data_9B2L
# 
_entry.id   9B2L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9B2L         pdb_00009b2l 10.2210/pdb9b2l/pdb 
WWPDB D_1000279061 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9B2L 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'wt GcL'                                  6n9i unspecified 
PDB 'wt GcL bound to substrate C4-HSL'        6N9Q unspecified 
PDB 'wt GcL bound to substrate 3-oxo-C12-HSL' 6N9R unspecified 
PDB 'wt GcL bound to substrate C6-HSL'        9AYT unspecified 
PDB 'Gcl mutant G156P'                        9B2I unspecified 
PDB 'GcL I237M mutant'                        9B2J unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mhelias@umn.edu 
_pdbx_contact_author.name_first         Mikael 
_pdbx_contact_author.name_last          Elias 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0406-7539 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Corbella, M.'     1 ? 
'Bravo, J.A.'      2 ? 
'Demkiv, A.O.'     3 ? 
'Calixto, A.R.'    4 ? 
'Sompiyachoke, K.' 5 ? 
'Bergonzi, C.'     6 ? 
'Kamerlin, S.C.L.' 7 ? 
'Elias, M.'        8 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            4 
_citation.language                  ? 
_citation.page_first                3519 
_citation.page_last                 3536 
_citation.title                     
'Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.4c00404 
_citation.pdbx_database_id_PubMed   39328773 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Corbella, M.'     1 0000-0001-9209-868X 
primary 'Bravo, J.'        2 ?                   
primary 'Demkiv, A.O.'     3 ?                   
primary 'Calixto, A.R.'    4 0000-0002-1123-0413 
primary 'Sompiyachoke, K.' 5 0000-0003-0627-8305 
primary 'Bergonzi, C.'     6 ?                   
primary 'Brownless, A.R.'  7 ?                   
primary 'Elias, M.H.'      8 0000-0003-0406-7539 
primary 'Kamerlin, S.C.L.' 9 0000-0002-3190-1173 
# 
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 'quorum-quenching N-acyl-homoserine lactonase' 31724.941 2   3.1.1.81 D122N ? 'D122N mutation' 
2 non-polymer syn 'SULFATE ION'                                  96.063    4   ?        ?     ? ?                
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                        106.120   2   ?        ?     ? ?                
4 non-polymer syn 'TRIETHYLENE GLYCOL'                           150.173   1   ?        ?     ? ?                
5 non-polymer syn 1,2-ETHANEDIOL                                 62.068    2   ?        ?     ? ?                
6 non-polymer syn 'FE (III) ION'                                 55.845    2   ?        ?     ? ?                
7 non-polymer syn 'COBALT (II) ION'                              58.933    2   ?        ?     ? ?                
8 water       nat water                                          18.015    110 ?        ?     ? ?                
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'GcL lactonase' 
# 
_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       
;RPKLYVMDNGRMRMDKNWMIAMHNPATIHNPNAQTEFVEFPIYTVLIDHPEGKILFDTSCNPNSMGPQGRWAESTQQMFP
WTATEECYLHNRLEQLKVRPEDIRYVVASHLHLNHAGCLEMFTNATIIVHEDEFNGALQCYARNQKEGAYIWADIDAWIK
NNLQWRTVKRHEDNILLAEGVKVLNFGSGHAWGMLGLHVELPETGGIILASDAIYTAESYGPPIKPPGIIYDSLGYMNTV
ERIRRIAQETKSQVWFGHDAEQFKKFRKSTEGYYE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RPKLYVMDNGRMRMDKNWMIAMHNPATIHNPNAQTEFVEFPIYTVLIDHPEGKILFDTSCNPNSMGPQGRWAESTQQMFP
WTATEECYLHNRLEQLKVRPEDIRYVVASHLHLNHAGCLEMFTNATIIVHEDEFNGALQCYARNQKEGAYIWADIDAWIK
NNLQWRTVKRHEDNILLAEGVKVLNFGSGHAWGMLGLHVELPETGGIILASDAIYTAESYGPPIKPPGIIYDSLGYMNTV
ERIRRIAQETKSQVWFGHDAEQFKKFRKSTEGYYE
;
_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 'SULFATE ION'           SO4 
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 'TRIETHYLENE GLYCOL'    PGE 
5 1,2-ETHANEDIOL          EDO 
6 'FE (III) ION'          FE  
7 'COBALT (II) ION'       CO  
8 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   PRO n 
1 3   LYS n 
1 4   LEU n 
1 5   TYR n 
1 6   VAL n 
1 7   MET n 
1 8   ASP n 
1 9   ASN n 
1 10  GLY n 
1 11  ARG n 
1 12  MET n 
1 13  ARG n 
1 14  MET n 
1 15  ASP n 
1 16  LYS n 
1 17  ASN n 
1 18  TRP n 
1 19  MET n 
1 20  ILE n 
1 21  ALA n 
1 22  MET n 
1 23  HIS n 
1 24  ASN n 
1 25  PRO n 
1 26  ALA n 
1 27  THR n 
1 28  ILE n 
1 29  HIS n 
1 30  ASN n 
1 31  PRO n 
1 32  ASN n 
1 33  ALA n 
1 34  GLN n 
1 35  THR n 
1 36  GLU n 
1 37  PHE n 
1 38  VAL n 
1 39  GLU n 
1 40  PHE n 
1 41  PRO n 
1 42  ILE n 
1 43  TYR n 
1 44  THR n 
1 45  VAL n 
1 46  LEU n 
1 47  ILE n 
1 48  ASP n 
1 49  HIS n 
1 50  PRO n 
1 51  GLU n 
1 52  GLY n 
1 53  LYS n 
1 54  ILE n 
1 55  LEU n 
1 56  PHE n 
1 57  ASP n 
1 58  THR n 
1 59  SER n 
1 60  CYS n 
1 61  ASN n 
1 62  PRO n 
1 63  ASN n 
1 64  SER n 
1 65  MET n 
1 66  GLY n 
1 67  PRO n 
1 68  GLN n 
1 69  GLY n 
1 70  ARG n 
1 71  TRP n 
1 72  ALA n 
1 73  GLU n 
1 74  SER n 
1 75  THR n 
1 76  GLN n 
1 77  GLN n 
1 78  MET n 
1 79  PHE n 
1 80  PRO n 
1 81  TRP n 
1 82  THR n 
1 83  ALA n 
1 84  THR n 
1 85  GLU n 
1 86  GLU n 
1 87  CYS n 
1 88  TYR n 
1 89  LEU n 
1 90  HIS n 
1 91  ASN n 
1 92  ARG n 
1 93  LEU n 
1 94  GLU n 
1 95  GLN n 
1 96  LEU n 
1 97  LYS n 
1 98  VAL n 
1 99  ARG n 
1 100 PRO n 
1 101 GLU n 
1 102 ASP n 
1 103 ILE n 
1 104 ARG n 
1 105 TYR n 
1 106 VAL n 
1 107 VAL n 
1 108 ALA n 
1 109 SER n 
1 110 HIS n 
1 111 LEU n 
1 112 HIS n 
1 113 LEU n 
1 114 ASN n 
1 115 HIS n 
1 116 ALA n 
1 117 GLY n 
1 118 CYS n 
1 119 LEU n 
1 120 GLU n 
1 121 MET n 
1 122 PHE n 
1 123 THR n 
1 124 ASN n 
1 125 ALA n 
1 126 THR n 
1 127 ILE n 
1 128 ILE n 
1 129 VAL n 
1 130 HIS n 
1 131 GLU n 
1 132 ASP n 
1 133 GLU n 
1 134 PHE n 
1 135 ASN n 
1 136 GLY n 
1 137 ALA n 
1 138 LEU n 
1 139 GLN n 
1 140 CYS n 
1 141 TYR n 
1 142 ALA n 
1 143 ARG n 
1 144 ASN n 
1 145 GLN n 
1 146 LYS n 
1 147 GLU n 
1 148 GLY n 
1 149 ALA n 
1 150 TYR n 
1 151 ILE n 
1 152 TRP n 
1 153 ALA n 
1 154 ASP n 
1 155 ILE n 
1 156 ASP n 
1 157 ALA n 
1 158 TRP n 
1 159 ILE n 
1 160 LYS n 
1 161 ASN n 
1 162 ASN n 
1 163 LEU n 
1 164 GLN n 
1 165 TRP n 
1 166 ARG n 
1 167 THR n 
1 168 VAL n 
1 169 LYS n 
1 170 ARG n 
1 171 HIS n 
1 172 GLU n 
1 173 ASP n 
1 174 ASN n 
1 175 ILE n 
1 176 LEU n 
1 177 LEU n 
1 178 ALA n 
1 179 GLU n 
1 180 GLY n 
1 181 VAL n 
1 182 LYS n 
1 183 VAL n 
1 184 LEU n 
1 185 ASN n 
1 186 PHE n 
1 187 GLY n 
1 188 SER n 
1 189 GLY n 
1 190 HIS n 
1 191 ALA n 
1 192 TRP n 
1 193 GLY n 
1 194 MET n 
1 195 LEU n 
1 196 GLY n 
1 197 LEU n 
1 198 HIS n 
1 199 VAL n 
1 200 GLU n 
1 201 LEU n 
1 202 PRO n 
1 203 GLU n 
1 204 THR n 
1 205 GLY n 
1 206 GLY n 
1 207 ILE n 
1 208 ILE n 
1 209 LEU n 
1 210 ALA n 
1 211 SER n 
1 212 ASP n 
1 213 ALA n 
1 214 ILE n 
1 215 TYR n 
1 216 THR n 
1 217 ALA n 
1 218 GLU n 
1 219 SER n 
1 220 TYR n 
1 221 GLY n 
1 222 PRO n 
1 223 PRO n 
1 224 ILE n 
1 225 LYS n 
1 226 PRO n 
1 227 PRO n 
1 228 GLY n 
1 229 ILE n 
1 230 ILE n 
1 231 TYR n 
1 232 ASP n 
1 233 SER n 
1 234 LEU n 
1 235 GLY n 
1 236 TYR n 
1 237 MET n 
1 238 ASN n 
1 239 THR n 
1 240 VAL n 
1 241 GLU n 
1 242 ARG n 
1 243 ILE n 
1 244 ARG n 
1 245 ARG n 
1 246 ILE n 
1 247 ALA n 
1 248 GLN n 
1 249 GLU n 
1 250 THR n 
1 251 LYS n 
1 252 SER n 
1 253 GLN n 
1 254 VAL n 
1 255 TRP n 
1 256 PHE n 
1 257 GLY n 
1 258 HIS n 
1 259 ASP n 
1 260 ALA n 
1 261 GLU n 
1 262 GLN n 
1 263 PHE n 
1 264 LYS n 
1 265 LYS n 
1 266 PHE n 
1 267 ARG n 
1 268 LYS n 
1 269 SER n 
1 270 THR n 
1 271 GLU n 
1 272 GLY n 
1 273 TYR n 
1 274 TYR n 
1 275 GLU 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                   275 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GCA01S_030_00190 
_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      'Parageobacillus caldoxylosilyticus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     81408 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ?                 'C4 H7 N O4'     133.103 
CO  non-polymer         . 'COBALT (II) ION'       ?                 'Co 2'           58.933  
CYS 'L-peptide linking' y CYSTEINE                ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
FE  non-polymer         . 'FE (III) ION'          ?                 'Fe 3'           55.845  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                 'C4 H10 O3'      106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'    ?                 'C6 H14 O4'      150.173 
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 
SO4 non-polymer         . 'SULFATE ION'           ?                 'O4 S -2'        96.063  
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   ARG 1   9   9   ARG ARG A . n 
A 1 2   PRO 2   10  10  PRO PRO A . n 
A 1 3   LYS 3   11  11  LYS LYS A . n 
A 1 4   LEU 4   12  12  LEU LEU A . n 
A 1 5   TYR 5   13  13  TYR TYR A . n 
A 1 6   VAL 6   14  14  VAL VAL A . n 
A 1 7   MET 7   15  15  MET MET A . n 
A 1 8   ASP 8   16  16  ASP ASP A . n 
A 1 9   ASN 9   17  17  ASN ASN A . n 
A 1 10  GLY 10  18  18  GLY GLY A . n 
A 1 11  ARG 11  19  19  ARG ARG A . n 
A 1 12  MET 12  20  20  MET MET A . n 
A 1 13  ARG 13  21  21  ARG ARG A . n 
A 1 14  MET 14  22  22  MET MET A . n 
A 1 15  ASP 15  23  23  ASP ASP A . n 
A 1 16  LYS 16  24  24  LYS LYS A . n 
A 1 17  ASN 17  25  25  ASN ASN A . n 
A 1 18  TRP 18  26  26  TRP TRP A . n 
A 1 19  MET 19  27  27  MET MET A . n 
A 1 20  ILE 20  28  28  ILE ILE A . n 
A 1 21  ALA 21  29  29  ALA ALA A . n 
A 1 22  MET 22  30  30  MET MET A . n 
A 1 23  HIS 23  31  31  HIS HIS A . n 
A 1 24  ASN 24  32  32  ASN ASN A . n 
A 1 25  PRO 25  33  33  PRO PRO A . n 
A 1 26  ALA 26  34  34  ALA ALA A . n 
A 1 27  THR 27  35  35  THR THR A . n 
A 1 28  ILE 28  36  36  ILE ILE A . n 
A 1 29  HIS 29  37  37  HIS HIS A . n 
A 1 30  ASN 30  38  38  ASN ASN A . n 
A 1 31  PRO 31  39  39  PRO PRO A . n 
A 1 32  ASN 32  40  40  ASN ASN A . n 
A 1 33  ALA 33  41  41  ALA ALA A . n 
A 1 34  GLN 34  42  42  GLN GLN A . n 
A 1 35  THR 35  43  43  THR THR A . n 
A 1 36  GLU 36  44  44  GLU GLU A . n 
A 1 37  PHE 37  45  45  PHE PHE A . n 
A 1 38  VAL 38  46  46  VAL VAL A . n 
A 1 39  GLU 39  47  47  GLU GLU A . n 
A 1 40  PHE 40  48  48  PHE PHE A . n 
A 1 41  PRO 41  49  49  PRO PRO A . n 
A 1 42  ILE 42  50  50  ILE ILE A . n 
A 1 43  TYR 43  51  51  TYR TYR A . n 
A 1 44  THR 44  52  52  THR THR A . n 
A 1 45  VAL 45  53  53  VAL VAL A . n 
A 1 46  LEU 46  54  54  LEU LEU A . n 
A 1 47  ILE 47  55  55  ILE ILE A . n 
A 1 48  ASP 48  56  56  ASP ASP A . n 
A 1 49  HIS 49  57  57  HIS HIS A . n 
A 1 50  PRO 50  58  58  PRO PRO A . n 
A 1 51  GLU 51  59  59  GLU GLU A . n 
A 1 52  GLY 52  60  60  GLY GLY A . n 
A 1 53  LYS 53  61  61  LYS LYS A . n 
A 1 54  ILE 54  62  62  ILE ILE A . n 
A 1 55  LEU 55  63  63  LEU LEU A . n 
A 1 56  PHE 56  64  64  PHE PHE A . n 
A 1 57  ASP 57  65  65  ASP ASP A . n 
A 1 58  THR 58  66  66  THR THR A . n 
A 1 59  SER 59  67  67  SER SER A . n 
A 1 60  CYS 60  68  68  CYS CYS A . n 
A 1 61  ASN 61  69  69  ASN ASN A . n 
A 1 62  PRO 62  70  70  PRO PRO A . n 
A 1 63  ASN 63  71  71  ASN ASN A . n 
A 1 64  SER 64  72  72  SER SER A . n 
A 1 65  MET 65  73  73  MET MET A . n 
A 1 66  GLY 66  74  74  GLY GLY A . n 
A 1 67  PRO 67  75  75  PRO PRO A . n 
A 1 68  GLN 68  76  76  GLN GLN A . n 
A 1 69  GLY 69  77  77  GLY GLY A . n 
A 1 70  ARG 70  78  78  ARG ARG A . n 
A 1 71  TRP 71  79  79  TRP TRP A . n 
A 1 72  ALA 72  80  80  ALA ALA A . n 
A 1 73  GLU 73  81  81  GLU GLU A . n 
A 1 74  SER 74  82  82  SER SER A . n 
A 1 75  THR 75  83  83  THR THR A . n 
A 1 76  GLN 76  84  84  GLN GLN A . n 
A 1 77  GLN 77  85  85  GLN GLN A . n 
A 1 78  MET 78  86  86  MET MET A . n 
A 1 79  PHE 79  87  87  PHE PHE A . n 
A 1 80  PRO 80  88  88  PRO PRO A . n 
A 1 81  TRP 81  89  89  TRP TRP A . n 
A 1 82  THR 82  90  90  THR THR A . n 
A 1 83  ALA 83  91  91  ALA ALA A . n 
A 1 84  THR 84  92  92  THR THR A . n 
A 1 85  GLU 85  93  93  GLU GLU A . n 
A 1 86  GLU 86  94  94  GLU GLU A . n 
A 1 87  CYS 87  95  95  CYS CYS A . n 
A 1 88  TYR 88  96  96  TYR TYR A . n 
A 1 89  LEU 89  97  97  LEU LEU A . n 
A 1 90  HIS 90  98  98  HIS HIS A . n 
A 1 91  ASN 91  99  99  ASN ASN A . n 
A 1 92  ARG 92  100 100 ARG ARG A . n 
A 1 93  LEU 93  101 101 LEU LEU A . n 
A 1 94  GLU 94  102 102 GLU GLU A . n 
A 1 95  GLN 95  103 103 GLN GLN A . n 
A 1 96  LEU 96  104 104 LEU LEU A . n 
A 1 97  LYS 97  105 105 LYS LYS A . n 
A 1 98  VAL 98  106 106 VAL VAL A . n 
A 1 99  ARG 99  107 107 ARG ARG A . n 
A 1 100 PRO 100 108 108 PRO PRO A . n 
A 1 101 GLU 101 109 109 GLU GLU A . n 
A 1 102 ASP 102 110 110 ASP ASP A . n 
A 1 103 ILE 103 111 111 ILE ILE A . n 
A 1 104 ARG 104 112 112 ARG ARG A . n 
A 1 105 TYR 105 113 113 TYR TYR A . n 
A 1 106 VAL 106 114 114 VAL VAL A . n 
A 1 107 VAL 107 115 115 VAL VAL A . n 
A 1 108 ALA 108 116 116 ALA ALA A . n 
A 1 109 SER 109 117 117 SER SER A . n 
A 1 110 HIS 110 118 118 HIS HIS A . n 
A 1 111 LEU 111 119 119 LEU LEU A . n 
A 1 112 HIS 112 120 120 HIS HIS A . n 
A 1 113 LEU 113 121 121 LEU LEU A . n 
A 1 114 ASN 114 122 122 ASN ASN A . n 
A 1 115 HIS 115 123 123 HIS HIS A . n 
A 1 116 ALA 116 124 124 ALA ALA A . n 
A 1 117 GLY 117 125 125 GLY GLY A . n 
A 1 118 CYS 118 126 126 CYS CYS A . n 
A 1 119 LEU 119 127 127 LEU LEU A . n 
A 1 120 GLU 120 128 128 GLU GLU A . n 
A 1 121 MET 121 129 129 MET MET A . n 
A 1 122 PHE 122 130 130 PHE PHE A . n 
A 1 123 THR 123 131 131 THR THR A . n 
A 1 124 ASN 124 132 132 ASN ASN A . n 
A 1 125 ALA 125 133 133 ALA ALA A . n 
A 1 126 THR 126 134 134 THR THR A . n 
A 1 127 ILE 127 135 135 ILE ILE A . n 
A 1 128 ILE 128 136 136 ILE ILE A . n 
A 1 129 VAL 129 137 137 VAL VAL A . n 
A 1 130 HIS 130 138 138 HIS HIS A . n 
A 1 131 GLU 131 139 139 GLU GLU A . n 
A 1 132 ASP 132 140 140 ASP ASP A . n 
A 1 133 GLU 133 141 141 GLU GLU A . n 
A 1 134 PHE 134 142 142 PHE PHE A . n 
A 1 135 ASN 135 143 143 ASN ASN A . n 
A 1 136 GLY 136 144 144 GLY GLY A . n 
A 1 137 ALA 137 145 145 ALA ALA A . n 
A 1 138 LEU 138 146 146 LEU LEU A . n 
A 1 139 GLN 139 147 147 GLN GLN A . n 
A 1 140 CYS 140 148 148 CYS CYS A . n 
A 1 141 TYR 141 149 149 TYR TYR A . n 
A 1 142 ALA 142 150 150 ALA ALA A . n 
A 1 143 ARG 143 151 151 ARG ARG A . n 
A 1 144 ASN 144 152 152 ASN ASN A . n 
A 1 145 GLN 145 153 153 GLN GLN A . n 
A 1 146 LYS 146 154 154 LYS LYS A . n 
A 1 147 GLU 147 155 155 GLU GLU A . n 
A 1 148 GLY 148 156 156 GLY GLY A . n 
A 1 149 ALA 149 157 157 ALA ALA A . n 
A 1 150 TYR 150 158 158 TYR TYR A . n 
A 1 151 ILE 151 159 159 ILE ILE A . n 
A 1 152 TRP 152 160 160 TRP TRP A . n 
A 1 153 ALA 153 161 161 ALA ALA A . n 
A 1 154 ASP 154 162 162 ASP ASP A . n 
A 1 155 ILE 155 163 163 ILE ILE A . n 
A 1 156 ASP 156 164 164 ASP ASP A . n 
A 1 157 ALA 157 165 165 ALA ALA A . n 
A 1 158 TRP 158 166 166 TRP TRP A . n 
A 1 159 ILE 159 167 167 ILE ILE A . n 
A 1 160 LYS 160 168 168 LYS LYS A . n 
A 1 161 ASN 161 169 169 ASN ASN A . n 
A 1 162 ASN 162 170 170 ASN ASN A . n 
A 1 163 LEU 163 171 171 LEU LEU A . n 
A 1 164 GLN 164 172 172 GLN GLN A . n 
A 1 165 TRP 165 173 173 TRP TRP A . n 
A 1 166 ARG 166 174 174 ARG ARG A . n 
A 1 167 THR 167 175 175 THR THR A . n 
A 1 168 VAL 168 176 176 VAL VAL A . n 
A 1 169 LYS 169 177 177 LYS LYS A . n 
A 1 170 ARG 170 178 178 ARG ARG A . n 
A 1 171 HIS 171 179 179 HIS HIS A . n 
A 1 172 GLU 172 180 180 GLU GLU A . n 
A 1 173 ASP 173 181 181 ASP ASP A . n 
A 1 174 ASN 174 182 182 ASN ASN A . n 
A 1 175 ILE 175 183 183 ILE ILE A . n 
A 1 176 LEU 176 184 184 LEU LEU A . n 
A 1 177 LEU 177 185 185 LEU LEU A . n 
A 1 178 ALA 178 186 186 ALA ALA A . n 
A 1 179 GLU 179 187 187 GLU GLU A . n 
A 1 180 GLY 180 188 188 GLY GLY A . n 
A 1 181 VAL 181 189 189 VAL VAL A . n 
A 1 182 LYS 182 190 190 LYS LYS A . n 
A 1 183 VAL 183 191 191 VAL VAL A . n 
A 1 184 LEU 184 192 192 LEU LEU A . n 
A 1 185 ASN 185 193 193 ASN ASN A . n 
A 1 186 PHE 186 194 194 PHE PHE A . n 
A 1 187 GLY 187 195 195 GLY GLY A . n 
A 1 188 SER 188 196 196 SER SER A . n 
A 1 189 GLY 189 197 197 GLY GLY A . n 
A 1 190 HIS 190 198 198 HIS HIS A . n 
A 1 191 ALA 191 199 199 ALA ALA A . n 
A 1 192 TRP 192 200 200 TRP TRP A . n 
A 1 193 GLY 193 201 201 GLY GLY A . n 
A 1 194 MET 194 202 202 MET MET A . n 
A 1 195 LEU 195 203 203 LEU LEU A . n 
A 1 196 GLY 196 204 204 GLY GLY A . n 
A 1 197 LEU 197 205 205 LEU LEU A . n 
A 1 198 HIS 198 206 206 HIS HIS A . n 
A 1 199 VAL 199 207 207 VAL VAL A . n 
A 1 200 GLU 200 208 208 GLU GLU A . n 
A 1 201 LEU 201 209 209 LEU LEU A . n 
A 1 202 PRO 202 210 210 PRO PRO A . n 
A 1 203 GLU 203 211 211 GLU GLU A . n 
A 1 204 THR 204 212 212 THR THR A . n 
A 1 205 GLY 205 213 213 GLY GLY A . n 
A 1 206 GLY 206 214 214 GLY GLY A . n 
A 1 207 ILE 207 215 215 ILE ILE A . n 
A 1 208 ILE 208 216 216 ILE ILE A . n 
A 1 209 LEU 209 217 217 LEU LEU A . n 
A 1 210 ALA 210 218 218 ALA ALA A . n 
A 1 211 SER 211 219 219 SER SER A . n 
A 1 212 ASP 212 220 220 ASP ASP A . n 
A 1 213 ALA 213 221 221 ALA ALA A . n 
A 1 214 ILE 214 222 222 ILE ILE A . n 
A 1 215 TYR 215 223 223 TYR TYR A . n 
A 1 216 THR 216 224 224 THR THR A . n 
A 1 217 ALA 217 225 225 ALA ALA A . n 
A 1 218 GLU 218 226 226 GLU GLU A . n 
A 1 219 SER 219 227 227 SER SER A . n 
A 1 220 TYR 220 228 228 TYR TYR A . n 
A 1 221 GLY 221 229 229 GLY GLY A . n 
A 1 222 PRO 222 230 230 PRO PRO A . n 
A 1 223 PRO 223 231 231 PRO PRO A . n 
A 1 224 ILE 224 232 232 ILE ILE A . n 
A 1 225 LYS 225 233 233 LYS LYS A . n 
A 1 226 PRO 226 234 234 PRO PRO A . n 
A 1 227 PRO 227 235 235 PRO PRO A . n 
A 1 228 GLY 228 236 236 GLY GLY A . n 
A 1 229 ILE 229 237 237 ILE ILE A . n 
A 1 230 ILE 230 238 238 ILE ILE A . n 
A 1 231 TYR 231 239 239 TYR TYR A . n 
A 1 232 ASP 232 240 240 ASP ASP A . n 
A 1 233 SER 233 241 241 SER SER A . n 
A 1 234 LEU 234 242 242 LEU LEU A . n 
A 1 235 GLY 235 243 243 GLY GLY A . n 
A 1 236 TYR 236 244 244 TYR TYR A . n 
A 1 237 MET 237 245 245 MET MET A . n 
A 1 238 ASN 238 246 246 ASN ASN A . n 
A 1 239 THR 239 247 247 THR THR A . n 
A 1 240 VAL 240 248 248 VAL VAL A . n 
A 1 241 GLU 241 249 249 GLU GLU A . n 
A 1 242 ARG 242 250 250 ARG ARG A . n 
A 1 243 ILE 243 251 251 ILE ILE A . n 
A 1 244 ARG 244 252 252 ARG ARG A . n 
A 1 245 ARG 245 253 253 ARG ARG A . n 
A 1 246 ILE 246 254 254 ILE ILE A . n 
A 1 247 ALA 247 255 255 ALA ALA A . n 
A 1 248 GLN 248 256 256 GLN GLN A . n 
A 1 249 GLU 249 257 257 GLU GLU A . n 
A 1 250 THR 250 258 258 THR THR A . n 
A 1 251 LYS 251 259 259 LYS LYS A . n 
A 1 252 SER 252 260 260 SER SER A . n 
A 1 253 GLN 253 261 261 GLN GLN A . n 
A 1 254 VAL 254 262 262 VAL VAL A . n 
A 1 255 TRP 255 263 263 TRP TRP A . n 
A 1 256 PHE 256 264 264 PHE PHE A . n 
A 1 257 GLY 257 265 265 GLY GLY A . n 
A 1 258 HIS 258 266 266 HIS HIS A . n 
A 1 259 ASP 259 267 267 ASP ASP A . n 
A 1 260 ALA 260 268 268 ALA ALA A . n 
A 1 261 GLU 261 269 269 GLU GLU A . n 
A 1 262 GLN 262 270 270 GLN GLN A . n 
A 1 263 PHE 263 271 271 PHE PHE A . n 
A 1 264 LYS 264 272 272 LYS LYS A . n 
A 1 265 LYS 265 273 273 LYS LYS A . n 
A 1 266 PHE 266 274 274 PHE PHE A . n 
A 1 267 ARG 267 275 275 ARG ARG A . n 
A 1 268 LYS 268 276 276 LYS LYS A . n 
A 1 269 SER 269 277 277 SER SER A . n 
A 1 270 THR 270 278 278 THR THR A . n 
A 1 271 GLU 271 279 279 GLU GLU A . n 
A 1 272 GLY 272 280 280 GLY GLY A . n 
A 1 273 TYR 273 281 281 TYR TYR A . n 
A 1 274 TYR 274 282 282 TYR TYR A . n 
A 1 275 GLU 275 283 283 GLU GLU A . n 
B 1 1   ARG 1   9   9   ARG ARG B . n 
B 1 2   PRO 2   10  10  PRO PRO B . n 
B 1 3   LYS 3   11  11  LYS LYS B . n 
B 1 4   LEU 4   12  12  LEU LEU B . n 
B 1 5   TYR 5   13  13  TYR TYR B . n 
B 1 6   VAL 6   14  14  VAL VAL B . n 
B 1 7   MET 7   15  15  MET MET B . n 
B 1 8   ASP 8   16  16  ASP ASP B . n 
B 1 9   ASN 9   17  17  ASN ASN B . n 
B 1 10  GLY 10  18  18  GLY GLY B . n 
B 1 11  ARG 11  19  19  ARG ARG B . n 
B 1 12  MET 12  20  20  MET MET B . n 
B 1 13  ARG 13  21  21  ARG ARG B . n 
B 1 14  MET 14  22  22  MET MET B . n 
B 1 15  ASP 15  23  23  ASP ASP B . n 
B 1 16  LYS 16  24  24  LYS LYS B . n 
B 1 17  ASN 17  25  25  ASN ASN B . n 
B 1 18  TRP 18  26  26  TRP TRP B . n 
B 1 19  MET 19  27  27  MET MET B . n 
B 1 20  ILE 20  28  28  ILE ILE B . n 
B 1 21  ALA 21  29  29  ALA ALA B . n 
B 1 22  MET 22  30  30  MET MET B . n 
B 1 23  HIS 23  31  31  HIS HIS B . n 
B 1 24  ASN 24  32  32  ASN ASN B . n 
B 1 25  PRO 25  33  33  PRO PRO B . n 
B 1 26  ALA 26  34  34  ALA ALA B . n 
B 1 27  THR 27  35  35  THR THR B . n 
B 1 28  ILE 28  36  36  ILE ILE B . n 
B 1 29  HIS 29  37  37  HIS HIS B . n 
B 1 30  ASN 30  38  38  ASN ASN B . n 
B 1 31  PRO 31  39  39  PRO PRO B . n 
B 1 32  ASN 32  40  40  ASN ASN B . n 
B 1 33  ALA 33  41  41  ALA ALA B . n 
B 1 34  GLN 34  42  42  GLN GLN B . n 
B 1 35  THR 35  43  43  THR THR B . n 
B 1 36  GLU 36  44  44  GLU GLU B . n 
B 1 37  PHE 37  45  45  PHE PHE B . n 
B 1 38  VAL 38  46  46  VAL VAL B . n 
B 1 39  GLU 39  47  47  GLU GLU B . n 
B 1 40  PHE 40  48  48  PHE PHE B . n 
B 1 41  PRO 41  49  49  PRO PRO B . n 
B 1 42  ILE 42  50  50  ILE ILE B . n 
B 1 43  TYR 43  51  51  TYR TYR B . n 
B 1 44  THR 44  52  52  THR THR B . n 
B 1 45  VAL 45  53  53  VAL VAL B . n 
B 1 46  LEU 46  54  54  LEU LEU B . n 
B 1 47  ILE 47  55  55  ILE ILE B . n 
B 1 48  ASP 48  56  56  ASP ASP B . n 
B 1 49  HIS 49  57  57  HIS HIS B . n 
B 1 50  PRO 50  58  58  PRO PRO B . n 
B 1 51  GLU 51  59  59  GLU GLU B . n 
B 1 52  GLY 52  60  60  GLY GLY B . n 
B 1 53  LYS 53  61  61  LYS LYS B . n 
B 1 54  ILE 54  62  62  ILE ILE B . n 
B 1 55  LEU 55  63  63  LEU LEU B . n 
B 1 56  PHE 56  64  64  PHE PHE B . n 
B 1 57  ASP 57  65  65  ASP ASP B . n 
B 1 58  THR 58  66  66  THR THR B . n 
B 1 59  SER 59  67  67  SER SER B . n 
B 1 60  CYS 60  68  68  CYS CYS B . n 
B 1 61  ASN 61  69  69  ASN ASN B . n 
B 1 62  PRO 62  70  70  PRO PRO B . n 
B 1 63  ASN 63  71  71  ASN ASN B . n 
B 1 64  SER 64  72  72  SER SER B . n 
B 1 65  MET 65  73  73  MET MET B . n 
B 1 66  GLY 66  74  74  GLY GLY B . n 
B 1 67  PRO 67  75  75  PRO PRO B . n 
B 1 68  GLN 68  76  76  GLN GLN B . n 
B 1 69  GLY 69  77  77  GLY GLY B . n 
B 1 70  ARG 70  78  78  ARG ARG B . n 
B 1 71  TRP 71  79  79  TRP TRP B . n 
B 1 72  ALA 72  80  80  ALA ALA B . n 
B 1 73  GLU 73  81  81  GLU GLU B . n 
B 1 74  SER 74  82  82  SER SER B . n 
B 1 75  THR 75  83  83  THR THR B . n 
B 1 76  GLN 76  84  84  GLN GLN B . n 
B 1 77  GLN 77  85  85  GLN GLN B . n 
B 1 78  MET 78  86  86  MET MET B . n 
B 1 79  PHE 79  87  87  PHE PHE B . n 
B 1 80  PRO 80  88  88  PRO PRO B . n 
B 1 81  TRP 81  89  89  TRP TRP B . n 
B 1 82  THR 82  90  90  THR THR B . n 
B 1 83  ALA 83  91  91  ALA ALA B . n 
B 1 84  THR 84  92  92  THR THR B . n 
B 1 85  GLU 85  93  93  GLU GLU B . n 
B 1 86  GLU 86  94  94  GLU GLU B . n 
B 1 87  CYS 87  95  95  CYS CYS B . n 
B 1 88  TYR 88  96  96  TYR TYR B . n 
B 1 89  LEU 89  97  97  LEU LEU B . n 
B 1 90  HIS 90  98  98  HIS HIS B . n 
B 1 91  ASN 91  99  99  ASN ASN B . n 
B 1 92  ARG 92  100 100 ARG ARG B . n 
B 1 93  LEU 93  101 101 LEU LEU B . n 
B 1 94  GLU 94  102 102 GLU GLU B . n 
B 1 95  GLN 95  103 103 GLN GLN B . n 
B 1 96  LEU 96  104 104 LEU LEU B . n 
B 1 97  LYS 97  105 105 LYS LYS B . n 
B 1 98  VAL 98  106 106 VAL VAL B . n 
B 1 99  ARG 99  107 107 ARG ARG B . n 
B 1 100 PRO 100 108 108 PRO PRO B . n 
B 1 101 GLU 101 109 109 GLU GLU B . n 
B 1 102 ASP 102 110 110 ASP ASP B . n 
B 1 103 ILE 103 111 111 ILE ILE B . n 
B 1 104 ARG 104 112 112 ARG ARG B . n 
B 1 105 TYR 105 113 113 TYR TYR B . n 
B 1 106 VAL 106 114 114 VAL VAL B . n 
B 1 107 VAL 107 115 115 VAL VAL B . n 
B 1 108 ALA 108 116 116 ALA ALA B . n 
B 1 109 SER 109 117 117 SER SER B . n 
B 1 110 HIS 110 118 118 HIS HIS B . n 
B 1 111 LEU 111 119 119 LEU LEU B . n 
B 1 112 HIS 112 120 120 HIS HIS B . n 
B 1 113 LEU 113 121 121 LEU LEU B . n 
B 1 114 ASN 114 122 122 ASN ASN B . n 
B 1 115 HIS 115 123 123 HIS HIS B . n 
B 1 116 ALA 116 124 124 ALA ALA B . n 
B 1 117 GLY 117 125 125 GLY GLY B . n 
B 1 118 CYS 118 126 126 CYS CYS B . n 
B 1 119 LEU 119 127 127 LEU LEU B . n 
B 1 120 GLU 120 128 128 GLU GLU B . n 
B 1 121 MET 121 129 129 MET MET B . n 
B 1 122 PHE 122 130 130 PHE PHE B . n 
B 1 123 THR 123 131 131 THR THR B . n 
B 1 124 ASN 124 132 132 ASN ASN B . n 
B 1 125 ALA 125 133 133 ALA ALA B . n 
B 1 126 THR 126 134 134 THR THR B . n 
B 1 127 ILE 127 135 135 ILE ILE B . n 
B 1 128 ILE 128 136 136 ILE ILE B . n 
B 1 129 VAL 129 137 137 VAL VAL B . n 
B 1 130 HIS 130 138 138 HIS HIS B . n 
B 1 131 GLU 131 139 139 GLU GLU B . n 
B 1 132 ASP 132 140 140 ASP ASP B . n 
B 1 133 GLU 133 141 141 GLU GLU B . n 
B 1 134 PHE 134 142 142 PHE PHE B . n 
B 1 135 ASN 135 143 143 ASN ASN B . n 
B 1 136 GLY 136 144 144 GLY GLY B . n 
B 1 137 ALA 137 145 145 ALA ALA B . n 
B 1 138 LEU 138 146 146 LEU LEU B . n 
B 1 139 GLN 139 147 147 GLN GLN B . n 
B 1 140 CYS 140 148 148 CYS CYS B . n 
B 1 141 TYR 141 149 149 TYR TYR B . n 
B 1 142 ALA 142 150 150 ALA ALA B . n 
B 1 143 ARG 143 151 151 ARG ARG B . n 
B 1 144 ASN 144 152 152 ASN ASN B . n 
B 1 145 GLN 145 153 153 GLN GLN B . n 
B 1 146 LYS 146 154 154 LYS LYS B . n 
B 1 147 GLU 147 155 155 GLU GLU B . n 
B 1 148 GLY 148 156 156 GLY GLY B . n 
B 1 149 ALA 149 157 157 ALA ALA B . n 
B 1 150 TYR 150 158 158 TYR TYR B . n 
B 1 151 ILE 151 159 159 ILE ILE B . n 
B 1 152 TRP 152 160 160 TRP TRP B . n 
B 1 153 ALA 153 161 161 ALA ALA B . n 
B 1 154 ASP 154 162 162 ASP ASP B . n 
B 1 155 ILE 155 163 163 ILE ILE B . n 
B 1 156 ASP 156 164 164 ASP ASP B . n 
B 1 157 ALA 157 165 165 ALA ALA B . n 
B 1 158 TRP 158 166 166 TRP TRP B . n 
B 1 159 ILE 159 167 167 ILE ILE B . n 
B 1 160 LYS 160 168 168 LYS LYS B . n 
B 1 161 ASN 161 169 169 ASN ASN B . n 
B 1 162 ASN 162 170 170 ASN ASN B . n 
B 1 163 LEU 163 171 171 LEU LEU B . n 
B 1 164 GLN 164 172 172 GLN GLN B . n 
B 1 165 TRP 165 173 173 TRP TRP B . n 
B 1 166 ARG 166 174 174 ARG ARG B . n 
B 1 167 THR 167 175 175 THR THR B . n 
B 1 168 VAL 168 176 176 VAL VAL B . n 
B 1 169 LYS 169 177 177 LYS LYS B . n 
B 1 170 ARG 170 178 178 ARG ARG B . n 
B 1 171 HIS 171 179 179 HIS HIS B . n 
B 1 172 GLU 172 180 180 GLU GLU B . n 
B 1 173 ASP 173 181 181 ASP ASP B . n 
B 1 174 ASN 174 182 182 ASN ASN B . n 
B 1 175 ILE 175 183 183 ILE ILE B . n 
B 1 176 LEU 176 184 184 LEU LEU B . n 
B 1 177 LEU 177 185 185 LEU LEU B . n 
B 1 178 ALA 178 186 186 ALA ALA B . n 
B 1 179 GLU 179 187 187 GLU GLU B . n 
B 1 180 GLY 180 188 188 GLY GLY B . n 
B 1 181 VAL 181 189 189 VAL VAL B . n 
B 1 182 LYS 182 190 190 LYS LYS B . n 
B 1 183 VAL 183 191 191 VAL VAL B . n 
B 1 184 LEU 184 192 192 LEU LEU B . n 
B 1 185 ASN 185 193 193 ASN ASN B . n 
B 1 186 PHE 186 194 194 PHE PHE B . n 
B 1 187 GLY 187 195 195 GLY GLY B . n 
B 1 188 SER 188 196 196 SER SER B . n 
B 1 189 GLY 189 197 197 GLY GLY B . n 
B 1 190 HIS 190 198 198 HIS HIS B . n 
B 1 191 ALA 191 199 199 ALA ALA B . n 
B 1 192 TRP 192 200 200 TRP TRP B . n 
B 1 193 GLY 193 201 201 GLY GLY B . n 
B 1 194 MET 194 202 202 MET MET B . n 
B 1 195 LEU 195 203 203 LEU LEU B . n 
B 1 196 GLY 196 204 204 GLY GLY B . n 
B 1 197 LEU 197 205 205 LEU LEU B . n 
B 1 198 HIS 198 206 206 HIS HIS B . n 
B 1 199 VAL 199 207 207 VAL VAL B . n 
B 1 200 GLU 200 208 208 GLU GLU B . n 
B 1 201 LEU 201 209 209 LEU LEU B . n 
B 1 202 PRO 202 210 210 PRO PRO B . n 
B 1 203 GLU 203 211 211 GLU GLU B . n 
B 1 204 THR 204 212 212 THR THR B . n 
B 1 205 GLY 205 213 213 GLY GLY B . n 
B 1 206 GLY 206 214 214 GLY GLY B . n 
B 1 207 ILE 207 215 215 ILE ILE B . n 
B 1 208 ILE 208 216 216 ILE ILE B . n 
B 1 209 LEU 209 217 217 LEU LEU B . n 
B 1 210 ALA 210 218 218 ALA ALA B . n 
B 1 211 SER 211 219 219 SER SER B . n 
B 1 212 ASP 212 220 220 ASP ASP B . n 
B 1 213 ALA 213 221 221 ALA ALA B . n 
B 1 214 ILE 214 222 222 ILE ILE B . n 
B 1 215 TYR 215 223 223 TYR TYR B . n 
B 1 216 THR 216 224 224 THR THR B . n 
B 1 217 ALA 217 225 225 ALA ALA B . n 
B 1 218 GLU 218 226 226 GLU GLU B . n 
B 1 219 SER 219 227 227 SER SER B . n 
B 1 220 TYR 220 228 228 TYR TYR B . n 
B 1 221 GLY 221 229 229 GLY GLY B . n 
B 1 222 PRO 222 230 230 PRO PRO B . n 
B 1 223 PRO 223 231 231 PRO PRO B . n 
B 1 224 ILE 224 232 232 ILE ILE B . n 
B 1 225 LYS 225 233 233 LYS LYS B . n 
B 1 226 PRO 226 234 234 PRO PRO B . n 
B 1 227 PRO 227 235 235 PRO PRO B . n 
B 1 228 GLY 228 236 236 GLY GLY B . n 
B 1 229 ILE 229 237 237 ILE ILE B . n 
B 1 230 ILE 230 238 238 ILE ILE B . n 
B 1 231 TYR 231 239 239 TYR TYR B . n 
B 1 232 ASP 232 240 240 ASP ASP B . n 
B 1 233 SER 233 241 241 SER SER B . n 
B 1 234 LEU 234 242 242 LEU LEU B . n 
B 1 235 GLY 235 243 243 GLY GLY B . n 
B 1 236 TYR 236 244 244 TYR TYR B . n 
B 1 237 MET 237 245 245 MET MET B . n 
B 1 238 ASN 238 246 246 ASN ASN B . n 
B 1 239 THR 239 247 247 THR THR B . n 
B 1 240 VAL 240 248 248 VAL VAL B . n 
B 1 241 GLU 241 249 249 GLU GLU B . n 
B 1 242 ARG 242 250 250 ARG ARG B . n 
B 1 243 ILE 243 251 251 ILE ILE B . n 
B 1 244 ARG 244 252 252 ARG ARG B . n 
B 1 245 ARG 245 253 253 ARG ARG B . n 
B 1 246 ILE 246 254 254 ILE ILE B . n 
B 1 247 ALA 247 255 255 ALA ALA B . n 
B 1 248 GLN 248 256 256 GLN GLN B . n 
B 1 249 GLU 249 257 257 GLU GLU B . n 
B 1 250 THR 250 258 258 THR THR B . n 
B 1 251 LYS 251 259 259 LYS LYS B . n 
B 1 252 SER 252 260 260 SER SER B . n 
B 1 253 GLN 253 261 261 GLN GLN B . n 
B 1 254 VAL 254 262 262 VAL VAL B . n 
B 1 255 TRP 255 263 263 TRP TRP B . n 
B 1 256 PHE 256 264 264 PHE PHE B . n 
B 1 257 GLY 257 265 265 GLY GLY B . n 
B 1 258 HIS 258 266 266 HIS HIS B . n 
B 1 259 ASP 259 267 267 ASP ASP B . n 
B 1 260 ALA 260 268 268 ALA ALA B . n 
B 1 261 GLU 261 269 269 GLU GLU B . n 
B 1 262 GLN 262 270 270 GLN GLN B . n 
B 1 263 PHE 263 271 271 PHE PHE B . n 
B 1 264 LYS 264 272 272 LYS LYS B . n 
B 1 265 LYS 265 273 273 LYS LYS B . n 
B 1 266 PHE 266 274 274 PHE PHE B . n 
B 1 267 ARG 267 275 275 ARG ARG B . n 
B 1 268 LYS 268 276 276 LYS LYS B . n 
B 1 269 SER 269 277 277 SER SER B . n 
B 1 270 THR 270 278 278 THR THR B . n 
B 1 271 GLU 271 279 279 GLU GLU B . n 
B 1 272 GLY 272 280 280 GLY GLY B . n 
B 1 273 TYR 273 281 281 TYR TYR B . n 
B 1 274 TYR 274 282 282 TYR TYR B . n 
B 1 275 GLU 275 283 283 GLU GLU 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 FE ? ? FE ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CO ? ? CO ? ? '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 SO4 1  301 301 SO4 SO4 A . 
D 3 PEG 1  302 402 PEG PEG A . 
E 4 PGE 1  303 403 PGE PGE A . 
F 2 SO4 1  304 401 SO4 SO4 A . 
G 5 EDO 1  305 403 EDO EDO A . 
H 6 FE  1  306 3   FE  FE  A . 
I 7 CO  1  307 4   CO  CO  A . 
J 2 SO4 1  401 401 SO4 SO4 B . 
K 2 SO4 1  402 301 SO4 SO4 B . 
L 5 EDO 1  403 402 EDO EDO B . 
M 3 PEG 1  404 404 PEG PEG B . 
N 6 FE  1  405 3   FE  FE  B . 
O 7 CO  1  406 4   CO  CO  B . 
P 8 HOH 1  401 92  HOH HOH A . 
P 8 HOH 2  402 94  HOH HOH A . 
P 8 HOH 3  403 104 HOH HOH A . 
P 8 HOH 4  404 37  HOH HOH A . 
P 8 HOH 5  405 40  HOH HOH A . 
P 8 HOH 6  406 88  HOH HOH A . 
P 8 HOH 7  407 38  HOH HOH A . 
P 8 HOH 8  408 107 HOH HOH A . 
P 8 HOH 9  409 59  HOH HOH A . 
P 8 HOH 10 410 35  HOH HOH A . 
P 8 HOH 11 411 80  HOH HOH A . 
P 8 HOH 12 412 50  HOH HOH A . 
P 8 HOH 13 413 56  HOH HOH A . 
P 8 HOH 14 414 30  HOH HOH A . 
P 8 HOH 15 415 111 HOH HOH A . 
P 8 HOH 16 416 47  HOH HOH A . 
P 8 HOH 17 417 16  HOH HOH A . 
P 8 HOH 18 418 65  HOH HOH A . 
P 8 HOH 19 419 109 HOH HOH A . 
P 8 HOH 20 420 57  HOH HOH A . 
P 8 HOH 21 421 33  HOH HOH A . 
P 8 HOH 22 422 105 HOH HOH A . 
P 8 HOH 23 423 84  HOH HOH A . 
P 8 HOH 24 424 5   HOH HOH A . 
P 8 HOH 25 425 17  HOH HOH A . 
P 8 HOH 26 426 115 HOH HOH A . 
P 8 HOH 27 427 49  HOH HOH A . 
P 8 HOH 28 428 63  HOH HOH A . 
P 8 HOH 29 429 46  HOH HOH A . 
P 8 HOH 30 430 81  HOH HOH A . 
P 8 HOH 31 431 25  HOH HOH A . 
P 8 HOH 32 432 112 HOH HOH A . 
P 8 HOH 33 433 28  HOH HOH A . 
P 8 HOH 34 434 103 HOH HOH A . 
P 8 HOH 35 435 45  HOH HOH A . 
P 8 HOH 36 436 14  HOH HOH A . 
P 8 HOH 37 437 67  HOH HOH A . 
P 8 HOH 38 438 61  HOH HOH A . 
P 8 HOH 39 439 43  HOH HOH A . 
P 8 HOH 40 440 23  HOH HOH A . 
P 8 HOH 41 441 11  HOH HOH A . 
P 8 HOH 42 442 70  HOH HOH A . 
P 8 HOH 43 443 121 HOH HOH A . 
P 8 HOH 44 444 85  HOH HOH A . 
P 8 HOH 45 445 86  HOH HOH A . 
P 8 HOH 46 446 8   HOH HOH A . 
P 8 HOH 47 447 68  HOH HOH A . 
P 8 HOH 48 448 31  HOH HOH A . 
P 8 HOH 49 449 82  HOH HOH A . 
P 8 HOH 50 450 39  HOH HOH A . 
P 8 HOH 51 451 54  HOH HOH A . 
P 8 HOH 52 452 118 HOH HOH A . 
P 8 HOH 53 453 3   HOH HOH A . 
Q 8 HOH 1  501 93  HOH HOH B . 
Q 8 HOH 2  502 96  HOH HOH B . 
Q 8 HOH 3  503 51  HOH HOH B . 
Q 8 HOH 4  504 60  HOH HOH B . 
Q 8 HOH 5  505 97  HOH HOH B . 
Q 8 HOH 6  506 99  HOH HOH B . 
Q 8 HOH 7  507 79  HOH HOH B . 
Q 8 HOH 8  508 110 HOH HOH B . 
Q 8 HOH 9  509 69  HOH HOH B . 
Q 8 HOH 10 510 21  HOH HOH B . 
Q 8 HOH 11 511 53  HOH HOH B . 
Q 8 HOH 12 512 62  HOH HOH B . 
Q 8 HOH 13 513 108 HOH HOH B . 
Q 8 HOH 14 514 52  HOH HOH B . 
Q 8 HOH 15 515 22  HOH HOH B . 
Q 8 HOH 16 516 10  HOH HOH B . 
Q 8 HOH 17 517 120 HOH HOH B . 
Q 8 HOH 18 518 19  HOH HOH B . 
Q 8 HOH 19 519 73  HOH HOH B . 
Q 8 HOH 20 520 72  HOH HOH B . 
Q 8 HOH 21 521 102 HOH HOH B . 
Q 8 HOH 22 522 98  HOH HOH B . 
Q 8 HOH 23 523 4   HOH HOH B . 
Q 8 HOH 24 524 44  HOH HOH B . 
Q 8 HOH 25 525 12  HOH HOH B . 
Q 8 HOH 26 526 95  HOH HOH B . 
Q 8 HOH 27 527 66  HOH HOH B . 
Q 8 HOH 28 528 74  HOH HOH B . 
Q 8 HOH 29 529 101 HOH HOH B . 
Q 8 HOH 30 530 26  HOH HOH B . 
Q 8 HOH 31 531 83  HOH HOH B . 
Q 8 HOH 32 532 114 HOH HOH B . 
Q 8 HOH 33 533 64  HOH HOH B . 
Q 8 HOH 34 534 106 HOH HOH B . 
Q 8 HOH 35 535 36  HOH HOH B . 
Q 8 HOH 36 536 24  HOH HOH B . 
Q 8 HOH 37 537 29  HOH HOH B . 
Q 8 HOH 38 538 32  HOH HOH B . 
Q 8 HOH 39 539 42  HOH HOH B . 
Q 8 HOH 40 540 48  HOH HOH B . 
Q 8 HOH 41 541 100 HOH HOH B . 
Q 8 HOH 42 542 27  HOH HOH B . 
Q 8 HOH 43 543 90  HOH HOH B . 
Q 8 HOH 44 544 71  HOH HOH B . 
Q 8 HOH 45 545 58  HOH HOH B . 
Q 8 HOH 46 546 55  HOH HOH B . 
Q 8 HOH 47 547 20  HOH HOH B . 
Q 8 HOH 48 548 91  HOH HOH B . 
Q 8 HOH 49 549 34  HOH HOH B . 
Q 8 HOH 50 550 15  HOH HOH B . 
Q 8 HOH 51 551 1   HOH HOH B . 
Q 8 HOH 52 552 113 HOH HOH B . 
Q 8 HOH 53 553 117 HOH HOH B . 
Q 8 HOH 54 554 77  HOH HOH B . 
Q 8 HOH 55 555 78  HOH HOH B . 
Q 8 HOH 56 556 119 HOH HOH B . 
Q 8 HOH 57 557 7   HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B2L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     109.220 
_cell.length_a_esd                 ? 
_cell.length_b                     109.220 
_cell.length_b_esd                 ? 
_cell.length_c                     221.660 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9B2L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9B2L 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.97 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          68.98 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.0 - 1.25 M ammonium sulfate and 0.1 M sodium acetate pH 4.0 - 5.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-03-21 
_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   1.03333 
_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                        'APS BEAMLINE 23-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03333 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B2L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               73.89 
_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                                     49981 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.21 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.58 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.3 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6245 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.34 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.918 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.27 
_refine.aniso_B[1][2]                            0.14 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.27 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.88 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               56.575 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9B2L 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             73.89 
_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                     47460 
_refine.ls_number_reflns_R_free                  2498 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21546 
_refine.ls_R_factor_R_free                       0.24148 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21407 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.193 
_refine.pdbx_overall_ESU_R_Free                  0.170 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             6.838 
_refine.overall_SU_ML                            0.158 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        73.89 
_refine_hist.number_atoms_solvent             110 
_refine_hist.number_atoms_total               4630 
_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        4516 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_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' ? 0.002  0.012  4679 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.016  4261 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.764  1.667  6345 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.258  1.587  9811 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.633  5.000  556  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.383  5.000  28   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.306 10.000 767  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.038  0.200  654  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  5586 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1126 ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.596  5.373  2218 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.594  5.374  2218 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.910  9.670  2776 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.910  9.669  2777 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.467  6.131  2461 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 6.466  6.132  2462 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 9.189  10.893 3570 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.451 57.70  5093 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.453 57.76  5073 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.200 
_refine_ls_shell.d_res_low                        2.257 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             186 
_refine_ls_shell.number_reflns_R_work             3551 
_refine_ls_shell.percent_reflns_obs               99.97 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.559 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.579 
# 
_struct.entry_id                     9B2L 
_struct.title                        'Structure of the quorum quenching lactonase GcL D122N mutant - bimetallic center' 
_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        9B2L 
_struct_keywords.text            'quorum sensing, quorum quenching, lactonase, metalloenzyme, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 2 ? 
K N N 2 ? 
L N N 5 ? 
M N N 3 ? 
N N N 6 ? 
O N N 7 ? 
P N N 8 ? 
Q N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A023DFE8_9BACI 
_struct_ref.pdbx_db_accession          A0A023DFE8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RPKLYVMDNGRMRMDKNWMIAMHNPATIHNPNAQTEFVEFPIYTVLIDHPEGKILFDTSCNPNSMGPQGRWAESTQQMFP
WTATEECYLHNRLEQLKVRPEDIRYVVASHLHLDHAGCLEMFTNATIIVHEDEFNGALQCYARNQKEGAYIWADIDAWIK
NNLQWRTVKRHEDNILLAEGVKVLNFGSGHAWGMLGLHVELPETGGIILASDAIYTAESYGPPIKPPGIIYDSLGYMNTV
ERIRRIAQETKSQVWFGHDAEQFKKFRKSTEGYYE
;
_struct_ref.pdbx_align_begin           8 
# 
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 9B2L A 1 ? 275 ? A0A023DFE8 8 ? 282 ? 9 283 
2 1 9B2L B 1 ? 275 ? A0A023DFE8 8 ? 282 ? 9 283 
# 
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 9B2L ASN A 114 ? UNP A0A023DFE8 ASP 121 'engineered mutation' 122 1 
2 9B2L ASN B 114 ? UNP A0A023DFE8 ASP 121 'engineered mutation' 122 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 4410  ? 
1 MORE         -106  ? 
1 'SSA (A^2)'  22830 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,P 
1 2 B,J,K,L,M,N,O,Q   
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000  
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 3_665 -x+y+1,-x+1,z -0.5000000000 0.8660254038 0.0000000000 54.6100000000 -0.8660254038 
-0.5000000000 0.0000000000 94.5872946013 0.0000000000 0.0000000000 1.0000000000 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 LYS A 16  ? ILE A 20  ? LYS A 24  ILE A 28  1 ? 5  
HELX_P HELX_P2  AA2 ALA A 72  ? PHE A 79  ? ALA A 80  PHE A 87  1 ? 8  
HELX_P HELX_P3  AA3 THR A 84  ? CYS A 87  ? THR A 92  CYS A 95  5 ? 4  
HELX_P HELX_P4  AA4 TYR A 88  ? GLN A 95  ? TYR A 96  GLN A 103 1 ? 8  
HELX_P HELX_P5  AA5 ARG A 99  ? GLU A 101 ? ARG A 107 GLU A 109 5 ? 3  
HELX_P HELX_P6  AA6 CYS A 118 ? PHE A 122 ? CYS A 126 PHE A 130 5 ? 5  
HELX_P HELX_P7  AA7 GLU A 131 ? ARG A 143 ? GLU A 139 ARG A 151 1 ? 13 
HELX_P HELX_P8  AA8 ILE A 151 ? ASN A 161 ? ILE A 159 ASN A 169 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 212 ? ILE A 214 ? ASP A 220 ILE A 222 5 ? 3  
HELX_P HELX_P10 AB1 THR A 216 ? GLY A 221 ? THR A 224 GLY A 229 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 232 ? THR A 250 ? ASP A 240 THR A 258 1 ? 19 
HELX_P HELX_P12 AB3 ASP A 259 ? PHE A 266 ? ASP A 267 PHE A 274 1 ? 8  
HELX_P HELX_P13 AB4 LYS B 16  ? ILE B 20  ? LYS B 24  ILE B 28  1 ? 5  
HELX_P HELX_P14 AB5 ALA B 72  ? PHE B 79  ? ALA B 80  PHE B 87  1 ? 8  
HELX_P HELX_P15 AB6 THR B 84  ? CYS B 87  ? THR B 92  CYS B 95  5 ? 4  
HELX_P HELX_P16 AB7 TYR B 88  ? GLN B 95  ? TYR B 96  GLN B 103 1 ? 8  
HELX_P HELX_P17 AB8 ARG B 99  ? GLU B 101 ? ARG B 107 GLU B 109 5 ? 3  
HELX_P HELX_P18 AB9 CYS B 118 ? PHE B 122 ? CYS B 126 PHE B 130 5 ? 5  
HELX_P HELX_P19 AC1 GLU B 131 ? ARG B 143 ? GLU B 139 ARG B 151 1 ? 13 
HELX_P HELX_P20 AC2 ILE B 151 ? ASN B 161 ? ILE B 159 ASN B 169 1 ? 11 
HELX_P HELX_P21 AC3 ASP B 212 ? ILE B 214 ? ASP B 220 ILE B 222 5 ? 3  
HELX_P HELX_P22 AC4 THR B 216 ? GLY B 221 ? THR B 224 GLY B 229 1 ? 6  
HELX_P HELX_P23 AC5 ASP B 232 ? LYS B 251 ? ASP B 240 LYS B 259 1 ? 20 
HELX_P HELX_P24 AC6 ASP B 259 ? PHE B 266 ? ASP B 267 PHE B 274 1 ? 8  
# 
_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 
metalc1  metalc ? ? A HIS 110 NE2 ? ? ? 1_555 I CO  . CO ? ? A HIS 118 A CO  307 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc2  metalc ? ? A HIS 112 ND1 ? ? ? 1_555 I CO  . CO ? ? A HIS 120 A CO  307 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc3  metalc ? ? A ASN 114 OD1 ? ? ? 1_555 H FE  . FE ? ? A ASN 122 A FE  306 1_555 ? ? ? ? ? ? ? 2.549 ? ? 
metalc4  metalc ? ? A HIS 115 NE2 ? ? ? 1_555 H FE  . FE ? ? A HIS 123 A FE  306 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc5  metalc ? ? A HIS 190 NE2 ? ? ? 1_555 I CO  . CO ? ? A HIS 198 A CO  307 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc6  metalc ? ? A ASP 212 OD2 ? ? ? 1_555 H FE  . FE ? ? A ASP 220 A FE  306 1_555 ? ? ? ? ? ? ? 2.261 ? ? 
metalc7  metalc ? ? A ASP 212 OD2 ? ? ? 1_555 I CO  . CO ? ? A ASP 220 A CO  307 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc8  metalc ? ? A HIS 258 NE2 ? ? ? 1_555 H FE  . FE ? ? A HIS 266 A FE  306 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc9  metalc ? ? H FE  .   FE  ? ? ? 1_555 P HOH . O  ? ? A FE  306 A HOH 411 1_555 ? ? ? ? ? ? ? 2.353 ? ? 
metalc10 metalc ? ? H FE  .   FE  ? ? ? 1_555 P HOH . O  ? ? A FE  306 A HOH 449 1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc11 metalc ? ? I CO  .   CO  ? ? ? 1_555 P HOH . O  ? ? A CO  307 A HOH 411 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc12 metalc ? ? I CO  .   CO  ? ? ? 1_555 P HOH . O  ? ? A CO  307 A HOH 430 1_555 ? ? ? ? ? ? ? 2.386 ? ? 
metalc13 metalc ? ? B HIS 110 NE2 ? ? ? 1_555 O CO  . CO ? ? B HIS 118 B CO  406 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc14 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 O CO  . CO ? ? B HIS 120 B CO  406 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc15 metalc ? ? B ASN 114 OD1 ? ? ? 1_555 N FE  . FE ? ? B ASN 122 B FE  405 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc16 metalc ? ? B HIS 115 NE2 ? ? ? 1_555 N FE  . FE ? ? B HIS 123 B FE  405 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
metalc17 metalc ? ? B HIS 190 NE2 ? ? ? 1_555 O CO  . CO ? ? B HIS 198 B CO  406 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc18 metalc ? ? B ASP 212 OD2 ? ? ? 1_555 N FE  . FE ? ? B ASP 220 B FE  405 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc19 metalc ? ? B ASP 212 OD2 ? ? ? 1_555 O CO  . CO ? ? B ASP 220 B CO  406 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc20 metalc ? ? B HIS 258 NE2 ? ? ? 1_555 N FE  . FE ? ? B HIS 266 B FE  405 1_555 ? ? ? ? ? ? ? 2.115 ? ? 
metalc21 metalc ? ? N FE  .   FE  ? ? ? 1_555 Q HOH . O  ? ? B FE  405 B HOH 507 1_555 ? ? ? ? ? ? ? 2.274 ? ? 
metalc22 metalc ? ? N FE  .   FE  ? ? ? 1_555 Q HOH . O  ? ? B FE  405 B HOH 551 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc23 metalc ? ? O CO  .   CO  ? ? ? 1_555 Q HOH . O  ? ? B CO  406 B HOH 507 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc24 metalc ? ? O CO  .   CO  ? ? ? 1_555 Q HOH . O  ? ? B CO  406 B HOH 531 1_555 ? ? ? ? ? ? ? 2.501 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  NE2 ? A HIS 110 ? A HIS 118 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 ND1 ? A HIS 112 ? A HIS 120 ? 1_555 86.7  ? 
2  NE2 ? A HIS 110 ? A HIS 118 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 NE2 ? A HIS 190 ? A HIS 198 ? 1_555 102.2 ? 
3  ND1 ? A HIS 112 ? A HIS 120 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 NE2 ? A HIS 190 ? A HIS 198 ? 1_555 91.8  ? 
4  NE2 ? A HIS 110 ? A HIS 118 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 94.3  ? 
5  ND1 ? A HIS 112 ? A HIS 120 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 172.4 ? 
6  NE2 ? A HIS 190 ? A HIS 198 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 95.4  ? 
7  NE2 ? A HIS 110 ? A HIS 118 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 108.5 ? 
8  ND1 ? A HIS 112 ? A HIS 120 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 91.3  ? 
9  NE2 ? A HIS 190 ? A HIS 198 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 149.3 ? 
10 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 81.3  ? 
11 NE2 ? A HIS 110 ? A HIS 118 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 430 ? 1_555 167.1 ? 
12 ND1 ? A HIS 112 ? A HIS 120 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 430 ? 1_555 95.8  ? 
13 NE2 ? A HIS 190 ? A HIS 198 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 430 ? 1_555 90.4  ? 
14 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 430 ? 1_555 81.6  ? 
15 O   ? P HOH .   ? A HOH 411 ? 1_555 CO ? I CO . ? A CO 307 ? 1_555 O   ? P HOH .   ? A HOH 430 ? 1_555 58.9  ? 
16 OD1 ? A ASN 114 ? A ASN 122 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 NE2 ? A HIS 115 ? A HIS 123 ? 1_555 88.4  ? 
17 OD1 ? A ASN 114 ? A ASN 122 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 160.6 ? 
18 NE2 ? A HIS 115 ? A HIS 123 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 94.7  ? 
19 OD1 ? A ASN 114 ? A ASN 122 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 NE2 ? A HIS 258 ? A HIS 266 ? 1_555 89.1  ? 
20 NE2 ? A HIS 115 ? A HIS 123 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 NE2 ? A HIS 258 ? A HIS 266 ? 1_555 99.3  ? 
21 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 NE2 ? A HIS 258 ? A HIS 266 ? 1_555 109.2 ? 
22 OD1 ? A ASN 114 ? A ASN 122 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 91.3  ? 
23 NE2 ? A HIS 115 ? A HIS 123 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 98.9  ? 
24 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 69.2  ? 
25 NE2 ? A HIS 258 ? A HIS 266 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 411 ? 1_555 161.8 ? 
26 OD1 ? A ASN 114 ? A ASN 122 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 449 ? 1_555 85.9  ? 
27 NE2 ? A HIS 115 ? A HIS 123 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 449 ? 1_555 165.1 ? 
28 OD2 ? A ASP 212 ? A ASP 220 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 449 ? 1_555 86.3  ? 
29 NE2 ? A HIS 258 ? A HIS 266 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 449 ? 1_555 94.4  ? 
30 O   ? P HOH .   ? A HOH 411 ? 1_555 FE ? H FE . ? A FE 306 ? 1_555 O   ? P HOH .   ? A HOH 449 ? 1_555 67.5  ? 
31 NE2 ? B HIS 110 ? B HIS 118 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 ND1 ? B HIS 112 ? B HIS 120 ? 1_555 85.3  ? 
32 NE2 ? B HIS 110 ? B HIS 118 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 NE2 ? B HIS 190 ? B HIS 198 ? 1_555 100.3 ? 
33 ND1 ? B HIS 112 ? B HIS 120 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 NE2 ? B HIS 190 ? B HIS 198 ? 1_555 91.0  ? 
34 NE2 ? B HIS 110 ? B HIS 118 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 92.7  ? 
35 ND1 ? B HIS 112 ? B HIS 120 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 173.6 ? 
36 NE2 ? B HIS 190 ? B HIS 198 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 95.3  ? 
37 NE2 ? B HIS 110 ? B HIS 118 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 111.3 ? 
38 ND1 ? B HIS 112 ? B HIS 120 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 96.9  ? 
39 NE2 ? B HIS 190 ? B HIS 198 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 147.9 ? 
40 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 78.1  ? 
41 NE2 ? B HIS 110 ? B HIS 118 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 531 ? 1_555 167.3 ? 
42 ND1 ? B HIS 112 ? B HIS 120 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 531 ? 1_555 98.4  ? 
43 NE2 ? B HIS 190 ? B HIS 198 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 531 ? 1_555 91.8  ? 
44 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 531 ? 1_555 82.3  ? 
45 O   ? Q HOH .   ? B HOH 507 ? 1_555 CO ? O CO . ? B CO 406 ? 1_555 O   ? Q HOH .   ? B HOH 531 ? 1_555 56.3  ? 
46 OD1 ? B ASN 114 ? B ASN 122 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 NE2 ? B HIS 115 ? B HIS 123 ? 1_555 85.7  ? 
47 OD1 ? B ASN 114 ? B ASN 122 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 158.7 ? 
48 NE2 ? B HIS 115 ? B HIS 123 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 94.7  ? 
49 OD1 ? B ASN 114 ? B ASN 122 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 NE2 ? B HIS 258 ? B HIS 266 ? 1_555 88.3  ? 
50 NE2 ? B HIS 115 ? B HIS 123 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 NE2 ? B HIS 258 ? B HIS 266 ? 1_555 100.3 ? 
51 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 NE2 ? B HIS 258 ? B HIS 266 ? 1_555 112.5 ? 
52 OD1 ? B ASN 114 ? B ASN 122 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 88.3  ? 
53 NE2 ? B HIS 115 ? B HIS 123 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 99.7  ? 
54 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 70.6  ? 
55 NE2 ? B HIS 258 ? B HIS 266 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 507 ? 1_555 159.4 ? 
56 OD1 ? B ASN 114 ? B ASN 122 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 551 ? 1_555 86.1  ? 
57 NE2 ? B HIS 115 ? B HIS 123 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 551 ? 1_555 162.1 ? 
58 OD2 ? B ASP 212 ? B ASP 220 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 551 ? 1_555 87.3  ? 
59 NE2 ? B HIS 258 ? B HIS 266 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 551 ? 1_555 95.3  ? 
60 O   ? Q HOH .   ? B HOH 507 ? 1_555 FE ? N FE . ? B FE 405 ? 1_555 O   ? Q HOH .   ? B HOH 551 ? 1_555 64.2  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 221 A . ? GLY 229 A PRO 222 A ? PRO 230 A 1 5.15  
2 PRO 222 A . ? PRO 230 A PRO 223 A ? PRO 231 A 1 1.80  
3 GLY 221 B . ? GLY 229 B PRO 222 B ? PRO 230 B 1 5.77  
4 PRO 222 B . ? PRO 230 B PRO 223 B ? PRO 231 B 1 -0.42 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? 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 TRP A 81  ? THR A 82  ? TRP A 89  THR A 90  
AA1 2 LYS A 3   ? ASP A 15  ? LYS A 11  ASP A 23  
AA1 3 PHE A 37  ? HIS A 49  ? PHE A 45  HIS A 57  
AA1 4 GLY A 52  ? PHE A 56  ? GLY A 60  PHE A 64  
AA1 5 ILE A 103 ? VAL A 107 ? ILE A 111 VAL A 115 
AA1 6 THR A 126 ? HIS A 130 ? THR A 134 HIS A 138 
AA1 7 GLN A 164 ? VAL A 168 ? GLN A 172 VAL A 176 
AA2 1 ILE A 175 ? ALA A 178 ? ILE A 183 ALA A 186 
AA2 2 VAL A 181 ? GLY A 187 ? VAL A 189 GLY A 195 
AA2 3 MET A 194 ? LEU A 201 ? MET A 202 LEU A 209 
AA2 4 GLY A 205 ? SER A 211 ? GLY A 213 SER A 219 
AA2 5 SER A 252 ? PHE A 256 ? SER A 260 PHE A 264 
AA3 1 TRP B 81  ? THR B 82  ? TRP B 89  THR B 90  
AA3 2 LYS B 3   ? ASP B 15  ? LYS B 11  ASP B 23  
AA3 3 PHE B 37  ? HIS B 49  ? PHE B 45  HIS B 57  
AA3 4 GLY B 52  ? PHE B 56  ? GLY B 60  PHE B 64  
AA3 5 ILE B 103 ? VAL B 107 ? ILE B 111 VAL B 115 
AA3 6 THR B 126 ? HIS B 130 ? THR B 134 HIS B 138 
AA3 7 GLN B 164 ? VAL B 168 ? GLN B 172 VAL B 176 
AA4 1 ILE B 175 ? ALA B 178 ? ILE B 183 ALA B 186 
AA4 2 VAL B 181 ? GLY B 187 ? VAL B 189 GLY B 195 
AA4 3 MET B 194 ? LEU B 201 ? MET B 202 LEU B 209 
AA4 4 GLY B 205 ? SER B 211 ? GLY B 213 SER B 219 
AA4 5 SER B 252 ? PHE B 256 ? SER B 260 PHE B 264 
# 
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 THR A 82  ? O THR A 90  N ARG A 11  ? N ARG A 19  
AA1 2 3 N TYR A 5   ? N TYR A 13  O LEU A 46  ? O LEU A 54  
AA1 3 4 N ILE A 47  ? N ILE A 55  O ILE A 54  ? O ILE A 62  
AA1 4 5 N LEU A 55  ? N LEU A 63  O VAL A 107 ? O VAL A 115 
AA1 5 6 N VAL A 106 ? N VAL A 114 O ILE A 128 ? O ILE A 136 
AA1 6 7 N ILE A 127 ? N ILE A 135 O GLN A 164 ? O GLN A 172 
AA2 1 2 N ILE A 175 ? N ILE A 183 O VAL A 183 ? O VAL A 191 
AA2 2 3 N LEU A 184 ? N LEU A 192 O GLY A 196 ? O GLY A 204 
AA2 3 4 N LEU A 201 ? N LEU A 209 O GLY A 205 ? O GLY A 213 
AA2 4 5 N ILE A 208 ? N ILE A 216 O TRP A 255 ? O TRP A 263 
AA3 1 2 O THR B 82  ? O THR B 90  N ARG B 11  ? N ARG B 19  
AA3 2 3 N TYR B 5   ? N TYR B 13  O LEU B 46  ? O LEU B 54  
AA3 3 4 N ILE B 47  ? N ILE B 55  O ILE B 54  ? O ILE B 62  
AA3 4 5 N LEU B 55  ? N LEU B 63  O VAL B 107 ? O VAL B 115 
AA3 5 6 N VAL B 106 ? N VAL B 114 O ILE B 128 ? O ILE B 136 
AA3 6 7 N ILE B 127 ? N ILE B 135 O GLN B 164 ? O GLN B 172 
AA4 1 2 N ILE B 175 ? N ILE B 183 O VAL B 183 ? O VAL B 191 
AA4 2 3 N LEU B 184 ? N LEU B 192 O GLY B 196 ? O GLY B 204 
AA4 3 4 N LEU B 201 ? N LEU B 209 O GLY B 205 ? O GLY B 213 
AA4 4 5 N ILE B 208 ? N ILE B 216 O TRP B 255 ? O TRP B 263 
# 
_pdbx_entry_details.entry_id                   9B2L 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B HOH 531 ? ? O B HOH 551 ? ? 1.97 
2 1 O A HOH 430 ? ? O A HOH 449 ? ? 2.03 
3 1 O A HOH 411 ? ? O A HOH 430 ? ? 2.18 
4 1 O B HOH 507 ? ? O B HOH 531 ? ? 2.19 
# 
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 65  ? ? 76.48   164.46  
2  1 THR A 66  ? ? -141.70 10.46   
3  1 SER A 67  ? ? 62.41   -154.76 
4  1 ASN A 71  ? ? -98.51  43.59   
5  1 SER A 219 ? ? 50.51   -134.50 
6  1 HIS A 266 ? ? -151.43 50.55   
7  1 ASP B 65  ? ? 76.09   165.08  
8  1 SER B 67  ? ? 60.36   -155.47 
9  1 ASN B 71  ? ? -99.21  31.21   
10 1 SER B 219 ? ? 52.21   -136.04 
11 1 HIS B 266 ? ? -147.40 52.02   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 151 ? ? 0.094 'SIDE CHAIN' 
2 1 ARG A 252 ? ? 0.089 'SIDE CHAIN' 
3 1 ARG A 253 ? ? 0.106 'SIDE CHAIN' 
4 1 ARG B 275 ? ? 0.096 'SIDE CHAIN' 
# 
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  
CO  CO   CO N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
FE  FE   FE N N 99  
GLN N    N  N N 100 
GLN CA   C  N S 101 
GLN C    C  N N 102 
GLN O    O  N N 103 
GLN CB   C  N N 104 
GLN CG   C  N N 105 
GLN CD   C  N N 106 
GLN OE1  O  N N 107 
GLN NE2  N  N N 108 
GLN OXT  O  N N 109 
GLN H    H  N N 110 
GLN H2   H  N N 111 
GLN HA   H  N N 112 
GLN HB2  H  N N 113 
GLN HB3  H  N N 114 
GLN HG2  H  N N 115 
GLN HG3  H  N N 116 
GLN HE21 H  N N 117 
GLN HE22 H  N N 118 
GLN HXT  H  N N 119 
GLU N    N  N N 120 
GLU CA   C  N S 121 
GLU C    C  N N 122 
GLU O    O  N N 123 
GLU CB   C  N N 124 
GLU CG   C  N N 125 
GLU CD   C  N N 126 
GLU OE1  O  N N 127 
GLU OE2  O  N N 128 
GLU OXT  O  N N 129 
GLU H    H  N N 130 
GLU H2   H  N N 131 
GLU HA   H  N N 132 
GLU HB2  H  N N 133 
GLU HB3  H  N N 134 
GLU HG2  H  N N 135 
GLU HG3  H  N N 136 
GLU HE2  H  N N 137 
GLU HXT  H  N N 138 
GLY N    N  N N 139 
GLY CA   C  N N 140 
GLY C    C  N N 141 
GLY O    O  N N 142 
GLY OXT  O  N N 143 
GLY H    H  N N 144 
GLY H2   H  N N 145 
GLY HA2  H  N N 146 
GLY HA3  H  N N 147 
GLY HXT  H  N N 148 
HIS N    N  N N 149 
HIS CA   C  N S 150 
HIS C    C  N N 151 
HIS O    O  N N 152 
HIS CB   C  N N 153 
HIS CG   C  Y N 154 
HIS ND1  N  Y N 155 
HIS CD2  C  Y N 156 
HIS CE1  C  Y N 157 
HIS NE2  N  Y N 158 
HIS OXT  O  N N 159 
HIS H    H  N N 160 
HIS H2   H  N N 161 
HIS HA   H  N N 162 
HIS HB2  H  N N 163 
HIS HB3  H  N N 164 
HIS HD1  H  N N 165 
HIS HD2  H  N N 166 
HIS HE1  H  N N 167 
HIS HE2  H  N N 168 
HIS HXT  H  N N 169 
HOH O    O  N N 170 
HOH H1   H  N N 171 
HOH H2   H  N N 172 
ILE N    N  N N 173 
ILE CA   C  N S 174 
ILE C    C  N N 175 
ILE O    O  N N 176 
ILE CB   C  N S 177 
ILE CG1  C  N N 178 
ILE CG2  C  N N 179 
ILE CD1  C  N N 180 
ILE OXT  O  N N 181 
ILE H    H  N N 182 
ILE H2   H  N N 183 
ILE HA   H  N N 184 
ILE HB   H  N N 185 
ILE HG12 H  N N 186 
ILE HG13 H  N N 187 
ILE HG21 H  N N 188 
ILE HG22 H  N N 189 
ILE HG23 H  N N 190 
ILE HD11 H  N N 191 
ILE HD12 H  N N 192 
ILE HD13 H  N N 193 
ILE HXT  H  N N 194 
LEU N    N  N N 195 
LEU CA   C  N S 196 
LEU C    C  N N 197 
LEU O    O  N N 198 
LEU CB   C  N N 199 
LEU CG   C  N N 200 
LEU CD1  C  N N 201 
LEU CD2  C  N N 202 
LEU OXT  O  N N 203 
LEU H    H  N N 204 
LEU H2   H  N N 205 
LEU HA   H  N N 206 
LEU HB2  H  N N 207 
LEU HB3  H  N N 208 
LEU HG   H  N N 209 
LEU HD11 H  N N 210 
LEU HD12 H  N N 211 
LEU HD13 H  N N 212 
LEU HD21 H  N N 213 
LEU HD22 H  N N 214 
LEU HD23 H  N N 215 
LEU HXT  H  N N 216 
LYS N    N  N N 217 
LYS CA   C  N S 218 
LYS C    C  N N 219 
LYS O    O  N N 220 
LYS CB   C  N N 221 
LYS CG   C  N N 222 
LYS CD   C  N N 223 
LYS CE   C  N N 224 
LYS NZ   N  N N 225 
LYS OXT  O  N N 226 
LYS H    H  N N 227 
LYS H2   H  N N 228 
LYS HA   H  N N 229 
LYS HB2  H  N N 230 
LYS HB3  H  N N 231 
LYS HG2  H  N N 232 
LYS HG3  H  N N 233 
LYS HD2  H  N N 234 
LYS HD3  H  N N 235 
LYS HE2  H  N N 236 
LYS HE3  H  N N 237 
LYS HZ1  H  N N 238 
LYS HZ2  H  N N 239 
LYS HZ3  H  N N 240 
LYS HXT  H  N N 241 
MET N    N  N N 242 
MET CA   C  N S 243 
MET C    C  N N 244 
MET O    O  N N 245 
MET CB   C  N N 246 
MET CG   C  N N 247 
MET SD   S  N N 248 
MET CE   C  N N 249 
MET OXT  O  N N 250 
MET H    H  N N 251 
MET H2   H  N N 252 
MET HA   H  N N 253 
MET HB2  H  N N 254 
MET HB3  H  N N 255 
MET HG2  H  N N 256 
MET HG3  H  N N 257 
MET HE1  H  N N 258 
MET HE2  H  N N 259 
MET HE3  H  N N 260 
MET HXT  H  N N 261 
PEG C1   C  N N 262 
PEG O1   O  N N 263 
PEG C2   C  N N 264 
PEG O2   O  N N 265 
PEG C3   C  N N 266 
PEG C4   C  N N 267 
PEG O4   O  N N 268 
PEG H11  H  N N 269 
PEG H12  H  N N 270 
PEG HO1  H  N N 271 
PEG H21  H  N N 272 
PEG H22  H  N N 273 
PEG H31  H  N N 274 
PEG H32  H  N N 275 
PEG H41  H  N N 276 
PEG H42  H  N N 277 
PEG HO4  H  N N 278 
PGE C1   C  N N 279 
PGE O1   O  N N 280 
PGE C2   C  N N 281 
PGE O2   O  N N 282 
PGE C3   C  N N 283 
PGE C4   C  N N 284 
PGE O4   O  N N 285 
PGE C6   C  N N 286 
PGE C5   C  N N 287 
PGE O3   O  N N 288 
PGE H1   H  N N 289 
PGE H12  H  N N 290 
PGE HO1  H  N N 291 
PGE H2   H  N N 292 
PGE H22  H  N N 293 
PGE H3   H  N N 294 
PGE H32  H  N N 295 
PGE H4   H  N N 296 
PGE H42  H  N N 297 
PGE HO4  H  N N 298 
PGE H6   H  N N 299 
PGE H62  H  N N 300 
PGE H5   H  N N 301 
PGE H52  H  N N 302 
PHE N    N  N N 303 
PHE CA   C  N S 304 
PHE C    C  N N 305 
PHE O    O  N N 306 
PHE CB   C  N N 307 
PHE CG   C  Y N 308 
PHE CD1  C  Y N 309 
PHE CD2  C  Y N 310 
PHE CE1  C  Y N 311 
PHE CE2  C  Y N 312 
PHE CZ   C  Y N 313 
PHE OXT  O  N N 314 
PHE H    H  N N 315 
PHE H2   H  N N 316 
PHE HA   H  N N 317 
PHE HB2  H  N N 318 
PHE HB3  H  N N 319 
PHE HD1  H  N N 320 
PHE HD2  H  N N 321 
PHE HE1  H  N N 322 
PHE HE2  H  N N 323 
PHE HZ   H  N N 324 
PHE HXT  H  N N 325 
PRO N    N  N N 326 
PRO CA   C  N S 327 
PRO C    C  N N 328 
PRO O    O  N N 329 
PRO CB   C  N N 330 
PRO CG   C  N N 331 
PRO CD   C  N N 332 
PRO OXT  O  N N 333 
PRO H    H  N N 334 
PRO HA   H  N N 335 
PRO HB2  H  N N 336 
PRO HB3  H  N N 337 
PRO HG2  H  N N 338 
PRO HG3  H  N N 339 
PRO HD2  H  N N 340 
PRO HD3  H  N N 341 
PRO HXT  H  N N 342 
SER N    N  N N 343 
SER CA   C  N S 344 
SER C    C  N N 345 
SER O    O  N N 346 
SER CB   C  N N 347 
SER OG   O  N N 348 
SER OXT  O  N N 349 
SER H    H  N N 350 
SER H2   H  N N 351 
SER HA   H  N N 352 
SER HB2  H  N N 353 
SER HB3  H  N N 354 
SER HG   H  N N 355 
SER HXT  H  N N 356 
SO4 S    S  N N 357 
SO4 O1   O  N N 358 
SO4 O2   O  N N 359 
SO4 O3   O  N N 360 
SO4 O4   O  N N 361 
THR N    N  N N 362 
THR CA   C  N S 363 
THR C    C  N N 364 
THR O    O  N N 365 
THR CB   C  N R 366 
THR OG1  O  N N 367 
THR CG2  C  N N 368 
THR OXT  O  N N 369 
THR H    H  N N 370 
THR H2   H  N N 371 
THR HA   H  N N 372 
THR HB   H  N N 373 
THR HG1  H  N N 374 
THR HG21 H  N N 375 
THR HG22 H  N N 376 
THR HG23 H  N N 377 
THR HXT  H  N N 378 
TRP N    N  N N 379 
TRP CA   C  N S 380 
TRP C    C  N N 381 
TRP O    O  N N 382 
TRP CB   C  N N 383 
TRP CG   C  Y N 384 
TRP CD1  C  Y N 385 
TRP CD2  C  Y N 386 
TRP NE1  N  Y N 387 
TRP CE2  C  Y N 388 
TRP CE3  C  Y N 389 
TRP CZ2  C  Y N 390 
TRP CZ3  C  Y N 391 
TRP CH2  C  Y N 392 
TRP OXT  O  N N 393 
TRP H    H  N N 394 
TRP H2   H  N N 395 
TRP HA   H  N N 396 
TRP HB2  H  N N 397 
TRP HB3  H  N N 398 
TRP HD1  H  N N 399 
TRP HE1  H  N N 400 
TRP HE3  H  N N 401 
TRP HZ2  H  N N 402 
TRP HZ3  H  N N 403 
TRP HH2  H  N N 404 
TRP HXT  H  N N 405 
TYR N    N  N N 406 
TYR CA   C  N S 407 
TYR C    C  N N 408 
TYR O    O  N N 409 
TYR CB   C  N N 410 
TYR CG   C  Y N 411 
TYR CD1  C  Y N 412 
TYR CD2  C  Y N 413 
TYR CE1  C  Y N 414 
TYR CE2  C  Y N 415 
TYR CZ   C  Y N 416 
TYR OH   O  N N 417 
TYR OXT  O  N N 418 
TYR H    H  N N 419 
TYR H2   H  N N 420 
TYR HA   H  N N 421 
TYR HB2  H  N N 422 
TYR HB3  H  N N 423 
TYR HD1  H  N N 424 
TYR HD2  H  N N 425 
TYR HE1  H  N N 426 
TYR HE2  H  N N 427 
TYR HH   H  N N 428 
TYR HXT  H  N N 429 
VAL N    N  N N 430 
VAL CA   C  N S 431 
VAL C    C  N N 432 
VAL O    O  N N 433 
VAL CB   C  N N 434 
VAL CG1  C  N N 435 
VAL CG2  C  N N 436 
VAL OXT  O  N N 437 
VAL H    H  N N 438 
VAL H2   H  N N 439 
VAL HA   H  N N 440 
VAL HB   H  N N 441 
VAL HG11 H  N N 442 
VAL HG12 H  N N 443 
VAL HG13 H  N N 444 
VAL HG21 H  N N 445 
VAL HG22 H  N N 446 
VAL HG23 H  N N 447 
VAL HXT  H  N N 448 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PGE C1  O1   sing N N 262 
PGE C1  C2   sing N N 263 
PGE C1  H1   sing N N 264 
PGE C1  H12  sing N N 265 
PGE O1  HO1  sing N N 266 
PGE C2  O2   sing N N 267 
PGE C2  H2   sing N N 268 
PGE C2  H22  sing N N 269 
PGE O2  C3   sing N N 270 
PGE C3  C4   sing N N 271 
PGE C3  H3   sing N N 272 
PGE C3  H32  sing N N 273 
PGE C4  O3   sing N N 274 
PGE C4  H4   sing N N 275 
PGE C4  H42  sing N N 276 
PGE O4  C6   sing N N 277 
PGE O4  HO4  sing N N 278 
PGE C6  C5   sing N N 279 
PGE C6  H6   sing N N 280 
PGE C6  H62  sing N N 281 
PGE C5  O3   sing N N 282 
PGE C5  H5   sing N N 283 
PGE C5  H52  sing N N 284 
PHE N   CA   sing N N 285 
PHE N   H    sing N N 286 
PHE N   H2   sing N N 287 
PHE CA  C    sing N N 288 
PHE CA  CB   sing N N 289 
PHE CA  HA   sing N N 290 
PHE C   O    doub N N 291 
PHE C   OXT  sing N N 292 
PHE CB  CG   sing N N 293 
PHE CB  HB2  sing N N 294 
PHE CB  HB3  sing N N 295 
PHE CG  CD1  doub Y N 296 
PHE CG  CD2  sing Y N 297 
PHE CD1 CE1  sing Y N 298 
PHE CD1 HD1  sing N N 299 
PHE CD2 CE2  doub Y N 300 
PHE CD2 HD2  sing N N 301 
PHE CE1 CZ   doub Y N 302 
PHE CE1 HE1  sing N N 303 
PHE CE2 CZ   sing Y N 304 
PHE CE2 HE2  sing N N 305 
PHE CZ  HZ   sing N N 306 
PHE OXT HXT  sing N N 307 
PRO N   CA   sing N N 308 
PRO N   CD   sing N N 309 
PRO N   H    sing N N 310 
PRO CA  C    sing N N 311 
PRO CA  CB   sing N N 312 
PRO CA  HA   sing N N 313 
PRO C   O    doub N N 314 
PRO C   OXT  sing N N 315 
PRO CB  CG   sing N N 316 
PRO CB  HB2  sing N N 317 
PRO CB  HB3  sing N N 318 
PRO CG  CD   sing N N 319 
PRO CG  HG2  sing N N 320 
PRO CG  HG3  sing N N 321 
PRO CD  HD2  sing N N 322 
PRO CD  HD3  sing N N 323 
PRO OXT HXT  sing N N 324 
SER N   CA   sing N N 325 
SER N   H    sing N N 326 
SER N   H2   sing N N 327 
SER CA  C    sing N N 328 
SER CA  CB   sing N N 329 
SER CA  HA   sing N N 330 
SER C   O    doub N N 331 
SER C   OXT  sing N N 332 
SER CB  OG   sing N N 333 
SER CB  HB2  sing N N 334 
SER CB  HB3  sing N N 335 
SER OG  HG   sing N N 336 
SER OXT HXT  sing N N 337 
SO4 S   O1   doub N N 338 
SO4 S   O2   doub N N 339 
SO4 S   O3   sing N N 340 
SO4 S   O4   sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM133487 
_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   6n9i 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9B2L 
_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]   0.009156 
_atom_sites.fract_transf_matrix[1][2]   0.005286 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010572 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004511 
_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  
CO 
FE 
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   . ARG A 1 1   ? 40.880 17.464  -22.856 1.00 91.52  ? 9   ARG A N   1 
ATOM   2    C  CA  . ARG A 1 1   ? 41.551 16.459  -21.988 1.00 95.99  ? 9   ARG A CA  1 
ATOM   3    C  C   . ARG A 1 1   ? 40.527 15.931  -20.978 1.00 86.22  ? 9   ARG A C   1 
ATOM   4    O  O   . ARG A 1 1   ? 39.975 14.852  -21.185 1.00 79.11  ? 9   ARG A O   1 
ATOM   5    C  CB  . ARG A 1 1   ? 42.816 17.073  -21.371 1.00 101.55 ? 9   ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 1   ? 43.983 16.102  -21.235 1.00 106.72 ? 9   ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 1   ? 45.203 16.725  -20.576 1.00 106.48 ? 9   ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 1   ? 46.241 17.080  -21.536 1.00 109.48 ? 9   ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 1   ? 46.530 18.317  -21.922 1.00 105.32 ? 9   ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 1   ? 47.489 18.524  -22.808 1.00 89.75  ? 9   ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 1   ? 45.854 19.342  -21.432 1.00 114.95 ? 9   ARG A NH2 1 
ATOM   12   N  N   . PRO A 1 2   ? 40.195 16.656  -19.882 1.00 78.23  ? 10  PRO A N   1 
ATOM   13   C  CA  . PRO A 1 2   ? 39.330 16.118  -18.831 1.00 64.04  ? 10  PRO A CA  1 
ATOM   14   C  C   . PRO A 1 2   ? 37.848 16.464  -18.978 1.00 48.79  ? 10  PRO A C   1 
ATOM   15   O  O   . PRO A 1 2   ? 37.490 17.400  -19.687 1.00 47.51  ? 10  PRO A O   1 
ATOM   16   C  CB  . PRO A 1 2   ? 39.896 16.782  -17.561 1.00 68.59  ? 10  PRO A CB  1 
ATOM   17   C  CG  . PRO A 1 2   ? 40.857 17.876  -18.047 1.00 82.63  ? 10  PRO A CG  1 
ATOM   18   C  CD  . PRO A 1 2   ? 40.647 18.009  -19.543 1.00 89.10  ? 10  PRO A CD  1 
ATOM   19   N  N   . LYS A 1 3   ? 36.996 15.692  -18.291 1.00 53.12  ? 11  LYS A N   1 
ATOM   20   C  CA  . LYS A 1 3   ? 35.568 15.965  -18.210 1.00 52.20  ? 11  LYS A CA  1 
ATOM   21   C  C   . LYS A 1 3   ? 35.149 16.022  -16.742 1.00 45.07  ? 11  LYS A C   1 
ATOM   22   O  O   . LYS A 1 3   ? 35.400 15.083  -15.991 1.00 45.44  ? 11  LYS A O   1 
ATOM   23   C  CB  . LYS A 1 3   ? 34.758 14.879  -18.928 1.00 56.32  ? 11  LYS A CB  1 
ATOM   24   C  CG  . LYS A 1 3   ? 34.709 14.963  -20.449 1.00 55.66  ? 11  LYS A CG  1 
ATOM   25   C  CD  . LYS A 1 3   ? 33.863 13.861  -21.065 1.00 62.67  ? 11  LYS A CD  1 
ATOM   26   C  CE  . LYS A 1 3   ? 33.985 13.761  -22.571 1.00 59.33  ? 11  LYS A CE  1 
ATOM   27   N  NZ  . LYS A 1 3   ? 35.319 14.199  -23.045 1.00 66.03  ? 11  LYS A NZ  1 
ATOM   28   N  N   . LEU A 1 4   ? 34.492 17.120  -16.347 1.00 49.59  ? 12  LEU A N   1 
ATOM   29   C  CA  . LEU A 1 4   ? 34.070 17.317  -14.968 1.00 49.14  ? 12  LEU A CA  1 
ATOM   30   C  C   . LEU A 1 4   ? 32.553 17.172  -14.872 1.00 42.53  ? 12  LEU A C   1 
ATOM   31   O  O   . LEU A 1 4   ? 31.819 17.814  -15.618 1.00 44.37  ? 12  LEU A O   1 
ATOM   32   C  CB  . LEU A 1 4   ? 34.539 18.700  -14.501 1.00 46.67  ? 12  LEU A CB  1 
ATOM   33   C  CG  . LEU A 1 4   ? 34.237 19.058  -13.046 1.00 48.83  ? 12  LEU A CG  1 
ATOM   34   C  CD1 . LEU A 1 4   ? 35.336 19.939  -12.471 1.00 52.28  ? 12  LEU A CD1 1 
ATOM   35   C  CD2 . LEU A 1 4   ? 32.893 19.761  -12.921 1.00 47.92  ? 12  LEU A CD2 1 
ATOM   36   N  N   . TYR A 1 5   ? 32.100 16.326  -13.936 1.00 46.75  ? 13  TYR A N   1 
ATOM   37   C  CA  . TYR A 1 5   ? 30.690 15.996  -13.802 1.00 46.01  ? 13  TYR A CA  1 
ATOM   38   C  C   . TYR A 1 5   ? 30.180 16.439  -12.431 1.00 51.99  ? 13  TYR A C   1 
ATOM   39   O  O   . TYR A 1 5   ? 30.784 16.121  -11.409 1.00 51.11  ? 13  TYR A O   1 
ATOM   40   C  CB  . TYR A 1 5   ? 30.425 14.492  -13.936 1.00 47.20  ? 13  TYR A CB  1 
ATOM   41   C  CG  . TYR A 1 5   ? 30.836 13.827  -15.244 1.00 54.44  ? 13  TYR A CG  1 
ATOM   42   C  CD1 . TYR A 1 5   ? 32.162 13.504  -15.508 1.00 56.95  ? 13  TYR A CD1 1 
ATOM   43   C  CD2 . TYR A 1 5   ? 29.887 13.498  -16.206 1.00 55.35  ? 13  TYR A CD2 1 
ATOM   44   C  CE1 . TYR A 1 5   ? 32.533 12.883  -16.690 1.00 60.15  ? 13  TYR A CE1 1 
ATOM   45   C  CE2 . TYR A 1 5   ? 30.245 12.880  -17.393 1.00 56.02  ? 13  TYR A CE2 1 
ATOM   46   C  CZ  . TYR A 1 5   ? 31.571 12.571  -17.636 1.00 54.92  ? 13  TYR A CZ  1 
ATOM   47   O  OH  . TYR A 1 5   ? 31.923 11.963  -18.806 1.00 61.96  ? 13  TYR A OH  1 
ATOM   48   N  N   . VAL A 1 6   ? 29.056 17.165  -12.429 1.00 45.59  ? 14  VAL A N   1 
ATOM   49   C  CA  . VAL A 1 6   ? 28.334 17.479  -11.207 1.00 43.88  ? 14  VAL A CA  1 
ATOM   50   C  C   . VAL A 1 6   ? 27.219 16.453  -11.023 1.00 51.88  ? 14  VAL A C   1 
ATOM   51   O  O   . VAL A 1 6   ? 26.311 16.365  -11.846 1.00 50.94  ? 14  VAL A O   1 
ATOM   52   C  CB  . VAL A 1 6   ? 27.762 18.909  -11.243 1.00 43.08  ? 14  VAL A CB  1 
ATOM   53   C  CG1 . VAL A 1 6   ? 26.934 19.211  -10.003 1.00 45.22  ? 14  VAL A CG1 1 
ATOM   54   C  CG2 . VAL A 1 6   ? 28.854 19.950  -11.425 1.00 50.10  ? 14  VAL A CG2 1 
ATOM   55   N  N   . MET A 1 7   ? 27.291 15.692  -9.926  1.00 53.15  ? 15  MET A N   1 
ATOM   56   C  CA  . MET A 1 7   ? 26.333 14.633  -9.659  1.00 49.10  ? 15  MET A CA  1 
ATOM   57   C  C   . MET A 1 7   ? 25.403 15.061  -8.525  1.00 53.52  ? 15  MET A C   1 
ATOM   58   O  O   . MET A 1 7   ? 25.861 15.415  -7.441  1.00 53.72  ? 15  MET A O   1 
ATOM   59   C  CB  . MET A 1 7   ? 27.066 13.344  -9.276  1.00 50.42  ? 15  MET A CB  1 
ATOM   60   C  CG  . MET A 1 7   ? 27.908 12.785  -10.411 1.00 49.62  ? 15  MET A CG  1 
ATOM   61   S  SD  . MET A 1 7   ? 28.824 11.289  -9.964  1.00 55.28  ? 15  MET A SD  1 
ATOM   62   C  CE  . MET A 1 7   ? 30.156 11.987  -8.988  1.00 58.55  ? 15  MET A CE  1 
ATOM   63   N  N   . ASP A 1 8   ? 24.093 15.026  -8.794  1.00 47.69  ? 16  ASP A N   1 
ATOM   64   C  CA  . ASP A 1 8   ? 23.085 15.417  -7.821  1.00 53.59  ? 16  ASP A CA  1 
ATOM   65   C  C   . ASP A 1 8   ? 22.873 14.268  -6.840  1.00 53.66  ? 16  ASP A C   1 
ATOM   66   O  O   . ASP A 1 8   ? 22.403 13.199  -7.224  1.00 58.60  ? 16  ASP A O   1 
ATOM   67   C  CB  . ASP A 1 8   ? 21.779 15.801  -8.522  1.00 52.36  ? 16  ASP A CB  1 
ATOM   68   C  CG  . ASP A 1 8   ? 20.717 16.367  -7.597  1.00 58.45  ? 16  ASP A CG  1 
ATOM   69   O  OD1 . ASP A 1 8   ? 20.902 16.284  -6.366  1.00 66.46  ? 16  ASP A OD1 1 
ATOM   70   O  OD2 . ASP A 1 8   ? 19.717 16.897  -8.121  1.00 55.96  ? 16  ASP A OD2 1 
ATOM   71   N  N   . ASN A 1 9   ? 23.214 14.500  -5.568  1.00 48.36  ? 17  ASN A N   1 
ATOM   72   C  CA  . ASN A 1 9   ? 23.178 13.441  -4.574  1.00 51.08  ? 17  ASN A CA  1 
ATOM   73   C  C   . ASN A 1 9   ? 22.098 13.738  -3.537  1.00 51.32  ? 17  ASN A C   1 
ATOM   74   O  O   . ASN A 1 9   ? 22.131 13.197  -2.435  1.00 59.71  ? 17  ASN A O   1 
ATOM   75   C  CB  . ASN A 1 9   ? 24.547 13.235  -3.920  1.00 47.47  ? 17  ASN A CB  1 
ATOM   76   C  CG  . ASN A 1 9   ? 25.630 12.906  -4.924  1.00 49.46  ? 17  ASN A CG  1 
ATOM   77   O  OD1 . ASN A 1 9   ? 26.585 13.664  -5.082  1.00 59.06  ? 17  ASN A OD1 1 
ATOM   78   N  ND2 . ASN A 1 9   ? 25.487 11.782  -5.607  1.00 55.91  ? 17  ASN A ND2 1 
ATOM   79   N  N   . GLY A 1 10  ? 21.141 14.600  -3.896  1.00 48.91  ? 18  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 10  ? 19.952 14.790  -3.082  1.00 49.55  ? 18  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 10  ? 19.844 16.197  -2.498  1.00 50.94  ? 18  GLY A C   1 
ATOM   82   O  O   . GLY A 1 10  ? 20.574 17.103  -2.894  1.00 50.86  ? 18  GLY A O   1 
ATOM   83   N  N   . ARG A 1 11  ? 18.912 16.352  -1.550  1.00 47.74  ? 19  ARG A N   1 
ATOM   84   C  CA  . ARG A 1 11  ? 18.635 17.625  -0.906  1.00 57.15  ? 19  ARG A CA  1 
ATOM   85   C  C   . ARG A 1 11  ? 18.591 17.421  0.606   1.00 57.75  ? 19  ARG A C   1 
ATOM   86   O  O   . ARG A 1 11  ? 18.247 16.341  1.084   1.00 56.28  ? 19  ARG A O   1 
ATOM   87   C  CB  . ARG A 1 11  ? 17.296 18.194  -1.389  1.00 56.86  ? 19  ARG A CB  1 
ATOM   88   C  CG  . ARG A 1 11  ? 17.179 18.348  -2.899  1.00 61.85  ? 19  ARG A CG  1 
ATOM   89   C  CD  . ARG A 1 11  ? 17.691 19.681  -3.412  1.00 75.50  ? 19  ARG A CD  1 
ATOM   90   N  NE  . ARG A 1 11  ? 17.653 19.725  -4.866  1.00 80.97  ? 19  ARG A NE  1 
ATOM   91   C  CZ  . ARG A 1 11  ? 18.497 19.076  -5.661  1.00 85.85  ? 19  ARG A CZ  1 
ATOM   92   N  NH1 . ARG A 1 11  ? 19.571 18.494  -5.155  1.00 87.21  ? 19  ARG A NH1 1 
ATOM   93   N  NH2 . ARG A 1 11  ? 18.281 19.043  -6.965  1.00 77.82  ? 19  ARG A NH2 1 
ATOM   94   N  N   . MET A 1 12  ? 18.932 18.475  1.352   1.00 60.73  ? 20  MET A N   1 
ATOM   95   C  CA  . MET A 1 12  ? 18.885 18.435  2.804   1.00 58.28  ? 20  MET A CA  1 
ATOM   96   C  C   . MET A 1 12  ? 18.270 19.740  3.305   1.00 52.86  ? 20  MET A C   1 
ATOM   97   O  O   . MET A 1 12  ? 18.403 20.777  2.659   1.00 57.37  ? 20  MET A O   1 
ATOM   98   C  CB  . MET A 1 12  ? 20.293 18.257  3.382   1.00 59.28  ? 20  MET A CB  1 
ATOM   99   C  CG  . MET A 1 12  ? 20.344 18.213  4.897   1.00 73.37  ? 20  MET A CG  1 
ATOM   100  S  SD  . MET A 1 12  ? 21.944 17.612  5.506   1.00 77.97  ? 20  MET A SD  1 
ATOM   101  C  CE  . MET A 1 12  ? 22.230 16.246  4.381   1.00 63.19  ? 20  MET A CE  1 
ATOM   102  N  N   . ARG A 1 13  ? 17.576 19.671  4.445   1.00 58.76  ? 21  ARG A N   1 
ATOM   103  C  CA  . ARG A 1 13  ? 16.971 20.846  5.052   1.00 60.95  ? 21  ARG A CA  1 
ATOM   104  C  C   . ARG A 1 13  ? 17.573 21.061  6.439   1.00 60.26  ? 21  ARG A C   1 
ATOM   105  O  O   . ARG A 1 13  ? 17.901 20.099  7.129   1.00 63.98  ? 21  ARG A O   1 
ATOM   106  C  CB  . ARG A 1 13  ? 15.449 20.684  5.130   1.00 62.31  ? 21  ARG A CB  1 
ATOM   107  C  CG  . ARG A 1 13  ? 14.718 20.989  3.830   1.00 73.17  ? 21  ARG A CG  1 
ATOM   108  C  CD  . ARG A 1 13  ? 13.303 20.440  3.802   1.00 73.09  ? 21  ARG A CD  1 
ATOM   109  N  NE  . ARG A 1 13  ? 13.260 19.003  4.038   1.00 82.78  ? 21  ARG A NE  1 
ATOM   110  C  CZ  . ARG A 1 13  ? 12.369 18.386  4.809   1.00 86.62  ? 21  ARG A CZ  1 
ATOM   111  N  NH1 . ARG A 1 13  ? 11.436 19.081  5.437   1.00 77.29  ? 21  ARG A NH1 1 
ATOM   112  N  NH2 . ARG A 1 13  ? 12.409 17.071  4.944   1.00 77.28  ? 21  ARG A NH2 1 
ATOM   113  N  N   . MET A 1 14  ? 17.723 22.332  6.833   1.00 55.02  ? 22  MET A N   1 
ATOM   114  C  CA  . MET A 1 14  ? 18.149 22.662  8.183   1.00 59.48  ? 22  MET A CA  1 
ATOM   115  C  C   . MET A 1 14  ? 17.765 24.104  8.505   1.00 57.08  ? 22  MET A C   1 
ATOM   116  O  O   . MET A 1 14  ? 17.340 24.854  7.629   1.00 50.63  ? 22  MET A O   1 
ATOM   117  C  CB  . MET A 1 14  ? 19.664 22.497  8.352   1.00 66.60  ? 22  MET A CB  1 
ATOM   118  C  CG  . MET A 1 14  ? 20.486 23.528  7.601   1.00 66.49  ? 22  MET A CG  1 
ATOM   119  S  SD  . MET A 1 14  ? 22.256 23.145  7.653   1.00 69.87  ? 22  MET A SD  1 
ATOM   120  C  CE  . MET A 1 14  ? 22.924 24.539  6.745   1.00 74.64  ? 22  MET A CE  1 
ATOM   121  N  N   . ASP A 1 15  ? 17.926 24.471  9.780   1.00 53.29  ? 23  ASP A N   1 
ATOM   122  C  CA  . ASP A 1 15  ? 17.669 25.820  10.252  1.00 53.85  ? 23  ASP A CA  1 
ATOM   123  C  C   . ASP A 1 15  ? 18.577 26.786  9.494   1.00 53.06  ? 23  ASP A C   1 
ATOM   124  O  O   . ASP A 1 15  ? 19.772 26.534  9.356   1.00 57.14  ? 23  ASP A O   1 
ATOM   125  C  CB  . ASP A 1 15  ? 17.863 25.880  11.771  1.00 55.12  ? 23  ASP A CB  1 
ATOM   126  C  CG  . ASP A 1 15  ? 17.520 27.214  12.410  1.00 53.29  ? 23  ASP A CG  1 
ATOM   127  O  OD1 . ASP A 1 15  ? 17.387 28.206  11.667  1.00 61.24  ? 23  ASP A OD1 1 
ATOM   128  O  OD2 . ASP A 1 15  ? 17.374 27.240  13.649  1.00 60.45  ? 23  ASP A OD2 1 
ATOM   129  N  N   . LYS A 1 16  ? 17.996 27.886  8.999   1.00 57.03  ? 24  LYS A N   1 
ATOM   130  C  CA  . LYS A 1 16  ? 18.727 28.849  8.190   1.00 65.13  ? 24  LYS A CA  1 
ATOM   131  C  C   . LYS A 1 16  ? 19.855 29.452  9.026   1.00 60.82  ? 24  LYS A C   1 
ATOM   132  O  O   . LYS A 1 16  ? 20.844 29.936  8.480   1.00 66.01  ? 24  LYS A O   1 
ATOM   133  C  CB  . LYS A 1 16  ? 17.774 29.929  7.663   1.00 60.69  ? 24  LYS A CB  1 
ATOM   134  C  CG  . LYS A 1 16  ? 18.116 30.513  6.296   1.00 77.84  ? 24  LYS A CG  1 
ATOM   135  C  CD  . LYS A 1 16  ? 18.926 31.794  6.336   1.00 99.55  ? 24  LYS A CD  1 
ATOM   136  C  CE  . LYS A 1 16  ? 18.759 32.630  5.082   1.00 107.40 ? 24  LYS A CE  1 
ATOM   137  N  NZ  . LYS A 1 16  ? 19.122 34.049  5.312   1.00 118.65 ? 24  LYS A NZ  1 
ATOM   138  N  N   . ASN A 1 17  ? 19.698 29.408  10.354  1.00 60.51  ? 25  ASN A N   1 
ATOM   139  C  CA  . ASN A 1 17  ? 20.677 29.983  11.263  1.00 65.36  ? 25  ASN A CA  1 
ATOM   140  C  C   . ASN A 1 17  ? 21.961 29.156  11.239  1.00 57.23  ? 25  ASN A C   1 
ATOM   141  O  O   . ASN A 1 17  ? 23.025 29.665  11.581  1.00 62.85  ? 25  ASN A O   1 
ATOM   142  C  CB  . ASN A 1 17  ? 20.128 30.128  12.686  1.00 70.90  ? 25  ASN A CB  1 
ATOM   143  C  CG  . ASN A 1 17  ? 19.179 31.298  12.844  1.00 69.89  ? 25  ASN A CG  1 
ATOM   144  O  OD1 . ASN A 1 17  ? 18.037 31.125  13.265  1.00 80.88  ? 25  ASN A OD1 1 
ATOM   145  N  ND2 . ASN A 1 17  ? 19.645 32.494  12.523  1.00 61.57  ? 25  ASN A ND2 1 
ATOM   146  N  N   . TRP A 1 18  ? 21.861 27.882  10.839  1.00 55.80  ? 26  TRP A N   1 
ATOM   147  C  CA  . TRP A 1 18  ? 23.044 27.067  10.615  1.00 65.20  ? 26  TRP A CA  1 
ATOM   148  C  C   . TRP A 1 18  ? 23.822 27.622  9.424   1.00 70.71  ? 26  TRP A C   1 
ATOM   149  O  O   . TRP A 1 18  ? 25.048 27.698  9.459   1.00 61.09  ? 26  TRP A O   1 
ATOM   150  C  CB  . TRP A 1 18  ? 22.687 25.594  10.362  1.00 63.32  ? 26  TRP A CB  1 
ATOM   151  C  CG  . TRP A 1 18  ? 22.159 24.825  11.546  1.00 70.07  ? 26  TRP A CG  1 
ATOM   152  C  CD1 . TRP A 1 18  ? 20.965 24.169  11.602  1.00 70.38  ? 26  TRP A CD1 1 
ATOM   153  C  CD2 . TRP A 1 18  ? 22.806 24.584  12.817  1.00 70.72  ? 26  TRP A CD2 1 
ATOM   154  N  NE1 . TRP A 1 18  ? 20.812 23.554  12.814  1.00 72.71  ? 26  TRP A NE1 1 
ATOM   155  C  CE2 . TRP A 1 18  ? 21.923 23.787  13.580  1.00 78.18  ? 26  TRP A CE2 1 
ATOM   156  C  CE3 . TRP A 1 18  ? 24.028 24.962  13.387  1.00 74.87  ? 26  TRP A CE3 1 
ATOM   157  C  CZ2 . TRP A 1 18  ? 22.226 23.368  14.873  1.00 77.44  ? 26  TRP A CZ2 1 
ATOM   158  C  CZ3 . TRP A 1 18  ? 24.326 24.543  14.665  1.00 74.66  ? 26  TRP A CZ3 1 
ATOM   159  C  CH2 . TRP A 1 18  ? 23.437 23.756  15.396  1.00 80.01  ? 26  TRP A CH2 1 
ATOM   160  N  N   . MET A 1 19  ? 23.089 27.991  8.366   1.00 66.38  ? 27  MET A N   1 
ATOM   161  C  CA  . MET A 1 19  ? 23.689 28.461  7.127   1.00 65.63  ? 27  MET A CA  1 
ATOM   162  C  C   . MET A 1 19  ? 24.166 29.901  7.286   1.00 63.86  ? 27  MET A C   1 
ATOM   163  O  O   . MET A 1 19  ? 25.273 30.241  6.873   1.00 64.66  ? 27  MET A O   1 
ATOM   164  C  CB  . MET A 1 19  ? 22.683 28.387  5.975   1.00 76.27  ? 27  MET A CB  1 
ATOM   165  C  CG  . MET A 1 19  ? 23.199 27.654  4.754   1.00 79.59  ? 27  MET A CG  1 
ATOM   166  S  SD  . MET A 1 19  ? 21.846 27.206  3.641   1.00 97.14  ? 27  MET A SD  1 
ATOM   167  C  CE  . MET A 1 19  ? 21.071 28.808  3.424   1.00 90.23  ? 27  MET A CE  1 
ATOM   168  N  N   . ILE A 1 20  ? 23.309 30.741  7.874   1.00 58.00  ? 28  ILE A N   1 
ATOM   169  C  CA  . ILE A 1 20  ? 23.616 32.145  8.090   1.00 60.63  ? 28  ILE A CA  1 
ATOM   170  C  C   . ILE A 1 20  ? 23.360 32.475  9.559   1.00 69.22  ? 28  ILE A C   1 
ATOM   171  O  O   . ILE A 1 20  ? 22.218 32.696  9.952   1.00 68.64  ? 28  ILE A O   1 
ATOM   172  C  CB  . ILE A 1 20  ? 22.770 33.036  7.158   1.00 65.94  ? 28  ILE A CB  1 
ATOM   173  C  CG1 . ILE A 1 20  ? 22.921 32.645  5.685   1.00 66.43  ? 28  ILE A CG1 1 
ATOM   174  C  CG2 . ILE A 1 20  ? 23.083 34.507  7.386   1.00 65.70  ? 28  ILE A CG2 1 
ATOM   175  C  CD1 . ILE A 1 20  ? 24.266 32.988  5.085   1.00 62.37  ? 28  ILE A CD1 1 
ATOM   176  N  N   . ALA A 1 21  ? 24.428 32.502  10.364  1.00 65.93  ? 29  ALA A N   1 
ATOM   177  C  CA  . ALA A 1 21  ? 24.302 32.739  11.793  1.00 70.10  ? 29  ALA A CA  1 
ATOM   178  C  C   . ALA A 1 21  ? 23.552 34.047  12.042  1.00 70.05  ? 29  ALA A C   1 
ATOM   179  O  O   . ALA A 1 21  ? 23.894 35.081  11.473  1.00 62.61  ? 29  ALA A O   1 
ATOM   180  C  CB  . ALA A 1 21  ? 25.670 32.754  12.435  1.00 66.01  ? 29  ALA A CB  1 
ATOM   181  N  N   . MET A 1 22  ? 22.519 33.974  12.893  1.00 63.49  ? 30  MET A N   1 
ATOM   182  C  CA  . MET A 1 22  ? 21.768 35.139  13.339  1.00 63.74  ? 30  MET A CA  1 
ATOM   183  C  C   . MET A 1 22  ? 21.193 35.885  12.136  1.00 61.55  ? 30  MET A C   1 
ATOM   184  O  O   . MET A 1 22  ? 21.438 37.078  11.971  1.00 68.26  ? 30  MET A O   1 
ATOM   185  C  CB  . MET A 1 22  ? 22.665 36.094  14.136  1.00 70.18  ? 30  MET A CB  1 
ATOM   186  C  CG  . MET A 1 22  ? 23.217 35.487  15.415  1.00 73.09  ? 30  MET A CG  1 
ATOM   187  S  SD  . MET A 1 22  ? 21.936 34.847  16.526  1.00 71.66  ? 30  MET A SD  1 
ATOM   188  C  CE  . MET A 1 22  ? 20.763 36.201  16.511  1.00 68.65  ? 30  MET A CE  1 
ATOM   189  N  N   . HIS A 1 23  ? 20.408 35.177  11.314  1.00 65.09  ? 31  HIS A N   1 
ATOM   190  C  CA  . HIS A 1 23  ? 19.960 35.706  10.034  1.00 71.76  ? 31  HIS A CA  1 
ATOM   191  C  C   . HIS A 1 23  ? 18.776 36.651  10.222  1.00 68.89  ? 31  HIS A C   1 
ATOM   192  O  O   . HIS A 1 23  ? 18.549 37.529  9.393   1.00 77.15  ? 31  HIS A O   1 
ATOM   193  C  CB  . HIS A 1 23  ? 19.605 34.581  9.054   1.00 73.67  ? 31  HIS A CB  1 
ATOM   194  C  CG  . HIS A 1 23  ? 18.257 33.966  9.260   1.00 84.61  ? 31  HIS A CG  1 
ATOM   195  N  ND1 . HIS A 1 23  ? 17.159 34.336  8.514   1.00 81.00  ? 31  HIS A ND1 1 
ATOM   196  C  CD2 . HIS A 1 23  ? 17.823 33.030  10.115  1.00 83.86  ? 31  HIS A CD2 1 
ATOM   197  C  CE1 . HIS A 1 23  ? 16.104 33.637  8.909   1.00 85.17  ? 31  HIS A CE1 1 
ATOM   198  N  NE2 . HIS A 1 23  ? 16.486 32.835  9.879   1.00 87.53  ? 31  HIS A NE2 1 
ATOM   199  N  N   . ASN A 1 24  ? 18.022 36.460  11.310  1.00 70.47  ? 32  ASN A N   1 
ATOM   200  C  CA  . ASN A 1 24  ? 16.814 37.233  11.550  1.00 79.66  ? 32  ASN A CA  1 
ATOM   201  C  C   . ASN A 1 24  ? 16.633 37.430  13.053  1.00 78.27  ? 32  ASN A C   1 
ATOM   202  O  O   . ASN A 1 24  ? 15.816 36.752  13.674  1.00 67.20  ? 32  ASN A O   1 
ATOM   203  C  CB  . ASN A 1 24  ? 15.590 36.555  10.928  1.00 83.04  ? 32  ASN A CB  1 
ATOM   204  C  CG  . ASN A 1 24  ? 14.298 37.301  11.185  1.00 75.92  ? 32  ASN A CG  1 
ATOM   205  O  OD1 . ASN A 1 24  ? 14.214 38.504  10.950  1.00 82.76  ? 32  ASN A OD1 1 
ATOM   206  N  ND2 . ASN A 1 24  ? 13.289 36.597  11.674  1.00 74.34  ? 32  ASN A ND2 1 
ATOM   207  N  N   . PRO A 1 25  ? 17.385 38.356  13.691  1.00 68.90  ? 33  PRO A N   1 
ATOM   208  C  CA  . PRO A 1 25  ? 17.357 38.490  15.147  1.00 69.39  ? 33  PRO A CA  1 
ATOM   209  C  C   . PRO A 1 25  ? 16.020 39.007  15.674  1.00 64.70  ? 33  PRO A C   1 
ATOM   210  O  O   . PRO A 1 25  ? 15.335 39.780  15.008  1.00 60.40  ? 33  PRO A O   1 
ATOM   211  C  CB  . PRO A 1 25  ? 18.497 39.478  15.452  1.00 69.35  ? 33  PRO A CB  1 
ATOM   212  C  CG  . PRO A 1 25  ? 19.328 39.513  14.179  1.00 70.69  ? 33  PRO A CG  1 
ATOM   213  C  CD  . PRO A 1 25  ? 18.330 39.292  13.063  1.00 68.54  ? 33  PRO A CD  1 
ATOM   214  N  N   . ALA A 1 26  ? 15.663 38.549  16.879  1.00 64.45  ? 34  ALA A N   1 
ATOM   215  C  CA  . ALA A 1 26  ? 14.461 38.995  17.560  1.00 68.93  ? 34  ALA A CA  1 
ATOM   216  C  C   . ALA A 1 26  ? 14.601 40.472  17.914  1.00 68.09  ? 34  ALA A C   1 
ATOM   217  O  O   . ALA A 1 26  ? 15.707 40.957  18.140  1.00 62.91  ? 34  ALA A O   1 
ATOM   218  C  CB  . ALA A 1 26  ? 14.229 38.152  18.790  1.00 64.63  ? 34  ALA A CB  1 
ATOM   219  N  N   . THR A 1 27  ? 13.465 41.176  17.949  1.00 62.19  ? 35  THR A N   1 
ATOM   220  C  CA  . THR A 1 27  ? 13.440 42.588  18.291  1.00 65.73  ? 35  THR A CA  1 
ATOM   221  C  C   . THR A 1 27  ? 12.358 42.827  19.338  1.00 66.35  ? 35  THR A C   1 
ATOM   222  O  O   . THR A 1 27  ? 11.618 41.911  19.691  1.00 54.32  ? 35  THR A O   1 
ATOM   223  C  CB  . THR A 1 27  ? 13.216 43.454  17.044  1.00 71.46  ? 35  THR A CB  1 
ATOM   224  O  OG1 . THR A 1 27  ? 12.031 42.993  16.394  1.00 82.48  ? 35  THR A OG1 1 
ATOM   225  C  CG2 . THR A 1 27  ? 14.380 43.408  16.079  1.00 75.18  ? 35  THR A CG2 1 
ATOM   226  N  N   . ILE A 1 28  ? 12.279 44.068  19.829  1.00 71.81  ? 36  ILE A N   1 
ATOM   227  C  CA  . ILE A 1 28  ? 11.266 44.440  20.801  1.00 82.03  ? 36  ILE A CA  1 
ATOM   228  C  C   . ILE A 1 28  ? 9.892  44.178  20.187  1.00 84.13  ? 36  ILE A C   1 
ATOM   229  O  O   . ILE A 1 28  ? 8.936  43.885  20.902  1.00 77.77  ? 36  ILE A O   1 
ATOM   230  C  CB  . ILE A 1 28  ? 11.442 45.909  21.241  1.00 90.49  ? 36  ILE A CB  1 
ATOM   231  C  CG1 . ILE A 1 28  ? 10.949 46.144  22.671  1.00 99.52  ? 36  ILE A CG1 1 
ATOM   232  C  CG2 . ILE A 1 28  ? 10.782 46.856  20.250  1.00 90.99  ? 36  ILE A CG2 1 
ATOM   233  C  CD1 . ILE A 1 28  ? 11.247 47.528  23.204  1.00 101.24 ? 36  ILE A CD1 1 
ATOM   234  N  N   . HIS A 1 29  ? 9.813  44.258  18.852  1.00 83.34  ? 37  HIS A N   1 
ATOM   235  C  CA  . HIS A 1 29  ? 8.547  44.136  18.145  1.00 84.32  ? 37  HIS A CA  1 
ATOM   236  C  C   . HIS A 1 29  ? 8.357  42.713  17.618  1.00 83.89  ? 37  HIS A C   1 
ATOM   237  O  O   . HIS A 1 29  ? 7.236  42.314  17.313  1.00 76.17  ? 37  HIS A O   1 
ATOM   238  C  CB  . HIS A 1 29  ? 8.437  45.202  17.048  1.00 90.84  ? 37  HIS A CB  1 
ATOM   239  C  CG  . HIS A 1 29  ? 8.135  46.565  17.582  1.00 116.59 ? 37  HIS A CG  1 
ATOM   240  N  ND1 . HIS A 1 29  ? 9.014  47.624  17.503  1.00 125.96 ? 37  HIS A ND1 1 
ATOM   241  C  CD2 . HIS A 1 29  ? 7.052  47.031  18.219  1.00 115.18 ? 37  HIS A CD2 1 
ATOM   242  C  CE1 . HIS A 1 29  ? 8.467  48.690  18.070  1.00 117.43 ? 37  HIS A CE1 1 
ATOM   243  N  NE2 . HIS A 1 29  ? 7.274  48.352  18.510  1.00 120.37 ? 37  HIS A NE2 1 
ATOM   244  N  N   . ASN A 1 30  ? 9.453  41.954  17.510  1.00 80.90  ? 38  ASN A N   1 
ATOM   245  C  CA  . ASN A 1 30  ? 9.371  40.549  17.141  1.00 73.10  ? 38  ASN A CA  1 
ATOM   246  C  C   . ASN A 1 30  ? 10.188 39.734  18.142  1.00 71.03  ? 38  ASN A C   1 
ATOM   247  O  O   . ASN A 1 30  ? 11.232 39.183  17.801  1.00 63.64  ? 38  ASN A O   1 
ATOM   248  C  CB  . ASN A 1 30  ? 9.823  40.306  15.697  1.00 74.45  ? 38  ASN A CB  1 
ATOM   249  C  CG  . ASN A 1 30  ? 9.461  38.929  15.178  1.00 74.33  ? 38  ASN A CG  1 
ATOM   250  O  OD1 . ASN A 1 30  ? 9.915  38.528  14.108  1.00 75.04  ? 38  ASN A OD1 1 
ATOM   251  N  ND2 . ASN A 1 30  ? 8.650  38.197  15.925  1.00 74.94  ? 38  ASN A ND2 1 
ATOM   252  N  N   . PRO A 1 31  ? 9.723  39.628  19.407  1.00 76.14  ? 39  PRO A N   1 
ATOM   253  C  CA  . PRO A 1 31  ? 10.490 38.972  20.469  1.00 71.71  ? 39  PRO A CA  1 
ATOM   254  C  C   . PRO A 1 31  ? 10.650 37.463  20.300  1.00 70.07  ? 39  PRO A C   1 
ATOM   255  O  O   . PRO A 1 31  ? 11.559 36.866  20.872  1.00 70.04  ? 39  PRO A O   1 
ATOM   256  C  CB  . PRO A 1 31  ? 9.656  39.265  21.727  1.00 79.04  ? 39  PRO A CB  1 
ATOM   257  C  CG  . PRO A 1 31  ? 8.246  39.415  21.201  1.00 71.10  ? 39  PRO A CG  1 
ATOM   258  C  CD  . PRO A 1 31  ? 8.424  40.133  19.880  1.00 77.46  ? 39  PRO A CD  1 
ATOM   259  N  N   . ASN A 1 32  ? 9.752  36.852  19.522  1.00 60.58  ? 40  ASN A N   1 
ATOM   260  C  CA  . ASN A 1 32  ? 9.789  35.416  19.306  1.00 70.38  ? 40  ASN A CA  1 
ATOM   261  C  C   . ASN A 1 32  ? 10.044 35.146  17.827  1.00 67.88  ? 40  ASN A C   1 
ATOM   262  O  O   . ASN A 1 32  ? 9.444  34.248  17.239  1.00 70.24  ? 40  ASN A O   1 
ATOM   263  C  CB  . ASN A 1 32  ? 8.510  34.748  19.816  1.00 72.66  ? 40  ASN A CB  1 
ATOM   264  C  CG  . ASN A 1 32  ? 8.226  35.077  21.266  1.00 77.61  ? 40  ASN A CG  1 
ATOM   265  O  OD1 . ASN A 1 32  ? 8.983  34.691  22.154  1.00 75.76  ? 40  ASN A OD1 1 
ATOM   266  N  ND2 . ASN A 1 32  ? 7.142  35.794  21.514  1.00 75.37  ? 40  ASN A ND2 1 
ATOM   267  N  N   . ALA A 1 33  ? 10.954 35.936  17.244  1.00 65.06  ? 41  ALA A N   1 
ATOM   268  C  CA  . ALA A 1 33  ? 11.299 35.820  15.837  1.00 67.96  ? 41  ALA A CA  1 
ATOM   269  C  C   . ALA A 1 33  ? 11.477 34.349  15.468  1.00 59.04  ? 41  ALA A C   1 
ATOM   270  O  O   . ALA A 1 33  ? 12.030 33.567  16.239  1.00 65.66  ? 41  ALA A O   1 
ATOM   271  C  CB  . ALA A 1 33  ? 12.540 36.626  15.542  1.00 70.21  ? 41  ALA A CB  1 
ATOM   272  N  N   . GLN A 1 34  ? 10.993 33.996  14.273  1.00 65.18  ? 42  GLN A N   1 
ATOM   273  C  CA  . GLN A 1 34  ? 11.002 32.627  13.785  1.00 74.31  ? 42  GLN A CA  1 
ATOM   274  C  C   . GLN A 1 34  ? 12.175 32.418  12.834  1.00 62.43  ? 42  GLN A C   1 
ATOM   275  O  O   . GLN A 1 34  ? 12.531 33.321  12.079  1.00 57.80  ? 42  GLN A O   1 
ATOM   276  C  CB  . GLN A 1 34  ? 9.702  32.328  13.036  1.00 84.58  ? 42  GLN A CB  1 
ATOM   277  C  CG  . GLN A 1 34  ? 8.532  31.995  13.948  1.00 88.53  ? 42  GLN A CG  1 
ATOM   278  C  CD  . GLN A 1 34  ? 7.216  31.979  13.210  1.00 86.09  ? 42  GLN A CD  1 
ATOM   279  O  OE1 . GLN A 1 34  ? 7.167  31.978  11.982  1.00 85.84  ? 42  GLN A OE1 1 
ATOM   280  N  NE2 . GLN A 1 34  ? 6.132  31.959  13.967  1.00 81.83  ? 42  GLN A NE2 1 
ATOM   281  N  N   . THR A 1 35  ? 12.757 31.215  12.865  1.00 61.25  ? 43  THR A N   1 
ATOM   282  C  CA  . THR A 1 35  ? 13.690 30.818  11.824  1.00 71.99  ? 43  THR A CA  1 
ATOM   283  C  C   . THR A 1 35  ? 12.929 30.060  10.739  1.00 73.48  ? 43  THR A C   1 
ATOM   284  O  O   . THR A 1 35  ? 11.760 29.722  10.911  1.00 69.69  ? 43  THR A O   1 
ATOM   285  C  CB  . THR A 1 35  ? 14.859 29.988  12.372  1.00 62.49  ? 43  THR A CB  1 
ATOM   286  O  OG1 . THR A 1 35  ? 15.795 29.834  11.304  1.00 67.43  ? 43  THR A OG1 1 
ATOM   287  C  CG2 . THR A 1 35  ? 14.448 28.630  12.897  1.00 58.92  ? 43  THR A CG2 1 
ATOM   288  N  N   . GLU A 1 36  ? 13.612 29.818  9.616   1.00 74.09  ? 44  GLU A N   1 
ATOM   289  C  CA  . GLU A 1 36  ? 13.070 29.016  8.533   1.00 74.28  ? 44  GLU A CA  1 
ATOM   290  C  C   . GLU A 1 36  ? 13.869 27.720  8.431   1.00 64.71  ? 44  GLU A C   1 
ATOM   291  O  O   . GLU A 1 36  ? 14.968 27.613  8.970   1.00 62.85  ? 44  GLU A O   1 
ATOM   292  C  CB  . GLU A 1 36  ? 13.150 29.754  7.195   1.00 73.76  ? 44  GLU A CB  1 
ATOM   293  C  CG  . GLU A 1 36  ? 12.904 31.248  7.286   1.00 85.06  ? 44  GLU A CG  1 
ATOM   294  C  CD  . GLU A 1 36  ? 13.529 32.032  6.144   1.00 102.79 ? 44  GLU A CD  1 
ATOM   295  O  OE1 . GLU A 1 36  ? 13.358 31.613  4.980   1.00 100.42 ? 44  GLU A OE1 1 
ATOM   296  O  OE2 . GLU A 1 36  ? 14.181 33.060  6.421   1.00 98.70  ? 44  GLU A OE2 1 
ATOM   297  N  N   . PHE A 1 37  ? 13.298 26.752  7.709   1.00 65.57  ? 45  PHE A N   1 
ATOM   298  C  CA  . PHE A 1 37  ? 13.887 25.437  7.524   1.00 58.96  ? 45  PHE A CA  1 
ATOM   299  C  C   . PHE A 1 37  ? 14.154 25.252  6.030   1.00 66.56  ? 45  PHE A C   1 
ATOM   300  O  O   . PHE A 1 37  ? 13.262 24.837  5.292   1.00 68.35  ? 45  PHE A O   1 
ATOM   301  C  CB  . PHE A 1 37  ? 12.924 24.402  8.116   1.00 56.44  ? 45  PHE A CB  1 
ATOM   302  C  CG  . PHE A 1 37  ? 13.489 23.043  8.448   1.00 61.04  ? 45  PHE A CG  1 
ATOM   303  C  CD1 . PHE A 1 37  ? 14.527 22.896  9.354   1.00 65.76  ? 45  PHE A CD1 1 
ATOM   304  C  CD2 . PHE A 1 37  ? 12.933 21.900  7.895   1.00 62.42  ? 45  PHE A CD2 1 
ATOM   305  C  CE1 . PHE A 1 37  ? 15.021 21.639  9.669   1.00 68.03  ? 45  PHE A CE1 1 
ATOM   306  C  CE2 . PHE A 1 37  ? 13.428 20.645  8.211   1.00 65.11  ? 45  PHE A CE2 1 
ATOM   307  C  CZ  . PHE A 1 37  ? 14.471 20.516  9.097   1.00 68.69  ? 45  PHE A CZ  1 
ATOM   308  N  N   . VAL A 1 38  ? 15.377 25.585  5.589   1.00 71.14  ? 46  VAL A N   1 
ATOM   309  C  CA  . VAL A 1 38  ? 15.665 25.775  4.173   1.00 71.36  ? 46  VAL A CA  1 
ATOM   310  C  C   . VAL A 1 38  ? 16.208 24.486  3.558   1.00 65.72  ? 46  VAL A C   1 
ATOM   311  O  O   . VAL A 1 38  ? 16.807 23.660  4.244   1.00 61.80  ? 46  VAL A O   1 
ATOM   312  C  CB  . VAL A 1 38  ? 16.639 26.949  3.933   1.00 80.57  ? 46  VAL A CB  1 
ATOM   313  C  CG1 . VAL A 1 38  ? 16.028 28.285  4.330   1.00 92.51  ? 46  VAL A CG1 1 
ATOM   314  C  CG2 . VAL A 1 38  ? 17.977 26.745  4.629   1.00 85.29  ? 46  VAL A CG2 1 
ATOM   315  N  N   . GLU A 1 39  ? 15.994 24.352  2.242   1.00 63.24  ? 47  GLU A N   1 
ATOM   316  C  CA  . GLU A 1 39  ? 16.440 23.211  1.459   1.00 64.53  ? 47  GLU A CA  1 
ATOM   317  C  C   . GLU A 1 39  ? 17.713 23.590  0.706   1.00 60.19  ? 47  GLU A C   1 
ATOM   318  O  O   . GLU A 1 39  ? 17.821 24.699  0.188   1.00 54.97  ? 47  GLU A O   1 
ATOM   319  C  CB  . GLU A 1 39  ? 15.331 22.800  0.487   1.00 74.09  ? 47  GLU A CB  1 
ATOM   320  C  CG  . GLU A 1 39  ? 15.639 21.554  -0.326  1.00 87.45  ? 47  GLU A CG  1 
ATOM   321  C  CD  . GLU A 1 39  ? 14.416 20.897  -0.946  1.00 93.00  ? 47  GLU A CD  1 
ATOM   322  O  OE1 . GLU A 1 39  ? 14.329 20.863  -2.190  1.00 96.36  ? 47  GLU A OE1 1 
ATOM   323  O  OE2 . GLU A 1 39  ? 13.557 20.414  -0.181  1.00 94.24  ? 47  GLU A OE2 1 
ATOM   324  N  N   . PHE A 1 40  ? 18.676 22.666  0.645   1.00 59.00  ? 48  PHE A N   1 
ATOM   325  C  CA  . PHE A 1 40  ? 19.918 22.930  -0.062  1.00 59.65  ? 48  PHE A CA  1 
ATOM   326  C  C   . PHE A 1 40  ? 20.431 21.640  -0.695  1.00 52.17  ? 48  PHE A C   1 
ATOM   327  O  O   . PHE A 1 40  ? 20.189 20.547  -0.190  1.00 50.72  ? 48  PHE A O   1 
ATOM   328  C  CB  . PHE A 1 40  ? 20.938 23.584  0.875   1.00 54.48  ? 48  PHE A CB  1 
ATOM   329  C  CG  . PHE A 1 40  ? 21.284 22.773  2.096   1.00 56.34  ? 48  PHE A CG  1 
ATOM   330  C  CD1 . PHE A 1 40  ? 22.275 21.805  2.050   1.00 58.92  ? 48  PHE A CD1 1 
ATOM   331  C  CD2 . PHE A 1 40  ? 20.599 22.960  3.285   1.00 64.23  ? 48  PHE A CD2 1 
ATOM   332  C  CE1 . PHE A 1 40  ? 22.588 21.058  3.175   1.00 63.36  ? 48  PHE A CE1 1 
ATOM   333  C  CE2 . PHE A 1 40  ? 20.909 22.207  4.407   1.00 65.29  ? 48  PHE A CE2 1 
ATOM   334  C  CZ  . PHE A 1 40  ? 21.902 21.258  4.350   1.00 68.68  ? 48  PHE A CZ  1 
ATOM   335  N  N   . PRO A 1 41  ? 21.140 21.744  -1.840  1.00 49.63  ? 49  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 41  ? 21.629 20.574  -2.565  1.00 47.37  ? 49  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 41  ? 22.848 19.911  -1.934  1.00 50.80  ? 49  PRO A C   1 
ATOM   338  O  O   . PRO A 1 41  ? 23.704 20.579  -1.360  1.00 54.00  ? 49  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 41  ? 22.045 21.159  -3.921  1.00 48.48  ? 49  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 41  ? 22.465 22.572  -3.583  1.00 54.28  ? 49  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 41  ? 21.492 23.007  -2.506  1.00 48.14  ? 49  PRO A CD  1 
ATOM   342  N  N   . ILE A 1 42  ? 22.900 18.585  -2.065  1.00 49.96  ? 50  ILE A N   1 
ATOM   343  C  CA  . ILE A 1 42  ? 24.092 17.814  -1.768  1.00 49.74  ? 50  ILE A CA  1 
ATOM   344  C  C   . ILE A 1 42  ? 24.636 17.300  -3.096  1.00 53.04  ? 50  ILE A C   1 
ATOM   345  O  O   . ILE A 1 42  ? 23.921 16.623  -3.830  1.00 57.88  ? 50  ILE A O   1 
ATOM   346  C  CB  . ILE A 1 42  ? 23.771 16.651  -0.809  1.00 49.06  ? 50  ILE A CB  1 
ATOM   347  C  CG1 . ILE A 1 42  ? 22.926 17.100  0.386   1.00 55.20  ? 50  ILE A CG1 1 
ATOM   348  C  CG2 . ILE A 1 42  ? 25.048 15.950  -0.374  1.00 53.91  ? 50  ILE A CG2 1 
ATOM   349  C  CD1 . ILE A 1 42  ? 23.576 18.164  1.237   1.00 60.32  ? 50  ILE A CD1 1 
ATOM   350  N  N   . TYR A 1 43  ? 25.892 17.629  -3.410  1.00 55.26  ? 51  TYR A N   1 
ATOM   351  C  CA  . TYR A 1 43  ? 26.449 17.208  -4.682  1.00 51.91  ? 51  TYR A CA  1 
ATOM   352  C  C   . TYR A 1 43  ? 27.906 16.787  -4.521  1.00 45.83  ? 51  TYR A C   1 
ATOM   353  O  O   . TYR A 1 43  ? 28.560 17.095  -3.528  1.00 47.70  ? 51  TYR A O   1 
ATOM   354  C  CB  . TYR A 1 43  ? 26.273 18.279  -5.764  1.00 46.35  ? 51  TYR A CB  1 
ATOM   355  C  CG  . TYR A 1 43  ? 27.136 19.533  -5.671  1.00 49.70  ? 51  TYR A CG  1 
ATOM   356  C  CD1 . TYR A 1 43  ? 26.799 20.587  -4.830  1.00 49.93  ? 51  TYR A CD1 1 
ATOM   357  C  CD2 . TYR A 1 43  ? 28.271 19.674  -6.459  1.00 55.11  ? 51  TYR A CD2 1 
ATOM   358  C  CE1 . TYR A 1 43  ? 27.572 21.736  -4.769  1.00 46.92  ? 51  TYR A CE1 1 
ATOM   359  C  CE2 . TYR A 1 43  ? 29.053 20.815  -6.405  1.00 51.69  ? 51  TYR A CE2 1 
ATOM   360  C  CZ  . TYR A 1 43  ? 28.704 21.849  -5.557  1.00 48.21  ? 51  TYR A CZ  1 
ATOM   361  O  OH  . TYR A 1 43  ? 29.478 22.973  -5.508  1.00 45.98  ? 51  TYR A OH  1 
ATOM   362  N  N   . THR A 1 44  ? 28.366 16.043  -5.529  1.00 44.58  ? 52  THR A N   1 
ATOM   363  C  CA  . THR A 1 44  ? 29.734 15.576  -5.639  1.00 47.35  ? 52  THR A CA  1 
ATOM   364  C  C   . THR A 1 44  ? 30.226 15.932  -7.038  1.00 48.51  ? 52  THR A C   1 
ATOM   365  O  O   . THR A 1 44  ? 29.421 16.167  -7.936  1.00 46.99  ? 52  THR A O   1 
ATOM   366  C  CB  . THR A 1 44  ? 29.815 14.069  -5.361  1.00 47.75  ? 52  THR A CB  1 
ATOM   367  O  OG1 . THR A 1 44  ? 28.908 13.421  -6.253  1.00 52.92  ? 52  THR A OG1 1 
ATOM   368  C  CG2 . THR A 1 44  ? 29.471 13.709  -3.932  1.00 48.82  ? 52  THR A CG2 1 
ATOM   369  N  N   . VAL A 1 45  ? 31.548 15.985  -7.209  1.00 47.72  ? 53  VAL A N   1 
ATOM   370  C  CA  . VAL A 1 45  ? 32.131 16.327  -8.492  1.00 39.95  ? 53  VAL A CA  1 
ATOM   371  C  C   . VAL A 1 45  ? 33.108 15.224  -8.883  1.00 43.29  ? 53  VAL A C   1 
ATOM   372  O  O   . VAL A 1 45  ? 33.982 14.858  -8.100  1.00 49.89  ? 53  VAL A O   1 
ATOM   373  C  CB  . VAL A 1 45  ? 32.816 17.707  -8.451  1.00 42.67  ? 53  VAL A CB  1 
ATOM   374  C  CG1 . VAL A 1 45  ? 33.618 17.981  -9.714  1.00 42.66  ? 53  VAL A CG1 1 
ATOM   375  C  CG2 . VAL A 1 45  ? 31.815 18.825  -8.196  1.00 45.11  ? 53  VAL A CG2 1 
ATOM   376  N  N   . LEU A 1 46  ? 32.922 14.689  -10.093 1.00 42.76  ? 54  LEU A N   1 
ATOM   377  C  CA  . LEU A 1 46  ? 33.845 13.724  -10.661 1.00 42.35  ? 54  LEU A CA  1 
ATOM   378  C  C   . LEU A 1 46  ? 34.688 14.419  -11.724 1.00 43.15  ? 54  LEU A C   1 
ATOM   379  O  O   . LEU A 1 46  ? 34.149 14.972  -12.679 1.00 43.22  ? 54  LEU A O   1 
ATOM   380  C  CB  . LEU A 1 46  ? 33.054 12.561  -11.270 1.00 49.45  ? 54  LEU A CB  1 
ATOM   381  C  CG  . LEU A 1 46  ? 33.888 11.525  -12.022 1.00 50.03  ? 54  LEU A CG  1 
ATOM   382  C  CD1 . LEU A 1 46  ? 34.808 10.778  -11.072 1.00 52.82  ? 54  LEU A CD1 1 
ATOM   383  C  CD2 . LEU A 1 46  ? 32.995 10.549  -12.773 1.00 57.24  ? 54  LEU A CD2 1 
ATOM   384  N  N   . ILE A 1 47  ? 36.011 14.401  -11.541 1.00 43.56  ? 55  ILE A N   1 
ATOM   385  C  CA  . ILE A 1 47  ? 36.908 14.804  -12.609 1.00 47.36  ? 55  ILE A CA  1 
ATOM   386  C  C   . ILE A 1 47  ? 37.450 13.538  -13.265 1.00 53.61  ? 55  ILE A C   1 
ATOM   387  O  O   . ILE A 1 47  ? 38.309 12.861  -12.705 1.00 55.46  ? 55  ILE A O   1 
ATOM   388  C  CB  . ILE A 1 47  ? 38.040 15.729  -12.115 1.00 50.64  ? 55  ILE A CB  1 
ATOM   389  C  CG1 . ILE A 1 47  ? 37.512 16.980  -11.405 1.00 51.67  ? 55  ILE A CG1 1 
ATOM   390  C  CG2 . ILE A 1 47  ? 38.954 16.103  -13.269 1.00 52.36  ? 55  ILE A CG2 1 
ATOM   391  C  CD1 . ILE A 1 47  ? 37.257 16.799  -9.930  1.00 57.81  ? 55  ILE A CD1 1 
ATOM   392  N  N   . ASP A 1 48  ? 36.914 13.219  -14.448 1.00 55.37  ? 56  ASP A N   1 
ATOM   393  C  CA  . ASP A 1 48  ? 37.425 12.124  -15.255 1.00 51.04  ? 56  ASP A CA  1 
ATOM   394  C  C   . ASP A 1 48  ? 38.668 12.619  -15.987 1.00 52.18  ? 56  ASP A C   1 
ATOM   395  O  O   . ASP A 1 48  ? 38.574 13.244  -17.041 1.00 54.29  ? 56  ASP A O   1 
ATOM   396  C  CB  . ASP A 1 48  ? 36.359 11.594  -16.218 1.00 54.63  ? 56  ASP A CB  1 
ATOM   397  C  CG  . ASP A 1 48  ? 36.803 10.381  -17.017 1.00 56.36  ? 56  ASP A CG  1 
ATOM   398  O  OD1 . ASP A 1 48  ? 37.890 9.847   -16.717 1.00 60.18  ? 56  ASP A OD1 1 
ATOM   399  O  OD2 . ASP A 1 48  ? 36.064 9.985   -17.939 1.00 65.66  ? 56  ASP A OD2 1 
ATOM   400  N  N   . HIS A 1 49  ? 39.830 12.328  -15.396 1.00 55.62  ? 57  HIS A N   1 
ATOM   401  C  CA  . HIS A 1 49  ? 41.104 12.866  -15.842 1.00 52.39  ? 57  HIS A CA  1 
ATOM   402  C  C   . HIS A 1 49  ? 41.926 11.722  -16.426 1.00 51.50  ? 57  HIS A C   1 
ATOM   403  O  O   . HIS A 1 49  ? 41.901 10.611  -15.901 1.00 56.41  ? 57  HIS A O   1 
ATOM   404  C  CB  . HIS A 1 49  ? 41.809 13.540  -14.658 1.00 51.74  ? 57  HIS A CB  1 
ATOM   405  C  CG  . HIS A 1 49  ? 42.927 14.464  -15.011 1.00 53.57  ? 57  HIS A CG  1 
ATOM   406  N  ND1 . HIS A 1 49  ? 44.166 14.043  -15.443 1.00 47.91  ? 57  HIS A ND1 1 
ATOM   407  C  CD2 . HIS A 1 49  ? 42.992 15.802  -14.947 1.00 55.43  ? 57  HIS A CD2 1 
ATOM   408  C  CE1 . HIS A 1 49  ? 44.938 15.102  -15.653 1.00 51.90  ? 57  HIS A CE1 1 
ATOM   409  N  NE2 . HIS A 1 49  ? 44.244 16.181  -15.358 1.00 50.25  ? 57  HIS A NE2 1 
ATOM   410  N  N   . PRO A 1 50  ? 42.664 11.943  -17.535 1.00 55.51  ? 58  PRO A N   1 
ATOM   411  C  CA  . PRO A 1 50  ? 43.496 10.892  -18.120 1.00 57.22  ? 58  PRO A CA  1 
ATOM   412  C  C   . PRO A 1 50  ? 44.499 10.287  -17.138 1.00 60.26  ? 58  PRO A C   1 
ATOM   413  O  O   . PRO A 1 50  ? 44.892 9.133   -17.290 1.00 64.45  ? 58  PRO A O   1 
ATOM   414  C  CB  . PRO A 1 50  ? 44.217 11.587  -19.288 1.00 56.03  ? 58  PRO A CB  1 
ATOM   415  C  CG  . PRO A 1 50  ? 44.041 13.074  -19.029 1.00 65.13  ? 58  PRO A CG  1 
ATOM   416  C  CD  . PRO A 1 50  ? 42.720 13.197  -18.300 1.00 59.79  ? 58  PRO A CD  1 
ATOM   417  N  N   . GLU A 1 51  ? 44.906 11.064  -16.127 1.00 59.66  ? 59  GLU A N   1 
ATOM   418  C  CA  . GLU A 1 51  ? 45.851 10.577  -15.134 1.00 61.17  ? 59  GLU A CA  1 
ATOM   419  C  C   . GLU A 1 51  ? 45.126 9.725   -14.096 1.00 55.31  ? 59  GLU A C   1 
ATOM   420  O  O   . GLU A 1 51  ? 45.764 9.043   -13.298 1.00 62.58  ? 59  GLU A O   1 
ATOM   421  C  CB  . GLU A 1 51  ? 46.568 11.732  -14.435 1.00 62.53  ? 59  GLU A CB  1 
ATOM   422  C  CG  . GLU A 1 51  ? 47.544 12.476  -15.323 1.00 61.83  ? 59  GLU A CG  1 
ATOM   423  C  CD  . GLU A 1 51  ? 48.211 13.650  -14.630 1.00 53.72  ? 59  GLU A CD  1 
ATOM   424  O  OE1 . GLU A 1 51  ? 48.746 13.451  -13.522 1.00 63.67  ? 59  GLU A OE1 1 
ATOM   425  O  OE2 . GLU A 1 51  ? 48.192 14.759  -15.197 1.00 58.75  ? 59  GLU A OE2 1 
ATOM   426  N  N   . GLY A 1 52  ? 43.790 9.781   -14.109 1.00 49.32  ? 60  GLY A N   1 
ATOM   427  C  CA  . GLY A 1 52  ? 42.979 9.016   -13.177 1.00 48.31  ? 60  GLY A CA  1 
ATOM   428  C  C   . GLY A 1 52  ? 41.780 9.820   -12.680 1.00 47.54  ? 60  GLY A C   1 
ATOM   429  O  O   . GLY A 1 52  ? 41.795 11.047  -12.716 1.00 54.38  ? 60  GLY A O   1 
ATOM   430  N  N   . LYS A 1 53  ? 40.752 9.104   -12.212 1.00 48.60  ? 61  LYS A N   1 
ATOM   431  C  CA  . LYS A 1 53  ? 39.488 9.707   -11.824 1.00 54.91  ? 61  LYS A CA  1 
ATOM   432  C  C   . LYS A 1 53  ? 39.588 10.250  -10.398 1.00 56.30  ? 61  LYS A C   1 
ATOM   433  O  O   . LYS A 1 53  ? 39.955 9.532   -9.470  1.00 53.82  ? 61  LYS A O   1 
ATOM   434  C  CB  . LYS A 1 53  ? 38.362 8.681   -11.997 1.00 62.29  ? 61  LYS A CB  1 
ATOM   435  C  CG  . LYS A 1 53  ? 38.106 8.260   -13.442 1.00 68.06  ? 61  LYS A CG  1 
ATOM   436  C  CD  . LYS A 1 53  ? 36.993 7.241   -13.622 1.00 71.72  ? 61  LYS A CD  1 
ATOM   437  C  CE  . LYS A 1 53  ? 36.497 7.139   -15.052 1.00 72.72  ? 61  LYS A CE  1 
ATOM   438  N  NZ  . LYS A 1 53  ? 37.580 6.779   -15.998 1.00 65.63  ? 61  LYS A NZ  1 
ATOM   439  N  N   . ILE A 1 54  ? 39.256 11.540  -10.255 1.00 51.49  ? 62  ILE A N   1 
ATOM   440  C  CA  . ILE A 1 54  ? 39.302 12.256  -8.990  1.00 50.37  ? 62  ILE A CA  1 
ATOM   441  C  C   . ILE A 1 54  ? 37.869 12.592  -8.584  1.00 53.10  ? 62  ILE A C   1 
ATOM   442  O  O   . ILE A 1 54  ? 37.125 13.181  -9.366  1.00 51.05  ? 62  ILE A O   1 
ATOM   443  C  CB  . ILE A 1 54  ? 40.169 13.528  -9.122  1.00 49.90  ? 62  ILE A CB  1 
ATOM   444  C  CG1 . ILE A 1 54  ? 41.603 13.210  -9.552  1.00 50.36  ? 62  ILE A CG1 1 
ATOM   445  C  CG2 . ILE A 1 54  ? 40.146 14.347  -7.841  1.00 51.84  ? 62  ILE A CG2 1 
ATOM   446  C  CD1 . ILE A 1 54  ? 42.324 14.385  -10.171 1.00 48.92  ? 62  ILE A CD1 1 
ATOM   447  N  N   . LEU A 1 55  ? 37.489 12.197  -7.363  1.00 49.71  ? 63  LEU A N   1 
ATOM   448  C  CA  . LEU A 1 55  ? 36.169 12.482  -6.825  1.00 47.99  ? 63  LEU A CA  1 
ATOM   449  C  C   . LEU A 1 55  ? 36.293 13.511  -5.702  1.00 51.73  ? 63  LEU A C   1 
ATOM   450  O  O   . LEU A 1 55  ? 37.119 13.355  -4.806  1.00 53.54  ? 63  LEU A O   1 
ATOM   451  C  CB  . LEU A 1 55  ? 35.549 11.175  -6.316  1.00 48.22  ? 63  LEU A CB  1 
ATOM   452  C  CG  . LEU A 1 55  ? 34.144 11.295  -5.726  1.00 49.85  ? 63  LEU A CG  1 
ATOM   453  C  CD1 . LEU A 1 55  ? 33.180 11.878  -6.744  1.00 51.96  ? 63  LEU A CD1 1 
ATOM   454  C  CD2 . LEU A 1 55  ? 33.640 9.946   -5.234  1.00 52.21  ? 63  LEU A CD2 1 
ATOM   455  N  N   . PHE A 1 56  ? 35.475 14.569  -5.767  1.00 46.13  ? 64  PHE A N   1 
ATOM   456  C  CA  . PHE A 1 56  ? 35.426 15.572  -4.714  1.00 41.33  ? 64  PHE A CA  1 
ATOM   457  C  C   . PHE A 1 56  ? 34.138 15.393  -3.912  1.00 47.02  ? 64  PHE A C   1 
ATOM   458  O  O   . PHE A 1 56  ? 33.051 15.675  -4.412  1.00 51.35  ? 64  PHE A O   1 
ATOM   459  C  CB  . PHE A 1 56  ? 35.531 16.979  -5.312  1.00 43.80  ? 64  PHE A CB  1 
ATOM   460  C  CG  . PHE A 1 56  ? 35.613 18.103  -4.308  1.00 43.29  ? 64  PHE A CG  1 
ATOM   461  C  CD1 . PHE A 1 56  ? 36.804 18.405  -3.668  1.00 46.23  ? 64  PHE A CD1 1 
ATOM   462  C  CD2 . PHE A 1 56  ? 34.493 18.861  -4.003  1.00 44.48  ? 64  PHE A CD2 1 
ATOM   463  C  CE1 . PHE A 1 56  ? 36.875 19.445  -2.752  1.00 49.26  ? 64  PHE A CE1 1 
ATOM   464  C  CE2 . PHE A 1 56  ? 34.564 19.898  -3.086  1.00 45.50  ? 64  PHE A CE2 1 
ATOM   465  C  CZ  . PHE A 1 56  ? 35.755 20.188  -2.462  1.00 42.83  ? 64  PHE A CZ  1 
ATOM   466  N  N   . ASP A 1 57  ? 34.279 14.913  -2.670  1.00 46.74  ? 65  ASP A N   1 
ATOM   467  C  CA  . ASP A 1 57  ? 33.159 14.687  -1.765  1.00 50.91  ? 65  ASP A CA  1 
ATOM   468  C  C   . ASP A 1 57  ? 32.418 13.414  -2.169  1.00 43.07  ? 65  ASP A C   1 
ATOM   469  O  O   . ASP A 1 57  ? 32.611 12.910  -3.272  1.00 44.06  ? 65  ASP A O   1 
ATOM   470  C  CB  . ASP A 1 57  ? 32.232 15.906  -1.698  1.00 44.86  ? 65  ASP A CB  1 
ATOM   471  C  CG  . ASP A 1 57  ? 32.724 16.987  -0.749  1.00 53.60  ? 65  ASP A CG  1 
ATOM   472  O  OD1 . ASP A 1 57  ? 33.720 16.734  -0.038  1.00 49.11  ? 65  ASP A OD1 1 
ATOM   473  O  OD2 . ASP A 1 57  ? 32.110 18.074  -0.726  1.00 54.07  ? 65  ASP A OD2 1 
ATOM   474  N  N   . THR A 1 58  ? 31.575 12.897  -1.262  1.00 44.01  ? 66  THR A N   1 
ATOM   475  C  CA  . THR A 1 58  ? 30.947 11.599  -1.456  1.00 44.00  ? 66  THR A CA  1 
ATOM   476  C  C   . THR A 1 58  ? 29.500 11.586  -0.964  1.00 43.13  ? 66  THR A C   1 
ATOM   477  O  O   . THR A 1 58  ? 28.898 10.519  -0.870  1.00 51.59  ? 66  THR A O   1 
ATOM   478  C  CB  . THR A 1 58  ? 31.721 10.488  -0.734  1.00 45.10  ? 66  THR A CB  1 
ATOM   479  O  OG1 . THR A 1 58  ? 31.607 10.724  0.670   1.00 45.79  ? 66  THR A OG1 1 
ATOM   480  C  CG2 . THR A 1 58  ? 33.180 10.418  -1.129  1.00 45.62  ? 66  THR A CG2 1 
ATOM   481  N  N   . SER A 1 59  ? 28.948 12.761  -0.642  1.00 45.62  ? 67  SER A N   1 
ATOM   482  C  CA  . SER A 1 59  ? 27.546 12.880  -0.262  1.00 54.69  ? 67  SER A CA  1 
ATOM   483  C  C   . SER A 1 59  ? 27.259 12.086  1.014   1.00 53.40  ? 67  SER A C   1 
ATOM   484  O  O   . SER A 1 59  ? 28.155 11.860  1.823   1.00 55.03  ? 67  SER A O   1 
ATOM   485  C  CB  . SER A 1 59  ? 26.647 12.444  -1.393  1.00 52.67  ? 67  SER A CB  1 
ATOM   486  O  OG  . SER A 1 59  ? 26.639 11.029  -1.525  1.00 61.70  ? 67  SER A OG  1 
ATOM   487  N  N   . CYS A 1 60  ? 25.994 11.675  1.184   1.00 53.25  ? 68  CYS A N   1 
ATOM   488  C  CA  . CYS A 1 60  ? 25.560 10.939  2.363   1.00 48.74  ? 68  CYS A CA  1 
ATOM   489  C  C   . CYS A 1 60  ? 25.513 9.445   2.048   1.00 46.95  ? 68  CYS A C   1 
ATOM   490  O  O   . CYS A 1 60  ? 25.444 9.059   0.884   1.00 55.47  ? 68  CYS A O   1 
ATOM   491  C  CB  . CYS A 1 60  ? 24.184 11.402  2.829   1.00 42.03  ? 68  CYS A CB  1 
ATOM   492  S  SG  . CYS A 1 60  ? 23.971 13.203  2.835   1.00 49.71  ? 68  CYS A SG  1 
ATOM   493  N  N   . ASN A 1 61  ? 25.554 8.607   3.091   1.00 47.17  ? 69  ASN A N   1 
ATOM   494  C  CA  . ASN A 1 61  ? 25.445 7.167   2.917   1.00 52.69  ? 69  ASN A CA  1 
ATOM   495  C  C   . ASN A 1 61  ? 23.991 6.816   2.616   1.00 53.94  ? 69  ASN A C   1 
ATOM   496  O  O   . ASN A 1 61  ? 23.076 7.400   3.192   1.00 48.78  ? 69  ASN A O   1 
ATOM   497  C  CB  . ASN A 1 61  ? 25.929 6.391   4.145   1.00 50.20  ? 69  ASN A CB  1 
ATOM   498  C  CG  . ASN A 1 61  ? 26.223 4.936   3.846   1.00 53.89  ? 69  ASN A CG  1 
ATOM   499  O  OD1 . ASN A 1 61  ? 27.277 4.611   3.303   1.00 56.47  ? 69  ASN A OD1 1 
ATOM   500  N  ND2 . ASN A 1 61  ? 25.312 4.051   4.216   1.00 56.95  ? 69  ASN A ND2 1 
ATOM   501  N  N   . PRO A 1 62  ? 23.729 5.867   1.689   1.00 58.60  ? 70  PRO A N   1 
ATOM   502  C  CA  . PRO A 1 62  ? 22.366 5.399   1.433   1.00 64.00  ? 70  PRO A CA  1 
ATOM   503  C  C   . PRO A 1 62  ? 21.584 5.022   2.690   1.00 56.88  ? 70  PRO A C   1 
ATOM   504  O  O   . PRO A 1 62  ? 20.384 5.274   2.767   1.00 55.98  ? 70  PRO A O   1 
ATOM   505  C  CB  . PRO A 1 62  ? 22.600 4.167   0.546   1.00 63.67  ? 70  PRO A CB  1 
ATOM   506  C  CG  . PRO A 1 62  ? 23.859 4.515   -0.217  1.00 67.24  ? 70  PRO A CG  1 
ATOM   507  C  CD  . PRO A 1 62  ? 24.719 5.236   0.801   1.00 64.37  ? 70  PRO A CD  1 
ATOM   508  N  N   . ASN A 1 63  ? 22.268 4.425   3.673   1.00 60.50  ? 71  ASN A N   1 
ATOM   509  C  CA  . ASN A 1 63  ? 21.601 3.930   4.867   1.00 61.29  ? 71  ASN A CA  1 
ATOM   510  C  C   . ASN A 1 63  ? 21.746 4.948   5.995   1.00 57.04  ? 71  ASN A C   1 
ATOM   511  O  O   . ASN A 1 63  ? 22.011 4.582   7.137   1.00 63.70  ? 71  ASN A O   1 
ATOM   512  C  CB  . ASN A 1 63  ? 22.144 2.567   5.306   1.00 71.95  ? 71  ASN A CB  1 
ATOM   513  C  CG  . ASN A 1 63  ? 21.077 1.678   5.910   1.00 97.48  ? 71  ASN A CG  1 
ATOM   514  O  OD1 . ASN A 1 63  ? 20.201 2.150   6.632   1.00 79.08  ? 71  ASN A OD1 1 
ATOM   515  N  ND2 . ASN A 1 63  ? 21.126 0.393   5.597   1.00 114.62 ? 71  ASN A ND2 1 
ATOM   516  N  N   . SER A 1 64  ? 21.553 6.227   5.663   1.00 59.79  ? 72  SER A N   1 
ATOM   517  C  CA  . SER A 1 64  ? 21.745 7.303   6.620   1.00 58.97  ? 72  SER A CA  1 
ATOM   518  C  C   . SER A 1 64  ? 20.458 7.566   7.397   1.00 60.32  ? 72  SER A C   1 
ATOM   519  O  O   . SER A 1 64  ? 20.498 7.782   8.606   1.00 56.80  ? 72  SER A O   1 
ATOM   520  C  CB  . SER A 1 64  ? 22.235 8.553   5.933   1.00 54.81  ? 72  SER A CB  1 
ATOM   521  O  OG  . SER A 1 64  ? 23.585 8.406   5.514   1.00 64.75  ? 72  SER A OG  1 
ATOM   522  N  N   . MET A 1 65  ? 19.320 7.532   6.696   1.00 61.00  ? 73  MET A N   1 
ATOM   523  C  CA  . MET A 1 65  ? 18.067 8.019   7.251   1.00 61.74  ? 73  MET A CA  1 
ATOM   524  C  C   . MET A 1 65  ? 17.118 6.852   7.519   1.00 63.13  ? 73  MET A C   1 
ATOM   525  O  O   . MET A 1 65  ? 17.305 5.761   6.985   1.00 59.40  ? 73  MET A O   1 
ATOM   526  C  CB  . MET A 1 65  ? 17.413 8.999   6.273   1.00 58.51  ? 73  MET A CB  1 
ATOM   527  C  CG  . MET A 1 65  ? 18.214 10.272  6.084   1.00 58.53  ? 73  MET A CG  1 
ATOM   528  S  SD  . MET A 1 65  ? 17.774 11.561  7.271   1.00 62.58  ? 73  MET A SD  1 
ATOM   529  C  CE  . MET A 1 65  ? 15.991 11.564  7.097   1.00 68.93  ? 73  MET A CE  1 
ATOM   530  N  N   . GLY A 1 66  ? 16.106 7.101   8.361   1.00 75.03  ? 74  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 66  ? 15.057 6.131   8.639   1.00 85.97  ? 74  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 66  ? 15.284 5.394   9.958   1.00 85.83  ? 74  GLY A C   1 
ATOM   533  O  O   . GLY A 1 66  ? 16.318 5.566   10.598  1.00 78.32  ? 74  GLY A O   1 
ATOM   534  N  N   . PRO A 1 67  ? 14.325 4.548   10.405  1.00 82.47  ? 75  PRO A N   1 
ATOM   535  C  CA  . PRO A 1 67  ? 14.453 3.832   11.677  1.00 77.51  ? 75  PRO A CA  1 
ATOM   536  C  C   . PRO A 1 67  ? 15.725 2.994   11.837  1.00 68.49  ? 75  PRO A C   1 
ATOM   537  O  O   . PRO A 1 67  ? 16.280 2.939   12.932  1.00 61.79  ? 75  PRO A O   1 
ATOM   538  C  CB  . PRO A 1 67  ? 13.187 2.957   11.734  1.00 85.67  ? 75  PRO A CB  1 
ATOM   539  C  CG  . PRO A 1 67  ? 12.672 2.920   10.308  1.00 87.00  ? 75  PRO A CG  1 
ATOM   540  C  CD  . PRO A 1 67  ? 13.049 4.267   9.730   1.00 80.00  ? 75  PRO A CD  1 
ATOM   541  N  N   . GLN A 1 68  ? 16.194 2.344   10.762  1.00 69.14  ? 76  GLN A N   1 
ATOM   542  C  CA  . GLN A 1 68  ? 17.430 1.573   10.832  1.00 72.32  ? 76  GLN A CA  1 
ATOM   543  C  C   . GLN A 1 68  ? 18.607 2.379   10.287  1.00 72.39  ? 76  GLN A C   1 
ATOM   544  O  O   . GLN A 1 68  ? 19.614 1.802   9.882   1.00 57.72  ? 76  GLN A O   1 
ATOM   545  C  CB  . GLN A 1 68  ? 17.346 0.265   10.040  1.00 81.17  ? 76  GLN A CB  1 
ATOM   546  C  CG  . GLN A 1 68  ? 16.700 -0.881  10.802  1.00 96.57  ? 76  GLN A CG  1 
ATOM   547  C  CD  . GLN A 1 68  ? 15.197 -0.762  10.812  1.00 106.55 ? 76  GLN A CD  1 
ATOM   548  O  OE1 . GLN A 1 68  ? 14.544 -0.836  9.774   1.00 117.19 ? 76  GLN A OE1 1 
ATOM   549  N  NE2 . GLN A 1 68  ? 14.636 -0.572  11.994  1.00 97.93  ? 76  GLN A NE2 1 
ATOM   550  N  N   . GLY A 1 69  ? 18.483 3.710   10.283  1.00 72.24  ? 77  GLY A N   1 
ATOM   551  C  CA  . GLY A 1 69  ? 19.505 4.570   9.708   1.00 73.39  ? 77  GLY A CA  1 
ATOM   552  C  C   . GLY A 1 69  ? 20.737 4.693   10.603  1.00 65.69  ? 77  GLY A C   1 
ATOM   553  O  O   . GLY A 1 69  ? 20.653 4.500   11.814  1.00 67.51  ? 77  GLY A O   1 
ATOM   554  N  N   . ARG A 1 70  ? 21.876 5.024   9.982   1.00 62.12  ? 78  ARG A N   1 
ATOM   555  C  CA  . ARG A 1 70  ? 23.132 5.216   10.689  1.00 57.30  ? 78  ARG A CA  1 
ATOM   556  C  C   . ARG A 1 70  ? 23.086 6.516   11.487  1.00 53.30  ? 78  ARG A C   1 
ATOM   557  O  O   . ARG A 1 70  ? 23.667 6.607   12.565  1.00 63.92  ? 78  ARG A O   1 
ATOM   558  C  CB  . ARG A 1 70  ? 24.307 5.265   9.708   1.00 55.32  ? 78  ARG A CB  1 
ATOM   559  C  CG  . ARG A 1 70  ? 24.668 3.925   9.083   1.00 56.61  ? 78  ARG A CG  1 
ATOM   560  C  CD  . ARG A 1 70  ? 25.925 4.044   8.243   1.00 56.98  ? 78  ARG A CD  1 
ATOM   561  N  NE  . ARG A 1 70  ? 26.210 2.846   7.468   1.00 58.96  ? 78  ARG A NE  1 
ATOM   562  C  CZ  . ARG A 1 70  ? 27.211 2.738   6.603   1.00 61.13  ? 78  ARG A CZ  1 
ATOM   563  N  NH1 . ARG A 1 70  ? 28.021 3.762   6.399   1.00 60.73  ? 78  ARG A NH1 1 
ATOM   564  N  NH2 . ARG A 1 70  ? 27.396 1.609   5.939   1.00 64.80  ? 78  ARG A NH2 1 
ATOM   565  N  N   . TRP A 1 71  ? 22.406 7.525   10.933  1.00 54.22  ? 79  TRP A N   1 
ATOM   566  C  CA  . TRP A 1 71  ? 22.270 8.811   11.596  1.00 57.80  ? 79  TRP A CA  1 
ATOM   567  C  C   . TRP A 1 71  ? 21.376 8.666   12.825  1.00 54.87  ? 79  TRP A C   1 
ATOM   568  O  O   . TRP A 1 71  ? 20.320 8.041   12.759  1.00 62.03  ? 79  TRP A O   1 
ATOM   569  C  CB  . TRP A 1 71  ? 21.693 9.863   10.638  1.00 55.76  ? 79  TRP A CB  1 
ATOM   570  C  CG  . TRP A 1 71  ? 22.558 10.198  9.449   1.00 58.53  ? 79  TRP A CG  1 
ATOM   571  C  CD1 . TRP A 1 71  ? 23.703 9.579   9.041   1.00 50.62  ? 79  TRP A CD1 1 
ATOM   572  C  CD2 . TRP A 1 71  ? 22.326 11.269  8.507   1.00 51.71  ? 79  TRP A CD2 1 
ATOM   573  N  NE1 . TRP A 1 71  ? 24.194 10.182  7.913   1.00 55.10  ? 79  TRP A NE1 1 
ATOM   574  C  CE2 . TRP A 1 71  ? 23.374 11.223  7.563   1.00 54.19  ? 79  TRP A CE2 1 
ATOM   575  C  CE3 . TRP A 1 71  ? 21.341 12.254  8.374   1.00 53.57  ? 79  TRP A CE3 1 
ATOM   576  C  CZ2 . TRP A 1 71  ? 23.459 12.124  6.504   1.00 50.31  ? 79  TRP A CZ2 1 
ATOM   577  C  CZ3 . TRP A 1 71  ? 21.427 13.145  7.327   1.00 57.07  ? 79  TRP A CZ3 1 
ATOM   578  C  CH2 . TRP A 1 71  ? 22.471 13.078  6.405   1.00 58.95  ? 79  TRP A CH2 1 
ATOM   579  N  N   . ALA A 1 72  ? 21.813 9.253   13.942  1.00 56.91  ? 80  ALA A N   1 
ATOM   580  C  CA  . ALA A 1 72  ? 20.984 9.364   15.131  1.00 56.76  ? 80  ALA A CA  1 
ATOM   581  C  C   . ALA A 1 72  ? 19.688 10.090  14.775  1.00 61.30  ? 80  ALA A C   1 
ATOM   582  O  O   . ALA A 1 72  ? 19.647 10.852  13.812  1.00 66.13  ? 80  ALA A O   1 
ATOM   583  C  CB  . ALA A 1 72  ? 21.750 10.084  16.213  1.00 57.40  ? 80  ALA A CB  1 
ATOM   584  N  N   . GLU A 1 73  ? 18.637 9.854   15.569  1.00 58.94  ? 81  GLU A N   1 
ATOM   585  C  CA  . GLU A 1 73  ? 17.300 10.339  15.259  1.00 64.11  ? 81  GLU A CA  1 
ATOM   586  C  C   . GLU A 1 73  ? 17.268 11.865  15.339  1.00 59.36  ? 81  GLU A C   1 
ATOM   587  O  O   . GLU A 1 73  ? 16.625 12.511  14.515  1.00 61.04  ? 81  GLU A O   1 
ATOM   588  C  CB  . GLU A 1 73  ? 16.280 9.673   16.190  1.00 73.79  ? 81  GLU A CB  1 
ATOM   589  C  CG  . GLU A 1 73  ? 14.841 10.113  15.969  1.00 77.95  ? 81  GLU A CG  1 
ATOM   590  C  CD  . GLU A 1 73  ? 14.347 10.022  14.535  1.00 88.09  ? 81  GLU A CD  1 
ATOM   591  O  OE1 . GLU A 1 73  ? 14.622 8.997   13.880  1.00 87.73  ? 81  GLU A OE1 1 
ATOM   592  O  OE2 . GLU A 1 73  ? 13.671 10.970  14.084  1.00 85.43  ? 81  GLU A OE2 1 
ATOM   593  N  N   . SER A 1 74  ? 17.969 12.437  16.326  1.00 57.31  ? 82  SER A N   1 
ATOM   594  C  CA  . SER A 1 74  ? 18.048 13.883  16.472  1.00 65.84  ? 82  SER A CA  1 
ATOM   595  C  C   . SER A 1 74  ? 18.696 14.505  15.237  1.00 61.16  ? 82  SER A C   1 
ATOM   596  O  O   . SER A 1 74  ? 18.316 15.596  14.817  1.00 62.16  ? 82  SER A O   1 
ATOM   597  C  CB  . SER A 1 74  ? 18.794 14.269  17.725  1.00 67.86  ? 82  SER A CB  1 
ATOM   598  O  OG  . SER A 1 74  ? 20.117 13.751  17.709  1.00 75.81  ? 82  SER A OG  1 
ATOM   599  N  N   . THR A 1 75  ? 19.680 13.803  14.664  1.00 60.78  ? 83  THR A N   1 
ATOM   600  C  CA  . THR A 1 75  ? 20.405 14.312  13.512  1.00 60.30  ? 83  THR A CA  1 
ATOM   601  C  C   . THR A 1 75  ? 19.498 14.243  12.284  1.00 61.40  ? 83  THR A C   1 
ATOM   602  O  O   . THR A 1 75  ? 19.477 15.166  11.473  1.00 52.93  ? 83  THR A O   1 
ATOM   603  C  CB  . THR A 1 75  ? 21.730 13.561  13.321  1.00 60.76  ? 83  THR A CB  1 
ATOM   604  O  OG1 . THR A 1 75  ? 22.371 13.456  14.592  1.00 58.38  ? 83  THR A OG1 1 
ATOM   605  C  CG2 . THR A 1 75  ? 22.658 14.240  12.338  1.00 65.22  ? 83  THR A CG2 1 
ATOM   606  N  N   . GLN A 1 76  ? 18.732 13.151  12.170  1.00 58.78  ? 84  GLN A N   1 
ATOM   607  C  CA  . GLN A 1 76  ? 17.833 12.957  11.044  1.00 63.76  ? 84  GLN A CA  1 
ATOM   608  C  C   . GLN A 1 76  ? 16.716 13.998  11.071  1.00 61.25  ? 84  GLN A C   1 
ATOM   609  O  O   . GLN A 1 76  ? 16.056 14.229  10.060  1.00 66.70  ? 84  GLN A O   1 
ATOM   610  C  CB  . GLN A 1 76  ? 17.211 11.559  11.067  1.00 55.29  ? 84  GLN A CB  1 
ATOM   611  C  CG  . GLN A 1 76  ? 18.218 10.424  10.970  1.00 61.03  ? 84  GLN A CG  1 
ATOM   612  C  CD  . GLN A 1 76  ? 17.522 9.107   10.735  1.00 65.67  ? 84  GLN A CD  1 
ATOM   613  O  OE1 . GLN A 1 76  ? 16.376 9.065   10.291  1.00 54.39  ? 84  GLN A OE1 1 
ATOM   614  N  NE2 . GLN A 1 76  ? 18.219 8.016   11.012  1.00 63.87  ? 84  GLN A NE2 1 
ATOM   615  N  N   . GLN A 1 77  ? 16.508 14.623  12.234  1.00 63.40  ? 85  GLN A N   1 
ATOM   616  C  CA  . GLN A 1 77  ? 15.381 15.520  12.427  1.00 57.78  ? 85  GLN A CA  1 
ATOM   617  C  C   . GLN A 1 77  ? 15.809 16.973  12.238  1.00 62.70  ? 85  GLN A C   1 
ATOM   618  O  O   . GLN A 1 77  ? 14.982 17.828  11.931  1.00 59.81  ? 85  GLN A O   1 
ATOM   619  C  CB  . GLN A 1 77  ? 14.772 15.312  13.815  1.00 69.31  ? 85  GLN A CB  1 
ATOM   620  C  CG  . GLN A 1 77  ? 13.586 14.358  13.820  1.00 86.19  ? 85  GLN A CG  1 
ATOM   621  C  CD  . GLN A 1 77  ? 13.227 13.914  15.216  1.00 98.22  ? 85  GLN A CD  1 
ATOM   622  O  OE1 . GLN A 1 77  ? 14.032 14.002  16.141  1.00 113.56 ? 85  GLN A OE1 1 
ATOM   623  N  NE2 . GLN A 1 77  ? 12.010 13.418  15.376  1.00 101.51 ? 85  GLN A NE2 1 
ATOM   624  N  N   . MET A 1 78  ? 17.102 17.246  12.428  1.00 60.04  ? 86  MET A N   1 
ATOM   625  C  CA  . MET A 1 78  ? 17.609 18.604  12.337  1.00 60.99  ? 86  MET A CA  1 
ATOM   626  C  C   . MET A 1 78  ? 18.248 18.823  10.968  1.00 53.81  ? 86  MET A C   1 
ATOM   627  O  O   . MET A 1 78  ? 18.351 19.956  10.504  1.00 51.00  ? 86  MET A O   1 
ATOM   628  C  CB  . MET A 1 78  ? 18.644 18.871  13.434  1.00 63.07  ? 86  MET A CB  1 
ATOM   629  C  CG  . MET A 1 78  ? 18.056 19.481  14.691  1.00 77.92  ? 86  MET A CG  1 
ATOM   630  S  SD  . MET A 1 78  ? 19.325 19.707  15.961  1.00 81.26  ? 86  MET A SD  1 
ATOM   631  C  CE  . MET A 1 78  ? 20.649 20.387  14.963  1.00 88.01  ? 86  MET A CE  1 
ATOM   632  N  N   . PHE A 1 79  ? 18.671 17.726  10.329  1.00 50.29  ? 87  PHE A N   1 
ATOM   633  C  CA  . PHE A 1 79  ? 19.334 17.795  9.037   1.00 56.02  ? 87  PHE A CA  1 
ATOM   634  C  C   . PHE A 1 79  ? 18.817 16.688  8.120   1.00 58.42  ? 87  PHE A C   1 
ATOM   635  O  O   . PHE A 1 79  ? 19.602 15.897  7.602   1.00 60.37  ? 87  PHE A O   1 
ATOM   636  C  CB  . PHE A 1 79  ? 20.853 17.678  9.207   1.00 57.59  ? 87  PHE A CB  1 
ATOM   637  C  CG  . PHE A 1 79  ? 21.467 18.672  10.160  1.00 65.39  ? 87  PHE A CG  1 
ATOM   638  C  CD1 . PHE A 1 79  ? 21.581 20.011  9.820   1.00 73.64  ? 87  PHE A CD1 1 
ATOM   639  C  CD2 . PHE A 1 79  ? 21.925 18.268  11.405  1.00 77.82  ? 87  PHE A CD2 1 
ATOM   640  C  CE1 . PHE A 1 79  ? 22.146 20.921  10.701  1.00 83.33  ? 87  PHE A CE1 1 
ATOM   641  C  CE2 . PHE A 1 79  ? 22.488 19.180  12.285  1.00 83.17  ? 87  PHE A CE2 1 
ATOM   642  C  CZ  . PHE A 1 79  ? 22.596 20.504  11.932  1.00 87.39  ? 87  PHE A CZ  1 
ATOM   643  N  N   . PRO A 1 80  ? 17.490 16.605  7.868   1.00 58.79  ? 88  PRO A N   1 
ATOM   644  C  CA  . PRO A 1 80  ? 16.922 15.531  7.048   1.00 55.59  ? 88  PRO A CA  1 
ATOM   645  C  C   . PRO A 1 80  ? 17.405 15.534  5.598   1.00 54.93  ? 88  PRO A C   1 
ATOM   646  O  O   . PRO A 1 80  ? 17.416 16.573  4.941   1.00 53.25  ? 88  PRO A O   1 
ATOM   647  C  CB  . PRO A 1 80  ? 15.409 15.799  7.097   1.00 56.25  ? 88  PRO A CB  1 
ATOM   648  C  CG  . PRO A 1 80  ? 15.304 17.278  7.412   1.00 61.43  ? 88  PRO A CG  1 
ATOM   649  C  CD  . PRO A 1 80  ? 16.467 17.549  8.344   1.00 61.15  ? 88  PRO A CD  1 
ATOM   650  N  N   . TRP A 1 81  ? 17.787 14.348  5.111   1.00 49.08  ? 89  TRP A N   1 
ATOM   651  C  CA  . TRP A 1 81  ? 18.255 14.169  3.746   1.00 60.14  ? 89  TRP A CA  1 
ATOM   652  C  C   . TRP A 1 81  ? 17.179 13.467  2.920   1.00 59.05  ? 89  TRP A C   1 
ATOM   653  O  O   . TRP A 1 81  ? 16.719 12.388  3.285   1.00 62.68  ? 89  TRP A O   1 
ATOM   654  C  CB  . TRP A 1 81  ? 19.565 13.366  3.756   1.00 48.91  ? 89  TRP A CB  1 
ATOM   655  C  CG  . TRP A 1 81  ? 20.156 13.076  2.401   1.00 47.25  ? 89  TRP A CG  1 
ATOM   656  C  CD1 . TRP A 1 81  ? 20.396 13.959  1.390   1.00 44.20  ? 89  TRP A CD1 1 
ATOM   657  C  CD2 . TRP A 1 81  ? 20.628 11.793  1.930   1.00 45.95  ? 89  TRP A CD2 1 
ATOM   658  N  NE1 . TRP A 1 81  ? 20.965 13.318  0.322   1.00 47.86  ? 89  TRP A NE1 1 
ATOM   659  C  CE2 . TRP A 1 81  ? 21.123 11.991  0.624   1.00 43.39  ? 89  TRP A CE2 1 
ATOM   660  C  CE3 . TRP A 1 81  ? 20.673 10.507  2.480   1.00 44.93  ? 89  TRP A CE3 1 
ATOM   661  C  CZ2 . TRP A 1 81  ? 21.654 10.950  -0.135  1.00 47.88  ? 89  TRP A CZ2 1 
ATOM   662  C  CZ3 . TRP A 1 81  ? 21.199 9.480   1.729   1.00 46.82  ? 89  TRP A CZ3 1 
ATOM   663  C  CH2 . TRP A 1 81  ? 21.687 9.701   0.442   1.00 49.40  ? 89  TRP A CH2 1 
ATOM   664  N  N   . THR A 1 82  ? 16.779 14.096  1.810   1.00 62.03  ? 90  THR A N   1 
ATOM   665  C  CA  . THR A 1 82  ? 15.825 13.499  0.889   1.00 59.42  ? 90  THR A CA  1 
ATOM   666  C  C   . THR A 1 82  ? 16.554 13.120  -0.398  1.00 57.50  ? 90  THR A C   1 
ATOM   667  O  O   . THR A 1 82  ? 17.207 13.959  -1.015  1.00 63.06  ? 90  THR A O   1 
ATOM   668  C  CB  . THR A 1 82  ? 14.649 14.446  0.615   1.00 63.88  ? 90  THR A CB  1 
ATOM   669  O  OG1 . THR A 1 82  ? 15.165 15.612  -0.027  1.00 84.07  ? 90  THR A OG1 1 
ATOM   670  C  CG2 . THR A 1 82  ? 13.898 14.844  1.867   1.00 60.27  ? 90  THR A CG2 1 
ATOM   671  N  N   . ALA A 1 83  ? 16.440 11.848  -0.795  1.00 55.51  ? 91  ALA A N   1 
ATOM   672  C  CA  . ALA A 1 83  ? 17.141 11.351  -1.967  1.00 62.79  ? 91  ALA A CA  1 
ATOM   673  C  C   . ALA A 1 83  ? 16.423 10.133  -2.542  1.00 65.51  ? 91  ALA A C   1 
ATOM   674  O  O   . ALA A 1 83  ? 16.083 9.202   -1.815  1.00 68.42  ? 91  ALA A O   1 
ATOM   675  C  CB  . ALA A 1 83  ? 18.567 11.017  -1.604  1.00 67.49  ? 91  ALA A CB  1 
ATOM   676  N  N   . THR A 1 84  ? 16.208 10.160  -3.862  1.00 64.17  ? 92  THR A N   1 
ATOM   677  C  CA  . THR A 1 84  ? 15.736 9.002   -4.602  1.00 69.90  ? 92  THR A CA  1 
ATOM   678  C  C   . THR A 1 84  ? 16.945 8.130   -4.924  1.00 72.12  ? 92  THR A C   1 
ATOM   679  O  O   . THR A 1 84  ? 18.078 8.601   -4.848  1.00 73.32  ? 92  THR A O   1 
ATOM   680  C  CB  . THR A 1 84  ? 14.984 9.441   -5.865  1.00 74.59  ? 92  THR A CB  1 
ATOM   681  O  OG1 . THR A 1 84  ? 15.943 9.958   -6.788  1.00 78.63  ? 92  THR A OG1 1 
ATOM   682  C  CG2 . THR A 1 84  ? 13.926 10.487  -5.589  1.00 71.31  ? 92  THR A CG2 1 
ATOM   683  N  N   . GLU A 1 85  ? 16.709 6.864   -5.285  1.00 65.28  ? 93  GLU A N   1 
ATOM   684  C  CA  . GLU A 1 85  ? 17.810 5.940   -5.507  1.00 74.92  ? 93  GLU A CA  1 
ATOM   685  C  C   . GLU A 1 85  ? 18.764 6.496   -6.560  1.00 65.71  ? 93  GLU A C   1 
ATOM   686  O  O   . GLU A 1 85  ? 19.958 6.210   -6.517  1.00 66.19  ? 93  GLU A O   1 
ATOM   687  C  CB  . GLU A 1 85  ? 17.323 4.552   -5.928  1.00 87.30  ? 93  GLU A CB  1 
ATOM   688  C  CG  . GLU A 1 85  ? 16.953 3.660   -4.757  1.00 105.03 ? 93  GLU A CG  1 
ATOM   689  C  CD  . GLU A 1 85  ? 17.470 2.236   -4.872  1.00 112.70 ? 93  GLU A CD  1 
ATOM   690  O  OE1 . GLU A 1 85  ? 17.244 1.608   -5.928  1.00 110.13 ? 93  GLU A OE1 1 
ATOM   691  O  OE2 . GLU A 1 85  ? 18.095 1.758   -3.902  1.00 120.83 ? 93  GLU A OE2 1 
ATOM   692  N  N   . GLU A 1 86  ? 18.238 7.285   -7.504  1.00 62.97  ? 94  GLU A N   1 
ATOM   693  C  CA  . GLU A 1 86  ? 19.045 7.757   -8.618  1.00 72.19  ? 94  GLU A CA  1 
ATOM   694  C  C   . GLU A 1 86  ? 20.062 8.779   -8.109  1.00 64.01  ? 94  GLU A C   1 
ATOM   695  O  O   . GLU A 1 86  ? 21.100 8.983   -8.735  1.00 56.67  ? 94  GLU A O   1 
ATOM   696  C  CB  . GLU A 1 86  ? 18.170 8.335   -9.736  1.00 82.15  ? 94  GLU A CB  1 
ATOM   697  C  CG  . GLU A 1 86  ? 17.941 9.836   -9.647  1.00 103.74 ? 94  GLU A CG  1 
ATOM   698  C  CD  . GLU A 1 86  ? 17.340 10.460  -10.898 1.00 108.56 ? 94  GLU A CD  1 
ATOM   699  O  OE1 . GLU A 1 86  ? 16.284 9.976   -11.350 1.00 104.22 ? 94  GLU A OE1 1 
ATOM   700  O  OE2 . GLU A 1 86  ? 17.923 11.436  -11.415 1.00 88.46  ? 94  GLU A OE2 1 
ATOM   701  N  N   . CYS A 1 87  ? 19.761 9.402   -6.961  1.00 55.50  ? 95  CYS A N   1 
ATOM   702  C  CA  . CYS A 1 87  ? 20.600 10.453  -6.406  1.00 54.17  ? 95  CYS A CA  1 
ATOM   703  C  C   . CYS A 1 87  ? 21.776 9.867   -5.624  1.00 56.10  ? 95  CYS A C   1 
ATOM   704  O  O   . CYS A 1 87  ? 22.732 10.578  -5.324  1.00 57.36  ? 95  CYS A O   1 
ATOM   705  C  CB  . CYS A 1 87  ? 19.793 11.385  -5.508  1.00 52.73  ? 95  CYS A CB  1 
ATOM   706  S  SG  . CYS A 1 87  ? 18.711 12.518  -6.417  1.00 60.39  ? 95  CYS A SG  1 
ATOM   707  N  N   . TYR A 1 88  ? 21.706 8.572   -5.294  1.00 58.25  ? 96  TYR A N   1 
ATOM   708  C  CA  . TYR A 1 88  ? 22.801 7.901   -4.608  1.00 53.51  ? 96  TYR A CA  1 
ATOM   709  C  C   . TYR A 1 88  ? 24.044 7.958   -5.491  1.00 53.48  ? 96  TYR A C   1 
ATOM   710  O  O   . TYR A 1 88  ? 23.950 7.804   -6.706  1.00 58.91  ? 96  TYR A O   1 
ATOM   711  C  CB  . TYR A 1 88  ? 22.467 6.445   -4.269  1.00 58.07  ? 96  TYR A CB  1 
ATOM   712  C  CG  . TYR A 1 88  ? 21.307 6.246   -3.302  1.00 62.63  ? 96  TYR A CG  1 
ATOM   713  C  CD1 . TYR A 1 88  ? 20.782 7.306   -2.573  1.00 64.49  ? 96  TYR A CD1 1 
ATOM   714  C  CD2 . TYR A 1 88  ? 20.726 4.995   -3.132  1.00 65.29  ? 96  TYR A CD2 1 
ATOM   715  C  CE1 . TYR A 1 88  ? 19.725 7.126   -1.697  1.00 63.15  ? 96  TYR A CE1 1 
ATOM   716  C  CE2 . TYR A 1 88  ? 19.667 4.802   -2.260  1.00 64.45  ? 96  TYR A CE2 1 
ATOM   717  C  CZ  . TYR A 1 88  ? 19.165 5.871   -1.541  1.00 60.70  ? 96  TYR A CZ  1 
ATOM   718  O  OH  . TYR A 1 88  ? 18.122 5.689   -0.680  1.00 61.95  ? 96  TYR A OH  1 
ATOM   719  N  N   . LEU A 1 89  ? 25.207 8.161   -4.863  1.00 53.38  ? 97  LEU A N   1 
ATOM   720  C  CA  . LEU A 1 89  ? 26.446 8.389   -5.590  1.00 57.99  ? 97  LEU A CA  1 
ATOM   721  C  C   . LEU A 1 89  ? 26.822 7.154   -6.407  1.00 49.16  ? 97  LEU A C   1 
ATOM   722  O  O   . LEU A 1 89  ? 27.293 7.282   -7.534  1.00 57.73  ? 97  LEU A O   1 
ATOM   723  C  CB  . LEU A 1 89  ? 27.557 8.758   -4.602  1.00 53.24  ? 97  LEU A CB  1 
ATOM   724  C  CG  . LEU A 1 89  ? 28.960 8.876   -5.200  1.00 56.69  ? 97  LEU A CG  1 
ATOM   725  C  CD1 . LEU A 1 89  ? 29.070 10.093  -6.107  1.00 57.33  ? 97  LEU A CD1 1 
ATOM   726  C  CD2 . LEU A 1 89  ? 30.014 8.935   -4.104  1.00 57.66  ? 97  LEU A CD2 1 
ATOM   727  N  N   A HIS A 1 90  ? 26.635 5.966   -5.820  0.50 54.61  ? 98  HIS A N   1 
ATOM   728  N  N   B HIS A 1 90  ? 26.597 5.963   -5.838  0.50 52.92  ? 98  HIS A N   1 
ATOM   729  C  CA  A HIS A 1 90  ? 26.962 4.722   -6.498  0.50 60.09  ? 98  HIS A CA  1 
ATOM   730  C  CA  B HIS A 1 90  ? 26.979 4.728   -6.505  0.50 56.72  ? 98  HIS A CA  1 
ATOM   731  C  C   A HIS A 1 90  ? 26.199 4.642   -7.817  0.50 54.13  ? 98  HIS A C   1 
ATOM   732  C  C   B HIS A 1 90  ? 26.177 4.579   -7.797  0.50 52.28  ? 98  HIS A C   1 
ATOM   733  O  O   A HIS A 1 90  ? 26.739 4.192   -8.826  0.50 55.39  ? 98  HIS A O   1 
ATOM   734  O  O   B HIS A 1 90  ? 26.672 4.022   -8.774  0.50 54.65  ? 98  HIS A O   1 
ATOM   735  C  CB  A HIS A 1 90  ? 26.649 3.506   -5.618  0.50 64.11  ? 98  HIS A CB  1 
ATOM   736  C  CB  B HIS A 1 90  ? 26.856 3.523   -5.563  0.50 57.08  ? 98  HIS A CB  1 
ATOM   737  C  CG  A HIS A 1 90  ? 26.557 2.230   -6.390  0.50 78.28  ? 98  HIS A CG  1 
ATOM   738  C  CG  B HIS A 1 90  ? 25.462 3.047   -5.310  0.50 68.39  ? 98  HIS A CG  1 
ATOM   739  N  ND1 A HIS A 1 90  ? 27.629 1.671   -7.052  0.50 81.42  ? 98  HIS A ND1 1 
ATOM   740  N  ND1 B HIS A 1 90  ? 24.540 3.745   -4.560  0.50 77.09  ? 98  HIS A ND1 1 
ATOM   741  C  CD2 A HIS A 1 90  ? 25.518 1.414   -6.613  0.50 81.46  ? 98  HIS A CD2 1 
ATOM   742  C  CD2 B HIS A 1 90  ? 24.852 1.914   -5.686  0.50 67.15  ? 98  HIS A CD2 1 
ATOM   743  C  CE1 A HIS A 1 90  ? 27.240 0.553   -7.648  0.50 80.22  ? 98  HIS A CE1 1 
ATOM   744  C  CE1 B HIS A 1 90  ? 23.409 3.055   -4.507  0.50 71.07  ? 98  HIS A CE1 1 
ATOM   745  N  NE2 A HIS A 1 90  ? 25.961 0.378   -7.395  0.50 83.18  ? 98  HIS A NE2 1 
ATOM   746  N  NE2 B HIS A 1 90  ? 23.576 1.940   -5.185  0.50 64.36  ? 98  HIS A NE2 1 
ATOM   747  N  N   . ASN A 1 91  ? 24.941 5.091   -7.793  1.00 50.63  ? 99  ASN A N   1 
ATOM   748  C  CA  . ASN A 1 91  ? 24.074 5.017   -8.957  1.00 58.96  ? 99  ASN A CA  1 
ATOM   749  C  C   . ASN A 1 91  ? 24.448 6.123   -9.943  1.00 62.14  ? 99  ASN A C   1 
ATOM   750  O  O   . ASN A 1 91  ? 24.498 5.887   -11.148 1.00 56.56  ? 99  ASN A O   1 
ATOM   751  C  CB  . ASN A 1 91  ? 22.600 5.058   -8.549  1.00 57.64  ? 99  ASN A CB  1 
ATOM   752  C  CG  . ASN A 1 91  ? 22.193 3.839   -7.748  1.00 57.66  ? 99  ASN A CG  1 
ATOM   753  O  OD1 . ASN A 1 91  ? 22.797 2.776   -7.880  1.00 67.10  ? 99  ASN A OD1 1 
ATOM   754  N  ND2 . ASN A 1 91  ? 21.167 3.976   -6.925  1.00 63.81  ? 99  ASN A ND2 1 
ATOM   755  N  N   . ARG A 1 92  ? 24.722 7.324   -9.422  1.00 54.67  ? 100 ARG A N   1 
ATOM   756  C  CA  . ARG A 1 92  ? 25.129 8.441   -10.259 1.00 58.46  ? 100 ARG A CA  1 
ATOM   757  C  C   . ARG A 1 92  ? 26.387 8.060   -11.036 1.00 51.00  ? 100 ARG A C   1 
ATOM   758  O  O   . ARG A 1 92  ? 26.530 8.420   -12.201 1.00 56.45  ? 100 ARG A O   1 
ATOM   759  C  CB  . ARG A 1 92  ? 25.359 9.694   -9.409  1.00 53.98  ? 100 ARG A CB  1 
ATOM   760  C  CG  . ARG A 1 92  ? 24.080 10.354  -8.916  1.00 53.16  ? 100 ARG A CG  1 
ATOM   761  C  CD  . ARG A 1 92  ? 23.345 11.077  -10.029 1.00 52.20  ? 100 ARG A CD  1 
ATOM   762  N  NE  . ARG A 1 92  ? 22.222 11.856  -9.526  1.00 60.47  ? 100 ARG A NE  1 
ATOM   763  C  CZ  . ARG A 1 92  ? 21.019 11.897  -10.088 1.00 53.50  ? 100 ARG A CZ  1 
ATOM   764  N  NH1 . ARG A 1 92  ? 20.792 11.247  -11.216 1.00 62.92  ? 100 ARG A NH1 1 
ATOM   765  N  NH2 . ARG A 1 92  ? 20.054 12.608  -9.531  1.00 54.51  ? 100 ARG A NH2 1 
ATOM   766  N  N   . LEU A 1 93  ? 27.289 7.324   -10.379 1.00 52.26  ? 101 LEU A N   1 
ATOM   767  C  CA  . LEU A 1 93  ? 28.544 6.912   -10.989 1.00 55.98  ? 101 LEU A CA  1 
ATOM   768  C  C   . LEU A 1 93  ? 28.290 5.799   -12.004 1.00 51.42  ? 101 LEU A C   1 
ATOM   769  O  O   . LEU A 1 93  ? 28.919 5.763   -13.059 1.00 57.67  ? 101 LEU A O   1 
ATOM   770  C  CB  . LEU A 1 93  ? 29.505 6.447   -9.890  1.00 51.12  ? 101 LEU A CB  1 
ATOM   771  C  CG  . LEU A 1 93  ? 30.149 7.559   -9.063  1.00 49.68  ? 101 LEU A CG  1 
ATOM   772  C  CD1 . LEU A 1 93  ? 30.895 6.983   -7.870  1.00 49.77  ? 101 LEU A CD1 1 
ATOM   773  C  CD2 . LEU A 1 93  ? 31.088 8.398   -9.916  1.00 46.84  ? 101 LEU A CD2 1 
ATOM   774  N  N   . GLU A 1 94  ? 27.369 4.890   -11.668 1.00 54.38  ? 102 GLU A N   1 
ATOM   775  C  CA  . GLU A 1 94  ? 27.046 3.765   -12.530 1.00 61.22  ? 102 GLU A CA  1 
ATOM   776  C  C   . GLU A 1 94  ? 26.491 4.281   -13.856 1.00 59.97  ? 102 GLU A C   1 
ATOM   777  O  O   . GLU A 1 94  ? 26.775 3.718   -14.911 1.00 51.98  ? 102 GLU A O   1 
ATOM   778  C  CB  . GLU A 1 94  ? 26.062 2.830   -11.822 1.00 67.95  ? 102 GLU A CB  1 
ATOM   779  C  CG  . GLU A 1 94  ? 25.538 1.709   -12.701 1.00 77.05  ? 102 GLU A CG  1 
ATOM   780  C  CD  . GLU A 1 94  ? 24.824 0.604   -11.942 1.00 94.77  ? 102 GLU A CD  1 
ATOM   781  O  OE1 . GLU A 1 94  ? 25.119 -0.579  -12.207 1.00 121.03 ? 102 GLU A OE1 1 
ATOM   782  O  OE2 . GLU A 1 94  ? 23.988 0.929   -11.073 1.00 97.22  ? 102 GLU A OE2 1 
ATOM   783  N  N   . GLN A 1 95  ? 25.712 5.366   -13.790 1.00 46.61  ? 103 GLN A N   1 
ATOM   784  C  CA  . GLN A 1 95  ? 25.093 5.942   -14.973 1.00 52.97  ? 103 GLN A CA  1 
ATOM   785  C  C   . GLN A 1 95  ? 26.149 6.633   -15.829 1.00 54.22  ? 103 GLN A C   1 
ATOM   786  O  O   . GLN A 1 95  ? 25.853 7.090   -16.930 1.00 60.88  ? 103 GLN A O   1 
ATOM   787  C  CB  . GLN A 1 95  ? 23.980 6.915   -14.579 1.00 55.59  ? 103 GLN A CB  1 
ATOM   788  C  CG  . GLN A 1 95  ? 22.720 6.213   -14.095 1.00 63.08  ? 103 GLN A CG  1 
ATOM   789  C  CD  . GLN A 1 95  ? 22.356 5.055   -14.993 1.00 77.35  ? 103 GLN A CD  1 
ATOM   790  O  OE1 . GLN A 1 95  ? 22.011 5.232   -16.160 1.00 61.80  ? 103 GLN A OE1 1 
ATOM   791  N  NE2 . GLN A 1 95  ? 22.443 3.850   -14.451 1.00 78.72  ? 103 GLN A NE2 1 
ATOM   792  N  N   . LEU A 1 96  ? 27.379 6.708   -15.312 1.00 52.88  ? 104 LEU A N   1 
ATOM   793  C  CA  . LEU A 1 96  ? 28.493 7.266   -16.060 1.00 51.96  ? 104 LEU A CA  1 
ATOM   794  C  C   . LEU A 1 96  ? 29.486 6.151   -16.374 1.00 49.24  ? 104 LEU A C   1 
ATOM   795  O  O   . LEU A 1 96  ? 30.599 6.412   -16.826 1.00 52.77  ? 104 LEU A O   1 
ATOM   796  C  CB  . LEU A 1 96  ? 29.153 8.374   -15.234 1.00 48.30  ? 104 LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 96  ? 28.246 9.539   -14.841 1.00 54.70  ? 104 LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 96  ? 28.989 10.523  -13.951 1.00 55.68  ? 104 LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 96  ? 27.700 10.247  -16.071 1.00 59.06  ? 104 LEU A CD2 1 
ATOM   800  N  N   . LYS A 1 97  ? 29.062 4.908   -16.123 1.00 54.90  ? 105 LYS A N   1 
ATOM   801  C  CA  . LYS A 1 97  ? 29.896 3.740   -16.354 1.00 62.22  ? 105 LYS A CA  1 
ATOM   802  C  C   . LYS A 1 97  ? 31.180 3.866   -15.539 1.00 54.26  ? 105 LYS A C   1 
ATOM   803  O  O   . LYS A 1 97  ? 32.261 3.522   -16.012 1.00 50.00  ? 105 LYS A O   1 
ATOM   804  C  CB  . LYS A 1 97  ? 30.195 3.581   -17.849 1.00 70.24  ? 105 LYS A CB  1 
ATOM   805  C  CG  . LYS A 1 97  ? 28.971 3.401   -18.739 1.00 87.62  ? 105 LYS A CG  1 
ATOM   806  C  CD  . LYS A 1 97  ? 29.277 2.700   -20.050 1.00 101.76 ? 105 LYS A CD  1 
ATOM   807  C  CE  . LYS A 1 97  ? 30.083 3.539   -21.020 1.00 108.47 ? 105 LYS A CE  1 
ATOM   808  N  NZ  . LYS A 1 97  ? 29.235 4.113   -22.092 1.00 114.03 ? 105 LYS A NZ  1 
ATOM   809  N  N   . VAL A 1 98  ? 31.044 4.360   -14.304 1.00 60.57  ? 106 VAL A N   1 
ATOM   810  C  CA  . VAL A 1 98  ? 32.179 4.531   -13.414 1.00 66.13  ? 106 VAL A CA  1 
ATOM   811  C  C   . VAL A 1 98  ? 31.973 3.638   -12.195 1.00 59.00  ? 106 VAL A C   1 
ATOM   812  O  O   . VAL A 1 98  ? 30.998 3.799   -11.463 1.00 60.54  ? 106 VAL A O   1 
ATOM   813  C  CB  . VAL A 1 98  ? 32.362 6.006   -13.004 1.00 64.74  ? 106 VAL A CB  1 
ATOM   814  C  CG1 . VAL A 1 98  ? 33.507 6.182   -12.018 1.00 65.56  ? 106 VAL A CG1 1 
ATOM   815  C  CG2 . VAL A 1 98  ? 32.555 6.909   -14.213 1.00 60.61  ? 106 VAL A CG2 1 
ATOM   816  N  N   . ARG A 1 99  ? 32.893 2.687   -12.004 1.00 56.41  ? 107 ARG A N   1 
ATOM   817  C  CA  . ARG A 1 99  ? 32.879 1.823   -10.836 1.00 67.87  ? 107 ARG A CA  1 
ATOM   818  C  C   . ARG A 1 99  ? 33.656 2.491   -9.707  1.00 53.36  ? 107 ARG A C   1 
ATOM   819  O  O   . ARG A 1 99  ? 34.613 3.221   -9.950  1.00 51.79  ? 107 ARG A O   1 
ATOM   820  C  CB  . ARG A 1 99  ? 33.485 0.455   -11.165 1.00 76.11  ? 107 ARG A CB  1 
ATOM   821  C  CG  . ARG A 1 99  ? 32.471 -0.581  -11.629 1.00 89.59  ? 107 ARG A CG  1 
ATOM   822  C  CD  . ARG A 1 99  ? 33.045 -1.459  -12.722 1.00 102.54 ? 107 ARG A CD  1 
ATOM   823  N  NE  . ARG A 1 99  ? 33.809 -0.650  -13.661 1.00 128.27 ? 107 ARG A NE  1 
ATOM   824  C  CZ  . ARG A 1 99  ? 33.343 -0.190  -14.817 1.00 144.01 ? 107 ARG A CZ  1 
ATOM   825  N  NH1 . ARG A 1 99  ? 34.104 0.578   -15.576 1.00 135.79 ? 107 ARG A NH1 1 
ATOM   826  N  NH2 . ARG A 1 99  ? 32.110 -0.478  -15.199 1.00 140.51 ? 107 ARG A NH2 1 
ATOM   827  N  N   . PRO A 1 100 ? 33.262 2.256   -8.437  1.00 62.50  ? 108 PRO A N   1 
ATOM   828  C  CA  . PRO A 1 100 ? 34.015 2.766   -7.291  1.00 59.33  ? 108 PRO A CA  1 
ATOM   829  C  C   . PRO A 1 100 ? 35.510 2.474   -7.397  1.00 56.95  ? 108 PRO A C   1 
ATOM   830  O  O   . PRO A 1 100 ? 36.336 3.291   -6.995  1.00 61.24  ? 108 PRO A O   1 
ATOM   831  C  CB  . PRO A 1 100 ? 33.388 2.013   -6.109  1.00 62.15  ? 108 PRO A CB  1 
ATOM   832  C  CG  . PRO A 1 100 ? 31.961 1.765   -6.553  1.00 65.28  ? 108 PRO A CG  1 
ATOM   833  C  CD  . PRO A 1 100 ? 32.067 1.494   -8.040  1.00 57.89  ? 108 PRO A CD  1 
ATOM   834  N  N   . GLU A 1 101 ? 35.841 1.305   -7.958  1.00 51.04  ? 109 GLU A N   1 
ATOM   835  C  CA  . GLU A 1 101 ? 37.216 0.843   -8.046  1.00 54.04  ? 109 GLU A CA  1 
ATOM   836  C  C   . GLU A 1 101 ? 38.007 1.679   -9.050  1.00 55.20  ? 109 GLU A C   1 
ATOM   837  O  O   . GLU A 1 101 ? 39.230 1.574   -9.108  1.00 57.60  ? 109 GLU A O   1 
ATOM   838  C  CB  . GLU A 1 101 ? 37.273 -0.633  -8.452  1.00 66.57  ? 109 GLU A CB  1 
ATOM   839  C  CG  . GLU A 1 101 ? 36.212 -1.037  -9.460  1.00 83.12  ? 109 GLU A CG  1 
ATOM   840  C  CD  . GLU A 1 101 ? 34.960 -1.645  -8.849  1.00 97.08  ? 109 GLU A CD  1 
ATOM   841  O  OE1 . GLU A 1 101 ? 34.549 -2.729  -9.311  1.00 106.72 ? 109 GLU A OE1 1 
ATOM   842  O  OE2 . GLU A 1 101 ? 34.408 -1.045  -7.903  1.00 74.61  ? 109 GLU A OE2 1 
ATOM   843  N  N   . ASP A 1 102 ? 37.306 2.499   -9.841  1.00 59.12  ? 110 ASP A N   1 
ATOM   844  C  CA  . ASP A 1 102 ? 37.945 3.250   -10.911 1.00 62.97  ? 110 ASP A CA  1 
ATOM   845  C  C   . ASP A 1 102 ? 38.422 4.603   -10.388 1.00 54.01  ? 110 ASP A C   1 
ATOM   846  O  O   . ASP A 1 102 ? 39.085 5.346   -11.108 1.00 56.97  ? 110 ASP A O   1 
ATOM   847  C  CB  . ASP A 1 102 ? 37.003 3.428   -12.106 1.00 71.50  ? 110 ASP A CB  1 
ATOM   848  C  CG  . ASP A 1 102 ? 36.493 2.124   -12.697 1.00 79.21  ? 110 ASP A CG  1 
ATOM   849  O  OD1 . ASP A 1 102 ? 37.088 1.069   -12.397 1.00 81.82  ? 110 ASP A OD1 1 
ATOM   850  O  OD2 . ASP A 1 102 ? 35.493 2.173   -13.443 1.00 68.56  ? 110 ASP A OD2 1 
ATOM   851  N  N   . ILE A 1 103 ? 38.080 4.918   -9.133  1.00 51.15  ? 111 ILE A N   1 
ATOM   852  C  CA  . ILE A 1 103 ? 38.469 6.182   -8.527  1.00 52.61  ? 111 ILE A CA  1 
ATOM   853  C  C   . ILE A 1 103 ? 39.867 6.036   -7.928  1.00 50.40  ? 111 ILE A C   1 
ATOM   854  O  O   . ILE A 1 103 ? 40.093 5.195   -7.061  1.00 54.08  ? 111 ILE A O   1 
ATOM   855  C  CB  . ILE A 1 103 ? 37.440 6.630   -7.469  1.00 51.22  ? 111 ILE A CB  1 
ATOM   856  C  CG1 . ILE A 1 103 ? 36.001 6.511   -7.979  1.00 52.36  ? 111 ILE A CG1 1 
ATOM   857  C  CG2 . ILE A 1 103 ? 37.746 8.039   -6.984  1.00 61.24  ? 111 ILE A CG2 1 
ATOM   858  C  CD1 . ILE A 1 103 ? 35.662 7.475   -9.093  1.00 46.36  ? 111 ILE A CD1 1 
ATOM   859  N  N   . ARG A 1 104 ? 40.799 6.869   -8.404  1.00 47.19  ? 112 ARG A N   1 
ATOM   860  C  CA  . ARG A 1 104 ? 42.171 6.861   -7.922  1.00 50.93  ? 112 ARG A CA  1 
ATOM   861  C  C   . ARG A 1 104 ? 42.290 7.735   -6.677  1.00 53.48  ? 112 ARG A C   1 
ATOM   862  O  O   . ARG A 1 104 ? 43.032 7.405   -5.754  1.00 52.12  ? 112 ARG A O   1 
ATOM   863  C  CB  . ARG A 1 104 ? 43.113 7.372   -9.016  1.00 53.46  ? 112 ARG A CB  1 
ATOM   864  C  CG  . ARG A 1 104 ? 44.585 7.392   -8.628  1.00 57.97  ? 112 ARG A CG  1 
ATOM   865  C  CD  . ARG A 1 104 ? 45.429 7.894   -9.783  1.00 64.97  ? 112 ARG A CD  1 
ATOM   866  N  NE  . ARG A 1 104 ? 46.859 7.867   -9.512  1.00 78.73  ? 112 ARG A NE  1 
ATOM   867  C  CZ  . ARG A 1 104 ? 47.726 8.766   -9.964  1.00 82.45  ? 112 ARG A CZ  1 
ATOM   868  N  NH1 . ARG A 1 104 ? 47.320 9.726   -10.776 1.00 85.25  ? 112 ARG A NH1 1 
ATOM   869  N  NH2 . ARG A 1 104 ? 49.000 8.688   -9.622  1.00 83.57  ? 112 ARG A NH2 1 
ATOM   870  N  N   . TYR A 1 105 ? 41.559 8.856   -6.670  1.00 47.16  ? 113 TYR A N   1 
ATOM   871  C  CA  . TYR A 1 105 ? 41.656 9.828   -5.594  1.00 53.59  ? 113 TYR A CA  1 
ATOM   872  C  C   . TYR A 1 105 ? 40.265 10.293  -5.178  1.00 45.35  ? 113 TYR A C   1 
ATOM   873  O  O   . TYR A 1 105 ? 39.457 10.680  -6.018  1.00 43.85  ? 113 TYR A O   1 
ATOM   874  C  CB  . TYR A 1 105 ? 42.454 11.068  -6.008  1.00 50.60  ? 113 TYR A CB  1 
ATOM   875  C  CG  . TYR A 1 105 ? 43.936 10.835  -6.256  1.00 51.02  ? 113 TYR A CG  1 
ATOM   876  C  CD1 . TYR A 1 105 ? 44.763 10.343  -5.255  1.00 56.86  ? 113 TYR A CD1 1 
ATOM   877  C  CD2 . TYR A 1 105 ? 44.510 11.125  -7.487  1.00 58.40  ? 113 TYR A CD2 1 
ATOM   878  C  CE1 . TYR A 1 105 ? 46.116 10.138  -5.473  1.00 57.85  ? 113 TYR A CE1 1 
ATOM   879  C  CE2 . TYR A 1 105 ? 45.860 10.925  -7.718  1.00 65.03  ? 113 TYR A CE2 1 
ATOM   880  C  CZ  . TYR A 1 105 ? 46.665 10.430  -6.708  1.00 65.13  ? 113 TYR A CZ  1 
ATOM   881  O  OH  . TYR A 1 105 ? 47.997 10.231  -6.933  1.00 68.66  ? 113 TYR A OH  1 
ATOM   882  N  N   . VAL A 1 106 ? 40.015 10.265  -3.867  1.00 47.59  ? 114 VAL A N   1 
ATOM   883  C  CA  . VAL A 1 106 ? 38.862 10.927  -3.285  1.00 47.88  ? 114 VAL A CA  1 
ATOM   884  C  C   . VAL A 1 106 ? 39.367 12.094  -2.441  1.00 45.85  ? 114 VAL A C   1 
ATOM   885  O  O   . VAL A 1 106 ? 40.228 11.912  -1.585  1.00 46.19  ? 114 VAL A O   1 
ATOM   886  C  CB  . VAL A 1 106 ? 38.013 9.962   -2.435  1.00 45.74  ? 114 VAL A CB  1 
ATOM   887  C  CG1 . VAL A 1 106 ? 36.756 10.643  -1.916  1.00 48.10  ? 114 VAL A CG1 1 
ATOM   888  C  CG2 . VAL A 1 106 ? 37.659 8.689   -3.189  1.00 48.88  ? 114 VAL A CG2 1 
ATOM   889  N  N   . VAL A 1 107 ? 38.834 13.293  -2.698  1.00 43.22  ? 115 VAL A N   1 
ATOM   890  C  CA  . VAL A 1 107 ? 39.147 14.454  -1.882  1.00 43.44  ? 115 VAL A CA  1 
ATOM   891  C  C   . VAL A 1 107 ? 37.954 14.752  -0.977  1.00 41.88  ? 115 VAL A C   1 
ATOM   892  O  O   . VAL A 1 107 ? 36.893 15.151  -1.450  1.00 46.43  ? 115 VAL A O   1 
ATOM   893  C  CB  . VAL A 1 107 ? 39.513 15.680  -2.740  1.00 41.77  ? 115 VAL A CB  1 
ATOM   894  C  CG1 . VAL A 1 107 ? 39.780 16.906  -1.878  1.00 38.92  ? 115 VAL A CG1 1 
ATOM   895  C  CG2 . VAL A 1 107 ? 40.697 15.402  -3.652  1.00 44.12  ? 115 VAL A CG2 1 
ATOM   896  N  N   . ALA A 1 108 ? 38.151 14.553  0.330   1.00 50.92  ? 116 ALA A N   1 
ATOM   897  C  CA  . ALA A 1 108 ? 37.142 14.858  1.330   1.00 49.44  ? 116 ALA A CA  1 
ATOM   898  C  C   . ALA A 1 108 ? 37.315 16.296  1.816   1.00 47.98  ? 116 ALA A C   1 
ATOM   899  O  O   . ALA A 1 108 ? 38.223 16.583  2.593   1.00 51.28  ? 116 ALA A O   1 
ATOM   900  C  CB  . ALA A 1 108 ? 37.256 13.876  2.470   1.00 49.33  ? 116 ALA A CB  1 
ATOM   901  N  N   . SER A 1 109 ? 36.437 17.195  1.354   1.00 45.89  ? 117 SER A N   1 
ATOM   902  C  CA  . SER A 1 109 ? 36.481 18.592  1.761   1.00 42.23  ? 117 SER A CA  1 
ATOM   903  C  C   . SER A 1 109 ? 36.538 18.681  3.284   1.00 43.56  ? 117 SER A C   1 
ATOM   904  O  O   . SER A 1 109 ? 37.292 19.474  3.841   1.00 40.77  ? 117 SER A O   1 
ATOM   905  C  CB  . SER A 1 109 ? 35.303 19.363  1.207   1.00 44.03  ? 117 SER A CB  1 
ATOM   906  O  OG  . SER A 1 109 ? 34.076 18.887  1.742   1.00 42.89  ? 117 SER A OG  1 
ATOM   907  N  N   . HIS A 1 110 ? 35.706 17.862  3.934   1.00 40.75  ? 118 HIS A N   1 
ATOM   908  C  CA  . HIS A 1 110 ? 35.703 17.680  5.376   1.00 40.65  ? 118 HIS A CA  1 
ATOM   909  C  C   . HIS A 1 110 ? 34.903 16.405  5.635   1.00 43.46  ? 118 HIS A C   1 
ATOM   910  O  O   . HIS A 1 110 ? 34.427 15.787  4.686   1.00 46.95  ? 118 HIS A O   1 
ATOM   911  C  CB  . HIS A 1 110 ? 35.225 18.953  6.088   1.00 39.03  ? 118 HIS A CB  1 
ATOM   912  C  CG  . HIS A 1 110 ? 33.826 19.367  5.777   1.00 40.05  ? 118 HIS A CG  1 
ATOM   913  N  ND1 . HIS A 1 110 ? 33.344 19.505  4.493   1.00 44.29  ? 118 HIS A ND1 1 
ATOM   914  C  CD2 . HIS A 1 110 ? 32.808 19.678  6.590   1.00 44.19  ? 118 HIS A CD2 1 
ATOM   915  C  CE1 . HIS A 1 110 ? 32.075 19.889  4.543   1.00 47.62  ? 118 HIS A CE1 1 
ATOM   916  N  NE2 . HIS A 1 110 ? 31.729 20.000  5.806   1.00 48.19  ? 118 HIS A NE2 1 
ATOM   917  N  N   . LEU A 1 111 ? 34.768 15.995  6.900   1.00 38.25  ? 119 LEU A N   1 
ATOM   918  C  CA  . LEU A 1 111 ? 34.244 14.667  7.181   1.00 37.84  ? 119 LEU A CA  1 
ATOM   919  C  C   . LEU A 1 111 ? 32.845 14.743  7.791   1.00 35.92  ? 119 LEU A C   1 
ATOM   920  O  O   . LEU A 1 111 ? 32.415 13.815  8.473   1.00 46.50  ? 119 LEU A O   1 
ATOM   921  C  CB  . LEU A 1 111 ? 35.233 13.932  8.090   1.00 39.25  ? 119 LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 111 ? 36.536 13.515  7.409   1.00 41.37  ? 119 LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 111 ? 37.470 12.821  8.387   1.00 45.04  ? 119 LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 111 ? 36.257 12.615  6.214   1.00 41.76  ? 119 LEU A CD2 1 
ATOM   925  N  N   . HIS A 1 112 ? 32.130 15.837  7.509   1.00 37.04  ? 120 HIS A N   1 
ATOM   926  C  CA  . HIS A 1 112 ? 30.731 15.968  7.885   1.00 40.80  ? 120 HIS A CA  1 
ATOM   927  C  C   . HIS A 1 112 ? 29.895 14.886  7.203   1.00 42.09  ? 120 HIS A C   1 
ATOM   928  O  O   . HIS A 1 112 ? 30.311 14.316  6.197   1.00 45.06  ? 120 HIS A O   1 
ATOM   929  C  CB  . HIS A 1 112 ? 30.209 17.367  7.542   1.00 44.83  ? 120 HIS A CB  1 
ATOM   930  C  CG  . HIS A 1 112 ? 30.492 18.395  8.585   1.00 42.45  ? 120 HIS A CG  1 
ATOM   931  N  ND1 . HIS A 1 112 ? 30.365 19.746  8.346   1.00 46.03  ? 120 HIS A ND1 1 
ATOM   932  C  CD2 . HIS A 1 112 ? 30.897 18.279  9.858   1.00 50.30  ? 120 HIS A CD2 1 
ATOM   933  C  CE1 . HIS A 1 112 ? 30.680 20.415  9.447   1.00 51.88  ? 120 HIS A CE1 1 
ATOM   934  N  NE2 . HIS A 1 112 ? 31.005 19.544  10.378  1.00 50.09  ? 120 HIS A NE2 1 
ATOM   935  N  N   . LEU A 1 113 ? 28.698 14.645  7.755   1.00 46.27  ? 121 LEU A N   1 
ATOM   936  C  CA  . LEU A 1 113 ? 27.859 13.512  7.389   1.00 50.09  ? 121 LEU A CA  1 
ATOM   937  C  C   . LEU A 1 113 ? 27.420 13.574  5.927   1.00 47.58  ? 121 LEU A C   1 
ATOM   938  O  O   . LEU A 1 113 ? 27.069 12.548  5.350   1.00 48.76  ? 121 LEU A O   1 
ATOM   939  C  CB  . LEU A 1 113 ? 26.636 13.472  8.315   1.00 48.92  ? 121 LEU A CB  1 
ATOM   940  C  CG  . LEU A 1 113 ? 25.625 14.610  8.166   1.00 50.97  ? 121 LEU A CG  1 
ATOM   941  C  CD1 . LEU A 1 113 ? 24.418 14.372  9.061   1.00 49.14  ? 121 LEU A CD1 1 
ATOM   942  C  CD2 . LEU A 1 113 ? 26.252 15.960  8.484   1.00 51.69  ? 121 LEU A CD2 1 
ATOM   943  N  N   . ASN A 1 114 ? 27.433 14.770  5.331   1.00 48.78  ? 122 ASN A N   1 
ATOM   944  C  CA  . ASN A 1 114 ? 26.832 14.964  4.020   1.00 48.47  ? 122 ASN A CA  1 
ATOM   945  C  C   . ASN A 1 114 ? 27.924 15.173  2.974   1.00 48.94  ? 122 ASN A C   1 
ATOM   946  O  O   . ASN A 1 114 ? 27.641 15.603  1.858   1.00 49.97  ? 122 ASN A O   1 
ATOM   947  C  CB  . ASN A 1 114 ? 25.816 16.111  4.038   1.00 52.61  ? 122 ASN A CB  1 
ATOM   948  C  CG  . ASN A 1 114 ? 26.425 17.450  4.394   1.00 50.98  ? 122 ASN A CG  1 
ATOM   949  O  OD1 . ASN A 1 114 ? 26.107 18.466  3.780   1.00 68.16  ? 122 ASN A OD1 1 
ATOM   950  N  ND2 . ASN A 1 114 ? 27.283 17.471  5.400   1.00 58.97  ? 122 ASN A ND2 1 
ATOM   951  N  N   . HIS A 1 115 ? 29.171 14.850  3.341   1.00 47.52  ? 123 HIS A N   1 
ATOM   952  C  CA  . HIS A 1 115 ? 30.285 14.952  2.414   1.00 42.73  ? 123 HIS A CA  1 
ATOM   953  C  C   . HIS A 1 115 ? 31.131 13.680  2.440   1.00 39.73  ? 123 HIS A C   1 
ATOM   954  O  O   . HIS A 1 115 ? 31.789 13.366  1.451   1.00 44.93  ? 123 HIS A O   1 
ATOM   955  C  CB  . HIS A 1 115 ? 31.135 16.195  2.703   1.00 44.72  ? 123 HIS A CB  1 
ATOM   956  C  CG  . HIS A 1 115 ? 30.383 17.482  2.609   1.00 42.35  ? 123 HIS A CG  1 
ATOM   957  N  ND1 . HIS A 1 115 ? 30.519 18.357  1.552   1.00 36.72  ? 123 HIS A ND1 1 
ATOM   958  C  CD2 . HIS A 1 115 ? 29.479 18.031  3.431   1.00 47.21  ? 123 HIS A CD2 1 
ATOM   959  C  CE1 . HIS A 1 115 ? 29.726 19.402  1.747   1.00 45.81  ? 123 HIS A CE1 1 
ATOM   960  N  NE2 . HIS A 1 115 ? 29.085 19.226  2.883   1.00 44.85  ? 123 HIS A NE2 1 
ATOM   961  N  N   . ALA A 1 116 ? 31.117 12.951  3.563   1.00 45.66  ? 124 ALA A N   1 
ATOM   962  C  CA  . ALA A 1 116 ? 31.987 11.795  3.728   1.00 47.33  ? 124 ALA A CA  1 
ATOM   963  C  C   . ALA A 1 116 ? 31.174 10.502  3.806   1.00 46.88  ? 124 ALA A C   1 
ATOM   964  O  O   . ALA A 1 116 ? 31.713 9.447   4.134   1.00 43.38  ? 124 ALA A O   1 
ATOM   965  C  CB  . ALA A 1 116 ? 32.842 11.976  4.960   1.00 44.42  ? 124 ALA A CB  1 
ATOM   966  N  N   . GLY A 1 117 ? 29.881 10.592  3.480   1.00 49.18  ? 125 GLY A N   1 
ATOM   967  C  CA  . GLY A 1 117 ? 28.948 9.489   3.653   1.00 49.35  ? 125 GLY A CA  1 
ATOM   968  C  C   . GLY A 1 117 ? 29.375 8.194   2.960   1.00 49.19  ? 125 GLY A C   1 
ATOM   969  O  O   . GLY A 1 117 ? 29.146 7.111   3.495   1.00 53.98  ? 125 GLY A O   1 
ATOM   970  N  N   . CYS A 1 118 ? 29.977 8.294   1.767   1.00 46.42  ? 126 CYS A N   1 
ATOM   971  C  CA  . CYS A 1 118 ? 30.227 7.107   0.963   1.00 46.88  ? 126 CYS A CA  1 
ATOM   972  C  C   . CYS A 1 118 ? 31.720 6.865   0.751   1.00 46.73  ? 126 CYS A C   1 
ATOM   973  O  O   . CYS A 1 118 ? 32.099 6.162   -0.183  1.00 51.15  ? 126 CYS A O   1 
ATOM   974  C  CB  . CYS A 1 118 ? 29.549 7.203   -0.399  1.00 52.16  ? 126 CYS A CB  1 
ATOM   975  S  SG  . CYS A 1 118 ? 27.753 7.421   -0.299  1.00 52.24  ? 126 CYS A SG  1 
ATOM   976  N  N   . LEU A 1 119 ? 32.564 7.430   1.619   1.00 46.45  ? 127 LEU A N   1 
ATOM   977  C  CA  . LEU A 1 119 ? 33.997 7.193   1.528   1.00 43.45  ? 127 LEU A CA  1 
ATOM   978  C  C   . LEU A 1 119 ? 34.272 5.689   1.486   1.00 39.44  ? 127 LEU A C   1 
ATOM   979  O  O   . LEU A 1 119 ? 35.215 5.253   0.832   1.00 44.52  ? 127 LEU A O   1 
ATOM   980  C  CB  . LEU A 1 119 ? 34.707 7.843   2.721   1.00 48.46  ? 127 LEU A CB  1 
ATOM   981  C  CG  . LEU A 1 119 ? 34.923 9.354   2.638   1.00 55.83  ? 127 LEU A CG  1 
ATOM   982  C  CD1 . LEU A 1 119 ? 35.593 9.866   3.903   1.00 64.21  ? 127 LEU A CD1 1 
ATOM   983  C  CD2 . LEU A 1 119 ? 35.754 9.728   1.418   1.00 55.21  ? 127 LEU A CD2 1 
ATOM   984  N  N   . GLU A 1 120 ? 33.444 4.903   2.185   1.00 45.13  ? 128 GLU A N   1 
ATOM   985  C  CA  . GLU A 1 120 ? 33.715 3.486   2.391   1.00 54.91  ? 128 GLU A CA  1 
ATOM   986  C  C   . GLU A 1 120 ? 33.746 2.727   1.064   1.00 51.49  ? 128 GLU A C   1 
ATOM   987  O  O   . GLU A 1 120 ? 34.341 1.655   0.986   1.00 54.25  ? 128 GLU A O   1 
ATOM   988  C  CB  . GLU A 1 120 ? 32.688 2.869   3.344   1.00 60.17  ? 128 GLU A CB  1 
ATOM   989  C  CG  . GLU A 1 120 ? 31.250 2.977   2.874   1.00 60.35  ? 128 GLU A CG  1 
ATOM   990  C  CD  . GLU A 1 120 ? 30.238 2.611   3.946   1.00 64.10  ? 128 GLU A CD  1 
ATOM   991  O  OE1 . GLU A 1 120 ? 30.064 1.403   4.208   1.00 67.12  ? 128 GLU A OE1 1 
ATOM   992  O  OE2 . GLU A 1 120 ? 29.651 3.536   4.542   1.00 65.31  ? 128 GLU A OE2 1 
ATOM   993  N  N   . MET A 1 121 ? 33.116 3.281   0.022   1.00 51.25  ? 129 MET A N   1 
ATOM   994  C  CA  . MET A 1 121 ? 32.995 2.589   -1.253  1.00 48.78  ? 129 MET A CA  1 
ATOM   995  C  C   . MET A 1 121 ? 34.344 2.562   -1.969  1.00 52.07  ? 129 MET A C   1 
ATOM   996  O  O   . MET A 1 121 ? 34.608 1.664   -2.764  1.00 54.44  ? 129 MET A O   1 
ATOM   997  C  CB  . MET A 1 121 ? 31.981 3.282   -2.170  1.00 52.99  ? 129 MET A CB  1 
ATOM   998  C  CG  . MET A 1 121 ? 30.582 3.363   -1.589  1.00 63.87  ? 129 MET A CG  1 
ATOM   999  S  SD  . MET A 1 121 ? 29.398 4.165   -2.708  1.00 76.47  ? 129 MET A SD  1 
ATOM   1000 C  CE  . MET A 1 121 ? 30.373 4.280   -4.208  1.00 75.80  ? 129 MET A CE  1 
ATOM   1001 N  N   . PHE A 1 122 ? 35.188 3.561   -1.693  1.00 51.15  ? 130 PHE A N   1 
ATOM   1002 C  CA  . PHE A 1 122 ? 36.381 3.786   -2.491  1.00 47.51  ? 130 PHE A CA  1 
ATOM   1003 C  C   . PHE A 1 122 ? 37.582 3.143   -1.804  1.00 48.72  ? 130 PHE A C   1 
ATOM   1004 O  O   . PHE A 1 122 ? 38.379 3.816   -1.156  1.00 67.05  ? 130 PHE A O   1 
ATOM   1005 C  CB  . PHE A 1 122 ? 36.507 5.284   -2.767  1.00 45.35  ? 130 PHE A CB  1 
ATOM   1006 C  CG  . PHE A 1 122 ? 35.223 5.858   -3.304  1.00 47.97  ? 130 PHE A CG  1 
ATOM   1007 C  CD1 . PHE A 1 122 ? 34.787 5.536   -4.580  1.00 52.30  ? 130 PHE A CD1 1 
ATOM   1008 C  CD2 . PHE A 1 122 ? 34.405 6.642   -2.507  1.00 52.43  ? 130 PHE A CD2 1 
ATOM   1009 C  CE1 . PHE A 1 122 ? 33.588 6.032   -5.065  1.00 47.94  ? 130 PHE A CE1 1 
ATOM   1010 C  CE2 . PHE A 1 122 ? 33.206 7.136   -2.994  1.00 55.26  ? 130 PHE A CE2 1 
ATOM   1011 C  CZ  . PHE A 1 122 ? 32.800 6.831   -4.271  1.00 54.50  ? 130 PHE A CZ  1 
ATOM   1012 N  N   . THR A 1 123 ? 37.693 1.823   -1.989  1.00 48.23  ? 131 THR A N   1 
ATOM   1013 C  CA  . THR A 1 123 ? 38.681 1.007   -1.305  1.00 51.89  ? 131 THR A CA  1 
ATOM   1014 C  C   . THR A 1 123 ? 39.944 0.876   -2.152  1.00 49.56  ? 131 THR A C   1 
ATOM   1015 O  O   . THR A 1 123 ? 40.944 0.334   -1.687  1.00 55.65  ? 131 THR A O   1 
ATOM   1016 C  CB  . THR A 1 123 ? 38.099 -0.373  -0.976  1.00 57.30  ? 131 THR A CB  1 
ATOM   1017 O  OG1 . THR A 1 123 ? 37.624 -0.945  -2.195  1.00 61.92  ? 131 THR A OG1 1 
ATOM   1018 C  CG2 . THR A 1 123 ? 36.971 -0.315  0.031   1.00 54.15  ? 131 THR A CG2 1 
ATOM   1019 N  N   . ASN A 1 124 ? 39.897 1.372   -3.394  1.00 49.96  ? 132 ASN A N   1 
ATOM   1020 C  CA  . ASN A 1 124 ? 41.055 1.309   -4.271  1.00 57.04  ? 132 ASN A CA  1 
ATOM   1021 C  C   . ASN A 1 124 ? 41.578 2.722   -4.525  1.00 53.57  ? 132 ASN A C   1 
ATOM   1022 O  O   . ASN A 1 124 ? 42.435 2.929   -5.382  1.00 51.69  ? 132 ASN A O   1 
ATOM   1023 C  CB  . ASN A 1 124 ? 40.737 0.571   -5.575  1.00 61.91  ? 132 ASN A CB  1 
ATOM   1024 C  CG  . ASN A 1 124 ? 41.978 0.049   -6.268  1.00 72.83  ? 132 ASN A CG  1 
ATOM   1025 O  OD1 . ASN A 1 124 ? 42.121 0.184   -7.481  1.00 87.02  ? 132 ASN A OD1 1 
ATOM   1026 N  ND2 . ASN A 1 124 ? 42.875 -0.558  -5.506  1.00 88.89  ? 132 ASN A ND2 1 
ATOM   1027 N  N   . ALA A 1 125 ? 41.074 3.686   -3.749  1.00 50.23  ? 133 ALA A N   1 
ATOM   1028 C  CA  . ALA A 1 125 ? 41.428 5.084   -3.932  1.00 53.33  ? 133 ALA A CA  1 
ATOM   1029 C  C   . ALA A 1 125 ? 42.348 5.545   -2.806  1.00 56.74  ? 133 ALA A C   1 
ATOM   1030 O  O   . ALA A 1 125 ? 42.423 4.911   -1.755  1.00 50.70  ? 133 ALA A O   1 
ATOM   1031 C  CB  . ALA A 1 125 ? 40.174 5.923   -3.981  1.00 51.15  ? 133 ALA A CB  1 
ATOM   1032 N  N   . THR A 1 126 ? 43.047 6.658   -3.045  1.00 52.89  ? 134 THR A N   1 
ATOM   1033 C  CA  . THR A 1 126 ? 43.729 7.377   -1.984  1.00 48.05  ? 134 THR A CA  1 
ATOM   1034 C  C   . THR A 1 126 ? 42.794 8.481   -1.497  1.00 45.23  ? 134 THR A C   1 
ATOM   1035 O  O   . THR A 1 126 ? 42.407 9.354   -2.271  1.00 53.57  ? 134 THR A O   1 
ATOM   1036 C  CB  . THR A 1 126 ? 45.091 7.902   -2.460  1.00 49.02  ? 134 THR A CB  1 
ATOM   1037 O  OG1 . THR A 1 126 ? 45.868 6.787   -2.895  1.00 55.63  ? 134 THR A OG1 1 
ATOM   1038 C  CG2 . THR A 1 126 ? 45.846 8.653   -1.386  1.00 56.17  ? 134 THR A CG2 1 
ATOM   1039 N  N   . ILE A 1 127 ? 42.405 8.405   -0.219  1.00 44.16  ? 135 ILE A N   1 
ATOM   1040 C  CA  . ILE A 1 127 ? 41.498 9.377   0.367   1.00 43.81  ? 135 ILE A CA  1 
ATOM   1041 C  C   . ILE A 1 127 ? 42.319 10.536  0.920   1.00 46.72  ? 135 ILE A C   1 
ATOM   1042 O  O   . ILE A 1 127 ? 43.069 10.372  1.880   1.00 45.24  ? 135 ILE A O   1 
ATOM   1043 C  CB  . ILE A 1 127 ? 40.627 8.758   1.478   1.00 50.40  ? 135 ILE A CB  1 
ATOM   1044 C  CG1 . ILE A 1 127 ? 40.092 7.373   1.104   1.00 53.51  ? 135 ILE A CG1 1 
ATOM   1045 C  CG2 . ILE A 1 127 ? 39.512 9.721   1.863   1.00 51.23  ? 135 ILE A CG2 1 
ATOM   1046 C  CD1 . ILE A 1 127 ? 39.162 7.365   -0.086  1.00 56.55  ? 135 ILE A CD1 1 
ATOM   1047 N  N   . ILE A 1 128 ? 42.148 11.710  0.309   1.00 42.24  ? 136 ILE A N   1 
ATOM   1048 C  CA  . ILE A 1 128 ? 42.867 12.897  0.726   1.00 43.58  ? 136 ILE A CA  1 
ATOM   1049 C  C   . ILE A 1 128 ? 41.975 13.696  1.666   1.00 42.85  ? 136 ILE A C   1 
ATOM   1050 O  O   . ILE A 1 128 ? 40.849 14.050  1.324   1.00 42.68  ? 136 ILE A O   1 
ATOM   1051 C  CB  . ILE A 1 128 ? 43.317 13.713  -0.498  1.00 48.16  ? 136 ILE A CB  1 
ATOM   1052 C  CG1 . ILE A 1 128 ? 44.140 12.843  -1.451  1.00 48.75  ? 136 ILE A CG1 1 
ATOM   1053 C  CG2 . ILE A 1 128 ? 44.069 14.963  -0.065  1.00 47.38  ? 136 ILE A CG2 1 
ATOM   1054 C  CD1 . ILE A 1 128 ? 44.356 13.451  -2.811  1.00 54.86  ? 136 ILE A CD1 1 
ATOM   1055 N  N   . VAL A 1 129 ? 42.507 13.964  2.860   1.00 44.64  ? 137 VAL A N   1 
ATOM   1056 C  CA  . VAL A 1 129 ? 41.740 14.598  3.913   1.00 41.98  ? 137 VAL A CA  1 
ATOM   1057 C  C   . VAL A 1 129 ? 42.691 15.436  4.758   1.00 41.05  ? 137 VAL A C   1 
ATOM   1058 O  O   . VAL A 1 129 ? 43.864 15.099  4.897   1.00 43.40  ? 137 VAL A O   1 
ATOM   1059 C  CB  . VAL A 1 129 ? 41.008 13.549  4.770   1.00 41.98  ? 137 VAL A CB  1 
ATOM   1060 C  CG1 . VAL A 1 129 ? 41.985 12.682  5.550   1.00 45.19  ? 137 VAL A CG1 1 
ATOM   1061 C  CG2 . VAL A 1 129 ? 39.996 14.196  5.700   1.00 41.76  ? 137 VAL A CG2 1 
ATOM   1062 N  N   . HIS A 1 130 ? 42.166 16.535  5.306   1.00 39.06  ? 138 HIS A N   1 
ATOM   1063 C  CA  . HIS A 1 130 ? 42.933 17.371  6.209   1.00 41.09  ? 138 HIS A CA  1 
ATOM   1064 C  C   . HIS A 1 130 ? 43.187 16.581  7.489   1.00 40.18  ? 138 HIS A C   1 
ATOM   1065 O  O   . HIS A 1 130 ? 42.279 15.941  8.011   1.00 44.63  ? 138 HIS A O   1 
ATOM   1066 C  CB  . HIS A 1 130 ? 42.203 18.692  6.471   1.00 45.66  ? 138 HIS A CB  1 
ATOM   1067 C  CG  . HIS A 1 130 ? 43.116 19.743  6.999   1.00 45.66  ? 138 HIS A CG  1 
ATOM   1068 N  ND1 . HIS A 1 130 ? 43.650 19.697  8.268   1.00 41.36  ? 138 HIS A ND1 1 
ATOM   1069 C  CD2 . HIS A 1 130 ? 43.604 20.850  6.427   1.00 50.54  ? 138 HIS A CD2 1 
ATOM   1070 C  CE1 . HIS A 1 130 ? 44.430 20.753  8.449   1.00 46.75  ? 138 HIS A CE1 1 
ATOM   1071 N  NE2 . HIS A 1 130 ? 44.417 21.466  7.344   1.00 52.32  ? 138 HIS A NE2 1 
ATOM   1072 N  N   . GLU A 1 131 ? 44.427 16.631  7.989   1.00 43.15  ? 139 GLU A N   1 
ATOM   1073 C  CA  . GLU A 1 131 ? 44.810 15.794  9.114   1.00 47.02  ? 139 GLU A CA  1 
ATOM   1074 C  C   . GLU A 1 131 ? 44.017 16.204  10.354  1.00 39.00  ? 139 GLU A C   1 
ATOM   1075 O  O   . GLU A 1 131 ? 43.635 15.349  11.149  1.00 43.62  ? 139 GLU A O   1 
ATOM   1076 C  CB  . GLU A 1 131 ? 46.323 15.832  9.353   1.00 48.51  ? 139 GLU A CB  1 
ATOM   1077 C  CG  . GLU A 1 131 ? 46.835 17.103  10.006  1.00 53.13  ? 139 GLU A CG  1 
ATOM   1078 C  CD  . GLU A 1 131 ? 48.319 17.059  10.338  1.00 61.41  ? 139 GLU A CD  1 
ATOM   1079 O  OE1 . GLU A 1 131 ? 48.895 15.950  10.314  1.00 51.32  ? 139 GLU A OE1 1 
ATOM   1080 O  OE2 . GLU A 1 131 ? 48.902 18.132  10.600  1.00 49.35  ? 139 GLU A OE2 1 
ATOM   1081 N  N   . ASP A 1 132 ? 43.756 17.507  10.512  1.00 35.37  ? 140 ASP A N   1 
ATOM   1082 C  CA  . ASP A 1 132 ? 43.046 17.985  11.688  1.00 35.97  ? 140 ASP A CA  1 
ATOM   1083 C  C   . ASP A 1 132 ? 41.594 17.513  11.634  1.00 32.89  ? 140 ASP A C   1 
ATOM   1084 O  O   . ASP A 1 132 ? 40.994 17.244  12.670  1.00 41.72  ? 140 ASP A O   1 
ATOM   1085 C  CB  . ASP A 1 132 ? 43.138 19.506  11.841  1.00 38.34  ? 140 ASP A CB  1 
ATOM   1086 C  CG  . ASP A 1 132 ? 44.540 20.011  12.138  1.00 36.79  ? 140 ASP A CG  1 
ATOM   1087 O  OD1 . ASP A 1 132 ? 45.228 19.374  12.959  1.00 44.63  ? 140 ASP A OD1 1 
ATOM   1088 O  OD2 . ASP A 1 132 ? 44.923 21.054  11.567  1.00 39.95  ? 140 ASP A OD2 1 
ATOM   1089 N  N   . GLU A 1 133 ? 41.036 17.417  10.422  1.00 39.99  ? 141 GLU A N   1 
ATOM   1090 C  CA  . GLU A 1 133 ? 39.676 16.931  10.249  1.00 40.78  ? 141 GLU A CA  1 
ATOM   1091 C  C   . GLU A 1 133 ? 39.619 15.446  10.592  1.00 38.32  ? 141 GLU A C   1 
ATOM   1092 O  O   . GLU A 1 133 ? 38.695 14.990  11.261  1.00 38.12  ? 141 GLU A O   1 
ATOM   1093 C  CB  . GLU A 1 133 ? 39.190 17.135  8.813   1.00 40.95  ? 141 GLU A CB  1 
ATOM   1094 C  CG  . GLU A 1 133 ? 37.708 16.858  8.640   1.00 41.50  ? 141 GLU A CG  1 
ATOM   1095 C  CD  . GLU A 1 133 ? 36.805 17.881  9.308   1.00 40.84  ? 141 GLU A CD  1 
ATOM   1096 O  OE1 . GLU A 1 133 ? 37.343 18.843  9.890   1.00 42.35  ? 141 GLU A OE1 1 
ATOM   1097 O  OE2 . GLU A 1 133 ? 35.570 17.713  9.245   1.00 45.98  ? 141 GLU A OE2 1 
ATOM   1098 N  N   . PHE A 1 134 ? 40.617 14.703  10.107  1.00 39.77  ? 142 PHE A N   1 
ATOM   1099 C  CA  . PHE A 1 134 ? 40.699 13.270  10.325  1.00 44.27  ? 142 PHE A CA  1 
ATOM   1100 C  C   . PHE A 1 134 ? 40.796 13.003  11.824  1.00 49.60  ? 142 PHE A C   1 
ATOM   1101 O  O   . PHE A 1 134 ? 40.035 12.213  12.379  1.00 47.03  ? 142 PHE A O   1 
ATOM   1102 C  CB  . PHE A 1 134 ? 41.901 12.713  9.556   1.00 44.28  ? 142 PHE A CB  1 
ATOM   1103 C  CG  . PHE A 1 134 ? 41.962 11.213  9.422   1.00 42.81  ? 142 PHE A CG  1 
ATOM   1104 C  CD1 . PHE A 1 134 ? 40.843 10.480  9.059   1.00 51.10  ? 142 PHE A CD1 1 
ATOM   1105 C  CD2 . PHE A 1 134 ? 43.159 10.539  9.606   1.00 45.25  ? 142 PHE A CD2 1 
ATOM   1106 C  CE1 . PHE A 1 134 ? 40.914 9.102   8.918   1.00 51.40  ? 142 PHE A CE1 1 
ATOM   1107 C  CE2 . PHE A 1 134 ? 43.229 9.163   9.459   1.00 48.39  ? 142 PHE A CE2 1 
ATOM   1108 C  CZ  . PHE A 1 134 ? 42.107 8.447   9.116   1.00 53.23  ? 142 PHE A CZ  1 
ATOM   1109 N  N   . ASN A 1 135 ? 41.745 13.693  12.465  1.00 48.30  ? 143 ASN A N   1 
ATOM   1110 C  CA  . ASN A 1 135 ? 41.975 13.573  13.893  1.00 42.66  ? 143 ASN A CA  1 
ATOM   1111 C  C   . ASN A 1 135 ? 40.678 13.853  14.648  1.00 41.74  ? 143 ASN A C   1 
ATOM   1112 O  O   . ASN A 1 135 ? 40.271 13.064  15.498  1.00 43.91  ? 143 ASN A O   1 
ATOM   1113 C  CB  . ASN A 1 135 ? 43.111 14.495  14.342  1.00 40.51  ? 143 ASN A CB  1 
ATOM   1114 C  CG  . ASN A 1 135 ? 44.465 14.034  13.845  1.00 41.23  ? 143 ASN A CG  1 
ATOM   1115 O  OD1 . ASN A 1 135 ? 44.614 12.897  13.401  1.00 43.37  ? 143 ASN A OD1 1 
ATOM   1116 N  ND2 . ASN A 1 135 ? 45.461 14.901  13.925  1.00 37.55  ? 143 ASN A ND2 1 
ATOM   1117 N  N   . GLY A 1 136 ? 40.036 14.981  14.328  1.00 41.28  ? 144 GLY A N   1 
ATOM   1118 C  CA  . GLY A 1 136 ? 38.825 15.402  15.015  1.00 41.84  ? 144 GLY A CA  1 
ATOM   1119 C  C   . GLY A 1 136 ? 37.714 14.356  14.944  1.00 41.76  ? 144 GLY A C   1 
ATOM   1120 O  O   . GLY A 1 136 ? 36.971 14.172  15.905  1.00 45.59  ? 144 GLY A O   1 
ATOM   1121 N  N   . ALA A 1 137 ? 37.601 13.681  13.795  1.00 39.84  ? 145 ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 137 ? 36.539 12.711  13.589  1.00 42.07  ? 145 ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 137 ? 36.895 11.400  14.285  1.00 40.87  ? 145 ALA A C   1 
ATOM   1124 O  O   . ALA A 1 137 ? 36.022 10.726  14.825  1.00 48.49  ? 145 ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 137 ? 36.295 12.506  12.115  1.00 44.16  ? 145 ALA A CB  1 
ATOM   1126 N  N   . LEU A 1 138 ? 38.182 11.045  14.266  1.00 44.39  ? 146 LEU A N   1 
ATOM   1127 C  CA  . LEU A 1 138 ? 38.630 9.838   14.938  1.00 44.77  ? 146 LEU A CA  1 
ATOM   1128 C  C   . LEU A 1 138 ? 38.422 9.979   16.448  1.00 45.96  ? 146 LEU A C   1 
ATOM   1129 O  O   . LEU A 1 138 ? 38.192 8.982   17.129  1.00 45.84  ? 146 LEU A O   1 
ATOM   1130 C  CB  . LEU A 1 138 ? 40.093 9.560   14.575  1.00 43.15  ? 146 LEU A CB  1 
ATOM   1131 C  CG  . LEU A 1 138 ? 40.338 9.168   13.117  1.00 42.24  ? 146 LEU A CG  1 
ATOM   1132 C  CD1 . LEU A 1 138 ? 41.812 8.891   12.870  1.00 45.10  ? 146 LEU A CD1 1 
ATOM   1133 C  CD2 . LEU A 1 138 ? 39.500 7.958   12.727  1.00 50.78  ? 146 LEU A CD2 1 
ATOM   1134 N  N   . GLN A 1 139 ? 38.471 11.211  16.973  1.00 42.78  ? 147 GLN A N   1 
ATOM   1135 C  CA  . GLN A 1 139 ? 38.191 11.419  18.387  1.00 43.85  ? 147 GLN A CA  1 
ATOM   1136 C  C   . GLN A 1 139 ? 36.698 11.226  18.643  1.00 42.27  ? 147 GLN A C   1 
ATOM   1137 O  O   . GLN A 1 139 ? 36.320 10.582  19.618  1.00 47.77  ? 147 GLN A O   1 
ATOM   1138 C  CB  . GLN A 1 139 ? 38.638 12.796  18.885  1.00 45.62  ? 147 GLN A CB  1 
ATOM   1139 C  CG  . GLN A 1 139 ? 40.132 12.903  19.167  1.00 53.94  ? 147 GLN A CG  1 
ATOM   1140 C  CD  . GLN A 1 139 ? 40.454 14.068  20.072  1.00 54.53  ? 147 GLN A CD  1 
ATOM   1141 O  OE1 . GLN A 1 139 ? 39.629 14.501  20.875  1.00 48.83  ? 147 GLN A OE1 1 
ATOM   1142 N  NE2 . GLN A 1 139 ? 41.673 14.570  19.969  1.00 54.43  ? 147 GLN A NE2 1 
ATOM   1143 N  N   . CYS A 1 140 ? 35.852 11.787  17.770  1.00 43.92  ? 148 CYS A N   1 
ATOM   1144 C  CA  . CYS A 1 140 ? 34.413 11.622  17.907  1.00 52.39  ? 148 CYS A CA  1 
ATOM   1145 C  C   . CYS A 1 140 ? 34.076 10.135  17.993  1.00 50.64  ? 148 CYS A C   1 
ATOM   1146 O  O   . CYS A 1 140 ? 33.166 9.740   18.719  1.00 49.39  ? 148 CYS A O   1 
ATOM   1147 C  CB  . CYS A 1 140 ? 33.651 12.258  16.749  1.00 49.83  ? 148 CYS A CB  1 
ATOM   1148 S  SG  . CYS A 1 140 ? 33.670 14.069  16.756  1.00 53.31  ? 148 CYS A SG  1 
ATOM   1149 N  N   . TYR A 1 141 ? 34.831 9.318   17.251  1.00 51.03  ? 149 TYR A N   1 
ATOM   1150 C  CA  . TYR A 1 141 ? 34.597 7.885   17.176  1.00 50.13  ? 149 TYR A CA  1 
ATOM   1151 C  C   . TYR A 1 141 ? 35.044 7.216   18.472  1.00 52.72  ? 149 TYR A C   1 
ATOM   1152 O  O   . TYR A 1 141 ? 34.296 6.443   19.066  1.00 56.53  ? 149 TYR A O   1 
ATOM   1153 C  CB  . TYR A 1 141 ? 35.350 7.315   15.969  1.00 43.54  ? 149 TYR A CB  1 
ATOM   1154 C  CG  . TYR A 1 141 ? 35.219 5.811   15.759  1.00 49.03  ? 149 TYR A CG  1 
ATOM   1155 C  CD1 . TYR A 1 141 ? 34.087 5.259   15.171  1.00 55.73  ? 149 TYR A CD1 1 
ATOM   1156 C  CD2 . TYR A 1 141 ? 36.230 4.942   16.152  1.00 50.77  ? 149 TYR A CD2 1 
ATOM   1157 C  CE1 . TYR A 1 141 ? 33.968 3.893   14.974  1.00 53.58  ? 149 TYR A CE1 1 
ATOM   1158 C  CE2 . TYR A 1 141 ? 36.121 3.574   15.966  1.00 53.74  ? 149 TYR A CE2 1 
ATOM   1159 C  CZ  . TYR A 1 141 ? 34.987 3.048   15.375  1.00 52.89  ? 149 TYR A CZ  1 
ATOM   1160 O  OH  . TYR A 1 141 ? 34.875 1.701   15.188  1.00 55.42  ? 149 TYR A OH  1 
ATOM   1161 N  N   . ALA A 1 142 ? 36.278 7.518   18.892  1.00 50.21  ? 150 ALA A N   1 
ATOM   1162 C  CA  . ALA A 1 142 ? 36.876 6.899   20.064  1.00 48.86  ? 150 ALA A CA  1 
ATOM   1163 C  C   . ALA A 1 142 ? 36.073 7.239   21.318  1.00 44.86  ? 150 ALA A C   1 
ATOM   1164 O  O   . ALA A 1 142 ? 35.991 6.430   22.238  1.00 59.87  ? 150 ALA A O   1 
ATOM   1165 C  CB  . ALA A 1 142 ? 38.314 7.336   20.196  1.00 47.99  ? 150 ALA A CB  1 
ATOM   1166 N  N   . ARG A 1 143 ? 35.491 8.443   21.344  1.00 44.96  ? 151 ARG A N   1 
ATOM   1167 C  CA  . ARG A 1 143 ? 34.700 8.899   22.476  1.00 51.26  ? 151 ARG A CA  1 
ATOM   1168 C  C   . ARG A 1 143 ? 33.251 8.448   22.304  1.00 53.63  ? 151 ARG A C   1 
ATOM   1169 O  O   . ARG A 1 143 ? 32.376 8.856   23.063  1.00 59.90  ? 151 ARG A O   1 
ATOM   1170 C  CB  . ARG A 1 143 ? 34.777 10.425  22.596  1.00 52.70  ? 151 ARG A CB  1 
ATOM   1171 C  CG  . ARG A 1 143 ? 36.181 10.968  22.822  1.00 52.44  ? 151 ARG A CG  1 
ATOM   1172 C  CD  . ARG A 1 143 ? 36.236 12.454  22.527  1.00 54.21  ? 151 ARG A CD  1 
ATOM   1173 N  NE  . ARG A 1 143 ? 37.535 13.072  22.749  1.00 58.12  ? 151 ARG A NE  1 
ATOM   1174 C  CZ  . ARG A 1 143 ? 37.845 13.800  23.814  1.00 53.13  ? 151 ARG A CZ  1 
ATOM   1175 N  NH1 . ARG A 1 143 ? 37.153 13.664  24.932  1.00 59.71  ? 151 ARG A NH1 1 
ATOM   1176 N  NH2 . ARG A 1 143 ? 38.889 14.611  23.779  1.00 63.15  ? 151 ARG A NH2 1 
ATOM   1177 N  N   . ASN A 1 144 ? 33.011 7.618   21.284  1.00 53.93  ? 152 ASN A N   1 
ATOM   1178 C  CA  . ASN A 1 144 ? 31.702 7.031   21.047  1.00 64.53  ? 152 ASN A CA  1 
ATOM   1179 C  C   . ASN A 1 144 ? 30.629 8.119   21.021  1.00 59.96  ? 152 ASN A C   1 
ATOM   1180 O  O   . ASN A 1 144 ? 29.558 7.947   21.599  1.00 63.63  ? 152 ASN A O   1 
ATOM   1181 C  CB  . ASN A 1 144 ? 31.386 5.945   22.081  1.00 56.48  ? 152 ASN A CB  1 
ATOM   1182 C  CG  . ASN A 1 144 ? 32.233 4.703   21.896  1.00 61.93  ? 152 ASN A CG  1 
ATOM   1183 O  OD1 . ASN A 1 144 ? 32.040 3.951   20.943  1.00 57.31  ? 152 ASN A OD1 1 
ATOM   1184 N  ND2 . ASN A 1 144 ? 33.171 4.477   22.800  1.00 66.53  ? 152 ASN A ND2 1 
ATOM   1185 N  N   A GLN A 1 145 ? 30.929 9.237   20.350  0.50 56.35  ? 153 GLN A N   1 
ATOM   1186 N  N   B GLN A 1 145 ? 30.929 9.237   20.350  0.50 56.69  ? 153 GLN A N   1 
ATOM   1187 C  CA  A GLN A 1 145 ? 29.938 10.273  20.113  0.50 61.55  ? 153 GLN A CA  1 
ATOM   1188 C  CA  B GLN A 1 145 ? 29.939 10.275  20.112  0.50 62.33  ? 153 GLN A CA  1 
ATOM   1189 C  C   A GLN A 1 145 ? 28.985 9.776   19.028  0.50 62.69  ? 153 GLN A C   1 
ATOM   1190 C  C   B GLN A 1 145 ? 28.985 9.779   19.027  0.50 63.07  ? 153 GLN A C   1 
ATOM   1191 O  O   A GLN A 1 145 ? 29.417 9.485   17.914  0.50 63.98  ? 153 GLN A O   1 
ATOM   1192 O  O   B GLN A 1 145 ? 29.416 9.492   17.911  0.50 64.30  ? 153 GLN A O   1 
ATOM   1193 C  CB  A GLN A 1 145 ? 30.618 11.588  19.718  0.50 64.05  ? 153 GLN A CB  1 
ATOM   1194 C  CB  B GLN A 1 145 ? 30.627 11.587  19.725  0.50 65.60  ? 153 GLN A CB  1 
ATOM   1195 C  CG  A GLN A 1 145 ? 31.663 12.060  20.721  0.50 64.61  ? 153 GLN A CG  1 
ATOM   1196 C  CG  B GLN A 1 145 ? 29.663 12.735  19.452  0.50 67.50  ? 153 GLN A CG  1 
ATOM   1197 C  CD  A GLN A 1 145 ? 32.282 13.384  20.343  0.50 63.50  ? 153 GLN A CD  1 
ATOM   1198 C  CD  B GLN A 1 145 ? 28.641 12.912  20.548  0.50 64.12  ? 153 GLN A CD  1 
ATOM   1199 O  OE1 A GLN A 1 145 ? 31.688 14.191  19.629  0.50 71.30  ? 153 GLN A OE1 1 
ATOM   1200 O  OE1 B GLN A 1 145 ? 27.476 12.549  20.401  0.50 57.69  ? 153 GLN A OE1 1 
ATOM   1201 N  NE2 A GLN A 1 145 ? 33.484 13.628  20.840  0.50 56.98  ? 153 GLN A NE2 1 
ATOM   1202 N  NE2 B GLN A 1 145 ? 29.072 13.470  21.668  0.50 66.39  ? 153 GLN A NE2 1 
ATOM   1203 N  N   . LYS A 1 146 ? 27.695 9.656   19.365  1.00 64.98  ? 154 LYS A N   1 
ATOM   1204 C  CA  . LYS A 1 146 ? 26.719 9.091   18.443  1.00 75.86  ? 154 LYS A CA  1 
ATOM   1205 C  C   . LYS A 1 146 ? 25.812 10.173  17.856  1.00 74.48  ? 154 LYS A C   1 
ATOM   1206 O  O   . LYS A 1 146 ? 25.139 9.930   16.856  1.00 75.19  ? 154 LYS A O   1 
ATOM   1207 C  CB  . LYS A 1 146 ? 25.896 7.985   19.114  1.00 78.98  ? 154 LYS A CB  1 
ATOM   1208 C  CG  . LYS A 1 146 ? 26.300 6.562   18.745  1.00 80.84  ? 154 LYS A CG  1 
ATOM   1209 C  CD  . LYS A 1 146 ? 27.714 6.195   19.136  1.00 81.20  ? 154 LYS A CD  1 
ATOM   1210 C  CE  . LYS A 1 146 ? 28.011 4.722   18.953  1.00 77.44  ? 154 LYS A CE  1 
ATOM   1211 N  NZ  . LYS A 1 146 ? 29.261 4.325   19.644  1.00 89.13  ? 154 LYS A NZ  1 
ATOM   1212 N  N   . GLU A 1 147 ? 25.791 11.361  18.469  1.00 69.39  ? 155 GLU A N   1 
ATOM   1213 C  CA  . GLU A 1 147 ? 25.083 12.495  17.895  1.00 77.40  ? 155 GLU A CA  1 
ATOM   1214 C  C   . GLU A 1 147 ? 26.109 13.399  17.216  1.00 78.76  ? 155 GLU A C   1 
ATOM   1215 O  O   . GLU A 1 147 ? 27.308 13.235  17.426  1.00 95.91  ? 155 GLU A O   1 
ATOM   1216 C  CB  . GLU A 1 147 ? 24.319 13.263  18.976  1.00 92.80  ? 155 GLU A CB  1 
ATOM   1217 C  CG  . GLU A 1 147 ? 23.744 12.379  20.070  1.00 102.94 ? 155 GLU A CG  1 
ATOM   1218 C  CD  . GLU A 1 147 ? 22.325 11.893  19.831  1.00 103.64 ? 155 GLU A CD  1 
ATOM   1219 O  OE1 . GLU A 1 147 ? 21.423 12.747  19.701  1.00 102.87 ? 155 GLU A OE1 1 
ATOM   1220 O  OE2 . GLU A 1 147 ? 22.123 10.663  19.786  1.00 104.33 ? 155 GLU A OE2 1 
ATOM   1221 N  N   . GLY A 1 148 ? 25.641 14.353  16.404  1.00 73.60  ? 156 GLY A N   1 
ATOM   1222 C  CA  . GLY A 1 148 ? 26.538 15.311  15.775  1.00 66.45  ? 156 GLY A CA  1 
ATOM   1223 C  C   . GLY A 1 148 ? 26.717 15.048  14.282  1.00 63.17  ? 156 GLY A C   1 
ATOM   1224 O  O   . GLY A 1 148 ? 26.065 14.170  13.721  1.00 61.32  ? 156 GLY A O   1 
ATOM   1225 N  N   . ALA A 1 149 ? 27.620 15.818  13.658  1.00 56.95  ? 157 ALA A N   1 
ATOM   1226 C  CA  . ALA A 1 149 ? 27.796 15.806  12.214  1.00 53.11  ? 157 ALA A CA  1 
ATOM   1227 C  C   . ALA A 1 149 ? 28.799 14.735  11.793  1.00 46.53  ? 157 ALA A C   1 
ATOM   1228 O  O   . ALA A 1 149 ? 29.000 14.519  10.601  1.00 56.55  ? 157 ALA A O   1 
ATOM   1229 C  CB  . ALA A 1 149 ? 28.238 17.169  11.741  1.00 53.65  ? 157 ALA A CB  1 
ATOM   1230 N  N   . TYR A 1 150 ? 29.428 14.074  12.767  1.00 42.11  ? 158 TYR A N   1 
ATOM   1231 C  CA  . TYR A 1 150 ? 30.366 13.006  12.463  1.00 48.60  ? 158 TYR A CA  1 
ATOM   1232 C  C   . TYR A 1 150 ? 29.700 11.675  12.805  1.00 48.07  ? 158 TYR A C   1 
ATOM   1233 O  O   . TYR A 1 150 ? 29.466 11.380  13.973  1.00 53.30  ? 158 TYR A O   1 
ATOM   1234 C  CB  . TYR A 1 150 ? 31.672 13.345  13.193  1.00 45.67  ? 158 TYR A CB  1 
ATOM   1235 C  CG  . TYR A 1 150 ? 32.314 14.627  12.679  1.00 45.38  ? 158 TYR A CG  1 
ATOM   1236 C  CD1 . TYR A 1 150 ? 33.141 14.619  11.562  1.00 44.29  ? 158 TYR A CD1 1 
ATOM   1237 C  CD2 . TYR A 1 150 ? 32.040 15.856  13.270  1.00 47.66  ? 158 TYR A CD2 1 
ATOM   1238 C  CE1 . TYR A 1 150 ? 33.712 15.784  11.076  1.00 43.90  ? 158 TYR A CE1 1 
ATOM   1239 C  CE2 . TYR A 1 150 ? 32.602 17.028  12.791  1.00 52.46  ? 158 TYR A CE2 1 
ATOM   1240 C  CZ  . TYR A 1 150 ? 33.440 16.992  11.691  1.00 47.42  ? 158 TYR A CZ  1 
ATOM   1241 O  OH  . TYR A 1 150 ? 33.997 18.143  11.212  1.00 44.86  ? 158 TYR A OH  1 
ATOM   1242 N  N   . ILE A 1 151 ? 29.377 10.890  11.766  1.00 54.50  ? 159 ILE A N   1 
ATOM   1243 C  CA  . ILE A 1 151 ? 28.602 9.669   11.928  1.00 51.31  ? 159 ILE A CA  1 
ATOM   1244 C  C   . ILE A 1 151 ? 29.530 8.522   12.323  1.00 50.71  ? 159 ILE A C   1 
ATOM   1245 O  O   . ILE A 1 151 ? 30.384 8.106   11.544  1.00 51.90  ? 159 ILE A O   1 
ATOM   1246 C  CB  . ILE A 1 151 ? 27.808 9.341   10.646  1.00 57.54  ? 159 ILE A CB  1 
ATOM   1247 C  CG1 . ILE A 1 151 ? 27.007 10.548  10.148  1.00 55.46  ? 159 ILE A CG1 1 
ATOM   1248 C  CG2 . ILE A 1 151 ? 26.919 8.123   10.858  1.00 63.66  ? 159 ILE A CG2 1 
ATOM   1249 C  CD1 . ILE A 1 151 ? 26.101 11.157  11.192  1.00 60.11  ? 159 ILE A CD1 1 
ATOM   1250 N  N   . TRP A 1 152 ? 29.322 8.005   13.540  1.00 49.79  ? 160 TRP A N   1 
ATOM   1251 C  CA  . TRP A 1 152 ? 30.140 6.943   14.104  1.00 48.96  ? 160 TRP A CA  1 
ATOM   1252 C  C   . TRP A 1 152 ? 30.162 5.735   13.171  1.00 48.86  ? 160 TRP A C   1 
ATOM   1253 O  O   . TRP A 1 152 ? 31.222 5.175   12.904  1.00 50.68  ? 160 TRP A O   1 
ATOM   1254 C  CB  . TRP A 1 152 ? 29.601 6.572   15.494  1.00 47.26  ? 160 TRP A CB  1 
ATOM   1255 C  CG  . TRP A 1 152 ? 30.550 5.782   16.357  1.00 50.42  ? 160 TRP A CG  1 
ATOM   1256 C  CD1 . TRP A 1 152 ? 31.387 6.275   17.314  1.00 50.53  ? 160 TRP A CD1 1 
ATOM   1257 C  CD2 . TRP A 1 152 ? 30.721 4.348   16.375  1.00 54.90  ? 160 TRP A CD2 1 
ATOM   1258 N  NE1 . TRP A 1 152 ? 32.085 5.257   17.906  1.00 58.22  ? 160 TRP A NE1 1 
ATOM   1259 C  CE2 . TRP A 1 152 ? 31.695 4.065   17.357  1.00 59.27  ? 160 TRP A CE2 1 
ATOM   1260 C  CE3 . TRP A 1 152 ? 30.157 3.287   15.657  1.00 54.06  ? 160 TRP A CE3 1 
ATOM   1261 C  CZ2 . TRP A 1 152 ? 32.112 2.765   17.635  1.00 62.62  ? 160 TRP A CZ2 1 
ATOM   1262 C  CZ3 . TRP A 1 152 ? 30.571 2.003   15.935  1.00 56.03  ? 160 TRP A CZ3 1 
ATOM   1263 C  CH2 . TRP A 1 152 ? 31.532 1.748   16.912  1.00 59.54  ? 160 TRP A CH2 1 
ATOM   1264 N  N   . ALA A 1 153 ? 28.979 5.347   12.681  1.00 54.30  ? 161 ALA A N   1 
ATOM   1265 C  CA  . ALA A 1 153 ? 28.839 4.177   11.828  1.00 55.59  ? 161 ALA A CA  1 
ATOM   1266 C  C   . ALA A 1 153 ? 29.559 4.402   10.501  1.00 48.97  ? 161 ALA A C   1 
ATOM   1267 O  O   . ALA A 1 153 ? 30.127 3.468   9.938   1.00 55.09  ? 161 ALA A O   1 
ATOM   1268 C  CB  . ALA A 1 153 ? 27.378 3.866   11.614  1.00 54.47  ? 161 ALA A CB  1 
ATOM   1269 N  N   . ASP A 1 154 ? 29.527 5.641   10.001  1.00 48.48  ? 162 ASP A N   1 
ATOM   1270 C  CA  . ASP A 1 154 ? 30.247 5.969   8.782   1.00 49.72  ? 162 ASP A CA  1 
ATOM   1271 C  C   . ASP A 1 154 ? 31.740 5.754   9.020   1.00 52.78  ? 162 ASP A C   1 
ATOM   1272 O  O   . ASP A 1 154 ? 32.413 5.107   8.221   1.00 48.12  ? 162 ASP A O   1 
ATOM   1273 C  CB  . ASP A 1 154 ? 29.951 7.394   8.307   1.00 48.22  ? 162 ASP A CB  1 
ATOM   1274 C  CG  . ASP A 1 154 ? 28.619 7.544   7.590   1.00 51.64  ? 162 ASP A CG  1 
ATOM   1275 O  OD1 . ASP A 1 154 ? 27.901 6.531   7.464   1.00 51.39  ? 162 ASP A OD1 1 
ATOM   1276 O  OD2 . ASP A 1 154 ? 28.315 8.672   7.154   1.00 54.84  ? 162 ASP A OD2 1 
ATOM   1277 N  N   . ILE A 1 155 ? 32.243 6.291   10.136  1.00 51.69  ? 163 ILE A N   1 
ATOM   1278 C  CA  . ILE A 1 155 ? 33.660 6.220   10.451  1.00 49.47  ? 163 ILE A CA  1 
ATOM   1279 C  C   . ILE A 1 155 ? 34.046 4.762   10.691  1.00 48.44  ? 163 ILE A C   1 
ATOM   1280 O  O   . ILE A 1 155 ? 35.121 4.323   10.287  1.00 47.83  ? 163 ILE A O   1 
ATOM   1281 C  CB  . ILE A 1 155 ? 33.989 7.116   11.662  1.00 45.85  ? 163 ILE A CB  1 
ATOM   1282 C  CG1 . ILE A 1 155 ? 33.599 8.572   11.398  1.00 50.41  ? 163 ILE A CG1 1 
ATOM   1283 C  CG2 . ILE A 1 155 ? 35.454 6.986   12.048  1.00 46.51  ? 163 ILE A CG2 1 
ATOM   1284 C  CD1 . ILE A 1 155 ? 33.414 9.399   12.648  1.00 51.47  ? 163 ILE A CD1 1 
ATOM   1285 N  N   . ASP A 1 156 ? 33.149 4.020   11.348  1.00 53.26  ? 164 ASP A N   1 
ATOM   1286 C  CA  . ASP A 1 156 ? 33.363 2.611   11.630  1.00 54.61  ? 164 ASP A CA  1 
ATOM   1287 C  C   . ASP A 1 156 ? 33.613 1.870   10.318  1.00 51.82  ? 164 ASP A C   1 
ATOM   1288 O  O   . ASP A 1 156 ? 34.534 1.061   10.222  1.00 54.43  ? 164 ASP A O   1 
ATOM   1289 C  CB  . ASP A 1 156 ? 32.179 2.035   12.411  1.00 59.69  ? 164 ASP A CB  1 
ATOM   1290 C  CG  . ASP A 1 156 ? 32.412 0.640   12.964  1.00 66.28  ? 164 ASP A CG  1 
ATOM   1291 O  OD1 . ASP A 1 156 ? 33.459 0.431   13.609  1.00 65.65  ? 164 ASP A OD1 1 
ATOM   1292 O  OD2 . ASP A 1 156 ? 31.531 -0.221  12.763  1.00 73.52  ? 164 ASP A OD2 1 
ATOM   1293 N  N   . ALA A 1 157 ? 32.793 2.170   9.305   1.00 49.16  ? 165 ALA A N   1 
ATOM   1294 C  CA  . ALA A 1 157 ? 32.899 1.520   8.008   1.00 48.87  ? 165 ALA A CA  1 
ATOM   1295 C  C   . ALA A 1 157 ? 34.230 1.859   7.337   1.00 51.28  ? 165 ALA A C   1 
ATOM   1296 O  O   . ALA A 1 157 ? 34.827 1.003   6.686   1.00 55.15  ? 165 ALA A O   1 
ATOM   1297 C  CB  . ALA A 1 157 ? 31.732 1.915   7.137   1.00 47.83  ? 165 ALA A CB  1 
ATOM   1298 N  N   . TRP A 1 158 ? 34.690 3.107   7.485   1.00 49.82  ? 166 TRP A N   1 
ATOM   1299 C  CA  . TRP A 1 158 ? 35.929 3.529   6.847   1.00 49.90  ? 166 TRP A CA  1 
ATOM   1300 C  C   . TRP A 1 158 ? 37.086 2.668   7.343   1.00 44.81  ? 166 TRP A C   1 
ATOM   1301 O  O   . TRP A 1 158 ? 37.962 2.295   6.567   1.00 49.81  ? 166 TRP A O   1 
ATOM   1302 C  CB  . TRP A 1 158 ? 36.230 5.009   7.117   1.00 48.49  ? 166 TRP A CB  1 
ATOM   1303 C  CG  . TRP A 1 158 ? 35.113 5.958   6.780   1.00 49.69  ? 166 TRP A CG  1 
ATOM   1304 C  CD1 . TRP A 1 158 ? 34.030 5.733   5.983   1.00 48.15  ? 166 TRP A CD1 1 
ATOM   1305 C  CD2 . TRP A 1 158 ? 34.974 7.305   7.278   1.00 48.53  ? 166 TRP A CD2 1 
ATOM   1306 N  NE1 . TRP A 1 158 ? 33.235 6.847   5.938   1.00 52.99  ? 166 TRP A NE1 1 
ATOM   1307 C  CE2 . TRP A 1 158 ? 33.785 7.825   6.726   1.00 50.09  ? 166 TRP A CE2 1 
ATOM   1308 C  CE3 . TRP A 1 158 ? 35.736 8.112   8.129   1.00 52.15  ? 166 TRP A CE3 1 
ATOM   1309 C  CZ2 . TRP A 1 158 ? 33.345 9.118   7.001   1.00 51.62  ? 166 TRP A CZ2 1 
ATOM   1310 C  CZ3 . TRP A 1 158 ? 35.299 9.390   8.400   1.00 49.99  ? 166 TRP A CZ3 1 
ATOM   1311 C  CH2 . TRP A 1 158 ? 34.119 9.882   7.844   1.00 52.12  ? 166 TRP A CH2 1 
ATOM   1312 N  N   . ILE A 1 159 ? 37.081 2.376   8.648   1.00 46.78  ? 167 ILE A N   1 
ATOM   1313 C  CA  . ILE A 1 159 ? 38.167 1.642   9.276   1.00 53.81  ? 167 ILE A CA  1 
ATOM   1314 C  C   . ILE A 1 159 ? 38.047 0.163   8.914   1.00 54.53  ? 167 ILE A C   1 
ATOM   1315 O  O   . ILE A 1 159 ? 39.052 -0.508  8.694   1.00 58.40  ? 167 ILE A O   1 
ATOM   1316 C  CB  . ILE A 1 159 ? 38.166 1.870   10.801  1.00 56.77  ? 167 ILE A CB  1 
ATOM   1317 C  CG1 . ILE A 1 159 ? 38.204 3.361   11.146  1.00 51.63  ? 167 ILE A CG1 1 
ATOM   1318 C  CG2 . ILE A 1 159 ? 39.308 1.111   11.463  1.00 61.58  ? 167 ILE A CG2 1 
ATOM   1319 C  CD1 . ILE A 1 159 ? 37.860 3.668   12.584  1.00 53.87  ? 167 ILE A CD1 1 
ATOM   1320 N  N   . LYS A 1 160 ? 36.807 -0.334  8.848   1.00 57.29  ? 168 LYS A N   1 
ATOM   1321 C  CA  . LYS A 1 160 ? 36.560 -1.730  8.527   1.00 59.53  ? 168 LYS A CA  1 
ATOM   1322 C  C   . LYS A 1 160 ? 36.899 -2.001  7.063   1.00 61.43  ? 168 LYS A C   1 
ATOM   1323 O  O   . LYS A 1 160 ? 37.356 -3.093  6.730   1.00 60.09  ? 168 LYS A O   1 
ATOM   1324 C  CB  . LYS A 1 160 ? 35.112 -2.101  8.862   1.00 61.50  ? 168 LYS A CB  1 
ATOM   1325 C  CG  . LYS A 1 160 ? 34.905 -2.611  10.282  1.00 66.37  ? 168 LYS A CG  1 
ATOM   1326 C  CD  . LYS A 1 160 ? 33.497 -2.437  10.803  1.00 85.04  ? 168 LYS A CD  1 
ATOM   1327 C  CE  . LYS A 1 160 ? 33.316 -3.003  12.196  1.00 87.03  ? 168 LYS A CE  1 
ATOM   1328 N  NZ  . LYS A 1 160 ? 31.922 -2.847  12.675  1.00 91.11  ? 168 LYS A NZ  1 
ATOM   1329 N  N   . ASN A 1 161 ? 36.689 -1.003  6.196   1.00 53.78  ? 169 ASN A N   1 
ATOM   1330 C  CA  . ASN A 1 161 ? 36.907 -1.185  4.769   1.00 52.05  ? 169 ASN A CA  1 
ATOM   1331 C  C   . ASN A 1 161 ? 38.368 -0.896  4.429   1.00 51.50  ? 169 ASN A C   1 
ATOM   1332 O  O   . ASN A 1 161 ? 38.771 -1.018  3.275   1.00 55.24  ? 169 ASN A O   1 
ATOM   1333 C  CB  . ASN A 1 161 ? 35.940 -0.346  3.927   1.00 60.79  ? 169 ASN A CB  1 
ATOM   1334 C  CG  . ASN A 1 161 ? 34.508 -0.837  3.999   1.00 63.20  ? 169 ASN A CG  1 
ATOM   1335 O  OD1 . ASN A 1 161 ? 34.139 -1.565  4.918   1.00 65.05  ? 169 ASN A OD1 1 
ATOM   1336 N  ND2 . ASN A 1 161 ? 33.689 -0.433  3.043   1.00 72.87  ? 169 ASN A ND2 1 
ATOM   1337 N  N   . ASN A 1 162 ? 39.152 -0.516  5.444   1.00 52.85  ? 170 ASN A N   1 
ATOM   1338 C  CA  . ASN A 1 162 ? 40.596 -0.398  5.313   1.00 51.35  ? 170 ASN A CA  1 
ATOM   1339 C  C   . ASN A 1 162 ? 40.952 0.637   4.248   1.00 50.18  ? 170 ASN A C   1 
ATOM   1340 O  O   . ASN A 1 162 ? 41.797 0.384   3.393   1.00 50.03  ? 170 ASN A O   1 
ATOM   1341 C  CB  . ASN A 1 162 ? 41.242 -1.742  4.970   1.00 54.33  ? 170 ASN A CB  1 
ATOM   1342 C  CG  . ASN A 1 162 ? 42.755 -1.699  5.024   1.00 66.39  ? 170 ASN A CG  1 
ATOM   1343 O  OD1 . ASN A 1 162 ? 43.335 -0.761  5.566   1.00 82.94  ? 170 ASN A OD1 1 
ATOM   1344 N  ND2 . ASN A 1 162 ? 43.402 -2.713  4.474   1.00 71.82  ? 170 ASN A ND2 1 
ATOM   1345 N  N   . LEU A 1 163 ? 40.316 1.810   4.315   1.00 51.58  ? 171 LEU A N   1 
ATOM   1346 C  CA  . LEU A 1 163 ? 40.604 2.883   3.379   1.00 45.64  ? 171 LEU A CA  1 
ATOM   1347 C  C   . LEU A 1 163 ? 42.064 3.309   3.509   1.00 51.41  ? 171 LEU A C   1 
ATOM   1348 O  O   . LEU A 1 163 ? 42.662 3.210   4.579   1.00 45.38  ? 171 LEU A O   1 
ATOM   1349 C  CB  . LEU A 1 163 ? 39.658 4.058   3.649   1.00 46.59  ? 171 LEU A CB  1 
ATOM   1350 C  CG  . LEU A 1 163 ? 38.175 3.751   3.453   1.00 46.84  ? 171 LEU A CG  1 
ATOM   1351 C  CD1 . LEU A 1 163 ? 37.336 5.015   3.557   1.00 49.88  ? 171 LEU A CD1 1 
ATOM   1352 C  CD2 . LEU A 1 163 ? 37.937 3.065   2.116   1.00 50.26  ? 171 LEU A CD2 1 
ATOM   1353 N  N   . GLN A 1 164 ? 42.611 3.788   2.388   1.00 56.38  ? 172 GLN A N   1 
ATOM   1354 C  CA  . GLN A 1 164 ? 43.990 4.234   2.296   1.00 56.12  ? 172 GLN A CA  1 
ATOM   1355 C  C   . GLN A 1 164 ? 44.017 5.758   2.365   1.00 55.81  ? 172 GLN A C   1 
ATOM   1356 O  O   . GLN A 1 164 ? 43.601 6.432   1.425   1.00 54.34  ? 172 GLN A O   1 
ATOM   1357 C  CB  . GLN A 1 164 ? 44.604 3.719   0.993   1.00 56.57  ? 172 GLN A CB  1 
ATOM   1358 C  CG  . GLN A 1 164 ? 44.576 2.201   0.876   1.00 64.63  ? 172 GLN A CG  1 
ATOM   1359 C  CD  . GLN A 1 164 ? 45.240 1.541   2.060   1.00 65.40  ? 172 GLN A CD  1 
ATOM   1360 O  OE1 . GLN A 1 164 ? 44.612 0.810   2.822   1.00 60.94  ? 172 GLN A OE1 1 
ATOM   1361 N  NE2 . GLN A 1 164 ? 46.524 1.810   2.229   1.00 58.97  ? 172 GLN A NE2 1 
ATOM   1362 N  N   . TRP A 1 165 ? 44.509 6.293   3.487   1.00 56.51  ? 173 TRP A N   1 
ATOM   1363 C  CA  . TRP A 1 165 ? 44.430 7.721   3.740   1.00 56.20  ? 173 TRP A CA  1 
ATOM   1364 C  C   . TRP A 1 165 ? 45.715 8.427   3.331   1.00 49.06  ? 173 TRP A C   1 
ATOM   1365 O  O   . TRP A 1 165 ? 46.810 7.879   3.428   1.00 47.71  ? 173 TRP A O   1 
ATOM   1366 C  CB  . TRP A 1 165 ? 44.125 8.008   5.214   1.00 49.90  ? 173 TRP A CB  1 
ATOM   1367 C  CG  . TRP A 1 165 ? 42.857 7.359   5.693   1.00 47.86  ? 173 TRP A CG  1 
ATOM   1368 C  CD1 . TRP A 1 165 ? 42.719 6.084   6.153   1.00 48.36  ? 173 TRP A CD1 1 
ATOM   1369 C  CD2 . TRP A 1 165 ? 41.538 7.944   5.713   1.00 47.41  ? 173 TRP A CD2 1 
ATOM   1370 N  NE1 . TRP A 1 165 ? 41.414 5.841   6.484   1.00 49.28  ? 173 TRP A NE1 1 
ATOM   1371 C  CE2 . TRP A 1 165 ? 40.665 6.957   6.220   1.00 45.25  ? 173 TRP A CE2 1 
ATOM   1372 C  CE3 . TRP A 1 165 ? 41.013 9.193   5.363   1.00 46.78  ? 173 TRP A CE3 1 
ATOM   1373 C  CZ2 . TRP A 1 165 ? 39.302 7.185   6.382   1.00 48.47  ? 173 TRP A CZ2 1 
ATOM   1374 C  CZ3 . TRP A 1 165 ? 39.663 9.415   5.522   1.00 44.64  ? 173 TRP A CZ3 1 
ATOM   1375 C  CH2 . TRP A 1 165 ? 38.822 8.424   6.024   1.00 48.63  ? 173 TRP A CH2 1 
ATOM   1376 N  N   . ARG A 1 166 ? 45.532 9.668   2.883   1.00 48.75  ? 174 ARG A N   1 
ATOM   1377 C  CA  . ARG A 1 166 ? 46.618 10.605  2.690   1.00 43.98  ? 174 ARG A CA  1 
ATOM   1378 C  C   . ARG A 1 166 ? 46.186 11.916  3.338   1.00 48.01  ? 174 ARG A C   1 
ATOM   1379 O  O   . ARG A 1 166 ? 45.341 12.629  2.800   1.00 45.05  ? 174 ARG A O   1 
ATOM   1380 C  CB  . ARG A 1 166 ? 46.907 10.741  1.193   1.00 52.41  ? 174 ARG A CB  1 
ATOM   1381 C  CG  . ARG A 1 166 ? 48.308 11.228  0.860   1.00 53.81  ? 174 ARG A CG  1 
ATOM   1382 C  CD  . ARG A 1 166 ? 48.476 12.686  1.221   1.00 63.16  ? 174 ARG A CD  1 
ATOM   1383 N  NE  . ARG A 1 166 ? 49.560 13.314  0.484   1.00 64.08  ? 174 ARG A NE  1 
ATOM   1384 C  CZ  . ARG A 1 166 ? 50.126 14.464  0.824   1.00 71.47  ? 174 ARG A CZ  1 
ATOM   1385 N  NH1 . ARG A 1 166 ? 49.771 15.066  1.946   1.00 61.78  ? 174 ARG A NH1 1 
ATOM   1386 N  NH2 . ARG A 1 166 ? 51.060 14.996  0.055   1.00 74.46  ? 174 ARG A NH2 1 
ATOM   1387 N  N   . THR A 1 167 ? 46.722 12.190  4.531   1.00 41.58  ? 175 THR A N   1 
ATOM   1388 C  CA  . THR A 1 167 ? 46.339 13.377  5.272   1.00 43.19  ? 175 THR A CA  1 
ATOM   1389 C  C   . THR A 1 167 ? 47.122 14.572  4.744   1.00 44.69  ? 175 THR A C   1 
ATOM   1390 O  O   . THR A 1 167 ? 48.295 14.455  4.394   1.00 46.18  ? 175 THR A O   1 
ATOM   1391 C  CB  . THR A 1 167 ? 46.556 13.211  6.782   1.00 42.77  ? 175 THR A CB  1 
ATOM   1392 O  OG1 . THR A 1 167 ? 47.931 12.905  7.010   1.00 47.24  ? 175 THR A OG1 1 
ATOM   1393 C  CG2 . THR A 1 167 ? 45.683 12.134  7.390   1.00 47.64  ? 175 THR A CG2 1 
ATOM   1394 N  N   . VAL A 1 168 ? 46.438 15.716  4.684   1.00 42.52  ? 176 VAL A N   1 
ATOM   1395 C  CA  . VAL A 1 168 ? 47.069 16.981  4.362   1.00 42.69  ? 176 VAL A CA  1 
ATOM   1396 C  C   . VAL A 1 168 ? 47.483 17.640  5.674   1.00 42.55  ? 176 VAL A C   1 
ATOM   1397 O  O   . VAL A 1 168 ? 46.650 17.872  6.547   1.00 40.26  ? 176 VAL A O   1 
ATOM   1398 C  CB  . VAL A 1 168 ? 46.114 17.862  3.538   1.00 42.72  ? 176 VAL A CB  1 
ATOM   1399 C  CG1 . VAL A 1 168 ? 46.730 19.208  3.190   1.00 45.12  ? 176 VAL A CG1 1 
ATOM   1400 C  CG2 . VAL A 1 168 ? 45.654 17.139  2.281   1.00 45.03  ? 176 VAL A CG2 1 
ATOM   1401 N  N   . LYS A 1 169 ? 48.785 17.911  5.813   1.00 43.59  ? 177 LYS A N   1 
ATOM   1402 C  CA  . LYS A 1 169 ? 49.327 18.418  7.062   1.00 43.48  ? 177 LYS A CA  1 
ATOM   1403 C  C   . LYS A 1 169 ? 48.906 19.877  7.224   1.00 49.64  ? 177 LYS A C   1 
ATOM   1404 O  O   . LYS A 1 169 ? 48.604 20.556  6.245   1.00 45.89  ? 177 LYS A O   1 
ATOM   1405 C  CB  . LYS A 1 169 ? 50.847 18.226  7.093   1.00 46.56  ? 177 LYS A CB  1 
ATOM   1406 C  CG  . LYS A 1 169 ? 51.322 16.819  6.749   1.00 52.73  ? 177 LYS A CG  1 
ATOM   1407 C  CD  . LYS A 1 169 ? 50.580 15.727  7.496   1.00 60.82  ? 177 LYS A CD  1 
ATOM   1408 C  CE  . LYS A 1 169 ? 51.002 14.328  7.096   1.00 60.59  ? 177 LYS A CE  1 
ATOM   1409 N  NZ  . LYS A 1 169 ? 50.902 14.120  5.632   1.00 66.91  ? 177 LYS A NZ  1 
ATOM   1410 N  N   . ARG A 1 170 ? 48.878 20.340  8.478   1.00 46.08  ? 178 ARG A N   1 
ATOM   1411 C  CA  . ARG A 1 170 ? 48.336 21.648  8.805   1.00 51.16  ? 178 ARG A CA  1 
ATOM   1412 C  C   . ARG A 1 170 ? 48.990 22.729  7.947   1.00 50.73  ? 178 ARG A C   1 
ATOM   1413 O  O   . ARG A 1 170 ? 48.299 23.593  7.413   1.00 54.28  ? 178 ARG A O   1 
ATOM   1414 C  CB  . ARG A 1 170 ? 48.520 21.947  10.296  1.00 51.86  ? 178 ARG A CB  1 
ATOM   1415 C  CG  . ARG A 1 170 ? 47.967 23.297  10.731  1.00 51.46  ? 178 ARG A CG  1 
ATOM   1416 C  CD  . ARG A 1 170 ? 48.049 23.474  12.234  1.00 50.07  ? 178 ARG A CD  1 
ATOM   1417 N  NE  . ARG A 1 170 ? 47.264 22.469  12.935  1.00 47.21  ? 178 ARG A NE  1 
ATOM   1418 C  CZ  . ARG A 1 170 ? 47.223 22.330  14.254  1.00 52.15  ? 178 ARG A CZ  1 
ATOM   1419 N  NH1 . ARG A 1 170 ? 48.005 23.068  15.023  1.00 45.17  ? 178 ARG A NH1 1 
ATOM   1420 N  NH2 . ARG A 1 170 ? 46.409 21.442  14.799  1.00 45.09  ? 178 ARG A NH2 1 
ATOM   1421 N  N   . HIS A 1 171 ? 50.320 22.685  7.818   1.00 51.70  ? 179 HIS A N   1 
ATOM   1422 C  CA  . HIS A 1 171 ? 51.029 23.755  7.134   1.00 68.69  ? 179 HIS A CA  1 
ATOM   1423 C  C   . HIS A 1 171 ? 51.493 23.286  5.756   1.00 66.43  ? 179 HIS A C   1 
ATOM   1424 O  O   . HIS A 1 171 ? 52.391 23.882  5.168   1.00 70.57  ? 179 HIS A O   1 
ATOM   1425 C  CB  . HIS A 1 171 ? 52.154 24.299  8.023   1.00 69.99  ? 179 HIS A CB  1 
ATOM   1426 C  CG  . HIS A 1 171 ? 51.651 24.837  9.323   1.00 83.35  ? 179 HIS A CG  1 
ATOM   1427 N  ND1 . HIS A 1 171 ? 50.584 25.708  9.392   1.00 79.91  ? 179 HIS A ND1 1 
ATOM   1428 C  CD2 . HIS A 1 171 ? 52.029 24.614  10.589  1.00 79.91  ? 179 HIS A CD2 1 
ATOM   1429 C  CE1 . HIS A 1 171 ? 50.344 26.007  10.660  1.00 76.73  ? 179 HIS A CE1 1 
ATOM   1430 N  NE2 . HIS A 1 171 ? 51.211 25.355  11.405  1.00 91.36  ? 179 HIS A NE2 1 
ATOM   1431 N  N   . GLU A 1 172 ? 50.852 22.234  5.235   1.00 54.57  ? 180 GLU A N   1 
ATOM   1432 C  CA  . GLU A 1 172 ? 51.231 21.676  3.947   1.00 55.21  ? 180 GLU A CA  1 
ATOM   1433 C  C   . GLU A 1 172 ? 50.735 22.584  2.825   1.00 55.54  ? 180 GLU A C   1 
ATOM   1434 O  O   . GLU A 1 172 ? 49.637 23.133  2.894   1.00 57.40  ? 180 GLU A O   1 
ATOM   1435 C  CB  . GLU A 1 172 ? 50.678 20.260  3.777   1.00 56.20  ? 180 GLU A CB  1 
ATOM   1436 C  CG  . GLU A 1 172 ? 51.061 19.626  2.452   1.00 49.95  ? 180 GLU A CG  1 
ATOM   1437 C  CD  . GLU A 1 172 ? 50.883 18.119  2.389   1.00 50.54  ? 180 GLU A CD  1 
ATOM   1438 O  OE1 . GLU A 1 172 ? 50.423 17.536  3.391   1.00 49.70  ? 180 GLU A OE1 1 
ATOM   1439 O  OE2 . GLU A 1 172 ? 51.209 17.531  1.338   1.00 68.57  ? 180 GLU A OE2 1 
ATOM   1440 N  N   . ASP A 1 173 ? 51.565 22.718  1.786   1.00 64.13  ? 181 ASP A N   1 
ATOM   1441 C  CA  . ASP A 1 173 ? 51.237 23.513  0.616   1.00 67.16  ? 181 ASP A CA  1 
ATOM   1442 C  C   . ASP A 1 173 ? 50.182 22.781  -0.211  1.00 54.98  ? 181 ASP A C   1 
ATOM   1443 O  O   . ASP A 1 173 ? 49.905 21.607  0.025   1.00 70.17  ? 181 ASP A O   1 
ATOM   1444 C  CB  . ASP A 1 173 ? 52.491 23.797  -0.216  1.00 73.13  ? 181 ASP A CB  1 
ATOM   1445 C  CG  . ASP A 1 173 ? 53.451 24.780  0.431   1.00 72.79  ? 181 ASP A CG  1 
ATOM   1446 O  OD1 . ASP A 1 173 ? 53.041 25.452  1.399   1.00 75.44  ? 181 ASP A OD1 1 
ATOM   1447 O  OD2 . ASP A 1 173 ? 54.608 24.854  -0.030  1.00 68.87  ? 181 ASP A OD2 1 
ATOM   1448 N  N   . ASN A 1 174 ? 49.604 23.493  -1.182  1.00 49.72  ? 182 ASN A N   1 
ATOM   1449 C  CA  . ASN A 1 174 ? 48.625 22.918  -2.089  1.00 54.27  ? 182 ASN A CA  1 
ATOM   1450 C  C   . ASN A 1 174 ? 49.266 21.746  -2.831  1.00 61.76  ? 182 ASN A C   1 
ATOM   1451 O  O   . ASN A 1 174 ? 50.452 21.783  -3.152  1.00 64.27  ? 182 ASN A O   1 
ATOM   1452 C  CB  . ASN A 1 174 ? 48.075 23.977  -3.048  1.00 54.58  ? 182 ASN A CB  1 
ATOM   1453 C  CG  . ASN A 1 174 ? 47.396 25.124  -2.328  1.00 64.55  ? 182 ASN A CG  1 
ATOM   1454 O  OD1 . ASN A 1 174 ? 47.271 26.219  -2.873  1.00 68.33  ? 182 ASN A OD1 1 
ATOM   1455 N  ND2 . ASN A 1 174 ? 46.977 24.891  -1.094  1.00 56.12  ? 182 ASN A ND2 1 
ATOM   1456 N  N   . ILE A 1 175 ? 48.466 20.704  -3.085  1.00 55.94  ? 183 ILE A N   1 
ATOM   1457 C  CA  . ILE A 1 175 ? 48.950 19.476  -3.692  1.00 54.94  ? 183 ILE A CA  1 
ATOM   1458 C  C   . ILE A 1 175 ? 48.511 19.426  -5.152  1.00 50.96  ? 183 ILE A C   1 
ATOM   1459 O  O   . ILE A 1 175 ? 47.319 19.478  -5.446  1.00 51.99  ? 183 ILE A O   1 
ATOM   1460 C  CB  . ILE A 1 175 ? 48.428 18.252  -2.915  1.00 60.02  ? 183 ILE A CB  1 
ATOM   1461 C  CG1 . ILE A 1 175 ? 48.958 18.240  -1.479  1.00 72.18  ? 183 ILE A CG1 1 
ATOM   1462 C  CG2 . ILE A 1 175 ? 48.759 16.963  -3.654  1.00 53.10  ? 183 ILE A CG2 1 
ATOM   1463 C  CD1 . ILE A 1 175 ? 47.934 17.819  -0.455  1.00 77.50  ? 183 ILE A CD1 1 
ATOM   1464 N  N   . LEU A 1 176 ? 49.490 19.316  -6.056  1.00 54.00  ? 184 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 176 ? 49.200 19.049  -7.453  1.00 51.92  ? 184 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 176 ? 48.833 17.576  -7.602  1.00 52.99  ? 184 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 176 ? 49.702 16.708  -7.606  1.00 55.04  ? 184 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 176 ? 50.408 19.403  -8.325  1.00 57.89  ? 184 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 176 ? 50.187 19.181  -9.821  1.00 76.18  ? 184 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 176 ? 49.048 20.053  -10.325 1.00 70.78  ? 184 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 176 ? 51.455 19.445  -10.619 1.00 81.16  ? 184 LEU A CD2 1 
ATOM   1472 N  N   . LEU A 1 177 ? 47.530 17.318  -7.731  1.00 52.60  ? 185 LEU A N   1 
ATOM   1473 C  CA  . LEU A 1 177 ? 46.995 15.968  -7.766  1.00 54.91  ? 185 LEU A CA  1 
ATOM   1474 C  C   . LEU A 1 177 ? 47.095 15.419  -9.189  1.00 50.15  ? 185 LEU A C   1 
ATOM   1475 O  O   . LEU A 1 177 ? 47.278 14.221  -9.390  1.00 53.35  ? 185 LEU A O   1 
ATOM   1476 C  CB  . LEU A 1 177 ? 45.543 16.047  -7.286  1.00 54.74  ? 185 LEU A CB  1 
ATOM   1477 C  CG  . LEU A 1 177 ? 44.928 14.757  -6.747  1.00 60.70  ? 185 LEU A CG  1 
ATOM   1478 C  CD1 . LEU A 1 177 ? 45.800 14.141  -5.663  1.00 62.06  ? 185 LEU A CD1 1 
ATOM   1479 C  CD2 . LEU A 1 177 ? 43.532 15.033  -6.210  1.00 56.05  ? 185 LEU A CD2 1 
ATOM   1480 N  N   . ALA A 1 178 ? 46.984 16.326  -10.164 1.00 51.80  ? 186 ALA A N   1 
ATOM   1481 C  CA  . ALA A 1 178 ? 46.994 15.991  -11.579 1.00 49.51  ? 186 ALA A CA  1 
ATOM   1482 C  C   . ALA A 1 178 ? 47.091 17.290  -12.375 1.00 54.95  ? 186 ALA A C   1 
ATOM   1483 O  O   . ALA A 1 178 ? 46.898 18.366  -11.814 1.00 46.92  ? 186 ALA A O   1 
ATOM   1484 C  CB  . ALA A 1 178 ? 45.745 15.219  -11.931 1.00 53.92  ? 186 ALA A CB  1 
ATOM   1485 N  N   . GLU A 1 179 ? 47.382 17.197  -13.677 1.00 54.42  ? 187 GLU A N   1 
ATOM   1486 C  CA  . GLU A 1 179 ? 47.458 18.394  -14.499 1.00 59.29  ? 187 GLU A CA  1 
ATOM   1487 C  C   . GLU A 1 179 ? 46.168 19.191  -14.315 1.00 57.69  ? 187 GLU A C   1 
ATOM   1488 O  O   . GLU A 1 179 ? 45.080 18.689  -14.585 1.00 52.87  ? 187 GLU A O   1 
ATOM   1489 C  CB  . GLU A 1 179 ? 47.686 18.047  -15.972 1.00 67.67  ? 187 GLU A CB  1 
ATOM   1490 C  CG  . GLU A 1 179 ? 47.957 19.264  -16.843 1.00 69.71  ? 187 GLU A CG  1 
ATOM   1491 C  CD  . GLU A 1 179 ? 48.284 18.957  -18.295 1.00 77.66  ? 187 GLU A CD  1 
ATOM   1492 O  OE1 . GLU A 1 179 ? 48.306 17.763  -18.656 1.00 71.98  ? 187 GLU A OE1 1 
ATOM   1493 O  OE2 . GLU A 1 179 ? 48.519 19.914  -19.059 1.00 79.48  ? 187 GLU A OE2 1 
ATOM   1494 N  N   . GLY A 1 180 ? 46.304 20.427  -13.821 1.00 54.89  ? 188 GLY A N   1 
ATOM   1495 C  CA  . GLY A 1 180 ? 45.183 21.345  -13.704 1.00 57.05  ? 188 GLY A CA  1 
ATOM   1496 C  C   . GLY A 1 180 ? 44.232 20.995  -12.560 1.00 47.19  ? 188 GLY A C   1 
ATOM   1497 O  O   . GLY A 1 180 ? 43.112 21.497  -12.520 1.00 56.99  ? 188 GLY A O   1 
ATOM   1498 N  N   . VAL A 1 181 ? 44.681 20.137  -11.636 1.00 44.28  ? 189 VAL A N   1 
ATOM   1499 C  CA  . VAL A 1 181 ? 43.888 19.781  -10.470 1.00 45.65  ? 189 VAL A CA  1 
ATOM   1500 C  C   . VAL A 1 181 ? 44.756 19.928  -9.223  1.00 47.50  ? 189 VAL A C   1 
ATOM   1501 O  O   . VAL A 1 181 ? 45.677 19.143  -9.005  1.00 45.80  ? 189 VAL A O   1 
ATOM   1502 C  CB  . VAL A 1 181 ? 43.316 18.353  -10.569 1.00 51.99  ? 189 VAL A CB  1 
ATOM   1503 C  CG1 . VAL A 1 181 ? 42.443 18.018  -9.369  1.00 53.66  ? 189 VAL A CG1 1 
ATOM   1504 C  CG2 . VAL A 1 181 ? 42.549 18.129  -11.863 1.00 55.53  ? 189 VAL A CG2 1 
ATOM   1505 N  N   . LYS A 1 182 ? 44.436 20.933  -8.402  1.00 49.00  ? 190 LYS A N   1 
ATOM   1506 C  CA  . LYS A 1 182 ? 45.186 21.211  -7.188  1.00 52.80  ? 190 LYS A CA  1 
ATOM   1507 C  C   . LYS A 1 182 ? 44.265 21.121  -5.974  1.00 49.15  ? 190 LYS A C   1 
ATOM   1508 O  O   . LYS A 1 182 ? 43.163 21.664  -5.986  1.00 50.79  ? 190 LYS A O   1 
ATOM   1509 C  CB  . LYS A 1 182 ? 45.840 22.594  -7.273  1.00 58.51  ? 190 LYS A CB  1 
ATOM   1510 C  CG  . LYS A 1 182 ? 47.357 22.588  -7.410  1.00 77.50  ? 190 LYS A CG  1 
ATOM   1511 C  CD  . LYS A 1 182 ? 47.941 23.959  -7.671  1.00 85.45  ? 190 LYS A CD  1 
ATOM   1512 C  CE  . LYS A 1 182 ? 47.061 25.080  -7.160  1.00 90.03  ? 190 LYS A CE  1 
ATOM   1513 N  NZ  . LYS A 1 182 ? 47.698 26.405  -7.342  1.00 96.68  ? 190 LYS A NZ  1 
ATOM   1514 N  N   . VAL A 1 183 ? 44.735 20.428  -4.930  1.00 45.62  ? 191 VAL A N   1 
ATOM   1515 C  CA  . VAL A 1 183 ? 44.031 20.381  -3.659  1.00 44.49  ? 191 VAL A CA  1 
ATOM   1516 C  C   . VAL A 1 183 ? 44.425 21.617  -2.857  1.00 45.30  ? 191 VAL A C   1 
ATOM   1517 O  O   . VAL A 1 183 ? 45.609 21.866  -2.644  1.00 49.63  ? 191 VAL A O   1 
ATOM   1518 C  CB  . VAL A 1 183 ? 44.340 19.092  -2.873  1.00 42.90  ? 191 VAL A CB  1 
ATOM   1519 C  CG1 . VAL A 1 183 ? 43.476 18.980  -1.626  1.00 50.28  ? 191 VAL A CG1 1 
ATOM   1520 C  CG2 . VAL A 1 183 ? 44.195 17.847  -3.734  1.00 42.00  ? 191 VAL A CG2 1 
ATOM   1521 N  N   . LEU A 1 184 ? 43.421 22.382  -2.417  1.00 47.73  ? 192 LEU A N   1 
ATOM   1522 C  CA  . LEU A 1 184 ? 43.654 23.618  -1.689  1.00 45.88  ? 192 LEU A CA  1 
ATOM   1523 C  C   . LEU A 1 184 ? 43.476 23.366  -0.193  1.00 46.31  ? 192 LEU A C   1 
ATOM   1524 O  O   . LEU A 1 184 ? 42.406 22.953  0.245   1.00 43.89  ? 192 LEU A O   1 
ATOM   1525 C  CB  . LEU A 1 184 ? 42.669 24.677  -2.194  1.00 48.12  ? 192 LEU A CB  1 
ATOM   1526 C  CG  . LEU A 1 184 ? 42.629 24.869  -3.710  1.00 57.53  ? 192 LEU A CG  1 
ATOM   1527 C  CD1 . LEU A 1 184 ? 41.566 25.882  -4.103  1.00 51.64  ? 192 LEU A CD1 1 
ATOM   1528 C  CD2 . LEU A 1 184 ? 43.989 25.294  -4.243  1.00 60.27  ? 192 LEU A CD2 1 
ATOM   1529 N  N   . ASN A 1 185 ? 44.537 23.620  0.581   1.00 44.91  ? 193 ASN A N   1 
ATOM   1530 C  CA  . ASN A 1 185 ? 44.502 23.456  2.025   1.00 44.63  ? 193 ASN A CA  1 
ATOM   1531 C  C   . ASN A 1 185 ? 43.963 24.731  2.670   1.00 41.84  ? 193 ASN A C   1 
ATOM   1532 O  O   . ASN A 1 185 ? 44.712 25.678  2.884   1.00 40.73  ? 193 ASN A O   1 
ATOM   1533 C  CB  . ASN A 1 185 ? 45.890 23.129  2.584   1.00 47.10  ? 193 ASN A CB  1 
ATOM   1534 C  CG  . ASN A 1 185 ? 45.883 22.855  4.072   1.00 41.56  ? 193 ASN A CG  1 
ATOM   1535 O  OD1 . ASN A 1 185 ? 44.827 22.842  4.701   1.00 41.91  ? 193 ASN A OD1 1 
ATOM   1536 N  ND2 . ASN A 1 185 ? 47.056 22.634  4.642   1.00 45.39  ? 193 ASN A ND2 1 
ATOM   1537 N  N   . PHE A 1 186 ? 42.663 24.740  2.988   1.00 46.21  ? 194 PHE A N   1 
ATOM   1538 C  CA  . PHE A 1 186 ? 42.029 25.903  3.589   1.00 45.17  ? 194 PHE A CA  1 
ATOM   1539 C  C   . PHE A 1 186 ? 42.255 25.928  5.099   1.00 44.51  ? 194 PHE A C   1 
ATOM   1540 O  O   . PHE A 1 186 ? 42.213 26.991  5.712   1.00 46.83  ? 194 PHE A O   1 
ATOM   1541 C  CB  . PHE A 1 186 ? 40.523 25.927  3.310   1.00 50.26  ? 194 PHE A CB  1 
ATOM   1542 C  CG  . PHE A 1 186 ? 40.136 26.131  1.867   1.00 51.79  ? 194 PHE A CG  1 
ATOM   1543 C  CD1 . PHE A 1 186 ? 40.904 26.921  1.026   1.00 48.98  ? 194 PHE A CD1 1 
ATOM   1544 C  CD2 . PHE A 1 186 ? 38.971 25.572  1.365   1.00 50.36  ? 194 PHE A CD2 1 
ATOM   1545 C  CE1 . PHE A 1 186 ? 40.535 27.114  -0.296  1.00 44.01  ? 194 PHE A CE1 1 
ATOM   1546 C  CE2 . PHE A 1 186 ? 38.602 25.772  0.044   1.00 49.69  ? 194 PHE A CE2 1 
ATOM   1547 C  CZ  . PHE A 1 186 ? 39.384 26.542  -0.783  1.00 44.79  ? 194 PHE A CZ  1 
ATOM   1548 N  N   . GLY A 1 187 ? 42.470 24.750  5.694   1.00 47.36  ? 195 GLY A N   1 
ATOM   1549 C  CA  . GLY A 1 187 ? 42.646 24.641  7.132   1.00 46.28  ? 195 GLY A CA  1 
ATOM   1550 C  C   . GLY A 1 187 ? 41.331 24.833  7.884   1.00 47.66  ? 195 GLY A C   1 
ATOM   1551 O  O   . GLY A 1 187 ? 40.254 24.649  7.321   1.00 50.97  ? 195 GLY A O   1 
ATOM   1552 N  N   . SER A 1 188 ? 41.438 25.218  9.160   1.00 44.29  ? 196 SER A N   1 
ATOM   1553 C  CA  . SER A 1 188 ? 40.292 25.283  10.049  1.00 44.66  ? 196 SER A CA  1 
ATOM   1554 C  C   . SER A 1 188 ? 39.401 26.469  9.692   1.00 43.78  ? 196 SER A C   1 
ATOM   1555 O  O   . SER A 1 188 ? 39.878 27.518  9.261   1.00 38.13  ? 196 SER A O   1 
ATOM   1556 C  CB  . SER A 1 188 ? 40.732 25.341  11.489  1.00 47.54  ? 196 SER A CB  1 
ATOM   1557 O  OG  . SER A 1 188 ? 41.645 26.408  11.694  1.00 45.60  ? 196 SER A OG  1 
ATOM   1558 N  N   . GLY A 1 189 ? 38.096 26.269  9.897   1.00 39.56  ? 197 GLY A N   1 
ATOM   1559 C  CA  . GLY A 1 189 ? 37.072 27.260  9.620   1.00 43.05  ? 197 GLY A CA  1 
ATOM   1560 C  C   . GLY A 1 189 ? 35.693 26.701  9.961   1.00 42.37  ? 197 GLY A C   1 
ATOM   1561 O  O   . GLY A 1 189 ? 35.324 26.624  11.129  1.00 50.45  ? 197 GLY A O   1 
ATOM   1562 N  N   . HIS A 1 190 ? 34.958 26.286  8.926   1.00 42.53  ? 198 HIS A N   1 
ATOM   1563 C  CA  . HIS A 1 190 ? 33.682 25.603  9.080   1.00 41.71  ? 198 HIS A CA  1 
ATOM   1564 C  C   . HIS A 1 190 ? 33.858 24.378  9.975   1.00 39.49  ? 198 HIS A C   1 
ATOM   1565 O  O   . HIS A 1 190 ? 33.067 24.156  10.888  1.00 42.23  ? 198 HIS A O   1 
ATOM   1566 C  CB  . HIS A 1 190 ? 33.140 25.235  7.694   1.00 41.41  ? 198 HIS A CB  1 
ATOM   1567 C  CG  . HIS A 1 190 ? 31.994 24.278  7.673   1.00 42.21  ? 198 HIS A CG  1 
ATOM   1568 N  ND1 . HIS A 1 190 ? 30.713 24.605  8.061   1.00 46.28  ? 198 HIS A ND1 1 
ATOM   1569 C  CD2 . HIS A 1 190 ? 31.940 23.005  7.255   1.00 39.60  ? 198 HIS A CD2 1 
ATOM   1570 C  CE1 . HIS A 1 190 ? 29.926 23.549  7.901   1.00 49.53  ? 198 HIS A CE1 1 
ATOM   1571 N  NE2 . HIS A 1 190 ? 30.650 22.567  7.411   1.00 45.56  ? 198 HIS A NE2 1 
ATOM   1572 N  N   . ALA A 1 191 ? 34.897 23.586  9.683   1.00 44.32  ? 199 ALA A N   1 
ATOM   1573 C  CA  . ALA A 1 191 ? 35.239 22.405  10.460  1.00 43.41  ? 199 ALA A CA  1 
ATOM   1574 C  C   . ALA A 1 191 ? 36.723 22.453  10.823  1.00 38.27  ? 199 ALA A C   1 
ATOM   1575 O  O   . ALA A 1 191 ? 37.378 23.469  10.607  1.00 41.92  ? 199 ALA A O   1 
ATOM   1576 C  CB  . ALA A 1 191 ? 34.896 21.162  9.676   1.00 43.28  ? 199 ALA A CB  1 
ATOM   1577 N  N   . TRP A 1 192 ? 37.250 21.347  11.363  1.00 46.41  ? 200 TRP A N   1 
ATOM   1578 C  CA  . TRP A 1 192 ? 38.613 21.320  11.876  1.00 46.73  ? 200 TRP A CA  1 
ATOM   1579 C  C   . TRP A 1 192 ? 39.618 21.558  10.750  1.00 45.10  ? 200 TRP A C   1 
ATOM   1580 O  O   . TRP A 1 192 ? 40.597 22.276  10.936  1.00 41.15  ? 200 TRP A O   1 
ATOM   1581 C  CB  . TRP A 1 192 ? 38.903 19.996  12.600  1.00 41.60  ? 200 TRP A CB  1 
ATOM   1582 C  CG  . TRP A 1 192 ? 38.088 19.788  13.849  1.00 48.24  ? 200 TRP A CG  1 
ATOM   1583 C  CD1 . TRP A 1 192 ? 38.058 20.586  14.955  1.00 50.20  ? 200 TRP A CD1 1 
ATOM   1584 C  CD2 . TRP A 1 192 ? 37.181 18.696  14.120  1.00 49.82  ? 200 TRP A CD2 1 
ATOM   1585 N  NE1 . TRP A 1 192 ? 37.197 20.076  15.889  1.00 49.30  ? 200 TRP A NE1 1 
ATOM   1586 C  CE2 . TRP A 1 192 ? 36.646 18.917  15.408  1.00 50.26  ? 200 TRP A CE2 1 
ATOM   1587 C  CE3 . TRP A 1 192 ? 36.773 17.564  13.405  1.00 43.89  ? 200 TRP A CE3 1 
ATOM   1588 C  CZ2 . TRP A 1 192 ? 35.728 18.047  15.990  1.00 43.82  ? 200 TRP A CZ2 1 
ATOM   1589 C  CZ3 . TRP A 1 192 ? 35.865 16.705  13.984  1.00 44.83  ? 200 TRP A CZ3 1 
ATOM   1590 C  CH2 . TRP A 1 192 ? 35.351 16.945  15.257  1.00 47.62  ? 200 TRP A CH2 1 
ATOM   1591 N  N   . GLY A 1 193 ? 39.374 20.945  9.587   1.00 42.53  ? 201 GLY A N   1 
ATOM   1592 C  CA  . GLY A 1 193 ? 40.262 21.096  8.445   1.00 44.70  ? 201 GLY A CA  1 
ATOM   1593 C  C   . GLY A 1 193 ? 39.517 20.967  7.118   1.00 48.03  ? 201 GLY A C   1 
ATOM   1594 O  O   . GLY A 1 193 ? 38.927 19.927  6.834   1.00 50.31  ? 201 GLY A O   1 
ATOM   1595 N  N   . MET A 1 194 ? 39.567 22.030  6.307   1.00 43.41  ? 202 MET A N   1 
ATOM   1596 C  CA  . MET A 1 194 ? 38.824 22.080  5.057   1.00 45.07  ? 202 MET A CA  1 
ATOM   1597 C  C   . MET A 1 194 ? 39.789 21.980  3.878   1.00 42.14  ? 202 MET A C   1 
ATOM   1598 O  O   . MET A 1 194 ? 40.846 22.607  3.872   1.00 39.34  ? 202 MET A O   1 
ATOM   1599 C  CB  . MET A 1 194 ? 38.034 23.388  4.937   1.00 39.58  ? 202 MET A CB  1 
ATOM   1600 C  CG  . MET A 1 194 ? 37.123 23.666  6.119   1.00 40.81  ? 202 MET A CG  1 
ATOM   1601 S  SD  . MET A 1 194 ? 35.749 22.495  6.311   1.00 49.07  ? 202 MET A SD  1 
ATOM   1602 C  CE  . MET A 1 194 ? 34.789 22.821  4.834   1.00 51.13  ? 202 MET A CE  1 
ATOM   1603 N  N   . LEU A 1 195 ? 39.394 21.186  2.877   1.00 43.35  ? 203 LEU A N   1 
ATOM   1604 C  CA  . LEU A 1 195 ? 40.096 21.116  1.607   1.00 39.10  ? 203 LEU A CA  1 
ATOM   1605 C  C   . LEU A 1 195 ? 39.188 21.650  0.503   1.00 44.83  ? 203 LEU A C   1 
ATOM   1606 O  O   . LEU A 1 195 ? 37.978 21.425  0.521   1.00 38.93  ? 203 LEU A O   1 
ATOM   1607 C  CB  . LEU A 1 195 ? 40.487 19.661  1.325   1.00 41.06  ? 203 LEU A CB  1 
ATOM   1608 C  CG  . LEU A 1 195 ? 41.451 19.024  2.325   1.00 42.42  ? 203 LEU A CG  1 
ATOM   1609 C  CD1 . LEU A 1 195 ? 41.886 17.644  1.854   1.00 42.69  ? 203 LEU A CD1 1 
ATOM   1610 C  CD2 . LEU A 1 195 ? 42.665 19.912  2.555   1.00 42.46  ? 203 LEU A CD2 1 
ATOM   1611 N  N   . GLY A 1 196 ? 39.792 22.372  -0.444  1.00 41.67  ? 204 GLY A N   1 
ATOM   1612 C  CA  . GLY A 1 196 ? 39.139 22.715  -1.695  1.00 41.15  ? 204 GLY A CA  1 
ATOM   1613 C  C   . GLY A 1 196 ? 39.877 22.107  -2.885  1.00 41.03  ? 204 GLY A C   1 
ATOM   1614 O  O   . GLY A 1 196 ? 40.936 21.506  -2.720  1.00 43.90  ? 204 GLY A O   1 
ATOM   1615 N  N   . LEU A 1 197 ? 39.287 22.251  -4.077  1.00 45.14  ? 205 LEU A N   1 
ATOM   1616 C  CA  . LEU A 1 197 ? 39.952 21.928  -5.329  1.00 45.14  ? 205 LEU A CA  1 
ATOM   1617 C  C   . LEU A 1 197 ? 40.010 23.182  -6.194  1.00 46.25  ? 205 LEU A C   1 
ATOM   1618 O  O   . LEU A 1 197 ? 39.045 23.939  -6.259  1.00 39.82  ? 205 LEU A O   1 
ATOM   1619 C  CB  . LEU A 1 197 ? 39.173 20.841  -6.079  1.00 46.38  ? 205 LEU A CB  1 
ATOM   1620 C  CG  . LEU A 1 197 ? 39.702 19.408  -6.018  1.00 48.85  ? 205 LEU A CG  1 
ATOM   1621 C  CD1 . LEU A 1 197 ? 39.301 18.662  -7.281  1.00 49.55  ? 205 LEU A CD1 1 
ATOM   1622 C  CD2 . LEU A 1 197 ? 41.211 19.349  -5.832  1.00 50.89  ? 205 LEU A CD2 1 
ATOM   1623 N  N   . HIS A 1 198 ? 41.147 23.383  -6.863  1.00 47.26  ? 206 HIS A N   1 
ATOM   1624 C  CA  . HIS A 1 198 ? 41.191 24.258  -8.019  1.00 49.18  ? 206 HIS A CA  1 
ATOM   1625 C  C   . HIS A 1 198 ? 41.359 23.392  -9.263  1.00 51.43  ? 206 HIS A C   1 
ATOM   1626 O  O   . HIS A 1 198 ? 42.329 22.646  -9.381  1.00 49.71  ? 206 HIS A O   1 
ATOM   1627 C  CB  . HIS A 1 198 ? 42.313 25.297  -7.933  1.00 52.94  ? 206 HIS A CB  1 
ATOM   1628 C  CG  . HIS A 1 198 ? 42.263 26.244  -9.085  1.00 60.53  ? 206 HIS A CG  1 
ATOM   1629 N  ND1 . HIS A 1 198 ? 43.033 26.090  -10.218 1.00 74.02  ? 206 HIS A ND1 1 
ATOM   1630 C  CD2 . HIS A 1 198 ? 41.479 27.305  -9.313  1.00 57.26  ? 206 HIS A CD2 1 
ATOM   1631 C  CE1 . HIS A 1 198 ? 42.742 27.056  -11.078 1.00 68.47  ? 206 HIS A CE1 1 
ATOM   1632 N  NE2 . HIS A 1 198 ? 41.802 27.806  -10.548 1.00 61.02  ? 206 HIS A NE2 1 
ATOM   1633 N  N   . VAL A 1 199 ? 40.388 23.491  -10.173 1.00 48.61  ? 207 VAL A N   1 
ATOM   1634 C  CA  . VAL A 1 199 ? 40.433 22.754  -11.423 1.00 48.00  ? 207 VAL A CA  1 
ATOM   1635 C  C   . VAL A 1 199 ? 40.598 23.755  -12.562 1.00 46.07  ? 207 VAL A C   1 
ATOM   1636 O  O   . VAL A 1 199 ? 39.848 24.725  -12.653 1.00 46.75  ? 207 VAL A O   1 
ATOM   1637 C  CB  . VAL A 1 199 ? 39.170 21.891  -11.603 1.00 45.79  ? 207 VAL A CB  1 
ATOM   1638 C  CG1 . VAL A 1 199 ? 39.202 21.106  -12.904 1.00 46.20  ? 207 VAL A CG1 1 
ATOM   1639 C  CG2 . VAL A 1 199 ? 38.956 20.957  -10.422 1.00 47.25  ? 207 VAL A CG2 1 
ATOM   1640 N  N   . GLU A 1 200 ? 41.603 23.518  -13.411 1.00 45.11  ? 208 GLU A N   1 
ATOM   1641 C  CA  . GLU A 1 200 ? 41.795 24.314  -14.611 1.00 55.98  ? 208 GLU A CA  1 
ATOM   1642 C  C   . GLU A 1 200 ? 41.385 23.470  -15.815 1.00 59.13  ? 208 GLU A C   1 
ATOM   1643 O  O   . GLU A 1 200 ? 42.101 22.552  -16.207 1.00 51.95  ? 208 GLU A O   1 
ATOM   1644 C  CB  . GLU A 1 200 ? 43.248 24.786  -14.717 1.00 54.11  ? 208 GLU A CB  1 
ATOM   1645 C  CG  . GLU A 1 200 ? 43.471 25.853  -15.776 1.00 65.73  ? 208 GLU A CG  1 
ATOM   1646 C  CD  . GLU A 1 200 ? 42.689 27.138  -15.562 1.00 73.33  ? 208 GLU A CD  1 
ATOM   1647 O  OE1 . GLU A 1 200 ? 42.724 27.668  -14.433 1.00 83.33  ? 208 GLU A OE1 1 
ATOM   1648 O  OE2 . GLU A 1 200 ? 42.059 27.613  -16.528 1.00 78.25  ? 208 GLU A OE2 1 
ATOM   1649 N  N   . LEU A 1 201 ? 40.210 23.779  -16.375 1.00 54.45  ? 209 LEU A N   1 
ATOM   1650 C  CA  . LEU A 1 201 ? 39.674 23.035  -17.503 1.00 52.98  ? 209 LEU A CA  1 
ATOM   1651 C  C   . LEU A 1 201 ? 40.001 23.770  -18.799 1.00 49.79  ? 209 LEU A C   1 
ATOM   1652 O  O   . LEU A 1 201 ? 39.842 24.985  -18.891 1.00 54.91  ? 209 LEU A O   1 
ATOM   1653 C  CB  . LEU A 1 201 ? 38.161 22.869  -17.328 1.00 55.10  ? 209 LEU A CB  1 
ATOM   1654 C  CG  . LEU A 1 201 ? 37.725 21.760  -16.373 1.00 57.22  ? 209 LEU A CG  1 
ATOM   1655 C  CD1 . LEU A 1 201 ? 36.220 21.786  -16.165 1.00 63.07  ? 209 LEU A CD1 1 
ATOM   1656 C  CD2 . LEU A 1 201 ? 38.163 20.397  -16.889 1.00 67.46  ? 209 LEU A CD2 1 
ATOM   1657 N  N   . PRO A 1 202 ? 40.471 23.047  -19.839 1.00 48.49  ? 210 PRO A N   1 
ATOM   1658 C  CA  . PRO A 1 202 ? 40.826 23.664  -21.116 1.00 57.10  ? 210 PRO A CA  1 
ATOM   1659 C  C   . PRO A 1 202 ? 39.772 24.631  -21.653 1.00 63.32  ? 210 PRO A C   1 
ATOM   1660 O  O   . PRO A 1 202 ? 40.111 25.717  -22.118 1.00 59.31  ? 210 PRO A O   1 
ATOM   1661 C  CB  . PRO A 1 202 ? 40.978 22.453  -22.048 1.00 57.74  ? 210 PRO A CB  1 
ATOM   1662 C  CG  . PRO A 1 202 ? 41.448 21.347  -21.126 1.00 59.35  ? 210 PRO A CG  1 
ATOM   1663 C  CD  . PRO A 1 202 ? 40.706 21.594  -19.829 1.00 54.78  ? 210 PRO A CD  1 
ATOM   1664 N  N   . GLU A 1 203 ? 38.496 24.236  -21.579 1.00 56.93  ? 211 GLU A N   1 
ATOM   1665 C  CA  . GLU A 1 203 ? 37.438 25.004  -22.214 1.00 65.23  ? 211 GLU A CA  1 
ATOM   1666 C  C   . GLU A 1 203 ? 36.750 25.901  -21.186 1.00 62.90  ? 211 GLU A C   1 
ATOM   1667 O  O   . GLU A 1 203 ? 36.632 27.106  -21.400 1.00 59.17  ? 211 GLU A O   1 
ATOM   1668 C  CB  . GLU A 1 203 ? 36.440 24.066  -22.895 1.00 72.00  ? 211 GLU A CB  1 
ATOM   1669 C  CG  . GLU A 1 203 ? 35.876 24.619  -24.191 1.00 97.60  ? 211 GLU A CG  1 
ATOM   1670 C  CD  . GLU A 1 203 ? 34.985 23.649  -24.950 1.00 117.46 ? 211 GLU A CD  1 
ATOM   1671 O  OE1 . GLU A 1 203 ? 35.385 23.224  -26.053 1.00 110.11 ? 211 GLU A OE1 1 
ATOM   1672 O  OE2 . GLU A 1 203 ? 33.894 23.323  -24.437 1.00 88.12  ? 211 GLU A OE2 1 
ATOM   1673 N  N   . THR A 1 204 ? 36.295 25.307  -20.076 1.00 57.89  ? 212 THR A N   1 
ATOM   1674 C  CA  . THR A 1 204 ? 35.489 26.025  -19.100 1.00 54.27  ? 212 THR A CA  1 
ATOM   1675 C  C   . THR A 1 204 ? 36.350 27.037  -18.349 1.00 52.42  ? 212 THR A C   1 
ATOM   1676 O  O   . THR A 1 204 ? 35.861 28.084  -17.930 1.00 51.06  ? 212 THR A O   1 
ATOM   1677 C  CB  . THR A 1 204 ? 34.796 25.056  -18.133 1.00 59.18  ? 212 THR A CB  1 
ATOM   1678 O  OG1 . THR A 1 204 ? 34.093 24.089  -18.914 1.00 62.41  ? 212 THR A OG1 1 
ATOM   1679 C  CG2 . THR A 1 204 ? 33.839 25.748  -17.187 1.00 60.02  ? 212 THR A CG2 1 
ATOM   1680 N  N   . GLY A 1 205 ? 37.636 26.715  -18.181 1.00 55.65  ? 213 GLY A N   1 
ATOM   1681 C  CA  . GLY A 1 205 ? 38.548 27.575  -17.445 1.00 51.87  ? 213 GLY A CA  1 
ATOM   1682 C  C   . GLY A 1 205 ? 38.708 27.112  -15.999 1.00 51.14  ? 213 GLY A C   1 
ATOM   1683 O  O   . GLY A 1 205 ? 38.646 25.918  -15.718 1.00 46.72  ? 213 GLY A O   1 
ATOM   1684 N  N   . GLY A 1 206 ? 38.902 28.073  -15.089 1.00 49.58  ? 214 GLY A N   1 
ATOM   1685 C  CA  . GLY A 1 206 ? 39.208 27.770  -13.700 1.00 46.81  ? 214 GLY A CA  1 
ATOM   1686 C  C   . GLY A 1 206 ? 37.951 27.609  -12.848 1.00 42.61  ? 214 GLY A C   1 
ATOM   1687 O  O   . GLY A 1 206 ? 37.003 28.382  -12.973 1.00 43.95  ? 214 GLY A O   1 
ATOM   1688 N  N   . ILE A 1 207 ? 37.965 26.597  -11.974 1.00 42.00  ? 215 ILE A N   1 
ATOM   1689 C  CA  . ILE A 1 207 ? 36.869 26.354  -11.051 1.00 44.53  ? 215 ILE A CA  1 
ATOM   1690 C  C   . ILE A 1 207 ? 37.441 26.073  -9.665  1.00 44.08  ? 215 ILE A C   1 
ATOM   1691 O  O   . ILE A 1 207 ? 38.318 25.225  -9.514  1.00 46.34  ? 215 ILE A O   1 
ATOM   1692 C  CB  . ILE A 1 207 ? 35.989 25.183  -11.532 1.00 44.61  ? 215 ILE A CB  1 
ATOM   1693 C  CG1 . ILE A 1 207 ? 35.369 25.455  -12.905 1.00 53.85  ? 215 ILE A CG1 1 
ATOM   1694 C  CG2 . ILE A 1 207 ? 34.929 24.854  -10.493 1.00 47.30  ? 215 ILE A CG2 1 
ATOM   1695 C  CD1 . ILE A 1 207 ? 34.884 24.209  -13.609 1.00 52.60  ? 215 ILE A CD1 1 
ATOM   1696 N  N   . ILE A 1 208 ? 36.927 26.791  -8.660  1.00 46.37  ? 216 ILE A N   1 
ATOM   1697 C  CA  . ILE A 1 208 ? 37.230 26.493  -7.270  1.00 44.15  ? 216 ILE A CA  1 
ATOM   1698 C  C   . ILE A 1 208 ? 36.035 25.779  -6.649  1.00 45.13  ? 216 ILE A C   1 
ATOM   1699 O  O   . ILE A 1 208 ? 34.935 26.325  -6.601  1.00 44.79  ? 216 ILE A O   1 
ATOM   1700 C  CB  . ILE A 1 208 ? 37.579 27.772  -6.485  1.00 46.33  ? 216 ILE A CB  1 
ATOM   1701 C  CG1 . ILE A 1 208 ? 38.862 28.426  -7.003  1.00 47.16  ? 216 ILE A CG1 1 
ATOM   1702 C  CG2 . ILE A 1 208 ? 37.661 27.473  -4.996  1.00 42.70  ? 216 ILE A CG2 1 
ATOM   1703 C  CD1 . ILE A 1 208 ? 39.027 29.867  -6.579  1.00 52.27  ? 216 ILE A CD1 1 
ATOM   1704 N  N   . LEU A 1 209 ? 36.271 24.551  -6.178  1.00 42.49  ? 217 LEU A N   1 
ATOM   1705 C  CA  . LEU A 1 209 ? 35.304 23.850  -5.355  1.00 40.98  ? 217 LEU A CA  1 
ATOM   1706 C  C   . LEU A 1 209 ? 35.586 24.193  -3.896  1.00 41.44  ? 217 LEU A C   1 
ATOM   1707 O  O   . LEU A 1 209 ? 36.609 23.794  -3.343  1.00 43.68  ? 217 LEU A O   1 
ATOM   1708 C  CB  . LEU A 1 209 ? 35.413 22.346  -5.623  1.00 44.21  ? 217 LEU A CB  1 
ATOM   1709 C  CG  . LEU A 1 209 ? 35.283 21.938  -7.090  1.00 45.53  ? 217 LEU A CG  1 
ATOM   1710 C  CD1 . LEU A 1 209 ? 35.314 20.425  -7.238  1.00 47.91  ? 217 LEU A CD1 1 
ATOM   1711 C  CD2 . LEU A 1 209 ? 34.011 22.508  -7.703  1.00 45.87  ? 217 LEU A CD2 1 
ATOM   1712 N  N   . ALA A 1 210 ? 34.669 24.960  -3.298  1.00 45.12  ? 218 ALA A N   1 
ATOM   1713 C  CA  . ALA A 1 210 ? 34.853 25.524  -1.971  1.00 43.76  ? 218 ALA A CA  1 
ATOM   1714 C  C   . ALA A 1 210 ? 34.240 24.620  -0.904  1.00 47.76  ? 218 ALA A C   1 
ATOM   1715 O  O   . ALA A 1 210 ? 34.622 24.695  0.262   1.00 46.02  ? 218 ALA A O   1 
ATOM   1716 C  CB  . ALA A 1 210 ? 34.235 26.900  -1.923  1.00 52.28  ? 218 ALA A CB  1 
ATOM   1717 N  N   . SER A 1 211 ? 33.281 23.780  -1.309  1.00 41.87  ? 219 SER A N   1 
ATOM   1718 C  CA  . SER A 1 211 ? 32.499 23.001  -0.362  1.00 42.82  ? 219 SER A CA  1 
ATOM   1719 C  C   . SER A 1 211 ? 31.954 23.936  0.717   1.00 43.45  ? 219 SER A C   1 
ATOM   1720 O  O   . SER A 1 211 ? 31.457 25.013  0.399   1.00 44.45  ? 219 SER A O   1 
ATOM   1721 C  CB  . SER A 1 211 ? 33.304 21.860  0.211   1.00 44.93  ? 219 SER A CB  1 
ATOM   1722 O  OG  . SER A 1 211 ? 32.526 21.093  1.119   1.00 45.07  ? 219 SER A OG  1 
ATOM   1723 N  N   . ASP A 1 212 ? 32.056 23.539  1.992   1.00 44.55  ? 220 ASP A N   1 
ATOM   1724 C  CA  . ASP A 1 212 ? 31.398 24.282  3.056   1.00 49.02  ? 220 ASP A CA  1 
ATOM   1725 C  C   . ASP A 1 212 ? 32.261 25.445  3.545   1.00 45.78  ? 220 ASP A C   1 
ATOM   1726 O  O   . ASP A 1 212 ? 31.866 26.143  4.474   1.00 47.36  ? 220 ASP A O   1 
ATOM   1727 C  CB  . ASP A 1 212 ? 30.997 23.375  4.222   1.00 55.40  ? 220 ASP A CB  1 
ATOM   1728 C  CG  . ASP A 1 212 ? 29.791 22.499  3.927   1.00 51.20  ? 220 ASP A CG  1 
ATOM   1729 O  OD1 . ASP A 1 212 ? 29.227 22.632  2.822   1.00 46.53  ? 220 ASP A OD1 1 
ATOM   1730 O  OD2 . ASP A 1 212 ? 29.427 21.692  4.805   1.00 55.20  ? 220 ASP A OD2 1 
ATOM   1731 N  N   . ALA A 1 213 ? 33.423 25.671  2.923   1.00 43.73  ? 221 ALA A N   1 
ATOM   1732 C  CA  . ALA A 1 213 ? 34.161 26.898  3.177   1.00 41.48  ? 221 ALA A CA  1 
ATOM   1733 C  C   . ALA A 1 213 ? 33.268 28.090  2.838   1.00 49.08  ? 221 ALA A C   1 
ATOM   1734 O  O   . ALA A 1 213 ? 33.350 29.134  3.481   1.00 50.53  ? 221 ALA A O   1 
ATOM   1735 C  CB  . ALA A 1 213 ? 35.451 26.924  2.396   1.00 44.22  ? 221 ALA A CB  1 
ATOM   1736 N  N   . ILE A 1 214 ? 32.416 27.918  1.819   1.00 55.54  ? 222 ILE A N   1 
ATOM   1737 C  CA  . ILE A 1 214 ? 31.381 28.890  1.497   1.00 49.86  ? 222 ILE A CA  1 
ATOM   1738 C  C   . ILE A 1 214 ? 30.083 28.146  1.192   1.00 54.65  ? 222 ILE A C   1 
ATOM   1739 O  O   . ILE A 1 214 ? 29.975 27.464  0.175   1.00 51.30  ? 222 ILE A O   1 
ATOM   1740 C  CB  . ILE A 1 214 ? 31.779 29.786  0.307   1.00 53.82  ? 222 ILE A CB  1 
ATOM   1741 C  CG1 . ILE A 1 214 ? 33.216 30.306  0.412   1.00 52.87  ? 222 ILE A CG1 1 
ATOM   1742 C  CG2 . ILE A 1 214 ? 30.775 30.920  0.156   1.00 51.64  ? 222 ILE A CG2 1 
ATOM   1743 C  CD1 . ILE A 1 214 ? 33.749 30.883  -0.881  1.00 49.27  ? 222 ILE A CD1 1 
ATOM   1744 N  N   . TYR A 1 215 ? 29.093 28.310  2.074   1.00 50.70  ? 223 TYR A N   1 
ATOM   1745 C  CA  . TYR A 1 215 ? 27.804 27.655  1.926   1.00 55.85  ? 223 TYR A CA  1 
ATOM   1746 C  C   . TYR A 1 215 ? 27.106 28.145  0.658   1.00 50.78  ? 223 TYR A C   1 
ATOM   1747 O  O   . TYR A 1 215 ? 26.706 27.338  -0.178  1.00 47.46  ? 223 TYR A O   1 
ATOM   1748 C  CB  . TYR A 1 215 ? 26.950 27.930  3.168   1.00 60.12  ? 223 TYR A CB  1 
ATOM   1749 C  CG  . TYR A 1 215 ? 26.999 26.906  4.297   1.00 56.03  ? 223 TYR A CG  1 
ATOM   1750 C  CD1 . TYR A 1 215 ? 27.377 25.584  4.081   1.00 57.51  ? 223 TYR A CD1 1 
ATOM   1751 C  CD2 . TYR A 1 215 ? 26.654 27.272  5.593   1.00 54.95  ? 223 TYR A CD2 1 
ATOM   1752 C  CE1 . TYR A 1 215 ? 27.404 24.663  5.116   1.00 51.88  ? 223 TYR A CE1 1 
ATOM   1753 C  CE2 . TYR A 1 215 ? 26.680 26.361  6.636   1.00 53.48  ? 223 TYR A CE2 1 
ATOM   1754 C  CZ  . TYR A 1 215 ? 27.056 25.053  6.397   1.00 49.26  ? 223 TYR A CZ  1 
ATOM   1755 O  OH  . TYR A 1 215 ? 27.079 24.153  7.424   1.00 54.05  ? 223 TYR A OH  1 
ATOM   1756 N  N   . THR A 1 216 ? 26.959 29.471  0.529   1.00 49.21  ? 224 THR A N   1 
ATOM   1757 C  CA  . THR A 1 216 ? 26.140 30.063  -0.519  1.00 49.66  ? 224 THR A CA  1 
ATOM   1758 C  C   . THR A 1 216 ? 26.699 31.417  -0.943  1.00 53.52  ? 224 THR A C   1 
ATOM   1759 O  O   . THR A 1 216 ? 27.655 31.915  -0.353  1.00 50.60  ? 224 THR A O   1 
ATOM   1760 C  CB  . THR A 1 216 ? 24.695 30.294  -0.056  1.00 48.81  ? 224 THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 216 ? 24.696 31.422  0.820   1.00 54.54  ? 224 THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 216 ? 24.087 29.100  0.645   1.00 47.96  ? 224 THR A CG2 1 
ATOM   1763 N  N   . ALA A 1 217 ? 26.055 32.011  -1.955  1.00 55.01  ? 225 ALA A N   1 
ATOM   1764 C  CA  . ALA A 1 217 ? 26.425 33.318  -2.472  1.00 62.92  ? 225 ALA A CA  1 
ATOM   1765 C  C   . ALA A 1 217 ? 26.166 34.383  -1.409  1.00 54.28  ? 225 ALA A C   1 
ATOM   1766 O  O   . ALA A 1 217 ? 26.812 35.428  -1.393  1.00 59.20  ? 225 ALA A O   1 
ATOM   1767 C  CB  . ALA A 1 217 ? 25.651 33.596  -3.740  1.00 55.22  ? 225 ALA A CB  1 
ATOM   1768 N  N   . GLU A 1 218 ? 25.210 34.091  -0.521  1.00 51.83  ? 226 GLU A N   1 
ATOM   1769 C  CA  . GLU A 1 218 ? 24.859 34.979  0.574   1.00 61.87  ? 226 GLU A CA  1 
ATOM   1770 C  C   . GLU A 1 218 ? 26.002 34.989  1.587   1.00 60.12  ? 226 GLU A C   1 
ATOM   1771 O  O   . GLU A 1 218 ? 26.336 36.030  2.149   1.00 54.90  ? 226 GLU A O   1 
ATOM   1772 C  CB  . GLU A 1 218 ? 23.548 34.509  1.209   1.00 63.60  ? 226 GLU A CB  1 
ATOM   1773 C  CG  . GLU A 1 218 ? 22.861 35.564  2.057   1.00 73.07  ? 226 GLU A CG  1 
ATOM   1774 C  CD  . GLU A 1 218 ? 21.712 35.042  2.902   1.00 73.21  ? 226 GLU A CD  1 
ATOM   1775 O  OE1 . GLU A 1 218 ? 21.328 33.868  2.718   1.00 76.63  ? 226 GLU A OE1 1 
ATOM   1776 O  OE2 . GLU A 1 218 ? 21.213 35.805  3.753   1.00 68.89  ? 226 GLU A OE2 1 
ATOM   1777 N  N   . SER A 1 219 ? 26.586 33.806  1.810   1.00 57.01  ? 227 SER A N   1 
ATOM   1778 C  CA  . SER A 1 219 ? 27.751 33.652  2.665   1.00 56.62  ? 227 SER A CA  1 
ATOM   1779 C  C   . SER A 1 219 ? 28.905 34.479  2.106   1.00 51.94  ? 227 SER A C   1 
ATOM   1780 O  O   . SER A 1 219 ? 29.583 35.196  2.839   1.00 49.11  ? 227 SER A O   1 
ATOM   1781 C  CB  . SER A 1 219 ? 28.141 32.197  2.783   1.00 54.60  ? 227 SER A CB  1 
ATOM   1782 O  OG  . SER A 1 219 ? 27.034 31.397  3.175   1.00 51.25  ? 227 SER A OG  1 
ATOM   1783 N  N   . TYR A 1 220 ? 29.096 34.365  0.789   1.00 45.61  ? 228 TYR A N   1 
ATOM   1784 C  CA  . TYR A 1 220 ? 30.245 34.924  0.098   1.00 50.99  ? 228 TYR A CA  1 
ATOM   1785 C  C   . TYR A 1 220 ? 30.197 36.449  0.128   1.00 54.30  ? 228 TYR A C   1 
ATOM   1786 O  O   . TYR A 1 220 ? 31.224 37.096  0.315   1.00 56.09  ? 228 TYR A O   1 
ATOM   1787 C  CB  . TYR A 1 220 ? 30.228 34.363  -1.327  1.00 45.92  ? 228 TYR A CB  1 
ATOM   1788 C  CG  . TYR A 1 220 ? 31.521 34.527  -2.112  1.00 48.05  ? 228 TYR A CG  1 
ATOM   1789 C  CD1 . TYR A 1 220 ? 32.753 34.218  -1.547  1.00 54.38  ? 228 TYR A CD1 1 
ATOM   1790 C  CD2 . TYR A 1 220 ? 31.504 34.958  -3.432  1.00 48.36  ? 228 TYR A CD2 1 
ATOM   1791 C  CE1 . TYR A 1 220 ? 33.929 34.354  -2.264  1.00 53.38  ? 228 TYR A CE1 1 
ATOM   1792 C  CE2 . TYR A 1 220 ? 32.673 35.095  -4.162  1.00 50.68  ? 228 TYR A CE2 1 
ATOM   1793 C  CZ  . TYR A 1 220 ? 33.889 34.792  -3.576  1.00 54.61  ? 228 TYR A CZ  1 
ATOM   1794 O  OH  . TYR A 1 220 ? 35.039 34.930  -4.297  1.00 55.46  ? 228 TYR A OH  1 
ATOM   1795 N  N   . GLY A 1 221 ? 29.002 37.016  -0.068  1.00 51.76  ? 229 GLY A N   1 
ATOM   1796 C  CA  . GLY A 1 221 ? 28.861 38.461  -0.129  1.00 58.57  ? 229 GLY A CA  1 
ATOM   1797 C  C   . GLY A 1 221 ? 29.680 39.051  -1.275  1.00 62.13  ? 229 GLY A C   1 
ATOM   1798 O  O   . GLY A 1 221 ? 29.674 38.510  -2.379  1.00 65.42  ? 229 GLY A O   1 
ATOM   1799 N  N   . PRO A 1 222 ? 30.433 40.156  -1.057  1.00 68.17  ? 230 PRO A N   1 
ATOM   1800 C  CA  . PRO A 1 222 ? 30.588 40.759  0.269   1.00 75.16  ? 230 PRO A CA  1 
ATOM   1801 C  C   . PRO A 1 222 ? 29.370 41.550  0.745   1.00 76.61  ? 230 PRO A C   1 
ATOM   1802 O  O   . PRO A 1 222 ? 28.553 41.992  -0.060  1.00 79.85  ? 230 PRO A O   1 
ATOM   1803 C  CB  . PRO A 1 222 ? 31.804 41.688  0.112   1.00 70.76  ? 230 PRO A CB  1 
ATOM   1804 C  CG  . PRO A 1 222 ? 31.892 41.998  -1.375  1.00 76.58  ? 230 PRO A CG  1 
ATOM   1805 C  CD  . PRO A 1 222 ? 31.188 40.868  -2.098  1.00 74.89  ? 230 PRO A CD  1 
ATOM   1806 N  N   . PRO A 1 223 ? 29.214 41.750  2.075   1.00 76.67  ? 231 PRO A N   1 
ATOM   1807 C  CA  . PRO A 1 223 ? 30.188 41.269  3.054   1.00 77.82  ? 231 PRO A CA  1 
ATOM   1808 C  C   . PRO A 1 223 ? 29.913 39.817  3.437   1.00 70.06  ? 231 PRO A C   1 
ATOM   1809 O  O   . PRO A 1 223 ? 28.844 39.289  3.141   1.00 63.98  ? 231 PRO A O   1 
ATOM   1810 C  CB  . PRO A 1 223 ? 29.933 42.228  4.224   1.00 75.11  ? 231 PRO A CB  1 
ATOM   1811 C  CG  . PRO A 1 223 ? 28.430 42.416  4.193   1.00 80.63  ? 231 PRO A CG  1 
ATOM   1812 C  CD  . PRO A 1 223 ? 28.075 42.426  2.717   1.00 82.97  ? 231 PRO A CD  1 
ATOM   1813 N  N   . ILE A 1 224 ? 30.882 39.184  4.105   1.00 68.25  ? 232 ILE A N   1 
ATOM   1814 C  CA  . ILE A 1 224 ? 30.758 37.785  4.479   1.00 64.30  ? 232 ILE A CA  1 
ATOM   1815 C  C   . ILE A 1 224 ? 29.700 37.655  5.572   1.00 60.59  ? 232 ILE A C   1 
ATOM   1816 O  O   . ILE A 1 224 ? 29.661 38.453  6.505   1.00 68.12  ? 232 ILE A O   1 
ATOM   1817 C  CB  . ILE A 1 224 ? 32.123 37.217  4.918   1.00 58.28  ? 232 ILE A CB  1 
ATOM   1818 C  CG1 . ILE A 1 224 ? 33.170 37.369  3.812   1.00 52.90  ? 232 ILE A CG1 1 
ATOM   1819 C  CG2 . ILE A 1 224 ? 31.990 35.771  5.373   1.00 59.40  ? 232 ILE A CG2 1 
ATOM   1820 C  CD1 . ILE A 1 224 ? 34.597 37.296  4.300   1.00 61.97  ? 232 ILE A CD1 1 
ATOM   1821 N  N   . LYS A 1 225 ? 28.837 36.644  5.426   1.00 65.44  ? 233 LYS A N   1 
ATOM   1822 C  CA  . LYS A 1 225 ? 27.831 36.322  6.425   1.00 66.51  ? 233 LYS A CA  1 
ATOM   1823 C  C   . LYS A 1 225 ? 28.109 34.914  6.945   1.00 61.29  ? 233 LYS A C   1 
ATOM   1824 O  O   . LYS A 1 225 ? 27.685 33.928  6.347   1.00 71.92  ? 233 LYS A O   1 
ATOM   1825 C  CB  . LYS A 1 225 ? 26.424 36.441  5.827   1.00 70.25  ? 233 LYS A CB  1 
ATOM   1826 C  CG  . LYS A 1 225 ? 26.049 37.838  5.347   1.00 82.98  ? 233 LYS A CG  1 
ATOM   1827 C  CD  . LYS A 1 225 ? 24.757 37.895  4.558   1.00 97.42  ? 233 LYS A CD  1 
ATOM   1828 C  CE  . LYS A 1 225 ? 23.543 38.215  5.404   1.00 93.41  ? 233 LYS A CE  1 
ATOM   1829 N  NZ  . LYS A 1 225 ? 22.316 38.316  4.579   1.00 90.08  ? 233 LYS A NZ  1 
ATOM   1830 N  N   . PRO A 1 226 ? 28.843 34.782  8.072   1.00 62.53  ? 234 PRO A N   1 
ATOM   1831 C  CA  . PRO A 1 226 ? 29.295 33.474  8.552   1.00 56.79  ? 234 PRO A CA  1 
ATOM   1832 C  C   . PRO A 1 226 ? 28.163 32.527  8.942   1.00 59.50  ? 234 PRO A C   1 
ATOM   1833 O  O   . PRO A 1 226 ? 27.036 32.957  9.173   1.00 65.43  ? 234 PRO A O   1 
ATOM   1834 C  CB  . PRO A 1 226 ? 30.143 33.828  9.784   1.00 57.45  ? 234 PRO A CB  1 
ATOM   1835 C  CG  . PRO A 1 226 ? 29.593 35.164  10.237  1.00 62.11  ? 234 PRO A CG  1 
ATOM   1836 C  CD  . PRO A 1 226 ? 29.275 35.885  8.944   1.00 56.56  ? 234 PRO A CD  1 
ATOM   1837 N  N   . PRO A 1 227 ? 28.441 31.206  9.019   1.00 58.39  ? 235 PRO A N   1 
ATOM   1838 C  CA  . PRO A 1 227 ? 27.444 30.212  9.417   1.00 58.74  ? 235 PRO A CA  1 
ATOM   1839 C  C   . PRO A 1 227 ? 27.397 29.930  10.917  1.00 67.24  ? 235 PRO A C   1 
ATOM   1840 O  O   . PRO A 1 227 ? 28.310 30.300  11.652  1.00 69.33  ? 235 PRO A O   1 
ATOM   1841 C  CB  . PRO A 1 227 ? 27.959 28.972  8.672   1.00 58.94  ? 235 PRO A CB  1 
ATOM   1842 C  CG  . PRO A 1 227 ? 29.467 29.102  8.763   1.00 58.72  ? 235 PRO A CG  1 
ATOM   1843 C  CD  . PRO A 1 227 ? 29.736 30.592  8.685   1.00 60.77  ? 235 PRO A CD  1 
ATOM   1844 N  N   . GLY A 1 228 ? 26.322 29.263  11.357  1.00 64.45  ? 236 GLY A N   1 
ATOM   1845 C  CA  . GLY A 1 228 ? 26.204 28.805  12.731  1.00 65.58  ? 236 GLY A CA  1 
ATOM   1846 C  C   . GLY A 1 228 ? 27.057 27.564  12.987  1.00 70.59  ? 236 GLY A C   1 
ATOM   1847 O  O   . GLY A 1 228 ? 27.549 27.366  14.096  1.00 72.54  ? 236 GLY A O   1 
ATOM   1848 N  N   . ILE A 1 229 ? 27.212 26.730  11.951  1.00 79.53  ? 237 ILE A N   1 
ATOM   1849 C  CA  . ILE A 1 229 ? 28.122 25.596  12.004  1.00 80.16  ? 237 ILE A CA  1 
ATOM   1850 C  C   . ILE A 1 229 ? 29.531 26.103  11.710  1.00 78.67  ? 237 ILE A C   1 
ATOM   1851 O  O   . ILE A 1 229 ? 29.894 26.298  10.552  1.00 70.80  ? 237 ILE A O   1 
ATOM   1852 C  CB  . ILE A 1 229 ? 27.705 24.486  11.016  1.00 84.46  ? 237 ILE A CB  1 
ATOM   1853 C  CG1 . ILE A 1 229 ? 26.186 24.304  10.957  1.00 91.28  ? 237 ILE A CG1 1 
ATOM   1854 C  CG2 . ILE A 1 229 ? 28.420 23.182  11.334  1.00 79.23  ? 237 ILE A CG2 1 
ATOM   1855 C  CD1 . ILE A 1 229 ? 25.745 22.864  10.823  1.00 85.16  ? 237 ILE A CD1 1 
ATOM   1856 N  N   . ILE A 1 230 ? 30.319 26.314  12.771  1.00 75.72  ? 238 ILE A N   1 
ATOM   1857 C  CA  . ILE A 1 230 ? 31.629 26.926  12.632  1.00 59.92  ? 238 ILE A CA  1 
ATOM   1858 C  C   . ILE A 1 230 ? 32.498 26.533  13.824  1.00 57.05  ? 238 ILE A C   1 
ATOM   1859 O  O   . ILE A 1 230 ? 32.040 26.543  14.963  1.00 63.65  ? 238 ILE A O   1 
ATOM   1860 C  CB  . ILE A 1 230 ? 31.488 28.456  12.497  1.00 57.06  ? 238 ILE A CB  1 
ATOM   1861 C  CG1 . ILE A 1 230 ? 32.759 29.106  11.948  1.00 53.41  ? 238 ILE A CG1 1 
ATOM   1862 C  CG2 . ILE A 1 230 ? 31.060 29.077  13.819  1.00 54.37  ? 238 ILE A CG2 1 
ATOM   1863 C  CD1 . ILE A 1 230 ? 32.536 30.487  11.379  1.00 60.50  ? 238 ILE A CD1 1 
ATOM   1864 N  N   . TYR A 1 231 ? 33.758 26.186  13.540  1.00 52.25  ? 239 TYR A N   1 
ATOM   1865 C  CA  . TYR A 1 231 ? 34.710 25.804  14.569  1.00 55.14  ? 239 TYR A CA  1 
ATOM   1866 C  C   . TYR A 1 231 ? 35.687 26.953  14.805  1.00 45.29  ? 239 TYR A C   1 
ATOM   1867 O  O   . TYR A 1 231 ? 35.966 27.305  15.949  1.00 52.07  ? 239 TYR A O   1 
ATOM   1868 C  CB  . TYR A 1 231 ? 35.414 24.508  14.149  1.00 43.61  ? 239 TYR A CB  1 
ATOM   1869 C  CG  . TYR A 1 231 ? 36.745 24.241  14.841  1.00 42.08  ? 239 TYR A CG  1 
ATOM   1870 C  CD1 . TYR A 1 231 ? 36.807 23.837  16.169  1.00 41.87  ? 239 TYR A CD1 1 
ATOM   1871 C  CD2 . TYR A 1 231 ? 37.945 24.408  14.160  1.00 46.14  ? 239 TYR A CD2 1 
ATOM   1872 C  CE1 . TYR A 1 231 ? 38.020 23.597  16.795  1.00 41.55  ? 239 TYR A CE1 1 
ATOM   1873 C  CE2 . TYR A 1 231 ? 39.163 24.173  14.774  1.00 42.83  ? 239 TYR A CE2 1 
ATOM   1874 C  CZ  . TYR A 1 231 ? 39.201 23.765  16.094  1.00 42.73  ? 239 TYR A CZ  1 
ATOM   1875 O  OH  . TYR A 1 231 ? 40.399 23.537  16.708  1.00 53.51  ? 239 TYR A OH  1 
ATOM   1876 N  N   . ASP A 1 232 ? 36.199 27.526  13.709  1.00 41.66  ? 240 ASP A N   1 
ATOM   1877 C  CA  . ASP A 1 232 ? 37.207 28.572  13.765  1.00 43.15  ? 240 ASP A CA  1 
ATOM   1878 C  C   . ASP A 1 232 ? 36.715 29.779  12.970  1.00 40.94  ? 240 ASP A C   1 
ATOM   1879 O  O   . ASP A 1 232 ? 36.945 29.869  11.767  1.00 46.03  ? 240 ASP A O   1 
ATOM   1880 C  CB  . ASP A 1 232 ? 38.546 28.054  13.231  1.00 43.86  ? 240 ASP A CB  1 
ATOM   1881 C  CG  . ASP A 1 232 ? 39.653 29.092  13.175  1.00 39.47  ? 240 ASP A CG  1 
ATOM   1882 O  OD1 . ASP A 1 232 ? 39.469 30.180  13.751  1.00 49.56  ? 240 ASP A OD1 1 
ATOM   1883 O  OD2 . ASP A 1 232 ? 40.688 28.804  12.538  1.00 42.12  ? 240 ASP A OD2 1 
ATOM   1884 N  N   . SER A 1 233 ? 36.035 30.700  13.661  1.00 43.38  ? 241 SER A N   1 
ATOM   1885 C  CA  . SER A 1 233 ? 35.452 31.875  13.033  1.00 45.44  ? 241 SER A CA  1 
ATOM   1886 C  C   . SER A 1 233 ? 36.500 32.621  12.208  1.00 45.11  ? 241 SER A C   1 
ATOM   1887 O  O   . SER A 1 233 ? 36.249 32.976  11.060  1.00 52.50  ? 241 SER A O   1 
ATOM   1888 C  CB  . SER A 1 233 ? 34.816 32.778  14.064  1.00 47.28  ? 241 SER A CB  1 
ATOM   1889 O  OG  . SER A 1 233 ? 35.739 33.117  15.087  1.00 54.37  ? 241 SER A OG  1 
ATOM   1890 N  N   . LEU A 1 234 ? 37.675 32.855  12.801  1.00 44.04  ? 242 LEU A N   1 
ATOM   1891 C  CA  . LEU A 1 234 ? 38.706 33.657  12.163  1.00 45.48  ? 242 LEU A CA  1 
ATOM   1892 C  C   . LEU A 1 234 ? 39.242 32.942  10.924  1.00 49.54  ? 242 LEU A C   1 
ATOM   1893 O  O   . LEU A 1 234 ? 39.391 33.557  9.871   1.00 45.95  ? 242 LEU A O   1 
ATOM   1894 C  CB  . LEU A 1 234 ? 39.824 33.937  13.171  1.00 42.72  ? 242 LEU A CB  1 
ATOM   1895 C  CG  . LEU A 1 234 ? 39.447 34.871  14.319  1.00 51.50  ? 242 LEU A CG  1 
ATOM   1896 C  CD1 . LEU A 1 234 ? 40.682 35.294  15.099  1.00 48.17  ? 242 LEU A CD1 1 
ATOM   1897 C  CD2 . LEU A 1 234 ? 38.696 36.092  13.808  1.00 48.86  ? 242 LEU A CD2 1 
ATOM   1898 N  N   . GLY A 1 235 ? 39.547 31.648  11.062  1.00 43.61  ? 243 GLY A N   1 
ATOM   1899 C  CA  . GLY A 1 235 ? 39.998 30.854  9.931   1.00 48.67  ? 243 GLY A CA  1 
ATOM   1900 C  C   . GLY A 1 235 ? 38.959 30.845  8.814   1.00 44.24  ? 243 GLY A C   1 
ATOM   1901 O  O   . GLY A 1 235 ? 39.302 30.890  7.635   1.00 46.85  ? 243 GLY A O   1 
ATOM   1902 N  N   . TYR A 1 236 ? 37.682 30.797  9.208   1.00 42.40  ? 244 TYR A N   1 
ATOM   1903 C  CA  . TYR A 1 236 ? 36.581 30.817  8.261   1.00 45.93  ? 244 TYR A CA  1 
ATOM   1904 C  C   . TYR A 1 236 ? 36.645 32.101  7.438   1.00 48.10  ? 244 TYR A C   1 
ATOM   1905 O  O   . TYR A 1 236 ? 36.616 32.059  6.211   1.00 44.77  ? 244 TYR A O   1 
ATOM   1906 C  CB  . TYR A 1 236 ? 35.231 30.717  8.977   1.00 47.08  ? 244 TYR A CB  1 
ATOM   1907 C  CG  . TYR A 1 236 ? 34.045 30.849  8.032   1.00 48.87  ? 244 TYR A CG  1 
ATOM   1908 C  CD1 . TYR A 1 236 ? 33.551 29.752  7.339   1.00 49.15  ? 244 TYR A CD1 1 
ATOM   1909 C  CD2 . TYR A 1 236 ? 33.457 32.085  7.794   1.00 51.08  ? 244 TYR A CD2 1 
ATOM   1910 C  CE1 . TYR A 1 236 ? 32.485 29.873  6.463   1.00 51.40  ? 244 TYR A CE1 1 
ATOM   1911 C  CE2 . TYR A 1 236 ? 32.392 32.221  6.920   1.00 55.43  ? 244 TYR A CE2 1 
ATOM   1912 C  CZ  . TYR A 1 236 ? 31.906 31.112  6.250   1.00 55.39  ? 244 TYR A CZ  1 
ATOM   1913 O  OH  . TYR A 1 236 ? 30.858 31.243  5.386   1.00 56.42  ? 244 TYR A OH  1 
ATOM   1914 N  N   . MET A 1 237 ? 36.725 33.242  8.131   1.00 45.40  ? 245 MET A N   1 
ATOM   1915 C  CA  . MET A 1 237 ? 36.721 34.537  7.474   1.00 43.72  ? 245 MET A CA  1 
ATOM   1916 C  C   . MET A 1 237 ? 37.950 34.643  6.573   1.00 46.56  ? 245 MET A C   1 
ATOM   1917 O  O   . MET A 1 237 ? 37.844 35.108  5.441   1.00 50.17  ? 245 MET A O   1 
ATOM   1918 C  CB  . MET A 1 237 ? 36.730 35.677  8.499   1.00 50.39  ? 245 MET A CB  1 
ATOM   1919 C  CG  . MET A 1 237 ? 35.521 35.668  9.422   1.00 56.78  ? 245 MET A CG  1 
ATOM   1920 S  SD  . MET A 1 237 ? 33.941 35.931  8.572   1.00 65.05  ? 245 MET A SD  1 
ATOM   1921 C  CE  . MET A 1 237 ? 34.180 37.589  7.934   1.00 71.04  ? 245 MET A CE  1 
ATOM   1922 N  N   . ASN A 1 238 ? 39.111 34.202  7.073   1.00 42.21  ? 246 ASN A N   1 
ATOM   1923 C  CA  . ASN A 1 238 ? 40.334 34.254  6.288   1.00 47.38  ? 246 ASN A CA  1 
ATOM   1924 C  C   . ASN A 1 238 ? 40.167 33.419  5.021   1.00 42.78  ? 246 ASN A C   1 
ATOM   1925 O  O   . ASN A 1 238 ? 40.585 33.837  3.944   1.00 47.65  ? 246 ASN A O   1 
ATOM   1926 C  CB  . ASN A 1 238 ? 41.568 33.777  7.059   1.00 51.10  ? 246 ASN A CB  1 
ATOM   1927 C  CG  . ASN A 1 238 ? 41.901 34.646  8.253   1.00 64.56  ? 246 ASN A CG  1 
ATOM   1928 O  OD1 . ASN A 1 238 ? 41.723 35.861  8.213   1.00 57.72  ? 246 ASN A OD1 1 
ATOM   1929 N  ND2 . ASN A 1 238 ? 42.372 34.029  9.324   1.00 60.71  ? 246 ASN A ND2 1 
ATOM   1930 N  N   . THR A 1 239 ? 39.560 32.235  5.161   1.00 44.53  ? 247 THR A N   1 
ATOM   1931 C  CA  . THR A 1 239 ? 39.442 31.304  4.051   1.00 45.53  ? 247 THR A CA  1 
ATOM   1932 C  C   . THR A 1 239 ? 38.584 31.911  2.940   1.00 46.39  ? 247 THR A C   1 
ATOM   1933 O  O   . THR A 1 239 ? 38.938 31.819  1.767   1.00 45.86  ? 247 THR A O   1 
ATOM   1934 C  CB  . THR A 1 239 ? 38.906 29.945  4.522   1.00 45.73  ? 247 THR A CB  1 
ATOM   1935 O  OG1 . THR A 1 239 ? 39.909 29.337  5.337   1.00 46.29  ? 247 THR A OG1 1 
ATOM   1936 C  CG2 . THR A 1 239 ? 38.555 29.021  3.376   1.00 47.46  ? 247 THR A CG2 1 
ATOM   1937 N  N   . VAL A 1 240 ? 37.459 32.536  3.305   1.00 44.09  ? 248 VAL A N   1 
ATOM   1938 C  CA  . VAL A 1 240 ? 36.547 33.076  2.308   1.00 48.42  ? 248 VAL A CA  1 
ATOM   1939 C  C   . VAL A 1 240 ? 37.276 34.128  1.476   1.00 49.76  ? 248 VAL A C   1 
ATOM   1940 O  O   . VAL A 1 240 ? 37.137 34.158  0.256   1.00 53.67  ? 248 VAL A O   1 
ATOM   1941 C  CB  . VAL A 1 240 ? 35.270 33.660  2.941   1.00 44.09  ? 248 VAL A CB  1 
ATOM   1942 C  CG1 . VAL A 1 240 ? 34.378 34.311  1.895   1.00 47.59  ? 248 VAL A CG1 1 
ATOM   1943 C  CG2 . VAL A 1 240 ? 34.496 32.608  3.721   1.00 46.76  ? 248 VAL A CG2 1 
ATOM   1944 N  N   . GLU A 1 241 ? 38.050 34.987  2.146   1.00 46.11  ? 249 GLU A N   1 
ATOM   1945 C  CA  . GLU A 1 241 ? 38.756 36.063  1.471   1.00 50.55  ? 249 GLU A CA  1 
ATOM   1946 C  C   . GLU A 1 241 ? 39.887 35.495  0.618   1.00 45.35  ? 249 GLU A C   1 
ATOM   1947 O  O   . GLU A 1 241 ? 40.212 36.050  -0.428  1.00 53.48  ? 249 GLU A O   1 
ATOM   1948 C  CB  . GLU A 1 241 ? 39.265 37.085  2.489   1.00 57.71  ? 249 GLU A CB  1 
ATOM   1949 C  CG  . GLU A 1 241 ? 38.207 38.093  2.905   1.00 65.26  ? 249 GLU A CG  1 
ATOM   1950 C  CD  . GLU A 1 241 ? 37.512 38.789  1.746   1.00 76.38  ? 249 GLU A CD  1 
ATOM   1951 O  OE1 . GLU A 1 241 ? 38.218 39.315  0.861   1.00 75.05  ? 249 GLU A OE1 1 
ATOM   1952 O  OE2 . GLU A 1 241 ? 36.264 38.810  1.736   1.00 88.86  ? 249 GLU A OE2 1 
ATOM   1953 N  N   . ARG A 1 242 ? 40.486 34.388  1.068   1.00 43.77  ? 250 ARG A N   1 
ATOM   1954 C  CA  . ARG A 1 242 ? 41.524 33.729  0.294   1.00 47.10  ? 250 ARG A CA  1 
ATOM   1955 C  C   . ARG A 1 242 ? 40.923 33.211  -1.010  1.00 43.60  ? 250 ARG A C   1 
ATOM   1956 O  O   . ARG A 1 242 ? 41.533 33.336  -2.069  1.00 50.17  ? 250 ARG A O   1 
ATOM   1957 C  CB  . ARG A 1 242 ? 42.162 32.595  1.102   1.00 44.81  ? 250 ARG A CB  1 
ATOM   1958 C  CG  . ARG A 1 242 ? 43.196 31.785  0.334   1.00 50.66  ? 250 ARG A CG  1 
ATOM   1959 C  CD  . ARG A 1 242 ? 43.636 30.573  1.129   1.00 53.12  ? 250 ARG A CD  1 
ATOM   1960 N  NE  . ARG A 1 242 ? 44.422 29.642  0.335   1.00 61.83  ? 250 ARG A NE  1 
ATOM   1961 C  CZ  . ARG A 1 242 ? 44.811 28.446  0.759   1.00 66.23  ? 250 ARG A CZ  1 
ATOM   1962 N  NH1 . ARG A 1 242 ? 44.568 28.078  2.005   1.00 60.56  ? 250 ARG A NH1 1 
ATOM   1963 N  NH2 . ARG A 1 242 ? 45.446 27.625  -0.061  1.00 72.72  ? 250 ARG A NH2 1 
ATOM   1964 N  N   . ILE A 1 243 ? 39.722 32.630  -0.917  1.00 44.66  ? 251 ILE A N   1 
ATOM   1965 C  CA  . ILE A 1 243 ? 39.023 32.116  -2.083  1.00 45.86  ? 251 ILE A CA  1 
ATOM   1966 C  C   . ILE A 1 243 ? 38.740 33.271  -3.042  1.00 46.37  ? 251 ILE A C   1 
ATOM   1967 O  O   . ILE A 1 243 ? 38.975 33.147  -4.242  1.00 50.10  ? 251 ILE A O   1 
ATOM   1968 C  CB  . ILE A 1 243 ? 37.745 31.359  -1.665  1.00 45.66  ? 251 ILE A CB  1 
ATOM   1969 C  CG1 . ILE A 1 243 ? 38.090 30.017  -1.013  1.00 44.69  ? 251 ILE A CG1 1 
ATOM   1970 C  CG2 . ILE A 1 243 ? 36.805 31.177  -2.848  1.00 46.42  ? 251 ILE A CG2 1 
ATOM   1971 C  CD1 . ILE A 1 243 ? 37.008 29.462  -0.120  1.00 45.33  ? 251 ILE A CD1 1 
ATOM   1972 N  N   . ARG A 1 244 ? 38.255 34.396  -2.505  1.00 49.52  ? 252 ARG A N   1 
ATOM   1973 C  CA  . ARG A 1 244 ? 37.923 35.553  -3.321  1.00 48.20  ? 252 ARG A CA  1 
ATOM   1974 C  C   . ARG A 1 244 ? 39.159 36.001  -4.100  1.00 48.82  ? 252 ARG A C   1 
ATOM   1975 O  O   . ARG A 1 244 ? 39.059 36.352  -5.273  1.00 50.64  ? 252 ARG A O   1 
ATOM   1976 C  CB  . ARG A 1 244 ? 37.367 36.685  -2.450  1.00 50.82  ? 252 ARG A CB  1 
ATOM   1977 C  CG  . ARG A 1 244 ? 36.668 37.788  -3.233  1.00 60.57  ? 252 ARG A CG  1 
ATOM   1978 C  CD  . ARG A 1 244 ? 36.029 38.836  -2.340  1.00 58.81  ? 252 ARG A CD  1 
ATOM   1979 N  NE  . ARG A 1 244 ? 35.456 38.308  -1.107  1.00 54.88  ? 252 ARG A NE  1 
ATOM   1980 C  CZ  . ARG A 1 244 ? 34.158 38.125  -0.889  1.00 65.47  ? 252 ARG A CZ  1 
ATOM   1981 N  NH1 . ARG A 1 244 ? 33.319 38.016  -1.906  1.00 60.39  ? 252 ARG A NH1 1 
ATOM   1982 N  NH2 . ARG A 1 244 ? 33.713 37.974  0.352   1.00 73.69  ? 252 ARG A NH2 1 
ATOM   1983 N  N   . ARG A 1 245 ? 40.325 35.972  -3.444  1.00 47.30  ? 253 ARG A N   1 
ATOM   1984 C  CA  . ARG A 1 245 ? 41.556 36.441  -4.061  1.00 55.22  ? 253 ARG A CA  1 
ATOM   1985 C  C   . ARG A 1 245 ? 41.996 35.472  -5.160  1.00 47.53  ? 253 ARG A C   1 
ATOM   1986 O  O   . ARG A 1 245 ? 42.341 35.904  -6.257  1.00 50.78  ? 253 ARG A O   1 
ATOM   1987 C  CB  . ARG A 1 245 ? 42.655 36.620  -3.009  1.00 55.43  ? 253 ARG A CB  1 
ATOM   1988 C  CG  . ARG A 1 245 ? 43.931 37.237  -3.563  1.00 69.40  ? 253 ARG A CG  1 
ATOM   1989 C  CD  . ARG A 1 245 ? 45.173 36.760  -2.837  1.00 72.77  ? 253 ARG A CD  1 
ATOM   1990 N  NE  . ARG A 1 245 ? 44.988 35.507  -2.117  1.00 76.51  ? 253 ARG A NE  1 
ATOM   1991 C  CZ  . ARG A 1 245 ? 45.603 34.366  -2.403  1.00 79.97  ? 253 ARG A CZ  1 
ATOM   1992 N  NH1 . ARG A 1 245 ? 46.049 34.130  -3.625  1.00 76.65  ? 253 ARG A NH1 1 
ATOM   1993 N  NH2 . ARG A 1 245 ? 45.695 33.430  -1.472  1.00 85.07  ? 253 ARG A NH2 1 
ATOM   1994 N  N   . ILE A 1 246 ? 41.998 34.166  -4.861  1.00 45.26  ? 254 ILE A N   1 
ATOM   1995 C  CA  . ILE A 1 246 ? 42.383 33.158  -5.839  1.00 50.43  ? 254 ILE A CA  1 
ATOM   1996 C  C   . ILE A 1 246 ? 41.478 33.276  -7.065  1.00 50.49  ? 254 ILE A C   1 
ATOM   1997 O  O   . ILE A 1 246 ? 41.961 33.263  -8.195  1.00 55.71  ? 254 ILE A O   1 
ATOM   1998 C  CB  . ILE A 1 246 ? 42.348 31.741  -5.229  1.00 53.90  ? 254 ILE A CB  1 
ATOM   1999 C  CG1 . ILE A 1 246 ? 43.361 31.592  -4.091  1.00 61.69  ? 254 ILE A CG1 1 
ATOM   2000 C  CG2 . ILE A 1 246 ? 42.559 30.680  -6.299  1.00 55.43  ? 254 ILE A CG2 1 
ATOM   2001 C  CD1 . ILE A 1 246 ? 43.171 30.344  -3.261  1.00 61.62  ? 254 ILE A CD1 1 
ATOM   2002 N  N   . ALA A 1 247 ? 40.166 33.395  -6.832  1.00 49.12  ? 255 ALA A N   1 
ATOM   2003 C  CA  . ALA A 1 247 ? 39.197 33.506  -7.912  1.00 55.80  ? 255 ALA A CA  1 
ATOM   2004 C  C   . ALA A 1 247 ? 39.539 34.698  -8.801  1.00 51.55  ? 255 ALA A C   1 
ATOM   2005 O  O   . ALA A 1 247 ? 39.511 34.593  -10.025 1.00 53.39  ? 255 ALA A O   1 
ATOM   2006 C  CB  . ALA A 1 247 ? 37.805 33.640  -7.347  1.00 46.54  ? 255 ALA A CB  1 
ATOM   2007 N  N   . GLN A 1 248 ? 39.850 35.831  -8.164  1.00 55.57  ? 256 GLN A N   1 
ATOM   2008 C  CA  . GLN A 1 248 ? 40.131 37.068  -8.872  1.00 58.39  ? 256 GLN A CA  1 
ATOM   2009 C  C   . GLN A 1 248 ? 41.412 36.922  -9.694  1.00 53.64  ? 256 GLN A C   1 
ATOM   2010 O  O   . GLN A 1 248 ? 41.453 37.334  -10.850 1.00 59.43  ? 256 GLN A O   1 
ATOM   2011 C  CB  . GLN A 1 248 ? 40.264 38.225  -7.881  1.00 65.98  ? 256 GLN A CB  1 
ATOM   2012 C  CG  . GLN A 1 248 ? 40.443 39.577  -8.554  1.00 85.78  ? 256 GLN A CG  1 
ATOM   2013 C  CD  . GLN A 1 248 ? 41.639 40.325  -8.017  1.00 81.55  ? 256 GLN A CD  1 
ATOM   2014 O  OE1 . GLN A 1 248 ? 42.256 39.927  -7.031  1.00 76.47  ? 256 GLN A OE1 1 
ATOM   2015 N  NE2 . GLN A 1 248 ? 41.983 41.419  -8.675  1.00 80.41  ? 256 GLN A NE2 1 
ATOM   2016 N  N   . GLU A 1 249 ? 42.453 36.333  -9.093  1.00 50.40  ? 257 GLU A N   1 
ATOM   2017 C  CA  . GLU A 1 249 ? 43.765 36.278  -9.721  1.00 57.82  ? 257 GLU A CA  1 
ATOM   2018 C  C   . GLU A 1 249 ? 43.823 35.165  -10.768 1.00 56.36  ? 257 GLU A C   1 
ATOM   2019 O  O   . GLU A 1 249 ? 44.636 35.233  -11.686 1.00 65.02  ? 257 GLU A O   1 
ATOM   2020 C  CB  . GLU A 1 249 ? 44.853 36.083  -8.663  1.00 69.52  ? 257 GLU A CB  1 
ATOM   2021 C  CG  . GLU A 1 249 ? 45.031 37.283  -7.747  1.00 73.51  ? 257 GLU A CG  1 
ATOM   2022 C  CD  . GLU A 1 249 ? 45.954 37.049  -6.563  1.00 80.28  ? 257 GLU A CD  1 
ATOM   2023 O  OE1 . GLU A 1 249 ? 46.320 35.879  -6.318  1.00 78.18  ? 257 GLU A OE1 1 
ATOM   2024 O  OE2 . GLU A 1 249 ? 46.314 38.040  -5.894  1.00 77.09  ? 257 GLU A OE2 1 
ATOM   2025 N  N   . THR A 1 250 ? 42.970 34.143  -10.627 1.00 53.55  ? 258 THR A N   1 
ATOM   2026 C  CA  . THR A 1 250 ? 42.972 33.014  -11.547 1.00 56.36  ? 258 THR A CA  1 
ATOM   2027 C  C   . THR A 1 250 ? 41.749 33.069  -12.459 1.00 50.71  ? 258 THR A C   1 
ATOM   2028 O  O   . THR A 1 250 ? 41.501 32.139  -13.221 1.00 56.67  ? 258 THR A O   1 
ATOM   2029 C  CB  . THR A 1 250 ? 43.002 31.674  -10.800 1.00 58.71  ? 258 THR A CB  1 
ATOM   2030 O  OG1 . THR A 1 250 ? 41.776 31.534  -10.082 1.00 52.84  ? 258 THR A OG1 1 
ATOM   2031 C  CG2 . THR A 1 250 ? 44.178 31.550  -9.856  1.00 60.96  ? 258 THR A CG2 1 
ATOM   2032 N  N   . LYS A 1 251 ? 40.989 34.165  -12.370 1.00 52.68  ? 259 LYS A N   1 
ATOM   2033 C  CA  . LYS A 1 251 ? 39.762 34.320  -13.134 1.00 56.88  ? 259 LYS A CA  1 
ATOM   2034 C  C   . LYS A 1 251 ? 38.988 33.004  -13.093 1.00 52.93  ? 259 LYS A C   1 
ATOM   2035 O  O   . LYS A 1 251 ? 38.692 32.417  -14.131 1.00 51.96  ? 259 LYS A O   1 
ATOM   2036 C  CB  . LYS A 1 251 ? 40.075 34.766  -14.567 1.00 65.66  ? 259 LYS A CB  1 
ATOM   2037 C  CG  . LYS A 1 251 ? 41.026 35.952  -14.666 1.00 78.57  ? 259 LYS A CG  1 
ATOM   2038 C  CD  . LYS A 1 251 ? 42.400 35.615  -15.212 1.00 102.82 ? 259 LYS A CD  1 
ATOM   2039 C  CE  . LYS A 1 251 ? 42.669 36.274  -16.549 1.00 118.10 ? 259 LYS A CE  1 
ATOM   2040 N  NZ  . LYS A 1 251 ? 42.315 37.714  -16.520 1.00 122.39 ? 259 LYS A NZ  1 
ATOM   2041 N  N   . SER A 1 252 ? 38.664 32.551  -11.877 1.00 49.73  ? 260 SER A N   1 
ATOM   2042 C  CA  . SER A 1 252 ? 38.025 31.259  -11.687 1.00 53.81  ? 260 SER A CA  1 
ATOM   2043 C  C   . SER A 1 252 ? 36.631 31.442  -11.096 1.00 46.14  ? 260 SER A C   1 
ATOM   2044 O  O   . SER A 1 252 ? 36.396 32.361  -10.315 1.00 45.22  ? 260 SER A O   1 
ATOM   2045 C  CB  . SER A 1 252 ? 38.866 30.354  -10.816 1.00 45.96  ? 260 SER A CB  1 
ATOM   2046 O  OG  . SER A 1 252 ? 40.104 30.046  -11.440 1.00 56.08  ? 260 SER A OG  1 
ATOM   2047 N  N   . GLN A 1 253 ? 35.711 30.559  -11.494 1.00 51.20  ? 261 GLN A N   1 
ATOM   2048 C  CA  . GLN A 1 253 ? 34.405 30.472  -10.864 1.00 51.84  ? 261 GLN A CA  1 
ATOM   2049 C  C   . GLN A 1 253 ? 34.558 29.899  -9.460  1.00 50.79  ? 261 GLN A C   1 
ATOM   2050 O  O   . GLN A 1 253 ? 35.475 29.122  -9.201  1.00 50.24  ? 261 GLN A O   1 
ATOM   2051 C  CB  . GLN A 1 253 ? 33.477 29.546  -11.647 1.00 60.37  ? 261 GLN A CB  1 
ATOM   2052 C  CG  . GLN A 1 253 ? 32.991 30.112  -12.968 1.00 65.77  ? 261 GLN A CG  1 
ATOM   2053 C  CD  . GLN A 1 253 ? 32.317 29.024  -13.767 1.00 67.56  ? 261 GLN A CD  1 
ATOM   2054 O  OE1 . GLN A 1 253 ? 31.317 28.448  -13.345 1.00 60.23  ? 261 GLN A OE1 1 
ATOM   2055 N  NE2 . GLN A 1 253 ? 32.887 28.711  -14.918 1.00 61.08  ? 261 GLN A NE2 1 
ATOM   2056 N  N   . VAL A 1 254 ? 33.631 30.269  -8.570  1.00 45.51  ? 262 VAL A N   1 
ATOM   2057 C  CA  . VAL A 1 254 ? 33.579 29.687  -7.241  1.00 46.62  ? 262 VAL A CA  1 
ATOM   2058 C  C   . VAL A 1 254 ? 32.290 28.885  -7.107  1.00 47.04  ? 262 VAL A C   1 
ATOM   2059 O  O   . VAL A 1 254 ? 31.198 29.444  -7.167  1.00 47.63  ? 262 VAL A O   1 
ATOM   2060 C  CB  . VAL A 1 254 ? 33.660 30.750  -6.131  1.00 47.56  ? 262 VAL A CB  1 
ATOM   2061 C  CG1 . VAL A 1 254 ? 33.536 30.109  -4.758  1.00 48.26  ? 262 VAL A CG1 1 
ATOM   2062 C  CG2 . VAL A 1 254 ? 34.925 31.589  -6.225  1.00 48.28  ? 262 VAL A CG2 1 
ATOM   2063 N  N   . TRP A 1 255 ? 32.437 27.575  -6.894  1.00 47.53  ? 263 TRP A N   1 
ATOM   2064 C  CA  . TRP A 1 255 ? 31.298 26.700  -6.686  1.00 42.83  ? 263 TRP A CA  1 
ATOM   2065 C  C   . TRP A 1 255 ? 31.092 26.469  -5.191  1.00 45.71  ? 263 TRP A C   1 
ATOM   2066 O  O   . TRP A 1 255 ? 31.910 25.832  -4.532  1.00 48.24  ? 263 TRP A O   1 
ATOM   2067 C  CB  . TRP A 1 255 ? 31.498 25.381  -7.441  1.00 45.03  ? 263 TRP A CB  1 
ATOM   2068 C  CG  . TRP A 1 255 ? 31.420 25.520  -8.939  1.00 42.24  ? 263 TRP A CG  1 
ATOM   2069 C  CD1 . TRP A 1 255 ? 31.400 26.672  -9.669  1.00 49.23  ? 263 TRP A CD1 1 
ATOM   2070 C  CD2 . TRP A 1 255 ? 31.330 24.441  -9.893  1.00 42.31  ? 263 TRP A CD2 1 
ATOM   2071 N  NE1 . TRP A 1 255 ? 31.318 26.387  -11.006 1.00 49.65  ? 263 TRP A NE1 1 
ATOM   2072 C  CE2 . TRP A 1 255 ? 31.271 25.028  -11.174 1.00 45.47  ? 263 TRP A CE2 1 
ATOM   2073 C  CE3 . TRP A 1 255 ? 31.298 23.047  -9.786  1.00 44.97  ? 263 TRP A CE3 1 
ATOM   2074 C  CZ2 . TRP A 1 255 ? 31.180 24.264  -12.335 1.00 49.60  ? 263 TRP A CZ2 1 
ATOM   2075 C  CZ3 . TRP A 1 255 ? 31.206 22.294  -10.934 1.00 49.12  ? 263 TRP A CZ3 1 
ATOM   2076 C  CH2 . TRP A 1 255 ? 31.147 22.896  -12.190 1.00 49.77  ? 263 TRP A CH2 1 
ATOM   2077 N  N   . PHE A 1 256 ? 29.979 27.006  -4.682  1.00 43.29  ? 264 PHE A N   1 
ATOM   2078 C  CA  . PHE A 1 256 ? 29.644 26.956  -3.269  1.00 40.82  ? 264 PHE A CA  1 
ATOM   2079 C  C   . PHE A 1 256 ? 29.194 25.541  -2.916  1.00 40.30  ? 264 PHE A C   1 
ATOM   2080 O  O   . PHE A 1 256 ? 28.901 24.742  -3.802  1.00 42.75  ? 264 PHE A O   1 
ATOM   2081 C  CB  . PHE A 1 256 ? 28.588 28.022  -2.965  1.00 43.05  ? 264 PHE A CB  1 
ATOM   2082 C  CG  . PHE A 1 256 ? 28.958 29.408  -3.437  1.00 48.49  ? 264 PHE A CG  1 
ATOM   2083 C  CD1 . PHE A 1 256 ? 30.148 29.995  -3.039  1.00 46.44  ? 264 PHE A CD1 1 
ATOM   2084 C  CD2 . PHE A 1 256 ? 28.126 30.122  -4.286  1.00 54.10  ? 264 PHE A CD2 1 
ATOM   2085 C  CE1 . PHE A 1 256 ? 30.495 31.266  -3.472  1.00 50.98  ? 264 PHE A CE1 1 
ATOM   2086 C  CE2 . PHE A 1 256 ? 28.474 31.393  -4.719  1.00 57.14  ? 264 PHE A CE2 1 
ATOM   2087 C  CZ  . PHE A 1 256 ? 29.658 31.962  -4.312  1.00 56.03  ? 264 PHE A CZ  1 
ATOM   2088 N  N   . GLY A 1 257 ? 29.152 25.236  -1.615  1.00 45.68  ? 265 GLY A N   1 
ATOM   2089 C  CA  . GLY A 1 257 ? 28.893 23.882  -1.155  1.00 48.08  ? 265 GLY A CA  1 
ATOM   2090 C  C   . GLY A 1 257 ? 27.423 23.490  -1.280  1.00 51.87  ? 265 GLY A C   1 
ATOM   2091 O  O   . GLY A 1 257 ? 27.113 22.345  -1.604  1.00 54.11  ? 265 GLY A O   1 
ATOM   2092 N  N   . HIS A 1 258 ? 26.527 24.452  -1.025  1.00 45.33  ? 266 HIS A N   1 
ATOM   2093 C  CA  . HIS A 1 258 ? 25.117 24.153  -0.833  1.00 49.36  ? 266 HIS A CA  1 
ATOM   2094 C  C   . HIS A 1 258 ? 24.242 25.334  -1.251  1.00 48.28  ? 266 HIS A C   1 
ATOM   2095 O  O   . HIS A 1 258 ? 23.375 25.756  -0.489  1.00 53.84  ? 266 HIS A O   1 
ATOM   2096 C  CB  . HIS A 1 258 ? 24.838 23.847  0.643   1.00 50.02  ? 266 HIS A CB  1 
ATOM   2097 C  CG  . HIS A 1 258 ? 25.602 22.697  1.216   1.00 52.48  ? 266 HIS A CG  1 
ATOM   2098 N  ND1 . HIS A 1 258 ? 25.613 21.436  0.660   1.00 47.32  ? 266 HIS A ND1 1 
ATOM   2099 C  CD2 . HIS A 1 258 ? 26.370 22.623  2.313   1.00 50.29  ? 266 HIS A CD2 1 
ATOM   2100 C  CE1 . HIS A 1 258 ? 26.369 20.638  1.402   1.00 47.67  ? 266 HIS A CE1 1 
ATOM   2101 N  NE2 . HIS A 1 258 ? 26.840 21.339  2.411   1.00 45.72  ? 266 HIS A NE2 1 
ATOM   2102 N  N   . ASP A 1 259 ? 24.467 25.862  -2.460  1.00 47.62  ? 267 ASP A N   1 
ATOM   2103 C  CA  . ASP A 1 259 ? 23.714 27.007  -2.951  1.00 55.99  ? 267 ASP A CA  1 
ATOM   2104 C  C   . ASP A 1 259 ? 22.661 26.527  -3.947  1.00 55.83  ? 267 ASP A C   1 
ATOM   2105 O  O   . ASP A 1 259 ? 22.988 26.157  -5.072  1.00 54.09  ? 267 ASP A O   1 
ATOM   2106 C  CB  . ASP A 1 259 ? 24.639 28.048  -3.588  1.00 56.21  ? 267 ASP A CB  1 
ATOM   2107 C  CG  . ASP A 1 259 ? 23.959 29.367  -3.916  1.00 55.64  ? 267 ASP A CG  1 
ATOM   2108 O  OD1 . ASP A 1 259 ? 22.849 29.331  -4.483  1.00 64.96  ? 267 ASP A OD1 1 
ATOM   2109 O  OD2 . ASP A 1 259 ? 24.555 30.422  -3.620  1.00 60.09  ? 267 ASP A OD2 1 
ATOM   2110 N  N   . ALA A 1 260 ? 21.395 26.547  -3.513  1.00 55.38  ? 268 ALA A N   1 
ATOM   2111 C  CA  . ALA A 1 260 ? 20.282 26.076  -4.322  1.00 59.13  ? 268 ALA A CA  1 
ATOM   2112 C  C   . ALA A 1 260 ? 20.313 26.723  -5.706  1.00 54.06  ? 268 ALA A C   1 
ATOM   2113 O  O   . ALA A 1 260 ? 20.242 26.022  -6.714  1.00 55.36  ? 268 ALA A O   1 
ATOM   2114 C  CB  . ALA A 1 260 ? 18.979 26.349  -3.608  1.00 58.35  ? 268 ALA A CB  1 
ATOM   2115 N  N   . GLU A 1 261 ? 20.421 28.057  -5.754  1.00 51.65  ? 269 GLU A N   1 
ATOM   2116 C  CA  . GLU A 1 261 ? 20.338 28.779  -7.015  1.00 58.91  ? 269 GLU A CA  1 
ATOM   2117 C  C   . GLU A 1 261 ? 21.456 28.334  -7.955  1.00 62.07  ? 269 GLU A C   1 
ATOM   2118 O  O   . GLU A 1 261 ? 21.198 27.993  -9.107  1.00 68.12  ? 269 GLU A O   1 
ATOM   2119 C  CB  . GLU A 1 261 ? 20.387 30.291  -6.790  1.00 69.83  ? 269 GLU A CB  1 
ATOM   2120 C  CG  . GLU A 1 261 ? 19.073 30.872  -6.296  1.00 90.65  ? 269 GLU A CG  1 
ATOM   2121 C  CD  . GLU A 1 261 ? 18.998 32.390  -6.324  1.00 111.36 ? 269 GLU A CD  1 
ATOM   2122 O  OE1 . GLU A 1 261 ? 19.979 33.022  -6.763  1.00 116.33 ? 269 GLU A OE1 1 
ATOM   2123 O  OE2 . GLU A 1 261 ? 17.956 32.936  -5.907  1.00 114.33 ? 269 GLU A OE2 1 
ATOM   2124 N  N   . GLN A 1 262 ? 22.698 28.344  -7.457  1.00 61.08  ? 270 GLN A N   1 
ATOM   2125 C  CA  . GLN A 1 262 ? 23.857 28.049  -8.283  1.00 52.03  ? 270 GLN A CA  1 
ATOM   2126 C  C   . GLN A 1 262 ? 23.752 26.626  -8.828  1.00 48.21  ? 270 GLN A C   1 
ATOM   2127 O  O   . GLN A 1 262 ? 24.142 26.369  -9.965  1.00 52.06  ? 270 GLN A O   1 
ATOM   2128 C  CB  . GLN A 1 262 ? 25.145 28.248  -7.481  1.00 47.25  ? 270 GLN A CB  1 
ATOM   2129 C  CG  . GLN A 1 262 ? 26.414 28.180  -8.320  1.00 46.43  ? 270 GLN A CG  1 
ATOM   2130 C  CD  . GLN A 1 262 ? 27.656 28.144  -7.462  1.00 54.57  ? 270 GLN A CD  1 
ATOM   2131 O  OE1 . GLN A 1 262 ? 27.762 27.361  -6.519  1.00 52.71  ? 270 GLN A OE1 1 
ATOM   2132 N  NE2 . GLN A 1 262 ? 28.610 29.005  -7.776  1.00 50.67  ? 270 GLN A NE2 1 
ATOM   2133 N  N   . PHE A 1 263 ? 23.216 25.708  -8.013  1.00 43.74  ? 271 PHE A N   1 
ATOM   2134 C  CA  . PHE A 1 263 ? 23.162 24.300  -8.375  1.00 50.09  ? 271 PHE A CA  1 
ATOM   2135 C  C   . PHE A 1 263 ? 22.166 24.089  -9.513  1.00 57.33  ? 271 PHE A C   1 
ATOM   2136 O  O   . PHE A 1 263 ? 22.398 23.260  -10.391 1.00 58.30  ? 271 PHE A O   1 
ATOM   2137 C  CB  . PHE A 1 263 ? 22.799 23.435  -7.165  1.00 46.73  ? 271 PHE A CB  1 
ATOM   2138 C  CG  . PHE A 1 263 ? 22.855 21.948  -7.414  1.00 50.16  ? 271 PHE A CG  1 
ATOM   2139 C  CD1 . PHE A 1 263 ? 24.069 21.297  -7.569  1.00 52.86  ? 271 PHE A CD1 1 
ATOM   2140 C  CD2 . PHE A 1 263 ? 21.691 21.200  -7.505  1.00 50.28  ? 271 PHE A CD2 1 
ATOM   2141 C  CE1 . PHE A 1 263 ? 24.117 19.930  -7.800  1.00 57.84  ? 271 PHE A CE1 1 
ATOM   2142 C  CE2 . PHE A 1 263 ? 21.741 19.834  -7.736  1.00 54.96  ? 271 PHE A CE2 1 
ATOM   2143 C  CZ  . PHE A 1 263 ? 22.953 19.202  -7.883  1.00 61.13  ? 271 PHE A CZ  1 
ATOM   2144 N  N   . LYS A 1 264 ? 21.055 24.835  -9.487  1.00 62.98  ? 272 LYS A N   1 
ATOM   2145 C  CA  . LYS A 1 264 ? 20.062 24.758  -10.547 1.00 67.79  ? 272 LYS A CA  1 
ATOM   2146 C  C   . LYS A 1 264 ? 20.725 25.056  -11.889 1.00 59.85  ? 272 LYS A C   1 
ATOM   2147 O  O   . LYS A 1 264 ? 20.399 24.431  -12.895 1.00 58.33  ? 272 LYS A O   1 
ATOM   2148 C  CB  . LYS A 1 264 ? 18.910 25.742  -10.313 1.00 76.29  ? 272 LYS A CB  1 
ATOM   2149 C  CG  . LYS A 1 264 ? 17.917 25.355  -9.224  1.00 96.30  ? 272 LYS A CG  1 
ATOM   2150 C  CD  . LYS A 1 264 ? 16.881 26.432  -8.982  1.00 110.95 ? 272 LYS A CD  1 
ATOM   2151 C  CE  . LYS A 1 264 ? 16.730 26.783  -7.517  1.00 121.47 ? 272 LYS A CE  1 
ATOM   2152 N  NZ  . LYS A 1 264 ? 16.411 28.219  -7.334  1.00 110.15 ? 272 LYS A NZ  1 
ATOM   2153 N  N   . LYS A 1 265 ? 21.659 26.015  -11.891 1.00 48.68  ? 273 LYS A N   1 
ATOM   2154 C  CA  . LYS A 1 265 ? 22.266 26.487  -13.125 1.00 55.29  ? 273 LYS A CA  1 
ATOM   2155 C  C   . LYS A 1 265 ? 23.380 25.539  -13.573 1.00 55.66  ? 273 LYS A C   1 
ATOM   2156 O  O   . LYS A 1 265 ? 23.828 25.616  -14.714 1.00 64.66  ? 273 LYS A O   1 
ATOM   2157 C  CB  . LYS A 1 265 ? 22.813 27.907  -12.951 1.00 64.57  ? 273 LYS A CB  1 
ATOM   2158 C  CG  . LYS A 1 265 ? 21.867 28.897  -12.282 1.00 78.39  ? 273 LYS A CG  1 
ATOM   2159 C  CD  . LYS A 1 265 ? 22.540 30.207  -11.932 1.00 91.71  ? 273 LYS A CD  1 
ATOM   2160 C  CE  . LYS A 1 265 ? 21.876 30.923  -10.774 1.00 113.30 ? 273 LYS A CE  1 
ATOM   2161 N  NZ  . LYS A 1 265 ? 22.878 31.403  -9.792  1.00 111.26 ? 273 LYS A NZ  1 
ATOM   2162 N  N   . PHE A 1 266 ? 23.829 24.648  -12.680 1.00 49.84  ? 274 PHE A N   1 
ATOM   2163 C  CA  . PHE A 1 266 ? 24.882 23.701  -13.022 1.00 50.75  ? 274 PHE A CA  1 
ATOM   2164 C  C   . PHE A 1 266 ? 24.351 22.691  -14.036 1.00 54.46  ? 274 PHE A C   1 
ATOM   2165 O  O   . PHE A 1 266 ? 23.190 22.294  -13.972 1.00 58.03  ? 274 PHE A O   1 
ATOM   2166 C  CB  . PHE A 1 266 ? 25.388 22.945  -11.789 1.00 49.31  ? 274 PHE A CB  1 
ATOM   2167 C  CG  . PHE A 1 266 ? 26.310 23.705  -10.867 1.00 52.36  ? 274 PHE A CG  1 
ATOM   2168 C  CD1 . PHE A 1 266 ? 27.014 24.818  -11.302 1.00 58.34  ? 274 PHE A CD1 1 
ATOM   2169 C  CD2 . PHE A 1 266 ? 26.467 23.304  -9.550  1.00 52.57  ? 274 PHE A CD2 1 
ATOM   2170 C  CE1 . PHE A 1 266 ? 27.859 25.504  -10.442 1.00 55.75  ? 274 PHE A CE1 1 
ATOM   2171 C  CE2 . PHE A 1 266 ? 27.309 23.993  -8.691  1.00 58.06  ? 274 PHE A CE2 1 
ATOM   2172 C  CZ  . PHE A 1 266 ? 28.003 25.092  -9.138  1.00 54.88  ? 274 PHE A CZ  1 
ATOM   2173 N  N   . ARG A 1 267 ? 25.213 22.273  -14.967 1.00 49.03  ? 275 ARG A N   1 
ATOM   2174 C  CA  . ARG A 1 267 ? 24.899 21.153  -15.838 1.00 51.78  ? 275 ARG A CA  1 
ATOM   2175 C  C   . ARG A 1 267 ? 25.269 19.864  -15.111 1.00 47.21  ? 275 ARG A C   1 
ATOM   2176 O  O   . ARG A 1 267 ? 26.443 19.615  -14.850 1.00 54.30  ? 275 ARG A O   1 
ATOM   2177 C  CB  . ARG A 1 267 ? 25.657 21.273  -17.164 1.00 58.10  ? 275 ARG A CB  1 
ATOM   2178 C  CG  . ARG A 1 267 ? 25.524 20.060  -18.074 1.00 65.68  ? 275 ARG A CG  1 
ATOM   2179 C  CD  . ARG A 1 267 ? 26.508 20.121  -19.227 1.00 71.06  ? 275 ARG A CD  1 
ATOM   2180 N  NE  . ARG A 1 267 ? 26.469 21.430  -19.861 1.00 70.04  ? 275 ARG A NE  1 
ATOM   2181 C  CZ  . ARG A 1 267 ? 27.502 22.260  -19.955 1.00 66.47  ? 275 ARG A CZ  1 
ATOM   2182 N  NH1 . ARG A 1 267 ? 27.308 23.513  -20.330 1.00 78.66  ? 275 ARG A NH1 1 
ATOM   2183 N  NH2 . ARG A 1 267 ? 28.716 21.855  -19.622 1.00 64.56  ? 275 ARG A NH2 1 
ATOM   2184 N  N   . LYS A 1 268 ? 24.261 19.048  -14.782 1.00 45.96  ? 276 LYS A N   1 
ATOM   2185 C  CA  . LYS A 1 268 ? 24.497 17.845  -14.002 1.00 44.67  ? 276 LYS A CA  1 
ATOM   2186 C  C   . LYS A 1 268 ? 24.833 16.676  -14.920 1.00 43.84  ? 276 LYS A C   1 
ATOM   2187 O  O   . LYS A 1 268 ? 24.810 16.802  -16.142 1.00 39.83  ? 276 LYS A O   1 
ATOM   2188 C  CB  . LYS A 1 268 ? 23.273 17.439  -13.178 1.00 50.73  ? 276 LYS A CB  1 
ATOM   2189 C  CG  . LYS A 1 268 ? 22.339 18.570  -12.780 1.00 61.71  ? 276 LYS A CG  1 
ATOM   2190 C  CD  . LYS A 1 268 ? 22.944 19.562  -11.823 1.00 57.96  ? 276 LYS A CD  1 
ATOM   2191 C  CE  . LYS A 1 268 ? 21.888 20.465  -11.224 1.00 63.08  ? 276 LYS A CE  1 
ATOM   2192 N  NZ  . LYS A 1 268 ? 21.287 21.349  -12.250 1.00 62.20  ? 276 LYS A NZ  1 
ATOM   2193 N  N   . SER A 1 269 ? 25.078 15.523  -14.287 1.00 46.35  ? 277 SER A N   1 
ATOM   2194 C  CA  . SER A 1 269 ? 25.623 14.346  -14.940 1.00 45.70  ? 277 SER A CA  1 
ATOM   2195 C  C   . SER A 1 269 ? 24.586 13.678  -15.839 1.00 51.31  ? 277 SER A C   1 
ATOM   2196 O  O   . SER A 1 269 ? 24.927 12.791  -16.619 1.00 57.24  ? 277 SER A O   1 
ATOM   2197 C  CB  . SER A 1 269 ? 26.143 13.378  -13.911 1.00 44.04  ? 277 SER A CB  1 
ATOM   2198 O  OG  . SER A 1 269 ? 25.118 13.017  -12.997 1.00 46.57  ? 277 SER A OG  1 
ATOM   2199 N  N   . THR A 1 270 ? 23.320 14.088  -15.711 1.00 48.55  ? 278 THR A N   1 
ATOM   2200 C  CA  . THR A 1 270 ? 22.265 13.550  -16.556 1.00 55.54  ? 278 THR A CA  1 
ATOM   2201 C  C   . THR A 1 270 ? 22.184 14.340  -17.861 1.00 54.15  ? 278 THR A C   1 
ATOM   2202 O  O   . THR A 1 270 ? 21.531 13.896  -18.802 1.00 59.50  ? 278 THR A O   1 
ATOM   2203 C  CB  . THR A 1 270 ? 20.906 13.537  -15.843 1.00 49.80  ? 278 THR A CB  1 
ATOM   2204 O  OG1 . THR A 1 270 ? 20.738 14.790  -15.178 1.00 53.01  ? 278 THR A OG1 1 
ATOM   2205 C  CG2 . THR A 1 270 ? 20.765 12.412  -14.841 1.00 47.17  ? 278 THR A CG2 1 
ATOM   2206 N  N   . GLU A 1 271 ? 22.842 15.506  -17.918 1.00 59.75  ? 279 GLU A N   1 
ATOM   2207 C  CA  . GLU A 1 271 ? 22.809 16.327  -19.120 1.00 55.90  ? 279 GLU A CA  1 
ATOM   2208 C  C   . GLU A 1 271 ? 24.186 16.408  -19.776 1.00 52.92  ? 279 GLU A C   1 
ATOM   2209 O  O   . GLU A 1 271 ? 24.270 16.632  -20.981 1.00 53.36  ? 279 GLU A O   1 
ATOM   2210 C  CB  . GLU A 1 271 ? 22.344 17.762  -18.855 1.00 66.30  ? 279 GLU A CB  1 
ATOM   2211 C  CG  . GLU A 1 271 ? 20.905 17.891  -18.389 1.00 71.55  ? 279 GLU A CG  1 
ATOM   2212 C  CD  . GLU A 1 271 ? 20.750 18.104  -16.893 1.00 94.03  ? 279 GLU A CD  1 
ATOM   2213 O  OE1 . GLU A 1 271 ? 20.121 17.248  -16.238 1.00 108.41 ? 279 GLU A OE1 1 
ATOM   2214 O  OE2 . GLU A 1 271 ? 21.258 19.129  -16.386 1.00 65.19  ? 279 GLU A OE2 1 
ATOM   2215 N  N   . GLY A 1 272 ? 25.263 16.274  -18.993 1.00 49.18  ? 280 GLY A N   1 
ATOM   2216 C  CA  . GLY A 1 272 ? 26.597 16.373  -19.565 1.00 54.19  ? 280 GLY A CA  1 
ATOM   2217 C  C   . GLY A 1 272 ? 27.678 16.701  -18.538 1.00 52.00  ? 280 GLY A C   1 
ATOM   2218 O  O   . GLY A 1 272 ? 27.607 16.272  -17.388 1.00 50.68  ? 280 GLY A O   1 
ATOM   2219 N  N   . TYR A 1 273 ? 28.681 17.468  -18.983 1.00 49.06  ? 281 TYR A N   1 
ATOM   2220 C  CA  . TYR A 1 273 ? 29.907 17.671  -18.230 1.00 50.76  ? 281 TYR A CA  1 
ATOM   2221 C  C   . TYR A 1 273 ? 30.550 19.001  -18.608 1.00 45.73  ? 281 TYR A C   1 
ATOM   2222 O  O   . TYR A 1 273 ? 30.023 19.743  -19.431 1.00 47.64  ? 281 TYR A O   1 
ATOM   2223 C  CB  . TYR A 1 273 ? 30.848 16.504  -18.541 1.00 46.68  ? 281 TYR A CB  1 
ATOM   2224 C  CG  . TYR A 1 273 ? 30.766 16.040  -19.989 1.00 51.92  ? 281 TYR A CG  1 
ATOM   2225 C  CD1 . TYR A 1 273 ? 31.250 16.823  -21.031 1.00 58.03  ? 281 TYR A CD1 1 
ATOM   2226 C  CD2 . TYR A 1 273 ? 30.167 14.829  -20.314 1.00 56.52  ? 281 TYR A CD2 1 
ATOM   2227 C  CE1 . TYR A 1 273 ? 31.166 16.402  -22.349 1.00 56.50  ? 281 TYR A CE1 1 
ATOM   2228 C  CE2 . TYR A 1 273 ? 30.075 14.399  -21.626 1.00 61.11  ? 281 TYR A CE2 1 
ATOM   2229 C  CZ  . TYR A 1 273 ? 30.576 15.187  -22.647 1.00 57.76  ? 281 TYR A CZ  1 
ATOM   2230 O  OH  . TYR A 1 273 ? 30.483 14.760  -23.940 1.00 56.58  ? 281 TYR A OH  1 
ATOM   2231 N  N   . TYR A 1 274 ? 31.709 19.273  -17.998 1.00 54.06  ? 282 TYR A N   1 
ATOM   2232 C  CA  . TYR A 1 274 ? 32.481 20.473  -18.274 1.00 46.72  ? 282 TYR A CA  1 
ATOM   2233 C  C   . TYR A 1 274 ? 33.864 20.053  -18.765 1.00 48.12  ? 282 TYR A C   1 
ATOM   2234 O  O   . TYR A 1 274 ? 34.488 19.174  -18.175 1.00 53.87  ? 282 TYR A O   1 
ATOM   2235 C  CB  . TYR A 1 274 ? 32.578 21.354  -17.023 1.00 47.54  ? 282 TYR A CB  1 
ATOM   2236 C  CG  . TYR A 1 274 ? 31.270 21.958  -16.528 1.00 47.84  ? 282 TYR A CG  1 
ATOM   2237 C  CD1 . TYR A 1 274 ? 30.407 21.247  -15.701 1.00 48.82  ? 282 TYR A CD1 1 
ATOM   2238 C  CD2 . TYR A 1 274 ? 30.897 23.247  -16.892 1.00 50.80  ? 282 TYR A CD2 1 
ATOM   2239 C  CE1 . TYR A 1 274 ? 29.222 21.802  -15.245 1.00 51.16  ? 282 TYR A CE1 1 
ATOM   2240 C  CE2 . TYR A 1 274 ? 29.713 23.811  -16.448 1.00 50.40  ? 282 TYR A CE2 1 
ATOM   2241 C  CZ  . TYR A 1 274 ? 28.872 23.087  -15.622 1.00 52.66  ? 282 TYR A CZ  1 
ATOM   2242 O  OH  . TYR A 1 274 ? 27.705 23.646  -15.189 1.00 50.77  ? 282 TYR A OH  1 
ATOM   2243 N  N   . GLU A 1 275 ? 34.334 20.688  -19.845 1.00 48.62  ? 283 GLU A N   1 
ATOM   2244 C  CA  . GLU A 1 275 ? 35.613 20.345  -20.447 1.00 59.74  ? 283 GLU A CA  1 
ATOM   2245 C  C   . GLU A 1 275 ? 36.568 21.543  -20.365 1.00 46.69  ? 283 GLU A C   1 
ATOM   2246 O  O   . GLU A 1 275 ? 36.060 22.662  -20.156 1.00 51.88  ? 283 GLU A O   1 
ATOM   2247 C  CB  . GLU A 1 275 ? 35.425 19.910  -21.902 1.00 61.10  ? 283 GLU A CB  1 
ATOM   2248 C  CG  . GLU A 1 275 ? 34.844 18.517  -22.055 1.00 66.82  ? 283 GLU A CG  1 
ATOM   2249 C  CD  . GLU A 1 275 ? 34.806 18.012  -23.488 1.00 69.54  ? 283 GLU A CD  1 
ATOM   2250 O  OE1 . GLU A 1 275 ? 35.269 18.747  -24.384 1.00 54.46  ? 283 GLU A OE1 1 
ATOM   2251 O  OE2 . GLU A 1 275 ? 34.316 16.885  -23.706 1.00 62.66  ? 283 GLU A OE2 1 
ATOM   2252 N  N   . ARG B 1 1   ? 49.296 12.598  54.426  1.00 97.85  ? 9   ARG B N   1 
ATOM   2253 C  CA  . ARG B 1 1   ? 48.107 12.701  53.538  1.00 101.38 ? 9   ARG B CA  1 
ATOM   2254 C  C   . ARG B 1 1   ? 48.133 11.533  52.547  1.00 86.23  ? 9   ARG B C   1 
ATOM   2255 O  O   . ARG B 1 1   ? 47.468 10.526  52.780  1.00 72.28  ? 9   ARG B O   1 
ATOM   2256 C  CB  . ARG B 1 1   ? 48.061 14.097  52.900  1.00 105.42 ? 9   ARG B CB  1 
ATOM   2257 C  CG  . ARG B 1 1   ? 46.654 14.609  52.616  1.00 111.78 ? 9   ARG B CG  1 
ATOM   2258 C  CD  . ARG B 1 1   ? 46.603 16.069  52.201  1.00 106.17 ? 9   ARG B CD  1 
ATOM   2259 N  NE  . ARG B 1 1   ? 47.408 16.941  53.048  1.00 109.62 ? 9   ARG B NE  1 
ATOM   2260 C  CZ  . ARG B 1 1   ? 47.157 18.228  53.261  1.00 112.26 ? 9   ARG B CZ  1 
ATOM   2261 N  NH1 . ARG B 1 1   ? 48.078 18.998  53.815  1.00 104.96 ? 9   ARG B NH1 1 
ATOM   2262 N  NH2 . ARG B 1 1   ? 46.007 18.753  52.873  1.00 116.43 ? 9   ARG B NH2 1 
ATOM   2263 N  N   . PRO B 1 2   ? 48.905 11.584  51.434  1.00 79.45  ? 10  PRO B N   1 
ATOM   2264 C  CA  . PRO B 1 2   ? 48.835 10.549  50.403  1.00 67.59  ? 10  PRO B CA  1 
ATOM   2265 C  C   . PRO B 1 2   ? 49.905 9.458   50.481  1.00 51.14  ? 10  PRO B C   1 
ATOM   2266 O  O   . PRO B 1 2   ? 50.924 9.624   51.147  1.00 52.42  ? 10  PRO B O   1 
ATOM   2267 C  CB  . PRO B 1 2   ? 49.025 11.389  49.131  1.00 74.24  ? 10  PRO B CB  1 
ATOM   2268 C  CG  . PRO B 1 2   ? 49.900 12.571  49.555  1.00 84.39  ? 10  PRO B CG  1 
ATOM   2269 C  CD  . PRO B 1 2   ? 49.867 12.635  51.072  1.00 93.09  ? 10  PRO B CD  1 
ATOM   2270 N  N   . LYS B 1 3   ? 49.659 8.341   49.782  1.00 51.31  ? 11  LYS B N   1 
ATOM   2271 C  CA  . LYS B 1 3   ? 50.610 7.242   49.691  1.00 53.13  ? 11  LYS B CA  1 
ATOM   2272 C  C   . LYS B 1 3   ? 50.892 6.924   48.224  1.00 46.96  ? 11  LYS B C   1 
ATOM   2273 O  O   . LYS B 1 3   ? 49.966 6.721   47.445  1.00 48.07  ? 11  LYS B O   1 
ATOM   2274 C  CB  . LYS B 1 3   ? 50.069 5.991   50.391  1.00 57.23  ? 11  LYS B CB  1 
ATOM   2275 C  CG  . LYS B 1 3   ? 50.261 5.947   51.901  1.00 55.62  ? 11  LYS B CG  1 
ATOM   2276 C  CD  . LYS B 1 3   ? 49.681 4.702   52.539  1.00 64.58  ? 11  LYS B CD  1 
ATOM   2277 C  CE  . LYS B 1 3   ? 49.597 4.795   54.047  1.00 60.36  ? 11  LYS B CE  1 
ATOM   2278 N  NZ  . LYS B 1 3   ? 49.213 6.156   54.491  1.00 64.84  ? 11  LYS B NZ  1 
ATOM   2279 N  N   . LEU B 1 4   ? 52.181 6.858   47.867  1.00 51.59  ? 12  LEU B N   1 
ATOM   2280 C  CA  . LEU B 1 4   ? 52.589 6.604   46.494  1.00 50.64  ? 12  LEU B CA  1 
ATOM   2281 C  C   . LEU B 1 4   ? 53.213 5.214   46.394  1.00 43.91  ? 12  LEU B C   1 
ATOM   2282 O  O   . LEU B 1 4   ? 54.158 4.902   47.115  1.00 45.05  ? 12  LEU B O   1 
ATOM   2283 C  CB  . LEU B 1 4   ? 53.569 7.699   46.055  1.00 51.54  ? 12  LEU B CB  1 
ATOM   2284 C  CG  . LEU B 1 4   ? 54.002 7.663   44.589  1.00 52.67  ? 12  LEU B CG  1 
ATOM   2285 C  CD1 . LEU B 1 4   ? 54.176 9.073   44.045  1.00 54.22  ? 12  LEU B CD1 1 
ATOM   2286 C  CD2 . LEU B 1 4   ? 55.295 6.880   44.418  1.00 52.62  ? 12  LEU B CD2 1 
ATOM   2287 N  N   . TYR B 1 5   ? 52.669 4.395   45.484  1.00 45.47  ? 13  TYR B N   1 
ATOM   2288 C  CA  . TYR B 1 5   ? 53.095 3.015   45.317  1.00 45.51  ? 13  TYR B CA  1 
ATOM   2289 C  C   . TYR B 1 5   ? 53.753 2.835   43.950  1.00 48.81  ? 13  TYR B C   1 
ATOM   2290 O  O   . TYR B 1 5   ? 53.217 3.270   42.934  1.00 47.44  ? 13  TYR B O   1 
ATOM   2291 C  CB  . TYR B 1 5   ? 51.932 2.021   45.409  1.00 48.62  ? 13  TYR B CB  1 
ATOM   2292 C  CG  . TYR B 1 5   ? 51.155 2.007   46.719  1.00 54.43  ? 13  TYR B CG  1 
ATOM   2293 C  CD1 . TYR B 1 5   ? 50.200 2.977   47.000  1.00 54.66  ? 13  TYR B CD1 1 
ATOM   2294 C  CD2 . TYR B 1 5   ? 51.371 1.016   47.669  1.00 53.90  ? 13  TYR B CD2 1 
ATOM   2295 C  CE1 . TYR B 1 5   ? 49.485 2.962   48.186  1.00 55.42  ? 13  TYR B CE1 1 
ATOM   2296 C  CE2 . TYR B 1 5   ? 50.664 0.991   48.860  1.00 52.26  ? 13  TYR B CE2 1 
ATOM   2297 C  CZ  . TYR B 1 5   ? 49.719 1.968   49.119  1.00 53.20  ? 13  TYR B CZ  1 
ATOM   2298 O  OH  . TYR B 1 5   ? 49.017 1.956   50.290  1.00 59.77  ? 13  TYR B OH  1 
ATOM   2299 N  N   . VAL B 1 6   ? 54.916 2.175   43.953  1.00 46.29  ? 14  VAL B N   1 
ATOM   2300 C  CA  . VAL B 1 6   ? 55.571 1.720   42.739  1.00 45.04  ? 14  VAL B CA  1 
ATOM   2301 C  C   . VAL B 1 6   ? 55.231 0.246   42.536  1.00 50.01  ? 14  VAL B C   1 
ATOM   2302 O  O   . VAL B 1 6   ? 55.587 -0.594  43.359  1.00 51.67  ? 14  VAL B O   1 
ATOM   2303 C  CB  . VAL B 1 6   ? 57.094 1.931   42.821  1.00 44.12  ? 14  VAL B CB  1 
ATOM   2304 C  CG1 . VAL B 1 6   ? 57.809 1.360   41.606  1.00 44.73  ? 14  VAL B CG1 1 
ATOM   2305 C  CG2 . VAL B 1 6   ? 57.452 3.395   43.018  1.00 53.50  ? 14  VAL B CG2 1 
ATOM   2306 N  N   . MET B 1 7   ? 54.551 -0.056  41.427  1.00 50.42  ? 15  MET B N   1 
ATOM   2307 C  CA  . MET B 1 7   ? 54.088 -1.404  41.150  1.00 47.84  ? 15  MET B CA  1 
ATOM   2308 C  C   . MET B 1 7   ? 54.915 -1.997  40.011  1.00 55.90  ? 15  MET B C   1 
ATOM   2309 O  O   . MET B 1 7   ? 55.038 -1.399  38.945  1.00 55.07  ? 15  MET B O   1 
ATOM   2310 C  CB  . MET B 1 7   ? 52.604 -1.387  40.772  1.00 50.15  ? 15  MET B CB  1 
ATOM   2311 C  CG  . MET B 1 7   ? 51.706 -0.958  41.920  1.00 51.13  ? 15  MET B CG  1 
ATOM   2312 S  SD  . MET B 1 7   ? 49.955 -0.864  41.466  1.00 53.64  ? 15  MET B SD  1 
ATOM   2313 C  CE  . MET B 1 7   ? 49.937 0.658   40.518  1.00 59.37  ? 15  MET B CE  1 
ATOM   2314 N  N   . ASP B 1 8   ? 55.482 -3.181  40.263  1.00 49.04  ? 16  ASP B N   1 
ATOM   2315 C  CA  . ASP B 1 8   ? 56.372 -3.844  39.324  1.00 53.82  ? 16  ASP B CA  1 
ATOM   2316 C  C   . ASP B 1 8   ? 55.535 -4.633  38.319  1.00 52.09  ? 16  ASP B C   1 
ATOM   2317 O  O   . ASP B 1 8   ? 54.861 -5.592  38.688  1.00 55.34  ? 16  ASP B O   1 
ATOM   2318 C  CB  . ASP B 1 8   ? 57.367 -4.722  40.089  1.00 55.95  ? 16  ASP B CB  1 
ATOM   2319 C  CG  . ASP B 1 8   ? 58.396 -5.422  39.220  1.00 60.35  ? 16  ASP B CG  1 
ATOM   2320 O  OD1 . ASP B 1 8   ? 58.194 -5.464  37.990  1.00 67.10  ? 16  ASP B OD1 1 
ATOM   2321 O  OD2 . ASP B 1 8   ? 59.399 -5.907  39.782  1.00 57.44  ? 16  ASP B OD2 1 
ATOM   2322 N  N   . ASN B 1 9   ? 55.579 -4.216  37.047  1.00 48.79  ? 17  ASN B N   1 
ATOM   2323 C  CA  . ASN B 1 9   ? 54.747 -4.818  36.018  1.00 48.07  ? 17  ASN B CA  1 
ATOM   2324 C  C   . ASN B 1 9   ? 55.606 -5.592  35.022  1.00 48.59  ? 17  ASN B C   1 
ATOM   2325 O  O   . ASN B 1 9   ? 55.200 -5.792  33.879  1.00 57.83  ? 17  ASN B O   1 
ATOM   2326 C  CB  . ASN B 1 9   ? 53.895 -3.775  35.294  1.00 44.61  ? 17  ASN B CB  1 
ATOM   2327 C  CG  . ASN B 1 9   ? 52.991 -3.014  36.238  1.00 47.55  ? 17  ASN B CG  1 
ATOM   2328 O  OD1 . ASN B 1 9   ? 53.109 -1.798  36.374  1.00 54.19  ? 17  ASN B OD1 1 
ATOM   2329 N  ND2 . ASN B 1 9   ? 52.101 -3.727  36.909  1.00 55.22  ? 17  ASN B ND2 1 
ATOM   2330 N  N   . GLY B 1 10  ? 56.789 -6.028  35.462  1.00 47.99  ? 18  GLY B N   1 
ATOM   2331 C  CA  . GLY B 1 10  ? 57.591 -6.954  34.680  1.00 46.16  ? 18  GLY B CA  1 
ATOM   2332 C  C   . GLY B 1 10  ? 58.781 -6.281  34.001  1.00 49.47  ? 18  GLY B C   1 
ATOM   2333 O  O   . GLY B 1 10  ? 59.138 -5.151  34.325  1.00 49.76  ? 18  GLY B O   1 
ATOM   2334 N  N   . ARG B 1 11  ? 59.380 -7.010  33.053  1.00 47.55  ? 19  ARG B N   1 
ATOM   2335 C  CA  . ARG B 1 11  ? 60.589 -6.582  32.371  1.00 57.80  ? 19  ARG B CA  1 
ATOM   2336 C  C   . ARG B 1 11  ? 60.386 -6.707  30.863  1.00 60.77  ? 19  ARG B C   1 
ATOM   2337 O  O   . ARG B 1 11  ? 59.595 -7.526  30.399  1.00 55.93  ? 19  ARG B O   1 
ATOM   2338 C  CB  . ARG B 1 11  ? 61.779 -7.437  32.821  1.00 60.93  ? 19  ARG B CB  1 
ATOM   2339 C  CG  . ARG B 1 11  ? 61.981 -7.490  34.329  1.00 66.77  ? 19  ARG B CG  1 
ATOM   2340 C  CD  . ARG B 1 11  ? 62.680 -6.260  34.877  1.00 81.95  ? 19  ARG B CD  1 
ATOM   2341 N  NE  . ARG B 1 11  ? 62.764 -6.287  36.331  1.00 84.75  ? 19  ARG B NE  1 
ATOM   2342 C  CZ  . ARG B 1 11  ? 61.771 -5.959  37.149  1.00 87.54  ? 19  ARG B CZ  1 
ATOM   2343 N  NH1 . ARG B 1 11  ? 60.649 -5.460  36.661  1.00 86.61  ? 19  ARG B NH1 1 
ATOM   2344 N  NH2 . ARG B 1 11  ? 61.914 -6.102  38.456  1.00 83.26  ? 19  ARG B NH2 1 
ATOM   2345 N  N   . MET B 1 12  ? 61.113 -5.879  30.109  1.00 62.08  ? 20  MET B N   1 
ATOM   2346 C  CA  . MET B 1 12  ? 61.091 -5.935  28.659  1.00 61.40  ? 20  MET B CA  1 
ATOM   2347 C  C   . MET B 1 12  ? 62.531 -5.846  28.160  1.00 53.40  ? 20  MET B C   1 
ATOM   2348 O  O   . MET B 1 12  ? 63.374 -5.227  28.806  1.00 59.71  ? 20  MET B O   1 
ATOM   2349 C  CB  . MET B 1 12  ? 60.257 -4.779  28.095  1.00 62.88  ? 20  MET B CB  1 
ATOM   2350 C  CG  . MET B 1 12  ? 60.146 -4.766  26.584  1.00 76.59  ? 20  MET B CG  1 
ATOM   2351 S  SD  . MET B 1 12  ? 58.768 -3.728  26.025  1.00 79.97  ? 20  MET B SD  1 
ATOM   2352 C  CE  . MET B 1 12  ? 57.501 -4.208  27.199  1.00 67.49  ? 20  MET B CE  1 
ATOM   2353 N  N   . ARG B 1 13  ? 62.815 -6.500  27.030  1.00 55.46  ? 21  ARG B N   1 
ATOM   2354 C  CA  . ARG B 1 13  ? 64.141 -6.457  26.436  1.00 62.63  ? 21  ARG B CA  1 
ATOM   2355 C  C   . ARG B 1 13  ? 64.046 -5.835  25.046  1.00 62.41  ? 21  ARG B C   1 
ATOM   2356 O  O   . ARG B 1 13  ? 63.079 -6.071  24.325  1.00 62.26  ? 21  ARG B O   1 
ATOM   2357 C  CB  . ARG B 1 13  ? 64.747 -7.863  26.372  1.00 68.52  ? 21  ARG B CB  1 
ATOM   2358 C  CG  . ARG B 1 13  ? 65.371 -8.335  27.677  1.00 79.44  ? 21  ARG B CG  1 
ATOM   2359 C  CD  . ARG B 1 13  ? 65.533 -9.844  27.741  1.00 79.46  ? 21  ARG B CD  1 
ATOM   2360 N  NE  . ARG B 1 13  ? 64.290 -10.554 27.469  1.00 93.13  ? 21  ARG B NE  1 
ATOM   2361 C  CZ  . ARG B 1 13  ? 64.185 -11.623 26.684  1.00 94.62  ? 21  ARG B CZ  1 
ATOM   2362 N  NH1 . ARG B 1 13  ? 65.239 -12.068 26.022  1.00 86.31  ? 21  ARG B NH1 1 
ATOM   2363 N  NH2 . ARG B 1 13  ? 63.024 -12.242 26.561  1.00 86.95  ? 21  ARG B NH2 1 
ATOM   2364 N  N   . MET B 1 14  ? 65.053 -5.033  24.681  1.00 55.95  ? 22  MET B N   1 
ATOM   2365 C  CA  . MET B 1 14  ? 65.131 -4.490  23.335  1.00 58.19  ? 22  MET B CA  1 
ATOM   2366 C  C   . MET B 1 14  ? 66.569 -4.085  23.021  1.00 56.58  ? 22  MET B C   1 
ATOM   2367 O  O   . MET B 1 14  ? 67.426 -4.056  23.901  1.00 50.78  ? 22  MET B O   1 
ATOM   2368 C  CB  . MET B 1 14  ? 64.221 -3.269  23.167  1.00 64.91  ? 22  MET B CB  1 
ATOM   2369 C  CG  . MET B 1 14  ? 64.687 -2.040  23.926  1.00 64.26  ? 22  MET B CG  1 
ATOM   2370 S  SD  . MET B 1 14  ? 63.461 -0.706  23.862  1.00 66.06  ? 22  MET B SD  1 
ATOM   2371 C  CE  . MET B 1 14  ? 64.325 0.586   24.753  1.00 68.37  ? 22  MET B CE  1 
ATOM   2372 N  N   . ASP B 1 15  ? 66.804 -3.773  21.743  1.00 57.69  ? 23  ASP B N   1 
ATOM   2373 C  CA  . ASP B 1 15  ? 68.097 -3.323  21.259  1.00 54.54  ? 23  ASP B CA  1 
ATOM   2374 C  C   . ASP B 1 15  ? 68.483 -2.048  22.005  1.00 50.95  ? 23  ASP B C   1 
ATOM   2375 O  O   . ASP B 1 15  ? 67.668 -1.138  22.139  1.00 56.52  ? 23  ASP B O   1 
ATOM   2376 C  CB  . ASP B 1 15  ? 68.042 -3.139  19.738  1.00 53.80  ? 23  ASP B CB  1 
ATOM   2377 C  CG  . ASP B 1 15  ? 69.368 -2.790  19.086  1.00 57.07  ? 23  ASP B CG  1 
ATOM   2378 O  OD1 . ASP B 1 15  ? 70.303 -2.407  19.818  1.00 61.73  ? 23  ASP B OD1 1 
ATOM   2379 O  OD2 . ASP B 1 15  ? 69.456 -2.919  17.848  1.00 62.91  ? 23  ASP B OD2 1 
ATOM   2380 N  N   . LYS B 1 16  ? 69.729 -2.001  22.491  1.00 56.81  ? 24  LYS B N   1 
ATOM   2381 C  CA  . LYS B 1 16  ? 70.211 -0.890  23.298  1.00 68.17  ? 24  LYS B CA  1 
ATOM   2382 C  C   . LYS B 1 16  ? 70.166 0.394   22.473  1.00 65.27  ? 24  LYS B C   1 
ATOM   2383 O  O   . LYS B 1 16  ? 70.085 1.488   23.026  1.00 64.37  ? 24  LYS B O   1 
ATOM   2384 C  CB  . LYS B 1 16  ? 71.631 -1.179  23.800  1.00 64.30  ? 24  LYS B CB  1 
ATOM   2385 C  CG  . LYS B 1 16  ? 71.986 -0.601  25.167  1.00 78.28  ? 24  LYS B CG  1 
ATOM   2386 C  CD  . LYS B 1 16  ? 72.708 0.731   25.130  1.00 97.30  ? 24  LYS B CD  1 
ATOM   2387 C  CE  . LYS B 1 16  ? 73.411 1.047   26.435  1.00 105.37 ? 24  LYS B CE  1 
ATOM   2388 N  NZ  . LYS B 1 16  ? 74.350 2.186   26.298  1.00 121.00 ? 24  LYS B NZ  1 
ATOM   2389 N  N   . ASN B 1 17  ? 70.214 0.247   21.144  1.00 62.82  ? 25  ASN B N   1 
ATOM   2390 C  CA  . ASN B 1 17  ? 70.208 1.389   20.245  1.00 65.02  ? 25  ASN B CA  1 
ATOM   2391 C  C   . ASN B 1 17  ? 68.848 2.081   20.302  1.00 59.04  ? 25  ASN B C   1 
ATOM   2392 O  O   . ASN B 1 17  ? 68.761 3.285   20.072  1.00 61.96  ? 25  ASN B O   1 
ATOM   2393 C  CB  . ASN B 1 17  ? 70.583 0.998   18.812  1.00 68.05  ? 25  ASN B CB  1 
ATOM   2394 C  CG  . ASN B 1 17  ? 72.062 0.718   18.641  1.00 70.71  ? 25  ASN B CG  1 
ATOM   2395 O  OD1 . ASN B 1 17  ? 72.448 -0.371  18.222  1.00 82.82  ? 25  ASN B OD1 1 
ATOM   2396 N  ND2 . ASN B 1 17  ? 72.896 1.698   18.949  1.00 59.46  ? 25  ASN B ND2 1 
ATOM   2397 N  N   . TRP B 1 18  ? 67.788 1.318   20.603  1.00 58.19  ? 26  TRP B N   1 
ATOM   2398 C  CA  . TRP B 1 18  ? 66.480 1.908   20.840  1.00 64.13  ? 26  TRP B CA  1 
ATOM   2399 C  C   . TRP B 1 18  ? 66.554 2.831   22.054  1.00 71.90  ? 26  TRP B C   1 
ATOM   2400 O  O   . TRP B 1 18  ? 65.899 3.871   22.087  1.00 57.29  ? 26  TRP B O   1 
ATOM   2401 C  CB  . TRP B 1 18  ? 65.398 0.842   21.070  1.00 60.63  ? 26  TRP B CB  1 
ATOM   2402 C  CG  . TRP B 1 18  ? 64.992 0.022   19.872  1.00 66.73  ? 26  TRP B CG  1 
ATOM   2403 C  CD1 . TRP B 1 18  ? 65.036 -1.339  19.792  1.00 75.10  ? 26  TRP B CD1 1 
ATOM   2404 C  CD2 . TRP B 1 18  ? 64.432 0.478   18.618  1.00 73.29  ? 26  TRP B CD2 1 
ATOM   2405 N  NE1 . TRP B 1 18  ? 64.568 -1.763  18.578  1.00 79.68  ? 26  TRP B NE1 1 
ATOM   2406 C  CE2 . TRP B 1 18  ? 64.188 -0.675  17.838  1.00 81.18  ? 26  TRP B CE2 1 
ATOM   2407 C  CE3 . TRP B 1 18  ? 64.123 1.731   18.076  1.00 78.85  ? 26  TRP B CE3 1 
ATOM   2408 C  CZ2 . TRP B 1 18  ? 63.653 -0.607  16.554  1.00 77.88  ? 26  TRP B CZ2 1 
ATOM   2409 C  CZ3 . TRP B 1 18  ? 63.591 1.795   16.806  1.00 78.71  ? 26  TRP B CZ3 1 
ATOM   2410 C  CH2 . TRP B 1 18  ? 63.357 0.642   16.059  1.00 79.43  ? 26  TRP B CH2 1 
ATOM   2411 N  N   . MET B 1 19  ? 67.347 2.431   23.056  1.00 66.54  ? 27  MET B N   1 
ATOM   2412 C  CA  . MET B 1 19  ? 67.404 3.138   24.326  1.00 66.06  ? 27  MET B CA  1 
ATOM   2413 C  C   . MET B 1 19  ? 68.433 4.263   24.253  1.00 61.69  ? 27  MET B C   1 
ATOM   2414 O  O   . MET B 1 19  ? 68.182 5.370   24.724  1.00 56.64  ? 27  MET B O   1 
ATOM   2415 C  CB  . MET B 1 19  ? 67.762 2.184   25.471  1.00 75.43  ? 27  MET B CB  1 
ATOM   2416 C  CG  . MET B 1 19  ? 66.853 2.321   26.678  1.00 84.22  ? 27  MET B CG  1 
ATOM   2417 S  SD  . MET B 1 19  ? 66.881 0.850   27.732  1.00 109.83 ? 27  MET B SD  1 
ATOM   2418 C  CE  . MET B 1 19  ? 68.568 0.913   28.335  1.00 106.63 ? 27  MET B CE  1 
ATOM   2419 N  N   . ILE B 1 20  ? 69.591 3.956   23.662  1.00 57.25  ? 28  ILE B N   1 
ATOM   2420 C  CA  . ILE B 1 20  ? 70.650 4.928   23.446  1.00 59.94  ? 28  ILE B CA  1 
ATOM   2421 C  C   . ILE B 1 20  ? 71.055 4.860   21.975  1.00 67.27  ? 28  ILE B C   1 
ATOM   2422 O  O   . ILE B 1 20  ? 71.761 3.940   21.570  1.00 66.63  ? 28  ILE B O   1 
ATOM   2423 C  CB  . ILE B 1 20  ? 71.845 4.642   24.378  1.00 65.86  ? 28  ILE B CB  1 
ATOM   2424 C  CG1 . ILE B 1 20  ? 71.425 4.573   25.850  1.00 64.53  ? 28  ILE B CG1 1 
ATOM   2425 C  CG2 . ILE B 1 20  ? 72.964 5.650   24.158  1.00 65.92  ? 28  ILE B CG2 1 
ATOM   2426 C  CD1 . ILE B 1 20  ? 70.999 5.899   26.437  1.00 61.49  ? 28  ILE B CD1 1 
ATOM   2427 N  N   . ALA B 1 21  ? 70.591 5.829   21.179  1.00 72.65  ? 29  ALA B N   1 
ATOM   2428 C  CA  . ALA B 1 21  ? 70.851 5.834   19.748  1.00 72.74  ? 29  ALA B CA  1 
ATOM   2429 C  C   . ALA B 1 21  ? 72.357 5.846   19.487  1.00 74.64  ? 29  ALA B C   1 
ATOM   2430 O  O   . ALA B 1 21  ? 73.081 6.664   20.051  1.00 68.83  ? 29  ALA B O   1 
ATOM   2431 C  CB  . ALA B 1 21  ? 70.169 7.019   19.106  1.00 67.58  ? 29  ALA B CB  1 
ATOM   2432 N  N   . MET B 1 22  ? 72.809 4.918   18.633  1.00 64.60  ? 30  MET B N   1 
ATOM   2433 C  CA  . MET B 1 22  ? 74.188 4.864   18.168  1.00 65.48  ? 30  MET B CA  1 
ATOM   2434 C  C   . MET B 1 22  ? 75.136 4.709   19.356  1.00 62.45  ? 30  MET B C   1 
ATOM   2435 O  O   . MET B 1 22  ? 76.103 5.458   19.481  1.00 69.74  ? 30  MET B O   1 
ATOM   2436 C  CB  . MET B 1 22  ? 74.552 6.137   17.395  1.00 70.20  ? 30  MET B CB  1 
ATOM   2437 C  CG  . MET B 1 22  ? 73.718 6.348   16.141  1.00 73.24  ? 30  MET B CG  1 
ATOM   2438 S  SD  . MET B 1 22  ? 73.743 4.939   15.001  1.00 77.27  ? 30  MET B SD  1 
ATOM   2439 C  CE  . MET B 1 22  ? 75.486 4.520   15.015  1.00 67.51  ? 30  MET B CE  1 
ATOM   2440 N  N   . HIS B 1 23  ? 74.863 3.712   20.206  1.00 63.33  ? 31  HIS B N   1 
ATOM   2441 C  CA  . HIS B 1 23  ? 75.538 3.579   21.488  1.00 73.14  ? 31  HIS B CA  1 
ATOM   2442 C  C   . HIS B 1 23  ? 76.949 3.025   21.306  1.00 72.77  ? 31  HIS B C   1 
ATOM   2443 O  O   . HIS B 1 23  ? 77.814 3.251   22.150  1.00 76.53  ? 31  HIS B O   1 
ATOM   2444 C  CB  . HIS B 1 23  ? 74.734 2.692   22.447  1.00 74.42  ? 31  HIS B CB  1 
ATOM   2445 C  CG  . HIS B 1 23  ? 74.894 1.224   22.216  1.00 77.81  ? 31  HIS B CG  1 
ATOM   2446 N  ND1 . HIS B 1 23  ? 75.760 0.458   22.967  1.00 77.49  ? 31  HIS B ND1 1 
ATOM   2447 C  CD2 . HIS B 1 23  ? 74.333 0.388   21.333  1.00 78.19  ? 31  HIS B CD2 1 
ATOM   2448 C  CE1 . HIS B 1 23  ? 75.708 -0.799  22.549  1.00 83.25  ? 31  HIS B CE1 1 
ATOM   2449 N  NE2 . HIS B 1 23  ? 74.845 -0.865  21.559  1.00 81.99  ? 31  HIS B NE2 1 
ATOM   2450 N  N   . ASN B 1 24  ? 77.169 2.291   20.210  1.00 68.97  ? 32  ASN B N   1 
ATOM   2451 C  CA  . ASN B 1 24  ? 78.443 1.636   19.963  1.00 76.34  ? 32  ASN B CA  1 
ATOM   2452 C  C   . ASN B 1 24  ? 78.686 1.572   18.456  1.00 72.48  ? 32  ASN B C   1 
ATOM   2453 O  O   . ASN B 1 24  ? 78.516 0.520   17.844  1.00 63.67  ? 32  ASN B O   1 
ATOM   2454 C  CB  . ASN B 1 24  ? 78.479 0.245   20.604  1.00 79.98  ? 32  ASN B CB  1 
ATOM   2455 C  CG  . ASN B 1 24  ? 79.736 -0.536  20.280  1.00 79.58  ? 32  ASN B CG  1 
ATOM   2456 O  OD1 . ASN B 1 24  ? 80.843 -0.020  20.412  1.00 82.62  ? 32  ASN B OD1 1 
ATOM   2457 N  ND2 . ASN B 1 24  ? 79.574 -1.777  19.851  1.00 76.84  ? 32  ASN B ND2 1 
ATOM   2458 N  N   . PRO B 1 25  ? 79.087 2.690   17.808  1.00 65.22  ? 33  PRO B N   1 
ATOM   2459 C  CA  . PRO B 1 25  ? 79.210 2.731   16.350  1.00 67.99  ? 33  PRO B CA  1 
ATOM   2460 C  C   . PRO B 1 25  ? 80.290 1.801   15.800  1.00 65.75  ? 33  PRO B C   1 
ATOM   2461 O  O   . PRO B 1 25  ? 81.287 1.530   16.466  1.00 60.98  ? 33  PRO B O   1 
ATOM   2462 C  CB  . PRO B 1 25  ? 79.575 4.195   16.054  1.00 64.62  ? 33  PRO B CB  1 
ATOM   2463 C  CG  . PRO B 1 25  ? 79.131 4.946   17.294  1.00 65.85  ? 33  PRO B CG  1 
ATOM   2464 C  CD  . PRO B 1 25  ? 79.415 3.983   18.428  1.00 68.52  ? 33  PRO B CD  1 
ATOM   2465 N  N   . ALA B 1 26  ? 80.069 1.324   14.571  1.00 65.38  ? 34  ALA B N   1 
ATOM   2466 C  CA  . ALA B 1 26  ? 81.040 0.504   13.868  1.00 66.67  ? 34  ALA B CA  1 
ATOM   2467 C  C   . ALA B 1 26  ? 82.269 1.347   13.534  1.00 70.82  ? 34  ALA B C   1 
ATOM   2468 O  O   . ALA B 1 26  ? 82.159 2.551   13.311  1.00 66.50  ? 34  ALA B O   1 
ATOM   2469 C  CB  . ALA B 1 26  ? 80.411 -0.079  12.626  1.00 63.41  ? 34  ALA B CB  1 
ATOM   2470 N  N   . THR B 1 27  ? 83.437 0.696   13.513  1.00 61.77  ? 35  THR B N   1 
ATOM   2471 C  CA  . THR B 1 27  ? 84.694 1.359   13.206  1.00 66.72  ? 35  THR B CA  1 
ATOM   2472 C  C   . THR B 1 27  ? 85.458 0.517   12.188  1.00 64.68  ? 35  THR B C   1 
ATOM   2473 O  O   . THR B 1 27  ? 85.023 -0.578  11.842  1.00 54.89  ? 35  THR B O   1 
ATOM   2474 C  CB  . THR B 1 27  ? 85.526 1.576   14.476  1.00 70.91  ? 35  THR B CB  1 
ATOM   2475 O  OG1 . THR B 1 27  ? 85.885 0.294   14.990  1.00 89.47  ? 35  THR B OG1 1 
ATOM   2476 C  CG2 . THR B 1 27  ? 84.794 2.363   15.540  1.00 78.59  ? 35  THR B CG2 1 
ATOM   2477 N  N   . ILE B 1 28  ? 86.601 1.032   11.719  1.00 71.25  ? 36  ILE B N   1 
ATOM   2478 C  CA  . ILE B 1 28  ? 87.447 0.284   10.804  1.00 80.69  ? 36  ILE B CA  1 
ATOM   2479 C  C   . ILE B 1 28  ? 87.866 -1.026  11.470  1.00 83.24  ? 36  ILE B C   1 
ATOM   2480 O  O   . ILE B 1 28  ? 88.000 -2.047  10.798  1.00 73.91  ? 36  ILE B O   1 
ATOM   2481 C  CB  . ILE B 1 28  ? 88.661 1.117   10.344  1.00 86.08  ? 36  ILE B CB  1 
ATOM   2482 C  CG1 . ILE B 1 28  ? 89.213 1.988   11.476  1.00 98.31  ? 36  ILE B CG1 1 
ATOM   2483 C  CG2 . ILE B 1 28  ? 88.309 1.951   9.121   1.00 86.31  ? 36  ILE B CG2 1 
ATOM   2484 C  CD1 . ILE B 1 28  ? 90.561 2.602   11.178  1.00 102.87 ? 36  ILE B CD1 1 
ATOM   2485 N  N   A HIS B 1 29  ? 88.057 -0.988  12.794  0.50 80.87  ? 37  HIS B N   1 
ATOM   2486 N  N   B HIS B 1 29  ? 88.060 -0.985  12.795  0.50 84.63  ? 37  HIS B N   1 
ATOM   2487 C  CA  A HIS B 1 29  ? 88.519 -2.154  13.530  0.50 79.26  ? 37  HIS B CA  1 
ATOM   2488 C  CA  B HIS B 1 29  ? 88.521 -2.146  13.540  0.50 85.67  ? 37  HIS B CA  1 
ATOM   2489 C  C   A HIS B 1 29  ? 87.331 -3.009  13.968  0.50 81.18  ? 37  HIS B C   1 
ATOM   2490 C  C   B HIS B 1 29  ? 87.329 -3.014  13.943  0.50 84.40  ? 37  HIS B C   1 
ATOM   2491 O  O   A HIS B 1 29  ? 87.494 -4.195  14.248  0.50 79.62  ? 37  HIS B O   1 
ATOM   2492 O  O   B HIS B 1 29  ? 87.485 -4.211  14.176  0.50 82.47  ? 37  HIS B O   1 
ATOM   2493 C  CB  A HIS B 1 29  ? 89.439 -1.735  14.683  0.50 81.20  ? 37  HIS B CB  1 
ATOM   2494 C  CB  B HIS B 1 29  ? 89.372 -1.718  14.743  0.50 91.71  ? 37  HIS B CB  1 
ATOM   2495 C  CG  A HIS B 1 29  ? 90.775 -1.266  14.210  0.50 83.98  ? 37  HIS B CG  1 
ATOM   2496 C  CG  B HIS B 1 29  ? 90.190 -2.822  15.332  0.50 101.60 ? 37  HIS B CG  1 
ATOM   2497 N  ND1 A HIS B 1 29  ? 91.008 0.013   13.755  0.50 83.21  ? 37  HIS B ND1 1 
ATOM   2498 N  ND1 B HIS B 1 29  ? 90.435 -2.945  16.683  0.50 99.06  ? 37  HIS B ND1 1 
ATOM   2499 C  CD2 A HIS B 1 29  ? 91.948 -1.909  14.129  0.50 82.44  ? 37  HIS B CD2 1 
ATOM   2500 C  CD2 B HIS B 1 29  ? 90.852 -3.829  14.744  0.50 99.17  ? 37  HIS B CD2 1 
ATOM   2501 C  CE1 A HIS B 1 29  ? 92.282 0.127   13.406  0.50 78.69  ? 37  HIS B CE1 1 
ATOM   2502 C  CE1 B HIS B 1 29  ? 91.202 -4.006  16.894  0.50 92.59  ? 37  HIS B CE1 1 
ATOM   2503 N  NE2 A HIS B 1 29  ? 92.870 -1.029  13.623  0.50 82.21  ? 37  HIS B NE2 1 
ATOM   2504 N  NE2 B HIS B 1 29  ? 91.464 -4.559  15.730  0.50 93.20  ? 37  HIS B NE2 1 
ATOM   2505 N  N   . ASN B 1 30  ? 86.139 -2.405  14.017  1.00 79.81  ? 38  ASN B N   1 
ATOM   2506 C  CA  . ASN B 1 30  ? 84.931 -3.136  14.369  1.00 73.84  ? 38  ASN B CA  1 
ATOM   2507 C  C   . ASN B 1 30  ? 83.841 -2.820  13.347  1.00 71.94  ? 38  ASN B C   1 
ATOM   2508 O  O   . ASN B 1 30  ? 82.835 -2.195  13.677  1.00 65.03  ? 38  ASN B O   1 
ATOM   2509 C  CB  . ASN B 1 30  ? 84.474 -2.833  15.800  1.00 72.42  ? 38  ASN B CB  1 
ATOM   2510 C  CG  . ASN B 1 30  ? 83.530 -3.877  16.361  1.00 70.85  ? 38  ASN B CG  1 
ATOM   2511 O  OD1 . ASN B 1 30  ? 82.965 -3.691  17.436  1.00 73.74  ? 38  ASN B OD1 1 
ATOM   2512 N  ND2 . ASN B 1 30  ? 83.349 -4.974  15.643  1.00 71.59  ? 38  ASN B ND2 1 
ATOM   2513 N  N   . PRO B 1 31  ? 83.997 -3.269  12.081  1.00 77.17  ? 39  PRO B N   1 
ATOM   2514 C  CA  . PRO B 1 31  ? 83.062 -2.920  11.011  1.00 70.52  ? 39  PRO B CA  1 
ATOM   2515 C  C   . PRO B 1 31  ? 81.677 -3.535  11.187  1.00 70.38  ? 39  PRO B C   1 
ATOM   2516 O  O   . PRO B 1 31  ? 80.692 -3.012  10.671  1.00 71.49  ? 39  PRO B O   1 
ATOM   2517 C  CB  . PRO B 1 31  ? 83.740 -3.495  9.758   1.00 76.49  ? 39  PRO B CB  1 
ATOM   2518 C  CG  . PRO B 1 31  ? 84.544 -4.661  10.288  1.00 72.38  ? 39  PRO B CG  1 
ATOM   2519 C  CD  . PRO B 1 31  ? 85.068 -4.167  11.620  1.00 79.62  ? 39  PRO B CD  1 
ATOM   2520 N  N   . ASN B 1 32  ? 81.612 -4.655  11.912  1.00 63.61  ? 40  ASN B N   1 
ATOM   2521 C  CA  . ASN B 1 32  ? 80.351 -5.345  12.122  1.00 75.79  ? 40  ASN B CA  1 
ATOM   2522 C  C   . ASN B 1 32  ? 80.001 -5.288  13.606  1.00 69.35  ? 40  ASN B C   1 
ATOM   2523 O  O   . ASN B 1 32  ? 79.614 -6.292  14.200  1.00 66.91  ? 40  ASN B O   1 
ATOM   2524 C  CB  . ASN B 1 32  ? 80.405 -6.775  11.577  1.00 79.24  ? 40  ASN B CB  1 
ATOM   2525 C  CG  . ASN B 1 32  ? 80.851 -6.827  10.130  1.00 75.03  ? 40  ASN B CG  1 
ATOM   2526 O  OD1 . ASN B 1 32  ? 80.184 -6.284  9.252   1.00 67.73  ? 40  ASN B OD1 1 
ATOM   2527 N  ND2 . ASN B 1 32  ? 81.978 -7.471  9.873   1.00 72.52  ? 40  ASN B ND2 1 
ATOM   2528 N  N   . ALA B 1 33  ? 80.133 -4.090  14.188  1.00 66.69  ? 41  ALA B N   1 
ATOM   2529 C  CA  . ALA B 1 33  ? 79.890 -3.885  15.607  1.00 68.38  ? 41  ALA B CA  1 
ATOM   2530 C  C   . ALA B 1 33  ? 78.532 -4.471  15.988  1.00 60.65  ? 41  ALA B C   1 
ATOM   2531 O  O   . ALA B 1 33  ? 77.576 -4.384  15.221  1.00 60.17  ? 41  ALA B O   1 
ATOM   2532 C  CB  . ALA B 1 33  ? 79.971 -2.414  15.937  1.00 70.61  ? 41  ALA B CB  1 
ATOM   2533 N  N   . GLN B 1 34  ? 78.467 -5.065  17.185  1.00 64.81  ? 42  GLN B N   1 
ATOM   2534 C  CA  . GLN B 1 34  ? 77.263 -5.733  17.653  1.00 72.13  ? 42  GLN B CA  1 
ATOM   2535 C  C   . GLN B 1 34  ? 76.557 -4.857  18.683  1.00 61.64  ? 42  GLN B C   1 
ATOM   2536 O  O   . GLN B 1 34  ? 77.204 -4.103  19.408  1.00 61.32  ? 42  GLN B O   1 
ATOM   2537 C  CB  . GLN B 1 34  ? 77.604 -7.080  18.293  1.00 78.52  ? 42  GLN B CB  1 
ATOM   2538 C  CG  . GLN B 1 34  ? 78.576 -7.924  17.484  1.00 91.84  ? 42  GLN B CG  1 
ATOM   2539 C  CD  . GLN B 1 34  ? 78.780 -9.286  18.101  1.00 87.57  ? 42  GLN B CD  1 
ATOM   2540 O  OE1 . GLN B 1 34  ? 78.406 -9.534  19.246  1.00 82.09  ? 42  GLN B OE1 1 
ATOM   2541 N  NE2 . GLN B 1 34  ? 79.385 -10.185 17.342  1.00 85.35  ? 42  GLN B NE2 1 
ATOM   2542 N  N   . THR B 1 35  ? 75.227 -4.981  18.748  1.00 60.50  ? 43  THR B N   1 
ATOM   2543 C  CA  . THR B 1 35  ? 74.448 -4.321  19.783  1.00 69.12  ? 43  THR B CA  1 
ATOM   2544 C  C   . THR B 1 35  ? 74.171 -5.313  20.909  1.00 70.01  ? 43  THR B C   1 
ATOM   2545 O  O   . THR B 1 35  ? 74.658 -6.441  20.879  1.00 67.34  ? 43  THR B O   1 
ATOM   2546 C  CB  . THR B 1 35  ? 73.141 -3.746  19.222  1.00 61.85  ? 43  THR B CB  1 
ATOM   2547 O  OG1 . THR B 1 35  ? 72.550 -2.943  20.244  1.00 63.09  ? 43  THR B OG1 1 
ATOM   2548 C  CG2 . THR B 1 35  ? 72.169 -4.815  18.773  1.00 63.72  ? 43  THR B CG2 1 
ATOM   2549 N  N   . GLU B 1 36  ? 73.381 -4.877  21.897  1.00 72.90  ? 44  GLU B N   1 
ATOM   2550 C  CA  . GLU B 1 36  ? 73.001 -5.724  23.016  1.00 70.81  ? 44  GLU B CA  1 
ATOM   2551 C  C   . GLU B 1 36  ? 71.480 -5.717  23.154  1.00 64.79  ? 44  GLU B C   1 
ATOM   2552 O  O   . GLU B 1 36  ? 70.831 -4.724  22.833  1.00 64.71  ? 44  GLU B O   1 
ATOM   2553 C  CB  . GLU B 1 36  ? 73.658 -5.251  24.316  1.00 75.83  ? 44  GLU B CB  1 
ATOM   2554 C  CG  . GLU B 1 36  ? 75.177 -5.292  24.298  1.00 87.85  ? 44  GLU B CG  1 
ATOM   2555 C  CD  . GLU B 1 36  ? 75.853 -3.950  24.073  1.00 112.53 ? 44  GLU B CD  1 
ATOM   2556 O  OE1 . GLU B 1 36  ? 75.687 -3.058  24.930  1.00 109.12 ? 44  GLU B OE1 1 
ATOM   2557 O  OE2 . GLU B 1 36  ? 76.548 -3.801  23.048  1.00 121.79 ? 44  GLU B OE2 1 
ATOM   2558 N  N   . PHE B 1 37  ? 70.926 -6.842  23.621  1.00 64.66  ? 45  PHE B N   1 
ATOM   2559 C  CA  . PHE B 1 37  ? 69.508 -6.940  23.927  1.00 61.18  ? 45  PHE B CA  1 
ATOM   2560 C  C   . PHE B 1 37  ? 69.327 -6.711  25.426  1.00 71.20  ? 45  PHE B C   1 
ATOM   2561 O  O   . PHE B 1 37  ? 69.418 -7.650  26.213  1.00 69.49  ? 45  PHE B O   1 
ATOM   2562 C  CB  . PHE B 1 37  ? 68.967 -8.306  23.491  1.00 63.52  ? 45  PHE B CB  1 
ATOM   2563 C  CG  . PHE B 1 37  ? 67.533 -8.316  23.023  1.00 66.84  ? 45  PHE B CG  1 
ATOM   2564 C  CD1 . PHE B 1 37  ? 67.099 -7.426  22.054  1.00 67.43  ? 45  PHE B CD1 1 
ATOM   2565 C  CD2 . PHE B 1 37  ? 66.625 -9.238  23.522  1.00 65.76  ? 45  PHE B CD2 1 
ATOM   2566 C  CE1 . PHE B 1 37  ? 65.785 -7.441  21.612  1.00 71.18  ? 45  PHE B CE1 1 
ATOM   2567 C  CE2 . PHE B 1 37  ? 65.311 -9.251  23.078  1.00 71.01  ? 45  PHE B CE2 1 
ATOM   2568 C  CZ  . PHE B 1 37  ? 64.894 -8.353  22.125  1.00 71.57  ? 45  PHE B CZ  1 
ATOM   2569 N  N   . VAL B 1 38  ? 69.083 -5.452  25.811  1.00 75.62  ? 46  VAL B N   1 
ATOM   2570 C  CA  . VAL B 1 38  ? 69.109 -5.054  27.211  1.00 67.40  ? 46  VAL B CA  1 
ATOM   2571 C  C   . VAL B 1 38  ? 67.720 -5.231  27.821  1.00 62.67  ? 46  VAL B C   1 
ATOM   2572 O  O   . VAL B 1 38  ? 66.713 -5.160  27.120  1.00 61.09  ? 46  VAL B O   1 
ATOM   2573 C  CB  . VAL B 1 38  ? 69.613 -3.606  27.374  1.00 75.78  ? 46  VAL B CB  1 
ATOM   2574 C  CG1 . VAL B 1 38  ? 71.090 -3.483  27.028  1.00 81.26  ? 46  VAL B CG1 1 
ATOM   2575 C  CG2 . VAL B 1 38  ? 68.787 -2.620  26.561  1.00 81.19  ? 46  VAL B CG2 1 
ATOM   2576 N  N   . GLU B 1 39  ? 67.687 -5.460  29.140  1.00 62.92  ? 47  GLU B N   1 
ATOM   2577 C  CA  . GLU B 1 39  ? 66.441 -5.629  29.871  1.00 64.55  ? 47  GLU B CA  1 
ATOM   2578 C  C   . GLU B 1 39  ? 66.164 -4.368  30.684  1.00 56.59  ? 47  GLU B C   1 
ATOM   2579 O  O   . GLU B 1 39  ? 67.089 -3.712  31.154  1.00 52.64  ? 47  GLU B O   1 
ATOM   2580 C  CB  . GLU B 1 39  ? 66.513 -6.846  30.794  1.00 72.65  ? 47  GLU B CB  1 
ATOM   2581 C  CG  . GLU B 1 39  ? 65.150 -7.346  31.244  1.00 92.56  ? 47  GLU B CG  1 
ATOM   2582 C  CD  . GLU B 1 39  ? 65.179 -8.645  32.032  1.00 96.55  ? 47  GLU B CD  1 
ATOM   2583 O  OE1 . GLU B 1 39  ? 65.743 -8.648  33.144  1.00 89.00  ? 47  GLU B OE1 1 
ATOM   2584 O  OE2 . GLU B 1 39  ? 64.641 -9.652  31.529  1.00 97.71  ? 47  GLU B OE2 1 
ATOM   2585 N  N   . PHE B 1 40  ? 64.878 -4.046  30.856  1.00 57.28  ? 48  PHE B N   1 
ATOM   2586 C  CA  . PHE B 1 40  ? 64.494 -2.840  31.569  1.00 59.62  ? 48  PHE B CA  1 
ATOM   2587 C  C   . PHE B 1 40  ? 63.114 -3.031  32.191  1.00 49.96  ? 48  PHE B C   1 
ATOM   2588 O  O   . PHE B 1 40  ? 62.291 -3.789  31.683  1.00 51.06  ? 48  PHE B O   1 
ATOM   2589 C  CB  . PHE B 1 40  ? 64.568 -1.628  30.635  1.00 55.30  ? 48  PHE B CB  1 
ATOM   2590 C  CG  . PHE B 1 40  ? 63.692 -1.710  29.412  1.00 57.11  ? 48  PHE B CG  1 
ATOM   2591 C  CD1 . PHE B 1 40  ? 62.381 -1.260  29.443  1.00 61.18  ? 48  PHE B CD1 1 
ATOM   2592 C  CD2 . PHE B 1 40  ? 64.172 -2.260  28.234  1.00 61.26  ? 48  PHE B CD2 1 
ATOM   2593 C  CE1 . PHE B 1 40  ? 61.578 -1.339  28.315  1.00 66.40  ? 48  PHE B CE1 1 
ATOM   2594 C  CE2 . PHE B 1 40  ? 63.365 -2.344  27.110  1.00 65.26  ? 48  PHE B CE2 1 
ATOM   2595 C  CZ  . PHE B 1 40  ? 62.070 -1.884  27.153  1.00 67.59  ? 48  PHE B CZ  1 
ATOM   2596 N  N   . PRO B 1 41  ? 62.839 -2.353  33.326  1.00 49.65  ? 49  PRO B N   1 
ATOM   2597 C  CA  . PRO B 1 41  ? 61.580 -2.515  34.052  1.00 49.32  ? 49  PRO B CA  1 
ATOM   2598 C  C   . PRO B 1 41  ? 60.389 -1.799  33.427  1.00 50.46  ? 49  PRO B C   1 
ATOM   2599 O  O   . PRO B 1 41  ? 60.525 -0.710  32.876  1.00 53.01  ? 49  PRO B O   1 
ATOM   2600 C  CB  . PRO B 1 41  ? 61.881 -1.850  35.401  1.00 48.72  ? 49  PRO B CB  1 
ATOM   2601 C  CG  . PRO B 1 41  ? 62.873 -0.766  35.044  1.00 54.44  ? 49  PRO B CG  1 
ATOM   2602 C  CD  . PRO B 1 41  ? 63.745 -1.397  33.979  1.00 49.89  ? 49  PRO B CD  1 
ATOM   2603 N  N   . ILE B 1 42  ? 59.221 -2.435  33.538  1.00 49.42  ? 50  ILE B N   1 
ATOM   2604 C  CA  . ILE B 1 42  ? 57.952 -1.791  33.255  1.00 48.10  ? 50  ILE B CA  1 
ATOM   2605 C  C   . ILE B 1 42  ? 57.249 -1.572  34.589  1.00 47.66  ? 50  ILE B C   1 
ATOM   2606 O  O   . ILE B 1 42  ? 57.037 -2.527  35.332  1.00 50.62  ? 50  ILE B O   1 
ATOM   2607 C  CB  . ILE B 1 42  ? 57.096 -2.654  32.308  1.00 48.86  ? 50  ILE B CB  1 
ATOM   2608 C  CG1 . ILE B 1 42  ? 57.896 -3.157  31.104  1.00 52.15  ? 50  ILE B CG1 1 
ATOM   2609 C  CG2 . ILE B 1 42  ? 55.844 -1.902  31.885  1.00 52.05  ? 50  ILE B CG2 1 
ATOM   2610 C  CD1 . ILE B 1 42  ? 58.462 -2.058  30.239  1.00 57.45  ? 50  ILE B CD1 1 
ATOM   2611 N  N   . TYR B 1 43  ? 56.899 -0.319  34.897  1.00 48.25  ? 51  TYR B N   1 
ATOM   2612 C  CA  . TYR B 1 43  ? 56.268 -0.039  36.174  1.00 49.06  ? 51  TYR B CA  1 
ATOM   2613 C  C   . TYR B 1 43  ? 55.185 1.024   36.023  1.00 43.85  ? 51  TYR B C   1 
ATOM   2614 O  O   . TYR B 1 43  ? 55.129 1.751   35.034  1.00 43.91  ? 51  TYR B O   1 
ATOM   2615 C  CB  . TYR B 1 43  ? 57.309 0.322   37.240  1.00 46.71  ? 51  TYR B CB  1 
ATOM   2616 C  CG  . TYR B 1 43  ? 57.937 1.709   37.183  1.00 49.84  ? 51  TYR B CG  1 
ATOM   2617 C  CD1 . TYR B 1 43  ? 59.029 1.980   36.366  1.00 48.90  ? 51  TYR B CD1 1 
ATOM   2618 C  CD2 . TYR B 1 43  ? 57.458 2.741   37.982  1.00 53.17  ? 51  TYR B CD2 1 
ATOM   2619 C  CE1 . TYR B 1 43  ? 59.615 3.235   36.337  1.00 47.08  ? 51  TYR B CE1 1 
ATOM   2620 C  CE2 . TYR B 1 43  ? 58.033 4.000   37.959  1.00 51.70  ? 51  TYR B CE2 1 
ATOM   2621 C  CZ  . TYR B 1 43  ? 59.114 4.248   37.135  1.00 45.50  ? 51  TYR B CZ  1 
ATOM   2622 O  OH  . TYR B 1 43  ? 59.680 5.491   37.112  1.00 48.57  ? 51  TYR B OH  1 
ATOM   2623 N  N   . THR B 1 44  ? 54.313 1.054   37.034  1.00 43.83  ? 52  THR B N   1 
ATOM   2624 C  CA  . THR B 1 44  ? 53.223 2.003   37.144  1.00 43.02  ? 52  THR B CA  1 
ATOM   2625 C  C   . THR B 1 44  ? 53.274 2.598   38.547  1.00 45.03  ? 52  THR B C   1 
ATOM   2626 O  O   . THR B 1 44  ? 53.891 2.024   39.442  1.00 44.07  ? 52  THR B O   1 
ATOM   2627 C  CB  . THR B 1 44  ? 51.880 1.321   36.854  1.00 46.53  ? 52  THR B CB  1 
ATOM   2628 O  OG1 . THR B 1 44  ? 51.774 0.192   37.722  1.00 52.09  ? 52  THR B OG1 1 
ATOM   2629 C  CG2 . THR B 1 44  ? 51.742 0.872   35.416  1.00 45.65  ? 52  THR B CG2 1 
ATOM   2630 N  N   . VAL B 1 45  ? 52.637 3.756   38.728  1.00 43.46  ? 53  VAL B N   1 
ATOM   2631 C  CA  . VAL B 1 45  ? 52.653 4.437   40.010  1.00 40.72  ? 53  VAL B CA  1 
ATOM   2632 C  C   . VAL B 1 45  ? 51.216 4.759   40.402  1.00 44.34  ? 53  VAL B C   1 
ATOM   2633 O  O   . VAL B 1 45  ? 50.493 5.406   39.647  1.00 48.88  ? 53  VAL B O   1 
ATOM   2634 C  CB  . VAL B 1 45  ? 53.530 5.703   39.963  1.00 44.70  ? 53  VAL B CB  1 
ATOM   2635 C  CG1 . VAL B 1 45  ? 53.407 6.527   41.235  1.00 48.70  ? 53  VAL B CG1 1 
ATOM   2636 C  CG2 . VAL B 1 45  ? 54.988 5.368   39.681  1.00 48.48  ? 53  VAL B CG2 1 
ATOM   2637 N  N   . LEU B 1 46  ? 50.812 4.273   41.581  1.00 43.13  ? 54  LEU B N   1 
ATOM   2638 C  CA  . LEU B 1 46  ? 49.526 4.620   42.161  1.00 41.78  ? 54  LEU B CA  1 
ATOM   2639 C  C   . LEU B 1 46  ? 49.733 5.715   43.200  1.00 43.21  ? 54  LEU B C   1 
ATOM   2640 O  O   . LEU B 1 46  ? 50.510 5.543   44.137  1.00 47.46  ? 54  LEU B O   1 
ATOM   2641 C  CB  . LEU B 1 46  ? 48.902 3.380   42.809  1.00 48.66  ? 54  LEU B CB  1 
ATOM   2642 C  CG  . LEU B 1 46  ? 47.590 3.629   43.553  1.00 50.08  ? 54  LEU B CG  1 
ATOM   2643 C  CD1 . LEU B 1 46  ? 46.493 4.050   42.589  1.00 56.93  ? 54  LEU B CD1 1 
ATOM   2644 C  CD2 . LEU B 1 46  ? 47.162 2.396   44.336  1.00 55.74  ? 54  LEU B CD2 1 
ATOM   2645 N  N   . ILE B 1 47  ? 49.039 6.843   43.025  1.00 47.56  ? 55  ILE B N   1 
ATOM   2646 C  CA  . ILE B 1 47  ? 48.955 7.829   44.087  1.00 46.63  ? 55  ILE B CA  1 
ATOM   2647 C  C   . ILE B 1 47  ? 47.592 7.688   44.756  1.00 54.22  ? 55  ILE B C   1 
ATOM   2648 O  O   . ILE B 1 47  ? 46.585 8.150   44.227  1.00 54.15  ? 55  ILE B O   1 
ATOM   2649 C  CB  . ILE B 1 47  ? 49.196 9.268   43.587  1.00 49.57  ? 55  ILE B CB  1 
ATOM   2650 C  CG1 . ILE B 1 47  ? 50.538 9.425   42.866  1.00 50.60  ? 55  ILE B CG1 1 
ATOM   2651 C  CG2 . ILE B 1 47  ? 49.075 10.247  44.743  1.00 50.67  ? 55  ILE B CG2 1 
ATOM   2652 C  CD1 . ILE B 1 47  ? 50.504 9.050   41.405  1.00 59.96  ? 55  ILE B CD1 1 
ATOM   2653 N  N   . ASP B 1 48  ? 47.583 7.024   45.918  1.00 55.85  ? 56  ASP B N   1 
ATOM   2654 C  CA  . ASP B 1 48  ? 46.393 6.926   46.744  1.00 52.32  ? 56  ASP B CA  1 
ATOM   2655 C  C   . ASP B 1 48  ? 46.204 8.255   47.470  1.00 49.80  ? 56  ASP B C   1 
ATOM   2656 O  O   . ASP B 1 48  ? 46.801 8.492   48.517  1.00 51.08  ? 56  ASP B O   1 
ATOM   2657 C  CB  . ASP B 1 48  ? 46.491 5.748   47.718  1.00 54.25  ? 56  ASP B CB  1 
ATOM   2658 C  CG  . ASP B 1 48  ? 45.218 5.499   48.508  1.00 54.59  ? 56  ASP B CG  1 
ATOM   2659 O  OD1 . ASP B 1 48  ? 44.204 6.164   48.212  1.00 58.99  ? 56  ASP B OD1 1 
ATOM   2660 O  OD2 . ASP B 1 48  ? 45.253 4.645   49.415  1.00 63.40  ? 56  ASP B OD2 1 
ATOM   2661 N  N   . HIS B 1 49  ? 45.361 9.110   46.883  1.00 53.57  ? 57  HIS B N   1 
ATOM   2662 C  CA  . HIS B 1 49  ? 45.189 10.484  47.319  1.00 50.75  ? 57  HIS B CA  1 
ATOM   2663 C  C   . HIS B 1 49  ? 43.790 10.624  47.911  1.00 48.64  ? 57  HIS B C   1 
ATOM   2664 O  O   . HIS B 1 49  ? 42.840 10.041  47.394  1.00 57.35  ? 57  HIS B O   1 
ATOM   2665 C  CB  . HIS B 1 49  ? 45.401 11.423  46.124  1.00 51.45  ? 57  HIS B CB  1 
ATOM   2666 C  CG  . HIS B 1 49  ? 45.667 12.852  46.464  1.00 51.59  ? 57  HIS B CG  1 
ATOM   2667 N  ND1 . HIS B 1 49  ? 44.691 13.740  46.863  1.00 48.58  ? 57  HIS B ND1 1 
ATOM   2668 C  CD2 . HIS B 1 49  ? 46.808 13.555  46.413  1.00 53.08  ? 57  HIS B CD2 1 
ATOM   2669 C  CE1 . HIS B 1 49  ? 45.240 14.929  47.069  1.00 50.76  ? 57  HIS B CE1 1 
ATOM   2670 N  NE2 . HIS B 1 49  ? 46.526 14.839  46.802  1.00 46.99  ? 57  HIS B NE2 1 
ATOM   2671 N  N   . PRO B 1 50  ? 43.614 11.380  49.017  1.00 53.50  ? 58  PRO B N   1 
ATOM   2672 C  CA  . PRO B 1 50  ? 42.287 11.587  49.598  1.00 58.37  ? 58  PRO B CA  1 
ATOM   2673 C  C   . PRO B 1 50  ? 41.263 12.175  48.627  1.00 63.89  ? 58  PRO B C   1 
ATOM   2674 O  O   . PRO B 1 50  ? 40.063 11.962  48.793  1.00 59.87  ? 58  PRO B O   1 
ATOM   2675 C  CB  . PRO B 1 50  ? 42.537 12.548  50.773  1.00 55.55  ? 58  PRO B CB  1 
ATOM   2676 C  CG  . PRO B 1 50  ? 43.914 13.132  50.514  1.00 60.42  ? 58  PRO B CG  1 
ATOM   2677 C  CD  . PRO B 1 50  ? 44.675 12.043  49.790  1.00 60.16  ? 58  PRO B CD  1 
ATOM   2678 N  N   . GLU B 1 51  ? 41.733 12.909  47.611  1.00 58.31  ? 59  GLU B N   1 
ATOM   2679 C  CA  . GLU B 1 51  ? 40.834 13.489  46.626  1.00 59.19  ? 59  GLU B CA  1 
ATOM   2680 C  C   . GLU B 1 51  ? 40.471 12.443  45.577  1.00 56.98  ? 59  GLU B C   1 
ATOM   2681 O  O   . GLU B 1 51  ? 39.581 12.669  44.760  1.00 63.05  ? 59  GLU B O   1 
ATOM   2682 C  CB  . GLU B 1 51  ? 41.460 14.701  45.934  1.00 62.77  ? 59  GLU B CB  1 
ATOM   2683 C  CG  . GLU B 1 51  ? 41.652 15.901  46.838  1.00 59.24  ? 59  GLU B CG  1 
ATOM   2684 C  CD  . GLU B 1 51  ? 42.269 17.091  46.124  1.00 52.16  ? 59  GLU B CD  1 
ATOM   2685 O  OE1 . GLU B 1 51  ? 41.747 17.470  45.058  1.00 68.22  ? 59  GLU B OE1 1 
ATOM   2686 O  OE2 . GLU B 1 51  ? 43.268 17.633  46.632  1.00 59.15  ? 59  GLU B OE2 1 
ATOM   2687 N  N   . GLY B 1 52  ? 41.183 11.311  45.598  1.00 49.52  ? 60  GLY B N   1 
ATOM   2688 C  CA  . GLY B 1 52  ? 40.918 10.218  44.676  1.00 49.84  ? 60  GLY B CA  1 
ATOM   2689 C  C   . GLY B 1 52  ? 42.208 9.567   44.183  1.00 50.08  ? 60  GLY B C   1 
ATOM   2690 O  O   . GLY B 1 52  ? 43.267 10.190  44.202  1.00 57.15  ? 60  GLY B O   1 
ATOM   2691 N  N   . LYS B 1 53  ? 42.094 8.310   43.740  1.00 47.58  ? 61  LYS B N   1 
ATOM   2692 C  CA  . LYS B 1 53  ? 43.240 7.513   43.331  1.00 50.94  ? 61  LYS B CA  1 
ATOM   2693 C  C   . LYS B 1 53  ? 43.642 7.872   41.901  1.00 52.45  ? 61  LYS B C   1 
ATOM   2694 O  O   . LYS B 1 53  ? 42.823 7.840   40.984  1.00 53.86  ? 61  LYS B O   1 
ATOM   2695 C  CB  . LYS B 1 53  ? 42.913 6.024   43.497  1.00 57.36  ? 61  LYS B CB  1 
ATOM   2696 C  CG  . LYS B 1 53  ? 42.640 5.599   44.936  1.00 64.91  ? 61  LYS B CG  1 
ATOM   2697 C  CD  . LYS B 1 53  ? 42.419 4.110   45.133  1.00 71.40  ? 61  LYS B CD  1 
ATOM   2698 C  CE  . LYS B 1 53  ? 42.569 3.677   46.578  1.00 74.31  ? 61  LYS B CE  1 
ATOM   2699 N  NZ  . LYS B 1 53  ? 41.713 4.472   47.490  1.00 66.26  ? 61  LYS B NZ  1 
ATOM   2700 N  N   . ILE B 1 54  ? 44.926 8.216   41.745  1.00 50.46  ? 62  ILE B N   1 
ATOM   2701 C  CA  . ILE B 1 54  ? 45.518 8.605   40.475  1.00 50.70  ? 62  ILE B CA  1 
ATOM   2702 C  C   . ILE B 1 54  ? 46.530 7.533   40.075  1.00 54.07  ? 62  ILE B C   1 
ATOM   2703 O  O   . ILE B 1 54  ? 47.386 7.158   40.874  1.00 49.59  ? 62  ILE B O   1 
ATOM   2704 C  CB  . ILE B 1 54  ? 46.182 9.994   40.598  1.00 50.02  ? 62  ILE B CB  1 
ATOM   2705 C  CG1 . ILE B 1 54  ? 45.203 11.062  41.091  1.00 50.91  ? 62  ILE B CG1 1 
ATOM   2706 C  CG2 . ILE B 1 54  ? 46.840 10.405  39.289  1.00 49.67  ? 62  ILE B CG2 1 
ATOM   2707 C  CD1 . ILE B 1 54  ? 45.877 12.248  41.741  1.00 50.72  ? 62  ILE B CD1 1 
ATOM   2708 N  N   . LEU B 1 55  ? 46.417 7.042   38.835  1.00 50.63  ? 63  LEU B N   1 
ATOM   2709 C  CA  . LEU B 1 55  ? 47.317 6.024   38.315  1.00 51.04  ? 63  LEU B CA  1 
ATOM   2710 C  C   . LEU B 1 55  ? 48.146 6.630   37.185  1.00 48.44  ? 63  LEU B C   1 
ATOM   2711 O  O   . LEU B 1 55  ? 47.600 7.263   36.285  1.00 50.36  ? 63  LEU B O   1 
ATOM   2712 C  CB  . LEU B 1 55  ? 46.487 4.827   37.833  1.00 51.37  ? 63  LEU B CB  1 
ATOM   2713 C  CG  . LEU B 1 55  ? 47.268 3.689   37.175  1.00 52.19  ? 63  LEU B CG  1 
ATOM   2714 C  CD1 . LEU B 1 55  ? 48.296 3.108   38.131  1.00 54.04  ? 63  LEU B CD1 1 
ATOM   2715 C  CD2 . LEU B 1 55  ? 46.329 2.595   36.685  1.00 54.15  ? 63  LEU B CD2 1 
ATOM   2716 N  N   . PHE B 1 56  ? 49.470 6.449   37.253  1.00 43.85  ? 64  PHE B N   1 
ATOM   2717 C  CA  . PHE B 1 56  ? 50.361 6.936   36.213  1.00 38.31  ? 64  PHE B CA  1 
ATOM   2718 C  C   . PHE B 1 56  ? 50.877 5.748   35.401  1.00 46.33  ? 64  PHE B C   1 
ATOM   2719 O  O   . PHE B 1 56  ? 51.679 4.958   35.895  1.00 51.58  ? 64  PHE B O   1 
ATOM   2720 C  CB  . PHE B 1 56  ? 51.492 7.766   36.830  1.00 42.06  ? 64  PHE B CB  1 
ATOM   2721 C  CG  . PHE B 1 56  ? 52.439 8.385   35.831  1.00 41.14  ? 64  PHE B CG  1 
ATOM   2722 C  CD1 . PHE B 1 56  ? 52.111 9.556   35.166  1.00 50.03  ? 64  PHE B CD1 1 
ATOM   2723 C  CD2 . PHE B 1 56  ? 53.649 7.779   35.537  1.00 43.16  ? 64  PHE B CD2 1 
ATOM   2724 C  CE1 . PHE B 1 56  ? 52.983 10.117  34.245  1.00 49.17  ? 64  PHE B CE1 1 
ATOM   2725 C  CE2 . PHE B 1 56  ? 54.518 8.338   34.614  1.00 46.32  ? 64  PHE B CE2 1 
ATOM   2726 C  CZ  . PHE B 1 56  ? 54.183 9.506   33.969  1.00 44.98  ? 64  PHE B CZ  1 
ATOM   2727 N  N   . ASP B 1 57  ? 50.390 5.634   34.157  1.00 43.90  ? 65  ASP B N   1 
ATOM   2728 C  CA  . ASP B 1 57  ? 50.735 4.548   33.247  1.00 48.36  ? 65  ASP B CA  1 
ATOM   2729 C  C   . ASP B 1 57  ? 49.994 3.272   33.649  1.00 44.17  ? 65  ASP B C   1 
ATOM   2730 O  O   . ASP B 1 57  ? 49.463 3.188   34.753  1.00 43.44  ? 65  ASP B O   1 
ATOM   2731 C  CB  . ASP B 1 57  ? 52.250 4.336   33.169  1.00 46.93  ? 65  ASP B CB  1 
ATOM   2732 C  CG  . ASP B 1 57  ? 52.957 5.314   32.244  1.00 57.20  ? 65  ASP B CG  1 
ATOM   2733 O  OD1 . ASP B 1 57  ? 52.255 6.064   31.534  1.00 51.81  ? 65  ASP B OD1 1 
ATOM   2734 O  OD2 . ASP B 1 57  ? 54.205 5.319   32.241  1.00 59.32  ? 65  ASP B OD2 1 
ATOM   2735 N  N   . THR B 1 58  ? 49.964 2.283   32.742  1.00 46.12  ? 66  THR B N   1 
ATOM   2736 C  CA  . THR B 1 58  ? 49.157 1.086   32.937  1.00 44.69  ? 66  THR B CA  1 
ATOM   2737 C  C   . THR B 1 58  ? 49.875 -0.177  32.454  1.00 44.83  ? 66  THR B C   1 
ATOM   2738 O  O   . THR B 1 58  ? 49.260 -1.239  32.386  1.00 52.16  ? 66  THR B O   1 
ATOM   2739 C  CB  . THR B 1 58  ? 47.806 1.207   32.219  1.00 43.03  ? 66  THR B CB  1 
ATOM   2740 O  OG1 . THR B 1 58  ? 48.044 1.175   30.811  1.00 46.54  ? 66  THR B OG1 1 
ATOM   2741 C  CG2 . THR B 1 58  ? 47.049 2.466   32.582  1.00 44.07  ? 66  THR B CG2 1 
ATOM   2742 N  N   . SER B 1 59  ? 51.168 -0.065  32.121  1.00 43.74  ? 67  SER B N   1 
ATOM   2743 C  CA  . SER B 1 59  ? 51.981 -1.213  31.739  1.00 55.17  ? 67  SER B CA  1 
ATOM   2744 C  C   . SER B 1 59  ? 51.408 -1.900  30.498  1.00 57.81  ? 67  SER B C   1 
ATOM   2745 O  O   . SER B 1 59  ? 50.720 -1.268  29.701  1.00 54.67  ? 67  SER B O   1 
ATOM   2746 C  CB  . SER B 1 59  ? 52.126 -2.182  32.887  1.00 54.69  ? 67  SER B CB  1 
ATOM   2747 O  OG  . SER B 1 59  ? 50.891 -2.821  33.175  1.00 56.11  ? 67  SER B OG  1 
ATOM   2748 N  N   . CYS B 1 60  ? 51.715 -3.196  30.337  1.00 56.05  ? 68  CYS B N   1 
ATOM   2749 C  CA  . CYS B 1 60  ? 51.307 -3.958  29.164  1.00 49.74  ? 68  CYS B CA  1 
ATOM   2750 C  C   . CYS B 1 60  ? 50.032 -4.742  29.466  1.00 46.10  ? 68  CYS B C   1 
ATOM   2751 O  O   . CYS B 1 60  ? 49.751 -5.050  30.621  1.00 52.49  ? 68  CYS B O   1 
ATOM   2752 C  CB  . CYS B 1 60  ? 52.396 -4.931  28.724  1.00 44.25  ? 68  CYS B CB  1 
ATOM   2753 S  SG  . CYS B 1 60  ? 54.052 -4.198  28.662  1.00 50.37  ? 68  CYS B SG  1 
ATOM   2754 N  N   . ASN B 1 61  ? 49.265 -5.064  28.417  1.00 46.37  ? 69  ASN B N   1 
ATOM   2755 C  CA  . ASN B 1 61  ? 48.058 -5.859  28.573  1.00 52.21  ? 69  ASN B CA  1 
ATOM   2756 C  C   . ASN B 1 61  ? 48.458 -7.308  28.840  1.00 56.42  ? 69  ASN B C   1 
ATOM   2757 O  O   . ASN B 1 61  ? 49.414 -7.810  28.254  1.00 53.32  ? 69  ASN B O   1 
ATOM   2758 C  CB  . ASN B 1 61  ? 47.141 -5.773  27.350  1.00 51.77  ? 69  ASN B CB  1 
ATOM   2759 C  CG  . ASN B 1 61  ? 45.740 -6.278  27.628  1.00 54.23  ? 69  ASN B CG  1 
ATOM   2760 O  OD1 . ASN B 1 61  ? 44.908 -5.553  28.170  1.00 55.03  ? 69  ASN B OD1 1 
ATOM   2761 N  ND2 . ASN B 1 61  ? 45.462 -7.513  27.242  1.00 49.56  ? 69  ASN B ND2 1 
ATOM   2762 N  N   . PRO B 1 62  ? 47.754 -8.017  29.751  1.00 61.54  ? 70  PRO B N   1 
ATOM   2763 C  CA  . PRO B 1 62  ? 48.019 -9.436  29.999  1.00 62.76  ? 70  PRO B CA  1 
ATOM   2764 C  C   . PRO B 1 62  ? 48.119 -10.311 28.748  1.00 59.86  ? 70  PRO B C   1 
ATOM   2765 O  O   . PRO B 1 62  ? 48.875 -11.281 28.736  1.00 62.40  ? 70  PRO B O   1 
ATOM   2766 C  CB  . PRO B 1 62  ? 46.812 -9.845  30.858  1.00 64.18  ? 70  PRO B CB  1 
ATOM   2767 C  CG  . PRO B 1 62  ? 46.489 -8.588  31.638  1.00 66.67  ? 70  PRO B CG  1 
ATOM   2768 C  CD  . PRO B 1 62  ? 46.714 -7.471  30.640  1.00 66.99  ? 70  PRO B CD  1 
ATOM   2769 N  N   . ASN B 1 63  ? 47.365 -9.966  27.696  1.00 62.15  ? 71  ASN B N   1 
ATOM   2770 C  CA  . ASN B 1 63  ? 47.302 -10.784 26.493  1.00 61.61  ? 71  ASN B CA  1 
ATOM   2771 C  C   . ASN B 1 63  ? 48.218 -10.224 25.409  1.00 54.53  ? 71  ASN B C   1 
ATOM   2772 O  O   . ASN B 1 63  ? 47.927 -10.364 24.224  1.00 57.59  ? 71  ASN B O   1 
ATOM   2773 C  CB  . ASN B 1 63  ? 45.892 -10.857 25.903  1.00 69.72  ? 71  ASN B CB  1 
ATOM   2774 C  CG  . ASN B 1 63  ? 44.839 -11.241 26.919  1.00 91.70  ? 71  ASN B CG  1 
ATOM   2775 O  OD1 . ASN B 1 63  ? 44.847 -12.353 27.441  1.00 100.72 ? 71  ASN B OD1 1 
ATOM   2776 N  ND2 . ASN B 1 63  ? 43.924 -10.326 27.198  1.00 94.24  ? 71  ASN B ND2 1 
ATOM   2777 N  N   . SER B 1 64  ? 49.322 -9.597  25.818  1.00 57.69  ? 72  SER B N   1 
ATOM   2778 C  CA  . SER B 1 64  ? 50.230 -8.976  24.869  1.00 58.58  ? 72  SER B CA  1 
ATOM   2779 C  C   . SER B 1 64  ? 51.027 -10.042 24.122  1.00 60.24  ? 72  SER B C   1 
ATOM   2780 O  O   . SER B 1 64  ? 51.133 -9.994  22.898  1.00 60.95  ? 72  SER B O   1 
ATOM   2781 C  CB  . SER B 1 64  ? 51.136 -7.992  25.560  1.00 56.59  ? 72  SER B CB  1 
ATOM   2782 O  OG  . SER B 1 64  ? 50.389 -6.900  26.077  1.00 59.49  ? 72  SER B OG  1 
ATOM   2783 N  N   . MET B 1 65  ? 51.562 -11.014 24.870  1.00 57.40  ? 73  MET B N   1 
ATOM   2784 C  CA  . MET B 1 65  ? 52.584 -11.914 24.359  1.00 61.42  ? 73  MET B CA  1 
ATOM   2785 C  C   . MET B 1 65  ? 51.972 -13.262 23.983  1.00 67.77  ? 73  MET B C   1 
ATOM   2786 O  O   . MET B 1 65  ? 50.879 -13.600 24.432  1.00 60.26  ? 73  MET B O   1 
ATOM   2787 C  CB  . MET B 1 65  ? 53.665 -12.135 25.422  1.00 60.44  ? 73  MET B CB  1 
ATOM   2788 C  CG  . MET B 1 65  ? 54.489 -10.894 25.705  1.00 57.82  ? 73  MET B CG  1 
ATOM   2789 S  SD  . MET B 1 65  ? 55.566 -10.417 24.328  1.00 58.89  ? 73  MET B SD  1 
ATOM   2790 C  CE  . MET B 1 65  ? 56.672 -11.825 24.257  1.00 63.89  ? 73  MET B CE  1 
ATOM   2791 N  N   . GLY B 1 66  ? 52.697 -14.021 23.151  1.00 78.24  ? 74  GLY B N   1 
ATOM   2792 C  CA  . GLY B 1 66  ? 52.351 -15.401 22.845  1.00 87.53  ? 74  GLY B CA  1 
ATOM   2793 C  C   . GLY B 1 66  ? 51.586 -15.540 21.529  1.00 85.69  ? 74  GLY B C   1 
ATOM   2794 O  O   . GLY B 1 66  ? 51.199 -14.544 20.922  1.00 77.66  ? 74  GLY B O   1 
ATOM   2795 N  N   . PRO B 1 67  ? 51.345 -16.784 21.053  1.00 81.53  ? 75  PRO B N   1 
ATOM   2796 C  CA  . PRO B 1 67  ? 50.670 -17.015 19.773  1.00 80.87  ? 75  PRO B CA  1 
ATOM   2797 C  C   . PRO B 1 67  ? 49.284 -16.381 19.629  1.00 69.75  ? 75  PRO B C   1 
ATOM   2798 O  O   . PRO B 1 67  ? 48.906 -15.989 18.528  1.00 59.88  ? 75  PRO B O   1 
ATOM   2799 C  CB  . PRO B 1 67  ? 50.578 -18.548 19.678  1.00 91.19  ? 75  PRO B CB  1 
ATOM   2800 C  CG  . PRO B 1 67  ? 50.787 -19.040 21.097  1.00 91.95  ? 75  PRO B CG  1 
ATOM   2801 C  CD  . PRO B 1 67  ? 51.743 -18.038 21.709  1.00 83.55  ? 75  PRO B CD  1 
ATOM   2802 N  N   . GLN B 1 68  ? 48.523 -16.285 20.727  1.00 67.80  ? 76  GLN B N   1 
ATOM   2803 C  CA  . GLN B 1 68  ? 47.233 -15.609 20.687  1.00 73.10  ? 76  GLN B CA  1 
ATOM   2804 C  C   . GLN B 1 68  ? 47.373 -14.173 21.191  1.00 75.47  ? 76  GLN B C   1 
ATOM   2805 O  O   . GLN B 1 68  ? 46.379 -13.538 21.536  1.00 60.68  ? 76  GLN B O   1 
ATOM   2806 C  CB  . GLN B 1 68  ? 46.177 -16.332 21.528  1.00 81.38  ? 76  GLN B CB  1 
ATOM   2807 C  CG  . GLN B 1 68  ? 45.423 -17.419 20.776  1.00 96.11  ? 76  GLN B CG  1 
ATOM   2808 C  CD  . GLN B 1 68  ? 46.207 -18.705 20.695  1.00 102.89 ? 76  GLN B CD  1 
ATOM   2809 O  OE1 . GLN B 1 68  ? 46.528 -19.323 21.708  1.00 108.43 ? 76  GLN B OE1 1 
ATOM   2810 N  NE2 . GLN B 1 68  ? 46.523 -19.121 19.480  1.00 95.28  ? 76  GLN B NE2 1 
ATOM   2811 N  N   . GLY B 1 69  ? 48.609 -13.667 21.223  1.00 70.46  ? 77  GLY B N   1 
ATOM   2812 C  CA  . GLY B 1 69  ? 48.881 -12.342 21.755  1.00 72.39  ? 77  GLY B CA  1 
ATOM   2813 C  C   . GLY B 1 69  ? 48.367 -11.228 20.845  1.00 65.04  ? 77  GLY B C   1 
ATOM   2814 O  O   . GLY B 1 69  ? 48.344 -11.370 19.624  1.00 68.27  ? 77  GLY B O   1 
ATOM   2815 N  N   . ARG B 1 70  ? 47.963 -10.118 21.473  1.00 56.09  ? 78  ARG B N   1 
ATOM   2816 C  CA  . ARG B 1 70  ? 47.531 -8.917  20.778  1.00 56.02  ? 78  ARG B CA  1 
ATOM   2817 C  C   . ARG B 1 70  ? 48.695 -8.308  20.001  1.00 53.08  ? 78  ARG B C   1 
ATOM   2818 O  O   . ARG B 1 70  ? 48.504 -7.763  18.916  1.00 60.28  ? 78  ARG B O   1 
ATOM   2819 C  CB  . ARG B 1 70  ? 46.995 -7.888  21.778  1.00 54.78  ? 78  ARG B CB  1 
ATOM   2820 C  CG  . ARG B 1 70  ? 45.673 -8.263  22.432  1.00 52.25  ? 78  ARG B CG  1 
ATOM   2821 C  CD  . ARG B 1 70  ? 45.126 -7.075  23.199  1.00 53.24  ? 78  ARG B CD  1 
ATOM   2822 N  NE  . ARG B 1 70  ? 43.883 -7.340  23.908  1.00 52.98  ? 78  ARG B NE  1 
ATOM   2823 C  CZ  . ARG B 1 70  ? 43.263 -6.452  24.676  1.00 59.34  ? 78  ARG B CZ  1 
ATOM   2824 N  NH1 . ARG B 1 70  ? 43.796 -5.258  24.864  1.00 63.73  ? 78  ARG B NH1 1 
ATOM   2825 N  NH2 . ARG B 1 70  ? 42.117 -6.760  25.258  1.00 57.05  ? 78  ARG B NH2 1 
ATOM   2826 N  N   . TRP B 1 71  ? 49.898 -8.382  20.578  1.00 55.51  ? 79  TRP B N   1 
ATOM   2827 C  CA  . TRP B 1 71  ? 51.089 -7.859  19.930  1.00 54.42  ? 79  TRP B CA  1 
ATOM   2828 C  C   . TRP B 1 71  ? 51.410 -8.695  18.694  1.00 56.57  ? 79  TRP B C   1 
ATOM   2829 O  O   . TRP B 1 71  ? 51.342 -9.922  18.736  1.00 66.02  ? 79  TRP B O   1 
ATOM   2830 C  CB  . TRP B 1 71  ? 52.278 -7.852  20.903  1.00 54.15  ? 79  TRP B CB  1 
ATOM   2831 C  CG  . TRP B 1 71  ? 52.144 -6.901  22.064  1.00 53.68  ? 79  TRP B CG  1 
ATOM   2832 C  CD1 . TRP B 1 71  ? 51.036 -6.203  22.448  1.00 53.09  ? 79  TRP B CD1 1 
ATOM   2833 C  CD2 . TRP B 1 71  ? 53.188 -6.535  22.994  1.00 49.40  ? 79  TRP B CD2 1 
ATOM   2834 N  NE1 . TRP B 1 71  ? 51.312 -5.440  23.552  1.00 56.04  ? 79  TRP B NE1 1 
ATOM   2835 C  CE2 . TRP B 1 71  ? 52.623 -5.619  23.908  1.00 54.78  ? 79  TRP B CE2 1 
ATOM   2836 C  CE3 . TRP B 1 71  ? 54.533 -6.892  23.143  1.00 54.18  ? 79  TRP B CE3 1 
ATOM   2837 C  CZ2 . TRP B 1 71  ? 53.360 -5.060  24.950  1.00 53.15  ? 79  TRP B CZ2 1 
ATOM   2838 C  CZ3 . TRP B 1 71  ? 55.260 -6.337  24.173  1.00 55.17  ? 79  TRP B CZ3 1 
ATOM   2839 C  CH2 . TRP B 1 71  ? 54.680 -5.434  25.063  1.00 54.34  ? 79  TRP B CH2 1 
ATOM   2840 N  N   . ALA B 1 72  ? 51.757 -8.017  17.595  1.00 59.99  ? 80  ALA B N   1 
ATOM   2841 C  CA  . ALA B 1 72  ? 52.233 -8.688  16.397  1.00 59.53  ? 80  ALA B CA  1 
ATOM   2842 C  C   . ALA B 1 72  ? 53.513 -9.450  16.732  1.00 64.43  ? 80  ALA B C   1 
ATOM   2843 O  O   . ALA B 1 72  ? 54.200 -9.117  17.695  1.00 70.15  ? 80  ALA B O   1 
ATOM   2844 C  CB  . ALA B 1 72  ? 52.453 -7.678  15.297  1.00 61.26  ? 80  ALA B CB  1 
ATOM   2845 N  N   . GLU B 1 73  ? 53.826 -10.471 15.926  1.00 59.50  ? 81  GLU B N   1 
ATOM   2846 C  CA  . GLU B 1 73  ? 54.922 -11.381 16.220  1.00 60.90  ? 81  GLU B CA  1 
ATOM   2847 C  C   . GLU B 1 73  ? 56.254 -10.635 16.130  1.00 58.60  ? 81  GLU B C   1 
ATOM   2848 O  O   . GLU B 1 73  ? 57.139 -10.856 16.953  1.00 62.08  ? 81  GLU B O   1 
ATOM   2849 C  CB  . GLU B 1 73  ? 54.845 -12.597 15.290  1.00 69.58  ? 81  GLU B CB  1 
ATOM   2850 C  CG  . GLU B 1 73  ? 55.926 -13.641 15.526  1.00 78.11  ? 81  GLU B CG  1 
ATOM   2851 C  CD  . GLU B 1 73  ? 56.021 -14.175 16.946  1.00 91.19  ? 81  GLU B CD  1 
ATOM   2852 O  OE1 . GLU B 1 73  ? 54.968 -14.526 17.518  1.00 87.09  ? 81  GLU B OE1 1 
ATOM   2853 O  OE2 . GLU B 1 73  ? 57.152 -14.259 17.469  1.00 86.74  ? 81  GLU B OE2 1 
ATOM   2854 N  N   . SER B 1 74  ? 56.390 -9.747  15.137  1.00 56.84  ? 82  SER B N   1 
ATOM   2855 C  CA  . SER B 1 74  ? 57.588 -8.932  14.999  1.00 60.71  ? 82  SER B CA  1 
ATOM   2856 C  C   . SER B 1 74  ? 57.796 -8.081  16.250  1.00 59.59  ? 82  SER B C   1 
ATOM   2857 O  O   . SER B 1 74  ? 58.922 -7.916  16.712  1.00 61.59  ? 82  SER B O   1 
ATOM   2858 C  CB  . SER B 1 74  ? 57.525 -8.068  13.765  1.00 63.20  ? 82  SER B CB  1 
ATOM   2859 O  OG  . SER B 1 74  ? 56.440 -7.155  13.841  1.00 69.38  ? 82  SER B OG  1 
ATOM   2860 N  N   . THR B 1 75  ? 56.698 -7.535  16.786  1.00 63.55  ? 83  THR B N   1 
ATOM   2861 C  CA  . THR B 1 75  ? 56.762 -6.700  17.973  1.00 60.37  ? 83  THR B CA  1 
ATOM   2862 C  C   . THR B 1 75  ? 57.208 -7.550  19.161  1.00 61.21  ? 83  THR B C   1 
ATOM   2863 O  O   . THR B 1 75  ? 58.066 -7.134  19.938  1.00 52.97  ? 83  THR B O   1 
ATOM   2864 C  CB  . THR B 1 75  ? 55.418 -6.004  18.232  1.00 62.82  ? 83  THR B CB  1 
ATOM   2865 O  OG1 . THR B 1 75  ? 54.961 -5.438  17.004  1.00 57.97  ? 83  THR B OG1 1 
ATOM   2866 C  CG2 . THR B 1 75  ? 55.505 -4.922  19.286  1.00 69.92  ? 83  THR B CG2 1 
ATOM   2867 N  N   . GLN B 1 76  ? 56.630 -8.750  19.282  1.00 55.52  ? 84  GLN B N   1 
ATOM   2868 C  CA  . GLN B 1 76  ? 56.916 -9.630  20.404  1.00 59.16  ? 84  GLN B CA  1 
ATOM   2869 C  C   . GLN B 1 76  ? 58.384 -10.053 20.385  1.00 60.83  ? 84  GLN B C   1 
ATOM   2870 O  O   . GLN B 1 76  ? 58.926 -10.451 21.413  1.00 66.52  ? 84  GLN B O   1 
ATOM   2871 C  CB  . GLN B 1 76  ? 56.024 -10.873 20.370  1.00 54.03  ? 84  GLN B CB  1 
ATOM   2872 C  CG  . GLN B 1 76  ? 54.544 -10.583 20.568  1.00 62.49  ? 84  GLN B CG  1 
ATOM   2873 C  CD  . GLN B 1 76  ? 53.765 -11.857 20.787  1.00 65.70  ? 84  GLN B CD  1 
ATOM   2874 O  OE1 . GLN B 1 76  ? 54.305 -12.861 21.245  1.00 57.90  ? 84  GLN B OE1 1 
ATOM   2875 N  NE2 . GLN B 1 76  ? 52.479 -11.819 20.478  1.00 63.62  ? 84  GLN B NE2 1 
ATOM   2876 N  N   . GLN B 1 77  ? 59.023 -9.966  19.215  1.00 58.81  ? 85  GLN B N   1 
ATOM   2877 C  CA  . GLN B 1 77  ? 60.377 -10.470 19.057  1.00 60.45  ? 85  GLN B CA  1 
ATOM   2878 C  C   . GLN B 1 77  ? 61.393 -9.350  19.266  1.00 58.32  ? 85  GLN B C   1 
ATOM   2879 O  O   . GLN B 1 77  ? 62.540 -9.616  19.621  1.00 64.12  ? 85  GLN B O   1 
ATOM   2880 C  CB  . GLN B 1 77  ? 60.554 -11.122 17.684  1.00 70.75  ? 85  GLN B CB  1 
ATOM   2881 C  CG  . GLN B 1 77  ? 59.894 -12.489 17.579  1.00 83.75  ? 85  GLN B CG  1 
ATOM   2882 C  CD  . GLN B 1 77  ? 60.554 -13.361 16.539  1.00 100.16 ? 85  GLN B CD  1 
ATOM   2883 O  OE1 . GLN B 1 77  ? 59.891 -14.008 15.731  1.00 100.26 ? 85  GLN B OE1 1 
ATOM   2884 N  NE2 . GLN B 1 77  ? 61.876 -13.400 16.568  1.00 108.22 ? 85  GLN B NE2 1 
ATOM   2885 N  N   . MET B 1 78  ? 60.969 -8.102  19.045  1.00 57.41  ? 86  MET B N   1 
ATOM   2886 C  CA  . MET B 1 78  ? 61.869 -6.965  19.149  1.00 61.19  ? 86  MET B CA  1 
ATOM   2887 C  C   . MET B 1 78  ? 61.770 -6.343  20.540  1.00 50.16  ? 86  MET B C   1 
ATOM   2888 O  O   . MET B 1 78  ? 62.737 -5.763  21.028  1.00 53.88  ? 86  MET B O   1 
ATOM   2889 C  CB  . MET B 1 78  ? 61.546 -5.906  18.091  1.00 60.21  ? 86  MET B CB  1 
ATOM   2890 C  CG  . MET B 1 78  ? 62.567 -5.836  16.970  1.00 72.34  ? 86  MET B CG  1 
ATOM   2891 S  SD  . MET B 1 78  ? 62.166 -4.568  15.739  1.00 76.80  ? 86  MET B SD  1 
ATOM   2892 C  CE  . MET B 1 78  ? 60.378 -4.689  15.709  1.00 73.58  ? 86  MET B CE  1 
ATOM   2893 N  N   . PHE B 1 79  ? 60.596 -6.469  21.171  1.00 47.99  ? 87  PHE B N   1 
ATOM   2894 C  CA  . PHE B 1 79  ? 60.364 -5.870  22.476  1.00 55.81  ? 87  PHE B CA  1 
ATOM   2895 C  C   . PHE B 1 79  ? 59.650 -6.863  23.392  1.00 53.35  ? 87  PHE B C   1 
ATOM   2896 O  O   . PHE B 1 79  ? 58.585 -6.556  23.923  1.00 58.44  ? 87  PHE B O   1 
ATOM   2897 C  CB  . PHE B 1 79  ? 59.538 -4.588  22.333  1.00 55.48  ? 87  PHE B CB  1 
ATOM   2898 C  CG  . PHE B 1 79  ? 59.999 -3.659  21.238  1.00 63.51  ? 87  PHE B CG  1 
ATOM   2899 C  CD1 . PHE B 1 79  ? 61.115 -2.853  21.405  1.00 69.61  ? 87  PHE B CD1 1 
ATOM   2900 C  CD2 . PHE B 1 79  ? 59.325 -3.607  20.028  1.00 65.66  ? 87  PHE B CD2 1 
ATOM   2901 C  CE1 . PHE B 1 79  ? 61.535 -2.005  20.391  1.00 74.94  ? 87  PHE B CE1 1 
ATOM   2902 C  CE2 . PHE B 1 79  ? 59.749 -2.761  19.015  1.00 73.37  ? 87  PHE B CE2 1 
ATOM   2903 C  CZ  . PHE B 1 79  ? 60.853 -1.962  19.198  1.00 73.31  ? 87  PHE B CZ  1 
ATOM   2904 N  N   . PRO B 1 80  ? 60.220 -8.067  23.632  1.00 57.14  ? 88  PRO B N   1 
ATOM   2905 C  CA  . PRO B 1 80  ? 59.556 -9.090  24.444  1.00 56.13  ? 88  PRO B CA  1 
ATOM   2906 C  C   . PRO B 1 80  ? 59.333 -8.682  25.898  1.00 55.48  ? 88  PRO B C   1 
ATOM   2907 O  O   . PRO B 1 80  ? 60.231 -8.156  26.552  1.00 54.91  ? 88  PRO B O   1 
ATOM   2908 C  CB  . PRO B 1 80  ? 60.521 -10.285 24.384  1.00 56.83  ? 88  PRO B CB  1 
ATOM   2909 C  CG  . PRO B 1 80  ? 61.864 -9.657  24.081  1.00 63.08  ? 88  PRO B CG  1 
ATOM   2910 C  CD  . PRO B 1 80  ? 61.540 -8.504  23.152  1.00 61.23  ? 88  PRO B CD  1 
ATOM   2911 N  N   . TRP B 1 81  ? 58.119 -8.955  26.387  1.00 52.71  ? 89  TRP B N   1 
ATOM   2912 C  CA  . TRP B 1 81  ? 57.726 -8.645  27.751  1.00 55.38  ? 89  TRP B CA  1 
ATOM   2913 C  C   . TRP B 1 81  ? 57.641 -9.933  28.566  1.00 59.95  ? 89  TRP B C   1 
ATOM   2914 O  O   . TRP B 1 81  ? 56.916 -10.855 28.201  1.00 63.09  ? 89  TRP B O   1 
ATOM   2915 C  CB  . TRP B 1 81  ? 56.380 -7.908  27.732  1.00 52.62  ? 89  TRP B CB  1 
ATOM   2916 C  CG  . TRP B 1 81  ? 55.829 -7.553  29.087  1.00 52.44  ? 89  TRP B CG  1 
ATOM   2917 C  CD1 . TRP B 1 81  ? 56.477 -6.932  30.114  1.00 46.85  ? 89  TRP B CD1 1 
ATOM   2918 C  CD2 . TRP B 1 81  ? 54.478 -7.778  29.544  1.00 47.49  ? 89  TRP B CD2 1 
ATOM   2919 N  NE1 . TRP B 1 81  ? 55.632 -6.768  31.179  1.00 47.53  ? 89  TRP B NE1 1 
ATOM   2920 C  CE2 . TRP B 1 81  ? 54.399 -7.273  30.859  1.00 45.89  ? 89  TRP B CE2 1 
ATOM   2921 C  CE3 . TRP B 1 81  ? 53.339 -8.357  28.975  1.00 46.64  ? 89  TRP B CE3 1 
ATOM   2922 C  CZ2 . TRP B 1 81  ? 53.226 -7.331  31.607  1.00 50.73  ? 89  TRP B CZ2 1 
ATOM   2923 C  CZ3 . TRP B 1 81  ? 52.180 -8.414  29.716  1.00 48.69  ? 89  TRP B CZ3 1 
ATOM   2924 C  CH2 . TRP B 1 81  ? 52.125 -7.903  31.013  1.00 50.10  ? 89  TRP B CH2 1 
ATOM   2925 N  N   . THR B 1 82  ? 58.394 -9.987  29.668  1.00 64.98  ? 90  THR B N   1 
ATOM   2926 C  CA  . THR B 1 82  ? 58.336 -11.117 30.580  1.00 64.07  ? 90  THR B CA  1 
ATOM   2927 C  C   . THR B 1 82  ? 57.708 -10.650 31.891  1.00 63.78  ? 90  THR B C   1 
ATOM   2928 O  O   . THR B 1 82  ? 58.176 -9.691  32.499  1.00 65.38  ? 90  THR B O   1 
ATOM   2929 C  CB  . THR B 1 82  ? 59.728 -11.730 30.792  1.00 67.94  ? 90  THR B CB  1 
ATOM   2930 O  OG1 . THR B 1 82  ? 60.547 -10.761 31.446  1.00 79.04  ? 90  THR B OG1 1 
ATOM   2931 C  CG2 . THR B 1 82  ? 60.389 -12.163 29.501  1.00 64.46  ? 90  THR B CG2 1 
ATOM   2932 N  N   . ALA B 1 83  ? 56.635 -11.330 32.312  1.00 59.27  ? 91  ALA B N   1 
ATOM   2933 C  CA  . ALA B 1 83  ? 55.907 -10.935 33.506  1.00 60.69  ? 91  ALA B CA  1 
ATOM   2934 C  C   . ALA B 1 83  ? 55.164 -12.132 34.092  1.00 59.81  ? 91  ALA B C   1 
ATOM   2935 O  O   . ALA B 1 83  ? 54.497 -12.869 33.370  1.00 63.84  ? 91  ALA B O   1 
ATOM   2936 C  CB  . ALA B 1 83  ? 54.953 -9.813  33.174  1.00 65.46  ? 91  ALA B CB  1 
ATOM   2937 N  N   . THR B 1 84  ? 55.285 -12.301 35.412  1.00 64.15  ? 92  THR B N   1 
ATOM   2938 C  CA  . THR B 1 84  ? 54.506 -13.287 36.142  1.00 67.42  ? 92  THR B CA  1 
ATOM   2939 C  C   . THR B 1 84  ? 53.127 -12.692 36.418  1.00 70.05  ? 92  THR B C   1 
ATOM   2940 O  O   . THR B 1 84  ? 52.949 -11.479 36.329  1.00 68.26  ? 92  THR B O   1 
ATOM   2941 C  CB  . THR B 1 84  ? 55.232 -13.707 37.426  1.00 69.96  ? 92  THR B CB  1 
ATOM   2942 O  OG1 . THR B 1 84  ? 55.196 -12.606 38.336  1.00 73.20  ? 92  THR B OG1 1 
ATOM   2943 C  CG2 . THR B 1 84  ? 56.667 -14.122 37.182  1.00 63.70  ? 92  THR B CG2 1 
ATOM   2944 N  N   . GLU B 1 85  ? 52.155 -13.550 36.745  1.00 61.92  ? 93  GLU B N   1 
ATOM   2945 C  CA  . GLU B 1 85  ? 50.791 -13.103 36.978  1.00 75.33  ? 93  GLU B CA  1 
ATOM   2946 C  C   . GLU B 1 85  ? 50.789 -12.014 38.047  1.00 69.01  ? 93  GLU B C   1 
ATOM   2947 O  O   . GLU B 1 85  ? 49.972 -11.097 38.003  1.00 62.11  ? 93  GLU B O   1 
ATOM   2948 C  CB  . GLU B 1 85  ? 49.909 -14.277 37.410  1.00 88.13  ? 93  GLU B CB  1 
ATOM   2949 C  CG  . GLU B 1 85  ? 49.874 -15.420 36.411  1.00 103.47 ? 93  GLU B CG  1 
ATOM   2950 C  CD  . GLU B 1 85  ? 48.679 -15.411 35.474  1.00 113.24 ? 93  GLU B CD  1 
ATOM   2951 O  OE1 . GLU B 1 85  ? 47.538 -15.400 35.979  1.00 102.63 ? 93  GLU B OE1 1 
ATOM   2952 O  OE2 . GLU B 1 85  ? 48.891 -15.429 34.245  1.00 109.87 ? 93  GLU B OE2 1 
ATOM   2953 N  N   . GLU B 1 86  ? 51.713 -12.136 39.006  1.00 64.37  ? 94  GLU B N   1 
ATOM   2954 C  CA  . GLU B 1 86  ? 51.830 -11.203 40.116  1.00 72.67  ? 94  GLU B CA  1 
ATOM   2955 C  C   . GLU B 1 86  ? 52.154 -9.806  39.589  1.00 65.64  ? 94  GLU B C   1 
ATOM   2956 O  O   . GLU B 1 86  ? 51.791 -8.809  40.209  1.00 53.29  ? 94  GLU B O   1 
ATOM   2957 C  CB  . GLU B 1 86  ? 52.893 -11.715 41.093  1.00 79.34  ? 94  GLU B CB  1 
ATOM   2958 C  CG  . GLU B 1 86  ? 53.521 -10.638 41.963  1.00 106.37 ? 94  GLU B CG  1 
ATOM   2959 C  CD  . GLU B 1 86  ? 54.738 -11.098 42.752  1.00 109.19 ? 94  GLU B CD  1 
ATOM   2960 O  OE1 . GLU B 1 86  ? 55.003 -12.317 42.767  1.00 101.29 ? 94  GLU B OE1 1 
ATOM   2961 O  OE2 . GLU B 1 86  ? 55.426 -10.237 43.341  1.00 90.55  ? 94  GLU B OE2 1 
ATOM   2962 N  N   . CYS B 1 87  ? 52.824 -9.747  38.431  1.00 57.41  ? 95  CYS B N   1 
ATOM   2963 C  CA  . CYS B 1 87  ? 53.315 -8.493  37.880  1.00 57.94  ? 95  CYS B CA  1 
ATOM   2964 C  C   . CYS B 1 87  ? 52.220 -7.766  37.097  1.00 57.26  ? 95  CYS B C   1 
ATOM   2965 O  O   . CYS B 1 87  ? 52.362 -6.584  36.793  1.00 59.53  ? 95  CYS B O   1 
ATOM   2966 C  CB  . CYS B 1 87  ? 54.535 -8.723  36.994  1.00 54.47  ? 95  CYS B CB  1 
ATOM   2967 S  SG  . CYS B 1 87  ? 56.058 -9.043  37.924  1.00 61.49  ? 95  CYS B SG  1 
ATOM   2968 N  N   . TYR B 1 88  ? 51.125 -8.467  36.778  1.00 55.57  ? 96  TYR B N   1 
ATOM   2969 C  CA  . TYR B 1 88  ? 50.001 -7.845  36.093  1.00 55.84  ? 96  TYR B CA  1 
ATOM   2970 C  C   . TYR B 1 88  ? 49.439 -6.737  36.979  1.00 56.01  ? 96  TYR B C   1 
ATOM   2971 O  O   . TYR B 1 88  ? 49.396 -6.877  38.199  1.00 65.70  ? 96  TYR B O   1 
ATOM   2972 C  CB  . TYR B 1 88  ? 48.909 -8.864  35.751  1.00 63.53  ? 96  TYR B CB  1 
ATOM   2973 C  CG  . TYR B 1 88  ? 49.329 -9.968  34.789  1.00 66.03  ? 96  TYR B CG  1 
ATOM   2974 C  CD1 . TYR B 1 88  ? 50.490 -9.865  34.034  1.00 67.28  ? 96  TYR B CD1 1 
ATOM   2975 C  CD2 . TYR B 1 88  ? 48.568 -11.123 34.652  1.00 67.28  ? 96  TYR B CD2 1 
ATOM   2976 C  CE1 . TYR B 1 88  ? 50.876 -10.871 33.163  1.00 65.69  ? 96  TYR B CE1 1 
ATOM   2977 C  CE2 . TYR B 1 88  ? 48.944 -12.137 33.786  1.00 69.59  ? 96  TYR B CE2 1 
ATOM   2978 C  CZ  . TYR B 1 88  ? 50.101 -12.010 33.040  1.00 62.71  ? 96  TYR B CZ  1 
ATOM   2979 O  OH  . TYR B 1 88  ? 50.480 -13.003 32.185  1.00 66.37  ? 96  TYR B OH  1 
ATOM   2980 N  N   . LEU B 1 89  ? 48.993 -5.643  36.350  1.00 53.31  ? 97  LEU B N   1 
ATOM   2981 C  CA  . LEU B 1 89  ? 48.596 -4.447  37.075  1.00 56.01  ? 97  LEU B CA  1 
ATOM   2982 C  C   . LEU B 1 89  ? 47.346 -4.713  37.912  1.00 48.70  ? 97  LEU B C   1 
ATOM   2983 O  O   . LEU B 1 89  ? 47.238 -4.213  39.028  1.00 57.86  ? 97  LEU B O   1 
ATOM   2984 C  CB  . LEU B 1 89  ? 48.366 -3.301  36.084  1.00 50.35  ? 97  LEU B CB  1 
ATOM   2985 C  CG  . LEU B 1 89  ? 47.802 -2.013  36.684  1.00 58.28  ? 97  LEU B CG  1 
ATOM   2986 C  CD1 . LEU B 1 89  ? 48.828 -1.325  37.575  1.00 57.29  ? 97  LEU B CD1 1 
ATOM   2987 C  CD2 . LEU B 1 89  ? 47.330 -1.065  35.592  1.00 54.06  ? 97  LEU B CD2 1 
ATOM   2988 N  N   A HIS B 1 90  ? 46.401 -5.480  37.355  0.50 56.49  ? 98  HIS B N   1 
ATOM   2989 N  N   B HIS B 1 90  ? 46.417 -5.512  37.374  0.50 54.10  ? 98  HIS B N   1 
ATOM   2990 C  CA  A HIS B 1 90  ? 45.167 -5.801  38.056  0.50 60.66  ? 98  HIS B CA  1 
ATOM   2991 C  CA  B HIS B 1 90  ? 45.165 -5.782  38.063  0.50 55.62  ? 98  HIS B CA  1 
ATOM   2992 C  C   A HIS B 1 90  ? 45.491 -6.496  39.375  0.50 51.42  ? 98  HIS B C   1 
ATOM   2993 C  C   B HIS B 1 90  ? 45.449 -6.541  39.358  0.50 48.79  ? 98  HIS B C   1 
ATOM   2994 O  O   A HIS B 1 90  ? 44.862 -6.222  40.395  0.50 54.50  ? 98  HIS B O   1 
ATOM   2995 O  O   B HIS B 1 90  ? 44.752 -6.351  40.353  0.50 52.94  ? 98  HIS B O   1 
ATOM   2996 C  CB  A HIS B 1 90  ? 44.247 -6.675  37.197  0.50 66.50  ? 98  HIS B CB  1 
ATOM   2997 C  CB  B HIS B 1 90  ? 44.162 -6.492  37.144  0.50 56.26  ? 98  HIS B CB  1 
ATOM   2998 C  CG  A HIS B 1 90  ? 43.236 -7.430  37.997  0.50 80.11  ? 98  HIS B CG  1 
ATOM   2999 C  CG  B HIS B 1 90  ? 44.454 -7.931  36.868  0.50 64.55  ? 98  HIS B CG  1 
ATOM   3000 N  ND1 A HIS B 1 90  ? 42.220 -6.823  38.704  0.50 81.54  ? 98  HIS B ND1 1 
ATOM   3001 N  ND1 B HIS B 1 90  ? 45.527 -8.361  36.118  0.50 70.34  ? 98  HIS B ND1 1 
ATOM   3002 C  CD2 A HIS B 1 90  ? 43.097 -8.746  38.206  0.50 83.72  ? 98  HIS B CD2 1 
ATOM   3003 C  CD2 B HIS B 1 90  ? 43.785 -9.037  37.223  0.50 63.24  ? 98  HIS B CD2 1 
ATOM   3004 C  CE1 A HIS B 1 90  ? 41.496 -7.752  39.313  0.50 83.56  ? 98  HIS B CE1 1 
ATOM   3005 C  CE1 B HIS B 1 90  ? 45.505 -9.684  36.042  0.50 67.47  ? 98  HIS B CE1 1 
ATOM   3006 N  NE2 A HIS B 1 90  ? 42.012 -8.927  39.025  0.50 85.10  ? 98  HIS B NE2 1 
ATOM   3007 N  NE2 B HIS B 1 90  ? 44.456 -10.116 36.707  0.50 58.87  ? 98  HIS B NE2 1 
ATOM   3008 N  N   . ASN B 1 91  ? 46.480 -7.394  39.339  1.00 48.10  ? 99  ASN B N   1 
ATOM   3009 C  CA  . ASN B 1 91  ? 46.853 -8.169  40.511  1.00 58.54  ? 99  ASN B CA  1 
ATOM   3010 C  C   . ASN B 1 91  ? 47.622 -7.283  41.489  1.00 59.90  ? 99  ASN B C   1 
ATOM   3011 O  O   . ASN B 1 91  ? 47.373 -7.326  42.691  1.00 55.16  ? 99  ASN B O   1 
ATOM   3012 C  CB  . ASN B 1 91  ? 47.634 -9.433  40.138  1.00 61.69  ? 99  ASN B CB  1 
ATOM   3013 C  CG  . ASN B 1 91  ? 46.815 -10.405 39.315  1.00 59.58  ? 99  ASN B CG  1 
ATOM   3014 O  OD1 . ASN B 1 91  ? 45.607 -10.527 39.511  1.00 69.89  ? 99  ASN B OD1 1 
ATOM   3015 N  ND2 . ASN B 1 91  ? 47.455 -11.088 38.380  1.00 71.49  ? 99  ASN B ND2 1 
ATOM   3016 N  N   . ARG B 1 92  ? 48.554 -6.478  40.964  1.00 55.09  ? 100 ARG B N   1 
ATOM   3017 C  CA  . ARG B 1 92  ? 49.317 -5.551  41.785  1.00 58.11  ? 100 ARG B CA  1 
ATOM   3018 C  C   . ARG B 1 92  ? 48.364 -4.633  42.547  1.00 49.69  ? 100 ARG B C   1 
ATOM   3019 O  O   . ARG B 1 92  ? 48.623 -4.281  43.694  1.00 57.18  ? 100 ARG B O   1 
ATOM   3020 C  CB  . ARG B 1 92  ? 50.279 -4.734  40.918  1.00 52.95  ? 100 ARG B CB  1 
ATOM   3021 C  CG  . ARG B 1 92  ? 51.471 -5.523  40.397  1.00 56.51  ? 100 ARG B CG  1 
ATOM   3022 C  CD  . ARG B 1 92  ? 52.511 -5.766  41.475  1.00 53.17  ? 100 ARG B CD  1 
ATOM   3023 N  NE  . ARG B 1 92  ? 53.699 -6.424  40.948  1.00 59.54  ? 100 ARG B NE  1 
ATOM   3024 C  CZ  . ARG B 1 92  ? 54.407 -7.341  41.597  1.00 55.05  ? 100 ARG B CZ  1 
ATOM   3025 N  NH1 . ARG B 1 92  ? 54.110 -7.646  42.847  1.00 61.47  ? 100 ARG B NH1 1 
ATOM   3026 N  NH2 . ARG B 1 92  ? 55.431 -7.928  41.001  1.00 54.49  ? 100 ARG B NH2 1 
ATOM   3027 N  N   . LEU B 1 93  ? 47.259 -4.253  41.896  1.00 52.49  ? 101 LEU B N   1 
ATOM   3028 C  CA  . LEU B 1 93  ? 46.279 -3.364  42.499  1.00 58.83  ? 101 LEU B CA  1 
ATOM   3029 C  C   . LEU B 1 93  ? 45.435 -4.133  43.512  1.00 53.51  ? 101 LEU B C   1 
ATOM   3030 O  O   . LEU B 1 93  ? 45.100 -3.610  44.572  1.00 56.66  ? 101 LEU B O   1 
ATOM   3031 C  CB  . LEU B 1 93  ? 45.404 -2.761  41.395  1.00 52.21  ? 101 LEU B CB  1 
ATOM   3032 C  CG  . LEU B 1 93  ? 46.051 -1.642  40.579  1.00 52.87  ? 101 LEU B CG  1 
ATOM   3033 C  CD1 . LEU B 1 93  ? 45.175 -1.258  39.397  1.00 52.01  ? 101 LEU B CD1 1 
ATOM   3034 C  CD2 . LEU B 1 93  ? 46.325 -0.424  41.449  1.00 49.53  ? 101 LEU B CD2 1 
ATOM   3035 N  N   . GLU B 1 94  ? 45.089 -5.377  43.167  1.00 53.79  ? 102 GLU B N   1 
ATOM   3036 C  CA  . GLU B 1 94  ? 44.300 -6.226  44.043  1.00 65.95  ? 102 GLU B CA  1 
ATOM   3037 C  C   . GLU B 1 94  ? 45.054 -6.430  45.355  1.00 57.47  ? 102 GLU B C   1 
ATOM   3038 O  O   . GLU B 1 94  ? 44.449 -6.456  46.424  1.00 53.09  ? 102 GLU B O   1 
ATOM   3039 C  CB  . GLU B 1 94  ? 44.005 -7.562  43.358  1.00 71.66  ? 102 GLU B CB  1 
ATOM   3040 C  CG  . GLU B 1 94  ? 42.880 -8.348  44.007  1.00 80.42  ? 102 GLU B CG  1 
ATOM   3041 C  CD  . GLU B 1 94  ? 42.543 -9.651  43.303  1.00 99.37  ? 102 GLU B CD  1 
ATOM   3042 O  OE1 . GLU B 1 94  ? 41.714 -10.414 43.838  1.00 117.20 ? 102 GLU B OE1 1 
ATOM   3043 O  OE2 . GLU B 1 94  ? 43.106 -9.898  42.217  1.00 106.86 ? 102 GLU B OE2 1 
ATOM   3044 N  N   . GLN B 1 95  ? 46.383 -6.563  45.260  1.00 48.59  ? 103 GLN B N   1 
ATOM   3045 C  CA  . GLN B 1 95  ? 47.212 -6.788  46.432  1.00 52.46  ? 103 GLN B CA  1 
ATOM   3046 C  C   . GLN B 1 95  ? 47.229 -5.535  47.304  1.00 55.87  ? 103 GLN B C   1 
ATOM   3047 O  O   . GLN B 1 95  ? 47.685 -5.583  48.443  1.00 63.90  ? 103 GLN B O   1 
ATOM   3048 C  CB  . GLN B 1 95  ? 48.628 -7.207  46.028  1.00 56.19  ? 103 GLN B CB  1 
ATOM   3049 C  CG  . GLN B 1 95  ? 48.740 -8.682  45.664  1.00 60.71  ? 103 GLN B CG  1 
ATOM   3050 C  CD  . GLN B 1 95  ? 48.183 -9.577  46.745  1.00 74.76  ? 103 GLN B CD  1 
ATOM   3051 O  OE1 . GLN B 1 95  ? 48.655 -9.585  47.881  1.00 65.04  ? 103 GLN B OE1 1 
ATOM   3052 N  NE2 . GLN B 1 95  ? 47.163 -10.342 46.396  1.00 65.90  ? 103 GLN B NE2 1 
ATOM   3053 N  N   . LEU B 1 96  ? 46.726 -4.420  46.764  1.00 53.04  ? 104 LEU B N   1 
ATOM   3054 C  CA  . LEU B 1 96  ? 46.612 -3.188  47.528  1.00 51.51  ? 104 LEU B CA  1 
ATOM   3055 C  C   . LEU B 1 96  ? 45.145 -2.930  47.855  1.00 51.00  ? 104 LEU B C   1 
ATOM   3056 O  O   . LEU B 1 96  ? 44.793 -1.854  48.336  1.00 54.47  ? 104 LEU B O   1 
ATOM   3057 C  CB  . LEU B 1 96  ? 47.207 -2.031  46.719  1.00 49.21  ? 104 LEU B CB  1 
ATOM   3058 C  CG  . LEU B 1 96  ? 48.680 -2.185  46.342  1.00 54.53  ? 104 LEU B CG  1 
ATOM   3059 C  CD1 . LEU B 1 96  ? 49.166 -0.990  45.535  1.00 57.93  ? 104 LEU B CD1 1 
ATOM   3060 C  CD2 . LEU B 1 96  ? 49.537 -2.372  47.584  1.00 57.61  ? 104 LEU B CD2 1 
ATOM   3061 N  N   . LYS B 1 97  ? 44.297 -3.931  47.591  1.00 55.31  ? 105 LYS B N   1 
ATOM   3062 C  CA  . LYS B 1 97  ? 42.870 -3.814  47.842  1.00 66.49  ? 105 LYS B CA  1 
ATOM   3063 C  C   . LYS B 1 97  ? 42.323 -2.636  47.039  1.00 59.95  ? 105 LYS B C   1 
ATOM   3064 O  O   . LYS B 1 97  ? 41.508 -1.860  47.535  1.00 50.90  ? 105 LYS B O   1 
ATOM   3065 C  CB  . LYS B 1 97  ? 42.616 -3.639  49.343  1.00 77.68  ? 105 LYS B CB  1 
ATOM   3066 C  CG  . LYS B 1 97  ? 43.273 -4.689  50.230  1.00 94.78  ? 105 LYS B CG  1 
ATOM   3067 C  CD  . LYS B 1 97  ? 43.657 -4.173  51.604  1.00 113.57 ? 105 LYS B CD  1 
ATOM   3068 C  CE  . LYS B 1 97  ? 44.657 -5.060  52.317  1.00 119.24 ? 105 LYS B CE  1 
ATOM   3069 N  NZ  . LYS B 1 97  ? 46.026 -4.897  51.771  1.00 119.46 ? 105 LYS B NZ  1 
ATOM   3070 N  N   . VAL B 1 98  ? 42.792 -2.511  45.793  1.00 60.60  ? 106 VAL B N   1 
ATOM   3071 C  CA  . VAL B 1 98  ? 42.343 -1.454  44.902  1.00 61.57  ? 106 VAL B CA  1 
ATOM   3072 C  C   . VAL B 1 98  ? 41.714 -2.099  43.672  1.00 52.77  ? 106 VAL B C   1 
ATOM   3073 O  O   . VAL B 1 98  ? 42.362 -2.880  42.979  1.00 58.82  ? 106 VAL B O   1 
ATOM   3074 C  CB  . VAL B 1 98  ? 43.496 -0.511  44.504  1.00 65.12  ? 106 VAL B CB  1 
ATOM   3075 C  CG1 . VAL B 1 98  ? 43.056 0.512   43.467  1.00 65.57  ? 106 VAL B CG1 1 
ATOM   3076 C  CG2 . VAL B 1 98  ? 44.106 0.184   45.712  1.00 62.78  ? 106 VAL B CG2 1 
ATOM   3077 N  N   . ARG B 1 99  ? 40.444 -1.769  43.419  1.00 57.82  ? 107 ARG B N   1 
ATOM   3078 C  CA  . ARG B 1 99  ? 39.759 -2.243  42.229  1.00 70.92  ? 107 ARG B CA  1 
ATOM   3079 C  C   . ARG B 1 99  ? 39.873 -1.190  41.131  1.00 55.15  ? 107 ARG B C   1 
ATOM   3080 O  O   . ARG B 1 99  ? 39.914 0.006   41.411  1.00 51.20  ? 107 ARG B O   1 
ATOM   3081 C  CB  . ARG B 1 99  ? 38.293 -2.573  42.529  1.00 79.15  ? 107 ARG B CB  1 
ATOM   3082 C  CG  . ARG B 1 99  ? 38.121 -3.791  43.425  1.00 94.89  ? 107 ARG B CG  1 
ATOM   3083 C  CD  . ARG B 1 99  ? 37.064 -4.763  42.931  1.00 104.38 ? 107 ARG B CD  1 
ATOM   3084 N  NE  . ARG B 1 99  ? 36.869 -4.742  41.485  1.00 127.65 ? 107 ARG B NE  1 
ATOM   3085 C  CZ  . ARG B 1 99  ? 37.429 -5.588  40.624  1.00 119.63 ? 107 ARG B CZ  1 
ATOM   3086 N  NH1 . ARG B 1 99  ? 38.454 -6.337  40.992  1.00 120.20 ? 107 ARG B NH1 1 
ATOM   3087 N  NH2 . ARG B 1 99  ? 36.997 -5.636  39.375  1.00 93.91  ? 107 ARG B NH2 1 
ATOM   3088 N  N   . PRO B 1 100 ? 39.937 -1.607  39.848  1.00 62.21  ? 108 PRO B N   1 
ATOM   3089 C  CA  . PRO B 1 100 ? 39.976 -0.661  38.733  1.00 60.87  ? 108 PRO B CA  1 
ATOM   3090 C  C   . PRO B 1 100 ? 38.977 0.483   38.889  1.00 58.77  ? 108 PRO B C   1 
ATOM   3091 O  O   . PRO B 1 100 ? 39.272 1.620   38.532  1.00 59.41  ? 108 PRO B O   1 
ATOM   3092 C  CB  . PRO B 1 100 ? 39.618 -1.547  37.532  1.00 61.73  ? 108 PRO B CB  1 
ATOM   3093 C  CG  . PRO B 1 100 ? 40.185 -2.903  37.904  1.00 69.02  ? 108 PRO B CG  1 
ATOM   3094 C  CD  . PRO B 1 100 ? 39.986 -3.009  39.403  1.00 57.56  ? 108 PRO B CD  1 
ATOM   3095 N  N   . GLU B 1 101 ? 37.801 0.165   39.443  1.00 55.76  ? 109 GLU B N   1 
ATOM   3096 C  CA  . GLU B 1 101 ? 36.702 1.113   39.533  1.00 55.51  ? 109 GLU B CA  1 
ATOM   3097 C  C   . GLU B 1 101 ? 37.033 2.227   40.522  1.00 50.78  ? 109 GLU B C   1 
ATOM   3098 O  O   . GLU B 1 101 ? 36.339 3.240   40.564  1.00 51.94  ? 109 GLU B O   1 
ATOM   3099 C  CB  . GLU B 1 101 ? 35.413 0.417   39.978  1.00 72.40  ? 109 GLU B CB  1 
ATOM   3100 C  CG  . GLU B 1 101 ? 35.102 -0.855  39.211  1.00 91.85  ? 109 GLU B CG  1 
ATOM   3101 C  CD  . GLU B 1 101 ? 35.716 -2.112  39.800  1.00 95.93  ? 109 GLU B CD  1 
ATOM   3102 O  OE1 . GLU B 1 101 ? 36.596 -2.704  39.143  1.00 77.42  ? 109 GLU B OE1 1 
ATOM   3103 O  OE2 . GLU B 1 101 ? 35.304 -2.501  40.913  1.00 101.54 ? 109 GLU B OE2 1 
ATOM   3104 N  N   . ASP B 1 102 ? 38.082 2.026   41.327  1.00 54.97  ? 110 ASP B N   1 
ATOM   3105 C  CA  . ASP B 1 102 ? 38.405 2.953   42.399  1.00 60.21  ? 110 ASP B CA  1 
ATOM   3106 C  C   . ASP B 1 102 ? 39.342 4.044   41.884  1.00 56.14  ? 110 ASP B C   1 
ATOM   3107 O  O   . ASP B 1 102 ? 39.679 4.968   42.621  1.00 58.65  ? 110 ASP B O   1 
ATOM   3108 C  CB  . ASP B 1 102 ? 39.024 2.221   43.595  1.00 68.51  ? 110 ASP B CB  1 
ATOM   3109 C  CG  . ASP B 1 102 ? 38.178 1.076   44.128  1.00 78.49  ? 110 ASP B CG  1 
ATOM   3110 O  OD1 . ASP B 1 102 ? 36.969 1.045   43.821  1.00 82.68  ? 110 ASP B OD1 1 
ATOM   3111 O  OD2 . ASP B 1 102 ? 38.743 0.213   44.831  1.00 62.65  ? 110 ASP B OD2 1 
ATOM   3112 N  N   . ILE B 1 103 ? 39.757 3.935   40.617  1.00 55.75  ? 111 ILE B N   1 
ATOM   3113 C  CA  . ILE B 1 103 ? 40.681 4.894   40.032  1.00 56.45  ? 111 ILE B CA  1 
ATOM   3114 C  C   . ILE B 1 103 ? 39.889 6.060   39.443  1.00 46.01  ? 111 ILE B C   1 
ATOM   3115 O  O   . ILE B 1 103 ? 39.086 5.875   38.530  1.00 52.82  ? 111 ILE B O   1 
ATOM   3116 C  CB  . ILE B 1 103 ? 41.582 4.220   38.976  1.00 51.18  ? 111 ILE B CB  1 
ATOM   3117 C  CG1 . ILE B 1 103 ? 42.212 2.928   39.505  1.00 52.38  ? 111 ILE B CG1 1 
ATOM   3118 C  CG2 . ILE B 1 103 ? 42.638 5.192   38.471  1.00 60.77  ? 111 ILE B CG2 1 
ATOM   3119 C  CD1 . ILE B 1 103 ? 43.206 3.140   40.623  1.00 45.44  ? 111 ILE B CD1 1 
ATOM   3120 N  N   . ARG B 1 104 ? 40.122 7.261   39.985  1.00 47.84  ? 112 ARG B N   1 
ATOM   3121 C  CA  . ARG B 1 104 ? 39.477 8.471   39.500  1.00 51.28  ? 112 ARG B CA  1 
ATOM   3122 C  C   . ARG B 1 104 ? 40.162 8.963   38.226  1.00 54.11  ? 112 ARG B C   1 
ATOM   3123 O  O   . ARG B 1 104 ? 39.491 9.390   37.289  1.00 50.13  ? 112 ARG B O   1 
ATOM   3124 C  CB  . ARG B 1 104 ? 39.516 9.562   40.576  1.00 53.09  ? 112 ARG B CB  1 
ATOM   3125 C  CG  . ARG B 1 104 ? 38.754 10.826  40.204  1.00 60.79  ? 112 ARG B CG  1 
ATOM   3126 C  CD  . ARG B 1 104 ? 38.865 11.902  41.266  1.00 65.56  ? 112 ARG B CD  1 
ATOM   3127 N  NE  . ARG B 1 104 ? 37.969 13.021  41.013  1.00 76.44  ? 112 ARG B NE  1 
ATOM   3128 C  CZ  . ARG B 1 104 ? 38.109 14.229  41.546  1.00 76.83  ? 112 ARG B CZ  1 
ATOM   3129 N  NH1 . ARG B 1 104 ? 39.148 14.494  42.319  1.00 76.80  ? 112 ARG B NH1 1 
ATOM   3130 N  NH2 . ARG B 1 104 ? 37.222 15.175  41.287  1.00 81.55  ? 112 ARG B NH2 1 
ATOM   3131 N  N   . TYR B 1 105 ? 41.501 8.909   38.202  1.00 50.58  ? 113 TYR B N   1 
ATOM   3132 C  CA  . TYR B 1 105 ? 42.274 9.467   37.103  1.00 53.71  ? 113 TYR B CA  1 
ATOM   3133 C  C   . TYR B 1 105 ? 43.371 8.500   36.671  1.00 43.24  ? 113 TYR B C   1 
ATOM   3134 O  O   . TYR B 1 105 ? 44.117 7.989   37.502  1.00 43.59  ? 113 TYR B O   1 
ATOM   3135 C  CB  . TYR B 1 105 ? 42.947 10.787  37.489  1.00 49.24  ? 113 TYR B CB  1 
ATOM   3136 C  CG  . TYR B 1 105 ? 41.997 11.949  37.740  1.00 49.62  ? 113 TYR B CG  1 
ATOM   3137 C  CD1 . TYR B 1 105 ? 41.137 12.399  36.747  1.00 52.45  ? 113 TYR B CD1 1 
ATOM   3138 C  CD2 . TYR B 1 105 ? 41.971 12.603  38.965  1.00 49.12  ? 113 TYR B CD2 1 
ATOM   3139 C  CE1 . TYR B 1 105 ? 40.274 13.460  36.966  1.00 49.10  ? 113 TYR B CE1 1 
ATOM   3140 C  CE2 . TYR B 1 105 ? 41.114 13.665  39.198  1.00 53.53  ? 113 TYR B CE2 1 
ATOM   3141 C  CZ  . TYR B 1 105 ? 40.263 14.095  38.195  1.00 54.42  ? 113 TYR B CZ  1 
ATOM   3142 O  OH  . TYR B 1 105 ? 39.416 15.141  38.419  1.00 61.73  ? 113 TYR B OH  1 
ATOM   3143 N  N   . VAL B 1 106 ? 43.469 8.277   35.357  1.00 44.81  ? 114 VAL B N   1 
ATOM   3144 C  CA  . VAL B 1 106 ? 44.618 7.607   34.774  1.00 44.04  ? 114 VAL B CA  1 
ATOM   3145 C  C   . VAL B 1 106 ? 45.381 8.622   33.927  1.00 45.76  ? 114 VAL B C   1 
ATOM   3146 O  O   . VAL B 1 106 ? 44.803 9.253   33.046  1.00 48.74  ? 114 VAL B O   1 
ATOM   3147 C  CB  . VAL B 1 106 ? 44.204 6.385   33.931  1.00 46.51  ? 114 VAL B CB  1 
ATOM   3148 C  CG1 . VAL B 1 106 ? 45.418 5.644   33.393  1.00 51.52  ? 114 VAL B CG1 1 
ATOM   3149 C  CG2 . VAL B 1 106 ? 43.300 5.438   34.705  1.00 51.32  ? 114 VAL B CG2 1 
ATOM   3150 N  N   . VAL B 1 107 ? 46.678 8.781   34.212  1.00 44.30  ? 115 VAL B N   1 
ATOM   3151 C  CA  . VAL B 1 107 ? 47.537 9.625   33.399  1.00 42.95  ? 115 VAL B CA  1 
ATOM   3152 C  C   . VAL B 1 107 ? 48.382 8.741   32.484  1.00 43.32  ? 115 VAL B C   1 
ATOM   3153 O  O   . VAL B 1 107 ? 49.253 8.009   32.947  1.00 49.06  ? 115 VAL B O   1 
ATOM   3154 C  CB  . VAL B 1 107 ? 48.423 10.539  34.265  1.00 42.54  ? 115 VAL B CB  1 
ATOM   3155 C  CG1 . VAL B 1 107 ? 49.398 11.341  33.415  1.00 39.44  ? 115 VAL B CG1 1 
ATOM   3156 C  CG2 . VAL B 1 107 ? 47.591 11.463  35.144  1.00 44.68  ? 115 VAL B CG2 1 
ATOM   3157 N  N   . ALA B 1 108 ? 48.111 8.831   31.178  1.00 48.66  ? 116 ALA B N   1 
ATOM   3158 C  CA  . ALA B 1 108 ? 48.869 8.116   30.165  1.00 45.58  ? 116 ALA B CA  1 
ATOM   3159 C  C   . ALA B 1 108 ? 50.041 8.971   29.686  1.00 43.98  ? 116 ALA B C   1 
ATOM   3160 O  O   . ALA B 1 108 ? 49.850 9.903   28.908  1.00 55.79  ? 116 ALA B O   1 
ATOM   3161 C  CB  . ALA B 1 108 ? 47.953 7.760   29.019  1.00 43.10  ? 116 ALA B CB  1 
ATOM   3162 N  N   . SER B 1 109 ? 51.255 8.642   30.144  1.00 42.84  ? 117 SER B N   1 
ATOM   3163 C  CA  . SER B 1 109 ? 52.447 9.376   29.747  1.00 41.21  ? 117 SER B CA  1 
ATOM   3164 C  C   . SER B 1 109 ? 52.494 9.488   28.225  1.00 43.03  ? 117 SER B C   1 
ATOM   3165 O  O   . SER B 1 109 ? 52.806 10.542  27.677  1.00 43.19  ? 117 SER B O   1 
ATOM   3166 C  CB  . SER B 1 109 ? 53.698 8.723   30.287  1.00 46.30  ? 117 SER B CB  1 
ATOM   3167 O  OG  . SER B 1 109 ? 53.878 7.424   29.740  1.00 45.98  ? 117 SER B OG  1 
ATOM   3168 N  N   . HIS B 1 110 ? 52.197 8.362   27.570  1.00 40.14  ? 118 HIS B N   1 
ATOM   3169 C  CA  . HIS B 1 110 ? 52.057 8.262   26.127  1.00 38.45  ? 118 HIS B CA  1 
ATOM   3170 C  C   . HIS B 1 110 ? 51.357 6.929   25.871  1.00 43.46  ? 118 HIS B C   1 
ATOM   3171 O  O   . HIS B 1 110 ? 51.059 6.210   26.823  1.00 44.74  ? 118 HIS B O   1 
ATOM   3172 C  CB  . HIS B 1 110 ? 53.406 8.484   25.427  1.00 38.53  ? 118 HIS B CB  1 
ATOM   3173 C  CG  . HIS B 1 110 ? 54.462 7.474   25.727  1.00 42.37  ? 118 HIS B CG  1 
ATOM   3174 N  ND1 . HIS B 1 110 ? 54.819 7.093   27.003  1.00 47.15  ? 118 HIS B ND1 1 
ATOM   3175 C  CD2 . HIS B 1 110 ? 55.250 6.775   24.899  1.00 42.80  ? 118 HIS B CD2 1 
ATOM   3176 C  CE1 . HIS B 1 110 ? 55.790 6.192   26.934  1.00 47.91  ? 118 HIS B CE1 1 
ATOM   3177 N  NE2 . HIS B 1 110 ? 56.066 5.984   25.666  1.00 48.09  ? 118 HIS B NE2 1 
ATOM   3178 N  N   . LEU B 1 111 ? 51.071 6.600   24.607  1.00 38.91  ? 119 LEU B N   1 
ATOM   3179 C  CA  . LEU B 1 111 ? 50.184 5.482   24.328  1.00 38.92  ? 119 LEU B CA  1 
ATOM   3180 C  C   . LEU B 1 111 ? 50.947 4.313   23.708  1.00 36.15  ? 119 LEU B C   1 
ATOM   3181 O  O   . LEU B 1 111 ? 50.361 3.485   23.014  1.00 43.73  ? 119 LEU B O   1 
ATOM   3182 C  CB  . LEU B 1 111 ? 49.047 5.973   23.426  1.00 41.54  ? 119 LEU B CB  1 
ATOM   3183 C  CG  . LEU B 1 111 ? 48.041 6.894   24.115  1.00 42.07  ? 119 LEU B CG  1 
ATOM   3184 C  CD1 . LEU B 1 111 ? 47.008 7.416   23.130  1.00 44.83  ? 119 LEU B CD1 1 
ATOM   3185 C  CD2 . LEU B 1 111 ? 47.358 6.179   25.273  1.00 42.50  ? 119 LEU B CD2 1 
ATOM   3186 N  N   . HIS B 1 112 ? 52.251 4.236   23.993  1.00 37.07  ? 120 HIS B N   1 
ATOM   3187 C  CA  . HIS B 1 112 ? 53.059 3.086   23.619  1.00 39.97  ? 120 HIS B CA  1 
ATOM   3188 C  C   . HIS B 1 112 ? 52.529 1.827   24.305  1.00 43.85  ? 120 HIS B C   1 
ATOM   3189 O  O   . HIS B 1 112 ? 51.809 1.910   25.297  1.00 44.16  ? 120 HIS B O   1 
ATOM   3190 C  CB  . HIS B 1 112 ? 54.535 3.331   23.955  1.00 41.62  ? 120 HIS B CB  1 
ATOM   3191 C  CG  . HIS B 1 112 ? 55.275 4.101   22.913  1.00 39.15  ? 120 HIS B CG  1 
ATOM   3192 N  ND1 . HIS B 1 112 ? 56.483 4.716   23.163  1.00 41.15  ? 120 HIS B ND1 1 
ATOM   3193 C  CD2 . HIS B 1 112 ? 54.982 4.367   21.633  1.00 48.08  ? 120 HIS B CD2 1 
ATOM   3194 C  CE1 . HIS B 1 112 ? 56.899 5.324   22.061  1.00 46.99  ? 120 HIS B CE1 1 
ATOM   3195 N  NE2 . HIS B 1 112 ? 56.003 5.123   21.118  1.00 47.00  ? 120 HIS B NE2 1 
ATOM   3196 N  N   . LEU B 1 113 ? 52.927 0.664   23.769  1.00 46.21  ? 121 LEU B N   1 
ATOM   3197 C  CA  . LEU B 1 113 ? 52.358 -0.624  24.136  1.00 51.01  ? 121 LEU B CA  1 
ATOM   3198 C  C   . LEU B 1 113 ? 52.634 -0.969  25.600  1.00 47.67  ? 121 LEU B C   1 
ATOM   3199 O  O   . LEU B 1 113 ? 51.897 -1.751  26.196  1.00 48.86  ? 121 LEU B O   1 
ATOM   3200 C  CB  . LEU B 1 113 ? 52.926 -1.706  23.208  1.00 49.06  ? 121 LEU B CB  1 
ATOM   3201 C  CG  . LEU B 1 113 ? 54.414 -2.027  23.357  1.00 52.35  ? 121 LEU B CG  1 
ATOM   3202 C  CD1 . LEU B 1 113 ? 54.790 -3.218  22.487  1.00 48.05  ? 121 LEU B CD1 1 
ATOM   3203 C  CD2 . LEU B 1 113 ? 55.286 -0.829  23.004  1.00 48.89  ? 121 LEU B CD2 1 
ATOM   3204 N  N   . ASN B 1 114 ? 53.692 -0.388  26.174  1.00 50.83  ? 122 ASN B N   1 
ATOM   3205 C  CA  . ASN B 1 114 ? 54.157 -0.794  27.490  1.00 47.32  ? 122 ASN B CA  1 
ATOM   3206 C  C   . ASN B 1 114 ? 53.774 0.259   28.528  1.00 50.54  ? 122 ASN B C   1 
ATOM   3207 O  O   . ASN B 1 114 ? 54.273 0.232   29.651  1.00 54.47  ? 122 ASN B O   1 
ATOM   3208 C  CB  . ASN B 1 114 ? 55.663 -1.080  27.481  1.00 53.33  ? 122 ASN B CB  1 
ATOM   3209 C  CG  . ASN B 1 114 ? 56.496 0.111   27.055  1.00 51.17  ? 122 ASN B CG  1 
ATOM   3210 O  OD1 . ASN B 1 114 ? 57.467 0.465   27.720  1.00 61.97  ? 122 ASN B OD1 1 
ATOM   3211 N  ND2 . ASN B 1 114 ? 56.138 0.724   25.940  1.00 59.10  ? 122 ASN B ND2 1 
ATOM   3212 N  N   . HIS B 1 115 ? 52.876 1.177   28.149  1.00 48.07  ? 123 HIS B N   1 
ATOM   3213 C  CA  . HIS B 1 115 ? 52.401 2.194   29.074  1.00 43.95  ? 123 HIS B CA  1 
ATOM   3214 C  C   . HIS B 1 115 ? 50.876 2.277   29.061  1.00 40.67  ? 123 HIS B C   1 
ATOM   3215 O  O   . HIS B 1 115 ? 50.280 2.679   30.057  1.00 45.30  ? 123 HIS B O   1 
ATOM   3216 C  CB  . HIS B 1 115 ? 53.052 3.551   28.780  1.00 43.21  ? 123 HIS B CB  1 
ATOM   3217 C  CG  . HIS B 1 115 ? 54.542 3.530   28.862  1.00 43.41  ? 123 HIS B CG  1 
ATOM   3218 N  ND1 . HIS B 1 115 ? 55.244 4.074   29.915  1.00 36.38  ? 123 HIS B ND1 1 
ATOM   3219 C  CD2 . HIS B 1 115 ? 55.459 3.007   28.036  1.00 48.55  ? 123 HIS B CD2 1 
ATOM   3220 C  CE1 . HIS B 1 115 ? 56.543 3.893   29.715  1.00 46.22  ? 123 HIS B CE1 1 
ATOM   3221 N  NE2 . HIS B 1 115 ? 56.696 3.248   28.578  1.00 46.61  ? 123 HIS B NE2 1 
ATOM   3222 N  N   . ALA B 1 116 ? 50.247 1.893   27.941  1.00 47.51  ? 124 ALA B N   1 
ATOM   3223 C  CA  . ALA B 1 116 ? 48.808 2.051   27.781  1.00 47.80  ? 124 ALA B CA  1 
ATOM   3224 C  C   . ALA B 1 116 ? 48.111 0.692   27.701  1.00 47.68  ? 124 ALA B C   1 
ATOM   3225 O  O   . ALA B 1 116 ? 46.930 0.618   27.366  1.00 45.31  ? 124 ALA B O   1 
ATOM   3226 C  CB  . ALA B 1 116 ? 48.521 2.877   26.550  1.00 47.03  ? 124 ALA B CB  1 
ATOM   3227 N  N   . GLY B 1 117 ? 48.849 -0.374  28.026  1.00 48.16  ? 125 GLY B N   1 
ATOM   3228 C  CA  . GLY B 1 117 ? 48.370 -1.739  27.864  1.00 47.27  ? 125 GLY B CA  1 
ATOM   3229 C  C   . GLY B 1 117 ? 47.017 -1.997  28.527  1.00 47.48  ? 125 GLY B C   1 
ATOM   3230 O  O   . GLY B 1 117 ? 46.188 -2.712  27.968  1.00 50.14  ? 125 GLY B O   1 
ATOM   3231 N  N   . CYS B 1 118 ? 46.797 -1.427  29.719  1.00 47.76  ? 126 CYS B N   1 
ATOM   3232 C  CA  . CYS B 1 118 ? 45.639 -1.791  30.523  1.00 47.71  ? 126 CYS B CA  1 
ATOM   3233 C  C   . CYS B 1 118 ? 44.683 -0.617  30.730  1.00 45.66  ? 126 CYS B C   1 
ATOM   3234 O  O   . CYS B 1 118 ? 43.854 -0.661  31.636  1.00 45.20  ? 126 CYS B O   1 
ATOM   3235 C  CB  . CYS B 1 118 ? 46.064 -2.322  31.888  1.00 53.32  ? 126 CYS B CB  1 
ATOM   3236 S  SG  . CYS B 1 118 ? 47.115 -3.796  31.799  1.00 54.48  ? 126 CYS B SG  1 
ATOM   3237 N  N   . LEU B 1 119 ? 44.777 0.422   29.893  1.00 45.24  ? 127 LEU B N   1 
ATOM   3238 C  CA  . LEU B 1 119 ? 43.849 1.539   29.989  1.00 43.82  ? 127 LEU B CA  1 
ATOM   3239 C  C   . LEU B 1 119 ? 42.413 1.021   30.011  1.00 41.56  ? 127 LEU B C   1 
ATOM   3240 O  O   . LEU B 1 119 ? 41.550 1.618   30.648  1.00 46.44  ? 127 LEU B O   1 
ATOM   3241 C  CB  . LEU B 1 119 ? 44.049 2.495   28.808  1.00 47.93  ? 127 LEU B CB  1 
ATOM   3242 C  CG  . LEU B 1 119 ? 45.237 3.452   28.902  1.00 52.02  ? 127 LEU B CG  1 
ATOM   3243 C  CD1 . LEU B 1 119 ? 45.326 4.311   27.651  1.00 60.41  ? 127 LEU B CD1 1 
ATOM   3244 C  CD2 . LEU B 1 119 ? 45.138 4.334   30.138  1.00 52.67  ? 127 LEU B CD2 1 
ATOM   3245 N  N   . GLU B 1 120 ? 42.164 -0.089  29.306  1.00 48.52  ? 128 GLU B N   1 
ATOM   3246 C  CA  . GLU B 1 120 ? 40.808 -0.557  29.060  1.00 57.62  ? 128 GLU B CA  1 
ATOM   3247 C  C   . GLU B 1 120 ? 40.104 -0.921  30.367  1.00 53.60  ? 128 GLU B C   1 
ATOM   3248 O  O   . GLU B 1 120 ? 38.876 -0.963  30.409  1.00 54.80  ? 128 GLU B O   1 
ATOM   3249 C  CB  . GLU B 1 120 ? 40.810 -1.742  28.089  1.00 57.20  ? 128 GLU B CB  1 
ATOM   3250 C  CG  . GLU B 1 120 ? 41.516 -2.980  28.608  1.00 59.76  ? 128 GLU B CG  1 
ATOM   3251 C  CD  . GLU B 1 120 ? 41.716 -4.049  27.547  1.00 62.54  ? 128 GLU B CD  1 
ATOM   3252 O  OE1 . GLU B 1 120 ? 40.985 -5.061  27.579  1.00 64.22  ? 128 GLU B OE1 1 
ATOM   3253 O  OE2 . GLU B 1 120 ? 42.603 -3.867  26.691  1.00 63.97  ? 128 GLU B OE2 1 
ATOM   3254 N  N   . MET B 1 121 ? 40.873 -1.168  31.434  1.00 50.67  ? 129 MET B N   1 
ATOM   3255 C  CA  . MET B 1 121 ? 40.306 -1.642  32.688  1.00 48.70  ? 129 MET B CA  1 
ATOM   3256 C  C   . MET B 1 121 ? 39.612 -0.494  33.419  1.00 50.62  ? 129 MET B C   1 
ATOM   3257 O  O   . MET B 1 121 ? 38.688 -0.718  34.196  1.00 49.62  ? 129 MET B O   1 
ATOM   3258 C  CB  . MET B 1 121 ? 41.389 -2.207  33.616  1.00 56.83  ? 129 MET B CB  1 
ATOM   3259 C  CG  . MET B 1 121 ? 42.220 -3.314  32.998  1.00 66.59  ? 129 MET B CG  1 
ATOM   3260 S  SD  . MET B 1 121 ? 43.510 -3.925  34.123  1.00 73.41  ? 129 MET B SD  1 
ATOM   3261 C  CE  . MET B 1 121 ? 43.034 -3.121  35.653  1.00 75.69  ? 129 MET B CE  1 
ATOM   3262 N  N   . PHE B 1 122 ? 40.080 0.735   33.179  1.00 50.18  ? 130 PHE B N   1 
ATOM   3263 C  CA  . PHE B 1 122 ? 39.689 1.874   33.993  1.00 45.69  ? 130 PHE B CA  1 
ATOM   3264 C  C   . PHE B 1 122 ? 38.520 2.596   33.331  1.00 49.42  ? 130 PHE B C   1 
ATOM   3265 O  O   . PHE B 1 122 ? 38.682 3.663   32.743  1.00 64.41  ? 130 PHE B O   1 
ATOM   3266 C  CB  . PHE B 1 122 ? 40.926 2.735   34.251  1.00 46.40  ? 130 PHE B CB  1 
ATOM   3267 C  CG  . PHE B 1 122 ? 42.066 1.916   34.795  1.00 50.74  ? 130 PHE B CG  1 
ATOM   3268 C  CD1 . PHE B 1 122 ? 42.004 1.392   36.075  1.00 52.65  ? 130 PHE B CD1 1 
ATOM   3269 C  CD2 . PHE B 1 122 ? 43.152 1.590   34.000  1.00 56.44  ? 130 PHE B CD2 1 
ATOM   3270 C  CE1 . PHE B 1 122 ? 43.032 0.605   36.568  1.00 49.72  ? 130 PHE B CE1 1 
ATOM   3271 C  CE2 . PHE B 1 122 ? 44.179 0.803   34.494  1.00 57.80  ? 130 PHE B CE2 1 
ATOM   3272 C  CZ  . PHE B 1 122 ? 44.117 0.313   35.777  1.00 53.11  ? 130 PHE B CZ  1 
ATOM   3273 N  N   . THR B 1 123 ? 37.336 1.991   33.470  1.00 48.14  ? 131 THR B N   1 
ATOM   3274 C  CA  . THR B 1 123 ? 36.133 2.438   32.791  1.00 52.89  ? 131 THR B CA  1 
ATOM   3275 C  C   . THR B 1 123 ? 35.406 3.492   33.622  1.00 49.74  ? 131 THR B C   1 
ATOM   3276 O  O   . THR B 1 123 ? 34.490 4.144   33.127  1.00 60.52  ? 131 THR B O   1 
ATOM   3277 C  CB  . THR B 1 123 ? 35.212 1.247   32.497  1.00 57.90  ? 131 THR B CB  1 
ATOM   3278 O  OG1 . THR B 1 123 ? 34.960 0.578   33.733  1.00 58.84  ? 131 THR B OG1 1 
ATOM   3279 C  CG2 . THR B 1 123 ? 35.806 0.273   31.504  1.00 53.27  ? 131 THR B CG2 1 
ATOM   3280 N  N   . ASN B 1 124 ? 35.815 3.656   34.885  1.00 51.96  ? 132 ASN B N   1 
ATOM   3281 C  CA  . ASN B 1 124 ? 35.173 4.622   35.762  1.00 58.20  ? 132 ASN B CA  1 
ATOM   3282 C  C   . ASN B 1 124 ? 36.118 5.798   36.002  1.00 55.12  ? 132 ASN B C   1 
ATOM   3283 O  O   . ASN B 1 124 ? 35.862 6.646   36.855  1.00 50.93  ? 132 ASN B O   1 
ATOM   3284 C  CB  . ASN B 1 124 ? 34.713 3.975   37.072  1.00 66.07  ? 132 ASN B CB  1 
ATOM   3285 C  CG  . ASN B 1 124 ? 33.650 4.789   37.780  1.00 75.65  ? 132 ASN B CG  1 
ATOM   3286 O  OD1 . ASN B 1 124 ? 33.673 4.921   39.002  1.00 90.64  ? 132 ASN B OD1 1 
ATOM   3287 N  ND2 . ASN B 1 124 ? 32.710 5.328   37.020  1.00 84.67  ? 132 ASN B ND2 1 
ATOM   3288 N  N   . ALA B 1 125 ? 37.199 5.854   35.218  1.00 56.37  ? 133 ALA B N   1 
ATOM   3289 C  CA  . ALA B 1 125 ? 38.215 6.879   35.382  1.00 53.25  ? 133 ALA B CA  1 
ATOM   3290 C  C   . ALA B 1 125 ? 38.135 7.887   34.240  1.00 54.39  ? 133 ALA B C   1 
ATOM   3291 O  O   . ALA B 1 125 ? 37.527 7.621   33.206  1.00 51.65  ? 133 ALA B O   1 
ATOM   3292 C  CB  . ALA B 1 125 ? 39.580 6.236   35.442  1.00 49.97  ? 133 ALA B CB  1 
ATOM   3293 N  N   . THR B 1 126 ? 38.756 9.050   34.457  1.00 51.18  ? 134 THR B N   1 
ATOM   3294 C  CA  . THR B 1 126 ? 39.032 10.001  33.393  1.00 49.30  ? 134 THR B CA  1 
ATOM   3295 C  C   . THR B 1 126 ? 40.464 9.769   32.919  1.00 47.93  ? 134 THR B C   1 
ATOM   3296 O  O   . THR B 1 126 ? 41.401 9.890   33.704  1.00 54.71  ? 134 THR B O   1 
ATOM   3297 C  CB  . THR B 1 126 ? 38.795 11.438  33.876  1.00 49.52  ? 134 THR B CB  1 
ATOM   3298 O  OG1 . THR B 1 126 ? 37.403 11.590  34.160  1.00 52.38  ? 134 THR B OG1 1 
ATOM   3299 C  CG2 . THR B 1 126 ? 39.222 12.483  32.869  1.00 52.72  ? 134 THR B CG2 1 
ATOM   3300 N  N   . ILE B 1 127 ? 40.625 9.403   31.642  1.00 46.37  ? 135 ILE B N   1 
ATOM   3301 C  CA  . ILE B 1 127 ? 41.941 9.108   31.100  1.00 45.14  ? 135 ILE B CA  1 
ATOM   3302 C  C   . ILE B 1 127 ? 42.547 10.397  30.559  1.00 49.94  ? 135 ILE B C   1 
ATOM   3303 O  O   . ILE B 1 127 ? 42.029 10.988  29.614  1.00 44.98  ? 135 ILE B O   1 
ATOM   3304 C  CB  . ILE B 1 127 ? 41.884 8.025   30.006  1.00 52.71  ? 135 ILE B CB  1 
ATOM   3305 C  CG1 . ILE B 1 127 ? 40.892 6.910   30.345  1.00 51.93  ? 135 ILE B CG1 1 
ATOM   3306 C  CG2 . ILE B 1 127 ? 43.278 7.480   29.733  1.00 53.91  ? 135 ILE B CG2 1 
ATOM   3307 C  CD1 . ILE B 1 127 ? 41.370 5.967   31.423  1.00 53.23  ? 135 ILE B CD1 1 
ATOM   3308 N  N   . ILE B 1 128 ? 43.661 10.809  31.167  1.00 46.08  ? 136 ILE B N   1 
ATOM   3309 C  CA  . ILE B 1 128 ? 44.339 12.028  30.772  1.00 43.81  ? 136 ILE B CA  1 
ATOM   3310 C  C   . ILE B 1 128 ? 45.484 11.660  29.839  1.00 43.84  ? 136 ILE B C   1 
ATOM   3311 O  O   . ILE B 1 128 ? 46.348 10.856  30.182  1.00 42.57  ? 136 ILE B O   1 
ATOM   3312 C  CB  . ILE B 1 128 ? 44.810 12.812  32.009  1.00 47.11  ? 136 ILE B CB  1 
ATOM   3313 C  CG1 . ILE B 1 128 ? 43.633 13.084  32.948  1.00 48.19  ? 136 ILE B CG1 1 
ATOM   3314 C  CG2 . ILE B 1 128 ? 45.525 14.090  31.597  1.00 50.21  ? 136 ILE B CG2 1 
ATOM   3315 C  CD1 . ILE B 1 128 ? 44.027 13.642  34.290  1.00 57.95  ? 136 ILE B CD1 1 
ATOM   3316 N  N   . VAL B 1 129 ? 45.455 12.261  28.648  1.00 44.95  ? 137 VAL B N   1 
ATOM   3317 C  CA  . VAL B 1 129 ? 46.392 11.925  27.595  1.00 40.11  ? 137 VAL B CA  1 
ATOM   3318 C  C   . VAL B 1 129 ? 46.617 13.169  26.747  1.00 41.72  ? 137 VAL B C   1 
ATOM   3319 O  O   . VAL B 1 129 ? 45.726 14.005  26.613  1.00 45.77  ? 137 VAL B O   1 
ATOM   3320 C  CB  . VAL B 1 129 ? 45.872 10.755  26.742  1.00 42.11  ? 137 VAL B CB  1 
ATOM   3321 C  CG1 . VAL B 1 129 ? 44.599 11.125  25.996  1.00 43.50  ? 137 VAL B CG1 1 
ATOM   3322 C  CG2 . VAL B 1 129 ? 46.933 10.251  25.778  1.00 43.26  ? 137 VAL B CG2 1 
ATOM   3323 N  N   . HIS B 1 130 ? 47.825 13.273  26.188  1.00 36.73  ? 138 HIS B N   1 
ATOM   3324 C  CA  . HIS B 1 130 ? 48.155 14.358  25.284  1.00 41.59  ? 138 HIS B CA  1 
ATOM   3325 C  C   . HIS B 1 130 ? 47.333 14.195  24.009  1.00 40.06  ? 138 HIS B C   1 
ATOM   3326 O  O   . HIS B 1 130 ? 47.220 13.091  23.482  1.00 43.33  ? 138 HIS B O   1 
ATOM   3327 C  CB  . HIS B 1 130 ? 49.661 14.374  25.006  1.00 44.57  ? 138 HIS B CB  1 
ATOM   3328 C  CG  . HIS B 1 130 ? 50.130 15.694  24.508  1.00 44.76  ? 138 HIS B CG  1 
ATOM   3329 N  ND1 . HIS B 1 130 ? 49.806 16.175  23.259  1.00 40.80  ? 138 HIS B ND1 1 
ATOM   3330 C  CD2 . HIS B 1 130 ? 50.878 16.637  25.091  1.00 47.53  ? 138 HIS B CD2 1 
ATOM   3331 C  CE1 . HIS B 1 130 ? 50.353 17.371  23.101  1.00 46.08  ? 138 HIS B CE1 1 
ATOM   3332 N  NE2 . HIS B 1 130 ? 51.006 17.672  24.202  1.00 49.94  ? 138 HIS B NE2 1 
ATOM   3333 N  N   . GLU B 1 131 ? 46.770 15.303  23.514  1.00 39.59  ? 139 GLU B N   1 
ATOM   3334 C  CA  . GLU B 1 131 ? 45.853 15.241  22.387  1.00 44.55  ? 139 GLU B CA  1 
ATOM   3335 C  C   . GLU B 1 131 ? 46.589 14.734  21.147  1.00 37.52  ? 139 GLU B C   1 
ATOM   3336 O  O   . GLU B 1 131 ? 46.017 13.983  20.361  1.00 44.50  ? 139 GLU B O   1 
ATOM   3337 C  CB  . GLU B 1 131 ? 45.163 16.590  22.153  1.00 48.27  ? 139 GLU B CB  1 
ATOM   3338 C  CG  . GLU B 1 131 ? 46.029 17.659  21.509  1.00 52.63  ? 139 GLU B CG  1 
ATOM   3339 C  CD  . GLU B 1 131 ? 45.270 18.929  21.156  1.00 60.78  ? 139 GLU B CD  1 
ATOM   3340 O  OE1 . GLU B 1 131 ? 44.021 18.876  21.105  1.00 51.59  ? 139 GLU B OE1 1 
ATOM   3341 O  OE2 . GLU B 1 131 ? 45.924 19.974  20.954  1.00 51.89  ? 139 GLU B OE2 1 
ATOM   3342 N  N   . ASP B 1 132 ? 47.857 15.128  20.977  1.00 35.28  ? 140 ASP B N   1 
ATOM   3343 C  CA  . ASP B 1 132 ? 48.608 14.744  19.792  1.00 37.49  ? 140 ASP B CA  1 
ATOM   3344 C  C   . ASP B 1 132 ? 48.935 13.254  19.850  1.00 36.97  ? 140 ASP B C   1 
ATOM   3345 O  O   . ASP B 1 132 ? 48.998 12.593  18.817  1.00 41.36  ? 140 ASP B O   1 
ATOM   3346 C  CB  . ASP B 1 132 ? 49.879 15.580  19.617  1.00 42.16  ? 140 ASP B CB  1 
ATOM   3347 C  CG  . ASP B 1 132 ? 49.619 17.052  19.343  1.00 40.40  ? 140 ASP B CG  1 
ATOM   3348 O  OD1 . ASP B 1 132 ? 48.726 17.344  18.523  1.00 46.17  ? 140 ASP B OD1 1 
ATOM   3349 O  OD2 . ASP B 1 132 ? 50.331 17.893  19.928  1.00 40.52  ? 140 ASP B OD2 1 
ATOM   3350 N  N   . GLU B 1 133 ? 49.154 12.733  21.062  1.00 40.81  ? 141 GLU B N   1 
ATOM   3351 C  CA  . GLU B 1 133 ? 49.424 11.315  21.240  1.00 43.78  ? 141 GLU B CA  1 
ATOM   3352 C  C   . GLU B 1 133 ? 48.162 10.519  20.917  1.00 41.81  ? 141 GLU B C   1 
ATOM   3353 O  O   . GLU B 1 133 ? 48.218 9.495   20.240  1.00 40.79  ? 141 GLU B O   1 
ATOM   3354 C  CB  . GLU B 1 133 ? 49.874 11.016  22.670  1.00 40.03  ? 141 GLU B CB  1 
ATOM   3355 C  CG  . GLU B 1 133 ? 50.369 9.593   22.856  1.00 42.12  ? 141 GLU B CG  1 
ATOM   3356 C  CD  . GLU B 1 133 ? 51.702 9.300   22.190  1.00 41.71  ? 141 GLU B CD  1 
ATOM   3357 O  OE1 . GLU B 1 133 ? 52.290 10.237  21.613  1.00 44.85  ? 141 GLU B OE1 1 
ATOM   3358 O  OE2 . GLU B 1 133 ? 52.149 8.136   22.248  1.00 42.47  ? 141 GLU B OE2 1 
ATOM   3359 N  N   . PHE B 1 134 ? 47.028 11.009  21.424  1.00 41.55  ? 142 PHE B N   1 
ATOM   3360 C  CA  . PHE B 1 134 ? 45.737 10.385  21.198  1.00 45.58  ? 142 PHE B CA  1 
ATOM   3361 C  C   . PHE B 1 134 ? 45.459 10.326  19.699  1.00 47.67  ? 142 PHE B C   1 
ATOM   3362 O  O   . PHE B 1 134 ? 45.137 9.272   19.154  1.00 47.00  ? 142 PHE B O   1 
ATOM   3363 C  CB  . PHE B 1 134 ? 44.655 11.179  21.934  1.00 46.02  ? 142 PHE B CB  1 
ATOM   3364 C  CG  . PHE B 1 134 ? 43.328 10.479  22.081  1.00 43.62  ? 142 PHE B CG  1 
ATOM   3365 C  CD1 . PHE B 1 134 ? 43.268 9.141   22.438  1.00 49.26  ? 142 PHE B CD1 1 
ATOM   3366 C  CD2 . PHE B 1 134 ? 42.140 11.170  21.908  1.00 43.84  ? 142 PHE B CD2 1 
ATOM   3367 C  CE1 . PHE B 1 134 ? 42.046 8.504   22.588  1.00 51.30  ? 142 PHE B CE1 1 
ATOM   3368 C  CE2 . PHE B 1 134 ? 40.920 10.533  22.065  1.00 42.08  ? 142 PHE B CE2 1 
ATOM   3369 C  CZ  . PHE B 1 134 ? 40.875 9.201   22.403  1.00 46.00  ? 142 PHE B CZ  1 
ATOM   3370 N  N   . ASN B 1 135 ? 45.594 11.486  19.050  1.00 45.57  ? 143 ASN B N   1 
ATOM   3371 C  CA  . ASN B 1 135 ? 45.335 11.624  17.628  1.00 42.26  ? 143 ASN B CA  1 
ATOM   3372 C  C   . ASN B 1 135 ? 46.208 10.639  16.856  1.00 42.72  ? 143 ASN B C   1 
ATOM   3373 O  O   . ASN B 1 135 ? 45.719 9.907   16.000  1.00 45.26  ? 143 ASN B O   1 
ATOM   3374 C  CB  . ASN B 1 135 ? 45.575 13.061  17.159  1.00 41.56  ? 143 ASN B CB  1 
ATOM   3375 C  CG  . ASN B 1 135 ? 44.533 14.034  17.668  1.00 40.43  ? 143 ASN B CG  1 
ATOM   3376 O  OD1 . ASN B 1 135 ? 43.475 13.628  18.142  1.00 42.52  ? 143 ASN B OD1 1 
ATOM   3377 N  ND2 . ASN B 1 135 ? 44.816 15.322  17.561  1.00 36.46  ? 143 ASN B ND2 1 
ATOM   3378 N  N   . GLY B 1 136 ? 47.506 10.638  17.174  1.00 42.20  ? 144 GLY B N   1 
ATOM   3379 C  CA  . GLY B 1 136 ? 48.474 9.800   16.487  1.00 42.20  ? 144 GLY B CA  1 
ATOM   3380 C  C   . GLY B 1 136 ? 48.125 8.317   16.574  1.00 42.59  ? 144 GLY B C   1 
ATOM   3381 O  O   . GLY B 1 136 ? 48.307 7.580   15.609  1.00 46.72  ? 144 GLY B O   1 
ATOM   3382 N  N   . ALA B 1 137 ? 47.633 7.882   17.739  1.00 40.66  ? 145 ALA B N   1 
ATOM   3383 C  CA  . ALA B 1 137 ? 47.325 6.476   17.940  1.00 42.34  ? 145 ALA B CA  1 
ATOM   3384 C  C   . ALA B 1 137 ? 46.016 6.130   17.235  1.00 40.22  ? 145 ALA B C   1 
ATOM   3385 O  O   . ALA B 1 137 ? 45.873 5.035   16.697  1.00 48.17  ? 145 ALA B O   1 
ATOM   3386 C  CB  . ALA B 1 137 ? 47.272 6.149   19.412  1.00 40.46  ? 145 ALA B CB  1 
ATOM   3387 N  N   . LEU B 1 138 ? 45.067 7.071   17.235  1.00 41.31  ? 146 LEU B N   1 
ATOM   3388 C  CA  . LEU B 1 138 ? 43.799 6.856   16.557  1.00 43.98  ? 146 LEU B CA  1 
ATOM   3389 C  C   . LEU B 1 138 ? 44.022 6.724   15.049  1.00 43.44  ? 146 LEU B C   1 
ATOM   3390 O  O   . LEU B 1 138 ? 43.282 6.000   14.387  1.00 45.17  ? 146 LEU B O   1 
ATOM   3391 C  CB  . LEU B 1 138 ? 42.833 7.996   16.900  1.00 41.53  ? 146 LEU B CB  1 
ATOM   3392 C  CG  . LEU B 1 138 ? 42.337 8.014   18.345  1.00 42.93  ? 146 LEU B CG  1 
ATOM   3393 C  CD1 . LEU B 1 138 ? 41.351 9.149   18.573  1.00 45.38  ? 146 LEU B CD1 1 
ATOM   3394 C  CD2 . LEU B 1 138 ? 41.705 6.681   18.721  1.00 47.50  ? 146 LEU B CD2 1 
ATOM   3395 N  N   . GLN B 1 139 ? 45.042 7.404   14.504  1.00 42.87  ? 147 GLN B N   1 
ATOM   3396 C  CA  . GLN B 1 139 ? 45.360 7.258   13.090  1.00 43.17  ? 147 GLN B CA  1 
ATOM   3397 C  C   . GLN B 1 139 ? 45.941 5.869   12.838  1.00 44.31  ? 147 GLN B C   1 
ATOM   3398 O  O   . GLN B 1 139 ? 45.564 5.208   11.874  1.00 50.58  ? 147 GLN B O   1 
ATOM   3399 C  CB  . GLN B 1 139 ? 46.336 8.326   12.588  1.00 43.82  ? 147 GLN B CB  1 
ATOM   3400 C  CG  . GLN B 1 139 ? 45.711 9.702   12.395  1.00 53.04  ? 147 GLN B CG  1 
ATOM   3401 C  CD  . GLN B 1 139 ? 46.510 10.557  11.440  1.00 50.80  ? 147 GLN B CD  1 
ATOM   3402 O  OE1 . GLN B 1 139 ? 47.289 10.055  10.632  1.00 47.73  ? 147 GLN B OE1 1 
ATOM   3403 N  NE2 . GLN B 1 139 ? 46.301 11.861  11.508  1.00 51.06  ? 147 GLN B NE2 1 
ATOM   3404 N  N   . CYS B 1 140 ? 46.868 5.432   13.700  1.00 46.07  ? 148 CYS B N   1 
ATOM   3405 C  CA  . CYS B 1 140 ? 47.409 4.086   13.597  1.00 51.47  ? 148 CYS B CA  1 
ATOM   3406 C  C   . CYS B 1 140 ? 46.258 3.085   13.537  1.00 51.49  ? 148 CYS B C   1 
ATOM   3407 O  O   . CYS B 1 140 ? 46.295 2.133   12.761  1.00 47.97  ? 148 CYS B O   1 
ATOM   3408 C  CB  . CYS B 1 140 ? 48.322 3.744   14.770  1.00 48.31  ? 148 CYS B CB  1 
ATOM   3409 S  SG  . CYS B 1 140 ? 49.903 4.629   14.752  1.00 51.87  ? 148 CYS B SG  1 
ATOM   3410 N  N   . TYR B 1 141 ? 45.234 3.327   14.362  1.00 51.09  ? 149 TYR B N   1 
ATOM   3411 C  CA  . TYR B 1 141 ? 44.074 2.455   14.446  1.00 50.84  ? 149 TYR B CA  1 
ATOM   3412 C  C   . TYR B 1 141 ? 43.302 2.486   13.130  1.00 54.35  ? 149 TYR B C   1 
ATOM   3413 O  O   . TYR B 1 141 ? 42.987 1.441   12.565  1.00 54.60  ? 149 TYR B O   1 
ATOM   3414 C  CB  . TYR B 1 141 ? 43.140 2.886   15.580  1.00 43.46  ? 149 TYR B CB  1 
ATOM   3415 C  CG  . TYR B 1 141 ? 41.930 1.981   15.768  1.00 49.55  ? 149 TYR B CG  1 
ATOM   3416 C  CD1 . TYR B 1 141 ? 42.078 0.677   16.222  1.00 52.42  ? 149 TYR B CD1 1 
ATOM   3417 C  CD2 . TYR B 1 141 ? 40.643 2.425   15.482  1.00 52.08  ? 149 TYR B CD2 1 
ATOM   3418 C  CE1 . TYR B 1 141 ? 40.986 -0.156  16.396  1.00 48.67  ? 149 TYR B CE1 1 
ATOM   3419 C  CE2 . TYR B 1 141 ? 39.543 1.601   15.649  1.00 50.75  ? 149 TYR B CE2 1 
ATOM   3420 C  CZ  . TYR B 1 141 ? 39.715 0.307   16.108  1.00 50.24  ? 149 TYR B CZ  1 
ATOM   3421 O  OH  . TYR B 1 141 ? 38.636 -0.511  16.278  1.00 53.65  ? 149 TYR B OH  1 
ATOM   3422 N  N   . ALA B 1 142 ? 42.994 3.701   12.665  1.00 50.64  ? 150 ALA B N   1 
ATOM   3423 C  CA  . ALA B 1 142 ? 42.097 3.903   11.539  1.00 50.36  ? 150 ALA B CA  1 
ATOM   3424 C  C   . ALA B 1 142 ? 42.728 3.375   10.252  1.00 50.55  ? 150 ALA B C   1 
ATOM   3425 O  O   . ALA B 1 142 ? 42.025 2.895   9.367   1.00 58.67  ? 150 ALA B O   1 
ATOM   3426 C  CB  . ALA B 1 142 ? 41.748 5.367   11.427  1.00 48.95  ? 150 ALA B CB  1 
ATOM   3427 N  N   . ARG B 1 143 ? 44.059 3.478   10.164  1.00 45.14  ? 151 ARG B N   1 
ATOM   3428 C  CA  . ARG B 1 143 ? 44.818 2.995   9.022   1.00 50.82  ? 151 ARG B CA  1 
ATOM   3429 C  C   . ARG B 1 143 ? 45.148 1.514   9.198   1.00 54.24  ? 151 ARG B C   1 
ATOM   3430 O  O   . ARG B 1 143 ? 45.975 0.970   8.470   1.00 54.20  ? 151 ARG B O   1 
ATOM   3431 C  CB  . ARG B 1 143 ? 46.136 3.763   8.881   1.00 53.42  ? 151 ARG B CB  1 
ATOM   3432 C  CG  . ARG B 1 143 ? 46.001 5.278   8.845   1.00 54.27  ? 151 ARG B CG  1 
ATOM   3433 C  CD  . ARG B 1 143 ? 47.374 5.922   8.853   1.00 54.30  ? 151 ARG B CD  1 
ATOM   3434 N  NE  . ARG B 1 143 ? 47.329 7.374   8.806   1.00 55.49  ? 151 ARG B NE  1 
ATOM   3435 C  CZ  . ARG B 1 143 ? 47.643 8.099   7.739   1.00 55.25  ? 151 ARG B CZ  1 
ATOM   3436 N  NH1 . ARG B 1 143 ? 47.927 7.503   6.595   1.00 63.05  ? 151 ARG B NH1 1 
ATOM   3437 N  NH2 . ARG B 1 143 ? 47.646 9.419   7.814   1.00 61.24  ? 151 ARG B NH2 1 
ATOM   3438 N  N   . ASN B 1 144 ? 44.520 0.880   10.192  1.00 53.10  ? 152 ASN B N   1 
ATOM   3439 C  CA  . ASN B 1 144 ? 44.701 -0.541  10.439  1.00 64.09  ? 152 ASN B CA  1 
ATOM   3440 C  C   . ASN B 1 144 ? 46.187 -0.901  10.441  1.00 60.26  ? 152 ASN B C   1 
ATOM   3441 O  O   . ASN B 1 144 ? 46.580 -1.909  9.859   1.00 60.79  ? 152 ASN B O   1 
ATOM   3442 C  CB  . ASN B 1 144 ? 43.926 -1.382  9.419   1.00 55.89  ? 152 ASN B CB  1 
ATOM   3443 C  CG  . ASN B 1 144 ? 42.429 -1.326  9.635   1.00 63.33  ? 152 ASN B CG  1 
ATOM   3444 O  OD1 . ASN B 1 144 ? 41.898 -2.004  10.513  1.00 56.67  ? 152 ASN B OD1 1 
ATOM   3445 N  ND2 . ASN B 1 144 ? 41.738 -0.528  8.837   1.00 60.79  ? 152 ASN B ND2 1 
ATOM   3446 N  N   . GLN B 1 145 ? 47.007 -0.080  11.108  1.00 56.21  ? 153 GLN B N   1 
ATOM   3447 C  CA  . GLN B 1 145 ? 48.403 -0.416  11.343  1.00 64.45  ? 153 GLN B CA  1 
ATOM   3448 C  C   . GLN B 1 145 ? 48.468 -1.485  12.432  1.00 65.57  ? 153 GLN B C   1 
ATOM   3449 O  O   . GLN B 1 145 ? 47.888 -1.313  13.502  1.00 62.15  ? 153 GLN B O   1 
ATOM   3450 C  CB  . GLN B 1 145 ? 49.199 0.829   11.748  1.00 69.78  ? 153 GLN B CB  1 
ATOM   3451 C  CG  . GLN B 1 145 ? 49.181 1.939   10.705  1.00 91.07  ? 153 GLN B CG  1 
ATOM   3452 C  CD  . GLN B 1 145 ? 50.097 3.086   11.061  1.00 98.40  ? 153 GLN B CD  1 
ATOM   3453 O  OE1 . GLN B 1 145 ? 51.225 2.888   11.505  1.00 108.43 ? 153 GLN B OE1 1 
ATOM   3454 N  NE2 . GLN B 1 145 ? 49.613 4.304   10.875  1.00 91.41  ? 153 GLN B NE2 1 
ATOM   3455 N  N   . LYS B 1 146 ? 49.171 -2.592  12.157  1.00 66.01  ? 154 LYS B N   1 
ATOM   3456 C  CA  . LYS B 1 146 ? 49.152 -3.741  13.052  1.00 79.19  ? 154 LYS B CA  1 
ATOM   3457 C  C   . LYS B 1 146 ? 50.524 -3.977  13.681  1.00 75.35  ? 154 LYS B C   1 
ATOM   3458 O  O   . LYS B 1 146 ? 50.617 -4.629  14.719  1.00 68.86  ? 154 LYS B O   1 
ATOM   3459 C  CB  . LYS B 1 146 ? 48.658 -4.993  12.321  1.00 79.87  ? 154 LYS B CB  1 
ATOM   3460 C  CG  . LYS B 1 146 ? 47.249 -5.443  12.688  1.00 85.83  ? 154 LYS B CG  1 
ATOM   3461 C  CD  . LYS B 1 146 ? 46.171 -4.421  12.404  1.00 87.07  ? 154 LYS B CD  1 
ATOM   3462 C  CE  . LYS B 1 146 ? 44.775 -4.967  12.624  1.00 87.62  ? 154 LYS B CE  1 
ATOM   3463 N  NZ  . LYS B 1 146 ? 43.749 -4.135  11.953  1.00 95.71  ? 154 LYS B NZ  1 
ATOM   3464 N  N   . GLU B 1 147 ? 51.585 -3.456  13.056  1.00 63.83  ? 155 GLU B N   1 
ATOM   3465 C  CA  . GLU B 1 147 ? 52.912 -3.511  13.648  1.00 70.32  ? 155 GLU B CA  1 
ATOM   3466 C  C   . GLU B 1 147 ? 53.188 -2.167  14.318  1.00 74.17  ? 155 GLU B C   1 
ATOM   3467 O  O   . GLU B 1 147 ? 52.415 -1.225  14.157  1.00 87.53  ? 155 GLU B O   1 
ATOM   3468 C  CB  . GLU B 1 147 ? 53.972 -3.812  12.585  1.00 89.63  ? 155 GLU B CB  1 
ATOM   3469 C  CG  . GLU B 1 147 ? 53.497 -4.746  11.483  1.00 101.34 ? 155 GLU B CG  1 
ATOM   3470 C  CD  . GLU B 1 147 ? 53.774 -6.223  11.709  1.00 105.48 ? 155 GLU B CD  1 
ATOM   3471 O  OE1 . GLU B 1 147 ? 54.961 -6.587  11.840  1.00 102.50 ? 155 GLU B OE1 1 
ATOM   3472 O  OE2 . GLU B 1 147 ? 52.804 -7.006  11.739  1.00 101.27 ? 155 GLU B OE2 1 
ATOM   3473 N  N   . GLY B 1 148 ? 54.292 -2.083  15.066  1.00 73.47  ? 156 GLY B N   1 
ATOM   3474 C  CA  . GLY B 1 148 ? 54.672 -0.842  15.721  1.00 68.39  ? 156 GLY B CA  1 
ATOM   3475 C  C   . GLY B 1 148 ? 54.327 -0.851  17.208  1.00 65.80  ? 156 GLY B C   1 
ATOM   3476 O  O   . GLY B 1 148 ? 53.941 -1.885  17.750  1.00 62.12  ? 156 GLY B O   1 
ATOM   3477 N  N   . ALA B 1 149 ? 54.455 0.318   17.848  1.00 57.36  ? 157 ALA B N   1 
ATOM   3478 C  CA  . ALA B 1 149 ? 54.378 0.422   19.296  1.00 56.64  ? 157 ALA B CA  1 
ATOM   3479 C  C   . ALA B 1 149 ? 52.958 0.761   19.741  1.00 48.55  ? 157 ALA B C   1 
ATOM   3480 O  O   . ALA B 1 149 ? 52.683 0.811   20.937  1.00 56.51  ? 157 ALA B O   1 
ATOM   3481 C  CB  . ALA B 1 149 ? 55.361 1.454   19.789  1.00 59.43  ? 157 ALA B CB  1 
ATOM   3482 N  N   . TYR B 1 150 ? 52.064 0.997   18.776  1.00 42.36  ? 158 TYR B N   1 
ATOM   3483 C  CA  . TYR B 1 150 ? 50.676 1.295   19.087  1.00 47.22  ? 158 TYR B CA  1 
ATOM   3484 C  C   . TYR B 1 150 ? 49.837 0.070   18.734  1.00 47.81  ? 158 TYR B C   1 
ATOM   3485 O  O   . TYR B 1 150 ? 49.657 -0.246  17.561  1.00 53.40  ? 158 TYR B O   1 
ATOM   3486 C  CB  . TYR B 1 150 ? 50.307 2.597   18.366  1.00 45.71  ? 158 TYR B CB  1 
ATOM   3487 C  CG  . TYR B 1 150 ? 51.108 3.794   18.861  1.00 46.75  ? 158 TYR B CG  1 
ATOM   3488 C  CD1 . TYR B 1 150 ? 50.697 4.527   19.968  1.00 46.35  ? 158 TYR B CD1 1 
ATOM   3489 C  CD2 . TYR B 1 150 ? 52.309 4.152   18.260  1.00 45.64  ? 158 TYR B CD2 1 
ATOM   3490 C  CE1 . TYR B 1 150 ? 51.431 5.605   20.434  1.00 45.89  ? 158 TYR B CE1 1 
ATOM   3491 C  CE2 . TYR B 1 150 ? 53.055 5.224   18.719  1.00 50.49  ? 158 TYR B CE2 1 
ATOM   3492 C  CZ  . TYR B 1 150 ? 52.615 5.953   19.810  1.00 47.98  ? 158 TYR B CZ  1 
ATOM   3493 O  OH  . TYR B 1 150 ? 53.342 7.011   20.277  1.00 44.61  ? 158 TYR B OH  1 
ATOM   3494 N  N   . ILE B 1 151 ? 49.342 -0.620  19.769  1.00 51.92  ? 159 ILE B N   1 
ATOM   3495 C  CA  . ILE B 1 151 ? 48.687 -1.908  19.601  1.00 50.78  ? 159 ILE B CA  1 
ATOM   3496 C  C   . ILE B 1 151 ? 47.229 -1.692  19.205  1.00 50.70  ? 159 ILE B C   1 
ATOM   3497 O  O   . ILE B 1 151 ? 46.435 -1.159  19.978  1.00 51.78  ? 159 ILE B O   1 
ATOM   3498 C  CB  . ILE B 1 151 ? 48.810 -2.764  20.878  1.00 55.50  ? 159 ILE B CB  1 
ATOM   3499 C  CG1 . ILE B 1 151 ? 50.265 -2.890  21.338  1.00 51.57  ? 159 ILE B CG1 1 
ATOM   3500 C  CG2 . ILE B 1 151 ? 48.159 -4.125  20.677  1.00 59.65  ? 159 ILE B CG2 1 
ATOM   3501 C  CD1 . ILE B 1 151 ? 51.212 -3.359  20.257  1.00 55.81  ? 159 ILE B CD1 1 
ATOM   3502 N  N   . TRP B 1 152 ? 46.896 -2.143  17.992  1.00 49.89  ? 160 TRP B N   1 
ATOM   3503 C  CA  . TRP B 1 152 ? 45.567 -1.986  17.425  1.00 50.43  ? 160 TRP B CA  1 
ATOM   3504 C  C   . TRP B 1 152 ? 44.521 -2.594  18.355  1.00 48.38  ? 160 TRP B C   1 
ATOM   3505 O  O   . TRP B 1 152 ? 43.493 -1.976  18.627  1.00 54.49  ? 160 TRP B O   1 
ATOM   3506 C  CB  . TRP B 1 152 ? 45.529 -2.636  16.034  1.00 46.33  ? 160 TRP B CB  1 
ATOM   3507 C  CG  . TRP B 1 152 ? 44.377 -2.199  15.167  1.00 52.63  ? 160 TRP B CG  1 
ATOM   3508 C  CD1 . TRP B 1 152 ? 44.400 -1.214  14.225  1.00 53.35  ? 160 TRP B CD1 1 
ATOM   3509 C  CD2 . TRP B 1 152 ? 43.047 -2.762  15.129  1.00 51.74  ? 160 TRP B CD2 1 
ATOM   3510 N  NE1 . TRP B 1 152 ? 43.176 -1.104  13.622  1.00 61.12  ? 160 TRP B NE1 1 
ATOM   3511 C  CE2 . TRP B 1 152 ? 42.328 -2.042  14.150  1.00 59.43  ? 160 TRP B CE2 1 
ATOM   3512 C  CE3 . TRP B 1 152 ? 42.396 -3.787  15.824  1.00 50.13  ? 160 TRP B CE3 1 
ATOM   3513 C  CZ2 . TRP B 1 152 ? 40.996 -2.319  13.852  1.00 59.35  ? 160 TRP B CZ2 1 
ATOM   3514 C  CZ3 . TRP B 1 152 ? 41.079 -4.061  15.527  1.00 52.78  ? 160 TRP B CZ3 1 
ATOM   3515 C  CH2 . TRP B 1 152 ? 40.392 -3.338  14.552  1.00 56.34  ? 160 TRP B CH2 1 
ATOM   3516 N  N   . ALA B 1 153 ? 44.799 -3.808  18.841  1.00 53.77  ? 161 ALA B N   1 
ATOM   3517 C  CA  . ALA B 1 153 ? 43.853 -4.542  19.665  1.00 53.18  ? 161 ALA B CA  1 
ATOM   3518 C  C   . ALA B 1 153 ? 43.650 -3.828  21.001  1.00 49.26  ? 161 ALA B C   1 
ATOM   3519 O  O   . ALA B 1 153 ? 42.593 -3.951  21.614  1.00 51.65  ? 161 ALA B O   1 
ATOM   3520 C  CB  . ALA B 1 153 ? 44.330 -5.963  19.853  1.00 53.43  ? 161 ALA B CB  1 
ATOM   3521 N  N   . ASP B 1 154 ? 44.663 -3.072  21.443  1.00 47.76  ? 162 ASP B N   1 
ATOM   3522 C  CA  . ASP B 1 154 ? 44.550 -2.312  22.677  1.00 50.19  ? 162 ASP B CA  1 
ATOM   3523 C  C   . ASP B 1 154 ? 43.611 -1.126  22.461  1.00 47.43  ? 162 ASP B C   1 
ATOM   3524 O  O   . ASP B 1 154 ? 42.717 -0.889  23.270  1.00 47.12  ? 162 ASP B O   1 
ATOM   3525 C  CB  . ASP B 1 154 ? 45.921 -1.866  23.198  1.00 48.01  ? 162 ASP B CB  1 
ATOM   3526 C  CG  . ASP B 1 154 ? 46.703 -2.966  23.897  1.00 55.16  ? 162 ASP B CG  1 
ATOM   3527 O  OD1 . ASP B 1 154 ? 46.165 -4.085  24.016  1.00 56.18  ? 162 ASP B OD1 1 
ATOM   3528 O  OD2 . ASP B 1 154 ? 47.845 -2.694  24.323  1.00 52.82  ? 162 ASP B OD2 1 
ATOM   3529 N  N   . ILE B 1 155 ? 43.821 -0.387  21.366  1.00 51.27  ? 163 ILE B N   1 
ATOM   3530 C  CA  . ILE B 1 155 ? 43.028 0.797   21.076  1.00 48.02  ? 163 ILE B CA  1 
ATOM   3531 C  C   . ILE B 1 155 ? 41.581 0.377   20.838  1.00 48.66  ? 163 ILE B C   1 
ATOM   3532 O  O   . ILE B 1 155 ? 40.652 1.059   21.265  1.00 50.58  ? 163 ILE B O   1 
ATOM   3533 C  CB  . ILE B 1 155 ? 43.612 1.565   19.872  1.00 44.61  ? 163 ILE B CB  1 
ATOM   3534 C  CG1 . ILE B 1 155 ? 45.102 1.859   20.066  1.00 47.31  ? 163 ILE B CG1 1 
ATOM   3535 C  CG2 . ILE B 1 155 ? 42.819 2.836   19.605  1.00 47.63  ? 163 ILE B CG2 1 
ATOM   3536 C  CD1 . ILE B 1 155 ? 45.854 2.099   18.778  1.00 49.21  ? 163 ILE B CD1 1 
ATOM   3537 N  N   . ASP B 1 156 ? 41.408 -0.757  20.153  1.00 52.96  ? 164 ASP B N   1 
ATOM   3538 C  CA  . ASP B 1 156 ? 40.090 -1.305  19.882  1.00 55.71  ? 164 ASP B CA  1 
ATOM   3539 C  C   . ASP B 1 156 ? 39.338 -1.470  21.201  1.00 51.76  ? 164 ASP B C   1 
ATOM   3540 O  O   . ASP B 1 156 ? 38.168 -1.105  21.304  1.00 53.00  ? 164 ASP B O   1 
ATOM   3541 C  CB  . ASP B 1 156 ? 40.203 -2.624  19.112  1.00 61.41  ? 164 ASP B CB  1 
ATOM   3542 C  CG  . ASP B 1 156 ? 38.884 -3.132  18.555  1.00 65.58  ? 164 ASP B CG  1 
ATOM   3543 O  OD1 . ASP B 1 156 ? 38.171 -2.333  17.916  1.00 65.40  ? 164 ASP B OD1 1 
ATOM   3544 O  OD2 . ASP B 1 156 ? 38.592 -4.329  18.750  1.00 74.47  ? 164 ASP B OD2 1 
ATOM   3545 N  N   . ALA B 1 157 ? 40.029 -2.011  22.210  1.00 51.20  ? 165 ALA B N   1 
ATOM   3546 C  CA  . ALA B 1 157 ? 39.427 -2.262  23.510  1.00 49.35  ? 165 ALA B CA  1 
ATOM   3547 C  C   . ALA B 1 157 ? 39.054 -0.943  24.186  1.00 49.01  ? 165 ALA B C   1 
ATOM   3548 O  O   . ALA B 1 157 ? 38.000 -0.847  24.811  1.00 54.52  ? 165 ALA B O   1 
ATOM   3549 C  CB  . ALA B 1 157 ? 40.367 -3.077  24.363  1.00 48.43  ? 165 ALA B CB  1 
ATOM   3550 N  N   . TRP B 1 158 ? 39.920 0.069   24.059  1.00 50.77  ? 166 TRP B N   1 
ATOM   3551 C  CA  . TRP B 1 158 ? 39.663 1.362   24.675  1.00 47.94  ? 166 TRP B CA  1 
ATOM   3552 C  C   . TRP B 1 158 ? 38.333 1.918   24.177  1.00 45.45  ? 166 TRP B C   1 
ATOM   3553 O  O   . TRP B 1 158 ? 37.564 2.481   24.953  1.00 52.46  ? 166 TRP B O   1 
ATOM   3554 C  CB  . TRP B 1 158 ? 40.788 2.362   24.376  1.00 45.82  ? 166 TRP B CB  1 
ATOM   3555 C  CG  . TRP B 1 158 ? 42.171 1.883   24.722  1.00 48.43  ? 166 TRP B CG  1 
ATOM   3556 C  CD1 . TRP B 1 158 ? 42.522 0.843   25.531  1.00 48.20  ? 166 TRP B CD1 1 
ATOM   3557 C  CD2 . TRP B 1 158 ? 43.406 2.438   24.223  1.00 46.48  ? 166 TRP B CD2 1 
ATOM   3558 N  NE1 . TRP B 1 158 ? 43.885 0.720   25.581  1.00 49.71  ? 166 TRP B NE1 1 
ATOM   3559 C  CE2 . TRP B 1 158 ? 44.455 1.681   24.786  1.00 47.76  ? 166 TRP B CE2 1 
ATOM   3560 C  CE3 . TRP B 1 158 ? 43.722 3.496   23.363  1.00 47.87  ? 166 TRP B CE3 1 
ATOM   3561 C  CZ2 . TRP B 1 158 ? 45.794 1.951   24.514  1.00 53.57  ? 166 TRP B CZ2 1 
ATOM   3562 C  CZ3 . TRP B 1 158 ? 45.046 3.760   23.094  1.00 49.07  ? 166 TRP B CZ3 1 
ATOM   3563 C  CH2 . TRP B 1 158 ? 46.066 2.996   23.660  1.00 52.73  ? 166 TRP B CH2 1 
ATOM   3564 N  N   . ILE B 1 159 ? 38.085 1.765   22.871  1.00 45.67  ? 167 ILE B N   1 
ATOM   3565 C  CA  . ILE B 1 159 ? 36.903 2.332   22.245  1.00 51.49  ? 167 ILE B CA  1 
ATOM   3566 C  C   . ILE B 1 159 ? 35.689 1.475   22.595  1.00 55.28  ? 167 ILE B C   1 
ATOM   3567 O  O   . ILE B 1 159 ? 34.615 2.007   22.867  1.00 58.12  ? 167 ILE B O   1 
ATOM   3568 C  CB  . ILE B 1 159 ? 37.102 2.468   20.721  1.00 55.00  ? 167 ILE B CB  1 
ATOM   3569 C  CG1 . ILE B 1 159 ? 38.349 3.293   20.392  1.00 51.56  ? 167 ILE B CG1 1 
ATOM   3570 C  CG2 . ILE B 1 159 ? 35.859 3.048   20.061  1.00 62.25  ? 167 ILE B CG2 1 
ATOM   3571 C  CD1 . ILE B 1 159 ? 38.832 3.138   18.970  1.00 50.79  ? 167 ILE B CD1 1 
ATOM   3572 N  N   . LYS B 1 160 ? 35.869 0.150   22.596  1.00 58.87  ? 168 LYS B N   1 
ATOM   3573 C  CA  . LYS B 1 160 ? 34.776 -0.760  22.894  1.00 60.45  ? 168 LYS B CA  1 
ATOM   3574 C  C   . LYS B 1 160 ? 34.381 -0.630  24.364  1.00 61.39  ? 168 LYS B C   1 
ATOM   3575 O  O   . LYS B 1 160 ? 33.217 -0.829  24.706  1.00 60.26  ? 168 LYS B O   1 
ATOM   3576 C  CB  . LYS B 1 160 ? 35.147 -2.194  22.503  1.00 61.73  ? 168 LYS B CB  1 
ATOM   3577 C  CG  . LYS B 1 160 ? 35.082 -2.454  21.004  1.00 66.56  ? 168 LYS B CG  1 
ATOM   3578 C  CD  . LYS B 1 160 ? 35.261 -3.897  20.596  1.00 79.22  ? 168 LYS B CD  1 
ATOM   3579 C  CE  . LYS B 1 160 ? 35.227 -4.065  19.092  1.00 86.12  ? 168 LYS B CE  1 
ATOM   3580 N  NZ  . LYS B 1 160 ? 35.920 -5.301  18.660  1.00 97.99  ? 168 LYS B NZ  1 
ATOM   3581 N  N   . ASN B 1 161 ? 35.340 -0.268  25.225  1.00 54.92  ? 169 ASN B N   1 
ATOM   3582 C  CA  . ASN B 1 161 ? 35.067 -0.177  26.652  1.00 53.28  ? 169 ASN B CA  1 
ATOM   3583 C  C   . ASN B 1 161 ? 34.631 1.243   27.016  1.00 48.51  ? 169 ASN B C   1 
ATOM   3584 O  O   . ASN B 1 161 ? 34.380 1.528   28.184  1.00 51.82  ? 169 ASN B O   1 
ATOM   3585 C  CB  . ASN B 1 161 ? 36.254 -0.658  27.494  1.00 60.69  ? 169 ASN B CB  1 
ATOM   3586 C  CG  . ASN B 1 161 ? 36.441 -2.162  27.456  1.00 62.98  ? 169 ASN B CG  1 
ATOM   3587 O  OD1 . ASN B 1 161 ? 35.707 -2.869  26.769  1.00 69.54  ? 169 ASN B OD1 1 
ATOM   3588 N  ND2 . ASN B 1 161 ? 37.419 -2.662  28.192  1.00 69.78  ? 169 ASN B ND2 1 
ATOM   3589 N  N   . ASN B 1 162 ? 34.534 2.124   26.013  1.00 51.80  ? 170 ASN B N   1 
ATOM   3590 C  CA  . ASN B 1 162 ? 33.916 3.431   26.182  1.00 50.37  ? 170 ASN B CA  1 
ATOM   3591 C  C   . ASN B 1 162 ? 34.641 4.241   27.257  1.00 49.64  ? 170 ASN B C   1 
ATOM   3592 O  O   . ASN B 1 162 ? 34.004 4.820   28.133  1.00 48.91  ? 170 ASN B O   1 
ATOM   3593 C  CB  . ASN B 1 162 ? 32.431 3.301   26.538  1.00 57.81  ? 170 ASN B CB  1 
ATOM   3594 C  CG  . ASN B 1 162 ? 31.702 4.628   26.543  1.00 64.63  ? 170 ASN B CG  1 
ATOM   3595 O  OD1 . ASN B 1 162 ? 32.166 5.601   25.953  1.00 80.00  ? 170 ASN B OD1 1 
ATOM   3596 N  ND2 . ASN B 1 162 ? 30.551 4.673   27.193  1.00 71.86  ? 170 ASN B ND2 1 
ATOM   3597 N  N   . LEU B 1 163 ? 35.975 4.297   27.175  1.00 49.35  ? 171 LEU B N   1 
ATOM   3598 C  CA  . LEU B 1 163 ? 36.764 5.080   28.112  1.00 45.03  ? 171 LEU B CA  1 
ATOM   3599 C  C   . LEU B 1 163 ? 36.406 6.559   27.993  1.00 51.90  ? 171 LEU B C   1 
ATOM   3600 O  O   . LEU B 1 163 ? 36.022 7.033   26.925  1.00 45.14  ? 171 LEU B O   1 
ATOM   3601 C  CB  . LEU B 1 163 ? 38.252 4.854   27.828  1.00 46.39  ? 171 LEU B CB  1 
ATOM   3602 C  CG  . LEU B 1 163 ? 38.736 3.418   28.018  1.00 46.10  ? 171 LEU B CG  1 
ATOM   3603 C  CD1 . LEU B 1 163 ? 40.252 3.339   27.943  1.00 46.83  ? 171 LEU B CD1 1 
ATOM   3604 C  CD2 . LEU B 1 163 ? 38.236 2.852   29.339  1.00 48.92  ? 171 LEU B CD2 1 
ATOM   3605 N  N   . GLN B 1 164 ? 36.553 7.272   29.116  1.00 52.57  ? 172 GLN B N   1 
ATOM   3606 C  CA  . GLN B 1 164 ? 36.270 8.694   29.196  1.00 53.91  ? 172 GLN B CA  1 
ATOM   3607 C  C   . GLN B 1 164 ? 37.586 9.466   29.136  1.00 55.95  ? 172 GLN B C   1 
ATOM   3608 O  O   . GLN B 1 164 ? 38.395 9.393   30.058  1.00 52.24  ? 172 GLN B O   1 
ATOM   3609 C  CB  . GLN B 1 164 ? 35.500 8.991   30.484  1.00 55.31  ? 172 GLN B CB  1 
ATOM   3610 C  CG  . GLN B 1 164 ? 34.196 8.213   30.599  1.00 60.46  ? 172 GLN B CG  1 
ATOM   3611 C  CD  . GLN B 1 164 ? 33.289 8.454   29.418  1.00 60.33  ? 172 GLN B CD  1 
ATOM   3612 O  OE1 . GLN B 1 164 ? 32.947 7.538   28.674  1.00 60.38  ? 172 GLN B OE1 1 
ATOM   3613 N  NE2 . GLN B 1 164 ? 32.896 9.704   29.233  1.00 57.62  ? 172 GLN B NE2 1 
ATOM   3614 N  N   . TRP B 1 165 ? 37.787 10.206  28.040  1.00 51.15  ? 173 TRP B N   1 
ATOM   3615 C  CA  . TRP B 1 165 ? 39.063 10.850  27.780  1.00 52.17  ? 173 TRP B CA  1 
ATOM   3616 C  C   . TRP B 1 165 ? 39.032 12.320  28.175  1.00 49.01  ? 173 TRP B C   1 
ATOM   3617 O  O   . TRP B 1 165 ? 38.015 12.999  28.050  1.00 44.34  ? 173 TRP B O   1 
ATOM   3618 C  CB  . TRP B 1 165 ? 39.461 10.723  26.305  1.00 46.74  ? 173 TRP B CB  1 
ATOM   3619 C  CG  . TRP B 1 165 ? 39.539 9.302   25.822  1.00 44.44  ? 173 TRP B CG  1 
ATOM   3620 C  CD1 . TRP B 1 165 ? 38.509 8.549   25.343  1.00 43.24  ? 173 TRP B CD1 1 
ATOM   3621 C  CD2 . TRP B 1 165 ? 40.705 8.452   25.808  1.00 45.48  ? 173 TRP B CD2 1 
ATOM   3622 N  NE1 . TRP B 1 165 ? 38.954 7.299   25.009  1.00 47.00  ? 173 TRP B NE1 1 
ATOM   3623 C  CE2 . TRP B 1 165 ? 40.292 7.206   25.288  1.00 43.43  ? 173 TRP B CE2 1 
ATOM   3624 C  CE3 . TRP B 1 165 ? 42.045 8.618   26.175  1.00 45.98  ? 173 TRP B CE3 1 
ATOM   3625 C  CZ2 . TRP B 1 165 ? 41.172 6.139   25.129  1.00 47.56  ? 173 TRP B CZ2 1 
ATOM   3626 C  CZ3 . TRP B 1 165 ? 42.913 7.561   26.018  1.00 40.82  ? 173 TRP B CZ3 1 
ATOM   3627 C  CH2 . TRP B 1 165 ? 42.481 6.340   25.504  1.00 44.29  ? 173 TRP B CH2 1 
ATOM   3628 N  N   . ARG B 1 166 ? 40.194 12.781  28.638  1.00 47.71  ? 174 ARG B N   1 
ATOM   3629 C  CA  . ARG B 1 166 ? 40.478 14.189  28.819  1.00 44.47  ? 174 ARG B CA  1 
ATOM   3630 C  C   . ARG B 1 166 ? 41.831 14.460  28.168  1.00 49.07  ? 174 ARG B C   1 
ATOM   3631 O  O   . ARG B 1 166 ? 42.869 14.070  28.700  1.00 44.28  ? 174 ARG B O   1 
ATOM   3632 C  CB  . ARG B 1 166 ? 40.472 14.517  30.314  1.00 48.51  ? 174 ARG B CB  1 
ATOM   3633 C  CG  . ARG B 1 166 ? 40.213 15.978  30.642  1.00 54.68  ? 174 ARG B CG  1 
ATOM   3634 C  CD  . ARG B 1 166 ? 41.398 16.848  30.286  1.00 60.21  ? 174 ARG B CD  1 
ATOM   3635 N  NE  . ARG B 1 166 ? 41.417 18.077  31.061  1.00 56.47  ? 174 ARG B NE  1 
ATOM   3636 C  CZ  . ARG B 1 166 ? 42.069 19.175  30.704  1.00 69.65  ? 174 ARG B CZ  1 
ATOM   3637 N  NH1 . ARG B 1 166 ? 42.662 19.236  29.524  1.00 63.82  ? 174 ARG B NH1 1 
ATOM   3638 N  NH2 . ARG B 1 166 ? 42.101 20.219  31.515  1.00 70.15  ? 174 ARG B NH2 1 
ATOM   3639 N  N   . THR B 1 167 ? 41.807 15.081  26.986  1.00 43.67  ? 175 THR B N   1 
ATOM   3640 C  CA  . THR B 1 167 ? 43.030 15.336  26.249  1.00 44.38  ? 175 THR B CA  1 
ATOM   3641 C  C   . THR B 1 167 ? 43.672 16.618  26.763  1.00 46.28  ? 175 THR B C   1 
ATOM   3642 O  O   . THR B 1 167 ? 42.989 17.596  27.059  1.00 45.85  ? 175 THR B O   1 
ATOM   3643 C  CB  . THR B 1 167 ? 42.787 15.427  24.738  1.00 41.43  ? 175 THR B CB  1 
ATOM   3644 O  OG1 . THR B 1 167 ? 41.833 16.462  24.502  1.00 46.93  ? 175 THR B OG1 1 
ATOM   3645 C  CG2 . THR B 1 167 ? 42.298 14.127  24.139  1.00 43.63  ? 175 THR B CG2 1 
ATOM   3646 N  N   . VAL B 1 168 ? 45.001 16.582  26.867  1.00 44.05  ? 176 VAL B N   1 
ATOM   3647 C  CA  . VAL B 1 168 ? 45.785 17.764  27.165  1.00 42.43  ? 176 VAL B CA  1 
ATOM   3648 C  C   . VAL B 1 168 ? 46.134 18.435  25.841  1.00 41.72  ? 176 VAL B C   1 
ATOM   3649 O  O   . VAL B 1 168 ? 46.734 17.814  24.967  1.00 41.75  ? 176 VAL B O   1 
ATOM   3650 C  CB  . VAL B 1 168 ? 47.039 17.386  27.974  1.00 42.53  ? 176 VAL B CB  1 
ATOM   3651 C  CG1 . VAL B 1 168 ? 47.858 18.608  28.358  1.00 42.75  ? 176 VAL B CG1 1 
ATOM   3652 C  CG2 . VAL B 1 168 ? 46.670 16.570  29.204  1.00 43.27  ? 176 VAL B CG2 1 
ATOM   3653 N  N   . LYS B 1 169 ? 45.727 19.699  25.694  1.00 42.85  ? 177 LYS B N   1 
ATOM   3654 C  CA  . LYS B 1 169 ? 45.892 20.406  24.435  1.00 45.33  ? 177 LYS B CA  1 
ATOM   3655 C  C   . LYS B 1 169 ? 47.367 20.765  24.271  1.00 44.05  ? 177 LYS B C   1 
ATOM   3656 O  O   . LYS B 1 169 ? 48.104 20.840  25.251  1.00 42.88  ? 177 LYS B O   1 
ATOM   3657 C  CB  . LYS B 1 169 ? 44.967 21.626  24.392  1.00 47.66  ? 177 LYS B CB  1 
ATOM   3658 C  CG  . LYS B 1 169 ? 43.527 21.353  24.811  1.00 55.57  ? 177 LYS B CG  1 
ATOM   3659 C  CD  . LYS B 1 169 ? 42.858 20.248  24.014  1.00 61.12  ? 177 LYS B CD  1 
ATOM   3660 C  CE  . LYS B 1 169 ? 41.417 20.000  24.412  1.00 60.84  ? 177 LYS B CE  1 
ATOM   3661 N  NZ  . LYS B 1 169 ? 41.313 19.230  25.674  1.00 57.97  ? 177 LYS B NZ  1 
ATOM   3662 N  N   . ARG B 1 170 ? 47.785 20.970  23.018  1.00 42.89  ? 178 ARG B N   1 
ATOM   3663 C  CA  . ARG B 1 170 ? 49.190 21.135  22.688  1.00 48.16  ? 178 ARG B CA  1 
ATOM   3664 C  C   . ARG B 1 170 ? 49.815 22.220  23.563  1.00 50.04  ? 178 ARG B C   1 
ATOM   3665 O  O   . ARG B 1 170 ? 50.916 22.041  24.079  1.00 51.97  ? 178 ARG B O   1 
ATOM   3666 C  CB  . ARG B 1 170 ? 49.354 21.467  21.201  1.00 48.57  ? 178 ARG B CB  1 
ATOM   3667 C  CG  . ARG B 1 170 ? 50.801 21.525  20.734  1.00 52.19  ? 178 ARG B CG  1 
ATOM   3668 C  CD  . ARG B 1 170 ? 50.905 21.687  19.231  1.00 49.91  ? 178 ARG B CD  1 
ATOM   3669 N  NE  . ARG B 1 170 ? 50.370 20.531  18.527  1.00 47.62  ? 178 ARG B NE  1 
ATOM   3670 C  CZ  . ARG B 1 170 ? 50.259 20.439  17.208  1.00 52.28  ? 178 ARG B CZ  1 
ATOM   3671 N  NH1 . ARG B 1 170 ? 50.547 21.479  16.445  1.00 44.15  ? 178 ARG B NH1 1 
ATOM   3672 N  NH2 . ARG B 1 170 ? 49.844 19.310  16.658  1.00 45.38  ? 178 ARG B NH2 1 
ATOM   3673 N  N   . HIS B 1 171 ? 49.111 23.343  23.728  1.00 48.12  ? 179 HIS B N   1 
ATOM   3674 C  CA  . HIS B 1 171 ? 49.681 24.481  24.430  1.00 66.77  ? 179 HIS B CA  1 
ATOM   3675 C  C   . HIS B 1 171 ? 49.007 24.657  25.789  1.00 64.24  ? 179 HIS B C   1 
ATOM   3676 O  O   . HIS B 1 171 ? 49.041 25.744  26.362  1.00 63.50  ? 179 HIS B O   1 
ATOM   3677 C  CB  . HIS B 1 171 ? 49.613 25.736  23.551  1.00 73.68  ? 179 HIS B CB  1 
ATOM   3678 C  CG  . HIS B 1 171 ? 50.346 25.584  22.259  1.00 83.99  ? 179 HIS B CG  1 
ATOM   3679 N  ND1 . HIS B 1 171 ? 51.639 25.109  22.203  1.00 85.47  ? 179 HIS B ND1 1 
ATOM   3680 C  CD2 . HIS B 1 171 ? 49.979 25.810  20.990  1.00 81.43  ? 179 HIS B CD2 1 
ATOM   3681 C  CE1 . HIS B 1 171 ? 52.034 25.066  20.939  1.00 75.95  ? 179 HIS B CE1 1 
ATOM   3682 N  NE2 . HIS B 1 171 ? 51.042 25.488  20.185  1.00 88.50  ? 179 HIS B NE2 1 
ATOM   3683 N  N   . GLU B 1 172 ? 48.416 23.577  26.311  1.00 53.55  ? 180 GLU B N   1 
ATOM   3684 C  CA  . GLU B 1 172 ? 47.727 23.641  27.589  1.00 53.81  ? 180 GLU B CA  1 
ATOM   3685 C  C   . GLU B 1 172 ? 48.753 23.676  28.717  1.00 54.05  ? 180 GLU B C   1 
ATOM   3686 O  O   . GLU B 1 172 ? 49.771 22.989  28.665  1.00 53.58  ? 180 GLU B O   1 
ATOM   3687 C  CB  . GLU B 1 172 ? 46.773 22.458  27.765  1.00 55.32  ? 180 GLU B CB  1 
ATOM   3688 C  CG  . GLU B 1 172 ? 45.848 22.617  28.958  1.00 50.46  ? 180 GLU B CG  1 
ATOM   3689 C  CD  . GLU B 1 172 ? 44.732 21.591  29.050  1.00 51.78  ? 180 GLU B CD  1 
ATOM   3690 O  OE1 . GLU B 1 172 ? 44.579 20.795  28.102  1.00 51.48  ? 180 GLU B OE1 1 
ATOM   3691 O  OE2 . GLU B 1 172 ? 44.020 21.591  30.073  1.00 67.01  ? 180 GLU B OE2 1 
ATOM   3692 N  N   . ASP B 1 173 ? 48.458 24.485  29.739  1.00 62.23  ? 181 ASP B N   1 
ATOM   3693 C  CA  . ASP B 1 173 ? 49.304 24.597  30.915  1.00 68.72  ? 181 ASP B CA  1 
ATOM   3694 C  C   . ASP B 1 173 ? 49.223 23.300  31.717  1.00 55.14  ? 181 ASP B C   1 
ATOM   3695 O  O   . ASP B 1 173 ? 48.347 22.472  31.482  1.00 65.95  ? 181 ASP B O   1 
ATOM   3696 C  CB  . ASP B 1 173 ? 48.895 25.801  31.769  1.00 73.09  ? 181 ASP B CB  1 
ATOM   3697 C  CG  . ASP B 1 173 ? 49.223 27.143  31.137  1.00 77.52  ? 181 ASP B CG  1 
ATOM   3698 O  OD1 . ASP B 1 173 ? 49.894 27.147  30.086  1.00 78.59  ? 181 ASP B OD1 1 
ATOM   3699 O  OD2 . ASP B 1 173 ? 48.801 28.172  31.700  1.00 77.96  ? 181 ASP B OD2 1 
ATOM   3700 N  N   . ASN B 1 174 ? 50.152 23.142  32.665  1.00 50.76  ? 182 ASN B N   1 
ATOM   3701 C  CA  . ASN B 1 174 ? 50.155 22.003  33.568  1.00 55.26  ? 182 ASN B CA  1 
ATOM   3702 C  C   . ASN B 1 174 ? 48.822 21.970  34.314  1.00 61.26  ? 182 ASN B C   1 
ATOM   3703 O  O   . ASN B 1 174 ? 48.268 23.016  34.645  1.00 61.24  ? 182 ASN B O   1 
ATOM   3704 C  CB  . ASN B 1 174 ? 51.351 22.065  34.522  1.00 56.10  ? 182 ASN B CB  1 
ATOM   3705 C  CG  . ASN B 1 174 ? 52.684 22.112  33.804  1.00 65.86  ? 182 ASN B CG  1 
ATOM   3706 O  OD1 . ASN B 1 174 ? 53.673 22.592  34.355  1.00 68.56  ? 182 ASN B OD1 1 
ATOM   3707 N  ND2 . ASN B 1 174 ? 52.719 21.641  32.567  1.00 53.48  ? 182 ASN B ND2 1 
ATOM   3708 N  N   . ILE B 1 175 ? 48.307 20.760  34.564  1.00 57.32  ? 183 ILE B N   1 
ATOM   3709 C  CA  . ILE B 1 175 ? 47.001 20.591  35.183  1.00 53.44  ? 183 ILE B CA  1 
ATOM   3710 C  C   . ILE B 1 175 ? 47.185 20.187  36.643  1.00 51.75  ? 183 ILE B C   1 
ATOM   3711 O  O   . ILE B 1 175 ? 47.897 19.229  36.930  1.00 52.78  ? 183 ILE B O   1 
ATOM   3712 C  CB  . ILE B 1 175 ? 46.161 19.543  34.425  1.00 57.28  ? 183 ILE B CB  1 
ATOM   3713 C  CG1 . ILE B 1 175 ? 45.738 20.029  33.036  1.00 66.43  ? 183 ILE B CG1 1 
ATOM   3714 C  CG2 . ILE B 1 175 ? 44.962 19.104  35.250  1.00 54.53  ? 183 ILE B CG2 1 
ATOM   3715 C  CD1 . ILE B 1 175 ? 46.355 19.251  31.899  1.00 71.60  ? 183 ILE B CD1 1 
ATOM   3716 N  N   . LEU B 1 176 ? 46.528 20.908  37.561  1.00 50.97  ? 184 LEU B N   1 
ATOM   3717 C  CA  . LEU B 1 176 ? 46.491 20.477  38.948  1.00 52.96  ? 184 LEU B CA  1 
ATOM   3718 C  C   . LEU B 1 176 ? 45.389 19.434  39.100  1.00 53.22  ? 184 LEU B C   1 
ATOM   3719 O  O   . LEU B 1 176 ? 44.207 19.768  39.101  1.00 57.90  ? 184 LEU B O   1 
ATOM   3720 C  CB  . LEU B 1 176 ? 46.254 21.667  39.884  1.00 60.19  ? 184 LEU B CB  1 
ATOM   3721 C  CG  . LEU B 1 176 ? 46.499 21.363  41.363  1.00 73.82  ? 184 LEU B CG  1 
ATOM   3722 C  CD1 . LEU B 1 176 ? 47.969 21.056  41.611  1.00 69.98  ? 184 LEU B CD1 1 
ATOM   3723 C  CD2 . LEU B 1 176 ? 46.038 22.510  42.250  1.00 74.38  ? 184 LEU B CD2 1 
ATOM   3724 N  N   . LEU B 1 177 ? 45.797 18.167  39.221  1.00 55.24  ? 185 LEU B N   1 
ATOM   3725 C  CA  . LEU B 1 177 ? 44.863 17.059  39.308  1.00 57.50  ? 185 LEU B CA  1 
ATOM   3726 C  C   . LEU B 1 177 ? 44.389 16.912  40.752  1.00 52.70  ? 185 LEU B C   1 
ATOM   3727 O  O   . LEU B 1 177 ? 43.266 16.481  41.003  1.00 59.72  ? 185 LEU B O   1 
ATOM   3728 C  CB  . LEU B 1 177 ? 45.573 15.794  38.815  1.00 56.18  ? 185 LEU B CB  1 
ATOM   3729 C  CG  . LEU B 1 177 ? 44.671 14.727  38.200  1.00 65.08  ? 185 LEU B CG  1 
ATOM   3730 C  CD1 . LEU B 1 177 ? 43.718 15.345  37.188  1.00 62.18  ? 185 LEU B CD1 1 
ATOM   3731 C  CD2 . LEU B 1 177 ? 45.509 13.639  37.546  1.00 62.59  ? 185 LEU B CD2 1 
ATOM   3732 N  N   . ALA B 1 178 ? 45.267 17.283  41.690  1.00 53.59  ? 186 ALA B N   1 
ATOM   3733 C  CA  . ALA B 1 178 ? 44.990 17.193  43.115  1.00 50.79  ? 186 ALA B CA  1 
ATOM   3734 C  C   . ALA B 1 178 ? 46.082 17.936  43.878  1.00 53.82  ? 186 ALA B C   1 
ATOM   3735 O  O   . ALA B 1 178 ? 47.101 18.300  43.297  1.00 49.27  ? 186 ALA B O   1 
ATOM   3736 C  CB  . ALA B 1 178 ? 44.918 15.745  43.535  1.00 55.74  ? 186 ALA B CB  1 
ATOM   3737 N  N   . GLU B 1 179 ? 45.868 18.155  45.180  1.00 53.26  ? 187 GLU B N   1 
ATOM   3738 C  CA  . GLU B 1 179 ? 46.871 18.810  46.001  1.00 57.06  ? 187 GLU B CA  1 
ATOM   3739 C  C   . GLU B 1 179 ? 48.195 18.069  45.828  1.00 51.84  ? 187 GLU B C   1 
ATOM   3740 O  O   . GLU B 1 179 ? 48.288 16.883  46.132  1.00 47.73  ? 187 GLU B O   1 
ATOM   3741 C  CB  . GLU B 1 179 ? 46.440 18.841  47.469  1.00 65.73  ? 187 GLU B CB  1 
ATOM   3742 C  CG  . GLU B 1 179 ? 47.269 19.786  48.323  1.00 66.33  ? 187 GLU B CG  1 
ATOM   3743 C  CD  . GLU B 1 179 ? 46.879 19.821  49.791  1.00 77.34  ? 187 GLU B CD  1 
ATOM   3744 O  OE1 . GLU B 1 179 ? 45.911 19.128  50.161  1.00 74.74  ? 187 GLU B OE1 1 
ATOM   3745 O  OE2 . GLU B 1 179 ? 47.548 20.540  50.560  1.00 73.96  ? 187 GLU B OE2 1 
ATOM   3746 N  N   . GLY B 1 180 ? 49.204 18.775  45.306  1.00 54.43  ? 188 GLY B N   1 
ATOM   3747 C  CA  . GLY B 1 180 ? 50.544 18.227  45.176  1.00 54.62  ? 188 GLY B CA  1 
ATOM   3748 C  C   . GLY B 1 180 ? 50.691 17.254  44.007  1.00 46.69  ? 188 GLY B C   1 
ATOM   3749 O  O   . GLY B 1 180 ? 51.698 16.557  43.920  1.00 55.72  ? 188 GLY B O   1 
ATOM   3750 N  N   . VAL B 1 181 ? 49.693 17.207  43.113  1.00 44.73  ? 189 VAL B N   1 
ATOM   3751 C  CA  . VAL B 1 181 ? 49.771 16.357  41.933  1.00 48.59  ? 189 VAL B CA  1 
ATOM   3752 C  C   . VAL B 1 181 ? 49.490 17.206  40.697  1.00 49.71  ? 189 VAL B C   1 
ATOM   3753 O  O   . VAL B 1 181 ? 48.352 17.615  40.469  1.00 45.89  ? 189 VAL B O   1 
ATOM   3754 C  CB  . VAL B 1 181 ? 48.800 15.160  41.999  1.00 48.44  ? 189 VAL B CB  1 
ATOM   3755 C  CG1 . VAL B 1 181 ? 49.044 14.184  40.857  1.00 50.51  ? 189 VAL B CG1 1 
ATOM   3756 C  CG2 . VAL B 1 181 ? 48.867 14.437  43.335  1.00 50.07  ? 189 VAL B CG2 1 
ATOM   3757 N  N   . LYS B 1 182 ? 50.534 17.447  39.897  1.00 49.16  ? 190 LYS B N   1 
ATOM   3758 C  CA  . LYS B 1 182 ? 50.410 18.264  38.702  1.00 53.75  ? 190 LYS B CA  1 
ATOM   3759 C  C   . LYS B 1 182 ? 50.789 17.426  37.481  1.00 48.47  ? 190 LYS B C   1 
ATOM   3760 O  O   . LYS B 1 182 ? 51.823 16.763  37.484  1.00 46.25  ? 190 LYS B O   1 
ATOM   3761 C  CB  . LYS B 1 182 ? 51.307 19.499  38.829  1.00 58.16  ? 190 LYS B CB  1 
ATOM   3762 C  CG  . LYS B 1 182 ? 50.748 20.780  38.225  1.00 80.07  ? 190 LYS B CG  1 
ATOM   3763 C  CD  . LYS B 1 182 ? 51.555 22.003  38.596  1.00 81.24  ? 190 LYS B CD  1 
ATOM   3764 C  CE  . LYS B 1 182 ? 53.010 21.678  38.855  1.00 87.10  ? 190 LYS B CE  1 
ATOM   3765 N  NZ  . LYS B 1 182 ? 53.741 22.840  39.414  1.00 92.41  ? 190 LYS B NZ  1 
ATOM   3766 N  N   . VAL B 1 183 ? 49.939 17.458  36.447  1.00 45.03  ? 191 VAL B N   1 
ATOM   3767 C  CA  . VAL B 1 183 ? 50.242 16.804  35.183  1.00 43.06  ? 191 VAL B CA  1 
ATOM   3768 C  C   . VAL B 1 183 ? 51.097 17.757  34.351  1.00 43.73  ? 191 VAL B C   1 
ATOM   3769 O  O   . VAL B 1 183 ? 50.677 18.875  34.066  1.00 50.75  ? 191 VAL B O   1 
ATOM   3770 C  CB  . VAL B 1 183 ? 48.964 16.401  34.421  1.00 44.25  ? 191 VAL B CB  1 
ATOM   3771 C  CG1 . VAL B 1 183 ? 49.287 15.595  33.171  1.00 52.80  ? 191 VAL B CG1 1 
ATOM   3772 C  CG2 . VAL B 1 183 ? 47.986 15.641  35.303  1.00 44.24  ? 191 VAL B CG2 1 
ATOM   3773 N  N   . LEU B 1 184 ? 52.296 17.305  33.967  1.00 46.18  ? 192 LEU B N   1 
ATOM   3774 C  CA  . LEU B 1 184 ? 53.228 18.130  33.215  1.00 46.17  ? 192 LEU B CA  1 
ATOM   3775 C  C   . LEU B 1 184 ? 53.100 17.814  31.725  1.00 45.72  ? 192 LEU B C   1 
ATOM   3776 O  O   . LEU B 1 184 ? 53.238 16.664  31.320  1.00 42.32  ? 192 LEU B O   1 
ATOM   3777 C  CB  . LEU B 1 184 ? 54.648 17.850  33.721  1.00 47.25  ? 192 LEU B CB  1 
ATOM   3778 C  CG  . LEU B 1 184 ? 54.831 17.897  35.238  1.00 58.77  ? 192 LEU B CG  1 
ATOM   3779 C  CD1 . LEU B 1 184 ? 56.210 17.393  35.635  1.00 53.98  ? 192 LEU B CD1 1 
ATOM   3780 C  CD2 . LEU B 1 184 ? 54.609 19.305  35.772  1.00 61.05  ? 192 LEU B CD2 1 
ATOM   3781 N  N   . ASN B 1 185 ? 52.832 18.845  30.914  1.00 48.96  ? 193 ASN B N   1 
ATOM   3782 C  CA  . ASN B 1 185 ? 52.719 18.694  29.470  1.00 45.38  ? 193 ASN B CA  1 
ATOM   3783 C  C   . ASN B 1 185 ? 54.097 18.861  28.836  1.00 44.79  ? 193 ASN B C   1 
ATOM   3784 O  O   . ASN B 1 185 ? 54.517 19.981  28.557  1.00 42.70  ? 193 ASN B O   1 
ATOM   3785 C  CB  . ASN B 1 185 ? 51.732 19.706  28.877  1.00 49.24  ? 193 ASN B CB  1 
ATOM   3786 C  CG  . ASN B 1 185 ? 51.500 19.533  27.390  1.00 43.26  ? 193 ASN B CG  1 
ATOM   3787 O  OD1 . ASN B 1 185 ? 52.069 18.641  26.763  1.00 43.97  ? 193 ASN B OD1 1 
ATOM   3788 N  ND2 . ASN B 1 185 ? 50.663 20.384  26.821  1.00 47.83  ? 193 ASN B ND2 1 
ATOM   3789 N  N   . PHE B 1 186 ? 54.786 17.738  28.604  1.00 46.69  ? 194 PHE B N   1 
ATOM   3790 C  CA  . PHE B 1 186 ? 56.122 17.759  28.030  1.00 48.79  ? 194 PHE B CA  1 
ATOM   3791 C  C   . PHE B 1 186 ? 56.035 17.970  26.520  1.00 49.02  ? 194 PHE B C   1 
ATOM   3792 O  O   . PHE B 1 186 ? 56.960 18.496  25.906  1.00 45.43  ? 194 PHE B O   1 
ATOM   3793 C  CB  . PHE B 1 186 ? 56.875 16.462  28.339  1.00 53.45  ? 194 PHE B CB  1 
ATOM   3794 C  CG  . PHE B 1 186 ? 57.192 16.229  29.796  1.00 48.82  ? 194 PHE B CG  1 
ATOM   3795 C  CD1 . PHE B 1 186 ? 57.478 17.289  30.642  1.00 46.57  ? 194 PHE B CD1 1 
ATOM   3796 C  CD2 . PHE B 1 186 ? 57.253 14.943  30.307  1.00 44.29  ? 194 PHE B CD2 1 
ATOM   3797 C  CE1 . PHE B 1 186 ? 57.782 17.067  31.976  1.00 42.47  ? 194 PHE B CE1 1 
ATOM   3798 C  CE2 . PHE B 1 186 ? 57.561 14.724  31.640  1.00 47.47  ? 194 PHE B CE2 1 
ATOM   3799 C  CZ  . PHE B 1 186 ? 57.823 15.786  32.472  1.00 46.93  ? 194 PHE B CZ  1 
ATOM   3800 N  N   . GLY B 1 187 ? 54.917 17.539  25.929  1.00 50.27  ? 195 GLY B N   1 
ATOM   3801 C  CA  . GLY B 1 187 ? 54.690 17.697  24.502  1.00 44.69  ? 195 GLY B CA  1 
ATOM   3802 C  C   . GLY B 1 187 ? 55.459 16.669  23.674  1.00 45.57  ? 195 GLY B C   1 
ATOM   3803 O  O   . GLY B 1 187 ? 55.737 15.569  24.144  1.00 49.99  ? 195 GLY B O   1 
ATOM   3804 N  N   . SER B 1 188 ? 55.801 17.051  22.437  1.00 44.84  ? 196 SER B N   1 
ATOM   3805 C  CA  . SER B 1 188 ? 56.424 16.151  21.478  1.00 44.75  ? 196 SER B CA  1 
ATOM   3806 C  C   . SER B 1 188 ? 57.878 15.882  21.860  1.00 41.66  ? 196 SER B C   1 
ATOM   3807 O  O   . SER B 1 188 ? 58.574 16.773  22.339  1.00 39.02  ? 196 SER B O   1 
ATOM   3808 C  CB  . SER B 1 188 ? 56.320 16.700  20.073  1.00 44.96  ? 196 SER B CB  1 
ATOM   3809 O  OG  . SER B 1 188 ? 56.798 18.036  20.004  1.00 52.15  ? 196 SER B OG  1 
ATOM   3810 N  N   . GLY B 1 189 ? 58.319 14.643  21.616  1.00 39.99  ? 197 GLY B N   1 
ATOM   3811 C  CA  . GLY B 1 189 ? 59.678 14.215  21.900  1.00 43.49  ? 197 GLY B CA  1 
ATOM   3812 C  C   . GLY B 1 189 ? 59.868 12.742  21.546  1.00 43.35  ? 197 GLY B C   1 
ATOM   3813 O  O   . GLY B 1 189 ? 59.952 12.389  20.374  1.00 49.35  ? 197 GLY B O   1 
ATOM   3814 N  N   . HIS B 1 190 ? 59.919 11.890  22.577  1.00 42.34  ? 198 HIS B N   1 
ATOM   3815 C  CA  . HIS B 1 190 ? 59.973 10.447  22.404  1.00 41.34  ? 198 HIS B CA  1 
ATOM   3816 C  C   . HIS B 1 190 ? 58.797 9.999   21.541  1.00 37.73  ? 198 HIS B C   1 
ATOM   3817 O  O   . HIS B 1 190 ? 58.953 9.167   20.653  1.00 41.74  ? 198 HIS B O   1 
ATOM   3818 C  CB  . HIS B 1 190 ? 59.971 9.771   23.780  1.00 41.30  ? 198 HIS B CB  1 
ATOM   3819 C  CG  . HIS B 1 190 ? 59.679 8.306   23.791  1.00 43.18  ? 198 HIS B CG  1 
ATOM   3820 N  ND1 . HIS B 1 190 ? 60.577 7.339   23.394  1.00 48.91  ? 198 HIS B ND1 1 
ATOM   3821 C  CD2 . HIS B 1 190 ? 58.591 7.647   24.215  1.00 42.68  ? 198 HIS B CD2 1 
ATOM   3822 C  CE1 . HIS B 1 190 ? 60.028 6.142   23.549  1.00 49.82  ? 198 HIS B CE1 1 
ATOM   3823 N  NE2 . HIS B 1 190 ? 58.823 6.306   24.049  1.00 42.71  ? 198 HIS B NE2 1 
ATOM   3824 N  N   . ALA B 1 191 ? 57.619 10.562  21.829  1.00 43.08  ? 199 ALA B N   1 
ATOM   3825 C  CA  . ALA B 1 191 ? 56.408 10.273  21.078  1.00 41.92  ? 199 ALA B CA  1 
ATOM   3826 C  C   . ALA B 1 191 ? 55.735 11.584  20.679  1.00 37.75  ? 199 ALA B C   1 
ATOM   3827 O  O   . ALA B 1 191 ? 56.315 12.653  20.847  1.00 45.43  ? 199 ALA B O   1 
ATOM   3828 C  CB  . ALA B 1 191 ? 55.494 9.405   21.906  1.00 41.06  ? 199 ALA B CB  1 
ATOM   3829 N  N   . TRP B 1 192 ? 54.507 11.493  20.153  1.00 45.78  ? 200 TRP B N   1 
ATOM   3830 C  CA  . TRP B 1 192 ? 53.789 12.662  19.666  1.00 46.85  ? 200 TRP B CA  1 
ATOM   3831 C  C   . TRP B 1 192 ? 53.474 13.613  20.817  1.00 43.78  ? 200 TRP B C   1 
ATOM   3832 O  O   . TRP B 1 192 ? 53.609 14.825  20.674  1.00 42.06  ? 200 TRP B O   1 
ATOM   3833 C  CB  . TRP B 1 192 ? 52.496 12.255  18.943  1.00 41.51  ? 200 TRP B CB  1 
ATOM   3834 C  CG  . TRP B 1 192 ? 52.700 11.393  17.726  1.00 44.51  ? 200 TRP B CG  1 
ATOM   3835 C  CD1 . TRP B 1 192 ? 53.381 11.708  16.587  1.00 48.00  ? 200 TRP B CD1 1 
ATOM   3836 C  CD2 . TRP B 1 192 ? 52.192 10.055  17.531  1.00 46.60  ? 200 TRP B CD2 1 
ATOM   3837 N  NE1 . TRP B 1 192 ? 53.340 10.662  15.704  1.00 46.48  ? 200 TRP B NE1 1 
ATOM   3838 C  CE2 . TRP B 1 192 ? 52.617 9.636   16.252  1.00 50.56  ? 200 TRP B CE2 1 
ATOM   3839 C  CE3 . TRP B 1 192 ? 51.427 9.180   18.308  1.00 48.97  ? 200 TRP B CE3 1 
ATOM   3840 C  CZ2 . TRP B 1 192 ? 52.300 8.380   15.740  1.00 48.55  ? 200 TRP B CZ2 1 
ATOM   3841 C  CZ3 . TRP B 1 192 ? 51.112 7.940   17.799  1.00 48.08  ? 200 TRP B CZ3 1 
ATOM   3842 C  CH2 . TRP B 1 192 ? 51.545 7.547   16.533  1.00 49.70  ? 200 TRP B CH2 1 
ATOM   3843 N  N   . GLY B 1 193 ? 53.034 13.051  21.949  1.00 44.69  ? 201 GLY B N   1 
ATOM   3844 C  CA  . GLY B 1 193 ? 52.634 13.851  23.096  1.00 44.40  ? 201 GLY B CA  1 
ATOM   3845 C  C   . GLY B 1 193 ? 52.961 13.161  24.418  1.00 47.49  ? 201 GLY B C   1 
ATOM   3846 O  O   . GLY B 1 193 ? 52.341 12.159  24.767  1.00 50.72  ? 201 GLY B O   1 
ATOM   3847 N  N   . MET B 1 194 ? 53.926 13.723  25.155  1.00 44.05  ? 202 MET B N   1 
ATOM   3848 C  CA  . MET B 1 194 ? 54.393 13.123  26.394  1.00 43.94  ? 202 MET B CA  1 
ATOM   3849 C  C   . MET B 1 194 ? 53.815 13.893  27.581  1.00 43.70  ? 202 MET B C   1 
ATOM   3850 O  O   . MET B 1 194 ? 53.844 15.121  27.607  1.00 40.71  ? 202 MET B O   1 
ATOM   3851 C  CB  . MET B 1 194 ? 55.925 13.145  26.464  1.00 39.93  ? 202 MET B CB  1 
ATOM   3852 C  CG  . MET B 1 194 ? 56.590 12.438  25.296  1.00 40.91  ? 202 MET B CG  1 
ATOM   3853 S  SD  . MET B 1 194 ? 56.251 10.661  25.244  1.00 49.61  ? 202 MET B SD  1 
ATOM   3854 C  CE  . MET B 1 194 ? 57.023 10.123  26.769  1.00 53.50  ? 202 MET B CE  1 
ATOM   3855 N  N   . LEU B 1 195 ? 53.280 13.155  28.560  1.00 43.19  ? 203 LEU B N   1 
ATOM   3856 C  CA  . LEU B 1 195 ? 52.806 13.741  29.803  1.00 41.04  ? 203 LEU B CA  1 
ATOM   3857 C  C   . LEU B 1 195 ? 53.668 13.229  30.955  1.00 46.75  ? 203 LEU B C   1 
ATOM   3858 O  O   . LEU B 1 195 ? 54.106 12.079  30.942  1.00 39.12  ? 203 LEU B O   1 
ATOM   3859 C  CB  . LEU B 1 195 ? 51.335 13.363  30.017  1.00 42.25  ? 203 LEU B CB  1 
ATOM   3860 C  CG  . LEU B 1 195 ? 50.324 14.003  29.066  1.00 42.57  ? 203 LEU B CG  1 
ATOM   3861 C  CD1 . LEU B 1 195 ? 48.903 13.696  29.517  1.00 43.04  ? 203 LEU B CD1 1 
ATOM   3862 C  CD2 . LEU B 1 195 ? 50.535 15.507  28.964  1.00 41.40  ? 203 LEU B CD2 1 
ATOM   3863 N  N   . GLY B 1 196 ? 53.908 14.094  31.946  1.00 46.52  ? 204 GLY B N   1 
ATOM   3864 C  CA  . GLY B 1 196 ? 54.597 13.699  33.164  1.00 43.50  ? 204 GLY B CA  1 
ATOM   3865 C  C   . GLY B 1 196 ? 53.793 14.085  34.403  1.00 41.26  ? 204 GLY B C   1 
ATOM   3866 O  O   . GLY B 1 196 ? 52.773 14.759  34.290  1.00 45.12  ? 204 GLY B O   1 
ATOM   3867 N  N   . LEU B 1 197 ? 54.251 13.635  35.578  1.00 45.53  ? 205 LEU B N   1 
ATOM   3868 C  CA  . LEU B 1 197 ? 53.653 14.032  36.843  1.00 45.18  ? 205 LEU B CA  1 
ATOM   3869 C  C   . LEU B 1 197 ? 54.708 14.711  37.708  1.00 48.47  ? 205 LEU B C   1 
ATOM   3870 O  O   . LEU B 1 197 ? 55.850 14.262  37.770  1.00 40.21  ? 205 LEU B O   1 
ATOM   3871 C  CB  . LEU B 1 197 ? 53.113 12.806  37.588  1.00 46.86  ? 205 LEU B CB  1 
ATOM   3872 C  CG  . LEU B 1 197 ? 51.613 12.518  37.511  1.00 48.04  ? 205 LEU B CG  1 
ATOM   3873 C  CD1 . LEU B 1 197 ? 51.180 11.747  38.748  1.00 48.27  ? 205 LEU B CD1 1 
ATOM   3874 C  CD2 . LEU B 1 197 ? 50.780 13.783  37.366  1.00 52.97  ? 205 LEU B CD2 1 
ATOM   3875 N  N   . HIS B 1 198 ? 54.301 15.788  38.384  1.00 48.77  ? 206 HIS B N   1 
ATOM   3876 C  CA  . HIS B 1 198 ? 55.028 16.269  39.545  1.00 50.34  ? 206 HIS B CA  1 
ATOM   3877 C  C   . HIS B 1 198 ? 54.188 15.988  40.786  1.00 52.33  ? 206 HIS B C   1 
ATOM   3878 O  O   . HIS B 1 198 ? 53.068 16.481  40.911  1.00 51.34  ? 206 HIS B O   1 
ATOM   3879 C  CB  . HIS B 1 198 ? 55.358 17.761  39.447  1.00 57.81  ? 206 HIS B CB  1 
ATOM   3880 C  CG  . HIS B 1 198 ? 56.198 18.219  40.593  1.00 64.94  ? 206 HIS B CG  1 
ATOM   3881 N  ND1 . HIS B 1 198 ? 55.678 18.855  41.700  1.00 75.92  ? 206 HIS B ND1 1 
ATOM   3882 C  CD2 . HIS B 1 198 ? 57.508 18.071  40.832  1.00 65.16  ? 206 HIS B CD2 1 
ATOM   3883 C  CE1 . HIS B 1 198 ? 56.657 19.108  42.558  1.00 77.95  ? 206 HIS B CE1 1 
ATOM   3884 N  NE2 . HIS B 1 198 ? 57.777 18.642  42.049  1.00 74.61  ? 206 HIS B NE2 1 
ATOM   3885 N  N   . VAL B 1 199 ? 54.743 15.175  41.689  1.00 51.87  ? 207 VAL B N   1 
ATOM   3886 C  CA  . VAL B 1 199 ? 54.091 14.860  42.948  1.00 50.57  ? 207 VAL B CA  1 
ATOM   3887 C  C   . VAL B 1 199 ? 54.874 15.524  44.076  1.00 46.15  ? 207 VAL B C   1 
ATOM   3888 O  O   . VAL B 1 199 ? 56.087 15.350  44.179  1.00 45.07  ? 207 VAL B O   1 
ATOM   3889 C  CB  . VAL B 1 199 ? 53.994 13.338  43.168  1.00 45.94  ? 207 VAL B CB  1 
ATOM   3890 C  CG1 . VAL B 1 199 ? 53.202 13.007  44.423  1.00 46.24  ? 207 VAL B CG1 1 
ATOM   3891 C  CG2 . VAL B 1 199 ? 53.406 12.626  41.960  1.00 47.01  ? 207 VAL B CG2 1 
ATOM   3892 N  N   . GLU B 1 200 ? 54.166 16.290  44.911  1.00 44.83  ? 208 GLU B N   1 
ATOM   3893 C  CA  . GLU B 1 200 ? 54.749 16.843  46.122  1.00 57.70  ? 208 GLU B CA  1 
ATOM   3894 C  C   . GLU B 1 200 ? 54.230 16.038  47.312  1.00 55.97  ? 208 GLU B C   1 
ATOM   3895 O  O   . GLU B 1 200 ? 53.063 16.149  47.680  1.00 46.87  ? 208 GLU B O   1 
ATOM   3896 C  CB  . GLU B 1 200 ? 54.417 18.333  46.237  1.00 57.06  ? 208 GLU B CB  1 
ATOM   3897 C  CG  . GLU B 1 200 ? 55.211 19.060  47.310  1.00 66.61  ? 208 GLU B CG  1 
ATOM   3898 C  CD  . GLU B 1 200 ? 56.718 19.043  47.113  1.00 73.36  ? 208 GLU B CD  1 
ATOM   3899 O  OE1 . GLU B 1 200 ? 57.168 19.326  45.985  1.00 78.79  ? 208 GLU B OE1 1 
ATOM   3900 O  OE2 . GLU B 1 200 ? 57.438 18.763  48.092  1.00 74.55  ? 208 GLU B OE2 1 
ATOM   3901 N  N   . LEU B 1 201 ? 55.107 15.208  47.888  1.00 53.61  ? 209 LEU B N   1 
ATOM   3902 C  CA  . LEU B 1 201 ? 54.745 14.351  49.007  1.00 56.71  ? 209 LEU B CA  1 
ATOM   3903 C  C   . LEU B 1 201 ? 55.212 14.991  50.310  1.00 54.56  ? 209 LEU B C   1 
ATOM   3904 O  O   . LEU B 1 201 ? 56.344 15.458  50.409  1.00 56.28  ? 209 LEU B O   1 
ATOM   3905 C  CB  . LEU B 1 201 ? 55.380 12.971  48.813  1.00 59.79  ? 209 LEU B CB  1 
ATOM   3906 C  CG  . LEU B 1 201 ? 54.607 12.004  47.919  1.00 57.92  ? 209 LEU B CG  1 
ATOM   3907 C  CD1 . LEU B 1 201 ? 55.422 10.751  47.649  1.00 63.77  ? 209 LEU B CD1 1 
ATOM   3908 C  CD2 . LEU B 1 201 ? 53.270 11.638  48.545  1.00 69.90  ? 209 LEU B CD2 1 
ATOM   3909 N  N   . PRO B 1 202 ? 54.348 15.029  51.349  1.00 55.98  ? 210 PRO B N   1 
ATOM   3910 C  CA  . PRO B 1 202 ? 54.695 15.662  52.621  1.00 60.27  ? 210 PRO B CA  1 
ATOM   3911 C  C   . PRO B 1 202 ? 56.056 15.251  53.177  1.00 61.94  ? 210 PRO B C   1 
ATOM   3912 O  O   . PRO B 1 202 ? 56.796 16.095  53.675  1.00 57.09  ? 210 PRO B O   1 
ATOM   3913 C  CB  . PRO B 1 202 ? 53.559 15.208  53.549  1.00 61.15  ? 210 PRO B CB  1 
ATOM   3914 C  CG  . PRO B 1 202 ? 52.378 15.043  52.617  1.00 63.08  ? 210 PRO B CG  1 
ATOM   3915 C  CD  . PRO B 1 202 ? 52.979 14.488  51.342  1.00 57.30  ? 210 PRO B CD  1 
ATOM   3916 N  N   . GLU B 1 203 ? 56.389 13.957  53.087  1.00 58.33  ? 211 GLU B N   1 
ATOM   3917 C  CA  . GLU B 1 203 ? 57.604 13.458  53.710  1.00 66.59  ? 211 GLU B CA  1 
ATOM   3918 C  C   . GLU B 1 203 ? 58.696 13.246  52.662  1.00 62.83  ? 211 GLU B C   1 
ATOM   3919 O  O   . GLU B 1 203 ? 59.827 13.686  52.858  1.00 59.36  ? 211 GLU B O   1 
ATOM   3920 C  CB  . GLU B 1 203 ? 57.329 12.170  54.489  1.00 69.82  ? 211 GLU B CB  1 
ATOM   3921 C  CG  . GLU B 1 203 ? 56.211 12.301  55.510  1.00 97.65  ? 211 GLU B CG  1 
ATOM   3922 C  CD  . GLU B 1 203 ? 56.306 13.513  56.424  1.00 118.46 ? 211 GLU B CD  1 
ATOM   3923 O  OE1 . GLU B 1 203 ? 55.308 14.257  56.522  1.00 108.04 ? 211 GLU B OE1 1 
ATOM   3924 O  OE2 . GLU B 1 203 ? 57.377 13.711  57.033  1.00 118.69 ? 211 GLU B OE2 1 
ATOM   3925 N  N   . THR B 1 204 ? 58.362 12.564  51.561  1.00 59.51  ? 212 THR B N   1 
ATOM   3926 C  CA  . THR B 1 204 ? 59.361 12.198  50.569  1.00 54.81  ? 212 THR B CA  1 
ATOM   3927 C  C   . THR B 1 204 ? 59.831 13.448  49.828  1.00 55.35  ? 212 THR B C   1 
ATOM   3928 O  O   . THR B 1 204 ? 60.985 13.532  49.413  1.00 52.22  ? 212 THR B O   1 
ATOM   3929 C  CB  . THR B 1 204 ? 58.827 11.128  49.608  1.00 62.99  ? 212 THR B CB  1 
ATOM   3930 O  OG1 . THR B 1 204 ? 58.358 10.032  50.394  1.00 65.77  ? 212 THR B OG1 1 
ATOM   3931 C  CG2 . THR B 1 204 ? 59.870 10.645  48.623  1.00 63.16  ? 212 THR B CG2 1 
ATOM   3932 N  N   . GLY B 1 205 ? 58.927 14.421  49.676  1.00 52.37  ? 213 GLY B N   1 
ATOM   3933 C  CA  . GLY B 1 205 ? 59.228 15.636  48.938  1.00 50.46  ? 213 GLY B CA  1 
ATOM   3934 C  C   . GLY B 1 205 ? 58.733 15.550  47.497  1.00 48.53  ? 213 GLY B C   1 
ATOM   3935 O  O   . GLY B 1 205 ? 57.716 14.916  47.226  1.00 45.49  ? 213 GLY B O   1 
ATOM   3936 N  N   . GLY B 1 206 ? 59.475 16.181  46.580  1.00 44.94  ? 214 GLY B N   1 
ATOM   3937 C  CA  . GLY B 1 206 ? 59.059 16.296  45.192  1.00 42.61  ? 214 GLY B CA  1 
ATOM   3938 C  C   . GLY B 1 206 ? 59.552 15.131  44.337  1.00 42.26  ? 214 GLY B C   1 
ATOM   3939 O  O   . GLY B 1 206 ? 60.692 14.691  44.468  1.00 46.67  ? 214 GLY B O   1 
ATOM   3940 N  N   . ILE B 1 207 ? 58.675 14.651  43.450  1.00 43.97  ? 215 ILE B N   1 
ATOM   3941 C  CA  . ILE B 1 207 ? 59.003 13.566  42.540  1.00 45.37  ? 215 ILE B CA  1 
ATOM   3942 C  C   . ILE B 1 207 ? 58.491 13.917  41.147  1.00 46.66  ? 215 ILE B C   1 
ATOM   3943 O  O   . ILE B 1 207 ? 57.322 14.260  40.982  1.00 46.62  ? 215 ILE B O   1 
ATOM   3944 C  CB  . ILE B 1 207 ? 58.396 12.237  43.033  1.00 46.82  ? 215 ILE B CB  1 
ATOM   3945 C  CG1 . ILE B 1 207 ? 58.950 11.822  44.398  1.00 55.07  ? 215 ILE B CG1 1 
ATOM   3946 C  CG2 . ILE B 1 207 ? 58.591 11.143  41.994  1.00 47.92  ? 215 ILE B CG2 1 
ATOM   3947 C  CD1 . ILE B 1 207 ? 58.173 10.703  45.054  1.00 57.74  ? 215 ILE B CD1 1 
ATOM   3948 N  N   . ILE B 1 208 ? 59.375 13.819  40.147  1.00 47.67  ? 216 ILE B N   1 
ATOM   3949 C  CA  . ILE B 1 208 ? 58.964 13.930  38.758  1.00 47.03  ? 216 ILE B CA  1 
ATOM   3950 C  C   . ILE B 1 208 ? 58.939 12.538  38.138  1.00 49.25  ? 216 ILE B C   1 
ATOM   3951 O  O   . ILE B 1 208 ? 59.962 11.859  38.074  1.00 43.51  ? 216 ILE B O   1 
ATOM   3952 C  CB  . ILE B 1 208 ? 59.883 14.874  37.958  1.00 46.38  ? 216 ILE B CB  1 
ATOM   3953 C  CG1 . ILE B 1 208 ? 59.801 16.318  38.458  1.00 49.35  ? 216 ILE B CG1 1 
ATOM   3954 C  CG2 . ILE B 1 208 ? 59.568 14.781  36.473  1.00 40.95  ? 216 ILE B CG2 1 
ATOM   3955 C  CD1 . ILE B 1 208 ? 60.955 17.184  38.006  1.00 58.49  ? 216 ILE B CD1 1 
ATOM   3956 N  N   . LEU B 1 209 ? 57.749 12.130  37.690  1.00 47.26  ? 217 LEU B N   1 
ATOM   3957 C  CA  . LEU B 1 209 ? 57.598 10.946  36.866  1.00 45.34  ? 217 LEU B CA  1 
ATOM   3958 C  C   . LEU B 1 209 ? 57.768 11.357  35.407  1.00 43.85  ? 217 LEU B C   1 
ATOM   3959 O  O   . LEU B 1 209 ? 56.895 12.005  34.836  1.00 45.36  ? 217 LEU B O   1 
ATOM   3960 C  CB  . LEU B 1 209 ? 56.219 10.332  37.124  1.00 44.53  ? 217 LEU B CB  1 
ATOM   3961 C  CG  . LEU B 1 209 ? 55.932 9.974   38.580  1.00 47.25  ? 217 LEU B CG  1 
ATOM   3962 C  CD1 . LEU B 1 209 ? 54.570 9.314   38.717  1.00 49.87  ? 217 LEU B CD1 1 
ATOM   3963 C  CD2 . LEU B 1 209 ? 57.022 9.072   39.143  1.00 51.04  ? 217 LEU B CD2 1 
ATOM   3964 N  N   . ALA B 1 210 ? 58.913 10.980  34.830  1.00 47.32  ? 218 ALA B N   1 
ATOM   3965 C  CA  . ALA B 1 210 ? 59.308 11.429  33.505  1.00 44.43  ? 218 ALA B CA  1 
ATOM   3966 C  C   . ALA B 1 210 ? 58.825 10.453  32.435  1.00 47.59  ? 218 ALA B C   1 
ATOM   3967 O  O   . ALA B 1 210 ? 58.680 10.830  31.274  1.00 44.69  ? 218 ALA B O   1 
ATOM   3968 C  CB  . ALA B 1 210 ? 60.807 11.583  33.453  1.00 52.17  ? 218 ALA B CB  1 
ATOM   3969 N  N   . SER B 1 211 ? 58.590 9.197   32.832  1.00 43.61  ? 219 SER B N   1 
ATOM   3970 C  CA  . SER B 1 211 ? 58.277 8.141   31.882  1.00 43.78  ? 219 SER B CA  1 
ATOM   3971 C  C   . SER B 1 211 ? 59.348 8.120   30.790  1.00 43.70  ? 219 SER B C   1 
ATOM   3972 O  O   . SER B 1 211 ? 60.532 8.234   31.098  1.00 44.43  ? 219 SER B O   1 
ATOM   3973 C  CB  . SER B 1 211 ? 56.881 8.299   31.326  1.00 46.73  ? 219 SER B CB  1 
ATOM   3974 O  OG  . SER B 1 211 ? 56.562 7.241   30.431  1.00 44.51  ? 219 SER B OG  1 
ATOM   3975 N  N   . ASP B 1 212 ? 58.942 7.992   29.520  1.00 41.18  ? 220 ASP B N   1 
ATOM   3976 C  CA  . ASP B 1 212 ? 59.903 7.778   28.447  1.00 48.01  ? 220 ASP B CA  1 
ATOM   3977 C  C   . ASP B 1 212 ? 60.469 9.104   27.941  1.00 43.21  ? 220 ASP B C   1 
ATOM   3978 O  O   . ASP B 1 212 ? 61.242 9.116   26.986  1.00 47.90  ? 220 ASP B O   1 
ATOM   3979 C  CB  . ASP B 1 212 ? 59.305 6.976   27.288  1.00 52.06  ? 220 ASP B CB  1 
ATOM   3980 C  CG  . ASP B 1 212 ? 59.156 5.489   27.569  1.00 51.63  ? 220 ASP B CG  1 
ATOM   3981 O  OD1 . ASP B 1 212 ? 59.566 5.052   28.663  1.00 49.45  ? 220 ASP B OD1 1 
ATOM   3982 O  OD2 . ASP B 1 212 ? 58.632 4.780   26.688  1.00 60.09  ? 220 ASP B OD2 1 
ATOM   3983 N  N   . ALA B 1 213 ? 60.091 10.217  28.576  1.00 41.96  ? 221 ALA B N   1 
ATOM   3984 C  CA  . ALA B 1 213 ? 60.775 11.478  28.340  1.00 44.69  ? 221 ALA B CA  1 
ATOM   3985 C  C   . ALA B 1 213 ? 62.258 11.316  28.675  1.00 46.97  ? 221 ALA B C   1 
ATOM   3986 O  O   . ALA B 1 213 ? 63.113 11.910  28.022  1.00 48.47  ? 221 ALA B O   1 
ATOM   3987 C  CB  . ALA B 1 213 ? 60.132 12.583  29.143  1.00 46.03  ? 221 ALA B CB  1 
ATOM   3988 N  N   . ILE B 1 214 ? 62.551 10.507  29.702  1.00 52.53  ? 222 ILE B N   1 
ATOM   3989 C  CA  . ILE B 1 214 ? 63.915 10.097  30.002  1.00 48.41  ? 222 ILE B CA  1 
ATOM   3990 C  C   . ILE B 1 214 ? 63.918 8.604   30.323  1.00 52.57  ? 222 ILE B C   1 
ATOM   3991 O  O   . ILE B 1 214 ? 63.418 8.188   31.366  1.00 51.02  ? 222 ILE B O   1 
ATOM   3992 C  CB  . ILE B 1 214 ? 64.523 10.899  31.170  1.00 54.26  ? 222 ILE B CB  1 
ATOM   3993 C  CG1 . ILE B 1 214 ? 64.245 12.401  31.069  1.00 54.72  ? 222 ILE B CG1 1 
ATOM   3994 C  CG2 . ILE B 1 214 ? 66.013 10.607  31.282  1.00 52.94  ? 222 ILE B CG2 1 
ATOM   3995 C  CD1 . ILE B 1 214 ? 64.478 13.148  32.363  1.00 50.08  ? 222 ILE B CD1 1 
ATOM   3996 N  N   . TYR B 1 215 ? 64.504 7.810   29.422  1.00 49.62  ? 223 TYR B N   1 
ATOM   3997 C  CA  . TYR B 1 215 ? 64.586 6.368   29.593  1.00 53.69  ? 223 TYR B CA  1 
ATOM   3998 C  C   . TYR B 1 215 ? 65.377 6.023   30.855  1.00 52.56  ? 223 TYR B C   1 
ATOM   3999 O  O   . TYR B 1 215 ? 64.902 5.256   31.690  1.00 47.84  ? 223 TYR B O   1 
ATOM   4000 C  CB  . TYR B 1 215 ? 65.255 5.737   28.367  1.00 55.66  ? 223 TYR B CB  1 
ATOM   4001 C  CG  . TYR B 1 215 ? 64.354 5.265   27.231  1.00 52.25  ? 223 TYR B CG  1 
ATOM   4002 C  CD1 . TYR B 1 215 ? 63.024 4.919   27.438  1.00 57.09  ? 223 TYR B CD1 1 
ATOM   4003 C  CD2 . TYR B 1 215 ? 64.853 5.158   25.939  1.00 55.13  ? 223 TYR B CD2 1 
ATOM   4004 C  CE1 . TYR B 1 215 ? 62.223 4.478   26.396  1.00 52.69  ? 223 TYR B CE1 1 
ATOM   4005 C  CE2 . TYR B 1 215 ? 64.063 4.721   24.889  1.00 52.30  ? 223 TYR B CE2 1 
ATOM   4006 C  CZ  . TYR B 1 215 ? 62.743 4.380   25.118  1.00 54.24  ? 223 TYR B CZ  1 
ATOM   4007 O  OH  . TYR B 1 215 ? 61.959 3.947   24.087  1.00 53.62  ? 223 TYR B OH  1 
ATOM   4008 N  N   . THR B 1 216 ? 66.589 6.584   30.976  1.00 47.51  ? 224 THR B N   1 
ATOM   4009 C  CA  . THR B 1 216 ? 67.534 6.171   32.004  1.00 48.63  ? 224 THR B CA  1 
ATOM   4010 C  C   . THR B 1 216 ? 68.449 7.322   32.410  1.00 52.21  ? 224 THR B C   1 
ATOM   4011 O  O   . THR B 1 216 ? 68.443 8.384   31.792  1.00 52.38  ? 224 THR B O   1 
ATOM   4012 C  CB  . THR B 1 216 ? 68.451 5.036   31.528  1.00 51.56  ? 224 THR B CB  1 
ATOM   4013 O  OG1 . THR B 1 216 ? 69.334 5.570   30.541  1.00 52.05  ? 224 THR B OG1 1 
ATOM   4014 C  CG2 . THR B 1 216 ? 67.703 3.852   30.958  1.00 49.14  ? 224 THR B CG2 1 
ATOM   4015 N  N   . ALA B 1 217 ? 69.262 7.063   33.442  1.00 55.69  ? 225 ALA B N   1 
ATOM   4016 C  CA  . ALA B 1 217 ? 70.226 8.021   33.954  1.00 59.74  ? 225 ALA B CA  1 
ATOM   4017 C  C   . ALA B 1 217 ? 71.277 8.307   32.886  1.00 53.40  ? 225 ALA B C   1 
ATOM   4018 O  O   . ALA B 1 217 ? 71.856 9.391   32.847  1.00 60.35  ? 225 ALA B O   1 
ATOM   4019 C  CB  . ALA B 1 217 ? 70.849 7.482   35.221  1.00 57.03  ? 225 ALA B CB  1 
ATOM   4020 N  N   . GLU B 1 218 ? 71.507 7.315   32.022  1.00 53.58  ? 226 GLU B N   1 
ATOM   4021 C  CA  . GLU B 1 218 ? 72.432 7.451   30.910  1.00 60.80  ? 226 GLU B CA  1 
ATOM   4022 C  C   . GLU B 1 218 ? 71.847 8.442   29.906  1.00 60.90  ? 226 GLU B C   1 
ATOM   4023 O  O   . GLU B 1 218 ? 72.565 9.268   29.346  1.00 52.21  ? 226 GLU B O   1 
ATOM   4024 C  CB  . GLU B 1 218 ? 72.681 6.083   30.269  1.00 61.05  ? 226 GLU B CB  1 
ATOM   4025 C  CG  . GLU B 1 218 ? 74.005 5.991   29.531  1.00 73.78  ? 226 GLU B CG  1 
ATOM   4026 C  CD  . GLU B 1 218 ? 74.133 4.809   28.584  1.00 72.00  ? 226 GLU B CD  1 
ATOM   4027 O  OE1 . GLU B 1 218 ? 73.322 3.867   28.697  1.00 81.52  ? 226 GLU B OE1 1 
ATOM   4028 O  OE2 . GLU B 1 218 ? 75.031 4.844   27.720  1.00 69.55  ? 226 GLU B OE2 1 
ATOM   4029 N  N   . SER B 1 219 ? 70.530 8.342   29.690  1.00 55.43  ? 227 SER B N   1 
ATOM   4030 C  CA  . SER B 1 219 ? 69.809 9.271   28.836  1.00 60.40  ? 227 SER B CA  1 
ATOM   4031 C  C   . SER B 1 219 ? 69.950 10.689  29.386  1.00 50.31  ? 227 SER B C   1 
ATOM   4032 O  O   . SER B 1 219 ? 70.156 11.638  28.634  1.00 50.08  ? 227 SER B O   1 
ATOM   4033 C  CB  . SER B 1 219 ? 68.355 8.878   28.722  1.00 55.77  ? 227 SER B CB  1 
ATOM   4034 O  OG  . SER B 1 219 ? 68.222 7.541   28.263  1.00 53.56  ? 227 SER B OG  1 
ATOM   4035 N  N   . TYR B 1 220 ? 69.852 10.801  30.714  1.00 44.30  ? 228 TYR B N   1 
ATOM   4036 C  CA  . TYR B 1 220 ? 69.738 12.077  31.399  1.00 49.68  ? 228 TYR B CA  1 
ATOM   4037 C  C   . TYR B 1 220 ? 71.074 12.813  31.383  1.00 51.07  ? 228 TYR B C   1 
ATOM   4038 O  O   . TYR B 1 220 ? 71.110 14.028  31.202  1.00 54.09  ? 228 TYR B O   1 
ATOM   4039 C  CB  . TYR B 1 220 ? 69.255 11.783  32.821  1.00 44.91  ? 228 TYR B CB  1 
ATOM   4040 C  CG  . TYR B 1 220 ? 68.744 12.979  33.613  1.00 49.91  ? 228 TYR B CG  1 
ATOM   4041 C  CD1 . TYR B 1 220 ? 67.853 13.888  33.056  1.00 54.77  ? 228 TYR B CD1 1 
ATOM   4042 C  CD2 . TYR B 1 220 ? 69.122 13.170  34.936  1.00 50.81  ? 228 TYR B CD2 1 
ATOM   4043 C  CE1 . TYR B 1 220 ? 67.374 14.966  33.783  1.00 51.67  ? 228 TYR B CE1 1 
ATOM   4044 C  CE2 . TYR B 1 220 ? 68.648 14.241  35.675  1.00 54.94  ? 228 TYR B CE2 1 
ATOM   4045 C  CZ  . TYR B 1 220 ? 67.771 15.141  35.096  1.00 54.31  ? 228 TYR B CZ  1 
ATOM   4046 O  OH  . TYR B 1 220 ? 67.307 16.197  35.824  1.00 51.43  ? 228 TYR B OH  1 
ATOM   4047 N  N   . GLY B 1 221 ? 72.166 12.070  31.588  1.00 50.90  ? 229 GLY B N   1 
ATOM   4048 C  CA  . GLY B 1 221 ? 73.484 12.676  31.682  1.00 55.66  ? 229 GLY B CA  1 
ATOM   4049 C  C   . GLY B 1 221 ? 73.548 13.689  32.822  1.00 64.28  ? 229 GLY B C   1 
ATOM   4050 O  O   . GLY B 1 221 ? 73.051 13.421  33.914  1.00 65.74  ? 229 GLY B O   1 
ATOM   4051 N  N   . PRO B 1 222 ? 74.131 14.893  32.609  1.00 64.29  ? 230 PRO B N   1 
ATOM   4052 C  CA  . PRO B 1 222 ? 74.601 15.324  31.290  1.00 72.78  ? 230 PRO B CA  1 
ATOM   4053 C  C   . PRO B 1 222 ? 75.882 14.637  30.818  1.00 77.53  ? 230 PRO B C   1 
ATOM   4054 O  O   . PRO B 1 222 ? 76.647 14.117  31.627  1.00 85.15  ? 230 PRO B O   1 
ATOM   4055 C  CB  . PRO B 1 222 ? 74.848 16.832  31.461  1.00 67.36  ? 230 PRO B CB  1 
ATOM   4056 C  CG  . PRO B 1 222 ? 75.077 17.036  32.950  1.00 72.52  ? 230 PRO B CG  1 
ATOM   4057 C  CD  . PRO B 1 222 ? 74.355 15.905  33.653  1.00 70.81  ? 230 PRO B CD  1 
ATOM   4058 N  N   . PRO B 1 223 ? 76.153 14.615  29.491  1.00 79.64  ? 231 PRO B N   1 
ATOM   4059 C  CA  . PRO B 1 223 ? 75.260 15.216  28.501  1.00 79.54  ? 231 PRO B CA  1 
ATOM   4060 C  C   . PRO B 1 223 ? 74.138 14.263  28.097  1.00 70.29  ? 231 PRO B C   1 
ATOM   4061 O  O   . PRO B 1 223 ? 74.202 13.070  28.383  1.00 63.43  ? 231 PRO B O   1 
ATOM   4062 C  CB  . PRO B 1 223 ? 76.219 15.467  27.330  1.00 77.38  ? 231 PRO B CB  1 
ATOM   4063 C  CG  . PRO B 1 223 ? 77.146 14.271  27.384  1.00 84.49  ? 231 PRO B CG  1 
ATOM   4064 C  CD  . PRO B 1 223 ? 77.335 13.999  28.865  1.00 86.83  ? 231 PRO B CD  1 
ATOM   4065 N  N   . ILE B 1 224 ? 73.122 14.797  27.414  1.00 71.39  ? 232 ILE B N   1 
ATOM   4066 C  CA  . ILE B 1 224 ? 71.968 14.006  27.021  1.00 65.78  ? 232 ILE B CA  1 
ATOM   4067 C  C   . ILE B 1 224 ? 72.382 13.027  25.926  1.00 65.48  ? 232 ILE B C   1 
ATOM   4068 O  O   . ILE B 1 224 ? 73.063 13.399  24.973  1.00 68.87  ? 232 ILE B O   1 
ATOM   4069 C  CB  . ILE B 1 224 ? 70.809 14.923  26.581  1.00 60.56  ? 232 ILE B CB  1 
ATOM   4070 C  CG1 . ILE B 1 224 ? 70.443 15.917  27.686  1.00 61.63  ? 232 ILE B CG1 1 
ATOM   4071 C  CG2 . ILE B 1 224 ? 69.606 14.104  26.135  1.00 58.47  ? 232 ILE B CG2 1 
ATOM   4072 C  CD1 . ILE B 1 224 ? 69.648 17.109  27.209  1.00 67.23  ? 232 ILE B CD1 1 
ATOM   4073 N  N   . LYS B 1 225 ? 71.967 11.766  26.093  1.00 64.38  ? 233 LYS B N   1 
ATOM   4074 C  CA  . LYS B 1 225 ? 72.187 10.727  25.101  1.00 65.41  ? 233 LYS B CA  1 
ATOM   4075 C  C   . LYS B 1 225 ? 70.827 10.276  24.574  1.00 63.23  ? 233 LYS B C   1 
ATOM   4076 O  O   . LYS B 1 225 ? 70.164 9.439   25.183  1.00 72.70  ? 233 LYS B O   1 
ATOM   4077 C  CB  . LYS B 1 225 ? 72.976 9.561   25.708  1.00 66.10  ? 233 LYS B CB  1 
ATOM   4078 C  CG  . LYS B 1 225 ? 74.336 9.937   26.283  1.00 77.03  ? 233 LYS B CG  1 
ATOM   4079 C  CD  . LYS B 1 225 ? 75.075 8.787   26.940  1.00 90.34  ? 233 LYS B CD  1 
ATOM   4080 C  CE  . LYS B 1 225 ? 75.895 7.961   25.972  1.00 85.53  ? 233 LYS B CE  1 
ATOM   4081 N  NZ  . LYS B 1 225 ? 76.719 6.952   26.680  1.00 84.52  ? 233 LYS B NZ  1 
ATOM   4082 N  N   . PRO B 1 226 ? 70.366 10.830  23.431  1.00 62.20  ? 234 PRO B N   1 
ATOM   4083 C  CA  . PRO B 1 226 ? 69.007 10.582  22.947  1.00 60.65  ? 234 PRO B CA  1 
ATOM   4084 C  C   . PRO B 1 226 ? 68.748 9.127   22.565  1.00 62.21  ? 234 PRO B C   1 
ATOM   4085 O  O   . PRO B 1 226 ? 69.678 8.366   22.309  1.00 62.22  ? 234 PRO B O   1 
ATOM   4086 C  CB  . PRO B 1 226 ? 68.896 11.491  21.713  1.00 61.24  ? 234 PRO B CB  1 
ATOM   4087 C  CG  . PRO B 1 226 ? 70.329 11.678  21.259  1.00 63.26  ? 234 PRO B CG  1 
ATOM   4088 C  CD  . PRO B 1 226 ? 71.130 11.720  22.543  1.00 58.77  ? 234 PRO B CD  1 
ATOM   4089 N  N   . PRO B 1 227 ? 67.464 8.705   22.527  1.00 58.98  ? 235 PRO B N   1 
ATOM   4090 C  CA  . PRO B 1 227 ? 67.096 7.341   22.146  1.00 58.68  ? 235 PRO B CA  1 
ATOM   4091 C  C   . PRO B 1 227 ? 66.945 7.133   20.641  1.00 66.01  ? 235 PRO B C   1 
ATOM   4092 O  O   . PRO B 1 227 ? 66.938 8.093   19.873  1.00 72.04  ? 235 PRO B O   1 
ATOM   4093 C  CB  . PRO B 1 227 ? 65.728 7.197   22.828  1.00 60.03  ? 235 PRO B CB  1 
ATOM   4094 C  CG  . PRO B 1 227 ? 65.122 8.578   22.694  1.00 58.61  ? 235 PRO B CG  1 
ATOM   4095 C  CD  . PRO B 1 227 ? 66.293 9.523   22.882  1.00 62.06  ? 235 PRO B CD  1 
ATOM   4096 N  N   . GLY B 1 228 ? 66.818 5.864   20.238  1.00 61.80  ? 236 GLY B N   1 
ATOM   4097 C  CA  . GLY B 1 228 ? 66.510 5.514   18.862  1.00 61.74  ? 236 GLY B CA  1 
ATOM   4098 C  C   . GLY B 1 228 ? 65.017 5.645   18.573  1.00 66.07  ? 236 GLY B C   1 
ATOM   4099 O  O   . GLY B 1 228 ? 64.624 5.964   17.453  1.00 71.90  ? 236 GLY B O   1 
ATOM   4100 N  N   . ILE B 1 229 ? 64.194 5.385   19.597  1.00 78.14  ? 237 ILE B N   1 
ATOM   4101 C  CA  . ILE B 1 229 ? 62.760 5.613   19.513  1.00 77.18  ? 237 ILE B CA  1 
ATOM   4102 C  C   . ILE B 1 229 ? 62.499 7.089   19.801  1.00 73.97  ? 237 ILE B C   1 
ATOM   4103 O  O   . ILE B 1 229 ? 62.517 7.508   20.957  1.00 72.70  ? 237 ILE B O   1 
ATOM   4104 C  CB  . ILE B 1 229 ? 61.983 4.703   20.489  1.00 83.66  ? 237 ILE B CB  1 
ATOM   4105 C  CG1 . ILE B 1 229 ? 62.564 3.287   20.548  1.00 94.13  ? 237 ILE B CG1 1 
ATOM   4106 C  CG2 . ILE B 1 229 ? 60.498 4.694   20.156  1.00 72.90  ? 237 ILE B CG2 1 
ATOM   4107 C  CD1 . ILE B 1 229 ? 61.523 2.204   20.723  1.00 93.05  ? 237 ILE B CD1 1 
ATOM   4108 N  N   . ILE B 1 230 ? 62.258 7.872   18.743  1.00 68.87  ? 238 ILE B N   1 
ATOM   4109 C  CA  . ILE B 1 230 ? 62.127 9.312   18.883  1.00 59.88  ? 238 ILE B CA  1 
ATOM   4110 C  C   . ILE B 1 230 ? 61.345 9.870   17.695  1.00 58.04  ? 238 ILE B C   1 
ATOM   4111 O  O   . ILE B 1 230 ? 61.599 9.503   16.551  1.00 62.85  ? 238 ILE B O   1 
ATOM   4112 C  CB  . ILE B 1 230 ? 63.520 9.962   19.017  1.00 58.12  ? 238 ILE B CB  1 
ATOM   4113 C  CG1 . ILE B 1 230 ? 63.446 11.367  19.617  1.00 54.33  ? 238 ILE B CG1 1 
ATOM   4114 C  CG2 . ILE B 1 230 ? 64.252 9.956   17.684  1.00 58.94  ? 238 ILE B CG2 1 
ATOM   4115 C  CD1 . ILE B 1 230 ? 64.768 11.869  20.149  1.00 63.32  ? 238 ILE B CD1 1 
ATOM   4116 N  N   . TYR B 1 231 ? 60.396 10.765  17.987  1.00 50.96  ? 239 TYR B N   1 
ATOM   4117 C  CA  . TYR B 1 231 ? 59.585 11.403  16.962  1.00 56.42  ? 239 TYR B CA  1 
ATOM   4118 C  C   . TYR B 1 231 ? 60.083 12.828  16.729  1.00 44.26  ? 239 TYR B C   1 
ATOM   4119 O  O   . TYR B 1 231 ? 60.264 13.242  15.586  1.00 48.19  ? 239 TYR B O   1 
ATOM   4120 C  CB  . TYR B 1 231 ? 58.110 11.356  17.378  1.00 44.57  ? 239 TYR B CB  1 
ATOM   4121 C  CG  . TYR B 1 231 ? 57.221 12.393  16.704  1.00 42.64  ? 239 TYR B CG  1 
ATOM   4122 C  CD1 . TYR B 1 231 ? 56.852 12.278  15.369  1.00 45.08  ? 239 TYR B CD1 1 
ATOM   4123 C  CD2 . TYR B 1 231 ? 56.763 13.500  17.408  1.00 47.40  ? 239 TYR B CD2 1 
ATOM   4124 C  CE1 . TYR B 1 231 ? 56.047 13.227  14.759  1.00 42.94  ? 239 TYR B CE1 1 
ATOM   4125 C  CE2 . TYR B 1 231 ? 55.960 14.457  16.810  1.00 42.91  ? 239 TYR B CE2 1 
ATOM   4126 C  CZ  . TYR B 1 231 ? 55.599 14.318  15.482  1.00 44.61  ? 239 TYR B CZ  1 
ATOM   4127 O  OH  . TYR B 1 231 ? 54.811 15.257  14.881  1.00 51.04  ? 239 TYR B OH  1 
ATOM   4128 N  N   . ASP B 1 232 ? 60.292 13.569  17.824  1.00 41.22  ? 240 ASP B N   1 
ATOM   4129 C  CA  . ASP B 1 232 ? 60.709 14.961  17.768  1.00 45.58  ? 240 ASP B CA  1 
ATOM   4130 C  C   . ASP B 1 232 ? 62.012 15.118  18.547  1.00 40.97  ? 240 ASP B C   1 
ATOM   4131 O  O   . ASP B 1 232 ? 61.992 15.345  19.754  1.00 45.80  ? 240 ASP B O   1 
ATOM   4132 C  CB  . ASP B 1 232 ? 59.617 15.878  18.328  1.00 42.58  ? 240 ASP B CB  1 
ATOM   4133 C  CG  . ASP B 1 232 ? 59.983 17.352  18.359  1.00 39.42  ? 240 ASP B CG  1 
ATOM   4134 O  OD1 . ASP B 1 232 ? 61.015 17.713  17.765  1.00 52.49  ? 240 ASP B OD1 1 
ATOM   4135 O  OD2 . ASP B 1 232 ? 59.234 18.124  18.992  1.00 42.21  ? 240 ASP B OD2 1 
ATOM   4136 N  N   . SER B 1 233 ? 63.140 14.998  17.840  1.00 44.83  ? 241 SER B N   1 
ATOM   4137 C  CA  . SER B 1 233 ? 64.457 15.065  18.454  1.00 45.46  ? 241 SER B CA  1 
ATOM   4138 C  C   . SER B 1 233 ? 64.603 16.344  19.277  1.00 42.65  ? 241 SER B C   1 
ATOM   4139 O  O   . SER B 1 233 ? 65.059 16.301  20.417  1.00 46.76  ? 241 SER B O   1 
ATOM   4140 C  CB  . SER B 1 233 ? 65.542 14.956  17.412  1.00 45.42  ? 241 SER B CB  1 
ATOM   4141 O  OG  . SER B 1 233 ? 65.400 15.962  16.422  1.00 53.17  ? 241 SER B OG  1 
ATOM   4142 N  N   . LEU B 1 234 ? 64.210 17.480  18.693  1.00 45.57  ? 242 LEU B N   1 
ATOM   4143 C  CA  . LEU B 1 234 ? 64.385 18.773  19.336  1.00 47.77  ? 242 LEU B CA  1 
ATOM   4144 C  C   . LEU B 1 234 ? 63.481 18.875  20.563  1.00 47.50  ? 242 LEU B C   1 
ATOM   4145 O  O   . LEU B 1 234 ? 63.920 19.320  21.621  1.00 43.98  ? 242 LEU B O   1 
ATOM   4146 C  CB  . LEU B 1 234 ? 64.084 19.884  18.326  1.00 46.70  ? 242 LEU B CB  1 
ATOM   4147 C  CG  . LEU B 1 234 ? 65.113 20.049  17.208  1.00 54.71  ? 242 LEU B CG  1 
ATOM   4148 C  CD1 . LEU B 1 234 ? 64.847 21.318  16.413  1.00 49.18  ? 242 LEU B CD1 1 
ATOM   4149 C  CD2 . LEU B 1 234 ? 66.531 20.059  17.764  1.00 53.54  ? 242 LEU B CD2 1 
ATOM   4150 N  N   . GLY B 1 235 ? 62.215 18.472  20.412  1.00 45.42  ? 243 GLY B N   1 
ATOM   4151 C  CA  . GLY B 1 235 ? 61.283 18.464  21.527  1.00 49.07  ? 243 GLY B CA  1 
ATOM   4152 C  C   . GLY B 1 235 ? 61.789 17.581  22.666  1.00 44.29  ? 243 GLY B C   1 
ATOM   4153 O  O   . GLY B 1 235 ? 61.608 17.903  23.838  1.00 47.03  ? 243 GLY B O   1 
ATOM   4154 N  N   . TYR B 1 236 ? 62.432 16.469  22.295  1.00 41.54  ? 244 TYR B N   1 
ATOM   4155 C  CA  . TYR B 1 236 ? 62.998 15.539  23.258  1.00 43.28  ? 244 TYR B CA  1 
ATOM   4156 C  C   . TYR B 1 236 ? 64.075 16.245  24.078  1.00 44.31  ? 244 TYR B C   1 
ATOM   4157 O  O   . TYR B 1 236 ? 64.022 16.249  25.306  1.00 43.53  ? 244 TYR B O   1 
ATOM   4158 C  CB  . TYR B 1 236 ? 63.553 14.301  22.546  1.00 44.48  ? 244 TYR B CB  1 
ATOM   4159 C  CG  . TYR B 1 236 ? 64.279 13.347  23.484  1.00 47.46  ? 244 TYR B CG  1 
ATOM   4160 C  CD1 . TYR B 1 236 ? 65.622 13.524  23.793  1.00 48.24  ? 244 TYR B CD1 1 
ATOM   4161 C  CD2 . TYR B 1 236 ? 63.602 12.306  24.107  1.00 49.88  ? 244 TYR B CD2 1 
ATOM   4162 C  CE1 . TYR B 1 236 ? 66.279 12.671  24.664  1.00 55.90  ? 244 TYR B CE1 1 
ATOM   4163 C  CE2 . TYR B 1 236 ? 64.246 11.450  24.985  1.00 47.31  ? 244 TYR B CE2 1 
ATOM   4164 C  CZ  . TYR B 1 236 ? 65.588 11.635  25.265  1.00 50.42  ? 244 TYR B CZ  1 
ATOM   4165 O  OH  . TYR B 1 236 ? 66.228 10.794  26.129  1.00 51.91  ? 244 TYR B OH  1 
ATOM   4166 N  N   . MET B 1 237 ? 65.054 16.836  23.385  1.00 45.27  ? 245 MET B N   1 
ATOM   4167 C  CA  . MET B 1 237 ? 66.167 17.498  24.043  1.00 48.26  ? 245 MET B CA  1 
ATOM   4168 C  C   . MET B 1 237 ? 65.634 18.598  24.958  1.00 48.71  ? 245 MET B C   1 
ATOM   4169 O  O   . MET B 1 237 ? 66.074 18.712  26.099  1.00 50.51  ? 245 MET B O   1 
ATOM   4170 C  CB  . MET B 1 237 ? 67.135 18.101  23.020  1.00 52.34  ? 245 MET B CB  1 
ATOM   4171 C  CG  . MET B 1 237 ? 67.736 17.070  22.075  1.00 65.46  ? 245 MET B CG  1 
ATOM   4172 S  SD  . MET B 1 237 ? 68.749 15.812  22.898  1.00 67.32  ? 245 MET B SD  1 
ATOM   4173 C  CE  . MET B 1 237 ? 70.081 16.821  23.546  1.00 73.19  ? 245 MET B CE  1 
ATOM   4174 N  N   . ASN B 1 238 ? 64.682 19.402  24.463  1.00 45.04  ? 246 ASN B N   1 
ATOM   4175 C  CA  . ASN B 1 238 ? 64.128 20.484  25.263  1.00 47.91  ? 246 ASN B CA  1 
ATOM   4176 C  C   . ASN B 1 238 ? 63.444 19.914  26.503  1.00 46.15  ? 246 ASN B C   1 
ATOM   4177 O  O   . ASN B 1 238 ? 63.539 20.492  27.583  1.00 49.50  ? 246 ASN B O   1 
ATOM   4178 C  CB  . ASN B 1 238 ? 63.123 21.359  24.508  1.00 51.12  ? 246 ASN B CB  1 
ATOM   4179 C  CG  . ASN B 1 238 ? 63.715 22.073  23.313  1.00 68.68  ? 246 ASN B CG  1 
ATOM   4180 O  OD1 . ASN B 1 238 ? 64.865 22.508  23.347  1.00 61.78  ? 246 ASN B OD1 1 
ATOM   4181 N  ND2 . ASN B 1 238 ? 62.937 22.192  22.250  1.00 67.83  ? 246 ASN B ND2 1 
ATOM   4182 N  N   . THR B 1 239 ? 62.741 18.789  26.337  1.00 44.36  ? 247 THR B N   1 
ATOM   4183 C  CA  . THR B 1 239 ? 61.967 18.222  27.429  1.00 44.10  ? 247 THR B CA  1 
ATOM   4184 C  C   . THR B 1 239 ? 62.910 17.783  28.547  1.00 45.54  ? 247 THR B C   1 
ATOM   4185 O  O   . THR B 1 239 ? 62.646 18.042  29.719  1.00 48.67  ? 247 THR B O   1 
ATOM   4186 C  CB  . THR B 1 239 ? 61.050 17.094  26.939  1.00 45.42  ? 247 THR B CB  1 
ATOM   4187 O  OG1 . THR B 1 239 ? 60.024 17.699  26.152  1.00 45.76  ? 247 THR B OG1 1 
ATOM   4188 C  CG2 . THR B 1 239 ? 60.423 16.305  28.068  1.00 49.14  ? 247 THR B CG2 1 
ATOM   4189 N  N   . VAL B 1 240 ? 64.021 17.135  28.182  1.00 46.00  ? 248 VAL B N   1 
ATOM   4190 C  CA  . VAL B 1 240 ? 64.968 16.660  29.177  1.00 47.49  ? 248 VAL B CA  1 
ATOM   4191 C  C   . VAL B 1 240 ? 65.502 17.849  29.971  1.00 47.77  ? 248 VAL B C   1 
ATOM   4192 O  O   . VAL B 1 240 ? 65.575 17.788  31.195  1.00 47.25  ? 248 VAL B O   1 
ATOM   4193 C  CB  . VAL B 1 240 ? 66.123 15.858  28.549  1.00 45.16  ? 248 VAL B CB  1 
ATOM   4194 C  CG1 . VAL B 1 240 ? 67.157 15.474  29.596  1.00 51.31  ? 248 VAL B CG1 1 
ATOM   4195 C  CG2 . VAL B 1 240 ? 65.620 14.626  27.813  1.00 45.98  ? 248 VAL B CG2 1 
ATOM   4196 N  N   . GLU B 1 241 ? 65.882 18.922  29.270  1.00 47.17  ? 249 GLU B N   1 
ATOM   4197 C  CA  . GLU B 1 241 ? 66.459 20.084  29.927  1.00 48.82  ? 249 GLU B CA  1 
ATOM   4198 C  C   . GLU B 1 241 ? 65.411 20.752  30.810  1.00 44.46  ? 249 GLU B C   1 
ATOM   4199 O  O   . GLU B 1 241 ? 65.738 21.305  31.858  1.00 49.56  ? 249 GLU B O   1 
ATOM   4200 C  CB  . GLU B 1 241 ? 67.026 21.073  28.907  1.00 58.01  ? 249 GLU B CB  1 
ATOM   4201 C  CG  . GLU B 1 241 ? 68.434 20.730  28.455  1.00 65.35  ? 249 GLU B CG  1 
ATOM   4202 C  CD  . GLU B 1 241 ? 69.383 20.349  29.580  1.00 78.61  ? 249 GLU B CD  1 
ATOM   4203 O  OE1 . GLU B 1 241 ? 69.488 21.121  30.556  1.00 74.02  ? 249 GLU B OE1 1 
ATOM   4204 O  OE2 . GLU B 1 241 ? 70.022 19.283  29.474  1.00 84.50  ? 249 GLU B OE2 1 
ATOM   4205 N  N   . ARG B 1 242 ? 64.151 20.700  30.377  1.00 49.05  ? 250 ARG B N   1 
ATOM   4206 C  CA  . ARG B 1 242 ? 63.071 21.301  31.136  1.00 49.75  ? 250 ARG B CA  1 
ATOM   4207 C  C   . ARG B 1 242 ? 62.890 20.529  32.441  1.00 46.72  ? 250 ARG B C   1 
ATOM   4208 O  O   . ARG B 1 242 ? 62.689 21.123  33.498  1.00 44.23  ? 250 ARG B O   1 
ATOM   4209 C  CB  . ARG B 1 242 ? 61.795 21.308  30.293  1.00 47.93  ? 250 ARG B CB  1 
ATOM   4210 C  CG  . ARG B 1 242 ? 60.576 21.845  31.023  1.00 55.09  ? 250 ARG B CG  1 
ATOM   4211 C  CD  . ARG B 1 242 ? 59.336 21.662  30.179  1.00 57.83  ? 250 ARG B CD  1 
ATOM   4212 N  NE  . ARG B 1 242 ? 58.144 21.812  30.992  1.00 63.44  ? 250 ARG B NE  1 
ATOM   4213 C  CZ  . ARG B 1 242 ? 56.913 21.567  30.567  1.00 62.30  ? 250 ARG B CZ  1 
ATOM   4214 N  NH1 . ARG B 1 242 ? 56.709 21.171  29.324  1.00 54.70  ? 250 ARG B NH1 1 
ATOM   4215 N  NH2 . ARG B 1 242 ? 55.892 21.720  31.392  1.00 66.94  ? 250 ARG B NH2 1 
ATOM   4216 N  N   . ILE B 1 243 ? 62.970 19.198  32.344  1.00 44.73  ? 251 ILE B N   1 
ATOM   4217 C  CA  . ILE B 1 243 ? 62.864 18.326  33.500  1.00 48.36  ? 251 ILE B CA  1 
ATOM   4218 C  C   . ILE B 1 243 ? 64.029 18.608  34.443  1.00 48.81  ? 251 ILE B C   1 
ATOM   4219 O  O   . ILE B 1 243 ? 63.840 18.677  35.655  1.00 49.88  ? 251 ILE B O   1 
ATOM   4220 C  CB  . ILE B 1 243 ? 62.807 16.846  33.069  1.00 47.84  ? 251 ILE B CB  1 
ATOM   4221 C  CG1 . ILE B 1 243 ? 61.447 16.499  32.458  1.00 46.02  ? 251 ILE B CG1 1 
ATOM   4222 C  CG2 . ILE B 1 243 ? 63.150 15.928  34.233  1.00 47.94  ? 251 ILE B CG2 1 
ATOM   4223 C  CD1 . ILE B 1 243 ? 61.418 15.187  31.711  1.00 46.49  ? 251 ILE B CD1 1 
ATOM   4224 N  N   . ARG B 1 244 ? 65.231 18.779  33.882  1.00 49.30  ? 252 ARG B N   1 
ATOM   4225 C  CA  . ARG B 1 244 ? 66.403 19.030  34.703  1.00 44.93  ? 252 ARG B CA  1 
ATOM   4226 C  C   . ARG B 1 244 ? 66.211 20.341  35.464  1.00 53.57  ? 252 ARG B C   1 
ATOM   4227 O  O   . ARG B 1 244 ? 66.534 20.419  36.647  1.00 52.62  ? 252 ARG B O   1 
ATOM   4228 C  CB  . ARG B 1 244 ? 67.687 19.045  33.867  1.00 48.69  ? 252 ARG B CB  1 
ATOM   4229 C  CG  . ARG B 1 244 ? 68.955 19.020  34.710  1.00 56.65  ? 252 ARG B CG  1 
ATOM   4230 C  CD  . ARG B 1 244 ? 70.225 19.289  33.924  1.00 54.83  ? 252 ARG B CD  1 
ATOM   4231 N  NE  . ARG B 1 244 ? 70.269 18.621  32.630  1.00 53.26  ? 252 ARG B NE  1 
ATOM   4232 C  CZ  . ARG B 1 244 ? 70.424 17.314  32.444  1.00 62.04  ? 252 ARG B CZ  1 
ATOM   4233 N  NH1 . ARG B 1 244 ? 70.511 16.491  33.474  1.00 62.35  ? 252 ARG B NH1 1 
ATOM   4234 N  NH2 . ARG B 1 244 ? 70.492 16.834  31.214  1.00 67.43  ? 252 ARG B NH2 1 
ATOM   4235 N  N   . ARG B 1 245 ? 65.666 21.365  34.795  1.00 48.90  ? 253 ARG B N   1 
ATOM   4236 C  CA  . ARG B 1 245 ? 65.470 22.654  35.440  1.00 52.43  ? 253 ARG B CA  1 
ATOM   4237 C  C   . ARG B 1 245 ? 64.399 22.546  36.527  1.00 47.13  ? 253 ARG B C   1 
ATOM   4238 O  O   . ARG B 1 245 ? 64.568 23.092  37.613  1.00 47.45  ? 253 ARG B O   1 
ATOM   4239 C  CB  . ARG B 1 245 ? 65.099 23.754  34.439  1.00 51.20  ? 253 ARG B CB  1 
ATOM   4240 C  CG  . ARG B 1 245 ? 64.588 25.024  35.107  1.00 64.00  ? 253 ARG B CG  1 
ATOM   4241 C  CD  . ARG B 1 245 ? 64.015 26.053  34.150  1.00 70.36  ? 253 ARG B CD  1 
ATOM   4242 N  NE  . ARG B 1 245 ? 62.966 25.523  33.289  1.00 81.22  ? 253 ARG B NE  1 
ATOM   4243 C  CZ  . ARG B 1 245 ? 61.721 25.256  33.672  1.00 78.90  ? 253 ARG B CZ  1 
ATOM   4244 N  NH1 . ARG B 1 245 ? 61.344 25.465  34.921  1.00 72.57  ? 253 ARG B NH1 1 
ATOM   4245 N  NH2 . ARG B 1 245 ? 60.851 24.787  32.794  1.00 81.56  ? 253 ARG B NH2 1 
ATOM   4246 N  N   . ILE B 1 246 ? 63.292 21.856  36.234  1.00 49.08  ? 254 ILE B N   1 
ATOM   4247 C  CA  . ILE B 1 246 ? 62.203 21.745  37.194  1.00 50.09  ? 254 ILE B CA  1 
ATOM   4248 C  C   . ILE B 1 246 ? 62.702 21.023  38.443  1.00 51.58  ? 254 ILE B C   1 
ATOM   4249 O  O   . ILE B 1 246 ? 62.336 21.385  39.559  1.00 52.53  ? 254 ILE B O   1 
ATOM   4250 C  CB  . ILE B 1 246 ? 60.973 21.044  36.581  1.00 56.56  ? 254 ILE B CB  1 
ATOM   4251 C  CG1 . ILE B 1 246 ? 60.301 21.911  35.513  1.00 59.70  ? 254 ILE B CG1 1 
ATOM   4252 C  CG2 . ILE B 1 246 ? 59.988 20.644  37.668  1.00 61.24  ? 254 ILE B CG2 1 
ATOM   4253 C  CD1 . ILE B 1 246 ? 59.279 21.175  34.679  1.00 58.71  ? 254 ILE B CD1 1 
ATOM   4254 N  N   . ALA B 1 247 ? 63.544 20.003  38.248  1.00 51.30  ? 255 ALA B N   1 
ATOM   4255 C  CA  . ALA B 1 247 ? 64.063 19.214  39.353  1.00 56.62  ? 255 ALA B CA  1 
ATOM   4256 C  C   . ALA B 1 247 ? 64.911 20.082  40.279  1.00 53.83  ? 255 ALA B C   1 
ATOM   4257 O  O   . ALA B 1 247 ? 64.797 19.974  41.498  1.00 51.15  ? 255 ALA B O   1 
ATOM   4258 C  CB  . ALA B 1 247 ? 64.859 18.047  38.826  1.00 48.04  ? 255 ALA B CB  1 
ATOM   4259 N  N   . GLN B 1 248 ? 65.770 20.928  39.696  1.00 56.91  ? 256 GLN B N   1 
ATOM   4260 C  CA  . GLN B 1 248 ? 66.703 21.714  40.488  1.00 61.67  ? 256 GLN B CA  1 
ATOM   4261 C  C   . GLN B 1 248 ? 65.956 22.833  41.215  1.00 55.59  ? 256 GLN B C   1 
ATOM   4262 O  O   . GLN B 1 248 ? 66.354 23.224  42.309  1.00 62.29  ? 256 GLN B O   1 
ATOM   4263 C  CB  . GLN B 1 248 ? 67.845 22.268  39.630  1.00 66.22  ? 256 GLN B CB  1 
ATOM   4264 C  CG  . GLN B 1 248 ? 67.420 23.353  38.651  1.00 92.22  ? 256 GLN B CG  1 
ATOM   4265 C  CD  . GLN B 1 248 ? 68.221 24.622  38.822  1.00 84.79  ? 256 GLN B CD  1 
ATOM   4266 O  OE1 . GLN B 1 248 ? 68.973 24.783  39.782  1.00 69.10  ? 256 GLN B OE1 1 
ATOM   4267 N  NE2 . GLN B 1 248 ? 68.042 25.552  37.899  1.00 80.59  ? 256 GLN B NE2 1 
ATOM   4268 N  N   . GLU B 1 249 ? 64.865 23.331  40.621  1.00 52.53  ? 257 GLU B N   1 
ATOM   4269 C  CA  . GLU B 1 249 ? 64.137 24.454  41.193  1.00 55.69  ? 257 GLU B CA  1 
ATOM   4270 C  C   . GLU B 1 249 ? 63.131 23.968  42.237  1.00 58.74  ? 257 GLU B C   1 
ATOM   4271 O  O   . GLU B 1 249 ? 62.771 24.721  43.138  1.00 60.41  ? 257 GLU B O   1 
ATOM   4272 C  CB  . GLU B 1 249 ? 63.440 25.261  40.093  1.00 64.00  ? 257 GLU B CB  1 
ATOM   4273 C  CG  . GLU B 1 249 ? 64.397 26.085  39.247  1.00 72.24  ? 257 GLU B CG  1 
ATOM   4274 C  CD  . GLU B 1 249 ? 63.755 26.829  38.088  1.00 79.11  ? 257 GLU B CD  1 
ATOM   4275 O  OE1 . GLU B 1 249 ? 62.549 26.620  37.844  1.00 75.64  ? 257 GLU B OE1 1 
ATOM   4276 O  OE2 . GLU B 1 249 ? 64.462 27.624  37.434  1.00 81.64  ? 257 GLU B OE2 1 
ATOM   4277 N  N   . THR B 1 250 ? 62.679 22.715  42.111  1.00 57.09  ? 258 THR B N   1 
ATOM   4278 C  CA  . THR B 1 250 ? 61.697 22.160  43.032  1.00 58.61  ? 258 THR B CA  1 
ATOM   4279 C  C   . THR B 1 250 ? 62.357 21.138  43.956  1.00 53.76  ? 258 THR B C   1 
ATOM   4280 O  O   . THR B 1 250 ? 61.679 20.488  44.748  1.00 58.37  ? 258 THR B O   1 
ATOM   4281 C  CB  . THR B 1 250 ? 60.522 21.514  42.285  1.00 58.85  ? 258 THR B CB  1 
ATOM   4282 O  OG1 . THR B 1 250 ? 61.016 20.384  41.564  1.00 52.00  ? 258 THR B OG1 1 
ATOM   4283 C  CG2 . THR B 1 250 ? 59.823 22.471  41.343  1.00 60.29  ? 258 THR B CG2 1 
ATOM   4284 N  N   . LYS B 1 251 ? 63.683 21.010  43.848  1.00 54.64  ? 259 LYS B N   1 
ATOM   4285 C  CA  . LYS B 1 251 ? 64.436 20.026  44.610  1.00 58.77  ? 259 LYS B CA  1 
ATOM   4286 C  C   . LYS B 1 251 ? 63.691 18.692  44.565  1.00 56.72  ? 259 LYS B C   1 
ATOM   4287 O  O   . LYS B 1 251 ? 63.430 18.087  45.602  1.00 51.51  ? 259 LYS B O   1 
ATOM   4288 C  CB  . LYS B 1 251 ? 64.645 20.498  46.055  1.00 68.06  ? 259 LYS B CB  1 
ATOM   4289 C  CG  . LYS B 1 251 ? 64.761 22.005  46.260  1.00 85.68  ? 259 LYS B CG  1 
ATOM   4290 C  CD  . LYS B 1 251 ? 65.908 22.652  45.509  1.00 109.76 ? 259 LYS B CD  1 
ATOM   4291 C  CE  . LYS B 1 251 ? 67.199 21.866  45.593  1.00 120.02 ? 259 LYS B CE  1 
ATOM   4292 N  NZ  . LYS B 1 251 ? 67.857 21.773  44.268  1.00 111.38 ? 259 LYS B NZ  1 
ATOM   4293 N  N   . SER B 1 252 ? 63.354 18.242  43.349  1.00 53.33  ? 260 SER B N   1 
ATOM   4294 C  CA  . SER B 1 252 ? 62.574 17.029  43.161  1.00 54.20  ? 260 SER B CA  1 
ATOM   4295 C  C   . SER B 1 252 ? 63.464 15.912  42.621  1.00 49.45  ? 260 SER B C   1 
ATOM   4296 O  O   . SER B 1 252 ? 64.434 16.176  41.916  1.00 47.28  ? 260 SER B O   1 
ATOM   4297 C  CB  . SER B 1 252 ? 61.399 17.270  42.240  1.00 45.15  ? 260 SER B CB  1 
ATOM   4298 O  OG  . SER B 1 252 ? 60.456 18.154  42.826  1.00 49.15  ? 260 SER B OG  1 
ATOM   4299 N  N   . GLN B 1 253 ? 63.116 14.664  42.956  1.00 49.37  ? 261 GLN B N   1 
ATOM   4300 C  CA  . GLN B 1 253 ? 63.758 13.505  42.358  1.00 51.52  ? 261 GLN B CA  1 
ATOM   4301 C  C   . GLN B 1 253 ? 63.193 13.317  40.954  1.00 49.93  ? 261 GLN B C   1 
ATOM   4302 O  O   . GLN B 1 253 ? 62.048 13.684  40.702  1.00 48.54  ? 261 GLN B O   1 
ATOM   4303 C  CB  . GLN B 1 253 ? 63.485 12.236  43.168  1.00 58.31  ? 261 GLN B CB  1 
ATOM   4304 C  CG  . GLN B 1 253 ? 63.906 12.306  44.627  1.00 67.38  ? 261 GLN B CG  1 
ATOM   4305 C  CD  . GLN B 1 253 ? 63.384 11.110  45.385  1.00 69.99  ? 261 GLN B CD  1 
ATOM   4306 O  OE1 . GLN B 1 253 ? 63.487 9.973   44.929  1.00 58.98  ? 261 GLN B OE1 1 
ATOM   4307 N  NE2 . GLN B 1 253 ? 62.791 11.362  46.541  1.00 59.55  ? 261 GLN B NE2 1 
ATOM   4308 N  N   . VAL B 1 254 ? 63.985 12.733  40.048  1.00 46.71  ? 262 VAL B N   1 
ATOM   4309 C  CA  . VAL B 1 254 ? 63.482 12.412  38.721  1.00 48.93  ? 262 VAL B CA  1 
ATOM   4310 C  C   . VAL B 1 254 ? 63.446 10.896  38.558  1.00 50.89  ? 262 VAL B C   1 
ATOM   4311 O  O   . VAL B 1 254 ? 64.487 10.242  38.555  1.00 44.12  ? 262 VAL B O   1 
ATOM   4312 C  CB  . VAL B 1 254 ? 64.311 13.069  37.600  1.00 47.71  ? 262 VAL B CB  1 
ATOM   4313 C  CG1 . VAL B 1 254 ? 63.837 12.622  36.225  1.00 47.93  ? 262 VAL B CG1 1 
ATOM   4314 C  CG2 . VAL B 1 254 ? 64.299 14.586  37.700  1.00 49.51  ? 262 VAL B CG2 1 
ATOM   4315 N  N   . TRP B 1 255 ? 62.233 10.353  38.410  1.00 47.46  ? 263 TRP B N   1 
ATOM   4316 C  CA  . TRP B 1 255 ? 62.054 8.929   38.192  1.00 45.89  ? 263 TRP B CA  1 
ATOM   4317 C  C   . TRP B 1 255 ? 61.958 8.639   36.698  1.00 46.01  ? 263 TRP B C   1 
ATOM   4318 O  O   . TRP B 1 255 ? 60.994 9.020   36.037  1.00 46.93  ? 263 TRP B O   1 
ATOM   4319 C  CB  . TRP B 1 255 ? 60.817 8.416   38.941  1.00 43.02  ? 263 TRP B CB  1 
ATOM   4320 C  CG  . TRP B 1 255 ? 60.981 8.395   40.437  1.00 42.83  ? 263 TRP B CG  1 
ATOM   4321 C  CD1 . TRP B 1 255 ? 62.002 8.928   41.167  1.00 48.19  ? 263 TRP B CD1 1 
ATOM   4322 C  CD2 . TRP B 1 255 ? 60.083 7.786   41.389  1.00 40.92  ? 263 TRP B CD2 1 
ATOM   4323 N  NE1 . TRP B 1 255 ? 61.799 8.704   42.502  1.00 51.77  ? 263 TRP B NE1 1 
ATOM   4324 C  CE2 . TRP B 1 255 ? 60.633 8.004   42.669  1.00 45.01  ? 263 TRP B CE2 1 
ATOM   4325 C  CE3 . TRP B 1 255 ? 58.878 7.085   41.281  1.00 45.59  ? 263 TRP B CE3 1 
ATOM   4326 C  CZ2 . TRP B 1 255 ? 60.015 7.544   43.828  1.00 49.33  ? 263 TRP B CZ2 1 
ATOM   4327 C  CZ3 . TRP B 1 255 ? 58.270 6.629   42.428  1.00 48.11  ? 263 TRP B CZ3 1 
ATOM   4328 C  CH2 . TRP B 1 255 ? 58.832 6.857   43.682  1.00 48.07  ? 263 TRP B CH2 1 
ATOM   4329 N  N   . PHE B 1 256 ? 62.980 7.945   36.193  1.00 47.42  ? 264 PHE B N   1 
ATOM   4330 C  CA  . PHE B 1 256 ? 63.102 7.634   34.781  1.00 44.12  ? 264 PHE B CA  1 
ATOM   4331 C  C   . PHE B 1 256 ? 62.094 6.544   34.426  1.00 43.63  ? 264 PHE B C   1 
ATOM   4332 O  O   . PHE B 1 256 ? 61.557 5.879   35.309  1.00 48.05  ? 264 PHE B O   1 
ATOM   4333 C  CB  . PHE B 1 256 ? 64.548 7.237   34.473  1.00 45.39  ? 264 PHE B CB  1 
ATOM   4334 C  CG  . PHE B 1 256 ? 65.575 8.252   34.913  1.00 48.38  ? 264 PHE B CG  1 
ATOM   4335 C  CD1 . PHE B 1 256 ? 65.502 9.567   34.481  1.00 45.84  ? 264 PHE B CD1 1 
ATOM   4336 C  CD2 . PHE B 1 256 ? 66.613 7.897   35.761  1.00 52.00  ? 264 PHE B CD2 1 
ATOM   4337 C  CE1 . PHE B 1 256 ? 66.445 10.500  34.882  1.00 53.11  ? 264 PHE B CE1 1 
ATOM   4338 C  CE2 . PHE B 1 256 ? 67.554 8.833   36.164  1.00 54.63  ? 264 PHE B CE2 1 
ATOM   4339 C  CZ  . PHE B 1 256 ? 67.469 10.133  35.723  1.00 52.40  ? 264 PHE B CZ  1 
ATOM   4340 N  N   . GLY B 1 257 ? 61.838 6.378   33.125  1.00 46.68  ? 265 GLY B N   1 
ATOM   4341 C  CA  . GLY B 1 257 ? 60.834 5.439   32.654  1.00 48.13  ? 265 GLY B CA  1 
ATOM   4342 C  C   . GLY B 1 257 ? 61.270 3.984   32.812  1.00 51.16  ? 265 GLY B C   1 
ATOM   4343 O  O   . GLY B 1 257 ? 60.471 3.137   33.207  1.00 52.62  ? 265 GLY B O   1 
ATOM   4344 N  N   . HIS B 1 258 ? 62.542 3.704   32.502  1.00 44.75  ? 266 HIS B N   1 
ATOM   4345 C  CA  . HIS B 1 258 ? 62.988 2.333   32.313  1.00 50.71  ? 266 HIS B CA  1 
ATOM   4346 C  C   . HIS B 1 258 ? 64.439 2.157   32.757  1.00 48.47  ? 266 HIS B C   1 
ATOM   4347 O  O   . HIS B 1 258 ? 65.253 1.634   32.001  1.00 56.61  ? 266 HIS B O   1 
ATOM   4348 C  CB  . HIS B 1 258 ? 62.861 1.937   30.837  1.00 48.73  ? 266 HIS B CB  1 
ATOM   4349 C  CG  . HIS B 1 258 ? 61.472 1.979   30.289  1.00 49.12  ? 266 HIS B CG  1 
ATOM   4350 N  ND1 . HIS B 1 258 ? 60.399 1.365   30.897  1.00 46.20  ? 266 HIS B ND1 1 
ATOM   4351 C  CD2 . HIS B 1 258 ? 60.987 2.559   29.181  1.00 48.35  ? 266 HIS B CD2 1 
ATOM   4352 C  CE1 . HIS B 1 258 ? 59.308 1.574   30.172  1.00 44.75  ? 266 HIS B CE1 1 
ATOM   4353 N  NE2 . HIS B 1 258 ? 59.642 2.298   29.125  1.00 42.72  ? 266 HIS B NE2 1 
ATOM   4354 N  N   . ASP B 1 259 ? 64.754 2.582   33.986  1.00 50.83  ? 267 ASP B N   1 
ATOM   4355 C  CA  . ASP B 1 259 ? 66.101 2.454   34.523  1.00 54.83  ? 267 ASP B CA  1 
ATOM   4356 C  C   . ASP B 1 259 ? 66.122 1.324   35.549  1.00 53.13  ? 267 ASP B C   1 
ATOM   4357 O  O   . ASP B 1 259 ? 65.530 1.444   36.619  1.00 55.55  ? 267 ASP B O   1 
ATOM   4358 C  CB  . ASP B 1 259 ? 66.574 3.769   35.149  1.00 55.31  ? 267 ASP B CB  1 
ATOM   4359 C  CG  . ASP B 1 259 ? 68.059 3.818   35.468  1.00 53.40  ? 267 ASP B CG  1 
ATOM   4360 O  OD1 . ASP B 1 259 ? 68.566 2.846   36.063  1.00 66.45  ? 267 ASP B OD1 1 
ATOM   4361 O  OD2 . ASP B 1 259 ? 68.691 4.839   35.139  1.00 62.64  ? 267 ASP B OD2 1 
ATOM   4362 N  N   . ALA B 1 260 ? 66.814 0.231   35.206  1.00 54.85  ? 268 ALA B N   1 
ATOM   4363 C  CA  . ALA B 1 260 ? 66.882 -0.950  36.053  1.00 60.90  ? 268 ALA B CA  1 
ATOM   4364 C  C   . ALA B 1 260 ? 67.477 -0.610  37.418  1.00 54.75  ? 268 ALA B C   1 
ATOM   4365 O  O   . ALA B 1 260 ? 66.944 -1.026  38.444  1.00 63.80  ? 268 ALA B O   1 
ATOM   4366 C  CB  . ALA B 1 260 ? 67.683 -2.024  35.359  1.00 57.13  ? 268 ALA B CB  1 
ATOM   4367 N  N   . GLU B 1 261 ? 68.588 0.136   37.423  1.00 55.43  ? 269 GLU B N   1 
ATOM   4368 C  CA  . GLU B 1 261 ? 69.278 0.472   38.659  1.00 61.20  ? 269 GLU B CA  1 
ATOM   4369 C  C   . GLU B 1 261 ? 68.341 1.233   39.595  1.00 61.79  ? 269 GLU B C   1 
ATOM   4370 O  O   . GLU B 1 261 ? 68.162 0.842   40.745  1.00 66.47  ? 269 GLU B O   1 
ATOM   4371 C  CB  . GLU B 1 261 ? 70.540 1.289   38.379  1.00 71.79  ? 269 GLU B CB  1 
ATOM   4372 C  CG  . GLU B 1 261 ? 71.773 0.441   38.127  1.00 88.71  ? 269 GLU B CG  1 
ATOM   4373 C  CD  . GLU B 1 261 ? 73.086 1.193   38.272  1.00 114.33 ? 269 GLU B CD  1 
ATOM   4374 O  OE1 . GLU B 1 261 ? 73.081 2.273   38.900  1.00 109.66 ? 269 GLU B OE1 1 
ATOM   4375 O  OE2 . GLU B 1 261 ? 74.106 0.705   37.742  1.00 121.75 ? 269 GLU B OE2 1 
ATOM   4376 N  N   . GLN B 1 262 ? 67.757 2.327   39.093  1.00 62.45  ? 270 GLN B N   1 
ATOM   4377 C  CA  . GLN B 1 262 ? 66.887 3.173   39.893  1.00 53.46  ? 270 GLN B CA  1 
ATOM   4378 C  C   . GLN B 1 262 ? 65.706 2.351   40.405  1.00 51.12  ? 270 GLN B C   1 
ATOM   4379 O  O   . GLN B 1 262 ? 65.281 2.521   41.545  1.00 53.96  ? 270 GLN B O   1 
ATOM   4380 C  CB  . GLN B 1 262 ? 66.416 4.371   39.067  1.00 48.81  ? 270 GLN B CB  1 
ATOM   4381 C  CG  . GLN B 1 262 ? 65.778 5.483   39.887  1.00 53.11  ? 270 GLN B CG  1 
ATOM   4382 C  CD  . GLN B 1 262 ? 65.168 6.541   39.000  1.00 54.60  ? 270 GLN B CD  1 
ATOM   4383 O  OE1 . GLN B 1 262 ? 64.461 6.242   38.039  1.00 54.85  ? 270 GLN B OE1 1 
ATOM   4384 N  NE2 . GLN B 1 262 ? 65.456 7.796   39.305  1.00 52.31  ? 270 GLN B NE2 1 
ATOM   4385 N  N   . PHE B 1 263 ? 65.184 1.458   39.556  1.00 44.03  ? 271 PHE B N   1 
ATOM   4386 C  CA  . PHE B 1 263 ? 64.011 0.672   39.906  1.00 52.75  ? 271 PHE B CA  1 
ATOM   4387 C  C   . PHE B 1 263 ? 64.354 -0.278  41.050  1.00 55.59  ? 271 PHE B C   1 
ATOM   4388 O  O   . PHE B 1 263 ? 63.554 -0.459  41.965  1.00 58.74  ? 271 PHE B O   1 
ATOM   4389 C  CB  . PHE B 1 263 ? 63.483 -0.098  38.693  1.00 49.37  ? 271 PHE B CB  1 
ATOM   4390 C  CG  . PHE B 1 263 ? 62.178 -0.818  38.924  1.00 49.90  ? 271 PHE B CG  1 
ATOM   4391 C  CD1 . PHE B 1 263 ? 60.995 -0.112  39.078  1.00 50.46  ? 271 PHE B CD1 1 
ATOM   4392 C  CD2 . PHE B 1 263 ? 62.133 -2.201  38.997  1.00 47.59  ? 271 PHE B CD2 1 
ATOM   4393 C  CE1 . PHE B 1 263 ? 59.796 -0.774  39.292  1.00 53.71  ? 271 PHE B CE1 1 
ATOM   4394 C  CE2 . PHE B 1 263 ? 60.933 -2.861  39.212  1.00 56.64  ? 271 PHE B CE2 1 
ATOM   4395 C  CZ  . PHE B 1 263 ? 59.767 -2.147  39.358  1.00 61.29  ? 271 PHE B CZ  1 
ATOM   4396 N  N   . LYS B 1 264 ? 65.547 -0.880  40.980  1.00 59.91  ? 272 LYS B N   1 
ATOM   4397 C  CA  . LYS B 1 264 ? 66.011 -1.794  42.012  1.00 65.95  ? 272 LYS B CA  1 
ATOM   4398 C  C   . LYS B 1 264 ? 65.942 -1.091  43.366  1.00 57.93  ? 272 LYS B C   1 
ATOM   4399 O  O   . LYS B 1 264 ? 65.573 -1.703  44.366  1.00 58.97  ? 272 LYS B O   1 
ATOM   4400 C  CB  . LYS B 1 264 ? 67.439 -2.267  41.713  1.00 71.23  ? 272 LYS B CB  1 
ATOM   4401 C  CG  . LYS B 1 264 ? 67.810 -3.627  42.293  1.00 89.69  ? 272 LYS B CG  1 
ATOM   4402 C  CD  . LYS B 1 264 ? 67.532 -4.779  41.348  1.00 110.96 ? 272 LYS B CD  1 
ATOM   4403 C  CE  . LYS B 1 264 ? 67.371 -6.111  42.051  1.00 114.29 ? 272 LYS B CE  1 
ATOM   4404 N  NZ  . LYS B 1 264 ? 67.199 -7.221  41.085  1.00 109.47 ? 272 LYS B NZ  1 
ATOM   4405 N  N   . LYS B 1 265 ? 66.287 0.203   43.381  1.00 50.34  ? 273 LYS B N   1 
ATOM   4406 C  CA  . LYS B 1 265 ? 66.383 0.966   44.617  1.00 51.80  ? 273 LYS B CA  1 
ATOM   4407 C  C   . LYS B 1 265 ? 65.001 1.428   45.082  1.00 51.68  ? 273 LYS B C   1 
ATOM   4408 O  O   . LYS B 1 265 ? 64.847 1.812   46.239  1.00 61.88  ? 273 LYS B O   1 
ATOM   4409 C  CB  . LYS B 1 265 ? 67.302 2.180   44.442  1.00 61.45  ? 273 LYS B CB  1 
ATOM   4410 C  CG  . LYS B 1 265 ? 68.683 1.887   43.868  1.00 78.59  ? 273 LYS B CG  1 
ATOM   4411 C  CD  . LYS B 1 265 ? 69.428 3.144   43.464  1.00 91.05  ? 273 LYS B CD  1 
ATOM   4412 C  CE  . LYS B 1 265 ? 70.435 2.907   42.359  1.00 108.64 ? 273 LYS B CE  1 
ATOM   4413 N  NZ  . LYS B 1 265 ? 70.285 3.901   41.269  1.00 107.81 ? 273 LYS B NZ  1 
ATOM   4414 N  N   . PHE B 1 266 ? 63.998 1.403   44.193  1.00 47.50  ? 274 PHE B N   1 
ATOM   4415 C  CA  . PHE B 1 266 ? 62.661 1.856   44.556  1.00 48.51  ? 274 PHE B CA  1 
ATOM   4416 C  C   . PHE B 1 266 ? 62.052 0.898   45.578  1.00 53.90  ? 274 PHE B C   1 
ATOM   4417 O  O   . PHE B 1 266 ? 62.315 -0.301  45.545  1.00 51.40  ? 274 PHE B O   1 
ATOM   4418 C  CB  . PHE B 1 266 ? 61.728 1.925   43.342  1.00 50.90  ? 274 PHE B CB  1 
ATOM   4419 C  CG  . PHE B 1 266 ? 61.940 3.083   42.398  1.00 51.67  ? 274 PHE B CG  1 
ATOM   4420 C  CD1 . PHE B 1 266 ? 62.546 4.259   42.816  1.00 60.21  ? 274 PHE B CD1 1 
ATOM   4421 C  CD2 . PHE B 1 266 ? 61.536 2.986   41.076  1.00 49.18  ? 274 PHE B CD2 1 
ATOM   4422 C  CE1 . PHE B 1 266 ? 62.732 5.312   41.934  1.00 55.48  ? 274 PHE B CE1 1 
ATOM   4423 C  CE2 . PHE B 1 266 ? 61.727 4.038   40.195  1.00 59.14  ? 274 PHE B CE2 1 
ATOM   4424 C  CZ  . PHE B 1 266 ? 62.324 5.199   40.626  1.00 55.12  ? 274 PHE B CZ  1 
ATOM   4425 N  N   . ARG B 1 267 ? 61.228 1.437   46.481  1.00 50.26  ? 275 ARG B N   1 
ATOM   4426 C  CA  . ARG B 1 267 ? 60.429 0.603   47.362  1.00 50.69  ? 275 ARG B CA  1 
ATOM   4427 C  C   . ARG B 1 267 ? 59.131 0.257   46.637  1.00 48.48  ? 275 ARG B C   1 
ATOM   4428 O  O   . ARG B 1 267 ? 58.300 1.133   46.411  1.00 53.92  ? 275 ARG B O   1 
ATOM   4429 C  CB  . ARG B 1 267 ? 60.158 1.331   48.683  1.00 53.13  ? 275 ARG B CB  1 
ATOM   4430 C  CG  . ARG B 1 267 ? 59.227 0.596   49.639  1.00 65.53  ? 275 ARG B CG  1 
ATOM   4431 C  CD  . ARG B 1 267 ? 58.779 1.508   50.767  1.00 68.09  ? 275 ARG B CD  1 
ATOM   4432 N  NE  . ARG B 1 267 ? 59.935 2.135   51.391  1.00 68.77  ? 275 ARG B NE  1 
ATOM   4433 C  CZ  . ARG B 1 267 ? 60.152 3.445   51.456  1.00 65.38  ? 275 ARG B CZ  1 
ATOM   4434 N  NH1 . ARG B 1 267 ? 61.383 3.894   51.663  1.00 78.19  ? 275 ARG B NH1 1 
ATOM   4435 N  NH2 . ARG B 1 267 ? 59.166 4.299   51.230  1.00 61.99  ? 275 ARG B NH2 1 
ATOM   4436 N  N   . LYS B 1 268 ? 58.966 -1.016  46.263  1.00 49.44  ? 276 LYS B N   1 
ATOM   4437 C  CA  . LYS B 1 268 ? 57.800 -1.419  45.494  1.00 45.73  ? 276 LYS B CA  1 
ATOM   4438 C  C   . LYS B 1 268 ? 56.623 -1.691  46.425  1.00 44.86  ? 276 LYS B C   1 
ATOM   4439 O  O   . LYS B 1 268 ? 56.743 -1.605  47.645  1.00 41.64  ? 276 LYS B O   1 
ATOM   4440 C  CB  . LYS B 1 268 ? 58.036 -2.694  44.682  1.00 51.11  ? 276 LYS B CB  1 
ATOM   4441 C  CG  . LYS B 1 268 ? 59.467 -2.952  44.242  1.00 61.46  ? 276 LYS B CG  1 
ATOM   4442 C  CD  . LYS B 1 268 ? 60.022 -1.922  43.294  1.00 55.36  ? 276 LYS B CD  1 
ATOM   4443 C  CE  . LYS B 1 268 ? 61.367 -2.343  42.746  1.00 59.32  ? 276 LYS B CE  1 
ATOM   4444 N  NZ  . LYS B 1 268 ? 62.410 -2.326  43.799  1.00 57.46  ? 276 LYS B NZ  1 
ATOM   4445 N  N   . SER B 1 269 ? 55.504 -2.078  45.804  1.00 45.58  ? 277 SER B N   1 
ATOM   4446 C  CA  . SER B 1 269 ? 54.217 -2.200  46.467  1.00 46.73  ? 277 SER B CA  1 
ATOM   4447 C  C   . SER B 1 269 ? 54.163 -3.444  47.350  1.00 55.15  ? 277 SER B C   1 
ATOM   4448 O  O   . SER B 1 269 ? 53.219 -3.610  48.120  1.00 57.86  ? 277 SER B O   1 
ATOM   4449 C  CB  . SER B 1 269 ? 53.111 -2.223  45.448  1.00 42.86  ? 277 SER B CB  1 
ATOM   4450 O  OG  . SER B 1 269 ? 53.338 -3.243  44.487  1.00 45.66  ? 277 SER B OG  1 
ATOM   4451 N  N   . THR B 1 270 ? 55.162 -4.325  47.219  1.00 47.07  ? 278 THR B N   1 
ATOM   4452 C  CA  . THR B 1 270 ? 55.231 -5.509  48.061  1.00 56.44  ? 278 THR B CA  1 
ATOM   4453 C  C   . THR B 1 270 ? 55.943 -5.173  49.371  1.00 55.66  ? 278 THR B C   1 
ATOM   4454 O  O   . THR B 1 270 ? 55.847 -5.934  50.329  1.00 58.59  ? 278 THR B O   1 
ATOM   4455 C  CB  . THR B 1 270 ? 55.894 -6.691  47.338  1.00 50.67  ? 278 THR B CB  1 
ATOM   4456 O  OG1 . THR B 1 270 ? 57.038 -6.205  46.635  1.00 54.27  ? 278 THR B OG1 1 
ATOM   4457 C  CG2 . THR B 1 270 ? 54.969 -7.395  46.369  1.00 50.39  ? 278 THR B CG2 1 
ATOM   4458 N  N   . GLU B 1 271 ? 56.647 -4.031  49.416  1.00 62.89  ? 279 GLU B N   1 
ATOM   4459 C  CA  . GLU B 1 271 ? 57.350 -3.630  50.628  1.00 55.79  ? 279 GLU B CA  1 
ATOM   4460 C  C   . GLU B 1 271 ? 56.701 -2.403  51.265  1.00 52.91  ? 279 GLU B C   1 
ATOM   4461 O  O   . GLU B 1 271 ? 56.803 -2.223  52.476  1.00 52.33  ? 279 GLU B O   1 
ATOM   4462 C  CB  . GLU B 1 271 ? 58.825 -3.297  50.382  1.00 66.42  ? 279 GLU B CB  1 
ATOM   4463 C  CG  . GLU B 1 271 ? 59.671 -4.466  49.915  1.00 70.95  ? 279 GLU B CG  1 
ATOM   4464 C  CD  . GLU B 1 271 ? 59.819 -4.561  48.407  1.00 93.48  ? 279 GLU B CD  1 
ATOM   4465 O  OE1 . GLU B 1 271 ? 59.334 -5.554  47.829  1.00 100.24 ? 279 GLU B OE1 1 
ATOM   4466 O  OE2 . GLU B 1 271 ? 60.424 -3.640  47.812  1.00 63.55  ? 279 GLU B OE2 1 
ATOM   4467 N  N   . GLY B 1 272 ? 56.070 -1.538  50.462  1.00 50.81  ? 280 GLY B N   1 
ATOM   4468 C  CA  . GLY B 1 272 ? 55.459 -0.342  51.019  1.00 52.03  ? 280 GLY B CA  1 
ATOM   4469 C  C   . GLY B 1 272 ? 55.235 0.767   49.994  1.00 52.49  ? 280 GLY B C   1 
ATOM   4470 O  O   . GLY B 1 272 ? 54.952 0.502   48.828  1.00 49.70  ? 280 GLY B O   1 
ATOM   4471 N  N   . TYR B 1 273 ? 55.366 2.015   50.461  1.00 47.97  ? 281 TYR B N   1 
ATOM   4472 C  CA  . TYR B 1 273 ? 54.934 3.183   49.712  1.00 49.16  ? 281 TYR B CA  1 
ATOM   4473 C  C   . TYR B 1 273 ? 55.789 4.392   50.080  1.00 47.24  ? 281 TYR B C   1 
ATOM   4474 O  O   . TYR B 1 273 ? 56.714 4.286   50.880  1.00 50.11  ? 281 TYR B O   1 
ATOM   4475 C  CB  . TYR B 1 273 ? 53.459 3.426   50.039  1.00 46.16  ? 281 TYR B CB  1 
ATOM   4476 C  CG  . TYR B 1 273 ? 53.117 3.153   51.497  1.00 52.66  ? 281 TYR B CG  1 
ATOM   4477 C  CD1 . TYR B 1 273 ? 53.552 3.993   52.517  1.00 57.26  ? 281 TYR B CD1 1 
ATOM   4478 C  CD2 . TYR B 1 273 ? 52.389 2.025   51.854  1.00 56.32  ? 281 TYR B CD2 1 
ATOM   4479 C  CE1 . TYR B 1 273 ? 53.249 3.734   53.844  1.00 59.64  ? 281 TYR B CE1 1 
ATOM   4480 C  CE2 . TYR B 1 273 ? 52.082 1.753   53.177  1.00 64.57  ? 281 TYR B CE2 1 
ATOM   4481 C  CZ  . TYR B 1 273 ? 52.512 2.610   54.174  1.00 59.90  ? 281 TYR B CZ  1 
ATOM   4482 O  OH  . TYR B 1 273 ? 52.206 2.336   55.476  1.00 61.80  ? 281 TYR B OH  1 
ATOM   4483 N  N   . TYR B 1 274 ? 55.446 5.541   49.488  1.00 55.60  ? 282 TYR B N   1 
ATOM   4484 C  CA  . TYR B 1 274 ? 56.108 6.804   49.772  1.00 48.39  ? 282 TYR B CA  1 
ATOM   4485 C  C   . TYR B 1 274 ? 55.058 7.799   50.262  1.00 49.89  ? 282 TYR B C   1 
ATOM   4486 O  O   . TYR B 1 274 ? 53.986 7.906   49.672  1.00 53.94  ? 282 TYR B O   1 
ATOM   4487 C  CB  . TYR B 1 274 ? 56.829 7.334   48.527  1.00 49.14  ? 282 TYR B CB  1 
ATOM   4488 C  CG  . TYR B 1 274 ? 58.017 6.514   48.037  1.00 46.40  ? 282 TYR B CG  1 
ATOM   4489 C  CD1 . TYR B 1 274 ? 57.850 5.434   47.179  1.00 46.15  ? 282 TYR B CD1 1 
ATOM   4490 C  CD2 . TYR B 1 274 ? 59.311 6.825   48.438  1.00 51.54  ? 282 TYR B CD2 1 
ATOM   4491 C  CE1 . TYR B 1 274 ? 58.933 4.695   46.729  1.00 47.75  ? 282 TYR B CE1 1 
ATOM   4492 C  CE2 . TYR B 1 274 ? 60.400 6.091   48.001  1.00 48.36  ? 282 TYR B CE2 1 
ATOM   4493 C  CZ  . TYR B 1 274 ? 60.212 5.023   47.144  1.00 52.25  ? 282 TYR B CZ  1 
ATOM   4494 O  OH  . TYR B 1 274 ? 61.288 4.300   46.716  1.00 52.42  ? 282 TYR B OH  1 
ATOM   4495 N  N   . GLU B 1 275 ? 55.378 8.525   51.341  1.00 51.80  ? 283 GLU B N   1 
ATOM   4496 C  CA  . GLU B 1 275 ? 54.438 9.451   51.955  1.00 56.87  ? 283 GLU B CA  1 
ATOM   4497 C  C   . GLU B 1 275 ? 54.986 10.883  51.891  1.00 45.95  ? 283 GLU B C   1 
ATOM   4498 O  O   . GLU B 1 275 ? 56.187 11.026  51.586  1.00 52.40  ? 283 GLU B O   1 
ATOM   4499 C  CB  . GLU B 1 275 ? 54.158 9.051   53.406  1.00 58.66  ? 283 GLU B CB  1 
ATOM   4500 C  CG  . GLU B 1 275 ? 53.141 7.932   53.548  1.00 63.23  ? 283 GLU B CG  1 
ATOM   4501 C  CD  . GLU B 1 275 ? 52.749 7.628   54.985  1.00 67.45  ? 283 GLU B CD  1 
ATOM   4502 O  OE1 . GLU B 1 275 ? 53.216 8.352   55.888  1.00 57.06  ? 283 GLU B OE1 1 
ATOM   4503 O  OE2 . GLU B 1 275 ? 51.983 6.668   55.200  1.00 60.19  ? 283 GLU B OE2 1 
HETATM 4504 S  S   . SO4 C 2 .   ? 47.247 30.346  -2.052  1.00 85.61  ? 301 SO4 A S   1 
HETATM 4505 O  O1  . SO4 C 2 .   ? 46.633 29.073  -2.321  1.00 70.91  ? 301 SO4 A O1  1 
HETATM 4506 O  O2  . SO4 C 2 .   ? 47.274 31.129  -3.259  1.00 76.22  ? 301 SO4 A O2  1 
HETATM 4507 O  O3  . SO4 C 2 .   ? 46.490 31.041  -1.045  1.00 77.63  ? 301 SO4 A O3  1 
HETATM 4508 O  O4  . SO4 C 2 .   ? 48.592 30.142  -1.586  1.00 75.35  ? 301 SO4 A O4  1 
HETATM 4509 C  C1  . PEG D 3 .   ? 47.055 3.008   -2.755  1.00 83.48  ? 302 PEG A C1  1 
HETATM 4510 O  O1  . PEG D 3 .   ? 47.705 2.721   -3.982  1.00 74.79  ? 302 PEG A O1  1 
HETATM 4511 C  C2  . PEG D 3 .   ? 45.580 3.217   -2.926  1.00 77.46  ? 302 PEG A C2  1 
HETATM 4512 O  O2  . PEG D 3 .   ? 44.867 2.134   -2.337  1.00 70.14  ? 302 PEG A O2  1 
HETATM 4513 C  C3  . PEG D 3 .   ? 44.739 1.016   -3.210  1.00 85.82  ? 302 PEG A C3  1 
HETATM 4514 C  C4  . PEG D 3 .   ? 45.395 -0.183  -2.600  1.00 85.89  ? 302 PEG A C4  1 
HETATM 4515 O  O4  . PEG D 3 .   ? 44.811 -0.544  -1.361  1.00 74.81  ? 302 PEG A O4  1 
HETATM 4516 C  C1  . PGE E 4 .   ? 28.713 10.193  -19.609 1.00 83.27  ? 303 PGE A C1  1 
HETATM 4517 O  O1  . PGE E 4 .   ? 27.399 10.221  -19.080 1.00 93.31  ? 303 PGE A O1  1 
HETATM 4518 C  C2  . PGE E 4 .   ? 28.959 8.993   -20.474 1.00 85.31  ? 303 PGE A C2  1 
HETATM 4519 O  O2  . PGE E 4 .   ? 28.858 7.801   -19.701 1.00 67.23  ? 303 PGE A O2  1 
HETATM 4520 C  C3  . PGE E 4 .   ? 28.314 6.707   -20.434 1.00 75.72  ? 303 PGE A C3  1 
HETATM 4521 C  C4  . PGE E 4 .   ? 26.834 6.616   -20.200 1.00 79.42  ? 303 PGE A C4  1 
HETATM 4522 O  O4  . PGE E 4 .   ? 24.643 2.855   -21.992 1.00 76.27  ? 303 PGE A O4  1 
HETATM 4523 C  C6  . PGE E 4 .   ? 25.804 3.660   -22.100 1.00 95.97  ? 303 PGE A C6  1 
HETATM 4524 C  C5  . PGE E 4 .   ? 26.044 4.483   -20.873 1.00 88.50  ? 303 PGE A C5  1 
HETATM 4525 O  O3  . PGE E 4 .   ? 26.227 5.848   -21.235 1.00 82.31  ? 303 PGE A O3  1 
HETATM 4526 S  S   . SO4 F 2 .   ? 50.336 10.416  4.961   1.00 84.70  ? 304 SO4 A S   1 
HETATM 4527 O  O1  . SO4 F 2 .   ? 50.538 10.916  3.627   1.00 95.20  ? 304 SO4 A O1  1 
HETATM 4528 O  O2  . SO4 F 2 .   ? 50.793 9.054   5.037   1.00 82.02  ? 304 SO4 A O2  1 
HETATM 4529 O  O3  . SO4 F 2 .   ? 48.935 10.470  5.287   1.00 64.04  ? 304 SO4 A O3  1 
HETATM 4530 O  O4  . SO4 F 2 .   ? 51.076 11.223  5.894   1.00 80.18  ? 304 SO4 A O4  1 
HETATM 4531 C  C1  . EDO G 5 .   ? 50.907 25.134  16.541  1.00 62.04  ? 305 EDO A C1  1 
HETATM 4532 O  O1  . EDO G 5 .   ? 51.909 24.342  17.151  1.00 65.17  ? 305 EDO A O1  1 
HETATM 4533 C  C2  . EDO G 5 .   ? 50.983 25.123  15.058  1.00 59.58  ? 305 EDO A C2  1 
HETATM 4534 O  O2  . EDO G 5 .   ? 49.790 25.569  14.440  1.00 62.61  ? 305 EDO A O2  1 
HETATM 4535 FE FE  . FE  H 6 .   ? 27.815 20.349  3.962   1.00 51.60  ? 306 FE  A FE  1 
HETATM 4536 CO CO  . CO  I 7 .   ? 29.971 20.843  6.572   1.00 48.39  ? 307 CO  A CO  1 
HETATM 4537 S  S   . SO4 J 2 .   ? 38.464 17.275  26.538  1.00 88.80  ? 401 SO4 B S   1 
HETATM 4538 O  O1  . SO4 J 2 .   ? 38.830 18.278  25.573  1.00 91.14  ? 401 SO4 B O1  1 
HETATM 4539 O  O2  . SO4 J 2 .   ? 39.202 16.068  26.275  1.00 65.90  ? 401 SO4 B O2  1 
HETATM 4540 O  O3  . SO4 J 2 .   ? 37.054 17.007  26.439  1.00 83.87  ? 401 SO4 B O3  1 
HETATM 4541 O  O4  . SO4 J 2 .   ? 38.772 17.747  27.862  1.00 98.88  ? 401 SO4 B O4  1 
HETATM 4542 S  S   . SO4 K 2 .   ? 57.254 24.587  33.584  1.00 88.47  ? 402 SO4 B S   1 
HETATM 4543 O  O1  . SO4 K 2 .   ? 58.259 24.305  32.593  1.00 82.43  ? 402 SO4 B O1  1 
HETATM 4544 O  O2  . SO4 K 2 .   ? 56.416 25.663  33.126  1.00 82.72  ? 402 SO4 B O2  1 
HETATM 4545 O  O3  . SO4 K 2 .   ? 56.453 23.413  33.801  1.00 83.60  ? 402 SO4 B O3  1 
HETATM 4546 O  O4  . SO4 K 2 .   ? 57.890 24.967  34.817  1.00 76.47  ? 402 SO4 B O4  1 
HETATM 4547 C  C1  . EDO L 5 .   ? 62.657 -0.017  53.597  1.00 68.66  ? 403 EDO B C1  1 
HETATM 4548 O  O1  . EDO L 5 .   ? 63.707 -0.901  53.937  1.00 72.62  ? 403 EDO B O1  1 
HETATM 4549 C  C2  . EDO L 5 .   ? 62.879 0.660   52.299  1.00 63.05  ? 403 EDO B C2  1 
HETATM 4550 O  O2  . EDO L 5 .   ? 63.257 -0.236  51.274  1.00 75.20  ? 403 EDO B O2  1 
HETATM 4551 C  C1  . PEG M 3 .   ? 32.017 7.246   33.546  1.00 78.11  ? 404 PEG B C1  1 
HETATM 4552 O  O1  . PEG M 3 .   ? 30.863 8.010   33.845  1.00 85.70  ? 404 PEG B O1  1 
HETATM 4553 C  C2  . PEG M 3 .   ? 33.151 7.539   34.481  1.00 76.96  ? 404 PEG B C2  1 
HETATM 4554 O  O2  . PEG M 3 .   ? 34.082 8.416   33.855  1.00 71.52  ? 404 PEG B O2  1 
HETATM 4555 C  C3  . PEG M 3 .   ? 34.486 9.490   34.698  1.00 81.28  ? 404 PEG B C3  1 
HETATM 4556 C  C4  . PEG M 3 .   ? 33.569 10.662  34.508  1.00 82.93  ? 404 PEG B C4  1 
HETATM 4557 O  O4  . PEG M 3 .   ? 33.072 11.164  35.736  1.00 72.02  ? 404 PEG B O4  1 
HETATM 4558 FE FE  . FE  N 6 .   ? 58.304 2.736   27.546  1.00 49.89  ? 405 FE  B FE  1 
HETATM 4559 CO CO  . CO  O 7 .   ? 57.641 4.819   24.888  1.00 47.37  ? 406 CO  B CO  1 
HETATM 4560 O  O   . HOH P 8 .   ? 41.130 3.695   -0.254  1.00 55.49  ? 401 HOH A O   1 
HETATM 4561 O  O   . HOH P 8 .   ? 18.057 22.082  11.619  1.00 55.03  ? 402 HOH A O   1 
HETATM 4562 O  O   . HOH P 8 .   ? 29.398 29.323  4.937   1.00 49.66  ? 403 HOH A O   1 
HETATM 4563 O  O   . HOH P 8 .   ? 41.741 28.549  7.979   1.00 47.68  ? 404 HOH A O   1 
HETATM 4564 O  O   . HOH P 8 .   ? 27.887 17.596  -15.010 1.00 42.58  ? 405 HOH A O   1 
HETATM 4565 O  O   . HOH P 8 .   ? 36.592 23.161  1.757   1.00 43.80  ? 406 HOH A O   1 
HETATM 4566 O  O   . HOH P 8 .   ? 39.471 30.674  -15.814 1.00 50.89  ? 407 HOH A O   1 
HETATM 4567 O  O   . HOH P 8 .   ? 26.398 9.886   5.975   1.00 48.40  ? 408 HOH A O   1 
HETATM 4568 O  O   . HOH P 8 .   ? 32.245 1.399   20.826  1.00 59.05  ? 409 HOH A O   1 
HETATM 4569 O  O   . HOH P 8 .   ? 45.763 23.873  7.684   1.00 43.61  ? 410 HOH A O   1 
HETATM 4570 O  O   . HOH P 8 .   ? 28.445 19.644  6.117   1.00 55.27  ? 411 HOH A O   1 
HETATM 4571 O  O   . HOH P 8 .   ? 47.920 19.040  12.801  1.00 40.70  ? 412 HOH A O   1 
HETATM 4572 O  O   . HOH P 8 .   ? 31.353 5.887   4.030   1.00 49.47  ? 413 HOH A O   1 
HETATM 4573 O  O   . HOH P 8 .   ? 38.384 3.332   -5.381  1.00 48.56  ? 414 HOH A O   1 
HETATM 4574 O  O   . HOH P 8 .   ? 48.121 13.506  9.806   1.00 49.46  ? 415 HOH A O   1 
HETATM 4575 O  O   . HOH P 8 .   ? 25.095 10.272  -13.465 1.00 48.01  ? 416 HOH A O   1 
HETATM 4576 O  O   . HOH P 8 .   ? 34.466 20.187  12.879  1.00 44.13  ? 417 HOH A O   1 
HETATM 4577 O  O   . HOH P 8 .   ? 29.826 10.886  6.944   1.00 50.77  ? 418 HOH A O   1 
HETATM 4578 O  O   . HOH P 8 .   ? 25.390 7.509   7.452   1.00 49.23  ? 419 HOH A O   1 
HETATM 4579 O  O   . HOH P 8 .   ? 23.207 14.130  -11.436 1.00 50.25  ? 420 HOH A O   1 
HETATM 4580 O  O   . HOH P 8 .   ? 30.643 11.888  9.201   1.00 44.53  ? 421 HOH A O   1 
HETATM 4581 O  O   . HOH P 8 .   ? 26.541 25.643  -4.803  1.00 51.84  ? 422 HOH A O   1 
HETATM 4582 O  O   . HOH P 8 .   ? 44.765 24.092  -10.856 1.00 59.59  ? 423 HOH A O   1 
HETATM 4583 O  O   . HOH P 8 .   ? 44.443 17.617  14.926  1.00 39.00  ? 424 HOH A O   1 
HETATM 4584 O  O   . HOH P 8 .   ? 38.811 26.948  6.199   1.00 35.75  ? 425 HOH A O   1 
HETATM 4585 O  O   . HOH P 8 .   ? 42.506 29.300  4.191   1.00 47.11  ? 426 HOH A O   1 
HETATM 4586 O  O   . HOH P 8 .   ? 26.220 6.288   13.644  1.00 50.14  ? 427 HOH A O   1 
HETATM 4587 O  O   . HOH P 8 .   ? 27.502 19.575  -1.561  1.00 49.43  ? 428 HOH A O   1 
HETATM 4588 O  O   . HOH P 8 .   ? 35.749 29.199  -15.362 1.00 48.43  ? 429 HOH A O   1 
HETATM 4589 O  O   . HOH P 8 .   ? 27.730 21.429  7.144   1.00 49.62  ? 430 HOH A O   1 
HETATM 4590 O  O   . HOH P 8 .   ? 10.654 26.731  6.717   1.00 63.06  ? 431 HOH A O   1 
HETATM 4591 O  O   . HOH P 8 .   ? 28.854 15.587  -0.795  1.00 49.60  ? 432 HOH A O   1 
HETATM 4592 O  O   . HOH P 8 .   ? 41.833 18.029  15.267  1.00 44.00  ? 433 HOH A O   1 
HETATM 4593 O  O   . HOH P 8 .   ? 36.180 27.101  6.484   1.00 42.58  ? 434 HOH A O   1 
HETATM 4594 O  O   . HOH P 8 .   ? 48.958 21.482  -13.601 1.00 54.35  ? 435 HOH A O   1 
HETATM 4595 O  O   . HOH P 8 .   ? 20.880 15.135  -12.321 1.00 47.70  ? 436 HOH A O   1 
HETATM 4596 O  O   . HOH P 8 .   ? 31.970 23.007  -3.948  1.00 47.52  ? 437 HOH A O   1 
HETATM 4597 O  O   . HOH P 8 .   ? 18.596 23.657  -6.493  1.00 56.72  ? 438 HOH A O   1 
HETATM 4598 O  O   . HOH P 8 .   ? 39.313 17.596  5.093   1.00 38.49  ? 439 HOH A O   1 
HETATM 4599 O  O   . HOH P 8 .   ? 9.508  36.268  12.319  1.00 62.72  ? 440 HOH A O   1 
HETATM 4600 O  O   . HOH P 8 .   ? 33.167 40.963  4.489   1.00 58.89  ? 441 HOH A O   1 
HETATM 4601 O  O   . HOH P 8 .   ? 45.947 4.655   5.457   1.00 64.23  ? 442 HOH A O   1 
HETATM 4602 O  O   . HOH P 8 .   ? 50.467 26.307  -1.478  1.00 53.25  ? 443 HOH A O   1 
HETATM 4603 O  O   . HOH P 8 .   ? 21.847 7.715   -11.321 1.00 53.40  ? 444 HOH A O   1 
HETATM 4604 O  O   . HOH P 8 .   ? 47.357 21.836  17.661  1.00 41.13  ? 445 HOH A O   1 
HETATM 4605 O  O   . HOH P 8 .   ? 22.277 9.347   -13.047 1.00 53.40  ? 446 HOH A O   1 
HETATM 4606 O  O   . HOH P 8 .   ? 47.846 6.665   -6.909  1.00 61.21  ? 447 HOH A O   1 
HETATM 4607 O  O   . HOH P 8 .   ? 43.399 31.194  8.729   1.00 52.06  ? 448 HOH A O   1 
HETATM 4608 O  O   . HOH P 8 .   ? 26.486 21.183  5.559   1.00 46.50  ? 449 HOH A O   1 
HETATM 4609 O  O   . HOH P 8 .   ? 50.132 26.502  -5.381  1.00 58.43  ? 450 HOH A O   1 
HETATM 4610 O  O   . HOH P 8 .   ? 44.598 25.048  9.812   1.00 49.67  ? 451 HOH A O   1 
HETATM 4611 O  O   . HOH P 8 .   ? 24.683 -0.127  6.940   1.00 53.43  ? 452 HOH A O   1 
HETATM 4612 O  O   . HOH P 8 .   ? 40.919 -3.470  -2.850  1.00 67.23  ? 453 HOH A O   1 
HETATM 4613 O  O   . HOH Q 8 .   ? 37.120 5.804   31.730  1.00 53.56  ? 501 HOH B O   1 
HETATM 4614 O  O   . HOH Q 8 .   ? 65.343 8.641   26.642  1.00 45.18  ? 502 HOH B O   1 
HETATM 4615 O  O   . HOH Q 8 .   ? 52.352 20.064  23.755  1.00 43.98  ? 503 HOH B O   1 
HETATM 4616 O  O   . HOH Q 8 .   ? 58.391 18.917  23.612  1.00 43.27  ? 504 HOH B O   1 
HETATM 4617 O  O   . HOH Q 8 .   ? 67.920 7.776   25.792  1.00 49.48  ? 505 HOH B O   1 
HETATM 4618 O  O   . HOH Q 8 .   ? 56.292 11.652  29.782  1.00 42.07  ? 506 HOH B O   1 
HETATM 4619 O  O   . HOH Q 8 .   ? 57.449 2.818   25.440  1.00 56.50  ? 507 HOH B O   1 
HETATM 4620 O  O   . HOH Q 8 .   ? 49.878 -3.731  25.465  1.00 53.00  ? 508 HOH B O   1 
HETATM 4621 O  O   . HOH Q 8 .   ? 55.756 1.368   46.507  1.00 41.94  ? 509 HOH B O   1 
HETATM 4622 O  O   . HOH Q 8 .   ? 62.625 17.620  15.778  1.00 43.23  ? 510 HOH B O   1 
HETATM 4623 O  O   . HOH Q 8 .   ? 38.324 3.266   36.794  1.00 51.93  ? 511 HOH B O   1 
HETATM 4624 O  O   . HOH Q 8 .   ? 43.991 -1.502  27.357  1.00 49.68  ? 512 HOH B O   1 
HETATM 4625 O  O   . HOH Q 8 .   ? 64.785 -4.728  19.840  1.00 57.50  ? 513 HOH B O   1 
HETATM 4626 O  O   . HOH Q 8 .   ? 55.033 -4.322  42.844  1.00 48.17  ? 514 HOH B O   1 
HETATM 4627 O  O   . HOH Q 8 .   ? 55.844 4.113   33.862  1.00 43.32  ? 515 HOH B O   1 
HETATM 4628 O  O   . HOH Q 8 .   ? 47.109 19.543  18.672  1.00 39.48  ? 516 HOH B O   1 
HETATM 4629 O  O   . HOH Q 8 .   ? 50.898 -4.588  44.976  1.00 49.34  ? 517 HOH B O   1 
HETATM 4630 O  O   . HOH Q 8 .   ? 54.826 8.417   18.622  1.00 46.75  ? 518 HOH B O   1 
HETATM 4631 O  O   . HOH Q 8 .   ? 33.357 4.204   30.736  1.00 54.95  ? 519 HOH B O   1 
HETATM 4632 O  O   . HOH Q 8 .   ? 72.698 14.509  36.326  1.00 63.08  ? 520 HOH B O   1 
HETATM 4633 O  O   . HOH Q 8 .   ? 49.527 1.015   22.349  1.00 49.67  ? 521 HOH B O   1 
HETATM 4634 O  O   . HOH Q 8 .   ? 62.259 14.026  26.582  1.00 44.20  ? 522 HOH B O   1 
HETATM 4635 O  O   . HOH Q 8 .   ? 47.632 15.769  16.624  1.00 39.97  ? 523 HOH B O   1 
HETATM 4636 O  O   . HOH Q 8 .   ? 61.886 13.992  46.798  1.00 50.55  ? 524 HOH B O   1 
HETATM 4637 O  O   . HOH Q 8 .   ? 58.532 15.569  25.351  1.00 37.29  ? 525 HOH B O   1 
HETATM 4638 O  O   . HOH Q 8 .   ? 63.173 8.014   25.404  1.00 48.51  ? 526 HOH B O   1 
HETATM 4639 O  O   . HOH Q 8 .   ? 63.514 4.271   36.328  1.00 53.57  ? 527 HOH B O   1 
HETATM 4640 O  O   . HOH Q 8 .   ? 39.348 5.545   46.560  1.00 62.45  ? 528 HOH B O   1 
HETATM 4641 O  O   . HOH Q 8 .   ? 48.866 -0.142  24.566  1.00 54.64  ? 529 HOH B O   1 
HETATM 4642 O  O   . HOH Q 8 .   ? 57.205 -5.894  43.889  1.00 49.97  ? 530 HOH B O   1 
HETATM 4643 O  O   . HOH Q 8 .   ? 59.315 3.052   24.312  1.00 49.39  ? 531 HOH B O   1 
HETATM 4644 O  O   . HOH Q 8 .   ? 42.130 16.899  21.721  1.00 48.86  ? 532 HOH B O   1 
HETATM 4645 O  O   . HOH Q 8 .   ? 58.785 19.939  27.473  1.00 46.70  ? 533 HOH B O   1 
HETATM 4646 O  O   . HOH Q 8 .   ? 48.367 -5.859  24.122  1.00 50.40  ? 534 HOH B O   1 
HETATM 4647 O  O   . HOH Q 8 .   ? 57.814 2.148   33.118  1.00 53.58  ? 535 HOH B O   1 
HETATM 4648 O  O   . HOH Q 8 .   ? 46.927 -2.215  51.532  1.00 57.80  ? 536 HOH B O   1 
HETATM 4649 O  O   . HOH Q 8 .   ? 49.369 13.787  16.264  1.00 43.00  ? 537 HOH B O   1 
HETATM 4650 O  O   . HOH Q 8 .   ? 50.169 11.332  26.451  1.00 41.60  ? 538 HOH B O   1 
HETATM 4651 O  O   . HOH Q 8 .   ? 46.836 -5.594  17.887  1.00 48.96  ? 539 HOH B O   1 
HETATM 4652 O  O   . HOH Q 8 .   ? 60.023 13.251  25.121  1.00 39.04  ? 540 HOH B O   1 
HETATM 4653 O  O   . HOH Q 8 .   ? 53.712 1.307   32.334  1.00 51.72  ? 541 HOH B O   1 
HETATM 4654 O  O   . HOH Q 8 .   ? 49.946 -12.011 17.286  1.00 62.40  ? 542 HOH B O   1 
HETATM 4655 O  O   . HOH Q 8 .   ? 49.821 20.457  13.823  1.00 39.48  ? 543 HOH B O   1 
HETATM 4656 O  O   . HOH Q 8 .   ? 72.586 -8.954  24.732  1.00 60.10  ? 544 HOH B O   1 
HETATM 4657 O  O   . HOH Q 8 .   ? 49.049 21.687  45.119  1.00 60.71  ? 545 HOH B O   1 
HETATM 4658 O  O   . HOH Q 8 .   ? 58.479 7.651   35.403  1.00 46.95  ? 546 HOH B O   1 
HETATM 4659 O  O   . HOH Q 8 .   ? 73.591 17.699  27.106  1.00 58.21  ? 547 HOH B O   1 
HETATM 4660 O  O   . HOH Q 8 .   ? 50.379 -8.822  42.822  1.00 56.87  ? 548 HOH B O   1 
HETATM 4661 O  O   . HOH Q 8 .   ? 36.405 13.165  38.385  1.00 58.68  ? 549 HOH B O   1 
HETATM 4662 O  O   . HOH Q 8 .   ? 51.537 -7.552  44.538  1.00 49.29  ? 550 HOH B O   1 
HETATM 4663 O  O   . HOH Q 8 .   ? 59.644 1.953   25.912  1.00 45.92  ? 551 HOH B O   1 
HETATM 4664 O  O   . HOH Q 8 .   ? 41.822 -10.072 24.771  1.00 54.90  ? 552 HOH B O   1 
HETATM 4665 O  O   . HOH Q 8 .   ? 63.514 25.790  30.103  1.00 61.08  ? 553 HOH B O   1 
HETATM 4666 O  O   . HOH Q 8 .   ? 53.993 19.688  21.673  1.00 50.74  ? 554 HOH B O   1 
HETATM 4667 O  O   . HOH Q 8 .   ? 59.713 21.487  22.874  1.00 52.70  ? 555 HOH B O   1 
HETATM 4668 O  O   . HOH Q 8 .   ? 57.776 5.371   34.092  1.00 71.28  ? 556 HOH B O   1 
HETATM 4669 O  O   . HOH Q 8 .   ? 31.063 1.774   34.227  1.00 65.76  ? 557 HOH B O   1 
# 
