349 -14.729 74.797  1.00 15.32 ?  197 ILE B CG2 1 
ATOM   3506 C  CD1 . ILE B 1 197 ? 50.019 -17.724 74.684  1.00 15.63 ?  197 ILE B CD1 1 
ATOM   3507 N  N   . ASP B 1 198 ? 54.496 -16.931 76.468  1.00 11.69 ?  198 ASP B N   1 
ATOM   3508 C  CA  . ASP B 1 198 ? 55.733 -17.385 75.836  1.00 12.39 ?  198 ASP B CA  1 
ATOM   3509 C  C   . ASP B 1 198 ? 55.342 -18.469 74.834  1.00 14.64 ?  198 ASP B C   1 
ATOM   3510 O  O   . ASP B 1 198 ? 54.765 -19.487 75.225  1.00 14.67 ?  198 ASP B O   1 
ATOM   3511 C  CB  . ASP B 1 198 ? 56.658 -17.939 76.929  1.00 14.09 ?  198 ASP B CB  1 
ATOM   3512 C  CG  . ASP B 1 198 ? 58.011 -18.457 76.431  1.00 15.53 ?  198 ASP B CG  1 
ATOM   3513 O  OD1 . ASP B 1 198 ? 58.205 -18.775 75.245  1.00 14.55 ?  198 ASP B OD1 1 
ATOM   3514 O  OD2 . ASP B 1 198 ? 58.917 -18.578 77.303  1.00 16.86 -1 198 ASP B OD2 1 
ATOM   3515 N  N   . TRP B 1 199 ? 55.634 -18.252 73.543  1.00 12.20 ?  199 TRP B N   1 
ATOM   3516 C  CA  . TRP B 1 199 ? 55.180 -19.209 72.531  1.00 13.43 ?  199 TRP B CA  1 
ATOM   3517 C  C   . TRP B 1 199 ? 55.738 -20.618 72.700  1.00 13.88 ?  199 TRP B C   1 
ATOM   3518 O  O   . TRP B 1 199 ? 55.233 -21.536 72.034  1.00 14.06 ?  199 TRP B O   1 
ATOM   3519 C  CB  . TRP B 1 199 ? 55.500 -18.687 71.122  1.00 15.78 ?  199 TRP B CB  1 
ATOM   3520 C  CG  . TRP B 1 199 ? 54.890 -17.336 70.914  1.00 14.00 ?  199 TRP B CG  1 
ATOM   3521 C  CD1 . TRP B 1 199 ? 55.550 -16.177 70.608  1.00 14.65 ?  199 TRP B CD1 1 
ATOM   3522 C  CD2 . TRP B 1 199 ? 53.506 -16.989 71.042  1.00 17.92 ?  199 TRP B CD2 1 
ATOM   3523 N  NE1 . TRP B 1 199 ? 54.662 -15.132 70.535  1.00 14.86 ?  199 TRP B NE1 1 
ATOM   3524 C  CE2 . TRP B 1 199 ? 53.402 -15.603 70.798  1.00 15.45 ?  199 TRP B CE2 1 
ATOM   3525 C  CE3 . TRP B 1 199 ? 52.342 -17.715 71.338  1.00 14.67 ?  199 TRP B CE3 1 
ATOM   3526 C  CZ2 . TRP B 1 199 ? 52.187 -14.929 70.834  1.00 17.14 ?  199 TRP B CZ2 1 
ATOM   3527 C  CZ3 . TRP B 1 199 ? 51.129 -17.035 71.378  1.00 17.47 ?  199 TRP B CZ3 1 
ATOM   3528 C  CH2 . TRP B 1 199 ? 51.067 -15.657 71.138  1.00 15.45 ?  199 TRP B CH2 1 
ATOM   3529 N  N   . ASP B 1 200 ? 56.732 -20.835 73.568  1.00 12.68 ?  200 ASP B N   1 
ATOM   3530 C  CA  . ASP B 1 200 ? 57.127 -22.218 73.812  1.00 15.39 ?  200 ASP B CA  1 
ATOM   3531 C  C   . ASP B 1 200 ? 56.044 -23.025 74.523  1.00 14.81 ?  200 ASP B C   1 
ATOM   3532 O  O   . ASP B 1 200 ? 56.193 -24.247 74.649  1.00 18.45 ?  200 ASP B O   1 
ATOM   3533 C  CB  . ASP B 1 200 ? 58.483 -22.289 74.565  1.00 18.31 ?  200 ASP B CB  1 
ATOM   3534 C  CG  . ASP B 1 200 ? 58.447 -21.730 76.002  1.00 18.07 ?  200 ASP B CG  1 
ATOM   3535 O  OD1 . ASP B 1 200 ? 57.422 -21.852 76.692  1.00 15.22 ?  200 ASP B OD1 1 
ATOM   3536 O  OD2 . ASP B 1 200 ? 59.501 -21.205 76.471  1.00 18.61 -1 200 ASP B OD2 1 
ATOM   3537 N  N   . VAL B 1 201 ? 54.955 -22.390 74.966  1.00 15.20 ?  201 VAL B N   1 
ATOM   3538 C  CA  . VAL B 1 201 ? 53.839 -23.134 75.540  1.00 9.97  ?  201 VAL B CA  1 
ATOM   3539 C  C   . VAL B 1 201 ? 53.176 -24.030 74.500  1.00 17.32 ?  201 VAL B C   1 
ATOM   3540 O  O   . VAL B 1 201 ? 52.577 -25.055 74.855  1.00 15.78 ?  201 VAL B O   1 
ATOM   3541 C  CB  . VAL B 1 201 ? 52.813 -22.171 76.169  1.00 13.60 ?  201 VAL B CB  1 
ATOM   3542 C  CG1 . VAL B 1 201 ? 52.049 -21.415 75.089  1.00 13.20 ?  201 VAL B CG1 1 
ATOM   3543 C  CG2 . VAL B 1 201 ? 51.837 -22.937 77.055  1.00 15.05 ?  201 VAL B CG2 1 
ATOM   3544 N  N   . LEU B 1 202 ? 53.301 -23.695 73.222  1.00 14.79 ?  202 LEU B N   1 
ATOM   3545 C  CA  . LEU B 1 202 ? 52.584 -24.419 72.178  1.00 15.63 ?  202 LEU B CA  1 
ATOM   3546 C  C   . LEU B 1 202 ? 53.225 -25.765 71.880  1.00 19.01 ?  202 LEU B C   1 
ATOM   3547 O  O   . LEU B 1 202 ? 54.438 -25.942 71.989  1.00 18.34 ?  202 LEU B O   1 
ATOM   3548 C  CB  . LEU B 1 202 ? 52.540 -23.612 70.882  1.00 16.76 ?  202 LEU B CB  1 
ATOM   3549 C  CG  . LEU B 1 202 ? 51.618 -22.398 70.838  1.00 22.56 ?  202 LEU B CG  1 
ATOM   3550 C  CD1 . LEU B 1 202 ? 51.750 -21.750 69.458  1.00 22.11 ?  202 LEU B CD1 1 
ATOM   3551 C  CD2 . LEU B 1 202 ? 50.187 -22.794 71.104  1.00 20.91 ?  202 LEU B CD2 1 
ATOM   3552 N  N   . GLU B 1 203 ? 52.379 -26.718 71.510  1.00 17.53 ?  203 GLU B N   1 
ATOM   3553 C  CA  . GLU B 1 203 ? 52.836 -27.914 70.822  1.00 22.08 ?  203 GLU B CA  1 
ATOM   3554 C  C   . GLU B 1 203 ? 53.763 -27.514 69.670  1.00 25.91 ?  203 GLU B C   1 
ATOM   3555 O  O   . GLU B 1 203 ? 53.405 -26.635 68.870  1.00 23.62 ?  203 GLU B O   1 
ATOM   3556 C  CB  . GLU B 1 203 ? 51.618 -28.683 70.300  1.00 24.96 ?  203 GLU B CB  1 
ATOM   3557 C  CG  . GLU B 1 203 ? 51.927 -29.912 69.450  1.00 29.42 ?  203 GLU B CG  1 
ATOM   3558 C  CD  . GLU B 1 203 ? 52.266 -31.133 70.280  1.00 37.83 ?  203 GLU B CD  1 
ATOM   3559 O  OE1 . GLU B 1 203 ? 52.450 -30.996 71.506  1.00 32.16 ?  203 GLU B OE1 1 
ATOM   3560 O  OE2 . GLU B 1 203 ? 52.354 -32.238 69.699  1.00 44.11 -1 203 GLU B OE2 1 
ATOM   3561 N  N   . PRO B 1 204 ? 54.962 -28.086 69.580  1.00 27.02 ?  204 PRO B N   1 
ATOM   3562 C  CA  . PRO B 1 204 ? 55.897 -27.653 68.535  1.00 29.68 ?  204 PRO B CA  1 
ATOM   3563 C  C   . PRO B 1 204 ? 55.304 -27.840 67.147  1.00 32.15 ?  204 PRO B C   1 
ATOM   3564 O  O   . PRO B 1 204 ? 54.555 -28.786 66.891  1.00 29.80 ?  204 PRO B O   1 
ATOM   3565 C  CB  . PRO B 1 204 ? 57.118 -28.550 68.763  1.00 32.78 ?  204 PRO B CB  1 
ATOM   3566 C  CG  . PRO B 1 204 ? 57.061 -28.880 70.226  1.00 30.44 ?  204 PRO B CG  1 
ATOM   3567 C  CD  . PRO B 1 204 ? 55.592 -29.024 70.532  1.00 29.21 ?  204 PRO B CD  1 
ATOM   3568 N  N   . GLY B 1 205 ? 55.603 -26.892 66.259  1.00 30.12 ?  205 GLY B N   1 
ATOM   3569 C  CA  . GLY B 1 205 ? 55.143 -27.006 64.888  1.00 28.65 ?  205 GLY B CA  1 
ATOM   3570 C  C   . GLY B 1 205 ? 54.364 -25.816 64.362  1.00 36.31 ?  205 GLY B C   1 
ATOM   3571 O  O   . GLY B 1 205 ? 54.106 -25.735 63.155  1.00 32.16 ?  205 GLY B O   1 
ATOM   3572 N  N   . SER B 1 206 ? 53.972 -24.889 65.241  1.00 28.19 ?  206 SER B N   1 
ATOM   3573 C  CA  . SER B 1 206 ? 53.246 -23.693 64.822  1.00 25.26 ?  206 SER B CA  1 
ATOM   3574 C  C   . SER B 1 206 ? 54.063 -22.411 64.912  1.00 26.31 ?  206 SER B C   1 
ATOM   3575 O  O   . SER B 1 206 ? 53.958 -21.569 64.018  1.00 26.19 ?  206 SER B O   1 
ATOM   3576 C  CB  . SER B 1 206 ? 51.952 -23.514 65.636  1.00 29.93 ?  206 SER B CB  1 
ATOM   3577 O  OG  . SER B 1 206 ? 51.124 -24.668 65.628  1.00 30.85 ?  206 SER B OG  1 
ATOM   3578 N  N   . ILE B 1 207 ? 54.878 -22.228 65.958  1.00 24.18 ?  207 ILE B N   1 
ATOM   3579 C  CA  . ILE B 1 207 ? 55.625 -20.997 66.166  1.00 20.77 ?  207 ILE B CA  1 
ATOM   3580 C  C   . ILE B 1 207 ? 57.066 -21.339 66.515  1.00 23.12 ?  207 ILE B C   1 
ATOM   3581 O  O   . ILE B 1 207 ? 57.314 -22.064 67.480  1.00 27.21 ?  207 ILE B O   1 
ATOM   3582 C  CB  . ILE B 1 207 ? 55.008 -20.118 67.274  1.00 17.84 ?  207 ILE B CB  1 
ATOM   3583 C  CG1 . ILE B 1 207 ? 53.601 -19.673 66.867  1.00 23.17 ?  207 ILE B CG1 1 
ATOM   3584 C  CG2 . ILE B 1 207 ? 55.898 -18.910 67.578  1.00 18.63 ?  207 ILE B CG2 1 
ATOM   3585 C  CD1 . ILE B 1 207 ? 52.882 -18.900 67.946  1.00 21.58 ?  207 ILE B CD1 1 
ATOM   3586 N  N   . PRO B 1 208 ? 58.054 -20.870 65.748  1.00 21.63 ?  208 PRO B N   1 
ATOM   3587 C  CA  . PRO B 1 208 ? 59.456 -21.164 66.083  1.00 23.14 ?  208 PRO B CA  1 
ATOM   3588 C  C   . PRO B 1 208 ? 59.881 -20.463 67.366  1.00 25.39 ?  208 PRO B C   1 
ATOM   3589 O  O   . PRO B 1 208 ? 59.780 -19.243 67.493  1.00 22.95 ?  208 PRO B O   1 
ATOM   3590 C  CB  . PRO B 1 208 ? 60.237 -20.634 64.872  1.00 21.99 ?  208 PRO B CB  1 
ATOM   3591 C  CG  . PRO B 1 208 ? 59.205 -20.491 63.750  1.00 25.92 ?  208 PRO B CG  1 
ATOM   3592 C  CD  . PRO B 1 208 ? 57.914 -20.177 64.453  1.00 23.60 ?  208 PRO B CD  1 
ATOM   3593 N  N   . ALA B 1 209 ? 60.388 -21.245 68.310  1.00 26.06 ?  209 ALA B N   1 
ATOM   3594 C  CA  . ALA B 1 209 ? 60.847 -20.705 69.578  1.00 30.86 ?  209 ALA B CA  1 
ATOM   3595 C  C   . ALA B 1 209 ? 61.970 -21.592 70.088  1.00 32.33 ?  209 ALA B C   1 
ATOM   3596 O  O   . ALA B 1 209 ? 62.083 -22.758 69.701  1.00 35.24 ?  209 ALA B O   1 
ATOM   3597 C  CB  . ALA B 1 209 ? 59.704 -20.625 70.601  1.00 26.32 ?  209 ALA B CB  1 
ATOM   3598 N  N   . ASP B 1 210 ? 62.816 -21.026 70.946  1.00 31.92 ?  210 ASP B N   1 
ATOM   3599 C  CA  . ASP B 1 210 ? 63.821 -21.849 71.603  1.00 33.16 ?  210 ASP B CA  1 
ATOM   3600 C  C   . ASP B 1 210 ? 63.218 -22.508 72.842  1.00 31.79 ?  210 ASP B C   1 
ATOM   3601 O  O   . ASP B 1 210 ? 62.167 -22.101 73.343  1.00 30.52 ?  210 ASP B O   1 
ATOM   3602 C  CB  . ASP B 1 210 ? 65.062 -21.020 71.964  1.00 33.73 ?  210 ASP B CB  1 
ATOM   3603 C  CG  . ASP B 1 210 ? 64.763 -19.898 72.964  1.00 42.47 ?  210 ASP B CG  1 
ATOM   3604 O  OD1 . ASP B 1 210 ? 63.584 -19.482 73.062  1.00 41.25 ?  210 ASP B OD1 1 
ATOM   3605 O  OD2 . ASP B 1 210 ? 65.713 -19.426 73.643  1.00 41.68 -1 210 ASP B OD2 1 
ATOM   3606 N  N   . TYR B 1 211 ? 63.883 -23.563 73.318  1.00 35.92 ?  211 TYR B N   1 
ATOM   3607 C  CA  . TYR B 1 211 ? 63.421 -24.307 74.493  1.00 33.45 ?  211 TYR B CA  1 
ATOM   3608 C  C   . TYR B 1 211 ? 62.036 -24.924 74.268  1.00 33.07 ?  211 TYR B C   1 
ATOM   3609 O  O   . TYR B 1 211 ? 61.166 -24.866 75.143  1.00 30.24 ?  211 TYR B O   1 
ATOM   3610 C  CB  . TYR B 1 211 ? 63.409 -23.418 75.741  1.00 32.20 ?  211 TYR B CB  1 
ATOM   3611 C  CG  . TYR B 1 211 ? 64.753 -22.882 76.172  1.00 37.99 ?  211 TYR B CG  1 
ATOM   3612 C  CD1 . TYR B 1 211 ? 65.661 -23.693 76.841  1.00 41.86 ?  211 TYR B CD1 1 
ATOM   3613 C  CD2 . TYR B 1 211 ? 65.106 -21.556 75.939  1.00 38.04 ?  211 TYR B CD2 1 
ATOM   3614 C  CE1 . TYR B 1 211 ? 66.892 -23.206 77.254  1.00 44.81 ?  211 TYR B CE1 1 
ATOM   3615 C  CE2 . TYR B 1 211 ? 66.338 -21.059 76.344  1.00 36.64 ?  211 TYR B CE2 1 
ATOM   3616 C  CZ  . TYR B 1 211 ? 67.225 -21.890 77.003  1.00 43.96 ?  211 TYR B CZ  1 
ATOM   3617 O  OH  . TYR B 1 211 ? 68.451 -21.416 77.418  1.00 45.37 ?  211 TYR B OH  1 
ATOM   3618 N  N   . THR B 1 212 ? 61.817 -25.503 73.083  1.00 34.39 ?  212 THR B N   1 
ATOM   3619 C  CA  . THR B 1 212 ? 60.570 -26.217 72.820  1.00 25.69 ?  212 THR B CA  1 
ATOM   3620 C  C   . THR B 1 212 ? 60.465 -27.425 73.750  1.00 31.27 ?  212 THR B C   1 
ATOM   3621 O  O   . THR B 1 212 ? 61.477 -27.965 74.209  1.00 35.01 ?  212 THR B O   1 
ATOM   3622 C  CB  . THR B 1 212 ? 60.496 -26.669 71.354  1.00 33.92 ?  212 THR B CB  1 
ATOM   3623 O  OG1 . THR B 1 212 ? 61.463 -27.697 71.115  1.00 41.77 ?  212 THR B OG1 1 
ATOM   3624 C  CG2 . THR B 1 212 ? 60.779 -25.514 70.415  1.00 36.53 ?  212 THR B CG2 1 
ATOM   3625 N  N   . VAL B 1 213 ? 59.230 -27.829 74.054  1.00 28.03 ?  213 VAL B N   1 
ATOM   3626 C  CA  . VAL B 1 213 ? 58.958 -29.001 74.897  1.00 28.65 ?  213 VAL B CA  1 
ATOM   3627 C  C   . VAL B 1 213 ? 57.749 -29.739 74.328  1.00 27.54 ?  213 VAL B C   1 
ATOM   3628 O  O   . VAL B 1 213 ? 56.725 -29.107 74.024  1.00 27.20 ?  213 VAL B O   1 
ATOM   3629 C  CB  . VAL B 1 213 ? 58.715 -28.609 76.369  1.00 29.17 ?  213 VAL B CB  1 
ATOM   3630 C  CG1 . VAL B 1 213 ? 58.352 -29.829 77.208  1.00 30.77 ?  213 VAL B CG1 1 
ATOM   3631 C  CG2 . VAL B 1 213 ? 59.931 -27.929 76.972  1.00 33.32 ?  213 VAL B CG2 1 
ATOM   3632 N  N   . PRO B 1 214 ? 57.809 -31.060 74.185  1.00 29.08 ?  214 PRO B N   1 
ATOM   3633 C  CA  . PRO B 1 214 ? 56.688 -31.797 73.588  1.00 31.19 ?  214 PRO B CA  1 
ATOM   3634 C  C   . PRO B 1 214 ? 55.440 -31.775 74.462  1.00 27.11 ?  214 PRO B C   1 
ATOM   3635 O  O   . PRO B 1 214 ? 55.485 -31.493 75.663  1.00 25.57 ?  214 PRO B O   1 
ATOM   3636 C  CB  . PRO B 1 214 ? 57.226 -33.229 73.459  1.00 31.42 ?  214 PRO B CB  1 
ATOM   3637 C  CG  . PRO B 1 214 ? 58.707 -33.114 73.628  1.00 32.21 ?  214 PRO B CG  1 
ATOM   3638 C  CD  . PRO B 1 214 ? 58.936 -31.946 74.522  1.00 35.06 ?  214 PRO B CD  1 
ATOM   3639 N  N   . ASP B 1 215 ? 54.312 -32.091 73.816  1.00 24.20 ?  215 ASP B N   1 
ATOM   3640 C  CA  . ASP B 1 215 ? 53.003 -32.260 74.458  1.00 26.28 ?  215 ASP B CA  1 
ATOM   3641 C  C   . ASP B 1 215 ? 52.494 -30.941 75.047  1.00 25.22 ?  215 ASP B C   1 
ATOM   3642 O  O   . ASP B 1 215 ? 52.144 -30.844 76.222  1.00 23.95 ?  215 ASP B O   1 
ATOM   3643 C  CB  . ASP B 1 215 ? 53.047 -33.359 75.526  1.00 29.42 ?  215 ASP B CB  1 
ATOM   3644 C  CG  . ASP B 1 215 ? 53.464 -34.703 74.960  1.00 38.24 ?  215 ASP B CG  1 
ATOM   3645 O  OD1 . ASP B 1 215 ? 53.025 -35.033 73.836  1.00 39.20 -1 215 ASP B OD1 1 
ATOM   3646 O  OD2 . ASP B 1 215 ? 54.222 -35.426 75.643  1.00 39.17 -1 215 ASP B OD2 1 
ATOM   3647 N  N   . GLY B 1 216 ? 52.411 -29.930 74.182  1.00 24.43 ?  216 GLY B N   1 
ATOM   3648 C  CA  . GLY B 1 216 ? 52.070 -28.587 74.595  1.00 22.12 ?  216 GLY B CA  1 
ATOM   3649 C  C   . GLY B 1 216 ? 50.619 -28.228 74.325  1.00 21.07 ?  216 GLY B C   1 
ATOM   3650 O  O   . GLY B 1 216 ? 49.784 -29.071 73.991  1.00 20.97 ?  216 GLY B O   1 
ATOM   3651 N  N   . MET B 1 217 ? 50.325 -26.936 74.477  1.00 17.60 ?  217 MET B N   1 
ATOM   3652 C  CA  . MET B 1 217 ? 48.988 -26.437 74.193  1.00 16.95 ?  217 MET B CA  1 
ATOM   3653 C  C   . MET B 1 217 ? 48.803 -26.235 72.695  1.00 14.59 ?  217 MET B C   1 
ATOM   3654 O  O   . MET B 1 217 ? 49.755 -25.979 71.955  1.00 17.99 ?  217 MET B O   1 
ATOM   3655 C  CB  . MET B 1 217 ? 48.731 -25.115 74.922  1.00 17.49 ?  217 MET B CB  1 
ATOM   3656 C  CG  . MET B 1 217 ? 48.503 -25.262 76.420  1.00 15.56 ?  217 MET B CG  1 
ATOM   3657 S  SD  . MET B 1 217 ? 48.172 -23.701 77.264  1.00 19.15 ?  217 MET B SD  1 
ATOM   3658 C  CE  . MET B 1 217 ? 46.408 -23.426 76.958  1.00 22.36 ?  217 MET B CE  1 
ATOM   3659 N  N   . LEU B 1 218 ? 47.567 -26.343 72.257  1.00 17.16 ?  218 LEU B N   1 
ATOM   3660 C  CA  . LEU B 1 218 ? 47.256 -26.160 70.848  1.00 16.10 ?  218 LEU B CA  1 
ATOM   3661 C  C   . LEU B 1 218 ? 46.691 -24.773 70.613  1.00 16.16 ?  218 LEU B C   1 
ATOM   3662 O  O   . LEU B 1 218 ? 46.125 -24.163 71.525  1.00 15.89 ?  218 LEU B O   1 
ATOM   3663 C  CB  . LEU B 1 218 ? 46.247 -27.224 70.397  1.00 18.57 ?  218 LEU B CB  1 
ATOM   3664 C  CG  . LEU B 1 218 ? 46.862 -28.623 70.354  1.00 23.97 ?  218 LEU B CG  1 
ATOM   3665 C  CD1 . LEU B 1 218 ? 45.818 -29.714 70.581  1.00 32.54 ?  218 LEU B CD1 1 
ATOM   3666 C  CD2 . LEU B 1 218 ? 47.595 -28.809 69.046  1.00 26.18 ?  218 LEU B CD2 1 
ATOM   3667 N  N   . PRO B 1 219 ? 46.804 -24.245 69.384  1.00 15.83 ?  219 PRO B N   1 
ATOM   3668 C  CA  . PRO B 1 219 ? 46.320 -22.877 69.143  1.00 19.24 ?  219 PRO B CA  1 
ATOM   3669 C  C   . PRO B 1 219 ? 44.855 -22.689 69.482  1.00 20.11 ?  219 PRO B C   1 
ATOM   3670 O  O   . PRO B 1 219 ? 44.481 -21.619 69.985  1.00 16.26 ?  219 PRO B O   1 
ATOM   3671 C  CB  . PRO B 1 219 ? 46.618 -22.667 67.648  1.00 17.98 ?  219 PRO B CB  1 
ATOM   3672 C  CG  . PRO B 1 219 ? 47.854 -23.479 67.420  1.00 17.13 ?  219 PRO B CG  1 
ATOM   3673 C  CD  . PRO B 1 219 ? 47.608 -24.744 68.255  1.00 15.08 ?  219 PRO B CD  1 
ATOM   3674 N  N   . ALA B 1 220 ? 44.014 -23.710 69.260  1.00 19.06 ?  220 ALA B N   1 
ATOM   3675 C  CA  . ALA B 1 220 ? 42.587 -23.555 69.544  1.00 16.68 ?  220 ALA B CA  1 
ATOM   3676 C  C   . ALA B 1 220 ? 42.342 -23.278 71.020  1.00 17.73 ?  220 ALA B C   1 
ATOM   3677 O  O   . ALA B 1 220 ? 41.434 -22.515 71.374  1.00 18.72 ?  220 ALA B O   1 
ATOM   3678 C  CB  . ALA B 1 220 ? 41.812 -24.801 69.103  1.00 19.36 ?  220 ALA B CB  1 
ATOM   3679 N  N   . GLN B 1 221 ? 43.143 -23.895 71.900  1.00 16.36 ?  221 GLN B N   1 
ATOM   3680 C  CA  . GLN B 1 221 ? 42.962 -23.684 73.330  1.00 16.61 ?  221 GLN B CA  1 
ATOM   3681 C  C   . GLN B 1 221 ? 43.453 -22.312 73.757  1.00 17.95 ?  221 GLN B C   1 
ATOM   3682 O  O   . GLN B 1 221 ? 42.852 -21.691 74.637  1.00 15.87 ?  221 GLN B O   1 
ATOM   3683 C  CB  . GLN B 1 221 ? 43.674 -24.772 74.127  1.00 19.41 ?  221 GLN B CB  1 
ATOM   3684 C  CG  . GLN B 1 221 ? 42.756 -25.956 74.436  1.00 27.55 ?  221 GLN B CG  1 
ATOM   3685 C  CD  . GLN B 1 221 ? 42.374 -26.705 73.179  1.00 28.67 ?  221 GLN B CD  1 
ATOM   3686 O  OE1 . GLN B 1 221 ? 43.234 -27.293 72.523  1.00 29.46 ?  221 GLN B OE1 1 
ATOM   3687 N  NE2 . GLN B 1 221 ? 41.075 -26.685 72.825  1.00 29.56 ?  221 GLN B NE2 1 
ATOM   3688 N  N   . ILE B 1 222 ? 44.558 -21.840 73.175  1.00 15.30 ?  222 ILE B N   1 
ATOM   3689 C  CA  . ILE B 1 222 ? 45.047 -20.501 73.503  1.00 14.75 ?  222 ILE B CA  1 
ATOM   3690 C  C   . ILE B 1 222 ? 44.032 -19.459 73.052  1.00 16.89 ?  222 ILE B C   1 
ATOM   3691 O  O   . ILE B 1 222 ? 43.663 -18.550 73.808  1.00 15.77 ?  222 ILE B O   1 
ATOM   3692 C  CB  . ILE B 1 222 ? 46.432 -20.259 72.871  1.00 14.32 ?  222 ILE B CB  1 
ATOM   3693 C  CG1 . ILE B 1 222 ? 47.475 -21.237 73.438  1.00 18.70 ?  222 ILE B CG1 1 
ATOM   3694 C  CG2 . ILE B 1 222 ? 46.861 -18.804 73.051  1.00 16.75 ?  222 ILE B CG2 1 
ATOM   3695 C  CD1 . ILE B 1 222 ? 47.914 -20.902 74.861  1.00 20.99 ?  222 ILE B CD1 1 
ATOM   3696 N  N   . ARG B 1 223 ? 43.536 -19.599 71.813  1.00 16.03 ?  223 ARG B N   1 
ATOM   3697 C  CA  . ARG B 1 223 ? 42.513 -18.685 71.320  1.00 15.42 ?  223 ARG B CA  1 
ATOM   3698 C  C   . ARG B 1 223 ? 41.282 -18.685 72.216  1.00 15.97 ?  223 ARG B C   1 
ATOM   3699 O  O   . ARG B 1 223 ? 40.687 -17.631 72.462  1.00 17.10 ?  223 ARG B O   1 
ATOM   3700 C  CB  . ARG B 1 223 ? 42.105 -19.046 69.892  1.00 16.22 ?  223 ARG B CB  1 
ATOM   3701 C  CG  . ARG B 1 223 ? 41.233 -17.958 69.265  1.00 19.35 ?  223 ARG B CG  1 
ATOM   3702 C  CD  . ARG B 1 223 ? 40.740 -18.341 67.858  1.00 19.20 ?  223 ARG B CD  1 
ATOM   3703 N  NE  . ARG B 1 223 ? 39.488 -17.648 67.556  1.00 26.83 ?  223 ARG B NE  1 
ATOM   3704 C  CZ  . ARG B 1 223 ? 39.404 -16.494 66.898  1.00 26.70 ?  223 ARG B CZ  1 
ATOM   3705 N  NH1 . ARG B 1 223 ? 40.493 -15.894 66.454  1.00 29.77 ?  223 ARG B NH1 1 
ATOM   3706 N  NH2 . ARG B 1 223 ? 38.224 -15.939 66.682  1.00 30.37 ?  223 ARG B NH2 1 
ATOM   3707 N  N   . ALA B 1 224 ? 40.884 -19.861 72.721  1.00 16.46 ?  224 ALA B N   1 
ATOM   3708 C  CA  . ALA B 1 224 ? 39.714 -19.915 73.598  1.00 16.82 ?  224 ALA B CA  1 
ATOM   3709 C  C   . ALA B 1 224 ? 39.934 -19.151 74.900  1.00 17.01 ?  224 ALA B C   1 
ATOM   3710 O  O   . ALA B 1 224 ? 38.984 -18.582 75.449  1.00 17.24 ?  224 ALA B O   1 
ATOM   3711 C  CB  . ALA B 1 224 ? 39.342 -21.373 73.891  1.00 21.25 ?  224 ALA B CB  1 
ATOM   3712 N  N   . VAL B 1 225 ? 41.164 -19.133 75.415  1.00 19.24 ?  225 VAL B N   1 
ATOM   3713 C  CA  . VAL B 1 225 ? 41.456 -18.327 76.604  1.00 16.93 ?  225 VAL B CA  1 
ATOM   3714 C  C   . VAL B 1 225 ? 41.269 -16.844 76.303  1.00 18.37 ?  225 VAL B C   1 
ATOM   3715 O  O   . VAL B 1 225 ? 40.612 -16.112 77.056  1.00 19.71 ?  225 VAL B O   1 
ATOM   3716 C  CB  . VAL B 1 225 ? 42.877 -18.626 77.116  1.00 17.90 ?  225 VAL B CB  1 
ATOM   3717 C  CG1 . VAL B 1 225 ? 43.302 -17.597 78.177  1.00 20.34 ?  225 VAL B CG1 1 
ATOM   3718 C  CG2 . VAL B 1 225 ? 42.952 -20.048 77.665  1.00 21.52 ?  225 VAL B CG2 1 
ATOM   3719 N  N   . PHE B 1 226 ? 41.835 -16.371 75.192  1.00 16.14 ?  226 PHE B N   1 
ATOM   3720 C  CA  . PHE B 1 226 ? 41.664 -14.961 74.848  1.00 19.40 ?  226 PHE B CA  1 
ATOM   3721 C  C   . PHE B 1 226 ? 40.195 -14.619 74.600  1.00 20.94 ?  226 PHE B C   1 
ATOM   3722 O  O   . PHE B 1 226 ? 39.745 -13.516 74.934  1.00 22.07 ?  226 PHE B O   1 
ATOM   3723 C  CB  . PHE B 1 226 ? 42.514 -14.612 73.622  1.00 19.79 ?  226 PHE B CB  1 
ATOM   3724 C  CG  . PHE B 1 226 ? 43.966 -14.393 73.938  1.00 16.97 ?  226 PHE B CG  1 
ATOM   3725 C  CD1 . PHE B 1 226 ? 44.396 -13.164 74.426  1.00 21.87 ?  226 PHE B CD1 1 
ATOM   3726 C  CD2 . PHE B 1 226 ? 44.899 -15.405 73.768  1.00 17.73 ?  226 PHE B CD2 1 
ATOM   3727 C  CE1 . PHE B 1 226 ? 45.724 -12.949 74.727  1.00 19.12 ?  226 PHE B CE1 1 
ATOM   3728 C  CE2 . PHE B 1 226 ? 46.240 -15.194 74.077  1.00 19.14 ?  226 PHE B CE2 1 
ATOM   3729 C  CZ  . PHE B 1 226 ? 46.646 -13.949 74.560  1.00 20.12 ?  226 PHE B CZ  1 
ATOM   3730 N  N   . GLU B 1 227 ? 39.431 -15.560 74.043  1.00 18.57 ?  227 GLU B N   1 
ATOM   3731 C  CA  . GLU B 1 227 ? 37.998 -15.363 73.862  1.00 19.37 ?  227 GLU B CA  1 
ATOM   3732 C  C   . GLU B 1 227 ? 37.258 -15.309 75.194  1.00 22.62 ?  227 GLU B C   1 
ATOM   3733 O  O   . GLU B 1 227 ? 36.270 -14.574 75.325  1.00 24.33 ?  227 GLU B O   1 
ATOM   3734 C  CB  . GLU B 1 227 ? 37.430 -16.479 72.985  1.00 23.33 ?  227 GLU B CB  1 
ATOM   3735 C  CG  . GLU B 1 227 ? 35.973 -16.298 72.649  1.00 27.34 ?  227 GLU B CG  1 
ATOM   3736 C  CD  . GLU B 1 227 ? 35.775 -15.404 71.442  1.00 33.76 ?  227 GLU B CD  1 
ATOM   3737 O  OE1 . GLU B 1 227 ? 35.666 -15.947 70.316  1.00 43.13 ?  227 GLU B OE1 1 
ATOM   3738 O  OE2 . GLU B 1 227 ? 35.747 -14.168 71.618  1.00 38.54 -1 227 GLU B OE2 1 
ATOM   3739 N  N   . ALA B 1 228 ? 37.738 -16.042 76.199  1.00 18.65 ?  228 ALA B N   1 
ATOM   3740 C  CA  . ALA B 1 228 ? 37.006 -16.187 77.454  1.00 20.43 ?  228 ALA B CA  1 
ATOM   3741 C  C   . ALA B 1 228 ? 37.216 -15.016 78.405  1.00 23.50 ?  228 ALA B C   1 
ATOM   3742 O  O   . ALA B 1 228 ? 36.313 -14.698 79.189  1.00 21.58 ?  228 ALA B O   1 
ATOM   3743 C  CB  . ALA B 1 228 ? 37.414 -17.490 78.146  1.00 20.36 ?  228 ALA B CB  1 
ATOM   3744 N  N   . ILE B 1 229 ? 38.386 -14.386 78.393  1.00 23.14 ?  229 ILE B N   1 
ATOM   3745 C  CA  . ILE B 1 229 ? 38.619 -13.317 79.371  1.00 20.87 ?  229 ILE B CA  1 
ATOM   3746 C  C   . ILE B 1 229 ? 37.762 -12.103 79.016  1.00 24.15 ?  229 ILE B C   1 
ATOM   3747 O  O   . ILE B 1 229 ? 37.846 -11.596 77.884  1.00 24.34 ?  229 ILE B O   1 
ATOM   3748 C  CB  . ILE B 1 229 ? 40.102 -12.942 79.424  1.00 20.11 ?  229 ILE B CB  1 
ATOM   3749 C  CG1 . ILE B 1 229 ? 40.959 -14.170 79.747  1.00 22.32 ?  229 ILE B CG1 1 
ATOM   3750 C  CG2 . ILE B 1 229 ? 40.315 -11.810 80.455  1.00 21.82 ?  229 ILE B CG2 1 
ATOM   3751 C  CD1 . ILE B 1 229 ? 40.732 -14.738 81.139  1.00 20.47 ?  229 ILE B CD1 1 
ATOM   3752 N  N   . PRO B 1 230 ? 36.956 -11.586 79.946  1.00 23.82 ?  230 PRO B N   1 
ATOM   3753 C  CA  . PRO B 1 230 ? 36.118 -10.426 79.630  1.00 23.32 ?  230 PRO B CA  1 
ATOM   3754 C  C   . PRO B 1 230 ? 36.960 -9.196  79.313  1.00 24.79 ?  230 PRO B C   1 
ATOM   3755 O  O   . PRO B 1 230 ? 37.951 -8.906  79.986  1.00 20.30 ?  230 PRO B O   1 
ATOM   3756 C  CB  . PRO B 1 230 ? 35.288 -10.225 80.907  1.00 26.22 ?  230 PRO B CB  1 
ATOM   3757 C  CG  . PRO B 1 230 ? 35.320 -11.526 81.609  1.00 25.14 ?  230 PRO B CG  1 
ATOM   3758 C  CD  . PRO B 1 230 ? 36.673 -12.124 81.287  1.00 24.41 ?  230 PRO B CD  1 
ATOM   3759 N  N   . ALA B 1 231 ? 36.547 -8.467  78.272  1.00 27.01 ?  231 ALA B N   1 
ATOM   3760 C  CA  . ALA B 1 231 ? 37.326 -7.320  77.809  1.00 29.16 ?  231 ALA B CA  1 
ATOM   3761 C  C   . ALA B 1 231 ? 37.495 -6.274  78.902  1.00 25.26 ?  231 ALA B C   1 
ATOM   3762 O  O   . ALA B 1 231 ? 38.540 -5.613  78.985  1.00 23.85 ?  231 ALA B O   1 
ATOM   3763 C  CB  . ALA B 1 231 ? 36.666 -6.695  76.578  1.00 28.51 ?  231 ALA B CB  1 
ATOM   3764 N  N   . GLU B 1 232 ? 36.477 -6.089  79.743  1.00 25.98 ?  232 GLU B N   1 
ATOM   3765 C  CA  . GLU B 1 232 ? 36.591 -5.052  80.760  1.00 27.12 ?  232 GLU B CA  1 
ATOM   3766 C  C   . GLU B 1 232 ? 37.527 -5.475  81.875  1.00 28.06 ?  232 GLU B C   1 
ATOM   3767 O  O   . GLU B 1 232 ? 37.928 -4.632  82.679  1.00 27.98 ?  232 GLU B O   1 
ATOM   3768 C  CB  . GLU B 1 232 ? 35.230 -4.710  81.369  1.00 32.53 ?  232 GLU B CB  1 
ATOM   3769 C  CG  . GLU B 1 232 ? 34.076 -4.647  80.381  1.00 41.34 ?  232 GLU B CG  1 
ATOM   3770 C  CD  . GLU B 1 232 ? 33.603 -6.034  79.983  1.00 43.22 ?  232 GLU B CD  1 
ATOM   3771 O  OE1 . GLU B 1 232 ? 32.899 -6.679  80.788  1.00 53.45 ?  232 GLU B OE1 1 
ATOM   3772 O  OE2 . GLU B 1 232 ? 33.921 -6.476  78.858  1.00 48.51 -1 232 GLU B OE2 1 
ATOM   3773 N  N   . ARG B 1 233 ? 37.873 -6.760  81.943  1.00 22.30 ?  233 ARG B N   1 
ATOM   3774 C  CA  . ARG B 1 233 ? 38.786 -7.253  82.968  1.00 18.43 ?  233 ARG B CA  1 
ATOM   3775 C  C   . ARG B 1 233 ? 40.229 -7.342  82.493  1.00 17.39 ?  233 ARG B C   1 
ATOM   3776 O  O   . ARG B 1 233 ? 41.115 -7.517  83.334  1.00 16.91 ?  233 ARG B O   1 
ATOM   3777 C  CB  . ARG B 1 233 ? 38.357 -8.636  83.462  1.00 21.84 ?  233 ARG B CB  1 
ATOM   3778 C  CG  . ARG B 1 233 ? 36.904 -8.733  83.854  1.00 27.87 ?  233 ARG B CG  1 
ATOM   3779 C  CD  . ARG B 1 233 ? 36.735 -8.941  85.344  1.00 28.08 ?  233 ARG B CD  1 
ATOM   3780 N  NE  . ARG B 1 233 ? 35.324 -8.830  85.714  1.00 37.12 ?  233 ARG B NE  1 
ATOM   3781 C  CZ  . ARG B 1 233 ? 34.533 -9.855  86.033  1.00 37.05 ?  233 ARG B CZ  1 
ATOM   3782 N  NH1 . ARG B 1 233 ? 35.002 -11.097 86.049  1.00 31.28 ?  233 ARG B NH1 1 
ATOM   3783 N  NH2 . ARG B 1 233 ? 33.259 -9.628  86.343  1.00 37.91 ?  233 ARG B NH2 1 
ATOM   3784 N  N   . LEU B 1 234 ? 40.489 -7.213  81.190  1.00 17.20 ?  234 LEU B N   1 
ATOM   3785 C  CA  . LEU B 1 234 ? 41.833 -7.426  80.649  1.00 17.77 ?  234 LEU B CA  1 
ATOM   3786 C  C   . LEU B 1 234 ? 42.663 -6.145  80.772  1.00 15.87 ?  234 LEU B C   1 
ATOM   3787 O  O   . LEU B 1 234 ? 42.378 -5.130  80.111  1.00 18.05 ?  234 LEU B O   1 
ATOM   3788 C  CB  . LEU B 1 234 ? 41.750 -7.903  79.198  1.00 18.35 ?  234 LEU B CB  1 
ATOM   3789 C  CG  . LEU B 1 234 ? 43.059 -8.406  78.564  1.00 18.13 ?  234 LEU B CG  1 
ATOM   3790 C  CD1 . LEU B 1 234 ? 43.719 -9.566  79.346  1.00 15.66 ?  234 LEU B CD1 1 
ATOM   3791 C  CD2 . LEU B 1 234 ? 42.838 -8.796  77.109  1.00 16.49 ?  234 LEU B CD2 1 
ATOM   3792 N  N   . ILE B 1 235 ? 43.693 -6.197  81.616  1.00 13.28 ?  235 ILE B N   1 
ATOM   3793 C  CA  . ILE B 1 235 ? 44.598 -5.066  81.808  1.00 15.21 ?  235 ILE B CA  1 
ATOM   3794 C  C   . ILE B 1 235 ? 45.558 -4.954  80.636  1.00 17.18 ?  235 ILE B C   1 
ATOM   3795 O  O   . ILE B 1 235 ? 45.814 -3.861  80.114  1.00 17.79 ?  235 ILE B O   1 
ATOM   3796 C  CB  . ILE B 1 235 ? 45.398 -5.221  83.118  1.00 13.91 ?  235 ILE B CB  1 
ATOM   3797 C  CG1 . ILE B 1 235 ? 44.515 -5.403  84.357  1.00 18.59 ?  235 ILE B CG1 1 
ATOM   3798 C  CG2 . ILE B 1 235 ? 46.385 -4.067  83.310  1.00 15.57 ?  235 ILE B CG2 1 
ATOM   3799 C  CD1 . ILE B 1 235 ? 45.322 -5.996  85.486  1.00 16.74 ?  235 ILE B CD1 1 
ATOM   3800 N  N   . GLY B 1 236 ? 46.142 -6.075  80.237  1.00 16.30 ?  236 GLY B N   1 
ATOM   3801 C  CA  . GLY B 1 236 ? 47.163 -6.025  79.209  1.00 14.29 ?  236 GLY B CA  1 
ATOM   3802 C  C   . GLY B 1 236 ? 47.601 -7.418  78.831  1.00 14.05 ?  236 GLY B C   1 
ATOM   3803 O  O   . GLY B 1 236 ? 47.190 -8.413  79.441  1.00 13.48 ?  236 GLY B O   1 
ATOM   3804 N  N   . VAL B 1 237 ? 48.438 -7.467  77.795  1.00 11.89 ?  237 VAL B N   1 
ATOM   3805 C  CA  . VAL B 1 237 ? 48.921 -8.713  77.208  1.00 10.88 ?  237 VAL B CA  1 
ATOM   3806 C  C   . VAL B 1 237 ? 50.386 -8.541  76.833  1.00 12.45 ?  237 VAL B C   1 
ATOM   3807 O  O   . VAL B 1 237 ? 50.752 -7.543  76.198  1.00 15.25 ?  237 VAL B O   1 
ATOM   3808 C  CB  . VAL B 1 237 ? 48.102 -9.104  75.957  1.00 13.31 ?  237 VAL B CB  1 
ATOM   3809 C  CG1 . VAL B 1 237 ? 48.655 -10.380 75.354  1.00 14.07 ?  237 VAL B CG1 1 
ATOM   3810 C  CG2 . VAL B 1 237 ? 46.626 -9.294  76.310  1.00 14.05 ?  237 VAL B CG2 1 
ATOM   3811 N  N   . GLU B 1 238 ? 51.229 -9.495  77.238  1.00 14.90 ?  238 GLU B N   1 
ATOM   3812 C  CA  . GLU B 1 238 ? 52.613 -9.558  76.772  1.00 12.67 ?  238 GLU B CA  1 
ATOM   3813 C  C   . GLU B 1 238 ? 52.781 -10.773 75.885  1.00 13.42 ?  238 GLU B C   1 
ATOM   3814 O  O   . GLU B 1 238 ? 52.433 -11.884 76.296  1.00 13.68 ?  238 GLU B O   1 
ATOM   3815 C  CB  . GLU B 1 238 ? 53.612 -9.673  77.928  1.00 15.93 ?  238 GLU B CB  1 
ATOM   3816 C  CG  . GLU B 1 238 ? 53.432 -8.685  78.997  1.00 21.50 ?  238 GLU B CG  1 
ATOM   3817 C  CD  . GLU B 1 238 ? 54.470 -8.891  80.071  1.00 18.09 ?  238 GLU B CD  1 
ATOM   3818 O  OE1 . GLU B 1 238 ? 54.302 -9.815  80.911  1.00 18.76 ?  238 GLU B OE1 1 
ATOM   3819 O  OE2 . GLU B 1 238 ? 55.465 -8.148  80.031  1.00 21.27 -1 238 GLU B OE2 1 
ATOM   3820 N  N   . LEU B 1 239 ? 53.312 -10.558 74.683  1.00 11.80 ?  239 LEU B N   1 
ATOM   3821 C  CA  . LEU B 1 239 ? 53.616 -11.618 73.723  1.00 12.17 ?  239 LEU B CA  1 
ATOM   3822 C  C   . LEU B 1 239 ? 55.128 -11.728 73.601  1.00 14.67 ?  239 LEU B C   1 
ATOM   3823 O  O   . LEU B 1 239 ? 55.796 -10.722 73.346  1.00 14.32 ?  239 LEU B O   1 
ATOM   3824 C  CB  . LEU B 1 239 ? 53.011 -11.294 72.352  1.00 12.96 ?  239 LEU B CB  1 
ATOM   3825 C  CG  . LEU B 1 239 ? 51.568 -10.805 72.271  1.00 16.85 ?  239 LEU B CG  1 
ATOM   3826 C  CD1 . LEU B 1 239 ? 51.224 -10.502 70.823  1.00 17.93 ?  239 LEU B CD1 1 
ATOM   3827 C  CD2 . LEU B 1 239 ? 50.638 -11.878 72.783  1.00 16.71 ?  239 LEU B CD2 1 
ATOM   3828 N  N   . ALA B 1 240 ? 55.684 -12.927 73.799  1.00 11.68 ?  240 ALA B N   1 
ATOM   3829 C  CA  . ALA B 1 240 ? 57.134 -13.028 73.842  1.00 11.00 ?  240 ALA B CA  1 
ATOM   3830 C  C   . ALA B 1 240 ? 57.659 -14.293 73.178  1.00 16.93 ?  240 ALA B C   1 
ATOM   3831 O  O   . ALA B 1 240 ? 57.027 -15.348 73.226  1.00 14.52 ?  240 ALA B O   1 
ATOM   3832 C  CB  . ALA B 1 240 ? 57.638 -12.996 75.287  1.00 16.33 ?  240 ALA B CB  1 
ATOM   3833 N  N   . GLU B 1 241 ? 58.847 -14.151 72.574  1.00 15.98 ?  241 GLU B N   1 
ATOM   3834 C  CA  . GLU B 1 241 ? 59.818 -15.208 72.262  1.00 15.79 ?  241 GLU B CA  1 
ATOM   3835 C  C   . GLU B 1 241 ? 59.572 -15.921 70.939  1.00 17.03 ?  241 GLU B C   1 
ATOM   3836 O  O   . GLU B 1 241 ? 59.905 -17.105 70.788  1.00 23.10 ?  241 GLU B O   1 
ATOM   3837 C  CB  . GLU B 1 241 ? 59.903 -16.227 73.407  1.00 15.77 ?  241 GLU B CB  1 
ATOM   3838 C  CG  . GLU B 1 241 ? 60.281 -15.549 74.718  1.00 16.53 ?  241 GLU B CG  1 
ATOM   3839 C  CD  . GLU B 1 241 ? 61.202 -16.351 75.583  1.00 20.58 ?  241 GLU B CD  1 
ATOM   3840 O  OE1 . GLU B 1 241 ? 61.921 -15.715 76.384  1.00 19.75 ?  241 GLU B OE1 1 
ATOM   3841 O  OE2 . GLU B 1 241 ? 61.211 -17.598 75.467  1.00 20.41 -1 241 GLU B OE2 1 
ATOM   3842 N  N   . LEU B 1 242 ? 59.038 -15.217 69.954  1.00 16.95 ?  242 LEU B N   1 
ATOM   3843 C  CA  . LEU B 1 242 ? 59.135 -15.713 68.594  1.00 14.38 ?  242 LEU B CA  1 
ATOM   3844 C  C   . LEU B 1 242 ? 60.588 -15.606 68.151  1.00 17.62 ?  242 LEU B C   1 
ATOM   3845 O  O   . LEU B 1 242 ? 61.152 -14.507 68.128  1.00 16.47 ?  242 LEU B O   1 
ATOM   3846 C  CB  . LEU B 1 242 ? 58.222 -14.913 67.660  1.00 14.75 ?  242 LEU B CB  1 
ATOM   3847 C  CG  . LEU B 1 242 ? 58.397 -15.154 66.157  1.00 16.28 ?  242 LEU B CG  1 
ATOM   3848 C  CD1 . LEU B 1 242 ? 58.192 -16.608 65.778  1.00 16.93 ?  242 LEU B CD1 1 
ATOM   3849 C  CD2 . LEU B 1 242 ? 57.456 -14.273 65.332  1.00 14.00 ?  242 LEU B CD2 1 
ATOM   3850 N  N   . ASN B 1 243 ? 61.195 -16.734 67.778  1.00 16.17 ?  243 ASN B N   1 
ATOM   3851 C  CA  . ASN B 1 243 ? 62.578 -16.748 67.316  1.00 17.18 ?  243 ASN B CA  1 
ATOM   3852 C  C   . ASN B 1 243 ? 62.592 -17.013 65.818  1.00 17.96 ?  243 ASN B C   1 
ATOM   3853 O  O   . ASN B 1 243 ? 62.666 -18.161 65.391  1.00 18.21 ?  243 ASN B O   1 
ATOM   3854 C  CB  . ASN B 1 243 ? 63.405 -17.812 68.042  1.00 15.04 ?  243 ASN B CB  1 
ATOM   3855 C  CG  . ASN B 1 243 ? 64.853 -17.757 67.637  1.00 17.95 ?  243 ASN B CG  1 
ATOM   3856 O  OD1 . ASN B 1 243 ? 65.406 -16.668 67.469  1.00 17.62 ?  243 ASN B OD1 1 
ATOM   3857 N  ND2 . ASN B 1 243 ? 65.478 -18.921 67.455  1.00 19.27 ?  243 ASN B ND2 1 
ATOM   3858 N  N   . ALA B 1 244 ? 62.527 -15.947 65.016  1.00 14.46 ?  244 ALA B N   1 
ATOM   3859 C  CA  . ALA B 1 244 ? 62.524 -16.146 63.570  1.00 19.21 ?  244 ALA B CA  1 
ATOM   3860 C  C   . ALA B 1 244 ? 62.949 -14.870 62.868  1.00 16.50 ?  244 ALA B C   1 
ATOM   3861 O  O   . ALA B 1 244 ? 62.525 -13.784 63.285  1.00 16.57 ?  244 ALA B O   1 
ATOM   3862 C  CB  . ALA B 1 244 ? 61.141 -16.566 63.070  1.00 19.20 ?  244 ALA B CB  1 
ATOM   3863 N  N   . PRO B 1 245 ? 63.753 -14.953 61.803  1.00 16.19 ?  245 PRO B N   1 
ATOM   3864 C  CA  . PRO B 1 245 ? 64.105 -13.740 61.056  1.00 16.06 ?  245 PRO B CA  1 
ATOM   3865 C  C   . PRO B 1 245 ? 62.860 -13.041 60.526  1.00 14.33 ?  245 PRO B C   1 
ATOM   3866 O  O   . PRO B 1 245 ? 61.888 -13.675 60.119  1.00 14.59 ?  245 PRO B O   1 
ATOM   3867 C  CB  . PRO B 1 245 ? 64.988 -14.262 59.911  1.00 18.03 ?  245 PRO B CB  1 
ATOM   3868 C  CG  . PRO B 1 245 ? 65.438 -15.610 60.332  1.00 16.96 ?  245 PRO B CG  1 
ATOM   3869 C  CD  . PRO B 1 245 ? 64.334 -16.163 61.198  1.00 18.81 ?  245 PRO B CD  1 
ATOM   3870 N  N   . ALA B 1 246 ? 62.908 -11.710 60.517  1.00 14.01 ?  246 ALA B N   1 
ATOM   3871 C  CA  . ALA B 1 246 ? 61.716 -10.928 60.179  1.00 19.09 ?  246 ALA B CA  1 
ATOM   3872 C  C   . ALA B 1 246 ? 61.218 -11.236 58.775  1.00 17.75 ?  246 ALA B C   1 
ATOM   3873 O  O   . ALA B 1 246 ? 60.004 -11.249 58.535  1.00 21.65 ?  246 ALA B O   1 
ATOM   3874 C  CB  . ALA B 1 246 ? 62.011 -9.431  60.339  1.00 18.16 ?  246 ALA B CB  1 
ATOM   3875 N  N   . ASP B 1 247 ? 62.125 -11.540 57.853  1.00 19.83 ?  247 ASP B N   1 
ATOM   3876 C  CA  . ASP B 1 247 ? 61.747 -11.786 56.466  1.00 21.64 ?  247 ASP B CA  1 
ATOM   3877 C  C   . ASP B 1 247 ? 61.593 -13.268 56.131  1.00 25.24 ?  247 ASP B C   1 
ATOM   3878 O  O   . ASP B 1 247 ? 61.466 -13.612 54.954  1.00 28.45 ?  247 ASP B O   1 
ATOM   3879 C  CB  . ASP B 1 247 ? 62.763 -11.131 55.521  1.00 23.20 ?  247 ASP B CB  1 
ATOM   3880 C  CG  . ASP B 1 247 ? 64.197 -11.540 55.807  1.00 32.39 ?  247 ASP B CG  1 
ATOM   3881 O  OD1 . ASP B 1 247 ? 64.446 -12.333 56.743  1.00 35.42 ?  247 ASP B OD1 1 
ATOM   3882 O  OD2 . ASP B 1 247 ? 65.099 -11.066 55.082  1.00 40.76 -1 247 ASP B OD2 1 
ATOM   3883 N  N   . SER B 1 248 ? 61.546 -14.146 57.120  1.00 16.99 ?  248 SER B N   1 
ATOM   3884 C  CA  . SER B 1 248 ? 61.488 -15.570 56.823  1.00 16.86 ?  248 SER B CA  1 
ATOM   3885 C  C   . SER B 1 248 ? 60.056 -16.060 56.630  1.00 19.18 ?  248 SER B C   1 
ATOM   3886 O  O   . SER B 1 248 ? 59.084 -15.487 57.140  1.00 18.05 ?  248 SER B O   1 
ATOM   3887 C  CB  . SER B 1 248 ? 62.159 -16.363 57.940  1.00 18.15 ?  248 SER B CB  1 
ATOM   3888 O  OG  . SER B 1 248 ? 61.403 -16.225 59.129  1.00 17.24 ?  248 SER B OG  1 
ATOM   3889 N  N   . GLU B 1 249 ? 59.933 -17.156 55.879  1.00 16.09 ?  249 GLU B N   1 
ATOM   3890 C  CA  . GLU B 1 249 ? 58.630 -17.783 55.718  1.00 20.55 ?  249 GLU B CA  1 
ATOM   3891 C  C   . GLU B 1 249 ? 58.100 -18.299 57.047  1.00 18.73 ?  249 GLU B C   1 
ATOM   3892 O  O   . GLU B 1 249 ? 56.895 -18.221 57.315  1.00 18.59 ?  249 GLU B O   1 
ATOM   3893 C  CB  . GLU B 1 249 ? 58.719 -18.915 54.697  1.00 24.78 ?  249 GLU B CB  1 
ATOM   3894 C  CG  . GLU B 1 249 ? 57.402 -19.635 54.479  1.00 28.49 ?  249 GLU B CG  1 
ATOM   3895 C  CD  . GLU B 1 249 ? 56.438 -18.816 53.644  1.00 40.64 ?  249 GLU B CD  1 
ATOM   3896 O  OE1 . GLU B 1 249 ? 56.896 -17.870 52.956  1.00 40.90 ?  249 GLU B OE1 1 
ATOM   3897 O  OE2 . GLU B 1 249 ? 55.223 -19.109 53.688  1.00 50.13 -1 249 GLU B OE2 1 
ATOM   3898 N  N   . ARG B 1 250 ? 58.984 -18.819 57.913  1.00 15.58 ?  250 ARG B N   1 
ATOM   3899 C  CA  . ARG B 1 250 ? 58.461 -19.341 59.162  1.00 16.30 ?  250 ARG B CA  1 
ATOM   3900 C  C   . ARG B 1 250 ? 57.931 -18.216 60.043  1.00 17.11 ?  250 ARG B C   1 
ATOM   3901 O  O   . ARG B 1 250 ? 56.980 -18.428 60.801  1.00 17.30 ?  250 ARG B O   1 
ATOM   3902 C  CB  . ARG B 1 250 ? 59.518 -20.172 59.911  1.00 19.73 ?  250 ARG B CB  1 
ATOM   3903 C  CG  . ARG B 1 250 ? 60.774 -19.435 60.393  1.00 15.24 ?  250 ARG B CG  1 
ATOM   3904 C  CD  . ARG B 1 250 ? 61.784 -20.507 60.850  1.00 17.22 ?  250 ARG B CD  1 
ATOM   3905 N  NE  . ARG B 1 250 ? 63.108 -20.010 61.210  1.00 16.73 ?  250 ARG B NE  1 
ATOM   3906 C  CZ  . ARG B 1 250 ? 64.067 -19.703 60.333  1.00 19.44 ?  250 ARG B CZ  1 
ATOM   3907 N  NH1 . ARG B 1 250 ? 65.248 -19.309 60.763  1.00 18.71 ?  250 ARG B NH1 1 
ATOM   3908 N  NH2 . ARG B 1 250 ? 63.847 -19.790 59.027  1.00 18.76 ?  250 ARG B NH2 1 
ATOM   3909 N  N   . ALA B 1 251 ? 58.516 -17.016 59.950  1.00 17.79 ?  251 ALA B N   1 
ATOM   3910 C  CA  . ALA B 1 251 ? 57.967 -15.891 60.703  1.00 15.13 ?  251 ALA B CA  1 
ATOM   3911 C  C   . ALA B 1 251 ? 56.617 -15.467 60.133  1.00 16.08 ?  251 ALA B C   1 
ATOM   3912 O  O   . ALA B 1 251 ? 55.698 -15.142 60.884  1.00 17.13 ?  251 ALA B O   1 
ATOM   3913 C  CB  . ALA B 1 251 ? 58.959 -14.725 60.712  1.00 13.73 ?  251 ALA B CB  1 
ATOM   3914 N  N   . GLU B 1 252 ? 56.473 -15.487 58.808  1.00 14.30 ?  252 GLU B N   1 
ATOM   3915 C  CA  . GLU B 1 252 ? 55.179 -15.180 58.201  1.00 16.98 ?  252 GLU B CA  1 
ATOM   3916 C  C   . GLU B 1 252 ? 54.102 -16.142 58.677  1.00 19.20 ?  252 GLU B C   1 
ATOM   3917 O  O   . GLU B 1 252 ? 52.997 -15.724 59.058  1.00 20.19 ?  252 GLU B O   1 
ATOM   3918 C  CB  . GLU B 1 252 ? 55.300 -15.226 56.681  1.00 21.61 ?  252 GLU B CB  1 
ATOM   3919 C  CG  . GLU B 1 252 ? 53.985 -15.056 55.966  1.00 22.82 ?  252 GLU B CG  1 
ATOM   3920 C  CD  . GLU B 1 252 ? 54.162 -15.004 54.461  1.00 40.37 ?  252 GLU B CD  1 
ATOM   3921 O  OE1 . GLU B 1 252 ? 54.445 -13.906 53.931  1.00 43.83 ?  252 GLU B OE1 1 
ATOM   3922 O  OE2 . GLU B 1 252 ? 54.034 -16.066 53.814  1.00 43.48 -1 252 GLU B OE2 1 
ATOM   3923 N  N   . GLN B 1 253 ? 54.401 -17.442 58.655  1.00 17.83 ?  253 GLN B N   1 
ATOM   3924 C  CA  . GLN B 1 253 ? 53.430 -18.429 59.123  1.00 17.59 ?  253 GLN B CA  1 
ATOM   3925 C  C   . GLN B 1 253 ? 53.168 -18.289 60.617  1.00 17.06 ?  253 GLN B C   1 
ATOM   3926 O  O   . GLN B 1 253 ? 52.031 -18.460 61.068  1.00 18.51 ?  253 GLN B O   1 
ATOM   3927 C  CB  . GLN B 1 253 ? 53.919 -19.839 58.797  1.00 20.73 ?  253 GLN B CB  1 
ATOM   3928 C  CG  . GLN B 1 253 ? 54.143 -20.095 57.313  1.00 23.48 ?  253 GLN B CG  1 
ATOM   3929 C  CD  . GLN B 1 253 ? 54.130 -21.587 56.988  1.00 39.89 ?  253 GLN B CD  1 
ATOM   3930 O  OE1 . GLN B 1 253 ? 53.639 -22.405 57.775  1.00 43.86 ?  253 GLN B OE1 1 
ATOM   3931 N  NE2 . GLN B 1 253 ? 54.664 -21.945 55.822  1.00 41.01 ?  253 GLN B NE2 1 
ATOM   3932 N  N   . ALA B 1 254 ? 54.199 -17.942 61.400  1.00 16.76 ?  254 ALA B N   1 
ATOM   3933 C  CA  . ALA B 1 254 ? 54.037 -17.869 62.852  1.00 13.27 ?  254 ALA B CA  1 
ATOM   3934 C  C   . ALA B 1 254 ? 53.173 -16.683 63.264  1.00 16.69 ?  254 ALA B C   1 
ATOM   3935 O  O   . ALA B 1 254 ? 52.320 -16.817 64.149  1.00 14.38 ?  254 ALA B O   1 
ATOM   3936 C  CB  . ALA B 1 254 ? 55.399 -17.775 63.547  1.00 16.68 ?  254 ALA B CB  1 
ATOM   3937 N  N   . VAL B 1 255 ? 53.380 -15.508 62.660  1.00 14.44 ?  255 VAL B N   1 
ATOM   3938 C  CA  . VAL B 1 255 ? 52.563 -14.377 63.103  1.00 15.15 ?  255 VAL B CA  1 
ATOM   3939 C  C   . VAL B 1 255 ? 51.116 -14.540 62.672  1.00 14.68 ?  255 VAL B C   1 
ATOM   3940 O  O   . VAL B 1 255 ? 50.219 -13.988 63.319  1.00 14.75 ?  255 VAL B O   1 
ATOM   3941 C  CB  . VAL B 1 255 ? 53.134 -13.012 62.657  1.00 18.60 ?  255 VAL B CB  1 
ATOM   3942 C  CG1 . VAL B 1 255 ? 54.585 -12.862 63.148  1.00 17.65 ?  255 VAL B CG1 1 
ATOM   3943 C  CG2 . VAL B 1 255 ? 53.017 -12.844 61.139  1.00 22.22 ?  255 VAL B CG2 1 
ATOM   3944 N  N   . ALA B 1 256 ? 50.841 -15.330 61.629  1.00 14.73 ?  256 ALA B N   1 
ATOM   3945 C  CA  . ALA B 1 256 ? 49.448 -15.564 61.281  1.00 19.91 ?  256 ALA B CA  1 
ATOM   3946 C  C   . ALA B 1 256 ? 48.741 -16.343 62.383  1.00 13.17 ?  256 ALA B C   1 
ATOM   3947 O  O   . ALA B 1 256 ? 47.564 -16.097 62.666  1.00 17.35 ?  256 ALA B O   1 
ATOM   3948 C  CB  . ALA B 1 256 ? 49.345 -16.286 59.936  1.00 21.83 ?  256 ALA B CB  1 
ATOM   3949 N  N   . VAL B 1 257 ? 49.444 -17.286 63.015  1.00 15.31 ?  257 VAL B N   1 
ATOM   3950 C  CA  . VAL B 1 257 ? 48.887 -17.999 64.160  1.00 13.02 ?  257 VAL B CA  1 
ATOM   3951 C  C   . VAL B 1 257 ? 48.768 -17.072 65.361  1.00 16.64 ?  257 VAL B C   1 
ATOM   3952 O  O   . VAL B 1 257 ? 47.782 -17.121 66.106  1.00 16.16 ?  257 VAL B O   1 
ATOM   3953 C  CB  . VAL B 1 257 ? 49.763 -19.224 64.498  1.00 17.96 ?  257 VAL B CB  1 
ATOM   3954 C  CG1 . VAL B 1 257 ? 49.166 -20.011 65.664  1.00 21.41 ?  257 VAL B CG1 1 
ATOM   3955 C  CG2 . VAL B 1 257 ? 49.977 -20.102 63.279  1.00 16.81 ?  257 VAL B CG2 1 
ATOM   3956 N  N   . ILE B 1 258 ? 49.783 -16.238 65.591  1.00 11.90 ?  258 ILE B N   1 
ATOM   3957 C  CA  . ILE B 1 258 ? 49.740 -15.303 66.717  1.00 14.76 ?  258 ILE B CA  1 
ATOM   3958 C  C   . ILE B 1 258 ? 48.538 -14.370 66.599  1.00 14.62 ?  258 ILE B C   1 
ATOM   3959 O  O   . ILE B 1 258 ? 47.767 -14.204 67.552  1.00 15.19 ?  258 ILE B O   1 
ATOM   3960 C  CB  . ILE B 1 258 ? 51.067 -14.527 66.823  1.00 14.30 ?  258 ILE B CB  1 
ATOM   3961 C  CG1 . ILE B 1 258 ? 52.177 -15.464 67.304  1.00 14.91 ?  258 ILE B CG1 1 
ATOM   3962 C  CG2 . ILE B 1 258 ? 50.926 -13.315 67.783  1.00 14.81 ?  258 ILE B CG2 1 
ATOM   3963 C  CD1 . ILE B 1 258 ? 53.611 -14.894 67.104  1.00 15.79 ?  258 ILE B CD1 1 
ATOM   3964 N  N   . LEU B 1 259 ? 48.335 -13.759 65.427  1.00 16.24 ?  259 LEU B N   1 
ATOM   3965 C  CA  . LEU B 1 259 ? 47.213 -12.832 65.311  1.00 13.01 ?  259 LEU B CA  1 
ATOM   3966 C  C   . LEU B 1 259 ? 45.889 -13.543 65.530  1.00 17.72 ?  259 LEU B C   1 
ATOM   3967 O  O   . LEU B 1 259 ? 44.956 -12.965 66.097  1.00 15.95 ?  259 LEU B O   1 
ATOM   3968 C  CB  . LEU B 1 259 ? 47.203 -12.142 63.939  1.00 15.53 ?  259 LEU B CB  1 
ATOM   3969 C  CG  . LEU B 1 259 ? 48.238 -11.044 63.678  1.00 22.82 ?  259 LEU B CG  1 
ATOM   3970 C  CD1 . LEU B 1 259 ? 48.183 -10.579 62.259  1.00 22.23 ?  259 LEU B CD1 1 
ATOM   3971 C  CD2 . LEU B 1 259 ? 47.983 -9.890  64.563  1.00 22.82 ?  259 LEU B CD2 1 
ATOM   3972 N  N   . ASP B 1 260 ? 45.801 -14.800 65.096  1.00 17.03 ?  260 ASP B N   1 
ATOM   3973 C  CA  . ASP B 1 260 ? 44.587 -15.582 65.294  1.00 17.34 ?  260 ASP B CA  1 
ATOM   3974 C  C   . ASP B 1 260 ? 44.329 -15.839 66.776  1.00 17.15 ?  260 ASP B C   1 
ATOM   3975 O  O   . ASP B 1 260 ? 43.183 -15.742 67.239  1.00 17.63 ?  260 ASP B O   1 
ATOM   3976 C  CB  . ASP B 1 260 ? 44.711 -16.891 64.505  1.00 16.68 ?  260 ASP B CB  1 
ATOM   3977 C  CG  . ASP B 1 260 ? 43.473 -17.769 64.611  1.00 24.97 ?  260 ASP B CG  1 
ATOM   3978 O  OD1 . ASP B 1 260 ? 42.355 -17.230 64.728  1.00 27.57 ?  260 ASP B OD1 1 
ATOM   3979 O  OD2 . ASP B 1 260 ? 43.629 -19.008 64.558  1.00 29.59 -1 260 ASP B OD2 1 
ATOM   3980 N  N   . MET B 1 261 ? 45.374 -16.152 67.551  1.00 17.38 ?  261 MET B N   1 
ATOM   3981 C  CA  . MET B 1 261 ? 45.123 -16.495 68.948  1.00 15.24 ?  261 MET B CA  1 
ATOM   3982 C  C   . MET B 1 261 ? 44.687 -15.260 69.751  1.00 16.09 ?  261 MET B C   1 
ATOM   3983 O  O   . MET B 1 261 ? 43.823 -15.363 70.631  1.00 15.34 ?  261 MET B O   1 
ATOM   3984 C  CB  . MET B 1 261 ? 46.360 -17.195 69.548  1.00 16.90 ?  261 MET B CB  1 
ATOM   3985 C  CG  . MET B 1 261 ? 46.534 -18.735 69.142  1.00 12.19 ?  261 MET B CG  1 
ATOM   3986 S  SD  . MET B 1 261 ? 48.136 -19.416 69.665  1.00 27.28 ?  261 MET B SD  1 
ATOM   3987 C  CE  . MET B 1 261 ? 49.293 -18.345 68.827  1.00 25.02 ?  261 MET B CE  1 
ATOM   3988 N  N   . VAL B 1 262 ? 45.232 -14.073 69.437  1.00 14.45 ?  262 VAL B N   1 
ATOM   3989 C  CA  . VAL B 1 262 ? 44.933 -12.867 70.221  1.00 18.35 ?  262 VAL B CA  1 
ATOM   3990 C  C   . VAL B 1 262 ? 43.745 -12.079 69.691  1.00 17.56 ?  262 VAL B C   1 
ATOM   3991 O  O   . VAL B 1 262 ? 43.232 -11.201 70.405  1.00 17.34 ?  262 VAL B O   1 
ATOM   3992 C  CB  . VAL B 1 262 ? 46.134 -11.894 70.299  1.00 18.14 ?  262 VAL B CB  1 
ATOM   3993 C  CG1 . VAL B 1 262 ? 47.354 -12.588 70.902  1.00 17.01 ?  262 VAL B CG1 1 
ATOM   3994 C  CG2 . VAL B 1 262 ? 46.447 -11.296 68.926  1.00 17.46 ?  262 VAL B CG2 1 
ATOM   3995 N  N   . ALA B 1 263 ? 43.288 -12.364 68.469  1.00 16.10 ?  263 ALA B N   1 
ATOM   3996 C  CA  . ALA B 1 263 ? 42.227 -11.575 67.845  1.00 13.68 ?  263 ALA B CA  1 
ATOM   3997 C  C   . ALA B 1 263 ? 40.981 -11.392 68.703  1.00 16.57 ?  263 ALA B C   1 
ATOM   3998 O  O   . ALA B 1 263 ? 40.428 -10.278 68.693  1.00 19.07 ?  263 ALA B O   1 
ATOM   3999 C  CB  . ALA B 1 263 ? 41.833 -12.211 66.505  1.00 16.14 ?  263 ALA B CB  1 
ATOM   4000 N  N   . PRO B 1 264 ? 40.470 -12.395 69.435  1.00 16.27 ?  264 PRO B N   1 
ATOM   4001 C  CA  . PRO B 1 264 ? 39.235 -12.130 70.197  1.00 15.86 ?  264 PRO B CA  1 
ATOM   4002 C  C   . PRO B 1 264 ? 39.387 -10.966 71.152  1.00 17.61 ?  264 PRO B C   1 
ATOM   4003 O  O   . PRO B 1 264 ? 38.474 -10.142 71.266  1.00 20.77 ?  264 PRO B O   1 
ATOM   4004 C  CB  . PRO B 1 264 ? 38.978 -13.450 70.936  1.00 18.77 ?  264 PRO B CB  1 
ATOM   4005 C  CG  . PRO B 1 264 ? 39.663 -14.481 70.119  1.00 17.68 ?  264 PRO B CG  1 
ATOM   4006 C  CD  . PRO B 1 264 ? 40.885 -13.808 69.553  1.00 18.70 ?  264 PRO B CD  1 
ATOM   4007 N  N   . ALA B 1 265 ? 40.537 -10.866 71.832  1.00 15.50 ?  265 ALA B N   1 
ATOM   4008 C  CA  . ALA B 1 265 ? 40.752 -9.770  72.765  1.00 15.96 ?  265 ALA B CA  1 
ATOM   4009 C  C   . ALA B 1 265 ? 41.109 -8.468  72.052  1.00 17.99 ?  265 ALA B C   1 
ATOM   4010 O  O   . ALA B 1 265 ? 40.655 -7.389  72.453  1.00 17.71 ?  265 ALA B O   1 
ATOM   4011 C  CB  . ALA B 1 265 ? 41.848 -10.148 73.765  1.00 18.98 ?  265 ALA B CB  1 
ATOM   4012 N  N   . PHE B 1 266 ? 41.961 -8.526  71.034  1.00 15.10 ?  266 PHE B N   1 
ATOM   4013 C  CA  . PHE B 1 266 ? 42.390 -7.273  70.432  1.00 17.44 ?  266 PHE B CA  1 
ATOM   4014 C  C   . PHE B 1 266 ? 41.297 -6.692  69.542  1.00 18.73 ?  266 PHE B C   1 
ATOM   4015 O  O   . PHE B 1 266 ? 41.183 -5.462  69.428  1.00 20.05 ?  266 PHE B O   1 
ATOM   4016 C  CB  . PHE B 1 266 ? 43.680 -7.466  69.627  1.00 16.14 ?  266 PHE B CB  1 
ATOM   4017 C  CG  . PHE B 1 266 ? 44.903 -7.781  70.457  1.00 16.71 ?  266 PHE B CG  1 
ATOM   4018 C  CD1 . PHE B 1 266 ? 44.829 -7.987  71.829  1.00 18.87 ?  266 PHE B CD1 1 
ATOM   4019 C  CD2 . PHE B 1 266 ? 46.142 -7.894  69.839  1.00 18.96 ?  266 PHE B CD2 1 
ATOM   4020 C  CE1 . PHE B 1 266 ? 45.973 -8.302  72.571  1.00 19.34 ?  266 PHE B CE1 1 
ATOM   4021 C  CE2 . PHE B 1 266 ? 47.293 -8.195  70.575  1.00 19.65 ?  266 PHE B CE2 1 
ATOM   4022 C  CZ  . PHE B 1 266 ? 47.208 -8.407  71.942  1.00 16.77 ?  266 PHE B CZ  1 
ATOM   4023 N  N   . ASP B 1 267 ? 40.487 -7.552  68.917  1.00 15.50 ?  267 ASP B N   1 
ATOM   4024 C  CA  . ASP B 1 267 ? 39.344 -7.058  68.151  1.00 18.18 ?  267 ASP B CA  1 
ATOM   4025 C  C   . ASP B 1 267 ? 38.400 -6.274  69.048  1.00 22.64 ?  267 ASP B C   1 
ATOM   4026 O  O   . ASP B 1 267 ? 37.919 -5.204  68.667  1.00 20.86 ?  267 ASP B O   1 
ATOM   4027 C  CB  . ASP B 1 267 ? 38.576 -8.208  67.499  1.00 18.05 ?  267 ASP B CB  1 
ATOM   4028 C  CG  . ASP B 1 267 ? 39.267 -8.771  66.287  1.00 21.32 ?  267 ASP B CG  1 
ATOM   4029 O  OD1 . ASP B 1 267 ? 40.290 -8.191  65.842  1.00 21.04 ?  267 ASP B OD1 1 
ATOM   4030 O  OD2 . ASP B 1 267 ? 38.780 -9.806  65.766  1.00 24.46 -1 267 ASP B OD2 1 
ATOM   4031 N  N   . ALA B 1 268 ? 38.121 -6.797  70.243  1.00 19.57 ?  268 ALA B N   1 
ATOM   4032 C  CA  . ALA B 1 268 ? 37.259 -6.081  71.182  1.00 22.93 ?  268 ALA B CA  1 
ATOM   4033 C  C   . ALA B 1 268 ? 37.858 -4.734  71.575  1.00 24.18 ?  268 ALA B C   1 
ATOM   4034 O  O   . ALA B 1 268 ? 37.163 -3.713  71.583  1.00 26.32 ?  268 ALA B O   1 
ATOM   4035 C  CB  . ALA B 1 268 ? 37.008 -6.942  72.423  1.00 24.73 ?  268 ALA B CB  1 
ATOM   4036 N  N   . ALA B 1 269 ? 39.151 -4.710  71.911  1.00 20.25 ?  269 ALA B N   1 
ATOM   4037 C  CA  . ALA B 1 269 ? 39.771 -3.463  72.341  1.00 25.36 ?  269 ALA B CA  1 
ATOM   4038 C  C   . ALA B 1 269 ? 39.837 -2.452  71.210  1.00 27.54 ?  269 ALA B C   1 
ATOM   4039 O  O   . ALA B 1 269 ? 39.705 -1.247  71.450  1.00 27.46 ?  269 ALA B O   1 
ATOM   4040 C  CB  . ALA B 1 269 ? 41.176 -3.726  72.895  1.00 23.25 ?  269 ALA B CB  1 
ATOM   4041 N  N   . ALA B 1 270 ? 40.020 -2.916  69.972  1.00 23.27 ?  270 ALA B N   1 
ATOM   4042 C  CA  . ALA B 1 270 ? 40.152 -1.989  68.856  1.00 24.00 ?  270 ALA B CA  1 
ATOM   4043 C  C   . ALA B 1 270 ? 38.824 -1.354  68.456  1.00 27.70 ?  270 ALA B C   1 
ATOM   4044 O  O   . ALA B 1 270 ? 38.824 -0.324  67.773  1.00 32.95 ?  270 ALA B O   1 
ATOM   4045 C  CB  . ALA B 1 270 ? 40.795 -2.705  67.661  1.00 22.11 ?  270 ALA B CB  1 
ATOM   4046 N  N   . ALA B 1 271 ? 37.694 -1.931  68.856  1.00 26.16 ?  271 ALA B N   1 
ATOM   4047 C  CA  . ALA B 1 271 ? 36.396 -1.351  68.539  1.00 26.32 ?  271 ALA B CA  1 
ATOM   4048 C  C   . ALA B 1 271 ? 35.839 -0.475  69.659  1.00 30.29 ?  271 ALA B C   1 
ATOM   4049 O  O   . ALA B 1 271 ? 34.817 0.190   69.451  1.00 31.99 ?  271 ALA B O   1 
ATOM   4050 C  CB  . ALA B 1 271 ? 35.395 -2.460  68.208  1.00 28.07 ?  271 ALA B CB  1 
ATOM   4051 N  N   . ARG B 1 272 ? 36.500 -0.434  70.821  1.00 29.23 ?  272 ARG B N   1 
ATOM   4052 C  CA  . ARG B 1 272 ? 35.985 0.232   72.012  1.00 31.73 ?  272 ARG B CA  1 
ATOM   4053 C  C   . ARG B 1 272 ? 36.073 1.751   71.889  1.00 36.96 ?  272 ARG B C   1 
ATOM   4054 O  O   . ARG B 1 272 ? 36.985 2.279   71.246  1.00 36.18 ?  272 ARG B O   1 
ATOM   4055 C  CB  . ARG B 1 272 ? 36.751 -0.218  73.255  1.00 32.94 ?  272 ARG B CB  1 
ATOM   4056 C  CG  . ARG B 1 272 ? 36.052 -1.312  74.043  1.00 37.18 ?  272 ARG B CG  1 
ATOM   4057 C  CD  . ARG B 1 272 ? 37.060 -2.191  74.784  1.00 42.82 ?  272 ARG B CD  1 
ATOM   4058 N  NE  . ARG B 1 272 ? 38.254 -1.444  75.189  1.00 45.26 ?  272 ARG B NE  1 
ATOM   4059 C  CZ  . ARG B 1 272 ? 39.227 -1.945  75.945  1.00 46.25 ?  272 ARG B CZ  1 
ATOM   4060 N  NH1 . ARG B 1 272 ? 39.156 -3.203  76.360  1.00 43.75 ?  272 ARG B NH1 1 
ATOM   4061 N  NH2 . ARG B 1 272 ? 40.278 -1.198  76.267  1.00 42.33 ?  272 ARG B NH2 1 
ATOM   4062 N  N   . PRO B 1 273 ? 35.136 2.470   72.511  1.00 38.99 ?  273 PRO B N   1 
ATOM   4063 C  CA  . PRO B 1 273 ? 35.180 3.936   72.490  1.00 38.28 ?  273 PRO B CA  1 
ATOM   4064 C  C   . PRO B 1 273 ? 36.417 4.478   73.192  1.00 47.56 ?  273 PRO B C   1 
ATOM   4065 O  O   . PRO B 1 273 ? 37.012 3.837   74.061  1.00 48.12 ?  273 PRO B O   1 
ATOM   4066 C  CB  . PRO B 1 273 ? 33.903 4.344   73.236  1.00 36.62 ?  273 PRO B CB  1 
ATOM   4067 C  CG  . PRO B 1 273 ? 33.021 3.151   73.189  1.00 39.77 ?  273 PRO B CG  1 
ATOM   4068 C  CD  . PRO B 1 273 ? 33.931 1.959   73.183  1.00 38.19 ?  273 PRO B CD  1 
ATOM   4069 N  N   . LEU B 1 274 ? 36.789 5.695   72.814  1.00 50.02 ?  274 LEU B N   1 
ATOM   4070 C  CA  . LEU B 1 274 ? 37.985 6.333   73.350  1.00 49.90 ?  274 LEU B CA  1 
ATOM   4071 C  C   . LEU B 1 274 ? 37.689 7.036   74.672  1.00 50.23 ?  274 LEU B C   1 
ATOM   4072 O  O   . LEU B 1 274 ? 36.537 7.097   75.110  1.00 49.96 ?  274 LEU B O   1 
ATOM   4073 C  CB  . LEU B 1 274 ? 38.552 7.324   72.328  1.00 48.34 ?  274 LEU B CB  1 
ATOM   4074 C  CG  . LEU B 1 274 ? 38.425 6.843   70.876  1.00 44.04 ?  274 LEU B CG  1 
ATOM   4075 C  CD1 . LEU B 1 274 ? 38.630 7.958   69.878  1.00 37.28 ?  274 LEU B CD1 1 
ATOM   4076 C  CD2 . LEU B 1 274 ? 39.383 5.706   70.599  1.00 45.31 ?  274 LEU B CD2 1 
HETATM 4077 MN MN  . MN  C 2 .   ? 50.720 4.269   55.432  0.82 8.08  ?  401 MN  A MN  1 
HETATM 4078 MG MG  . MG  D 3 .   ? 51.451 4.010   58.670  0.92 5.96  ?  402 MG  A MG  1 
HETATM 4079 MG MG  . MG  E 3 .   ? 59.179 -18.244 79.380  0.83 7.42  ?  401 MG  B MG  1 
HETATM 4080 MG MG  . MG  F 3 .   ? 60.340 -19.391 75.883  0.73 12.82 ?  402 MG  B MG  1 
HETATM 4081 MG MG  . MG  G 3 .   ? 62.330 -25.421 84.130  0.67 21.70 ?  403 MG  B MG  1 
HETATM 4082 O  O   . HOH H 4 .   ? 48.616 7.399   35.978  1.00 34.66 ?  501 HOH A O   1 
HETATM 4083 O  O   . HOH H 4 .   ? 60.674 19.755  40.472  1.00 34.27 ?  502 HOH A O   1 
HETATM 4084 O  O   . HOH H 4 .   ? 61.934 28.152  42.757  1.00 39.41 ?  503 HOH A O   1 
HETATM 4085 O  O   . HOH H 4 .   ? 40.526 0.382   65.657  1.00 33.55 ?  504 HOH A O   1 
HETATM 4086 O  O   . HOH H 4 .   ? 47.689 2.776   59.241  1.00 19.15 ?  505 HOH A O   1 
HETATM 4087 O  O   . HOH H 4 .   ? 58.265 5.368   68.930  1.00 26.94 ?  506 HOH A O   1 
HETATM 4088 O  O   . HOH H 4 .   ? 57.038 27.053  52.199  1.00 28.83 ?  507 HOH A O   1 
HETATM 4089 O  O   . HOH H 4 .   ? 40.207 4.265   65.591  1.00 38.89 ?  508 HOH A O   1 
HETATM 4090 O  O   . HOH H 4 .   ? 30.447 4.527   62.064  1.00 36.74 ?  509 HOH A O   1 
HETATM 4091 O  O   . HOH H 4 .   ? 67.019 10.540  44.172  1.00 34.15 ?  510 HOH A O   1 
HETATM 4092 O  O   . HOH H 4 .   ? 38.894 -5.095  52.929  1.00 28.15 ?  511 HOH A O   1 
HETATM 4093 O  O   . HOH H 4 .   ? 34.738 14.531  37.825  1.00 39.63 ?  512 HOH A O   1 
HETATM 4094 O  O   . HOH H 4 .   ? 50.173 5.695   66.317  1.00 26.65 ?  513 HOH A O   1 
HETATM 4095 O  O   . HOH H 4 .   ? 66.404 10.579  54.616  1.00 25.55 ?  514 HOH A O   1 
HETATM 4096 O  O   . HOH H 4 .   ? 30.113 2.368   50.843  1.00 38.28 ?  515 HOH A O   1 
HETATM 4097 O  O   . HOH H 4 .   ? 46.673 -14.504 58.492  1.00 34.13 ?  516 HOH A O   1 
HETATM 4098 O  O   . HOH H 4 .   ? 59.323 30.594  43.156  1.00 31.79 ?  517 HOH A O   1 
HETATM 4099 O  O   . HOH H 4 .   ? 66.721 15.179  49.340  1.00 28.23 ?  518 HOH A O   1 
HETATM 4100 O  O   . HOH H 4 .   ? 34.976 -5.591  57.819  1.00 40.76 ?  519 HOH A O   1 
HETATM 4101 O  O   . HOH H 4 .   ? 43.274 20.769  67.530  1.00 42.25 ?  520 HOH A O   1 
HETATM 4102 O  O   . HOH H 4 .   ? 39.700 10.832  34.028  1.00 34.81 ?  521 HOH A O   1 
HETATM 4103 O  O   . HOH H 4 .   ? 45.192 20.666  40.474  1.00 31.33 ?  522 HOH A O   1 
HETATM 4104 O  O   . HOH H 4 .   ? 58.619 30.250  62.640  1.00 30.99 ?  523 HOH A O   1 
HETATM 4105 O  O   . HOH H 4 .   ? 53.699 1.525   35.983  1.00 26.61 ?  524 HOH A O   1 
HETATM 4106 O  O   . HOH H 4 .   ? 36.186 7.027   38.356  1.00 28.34 ?  525 HOH A O   1 
HETATM 4107 O  O   . HOH H 4 .   ? 41.254 -7.629  46.924  1.00 23.10 ?  526 HOH A O   1 
HETATM 4108 O  O   . HOH H 4 .   ? 39.114 -3.430  44.846  1.00 20.30 ?  527 HOH A O   1 
HETATM 4109 O  O   . HOH H 4 .   ? 46.973 -1.473  51.619  1.00 18.93 ?  528 HOH A O   1 
HETATM 4110 O  O   . HOH H 4 .   ? 57.168 25.528  42.185  1.00 33.78 ?  529 HOH A O   1 
HETATM 4111 O  O   . HOH H 4 .   ? 55.671 -3.944  52.776  1.00 15.61 ?  530 HOH A O   1 
HETATM 4112 O  O   . HOH H 4 .   ? 56.546 -10.411 49.391  1.00 27.90 ?  531 HOH A O   1 
HETATM 4113 O  O   . HOH H 4 .   ? 28.753 12.961  60.795  1.00 37.54 ?  532 HOH A O   1 
HETATM 4114 O  O   . HOH H 4 .   ? 40.110 -13.070 54.254  1.00 34.36 ?  533 HOH A O   1 
HETATM 4115 O  O   . HOH H 4 .   ? 58.623 12.661  70.370  1.00 33.63 ?  534 HOH A O   1 
HETATM 4116 O  O   . HOH H 4 .   ? 58.861 9.602   67.899  1.00 30.06 ?  535 HOH A O   1 
HETATM 4117 O  O   . HOH H 4 .   ? 36.133 -2.360  42.501  1.00 33.89 ?  536 HOH A O   1 
HETATM 4118 O  O   . HOH H 4 .   ? 64.875 -2.663  46.335  1.00 32.20 ?  537 HOH A O   1 
HETATM 4119 O  O   . HOH H 4 .   ? 60.465 9.454   40.106  1.00 32.69 ?  538 HOH A O   1 
HETATM 4120 O  O   . HOH H 4 .   ? 41.960 20.952  40.812  1.00 31.68 ?  539 HOH A O   1 
HETATM 4121 O  O   . HOH H 4 .   ? 54.789 14.956  68.817  1.00 23.33 ?  540 HOH A O   1 
HETATM 4122 O  O   . HOH H 4 .   ? 60.954 -9.213  50.408  1.00 34.04 ?  541 HOH A O   1 
HETATM 4123 O  O   . HOH H 4 .   ? 47.432 -7.409  51.815  1.00 13.15 ?  542 HOH A O   1 
HETATM 4124 O  O   . HOH H 4 .   ? 52.396 3.850   41.607  1.00 19.34 ?  543 HOH A O   1 
HETATM 4125 O  O   . HOH H 4 .   ? 55.915 5.305   67.673  1.00 28.35 ?  544 HOH A O   1 
HETATM 4126 O  O   . HOH H 4 .   ? 43.589 -12.459 48.218  1.00 29.87 ?  545 HOH A O   1 
HETATM 4127 O  O   . HOH H 4 .   ? 53.578 10.719  36.967  1.00 28.00 ?  546 HOH A O   1 
HETATM 4128 O  O   . HOH H 4 .   ? 53.266 6.581   73.423  1.00 42.50 ?  547 HOH A O   1 
HETATM 4129 O  O   . HOH H 4 .   ? 37.085 -5.013  46.128  1.00 29.29 ?  548 HOH A O   1 
HETATM 4130 O  O   . HOH H 4 .   ? 59.474 -0.560  62.494  1.00 31.98 ?  549 HOH A O   1 
HETATM 4131 O  O   . HOH H 4 .   ? 62.953 14.950  49.949  1.00 20.24 ?  550 HOH A O   1 
HETATM 4132 O  O   . HOH H 4 .   ? 51.765 2.870   56.934  1.00 11.09 ?  551 HOH A O   1 
HETATM 4133 O  O   . HOH H 4 .   ? 38.435 20.402  40.399  1.00 32.96 ?  552 HOH A O   1 
HETATM 4134 O  O   . HOH H 4 .   ? 43.350 19.610  42.895  1.00 25.27 ?  553 HOH A O   1 
HETATM 4135 O  O   . HOH H 4 .   ? 29.889 16.441  60.007  1.00 33.81 ?  554 HOH A O   1 
HETATM 4136 O  O   . HOH H 4 .   ? 31.376 12.788  65.268  1.00 31.14 ?  555 HOH A O   1 
HETATM 4137 O  O   . HOH H 4 .   ? 51.034 -9.639  40.260  1.00 30.47 ?  556 HOH A O   1 
HETATM 4138 O  O   . HOH H 4 .   ? 56.037 -11.597 46.019  1.00 31.46 ?  557 HOH A O   1 
HETATM 4139 O  O   . HOH H 4 .   ? 53.276 25.742  40.495  1.00 39.75 ?  558 HOH A O   1 
HETATM 4140 O  O   . HOH H 4 .   ? 59.082 12.513  36.907  1.00 35.37 ?  559 HOH A O   1 
HETATM 4141 O  O   . HOH H 4 .   ? 53.040 20.914  63.494  1.00 20.64 ?  560 HOH A O   1 
HETATM 4142 O  O   . HOH H 4 .   ? 51.975 23.187  39.461  1.00 31.19 ?  561 HOH A O   1 
HETATM 4143 O  O   . HOH H 4 .   ? 46.458 -2.930  40.213  1.00 19.12 ?  562 HOH A O   1 
HETATM 4144 O  O   . HOH H 4 .   ? 41.127 -7.690  39.476  1.00 35.62 ?  563 HOH A O   1 
HETATM 4145 O  O   . HOH H 4 .   ? 37.848 0.643   36.824  1.00 24.81 ?  564 HOH A O   1 
HETATM 4146 O  O   . HOH H 4 .   ? 49.681 -6.730  50.223  1.00 13.91 ?  565 HOH A O   1 
HETATM 4147 O  O   . HOH H 4 .   ? 42.714 24.970  51.164  1.00 29.83 ?  566 HOH A O   1 
HETATM 4148 O  O   . HOH H 4 .   ? 33.722 14.257  43.568  1.00 33.96 ?  567 HOH A O   1 
HETATM 4149 O  O   . HOH H 4 .   ? 62.410 21.643  57.786  1.00 30.95 ?  568 HOH A O   1 
HETATM 4150 O  O   . HOH H 4 .   ? 45.433 6.762   64.892  1.00 28.80 ?  569 HOH A O   1 
HETATM 4151 O  O   . HOH H 4 .   ? 66.012 14.883  61.950  1.00 40.42 ?  570 HOH A O   1 
HETATM 4152 O  O   . HOH H 4 .   ? 30.504 19.614  63.795  1.00 36.05 ?  571 HOH A O   1 
HETATM 4153 O  O   . HOH H 4 .   ? 58.150 -9.560  47.186  1.00 25.00 ?  572 HOH A O   1 
HETATM 4154 O  O   . HOH H 4 .   ? 39.273 -2.654  55.576  1.00 17.20 ?  573 HOH A O   1 
HETATM 4155 O  O   . HOH H 4 .   ? 58.574 9.779   74.238  1.00 36.67 ?  574 HOH A O   1 
HETATM 4156 O  O   . HOH H 4 .   ? 65.359 12.926  60.118  1.00 31.18 ?  575 HOH A O   1 
HETATM 4157 O  O   . HOH H 4 .   ? 30.619 -5.958  48.636  1.00 33.65 ?  576 HOH A O   1 
HETATM 4158 O  O   . HOH H 4 .   ? 29.817 7.356   53.403  1.00 33.12 ?  577 HOH A O   1 
HETATM 4159 O  O   . HOH H 4 .   ? 40.249 4.249   56.301  1.00 14.25 ?  578 HOH A O   1 
HETATM 4160 O  O   . HOH H 4 .   ? 38.818 27.859  59.259  1.00 31.26 ?  579 HOH A O   1 
HETATM 4161 O  O   . HOH H 4 .   ? 33.283 -7.071  46.186  1.00 38.84 ?  580 HOH A O   1 
HETATM 4162 O  O   . HOH H 4 .   ? 63.087 6.702   64.909  1.00 36.40 ?  581 HOH A O   1 
HETATM 4163 O  O   . HOH H 4 .   ? 54.933 8.563   75.051  1.00 40.40 ?  582 HOH A O   1 
HETATM 4164 O  O   . HOH H 4 .   ? 45.369 -11.606 42.311  1.00 25.52 ?  583 HOH A O   1 
HETATM 4165 O  O   . HOH H 4 .   ? 48.043 6.252   38.240  1.00 22.77 ?  584 HOH A O   1 
HETATM 4166 O  O   . HOH H 4 .   ? 32.445 16.189  45.853  1.00 30.77 ?  585 HOH A O   1 
HETATM 4167 O  O   . HOH H 4 .   ? 44.307 -13.908 54.892  1.00 37.20 ?  586 HOH A O   1 
HETATM 4168 O  O   . HOH H 4 .   ? 36.362 20.076  59.150  1.00 21.90 ?  587 HOH A O   1 
HETATM 4169 O  O   . HOH H 4 .   ? 47.200 23.618  66.242  1.00 26.54 ?  588 HOH A O   1 
HETATM 4170 O  O   . HOH H 4 .   ? 45.625 6.706   50.321  1.00 17.09 ?  589 HOH A O   1 
HETATM 4171 O  O   . HOH H 4 .   ? 35.850 -2.124  56.524  1.00 17.79 ?  590 HOH A O   1 
HETATM 4172 O  O   . HOH H 4 .   ? 44.952 -2.433  55.871  1.00 24.97 ?  591 HOH A O   1 
HETATM 4173 O  O   . HOH H 4 .   ? 39.310 -3.858  42.190  1.00 19.29 ?  592 HOH A O   1 
HETATM 4174 O  O   . HOH H 4 .   ? 51.697 30.355  55.054  1.00 37.06 ?  593 HOH A O   1 
HETATM 4175 O  O   . HOH H 4 .   ? 34.942 18.377  65.180  1.00 28.18 ?  594 HOH A O   1 
HETATM 4176 O  O   . HOH H 4 .   ? 43.461 -5.738  46.989  1.00 15.02 ?  595 HOH A O   1 
HETATM 4177 O  O   . HOH H 4 .   ? 57.138 1.134   56.313  1.00 26.09 ?  596 HOH A O   1 
HETATM 4178 O  O   . HOH H 4 .   ? 50.278 26.904  61.866  1.00 27.29 ?  597 HOH A O   1 
HETATM 4179 O  O   . HOH H 4 .   ? 62.398 9.140   62.309  1.00 24.27 ?  598 HOH A O   1 
HETATM 4180 O  O   . HOH H 4 .   ? 40.640 28.500  57.315  1.00 31.42 ?  599 HOH A O   1 
HETATM 4181 O  O   . HOH H 4 .   ? 55.539 2.349   40.052  1.00 15.69 ?  600 HOH A O   1 
HETATM 4182 O  O   . HOH H 4 .   ? 51.929 -11.458 52.509  1.00 33.40 ?  601 HOH A O   1 
HETATM 4183 O  O   . HOH H 4 .   ? 33.107 23.173  48.241  1.00 37.37 ?  602 HOH A O   1 
HETATM 4184 O  O   . HOH H 4 .   ? 39.838 9.144   57.446  1.00 15.03 ?  603 HOH A O   1 
HETATM 4185 O  O   . HOH H 4 .   ? 49.205 0.562   60.320  1.00 22.90 ?  604 HOH A O   1 
HETATM 4186 O  O   . HOH H 4 .   ? 48.853 -2.992  38.428  1.00 24.20 ?  605 HOH A O   1 
HETATM 4187 O  O   . HOH H 4 .   ? 62.043 21.164  63.897  1.00 23.98 ?  606 HOH A O   1 
HETATM 4188 O  O   . HOH H 4 .   ? 29.775 -2.256  56.479  1.00 46.31 ?  607 HOH A O   1 
HETATM 4189 O  O   . HOH H 4 .   ? 49.955 2.336   54.993  1.00 13.76 ?  608 HOH A O   1 
HETATM 4190 O  O   . HOH H 4 .   ? 59.466 24.468  43.525  1.00 38.22 ?  609 HOH A O   1 
HETATM 4191 O  O   . HOH H 4 .   ? 39.941 6.955   55.603  1.00 17.19 ?  610 HOH A O   1 
HETATM 4192 O  O   . HOH H 4 .   ? 26.951 22.074  57.143  1.00 31.42 ?  611 HOH A O   1 
HETATM 4193 O  O   . HOH H 4 .   ? 61.498 20.981  48.633  1.00 28.47 ?  612 HOH A O   1 
HETATM 4194 O  O   . HOH H 4 .   ? 60.434 12.566  67.455  1.00 25.67 ?  613 HOH A O   1 
HETATM 4195 O  O   . HOH H 4 .   ? 59.574 21.954  44.037  1.00 32.41 ?  614 HOH A O   1 
HETATM 4196 O  O   . HOH H 4 .   ? 34.290 27.830  54.791  1.00 37.05 ?  615 HOH A O   1 
HETATM 4197 O  O   . HOH H 4 .   ? 31.247 24.042  57.104  1.00 17.74 ?  616 HOH A O   1 
HETATM 4198 O  O   . HOH H 4 .   ? 43.491 20.331  30.068  1.00 33.51 ?  617 HOH A O   1 
HETATM 4199 O  O   . HOH H 4 .   ? 37.513 14.208  31.831  1.00 36.85 ?  618 HOH A O   1 
HETATM 4200 O  O   . HOH H 4 .   ? 42.588 4.068   63.130  1.00 24.18 ?  619 HOH A O   1 
HETATM 4201 O  O   . HOH H 4 .   ? 57.869 14.935  41.154  1.00 23.16 ?  620 HOH A O   1 
HETATM 4202 O  O   . HOH H 4 .   ? 38.500 -11.610 56.586  1.00 32.71 ?  621 HOH A O   1 
HETATM 4203 O  O   . HOH H 4 .   ? 48.756 -12.612 41.303  1.00 30.05 ?  622 HOH A O   1 
HETATM 4204 O  O   . HOH H 4 .   ? 55.057 7.163   35.238  1.00 33.39 ?  623 HOH A O   1 
HETATM 4205 O  O   . HOH H 4 .   ? 36.082 12.925  69.887  1.00 38.03 ?  624 HOH A O   1 
HETATM 4206 O  O   . HOH H 4 .   ? 55.579 16.396  41.990  1.00 20.98 ?  625 HOH A O   1 
HETATM 4207 O  O   . HOH H 4 .   ? 49.090 -12.858 59.454  1.00 28.97 ?  626 HOH A O   1 
HETATM 4208 O  O   . HOH H 4 .   ? 56.528 -5.120  39.067  1.00 44.20 ?  627 HOH A O   1 
HETATM 4209 O  O   . HOH H 4 .   ? 31.763 0.830   54.219  1.00 26.35 ?  628 HOH A O   1 
HETATM 4210 O  O   . HOH H 4 .   ? 52.933 31.277  49.417  1.00 37.20 ?  629 HOH A O   1 
HETATM 4211 O  O   . HOH H 4 .   ? 65.941 13.697  56.361  1.00 27.61 ?  630 HOH A O   1 
HETATM 4212 O  O   . HOH H 4 .   ? 29.223 8.064   43.877  1.00 27.07 ?  631 HOH A O   1 
HETATM 4213 O  O   . HOH H 4 .   ? 57.920 -4.974  55.917  1.00 27.80 ?  632 HOH A O   1 
HETATM 4214 O  O   . HOH H 4 .   ? 36.863 -6.667  56.374  1.00 31.07 ?  633 HOH A O   1 
HETATM 4215 O  O   . HOH H 4 .   ? 66.895 4.062   47.238  1.00 30.73 ?  634 HOH A O   1 
HETATM 4216 O  O   . HOH H 4 .   ? 25.520 17.010  51.629  1.00 35.35 ?  635 HOH A O   1 
HETATM 4217 O  O   . HOH H 4 .   ? 44.721 25.591  45.289  1.00 38.22 ?  636 HOH A O   1 
HETATM 4218 O  O   . HOH H 4 .   ? 43.601 22.896  44.372  1.00 33.91 ?  637 HOH A O   1 
HETATM 4219 O  O   . HOH H 4 .   ? 35.907 21.059  64.259  1.00 28.17 ?  638 HOH A O   1 
HETATM 4220 O  O   . HOH H 4 .   ? 60.563 -6.276  60.673  1.00 41.62 ?  639 HOH A O   1 
HETATM 4221 O  O   . HOH H 4 .   ? 30.126 1.576   70.160  1.00 34.59 ?  640 HOH A O   1 
HETATM 4222 O  O   . HOH H 4 .   ? 32.902 1.934   41.260  1.00 33.34 ?  641 HOH A O   1 
HETATM 4223 O  O   . HOH H 4 .   ? 64.246 20.621  53.975  1.00 31.95 ?  642 HOH A O   1 
HETATM 4224 O  O   . HOH H 4 .   ? 41.117 10.848  64.747  1.00 31.30 ?  643 HOH A O   1 
HETATM 4225 O  O   . HOH H 4 .   ? 59.285 -3.778  40.216  1.00 26.90 ?  644 HOH A O   1 
HETATM 4226 O  O   . HOH H 4 .   ? 59.432 8.118   69.636  1.00 38.69 ?  645 HOH A O   1 
HETATM 4227 O  O   . HOH H 4 .   ? 29.729 20.137  61.254  1.00 31.99 ?  646 HOH A O   1 
HETATM 4228 O  O   . HOH H 4 .   ? 54.957 20.973  67.133  1.00 23.56 ?  647 HOH A O   1 
HETATM 4229 O  O   . HOH H 4 .   ? 34.995 -4.713  53.616  1.00 32.64 ?  648 HOH A O   1 
HETATM 4230 O  O   . HOH H 4 .   ? 46.500 17.785  70.378  1.00 19.09 ?  649 HOH A O   1 
HETATM 4231 O  O   . HOH H 4 .   ? 31.702 23.475  50.171  1.00 41.15 ?  650 HOH A O   1 
HETATM 4232 O  O   . HOH H 4 .   ? 48.987 -14.519 49.197  1.00 20.57 ?  651 HOH A O   1 
HETATM 4233 O  O   . HOH H 4 .   ? 56.622 2.482   37.451  1.00 33.89 ?  652 HOH A O   1 
HETATM 4234 O  O   . HOH H 4 .   ? 53.534 24.687  64.824  1.00 27.48 ?  653 HOH A O   1 
HETATM 4235 O  O   . HOH H 4 .   ? 40.500 -9.891  62.060  1.00 41.42 ?  654 HOH A O   1 
HETATM 4236 O  O   . HOH H 4 .   ? 52.099 -11.353 56.254  1.00 34.86 ?  655 HOH A O   1 
HETATM 4237 O  O   . HOH H 4 .   ? 63.844 2.090   66.424  1.00 35.38 ?  656 HOH A O   1 
HETATM 4238 O  O   . HOH H 4 .   ? 59.885 7.526   38.291  1.00 32.81 ?  657 HOH A O   1 
HETATM 4239 O  O   . HOH H 4 .   ? 45.093 21.077  33.257  1.00 42.13 ?  658 HOH A O   1 
HETATM 4240 O  O   . HOH H 4 .   ? 44.719 25.762  52.899  1.00 32.93 ?  659 HOH A O   1 
HETATM 4241 O  O   . HOH H 4 .   ? 65.040 13.191  66.387  1.00 43.77 ?  660 HOH A O   1 
HETATM 4242 O  O   . HOH H 4 .   ? 63.031 27.160  46.534  1.00 41.36 ?  661 HOH A O   1 
HETATM 4243 O  O   . HOH H 4 .   ? 35.473 16.573  39.744  1.00 35.50 ?  662 HOH A O   1 
HETATM 4244 O  O   . HOH H 4 .   ? 37.506 -4.855  54.777  1.00 28.05 ?  663 HOH A O   1 
HETATM 4245 O  O   . HOH H 4 .   ? 50.747 6.030   74.226  1.00 41.22 ?  664 HOH A O   1 
HETATM 4246 O  O   . HOH H 4 .   ? 61.182 -4.466  41.877  1.00 41.67 ?  665 HOH A O   1 
HETATM 4247 O  O   . HOH H 4 .   ? 29.018 9.829   41.865  1.00 37.89 ?  666 HOH A O   1 
HETATM 4248 O  O   . HOH H 4 .   ? 63.366 6.488   61.841  1.00 33.19 ?  667 HOH A O   1 
HETATM 4249 O  O   . HOH H 4 .   ? 49.900 -14.721 55.655  1.00 41.47 ?  668 HOH A O   1 
HETATM 4250 O  O   . HOH H 4 .   ? 35.658 13.261  40.325  1.00 35.37 ?  669 HOH A O   1 
HETATM 4251 O  O   . HOH H 4 .   ? 39.317 -11.656 61.136  1.00 36.50 ?  670 HOH A O   1 
HETATM 4252 O  O   . HOH H 4 .   ? 58.290 2.189   59.235  1.00 15.15 ?  671 HOH A O   1 
HETATM 4253 O  O   . HOH H 4 .   ? 60.525 22.404  46.603  1.00 34.76 ?  672 HOH A O   1 
HETATM 4254 O  O   . HOH H 4 .   ? 60.445 29.397  49.677  1.00 36.94 ?  673 HOH A O   1 
HETATM 4255 O  O   . HOH H 4 .   ? 63.887 22.882  55.781  1.00 35.66 ?  674 HOH A O   1 
HETATM 4256 O  O   . HOH H 4 .   ? 64.270 21.294  48.856  1.00 37.93 ?  675 HOH A O   1 
HETATM 4257 O  O   . HOH H 4 .   ? 57.573 -11.158 52.208  1.00 36.73 ?  676 HOH A O   1 
HETATM 4258 O  O   . HOH H 4 .   ? 52.954 5.249   71.048  1.00 34.91 ?  677 HOH A O   1 
HETATM 4259 O  O   . HOH H 4 .   ? 33.063 -6.997  52.631  1.00 35.40 ?  678 HOH A O   1 
HETATM 4260 O  O   . HOH H 4 .   ? 64.608 10.336  61.196  1.00 34.25 ?  679 HOH A O   1 
HETATM 4261 O  O   . HOH H 4 .   ? 64.370 20.121  60.938  1.00 42.47 ?  680 HOH A O   1 
HETATM 4262 O  O   . HOH H 4 .   ? 35.554 9.458   36.942  1.00 33.71 ?  681 HOH A O   1 
HETATM 4263 O  O   . HOH H 4 .   ? 57.543 30.876  49.852  1.00 39.46 ?  682 HOH A O   1 
HETATM 4264 O  O   . HOH H 4 .   ? 51.281 22.362  67.741  1.00 33.91 ?  683 HOH A O   1 
HETATM 4265 O  O   . HOH H 4 .   ? 50.087 29.250  60.404  1.00 36.21 ?  684 HOH A O   1 
HETATM 4266 O  O   . HOH H 4 .   ? 48.353 -5.452  38.618  1.00 33.32 ?  685 HOH A O   1 
HETATM 4267 O  O   . HOH H 4 .   ? 33.785 -3.201  55.184  1.00 26.60 ?  686 HOH A O   1 
HETATM 4268 O  O   . HOH H 4 .   ? 32.406 17.303  64.817  1.00 30.98 ?  687 HOH A O   1 
HETATM 4269 O  O   . HOH H 4 .   ? 58.307 8.232   76.246  1.00 41.98 ?  688 HOH A O   1 
HETATM 4270 O  O   . HOH H 4 .   ? 44.022 -10.869 40.038  1.00 27.68 ?  689 HOH A O   1 
HETATM 4271 O  O   . HOH H 4 .   ? 38.772 -7.049  45.564  1.00 38.24 ?  690 HOH A O   1 
HETATM 4272 O  O   . HOH H 4 .   ? 50.720 31.535  48.794  1.00 41.21 ?  691 HOH A O   1 
HETATM 4273 O  O   . HOH H 4 .   ? 43.692 18.942  69.564  1.00 35.56 ?  692 HOH A O   1 
HETATM 4274 O  O   . HOH H 4 .   ? 51.654 -0.083  57.279  1.00 27.07 ?  693 HOH A O   1 
HETATM 4275 O  O   . HOH H 4 .   ? 51.003 20.232  69.666  1.00 33.77 ?  694 HOH A O   1 
HETATM 4276 O  O   . HOH H 4 .   ? 52.994 22.255  65.842  1.00 25.02 ?  695 HOH A O   1 
HETATM 4277 O  O   . HOH H 4 .   ? 40.906 -2.808  35.277  1.00 32.67 ?  696 HOH A O   1 
HETATM 4278 O  O   . HOH H 4 .   ? 64.259 8.188   40.552  1.00 36.46 ?  697 HOH A O   1 
HETATM 4279 O  O   . HOH H 4 .   ? 42.644 24.533  33.094  1.00 46.29 ?  698 HOH A O   1 
HETATM 4280 O  O   . HOH H 4 .   ? 37.046 2.948   35.449  1.00 33.08 ?  699 HOH A O   1 
HETATM 4281 O  O   . HOH H 4 .   ? 45.407 -14.974 51.799  1.00 36.83 ?  700 HOH A O   1 
HETATM 4282 O  O   . HOH H 4 .   ? 55.171 11.914  35.251  1.00 32.99 ?  701 HOH A O   1 
HETATM 4283 O  O   . HOH H 4 .   ? 67.191 5.197   44.703  1.00 43.91 ?  702 HOH A O   1 
HETATM 4284 O  O   . HOH H 4 .   ? 44.945 22.911  67.924  1.00 36.35 ?  703 HOH A O   1 
HETATM 4285 O  O   . HOH H 4 .   ? 62.596 28.922  48.286  1.00 36.01 ?  704 HOH A O   1 
HETATM 4286 O  O   . HOH H 4 .   ? 63.472 -6.562  62.268  1.00 31.79 ?  705 HOH A O   1 
HETATM 4287 O  O   . HOH H 4 .   ? 65.698 0.095   45.215  1.00 40.45 ?  706 HOH A O   1 
HETATM 4288 O  O   . HOH H 4 .   ? 49.378 31.671  54.767  1.00 44.07 ?  707 HOH A O   1 
HETATM 4289 O  O   . HOH H 4 .   ? 31.667 -1.685  54.119  1.00 32.39 ?  708 HOH A O   1 
HETATM 4290 O  O   . HOH H 4 .   ? 42.121 16.851  69.459  1.00 42.89 ?  709 HOH A O   1 
HETATM 4291 O  O   . HOH H 4 .   ? 42.054 9.227   63.302  1.00 26.53 ?  710 HOH A O   1 
HETATM 4292 O  O   . HOH H 4 .   ? 63.508 19.994  58.736  1.00 43.97 ?  711 HOH A O   1 
HETATM 4293 O  O   . HOH H 4 .   ? 42.928 6.420   64.013  1.00 32.83 ?  712 HOH A O   1 
HETATM 4294 O  O   . HOH H 4 .   ? 38.655 -1.173  34.979  1.00 32.35 ?  713 HOH A O   1 
HETATM 4295 O  O   . HOH H 4 .   ? 62.996 9.104   65.119  1.00 39.17 ?  714 HOH A O   1 
HETATM 4296 O  O   . HOH H 4 .   ? 65.692 6.651   43.609  1.00 41.44 ?  715 HOH A O   1 
HETATM 4297 O  O   . HOH H 4 .   ? 35.424 5.004   36.160  1.00 37.90 ?  716 HOH A O   1 
HETATM 4298 O  O   . HOH H 4 .   ? 58.844 14.809  35.459  1.00 40.28 ?  717 HOH A O   1 
HETATM 4299 O  O   . HOH H 4 .   ? 51.119 -7.175  39.224  1.00 40.93 ?  718 HOH A O   1 
HETATM 4300 O  O   . HOH H 4 .   ? 41.430 9.863   67.558  1.00 36.78 ?  719 HOH A O   1 
HETATM 4301 O  O   . HOH H 4 .   ? 63.452 18.759  56.390  1.00 38.87 ?  720 HOH A O   1 
HETATM 4302 O  O   . HOH H 4 .   ? 62.751 11.802  67.238  1.00 37.69 ?  721 HOH A O   1 
HETATM 4303 O  O   . HOH H 4 .   ? 29.658 -3.268  53.190  1.00 42.70 ?  722 HOH A O   1 
HETATM 4304 O  O   . HOH H 4 .   ? 27.307 -3.433  53.467  1.00 49.63 ?  723 HOH A O   1 
HETATM 4305 O  O   . HOH I 4 .   ? 40.116 -5.209  76.844  1.00 37.05 ?  501 HOH B O   1 
HETATM 4306 O  O   . HOH I 4 .   ? 33.899 -20.254 87.741  1.00 41.19 ?  502 HOH B O   1 
HETATM 4307 O  O   . HOH I 4 .   ? 40.219 -18.042 63.846  1.00 26.46 ?  503 HOH B O   1 
HETATM 4308 O  O   . HOH I 4 .   ? 61.115 -19.984 74.044  1.00 18.40 ?  504 HOH B O   1 
HETATM 4309 O  O   . HOH I 4 .   ? 65.457 -14.562 56.371  1.00 31.75 ?  505 HOH B O   1 
HETATM 4310 O  O   . HOH I 4 .   ? 46.856 2.772   87.642  1.00 34.27 ?  506 HOH B O   1 
HETATM 4311 O  O   . HOH I 4 .   ? 50.879 -26.231 67.560  1.00 28.12 ?  507 HOH B O   1 
HETATM 4312 O  O   . HOH I 4 .   ? 67.135 -20.351 84.793  1.00 21.80 ?  508 HOH B O   1 
HETATM 4313 O  O   . HOH I 4 .   ? 64.453 5.569   80.322  1.00 40.72 ?  509 HOH B O   1 
HETATM 4314 O  O   . HOH I 4 .   ? 65.806 -13.685 78.496  1.00 25.14 ?  510 HOH B O   1 
HETATM 4315 O  O   . HOH I 4 .   ? 61.711 4.546   69.684  1.00 28.89 ?  511 HOH B O   1 
HETATM 4316 O  O   . HOH I 4 .   ? 45.541 -9.261  96.895  1.00 34.18 ?  512 HOH B O   1 
HETATM 4317 O  O   . HOH I 4 .   ? 51.729 -25.667 92.389  1.00 27.15 ?  513 HOH B O   1 
HETATM 4318 O  O   . HOH I 4 .   ? 74.066 -19.327 87.396  1.00 26.98 ?  514 HOH B O   1 
HETATM 4319 O  O   . HOH I 4 .   ? 69.395 -9.630  63.467  1.00 36.38 ?  515 HOH B O   1 
HETATM 4320 O  O   . HOH I 4 .   ? 57.353 -25.899 73.054  1.00 26.37 ?  516 HOH B O   1 
HETATM 4321 O  O   . HOH I 4 .   ? 42.991 -0.217  66.074  1.00 33.92 ?  517 HOH B O   1 
HETATM 4322 O  O   . HOH I 4 .   ? 48.340 -19.279 92.244  1.00 21.98 ?  518 HOH B O   1 
HETATM 4323 O  O   . HOH I 4 .   ? 61.591 -8.165  88.794  1.00 20.47 ?  519 HOH B O   1 
HETATM 4324 O  O   . HOH I 4 .   ? 59.802 -27.594 81.424  1.00 27.04 ?  520 HOH B O   1 
HETATM 4325 O  O   . HOH I 4 .   ? 65.757 -25.890 87.257  1.00 31.38 ?  521 HOH B O   1 
HETATM 4326 O  O   . HOH I 4 .   ? 71.858 -11.610 67.640  1.00 35.08 ?  522 HOH B O   1 
HETATM 4327 O  O   . HOH I 4 .   ? 60.291 -0.080  58.902  1.00 29.55 ?  523 HOH B O   1 
HETATM 4328 O  O   . HOH I 4 .   ? 59.955 -2.659  87.433  1.00 28.56 ?  524 HOH B O   1 
HETATM 4329 O  O   . HOH I 4 .   ? 56.170 -22.834 69.958  1.00 23.26 ?  525 HOH B O   1 
HETATM 4330 O  O   . HOH I 4 .   ? 34.560 -3.689  71.894  1.00 32.23 ?  526 HOH B O   1 
HETATM 4331 O  O   . HOH I 4 .   ? 69.576 -4.087  76.459  1.00 22.71 ?  527 HOH B O   1 
HETATM 4332 O  O   . HOH I 4 .   ? 40.451 -28.499 83.150  1.00 28.09 ?  528 HOH B O   1 
HETATM 4333 O  O   . HOH I 4 .   ? 68.550 -0.261  75.125  1.00 29.33 ?  529 HOH B O   1 
HETATM 4334 O  O   . HOH I 4 .   ? 36.524 -19.373 74.949  1.00 25.46 ?  530 HOH B O   1 
HETATM 4335 O  O   . HOH I 4 .   ? 41.935 -33.194 78.581  1.00 31.22 ?  531 HOH B O   1 
HETATM 4336 O  O   . HOH I 4 .   ? 39.519 -11.235 63.676  1.00 32.30 ?  532 HOH B O   1 
HETATM 4337 O  O   . HOH I 4 .   ? 53.692 4.183   77.075  1.00 34.39 ?  533 HOH B O   1 
HETATM 4338 O  O   . HOH I 4 .   ? 37.650 -7.191  88.312  1.00 36.43 ?  534 HOH B O   1 
HETATM 4339 O  O   . HOH I 4 .   ? 46.753 -1.363  80.833  1.00 26.06 ?  535 HOH B O   1 
HETATM 4340 O  O   . HOH I 4 .   ? 55.096 -4.365  92.701  1.00 26.51 ?  536 HOH B O   1 
HETATM 4341 O  O   . HOH I 4 .   ? 63.725 -20.051 63.856  1.00 23.14 ?  537 HOH B O   1 
HETATM 4342 O  O   . HOH I 4 .   ? 51.760 -13.716 99.360  1.00 31.97 ?  538 HOH B O   1 
HETATM 4343 O  O   . HOH I 4 .   ? 69.441 -4.606  85.316  1.00 24.75 ?  539 HOH B O   1 
HETATM 4344 O  O   . HOH I 4 .   ? 66.312 -10.948 58.667  1.00 36.24 ?  540 HOH B O   1 
HETATM 4345 O  O   . HOH I 4 .   ? 56.901 0.004   62.408  1.00 22.32 ?  541 HOH B O   1 
HETATM 4346 O  O   . HOH I 4 .   ? 37.719 -11.974 85.974  1.00 26.17 ?  542 HOH B O   1 
HETATM 4347 O  O   . HOH I 4 .   ? 56.443 -32.852 77.756  1.00 33.81 ?  543 HOH B O   1 
HETATM 4348 O  O   . HOH I 4 .   ? 45.289 1.030   80.955  1.00 32.53 ?  544 HOH B O   1 
HETATM 4349 O  O   . HOH I 4 .   ? 32.968 2.068   69.917  1.00 33.03 ?  545 HOH B O   1 
HETATM 4350 O  O   . HOH I 4 .   ? 33.685 -15.177 79.381  1.00 24.80 ?  546 HOH B O   1 
HETATM 4351 O  O   . HOH I 4 .   ? 62.828 -27.470 84.616  1.00 30.58 ?  547 HOH B O   1 
HETATM 4352 O  O   . HOH I 4 .   ? 41.248 -23.971 87.434  1.00 27.91 ?  548 HOH B O   1 
HETATM 4353 O  O   . HOH I 4 .   ? 60.429 -26.169 83.766  1.00 28.40 ?  549 HOH B O   1 
HETATM 4354 O  O   . HOH I 4 .   ? 40.355 -7.574  63.232  1.00 31.63 ?  550 HOH B O   1 
HETATM 4355 O  O   . HOH I 4 .   ? 55.846 -12.186 55.625  1.00 32.71 ?  551 HOH B O   1 
HETATM 4356 O  O   . HOH I 4 .   ? 45.614 -0.438  83.619  1.00 33.70 ?  552 HOH B O   1 
HETATM 4357 O  O   . HOH I 4 .   ? 66.805 3.584   80.263  1.00 28.70 ?  553 HOH B O   1 
HETATM 4358 O  O   . HOH I 4 .   ? 53.742 -15.045 51.341  1.00 32.66 ?  554 HOH B O   1 
HETATM 4359 O  O   . HOH I 4 .   ? 65.956 -21.189 95.882  1.00 26.59 ?  555 HOH B O   1 
HETATM 4360 O  O   . HOH I 4 .   ? 69.604 -5.582  88.574  1.00 31.38 ?  556 HOH B O   1 
HETATM 4361 O  O   . HOH I 4 .   ? 76.348 -13.273 68.953  1.00 35.13 ?  557 HOH B O   1 
HETATM 4362 O  O   . HOH I 4 .   ? 77.224 -10.809 77.719  1.00 31.86 ?  558 HOH B O   1 
HETATM 4363 O  O   . HOH I 4 .   ? 75.676 -16.779 88.912  1.00 28.13 ?  559 HOH B O   1 
HETATM 4364 O  O   . HOH I 4 .   ? 59.818 -20.248 79.230  1.00 18.43 ?  560 HOH B O   1 
HETATM 4365 O  O   . HOH I 4 .   ? 42.460 -11.083 93.095  1.00 30.38 ?  561 HOH B O   1 
HETATM 4366 O  O   . HOH I 4 .   ? 45.734 -18.609 95.156  1.00 26.87 ?  562 HOH B O   1 
HETATM 4367 O  O   . HOH I 4 .   ? 46.640 -1.830  57.651  1.00 25.25 ?  563 HOH B O   1 
HETATM 4368 O  O   . HOH I 4 .   ? 47.552 -20.552 95.909  1.00 31.20 ?  564 HOH B O   1 
HETATM 4369 O  O   . HOH I 4 .   ? 70.704 -11.851 64.936  1.00 28.93 ?  565 HOH B O   1 
HETATM 4370 O  O   . HOH I 4 .   ? 70.331 -10.285 71.678  1.00 26.70 ?  566 HOH B O   1 
HETATM 4371 O  O   . HOH I 4 .   ? 71.549 -15.210 78.646  1.00 19.11 ?  567 HOH B O   1 
HETATM 4372 O  O   . HOH I 4 .   ? 41.182 -4.906  62.275  1.00 18.94 ?  568 HOH B O   1 
HETATM 4373 O  O   . HOH I 4 .   ? 73.083 -18.686 89.916  1.00 26.65 ?  569 HOH B O   1 
HETATM 4374 O  O   . HOH I 4 .   ? 58.076 -3.569  63.163  1.00 33.22 ?  570 HOH B O   1 
HETATM 4375 O  O   . HOH I 4 .   ? 49.049 -28.996 88.312  1.00 32.02 ?  571 HOH B O   1 
HETATM 4376 O  O   . HOH I 4 .   ? 39.228 -22.127 69.823  1.00 19.59 ?  572 HOH B O   1 
HETATM 4377 O  O   . HOH I 4 .   ? 52.941 -22.062 61.535  1.00 37.31 ?  573 HOH B O   1 
HETATM 4378 O  O   . HOH I 4 .   ? 73.600 -18.235 72.561  1.00 35.12 ?  574 HOH B O   1 
HETATM 4379 O  O   . HOH I 4 .   ? 48.751 -7.692  95.663  1.00 25.23 ?  575 HOH B O   1 
HETATM 4380 O  O   . HOH I 4 .   ? 57.941 -10.734 78.219  1.00 23.27 ?  576 HOH B O   1 
HETATM 4381 O  O   . HOH I 4 .   ? 60.563 4.604   77.973  1.00 27.83 ?  577 HOH B O   1 
HETATM 4382 O  O   . HOH I 4 .   ? 65.623 -0.252  88.933  1.00 39.78 ?  578 HOH B O   1 
HETATM 4383 O  O   . HOH I 4 .   ? 49.871 -2.290  95.095  1.00 21.99 ?  579 HOH B O   1 
HETATM 4384 O  O   . HOH I 4 .   ? 67.019 -16.591 74.753  1.00 23.85 ?  580 HOH B O   1 
HETATM 4385 O  O   . HOH I 4 .   ? 45.930 -20.243 63.709  1.00 28.27 ?  581 HOH B O   1 
HETATM 4386 O  O   . HOH I 4 .   ? 61.916 -19.738 77.042  1.00 22.57 ?  582 HOH B O   1 
HETATM 4387 O  O   . HOH I 4 .   ? 52.248 2.742   71.627  1.00 34.17 ?  583 HOH B O   1 
HETATM 4388 O  O   . HOH I 4 .   ? 58.093 -12.708 57.193  1.00 25.11 ?  584 HOH B O   1 
HETATM 4389 O  O   . HOH I 4 .   ? 63.946 -18.132 75.729  1.00 29.83 ?  585 HOH B O   1 
HETATM 4390 O  O   . HOH I 4 .   ? 53.906 -12.605 51.562  1.00 36.70 ?  586 HOH B O   1 
HETATM 4391 O  O   . HOH I 4 .   ? 45.921 -14.369 61.284  1.00 24.38 ?  587 HOH B O   1 
HETATM 4392 O  O   . HOH I 4 .   ? 43.197 -17.829 95.010  1.00 37.60 ?  588 HOH B O   1 
HETATM 4393 O  O   . HOH I 4 .   ? 45.143 -26.860 76.573  1.00 26.17 ?  589 HOH B O   1 
HETATM 4394 O  O   . HOH I 4 .   ? 50.461 -5.386  94.933  1.00 28.06 ?  590 HOH B O   1 
HETATM 4395 O  O   . HOH I 4 .   ? 44.561 -10.293 65.308  1.00 21.38 ?  591 HOH B O   1 
HETATM 4396 O  O   . HOH I 4 .   ? 52.111 4.504   91.212  1.00 43.10 ?  592 HOH B O   1 
HETATM 4397 O  O   . HOH I 4 .   ? 37.737 -11.715 74.247  1.00 30.88 ?  593 HOH B O   1 
HETATM 4398 O  O   . HOH I 4 .   ? 36.242 -15.753 85.551  1.00 28.42 ?  594 HOH B O   1 
HETATM 4399 O  O   . HOH I 4 .   ? 37.219 -11.680 67.116  1.00 34.19 ?  595 HOH B O   1 
HETATM 4400 O  O   . HOH I 4 .   ? 50.294 -20.159 59.701  1.00 31.59 ?  596 HOH B O   1 
HETATM 4401 O  O   . HOH I 4 .   ? 46.563 1.511   91.893  1.00 20.62 ?  597 HOH B O   1 
HETATM 4402 O  O   . HOH I 4 .   ? 52.776 -29.815 84.532  1.00 25.16 ?  598 HOH B O   1 
HETATM 4403 O  O   . HOH I 4 .   ? 49.243 -18.896 100.555 1.00 37.79 ?  599 HOH B O   1 
HETATM 4404 O  O   . HOH I 4 .   ? 36.050 -10.376 69.893  1.00 31.48 ?  600 HOH B O   1 
HETATM 4405 O  O   . HOH I 4 .   ? 52.145 -9.105  58.799  1.00 27.13 ?  601 HOH B O   1 
HETATM 4406 O  O   . HOH I 4 .   ? 59.199 -31.508 93.030  1.00 32.01 ?  602 HOH B O   1 
HETATM 4407 O  O   . HOH I 4 .   ? 70.855 -15.272 81.367  1.00 17.30 ?  603 HOH B O   1 
HETATM 4408 O  O   . HOH I 4 .   ? 57.095 2.625   87.336  1.00 34.47 ?  604 HOH B O   1 
HETATM 4409 O  O   . HOH I 4 .   ? 53.548 5.143   68.202  1.00 32.93 ?  605 HOH B O   1 
HETATM 4410 O  O   . HOH I 4 .   ? 49.327 -31.643 72.960  1.00 38.98 ?  606 HOH B O   1 
HETATM 4411 O  O   . HOH I 4 .   ? 71.068 -8.837  78.562  1.00 18.08 ?  607 HOH B O   1 
HETATM 4412 O  O   . HOH I 4 .   ? 67.535 -12.152 69.817  1.00 19.57 ?  608 HOH B O   1 
HETATM 4413 O  O   . HOH I 4 .   ? 67.103 -10.574 66.564  1.00 17.50 ?  609 HOH B O   1 
HETATM 4414 O  O   . HOH I 4 .   ? 39.048 -7.794  91.899  1.00 42.89 ?  610 HOH B O   1 
HETATM 4415 O  O   . HOH I 4 .   ? 56.819 -30.568 94.409  1.00 38.76 ?  611 HOH B O   1 
HETATM 4416 O  O   . HOH I 4 .   ? 64.041 -4.926  93.416  1.00 32.23 ?  612 HOH B O   1 
HETATM 4417 O  O   . HOH I 4 .   ? 64.434 -5.859  64.674  1.00 24.58 ?  613 HOH B O   1 
HETATM 4418 O  O   . HOH I 4 .   ? 38.051 -25.560 88.206  1.00 34.16 ?  614 HOH B O   1 
HETATM 4419 O  O   . HOH I 4 .   ? 62.004 -23.590 83.718  1.00 24.72 ?  615 HOH B O   1 
HETATM 4420 O  O   . HOH I 4 .   ? 45.610 -27.475 74.052  1.00 21.83 ?  616 HOH B O   1 
HETATM 4421 O  O   . HOH I 4 .   ? 62.643 -1.393  86.835  1.00 31.97 ?  617 HOH B O   1 
HETATM 4422 O  O   . HOH I 4 .   ? 39.954 -7.013  75.178  1.00 28.41 ?  618 HOH B O   1 
HETATM 4423 O  O   . HOH I 4 .   ? 51.944 -32.243 78.686  1.00 29.40 ?  619 HOH B O   1 
HETATM 4424 O  O   . HOH I 4 .   ? 46.716 3.622   78.093  1.00 28.46 ?  620 HOH B O   1 
HETATM 4425 O  O   . HOH I 4 .   ? 75.357 -8.489  73.813  1.00 29.39 ?  621 HOH B O   1 
HETATM 4426 O  O   . HOH I 4 .   ? 61.745 -28.983 80.011  1.00 40.68 ?  622 HOH B O   1 
HETATM 4427 O  O   . HOH I 4 .   ? 50.878 -29.190 97.874  1.00 32.73 ?  623 HOH B O   1 
HETATM 4428 O  O   . HOH I 4 .   ? 55.748 -12.741 69.418  1.00 16.45 ?  624 HOH B O   1 
HETATM 4429 O  O   . HOH I 4 .   ? 46.434 4.059   65.451  1.00 33.16 ?  625 HOH B O   1 
HETATM 4430 O  O   . HOH I 4 .   ? 49.284 -24.071 63.520  1.00 26.74 ?  626 HOH B O   1 
HETATM 4431 O  O   . HOH I 4 .   ? 57.847 -11.404 70.446  1.00 15.88 ?  627 HOH B O   1 
HETATM 4432 O  O   . HOH I 4 .   ? 56.664 6.325   83.210  1.00 33.62 ?  628 HOH B O   1 
HETATM 4433 O  O   . HOH I 4 .   ? 42.712 -16.190 91.791  1.00 31.03 ?  629 HOH B O   1 
HETATM 4434 O  O   . HOH I 4 .   ? 61.176 -17.732 79.194  1.00 18.53 ?  630 HOH B O   1 
HETATM 4435 O  O   . HOH I 4 .   ? 49.224 3.271   67.228  1.00 20.29 ?  631 HOH B O   1 
HETATM 4436 O  O   . HOH I 4 .   ? 64.166 -32.929 87.804  1.00 42.46 ?  632 HOH B O   1 
HETATM 4437 O  O   . HOH I 4 .   ? 60.373 -12.559 70.178  1.00 17.31 ?  633 HOH B O   1 
HETATM 4438 O  O   . HOH I 4 .   ? 79.260 -13.516 86.811  1.00 33.25 ?  634 HOH B O   1 
HETATM 4439 O  O   . HOH I 4 .   ? 36.250 -24.602 78.536  1.00 26.15 ?  635 HOH B O   1 
HETATM 4440 O  O   . HOH I 4 .   ? 72.312 -1.605  67.593  1.00 39.88 ?  636 HOH B O   1 
HETATM 4441 O  O   . HOH I 4 .   ? 62.849 -9.044  92.199  1.00 19.81 ?  637 HOH B O   1 
HETATM 4442 O  O   . HOH I 4 .   ? 70.805 -3.991  74.386  1.00 33.07 ?  638 HOH B O   1 
HETATM 4443 O  O   . HOH I 4 .   ? 39.033 -26.918 70.736  1.00 28.66 ?  639 HOH B O   1 
HETATM 4444 O  O   . HOH I 4 .   ? 66.857 -17.016 96.227  1.00 36.49 ?  640 HOH B O   1 
HETATM 4445 O  O   . HOH I 4 .   ? 42.589 -22.346 90.578  1.00 35.67 ?  641 HOH B O   1 
HETATM 4446 O  O   . HOH I 4 .   ? 55.161 -11.021 96.585  1.00 27.94 ?  642 HOH B O   1 
HETATM 4447 O  O   . HOH I 4 .   ? 46.306 -30.231 88.316  1.00 50.71 ?  643 HOH B O   1 
HETATM 4448 O  O   . HOH I 4 .   ? 56.085 -21.172 61.399  1.00 34.62 ?  644 HOH B O   1 
HETATM 4449 O  O   . HOH I 4 .   ? 43.331 0.804   68.874  1.00 30.50 ?  645 HOH B O   1 
HETATM 4450 O  O   . HOH I 4 .   ? 58.902 -21.079 97.192  1.00 28.44 ?  646 HOH B O   1 
HETATM 4451 O  O   . HOH I 4 .   ? 48.623 -8.396  91.211  1.00 17.10 ?  647 HOH B O   1 
HETATM 4452 O  O   . HOH I 4 .   ? 78.273 -16.734 73.922  1.00 39.11 ?  648 HOH B O   1 
HETATM 4453 O  O   . HOH I 4 .   ? 49.858 -9.262  93.460  1.00 18.52 ?  649 HOH B O   1 
HETATM 4454 O  O   . HOH I 4 .   ? 49.125 -8.333  59.412  1.00 30.86 ?  650 HOH B O   1 
HETATM 4455 O  O   . HOH I 4 .   ? 78.593 -15.440 81.758  1.00 22.98 ?  651 HOH B O   1 
HETATM 4456 O  O   . HOH I 4 .   ? 43.598 2.154   64.770  1.00 34.92 ?  652 HOH B O   1 
HETATM 4457 O  O   . HOH I 4 .   ? 39.082 -9.630  75.976  1.00 35.30 ?  653 HOH B O   1 
HETATM 4458 O  O   . HOH I 4 .   ? 33.946 -12.936 74.344  1.00 34.87 ?  654 HOH B O   1 
HETATM 4459 O  O   . HOH I 4 .   ? 46.040 -18.454 61.575  1.00 27.89 ?  655 HOH B O   1 
HETATM 4460 O  O   . HOH I 4 .   ? 68.606 -12.441 95.007  1.00 31.34 ?  656 HOH B O   1 
HETATM 4461 O  O   . HOH I 4 .   ? 50.987 -13.775 57.898  1.00 28.51 ?  657 HOH B O   1 
HETATM 4462 O  O   . HOH I 4 .   ? 54.807 -33.036 82.553  1.00 37.08 ?  658 HOH B O   1 
HETATM 4463 O  O   . HOH I 4 .   ? 38.666 -24.524 75.898  1.00 26.16 ?  659 HOH B O   1 
HETATM 4464 O  O   . HOH I 4 .   ? 49.221 -32.325 80.353  1.00 27.22 ?  660 HOH B O   1 
HETATM 4465 O  O   . HOH I 4 .   ? 63.995 -21.803 67.519  1.00 34.14 ?  661 HOH B O   1 
HETATM 4466 O  O   . HOH I 4 .   ? 46.904 -30.017 74.365  1.00 31.71 ?  662 HOH B O   1 
HETATM 4467 O  O   . HOH I 4 .   ? 62.420 -18.465 54.671  1.00 18.19 ?  663 HOH B O   1 
HETATM 4468 O  O   . HOH I 4 .   ? 32.995 -18.756 84.806  1.00 36.60 ?  664 HOH B O   1 
HETATM 4469 O  O   . HOH I 4 .   ? 48.644 -26.399 91.258  1.00 26.76 ?  665 HOH B O   1 
HETATM 4470 O  O   . HOH I 4 .   ? 57.534 -9.548  96.692  1.00 30.87 ?  666 HOH B O   1 
HETATM 4471 O  O   . HOH I 4 .   ? 49.547 1.687   69.613  1.00 24.88 ?  667 HOH B O   1 
HETATM 4472 O  O   . HOH I 4 .   ? 67.363 -24.305 84.451  1.00 35.67 ?  668 HOH B O   1 
HETATM 4473 O  O   . HOH I 4 .   ? 64.514 3.432   74.081  1.00 33.48 ?  669 HOH B O   1 
HETATM 4474 O  O   . HOH I 4 .   ? 64.467 -25.087 84.450  1.00 30.15 ?  670 HOH B O   1 
HETATM 4475 O  O   . HOH I 4 .   ? 63.060 -25.814 82.241  1.00 23.78 ?  671 HOH B O   1 
HETATM 4476 O  O   . HOH I 4 .   ? 61.473 -24.027 66.898  1.00 41.49 ?  672 HOH B O   1 
HETATM 4477 O  O   . HOH I 4 .   ? 65.952 -22.397 82.840  1.00 23.27 ?  673 HOH B O   1 
HETATM 4478 O  O   . HOH I 4 .   ? 58.406 6.539   78.088  1.00 41.02 ?  674 HOH B O   1 
HETATM 4479 O  O   . HOH I 4 .   ? 58.526 -4.438  95.145  1.00 35.65 ?  675 HOH B O   1 
HETATM 4480 O  O   . HOH I 4 .   ? 69.984 -10.883 68.701  1.00 28.67 ?  676 HOH B O   1 
HETATM 4481 O  O   . HOH I 4 .   ? 37.993 -12.711 92.730  1.00 36.91 ?  677 HOH B O   1 
HETATM 4482 O  O   . HOH I 4 .   ? 57.349 -14.696 98.085  1.00 42.80 ?  678 HOH B O   1 
HETATM 4483 O  O   . HOH I 4 .   ? 55.834 -3.404  55.484  1.00 21.45 ?  679 HOH B O   1 
HETATM 4484 O  O   . HOH I 4 .   ? 55.464 -30.795 85.400  1.00 30.62 ?  680 HOH B O   1 
HETATM 4485 O  O   . HOH I 4 .   ? 41.703 -29.006 70.195  1.00 32.67 ?  681 HOH B O   1 
HETATM 4486 O  O   . HOH I 4 .   ? 59.936 -11.895 52.600  1.00 38.83 ?  682 HOH B O   1 
HETATM 4487 O  O   . HOH I 4 .   ? 53.491 -9.057  97.579  1.00 36.14 ?  683 HOH B O   1 
HETATM 4488 O  O   . HOH I 4 .   ? 73.953 -22.239 86.300  1.00 38.08 ?  684 HOH B O   1 
HETATM 4489 O  O   . HOH I 4 .   ? 71.554 -19.805 69.205  1.00 42.49 ?  685 HOH B O   1 
HETATM 4490 O  O   . HOH I 4 .   ? 37.304 -8.344  63.109  1.00 42.03 ?  686 HOH B O   1 
HETATM 4491 O  O   . HOH I 4 .   ? 65.085 -7.260  60.239  1.00 37.63 ?  687 HOH B O   1 
HETATM 4492 O  O   . HOH I 4 .   ? 50.589 -24.735 94.828  1.00 34.67 ?  688 HOH B O   1 
HETATM 4493 O  O   . HOH I 4 .   ? 71.491 -16.083 60.929  1.00 35.30 ?  689 HOH B O   1 
HETATM 4494 O  O   . HOH I 4 .   ? 70.076 -8.117  67.507  1.00 32.61 ?  690 HOH B O   1 
HETATM 4495 O  O   . HOH I 4 .   ? 72.354 -6.801  88.099  1.00 36.78 ?  691 HOH B O   1 
HETATM 4496 O  O   . HOH I 4 .   ? 57.900 -14.382 53.319  1.00 43.41 ?  692 HOH B O   1 
HETATM 4497 O  O   . HOH I 4 .   ? 62.821 -8.514  95.257  1.00 35.13 ?  693 HOH B O   1 
HETATM 4498 O  O   . HOH I 4 .   ? 37.865 -19.700 70.004  1.00 33.11 ?  694 HOH B O   1 
HETATM 4499 O  O   . HOH I 4 .   ? 48.431 -23.862 94.728  1.00 34.63 ?  695 HOH B O   1 
HETATM 4500 O  O   . HOH I 4 .   ? 57.115 -23.121 63.054  1.00 36.66 ?  696 HOH B O   1 
HETATM 4501 O  O   . HOH I 4 .   ? 34.325 -20.230 78.794  1.00 37.55 ?  697 HOH B O   1 
HETATM 4502 O  O   . HOH I 4 .   ? 61.493 -5.750  95.885  1.00 38.91 ?  698 HOH B O   1 
HETATM 4503 O  O   . HOH I 4 .   ? 46.213 -32.126 76.092  1.00 38.57 ?  699 HOH B O   1 
HETATM 4504 O  O   . HOH I 4 .   ? 32.845 -16.013 91.821  1.00 43.64 ?  700 HOH B O   1 
HETATM 4505 O  O   . HOH I 4 .   ? 58.892 -1.094  89.139  1.00 33.93 ?  701 HOH B O   1 
HETATM 4506 O  O   . HOH I 4 .   ? 77.033 -10.135 75.371  1.00 44.43 ?  702 HOH B O   1 
HETATM 4507 O  O   . HOH I 4 .   ? 33.533 -12.471 77.743  1.00 32.97 ?  703 HOH B O   1 
HETATM 4508 O  O   . HOH I 4 .   ? 63.127 -21.321 79.455  1.00 33.08 ?  704 HOH B O   1 
HETATM 4509 O  O   . HOH I 4 .   ? 53.864 -3.647  94.606  1.00 28.97 ?  705 HOH B O   1 
HETATM 4510 O  O   . HOH I 4 .   ? 51.370 -30.001 87.103  1.00 33.04 ?  706 HOH B O   1 
HETATM 4511 O  O   . HOH I 4 .   ? 39.267 -10.246 92.957  1.00 34.79 ?  707 HOH B O   1 
HETATM 4512 O  O   . HOH I 4 .   ? 50.483 -22.339 60.164  1.00 41.68 ?  708 HOH B O   1 
HETATM 4513 O  O   . HOH I 4 .   ? 59.824 -15.484 99.326  1.00 38.85 ?  709 HOH B O   1 
HETATM 4514 O  O   . HOH I 4 .   ? 79.790 -17.956 75.502  1.00 34.01 ?  710 HOH B O   1 
HETATM 4515 O  O   . HOH I 4 .   ? 57.876 -19.133 98.759  1.00 34.17 ?  711 HOH B O   1 
HETATM 4516 O  O   . HOH I 4 .   ? 36.844 -8.676  93.045  1.00 45.66 ?  712 HOH B O   1 
HETATM 4517 O  O   . HOH I 4 .   ? 68.395 -12.076 57.968  1.00 42.64 ?  713 HOH B O   1 
HETATM 4518 O  O   . HOH I 4 .   ? 44.475 -33.862 76.695  1.00 38.28 ?  714 HOH B O   1 
HETATM 4519 O  O   . HOH I 4 .   ? 70.301 -12.588 93.523  1.00 40.54 ?  715 HOH B O   1 
HETATM 4520 O  O   . HOH I 4 .   ? 44.798 -9.795  99.630  1.00 40.61 ?  716 HOH B O   1 
HETATM 4521 O  O   . HOH I 4 .   ? 53.688 -33.531 79.447  1.00 37.85 ?  717 HOH B O   1 
HETATM 4522 O  O   . HOH I 4 .   ? 68.357 -8.350  65.905  1.00 26.85 ?  718 HOH B O   1 
HETATM 4523 O  O   . HOH I 4 .   ? 54.558 -12.543 98.315  1.00 42.46 ?  719 HOH B O   1 
HETATM 4524 O  O   . HOH I 4 .   ? 76.879 -6.276  72.715  1.00 37.50 ?  720 HOH B O   1 
HETATM 4525 O  O   . HOH I 4 .   ? 37.475 -24.273 70.432  1.00 31.68 ?  721 HOH B O   1 
HETATM 4526 O  O   . HOH I 4 .   ? 79.521 -15.764 84.409  1.00 33.98 ?  722 HOH B O   1 
HETATM 4527 O  O   . HOH I 4 .   ? 67.119 -6.048  64.720  1.00 31.88 ?  723 HOH B O   1 
HETATM 4528 O  O   . HOH I 4 .   ? 64.166 -20.112 97.281  1.00 33.82 ?  724 HOH B O   1 
HETATM 4529 O  O   . HOH I 4 .   ? 36.107 -20.790 72.403  1.00 37.19 ?  725 HOH B O   1 
HETATM 4530 O  O   . HOH I 4 .   ? 36.889 -24.197 73.729  1.00 37.02 ?  726 HOH B O   1 
HETATM 4531 O  O   . HOH I 4 .   ? 76.324 -4.289  73.962  1.00 36.92 ?  727 HOH B O   1 
HETATM 4532 O  O   . HOH I 4 .   ? 64.798 -37.493 93.596  1.00 56.57 ?  728 HOH B O   1 
# 
