data_9IXD
# 
_entry.id   9IXD 
# 
_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   9IXD         pdb_00009ixd 10.2210/pdb9ixd/pdb 
WWPDB D_1300049869 ?            ?                   
# 
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           9IXD 
_pdbx_database_PDB_obs_spr.replace_pdb_id   8IUW 
_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                        9IXD 
_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 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9IXC 
_pdbx_database_related.content_type   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    2   ?        ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                24.305    2   ?        ? ? ? 
4 non-polymer syn 'COPPER (II) ION'                              63.546    1   ?        ? ? ? 
5 non-polymer syn 'COPPER (I) ION'                               63.546    1   ?        ? ? ? 
6 water       nat water                                          18.015    502 ?        ? ? ? 
# 
_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 'COPPER (II) ION'    CU  
5 'COPPER (I) ION'     CU1 
6 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 86  CSD 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 
CSD 'L-peptide linking' n 3-SULFINOALANINE     'S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE' 'C3 H7 N O4 S'   153.157 
CSO 'L-peptide linking' n S-HYDROXYCYSTEINE    ?                                            'C3 H7 N O3 S'   137.158 
CU  non-polymer         . 'COPPER (II) ION'    ?                                            'Cu 2'           63.546  
CU1 non-polymer         . 'COPPER (I) ION'     ?                                            'Cu 1'           63.546  
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 86  CSD 86  86  86  CSD CSD 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 CSD ? ? CSD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CSO ? ? CSO ? ? 'SUBJECT OF INVESTIGATION' ? 
3 CU  ? ? CU  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
5 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 2 MN  1   402 402  MN  MN  A . 
E 3 MG  1   403 403  MG  MG  A . 
F 4 CU  1   401 401  CU  CU  B . 
G 5 CU1 1   402 402  CU1 CU  B . 
H 3 MG  1   403 403  MG  MG  B . 
I 6 HOH 1   501 1159 HOH HOH A . 
I 6 HOH 2   502 1259 HOH HOH A . 
I 6 HOH 3   503 1191 HOH HOH A . 
I 6 HOH 4   504 1052 HOH HOH A . 
I 6 HOH 5   505 1333 HOH HOH A . 
I 6 HOH 6   506 1188 HOH HOH A . 
I 6 HOH 7   507 1198 HOH HOH A . 
I 6 HOH 8   508 1184 HOH HOH A . 
I 6 HOH 9   509 1171 HOH HOH A . 
I 6 HOH 10  510 1265 HOH HOH A . 
I 6 HOH 11  511 1166 HOH HOH A . 
I 6 HOH 12  512 1260 HOH HOH A . 
I 6 HOH 13  513 1156 HOH HOH A . 
I 6 HOH 14  514 1164 HOH HOH A . 
I 6 HOH 15  515 1062 HOH HOH A . 
I 6 HOH 16  516 1015 HOH HOH A . 
I 6 HOH 17  517 1054 HOH HOH A . 
I 6 HOH 18  518 1180 HOH HOH A . 
I 6 HOH 19  519 1168 HOH HOH A . 
I 6 HOH 20  520 1041 HOH HOH A . 
I 6 HOH 21  521 1105 HOH HOH A . 
I 6 HOH 22  522 1474 HOH HOH A . 
I 6 HOH 23  523 1055 HOH HOH A . 
I 6 HOH 24  524 1058 HOH HOH A . 
I 6 HOH 25  525 1373 HOH HOH A . 
I 6 HOH 26  526 1268 HOH HOH A . 
I 6 HOH 27  527 1150 HOH HOH A . 
I 6 HOH 28  528 1017 HOH HOH A . 
I 6 HOH 29  529 1385 HOH HOH A . 
I 6 HOH 30  530 1037 HOH HOH A . 
I 6 HOH 31  531 1134 HOH HOH A . 
I 6 HOH 32  532 1047 HOH HOH A . 
I 6 HOH 33  533 1039 HOH HOH A . 
I 6 HOH 34  534 1027 HOH HOH A . 
I 6 HOH 35  535 1223 HOH HOH A . 
I 6 HOH 36  536 1026 HOH HOH A . 
I 6 HOH 37  537 1216 HOH HOH A . 
I 6 HOH 38  538 1031 HOH HOH A . 
I 6 HOH 39  539 1203 HOH HOH A . 
I 6 HOH 40  540 1118 HOH HOH A . 
I 6 HOH 41  541 1022 HOH HOH A . 
I 6 HOH 42  542 1116 HOH HOH A . 
I 6 HOH 43  543 1032 HOH HOH A . 
I 6 HOH 44  544 1035 HOH HOH A . 
I 6 HOH 45  545 1028 HOH HOH A . 
I 6 HOH 46  546 1125 HOH HOH A . 
I 6 HOH 47  547 1160 HOH HOH A . 
I 6 HOH 48  548 1059 HOH HOH A . 
I 6 HOH 49  549 1137 HOH HOH A . 
I 6 HOH 50  550 1113 HOH HOH A . 
I 6 HOH 51  551 1004 HOH HOH A . 
I 6 HOH 52  552 1169 HOH HOH A . 
I 6 HOH 53  553 1025 HOH HOH A . 
I 6 HOH 54  554 1239 HOH HOH A . 
I 6 HOH 55  555 1117 HOH HOH A . 
I 6 HOH 56  556 1072 HOH HOH A . 
I 6 HOH 57  557 1063 HOH HOH A . 
I 6 HOH 58  558 1102 HOH HOH A . 
I 6 HOH 59  559 1158 HOH HOH A . 
I 6 HOH 60  560 1030 HOH HOH A . 
I 6 HOH 61  561 1213 HOH HOH A . 
I 6 HOH 62  562 1076 HOH HOH A . 
I 6 HOH 63  563 1056 HOH HOH A . 
I 6 HOH 64  564 1005 HOH HOH A . 
I 6 HOH 65  565 1206 HOH HOH A . 
I 6 HOH 66  566 1147 HOH HOH A . 
I 6 HOH 67  567 1051 HOH HOH A . 
I 6 HOH 68  568 1210 HOH HOH A . 
I 6 HOH 69  569 1214 HOH HOH A . 
I 6 HOH 70  570 1209 HOH HOH A . 
I 6 HOH 71  571 1096 HOH HOH A . 
I 6 HOH 72  572 1202 HOH HOH A . 
I 6 HOH 73  573 1036 HOH HOH A . 
I 6 HOH 74  574 1098 HOH HOH A . 
I 6 HOH 75  575 1034 HOH HOH A . 
I 6 HOH 76  576 1045 HOH HOH A . 
I 6 HOH 77  577 1043 HOH HOH A . 
I 6 HOH 78  578 1212 HOH HOH A . 
I 6 HOH 79  579 1110 HOH HOH A . 
I 6 HOH 80  580 1204 HOH HOH A . 
I 6 HOH 81  581 1192 HOH HOH A . 
I 6 HOH 82  582 1130 HOH HOH A . 
I 6 HOH 83  583 1011 HOH HOH A . 
I 6 HOH 84  584 1207 HOH HOH A . 
I 6 HOH 85  585 1142 HOH HOH A . 
I 6 HOH 86  586 1066 HOH HOH A . 
I 6 HOH 87  587 1141 HOH HOH A . 
I 6 HOH 88  588 1006 HOH HOH A . 
I 6 HOH 89  589 1001 HOH HOH A . 
I 6 HOH 90  590 1010 HOH HOH A . 
I 6 HOH 91  591 1013 HOH HOH A . 
I 6 HOH 92  592 1182 HOH HOH A . 
I 6 HOH 93  593 1042 HOH HOH A . 
I 6 HOH 94  594 1111 HOH HOH A . 
I 6 HOH 95  595 1088 HOH HOH A . 
I 6 HOH 96  596 1262 HOH HOH A . 
I 6 HOH 97  597 1311 HOH HOH A . 
I 6 HOH 98  598 1290 HOH HOH A . 
I 6 HOH 99  599 1145 HOH HOH A . 
I 6 HOH 100 600 1253 HOH HOH A . 
I 6 HOH 101 601 1205 HOH HOH A . 
I 6 HOH 102 602 1218 HOH HOH A . 
I 6 HOH 103 603 1012 HOH HOH A . 
I 6 HOH 104 604 1187 HOH HOH A . 
I 6 HOH 105 605 1073 HOH HOH A . 
I 6 HOH 106 606 1146 HOH HOH A . 
I 6 HOH 107 607 1152 HOH HOH A . 
I 6 HOH 108 608 1121 HOH HOH A . 
I 6 HOH 109 609 1038 HOH HOH A . 
I 6 HOH 110 610 1211 HOH HOH A . 
I 6 HOH 111 611 1044 HOH HOH A . 
I 6 HOH 112 612 1234 HOH HOH A . 
I 6 HOH 113 613 1229 HOH HOH A . 
I 6 HOH 114 614 1016 HOH HOH A . 
I 6 HOH 115 615 1050 HOH HOH A . 
I 6 HOH 116 616 1108 HOH HOH A . 
I 6 HOH 117 617 1264 HOH HOH A . 
I 6 HOH 118 618 1029 HOH HOH A . 
I 6 HOH 119 619 1081 HOH HOH A . 
I 6 HOH 120 620 1273 HOH HOH A . 
I 6 HOH 121 621 1163 HOH HOH A . 
I 6 HOH 122 622 1208 HOH HOH A . 
I 6 HOH 123 623 1221 HOH HOH A . 
I 6 HOH 124 624 1020 HOH HOH A . 
I 6 HOH 125 625 1261 HOH HOH A . 
I 6 HOH 126 626 1046 HOH HOH A . 
I 6 HOH 127 627 1120 HOH HOH A . 
I 6 HOH 128 628 1499 HOH HOH A . 
I 6 HOH 129 629 1405 HOH HOH A . 
I 6 HOH 130 630 1371 HOH HOH A . 
I 6 HOH 131 631 1279 HOH HOH A . 
I 6 HOH 132 632 1109 HOH HOH A . 
I 6 HOH 133 633 1119 HOH HOH A . 
I 6 HOH 134 634 1494 HOH HOH A . 
I 6 HOH 135 635 1002 HOH HOH A . 
I 6 HOH 136 636 1252 HOH HOH A . 
I 6 HOH 137 637 1127 HOH HOH A . 
I 6 HOH 138 638 1069 HOH HOH A . 
I 6 HOH 139 639 1053 HOH HOH A . 
I 6 HOH 140 640 1065 HOH HOH A . 
I 6 HOH 141 641 1007 HOH HOH A . 
I 6 HOH 142 642 1014 HOH HOH A . 
I 6 HOH 143 643 1195 HOH HOH A . 
I 6 HOH 144 644 1061 HOH HOH A . 
I 6 HOH 145 645 1217 HOH HOH A . 
I 6 HOH 146 646 1087 HOH HOH A . 
I 6 HOH 147 647 1086 HOH HOH A . 
I 6 HOH 148 648 1220 HOH HOH A . 
I 6 HOH 149 649 1172 HOH HOH A . 
I 6 HOH 150 650 1243 HOH HOH A . 
I 6 HOH 151 651 1082 HOH HOH A . 
I 6 HOH 152 652 1257 HOH HOH A . 
I 6 HOH 153 653 1090 HOH HOH A . 
I 6 HOH 154 654 1374 HOH HOH A . 
I 6 HOH 155 655 1468 HOH HOH A . 
I 6 HOH 156 656 1040 HOH HOH A . 
I 6 HOH 157 657 1057 HOH HOH A . 
I 6 HOH 158 658 1248 HOH HOH A . 
I 6 HOH 159 659 1100 HOH HOH A . 
I 6 HOH 160 660 1256 HOH HOH A . 
I 6 HOH 161 661 1023 HOH HOH A . 
I 6 HOH 162 662 1225 HOH HOH A . 
I 6 HOH 163 663 1104 HOH HOH A . 
I 6 HOH 164 664 1140 HOH HOH A . 
I 6 HOH 165 665 1227 HOH HOH A . 
I 6 HOH 166 666 1185 HOH HOH A . 
I 6 HOH 167 667 1078 HOH HOH A . 
I 6 HOH 168 668 1048 HOH HOH A . 
I 6 HOH 169 669 1112 HOH HOH A . 
I 6 HOH 170 670 1258 HOH HOH A . 
I 6 HOH 171 671 1162 HOH HOH A . 
I 6 HOH 172 672 1003 HOH HOH A . 
I 6 HOH 173 673 1075 HOH HOH A . 
I 6 HOH 174 674 1249 HOH HOH A . 
I 6 HOH 175 675 1222 HOH HOH A . 
I 6 HOH 176 676 1071 HOH HOH A . 
I 6 HOH 177 677 1161 HOH HOH A . 
I 6 HOH 178 678 1008 HOH HOH A . 
I 6 HOH 179 679 1099 HOH HOH A . 
I 6 HOH 180 680 1060 HOH HOH A . 
I 6 HOH 181 681 1136 HOH HOH A . 
I 6 HOH 182 682 1201 HOH HOH A . 
I 6 HOH 183 683 1236 HOH HOH A . 
I 6 HOH 184 684 1199 HOH HOH A . 
I 6 HOH 185 685 1092 HOH HOH A . 
I 6 HOH 186 686 1129 HOH HOH A . 
I 6 HOH 187 687 1196 HOH HOH A . 
I 6 HOH 188 688 1489 HOH HOH A . 
I 6 HOH 189 689 1128 HOH HOH A . 
I 6 HOH 190 690 1033 HOH HOH A . 
I 6 HOH 191 691 1115 HOH HOH A . 
I 6 HOH 192 692 1453 HOH HOH A . 
I 6 HOH 193 693 1021 HOH HOH A . 
I 6 HOH 194 694 1174 HOH HOH A . 
I 6 HOH 195 695 1178 HOH HOH A . 
I 6 HOH 196 696 1449 HOH HOH A . 
I 6 HOH 197 697 1189 HOH HOH A . 
I 6 HOH 198 698 1122 HOH HOH A . 
I 6 HOH 199 699 1093 HOH HOH A . 
I 6 HOH 200 700 1177 HOH HOH A . 
I 6 HOH 201 701 1157 HOH HOH A . 
I 6 HOH 202 702 1165 HOH HOH A . 
I 6 HOH 203 703 1246 HOH HOH A . 
I 6 HOH 204 704 1106 HOH HOH A . 
I 6 HOH 205 705 1193 HOH HOH A . 
I 6 HOH 206 706 1148 HOH HOH A . 
I 6 HOH 207 707 1250 HOH HOH A . 
I 6 HOH 208 708 1138 HOH HOH A . 
I 6 HOH 209 709 1170 HOH HOH A . 
I 6 HOH 210 710 1238 HOH HOH A . 
I 6 HOH 211 711 1476 HOH HOH A . 
I 6 HOH 212 712 1181 HOH HOH A . 
I 6 HOH 213 713 1219 HOH HOH A . 
I 6 HOH 214 714 1154 HOH HOH A . 
I 6 HOH 215 715 1247 HOH HOH A . 
I 6 HOH 216 716 1132 HOH HOH A . 
I 6 HOH 217 717 1133 HOH HOH A . 
I 6 HOH 218 718 1175 HOH HOH A . 
I 6 HOH 219 719 1064 HOH HOH A . 
I 6 HOH 220 720 1135 HOH HOH A . 
I 6 HOH 221 721 1263 HOH HOH A . 
I 6 HOH 222 722 1495 HOH HOH A . 
I 6 HOH 223 723 1266 HOH HOH A . 
I 6 HOH 224 724 1067 HOH HOH A . 
I 6 HOH 225 725 1451 HOH HOH A . 
I 6 HOH 226 726 1245 HOH HOH A . 
I 6 HOH 227 727 1074 HOH HOH A . 
I 6 HOH 228 728 1114 HOH HOH A . 
I 6 HOH 229 729 1232 HOH HOH A . 
I 6 HOH 230 730 1024 HOH HOH A . 
I 6 HOH 231 731 1197 HOH HOH A . 
I 6 HOH 232 732 1241 HOH HOH A . 
I 6 HOH 233 733 1340 HOH HOH A . 
I 6 HOH 234 734 1083 HOH HOH A . 
I 6 HOH 235 735 1242 HOH HOH A . 
I 6 HOH 236 736 1167 HOH HOH A . 
I 6 HOH 237 737 1235 HOH HOH A . 
I 6 HOH 238 738 1107 HOH HOH A . 
I 6 HOH 239 739 1101 HOH HOH A . 
I 6 HOH 240 740 1091 HOH HOH A . 
I 6 HOH 241 741 1131 HOH HOH A . 
I 6 HOH 242 742 1485 HOH HOH A . 
I 6 HOH 243 743 1237 HOH HOH A . 
I 6 HOH 244 744 1103 HOH HOH A . 
I 6 HOH 245 745 1244 HOH HOH A . 
I 6 HOH 246 746 1094 HOH HOH A . 
I 6 HOH 247 747 1176 HOH HOH A . 
I 6 HOH 248 748 1215 HOH HOH A . 
I 6 HOH 249 749 1097 HOH HOH A . 
I 6 HOH 250 750 1254 HOH HOH A . 
I 6 HOH 251 751 1183 HOH HOH A . 
I 6 HOH 252 752 1194 HOH HOH A . 
I 6 HOH 253 753 1070 HOH HOH A . 
I 6 HOH 254 754 1068 HOH HOH A . 
I 6 HOH 255 755 1155 HOH HOH A . 
I 6 HOH 256 756 1153 HOH HOH A . 
I 6 HOH 257 757 1233 HOH HOH A . 
I 6 HOH 258 758 1084 HOH HOH A . 
I 6 HOH 259 759 1413 HOH HOH A . 
I 6 HOH 260 760 1126 HOH HOH A . 
I 6 HOH 261 761 1143 HOH HOH A . 
I 6 HOH 262 762 1085 HOH HOH A . 
I 6 HOH 263 763 1151 HOH HOH A . 
I 6 HOH 264 764 1139 HOH HOH A . 
I 6 HOH 265 765 1228 HOH HOH A . 
I 6 HOH 266 766 1077 HOH HOH A . 
I 6 HOH 267 767 1173 HOH HOH A . 
I 6 HOH 268 768 1251 HOH HOH A . 
I 6 HOH 269 769 1190 HOH HOH A . 
J 6 HOH 1   501 1445 HOH HOH B . 
J 6 HOH 2   502 1458 HOH HOH B . 
J 6 HOH 3   503 1500 HOH HOH B . 
J 6 HOH 4   504 1089 HOH HOH B . 
J 6 HOH 5   505 1224 HOH HOH B . 
J 6 HOH 6   506 1501 HOH HOH B . 
J 6 HOH 7   507 1325 HOH HOH B . 
J 6 HOH 8   508 1432 HOH HOH B . 
J 6 HOH 9   509 1409 HOH HOH B . 
J 6 HOH 10  510 1292 HOH HOH B . 
J 6 HOH 11  511 1442 HOH HOH B . 
J 6 HOH 12  512 1309 HOH HOH B . 
J 6 HOH 13  513 1365 HOH HOH B . 
J 6 HOH 14  514 1419 HOH HOH B . 
J 6 HOH 15  515 1337 HOH HOH B . 
J 6 HOH 16  516 1497 HOH HOH B . 
J 6 HOH 17  517 1300 HOH HOH B . 
J 6 HOH 18  518 1271 HOH HOH B . 
J 6 HOH 19  519 1496 HOH HOH B . 
J 6 HOH 20  520 1319 HOH HOH B . 
J 6 HOH 21  521 1272 HOH HOH B . 
J 6 HOH 22  522 1433 HOH HOH B . 
J 6 HOH 23  523 1304 HOH HOH B . 
J 6 HOH 24  524 1414 HOH HOH B . 
J 6 HOH 25  525 1411 HOH HOH B . 
J 6 HOH 26  526 1226 HOH HOH B . 
J 6 HOH 27  527 1018 HOH HOH B . 
J 6 HOH 28  528 1477 HOH HOH B . 
J 6 HOH 29  529 1359 HOH HOH B . 
J 6 HOH 30  530 1368 HOH HOH B . 
J 6 HOH 31  531 1274 HOH HOH B . 
J 6 HOH 32  532 1326 HOH HOH B . 
J 6 HOH 33  533 1377 HOH HOH B . 
J 6 HOH 34  534 1471 HOH HOH B . 
J 6 HOH 35  535 1351 HOH HOH B . 
J 6 HOH 36  536 1269 HOH HOH B . 
J 6 HOH 37  537 1455 HOH HOH B . 
J 6 HOH 38  538 1420 HOH HOH B . 
J 6 HOH 39  539 1404 HOH HOH B . 
J 6 HOH 40  540 1398 HOH HOH B . 
J 6 HOH 41  541 1317 HOH HOH B . 
J 6 HOH 42  542 1291 HOH HOH B . 
J 6 HOH 43  543 1401 HOH HOH B . 
J 6 HOH 44  544 1372 HOH HOH B . 
J 6 HOH 45  545 1447 HOH HOH B . 
J 6 HOH 46  546 1284 HOH HOH B . 
J 6 HOH 47  547 1288 HOH HOH B . 
J 6 HOH 48  548 1427 HOH HOH B . 
J 6 HOH 49  549 1289 HOH HOH B . 
J 6 HOH 50  550 1338 HOH HOH B . 
J 6 HOH 51  551 1465 HOH HOH B . 
J 6 HOH 52  552 1382 HOH HOH B . 
J 6 HOH 53  553 1049 HOH HOH B . 
J 6 HOH 54  554 1424 HOH HOH B . 
J 6 HOH 55  555 1331 HOH HOH B . 
J 6 HOH 56  556 1280 HOH HOH B . 
J 6 HOH 57  557 1502 HOH HOH B . 
J 6 HOH 58  558 1321 HOH HOH B . 
J 6 HOH 59  559 1347 HOH HOH B . 
J 6 HOH 60  560 1463 HOH HOH B . 
J 6 HOH 61  561 1361 HOH HOH B . 
J 6 HOH 62  562 1328 HOH HOH B . 
J 6 HOH 63  563 1380 HOH HOH B . 
J 6 HOH 64  564 1383 HOH HOH B . 
J 6 HOH 65  565 1426 HOH HOH B . 
J 6 HOH 66  566 1487 HOH HOH B . 
J 6 HOH 67  567 1478 HOH HOH B . 
J 6 HOH 68  568 1461 HOH HOH B . 
J 6 HOH 69  569 1315 HOH HOH B . 
J 6 HOH 70  570 1399 HOH HOH B . 
J 6 HOH 71  571 1343 HOH HOH B . 
J 6 HOH 72  572 1277 HOH HOH B . 
J 6 HOH 73  573 1392 HOH HOH B . 
J 6 HOH 74  574 1386 HOH HOH B . 
J 6 HOH 75  575 1283 HOH HOH B . 
J 6 HOH 76  576 1327 HOH HOH B . 
J 6 HOH 77  577 1267 HOH HOH B . 
J 6 HOH 78  578 1334 HOH HOH B . 
J 6 HOH 79  579 1358 HOH HOH B . 
J 6 HOH 80  580 1467 HOH HOH B . 
J 6 HOH 81  581 1402 HOH HOH B . 
J 6 HOH 82  582 1466 HOH HOH B . 
J 6 HOH 83  583 1308 HOH HOH B . 
J 6 HOH 84  584 1301 HOH HOH B . 
J 6 HOH 85  585 1079 HOH HOH B . 
J 6 HOH 86  586 1484 HOH HOH B . 
J 6 HOH 87  587 1469 HOH HOH B . 
J 6 HOH 88  588 1282 HOH HOH B . 
J 6 HOH 89  589 1278 HOH HOH B . 
J 6 HOH 90  590 1352 HOH HOH B . 
J 6 HOH 91  591 1332 HOH HOH B . 
J 6 HOH 92  592 1370 HOH HOH B . 
J 6 HOH 93  593 1322 HOH HOH B . 
J 6 HOH 94  594 1488 HOH HOH B . 
J 6 HOH 95  595 1428 HOH HOH B . 
J 6 HOH 96  596 1454 HOH HOH B . 
J 6 HOH 97  597 1444 HOH HOH B . 
J 6 HOH 98  598 1179 HOH HOH B . 
J 6 HOH 99  599 1429 HOH HOH B . 
J 6 HOH 100 600 1295 HOH HOH B . 
J 6 HOH 101 601 1286 HOH HOH B . 
J 6 HOH 102 602 1400 HOH HOH B . 
J 6 HOH 103 603 1394 HOH HOH B . 
J 6 HOH 104 604 1418 HOH HOH B . 
J 6 HOH 105 605 1345 HOH HOH B . 
J 6 HOH 106 606 1307 HOH HOH B . 
J 6 HOH 107 607 1285 HOH HOH B . 
J 6 HOH 108 608 1346 HOH HOH B . 
J 6 HOH 109 609 1344 HOH HOH B . 
J 6 HOH 110 610 1306 HOH HOH B . 
J 6 HOH 111 611 1341 HOH HOH B . 
J 6 HOH 112 612 1316 HOH HOH B . 
J 6 HOH 113 613 1393 HOH HOH B . 
J 6 HOH 114 614 1406 HOH HOH B . 
J 6 HOH 115 615 1276 HOH HOH B . 
J 6 HOH 116 616 1287 HOH HOH B . 
J 6 HOH 117 617 1299 HOH HOH B . 
J 6 HOH 118 618 1302 HOH HOH B . 
J 6 HOH 119 619 1275 HOH HOH B . 
J 6 HOH 120 620 1364 HOH HOH B . 
J 6 HOH 121 621 1320 HOH HOH B . 
J 6 HOH 122 622 1296 HOH HOH B . 
J 6 HOH 123 623 1396 HOH HOH B . 
J 6 HOH 124 624 1312 HOH HOH B . 
J 6 HOH 125 625 1354 HOH HOH B . 
J 6 HOH 126 626 1303 HOH HOH B . 
J 6 HOH 127 627 1434 HOH HOH B . 
J 6 HOH 128 628 1431 HOH HOH B . 
J 6 HOH 129 629 1408 HOH HOH B . 
J 6 HOH 130 630 1297 HOH HOH B . 
J 6 HOH 131 631 1353 HOH HOH B . 
J 6 HOH 132 632 1390 HOH HOH B . 
J 6 HOH 133 633 1314 HOH HOH B . 
J 6 HOH 134 634 1438 HOH HOH B . 
J 6 HOH 135 635 1473 HOH HOH B . 
J 6 HOH 136 636 1491 HOH HOH B . 
J 6 HOH 137 637 1475 HOH HOH B . 
J 6 HOH 138 638 1270 HOH HOH B . 
J 6 HOH 139 639 1403 HOH HOH B . 
J 6 HOH 140 640 1483 HOH HOH B . 
J 6 HOH 141 641 1423 HOH HOH B . 
J 6 HOH 142 642 1281 HOH HOH B . 
J 6 HOH 143 643 1336 HOH HOH B . 
J 6 HOH 144 644 1439 HOH HOH B . 
J 6 HOH 145 645 1313 HOH HOH B . 
J 6 HOH 146 646 1330 HOH HOH B . 
J 6 HOH 147 647 1375 HOH HOH B . 
J 6 HOH 148 648 1323 HOH HOH B . 
J 6 HOH 149 649 1298 HOH HOH B . 
J 6 HOH 150 650 1294 HOH HOH B . 
J 6 HOH 151 651 1391 HOH HOH B . 
J 6 HOH 152 652 1318 HOH HOH B . 
J 6 HOH 153 653 1457 HOH HOH B . 
J 6 HOH 154 654 1381 HOH HOH B . 
J 6 HOH 155 655 1310 HOH HOH B . 
J 6 HOH 156 656 1395 HOH HOH B . 
J 6 HOH 157 657 1342 HOH HOH B . 
J 6 HOH 158 658 1080 HOH HOH B . 
J 6 HOH 159 659 1436 HOH HOH B . 
J 6 HOH 160 660 1412 HOH HOH B . 
J 6 HOH 161 661 1470 HOH HOH B . 
J 6 HOH 162 662 1329 HOH HOH B . 
J 6 HOH 163 663 1305 HOH HOH B . 
J 6 HOH 164 664 1348 HOH HOH B . 
J 6 HOH 165 665 1482 HOH HOH B . 
J 6 HOH 166 666 1415 HOH HOH B . 
J 6 HOH 167 667 1293 HOH HOH B . 
J 6 HOH 168 668 1384 HOH HOH B . 
J 6 HOH 169 669 1363 HOH HOH B . 
J 6 HOH 170 670 1360 HOH HOH B . 
J 6 HOH 171 671 1481 HOH HOH B . 
J 6 HOH 172 672 1376 HOH HOH B . 
J 6 HOH 173 673 1479 HOH HOH B . 
J 6 HOH 174 674 1200 HOH HOH B . 
J 6 HOH 175 675 1437 HOH HOH B . 
J 6 HOH 176 676 1355 HOH HOH B . 
J 6 HOH 177 677 1387 HOH HOH B . 
J 6 HOH 178 678 1240 HOH HOH B . 
J 6 HOH 179 679 1464 HOH HOH B . 
J 6 HOH 180 680 1369 HOH HOH B . 
J 6 HOH 181 681 1421 HOH HOH B . 
J 6 HOH 182 682 1335 HOH HOH B . 
J 6 HOH 183 683 1349 HOH HOH B . 
J 6 HOH 184 684 1362 HOH HOH B . 
J 6 HOH 185 685 1367 HOH HOH B . 
J 6 HOH 186 686 1379 HOH HOH B . 
J 6 HOH 187 687 1493 HOH HOH B . 
J 6 HOH 188 688 1498 HOH HOH B . 
J 6 HOH 189 689 1144 HOH HOH B . 
J 6 HOH 190 690 1009 HOH HOH B . 
J 6 HOH 191 691 1324 HOH HOH B . 
J 6 HOH 192 692 1446 HOH HOH B . 
J 6 HOH 193 693 1357 HOH HOH B . 
J 6 HOH 194 694 1456 HOH HOH B . 
J 6 HOH 195 695 1255 HOH HOH B . 
J 6 HOH 196 696 1186 HOH HOH B . 
J 6 HOH 197 697 1425 HOH HOH B . 
J 6 HOH 198 698 1389 HOH HOH B . 
J 6 HOH 199 699 1435 HOH HOH B . 
J 6 HOH 200 700 1490 HOH HOH B . 
J 6 HOH 201 701 1459 HOH HOH B . 
J 6 HOH 202 702 1095 HOH HOH B . 
J 6 HOH 203 703 1462 HOH HOH B . 
J 6 HOH 204 704 1397 HOH HOH B . 
J 6 HOH 205 705 1440 HOH HOH B . 
J 6 HOH 206 706 1388 HOH HOH B . 
J 6 HOH 207 707 1450 HOH HOH B . 
J 6 HOH 208 708 1124 HOH HOH B . 
J 6 HOH 209 709 1480 HOH HOH B . 
J 6 HOH 210 710 1460 HOH HOH B . 
J 6 HOH 211 711 1356 HOH HOH B . 
J 6 HOH 212 712 1486 HOH HOH B . 
J 6 HOH 213 713 1416 HOH HOH B . 
J 6 HOH 214 714 1452 HOH HOH B . 
J 6 HOH 215 715 1417 HOH HOH B . 
J 6 HOH 216 716 1123 HOH HOH B . 
J 6 HOH 217 717 1350 HOH HOH B . 
J 6 HOH 218 718 1366 HOH HOH B . 
J 6 HOH 219 719 1410 HOH HOH B . 
J 6 HOH 220 720 1448 HOH HOH B . 
J 6 HOH 221 721 1019 HOH HOH B . 
J 6 HOH 222 722 1378 HOH HOH B . 
J 6 HOH 223 723 1339 HOH HOH B . 
J 6 HOH 224 724 1231 HOH HOH B . 
J 6 HOH 225 725 1441 HOH HOH B . 
J 6 HOH 226 726 1430 HOH HOH B . 
J 6 HOH 227 727 1149 HOH HOH B . 
J 6 HOH 228 728 1443 HOH HOH B . 
J 6 HOH 229 729 1492 HOH HOH B . 
J 6 HOH 230 730 1407 HOH HOH B . 
J 6 HOH 231 731 1422 HOH HOH B . 
J 6 HOH 232 732 1472 HOH HOH B . 
J 6 HOH 233 733 1230 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                  83.69 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   84.70 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  70.27 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IXD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.400 
_cell.length_a_esd                 ? 
_cell.length_b                     47.145 
_cell.length_b_esd                 ? 
_cell.length_c                     59.393 
_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                         9IXD 
_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                   9IXD 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.15 
_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   1.3500 
_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        1.3500 
_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                                       9IXD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               44.22 
_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                                     70228 
_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                           93.3 
_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                          13.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_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                                0.059 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       256067 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.050 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           11971 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3255 
_reflns_shell.percent_possible_obs                          87.0 
_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                               3.7 
_reflns_shell.pdbx_chi_squared                              0.75 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.9 
_reflns_shell.pdbx_Rrim_I_all                               0.824 
_reflns_shell.pdbx_Rpim_I_all                               0.426 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.708 
_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                                  0.704 
_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                                 9IXD 
_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                            1.50 
_refine.ls_d_res_low                             44.22 
_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                     70216 
_refine.ls_number_reflns_R_free                  3450 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.26 
_refine.ls_percent_reflns_R_free                 4.91 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1699 
_refine.ls_R_factor_R_free                       0.2046 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1682 
_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                 20.65 
_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                            0.18 
_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                       1.50 
_refine_hist.d_res_low                        44.22 
_refine_hist.number_atoms_solvent             502 
_refine_hist.number_atoms_total               4592 
_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        4084 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_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' ? 0.006  ? 4298 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.853  ? 5888 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.268 ? 618  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 676  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 792  ? 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' 1.50 1.52  . . 149 2458 87.00 . . . . 0.2862 . . . . . . . . . . . 0.3371 
'X-RAY DIFFRACTION' 1.52 1.54  . . 127 2524 88.00 . . . . 0.2430 . . . . . . . . . . . 0.2942 
'X-RAY DIFFRACTION' 1.54 1.57  . . 124 2615 90.00 . . . . 0.2249 . . . . . . . . . . . 0.2314 
'X-RAY DIFFRACTION' 1.57 1.59  . . 128 2560 90.00 . . . . 0.2052 . . . . . . . . . . . 0.2522 
'X-RAY DIFFRACTION' 1.59 1.62  . . 131 2627 91.00 . . . . 0.1917 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 1.62 1.64  . . 132 2596 91.00 . . . . 0.1878 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 1.64 1.67  . . 147 2631 92.00 . . . . 0.1858 . . . . . . . . . . . 0.2223 
'X-RAY DIFFRACTION' 1.67 1.71  . . 139 2644 92.00 . . . . 0.1883 . . . . . . . . . . . 0.2363 
'X-RAY DIFFRACTION' 1.71 1.74  . . 132 2672 92.00 . . . . 0.1891 . . . . . . . . . . . 0.2636 
'X-RAY DIFFRACTION' 1.74 1.78  . . 138 2632 93.00 . . . . 0.1902 . . . . . . . . . . . 0.2249 
'X-RAY DIFFRACTION' 1.78 1.82  . . 143 2647 93.00 . . . . 0.1797 . . . . . . . . . . . 0.2125 
'X-RAY DIFFRACTION' 1.82 1.87  . . 143 2632 93.00 . . . . 0.1776 . . . . . . . . . . . 0.2084 
'X-RAY DIFFRACTION' 1.87 1.92  . . 128 2706 93.00 . . . . 0.1774 . . . . . . . . . . . 0.2503 
'X-RAY DIFFRACTION' 1.92 1.97  . . 149 2664 93.00 . . . . 0.1798 . . . . . . . . . . . 0.2092 
'X-RAY DIFFRACTION' 1.97 2.04  . . 140 2680 94.00 . . . . 0.1744 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 2.04 2.11  . . 137 2695 94.00 . . . . 0.1725 . . . . . . . . . . . 0.2327 
'X-RAY DIFFRACTION' 2.11 2.19  . . 155 2657 94.00 . . . . 0.1665 . . . . . . . . . . . 0.1825 
'X-RAY DIFFRACTION' 2.19 2.29  . . 142 2680 94.00 . . . . 0.1652 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 2.29 2.41  . . 142 2737 95.00 . . . . 0.1760 . . . . . . . . . . . 0.1865 
'X-RAY DIFFRACTION' 2.41 2.56  . . 152 2758 96.00 . . . . 0.1687 . . . . . . . . . . . 0.2261 
'X-RAY DIFFRACTION' 2.56 2.76  . . 127 2755 96.00 . . . . 0.1694 . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 2.76 3.04  . . 149 2742 97.00 . . . . 0.1734 . . . . . . . . . . . 0.2298 
'X-RAY DIFFRACTION' 3.04 3.48  . . 128 2814 97.00 . . . . 0.1582 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 3.48 4.38  . . 130 2817 98.00 . . . . 0.1384 . . . . . . . . . . . 0.1551 
'X-RAY DIFFRACTION' 4.39 44.22 . . 138 2823 98.00 . . . . 0.1527 . . . . . . . . . . . 0.1729 
# 
_struct.entry_id                     9IXD 
_struct.title                        'Crystal structure of Copper-bound 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        9IXD 
_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 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
# 
_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 9IXD A 1 ? 273 ? D2Z025 1 ? 273 ? 1 273 
2 1 9IXD 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 9IXD LEU A 274 ? UNP D2Z025 ? ? 'expression tag' 274 1  
1 9IXD GLU A 275 ? UNP D2Z025 ? ? 'expression tag' 275 2  
1 9IXD HIS A 276 ? UNP D2Z025 ? ? 'expression tag' 276 3  
1 9IXD HIS A 277 ? UNP D2Z025 ? ? 'expression tag' 277 4  
1 9IXD HIS A 278 ? UNP D2Z025 ? ? 'expression tag' 278 5  
1 9IXD HIS A 279 ? UNP D2Z025 ? ? 'expression tag' 279 6  
1 9IXD HIS A 280 ? UNP D2Z025 ? ? 'expression tag' 280 7  
1 9IXD HIS A 281 ? UNP D2Z025 ? ? 'expression tag' 281 8  
2 9IXD LEU B 274 ? UNP D2Z025 ? ? 'expression tag' 274 9  
2 9IXD GLU B 275 ? UNP D2Z025 ? ? 'expression tag' 275 10 
2 9IXD HIS B 276 ? UNP D2Z025 ? ? 'expression tag' 276 11 
2 9IXD HIS B 277 ? UNP D2Z025 ? ? 'expression tag' 277 12 
2 9IXD HIS B 278 ? UNP D2Z025 ? ? 'expression tag' 278 13 
2 9IXD HIS B 279 ? UNP D2Z025 ? ? 'expression tag' 279 14 
2 9IXD HIS B 280 ? UNP D2Z025 ? ? 'expression tag' 280 15 
2 9IXD 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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  11580 ? 
2 'ABSA (A^2)' 230   ? 
2 MORE         -22   ? 
2 'SSA (A^2)'  10870 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_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 ? ALA A 271 ? SER A 248 ALA A 271 1 ? 24 
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 ? ? ? ? ? ? ? 1.331 ? ? 
covale2  covale both ? B THR 85  C   ? ? ? 1_555 B CSD 86 N  C ? B THR 85  B CSD 86  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale3  covale both ? B CSO 86  C   B ? ? 1_555 B SER 87 N  ? ? B CSO 86  B SER 87  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale4  covale both ? B CSD 86  C   C ? ? 1_555 B SER 87 N  ? ? B CSD 86  B SER 87  1_555 ? ? ? ? ? ? ? 1.332 ? ? 
metalc1  metalc ?    ? A ASN 77  O   ? ? ? 1_555 E MG  .  MG ? ? A ASN 77  A MG  403 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc2  metalc ?    ? A CYS 86  SG  ? ? ? 1_555 C MN  .  MN ? ? A CYS 86  A MN  401 1_555 ? ? ? ? ? ? ? 2.486 ? ? 
metalc3  metalc ?    ? A ASP 109 OD2 ? ? ? 1_555 C MN  .  MN ? ? A ASP 109 A MN  401 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc4  metalc ?    ? A ASP 109 OD1 ? ? ? 1_555 D MN  .  MN ? ? A ASP 109 A MN  402 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc5  metalc ?    ? A HIS 111 ND1 ? ? ? 1_555 D MN  .  MN ? ? A HIS 111 A MN  402 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc6  metalc ?    ? A ASP 113 OD2 ? ? ? 1_555 C MN  .  MN ? ? A ASP 113 A MN  401 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc7  metalc ?    ? A ASP 198 OD2 ? ? ? 1_555 C MN  .  MN ? ? A ASP 198 A MN  401 1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc8  metalc ?    ? A ASP 198 OD2 ? ? ? 1_555 D MN  .  MN ? ? A ASP 198 A MN  402 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc9  metalc ?    ? A ASP 200 OD1 ? ? ? 1_555 D MN  .  MN ? ? A ASP 200 A MN  402 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc10 metalc ?    ? A ASP 200 OD2 ? ? ? 1_555 D MN  .  MN ? ? A ASP 200 A MN  402 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc11 metalc ?    ? C MN  .   MN  ? ? ? 1_555 I HOH .  O  ? ? A MN  401 A HOH 528 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc12 metalc ?    ? C MN  .   MN  ? ? ? 1_555 I HOH .  O  ? ? A MN  401 A HOH 656 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc13 metalc ?    ? D MN  .   MN  ? ? ? 1_555 I HOH .  O  ? ? A MN  402 A HOH 528 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc14 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? A MG  403 A HOH 533 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc15 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? A MG  403 A HOH 561 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc16 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? A MG  403 A HOH 636 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc17 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? A MG  403 A HOH 669 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc18 metalc ?    ? E MG  .   MG  ? ? ? 1_555 I HOH .  O  ? ? A MG  403 A HOH 716 1_555 ? ? ? ? ? ? ? 2.184 ? ? 
metalc19 metalc ?    ? B CYS 86  SG  A ? ? 1_555 F CU  .  CU ? ? B CYS 86  B CU  401 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc20 metalc ?    ? B CSO 86  OD  B ? ? 1_555 F CU  .  CU ? ? B CSO 86  B CU  401 1_555 ? ? ? ? ? ? ? 1.775 ? ? 
metalc21 metalc ?    ? B CSD 86  OD2 C ? ? 1_555 F CU  .  CU ? ? B CSD 86  B CU  401 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
metalc22 metalc ?    ? B ASP 109 OD2 A ? ? 1_555 F CU  .  CU ? ? B ASP 109 B CU  401 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc23 metalc ?    ? B ASP 109 OD2 B ? ? 1_555 F CU  .  CU ? ? B ASP 109 B CU  401 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc24 metalc ?    ? B ASP 109 OD1 A ? ? 1_555 G CU1 .  CU ? ? B ASP 109 B CU1 402 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc25 metalc ?    ? B HIS 111 ND1 A ? ? 1_555 G CU1 .  CU ? ? B HIS 111 B CU1 402 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc26 metalc ?    ? B ASP 113 OD2 ? ? ? 1_555 F CU  .  CU ? ? B ASP 113 B CU  401 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc27 metalc ?    ? B ASP 198 OD2 ? ? ? 1_555 F CU  .  CU ? ? B ASP 198 B CU  401 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc28 metalc ?    ? B ASP 198 OD2 ? ? ? 1_555 G CU1 .  CU ? ? B ASP 198 B CU1 402 1_555 ? ? ? ? ? ? ? 2.651 ? ? 
metalc29 metalc ?    ? B ASP 198 OD1 ? ? ? 1_555 H MG  .  MG ? ? B ASP 198 B MG  403 1_555 ? ? ? ? ? ? ? 2.406 ? ? 
metalc30 metalc ?    ? B ASP 198 OD2 ? ? ? 1_555 H MG  .  MG ? ? B ASP 198 B MG  403 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc31 metalc ?    ? B ASP 200 OD1 ? ? ? 1_555 G CU1 .  CU ? ? B ASP 200 B CU1 402 1_555 ? ? ? ? ? ? ? 2.608 ? ? 
metalc32 metalc ?    ? B ASP 200 OD2 ? ? ? 1_555 G CU1 .  CU ? ? B ASP 200 B CU1 402 1_555 ? ? ? ? ? ? ? 1.930 ? ? 
metalc33 metalc ?    ? B ASP 200 OD2 ? ? ? 1_555 H MG  .  MG ? ? B ASP 200 B MG  403 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc34 metalc ?    ? B GLU 241 OE2 ? ? ? 1_555 H MG  .  MG ? ? B GLU 241 B MG  403 1_555 ? ? ? ? ? ? ? 2.707 ? ? 
metalc35 metalc ?    ? F CU  .   CU  ? ? ? 1_555 J HOH .  O  ? ? B CU  401 B HOH 603 1_555 ? ? ? ? ? ? ? 2.197 ? ? 
metalc36 metalc ?    ? F CU  .   CU  ? ? ? 1_555 J HOH .  O  ? ? B CU  401 B HOH 647 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc37 metalc ?    ? G CU1 .   CU  ? ? ? 1_555 J HOH .  O  ? ? B CU1 402 B HOH 603 1_555 ? ? ? ? ? ? ? 1.897 ? ? 
metalc38 metalc ?    ? H MG  .   MG  ? ? ? 1_555 J HOH .  O  ? ? B MG  403 B HOH 576 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc39 metalc ?    ? H MG  .   MG  ? ? ? 1_555 J HOH .  O  ? ? B MG  403 B HOH 672 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
# 
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   O   ? A ASN 77  ? A ASN 77  ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 533 ? 1_555 88.1  ? 
2   O   ? A ASN 77  ? A ASN 77  ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 561 ? 1_555 86.7  ? 
3   O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 561 ? 1_555 78.3  ? 
4   O   ? A ASN 77  ? A ASN 77  ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 636 ? 1_555 94.9  ? 
5   O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 636 ? 1_555 104.0 ? 
6   O   ? I HOH .   ? A HOH 561 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 636 ? 1_555 177.2 ? 
7   O   ? A ASN 77  ? A ASN 77  ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 669 ? 1_555 99.7  ? 
8   O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 669 ? 1_555 163.4 ? 
9   O   ? I HOH .   ? A HOH 561 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 669 ? 1_555 87.5  ? 
10  O   ? I HOH .   ? A HOH 636 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 669 ? 1_555 90.0  ? 
11  O   ? A ASN 77  ? A ASN 77  ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 716 ? 1_555 170.7 ? 
12  O   ? I HOH .   ? A HOH 533 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 716 ? 1_555 83.1  ? 
13  O   ? I HOH .   ? A HOH 561 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 716 ? 1_555 94.7  ? 
14  O   ? I HOH .   ? A HOH 636 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 716 ? 1_555 84.1  ? 
15  O   ? I HOH .   ? A HOH 669 ? 1_555 MG ? E MG  . ? A MG  403 ? 1_555 O   ? I HOH .   ? A HOH 716 ? 1_555 89.6  ? 
16  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_555 106.0 ? 
17  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_555 105.6 ? 
18  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  ? 
19  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 94.2  ? 
20  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 82.8  ? 
21  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_555 157.3 ? 
22  SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 156.2 ? 
23  OD2 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 93.7  ? 
24  OD2 ? A ASP 113 ? A ASP 113 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 90.2  ? 
25  OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 74.9  ? 
26  SG  ? A CYS 86  ? A CYS 86  ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 656 ? 1_555 89.2  ? 
27  OD2 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 656 ? 1_555 164.1 ? 
28  OD2 ? A ASP 113 ? A ASP 113 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 656 ? 1_555 90.5  ? 
29  OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 656 ? 1_555 101.0 ? 
30  O   ? I HOH .   ? A HOH 528 ? 1_555 MN ? C MN  . ? A MN  401 ? 1_555 O   ? I HOH .   ? A HOH 656 ? 1_555 72.7  ? 
31  OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 ND1 ? A HIS 111 ? A HIS 111 ? 1_555 103.8 ? 
32  OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 88.5  ? 
33  ND1 ? A HIS 111 ? A HIS 111 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD2 ? A ASP 198 ? A ASP 198 ? 1_555 164.3 ? 
34  OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 83.5  ? 
35  ND1 ? A HIS 111 ? A HIS 111 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 100.5 ? 
36  OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD1 ? A ASP 200 ? A ASP 200 ? 1_555 90.4  ? 
37  OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 140.7 ? 
38  ND1 ? A HIS 111 ? A HIS 111 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 90.9  ? 
39  OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 85.5  ? 
40  OD1 ? A ASP 200 ? A ASP 200 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 OD2 ? A ASP 200 ? A ASP 200 ? 1_555 57.8  ? 
41  OD1 ? A ASP 109 ? A ASP 109 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 96.4  ? 
42  ND1 ? A HIS 111 ? A HIS 111 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 91.0  ? 
43  OD2 ? A ASP 198 ? A ASP 198 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 77.7  ? 
44  OD1 ? A ASP 200 ? A ASP 200 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 168.2 ? 
45  OD2 ? A ASP 200 ? A ASP 200 ? 1_555 MN ? D MN  . ? A MN  402 ? 1_555 O   ? I HOH .   ? A HOH 528 ? 1_555 120.0 ? 
46  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD  B B CSO 86  ? B CSO 86  ? 1_555 43.9  ? 
47  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 C B CSD 86  ? B CSD 86  ? 1_555 41.0  ? 
48  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 C B CSD 86  ? B CSD 86  ? 1_555 9.4   ? 
49  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 A B ASP 109 ? B ASP 109 ? 1_555 111.8 ? 
50  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 A B ASP 109 ? B ASP 109 ? 1_555 72.4  ? 
51  OD2 C B CSD 86  ? B CSD 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 A B ASP 109 ? B ASP 109 ? 1_555 79.7  ? 
52  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 B B ASP 109 ? B ASP 109 ? 1_555 128.2 ? 
53  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 B B ASP 109 ? B ASP 109 ? 1_555 86.8  ? 
54  OD2 C B CSD 86  ? B CSD 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 B B ASP 109 ? B ASP 109 ? 1_555 93.0  ? 
55  OD2 A B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 B B ASP 109 ? B ASP 109 ? 1_555 16.9  ? 
56  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 110.7 ? 
57  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 93.7  ? 
58  OD2 C B CSD 86  ? B CSD 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 87.5  ? 
59  OD2 A B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 91.6  ? 
60  OD2 B B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 113 ? B ASP 113 ? 1_555 81.9  ? 
61  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 79.3  ? 
62  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 95.4  ? 
63  OD2 C B CSD 86  ? B CSD 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 102.1 ? 
64  OD2 A B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 86.6  ? 
65  OD2 B B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 93.9  ? 
66  OD2 ? B ASP 113 ? B ASP 113 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 169.7 ? 
67  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 136.7 ? 
68  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 170.7 ? 
69  OD2 C B CSD 86  ? B CSD 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 177.6 ? 
70  OD2 A B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 102.1 ? 
71  OD2 B B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 89.1  ? 
72  OD2 ? B ASP 113 ? B ASP 113 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 94.0  ? 
73  OD2 ? B ASP 198 ? B ASP 198 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 76.5  ? 
74  SG  A B CYS 86  ? B CYS 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 78.3  ? 
75  OD  B B CSO 86  ? B CSO 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 117.0 ? 
76  OD2 C B CSD 86  ? B CSD 86  ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 109.3 ? 
77  OD2 A B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 169.9 ? 
78  OD2 B B ASP 109 ? B ASP 109 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 153.2 ? 
79  OD2 ? B ASP 113 ? B ASP 113 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 84.3  ? 
80  OD2 ? B ASP 198 ? B ASP 198 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 95.7  ? 
81  O   ? J HOH .   ? B HOH 603 ? 1_555 CU ? F CU  . ? B CU  401 ? 1_555 O   ? J HOH .   ? B HOH 647 ? 1_555 69.0  ? 
82  OD1 A B ASP 109 ? B ASP 109 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 ND1 A B HIS 111 ? B HIS 111 ? 1_555 106.4 ? 
83  OD1 A B ASP 109 ? B ASP 109 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 89.5  ? 
84  ND1 A B HIS 111 ? B HIS 111 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 162.8 ? 
85  OD1 A B ASP 109 ? B ASP 109 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD1 ? B ASP 200 ? B ASP 200 ? 1_555 77.4  ? 
86  ND1 A B HIS 111 ? B HIS 111 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD1 ? B ASP 200 ? B ASP 200 ? 1_555 103.8 ? 
87  OD2 ? B ASP 198 ? B ASP 198 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD1 ? B ASP 200 ? B ASP 200 ? 1_555 85.6  ? 
88  OD1 A B ASP 109 ? B ASP 109 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 131.2 ? 
89  ND1 A B HIS 111 ? B HIS 111 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 95.0  ? 
90  OD2 ? B ASP 198 ? B ASP 198 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 78.5  ? 
91  OD1 ? B ASP 200 ? B ASP 200 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 54.8  ? 
92  OD1 A B ASP 109 ? B ASP 109 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 92.5  ? 
93  ND1 A B HIS 111 ? B HIS 111 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 96.8  ? 
94  OD2 ? B ASP 198 ? B ASP 198 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 75.7  ? 
95  OD1 ? B ASP 200 ? B ASP 200 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 158.9 ? 
96  OD2 ? B ASP 200 ? B ASP 200 ? 1_555 CU ? G CU1 . ? B CU1 402 ? 1_555 O   ? J HOH .   ? B HOH 603 ? 1_555 128.5 ? 
97  OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 59.3  ? 
98  OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 85.2  ? 
99  OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 88.0  ? 
100 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 107.7 ? 
101 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 113.9 ? 
102 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 157.9 ? 
103 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 576 ? 1_555 97.5  ? 
104 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 576 ? 1_555 156.7 ? 
105 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 576 ? 1_555 92.2  ? 
106 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 576 ? 1_555 68.8  ? 
107 OD1 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 672 ? 1_555 163.3 ? 
108 OD2 ? B ASP 198 ? B ASP 198 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 672 ? 1_555 104.1 ? 
109 OD2 ? B ASP 200 ? B ASP 200 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 672 ? 1_555 93.2  ? 
110 OE2 ? B GLU 241 ? B GLU 241 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 672 ? 1_555 79.4  ? 
111 O   ? J HOH .   ? B HOH 576 ? 1_555 MG ? H MG  . ? B MG  403 ? 1_555 O   ? J HOH .   ? B HOH 672 ? 1_555 99.2  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CSO B 86 B . . . . CSO B 86 ? 1_555 . . . . . . . CYS 1 CSO Hydroxylation 'Named protein modification' 
2 CSD B 86 C . . . . CSD B 86 ? 1_555 . . . . . . . CYS 1 CSD Oxidation     'Named protein modification' 
3 CSD B 86 C . . . . CSD B 86 ? 1_555 . . . . . . . CYS 2 CSD Hydroxylation '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 VAL A 40  ? O VAL A 40  N VAL A 6   ? N VAL A 6   
AA1 2 3 N ASP A 3   ? N ASP A 3   O VAL A 80  ? O VAL A 80  
AA1 3 4 N LEU A 81  ? N LEU A 81  O LEU A 239 ? O LEU A 239 
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 ARG A 172 ? O ARG A 172 
AA2 1 2 O VAL B 40  ? O VAL B 40  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 LEU B 81  ? N LEU B 81  O LEU B 239 ? O LEU B 239 
AA2 4 5 O ILE B 235 ? O ILE B 235 N VAL B 193 ? N VAL B 193 
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                   9IXD 
_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  ? ? -97.87  50.68   
2  1 ALA A 143 ? ? -145.40 -128.41 
3  1 LYS A 189 ? ? 55.59   -130.22 
4  1 PRO A 208 ? ? -55.16  71.58   
5  1 GLU A 241 ? ? 71.30   50.07   
6  1 ASP B 48  ? ? -101.12 66.61   
7  1 HIS B 111 ? B -121.66 -50.35  
8  1 ALA B 143 ? ? -144.94 -127.28 
9  1 ARG B 156 ? A -149.52 -18.80  
10 1 ASP B 157 ? A -102.81 75.23   
11 1 LYS B 189 ? ? 57.01   -128.42 
12 1 ASP B 215 ? A 61.41   60.78   
13 1 GLU B 241 ? ? 79.67   39.85   
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       769 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.92 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A 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  
CSD N    N  N N 74  
CSD CA   C  N R 75  
CSD CB   C  N N 76  
CSD SG   S  N N 77  
CSD C    C  N N 78  
CSD O    O  N N 79  
CSD OXT  O  N N 80  
CSD OD1  O  N N 81  
CSD OD2  O  N N 82  
CSD H    H  N N 83  
CSD H2   H  N N 84  
CSD HA   H  N N 85  
CSD HB2  H  N N 86  
CSD HB3  H  N N 87  
CSD HXT  H  N N 88  
CSD HD2  H  N N 89  
CSO N    N  N N 90  
CSO CA   C  N R 91  
CSO CB   C  N N 92  
CSO SG   S  N N 93  
CSO C    C  N N 94  
CSO O    O  N N 95  
CSO OXT  O  N N 96  
CSO OD   O  N N 97  
CSO H    H  N N 98  
CSO H2   H  N N 99  
CSO HA   H  N N 100 
CSO HB2  H  N N 101 
CSO HB3  H  N N 102 
CSO HXT  H  N N 103 
CSO HD   H  N N 104 
CU  CU   CU N N 105 
CU1 CU   CU N N 106 
CYS N    N  N N 107 
CYS CA   C  N R 108 
CYS C    C  N N 109 
CYS O    O  N N 110 
CYS CB   C  N N 111 
CYS SG   S  N N 112 
CYS OXT  O  N N 113 
CYS H    H  N N 114 
CYS H2   H  N N 115 
CYS HA   H  N N 116 
CYS HB2  H  N N 117 
CYS HB3  H  N N 118 
CYS HG   H  N N 119 
CYS HXT  H  N N 120 
GLN N    N  N N 121 
GLN CA   C  N S 122 
GLN C    C  N N 123 
GLN O    O  N N 124 
GLN CB   C  N N 125 
GLN CG   C  N N 126 
GLN CD   C  N N 127 
GLN OE1  O  N N 128 
GLN NE2  N  N N 129 
GLN OXT  O  N N 130 
GLN H    H  N N 131 
GLN H2   H  N N 132 
GLN HA   H  N N 133 
GLN HB2  H  N N 134 
GLN HB3  H  N N 135 
GLN HG2  H  N N 136 
GLN HG3  H  N N 137 
GLN HE21 H  N N 138 
GLN HE22 H  N N 139 
GLN HXT  H  N N 140 
GLU N    N  N N 141 
GLU CA   C  N S 142 
GLU C    C  N N 143 
GLU O    O  N N 144 
GLU CB   C  N N 145 
GLU CG   C  N N 146 
GLU CD   C  N N 147 
GLU OE1  O  N N 148 
GLU OE2  O  N N 149 
GLU OXT  O  N N 150 
GLU H    H  N N 151 
GLU H2   H  N N 152 
GLU HA   H  N N 153 
GLU HB2  H  N N 154 
GLU HB3  H  N N 155 
GLU HG2  H  N N 156 
GLU HG3  H  N N 157 
GLU HE2  H  N N 158 
GLU HXT  H  N N 159 
GLY N    N  N N 160 
GLY CA   C  N N 161 
GLY C    C  N N 162 
GLY O    O  N N 163 
GLY OXT  O  N N 164 
GLY H    H  N N 165 
GLY H2   H  N N 166 
GLY HA2  H  N N 167 
GLY HA3  H  N N 168 
GLY HXT  H  N N 169 
HIS N    N  N N 170 
HIS CA   C  N S 171 
HIS C    C  N N 172 
HIS O    O  N N 173 
HIS CB   C  N N 174 
HIS CG   C  Y N 175 
HIS ND1  N  Y N 176 
HIS CD2  C  Y N 177 
HIS CE1  C  Y N 178 
HIS NE2  N  Y N 179 
HIS OXT  O  N N 180 
HIS H    H  N N 181 
HIS H2   H  N N 182 
HIS HA   H  N N 183 
HIS HB2  H  N N 184 
HIS HB3  H  N N 185 
HIS HD1  H  N N 186 
HIS HD2  H  N N 187 
HIS HE1  H  N N 188 
HIS HE2  H  N N 189 
HIS HXT  H  N N 190 
HOH O    O  N N 191 
HOH H1   H  N N 192 
HOH H2   H  N N 193 
ILE N    N  N N 194 
ILE CA   C  N S 195 
ILE C    C  N N 196 
ILE O    O  N N 197 
ILE CB   C  N S 198 
ILE CG1  C  N N 199 
ILE CG2  C  N N 200 
ILE CD1  C  N N 201 
ILE OXT  O  N N 202 
ILE H    H  N N 203 
ILE H2   H  N N 204 
ILE HA   H  N N 205 
ILE HB   H  N N 206 
ILE HG12 H  N N 207 
ILE HG13 H  N N 208 
ILE HG21 H  N N 209 
ILE HG22 H  N N 210 
ILE HG23 H  N N 211 
ILE HD11 H  N N 212 
ILE HD12 H  N N 213 
ILE HD13 H  N N 214 
ILE HXT  H  N N 215 
LEU N    N  N N 216 
LEU CA   C  N S 217 
LEU C    C  N N 218 
LEU O    O  N N 219 
LEU CB   C  N N 220 
LEU CG   C  N N 221 
LEU CD1  C  N N 222 
LEU CD2  C  N N 223 
LEU OXT  O  N N 224 
LEU H    H  N N 225 
LEU H2   H  N N 226 
LEU HA   H  N N 227 
LEU HB2  H  N N 228 
LEU HB3  H  N N 229 
LEU HG   H  N N 230 
LEU HD11 H  N N 231 
LEU HD12 H  N N 232 
LEU HD13 H  N N 233 
LEU HD21 H  N N 234 
LEU HD22 H  N N 235 
LEU HD23 H  N N 236 
LEU HXT  H  N N 237 
LYS N    N  N N 238 
LYS CA   C  N S 239 
LYS C    C  N N 240 
LYS O    O  N N 241 
LYS CB   C  N N 242 
LYS CG   C  N N 243 
LYS CD   C  N N 244 
LYS CE   C  N N 245 
LYS NZ   N  N N 246 
LYS OXT  O  N N 247 
LYS H    H  N N 248 
LYS H2   H  N N 249 
LYS HA   H  N N 250 
LYS HB2  H  N N 251 
LYS HB3  H  N N 252 
LYS HG2  H  N N 253 
LYS HG3  H  N N 254 
LYS HD2  H  N N 255 
LYS HD3  H  N N 256 
LYS HE2  H  N N 257 
LYS HE3  H  N N 258 
LYS HZ1  H  N N 259 
LYS HZ2  H  N N 260 
LYS HZ3  H  N N 261 
LYS HXT  H  N N 262 
MET N    N  N N 263 
MET CA   C  N S 264 
MET C    C  N N 265 
MET O    O  N N 266 
MET CB   C  N N 267 
MET CG   C  N N 268 
MET SD   S  N N 269 
MET CE   C  N N 270 
MET OXT  O  N N 271 
MET H    H  N N 272 
MET H2   H  N N 273 
MET HA   H  N N 274 
MET HB2  H  N N 275 
MET HB3  H  N N 276 
MET HG2  H  N N 277 
MET HG3  H  N N 278 
MET HE1  H  N N 279 
MET HE2  H  N N 280 
MET HE3  H  N N 281 
MET HXT  H  N N 282 
MG  MG   MG N N 283 
MN  MN   MN N N 284 
PHE N    N  N N 285 
PHE CA   C  N S 286 
PHE C    C  N N 287 
PHE O    O  N N 288 
PHE CB   C  N N 289 
PHE CG   C  Y N 290 
PHE CD1  C  Y N 291 
PHE CD2  C  Y N 292 
PHE CE1  C  Y N 293 
PHE CE2  C  Y N 294 
PHE CZ   C  Y N 295 
PHE OXT  O  N N 296 
PHE H    H  N N 297 
PHE H2   H  N N 298 
PHE HA   H  N N 299 
PHE HB2  H  N N 300 
PHE HB3  H  N N 301 
PHE HD1  H  N N 302 
PHE HD2  H  N N 303 
PHE HE1  H  N N 304 
PHE HE2  H  N N 305 
PHE HZ   H  N N 306 
PHE HXT  H  N N 307 
PRO N    N  N N 308 
PRO CA   C  N S 309 
PRO C    C  N N 310 
PRO O    O  N N 311 
PRO CB   C  N N 312 
PRO CG   C  N N 313 
PRO CD   C  N N 314 
PRO OXT  O  N N 315 
PRO H    H  N N 316 
PRO HA   H  N N 317 
PRO HB2  H  N N 318 
PRO HB3  H  N N 319 
PRO HG2  H  N N 320 
PRO HG3  H  N N 321 
PRO HD2  H  N N 322 
PRO HD3  H  N N 323 
PRO HXT  H  N N 324 
SER N    N  N N 325 
SER CA   C  N S 326 
SER C    C  N N 327 
SER O    O  N N 328 
SER CB   C  N N 329 
SER OG   O  N N 330 
SER OXT  O  N N 331 
SER H    H  N N 332 
SER H2   H  N N 333 
SER HA   H  N N 334 
SER HB2  H  N N 335 
SER HB3  H  N N 336 
SER HG   H  N N 337 
SER HXT  H  N N 338 
THR N    N  N N 339 
THR CA   C  N S 340 
THR C    C  N N 341 
THR O    O  N N 342 
THR CB   C  N R 343 
THR OG1  O  N N 344 
THR CG2  C  N N 345 
THR OXT  O  N N 346 
THR H    H  N N 347 
THR H2   H  N N 348 
THR HA   H  N N 349 
THR HB   H  N N 350 
THR HG1  H  N N 351 
THR HG21 H  N N 352 
THR HG22 H  N N 353 
THR HG23 H  N N 354 
THR HXT  H  N N 355 
TRP N    N  N N 356 
TRP CA   C  N S 357 
TRP C    C  N N 358 
TRP O    O  N N 359 
TRP CB   C  N N 360 
TRP CG   C  Y N 361 
TRP CD1  C  Y N 362 
TRP CD2  C  Y N 363 
TRP NE1  N  Y N 364 
TRP CE2  C  Y N 365 
TRP CE3  C  Y N 366 
TRP CZ2  C  Y N 367 
TRP CZ3  C  Y N 368 
TRP CH2  C  Y N 369 
TRP OXT  O  N N 370 
TRP H    H  N N 371 
TRP H2   H  N N 372 
TRP HA   H  N N 373 
TRP HB2  H  N N 374 
TRP HB3  H  N N 375 
TRP HD1  H  N N 376 
TRP HE1  H  N N 377 
TRP HE3  H  N N 378 
TRP HZ2  H  N N 379 
TRP HZ3  H  N N 380 
TRP HH2  H  N N 381 
TRP HXT  H  N N 382 
TYR N    N  N N 383 
TYR CA   C  N S 384 
TYR C    C  N N 385 
TYR O    O  N N 386 
TYR CB   C  N N 387 
TYR CG   C  Y N 388 
TYR CD1  C  Y N 389 
TYR CD2  C  Y N 390 
TYR CE1  C  Y N 391 
TYR CE2  C  Y N 392 
TYR CZ   C  Y N 393 
TYR OH   O  N N 394 
TYR OXT  O  N N 395 
TYR H    H  N N 396 
TYR H2   H  N N 397 
TYR HA   H  N N 398 
TYR HB2  H  N N 399 
TYR HB3  H  N N 400 
TYR HD1  H  N N 401 
TYR HD2  H  N N 402 
TYR HE1  H  N N 403 
TYR HE2  H  N N 404 
TYR HH   H  N N 405 
TYR HXT  H  N N 406 
VAL N    N  N N 407 
VAL CA   C  N S 408 
VAL C    C  N N 409 
VAL O    O  N N 410 
VAL CB   C  N N 411 
VAL CG1  C  N N 412 
VAL CG2  C  N N 413 
VAL OXT  O  N N 414 
VAL H    H  N N 415 
VAL H2   H  N N 416 
VAL HA   H  N N 417 
VAL HB   H  N N 418 
VAL HG11 H  N N 419 
VAL HG12 H  N N 420 
VAL HG13 H  N N 421 
VAL HG21 H  N N 422 
VAL HG22 H  N N 423 
VAL HG23 H  N N 424 
VAL HXT  H  N N 425 
# 
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  
CSD N   CA   sing N N 70  
CSD N   H    sing N N 71  
CSD N   H2   sing N N 72  
CSD CA  CB   sing N N 73  
CSD CA  C    sing N N 74  
CSD CA  HA   sing N N 75  
CSD CB  SG   sing N N 76  
CSD CB  HB2  sing N N 77  
CSD CB  HB3  sing N N 78  
CSD SG  OD1  doub N N 79  
CSD SG  OD2  sing N N 80  
CSD C   O    doub N N 81  
CSD C   OXT  sing N N 82  
CSD OXT HXT  sing N N 83  
CSD OD2 HD2  sing N N 84  
CSO N   CA   sing N N 85  
CSO N   H    sing N N 86  
CSO N   H2   sing N N 87  
CSO CA  CB   sing N N 88  
CSO CA  C    sing N N 89  
CSO CA  HA   sing N N 90  
CSO CB  SG   sing N N 91  
CSO CB  HB2  sing N N 92  
CSO CB  HB3  sing N N 93  
CSO SG  OD   sing N N 94  
CSO C   O    doub N N 95  
CSO C   OXT  sing N N 96  
CSO OXT HXT  sing N N 97  
CSO OD  HD   sing N N 98  
CYS N   CA   sing N N 99  
CYS N   H    sing N N 100 
CYS N   H2   sing N N 101 
CYS CA  C    sing N N 102 
CYS CA  CB   sing N N 103 
CYS CA  HA   sing N N 104 
CYS C   O    doub N N 105 
CYS C   OXT  sing N N 106 
CYS CB  SG   sing N N 107 
CYS CB  HB2  sing N N 108 
CYS CB  HB3  sing N N 109 
CYS SG  HG   sing N N 110 
CYS OXT HXT  sing N N 111 
GLN N   CA   sing N N 112 
GLN N   H    sing N N 113 
GLN N   H2   sing N N 114 
GLN CA  C    sing N N 115 
GLN CA  CB   sing N N 116 
GLN CA  HA   sing N N 117 
GLN C   O    doub N N 118 
GLN C   OXT  sing N N 119 
GLN CB  CG   sing N N 120 
GLN CB  HB2  sing N N 121 
GLN CB  HB3  sing N N 122 
GLN CG  CD   sing N N 123 
GLN CG  HG2  sing N N 124 
GLN CG  HG3  sing N N 125 
GLN CD  OE1  doub N N 126 
GLN CD  NE2  sing N N 127 
GLN NE2 HE21 sing N N 128 
GLN NE2 HE22 sing N N 129 
GLN OXT HXT  sing N N 130 
GLU N   CA   sing N N 131 
GLU N   H    sing N N 132 
GLU N   H2   sing N N 133 
GLU CA  C    sing N N 134 
GLU CA  CB   sing N N 135 
GLU CA  HA   sing N N 136 
GLU C   O    doub N N 137 
GLU C   OXT  sing N N 138 
GLU CB  CG   sing N N 139 
GLU CB  HB2  sing N N 140 
GLU CB  HB3  sing N N 141 
GLU CG  CD   sing N N 142 
GLU CG  HG2  sing N N 143 
GLU CG  HG3  sing N N 144 
GLU CD  OE1  doub N N 145 
GLU CD  OE2  sing N N 146 
GLU OE2 HE2  sing N N 147 
GLU OXT HXT  sing N N 148 
GLY N   CA   sing N N 149 
GLY N   H    sing N N 150 
GLY N   H2   sing N N 151 
GLY CA  C    sing N N 152 
GLY CA  HA2  sing N N 153 
GLY CA  HA3  sing N N 154 
GLY C   O    doub N N 155 
GLY C   OXT  sing N N 156 
GLY OXT HXT  sing N N 157 
HIS N   CA   sing N N 158 
HIS N   H    sing N N 159 
HIS N   H2   sing N N 160 
HIS CA  C    sing N N 161 
HIS CA  CB   sing N N 162 
HIS CA  HA   sing N N 163 
HIS C   O    doub N N 164 
HIS C   OXT  sing N N 165 
HIS CB  CG   sing N N 166 
HIS CB  HB2  sing N N 167 
HIS CB  HB3  sing N N 168 
HIS CG  ND1  sing Y N 169 
HIS CG  CD2  doub Y N 170 
HIS ND1 CE1  doub Y N 171 
HIS ND1 HD1  sing N N 172 
HIS CD2 NE2  sing Y N 173 
HIS CD2 HD2  sing N N 174 
HIS CE1 NE2  sing Y N 175 
HIS CE1 HE1  sing N N 176 
HIS NE2 HE2  sing N N 177 
HIS OXT HXT  sing N N 178 
HOH O   H1   sing N N 179 
HOH O   H2   sing N N 180 
ILE N   CA   sing N N 181 
ILE N   H    sing N N 182 
ILE N   H2   sing N N 183 
ILE CA  C    sing N N 184 
ILE CA  CB   sing N N 185 
ILE CA  HA   sing N N 186 
ILE C   O    doub N N 187 
ILE C   OXT  sing N N 188 
ILE CB  CG1  sing N N 189 
ILE CB  CG2  sing N N 190 
ILE CB  HB   sing N N 191 
ILE CG1 CD1  sing N N 192 
ILE CG1 HG12 sing N N 193 
ILE CG1 HG13 sing N N 194 
ILE CG2 HG21 sing N N 195 
ILE CG2 HG22 sing N N 196 
ILE CG2 HG23 sing N N 197 
ILE CD1 HD11 sing N N 198 
ILE CD1 HD12 sing N N 199 
ILE CD1 HD13 sing N N 200 
ILE OXT HXT  sing N N 201 
LEU N   CA   sing N N 202 
LEU N   H    sing N N 203 
LEU N   H2   sing N N 204 
LEU CA  C    sing N N 205 
LEU CA  CB   sing N N 206 
LEU CA  HA   sing N N 207 
LEU C   O    doub N N 208 
LEU C   OXT  sing N N 209 
LEU CB  CG   sing N N 210 
LEU CB  HB2  sing N N 211 
LEU CB  HB3  sing N N 212 
LEU CG  CD1  sing N N 213 
LEU CG  CD2  sing N N 214 
LEU CG  HG   sing N N 215 
LEU CD1 HD11 sing N N 216 
LEU CD1 HD12 sing N N 217 
LEU CD1 HD13 sing N N 218 
LEU CD2 HD21 sing N N 219 
LEU CD2 HD22 sing N N 220 
LEU CD2 HD23 sing N N 221 
LEU OXT HXT  sing N N 222 
LYS N   CA   sing N N 223 
LYS N   H    sing N N 224 
LYS N   H2   sing N N 225 
LYS CA  C    sing N N 226 
LYS CA  CB   sing N N 227 
LYS CA  HA   sing N N 228 
LYS C   O    doub N N 229 
LYS C   OXT  sing N N 230 
LYS CB  CG   sing N N 231 
LYS CB  HB2  sing N N 232 
LYS CB  HB3  sing N N 233 
LYS CG  CD   sing N N 234 
LYS CG  HG2  sing N N 235 
LYS CG  HG3  sing N N 236 
LYS CD  CE   sing N N 237 
LYS CD  HD2  sing N N 238 
LYS CD  HD3  sing N N 239 
LYS CE  NZ   sing N N 240 
LYS CE  HE2  sing N N 241 
LYS CE  HE3  sing N N 242 
LYS NZ  HZ1  sing N N 243 
LYS NZ  HZ2  sing N N 244 
LYS NZ  HZ3  sing N N 245 
LYS OXT HXT  sing N N 246 
MET N   CA   sing N N 247 
MET N   H    sing N N 248 
MET N   H2   sing N N 249 
MET CA  C    sing N N 250 
MET CA  CB   sing N N 251 
MET CA  HA   sing N N 252 
MET C   O    doub N N 253 
MET C   OXT  sing N N 254 
MET CB  CG   sing N N 255 
MET CB  HB2  sing N N 256 
MET CB  HB3  sing N N 257 
MET CG  SD   sing N N 258 
MET CG  HG2  sing N N 259 
MET CG  HG3  sing N N 260 
MET SD  CE   sing N N 261 
MET CE  HE1  sing N N 262 
MET CE  HE2  sing N N 263 
MET CE  HE3  sing N N 264 
MET OXT HXT  sing N N 265 
PHE N   CA   sing N N 266 
PHE N   H    sing N N 267 
PHE N   H2   sing N N 268 
PHE CA  C    sing N N 269 
PHE CA  CB   sing N N 270 
PHE CA  HA   sing N N 271 
PHE C   O    doub N N 272 
PHE C   OXT  sing N N 273 
PHE CB  CG   sing N N 274 
PHE CB  HB2  sing N N 275 
PHE CB  HB3  sing N N 276 
PHE CG  CD1  doub Y N 277 
PHE CG  CD2  sing Y N 278 
PHE CD1 CE1  sing Y N 279 
PHE CD1 HD1  sing N N 280 
PHE CD2 CE2  doub Y N 281 
PHE CD2 HD2  sing N N 282 
PHE CE1 CZ   doub Y N 283 
PHE CE1 HE1  sing N N 284 
PHE CE2 CZ   sing Y N 285 
PHE CE2 HE2  sing N N 286 
PHE CZ  HZ   sing N N 287 
PHE OXT HXT  sing N N 288 
PRO N   CA   sing N N 289 
PRO N   CD   sing N N 290 
PRO N   H    sing N N 291 
PRO CA  C    sing N N 292 
PRO CA  CB   sing N N 293 
PRO CA  HA   sing N N 294 
PRO C   O    doub N N 295 
PRO C   OXT  sing N N 296 
PRO CB  CG   sing N N 297 
PRO CB  HB2  sing N N 298 
PRO CB  HB3  sing N N 299 
PRO CG  CD   sing N N 300 
PRO CG  HG2  sing N N 301 
PRO CG  HG3  sing N N 302 
PRO CD  HD2  sing N N 303 
PRO CD  HD3  sing N N 304 
PRO OXT HXT  sing N N 305 
SER N   CA   sing N N 306 
SER N   H    sing N N 307 
SER N   H2   sing N N 308 
SER CA  C    sing N N 309 
SER CA  CB   sing N N 310 
SER CA  HA   sing N N 311 
SER C   O    doub N N 312 
SER C   OXT  sing N N 313 
SER CB  OG   sing N N 314 
SER CB  HB2  sing N N 315 
SER CB  HB3  sing N N 316 
SER OG  HG   sing N N 317 
SER OXT HXT  sing N N 318 
THR N   CA   sing N N 319 
THR N   H    sing N N 320 
THR N   H2   sing N N 321 
THR CA  C    sing N N 322 
THR CA  CB   sing N N 323 
THR CA  HA   sing N N 324 
THR C   O    doub N N 325 
THR C   OXT  sing N N 326 
THR CB  OG1  sing N N 327 
THR CB  CG2  sing N N 328 
THR CB  HB   sing N N 329 
THR OG1 HG1  sing N N 330 
THR CG2 HG21 sing N N 331 
THR CG2 HG22 sing N N 332 
THR CG2 HG23 sing N N 333 
THR OXT HXT  sing N N 334 
TRP N   CA   sing N N 335 
TRP N   H    sing N N 336 
TRP N   H2   sing N N 337 
TRP CA  C    sing N N 338 
TRP CA  CB   sing N N 339 
TRP CA  HA   sing N N 340 
TRP C   O    doub N N 341 
TRP C   OXT  sing N N 342 
TRP CB  CG   sing N N 343 
TRP CB  HB2  sing N N 344 
TRP CB  HB3  sing N N 345 
TRP CG  CD1  doub Y N 346 
TRP CG  CD2  sing Y N 347 
TRP CD1 NE1  sing Y N 348 
TRP CD1 HD1  sing N N 349 
TRP CD2 CE2  doub Y N 350 
TRP CD2 CE3  sing Y N 351 
TRP NE1 CE2  sing Y N 352 
TRP NE1 HE1  sing N N 353 
TRP CE2 CZ2  sing Y N 354 
TRP CE3 CZ3  doub Y N 355 
TRP CE3 HE3  sing N N 356 
TRP CZ2 CH2  doub Y N 357 
TRP CZ2 HZ2  sing N N 358 
TRP CZ3 CH2  sing Y N 359 
TRP CZ3 HZ3  sing N N 360 
TRP CH2 HH2  sing N N 361 
TRP OXT HXT  sing N N 362 
TYR N   CA   sing N N 363 
TYR N   H    sing N N 364 
TYR N   H2   sing N N 365 
TYR CA  C    sing N N 366 
TYR CA  CB   sing N N 367 
TYR CA  HA   sing N N 368 
TYR C   O    doub N N 369 
TYR C   OXT  sing N N 370 
TYR CB  CG   sing N N 371 
TYR CB  HB2  sing N N 372 
TYR CB  HB3  sing N N 373 
TYR CG  CD1  doub Y N 374 
TYR CG  CD2  sing Y N 375 
TYR CD1 CE1  sing Y N 376 
TYR CD1 HD1  sing N N 377 
TYR CD2 CE2  doub Y N 378 
TYR CD2 HD2  sing N N 379 
TYR CE1 CZ   doub Y N 380 
TYR CE1 HE1  sing N N 381 
TYR CE2 CZ   sing Y N 382 
TYR CE2 HE2  sing N N 383 
TYR CZ  OH   sing N N 384 
TYR OH  HH   sing N N 385 
TYR OXT HXT  sing N N 386 
VAL N   CA   sing N N 387 
VAL N   H    sing N N 388 
VAL N   H2   sing N N 389 
VAL CA  C    sing N N 390 
VAL CA  CB   sing N N 391 
VAL CA  HA   sing N N 392 
VAL C   O    doub N N 393 
VAL C   OXT  sing N N 394 
VAL CB  CG1  sing N N 395 
VAL CB  CG2  sing N N 396 
VAL CB  HB   sing N N 397 
VAL CG1 HG11 sing N N 398 
VAL CG1 HG12 sing N N 399 
VAL CG1 HG13 sing N N 400 
VAL CG2 HG21 sing N N 401 
VAL CG2 HG22 sing N N 402 
VAL CG2 HG23 sing N N 403 
VAL OXT HXT  sing N N 404 
# 
_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                    9IXD 
_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]   0.021552 
_atom_sites.fract_transf_matrix[1][2]   -0.007729 
_atom_sites.fract_transf_matrix[1][3]   -0.001353 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022534 
_atom_sites.fract_transf_matrix[2][3]   -0.001901 
_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]   0.016969 
_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  
CU 
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   ? 35.859 25.487  45.530  1.00 36.01 ?  1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 35.127 24.513  46.323  1.00 37.71 ?  1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 35.892 23.193  46.407  1.00 30.17 ?  1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 37.090 23.162  46.135  1.00 22.87 ?  1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 33.733 24.311  45.744  1.00 45.31 ?  1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 32.649 24.701  46.719  1.00 58.39 ?  1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 32.484 23.394  47.934  1.00 74.39 ?  1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 31.957 22.082  46.834  1.00 47.59 ?  1   MET A CE  1 
ATOM   9    N  N   . ILE A 1 2   ? 35.204 22.117  46.781  1.00 26.96 ?  2   ILE A N   1 
ATOM   10   C  CA  . ILE A 1 2   ? 35.824 20.846  47.149  1.00 23.28 ?  2   ILE A CA  1 
ATOM   11   C  C   . ILE A 1 2   ? 35.256 19.729  46.279  1.00 23.68 ?  2   ILE A C   1 
ATOM   12   O  O   . ILE A 1 2   ? 34.033 19.601  46.148  1.00 26.10 ?  2   ILE A O   1 
ATOM   13   C  CB  . ILE A 1 2   ? 35.594 20.523  48.638  1.00 21.46 ?  2   ILE A CB  1 
ATOM   14   C  CG1 . ILE A 1 2   ? 36.199 21.607  49.537  1.00 22.70 ?  2   ILE A CG1 1 
ATOM   15   C  CG2 . ILE A 1 2   ? 36.146 19.157  48.984  1.00 22.94 ?  2   ILE A CG2 1 
ATOM   16   C  CD1 . ILE A 1 2   ? 35.812 21.504  51.008  1.00 24.99 ?  2   ILE A CD1 1 
ATOM   17   N  N   . ASP A 1 3   ? 36.141 18.906  45.715  1.00 18.79 ?  3   ASP A N   1 
ATOM   18   C  CA  . ASP A 1 3   ? 35.777 17.627  45.101  1.00 18.37 ?  3   ASP A CA  1 
ATOM   19   C  C   . ASP A 1 3   ? 36.103 16.500  46.080  1.00 20.00 ?  3   ASP A C   1 
ATOM   20   O  O   . ASP A 1 3   ? 37.272 16.318  46.434  1.00 21.11 ?  3   ASP A O   1 
ATOM   21   C  CB  . ASP A 1 3   ? 36.552 17.376  43.811  1.00 19.35 ?  3   ASP A CB  1 
ATOM   22   C  CG  . ASP A 1 3   ? 36.206 18.342  42.690  1.00 25.41 ?  3   ASP A CG  1 
ATOM   23   O  OD1 . ASP A 1 3   ? 35.079 18.885  42.670  1.00 30.66 ?  3   ASP A OD1 1 
ATOM   24   O  OD2 . ASP A 1 3   ? 37.073 18.527  41.802  1.00 27.22 -1 3   ASP A OD2 1 
ATOM   25   N  N   . LEU A 1 4   ? 35.096 15.731  46.493  1.00 16.47 ?  4   LEU A N   1 
ATOM   26   C  CA  . LEU A 1 4   ? 35.275 14.624  47.424  1.00 15.76 ?  4   LEU A CA  1 
ATOM   27   C  C   . LEU A 1 4   ? 35.205 13.306  46.658  1.00 18.27 ?  4   LEU A C   1 
ATOM   28   O  O   . LEU A 1 4   ? 34.201 13.024  45.987  1.00 19.55 ?  4   LEU A O   1 
ATOM   29   C  CB  . LEU A 1 4   ? 34.207 14.656  48.517  1.00 19.29 ?  4   LEU A CB  1 
ATOM   30   C  CG  . LEU A 1 4   ? 34.193 13.479  49.490  1.00 17.77 ?  4   LEU A CG  1 
ATOM   31   C  CD1 . LEU A 1 4   ? 35.515 13.412  50.273  1.00 21.87 ?  4   LEU A CD1 1 
ATOM   32   C  CD2 . LEU A 1 4   ? 33.023 13.589  50.450  1.00 18.31 ?  4   LEU A CD2 1 
ATOM   33   N  N   . ILE A 1 5   ? 36.271 12.509  46.746  1.00 16.17 ?  5   ILE A N   1 
ATOM   34   C  CA  . ILE A 1 5   ? 36.366 11.195  46.117  1.00 16.06 ?  5   ILE A CA  1 
ATOM   35   C  C   . ILE A 1 5   ? 36.636 10.180  47.226  1.00 20.46 ?  5   ILE A C   1 
ATOM   36   O  O   . ILE A 1 5   ? 37.478 10.426  48.096  1.00 17.89 ?  5   ILE A O   1 
ATOM   37   C  CB  . ILE A 1 5   ? 37.478 11.163  45.050  1.00 16.30 ?  5   ILE A CB  1 
ATOM   38   C  CG1 . ILE A 1 5   ? 37.225 12.216  43.961  1.00 19.50 ?  5   ILE A CG1 1 
ATOM   39   C  CG2 . ILE A 1 5   ? 37.624 9.762   44.441  1.00 17.02 ?  5   ILE A CG2 1 
ATOM   40   C  CD1 . ILE A 1 5   ? 38.438 12.538  43.123  1.00 20.60 ?  5   ILE A CD1 1 
ATOM   41   N  N   . VAL A 1 6   ? 35.909 9.060   47.218  1.00 15.93 ?  6   VAL A N   1 
ATOM   42   C  CA  . VAL A 1 6   ? 35.958 8.090   48.314  1.00 14.40 ?  6   VAL A CA  1 
ATOM   43   C  C   . VAL A 1 6   ? 36.247 6.714   47.738  1.00 18.09 ?  6   VAL A C   1 
ATOM   44   O  O   . VAL A 1 6   ? 35.491 6.226   46.887  1.00 18.55 ?  6   VAL A O   1 
ATOM   45   C  CB  . VAL A 1 6   ? 34.653 8.049   49.121  1.00 13.98 ?  6   VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 6   ? 34.834 7.196   50.376  1.00 13.73 ?  6   VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 6   ? 34.200 9.455   49.466  1.00 16.65 ?  6   VAL A CG2 1 
ATOM   48   N  N   . SER A 1 7   ? 37.319 6.078   48.202  1.00 15.28 ?  7   SER A N   1 
ATOM   49   C  CA  . SER A 1 7   ? 37.594 4.695   47.821  1.00 14.71 ?  7   SER A CA  1 
ATOM   50   C  C   . SER A 1 7   ? 36.865 3.736   48.751  1.00 17.25 ?  7   SER A C   1 
ATOM   51   O  O   . SER A 1 7   ? 36.970 3.844   49.981  1.00 17.97 ?  7   SER A O   1 
ATOM   52   C  CB  . SER A 1 7   ? 39.090 4.386   47.833  1.00 18.43 ?  7   SER A CB  1 
ATOM   53   O  OG  . SER A 1 7   ? 39.300 3.003   47.530  1.00 20.17 ?  7   SER A OG  1 
ATOM   54   N  N   . GLN A 1 8   ? 36.101 2.813   48.153  1.00 17.18 ?  8   GLN A N   1 
ATOM   55   C  CA  . GLN A 1 8   ? 35.405 1.759   48.878  1.00 15.61 ?  8   GLN A CA  1 
ATOM   56   C  C   . GLN A 1 8   ? 35.770 0.378   48.358  1.00 20.14 ?  8   GLN A C   1 
ATOM   57   O  O   . GLN A 1 8   ? 35.179 -0.612  48.796  1.00 22.85 ?  8   GLN A O   1 
ATOM   58   C  CB  . GLN A 1 8   ? 33.887 1.963   48.809  1.00 18.53 ?  8   GLN A CB  1 
ATOM   59   C  CG  . GLN A 1 8   ? 33.398 3.173   49.610  1.00 18.75 ?  8   GLN A CG  1 
ATOM   60   C  CD  . GLN A 1 8   ? 33.497 2.957   51.102  1.00 20.97 ?  8   GLN A CD  1 
ATOM   61   O  OE1 . GLN A 1 8   ? 32.553 2.462   51.722  1.00 23.36 ?  8   GLN A OE1 1 
ATOM   62   N  NE2 . GLN A 1 8   ? 34.644 3.328   51.698  1.00 18.73 ?  8   GLN A NE2 1 
ATOM   63   N  N   . GLY A 1 9   ? 36.709 0.291   47.428  1.00 19.23 ?  9   GLY A N   1 
ATOM   64   C  CA  . GLY A 1 9   ? 37.215 -0.985  46.987  1.00 19.10 ?  9   GLY A CA  1 
ATOM   65   C  C   . GLY A 1 9   ? 38.462 -1.400  47.742  1.00 20.68 ?  9   GLY A C   1 
ATOM   66   O  O   . GLY A 1 9   ? 39.282 -0.570  48.141  1.00 18.89 ?  9   GLY A O   1 
ATOM   67   N  N   . ARG A 1 10  ? 38.603 -2.705  47.935  1.00 17.69 ?  10  ARG A N   1 
ATOM   68   C  CA  . ARG A 1 10  ? 39.781 -3.211  48.624  1.00 16.84 ?  10  ARG A CA  1 
ATOM   69   C  C   . ARG A 1 10  ? 41.046 -2.865  47.849  1.00 16.68 ?  10  ARG A C   1 
ATOM   70   O  O   . ARG A 1 10  ? 41.141 -3.122  46.646  1.00 17.95 ?  10  ARG A O   1 
ATOM   71   C  CB  . ARG A 1 10  ? 39.686 -4.725  48.812  1.00 19.26 ?  10  ARG A CB  1 
ATOM   72   C  CG  . ARG A 1 10  ? 40.950 -5.287  49.432  1.00 20.78 ?  10  ARG A CG  1 
ATOM   73   C  CD  . ARG A 1 10  ? 40.787 -6.694  49.987  1.00 22.16 ?  10  ARG A CD  1 
ATOM   74   N  NE  . ARG A 1 10  ? 41.961 -7.011  50.796  1.00 19.97 ?  10  ARG A NE  1 
ATOM   75   C  CZ  . ARG A 1 10  ? 43.015 -7.702  50.376  1.00 20.43 ?  10  ARG A CZ  1 
ATOM   76   N  NH1 . ARG A 1 10  ? 43.062 -8.202  49.146  1.00 21.52 ?  10  ARG A NH1 1 
ATOM   77   N  NH2 . ARG A 1 10  ? 44.038 -7.893  51.199  1.00 20.27 ?  10  ARG A NH2 1 
ATOM   78   N  N   . VAL A 1 11  ? 42.021 -2.274  48.539  1.00 16.63 ?  11  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 11  ? 43.362 -2.127  47.988  1.00 15.28 ?  11  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 11  ? 44.331 -2.665  49.031  1.00 17.15 ?  11  VAL A C   1 
ATOM   81   O  O   . VAL A 1 11  ? 44.873 -1.912  49.854  1.00 15.82 ?  11  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 11  ? 43.701 -0.682  47.578  1.00 17.43 ?  11  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 11  ? 45.021 -0.655  46.809  1.00 16.46 ?  11  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 11  ? 42.593 -0.095  46.709  1.00 19.52 ?  11  VAL A CG2 1 
ATOM   85   N  N   . ALA A 1 12  ? 44.478 -3.994  49.043  1.00 15.94 ?  12  ALA A N   1 
ATOM   86   C  CA  . ALA A 1 12  ? 45.398 -4.769  49.875  1.00 14.96 ?  12  ALA A CA  1 
ATOM   87   C  C   . ALA A 1 12  ? 45.072 -4.753  51.370  1.00 15.48 ?  12  ALA A C   1 
ATOM   88   O  O   . ALA A 1 12  ? 45.890 -5.263  52.153  1.00 15.06 ?  12  ALA A O   1 
ATOM   89   C  CB  . ALA A 1 12  ? 46.855 -4.328  49.671  1.00 13.92 ?  12  ALA A CB  1 
ATOM   90   N  N   . ASP A 1 13  ? 43.898 -4.241  51.779  1.00 13.31 ?  13  ASP A N   1 
ATOM   91   C  CA  . ASP A 1 13  ? 43.564 -4.060  53.198  1.00 15.61 ?  13  ASP A CA  1 
ATOM   92   C  C   . ASP A 1 13  ? 43.881 -5.301  54.013  1.00 15.49 ?  13  ASP A C   1 
ATOM   93   O  O   . ASP A 1 13  ? 43.398 -6.394  53.701  1.00 16.34 ?  13  ASP A O   1 
ATOM   94   C  CB  . ASP A 1 13  ? 42.075 -3.756  53.393  1.00 16.19 ?  13  ASP A CB  1 
ATOM   95   C  CG  . ASP A 1 13  ? 41.582 -2.579  52.581  1.00 16.16 ?  13  ASP A CG  1 
ATOM   96   O  OD1 . ASP A 1 13  ? 41.965 -2.454  51.402  1.00 16.88 ?  13  ASP A OD1 1 
ATOM   97   O  OD2 . ASP A 1 13  ? 40.759 -1.798  53.112  1.00 19.87 -1 13  ASP A OD2 1 
ATOM   98   N  N   . ARG A 1 14  ? 44.654 -5.112  55.088  1.00 13.47 ?  14  ARG A N   1 
ATOM   99   C  CA  . ARG A 1 14  ? 44.859 -6.150  56.091  1.00 14.72 ?  14  ARG A CA  1 
ATOM   100  C  C   . ARG A 1 14  ? 44.103 -5.877  57.381  1.00 16.57 ?  14  ARG A C   1 
ATOM   101  O  O   . ARG A 1 14  ? 44.068 -6.749  58.253  1.00 17.42 ?  14  ARG A O   1 
ATOM   102  C  CB  . ARG A 1 14  ? 46.362 -6.331  56.380  1.00 15.42 ?  14  ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 14  ? 47.111 -6.836  55.156  1.00 15.28 ?  14  ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 14  ? 48.544 -7.271  55.435  1.00 15.10 ?  14  ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 14  ? 49.149 -7.906  54.246  1.00 14.81 ?  14  ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 14  ? 50.363 -8.469  54.216  1.00 16.12 ?  14  ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 14  ? 51.140 -8.482  55.297  1.00 19.55 ?  14  ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 14  ? 50.820 -9.015  53.094  1.00 18.64 ?  14  ARG A NH2 1 
ATOM   109  N  N   . ALA A 1 15  ? 43.495 -4.705  57.528  1.00 15.12 ?  15  ALA A N   1 
ATOM   110  C  CA  . ALA A 1 15  ? 42.678 -4.369  58.683  1.00 13.40 ?  15  ALA A CA  1 
ATOM   111  C  C   . ALA A 1 15  ? 41.205 -4.454  58.312  1.00 16.21 ?  15  ALA A C   1 
ATOM   112  O  O   . ALA A 1 15  ? 40.837 -4.297  57.150  1.00 16.83 ?  15  ALA A O   1 
ATOM   113  C  CB  . ALA A 1 15  ? 43.008 -2.966  59.189  1.00 14.64 ?  15  ALA A CB  1 
ATOM   114  N  N   . ALA A 1 16  ? 40.363 -4.702  59.317  1.00 15.93 ?  16  ALA A N   1 
ATOM   115  C  CA  . ALA A 1 16  ? 38.967 -5.049  59.047  1.00 16.15 ?  16  ALA A CA  1 
ATOM   116  C  C   . ALA A 1 16  ? 38.081 -3.853  58.724  1.00 14.57 ?  16  ALA A C   1 
ATOM   117  O  O   . ALA A 1 16  ? 37.084 -4.014  58.005  1.00 17.93 ?  16  ALA A O   1 
ATOM   118  C  CB  . ALA A 1 16  ? 38.372 -5.792  60.247  1.00 16.56 ?  16  ALA A CB  1 
ATOM   119  N  N   . TRP A 1 17  ? 38.388 -2.667  59.251  1.00 15.89 ?  17  TRP A N   1 
ATOM   120  C  CA  . TRP A 1 17  ? 37.406 -1.589  59.284  1.00 14.25 ?  17  TRP A CA  1 
ATOM   121  C  C   . TRP A 1 17  ? 37.873 -0.325  58.575  1.00 16.04 ?  17  TRP A C   1 
ATOM   122  O  O   . TRP A 1 17  ? 37.302 0.743   58.806  1.00 15.19 ?  17  TRP A O   1 
ATOM   123  C  CB  . TRP A 1 17  ? 37.005 -1.260  60.728  1.00 15.51 ?  17  TRP A CB  1 
ATOM   124  C  CG  . TRP A 1 17  ? 36.476 -2.434  61.495  1.00 17.53 ?  17  TRP A CG  1 
ATOM   125  C  CD1 . TRP A 1 17  ? 35.467 -3.277  61.122  1.00 20.43 ?  17  TRP A CD1 1 
ATOM   126  C  CD2 . TRP A 1 17  ? 36.951 -2.903  62.756  1.00 19.17 ?  17  TRP A CD2 1 
ATOM   127  N  NE1 . TRP A 1 17  ? 35.290 -4.246  62.079  1.00 21.56 ?  17  TRP A NE1 1 
ATOM   128  C  CE2 . TRP A 1 17  ? 36.174 -4.031  63.101  1.00 21.89 ?  17  TRP A CE2 1 
ATOM   129  C  CE3 . TRP A 1 17  ? 37.945 -2.468  63.639  1.00 24.17 ?  17  TRP A CE3 1 
ATOM   130  C  CZ2 . TRP A 1 17  ? 36.380 -4.749  64.277  1.00 23.23 ?  17  TRP A CZ2 1 
ATOM   131  C  CZ3 . TRP A 1 17  ? 38.139 -3.173  64.821  1.00 28.78 ?  17  TRP A CZ3 1 
ATOM   132  C  CH2 . TRP A 1 17  ? 37.353 -4.296  65.132  1.00 24.69 ?  17  TRP A CH2 1 
ATOM   133  N  N   . MET A 1 18  ? 38.856 -0.420  57.678  1.00 15.15 ?  18  MET A N   1 
ATOM   134  C  CA  . MET A 1 18  ? 39.323 0.805   57.033  1.00 13.86 ?  18  MET A CA  1 
ATOM   135  C  C   . MET A 1 18  ? 38.419 1.249   55.882  1.00 13.30 ?  18  MET A C   1 
ATOM   136  O  O   . MET A 1 18  ? 38.344 2.447   55.591  1.00 13.93 ?  18  MET A O   1 
ATOM   137  C  CB  . MET A 1 18  ? 40.783 0.640   56.587  1.00 15.18 ?  18  MET A CB  1 
ATOM   138  C  CG  . MET A 1 18  ? 41.768 0.807   57.766  1.00 13.87 ?  18  MET A CG  1 
ATOM   139  S  SD  . MET A 1 18  ? 43.461 0.608   57.194  1.00 15.74 ?  18  MET A SD  1 
ATOM   140  C  CE  . MET A 1 18  ? 44.357 0.590   58.737  1.00 13.24 ?  18  MET A CE  1 
ATOM   141  N  N   . ILE A 1 19  ? 37.724 0.318   55.213  1.00 14.42 ?  19  ILE A N   1 
ATOM   142  C  CA  . ILE A 1 19  ? 36.716 0.751   54.250  1.00 15.71 ?  19  ILE A CA  1 
ATOM   143  C  C   . ILE A 1 19  ? 35.560 1.426   54.986  1.00 14.03 ?  19  ILE A C   1 
ATOM   144  O  O   . ILE A 1 19  ? 35.073 2.488   54.577  1.00 15.48 ?  19  ILE A O   1 
ATOM   145  C  CB  . ILE A 1 19  ? 36.259 -0.439  53.388  1.00 15.09 ?  19  ILE A CB  1 
ATOM   146  C  CG1 . ILE A 1 19  ? 37.369 -0.848  52.417  1.00 16.81 ?  19  ILE A CG1 1 
ATOM   147  C  CG2 . ILE A 1 19  ? 34.954 -0.103  52.646  1.00 19.77 ?  19  ILE A CG2 1 
ATOM   148  C  CD1 . ILE A 1 19  ? 37.158 -2.208  51.723  1.00 21.33 ?  19  ILE A CD1 1 
ATOM   149  N  N   . GLU A 1 20  ? 35.152 0.855   56.122  1.00 15.30 ?  20  GLU A N   1 
ATOM   150  C  CA  . GLU A 1 20  ? 34.115 1.476   56.943  1.00 16.21 ?  20  GLU A CA  1 
ATOM   151  C  C   . GLU A 1 20  ? 34.562 2.825   57.495  1.00 16.45 ?  20  GLU A C   1 
ATOM   152  O  O   . GLU A 1 20  ? 33.774 3.778   57.530  1.00 17.32 ?  20  GLU A O   1 
ATOM   153  C  CB  . GLU A 1 20  ? 33.700 0.523   58.073  1.00 20.98 ?  20  GLU A CB  1 
ATOM   154  C  CG  . GLU A 1 20  ? 32.941 -0.696  57.512  1.00 21.91 ?  20  GLU A CG  1 
ATOM   155  C  CD  . GLU A 1 20  ? 32.494 -1.703  58.557  1.00 31.18 ?  20  GLU A CD  1 
ATOM   156  O  OE1 . GLU A 1 20  ? 32.492 -1.380  59.755  1.00 30.97 ?  20  GLU A OE1 1 
ATOM   157  O  OE2 . GLU A 1 20  ? 32.121 -2.826  58.161  1.00 39.66 -1 20  GLU A OE2 1 
ATOM   158  N  N   . GLY A 1 21  ? 35.827 2.939   57.925  1.00 14.93 ?  21  GLY A N   1 
ATOM   159  C  CA  . GLY A 1 21  ? 36.301 4.214   58.446  1.00 14.87 ?  21  GLY A CA  1 
ATOM   160  C  C   . GLY A 1 21  ? 36.326 5.308   57.387  1.00 14.16 ?  21  GLY A C   1 
ATOM   161  O  O   . GLY A 1 21  ? 36.038 6.477   57.670  1.00 14.64 ?  21  GLY A O   1 
ATOM   162  N  N   . ALA A 1 22  ? 36.676 4.944   56.151  1.00 13.33 ?  22  ALA A N   1 
ATOM   163  C  CA  . ALA A 1 22  ? 36.624 5.902   55.050  1.00 13.55 ?  22  ALA A CA  1 
ATOM   164  C  C   . ALA A 1 22  ? 35.193 6.351   54.781  1.00 14.79 ?  22  ALA A C   1 
ATOM   165  O  O   . ALA A 1 22  ? 34.929 7.541   54.583  1.00 15.49 ?  22  ALA A O   1 
ATOM   166  C  CB  . ALA A 1 22  ? 37.243 5.284   53.795  1.00 12.99 ?  22  ALA A CB  1 
ATOM   167  N  N   . ALA A 1 23  ? 34.253 5.403   54.781  1.00 19.52 ?  23  ALA A N   1 
ATOM   168  C  CA  . ALA A 1 23  ? 32.858 5.765   54.564  1.00 16.63 ?  23  ALA A CA  1 
ATOM   169  C  C   . ALA A 1 23  ? 32.364 6.738   55.632  1.00 16.43 ?  23  ALA A C   1 
ATOM   170  O  O   . ALA A 1 23  ? 31.692 7.725   55.315  1.00 18.64 ?  23  ALA A O   1 
ATOM   171  C  CB  . ALA A 1 23  ? 31.999 4.499   54.524  1.00 17.56 ?  23  ALA A CB  1 
ATOM   172  N  N   . ARG A 1 24  ? 32.693 6.485   56.904  1.00 14.45 ?  24  ARG A N   1 
ATOM   173  C  CA  . ARG A 1 24  ? 32.229 7.361   57.978  1.00 16.39 ?  24  ARG A CA  1 
ATOM   174  C  C   . ARG A 1 24  ? 32.890 8.731   57.907  1.00 16.97 ?  24  ARG A C   1 
ATOM   175  O  O   . ARG A 1 24  ? 32.249 9.754   58.165  1.00 17.35 ?  24  ARG A O   1 
ATOM   176  C  CB  . ARG A 1 24  ? 32.481 6.708   59.331  1.00 17.83 ?  24  ARG A CB  1 
ATOM   177  C  CG  . ARG A 1 24  ? 31.934 7.508   60.503  1.00 19.03 ?  24  ARG A CG  1 
ATOM   178  C  CD  . ARG A 1 24  ? 30.407 7.490   60.460  1.00 26.10 ?  24  ARG A CD  1 
ATOM   179  N  NE  . ARG A 1 24  ? 29.800 8.332   61.481  1.00 29.30 ?  24  ARG A NE  1 
ATOM   180  C  CZ  . ARG A 1 24  ? 29.588 9.637   61.342  1.00 27.04 ?  24  ARG A CZ  1 
ATOM   181  N  NH1 . ARG A 1 24  ? 29.953 10.256  60.233  1.00 22.97 ?  24  ARG A NH1 1 
ATOM   182  N  NH2 . ARG A 1 24  ? 29.015 10.326  62.320  1.00 36.36 ?  24  ARG A NH2 1 
ATOM   183  N  N   . THR A 1 25  ? 34.178 8.775   57.557  1.00 13.83 ?  25  THR A N   1 
ATOM   184  C  CA  . THR A 1 25  ? 34.839 10.061  57.363  1.00 15.45 ?  25  THR A CA  1 
ATOM   185  C  C   . THR A 1 25  ? 34.182 10.856  56.241  1.00 13.44 ?  25  THR A C   1 
ATOM   186  O  O   . THR A 1 25  ? 33.931 12.056  56.376  1.00 15.81 ?  25  THR A O   1 
ATOM   187  C  CB  . THR A 1 25  ? 36.325 9.846   57.061  1.00 13.80 ?  25  THR A CB  1 
ATOM   188  O  OG1 . THR A 1 25  ? 36.917 9.141   58.148  1.00 14.21 ?  25  THR A OG1 1 
ATOM   189  C  CG2 . THR A 1 25  ? 37.051 11.190  56.871  1.00 16.25 ?  25  THR A CG2 1 
ATOM   190  N  N   . ALA A 1 26  ? 33.926 10.202  55.110  1.00 14.52 ?  26  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 26  ? 33.279 10.883  53.995  1.00 14.88 ?  26  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 26  ? 31.909 11.419  54.389  1.00 15.74 ?  26  ALA A C   1 
ATOM   193  O  O   . ALA A 1 26  ? 31.564 12.543  54.025  1.00 16.55 ?  26  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 26  ? 33.158 9.942   52.800  1.00 16.89 ?  26  ALA A CB  1 
ATOM   195  N  N   . ARG A 1 27  ? 31.131 10.627  55.142  1.00 16.25 ?  27  ARG A N   1 
ATOM   196  C  CA  . ARG A 1 27  ? 29.809 11.075  55.581  1.00 17.86 ?  27  ARG A CA  1 
ATOM   197  C  C   . ARG A 1 27  ? 29.910 12.350  56.408  1.00 20.58 ?  27  ARG A C   1 
ATOM   198  O  O   . ARG A 1 27  ? 29.134 13.294  56.207  1.00 19.76 ?  27  ARG A O   1 
ATOM   199  C  CB  . ARG A 1 27  ? 29.116 9.967   56.382  1.00 19.52 ?  27  ARG A CB  1 
ATOM   200  C  CG  . ARG A 1 27  ? 27.664 10.310  56.764  1.00 24.67 ?  27  ARG A CG  1 
ATOM   201  C  CD  . ARG A 1 27  ? 27.228 9.783   58.134  1.00 35.25 ?  27  ARG A CD  1 
ATOM   202  N  NE  . ARG A 1 27  ? 27.268 8.328   58.235  1.00 33.09 ?  27  ARG A NE  1 
ATOM   203  C  CZ  . ARG A 1 27  ? 26.940 7.647   59.330  1.00 45.13 ?  27  ARG A CZ  1 
ATOM   204  N  NH1 . ARG A 1 27  ? 26.543 8.292   60.420  1.00 38.41 ?  27  ARG A NH1 1 
ATOM   205  N  NH2 . ARG A 1 27  ? 27.011 6.322   59.339  1.00 41.04 ?  27  ARG A NH2 1 
ATOM   206  N  N   . ALA A 1 28  ? 30.879 12.407  57.332  1.00 16.28 ?  28  ALA A N   1 
ATOM   207  C  CA  . ALA A 1 28  ? 31.036 13.598  58.158  1.00 17.45 ?  28  ALA A CA  1 
ATOM   208  C  C   . ALA A 1 28  ? 31.378 14.816  57.310  1.00 19.03 ?  28  ALA A C   1 
ATOM   209  O  O   . ALA A 1 28  ? 30.893 15.919  57.577  1.00 19.48 ?  28  ALA A O   1 
ATOM   210  C  CB  . ALA A 1 28  ? 32.107 13.369  59.226  1.00 18.59 ?  28  ALA A CB  1 
ATOM   211  N  N   . LEU A 1 29  ? 32.213 14.639  56.283  1.00 15.43 ?  29  LEU A N   1 
ATOM   212  C  CA  . LEU A 1 29  ? 32.575 15.774  55.439  1.00 16.21 ?  29  LEU A CA  1 
ATOM   213  C  C   . LEU A 1 29  ? 31.399 16.219  54.575  1.00 16.62 ?  29  LEU A C   1 
ATOM   214  O  O   . LEU A 1 29  ? 31.216 17.418  54.340  1.00 19.16 ?  29  LEU A O   1 
ATOM   215  C  CB  . LEU A 1 29  ? 33.772 15.416  54.556  1.00 16.09 ?  29  LEU A CB  1 
ATOM   216  C  CG  . LEU A 1 29  ? 35.096 15.208  55.295  1.00 15.74 ?  29  LEU A CG  1 
ATOM   217  C  CD1 . LEU A 1 29  ? 36.115 14.626  54.322  1.00 17.06 ?  29  LEU A CD1 1 
ATOM   218  C  CD2 . LEU A 1 29  ? 35.615 16.499  55.907  1.00 16.59 ?  29  LEU A CD2 1 
ATOM   219  N  N   . GLU A 1 30  ? 30.628 15.257  54.055  1.00 17.37 ?  30  GLU A N   1 
ATOM   220  C  CA  . GLU A 1 30  ? 29.425 15.572  53.286  1.00 19.23 ?  30  GLU A CA  1 
ATOM   221  C  C   . GLU A 1 30  ? 28.453 16.416  54.104  1.00 20.19 ?  30  GLU A C   1 
ATOM   222  O  O   . GLU A 1 30  ? 27.904 17.407  53.608  1.00 23.54 ?  30  GLU A O   1 
ATOM   223  C  CB  . GLU A 1 30  ? 28.751 14.277  52.831  1.00 19.59 ?  30  GLU A CB  1 
ATOM   224  C  CG  . GLU A 1 30  ? 29.540 13.527  51.753  1.00 20.76 ?  30  GLU A CG  1 
ATOM   225  C  CD  . GLU A 1 30  ? 28.894 12.210  51.341  1.00 26.40 ?  30  GLU A CD  1 
ATOM   226  O  OE1 . GLU A 1 30  ? 28.350 11.509  52.217  1.00 32.19 ?  30  GLU A OE1 1 
ATOM   227  O  OE2 . GLU A 1 30  ? 28.942 11.876  50.138  1.00 27.11 -1 30  GLU A OE2 1 
ATOM   228  N  N   . GLU A 1 31  ? 28.234 16.030  55.362  1.00 18.69 ?  31  GLU A N   1 
ATOM   229  C  CA  . GLU A 1 31  ? 27.291 16.742  56.218  1.00 23.52 ?  31  GLU A CA  1 
ATOM   230  C  C   . GLU A 1 31  ? 27.828 18.109  56.618  1.00 24.66 ?  31  GLU A C   1 
ATOM   231  O  O   . GLU A 1 31  ? 27.072 19.087  56.666  1.00 25.22 ?  31  GLU A O   1 
ATOM   232  C  CB  . GLU A 1 31  ? 26.964 15.902  57.457  1.00 22.91 ?  31  GLU A CB  1 
ATOM   233  C  CG  . GLU A 1 31  ? 26.249 14.590  57.125  1.00 31.41 ?  31  GLU A CG  1 
ATOM   234  C  CD  . GLU A 1 31  ? 26.120 13.637  58.308  1.00 37.30 ?  31  GLU A CD  1 
ATOM   235  O  OE1 . GLU A 1 31  ? 25.426 12.604  58.163  1.00 36.28 ?  31  GLU A OE1 1 
ATOM   236  O  OE2 . GLU A 1 31  ? 26.703 13.908  59.379  1.00 42.47 -1 31  GLU A OE2 1 
ATOM   237  N  N   . ARG A 1 32  ? 29.135 18.212  56.887  1.00 17.60 ?  32  ARG A N   1 
ATOM   238  C  CA  . ARG A 1 32  ? 29.660 19.495  57.334  1.00 20.16 ?  32  ARG A CA  1 
ATOM   239  C  C   . ARG A 1 32  ? 29.711 20.510  56.203  1.00 19.84 ?  32  ARG A C   1 
ATOM   240  O  O   . ARG A 1 32  ? 29.459 21.703  56.420  1.00 22.00 ?  32  ARG A O   1 
ATOM   241  C  CB  . ARG A 1 32  ? 31.057 19.327  57.942  1.00 17.95 ?  32  ARG A CB  1 
ATOM   242  C  CG  . ARG A 1 32  ? 31.778 20.663  58.135  1.00 17.29 ?  32  ARG A CG  1 
ATOM   243  C  CD  . ARG A 1 32  ? 32.942 20.573  59.121  1.00 19.08 ?  32  ARG A CD  1 
ATOM   244  N  NE  . ARG A 1 32  ? 32.493 20.473  60.501  1.00 19.80 ?  32  ARG A NE  1 
ATOM   245  C  CZ  . ARG A 1 32  ? 33.267 20.697  61.557  1.00 18.44 ?  32  ARG A CZ  1 
ATOM   246  N  NH1 . ARG A 1 32  ? 34.545 21.000  61.389  1.00 19.48 ?  32  ARG A NH1 1 
ATOM   247  N  NH2 . ARG A 1 32  ? 32.758 20.616  62.781  1.00 21.85 ?  32  ARG A NH2 1 
ATOM   248  N  N   . TYR A 1 33  ? 30.116 20.080  55.008  1.00 19.31 ?  33  TYR A N   1 
ATOM   249  C  CA  . TYR A 1 33  ? 30.404 20.994  53.920  1.00 19.74 ?  33  TYR A CA  1 
ATOM   250  C  C   . TYR A 1 33  ? 29.352 20.973  52.822  1.00 18.69 ?  33  TYR A C   1 
ATOM   251  O  O   . TYR A 1 33  ? 29.516 21.678  51.823  1.00 26.58 ?  33  TYR A O   1 
ATOM   252  C  CB  . TYR A 1 33  ? 31.788 20.682  53.331  1.00 18.01 ?  33  TYR A CB  1 
ATOM   253  C  CG  . TYR A 1 33  ? 32.889 21.037  54.310  1.00 19.00 ?  33  TYR A CG  1 
ATOM   254  C  CD1 . TYR A 1 33  ? 33.218 22.366  54.546  1.00 16.97 ?  33  TYR A CD1 1 
ATOM   255  C  CD2 . TYR A 1 33  ? 33.565 20.048  55.028  1.00 17.16 ?  33  TYR A CD2 1 
ATOM   256  C  CE1 . TYR A 1 33  ? 34.195 22.716  55.471  1.00 17.05 ?  33  TYR A CE1 1 
ATOM   257  C  CE2 . TYR A 1 33  ? 34.562 20.386  55.956  1.00 16.95 ?  33  TYR A CE2 1 
ATOM   258  C  CZ  . TYR A 1 33  ? 34.870 21.721  56.170  1.00 15.33 ?  33  TYR A CZ  1 
ATOM   259  O  OH  . TYR A 1 33  ? 35.845 22.082  57.087  1.00 17.68 ?  33  TYR A OH  1 
ATOM   260  N  N   . GLY A 1 34  ? 28.295 20.188  52.974  1.00 22.82 ?  34  GLY A N   1 
ATOM   261  C  CA  . GLY A 1 34  ? 27.257 20.153  51.957  1.00 25.59 ?  34  GLY A CA  1 
ATOM   262  C  C   . GLY A 1 34  ? 27.713 19.530  50.658  1.00 26.96 ?  34  GLY A C   1 
ATOM   263  O  O   . GLY A 1 34  ? 27.387 20.042  49.581  1.00 35.85 ?  34  GLY A O   1 
ATOM   264  N  N   . LEU A 1 35  ? 28.467 18.441  50.736  1.00 21.83 ?  35  LEU A N   1 
ATOM   265  C  CA  . LEU A 1 35  ? 29.016 17.760  49.573  1.00 24.93 ?  35  LEU A CA  1 
ATOM   266  C  C   . LEU A 1 35  ? 28.344 16.414  49.367  1.00 20.94 ?  35  LEU A C   1 
ATOM   267  O  O   . LEU A 1 35  ? 27.731 15.850  50.274  1.00 23.86 ?  35  LEU A O   1 
ATOM   268  C  CB  . LEU A 1 35  ? 30.525 17.510  49.719  1.00 28.11 ?  35  LEU A CB  1 
ATOM   269  C  CG  . LEU A 1 35  ? 31.421 18.598  50.273  1.00 25.98 ?  35  LEU A CG  1 
ATOM   270  C  CD1 . LEU A 1 35  ? 32.785 18.000  50.654  1.00 22.56 ?  35  LEU A CD1 1 
ATOM   271  C  CD2 . LEU A 1 35  ? 31.563 19.653  49.224  1.00 25.51 ?  35  LEU A CD2 1 
ATOM   272  N  N   . LYS A 1 36  ? 28.531 15.876  48.168  1.00 22.65 ?  36  LYS A N   1 
ATOM   273  C  CA  . LYS A 1 36  ? 28.211 14.489  47.864  1.00 24.56 ?  36  LYS A CA  1 
ATOM   274  C  C   . LYS A 1 36  ? 29.462 13.849  47.282  1.00 21.49 ?  36  LYS A C   1 
ATOM   275  O  O   . LYS A 1 36  ? 29.992 14.322  46.270  1.00 24.99 ?  36  LYS A O   1 
ATOM   276  C  CB  . LYS A 1 36  ? 27.030 14.370  46.892  1.00 31.86 ?  36  LYS A CB  1 
ATOM   277  C  CG  . LYS A 1 36  ? 25.676 14.821  47.465  1.00 34.22 ?  36  LYS A CG  1 
ATOM   278  C  CD  . LYS A 1 36  ? 25.211 13.938  48.621  1.00 44.50 ?  36  LYS A CD  1 
ATOM   279  C  CE  . LYS A 1 36  ? 24.259 14.691  49.546  1.00 41.03 ?  36  LYS A CE  1 
ATOM   280  N  NZ  . LYS A 1 36  ? 23.405 13.786  50.365  1.00 43.82 ?  36  LYS A NZ  1 
ATOM   281  N  N   . GLY A 1 37  ? 29.931 12.786  47.927  1.00 22.64 ?  37  GLY A N   1 
ATOM   282  C  CA  . GLY A 1 37  ? 31.141 12.135  47.475  1.00 22.34 ?  37  GLY A CA  1 
ATOM   283  C  C   . GLY A 1 37  ? 30.922 11.308  46.223  1.00 26.73 ?  37  GLY A C   1 
ATOM   284  O  O   . GLY A 1 37  ? 29.835 10.783  45.960  1.00 26.55 ?  37  GLY A O   1 
ATOM   285  N  N   . HIS A 1 38  ? 31.985 11.202  45.436  1.00 20.11 ?  38  HIS A N   1 
ATOM   286  C  CA  . HIS A 1 38  ? 32.054 10.257  44.334  1.00 18.05 ?  38  HIS A CA  1 
ATOM   287  C  C   . HIS A 1 38  ? 32.694 8.981   44.873  1.00 22.19 ?  38  HIS A C   1 
ATOM   288  O  O   . HIS A 1 38  ? 33.895 8.964   45.174  1.00 19.09 ?  38  HIS A O   1 
ATOM   289  C  CB  . HIS A 1 38  ? 32.853 10.844  43.174  1.00 20.72 ?  38  HIS A CB  1 
ATOM   290  C  CG  . HIS A 1 38  ? 33.020 9.908   42.022  1.00 26.52 ?  38  HIS A CG  1 
ATOM   291  N  ND1 . HIS A 1 38  ? 34.023 10.049  41.091  1.00 33.24 ?  38  HIS A ND1 1 
ATOM   292  C  CD2 . HIS A 1 38  ? 32.302 8.823   41.643  1.00 33.75 ?  38  HIS A CD2 1 
ATOM   293  C  CE1 . HIS A 1 38  ? 33.924 9.085   40.191  1.00 34.32 ?  38  HIS A CE1 1 
ATOM   294  N  NE2 . HIS A 1 38  ? 32.888 8.328   40.504  1.00 30.67 ?  38  HIS A NE2 1 
ATOM   295  N  N   . TYR A 1 39  ? 31.893 7.923   45.015  1.00 22.72 ?  39  TYR A N   1 
ATOM   296  C  CA  . TYR A 1 39  ? 32.349 6.679   45.624  1.00 18.03 ?  39  TYR A CA  1 
ATOM   297  C  C   . TYR A 1 39  ? 32.792 5.705   44.542  1.00 26.66 ?  39  TYR A C   1 
ATOM   298  O  O   . TYR A 1 39  ? 32.076 5.496   43.556  1.00 26.42 ?  39  TYR A O   1 
ATOM   299  C  CB  . TYR A 1 39  ? 31.249 6.051   46.483  1.00 19.06 ?  39  TYR A CB  1 
ATOM   300  C  CG  . TYR A 1 39  ? 30.922 6.876   47.705  1.00 19.36 ?  39  TYR A CG  1 
ATOM   301  C  CD1 . TYR A 1 39  ? 30.177 8.045   47.601  1.00 21.29 ?  39  TYR A CD1 1 
ATOM   302  C  CD2 . TYR A 1 39  ? 31.384 6.505   48.964  1.00 19.73 ?  39  TYR A CD2 1 
ATOM   303  C  CE1 . TYR A 1 39  ? 29.882 8.816   48.715  1.00 23.33 ?  39  TYR A CE1 1 
ATOM   304  C  CE2 . TYR A 1 39  ? 31.096 7.265   50.090  1.00 22.80 ?  39  TYR A CE2 1 
ATOM   305  C  CZ  . TYR A 1 39  ? 30.350 8.425   49.959  1.00 18.46 ?  39  TYR A CZ  1 
ATOM   306  O  OH  . TYR A 1 39  ? 30.082 9.178   51.066  1.00 23.83 ?  39  TYR A OH  1 
ATOM   307  N  N   . VAL A 1 40  ? 33.974 5.116   44.728  1.00 20.28 ?  40  VAL A N   1 
ATOM   308  C  CA  . VAL A 1 40  ? 34.612 4.274   43.724  1.00 22.31 ?  40  VAL A CA  1 
ATOM   309  C  C   . VAL A 1 40  ? 35.022 2.945   44.357  1.00 24.82 ?  40  VAL A C   1 
ATOM   310  O  O   . VAL A 1 40  ? 35.672 2.925   45.409  1.00 21.86 ?  40  VAL A O   1 
ATOM   311  C  CB  . VAL A 1 40  ? 35.833 4.985   43.110  1.00 26.33 ?  40  VAL A CB  1 
ATOM   312  C  CG1 . VAL A 1 40  ? 36.770 3.983   42.474  1.00 31.26 ?  40  VAL A CG1 1 
ATOM   313  C  CG2 . VAL A 1 40  ? 35.385 6.047   42.108  1.00 31.47 ?  40  VAL A CG2 1 
ATOM   314  N  N   . GLY A 1 41  ? 34.653 1.839   43.716  1.00 24.72 ?  41  GLY A N   1 
ATOM   315  C  CA  . GLY A 1 41  ? 35.105 0.532   44.144  1.00 21.76 ?  41  GLY A CA  1 
ATOM   316  C  C   . GLY A 1 41  ? 34.069 -0.219  44.965  1.00 25.17 ?  41  GLY A C   1 
ATOM   317  O  O   . GLY A 1 41  ? 33.175 0.359   45.588  1.00 28.20 ?  41  GLY A O   1 
ATOM   318  N  N   . GLU A 1 42  ? 34.222 -1.545  44.980  1.00 28.32 ?  42  GLU A N   1 
ATOM   319  C  CA  . GLU A 1 42  ? 33.358 -2.482  45.678  1.00 30.86 ?  42  GLU A CA  1 
ATOM   320  C  C   . GLU A 1 42  ? 34.079 -3.063  46.881  1.00 26.88 ?  42  GLU A C   1 
ATOM   321  O  O   . GLU A 1 42  ? 35.199 -3.571  46.726  1.00 29.04 ?  42  GLU A O   1 
ATOM   322  C  CB  . GLU A 1 42  ? 32.933 -3.620  44.736  1.00 39.83 ?  42  GLU A CB  1 
ATOM   323  C  CG  . GLU A 1 42  ? 31.721 -3.306  43.875  1.00 50.10 ?  42  GLU A CG  1 
ATOM   324  C  CD  . GLU A 1 42  ? 30.480 -3.029  44.698  1.00 54.85 ?  42  GLU A CD  1 
ATOM   325  O  OE1 . GLU A 1 42  ? 30.101 -3.893  45.520  1.00 59.50 ?  42  GLU A OE1 1 
ATOM   326  O  OE2 . GLU A 1 42  ? 29.885 -1.944  44.524  1.00 58.27 -1 42  GLU A OE2 1 
ATOM   327  N  N   . PRO A 1 43  ? 33.478 -3.022  48.074  1.00 27.03 ?  43  PRO A N   1 
ATOM   328  C  CA  . PRO A 1 43  ? 34.135 -3.600  49.257  1.00 27.08 ?  43  PRO A CA  1 
ATOM   329  C  C   . PRO A 1 43  ? 34.364 -5.098  49.111  1.00 33.16 ?  43  PRO A C   1 
ATOM   330  O  O   . PRO A 1 43  ? 33.546 -5.816  48.534  1.00 31.73 ?  43  PRO A O   1 
ATOM   331  C  CB  . PRO A 1 43  ? 33.154 -3.293  50.395  1.00 27.21 ?  43  PRO A CB  1 
ATOM   332  C  CG  . PRO A 1 43  ? 32.399 -2.087  49.932  1.00 29.13 ?  43  PRO A CG  1 
ATOM   333  C  CD  . PRO A 1 43  ? 32.275 -2.245  48.434  1.00 27.94 ?  43  PRO A CD  1 
ATOM   334  N  N   . ALA A 1 44  ? 35.502 -5.559  49.627  1.00 23.23 ?  44  ALA A N   1 
ATOM   335  C  CA  . ALA A 1 44  ? 35.864 -6.966  49.707  1.00 25.18 ?  44  ALA A CA  1 
ATOM   336  C  C   . ALA A 1 44  ? 36.575 -7.204  51.030  1.00 28.49 ?  44  ALA A C   1 
ATOM   337  O  O   . ALA A 1 44  ? 37.144 -6.267  51.604  1.00 26.22 ?  44  ALA A O   1 
ATOM   338  C  CB  . ALA A 1 44  ? 36.763 -7.391  48.532  1.00 27.59 ?  44  ALA A CB  1 
ATOM   339  N  N   . PRO A 1 45  ? 36.528 -8.427  51.563  1.00 29.20 ?  45  PRO A N   1 
ATOM   340  C  CA  . PRO A 1 45  ? 37.098 -8.677  52.893  1.00 28.11 ?  45  PRO A CA  1 
ATOM   341  C  C   . PRO A 1 45  ? 38.612 -8.524  52.929  1.00 21.21 ?  45  PRO A C   1 
ATOM   342  O  O   . PRO A 1 45  ? 39.313 -8.765  51.942  1.00 21.63 ?  45  PRO A O   1 
ATOM   343  C  CB  . PRO A 1 45  ? 36.692 -10.126 53.187  1.00 30.08 ?  45  PRO A CB  1 
ATOM   344  C  CG  . PRO A 1 45  ? 35.496 -10.368 52.316  1.00 28.17 ?  45  PRO A CG  1 
ATOM   345  C  CD  . PRO A 1 45  ? 35.770 -9.592  51.066  1.00 31.39 ?  45  PRO A CD  1 
ATOM   346  N  N   . HIS A 1 46  ? 39.112 -8.139  54.107  1.00 22.01 ?  46  HIS A N   1 
ATOM   347  C  CA  . HIS A 1 46  ? 40.550 -8.010  54.316  1.00 20.54 ?  46  HIS A CA  1 
ATOM   348  C  C   . HIS A 1 46  ? 41.222 -9.387  54.295  1.00 22.13 ?  46  HIS A C   1 
ATOM   349  O  O   . HIS A 1 46  ? 40.593 -10.420 54.557  1.00 25.26 ?  46  HIS A O   1 
ATOM   350  C  CB  . HIS A 1 46  ? 40.844 -7.273  55.629  1.00 19.22 ?  46  HIS A CB  1 
ATOM   351  C  CG  . HIS A 1 46  ? 40.409 -8.006  56.861  1.00 23.77 ?  46  HIS A CG  1 
ATOM   352  N  ND1 . HIS A 1 46  ? 39.083 -8.176  57.193  1.00 26.02 ?  46  HIS A ND1 1 
ATOM   353  C  CD2 . HIS A 1 46  ? 41.122 -8.603  57.846  1.00 28.11 ?  46  HIS A CD2 1 
ATOM   354  C  CE1 . HIS A 1 46  ? 38.996 -8.850  58.326  1.00 30.36 ?  46  HIS A CE1 1 
ATOM   355  N  NE2 . HIS A 1 46  ? 40.219 -9.122  58.744  1.00 30.24 ?  46  HIS A NE2 1 
ATOM   356  N  N   . ALA A 1 47  ? 42.512 -9.392  53.951  1.00 22.00 ?  47  ALA A N   1 
ATOM   357  C  CA  . ALA A 1 47  ? 43.286 -10.624 53.892  1.00 20.58 ?  47  ALA A CA  1 
ATOM   358  C  C   . ALA A 1 47  ? 44.770 -10.302 53.982  1.00 23.16 ?  47  ALA A C   1 
ATOM   359  O  O   . ALA A 1 47  ? 45.201 -9.185  53.681  1.00 20.28 ?  47  ALA A O   1 
ATOM   360  C  CB  . ALA A 1 47  ? 42.993 -11.401 52.605  1.00 25.85 ?  47  ALA A CB  1 
ATOM   361  N  N   . ASP A 1 48  ? 45.551 -11.312 54.350  1.00 23.82 ?  48  ASP A N   1 
ATOM   362  C  CA  . ASP A 1 48  ? 47.007 -11.180 54.470  1.00 21.68 ?  48  ASP A CA  1 
ATOM   363  C  C   . ASP A 1 48  ? 47.722 -11.692 53.228  1.00 27.08 ?  48  ASP A C   1 
ATOM   364  O  O   . ASP A 1 48  ? 48.654 -12.489 53.320  1.00 32.57 ?  48  ASP A O   1 
ATOM   365  C  CB  . ASP A 1 48  ? 47.504 -11.910 55.713  1.00 31.11 ?  48  ASP A CB  1 
ATOM   366  C  CG  . ASP A 1 48  ? 46.982 -11.299 56.996  1.00 36.33 ?  48  ASP A CG  1 
ATOM   367  O  OD1 . ASP A 1 48  ? 47.076 -10.062 57.149  1.00 30.12 ?  48  ASP A OD1 1 
ATOM   368  O  OD2 . ASP A 1 48  ? 46.487 -12.059 57.854  1.00 42.28 -1 48  ASP A OD2 1 
ATOM   369  N  N   . ASP A 1 49  ? 47.303 -11.235 52.054  1.00 18.36 ?  49  ASP A N   1 
ATOM   370  C  CA  . ASP A 1 49  ? 47.899 -11.689 50.810  1.00 21.45 ?  49  ASP A CA  1 
ATOM   371  C  C   . ASP A 1 49  ? 49.144 -10.876 50.466  1.00 20.87 ?  49  ASP A C   1 
ATOM   372  O  O   . ASP A 1 49  ? 49.320 -9.734  50.896  1.00 20.66 ?  49  ASP A O   1 
ATOM   373  C  CB  . ASP A 1 49  ? 46.884 -11.627 49.660  1.00 21.01 ?  49  ASP A CB  1 
ATOM   374  C  CG  . ASP A 1 49  ? 46.061 -10.342 49.648  1.00 24.19 ?  49  ASP A CG  1 
ATOM   375  O  OD1 . ASP A 1 49  ? 46.344 -9.417  50.445  1.00 21.87 ?  49  ASP A OD1 1 
ATOM   376  O  OD2 . ASP A 1 49  ? 45.133 -10.245 48.817  1.00 27.09 -1 49  ASP A OD2 1 
ATOM   377  N  N   . ASP A 1 50  ? 50.027 -11.497 49.691  1.00 21.82 ?  50  ASP A N   1 
ATOM   378  C  CA  . ASP A 1 50  ? 51.222 -10.821 49.214  1.00 19.37 ?  50  ASP A CA  1 
ATOM   379  C  C   . ASP A 1 50  ? 50.859 -9.696  48.250  1.00 18.15 ?  50  ASP A C   1 
ATOM   380  O  O   . ASP A 1 50  ? 49.854 -9.758  47.535  1.00 19.33 ?  50  ASP A O   1 
ATOM   381  C  CB  . ASP A 1 50  ? 52.148 -11.816 48.516  1.00 22.08 ?  50  ASP A CB  1 
ATOM   382  C  CG  . ASP A 1 50  ? 53.516 -11.230 48.226  1.00 20.23 ?  50  ASP A CG  1 
ATOM   383  O  OD1 . ASP A 1 50  ? 54.271 -10.996 49.196  1.00 21.53 ?  50  ASP A OD1 1 
ATOM   384  O  OD2 . ASP A 1 50  ? 53.841 -10.997 47.037  1.00 24.45 -1 50  ASP A OD2 1 
ATOM   385  N  N   . TRP A 1 51  ? 51.685 -8.646  48.253  1.00 20.19 ?  51  TRP A N   1 
ATOM   386  C  CA  . TRP A 1 51  ? 51.472 -7.523  47.341  1.00 16.64 ?  51  TRP A CA  1 
ATOM   387  C  C   . TRP A 1 51  ? 51.334 -7.982  45.895  1.00 21.13 ?  51  TRP A C   1 
ATOM   388  O  O   . TRP A 1 51  ? 50.584 -7.376  45.124  1.00 20.21 ?  51  TRP A O   1 
ATOM   389  C  CB  . TRP A 1 51  ? 52.613 -6.505  47.464  1.00 17.42 ?  51  TRP A CB  1 
ATOM   390  C  CG  . TRP A 1 51  ? 53.904 -7.009  46.912  1.00 17.21 ?  51  TRP A CG  1 
ATOM   391  C  CD1 . TRP A 1 51  ? 54.908 -7.635  47.596  1.00 20.16 ?  51  TRP A CD1 1 
ATOM   392  C  CD2 . TRP A 1 51  ? 54.319 -6.961  45.538  1.00 19.31 ?  51  TRP A CD2 1 
ATOM   393  N  NE1 . TRP A 1 51  ? 55.926 -7.971  46.730  1.00 23.37 ?  51  TRP A NE1 1 
ATOM   394  C  CE2 . TRP A 1 51  ? 55.585 -7.572  45.464  1.00 23.52 ?  51  TRP A CE2 1 
ATOM   395  C  CE3 . TRP A 1 51  ? 53.739 -6.466  44.365  1.00 22.58 ?  51  TRP A CE3 1 
ATOM   396  C  CZ2 . TRP A 1 51  ? 56.285 -7.697  44.262  1.00 22.17 ?  51  TRP A CZ2 1 
ATOM   397  C  CZ3 . TRP A 1 51  ? 54.442 -6.591  43.169  1.00 23.63 ?  51  TRP A CZ3 1 
ATOM   398  C  CH2 . TRP A 1 51  ? 55.697 -7.199  43.134  1.00 23.31 ?  51  TRP A CH2 1 
ATOM   399  N  N   . SER A 1 52  ? 52.027 -9.063  45.514  1.00 22.59 ?  52  SER A N   1 
ATOM   400  C  CA  . SER A 1 52  ? 51.977 -9.529  44.130  1.00 23.45 ?  52  SER A CA  1 
ATOM   401  C  C   . SER A 1 52  ? 50.615 -10.091 43.764  1.00 23.01 ?  52  SER A C   1 
ATOM   402  O  O   . SER A 1 52  ? 50.309 -10.212 42.573  1.00 23.57 ?  52  SER A O   1 
ATOM   403  C  CB  . SER A 1 52  ? 53.051 -10.590 43.887  1.00 19.85 ?  52  SER A CB  1 
ATOM   404  O  OG  . SER A 1 52  ? 52.788 -11.757 44.646  1.00 25.57 ?  52  SER A OG  1 
ATOM   405  N  N   . VAL A 1 53  ? 49.808 -10.442 44.756  1.00 20.22 ?  53  VAL A N   1 
ATOM   406  C  CA  . VAL A 1 53  ? 48.440 -10.896 44.547  1.00 19.87 ?  53  VAL A CA  1 
ATOM   407  C  C   . VAL A 1 53  ? 47.450 -9.764  44.777  1.00 26.63 ?  53  VAL A C   1 
ATOM   408  O  O   . VAL A 1 53  ? 46.540 -9.544  43.979  1.00 22.63 ?  53  VAL A O   1 
ATOM   409  C  CB  . VAL A 1 53  ? 48.141 -12.102 45.466  1.00 25.86 ?  53  VAL A CB  1 
ATOM   410  C  CG1 . VAL A 1 53  ? 46.654 -12.435 45.475  1.00 24.84 ?  53  VAL A CG1 1 
ATOM   411  C  CG2 . VAL A 1 53  ? 48.984 -13.305 45.057  1.00 26.83 ?  53  VAL A CG2 1 
ATOM   412  N  N   . ALA A 1 54  ? 47.644 -9.012  45.863  1.00 22.20 ?  54  ALA A N   1 
ATOM   413  C  CA  . ALA A 1 54  ? 46.726 -7.927  46.197  1.00 21.12 ?  54  ALA A CA  1 
ATOM   414  C  C   . ALA A 1 54  ? 46.768 -6.814  45.154  1.00 17.55 ?  54  ALA A C   1 
ATOM   415  O  O   . ALA A 1 54  ? 45.735 -6.203  44.849  1.00 18.52 ?  54  ALA A O   1 
ATOM   416  C  CB  . ALA A 1 54  ? 47.070 -7.383  47.588  1.00 17.27 ?  54  ALA A CB  1 
ATOM   417  N  N   . LEU A 1 55  ? 47.952 -6.512  44.622  1.00 19.69 ?  55  LEU A N   1 
ATOM   418  C  CA  . LEU A 1 55  ? 48.061 -5.410  43.666  1.00 18.62 ?  55  LEU A CA  1 
ATOM   419  C  C   . LEU A 1 55  ? 47.240 -5.652  42.404  1.00 22.18 ?  55  LEU A C   1 
ATOM   420  O  O   . LEU A 1 55  ? 46.425 -4.783  42.054  1.00 19.94 ?  55  LEU A O   1 
ATOM   421  C  CB  . LEU A 1 55  ? 49.538 -5.132  43.362  1.00 20.25 ?  55  LEU A CB  1 
ATOM   422  C  CG  . LEU A 1 55  ? 49.875 -4.022  42.366  1.00 21.40 ?  55  LEU A CG  1 
ATOM   423  C  CD1 . LEU A 1 55  ? 49.236 -2.695  42.795  1.00 20.04 ?  55  LEU A CD1 1 
ATOM   424  C  CD2 . LEU A 1 55  ? 51.382 -3.885  42.208  1.00 23.22 ?  55  LEU A CD2 1 
ATOM   425  N  N   . PRO A 1 56  ? 47.355 -6.788  41.703  1.00 22.19 ?  56  PRO A N   1 
ATOM   426  C  CA  . PRO A 1 56  ? 46.459 -7.004  40.551  1.00 24.24 ?  56  PRO A CA  1 
ATOM   427  C  C   . PRO A 1 56  ? 44.988 -7.053  40.922  1.00 20.39 ?  56  PRO A C   1 
ATOM   428  O  O   . PRO A 1 56  ? 44.145 -6.582  40.147  1.00 25.18 ?  56  PRO A O   1 
ATOM   429  C  CB  . PRO A 1 56  ? 46.942 -8.344  39.969  1.00 28.53 ?  56  PRO A CB  1 
ATOM   430  C  CG  . PRO A 1 56  ? 47.766 -8.967  41.031  1.00 28.93 ?  56  PRO A CG  1 
ATOM   431  C  CD  . PRO A 1 56  ? 48.383 -7.837  41.791  1.00 24.82 ?  56  PRO A CD  1 
ATOM   432  N  N   . GLN A 1 57  ? 44.640 -7.590  42.093  1.00 20.18 ?  57  GLN A N   1 
ATOM   433  C  CA  . GLN A 1 57  ? 43.241 -7.612  42.505  1.00 19.42 ?  57  GLN A CA  1 
ATOM   434  C  C   . GLN A 1 57  ? 42.656 -6.205  42.607  1.00 23.47 ?  57  GLN A C   1 
ATOM   435  O  O   . GLN A 1 57  ? 41.470 -6.004  42.340  1.00 23.77 ?  57  GLN A O   1 
ATOM   436  C  CB  . GLN A 1 57  ? 43.097 -8.340  43.843  1.00 25.10 ?  57  GLN A CB  1 
ATOM   437  C  CG  . GLN A 1 57  ? 41.727 -8.210  44.494  1.00 32.83 ?  57  GLN A CG  1 
ATOM   438  C  CD  . GLN A 1 57  ? 41.765 -8.540  45.973  1.00 40.11 ?  57  GLN A CD  1 
ATOM   439  O  OE1 . GLN A 1 57  ? 41.560 -7.666  46.825  1.00 30.26 ?  57  GLN A OE1 1 
ATOM   440  N  NE2 . GLN A 1 57  ? 42.046 -9.802  46.290  1.00 42.78 ?  57  GLN A NE2 1 
ATOM   441  N  N   . ALA A 1 58  ? 43.478 -5.217  42.952  1.00 20.02 ?  58  ALA A N   1 
ATOM   442  C  CA  . ALA A 1 58  ? 43.013 -3.848  43.141  1.00 18.73 ?  58  ALA A CA  1 
ATOM   443  C  C   . ALA A 1 58  ? 43.008 -3.013  41.862  1.00 19.04 ?  58  ALA A C   1 
ATOM   444  O  O   . ALA A 1 58  ? 42.658 -1.830  41.917  1.00 20.63 ?  58  ALA A O   1 
ATOM   445  C  CB  . ALA A 1 58  ? 43.880 -3.151  44.201  1.00 17.60 ?  58  ALA A CB  1 
ATOM   446  N  N   . ARG A 1 59  ? 43.354 -3.588  40.704  1.00 19.58 ?  59  ARG A N   1 
ATOM   447  C  CA  . ARG A 1 59  ? 43.570 -2.758  39.520  1.00 21.35 ?  59  ARG A CA  1 
ATOM   448  C  C   . ARG A 1 59  ? 42.332 -1.939  39.156  1.00 17.63 ?  59  ARG A C   1 
ATOM   449  O  O   . ARG A 1 59  ? 42.431 -0.743  38.850  1.00 17.41 ?  59  ARG A O   1 
ATOM   450  C  CB  . ARG A 1 59  ? 44.001 -3.631  38.342  1.00 20.74 ?  59  ARG A CB  1 
ATOM   451  C  CG  . ARG A 1 59  ? 43.958 -2.890  37.010  1.00 26.12 ?  59  ARG A CG  1 
ATOM   452  C  CD  . ARG A 1 59  ? 44.899 -3.494  35.980  1.00 29.95 ?  59  ARG A CD  1 
ATOM   453  N  NE  . ARG A 1 59  ? 46.292 -3.196  36.290  1.00 32.17 ?  59  ARG A NE  1 
ATOM   454  C  CZ  . ARG A 1 59  ? 46.927 -2.099  35.887  1.00 23.88 ?  59  ARG A CZ  1 
ATOM   455  N  NH1 . ARG A 1 59  ? 46.288 -1.189  35.160  1.00 29.22 ?  59  ARG A NH1 1 
ATOM   456  N  NH2 . ARG A 1 59  ? 48.195 -1.903  36.229  1.00 25.58 ?  59  ARG A NH2 1 
ATOM   457  N  N   . GLU A 1 60  ? 41.153 -2.567  39.160  1.00 21.55 ?  60  GLU A N   1 
ATOM   458  C  CA  . GLU A 1 60  ? 39.946 -1.857  38.740  1.00 22.10 ?  60  GLU A CA  1 
ATOM   459  C  C   . GLU A 1 60  ? 39.677 -0.639  39.622  1.00 23.00 ?  60  GLU A C   1 
ATOM   460  O  O   . GLU A 1 60  ? 39.381 0.452   39.121  1.00 24.42 ?  60  GLU A O   1 
ATOM   461  C  CB  . GLU A 1 60  ? 38.745 -2.802  38.750  1.00 31.08 ?  60  GLU A CB  1 
ATOM   462  C  CG  . GLU A 1 60  ? 37.541 -2.227  38.026  1.00 40.06 ?  60  GLU A CG  1 
ATOM   463  C  CD  . GLU A 1 60  ? 36.259 -2.987  38.303  1.00 59.06 ?  60  GLU A CD  1 
ATOM   464  O  OE1 . GLU A 1 60  ? 35.562 -2.647  39.284  1.00 61.06 ?  60  GLU A OE1 1 
ATOM   465  O  OE2 . GLU A 1 60  ? 35.939 -3.916  37.530  1.00 53.82 -1 60  GLU A OE2 1 
ATOM   466  N  N   . THR A 1 61  ? 39.781 -0.811  40.947  1.00 21.71 ?  61  THR A N   1 
ATOM   467  C  CA  . THR A 1 61  ? 39.594 0.311   41.862  1.00 18.64 ?  61  THR A CA  1 
ATOM   468  C  C   . THR A 1 61  ? 40.645 1.393   41.637  1.00 18.24 ?  61  THR A C   1 
ATOM   469  O  O   . THR A 1 61  ? 40.315 2.584   41.578  1.00 21.42 ?  61  THR A O   1 
ATOM   470  C  CB  . THR A 1 61  ? 39.642 -0.192  43.309  1.00 18.16 ?  61  THR A CB  1 
ATOM   471  O  OG1 . THR A 1 61  ? 38.515 -1.046  43.558  1.00 20.32 ?  61  THR A OG1 1 
ATOM   472  C  CG2 . THR A 1 61  ? 39.609 0.985   44.304  1.00 19.91 ?  61  THR A CG2 1 
ATOM   473  N  N   . LEU A 1 62  ? 41.913 0.995   41.490  1.00 18.54 ?  62  LEU A N   1 
ATOM   474  C  CA  . LEU A 1 62  ? 42.982 1.970   41.335  1.00 18.24 ?  62  LEU A CA  1 
ATOM   475  C  C   . LEU A 1 62  ? 42.831 2.764   40.044  1.00 19.74 ?  62  LEU A C   1 
ATOM   476  O  O   . LEU A 1 62  ? 43.085 3.969   40.018  1.00 19.09 ?  62  LEU A O   1 
ATOM   477  C  CB  . LEU A 1 62  ? 44.338 1.266   41.375  1.00 17.73 ?  62  LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 62  ? 44.751 0.764   42.761  1.00 19.11 ?  62  LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 62  ? 45.902 -0.217  42.655  1.00 18.92 ?  62  LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 62  ? 45.128 1.942   43.688  1.00 18.87 ?  62  LEU A CD2 1 
ATOM   481  N  N   . VAL A 1 63  ? 42.432 2.102   38.956  1.00 19.52 ?  63  VAL A N   1 
ATOM   482  C  CA  . VAL A 1 63  ? 42.240 2.816   37.696  1.00 21.78 ?  63  VAL A CA  1 
ATOM   483  C  C   . VAL A 1 63  ? 41.090 3.808   37.821  1.00 20.35 ?  63  VAL A C   1 
ATOM   484  O  O   . VAL A 1 63  ? 41.171 4.941   37.321  1.00 22.30 ?  63  VAL A O   1 
ATOM   485  C  CB  . VAL A 1 63  ? 42.014 1.815   36.545  1.00 26.05 ?  63  VAL A CB  1 
ATOM   486  C  CG1 . VAL A 1 63  ? 41.494 2.526   35.298  1.00 26.90 ?  63  VAL A CG1 1 
ATOM   487  C  CG2 . VAL A 1 63  ? 43.288 1.071   36.235  1.00 25.09 ?  63  VAL A CG2 1 
ATOM   488  N  N   . ALA A 1 64  ? 40.011 3.409   38.508  1.00 19.58 ?  64  ALA A N   1 
ATOM   489  C  CA  . ALA A 1 64  ? 38.871 4.306   38.662  1.00 21.65 ?  64  ALA A CA  1 
ATOM   490  C  C   . ALA A 1 64  ? 39.219 5.490   39.557  1.00 22.40 ?  64  ALA A C   1 
ATOM   491  O  O   . ALA A 1 64  ? 38.770 6.615   39.307  1.00 21.52 ?  64  ALA A O   1 
ATOM   492  C  CB  . ALA A 1 64  ? 37.664 3.538   39.200  1.00 22.70 ?  64  ALA A CB  1 
ATOM   493  N  N   . VAL A 1 65  ? 40.026 5.267   40.598  1.00 23.03 ?  65  VAL A N   1 
ATOM   494  C  CA  . VAL A 1 65  ? 40.441 6.393   41.429  1.00 21.13 ?  65  VAL A CA  1 
ATOM   495  C  C   . VAL A 1 65  ? 41.332 7.329   40.630  1.00 22.07 ?  65  VAL A C   1 
ATOM   496  O  O   . VAL A 1 65  ? 41.198 8.557   40.717  1.00 21.96 ?  65  VAL A O   1 
ATOM   497  C  CB  . VAL A 1 65  ? 41.141 5.906   42.714  1.00 18.11 ?  65  VAL A CB  1 
ATOM   498  C  CG1 . VAL A 1 65  ? 41.806 7.087   43.450  1.00 19.57 ?  65  VAL A CG1 1 
ATOM   499  C  CG2 . VAL A 1 65  ? 40.158 5.193   43.632  1.00 19.26 ?  65  VAL A CG2 1 
ATOM   500  N  N   . ARG A 1 66  ? 42.233 6.765   39.816  1.00 19.39 ?  66  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 66  ? 43.106 7.588   38.985  1.00 18.65 ?  66  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 66  ? 42.296 8.491   38.069  1.00 19.54 ?  66  ARG A C   1 
ATOM   503  O  O   . ARG A 1 66  ? 42.605 9.679   37.912  1.00 21.02 ?  66  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 66  ? 44.046 6.710   38.155  1.00 22.15 ?  66  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 66  ? 44.856 7.503   37.141  1.00 23.85 ?  66  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 66  ? 45.866 6.600   36.447  1.00 31.20 ?  66  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 66  ? 46.387 7.150   35.200  1.00 47.19 ?  66  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 66  ? 47.628 7.603   35.033  1.00 51.45 ?  66  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 66  ? 48.495 7.589   36.041  1.00 41.57 ?  66  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 66  ? 48.002 8.074   33.851  1.00 46.34 ?  66  ARG A NH2 1 
ATOM   511  N  N   . GLU A 1 67  ? 41.258 7.942   37.449  1.00 21.97 ?  67  GLU A N   1 
ATOM   512  C  CA  . GLU A 1 67  ? 40.494 8.747   36.508  1.00 26.09 ?  67  GLU A CA  1 
ATOM   513  C  C   . GLU A 1 67  ? 39.752 9.867   37.225  1.00 20.05 ?  67  GLU A C   1 
ATOM   514  O  O   . GLU A 1 67  ? 39.791 11.019  36.778  1.00 23.40 ?  67  GLU A O   1 
ATOM   515  C  CB  . GLU A 1 67  ? 39.553 7.847   35.710  1.00 29.38 ?  67  GLU A CB  1 
ATOM   516  C  CG  . GLU A 1 67  ? 40.282 7.135   34.568  1.00 35.02 ?  67  GLU A CG  1 
ATOM   517  C  CD  . GLU A 1 67  ? 39.488 5.993   33.954  1.00 51.70 ?  67  GLU A CD  1 
ATOM   518  O  OE1 . GLU A 1 67  ? 40.060 5.251   33.124  1.00 49.60 ?  67  GLU A OE1 1 
ATOM   519  O  OE2 . GLU A 1 67  ? 38.297 5.839   34.298  1.00 55.22 -1 67  GLU A OE2 1 
ATOM   520  N  N   . ALA A 1 68  ? 39.135 9.570   38.374  1.00 23.35 ?  68  ALA A N   1 
ATOM   521  C  CA  . ALA A 1 68  ? 38.436 10.619  39.113  1.00 21.51 ?  68  ALA A CA  1 
ATOM   522  C  C   . ALA A 1 68  ? 39.409 11.672  39.641  1.00 23.86 ?  68  ALA A C   1 
ATOM   523  O  O   . ALA A 1 68  ? 39.130 12.877  39.566  1.00 23.41 ?  68  ALA A O   1 
ATOM   524  C  CB  . ALA A 1 68  ? 37.615 10.015  40.253  1.00 25.76 ?  68  ALA A CB  1 
ATOM   525  N  N   . ALA A 1 69  ? 40.557 11.246  40.170  1.00 20.76 ?  69  ALA A N   1 
ATOM   526  C  CA  . ALA A 1 69  ? 41.525 12.216  40.683  1.00 20.69 ?  69  ALA A CA  1 
ATOM   527  C  C   . ALA A 1 69  ? 42.085 13.097  39.568  1.00 19.52 ?  69  ALA A C   1 
ATOM   528  O  O   . ALA A 1 69  ? 42.341 14.291  39.776  1.00 20.89 ?  69  ALA A O   1 
ATOM   529  C  CB  . ALA A 1 69  ? 42.662 11.488  41.404  1.00 24.99 ?  69  ALA A CB  1 
ATOM   530  N  N   . THR A 1 70  ? 42.299 12.525  38.382  1.00 19.92 ?  70  THR A N   1 
ATOM   531  C  CA  . THR A 1 70  ? 42.807 13.314  37.264  1.00 22.20 ?  70  THR A CA  1 
ATOM   532  C  C   . THR A 1 70  ? 41.850 14.445  36.900  1.00 23.30 ?  70  THR A C   1 
ATOM   533  O  O   . THR A 1 70  ? 42.273 15.596  36.746  1.00 24.08 ?  70  THR A O   1 
ATOM   534  C  CB  . THR A 1 70  ? 43.059 12.415  36.058  1.00 24.29 ?  70  THR A CB  1 
ATOM   535  O  OG1 . THR A 1 70  ? 43.995 11.395  36.421  1.00 24.69 ?  70  THR A OG1 1 
ATOM   536  C  CG2 . THR A 1 70  ? 43.660 13.237  34.915  1.00 24.68 ?  70  THR A CG2 1 
ATOM   537  N  N   . GLU A 1 71  ? 40.557 14.134  36.760  1.00 26.05 ?  71  GLU A N   1 
ATOM   538  C  CA  . GLU A 1 71  ? 39.570 15.165  36.441  1.00 30.78 ?  71  GLU A CA  1 
ATOM   539  C  C   . GLU A 1 71  ? 39.594 16.276  37.478  1.00 29.48 ?  71  GLU A C   1 
ATOM   540  O  O   . GLU A 1 71  ? 39.608 17.463  37.133  1.00 26.96 ?  71  GLU A O   1 
ATOM   541  C  CB  . GLU A 1 71  ? 38.158 14.574  36.350  1.00 32.78 ?  71  GLU A CB  1 
ATOM   542  C  CG  . GLU A 1 71  ? 38.012 13.191  35.723  1.00 40.85 ?  71  GLU A CG  1 
ATOM   543  C  CD  . GLU A 1 71  ? 38.777 13.018  34.424  1.00 52.31 ?  71  GLU A CD  1 
ATOM   544  O  OE1 . GLU A 1 71  ? 38.781 13.963  33.601  1.00 55.56 ?  71  GLU A OE1 1 
ATOM   545  O  OE2 . GLU A 1 71  ? 39.363 11.928  34.220  1.00 50.93 -1 71  GLU A OE2 1 
ATOM   546  N  N   . SER A 1 72  ? 39.621 15.899  38.762  1.00 24.14 ?  72  SER A N   1 
ATOM   547  C  CA  . SER A 1 72  ? 39.600 16.892  39.831  1.00 21.27 ?  72  SER A CA  1 
ATOM   548  C  C   . SER A 1 72  ? 40.867 17.744  39.832  1.00 23.57 ?  72  SER A C   1 
ATOM   549  O  O   . SER A 1 72  ? 40.798 18.970  39.979  1.00 22.63 ?  72  SER A O   1 
ATOM   550  C  CB  . SER A 1 72  ? 39.426 16.186  41.178  1.00 17.92 ?  72  SER A CB  1 
ATOM   551  O  OG  . SER A 1 72  ? 39.438 17.122  42.236  1.00 20.17 ?  72  SER A OG  1 
ATOM   552  N  N   . ILE A 1 73  ? 42.033 17.116  39.672  1.00 19.73 ?  73  ILE A N   1 
ATOM   553  C  CA  . ILE A 1 73  ? 43.287 17.862  39.660  1.00 22.77 ?  73  ILE A CA  1 
ATOM   554  C  C   . ILE A 1 73  ? 43.361 18.794  38.450  1.00 28.64 ?  73  ILE A C   1 
ATOM   555  O  O   . ILE A 1 73  ? 43.948 19.882  38.526  1.00 28.54 ?  73  ILE A O   1 
ATOM   556  C  CB  . ILE A 1 73  ? 44.460 16.864  39.716  1.00 23.83 ?  73  ILE A CB  1 
ATOM   557  C  CG1 . ILE A 1 73  ? 44.524 16.227  41.110  1.00 21.81 ?  73  ILE A CG1 1 
ATOM   558  C  CG2 . ILE A 1 73  ? 45.781 17.541  39.391  1.00 26.77 ?  73  ILE A CG2 1 
ATOM   559  C  CD1 . ILE A 1 73  ? 45.395 14.988  41.194  1.00 24.62 ?  73  ILE A CD1 1 
ATOM   560  N  N   . LYS A 1 74  ? 42.744 18.414  37.333  1.00 21.25 ?  74  LYS A N   1 
ATOM   561  C  CA  . LYS A 1 74  ? 42.751 19.273  36.154  1.00 28.02 ?  74  LYS A CA  1 
ATOM   562  C  C   . LYS A 1 74  ? 41.812 20.468  36.281  1.00 30.45 ?  74  LYS A C   1 
ATOM   563  O  O   . LYS A 1 74  ? 42.024 21.476  35.598  1.00 33.78 ?  74  LYS A O   1 
ATOM   564  C  CB  . LYS A 1 74  ? 42.400 18.446  34.913  1.00 25.81 ?  74  LYS A CB  1 
ATOM   565  C  CG  . LYS A 1 74  ? 43.555 17.568  34.437  1.00 30.29 ?  74  LYS A CG  1 
ATOM   566  C  CD  . LYS A 1 74  ? 43.292 16.970  33.073  1.00 35.36 ?  74  LYS A CD  1 
ATOM   567  C  CE  . LYS A 1 74  ? 44.464 16.117  32.611  1.00 41.02 ?  74  LYS A CE  1 
ATOM   568  N  NZ  . LYS A 1 74  ? 44.129 15.337  31.385  1.00 40.32 ?  74  LYS A NZ  1 
ATOM   569  N  N   . GLY A 1 75  ? 40.804 20.391  37.150  1.00 25.66 ?  75  GLY A N   1 
ATOM   570  C  CA  . GLY A 1 75  ? 39.861 21.473  37.358  1.00 27.07 ?  75  GLY A CA  1 
ATOM   571  C  C   . GLY A 1 75  ? 40.342 22.506  38.360  1.00 23.05 ?  75  GLY A C   1 
ATOM   572  O  O   . GLY A 1 75  ? 41.540 22.669  38.609  1.00 28.53 ?  75  GLY A O   1 
ATOM   573  N  N   . ASP A 1 76  ? 39.380 23.204  38.961  1.00 27.71 ?  76  ASP A N   1 
ATOM   574  C  CA  . ASP A 1 76  ? 39.666 24.366  39.790  1.00 33.95 ?  76  ASP A CA  1 
ATOM   575  C  C   . ASP A 1 76  ? 39.397 24.159  41.277  1.00 26.93 ?  76  ASP A C   1 
ATOM   576  O  O   . ASP A 1 76  ? 39.537 25.111  42.049  1.00 30.12 ?  76  ASP A O   1 
ATOM   577  C  CB  . ASP A 1 76  ? 38.851 25.568  39.294  1.00 38.67 ?  76  ASP A CB  1 
ATOM   578  C  CG  . ASP A 1 76  ? 39.453 26.213  38.056  1.00 46.58 ?  76  ASP A CG  1 
ATOM   579  O  OD1 . ASP A 1 76  ? 39.951 25.477  37.177  1.00 50.28 -1 76  ASP A OD1 1 
ATOM   580  O  OD2 . ASP A 1 76  ? 39.428 27.458  37.961  1.00 61.48 -1 76  ASP A OD2 1 
ATOM   581  N  N   . ASN A 1 77  ? 39.029 22.959  41.704  1.00 25.32 ?  77  ASN A N   1 
ATOM   582  C  CA  . ASN A 1 77  ? 38.636 22.730  43.089  1.00 28.48 ?  77  ASN A CA  1 
ATOM   583  C  C   . ASN A 1 77  ? 39.765 22.084  43.894  1.00 24.44 ?  77  ASN A C   1 
ATOM   584  O  O   . ASN A 1 77  ? 40.792 21.661  43.358  1.00 21.27 ?  77  ASN A O   1 
ATOM   585  C  CB  . ASN A 1 77  ? 37.379 21.857  43.149  1.00 27.06 ?  77  ASN A CB  1 
ATOM   586  C  CG  . ASN A 1 77  ? 36.176 22.524  42.512  1.00 37.26 ?  77  ASN A CG  1 
ATOM   587  O  OD1 . ASN A 1 77  ? 36.102 23.754  42.425  1.00 35.66 ?  77  ASN A OD1 1 
ATOM   588  N  ND2 . ASN A 1 77  ? 35.226 21.716  42.062  1.00 36.82 ?  77  ASN A ND2 1 
ATOM   589  N  N   . LEU A 1 78  ? 39.562 22.023  45.213  1.00 21.03 ?  78  LEU A N   1 
ATOM   590  C  CA  . LEU A 1 78  ? 40.435 21.246  46.090  1.00 19.65 ?  78  LEU A CA  1 
ATOM   591  C  C   . LEU A 1 78  ? 40.080 19.771  45.967  1.00 19.44 ?  78  LEU A C   1 
ATOM   592  O  O   . LEU A 1 78  ? 38.927 19.388  46.187  1.00 20.87 ?  78  LEU A O   1 
ATOM   593  C  CB  . LEU A 1 78  ? 40.290 21.698  47.542  1.00 18.85 ?  78  LEU A CB  1 
ATOM   594  C  CG  . LEU A 1 78  ? 41.157 20.918  48.546  1.00 17.38 ?  78  LEU A CG  1 
ATOM   595  C  CD1 . LEU A 1 78  ? 42.620 21.253  48.370  1.00 17.21 ?  78  LEU A CD1 1 
ATOM   596  C  CD2 . LEU A 1 78  ? 40.737 21.181  49.987  1.00 16.66 ?  78  LEU A CD2 1 
ATOM   597  N  N   . THR A 1 79  ? 41.060 18.943  45.630  1.00 15.34 ?  79  THR A N   1 
ATOM   598  C  CA  . THR A 1 79  ? 40.845 17.507  45.501  1.00 13.95 ?  79  THR A CA  1 
ATOM   599  C  C   . THR A 1 79  ? 40.991 16.845  46.871  1.00 15.71 ?  79  THR A C   1 
ATOM   600  O  O   . THR A 1 79  ? 42.068 16.894  47.472  1.00 15.16 ?  79  THR A O   1 
ATOM   601  C  CB  . THR A 1 79  ? 41.837 16.916  44.509  1.00 15.69 ?  79  THR A CB  1 
ATOM   602  O  OG1 . THR A 1 79  ? 41.763 17.633  43.262  1.00 18.19 ?  79  THR A OG1 1 
ATOM   603  C  CG2 . THR A 1 79  ? 41.572 15.433  44.279  1.00 19.91 ?  79  THR A CG2 1 
ATOM   604  N  N   . VAL A 1 80  ? 39.921 16.241  47.376  1.00 15.33 ?  80  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 80  ? 39.962 15.539  48.659  1.00 12.21 ?  80  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 80  ? 39.634 14.071  48.416  1.00 16.37 ?  80  VAL A C   1 
ATOM   607  O  O   . VAL A 1 80  ? 38.531 13.738  47.961  1.00 16.22 ?  80  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 80  ? 38.992 16.156  49.686  1.00 13.49 ?  80  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 80  ? 39.017 15.374  50.989  1.00 15.08 ?  80  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 80  ? 39.334 17.621  49.951  1.00 15.72 ?  80  VAL A CG2 1 
ATOM   611  N  N   . LEU A 1 81  ? 40.589 13.195  48.709  1.00 14.36 ?  81  LEU A N   1 
ATOM   612  C  CA  . LEU A 1 81  ? 40.401 11.757  48.625  1.00 13.45 ?  81  LEU A CA  1 
ATOM   613  C  C   . LEU A 1 81  ? 40.295 11.189  50.029  1.00 13.79 ?  81  LEU A C   1 
ATOM   614  O  O   . LEU A 1 81  ? 41.176 11.418  50.865  1.00 15.45 ?  81  LEU A O   1 
ATOM   615  C  CB  . LEU A 1 81  ? 41.556 11.089  47.885  1.00 16.79 ?  81  LEU A CB  1 
ATOM   616  C  CG  . LEU A 1 81  ? 41.558 11.415  46.402  1.00 16.96 ?  81  LEU A CG  1 
ATOM   617  C  CD1 . LEU A 1 81  ? 42.865 12.036  46.001  1.00 19.00 ?  81  LEU A CD1 1 
ATOM   618  C  CD2 . LEU A 1 81  ? 41.274 10.138  45.600  1.00 20.19 ?  81  LEU A CD2 1 
ATOM   619  N  N   . VAL A 1 82  ? 39.215 10.470  50.301  1.00 14.39 ?  82  VAL A N   1 
ATOM   620  C  CA  . VAL A 1 82  ? 39.095 9.728   51.547  1.00 13.35 ?  82  VAL A CA  1 
ATOM   621  C  C   . VAL A 1 82  ? 39.279 8.263   51.195  1.00 16.26 ?  82  VAL A C   1 
ATOM   622  O  O   . VAL A 1 82  ? 38.410 7.660   50.552  1.00 17.06 ?  82  VAL A O   1 
ATOM   623  C  CB  . VAL A 1 82  ? 37.756 9.985   52.247  1.00 14.65 ?  82  VAL A CB  1 
ATOM   624  C  CG1 . VAL A 1 82  ? 37.647 9.132   53.490  1.00 15.85 ?  82  VAL A CG1 1 
ATOM   625  C  CG2 . VAL A 1 82  ? 37.627 11.456  52.581  1.00 15.13 ?  82  VAL A CG2 1 
ATOM   626  N  N   . ASN A 1 83  ? 40.428 7.702   51.584  1.00 14.28 ?  83  ASN A N   1 
ATOM   627  C  CA  . ASN A 1 83  ? 40.892 6.408   51.101  1.00 14.09 ?  83  ASN A CA  1 
ATOM   628  C  C   . ASN A 1 83  ? 40.910 5.379   52.223  1.00 12.94 ?  83  ASN A C   1 
ATOM   629  O  O   . ASN A 1 83  ? 41.245 5.700   53.370  1.00 14.27 ?  83  ASN A O   1 
ATOM   630  C  CB  . ASN A 1 83  ? 42.289 6.522   50.499  1.00 15.06 ?  83  ASN A CB  1 
ATOM   631  C  CG  . ASN A 1 83  ? 42.326 7.430   49.275  1.00 15.09 ?  83  ASN A CG  1 
ATOM   632  O  OD1 . ASN A 1 83  ? 41.325 7.560   48.560  1.00 19.49 ?  83  ASN A OD1 1 
ATOM   633  N  ND2 . ASN A 1 83  ? 43.466 8.052   49.035  1.00 15.19 ?  83  ASN A ND2 1 
ATOM   634  N  N   . ASN A 1 84  ? 40.552 4.132   51.900  1.00 13.90 ?  84  ASN A N   1 
ATOM   635  C  CA  . ASN A 1 84  ? 40.620 3.090   52.917  1.00 14.14 ?  84  ASN A CA  1 
ATOM   636  C  C   . ASN A 1 84  ? 42.069 2.845   53.329  1.00 14.10 ?  84  ASN A C   1 
ATOM   637  O  O   . ASN A 1 84  ? 42.385 2.836   54.525  1.00 15.28 ?  84  ASN A O   1 
ATOM   638  C  CB  . ASN A 1 84  ? 39.919 1.802   52.438  1.00 15.44 ?  84  ASN A CB  1 
ATOM   639  C  CG  . ASN A 1 84  ? 40.264 1.401   50.998  1.00 15.16 ?  84  ASN A CG  1 
ATOM   640  O  OD1 . ASN A 1 84  ? 40.278 2.223   50.081  1.00 16.78 ?  84  ASN A OD1 1 
ATOM   641  N  ND2 . ASN A 1 84  ? 40.507 0.099   50.792  1.00 15.57 ?  84  ASN A ND2 1 
ATOM   642  N  N   . THR A 1 85  ? 42.982 2.724   52.360  1.00 14.38 ?  85  THR A N   1 
ATOM   643  C  CA  . THR A 1 85  ? 44.383 2.432   52.650  1.00 14.73 ?  85  THR A CA  1 
ATOM   644  C  C   . THR A 1 85  ? 45.309 3.407   51.933  1.00 13.29 ?  85  THR A C   1 
ATOM   645  O  O   . THR A 1 85  ? 44.936 4.055   50.946  1.00 14.45 ?  85  THR A O   1 
ATOM   646  C  CB  . THR A 1 85  ? 44.784 1.009   52.229  1.00 14.57 ?  85  THR A CB  1 
ATOM   647  O  OG1 . THR A 1 85  ? 44.666 0.881   50.800  1.00 14.60 ?  85  THR A OG1 1 
ATOM   648  C  CG2 . THR A 1 85  ? 43.928 -0.040  52.914  1.00 16.10 ?  85  THR A CG2 1 
ATOM   649  N  N   . CYS A 1 86  ? 46.535 3.516   52.461  1.00 11.12 ?  86  CYS A N   1 
ATOM   650  C  CA  . CYS A 1 86  ? 47.541 4.324   51.783  1.00 11.67 ?  86  CYS A CA  1 
ATOM   651  C  C   . CYS A 1 86  ? 47.787 3.831   50.364  1.00 12.73 ?  86  CYS A C   1 
ATOM   652  O  O   . CYS A 1 86  ? 48.207 4.620   49.511  1.00 11.88 ?  86  CYS A O   1 
ATOM   653  C  CB  . CYS A 1 86  ? 48.866 4.312   52.559  1.00 13.10 ?  86  CYS A CB  1 
ATOM   654  S  SG  . CYS A 1 86  ? 48.826 5.309   54.081  1.00 13.71 ?  86  CYS A SG  1 
ATOM   655  N  N   . SER A 1 87  ? 47.569 2.530   50.104  1.00 14.21 ?  87  SER A N   1 
ATOM   656  C  CA  . SER A 1 87  ? 47.880 1.963   48.790  1.00 12.89 ?  87  SER A CA  1 
ATOM   657  C  C   . SER A 1 87  ? 47.051 2.573   47.673  1.00 13.18 ?  87  SER A C   1 
ATOM   658  O  O   . SER A 1 87  ? 47.475 2.509   46.515  1.00 13.90 ?  87  SER A O   1 
ATOM   659  C  CB  . SER A 1 87  ? 47.702 0.445   48.816  1.00 15.29 ?  87  SER A CB  1 
ATOM   660  O  OG  . SER A 1 87  ? 48.627 -0.145  49.695  1.00 16.53 ?  87  SER A OG  1 
ATOM   661  N  N   . VAL A 1 88  ? 45.909 3.195   47.982  1.00 13.66 ?  88  VAL A N   1 
ATOM   662  C  CA  . VAL A 1 88  ? 45.176 3.936   46.949  1.00 14.15 ?  88  VAL A CA  1 
ATOM   663  C  C   . VAL A 1 88  ? 46.066 4.987   46.291  1.00 14.47 ?  88  VAL A C   1 
ATOM   664  O  O   . VAL A 1 88  ? 45.899 5.306   45.107  1.00 16.27 ?  88  VAL A O   1 
ATOM   665  C  CB  . VAL A 1 88  ? 43.899 4.551   47.565  1.00 14.65 ?  88  VAL A CB  1 
ATOM   666  C  CG1 . VAL A 1 88  ? 43.149 5.417   46.540  1.00 16.40 ?  88  VAL A CG1 1 
ATOM   667  C  CG2 . VAL A 1 88  ? 43.022 3.441   48.082  1.00 15.54 ?  88  VAL A CG2 1 
ATOM   668  N  N   . SER A 1 89  ? 47.053 5.519   47.022  1.00 11.67 ?  89  SER A N   1 
ATOM   669  C  CA  . SER A 1 89  ? 47.887 6.586   46.499  1.00 13.13 ?  89  SER A CA  1 
ATOM   670  C  C   . SER A 1 89  ? 48.899 6.102   45.459  1.00 14.02 ?  89  SER A C   1 
ATOM   671  O  O   . SER A 1 89  ? 49.588 6.938   44.862  1.00 14.38 ?  89  SER A O   1 
ATOM   672  C  CB  . SER A 1 89  ? 48.583 7.277   47.673  1.00 13.91 ?  89  SER A CB  1 
ATOM   673  O  OG  . SER A 1 89  ? 47.602 7.790   48.560  1.00 15.87 ?  89  SER A OG  1 
ATOM   674  N  N   . LEU A 1 90  ? 49.023 4.781   45.240  1.00 14.42 ?  90  LEU A N   1 
ATOM   675  C  CA  . LEU A 1 90  ? 49.787 4.303   44.091  1.00 15.81 ?  90  LEU A CA  1 
ATOM   676  C  C   . LEU A 1 90  ? 49.171 4.804   42.790  1.00 16.47 ?  90  LEU A C   1 
ATOM   677  O  O   . LEU A 1 90  ? 49.885 4.984   41.790  1.00 17.30 ?  90  LEU A O   1 
ATOM   678  C  CB  . LEU A 1 90  ? 49.854 2.777   44.114  1.00 15.48 ?  90  LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 90  ? 50.770 2.229   45.208  1.00 15.04 ?  90  LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 90  ? 50.528 0.730   45.384  1.00 17.73 ?  90  LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 90  ? 52.233 2.492   44.889  1.00 18.37 ?  90  LEU A CD2 1 
ATOM   682  N  N   . ALA A 1 91  ? 47.872 5.078   42.805  1.00 15.23 ?  91  ALA A N   1 
ATOM   683  C  CA  . ALA A 1 91  ? 47.165 5.617   41.647  1.00 18.49 ?  91  ALA A CA  1 
ATOM   684  C  C   . ALA A 1 91  ? 47.161 7.141   41.599  1.00 21.44 ?  91  ALA A C   1 
ATOM   685  O  O   . ALA A 1 91  ? 47.175 7.718   40.503  1.00 23.97 ?  91  ALA A O   1 
ATOM   686  C  CB  . ALA A 1 91  ? 45.718 5.109   41.631  1.00 20.81 ?  91  ALA A CB  1 
ATOM   687  N  N   . THR A 1 92  ? 47.154 7.819   42.747  1.00 15.24 ?  92  THR A N   1 
ATOM   688  C  CA  . THR A 1 92  ? 46.990 9.269   42.734  1.00 16.55 ?  92  THR A CA  1 
ATOM   689  C  C   . THR A 1 92  ? 48.308 10.040  42.676  1.00 16.01 ?  92  THR A C   1 
ATOM   690  O  O   . THR A 1 92  ? 48.390 11.069  41.983  1.00 17.24 ?  92  THR A O   1 
ATOM   691  C  CB  . THR A 1 92  ? 46.218 9.716   43.975  1.00 16.90 ?  92  THR A CB  1 
ATOM   692  O  OG1 . THR A 1 92  ? 46.976 9.332   45.128  1.00 18.45 ?  92  THR A OG1 1 
ATOM   693  C  CG2 . THR A 1 92  ? 44.828 9.058   44.032  1.00 20.46 ?  92  THR A CG2 1 
ATOM   694  N  N   . LEU A 1 93  ? 49.344 9.587   43.391  1.00 13.10 ?  93  LEU A N   1 
ATOM   695  C  CA  . LEU A 1 93  ? 50.593 10.346  43.429  1.00 12.44 ?  93  LEU A CA  1 
ATOM   696  C  C   . LEU A 1 93  ? 51.252 10.476  42.058  1.00 15.23 ?  93  LEU A C   1 
ATOM   697  O  O   . LEU A 1 93  ? 51.816 11.553  41.784  1.00 15.93 ?  93  LEU A O   1 
ATOM   698  C  CB  . LEU A 1 93  ? 51.550 9.734   44.464  1.00 14.81 ?  93  LEU A CB  1 
ATOM   699  C  CG  . LEU A 1 93  ? 51.042 9.850   45.915  1.00 13.80 ?  93  LEU A CG  1 
ATOM   700  C  CD1 . LEU A 1 93  ? 51.991 9.106   46.830  1.00 15.88 ?  93  LEU A CD1 1 
ATOM   701  C  CD2 . LEU A 1 93  ? 50.943 11.308  46.319  1.00 14.28 ?  93  LEU A CD2 1 
ATOM   702  N  N   . PRO A 1 94  ? 51.210 9.477   41.160  1.00 16.34 ?  94  PRO A N   1 
ATOM   703  C  CA  . PRO A 1 94  ? 51.750 9.722   39.808  1.00 15.40 ?  94  PRO A CA  1 
ATOM   704  C  C   . PRO A 1 94  ? 50.996 10.813  39.057  1.00 17.02 ?  94  PRO A C   1 
ATOM   705  O  O   . PRO A 1 94  ? 51.611 11.555  38.278  1.00 19.49 ?  94  PRO A O   1 
ATOM   706  C  CB  . PRO A 1 94  ? 51.619 8.349   39.128  1.00 16.50 ?  94  PRO A CB  1 
ATOM   707  C  CG  . PRO A 1 94  ? 51.738 7.364   40.268  1.00 14.73 ?  94  PRO A CG  1 
ATOM   708  C  CD  . PRO A 1 94  ? 50.892 8.043   41.353  1.00 15.67 ?  94  PRO A CD  1 
ATOM   709  N  N   . VAL A 1 95  ? 49.690 10.951  39.279  1.00 19.21 ?  95  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 95  ? 48.932 12.026  38.638  1.00 19.42 ?  95  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 95  ? 49.381 13.382  39.168  1.00 21.42 ?  95  VAL A C   1 
ATOM   712  O  O   . VAL A 1 95  ? 49.616 14.329  38.403  1.00 19.37 ?  95  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 95  ? 47.422 11.824  38.848  1.00 22.31 ?  95  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 95  ? 46.653 12.942  38.167  1.00 24.86 ?  95  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 95  ? 46.977 10.439  38.323  1.00 25.34 ?  95  VAL A CG2 1 
ATOM   716  N  N   . VAL A 1 96  ? 49.501 13.498  40.490  1.00 17.88 ?  96  VAL A N   1 
ATOM   717  C  CA  . VAL A 1 96  ? 49.943 14.752  41.096  1.00 19.79 ?  96  VAL A CA  1 
ATOM   718  C  C   . VAL A 1 96  ? 51.290 15.174  40.521  1.00 16.64 ?  96  VAL A C   1 
ATOM   719  O  O   . VAL A 1 96  ? 51.484 16.335  40.135  1.00 18.78 ?  96  VAL A O   1 
ATOM   720  C  CB  . VAL A 1 96  ? 49.991 14.598  42.628  1.00 18.82 ?  96  VAL A CB  1 
ATOM   721  C  CG1 . VAL A 1 96  ? 50.484 15.876  43.295  1.00 19.33 ?  96  VAL A CG1 1 
ATOM   722  C  CG2 . VAL A 1 96  ? 48.615 14.213  43.162  1.00 18.21 ?  96  VAL A CG2 1 
ATOM   723  N  N   . ALA A 1 97  ? 52.234 14.231  40.426  1.00 17.25 ?  97  ALA A N   1 
ATOM   724  C  CA  . ALA A 1 97  ? 53.584 14.554  39.966  1.00 18.14 ?  97  ALA A CA  1 
ATOM   725  C  C   . ALA A 1 97  ? 53.598 14.949  38.494  1.00 16.05 ?  97  ALA A C   1 
ATOM   726  O  O   . ALA A 1 97  ? 54.402 15.796  38.081  1.00 23.19 ?  97  ALA A O   1 
ATOM   727  C  CB  . ALA A 1 97  ? 54.513 13.365  40.205  1.00 21.78 ?  97  ALA A CB  1 
ATOM   728  N  N   . ARG A 1 98  ? 52.734 14.334  37.692  1.00 17.69 ?  98  ARG A N   1 
ATOM   729  C  CA  . ARG A 1 98  ? 52.671 14.675  36.274  1.00 23.78 ?  98  ARG A CA  1 
ATOM   730  C  C   . ARG A 1 98  ? 52.048 16.050  36.069  1.00 22.32 ?  98  ARG A C   1 
ATOM   731  O  O   . ARG A 1 98  ? 52.564 16.874  35.299  1.00 22.22 ?  98  ARG A O   1 
ATOM   732  C  CB  . ARG A 1 98  ? 51.879 13.604  35.522  1.00 22.29 ?  98  ARG A CB  1 
ATOM   733  C  CG  . ARG A 1 98  ? 51.980 13.705  34.005  1.00 31.61 ?  98  ARG A CG  1 
ATOM   734  C  CD  . ARG A 1 98  ? 51.057 12.697  33.340  1.00 36.91 ?  98  ARG A CD  1 
ATOM   735  N  NE  . ARG A 1 98  ? 49.654 13.082  33.466  1.00 38.98 ?  98  ARG A NE  1 
ATOM   736  C  CZ  . ARG A 1 98  ? 48.711 12.329  34.024  1.00 44.72 ?  98  ARG A CZ  1 
ATOM   737  N  NH1 . ARG A 1 98  ? 49.011 11.131  34.513  1.00 44.03 ?  98  ARG A NH1 1 
ATOM   738  N  NH2 . ARG A 1 98  ? 47.463 12.776  34.090  1.00 41.92 ?  98  ARG A NH2 1 
ATOM   739  N  N   . GLU A 1 99  ? 50.942 16.317  36.763  1.00 19.04 ?  99  GLU A N   1 
ATOM   740  C  CA  . GLU A 1 99  ? 50.225 17.579  36.604  1.00 21.07 ?  99  GLU A CA  1 
ATOM   741  C  C   . GLU A 1 99  ? 50.942 18.735  37.297  1.00 24.12 ?  99  GLU A C   1 
ATOM   742  O  O   . GLU A 1 99  ? 50.825 19.888  36.864  1.00 24.76 ?  99  GLU A O   1 
ATOM   743  C  CB  . GLU A 1 99  ? 48.802 17.448  37.146  1.00 25.05 ?  99  GLU A CB  1 
ATOM   744  C  CG  . GLU A 1 99  ? 47.893 16.535  36.334  1.00 25.36 ?  99  GLU A CG  1 
ATOM   745  C  CD  . GLU A 1 99  ? 47.724 17.034  34.906  1.00 34.68 ?  99  GLU A CD  1 
ATOM   746  O  OE1 . GLU A 1 99  ? 47.938 16.244  33.966  1.00 36.67 ?  99  GLU A OE1 1 
ATOM   747  O  OE2 . GLU A 1 99  ? 47.388 18.224  34.733  1.00 35.36 -1 99  GLU A OE2 1 
ATOM   748  N  N   . HIS A 1 100 ? 51.680 18.459  38.371  1.00 19.58 ?  100 HIS A N   1 
ATOM   749  C  CA  . HIS A 1 100 ? 52.366 19.487  39.156  1.00 19.62 ?  100 HIS A CA  1 
ATOM   750  C  C   . HIS A 1 100 ? 53.780 19.008  39.443  1.00 20.38 ?  100 HIS A C   1 
ATOM   751  O  O   . HIS A 1 100 ? 54.088 18.568  40.560  1.00 17.97 ?  100 HIS A O   1 
ATOM   752  C  CB  . HIS A 1 100 ? 51.632 19.786  40.462  1.00 18.31 ?  100 HIS A CB  1 
ATOM   753  C  CG  . HIS A 1 100 ? 50.243 20.309  40.274  1.00 21.02 ?  100 HIS A CG  1 
ATOM   754  N  ND1 . HIS A 1 100 ? 49.976 21.640  40.027  1.00 26.23 ?  100 HIS A ND1 1 
ATOM   755  C  CD2 . HIS A 1 100 ? 49.044 19.680  40.284  1.00 23.08 ?  100 HIS A CD2 1 
ATOM   756  C  CE1 . HIS A 1 100 ? 48.670 21.807  39.901  1.00 28.69 ?  100 HIS A CE1 1 
ATOM   757  N  NE2 . HIS A 1 100 ? 48.083 20.634  40.055  1.00 27.95 ?  100 HIS A NE2 1 
ATOM   758  N  N   . PRO A 1 101 ? 54.672 19.085  38.455  1.00 17.75 ?  101 PRO A N   1 
ATOM   759  C  CA  . PRO A 1 101 ? 56.049 18.607  38.652  1.00 19.68 ?  101 PRO A CA  1 
ATOM   760  C  C   . PRO A 1 101 ? 56.800 19.346  39.743  1.00 16.45 ?  101 PRO A C   1 
ATOM   761  O  O   . PRO A 1 101 ? 57.782 18.811  40.268  1.00 18.53 ?  101 PRO A O   1 
ATOM   762  C  CB  . PRO A 1 101 ? 56.698 18.821  37.266  1.00 19.58 ?  101 PRO A CB  1 
ATOM   763  C  CG  . PRO A 1 101 ? 55.810 19.792  36.572  1.00 21.34 ?  101 PRO A CG  1 
ATOM   764  C  CD  . PRO A 1 101 ? 54.428 19.571  37.084  1.00 20.92 ?  101 PRO A CD  1 
ATOM   765  N  N   . ASP A 1 102 ? 56.335 20.532  40.141  1.00 16.56 ?  102 ASP A N   1 
ATOM   766  C  CA  . ASP A 1 102 ? 56.940 21.271  41.241  1.00 18.74 ?  102 ASP A CA  1 
ATOM   767  C  C   . ASP A 1 102 ? 56.264 21.012  42.593  1.00 15.08 ?  102 ASP A C   1 
ATOM   768  O  O   . ASP A 1 102 ? 56.704 21.572  43.598  1.00 16.82 ?  102 ASP A O   1 
ATOM   769  C  CB  . ASP A 1 102 ? 56.934 22.781  40.933  1.00 20.33 ?  102 ASP A CB  1 
ATOM   770  C  CG  . ASP A 1 102 ? 55.544 23.332  40.653  1.00 26.72 ?  102 ASP A CG  1 
ATOM   771  O  OD1 . ASP A 1 102 ? 54.610 22.567  40.306  1.00 22.74 ?  102 ASP A OD1 1 
ATOM   772  O  OD2 . ASP A 1 102 ? 55.390 24.570  40.770  1.00 31.06 -1 102 ASP A OD2 1 
ATOM   773  N  N   . ALA A 1 103 ? 55.249 20.155  42.648  1.00 15.12 ?  103 ALA A N   1 
ATOM   774  C  CA  . ALA A 1 103 ? 54.563 19.909  43.913  1.00 16.44 ?  103 ALA A CA  1 
ATOM   775  C  C   . ALA A 1 103 ? 55.489 19.224  44.911  1.00 16.19 ?  103 ALA A C   1 
ATOM   776  O  O   . ALA A 1 103 ? 56.321 18.392  44.545  1.00 14.91 ?  103 ALA A O   1 
ATOM   777  C  CB  . ALA A 1 103 ? 53.329 19.039  43.689  1.00 13.63 ?  103 ALA A CB  1 
ATOM   778  N  N   . VAL A 1 104 ? 55.346 19.587  46.184  1.00 12.42 ?  104 VAL A N   1 
ATOM   779  C  CA  . VAL A 1 104 ? 55.920 18.831  47.286  1.00 12.58 ?  104 VAL A CA  1 
ATOM   780  C  C   . VAL A 1 104 ? 54.815 17.972  47.890  1.00 11.84 ?  104 VAL A C   1 
ATOM   781  O  O   . VAL A 1 104 ? 53.714 18.469  48.172  1.00 13.69 ?  104 VAL A O   1 
ATOM   782  C  CB  . VAL A 1 104 ? 56.522 19.761  48.351  1.00 13.13 ?  104 VAL A CB  1 
ATOM   783  C  CG1 . VAL A 1 104 ? 56.859 18.984  49.623  1.00 15.37 ?  104 VAL A CG1 1 
ATOM   784  C  CG2 . VAL A 1 104 ? 57.782 20.471  47.795  1.00 13.56 ?  104 VAL A CG2 1 
ATOM   785  N  N   . VAL A 1 105 ? 55.104 16.689  48.085  1.00 11.82 ?  105 VAL A N   1 
ATOM   786  C  CA  . VAL A 1 105 ? 54.181 15.764  48.748  1.00 11.58 ?  105 VAL A CA  1 
ATOM   787  C  C   . VAL A 1 105 ? 54.601 15.641  50.204  1.00 11.33 ?  105 VAL A C   1 
ATOM   788  O  O   . VAL A 1 105 ? 55.712 15.185  50.500  1.00 12.77 ?  105 VAL A O   1 
ATOM   789  C  CB  . VAL A 1 105 ? 54.173 14.393  48.062  1.00 12.83 ?  105 VAL A CB  1 
ATOM   790  C  CG1 . VAL A 1 105 ? 53.352 13.383  48.906  1.00 14.50 ?  105 VAL A CG1 1 
ATOM   791  C  CG2 . VAL A 1 105 ? 53.629 14.517  46.633  1.00 12.05 ?  105 VAL A CG2 1 
ATOM   792  N  N   . LEU A 1 106 ? 53.710 16.050  51.109  1.00 10.58 ?  106 LEU A N   1 
ATOM   793  C  CA  . LEU A 1 106 ? 53.869 15.790  52.534  1.00 10.18 ?  106 LEU A CA  1 
ATOM   794  C  C   . LEU A 1 106 ? 53.187 14.458  52.816  1.00 11.26 ?  106 LEU A C   1 
ATOM   795  O  O   . LEU A 1 106 ? 51.963 14.359  52.728  1.00 11.76 ?  106 LEU A O   1 
ATOM   796  C  CB  . LEU A 1 106 ? 53.244 16.908  53.359  1.00 9.38  ?  106 LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 106 ? 53.800 18.306  53.089  1.00 10.20 ?  106 LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 106 ? 52.990 19.354  53.850  1.00 13.74 ?  106 LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 106 ? 55.285 18.410  53.458  1.00 12.04 ?  106 LEU A CD2 1 
ATOM   800  N  N   . TYR A 1 107 ? 53.979 13.431  53.092  1.00 10.43 ?  107 TYR A N   1 
ATOM   801  C  CA  . TYR A 1 107 ? 53.490 12.080  53.351  1.00 9.74  ?  107 TYR A CA  1 
ATOM   802  C  C   . TYR A 1 107 ? 53.525 11.895  54.868  1.00 10.22 ?  107 TYR A C   1 
ATOM   803  O  O   . TYR A 1 107 ? 54.584 11.640  55.455  1.00 10.71 ?  107 TYR A O   1 
ATOM   804  C  CB  . TYR A 1 107 ? 54.365 11.082  52.596  1.00 10.44 ?  107 TYR A CB  1 
ATOM   805  C  CG  . TYR A 1 107 ? 53.726 9.733   52.416  1.00 10.44 ?  107 TYR A CG  1 
ATOM   806  C  CD1 . TYR A 1 107 ? 53.730 8.803   53.453  1.00 9.41  ?  107 TYR A CD1 1 
ATOM   807  C  CD2 . TYR A 1 107 ? 53.126 9.373   51.216  1.00 9.37  ?  107 TYR A CD2 1 
ATOM   808  C  CE1 . TYR A 1 107 ? 53.138 7.548   53.302  1.00 9.98  ?  107 TYR A CE1 1 
ATOM   809  C  CE2 . TYR A 1 107 ? 52.535 8.130   51.044  1.00 11.93 ?  107 TYR A CE2 1 
ATOM   810  C  CZ  . TYR A 1 107 ? 52.547 7.203   52.087  1.00 10.53 ?  107 TYR A CZ  1 
ATOM   811  O  OH  . TYR A 1 107 ? 51.951 5.956   51.928  1.00 11.90 ?  107 TYR A OH  1 
ATOM   812  N  N   . ILE A 1 108 ? 52.374 12.087  55.510  1.00 9.08  ?  108 ILE A N   1 
ATOM   813  C  CA  . ILE A 1 108 ? 52.284 12.184  56.960  1.00 10.55 ?  108 ILE A CA  1 
ATOM   814  C  C   . ILE A 1 108 ? 51.888 10.810  57.480  1.00 11.48 ?  108 ILE A C   1 
ATOM   815  O  O   . ILE A 1 108 ? 50.785 10.337  57.207  1.00 11.12 ?  108 ILE A O   1 
ATOM   816  C  CB  . ILE A 1 108 ? 51.297 13.283  57.382  1.00 10.31 ?  108 ILE A CB  1 
ATOM   817  C  CG1 . ILE A 1 108 ? 51.677 14.605  56.681  1.00 12.51 ?  108 ILE A CG1 1 
ATOM   818  C  CG2 . ILE A 1 108 ? 51.266 13.438  58.914  1.00 11.66 ?  108 ILE A CG2 1 
ATOM   819  C  CD1 . ILE A 1 108 ? 50.815 15.777  57.084  1.00 13.68 ?  108 ILE A CD1 1 
ATOM   820  N  N   . ASP A 1 109 ? 52.796 10.139  58.186  1.00 9.22  ?  109 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 109 ? 52.640 8.714   58.444  1.00 9.09  ?  109 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 109 ? 53.583 8.332   59.573  1.00 10.13 ?  109 ASP A C   1 
ATOM   823  O  O   . ASP A 1 109 ? 54.698 8.853   59.638  1.00 10.13 ?  109 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 109 ? 52.969 7.961   57.141  1.00 8.86  ?  109 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 109 ? 52.439 6.558   57.094  1.00 8.72  ?  109 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 109 ? 52.550 5.793   58.084  1.00 10.03 ?  109 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 109 ? 51.909 6.210   56.021  1.00 10.59 -1 109 ASP A OD2 1 
ATOM   828  N  N   . GLY A 1 110 ? 53.147 7.438   60.463  1.00 9.34  ?  110 GLY A N   1 
ATOM   829  C  CA  . GLY A 1 110 ? 54.085 6.910   61.444  1.00 12.54 ?  110 GLY A CA  1 
ATOM   830  C  C   . GLY A 1 110 ? 55.154 6.020   60.837  1.00 11.32 ?  110 GLY A C   1 
ATOM   831  O  O   . GLY A 1 110 ? 56.200 5.797   61.462  1.00 12.67 ?  110 GLY A O   1 
ATOM   832  N  N   . HIS A 1 111 ? 54.916 5.531   59.616  1.00 10.93 ?  111 HIS A N   1 
ATOM   833  C  CA  . HIS A 1 111 ? 55.840 4.688   58.868  1.00 11.40 ?  111 HIS A CA  1 
ATOM   834  C  C   . HIS A 1 111 ? 56.463 5.454   57.714  1.00 10.63 ?  111 HIS A C   1 
ATOM   835  O  O   . HIS A 1 111 ? 56.019 6.540   57.333  1.00 14.79 ?  111 HIS A O   1 
ATOM   836  C  CB  . HIS A 1 111 ? 55.113 3.467   58.299  1.00 10.87 ?  111 HIS A CB  1 
ATOM   837  C  CG  . HIS A 1 111 ? 54.405 2.654   59.329  1.00 10.57 ?  111 HIS A CG  1 
ATOM   838  N  ND1 . HIS A 1 111 ? 53.097 2.892   59.685  1.00 11.06 ?  111 HIS A ND1 1 
ATOM   839  C  CD2 . HIS A 1 111 ? 54.821 1.603   60.074  1.00 11.33 ?  111 HIS A CD2 1 
ATOM   840  C  CE1 . HIS A 1 111 ? 52.730 2.011   60.603  1.00 13.60 ?  111 HIS A CE1 1 
ATOM   841  N  NE2 . HIS A 1 111 ? 53.754 1.213   60.850  1.00 11.30 ?  111 HIS A NE2 1 
ATOM   842  N  N   . GLY A 1 112 ? 57.483 4.838   57.105  1.00 11.66 ?  112 GLY A N   1 
ATOM   843  C  CA  . GLY A 1 112 ? 58.044 5.407   55.886  1.00 11.96 ?  112 GLY A CA  1 
ATOM   844  C  C   . GLY A 1 112 ? 57.356 4.991   54.590  1.00 11.10 ?  112 GLY A C   1 
ATOM   845  O  O   . GLY A 1 112 ? 57.492 5.675   53.565  1.00 12.39 ?  112 GLY A O   1 
ATOM   846  N  N   . ASP A 1 113 ? 56.615 3.880   54.623  1.00 12.10 ?  113 ASP A N   1 
ATOM   847  C  CA  . ASP A 1 113 ? 55.944 3.311   53.449  1.00 12.39 ?  113 ASP A CA  1 
ATOM   848  C  C   . ASP A 1 113 ? 56.881 3.281   52.234  1.00 13.36 ?  113 ASP A C   1 
ATOM   849  O  O   . ASP A 1 113 ? 56.484 3.560   51.100  1.00 13.79 ?  113 ASP A O   1 
ATOM   850  C  CB  . ASP A 1 113 ? 54.627 4.047   53.151  1.00 12.59 ?  113 ASP A CB  1 
ATOM   851  C  CG  . ASP A 1 113 ? 53.536 3.751   54.189  1.00 13.11 ?  113 ASP A CG  1 
ATOM   852  O  OD1 . ASP A 1 113 ? 53.828 3.022   55.164  1.00 12.90 ?  113 ASP A OD1 1 
ATOM   853  O  OD2 . ASP A 1 113 ? 52.379 4.248   54.015  1.00 11.88 -1 113 ASP A OD2 1 
ATOM   854  N  N   . PHE A 1 114 ? 58.137 2.878   52.473  1.00 12.58 ?  114 PHE A N   1 
ATOM   855  C  CA  . PHE A 1 114 ? 59.188 2.989   51.457  1.00 11.86 ?  114 PHE A CA  1 
ATOM   856  C  C   . PHE A 1 114 ? 59.873 1.653   51.182  1.00 18.44 ?  114 PHE A C   1 
ATOM   857  O  O   . PHE A 1 114 ? 61.018 1.635   50.722  1.00 18.98 ?  114 PHE A O   1 
ATOM   858  C  CB  . PHE A 1 114 ? 60.226 4.054   51.862  1.00 16.53 ?  114 PHE A CB  1 
ATOM   859  C  CG  . PHE A 1 114 ? 60.827 4.822   50.689  1.00 15.71 ?  114 PHE A CG  1 
ATOM   860  C  CD1 . PHE A 1 114 ? 60.061 5.716   49.965  1.00 16.41 ?  114 PHE A CD1 1 
ATOM   861  C  CD2 . PHE A 1 114 ? 62.156 4.646   50.312  1.00 15.96 ?  114 PHE A CD2 1 
ATOM   862  C  CE1 . PHE A 1 114 ? 60.595 6.449   48.885  1.00 18.94 ?  114 PHE A CE1 1 
ATOM   863  C  CE2 . PHE A 1 114 ? 62.690 5.381   49.240  1.00 14.04 ?  114 PHE A CE2 1 
ATOM   864  C  CZ  . PHE A 1 114 ? 61.919 6.262   48.532  1.00 14.93 ?  114 PHE A CZ  1 
ATOM   865  N  N   . ASN A 1 115 ? 59.207 0.537   51.433  1.00 14.67 ?  115 ASN A N   1 
ATOM   866  C  CA  . ASN A 1 115 ? 59.765 -0.759  51.079  1.00 18.39 ?  115 ASN A CA  1 
ATOM   867  C  C   . ASN A 1 115 ? 59.622 -1.052  49.585  1.00 19.56 ?  115 ASN A C   1 
ATOM   868  O  O   . ASN A 1 115 ? 58.764 -0.513  48.884  1.00 18.38 ?  115 ASN A O   1 
ATOM   869  C  CB  . ASN A 1 115 ? 59.081 -1.867  51.876  1.00 20.85 ?  115 ASN A CB  1 
ATOM   870  C  CG  . ASN A 1 115 ? 59.455 -1.835  53.334  1.00 23.54 ?  115 ASN A CG  1 
ATOM   871  O  OD1 . ASN A 1 115 ? 60.599 -2.099  53.695  1.00 28.71 ?  115 ASN A OD1 1 
ATOM   872  N  ND2 . ASN A 1 115 ? 58.504 -1.470  54.181  1.00 24.27 ?  115 ASN A ND2 1 
ATOM   873  N  N   . THR A 1 116 ? 60.485 -1.934  49.107  1.00 19.53 ?  116 THR A N   1 
ATOM   874  C  CA  . THR A 1 116 ? 60.410 -2.486  47.771  1.00 21.29 ?  116 THR A CA  1 
ATOM   875  C  C   . THR A 1 116 ? 60.113 -3.969  47.862  1.00 21.60 ?  116 THR A C   1 
ATOM   876  O  O   . THR A 1 116 ? 60.162 -4.560  48.951  1.00 21.47 ?  116 THR A O   1 
ATOM   877  C  CB  . THR A 1 116 ? 61.735 -2.260  47.024  1.00 22.78 ?  116 THR A CB  1 
ATOM   878  O  OG1 . THR A 1 116 ? 62.782 -2.941  47.722  1.00 26.22 ?  116 THR A OG1 1 
ATOM   879  C  CG2 . THR A 1 116 ? 62.057 -0.781  46.931  1.00 22.59 ?  116 THR A CG2 1 
ATOM   880  N  N   . PRO A 1 117 ? 59.781 -4.618  46.746  1.00 19.44 ?  117 PRO A N   1 
ATOM   881  C  CA  . PRO A 1 117 ? 59.613 -6.075  46.779  1.00 20.27 ?  117 PRO A CA  1 
ATOM   882  C  C   . PRO A 1 117 ? 60.806 -6.794  47.372  1.00 23.43 ?  117 PRO A C   1 
ATOM   883  O  O   . PRO A 1 117 ? 60.637 -7.843  48.009  1.00 24.41 ?  117 PRO A O   1 
ATOM   884  C  CB  . PRO A 1 117 ? 59.411 -6.423  45.301  1.00 24.95 ?  117 PRO A CB  1 
ATOM   885  C  CG  . PRO A 1 117 ? 58.757 -5.219  44.741  1.00 24.53 ?  117 PRO A CG  1 
ATOM   886  C  CD  . PRO A 1 117 ? 59.417 -4.059  45.432  1.00 21.68 ?  117 PRO A CD  1 
ATOM   887  N  N   . GLU A 1 118 ? 62.012 -6.242  47.209  1.00 24.43 ?  118 GLU A N   1 
ATOM   888  C  CA  . GLU A 1 118 ? 63.212 -6.870  47.746  1.00 27.39 ?  118 GLU A CA  1 
ATOM   889  C  C   . GLU A 1 118 ? 63.347 -6.683  49.253  1.00 32.42 ?  118 GLU A C   1 
ATOM   890  O  O   . GLU A 1 118 ? 63.907 -7.555  49.928  1.00 38.89 ?  118 GLU A O   1 
ATOM   891  C  CB  . GLU A 1 118 ? 64.453 -6.316  47.038  1.00 34.77 ?  118 GLU A CB  1 
ATOM   892  C  CG  . GLU A 1 118 ? 64.263 -6.094  45.534  1.00 43.70 ?  118 GLU A CG  1 
ATOM   893  C  CD  . GLU A 1 118 ? 63.909 -4.649  45.178  1.00 52.08 ?  118 GLU A CD  1 
ATOM   894  O  OE1 . GLU A 1 118 ? 62.833 -4.424  44.576  1.00 37.22 ?  118 GLU A OE1 1 
ATOM   895  O  OE2 . GLU A 1 118 ? 64.711 -3.740  45.496  1.00 57.99 -1 118 GLU A OE2 1 
ATOM   896  N  N   . THR A 1 119 ? 62.844 -5.577  49.810  1.00 23.60 ?  119 THR A N   1 
ATOM   897  C  CA  . THR A 1 119 ? 63.108 -5.269  51.206  1.00 23.65 ?  119 THR A CA  1 
ATOM   898  C  C   . THR A 1 119 ? 61.934 -5.522  52.145  1.00 24.25 ?  119 THR A C   1 
ATOM   899  O  O   . THR A 1 119 ? 62.138 -5.539  53.363  1.00 24.65 ?  119 THR A O   1 
ATOM   900  C  CB  . THR A 1 119 ? 63.559 -3.807  51.361  1.00 29.68 ?  119 THR A CB  1 
ATOM   901  O  OG1 . THR A 1 119 ? 62.471 -2.923  51.056  1.00 25.35 ?  119 THR A OG1 1 
ATOM   902  C  CG2 . THR A 1 119 ? 64.729 -3.509  50.427  1.00 32.44 ?  119 THR A CG2 1 
ATOM   903  N  N   . THR A 1 120 ? 60.725 -5.723  51.634  1.00 20.14 ?  120 THR A N   1 
ATOM   904  C  CA  . THR A 1 120 ? 59.593 -5.911  52.536  1.00 17.40 ?  120 THR A CA  1 
ATOM   905  C  C   . THR A 1 120 ? 59.735 -7.203  53.341  1.00 22.12 ?  120 THR A C   1 
ATOM   906  O  O   . THR A 1 120 ? 60.145 -8.245  52.818  1.00 24.21 ?  120 THR A O   1 
ATOM   907  C  CB  . THR A 1 120 ? 58.271 -5.908  51.756  1.00 16.50 ?  120 THR A CB  1 
ATOM   908  O  OG1 . THR A 1 120 ? 57.176 -6.139  52.658  1.00 17.80 ?  120 THR A OG1 1 
ATOM   909  C  CG2 . THR A 1 120 ? 58.254 -6.969  50.655  1.00 20.15 ?  120 THR A CG2 1 
ATOM   910  N  N   . ASP A 1 121 ? 59.420 -7.119  54.636  1.00 19.33 ?  121 ASP A N   1 
ATOM   911  C  CA  . ASP A 1 121 ? 59.395 -8.291  55.506  1.00 19.75 ?  121 ASP A CA  1 
ATOM   912  C  C   . ASP A 1 121 ? 58.029 -8.951  55.576  1.00 23.30 ?  121 ASP A C   1 
ATOM   913  O  O   . ASP A 1 121 ? 57.942 -10.130 55.945  1.00 25.31 ?  121 ASP A O   1 
ATOM   914  C  CB  . ASP A 1 121 ? 59.780 -7.926  56.945  1.00 21.30 ?  121 ASP A CB  1 
ATOM   915  C  CG  . ASP A 1 121 ? 61.232 -7.562  57.105  1.00 27.84 ?  121 ASP A CG  1 
ATOM   916  O  OD1 . ASP A 1 121 ? 62.092 -8.117  56.391  1.00 29.43 ?  121 ASP A OD1 1 
ATOM   917  O  OD2 . ASP A 1 121 ? 61.512 -6.707  57.972  1.00 32.49 -1 121 ASP A OD2 1 
ATOM   918  N  N   . THR A 1 122 ? 56.962 -8.212  55.276  1.00 18.48 ?  122 THR A N   1 
ATOM   919  C  CA  . THR A 1 122 ? 55.599 -8.695  55.445  1.00 19.39 ?  122 THR A CA  1 
ATOM   920  C  C   . THR A 1 122 ? 54.869 -8.897  54.136  1.00 17.21 ?  122 THR A C   1 
ATOM   921  O  O   . THR A 1 122 ? 53.761 -9.454  54.152  1.00 20.95 ?  122 THR A O   1 
ATOM   922  C  CB  . THR A 1 122 ? 54.769 -7.718  56.292  1.00 17.85 ?  122 THR A CB  1 
ATOM   923  O  OG1 . THR A 1 122 ? 54.507 -6.544  55.510  1.00 19.98 ?  122 THR A OG1 1 
ATOM   924  C  CG2 . THR A 1 122 ? 55.503 -7.317  57.572  1.00 19.31 ?  122 THR A CG2 1 
ATOM   925  N  N   . GLY A 1 123 ? 55.426 -8.417  53.020  1.00 18.11 ?  123 GLY A N   1 
ATOM   926  C  CA  . GLY A 1 123 ? 54.757 -8.440  51.734  1.00 18.62 ?  123 GLY A CA  1 
ATOM   927  C  C   . GLY A 1 123 ? 53.605 -7.468  51.580  1.00 19.96 ?  123 GLY A C   1 
ATOM   928  O  O   . GLY A 1 123 ? 52.866 -7.562  50.599  1.00 18.40 ?  123 GLY A O   1 
ATOM   929  N  N   . TYR A 1 124 ? 53.424 -6.533  52.509  1.00 16.96 ?  124 TYR A N   1 
ATOM   930  C  CA  . TYR A 1 124 ? 52.235 -5.678  52.508  1.00 14.39 ?  124 TYR A CA  1 
ATOM   931  C  C   . TYR A 1 124 ? 52.395 -4.497  51.548  1.00 14.53 ?  124 TYR A C   1 
ATOM   932  O  O   . TYR A 1 124 ? 53.339 -3.698  51.669  1.00 15.56 ?  124 TYR A O   1 
ATOM   933  C  CB  . TYR A 1 124 ? 51.945 -5.185  53.930  1.00 14.12 ?  124 TYR A CB  1 
ATOM   934  C  CG  . TYR A 1 124 ? 50.751 -4.268  54.058  1.00 13.73 ?  124 TYR A CG  1 
ATOM   935  C  CD1 . TYR A 1 124 ? 49.549 -4.557  53.419  1.00 15.72 ?  124 TYR A CD1 1 
ATOM   936  C  CD2 . TYR A 1 124 ? 50.830 -3.111  54.817  1.00 16.46 ?  124 TYR A CD2 1 
ATOM   937  C  CE1 . TYR A 1 124 ? 48.452 -3.719  53.539  1.00 15.01 ?  124 TYR A CE1 1 
ATOM   938  C  CE2 . TYR A 1 124 ? 49.749 -2.255  54.930  1.00 18.14 ?  124 TYR A CE2 1 
ATOM   939  C  CZ  . TYR A 1 124 ? 48.564 -2.561  54.292  1.00 20.46 ?  124 TYR A CZ  1 
ATOM   940  O  OH  . TYR A 1 124 ? 47.498 -1.698  54.401  1.00 25.96 ?  124 TYR A OH  1 
ATOM   941  N  N   . LEU A 1 125 ? 51.445 -4.379  50.611  1.00 13.26 ?  125 LEU A N   1 
ATOM   942  C  CA  . LEU A 1 125 ? 51.484 -3.305  49.621  1.00 13.87 ?  125 LEU A CA  1 
ATOM   943  C  C   . LEU A 1 125 ? 51.497 -1.929  50.274  1.00 12.97 ?  125 LEU A C   1 
ATOM   944  O  O   . LEU A 1 125 ? 52.144 -1.002  49.772  1.00 14.82 ?  125 LEU A O   1 
ATOM   945  C  CB  . LEU A 1 125 ? 50.281 -3.432  48.691  1.00 12.42 ?  125 LEU A CB  1 
ATOM   946  C  CG  . LEU A 1 125 ? 50.191 -2.450  47.521  1.00 13.37 ?  125 LEU A CG  1 
ATOM   947  C  CD1 . LEU A 1 125 ? 51.361 -2.679  46.571  1.00 14.63 ?  125 LEU A CD1 1 
ATOM   948  C  CD2 . LEU A 1 125 ? 48.874 -2.634  46.793  1.00 15.74 ?  125 LEU A CD2 1 
ATOM   949  N  N   . GLY A 1 126 ? 50.781 -1.778  51.389  1.00 12.86 ?  126 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 126 ? 50.698 -0.491  52.050  1.00 13.88 ?  126 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 126 ? 52.011 -0.011  52.614  1.00 14.18 ?  126 GLY A C   1 
ATOM   952  O  O   . GLY A 1 126 ? 52.137 1.179   52.916  1.00 21.06 ?  126 GLY A O   1 
ATOM   953  N  N   . GLY A 1 127 ? 52.997 -0.893  52.750  1.00 13.99 ?  127 GLY A N   1 
ATOM   954  C  CA  . GLY A 1 127 ? 54.313 -0.450  53.154  1.00 12.18 ?  127 GLY A CA  1 
ATOM   955  C  C   . GLY A 1 127 ? 55.226 -0.118  52.000  1.00 11.65 ?  127 GLY A C   1 
ATOM   956  O  O   . GLY A 1 127 ? 56.410 0.112   52.236  1.00 13.48 ?  127 GLY A O   1 
ATOM   957  N  N   . MET A 1 128 ? 54.693 -0.081  50.778  1.00 12.73 ?  128 MET A N   1 
ATOM   958  C  CA  . MET A 1 128 ? 55.462 0.091   49.544  1.00 13.02 ?  128 MET A CA  1 
ATOM   959  C  C   . MET A 1 128 ? 54.962 1.275   48.716  1.00 15.26 ?  128 MET A C   1 
ATOM   960  O  O   . MET A 1 128 ? 55.302 1.395   47.533  1.00 13.79 ?  128 MET A O   1 
ATOM   961  C  CB  . MET A 1 128 ? 55.395 -1.199  48.718  1.00 14.53 ?  128 MET A CB  1 
ATOM   962  C  CG  . MET A 1 128 ? 55.772 -2.446  49.512  1.00 15.21 ?  128 MET A CG  1 
ATOM   963  S  SD  . MET A 1 128 ? 55.277 -4.030  48.759  1.00 20.81 ?  128 MET A SD  1 
ATOM   964  C  CE  . MET A 1 128 ? 56.321 -4.004  47.315  1.00 22.31 ?  128 MET A CE  1 
ATOM   965  N  N   . VAL A 1 129 ? 54.169 2.168   49.310  1.00 12.88 ?  129 VAL A N   1 
ATOM   966  C  CA  . VAL A 1 129 ? 53.408 3.146   48.542  1.00 12.55 ?  129 VAL A CA  1 
ATOM   967  C  C   . VAL A 1 129 ? 54.303 4.265   48.037  1.00 14.50 ?  129 VAL A C   1 
ATOM   968  O  O   . VAL A 1 129 ? 54.271 4.624   46.857  1.00 14.11 ?  129 VAL A O   1 
ATOM   969  C  CB  . VAL A 1 129 ? 52.259 3.712   49.403  1.00 12.26 ?  129 VAL A CB  1 
ATOM   970  C  CG1 . VAL A 1 129 ? 51.524 4.839   48.653  1.00 14.93 ?  129 VAL A CG1 1 
ATOM   971  C  CG2 . VAL A 1 129 ? 51.299 2.593   49.814  1.00 17.98 ?  129 VAL A CG2 1 
ATOM   972  N  N   . LEU A 1 130 ? 55.068 4.883   48.934  1.00 12.07 ?  130 LEU A N   1 
ATOM   973  C  CA  . LEU A 1 130 ? 55.836 6.053   48.530  1.00 12.06 ?  130 LEU A CA  1 
ATOM   974  C  C   . LEU A 1 130 ? 56.988 5.644   47.630  1.00 15.05 ?  130 LEU A C   1 
ATOM   975  O  O   . LEU A 1 130 ? 57.310 6.352   46.676  1.00 14.76 ?  130 LEU A O   1 
ATOM   976  C  CB  . LEU A 1 130 ? 56.317 6.805   49.775  1.00 12.58 ?  130 LEU A CB  1 
ATOM   977  C  CG  . LEU A 1 130 ? 57.074 8.124   49.589  1.00 13.36 ?  130 LEU A CG  1 
ATOM   978  C  CD1 . LEU A 1 130 ? 56.239 9.095   48.764  1.00 13.84 ?  130 LEU A CD1 1 
ATOM   979  C  CD2 . LEU A 1 130 ? 57.452 8.738   50.934  1.00 13.31 ?  130 LEU A CD2 1 
ATOM   980  N  N   . SER A 1 131 ? 57.603 4.497   47.911  1.00 13.24 ?  131 SER A N   1 
ATOM   981  C  CA  . SER A 1 131 ? 58.660 3.992   47.039  1.00 14.02 ?  131 SER A CA  1 
ATOM   982  C  C   . SER A 1 131 ? 58.131 3.654   45.651  1.00 15.92 ?  131 SER A C   1 
ATOM   983  O  O   . SER A 1 131 ? 58.837 3.844   44.651  1.00 15.48 ?  131 SER A O   1 
ATOM   984  C  CB  . SER A 1 131 ? 59.295 2.770   47.679  1.00 16.03 ?  131 SER A CB  1 
ATOM   985  O  OG  . SER A 1 131 ? 58.260 1.899   48.084  1.00 16.21 ?  131 SER A OG  1 
ATOM   986  N  N   . GLY A 1 132 ? 56.907 3.140   45.567  1.00 13.41 ?  132 GLY A N   1 
ATOM   987  C  CA  . GLY A 1 132 ? 56.311 2.863   44.270  1.00 13.18 ?  132 GLY A CA  1 
ATOM   988  C  C   . GLY A 1 132 ? 56.044 4.123   43.470  1.00 16.00 ?  132 GLY A C   1 
ATOM   989  O  O   . GLY A 1 132 ? 56.338 4.192   42.270  1.00 18.28 ?  132 GLY A O   1 
ATOM   990  N  N   . ALA A 1 133 ? 55.489 5.147   44.126  1.00 14.46 ?  133 ALA A N   1 
ATOM   991  C  CA  . ALA A 1 133 ? 55.206 6.406   43.442  1.00 15.34 ?  133 ALA A CA  1 
ATOM   992  C  C   . ALA A 1 133 ? 56.485 7.084   42.977  1.00 17.55 ?  133 ALA A C   1 
ATOM   993  O  O   . ALA A 1 133 ? 56.474 7.818   41.978  1.00 16.76 ?  133 ALA A O   1 
ATOM   994  C  CB  . ALA A 1 133 ? 54.420 7.340   44.374  1.00 14.35 ?  133 ALA A CB  1 
ATOM   995  N  N   . CYS A 1 134 ? 57.583 6.865   43.692  1.00 15.96 ?  134 CYS A N   1 
ATOM   996  C  CA  . CYS A 1 134 ? 58.886 7.438   43.366  1.00 16.94 ?  134 CYS A CA  1 
ATOM   997  C  C   . CYS A 1 134 ? 59.689 6.565   42.405  1.00 21.37 ?  134 CYS A C   1 
ATOM   998  O  O   . CYS A 1 134 ? 60.831 6.913   42.085  1.00 23.08 ?  134 CYS A O   1 
ATOM   999  C  CB  . CYS A 1 134 ? 59.692 7.671   44.648  1.00 17.85 ?  134 CYS A CB  1 
ATOM   1000 S  SG  . CYS A 1 134 ? 59.074 9.000   45.717  1.00 18.87 ?  134 CYS A SG  1 
ATOM   1001 N  N   . GLY A 1 135 ? 59.136 5.434   41.970  1.00 19.30 ?  135 GLY A N   1 
ATOM   1002 C  CA  . GLY A 1 135 ? 59.768 4.621   40.942  1.00 18.91 ?  135 GLY A CA  1 
ATOM   1003 C  C   . GLY A 1 135 ? 60.864 3.682   41.395  1.00 22.82 ?  135 GLY A C   1 
ATOM   1004 O  O   . GLY A 1 135 ? 61.609 3.170   40.547  1.00 20.96 ?  135 GLY A O   1 
ATOM   1005 N  N   . LEU A 1 136 ? 61.002 3.431   42.697  1.00 20.14 ?  136 LEU A N   1 
ATOM   1006 C  CA  . LEU A 1 136 ? 61.980 2.449   43.157  1.00 18.38 ?  136 LEU A CA  1 
ATOM   1007 C  C   . LEU A 1 136 ? 61.561 1.030   42.796  1.00 17.81 ?  136 LEU A C   1 
ATOM   1008 O  O   . LEU A 1 136 ? 62.407 0.130   42.747  1.00 20.85 ?  136 LEU A O   1 
ATOM   1009 C  CB  . LEU A 1 136 ? 62.176 2.559   44.670  1.00 21.16 ?  136 LEU A CB  1 
ATOM   1010 C  CG  . LEU A 1 136 ? 63.175 3.612   45.164  1.00 23.44 ?  136 LEU A CG  1 
ATOM   1011 C  CD1 . LEU A 1 136 ? 62.626 5.028   45.025  1.00 23.18 ?  136 LEU A CD1 1 
ATOM   1012 C  CD2 . LEU A 1 136 ? 63.566 3.316   46.603  1.00 25.14 ?  136 LEU A CD2 1 
ATOM   1013 N  N   . TRP A 1 137 ? 60.272 0.816   42.567  1.00 14.48 ?  137 TRP A N   1 
ATOM   1014 C  CA  . TRP A 1 137 ? 59.721 -0.419  42.027  1.00 16.88 ?  137 TRP A CA  1 
ATOM   1015 C  C   . TRP A 1 137 ? 58.485 -0.042  41.222  1.00 18.35 ?  137 TRP A C   1 
ATOM   1016 O  O   . TRP A 1 137 ? 57.964 1.076   41.340  1.00 19.43 ?  137 TRP A O   1 
ATOM   1017 C  CB  . TRP A 1 137 ? 59.389 -1.449  43.127  1.00 16.65 ?  137 TRP A CB  1 
ATOM   1018 C  CG  . TRP A 1 137 ? 58.220 -1.039  44.008  1.00 14.88 ?  137 TRP A CG  1 
ATOM   1019 C  CD1 . TRP A 1 137 ? 58.233 -0.115  45.033  1.00 17.14 ?  137 TRP A CD1 1 
ATOM   1020 C  CD2 . TRP A 1 137 ? 56.884 -1.525  43.918  1.00 14.05 ?  137 TRP A CD2 1 
ATOM   1021 N  NE1 . TRP A 1 137 ? 56.978 -0.014  45.574  1.00 14.99 ?  137 TRP A NE1 1 
ATOM   1022 C  CE2 . TRP A 1 137 ? 56.125 -0.857  44.908  1.00 14.66 ?  137 TRP A CE2 1 
ATOM   1023 C  CE3 . TRP A 1 137 ? 56.243 -2.457  43.091  1.00 16.76 ?  137 TRP A CE3 1 
ATOM   1024 C  CZ2 . TRP A 1 137 ? 54.769 -1.102  45.099  1.00 17.31 ?  137 TRP A CZ2 1 
ATOM   1025 C  CZ3 . TRP A 1 137 ? 54.903 -2.705  43.282  1.00 19.00 ?  137 TRP A CZ3 1 
ATOM   1026 C  CH2 . TRP A 1 137 ? 54.171 -2.034  44.284  1.00 18.06 ?  137 TRP A CH2 1 
ATOM   1027 N  N   . ASP A 1 138 ? 58.024 -0.977  40.389  1.00 19.30 ?  138 ASP A N   1 
ATOM   1028 C  CA  . ASP A 1 138 ? 57.007 -0.699  39.377  1.00 20.30 ?  138 ASP A CA  1 
ATOM   1029 C  C   . ASP A 1 138 ? 55.658 -1.254  39.823  1.00 21.24 ?  138 ASP A C   1 
ATOM   1030 O  O   . ASP A 1 138 ? 55.422 -2.471  39.798  1.00 19.43 ?  138 ASP A O   1 
ATOM   1031 C  CB  . ASP A 1 138 ? 57.423 -1.280  38.022  1.00 21.43 ?  138 ASP A CB  1 
ATOM   1032 C  CG  . ASP A 1 138 ? 56.416 -0.997  36.919  1.00 27.63 ?  138 ASP A CG  1 
ATOM   1033 O  OD1 . ASP A 1 138 ? 55.473 -0.196  37.108  1.00 26.04 ?  138 ASP A OD1 1 
ATOM   1034 O  OD2 . ASP A 1 138 ? 56.577 -1.582  35.826  1.00 35.53 -1 138 ASP A OD2 1 
ATOM   1035 N  N   . SER A 1 139 ? 54.764 -0.351  40.217  1.00 18.93 ?  139 SER A N   1 
ATOM   1036 C  CA  . SER A 1 139 ? 53.442 -0.736  40.678  1.00 18.55 ?  139 SER A CA  1 
ATOM   1037 C  C   . SER A 1 139 ? 52.471 -1.049  39.550  1.00 18.30 ?  139 SER A C   1 
ATOM   1038 O  O   . SER A 1 139 ? 51.383 -1.566  39.820  1.00 20.36 ?  139 SER A O   1 
ATOM   1039 C  CB  . SER A 1 139 ? 52.856 0.394   41.524  1.00 18.66 ?  139 SER A CB  1 
ATOM   1040 O  OG  . SER A 1 139 ? 52.510 1.469   40.669  1.00 18.18 ?  139 SER A OG  1 
ATOM   1041 N  N   . GLY A 1 140 ? 52.820 -0.732  38.302  1.00 20.54 ?  140 GLY A N   1 
ATOM   1042 C  CA  . GLY A 1 140 ? 51.857 -0.811  37.228  1.00 21.41 ?  140 GLY A CA  1 
ATOM   1043 C  C   . GLY A 1 140 ? 50.945 0.389   37.108  1.00 22.58 ?  140 GLY A C   1 
ATOM   1044 O  O   . GLY A 1 140 ? 50.066 0.397   36.235  1.00 24.98 ?  140 GLY A O   1 
ATOM   1045 N  N   . HIS A 1 141 ? 51.110 1.402   37.964  1.00 18.00 ?  141 HIS A N   1 
ATOM   1046 C  CA  . HIS A 1 141 ? 50.270 2.595   37.929  1.00 18.74 ?  141 HIS A CA  1 
ATOM   1047 C  C   . HIS A 1 141 ? 51.107 3.858   37.771  1.00 17.74 ?  141 HIS A C   1 
ATOM   1048 O  O   . HIS A 1 141 ? 50.646 4.963   38.095  1.00 22.81 ?  141 HIS A O   1 
ATOM   1049 C  CB  . HIS A 1 141 ? 49.390 2.644   39.182  1.00 17.80 ?  141 HIS A CB  1 
ATOM   1050 C  CG  . HIS A 1 141 ? 48.382 1.541   39.209  1.00 17.19 ?  141 HIS A CG  1 
ATOM   1051 N  ND1 . HIS A 1 141 ? 47.165 1.627   38.571  1.00 19.03 ?  141 HIS A ND1 1 
ATOM   1052 C  CD2 . HIS A 1 141 ? 48.448 0.291   39.726  1.00 17.71 ?  141 HIS A CD2 1 
ATOM   1053 C  CE1 . HIS A 1 141 ? 46.514 0.486   38.711  1.00 19.52 ?  141 HIS A CE1 1 
ATOM   1054 N  NE2 . HIS A 1 141 ? 47.271 -0.340  39.413  1.00 20.84 ?  141 HIS A NE2 1 
ATOM   1055 N  N   . GLY A 1 142 ? 52.313 3.716   37.255  1.00 20.86 ?  142 GLY A N   1 
ATOM   1056 C  CA  . GLY A 1 142 ? 53.162 4.855   37.002  1.00 23.26 ?  142 GLY A CA  1 
ATOM   1057 C  C   . GLY A 1 142 ? 53.993 5.238   38.204  1.00 19.37 ?  142 GLY A C   1 
ATOM   1058 O  O   . GLY A 1 142 ? 53.881 4.693   39.308  1.00 20.55 ?  142 GLY A O   1 
ATOM   1059 N  N   . ALA A 1 143 ? 54.855 6.215   37.966  1.00 19.10 ?  143 ALA A N   1 
ATOM   1060 C  CA  . ALA A 1 143 ? 55.709 6.763   39.006  1.00 18.67 ?  143 ALA A CA  1 
ATOM   1061 C  C   . ALA A 1 143 ? 55.871 8.249   38.720  1.00 17.16 ?  143 ALA A C   1 
ATOM   1062 O  O   . ALA A 1 143 ? 54.874 8.942   38.504  1.00 24.14 ?  143 ALA A O   1 
ATOM   1063 C  CB  . ALA A 1 143 ? 57.051 6.036   39.050  1.00 19.04 ?  143 ALA A CB  1 
ATOM   1064 N  N   . GLY A 1 144 ? 57.106 8.740   38.679  1.00 17.47 ?  144 GLY A N   1 
ATOM   1065 C  CA  . GLY A 1 144 ? 57.352 10.117  38.313  1.00 18.76 ?  144 GLY A CA  1 
ATOM   1066 C  C   . GLY A 1 144 ? 57.478 11.098  39.463  1.00 16.34 ?  144 GLY A C   1 
ATOM   1067 O  O   . GLY A 1 144 ? 57.905 12.236  39.239  1.00 19.43 ?  144 GLY A O   1 
ATOM   1068 N  N   . LEU A 1 145 ? 57.089 10.720  40.681  1.00 17.36 ?  145 LEU A N   1 
ATOM   1069 C  CA  . LEU A 1 145 ? 57.324 11.595  41.820  1.00 14.97 ?  145 LEU A CA  1 
ATOM   1070 C  C   . LEU A 1 145 ? 58.814 11.599  42.145  1.00 16.10 ?  145 LEU A C   1 
ATOM   1071 O  O   . LEU A 1 145 ? 59.405 10.539  42.370  1.00 17.24 ?  145 LEU A O   1 
ATOM   1072 C  CB  . LEU A 1 145 ? 56.511 11.131  43.029  1.00 13.91 ?  145 LEU A CB  1 
ATOM   1073 C  CG  . LEU A 1 145 ? 56.658 11.983  44.295  1.00 14.27 ?  145 LEU A CG  1 
ATOM   1074 C  CD1 . LEU A 1 145 ? 56.179 13.413  44.094  1.00 17.39 ?  145 LEU A CD1 1 
ATOM   1075 C  CD2 . LEU A 1 145 ? 55.888 11.319  45.450  1.00 14.09 ?  145 LEU A CD2 1 
ATOM   1076 N  N   . ARG A 1 146 ? 59.431 12.772  42.142  1.00 16.26 ?  146 ARG A N   1 
ATOM   1077 C  CA  . ARG A 1 146 ? 60.822 12.865  42.567  1.00 15.51 ?  146 ARG A CA  1 
ATOM   1078 C  C   . ARG A 1 146 ? 60.908 12.606  44.069  1.00 16.34 ?  146 ARG A C   1 
ATOM   1079 O  O   . ARG A 1 146 ? 60.196 13.260  44.841  1.00 15.38 ?  146 ARG A O   1 
ATOM   1080 C  CB  . ARG A 1 146 ? 61.400 14.249  42.265  1.00 16.38 ?  146 ARG A CB  1 
ATOM   1081 C  CG  . ARG A 1 146 ? 61.677 14.529  40.811  1.00 17.46 ?  146 ARG A CG  1 
ATOM   1082 C  CD  . ARG A 1 146 ? 62.288 15.923  40.656  1.00 18.89 ?  146 ARG A CD  1 
ATOM   1083 N  NE  . ARG A 1 146 ? 61.274 16.974  40.727  1.00 18.28 ?  146 ARG A NE  1 
ATOM   1084 C  CZ  . ARG A 1 146 ? 61.537 18.267  40.904  1.00 15.63 ?  146 ARG A CZ  1 
ATOM   1085 N  NH1 . ARG A 1 146 ? 62.793 18.693  41.032  1.00 19.50 ?  146 ARG A NH1 1 
ATOM   1086 N  NH2 . ARG A 1 146 ? 60.535 19.141  40.949  1.00 18.28 ?  146 ARG A NH2 1 
ATOM   1087 N  N   . PRO A 1 147 ? 61.759 11.681  44.527  1.00 14.83 ?  147 PRO A N   1 
ATOM   1088 C  CA  . PRO A 1 147 ? 61.976 11.571  45.981  1.00 16.71 ?  147 PRO A CA  1 
ATOM   1089 C  C   . PRO A 1 147 ? 62.398 12.893  46.600  1.00 16.74 ?  147 PRO A C   1 
ATOM   1090 O  O   . PRO A 1 147 ? 62.073 13.184  47.755  1.00 14.41 ?  147 PRO A O   1 
ATOM   1091 C  CB  . PRO A 1 147 ? 63.077 10.505  46.109  1.00 14.27 ?  147 PRO A CB  1 
ATOM   1092 C  CG  . PRO A 1 147 ? 63.088 9.767   44.800  1.00 22.91 ?  147 PRO A CG  1 
ATOM   1093 C  CD  . PRO A 1 147 ? 62.519 10.678  43.751  1.00 16.21 ?  147 PRO A CD  1 
ATOM   1094 N  N   . GLU A 1 148 ? 63.098 13.733  45.837  1.00 15.30 ?  148 GLU A N   1 
ATOM   1095 C  CA  . GLU A 1 148 ? 63.502 15.041  46.324  1.00 16.34 ?  148 GLU A CA  1 
ATOM   1096 C  C   . GLU A 1 148 ? 62.321 15.956  46.610  1.00 13.33 ?  148 GLU A C   1 
ATOM   1097 O  O   . GLU A 1 148 ? 62.496 16.977  47.286  1.00 16.80 ?  148 GLU A O   1 
ATOM   1098 C  CB  . GLU A 1 148 ? 64.422 15.683  45.280  1.00 19.06 ?  148 GLU A CB  1 
ATOM   1099 C  CG  . GLU A 1 148 ? 65.717 14.900  45.040  1.00 21.37 ?  148 GLU A CG  1 
ATOM   1100 C  CD  . GLU A 1 148 ? 65.649 13.828  43.943  1.00 22.58 ?  148 GLU A CD  1 
ATOM   1101 O  OE1 . GLU A 1 148 ? 64.571 13.512  43.410  1.00 17.41 ?  148 GLU A OE1 1 
ATOM   1102 O  OE2 . GLU A 1 148 ? 66.725 13.292  43.591  1.00 22.30 -1 148 GLU A OE2 1 
ATOM   1103 N  N   . GLN A 1 149 ? 61.141 15.629  46.085  1.00 13.32 ?  149 GLN A N   1 
ATOM   1104 C  CA  . GLN A 1 149 ? 59.928 16.397  46.316  1.00 13.90 ?  149 GLN A CA  1 
ATOM   1105 C  C   . GLN A 1 149 ? 59.031 15.751  47.355  1.00 14.21 ?  149 GLN A C   1 
ATOM   1106 O  O   . GLN A 1 149 ? 57.931 16.245  47.585  1.00 14.90 ?  149 GLN A O   1 
ATOM   1107 C  CB  . GLN A 1 149 ? 59.152 16.571  45.007  1.00 12.31 ?  149 GLN A CB  1 
ATOM   1108 C  CG  . GLN A 1 149 ? 59.902 17.404  43.953  1.00 15.62 ?  149 GLN A CG  1 
ATOM   1109 C  CD  . GLN A 1 149 ? 60.125 18.826  44.360  1.00 18.61 ?  149 GLN A CD  1 
ATOM   1110 O  OE1 . GLN A 1 149 ? 61.262 19.272  44.491  1.00 21.64 ?  149 GLN A OE1 1 
ATOM   1111 N  NE2 . GLN A 1 149 ? 59.041 19.565  44.566  1.00 19.47 ?  149 GLN A NE2 1 
ATOM   1112 N  N   . ALA A 1 150 ? 59.479 14.671  47.989  1.00 13.00 ?  150 ALA A N   1 
ATOM   1113 C  CA  . ALA A 1 150 ? 58.682 13.956  48.989  1.00 13.14 ?  150 ALA A CA  1 
ATOM   1114 C  C   . ALA A 1 150 ? 59.249 14.198  50.381  1.00 15.29 ?  150 ALA A C   1 
ATOM   1115 O  O   . ALA A 1 150 ? 60.462 14.140  50.590  1.00 13.45 ?  150 ALA A O   1 
ATOM   1116 C  CB  . ALA A 1 150 ? 58.650 12.453  48.677  1.00 14.25 ?  150 ALA A CB  1 
ATOM   1117 N  N   . VAL A 1 151 ? 58.374 14.467  51.346  1.00 12.87 ?  151 VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 151 ? 58.788 14.726  52.728  1.00 12.36 ?  151 VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 151 ? 57.948 13.843  53.645  1.00 11.14 ?  151 VAL A C   1 
ATOM   1120 O  O   . VAL A 1 151 ? 56.718 14.003  53.710  1.00 11.63 ?  151 VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 151 ? 58.629 16.201  53.112  1.00 10.63 ?  151 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 151 ? 59.137 16.430  54.506  1.00 14.16 ?  151 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 151 ? 59.388 17.096  52.109  1.00 12.32 ?  151 VAL A CG2 1 
ATOM   1124 N  N   . LEU A 1 152 ? 58.602 12.900  54.328  1.00 8.98  ?  152 LEU A N   1 
ATOM   1125 C  CA  . LEU A 1 152 ? 57.922 12.108  55.350  1.00 11.05 ?  152 LEU A CA  1 
ATOM   1126 C  C   . LEU A 1 152 ? 57.786 12.946  56.607  1.00 12.26 ?  152 LEU A C   1 
ATOM   1127 O  O   . LEU A 1 152 ? 58.763 13.523  57.086  1.00 13.29 ?  152 LEU A O   1 
ATOM   1128 C  CB  . LEU A 1 152 ? 58.701 10.835  55.632  1.00 10.36 ?  152 LEU A CB  1 
ATOM   1129 C  CG  . LEU A 1 152 ? 58.536 9.722   54.602  1.00 10.27 ?  152 LEU A CG  1 
ATOM   1130 C  CD1 . LEU A 1 152 ? 59.622 8.664   54.726  1.00 12.26 ?  152 LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A 1 152 ? 57.122 9.082   54.700  1.00 11.93 ?  152 LEU A CD2 1 
ATOM   1132 N  N   . VAL A 1 153 ? 56.577 13.026  57.149  1.00 9.90  ?  153 VAL A N   1 
ATOM   1133 C  CA  . VAL A 1 153 ? 56.302 13.856  58.316  1.00 10.26 ?  153 VAL A CA  1 
ATOM   1134 C  C   . VAL A 1 153 ? 55.706 12.955  59.393  1.00 10.94 ?  153 VAL A C   1 
ATOM   1135 O  O   . VAL A 1 153 ? 54.674 12.311  59.172  1.00 10.72 ?  153 VAL A O   1 
ATOM   1136 C  CB  . VAL A 1 153 ? 55.360 15.021  57.969  1.00 9.19  ?  153 VAL A CB  1 
ATOM   1137 C  CG1 . VAL A 1 153 ? 55.105 15.878  59.196  1.00 12.16 ?  153 VAL A CG1 1 
ATOM   1138 C  CG2 . VAL A 1 153 ? 55.940 15.853  56.806  1.00 12.18 ?  153 VAL A CG2 1 
ATOM   1139 N  N   . GLY A 1 154 ? 56.338 12.930  60.570  1.00 10.84 ?  154 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 154 ? 55.826 12.136  61.675  1.00 11.74 ?  154 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 154 ? 56.338 10.720  61.748  1.00 9.43  ?  154 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 154 ? 56.002 10.008  62.706  1.00 11.80 ?  154 GLY A O   1 
ATOM   1143 N  N   . SER A 1 155 ? 57.152 10.290  60.777  1.00 11.47 ?  155 SER A N   1 
ATOM   1144 C  CA  . SER A 1 155 ? 57.650 8.924   60.738  1.00 10.33 ?  155 SER A CA  1 
ATOM   1145 C  C   . SER A 1 155 ? 58.684 8.705   61.836  1.00 13.74 ?  155 SER A C   1 
ATOM   1146 O  O   . SER A 1 155 ? 59.456 9.609   62.166  1.00 14.76 ?  155 SER A O   1 
ATOM   1147 C  CB  . SER A 1 155 ? 58.275 8.647   59.373  1.00 12.79 ?  155 SER A CB  1 
ATOM   1148 O  OG  . SER A 1 155 ? 57.404 9.066   58.341  1.00 13.62 ?  155 SER A OG  1 
ATOM   1149 N  N   . ARG A 1 156 ? 58.695 7.495   62.397  1.00 11.88 ?  156 ARG A N   1 
ATOM   1150 C  CA  . ARG A 1 156 ? 59.590 7.196   63.510  1.00 14.24 ?  156 ARG A CA  1 
ATOM   1151 C  C   . ARG A 1 156 ? 59.783 5.694   63.563  1.00 15.16 ?  156 ARG A C   1 
ATOM   1152 O  O   . ARG A 1 156 ? 59.002 4.933   62.984  1.00 13.71 ?  156 ARG A O   1 
ATOM   1153 C  CB  . ARG A 1 156 ? 59.051 7.711   64.853  1.00 17.24 ?  156 ARG A CB  1 
ATOM   1154 C  CG  . ARG A 1 156 ? 57.805 6.977   65.342  1.00 21.75 ?  156 ARG A CG  1 
ATOM   1155 C  CD  . ARG A 1 156 ? 56.625 7.920   65.355  1.00 20.89 ?  156 ARG A CD  1 
ATOM   1156 N  NE  . ARG A 1 156 ? 55.372 7.359   65.858  1.00 17.07 ?  156 ARG A NE  1 
ATOM   1157 C  CZ  . ARG A 1 156 ? 54.183 7.814   65.487  1.00 17.32 ?  156 ARG A CZ  1 
ATOM   1158 N  NH1 . ARG A 1 156 ? 54.108 8.839   64.611  1.00 11.98 ?  156 ARG A NH1 1 
ATOM   1159 N  NH2 . ARG A 1 156 ? 53.072 7.265   66.005  1.00 19.76 ?  156 ARG A NH2 1 
ATOM   1160 N  N   . ASP A 1 157 ? 60.837 5.279   64.262  1.00 17.10 ?  157 ASP A N   1 
ATOM   1161 C  CA  . ASP A 1 157 ? 61.123 3.860   64.456  1.00 14.41 ?  157 ASP A CA  1 
ATOM   1162 C  C   . ASP A 1 157 ? 61.112 3.106   63.123  1.00 16.82 ?  157 ASP A C   1 
ATOM   1163 O  O   . ASP A 1 157 ? 60.432 2.090   62.943  1.00 19.76 ?  157 ASP A O   1 
ATOM   1164 C  CB  . ASP A 1 157 ? 60.137 3.244   65.454  1.00 14.67 ?  157 ASP A CB  1 
ATOM   1165 C  CG  . ASP A 1 157 ? 60.286 3.794   66.857  1.00 20.92 ?  157 ASP A CG  1 
ATOM   1166 O  OD1 . ASP A 1 157 ? 61.366 4.291   67.226  1.00 21.67 ?  157 ASP A OD1 1 
ATOM   1167 O  OD2 . ASP A 1 157 ? 59.311 3.683   67.627  1.00 27.90 -1 157 ASP A OD2 1 
ATOM   1168 N  N   . ILE A 1 158 ? 61.867 3.633   62.158  1.00 16.59 ?  158 ILE A N   1 
ATOM   1169 C  CA  . ILE A 1 158 ? 61.960 3.049   60.827  1.00 14.25 ?  158 ILE A CA  1 
ATOM   1170 C  C   . ILE A 1 158 ? 63.079 2.017   60.832  1.00 22.09 ?  158 ILE A C   1 
ATOM   1171 O  O   . ILE A 1 158 ? 64.160 2.267   61.380  1.00 24.09 ?  158 ILE A O   1 
ATOM   1172 C  CB  . ILE A 1 158 ? 62.218 4.137   59.765  1.00 17.37 ?  158 ILE A CB  1 
ATOM   1173 C  CG1 . ILE A 1 158 ? 61.129 5.220   59.827  1.00 18.59 ?  158 ILE A CG1 1 
ATOM   1174 C  CG2 . ILE A 1 158 ? 62.212 3.543   58.382  1.00 17.48 ?  158 ILE A CG2 1 
ATOM   1175 C  CD1 . ILE A 1 158 ? 61.330 6.347   58.784  1.00 20.55 ?  158 ILE A CD1 1 
ATOM   1176 N  N   . ASP A 1 159 ? 62.802 0.850   60.254  1.00 21.30 ?  159 ASP A N   1 
ATOM   1177 C  CA  . ASP A 1 159 ? 63.811 -0.189  60.099  1.00 28.01 ?  159 ASP A CA  1 
ATOM   1178 C  C   . ASP A 1 159 ? 65.055 0.385   59.433  1.00 31.82 ?  159 ASP A C   1 
ATOM   1179 O  O   . ASP A 1 159 ? 64.970 1.254   58.561  1.00 24.21 ?  159 ASP A O   1 
ATOM   1180 C  CB  . ASP A 1 159 ? 63.230 -1.345  59.277  1.00 33.79 ?  159 ASP A CB  1 
ATOM   1181 C  CG  . ASP A 1 159 ? 64.281 -2.323  58.812  1.00 46.64 ?  159 ASP A CG  1 
ATOM   1182 O  OD1 . ASP A 1 159 ? 64.864 -2.095  57.731  1.00 42.09 -1 159 ASP A OD1 1 
ATOM   1183 O  OD2 . ASP A 1 159 ? 64.518 -3.323  59.525  1.00 48.73 -1 159 ASP A OD2 1 
ATOM   1184 N  N   . GLU A 1 160 ? 66.224 -0.087  59.864  1.00 29.49 ?  160 GLU A N   1 
ATOM   1185 C  CA  . GLU A 1 160 ? 67.457 0.554   59.423  1.00 34.34 ?  160 GLU A CA  1 
ATOM   1186 C  C   . GLU A 1 160 ? 67.684 0.354   57.930  1.00 30.33 ?  160 GLU A C   1 
ATOM   1187 O  O   . GLU A 1 160 ? 68.188 1.260   57.256  1.00 29.91 ?  160 GLU A O   1 
ATOM   1188 C  CB  . GLU A 1 160 ? 68.638 0.039   60.247  1.00 40.73 ?  160 GLU A CB  1 
ATOM   1189 C  CG  . GLU A 1 160 ? 68.627 0.527   61.703  1.00 51.66 ?  160 GLU A CG  1 
ATOM   1190 C  CD  . GLU A 1 160 ? 67.351 0.150   62.453  1.00 59.29 ?  160 GLU A CD  1 
ATOM   1191 O  OE1 . GLU A 1 160 ? 66.635 1.064   62.923  1.00 64.21 ?  160 GLU A OE1 1 
ATOM   1192 O  OE2 . GLU A 1 160 ? 67.054 -1.062  62.551  1.00 58.42 -1 160 GLU A OE2 1 
ATOM   1193 N  N   . GLY A 1 161 ? 67.284 -0.799  57.390  1.00 28.43 ?  161 GLY A N   1 
ATOM   1194 C  CA  . GLY A 1 161 ? 67.354 -0.986  55.948  1.00 32.21 ?  161 GLY A CA  1 
ATOM   1195 C  C   . GLY A 1 161 ? 66.488 0.002   55.187  1.00 31.48 ?  161 GLY A C   1 
ATOM   1196 O  O   . GLY A 1 161 ? 66.944 0.643   54.235  1.00 28.96 ?  161 GLY A O   1 
ATOM   1197 N  N   . GLU A 1 162 ? 65.224 0.152   55.609  1.00 23.27 ?  162 GLU A N   1 
ATOM   1198 C  CA  . GLU A 1 162 ? 64.315 1.062   54.922  1.00 21.51 ?  162 GLU A CA  1 
ATOM   1199 C  C   . GLU A 1 162 ? 64.762 2.511   55.071  1.00 19.78 ?  162 GLU A C   1 
ATOM   1200 O  O   . GLU A 1 162 ? 64.644 3.304   54.125  1.00 18.14 ?  162 GLU A O   1 
ATOM   1201 C  CB  . GLU A 1 162 ? 62.897 0.877   55.466  1.00 23.89 ?  162 GLU A CB  1 
ATOM   1202 C  CG  . GLU A 1 162 ? 61.829 1.695   54.762  1.00 21.20 ?  162 GLU A CG  1 
ATOM   1203 C  CD  . GLU A 1 162 ? 60.448 1.456   55.338  1.00 25.51 ?  162 GLU A CD  1 
ATOM   1204 O  OE1 . GLU A 1 162 ? 60.325 0.566   56.203  1.00 27.83 ?  162 GLU A OE1 1 
ATOM   1205 O  OE2 . GLU A 1 162 ? 59.493 2.155   54.934  1.00 19.29 -1 162 GLU A OE2 1 
ATOM   1206 N  N   . ARG A 1 163 ? 65.269 2.876   56.255  1.00 20.86 ?  163 ARG A N   1 
ATOM   1207 C  CA  . ARG A 1 163 ? 65.742 4.237   56.486  1.00 20.64 ?  163 ARG A CA  1 
ATOM   1208 C  C   . ARG A 1 163 ? 66.865 4.613   55.526  1.00 21.84 ?  163 ARG A C   1 
ATOM   1209 O  O   . ARG A 1 163 ? 66.961 5.775   55.117  1.00 23.73 ?  163 ARG A O   1 
ATOM   1210 C  CB  . ARG A 1 163 ? 66.212 4.406   57.937  1.00 22.17 ?  163 ARG A CB  1 
ATOM   1211 C  CG  . ARG A 1 163 ? 66.539 5.851   58.314  1.00 27.01 ?  163 ARG A CG  1 
ATOM   1212 C  CD  . ARG A 1 163 ? 65.285 6.717   58.372  1.00 30.08 ?  163 ARG A CD  1 
ATOM   1213 N  NE  . ARG A 1 163 ? 65.576 8.127   58.636  1.00 30.61 ?  163 ARG A NE  1 
ATOM   1214 C  CZ  . ARG A 1 163 ? 66.026 8.984   57.724  1.00 32.77 ?  163 ARG A CZ  1 
ATOM   1215 N  NH1 . ARG A 1 163 ? 66.246 8.577   56.481  1.00 27.96 ?  163 ARG A NH1 1 
ATOM   1216 N  NH2 . ARG A 1 163 ? 66.258 10.250  58.052  1.00 37.14 ?  163 ARG A NH2 1 
ATOM   1217 N  N   . GLU A 1 164 ? 67.703 3.652   55.134  1.00 25.61 ?  164 GLU A N   1 
ATOM   1218 C  CA  . GLU A 1 164 ? 68.782 3.997   54.215  1.00 27.31 ?  164 GLU A CA  1 
ATOM   1219 C  C   . GLU A 1 164 ? 68.312 4.049   52.766  1.00 26.12 ?  164 GLU A C   1 
ATOM   1220 O  O   . GLU A 1 164 ? 68.848 4.846   51.989  1.00 26.85 ?  164 GLU A O   1 
ATOM   1221 C  CB  . GLU A 1 164 ? 69.956 3.032   54.381  1.00 36.17 ?  164 GLU A CB  1 
ATOM   1222 C  CG  . GLU A 1 164 ? 71.163 3.682   55.066  1.00 45.35 ?  164 GLU A CG  1 
ATOM   1223 C  CD  . GLU A 1 164 ? 71.889 4.672   54.163  1.00 50.33 ?  164 GLU A CD  1 
ATOM   1224 O  OE1 . GLU A 1 164 ? 72.235 4.301   53.020  1.00 48.75 ?  164 GLU A OE1 1 
ATOM   1225 O  OE2 . GLU A 1 164 ? 72.109 5.825   54.596  1.00 49.73 -1 164 GLU A OE2 1 
ATOM   1226 N  N   . LEU A 1 165 ? 67.334 3.224   52.373  1.00 21.43 ?  165 LEU A N   1 
ATOM   1227 C  CA  . LEU A 1 165 ? 66.652 3.444   51.099  1.00 18.70 ?  165 LEU A CA  1 
ATOM   1228 C  C   . LEU A 1 165 ? 66.117 4.871   51.017  1.00 17.31 ?  165 LEU A C   1 
ATOM   1229 O  O   . LEU A 1 165 ? 66.296 5.573   50.011  1.00 17.69 ?  165 LEU A O   1 
ATOM   1230 C  CB  . LEU A 1 165 ? 65.512 2.439   50.941  1.00 26.27 ?  165 LEU A CB  1 
ATOM   1231 C  CG  . LEU A 1 165 ? 65.337 1.689   49.622  1.00 30.56 ?  165 LEU A CG  1 
ATOM   1232 C  CD1 . LEU A 1 165 ? 66.669 1.085   49.159  1.00 30.49 ?  165 LEU A CD1 1 
ATOM   1233 C  CD2 . LEU A 1 165 ? 64.261 0.614   49.744  1.00 28.45 ?  165 LEU A CD2 1 
ATOM   1234 N  N   . ILE A 1 166 ? 65.451 5.314   52.093  1.00 16.28 ?  166 ILE A N   1 
ATOM   1235 C  CA  . ILE A 1 166 ? 64.913 6.664   52.167  1.00 18.66 ?  166 ILE A CA  1 
ATOM   1236 C  C   . ILE A 1 166 ? 66.024 7.685   52.000  1.00 19.36 ?  166 ILE A C   1 
ATOM   1237 O  O   . ILE A 1 166 ? 65.912 8.621   51.202  1.00 16.10 ?  166 ILE A O   1 
ATOM   1238 C  CB  . ILE A 1 166 ? 64.166 6.845   53.500  1.00 15.06 ?  166 ILE A CB  1 
ATOM   1239 C  CG1 . ILE A 1 166 ? 62.876 6.028   53.483  1.00 14.43 ?  166 ILE A CG1 1 
ATOM   1240 C  CG2 . ILE A 1 166 ? 63.882 8.316   53.802  1.00 18.75 ?  166 ILE A CG2 1 
ATOM   1241 C  CD1 . ILE A 1 166 ? 62.242 5.910   54.843  1.00 14.19 ?  166 ILE A CD1 1 
ATOM   1242 N  N   . ARG A 1 167 ? 67.112 7.513   52.758  1.00 18.84 ?  167 ARG A N   1 
ATOM   1243 C  CA  . ARG A 1 167 ? 68.222 8.462   52.701  1.00 22.68 ?  167 ARG A CA  1 
ATOM   1244 C  C   . ARG A 1 167 ? 68.870 8.488   51.320  1.00 19.84 ?  167 ARG A C   1 
ATOM   1245 O  O   . ARG A 1 167 ? 69.155 9.567   50.783  1.00 23.20 ?  167 ARG A O   1 
ATOM   1246 C  CB  . ARG A 1 167 ? 69.253 8.118   53.778  1.00 31.84 ?  167 ARG A CB  1 
ATOM   1247 C  CG  . ARG A 1 167 ? 69.734 9.325   54.565  1.00 41.55 ?  167 ARG A CG  1 
ATOM   1248 C  CD  . ARG A 1 167 ? 70.943 8.987   55.428  1.00 44.96 ?  167 ARG A CD  1 
ATOM   1249 N  NE  . ARG A 1 167 ? 70.787 7.728   56.159  1.00 46.18 ?  167 ARG A NE  1 
ATOM   1250 C  CZ  . ARG A 1 167 ? 70.197 7.617   57.346  1.00 44.31 ?  167 ARG A CZ  1 
ATOM   1251 N  NH1 . ARG A 1 167 ? 69.691 8.688   57.944  1.00 42.45 ?  167 ARG A NH1 1 
ATOM   1252 N  NH2 . ARG A 1 167 ? 70.114 6.433   57.938  1.00 45.85 ?  167 ARG A NH2 1 
ATOM   1253 N  N   . LYS A 1 168 ? 69.102 7.313   50.722  1.00 22.77 ?  168 LYS A N   1 
ATOM   1254 C  CA  . LYS A 1 168 ? 69.774 7.268   49.422  1.00 21.84 ?  168 LYS A CA  1 
ATOM   1255 C  C   . LYS A 1 168 ? 68.925 7.910   48.330  1.00 22.31 ?  168 LYS A C   1 
ATOM   1256 O  O   . LYS A 1 168 ? 69.458 8.562   47.422  1.00 22.95 ?  168 LYS A O   1 
ATOM   1257 C  CB  . LYS A 1 168 ? 70.117 5.823   49.050  1.00 26.41 ?  168 LYS A CB  1 
ATOM   1258 C  CG  . LYS A 1 168 ? 70.919 5.680   47.756  1.00 39.89 ?  168 LYS A CG  1 
ATOM   1259 C  CD  . LYS A 1 168 ? 72.162 6.574   47.749  1.00 46.69 ?  168 LYS A CD  1 
ATOM   1260 C  CE  . LYS A 1 168 ? 72.942 6.466   46.436  1.00 45.16 ?  168 LYS A CE  1 
ATOM   1261 N  NZ  . LYS A 1 168 ? 73.923 5.340   46.463  1.00 44.78 ?  168 LYS A NZ  1 
ATOM   1262 N  N   . ALA A 1 169 ? 67.604 7.732   48.396  1.00 19.64 ?  169 ALA A N   1 
ATOM   1263 C  CA  . ALA A 1 169 ? 66.693 8.328   47.427  1.00 18.06 ?  169 ALA A CA  1 
ATOM   1264 C  C   . ALA A 1 169 ? 66.577 9.844   47.576  1.00 15.25 ?  169 ALA A C   1 
ATOM   1265 O  O   . ALA A 1 169 ? 66.181 10.515  46.619  1.00 19.87 ?  169 ALA A O   1 
ATOM   1266 C  CB  . ALA A 1 169 ? 65.298 7.695   47.573  1.00 17.83 ?  169 ALA A CB  1 
ATOM   1267 N  N   . GLY A 1 170 ? 66.905 10.406  48.734  1.00 16.87 ?  170 GLY A N   1 
ATOM   1268 C  CA  . GLY A 1 170 ? 66.741 11.833  48.927  1.00 17.44 ?  170 GLY A CA  1 
ATOM   1269 C  C   . GLY A 1 170 ? 65.423 12.256  49.532  1.00 16.53 ?  170 GLY A C   1 
ATOM   1270 O  O   . GLY A 1 170 ? 65.076 13.436  49.449  1.00 16.04 ?  170 GLY A O   1 
ATOM   1271 N  N   . VAL A 1 171 ? 64.690 11.333  50.151  1.00 15.89 ?  171 VAL A N   1 
ATOM   1272 C  CA  . VAL A 1 171 ? 63.449 11.674  50.850  1.00 15.32 ?  171 VAL A CA  1 
ATOM   1273 C  C   . VAL A 1 171 ? 63.788 12.259  52.213  1.00 15.42 ?  171 VAL A C   1 
ATOM   1274 O  O   . VAL A 1 171 ? 64.492 11.632  53.009  1.00 21.04 ?  171 VAL A O   1 
ATOM   1275 C  CB  . VAL A 1 171 ? 62.556 10.435  50.997  1.00 12.36 ?  171 VAL A CB  1 
ATOM   1276 C  CG1 . VAL A 1 171 ? 61.290 10.786  51.817  1.00 13.84 ?  171 VAL A CG1 1 
ATOM   1277 C  CG2 . VAL A 1 171 ? 62.182 9.852   49.640  1.00 13.94 ?  171 VAL A CG2 1 
ATOM   1278 N  N   . ARG A 1 172 ? 63.246 13.439  52.504  1.00 13.51 ?  172 ARG A N   1 
ATOM   1279 C  CA  . ARG A 1 172 ? 63.469 14.072  53.794  1.00 13.47 ?  172 ARG A CA  1 
ATOM   1280 C  C   . ARG A 1 172 ? 62.504 13.480  54.825  1.00 13.75 ?  172 ARG A C   1 
ATOM   1281 O  O   . ARG A 1 172 ? 61.400 13.048  54.484  1.00 13.60 ?  172 ARG A O   1 
ATOM   1282 C  CB  . ARG A 1 172 ? 63.285 15.587  53.684  1.00 15.99 ?  172 ARG A CB  1 
ATOM   1283 C  CG  . ARG A 1 172 ? 64.417 16.284  52.906  1.00 16.17 ?  172 ARG A CG  1 
ATOM   1284 C  CD  . ARG A 1 172 ? 63.985 17.677  52.476  1.00 18.12 ?  172 ARG A CD  1 
ATOM   1285 N  NE  . ARG A 1 172 ? 63.138 17.629  51.290  1.00 17.87 ?  172 ARG A NE  1 
ATOM   1286 C  CZ  . ARG A 1 172 ? 62.440 18.665  50.834  1.00 14.46 ?  172 ARG A CZ  1 
ATOM   1287 N  NH1 . ARG A 1 172 ? 62.477 19.818  51.481  1.00 20.16 ?  172 ARG A NH1 1 
ATOM   1288 N  NH2 . ARG A 1 172 ? 61.697 18.549  49.755  1.00 15.43 ?  172 ARG A NH2 1 
ATOM   1289 N  N   . VAL A 1 173 ? 62.948 13.421  56.078  1.00 13.03 ?  173 VAL A N   1 
ATOM   1290 C  CA  . VAL A 1 173 ? 62.144 12.914  57.193  1.00 14.11 ?  173 VAL A CA  1 
ATOM   1291 C  C   . VAL A 1 173 ? 62.107 13.985  58.276  1.00 15.05 ?  173 VAL A C   1 
ATOM   1292 O  O   . VAL A 1 173 ? 63.162 14.446  58.743  1.00 16.36 ?  173 VAL A O   1 
ATOM   1293 C  CB  . VAL A 1 173 ? 62.698 11.591  57.748  1.00 14.83 ?  173 VAL A CB  1 
ATOM   1294 C  CG1 . VAL A 1 173 ? 61.818 11.097  58.903  1.00 16.02 ?  173 VAL A CG1 1 
ATOM   1295 C  CG2 . VAL A 1 173 ? 62.766 10.525  56.651  1.00 15.36 ?  173 VAL A CG2 1 
ATOM   1296 N  N   . ILE A 1 174 ? 60.896 14.369  58.683  1.00 13.00 ?  174 ILE A N   1 
ATOM   1297 C  CA  . ILE A 1 174 ? 60.679 15.275  59.808  1.00 12.87 ?  174 ILE A CA  1 
ATOM   1298 C  C   . ILE A 1 174 ? 59.959 14.494  60.909  1.00 14.12 ?  174 ILE A C   1 
ATOM   1299 O  O   . ILE A 1 174 ? 58.735 14.304  60.828  1.00 13.38 ?  174 ILE A O   1 
ATOM   1300 C  CB  . ILE A 1 174 ? 59.870 16.507  59.381  1.00 13.85 ?  174 ILE A CB  1 
ATOM   1301 C  CG1 . ILE A 1 174 ? 60.512 17.216  58.191  1.00 14.66 ?  174 ILE A CG1 1 
ATOM   1302 C  CG2 . ILE A 1 174 ? 59.699 17.474  60.558  1.00 15.02 ?  174 ILE A CG2 1 
ATOM   1303 C  CD1 . ILE A 1 174 ? 59.694 18.403  57.678  1.00 17.37 ?  174 ILE A CD1 1 
ATOM   1304 N  N   . PRO A 1 175 ? 60.650 14.036  61.950  1.00 13.63 ?  175 PRO A N   1 
ATOM   1305 C  CA  . PRO A 1 175 ? 59.987 13.220  62.994  1.00 13.51 ?  175 PRO A CA  1 
ATOM   1306 C  C   . PRO A 1 175 ? 59.033 14.052  63.837  1.00 15.34 ?  175 PRO A C   1 
ATOM   1307 O  O   . PRO A 1 175 ? 59.061 15.287  63.769  1.00 14.16 ?  175 PRO A O   1 
ATOM   1308 C  CB  . PRO A 1 175 ? 61.165 12.687  63.824  1.00 17.63 ?  175 PRO A CB  1 
ATOM   1309 C  CG  . PRO A 1 175 ? 62.267 13.684  63.592  1.00 19.94 ?  175 PRO A CG  1 
ATOM   1310 C  CD  . PRO A 1 175 ? 62.094 14.211  62.195  1.00 17.01 ?  175 PRO A CD  1 
ATOM   1311 N  N   . PRO A 1 176 ? 58.163 13.413  64.641  1.00 13.99 ?  176 PRO A N   1 
ATOM   1312 C  CA  . PRO A 1 176 ? 57.096 14.179  65.325  1.00 12.11 ?  176 PRO A CA  1 
ATOM   1313 C  C   . PRO A 1 176 ? 57.593 15.347  66.163  1.00 15.01 ?  176 PRO A C   1 
ATOM   1314 O  O   . PRO A 1 176 ? 56.976 16.426  66.136  1.00 14.97 ?  176 PRO A O   1 
ATOM   1315 C  CB  . PRO A 1 176 ? 56.411 13.113  66.193  1.00 14.74 ?  176 PRO A CB  1 
ATOM   1316 C  CG  . PRO A 1 176 ? 56.594 11.848  65.405  1.00 14.16 ?  176 PRO A CG  1 
ATOM   1317 C  CD  . PRO A 1 176 ? 57.972 11.953  64.792  1.00 13.27 ?  176 PRO A CD  1 
ATOM   1318 N  N   . GLY A 1 177 ? 58.701 15.180  66.883  1.00 15.98 ?  177 GLY A N   1 
ATOM   1319 C  CA  . GLY A 1 177 ? 59.193 16.270  67.712  1.00 18.20 ?  177 GLY A CA  1 
ATOM   1320 C  C   . GLY A 1 177 ? 59.799 17.421  66.943  1.00 15.79 ?  177 GLY A C   1 
ATOM   1321 O  O   . GLY A 1 177 ? 60.056 18.476  67.539  1.00 15.47 ?  177 GLY A O   1 
ATOM   1322 N  N   . GLU A 1 178 ? 60.017 17.252  65.644  1.00 14.37 ?  178 GLU A N   1 
ATOM   1323 C  CA  . GLU A 1 178 ? 60.469 18.340  64.787  1.00 12.91 ?  178 GLU A CA  1 
ATOM   1324 C  C   . GLU A 1 178 ? 59.350 18.889  63.909  1.00 16.75 ?  178 GLU A C   1 
ATOM   1325 O  O   . GLU A 1 178 ? 59.560 19.896  63.233  1.00 15.98 ?  178 GLU A O   1 
ATOM   1326 C  CB  . GLU A 1 178 ? 61.644 17.874  63.910  1.00 16.06 ?  178 GLU A CB  1 
ATOM   1327 C  CG  . GLU A 1 178 ? 62.913 17.489  64.691  1.00 19.04 ?  178 GLU A CG  1 
ATOM   1328 C  CD  . GLU A 1 178 ? 64.023 16.965  63.781  1.00 22.73 ?  178 GLU A CD  1 
ATOM   1329 O  OE1 . GLU A 1 178 ? 64.004 17.271  62.572  1.00 34.76 ?  178 GLU A OE1 1 
ATOM   1330 O  OE2 . GLU A 1 178 ? 64.907 16.246  64.281  1.00 37.20 -1 178 GLU A OE2 1 
ATOM   1331 N  N   . ALA A 1 179 ? 58.159 18.281  63.935  1.00 14.55 ?  179 ALA A N   1 
ATOM   1332 C  CA  . ALA A 1 179 ? 57.130 18.539  62.918  1.00 14.28 ?  179 ALA A CA  1 
ATOM   1333 C  C   . ALA A 1 179 ? 56.222 19.699  63.327  1.00 16.28 ?  179 ALA A C   1 
ATOM   1334 O  O   . ALA A 1 179 ? 55.000 19.587  63.437  1.00 17.18 ?  179 ALA A O   1 
ATOM   1335 C  CB  . ALA A 1 179 ? 56.325 17.266  62.645  1.00 15.04 ?  179 ALA A CB  1 
ATOM   1336 N  N   . THR A 1 180 ? 56.853 20.844  63.555  1.00 15.21 ?  180 THR A N   1 
ATOM   1337 C  CA  . THR A 1 180 ? 56.099 22.074  63.735  1.00 14.40 ?  180 THR A CA  1 
ATOM   1338 C  C   . THR A 1 180 ? 55.611 22.577  62.378  1.00 14.56 ?  180 THR A C   1 
ATOM   1339 O  O   . THR A 1 180 ? 56.112 22.180  61.318  1.00 16.15 ?  180 THR A O   1 
ATOM   1340 C  CB  . THR A 1 180 ? 56.969 23.152  64.389  1.00 16.41 ?  180 THR A CB  1 
ATOM   1341 O  OG1 . THR A 1 180 ? 58.000 23.517  63.472  1.00 16.51 ?  180 THR A OG1 1 
ATOM   1342 C  CG2 . THR A 1 180 ? 57.592 22.643  65.674  1.00 20.88 ?  180 THR A CG2 1 
ATOM   1343 N  N   . ALA A 1 181 ? 54.646 23.498  62.418  1.00 17.62 ?  181 ALA A N   1 
ATOM   1344 C  CA  . ALA A 1 181 ? 54.162 24.097  61.175  1.00 17.15 ?  181 ALA A CA  1 
ATOM   1345 C  C   . ALA A 1 181 ? 55.286 24.789  60.417  1.00 16.21 ?  181 ALA A C   1 
ATOM   1346 O  O   . ALA A 1 181 ? 55.366 24.692  59.185  1.00 19.84 ?  181 ALA A O   1 
ATOM   1347 C  CB  . ALA A 1 181 ? 53.035 25.082  61.466  1.00 17.81 ?  181 ALA A CB  1 
ATOM   1348 N  N   . GLN A 1 182 ? 56.179 25.487  61.127  1.00 17.46 ?  182 GLN A N   1 
ATOM   1349 C  CA  . GLN A 1 182 ? 57.251 26.188  60.427  1.00 18.47 ?  182 GLN A CA  1 
ATOM   1350 C  C   . GLN A 1 182 ? 58.258 25.215  59.830  1.00 17.65 ?  182 GLN A C   1 
ATOM   1351 O  O   . GLN A 1 182 ? 58.782 25.450  58.738  1.00 15.64 ?  182 GLN A O   1 
ATOM   1352 C  CB  . GLN A 1 182 ? 57.956 27.167  61.369  1.00 18.97 ?  182 GLN A CB  1 
ATOM   1353 C  CG  . GLN A 1 182 ? 58.980 28.033  60.656  1.00 24.01 ?  182 GLN A CG  1 
ATOM   1354 C  CD  . GLN A 1 182 ? 58.321 28.990  59.682  1.00 33.13 ?  182 GLN A CD  1 
ATOM   1355 O  OE1 . GLN A 1 182 ? 57.428 29.743  60.057  1.00 37.00 ?  182 GLN A OE1 1 
ATOM   1356 N  NE2 . GLN A 1 182 ? 58.739 28.947  58.423  1.00 26.86 ?  182 GLN A NE2 1 
ATOM   1357 N  N   . ALA A 1 183 ? 58.526 24.097  60.506  1.00 15.36 ?  183 ALA A N   1 
ATOM   1358 C  CA  . ALA A 1 183 ? 59.443 23.126  59.928  1.00 18.22 ?  183 ALA A CA  1 
ATOM   1359 C  C   . ALA A 1 183 ? 58.881 22.579  58.626  1.00 14.19 ?  183 ALA A C   1 
ATOM   1360 O  O   . ALA A 1 183 ? 59.613 22.374  57.652  1.00 15.13 ?  183 ALA A O   1 
ATOM   1361 C  CB  . ALA A 1 183 ? 59.717 22.000  60.927  1.00 18.75 ?  183 ALA A CB  1 
ATOM   1362 N  N   . VAL A 1 184 ? 57.569 22.359  58.584  1.00 16.30 ?  184 VAL A N   1 
ATOM   1363 C  CA  . VAL A 1 184 ? 56.964 21.850  57.364  1.00 15.49 ?  184 VAL A CA  1 
ATOM   1364 C  C   . VAL A 1 184 ? 56.971 22.918  56.274  1.00 17.91 ?  184 VAL A C   1 
ATOM   1365 O  O   . VAL A 1 184 ? 57.314 22.636  55.121  1.00 19.03 ?  184 VAL A O   1 
ATOM   1366 C  CB  . VAL A 1 184 ? 55.555 21.322  57.679  1.00 16.13 ?  184 VAL A CB  1 
ATOM   1367 C  CG1 . VAL A 1 184 ? 54.818 20.949  56.390  1.00 20.16 ?  184 VAL A CG1 1 
ATOM   1368 C  CG2 . VAL A 1 184 ? 55.654 20.124  58.621  1.00 17.26 ?  184 VAL A CG2 1 
ATOM   1369 N  N   . LEU A 1 185 ? 56.630 24.161  56.626  1.00 17.98 ?  185 LEU A N   1 
ATOM   1370 C  CA  . LEU A 1 185 ? 56.695 25.261  55.658  1.00 18.57 ?  185 LEU A CA  1 
ATOM   1371 C  C   . LEU A 1 185 ? 58.086 25.420  55.067  1.00 21.00 ?  185 LEU A C   1 
ATOM   1372 O  O   . LEU A 1 185 ? 58.234 25.690  53.868  1.00 21.72 ?  185 LEU A O   1 
ATOM   1373 C  CB  . LEU A 1 185 ? 56.285 26.576  56.319  1.00 24.82 ?  185 LEU A CB  1 
ATOM   1374 C  CG  . LEU A 1 185 ? 54.802 26.896  56.388  1.00 23.75 ?  185 LEU A CG  1 
ATOM   1375 C  CD1 . LEU A 1 185 ? 54.608 28.317  56.924  1.00 26.43 ?  185 LEU A CD1 1 
ATOM   1376 C  CD2 . LEU A 1 185 ? 54.142 26.733  55.014  1.00 24.62 ?  185 LEU A CD2 1 
ATOM   1377 N  N   . ASP A 1 186 ? 59.121 25.304  55.899  1.00 18.15 ?  186 ASP A N   1 
ATOM   1378 C  CA  . ASP A 1 186 ? 60.483 25.444  55.391  1.00 18.92 ?  186 ASP A CA  1 
ATOM   1379 C  C   . ASP A 1 186 ? 60.822 24.341  54.393  1.00 21.84 ?  186 ASP A C   1 
ATOM   1380 O  O   . ASP A 1 186 ? 61.576 24.571  53.440  1.00 22.78 ?  186 ASP A O   1 
ATOM   1381 C  CB  . ASP A 1 186 ? 61.473 25.459  56.559  1.00 19.76 ?  186 ASP A CB  1 
ATOM   1382 C  CG  . ASP A 1 186 ? 61.352 26.721  57.408  1.00 29.69 ?  186 ASP A CG  1 
ATOM   1383 O  OD1 . ASP A 1 186 ? 60.659 27.667  56.979  1.00 33.51 ?  186 ASP A OD1 1 
ATOM   1384 O  OD2 . ASP A 1 186 ? 61.939 26.762  58.511  1.00 35.94 -1 186 ASP A OD2 1 
ATOM   1385 N  N   . ALA A 1 187 ? 60.247 23.148  54.576  1.00 17.43 ?  187 ALA A N   1 
ATOM   1386 C  CA  . ALA A 1 187 ? 60.499 22.052  53.656  1.00 16.27 ?  187 ALA A CA  1 
ATOM   1387 C  C   . ALA A 1 187 ? 59.818 22.279  52.317  1.00 17.91 ?  187 ALA A C   1 
ATOM   1388 O  O   . ALA A 1 187 ? 60.344 21.884  51.271  1.00 18.92 ?  187 ALA A O   1 
ATOM   1389 C  CB  . ALA A 1 187 ? 60.019 20.737  54.277  1.00 16.05 ?  187 ALA A CB  1 
ATOM   1390 N  N   . VAL A 1 188 ? 58.654 22.918  52.330  1.00 17.02 ?  188 VAL A N   1 
ATOM   1391 C  CA  . VAL A 1 188 ? 57.869 23.097  51.114  1.00 16.29 ?  188 VAL A CA  1 
ATOM   1392 C  C   . VAL A 1 188 ? 58.387 24.256  50.254  1.00 21.94 ?  188 VAL A C   1 
ATOM   1393 O  O   . VAL A 1 188 ? 58.212 24.251  49.029  1.00 20.21 ?  188 VAL A O   1 
ATOM   1394 C  CB  . VAL A 1 188 ? 56.402 23.294  51.537  1.00 19.53 ?  188 VAL A CB  1 
ATOM   1395 C  CG1 . VAL A 1 188 ? 55.593 23.930  50.442  1.00 24.16 ?  188 VAL A CG1 1 
ATOM   1396 C  CG2 . VAL A 1 188 ? 55.800 21.957  52.032  1.00 16.54 ?  188 VAL A CG2 1 
ATOM   1397 N  N   . LYS A 1 189 ? 59.001 25.261  50.869  1.00 19.71 ?  189 LYS A N   1 
ATOM   1398 C  CA  . LYS A 1 189 ? 59.495 26.465  50.173  1.00 21.75 ?  189 LYS A CA  1 
ATOM   1399 C  C   . LYS A 1 189 ? 58.328 27.094  49.411  1.00 18.10 ?  189 LYS A C   1 
ATOM   1400 O  O   . LYS A 1 189 ? 57.252 27.282  49.996  1.00 22.75 ?  189 LYS A O   1 
ATOM   1401 C  CB  . LYS A 1 189 ? 60.708 26.087  49.333  1.00 24.37 ?  189 LYS A CB  1 
ATOM   1402 C  CG  . LYS A 1 189 ? 61.957 25.778  50.159  1.00 32.33 ?  189 LYS A CG  1 
ATOM   1403 C  CD  . LYS A 1 189 ? 62.850 24.750  49.471  1.00 37.21 ?  189 LYS A CD  1 
ATOM   1404 C  CE  . LYS A 1 189 ? 63.368 23.706  50.471  1.00 40.58 ?  189 LYS A CE  1 
ATOM   1405 N  NZ  . LYS A 1 189 ? 63.797 22.432  49.809  1.00 34.94 ?  189 LYS A NZ  1 
ATOM   1406 N  N   . ASP A 1 190 ? 58.477 27.416  48.122  1.00 22.91 ?  190 ASP A N   1 
ATOM   1407 C  CA  . ASP A 1 190 ? 57.424 28.097  47.380  1.00 23.88 ?  190 ASP A CA  1 
ATOM   1408 C  C   . ASP A 1 190 ? 56.551 27.140  46.580  1.00 27.53 ?  190 ASP A C   1 
ATOM   1409 O  O   . ASP A 1 190 ? 55.814 27.579  45.693  1.00 27.50 ?  190 ASP A O   1 
ATOM   1410 C  CB  . ASP A 1 190 ? 58.029 29.155  46.451  1.00 25.42 ?  190 ASP A CB  1 
ATOM   1411 C  CG  . ASP A 1 190 ? 59.033 28.578  45.470  1.00 33.07 ?  190 ASP A CG  1 
ATOM   1412 O  OD1 . ASP A 1 190 ? 59.545 27.458  45.702  1.00 37.09 ?  190 ASP A OD1 1 
ATOM   1413 O  OD2 . ASP A 1 190 ? 59.325 29.258  44.457  1.00 41.72 -1 190 ASP A OD2 1 
ATOM   1414 N  N   . ALA A 1 191 ? 56.590 25.853  46.893  1.00 21.75 ?  191 ALA A N   1 
ATOM   1415 C  CA  . ALA A 1 191 ? 55.966 24.865  46.032  1.00 16.60 ?  191 ALA A CA  1 
ATOM   1416 C  C   . ALA A 1 191 ? 54.475 24.718  46.328  1.00 16.22 ?  191 ALA A C   1 
ATOM   1417 O  O   . ALA A 1 191 ? 54.013 24.976  47.450  1.00 18.41 ?  191 ALA A O   1 
ATOM   1418 C  CB  . ALA A 1 191 ? 56.654 23.516  46.211  1.00 17.88 ?  191 ALA A CB  1 
ATOM   1419 N  N   . PRO A 1 192 ? 53.698 24.279  45.344  1.00 14.25 ?  192 PRO A N   1 
ATOM   1420 C  CA  . PRO A 1 192 ? 52.356 23.780  45.654  1.00 15.01 ?  192 PRO A CA  1 
ATOM   1421 C  C   . PRO A 1 192 ? 52.476 22.464  46.406  1.00 12.87 ?  192 PRO A C   1 
ATOM   1422 O  O   . PRO A 1 192 ? 53.501 21.783  46.362  1.00 14.24 ?  192 PRO A O   1 
ATOM   1423 C  CB  . PRO A 1 192 ? 51.697 23.606  44.280  1.00 19.15 ?  192 PRO A CB  1 
ATOM   1424 C  CG  . PRO A 1 192 ? 52.828 23.446  43.326  1.00 21.09 ?  192 PRO A CG  1 
ATOM   1425 C  CD  . PRO A 1 192 ? 54.062 24.086  43.928  1.00 15.90 ?  192 PRO A CD  1 
ATOM   1426 N  N   . VAL A 1 193 ? 51.413 22.118  47.141  1.00 11.81 ?  193 VAL A N   1 
ATOM   1427 C  CA  . VAL A 1 193 ? 51.494 21.091  48.177  1.00 14.15 ?  193 VAL A CA  1 
ATOM   1428 C  C   . VAL A 1 193 ? 50.389 20.060  48.008  1.00 13.54 ?  193 VAL A C   1 
ATOM   1429 O  O   . VAL A 1 193 ? 49.220 20.405  47.811  1.00 14.87 ?  193 VAL A O   1 
ATOM   1430 C  CB  . VAL A 1 193 ? 51.403 21.718  49.583  1.00 13.23 ?  193 VAL A CB  1 
ATOM   1431 C  CG1 . VAL A 1 193 ? 51.449 20.622  50.672  1.00 16.20 ?  193 VAL A CG1 1 
ATOM   1432 C  CG2 . VAL A 1 193 ? 52.518 22.740  49.771  1.00 17.77 ?  193 VAL A CG2 1 
ATOM   1433 N  N   . TRP A 1 194 ? 50.759 18.784  48.122  1.00 12.20 ?  194 TRP A N   1 
ATOM   1434 C  CA  . TRP A 1 194 ? 49.810 17.683  48.241  1.00 11.14 ?  194 TRP A CA  1 
ATOM   1435 C  C   . TRP A 1 194 ? 50.012 17.033  49.604  1.00 10.87 ?  194 TRP A C   1 
ATOM   1436 O  O   . TRP A 1 194 ? 51.140 16.697  49.955  1.00 11.59 ?  194 TRP A O   1 
ATOM   1437 C  CB  . TRP A 1 194 ? 50.024 16.651  47.126  1.00 14.45 ?  194 TRP A CB  1 
ATOM   1438 C  CG  . TRP A 1 194 ? 49.081 15.484  47.152  1.00 11.83 ?  194 TRP A CG  1 
ATOM   1439 C  CD1 . TRP A 1 194 ? 49.259 14.293  47.806  1.00 14.51 ?  194 TRP A CD1 1 
ATOM   1440 C  CD2 . TRP A 1 194 ? 47.837 15.379  46.455  1.00 13.24 ?  194 TRP A CD2 1 
ATOM   1441 N  NE1 . TRP A 1 194 ? 48.187 13.451  47.563  1.00 14.77 ?  194 TRP A NE1 1 
ATOM   1442 C  CE2 . TRP A 1 194 ? 47.301 14.103  46.740  1.00 15.32 ?  194 TRP A CE2 1 
ATOM   1443 C  CE3 . TRP A 1 194 ? 47.120 16.248  45.627  1.00 15.42 ?  194 TRP A CE3 1 
ATOM   1444 C  CZ2 . TRP A 1 194 ? 46.076 13.671  46.216  1.00 17.03 ?  194 TRP A CZ2 1 
ATOM   1445 C  CZ3 . TRP A 1 194 ? 45.907 15.816  45.097  1.00 16.70 ?  194 TRP A CZ3 1 
ATOM   1446 C  CH2 . TRP A 1 194 ? 45.394 14.539  45.406  1.00 14.88 ?  194 TRP A CH2 1 
ATOM   1447 N  N   . ILE A 1 195 ? 48.937 16.860  50.374  1.00 12.11 ?  195 ILE A N   1 
ATOM   1448 C  CA  . ILE A 1 195 ? 49.035 16.308  51.722  1.00 11.26 ?  195 ILE A CA  1 
ATOM   1449 C  C   . ILE A 1 195 ? 48.409 14.920  51.731  1.00 12.75 ?  195 ILE A C   1 
ATOM   1450 O  O   . ILE A 1 195 ? 47.246 14.762  51.350  1.00 14.27 ?  195 ILE A O   1 
ATOM   1451 C  CB  . ILE A 1 195 ? 48.356 17.211  52.762  1.00 10.53 ?  195 ILE A CB  1 
ATOM   1452 C  CG1 . ILE A 1 195 ? 49.089 18.547  52.868  1.00 13.42 ?  195 ILE A CG1 1 
ATOM   1453 C  CG2 . ILE A 1 195 ? 48.278 16.504  54.140  1.00 15.73 ?  195 ILE A CG2 1 
ATOM   1454 C  CD1 . ILE A 1 195 ? 48.395 19.539  53.803  1.00 18.05 ?  195 ILE A CD1 1 
ATOM   1455 N  N   . HIS A 1 196 ? 49.171 13.927  52.172  1.00 10.49 ?  196 HIS A N   1 
ATOM   1456 C  CA  . HIS A 1 196 ? 48.714 12.549  52.325  1.00 10.83 ?  196 HIS A CA  1 
ATOM   1457 C  C   . HIS A 1 196 ? 48.836 12.188  53.804  1.00 10.98 ?  196 HIS A C   1 
ATOM   1458 O  O   . HIS A 1 196 ? 49.920 12.301  54.368  1.00 12.21 ?  196 HIS A O   1 
ATOM   1459 C  CB  . HIS A 1 196 ? 49.572 11.627  51.437  1.00 12.67 ?  196 HIS A CB  1 
ATOM   1460 C  CG  . HIS A 1 196 ? 49.407 10.168  51.727  1.00 12.68 ?  196 HIS A CG  1 
ATOM   1461 N  ND1 . HIS A 1 196 ? 48.800 9.307   50.835  1.00 14.37 ?  196 HIS A ND1 1 
ATOM   1462 C  CD2 . HIS A 1 196 ? 49.741 9.426   52.810  1.00 12.19 ?  196 HIS A CD2 1 
ATOM   1463 C  CE1 . HIS A 1 196 ? 48.772 8.092   51.362  1.00 16.04 ?  196 HIS A CE1 1 
ATOM   1464 N  NE2 . HIS A 1 196 ? 49.318 8.139   52.567  1.00 12.98 ?  196 HIS A NE2 1 
ATOM   1465 N  N   . ILE A 1 197 ? 47.746 11.769  54.455  1.00 9.87  ?  197 ILE A N   1 
ATOM   1466 C  CA  . ILE A 1 197 ? 47.802 11.443  55.882  1.00 11.10 ?  197 ILE A CA  1 
ATOM   1467 C  C   . ILE A 1 197 ? 47.335 10.021  56.138  1.00 11.45 ?  197 ILE A C   1 
ATOM   1468 O  O   . ILE A 1 197 ? 46.240 9.636   55.707  1.00 12.10 ?  197 ILE A O   1 
ATOM   1469 C  CB  . ILE A 1 197 ? 46.953 12.394  56.736  1.00 12.92 ?  197 ILE A CB  1 
ATOM   1470 C  CG1 . ILE A 1 197 ? 47.426 13.822  56.585  1.00 16.91 ?  197 ILE A CG1 1 
ATOM   1471 C  CG2 . ILE A 1 197 ? 47.052 11.997  58.226  1.00 17.45 ?  197 ILE A CG2 1 
ATOM   1472 C  CD1 . ILE A 1 197 ? 46.428 14.818  57.174  1.00 19.45 ?  197 ILE A CD1 1 
ATOM   1473 N  N   . ASP A 1 198 ? 48.166 9.259   56.847  1.00 10.41 ?  198 ASP A N   1 
ATOM   1474 C  CA  . ASP A 1 198 ? 47.833 7.970   57.444  1.00 10.20 ?  198 ASP A CA  1 
ATOM   1475 C  C   . ASP A 1 198 ? 47.655 8.197   58.936  1.00 9.04  ?  198 ASP A C   1 
ATOM   1476 O  O   . ASP A 1 198 ? 48.597 8.645   59.595  1.00 11.47 ?  198 ASP A O   1 
ATOM   1477 C  CB  . ASP A 1 198 ? 48.998 7.018   57.149  1.00 10.17 ?  198 ASP A CB  1 
ATOM   1478 C  CG  . ASP A 1 198 ? 48.907 5.651   57.806  1.00 10.98 ?  198 ASP A CG  1 
ATOM   1479 O  OD1 . ASP A 1 198 ? 48.108 5.411   58.738  1.00 11.42 ?  198 ASP A OD1 1 
ATOM   1480 O  OD2 . ASP A 1 198 ? 49.724 4.778   57.394  1.00 13.15 -1 198 ASP A OD2 1 
ATOM   1481 N  N   . TRP A 1 199 ? 46.442 7.925   59.465  1.00 9.38  ?  199 TRP A N   1 
ATOM   1482 C  CA  . TRP A 1 199 ? 46.147 8.265   60.851  1.00 11.38 ?  199 TRP A CA  1 
ATOM   1483 C  C   . TRP A 1 199 ? 47.004 7.512   61.861  1.00 10.06 ?  199 TRP A C   1 
ATOM   1484 O  O   . TRP A 1 199 ? 47.042 7.925   63.023  1.00 10.62 ?  199 TRP A O   1 
ATOM   1485 C  CB  . TRP A 1 199 ? 44.645 8.070   61.146  1.00 12.54 ?  199 TRP A CB  1 
ATOM   1486 C  CG  . TRP A 1 199 ? 43.782 8.963   60.295  1.00 10.98 ?  199 TRP A CG  1 
ATOM   1487 C  CD1 . TRP A 1 199 ? 42.789 8.562   59.422  1.00 12.25 ?  199 TRP A CD1 1 
ATOM   1488 C  CD2 . TRP A 1 199 ? 43.811 10.401  60.220  1.00 12.19 ?  199 TRP A CD2 1 
ATOM   1489 N  NE1 . TRP A 1 199 ? 42.241 9.643   58.801  1.00 12.64 ?  199 TRP A NE1 1 
ATOM   1490 C  CE2 . TRP A 1 199 ? 42.838 10.786  59.268  1.00 11.38 ?  199 TRP A CE2 1 
ATOM   1491 C  CE3 . TRP A 1 199 ? 44.572 11.393  60.848  1.00 12.81 ?  199 TRP A CE3 1 
ATOM   1492 C  CZ2 . TRP A 1 199 ? 42.600 12.124  58.931  1.00 11.91 ?  199 TRP A CZ2 1 
ATOM   1493 C  CZ3 . TRP A 1 199 ? 44.341 12.726  60.499  1.00 13.79 ?  199 TRP A CZ3 1 
ATOM   1494 C  CH2 . TRP A 1 199 ? 43.357 13.072  59.551  1.00 15.56 ?  199 TRP A CH2 1 
ATOM   1495 N  N   . ASP A 1 200 ? 47.756 6.476   61.456  1.00 10.60 ?  200 ASP A N   1 
ATOM   1496 C  CA  . ASP A 1 200 ? 48.653 5.887   62.446  1.00 12.00 ?  200 ASP A CA  1 
ATOM   1497 C  C   . ASP A 1 200 ? 49.816 6.820   62.821  1.00 9.41  ?  200 ASP A C   1 
ATOM   1498 O  O   . ASP A 1 200 ? 50.579 6.486   63.725  1.00 13.10 ?  200 ASP A O   1 
ATOM   1499 C  CB  . ASP A 1 200 ? 49.181 4.493   62.017  1.00 11.33 ?  200 ASP A CB  1 
ATOM   1500 C  CG  . ASP A 1 200 ? 50.105 4.500   60.766  1.00 13.79 ?  200 ASP A CG  1 
ATOM   1501 O  OD1 . ASP A 1 200 ? 50.806 5.496   60.526  1.00 11.79 ?  200 ASP A OD1 1 
ATOM   1502 O  OD2 . ASP A 1 200 ? 50.138 3.459   60.045  1.00 13.21 -1 200 ASP A OD2 1 
ATOM   1503 N  N   . VAL A 1 201 ? 49.926 7.995   62.199  1.00 10.09 ?  201 VAL A N   1 
ATOM   1504 C  CA  . VAL A 1 201 ? 50.902 8.976   62.645  1.00 10.98 ?  201 VAL A CA  1 
ATOM   1505 C  C   . VAL A 1 201 ? 50.556 9.519   64.032  1.00 12.38 ?  201 VAL A C   1 
ATOM   1506 O  O   . VAL A 1 201 ? 51.443 10.014  64.742  1.00 11.21 ?  201 VAL A O   1 
ATOM   1507 C  CB  . VAL A 1 201 ? 51.004 10.117  61.610  1.00 9.71  ?  201 VAL A CB  1 
ATOM   1508 C  CG1 . VAL A 1 201 ? 49.775 11.045  61.699  1.00 11.45 ?  201 VAL A CG1 1 
ATOM   1509 C  CG2 . VAL A 1 201 ? 52.322 10.900  61.781  1.00 11.84 ?  201 VAL A CG2 1 
ATOM   1510 N  N   . LEU A 1 202 ? 49.296 9.431   64.456  1.00 12.71 ?  202 LEU A N   1 
ATOM   1511 C  CA  . LEU A 1 202 ? 48.860 10.127  65.668  1.00 13.70 ?  202 LEU A CA  1 
ATOM   1512 C  C   . LEU A 1 202 ? 49.287 9.394   66.930  1.00 12.76 ?  202 LEU A C   1 
ATOM   1513 O  O   . LEU A 1 202 ? 49.208 8.168   67.004  1.00 18.87 ?  202 LEU A O   1 
ATOM   1514 C  CB  . LEU A 1 202 ? 47.337 10.255  65.679  1.00 13.98 ?  202 LEU A CB  1 
ATOM   1515 C  CG  . LEU A 1 202 ? 46.718 11.152  64.619  1.00 16.60 ?  202 LEU A CG  1 
ATOM   1516 C  CD1 . LEU A 1 202 ? 45.195 10.995  64.663  1.00 17.39 ?  202 LEU A CD1 1 
ATOM   1517 C  CD2 . LEU A 1 202 ? 47.147 12.589  64.834  1.00 19.29 ?  202 LEU A CD2 1 
ATOM   1518 N  N   . GLU A 1 203 ? 49.676 10.160  67.952  1.00 14.49 ?  203 GLU A N   1 
ATOM   1519 C  CA  . GLU A 1 203 ? 49.876 9.579   69.274  1.00 19.26 ?  203 GLU A CA  1 
ATOM   1520 C  C   . GLU A 1 203 ? 48.606 8.858   69.729  1.00 24.70 ?  203 GLU A C   1 
ATOM   1521 O  O   . GLU A 1 203 ? 47.523 9.447   69.671  1.00 22.04 ?  203 GLU A O   1 
ATOM   1522 C  CB  . GLU A 1 203 ? 50.237 10.683  70.261  1.00 22.60 ?  203 GLU A CB  1 
ATOM   1523 C  CG  . GLU A 1 203 ? 50.274 10.239  71.712  1.00 24.87 ?  203 GLU A CG  1 
ATOM   1524 C  CD  . GLU A 1 203 ? 51.514 9.429   72.053  1.00 31.63 ?  203 GLU A CD  1 
ATOM   1525 O  OE1 . GLU A 1 203 ? 52.384 9.270   71.180  1.00 22.96 ?  203 GLU A OE1 1 
ATOM   1526 O  OE2 . GLU A 1 203 ? 51.621 8.944   73.198  1.00 37.25 -1 203 GLU A OE2 1 
ATOM   1527 N  N   . PRO A 1 204 ? 48.689 7.598   70.167  1.00 22.07 ?  204 PRO A N   1 
ATOM   1528 C  CA  . PRO A 1 204 ? 47.490 6.915   70.672  1.00 27.34 ?  204 PRO A CA  1 
ATOM   1529 C  C   . PRO A 1 204 ? 46.761 7.778   71.694  1.00 43.37 ?  204 PRO A C   1 
ATOM   1530 O  O   . PRO A 1 204 ? 47.369 8.339   72.613  1.00 37.99 ?  204 PRO A O   1 
ATOM   1531 C  CB  . PRO A 1 204 ? 48.051 5.633   71.291  1.00 30.89 ?  204 PRO A CB  1 
ATOM   1532 C  CG  . PRO A 1 204 ? 49.252 5.336   70.445  1.00 32.38 ?  204 PRO A CG  1 
ATOM   1533 C  CD  . PRO A 1 204 ? 49.845 6.685   70.085  1.00 29.20 ?  204 PRO A CD  1 
ATOM   1534 N  N   . GLY A 1 205 ? 45.444 7.892   71.511  1.00 51.08 ?  205 GLY A N   1 
ATOM   1535 C  CA  . GLY A 1 205 ? 44.663 8.991   72.049  1.00 51.27 ?  205 GLY A CA  1 
ATOM   1536 C  C   . GLY A 1 205 ? 44.287 8.943   73.514  1.00 68.63 ?  205 GLY A C   1 
ATOM   1537 O  O   . GLY A 1 205 ? 43.130 9.195   73.865  1.00 70.57 ?  205 GLY A O   1 
ATOM   1538 N  N   . SER A 1 206 ? 45.244 8.630   74.385  1.00 69.79 ?  206 SER A N   1 
ATOM   1539 C  CA  . SER A 1 206 ? 45.059 8.861   75.818  1.00 67.98 ?  206 SER A CA  1 
ATOM   1540 C  C   . SER A 1 206 ? 45.447 10.313  76.109  1.00 74.44 ?  206 SER A C   1 
ATOM   1541 O  O   . SER A 1 206 ? 46.492 10.625  76.685  1.00 74.26 ?  206 SER A O   1 
ATOM   1542 C  CB  . SER A 1 206 ? 45.878 7.874   76.637  1.00 65.59 ?  206 SER A CB  1 
ATOM   1543 O  OG  . SER A 1 206 ? 45.096 6.740   76.988  1.00 54.49 ?  206 SER A OG  1 
ATOM   1544 N  N   . ILE A 1 207 ? 44.554 11.215  75.679  1.00 77.81 ?  207 ILE A N   1 
ATOM   1545 C  CA  . ILE A 1 207 ? 44.884 12.647  75.658  1.00 71.26 ?  207 ILE A CA  1 
ATOM   1546 C  C   . ILE A 1 207 ? 45.283 13.177  77.029  1.00 79.63 ?  207 ILE A C   1 
ATOM   1547 O  O   . ILE A 1 207 ? 46.149 14.059  77.093  1.00 76.98 ?  207 ILE A O   1 
ATOM   1548 C  CB  . ILE A 1 207 ? 43.739 13.443  75.022  1.00 73.47 ?  207 ILE A CB  1 
ATOM   1549 C  CG1 . ILE A 1 207 ? 43.259 12.749  73.746  1.00 72.33 ?  207 ILE A CG1 1 
ATOM   1550 C  CG2 . ILE A 1 207 ? 44.190 14.870  74.726  1.00 72.64 ?  207 ILE A CG2 1 
ATOM   1551 C  CD1 . ILE A 1 207 ? 41.972 11.976  73.925  1.00 65.01 ?  207 ILE A CD1 1 
ATOM   1552 N  N   . PRO A 1 208 ? 44.689 12.727  78.164  1.00 82.64 ?  208 PRO A N   1 
ATOM   1553 C  CA  . PRO A 1 208 ? 45.241 13.128  79.470  1.00 79.49 ?  208 PRO A CA  1 
ATOM   1554 C  C   . PRO A 1 208 ? 46.719 12.784  79.601  1.00 73.58 ?  208 PRO A C   1 
ATOM   1555 O  O   . PRO A 1 208 ? 47.097 11.878  80.351  1.00 70.49 ?  208 PRO A O   1 
ATOM   1556 C  CB  . PRO A 1 208 ? 44.385 12.338  80.465  1.00 82.93 ?  208 PRO A CB  1 
ATOM   1557 C  CG  . PRO A 1 208 ? 43.080 12.178  79.781  1.00 82.55 ?  208 PRO A CG  1 
ATOM   1558 C  CD  . PRO A 1 208 ? 43.390 12.042  78.312  1.00 78.10 ?  208 PRO A CD  1 
ATOM   1559 N  N   . ALA A 1 209 ? 47.560 13.522  78.874  1.00 71.43 ?  209 ALA A N   1 
ATOM   1560 C  CA  . ALA A 1 209 ? 48.981 13.236  78.763  1.00 55.07 ?  209 ALA A CA  1 
ATOM   1561 C  C   . ALA A 1 209 ? 49.756 14.553  78.805  1.00 48.75 ?  209 ALA A C   1 
ATOM   1562 O  O   . ALA A 1 209 ? 50.517 14.900  77.905  1.00 45.49 ?  209 ALA A O   1 
ATOM   1563 C  CB  . ALA A 1 209 ? 49.278 12.449  77.489  1.00 57.99 ?  209 ALA A CB  1 
ATOM   1564 N  N   . ASP A 1 210 ? 49.554 15.306  79.883  1.00 38.80 ?  210 ASP A N   1 
ATOM   1565 C  CA  . ASP A 1 210 ? 50.213 16.595  80.038  1.00 30.45 ?  210 ASP A CA  1 
ATOM   1566 C  C   . ASP A 1 210 ? 51.625 16.480  80.597  1.00 31.69 ?  210 ASP A C   1 
ATOM   1567 O  O   . ASP A 1 210 ? 52.386 17.445  80.504  1.00 28.09 ?  210 ASP A O   1 
ATOM   1568 C  CB  . ASP A 1 210 ? 49.378 17.504  80.944  1.00 39.71 ?  210 ASP A CB  1 
ATOM   1569 C  CG  . ASP A 1 210 ? 48.197 18.124  80.219  1.00 47.56 ?  210 ASP A CG  1 
ATOM   1570 O  OD1 . ASP A 1 210 ? 48.225 18.171  78.970  1.00 55.27 -1 210 ASP A OD1 1 
ATOM   1571 O  OD2 . ASP A 1 210 ? 47.244 18.563  80.899  1.00 50.94 -1 210 ASP A OD2 1 
ATOM   1572 N  N   . TYR A 1 211 ? 51.999 15.334  81.164  1.00 28.19 ?  211 TYR A N   1 
ATOM   1573 C  CA  . TYR A 1 211 ? 53.294 15.193  81.818  1.00 27.25 ?  211 TYR A CA  1 
ATOM   1574 C  C   . TYR A 1 211 ? 54.203 14.190  81.123  1.00 24.51 ?  211 TYR A C   1 
ATOM   1575 O  O   . TYR A 1 211 ? 55.281 13.883  81.644  1.00 27.67 ?  211 TYR A O   1 
ATOM   1576 C  CB  . TYR A 1 211 ? 53.090 14.819  83.289  1.00 27.64 ?  211 TYR A CB  1 
ATOM   1577 C  CG  . TYR A 1 211 ? 52.356 15.901  84.050  1.00 28.13 ?  211 TYR A CG  1 
ATOM   1578 C  CD1 . TYR A 1 211 ? 52.981 17.105  84.359  1.00 22.90 ?  211 TYR A CD1 1 
ATOM   1579 C  CD2 . TYR A 1 211 ? 51.030 15.734  84.434  1.00 31.75 ?  211 TYR A CD2 1 
ATOM   1580 C  CE1 . TYR A 1 211 ? 52.311 18.109  85.045  1.00 26.04 ?  211 TYR A CE1 1 
ATOM   1581 C  CE2 . TYR A 1 211 ? 50.351 16.727  85.123  1.00 34.82 ?  211 TYR A CE2 1 
ATOM   1582 C  CZ  . TYR A 1 211 ? 50.998 17.912  85.430  1.00 29.95 ?  211 TYR A CZ  1 
ATOM   1583 O  OH  . TYR A 1 211 ? 50.329 18.900  86.111  1.00 28.82 ?  211 TYR A OH  1 
ATOM   1584 N  N   . THR A 1 212 ? 53.810 13.692  79.955  1.00 28.30 ?  212 THR A N   1 
ATOM   1585 C  CA  . THR A 1 212 ? 54.609 12.767  79.168  1.00 28.97 ?  212 THR A CA  1 
ATOM   1586 C  C   . THR A 1 212 ? 54.827 13.348  77.775  1.00 23.35 ?  212 THR A C   1 
ATOM   1587 O  O   . THR A 1 212 ? 53.983 14.078  77.245  1.00 25.33 ?  212 THR A O   1 
ATOM   1588 C  CB  . THR A 1 212 ? 53.927 11.384  79.073  1.00 29.44 ?  212 THR A CB  1 
ATOM   1589 O  OG1 . THR A 1 212 ? 54.744 10.488  78.314  1.00 42.16 ?  212 THR A OG1 1 
ATOM   1590 C  CG2 . THR A 1 212 ? 52.578 11.503  78.414  1.00 32.21 ?  212 THR A CG2 1 
ATOM   1591 N  N   . VAL A 1 213 ? 55.978 13.034  77.197  1.00 21.05 ?  213 VAL A N   1 
ATOM   1592 C  CA  . VAL A 1 213 ? 56.331 13.503  75.857  1.00 18.10 ?  213 VAL A CA  1 
ATOM   1593 C  C   . VAL A 1 213 ? 55.797 12.486  74.855  1.00 17.76 ?  213 VAL A C   1 
ATOM   1594 O  O   . VAL A 1 213 ? 56.120 11.295  74.956  1.00 20.15 ?  213 VAL A O   1 
ATOM   1595 C  CB  . VAL A 1 213 ? 57.847 13.687  75.711  1.00 20.36 ?  213 VAL A CB  1 
ATOM   1596 C  CG1 . VAL A 1 213 ? 58.202 14.008  74.273  1.00 22.68 ?  213 VAL A CG1 1 
ATOM   1597 C  CG2 . VAL A 1 213 ? 58.336 14.791  76.638  1.00 25.54 ?  213 VAL A CG2 1 
ATOM   1598 N  N   . PRO A 1 214 ? 55.002 12.906  73.876  1.00 17.63 ?  214 PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 214 ? 54.390 11.943  72.955  1.00 18.30 ?  214 PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 214 ? 55.388 11.385  71.959  1.00 17.57 ?  214 PRO A C   1 
ATOM   1601 O  O   . PRO A 1 214 ? 56.362 12.038  71.568  1.00 22.58 ?  214 PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 214 ? 53.313 12.770  72.249  1.00 21.70 ?  214 PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 214 ? 53.844 14.144  72.262  1.00 19.74 ?  214 PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 214 ? 54.612 14.290  73.563  1.00 16.42 ?  214 PRO A CD  1 
ATOM   1605 N  N   . ASP A 1 215 ? 55.124 10.156  71.543  1.00 17.25 ?  215 ASP A N   1 
ATOM   1606 C  CA  . ASP A 1 215 ? 55.928 9.541   70.501  1.00 15.67 ?  215 ASP A CA  1 
ATOM   1607 C  C   . ASP A 1 215 ? 55.387 9.819   69.113  1.00 15.88 ?  215 ASP A C   1 
ATOM   1608 O  O   . ASP A 1 215 ? 56.172 9.911   68.160  1.00 17.37 ?  215 ASP A O   1 
ATOM   1609 C  CB  . ASP A 1 215 ? 55.997 8.029   70.725  1.00 22.05 ?  215 ASP A CB  1 
ATOM   1610 C  CG  . ASP A 1 215 ? 56.560 7.679   72.081  1.00 28.33 ?  215 ASP A CG  1 
ATOM   1611 O  OD1 . ASP A 1 215 ? 57.731 8.046   72.329  1.00 34.08 ?  215 ASP A OD1 1 
ATOM   1612 O  OD2 . ASP A 1 215 ? 55.830 7.053   72.887  1.00 37.02 -1 215 ASP A OD2 1 
ATOM   1613 N  N   . GLY A 1 216 ? 54.068 9.948   68.975  1.00 15.50 ?  216 GLY A N   1 
ATOM   1614 C  CA  . GLY A 1 216 ? 53.464 10.321  67.716  1.00 13.40 ?  216 GLY A CA  1 
ATOM   1615 C  C   . GLY A 1 216 ? 53.157 11.811  67.642  1.00 13.53 ?  216 GLY A C   1 
ATOM   1616 O  O   . GLY A 1 216 ? 53.447 12.588  68.550  1.00 16.14 ?  216 GLY A O   1 
ATOM   1617 N  N   . MET A 1 217 ? 52.573 12.204  66.516  1.00 12.96 ?  217 MET A N   1 
ATOM   1618 C  CA  . MET A 1 217 ? 52.108 13.576  66.350  1.00 12.46 ?  217 MET A CA  1 
ATOM   1619 C  C   . MET A 1 217 ? 50.790 13.777  67.077  1.00 14.13 ?  217 MET A C   1 
ATOM   1620 O  O   . MET A 1 217 ? 49.968 12.867  67.175  1.00 16.06 ?  217 MET A O   1 
ATOM   1621 C  CB  . MET A 1 217 ? 51.942 13.928  64.873  1.00 15.78 ?  217 MET A CB  1 
ATOM   1622 C  CG  . MET A 1 217 ? 53.263 14.109  64.193  1.00 16.13 ?  217 MET A CG  1 
ATOM   1623 S  SD  . MET A 1 217 ? 53.121 14.613  62.477  1.00 17.20 ?  217 MET A SD  1 
ATOM   1624 C  CE  . MET A 1 217 ? 52.574 16.325  62.611  1.00 17.41 ?  217 MET A CE  1 
ATOM   1625 N  N   . LEU A 1 218 ? 50.609 14.973  67.584  1.00 13.88 ?  218 LEU A N   1 
ATOM   1626 C  CA  . LEU A 1 218 ? 49.352 15.322  68.234  1.00 13.83 ?  218 LEU A CA  1 
ATOM   1627 C  C   . LEU A 1 218 ? 48.390 15.893  67.206  1.00 14.63 ?  218 LEU A C   1 
ATOM   1628 O  O   . LEU A 1 218 ? 48.826 16.485  66.219  1.00 15.57 ?  218 LEU A O   1 
ATOM   1629 C  CB  . LEU A 1 218 ? 49.585 16.354  69.327  1.00 14.71 ?  218 LEU A CB  1 
ATOM   1630 C  CG  . LEU A 1 218 ? 50.520 15.985  70.475  1.00 21.43 ?  218 LEU A CG  1 
ATOM   1631 C  CD1 . LEU A 1 218 ? 50.774 17.215  71.339  1.00 26.15 ?  218 LEU A CD1 1 
ATOM   1632 C  CD2 . LEU A 1 218 ? 49.935 14.856  71.300  1.00 22.44 ?  218 LEU A CD2 1 
ATOM   1633 N  N   . PRO A 1 219 ? 47.076 15.731  67.416  1.00 14.33 ?  219 PRO A N   1 
ATOM   1634 C  CA  . PRO A 1 219 ? 46.112 16.394  66.515  1.00 15.90 ?  219 PRO A CA  1 
ATOM   1635 C  C   . PRO A 1 219 ? 46.394 17.883  66.310  1.00 15.42 ?  219 PRO A C   1 
ATOM   1636 O  O   . PRO A 1 219 ? 46.268 18.393  65.191  1.00 16.47 ?  219 PRO A O   1 
ATOM   1637 C  CB  . PRO A 1 219 ? 44.771 16.155  67.224  1.00 16.63 ?  219 PRO A CB  1 
ATOM   1638 C  CG  . PRO A 1 219 ? 44.959 14.828  67.896  1.00 18.84 ?  219 PRO A CG  1 
ATOM   1639 C  CD  . PRO A 1 219 ? 46.414 14.821  68.368  1.00 18.24 ?  219 PRO A CD  1 
ATOM   1640 N  N   . ALA A 1 220 ? 46.783 18.597  67.365  1.00 15.23 ?  220 ALA A N   1 
ATOM   1641 C  CA  . ALA A 1 220 ? 47.090 20.013  67.213  1.00 15.37 ?  220 ALA A CA  1 
ATOM   1642 C  C   . ALA A 1 220 ? 48.222 20.253  66.226  1.00 15.79 ?  220 ALA A C   1 
ATOM   1643 O  O   . ALA A 1 220 ? 48.249 21.291  65.553  1.00 17.05 ?  220 ALA A O   1 
ATOM   1644 C  CB  . ALA A 1 220 ? 47.437 20.622  68.580  1.00 17.57 ?  220 ALA A CB  1 
ATOM   1645 N  N   . GLN A 1 221 ? 49.178 19.323  66.135  1.00 16.31 ?  221 GLN A N   1 
ATOM   1646 C  CA  . GLN A 1 221 ? 50.270 19.506  65.188  1.00 14.93 ?  221 GLN A CA  1 
ATOM   1647 C  C   . GLN A 1 221 ? 49.803 19.345  63.750  1.00 15.50 ?  221 GLN A C   1 
ATOM   1648 O  O   . GLN A 1 221 ? 50.278 20.055  62.857  1.00 14.60 ?  221 GLN A O   1 
ATOM   1649 C  CB  . GLN A 1 221 ? 51.397 18.514  65.460  1.00 14.85 ?  221 GLN A CB  1 
ATOM   1650 C  CG  . GLN A 1 221 ? 52.200 18.780  66.705  1.00 16.42 ?  221 GLN A CG  1 
ATOM   1651 C  CD  . GLN A 1 221 ? 53.287 17.743  66.874  1.00 12.76 ?  221 GLN A CD  1 
ATOM   1652 O  OE1 . GLN A 1 221 ? 52.997 16.573  67.095  1.00 15.57 ?  221 GLN A OE1 1 
ATOM   1653 N  NE2 . GLN A 1 221 ? 54.552 18.168  66.769  1.00 17.42 ?  221 GLN A NE2 1 
ATOM   1654 N  N   . ILE A 1 222 ? 48.896 18.395  63.505  1.00 16.12 ?  222 ILE A N   1 
ATOM   1655 C  CA  . ILE A 1 222 ? 48.329 18.248  62.169  1.00 13.18 ?  222 ILE A CA  1 
ATOM   1656 C  C   . ILE A 1 222 ? 47.495 19.473  61.820  1.00 13.88 ?  222 ILE A C   1 
ATOM   1657 O  O   . ILE A 1 222 ? 47.578 20.005  60.706  1.00 15.20 ?  222 ILE A O   1 
ATOM   1658 C  CB  . ILE A 1 222 ? 47.490 16.963  62.080  1.00 14.90 ?  222 ILE A CB  1 
ATOM   1659 C  CG1 . ILE A 1 222 ? 48.296 15.755  62.538  1.00 19.59 ?  222 ILE A CG1 1 
ATOM   1660 C  CG2 . ILE A 1 222 ? 46.934 16.797  60.675  1.00 17.94 ?  222 ILE A CG2 1 
ATOM   1661 C  CD1 . ILE A 1 222 ? 49.304 15.310  61.514  1.00 21.27 ?  222 ILE A CD1 1 
ATOM   1662 N  N   . ARG A 1 223 ? 46.681 19.937  62.770  1.00 14.12 ?  223 ARG A N   1 
ATOM   1663 C  CA  . ARG A 1 223 ? 45.877 21.122  62.509  1.00 13.93 ?  223 ARG A CA  1 
ATOM   1664 C  C   . ARG A 1 223 ? 46.771 22.296  62.148  1.00 14.72 ?  223 ARG A C   1 
ATOM   1665 O  O   . ARG A 1 223 ? 46.467 23.054  61.224  1.00 14.89 ?  223 ARG A O   1 
ATOM   1666 C  CB  . ARG A 1 223 ? 44.993 21.461  63.718  1.00 15.94 ?  223 ARG A CB  1 
ATOM   1667 C  CG  . ARG A 1 223 ? 43.971 22.550  63.394  1.00 19.89 ?  223 ARG A CG  1 
ATOM   1668 C  CD  . ARG A 1 223 ? 43.030 22.859  64.541  1.00 27.94 ?  223 ARG A CD  1 
ATOM   1669 N  NE  . ARG A 1 223 ? 42.466 24.200  64.384  1.00 37.78 ?  223 ARG A NE  1 
ATOM   1670 C  CZ  . ARG A 1 223 ? 41.197 24.464  64.081  1.00 40.85 ?  223 ARG A CZ  1 
ATOM   1671 N  NH1 . ARG A 1 223 ? 40.323 23.478  63.896  1.00 33.02 ?  223 ARG A NH1 1 
ATOM   1672 N  NH2 . ARG A 1 223 ? 40.803 25.729  63.966  1.00 31.41 ?  223 ARG A NH2 1 
ATOM   1673 N  N   . ALA A 1 224 ? 47.900 22.443  62.848  1.00 15.57 ?  224 ALA A N   1 
ATOM   1674 C  CA  . ALA A 1 224 ? 48.789 23.573  62.595  1.00 17.54 ?  224 ALA A CA  1 
ATOM   1675 C  C   . ALA A 1 224 ? 49.394 23.519  61.195  1.00 15.06 ?  224 ALA A C   1 
ATOM   1676 O  O   . ALA A 1 224 ? 49.597 24.565  60.577  1.00 17.65 ?  224 ALA A O   1 
ATOM   1677 C  CB  . ALA A 1 224 ? 49.884 23.619  63.663  1.00 15.82 ?  224 ALA A CB  1 
ATOM   1678 N  N   . VAL A 1 225 ? 49.633 22.315  60.656  1.00 14.51 ?  225 VAL A N   1 
ATOM   1679 C  CA  . VAL A 1 225 ? 50.064 22.186  59.266  1.00 16.45 ?  225 VAL A CA  1 
ATOM   1680 C  C   . VAL A 1 225 ? 48.976 22.659  58.306  1.00 17.99 ?  225 VAL A C   1 
ATOM   1681 O  O   . VAL A 1 225 ? 49.251 23.421  57.373  1.00 17.74 ?  225 VAL A O   1 
ATOM   1682 C  CB  . VAL A 1 225 ? 50.484 20.739  58.966  1.00 13.17 ?  225 VAL A CB  1 
ATOM   1683 C  CG1 . VAL A 1 225 ? 50.728 20.575  57.481  1.00 16.62 ?  225 VAL A CG1 1 
ATOM   1684 C  CG2 . VAL A 1 225 ? 51.748 20.391  59.763  1.00 17.27 ?  225 VAL A CG2 1 
ATOM   1685 N  N   . PHE A 1 226 ? 47.733 22.188  58.492  1.00 15.91 ?  226 PHE A N   1 
ATOM   1686 C  CA  . PHE A 1 226 ? 46.643 22.635  57.619  1.00 15.48 ?  226 PHE A CA  1 
ATOM   1687 C  C   . PHE A 1 226 ? 46.420 24.145  57.724  1.00 18.64 ?  226 PHE A C   1 
ATOM   1688 O  O   . PHE A 1 226 ? 46.030 24.784  56.740  1.00 21.62 ?  226 PHE A O   1 
ATOM   1689 C  CB  . PHE A 1 226 ? 45.354 21.869  57.957  1.00 13.94 ?  226 PHE A CB  1 
ATOM   1690 C  CG  . PHE A 1 226 ? 45.307 20.464  57.393  1.00 14.00 ?  226 PHE A CG  1 
ATOM   1691 C  CD1 . PHE A 1 226 ? 45.238 20.269  56.016  1.00 20.48 ?  226 PHE A CD1 1 
ATOM   1692 C  CD2 . PHE A 1 226 ? 45.342 19.357  58.216  1.00 18.61 ?  226 PHE A CD2 1 
ATOM   1693 C  CE1 . PHE A 1 226 ? 45.190 18.985  55.479  1.00 18.12 ?  226 PHE A CE1 1 
ATOM   1694 C  CE2 . PHE A 1 226 ? 45.290 18.074  57.696  1.00 19.49 ?  226 PHE A CE2 1 
ATOM   1695 C  CZ  . PHE A 1 226 ? 45.211 17.892  56.315  1.00 16.70 ?  226 PHE A CZ  1 
ATOM   1696 N  N   . GLU A 1 227 ? 46.654 24.730  58.905  1.00 17.10 ?  227 GLU A N   1 
ATOM   1697 C  CA  . GLU A 1 227 ? 46.528 26.177  59.078  1.00 20.89 ?  227 GLU A CA  1 
ATOM   1698 C  C   . GLU A 1 227 ? 47.623 26.930  58.332  1.00 22.30 ?  227 GLU A C   1 
ATOM   1699 O  O   . GLU A 1 227 ? 47.377 28.037  57.842  1.00 22.63 ?  227 GLU A O   1 
ATOM   1700 C  CB  . GLU A 1 227 ? 46.556 26.551  60.571  1.00 18.63 ?  227 GLU A CB  1 
ATOM   1701 C  CG  . GLU A 1 227 ? 45.407 25.961  61.384  1.00 25.96 ?  227 GLU A CG  1 
ATOM   1702 C  CD  . GLU A 1 227 ? 45.411 26.266  62.888  1.00 40.13 ?  227 GLU A CD  1 
ATOM   1703 O  OE1 . GLU A 1 227 ? 46.427 26.004  63.569  1.00 44.75 ?  227 GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A 1 227 ? 44.360 26.723  63.402  1.00 37.51 -1 227 GLU A OE2 1 
ATOM   1705 N  N   . ALA A 1 228 ? 48.822 26.340  58.211  1.00 18.58 ?  228 ALA A N   1 
ATOM   1706 C  CA  . ALA A 1 228 ? 49.985 27.034  57.662  1.00 22.81 ?  228 ALA A CA  1 
ATOM   1707 C  C   . ALA A 1 228 ? 50.087 26.986  56.140  1.00 19.50 ?  228 ALA A C   1 
ATOM   1708 O  O   . ALA A 1 228 ? 50.671 27.899  55.548  1.00 21.92 ?  228 ALA A O   1 
ATOM   1709 C  CB  . ALA A 1 228 ? 51.275 26.464  58.267  1.00 21.74 ?  228 ALA A CB  1 
ATOM   1710 N  N   . ILE A 1 229 ? 49.563 25.957  55.479  1.00 18.24 ?  229 ILE A N   1 
ATOM   1711 C  CA  . ILE A 1 229 ? 49.714 25.881  54.025  1.00 15.89 ?  229 ILE A CA  1 
ATOM   1712 C  C   . ILE A 1 229 ? 48.735 26.852  53.373  1.00 19.24 ?  229 ILE A C   1 
ATOM   1713 O  O   . ILE A 1 229 ? 47.523 26.755  53.617  1.00 22.89 ?  229 ILE A O   1 
ATOM   1714 C  CB  . ILE A 1 229 ? 49.498 24.449  53.510  1.00 20.77 ?  229 ILE A CB  1 
ATOM   1715 C  CG1 . ILE A 1 229 ? 50.417 23.458  54.238  1.00 20.93 ?  229 ILE A CG1 1 
ATOM   1716 C  CG2 . ILE A 1 229 ? 49.663 24.391  51.990  1.00 18.61 ?  229 ILE A CG2 1 
ATOM   1717 C  CD1 . ILE A 1 229 ? 51.887 23.644  53.985  1.00 20.79 ?  229 ILE A CD1 1 
ATOM   1718 N  N   . PRO A 1 230 ? 49.197 27.803  52.558  1.00 20.20 ?  230 PRO A N   1 
ATOM   1719 C  CA  . PRO A 1 230 ? 48.260 28.760  51.950  1.00 21.00 ?  230 PRO A CA  1 
ATOM   1720 C  C   . PRO A 1 230 ? 47.253 28.046  51.061  1.00 19.38 ?  230 PRO A C   1 
ATOM   1721 O  O   . PRO A 1 230 ? 47.597 27.121  50.321  1.00 20.45 ?  230 PRO A O   1 
ATOM   1722 C  CB  . PRO A 1 230 ? 49.171 29.688  51.140  1.00 27.27 ?  230 PRO A CB  1 
ATOM   1723 C  CG  . PRO A 1 230 ? 50.510 29.548  51.771  1.00 26.70 ?  230 PRO A CG  1 
ATOM   1724 C  CD  . PRO A 1 230 ? 50.596 28.110  52.208  1.00 20.50 ?  230 PRO A CD  1 
ATOM   1725 N  N   . ALA A 1 231 ? 45.990 28.477  51.158  1.00 21.01 ?  231 ALA A N   1 
ATOM   1726 C  CA  . ALA A 1 231 ? 44.928 27.860  50.367  1.00 21.20 ?  231 ALA A CA  1 
ATOM   1727 C  C   . ALA A 1 231 ? 45.268 27.830  48.881  1.00 20.96 ?  231 ALA A C   1 
ATOM   1728 O  O   . ALA A 1 231 ? 44.983 26.843  48.195  1.00 21.37 ?  231 ALA A O   1 
ATOM   1729 C  CB  . ALA A 1 231 ? 43.604 28.598  50.601  1.00 23.12 ?  231 ALA A CB  1 
ATOM   1730 N  N   . GLU A 1 232 ? 45.893 28.890  48.367  1.00 23.91 ?  232 GLU A N   1 
ATOM   1731 C  CA  . GLU A 1 232 ? 46.163 28.919  46.935  1.00 24.42 ?  232 GLU A CA  1 
ATOM   1732 C  C   . GLU A 1 232 ? 47.285 27.975  46.533  1.00 27.41 ?  232 GLU A C   1 
ATOM   1733 O  O   . GLU A 1 232 ? 47.460 27.729  45.333  1.00 28.13 ?  232 GLU A O   1 
ATOM   1734 C  CB  . GLU A 1 232 ? 46.476 30.347  46.476  1.00 34.13 ?  232 GLU A CB  1 
ATOM   1735 C  CG  . GLU A 1 232 ? 47.857 30.843  46.836  1.00 38.44 ?  232 GLU A CG  1 
ATOM   1736 C  CD  . GLU A 1 232 ? 48.795 30.872  45.638  1.00 55.99 ?  232 GLU A CD  1 
ATOM   1737 O  OE1 . GLU A 1 232 ? 48.459 30.270  44.593  1.00 56.31 ?  232 GLU A OE1 1 
ATOM   1738 O  OE2 . GLU A 1 232 ? 49.869 31.502  45.740  1.00 61.17 -1 232 GLU A OE2 1 
ATOM   1739 N  N   . ARG A 1 233 ? 48.030 27.421  47.497  1.00 19.13 ?  233 ARG A N   1 
ATOM   1740 C  CA  . ARG A 1 233 ? 49.084 26.472  47.182  1.00 20.23 ?  233 ARG A CA  1 
ATOM   1741 C  C   . ARG A 1 233 ? 48.656 25.022  47.380  1.00 18.87 ?  233 ARG A C   1 
ATOM   1742 O  O   . ARG A 1 233 ? 49.376 24.120  46.954  1.00 19.59 ?  233 ARG A O   1 
ATOM   1743 C  CB  . ARG A 1 233 ? 50.329 26.748  48.043  1.00 20.87 ?  233 ARG A CB  1 
ATOM   1744 C  CG  . ARG A 1 233 ? 51.037 28.076  47.744  1.00 27.71 ?  233 ARG A CG  1 
ATOM   1745 C  CD  . ARG A 1 233 ? 51.076 28.340  46.245  1.00 37.82 ?  233 ARG A CD  1 
ATOM   1746 N  NE  . ARG A 1 233 ? 52.394 28.115  45.663  1.00 44.48 ?  233 ARG A NE  1 
ATOM   1747 C  CZ  . ARG A 1 233 ? 52.595 27.735  44.404  1.00 39.97 ?  233 ARG A CZ  1 
ATOM   1748 N  NH1 . ARG A 1 233 ? 51.558 27.535  43.596  1.00 46.59 ?  233 ARG A NH1 1 
ATOM   1749 N  NH2 . ARG A 1 233 ? 53.830 27.557  43.949  1.00 32.56 ?  233 ARG A NH2 1 
ATOM   1750 N  N   . LEU A 1 234 ? 47.509 24.771  47.996  1.00 15.93 ?  234 LEU A N   1 
ATOM   1751 C  CA  . LEU A 1 234 ? 47.126 23.405  48.339  1.00 15.43 ?  234 LEU A CA  1 
ATOM   1752 C  C   . LEU A 1 234 ? 46.445 22.735  47.146  1.00 17.12 ?  234 LEU A C   1 
ATOM   1753 O  O   . LEU A 1 234 ? 45.365 23.160  46.720  1.00 18.56 ?  234 LEU A O   1 
ATOM   1754 C  CB  . LEU A 1 234 ? 46.218 23.398  49.571  1.00 14.20 ?  234 LEU A CB  1 
ATOM   1755 C  CG  . LEU A 1 234 ? 45.914 21.999  50.138  1.00 13.71 ?  234 LEU A CG  1 
ATOM   1756 C  CD1 . LEU A 1 234 ? 47.178 21.250  50.562  1.00 16.02 ?  234 LEU A CD1 1 
ATOM   1757 C  CD2 . LEU A 1 234 ? 44.923 22.116  51.317  1.00 14.36 ?  234 LEU A CD2 1 
ATOM   1758 N  N   . ILE A 1 235 ? 47.071 21.678  46.619  1.00 14.92 ?  235 ILE A N   1 
ATOM   1759 C  CA  . ILE A 1 235 ? 46.508 20.949  45.483  1.00 15.32 ?  235 ILE A CA  1 
ATOM   1760 C  C   . ILE A 1 235 ? 45.405 20.006  45.953  1.00 16.43 ?  235 ILE A C   1 
ATOM   1761 O  O   . ILE A 1 235 ? 44.306 19.951  45.380  1.00 16.51 ?  235 ILE A O   1 
ATOM   1762 C  CB  . ILE A 1 235 ? 47.619 20.179  44.736  1.00 16.68 ?  235 ILE A CB  1 
ATOM   1763 C  CG1 . ILE A 1 235 ? 48.703 21.121  44.218  1.00 19.29 ?  235 ILE A CG1 1 
ATOM   1764 C  CG2 . ILE A 1 235 ? 47.027 19.354  43.591  1.00 16.57 ?  235 ILE A CG2 1 
ATOM   1765 C  CD1 . ILE A 1 235 ? 49.987 20.399  43.880  1.00 18.35 ?  235 ILE A CD1 1 
ATOM   1766 N  N   . GLY A 1 236 ? 45.679 19.245  47.001  1.00 12.95 ?  236 GLY A N   1 
ATOM   1767 C  CA  . GLY A 1 236 ? 44.724 18.253  47.449  1.00 13.43 ?  236 GLY A CA  1 
ATOM   1768 C  C   . GLY A 1 236 ? 45.197 17.589  48.718  1.00 11.79 ?  236 GLY A C   1 
ATOM   1769 O  O   . GLY A 1 236 ? 46.325 17.808  49.189  1.00 12.48 ?  236 GLY A O   1 
ATOM   1770 N  N   . VAL A 1 237 ? 44.307 16.760  49.258  1.00 12.36 ?  237 VAL A N   1 
ATOM   1771 C  CA  . VAL A 1 237 ? 44.469 16.139  50.561  1.00 12.09 ?  237 VAL A CA  1 
ATOM   1772 C  C   . VAL A 1 237 ? 43.923 14.725  50.465  1.00 13.14 ?  237 VAL A C   1 
ATOM   1773 O  O   . VAL A 1 237 ? 42.817 14.522  49.944  1.00 14.38 ?  237 VAL A O   1 
ATOM   1774 C  CB  . VAL A 1 237 ? 43.721 16.917  51.659  1.00 14.67 ?  237 VAL A CB  1 
ATOM   1775 C  CG1 . VAL A 1 237 ? 43.855 16.192  52.994  1.00 14.91 ?  237 VAL A CG1 1 
ATOM   1776 C  CG2 . VAL A 1 237 ? 44.218 18.369  51.750  1.00 14.63 ?  237 VAL A CG2 1 
ATOM   1777 N  N   . GLU A 1 238 ? 44.686 13.748  50.958  1.00 11.71 ?  238 GLU A N   1 
ATOM   1778 C  CA  . GLU A 1 238 ? 44.240 12.366  51.093  1.00 11.32 ?  238 GLU A CA  1 
ATOM   1779 C  C   . GLU A 1 238 ? 44.210 11.976  52.564  1.00 11.12 ?  238 GLU A C   1 
ATOM   1780 O  O   . GLU A 1 238 ? 45.189 12.191  53.289  1.00 12.15 ?  238 GLU A O   1 
ATOM   1781 C  CB  . GLU A 1 238 ? 45.158 11.396  50.355  1.00 13.22 ?  238 GLU A CB  1 
ATOM   1782 C  CG  . GLU A 1 238 ? 45.487 11.754  48.953  1.00 15.79 ?  238 GLU A CG  1 
ATOM   1783 C  CD  . GLU A 1 238 ? 46.413 10.720  48.340  1.00 16.76 ?  238 GLU A CD  1 
ATOM   1784 O  OE1 . GLU A 1 238 ? 47.635 10.773  48.603  1.00 16.68 ?  238 GLU A OE1 1 
ATOM   1785 O  OE2 . GLU A 1 238 ? 45.912 9.839   47.612  1.00 18.01 -1 238 GLU A OE2 1 
ATOM   1786 N  N   . LEU A 1 239 ? 43.075 11.437  53.002  1.00 11.80 ?  239 LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 239 ? 42.855 10.984  54.374  1.00 10.93 ?  239 LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 239 ? 42.713 9.469   54.355  1.00 14.86 ?  239 LEU A C   1 
ATOM   1789 O  O   . LEU A 1 239 ? 41.754 8.957   53.771  1.00 15.24 ?  239 LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 239 ? 41.593 11.634  54.955  1.00 12.61 ?  239 LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 239 ? 41.565 13.150  54.816  1.00 12.90 ?  239 LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 239 ? 40.254 13.742  55.383  1.00 15.09 ?  239 LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 239 ? 42.764 13.789  55.515  1.00 15.36 ?  239 LEU A CD2 1 
ATOM   1794 N  N   . ALA A 1 240 ? 43.648 8.754   54.982  1.00 11.07 ?  240 ALA A N   1 
ATOM   1795 C  CA  . ALA A 1 240 ? 43.715 7.300   54.856  1.00 10.98 ?  240 ALA A CA  1 
ATOM   1796 C  C   . ALA A 1 240 ? 43.853 6.604   56.203  1.00 11.55 ?  240 ALA A C   1 
ATOM   1797 O  O   . ALA A 1 240 ? 44.473 7.123   57.149  1.00 10.87 ?  240 ALA A O   1 
ATOM   1798 C  CB  . ALA A 1 240 ? 44.889 6.855   53.942  1.00 13.83 ?  240 ALA A CB  1 
ATOM   1799 N  N   . GLU A 1 241 ? 43.287 5.394   56.261  1.00 13.79 ?  241 GLU A N   1 
ATOM   1800 C  CA  . GLU A 1 241 ? 43.561 4.396   57.299  1.00 11.98 ?  241 GLU A CA  1 
ATOM   1801 C  C   . GLU A 1 241 ? 42.969 4.778   58.661  1.00 13.13 ?  241 GLU A C   1 
ATOM   1802 O  O   . GLU A 1 241 ? 43.625 4.695   59.700  1.00 17.39 ?  241 GLU A O   1 
ATOM   1803 C  CB  . GLU A 1 241 ? 45.063 4.100   57.394  1.00 13.46 ?  241 GLU A CB  1 
ATOM   1804 C  CG  . GLU A 1 241 ? 45.683 3.784   56.004  1.00 17.09 ?  241 GLU A CG  1 
ATOM   1805 C  CD  . GLU A 1 241 ? 46.636 2.588   55.973  1.00 18.05 ?  241 GLU A CD  1 
ATOM   1806 O  OE1 . GLU A 1 241 ? 47.018 2.071   57.047  1.00 18.68 ?  241 GLU A OE1 1 
ATOM   1807 O  OE2 . GLU A 1 241 ? 47.045 2.180   54.854  1.00 17.23 -1 241 GLU A OE2 1 
ATOM   1808 N  N   . LEU A 1 242 ? 41.685 5.134   58.661  1.00 14.16 ?  242 LEU A N   1 
ATOM   1809 C  CA  . LEU A 1 242 ? 40.889 5.130   59.885  1.00 12.60 ?  242 LEU A CA  1 
ATOM   1810 C  C   . LEU A 1 242 ? 40.300 3.736   60.060  1.00 15.56 ?  242 LEU A C   1 
ATOM   1811 O  O   . LEU A 1 242 ? 39.458 3.319   59.263  1.00 15.57 ?  242 LEU A O   1 
ATOM   1812 C  CB  . LEU A 1 242 ? 39.772 6.165   59.808  1.00 14.37 ?  242 LEU A CB  1 
ATOM   1813 C  CG  . LEU A 1 242 ? 38.804 6.104   60.997  1.00 14.03 ?  242 LEU A CG  1 
ATOM   1814 C  CD1 . LEU A 1 242 ? 39.559 6.347   62.303  1.00 17.76 ?  242 LEU A CD1 1 
ATOM   1815 C  CD2 . LEU A 1 242 ? 37.672 7.096   60.823  1.00 15.88 ?  242 LEU A CD2 1 
ATOM   1816 N  N   . ASN A 1 243 ? 40.747 3.012   61.082  1.00 15.47 ?  243 ASN A N   1 
ATOM   1817 C  CA  . ASN A 1 243 ? 40.262 1.649   61.335  1.00 15.08 ?  243 ASN A CA  1 
ATOM   1818 C  C   . ASN A 1 243 ? 39.200 1.722   62.426  1.00 17.57 ?  243 ASN A C   1 
ATOM   1819 O  O   . ASN A 1 243 ? 39.503 1.636   63.613  1.00 21.78 ?  243 ASN A O   1 
ATOM   1820 C  CB  . ASN A 1 243 ? 41.395 0.706   61.732  1.00 14.06 ?  243 ASN A CB  1 
ATOM   1821 C  CG  . ASN A 1 243 ? 40.996 -0.755  61.616  1.00 14.98 ?  243 ASN A CG  1 
ATOM   1822 O  OD1 . ASN A 1 243 ? 40.275 -1.130  60.685  1.00 17.18 ?  243 ASN A OD1 1 
ATOM   1823 N  ND2 . ASN A 1 243 ? 41.475 -1.592  62.537  1.00 17.66 ?  243 ASN A ND2 1 
ATOM   1824 N  N   . ALA A 1 244 ? 37.938 1.897   62.018  1.00 17.13 ?  244 ALA A N   1 
ATOM   1825 C  CA  . ALA A 1 244 ? 36.896 2.046   63.028  1.00 18.34 ?  244 ALA A CA  1 
ATOM   1826 C  C   . ALA A 1 244 ? 35.614 1.486   62.436  1.00 16.96 ?  244 ALA A C   1 
ATOM   1827 O  O   . ALA A 1 244 ? 35.254 1.867   61.315  1.00 18.55 ?  244 ALA A O   1 
ATOM   1828 C  CB  . ALA A 1 244 ? 36.691 3.504   63.432  1.00 20.99 ?  244 ALA A CB  1 
ATOM   1829 N  N   . PRO A 1 245 ? 34.902 0.623   63.164  1.00 19.92 ?  245 PRO A N   1 
ATOM   1830 C  CA  . PRO A 1 245 ? 33.715 -0.019  62.597  1.00 21.03 ?  245 PRO A CA  1 
ATOM   1831 C  C   . PRO A 1 245 ? 32.613 0.977   62.288  1.00 25.79 ?  245 PRO A C   1 
ATOM   1832 O  O   . PRO A 1 245 ? 32.470 2.013   62.944  1.00 23.25 ?  245 PRO A O   1 
ATOM   1833 C  CB  . PRO A 1 245 ? 33.269 -0.986  63.702  1.00 20.89 ?  245 PRO A CB  1 
ATOM   1834 C  CG  . PRO A 1 245 ? 34.422 -1.155  64.580  1.00 23.92 ?  245 PRO A CG  1 
ATOM   1835 C  CD  . PRO A 1 245 ? 35.229 0.113   64.501  1.00 22.55 ?  245 PRO A CD  1 
ATOM   1836 N  N   . ALA A 1 246 ? 31.829 0.632   61.269  1.00 35.59 ?  246 ALA A N   1 
ATOM   1837 C  CA  . ALA A 1 246 ? 30.603 1.355   60.971  1.00 38.18 ?  246 ALA A CA  1 
ATOM   1838 C  C   . ALA A 1 246 ? 29.681 1.370   62.185  1.00 35.35 ?  246 ALA A C   1 
ATOM   1839 O  O   . ALA A 1 246 ? 29.537 0.366   62.892  1.00 36.53 ?  246 ALA A O   1 
ATOM   1840 C  CB  . ALA A 1 246 ? 29.890 0.710   59.784  1.00 38.09 ?  246 ALA A CB  1 
ATOM   1841 N  N   . ASP A 1 247 ? 29.065 2.526   62.426  1.00 41.65 ?  247 ASP A N   1 
ATOM   1842 C  CA  . ASP A 1 247 ? 28.073 2.748   63.476  1.00 42.87 ?  247 ASP A CA  1 
ATOM   1843 C  C   . ASP A 1 247 ? 28.651 2.669   64.883  1.00 37.13 ?  247 ASP A C   1 
ATOM   1844 O  O   . ASP A 1 247 ? 27.890 2.697   65.857  1.00 42.42 ?  247 ASP A O   1 
ATOM   1845 C  CB  . ASP A 1 247 ? 26.893 1.774   63.354  1.00 43.46 ?  247 ASP A CB  1 
ATOM   1846 C  CG  . ASP A 1 247 ? 26.477 1.544   61.913  1.00 57.50 ?  247 ASP A CG  1 
ATOM   1847 O  OD1 . ASP A 1 247 ? 26.169 0.386   61.555  1.00 64.85 -1 247 ASP A OD1 1 
ATOM   1848 O  OD2 . ASP A 1 247 ? 26.468 2.523   61.132  1.00 60.42 -1 247 ASP A OD2 1 
ATOM   1849 N  N   . SER A 1 248 ? 29.969 2.584   65.028  1.00 30.38 ?  248 SER A N   1 
ATOM   1850 C  CA  . SER A 1 248 ? 30.557 2.551   66.355  1.00 31.99 ?  248 SER A CA  1 
ATOM   1851 C  C   . SER A 1 248 ? 30.683 3.959   66.926  1.00 30.33 ?  248 SER A C   1 
ATOM   1852 O  O   . SER A 1 248 ? 30.891 4.939   66.199  1.00 27.24 ?  248 SER A O   1 
ATOM   1853 C  CB  . SER A 1 248 ? 31.929 1.877   66.330  1.00 28.53 ?  248 SER A CB  1 
ATOM   1854 O  OG  . SER A 1 248 ? 32.898 2.656   65.633  1.00 27.97 ?  248 SER A OG  1 
ATOM   1855 N  N   . GLU A 1 249 ? 30.537 4.053   68.249  1.00 27.53 ?  249 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 249 ? 30.903 5.286   68.936  1.00 30.98 ?  249 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 249 ? 32.346 5.664   68.642  1.00 29.81 ?  249 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 249 ? 32.673 6.853   68.549  1.00 26.13 ?  249 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 249 ? 30.699 5.138   70.443  1.00 38.58 ?  249 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 249 ? 29.336 5.575   70.941  1.00 51.36 ?  249 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 249 ? 29.219 5.468   72.450  1.00 68.95 ?  249 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 249 ? 30.259 5.591   73.135  1.00 62.81 ?  249 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 249 ? 28.093 5.253   72.949  1.00 80.60 -1 249 GLU A OE2 1 
ATOM   1864 N  N   . ARG A 1 250 ? 33.218 4.667   68.488  1.00 25.76 ?  250 ARG A N   1 
ATOM   1865 C  CA  . ARG A 1 250 ? 34.619 4.950   68.211  1.00 24.42 ?  250 ARG A CA  1 
ATOM   1866 C  C   . ARG A 1 250 ? 34.779 5.744   66.922  1.00 21.63 ?  250 ARG A C   1 
ATOM   1867 O  O   . ARG A 1 250 ? 35.533 6.722   66.879  1.00 22.42 ?  250 ARG A O   1 
ATOM   1868 C  CB  . ARG A 1 250 ? 35.408 3.649   68.130  1.00 25.88 ?  250 ARG A CB  1 
ATOM   1869 C  CG  . ARG A 1 250 ? 36.886 3.866   67.977  1.00 27.36 ?  250 ARG A CG  1 
ATOM   1870 C  CD  . ARG A 1 250 ? 37.554 2.591   67.522  1.00 34.89 ?  250 ARG A CD  1 
ATOM   1871 N  NE  . ARG A 1 250 ? 38.998 2.753   67.391  1.00 36.20 ?  250 ARG A NE  1 
ATOM   1872 C  CZ  . ARG A 1 250 ? 39.861 2.588   68.387  1.00 42.28 ?  250 ARG A CZ  1 
ATOM   1873 N  NH1 . ARG A 1 250 ? 39.428 2.246   69.600  1.00 33.56 ?  250 ARG A NH1 1 
ATOM   1874 N  NH2 . ARG A 1 250 ? 41.158 2.757   68.168  1.00 36.65 ?  250 ARG A NH2 1 
ATOM   1875 N  N   . ALA A 1 251 ? 34.071 5.339   65.861  1.00 22.68 ?  251 ALA A N   1 
ATOM   1876 C  CA  . ALA A 1 251 ? 34.160 6.068   64.600  1.00 19.85 ?  251 ALA A CA  1 
ATOM   1877 C  C   . ALA A 1 251 ? 33.596 7.475   64.743  1.00 24.51 ?  251 ALA A C   1 
ATOM   1878 O  O   . ALA A 1 251 ? 34.143 8.429   64.173  1.00 21.53 ?  251 ALA A O   1 
ATOM   1879 C  CB  . ALA A 1 251 ? 33.437 5.307   63.493  1.00 19.63 ?  251 ALA A CB  1 
ATOM   1880 N  N   . GLU A 1 252 ? 32.504 7.624   65.505  1.00 22.18 ?  252 GLU A N   1 
ATOM   1881 C  CA  . GLU A 1 252 ? 31.937 8.948   65.752  1.00 23.26 ?  252 GLU A CA  1 
ATOM   1882 C  C   . GLU A 1 252 ? 32.966 9.886   66.368  1.00 22.47 ?  252 GLU A C   1 
ATOM   1883 O  O   . GLU A 1 252 ? 33.120 11.036  65.935  1.00 23.70 ?  252 GLU A O   1 
ATOM   1884 C  CB  . GLU A 1 252 ? 30.715 8.832   66.675  1.00 30.07 ?  252 GLU A CB  1 
ATOM   1885 C  CG  . GLU A 1 252 ? 29.529 8.135   66.044  1.00 41.65 ?  252 GLU A CG  1 
ATOM   1886 C  CD  . GLU A 1 252 ? 28.964 8.913   64.880  1.00 50.45 ?  252 GLU A CD  1 
ATOM   1887 O  OE1 . GLU A 1 252 ? 28.437 8.284   63.935  1.00 55.41 ?  252 GLU A OE1 1 
ATOM   1888 O  OE2 . GLU A 1 252 ? 29.055 10.161  64.901  1.00 56.10 -1 252 GLU A OE2 1 
ATOM   1889 N  N   . GLN A 1 253 ? 33.670 9.414   67.394  1.00 19.83 ?  253 GLN A N   1 
ATOM   1890 C  CA  . GLN A 1 253 ? 34.655 10.252  68.076  1.00 21.88 ?  253 GLN A CA  1 
ATOM   1891 C  C   . GLN A 1 253 ? 35.873 10.511  67.199  1.00 20.45 ?  253 GLN A C   1 
ATOM   1892 O  O   . GLN A 1 253 ? 36.429 11.613  67.209  1.00 22.31 ?  253 GLN A O   1 
ATOM   1893 C  CB  . GLN A 1 253 ? 35.078 9.590   69.383  1.00 24.08 ?  253 GLN A CB  1 
ATOM   1894 C  CG  . GLN A 1 253 ? 33.897 9.307   70.318  1.00 27.80 ?  253 GLN A CG  1 
ATOM   1895 C  CD  . GLN A 1 253 ? 34.256 8.373   71.455  1.00 42.29 ?  253 GLN A CD  1 
ATOM   1896 O  OE1 . GLN A 1 253 ? 35.127 7.513   71.319  1.00 38.09 ?  253 GLN A OE1 1 
ATOM   1897 N  NE2 . GLN A 1 253 ? 33.582 8.536   72.588  1.00 42.35 ?  253 GLN A NE2 1 
ATOM   1898 N  N   . ALA A 1 254 ? 36.301 9.503   66.443  1.00 21.66 ?  254 ALA A N   1 
ATOM   1899 C  CA  . ALA A 1 254 ? 37.454 9.673   65.573  1.00 21.59 ?  254 ALA A CA  1 
ATOM   1900 C  C   . ALA A 1 254 ? 37.190 10.721  64.499  1.00 17.87 ?  254 ALA A C   1 
ATOM   1901 O  O   . ALA A 1 254 ? 38.042 11.583  64.252  1.00 17.79 ?  254 ALA A O   1 
ATOM   1902 C  CB  . ALA A 1 254 ? 37.833 8.332   64.945  1.00 17.77 ?  254 ALA A CB  1 
ATOM   1903 N  N   . VAL A 1 255 ? 36.011 10.681  63.858  1.00 17.22 ?  255 VAL A N   1 
ATOM   1904 C  CA  . VAL A 1 255 ? 35.791 11.622  62.760  1.00 15.78 ?  255 VAL A CA  1 
ATOM   1905 C  C   . VAL A 1 255 ? 35.627 13.044  63.281  1.00 17.28 ?  255 VAL A C   1 
ATOM   1906 O  O   . VAL A 1 255 ? 35.927 14.002  62.568  1.00 17.29 ?  255 VAL A O   1 
ATOM   1907 C  CB  . VAL A 1 255 ? 34.606 11.210  61.862  1.00 18.97 ?  255 VAL A CB  1 
ATOM   1908 C  CG1 . VAL A 1 255 ? 34.873 9.841   61.211  1.00 19.28 ?  255 VAL A CG1 1 
ATOM   1909 C  CG2 . VAL A 1 255 ? 33.299 11.220  62.634  1.00 26.12 ?  255 VAL A CG2 1 
ATOM   1910 N  N   . ALA A 1 256 ? 35.183 13.216  64.530  1.00 18.85 ?  256 ALA A N   1 
ATOM   1911 C  CA  . ALA A 1 256 ? 35.132 14.563  65.093  1.00 17.06 ?  256 ALA A CA  1 
ATOM   1912 C  C   . ALA A 1 256 ? 36.531 15.165  65.237  1.00 14.88 ?  256 ALA A C   1 
ATOM   1913 O  O   . ALA A 1 256 ? 36.750 16.334  64.899  1.00 18.70 ?  256 ALA A O   1 
ATOM   1914 C  CB  . ALA A 1 256 ? 34.395 14.539  66.434  1.00 21.23 ?  256 ALA A CB  1 
ATOM   1915 N  N   . VAL A 1 257 ? 37.504 14.361  65.672  1.00 19.73 ?  257 VAL A N   1 
ATOM   1916 C  CA  . VAL A 1 257 ? 38.889 14.822  65.732  1.00 18.29 ?  257 VAL A CA  1 
ATOM   1917 C  C   . VAL A 1 257 ? 39.427 15.095  64.330  1.00 14.34 ?  257 VAL A C   1 
ATOM   1918 O  O   . VAL A 1 257 ? 40.132 16.094  64.106  1.00 16.08 ?  257 VAL A O   1 
ATOM   1919 C  CB  . VAL A 1 257 ? 39.755 13.799  66.487  1.00 19.89 ?  257 VAL A CB  1 
ATOM   1920 C  CG1 . VAL A 1 257 ? 41.204 14.224  66.496  1.00 21.05 ?  257 VAL A CG1 1 
ATOM   1921 C  CG2 . VAL A 1 257 ? 39.243 13.651  67.920  1.00 25.77 ?  257 VAL A CG2 1 
ATOM   1922 N  N   . ILE A 1 258 ? 39.079 14.236  63.361  1.00 15.02 ?  258 ILE A N   1 
ATOM   1923 C  CA  . ILE A 1 258 ? 39.552 14.447  61.993  1.00 14.77 ?  258 ILE A CA  1 
ATOM   1924 C  C   . ILE A 1 258 ? 39.033 15.771  61.449  1.00 12.95 ?  258 ILE A C   1 
ATOM   1925 O  O   . ILE A 1 258 ? 39.780 16.559  60.855  1.00 14.60 ?  258 ILE A O   1 
ATOM   1926 C  CB  . ILE A 1 258 ? 39.142 13.273  61.087  1.00 13.64 ?  258 ILE A CB  1 
ATOM   1927 C  CG1 . ILE A 1 258 ? 39.955 12.015  61.406  1.00 13.04 ?  258 ILE A CG1 1 
ATOM   1928 C  CG2 . ILE A 1 258 ? 39.300 13.672  59.623  1.00 15.77 ?  258 ILE A CG2 1 
ATOM   1929 C  CD1 . ILE A 1 258 ? 39.384 10.731  60.769  1.00 14.92 ?  258 ILE A CD1 1 
ATOM   1930 N  N   . LEU A 1 259 ? 37.735 16.041  61.639  1.00 16.61 ?  259 LEU A N   1 
ATOM   1931 C  CA  . LEU A 1 259 ? 37.174 17.280  61.108  1.00 16.81 ?  259 LEU A CA  1 
ATOM   1932 C  C   . LEU A 1 259 ? 37.854 18.498  61.721  1.00 15.93 ?  259 LEU A C   1 
ATOM   1933 O  O   . LEU A 1 259 ? 38.089 19.493  61.029  1.00 15.16 ?  259 LEU A O   1 
ATOM   1934 C  CB  . LEU A 1 259 ? 35.659 17.323  61.341  1.00 17.47 ?  259 LEU A CB  1 
ATOM   1935 C  CG  . LEU A 1 259 ? 34.777 16.831  60.177  1.00 18.08 ?  259 LEU A CG  1 
ATOM   1936 C  CD1 . LEU A 1 259 ? 35.253 15.499  59.586  1.00 24.64 ?  259 LEU A CD1 1 
ATOM   1937 C  CD2 . LEU A 1 259 ? 33.303 16.748  60.630  1.00 22.19 ?  259 LEU A CD2 1 
ATOM   1938 N  N   . ASP A 1 260 ? 38.206 18.422  63.008  1.00 17.26 ?  260 ASP A N   1 
ATOM   1939 C  CA  . ASP A 1 260 ? 38.903 19.532  63.653  1.00 17.65 ?  260 ASP A CA  1 
ATOM   1940 C  C   . ASP A 1 260 ? 40.289 19.753  63.045  1.00 16.24 ?  260 ASP A C   1 
ATOM   1941 O  O   . ASP A 1 260 ? 40.729 20.899  62.874  1.00 18.48 ?  260 ASP A O   1 
ATOM   1942 C  CB  . ASP A 1 260 ? 39.007 19.282  65.160  1.00 20.23 ?  260 ASP A CB  1 
ATOM   1943 C  CG  . ASP A 1 260 ? 39.776 20.385  65.885  1.00 35.71 ?  260 ASP A CG  1 
ATOM   1944 O  OD1 . ASP A 1 260 ? 39.149 21.397  66.257  1.00 43.05 ?  260 ASP A OD1 1 
ATOM   1945 O  OD2 . ASP A 1 260 ? 41.007 20.250  66.072  1.00 38.05 -1 260 ASP A OD2 1 
ATOM   1946 N  N   . MET A 1 261 ? 40.983 18.665  62.690  1.00 15.75 ?  261 MET A N   1 
ATOM   1947 C  CA  . MET A 1 261 ? 42.322 18.807  62.130  1.00 15.58 ?  261 MET A CA  1 
ATOM   1948 C  C   . MET A 1 261 ? 42.284 19.423  60.737  1.00 15.05 ?  261 MET A C   1 
ATOM   1949 O  O   . MET A 1 261 ? 43.129 20.261  60.402  1.00 13.12 ?  261 MET A O   1 
ATOM   1950 C  CB  . MET A 1 261 ? 43.015 17.440  62.088  1.00 14.43 ?  261 MET A CB  1 
ATOM   1951 C  CG  . MET A 1 261 ? 43.447 16.954  63.468  1.00 16.33 ?  261 MET A CG  1 
ATOM   1952 S  SD  . MET A 1 261 ? 44.358 15.380  63.432  1.00 18.58 ?  261 MET A SD  1 
ATOM   1953 C  CE  . MET A 1 261 ? 43.003 14.231  63.255  1.00 19.91 ?  261 MET A CE  1 
ATOM   1954 N  N   . VAL A 1 262 ? 41.316 19.021  59.906  1.00 12.29 ?  262 VAL A N   1 
ATOM   1955 C  CA  . VAL A 1 262 ? 41.325 19.453  58.505  1.00 13.23 ?  262 VAL A CA  1 
ATOM   1956 C  C   . VAL A 1 262 ? 40.581 20.753  58.269  1.00 15.20 ?  262 VAL A C   1 
ATOM   1957 O  O   . VAL A 1 262 ? 40.724 21.345  57.185  1.00 14.31 ?  262 VAL A O   1 
ATOM   1958 C  CB  . VAL A 1 262 ? 40.722 18.385  57.562  1.00 14.07 ?  262 VAL A CB  1 
ATOM   1959 C  CG1 . VAL A 1 262 ? 41.523 17.093  57.647  1.00 15.07 ?  262 VAL A CG1 1 
ATOM   1960 C  CG2 . VAL A 1 262 ? 39.223 18.157  57.862  1.00 14.63 ?  262 VAL A CG2 1 
ATOM   1961 N  N   . ALA A 1 263 ? 39.799 21.221  59.246  1.00 13.87 ?  263 ALA A N   1 
ATOM   1962 C  CA  . ALA A 1 263 ? 38.956 22.402  59.051  1.00 16.07 ?  263 ALA A CA  1 
ATOM   1963 C  C   . ALA A 1 263 ? 39.668 23.617  58.467  1.00 17.83 ?  263 ALA A C   1 
ATOM   1964 O  O   . ALA A 1 263 ? 39.099 24.246  57.558  1.00 18.30 ?  263 ALA A O   1 
ATOM   1965 C  CB  . ALA A 1 263 ? 38.284 22.767  60.386  1.00 16.58 ?  263 ALA A CB  1 
ATOM   1966 N  N   . PRO A 1 264 ? 40.878 23.992  58.890  1.00 16.46 ?  264 PRO A N   1 
ATOM   1967 C  CA  . PRO A 1 264 ? 41.472 25.221  58.329  1.00 19.44 ?  264 PRO A CA  1 
ATOM   1968 C  C   . PRO A 1 264 ? 41.602 25.178  56.822  1.00 18.53 ?  264 PRO A C   1 
ATOM   1969 O  O   . PRO A 1 264 ? 41.317 26.176  56.145  1.00 23.34 ?  264 PRO A O   1 
ATOM   1970 C  CB  . PRO A 1 264 ? 42.838 25.290  59.021  1.00 19.74 ?  264 PRO A CB  1 
ATOM   1971 C  CG  . PRO A 1 264 ? 42.615 24.560  60.298  1.00 19.43 ?  264 PRO A CG  1 
ATOM   1972 C  CD  . PRO A 1 264 ? 41.708 23.431  59.966  1.00 17.08 ?  264 PRO A CD  1 
ATOM   1973 N  N   . ALA A 1 265 ? 42.006 24.029  56.275  1.00 19.05 ?  265 ALA A N   1 
ATOM   1974 C  CA  . ALA A 1 265 ? 42.167 23.906  54.835  1.00 19.85 ?  265 ALA A CA  1 
ATOM   1975 C  C   . ALA A 1 265 ? 40.829 23.763  54.123  1.00 17.04 ?  265 ALA A C   1 
ATOM   1976 O  O   . ALA A 1 265 ? 40.604 24.389  53.081  1.00 20.23 ?  265 ALA A O   1 
ATOM   1977 C  CB  . ALA A 1 265 ? 43.063 22.712  54.523  1.00 20.22 ?  265 ALA A CB  1 
ATOM   1978 N  N   . PHE A 1 266 ? 39.916 22.964  54.677  1.00 16.60 ?  266 PHE A N   1 
ATOM   1979 C  CA  . PHE A 1 266 ? 38.672 22.709  53.968  1.00 15.94 ?  266 PHE A CA  1 
ATOM   1980 C  C   . PHE A 1 266 ? 37.750 23.925  54.039  1.00 18.20 ?  266 PHE A C   1 
ATOM   1981 O  O   . PHE A 1 266 ? 37.054 24.237  53.064  1.00 17.98 ?  266 PHE A O   1 
ATOM   1982 C  CB  . PHE A 1 266 ? 37.987 21.458  54.527  1.00 18.33 ?  266 PHE A CB  1 
ATOM   1983 C  CG  . PHE A 1 266 ? 38.722 20.160  54.230  1.00 16.04 ?  266 PHE A CG  1 
ATOM   1984 C  CD1 . PHE A 1 266 ? 39.976 20.150  53.634  1.00 21.90 ?  266 PHE A CD1 1 
ATOM   1985 C  CD2 . PHE A 1 266 ? 38.150 18.956  54.580  1.00 20.07 ?  266 PHE A CD2 1 
ATOM   1986 C  CE1 . PHE A 1 266 ? 40.627 18.946  53.379  1.00 18.82 ?  266 PHE A CE1 1 
ATOM   1987 C  CE2 . PHE A 1 266 ? 38.793 17.761  54.327  1.00 18.75 ?  266 PHE A CE2 1 
ATOM   1988 C  CZ  . PHE A 1 266 ? 40.031 17.752  53.737  1.00 17.27 ?  266 PHE A CZ  1 
ATOM   1989 N  N   . ASP A 1 267 ? 37.765 24.639  55.172  1.00 19.07 ?  267 ASP A N   1 
ATOM   1990 C  CA  . ASP A 1 267 ? 36.982 25.866  55.291  1.00 20.69 ?  267 ASP A CA  1 
ATOM   1991 C  C   . ASP A 1 267 ? 37.430 26.899  54.272  1.00 21.01 ?  267 ASP A C   1 
ATOM   1992 O  O   . ASP A 1 267 ? 36.598 27.588  53.669  1.00 23.08 ?  267 ASP A O   1 
ATOM   1993 C  CB  . ASP A 1 267 ? 37.112 26.460  56.694  1.00 17.60 ?  267 ASP A CB  1 
ATOM   1994 C  CG  . ASP A 1 267 ? 36.376 25.661  57.761  1.00 20.14 ?  267 ASP A CG  1 
ATOM   1995 O  OD1 . ASP A 1 267 ? 35.585 24.762  57.431  1.00 19.19 ?  267 ASP A OD1 1 
ATOM   1996 O  OD2 . ASP A 1 267 ? 36.620 25.942  58.956  1.00 19.76 -1 267 ASP A OD2 1 
ATOM   1997 N  N   . ALA A 1 268 ? 38.746 27.047  54.095  1.00 21.23 ?  268 ALA A N   1 
ATOM   1998 C  CA  . ALA A 1 268 ? 39.255 27.998  53.109  1.00 21.86 ?  268 ALA A CA  1 
ATOM   1999 C  C   . ALA A 1 268 ? 38.843 27.603  51.697  1.00 25.39 ?  268 ALA A C   1 
ATOM   2000 O  O   . ALA A 1 268 ? 38.432 28.454  50.899  1.00 30.73 ?  268 ALA A O   1 
ATOM   2001 C  CB  . ALA A 1 268 ? 40.779 28.099  53.211  1.00 23.18 ?  268 ALA A CB  1 
ATOM   2002 N  N   . ALA A 1 269 ? 38.956 26.312  51.368  1.00 21.44 ?  269 ALA A N   1 
ATOM   2003 C  CA  . ALA A 1 269 ? 38.608 25.856  50.028  1.00 22.06 ?  269 ALA A CA  1 
ATOM   2004 C  C   . ALA A 1 269 ? 37.124 26.050  49.745  1.00 29.12 ?  269 ALA A C   1 
ATOM   2005 O  O   . ALA A 1 269 ? 36.744 26.435  48.634  1.00 32.61 ?  269 ALA A O   1 
ATOM   2006 C  CB  . ALA A 1 269 ? 39.008 24.391  49.854  1.00 22.34 ?  269 ALA A CB  1 
ATOM   2007 N  N   . ALA A 1 270 ? 36.268 25.810  50.743  1.00 24.43 ?  270 ALA A N   1 
ATOM   2008 C  CA  . ALA A 1 270 ? 34.838 26.002  50.557  1.00 30.41 ?  270 ALA A CA  1 
ATOM   2009 C  C   . ALA A 1 270 ? 34.473 27.476  50.436  1.00 36.02 ?  270 ALA A C   1 
ATOM   2010 O  O   . ALA A 1 270 ? 33.379 27.795  49.962  1.00 39.55 ?  270 ALA A O   1 
ATOM   2011 C  CB  . ALA A 1 270 ? 34.073 25.346  51.710  1.00 26.77 ?  270 ALA A CB  1 
ATOM   2012 N  N   . ALA A 1 271 ? 35.366 28.378  50.836  1.00 35.99 ?  271 ALA A N   1 
ATOM   2013 C  CA  . ALA A 1 271 ? 35.156 29.812  50.699  1.00 46.80 ?  271 ALA A CA  1 
ATOM   2014 C  C   . ALA A 1 271 ? 35.945 30.419  49.541  1.00 52.84 ?  271 ALA A C   1 
ATOM   2015 O  O   . ALA A 1 271 ? 35.974 31.646  49.403  1.00 62.01 ?  271 ALA A O   1 
ATOM   2016 C  CB  . ALA A 1 271 ? 35.517 30.520  52.007  1.00 47.38 ?  271 ALA A CB  1 
ATOM   2017 N  N   . ARG A 1 272 ? 36.582 29.596  48.709  1.00 51.93 ?  272 ARG A N   1 
ATOM   2018 C  CA  . ARG A 1 272 ? 37.349 30.092  47.563  1.00 56.69 ?  272 ARG A CA  1 
ATOM   2019 C  C   . ARG A 1 272 ? 36.444 30.737  46.516  1.00 59.00 ?  272 ARG A C   1 
ATOM   2020 O  O   . ARG A 1 272 ? 35.219 30.735  46.646  1.00 59.29 ?  272 ARG A O   1 
ATOM   2021 C  CB  . ARG A 1 272 ? 38.161 28.960  46.920  1.00 50.42 ?  272 ARG A CB  1 
ATOM   2022 C  CG  . ARG A 1 272 ? 39.592 28.831  47.447  1.00 56.83 ?  272 ARG A CG  1 
ATOM   2023 C  CD  . ARG A 1 272 ? 40.346 27.660  46.803  1.00 50.22 ?  272 ARG A CD  1 
ATOM   2024 N  NE  . ARG A 1 272 ? 41.221 26.988  47.765  1.00 51.49 ?  272 ARG A NE  1 
ATOM   2025 C  CZ  . ARG A 1 272 ? 41.805 25.804  47.574  1.00 46.26 ?  272 ARG A CZ  1 
ATOM   2026 N  NH1 . ARG A 1 272 ? 41.625 25.126  46.437  1.00 32.36 ?  272 ARG A NH1 1 
ATOM   2027 N  NH2 . ARG A 1 272 ? 42.579 25.295  48.529  1.00 24.55 ?  272 ARG A NH2 1 
ATOM   2028 N  N   . MET B 1 1   ? 41.676 0.963   70.945  1.00 34.41 ?  1   MET B N   1 
ATOM   2029 C  CA  . MET B 1 1   ? 42.334 1.444   72.146  1.00 30.19 ?  1   MET B CA  1 
ATOM   2030 C  C   . MET B 1 1   ? 43.445 0.506   72.565  1.00 24.15 ?  1   MET B C   1 
ATOM   2031 O  O   . MET B 1 1   ? 43.529 0.112   73.717  1.00 23.94 ?  1   MET B O   1 
ATOM   2032 C  CB  . MET B 1 1   ? 41.336 1.607   73.293  1.00 38.55 ?  1   MET B CB  1 
ATOM   2033 C  CG  . MET B 1 1   ? 40.678 2.979   73.344  1.00 48.76 ?  1   MET B CG  1 
ATOM   2034 S  SD  . MET B 1 1   ? 39.916 3.331   74.942  1.00 72.24 ?  1   MET B SD  1 
ATOM   2035 C  CE  . MET B 1 1   ? 38.511 2.240   74.881  1.00 54.19 ?  1   MET B CE  1 
ATOM   2036 N  N   . ILE B 1 2   ? 44.304 0.158   71.613  1.00 25.89 ?  2   ILE B N   1 
ATOM   2037 C  CA  . ILE B 1 2   ? 45.478 -0.667  71.868  1.00 22.35 ?  2   ILE B CA  1 
ATOM   2038 C  C   . ILE B 1 2   ? 46.709 0.227   71.973  1.00 20.12 ?  2   ILE B C   1 
ATOM   2039 O  O   . ILE B 1 2   ? 46.977 1.032   71.071  1.00 22.27 ?  2   ILE B O   1 
ATOM   2040 C  CB  . ILE B 1 2   ? 45.655 -1.716  70.760  1.00 20.89 ?  2   ILE B CB  1 
ATOM   2041 C  CG1 . ILE B 1 2   ? 44.529 -2.747  70.797  1.00 22.06 ?  2   ILE B CG1 1 
ATOM   2042 C  CG2 . ILE B 1 2   ? 46.996 -2.385  70.883  1.00 19.13 ?  2   ILE B CG2 1 
ATOM   2043 C  CD1 . ILE B 1 2   ? 44.488 -3.649  69.571  1.00 23.51 ?  2   ILE B CD1 1 
ATOM   2044 N  N   . ASP B 1 3   ? 47.460 0.081   73.072  1.00 18.71 ?  3   ASP B N   1 
ATOM   2045 C  CA  . ASP B 1 3   ? 48.792 0.670   73.237  1.00 20.10 ?  3   ASP B CA  1 
ATOM   2046 C  C   . ASP B 1 3   ? 49.830 -0.398  72.908  1.00 19.41 ?  3   ASP B C   1 
ATOM   2047 O  O   . ASP B 1 3   ? 50.072 -1.290  73.726  1.00 20.94 ?  3   ASP B O   1 
ATOM   2048 C  CB  . ASP B 1 3   ? 49.029 1.132   74.675  1.00 24.42 ?  3   ASP B CB  1 
ATOM   2049 C  CG  . ASP B 1 3   ? 48.581 2.546   74.940  1.00 32.31 ?  3   ASP B CG  1 
ATOM   2050 O  OD1 . ASP B 1 3   ? 48.111 3.229   74.005  1.00 35.09 ?  3   ASP B OD1 1 
ATOM   2051 O  OD2 . ASP B 1 3   ? 48.708 2.968   76.120  1.00 32.25 -1 3   ASP B OD2 1 
ATOM   2052 N  N   . LEU B 1 4   ? 50.493 -0.283  71.759  1.00 14.54 ?  4   LEU B N   1 
ATOM   2053 C  CA  . LEU B 1 4   ? 51.468 -1.279  71.329  1.00 13.73 ?  4   LEU B CA  1 
ATOM   2054 C  C   . LEU B 1 4   ? 52.892 -0.823  71.675  1.00 14.55 ?  4   LEU B C   1 
ATOM   2055 O  O   . LEU B 1 4   ? 53.362 0.203   71.163  1.00 18.70 ?  4   LEU B O   1 
ATOM   2056 C  CB  . LEU B 1 4   ? 51.316 -1.532  69.828  1.00 14.10 ?  4   LEU B CB  1 
ATOM   2057 C  CG  . LEU B 1 4   ? 52.364 -2.471  69.221  1.00 14.66 ?  4   LEU B CG  1 
ATOM   2058 C  CD1 . LEU B 1 4   ? 52.321 -3.855  69.867  1.00 18.22 ?  4   LEU B CD1 1 
ATOM   2059 C  CD2 . LEU B 1 4   ? 52.183 -2.554  67.701  1.00 14.94 ?  4   LEU B CD2 1 
ATOM   2060 N  N   . ILE B 1 5   ? 53.574 -1.584  72.545  1.00 14.50 ?  5   ILE B N   1 
ATOM   2061 C  CA  . ILE B 1 5   ? 54.941 -1.319  72.994  1.00 14.66 ?  5   ILE B CA  1 
ATOM   2062 C  C   . ILE B 1 5   ? 55.795 -2.523  72.617  1.00 15.96 ?  5   ILE B C   1 
ATOM   2063 O  O   . ILE B 1 5   ? 55.415 -3.661  72.899  1.00 14.62 ?  5   ILE B O   1 
ATOM   2064 C  CB  . ILE B 1 5   ? 54.998 -1.078  74.518  1.00 16.43 ?  5   ILE B CB  1 
ATOM   2065 C  CG1 . ILE B 1 5   ? 54.071 0.072   74.916  1.00 19.91 ?  5   ILE B CG1 1 
ATOM   2066 C  CG2 . ILE B 1 5   ? 56.420 -0.868  74.985  1.00 16.59 ?  5   ILE B CG2 1 
ATOM   2067 C  CD1 . ILE B 1 5   ? 53.771 0.097   76.397  1.00 20.75 ?  5   ILE B CD1 1 
ATOM   2068 N  N   . VAL B 1 6   ? 56.961 -2.280  72.025  1.00 13.83 ?  6   VAL B N   1 
ATOM   2069 C  CA  . VAL B 1 6   ? 57.782 -3.342  71.442  1.00 13.44 ?  6   VAL B CA  1 
ATOM   2070 C  C   . VAL B 1 6   ? 59.196 -3.232  71.987  1.00 13.71 ?  6   VAL B C   1 
ATOM   2071 O  O   . VAL B 1 6   ? 59.850 -2.201  71.793  1.00 16.80 ?  6   VAL B O   1 
ATOM   2072 C  CB  . VAL B 1 6   ? 57.826 -3.246  69.909  1.00 13.11 ?  6   VAL B CB  1 
ATOM   2073 C  CG1 . VAL B 1 6   ? 58.540 -4.470  69.317  1.00 15.12 ?  6   VAL B CG1 1 
ATOM   2074 C  CG2 . VAL B 1 6   ? 56.438 -3.038  69.341  1.00 16.32 ?  6   VAL B CG2 1 
ATOM   2075 N  N   . SER B 1 7   ? 59.697 -4.302  72.607  1.00 13.27 ?  7   SER B N   1 
ATOM   2076 C  CA  . SER B 1 7   ? 61.081 -4.276  73.079  1.00 13.99 ?  7   SER B CA  1 
ATOM   2077 C  C   . SER B 1 7   ? 61.992 -4.726  71.945  1.00 14.65 ?  7   SER B C   1 
ATOM   2078 O  O   . SER B 1 7   ? 61.700 -5.715  71.257  1.00 16.37 ?  7   SER B O   1 
ATOM   2079 C  CB  . SER B 1 7   ? 61.274 -5.158  74.314  1.00 16.93 ?  7   SER B CB  1 
ATOM   2080 O  OG  . SER B 1 7   ? 62.665 -5.401  74.516  1.00 19.58 ?  7   SER B OG  1 
ATOM   2081 N  N   . GLN B 1 8   ? 63.064 -3.950  71.715  1.00 16.41 ?  8   GLN B N   1 
ATOM   2082 C  CA  . GLN B 1 8   ? 64.074 -4.261  70.713  1.00 16.09 ?  8   GLN B CA  1 
ATOM   2083 C  C   . GLN B 1 8   ? 65.472 -4.270  71.325  1.00 17.51 ?  8   GLN B C   1 
ATOM   2084 O  O   . GLN B 1 8   ? 66.459 -4.348  70.584  1.00 21.58 ?  8   GLN B O   1 
ATOM   2085 C  CB  . GLN B 1 8   ? 64.004 -3.253  69.556  1.00 17.24 ?  8   GLN B CB  1 
ATOM   2086 C  CG  . GLN B 1 8   ? 62.749 -3.392  68.683  1.00 15.92 ?  8   GLN B CG  1 
ATOM   2087 C  CD  . GLN B 1 8   ? 62.789 -4.659  67.825  1.00 16.54 ?  8   GLN B CD  1 
ATOM   2088 O  OE1 . GLN B 1 8   ? 63.329 -4.660  66.716  1.00 19.24 ?  8   GLN B OE1 1 
ATOM   2089 N  NE2 . GLN B 1 8   ? 62.232 -5.748  68.344  1.00 14.71 ?  8   GLN B NE2 1 
ATOM   2090 N  N   . GLY B 1 9   ? 65.582 -4.169  72.648  1.00 16.53 ?  9   GLY B N   1 
ATOM   2091 C  CA  . GLY B 1 9   ? 66.858 -4.275  73.331  1.00 20.19 ?  9   GLY B CA  1 
ATOM   2092 C  C   . GLY B 1 9   ? 67.097 -5.696  73.803  1.00 18.99 ?  9   GLY B C   1 
ATOM   2093 O  O   . GLY B 1 9   ? 66.158 -6.420  74.142  1.00 17.71 ?  9   GLY B O   1 
ATOM   2094 N  N   . ARG B 1 10  ? 68.363 -6.106  73.802  1.00 17.74 ?  10  ARG B N   1 
ATOM   2095 C  CA  . ARG B 1 10  ? 68.696 -7.430  74.311  1.00 16.00 ?  10  ARG B CA  1 
ATOM   2096 C  C   . ARG B 1 10  ? 68.344 -7.526  75.791  1.00 15.36 ?  10  ARG B C   1 
ATOM   2097 O  O   . ARG B 1 10  ? 68.757 -6.689  76.599  1.00 17.36 ?  10  ARG B O   1 
ATOM   2098 C  CB  . ARG B 1 10  ? 70.179 -7.755  74.125  1.00 18.19 ?  10  ARG B CB  1 
ATOM   2099 C  CG  . ARG B 1 10  ? 70.465 -9.187  74.577  1.00 21.05 ?  10  ARG B CG  1 
ATOM   2100 C  CD  . ARG B 1 10  ? 71.866 -9.719  74.259  1.00 19.20 ?  10  ARG B CD  1 
ATOM   2101 N  NE  . ARG B 1 10  ? 71.964 -11.101 74.724  1.00 20.21 ?  10  ARG B NE  1 
ATOM   2102 C  CZ  . ARG B 1 10  ? 72.607 -11.490 75.821  1.00 18.80 ?  10  ARG B CZ  1 
ATOM   2103 N  NH1 . ARG B 1 10  ? 73.273 -10.602 76.560  1.00 22.58 ?  10  ARG B NH1 1 
ATOM   2104 N  NH2 . ARG B 1 10  ? 72.609 -12.772 76.149  1.00 21.23 ?  10  ARG B NH2 1 
ATOM   2105 N  N   . VAL B 1 11  ? 67.576 -8.558  76.145  1.00 16.92 ?  11  VAL B N   1 
ATOM   2106 C  CA  . VAL B 1 11  ? 67.410 -8.924  77.547  1.00 16.89 ?  11  VAL B CA  1 
ATOM   2107 C  C   . VAL B 1 11  ? 67.713 -10.412 77.657  1.00 19.28 ?  11  VAL B C   1 
ATOM   2108 O  O   . VAL B 1 11  ? 66.806 -11.251 77.613  1.00 17.65 ?  11  VAL B O   1 
ATOM   2109 C  CB  . VAL B 1 11  ? 66.005 -8.577  78.086  1.00 16.87 ?  11  VAL B CB  1 
ATOM   2110 C  CG1 . VAL B 1 11  ? 65.959 -8.754  79.610  1.00 18.19 ?  11  VAL B CG1 1 
ATOM   2111 C  CG2 . VAL B 1 11  ? 65.632 -7.144  77.726  1.00 19.10 ?  11  VAL B CG2 1 
ATOM   2112 N  N   . ALA B 1 12  ? 69.005 -10.745 77.725  1.00 17.45 ?  12  ALA B N   1 
ATOM   2113 C  CA  . ALA B 1 12  ? 69.528 -12.092 77.926  1.00 19.07 ?  12  ALA B CA  1 
ATOM   2114 C  C   . ALA B 1 12  ? 69.305 -13.037 76.744  1.00 16.29 ?  12  ALA B C   1 
ATOM   2115 O  O   . ALA B 1 12  ? 69.524 -14.251 76.900  1.00 18.64 ?  12  ALA B O   1 
ATOM   2116 C  CB  . ALA B 1 12  ? 68.958 -12.735 79.204  1.00 17.83 ?  12  ALA B CB  1 
ATOM   2117 N  N   . ASP B 1 13  ? 68.917 -12.527 75.556  1.00 16.19 ?  13  ASP B N   1 
ATOM   2118 C  CA  . ASP B 1 13  ? 68.618 -13.395 74.415  1.00 19.41 ?  13  ASP B CA  1 
ATOM   2119 C  C   . ASP B 1 13  ? 69.759 -14.368 74.150  1.00 18.53 ?  13  ASP B C   1 
ATOM   2120 O  O   . ASP B 1 13  ? 70.913 -13.955 73.969  1.00 19.90 ?  13  ASP B O   1 
ATOM   2121 C  CB  . ASP B 1 13  ? 68.389 -12.600 73.118  1.00 18.87 ?  13  ASP B CB  1 
ATOM   2122 C  CG  . ASP B 1 13  ? 67.439 -11.426 73.260  1.00 17.59 ?  13  ASP B CG  1 
ATOM   2123 O  OD1 . ASP B 1 13  ? 67.442 -10.748 74.303  1.00 18.91 ?  13  ASP B OD1 1 
ATOM   2124 O  OD2 . ASP B 1 13  ? 66.728 -11.141 72.263  1.00 19.58 -1 13  ASP B OD2 1 
ATOM   2125 N  N   . ARG B 1 14  ? 69.416 -15.647 74.052  1.00 17.88 ?  14  ARG B N   1 
ATOM   2126 C  CA  . ARG B 1 14  ? 70.363 -16.670 73.630  1.00 18.03 ?  14  ARG B CA  1 
ATOM   2127 C  C   . ARG B 1 14  ? 70.135 -17.144 72.203  1.00 25.27 ?  14  ARG B C   1 
ATOM   2128 O  O   . ARG B 1 14  ? 71.044 -17.734 71.611  1.00 27.59 ?  14  ARG B O   1 
ATOM   2129 C  CB  . ARG B 1 14  ? 70.298 -17.867 74.589  1.00 22.59 ?  14  ARG B CB  1 
ATOM   2130 C  CG  . ARG B 1 14  ? 70.740 -17.482 75.998  1.00 23.06 ?  14  ARG B CG  1 
ATOM   2131 C  CD  . ARG B 1 14  ? 70.979 -18.695 76.864  1.00 24.52 ?  14  ARG B CD  1 
ATOM   2132 N  NE  . ARG B 1 14  ? 71.648 -18.337 78.109  1.00 23.56 ?  14  ARG B NE  1 
ATOM   2133 C  CZ  . ARG B 1 14  ? 71.943 -19.210 79.067  1.00 22.50 ?  14  ARG B CZ  1 
ATOM   2134 N  NH1 . ARG B 1 14  ? 71.621 -20.488 78.929  1.00 25.34 ?  14  ARG B NH1 1 
ATOM   2135 N  NH2 . ARG B 1 14  ? 72.563 -18.797 80.161  1.00 24.00 ?  14  ARG B NH2 1 
ATOM   2136 N  N   . ALA B 1 15  ? 68.961 -16.891 71.636  1.00 20.48 ?  15  ALA B N   1 
ATOM   2137 C  CA  . ALA B 1 15  ? 68.655 -17.210 70.250  1.00 21.26 ?  15  ALA B CA  1 
ATOM   2138 C  C   . ALA B 1 15  ? 68.813 -15.965 69.378  1.00 20.83 ?  15  ALA B C   1 
ATOM   2139 O  O   . ALA B 1 15  ? 68.749 -14.828 69.851  1.00 21.32 ?  15  ALA B O   1 
ATOM   2140 C  CB  . ALA B 1 15  ? 67.241 -17.790 70.122  1.00 25.59 ?  15  ALA B CB  1 
ATOM   2141 N  N   . ALA B 1 16  ? 69.031 -16.200 68.080  1.00 22.70 ?  16  ALA B N   1 
ATOM   2142 C  CA  . ALA B 1 16  ? 69.456 -15.140 67.174  1.00 20.29 ?  16  ALA B CA  1 
ATOM   2143 C  C   . ALA B 1 16  ? 68.320 -14.232 66.703  1.00 16.19 ?  16  ALA B C   1 
ATOM   2144 O  O   . ALA B 1 16  ? 68.581 -13.077 66.335  1.00 19.59 ?  16  ALA B O   1 
ATOM   2145 C  CB  . ALA B 1 16  ? 70.151 -15.763 65.952  1.00 17.14 ?  16  ALA B CB  1 
ATOM   2146 N  N   . TRP B 1 17  ? 67.072 -14.701 66.725  1.00 18.54 ?  17  TRP B N   1 
ATOM   2147 C  CA  . TRP B 1 17  ? 66.012 -14.019 65.991  1.00 17.20 ?  17  TRP B CA  1 
ATOM   2148 C  C   . TRP B 1 17  ? 64.831 -13.642 66.875  1.00 16.89 ?  17  TRP B C   1 
ATOM   2149 O  O   . TRP B 1 17  ? 63.714 -13.491 66.376  1.00 16.77 ?  17  TRP B O   1 
ATOM   2150 C  CB  . TRP B 1 17  ? 65.517 -14.874 64.823  1.00 17.26 ?  17  TRP B CB  1 
ATOM   2151 C  CG  . TRP B 1 17  ? 66.594 -15.481 63.980  1.00 21.08 ?  17  TRP B CG  1 
ATOM   2152 C  CD1 . TRP B 1 17  ? 67.542 -14.825 63.267  1.00 23.13 ?  17  TRP B CD1 1 
ATOM   2153 C  CD2 . TRP B 1 17  ? 66.811 -16.881 63.768  1.00 23.20 ?  17  TRP B CD2 1 
ATOM   2154 N  NE1 . TRP B 1 17  ? 68.352 -15.737 62.623  1.00 20.41 ?  17  TRP B NE1 1 
ATOM   2155 C  CE2 . TRP B 1 17  ? 67.919 -17.003 62.916  1.00 23.22 ?  17  TRP B CE2 1 
ATOM   2156 C  CE3 . TRP B 1 17  ? 66.174 -18.044 64.220  1.00 24.35 ?  17  TRP B CE3 1 
ATOM   2157 C  CZ2 . TRP B 1 17  ? 68.404 -18.250 62.496  1.00 23.52 ?  17  TRP B CZ2 1 
ATOM   2158 C  CZ3 . TRP B 1 17  ? 66.653 -19.275 63.806  1.00 24.60 ?  17  TRP B CZ3 1 
ATOM   2159 C  CH2 . TRP B 1 17  ? 67.763 -19.366 62.957  1.00 25.01 ?  17  TRP B CH2 1 
ATOM   2160 N  N   . MET B 1 18  ? 65.057 -13.460 68.176  1.00 15.36 ?  18  MET B N   1 
ATOM   2161 C  CA  . MET B 1 18  ? 63.917 -13.081 69.011  1.00 14.60 ?  18  MET B CA  1 
ATOM   2162 C  C   . MET B 1 18  ? 63.649 -11.584 68.958  1.00 14.77 ?  18  MET B C   1 
ATOM   2163 O  O   . MET B 1 18  ? 62.487 -11.175 69.072  1.00 13.48 ?  18  MET B O   1 
ATOM   2164 C  CB  . MET B 1 18  ? 64.110 -13.604 70.437  1.00 20.48 ?  18  MET B CB  1 
ATOM   2165 C  CG  . MET B 1 18  ? 63.500 -15.030 70.585  1.00 22.19 ?  18  MET B CG  1 
ATOM   2166 S  SD  . MET B 1 18  ? 63.782 -15.728 72.207  1.00 35.42 ?  18  MET B SD  1 
ATOM   2167 C  CE  . MET B 1 18  ? 65.538 -15.395 72.249  1.00 15.69 ?  18  MET B CE  1 
ATOM   2168 N  N   . ILE B 1 19  ? 64.659 -10.753 68.699  1.00 13.22 ?  19  ILE B N   1 
ATOM   2169 C  CA  . ILE B 1 19  ? 64.390 -9.336  68.463  1.00 12.51 ?  19  ILE B CA  1 
ATOM   2170 C  C   . ILE B 1 19  ? 63.692 -9.147  67.112  1.00 16.58 ?  19  ILE B C   1 
ATOM   2171 O  O   . ILE B 1 19  ? 62.708 -8.401  66.998  1.00 14.19 ?  19  ILE B O   1 
ATOM   2172 C  CB  . ILE B 1 19  ? 65.698 -8.521  68.584  1.00 15.07 ?  19  ILE B CB  1 
ATOM   2173 C  CG1 . ILE B 1 19  ? 66.123 -8.450  70.054  1.00 15.04 ?  19  ILE B CG1 1 
ATOM   2174 C  CG2 . ILE B 1 19  ? 65.550 -7.136  67.968  1.00 14.43 ?  19  ILE B CG2 1 
ATOM   2175 C  CD1 . ILE B 1 19  ? 67.485 -7.790  70.270  1.00 19.65 ?  19  ILE B CD1 1 
ATOM   2176 N  N   . GLU B 1 20  ? 64.148 -9.869  66.083  1.00 14.76 ?  20  GLU B N   1 
ATOM   2177 C  CA  . GLU B 1 20  ? 63.450 -9.844  64.799  1.00 15.53 ?  20  GLU B CA  1 
ATOM   2178 C  C   . GLU B 1 20  ? 62.041 -10.407 64.911  1.00 13.89 ?  20  GLU B C   1 
ATOM   2179 O  O   . GLU B 1 20  ? 61.106 -9.898  64.270  1.00 14.32 ?  20  GLU B O   1 
ATOM   2180 C  CB  . GLU B 1 20  ? 64.246 -10.630 63.760  1.00 16.75 ?  20  GLU B CB  1 
ATOM   2181 C  CG  . GLU B 1 20  ? 65.457 -9.896  63.239  1.00 17.82 ?  20  GLU B CG  1 
ATOM   2182 C  CD  . GLU B 1 20  ? 66.015 -10.580 62.005  1.00 25.13 ?  20  GLU B CD  1 
ATOM   2183 O  OE1 . GLU B 1 20  ? 65.248 -10.788 61.042  1.00 19.20 ?  20  GLU B OE1 1 
ATOM   2184 O  OE2 . GLU B 1 20  ? 67.221 -10.920 62.002  1.00 39.48 -1 20  GLU B OE2 1 
ATOM   2185 N  N   . GLY B 1 21  ? 61.875 -11.484 65.695  1.00 14.18 ?  21  GLY B N   1 
ATOM   2186 C  CA  . GLY B 1 21  ? 60.549 -12.055 65.882  1.00 13.33 ?  21  GLY B CA  1 
ATOM   2187 C  C   . GLY B 1 21  ? 59.584 -11.086 66.537  1.00 13.52 ?  21  GLY B C   1 
ATOM   2188 O  O   . GLY B 1 21  ? 58.415 -11.011 66.155  1.00 12.81 ?  21  GLY B O   1 
ATOM   2189 N  N   . ALA B 1 22  ? 60.061 -10.335 67.528  1.00 12.99 ?  22  ALA B N   1 
ATOM   2190 C  CA  . ALA B 1 22  ? 59.221 -9.313  68.143  1.00 11.72 ?  22  ALA B CA  1 
ATOM   2191 C  C   . ALA B 1 22  ? 58.864 -8.217  67.144  1.00 11.95 ?  22  ALA B C   1 
ATOM   2192 O  O   . ALA B 1 22  ? 57.704 -7.787  67.069  1.00 14.24 ?  22  ALA B O   1 
ATOM   2193 C  CB  . ALA B 1 22  ? 59.927 -8.732  69.368  1.00 12.86 ?  22  ALA B CB  1 
ATOM   2194 N  N   . ALA B 1 23  ? 59.842 -7.761  66.345  1.00 12.64 ?  23  ALA B N   1 
ATOM   2195 C  CA  . ALA B 1 23  ? 59.538 -6.737  65.356  1.00 12.07 ?  23  ALA B CA  1 
ATOM   2196 C  C   . ALA B 1 23  ? 58.508 -7.234  64.342  1.00 12.76 ?  23  ALA B C   1 
ATOM   2197 O  O   . ALA B 1 23  ? 57.599 -6.487  63.946  1.00 13.88 ?  23  ALA B O   1 
ATOM   2198 C  CB  . ALA B 1 23  ? 60.823 -6.312  64.643  1.00 14.44 ?  23  ALA B CB  1 
ATOM   2199 N  N   . ARG B 1 24  ? 58.630 -8.489  63.916  1.00 11.92 ?  24  ARG B N   1 
ATOM   2200 C  CA  . ARG B 1 24  ? 57.729 -9.013  62.903  1.00 10.87 ?  24  ARG B CA  1 
ATOM   2201 C  C   . ARG B 1 24  ? 56.317 -9.187  63.460  1.00 13.26 ?  24  ARG B C   1 
ATOM   2202 O  O   . ARG B 1 24  ? 55.337 -8.944  62.749  1.00 13.31 ?  24  ARG B O   1 
ATOM   2203 C  CB  . ARG B 1 24  ? 58.286 -10.331 62.342  1.00 12.07 ?  24  ARG B CB  1 
ATOM   2204 C  CG  . ARG B 1 24  ? 57.392 -10.970 61.282  1.00 14.45 ?  24  ARG B CG  1 
ATOM   2205 C  CD  . ARG B 1 24  ? 57.248 -10.053 60.038  1.00 14.79 ?  24  ARG B CD  1 
ATOM   2206 N  NE  . ARG B 1 24  ? 56.484 -10.696 58.975  1.00 18.47 ?  24  ARG B NE  1 
ATOM   2207 C  CZ  . ARG B 1 24  ? 55.166 -10.643 58.862  1.00 19.65 ?  24  ARG B CZ  1 
ATOM   2208 N  NH1 . ARG B 1 24  ? 54.441 -9.983  59.769  1.00 17.41 ?  24  ARG B NH1 1 
ATOM   2209 N  NH2 . ARG B 1 24  ? 54.572 -11.257 57.841  1.00 22.05 ?  24  ARG B NH2 1 
ATOM   2210 N  N   . THR B 1 25  ? 56.196 -9.639  64.720  1.00 12.26 ?  25  THR B N   1 
ATOM   2211 C  CA  . THR B 1 25  ? 54.887 -9.723  65.368  1.00 10.75 ?  25  THR B CA  1 
ATOM   2212 C  C   . THR B 1 25  ? 54.263 -8.341  65.493  1.00 11.36 ?  25  THR B C   1 
ATOM   2213 O  O   . THR B 1 25  ? 53.074 -8.151  65.211  1.00 11.84 ?  25  THR B O   1 
ATOM   2214 C  CB  . THR B 1 25  ? 55.023 -10.347 66.760  1.00 11.65 ?  25  THR B CB  1 
ATOM   2215 O  OG1 . THR B 1 25  ? 55.589 -11.657 66.667  1.00 13.34 ?  25  THR B OG1 1 
ATOM   2216 C  CG2 . THR B 1 25  ? 53.662 -10.452 67.453  1.00 12.76 ?  25  THR B CG2 1 
ATOM   2217 N  N   . ALA B 1 26  ? 55.052 -7.371  65.946  1.00 12.13 ?  26  ALA B N   1 
ATOM   2218 C  CA  . ALA B 1 26  ? 54.554 -6.007  66.066  1.00 12.28 ?  26  ALA B CA  1 
ATOM   2219 C  C   . ALA B 1 26  ? 54.097 -5.454  64.714  1.00 11.81 ?  26  ALA B C   1 
ATOM   2220 O  O   . ALA B 1 26  ? 53.047 -4.812  64.620  1.00 11.73 ?  26  ALA B O   1 
ATOM   2221 C  CB  . ALA B 1 26  ? 55.631 -5.122  66.690  1.00 14.13 ?  26  ALA B CB  1 
ATOM   2222 N  N   . ARG B 1 27  ? 54.850 -5.709  63.638  1.00 11.16 ?  27  ARG B N   1 
ATOM   2223 C  CA  . ARG B 1 27  ? 54.409 -5.205  62.338  1.00 13.23 ?  27  ARG B CA  1 
ATOM   2224 C  C   . ARG B 1 27  ? 53.096 -5.850  61.897  1.00 13.40 ?  27  ARG B C   1 
ATOM   2225 O  O   . ARG B 1 27  ? 52.258 -5.198  61.261  1.00 14.28 ?  27  ARG B O   1 
ATOM   2226 C  CB  . ARG B 1 27  ? 55.488 -5.447  61.282  1.00 14.78 ?  27  ARG B CB  1 
ATOM   2227 C  CG  . ARG B 1 27  ? 55.319 -4.578  60.032  1.00 23.77 ?  27  ARG B CG  1 
ATOM   2228 C  CD  . ARG B 1 27  ? 55.392 -3.070  60.338  1.00 29.21 ?  27  ARG B CD  1 
ATOM   2229 N  NE  . ARG B 1 27  ? 55.719 -2.301  59.141  1.00 39.35 ?  27  ARG B NE  1 
ATOM   2230 C  CZ  . ARG B 1 27  ? 56.880 -1.684  58.932  1.00 31.66 ?  27  ARG B CZ  1 
ATOM   2231 N  NH1 . ARG B 1 27  ? 57.832 -1.715  59.855  1.00 40.00 ?  27  ARG B NH1 1 
ATOM   2232 N  NH2 . ARG B 1 27  ? 57.084 -1.023  57.801  1.00 44.56 ?  27  ARG B NH2 1 
ATOM   2233 N  N   . ALA B 1 28  ? 52.914 -7.141  62.200  1.00 13.25 ?  28  ALA B N   1 
ATOM   2234 C  CA  . ALA B 1 28  ? 51.665 -7.807  61.869  1.00 13.31 ?  28  ALA B CA  1 
ATOM   2235 C  C   . ALA B 1 28  ? 50.500 -7.167  62.609  1.00 11.88 ?  28  ALA B C   1 
ATOM   2236 O  O   . ALA B 1 28  ? 49.419 -6.974  62.039  1.00 13.36 ?  28  ALA B O   1 
ATOM   2237 C  CB  . ALA B 1 28  ? 51.761 -9.287  62.215  1.00 15.28 ?  28  ALA B CB  1 
ATOM   2238 N  N   . LEU B 1 29  ? 50.713 -6.801  63.874  1.00 10.96 ?  29  LEU B N   1 
ATOM   2239 C  CA  . LEU B 1 29  ? 49.660 -6.137  64.634  1.00 12.54 ?  29  LEU B CA  1 
ATOM   2240 C  C   . LEU B 1 29  ? 49.404 -4.741  64.095  1.00 11.86 ?  29  LEU B C   1 
ATOM   2241 O  O   . LEU B 1 29  ? 48.245 -4.304  64.020  1.00 12.11 ?  29  LEU B O   1 
ATOM   2242 C  CB  . LEU B 1 29  ? 50.034 -6.072  66.110  1.00 13.46 ?  29  LEU B CB  1 
ATOM   2243 C  CG  . LEU B 1 29  ? 50.012 -7.422  66.828  1.00 10.41 ?  29  LEU B CG  1 
ATOM   2244 C  CD1 . LEU B 1 29  ? 50.665 -7.296  68.202  1.00 12.18 ?  29  LEU B CD1 1 
ATOM   2245 C  CD2 . LEU B 1 29  ? 48.564 -7.881  66.997  1.00 13.03 ?  29  LEU B CD2 1 
ATOM   2246 N  N   . GLU B 1 30  ? 50.470 -4.034  63.691  1.00 11.58 ?  30  GLU B N   1 
ATOM   2247 C  CA  . GLU B 1 30  ? 50.291 -2.710  63.099  1.00 11.52 ?  30  GLU B CA  1 
ATOM   2248 C  C   . GLU B 1 30  ? 49.425 -2.783  61.848  1.00 12.21 ?  30  GLU B C   1 
ATOM   2249 O  O   . GLU B 1 30  ? 48.527 -1.953  61.655  1.00 14.41 ?  30  GLU B O   1 
ATOM   2250 C  CB  . GLU B 1 30  ? 51.656 -2.099  62.771  1.00 12.29 ?  30  GLU B CB  1 
ATOM   2251 C  CG  . GLU B 1 30  ? 52.481 -1.758  64.008  1.00 12.52 ?  30  GLU B CG  1 
ATOM   2252 C  CD  . GLU B 1 30  ? 53.829 -1.136  63.668  1.00 14.70 ?  30  GLU B CD  1 
ATOM   2253 O  OE1 . GLU B 1 30  ? 54.176 -1.095  62.471  1.00 16.88 ?  30  GLU B OE1 1 
ATOM   2254 O  OE2 . GLU B 1 30  ? 54.513 -0.687  64.615  1.00 18.10 -1 30  GLU B OE2 1 
ATOM   2255 N  N   . GLU B 1 31  ? 49.689 -3.774  60.991  1.00 11.77 ?  31  GLU B N   1 
ATOM   2256 C  CA  . GLU B 1 31  ? 48.935 -3.953  59.751  1.00 15.84 ?  31  GLU B CA  1 
ATOM   2257 C  C   . GLU B 1 31  ? 47.502 -4.390  60.021  1.00 13.87 ?  31  GLU B C   1 
ATOM   2258 O  O   . GLU B 1 31  ? 46.577 -3.938  59.339  1.00 16.12 ?  31  GLU B O   1 
ATOM   2259 C  CB  . GLU B 1 31  ? 49.652 -4.964  58.847  1.00 14.02 ?  31  GLU B CB  1 
ATOM   2260 C  CG  . GLU B 1 31  ? 51.017 -4.463  58.375  1.00 15.60 ?  31  GLU B CG  1 
ATOM   2261 C  CD  . GLU B 1 31  ? 51.836 -5.489  57.602  1.00 19.22 ?  31  GLU B CD  1 
ATOM   2262 O  OE1 . GLU B 1 31  ? 51.435 -6.673  57.503  1.00 22.09 ?  31  GLU B OE1 1 
ATOM   2263 O  OE2 . GLU B 1 31  ? 52.904 -5.070  57.106  1.00 21.81 -1 31  GLU B OE2 1 
ATOM   2264 N  N   . ARG B 1 32  ? 47.293 -5.271  61.010  1.00 12.66 ?  32  ARG B N   1 
ATOM   2265 C  CA  . ARG B 1 32  ? 45.942 -5.768  61.256  1.00 12.90 ?  32  ARG B CA  1 
ATOM   2266 C  C   . ARG B 1 32  ? 45.055 -4.708  61.903  1.00 13.88 ?  32  ARG B C   1 
ATOM   2267 O  O   . ARG B 1 32  ? 43.851 -4.677  61.629  1.00 14.59 ?  32  ARG B O   1 
ATOM   2268 C  CB  . ARG B 1 32  ? 46.006 -7.028  62.126  1.00 13.47 ?  32  ARG B CB  1 
ATOM   2269 C  CG  . ARG B 1 32  ? 44.641 -7.572  62.568  1.00 16.15 ?  32  ARG B CG  1 
ATOM   2270 C  CD  . ARG B 1 32  ? 43.896 -8.172  61.392  1.00 21.70 ?  32  ARG B CD  1 
ATOM   2271 N  NE  . ARG B 1 32  ? 44.312 -9.550  61.153  1.00 25.89 ?  32  ARG B NE  1 
ATOM   2272 C  CZ  . ARG B 1 32  ? 45.118 -9.939  60.172  1.00 27.20 ?  32  ARG B CZ  1 
ATOM   2273 N  NH1 . ARG B 1 32  ? 45.599 -9.051  59.299  1.00 30.82 ?  32  ARG B NH1 1 
ATOM   2274 N  NH2 . ARG B 1 32  ? 45.428 -11.227 60.049  1.00 27.42 ?  32  ARG B NH2 1 
ATOM   2275 N  N   . TYR B 1 33  ? 45.624 -3.817  62.726  1.00 11.64 ?  33  TYR B N   1 
ATOM   2276 C  CA  . TYR B 1 33  ? 44.820 -2.910  63.541  1.00 11.45 ?  33  TYR B CA  1 
ATOM   2277 C  C   . TYR B 1 33  ? 45.031 -1.439  63.224  1.00 14.58 ?  33  TYR B C   1 
ATOM   2278 O  O   . TYR B 1 33  ? 44.395 -0.587  63.861  1.00 15.79 ?  33  TYR B O   1 
ATOM   2279 C  CB  . TYR B 1 33  ? 45.069 -3.184  65.035  1.00 12.07 ?  33  TYR B CB  1 
ATOM   2280 C  CG  . TYR B 1 33  ? 44.508 -4.537  65.421  1.00 13.97 ?  33  TYR B CG  1 
ATOM   2281 C  CD1 . TYR B 1 33  ? 43.132 -4.745  65.437  1.00 14.33 ?  33  TYR B CD1 1 
ATOM   2282 C  CD2 . TYR B 1 33  ? 45.333 -5.617  65.694  1.00 12.54 ?  33  TYR B CD2 1 
ATOM   2283 C  CE1 . TYR B 1 33  ? 42.592 -6.003  65.760  1.00 14.82 ?  33  TYR B CE1 1 
ATOM   2284 C  CE2 . TYR B 1 33  ? 44.807 -6.868  66.006  1.00 12.65 ?  33  TYR B CE2 1 
ATOM   2285 C  CZ  . TYR B 1 33  ? 43.439 -7.051  66.055  1.00 13.21 ?  33  TYR B CZ  1 
ATOM   2286 O  OH  . TYR B 1 33  ? 42.945 -8.300  66.355  1.00 15.62 ?  33  TYR B OH  1 
ATOM   2287 N  N   . GLY B 1 34  ? 45.864 -1.117  62.242  1.00 13.29 ?  34  GLY B N   1 
ATOM   2288 C  CA  . GLY B 1 34  ? 46.095 0.278   61.907  1.00 14.31 ?  34  GLY B CA  1 
ATOM   2289 C  C   . GLY B 1 34  ? 46.892 1.028   62.947  1.00 14.51 ?  34  GLY B C   1 
ATOM   2290 O  O   . GLY B 1 34  ? 46.595 2.201   63.224  1.00 18.37 ?  34  GLY B O   1 
ATOM   2291 N  N   . LEU B 1 35  ? 47.918 0.399   63.507  1.00 13.09 ?  35  LEU B N   1 
ATOM   2292 C  CA  . LEU B 1 35  ? 48.680 0.961   64.619  1.00 13.68 ?  35  LEU B CA  1 
ATOM   2293 C  C   . LEU B 1 35  ? 50.091 1.334   64.179  1.00 14.08 ?  35  LEU B C   1 
ATOM   2294 O  O   . LEU B 1 35  ? 50.594 0.882   63.149  1.00 13.47 ?  35  LEU B O   1 
ATOM   2295 C  CB  . LEU B 1 35  ? 48.774 -0.038  65.787  1.00 16.90 ?  35  LEU B CB  1 
ATOM   2296 C  CG  . LEU B 1 35  ? 47.490 -0.726  66.222  1.00 16.13 ?  35  LEU B CG  1 
ATOM   2297 C  CD1 . LEU B 1 35  ? 47.794 -1.800  67.266  1.00 18.00 ?  35  LEU B CD1 1 
ATOM   2298 C  CD2 . LEU B 1 35  ? 46.521 0.297   66.768  1.00 18.34 ?  35  LEU B CD2 1 
ATOM   2299 N  N   . LYS B 1 36  ? 50.747 2.121   65.029  1.00 14.34 ?  36  LYS B N   1 
ATOM   2300 C  CA  . LYS B 1 36  ? 52.197 2.299   64.991  1.00 13.29 ?  36  LYS B CA  1 
ATOM   2301 C  C   . LYS B 1 36  ? 52.720 2.043   66.393  1.00 14.44 ?  36  LYS B C   1 
ATOM   2302 O  O   . LYS B 1 36  ? 52.332 2.735   67.341  1.00 18.87 ?  36  LYS B O   1 
ATOM   2303 C  CB  . LYS B 1 36  ? 52.600 3.701   64.499  1.00 13.59 ?  36  LYS B CB  1 
ATOM   2304 C  CG  . LYS B 1 36  ? 54.119 3.943   64.517  1.00 11.27 ?  36  LYS B CG  1 
ATOM   2305 C  CD  . LYS B 1 36  ? 54.896 3.130   63.494  1.00 15.47 ?  36  LYS B CD  1 
ATOM   2306 C  CE  . LYS B 1 36  ? 56.393 3.356   63.738  1.00 16.57 ?  36  LYS B CE  1 
ATOM   2307 N  NZ  . LYS B 1 36  ? 57.255 2.937   62.609  1.00 17.44 ?  36  LYS B NZ  1 
ATOM   2308 N  N   . GLY B 1 37  ? 53.580 1.030   66.528  1.00 13.86 ?  37  GLY B N   1 
ATOM   2309 C  CA  . GLY B 1 37  ? 54.114 0.703   67.829  1.00 17.14 ?  37  GLY B CA  1 
ATOM   2310 C  C   . GLY B 1 37  ? 55.134 1.718   68.306  1.00 21.51 ?  37  GLY B C   1 
ATOM   2311 O  O   . GLY B 1 37  ? 55.667 2.523   67.543  1.00 17.18 ?  37  GLY B O   1 
ATOM   2312 N  N   . HIS B 1 38  ? 55.374 1.676   69.609  1.00 18.44 ?  38  HIS B N   1 
ATOM   2313 C  CA  . HIS B 1 38  ? 56.457 2.400   70.253  1.00 22.47 ?  38  HIS B CA  1 
ATOM   2314 C  C   . HIS B 1 38  ? 57.582 1.410   70.549  1.00 20.00 ?  38  HIS B C   1 
ATOM   2315 O  O   . HIS B 1 38  ? 57.381 0.446   71.293  1.00 16.42 ?  38  HIS B O   1 
ATOM   2316 C  CB  . HIS B 1 38  ? 55.931 3.054   71.524  1.00 22.47 ?  38  HIS B CB  1 
ATOM   2317 C  CG  . HIS B 1 38  ? 56.988 3.692   72.365  1.00 24.14 ?  38  HIS B CG  1 
ATOM   2318 N  ND1 . HIS B 1 38  ? 57.982 4.491   71.841  1.00 31.24 ?  38  HIS B ND1 1 
ATOM   2319 C  CD2 . HIS B 1 38  ? 57.208 3.642   73.698  1.00 26.45 ?  38  HIS B CD2 1 
ATOM   2320 C  CE1 . HIS B 1 38  ? 58.762 4.914   72.820  1.00 27.73 ?  38  HIS B CE1 1 
ATOM   2321 N  NE2 . HIS B 1 38  ? 58.314 4.414   73.955  1.00 27.58 ?  38  HIS B NE2 1 
ATOM   2322 N  N   . TYR B 1 39  ? 58.755 1.634   69.956  1.00 18.76 ?  39  TYR B N   1 
ATOM   2323 C  CA  . TYR B 1 39  ? 59.842 0.665   69.977  1.00 20.34 ?  39  TYR B CA  1 
ATOM   2324 C  C   . TYR B 1 39  ? 60.891 1.121   70.978  1.00 20.92 ?  39  TYR B C   1 
ATOM   2325 O  O   . TYR B 1 39  ? 61.336 2.272   70.934  1.00 27.74 ?  39  TYR B O   1 
ATOM   2326 C  CB  . TYR B 1 39  ? 60.441 0.492   68.575  1.00 21.15 ?  39  TYR B CB  1 
ATOM   2327 C  CG  . TYR B 1 39  ? 59.469 -0.170  67.612  1.00 16.01 ?  39  TYR B CG  1 
ATOM   2328 C  CD1 . TYR B 1 39  ? 58.393 0.541   67.078  1.00 19.98 ?  39  TYR B CD1 1 
ATOM   2329 C  CD2 . TYR B 1 39  ? 59.598 -1.505  67.261  1.00 16.30 ?  39  TYR B CD2 1 
ATOM   2330 C  CE1 . TYR B 1 39  ? 57.491 -0.064  66.207  1.00 17.19 ?  39  TYR B CE1 1 
ATOM   2331 C  CE2 . TYR B 1 39  ? 58.695 -2.124  66.395  1.00 17.55 ?  39  TYR B CE2 1 
ATOM   2332 C  CZ  . TYR B 1 39  ? 57.630 -1.393  65.876  1.00 15.84 ?  39  TYR B CZ  1 
ATOM   2333 O  OH  . TYR B 1 39  ? 56.745 -2.012  65.008  1.00 18.70 ?  39  TYR B OH  1 
ATOM   2334 N  N   . VAL B 1 40  ? 61.239 0.237   71.913  1.00 18.22 ?  40  VAL B N   1 
ATOM   2335 C  CA  . VAL B 1 40  ? 62.078 0.578   73.058  1.00 18.76 ?  40  VAL B CA  1 
ATOM   2336 C  C   . VAL B 1 40  ? 63.312 -0.314  73.047  1.00 21.76 ?  40  VAL B C   1 
ATOM   2337 O  O   . VAL B 1 40  ? 63.194 -1.542  72.982  1.00 22.88 ?  40  VAL B O   1 
ATOM   2338 C  CB  . VAL B 1 40  ? 61.305 0.398   74.378  1.00 26.61 ?  40  VAL B CB  1 
ATOM   2339 C  CG1 . VAL B 1 40  ? 62.230 0.521   75.565  1.00 28.22 ?  40  VAL B CG1 1 
ATOM   2340 C  CG2 . VAL B 1 40  ? 60.146 1.383   74.471  1.00 28.62 ?  40  VAL B CG2 1 
ATOM   2341 N  N   . GLY B 1 41  ? 64.489 0.295   73.116  1.00 24.12 ?  41  GLY B N   1 
ATOM   2342 C  CA  . GLY B 1 41  ? 65.702 -0.464  73.329  1.00 24.61 ?  41  GLY B CA  1 
ATOM   2343 C  C   . GLY B 1 41  ? 66.544 -0.568  72.065  1.00 28.20 ?  41  GLY B C   1 
ATOM   2344 O  O   . GLY B 1 41  ? 66.067 -0.393  70.940  1.00 29.51 ?  41  GLY B O   1 
ATOM   2345 N  N   . GLU B 1 42  ? 67.829 -0.878  72.271  1.00 30.27 ?  42  GLU B N   1 
ATOM   2346 C  CA  . GLU B 1 42  ? 68.804 -0.996  71.196  1.00 32.81 ?  42  GLU B CA  1 
ATOM   2347 C  C   . GLU B 1 42  ? 69.190 -2.453  70.985  1.00 22.05 ?  42  GLU B C   1 
ATOM   2348 O  O   . GLU B 1 42  ? 69.593 -3.122  71.948  1.00 29.20 ?  42  GLU B O   1 
ATOM   2349 C  CB  . GLU B 1 42  ? 70.055 -0.172  71.528  1.00 38.19 ?  42  GLU B CB  1 
ATOM   2350 C  CG  . GLU B 1 42  ? 69.772 1.282   71.860  1.00 42.61 ?  42  GLU B CG  1 
ATOM   2351 C  CD  . GLU B 1 42  ? 69.376 2.094   70.643  1.00 53.62 ?  42  GLU B CD  1 
ATOM   2352 O  OE1 . GLU B 1 42  ? 69.366 3.339   70.740  1.00 65.10 ?  42  GLU B OE1 1 
ATOM   2353 O  OE2 . GLU B 1 42  ? 69.082 1.490   69.587  1.00 56.25 -1 42  GLU B OE2 1 
ATOM   2354 N  N   . PRO B 1 43  ? 69.085 -2.977  69.761  1.00 25.84 ?  43  PRO B N   1 
ATOM   2355 C  CA  . PRO B 1 43  ? 69.476 -4.372  69.518  1.00 27.89 ?  43  PRO B CA  1 
ATOM   2356 C  C   . PRO B 1 43  ? 70.950 -4.612  69.816  1.00 30.73 ?  43  PRO B C   1 
ATOM   2357 O  O   . PRO B 1 43  ? 71.791 -3.726  69.660  1.00 30.55 ?  43  PRO B O   1 
ATOM   2358 C  CB  . PRO B 1 43  ? 69.172 -4.574  68.027  1.00 28.31 ?  43  PRO B CB  1 
ATOM   2359 C  CG  . PRO B 1 43  ? 68.136 -3.533  67.711  1.00 31.28 ?  43  PRO B CG  1 
ATOM   2360 C  CD  . PRO B 1 43  ? 68.510 -2.351  68.558  1.00 30.36 ?  43  PRO B CD  1 
ATOM   2361 N  N   . ALA B 1 44  ? 71.251 -5.833  70.248  1.00 25.57 ?  44  ALA B N   1 
ATOM   2362 C  CA  . ALA B 1 44  ? 72.614 -6.282  70.499  1.00 27.90 ?  44  ALA B CA  1 
ATOM   2363 C  C   . ALA B 1 44  ? 72.674 -7.775  70.216  1.00 31.79 ?  44  ALA B C   1 
ATOM   2364 O  O   . ALA B 1 44  ? 71.657 -8.464  70.343  1.00 27.19 ?  44  ALA B O   1 
ATOM   2365 C  CB  . ALA B 1 44  ? 73.062 -5.996  71.940  1.00 25.06 ?  44  ALA B CB  1 
ATOM   2366 N  N   . PRO B 1 45  ? 73.834 -8.292  69.823  1.00 27.76 ?  45  PRO B N   1 
ATOM   2367 C  CA  . PRO B 1 45  ? 73.901 -9.710  69.446  1.00 24.45 ?  45  PRO B CA  1 
ATOM   2368 C  C   . PRO B 1 45  ? 73.603 -10.629 70.623  1.00 21.72 ?  45  PRO B C   1 
ATOM   2369 O  O   . PRO B 1 45  ? 73.900 -10.317 71.780  1.00 21.44 ?  45  PRO B O   1 
ATOM   2370 C  CB  . PRO B 1 45  ? 75.345 -9.882  68.948  1.00 27.52 ?  45  PRO B CB  1 
ATOM   2371 C  CG  . PRO B 1 45  ? 76.087 -8.689  69.464  1.00 32.94 ?  45  PRO B CG  1 
ATOM   2372 C  CD  . PRO B 1 45  ? 75.087 -7.579  69.529  1.00 31.90 ?  45  PRO B CD  1 
ATOM   2373 N  N   . HIS B 1 46  ? 73.016 -11.775 70.299  1.00 22.00 ?  46  HIS B N   1 
ATOM   2374 C  CA  . HIS B 1 46  ? 72.725 -12.795 71.293  1.00 22.84 ?  46  HIS B CA  1 
ATOM   2375 C  C   . HIS B 1 46  ? 74.024 -13.403 71.814  1.00 24.80 ?  46  HIS B C   1 
ATOM   2376 O  O   . HIS B 1 46  ? 75.094 -13.274 71.207  1.00 25.69 ?  46  HIS B O   1 
ATOM   2377 C  CB  . HIS B 1 46  ? 71.832 -13.885 70.695  1.00 21.40 ?  46  HIS B CB  1 
ATOM   2378 C  CG  . HIS B 1 46  ? 72.442 -14.586 69.521  1.00 26.82 ?  46  HIS B CG  1 
ATOM   2379 N  ND1 . HIS B 1 46  ? 72.693 -13.952 68.323  1.00 30.75 ?  46  HIS B ND1 1 
ATOM   2380 C  CD2 . HIS B 1 46  ? 72.859 -15.864 69.365  1.00 31.02 ?  46  HIS B CD2 1 
ATOM   2381 C  CE1 . HIS B 1 46  ? 73.238 -14.810 67.480  1.00 28.32 ?  46  HIS B CE1 1 
ATOM   2382 N  NE2 . HIS B 1 46  ? 73.348 -15.978 68.087  1.00 30.05 ?  46  HIS B NE2 1 
ATOM   2383 N  N   . ALA B 1 47  ? 73.922 -14.071 72.959  1.00 21.93 ?  47  ALA B N   1 
ATOM   2384 C  CA  . ALA B 1 47  ? 75.090 -14.612 73.640  1.00 23.90 ?  47  ALA B CA  1 
ATOM   2385 C  C   . ALA B 1 47  ? 74.637 -15.637 74.666  1.00 28.33 ?  47  ALA B C   1 
ATOM   2386 O  O   . ALA B 1 47  ? 73.515 -15.584 75.174  1.00 25.52 ?  47  ALA B O   1 
ATOM   2387 C  CB  . ALA B 1 47  ? 75.905 -13.511 74.320  1.00 25.23 ?  47  ALA B CB  1 
ATOM   2388 N  N   . ASP B 1 48  ? 75.545 -16.548 74.992  1.00 30.11 ?  48  ASP B N   1 
ATOM   2389 C  CA  . ASP B 1 48  ? 75.278 -17.620 75.949  1.00 33.21 ?  48  ASP B CA  1 
ATOM   2390 C  C   . ASP B 1 48  ? 75.897 -17.261 77.303  1.00 34.44 ?  48  ASP B C   1 
ATOM   2391 O  O   . ASP B 1 48  ? 76.839 -17.894 77.785  1.00 38.91 ?  48  ASP B O   1 
ATOM   2392 C  CB  . ASP B 1 48  ? 75.817 -18.940 75.399  1.00 35.43 ?  48  ASP B CB  1 
ATOM   2393 C  CG  . ASP B 1 48  ? 75.523 -20.123 76.298  1.00 46.97 ?  48  ASP B CG  1 
ATOM   2394 O  OD1 . ASP B 1 48  ? 74.513 -20.080 77.028  1.00 41.31 -1 48  ASP B OD1 1 
ATOM   2395 O  OD2 . ASP B 1 48  ? 76.308 -21.099 76.270  1.00 56.77 ?  48  ASP B OD2 1 
ATOM   2396 N  N   . ASP B 1 49  ? 75.351 -16.216 77.926  1.00 25.18 ?  49  ASP B N   1 
ATOM   2397 C  CA  . ASP B 1 49  ? 75.932 -15.681 79.149  1.00 23.97 ?  49  ASP B CA  1 
ATOM   2398 C  C   . ASP B 1 49  ? 75.056 -15.962 80.369  1.00 23.98 ?  49  ASP B C   1 
ATOM   2399 O  O   . ASP B 1 49  ? 73.856 -16.230 80.263  1.00 26.07 ?  49  ASP B O   1 
ATOM   2400 C  CB  . ASP B 1 49  ? 76.220 -14.174 79.022  1.00 25.41 ?  49  ASP B CB  1 
ATOM   2401 C  CG  . ASP B 1 49  ? 75.012 -13.356 78.556  1.00 23.01 ?  49  ASP B CG  1 
ATOM   2402 O  OD1 . ASP B 1 49  ? 73.922 -13.932 78.335  1.00 26.34 ?  49  ASP B OD1 1 
ATOM   2403 O  OD2 . ASP B 1 49  ? 75.168 -12.116 78.420  1.00 25.71 -1 49  ASP B OD2 1 
ATOM   2404 N  N   . ASP B 1 50  ? 75.695 -15.924 81.537  1.00 25.13 ?  50  ASP B N   1 
ATOM   2405 C  CA  . ASP B 1 50  ? 74.999 -16.151 82.797  1.00 24.13 ?  50  ASP B CA  1 
ATOM   2406 C  C   . ASP B 1 50  ? 74.084 -14.972 83.115  1.00 22.25 ?  50  ASP B C   1 
ATOM   2407 O  O   . ASP B 1 50  ? 74.329 -13.834 82.701  1.00 23.63 ?  50  ASP B O   1 
ATOM   2408 C  CB  . ASP B 1 50  ? 76.022 -16.354 83.918  1.00 20.25 ?  50  ASP B CB  1 
ATOM   2409 C  CG  . ASP B 1 50  ? 75.394 -16.785 85.238  1.00 20.07 ?  50  ASP B CG  1 
ATOM   2410 O  OD1 . ASP B 1 50  ? 74.899 -17.924 85.319  1.00 26.87 ?  50  ASP B OD1 1 
ATOM   2411 O  OD2 . ASP B 1 50  ? 75.430 -15.979 86.186  1.00 26.63 -1 50  ASP B OD2 1 
ATOM   2412 N  N   . TRP B 1 51  ? 73.003 -15.257 83.859  1.00 23.37 ?  51  TRP B N   1 
ATOM   2413 C  CA  . TRP B 1 51  ? 72.078 -14.202 84.270  1.00 24.05 ?  51  TRP B CA  1 
ATOM   2414 C  C   . TRP B 1 51  ? 72.802 -13.044 84.942  1.00 21.19 ?  51  TRP B C   1 
ATOM   2415 O  O   . TRP B 1 51  ? 72.416 -11.884 84.774  1.00 23.31 ?  51  TRP B O   1 
ATOM   2416 C  CB  . TRP B 1 51  ? 71.005 -14.763 85.214  1.00 21.91 ?  51  TRP B CB  1 
ATOM   2417 C  CG  . TRP B 1 51  ? 71.540 -15.141 86.573  1.00 24.76 ?  51  TRP B CG  1 
ATOM   2418 C  CD1 . TRP B 1 51  ? 71.979 -16.370 86.964  1.00 24.67 ?  51  TRP B CD1 1 
ATOM   2419 C  CD2 . TRP B 1 51  ? 71.686 -14.277 87.711  1.00 27.57 ?  51  TRP B CD2 1 
ATOM   2420 N  NE1 . TRP B 1 51  ? 72.412 -16.324 88.276  1.00 26.84 ?  51  TRP B NE1 1 
ATOM   2421 C  CE2 . TRP B 1 51  ? 72.236 -15.051 88.756  1.00 28.91 ?  51  TRP B CE2 1 
ATOM   2422 C  CE3 . TRP B 1 51  ? 71.407 -12.926 87.948  1.00 25.75 ?  51  TRP B CE3 1 
ATOM   2423 C  CZ2 . TRP B 1 51  ? 72.508 -14.518 90.015  1.00 29.99 ?  51  TRP B CZ2 1 
ATOM   2424 C  CZ3 . TRP B 1 51  ? 71.685 -12.396 89.197  1.00 34.29 ?  51  TRP B CZ3 1 
ATOM   2425 C  CH2 . TRP B 1 51  ? 72.230 -13.193 90.215  1.00 31.39 ?  51  TRP B CH2 1 
ATOM   2426 N  N   . SER B 1 52  ? 73.855 -13.344 85.723  1.00 25.66 ?  52  SER B N   1 
ATOM   2427 C  CA  . SER B 1 52  ? 74.584 -12.312 86.456  1.00 25.42 ?  52  SER B CA  1 
ATOM   2428 C  C   . SER B 1 52  ? 75.292 -11.331 85.534  1.00 27.46 ?  52  SER B C   1 
ATOM   2429 O  O   . SER B 1 52  ? 75.638 -10.228 85.972  1.00 28.74 ?  52  SER B O   1 
ATOM   2430 C  CB  . SER B 1 52  ? 75.616 -12.954 87.387  1.00 27.02 ?  52  SER B CB  1 
ATOM   2431 O  OG  . SER B 1 52  ? 76.450 -13.849 86.665  1.00 32.58 ?  52  SER B OG  1 
ATOM   2432 N  N   . VAL B 1 53  ? 75.527 -11.720 84.286  1.00 25.72 ?  53  VAL B N   1 
ATOM   2433 C  CA  . VAL B 1 53  ? 76.108 -10.846 83.280  1.00 26.11 ?  53  VAL B CA  1 
ATOM   2434 C  C   . VAL B 1 53  ? 75.030 -10.194 82.424  1.00 24.32 ?  53  VAL B C   1 
ATOM   2435 O  O   . VAL B 1 53  ? 75.068 -8.988  82.182  1.00 26.96 ?  53  VAL B O   1 
ATOM   2436 C  CB  . VAL B 1 53  ? 77.102 -11.650 82.415  1.00 27.33 ?  53  VAL B CB  1 
ATOM   2437 C  CG1 . VAL B 1 53  ? 77.664 -10.792 81.289  1.00 31.45 ?  53  VAL B CG1 1 
ATOM   2438 C  CG2 . VAL B 1 53  ? 78.222 -12.223 83.288  1.00 27.76 ?  53  VAL B CG2 1 
ATOM   2439 N  N   . ALA B 1 54  ? 74.033 -10.982 82.012  1.00 23.66 ?  54  ALA B N   1 
ATOM   2440 C  CA  . ALA B 1 54  ? 73.002 -10.472 81.113  1.00 22.92 ?  54  ALA B CA  1 
ATOM   2441 C  C   . ALA B 1 54  ? 72.087 -9.475  81.812  1.00 20.43 ?  54  ALA B C   1 
ATOM   2442 O  O   . ALA B 1 54  ? 71.638 -8.498  81.201  1.00 21.40 ?  54  ALA B O   1 
ATOM   2443 C  CB  . ALA B 1 54  ? 72.192 -11.640 80.548  1.00 18.64 ?  54  ALA B CB  1 
ATOM   2444 N  N   . LEU B 1 55  ? 71.782 -9.710  83.092  1.00 21.61 ?  55  LEU B N   1 
ATOM   2445 C  CA  . LEU B 1 55  ? 70.838 -8.832  83.777  1.00 24.34 ?  55  LEU B CA  1 
ATOM   2446 C  C   . LEU B 1 55  ? 71.345 -7.397  83.879  1.00 20.30 ?  55  LEU B C   1 
ATOM   2447 O  O   . LEU B 1 55  ? 70.609 -6.481  83.472  1.00 23.28 ?  55  LEU B O   1 
ATOM   2448 C  CB  . LEU B 1 55  ? 70.484 -9.437  85.141  1.00 22.83 ?  55  LEU B CB  1 
ATOM   2449 C  CG  . LEU B 1 55  ? 69.513 -8.693  86.053  1.00 22.51 ?  55  LEU B CG  1 
ATOM   2450 C  CD1 . LEU B 1 55  ? 68.187 -8.394  85.354  1.00 21.41 ?  55  LEU B CD1 1 
ATOM   2451 C  CD2 . LEU B 1 55  ? 69.285 -9.520  87.315  1.00 23.37 ?  55  LEU B CD2 1 
ATOM   2452 N  N   . PRO B 1 56  ? 72.553 -7.113  84.392  1.00 22.77 ?  56  PRO B N   1 
ATOM   2453 C  CA  . PRO B 1 56  ? 73.000 -5.709  84.405  1.00 27.07 ?  56  PRO B CA  1 
ATOM   2454 C  C   . PRO B 1 56  ? 73.176 -5.114  83.017  1.00 22.82 ?  56  PRO B C   1 
ATOM   2455 O  O   . PRO B 1 56  ? 72.938 -3.911  82.836  1.00 26.90 ?  56  PRO B O   1 
ATOM   2456 C  CB  . PRO B 1 56  ? 74.333 -5.765  85.172  1.00 26.04 ?  56  PRO B CB  1 
ATOM   2457 C  CG  . PRO B 1 56  ? 74.767 -7.176  85.109  1.00 27.02 ?  56  PRO B CG  1 
ATOM   2458 C  CD  . PRO B 1 56  ? 73.501 -7.989  85.103  1.00 25.56 ?  56  PRO B CD  1 
ATOM   2459 N  N   . GLN B 1 57  ? 73.555 -5.924  82.023  1.00 23.48 ?  57  GLN B N   1 
ATOM   2460 C  CA  . GLN B 1 57  ? 73.650 -5.414  80.659  1.00 23.53 ?  57  GLN B CA  1 
ATOM   2461 C  C   . GLN B 1 57  ? 72.297 -4.938  80.137  1.00 28.75 ?  57  GLN B C   1 
ATOM   2462 O  O   . GLN B 1 57  ? 72.237 -3.991  79.344  1.00 26.72 ?  57  GLN B O   1 
ATOM   2463 C  CB  . GLN B 1 57  ? 74.237 -6.482  79.736  1.00 27.63 ?  57  GLN B CB  1 
ATOM   2464 C  CG  . GLN B 1 57  ? 75.706 -6.780  80.031  1.00 38.56 ?  57  GLN B CG  1 
ATOM   2465 C  CD  . GLN B 1 57  ? 76.330 -7.744  79.039  1.00 45.87 ?  57  GLN B CD  1 
ATOM   2466 O  OE1 . GLN B 1 57  ? 77.451 -8.222  79.238  1.00 47.94 ?  57  GLN B OE1 1 
ATOM   2467 N  NE2 . GLN B 1 57  ? 75.609 -8.032  77.959  1.00 46.44 ?  57  GLN B NE2 1 
ATOM   2468 N  N   . ALA B 1 58  ? 71.204 -5.562  80.587  1.00 23.96 ?  58  ALA B N   1 
ATOM   2469 C  CA  . ALA B 1 58  ? 69.862 -5.231  80.129  1.00 26.73 ?  58  ALA B CA  1 
ATOM   2470 C  C   . ALA B 1 58  ? 69.233 -4.064  80.889  1.00 22.67 ?  58  ALA B C   1 
ATOM   2471 O  O   . ALA B 1 58  ? 68.085 -3.708  80.604  1.00 22.77 ?  58  ALA B O   1 
ATOM   2472 C  CB  . ALA B 1 58  ? 68.960 -6.471  80.238  1.00 19.91 ?  58  ALA B CB  1 
ATOM   2473 N  N   . ARG B 1 59  ? 69.958 -3.434  81.820  1.00 23.65 ?  59  ARG B N   1 
ATOM   2474 C  CA  . ARG B 1 59  ? 69.321 -2.473  82.723  1.00 24.07 ?  59  ARG B CA  1 
ATOM   2475 C  C   . ARG B 1 59  ? 68.620 -1.341  81.970  1.00 23.72 ?  59  ARG B C   1 
ATOM   2476 O  O   . ARG B 1 59  ? 67.484 -0.985  82.296  1.00 25.88 ?  59  ARG B O   1 
ATOM   2477 C  CB  . ARG B 1 59  ? 70.339 -1.901  83.715  1.00 24.65 ?  59  ARG B CB  1 
ATOM   2478 C  CG  . ARG B 1 59  ? 69.757 -0.744  84.529  1.00 30.26 ?  59  ARG B CG  1 
ATOM   2479 C  CD  . ARG B 1 59  ? 70.467 -0.527  85.860  1.00 39.99 ?  59  ARG B CD  1 
ATOM   2480 N  NE  . ARG B 1 59  ? 69.988 -1.441  86.897  1.00 47.92 ?  59  ARG B NE  1 
ATOM   2481 C  CZ  . ARG B 1 59  ? 68.884 -1.251  87.618  1.00 43.13 ?  59  ARG B CZ  1 
ATOM   2482 N  NH1 . ARG B 1 59  ? 68.130 -0.175  87.420  1.00 39.47 ?  59  ARG B NH1 1 
ATOM   2483 N  NH2 . ARG B 1 59  ? 68.531 -2.141  88.539  1.00 40.46 ?  59  ARG B NH2 1 
ATOM   2484 N  N   . GLU B 1 60  ? 69.274 -0.741  80.967  1.00 24.25 ?  60  GLU B N   1 
ATOM   2485 C  CA  . GLU B 1 60  ? 68.652 0.435   80.356  1.00 25.83 ?  60  GLU B CA  1 
ATOM   2486 C  C   . GLU B 1 60  ? 67.410 0.056   79.553  1.00 23.02 ?  60  GLU B C   1 
ATOM   2487 O  O   . GLU B 1 60  ? 66.415 0.793   79.559  1.00 24.62 ?  60  GLU B O   1 
ATOM   2488 C  CB  . GLU B 1 60  ? 69.654 1.209   79.492  1.00 35.17 ?  60  GLU B CB  1 
ATOM   2489 C  CG  . GLU B 1 60  ? 70.478 0.375   78.548  1.00 41.93 ?  60  GLU B CG  1 
ATOM   2490 C  CD  . GLU B 1 60  ? 71.864 0.053   79.092  1.00 52.62 ?  60  GLU B CD  1 
ATOM   2491 O  OE1 . GLU B 1 60  ? 71.961 -0.661  80.120  1.00 35.56 ?  60  GLU B OE1 1 
ATOM   2492 O  OE2 . GLU B 1 60  ? 72.859 0.510   78.481  1.00 58.85 -1 60  GLU B OE2 1 
ATOM   2493 N  N   . THR B 1 61  ? 67.430 -1.101  78.891  1.00 25.54 ?  61  THR B N   1 
ATOM   2494 C  CA  . THR B 1 61  ? 66.228 -1.575  78.209  1.00 26.25 ?  61  THR B CA  1 
ATOM   2495 C  C   . THR B 1 61  ? 65.095 -1.823  79.203  1.00 25.06 ?  61  THR B C   1 
ATOM   2496 O  O   . THR B 1 61  ? 63.958 -1.392  78.983  1.00 20.79 ?  61  THR B O   1 
ATOM   2497 C  CB  . THR B 1 61  ? 66.540 -2.845  77.412  1.00 25.67 ?  61  THR B CB  1 
ATOM   2498 O  OG1 . THR B 1 61  ? 67.460 -2.535  76.355  1.00 23.91 ?  61  THR B OG1 1 
ATOM   2499 C  CG2 . THR B 1 61  ? 65.246 -3.444  76.809  1.00 22.37 ?  61  THR B CG2 1 
ATOM   2500 N  N   . LEU B 1 62  ? 65.401 -2.492  80.321  1.00 20.75 ?  62  LEU B N   1 
ATOM   2501 C  CA  . LEU B 1 62  ? 64.369 -2.817  81.307  1.00 22.14 ?  62  LEU B CA  1 
ATOM   2502 C  C   . LEU B 1 62  ? 63.772 -1.561  81.937  1.00 24.51 ?  62  LEU B C   1 
ATOM   2503 O  O   . LEU B 1 62  ? 62.555 -1.484  82.159  1.00 24.32 ?  62  LEU B O   1 
ATOM   2504 C  CB  . LEU B 1 62  ? 64.946 -3.732  82.385  1.00 19.45 ?  62  LEU B CB  1 
ATOM   2505 C  CG  . LEU B 1 62  ? 65.189 -5.154  81.883  1.00 20.98 ?  62  LEU B CG  1 
ATOM   2506 C  CD1 . LEU B 1 62  ? 66.052 -5.951  82.855  1.00 24.12 ?  62  LEU B CD1 1 
ATOM   2507 C  CD2 . LEU B 1 62  ? 63.853 -5.853  81.647  1.00 19.50 ?  62  LEU B CD2 1 
ATOM   2508 N  N   . VAL B 1 63  ? 64.610 -0.560  82.226  1.00 26.16 ?  63  VAL B N   1 
ATOM   2509 C  CA  . VAL B 1 63  ? 64.093 0.686   82.782  1.00 26.27 ?  63  VAL B CA  1 
ATOM   2510 C  C   . VAL B 1 63  ? 63.179 1.376   81.779  1.00 23.44 ?  63  VAL B C   1 
ATOM   2511 O  O   . VAL B 1 63  ? 62.093 1.852   82.132  1.00 26.97 ?  63  VAL B O   1 
ATOM   2512 C  CB  . VAL B 1 63  ? 65.256 1.596   83.222  1.00 29.19 ?  63  VAL B CB  1 
ATOM   2513 C  CG1 . VAL B 1 63  ? 64.726 2.943   83.658  1.00 33.94 ?  63  VAL B CG1 1 
ATOM   2514 C  CG2 . VAL B 1 63  ? 66.028 0.938   84.362  1.00 29.35 ?  63  VAL B CG2 1 
ATOM   2515 N  N   . ALA B 1 64  ? 63.578 1.400   80.503  1.00 25.46 ?  64  ALA B N   1 
ATOM   2516 C  CA  . ALA B 1 64  ? 62.766 2.075   79.496  1.00 22.89 ?  64  ALA B CA  1 
ATOM   2517 C  C   . ALA B 1 64  ? 61.447 1.340   79.262  1.00 23.42 ?  64  ALA B C   1 
ATOM   2518 O  O   . ALA B 1 64  ? 60.407 1.974   79.053  1.00 26.94 ?  64  ALA B O   1 
ATOM   2519 C  CB  . ALA B 1 64  ? 63.559 2.217   78.197  1.00 26.14 ?  64  ALA B CB  1 
ATOM   2520 N  N   . VAL B 1 65  ? 61.463 0.006   79.311  1.00 26.43 ?  65  VAL B N   1 
ATOM   2521 C  CA  . VAL B 1 65  ? 60.215 -0.742  79.186  1.00 21.74 ?  65  VAL B CA  1 
ATOM   2522 C  C   . VAL B 1 65  ? 59.304 -0.468  80.375  1.00 21.95 ?  65  VAL B C   1 
ATOM   2523 O  O   . VAL B 1 65  ? 58.087 -0.299  80.217  1.00 22.75 ?  65  VAL B O   1 
ATOM   2524 C  CB  . VAL B 1 65  ? 60.500 -2.246  79.039  1.00 20.17 ?  65  VAL B CB  1 
ATOM   2525 C  CG1 . VAL B 1 65  ? 59.201 -3.047  79.165  1.00 22.74 ?  65  VAL B CG1 1 
ATOM   2526 C  CG2 . VAL B 1 65  ? 61.181 -2.531  77.715  1.00 23.90 ?  65  VAL B CG2 1 
ATOM   2527 N  N   . ARG B 1 66  ? 59.872 -0.425  81.584  1.00 22.65 ?  66  ARG B N   1 
ATOM   2528 C  CA  . ARG B 1 66  ? 59.057 -0.144  82.761  1.00 21.44 ?  66  ARG B CA  1 
ATOM   2529 C  C   . ARG B 1 66  ? 58.339 1.198   82.643  1.00 24.31 ?  66  ARG B C   1 
ATOM   2530 O  O   . ARG B 1 66  ? 57.158 1.308   82.992  1.00 25.26 ?  66  ARG B O   1 
ATOM   2531 C  CB  . ARG B 1 66  ? 59.921 -0.172  84.023  1.00 26.69 ?  66  ARG B CB  1 
ATOM   2532 C  CG  . ARG B 1 66  ? 59.176 0.359   85.234  1.00 28.37 ?  66  ARG B CG  1 
ATOM   2533 C  CD  . ARG B 1 66  ? 59.953 0.201   86.525  1.00 41.03 ?  66  ARG B CD  1 
ATOM   2534 N  NE  . ARG B 1 66  ? 61.241 0.883   86.520  1.00 41.83 ?  66  ARG B NE  1 
ATOM   2535 C  CZ  . ARG B 1 66  ? 62.413 0.261   86.423  1.00 44.06 ?  66  ARG B CZ  1 
ATOM   2536 N  NH1 . ARG B 1 66  ? 62.462 -1.067  86.300  1.00 32.45 ?  66  ARG B NH1 1 
ATOM   2537 N  NH2 . ARG B 1 66  ? 63.534 0.970   86.442  1.00 37.60 ?  66  ARG B NH2 1 
ATOM   2538 N  N   . GLU B 1 67  ? 59.039 2.232   82.170  1.00 26.45 ?  67  GLU B N   1 
ATOM   2539 C  CA  . GLU B 1 67  ? 58.429 3.554   82.054  1.00 28.87 ?  67  GLU B CA  1 
ATOM   2540 C  C   . GLU B 1 67  ? 57.322 3.571   81.004  1.00 25.66 ?  67  GLU B C   1 
ATOM   2541 O  O   . GLU B 1 67  ? 56.256 4.156   81.230  1.00 27.86 ?  67  GLU B O   1 
ATOM   2542 C  CB  . GLU B 1 67  ? 59.497 4.601   81.736  1.00 33.47 ?  67  GLU B CB  1 
ATOM   2543 C  CG  . GLU B 1 67  ? 60.702 4.544   82.658  1.00 38.61 ?  67  GLU B CG  1 
ATOM   2544 C  CD  . GLU B 1 67  ? 61.798 5.521   82.268  1.00 53.39 ?  67  GLU B CD  1 
ATOM   2545 O  OE1 . GLU B 1 67  ? 62.638 5.841   83.137  1.00 56.39 ?  67  GLU B OE1 1 
ATOM   2546 O  OE2 . GLU B 1 67  ? 61.820 5.968   81.098  1.00 55.27 -1 67  GLU B OE2 1 
ATOM   2547 N  N   . ALA B 1 68  ? 57.556 2.933   79.853  1.00 26.30 ?  68  ALA B N   1 
ATOM   2548 C  CA  . ALA B 1 68  ? 56.519 2.858   78.828  1.00 23.58 ?  68  ALA B CA  1 
ATOM   2549 C  C   . ALA B 1 68  ? 55.322 2.053   79.317  1.00 24.67 ?  68  ALA B C   1 
ATOM   2550 O  O   . ALA B 1 68  ? 54.169 2.458   79.125  1.00 26.48 ?  68  ALA B O   1 
ATOM   2551 C  CB  . ALA B 1 68  ? 57.100 2.257   77.549  1.00 28.84 ?  68  ALA B CB  1 
ATOM   2552 N  N   . ALA B 1 69  ? 55.578 0.919   79.972  1.00 22.68 ?  69  ALA B N   1 
ATOM   2553 C  CA  . ALA B 1 69  ? 54.487 0.110   80.506  1.00 22.42 ?  69  ALA B CA  1 
ATOM   2554 C  C   . ALA B 1 69  ? 53.691 0.871   81.558  1.00 22.86 ?  69  ALA B C   1 
ATOM   2555 O  O   . ALA B 1 69  ? 52.462 0.740   81.634  1.00 25.16 ?  69  ALA B O   1 
ATOM   2556 C  CB  . ALA B 1 69  ? 55.040 -1.191  81.092  1.00 25.10 ?  69  ALA B CB  1 
ATOM   2557 N  N   . THR B 1 70  ? 54.380 1.656   82.393  1.00 23.97 ?  70  THR B N   1 
ATOM   2558 C  CA  . THR B 1 70  ? 53.705 2.373   83.470  1.00 27.09 ?  70  THR B CA  1 
ATOM   2559 C  C   . THR B 1 70  ? 52.712 3.391   82.919  1.00 21.53 ?  70  THR B C   1 
ATOM   2560 O  O   . THR B 1 70  ? 51.554 3.440   83.350  1.00 26.84 ?  70  THR B O   1 
ATOM   2561 C  CB  . THR B 1 70  ? 54.738 3.057   84.372  1.00 29.84 ?  70  THR B CB  1 
ATOM   2562 O  OG1 . THR B 1 70  ? 55.560 2.068   85.007  1.00 27.64 ?  70  THR B OG1 1 
ATOM   2563 C  CG2 . THR B 1 70  ? 54.043 3.866   85.430  1.00 27.42 ?  70  THR B CG2 1 
ATOM   2564 N  N   . GLU B 1 71  ? 53.148 4.211   81.958  1.00 24.51 ?  71  GLU B N   1 
ATOM   2565 C  CA  . GLU B 1 71  ? 52.240 5.189   81.366  1.00 28.11 ?  71  GLU B CA  1 
ATOM   2566 C  C   . GLU B 1 71  ? 51.033 4.501   80.751  1.00 26.89 ?  71  GLU B C   1 
ATOM   2567 O  O   . GLU B 1 71  ? 49.896 4.961   80.907  1.00 28.09 ?  71  GLU B O   1 
ATOM   2568 C  CB  . GLU B 1 71  ? 52.959 6.020   80.304  1.00 32.48 ?  71  GLU B CB  1 
ATOM   2569 C  CG  . GLU B 1 71  ? 54.264 6.649   80.746  1.00 40.46 ?  71  GLU B CG  1 
ATOM   2570 C  CD  . GLU B 1 71  ? 55.165 6.979   79.566  1.00 53.99 ?  71  GLU B CD  1 
ATOM   2571 O  OE1 . GLU B 1 71  ? 56.401 7.036   79.751  1.00 55.21 ?  71  GLU B OE1 1 
ATOM   2572 O  OE2 . GLU B 1 71  ? 54.631 7.176   78.451  1.00 53.14 -1 71  GLU B OE2 1 
ATOM   2573 N  N   . SER B 1 72  ? 51.262 3.388   80.051  1.00 23.85 ?  72  SER B N   1 
ATOM   2574 C  CA  . SER B 1 72  ? 50.155 2.688   79.412  1.00 24.40 ?  72  SER B CA  1 
ATOM   2575 C  C   . SER B 1 72  ? 49.184 2.134   80.449  1.00 26.00 ?  72  SER B C   1 
ATOM   2576 O  O   . SER B 1 72  ? 47.963 2.292   80.319  1.00 25.43 ?  72  SER B O   1 
ATOM   2577 C  CB  . SER B 1 72  ? 50.694 1.564   78.520  1.00 20.88 ?  72  SER B CB  1 
ATOM   2578 O  OG  . SER B 1 72  ? 49.621 0.899   77.880  1.00 21.59 ?  72  SER B OG  1 
ATOM   2579 N  N   . ILE B 1 73  ? 49.708 1.474   81.487  1.00 22.84 ?  73  ILE B N   1 
ATOM   2580 C  CA  . ILE B 1 73  ? 48.834 0.845   82.477  1.00 24.32 ?  73  ILE B CA  1 
ATOM   2581 C  C   . ILE B 1 73  ? 48.045 1.892   83.253  1.00 30.64 ?  73  ILE B C   1 
ATOM   2582 O  O   . ILE B 1 73  ? 46.900 1.645   83.661  1.00 29.91 ?  73  ILE B O   1 
ATOM   2583 C  CB  . ILE B 1 73  ? 49.666 -0.056  83.409  1.00 25.46 ?  73  ILE B CB  1 
ATOM   2584 C  CG1 . ILE B 1 73  ? 50.072 -1.335  82.681  1.00 28.18 ?  73  ILE B CG1 1 
ATOM   2585 C  CG2 . ILE B 1 73  ? 48.895 -0.414  84.666  1.00 32.58 ?  73  ILE B CG2 1 
ATOM   2586 C  CD1 . ILE B 1 73  ? 51.165 -2.097  83.386  1.00 29.21 ?  73  ILE B CD1 1 
ATOM   2587 N  N   . LYS B 1 74  ? 48.628 3.074   83.459  1.00 29.84 ?  74  LYS B N   1 
ATOM   2588 C  CA  . LYS B 1 74  ? 47.920 4.141   84.152  1.00 37.90 ?  74  LYS B CA  1 
ATOM   2589 C  C   . LYS B 1 74  ? 46.923 4.863   83.254  1.00 33.95 ?  74  LYS B C   1 
ATOM   2590 O  O   . LYS B 1 74  ? 46.041 5.561   83.769  1.00 39.94 ?  74  LYS B O   1 
ATOM   2591 C  CB  . LYS B 1 74  ? 48.924 5.128   84.748  1.00 32.69 ?  74  LYS B CB  1 
ATOM   2592 C  CG  . LYS B 1 74  ? 49.376 4.733   86.148  1.00 36.92 ?  74  LYS B CG  1 
ATOM   2593 C  CD  . LYS B 1 74  ? 50.827 5.089   86.417  1.00 34.99 ?  74  LYS B CD  1 
ATOM   2594 C  CE  . LYS B 1 74  ? 51.037 6.588   86.502  1.00 45.40 ?  74  LYS B CE  1 
ATOM   2595 N  NZ  . LYS B 1 74  ? 52.482 6.940   86.640  1.00 53.66 ?  74  LYS B NZ  1 
ATOM   2596 N  N   . GLY B 1 75  ? 47.030 4.698   81.936  1.00 32.40 ?  75  GLY B N   1 
ATOM   2597 C  CA  . GLY B 1 75  ? 46.050 5.215   81.003  1.00 33.24 ?  75  GLY B CA  1 
ATOM   2598 C  C   . GLY B 1 75  ? 44.846 4.302   80.861  1.00 35.98 ?  75  GLY B C   1 
ATOM   2599 O  O   . GLY B 1 75  ? 44.561 3.462   81.717  1.00 34.31 ?  75  GLY B O   1 
ATOM   2600 N  N   . ASP B 1 76  ? 44.133 4.465   79.746  1.00 38.45 ?  76  ASP B N   1 
ATOM   2601 C  CA  . ASP B 1 76  ? 42.874 3.757   79.531  1.00 42.83 ?  76  ASP B CA  1 
ATOM   2602 C  C   . ASP B 1 76  ? 42.931 2.688   78.446  1.00 41.63 ?  76  ASP B C   1 
ATOM   2603 O  O   . ASP B 1 76  ? 41.936 1.983   78.243  1.00 40.08 ?  76  ASP B O   1 
ATOM   2604 C  CB  . ASP B 1 76  ? 41.759 4.751   79.188  1.00 45.73 ?  76  ASP B CB  1 
ATOM   2605 C  CG  . ASP B 1 76  ? 41.401 5.651   80.350  1.00 55.18 ?  76  ASP B CG  1 
ATOM   2606 O  OD1 . ASP B 1 76  ? 41.136 5.126   81.454  1.00 58.11 ?  76  ASP B OD1 1 
ATOM   2607 O  OD2 . ASP B 1 76  ? 41.383 6.885   80.154  1.00 59.65 -1 76  ASP B OD2 1 
ATOM   2608 N  N   . ASN B 1 77  ? 44.045 2.549   77.742  1.00 36.57 ?  77  ASN B N   1 
ATOM   2609 C  CA  . ASN B 1 77  ? 44.114 1.630   76.614  1.00 30.53 ?  77  ASN B CA  1 
ATOM   2610 C  C   . ASN B 1 77  ? 44.449 0.216   77.083  1.00 28.65 ?  77  ASN B C   1 
ATOM   2611 O  O   . ASN B 1 77  ? 44.911 -0.002  78.204  1.00 30.11 ?  77  ASN B O   1 
ATOM   2612 C  CB  . ASN B 1 77  ? 45.159 2.112   75.605  1.00 33.64 ?  77  ASN B CB  1 
ATOM   2613 C  CG  . ASN B 1 77  ? 44.697 3.323   74.812  1.00 39.86 ?  77  ASN B CG  1 
ATOM   2614 O  OD1 . ASN B 1 77  ? 43.509 3.647   74.785  1.00 43.59 ?  77  ASN B OD1 1 
ATOM   2615 N  ND2 . ASN B 1 77  ? 45.638 3.997   74.159  1.00 41.11 ?  77  ASN B ND2 1 
ATOM   2616 N  N   . LEU B 1 78  ? 44.201 -0.757  76.203  1.00 21.53 ?  78  LEU B N   1 
ATOM   2617 C  CA  . LEU B 1 78  ? 44.708 -2.106  76.426  1.00 16.69 ?  78  LEU B CA  1 
ATOM   2618 C  C   . LEU B 1 78  ? 46.213 -2.111  76.170  1.00 17.13 ?  78  LEU B C   1 
ATOM   2619 O  O   . LEU B 1 78  ? 46.657 -1.773  75.069  1.00 19.45 ?  78  LEU B O   1 
ATOM   2620 C  CB  . LEU B 1 78  ? 44.004 -3.104  75.502  1.00 17.54 ?  78  LEU B CB  1 
ATOM   2621 C  CG  . LEU B 1 78  ? 44.554 -4.535  75.598  1.00 13.96 ?  78  LEU B CG  1 
ATOM   2622 C  CD1 . LEU B 1 78  ? 44.157 -5.181  76.938  1.00 17.91 ?  78  LEU B CD1 1 
ATOM   2623 C  CD2 . LEU B 1 78  ? 44.107 -5.397  74.446  1.00 17.19 ?  78  LEU B CD2 1 
ATOM   2624 N  N   . THR B 1 79  ? 46.996 -2.466  77.185  1.00 14.35 ?  79  THR B N   1 
ATOM   2625 C  CA  . THR B 1 79  ? 48.450 -2.472  77.066  1.00 15.41 ?  79  THR B CA  1 
ATOM   2626 C  C   . THR B 1 79  ? 48.875 -3.763  76.375  1.00 12.83 ?  79  THR B C   1 
ATOM   2627 O  O   . THR B 1 79  ? 48.592 -4.852  76.885  1.00 17.51 ?  79  THR B O   1 
ATOM   2628 C  CB  . THR B 1 79  ? 49.098 -2.375  78.448  1.00 16.63 ?  79  THR B CB  1 
ATOM   2629 O  OG1 . THR B 1 79  ? 48.628 -1.196  79.121  1.00 20.53 ?  79  THR B OG1 1 
ATOM   2630 C  CG2 . THR B 1 79  ? 50.615 -2.353  78.348  1.00 16.93 ?  79  THR B CG2 1 
ATOM   2631 N  N   . VAL B 1 80  ? 49.581 -3.657  75.247  1.00 14.11 ?  80  VAL B N   1 
ATOM   2632 C  CA  . VAL B 1 80  ? 50.096 -4.825  74.524  1.00 14.82 ?  80  VAL B CA  1 
ATOM   2633 C  C   . VAL B 1 80  ? 51.602 -4.682  74.382  1.00 12.76 ?  80  VAL B C   1 
ATOM   2634 O  O   . VAL B 1 80  ? 52.089 -3.798  73.661  1.00 14.83 ?  80  VAL B O   1 
ATOM   2635 C  CB  . VAL B 1 80  ? 49.430 -4.999  73.158  1.00 13.04 ?  80  VAL B CB  1 
ATOM   2636 C  CG1 . VAL B 1 80  ? 50.052 -6.189  72.416  1.00 14.46 ?  80  VAL B CG1 1 
ATOM   2637 C  CG2 . VAL B 1 80  ? 47.929 -5.200  73.337  1.00 15.28 ?  80  VAL B CG2 1 
ATOM   2638 N  N   . LEU B 1 81  ? 52.335 -5.542  75.076  1.00 11.15 ?  81  LEU B N   1 
ATOM   2639 C  CA  . LEU B 1 81  ? 53.789 -5.593  75.011  1.00 12.69 ?  81  LEU B CA  1 
ATOM   2640 C  C   . LEU B 1 81  ? 54.213 -6.739  74.110  1.00 15.24 ?  81  LEU B C   1 
ATOM   2641 O  O   . LEU B 1 81  ? 53.835 -7.894  74.346  1.00 14.52 ?  81  LEU B O   1 
ATOM   2642 C  CB  . LEU B 1 81  ? 54.382 -5.781  76.403  1.00 14.53 ?  81  LEU B CB  1 
ATOM   2643 C  CG  . LEU B 1 81  ? 54.236 -4.523  77.243  1.00 20.11 ?  81  LEU B CG  1 
ATOM   2644 C  CD1 . LEU B 1 81  ? 53.826 -4.867  78.650  1.00 23.29 ?  81  LEU B CD1 1 
ATOM   2645 C  CD2 . LEU B 1 81  ? 55.568 -3.785  77.231  1.00 21.10 ?  81  LEU B CD2 1 
ATOM   2646 N  N   . VAL B 1 82  ? 54.996 -6.431  73.081  1.00 12.37 ?  82  VAL B N   1 
ATOM   2647 C  CA  . VAL B 1 82  ? 55.588 -7.460  72.237  1.00 14.91 ?  82  VAL B CA  1 
ATOM   2648 C  C   . VAL B 1 82  ? 57.057 -7.517  72.627  1.00 12.70 ?  82  VAL B C   1 
ATOM   2649 O  O   . VAL B 1 82  ? 57.813 -6.575  72.368  1.00 13.62 ?  82  VAL B O   1 
ATOM   2650 C  CB  . VAL B 1 82  ? 55.390 -7.183  70.738  1.00 11.34 ?  82  VAL B CB  1 
ATOM   2651 C  CG1 . VAL B 1 82  ? 55.993 -8.303  69.928  1.00 14.11 ?  82  VAL B CG1 1 
ATOM   2652 C  CG2 . VAL B 1 82  ? 53.906 -7.106  70.392  1.00 14.63 ?  82  VAL B CG2 1 
ATOM   2653 N  N   . ASN B 1 83  ? 57.442 -8.596  73.296  1.00 13.10 ?  83  ASN B N   1 
ATOM   2654 C  CA  . ASN B 1 83  ? 58.748 -8.688  73.929  1.00 14.64 ?  83  ASN B CA  1 
ATOM   2655 C  C   . ASN B 1 83  ? 59.611 -9.713  73.217  1.00 16.80 ?  83  ASN B C   1 
ATOM   2656 O  O   . ASN B 1 83  ? 59.133 -10.783 72.811  1.00 14.91 ?  83  ASN B O   1 
ATOM   2657 C  CB  . ASN B 1 83  ? 58.597 -9.034  75.412  1.00 15.86 ?  83  ASN B CB  1 
ATOM   2658 C  CG  . ASN B 1 83  ? 57.866 -7.938  76.172  1.00 15.44 ?  83  ASN B CG  1 
ATOM   2659 O  OD1 . ASN B 1 83  ? 57.924 -6.757  75.790  1.00 18.04 ?  83  ASN B OD1 1 
ATOM   2660 N  ND2 . ASN B 1 83  ? 57.168 -8.321  77.233  1.00 18.33 ?  83  ASN B ND2 1 
ATOM   2661 N  N   . ASN B 1 84  ? 60.889 -9.370  73.042  1.00 13.31 ?  84  ASN B N   1 
ATOM   2662 C  CA  . ASN B 1 84  ? 61.799 -10.349 72.462  1.00 12.84 ?  84  ASN B CA  1 
ATOM   2663 C  C   . ASN B 1 84  ? 61.962 -11.568 73.371  1.00 14.65 ?  84  ASN B C   1 
ATOM   2664 O  O   . ASN B 1 84  ? 61.932 -12.710 72.889  1.00 15.39 ?  84  ASN B O   1 
ATOM   2665 C  CB  . ASN B 1 84  ? 63.146 -9.686  72.123  1.00 12.75 ?  84  ASN B CB  1 
ATOM   2666 C  CG  . ASN B 1 84  ? 63.715 -8.844  73.250  1.00 14.07 ?  84  ASN B CG  1 
ATOM   2667 O  OD1 . ASN B 1 84  ? 63.031 -8.003  73.841  1.00 16.87 ?  84  ASN B OD1 1 
ATOM   2668 N  ND2 . ASN B 1 84  ? 65.002 -9.024  73.516  1.00 17.54 ?  84  ASN B ND2 1 
ATOM   2669 N  N   . THR B 1 85  ? 62.106 -11.362 74.687  1.00 15.11 ?  85  THR B N   1 
ATOM   2670 C  CA  . THR B 1 85  ? 62.267 -12.469 75.626  1.00 14.63 ?  85  THR B CA  1 
ATOM   2671 C  C   . THR B 1 85  ? 61.326 -12.327 76.817  1.00 13.86 ?  85  THR B C   1 
ATOM   2672 O  O   . THR B 1 85  ? 60.860 -11.229 77.136  1.00 15.18 ?  85  THR B O   1 
ATOM   2673 C  CB  . THR B 1 85  ? 63.700 -12.550 76.180  1.00 17.63 ?  85  THR B CB  1 
ATOM   2674 O  OG1 . THR B 1 85  ? 63.991 -11.376 76.956  1.00 18.43 ?  85  THR B OG1 1 
ATOM   2675 C  CG2 . THR B 1 85  ? 64.709 -12.694 75.043  1.00 17.36 ?  85  THR B CG2 1 
ATOM   2676 N  N   A CYS B 1 86  ? 61.054 -13.466 77.472  0.48 14.58 ?  86  CYS B N   1 
ATOM   2677 C  CA  A CYS B 1 86  ? 60.283 -13.447 78.716  0.48 15.70 ?  86  CYS B CA  1 
ATOM   2678 C  C   A CYS B 1 86  ? 60.914 -12.532 79.761  0.48 15.67 ?  86  CYS B C   1 
ATOM   2679 O  O   A CYS B 1 86  ? 60.199 -11.935 80.572  0.48 15.19 ?  86  CYS B O   1 
ATOM   2680 C  CB  A CYS B 1 86  ? 60.156 -14.861 79.294  0.48 18.65 ?  86  CYS B CB  1 
ATOM   2681 S  SG  A CYS B 1 86  ? 59.043 -16.015 78.423  0.48 17.15 ?  86  CYS B SG  1 
HETATM 2682 N  N   B CSO B 1 86  ? 61.052 -13.440 77.493  0.25 14.65 ?  86  CSO B N   1 
HETATM 2683 C  CA  B CSO B 1 86  ? 60.269 -13.374 78.726  0.25 15.73 ?  86  CSO B CA  1 
HETATM 2684 C  CB  B CSO B 1 86  ? 60.042 -14.760 79.319  0.25 18.53 ?  86  CSO B CB  1 
HETATM 2685 S  SG  B CSO B 1 86  ? 58.841 -15.660 78.331  0.25 18.34 ?  86  CSO B SG  1 
HETATM 2686 C  C   B CSO B 1 86  ? 60.919 -12.496 79.780  0.25 15.70 ?  86  CSO B C   1 
HETATM 2687 O  O   B CSO B 1 86  ? 60.227 -11.907 80.608  0.25 15.24 ?  86  CSO B O   1 
HETATM 2688 O  OD  B CSO B 1 86  ? 57.916 -16.742 79.389  0.25 17.50 ?  86  CSO B OD  1 
HETATM 2689 N  N   C CSD B 1 86  ? 61.071 -13.442 77.492  0.27 14.65 ?  86  CSD B N   1 
HETATM 2690 C  CA  C CSD B 1 86  ? 60.304 -13.408 78.717  0.27 15.73 ?  86  CSD B CA  1 
HETATM 2691 C  CB  C CSD B 1 86  ? 60.075 -14.812 79.255  0.27 18.56 ?  86  CSD B CB  1 
HETATM 2692 S  SG  C CSD B 1 86  ? 58.841 -15.597 78.289  0.27 18.33 ?  86  CSD B SG  1 
HETATM 2693 C  C   C CSD B 1 86  ? 60.928 -12.586 79.838  0.27 15.68 ?  86  CSD B C   1 
HETATM 2694 O  O   C CSD B 1 86  ? 60.272 -12.112 80.765  0.27 15.39 ?  86  CSD B O   1 
HETATM 2695 O  OD1 C CSD B 1 86  ? 57.888 -14.562 77.901  0.27 16.37 -1 86  CSD B OD1 1 
HETATM 2696 O  OD2 C CSD B 1 86  ? 57.894 -16.185 79.564  0.27 16.29 ?  86  CSD B OD2 1 
ATOM   2697 N  N   . SER B 1 87  ? 62.244 -12.402 79.750  1.00 15.99 ?  87  SER B N   1 
ATOM   2698 C  CA  . SER B 1 87  ? 62.961 -11.628 80.765  1.00 14.53 ?  87  SER B CA  1 
ATOM   2699 C  C   . SER B 1 87  ? 62.568 -10.155 80.782  1.00 16.02 ?  87  SER B C   1 
ATOM   2700 O  O   . SER B 1 87  ? 62.797 -9.481  81.793  1.00 17.37 ?  87  SER B O   1 
ATOM   2701 C  CB  . SER B 1 87  ? 64.472 -11.745 80.559  1.00 17.49 ?  87  SER B CB  1 
ATOM   2702 O  OG  . SER B 1 87  ? 64.913 -13.059 80.808  1.00 21.43 ?  87  SER B OG  1 
ATOM   2703 N  N   . VAL B 1 88  ? 61.991 -9.636  79.693  1.00 14.34 ?  88  VAL B N   1 
ATOM   2704 C  CA  . VAL B 1 88  ? 61.456 -8.274  79.699  1.00 17.18 ?  88  VAL B CA  1 
ATOM   2705 C  C   . VAL B 1 88  ? 60.440 -8.113  80.823  1.00 19.79 ?  88  VAL B C   1 
ATOM   2706 O  O   . VAL B 1 88  ? 60.303 -7.025  81.409  1.00 17.88 ?  88  VAL B O   1 
ATOM   2707 C  CB  . VAL B 1 88  ? 60.845 -7.935  78.317  1.00 17.99 ?  88  VAL B CB  1 
ATOM   2708 C  CG1 . VAL B 1 88  ? 60.155 -6.577  78.331  1.00 19.78 ?  88  VAL B CG1 1 
ATOM   2709 C  CG2 . VAL B 1 88  ? 61.922 -7.972  77.216  1.00 14.93 ?  88  VAL B CG2 1 
ATOM   2710 N  N   . SER B 1 89  ? 59.743 -9.200  81.176  1.00 15.73 ?  89  SER B N   1 
ATOM   2711 C  CA  . SER B 1 89  ? 58.663 -9.117  82.154  1.00 15.66 ?  89  SER B CA  1 
ATOM   2712 C  C   . SER B 1 89  ? 59.161 -8.900  83.573  1.00 16.01 ?  89  SER B C   1 
ATOM   2713 O  O   . SER B 1 89  ? 58.346 -8.562  84.441  1.00 16.64 ?  89  SER B O   1 
ATOM   2714 C  CB  . SER B 1 89  ? 57.792 -10.374 82.087  1.00 15.39 ?  89  SER B CB  1 
ATOM   2715 O  OG  . SER B 1 89  ? 57.206 -10.429 80.791  1.00 19.34 ?  89  SER B OG  1 
ATOM   2716 N  N   . LEU B 1 90  ? 60.463 -9.069  83.819  1.00 15.15 ?  90  LEU B N   1 
ATOM   2717 C  CA  . LEU B 1 90  ? 61.044 -8.637  85.088  1.00 15.85 ?  90  LEU B CA  1 
ATOM   2718 C  C   . LEU B 1 90  ? 60.775 -7.159  85.350  1.00 17.94 ?  90  LEU B C   1 
ATOM   2719 O  O   . LEU B 1 90  ? 60.703 -6.735  86.513  1.00 21.25 ?  90  LEU B O   1 
ATOM   2720 C  CB  . LEU B 1 90  ? 62.548 -8.916  85.086  1.00 15.68 ?  90  LEU B CB  1 
ATOM   2721 C  CG  . LEU B 1 90  ? 62.998 -10.374 85.253  1.00 15.86 ?  90  LEU B CG  1 
ATOM   2722 C  CD1 . LEU B 1 90  ? 64.490 -10.512 84.954  1.00 19.68 ?  90  LEU B CD1 1 
ATOM   2723 C  CD2 . LEU B 1 90  ? 62.676 -10.875 86.659  1.00 18.28 ?  90  LEU B CD2 1 
ATOM   2724 N  N   . ALA B 1 91  ? 60.589 -6.365  84.301  1.00 16.75 ?  91  ALA B N   1 
ATOM   2725 C  CA  . ALA B 1 91  ? 60.284 -4.947  84.470  1.00 19.00 ?  91  ALA B CA  1 
ATOM   2726 C  C   . ALA B 1 91  ? 58.790 -4.656  84.465  1.00 21.27 ?  91  ALA B C   1 
ATOM   2727 O  O   . ALA B 1 91  ? 58.342 -3.710  85.124  1.00 23.09 ?  91  ALA B O   1 
ATOM   2728 C  CB  . ALA B 1 91  ? 60.960 -4.125  83.367  1.00 25.57 ?  91  ALA B CB  1 
ATOM   2729 N  N   . THR B 1 92  ? 57.997 -5.447  83.751  1.00 15.50 ?  92  THR B N   1 
ATOM   2730 C  CA  . THR B 1 92  ? 56.586 -5.128  83.624  1.00 16.87 ?  92  THR B CA  1 
ATOM   2731 C  C   . THR B 1 92  ? 55.736 -5.734  84.736  1.00 16.52 ?  92  THR B C   1 
ATOM   2732 O  O   . THR B 1 92  ? 54.808 -5.080  85.224  1.00 17.73 ?  92  THR B O   1 
ATOM   2733 C  CB  . THR B 1 92  ? 56.072 -5.599  82.267  1.00 17.53 ?  92  THR B CB  1 
ATOM   2734 O  OG1 . THR B 1 92  ? 56.207 -7.015  82.191  1.00 20.44 ?  92  THR B OG1 1 
ATOM   2735 C  CG2 . THR B 1 92  ? 56.893 -4.972  81.156  1.00 22.45 ?  92  THR B CG2 1 
ATOM   2736 N  N   . LEU B 1 93  ? 56.002 -6.969  85.148  1.00 15.92 ?  93  LEU B N   1 
ATOM   2737 C  CA  . LEU B 1 93  ? 55.147 -7.579  86.169  1.00 15.93 ?  93  LEU B CA  1 
ATOM   2738 C  C   . LEU B 1 93  ? 55.133 -6.811  87.494  1.00 18.23 ?  93  LEU B C   1 
ATOM   2739 O  O   . LEU B 1 93  ? 54.061 -6.744  88.120  1.00 17.18 ?  93  LEU B O   1 
ATOM   2740 C  CB  . LEU B 1 93  ? 55.545 -9.048  86.365  1.00 16.26 ?  93  LEU B CB  1 
ATOM   2741 C  CG  . LEU B 1 93  ? 55.205 -9.943  85.154  1.00 15.54 ?  93  LEU B CG  1 
ATOM   2742 C  CD1 . LEU B 1 93  ? 55.782 -11.339 85.332  1.00 16.21 ?  93  LEU B CD1 1 
ATOM   2743 C  CD2 . LEU B 1 93  ? 53.679 -10.004 84.885  1.00 17.29 ?  93  LEU B CD2 1 
ATOM   2744 N  N   . PRO B 1 94  ? 56.233 -6.216  87.975  1.00 17.12 ?  94  PRO B N   1 
ATOM   2745 C  CA  . PRO B 1 94  ? 56.113 -5.382  89.184  1.00 16.66 ?  94  PRO B CA  1 
ATOM   2746 C  C   . PRO B 1 94  ? 55.210 -4.180  89.003  1.00 19.74 ?  94  PRO B C   1 
ATOM   2747 O  O   . PRO B 1 94  ? 54.539 -3.775  89.960  1.00 19.44 ?  94  PRO B O   1 
ATOM   2748 C  CB  . PRO B 1 94  ? 57.565 -4.963  89.456  1.00 18.01 ?  94  PRO B CB  1 
ATOM   2749 C  CG  . PRO B 1 94  ? 58.367 -6.105  88.904  1.00 21.61 ?  94  PRO B CG  1 
ATOM   2750 C  CD  . PRO B 1 94  ? 57.649 -6.477  87.643  1.00 17.12 ?  94  PRO B CD  1 
ATOM   2751 N  N   . VAL B 1 95  ? 55.173 -3.584  87.811  1.00 20.01 ?  95  VAL B N   1 
ATOM   2752 C  CA  . VAL B 1 95  ? 54.243 -2.485  87.570  1.00 21.06 ?  95  VAL B CA  1 
ATOM   2753 C  C   . VAL B 1 95  ? 52.804 -2.978  87.635  1.00 22.25 ?  95  VAL B C   1 
ATOM   2754 O  O   . VAL B 1 95  ? 51.927 -2.322  88.215  1.00 20.31 ?  95  VAL B O   1 
ATOM   2755 C  CB  . VAL B 1 95  ? 54.545 -1.816  86.215  1.00 19.93 ?  95  VAL B CB  1 
ATOM   2756 C  CG1 . VAL B 1 95  ? 53.574 -0.673  85.979  1.00 24.23 ?  95  VAL B CG1 1 
ATOM   2757 C  CG2 . VAL B 1 95  ? 55.994 -1.327  86.156  1.00 21.86 ?  95  VAL B CG2 1 
ATOM   2758 N  N   . VAL B 1 96  ? 52.529 -4.139  87.037  1.00 18.39 ?  96  VAL B N   1 
ATOM   2759 C  CA  . VAL B 1 96  ? 51.172 -4.680  87.074  1.00 21.16 ?  96  VAL B CA  1 
ATOM   2760 C  C   . VAL B 1 96  ? 50.719 -4.870  88.515  1.00 19.42 ?  96  VAL B C   1 
ATOM   2761 O  O   . VAL B 1 96  ? 49.618 -4.460  88.899  1.00 19.60 ?  96  VAL B O   1 
ATOM   2762 C  CB  . VAL B 1 96  ? 51.102 -5.995  86.278  1.00 16.10 ?  96  VAL B CB  1 
ATOM   2763 C  CG1 . VAL B 1 96  ? 49.715 -6.601  86.368  1.00 22.37 ?  96  VAL B CG1 1 
ATOM   2764 C  CG2 . VAL B 1 96  ? 51.480 -5.733  84.830  1.00 16.11 ?  96  VAL B CG2 1 
ATOM   2765 N  N   . ALA B 1 97  ? 51.572 -5.491  89.332  1.00 22.02 ?  97  ALA B N   1 
ATOM   2766 C  CA  . ALA B 1 97  ? 51.212 -5.799  90.710  1.00 18.42 ?  97  ALA B CA  1 
ATOM   2767 C  C   . ALA B 1 97  ? 51.057 -4.534  91.536  1.00 24.35 ?  97  ALA B C   1 
ATOM   2768 O  O   . ALA B 1 97  ? 50.235 -4.492  92.460  1.00 23.32 ?  97  ALA B O   1 
ATOM   2769 C  CB  . ALA B 1 97  ? 52.264 -6.721  91.330  1.00 22.38 ?  97  ALA B CB  1 
ATOM   2770 N  N   . ARG B 1 98  ? 51.815 -3.488  91.203  1.00 20.42 ?  98  ARG B N   1 
ATOM   2771 C  CA  . ARG B 1 98  ? 51.705 -2.230  91.937  1.00 22.36 ?  98  ARG B CA  1 
ATOM   2772 C  C   . ARG B 1 98  ? 50.379 -1.533  91.649  1.00 26.06 ?  98  ARG B C   1 
ATOM   2773 O  O   . ARG B 1 98  ? 49.650 -1.164  92.578  1.00 24.08 ?  98  ARG B O   1 
ATOM   2774 C  CB  . ARG B 1 98  ? 52.888 -1.323  91.593  1.00 25.47 ?  98  ARG B CB  1 
ATOM   2775 C  CG  . ARG B 1 98  ? 53.030 -0.094  92.489  1.00 28.18 ?  98  ARG B CG  1 
ATOM   2776 C  CD  . ARG B 1 98  ? 53.480 1.125   91.683  1.00 36.57 ?  98  ARG B CD  1 
ATOM   2777 N  NE  . ARG B 1 98  ? 54.828 0.980   91.133  1.00 47.23 ?  98  ARG B NE  1 
ATOM   2778 C  CZ  . ARG B 1 98  ? 55.196 1.387   89.918  1.00 46.30 ?  98  ARG B CZ  1 
ATOM   2779 N  NH1 . ARG B 1 98  ? 56.449 1.212   89.512  1.00 45.87 ?  98  ARG B NH1 1 
ATOM   2780 N  NH2 . ARG B 1 98  ? 54.316 1.964   89.102  1.00 39.14 ?  98  ARG B NH2 1 
ATOM   2781 N  N   . GLU B 1 99  ? 50.030 -1.373  90.368  1.00 19.89 ?  99  GLU B N   1 
ATOM   2782 C  CA  . GLU B 1 99  ? 48.843 -0.621  89.979  1.00 21.02 ?  99  GLU B CA  1 
ATOM   2783 C  C   . GLU B 1 99  ? 47.559 -1.438  90.055  1.00 24.91 ?  99  GLU B C   1 
ATOM   2784 O  O   . GLU B 1 99  ? 46.479 -0.851  90.168  1.00 26.69 ?  99  GLU B O   1 
ATOM   2785 C  CB  . GLU B 1 99  ? 49.004 -0.072  88.558  1.00 29.42 ?  99  GLU B CB  1 
ATOM   2786 C  CG  . GLU B 1 99  ? 50.305 0.702   88.327  1.00 29.92 ?  99  GLU B CG  1 
ATOM   2787 C  CD  . GLU B 1 99  ? 50.411 1.969   89.167  1.00 40.83 ?  99  GLU B CD  1 
ATOM   2788 O  OE1 . GLU B 1 99  ? 49.368 2.607   89.428  1.00 35.63 ?  99  GLU B OE1 1 
ATOM   2789 O  OE2 . GLU B 1 99  ? 51.545 2.327   89.561  1.00 41.91 -1 99  GLU B OE2 1 
ATOM   2790 N  N   . HIS B 1 100 ? 47.637 -2.769  89.988  1.00 22.31 ?  100 HIS B N   1 
ATOM   2791 C  CA  . HIS B 1 100 ? 46.469 -3.644  90.092  1.00 22.50 ?  100 HIS B CA  1 
ATOM   2792 C  C   . HIS B 1 100 ? 46.781 -4.754  91.091  1.00 22.93 ?  100 HIS B C   1 
ATOM   2793 O  O   . HIS B 1 100 ? 47.034 -5.903  90.709  1.00 20.91 ?  100 HIS B O   1 
ATOM   2794 C  CB  . HIS B 1 100 ? 46.072 -4.206  88.721  1.00 22.53 ?  100 HIS B CB  1 
ATOM   2795 C  CG  . HIS B 1 100 ? 45.680 -3.157  87.721  1.00 27.32 ?  100 HIS B CG  1 
ATOM   2796 N  ND1 . HIS B 1 100 ? 44.420 -2.596  87.692  1.00 30.10 ?  100 HIS B ND1 1 
ATOM   2797 C  CD2 . HIS B 1 100 ? 46.369 -2.584  86.704  1.00 28.56 ?  100 HIS B CD2 1 
ATOM   2798 C  CE1 . HIS B 1 100 ? 44.354 -1.716  86.709  1.00 33.26 ?  100 HIS B CE1 1 
ATOM   2799 N  NE2 . HIS B 1 100 ? 45.521 -1.690  86.092  1.00 25.43 ?  100 HIS B NE2 1 
ATOM   2800 N  N   . PRO B 1 101 ? 46.766 -4.447  92.393  1.00 21.82 ?  101 PRO B N   1 
ATOM   2801 C  CA  . PRO B 1 101 ? 47.149 -5.459  93.393  1.00 21.82 ?  101 PRO B CA  1 
ATOM   2802 C  C   . PRO B 1 101 ? 46.197 -6.637  93.483  1.00 18.11 ?  101 PRO B C   1 
ATOM   2803 O  O   . PRO B 1 101 ? 46.566 -7.665  94.063  1.00 19.45 ?  101 PRO B O   1 
ATOM   2804 C  CB  . PRO B 1 101 ? 47.176 -4.660  94.706  1.00 24.23 ?  101 PRO B CB  1 
ATOM   2805 C  CG  . PRO B 1 101 ? 46.276 -3.509  94.441  1.00 26.77 ?  101 PRO B CG  1 
ATOM   2806 C  CD  . PRO B 1 101 ? 46.478 -3.142  93.012  1.00 26.88 ?  101 PRO B CD  1 
ATOM   2807 N  N   . ASP B 1 102 ? 44.994 -6.528  92.926  1.00 21.34 ?  102 ASP B N   1 
ATOM   2808 C  CA  . ASP B 1 102 ? 44.060 -7.639  92.857  1.00 22.85 ?  102 ASP B CA  1 
ATOM   2809 C  C   . ASP B 1 102 ? 44.165 -8.428  91.554  1.00 20.93 ?  102 ASP B C   1 
ATOM   2810 O  O   . ASP B 1 102 ? 43.432 -9.411  91.379  1.00 21.88 ?  102 ASP B O   1 
ATOM   2811 C  CB  . ASP B 1 102 ? 42.624 -7.123  93.033  1.00 24.44 ?  102 ASP B CB  1 
ATOM   2812 C  CG  . ASP B 1 102 ? 42.288 -5.970  92.092  1.00 32.61 ?  102 ASP B CG  1 
ATOM   2813 O  OD1 . ASP B 1 102 ? 43.212 -5.325  91.527  1.00 33.23 ?  102 ASP B OD1 1 
ATOM   2814 O  OD2 . ASP B 1 102 ? 41.081 -5.696  91.924  1.00 41.38 -1 102 ASP B OD2 1 
ATOM   2815 N  N   . ALA B 1 103 ? 45.055 -8.029  90.643  1.00 18.71 ?  103 ALA B N   1 
ATOM   2816 C  CA  . ALA B 1 103 ? 45.145 -8.694  89.346  1.00 16.89 ?  103 ALA B CA  1 
ATOM   2817 C  C   . ALA B 1 103 ? 45.696 -10.108 89.472  1.00 17.01 ?  103 ALA B C   1 
ATOM   2818 O  O   . ALA B 1 103 ? 46.597 -10.378 90.266  1.00 20.75 ?  103 ALA B O   1 
ATOM   2819 C  CB  . ALA B 1 103 ? 46.046 -7.902  88.402  1.00 20.57 ?  103 ALA B CB  1 
ATOM   2820 N  N   . VAL B 1 104 ? 45.155 -11.010 88.661  1.00 16.35 ?  104 VAL B N   1 
ATOM   2821 C  CA  . VAL B 1 104 ? 45.706 -12.348 88.489  1.00 16.21 ?  104 VAL B CA  1 
ATOM   2822 C  C   . VAL B 1 104 ? 46.533 -12.368 87.207  1.00 15.74 ?  104 VAL B C   1 
ATOM   2823 O  O   . VAL B 1 104 ? 46.073 -11.903 86.158  1.00 17.75 ?  104 VAL B O   1 
ATOM   2824 C  CB  . VAL B 1 104 ? 44.591 -13.403 88.442  1.00 18.07 ?  104 VAL B CB  1 
ATOM   2825 C  CG1 . VAL B 1 104 ? 45.133 -14.765 88.048  1.00 15.70 ?  104 VAL B CG1 1 
ATOM   2826 C  CG2 . VAL B 1 104 ? 43.907 -13.494 89.812  1.00 20.90 ?  104 VAL B CG2 1 
ATOM   2827 N  N   . VAL B 1 105 ? 47.763 -12.870 87.308  1.00 14.29 ?  105 VAL B N   1 
ATOM   2828 C  CA  . VAL B 1 105 ? 48.668 -13.013 86.165  1.00 13.92 ?  105 VAL B CA  1 
ATOM   2829 C  C   . VAL B 1 105 ? 48.544 -14.431 85.652  1.00 13.93 ?  105 VAL B C   1 
ATOM   2830 O  O   . VAL B 1 105 ? 48.851 -15.391 86.372  1.00 15.16 ?  105 VAL B O   1 
ATOM   2831 C  CB  . VAL B 1 105 ? 50.123 -12.692 86.551  1.00 14.99 ?  105 VAL B CB  1 
ATOM   2832 C  CG1 . VAL B 1 105 ? 51.089 -13.131 85.414  1.00 15.43 ?  105 VAL B CG1 1 
ATOM   2833 C  CG2 . VAL B 1 105 ? 50.266 -11.229 86.839  1.00 15.48 ?  105 VAL B CG2 1 
ATOM   2834 N  N   . LEU B 1 106 ? 48.080 -14.571 84.410  1.00 13.63 ?  106 LEU B N   1 
ATOM   2835 C  CA  . LEU B 1 106 ? 48.093 -15.852 83.720  1.00 12.41 ?  106 LEU B CA  1 
ATOM   2836 C  C   . LEU B 1 106 ? 49.420 -15.930 82.999  1.00 13.12 ?  106 LEU B C   1 
ATOM   2837 O  O   . LEU B 1 106 ? 49.652 -15.167 82.056  1.00 13.50 ?  106 LEU B O   1 
ATOM   2838 C  CB  . LEU B 1 106 ? 46.935 -15.958 82.737  1.00 10.47 ?  106 LEU B CB  1 
ATOM   2839 C  CG  . LEU B 1 106 ? 45.544 -15.865 83.346  1.00 13.23 ?  106 LEU B CG  1 
ATOM   2840 C  CD1 . LEU B 1 106 ? 44.479 -15.891 82.250  1.00 17.81 ?  106 LEU B CD1 1 
ATOM   2841 C  CD2 . LEU B 1 106 ? 45.358 -17.025 84.322  1.00 15.37 ?  106 LEU B CD2 1 
ATOM   2842 N  N   . TYR B 1 107 ? 50.309 -16.785 83.489  1.00 13.55 ?  107 TYR B N   1 
ATOM   2843 C  CA  . TYR B 1 107 ? 51.657 -16.917 82.940  1.00 12.74 ?  107 TYR B CA  1 
ATOM   2844 C  C   . TYR B 1 107 ? 51.612 -18.167 82.073  1.00 12.57 ?  107 TYR B C   1 
ATOM   2845 O  O   . TYR B 1 107 ? 51.697 -19.292 82.572  1.00 11.99 ?  107 TYR B O   1 
ATOM   2846 C  CB  . TYR B 1 107 ? 52.688 -16.996 84.063  1.00 13.48 ?  107 TYR B CB  1 
ATOM   2847 C  CG  . TYR B 1 107 ? 54.107 -16.686 83.634  1.00 12.49 ?  107 TYR B CG  1 
ATOM   2848 C  CD1 . TYR B 1 107 ? 54.916 -17.679 83.110  1.00 15.06 ?  107 TYR B CD1 1 
ATOM   2849 C  CD2 . TYR B 1 107 ? 54.640 -15.413 83.799  1.00 12.40 ?  107 TYR B CD2 1 
ATOM   2850 C  CE1 . TYR B 1 107 ? 56.225 -17.405 82.729  1.00 12.95 ?  107 TYR B CE1 1 
ATOM   2851 C  CE2 . TYR B 1 107 ? 55.948 -15.123 83.419  1.00 15.99 ?  107 TYR B CE2 1 
ATOM   2852 C  CZ  . TYR B 1 107 ? 56.726 -16.123 82.879  1.00 17.04 ?  107 TYR B CZ  1 
ATOM   2853 O  OH  . TYR B 1 107 ? 58.025 -15.830 82.504  1.00 17.32 ?  107 TYR B OH  1 
ATOM   2854 N  N   . ILE B 1 108 ? 51.403 -17.967 80.774  1.00 13.94 ?  108 ILE B N   1 
ATOM   2855 C  CA  . ILE B 1 108 ? 51.106 -19.041 79.831  1.00 11.96 ?  108 ILE B CA  1 
ATOM   2856 C  C   . ILE B 1 108 ? 52.424 -19.420 79.168  1.00 11.99 ?  108 ILE B C   1 
ATOM   2857 O  O   . ILE B 1 108 ? 52.946 -18.680 78.327  1.00 14.17 ?  108 ILE B O   1 
ATOM   2858 C  CB  . ILE B 1 108 ? 50.042 -18.622 78.809  1.00 13.15 ?  108 ILE B CB  1 
ATOM   2859 C  CG1 . ILE B 1 108 ? 48.817 -18.021 79.513  1.00 13.62 ?  108 ILE B CG1 1 
ATOM   2860 C  CG2 . ILE B 1 108 ? 49.656 -19.805 77.937  1.00 13.73 ?  108 ILE B CG2 1 
ATOM   2861 C  CD1 . ILE B 1 108 ? 47.664 -17.758 78.554  1.00 17.49 ?  108 ILE B CD1 1 
ATOM   2862 N  N   A ASP B 1 109 ? 52.960 -20.580 79.535  0.69 12.48 ?  109 ASP B N   1 
ATOM   2863 N  N   B ASP B 1 109 ? 52.965 -20.565 79.572  0.31 12.57 ?  109 ASP B N   1 
ATOM   2864 C  CA  A ASP B 1 109 ? 54.346 -20.907 79.228  0.69 14.26 ?  109 ASP B CA  1 
ATOM   2865 C  CA  B ASP B 1 109 ? 54.390 -20.838 79.444  0.31 14.50 ?  109 ASP B CA  1 
ATOM   2866 C  C   A ASP B 1 109 ? 54.518 -22.416 79.279  0.69 14.59 ?  109 ASP B C   1 
ATOM   2867 C  C   B ASP B 1 109 ? 54.596 -22.334 79.616  0.31 14.50 ?  109 ASP B C   1 
ATOM   2868 O  O   A ASP B 1 109 ? 53.887 -23.084 80.095  0.69 14.21 ?  109 ASP B O   1 
ATOM   2869 O  O   B ASP B 1 109 ? 54.039 -22.927 80.541  0.31 15.03 ?  109 ASP B O   1 
ATOM   2870 C  CB  A ASP B 1 109 ? 55.272 -20.218 80.244  0.69 15.73 ?  109 ASP B CB  1 
ATOM   2871 C  CB  B ASP B 1 109 ? 55.157 -20.036 80.511  0.31 15.45 ?  109 ASP B CB  1 
ATOM   2872 C  CG  A ASP B 1 109 ? 56.671 -19.978 79.715  0.69 16.68 ?  109 ASP B CG  1 
ATOM   2873 C  CG  B ASP B 1 109 ? 56.662 -20.209 80.433  0.31 15.90 ?  109 ASP B CG  1 
ATOM   2874 O  OD1 A ASP B 1 109 ? 57.356 -20.955 79.319  0.69 14.68 ?  109 ASP B OD1 1 
ATOM   2875 O  OD1 B ASP B 1 109 ? 57.173 -21.304 80.753  0.31 15.50 ?  109 ASP B OD1 1 
ATOM   2876 O  OD2 A ASP B 1 109 ? 57.091 -18.803 79.733  0.69 14.72 -1 109 ASP B OD2 1 
ATOM   2877 O  OD2 B ASP B 1 109 ? 57.337 -19.220 80.083  0.31 14.43 -1 109 ASP B OD2 1 
ATOM   2878 N  N   A GLY B 1 110 ? 55.376 -22.953 78.409  0.69 14.77 ?  110 GLY B N   1 
ATOM   2879 N  N   B GLY B 1 110 ? 55.388 -22.942 78.732  0.31 14.80 ?  110 GLY B N   1 
ATOM   2880 C  CA  A GLY B 1 110 ? 55.766 -24.349 78.542  0.69 14.62 ?  110 GLY B CA  1 
ATOM   2881 C  CA  B GLY B 1 110 ? 55.578 -24.382 78.779  0.31 15.07 ?  110 GLY B CA  1 
ATOM   2882 C  C   A GLY B 1 110 ? 56.615 -24.626 79.768  0.69 15.49 ?  110 GLY B C   1 
ATOM   2883 C  C   B GLY B 1 110 ? 56.474 -24.876 79.900  0.31 16.14 ?  110 GLY B C   1 
ATOM   2884 O  O   A GLY B 1 110 ? 56.699 -25.779 80.206  0.69 17.34 ?  110 GLY B O   1 
ATOM   2885 O  O   B GLY B 1 110 ? 56.552 -26.093 80.109  0.31 16.76 ?  110 GLY B O   1 
ATOM   2886 N  N   A HIS B 1 111 ? 57.244 -23.595 80.321  0.69 14.84 ?  111 HIS B N   1 
ATOM   2887 N  N   B HIS B 1 111 ? 57.127 -23.976 80.633  0.31 16.45 ?  111 HIS B N   1 
ATOM   2888 C  CA  A HIS B 1 111 ? 58.076 -23.682 81.512  0.69 17.11 ?  111 HIS B CA  1 
ATOM   2889 C  CA  B HIS B 1 111 ? 58.159 -24.361 81.590  0.31 16.59 ?  111 HIS B CA  1 
ATOM   2890 C  C   A HIS B 1 111 ? 57.409 -22.989 82.695  0.69 16.94 ?  111 HIS B C   1 
ATOM   2891 C  C   B HIS B 1 111 ? 57.878 -23.919 83.016  0.31 18.66 ?  111 HIS B C   1 
ATOM   2892 O  O   A HIS B 1 111 ? 56.373 -22.326 82.571  0.69 17.37 ?  111 HIS B O   1 
ATOM   2893 O  O   B HIS B 1 111 ? 58.002 -24.730 83.939  0.31 20.45 ?  111 HIS B O   1 
ATOM   2894 C  CB  A HIS B 1 111 ? 59.444 -23.049 81.246  0.69 18.22 ?  111 HIS B CB  1 
ATOM   2895 C  CB  B HIS B 1 111 ? 59.509 -23.802 81.134  0.31 18.24 ?  111 HIS B CB  1 
ATOM   2896 C  CG  A HIS B 1 111 ? 60.119 -23.584 80.026  0.69 19.35 ?  111 HIS B CG  1 
ATOM   2897 C  CG  B HIS B 1 111 ? 60.001 -24.409 79.862  0.31 19.39 ?  111 HIS B CG  1 
ATOM   2898 N  ND1 A HIS B 1 111 ? 59.966 -23.014 78.781  0.69 19.56 ?  111 HIS B ND1 1 
ATOM   2899 N  ND1 B HIS B 1 111 ? 60.706 -25.592 79.829  0.31 23.09 ?  111 HIS B ND1 1 
ATOM   2900 C  CD2 A HIS B 1 111 ? 60.921 -24.661 79.855  0.69 22.34 ?  111 HIS B CD2 1 
ATOM   2901 C  CD2 B HIS B 1 111 ? 59.868 -24.011 78.576  0.31 21.76 ?  111 HIS B CD2 1 
ATOM   2902 C  CE1 A HIS B 1 111 ? 60.658 -23.710 77.896  0.69 23.08 ?  111 HIS B CE1 1 
ATOM   2903 C  CE1 B HIS B 1 111 ? 60.995 -25.891 78.576  0.31 24.04 ?  111 HIS B CE1 1 
ATOM   2904 N  NE2 A HIS B 1 111 ? 61.248 -24.712 78.522  0.69 25.05 ?  111 HIS B NE2 1 
ATOM   2905 N  NE2 B HIS B 1 111 ? 60.500 -24.947 77.796  0.31 20.73 ?  111 HIS B NE2 1 
ATOM   2906 N  N   A GLY B 1 112 ? 58.046 -23.129 83.856  0.69 17.93 ?  112 GLY B N   1 
ATOM   2907 N  N   B GLY B 1 112 ? 57.553 -22.649 83.239  0.31 16.79 ?  112 GLY B N   1 
ATOM   2908 C  CA  A GLY B 1 112 ? 57.583 -22.457 85.052  0.69 18.48 ?  112 GLY B CA  1 
ATOM   2909 C  CA  B GLY B 1 112 ? 57.319 -22.190 84.596  0.31 17.97 ?  112 GLY B CA  1 
ATOM   2910 C  C   A GLY B 1 112 ? 58.216 -21.100 85.247  0.69 17.41 ?  112 GLY B C   1 
ATOM   2911 C  C   B GLY B 1 112 ? 58.085 -20.941 84.977  0.31 17.73 ?  112 GLY B C   1 
ATOM   2912 O  O   A GLY B 1 112 ? 57.670 -20.256 85.963  0.69 16.71 ?  112 GLY B O   1 
ATOM   2913 O  O   B GLY B 1 112 ? 57.532 -20.048 85.627  0.31 17.37 ?  112 GLY B O   1 
ATOM   2914 N  N   . ASP B 1 113 ? 59.364 -20.879 84.597  1.00 17.59 ?  113 ASP B N   1 
ATOM   2915 C  CA  . ASP B 1 113 ? 60.186 -19.682 84.767  1.00 18.62 ?  113 ASP B CA  1 
ATOM   2916 C  C   . ASP B 1 113 ? 60.278 -19.284 86.237  1.00 15.50 ?  113 ASP B C   1 
ATOM   2917 O  O   . ASP B 1 113 ? 60.189 -18.104 86.584  1.00 16.38 ?  113 ASP B O   1 
ATOM   2918 C  CB  . ASP B 1 113 ? 59.655 -18.530 83.901  1.00 15.13 ?  113 ASP B CB  1 
ATOM   2919 C  CG  . ASP B 1 113 ? 59.805 -18.809 82.402  1.00 15.75 ?  113 ASP B CG  1 
ATOM   2920 O  OD1 . ASP B 1 113 ? 60.420 -19.841 82.049  1.00 19.44 ?  113 ASP B OD1 1 
ATOM   2921 O  OD2 . ASP B 1 113 ? 59.300 -17.991 81.596  1.00 18.23 ?  113 ASP B OD2 1 
ATOM   2922 N  N   . PHE B 1 114 ? 60.455 -20.274 87.108  1.00 17.96 ?  114 PHE B N   1 
ATOM   2923 C  CA  . PHE B 1 114 ? 60.403 -20.034 88.545  1.00 16.61 ?  114 PHE B CA  1 
ATOM   2924 C  C   . PHE B 1 114 ? 61.705 -20.438 89.225  1.00 20.81 ?  114 PHE B C   1 
ATOM   2925 O  O   . PHE B 1 114 ? 61.727 -20.734 90.421  1.00 22.28 ?  114 PHE B O   1 
ATOM   2926 C  CB  . PHE B 1 114 ? 59.212 -20.775 89.153  1.00 19.00 ?  114 PHE B CB  1 
ATOM   2927 C  CG  . PHE B 1 114 ? 58.584 -20.076 90.326  1.00 16.55 ?  114 PHE B CG  1 
ATOM   2928 C  CD1 . PHE B 1 114 ? 57.787 -18.963 90.140  1.00 18.68 ?  114 PHE B CD1 1 
ATOM   2929 C  CD2 . PHE B 1 114 ? 58.766 -20.564 91.615  1.00 17.65 ?  114 PHE B CD2 1 
ATOM   2930 C  CE1 . PHE B 1 114 ? 57.184 -18.318 91.208  1.00 17.26 ?  114 PHE B CE1 1 
ATOM   2931 C  CE2 . PHE B 1 114 ? 58.161 -19.937 92.696  1.00 18.64 ?  114 PHE B CE2 1 
ATOM   2932 C  CZ  . PHE B 1 114 ? 57.369 -18.814 92.498  1.00 17.30 ?  114 PHE B CZ  1 
ATOM   2933 N  N   . ASN B 1 115 ? 62.801 -20.446 88.474  1.00 21.14 ?  115 ASN B N   1 
ATOM   2934 C  CA  . ASN B 1 115 ? 64.087 -20.754 89.072  1.00 21.18 ?  115 ASN B CA  1 
ATOM   2935 C  C   . ASN B 1 115 ? 64.655 -19.545 89.802  1.00 18.40 ?  115 ASN B C   1 
ATOM   2936 O  O   . ASN B 1 115 ? 64.278 -18.395 89.569  1.00 18.81 ?  115 ASN B O   1 
ATOM   2937 C  CB  . ASN B 1 115 ? 65.085 -21.223 88.009  1.00 23.12 ?  115 ASN B CB  1 
ATOM   2938 C  CG  . ASN B 1 115 ? 64.706 -22.554 87.409  1.00 30.21 ?  115 ASN B CG  1 
ATOM   2939 O  OD1 . ASN B 1 115 ? 64.894 -23.597 88.034  1.00 33.58 ?  115 ASN B OD1 1 
ATOM   2940 N  ND2 . ASN B 1 115 ? 64.172 -22.531 86.185  1.00 29.87 ?  115 ASN B ND2 1 
ATOM   2941 N  N   . THR B 1 116 ? 65.589 -19.828 90.706  1.00 24.02 ?  116 THR B N   1 
ATOM   2942 C  CA  . THR B 1 116 ? 66.327 -18.811 91.434  1.00 22.56 ?  116 THR B CA  1 
ATOM   2943 C  C   . THR B 1 116 ? 67.796 -18.955 91.067  1.00 23.41 ?  116 THR B C   1 
ATOM   2944 O  O   . THR B 1 116 ? 68.179 -19.958 90.449  1.00 24.98 ?  116 THR B O   1 
ATOM   2945 C  CB  . THR B 1 116 ? 66.154 -18.965 92.947  1.00 26.88 ?  116 THR B CB  1 
ATOM   2946 O  OG1 . THR B 1 116 ? 66.682 -20.235 93.348  1.00 29.06 ?  116 THR B OG1 1 
ATOM   2947 C  CG2 . THR B 1 116 ? 64.685 -18.864 93.332  1.00 29.24 ?  116 THR B CG2 1 
ATOM   2948 N  N   . PRO B 1 117 ? 68.640 -17.991 91.431  1.00 22.78 ?  117 PRO B N   1 
ATOM   2949 C  CA  . PRO B 1 117 ? 70.081 -18.155 91.158  1.00 26.78 ?  117 PRO B CA  1 
ATOM   2950 C  C   . PRO B 1 117 ? 70.650 -19.459 91.687  1.00 33.92 ?  117 PRO B C   1 
ATOM   2951 O  O   . PRO B 1 117 ? 71.581 -20.011 91.086  1.00 37.74 ?  117 PRO B O   1 
ATOM   2952 C  CB  . PRO B 1 117 ? 70.697 -16.940 91.859  1.00 30.07 ?  117 PRO B CB  1 
ATOM   2953 C  CG  . PRO B 1 117 ? 69.644 -15.899 91.759  1.00 29.44 ?  117 PRO B CG  1 
ATOM   2954 C  CD  . PRO B 1 117 ? 68.329 -16.635 91.919  1.00 26.30 ?  117 PRO B CD  1 
ATOM   2955 N  N   . GLU B 1 118 ? 70.090 -19.993 92.773  1.00 36.46 ?  118 GLU B N   1 
ATOM   2956 C  CA  . GLU B 1 118 ? 70.595 -21.223 93.364  1.00 37.32 ?  118 GLU B CA  1 
ATOM   2957 C  C   . GLU B 1 118 ? 70.012 -22.484 92.740  1.00 40.54 ?  118 GLU B C   1 
ATOM   2958 O  O   . GLU B 1 118 ? 70.635 -23.548 92.844  1.00 51.42 ?  118 GLU B O   1 
ATOM   2959 C  CB  . GLU B 1 118 ? 70.329 -21.226 94.873  1.00 43.53 ?  118 GLU B CB  1 
ATOM   2960 C  CG  . GLU B 1 118 ? 70.975 -20.058 95.600  1.00 49.68 ?  118 GLU B CG  1 
ATOM   2961 C  CD  . GLU B 1 118 ? 69.986 -18.976 96.000  1.00 50.10 ?  118 GLU B CD  1 
ATOM   2962 O  OE1 . GLU B 1 118 ? 69.950 -18.634 97.202  1.00 62.26 ?  118 GLU B OE1 1 
ATOM   2963 O  OE2 . GLU B 1 118 ? 69.251 -18.462 95.125  1.00 41.25 -1 118 GLU B OE2 1 
ATOM   2964 N  N   . THR B 1 119 ? 68.850 -22.408 92.091  1.00 32.41 ?  119 THR B N   1 
ATOM   2965 C  CA  . THR B 1 119 ? 68.273 -23.597 91.475  1.00 35.63 ?  119 THR B CA  1 
ATOM   2966 C  C   . THR B 1 119 ? 68.505 -23.685 89.969  1.00 36.17 ?  119 THR B C   1 
ATOM   2967 O  O   . THR B 1 119 ? 68.253 -24.746 89.389  1.00 44.48 ?  119 THR B O   1 
ATOM   2968 C  CB  . THR B 1 119 ? 66.764 -23.680 91.752  1.00 41.08 ?  119 THR B CB  1 
ATOM   2969 O  OG1 . THR B 1 119 ? 66.060 -22.719 90.952  1.00 36.53 ?  119 THR B OG1 1 
ATOM   2970 C  CG2 . THR B 1 119 ? 66.475 -23.435 93.228  1.00 39.99 ?  119 THR B CG2 1 
ATOM   2971 N  N   . THR B 1 120 ? 68.970 -22.620 89.317  1.00 36.30 ?  120 THR B N   1 
ATOM   2972 C  CA  . THR B 1 120 ? 69.092 -22.657 87.866  1.00 35.30 ?  120 THR B CA  1 
ATOM   2973 C  C   . THR B 1 120 ? 70.273 -23.530 87.448  1.00 40.99 ?  120 THR B C   1 
ATOM   2974 O  O   . THR B 1 120 ? 71.395 -23.359 87.934  1.00 44.27 ?  120 THR B O   1 
ATOM   2975 C  CB  . THR B 1 120 ? 69.232 -21.242 87.287  1.00 32.29 ?  120 THR B CB  1 
ATOM   2976 O  OG1 . THR B 1 120 ? 69.443 -21.319 85.868  1.00 31.17 ?  120 THR B OG1 1 
ATOM   2977 C  CG2 . THR B 1 120 ? 70.378 -20.465 87.941  1.00 26.20 ?  120 THR B CG2 1 
ATOM   2978 N  N   . ASP B 1 121 ? 70.001 -24.489 86.563  1.00 40.82 ?  121 ASP B N   1 
ATOM   2979 C  CA  . ASP B 1 121 ? 71.045 -25.300 85.952  1.00 44.82 ?  121 ASP B CA  1 
ATOM   2980 C  C   . ASP B 1 121 ? 71.652 -24.634 84.728  1.00 48.35 ?  121 ASP B C   1 
ATOM   2981 O  O   . ASP B 1 121 ? 72.796 -24.937 84.371  1.00 47.58 ?  121 ASP B O   1 
ATOM   2982 C  CB  . ASP B 1 121 ? 70.482 -26.662 85.540  1.00 44.91 ?  121 ASP B CB  1 
ATOM   2983 C  CG  . ASP B 1 121 ? 70.067 -27.505 86.725  1.00 59.64 ?  121 ASP B CG  1 
ATOM   2984 O  OD1 . ASP B 1 121 ? 68.845 -27.653 86.943  1.00 63.94 -1 121 ASP B OD1 1 
ATOM   2985 O  OD2 . ASP B 1 121 ? 70.956 -28.033 87.428  1.00 61.37 ?  121 ASP B OD2 1 
ATOM   2986 N  N   . THR B 1 122 ? 70.906 -23.737 84.085  1.00 41.67 ?  122 THR B N   1 
ATOM   2987 C  CA  . THR B 1 122 ? 71.306 -23.109 82.835  1.00 37.73 ?  122 THR B CA  1 
ATOM   2988 C  C   . THR B 1 122 ? 71.932 -21.734 83.021  1.00 33.87 ?  122 THR B C   1 
ATOM   2989 O  O   . THR B 1 122 ? 72.630 -21.261 82.115  1.00 33.36 ?  122 THR B O   1 
ATOM   2990 C  CB  . THR B 1 122 ? 70.086 -22.967 81.917  1.00 33.92 ?  122 THR B CB  1 
ATOM   2991 O  OG1 . THR B 1 122 ? 69.105 -22.144 82.566  1.00 32.94 ?  122 THR B OG1 1 
ATOM   2992 C  CG2 . THR B 1 122 ? 69.464 -24.324 81.636  1.00 33.50 ?  122 THR B CG2 1 
ATOM   2993 N  N   . GLY B 1 123 ? 71.698 -21.085 84.161  1.00 28.79 ?  123 GLY B N   1 
ATOM   2994 C  CA  . GLY B 1 123 ? 72.042 -19.687 84.316  1.00 27.41 ?  123 GLY B CA  1 
ATOM   2995 C  C   . GLY B 1 123 ? 71.201 -18.741 83.487  1.00 22.62 ?  123 GLY B C   1 
ATOM   2996 O  O   . GLY B 1 123 ? 71.500 -17.545 83.445  1.00 26.58 ?  123 GLY B O   1 
ATOM   2997 N  N   . TYR B 1 124 ? 70.142 -19.238 82.850  1.00 25.28 ?  124 TYR B N   1 
ATOM   2998 C  CA  . TYR B 1 124 ? 69.358 -18.444 81.912  1.00 25.42 ?  124 TYR B CA  1 
ATOM   2999 C  C   . TYR B 1 124 ? 68.358 -17.564 82.660  1.00 25.44 ?  124 TYR B C   1 
ATOM   3000 O  O   . TYR B 1 124 ? 67.452 -18.076 83.332  1.00 24.38 ?  124 TYR B O   1 
ATOM   3001 C  CB  . TYR B 1 124 ? 68.638 -19.357 80.928  1.00 26.26 ?  124 TYR B CB  1 
ATOM   3002 C  CG  . TYR B 1 124 ? 67.836 -18.596 79.912  1.00 20.96 ?  124 TYR B CG  1 
ATOM   3003 C  CD1 . TYR B 1 124 ? 68.361 -17.461 79.298  1.00 20.07 ?  124 TYR B CD1 1 
ATOM   3004 C  CD2 . TYR B 1 124 ? 66.542 -18.984 79.585  1.00 28.26 ?  124 TYR B CD2 1 
ATOM   3005 C  CE1 . TYR B 1 124 ? 67.620 -16.744 78.360  1.00 22.29 ?  124 TYR B CE1 1 
ATOM   3006 C  CE2 . TYR B 1 124 ? 65.787 -18.266 78.662  1.00 23.88 ?  124 TYR B CE2 1 
ATOM   3007 C  CZ  . TYR B 1 124 ? 66.335 -17.153 78.053  1.00 27.03 ?  124 TYR B CZ  1 
ATOM   3008 O  OH  . TYR B 1 124 ? 65.602 -16.442 77.136  1.00 26.84 ?  124 TYR B OH  1 
ATOM   3009 N  N   . LEU B 1 125 ? 68.520 -16.245 82.525  1.00 20.44 ?  125 LEU B N   1 
ATOM   3010 C  CA  . LEU B 1 125 ? 67.610 -15.287 83.158  1.00 17.31 ?  125 LEU B CA  1 
ATOM   3011 C  C   . LEU B 1 125 ? 66.156 -15.562 82.803  1.00 19.99 ?  125 LEU B C   1 
ATOM   3012 O  O   . LEU B 1 125 ? 65.257 -15.341 83.627  1.00 18.35 ?  125 LEU B O   1 
ATOM   3013 C  CB  . LEU B 1 125 ? 67.987 -13.866 82.741  1.00 16.08 ?  125 LEU B CB  1 
ATOM   3014 C  CG  . LEU B 1 125 ? 67.246 -12.684 83.360  1.00 18.95 ?  125 LEU B CG  1 
ATOM   3015 C  CD1 . LEU B 1 125 ? 67.507 -12.627 84.869  1.00 19.14 ?  125 LEU B CD1 1 
ATOM   3016 C  CD2 . LEU B 1 125 ? 67.679 -11.388 82.669  1.00 20.93 ?  125 LEU B CD2 1 
ATOM   3017 N  N   . GLY B 1 126 ? 65.901 -16.022 81.573  1.00 17.28 ?  126 GLY B N   1 
ATOM   3018 C  CA  . GLY B 1 126 ? 64.534 -16.249 81.133  1.00 19.79 ?  126 GLY B CA  1 
ATOM   3019 C  C   . GLY B 1 126 ? 63.797 -17.285 81.956  1.00 21.60 ?  126 GLY B C   1 
ATOM   3020 O  O   . GLY B 1 126 ? 62.565 -17.268 82.020  1.00 24.07 ?  126 GLY B O   1 
ATOM   3021 N  N   . GLY B 1 127 ? 64.521 -18.190 82.599  1.00 18.84 ?  127 GLY B N   1 
ATOM   3022 C  CA  . GLY B 1 127 ? 63.883 -19.171 83.453  1.00 19.92 ?  127 GLY B CA  1 
ATOM   3023 C  C   . GLY B 1 127 ? 63.728 -18.741 84.895  1.00 17.99 ?  127 GLY B C   1 
ATOM   3024 O  O   . GLY B 1 127 ? 63.390 -19.579 85.744  1.00 17.65 ?  127 GLY B O   1 
ATOM   3025 N  N   . MET B 1 128 ? 63.948 -17.457 85.181  1.00 16.55 ?  128 MET B N   1 
ATOM   3026 C  CA  . MET B 1 128 ? 63.893 -16.894 86.528  1.00 16.70 ?  128 MET B CA  1 
ATOM   3027 C  C   . MET B 1 128 ? 62.920 -15.718 86.608  1.00 15.35 ?  128 MET B C   1 
ATOM   3028 O  O   . MET B 1 128 ? 62.953 -14.943 87.573  1.00 17.37 ?  128 MET B O   1 
ATOM   3029 C  CB  . MET B 1 128 ? 65.300 -16.470 86.966  1.00 23.41 ?  128 MET B CB  1 
ATOM   3030 C  CG  . MET B 1 128 ? 66.361 -17.583 86.807  1.00 17.94 ?  128 MET B CG  1 
ATOM   3031 S  SD  . MET B 1 128 ? 68.080 -16.963 86.615  1.00 27.52 ?  128 MET B SD  1 
ATOM   3032 C  CE  . MET B 1 128 ? 68.233 -16.151 88.185  1.00 23.03 ?  128 MET B CE  1 
ATOM   3033 N  N   . VAL B 1 129 ? 62.012 -15.600 85.631  1.00 15.01 ?  129 VAL B N   1 
ATOM   3034 C  CA  . VAL B 1 129 ? 61.213 -14.382 85.494  1.00 14.68 ?  129 VAL B CA  1 
ATOM   3035 C  C   . VAL B 1 129 ? 60.091 -14.337 86.526  1.00 16.07 ?  129 VAL B C   1 
ATOM   3036 O  O   . VAL B 1 129 ? 59.900 -13.326 87.215  1.00 14.88 ?  129 VAL B O   1 
ATOM   3037 C  CB  . VAL B 1 129 ? 60.650 -14.274 84.063  1.00 15.00 ?  129 VAL B CB  1 
ATOM   3038 C  CG1 . VAL B 1 129 ? 59.650 -13.135 83.982  1.00 14.46 ?  129 VAL B CG1 1 
ATOM   3039 C  CG2 . VAL B 1 129 ? 61.783 -14.057 83.052  1.00 18.00 ?  129 VAL B CG2 1 
ATOM   3040 N  N   . LEU B 1 130 ? 59.280 -15.393 86.587  1.00 16.48 ?  130 LEU B N   1 
ATOM   3041 C  CA  . LEU B 1 130 ? 58.122 -15.343 87.468  1.00 14.78 ?  130 LEU B CA  1 
ATOM   3042 C  C   . LEU B 1 130 ? 58.555 -15.370 88.925  1.00 15.78 ?  130 LEU B C   1 
ATOM   3043 O  O   . LEU B 1 130 ? 57.963 -14.682 89.764  1.00 15.80 ?  130 LEU B O   1 
ATOM   3044 C  CB  . LEU B 1 130 ? 57.172 -16.489 87.121  1.00 13.73 ?  130 LEU B CB  1 
ATOM   3045 C  CG  . LEU B 1 130 ? 55.872 -16.559 87.942  1.00 13.88 ?  130 LEU B CG  1 
ATOM   3046 C  CD1 . LEU B 1 130 ? 55.061 -15.287 87.760  1.00 15.47 ?  130 LEU B CD1 1 
ATOM   3047 C  CD2 . LEU B 1 130 ? 55.072 -17.780 87.520  1.00 17.48 ?  130 LEU B CD2 1 
ATOM   3048 N  N   . SER B 1 131 ? 59.607 -16.121 89.237  1.00 15.08 ?  131 SER B N   1 
ATOM   3049 C  CA  . SER B 1 131 ? 60.126 -16.103 90.604  1.00 17.82 ?  131 SER B CA  1 
ATOM   3050 C  C   . SER B 1 131 ? 60.682 -14.732 90.977  1.00 19.61 ?  131 SER B C   1 
ATOM   3051 O  O   . SER B 1 131 ? 60.547 -14.300 92.132  1.00 18.72 ?  131 SER B O   1 
ATOM   3052 C  CB  . SER B 1 131 ? 61.188 -17.188 90.757  1.00 19.46 ?  131 SER B CB  1 
ATOM   3053 O  OG  . SER B 1 131 ? 62.153 -17.041 89.716  1.00 19.97 ?  131 SER B OG  1 
ATOM   3054 N  N   . GLY B 1 132 ? 61.288 -14.028 90.017  1.00 17.31 ?  132 GLY B N   1 
ATOM   3055 C  CA  . GLY B 1 132 ? 61.770 -12.678 90.286  1.00 17.57 ?  132 GLY B CA  1 
ATOM   3056 C  C   . GLY B 1 132 ? 60.648 -11.698 90.578  1.00 18.93 ?  132 GLY B C   1 
ATOM   3057 O  O   . GLY B 1 132 ? 60.733 -10.898 91.513  1.00 22.16 ?  132 GLY B O   1 
ATOM   3058 N  N   . ALA B 1 133 ? 59.574 -11.756 89.790  1.00 16.50 ?  133 ALA B N   1 
ATOM   3059 C  CA  . ALA B 1 133 ? 58.445 -10.861 89.997  1.00 18.36 ?  133 ALA B CA  1 
ATOM   3060 C  C   . ALA B 1 133 ? 57.735 -11.154 91.313  1.00 18.89 ?  133 ALA B C   1 
ATOM   3061 O  O   . ALA B 1 133 ? 57.181 -10.234 91.929  1.00 18.49 ?  133 ALA B O   1 
ATOM   3062 C  CB  . ALA B 1 133 ? 57.470 -10.984 88.822  1.00 20.58 ?  133 ALA B CB  1 
ATOM   3063 N  N   . CYS B 1 134 ? 57.751 -12.413 91.756  1.00 17.92 ?  134 CYS B N   1 
ATOM   3064 C  CA  . CYS B 1 134 ? 57.140 -12.803 93.026  1.00 18.39 ?  134 CYS B CA  1 
ATOM   3065 C  C   . CYS B 1 134 ? 58.083 -12.651 94.217  1.00 20.85 ?  134 CYS B C   1 
ATOM   3066 O  O   . CYS B 1 134 ? 57.689 -12.971 95.346  1.00 23.99 ?  134 CYS B O   1 
ATOM   3067 C  CB  . CYS B 1 134 ? 56.620 -14.248 92.956  1.00 17.89 ?  134 CYS B CB  1 
ATOM   3068 S  SG  . CYS B 1 134 ? 55.230 -14.522 91.826  1.00 20.23 ?  134 CYS B SG  1 
ATOM   3069 N  N   . GLY B 1 135 ? 59.300 -12.160 94.000  1.00 21.89 ?  135 GLY B N   1 
ATOM   3070 C  CA  . GLY B 1 135 ? 60.201 -11.794 95.079  1.00 21.08 ?  135 GLY B CA  1 
ATOM   3071 C  C   . GLY B 1 135 ? 61.035 -12.904 95.682  1.00 24.63 ?  135 GLY B C   1 
ATOM   3072 O  O   . GLY B 1 135 ? 61.678 -12.672 96.717  1.00 26.07 ?  135 GLY B O   1 
ATOM   3073 N  N   . LEU B 1 136 ? 61.044 -14.100 95.091  1.00 21.04 ?  136 LEU B N   1 
ATOM   3074 C  CA  . LEU B 1 136 ? 61.915 -15.162 95.588  1.00 21.77 ?  136 LEU B CA  1 
ATOM   3075 C  C   . LEU B 1 136 ? 63.386 -14.799 95.436  1.00 23.63 ?  136 LEU B C   1 
ATOM   3076 O  O   . LEU B 1 136 ? 64.232 -15.344 96.150  1.00 26.66 ?  136 LEU B O   1 
ATOM   3077 C  CB  . LEU B 1 136 ? 61.636 -16.478 94.860  1.00 23.21 ?  136 LEU B CB  1 
ATOM   3078 C  CG  . LEU B 1 136 ? 60.521 -17.366 95.409  1.00 25.74 ?  136 LEU B CG  1 
ATOM   3079 C  CD1 . LEU B 1 136 ? 59.162 -16.757 95.133  1.00 25.97 ?  136 LEU B CD1 1 
ATOM   3080 C  CD2 . LEU B 1 136 ? 60.618 -18.756 94.826  1.00 27.88 ?  136 LEU B CD2 1 
ATOM   3081 N  N   . TRP B 1 137 ? 63.712 -13.924 94.485  1.00 21.33 ?  137 TRP B N   1 
ATOM   3082 C  CA  . TRP B 1 137 ? 65.049 -13.359 94.358  1.00 24.73 ?  137 TRP B CA  1 
ATOM   3083 C  C   . TRP B 1 137 ? 64.901 -11.930 93.856  1.00 24.59 ?  137 TRP B C   1 
ATOM   3084 O  O   . TRP B 1 137 ? 63.828 -11.522 93.397  1.00 25.65 ?  137 TRP B O   1 
ATOM   3085 C  CB  . TRP B 1 137 ? 65.944 -14.203 93.433  1.00 24.49 ?  137 TRP B CB  1 
ATOM   3086 C  CG  . TRP B 1 137 ? 65.534 -14.181 91.978  1.00 22.51 ?  137 TRP B CG  1 
ATOM   3087 C  CD1 . TRP B 1 137 ? 64.487 -14.853 91.410  1.00 21.13 ?  137 TRP B CD1 1 
ATOM   3088 C  CD2 . TRP B 1 137 ? 66.180 -13.466 90.914  1.00 20.47 ?  137 TRP B CD2 1 
ATOM   3089 N  NE1 . TRP B 1 137 ? 64.436 -14.594 90.056  1.00 21.66 ?  137 TRP B NE1 1 
ATOM   3090 C  CE2 . TRP B 1 137 ? 65.460 -13.741 89.731  1.00 17.80 ?  137 TRP B CE2 1 
ATOM   3091 C  CE3 . TRP B 1 137 ? 67.292 -12.612 90.851  1.00 23.54 ?  137 TRP B CE3 1 
ATOM   3092 C  CZ2 . TRP B 1 137 ? 65.814 -13.193 88.500  1.00 19.63 ?  137 TRP B CZ2 1 
ATOM   3093 C  CZ3 . TRP B 1 137 ? 67.643 -12.070 89.627  1.00 21.90 ?  137 TRP B CZ3 1 
ATOM   3094 C  CH2 . TRP B 1 137 ? 66.906 -12.359 88.471  1.00 22.65 ?  137 TRP B CH2 1 
ATOM   3095 N  N   . ASP B 1 138 ? 65.980 -11.159 93.964  1.00 23.48 ?  138 ASP B N   1 
ATOM   3096 C  CA  . ASP B 1 138 ? 65.930 -9.723  93.710  1.00 24.49 ?  138 ASP B CA  1 
ATOM   3097 C  C   . ASP B 1 138 ? 66.533 -9.440  92.340  1.00 29.39 ?  138 ASP B C   1 
ATOM   3098 O  O   . ASP B 1 138 ? 67.755 -9.497  92.161  1.00 26.85 ?  138 ASP B O   1 
ATOM   3099 C  CB  . ASP B 1 138 ? 66.667 -8.935  94.789  1.00 29.27 ?  138 ASP B CB  1 
ATOM   3100 C  CG  . ASP B 1 138 ? 66.427 -7.433  94.684  1.00 37.03 ?  138 ASP B CG  1 
ATOM   3101 O  OD1 . ASP B 1 138 ? 65.763 -6.982  93.725  1.00 36.21 ?  138 ASP B OD1 1 
ATOM   3102 O  OD2 . ASP B 1 138 ? 66.907 -6.692  95.568  1.00 50.78 -1 138 ASP B OD2 1 
ATOM   3103 N  N   . SER B 1 139 ? 65.669 -9.106  91.388  1.00 23.78 ?  139 SER B N   1 
ATOM   3104 C  CA  . SER B 1 139 ? 66.078 -8.750  90.041  1.00 22.98 ?  139 SER B CA  1 
ATOM   3105 C  C   . SER B 1 139 ? 66.692 -7.360  89.939  1.00 25.29 ?  139 SER B C   1 
ATOM   3106 O  O   . SER B 1 139 ? 67.360 -7.069  88.941  1.00 25.76 ?  139 SER B O   1 
ATOM   3107 C  CB  . SER B 1 139 ? 64.859 -8.887  89.126  1.00 19.77 ?  139 SER B CB  1 
ATOM   3108 O  OG  . SER B 1 139 ? 64.025 -7.747  89.236  1.00 22.20 ?  139 SER B OG  1 
ATOM   3109 N  N   . GLY B 1 140 ? 66.513 -6.507  90.945  1.00 23.29 ?  140 GLY B N   1 
ATOM   3110 C  CA  . GLY B 1 140 ? 66.812 -5.102  90.804  1.00 26.54 ?  140 GLY B CA  1 
ATOM   3111 C  C   . GLY B 1 140 ? 65.726 -4.296  90.132  1.00 29.73 ?  140 GLY B C   1 
ATOM   3112 O  O   . GLY B 1 140 ? 65.887 -3.080  89.978  1.00 28.25 ?  140 GLY B O   1 
ATOM   3113 N  N   . HIS B 1 141 ? 64.618 -4.925  89.726  1.00 21.10 ?  141 HIS B N   1 
ATOM   3114 C  CA  . HIS B 1 141 ? 63.558 -4.212  89.028  1.00 22.02 ?  141 HIS B CA  1 
ATOM   3115 C  C   . HIS B 1 141 ? 62.219 -4.352  89.736  1.00 22.64 ?  141 HIS B C   1 
ATOM   3116 O  O   . HIS B 1 141 ? 61.167 -4.069  89.147  1.00 26.01 ?  141 HIS B O   1 
ATOM   3117 C  CB  . HIS B 1 141 ? 63.477 -4.680  87.573  1.00 20.66 ?  141 HIS B CB  1 
ATOM   3118 C  CG  . HIS B 1 141 ? 64.697 -4.323  86.784  1.00 20.20 ?  141 HIS B CG  1 
ATOM   3119 N  ND1 . HIS B 1 141 ? 64.842 -3.104  86.163  1.00 22.77 ?  141 HIS B ND1 1 
ATOM   3120 C  CD2 . HIS B 1 141 ? 65.856 -4.993  86.577  1.00 22.12 ?  141 HIS B CD2 1 
ATOM   3121 C  CE1 . HIS B 1 141 ? 66.025 -3.046  85.580  1.00 22.16 ?  141 HIS B CE1 1 
ATOM   3122 N  NE2 . HIS B 1 141 ? 66.661 -4.180  85.815  1.00 21.84 ?  141 HIS B NE2 1 
ATOM   3123 N  N   . GLY B 1 142 ? 62.242 -4.724  91.008  1.00 24.40 ?  142 GLY B N   1 
ATOM   3124 C  CA  . GLY B 1 142 ? 61.034 -4.795  91.800  1.00 23.46 ?  142 GLY B CA  1 
ATOM   3125 C  C   . GLY B 1 142 ? 60.452 -6.195  91.847  1.00 24.77 ?  142 GLY B C   1 
ATOM   3126 O  O   . GLY B 1 142 ? 60.883 -7.120  91.153  1.00 22.52 ?  142 GLY B O   1 
ATOM   3127 N  N   . ALA B 1 143 ? 59.458 -6.341  92.719  1.00 22.56 ?  143 ALA B N   1 
ATOM   3128 C  CA  . ALA B 1 143 ? 58.705 -7.582  92.830  1.00 23.94 ?  143 ALA B CA  1 
ATOM   3129 C  C   . ALA B 1 143 ? 57.260 -7.242  93.156  1.00 20.11 ?  143 ALA B C   1 
ATOM   3130 O  O   . ALA B 1 143 ? 56.637 -6.433  92.458  1.00 21.57 ?  143 ALA B O   1 
ATOM   3131 C  CB  . ALA B 1 143 ? 59.325 -8.508  93.878  1.00 22.08 ?  143 ALA B CB  1 
ATOM   3132 N  N   . GLY B 1 144 ? 56.710 -7.838  94.211  1.00 20.04 ?  144 GLY B N   1 
ATOM   3133 C  CA  . GLY B 1 144 ? 55.385 -7.471  94.659  1.00 23.71 ?  144 GLY B CA  1 
ATOM   3134 C  C   . GLY B 1 144 ? 54.240 -8.253  94.057  1.00 22.42 ?  144 GLY B C   1 
ATOM   3135 O  O   . GLY B 1 144 ? 53.085 -8.026  94.446  1.00 23.88 ?  144 GLY B O   1 
ATOM   3136 N  N   . LEU B 1 145 ? 54.497 -9.153  93.110  1.00 19.60 ?  145 LEU B N   1 
ATOM   3137 C  CA  . LEU B 1 145 ? 53.434 -10.026 92.633  1.00 15.30 ?  145 LEU B CA  1 
ATOM   3138 C  C   . LEU B 1 145 ? 53.237 -11.141 93.652  1.00 17.23 ?  145 LEU B C   1 
ATOM   3139 O  O   . LEU B 1 145 ? 54.167 -11.904 93.940  1.00 20.09 ?  145 LEU B O   1 
ATOM   3140 C  CB  . LEU B 1 145 ? 53.766 -10.595 91.253  1.00 15.86 ?  145 LEU B CB  1 
ATOM   3141 C  CG  . LEU B 1 145 ? 52.819 -11.643 90.646  1.00 16.79 ?  145 LEU B CG  1 
ATOM   3142 C  CD1 . LEU B 1 145 ? 51.413 -11.127 90.423  1.00 21.14 ?  145 LEU B CD1 1 
ATOM   3143 C  CD2 . LEU B 1 145 ? 53.414 -12.133 89.312  1.00 18.58 ?  145 LEU B CD2 1 
ATOM   3144 N  N   . ARG B 1 146 ? 52.041 -11.225 94.213  1.00 18.51 ?  146 ARG B N   1 
ATOM   3145 C  CA  . ARG B 1 146 ? 51.741 -12.311 95.133  1.00 19.65 ?  146 ARG B CA  1 
ATOM   3146 C  C   . ARG B 1 146 ? 51.703 -13.613 94.353  1.00 17.11 ?  146 ARG B C   1 
ATOM   3147 O  O   . ARG B 1 146 ? 50.977 -13.699 93.349  1.00 16.75 ?  146 ARG B O   1 
ATOM   3148 C  CB  . ARG B 1 146 ? 50.412 -12.060 95.832  1.00 20.51 ?  146 ARG B CB  1 
ATOM   3149 C  CG  . ARG B 1 146 ? 50.456 -10.886 96.819  1.00 31.24 ?  146 ARG B CG  1 
ATOM   3150 C  CD  . ARG B 1 146 ? 49.085 -10.576 97.408  1.00 34.87 ?  146 ARG B CD  1 
ATOM   3151 N  NE  . ARG B 1 146 ? 48.722 -11.499 98.478  1.00 34.34 ?  146 ARG B NE  1 
ATOM   3152 C  CZ  . ARG B 1 146 ? 47.954 -12.575 98.322  1.00 41.61 ?  146 ARG B CZ  1 
ATOM   3153 N  NH1 . ARG B 1 146 ? 47.449 -12.878 97.133  1.00 40.86 ?  146 ARG B NH1 1 
ATOM   3154 N  NH2 . ARG B 1 146 ? 47.683 -13.349 99.366  1.00 47.41 ?  146 ARG B NH2 1 
ATOM   3155 N  N   . PRO B 1 147 ? 52.474 -14.633 94.748  1.00 17.78 ?  147 PRO B N   1 
ATOM   3156 C  CA  . PRO B 1 147 ? 52.466 -15.892 93.989  1.00 17.41 ?  147 PRO B CA  1 
ATOM   3157 C  C   . PRO B 1 147 ? 51.111 -16.574 93.982  1.00 14.53 ?  147 PRO B C   1 
ATOM   3158 O  O   . PRO B 1 147 ? 50.779 -17.287 93.019  1.00 17.50 ?  147 PRO B O   1 
ATOM   3159 C  CB  . PRO B 1 147 ? 53.545 -16.738 94.689  1.00 19.97 ?  147 PRO B CB  1 
ATOM   3160 C  CG  . PRO B 1 147 ? 53.778 -16.069 96.030  1.00 23.11 ?  147 PRO B CG  1 
ATOM   3161 C  CD  . PRO B 1 147 ? 53.484 -14.619 95.823  1.00 22.61 ?  147 PRO B CD  1 
ATOM   3162 N  N   . GLU B 1 148 ? 50.300 -16.365 95.020  1.00 18.02 ?  148 GLU B N   1 
ATOM   3163 C  CA  . GLU B 1 148 ? 48.956 -16.927 94.998  1.00 19.43 ?  148 GLU B CA  1 
ATOM   3164 C  C   . GLU B 1 148 ? 48.038 -16.201 94.021  1.00 18.68 ?  148 GLU B C   1 
ATOM   3165 O  O   . GLU B 1 148 ? 46.882 -16.611 93.866  1.00 21.32 ?  148 GLU B O   1 
ATOM   3166 C  CB  . GLU B 1 148 ? 48.373 -16.915 96.415  1.00 20.55 ?  148 GLU B CB  1 
ATOM   3167 C  CG  . GLU B 1 148 ? 49.176 -17.763 97.403  1.00 20.19 ?  148 GLU B CG  1 
ATOM   3168 C  CD  . GLU B 1 148 ? 50.193 -16.971 98.221  1.00 27.79 ?  148 GLU B CD  1 
ATOM   3169 O  OE1 . GLU B 1 148 ? 50.602 -15.866 97.792  1.00 22.46 ?  148 GLU B OE1 1 
ATOM   3170 O  OE2 . GLU B 1 148 ? 50.579 -17.462 99.310  1.00 27.88 -1 148 GLU B OE2 1 
ATOM   3171 N  N   . GLN B 1 149 ? 48.533 -15.161 93.340  1.00 15.42 ?  149 GLN B N   1 
ATOM   3172 C  CA  . GLN B 1 149 ? 47.800 -14.491 92.268  1.00 17.34 ?  149 GLN B CA  1 
ATOM   3173 C  C   . GLN B 1 149 ? 48.442 -14.747 90.915  1.00 15.89 ?  149 GLN B C   1 
ATOM   3174 O  O   . GLN B 1 149 ? 48.066 -14.111 89.923  1.00 19.17 ?  149 GLN B O   1 
ATOM   3175 C  CB  . GLN B 1 149 ? 47.687 -12.992 92.552  1.00 17.99 ?  149 GLN B CB  1 
ATOM   3176 C  CG  . GLN B 1 149 ? 46.830 -12.742 93.792  1.00 20.37 ?  149 GLN B CG  1 
ATOM   3177 C  CD  . GLN B 1 149 ? 46.736 -11.287 94.193  1.00 24.73 ?  149 GLN B CD  1 
ATOM   3178 O  OE1 . GLN B 1 149 ? 46.722 -10.972 95.383  1.00 28.96 ?  149 GLN B OE1 1 
ATOM   3179 N  NE2 . GLN B 1 149 ? 46.638 -10.395 93.217  1.00 21.84 ?  149 GLN B NE2 1 
ATOM   3180 N  N   . ALA B 1 150 ? 49.377 -15.685 90.855  1.00 13.71 ?  150 ALA B N   1 
ATOM   3181 C  CA  . ALA B 1 150 ? 49.982 -16.136 89.609  1.00 14.55 ?  150 ALA B CA  1 
ATOM   3182 C  C   . ALA B 1 150 ? 49.513 -17.551 89.294  1.00 16.17 ?  150 ALA B C   1 
ATOM   3183 O  O   . ALA B 1 150 ? 49.475 -18.418 90.179  1.00 15.78 ?  150 ALA B O   1 
ATOM   3184 C  CB  . ALA B 1 150 ? 51.502 -16.116 89.712  1.00 16.34 ?  150 ALA B CB  1 
ATOM   3185 N  N   . VAL B 1 151 ? 49.146 -17.790 88.031  1.00 13.95 ?  151 VAL B N   1 
ATOM   3186 C  CA  . VAL B 1 151 ? 48.698 -19.100 87.582  1.00 13.78 ?  151 VAL B CA  1 
ATOM   3187 C  C   . VAL B 1 151 ? 49.533 -19.489 86.370  1.00 15.79 ?  151 VAL B C   1 
ATOM   3188 O  O   . VAL B 1 151 ? 49.517 -18.779 85.354  1.00 14.72 ?  151 VAL B O   1 
ATOM   3189 C  CB  . VAL B 1 151 ? 47.205 -19.109 87.223  1.00 14.57 ?  151 VAL B CB  1 
ATOM   3190 C  CG1 . VAL B 1 151 ? 46.796 -20.490 86.712  1.00 17.75 ?  151 VAL B CG1 1 
ATOM   3191 C  CG2 . VAL B 1 151 ? 46.358 -18.667 88.420  1.00 17.54 ?  151 VAL B CG2 1 
ATOM   3192 N  N   . LEU B 1 152 ? 50.275 -20.590 86.482  1.00 13.21 ?  152 LEU B N   1 
ATOM   3193 C  CA  . LEU B 1 152 ? 51.015 -21.126 85.344  1.00 12.81 ?  152 LEU B CA  1 
ATOM   3194 C  C   . LEU B 1 152 ? 50.063 -21.944 84.493  1.00 16.95 ?  152 LEU B C   1 
ATOM   3195 O  O   . LEU B 1 152 ? 49.394 -22.852 84.996  1.00 18.20 ?  152 LEU B O   1 
ATOM   3196 C  CB  . LEU B 1 152 ? 52.182 -21.989 85.816  1.00 16.20 ?  152 LEU B CB  1 
ATOM   3197 C  CG  . LEU B 1 152 ? 53.373 -21.213 86.369  1.00 15.07 ?  152 LEU B CG  1 
ATOM   3198 C  CD1 . LEU B 1 152 ? 54.303 -22.122 87.151  1.00 17.27 ?  152 LEU B CD1 1 
ATOM   3199 C  CD2 . LEU B 1 152 ? 54.149 -20.511 85.265  1.00 16.76 ?  152 LEU B CD2 1 
ATOM   3200 N  N   . VAL B 1 153 ? 49.993 -21.623 83.209  1.00 13.95 ?  153 VAL B N   1 
ATOM   3201 C  CA  . VAL B 1 153 ? 49.049 -22.273 82.301  1.00 14.23 ?  153 VAL B CA  1 
ATOM   3202 C  C   . VAL B 1 153 ? 49.835 -22.935 81.181  1.00 14.83 ?  153 VAL B C   1 
ATOM   3203 O  O   . VAL B 1 153 ? 50.551 -22.250 80.436  1.00 14.14 ?  153 VAL B O   1 
ATOM   3204 C  CB  . VAL B 1 153 ? 48.037 -21.268 81.730  1.00 12.92 ?  153 VAL B CB  1 
ATOM   3205 C  CG1 . VAL B 1 153 ? 47.007 -21.974 80.850  1.00 15.26 ?  153 VAL B CG1 1 
ATOM   3206 C  CG2 . VAL B 1 153 ? 47.350 -20.486 82.863  1.00 16.04 ?  153 VAL B CG2 1 
ATOM   3207 N  N   . GLY B 1 154 ? 49.702 -24.253 81.055  1.00 15.25 ?  154 GLY B N   1 
ATOM   3208 C  CA  . GLY B 1 154 ? 50.362 -24.992 80.002  1.00 12.80 ?  154 GLY B CA  1 
ATOM   3209 C  C   . GLY B 1 154 ? 51.722 -25.541 80.360  1.00 15.48 ?  154 GLY B C   1 
ATOM   3210 O  O   . GLY B 1 154 ? 52.332 -26.221 79.530  1.00 17.61 ?  154 GLY B O   1 
ATOM   3211 N  N   A SER B 1 155 ? 52.219 -25.269 81.565  0.52 16.27 ?  155 SER B N   1 
ATOM   3212 N  N   B SER B 1 155 ? 52.202 -25.297 81.574  0.48 16.26 ?  155 SER B N   1 
ATOM   3213 C  CA  A SER B 1 155 ? 53.598 -25.590 81.912  0.52 17.25 ?  155 SER B CA  1 
ATOM   3214 C  CA  B SER B 1 155 ? 53.537 -25.732 81.949  0.48 17.24 ?  155 SER B CA  1 
ATOM   3215 C  C   A SER B 1 155 ? 53.763 -27.084 82.157  0.52 18.77 ?  155 SER B C   1 
ATOM   3216 C  C   B SER B 1 155 ? 53.610 -27.253 82.018  0.48 19.04 ?  155 SER B C   1 
ATOM   3217 O  O   A SER B 1 155 ? 52.924 -27.718 82.805  0.52 19.81 ?  155 SER B O   1 
ATOM   3218 O  O   B SER B 1 155 ? 52.628 -27.936 82.325  0.48 19.21 ?  155 SER B O   1 
ATOM   3219 C  CB  A SER B 1 155 ? 54.033 -24.798 83.147  0.52 17.40 ?  155 SER B CB  1 
ATOM   3220 C  CB  B SER B 1 155 ? 53.936 -25.119 83.289  0.48 18.13 ?  155 SER B CB  1 
ATOM   3221 O  OG  A SER B 1 155 ? 53.835 -23.405 82.959  0.52 16.42 ?  155 SER B OG  1 
ATOM   3222 O  OG  B SER B 1 155 ? 53.541 -23.762 83.350  0.48 16.40 ?  155 SER B OG  1 
ATOM   3223 N  N   A ARG B 1 156 ? 54.858 -27.643 81.637  0.52 19.03 ?  156 ARG B N   1 
ATOM   3224 N  N   B ARG B 1 156 ? 54.793 -27.780 81.715  0.48 19.20 ?  156 ARG B N   1 
ATOM   3225 C  CA  A ARG B 1 156 ? 55.036 -29.090 81.628  0.52 20.47 ?  156 ARG B CA  1 
ATOM   3226 C  CA  B ARG B 1 156 ? 54.985 -29.220 81.659  0.48 20.41 ?  156 ARG B CA  1 
ATOM   3227 C  C   A ARG B 1 156 ? 56.506 -29.481 81.714  0.52 22.36 ?  156 ARG B C   1 
ATOM   3228 C  C   B ARG B 1 156 ? 56.471 -29.513 81.787  0.48 22.40 ?  156 ARG B C   1 
ATOM   3229 O  O   A ARG B 1 156 ? 56.825 -30.626 82.053  0.52 29.18 ?  156 ARG B O   1 
ATOM   3230 O  O   B ARG B 1 156 ? 57.315 -28.661 81.503  0.48 20.29 ?  156 ARG B O   1 
ATOM   3231 C  CB  A ARG B 1 156 ? 54.406 -29.688 80.369  0.52 22.69 ?  156 ARG B CB  1 
ATOM   3232 C  CB  B ARG B 1 156 ? 54.419 -29.810 80.360  0.48 22.73 ?  156 ARG B CB  1 
ATOM   3233 C  CG  A ARG B 1 156 ? 55.019 -29.170 79.068  0.52 23.33 ?  156 ARG B CG  1 
ATOM   3234 C  CG  B ARG B 1 156 ? 54.998 -29.192 79.086  0.48 23.32 ?  156 ARG B CG  1 
ATOM   3235 C  CD  A ARG B 1 156 ? 54.026 -29.266 77.930  0.52 24.90 ?  156 ARG B CD  1 
ATOM   3236 C  CD  B ARG B 1 156 ? 54.086 -29.427 77.892  0.48 24.87 ?  156 ARG B CD  1 
ATOM   3237 N  NE  A ARG B 1 156 ? 54.538 -28.734 76.669  0.52 23.51 ?  156 ARG B NE  1 
ATOM   3238 N  NE  B ARG B 1 156 ? 54.621 -28.880 76.645  0.48 23.40 ?  156 ARG B NE  1 
ATOM   3239 C  CZ  A ARG B 1 156 ? 54.281 -27.508 76.212  0.52 21.26 ?  156 ARG B CZ  1 
ATOM   3240 C  CZ  B ARG B 1 156 ? 54.387 -27.645 76.200  0.48 21.54 ?  156 ARG B CZ  1 
ATOM   3241 N  NH1 A ARG B 1 156 ? 54.771 -27.124 75.042  0.52 22.20 ?  156 ARG B NH1 1 
ATOM   3242 N  NH1 B ARG B 1 156 ? 53.628 -26.806 76.902  0.48 19.77 ?  156 ARG B NH1 1 
ATOM   3243 N  NH2 A ARG B 1 156 ? 53.517 -26.675 76.916  0.52 19.51 ?  156 ARG B NH2 1 
ATOM   3244 N  NH2 B ARG B 1 156 ? 54.904 -27.254 75.043  0.48 22.37 ?  156 ARG B NH2 1 
ATOM   3245 N  N   A ASP B 1 157 ? 57.409 -28.551 81.401  0.52 20.42 ?  157 ASP B N   1 
ATOM   3246 N  N   B ASP B 1 157 ? 56.771 -30.735 82.240  0.48 28.83 ?  157 ASP B N   1 
ATOM   3247 C  CA  A ASP B 1 157 ? 58.848 -28.818 81.461  0.52 23.11 ?  157 ASP B CA  1 
ATOM   3248 C  CA  B ASP B 1 157 ? 58.139 -31.252 82.336  0.48 26.60 ?  157 ASP B CA  1 
ATOM   3249 C  C   A ASP B 1 157 ? 59.398 -28.175 82.728  0.52 25.83 ?  157 ASP B C   1 
ATOM   3250 C  C   B ASP B 1 157 ? 59.031 -30.383 83.218  0.48 25.66 ?  157 ASP B C   1 
ATOM   3251 O  O   A ASP B 1 157 ? 60.056 -27.135 82.702  0.52 25.18 ?  157 ASP B O   1 
ATOM   3252 O  O   B ASP B 1 157 ? 60.229 -30.248 82.964  0.48 26.41 ?  157 ASP B O   1 
ATOM   3253 C  CB  A ASP B 1 157 ? 59.555 -28.301 80.214  0.52 24.47 ?  157 ASP B CB  1 
ATOM   3254 C  CB  B ASP B 1 157 ? 58.767 -31.418 80.949  0.48 27.21 ?  157 ASP B CB  1 
ATOM   3255 C  CG  A ASP B 1 157 ? 60.992 -28.793 80.109  0.52 30.07 ?  157 ASP B CG  1 
ATOM   3256 C  CG  B ASP B 1 157 ? 59.218 -32.842 80.683  0.48 33.98 ?  157 ASP B CG  1 
ATOM   3257 O  OD1 A ASP B 1 157 ? 61.427 -29.579 80.981  0.52 29.59 ?  157 ASP B OD1 1 
ATOM   3258 O  OD1 B ASP B 1 157 ? 58.350 -33.737 80.593  0.48 37.33 ?  157 ASP B OD1 1 
ATOM   3259 O  OD2 A ASP B 1 157 ? 61.688 -28.393 79.154  0.52 32.68 -1 157 ASP B OD2 1 
ATOM   3260 O  OD2 B ASP B 1 157 ? 60.441 -33.066 80.571  0.48 39.85 -1 157 ASP B OD2 1 
ATOM   3261 N  N   A ILE B 1 158 ? 59.114 -28.818 83.856  0.52 24.62 ?  158 ILE B N   1 
ATOM   3262 N  N   B ILE B 1 158 ? 58.457 -29.796 84.267  0.48 24.54 ?  158 ILE B N   1 
ATOM   3263 C  CA  A ILE B 1 158 ? 59.515 -28.335 85.172  0.52 26.40 ?  158 ILE B CA  1 
ATOM   3264 C  CA  B ILE B 1 158 ? 59.228 -28.967 85.185  0.48 27.93 ?  158 ILE B CA  1 
ATOM   3265 C  C   A ILE B 1 158 ? 60.104 -29.509 85.949  0.52 24.07 ?  158 ILE B C   1 
ATOM   3266 C  C   B ILE B 1 158 ? 60.153 -29.858 86.003  0.48 23.50 ?  158 ILE B C   1 
ATOM   3267 O  O   A ILE B 1 158 ? 59.399 -30.475 86.266  0.52 28.32 ?  158 ILE B O   1 
ATOM   3268 O  O   B ILE B 1 158 ? 59.762 -30.960 86.409  0.48 30.30 ?  158 ILE B O   1 
ATOM   3269 C  CB  A ILE B 1 158 ? 58.355 -27.698 85.948  0.52 25.63 ?  158 ILE B CB  1 
ATOM   3270 C  CB  B ILE B 1 158 ? 58.261 -28.174 86.083  0.48 24.80 ?  158 ILE B CB  1 
ATOM   3271 C  CG1 A ILE B 1 158 ? 57.556 -26.741 85.058  0.52 23.37 ?  158 ILE B CG1 1 
ATOM   3272 C  CG1 B ILE B 1 158 ? 57.151 -27.540 85.230  0.48 24.97 ?  158 ILE B CG1 1 
ATOM   3273 C  CG2 A ILE B 1 158 ? 58.887 -26.940 87.148  0.52 26.04 ?  158 ILE B CG2 1 
ATOM   3274 C  CG2 B ILE B 1 158 ? 59.009 -27.138 86.909  0.48 26.09 ?  158 ILE B CG2 1 
ATOM   3275 C  CD1 A ILE B 1 158 ? 56.268 -26.268 85.697  0.52 24.31 ?  158 ILE B CD1 1 
ATOM   3276 C  CD1 B ILE B 1 158 ? 55.936 -27.077 86.023  0.48 24.60 ?  158 ILE B CD1 1 
ATOM   3277 N  N   . ASP B 1 159 ? 61.390 -29.411 86.251  1.00 29.48 ?  159 ASP B N   1 
ATOM   3278 C  CA  . ASP B 1 159 ? 62.181 -30.323 87.064  1.00 30.72 ?  159 ASP B CA  1 
ATOM   3279 C  C   . ASP B 1 159 ? 61.745 -30.255 88.528  1.00 32.31 ?  159 ASP B C   1 
ATOM   3280 O  O   . ASP B 1 159 ? 61.018 -29.350 88.952  1.00 30.04 ?  159 ASP B O   1 
ATOM   3281 C  CB  . ASP B 1 159 ? 63.671 -30.010 86.949  1.00 31.61 ?  159 ASP B CB  1 
ATOM   3282 C  CG  . ASP B 1 159 ? 64.019 -28.629 87.486  1.00 42.93 ?  159 ASP B CG  1 
ATOM   3283 O  OD1 . ASP B 1 159 ? 63.700 -27.625 86.812  1.00 50.52 -1 159 ASP B OD1 1 
ATOM   3284 O  OD2 . ASP B 1 159 ? 64.599 -28.546 88.593  1.00 45.61 ?  159 ASP B OD2 1 
ATOM   3285 N  N   . GLU B 1 160 ? 62.229 -31.222 89.311  1.00 33.48 ?  160 GLU B N   1 
ATOM   3286 C  CA  . GLU B 1 160 ? 61.714 -31.418 90.665  1.00 35.89 ?  160 GLU B CA  1 
ATOM   3287 C  C   . GLU B 1 160 ? 62.008 -30.222 91.565  1.00 33.08 ?  160 GLU B C   1 
ATOM   3288 O  O   . GLU B 1 160 ? 61.137 -29.786 92.330  1.00 27.42 ?  160 GLU B O   1 
ATOM   3289 C  CB  . GLU B 1 160 ? 62.296 -32.701 91.255  1.00 44.55 ?  160 GLU B CB  1 
ATOM   3290 C  CG  . GLU B 1 160 ? 61.786 -33.965 90.573  1.00 57.36 ?  160 GLU B CG  1 
ATOM   3291 C  CD  . GLU B 1 160 ? 62.456 -35.226 91.091  1.00 78.51 ?  160 GLU B CD  1 
ATOM   3292 O  OE1 . GLU B 1 160 ? 63.496 -35.627 90.522  1.00 76.57 ?  160 GLU B OE1 1 
ATOM   3293 O  OE2 . GLU B 1 160 ? 61.942 -35.817 92.066  1.00 80.37 -1 160 GLU B OE2 1 
ATOM   3294 N  N   . GLY B 1 161 ? 63.225 -29.678 91.495  1.00 28.48 ?  161 GLY B N   1 
ATOM   3295 C  CA  . GLY B 1 161 ? 63.570 -28.557 92.357  1.00 29.50 ?  161 GLY B CA  1 
ATOM   3296 C  C   . GLY B 1 161 ? 62.726 -27.327 92.079  1.00 30.61 ?  161 GLY B C   1 
ATOM   3297 O  O   . GLY B 1 161 ? 62.266 -26.654 93.005  1.00 24.61 ?  161 GLY B O   1 
ATOM   3298 N  N   . GLU B 1 162 ? 62.503 -27.025 90.798  1.00 24.57 ?  162 GLU B N   1 
ATOM   3299 C  CA  . GLU B 1 162 ? 61.658 -25.896 90.433  1.00 26.46 ?  162 GLU B CA  1 
ATOM   3300 C  C   . GLU B 1 162 ? 60.212 -26.144 90.835  1.00 20.07 ?  162 GLU B C   1 
ATOM   3301 O  O   . GLU B 1 162 ? 59.542 -25.234 91.347  1.00 19.19 ?  162 GLU B O   1 
ATOM   3302 C  CB  . GLU B 1 162 ? 61.756 -25.637 88.926  1.00 22.92 ?  162 GLU B CB  1 
ATOM   3303 C  CG  . GLU B 1 162 ? 61.116 -24.336 88.495  1.00 21.53 ?  162 GLU B CG  1 
ATOM   3304 C  CD  . GLU B 1 162 ? 61.168 -24.124 86.989  1.00 26.32 ?  162 GLU B CD  1 
ATOM   3305 O  OE1 . GLU B 1 162 ? 61.535 -25.069 86.252  1.00 25.82 ?  162 GLU B OE1 1 
ATOM   3306 O  OE2 . GLU B 1 162 ? 60.841 -23.005 86.549  1.00 26.52 -1 162 GLU B OE2 1 
ATOM   3307 N  N   A ARG B 1 163 ? 59.712 -27.363 90.598  0.44 22.00 ?  163 ARG B N   1 
ATOM   3308 N  N   B ARG B 1 163 ? 59.714 -27.364 90.603  0.56 21.98 ?  163 ARG B N   1 
ATOM   3309 C  CA  A ARG B 1 163 ? 58.348 -27.706 90.989  0.44 21.23 ?  163 ARG B CA  1 
ATOM   3310 C  CA  B ARG B 1 163 ? 58.348 -27.708 90.984  0.56 21.19 ?  163 ARG B CA  1 
ATOM   3311 C  C   A ARG B 1 163 ? 58.140 -27.497 92.481  0.44 22.58 ?  163 ARG B C   1 
ATOM   3312 C  C   B ARG B 1 163 ? 58.129 -27.539 92.478  0.56 22.58 ?  163 ARG B C   1 
ATOM   3313 O  O   A ARG B 1 163 ? 57.071 -27.045 92.909  0.44 20.15 ?  163 ARG B O   1 
ATOM   3314 O  O   B ARG B 1 163 ? 57.033 -27.159 92.904  0.56 20.18 ?  163 ARG B O   1 
ATOM   3315 C  CB  A ARG B 1 163 ? 58.030 -29.154 90.603  0.44 26.00 ?  163 ARG B CB  1 
ATOM   3316 C  CB  B ARG B 1 163 ? 58.024 -29.144 90.559  0.56 26.01 ?  163 ARG B CB  1 
ATOM   3317 C  CG  A ARG B 1 163 ? 57.495 -29.318 89.190  0.44 25.82 ?  163 ARG B CG  1 
ATOM   3318 C  CG  B ARG B 1 163 ? 56.543 -29.513 90.633  0.56 26.45 ?  163 ARG B CG  1 
ATOM   3319 C  CD  A ARG B 1 163 ? 56.998 -30.731 88.905  0.44 27.55 ?  163 ARG B CD  1 
ATOM   3320 C  CD  B ARG B 1 163 ? 55.737 -28.760 89.583  0.56 28.03 ?  163 ARG B CD  1 
ATOM   3321 N  NE  A ARG B 1 163 ? 56.772 -30.943 87.475  0.44 26.89 ?  163 ARG B NE  1 
ATOM   3322 N  NE  B ARG B 1 163 ? 54.294 -28.964 89.698  0.56 27.73 ?  163 ARG B NE  1 
ATOM   3323 C  CZ  A ARG B 1 163 ? 55.660 -30.601 86.829  0.44 30.59 ?  163 ARG B CZ  1 
ATOM   3324 C  CZ  B ARG B 1 163 ? 53.531 -28.400 90.630  0.56 28.19 ?  163 ARG B CZ  1 
ATOM   3325 N  NH1 A ARG B 1 163 ? 54.655 -30.027 87.481  0.44 30.00 ?  163 ARG B NH1 1 
ATOM   3326 N  NH1 B ARG B 1 163 ? 54.069 -27.601 91.547  0.56 24.89 ?  163 ARG B NH1 1 
ATOM   3327 N  NH2 A ARG B 1 163 ? 55.551 -30.832 85.526  0.44 25.59 ?  163 ARG B NH2 1 
ATOM   3328 N  NH2 B ARG B 1 163 ? 52.224 -28.637 90.654  0.56 30.44 ?  163 ARG B NH2 1 
ATOM   3329 N  N   . GLU B 1 164 ? 59.160 -27.798 93.286  1.00 21.07 ?  164 GLU B N   1 
ATOM   3330 C  CA  . GLU B 1 164 ? 59.031 -27.620 94.732  1.00 21.83 ?  164 GLU B CA  1 
ATOM   3331 C  C   . GLU B 1 164 ? 58.982 -26.142 95.113  1.00 20.46 ?  164 GLU B C   1 
ATOM   3332 O  O   . GLU B 1 164 ? 58.243 -25.758 96.027  1.00 19.76 ?  164 GLU B O   1 
ATOM   3333 C  CB  . GLU B 1 164 ? 60.180 -28.327 95.451  1.00 23.35 ?  164 GLU B CB  1 
ATOM   3334 C  CG  . GLU B 1 164 ? 60.391 -27.879 96.897  1.00 25.32 ?  164 GLU B CG  1 
ATOM   3335 C  CD  . GLU B 1 164 ? 59.219 -28.241 97.793  1.00 23.24 ?  164 GLU B CD  1 
ATOM   3336 O  OE1 . GLU B 1 164 ? 59.142 -27.685 98.911  1.00 30.10 ?  164 GLU B OE1 1 
ATOM   3337 O  OE2 . GLU B 1 164 ? 58.377 -29.066 97.377  1.00 25.40 -1 164 GLU B OE2 1 
ATOM   3338 N  N   . LEU B 1 165 ? 59.742 -25.287 94.417  1.00 20.85 ?  165 LEU B N   1 
ATOM   3339 C  CA  . LEU B 1 165 ? 59.645 -23.849 94.668  1.00 17.29 ?  165 LEU B CA  1 
ATOM   3340 C  C   . LEU B 1 165 ? 58.252 -23.333 94.320  1.00 16.53 ?  165 LEU B C   1 
ATOM   3341 O  O   . LEU B 1 165 ? 57.680 -22.500 95.036  1.00 17.09 ?  165 LEU B O   1 
ATOM   3342 C  CB  . LEU B 1 165 ? 60.693 -23.096 93.841  1.00 21.69 ?  165 LEU B CB  1 
ATOM   3343 C  CG  . LEU B 1 165 ? 62.169 -23.246 94.209  1.00 27.61 ?  165 LEU B CG  1 
ATOM   3344 C  CD1 . LEU B 1 165 ? 63.021 -22.348 93.315  1.00 28.87 ?  165 LEU B CD1 1 
ATOM   3345 C  CD2 . LEU B 1 165 ? 62.396 -22.915 95.679  1.00 30.69 ?  165 LEU B CD2 1 
ATOM   3346 N  N   . ILE B 1 166 ? 57.709 -23.815 93.201  1.00 17.08 ?  166 ILE B N   1 
ATOM   3347 C  CA  . ILE B 1 166 ? 56.369 -23.446 92.760  1.00 18.17 ?  166 ILE B CA  1 
ATOM   3348 C  C   . ILE B 1 166 ? 55.339 -23.876 93.796  1.00 17.09 ?  166 ILE B C   1 
ATOM   3349 O  O   . ILE B 1 166 ? 54.479 -23.086 94.206  1.00 16.18 ?  166 ILE B O   1 
ATOM   3350 C  CB  . ILE B 1 166 ? 56.093 -24.074 91.380  1.00 17.04 ?  166 ILE B CB  1 
ATOM   3351 C  CG1 . ILE B 1 166 ? 56.938 -23.383 90.304  1.00 16.01 ?  166 ILE B CG1 1 
ATOM   3352 C  CG2 . ILE B 1 166 ? 54.602 -23.993 91.037  1.00 19.29 ?  166 ILE B CG2 1 
ATOM   3353 C  CD1 . ILE B 1 166 ? 56.984 -24.147 88.989  1.00 17.11 ?  166 ILE B CD1 1 
ATOM   3354 N  N   . ARG B 1 167 ? 55.425 -25.138 94.233  1.00 16.69 ?  167 ARG B N   1 
ATOM   3355 C  CA  . ARG B 1 167 ? 54.500 -25.668 95.234  1.00 17.54 ?  167 ARG B CA  1 
ATOM   3356 C  C   . ARG B 1 167 ? 54.564 -24.858 96.524  1.00 17.85 ?  167 ARG B C   1 
ATOM   3357 O  O   . ARG B 1 167 ? 53.529 -24.402 97.035  1.00 18.60 ?  167 ARG B O   1 
ATOM   3358 C  CB  . ARG B 1 167 ? 54.803 -27.145 95.507  1.00 18.47 ?  167 ARG B CB  1 
ATOM   3359 C  CG  . ARG B 1 167 ? 53.895 -27.757 96.599  1.00 19.12 ?  167 ARG B CG  1 
ATOM   3360 C  CD  . ARG B 1 167 ? 54.591 -28.868 97.380  1.00 21.65 ?  167 ARG B CD  1 
ATOM   3361 N  NE  . ARG B 1 167 ? 55.678 -28.385 98.219  1.00 19.40 ?  167 ARG B NE  1 
ATOM   3362 C  CZ  . ARG B 1 167 ? 55.525 -27.679 99.339  1.00 24.07 ?  167 ARG B CZ  1 
ATOM   3363 N  NH1 . ARG B 1 167 ? 54.305 -27.359 99.776  1.00 20.09 ?  167 ARG B NH1 1 
ATOM   3364 N  NH2 . ARG B 1 167 ? 56.597 -27.286 100.021 1.00 21.42 ?  167 ARG B NH2 1 
ATOM   3365 N  N   . LYS B 1 168 ? 55.771 -24.666 97.067  1.00 18.33 ?  168 LYS B N   1 
ATOM   3366 C  CA  . LYS B 1 168 ? 55.920 -23.953 98.334  1.00 19.71 ?  168 LYS B CA  1 
ATOM   3367 C  C   . LYS B 1 168 ? 55.406 -22.522 98.245  1.00 19.30 ?  168 LYS B C   1 
ATOM   3368 O  O   . LYS B 1 168 ? 54.855 -21.992 99.218  1.00 18.55 ?  168 LYS B O   1 
ATOM   3369 C  CB  . LYS B 1 168 ? 57.393 -23.976 98.773  1.00 21.66 ?  168 LYS B CB  1 
ATOM   3370 C  CG  . LYS B 1 168 ? 57.668 -23.282 100.112 1.00 25.26 ?  168 LYS B CG  1 
ATOM   3371 C  CD  . LYS B 1 168 ? 59.146 -22.961 100.303 1.00 39.46 ?  168 LYS B CD  1 
ATOM   3372 C  CE  . LYS B 1 168 ? 60.023 -24.151 99.957  1.00 44.73 ?  168 LYS B CE  1 
ATOM   3373 N  NZ  . LYS B 1 168 ? 61.376 -23.743 99.464  1.00 49.48 ?  168 LYS B NZ  1 
ATOM   3374 N  N   . ALA B 1 169 ? 55.554 -21.879 97.084  1.00 15.22 ?  169 ALA B N   1 
ATOM   3375 C  CA  . ALA B 1 169 ? 55.111 -20.499 96.937  1.00 15.04 ?  169 ALA B CA  1 
ATOM   3376 C  C   . ALA B 1 169 ? 53.603 -20.363 96.772  1.00 17.59 ?  169 ALA B C   1 
ATOM   3377 O  O   . ALA B 1 169 ? 53.080 -19.262 96.959  1.00 16.75 ?  169 ALA B O   1 
ATOM   3378 C  CB  . ALA B 1 169 ? 55.828 -19.859 95.738  1.00 16.33 ?  169 ALA B CB  1 
ATOM   3379 N  N   . GLY B 1 170 ? 52.901 -21.435 96.421  1.00 17.46 ?  170 GLY B N   1 
ATOM   3380 C  CA  . GLY B 1 170 ? 51.476 -21.352 96.201  1.00 15.01 ?  170 GLY B CA  1 
ATOM   3381 C  C   . GLY B 1 170 ? 51.072 -20.963 94.798  1.00 17.90 ?  170 GLY B C   1 
ATOM   3382 O  O   . GLY B 1 170 ? 49.950 -20.490 94.606  1.00 17.17 ?  170 GLY B O   1 
ATOM   3383 N  N   . VAL B 1 171 ? 51.945 -21.156 93.813  1.00 15.44 ?  171 VAL B N   1 
ATOM   3384 C  CA  . VAL B 1 171 ? 51.615 -20.870 92.416  1.00 16.93 ?  171 VAL B CA  1 
ATOM   3385 C  C   . VAL B 1 171 ? 50.856 -22.059 91.834  1.00 15.11 ?  171 VAL B C   1 
ATOM   3386 O  O   . VAL B 1 171 ? 51.377 -23.178 91.796  1.00 18.51 ?  171 VAL B O   1 
ATOM   3387 C  CB  . VAL B 1 171 ? 52.882 -20.576 91.601  1.00 16.78 ?  171 VAL B CB  1 
ATOM   3388 C  CG1 . VAL B 1 171 ? 52.538 -20.430 90.110  1.00 16.29 ?  171 VAL B CG1 1 
ATOM   3389 C  CG2 . VAL B 1 171 ? 53.550 -19.321 92.108  1.00 18.48 ?  171 VAL B CG2 1 
ATOM   3390 N  N   . ARG B 1 172 ? 49.624 -21.820 91.383  1.00 15.56 ?  172 ARG B N   1 
ATOM   3391 C  CA  . ARG B 1 172 ? 48.823 -22.874 90.767  1.00 17.55 ?  172 ARG B CA  1 
ATOM   3392 C  C   . ARG B 1 172 ? 49.358 -23.230 89.382  1.00 18.32 ?  172 ARG B C   1 
ATOM   3393 O  O   . ARG B 1 172 ? 49.806 -22.353 88.634  1.00 16.87 ?  172 ARG B O   1 
ATOM   3394 C  CB  . ARG B 1 172 ? 47.352 -22.436 90.662  1.00 19.63 ?  172 ARG B CB  1 
ATOM   3395 C  CG  . ARG B 1 172 ? 46.629 -22.305 92.024  1.00 17.97 ?  172 ARG B CG  1 
ATOM   3396 C  CD  . ARG B 1 172 ? 45.366 -21.457 91.917  1.00 22.79 ?  172 ARG B CD  1 
ATOM   3397 N  NE  . ARG B 1 172 ? 45.650 -20.026 91.982  1.00 20.11 ?  172 ARG B NE  1 
ATOM   3398 C  CZ  . ARG B 1 172 ? 44.760 -19.078 91.705  1.00 20.34 ?  172 ARG B CZ  1 
ATOM   3399 N  NH1 . ARG B 1 172 ? 43.527 -19.412 91.340  1.00 23.80 ?  172 ARG B NH1 1 
ATOM   3400 N  NH2 . ARG B 1 172 ? 45.093 -17.801 91.786  1.00 21.85 ?  172 ARG B NH2 1 
ATOM   3401 N  N   . VAL B 1 173 ? 49.316 -24.519 89.043  1.00 16.23 ?  173 VAL B N   1 
ATOM   3402 C  CA  . VAL B 1 173 ? 49.771 -25.021 87.743  1.00 15.59 ?  173 VAL B CA  1 
ATOM   3403 C  C   . VAL B 1 173 ? 48.610 -25.728 87.054  1.00 21.17 ?  173 VAL B C   1 
ATOM   3404 O  O   . VAL B 1 173 ? 48.074 -26.711 87.581  1.00 20.34 ?  173 VAL B O   1 
ATOM   3405 C  CB  . VAL B 1 173 ? 50.975 -25.967 87.887  1.00 17.31 ?  173 VAL B CB  1 
ATOM   3406 C  CG1 . VAL B 1 173 ? 51.379 -26.547 86.526  1.00 21.03 ?  173 VAL B CG1 1 
ATOM   3407 C  CG2 . VAL B 1 173 ? 52.148 -25.254 88.556  1.00 19.71 ?  173 VAL B CG2 1 
ATOM   3408 N  N   . ILE B 1 174 ? 48.224 -25.232 85.882  1.00 16.66 ?  174 ILE B N   1 
ATOM   3409 C  CA  . ILE B 1 174 ? 47.199 -25.881 85.062  1.00 15.52 ?  174 ILE B CA  1 
ATOM   3410 C  C   . ILE B 1 174 ? 47.883 -26.491 83.845  1.00 17.79 ?  174 ILE B C   1 
ATOM   3411 O  O   . ILE B 1 174 ? 48.219 -25.769 82.892  1.00 18.36 ?  174 ILE B O   1 
ATOM   3412 C  CB  . ILE B 1 174 ? 46.098 -24.894 84.638  1.00 15.05 ?  174 ILE B CB  1 
ATOM   3413 C  CG1 . ILE B 1 174 ? 45.501 -24.184 85.858  1.00 15.63 ?  174 ILE B CG1 1 
ATOM   3414 C  CG2 . ILE B 1 174 ? 45.018 -25.603 83.803  1.00 14.14 ?  174 ILE B CG2 1 
ATOM   3415 C  CD1 . ILE B 1 174 ? 44.463 -23.120 85.487  1.00 17.47 ?  174 ILE B CD1 1 
ATOM   3416 N  N   . PRO B 1 175 ? 48.125 -27.792 83.823  1.00 16.16 ?  175 PRO B N   1 
ATOM   3417 C  CA  . PRO B 1 175 ? 48.888 -28.387 82.723  1.00 18.32 ?  175 PRO B CA  1 
ATOM   3418 C  C   . PRO B 1 175 ? 48.055 -28.436 81.454  1.00 16.34 ?  175 PRO B C   1 
ATOM   3419 O  O   . PRO B 1 175 ? 46.838 -28.219 81.502  1.00 17.50 ?  175 PRO B O   1 
ATOM   3420 C  CB  . PRO B 1 175 ? 49.214 -29.795 83.247  1.00 23.30 ?  175 PRO B CB  1 
ATOM   3421 C  CG  . PRO B 1 175 ? 48.077 -30.098 84.174  1.00 24.75 ?  175 PRO B CG  1 
ATOM   3422 C  CD  . PRO B 1 175 ? 47.701 -28.792 84.818  1.00 23.32 ?  175 PRO B CD  1 
ATOM   3423 N  N   . PRO B 1 176 ? 48.676 -28.697 80.303  1.00 17.31 ?  176 PRO B N   1 
ATOM   3424 C  CA  . PRO B 1 176 ? 47.927 -28.622 79.035  1.00 18.21 ?  176 PRO B CA  1 
ATOM   3425 C  C   . PRO B 1 176 ? 46.642 -29.428 79.000  1.00 23.72 ?  176 PRO B C   1 
ATOM   3426 O  O   . PRO B 1 176 ? 45.640 -28.928 78.480  1.00 20.85 ?  176 PRO B O   1 
ATOM   3427 C  CB  . PRO B 1 176 ? 48.941 -29.140 77.998  1.00 19.69 ?  176 PRO B CB  1 
ATOM   3428 C  CG  . PRO B 1 176 ? 50.260 -28.834 78.594  1.00 21.22 ?  176 PRO B CG  1 
ATOM   3429 C  CD  . PRO B 1 176 ? 50.110 -28.957 80.088  1.00 19.14 ?  176 PRO B CD  1 
ATOM   3430 N  N   . GLY B 1 177 ? 46.629 -30.646 79.550  1.00 19.43 ?  177 GLY B N   1 
ATOM   3431 C  CA  . GLY B 1 177 ? 45.421 -31.459 79.508  1.00 22.40 ?  177 GLY B CA  1 
ATOM   3432 C  C   . GLY B 1 177 ? 44.245 -30.886 80.275  1.00 22.18 ?  177 GLY B C   1 
ATOM   3433 O  O   . GLY B 1 177 ? 43.102 -31.293 80.036  1.00 25.33 ?  177 GLY B O   1 
ATOM   3434 N  N   . GLU B 1 178 ? 44.494 -29.962 81.196  1.00 20.03 ?  178 GLU B N   1 
ATOM   3435 C  CA  . GLU B 1 178 ? 43.450 -29.314 81.975  1.00 19.17 ?  178 GLU B CA  1 
ATOM   3436 C  C   . GLU B 1 178 ? 43.248 -27.855 81.594  1.00 16.90 ?  178 GLU B C   1 
ATOM   3437 O  O   . GLU B 1 178 ? 42.394 -27.183 82.187  1.00 18.69 ?  178 GLU B O   1 
ATOM   3438 C  CB  . GLU B 1 178 ? 43.785 -29.407 83.472  1.00 23.61 ?  178 GLU B CB  1 
ATOM   3439 C  CG  . GLU B 1 178 ? 43.934 -30.842 83.990  1.00 28.97 ?  178 GLU B CG  1 
ATOM   3440 C  CD  . GLU B 1 178 ? 44.591 -30.898 85.359  1.00 39.48 ?  178 GLU B CD  1 
ATOM   3441 O  OE1 . GLU B 1 178 ? 45.400 -31.818 85.595  1.00 45.52 ?  178 GLU B OE1 1 
ATOM   3442 O  OE2 . GLU B 1 178 ? 44.303 -30.015 86.197  1.00 42.40 -1 178 GLU B OE2 1 
ATOM   3443 N  N   . ALA B 1 179 ? 44.022 -27.336 80.635  1.00 18.04 ?  179 ALA B N   1 
ATOM   3444 C  CA  . ALA B 1 179 ? 44.043 -25.899 80.360  1.00 18.47 ?  179 ALA B CA  1 
ATOM   3445 C  C   . ALA B 1 179 ? 42.955 -25.564 79.348  1.00 19.75 ?  179 ALA B C   1 
ATOM   3446 O  O   . ALA B 1 179 ? 43.200 -25.333 78.157  1.00 19.62 ?  179 ALA B O   1 
ATOM   3447 C  CB  . ALA B 1 179 ? 45.422 -25.468 79.886  1.00 17.21 ?  179 ALA B CB  1 
ATOM   3448 N  N   . THR B 1 180 ? 41.731 -25.544 79.846  1.00 19.17 ?  180 THR B N   1 
ATOM   3449 C  CA  . THR B 1 180 ? 40.562 -25.129 79.090  1.00 18.37 ?  180 THR B CA  1 
ATOM   3450 C  C   . THR B 1 180 ? 40.171 -23.710 79.485  1.00 18.95 ?  180 THR B C   1 
ATOM   3451 O  O   . THR B 1 180 ? 40.605 -23.183 80.514  1.00 16.85 ?  180 THR B O   1 
ATOM   3452 C  CB  . THR B 1 180 ? 39.390 -26.077 79.350  1.00 23.22 ?  180 THR B CB  1 
ATOM   3453 O  OG1 . THR B 1 180 ? 38.947 -25.900 80.699  1.00 21.03 ?  180 THR B OG1 1 
ATOM   3454 C  CG2 . THR B 1 180 ? 39.804 -27.523 79.142  1.00 23.61 ?  180 THR B CG2 1 
ATOM   3455 N  N   . ALA B 1 181 ? 39.334 -23.093 78.648  1.00 19.59 ?  181 ALA B N   1 
ATOM   3456 C  CA  . ALA B 1 181 ? 38.809 -21.767 78.961  1.00 18.76 ?  181 ALA B CA  1 
ATOM   3457 C  C   . ALA B 1 181 ? 38.136 -21.737 80.331  1.00 16.35 ?  181 ALA B C   1 
ATOM   3458 O  O   . ALA B 1 181 ? 38.381 -20.826 81.133  1.00 17.83 ?  181 ALA B O   1 
ATOM   3459 C  CB  . ALA B 1 181 ? 37.837 -21.325 77.864  1.00 22.30 ?  181 ALA B CB  1 
ATOM   3460 N  N   . GLN B 1 182 ? 37.296 -22.741 80.627  1.00 17.56 ?  182 GLN B N   1 
ATOM   3461 C  CA  . GLN B 1 182 ? 36.595 -22.751 81.910  1.00 20.41 ?  182 GLN B CA  1 
ATOM   3462 C  C   . GLN B 1 182 ? 37.551 -22.957 83.081  1.00 15.53 ?  182 GLN B C   1 
ATOM   3463 O  O   . GLN B 1 182 ? 37.376 -22.337 84.133  1.00 17.59 ?  182 GLN B O   1 
ATOM   3464 C  CB  . GLN B 1 182 ? 35.506 -23.822 81.923  1.00 22.20 ?  182 GLN B CB  1 
ATOM   3465 C  CG  . GLN B 1 182 ? 34.544 -23.674 83.098  1.00 24.30 ?  182 GLN B CG  1 
ATOM   3466 C  CD  . GLN B 1 182 ? 33.836 -22.327 83.109  1.00 27.45 ?  182 GLN B CD  1 
ATOM   3467 O  OE1 . GLN B 1 182 ? 33.149 -21.968 82.153  1.00 35.27 ?  182 GLN B OE1 1 
ATOM   3468 N  NE2 . GLN B 1 182 ? 34.004 -21.574 84.192  1.00 25.64 ?  182 GLN B NE2 1 
ATOM   3469 N  N   . ALA B 1 183 ? 38.579 -23.800 82.922  1.00 15.46 ?  183 ALA B N   1 
ATOM   3470 C  CA  . ALA B 1 183 ? 39.547 -23.955 84.006  1.00 17.91 ?  183 ALA B CA  1 
ATOM   3471 C  C   . ALA B 1 183 ? 40.246 -22.635 84.306  1.00 16.78 ?  183 ALA B C   1 
ATOM   3472 O  O   . ALA B 1 183 ? 40.497 -22.300 85.472  1.00 17.39 ?  183 ALA B O   1 
ATOM   3473 C  CB  . ALA B 1 183 ? 40.574 -25.034 83.661  1.00 18.93 ?  183 ALA B CB  1 
ATOM   3474 N  N   . VAL B 1 184 ? 40.540 -21.855 83.264  1.00 14.64 ?  184 VAL B N   1 
ATOM   3475 C  CA  . VAL B 1 184 ? 41.200 -20.571 83.460  1.00 15.64 ?  184 VAL B CA  1 
ATOM   3476 C  C   . VAL B 1 184 ? 40.244 -19.556 84.082  1.00 16.24 ?  184 VAL B C   1 
ATOM   3477 O  O   . VAL B 1 184 ? 40.621 -18.808 84.994  1.00 17.85 ?  184 VAL B O   1 
ATOM   3478 C  CB  . VAL B 1 184 ? 41.776 -20.081 82.116  1.00 17.27 ?  184 VAL B CB  1 
ATOM   3479 C  CG1 . VAL B 1 184 ? 42.267 -18.668 82.244  1.00 21.70 ?  184 VAL B CG1 1 
ATOM   3480 C  CG2 . VAL B 1 184 ? 42.905 -21.017 81.657  1.00 16.41 ?  184 VAL B CG2 1 
ATOM   3481 N  N   . LEU B 1 185 ? 38.983 -19.530 83.627  1.00 17.89 ?  185 LEU B N   1 
ATOM   3482 C  CA  . LEU B 1 185 ? 37.993 -18.653 84.249  1.00 20.18 ?  185 LEU B CA  1 
ATOM   3483 C  C   . LEU B 1 185 ? 37.805 -18.984 85.722  1.00 20.51 ?  185 LEU B C   1 
ATOM   3484 O  O   . LEU B 1 185 ? 37.630 -18.082 86.549  1.00 21.30 ?  185 LEU B O   1 
ATOM   3485 C  CB  . LEU B 1 185 ? 36.653 -18.773 83.518  1.00 18.89 ?  185 LEU B CB  1 
ATOM   3486 C  CG  . LEU B 1 185 ? 36.553 -18.038 82.187  1.00 18.85 ?  185 LEU B CG  1 
ATOM   3487 C  CD1 . LEU B 1 185 ? 35.154 -18.223 81.620  1.00 22.45 ?  185 LEU B CD1 1 
ATOM   3488 C  CD2 . LEU B 1 185 ? 36.844 -16.553 82.368  1.00 21.66 ?  185 LEU B CD2 1 
ATOM   3489 N  N   . ASP B 1 186 ? 37.813 -20.276 86.069  1.00 19.29 ?  186 ASP B N   1 
ATOM   3490 C  CA  . ASP B 1 186 ? 37.673 -20.652 87.473  1.00 16.22 ?  186 ASP B CA  1 
ATOM   3491 C  C   . ASP B 1 186 ? 38.829 -20.109 88.297  1.00 22.25 ?  186 ASP B C   1 
ATOM   3492 O  O   . ASP B 1 186 ? 38.652 -19.700 89.450  1.00 24.81 ?  186 ASP B O   1 
ATOM   3493 C  CB  . ASP B 1 186 ? 37.602 -22.170 87.619  1.00 18.79 ?  186 ASP B CB  1 
ATOM   3494 C  CG  . ASP B 1 186 ? 36.271 -22.746 87.169  1.00 26.74 ?  186 ASP B CG  1 
ATOM   3495 O  OD1 . ASP B 1 186 ? 35.349 -21.972 86.837  1.00 24.27 ?  186 ASP B OD1 1 
ATOM   3496 O  OD2 . ASP B 1 186 ? 36.155 -23.988 87.151  1.00 27.46 -1 186 ASP B OD2 1 
ATOM   3497 N  N   . ALA B 1 187 ? 40.025 -20.088 87.713  1.00 17.40 ?  187 ALA B N   1 
ATOM   3498 C  CA  . ALA B 1 187 ? 41.197 -19.650 88.458  1.00 17.60 ?  187 ALA B CA  1 
ATOM   3499 C  C   . ALA B 1 187 ? 41.229 -18.141 88.658  1.00 22.11 ?  187 ALA B C   1 
ATOM   3500 O  O   . ALA B 1 187 ? 41.714 -17.672 89.697  1.00 22.55 ?  187 ALA B O   1 
ATOM   3501 C  CB  . ALA B 1 187 ? 42.464 -20.120 87.740  1.00 19.29 ?  187 ALA B CB  1 
ATOM   3502 N  N   . VAL B 1 188 ? 40.721 -17.358 87.698  1.00 17.21 ?  188 VAL B N   1 
ATOM   3503 C  CA  . VAL B 1 188 ? 40.797 -15.908 87.835  1.00 18.76 ?  188 VAL B CA  1 
ATOM   3504 C  C   . VAL B 1 188 ? 39.639 -15.329 88.634  1.00 19.22 ?  188 VAL B C   1 
ATOM   3505 O  O   . VAL B 1 188 ? 39.766 -14.212 89.150  1.00 20.07 ?  188 VAL B O   1 
ATOM   3506 C  CB  . VAL B 1 188 ? 40.882 -15.171 86.477  1.00 22.09 ?  188 VAL B CB  1 
ATOM   3507 C  CG1 . VAL B 1 188 ? 42.086 -15.651 85.675  1.00 19.47 ?  188 VAL B CG1 1 
ATOM   3508 C  CG2 . VAL B 1 188 ? 39.601 -15.321 85.672  1.00 25.29 ?  188 VAL B CG2 1 
ATOM   3509 N  N   . LYS B 1 189 ? 38.516 -16.042 88.735  1.00 21.15 ?  189 LYS B N   1 
ATOM   3510 C  CA  . LYS B 1 189 ? 37.351 -15.603 89.520  1.00 26.54 ?  189 LYS B CA  1 
ATOM   3511 C  C   . LYS B 1 189 ? 36.912 -14.235 88.997  1.00 21.82 ?  189 LYS B C   1 
ATOM   3512 O  O   . LYS B 1 189 ? 36.717 -14.084 87.778  1.00 23.60 ?  189 LYS B O   1 
ATOM   3513 C  CB  . LYS B 1 189 ? 37.703 -15.658 91.006  1.00 24.44 ?  189 LYS B CB  1 
ATOM   3514 C  CG  . LYS B 1 189 ? 38.111 -17.042 91.479  1.00 28.39 ?  189 LYS B CG  1 
ATOM   3515 C  CD  . LYS B 1 189 ? 38.116 -17.133 92.988  1.00 37.34 ?  189 LYS B CD  1 
ATOM   3516 C  CE  . LYS B 1 189 ? 38.989 -18.282 93.435  1.00 37.20 ?  189 LYS B CE  1 
ATOM   3517 N  NZ  . LYS B 1 189 ? 40.439 -18.022 93.160  1.00 42.34 ?  189 LYS B NZ  1 
ATOM   3518 N  N   . ASP B 1 190 ? 36.747 -13.232 89.860  1.00 25.16 ?  190 ASP B N   1 
ATOM   3519 C  CA  . ASP B 1 190 ? 36.254 -11.914 89.493  1.00 23.37 ?  190 ASP B CA  1 
ATOM   3520 C  C   . ASP B 1 190 ? 37.370 -10.905 89.249  1.00 28.43 ?  190 ASP B C   1 
ATOM   3521 O  O   . ASP B 1 190 ? 37.080 -9.722  89.052  1.00 25.12 ?  190 ASP B O   1 
ATOM   3522 C  CB  . ASP B 1 190 ? 35.324 -11.390 90.597  1.00 32.06 ?  190 ASP B CB  1 
ATOM   3523 C  CG  . ASP B 1 190 ? 35.970 -11.444 91.979  1.00 49.10 ?  190 ASP B CG  1 
ATOM   3524 O  OD1 . ASP B 1 190 ? 37.181 -11.750 92.071  1.00 58.36 ?  190 ASP B OD1 1 
ATOM   3525 O  OD2 . ASP B 1 190 ? 35.270 -11.178 92.981  1.00 61.99 -1 190 ASP B OD2 1 
ATOM   3526 N  N   . ALA B 1 191 ? 38.633 -11.346 89.235  1.00 19.47 ?  191 ALA B N   1 
ATOM   3527 C  CA  . ALA B 1 191 ? 39.781 -10.444 89.258  1.00 17.30 ?  191 ALA B CA  1 
ATOM   3528 C  C   . ALA B 1 191 ? 40.083 -9.848  87.882  1.00 17.46 ?  191 ALA B C   1 
ATOM   3529 O  O   . ALA B 1 191 ? 39.734 -10.431 86.850  1.00 20.19 ?  191 ALA B O   1 
ATOM   3530 C  CB  . ALA B 1 191 ? 41.017 -11.185 89.759  1.00 20.86 ?  191 ALA B CB  1 
ATOM   3531 N  N   . PRO B 1 192 ? 40.719 -8.677  87.846  1.00 16.94 ?  192 PRO B N   1 
ATOM   3532 C  CA  . PRO B 1 192 ? 41.341 -8.220  86.596  1.00 18.25 ?  192 PRO B CA  1 
ATOM   3533 C  C   . PRO B 1 192 ? 42.471 -9.161  86.233  1.00 16.52 ?  192 PRO B C   1 
ATOM   3534 O  O   . PRO B 1 192 ? 43.035 -9.839  87.090  1.00 17.20 ?  192 PRO B O   1 
ATOM   3535 C  CB  . PRO B 1 192 ? 41.872 -6.824  86.940  1.00 21.74 ?  192 PRO B CB  1 
ATOM   3536 C  CG  . PRO B 1 192 ? 42.088 -6.867  88.416  1.00 27.81 ?  192 PRO B CG  1 
ATOM   3537 C  CD  . PRO B 1 192 ? 41.006 -7.759  88.963  1.00 19.49 ?  192 PRO B CD  1 
ATOM   3538 N  N   . VAL B 1 193 ? 42.804 -9.199  84.937  1.00 15.90 ?  193 VAL B N   1 
ATOM   3539 C  CA  . VAL B 1 193 ? 43.685 -10.232 84.399  1.00 14.19 ?  193 VAL B CA  1 
ATOM   3540 C  C   . VAL B 1 193 ? 44.798 -9.616  83.554  1.00 13.97 ?  193 VAL B C   1 
ATOM   3541 O  O   . VAL B 1 193 ? 44.561 -8.727  82.728  1.00 16.87 ?  193 VAL B O   1 
ATOM   3542 C  CB  . VAL B 1 193 ? 42.900 -11.259 83.559  1.00 17.15 ?  193 VAL B CB  1 
ATOM   3543 C  CG1 . VAL B 1 193 ? 43.843 -12.323 82.997  1.00 19.14 ?  193 VAL B CG1 1 
ATOM   3544 C  CG2 . VAL B 1 193 ? 41.824 -11.935 84.403  1.00 19.65 ?  193 VAL B CG2 1 
ATOM   3545 N  N   . TRP B 1 194 ? 46.015 -10.103 83.766  1.00 14.26 ?  194 TRP B N   1 
ATOM   3546 C  CA  . TRP B 1 194 ? 47.156 -9.796  82.915  1.00 14.76 ?  194 TRP B CA  1 
ATOM   3547 C  C   . TRP B 1 194 ? 47.611 -11.101 82.286  1.00 12.15 ?  194 TRP B C   1 
ATOM   3548 O  O   . TRP B 1 194 ? 47.816 -12.087 82.996  1.00 14.48 ?  194 TRP B O   1 
ATOM   3549 C  CB  . TRP B 1 194 ? 48.297 -9.173  83.725  1.00 13.56 ?  194 TRP B CB  1 
ATOM   3550 C  CG  . TRP B 1 194 ? 49.534 -8.856  82.926  1.00 12.86 ?  194 TRP B CG  1 
ATOM   3551 C  CD1 . TRP B 1 194 ? 50.596 -9.673  82.705  1.00 16.54 ?  194 TRP B CD1 1 
ATOM   3552 C  CD2 . TRP B 1 194 ? 49.818 -7.623  82.268  1.00 13.51 ?  194 TRP B CD2 1 
ATOM   3553 N  NE1 . TRP B 1 194 ? 51.544 -9.017  81.930  1.00 14.32 ?  194 TRP B NE1 1 
ATOM   3554 C  CE2 . TRP B 1 194 ? 51.085 -7.753  81.656  1.00 13.09 ?  194 TRP B CE2 1 
ATOM   3555 C  CE3 . TRP B 1 194 ? 49.127 -6.412  82.145  1.00 14.99 ?  194 TRP B CE3 1 
ATOM   3556 C  CZ2 . TRP B 1 194 ? 51.675 -6.716  80.931  1.00 15.48 ?  194 TRP B CZ2 1 
ATOM   3557 C  CZ3 . TRP B 1 194 ? 49.714 -5.379  81.420  1.00 16.30 ?  194 TRP B CZ3 1 
ATOM   3558 C  CH2 . TRP B 1 194 ? 50.973 -5.546  80.814  1.00 17.57 ?  194 TRP B CH2 1 
ATOM   3559 N  N   . ILE B 1 195 ? 47.765 -11.122 80.958  1.00 12.95 ?  195 ILE B N   1 
ATOM   3560 C  CA  . ILE B 1 195 ? 48.158 -12.336 80.254  1.00 11.48 ?  195 ILE B CA  1 
ATOM   3561 C  C   . ILE B 1 195 ? 49.588 -12.187 79.757  1.00 13.96 ?  195 ILE B C   1 
ATOM   3562 O  O   . ILE B 1 195 ? 49.919 -11.225 79.049  1.00 14.45 ?  195 ILE B O   1 
ATOM   3563 C  CB  . ILE B 1 195 ? 47.217 -12.652 79.081  1.00 11.29 ?  195 ILE B CB  1 
ATOM   3564 C  CG1 . ILE B 1 195 ? 45.793 -12.916 79.575  1.00 14.25 ?  195 ILE B CG1 1 
ATOM   3565 C  CG2 . ILE B 1 195 ? 47.749 -13.861 78.296  1.00 18.71 ?  195 ILE B CG2 1 
ATOM   3566 C  CD1 . ILE B 1 195 ? 44.812 -13.189 78.432  1.00 18.30 ?  195 ILE B CD1 1 
ATOM   3567 N  N   . HIS B 1 196 ? 50.425 -13.141 80.121  1.00 13.61 ?  196 HIS B N   1 
ATOM   3568 C  CA  . HIS B 1 196 ? 51.798 -13.240 79.653  1.00 13.94 ?  196 HIS B CA  1 
ATOM   3569 C  C   . HIS B 1 196 ? 51.916 -14.546 78.896  1.00 12.33 ?  196 HIS B C   1 
ATOM   3570 O  O   . HIS B 1 196 ? 51.680 -15.607 79.478  1.00 15.92 ?  196 HIS B O   1 
ATOM   3571 C  CB  . HIS B 1 196 ? 52.760 -13.220 80.842  1.00 15.24 ?  196 HIS B CB  1 
ATOM   3572 C  CG  . HIS B 1 196 ? 54.167 -13.595 80.502  1.00 15.67 ?  196 HIS B CG  1 
ATOM   3573 N  ND1 . HIS B 1 196 ? 55.191 -12.675 80.521  1.00 19.05 ?  196 HIS B ND1 1 
ATOM   3574 C  CD2 . HIS B 1 196 ? 54.728 -14.781 80.173  1.00 15.84 ?  196 HIS B CD2 1 
ATOM   3575 C  CE1 . HIS B 1 196 ? 56.321 -13.272 80.190  1.00 23.19 ?  196 HIS B CE1 1 
ATOM   3576 N  NE2 . HIS B 1 196 ? 56.069 -14.550 79.971  1.00 21.15 ?  196 HIS B NE2 1 
ATOM   3577 N  N   . ILE B 1 197 ? 52.253 -14.498 77.605  1.00 11.66 ?  197 ILE B N   1 
ATOM   3578 C  CA  . ILE B 1 197 ? 52.339 -15.740 76.845  1.00 13.08 ?  197 ILE B CA  1 
ATOM   3579 C  C   . ILE B 1 197 ? 53.694 -15.883 76.142  1.00 12.30 ?  197 ILE B C   1 
ATOM   3580 O  O   . ILE B 1 197 ? 54.145 -14.984 75.411  1.00 13.13 ?  197 ILE B O   1 
ATOM   3581 C  CB  . ILE B 1 197 ? 51.156 -15.898 75.864  1.00 13.44 ?  197 ILE B CB  1 
ATOM   3582 C  CG1 . ILE B 1 197 ? 51.184 -17.270 75.180  1.00 15.70 ?  197 ILE B CG1 1 
ATOM   3583 C  CG2 . ILE B 1 197 ? 51.077 -14.769 74.856  1.00 18.60 ?  197 ILE B CG2 1 
ATOM   3584 C  CD1 . ILE B 1 197 ? 49.809 -17.679 74.667  1.00 16.09 ?  197 ILE B CD1 1 
ATOM   3585 N  N   . ASP B 1 198 ? 54.322 -17.023 76.384  1.00 13.79 ?  198 ASP B N   1 
ATOM   3586 C  CA  . ASP B 1 198 ? 55.547 -17.484 75.739  1.00 13.50 ?  198 ASP B CA  1 
ATOM   3587 C  C   . ASP B 1 198 ? 55.122 -18.562 74.750  1.00 14.85 ?  198 ASP B C   1 
ATOM   3588 O  O   . ASP B 1 198 ? 54.474 -19.541 75.138  1.00 15.23 ?  198 ASP B O   1 
ATOM   3589 C  CB  . ASP B 1 198 ? 56.494 -18.023 76.818  1.00 14.53 ?  198 ASP B CB  1 
ATOM   3590 C  CG  . ASP B 1 198 ? 57.787 -18.618 76.295  1.00 17.46 ?  198 ASP B CG  1 
ATOM   3591 O  OD1 . ASP B 1 198 ? 57.898 -18.953 75.102  1.00 18.10 ?  198 ASP B OD1 1 
ATOM   3592 O  OD2 . ASP B 1 198 ? 58.697 -18.771 77.148  1.00 20.95 -1 198 ASP B OD2 1 
ATOM   3593 N  N   . TRP B 1 199 ? 55.456 -18.376 73.467  1.00 13.81 ?  199 TRP B N   1 
ATOM   3594 C  CA  . TRP B 1 199 ? 54.942 -19.292 72.450  1.00 15.13 ?  199 TRP B CA  1 
ATOM   3595 C  C   . TRP B 1 199 ? 55.481 -20.716 72.583  1.00 15.09 ?  199 TRP B C   1 
ATOM   3596 O  O   . TRP B 1 199 ? 54.960 -21.617 71.907  1.00 16.18 ?  199 TRP B O   1 
ATOM   3597 C  CB  . TRP B 1 199 ? 55.235 -18.753 71.040  1.00 15.37 ?  199 TRP B CB  1 
ATOM   3598 C  CG  . TRP B 1 199 ? 54.646 -17.383 70.836  1.00 15.37 ?  199 TRP B CG  1 
ATOM   3599 C  CD1 . TRP B 1 199 ? 55.330 -16.235 70.535  1.00 15.60 ?  199 TRP B CD1 1 
ATOM   3600 C  CD2 . TRP B 1 199 ? 53.267 -17.002 70.975  1.00 15.33 ?  199 TRP B CD2 1 
ATOM   3601 N  NE1 . TRP B 1 199 ? 54.463 -15.175 70.458  1.00 15.32 ?  199 TRP B NE1 1 
ATOM   3602 C  CE2 . TRP B 1 199 ? 53.193 -15.615 70.726  1.00 12.70 ?  199 TRP B CE2 1 
ATOM   3603 C  CE3 . TRP B 1 199 ? 52.089 -17.696 71.274  1.00 14.97 ?  199 TRP B CE3 1 
ATOM   3604 C  CZ2 . TRP B 1 199 ? 51.998 -14.908 70.765  1.00 15.94 ?  199 TRP B CZ2 1 
ATOM   3605 C  CZ3 . TRP B 1 199 ? 50.891 -16.988 71.296  1.00 15.95 ?  199 TRP B CZ3 1 
ATOM   3606 C  CH2 . TRP B 1 199 ? 50.861 -15.605 71.063  1.00 17.30 ?  199 TRP B CH2 1 
ATOM   3607 N  N   . ASP B 1 200 ? 56.496 -20.953 73.426  1.00 14.74 ?  200 ASP B N   1 
ATOM   3608 C  CA  . ASP B 1 200 ? 56.834 -22.352 73.681  1.00 16.39 ?  200 ASP B CA  1 
ATOM   3609 C  C   . ASP B 1 200 ? 55.745 -23.101 74.434  1.00 16.77 ?  200 ASP B C   1 
ATOM   3610 O  O   . ASP B 1 200 ? 55.872 -24.317 74.606  1.00 17.29 ?  200 ASP B O   1 
ATOM   3611 C  CB  . ASP B 1 200 ? 58.189 -22.488 74.407  1.00 17.75 ?  200 ASP B CB  1 
ATOM   3612 C  CG  . ASP B 1 200 ? 58.204 -21.939 75.831  1.00 20.78 ?  200 ASP B CG  1 
ATOM   3613 O  OD1 . ASP B 1 200 ? 57.179 -21.949 76.535  1.00 19.17 ?  200 ASP B OD1 1 
ATOM   3614 O  OD2 . ASP B 1 200 ? 59.296 -21.527 76.275  1.00 20.72 -1 200 ASP B OD2 1 
ATOM   3615 N  N   . VAL B 1 201 ? 54.666 -22.441 74.863  1.00 14.00 ?  201 VAL B N   1 
ATOM   3616 C  CA  . VAL B 1 201 ? 53.578 -23.193 75.464  1.00 14.19 ?  201 VAL B CA  1 
ATOM   3617 C  C   . VAL B 1 201 ? 52.867 -24.086 74.454  1.00 16.29 ?  201 VAL B C   1 
ATOM   3618 O  O   . VAL B 1 201 ? 52.199 -25.050 74.853  1.00 15.70 ?  201 VAL B O   1 
ATOM   3619 C  CB  . VAL B 1 201 ? 52.582 -22.236 76.141  1.00 12.91 ?  201 VAL B CB  1 
ATOM   3620 C  CG1 . VAL B 1 201 ? 51.704 -21.539 75.104  1.00 15.94 ?  201 VAL B CG1 1 
ATOM   3621 C  CG2 . VAL B 1 201 ? 51.740 -23.002 77.169  1.00 15.54 ?  201 VAL B CG2 1 
ATOM   3622 N  N   . LEU B 1 202 ? 52.982 -23.789 73.164  1.00 14.90 ?  202 LEU B N   1 
ATOM   3623 C  CA  . LEU B 1 202 ? 52.205 -24.486 72.154  1.00 15.23 ?  202 LEU B CA  1 
ATOM   3624 C  C   . LEU B 1 202 ? 52.795 -25.854 71.857  1.00 16.03 ?  202 LEU B C   1 
ATOM   3625 O  O   . LEU B 1 202 ? 54.012 -26.062 71.929  1.00 18.96 ?  202 LEU B O   1 
ATOM   3626 C  CB  . LEU B 1 202 ? 52.168 -23.687 70.853  1.00 18.42 ?  202 LEU B CB  1 
ATOM   3627 C  CG  . LEU B 1 202 ? 51.211 -22.508 70.713  1.00 22.78 ?  202 LEU B CG  1 
ATOM   3628 C  CD1 . LEU B 1 202 ? 51.356 -21.971 69.300  1.00 28.62 ?  202 LEU B CD1 1 
ATOM   3629 C  CD2 . LEU B 1 202 ? 49.763 -22.881 70.990  1.00 24.40 ?  202 LEU B CD2 1 
ATOM   3630 N  N   . GLU B 1 203 ? 51.918 -26.768 71.470  1.00 17.58 ?  203 GLU B N   1 
ATOM   3631 C  CA  . GLU B 1 203 ? 52.344 -28.012 70.856  1.00 23.15 ?  203 GLU B CA  1 
ATOM   3632 C  C   . GLU B 1 203 ? 53.288 -27.697 69.696  1.00 25.31 ?  203 GLU B C   1 
ATOM   3633 O  O   . GLU B 1 203 ? 52.986 -26.811 68.885  1.00 22.43 ?  203 GLU B O   1 
ATOM   3634 C  CB  . GLU B 1 203 ? 51.112 -28.783 70.376  1.00 26.09 ?  203 GLU B CB  1 
ATOM   3635 C  CG  . GLU B 1 203 ? 51.391 -30.013 69.531  1.00 26.22 ?  203 GLU B CG  1 
ATOM   3636 C  CD  . GLU B 1 203 ? 51.811 -31.214 70.349  1.00 37.53 ?  203 GLU B CD  1 
ATOM   3637 O  OE1 . GLU B 1 203 ? 51.959 -31.095 71.585  1.00 30.49 ?  203 GLU B OE1 1 
ATOM   3638 O  OE2 . GLU B 1 203 ? 52.002 -32.290 69.744  1.00 45.78 -1 203 GLU B OE2 1 
ATOM   3639 N  N   . PRO B 1 204 ? 54.454 -28.339 69.624  1.00 26.24 ?  204 PRO B N   1 
ATOM   3640 C  CA  . PRO B 1 204 ? 55.422 -28.000 68.571  1.00 26.72 ?  204 PRO B CA  1 
ATOM   3641 C  C   . PRO B 1 204 ? 54.817 -28.125 67.180  1.00 29.62 ?  204 PRO B C   1 
ATOM   3642 O  O   . PRO B 1 204 ? 54.064 -29.060 66.894  1.00 28.10 ?  204 PRO B O   1 
ATOM   3643 C  CB  . PRO B 1 204 ? 56.543 -29.020 68.788  1.00 32.41 ?  204 PRO B CB  1 
ATOM   3644 C  CG  . PRO B 1 204 ? 56.462 -29.342 70.256  1.00 37.57 ?  204 PRO B CG  1 
ATOM   3645 C  CD  . PRO B 1 204 ? 54.993 -29.319 70.584  1.00 27.85 ?  204 PRO B CD  1 
ATOM   3646 N  N   . GLY B 1 205 ? 55.136 -27.149 66.324  1.00 29.17 ?  205 GLY B N   1 
ATOM   3647 C  CA  . GLY B 1 205 ? 54.706 -27.180 64.937  1.00 28.56 ?  205 GLY B CA  1 
ATOM   3648 C  C   . GLY B 1 205 ? 54.061 -25.926 64.373  1.00 34.56 ?  205 GLY B C   1 
ATOM   3649 O  O   . GLY B 1 205 ? 53.939 -25.803 63.149  1.00 40.54 ?  205 GLY B O   1 
ATOM   3650 N  N   . SER B 1 206 ? 53.634 -24.995 65.228  1.00 27.18 ?  206 SER B N   1 
ATOM   3651 C  CA  . SER B 1 206 ? 52.940 -23.789 64.782  1.00 24.06 ?  206 SER B CA  1 
ATOM   3652 C  C   . SER B 1 206 ? 53.787 -22.529 64.867  1.00 25.19 ?  206 SER B C   1 
ATOM   3653 O  O   . SER B 1 206 ? 53.748 -21.706 63.954  1.00 27.40 ?  206 SER B O   1 
ATOM   3654 C  CB  . SER B 1 206 ? 51.647 -23.572 65.583  1.00 30.10 ?  206 SER B CB  1 
ATOM   3655 O  OG  . SER B 1 206 ? 50.780 -24.695 65.542  1.00 29.74 ?  206 SER B OG  1 
ATOM   3656 N  N   . ILE B 1 207 ? 54.538 -22.345 65.947  1.00 24.73 ?  207 ILE B N   1 
ATOM   3657 C  CA  . ILE B 1 207 ? 55.335 -21.138 66.135  1.00 22.95 ?  207 ILE B CA  1 
ATOM   3658 C  C   . ILE B 1 207 ? 56.764 -21.513 66.505  1.00 24.08 ?  207 ILE B C   1 
ATOM   3659 O  O   . ILE B 1 207 ? 56.974 -22.243 67.485  1.00 29.54 ?  207 ILE B O   1 
ATOM   3660 C  CB  . ILE B 1 207 ? 54.715 -20.240 67.217  1.00 21.70 ?  207 ILE B CB  1 
ATOM   3661 C  CG1 . ILE B 1 207 ? 53.306 -19.800 66.794  1.00 22.51 ?  207 ILE B CG1 1 
ATOM   3662 C  CG2 . ILE B 1 207 ? 55.618 -19.050 67.488  1.00 22.64 ?  207 ILE B CG2 1 
ATOM   3663 C  CD1 . ILE B 1 207 ? 52.579 -19.003 67.852  1.00 24.31 ?  207 ILE B CD1 1 
ATOM   3664 N  N   . PRO B 1 208 ? 57.774 -21.044 65.770  1.00 22.09 ?  208 PRO B N   1 
ATOM   3665 C  CA  . PRO B 1 208 ? 59.167 -21.333 66.140  1.00 28.32 ?  208 PRO B CA  1 
ATOM   3666 C  C   . PRO B 1 208 ? 59.557 -20.610 67.424  1.00 29.09 ?  208 PRO B C   1 
ATOM   3667 O  O   . PRO B 1 208 ? 59.523 -19.382 67.491  1.00 27.55 ?  208 PRO B O   1 
ATOM   3668 C  CB  . PRO B 1 208 ? 59.970 -20.813 64.940  1.00 26.68 ?  208 PRO B CB  1 
ATOM   3669 C  CG  . PRO B 1 208 ? 58.979 -20.670 63.832  1.00 30.57 ?  208 PRO B CG  1 
ATOM   3670 C  CD  . PRO B 1 208 ? 57.693 -20.308 64.495  1.00 20.59 ?  208 PRO B CD  1 
ATOM   3671 N  N   A ALA B 1 209 ? 59.943 -21.371 68.439  0.49 32.97 ?  209 ALA B N   1 
ATOM   3672 N  N   B ALA B 1 209 ? 59.928 -21.394 68.434  0.51 32.97 ?  209 ALA B N   1 
ATOM   3673 C  CA  A ALA B 1 209 ? 60.374 -20.786 69.701  0.49 34.08 ?  209 ALA B CA  1 
ATOM   3674 C  CA  B ALA B 1 209 ? 60.455 -20.888 69.692  0.51 34.16 ?  209 ALA B CA  1 
ATOM   3675 C  C   A ALA B 1 209 ? 61.811 -21.199 70.001  0.49 34.51 ?  209 ALA B C   1 
ATOM   3676 C  C   B ALA B 1 209 ? 61.482 -21.883 70.212  0.51 35.95 ?  209 ALA B C   1 
ATOM   3677 O  O   A ALA B 1 209 ? 62.372 -22.095 69.364  0.49 38.93 ?  209 ALA B O   1 
ATOM   3678 O  O   B ALA B 1 209 ? 61.423 -23.077 69.901  0.51 36.99 ?  209 ALA B O   1 
ATOM   3679 C  CB  A ALA B 1 209 ? 59.441 -21.199 70.849  0.49 30.81 ?  209 ALA B CB  1 
ATOM   3680 C  CB  B ALA B 1 209 ? 59.347 -20.669 70.731  0.51 30.83 ?  209 ALA B CB  1 
ATOM   3681 N  N   A ASP B 1 210 ? 62.412 -20.515 70.980  0.49 36.14 ?  210 ASP B N   1 
ATOM   3682 N  N   B ASP B 1 210 ? 62.428 -21.383 71.001  0.51 38.68 ?  210 ASP B N   1 
ATOM   3683 C  CA  A ASP B 1 210 ? 63.723 -20.928 71.472  0.49 36.98 ?  210 ASP B CA  1 
ATOM   3684 C  CA  B ASP B 1 210 ? 63.443 -22.248 71.576  0.51 37.21 ?  210 ASP B CA  1 
ATOM   3685 C  C   A ASP B 1 210 ? 63.677 -22.356 71.998  0.49 37.95 ?  210 ASP B C   1 
ATOM   3686 C  C   B ASP B 1 210 ? 62.880 -23.017 72.770  0.51 39.12 ?  210 ASP B C   1 
ATOM   3687 O  O   A ASP B 1 210 ? 64.624 -23.130 71.811  0.49 39.25 ?  210 ASP B O   1 
ATOM   3688 O  O   B ASP B 1 210 ? 61.852 -22.654 73.350  0.51 36.97 ?  210 ASP B O   1 
ATOM   3689 C  CB  A ASP B 1 210 ? 64.201 -19.967 72.566  0.49 36.63 ?  210 ASP B CB  1 
ATOM   3690 C  CB  B ASP B 1 210 ? 64.667 -21.437 72.005  0.51 38.63 ?  210 ASP B CB  1 
ATOM   3691 C  CG  A ASP B 1 210 ? 65.714 -19.929 72.701  0.49 37.06 ?  210 ASP B CG  1 
ATOM   3692 C  CG  B ASP B 1 210 ? 65.850 -21.626 71.074  0.51 41.32 ?  210 ASP B CG  1 
ATOM   3693 O  OD1 A ASP B 1 210 ? 66.404 -20.532 71.855  0.49 33.76 ?  210 ASP B OD1 1 
ATOM   3694 O  OD1 B ASP B 1 210 ? 65.657 -22.159 69.960  0.51 41.94 -1 210 ASP B OD1 1 
ATOM   3695 O  OD2 A ASP B 1 210 ? 66.213 -19.292 73.656  0.49 32.84 ?  210 ASP B OD2 1 
ATOM   3696 O  OD2 B ASP B 1 210 ? 66.975 -21.239 71.459  0.51 42.11 -1 210 ASP B OD2 1 
ATOM   3697 N  N   A TYR B 1 211 ? 62.575 -22.725 72.647  0.49 39.30 ?  211 TYR B N   1 
ATOM   3698 N  N   B TYR B 1 211 ? 63.573 -24.101 73.125  0.51 38.23 ?  211 TYR B N   1 
ATOM   3699 C  CA  A TYR B 1 211 ? 62.379 -24.057 73.192  0.49 39.16 ?  211 TYR B CA  1 
ATOM   3700 C  CA  B TYR B 1 211 ? 63.233 -24.942 74.273  0.51 38.68 ?  211 TYR B CA  1 
ATOM   3701 C  C   A TYR B 1 211 ? 61.211 -24.737 72.488  0.49 38.53 ?  211 TYR B C   1 
ATOM   3702 C  C   B TYR B 1 211 ? 61.817 -25.511 74.125  0.51 37.12 ?  211 TYR B C   1 
ATOM   3703 O  O   A TYR B 1 211 ? 60.241 -24.085 72.083  0.49 32.42 ?  211 TYR B O   1 
ATOM   3704 O  O   B TYR B 1 211 ? 60.881 -25.174 74.857  0.51 36.34 ?  211 TYR B O   1 
ATOM   3705 C  CB  A TYR B 1 211 ? 62.132 -24.001 74.706  0.49 35.91 ?  211 TYR B CB  1 
ATOM   3706 C  CB  B TYR B 1 211 ? 63.408 -24.158 75.581  0.51 37.74 ?  211 TYR B CB  1 
ATOM   3707 C  CG  A TYR B 1 211 ? 63.320 -23.489 75.497  0.49 36.30 ?  211 TYR B CG  1 
ATOM   3708 C  CG  B TYR B 1 211 ? 64.700 -23.365 75.629  0.51 37.61 ?  211 TYR B CG  1 
ATOM   3709 C  CD1 A TYR B 1 211 ? 63.516 -22.128 75.693  0.49 34.93 ?  211 TYR B CD1 1 
ATOM   3710 C  CD1 B TYR B 1 211 ? 65.907 -23.943 75.245  0.51 41.20 ?  211 TYR B CD1 1 
ATOM   3711 C  CD2 A TYR B 1 211 ? 64.248 -24.370 76.042  0.49 38.72 ?  211 TYR B CD2 1 
ATOM   3712 C  CD2 B TYR B 1 211 ? 64.712 -22.040 76.046  0.51 37.41 ?  211 TYR B CD2 1 
ATOM   3713 C  CE1 A TYR B 1 211 ? 64.601 -21.658 76.411  0.49 37.05 ?  211 TYR B CE1 1 
ATOM   3714 C  CE1 B TYR B 1 211 ? 67.089 -23.225 75.278  0.51 39.89 ?  211 TYR B CE1 1 
ATOM   3715 C  CE2 A TYR B 1 211 ? 65.334 -23.909 76.762  0.49 38.08 ?  211 TYR B CE2 1 
ATOM   3716 C  CE2 B TYR B 1 211 ? 65.891 -21.314 76.083  0.51 36.16 ?  211 TYR B CE2 1 
ATOM   3717 C  CZ  A TYR B 1 211 ? 65.507 -22.553 76.943  0.49 38.30 ?  211 TYR B CZ  1 
ATOM   3718 C  CZ  B TYR B 1 211 ? 67.076 -21.914 75.701  0.51 38.70 ?  211 TYR B CZ  1 
ATOM   3719 O  OH  A TYR B 1 211 ? 66.590 -22.092 77.659  0.49 40.28 ?  211 TYR B OH  1 
ATOM   3720 O  OH  B TYR B 1 211 ? 68.250 -21.197 75.735  0.51 34.96 ?  211 TYR B OH  1 
ATOM   3721 N  N   A THR B 1 212 ? 61.319 -26.057 72.341  0.49 39.16 ?  212 THR B N   1 
ATOM   3722 N  N   B THR B 1 212 ? 61.696 -26.391 73.134  0.51 41.32 ?  212 THR B N   1 
ATOM   3723 C  CA  A THR B 1 212 ? 60.339 -26.887 71.640  0.49 38.57 ?  212 THR B CA  1 
ATOM   3724 C  CA  B THR B 1 212 ? 60.442 -27.065 72.837  0.51 37.54 ?  212 THR B CA  1 
ATOM   3725 C  C   A THR B 1 212 ? 59.873 -27.980 72.603  0.49 37.72 ?  212 THR B C   1 
ATOM   3726 C  C   B THR B 1 212 ? 60.250 -28.267 73.754  0.51 37.44 ?  212 THR B C   1 
ATOM   3727 O  O   A THR B 1 212 ? 60.423 -29.084 72.625  0.49 37.69 ?  212 THR B O   1 
ATOM   3728 O  O   B THR B 1 212 ? 61.213 -28.911 74.180  0.51 41.06 ?  212 THR B O   1 
ATOM   3729 C  CB  A THR B 1 212 ? 60.942 -27.474 70.365  0.49 37.58 ?  212 THR B CB  1 
ATOM   3730 C  CB  B THR B 1 212 ? 60.413 -27.526 71.377  0.51 38.14 ?  212 THR B CB  1 
ATOM   3731 O  OG1 A THR B 1 212 ? 61.525 -26.422 69.585  0.49 38.32 ?  212 THR B OG1 1 
ATOM   3732 O  OG1 B THR B 1 212 ? 61.590 -27.061 70.706  0.51 37.02 ?  212 THR B OG1 1 
ATOM   3733 C  CG2 A THR B 1 212 ? 59.879 -28.165 69.541  0.49 36.93 ?  212 THR B CG2 1 
ATOM   3734 C  CG2 B THR B 1 212 ? 59.187 -26.983 70.663  0.51 38.62 ?  212 THR B CG2 1 
ATOM   3735 N  N   A VAL B 1 213 ? 58.844 -27.669 73.381  0.49 34.84 ?  213 VAL B N   1 
ATOM   3736 N  N   B VAL B 1 213 ? 58.988 -28.565 74.054  0.51 34.20 ?  213 VAL B N   1 
ATOM   3737 C  CA  A VAL B 1 213 ? 58.420 -28.485 74.517  0.49 34.49 ?  213 VAL B CA  1 
ATOM   3738 C  CA  B VAL B 1 213 ? 58.618 -29.726 74.864  0.51 31.93 ?  213 VAL B CA  1 
ATOM   3739 C  C   A VAL B 1 213 ? 57.291 -29.398 74.063  0.49 30.58 ?  213 VAL B C   1 
ATOM   3740 C  C   B VAL B 1 213 ? 57.315 -30.307 74.323  0.51 32.47 ?  213 VAL B C   1 
ATOM   3741 O  O   A VAL B 1 213 ? 56.219 -28.898 73.683  0.49 29.73 ?  213 VAL B O   1 
ATOM   3742 O  O   B VAL B 1 213 ? 56.350 -29.558 74.105  0.51 26.33 ?  213 VAL B O   1 
ATOM   3743 C  CB  A VAL B 1 213 ? 57.974 -27.600 75.690  0.49 30.94 ?  213 VAL B CB  1 
ATOM   3744 C  CB  B VAL B 1 213 ? 58.487 -29.354 76.351  0.51 32.22 ?  213 VAL B CB  1 
ATOM   3745 C  CG1 A VAL B 1 213 ? 58.258 -28.283 77.004  0.49 29.43 ?  213 VAL B CG1 1 
ATOM   3746 C  CG1 B VAL B 1 213 ? 57.792 -30.462 77.115  0.51 32.11 ?  213 VAL B CG1 1 
ATOM   3747 C  CG2 A VAL B 1 213 ? 58.663 -26.240 75.620  0.49 30.81 ?  213 VAL B CG2 1 
ATOM   3748 C  CG2 B VAL B 1 213 ? 59.853 -29.073 76.972  0.51 32.89 ?  213 VAL B CG2 1 
ATOM   3749 N  N   A PRO B 1 214 ? 57.461 -30.720 74.101  0.49 32.24 ?  214 PRO B N   1 
ATOM   3750 N  N   B PRO B 1 214 ? 57.230 -31.620 74.101  0.51 30.57 ?  214 PRO B N   1 
ATOM   3751 C  CA  A PRO B 1 214 ? 56.420 -31.621 73.590  0.49 30.68 ?  214 PRO B CA  1 
ATOM   3752 C  CA  B PRO B 1 214 ? 56.024 -32.197 73.489  0.51 30.96 ?  214 PRO B CA  1 
ATOM   3753 C  C   A PRO B 1 214 ? 55.172 -31.640 74.468  0.49 29.87 ?  214 PRO B C   1 
ATOM   3754 C  C   B PRO B 1 214 ? 54.810 -32.101 74.405  0.51 28.43 ?  214 PRO B C   1 
ATOM   3755 O  O   A PRO B 1 214 ? 55.195 -31.282 75.650  0.49 28.45 ?  214 PRO B O   1 
ATOM   3756 O  O   B PRO B 1 214 ? 54.902 -31.795 75.596  0.51 29.71 ?  214 PRO B O   1 
ATOM   3757 C  CB  A PRO B 1 214 ? 57.103 -32.996 73.583  0.49 33.15 ?  214 PRO B CB  1 
ATOM   3758 C  CB  B PRO B 1 214 ? 56.412 -33.660 73.239  0.51 30.79 ?  214 PRO B CB  1 
ATOM   3759 C  CG  A PRO B 1 214 ? 58.576 -32.721 73.758  0.49 33.29 ?  214 PRO B CG  1 
ATOM   3760 C  CG  B PRO B 1 214 ? 57.911 -33.695 73.330  0.51 32.80 ?  214 PRO B CG  1 
ATOM   3761 C  CD  A PRO B 1 214 ? 58.662 -31.449 74.540  0.49 35.35 ?  214 PRO B CD  1 
ATOM   3762 C  CD  B PRO B 1 214 ? 58.274 -32.636 74.319  0.51 34.34 ?  214 PRO B CD  1 
ATOM   3763 N  N   A ASP B 1 215 ? 54.067 -32.071 73.849  0.49 28.68 ?  215 ASP B N   1 
ATOM   3764 N  N   B ASP B 1 215 ? 53.646 -32.370 73.805  0.51 28.94 ?  215 ASP B N   1 
ATOM   3765 C  CA  A ASP B 1 215 ? 52.773 -32.289 74.510  0.49 28.45 ?  215 ASP B CA  1 
ATOM   3766 C  CA  B ASP B 1 215 ? 52.352 -32.400 74.493  0.51 27.90 ?  215 ASP B CA  1 
ATOM   3767 C  C   A ASP B 1 215 ? 52.222 -30.993 75.113  0.49 24.95 ?  215 ASP B C   1 
ATOM   3768 C  C   B ASP B 1 215 ? 52.000 -31.035 75.095  0.51 24.91 ?  215 ASP B C   1 
ATOM   3769 O  O   A ASP B 1 215 ? 51.970 -30.886 76.313  0.49 23.39 ?  215 ASP B O   1 
ATOM   3770 O  O   B ASP B 1 215 ? 51.716 -30.902 76.286  0.51 23.27 ?  215 ASP B O   1 
ATOM   3771 C  CB  A ASP B 1 215 ? 52.880 -33.396 75.565  0.49 28.16 ?  215 ASP B CB  1 
ATOM   3772 C  CB  B ASP B 1 215 ? 52.324 -33.498 75.563  0.51 27.44 ?  215 ASP B CB  1 
ATOM   3773 C  CG  A ASP B 1 215 ? 53.349 -34.714 74.977  0.49 32.94 ?  215 ASP B CG  1 
ATOM   3774 C  CG  B ASP B 1 215 ? 52.024 -34.871 74.987  0.51 33.99 ?  215 ASP B CG  1 
ATOM   3775 O  OD1 A ASP B 1 215 ? 53.196 -34.905 73.752  0.49 35.98 ?  215 ASP B OD1 1 
ATOM   3776 O  OD1 B ASP B 1 215 ? 51.384 -34.947 73.916  0.51 38.36 -1 215 ASP B OD1 1 
ATOM   3777 O  OD2 A ASP B 1 215 ? 53.871 -35.559 75.734  0.49 35.14 ?  215 ASP B OD2 1 
ATOM   3778 O  OD2 B ASP B 1 215 ? 52.427 -35.875 75.613  0.51 36.69 -1 215 ASP B OD2 1 
ATOM   3779 N  N   . GLY B 1 216 ? 51.995 -30.013 74.239  1.00 21.39 ?  216 GLY B N   1 
ATOM   3780 C  CA  . GLY B 1 216 ? 51.647 -28.670 74.648  1.00 18.24 ?  216 GLY B CA  1 
ATOM   3781 C  C   . GLY B 1 216 ? 50.199 -28.290 74.393  1.00 19.99 ?  216 GLY B C   1 
ATOM   3782 O  O   . GLY B 1 216 ? 49.335 -29.119 74.093  1.00 20.20 ?  216 GLY B O   1 
ATOM   3783 N  N   . MET B 1 217 ? 49.932 -26.992 74.544  1.00 16.07 ?  217 MET B N   1 
ATOM   3784 C  CA  . MET B 1 217 ? 48.608 -26.460 74.259  1.00 15.47 ?  217 MET B CA  1 
ATOM   3785 C  C   . MET B 1 217 ? 48.414 -26.253 72.757  1.00 16.69 ?  217 MET B C   1 
ATOM   3786 O  O   . MET B 1 217 ? 49.349 -25.941 72.016  1.00 17.40 ?  217 MET B O   1 
ATOM   3787 C  CB  . MET B 1 217 ? 48.384 -25.140 75.006  1.00 16.91 ?  217 MET B CB  1 
ATOM   3788 C  CG  . MET B 1 217 ? 48.214 -25.294 76.518  1.00 18.11 ?  217 MET B CG  1 
ATOM   3789 S  SD  . MET B 1 217 ? 47.935 -23.726 77.373  1.00 18.31 ?  217 MET B SD  1 
ATOM   3790 C  CE  . MET B 1 217 ? 46.203 -23.381 76.982  1.00 17.32 ?  217 MET B CE  1 
ATOM   3791 N  N   . LEU B 1 218 ? 47.187 -26.420 72.316  1.00 17.17 ?  218 LEU B N   1 
ATOM   3792 C  CA  . LEU B 1 218 ? 46.898 -26.228 70.904  1.00 14.80 ?  218 LEU B CA  1 
ATOM   3793 C  C   . LEU B 1 218 ? 46.307 -24.845 70.663  1.00 17.14 ?  218 LEU B C   1 
ATOM   3794 O  O   . LEU B 1 218 ? 45.713 -24.254 71.570  1.00 15.37 ?  218 LEU B O   1 
ATOM   3795 C  CB  . LEU B 1 218 ? 45.911 -27.300 70.422  1.00 17.87 ?  218 LEU B CB  1 
ATOM   3796 C  CG  . LEU B 1 218 ? 46.534 -28.692 70.376  1.00 22.88 ?  218 LEU B CG  1 
ATOM   3797 C  CD1 . LEU B 1 218 ? 45.463 -29.773 70.410  1.00 30.44 ?  218 LEU B CD1 1 
ATOM   3798 C  CD2 . LEU B 1 218 ? 47.398 -28.803 69.139  1.00 25.59 ?  218 LEU B CD2 1 
ATOM   3799 N  N   . PRO B 1 219 ? 46.442 -24.306 69.445  1.00 14.08 ?  219 PRO B N   1 
ATOM   3800 C  CA  . PRO B 1 219 ? 45.920 -22.952 69.188  1.00 14.77 ?  219 PRO B CA  1 
ATOM   3801 C  C   . PRO B 1 219 ? 44.454 -22.759 69.549  1.00 16.98 ?  219 PRO B C   1 
ATOM   3802 O  O   . PRO B 1 219 ? 44.086 -21.676 70.022  1.00 16.13 ?  219 PRO B O   1 
ATOM   3803 C  CB  . PRO B 1 219 ? 46.183 -22.772 67.684  1.00 15.64 ?  219 PRO B CB  1 
ATOM   3804 C  CG  . PRO B 1 219 ? 47.400 -23.612 67.448  1.00 14.45 ?  219 PRO B CG  1 
ATOM   3805 C  CD  . PRO B 1 219 ? 47.219 -24.825 68.304  1.00 15.85 ?  219 PRO B CD  1 
ATOM   3806 N  N   . ALA B 1 220 ? 43.602 -23.773 69.353  1.00 16.00 ?  220 ALA B N   1 
ATOM   3807 C  CA  . ALA B 1 220 ? 42.190 -23.606 69.674  1.00 16.01 ?  220 ALA B CA  1 
ATOM   3808 C  C   . ALA B 1 220 ? 41.979 -23.282 71.149  1.00 17.27 ?  220 ALA B C   1 
ATOM   3809 O  O   . ALA B 1 220 ? 41.104 -22.481 71.492  1.00 16.14 ?  220 ALA B O   1 
ATOM   3810 C  CB  . ALA B 1 220 ? 41.412 -24.871 69.292  1.00 19.57 ?  220 ALA B CB  1 
ATOM   3811 N  N   . GLN B 1 221 ? 42.762 -23.907 72.037  1.00 18.91 ?  221 GLN B N   1 
ATOM   3812 C  CA  . GLN B 1 221 ? 42.586 -23.657 73.466  1.00 18.50 ?  221 GLN B CA  1 
ATOM   3813 C  C   . GLN B 1 221 ? 43.137 -22.298 73.867  1.00 16.75 ?  221 GLN B C   1 
ATOM   3814 O  O   . GLN B 1 221 ? 42.552 -21.624 74.718  1.00 18.98 ?  221 GLN B O   1 
ATOM   3815 C  CB  . GLN B 1 221 ? 43.244 -24.759 74.301  1.00 19.59 ?  221 GLN B CB  1 
ATOM   3816 C  CG  . GLN B 1 221 ? 42.323 -25.955 74.537  1.00 22.98 ?  221 GLN B CG  1 
ATOM   3817 C  CD  . GLN B 1 221 ? 41.919 -26.633 73.242  1.00 28.02 ?  221 GLN B CD  1 
ATOM   3818 O  OE1 . GLN B 1 221 ? 42.738 -27.294 72.603  1.00 27.76 ?  221 GLN B OE1 1 
ATOM   3819 N  NE2 . GLN B 1 221 ? 40.650 -26.481 72.850  1.00 26.80 ?  221 GLN B NE2 1 
ATOM   3820 N  N   . ILE B 1 222 ? 44.262 -21.881 73.277  1.00 16.39 ?  222 ILE B N   1 
ATOM   3821 C  CA  . ILE B 1 222 ? 44.778 -20.540 73.553  1.00 15.71 ?  222 ILE B CA  1 
ATOM   3822 C  C   . ILE B 1 222 ? 43.775 -19.487 73.097  1.00 16.03 ?  222 ILE B C   1 
ATOM   3823 O  O   . ILE B 1 222 ? 43.448 -18.559 73.844  1.00 16.36 ?  222 ILE B O   1 
ATOM   3824 C  CB  . ILE B 1 222 ? 46.159 -20.347 72.900  1.00 15.70 ?  222 ILE B CB  1 
ATOM   3825 C  CG1 . ILE B 1 222 ? 47.173 -21.304 73.532  1.00 17.39 ?  222 ILE B CG1 1 
ATOM   3826 C  CG2 . ILE B 1 222 ? 46.624 -18.899 73.027  1.00 18.70 ?  222 ILE B CG2 1 
ATOM   3827 C  CD1 . ILE B 1 222 ? 47.644 -20.888 74.896  1.00 22.99 ?  222 ILE B CD1 1 
ATOM   3828 N  N   . ARG B 1 223 ? 43.238 -19.637 71.877  1.00 14.47 ?  223 ARG B N   1 
ATOM   3829 C  CA  . ARG B 1 223 ? 42.262 -18.669 71.390  1.00 14.33 ?  223 ARG B CA  1 
ATOM   3830 C  C   . ARG B 1 223 ? 41.042 -18.630 72.292  1.00 13.90 ?  223 ARG B C   1 
ATOM   3831 O  O   . ARG B 1 223 ? 40.482 -17.557 72.553  1.00 14.34 ?  223 ARG B O   1 
ATOM   3832 C  CB  . ARG B 1 223 ? 41.859 -19.005 69.945  1.00 15.49 ?  223 ARG B CB  1 
ATOM   3833 C  CG  . ARG B 1 223 ? 40.958 -17.961 69.285  1.00 16.95 ?  223 ARG B CG  1 
ATOM   3834 C  CD  . ARG B 1 223 ? 40.534 -18.353 67.853  1.00 16.59 ?  223 ARG B CD  1 
ATOM   3835 N  NE  . ARG B 1 223 ? 39.282 -17.689 67.512  1.00 29.77 ?  223 ARG B NE  1 
ATOM   3836 C  CZ  . ARG B 1 223 ? 39.216 -16.501 66.929  1.00 22.33 ?  223 ARG B CZ  1 
ATOM   3837 N  NH1 . ARG B 1 223 ? 40.330 -15.871 66.601  1.00 29.35 ?  223 ARG B NH1 1 
ATOM   3838 N  NH2 . ARG B 1 223 ? 38.042 -15.959 66.649  1.00 33.91 ?  223 ARG B NH2 1 
ATOM   3839 N  N   . ALA B 1 224 ? 40.618 -19.803 72.783  1.00 15.31 ?  224 ALA B N   1 
ATOM   3840 C  CA  . ALA B 1 224 ? 39.480 -19.856 73.692  1.00 16.52 ?  224 ALA B CA  1 
ATOM   3841 C  C   . ALA B 1 224 ? 39.745 -19.109 74.995  1.00 17.53 ?  224 ALA B C   1 
ATOM   3842 O  O   . ALA B 1 224 ? 38.817 -18.534 75.565  1.00 15.96 ?  224 ALA B O   1 
ATOM   3843 C  CB  . ALA B 1 224 ? 39.115 -21.310 73.964  1.00 16.38 ?  224 ALA B CB  1 
ATOM   3844 N  N   . VAL B 1 225 ? 40.989 -19.089 75.472  1.00 14.08 ?  225 VAL B N   1 
ATOM   3845 C  CA  . VAL B 1 225 ? 41.303 -18.305 76.668  1.00 16.04 ?  225 VAL B CA  1 
ATOM   3846 C  C   . VAL B 1 225 ? 41.112 -16.817 76.394  1.00 18.13 ?  225 VAL B C   1 
ATOM   3847 O  O   . VAL B 1 225 ? 40.459 -16.107 77.165  1.00 17.83 ?  225 VAL B O   1 
ATOM   3848 C  CB  . VAL B 1 225 ? 42.727 -18.624 77.156  1.00 18.79 ?  225 VAL B CB  1 
ATOM   3849 C  CG1 . VAL B 1 225 ? 43.170 -17.647 78.228  1.00 19.36 ?  225 VAL B CG1 1 
ATOM   3850 C  CG2 . VAL B 1 225 ? 42.773 -20.043 77.678  1.00 18.23 ?  225 VAL B CG2 1 
ATOM   3851 N  N   . PHE B 1 226 ? 41.675 -16.320 75.290  1.00 14.91 ?  226 PHE B N   1 
ATOM   3852 C  CA  . PHE B 1 226 ? 41.497 -14.909 74.962  1.00 16.70 ?  226 PHE B CA  1 
ATOM   3853 C  C   . PHE B 1 226 ? 40.029 -14.571 74.736  1.00 19.53 ?  226 PHE B C   1 
ATOM   3854 O  O   . PHE B 1 226 ? 39.588 -13.466 75.072  1.00 22.87 ?  226 PHE B O   1 
ATOM   3855 C  CB  . PHE B 1 226 ? 42.326 -14.543 73.723  1.00 15.59 ?  226 PHE B CB  1 
ATOM   3856 C  CG  . PHE B 1 226 ? 43.803 -14.367 74.008  1.00 15.93 ?  226 PHE B CG  1 
ATOM   3857 C  CD1 . PHE B 1 226 ? 44.292 -13.166 74.521  1.00 18.83 ?  226 PHE B CD1 1 
ATOM   3858 C  CD2 . PHE B 1 226 ? 44.688 -15.409 73.813  1.00 18.15 ?  226 PHE B CD2 1 
ATOM   3859 C  CE1 . PHE B 1 226 ? 45.640 -13.005 74.795  1.00 17.89 ?  226 PHE B CE1 1 
ATOM   3860 C  CE2 . PHE B 1 226 ? 46.044 -15.256 74.085  1.00 17.78 ?  226 PHE B CE2 1 
ATOM   3861 C  CZ  . PHE B 1 226 ? 46.516 -14.039 74.590  1.00 18.05 ?  226 PHE B CZ  1 
ATOM   3862 N  N   . GLU B 1 227 ? 39.249 -15.509 74.190  1.00 17.02 ?  227 GLU B N   1 
ATOM   3863 C  CA  . GLU B 1 227 ? 37.826 -15.251 74.013  1.00 18.43 ?  227 GLU B CA  1 
ATOM   3864 C  C   . GLU B 1 227 ? 37.094 -15.207 75.348  1.00 21.27 ?  227 GLU B C   1 
ATOM   3865 O  O   . GLU B 1 227 ? 36.120 -14.462 75.488  1.00 21.21 ?  227 GLU B O   1 
ATOM   3866 C  CB  . GLU B 1 227 ? 37.212 -16.301 73.091  1.00 22.67 ?  227 GLU B CB  1 
ATOM   3867 C  CG  . GLU B 1 227 ? 35.747 -16.036 72.778  1.00 27.22 ?  227 GLU B CG  1 
ATOM   3868 C  CD  . GLU B 1 227 ? 35.446 -16.177 71.303  1.00 47.49 ?  227 GLU B CD  1 
ATOM   3869 O  OE1 . GLU B 1 227 ? 35.391 -15.134 70.614  1.00 50.70 ?  227 GLU B OE1 1 
ATOM   3870 O  OE2 . GLU B 1 227 ? 35.264 -17.321 70.836  1.00 56.40 -1 227 GLU B OE2 1 
ATOM   3871 N  N   . ALA B 1 228 ? 37.573 -15.955 76.346  1.00 15.81 ?  228 ALA B N   1 
ATOM   3872 C  CA  . ALA B 1 228 ? 36.832 -16.111 77.594  1.00 18.26 ?  228 ALA B CA  1 
ATOM   3873 C  C   . ALA B 1 228 ? 37.050 -14.968 78.583  1.00 19.67 ?  228 ALA B C   1 
ATOM   3874 O  O   . ALA B 1 228 ? 36.148 -14.676 79.375  1.00 18.87 ?  228 ALA B O   1 
ATOM   3875 C  CB  . ALA B 1 228 ? 37.202 -17.439 78.253  1.00 20.51 ?  228 ALA B CB  1 
ATOM   3876 N  N   . ILE B 1 229 ? 38.218 -14.336 78.605  1.00 18.94 ?  229 ILE B N   1 
ATOM   3877 C  CA  . ILE B 1 229 ? 38.467 -13.276 79.582  1.00 17.43 ?  229 ILE B CA  1 
ATOM   3878 C  C   . ILE B 1 229 ? 37.622 -12.058 79.223  1.00 19.17 ?  229 ILE B C   1 
ATOM   3879 O  O   . ILE B 1 229 ? 37.719 -11.553 78.094  1.00 22.60 ?  229 ILE B O   1 
ATOM   3880 C  CB  . ILE B 1 229 ? 39.958 -12.899 79.657  1.00 17.71 ?  229 ILE B CB  1 
ATOM   3881 C  CG1 . ILE B 1 229 ? 40.831 -14.126 79.971  1.00 21.30 ?  229 ILE B CG1 1 
ATOM   3882 C  CG2 . ILE B 1 229 ? 40.172 -11.756 80.680  1.00 17.84 ?  229 ILE B CG2 1 
ATOM   3883 C  CD1 . ILE B 1 229 ? 40.518 -14.813 81.264  1.00 22.39 ?  229 ILE B CD1 1 
ATOM   3884 N  N   . PRO B 1 230 ? 36.774 -11.568 80.128  1.00 18.25 ?  230 PRO B N   1 
ATOM   3885 C  CA  . PRO B 1 230 ? 35.956 -10.394 79.810  1.00 19.15 ?  230 PRO B CA  1 
ATOM   3886 C  C   . PRO B 1 230 ? 36.812 -9.180  79.486  1.00 22.78 ?  230 PRO B C   1 
ATOM   3887 O  O   . PRO B 1 230 ? 37.807 -8.897  80.158  1.00 19.73 ?  230 PRO B O   1 
ATOM   3888 C  CB  . PRO B 1 230 ? 35.132 -10.180 81.088  1.00 22.84 ?  230 PRO B CB  1 
ATOM   3889 C  CG  . PRO B 1 230 ? 35.069 -11.528 81.708  1.00 22.20 ?  230 PRO B CG  1 
ATOM   3890 C  CD  . PRO B 1 230 ? 36.434 -12.134 81.440  1.00 20.23 ?  230 PRO B CD  1 
ATOM   3891 N  N   . ALA B 1 231 ? 36.391 -8.448  78.451  1.00 24.41 ?  231 ALA B N   1 
ATOM   3892 C  CA  . ALA B 1 231 ? 37.154 -7.298  77.967  1.00 23.90 ?  231 ALA B CA  1 
ATOM   3893 C  C   . ALA B 1 231 ? 37.378 -6.270  79.063  1.00 24.56 ?  231 ALA B C   1 
ATOM   3894 O  O   . ALA B 1 231 ? 38.460 -5.676  79.157  1.00 28.66 ?  231 ALA B O   1 
ATOM   3895 C  CB  . ALA B 1 231 ? 36.434 -6.653  76.781  1.00 26.78 ?  231 ALA B CB  1 
ATOM   3896 N  N   . GLU B 1 232 ? 36.368 -6.045  79.902  1.00 25.46 ?  232 GLU B N   1 
ATOM   3897 C  CA  . GLU B 1 232 ? 36.488 -5.046  80.951  1.00 27.98 ?  232 GLU B CA  1 
ATOM   3898 C  C   . GLU B 1 232 ? 37.489 -5.454  82.019  1.00 27.05 ?  232 GLU B C   1 
ATOM   3899 O  O   . GLU B 1 232 ? 37.924 -4.598  82.795  1.00 31.97 ?  232 GLU B O   1 
ATOM   3900 C  CB  . GLU B 1 232 ? 35.120 -4.780  81.584  1.00 32.37 ?  232 GLU B CB  1 
ATOM   3901 C  CG  . GLU B 1 232 ? 34.410 -6.031  82.105  1.00 39.13 ?  232 GLU B CG  1 
ATOM   3902 C  CD  . GLU B 1 232 ? 33.583 -6.744  81.036  1.00 43.68 ?  232 GLU B CD  1 
ATOM   3903 O  OE1 . GLU B 1 232 ? 33.930 -6.654  79.838  1.00 36.81 ?  232 GLU B OE1 1 
ATOM   3904 O  OE2 . GLU B 1 232 ? 32.579 -7.397  81.402  1.00 47.17 -1 232 GLU B OE2 1 
ATOM   3905 N  N   . ARG B 1 233 ? 37.879 -6.730  82.066  1.00 23.14 ?  233 ARG B N   1 
ATOM   3906 C  CA  . ARG B 1 233 ? 38.797 -7.209  83.087  1.00 19.09 ?  233 ARG B CA  1 
ATOM   3907 C  C   . ARG B 1 233 ? 40.221 -7.400  82.587  1.00 20.65 ?  233 ARG B C   1 
ATOM   3908 O  O   . ARG B 1 233 ? 41.118 -7.575  83.411  1.00 19.57 ?  233 ARG B O   1 
ATOM   3909 C  CB  . ARG B 1 233 ? 38.298 -8.527  83.675  1.00 24.69 ?  233 ARG B CB  1 
ATOM   3910 C  CG  . ARG B 1 233 ? 36.826 -8.476  84.034  1.00 27.34 ?  233 ARG B CG  1 
ATOM   3911 C  CD  . ARG B 1 233 ? 36.523 -9.132  85.362  1.00 33.75 ?  233 ARG B CD  1 
ATOM   3912 N  NE  . ARG B 1 233 ? 35.092 -9.047  85.650  1.00 49.76 ?  233 ARG B NE  1 
ATOM   3913 C  CZ  . ARG B 1 233 ? 34.296 -10.094 85.846  1.00 46.97 ?  233 ARG B CZ  1 
ATOM   3914 N  NH1 . ARG B 1 233 ? 34.791 -11.325 85.805  1.00 36.09 ?  233 ARG B NH1 1 
ATOM   3915 N  NH2 . ARG B 1 233 ? 33.003 -9.909  86.090  1.00 55.04 ?  233 ARG B NH2 1 
ATOM   3916 N  N   . LEU B 1 234 ? 40.450 -7.340  81.282  1.00 18.02 ?  234 LEU B N   1 
ATOM   3917 C  CA  . LEU B 1 234 ? 41.778 -7.578  80.731  1.00 19.48 ?  234 LEU B CA  1 
ATOM   3918 C  C   . LEU B 1 234 ? 42.600 -6.296  80.831  1.00 17.14 ?  234 LEU B C   1 
ATOM   3919 O  O   . LEU B 1 234 ? 42.291 -5.299  80.165  1.00 20.04 ?  234 LEU B O   1 
ATOM   3920 C  CB  . LEU B 1 234 ? 41.654 -8.061  79.290  1.00 16.83 ?  234 LEU B CB  1 
ATOM   3921 C  CG  . LEU B 1 234 ? 42.978 -8.453  78.621  1.00 13.95 ?  234 LEU B CG  1 
ATOM   3922 C  CD1 . LEU B 1 234 ? 43.624 -9.626  79.322  1.00 16.78 ?  234 LEU B CD1 1 
ATOM   3923 C  CD2 . LEU B 1 234 ? 42.716 -8.753  77.123  1.00 18.61 ?  234 LEU B CD2 1 
ATOM   3924 N  N   . ILE B 1 235 ? 43.661 -6.338  81.645  1.00 15.27 ?  235 ILE B N   1 
ATOM   3925 C  CA  . ILE B 1 235 ? 44.562 -5.198  81.804  1.00 18.22 ?  235 ILE B CA  1 
ATOM   3926 C  C   . ILE B 1 235 ? 45.506 -5.095  80.616  1.00 18.87 ?  235 ILE B C   1 
ATOM   3927 O  O   . ILE B 1 235 ? 45.772 -4.007  80.092  1.00 18.39 ?  235 ILE B O   1 
ATOM   3928 C  CB  . ILE B 1 235 ? 45.373 -5.327  83.107  1.00 18.25 ?  235 ILE B CB  1 
ATOM   3929 C  CG1 . ILE B 1 235 ? 44.472 -5.455  84.332  1.00 20.60 ?  235 ILE B CG1 1 
ATOM   3930 C  CG2 . ILE B 1 235 ? 46.338 -4.163  83.260  1.00 18.01 ?  235 ILE B CG2 1 
ATOM   3931 C  CD1 . ILE B 1 235 ? 45.257 -5.968  85.519  1.00 19.79 ?  235 ILE B CD1 1 
ATOM   3932 N  N   . GLY B 1 236 ? 46.059 -6.222  80.197  1.00 15.49 ?  236 GLY B N   1 
ATOM   3933 C  CA  . GLY B 1 236 ? 47.073 -6.163  79.161  1.00 12.44 ?  236 GLY B CA  1 
ATOM   3934 C  C   . GLY B 1 236 ? 47.542 -7.552  78.812  1.00 13.26 ?  236 GLY B C   1 
ATOM   3935 O  O   . GLY B 1 236 ? 47.195 -8.541  79.467  1.00 13.54 ?  236 GLY B O   1 
ATOM   3936 N  N   . VAL B 1 237 ? 48.361 -7.602  77.760  1.00 13.62 ?  237 VAL B N   1 
ATOM   3937 C  CA  . VAL B 1 237 ? 48.859 -8.842  77.182  1.00 13.98 ?  237 VAL B CA  1 
ATOM   3938 C  C   . VAL B 1 237 ? 50.320 -8.635  76.809  1.00 13.96 ?  237 VAL B C   1 
ATOM   3939 O  O   . VAL B 1 237 ? 50.668 -7.621  76.190  1.00 13.44 ?  237 VAL B O   1 
ATOM   3940 C  CB  . VAL B 1 237 ? 48.043 -9.258  75.934  1.00 11.79 ?  237 VAL B CB  1 
ATOM   3941 C  CG1 . VAL B 1 237 ? 48.573 -10.550 75.347  1.00 15.49 ?  237 VAL B CG1 1 
ATOM   3942 C  CG2 . VAL B 1 237 ? 46.546 -9.401  76.265  1.00 13.18 ?  237 VAL B CG2 1 
ATOM   3943 N  N   . GLU B 1 238 ? 51.170 -9.578  77.196  1.00 12.30 ?  238 GLU B N   1 
ATOM   3944 C  CA  . GLU B 1 238 ? 52.558 -9.639  76.739  1.00 12.95 ?  238 GLU B CA  1 
ATOM   3945 C  C   . GLU B 1 238 ? 52.719 -10.842 75.834  1.00 13.57 ?  238 GLU B C   1 
ATOM   3946 O  O   . GLU B 1 238 ? 52.320 -11.949 76.199  1.00 14.01 ?  238 GLU B O   1 
ATOM   3947 C  CB  . GLU B 1 238 ? 53.557 -9.768  77.889  1.00 16.40 ?  238 GLU B CB  1 
ATOM   3948 C  CG  . GLU B 1 238 ? 53.417 -8.796  78.990  1.00 19.16 ?  238 GLU B CG  1 
ATOM   3949 C  CD  . GLU B 1 238 ? 54.441 -9.056  80.065  1.00 19.00 ?  238 GLU B CD  1 
ATOM   3950 O  OE1 . GLU B 1 238 ? 54.222 -9.943  80.923  1.00 19.57 ?  238 GLU B OE1 1 
ATOM   3951 O  OE2 . GLU B 1 238 ? 55.477 -8.372  80.036  1.00 22.26 -1 238 GLU B OE2 1 
ATOM   3952 N  N   . LEU B 1 239 ? 53.320 -10.622 74.673  1.00 12.35 ?  239 LEU B N   1 
ATOM   3953 C  CA  . LEU B 1 239 ? 53.597 -11.665 73.692  1.00 13.76 ?  239 LEU B CA  1 
ATOM   3954 C  C   . LEU B 1 239 ? 55.106 -11.813 73.579  1.00 13.33 ?  239 LEU B C   1 
ATOM   3955 O  O   . LEU B 1 239 ? 55.786 -10.838 73.234  1.00 14.55 ?  239 LEU B O   1 
ATOM   3956 C  CB  . LEU B 1 239 ? 53.008 -11.294 72.329  1.00 14.53 ?  239 LEU B CB  1 
ATOM   3957 C  CG  . LEU B 1 239 ? 51.542 -10.908 72.253  1.00 14.53 ?  239 LEU B CG  1 
ATOM   3958 C  CD1 . LEU B 1 239 ? 51.168 -10.591 70.799  1.00 19.38 ?  239 LEU B CD1 1 
ATOM   3959 C  CD2 . LEU B 1 239 ? 50.691 -12.036 72.787  1.00 13.68 ?  239 LEU B CD2 1 
ATOM   3960 N  N   . ALA B 1 240 ? 55.629 -13.022 73.811  1.00 11.58 ?  240 ALA B N   1 
ATOM   3961 C  CA  . ALA B 1 240 ? 57.079 -13.178 73.890  1.00 12.70 ?  240 ALA B CA  1 
ATOM   3962 C  C   . ALA B 1 240 ? 57.572 -14.441 73.190  1.00 15.02 ?  240 ALA B C   1 
ATOM   3963 O  O   . ALA B 1 240 ? 56.906 -15.481 73.178  1.00 13.18 ?  240 ALA B O   1 
ATOM   3964 C  CB  . ALA B 1 240 ? 57.562 -13.211 75.348  1.00 17.81 ?  240 ALA B CB  1 
ATOM   3965 N  N   . GLU B 1 241 ? 58.784 -14.321 72.626  1.00 16.44 ?  241 GLU B N   1 
ATOM   3966 C  CA  . GLU B 1 241 ? 59.690 -15.415 72.261  1.00 17.69 ?  241 GLU B CA  1 
ATOM   3967 C  C   . GLU B 1 241 ? 59.338 -16.105 70.950  1.00 18.13 ?  241 GLU B C   1 
ATOM   3968 O  O   . GLU B 1 241 ? 59.472 -17.328 70.827  1.00 24.59 ?  241 GLU B O   1 
ATOM   3969 C  CB  . GLU B 1 241 ? 59.779 -16.442 73.388  1.00 18.33 ?  241 GLU B CB  1 
ATOM   3970 C  CG  . GLU B 1 241 ? 60.166 -15.807 74.716  1.00 18.57 ?  241 GLU B CG  1 
ATOM   3971 C  CD  . GLU B 1 241 ? 61.385 -16.404 75.357  1.00 24.19 ?  241 GLU B CD  1 
ATOM   3972 O  OE1 . GLU B 1 241 ? 61.961 -15.730 76.229  1.00 21.01 ?  241 GLU B OE1 1 
ATOM   3973 O  OE2 . GLU B 1 241 ? 61.779 -17.537 75.000  1.00 34.21 -1 241 GLU B OE2 1 
ATOM   3974 N  N   . LEU B 1 242 ? 58.930 -15.336 69.952  1.00 17.87 ?  242 LEU B N   1 
ATOM   3975 C  CA  . LEU B 1 242 ? 58.972 -15.824 68.581  1.00 15.92 ?  242 LEU B CA  1 
ATOM   3976 C  C   . LEU B 1 242 ? 60.413 -15.721 68.091  1.00 16.30 ?  242 LEU B C   1 
ATOM   3977 O  O   . LEU B 1 242 ? 60.961 -14.617 68.009  1.00 17.16 ?  242 LEU B O   1 
ATOM   3978 C  CB  . LEU B 1 242 ? 58.038 -15.013 67.686  1.00 16.76 ?  242 LEU B CB  1 
ATOM   3979 C  CG  . LEU B 1 242 ? 58.168 -15.335 66.193  1.00 18.54 ?  242 LEU B CG  1 
ATOM   3980 C  CD1 . LEU B 1 242 ? 57.818 -16.792 65.897  1.00 21.20 ?  242 LEU B CD1 1 
ATOM   3981 C  CD2 . LEU B 1 242 ? 57.305 -14.388 65.371  1.00 16.91 ?  242 LEU B CD2 1 
ATOM   3982 N  N   . ASN B 1 243 ? 61.034 -16.862 67.775  1.00 14.81 ?  243 ASN B N   1 
ATOM   3983 C  CA  . ASN B 1 243 ? 62.423 -16.900 67.306  1.00 14.05 ?  243 ASN B CA  1 
ATOM   3984 C  C   . ASN B 1 243 ? 62.398 -17.191 65.811  1.00 16.99 ?  243 ASN B C   1 
ATOM   3985 O  O   . ASN B 1 243 ? 62.442 -18.352 65.398  1.00 19.97 ?  243 ASN B O   1 
ATOM   3986 C  CB  . ASN B 1 243 ? 63.250 -17.960 68.052  1.00 16.32 ?  243 ASN B CB  1 
ATOM   3987 C  CG  . ASN B 1 243 ? 64.716 -17.938 67.638  1.00 15.96 ?  243 ASN B CG  1 
ATOM   3988 O  OD1 . ASN B 1 243 ? 65.288 -16.872 67.454  1.00 17.11 ?  243 ASN B OD1 1 
ATOM   3989 N  ND2 . ASN B 1 243 ? 65.309 -19.116 67.450  1.00 21.87 ?  243 ASN B ND2 1 
ATOM   3990 N  N   . ALA B 1 244 ? 62.351 -16.128 64.998  1.00 14.16 ?  244 ALA B N   1 
ATOM   3991 C  CA  . ALA B 1 244 ? 62.314 -16.347 63.555  1.00 18.08 ?  244 ALA B CA  1 
ATOM   3992 C  C   . ALA B 1 244 ? 62.784 -15.091 62.848  1.00 16.30 ?  244 ALA B C   1 
ATOM   3993 O  O   . ALA B 1 244 ? 62.393 -13.992 63.258  1.00 15.29 ?  244 ALA B O   1 
ATOM   3994 C  CB  . ALA B 1 244 ? 60.895 -16.714 63.092  1.00 21.19 ?  244 ALA B CB  1 
ATOM   3995 N  N   . PRO B 1 245 ? 63.596 -15.196 61.791  1.00 14.24 ?  245 PRO B N   1 
ATOM   3996 C  CA  . PRO B 1 245 ? 63.957 -14.004 61.015  1.00 14.52 ?  245 PRO B CA  1 
ATOM   3997 C  C   . PRO B 1 245 ? 62.708 -13.306 60.489  1.00 12.73 ?  245 PRO B C   1 
ATOM   3998 O  O   . PRO B 1 245 ? 61.735 -13.949 60.085  1.00 13.63 ?  245 PRO B O   1 
ATOM   3999 C  CB  . PRO B 1 245 ? 64.820 -14.567 59.872  1.00 15.79 ?  245 PRO B CB  1 
ATOM   4000 C  CG  . PRO B 1 245 ? 65.285 -15.920 60.390  1.00 18.12 ?  245 PRO B CG  1 
ATOM   4001 C  CD  . PRO B 1 245 ? 64.160 -16.432 61.229  1.00 16.47 ?  245 PRO B CD  1 
ATOM   4002 N  N   . ALA B 1 246 ? 62.750 -11.974 60.487  1.00 14.96 ?  246 ALA B N   1 
ATOM   4003 C  CA  . ALA B 1 246 ? 61.544 -11.204 60.174  1.00 15.95 ?  246 ALA B CA  1 
ATOM   4004 C  C   . ALA B 1 246 ? 61.049 -11.457 58.752  1.00 18.22 ?  246 ALA B C   1 
ATOM   4005 O  O   . ALA B 1 246 ? 59.839 -11.419 58.502  1.00 20.83 ?  246 ALA B O   1 
ATOM   4006 C  CB  . ALA B 1 246 ? 61.798 -9.714  60.392  1.00 16.86 ?  246 ALA B CB  1 
ATOM   4007 N  N   . ASP B 1 247 ? 61.947 -11.759 57.822  1.00 17.15 ?  247 ASP B N   1 
ATOM   4008 C  CA  . ASP B 1 247 ? 61.559 -11.978 56.436  1.00 19.79 ?  247 ASP B CA  1 
ATOM   4009 C  C   . ASP B 1 247 ? 61.392 -13.455 56.090  1.00 23.43 ?  247 ASP B C   1 
ATOM   4010 O  O   . ASP B 1 247 ? 61.313 -13.799 54.909  1.00 28.39 ?  247 ASP B O   1 
ATOM   4011 C  CB  . ASP B 1 247 ? 62.586 -11.332 55.501  1.00 20.90 ?  247 ASP B CB  1 
ATOM   4012 C  CG  . ASP B 1 247 ? 63.959 -11.937 55.641  1.00 29.57 ?  247 ASP B CG  1 
ATOM   4013 O  OD1 . ASP B 1 247 ? 64.247 -12.543 56.698  1.00 28.20 ?  247 ASP B OD1 1 
ATOM   4014 O  OD2 . ASP B 1 247 ? 64.768 -11.799 54.699  1.00 41.43 -1 247 ASP B OD2 1 
ATOM   4015 N  N   . SER B 1 248 ? 61.319 -14.333 57.079  1.00 15.26 ?  248 SER B N   1 
ATOM   4016 C  CA  . SER B 1 248 ? 61.290 -15.764 56.807  1.00 14.97 ?  248 SER B CA  1 
ATOM   4017 C  C   . SER B 1 248 ? 59.868 -16.285 56.607  1.00 18.86 ?  248 SER B C   1 
ATOM   4018 O  O   . SER B 1 248 ? 58.888 -15.705 57.095  1.00 16.49 ?  248 SER B O   1 
ATOM   4019 C  CB  . SER B 1 248 ? 61.976 -16.535 57.945  1.00 16.22 ?  248 SER B CB  1 
ATOM   4020 O  OG  . SER B 1 248 ? 61.203 -16.500 59.149  1.00 15.07 ?  248 SER B OG  1 
ATOM   4021 N  N   . GLU B 1 249 ? 59.766 -17.398 55.880  1.00 17.37 ?  249 GLU B N   1 
ATOM   4022 C  CA  . GLU B 1 249 ? 58.483 -18.074 55.728  1.00 18.70 ?  249 GLU B CA  1 
ATOM   4023 C  C   . GLU B 1 249 ? 57.920 -18.517 57.072  1.00 15.82 ?  249 GLU B C   1 
ATOM   4024 O  O   . GLU B 1 249 ? 56.715 -18.383 57.327  1.00 17.13 ?  249 GLU B O   1 
ATOM   4025 C  CB  . GLU B 1 249 ? 58.639 -19.282 54.801  1.00 23.22 ?  249 GLU B CB  1 
ATOM   4026 C  CG  . GLU B 1 249 ? 57.349 -20.040 54.573  1.00 35.08 ?  249 GLU B CG  1 
ATOM   4027 C  CD  . GLU B 1 249 ? 56.328 -19.210 53.827  1.00 39.42 ?  249 GLU B CD  1 
ATOM   4028 O  OE1 . GLU B 1 249 ? 56.740 -18.323 53.047  1.00 46.47 ?  249 GLU B OE1 1 
ATOM   4029 O  OE2 . GLU B 1 249 ? 55.116 -19.444 54.021  1.00 46.00 -1 249 GLU B OE2 1 
ATOM   4030 N  N   . ARG B 1 250 ? 58.769 -19.064 57.945  1.00 15.38 ?  250 ARG B N   1 
ATOM   4031 C  CA  . ARG B 1 250 ? 58.264 -19.535 59.223  1.00 15.61 ?  250 ARG B CA  1 
ATOM   4032 C  C   . ARG B 1 250 ? 57.769 -18.387 60.091  1.00 15.46 ?  250 ARG B C   1 
ATOM   4033 O  O   . ARG B 1 250 ? 56.848 -18.596 60.886  1.00 14.97 ?  250 ARG B O   1 
ATOM   4034 C  CB  . ARG B 1 250 ? 59.325 -20.353 59.961  1.00 19.14 ?  250 ARG B CB  1 
ATOM   4035 C  CG  . ARG B 1 250 ? 60.608 -19.631 60.350  1.00 16.44 ?  250 ARG B CG  1 
ATOM   4036 C  CD  . ARG B 1 250 ? 61.618 -20.706 60.791  1.00 18.17 ?  250 ARG B CD  1 
ATOM   4037 N  NE  . ARG B 1 250 ? 62.953 -20.243 61.171  1.00 16.07 ?  250 ARG B NE  1 
ATOM   4038 C  CZ  . ARG B 1 250 ? 63.918 -19.927 60.306  1.00 15.62 ?  250 ARG B CZ  1 
ATOM   4039 N  NH1 . ARG B 1 250 ? 65.112 -19.567 60.757  1.00 17.45 ?  250 ARG B NH1 1 
ATOM   4040 N  NH2 . ARG B 1 250 ? 63.688 -19.948 58.992  1.00 16.90 ?  250 ARG B NH2 1 
ATOM   4041 N  N   . ALA B 1 251 ? 58.351 -17.187 59.964  1.00 12.64 ?  251 ALA B N   1 
ATOM   4042 C  CA  . ALA B 1 251 ? 57.806 -16.048 60.704  1.00 14.32 ?  251 ALA B CA  1 
ATOM   4043 C  C   . ALA B 1 251 ? 56.433 -15.676 60.169  1.00 14.08 ?  251 ALA B C   1 
ATOM   4044 O  O   . ALA B 1 251 ? 55.519 -15.369 60.941  1.00 15.46 ?  251 ALA B O   1 
ATOM   4045 C  CB  . ALA B 1 251 ? 58.753 -14.848 60.638  1.00 15.25 ?  251 ALA B CB  1 
ATOM   4046 N  N   . GLU B 1 252 ? 56.272 -15.682 58.850  1.00 14.50 ?  252 GLU B N   1 
ATOM   4047 C  CA  . GLU B 1 252 ? 54.981 -15.353 58.253  1.00 16.88 ?  252 GLU B CA  1 
ATOM   4048 C  C   . GLU B 1 252 ? 53.903 -16.309 58.734  1.00 17.74 ?  252 GLU B C   1 
ATOM   4049 O  O   . GLU B 1 252 ? 52.807 -15.885 59.121  1.00 15.82 ?  252 GLU B O   1 
ATOM   4050 C  CB  . GLU B 1 252 ? 55.102 -15.394 56.733  1.00 17.72 ?  252 GLU B CB  1 
ATOM   4051 C  CG  . GLU B 1 252 ? 53.870 -14.896 55.993  1.00 20.01 ?  252 GLU B CG  1 
ATOM   4052 C  CD  . GLU B 1 252 ? 54.052 -14.998 54.492  1.00 36.03 ?  252 GLU B CD  1 
ATOM   4053 O  OE1 . GLU B 1 252 ? 53.821 -16.094 53.936  1.00 40.07 ?  252 GLU B OE1 1 
ATOM   4054 O  OE2 . GLU B 1 252 ? 54.468 -13.991 53.881  1.00 40.66 -1 252 GLU B OE2 1 
ATOM   4055 N  N   . GLN B 1 253 ? 54.205 -17.609 58.726  1.00 13.61 ?  253 GLN B N   1 
ATOM   4056 C  CA  . GLN B 1 253 ? 53.244 -18.603 59.194  1.00 16.79 ?  253 GLN B CA  1 
ATOM   4057 C  C   . GLN B 1 253 ? 52.959 -18.428 60.676  1.00 16.94 ?  253 GLN B C   1 
ATOM   4058 O  O   . GLN B 1 253 ? 51.803 -18.513 61.105  1.00 17.75 ?  253 GLN B O   1 
ATOM   4059 C  CB  . GLN B 1 253 ? 53.764 -20.016 58.904  1.00 20.92 ?  253 GLN B CB  1 
ATOM   4060 C  CG  . GLN B 1 253 ? 53.999 -20.294 57.427  1.00 27.46 ?  253 GLN B CG  1 
ATOM   4061 C  CD  . GLN B 1 253 ? 52.736 -20.145 56.602  1.00 40.88 ?  253 GLN B CD  1 
ATOM   4062 O  OE1 . GLN B 1 253 ? 52.558 -19.156 55.889  1.00 48.23 ?  253 GLN B OE1 1 
ATOM   4063 N  NE2 . GLN B 1 253 ? 51.847 -21.130 56.699  1.00 51.85 ?  253 GLN B NE2 1 
ATOM   4064 N  N   . ALA B 1 254 ? 53.992 -18.137 61.466  1.00 15.25 ?  254 ALA B N   1 
ATOM   4065 C  CA  . ALA B 1 254 ? 53.806 -18.006 62.905  1.00 13.59 ?  254 ALA B CA  1 
ATOM   4066 C  C   . ALA B 1 254 ? 52.930 -16.811 63.255  1.00 14.93 ?  254 ALA B C   1 
ATOM   4067 O  O   . ALA B 1 254 ? 52.061 -16.924 64.129  1.00 14.31 ?  254 ALA B O   1 
ATOM   4068 C  CB  . ALA B 1 254 ? 55.152 -17.885 63.611  1.00 17.11 ?  254 ALA B CB  1 
ATOM   4069 N  N   . VAL B 1 255 ? 53.154 -15.655 62.616  1.00 14.87 ?  255 VAL B N   1 
ATOM   4070 C  CA  . VAL B 1 255 ? 52.364 -14.486 63.014  1.00 13.57 ?  255 VAL B CA  1 
ATOM   4071 C  C   . VAL B 1 255 ? 50.907 -14.665 62.622  1.00 14.02 ?  255 VAL B C   1 
ATOM   4072 O  O   . VAL B 1 255 ? 50.029 -14.071 63.249  1.00 14.69 ?  255 VAL B O   1 
ATOM   4073 C  CB  . VAL B 1 255 ? 52.925 -13.152 62.472  1.00 13.70 ?  255 VAL B CB  1 
ATOM   4074 C  CG1 . VAL B 1 255 ? 54.317 -12.894 63.040  1.00 17.74 ?  255 VAL B CG1 1 
ATOM   4075 C  CG2 . VAL B 1 255 ? 52.899 -13.089 60.937  1.00 18.18 ?  255 VAL B CG2 1 
ATOM   4076 N  N   . ALA B 1 256 ? 50.613 -15.468 61.598  1.00 13.83 ?  256 ALA B N   1 
ATOM   4077 C  CA  . ALA B 1 256 ? 49.219 -15.754 61.279  1.00 14.87 ?  256 ALA B CA  1 
ATOM   4078 C  C   . ALA B 1 256 ? 48.536 -16.473 62.430  1.00 14.08 ?  256 ALA B C   1 
ATOM   4079 O  O   . ALA B 1 256 ? 47.376 -16.186 62.754  1.00 16.00 ?  256 ALA B O   1 
ATOM   4080 C  CB  . ALA B 1 256 ? 49.124 -16.582 59.995  1.00 17.19 ?  256 ALA B CB  1 
ATOM   4081 N  N   . VAL B 1 257 ? 49.246 -17.398 63.078  1.00 14.19 ?  257 VAL B N   1 
ATOM   4082 C  CA  . VAL B 1 257 ? 48.672 -18.108 64.210  1.00 13.38 ?  257 VAL B CA  1 
ATOM   4083 C  C   . VAL B 1 257 ? 48.559 -17.180 65.404  1.00 15.52 ?  257 VAL B C   1 
ATOM   4084 O  O   . VAL B 1 257 ? 47.541 -17.177 66.112  1.00 14.88 ?  257 VAL B O   1 
ATOM   4085 C  CB  . VAL B 1 257 ? 49.514 -19.356 64.525  1.00 15.85 ?  257 VAL B CB  1 
ATOM   4086 C  CG1 . VAL B 1 257 ? 48.936 -20.110 65.722  1.00 22.38 ?  257 VAL B CG1 1 
ATOM   4087 C  CG2 . VAL B 1 257 ? 49.588 -20.256 63.297  1.00 18.35 ?  257 VAL B CG2 1 
ATOM   4088 N  N   . ILE B 1 258 ? 49.598 -16.372 65.641  1.00 14.15 ?  258 ILE B N   1 
ATOM   4089 C  CA  . ILE B 1 258 ? 49.584 -15.433 66.762  1.00 15.33 ?  258 ILE B CA  1 
ATOM   4090 C  C   . ILE B 1 258 ? 48.398 -14.486 66.658  1.00 15.11 ?  258 ILE B C   1 
ATOM   4091 O  O   . ILE B 1 258 ? 47.653 -14.297 67.624  1.00 14.01 ?  258 ILE B O   1 
ATOM   4092 C  CB  . ILE B 1 258 ? 50.915 -14.661 66.826  1.00 15.66 ?  258 ILE B CB  1 
ATOM   4093 C  CG1 . ILE B 1 258 ? 52.023 -15.604 67.297  1.00 15.83 ?  258 ILE B CG1 1 
ATOM   4094 C  CG2 . ILE B 1 258 ? 50.777 -13.459 67.775  1.00 16.39 ?  258 ILE B CG2 1 
ATOM   4095 C  CD1 . ILE B 1 258 ? 53.446 -15.051 67.120  1.00 16.39 ?  258 ILE B CD1 1 
ATOM   4096 N  N   . LEU B 1 259 ? 48.208 -13.867 65.494  1.00 14.08 ?  259 LEU B N   1 
ATOM   4097 C  CA  . LEU B 1 259 ? 47.110 -12.910 65.350  1.00 12.79 ?  259 LEU B CA  1 
ATOM   4098 C  C   . LEU B 1 259 ? 45.767 -13.582 65.587  1.00 15.17 ?  259 LEU B C   1 
ATOM   4099 O  O   . LEU B 1 259 ? 44.852 -12.972 66.157  1.00 14.35 ?  259 LEU B O   1 
ATOM   4100 C  CB  . LEU B 1 259 ? 47.125 -12.273 63.957  1.00 13.92 ?  259 LEU B CB  1 
ATOM   4101 C  CG  . LEU B 1 259 ? 48.230 -11.286 63.624  1.00 27.41 ?  259 LEU B CG  1 
ATOM   4102 C  CD1 . LEU B 1 259 ? 48.034 -10.685 62.246  1.00 24.38 ?  259 LEU B CD1 1 
ATOM   4103 C  CD2 . LEU B 1 259 ? 48.213 -10.235 64.643  1.00 24.68 ?  259 LEU B CD2 1 
ATOM   4104 N  N   . ASP B 1 260 ? 45.622 -14.826 65.125  1.00 15.03 ?  260 ASP B N   1 
ATOM   4105 C  CA  . ASP B 1 260 ? 44.377 -15.568 65.336  1.00 13.87 ?  260 ASP B CA  1 
ATOM   4106 C  C   . ASP B 1 260 ? 44.119 -15.808 66.817  1.00 13.96 ?  260 ASP B C   1 
ATOM   4107 O  O   . ASP B 1 260 ? 42.982 -15.667 67.288  1.00 15.21 ?  260 ASP B O   1 
ATOM   4108 C  CB  . ASP B 1 260 ? 44.455 -16.898 64.573  1.00 16.15 ?  260 ASP B CB  1 
ATOM   4109 C  CG  . ASP B 1 260 ? 43.195 -17.741 64.707  1.00 18.66 ?  260 ASP B CG  1 
ATOM   4110 O  OD1 . ASP B 1 260 ? 42.099 -17.159 64.738  1.00 20.86 ?  260 ASP B OD1 1 
ATOM   4111 O  OD2 . ASP B 1 260 ? 43.324 -18.981 64.718  1.00 29.53 -1 260 ASP B OD2 1 
ATOM   4112 N  N   . MET B 1 261 ? 45.153 -16.182 67.568  1.00 14.40 ?  261 MET B N   1 
ATOM   4113 C  CA  . MET B 1 261 ? 44.923 -16.520 68.970  1.00 13.35 ?  261 MET B CA  1 
ATOM   4114 C  C   . MET B 1 261 ? 44.559 -15.272 69.792  1.00 14.70 ?  261 MET B C   1 
ATOM   4115 O  O   . MET B 1 261 ? 43.706 -15.359 70.685  1.00 14.57 ?  261 MET B O   1 
ATOM   4116 C  CB  . MET B 1 261 ? 46.139 -17.316 69.514  1.00 20.23 ?  261 MET B CB  1 
ATOM   4117 C  CG  . MET B 1 261 ? 46.124 -18.942 69.204  1.00 11.23 ?  261 MET B CG  1 
ATOM   4118 S  SD  . MET B 1 261 ? 47.781 -19.603 69.633  1.00 24.30 ?  261 MET B SD  1 
ATOM   4119 C  CE  . MET B 1 261 ? 48.930 -18.462 68.848  1.00 25.80 ?  261 MET B CE  1 
ATOM   4120 N  N   . VAL B 1 262 ? 45.103 -14.088 69.464  1.00 14.03 ?  262 VAL B N   1 
ATOM   4121 C  CA  . VAL B 1 262 ? 44.814 -12.881 70.250  1.00 16.19 ?  262 VAL B CA  1 
ATOM   4122 C  C   . VAL B 1 262 ? 43.608 -12.092 69.745  1.00 16.22 ?  262 VAL B C   1 
ATOM   4123 O  O   . VAL B 1 262 ? 43.106 -11.212 70.470  1.00 15.36 ?  262 VAL B O   1 
ATOM   4124 C  CB  . VAL B 1 262 ? 46.025 -11.915 70.298  1.00 15.30 ?  262 VAL B CB  1 
ATOM   4125 C  CG1 . VAL B 1 262 ? 47.260 -12.623 70.833  1.00 17.92 ?  262 VAL B CG1 1 
ATOM   4126 C  CG2 . VAL B 1 262 ? 46.307 -11.306 68.930  1.00 16.59 ?  262 VAL B CG2 1 
ATOM   4127 N  N   . ALA B 1 263 ? 43.120 -12.388 68.541  1.00 14.16 ?  263 ALA B N   1 
ATOM   4128 C  CA  . ALA B 1 263 ? 42.072 -11.585 67.911  1.00 12.27 ?  263 ALA B CA  1 
ATOM   4129 C  C   . ALA B 1 263 ? 40.837 -11.365 68.775  1.00 14.27 ?  263 ALA B C   1 
ATOM   4130 O  O   . ALA B 1 263 ? 40.295 -10.252 68.732  1.00 15.90 ?  263 ALA B O   1 
ATOM   4131 C  CB  . ALA B 1 263 ? 41.646 -12.228 66.584  1.00 13.55 ?  263 ALA B CB  1 
ATOM   4132 N  N   . PRO B 1 264 ? 40.315 -12.348 69.527  1.00 15.67 ?  264 PRO B N   1 
ATOM   4133 C  CA  . PRO B 1 264 ? 39.097 -12.066 70.299  1.00 14.94 ?  264 PRO B CA  1 
ATOM   4134 C  C   . PRO B 1 264 ? 39.261 -10.894 71.236  1.00 15.95 ?  264 PRO B C   1 
ATOM   4135 O  O   . PRO B 1 264 ? 38.365 -10.048 71.337  1.00 20.89 ?  264 PRO B O   1 
ATOM   4136 C  CB  . PRO B 1 264 ? 38.860 -13.381 71.059  1.00 14.04 ?  264 PRO B CB  1 
ATOM   4137 C  CG  . PRO B 1 264 ? 39.447 -14.429 70.204  1.00 14.57 ?  264 PRO B CG  1 
ATOM   4138 C  CD  . PRO B 1 264 ? 40.695 -13.769 69.625  1.00 14.16 ?  264 PRO B CD  1 
ATOM   4139 N  N   . ALA B 1 265 ? 40.420 -10.799 71.889  1.00 15.52 ?  265 ALA B N   1 
ATOM   4140 C  CA  . ALA B 1 265 ? 40.691 -9.694  72.794  1.00 14.47 ?  265 ALA B CA  1 
ATOM   4141 C  C   . ALA B 1 265 ? 41.062 -8.417  72.045  1.00 17.15 ?  265 ALA B C   1 
ATOM   4142 O  O   . ALA B 1 265 ? 40.629 -7.322  72.423  1.00 16.76 ?  265 ALA B O   1 
ATOM   4143 C  CB  . ALA B 1 265 ? 41.811 -10.084 73.755  1.00 15.54 ?  265 ALA B CB  1 
ATOM   4144 N  N   . PHE B 1 266 ? 41.877 -8.516  70.994  1.00 14.46 ?  266 PHE B N   1 
ATOM   4145 C  CA  . PHE B 1 266 ? 42.348 -7.275  70.393  1.00 14.09 ?  266 PHE B CA  1 
ATOM   4146 C  C   . PHE B 1 266 ? 41.287 -6.640  69.499  1.00 16.35 ?  266 PHE B C   1 
ATOM   4147 O  O   . PHE B 1 266 ? 41.219 -5.405  69.413  1.00 17.07 ?  266 PHE B O   1 
ATOM   4148 C  CB  . PHE B 1 266 ? 43.632 -7.515  69.583  1.00 14.20 ?  266 PHE B CB  1 
ATOM   4149 C  CG  . PHE B 1 266 ? 44.845 -7.854  70.414  1.00 13.91 ?  266 PHE B CG  1 
ATOM   4150 C  CD1 . PHE B 1 266 ? 44.764 -8.103  71.781  1.00 17.19 ?  266 PHE B CD1 1 
ATOM   4151 C  CD2 . PHE B 1 266 ? 46.090 -7.926  69.803  1.00 15.03 ?  266 PHE B CD2 1 
ATOM   4152 C  CE1 . PHE B 1 266 ? 45.916 -8.419  72.510  1.00 17.15 ?  266 PHE B CE1 1 
ATOM   4153 C  CE2 . PHE B 1 266 ? 47.226 -8.229  70.521  1.00 13.78 ?  266 PHE B CE2 1 
ATOM   4154 C  CZ  . PHE B 1 266 ? 47.143 -8.484  71.874  1.00 14.38 ?  266 PHE B CZ  1 
ATOM   4155 N  N   . ASP B 1 267 ? 40.476 -7.462  68.811  1.00 15.57 ?  267 ASP B N   1 
ATOM   4156 C  CA  . ASP B 1 267 ? 39.331 -6.939  68.061  1.00 17.69 ?  267 ASP B CA  1 
ATOM   4157 C  C   . ASP B 1 267 ? 38.411 -6.138  68.971  1.00 19.18 ?  267 ASP B C   1 
ATOM   4158 O  O   . ASP B 1 267 ? 37.916 -5.073  68.588  1.00 21.41 ?  267 ASP B O   1 
ATOM   4159 C  CB  . ASP B 1 267 ? 38.512 -8.075  67.430  1.00 18.18 ?  267 ASP B CB  1 
ATOM   4160 C  CG  . ASP B 1 267 ? 39.207 -8.762  66.283  1.00 19.66 ?  267 ASP B CG  1 
ATOM   4161 O  OD1 . ASP B 1 267 ? 40.265 -8.277  65.824  1.00 17.76 ?  267 ASP B OD1 1 
ATOM   4162 O  OD2 . ASP B 1 267 ? 38.678 -9.802  65.836  1.00 21.17 -1 267 ASP B OD2 1 
ATOM   4163 N  N   . ALA B 1 268 ? 38.143 -6.657  70.170  1.00 17.92 ?  268 ALA B N   1 
ATOM   4164 C  CA  . ALA B 1 268 ? 37.294 -5.931  71.112  1.00 19.58 ?  268 ALA B CA  1 
ATOM   4165 C  C   . ALA B 1 268 ? 37.916 -4.593  71.489  1.00 24.13 ?  268 ALA B C   1 
ATOM   4166 O  O   . ALA B 1 268 ? 37.238 -3.557  71.482  1.00 22.94 ?  268 ALA B O   1 
ATOM   4167 C  CB  . ALA B 1 268 ? 37.043 -6.787  72.357  1.00 21.87 ?  268 ALA B CB  1 
ATOM   4168 N  N   . ALA B 1 269 ? 39.217 -4.589  71.811  1.00 17.26 ?  269 ALA B N   1 
ATOM   4169 C  CA  . ALA B 1 269 ? 39.864 -3.348  72.230  1.00 20.78 ?  269 ALA B CA  1 
ATOM   4170 C  C   . ALA B 1 269 ? 39.890 -2.333  71.100  1.00 25.40 ?  269 ALA B C   1 
ATOM   4171 O  O   . ALA B 1 269 ? 39.732 -1.129  71.331  1.00 23.90 ?  269 ALA B O   1 
ATOM   4172 C  CB  . ALA B 1 269 ? 41.289 -3.625  72.720  1.00 20.11 ?  269 ALA B CB  1 
ATOM   4173 N  N   . ALA B 1 270 ? 40.061 -2.807  69.866  1.00 20.13 ?  270 ALA B N   1 
ATOM   4174 C  CA  . ALA B 1 270 ? 40.164 -1.915  68.721  1.00 21.54 ?  270 ALA B CA  1 
ATOM   4175 C  C   . ALA B 1 270 ? 38.828 -1.290  68.344  1.00 24.48 ?  270 ALA B C   1 
ATOM   4176 O  O   . ALA B 1 270 ? 38.809 -0.275  67.642  1.00 29.82 ?  270 ALA B O   1 
ATOM   4177 C  CB  . ALA B 1 270 ? 40.750 -2.680  67.529  1.00 22.05 ?  270 ALA B CB  1 
ATOM   4178 N  N   . ALA B 1 271 ? 37.710 -1.872  68.782  1.00 23.40 ?  271 ALA B N   1 
ATOM   4179 C  CA  . ALA B 1 271 ? 36.386 -1.347  68.475  1.00 27.68 ?  271 ALA B CA  1 
ATOM   4180 C  C   . ALA B 1 271 ? 35.819 -0.467  69.580  1.00 29.71 ?  271 ALA B C   1 
ATOM   4181 O  O   . ALA B 1 271 ? 34.803 0.198   69.355  1.00 33.50 ?  271 ALA B O   1 
ATOM   4182 C  CB  . ALA B 1 271 ? 35.410 -2.498  68.198  1.00 27.03 ?  271 ALA B CB  1 
ATOM   4183 N  N   . ARG B 1 272 ? 36.459 -0.437  70.747  1.00 29.15 ?  272 ARG B N   1 
ATOM   4184 C  CA  . ARG B 1 272 ? 35.918 0.250   71.910  1.00 32.52 ?  272 ARG B CA  1 
ATOM   4185 C  C   . ARG B 1 272 ? 35.951 1.765   71.712  1.00 34.99 ?  272 ARG B C   1 
ATOM   4186 O  O   . ARG B 1 272 ? 36.823 2.289   71.016  1.00 37.29 ?  272 ARG B O   1 
ATOM   4187 C  CB  . ARG B 1 272 ? 36.716 -0.116  73.159  1.00 36.37 ?  272 ARG B CB  1 
ATOM   4188 C  CG  . ARG B 1 272 ? 36.347 -1.427  73.820  1.00 43.65 ?  272 ARG B CG  1 
ATOM   4189 C  CD  . ARG B 1 272 ? 36.823 -1.442  75.278  1.00 44.51 ?  272 ARG B CD  1 
ATOM   4190 N  NE  . ARG B 1 272 ? 38.138 -0.815  75.444  1.00 52.79 ?  272 ARG B NE  1 
ATOM   4191 C  CZ  . ARG B 1 272 ? 39.244 -1.441  75.847  1.00 47.06 ?  272 ARG B CZ  1 
ATOM   4192 N  NH1 . ARG B 1 272 ? 39.222 -2.737  76.126  1.00 40.11 ?  272 ARG B NH1 1 
ATOM   4193 N  NH2 . ARG B 1 272 ? 40.382 -0.767  75.968  1.00 46.07 ?  272 ARG B NH2 1 
ATOM   4194 N  N   . PRO B 1 273 ? 35.017 2.490   72.331  1.00 39.33 ?  273 PRO B N   1 
ATOM   4195 C  CA  . PRO B 1 273 ? 34.983 3.951   72.165  1.00 40.81 ?  273 PRO B CA  1 
ATOM   4196 C  C   . PRO B 1 273 ? 36.148 4.632   72.867  1.00 45.25 ?  273 PRO B C   1 
ATOM   4197 O  O   . PRO B 1 273 ? 36.474 4.315   74.012  1.00 51.77 ?  273 PRO B O   1 
ATOM   4198 C  CB  . PRO B 1 273 ? 33.647 4.353   72.807  1.00 41.29 ?  273 PRO B CB  1 
ATOM   4199 C  CG  . PRO B 1 273 ? 32.852 3.086   72.915  1.00 45.23 ?  273 PRO B CG  1 
ATOM   4200 C  CD  . PRO B 1 273 ? 33.856 1.988   73.085  1.00 36.81 ?  273 PRO B CD  1 
ATOM   4201 N  N   . LEU B 1 274 ? 36.755 5.597   72.176  1.00 51.04 ?  274 LEU B N   1 
ATOM   4202 C  CA  . LEU B 1 274 ? 37.875 6.377   72.714  1.00 51.13 ?  274 LEU B CA  1 
ATOM   4203 C  C   . LEU B 1 274 ? 37.502 7.086   74.019  1.00 51.97 ?  274 LEU B C   1 
ATOM   4204 O  O   . LEU B 1 274 ? 37.920 6.682   75.107  1.00 53.04 ?  274 LEU B O   1 
ATOM   4205 C  CB  . LEU B 1 274 ? 38.353 7.412   71.684  1.00 45.86 ?  274 LEU B CB  1 
ATOM   4206 C  CG  . LEU B 1 274 ? 38.377 7.016   70.203  1.00 47.60 ?  274 LEU B CG  1 
ATOM   4207 C  CD1 . LEU B 1 274 ? 38.471 8.244   69.303  1.00 42.02 ?  274 LEU B CD1 1 
ATOM   4208 C  CD2 . LEU B 1 274 ? 39.521 6.057   69.908  1.00 51.22 ?  274 LEU B CD2 1 
HETATM 4209 MN MN  . MN  C 2 .   ? 50.737 4.439   55.411  0.79 9.53  ?  401 MN  A MN  1 
HETATM 4210 MN MN  . MN  D 2 .   ? 51.547 4.084   58.681  0.76 13.00 ?  402 MN  A MN  1 
HETATM 4211 MG MG  . MG  E 3 .   ? 42.736 22.162  42.844  0.52 24.41 ?  403 MG  A MG  1 
HETATM 4212 CU CU  . CU  F 4 .   ? 58.980 -18.161 79.458  0.53 16.89 ?  401 CU  B CU  1 
HETATM 4213 CU CU  . CU1 G 5 .   ? 59.072 -21.192 78.162  0.51 21.24 ?  402 CU1 B CU  1 
HETATM 4214 MG MG  . MG  H 3 .   ? 60.104 -19.453 75.922  0.45 15.47 ?  403 MG  B MG  1 
HETATM 4215 O  O   . HOH I 6 .   ? 74.094 6.447   55.310  1.00 43.41 ?  501 HOH A O   1 
HETATM 4216 O  O   . HOH I 6 .   ? 33.119 -4.236  56.724  1.00 44.18 ?  502 HOH A O   1 
HETATM 4217 O  O   . HOH I 6 .   ? 42.256 25.855  44.394  1.00 45.61 ?  503 HOH A O   1 
HETATM 4218 O  O   . HOH I 6 .   ? 30.230 4.465   61.742  1.00 37.75 ?  504 HOH A O   1 
HETATM 4219 O  O   . HOH I 6 .   ? 58.365 5.360   69.028  1.00 25.48 ?  505 HOH A O   1 
HETATM 4220 O  O   . HOH I 6 .   ? 31.450 2.017   45.958  1.00 35.13 ?  506 HOH A O   1 
HETATM 4221 O  O   . HOH I 6 .   ? 53.499 6.441   72.654  1.00 38.67 ?  507 HOH A O   1 
HETATM 4222 O  O   . HOH I 6 .   ? 35.940 18.481  39.627  1.00 41.15 ?  508 HOH A O   1 
HETATM 4223 O  O   . HOH I 6 .   ? 65.810 4.105   61.304  1.00 33.60 ?  509 HOH A O   1 
HETATM 4224 O  O   . HOH I 6 .   ? 40.514 0.619   65.645  1.00 27.35 ?  510 HOH A O   1 
HETATM 4225 O  O   . HOH I 6 .   ? 53.972 -12.025 51.448  1.00 35.97 ?  511 HOH A O   1 
HETATM 4226 O  O   . HOH I 6 .   ? 46.755 3.695   37.221  1.00 39.67 ?  512 HOH A O   1 
HETATM 4227 O  O   . HOH I 6 .   ? 64.433 16.612  59.095  1.00 37.34 ?  513 HOH A O   1 
HETATM 4228 O  O   . HOH I 6 .   ? 30.504 1.475   50.597  1.00 42.92 ?  514 HOH A O   1 
HETATM 4229 O  O   . HOH I 6 .   ? 53.957 10.878  37.118  1.00 28.48 ?  515 HOH A O   1 
HETATM 4230 O  O   . HOH I 6 .   ? 45.936 24.762  54.004  1.00 29.33 ?  516 HOH A O   1 
HETATM 4231 O  O   . HOH I 6 .   ? 39.193 -5.179  52.743  1.00 27.26 ?  517 HOH A O   1 
HETATM 4232 O  O   . HOH I 6 .   ? 68.763 13.341  45.183  1.00 36.18 ?  518 HOH A O   1 
HETATM 4233 O  O   . HOH I 6 .   ? 41.068 24.125  35.274  1.00 39.29 ?  519 HOH A O   1 
HETATM 4234 O  O   . HOH I 6 .   ? 47.555 2.636   59.518  1.00 21.66 ?  520 HOH A O   1 
HETATM 4235 O  O   . HOH I 6 .   ? 45.284 4.210   61.632  1.00 29.77 ?  521 HOH A O   1 
HETATM 4236 O  O   . HOH I 6 .   ? 47.435 9.448   79.475  1.00 66.16 ?  522 HOH A O   1 
HETATM 4237 O  O   . HOH I 6 .   ? 43.890 -12.142 47.531  1.00 34.48 ?  523 HOH A O   1 
HETATM 4238 O  O   . HOH I 6 .   ? 56.687 27.385  52.557  1.00 23.89 ?  524 HOH A O   1 
HETATM 4239 O  O   . HOH I 6 .   ? 61.679 4.793   69.796  1.00 33.10 ?  525 HOH A O   1 
HETATM 4240 O  O   . HOH I 6 .   ? 49.954 5.724   66.315  1.00 25.14 ?  526 HOH A O   1 
HETATM 4241 O  O   . HOH I 6 .   ? 52.284 23.343  39.309  1.00 34.43 ?  527 HOH A O   1 
HETATM 4242 O  O   . HOH I 6 .   ? 51.827 3.016   56.900  1.00 12.65 ?  528 HOH A O   1 
HETATM 4243 O  O   . HOH I 6 .   ? 63.892 -5.743  58.630  1.00 40.67 ?  529 HOH A O   1 
HETATM 4244 O  O   . HOH I 6 .   ? 52.381 3.986   41.509  1.00 21.85 ?  530 HOH A O   1 
HETATM 4245 O  O   . HOH I 6 .   ? 38.653 18.468  34.865  1.00 38.51 ?  531 HOH A O   1 
HETATM 4246 O  O   . HOH I 6 .   ? 56.817 -10.252 49.406  1.00 29.03 ?  532 HOH A O   1 
HETATM 4247 O  O   . HOH I 6 .   ? 43.234 20.039  42.944  1.00 25.98 ?  533 HOH A O   1 
HETATM 4248 O  O   . HOH I 6 .   ? 38.565 27.721  59.348  1.00 28.24 ?  534 HOH A O   1 
HETATM 4249 O  O   . HOH I 6 .   ? 66.645 10.431  43.994  1.00 26.05 ?  535 HOH A O   1 
HETATM 4250 O  O   . HOH I 6 .   ? 62.826 15.227  50.000  1.00 16.33 ?  536 HOH A O   1 
HETATM 4251 O  O   . HOH I 6 .   ? 66.590 15.618  49.166  1.00 26.75 ?  537 HOH A O   1 
HETATM 4252 O  O   . HOH I 6 .   ? 55.833 -3.839  52.900  1.00 18.86 ?  538 HOH A O   1 
HETATM 4253 O  O   . HOH I 6 .   ? 27.271 10.287  46.562  1.00 35.99 ?  539 HOH A O   1 
HETATM 4254 O  O   . HOH I 6 .   ? 63.947 19.277  44.354  1.00 32.52 ?  540 HOH A O   1 
HETATM 4255 O  O   . HOH I 6 .   ? 42.420 25.121  51.235  1.00 25.22 ?  541 HOH A O   1 
HETATM 4256 O  O   . HOH I 6 .   ? 45.462 21.225  40.300  1.00 33.78 ?  542 HOH A O   1 
HETATM 4257 O  O   . HOH I 6 .   ? 47.160 -1.381  51.593  1.00 19.43 ?  543 HOH A O   1 
HETATM 4258 O  O   . HOH I 6 .   ? 39.354 -3.389  44.607  1.00 23.25 ?  544 HOH A O   1 
HETATM 4259 O  O   . HOH I 6 .   ? 35.012 18.392  65.098  1.00 24.84 ?  545 HOH A O   1 
HETATM 4260 O  O   . HOH I 6 .   ? 29.630 5.883   63.593  1.00 37.57 ?  546 HOH A O   1 
HETATM 4261 O  O   . HOH I 6 .   ? 58.527 12.905  70.200  1.00 31.52 ?  547 HOH A O   1 
HETATM 4262 O  O   . HOH I 6 .   ? 38.552 20.454  40.236  1.00 26.06 ?  548 HOH A O   1 
HETATM 4263 O  O   . HOH I 6 .   ? 63.047 8.055   41.033  1.00 32.25 ?  549 HOH A O   1 
HETATM 4264 O  O   . HOH I 6 .   ? 53.917 1.693   35.943  1.00 30.39 ?  550 HOH A O   1 
HETATM 4265 O  O   . HOH I 6 .   ? 37.415 -4.915  45.932  1.00 28.51 ?  551 HOH A O   1 
HETATM 4266 O  O   . HOH I 6 .   ? 36.321 -2.147  42.405  1.00 39.66 ?  552 HOH A O   1 
HETATM 4267 O  O   . HOH I 6 .   ? 29.801 7.398   53.398  1.00 25.41 ?  553 HOH A O   1 
HETATM 4268 O  O   . HOH I 6 .   ? 52.355 17.680  32.712  1.00 31.71 ?  554 HOH A O   1 
HETATM 4269 O  O   . HOH I 6 .   ? 25.529 16.395  51.777  1.00 33.66 ?  555 HOH A O   1 
HETATM 4270 O  O   . HOH I 6 .   ? 28.731 12.663  60.704  1.00 34.00 ?  556 HOH A O   1 
HETATM 4271 O  O   . HOH I 6 .   ? 66.338 11.009  54.916  1.00 27.17 ?  557 HOH A O   1 
HETATM 4272 O  O   . HOH I 6 .   ? 58.516 10.303  74.114  1.00 33.55 ?  558 HOH A O   1 
HETATM 4273 O  O   . HOH I 6 .   ? 58.893 25.559  43.852  1.00 38.33 ?  559 HOH A O   1 
HETATM 4274 O  O   . HOH I 6 .   ? 36.956 -6.845  56.115  1.00 33.41 ?  560 HOH A O   1 
HETATM 4275 O  O   . HOH I 6 .   ? 42.282 21.549  40.990  1.00 28.41 ?  561 HOH A O   1 
HETATM 4276 O  O   . HOH I 6 .   ? 35.099 -5.902  58.013  1.00 31.43 ?  562 HOH A O   1 
HETATM 4277 O  O   . HOH I 6 .   ? 45.330 -11.406 42.370  1.00 33.06 ?  563 HOH A O   1 
HETATM 4278 O  O   . HOH I 6 .   ? 52.712 21.162  63.479  1.00 18.56 ?  564 HOH A O   1 
HETATM 4279 O  O   . HOH I 6 .   ? 45.712 6.867   50.330  1.00 17.58 ?  565 HOH A O   1 
HETATM 4280 O  O   . HOH I 6 .   ? 44.107 -1.287  33.489  1.00 35.77 ?  566 HOH A O   1 
HETATM 4281 O  O   . HOH I 6 .   ? 60.394 0.200   58.929  1.00 31.35 ?  567 HOH A O   1 
HETATM 4282 O  O   . HOH I 6 .   ? 54.578 15.073  68.894  1.00 21.95 ?  568 HOH A O   1 
HETATM 4283 O  O   . HOH I 6 .   ? 58.932 10.012  68.062  1.00 26.25 ?  569 HOH A O   1 
HETATM 4284 O  O   . HOH I 6 .   ? 58.261 -9.299  47.402  1.00 28.69 ?  570 HOH A O   1 
HETATM 4285 O  O   . HOH I 6 .   ? 57.415 1.509   56.650  1.00 26.62 ?  571 HOH A O   1 
HETATM 4286 O  O   . HOH I 6 .   ? 42.025 -7.072  38.428  1.00 42.82 ?  572 HOH A O   1 
HETATM 4287 O  O   . HOH I 6 .   ? 40.210 4.400   56.224  1.00 16.40 ?  573 HOH A O   1 
HETATM 4288 O  O   . HOH I 6 .   ? 45.432 6.697   64.920  1.00 19.42 ?  574 HOH A O   1 
HETATM 4289 O  O   . HOH I 6 .   ? 65.173 13.257  60.243  1.00 27.82 ?  575 HOH A O   1 
HETATM 4290 O  O   . HOH I 6 .   ? 46.810 -3.068  39.901  1.00 23.74 ?  576 HOH A O   1 
HETATM 4291 O  O   . HOH I 6 .   ? 47.689 -7.356  51.740  1.00 17.32 ?  577 HOH A O   1 
HETATM 4292 O  O   . HOH I 6 .   ? 61.181 21.319  48.676  1.00 26.17 ?  578 HOH A O   1 
HETATM 4293 O  O   . HOH I 6 .   ? 36.249 7.054   38.196  1.00 33.05 ?  579 HOH A O   1 
HETATM 4294 O  O   . HOH I 6 .   ? 39.893 9.166   57.370  1.00 15.32 ?  580 HOH A O   1 
HETATM 4295 O  O   . HOH I 6 .   ? 24.982 19.204  54.820  1.00 38.35 ?  581 HOH A O   1 
HETATM 4296 O  O   . HOH I 6 .   ? 38.477 -11.355 56.123  1.00 36.60 ?  582 HOH A O   1 
HETATM 4297 O  O   . HOH I 6 .   ? 38.045 0.755   36.685  1.00 26.59 ?  583 HOH A O   1 
HETATM 4298 O  O   . HOH I 6 .   ? 55.585 2.511   40.162  1.00 18.88 ?  584 HOH A O   1 
HETATM 4299 O  O   . HOH I 6 .   ? 68.863 -0.258  52.406  1.00 37.59 ?  585 HOH A O   1 
HETATM 4300 O  O   . HOH I 6 .   ? 36.038 12.970  69.628  1.00 32.92 ?  586 HOH A O   1 
HETATM 4301 O  O   . HOH I 6 .   ? 49.556 -12.343 40.914  1.00 37.02 ?  587 HOH A O   1 
HETATM 4302 O  O   . HOH I 6 .   ? 39.349 -2.488  55.435  1.00 20.83 ?  588 HOH A O   1 
HETATM 4303 O  O   . HOH I 6 .   ? 62.342 21.732  57.683  1.00 31.48 ?  589 HOH A O   1 
HETATM 4304 O  O   . HOH I 6 .   ? 31.739 1.086   54.026  1.00 25.39 ?  590 HOH A O   1 
HETATM 4305 O  O   . HOH I 6 .   ? 62.248 9.496   62.412  1.00 23.76 ?  591 HOH A O   1 
HETATM 4306 O  O   . HOH I 6 .   ? 49.470 -3.262  38.659  1.00 26.90 ?  592 HOH A O   1 
HETATM 4307 O  O   . HOH I 6 .   ? 49.838 -6.645  50.187  1.00 15.44 ?  593 HOH A O   1 
HETATM 4308 O  O   . HOH I 6 .   ? 60.458 12.113  38.071  1.00 23.39 ?  594 HOH A O   1 
HETATM 4309 O  O   . HOH I 6 .   ? 30.750 -5.603  48.347  1.00 38.46 ?  595 HOH A O   1 
HETATM 4310 O  O   . HOH I 6 .   ? 50.985 9.280   35.292  1.00 46.08 ?  596 HOH A O   1 
HETATM 4311 O  O   . HOH I 6 .   ? 55.828 5.334   67.762  1.00 22.96 ?  597 HOH A O   1 
HETATM 4312 O  O   . HOH I 6 .   ? 46.242 -14.756 58.651  1.00 30.49 ?  598 HOH A O   1 
HETATM 4313 O  O   . HOH I 6 .   ? 60.049 12.804  67.607  1.00 24.52 ?  599 HOH A O   1 
HETATM 4314 O  O   . HOH I 6 .   ? 60.151 7.687   70.904  1.00 47.24 ?  600 HOH A O   1 
HETATM 4315 O  O   . HOH I 6 .   ? 36.112 20.092  59.092  1.00 19.75 ?  601 HOH A O   1 
HETATM 4316 O  O   . HOH I 6 .   ? 64.988 17.925  48.241  1.00 24.63 ?  602 HOH A O   1 
HETATM 4317 O  O   . HOH I 6 .   ? 49.895 27.019  61.964  1.00 23.68 ?  603 HOH A O   1 
HETATM 4318 O  O   . HOH I 6 .   ? 47.691 1.255   34.854  1.00 37.99 ?  604 HOH A O   1 
HETATM 4319 O  O   . HOH I 6 .   ? 40.176 4.195   65.252  1.00 39.69 ?  605 HOH A O   1 
HETATM 4320 O  O   . HOH I 6 .   ? 39.844 -3.696  42.024  1.00 26.86 ?  606 HOH A O   1 
HETATM 4321 O  O   . HOH I 6 .   ? 26.688 10.429  49.180  1.00 33.48 ?  607 HOH A O   1 
HETATM 4322 O  O   . HOH I 6 .   ? 41.695 17.316  66.146  1.00 28.89 ?  608 HOH A O   1 
HETATM 4323 O  O   . HOH I 6 .   ? 47.033 23.765  66.261  1.00 25.83 ?  609 HOH A O   1 
HETATM 4324 O  O   . HOH I 6 .   ? 40.494 28.609  57.373  1.00 30.54 ?  610 HOH A O   1 
HETATM 4325 O  O   . HOH I 6 .   ? 43.679 -5.654  46.871  1.00 18.33 ?  611 HOH A O   1 
HETATM 4326 O  O   . HOH I 6 .   ? 61.209 -9.426  50.453  1.00 41.76 ?  612 HOH A O   1 
HETATM 4327 O  O   . HOH I 6 .   ? 32.376 16.193  45.771  1.00 30.20 ?  613 HOH A O   1 
HETATM 4328 O  O   . HOH I 6 .   ? 35.881 -2.022  56.355  1.00 18.90 ?  614 HOH A O   1 
HETATM 4329 O  O   . HOH I 6 .   ? 59.242 22.661  44.316  1.00 26.80 ?  615 HOH A O   1 
HETATM 4330 O  O   . HOH I 6 .   ? 58.889 16.404  39.197  1.00 25.66 ?  616 HOH A O   1 
HETATM 4331 O  O   . HOH I 6 .   ? 49.225 0.781   60.463  1.00 21.87 ?  617 HOH A O   1 
HETATM 4332 O  O   . HOH I 6 .   ? 39.947 7.054   55.535  1.00 16.84 ?  618 HOH A O   1 
HETATM 4333 O  O   . HOH I 6 .   ? 67.344 4.530   47.557  1.00 31.27 ?  619 HOH A O   1 
HETATM 4334 O  O   . HOH I 6 .   ? 30.895 24.071  57.154  1.00 16.61 ?  620 HOH A O   1 
HETATM 4335 O  O   . HOH I 6 .   ? 45.350 30.427  53.167  1.00 38.23 ?  621 HOH A O   1 
HETATM 4336 O  O   . HOH I 6 .   ? 58.045 15.197  41.473  1.00 22.97 ?  622 HOH A O   1 
HETATM 4337 O  O   . HOH I 6 .   ? 44.610 -2.372  55.953  1.00 26.49 ?  623 HOH A O   1 
HETATM 4338 O  O   . HOH I 6 .   ? 31.197 12.937  64.941  1.00 29.50 ?  624 HOH A O   1 
HETATM 4339 O  O   . HOH I 6 .   ? 61.287 -3.142  56.292  1.00 44.78 ?  625 HOH A O   1 
HETATM 4340 O  O   . HOH I 6 .   ? 61.805 21.546  63.985  1.00 21.00 ?  626 HOH A O   1 
HETATM 4341 O  O   . HOH I 6 .   ? 48.625 -0.258  57.655  1.00 30.74 ?  627 HOH A O   1 
HETATM 4342 O  O   . HOH I 6 .   ? 39.394 -10.104 61.340  1.00 46.76 ?  628 HOH A O   1 
HETATM 4343 O  O   . HOH I 6 .   ? 33.840 27.757  54.562  1.00 30.04 ?  629 HOH A O   1 
HETATM 4344 O  O   . HOH I 6 .   ? 61.106 -6.509  60.844  1.00 35.70 ?  630 HOH A O   1 
HETATM 4345 O  O   . HOH I 6 .   ? 52.135 19.672  78.648  1.00 27.84 ?  631 HOH A O   1 
HETATM 4346 O  O   . HOH I 6 .   ? 55.733 16.754  42.204  1.00 19.41 ?  632 HOH A O   1 
HETATM 4347 O  O   . HOH I 6 .   ? 59.860 8.692   39.677  1.00 35.36 ?  633 HOH A O   1 
HETATM 4348 O  O   . HOH I 6 .   ? 62.577 -4.141  61.565  1.00 39.32 ?  634 HOH A O   1 
HETATM 4349 O  O   . HOH I 6 .   ? 29.717 16.380  60.231  1.00 28.67 ?  635 HOH A O   1 
HETATM 4350 O  O   . HOH I 6 .   ? 43.232 22.881  44.715  1.00 27.59 ?  636 HOH A O   1 
HETATM 4351 O  O   . HOH I 6 .   ? 37.610 3.140   35.243  1.00 35.93 ?  637 HOH A O   1 
HETATM 4352 O  O   . HOH I 6 .   ? 64.216 20.810  53.639  1.00 27.73 ?  638 HOH A O   1 
HETATM 4353 O  O   . HOH I 6 .   ? 42.678 4.058   63.043  1.00 22.57 ?  639 HOH A O   1 
HETATM 4354 O  O   . HOH I 6 .   ? 33.909 14.407  43.397  1.00 35.46 ?  640 HOH A O   1 
HETATM 4355 O  O   . HOH I 6 .   ? 49.298 -14.210 48.782  1.00 30.04 ?  641 HOH A O   1 
HETATM 4356 O  O   . HOH I 6 .   ? 66.013 14.922  61.883  1.00 36.44 ?  642 HOH A O   1 
HETATM 4357 O  O   . HOH I 6 .   ? 26.728 22.238  57.411  1.00 31.06 ?  643 HOH A O   1 
HETATM 4358 O  O   . HOH I 6 .   ? 60.088 23.198  47.004  1.00 29.33 ?  644 HOH A O   1 
HETATM 4359 O  O   . HOH I 6 .   ? 29.143 8.074   43.941  1.00 24.93 ?  645 HOH A O   1 
HETATM 4360 O  O   . HOH I 6 .   ? 57.907 -5.095  56.174  1.00 27.75 ?  646 HOH A O   1 
HETATM 4361 O  O   . HOH I 6 .   ? 62.646 7.206   65.591  1.00 31.10 ?  647 HOH A O   1 
HETATM 4362 O  O   . HOH I 6 .   ? 50.713 12.714  81.680  1.00 37.83 ?  648 HOH A O   1 
HETATM 4363 O  O   . HOH I 6 .   ? 53.039 26.387  40.778  1.00 42.31 ?  649 HOH A O   1 
HETATM 4364 O  O   . HOH I 6 .   ? 32.216 5.029   40.624  1.00 45.18 ?  650 HOH A O   1 
HETATM 4365 O  O   . HOH I 6 .   ? 40.888 10.832  64.669  1.00 24.53 ?  651 HOH A O   1 
HETATM 4366 O  O   . HOH I 6 .   ? 61.053 7.074   68.226  1.00 43.72 ?  652 HOH A O   1 
HETATM 4367 O  O   . HOH I 6 .   ? 54.435 7.463   35.292  1.00 40.21 ?  653 HOH A O   1 
HETATM 4368 O  O   . HOH I 6 .   ? 48.896 -13.268 59.169  1.00 36.31 ?  654 HOH A O   1 
HETATM 4369 O  O   . HOH I 6 .   ? 47.128 -5.988  37.007  1.00 31.27 ?  655 HOH A O   1 
HETATM 4370 O  O   . HOH I 6 .   ? 50.045 2.265   54.924  1.00 16.94 ?  656 HOH A O   1 
HETATM 4371 O  O   . HOH I 6 .   ? 29.603 1.562   69.676  1.00 35.47 ?  657 HOH A O   1 
HETATM 4372 O  O   . HOH I 6 .   ? 61.730 -4.169  41.777  1.00 45.04 ?  658 HOH A O   1 
HETATM 4373 O  O   . HOH I 6 .   ? 44.662 25.878  45.346  1.00 36.26 ?  659 HOH A O   1 
HETATM 4374 O  O   . HOH I 6 .   ? 40.281 -13.266 53.554  1.00 38.75 ?  660 HOH A O   1 
HETATM 4375 O  O   . HOH I 6 .   ? 35.865 21.153  64.125  1.00 23.97 ?  661 HOH A O   1 
HETATM 4376 O  O   . HOH I 6 .   ? 51.965 -11.879 54.534  1.00 39.16 ?  662 HOH A O   1 
HETATM 4377 O  O   . HOH I 6 .   ? 65.857 14.254  56.426  1.00 24.68 ?  663 HOH A O   1 
HETATM 4378 O  O   . HOH I 6 .   ? 65.673 20.032  49.811  1.00 35.93 ?  664 HOH A O   1 
HETATM 4379 O  O   . HOH I 6 .   ? 29.521 20.029  61.001  1.00 32.07 ?  665 HOH A O   1 
HETATM 4380 O  O   . HOH I 6 .   ? 45.830 28.782  55.173  1.00 38.29 ?  666 HOH A O   1 
HETATM 4381 O  O   . HOH I 6 .   ? 33.414 21.929  65.490  1.00 31.07 ?  667 HOH A O   1 
HETATM 4382 O  O   . HOH I 6 .   ? 54.852 21.193  67.285  1.00 21.26 ?  668 HOH A O   1 
HETATM 4383 O  O   . HOH I 6 .   ? 42.437 24.069  42.190  1.00 30.19 ?  669 HOH A O   1 
HETATM 4384 O  O   . HOH I 6 .   ? 53.533 -4.781  38.960  1.00 41.46 ?  670 HOH A O   1 
HETATM 4385 O  O   . HOH I 6 .   ? 51.897 -8.696  40.382  1.00 40.25 ?  671 HOH A O   1 
HETATM 4386 O  O   . HOH I 6 .   ? 35.137 -4.699  53.379  1.00 36.21 ?  672 HOH A O   1 
HETATM 4387 O  O   . HOH I 6 .   ? 43.676 20.872  67.532  1.00 33.18 ?  673 HOH A O   1 
HETATM 4388 O  O   . HOH I 6 .   ? 40.566 -10.761 48.852  1.00 41.82 ?  674 HOH A O   1 
HETATM 4389 O  O   . HOH I 6 .   ? 53.604 24.935  64.976  1.00 20.16 ?  675 HOH A O   1 
HETATM 4390 O  O   . HOH I 6 .   ? 33.162 2.164   41.002  1.00 31.35 ?  676 HOH A O   1 
HETATM 4391 O  O   . HOH I 6 .   ? 30.777 3.005   57.872  1.00 40.80 ?  677 HOH A O   1 
HETATM 4392 O  O   . HOH I 6 .   ? 46.322 17.829  70.348  1.00 20.59 ?  678 HOH A O   1 
HETATM 4393 O  O   . HOH I 6 .   ? 31.592 23.493  50.365  1.00 39.10 ?  679 HOH A O   1 
HETATM 4394 O  O   . HOH I 6 .   ? 59.572 -3.708  40.284  1.00 28.26 ?  680 HOH A O   1 
HETATM 4395 O  O   . HOH I 6 .   ? 51.847 30.725  54.770  1.00 39.53 ?  681 HOH A O   1 
HETATM 4396 O  O   . HOH I 6 .   ? 34.945 13.070  41.087  1.00 36.71 ?  682 HOH A O   1 
HETATM 4397 O  O   . HOH I 6 .   ? 72.553 2.214   50.654  1.00 44.12 ?  683 HOH A O   1 
HETATM 4398 O  O   . HOH I 6 .   ? 63.440 -9.121  52.663  1.00 44.33 ?  684 HOH A O   1 
HETATM 4399 O  O   . HOH I 6 .   ? 29.172 5.794   57.043  1.00 33.78 ?  685 HOH A O   1 
HETATM 4400 O  O   . HOH I 6 .   ? 58.606 -4.070  35.737  1.00 48.04 ?  686 HOH A O   1 
HETATM 4401 O  O   . HOH I 6 .   ? 54.314 28.700  60.449  1.00 40.40 ?  687 HOH A O   1 
HETATM 4402 O  O   . HOH I 6 .   ? 59.527 -11.497 52.724  1.00 43.50 ?  688 HOH A O   1 
HETATM 4403 O  O   . HOH I 6 .   ? 21.267 16.166  51.334  1.00 36.93 ?  689 HOH A O   1 
HETATM 4404 O  O   . HOH I 6 .   ? 37.591 -4.788  54.578  1.00 32.35 ?  690 HOH A O   1 
HETATM 4405 O  O   . HOH I 6 .   ? 40.889 27.757  61.272  1.00 33.59 ?  691 HOH A O   1 
HETATM 4406 O  O   . HOH I 6 .   ? 44.641 -7.108  36.851  1.00 38.79 ?  692 HOH A O   1 
HETATM 4407 O  O   . HOH I 6 .   ? 44.303 25.938  52.982  1.00 28.98 ?  693 HOH A O   1 
HETATM 4408 O  O   . HOH I 6 .   ? 50.314 16.557  31.436  1.00 38.08 ?  694 HOH A O   1 
HETATM 4409 O  O   . HOH I 6 .   ? 69.874 1.612   50.525  1.00 40.54 ?  695 HOH A O   1 
HETATM 4410 O  O   . HOH I 6 .   ? 59.504 31.051  62.604  1.00 30.83 ?  696 HOH A O   1 
HETATM 4411 O  O   . HOH I 6 .   ? 43.584 25.201  40.025  1.00 41.29 ?  697 HOH A O   1 
HETATM 4412 O  O   . HOH I 6 .   ? 67.661 13.596  58.097  1.00 58.76 ?  698 HOH A O   1 
HETATM 4413 O  O   . HOH I 6 .   ? 64.552 10.763  61.219  1.00 31.91 ?  699 HOH A O   1 
HETATM 4414 O  O   . HOH I 6 .   ? 48.250 25.041  42.995  1.00 44.71 ?  700 HOH A O   1 
HETATM 4415 O  O   . HOH I 6 .   ? 37.064 -4.955  41.679  1.00 37.40 ?  701 HOH A O   1 
HETATM 4416 O  O   . HOH I 6 .   ? 25.156 14.943  53.708  1.00 38.68 ?  702 HOH A O   1 
HETATM 4417 O  O   . HOH I 6 .   ? 33.272 -6.953  52.477  1.00 35.09 ?  703 HOH A O   1 
HETATM 4418 O  O   . HOH I 6 .   ? 31.945 14.839  63.631  1.00 37.84 ?  704 HOH A O   1 
HETATM 4419 O  O   . HOH I 6 .   ? 52.605 1.983   33.945  1.00 45.90 ?  705 HOH A O   1 
HETATM 4420 O  O   . HOH I 6 .   ? 43.854 -10.512 39.876  1.00 43.36 ?  706 HOH A O   1 
HETATM 4421 O  O   . HOH I 6 .   ? 55.509 30.957  47.311  1.00 45.78 ?  707 HOH A O   1 
HETATM 4422 O  O   . HOH I 6 .   ? 64.089 22.815  55.630  1.00 37.15 ?  708 HOH A O   1 
HETATM 4423 O  O   . HOH I 6 .   ? 51.173 12.267  74.943  1.00 50.69 ?  709 HOH A O   1 
HETATM 4424 O  O   . HOH I 6 .   ? 56.874 31.043  50.157  1.00 39.04 ?  710 HOH A O   1 
HETATM 4425 O  O   . HOH I 6 .   ? 43.870 4.586   70.074  1.00 48.64 ?  711 HOH A O   1 
HETATM 4426 O  O   . HOH I 6 .   ? 46.045 24.589  43.249  1.00 40.11 ?  712 HOH A O   1 
HETATM 4427 O  O   . HOH I 6 .   ? 33.903 -3.224  54.808  1.00 27.39 ?  713 HOH A O   1 
HETATM 4428 O  O   . HOH I 6 .   ? 32.300 17.374  64.750  1.00 33.19 ?  714 HOH A O   1 
HETATM 4429 O  O   . HOH I 6 .   ? 53.844 27.545  51.746  1.00 31.87 ?  715 HOH A O   1 
HETATM 4430 O  O   . HOH I 6 .   ? 44.872 22.376  42.444  1.00 33.07 ?  716 HOH A O   1 
HETATM 4431 O  O   . HOH I 6 .   ? 63.403 21.037  61.948  1.00 42.17 ?  717 HOH A O   1 
HETATM 4432 O  O   . HOH I 6 .   ? 35.497 9.504   37.018  1.00 41.32 ?  718 HOH A O   1 
HETATM 4433 O  O   . HOH I 6 .   ? 51.116 22.575  67.841  1.00 31.07 ?  719 HOH A O   1 
HETATM 4434 O  O   . HOH I 6 .   ? 60.211 11.631  71.976  1.00 37.39 ?  720 HOH A O   1 
HETATM 4435 O  O   . HOH I 6 .   ? 55.422 -6.200  38.636  1.00 50.91 ?  721 HOH A O   1 
HETATM 4436 O  O   . HOH I 6 .   ? 62.325 -11.280 51.674  1.00 48.57 ?  722 HOH A O   1 
HETATM 4437 O  O   . HOH I 6 .   ? 53.101 5.299   70.673  1.00 35.70 ?  723 HOH A O   1 
HETATM 4438 O  O   . HOH I 6 .   ? 43.732 18.878  69.856  1.00 36.73 ?  724 HOH A O   1 
HETATM 4439 O  O   . HOH I 6 .   ? 50.109 21.511  78.020  1.00 44.62 ?  725 HOH A O   1 
HETATM 4440 O  O   . HOH I 6 .   ? 39.307 1.430   32.424  1.00 45.90 ?  726 HOH A O   1 
HETATM 4441 O  O   . HOH I 6 .   ? 50.958 20.368  69.581  1.00 27.99 ?  727 HOH A O   1 
HETATM 4442 O  O   . HOH I 6 .   ? 51.556 0.181   57.091  1.00 30.99 ?  728 HOH A O   1 
HETATM 4443 O  O   . HOH I 6 .   ? 50.512 -6.314  39.200  1.00 38.25 ?  729 HOH A O   1 
HETATM 4444 O  O   . HOH I 6 .   ? 52.877 22.452  65.936  1.00 19.93 ?  730 HOH A O   1 
HETATM 4445 O  O   . HOH I 6 .   ? 50.488 29.244  60.586  1.00 37.56 ?  731 HOH A O   1 
HETATM 4446 O  O   . HOH I 6 .   ? 43.783 11.053  68.827  1.00 43.06 ?  732 HOH A O   1 
HETATM 4447 O  O   . HOH I 6 .   ? 63.356 -6.386  62.107  1.00 31.10 ?  733 HOH A O   1 
HETATM 4448 O  O   . HOH I 6 .   ? 29.944 14.643  61.920  1.00 40.01 ?  734 HOH A O   1 
HETATM 4449 O  O   . HOH I 6 .   ? 66.944 5.641   44.829  1.00 36.98 ?  735 HOH A O   1 
HETATM 4450 O  O   . HOH I 6 .   ? 38.637 31.585  53.678  1.00 43.37 ?  736 HOH A O   1 
HETATM 4451 O  O   . HOH I 6 .   ? 35.501 -7.806  39.038  1.00 62.06 ?  737 HOH A O   1 
HETATM 4452 O  O   . HOH I 6 .   ? 53.196 19.771  70.421  1.00 32.87 ?  738 HOH A O   1 
HETATM 4453 O  O   . HOH I 6 .   ? 59.973 10.519  76.583  1.00 36.23 ?  739 HOH A O   1 
HETATM 4454 O  O   . HOH I 6 .   ? 41.889 9.104   63.023  1.00 21.04 ?  740 HOH A O   1 
HETATM 4455 O  O   . HOH I 6 .   ? 39.537 30.754  56.104  1.00 37.54 ?  741 HOH A O   1 
HETATM 4456 O  O   . HOH I 6 .   ? 42.214 30.396  63.967  1.00 44.85 ?  742 HOH A O   1 
HETATM 4457 O  O   . HOH I 6 .   ? 49.365 31.933  54.704  1.00 44.88 ?  743 HOH A O   1 
HETATM 4458 O  O   . HOH I 6 .   ? 41.703 17.129  69.023  1.00 37.82 ?  744 HOH A O   1 
HETATM 4459 O  O   . HOH I 6 .   ? 59.061 -10.839 45.245  1.00 44.98 ?  745 HOH A O   1 
HETATM 4460 O  O   . HOH I 6 .   ? 44.857 23.083  67.887  1.00 29.54 ?  746 HOH A O   1 
HETATM 4461 O  O   . HOH I 6 .   ? 71.108 -0.864  54.178  1.00 42.09 ?  747 HOH A O   1 
HETATM 4462 O  O   . HOH I 6 .   ? 31.545 -1.653  53.926  1.00 27.50 ?  748 HOH A O   1 
HETATM 4463 O  O   . HOH I 6 .   ? 62.818 9.657   65.137  1.00 35.02 ?  749 HOH A O   1 
HETATM 4464 O  O   . HOH I 6 .   ? 67.643 -2.667  48.769  1.00 41.50 ?  750 HOH A O   1 
HETATM 4465 O  O   . HOH I 6 .   ? 66.635 18.808  46.542  1.00 39.41 ?  751 HOH A O   1 
HETATM 4466 O  O   . HOH I 6 .   ? 68.165 17.540  44.572  1.00 42.76 ?  752 HOH A O   1 
HETATM 4467 O  O   . HOH I 6 .   ? 29.944 1.837   55.884  1.00 36.66 ?  753 HOH A O   1 
HETATM 4468 O  O   . HOH I 6 .   ? 42.743 6.651   64.084  1.00 22.63 ?  754 HOH A O   1 
HETATM 4469 O  O   . HOH I 6 .   ? 62.968 29.330  48.218  1.00 38.23 ?  755 HOH A O   1 
HETATM 4470 O  O   . HOH I 6 .   ? 60.931 10.136  36.411  1.00 35.79 ?  756 HOH A O   1 
HETATM 4471 O  O   . HOH I 6 .   ? 46.609 25.026  40.608  1.00 54.49 ?  757 HOH A O   1 
HETATM 4472 O  O   . HOH I 6 .   ? 39.420 -0.629  34.551  1.00 41.02 ?  758 HOH A O   1 
HETATM 4473 O  O   . HOH I 6 .   ? 65.826 21.351  61.058  1.00 44.47 ?  759 HOH A O   1 
HETATM 4474 O  O   . HOH I 6 .   ? 28.425 -0.064  57.036  1.00 39.85 ?  760 HOH A O   1 
HETATM 4475 O  O   . HOH I 6 .   ? 41.018 7.295   66.612  1.00 47.38 ?  761 HOH A O   1 
HETATM 4476 O  O   . HOH I 6 .   ? 53.664 30.380  52.667  1.00 29.57 ?  762 HOH A O   1 
HETATM 4477 O  O   . HOH I 6 .   ? 62.497 12.198  67.254  1.00 34.98 ?  763 HOH A O   1 
HETATM 4478 O  O   . HOH I 6 .   ? 48.629 19.855  71.700  1.00 34.91 ?  764 HOH A O   1 
HETATM 4479 O  O   . HOH I 6 .   ? 48.188 32.614  52.590  1.00 48.96 ?  765 HOH A O   1 
HETATM 4480 O  O   . HOH I 6 .   ? 41.552 10.112  67.344  1.00 35.89 ?  766 HOH A O   1 
HETATM 4481 O  O   . HOH I 6 .   ? 42.479 12.734  69.867  1.00 44.12 ?  767 HOH A O   1 
HETATM 4482 O  O   . HOH I 6 .   ? 49.652 -16.097 42.688  1.00 52.94 ?  768 HOH A O   1 
HETATM 4483 O  O   . HOH I 6 .   ? 41.915 15.118  70.258  1.00 38.21 ?  769 HOH A O   1 
HETATM 4484 O  O   . HOH J 6 .   ? 37.896 -4.216  74.990  1.00 35.95 ?  501 HOH B O   1 
HETATM 4485 O  O   . HOH J 6 .   ? 46.275 -13.354 101.177 1.00 37.33 ?  502 HOH B O   1 
HETATM 4486 O  O   . HOH J 6 .   ? 61.738 -18.419 71.673  0.62 28.79 ?  503 HOH B O   1 
HETATM 4487 O  O   . HOH J 6 .   ? 64.057 -21.732 67.784  1.00 41.24 ?  504 HOH B O   1 
HETATM 4488 O  O   . HOH J 6 .   ? 44.372 -9.431  57.319  1.00 30.18 ?  505 HOH B O   1 
HETATM 4489 O  O   . HOH J 6 .   ? 52.048 -27.459 92.904  0.86 36.71 ?  506 HOH B O   1 
HETATM 4490 O  O   . HOH J 6 .   ? 70.744 -3.983  73.973  1.00 30.48 ?  507 HOH B O   1 
HETATM 4491 O  O   . HOH J 6 .   ? 42.296 -2.822  88.995  1.00 43.39 ?  508 HOH B O   1 
HETATM 4492 O  O   . HOH J 6 .   ? 61.281 -26.991 100.028 1.00 33.55 ?  509 HOH B O   1 
HETATM 4493 O  O   . HOH J 6 .   ? 71.709 -11.897 67.258  1.00 36.70 ?  510 HOH B O   1 
HETATM 4494 O  O   . HOH J 6 .   ? 67.834 -24.337 85.262  1.00 45.47 ?  511 HOH B O   1 
HETATM 4495 O  O   . HOH J 6 .   ? 57.584 2.349   87.554  1.00 46.25 ?  512 HOH B O   1 
HETATM 4496 O  O   . HOH J 6 .   ? 77.134 -10.805 77.504  1.00 33.89 ?  513 HOH B O   1 
HETATM 4497 O  O   . HOH J 6 .   ? 60.629 -24.499 83.951  1.00 29.44 ?  514 HOH B O   1 
HETATM 4498 O  O   . HOH J 6 .   ? 55.227 -4.313  92.613  1.00 28.32 ?  515 HOH B O   1 
HETATM 4499 O  O   . HOH J 6 .   ? 45.713 -27.318 88.349  1.00 35.76 ?  516 HOH B O   1 
HETATM 4500 O  O   . HOH J 6 .   ? 53.337 3.935   77.209  1.00 35.94 ?  517 HOH B O   1 
HETATM 4501 O  O   . HOH J 6 .   ? 69.474 -4.111  76.263  1.00 24.84 ?  518 HOH B O   1 
HETATM 4502 O  O   . HOH J 6 .   ? 62.542 -14.894 52.949  1.00 36.87 ?  519 HOH B O   1 
HETATM 4503 O  O   . HOH J 6 .   ? 33.614 -15.151 79.400  1.00 28.37 ?  520 HOH B O   1 
HETATM 4504 O  O   . HOH J 6 .   ? 61.528 -8.164  88.726  1.00 21.69 ?  521 HOH B O   1 
HETATM 4505 O  O   . HOH J 6 .   ? 65.639 -25.947 87.150  1.00 43.12 ?  522 HOH B O   1 
HETATM 4506 O  O   . HOH J 6 .   ? 60.090 -2.822  87.147  1.00 31.26 ?  523 HOH B O   1 
HETATM 4507 O  O   . HOH J 6 .   ? 39.650 -11.006 76.449  1.00 28.15 ?  524 HOH B O   1 
HETATM 4508 O  O   . HOH J 6 .   ? 45.061 -13.873 96.855  1.00 35.71 ?  525 HOH B O   1 
HETATM 4509 O  O   . HOH J 6 .   ? 53.590 -2.567  57.315  1.00 33.65 ?  526 HOH B O   1 
HETATM 4510 O  O   . HOH J 6 .   ? 41.981 -33.064 78.483  1.00 28.92 ?  527 HOH B O   1 
HETATM 4511 O  O   . HOH J 6 .   ? 73.842 -1.649  81.634  1.00 44.13 ?  528 HOH B O   1 
HETATM 4512 O  O   . HOH J 6 .   ? 70.318 -2.569  78.284  1.00 31.96 ?  529 HOH B O   1 
HETATM 4513 O  O   . HOH J 6 .   ? 69.221 -9.908  63.351  1.00 29.50 ?  530 HOH B O   1 
HETATM 4514 O  O   . HOH J 6 .   ? 40.355 -28.424 83.261  1.00 26.86 ?  531 HOH B O   1 
HETATM 4515 O  O   . HOH J 6 .   ? 67.195 -20.430 84.863  1.00 26.81 ?  532 HOH B O   1 
HETATM 4516 O  O   . HOH J 6 .   ? 52.181 2.542   71.291  1.00 34.11 ?  533 HOH B O   1 
HETATM 4517 O  O   . HOH J 6 .   ? 63.908 -17.296 97.874  1.00 38.13 ?  534 HOH B O   1 
HETATM 4518 O  O   . HOH J 6 .   ? 64.470 -18.468 75.440  1.00 41.69 ?  535 HOH B O   1 
HETATM 4519 O  O   . HOH J 6 .   ? 39.740 -17.958 63.899  1.00 19.08 ?  536 HOH B O   1 
HETATM 4520 O  O   . HOH J 6 .   ? 57.900 -3.715  63.370  1.00 30.92 ?  537 HOH B O   1 
HETATM 4521 O  O   . HOH J 6 .   ? 51.277 -25.398 93.207  1.00 26.78 ?  538 HOH B O   1 
HETATM 4522 O  O   . HOH J 6 .   ? 36.892 -11.126 67.254  1.00 29.52 ?  539 HOH B O   1 
HETATM 4523 O  O   . HOH J 6 .   ? 48.901 -24.048 63.807  1.00 29.12 ?  540 HOH B O   1 
HETATM 4524 O  O   . HOH J 6 .   ? 55.714 -12.279 55.684  1.00 35.97 ?  541 HOH B O   1 
HETATM 4525 O  O   . HOH J 6 .   ? 46.557 -1.357  80.765  1.00 30.05 ?  542 HOH B O   1 
HETATM 4526 O  O   . HOH J 6 .   ? 46.628 -1.860  57.690  1.00 24.74 ?  543 HOH B O   1 
HETATM 4527 O  O   . HOH J 6 .   ? 65.313 -14.972 56.499  1.00 30.62 ?  544 HOH B O   1 
HETATM 4528 O  O   . HOH J 6 .   ? 73.590 -18.587 90.079  1.00 36.25 ?  545 HOH B O   1 
HETATM 4529 O  O   . HOH J 6 .   ? 58.009 -12.843 57.197  1.00 22.26 ?  546 HOH B O   1 
HETATM 4530 O  O   . HOH J 6 .   ? 55.956 -22.992 69.857  1.00 29.30 ?  547 HOH B O   1 
HETATM 4531 O  O   . HOH J 6 .   ? 74.102 -19.425 87.376  1.00 33.98 ?  548 HOH B O   1 
HETATM 4532 O  O   . HOH J 6 .   ? 52.663 -22.191 61.565  1.00 34.60 ?  549 HOH B O   1 
HETATM 4533 O  O   . HOH J 6 .   ? 52.854 -29.807 84.464  1.00 29.62 ?  550 HOH B O   1 
HETATM 4534 O  O   . HOH J 6 .   ? 37.714 -12.011 86.084  1.00 28.51 ?  551 HOH B O   1 
HETATM 4535 O  O   . HOH J 6 .   ? 65.989 -11.179 58.497  1.00 31.98 ?  552 HOH B O   1 
HETATM 4536 O  O   . HOH J 6 .   ? 32.815 1.979   69.640  1.00 27.50 ?  553 HOH B O   1 
HETATM 4537 O  O   . HOH J 6 .   ? 45.513 -0.643  83.425  1.00 35.63 ?  554 HOH B O   1 
HETATM 4538 O  O   . HOH J 6 .   ? 38.916 -22.271 69.945  1.00 23.60 ?  555 HOH B O   1 
HETATM 4539 O  O   . HOH J 6 .   ? 56.963 -25.876 72.691  1.00 35.11 ?  556 HOH B O   1 
HETATM 4540 O  O   . HOH J 6 .   ? 63.322 -27.220 77.366  0.92 45.91 ?  557 HOH B O   1 
HETATM 4541 O  O   . HOH J 6 .   ? 63.408 -20.319 63.830  1.00 24.31 ?  558 HOH B O   1 
HETATM 4542 O  O   . HOH J 6 .   ? 36.125 -15.905 85.882  1.00 32.74 ?  559 HOH B O   1 
HETATM 4543 O  O   . HOH J 6 .   ? 66.888 -16.591 74.772  1.00 31.56 ?  560 HOH B O   1 
HETATM 4544 O  O   . HOH J 6 .   ? 54.139 -33.404 70.953  1.00 38.02 ?  561 HOH B O   1 
HETATM 4545 O  O   . HOH J 6 .   ? 48.399 -19.365 92.468  1.00 17.86 ?  562 HOH B O   1 
HETATM 4546 O  O   . HOH J 6 .   ? 70.208 -10.498 71.372  1.00 25.68 ?  563 HOH B O   1 
HETATM 4547 O  O   . HOH J 6 .   ? 68.560 -0.336  75.233  1.00 31.70 ?  564 HOH B O   1 
HETATM 4548 O  O   . HOH J 6 .   ? 61.642 -21.294 98.348  1.00 35.62 ?  565 HOH B O   1 
HETATM 4549 O  O   . HOH J 6 .   ? 41.171 -9.678  63.691  1.00 43.58 ?  566 HOH B O   1 
HETATM 4550 O  O   . HOH J 6 .   ? 52.467 -6.118  96.280  1.00 38.14 ?  567 HOH B O   1 
HETATM 4551 O  O   . HOH J 6 .   ? 49.007 -29.123 88.420  1.00 31.91 ?  568 HOH B O   1 
HETATM 4552 O  O   . HOH J 6 .   ? 36.070 -10.142 69.881  1.00 27.29 ?  569 HOH B O   1 
HETATM 4553 O  O   . HOH J 6 .   ? 55.086 -21.700 101.913 1.00 30.83 ?  570 HOH B O   1 
HETATM 4554 O  O   . HOH J 6 .   ? 45.562 -20.283 63.878  1.00 24.31 ?  571 HOH B O   1 
HETATM 4555 O  O   . HOH J 6 .   ? 41.192 -4.662  62.215  1.00 18.04 ?  572 HOH B O   1 
HETATM 4556 O  O   . HOH J 6 .   ? 48.781 -8.072  59.630  1.00 31.06 ?  573 HOH B O   1 
HETATM 4557 O  O   . HOH J 6 .   ? 53.098 5.248   68.064  1.00 30.08 ?  574 HOH B O   1 
HETATM 4558 O  O   . HOH J 6 .   ? 50.544 -26.299 67.787  1.00 26.06 ?  575 HOH B O   1 
HETATM 4559 O  O   . HOH J 6 .   ? 60.925 -19.988 74.157  1.00 22.93 ?  576 HOH B O   1 
HETATM 4560 O  O   . HOH J 6 .   ? 46.446 4.121   65.160  1.00 29.15 ?  577 HOH B O   1 
HETATM 4561 O  O   . HOH J 6 .   ? 45.614 -8.919  96.809  1.00 34.59 ?  578 HOH B O   1 
HETATM 4562 O  O   . HOH J 6 .   ? 40.482 -5.246  77.364  1.00 30.83 ?  579 HOH B O   1 
HETATM 4563 O  O   . HOH J 6 .   ? 43.234 -10.968 63.231  1.00 30.14 ?  580 HOH B O   1 
HETATM 4564 O  O   . HOH J 6 .   ? 53.568 -17.650 99.117  1.00 30.38 ?  581 HOH B O   1 
HETATM 4565 O  O   . HOH J 6 .   ? 43.505 0.965   68.905  1.00 31.88 ?  582 HOH B O   1 
HETATM 4566 O  O   . HOH J 6 .   ? 36.207 -19.285 75.169  1.00 24.63 ?  583 HOH B O   1 
HETATM 4567 O  O   . HOH J 6 .   ? 44.596 -10.313 65.481  1.00 20.94 ?  584 HOH B O   1 
HETATM 4568 O  O   . HOH J 6 .   ? 51.048 -25.026 96.037  1.00 21.24 ?  585 HOH B O   1 
HETATM 4569 O  O   . HOH J 6 .   ? 52.481 -14.588 99.336  1.00 43.06 ?  586 HOH B O   1 
HETATM 4570 O  O   . HOH J 6 .   ? 60.283 4.483   77.936  1.00 33.27 ?  587 HOH B O   1 
HETATM 4571 O  O   . HOH J 6 .   ? 57.896 -10.957 78.182  1.00 21.28 ?  588 HOH B O   1 
HETATM 4572 O  O   . HOH J 6 .   ? 65.814 -13.975 78.371  1.00 25.20 ?  589 HOH B O   1 
HETATM 4573 O  O   . HOH J 6 .   ? 51.678 -32.145 78.748  1.00 31.55 ?  590 HOH B O   1 
HETATM 4574 O  O   . HOH J 6 .   ? 69.349 -4.735  85.197  1.00 26.37 ?  591 HOH B O   1 
HETATM 4575 O  O   . HOH J 6 .   ? 51.815 -9.083  58.798  1.00 23.94 ?  592 HOH B O   1 
HETATM 4576 O  O   . HOH J 6 .   ? 70.949 -8.894  78.410  1.00 19.23 ?  593 HOH B O   1 
HETATM 4577 O  O   . HOH J 6 .   ? 42.512 -11.373 93.117  1.00 35.30 ?  594 HOH B O   1 
HETATM 4578 O  O   . HOH J 6 .   ? 77.737 -12.446 71.424  1.00 35.09 ?  595 HOH B O   1 
HETATM 4579 O  O   . HOH J 6 .   ? 66.579 3.552   79.846  1.00 37.45 ?  596 HOH B O   1 
HETATM 4580 O  O   . HOH J 6 .   ? 44.779 0.819   80.881  1.00 40.77 ?  597 HOH B O   1 
HETATM 4581 O  O   . HOH J 6 .   ? 55.109 0.205   56.274  1.00 37.54 ?  598 HOH B O   1 
HETATM 4582 O  O   . HOH J 6 .   ? 64.254 -4.719  93.138  1.00 34.02 ?  599 HOH B O   1 
HETATM 4583 O  O   . HOH J 6 .   ? 71.562 -15.390 78.570  1.00 22.21 ?  600 HOH B O   1 
HETATM 4584 O  O   . HOH J 6 .   ? 70.579 -12.160 64.626  1.00 28.82 ?  601 HOH B O   1 
HETATM 4585 O  O   . HOH J 6 .   ? 64.732 -2.384  65.937  1.00 32.55 ?  602 HOH B O   1 
HETATM 4586 O  O   . HOH J 6 .   ? 60.088 -20.051 79.287  1.00 27.39 ?  603 HOH B O   1 
HETATM 4587 O  O   . HOH J 6 .   ? 79.200 -13.459 86.961  1.00 32.88 ?  604 HOH B O   1 
HETATM 4588 O  O   . HOH J 6 .   ? 65.980 -21.178 95.884  1.00 32.67 ?  605 HOH B O   1 
HETATM 4589 O  O   . HOH J 6 .   ? 50.965 -14.083 58.032  1.00 21.96 ?  606 HOH B O   1 
HETATM 4590 O  O   . HOH J 6 .   ? 45.049 -26.901 76.643  1.00 23.25 ?  607 HOH B O   1 
HETATM 4591 O  O   . HOH J 6 .   ? 50.121 -20.257 59.699  1.00 30.44 ?  608 HOH B O   1 
HETATM 4592 O  O   . HOH J 6 .   ? 42.532 -16.161 91.912  1.00 35.20 ?  609 HOH B O   1 
HETATM 4593 O  O   . HOH J 6 .   ? 66.967 -10.789 66.477  1.00 16.91 ?  610 HOH B O   1 
HETATM 4594 O  O   . HOH J 6 .   ? 64.416 -6.116  64.576  1.00 24.02 ?  611 HOH B O   1 
HETATM 4595 O  O   . HOH J 6 .   ? 55.526 -12.775 69.446  1.00 16.11 ?  612 HOH B O   1 
HETATM 4596 O  O   . HOH J 6 .   ? 43.026 0.214   66.185  1.00 32.65 ?  613 HOH B O   1 
HETATM 4597 O  O   . HOH J 6 .   ? 39.008 -11.488 63.604  1.00 36.88 ?  614 HOH B O   1 
HETATM 4598 O  O   . HOH J 6 .   ? 46.764 3.602   78.060  1.00 31.12 ?  615 HOH B O   1 
HETATM 4599 O  O   . HOH J 6 .   ? 45.754 -14.326 61.386  1.00 22.19 ?  616 HOH B O   1 
HETATM 4600 O  O   . HOH J 6 .   ? 39.886 -6.554  75.040  1.00 27.79 ?  617 HOH B O   1 
HETATM 4601 O  O   . HOH J 6 .   ? 34.451 -3.847  71.858  1.00 29.37 ?  618 HOH B O   1 
HETATM 4602 O  O   . HOH J 6 .   ? 56.880 0.134   62.485  1.00 20.05 ?  619 HOH B O   1 
HETATM 4603 O  O   . HOH J 6 .   ? 40.128 -7.178  63.212  1.00 32.62 ?  620 HOH B O   1 
HETATM 4604 O  O   . HOH J 6 .   ? 62.854 -9.124  92.152  1.00 23.19 ?  621 HOH B O   1 
HETATM 4605 O  O   . HOH J 6 .   ? 41.146 -24.142 87.535  1.00 24.48 ?  622 HOH B O   1 
HETATM 4606 O  O   . HOH J 6 .   ? 36.187 -20.450 90.657  1.00 37.45 ?  623 HOH B O   1 
HETATM 4607 O  O   . HOH J 6 .   ? 57.716 -11.543 70.452  1.00 18.34 ?  624 HOH B O   1 
HETATM 4608 O  O   . HOH J 6 .   ? 55.331 -11.270 96.469  1.00 33.61 ?  625 HOH B O   1 
HETATM 4609 O  O   . HOH J 6 .   ? 67.481 -12.269 69.722  1.00 20.91 ?  626 HOH B O   1 
HETATM 4610 O  O   . HOH J 6 .   ? 68.578 2.534   86.622  1.00 44.66 ?  627 HOH B O   1 
HETATM 4611 O  O   . HOH J 6 .   ? 69.479 -5.389  88.011  1.00 33.84 ?  628 HOH B O   1 
HETATM 4612 O  O   . HOH J 6 .   ? 44.456 -15.889 95.198  1.00 34.68 ?  629 HOH B O   1 
HETATM 4613 O  O   . HOH J 6 .   ? 35.484 -11.738 76.101  1.00 35.84 ?  630 HOH B O   1 
HETATM 4614 O  O   . HOH J 6 .   ? 38.325 -25.527 88.211  1.00 40.94 ?  631 HOH B O   1 
HETATM 4615 O  O   . HOH J 6 .   ? 48.919 -31.663 72.843  1.00 35.32 ?  632 HOH B O   1 
HETATM 4616 O  O   . HOH J 6 .   ? 54.356 -24.413 68.096  1.00 24.61 ?  633 HOH B O   1 
HETATM 4617 O  O   . HOH J 6 .   ? 41.402 -28.773 70.528  1.00 30.56 ?  634 HOH B O   1 
HETATM 4618 O  O   . HOH J 6 .   ? 45.137 2.565   69.458  1.00 39.41 ?  635 HOH B O   1 
HETATM 4619 O  O   . HOH J 6 .   ? 58.583 -0.712  89.192  1.00 44.18 ?  636 HOH B O   1 
HETATM 4620 O  O   . HOH J 6 .   ? 55.981 -21.254 61.639  1.00 31.19 ?  637 HOH B O   1 
HETATM 4621 O  O   . HOH J 6 .   ? 70.927 -15.314 81.205  1.00 20.72 ?  638 HOH B O   1 
HETATM 4622 O  O   . HOH J 6 .   ? 63.879 -26.615 95.415  1.00 39.53 ?  639 HOH B O   1 
HETATM 4623 O  O   . HOH J 6 .   ? 35.636 -19.658 72.518  1.00 42.71 ?  640 HOH B O   1 
HETATM 4624 O  O   . HOH J 6 .   ? 48.920 -7.904  95.748  1.00 34.66 ?  641 HOH B O   1 
HETATM 4625 O  O   . HOH J 6 .   ? 48.541 -8.443  91.240  1.00 19.62 ?  642 HOH B O   1 
HETATM 4626 O  O   . HOH J 6 .   ? 48.894 -32.280 80.380  1.00 26.82 ?  643 HOH B O   1 
HETATM 4627 O  O   . HOH J 6 .   ? 68.221 -12.184 95.526  1.00 37.44 ?  644 HOH B O   1 
HETATM 4628 O  O   . HOH J 6 .   ? 49.394 1.755   69.594  1.00 28.62 ?  645 HOH B O   1 
HETATM 4629 O  O   . HOH J 6 .   ? 78.612 -15.718 81.466  1.00 27.71 ?  646 HOH B O   1 
HETATM 4630 O  O   . HOH J 6 .   ? 61.147 -17.794 79.325  1.00 28.87 ?  647 HOH B O   1 
HETATM 4631 O  O   . HOH J 6 .   ? 60.257 -12.693 70.226  1.00 16.29 ?  648 HOH B O   1 
HETATM 4632 O  O   . HOH J 6 .   ? 51.664 -28.394 98.994  1.00 22.86 ?  649 HOH B O   1 
HETATM 4633 O  O   . HOH J 6 .   ? 45.216 -27.647 74.150  1.00 20.27 ?  650 HOH B O   1 
HETATM 4634 O  O   . HOH J 6 .   ? 66.217 -22.623 82.885  1.00 34.04 ?  651 HOH B O   1 
HETATM 4635 O  O   . HOH J 6 .   ? 49.991 -9.248  93.463  1.00 23.10 ?  652 HOH B O   1 
HETATM 4636 O  O   . HOH J 6 .   ? 59.018 -20.950 97.163  1.00 25.76 ?  653 HOH B O   1 
HETATM 4637 O  O   . HOH J 6 .   ? 58.914 -31.447 93.385  1.00 36.42 ?  654 HOH B O   1 
HETATM 4638 O  O   . HOH J 6 .   ? 57.207 -30.580 95.086  1.00 36.58 ?  655 HOH B O   1 
HETATM 4639 O  O   . HOH J 6 .   ? 75.477 -8.471  73.528  1.00 34.78 ?  656 HOH B O   1 
HETATM 4640 O  O   . HOH J 6 .   ? 57.573 -9.546  96.527  1.00 31.15 ?  657 HOH B O   1 
HETATM 4641 O  O   . HOH J 6 .   ? 38.645 -27.111 70.702  1.00 27.64 ?  658 HOH B O   1 
HETATM 4642 O  O   . HOH J 6 .   ? 56.913 6.409   83.129  1.00 39.03 ?  659 HOH B O   1 
HETATM 4643 O  O   . HOH J 6 .   ? 65.428 -31.167 90.060  1.00 43.88 ?  660 HOH B O   1 
HETATM 4644 O  O   . HOH J 6 .   ? 56.245 -32.999 78.021  1.00 37.68 ?  661 HOH B O   1 
HETATM 4645 O  O   . HOH J 6 .   ? 48.871 3.352   67.058  1.00 23.50 ?  662 HOH B O   1 
HETATM 4646 O  O   . HOH J 6 .   ? 62.256 -18.691 54.747  1.00 17.80 ?  663 HOH B O   1 
HETATM 4647 O  O   . HOH J 6 .   ? 40.988 -14.266 91.919  1.00 33.81 ?  664 HOH B O   1 
HETATM 4648 O  O   . HOH J 6 .   ? 41.960 -16.424 95.268  1.00 48.61 ?  665 HOH B O   1 
HETATM 4649 O  O   . HOH J 6 .   ? 58.838 -4.061  94.657  1.00 34.92 ?  666 HOH B O   1 
HETATM 4650 O  O   . HOH J 6 .   ? 50.800 -4.465  95.467  1.00 39.71 ?  667 HOH B O   1 
HETATM 4651 O  O   . HOH J 6 .   ? 51.598 -11.501 57.111  1.00 27.16 ?  668 HOH B O   1 
HETATM 4652 O  O   . HOH J 6 .   ? 48.919 -26.491 91.368  1.00 30.13 ?  669 HOH B O   1 
HETATM 4653 O  O   . HOH J 6 .   ? 45.833 -18.584 61.576  1.00 26.30 ?  670 HOH B O   1 
HETATM 4654 O  O   . HOH J 6 .   ? 35.184 -6.148  67.636  1.00 40.79 ?  671 HOH B O   1 
HETATM 4655 O  O   . HOH J 6 .   ? 61.763 -19.759 77.169  1.00 28.80 ?  672 HOH B O   1 
HETATM 4656 O  O   . HOH J 6 .   ? 56.216 -13.878 97.959  1.00 54.12 ?  673 HOH B O   1 
HETATM 4657 O  O   . HOH J 6 .   ? 47.070 0.338   93.531  1.00 42.43 ?  674 HOH B O   1 
HETATM 4658 O  O   . HOH J 6 .   ? 73.909 -21.893 86.746  1.00 42.99 ?  675 HOH B O   1 
HETATM 4659 O  O   . HOH J 6 .   ? 64.375 3.352   73.895  1.00 37.68 ?  676 HOH B O   1 
HETATM 4660 O  O   . HOH J 6 .   ? 78.243 -16.482 73.341  1.00 43.96 ?  677 HOH B O   1 
HETATM 4661 O  O   . HOH J 6 .   ? 43.071 -11.760 57.986  1.00 37.79 ?  678 HOH B O   1 
HETATM 4662 O  O   . HOH J 6 .   ? 38.797 -24.614 75.891  1.00 21.66 ?  679 HOH B O   1 
HETATM 4663 O  O   . HOH J 6 .   ? 43.396 2.285   64.860  1.00 33.97 ?  680 HOH B O   1 
HETATM 4664 O  O   . HOH J 6 .   ? 32.760 -18.661 84.672  1.00 36.51 ?  681 HOH B O   1 
HETATM 4665 O  O   . HOH J 6 .   ? 43.639 -9.813  95.795  1.00 34.58 ?  682 HOH B O   1 
HETATM 4666 O  O   . HOH J 6 .   ? 69.937 -8.207  67.514  1.00 34.69 ?  683 HOH B O   1 
HETATM 4667 O  O   . HOH J 6 .   ? 46.197 -30.261 74.120  1.00 31.63 ?  684 HOH B O   1 
HETATM 4668 O  O   . HOH J 6 .   ? 37.758 -19.504 70.163  1.00 37.98 ?  685 HOH B O   1 
HETATM 4669 O  O   . HOH J 6 .   ? 72.566 -7.019  66.953  1.00 36.70 ?  686 HOH B O   1 
HETATM 4670 O  O   . HOH J 6 .   ? 71.389 -0.898  75.767  1.00 41.68 ?  687 HOH B O   1 
HETATM 4671 O  O   . HOH J 6 .   ? 52.579 -38.172 73.015  1.00 55.58 ?  688 HOH B O   1 
HETATM 4672 O  O   . HOH J 6 .   ? 58.363 2.399   59.419  1.00 15.92 ?  689 HOH B O   1 
HETATM 4673 O  O   . HOH J 6 .   ? 55.812 -3.354  55.620  1.00 26.60 ?  690 HOH B O   1 
HETATM 4674 O  O   . HOH J 6 .   ? 69.758 -10.941 68.761  1.00 30.34 ?  691 HOH B O   1 
HETATM 4675 O  O   . HOH J 6 .   ? 65.315 -7.420  60.323  1.00 36.28 ?  692 HOH B O   1 
HETATM 4676 O  O   . HOH J 6 .   ? 51.261 -30.181 86.870  1.00 34.22 ?  693 HOH B O   1 
HETATM 4677 O  O   . HOH J 6 .   ? 64.748 -0.335  67.735  1.00 43.87 ?  694 HOH B O   1 
HETATM 4678 O  O   . HOH J 6 .   ? 48.318 -23.511 95.114  1.00 35.99 ?  695 HOH B O   1 
HETATM 4679 O  O   . HOH J 6 .   ? 57.019 -31.819 99.130  1.00 38.66 ?  696 HOH B O   1 
HETATM 4680 O  O   . HOH J 6 .   ? 78.313 -18.301 81.239  1.00 40.29 ?  697 HOH B O   1 
HETATM 4681 O  O   . HOH J 6 .   ? 37.398 -8.068  63.010  1.00 38.01 ?  698 HOH B O   1 
HETATM 4682 O  O   . HOH J 6 .   ? 46.112 -31.800 76.203  1.00 35.90 ?  699 HOH B O   1 
HETATM 4683 O  O   . HOH J 6 .   ? 56.785 -23.371 63.020  1.00 37.78 ?  700 HOH B O   1 
HETATM 4684 O  O   . HOH J 6 .   ? 54.930 -30.355 93.693  1.00 35.85 ?  701 HOH B O   1 
HETATM 4685 O  O   . HOH J 6 .   ? 35.744 -17.282 64.181  1.00 28.93 ?  702 HOH B O   1 
HETATM 4686 O  O   . HOH J 6 .   ? 34.838 -7.992  69.385  1.00 39.26 ?  703 HOH B O   1 
HETATM 4687 O  O   . HOH J 6 .   ? 38.180 -15.818 62.991  1.00 28.92 ?  704 HOH B O   1 
HETATM 4688 O  O   . HOH J 6 .   ? 33.506 -15.273 89.145  1.00 42.90 ?  705 HOH B O   1 
HETATM 4689 O  O   . HOH J 6 .   ? 38.714 -8.884  75.588  1.00 29.51 ?  706 HOH B O   1 
HETATM 4690 O  O   . HOH J 6 .   ? 67.539 -14.219 57.439  1.00 38.28 ?  707 HOH B O   1 
HETATM 4691 O  O   . HOH J 6 .   ? 55.199 -30.909 101.033 1.00 36.70 ?  708 HOH B O   1 
HETATM 4692 O  O   . HOH J 6 .   ? 77.559 -20.125 86.941  1.00 49.35 ?  709 HOH B O   1 
HETATM 4693 O  O   . HOH J 6 .   ? 32.559 -1.437  72.031  1.00 40.07 ?  710 HOH B O   1 
HETATM 4694 O  O   . HOH J 6 .   ? 35.130 -4.306  74.628  1.00 36.06 ?  711 HOH B O   1 
HETATM 4695 O  O   . HOH J 6 .   ? 53.539 -17.245 101.858 1.00 50.67 ?  712 HOH B O   1 
HETATM 4696 O  O   . HOH J 6 .   ? 52.477 -32.067 83.404  1.00 38.46 ?  713 HOH B O   1 
HETATM 4697 O  O   . HOH J 6 .   ? 67.111 -6.986  61.734  1.00 43.32 ?  714 HOH B O   1 
HETATM 4698 O  O   . HOH J 6 .   ? 56.897 -16.052 97.728  1.00 48.56 ?  715 HOH B O   1 
HETATM 4699 O  O   . HOH J 6 .   ? 52.481 -29.429 62.333  1.00 42.15 ?  716 HOH B O   1 
HETATM 4700 O  O   . HOH J 6 .   ? 33.270 -12.202 78.034  1.00 33.78 ?  717 HOH B O   1 
HETATM 4701 O  O   . HOH J 6 .   ? 58.004 -19.022 98.644  1.00 31.07 ?  718 HOH B O   1 
HETATM 4702 O  O   . HOH J 6 .   ? 35.143 -7.704  65.745  1.00 41.86 ?  719 HOH B O   1 
HETATM 4703 O  O   . HOH J 6 .   ? 55.983 -4.507  96.645  1.00 42.03 ?  720 HOH B O   1 
HETATM 4704 O  O   . HOH J 6 .   ? 47.242 2.637   93.077  1.00 40.64 ?  721 HOH B O   1 
HETATM 4705 O  O   . HOH J 6 .   ? 54.026 -3.837  94.990  1.00 34.02 ?  722 HOH B O   1 
HETATM 4706 O  O   . HOH J 6 .   ? 68.260 -8.468  65.672  1.00 21.97 ?  723 HOH B O   1 
HETATM 4707 O  O   . HOH J 6 .   ? 52.732 -7.454  98.780  1.00 43.51 ?  724 HOH B O   1 
HETATM 4708 O  O   . HOH J 6 .   ? 79.702 -15.202 84.024  1.00 39.29 ?  725 HOH B O   1 
HETATM 4709 O  O   . HOH J 6 .   ? 34.311 -10.630 65.531  1.00 41.52 ?  726 HOH B O   1 
HETATM 4710 O  O   . HOH J 6 .   ? 49.282 6.652   91.317  1.00 47.88 ?  727 HOH B O   1 
HETATM 4711 O  O   . HOH J 6 .   ? 66.553 -27.373 94.146  1.00 53.50 ?  728 HOH B O   1 
HETATM 4712 O  O   . HOH J 6 .   ? 63.795 -29.410 96.251  1.00 39.72 ?  729 HOH B O   1 
HETATM 4713 O  O   . HOH J 6 .   ? 76.983 -6.292  72.488  1.00 38.69 ?  730 HOH B O   1 
HETATM 4714 O  O   . HOH J 6 .   ? 66.996 -6.395  64.450  1.00 31.58 ?  731 HOH B O   1 
HETATM 4715 O  O   . HOH J 6 .   ? 43.183 -23.732 89.650  1.00 38.00 ?  732 HOH B O   1 
HETATM 4716 O  O   . HOH J 6 .   ? 78.114 -21.808 71.667  1.00 39.39 ?  733 HOH B O   1 
# 
