data_8RHU
# 
_entry.id   8RHU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8RHU         pdb_00008rhu 10.2210/pdb8rhu/pdb 
WWPDB D_1292135164 ?            ?                   
# 
_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       2024-11-20 
# 
_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                        8RHU 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Crystal Structure of Trypanosoma brucei DHFR in complex with the cofactor and inhibitor P25' 
_pdbx_database_related.db_id          8RHT 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pozzi4@unisi.it 
_pdbx_contact_author.name_first         Cecilia 
_pdbx_contact_author.name_last          Pozzi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2574-3911 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pozzi, C.'   1 0000-0003-2574-3911 
'Mangani, S.' 2 0000-0003-4824-7478 
'Landi, G.'   3 0000-0001-6332-166X 
# 
_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            'Acs Infect Dis.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2373-8227 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                2755 
_citation.page_last                 2774 
_citation.title                     
;Identification of Innovative Folate Inhibitors Leveraging the Amino Dihydrotriazine Motif from Cycloguanil for Their Potential as Anti- Trypanosoma brucei Agents.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsinfecdis.4c00113 
_citation.pdbx_database_id_PubMed   38953453 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Francesconi, V.'       1  ?                   
primary 'Rizzo, M.'             2  ?                   
primary 'Pozzi, C.'             3  0000-0003-2574-3911 
primary 'Tagliazucchi, L.'      4  0000-0002-7244-7106 
primary 'Konchie Simo, C.U.'    5  ?                   
primary 'Saporito, G.'          6  ?                   
primary 'Landi, G.'             7  ?                   
primary 'Mangani, S.'           8  0000-0003-4824-7478 
primary 'Carbone, A.'           9  0000-0002-6767-2376 
primary 'Schenone, S.'          10 ?                   
primary 'Santarem, N.'          11 ?                   
primary 'Tavares, J.'           12 ?                   
primary 'Cordeiro-da-Silva, A.' 13 0000-0003-2392-6087 
primary 'Costi, M.P.'           14 0000-0002-0443-5402 
primary 'Tonelli, M.'           15 0000-0003-1518-2890 
# 
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 'Pteridine reductase'                                                   30816.982 4   ? ? ? ? 
2 non-polymer syn 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'             745.421   4   ? ? ? ? 
3 non-polymer syn '4,4,7,8-tetramethyl-10~{H}-[1,3,5]triazino[1,2-a]benzimidazol-2-amine' 243.308   3   ? ? ? ? 
4 non-polymer syn 'ACETATE ION'                                                           59.044    4   ? ? ? ? 
5 water       nat water                                                                   18.015    540 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSSGLVPRGSHMMEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVC
QADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFA
QRQKGTNPNCTSSNLSIVNLCDAMVDQP(CSX)MAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGE
EEKDKWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMMEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVC
QADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFA
QRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKD
KWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'             NDP   
3 '4,4,7,8-tetramethyl-10~{H}-[1,3,5]triazino[1,2-a]benzimidazol-2-amine' A1H0S 
4 'ACETATE ION'                                                           ACT   
5 water                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  MET n 
1 23  GLU n 
1 24  ALA n 
1 25  PRO n 
1 26  ALA n 
1 27  ALA n 
1 28  VAL n 
1 29  VAL n 
1 30  THR n 
1 31  GLY n 
1 32  ALA n 
1 33  ALA n 
1 34  LYS n 
1 35  ARG n 
1 36  ILE n 
1 37  GLY n 
1 38  ARG n 
1 39  ALA n 
1 40  ILE n 
1 41  ALA n 
1 42  VAL n 
1 43  LYS n 
1 44  LEU n 
1 45  HIS n 
1 46  GLN n 
1 47  THR n 
1 48  GLY n 
1 49  TYR n 
1 50  ARG n 
1 51  VAL n 
1 52  VAL n 
1 53  ILE n 
1 54  HIS n 
1 55  TYR n 
1 56  HIS n 
1 57  ASN n 
1 58  SER n 
1 59  ALA n 
1 60  GLU n 
1 61  ALA n 
1 62  ALA n 
1 63  VAL n 
1 64  SER n 
1 65  LEU n 
1 66  ALA n 
1 67  ASP n 
1 68  GLU n 
1 69  LEU n 
1 70  ASN n 
1 71  LYS n 
1 72  GLU n 
1 73  ARG n 
1 74  SER n 
1 75  ASN n 
1 76  THR n 
1 77  ALA n 
1 78  VAL n 
1 79  VAL n 
1 80  CYS n 
1 81  GLN n 
1 82  ALA n 
1 83  ASP n 
1 84  LEU n 
1 85  THR n 
1 86  ASN n 
1 87  SER n 
1 88  ASN n 
1 89  VAL n 
1 90  LEU n 
1 91  PRO n 
1 92  ALA n 
1 93  SER n 
1 94  CYS n 
1 95  GLU n 
1 96  GLU n 
1 97  ILE n 
1 98  ILE n 
1 99  ASN n 
1 100 SER n 
1 101 CYS n 
1 102 PHE n 
1 103 ARG n 
1 104 ALA n 
1 105 PHE n 
1 106 GLY n 
1 107 ARG n 
1 108 CYS n 
1 109 ASP n 
1 110 VAL n 
1 111 LEU n 
1 112 VAL n 
1 113 ASN n 
1 114 ASN n 
1 115 ALA n 
1 116 SER n 
1 117 ALA n 
1 118 PHE n 
1 119 TYR n 
1 120 PRO n 
1 121 THR n 
1 122 PRO n 
1 123 LEU n 
1 124 VAL n 
1 125 GLN n 
1 126 GLY n 
1 127 ASP n 
1 128 HIS n 
1 129 GLU n 
1 130 ASP n 
1 131 ASN n 
1 132 SER n 
1 133 ASN n 
1 134 GLY n 
1 135 LYS n 
1 136 THR n 
1 137 VAL n 
1 138 GLU n 
1 139 THR n 
1 140 GLN n 
1 141 VAL n 
1 142 ALA n 
1 143 GLU n 
1 144 LEU n 
1 145 ILE n 
1 146 GLY n 
1 147 THR n 
1 148 ASN n 
1 149 ALA n 
1 150 ILE n 
1 151 ALA n 
1 152 PRO n 
1 153 PHE n 
1 154 LEU n 
1 155 LEU n 
1 156 THR n 
1 157 MET n 
1 158 SER n 
1 159 PHE n 
1 160 ALA n 
1 161 GLN n 
1 162 ARG n 
1 163 GLN n 
1 164 LYS n 
1 165 GLY n 
1 166 THR n 
1 167 ASN n 
1 168 PRO n 
1 169 ASN n 
1 170 CYS n 
1 171 THR n 
1 172 SER n 
1 173 SER n 
1 174 ASN n 
1 175 LEU n 
1 176 SER n 
1 177 ILE n 
1 178 VAL n 
1 179 ASN n 
1 180 LEU n 
1 181 CYS n 
1 182 ASP n 
1 183 ALA n 
1 184 MET n 
1 185 VAL n 
1 186 ASP n 
1 187 GLN n 
1 188 PRO n 
1 189 CSX n 
1 190 MET n 
1 191 ALA n 
1 192 PHE n 
1 193 SER n 
1 194 LEU n 
1 195 TYR n 
1 196 ASN n 
1 197 MET n 
1 198 GLY n 
1 199 LYS n 
1 200 HIS n 
1 201 ALA n 
1 202 LEU n 
1 203 VAL n 
1 204 GLY n 
1 205 LEU n 
1 206 THR n 
1 207 GLN n 
1 208 SER n 
1 209 ALA n 
1 210 ALA n 
1 211 LEU n 
1 212 GLU n 
1 213 LEU n 
1 214 ALA n 
1 215 PRO n 
1 216 TYR n 
1 217 GLY n 
1 218 ILE n 
1 219 ARG n 
1 220 VAL n 
1 221 ASN n 
1 222 GLY n 
1 223 VAL n 
1 224 ALA n 
1 225 PRO n 
1 226 GLY n 
1 227 VAL n 
1 228 SER n 
1 229 LEU n 
1 230 LEU n 
1 231 PRO n 
1 232 VAL n 
1 233 ALA n 
1 234 MET n 
1 235 GLY n 
1 236 GLU n 
1 237 GLU n 
1 238 GLU n 
1 239 LYS n 
1 240 ASP n 
1 241 LYS n 
1 242 TRP n 
1 243 ARG n 
1 244 ARG n 
1 245 LYS n 
1 246 VAL n 
1 247 PRO n 
1 248 LEU n 
1 249 GLY n 
1 250 ARG n 
1 251 ARG n 
1 252 GLU n 
1 253 ALA n 
1 254 SER n 
1 255 ALA n 
1 256 GLU n 
1 257 GLN n 
1 258 ILE n 
1 259 ALA n 
1 260 ASP n 
1 261 ALA n 
1 262 VAL n 
1 263 ILE n 
1 264 PHE n 
1 265 LEU n 
1 266 VAL n 
1 267 SER n 
1 268 GLY n 
1 269 SER n 
1 270 ALA n 
1 271 GLN n 
1 272 TYR n 
1 273 ILE n 
1 274 THR n 
1 275 GLY n 
1 276 SER n 
1 277 ILE n 
1 278 ILE n 
1 279 LYS n 
1 280 VAL n 
1 281 ASP n 
1 282 GLY n 
1 283 GLY n 
1 284 LEU n 
1 285 SER n 
1 286 LEU n 
1 287 VAL n 
1 288 HIS n 
1 289 ALA 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                   289 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PTR1 
_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      'Trypanosoma brucei brucei' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5702 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_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 
A1H0S non-polymer         . '4,4,7,8-tetramethyl-10~{H}-[1,3,5]triazino[1,2-a]benzimidazol-2-amine' 'Mecillinam, bound form' 
'C13 H17 N5'        243.308 
ACT   non-polymer         . 'ACETATE ION'                                                           ?                        
'C2 H3 O2 -1'       59.044  
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 
CSX   'L-peptide linking' n 'S-OXY CYSTEINE'                                                        ?                        
'C3 H7 N O3 S'      137.158 
CYS   'L-peptide linking' y CYSTEINE                                                                ?                        
'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                               ?                        
'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                         ?                        
'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                 ?                        
'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                               ?                        
'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                   ?                        
'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                              ?                        
'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                 ?                        
'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                  ?                        
'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                              ?                        
'C5 H11 N O2 S'     149.211 
NDP   non-polymer         . 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'             ?                        
'C21 H30 N7 O17 P3' 745.421 
PHE   'L-peptide linking' y PHENYLALANINE                                                           ?                        
'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                 ?                        
'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                  ?                        
'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                               ?                        
'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                              ?                        
'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                                ?                        
'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                  ?                        
'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -20 ?   ?   ?   A . n 
A 1 2   GLY 2   -19 ?   ?   ?   A . n 
A 1 3   SER 3   -18 ?   ?   ?   A . n 
A 1 4   SER 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   HIS 9   -12 ?   ?   ?   A . n 
A 1 10  HIS 10  -11 ?   ?   ?   A . n 
A 1 11  SER 11  -10 ?   ?   ?   A . n 
A 1 12  SER 12  -9  ?   ?   ?   A . n 
A 1 13  GLY 13  -8  ?   ?   ?   A . n 
A 1 14  LEU 14  -7  ?   ?   ?   A . n 
A 1 15  VAL 15  -6  ?   ?   ?   A . n 
A 1 16  PRO 16  -5  ?   ?   ?   A . n 
A 1 17  ARG 17  -4  ?   ?   ?   A . n 
A 1 18  GLY 18  -3  ?   ?   ?   A . n 
A 1 19  SER 19  -2  ?   ?   ?   A . n 
A 1 20  HIS 20  -1  ?   ?   ?   A . n 
A 1 21  MET 21  0   ?   ?   ?   A . n 
A 1 22  MET 22  1   ?   ?   ?   A . n 
A 1 23  GLU 23  2   2   GLU GLU A . n 
A 1 24  ALA 24  3   3   ALA ALA A . n 
A 1 25  PRO 25  4   4   PRO PRO A . n 
A 1 26  ALA 26  5   5   ALA ALA A . n 
A 1 27  ALA 27  6   6   ALA ALA A . n 
A 1 28  VAL 28  7   7   VAL VAL A . n 
A 1 29  VAL 29  8   8   VAL VAL A . n 
A 1 30  THR 30  9   9   THR THR A . n 
A 1 31  GLY 31  10  10  GLY GLY A . n 
A 1 32  ALA 32  11  11  ALA ALA A . n 
A 1 33  ALA 33  12  12  ALA ALA A . n 
A 1 34  LYS 34  13  13  LYS LYS A . n 
A 1 35  ARG 35  14  14  ARG ARG A . n 
A 1 36  ILE 36  15  15  ILE ILE A . n 
A 1 37  GLY 37  16  16  GLY GLY A . n 
A 1 38  ARG 38  17  17  ARG ARG A . n 
A 1 39  ALA 39  18  18  ALA ALA A . n 
A 1 40  ILE 40  19  19  ILE ILE A . n 
A 1 41  ALA 41  20  20  ALA ALA A . n 
A 1 42  VAL 42  21  21  VAL VAL A . n 
A 1 43  LYS 43  22  22  LYS LYS A . n 
A 1 44  LEU 44  23  23  LEU LEU A . n 
A 1 45  HIS 45  24  24  HIS HIS A . n 
A 1 46  GLN 46  25  25  GLN GLN A . n 
A 1 47  THR 47  26  26  THR THR A . n 
A 1 48  GLY 48  27  27  GLY GLY A . n 
A 1 49  TYR 49  28  28  TYR TYR A . n 
A 1 50  ARG 50  29  29  ARG ARG A . n 
A 1 51  VAL 51  30  30  VAL VAL A . n 
A 1 52  VAL 52  31  31  VAL VAL A . n 
A 1 53  ILE 53  32  32  ILE ILE A . n 
A 1 54  HIS 54  33  33  HIS HIS A . n 
A 1 55  TYR 55  34  34  TYR TYR A . n 
A 1 56  HIS 56  35  35  HIS HIS A . n 
A 1 57  ASN 57  36  36  ASN ASN A . n 
A 1 58  SER 58  37  37  SER SER A . n 
A 1 59  ALA 59  38  38  ALA ALA A . n 
A 1 60  GLU 60  39  39  GLU GLU A . n 
A 1 61  ALA 61  40  40  ALA ALA A . n 
A 1 62  ALA 62  41  41  ALA ALA A . n 
A 1 63  VAL 63  42  42  VAL VAL A . n 
A 1 64  SER 64  43  43  SER SER A . n 
A 1 65  LEU 65  44  44  LEU LEU A . n 
A 1 66  ALA 66  45  45  ALA ALA A . n 
A 1 67  ASP 67  46  46  ASP ASP A . n 
A 1 68  GLU 68  47  47  GLU GLU A . n 
A 1 69  LEU 69  48  48  LEU LEU A . n 
A 1 70  ASN 70  49  49  ASN ASN A . n 
A 1 71  LYS 71  50  50  LYS LYS A . n 
A 1 72  GLU 72  51  51  GLU GLU A . n 
A 1 73  ARG 73  52  52  ARG ARG A . n 
A 1 74  SER 74  53  53  SER SER A . n 
A 1 75  ASN 75  54  54  ASN ASN A . n 
A 1 76  THR 76  55  55  THR THR A . n 
A 1 77  ALA 77  56  56  ALA ALA A . n 
A 1 78  VAL 78  57  57  VAL VAL A . n 
A 1 79  VAL 79  58  58  VAL VAL A . n 
A 1 80  CYS 80  59  59  CYS CYS A . n 
A 1 81  GLN 81  60  60  GLN GLN A . n 
A 1 82  ALA 82  61  61  ALA ALA A . n 
A 1 83  ASP 83  62  62  ASP ASP A . n 
A 1 84  LEU 84  63  63  LEU LEU A . n 
A 1 85  THR 85  64  64  THR THR A . n 
A 1 86  ASN 86  65  65  ASN ASN A . n 
A 1 87  SER 87  66  66  SER SER A . n 
A 1 88  ASN 88  67  67  ASN ASN A . n 
A 1 89  VAL 89  68  68  VAL VAL A . n 
A 1 90  LEU 90  69  69  LEU LEU A . n 
A 1 91  PRO 91  70  70  PRO PRO A . n 
A 1 92  ALA 92  71  71  ALA ALA A . n 
A 1 93  SER 93  72  72  SER SER A . n 
A 1 94  CYS 94  73  73  CYS CYS A . n 
A 1 95  GLU 95  74  74  GLU GLU A . n 
A 1 96  GLU 96  75  75  GLU GLU A . n 
A 1 97  ILE 97  76  76  ILE ILE A . n 
A 1 98  ILE 98  77  77  ILE ILE A . n 
A 1 99  ASN 99  78  78  ASN ASN A . n 
A 1 100 SER 100 79  79  SER SER A . n 
A 1 101 CYS 101 80  80  CYS CYS A . n 
A 1 102 PHE 102 81  81  PHE PHE A . n 
A 1 103 ARG 103 82  82  ARG ARG A . n 
A 1 104 ALA 104 83  83  ALA ALA A . n 
A 1 105 PHE 105 84  84  PHE PHE A . n 
A 1 106 GLY 106 85  85  GLY GLY A . n 
A 1 107 ARG 107 86  86  ARG ARG A . n 
A 1 108 CYS 108 87  87  CYS CYS A . n 
A 1 109 ASP 109 88  88  ASP ASP A . n 
A 1 110 VAL 110 89  89  VAL VAL A . n 
A 1 111 LEU 111 90  90  LEU LEU A . n 
A 1 112 VAL 112 91  91  VAL VAL A . n 
A 1 113 ASN 113 92  92  ASN ASN A . n 
A 1 114 ASN 114 93  93  ASN ASN A . n 
A 1 115 ALA 115 94  94  ALA ALA A . n 
A 1 116 SER 116 95  95  SER SER A . n 
A 1 117 ALA 117 96  96  ALA ALA A . n 
A 1 118 PHE 118 97  97  PHE PHE A . n 
A 1 119 TYR 119 98  98  TYR TYR A . n 
A 1 120 PRO 120 99  99  PRO PRO A . n 
A 1 121 THR 121 100 100 THR THR A . n 
A 1 122 PRO 122 101 101 PRO PRO A . n 
A 1 123 LEU 123 102 102 LEU LEU A . n 
A 1 124 VAL 124 103 103 VAL VAL A . n 
A 1 125 GLN 125 104 ?   ?   ?   A . n 
A 1 126 GLY 126 105 ?   ?   ?   A . n 
A 1 127 ASP 127 106 ?   ?   ?   A . n 
A 1 128 HIS 128 107 ?   ?   ?   A . n 
A 1 129 GLU 129 108 ?   ?   ?   A . n 
A 1 130 ASP 130 109 ?   ?   ?   A . n 
A 1 131 ASN 131 110 ?   ?   ?   A . n 
A 1 132 SER 132 111 ?   ?   ?   A . n 
A 1 133 ASN 133 112 ?   ?   ?   A . n 
A 1 134 GLY 134 113 113 GLY GLY A . n 
A 1 135 LYS 135 114 114 LYS LYS A . n 
A 1 136 THR 136 115 115 THR THR A . n 
A 1 137 VAL 137 116 116 VAL VAL A . n 
A 1 138 GLU 138 117 117 GLU GLU A . n 
A 1 139 THR 139 118 118 THR THR A . n 
A 1 140 GLN 140 119 119 GLN GLN A . n 
A 1 141 VAL 141 120 120 VAL VAL A . n 
A 1 142 ALA 142 121 121 ALA ALA A . n 
A 1 143 GLU 143 122 122 GLU GLU A . n 
A 1 144 LEU 144 123 123 LEU LEU A . n 
A 1 145 ILE 145 124 124 ILE ILE A . n 
A 1 146 GLY 146 125 125 GLY GLY A . n 
A 1 147 THR 147 126 126 THR THR A . n 
A 1 148 ASN 148 127 127 ASN ASN A . n 
A 1 149 ALA 149 128 128 ALA ALA A . n 
A 1 150 ILE 150 129 129 ILE ILE A . n 
A 1 151 ALA 151 130 130 ALA ALA A . n 
A 1 152 PRO 152 131 131 PRO PRO A . n 
A 1 153 PHE 153 132 132 PHE PHE A . n 
A 1 154 LEU 154 133 133 LEU LEU A . n 
A 1 155 LEU 155 134 134 LEU LEU A . n 
A 1 156 THR 156 135 135 THR THR A . n 
A 1 157 MET 157 136 136 MET MET A . n 
A 1 158 SER 158 137 137 SER SER A . n 
A 1 159 PHE 159 138 138 PHE PHE A . n 
A 1 160 ALA 160 139 139 ALA ALA A . n 
A 1 161 GLN 161 140 140 GLN GLN A . n 
A 1 162 ARG 162 141 141 ARG ARG A . n 
A 1 163 GLN 163 142 142 GLN GLN A . n 
A 1 164 LYS 164 143 ?   ?   ?   A . n 
A 1 165 GLY 165 144 ?   ?   ?   A . n 
A 1 166 THR 166 145 ?   ?   ?   A . n 
A 1 167 ASN 167 146 ?   ?   ?   A . n 
A 1 168 PRO 168 147 ?   ?   ?   A . n 
A 1 169 ASN 169 148 ?   ?   ?   A . n 
A 1 170 CYS 170 149 ?   ?   ?   A . n 
A 1 171 THR 171 150 ?   ?   ?   A . n 
A 1 172 SER 172 151 ?   ?   ?   A . n 
A 1 173 SER 173 152 152 SER SER A . n 
A 1 174 ASN 174 153 153 ASN ASN A . n 
A 1 175 LEU 175 154 154 LEU LEU A . n 
A 1 176 SER 176 155 155 SER SER A . n 
A 1 177 ILE 177 156 156 ILE ILE A . n 
A 1 178 VAL 178 157 157 VAL VAL A . n 
A 1 179 ASN 179 158 158 ASN ASN A . n 
A 1 180 LEU 180 159 159 LEU LEU A . n 
A 1 181 CYS 181 160 160 CYS CYS A . n 
A 1 182 ASP 182 161 161 ASP ASP A . n 
A 1 183 ALA 183 162 162 ALA ALA A . n 
A 1 184 MET 184 163 163 MET MET A . n 
A 1 185 VAL 185 164 164 VAL VAL A . n 
A 1 186 ASP 186 165 165 ASP ASP A . n 
A 1 187 GLN 187 166 166 GLN GLN A . n 
A 1 188 PRO 188 167 167 PRO PRO A . n 
A 1 189 CSX 189 168 168 CSX CSX A . n 
A 1 190 MET 190 169 169 MET MET A . n 
A 1 191 ALA 191 170 170 ALA ALA A . n 
A 1 192 PHE 192 171 171 PHE PHE A . n 
A 1 193 SER 193 172 172 SER SER A . n 
A 1 194 LEU 194 173 173 LEU LEU A . n 
A 1 195 TYR 195 174 174 TYR TYR A . n 
A 1 196 ASN 196 175 175 ASN ASN A . n 
A 1 197 MET 197 176 176 MET MET A . n 
A 1 198 GLY 198 177 177 GLY GLY A . n 
A 1 199 LYS 199 178 178 LYS LYS A . n 
A 1 200 HIS 200 179 179 HIS HIS A . n 
A 1 201 ALA 201 180 180 ALA ALA A . n 
A 1 202 LEU 202 181 181 LEU LEU A . n 
A 1 203 VAL 203 182 182 VAL VAL A . n 
A 1 204 GLY 204 183 183 GLY GLY A . n 
A 1 205 LEU 205 184 184 LEU LEU A . n 
A 1 206 THR 206 185 185 THR THR A . n 
A 1 207 GLN 207 186 186 GLN GLN A . n 
A 1 208 SER 208 187 187 SER SER A . n 
A 1 209 ALA 209 188 188 ALA ALA A . n 
A 1 210 ALA 210 189 189 ALA ALA A . n 
A 1 211 LEU 211 190 190 LEU LEU A . n 
A 1 212 GLU 212 191 191 GLU GLU A . n 
A 1 213 LEU 213 192 192 LEU LEU A . n 
A 1 214 ALA 214 193 193 ALA ALA A . n 
A 1 215 PRO 215 194 194 PRO PRO A . n 
A 1 216 TYR 216 195 195 TYR TYR A . n 
A 1 217 GLY 217 196 196 GLY GLY A . n 
A 1 218 ILE 218 197 197 ILE ILE A . n 
A 1 219 ARG 219 198 198 ARG ARG A . n 
A 1 220 VAL 220 199 199 VAL VAL A . n 
A 1 221 ASN 221 200 200 ASN ASN A . n 
A 1 222 GLY 222 201 201 GLY GLY A . n 
A 1 223 VAL 223 202 202 VAL VAL A . n 
A 1 224 ALA 224 203 203 ALA ALA A . n 
A 1 225 PRO 225 204 204 PRO PRO A . n 
A 1 226 GLY 226 205 205 GLY GLY A . n 
A 1 227 VAL 227 206 206 VAL VAL A . n 
A 1 228 SER 228 207 207 SER SER A . n 
A 1 229 LEU 229 208 208 LEU LEU A . n 
A 1 230 LEU 230 209 209 LEU LEU A . n 
A 1 231 PRO 231 210 210 PRO PRO A . n 
A 1 232 VAL 232 211 211 VAL VAL A . n 
A 1 233 ALA 233 212 212 ALA ALA A . n 
A 1 234 MET 234 213 213 MET MET A . n 
A 1 235 GLY 235 214 214 GLY GLY A . n 
A 1 236 GLU 236 215 215 GLU GLU A . n 
A 1 237 GLU 237 216 216 GLU GLU A . n 
A 1 238 GLU 238 217 217 GLU GLU A . n 
A 1 239 LYS 239 218 218 LYS LYS A . n 
A 1 240 ASP 240 219 219 ASP ASP A . n 
A 1 241 LYS 241 220 220 LYS LYS A . n 
A 1 242 TRP 242 221 221 TRP TRP A . n 
A 1 243 ARG 243 222 222 ARG ARG A . n 
A 1 244 ARG 244 223 223 ARG ARG A . n 
A 1 245 LYS 245 224 224 LYS LYS A . n 
A 1 246 VAL 246 225 225 VAL VAL A . n 
A 1 247 PRO 247 226 226 PRO PRO A . n 
A 1 248 LEU 248 227 227 LEU LEU A . n 
A 1 249 GLY 249 228 228 GLY GLY A . n 
A 1 250 ARG 250 229 229 ARG ARG A . n 
A 1 251 ARG 251 230 230 ARG ARG A . n 
A 1 252 GLU 252 231 231 GLU GLU A . n 
A 1 253 ALA 253 232 232 ALA ALA A . n 
A 1 254 SER 254 233 233 SER SER A . n 
A 1 255 ALA 255 234 234 ALA ALA A . n 
A 1 256 GLU 256 235 235 GLU GLU A . n 
A 1 257 GLN 257 236 236 GLN GLN A . n 
A 1 258 ILE 258 237 237 ILE ILE A . n 
A 1 259 ALA 259 238 238 ALA ALA A . n 
A 1 260 ASP 260 239 239 ASP ASP A . n 
A 1 261 ALA 261 240 240 ALA ALA A . n 
A 1 262 VAL 262 241 241 VAL VAL A . n 
A 1 263 ILE 263 242 242 ILE ILE A . n 
A 1 264 PHE 264 243 243 PHE PHE A . n 
A 1 265 LEU 265 244 244 LEU LEU A . n 
A 1 266 VAL 266 245 245 VAL VAL A . n 
A 1 267 SER 267 246 246 SER SER A . n 
A 1 268 GLY 268 247 247 GLY GLY A . n 
A 1 269 SER 269 248 248 SER SER A . n 
A 1 270 ALA 270 249 249 ALA ALA A . n 
A 1 271 GLN 271 250 250 GLN GLN A . n 
A 1 272 TYR 272 251 251 TYR TYR A . n 
A 1 273 ILE 273 252 252 ILE ILE A . n 
A 1 274 THR 274 253 253 THR THR A . n 
A 1 275 GLY 275 254 254 GLY GLY A . n 
A 1 276 SER 276 255 255 SER SER A . n 
A 1 277 ILE 277 256 256 ILE ILE A . n 
A 1 278 ILE 278 257 257 ILE ILE A . n 
A 1 279 LYS 279 258 258 LYS LYS A . n 
A 1 280 VAL 280 259 259 VAL VAL A . n 
A 1 281 ASP 281 260 260 ASP ASP A . n 
A 1 282 GLY 282 261 261 GLY GLY A . n 
A 1 283 GLY 283 262 262 GLY GLY A . n 
A 1 284 LEU 284 263 263 LEU LEU A . n 
A 1 285 SER 285 264 264 SER SER A . n 
A 1 286 LEU 286 265 265 LEU LEU A . n 
A 1 287 VAL 287 266 266 VAL VAL A . n 
A 1 288 HIS 288 267 267 HIS HIS A . n 
A 1 289 ALA 289 268 268 ALA ALA A . n 
B 1 1   MET 1   -20 ?   ?   ?   B . n 
B 1 2   GLY 2   -19 ?   ?   ?   B . n 
B 1 3   SER 3   -18 ?   ?   ?   B . n 
B 1 4   SER 4   -17 ?   ?   ?   B . n 
B 1 5   HIS 5   -16 ?   ?   ?   B . n 
B 1 6   HIS 6   -15 ?   ?   ?   B . n 
B 1 7   HIS 7   -14 ?   ?   ?   B . n 
B 1 8   HIS 8   -13 ?   ?   ?   B . n 
B 1 9   HIS 9   -12 ?   ?   ?   B . n 
B 1 10  HIS 10  -11 ?   ?   ?   B . n 
B 1 11  SER 11  -10 ?   ?   ?   B . n 
B 1 12  SER 12  -9  ?   ?   ?   B . n 
B 1 13  GLY 13  -8  ?   ?   ?   B . n 
B 1 14  LEU 14  -7  ?   ?   ?   B . n 
B 1 15  VAL 15  -6  ?   ?   ?   B . n 
B 1 16  PRO 16  -5  ?   ?   ?   B . n 
B 1 17  ARG 17  -4  ?   ?   ?   B . n 
B 1 18  GLY 18  -3  ?   ?   ?   B . n 
B 1 19  SER 19  -2  ?   ?   ?   B . n 
B 1 20  HIS 20  -1  ?   ?   ?   B . n 
B 1 21  MET 21  0   ?   ?   ?   B . n 
B 1 22  MET 22  1   ?   ?   ?   B . n 
B 1 23  GLU 23  2   2   GLU GLU B . n 
B 1 24  ALA 24  3   3   ALA ALA B . n 
B 1 25  PRO 25  4   4   PRO PRO B . n 
B 1 26  ALA 26  5   5   ALA ALA B . n 
B 1 27  ALA 27  6   6   ALA ALA B . n 
B 1 28  VAL 28  7   7   VAL VAL B . n 
B 1 29  VAL 29  8   8   VAL VAL B . n 
B 1 30  THR 30  9   9   THR THR B . n 
B 1 31  GLY 31  10  10  GLY GLY B . n 
B 1 32  ALA 32  11  11  ALA ALA B . n 
B 1 33  ALA 33  12  12  ALA ALA B . n 
B 1 34  LYS 34  13  13  LYS LYS B . n 
B 1 35  ARG 35  14  14  ARG ARG B . n 
B 1 36  ILE 36  15  15  ILE ILE B . n 
B 1 37  GLY 37  16  16  GLY GLY B . n 
B 1 38  ARG 38  17  17  ARG ARG B . n 
B 1 39  ALA 39  18  18  ALA ALA B . n 
B 1 40  ILE 40  19  19  ILE ILE B . n 
B 1 41  ALA 41  20  20  ALA ALA B . n 
B 1 42  VAL 42  21  21  VAL VAL B . n 
B 1 43  LYS 43  22  22  LYS LYS B . n 
B 1 44  LEU 44  23  23  LEU LEU B . n 
B 1 45  HIS 45  24  24  HIS HIS B . n 
B 1 46  GLN 46  25  25  GLN GLN B . n 
B 1 47  THR 47  26  26  THR THR B . n 
B 1 48  GLY 48  27  27  GLY GLY B . n 
B 1 49  TYR 49  28  28  TYR TYR B . n 
B 1 50  ARG 50  29  29  ARG ARG B . n 
B 1 51  VAL 51  30  30  VAL VAL B . n 
B 1 52  VAL 52  31  31  VAL VAL B . n 
B 1 53  ILE 53  32  32  ILE ILE B . n 
B 1 54  HIS 54  33  33  HIS HIS B . n 
B 1 55  TYR 55  34  34  TYR TYR B . n 
B 1 56  HIS 56  35  35  HIS HIS B . n 
B 1 57  ASN 57  36  36  ASN ASN B . n 
B 1 58  SER 58  37  37  SER SER B . n 
B 1 59  ALA 59  38  38  ALA ALA B . n 
B 1 60  GLU 60  39  39  GLU GLU B . n 
B 1 61  ALA 61  40  40  ALA ALA B . n 
B 1 62  ALA 62  41  41  ALA ALA B . n 
B 1 63  VAL 63  42  42  VAL VAL B . n 
B 1 64  SER 64  43  43  SER SER B . n 
B 1 65  LEU 65  44  44  LEU LEU B . n 
B 1 66  ALA 66  45  45  ALA ALA B . n 
B 1 67  ASP 67  46  46  ASP ASP B . n 
B 1 68  GLU 68  47  47  GLU GLU B . n 
B 1 69  LEU 69  48  48  LEU LEU B . n 
B 1 70  ASN 70  49  49  ASN ASN B . n 
B 1 71  LYS 71  50  50  LYS LYS B . n 
B 1 72  GLU 72  51  51  GLU GLU B . n 
B 1 73  ARG 73  52  52  ARG ARG B . n 
B 1 74  SER 74  53  53  SER SER B . n 
B 1 75  ASN 75  54  54  ASN ASN B . n 
B 1 76  THR 76  55  55  THR THR B . n 
B 1 77  ALA 77  56  56  ALA ALA B . n 
B 1 78  VAL 78  57  57  VAL VAL B . n 
B 1 79  VAL 79  58  58  VAL VAL B . n 
B 1 80  CYS 80  59  59  CYS CYS B . n 
B 1 81  GLN 81  60  60  GLN GLN B . n 
B 1 82  ALA 82  61  61  ALA ALA B . n 
B 1 83  ASP 83  62  62  ASP ASP B . n 
B 1 84  LEU 84  63  63  LEU LEU B . n 
B 1 85  THR 85  64  64  THR THR B . n 
B 1 86  ASN 86  65  65  ASN ASN B . n 
B 1 87  SER 87  66  66  SER SER B . n 
B 1 88  ASN 88  67  67  ASN ASN B . n 
B 1 89  VAL 89  68  68  VAL VAL B . n 
B 1 90  LEU 90  69  69  LEU LEU B . n 
B 1 91  PRO 91  70  70  PRO PRO B . n 
B 1 92  ALA 92  71  71  ALA ALA B . n 
B 1 93  SER 93  72  72  SER SER B . n 
B 1 94  CYS 94  73  73  CYS CYS B . n 
B 1 95  GLU 95  74  74  GLU GLU B . n 
B 1 96  GLU 96  75  75  GLU GLU B . n 
B 1 97  ILE 97  76  76  ILE ILE B . n 
B 1 98  ILE 98  77  77  ILE ILE B . n 
B 1 99  ASN 99  78  78  ASN ASN B . n 
B 1 100 SER 100 79  79  SER SER B . n 
B 1 101 CYS 101 80  80  CYS CYS B . n 
B 1 102 PHE 102 81  81  PHE PHE B . n 
B 1 103 ARG 103 82  82  ARG ARG B . n 
B 1 104 ALA 104 83  83  ALA ALA B . n 
B 1 105 PHE 105 84  84  PHE PHE B . n 
B 1 106 GLY 106 85  85  GLY GLY B . n 
B 1 107 ARG 107 86  86  ARG ARG B . n 
B 1 108 CYS 108 87  87  CYS CYS B . n 
B 1 109 ASP 109 88  88  ASP ASP B . n 
B 1 110 VAL 110 89  89  VAL VAL B . n 
B 1 111 LEU 111 90  90  LEU LEU B . n 
B 1 112 VAL 112 91  91  VAL VAL B . n 
B 1 113 ASN 113 92  92  ASN ASN B . n 
B 1 114 ASN 114 93  93  ASN ASN B . n 
B 1 115 ALA 115 94  94  ALA ALA B . n 
B 1 116 SER 116 95  95  SER SER B . n 
B 1 117 ALA 117 96  96  ALA ALA B . n 
B 1 118 PHE 118 97  97  PHE PHE B . n 
B 1 119 TYR 119 98  98  TYR TYR B . n 
B 1 120 PRO 120 99  99  PRO PRO B . n 
B 1 121 THR 121 100 100 THR THR B . n 
B 1 122 PRO 122 101 101 PRO PRO B . n 
B 1 123 LEU 123 102 102 LEU LEU B . n 
B 1 124 VAL 124 103 103 VAL VAL B . n 
B 1 125 GLN 125 104 ?   ?   ?   B . n 
B 1 126 GLY 126 105 ?   ?   ?   B . n 
B 1 127 ASP 127 106 ?   ?   ?   B . n 
B 1 128 HIS 128 107 ?   ?   ?   B . n 
B 1 129 GLU 129 108 ?   ?   ?   B . n 
B 1 130 ASP 130 109 ?   ?   ?   B . n 
B 1 131 ASN 131 110 ?   ?   ?   B . n 
B 1 132 SER 132 111 ?   ?   ?   B . n 
B 1 133 ASN 133 112 ?   ?   ?   B . n 
B 1 134 GLY 134 113 113 GLY GLY B . n 
B 1 135 LYS 135 114 114 LYS LYS B . n 
B 1 136 THR 136 115 115 THR THR B . n 
B 1 137 VAL 137 116 116 VAL VAL B . n 
B 1 138 GLU 138 117 117 GLU GLU B . n 
B 1 139 THR 139 118 118 THR THR B . n 
B 1 140 GLN 140 119 119 GLN GLN B . n 
B 1 141 VAL 141 120 120 VAL VAL B . n 
B 1 142 ALA 142 121 121 ALA ALA B . n 
B 1 143 GLU 143 122 122 GLU GLU B . n 
B 1 144 LEU 144 123 123 LEU LEU B . n 
B 1 145 ILE 145 124 124 ILE ILE B . n 
B 1 146 GLY 146 125 125 GLY GLY B . n 
B 1 147 THR 147 126 126 THR THR B . n 
B 1 148 ASN 148 127 127 ASN ASN B . n 
B 1 149 ALA 149 128 128 ALA ALA B . n 
B 1 150 ILE 150 129 129 ILE ILE B . n 
B 1 151 ALA 151 130 130 ALA ALA B . n 
B 1 152 PRO 152 131 131 PRO PRO B . n 
B 1 153 PHE 153 132 132 PHE PHE B . n 
B 1 154 LEU 154 133 133 LEU LEU B . n 
B 1 155 LEU 155 134 134 LEU LEU B . n 
B 1 156 THR 156 135 135 THR THR B . n 
B 1 157 MET 157 136 136 MET MET B . n 
B 1 158 SER 158 137 137 SER SER B . n 
B 1 159 PHE 159 138 138 PHE PHE B . n 
B 1 160 ALA 160 139 139 ALA ALA B . n 
B 1 161 GLN 161 140 140 GLN GLN B . n 
B 1 162 ARG 162 141 141 ARG ARG B . n 
B 1 163 GLN 163 142 142 GLN GLN B . n 
B 1 164 LYS 164 143 143 LYS LYS B . n 
B 1 165 GLY 165 144 ?   ?   ?   B . n 
B 1 166 THR 166 145 ?   ?   ?   B . n 
B 1 167 ASN 167 146 ?   ?   ?   B . n 
B 1 168 PRO 168 147 ?   ?   ?   B . n 
B 1 169 ASN 169 148 ?   ?   ?   B . n 
B 1 170 CYS 170 149 ?   ?   ?   B . n 
B 1 171 THR 171 150 ?   ?   ?   B . n 
B 1 172 SER 172 151 ?   ?   ?   B . n 
B 1 173 SER 173 152 152 SER SER B . n 
B 1 174 ASN 174 153 153 ASN ASN B . n 
B 1 175 LEU 175 154 154 LEU LEU B . n 
B 1 176 SER 176 155 155 SER SER B . n 
B 1 177 ILE 177 156 156 ILE ILE B . n 
B 1 178 VAL 178 157 157 VAL VAL B . n 
B 1 179 ASN 179 158 158 ASN ASN B . n 
B 1 180 LEU 180 159 159 LEU LEU B . n 
B 1 181 CYS 181 160 160 CYS CYS B . n 
B 1 182 ASP 182 161 161 ASP ASP B . n 
B 1 183 ALA 183 162 162 ALA ALA B . n 
B 1 184 MET 184 163 163 MET MET B . n 
B 1 185 VAL 185 164 164 VAL VAL B . n 
B 1 186 ASP 186 165 165 ASP ASP B . n 
B 1 187 GLN 187 166 166 GLN GLN B . n 
B 1 188 PRO 188 167 167 PRO PRO B . n 
B 1 189 CSX 189 168 168 CSX CSX B . n 
B 1 190 MET 190 169 169 MET MET B . n 
B 1 191 ALA 191 170 170 ALA ALA B . n 
B 1 192 PHE 192 171 171 PHE PHE B . n 
B 1 193 SER 193 172 172 SER SER B . n 
B 1 194 LEU 194 173 173 LEU LEU B . n 
B 1 195 TYR 195 174 174 TYR TYR B . n 
B 1 196 ASN 196 175 175 ASN ASN B . n 
B 1 197 MET 197 176 176 MET MET B . n 
B 1 198 GLY 198 177 177 GLY GLY B . n 
B 1 199 LYS 199 178 178 LYS LYS B . n 
B 1 200 HIS 200 179 179 HIS HIS B . n 
B 1 201 ALA 201 180 180 ALA ALA B . n 
B 1 202 LEU 202 181 181 LEU LEU B . n 
B 1 203 VAL 203 182 182 VAL VAL B . n 
B 1 204 GLY 204 183 183 GLY GLY B . n 
B 1 205 LEU 205 184 184 LEU LEU B . n 
B 1 206 THR 206 185 185 THR THR B . n 
B 1 207 GLN 207 186 186 GLN GLN B . n 
B 1 208 SER 208 187 187 SER SER B . n 
B 1 209 ALA 209 188 188 ALA ALA B . n 
B 1 210 ALA 210 189 189 ALA ALA B . n 
B 1 211 LEU 211 190 190 LEU LEU B . n 
B 1 212 GLU 212 191 191 GLU GLU B . n 
B 1 213 LEU 213 192 192 LEU LEU B . n 
B 1 214 ALA 214 193 193 ALA ALA B . n 
B 1 215 PRO 215 194 194 PRO PRO B . n 
B 1 216 TYR 216 195 195 TYR TYR B . n 
B 1 217 GLY 217 196 196 GLY GLY B . n 
B 1 218 ILE 218 197 197 ILE ILE B . n 
B 1 219 ARG 219 198 198 ARG ARG B . n 
B 1 220 VAL 220 199 199 VAL VAL B . n 
B 1 221 ASN 221 200 200 ASN ASN B . n 
B 1 222 GLY 222 201 201 GLY GLY B . n 
B 1 223 VAL 223 202 202 VAL VAL B . n 
B 1 224 ALA 224 203 203 ALA ALA B . n 
B 1 225 PRO 225 204 204 PRO PRO B . n 
B 1 226 GLY 226 205 205 GLY GLY B . n 
B 1 227 VAL 227 206 206 VAL VAL B . n 
B 1 228 SER 228 207 207 SER SER B . n 
B 1 229 LEU 229 208 208 LEU LEU B . n 
B 1 230 LEU 230 209 209 LEU LEU B . n 
B 1 231 PRO 231 210 210 PRO PRO B . n 
B 1 232 VAL 232 211 211 VAL VAL B . n 
B 1 233 ALA 233 212 212 ALA ALA B . n 
B 1 234 MET 234 213 213 MET MET B . n 
B 1 235 GLY 235 214 214 GLY GLY B . n 
B 1 236 GLU 236 215 215 GLU GLU B . n 
B 1 237 GLU 237 216 216 GLU GLU B . n 
B 1 238 GLU 238 217 217 GLU GLU B . n 
B 1 239 LYS 239 218 218 LYS LYS B . n 
B 1 240 ASP 240 219 219 ASP ASP B . n 
B 1 241 LYS 241 220 220 LYS LYS B . n 
B 1 242 TRP 242 221 221 TRP TRP B . n 
B 1 243 ARG 243 222 222 ARG ARG B . n 
B 1 244 ARG 244 223 223 ARG ARG B . n 
B 1 245 LYS 245 224 224 LYS LYS B . n 
B 1 246 VAL 246 225 225 VAL VAL B . n 
B 1 247 PRO 247 226 226 PRO PRO B . n 
B 1 248 LEU 248 227 227 LEU LEU B . n 
B 1 249 GLY 249 228 228 GLY GLY B . n 
B 1 250 ARG 250 229 229 ARG ARG B . n 
B 1 251 ARG 251 230 230 ARG ARG B . n 
B 1 252 GLU 252 231 231 GLU GLU B . n 
B 1 253 ALA 253 232 232 ALA ALA B . n 
B 1 254 SER 254 233 233 SER SER B . n 
B 1 255 ALA 255 234 234 ALA ALA B . n 
B 1 256 GLU 256 235 235 GLU GLU B . n 
B 1 257 GLN 257 236 236 GLN GLN B . n 
B 1 258 ILE 258 237 237 ILE ILE B . n 
B 1 259 ALA 259 238 238 ALA ALA B . n 
B 1 260 ASP 260 239 239 ASP ASP B . n 
B 1 261 ALA 261 240 240 ALA ALA B . n 
B 1 262 VAL 262 241 241 VAL VAL B . n 
B 1 263 ILE 263 242 242 ILE ILE B . n 
B 1 264 PHE 264 243 243 PHE PHE B . n 
B 1 265 LEU 265 244 244 LEU LEU B . n 
B 1 266 VAL 266 245 245 VAL VAL B . n 
B 1 267 SER 267 246 246 SER SER B . n 
B 1 268 GLY 268 247 247 GLY GLY B . n 
B 1 269 SER 269 248 248 SER SER B . n 
B 1 270 ALA 270 249 249 ALA ALA B . n 
B 1 271 GLN 271 250 250 GLN GLN B . n 
B 1 272 TYR 272 251 251 TYR TYR B . n 
B 1 273 ILE 273 252 252 ILE ILE B . n 
B 1 274 THR 274 253 253 THR THR B . n 
B 1 275 GLY 275 254 254 GLY GLY B . n 
B 1 276 SER 276 255 255 SER SER B . n 
B 1 277 ILE 277 256 256 ILE ILE B . n 
B 1 278 ILE 278 257 257 ILE ILE B . n 
B 1 279 LYS 279 258 258 LYS LYS B . n 
B 1 280 VAL 280 259 259 VAL VAL B . n 
B 1 281 ASP 281 260 260 ASP ASP B . n 
B 1 282 GLY 282 261 261 GLY GLY B . n 
B 1 283 GLY 283 262 262 GLY GLY B . n 
B 1 284 LEU 284 263 263 LEU LEU B . n 
B 1 285 SER 285 264 264 SER SER B . n 
B 1 286 LEU 286 265 265 LEU LEU B . n 
B 1 287 VAL 287 266 266 VAL VAL B . n 
B 1 288 HIS 288 267 267 HIS HIS B . n 
B 1 289 ALA 289 268 268 ALA ALA B . n 
C 1 1   MET 1   -20 ?   ?   ?   C . n 
C 1 2   GLY 2   -19 ?   ?   ?   C . n 
C 1 3   SER 3   -18 ?   ?   ?   C . n 
C 1 4   SER 4   -17 ?   ?   ?   C . n 
C 1 5   HIS 5   -16 ?   ?   ?   C . n 
C 1 6   HIS 6   -15 ?   ?   ?   C . n 
C 1 7   HIS 7   -14 ?   ?   ?   C . n 
C 1 8   HIS 8   -13 ?   ?   ?   C . n 
C 1 9   HIS 9   -12 ?   ?   ?   C . n 
C 1 10  HIS 10  -11 ?   ?   ?   C . n 
C 1 11  SER 11  -10 ?   ?   ?   C . n 
C 1 12  SER 12  -9  ?   ?   ?   C . n 
C 1 13  GLY 13  -8  ?   ?   ?   C . n 
C 1 14  LEU 14  -7  ?   ?   ?   C . n 
C 1 15  VAL 15  -6  ?   ?   ?   C . n 
C 1 16  PRO 16  -5  ?   ?   ?   C . n 
C 1 17  ARG 17  -4  ?   ?   ?   C . n 
C 1 18  GLY 18  -3  ?   ?   ?   C . n 
C 1 19  SER 19  -2  ?   ?   ?   C . n 
C 1 20  HIS 20  -1  ?   ?   ?   C . n 
C 1 21  MET 21  0   ?   ?   ?   C . n 
C 1 22  MET 22  1   ?   ?   ?   C . n 
C 1 23  GLU 23  2   2   GLU GLU C . n 
C 1 24  ALA 24  3   3   ALA ALA C . n 
C 1 25  PRO 25  4   4   PRO PRO C . n 
C 1 26  ALA 26  5   5   ALA ALA C . n 
C 1 27  ALA 27  6   6   ALA ALA C . n 
C 1 28  VAL 28  7   7   VAL VAL C . n 
C 1 29  VAL 29  8   8   VAL VAL C . n 
C 1 30  THR 30  9   9   THR THR C . n 
C 1 31  GLY 31  10  10  GLY GLY C . n 
C 1 32  ALA 32  11  11  ALA ALA C . n 
C 1 33  ALA 33  12  12  ALA ALA C . n 
C 1 34  LYS 34  13  13  LYS LYS C . n 
C 1 35  ARG 35  14  14  ARG ARG C . n 
C 1 36  ILE 36  15  15  ILE ILE C . n 
C 1 37  GLY 37  16  16  GLY GLY C . n 
C 1 38  ARG 38  17  17  ARG ARG C . n 
C 1 39  ALA 39  18  18  ALA ALA C . n 
C 1 40  ILE 40  19  19  ILE ILE C . n 
C 1 41  ALA 41  20  20  ALA ALA C . n 
C 1 42  VAL 42  21  21  VAL VAL C . n 
C 1 43  LYS 43  22  22  LYS LYS C . n 
C 1 44  LEU 44  23  23  LEU LEU C . n 
C 1 45  HIS 45  24  24  HIS HIS C . n 
C 1 46  GLN 46  25  25  GLN GLN C . n 
C 1 47  THR 47  26  26  THR THR C . n 
C 1 48  GLY 48  27  27  GLY GLY C . n 
C 1 49  TYR 49  28  28  TYR TYR C . n 
C 1 50  ARG 50  29  29  ARG ARG C . n 
C 1 51  VAL 51  30  30  VAL VAL C . n 
C 1 52  VAL 52  31  31  VAL VAL C . n 
C 1 53  ILE 53  32  32  ILE ILE C . n 
C 1 54  HIS 54  33  33  HIS HIS C . n 
C 1 55  TYR 55  34  34  TYR TYR C . n 
C 1 56  HIS 56  35  35  HIS HIS C . n 
C 1 57  ASN 57  36  36  ASN ASN C . n 
C 1 58  SER 58  37  37  SER SER C . n 
C 1 59  ALA 59  38  38  ALA ALA C . n 
C 1 60  GLU 60  39  39  GLU GLU C . n 
C 1 61  ALA 61  40  40  ALA ALA C . n 
C 1 62  ALA 62  41  41  ALA ALA C . n 
C 1 63  VAL 63  42  42  VAL VAL C . n 
C 1 64  SER 64  43  43  SER SER C . n 
C 1 65  LEU 65  44  44  LEU LEU C . n 
C 1 66  ALA 66  45  45  ALA ALA C . n 
C 1 67  ASP 67  46  46  ASP ASP C . n 
C 1 68  GLU 68  47  47  GLU GLU C . n 
C 1 69  LEU 69  48  48  LEU LEU C . n 
C 1 70  ASN 70  49  49  ASN ASN C . n 
C 1 71  LYS 71  50  50  LYS LYS C . n 
C 1 72  GLU 72  51  51  GLU GLU C . n 
C 1 73  ARG 73  52  52  ARG ARG C . n 
C 1 74  SER 74  53  53  SER SER C . n 
C 1 75  ASN 75  54  54  ASN ASN C . n 
C 1 76  THR 76  55  55  THR THR C . n 
C 1 77  ALA 77  56  56  ALA ALA C . n 
C 1 78  VAL 78  57  57  VAL VAL C . n 
C 1 79  VAL 79  58  58  VAL VAL C . n 
C 1 80  CYS 80  59  59  CYS CYS C . n 
C 1 81  GLN 81  60  60  GLN GLN C . n 
C 1 82  ALA 82  61  61  ALA ALA C . n 
C 1 83  ASP 83  62  62  ASP ASP C . n 
C 1 84  LEU 84  63  63  LEU LEU C . n 
C 1 85  THR 85  64  64  THR THR C . n 
C 1 86  ASN 86  65  65  ASN ASN C . n 
C 1 87  SER 87  66  66  SER SER C . n 
C 1 88  ASN 88  67  67  ASN ASN C . n 
C 1 89  VAL 89  68  68  VAL VAL C . n 
C 1 90  LEU 90  69  69  LEU LEU C . n 
C 1 91  PRO 91  70  70  PRO PRO C . n 
C 1 92  ALA 92  71  71  ALA ALA C . n 
C 1 93  SER 93  72  72  SER SER C . n 
C 1 94  CYS 94  73  73  CYS CYS C . n 
C 1 95  GLU 95  74  74  GLU GLU C . n 
C 1 96  GLU 96  75  75  GLU GLU C . n 
C 1 97  ILE 97  76  76  ILE ILE C . n 
C 1 98  ILE 98  77  77  ILE ILE C . n 
C 1 99  ASN 99  78  78  ASN ASN C . n 
C 1 100 SER 100 79  79  SER SER C . n 
C 1 101 CYS 101 80  80  CYS CYS C . n 
C 1 102 PHE 102 81  81  PHE PHE C . n 
C 1 103 ARG 103 82  82  ARG ARG C . n 
C 1 104 ALA 104 83  83  ALA ALA C . n 
C 1 105 PHE 105 84  84  PHE PHE C . n 
C 1 106 GLY 106 85  85  GLY GLY C . n 
C 1 107 ARG 107 86  86  ARG ARG C . n 
C 1 108 CYS 108 87  87  CYS CYS C . n 
C 1 109 ASP 109 88  88  ASP ASP C . n 
C 1 110 VAL 110 89  89  VAL VAL C . n 
C 1 111 LEU 111 90  90  LEU LEU C . n 
C 1 112 VAL 112 91  91  VAL VAL C . n 
C 1 113 ASN 113 92  92  ASN ASN C . n 
C 1 114 ASN 114 93  93  ASN ASN C . n 
C 1 115 ALA 115 94  94  ALA ALA C . n 
C 1 116 SER 116 95  95  SER SER C . n 
C 1 117 ALA 117 96  96  ALA ALA C . n 
C 1 118 PHE 118 97  97  PHE PHE C . n 
C 1 119 TYR 119 98  98  TYR TYR C . n 
C 1 120 PRO 120 99  99  PRO PRO C . n 
C 1 121 THR 121 100 100 THR THR C . n 
C 1 122 PRO 122 101 101 PRO PRO C . n 
C 1 123 LEU 123 102 102 LEU LEU C . n 
C 1 124 VAL 124 103 103 VAL VAL C . n 
C 1 125 GLN 125 104 104 GLN GLN C . n 
C 1 126 GLY 126 105 ?   ?   ?   C . n 
C 1 127 ASP 127 106 ?   ?   ?   C . n 
C 1 128 HIS 128 107 ?   ?   ?   C . n 
C 1 129 GLU 129 108 ?   ?   ?   C . n 
C 1 130 ASP 130 109 ?   ?   ?   C . n 
C 1 131 ASN 131 110 ?   ?   ?   C . n 
C 1 132 SER 132 111 ?   ?   ?   C . n 
C 1 133 ASN 133 112 ?   ?   ?   C . n 
C 1 134 GLY 134 113 ?   ?   ?   C . n 
C 1 135 LYS 135 114 114 LYS LYS C . n 
C 1 136 THR 136 115 115 THR THR C . n 
C 1 137 VAL 137 116 116 VAL VAL C . n 
C 1 138 GLU 138 117 117 GLU GLU C . n 
C 1 139 THR 139 118 118 THR THR C . n 
C 1 140 GLN 140 119 119 GLN GLN C . n 
C 1 141 VAL 141 120 120 VAL VAL C . n 
C 1 142 ALA 142 121 121 ALA ALA C . n 
C 1 143 GLU 143 122 122 GLU GLU C . n 
C 1 144 LEU 144 123 123 LEU LEU C . n 
C 1 145 ILE 145 124 124 ILE ILE C . n 
C 1 146 GLY 146 125 125 GLY GLY C . n 
C 1 147 THR 147 126 126 THR THR C . n 
C 1 148 ASN 148 127 127 ASN ASN C . n 
C 1 149 ALA 149 128 128 ALA ALA C . n 
C 1 150 ILE 150 129 129 ILE ILE C . n 
C 1 151 ALA 151 130 130 ALA ALA C . n 
C 1 152 PRO 152 131 131 PRO PRO C . n 
C 1 153 PHE 153 132 132 PHE PHE C . n 
C 1 154 LEU 154 133 133 LEU LEU C . n 
C 1 155 LEU 155 134 134 LEU LEU C . n 
C 1 156 THR 156 135 135 THR THR C . n 
C 1 157 MET 157 136 136 MET MET C . n 
C 1 158 SER 158 137 137 SER SER C . n 
C 1 159 PHE 159 138 138 PHE PHE C . n 
C 1 160 ALA 160 139 139 ALA ALA C . n 
C 1 161 GLN 161 140 140 GLN GLN C . n 
C 1 162 ARG 162 141 141 ARG ARG C . n 
C 1 163 GLN 163 142 142 GLN GLN C . n 
C 1 164 LYS 164 143 ?   ?   ?   C . n 
C 1 165 GLY 165 144 ?   ?   ?   C . n 
C 1 166 THR 166 145 ?   ?   ?   C . n 
C 1 167 ASN 167 146 ?   ?   ?   C . n 
C 1 168 PRO 168 147 ?   ?   ?   C . n 
C 1 169 ASN 169 148 ?   ?   ?   C . n 
C 1 170 CYS 170 149 ?   ?   ?   C . n 
C 1 171 THR 171 150 ?   ?   ?   C . n 
C 1 172 SER 172 151 ?   ?   ?   C . n 
C 1 173 SER 173 152 152 SER SER C . n 
C 1 174 ASN 174 153 153 ASN ASN C . n 
C 1 175 LEU 175 154 154 LEU LEU C . n 
C 1 176 SER 176 155 155 SER SER C . n 
C 1 177 ILE 177 156 156 ILE ILE C . n 
C 1 178 VAL 178 157 157 VAL VAL C . n 
C 1 179 ASN 179 158 158 ASN ASN C . n 
C 1 180 LEU 180 159 159 LEU LEU C . n 
C 1 181 CYS 181 160 160 CYS CYS C . n 
C 1 182 ASP 182 161 161 ASP ASP C . n 
C 1 183 ALA 183 162 162 ALA ALA C . n 
C 1 184 MET 184 163 163 MET MET C . n 
C 1 185 VAL 185 164 164 VAL VAL C . n 
C 1 186 ASP 186 165 165 ASP ASP C . n 
C 1 187 GLN 187 166 166 GLN GLN C . n 
C 1 188 PRO 188 167 167 PRO PRO C . n 
C 1 189 CSX 189 168 168 CSX CSX C . n 
C 1 190 MET 190 169 169 MET MET C . n 
C 1 191 ALA 191 170 170 ALA ALA C . n 
C 1 192 PHE 192 171 171 PHE PHE C . n 
C 1 193 SER 193 172 172 SER SER C . n 
C 1 194 LEU 194 173 173 LEU LEU C . n 
C 1 195 TYR 195 174 174 TYR TYR C . n 
C 1 196 ASN 196 175 175 ASN ASN C . n 
C 1 197 MET 197 176 176 MET MET C . n 
C 1 198 GLY 198 177 177 GLY GLY C . n 
C 1 199 LYS 199 178 178 LYS LYS C . n 
C 1 200 HIS 200 179 179 HIS HIS C . n 
C 1 201 ALA 201 180 180 ALA ALA C . n 
C 1 202 LEU 202 181 181 LEU LEU C . n 
C 1 203 VAL 203 182 182 VAL VAL C . n 
C 1 204 GLY 204 183 183 GLY GLY C . n 
C 1 205 LEU 205 184 184 LEU LEU C . n 
C 1 206 THR 206 185 185 THR THR C . n 
C 1 207 GLN 207 186 186 GLN GLN C . n 
C 1 208 SER 208 187 187 SER SER C . n 
C 1 209 ALA 209 188 188 ALA ALA C . n 
C 1 210 ALA 210 189 189 ALA ALA C . n 
C 1 211 LEU 211 190 190 LEU LEU C . n 
C 1 212 GLU 212 191 191 GLU GLU C . n 
C 1 213 LEU 213 192 192 LEU LEU C . n 
C 1 214 ALA 214 193 193 ALA ALA C . n 
C 1 215 PRO 215 194 194 PRO PRO C . n 
C 1 216 TYR 216 195 195 TYR TYR C . n 
C 1 217 GLY 217 196 196 GLY GLY C . n 
C 1 218 ILE 218 197 197 ILE ILE C . n 
C 1 219 ARG 219 198 198 ARG ARG C . n 
C 1 220 VAL 220 199 199 VAL VAL C . n 
C 1 221 ASN 221 200 200 ASN ASN C . n 
C 1 222 GLY 222 201 201 GLY GLY C . n 
C 1 223 VAL 223 202 202 VAL VAL C . n 
C 1 224 ALA 224 203 203 ALA ALA C . n 
C 1 225 PRO 225 204 204 PRO PRO C . n 
C 1 226 GLY 226 205 205 GLY GLY C . n 
C 1 227 VAL 227 206 206 VAL VAL C . n 
C 1 228 SER 228 207 207 SER SER C . n 
C 1 229 LEU 229 208 208 LEU LEU C . n 
C 1 230 LEU 230 209 209 LEU LEU C . n 
C 1 231 PRO 231 210 210 PRO PRO C . n 
C 1 232 VAL 232 211 211 VAL VAL C . n 
C 1 233 ALA 233 212 212 ALA ALA C . n 
C 1 234 MET 234 213 213 MET MET C . n 
C 1 235 GLY 235 214 214 GLY GLY C . n 
C 1 236 GLU 236 215 215 GLU GLU C . n 
C 1 237 GLU 237 216 216 GLU GLU C . n 
C 1 238 GLU 238 217 217 GLU GLU C . n 
C 1 239 LYS 239 218 218 LYS LYS C . n 
C 1 240 ASP 240 219 219 ASP ASP C . n 
C 1 241 LYS 241 220 220 LYS LYS C . n 
C 1 242 TRP 242 221 221 TRP TRP C . n 
C 1 243 ARG 243 222 222 ARG ARG C . n 
C 1 244 ARG 244 223 223 ARG ARG C . n 
C 1 245 LYS 245 224 224 LYS LYS C . n 
C 1 246 VAL 246 225 225 VAL VAL C . n 
C 1 247 PRO 247 226 226 PRO PRO C . n 
C 1 248 LEU 248 227 227 LEU LEU C . n 
C 1 249 GLY 249 228 228 GLY GLY C . n 
C 1 250 ARG 250 229 229 ARG ARG C . n 
C 1 251 ARG 251 230 230 ARG ARG C . n 
C 1 252 GLU 252 231 231 GLU GLU C . n 
C 1 253 ALA 253 232 232 ALA ALA C . n 
C 1 254 SER 254 233 233 SER SER C . n 
C 1 255 ALA 255 234 234 ALA ALA C . n 
C 1 256 GLU 256 235 235 GLU GLU C . n 
C 1 257 GLN 257 236 236 GLN GLN C . n 
C 1 258 ILE 258 237 237 ILE ILE C . n 
C 1 259 ALA 259 238 238 ALA ALA C . n 
C 1 260 ASP 260 239 239 ASP ASP C . n 
C 1 261 ALA 261 240 240 ALA ALA C . n 
C 1 262 VAL 262 241 241 VAL VAL C . n 
C 1 263 ILE 263 242 242 ILE ILE C . n 
C 1 264 PHE 264 243 243 PHE PHE C . n 
C 1 265 LEU 265 244 244 LEU LEU C . n 
C 1 266 VAL 266 245 245 VAL VAL C . n 
C 1 267 SER 267 246 246 SER SER C . n 
C 1 268 GLY 268 247 247 GLY GLY C . n 
C 1 269 SER 269 248 248 SER SER C . n 
C 1 270 ALA 270 249 249 ALA ALA C . n 
C 1 271 GLN 271 250 250 GLN GLN C . n 
C 1 272 TYR 272 251 251 TYR TYR C . n 
C 1 273 ILE 273 252 252 ILE ILE C . n 
C 1 274 THR 274 253 253 THR THR C . n 
C 1 275 GLY 275 254 254 GLY GLY C . n 
C 1 276 SER 276 255 255 SER SER C . n 
C 1 277 ILE 277 256 256 ILE ILE C . n 
C 1 278 ILE 278 257 257 ILE ILE C . n 
C 1 279 LYS 279 258 258 LYS LYS C . n 
C 1 280 VAL 280 259 259 VAL VAL C . n 
C 1 281 ASP 281 260 260 ASP ASP C . n 
C 1 282 GLY 282 261 261 GLY GLY C . n 
C 1 283 GLY 283 262 262 GLY GLY C . n 
C 1 284 LEU 284 263 263 LEU LEU C . n 
C 1 285 SER 285 264 264 SER SER C . n 
C 1 286 LEU 286 265 265 LEU LEU C . n 
C 1 287 VAL 287 266 266 VAL VAL C . n 
C 1 288 HIS 288 267 267 HIS HIS C . n 
C 1 289 ALA 289 268 268 ALA ALA C . n 
D 1 1   MET 1   -20 ?   ?   ?   D . n 
D 1 2   GLY 2   -19 ?   ?   ?   D . n 
D 1 3   SER 3   -18 ?   ?   ?   D . n 
D 1 4   SER 4   -17 ?   ?   ?   D . n 
D 1 5   HIS 5   -16 ?   ?   ?   D . n 
D 1 6   HIS 6   -15 ?   ?   ?   D . n 
D 1 7   HIS 7   -14 ?   ?   ?   D . n 
D 1 8   HIS 8   -13 ?   ?   ?   D . n 
D 1 9   HIS 9   -12 ?   ?   ?   D . n 
D 1 10  HIS 10  -11 ?   ?   ?   D . n 
D 1 11  SER 11  -10 ?   ?   ?   D . n 
D 1 12  SER 12  -9  ?   ?   ?   D . n 
D 1 13  GLY 13  -8  ?   ?   ?   D . n 
D 1 14  LEU 14  -7  ?   ?   ?   D . n 
D 1 15  VAL 15  -6  ?   ?   ?   D . n 
D 1 16  PRO 16  -5  ?   ?   ?   D . n 
D 1 17  ARG 17  -4  ?   ?   ?   D . n 
D 1 18  GLY 18  -3  ?   ?   ?   D . n 
D 1 19  SER 19  -2  ?   ?   ?   D . n 
D 1 20  HIS 20  -1  ?   ?   ?   D . n 
D 1 21  MET 21  0   ?   ?   ?   D . n 
D 1 22  MET 22  1   ?   ?   ?   D . n 
D 1 23  GLU 23  2   2   GLU GLU D . n 
D 1 24  ALA 24  3   3   ALA ALA D . n 
D 1 25  PRO 25  4   4   PRO PRO D . n 
D 1 26  ALA 26  5   5   ALA ALA D . n 
D 1 27  ALA 27  6   6   ALA ALA D . n 
D 1 28  VAL 28  7   7   VAL VAL D . n 
D 1 29  VAL 29  8   8   VAL VAL D . n 
D 1 30  THR 30  9   9   THR THR D . n 
D 1 31  GLY 31  10  10  GLY GLY D . n 
D 1 32  ALA 32  11  11  ALA ALA D . n 
D 1 33  ALA 33  12  12  ALA ALA D . n 
D 1 34  LYS 34  13  13  LYS LYS D . n 
D 1 35  ARG 35  14  14  ARG ARG D . n 
D 1 36  ILE 36  15  15  ILE ILE D . n 
D 1 37  GLY 37  16  16  GLY GLY D . n 
D 1 38  ARG 38  17  17  ARG ARG D . n 
D 1 39  ALA 39  18  18  ALA ALA D . n 
D 1 40  ILE 40  19  19  ILE ILE D . n 
D 1 41  ALA 41  20  20  ALA ALA D . n 
D 1 42  VAL 42  21  21  VAL VAL D . n 
D 1 43  LYS 43  22  22  LYS LYS D . n 
D 1 44  LEU 44  23  23  LEU LEU D . n 
D 1 45  HIS 45  24  24  HIS HIS D . n 
D 1 46  GLN 46  25  25  GLN GLN D . n 
D 1 47  THR 47  26  26  THR THR D . n 
D 1 48  GLY 48  27  27  GLY GLY D . n 
D 1 49  TYR 49  28  28  TYR TYR D . n 
D 1 50  ARG 50  29  29  ARG ARG D . n 
D 1 51  VAL 51  30  30  VAL VAL D . n 
D 1 52  VAL 52  31  31  VAL VAL D . n 
D 1 53  ILE 53  32  32  ILE ILE D . n 
D 1 54  HIS 54  33  33  HIS HIS D . n 
D 1 55  TYR 55  34  34  TYR TYR D . n 
D 1 56  HIS 56  35  35  HIS HIS D . n 
D 1 57  ASN 57  36  36  ASN ASN D . n 
D 1 58  SER 58  37  37  SER SER D . n 
D 1 59  ALA 59  38  38  ALA ALA D . n 
D 1 60  GLU 60  39  39  GLU GLU D . n 
D 1 61  ALA 61  40  40  ALA ALA D . n 
D 1 62  ALA 62  41  41  ALA ALA D . n 
D 1 63  VAL 63  42  42  VAL VAL D . n 
D 1 64  SER 64  43  43  SER SER D . n 
D 1 65  LEU 65  44  44  LEU LEU D . n 
D 1 66  ALA 66  45  45  ALA ALA D . n 
D 1 67  ASP 67  46  46  ASP ASP D . n 
D 1 68  GLU 68  47  47  GLU GLU D . n 
D 1 69  LEU 69  48  48  LEU LEU D . n 
D 1 70  ASN 70  49  49  ASN ASN D . n 
D 1 71  LYS 71  50  50  LYS LYS D . n 
D 1 72  GLU 72  51  51  GLU GLU D . n 
D 1 73  ARG 73  52  52  ARG ARG D . n 
D 1 74  SER 74  53  53  SER SER D . n 
D 1 75  ASN 75  54  54  ASN ASN D . n 
D 1 76  THR 76  55  55  THR THR D . n 
D 1 77  ALA 77  56  56  ALA ALA D . n 
D 1 78  VAL 78  57  57  VAL VAL D . n 
D 1 79  VAL 79  58  58  VAL VAL D . n 
D 1 80  CYS 80  59  59  CYS CYS D . n 
D 1 81  GLN 81  60  60  GLN GLN D . n 
D 1 82  ALA 82  61  61  ALA ALA D . n 
D 1 83  ASP 83  62  62  ASP ASP D . n 
D 1 84  LEU 84  63  63  LEU LEU D . n 
D 1 85  THR 85  64  64  THR THR D . n 
D 1 86  ASN 86  65  65  ASN ASN D . n 
D 1 87  SER 87  66  66  SER SER D . n 
D 1 88  ASN 88  67  67  ASN ASN D . n 
D 1 89  VAL 89  68  68  VAL VAL D . n 
D 1 90  LEU 90  69  69  LEU LEU D . n 
D 1 91  PRO 91  70  70  PRO PRO D . n 
D 1 92  ALA 92  71  71  ALA ALA D . n 
D 1 93  SER 93  72  72  SER SER D . n 
D 1 94  CYS 94  73  73  CYS CYS D . n 
D 1 95  GLU 95  74  74  GLU GLU D . n 
D 1 96  GLU 96  75  75  GLU GLU D . n 
D 1 97  ILE 97  76  76  ILE ILE D . n 
D 1 98  ILE 98  77  77  ILE ILE D . n 
D 1 99  ASN 99  78  78  ASN ASN D . n 
D 1 100 SER 100 79  79  SER SER D . n 
D 1 101 CYS 101 80  80  CYS CYS D . n 
D 1 102 PHE 102 81  81  PHE PHE D . n 
D 1 103 ARG 103 82  82  ARG ARG D . n 
D 1 104 ALA 104 83  83  ALA ALA D . n 
D 1 105 PHE 105 84  84  PHE PHE D . n 
D 1 106 GLY 106 85  85  GLY GLY D . n 
D 1 107 ARG 107 86  86  ARG ARG D . n 
D 1 108 CYS 108 87  87  CYS CYS D . n 
D 1 109 ASP 109 88  88  ASP ASP D . n 
D 1 110 VAL 110 89  89  VAL VAL D . n 
D 1 111 LEU 111 90  90  LEU LEU D . n 
D 1 112 VAL 112 91  91  VAL VAL D . n 
D 1 113 ASN 113 92  92  ASN ASN D . n 
D 1 114 ASN 114 93  93  ASN ASN D . n 
D 1 115 ALA 115 94  94  ALA ALA D . n 
D 1 116 SER 116 95  95  SER SER D . n 
D 1 117 ALA 117 96  96  ALA ALA D . n 
D 1 118 PHE 118 97  97  PHE PHE D . n 
D 1 119 TYR 119 98  98  TYR TYR D . n 
D 1 120 PRO 120 99  99  PRO PRO D . n 
D 1 121 THR 121 100 100 THR THR D . n 
D 1 122 PRO 122 101 101 PRO PRO D . n 
D 1 123 LEU 123 102 102 LEU LEU D . n 
D 1 124 VAL 124 103 103 VAL VAL D . n 
D 1 125 GLN 125 104 ?   ?   ?   D . n 
D 1 126 GLY 126 105 ?   ?   ?   D . n 
D 1 127 ASP 127 106 ?   ?   ?   D . n 
D 1 128 HIS 128 107 ?   ?   ?   D . n 
D 1 129 GLU 129 108 ?   ?   ?   D . n 
D 1 130 ASP 130 109 ?   ?   ?   D . n 
D 1 131 ASN 131 110 ?   ?   ?   D . n 
D 1 132 SER 132 111 ?   ?   ?   D . n 
D 1 133 ASN 133 112 ?   ?   ?   D . n 
D 1 134 GLY 134 113 113 GLY GLY D . n 
D 1 135 LYS 135 114 114 LYS LYS D . n 
D 1 136 THR 136 115 115 THR THR D . n 
D 1 137 VAL 137 116 116 VAL VAL D . n 
D 1 138 GLU 138 117 117 GLU GLU D . n 
D 1 139 THR 139 118 118 THR THR D . n 
D 1 140 GLN 140 119 119 GLN GLN D . n 
D 1 141 VAL 141 120 120 VAL VAL D . n 
D 1 142 ALA 142 121 121 ALA ALA D . n 
D 1 143 GLU 143 122 122 GLU GLU D . n 
D 1 144 LEU 144 123 123 LEU LEU D . n 
D 1 145 ILE 145 124 124 ILE ILE D . n 
D 1 146 GLY 146 125 125 GLY GLY D . n 
D 1 147 THR 147 126 126 THR THR D . n 
D 1 148 ASN 148 127 127 ASN ASN D . n 
D 1 149 ALA 149 128 128 ALA ALA D . n 
D 1 150 ILE 150 129 129 ILE ILE D . n 
D 1 151 ALA 151 130 130 ALA ALA D . n 
D 1 152 PRO 152 131 131 PRO PRO D . n 
D 1 153 PHE 153 132 132 PHE PHE D . n 
D 1 154 LEU 154 133 133 LEU LEU D . n 
D 1 155 LEU 155 134 134 LEU LEU D . n 
D 1 156 THR 156 135 135 THR THR D . n 
D 1 157 MET 157 136 136 MET MET D . n 
D 1 158 SER 158 137 137 SER SER D . n 
D 1 159 PHE 159 138 138 PHE PHE D . n 
D 1 160 ALA 160 139 139 ALA ALA D . n 
D 1 161 GLN 161 140 140 GLN GLN D . n 
D 1 162 ARG 162 141 141 ARG ARG D . n 
D 1 163 GLN 163 142 142 GLN GLN D . n 
D 1 164 LYS 164 143 ?   ?   ?   D . n 
D 1 165 GLY 165 144 ?   ?   ?   D . n 
D 1 166 THR 166 145 ?   ?   ?   D . n 
D 1 167 ASN 167 146 ?   ?   ?   D . n 
D 1 168 PRO 168 147 ?   ?   ?   D . n 
D 1 169 ASN 169 148 ?   ?   ?   D . n 
D 1 170 CYS 170 149 ?   ?   ?   D . n 
D 1 171 THR 171 150 ?   ?   ?   D . n 
D 1 172 SER 172 151 ?   ?   ?   D . n 
D 1 173 SER 173 152 152 SER SER D . n 
D 1 174 ASN 174 153 153 ASN ASN D . n 
D 1 175 LEU 175 154 154 LEU LEU D . n 
D 1 176 SER 176 155 155 SER SER D . n 
D 1 177 ILE 177 156 156 ILE ILE D . n 
D 1 178 VAL 178 157 157 VAL VAL D . n 
D 1 179 ASN 179 158 158 ASN ASN D . n 
D 1 180 LEU 180 159 159 LEU LEU D . n 
D 1 181 CYS 181 160 160 CYS CYS D . n 
D 1 182 ASP 182 161 161 ASP ASP D . n 
D 1 183 ALA 183 162 162 ALA ALA D . n 
D 1 184 MET 184 163 163 MET MET D . n 
D 1 185 VAL 185 164 164 VAL VAL D . n 
D 1 186 ASP 186 165 165 ASP ASP D . n 
D 1 187 GLN 187 166 166 GLN GLN D . n 
D 1 188 PRO 188 167 167 PRO PRO D . n 
D 1 189 CSX 189 168 168 CSX CSX D . n 
D 1 190 MET 190 169 169 MET MET D . n 
D 1 191 ALA 191 170 170 ALA ALA D . n 
D 1 192 PHE 192 171 171 PHE PHE D . n 
D 1 193 SER 193 172 172 SER SER D . n 
D 1 194 LEU 194 173 173 LEU LEU D . n 
D 1 195 TYR 195 174 174 TYR TYR D . n 
D 1 196 ASN 196 175 175 ASN ASN D . n 
D 1 197 MET 197 176 176 MET MET D . n 
D 1 198 GLY 198 177 177 GLY GLY D . n 
D 1 199 LYS 199 178 178 LYS LYS D . n 
D 1 200 HIS 200 179 179 HIS HIS D . n 
D 1 201 ALA 201 180 180 ALA ALA D . n 
D 1 202 LEU 202 181 181 LEU LEU D . n 
D 1 203 VAL 203 182 182 VAL VAL D . n 
D 1 204 GLY 204 183 183 GLY GLY D . n 
D 1 205 LEU 205 184 184 LEU LEU D . n 
D 1 206 THR 206 185 185 THR THR D . n 
D 1 207 GLN 207 186 186 GLN GLN D . n 
D 1 208 SER 208 187 187 SER SER D . n 
D 1 209 ALA 209 188 188 ALA ALA D . n 
D 1 210 ALA 210 189 189 ALA ALA D . n 
D 1 211 LEU 211 190 190 LEU LEU D . n 
D 1 212 GLU 212 191 191 GLU GLU D . n 
D 1 213 LEU 213 192 192 LEU LEU D . n 
D 1 214 ALA 214 193 193 ALA ALA D . n 
D 1 215 PRO 215 194 194 PRO PRO D . n 
D 1 216 TYR 216 195 195 TYR TYR D . n 
D 1 217 GLY 217 196 196 GLY GLY D . n 
D 1 218 ILE 218 197 197 ILE ILE D . n 
D 1 219 ARG 219 198 198 ARG ARG D . n 
D 1 220 VAL 220 199 199 VAL VAL D . n 
D 1 221 ASN 221 200 200 ASN ASN D . n 
D 1 222 GLY 222 201 201 GLY GLY D . n 
D 1 223 VAL 223 202 202 VAL VAL D . n 
D 1 224 ALA 224 203 203 ALA ALA D . n 
D 1 225 PRO 225 204 204 PRO PRO D . n 
D 1 226 GLY 226 205 205 GLY GLY D . n 
D 1 227 VAL 227 206 206 VAL VAL D . n 
D 1 228 SER 228 207 207 SER SER D . n 
D 1 229 LEU 229 208 208 LEU LEU D . n 
D 1 230 LEU 230 209 209 LEU LEU D . n 
D 1 231 PRO 231 210 210 PRO PRO D . n 
D 1 232 VAL 232 211 211 VAL VAL D . n 
D 1 233 ALA 233 212 212 ALA ALA D . n 
D 1 234 MET 234 213 213 MET MET D . n 
D 1 235 GLY 235 214 214 GLY GLY D . n 
D 1 236 GLU 236 215 215 GLU GLU D . n 
D 1 237 GLU 237 216 216 GLU GLU D . n 
D 1 238 GLU 238 217 217 GLU GLU D . n 
D 1 239 LYS 239 218 218 LYS LYS D . n 
D 1 240 ASP 240 219 219 ASP ASP D . n 
D 1 241 LYS 241 220 220 LYS LYS D . n 
D 1 242 TRP 242 221 221 TRP TRP D . n 
D 1 243 ARG 243 222 222 ARG ARG D . n 
D 1 244 ARG 244 223 223 ARG ARG D . n 
D 1 245 LYS 245 224 224 LYS LYS D . n 
D 1 246 VAL 246 225 225 VAL VAL D . n 
D 1 247 PRO 247 226 226 PRO PRO D . n 
D 1 248 LEU 248 227 227 LEU LEU D . n 
D 1 249 GLY 249 228 228 GLY GLY D . n 
D 1 250 ARG 250 229 229 ARG ARG D . n 
D 1 251 ARG 251 230 230 ARG ARG D . n 
D 1 252 GLU 252 231 231 GLU GLU D . n 
D 1 253 ALA 253 232 232 ALA ALA D . n 
D 1 254 SER 254 233 233 SER SER D . n 
D 1 255 ALA 255 234 234 ALA ALA D . n 
D 1 256 GLU 256 235 235 GLU GLU D . n 
D 1 257 GLN 257 236 236 GLN GLN D . n 
D 1 258 ILE 258 237 237 ILE ILE D . n 
D 1 259 ALA 259 238 238 ALA ALA D . n 
D 1 260 ASP 260 239 239 ASP ASP D . n 
D 1 261 ALA 261 240 240 ALA ALA D . n 
D 1 262 VAL 262 241 241 VAL VAL D . n 
D 1 263 ILE 263 242 242 ILE ILE D . n 
D 1 264 PHE 264 243 243 PHE PHE D . n 
D 1 265 LEU 265 244 244 LEU LEU D . n 
D 1 266 VAL 266 245 245 VAL VAL D . n 
D 1 267 SER 267 246 246 SER SER D . n 
D 1 268 GLY 268 247 247 GLY GLY D . n 
D 1 269 SER 269 248 248 SER SER D . n 
D 1 270 ALA 270 249 249 ALA ALA D . n 
D 1 271 GLN 271 250 250 GLN GLN D . n 
D 1 272 TYR 272 251 251 TYR TYR D . n 
D 1 273 ILE 273 252 252 ILE ILE D . n 
D 1 274 THR 274 253 253 THR THR D . n 
D 1 275 GLY 275 254 254 GLY GLY D . n 
D 1 276 SER 276 255 255 SER SER D . n 
D 1 277 ILE 277 256 256 ILE ILE D . n 
D 1 278 ILE 278 257 257 ILE ILE D . n 
D 1 279 LYS 279 258 258 LYS LYS D . n 
D 1 280 VAL 280 259 259 VAL VAL D . n 
D 1 281 ASP 281 260 260 ASP ASP D . n 
D 1 282 GLY 282 261 261 GLY GLY D . n 
D 1 283 GLY 283 262 262 GLY GLY D . n 
D 1 284 LEU 284 263 263 LEU LEU D . n 
D 1 285 SER 285 264 264 SER SER D . n 
D 1 286 LEU 286 265 265 LEU LEU D . n 
D 1 287 VAL 287 266 266 VAL VAL D . n 
D 1 288 HIS 288 267 267 HIS HIS D . n 
D 1 289 ALA 289 268 268 ALA ALA D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H0S 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H0S 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 NDP   1   301 269 NDP   NDP A . 
F 3 A1H0S 1   302 270 A1H0S DH4 A . 
G 4 ACT   1   303 271 ACT   ACT A . 
H 4 ACT   1   304 272 ACT   ACT A . 
I 2 NDP   1   301 269 NDP   NDP B . 
J 4 ACT   1   302 271 ACT   ACT B . 
K 2 NDP   1   301 269 NDP   NDP C . 
L 3 A1H0S 1   302 270 A1H0S DH4 C . 
M 4 ACT   1   303 271 ACT   ACT C . 
N 2 NDP   1   301 269 NDP   NDP D . 
O 3 A1H0S 1   302 270 A1H0S DH4 D . 
P 5 HOH   1   401 242 HOH   HOH A . 
P 5 HOH   2   402 570 HOH   HOH A . 
P 5 HOH   3   403 355 HOH   HOH A . 
P 5 HOH   4   404 583 HOH   HOH A . 
P 5 HOH   5   405 554 HOH   HOH A . 
P 5 HOH   6   406 190 HOH   HOH A . 
P 5 HOH   7   407 470 HOH   HOH A . 
P 5 HOH   8   408 114 HOH   HOH A . 
P 5 HOH   9   409 266 HOH   HOH A . 
P 5 HOH   10  410 44  HOH   HOH A . 
P 5 HOH   11  411 53  HOH   HOH A . 
P 5 HOH   12  412 307 HOH   HOH A . 
P 5 HOH   13  413 545 HOH   HOH A . 
P 5 HOH   14  414 8   HOH   HOH A . 
P 5 HOH   15  415 261 HOH   HOH A . 
P 5 HOH   16  416 314 HOH   HOH A . 
P 5 HOH   17  417 373 HOH   HOH A . 
P 5 HOH   18  418 181 HOH   HOH A . 
P 5 HOH   19  419 341 HOH   HOH A . 
P 5 HOH   20  420 281 HOH   HOH A . 
P 5 HOH   21  421 217 HOH   HOH A . 
P 5 HOH   22  422 511 HOH   HOH A . 
P 5 HOH   23  423 2   HOH   HOH A . 
P 5 HOH   24  424 240 HOH   HOH A . 
P 5 HOH   25  425 54  HOH   HOH A . 
P 5 HOH   26  426 188 HOH   HOH A . 
P 5 HOH   27  427 496 HOH   HOH A . 
P 5 HOH   28  428 210 HOH   HOH A . 
P 5 HOH   29  429 397 HOH   HOH A . 
P 5 HOH   30  430 11  HOH   HOH A . 
P 5 HOH   31  431 376 HOH   HOH A . 
P 5 HOH   32  432 129 HOH   HOH A . 
P 5 HOH   33  433 149 HOH   HOH A . 
P 5 HOH   34  434 134 HOH   HOH A . 
P 5 HOH   35  435 305 HOH   HOH A . 
P 5 HOH   36  436 222 HOH   HOH A . 
P 5 HOH   37  437 582 HOH   HOH A . 
P 5 HOH   38  438 99  HOH   HOH A . 
P 5 HOH   39  439 103 HOH   HOH A . 
P 5 HOH   40  440 270 HOH   HOH A . 
P 5 HOH   41  441 51  HOH   HOH A . 
P 5 HOH   42  442 426 HOH   HOH A . 
P 5 HOH   43  443 296 HOH   HOH A . 
P 5 HOH   44  444 446 HOH   HOH A . 
P 5 HOH   45  445 144 HOH   HOH A . 
P 5 HOH   46  446 302 HOH   HOH A . 
P 5 HOH   47  447 80  HOH   HOH A . 
P 5 HOH   48  448 141 HOH   HOH A . 
P 5 HOH   49  449 425 HOH   HOH A . 
P 5 HOH   50  450 292 HOH   HOH A . 
P 5 HOH   51  451 76  HOH   HOH A . 
P 5 HOH   52  452 344 HOH   HOH A . 
P 5 HOH   53  453 429 HOH   HOH A . 
P 5 HOH   54  454 476 HOH   HOH A . 
P 5 HOH   55  455 16  HOH   HOH A . 
P 5 HOH   56  456 212 HOH   HOH A . 
P 5 HOH   57  457 458 HOH   HOH A . 
P 5 HOH   58  458 572 HOH   HOH A . 
P 5 HOH   59  459 173 HOH   HOH A . 
P 5 HOH   60  460 571 HOH   HOH A . 
P 5 HOH   61  461 127 HOH   HOH A . 
P 5 HOH   62  462 320 HOH   HOH A . 
P 5 HOH   63  463 390 HOH   HOH A . 
P 5 HOH   64  464 361 HOH   HOH A . 
P 5 HOH   65  465 487 HOH   HOH A . 
P 5 HOH   66  466 47  HOH   HOH A . 
P 5 HOH   67  467 249 HOH   HOH A . 
P 5 HOH   68  468 257 HOH   HOH A . 
P 5 HOH   69  469 551 HOH   HOH A . 
P 5 HOH   70  470 67  HOH   HOH A . 
P 5 HOH   71  471 159 HOH   HOH A . 
P 5 HOH   72  472 15  HOH   HOH A . 
P 5 HOH   73  473 581 HOH   HOH A . 
P 5 HOH   74  474 56  HOH   HOH A . 
P 5 HOH   75  475 20  HOH   HOH A . 
P 5 HOH   76  476 273 HOH   HOH A . 
P 5 HOH   77  477 166 HOH   HOH A . 
P 5 HOH   78  478 219 HOH   HOH A . 
P 5 HOH   79  479 233 HOH   HOH A . 
P 5 HOH   80  480 42  HOH   HOH A . 
P 5 HOH   81  481 89  HOH   HOH A . 
P 5 HOH   82  482 395 HOH   HOH A . 
P 5 HOH   83  483 23  HOH   HOH A . 
P 5 HOH   84  484 203 HOH   HOH A . 
P 5 HOH   85  485 312 HOH   HOH A . 
P 5 HOH   86  486 85  HOH   HOH A . 
P 5 HOH   87  487 175 HOH   HOH A . 
P 5 HOH   88  488 306 HOH   HOH A . 
P 5 HOH   89  489 30  HOH   HOH A . 
P 5 HOH   90  490 556 HOH   HOH A . 
P 5 HOH   91  491 59  HOH   HOH A . 
P 5 HOH   92  492 234 HOH   HOH A . 
P 5 HOH   93  493 276 HOH   HOH A . 
P 5 HOH   94  494 560 HOH   HOH A . 
P 5 HOH   95  495 231 HOH   HOH A . 
P 5 HOH   96  496 298 HOH   HOH A . 
P 5 HOH   97  497 86  HOH   HOH A . 
P 5 HOH   98  498 478 HOH   HOH A . 
P 5 HOH   99  499 274 HOH   HOH A . 
P 5 HOH   100 500 472 HOH   HOH A . 
P 5 HOH   101 501 525 HOH   HOH A . 
P 5 HOH   102 502 150 HOH   HOH A . 
P 5 HOH   103 503 260 HOH   HOH A . 
P 5 HOH   104 504 230 HOH   HOH A . 
P 5 HOH   105 505 465 HOH   HOH A . 
P 5 HOH   106 506 514 HOH   HOH A . 
P 5 HOH   107 507 599 HOH   HOH A . 
P 5 HOH   108 508 349 HOH   HOH A . 
P 5 HOH   109 509 322 HOH   HOH A . 
P 5 HOH   110 510 393 HOH   HOH A . 
P 5 HOH   111 511 536 HOH   HOH A . 
P 5 HOH   112 512 473 HOH   HOH A . 
P 5 HOH   113 513 310 HOH   HOH A . 
P 5 HOH   114 514 499 HOH   HOH A . 
P 5 HOH   115 515 367 HOH   HOH A . 
P 5 HOH   116 516 534 HOH   HOH A . 
P 5 HOH   117 517 501 HOH   HOH A . 
P 5 HOH   118 518 412 HOH   HOH A . 
P 5 HOH   119 519 504 HOH   HOH A . 
P 5 HOH   120 520 399 HOH   HOH A . 
P 5 HOH   121 521 396 HOH   HOH A . 
P 5 HOH   122 522 299 HOH   HOH A . 
P 5 HOH   123 523 400 HOH   HOH A . 
P 5 HOH   124 524 402 HOH   HOH A . 
P 5 HOH   125 525 248 HOH   HOH A . 
P 5 HOH   126 526 360 HOH   HOH A . 
P 5 HOH   127 527 346 HOH   HOH A . 
P 5 HOH   128 528 398 HOH   HOH A . 
P 5 HOH   129 529 518 HOH   HOH A . 
P 5 HOH   130 530 489 HOH   HOH A . 
P 5 HOH   131 531 564 HOH   HOH A . 
P 5 HOH   132 532 558 HOH   HOH A . 
P 5 HOH   133 533 529 HOH   HOH A . 
P 5 HOH   134 534 537 HOH   HOH A . 
P 5 HOH   135 535 544 HOH   HOH A . 
Q 5 HOH   1   401 584 HOH   HOH B . 
Q 5 HOH   2   402 586 HOH   HOH B . 
Q 5 HOH   3   403 339 HOH   HOH B . 
Q 5 HOH   4   404 309 HOH   HOH B . 
Q 5 HOH   5   405 125 HOH   HOH B . 
Q 5 HOH   6   406 130 HOH   HOH B . 
Q 5 HOH   7   407 26  HOH   HOH B . 
Q 5 HOH   8   408 464 HOH   HOH B . 
Q 5 HOH   9   409 565 HOH   HOH B . 
Q 5 HOH   10  410 268 HOH   HOH B . 
Q 5 HOH   11  411 513 HOH   HOH B . 
Q 5 HOH   12  412 7   HOH   HOH B . 
Q 5 HOH   13  413 221 HOH   HOH B . 
Q 5 HOH   14  414 245 HOH   HOH B . 
Q 5 HOH   15  415 41  HOH   HOH B . 
Q 5 HOH   16  416 238 HOH   HOH B . 
Q 5 HOH   17  417 100 HOH   HOH B . 
Q 5 HOH   18  418 146 HOH   HOH B . 
Q 5 HOH   19  419 66  HOH   HOH B . 
Q 5 HOH   20  420 147 HOH   HOH B . 
Q 5 HOH   21  421 497 HOH   HOH B . 
Q 5 HOH   22  422 156 HOH   HOH B . 
Q 5 HOH   23  423 206 HOH   HOH B . 
Q 5 HOH   24  424 93  HOH   HOH B . 
Q 5 HOH   25  425 186 HOH   HOH B . 
Q 5 HOH   26  426 576 HOH   HOH B . 
Q 5 HOH   27  427 31  HOH   HOH B . 
Q 5 HOH   28  428 122 HOH   HOH B . 
Q 5 HOH   29  429 353 HOH   HOH B . 
Q 5 HOH   30  430 289 HOH   HOH B . 
Q 5 HOH   31  431 455 HOH   HOH B . 
Q 5 HOH   32  432 338 HOH   HOH B . 
Q 5 HOH   33  433 237 HOH   HOH B . 
Q 5 HOH   34  434 223 HOH   HOH B . 
Q 5 HOH   35  435 180 HOH   HOH B . 
Q 5 HOH   36  436 79  HOH   HOH B . 
Q 5 HOH   37  437 282 HOH   HOH B . 
Q 5 HOH   38  438 224 HOH   HOH B . 
Q 5 HOH   39  439 84  HOH   HOH B . 
Q 5 HOH   40  440 351 HOH   HOH B . 
Q 5 HOH   41  441 445 HOH   HOH B . 
Q 5 HOH   42  442 1   HOH   HOH B . 
Q 5 HOH   43  443 552 HOH   HOH B . 
Q 5 HOH   44  444 469 HOH   HOH B . 
Q 5 HOH   45  445 250 HOH   HOH B . 
Q 5 HOH   46  446 113 HOH   HOH B . 
Q 5 HOH   47  447 64  HOH   HOH B . 
Q 5 HOH   48  448 25  HOH   HOH B . 
Q 5 HOH   49  449 88  HOH   HOH B . 
Q 5 HOH   50  450 484 HOH   HOH B . 
Q 5 HOH   51  451 337 HOH   HOH B . 
Q 5 HOH   52  452 523 HOH   HOH B . 
Q 5 HOH   53  453 154 HOH   HOH B . 
Q 5 HOH   54  454 174 HOH   HOH B . 
Q 5 HOH   55  455 19  HOH   HOH B . 
Q 5 HOH   56  456 142 HOH   HOH B . 
Q 5 HOH   57  457 255 HOH   HOH B . 
Q 5 HOH   58  458 58  HOH   HOH B . 
Q 5 HOH   59  459 55  HOH   HOH B . 
Q 5 HOH   60  460 199 HOH   HOH B . 
Q 5 HOH   61  461 17  HOH   HOH B . 
Q 5 HOH   62  462 319 HOH   HOH B . 
Q 5 HOH   63  463 409 HOH   HOH B . 
Q 5 HOH   64  464 104 HOH   HOH B . 
Q 5 HOH   65  465 115 HOH   HOH B . 
Q 5 HOH   66  466 70  HOH   HOH B . 
Q 5 HOH   67  467 145 HOH   HOH B . 
Q 5 HOH   68  468 169 HOH   HOH B . 
Q 5 HOH   69  469 269 HOH   HOH B . 
Q 5 HOH   70  470 366 HOH   HOH B . 
Q 5 HOH   71  471 575 HOH   HOH B . 
Q 5 HOH   72  472 483 HOH   HOH B . 
Q 5 HOH   73  473 321 HOH   HOH B . 
Q 5 HOH   74  474 61  HOH   HOH B . 
Q 5 HOH   75  475 68  HOH   HOH B . 
Q 5 HOH   76  476 87  HOH   HOH B . 
Q 5 HOH   77  477 34  HOH   HOH B . 
Q 5 HOH   78  478 315 HOH   HOH B . 
Q 5 HOH   79  479 436 HOH   HOH B . 
Q 5 HOH   80  480 345 HOH   HOH B . 
Q 5 HOH   81  481 452 HOH   HOH B . 
Q 5 HOH   82  482 48  HOH   HOH B . 
Q 5 HOH   83  483 561 HOH   HOH B . 
Q 5 HOH   84  484 9   HOH   HOH B . 
Q 5 HOH   85  485 605 HOH   HOH B . 
Q 5 HOH   86  486 185 HOH   HOH B . 
Q 5 HOH   87  487 522 HOH   HOH B . 
Q 5 HOH   88  488 197 HOH   HOH B . 
Q 5 HOH   89  489 97  HOH   HOH B . 
Q 5 HOH   90  490 46  HOH   HOH B . 
Q 5 HOH   91  491 420 HOH   HOH B . 
Q 5 HOH   92  492 4   HOH   HOH B . 
Q 5 HOH   93  493 123 HOH   HOH B . 
Q 5 HOH   94  494 283 HOH   HOH B . 
Q 5 HOH   95  495 214 HOH   HOH B . 
Q 5 HOH   96  496 109 HOH   HOH B . 
Q 5 HOH   97  497 235 HOH   HOH B . 
Q 5 HOH   98  498 297 HOH   HOH B . 
Q 5 HOH   99  499 218 HOH   HOH B . 
Q 5 HOH   100 500 370 HOH   HOH B . 
Q 5 HOH   101 501 90  HOH   HOH B . 
Q 5 HOH   102 502 137 HOH   HOH B . 
Q 5 HOH   103 503 208 HOH   HOH B . 
Q 5 HOH   104 504 265 HOH   HOH B . 
Q 5 HOH   105 505 326 HOH   HOH B . 
Q 5 HOH   106 506 601 HOH   HOH B . 
Q 5 HOH   107 507 362 HOH   HOH B . 
Q 5 HOH   108 508 510 HOH   HOH B . 
Q 5 HOH   109 509 526 HOH   HOH B . 
Q 5 HOH   110 510 430 HOH   HOH B . 
Q 5 HOH   111 511 303 HOH   HOH B . 
Q 5 HOH   112 512 423 HOH   HOH B . 
Q 5 HOH   113 513 542 HOH   HOH B . 
Q 5 HOH   114 514 493 HOH   HOH B . 
Q 5 HOH   115 515 503 HOH   HOH B . 
Q 5 HOH   116 516 424 HOH   HOH B . 
Q 5 HOH   117 517 204 HOH   HOH B . 
Q 5 HOH   118 518 573 HOH   HOH B . 
Q 5 HOH   119 519 600 HOH   HOH B . 
Q 5 HOH   120 520 468 HOH   HOH B . 
Q 5 HOH   121 521 578 HOH   HOH B . 
Q 5 HOH   122 522 505 HOH   HOH B . 
Q 5 HOH   123 523 491 HOH   HOH B . 
Q 5 HOH   124 524 519 HOH   HOH B . 
Q 5 HOH   125 525 363 HOH   HOH B . 
Q 5 HOH   126 526 498 HOH   HOH B . 
Q 5 HOH   127 527 486 HOH   HOH B . 
Q 5 HOH   128 528 448 HOH   HOH B . 
Q 5 HOH   129 529 254 HOH   HOH B . 
Q 5 HOH   130 530 451 HOH   HOH B . 
Q 5 HOH   131 531 405 HOH   HOH B . 
Q 5 HOH   132 532 602 HOH   HOH B . 
Q 5 HOH   133 533 485 HOH   HOH B . 
Q 5 HOH   134 534 244 HOH   HOH B . 
Q 5 HOH   135 535 241 HOH   HOH B . 
Q 5 HOH   136 536 377 HOH   HOH B . 
Q 5 HOH   137 537 365 HOH   HOH B . 
Q 5 HOH   138 538 603 HOH   HOH B . 
Q 5 HOH   139 539 333 HOH   HOH B . 
Q 5 HOH   140 540 604 HOH   HOH B . 
Q 5 HOH   141 541 543 HOH   HOH B . 
Q 5 HOH   142 542 411 HOH   HOH B . 
Q 5 HOH   143 543 440 HOH   HOH B . 
Q 5 HOH   144 544 461 HOH   HOH B . 
Q 5 HOH   145 545 453 HOH   HOH B . 
Q 5 HOH   146 546 559 HOH   HOH B . 
R 5 HOH   1   401 284 HOH   HOH C . 
R 5 HOH   2   402 259 HOH   HOH C . 
R 5 HOH   3   403 336 HOH   HOH C . 
R 5 HOH   4   404 14  HOH   HOH C . 
R 5 HOH   5   405 475 HOH   HOH C . 
R 5 HOH   6   406 38  HOH   HOH C . 
R 5 HOH   7   407 215 HOH   HOH C . 
R 5 HOH   8   408 553 HOH   HOH C . 
R 5 HOH   9   409 285 HOH   HOH C . 
R 5 HOH   10  410 588 HOH   HOH C . 
R 5 HOH   11  411 28  HOH   HOH C . 
R 5 HOH   12  412 278 HOH   HOH C . 
R 5 HOH   13  413 459 HOH   HOH C . 
R 5 HOH   14  414 69  HOH   HOH C . 
R 5 HOH   15  415 589 HOH   HOH C . 
R 5 HOH   16  416 71  HOH   HOH C . 
R 5 HOH   17  417 527 HOH   HOH C . 
R 5 HOH   18  418 152 HOH   HOH C . 
R 5 HOH   19  419 394 HOH   HOH C . 
R 5 HOH   20  420 107 HOH   HOH C . 
R 5 HOH   21  421 6   HOH   HOH C . 
R 5 HOH   22  422 178 HOH   HOH C . 
R 5 HOH   23  423 592 HOH   HOH C . 
R 5 HOH   24  424 202 HOH   HOH C . 
R 5 HOH   25  425 110 HOH   HOH C . 
R 5 HOH   26  426 10  HOH   HOH C . 
R 5 HOH   27  427 587 HOH   HOH C . 
R 5 HOH   28  428 196 HOH   HOH C . 
R 5 HOH   29  429 177 HOH   HOH C . 
R 5 HOH   30  430 136 HOH   HOH C . 
R 5 HOH   31  431 91  HOH   HOH C . 
R 5 HOH   32  432 546 HOH   HOH C . 
R 5 HOH   33  433 352 HOH   HOH C . 
R 5 HOH   34  434 392 HOH   HOH C . 
R 5 HOH   35  435 354 HOH   HOH C . 
R 5 HOH   36  436 457 HOH   HOH C . 
R 5 HOH   37  437 143 HOH   HOH C . 
R 5 HOH   38  438 182 HOH   HOH C . 
R 5 HOH   39  439 24  HOH   HOH C . 
R 5 HOH   40  440 288 HOH   HOH C . 
R 5 HOH   41  441 60  HOH   HOH C . 
R 5 HOH   42  442 124 HOH   HOH C . 
R 5 HOH   43  443 35  HOH   HOH C . 
R 5 HOH   44  444 52  HOH   HOH C . 
R 5 HOH   45  445 535 HOH   HOH C . 
R 5 HOH   46  446 27  HOH   HOH C . 
R 5 HOH   47  447 138 HOH   HOH C . 
R 5 HOH   48  448 597 HOH   HOH C . 
R 5 HOH   49  449 447 HOH   HOH C . 
R 5 HOH   50  450 102 HOH   HOH C . 
R 5 HOH   51  451 135 HOH   HOH C . 
R 5 HOH   52  452 357 HOH   HOH C . 
R 5 HOH   53  453 439 HOH   HOH C . 
R 5 HOH   54  454 316 HOH   HOH C . 
R 5 HOH   55  455 300 HOH   HOH C . 
R 5 HOH   56  456 550 HOH   HOH C . 
R 5 HOH   57  457 580 HOH   HOH C . 
R 5 HOH   58  458 151 HOH   HOH C . 
R 5 HOH   59  459 435 HOH   HOH C . 
R 5 HOH   60  460 225 HOH   HOH C . 
R 5 HOH   61  461 251 HOH   HOH C . 
R 5 HOH   62  462 422 HOH   HOH C . 
R 5 HOH   63  463 318 HOH   HOH C . 
R 5 HOH   64  464 331 HOH   HOH C . 
R 5 HOH   65  465 207 HOH   HOH C . 
R 5 HOH   66  466 194 HOH   HOH C . 
R 5 HOH   67  467 232 HOH   HOH C . 
R 5 HOH   68  468 18  HOH   HOH C . 
R 5 HOH   69  469 450 HOH   HOH C . 
R 5 HOH   70  470 228 HOH   HOH C . 
R 5 HOH   71  471 133 HOH   HOH C . 
R 5 HOH   72  472 515 HOH   HOH C . 
R 5 HOH   73  473 383 HOH   HOH C . 
R 5 HOH   74  474 162 HOH   HOH C . 
R 5 HOH   75  475 431 HOH   HOH C . 
R 5 HOH   76  476 105 HOH   HOH C . 
R 5 HOH   77  477 21  HOH   HOH C . 
R 5 HOH   78  478 311 HOH   HOH C . 
R 5 HOH   79  479 77  HOH   HOH C . 
R 5 HOH   80  480 540 HOH   HOH C . 
R 5 HOH   81  481 118 HOH   HOH C . 
R 5 HOH   82  482 3   HOH   HOH C . 
R 5 HOH   83  483 5   HOH   HOH C . 
R 5 HOH   84  484 591 HOH   HOH C . 
R 5 HOH   85  485 148 HOH   HOH C . 
R 5 HOH   86  486 236 HOH   HOH C . 
R 5 HOH   87  487 280 HOH   HOH C . 
R 5 HOH   88  488 227 HOH   HOH C . 
R 5 HOH   89  489 106 HOH   HOH C . 
R 5 HOH   90  490 211 HOH   HOH C . 
R 5 HOH   91  491 549 HOH   HOH C . 
R 5 HOH   92  492 369 HOH   HOH C . 
R 5 HOH   93  493 96  HOH   HOH C . 
R 5 HOH   94  494 62  HOH   HOH C . 
R 5 HOH   95  495 111 HOH   HOH C . 
R 5 HOH   96  496 350 HOH   HOH C . 
R 5 HOH   97  497 101 HOH   HOH C . 
R 5 HOH   98  498 49  HOH   HOH C . 
R 5 HOH   99  499 480 HOH   HOH C . 
R 5 HOH   100 500 158 HOH   HOH C . 
R 5 HOH   101 501 246 HOH   HOH C . 
R 5 HOH   102 502 538 HOH   HOH C . 
R 5 HOH   103 503 579 HOH   HOH C . 
R 5 HOH   104 504 117 HOH   HOH C . 
R 5 HOH   105 505 359 HOH   HOH C . 
R 5 HOH   106 506 512 HOH   HOH C . 
R 5 HOH   107 507 406 HOH   HOH C . 
R 5 HOH   108 508 567 HOH   HOH C . 
R 5 HOH   109 509 329 HOH   HOH C . 
R 5 HOH   110 510 434 HOH   HOH C . 
R 5 HOH   111 511 164 HOH   HOH C . 
R 5 HOH   112 512 356 HOH   HOH C . 
R 5 HOH   113 513 272 HOH   HOH C . 
R 5 HOH   114 514 548 HOH   HOH C . 
R 5 HOH   115 515 140 HOH   HOH C . 
R 5 HOH   116 516 43  HOH   HOH C . 
R 5 HOH   117 517 539 HOH   HOH C . 
R 5 HOH   118 518 530 HOH   HOH C . 
R 5 HOH   119 519 441 HOH   HOH C . 
R 5 HOH   120 520 419 HOH   HOH C . 
R 5 HOH   121 521 287 HOH   HOH C . 
R 5 HOH   122 522 428 HOH   HOH C . 
R 5 HOH   123 523 490 HOH   HOH C . 
R 5 HOH   124 524 403 HOH   HOH C . 
R 5 HOH   125 525 471 HOH   HOH C . 
R 5 HOH   126 526 462 HOH   HOH C . 
R 5 HOH   127 527 407 HOH   HOH C . 
R 5 HOH   128 528 532 HOH   HOH C . 
R 5 HOH   129 529 590 HOH   HOH C . 
R 5 HOH   130 530 328 HOH   HOH C . 
R 5 HOH   131 531 563 HOH   HOH C . 
R 5 HOH   132 532 313 HOH   HOH C . 
R 5 HOH   133 533 327 HOH   HOH C . 
R 5 HOH   134 534 467 HOH   HOH C . 
R 5 HOH   135 535 433 HOH   HOH C . 
R 5 HOH   136 536 413 HOH   HOH C . 
R 5 HOH   137 537 524 HOH   HOH C . 
S 5 HOH   1   401 165 HOH   HOH D . 
S 5 HOH   2   402 277 HOH   HOH D . 
S 5 HOH   3   403 482 HOH   HOH D . 
S 5 HOH   4   404 57  HOH   HOH D . 
S 5 HOH   5   405 520 HOH   HOH D . 
S 5 HOH   6   406 508 HOH   HOH D . 
S 5 HOH   7   407 547 HOH   HOH D . 
S 5 HOH   8   408 466 HOH   HOH D . 
S 5 HOH   9   409 263 HOH   HOH D . 
S 5 HOH   10  410 37  HOH   HOH D . 
S 5 HOH   11  411 593 HOH   HOH D . 
S 5 HOH   12  412 183 HOH   HOH D . 
S 5 HOH   13  413 477 HOH   HOH D . 
S 5 HOH   14  414 347 HOH   HOH D . 
S 5 HOH   15  415 95  HOH   HOH D . 
S 5 HOH   16  416 594 HOH   HOH D . 
S 5 HOH   17  417 160 HOH   HOH D . 
S 5 HOH   18  418 168 HOH   HOH D . 
S 5 HOH   19  419 13  HOH   HOH D . 
S 5 HOH   20  420 317 HOH   HOH D . 
S 5 HOH   21  421 155 HOH   HOH D . 
S 5 HOH   22  422 39  HOH   HOH D . 
S 5 HOH   23  423 200 HOH   HOH D . 
S 5 HOH   24  424 494 HOH   HOH D . 
S 5 HOH   25  425 371 HOH   HOH D . 
S 5 HOH   26  426 479 HOH   HOH D . 
S 5 HOH   27  427 220 HOH   HOH D . 
S 5 HOH   28  428 193 HOH   HOH D . 
S 5 HOH   29  429 75  HOH   HOH D . 
S 5 HOH   30  430 94  HOH   HOH D . 
S 5 HOH   31  431 304 HOH   HOH D . 
S 5 HOH   32  432 32  HOH   HOH D . 
S 5 HOH   33  433 126 HOH   HOH D . 
S 5 HOH   34  434 108 HOH   HOH D . 
S 5 HOH   35  435 463 HOH   HOH D . 
S 5 HOH   36  436 258 HOH   HOH D . 
S 5 HOH   37  437 421 HOH   HOH D . 
S 5 HOH   38  438 374 HOH   HOH D . 
S 5 HOH   39  439 36  HOH   HOH D . 
S 5 HOH   40  440 29  HOH   HOH D . 
S 5 HOH   41  441 139 HOH   HOH D . 
S 5 HOH   42  442 63  HOH   HOH D . 
S 5 HOH   43  443 171 HOH   HOH D . 
S 5 HOH   44  444 264 HOH   HOH D . 
S 5 HOH   45  445 128 HOH   HOH D . 
S 5 HOH   46  446 179 HOH   HOH D . 
S 5 HOH   47  447 161 HOH   HOH D . 
S 5 HOH   48  448 172 HOH   HOH D . 
S 5 HOH   49  449 577 HOH   HOH D . 
S 5 HOH   50  450 81  HOH   HOH D . 
S 5 HOH   51  451 116 HOH   HOH D . 
S 5 HOH   52  452 195 HOH   HOH D . 
S 5 HOH   53  453 121 HOH   HOH D . 
S 5 HOH   54  454 229 HOH   HOH D . 
S 5 HOH   55  455 308 HOH   HOH D . 
S 5 HOH   56  456 112 HOH   HOH D . 
S 5 HOH   57  457 120 HOH   HOH D . 
S 5 HOH   58  458 170 HOH   HOH D . 
S 5 HOH   59  459 481 HOH   HOH D . 
S 5 HOH   60  460 163 HOH   HOH D . 
S 5 HOH   61  461 78  HOH   HOH D . 
S 5 HOH   62  462 334 HOH   HOH D . 
S 5 HOH   63  463 323 HOH   HOH D . 
S 5 HOH   64  464 82  HOH   HOH D . 
S 5 HOH   65  465 50  HOH   HOH D . 
S 5 HOH   66  466 45  HOH   HOH D . 
S 5 HOH   67  467 12  HOH   HOH D . 
S 5 HOH   68  468 286 HOH   HOH D . 
S 5 HOH   69  469 98  HOH   HOH D . 
S 5 HOH   70  470 73  HOH   HOH D . 
S 5 HOH   71  471 368 HOH   HOH D . 
S 5 HOH   72  472 456 HOH   HOH D . 
S 5 HOH   73  473 267 HOH   HOH D . 
S 5 HOH   74  474 293 HOH   HOH D . 
S 5 HOH   75  475 332 HOH   HOH D . 
S 5 HOH   76  476 22  HOH   HOH D . 
S 5 HOH   77  477 33  HOH   HOH D . 
S 5 HOH   78  478 279 HOH   HOH D . 
S 5 HOH   79  479 153 HOH   HOH D . 
S 5 HOH   80  480 201 HOH   HOH D . 
S 5 HOH   81  481 290 HOH   HOH D . 
S 5 HOH   82  482 295 HOH   HOH D . 
S 5 HOH   83  483 213 HOH   HOH D . 
S 5 HOH   84  484 74  HOH   HOH D . 
S 5 HOH   85  485 72  HOH   HOH D . 
S 5 HOH   86  486 83  HOH   HOH D . 
S 5 HOH   87  487 474 HOH   HOH D . 
S 5 HOH   88  488 119 HOH   HOH D . 
S 5 HOH   89  489 372 HOH   HOH D . 
S 5 HOH   90  490 132 HOH   HOH D . 
S 5 HOH   91  491 358 HOH   HOH D . 
S 5 HOH   92  492 585 HOH   HOH D . 
S 5 HOH   93  493 415 HOH   HOH D . 
S 5 HOH   94  494 460 HOH   HOH D . 
S 5 HOH   95  495 598 HOH   HOH D . 
S 5 HOH   96  496 92  HOH   HOH D . 
S 5 HOH   97  497 348 HOH   HOH D . 
S 5 HOH   98  498 410 HOH   HOH D . 
S 5 HOH   99  499 595 HOH   HOH D . 
S 5 HOH   100 500 454 HOH   HOH D . 
S 5 HOH   101 501 414 HOH   HOH D . 
S 5 HOH   102 502 495 HOH   HOH D . 
S 5 HOH   103 503 416 HOH   HOH D . 
S 5 HOH   104 504 502 HOH   HOH D . 
S 5 HOH   105 505 449 HOH   HOH D . 
S 5 HOH   106 506 432 HOH   HOH D . 
S 5 HOH   107 507 404 HOH   HOH D . 
S 5 HOH   108 508 343 HOH   HOH D . 
S 5 HOH   109 509 533 HOH   HOH D . 
S 5 HOH   110 510 408 HOH   HOH D . 
S 5 HOH   111 511 492 HOH   HOH D . 
S 5 HOH   112 512 375 HOH   HOH D . 
S 5 HOH   113 513 387 HOH   HOH D . 
S 5 HOH   114 514 500 HOH   HOH D . 
S 5 HOH   115 515 418 HOH   HOH D . 
S 5 HOH   116 516 443 HOH   HOH D . 
S 5 HOH   117 517 517 HOH   HOH D . 
S 5 HOH   118 518 401 HOH   HOH D . 
S 5 HOH   119 519 437 HOH   HOH D . 
S 5 HOH   120 520 256 HOH   HOH D . 
S 5 HOH   121 521 596 HOH   HOH D . 
S 5 HOH   122 522 568 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A SER 152 ? OG  ? A SER 173 OG  
2  1 Y 1 A GLU 216 ? CG  ? A GLU 237 CG  
3  1 Y 1 A GLU 216 ? CD  ? A GLU 237 CD  
4  1 Y 1 A GLU 216 ? OE1 ? A GLU 237 OE1 
5  1 Y 1 A GLU 216 ? OE2 ? A GLU 237 OE2 
6  1 Y 1 A LYS 220 ? CG  ? A LYS 241 CG  
7  1 Y 1 A LYS 220 ? CD  ? A LYS 241 CD  
8  1 Y 1 A LYS 220 ? CE  ? A LYS 241 CE  
9  1 Y 1 A LYS 220 ? NZ  ? A LYS 241 NZ  
10 1 Y 1 B LYS 143 ? CD  ? B LYS 164 CD  
11 1 Y 1 B LYS 143 ? CE  ? B LYS 164 CE  
12 1 Y 1 B LYS 143 ? NZ  ? B LYS 164 NZ  
13 1 Y 1 B SER 152 ? OG  ? B SER 173 OG  
14 1 Y 1 B VAL 211 ? CG1 ? B VAL 232 CG1 
15 1 Y 1 B VAL 211 ? CG2 ? B VAL 232 CG2 
16 1 Y 1 C LYS 13  ? CE  ? C LYS 34  CE  
17 1 Y 1 C LYS 13  ? NZ  ? C LYS 34  NZ  
18 1 Y 1 C LYS 50  ? CE  ? C LYS 71  CE  
19 1 Y 1 C LYS 50  ? NZ  ? C LYS 71  NZ  
20 1 Y 1 C GLN 104 ? CG  ? C GLN 125 CG  
21 1 Y 1 C GLN 104 ? CD  ? C GLN 125 CD  
22 1 Y 1 C GLN 104 ? OE1 ? C GLN 125 OE1 
23 1 Y 1 C GLN 104 ? NE2 ? C GLN 125 NE2 
24 1 Y 1 C SER 152 ? OG  ? C SER 173 OG  
25 1 Y 1 C VAL 211 ? CG1 ? C VAL 232 CG1 
26 1 Y 1 C VAL 211 ? CG2 ? C VAL 232 CG2 
27 1 Y 1 C GLU 216 ? CG  ? C GLU 237 CG  
28 1 Y 1 C GLU 216 ? CD  ? C GLU 237 CD  
29 1 Y 1 C GLU 216 ? OE1 ? C GLU 237 OE1 
30 1 Y 1 C GLU 216 ? OE2 ? C GLU 237 OE2 
31 1 Y 1 C GLU 217 ? CD  ? C GLU 238 CD  
32 1 Y 1 C GLU 217 ? OE1 ? C GLU 238 OE1 
33 1 Y 1 C GLU 217 ? OE2 ? C GLU 238 OE2 
34 1 Y 1 C LYS 220 ? CD  ? C LYS 241 CD  
35 1 Y 1 C LYS 220 ? CE  ? C LYS 241 CE  
36 1 Y 1 C LYS 220 ? NZ  ? C LYS 241 NZ  
37 1 Y 1 D LYS 13  ? NZ  ? D LYS 34  NZ  
38 1 Y 1 D LYS 50  ? CD  ? D LYS 71  CD  
39 1 Y 1 D LYS 50  ? CE  ? D LYS 71  CE  
40 1 Y 1 D LYS 50  ? NZ  ? D LYS 71  NZ  
41 1 Y 1 D SER 152 ? OG  ? D SER 173 OG  
42 1 Y 1 D VAL 211 ? CG1 ? D VAL 232 CG1 
43 1 Y 1 D VAL 211 ? CG2 ? D VAL 232 CG2 
44 1 Y 1 D GLU 216 ? CD  ? D GLU 237 CD  
45 1 Y 1 D GLU 216 ? OE1 ? D GLU 237 OE1 
46 1 Y 1 D GLU 216 ? OE2 ? D GLU 237 OE2 
47 1 Y 1 D GLU 217 ? CD  ? D GLU 238 CD  
48 1 Y 1 D GLU 217 ? OE1 ? D GLU 238 OE1 
49 1 Y 1 D GLU 217 ? OE2 ? D GLU 238 OE2 
50 1 Y 1 D ARG 230 ? CZ  ? D ARG 251 CZ  
51 1 Y 1 D ARG 230 ? NH1 ? D ARG 251 NH1 
52 1 Y 1 D ARG 230 ? NH2 ? D ARG 251 NH2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   115.88 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RHU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.032 
_cell.length_a_esd                 ? 
_cell.length_b                     89.646 
_cell.length_b_esd                 ? 
_cell.length_c                     84.165 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8RHU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RHU 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.14 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_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    '1.6-2.5 M sodium acetate and 0.1 M sodium citrate, pH 5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            297 
# 
_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 EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-13 
_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                    'Double Crystal' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95374 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95374 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          25.5 
_reflns.entry_id                                       8RHU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.71 
_reflns.d_resolution_low                               75.72 
_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                                     106180 
_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                     2.0 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.9 
_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                                0.058 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.046 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.71 
_reflns_shell.d_res_low                                     1.74 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5229 
_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                               4.8 
_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                               0.822 
_reflns_shell.pdbx_Rpim_I_all                               0.490 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.835 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.655 
_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]                            0.00 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.262 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RHU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.71 
_refine.ls_d_res_low                             75.72 
_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                     100808 
_refine.ls_number_reflns_R_free                  5331 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.42 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18681 
_refine.ls_R_factor_R_free                       0.22121 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18495 
_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                       0.113 
_refine.pdbx_overall_ESU_R_Free                  0.111 
_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                             3.471 
_refine.overall_SU_ML                            0.101 
_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_analyze.entry_id                        8RHU 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.71 
_refine_hist.d_res_low                        75.72 
_refine_hist.number_atoms_solvent             540 
_refine_hist.number_atoms_total               8184 
_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        7382 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         262 
_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' ? 0.009  0.012  7915  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.850  1.816  10837 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.162  5.000  1030  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.206  5.000  70    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.154 10.000 1227  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.131  0.200  1294  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  5885  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? 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' ? 2.493  2.703  4026  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.414  4.827  5018  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.182  3.018  3889  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.618  31.00  12593 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? 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                       1.710 
_refine_ls_shell.d_res_low                        1.754 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             426 
_refine_ls_shell.number_reflns_R_work             7449 
_refine_ls_shell.percent_reflns_obs               99.42 
_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                  0.450 
_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                  0.444 
# 
_struct.entry_id                     8RHU 
_struct.title                        'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P25' 
_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        8RHU 
_struct_keywords.text            'Trypanosoma brucei, PTR1, Pteridine reductase, cofactor, NADPH, inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 2 ? 
O N N 3 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
S N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O76290_TRYBB 
_struct_ref.pdbx_db_accession          O76290 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVCQADLTNSNVLPASCEEIINSC
FRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFAQRQKGTNPNCTSSNLSIVNLC
DAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKDKWRRKVPLGRREASAEQIADA
VIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8RHU A 22 ? 289 ? O76290 1 ? 268 ? 1 268 
2 1 8RHU B 22 ? 289 ? O76290 1 ? 268 ? 1 268 
3 1 8RHU C 22 ? 289 ? O76290 1 ? 268 ? 1 268 
4 1 8RHU D 22 ? 289 ? O76290 1 ? 268 ? 1 268 
# 
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 8RHU MET A 1  ? UNP O76290 ? ? 'initiating methionine' -20 1  
1 8RHU GLY A 2  ? UNP O76290 ? ? 'expression tag'        -19 2  
1 8RHU SER A 3  ? UNP O76290 ? ? 'expression tag'        -18 3  
1 8RHU SER A 4  ? UNP O76290 ? ? 'expression tag'        -17 4  
1 8RHU HIS A 5  ? UNP O76290 ? ? 'expression tag'        -16 5  
1 8RHU HIS A 6  ? UNP O76290 ? ? 'expression tag'        -15 6  
1 8RHU HIS A 7  ? UNP O76290 ? ? 'expression tag'        -14 7  
1 8RHU HIS A 8  ? UNP O76290 ? ? 'expression tag'        -13 8  
1 8RHU HIS A 9  ? UNP O76290 ? ? 'expression tag'        -12 9  
1 8RHU HIS A 10 ? UNP O76290 ? ? 'expression tag'        -11 10 
1 8RHU SER A 11 ? UNP O76290 ? ? 'expression tag'        -10 11 
1 8RHU SER A 12 ? UNP O76290 ? ? 'expression tag'        -9  12 
1 8RHU GLY A 13 ? UNP O76290 ? ? 'expression tag'        -8  13 
1 8RHU LEU A 14 ? UNP O76290 ? ? 'expression tag'        -7  14 
1 8RHU VAL A 15 ? UNP O76290 ? ? 'expression tag'        -6  15 
1 8RHU PRO A 16 ? UNP O76290 ? ? 'expression tag'        -5  16 
1 8RHU ARG A 17 ? UNP O76290 ? ? 'expression tag'        -4  17 
1 8RHU GLY A 18 ? UNP O76290 ? ? 'expression tag'        -3  18 
1 8RHU SER A 19 ? UNP O76290 ? ? 'expression tag'        -2  19 
1 8RHU HIS A 20 ? UNP O76290 ? ? 'expression tag'        -1  20 
1 8RHU MET A 21 ? UNP O76290 ? ? 'expression tag'        0   21 
2 8RHU MET B 1  ? UNP O76290 ? ? 'initiating methionine' -20 22 
2 8RHU GLY B 2  ? UNP O76290 ? ? 'expression tag'        -19 23 
2 8RHU SER B 3  ? UNP O76290 ? ? 'expression tag'        -18 24 
2 8RHU SER B 4  ? UNP O76290 ? ? 'expression tag'        -17 25 
2 8RHU HIS B 5  ? UNP O76290 ? ? 'expression tag'        -16 26 
2 8RHU HIS B 6  ? UNP O76290 ? ? 'expression tag'        -15 27 
2 8RHU HIS B 7  ? UNP O76290 ? ? 'expression tag'        -14 28 
2 8RHU HIS B 8  ? UNP O76290 ? ? 'expression tag'        -13 29 
2 8RHU HIS B 9  ? UNP O76290 ? ? 'expression tag'        -12 30 
2 8RHU HIS B 10 ? UNP O76290 ? ? 'expression tag'        -11 31 
2 8RHU SER B 11 ? UNP O76290 ? ? 'expression tag'        -10 32 
2 8RHU SER B 12 ? UNP O76290 ? ? 'expression tag'        -9  33 
2 8RHU GLY B 13 ? UNP O76290 ? ? 'expression tag'        -8  34 
2 8RHU LEU B 14 ? UNP O76290 ? ? 'expression tag'        -7  35 
2 8RHU VAL B 15 ? UNP O76290 ? ? 'expression tag'        -6  36 
2 8RHU PRO B 16 ? UNP O76290 ? ? 'expression tag'        -5  37 
2 8RHU ARG B 17 ? UNP O76290 ? ? 'expression tag'        -4  38 
2 8RHU GLY B 18 ? UNP O76290 ? ? 'expression tag'        -3  39 
2 8RHU SER B 19 ? UNP O76290 ? ? 'expression tag'        -2  40 
2 8RHU HIS B 20 ? UNP O76290 ? ? 'expression tag'        -1  41 
2 8RHU MET B 21 ? UNP O76290 ? ? 'expression tag'        0   42 
3 8RHU MET C 1  ? UNP O76290 ? ? 'initiating methionine' -20 43 
3 8RHU GLY C 2  ? UNP O76290 ? ? 'expression tag'        -19 44 
3 8RHU SER C 3  ? UNP O76290 ? ? 'expression tag'        -18 45 
3 8RHU SER C 4  ? UNP O76290 ? ? 'expression tag'        -17 46 
3 8RHU HIS C 5  ? UNP O76290 ? ? 'expression tag'        -16 47 
3 8RHU HIS C 6  ? UNP O76290 ? ? 'expression tag'        -15 48 
3 8RHU HIS C 7  ? UNP O76290 ? ? 'expression tag'        -14 49 
3 8RHU HIS C 8  ? UNP O76290 ? ? 'expression tag'        -13 50 
3 8RHU HIS C 9  ? UNP O76290 ? ? 'expression tag'        -12 51 
3 8RHU HIS C 10 ? UNP O76290 ? ? 'expression tag'        -11 52 
3 8RHU SER C 11 ? UNP O76290 ? ? 'expression tag'        -10 53 
3 8RHU SER C 12 ? UNP O76290 ? ? 'expression tag'        -9  54 
3 8RHU GLY C 13 ? UNP O76290 ? ? 'expression tag'        -8  55 
3 8RHU LEU C 14 ? UNP O76290 ? ? 'expression tag'        -7  56 
3 8RHU VAL C 15 ? UNP O76290 ? ? 'expression tag'        -6  57 
3 8RHU PRO C 16 ? UNP O76290 ? ? 'expression tag'        -5  58 
3 8RHU ARG C 17 ? UNP O76290 ? ? 'expression tag'        -4  59 
3 8RHU GLY C 18 ? UNP O76290 ? ? 'expression tag'        -3  60 
3 8RHU SER C 19 ? UNP O76290 ? ? 'expression tag'        -2  61 
3 8RHU HIS C 20 ? UNP O76290 ? ? 'expression tag'        -1  62 
3 8RHU MET C 21 ? UNP O76290 ? ? 'expression tag'        0   63 
4 8RHU MET D 1  ? UNP O76290 ? ? 'initiating methionine' -20 64 
4 8RHU GLY D 2  ? UNP O76290 ? ? 'expression tag'        -19 65 
4 8RHU SER D 3  ? UNP O76290 ? ? 'expression tag'        -18 66 
4 8RHU SER D 4  ? UNP O76290 ? ? 'expression tag'        -17 67 
4 8RHU HIS D 5  ? UNP O76290 ? ? 'expression tag'        -16 68 
4 8RHU HIS D 6  ? UNP O76290 ? ? 'expression tag'        -15 69 
4 8RHU HIS D 7  ? UNP O76290 ? ? 'expression tag'        -14 70 
4 8RHU HIS D 8  ? UNP O76290 ? ? 'expression tag'        -13 71 
4 8RHU HIS D 9  ? UNP O76290 ? ? 'expression tag'        -12 72 
4 8RHU HIS D 10 ? UNP O76290 ? ? 'expression tag'        -11 73 
4 8RHU SER D 11 ? UNP O76290 ? ? 'expression tag'        -10 74 
4 8RHU SER D 12 ? UNP O76290 ? ? 'expression tag'        -9  75 
4 8RHU GLY D 13 ? UNP O76290 ? ? 'expression tag'        -8  76 
4 8RHU LEU D 14 ? UNP O76290 ? ? 'expression tag'        -7  77 
4 8RHU VAL D 15 ? UNP O76290 ? ? 'expression tag'        -6  78 
4 8RHU PRO D 16 ? UNP O76290 ? ? 'expression tag'        -5  79 
4 8RHU ARG D 17 ? UNP O76290 ? ? 'expression tag'        -4  80 
4 8RHU GLY D 18 ? UNP O76290 ? ? 'expression tag'        -3  81 
4 8RHU SER D 19 ? UNP O76290 ? ? 'expression tag'        -2  82 
4 8RHU HIS D 20 ? UNP O76290 ? ? 'expression tag'        -1  83 
4 8RHU MET D 21 ? UNP O76290 ? ? 'expression tag'        0   84 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 20750 ? 
1 MORE         -131  ? 
1 'SSA (A^2)'  31630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 34  ? THR A 47  ? LYS A 13  THR A 26  1 ? 14 
HELX_P HELX_P2  AA2 SER A 58  ? ARG A 73  ? SER A 37  ARG A 52  1 ? 16 
HELX_P HELX_P3  AA3 VAL A 89  ? GLY A 106 ? VAL A 68  GLY A 85  1 ? 18 
HELX_P HELX_P4  AA4 THR A 136 ? ALA A 149 ? THR A 115 ALA A 128 1 ? 14 
HELX_P HELX_P5  AA5 ALA A 149 ? ARG A 162 ? ALA A 128 ARG A 141 1 ? 14 
HELX_P HELX_P6  AA6 PHE A 192 ? ALA A 214 ? PHE A 171 ALA A 193 1 ? 23 
HELX_P HELX_P7  AA7 PRO A 215 ? GLY A 217 ? PRO A 194 GLY A 196 5 ? 3  
HELX_P HELX_P8  AA8 GLY A 235 ? ARG A 244 ? GLY A 214 ARG A 223 1 ? 10 
HELX_P HELX_P9  AA9 SER A 254 ? SER A 267 ? SER A 233 SER A 246 1 ? 14 
HELX_P HELX_P10 AB1 GLY A 268 ? GLN A 271 ? GLY A 247 GLN A 250 5 ? 4  
HELX_P HELX_P11 AB2 GLY A 283 ? VAL A 287 ? GLY A 262 VAL A 266 5 ? 5  
HELX_P HELX_P12 AB3 LYS B 34  ? THR B 47  ? LYS B 13  THR B 26  1 ? 14 
HELX_P HELX_P13 AB4 SER B 58  ? ARG B 73  ? SER B 37  ARG B 52  1 ? 16 
HELX_P HELX_P14 AB5 VAL B 89  ? GLY B 106 ? VAL B 68  GLY B 85  1 ? 18 
HELX_P HELX_P15 AB6 THR B 136 ? ALA B 149 ? THR B 115 ALA B 128 1 ? 14 
HELX_P HELX_P16 AB7 ALA B 149 ? ARG B 162 ? ALA B 128 ARG B 141 1 ? 14 
HELX_P HELX_P17 AB8 PHE B 192 ? ALA B 214 ? PHE B 171 ALA B 193 1 ? 23 
HELX_P HELX_P18 AB9 PRO B 215 ? GLY B 217 ? PRO B 194 GLY B 196 5 ? 3  
HELX_P HELX_P19 AC1 GLY B 235 ? LYS B 245 ? GLY B 214 LYS B 224 1 ? 11 
HELX_P HELX_P20 AC2 SER B 254 ? SER B 267 ? SER B 233 SER B 246 1 ? 14 
HELX_P HELX_P21 AC3 GLY B 268 ? GLN B 271 ? GLY B 247 GLN B 250 5 ? 4  
HELX_P HELX_P22 AC4 GLY B 283 ? VAL B 287 ? GLY B 262 VAL B 266 5 ? 5  
HELX_P HELX_P23 AC5 LYS C 34  ? GLY C 48  ? LYS C 13  GLY C 27  1 ? 15 
HELX_P HELX_P24 AC6 SER C 58  ? ARG C 73  ? SER C 37  ARG C 52  1 ? 16 
HELX_P HELX_P25 AC7 VAL C 89  ? GLY C 106 ? VAL C 68  GLY C 85  1 ? 18 
HELX_P HELX_P26 AC8 THR C 136 ? ALA C 149 ? THR C 115 ALA C 128 1 ? 14 
HELX_P HELX_P27 AC9 ALA C 149 ? ARG C 162 ? ALA C 128 ARG C 141 1 ? 14 
HELX_P HELX_P28 AD1 PHE C 192 ? ALA C 214 ? PHE C 171 ALA C 193 1 ? 23 
HELX_P HELX_P29 AD2 PRO C 215 ? GLY C 217 ? PRO C 194 GLY C 196 5 ? 3  
HELX_P HELX_P30 AD3 GLY C 235 ? ARG C 244 ? GLY C 214 ARG C 223 1 ? 10 
HELX_P HELX_P31 AD4 SER C 254 ? SER C 267 ? SER C 233 SER C 246 1 ? 14 
HELX_P HELX_P32 AD5 GLY C 268 ? GLN C 271 ? GLY C 247 GLN C 250 5 ? 4  
HELX_P HELX_P33 AD6 GLY C 283 ? VAL C 287 ? GLY C 262 VAL C 266 5 ? 5  
HELX_P HELX_P34 AD7 LYS D 34  ? THR D 47  ? LYS D 13  THR D 26  1 ? 14 
HELX_P HELX_P35 AD8 SER D 58  ? ARG D 73  ? SER D 37  ARG D 52  1 ? 16 
HELX_P HELX_P36 AD9 VAL D 89  ? GLY D 106 ? VAL D 68  GLY D 85  1 ? 18 
HELX_P HELX_P37 AE1 THR D 136 ? ALA D 149 ? THR D 115 ALA D 128 1 ? 14 
HELX_P HELX_P38 AE2 ALA D 149 ? ARG D 162 ? ALA D 128 ARG D 141 1 ? 14 
HELX_P HELX_P39 AE3 PHE D 192 ? ALA D 214 ? PHE D 171 ALA D 193 1 ? 23 
HELX_P HELX_P40 AE4 GLY D 235 ? ARG D 244 ? GLY D 214 ARG D 223 1 ? 10 
HELX_P HELX_P41 AE5 SER D 254 ? SER D 267 ? SER D 233 SER D 246 1 ? 14 
HELX_P HELX_P42 AE6 GLY D 268 ? GLN D 271 ? GLY D 247 GLN D 250 5 ? 4  
HELX_P HELX_P43 AE7 GLY D 283 ? VAL D 287 ? GLY D 262 VAL D 266 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A PRO 188 C ? ? ? 1_555 A CSX 189 N ? ? A PRO 167 A CSX 168 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale2 covale both ? A CSX 189 C ? ? ? 1_555 A MET 190 N ? ? A CSX 168 A MET 169 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale3 covale both ? B PRO 188 C ? ? ? 1_555 B CSX 189 N ? ? B PRO 167 B CSX 168 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale4 covale both ? B CSX 189 C ? ? ? 1_555 B MET 190 N ? ? B CSX 168 B MET 169 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale5 covale both ? C PRO 188 C ? ? ? 1_555 C CSX 189 N ? ? C PRO 167 C CSX 168 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale6 covale both ? C CSX 189 C ? ? ? 1_555 C MET 190 N ? ? C CSX 168 C MET 169 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale7 covale both ? D PRO 188 C ? ? ? 1_555 D CSX 189 N ? ? D PRO 167 D CSX 168 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale8 covale both ? D CSX 189 C ? ? ? 1_555 D MET 190 N ? ? D CSX 168 D MET 169 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CSX A 189 ? . . . . CSX A 168 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
2 CSX B 189 ? . . . . CSX B 168 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
3 CSX C 189 ? . . . . CSX C 168 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
4 CSX D 189 ? . . . . CSX D 168 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA4 1 2 ? parallel 
AA4 2 3 ? parallel 
AA4 3 4 ? parallel 
AA4 4 5 ? parallel 
AA4 5 6 ? parallel 
AA4 6 7 ? 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 ALA A 77  ? GLN A 81  ? ALA A 56  GLN A 60  
AA1 2 ARG A 50  ? TYR A 55  ? ARG A 29  TYR A 34  
AA1 3 ALA A 26  ? VAL A 29  ? ALA A 5   VAL A 8   
AA1 4 VAL A 110 ? ASN A 113 ? VAL A 89  ASN A 92  
AA1 5 SER A 176 ? LEU A 180 ? SER A 155 LEU A 159 
AA1 6 ARG A 219 ? PRO A 225 ? ARG A 198 PRO A 204 
AA1 7 ILE A 277 ? VAL A 280 ? ILE A 256 VAL A 259 
AA2 1 ALA B 77  ? GLN B 81  ? ALA B 56  GLN B 60  
AA2 2 ARG B 50  ? TYR B 55  ? ARG B 29  TYR B 34  
AA2 3 ALA B 26  ? VAL B 29  ? ALA B 5   VAL B 8   
AA2 4 VAL B 110 ? ASN B 113 ? VAL B 89  ASN B 92  
AA2 5 SER B 176 ? LEU B 180 ? SER B 155 LEU B 159 
AA2 6 ARG B 219 ? PRO B 225 ? ARG B 198 PRO B 204 
AA2 7 ILE B 277 ? VAL B 280 ? ILE B 256 VAL B 259 
AA3 1 ALA C 77  ? GLN C 81  ? ALA C 56  GLN C 60  
AA3 2 ARG C 50  ? TYR C 55  ? ARG C 29  TYR C 34  
AA3 3 ALA C 26  ? VAL C 29  ? ALA C 5   VAL C 8   
AA3 4 VAL C 110 ? ASN C 113 ? VAL C 89  ASN C 92  
AA3 5 SER C 176 ? LEU C 180 ? SER C 155 LEU C 159 
AA3 6 ARG C 219 ? PRO C 225 ? ARG C 198 PRO C 204 
AA3 7 ILE C 277 ? VAL C 280 ? ILE C 256 VAL C 259 
AA4 1 ALA D 77  ? GLN D 81  ? ALA D 56  GLN D 60  
AA4 2 ARG D 50  ? TYR D 55  ? ARG D 29  TYR D 34  
AA4 3 ALA D 26  ? VAL D 29  ? ALA D 5   VAL D 8   
AA4 4 VAL D 110 ? ASN D 113 ? VAL D 89  ASN D 92  
AA4 5 LEU D 175 ? LEU D 180 ? LEU D 154 LEU D 159 
AA4 6 ILE D 218 ? PRO D 225 ? ILE D 197 PRO D 204 
AA4 7 ILE D 277 ? VAL D 280 ? ILE D 256 VAL D 259 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 78  ? O VAL A 57  N ILE A 53  ? N ILE A 32  
AA1 2 3 O VAL A 52  ? O VAL A 31  N ALA A 27  ? N ALA A 6   
AA1 3 4 N VAL A 28  ? N VAL A 7   O VAL A 112 ? O VAL A 91  
AA1 4 5 N ASN A 113 ? N ASN A 92  O LEU A 180 ? O LEU A 159 
AA1 5 6 N ASN A 179 ? N ASN A 158 O ASN A 221 ? O ASN A 200 
AA1 6 7 N ALA A 224 ? N ALA A 203 O ILE A 278 ? O ILE A 257 
AA2 1 2 O VAL B 78  ? O VAL B 57  N ILE B 53  ? N ILE B 32  
AA2 2 3 O ARG B 50  ? O ARG B 29  N ALA B 27  ? N ALA B 6   
AA2 3 4 N VAL B 28  ? N VAL B 7   O VAL B 112 ? O VAL B 91  
AA2 4 5 N ASN B 113 ? N ASN B 92  O LEU B 180 ? O LEU B 159 
AA2 5 6 N ASN B 179 ? N ASN B 158 O ASN B 221 ? O ASN B 200 
AA2 6 7 N ALA B 224 ? N ALA B 203 O VAL B 280 ? O VAL B 259 
AA3 1 2 O VAL C 78  ? O VAL C 57  N ILE C 53  ? N ILE C 32  
AA3 2 3 O VAL C 52  ? O VAL C 31  N ALA C 27  ? N ALA C 6   
AA3 3 4 N VAL C 28  ? N VAL C 7   O VAL C 112 ? O VAL C 91  
AA3 4 5 N ASN C 113 ? N ASN C 92  O LEU C 180 ? O LEU C 159 
AA3 5 6 N ASN C 179 ? N ASN C 158 O ASN C 221 ? O ASN C 200 
AA3 6 7 N ALA C 224 ? N ALA C 203 O ILE C 278 ? O ILE C 257 
AA4 1 2 O VAL D 78  ? O VAL D 57  N ILE D 53  ? N ILE D 32  
AA4 2 3 O ARG D 50  ? O ARG D 29  N ALA D 27  ? N ALA D 6   
AA4 3 4 N VAL D 28  ? N VAL D 7   O VAL D 112 ? O VAL D 91  
AA4 4 5 N ASN D 113 ? N ASN D 92  O LEU D 180 ? O LEU D 159 
AA4 5 6 N ILE D 177 ? N ILE D 156 O ASN D 221 ? O ASN D 200 
AA4 6 7 N GLY D 222 ? N GLY D 201 O ILE D 278 ? O ILE D 257 
# 
_pdbx_entry_details.entry_id                   8RHU 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 14  ? ? 59.02   -131.15 
2  1 HIS A 35  ? ? -111.29 -71.69  
3  1 ALA A 128 ? ? -141.08 -54.26  
4  1 CYS A 160 ? ? -102.48 -152.88 
5  1 SER A 207 ? ? -121.64 -139.35 
6  1 ARG B 14  ? ? 61.52   -132.52 
7  1 HIS B 35  ? ? -123.21 -68.77  
8  1 ALA B 128 ? ? -139.41 -57.62  
9  1 CYS B 160 ? ? -93.25  -155.05 
10 1 SER B 207 ? ? -117.76 -149.07 
11 1 ARG C 14  ? ? 53.49   -128.08 
12 1 ALA C 128 ? ? -138.54 -53.26  
13 1 CYS C 160 ? ? -98.97  -151.46 
14 1 SER C 207 ? ? -117.28 -146.86 
15 1 ARG D 14  ? ? 56.28   -128.10 
16 1 ALA D 128 ? ? -138.81 -57.08  
17 1 ASN D 153 ? ? -105.49 74.82   
18 1 CYS D 160 ? ? -101.16 -150.04 
19 1 PHE D 171 ? ? -109.94 43.00   
20 1 SER D 207 ? ? -114.97 -144.31 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSX 189 A CSX 168 ? CYS 'modified residue' 
2 B CSX 189 B CSX 168 ? CYS 'modified residue' 
3 C CSX 189 C CSX 168 ? CYS 'modified residue' 
4 D CSX 189 D CSX 168 ? CYS 'modified residue' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -20 ? A MET 1   
2   1 Y 1 A GLY -19 ? A GLY 2   
3   1 Y 1 A SER -18 ? A SER 3   
4   1 Y 1 A SER -17 ? A SER 4   
5   1 Y 1 A HIS -16 ? A HIS 5   
6   1 Y 1 A HIS -15 ? A HIS 6   
7   1 Y 1 A HIS -14 ? A HIS 7   
8   1 Y 1 A HIS -13 ? A HIS 8   
9   1 Y 1 A HIS -12 ? A HIS 9   
10  1 Y 1 A HIS -11 ? A HIS 10  
11  1 Y 1 A SER -10 ? A SER 11  
12  1 Y 1 A SER -9  ? A SER 12  
13  1 Y 1 A GLY -8  ? A GLY 13  
14  1 Y 1 A LEU -7  ? A LEU 14  
15  1 Y 1 A VAL -6  ? A VAL 15  
16  1 Y 1 A PRO -5  ? A PRO 16  
17  1 Y 1 A ARG -4  ? A ARG 17  
18  1 Y 1 A GLY -3  ? A GLY 18  
19  1 Y 1 A SER -2  ? A SER 19  
20  1 Y 1 A HIS -1  ? A HIS 20  
21  1 Y 1 A MET 0   ? A MET 21  
22  1 Y 1 A MET 1   ? A MET 22  
23  1 Y 1 A GLN 104 ? A GLN 125 
24  1 Y 1 A GLY 105 ? A GLY 126 
25  1 Y 1 A ASP 106 ? A ASP 127 
26  1 Y 1 A HIS 107 ? A HIS 128 
27  1 Y 1 A GLU 108 ? A GLU 129 
28  1 Y 1 A ASP 109 ? A ASP 130 
29  1 Y 1 A ASN 110 ? A ASN 131 
30  1 Y 1 A SER 111 ? A SER 132 
31  1 Y 1 A ASN 112 ? A ASN 133 
32  1 Y 1 A LYS 143 ? A LYS 164 
33  1 Y 1 A GLY 144 ? A GLY 165 
34  1 Y 1 A THR 145 ? A THR 166 
35  1 Y 1 A ASN 146 ? A ASN 167 
36  1 Y 1 A PRO 147 ? A PRO 168 
37  1 Y 1 A ASN 148 ? A ASN 169 
38  1 Y 1 A CYS 149 ? A CYS 170 
39  1 Y 1 A THR 150 ? A THR 171 
40  1 Y 1 A SER 151 ? A SER 172 
41  1 Y 1 B MET -20 ? B MET 1   
42  1 Y 1 B GLY -19 ? B GLY 2   
43  1 Y 1 B SER -18 ? B SER 3   
44  1 Y 1 B SER -17 ? B SER 4   
45  1 Y 1 B HIS -16 ? B HIS 5   
46  1 Y 1 B HIS -15 ? B HIS 6   
47  1 Y 1 B HIS -14 ? B HIS 7   
48  1 Y 1 B HIS -13 ? B HIS 8   
49  1 Y 1 B HIS -12 ? B HIS 9   
50  1 Y 1 B HIS -11 ? B HIS 10  
51  1 Y 1 B SER -10 ? B SER 11  
52  1 Y 1 B SER -9  ? B SER 12  
53  1 Y 1 B GLY -8  ? B GLY 13  
54  1 Y 1 B LEU -7  ? B LEU 14  
55  1 Y 1 B VAL -6  ? B VAL 15  
56  1 Y 1 B PRO -5  ? B PRO 16  
57  1 Y 1 B ARG -4  ? B ARG 17  
58  1 Y 1 B GLY -3  ? B GLY 18  
59  1 Y 1 B SER -2  ? B SER 19  
60  1 Y 1 B HIS -1  ? B HIS 20  
61  1 Y 1 B MET 0   ? B MET 21  
62  1 Y 1 B MET 1   ? B MET 22  
63  1 Y 1 B GLN 104 ? B GLN 125 
64  1 Y 1 B GLY 105 ? B GLY 126 
65  1 Y 1 B ASP 106 ? B ASP 127 
66  1 Y 1 B HIS 107 ? B HIS 128 
67  1 Y 1 B GLU 108 ? B GLU 129 
68  1 Y 1 B ASP 109 ? B ASP 130 
69  1 Y 1 B ASN 110 ? B ASN 131 
70  1 Y 1 B SER 111 ? B SER 132 
71  1 Y 1 B ASN 112 ? B ASN 133 
72  1 Y 1 B GLY 144 ? B GLY 165 
73  1 Y 1 B THR 145 ? B THR 166 
74  1 Y 1 B ASN 146 ? B ASN 167 
75  1 Y 1 B PRO 147 ? B PRO 168 
76  1 Y 1 B ASN 148 ? B ASN 169 
77  1 Y 1 B CYS 149 ? B CYS 170 
78  1 Y 1 B THR 150 ? B THR 171 
79  1 Y 1 B SER 151 ? B SER 172 
80  1 Y 1 C MET -20 ? C MET 1   
81  1 Y 1 C GLY -19 ? C GLY 2   
82  1 Y 1 C SER -18 ? C SER 3   
83  1 Y 1 C SER -17 ? C SER 4   
84  1 Y 1 C HIS -16 ? C HIS 5   
85  1 Y 1 C HIS -15 ? C HIS 6   
86  1 Y 1 C HIS -14 ? C HIS 7   
87  1 Y 1 C HIS -13 ? C HIS 8   
88  1 Y 1 C HIS -12 ? C HIS 9   
89  1 Y 1 C HIS -11 ? C HIS 10  
90  1 Y 1 C SER -10 ? C SER 11  
91  1 Y 1 C SER -9  ? C SER 12  
92  1 Y 1 C GLY -8  ? C GLY 13  
93  1 Y 1 C LEU -7  ? C LEU 14  
94  1 Y 1 C VAL -6  ? C VAL 15  
95  1 Y 1 C PRO -5  ? C PRO 16  
96  1 Y 1 C ARG -4  ? C ARG 17  
97  1 Y 1 C GLY -3  ? C GLY 18  
98  1 Y 1 C SER -2  ? C SER 19  
99  1 Y 1 C HIS -1  ? C HIS 20  
100 1 Y 1 C MET 0   ? C MET 21  
101 1 Y 1 C MET 1   ? C MET 22  
102 1 Y 1 C GLY 105 ? C GLY 126 
103 1 Y 1 C ASP 106 ? C ASP 127 
104 1 Y 1 C HIS 107 ? C HIS 128 
105 1 Y 1 C GLU 108 ? C GLU 129 
106 1 Y 1 C ASP 109 ? C ASP 130 
107 1 Y 1 C ASN 110 ? C ASN 131 
108 1 Y 1 C SER 111 ? C SER 132 
109 1 Y 1 C ASN 112 ? C ASN 133 
110 1 Y 1 C GLY 113 ? C GLY 134 
111 1 Y 1 C LYS 143 ? C LYS 164 
112 1 Y 1 C GLY 144 ? C GLY 165 
113 1 Y 1 C THR 145 ? C THR 166 
114 1 Y 1 C ASN 146 ? C ASN 167 
115 1 Y 1 C PRO 147 ? C PRO 168 
116 1 Y 1 C ASN 148 ? C ASN 169 
117 1 Y 1 C CYS 149 ? C CYS 170 
118 1 Y 1 C THR 150 ? C THR 171 
119 1 Y 1 C SER 151 ? C SER 172 
120 1 Y 1 D MET -20 ? D MET 1   
121 1 Y 1 D GLY -19 ? D GLY 2   
122 1 Y 1 D SER -18 ? D SER 3   
123 1 Y 1 D SER -17 ? D SER 4   
124 1 Y 1 D HIS -16 ? D HIS 5   
125 1 Y 1 D HIS -15 ? D HIS 6   
126 1 Y 1 D HIS -14 ? D HIS 7   
127 1 Y 1 D HIS -13 ? D HIS 8   
128 1 Y 1 D HIS -12 ? D HIS 9   
129 1 Y 1 D HIS -11 ? D HIS 10  
130 1 Y 1 D SER -10 ? D SER 11  
131 1 Y 1 D SER -9  ? D SER 12  
132 1 Y 1 D GLY -8  ? D GLY 13  
133 1 Y 1 D LEU -7  ? D LEU 14  
134 1 Y 1 D VAL -6  ? D VAL 15  
135 1 Y 1 D PRO -5  ? D PRO 16  
136 1 Y 1 D ARG -4  ? D ARG 17  
137 1 Y 1 D GLY -3  ? D GLY 18  
138 1 Y 1 D SER -2  ? D SER 19  
139 1 Y 1 D HIS -1  ? D HIS 20  
140 1 Y 1 D MET 0   ? D MET 21  
141 1 Y 1 D MET 1   ? D MET 22  
142 1 Y 1 D GLN 104 ? D GLN 125 
143 1 Y 1 D GLY 105 ? D GLY 126 
144 1 Y 1 D ASP 106 ? D ASP 127 
145 1 Y 1 D HIS 107 ? D HIS 128 
146 1 Y 1 D GLU 108 ? D GLU 129 
147 1 Y 1 D ASP 109 ? D ASP 130 
148 1 Y 1 D ASN 110 ? D ASN 131 
149 1 Y 1 D SER 111 ? D SER 132 
150 1 Y 1 D ASN 112 ? D ASN 133 
151 1 Y 1 D LYS 143 ? D LYS 164 
152 1 Y 1 D GLY 144 ? D GLY 165 
153 1 Y 1 D THR 145 ? D THR 166 
154 1 Y 1 D ASN 146 ? D ASN 167 
155 1 Y 1 D PRO 147 ? D PRO 168 
156 1 Y 1 D ASN 148 ? D ASN 169 
157 1 Y 1 D CYS 149 ? D CYS 170 
158 1 Y 1 D THR 150 ? D THR 171 
159 1 Y 1 D SER 151 ? D SER 172 
# 
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 
A1H0S CAC  C Y N 1   
A1H0S CAE  C Y N 2   
A1H0S CAG  C N N 3   
A1H0S CAJ  C N N 4   
A1H0S CAO  C N N 5   
A1H0S CAP  C Y N 6   
A1H0S CAD  C Y N 7   
A1H0S NAF  N N N 8   
A1H0S CAL  C N N 9   
A1H0S CAM  C N N 10  
A1H0S CAN  C N N 11  
A1H0S NAQ  N N N 12  
A1H0S NAK  N N N 13  
A1H0S NAI  N N N 14  
A1H0S NAH  N N N 15  
A1H0S CAA  C Y N 16  
A1H0S CAB  C Y N 17  
A1H0S CAR  C N N 18  
A1H0S H2   H N N 19  
A1H0S H3   H N N 20  
A1H0S H4   H N N 21  
A1H0S H5   H N N 22  
A1H0S H6   H N N 23  
A1H0S H7   H N N 24  
A1H0S H8   H N N 25  
A1H0S H9   H N N 26  
A1H0S H10  H N N 27  
A1H0S H11  H N N 28  
A1H0S H13  H N N 29  
A1H0S H14  H N N 30  
A1H0S H15  H N N 31  
A1H0S H16  H N N 32  
A1H0S H17  H N N 33  
A1H0S H18  H N N 34  
A1H0S H19  H N N 35  
ACT   C    C N N 36  
ACT   O    O N N 37  
ACT   OXT  O N N 38  
ACT   CH3  C N N 39  
ACT   H1   H N N 40  
ACT   H2   H N N 41  
ACT   H3   H N N 42  
ALA   N    N N N 43  
ALA   CA   C N S 44  
ALA   C    C N N 45  
ALA   O    O N N 46  
ALA   CB   C N N 47  
ALA   OXT  O N N 48  
ALA   H    H N N 49  
ALA   H2   H N N 50  
ALA   HA   H N N 51  
ALA   HB1  H N N 52  
ALA   HB2  H N N 53  
ALA   HB3  H N N 54  
ALA   HXT  H N N 55  
ARG   N    N N N 56  
ARG   CA   C N S 57  
ARG   C    C N N 58  
ARG   O    O N N 59  
ARG   CB   C N N 60  
ARG   CG   C N N 61  
ARG   CD   C N N 62  
ARG   NE   N N N 63  
ARG   CZ   C N N 64  
ARG   NH1  N N N 65  
ARG   NH2  N N N 66  
ARG   OXT  O N N 67  
ARG   H    H N N 68  
ARG   H2   H N N 69  
ARG   HA   H N N 70  
ARG   HB2  H N N 71  
ARG   HB3  H N N 72  
ARG   HG2  H N N 73  
ARG   HG3  H N N 74  
ARG   HD2  H N N 75  
ARG   HD3  H N N 76  
ARG   HE   H N N 77  
ARG   HH11 H N N 78  
ARG   HH12 H N N 79  
ARG   HH21 H N N 80  
ARG   HH22 H N N 81  
ARG   HXT  H N N 82  
ASN   N    N N N 83  
ASN   CA   C N S 84  
ASN   C    C N N 85  
ASN   O    O N N 86  
ASN   CB   C N N 87  
ASN   CG   C N N 88  
ASN   OD1  O N N 89  
ASN   ND2  N N N 90  
ASN   OXT  O N N 91  
ASN   H    H N N 92  
ASN   H2   H N N 93  
ASN   HA   H N N 94  
ASN   HB2  H N N 95  
ASN   HB3  H N N 96  
ASN   HD21 H N N 97  
ASN   HD22 H N N 98  
ASN   HXT  H N N 99  
ASP   N    N N N 100 
ASP   CA   C N S 101 
ASP   C    C N N 102 
ASP   O    O N N 103 
ASP   CB   C N N 104 
ASP   CG   C N N 105 
ASP   OD1  O N N 106 
ASP   OD2  O N N 107 
ASP   OXT  O N N 108 
ASP   H    H N N 109 
ASP   H2   H N N 110 
ASP   HA   H N N 111 
ASP   HB2  H N N 112 
ASP   HB3  H N N 113 
ASP   HD2  H N N 114 
ASP   HXT  H N N 115 
CSX   N    N N N 116 
CSX   CA   C N R 117 
CSX   CB   C N N 118 
CSX   SG   S N S 119 
CSX   C    C N N 120 
CSX   O    O N N 121 
CSX   OXT  O N N 122 
CSX   OD   O N N 123 
CSX   H    H N N 124 
CSX   H2   H N N 125 
CSX   HA   H N N 126 
CSX   HB2  H N N 127 
CSX   HB3  H N N 128 
CSX   HG   H N N 129 
CSX   HXT  H N N 130 
CYS   N    N N N 131 
CYS   CA   C N R 132 
CYS   C    C N N 133 
CYS   O    O N N 134 
CYS   CB   C N N 135 
CYS   SG   S N N 136 
CYS   OXT  O N N 137 
CYS   H    H N N 138 
CYS   H2   H N N 139 
CYS   HA   H N N 140 
CYS   HB2  H N N 141 
CYS   HB3  H N N 142 
CYS   HG   H N N 143 
CYS   HXT  H N N 144 
GLN   N    N N N 145 
GLN   CA   C N S 146 
GLN   C    C N N 147 
GLN   O    O N N 148 
GLN   CB   C N N 149 
GLN   CG   C N N 150 
GLN   CD   C N N 151 
GLN   OE1  O N N 152 
GLN   NE2  N N N 153 
GLN   OXT  O N N 154 
GLN   H    H N N 155 
GLN   H2   H N N 156 
GLN   HA   H N N 157 
GLN   HB2  H N N 158 
GLN   HB3  H N N 159 
GLN   HG2  H N N 160 
GLN   HG3  H N N 161 
GLN   HE21 H N N 162 
GLN   HE22 H N N 163 
GLN   HXT  H N N 164 
GLU   N    N N N 165 
GLU   CA   C N S 166 
GLU   C    C N N 167 
GLU   O    O N N 168 
GLU   CB   C N N 169 
GLU   CG   C N N 170 
GLU   CD   C N N 171 
GLU   OE1  O N N 172 
GLU   OE2  O N N 173 
GLU   OXT  O N N 174 
GLU   H    H N N 175 
GLU   H2   H N N 176 
GLU   HA   H N N 177 
GLU   HB2  H N N 178 
GLU   HB3  H N N 179 
GLU   HG2  H N N 180 
GLU   HG3  H N N 181 
GLU   HE2  H N N 182 
GLU   HXT  H N N 183 
GLY   N    N N N 184 
GLY   CA   C N N 185 
GLY   C    C N N 186 
GLY   O    O N N 187 
GLY   OXT  O N N 188 
GLY   H    H N N 189 
GLY   H2   H N N 190 
GLY   HA2  H N N 191 
GLY   HA3  H N N 192 
GLY   HXT  H N N 193 
HIS   N    N N N 194 
HIS   CA   C N S 195 
HIS   C    C N N 196 
HIS   O    O N N 197 
HIS   CB   C N N 198 
HIS   CG   C Y N 199 
HIS   ND1  N Y N 200 
HIS   CD2  C Y N 201 
HIS   CE1  C Y N 202 
HIS   NE2  N Y N 203 
HIS   OXT  O N N 204 
HIS   H    H N N 205 
HIS   H2   H N N 206 
HIS   HA   H N N 207 
HIS   HB2  H N N 208 
HIS   HB3  H N N 209 
HIS   HD1  H N N 210 
HIS   HD2  H N N 211 
HIS   HE1  H N N 212 
HIS   HE2  H N N 213 
HIS   HXT  H N N 214 
HOH   O    O N N 215 
HOH   H1   H N N 216 
HOH   H2   H N N 217 
ILE   N    N N N 218 
ILE   CA   C N S 219 
ILE   C    C N N 220 
ILE   O    O N N 221 
ILE   CB   C N S 222 
ILE   CG1  C N N 223 
ILE   CG2  C N N 224 
ILE   CD1  C N N 225 
ILE   OXT  O N N 226 
ILE   H    H N N 227 
ILE   H2   H N N 228 
ILE   HA   H N N 229 
ILE   HB   H N N 230 
ILE   HG12 H N N 231 
ILE   HG13 H N N 232 
ILE   HG21 H N N 233 
ILE   HG22 H N N 234 
ILE   HG23 H N N 235 
ILE   HD11 H N N 236 
ILE   HD12 H N N 237 
ILE   HD13 H N N 238 
ILE   HXT  H N N 239 
LEU   N    N N N 240 
LEU   CA   C N S 241 
LEU   C    C N N 242 
LEU   O    O N N 243 
LEU   CB   C N N 244 
LEU   CG   C N N 245 
LEU   CD1  C N N 246 
LEU   CD2  C N N 247 
LEU   OXT  O N N 248 
LEU   H    H N N 249 
LEU   H2   H N N 250 
LEU   HA   H N N 251 
LEU   HB2  H N N 252 
LEU   HB3  H N N 253 
LEU   HG   H N N 254 
LEU   HD11 H N N 255 
LEU   HD12 H N N 256 
LEU   HD13 H N N 257 
LEU   HD21 H N N 258 
LEU   HD22 H N N 259 
LEU   HD23 H N N 260 
LEU   HXT  H N N 261 
LYS   N    N N N 262 
LYS   CA   C N S 263 
LYS   C    C N N 264 
LYS   O    O N N 265 
LYS   CB   C N N 266 
LYS   CG   C N N 267 
LYS   CD   C N N 268 
LYS   CE   C N N 269 
LYS   NZ   N N N 270 
LYS   OXT  O N N 271 
LYS   H    H N N 272 
LYS   H2   H N N 273 
LYS   HA   H N N 274 
LYS   HB2  H N N 275 
LYS   HB3  H N N 276 
LYS   HG2  H N N 277 
LYS   HG3  H N N 278 
LYS   HD2  H N N 279 
LYS   HD3  H N N 280 
LYS   HE2  H N N 281 
LYS   HE3  H N N 282 
LYS   HZ1  H N N 283 
LYS   HZ2  H N N 284 
LYS   HZ3  H N N 285 
LYS   HXT  H N N 286 
MET   N    N N N 287 
MET   CA   C N S 288 
MET   C    C N N 289 
MET   O    O N N 290 
MET   CB   C N N 291 
MET   CG   C N N 292 
MET   SD   S N N 293 
MET   CE   C N N 294 
MET   OXT  O N N 295 
MET   H    H N N 296 
MET   H2   H N N 297 
MET   HA   H N N 298 
MET   HB2  H N N 299 
MET   HB3  H N N 300 
MET   HG2  H N N 301 
MET   HG3  H N N 302 
MET   HE1  H N N 303 
MET   HE2  H N N 304 
MET   HE3  H N N 305 
MET   HXT  H N N 306 
NDP   PA   P N S 307 
NDP   O1A  O N N 308 
NDP   O2A  O N N 309 
NDP   O5B  O N N 310 
NDP   C5B  C N N 311 
NDP   C4B  C N R 312 
NDP   O4B  O N N 313 
NDP   C3B  C N R 314 
NDP   O3B  O N N 315 
NDP   C2B  C N R 316 
NDP   O2B  O N N 317 
NDP   C1B  C N R 318 
NDP   N9A  N Y N 319 
NDP   C8A  C Y N 320 
NDP   N7A  N Y N 321 
NDP   C5A  C Y N 322 
NDP   C6A  C Y N 323 
NDP   N6A  N N N 324 
NDP   N1A  N Y N 325 
NDP   C2A  C Y N 326 
NDP   N3A  N Y N 327 
NDP   C4A  C Y N 328 
NDP   O3   O N N 329 
NDP   PN   P N S 330 
NDP   O1N  O N N 331 
NDP   O2N  O N N 332 
NDP   O5D  O N N 333 
NDP   C5D  C N N 334 
NDP   C4D  C N R 335 
NDP   O4D  O N N 336 
NDP   C3D  C N S 337 
NDP   O3D  O N N 338 
NDP   C2D  C N R 339 
NDP   O2D  O N N 340 
NDP   C1D  C N R 341 
NDP   N1N  N N N 342 
NDP   C2N  C N N 343 
NDP   C3N  C N N 344 
NDP   C7N  C N N 345 
NDP   O7N  O N N 346 
NDP   N7N  N N N 347 
NDP   C4N  C N N 348 
NDP   C5N  C N N 349 
NDP   C6N  C N N 350 
NDP   P2B  P N N 351 
NDP   O1X  O N N 352 
NDP   O2X  O N N 353 
NDP   O3X  O N N 354 
NDP   HOA2 H N N 355 
NDP   H51A H N N 356 
NDP   H52A H N N 357 
NDP   H4B  H N N 358 
NDP   H3B  H N N 359 
NDP   HO3A H N N 360 
NDP   H2B  H N N 361 
NDP   H1B  H N N 362 
NDP   H8A  H N N 363 
NDP   H61A H N N 364 
NDP   H62A H N N 365 
NDP   H2A  H N N 366 
NDP   H21N H N N 367 
NDP   H51N H N N 368 
NDP   H52N H N N 369 
NDP   H4D  H N N 370 
NDP   H3D  H N N 371 
NDP   HO3N H N N 372 
NDP   H2D  H N N 373 
NDP   HO2N H N N 374 
NDP   H1D  H N N 375 
NDP   H2N  H N N 376 
NDP   H71N H N N 377 
NDP   H72N H N N 378 
NDP   H41N H N N 379 
NDP   H42N H N N 380 
NDP   H5N  H N N 381 
NDP   H6N  H N N 382 
NDP   HOP2 H N N 383 
NDP   HOP3 H N N 384 
PHE   N    N N N 385 
PHE   CA   C N S 386 
PHE   C    C N N 387 
PHE   O    O N N 388 
PHE   CB   C N N 389 
PHE   CG   C Y N 390 
PHE   CD1  C Y N 391 
PHE   CD2  C Y N 392 
PHE   CE1  C Y N 393 
PHE   CE2  C Y N 394 
PHE   CZ   C Y N 395 
PHE   OXT  O N N 396 
PHE   H    H N N 397 
PHE   H2   H N N 398 
PHE   HA   H N N 399 
PHE   HB2  H N N 400 
PHE   HB3  H N N 401 
PHE   HD1  H N N 402 
PHE   HD2  H N N 403 
PHE   HE1  H N N 404 
PHE   HE2  H N N 405 
PHE   HZ   H N N 406 
PHE   HXT  H N N 407 
PRO   N    N N N 408 
PRO   CA   C N S 409 
PRO   C    C N N 410 
PRO   O    O N N 411 
PRO   CB   C N N 412 
PRO   CG   C N N 413 
PRO   CD   C N N 414 
PRO   OXT  O N N 415 
PRO   H    H N N 416 
PRO   HA   H N N 417 
PRO   HB2  H N N 418 
PRO   HB3  H N N 419 
PRO   HG2  H N N 420 
PRO   HG3  H N N 421 
PRO   HD2  H N N 422 
PRO   HD3  H N N 423 
PRO   HXT  H N N 424 
SER   N    N N N 425 
SER   CA   C N S 426 
SER   C    C N N 427 
SER   O    O N N 428 
SER   CB   C N N 429 
SER   OG   O N N 430 
SER   OXT  O N N 431 
SER   H    H N N 432 
SER   H2   H N N 433 
SER   HA   H N N 434 
SER   HB2  H N N 435 
SER   HB3  H N N 436 
SER   HG   H N N 437 
SER   HXT  H N N 438 
THR   N    N N N 439 
THR   CA   C N S 440 
THR   C    C N N 441 
THR   O    O N N 442 
THR   CB   C N R 443 
THR   OG1  O N N 444 
THR   CG2  C N N 445 
THR   OXT  O N N 446 
THR   H    H N N 447 
THR   H2   H N N 448 
THR   HA   H N N 449 
THR   HB   H N N 450 
THR   HG1  H N N 451 
THR   HG21 H N N 452 
THR   HG22 H N N 453 
THR   HG23 H N N 454 
THR   HXT  H N N 455 
TRP   N    N N N 456 
TRP   CA   C N S 457 
TRP   C    C N N 458 
TRP   O    O N N 459 
TRP   CB   C N N 460 
TRP   CG   C Y N 461 
TRP   CD1  C Y N 462 
TRP   CD2  C Y N 463 
TRP   NE1  N Y N 464 
TRP   CE2  C Y N 465 
TRP   CE3  C Y N 466 
TRP   CZ2  C Y N 467 
TRP   CZ3  C Y N 468 
TRP   CH2  C Y N 469 
TRP   OXT  O N N 470 
TRP   H    H N N 471 
TRP   H2   H N N 472 
TRP   HA   H N N 473 
TRP   HB2  H N N 474 
TRP   HB3  H N N 475 
TRP   HD1  H N N 476 
TRP   HE1  H N N 477 
TRP   HE3  H N N 478 
TRP   HZ2  H N N 479 
TRP   HZ3  H N N 480 
TRP   HH2  H N N 481 
TRP   HXT  H N N 482 
TYR   N    N N N 483 
TYR   CA   C N S 484 
TYR   C    C N N 485 
TYR   O    O N N 486 
TYR   CB   C N N 487 
TYR   CG   C Y N 488 
TYR   CD1  C Y N 489 
TYR   CD2  C Y N 490 
TYR   CE1  C Y N 491 
TYR   CE2  C Y N 492 
TYR   CZ   C Y N 493 
TYR   OH   O N N 494 
TYR   OXT  O N N 495 
TYR   H    H N N 496 
TYR   H2   H N N 497 
TYR   HA   H N N 498 
TYR   HB2  H N N 499 
TYR   HB3  H N N 500 
TYR   HD1  H N N 501 
TYR   HD2  H N N 502 
TYR   HE1  H N N 503 
TYR   HE2  H N N 504 
TYR   HH   H N N 505 
TYR   HXT  H N N 506 
VAL   N    N N N 507 
VAL   CA   C N S 508 
VAL   C    C N N 509 
VAL   O    O N N 510 
VAL   CB   C N N 511 
VAL   CG1  C N N 512 
VAL   CG2  C N N 513 
VAL   OXT  O N N 514 
VAL   H    H N N 515 
VAL   H2   H N N 516 
VAL   HA   H N N 517 
VAL   HB   H N N 518 
VAL   HG11 H N N 519 
VAL   HG12 H N N 520 
VAL   HG13 H N N 521 
VAL   HG21 H N N 522 
VAL   HG22 H N N 523 
VAL   HG23 H N N 524 
VAL   HXT  H N N 525 
# 
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 
A1H0S CAR CAB  sing N N 1   
A1H0S CAB CAA  doub Y N 2   
A1H0S CAB CAC  sing Y N 3   
A1H0S CAA CAE  sing Y N 4   
A1H0S CAO CAC  sing N N 5   
A1H0S CAC CAP  doub Y N 6   
A1H0S CAE NAH  sing N N 7   
A1H0S CAE CAD  doub Y N 8   
A1H0S NAH CAG  sing N N 9   
A1H0S CAP CAD  sing Y N 10  
A1H0S CAD NAF  sing N N 11  
A1H0S CAG NAF  sing N N 12  
A1H0S CAG NAI  doub N N 13  
A1H0S NAF CAL  sing N N 14  
A1H0S NAI CAJ  sing N N 15  
A1H0S CAM CAL  sing N N 16  
A1H0S CAL NAQ  sing N N 17  
A1H0S CAL CAN  sing N N 18  
A1H0S CAJ NAQ  doub N N 19  
A1H0S CAJ NAK  sing N N 20  
A1H0S CAO H2   sing N N 21  
A1H0S CAO H3   sing N N 22  
A1H0S CAO H4   sing N N 23  
A1H0S CAP H5   sing N N 24  
A1H0S CAM H6   sing N N 25  
A1H0S CAM H7   sing N N 26  
A1H0S CAM H8   sing N N 27  
A1H0S CAN H9   sing N N 28  
A1H0S CAN H10  sing N N 29  
A1H0S CAN H11  sing N N 30  
A1H0S NAK H13  sing N N 31  
A1H0S NAK H14  sing N N 32  
A1H0S NAH H15  sing N N 33  
A1H0S CAA H16  sing N N 34  
A1H0S CAR H17  sing N N 35  
A1H0S CAR H18  sing N N 36  
A1H0S CAR H19  sing N N 37  
ACT   C   O    doub N N 38  
ACT   C   OXT  sing N N 39  
ACT   C   CH3  sing N N 40  
ACT   CH3 H1   sing N N 41  
ACT   CH3 H2   sing N N 42  
ACT   CH3 H3   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CSX   N   CA   sing N N 113 
CSX   N   H    sing N N 114 
CSX   N   H2   sing N N 115 
CSX   CA  CB   sing N N 116 
CSX   CA  C    sing N N 117 
CSX   CA  HA   sing N N 118 
CSX   CB  SG   sing N N 119 
CSX   CB  HB2  sing N N 120 
CSX   CB  HB3  sing N N 121 
CSX   SG  OD   doub N N 122 
CSX   SG  HG   sing N N 123 
CSX   C   O    doub N N 124 
CSX   C   OXT  sing N N 125 
CSX   OXT HXT  sing N N 126 
CYS   N   CA   sing N N 127 
CYS   N   H    sing N N 128 
CYS   N   H2   sing N N 129 
CYS   CA  C    sing N N 130 
CYS   CA  CB   sing N N 131 
CYS   CA  HA   sing N N 132 
CYS   C   O    doub N N 133 
CYS   C   OXT  sing N N 134 
CYS   CB  SG   sing N N 135 
CYS   CB  HB2  sing N N 136 
CYS   CB  HB3  sing N N 137 
CYS   SG  HG   sing N N 138 
CYS   OXT HXT  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
NDP   PA  O1A  doub N N 294 
NDP   PA  O2A  sing N N 295 
NDP   PA  O5B  sing N N 296 
NDP   PA  O3   sing N N 297 
NDP   O2A HOA2 sing N N 298 
NDP   O5B C5B  sing N N 299 
NDP   C5B C4B  sing N N 300 
NDP   C5B H51A sing N N 301 
NDP   C5B H52A sing N N 302 
NDP   C4B O4B  sing N N 303 
NDP   C4B C3B  sing N N 304 
NDP   C4B H4B  sing N N 305 
NDP   O4B C1B  sing N N 306 
NDP   C3B O3B  sing N N 307 
NDP   C3B C2B  sing N N 308 
NDP   C3B H3B  sing N N 309 
NDP   O3B HO3A sing N N 310 
NDP   C2B O2B  sing N N 311 
NDP   C2B C1B  sing N N 312 
NDP   C2B H2B  sing N N 313 
NDP   O2B P2B  sing N N 314 
NDP   C1B N9A  sing N N 315 
NDP   C1B H1B  sing N N 316 
NDP   N9A C8A  sing Y N 317 
NDP   N9A C4A  sing Y N 318 
NDP   C8A N7A  doub Y N 319 
NDP   C8A H8A  sing N N 320 
NDP   N7A C5A  sing Y N 321 
NDP   C5A C6A  sing Y N 322 
NDP   C5A C4A  doub Y N 323 
NDP   C6A N6A  sing N N 324 
NDP   C6A N1A  doub Y N 325 
NDP   N6A H61A sing N N 326 
NDP   N6A H62A sing N N 327 
NDP   N1A C2A  sing Y N 328 
NDP   C2A N3A  doub Y N 329 
NDP   C2A H2A  sing N N 330 
NDP   N3A C4A  sing Y N 331 
NDP   O3  PN   sing N N 332 
NDP   PN  O1N  doub N N 333 
NDP   PN  O2N  sing N N 334 
NDP   PN  O5D  sing N N 335 
NDP   O2N H21N sing N N 336 
NDP   O5D C5D  sing N N 337 
NDP   C5D C4D  sing N N 338 
NDP   C5D H51N sing N N 339 
NDP   C5D H52N sing N N 340 
NDP   C4D O4D  sing N N 341 
NDP   C4D C3D  sing N N 342 
NDP   C4D H4D  sing N N 343 
NDP   O4D C1D  sing N N 344 
NDP   C3D O3D  sing N N 345 
NDP   C3D C2D  sing N N 346 
NDP   C3D H3D  sing N N 347 
NDP   O3D HO3N sing N N 348 
NDP   C2D O2D  sing N N 349 
NDP   C2D C1D  sing N N 350 
NDP   C2D H2D  sing N N 351 
NDP   O2D HO2N sing N N 352 
NDP   C1D N1N  sing N N 353 
NDP   C1D H1D  sing N N 354 
NDP   N1N C2N  sing N N 355 
NDP   N1N C6N  sing N N 356 
NDP   C2N C3N  doub N N 357 
NDP   C2N H2N  sing N N 358 
NDP   C3N C7N  sing N N 359 
NDP   C3N C4N  sing N N 360 
NDP   C7N O7N  doub N N 361 
NDP   C7N N7N  sing N N 362 
NDP   N7N H71N sing N N 363 
NDP   N7N H72N sing N N 364 
NDP   C4N C5N  sing N N 365 
NDP   C4N H41N sing N N 366 
NDP   C4N H42N sing N N 367 
NDP   C5N C6N  doub N N 368 
NDP   C5N H5N  sing N N 369 
NDP   C6N H6N  sing N N 370 
NDP   P2B O1X  doub N N 371 
NDP   P2B O2X  sing N N 372 
NDP   P2B O3X  sing N N 373 
NDP   O2X HOP2 sing N N 374 
NDP   O3X HOP3 sing N N 375 
PHE   N   CA   sing N N 376 
PHE   N   H    sing N N 377 
PHE   N   H2   sing N N 378 
PHE   CA  C    sing N N 379 
PHE   CA  CB   sing N N 380 
PHE   CA  HA   sing N N 381 
PHE   C   O    doub N N 382 
PHE   C   OXT  sing N N 383 
PHE   CB  CG   sing N N 384 
PHE   CB  HB2  sing N N 385 
PHE   CB  HB3  sing N N 386 
PHE   CG  CD1  doub Y N 387 
PHE   CG  CD2  sing Y N 388 
PHE   CD1 CE1  sing Y N 389 
PHE   CD1 HD1  sing N N 390 
PHE   CD2 CE2  doub Y N 391 
PHE   CD2 HD2  sing N N 392 
PHE   CE1 CZ   doub Y N 393 
PHE   CE1 HE1  sing N N 394 
PHE   CE2 CZ   sing Y N 395 
PHE   CE2 HE2  sing N N 396 
PHE   CZ  HZ   sing N N 397 
PHE   OXT HXT  sing N N 398 
PRO   N   CA   sing N N 399 
PRO   N   CD   sing N N 400 
PRO   N   H    sing N N 401 
PRO   CA  C    sing N N 402 
PRO   CA  CB   sing N N 403 
PRO   CA  HA   sing N N 404 
PRO   C   O    doub N N 405 
PRO   C   OXT  sing N N 406 
PRO   CB  CG   sing N N 407 
PRO   CB  HB2  sing N N 408 
PRO   CB  HB3  sing N N 409 
PRO   CG  CD   sing N N 410 
PRO   CG  HG2  sing N N 411 
PRO   CG  HG3  sing N N 412 
PRO   CD  HD2  sing N N 413 
PRO   CD  HD3  sing N N 414 
PRO   OXT HXT  sing N N 415 
SER   N   CA   sing N N 416 
SER   N   H    sing N N 417 
SER   N   H2   sing N N 418 
SER   CA  C    sing N N 419 
SER   CA  CB   sing N N 420 
SER   CA  HA   sing N N 421 
SER   C   O    doub N N 422 
SER   C   OXT  sing N N 423 
SER   CB  OG   sing N N 424 
SER   CB  HB2  sing N N 425 
SER   CB  HB3  sing N N 426 
SER   OG  HG   sing N N 427 
SER   OXT HXT  sing N N 428 
THR   N   CA   sing N N 429 
THR   N   H    sing N N 430 
THR   N   H2   sing N N 431 
THR   CA  C    sing N N 432 
THR   CA  CB   sing N N 433 
THR   CA  HA   sing N N 434 
THR   C   O    doub N N 435 
THR   C   OXT  sing N N 436 
THR   CB  OG1  sing N N 437 
THR   CB  CG2  sing N N 438 
THR   CB  HB   sing N N 439 
THR   OG1 HG1  sing N N 440 
THR   CG2 HG21 sing N N 441 
THR   CG2 HG22 sing N N 442 
THR   CG2 HG23 sing N N 443 
THR   OXT HXT  sing N N 444 
TRP   N   CA   sing N N 445 
TRP   N   H    sing N N 446 
TRP   N   H2   sing N N 447 
TRP   CA  C    sing N N 448 
TRP   CA  CB   sing N N 449 
TRP   CA  HA   sing N N 450 
TRP   C   O    doub N N 451 
TRP   C   OXT  sing N N 452 
TRP   CB  CG   sing N N 453 
TRP   CB  HB2  sing N N 454 
TRP   CB  HB3  sing N N 455 
TRP   CG  CD1  doub Y N 456 
TRP   CG  CD2  sing Y N 457 
TRP   CD1 NE1  sing Y N 458 
TRP   CD1 HD1  sing N N 459 
TRP   CD2 CE2  doub Y N 460 
TRP   CD2 CE3  sing Y N 461 
TRP   NE1 CE2  sing Y N 462 
TRP   NE1 HE1  sing N N 463 
TRP   CE2 CZ2  sing Y N 464 
TRP   CE3 CZ3  doub Y N 465 
TRP   CE3 HE3  sing N N 466 
TRP   CZ2 CH2  doub Y N 467 
TRP   CZ2 HZ2  sing N N 468 
TRP   CZ3 CH2  sing Y N 469 
TRP   CZ3 HZ3  sing N N 470 
TRP   CH2 HH2  sing N N 471 
TRP   OXT HXT  sing N N 472 
TYR   N   CA   sing N N 473 
TYR   N   H    sing N N 474 
TYR   N   H2   sing N N 475 
TYR   CA  C    sing N N 476 
TYR   CA  CB   sing N N 477 
TYR   CA  HA   sing N N 478 
TYR   C   O    doub N N 479 
TYR   C   OXT  sing N N 480 
TYR   CB  CG   sing N N 481 
TYR   CB  HB2  sing N N 482 
TYR   CB  HB3  sing N N 483 
TYR   CG  CD1  doub Y N 484 
TYR   CG  CD2  sing Y N 485 
TYR   CD1 CE1  sing Y N 486 
TYR   CD1 HD1  sing N N 487 
TYR   CD2 CE2  doub Y N 488 
TYR   CD2 HD2  sing N N 489 
TYR   CE1 CZ   doub Y N 490 
TYR   CE1 HE1  sing N N 491 
TYR   CE2 CZ   sing Y N 492 
TYR   CE2 HE2  sing N N 493 
TYR   CZ  OH   sing N N 494 
TYR   OH  HH   sing N N 495 
TYR   OXT HXT  sing N N 496 
VAL   N   CA   sing N N 497 
VAL   N   H    sing N N 498 
VAL   N   H2   sing N N 499 
VAL   CA  C    sing N N 500 
VAL   CA  CB   sing N N 501 
VAL   CA  HA   sing N N 502 
VAL   C   O    doub N N 503 
VAL   C   OXT  sing N N 504 
VAL   CB  CG1  sing N N 505 
VAL   CB  CG2  sing N N 506 
VAL   CB  HB   sing N N 507 
VAL   CG1 HG11 sing N N 508 
VAL   CG1 HG12 sing N N 509 
VAL   CG1 HG13 sing N N 510 
VAL   CG2 HG21 sing N N 511 
VAL   CG2 HG22 sing N N 512 
VAL   CG2 HG23 sing N N 513 
VAL   OXT HXT  sing N N 514 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           CA21111 
_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   6TBX 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RHU 
_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]   0.013508 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006553 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011155 
_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]   0.013206 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
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   . GLU   A 1 23  ? 18.503  9.252   -11.704 0.80 54.19 ? 2   GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 23  ? 19.310  8.454   -10.740 0.80 53.87 ? 2   GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 23  ? 18.387  7.836   -9.690  0.80 46.57 ? 2   GLU   A C   1 
ATOM   4    O O   . GLU   A 1 23  ? 17.402  8.440   -9.276  0.80 46.57 ? 2   GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 23  ? 20.368  9.305   -10.043 0.80 57.61 ? 2   GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 23  ? 19.825  9.961   -8.783  0.80 57.73 ? 2   GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 23  ? 20.888  10.367  -7.792  0.80 63.19 ? 2   GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 23  ? 21.927  9.678   -7.698  0.80 70.71 ? 2   GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 23  ? 20.628  11.358  -7.081  0.80 57.87 ? 2   GLU   A OE2 1 
ATOM   10   N N   . ALA   A 1 24  ? 18.733  6.627   -9.247  1.00 42.38 ? 3   ALA   A N   1 
ATOM   11   C CA  . ALA   A 1 24  ? 17.783  5.775   -8.554  1.00 35.44 ? 3   ALA   A CA  1 
ATOM   12   C C   . ALA   A 1 24  ? 17.687  6.168   -7.076  1.00 38.56 ? 3   ALA   A C   1 
ATOM   13   O O   . ALA   A 1 24  ? 18.669  6.576   -6.474  1.00 36.05 ? 3   ALA   A O   1 
ATOM   14   C CB  . ALA   A 1 24  ? 18.170  4.325   -8.744  1.00 31.43 ? 3   ALA   A CB  1 
ATOM   15   N N   . PRO   A 1 25  ? 16.495  6.095   -6.437  1.00 34.30 ? 4   PRO   A N   1 
ATOM   16   C CA  . PRO   A 1 25  ? 16.419  6.302   -4.990  1.00 27.73 ? 4   PRO   A CA  1 
ATOM   17   C C   . PRO   A 1 25  ? 17.119  5.166   -4.247  1.00 26.76 ? 4   PRO   A C   1 
ATOM   18   O O   . PRO   A 1 25  ? 17.376  4.100   -4.831  1.00 27.68 ? 4   PRO   A O   1 
ATOM   19   C CB  . PRO   A 1 25  ? 14.883  6.373   -4.755  1.00 27.99 ? 4   PRO   A CB  1 
ATOM   20   C CG  . PRO   A 1 25  ? 14.305  5.487   -5.845  1.00 35.80 ? 4   PRO   A CG  1 
ATOM   21   C CD  . PRO   A 1 25  ? 15.195  5.795   -7.066  1.00 33.76 ? 4   PRO   A CD  1 
ATOM   22   N N   . ALA   A 1 26  ? 17.401  5.393   -2.946  1.00 27.15 ? 5   ALA   A N   1 
ATOM   23   C CA  . ALA   A 1 26  ? 18.078  4.389   -2.126  1.00 28.53 ? 5   ALA   A CA  1 
ATOM   24   C C   . ALA   A 1 26  ? 17.279  4.096   -0.846  1.00 26.23 ? 5   ALA   A C   1 
ATOM   25   O O   . ALA   A 1 26  ? 16.632  4.994   -0.302  1.00 27.82 ? 5   ALA   A O   1 
ATOM   26   C CB  . ALA   A 1 26  ? 19.464  4.883   -1.772  1.00 27.67 ? 5   ALA   A CB  1 
ATOM   27   N N   . ALA   A 1 27  ? 17.384  2.846   -0.370  1.00 24.88 ? 6   ALA   A N   1 
ATOM   28   C CA  . ALA   A 1 27  ? 16.679  2.395   0.827   1.00 25.93 ? 6   ALA   A CA  1 
ATOM   29   C C   . ALA   A 1 27  ? 17.619  1.647   1.772   1.00 24.79 ? 6   ALA   A C   1 
ATOM   30   O O   . ALA   A 1 27  ? 18.495  0.913   1.328   1.00 26.01 ? 6   ALA   A O   1 
ATOM   31   C CB  . ALA   A 1 27  ? 15.531  1.480   0.451   1.00 22.48 ? 6   ALA   A CB  1 
ATOM   32   N N   . VAL   A 1 28  ? 17.389  1.815   3.087   1.00 21.75 ? 7   VAL   A N   1 
ATOM   33   C CA  . VAL   A 1 28  ? 17.991  0.973   4.111   1.00 22.31 ? 7   VAL   A CA  1 
ATOM   34   C C   . VAL   A 1 28  ? 16.955  -0.054  4.570   1.00 23.13 ? 7   VAL   A C   1 
ATOM   35   O O   . VAL   A 1 28  ? 15.823  0.298   4.948   1.00 22.70 ? 7   VAL   A O   1 
ATOM   36   C CB  . VAL   A 1 28  ? 18.496  1.845   5.277   1.00 21.96 ? 7   VAL   A CB  1 
ATOM   37   C CG1 . VAL   A 1 28  ? 18.840  1.037   6.519   1.00 21.31 ? 7   VAL   A CG1 1 
ATOM   38   C CG2 . VAL   A 1 28  ? 19.690  2.720   4.856   1.00 23.99 ? 7   VAL   A CG2 1 
ATOM   39   N N   . VAL   A 1 29  ? 17.348  -1.321  4.533   1.00 21.63 ? 8   VAL   A N   1 
ATOM   40   C CA  . VAL   A 1 29  ? 16.516  -2.358  5.116   1.00 23.30 ? 8   VAL   A CA  1 
ATOM   41   C C   . VAL   A 1 29  ? 17.297  -3.004  6.265   1.00 24.60 ? 8   VAL   A C   1 
ATOM   42   O O   . VAL   A 1 29  ? 18.364  -3.577  6.036   1.00 22.40 ? 8   VAL   A O   1 
ATOM   43   C CB  . VAL   A 1 29  ? 16.047  -3.422  4.112   1.00 23.88 ? 8   VAL   A CB  1 
ATOM   44   C CG1 . VAL   A 1 29  ? 15.100  -4.418  4.789   1.00 23.99 ? 8   VAL   A CG1 1 
ATOM   45   C CG2 . VAL   A 1 29  ? 15.355  -2.782  2.908   1.00 24.25 ? 8   VAL   A CG2 1 
ATOM   46   N N   . THR   A 1 30  ? 16.744  -2.951  7.493   1.00 24.17 ? 9   THR   A N   1 
ATOM   47   C CA  . THR   A 1 30  ? 17.450  -3.573  8.620   1.00 22.16 ? 9   THR   A CA  1 
ATOM   48   C C   . THR   A 1 30  ? 17.134  -5.065  8.641   1.00 23.57 ? 9   THR   A C   1 
ATOM   49   O O   . THR   A 1 30  ? 16.043  -5.461  8.249   1.00 25.14 ? 9   THR   A O   1 
ATOM   50   C CB  . THR   A 1 30  ? 17.185  -2.864  9.956   1.00 23.60 ? 9   THR   A CB  1 
ATOM   51   O OG1 . THR   A 1 30  ? 15.796  -2.978  10.285  1.00 22.87 ? 9   THR   A OG1 1 
ATOM   52   C CG2 . THR   A 1 30  ? 17.532  -1.380  9.929   1.00 20.61 ? 9   THR   A CG2 1 
ATOM   53   N N   . GLY   A 1 31  ? 18.102  -5.894  9.103   1.00 22.56 ? 10  GLY   A N   1 
ATOM   54   C CA  . GLY   A 1 31  ? 17.934  -7.345  9.162   1.00 22.55 ? 10  GLY   A CA  1 
ATOM   55   C C   . GLY   A 1 31  ? 17.554  -7.921  7.794   1.00 23.45 ? 10  GLY   A C   1 
ATOM   56   O O   . GLY   A 1 31  ? 16.693  -8.794  7.698   1.00 23.85 ? 10  GLY   A O   1 
ATOM   57   N N   . ALA   A 1 32  ? 18.251  -7.477  6.738   1.00 23.63 ? 11  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 32  ? 17.820  -7.762  5.360   1.00 24.10 ? 11  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 32  ? 18.533  -8.972  4.750   1.00 26.01 ? 11  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 32  ? 18.325  -9.232  3.583   1.00 26.94 ? 11  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 32  ? 18.027  -6.528  4.488   1.00 22.84 ? 11  ALA   A CB  1 
ATOM   62   N N   . ALA   A 1 33  ? 19.345  -9.718  5.517   1.00 26.51 ? 12  ALA   A N   1 
ATOM   63   C CA  . ALA   A 1 33  ? 20.139  -10.793 4.937   1.00 29.71 ? 12  ALA   A CA  1 
ATOM   64   C C   . ALA   A 1 33  ? 19.244  -11.975 4.569   1.00 33.76 ? 12  ALA   A C   1 
ATOM   65   O O   . ALA   A 1 33  ? 19.540  -12.713 3.626   1.00 31.33 ? 12  ALA   A O   1 
ATOM   66   C CB  . ALA   A 1 33  ? 21.267  -11.224 5.881   1.00 26.61 ? 12  ALA   A CB  1 
ATOM   67   N N   . LYS   A 1 34  ? 18.149  -12.156 5.322   1.00 26.92 ? 13  LYS   A N   1 
ATOM   68   C CA  . LYS   A 1 34  ? 17.350  -13.358 5.187   1.00 28.20 ? 13  LYS   A CA  1 
ATOM   69   C C   . LYS   A 1 34  ? 15.868  -12.994 5.242   1.00 29.20 ? 13  LYS   A C   1 
ATOM   70   O O   . LYS   A 1 34  ? 15.521  -11.866 5.606   1.00 28.36 ? 13  LYS   A O   1 
ATOM   71   C CB  . LYS   A 1 34  ? 17.655  -14.349 6.321   1.00 32.08 ? 13  LYS   A CB  1 
ATOM   72   C CG  . LYS   A 1 34  ? 19.093  -14.854 6.295   1.00 36.83 ? 13  LYS   A CG  1 
ATOM   73   C CD  . LYS   A 1 34  ? 19.590  -15.993 7.184   1.00 42.16 ? 13  LYS   A CD  1 
ATOM   74   C CE  . LYS   A 1 34  ? 19.573  -15.690 8.643   1.00 52.74 ? 13  LYS   A CE  1 
ATOM   75   N NZ  . LYS   A 1 34  ? 20.556  -16.517 9.359   1.00 51.20 ? 13  LYS   A NZ  1 
ATOM   76   N N   . ARG   A 1 35  ? 15.027  -13.943 4.815   1.00 27.53 ? 14  ARG   A N   1 
ATOM   77   C CA  . ARG   A 1 35  ? 13.600  -13.998 5.156   1.00 27.77 ? 14  ARG   A CA  1 
ATOM   78   C C   . ARG   A 1 35  ? 12.886  -12.726 4.693   1.00 25.56 ? 14  ARG   A C   1 
ATOM   79   O O   . ARG   A 1 35  ? 13.008  -12.319 3.546   1.00 23.87 ? 14  ARG   A O   1 
ATOM   80   C CB  . ARG   A 1 35  ? 13.543  -14.301 6.660   1.00 29.19 ? 14  ARG   A CB  1 
ATOM   81   C CG  . ARG   A 1 35  ? 14.065  -15.704 6.957   1.00 29.56 ? 14  ARG   A CG  1 
ATOM   82   C CD  . ARG   A 1 35  ? 14.392  -15.972 8.438   1.00 33.61 ? 14  ARG   A CD  1 
ATOM   83   N NE  . ARG   A 1 35  ? 13.229  -15.807 9.318   1.00 27.56 ? 14  ARG   A NE  1 
ATOM   84   C CZ  . ARG   A 1 35  ? 12.240  -16.665 9.510   1.00 29.32 ? 14  ARG   A CZ  1 
ATOM   85   N NH1 . ARG   A 1 35  ? 12.216  -17.818 8.851   1.00 28.31 ? 14  ARG   A NH1 1 
ATOM   86   N NH2 . ARG   A 1 35  ? 11.254  -16.334 10.349  1.00 29.79 ? 14  ARG   A NH2 1 
ATOM   87   N N   . ILE   A 1 36  ? 12.097  -12.103 5.576   1.00 24.64 ? 15  ILE   A N   1 
ATOM   88   C CA  . ILE   A 1 36  ? 11.227  -11.022 5.160   1.00 24.79 ? 15  ILE   A CA  1 
ATOM   89   C C   . ILE   A 1 36  ? 12.065  -9.803  4.755   1.00 24.54 ? 15  ILE   A C   1 
ATOM   90   O O   . ILE   A 1 36  ? 11.730  -9.096  3.798   1.00 23.74 ? 15  ILE   A O   1 
ATOM   91   C CB  . ILE   A 1 36  ? 10.207  -10.670 6.272   1.00 24.79 ? 15  ILE   A CB  1 
ATOM   92   C CG1 . ILE   A 1 36  ? 9.100   -11.730 6.343   1.00 26.89 ? 15  ILE   A CG1 1 
ATOM   93   C CG2 . ILE   A 1 36  ? 9.616   -9.282  6.036   1.00 21.17 ? 15  ILE   A CG2 1 
ATOM   94   C CD1 . ILE   A 1 36  ? 8.222   -11.662 7.588   1.00 26.96 ? 15  ILE   A CD1 1 
ATOM   95   N N   . GLY   A 1 37  ? 13.137  -9.532  5.509   1.00 23.62 ? 16  GLY   A N   1 
ATOM   96   C CA  . GLY   A 1 37  ? 13.985  -8.387  5.179   1.00 24.63 ? 16  GLY   A CA  1 
ATOM   97   C C   . GLY   A 1 37  ? 14.645  -8.537  3.799   1.00 20.71 ? 16  GLY   A C   1 
ATOM   98   O O   . GLY   A 1 37  ? 14.695  -7.599  3.017   1.00 21.75 ? 16  GLY   A O   1 
ATOM   99   N N   . ARG   A 1 38  ? 15.121  -9.731  3.489   1.00 22.58 ? 17  ARG   A N   1 
ATOM   100  C CA  . ARG   A 1 38  ? 15.650  -9.987  2.152   1.00 24.21 ? 17  ARG   A CA  1 
ATOM   101  C C   . ARG   A 1 38  ? 14.569  -9.823  1.092   1.00 24.82 ? 17  ARG   A C   1 
ATOM   102  O O   . ARG   A 1 38  ? 14.828  -9.255  0.040   1.00 27.16 ? 17  ARG   A O   1 
ATOM   103  C CB  . ARG   A 1 38  ? 16.285  -11.380 2.043   1.00 26.85 ? 17  ARG   A CB  1 
ATOM   104  C CG  . ARG   A 1 38  ? 16.617  -11.772 0.608   1.00 25.29 ? 17  ARG   A CG  1 
ATOM   105  C CD  . ARG   A 1 38  ? 17.429  -13.082 0.558   1.00 28.35 ? 17  ARG   A CD  1 
ATOM   106  N NE  . ARG   A 1 38  ? 17.641  -13.423 -0.863  1.00 32.90 ? 17  ARG   A NE  1 
ATOM   107  C CZ  . ARG   A 1 38  ? 18.746  -13.874 -1.467  1.00 33.01 ? 17  ARG   A CZ  1 
ATOM   108  N NH1 . ARG   A 1 38  ? 19.857  -14.054 -0.766  1.00 31.13 ? 17  ARG   A NH1 1 
ATOM   109  N NH2 . ARG   A 1 38  ? 18.706  -14.167 -2.766  1.00 29.59 ? 17  ARG   A NH2 1 
ATOM   110  N N   . ALA   A 1 39  ? 13.354  -10.332 1.365   1.00 25.16 ? 18  ALA   A N   1 
ATOM   111  C CA  . ALA   A 1 39  ? 12.265  -10.183 0.416   1.00 26.90 ? 18  ALA   A CA  1 
ATOM   112  C C   . ALA   A 1 39  ? 11.988  -8.708  0.137   1.00 27.52 ? 18  ALA   A C   1 
ATOM   113  O O   . ALA   A 1 39  ? 11.801  -8.311  -1.004  1.00 27.39 ? 18  ALA   A O   1 
ATOM   114  C CB  . ALA   A 1 39  ? 11.027  -10.889 0.927   1.00 26.37 ? 18  ALA   A CB  1 
ATOM   115  N N   . ILE   A 1 40  ? 11.965  -7.898  1.193   1.00 24.71 ? 19  ILE   A N   1 
ATOM   116  C CA  . ILE   A 1 40  ? 11.730  -6.468  1.043   1.00 23.46 ? 19  ILE   A CA  1 
ATOM   117  C C   . ILE   A 1 40  ? 12.898  -5.824  0.276   1.00 25.29 ? 19  ILE   A C   1 
ATOM   118  O O   . ILE   A 1 40  ? 12.665  -4.987  -0.598  1.00 26.15 ? 19  ILE   A O   1 
ATOM   119  C CB  . ILE   A 1 40  ? 11.568  -5.826  2.430   1.00 23.70 ? 19  ILE   A CB  1 
ATOM   120  C CG1 . ILE   A 1 40  ? 10.234  -6.242  3.097   1.00 24.13 ? 19  ILE   A CG1 1 
ATOM   121  C CG2 . ILE   A 1 40  ? 11.717  -4.289  2.358   1.00 20.96 ? 19  ILE   A CG2 1 
ATOM   122  C CD1 . ILE   A 1 40  ? 10.213  -5.951  4.596   1.00 20.77 ? 19  ILE   A CD1 1 
ATOM   123  N N   . ALA   A 1 41  ? 14.144  -6.188  0.616   1.00 24.03 ? 20  ALA   A N   1 
ATOM   124  C CA  . ALA   A 1 41  ? 15.282  -5.628  -0.123  1.00 25.01 ? 20  ALA   A CA  1 
ATOM   125  C C   . ALA   A 1 41  ? 15.217  -5.990  -1.614  1.00 23.12 ? 20  ALA   A C   1 
ATOM   126  O O   . ALA   A 1 41  ? 15.477  -5.147  -2.470  1.00 26.14 ? 20  ALA   A O   1 
ATOM   127  C CB  . ALA   A 1 41  ? 16.631  -5.982  0.518   1.00 23.81 ? 20  ALA   A CB  1 
ATOM   128  N N   . VAL   A 1 42  ? 14.903  -7.242  -1.920  1.00 23.33 ? 21  VAL   A N   1 
ATOM   129  C CA  . VAL   A 1 42  ? 14.824  -7.704  -3.301  1.00 26.57 ? 21  VAL   A CA  1 
ATOM   130  C C   . VAL   A 1 42  ? 13.732  -6.970  -4.090  1.00 30.92 ? 21  VAL   A C   1 
ATOM   131  O O   . VAL   A 1 42  ? 13.964  -6.488  -5.202  1.00 31.66 ? 21  VAL   A O   1 
ATOM   132  C CB  . VAL   A 1 42  ? 14.610  -9.230  -3.304  1.00 27.00 ? 21  VAL   A CB  1 
ATOM   133  C CG1 . VAL   A 1 42  ? 14.245  -9.757  -4.695  1.00 31.13 ? 21  VAL   A CG1 1 
ATOM   134  C CG2 . VAL   A 1 42  ? 15.846  -9.965  -2.798  1.00 28.22 ? 21  VAL   A CG2 1 
ATOM   135  N N   . LYS   A 1 43  ? 12.535  -6.825  -3.487  1.00 26.19 ? 22  LYS   A N   1 
ATOM   136  C CA  . LYS   A 1 43  ? 11.437  -6.179  -4.171  1.00 25.59 ? 22  LYS   A CA  1 
ATOM   137  C C   . LYS   A 1 43  ? 11.732  -4.682  -4.334  1.00 26.40 ? 22  LYS   A C   1 
ATOM   138  O O   . LYS   A 1 43  ? 11.417  -4.097  -5.367  1.00 29.20 ? 22  LYS   A O   1 
ATOM   139  C CB  . LYS   A 1 43  ? 10.122  -6.554  -3.459  1.00 29.95 ? 22  LYS   A CB  1 
ATOM   140  C CG  . LYS   A 1 43  ? 8.843   -6.170  -4.227  1.00 38.10 ? 22  LYS   A CG  1 
ATOM   141  C CD  . LYS   A 1 43  ? 7.554   -6.782  -3.684  1.00 40.20 ? 22  LYS   A CD  1 
ATOM   142  C CE  . LYS   A 1 43  ? 7.384   -8.243  -4.019  1.00 46.65 ? 22  LYS   A CE  1 
ATOM   143  N NZ  . LYS   A 1 43  ? 7.002   -8.463  -5.416  1.00 44.85 ? 22  LYS   A NZ  1 
ATOM   144  N N   . LEU   A 1 44  ? 12.356  -4.035  -3.350  1.00 23.20 ? 23  LEU   A N   1 
ATOM   145  C CA  . LEU   A 1 44  ? 12.725  -2.641  -3.579  1.00 23.66 ? 23  LEU   A CA  1 
ATOM   146  C C   . LEU   A 1 44  ? 13.736  -2.532  -4.745  1.00 25.40 ? 23  LEU   A C   1 
ATOM   147  O O   . LEU   A 1 44  ? 13.651  -1.624  -5.583  1.00 29.22 ? 23  LEU   A O   1 
ATOM   148  C CB  . LEU   A 1 44  ? 13.328  -2.021  -2.324  1.00 23.42 ? 23  LEU   A CB  1 
ATOM   149  C CG  . LEU   A 1 44  ? 12.345  -1.668  -1.198  1.00 26.54 ? 23  LEU   A CG  1 
ATOM   150  C CD1 . LEU   A 1 44  ? 13.152  -1.463  0.078   1.00 26.18 ? 23  LEU   A CD1 1 
ATOM   151  C CD2 . LEU   A 1 44  ? 11.580  -0.416  -1.511  1.00 23.08 ? 23  LEU   A CD2 1 
ATOM   152  N N   . HIS   A 1 45  ? 14.723  -3.431  -4.761  1.00 26.56 ? 24  HIS   A N   1 
ATOM   153  C CA  . HIS   A 1 45  ? 15.751  -3.401  -5.796  1.00 28.40 ? 24  HIS   A CA  1 
ATOM   154  C C   . HIS   A 1 45  ? 15.129  -3.575  -7.195  1.00 32.09 ? 24  HIS   A C   1 
ATOM   155  O O   . HIS   A 1 45  ? 15.443  -2.834  -8.141  1.00 31.55 ? 24  HIS   A O   1 
ATOM   156  C CB  . HIS   A 1 45  ? 16.846  -4.412  -5.475  1.00 29.70 ? 24  HIS   A CB  1 
ATOM   157  C CG  . HIS   A 1 45  ? 18.029  -4.294  -6.382  1.00 33.75 ? 24  HIS   A CG  1 
ATOM   158  N ND1 . HIS   A 1 45  ? 18.233  -5.160  -7.442  1.00 34.22 ? 24  HIS   A ND1 1 
ATOM   159  C CD2 . HIS   A 1 45  ? 19.064  -3.430  -6.380  1.00 37.50 ? 24  HIS   A CD2 1 
ATOM   160  C CE1 . HIS   A 1 45  ? 19.366  -4.837  -8.049  1.00 35.17 ? 24  HIS   A CE1 1 
ATOM   161  N NE2 . HIS   A 1 45  ? 19.889  -3.781  -7.430  1.00 34.17 ? 24  HIS   A NE2 1 
ATOM   162  N N   . GLN   A 1 46  ? 14.233  -4.548  -7.313  1.00 30.78 ? 25  GLN   A N   1 
ATOM   163  C CA  . GLN   A 1 46  ? 13.517  -4.786  -8.561  1.00 35.62 ? 25  GLN   A CA  1 
ATOM   164  C C   . GLN   A 1 46  ? 12.656  -3.595  -8.970  1.00 35.96 ? 25  GLN   A C   1 
ATOM   165  O O   . GLN   A 1 46  ? 12.321  -3.494  -10.138 1.00 33.24 ? 25  GLN   A O   1 
ATOM   166  C CB  . GLN   A 1 46  ? 12.576  -5.976  -8.382  1.00 35.04 ? 25  GLN   A CB  1 
ATOM   167  C CG  . GLN   A 1 46  ? 13.346  -7.273  -8.252  1.00 33.34 ? 25  GLN   A CG  1 
ATOM   168  C CD  . GLN   A 1 46  ? 12.487  -8.446  -7.848  1.00 38.88 ? 25  GLN   A CD  1 
ATOM   169  O OE1 . GLN   A 1 46  ? 12.917  -9.601  -7.961  1.00 43.45 ? 25  GLN   A OE1 1 
ATOM   170  N NE2 . GLN   A 1 46  ? 11.276  -8.170  -7.388  1.00 38.56 ? 25  GLN   A NE2 1 
ATOM   171  N N   . THR   A 1 47  ? 12.265  -2.719  -8.033  1.00 31.52 ? 26  THR   A N   1 
ATOM   172  C CA  . THR   A 1 47  ? 11.431  -1.566  -8.363  1.00 32.97 ? 26  THR   A CA  1 
ATOM   173  C C   . THR   A 1 47  ? 12.319  -0.418  -8.829  1.00 35.22 ? 26  THR   A C   1 
ATOM   174  O O   . THR   A 1 47  ? 11.818  0.616   -9.292  1.00 38.42 ? 26  THR   A O   1 
ATOM   175  C CB  . THR   A 1 47  ? 10.594  -1.140  -7.147  1.00 39.06 ? 26  THR   A CB  1 
ATOM   176  O OG1 . THR   A 1 47  ? 9.804   -2.263  -6.776  1.00 42.78 ? 26  THR   A OG1 1 
ATOM   177  C CG2 . THR   A 1 47  ? 9.636   0.002   -7.429  1.00 34.87 ? 26  THR   A CG2 1 
ATOM   178  N N   . GLY   A 1 48  ? 13.632  -0.566  -8.629  1.00 31.12 ? 27  GLY   A N   1 
ATOM   179  C CA  . GLY   A 1 48  ? 14.594  0.436   -9.072  1.00 35.46 ? 27  GLY   A CA  1 
ATOM   180  C C   . GLY   A 1 48  ? 15.421  1.053   -7.938  1.00 36.49 ? 27  GLY   A C   1 
ATOM   181  O O   . GLY   A 1 48  ? 16.203  1.975   -8.194  1.00 32.21 ? 27  GLY   A O   1 
ATOM   182  N N   . TYR   A 1 49  ? 15.259  0.557   -6.688  1.00 30.31 ? 28  TYR   A N   1 
ATOM   183  C CA  . TYR   A 1 49  ? 16.007  1.104   -5.553  1.00 31.37 ? 28  TYR   A CA  1 
ATOM   184  C C   . TYR   A 1 49  ? 17.422  0.529   -5.495  1.00 28.22 ? 28  TYR   A C   1 
ATOM   185  O O   . TYR   A 1 49  ? 17.633  -0.656  -5.757  1.00 27.50 ? 28  TYR   A O   1 
ATOM   186  C CB  . TYR   A 1 49  ? 15.399  0.919   -4.148  1.00 29.20 ? 28  TYR   A CB  1 
ATOM   187  C CG  . TYR   A 1 49  ? 14.173  1.790   -3.896  1.00 27.10 ? 28  TYR   A CG  1 
ATOM   188  C CD1 . TYR   A 1 49  ? 12.932  1.456   -4.438  1.00 30.15 ? 28  TYR   A CD1 1 
ATOM   189  C CD2 . TYR   A 1 49  ? 14.266  2.964   -3.159  1.00 26.36 ? 28  TYR   A CD2 1 
ATOM   190  C CE1 . TYR   A 1 49  ? 11.812  2.252   -4.229  1.00 29.15 ? 28  TYR   A CE1 1 
ATOM   191  C CE2 . TYR   A 1 49  ? 13.159  3.778   -2.956  1.00 27.70 ? 28  TYR   A CE2 1 
ATOM   192  C CZ  . TYR   A 1 49  ? 11.929  3.423   -3.499  1.00 29.34 ? 28  TYR   A CZ  1 
ATOM   193  O OH  . TYR   A 1 49  ? 10.830  4.219   -3.321  1.00 28.69 ? 28  TYR   A OH  1 
ATOM   194  N N   . ARG   A 1 50  ? 18.372  1.384   -5.083  1.00 28.85 ? 29  ARG   A N   1 
ATOM   195  C CA  . ARG   A 1 50  ? 19.636  0.901   -4.541  1.00 29.81 ? 29  ARG   A CA  1 
ATOM   196  C C   . ARG   A 1 50  ? 19.411  0.597   -3.055  1.00 29.74 ? 29  ARG   A C   1 
ATOM   197  O O   . ARG   A 1 50  ? 18.643  1.302   -2.421  1.00 26.93 ? 29  ARG   A O   1 
ATOM   198  C CB  . ARG   A 1 50  ? 20.704  1.986   -4.738  1.00 32.27 ? 29  ARG   A CB  1 
ATOM   199  C CG  . ARG   A 1 50  ? 20.901  2.249   -6.233  1.00 32.96 ? 29  ARG   A CG  1 
ATOM   200  C CD  . ARG   A 1 50  ? 21.892  3.349   -6.486  1.00 38.77 ? 29  ARG   A CD  1 
ATOM   201  N NE  . ARG   A 1 50  ? 21.294  4.672   -6.281  1.00 34.26 ? 29  ARG   A NE  1 
ATOM   202  C CZ  . ARG   A 1 50  ? 22.043  5.768   -6.203  1.00 37.59 ? 29  ARG   A CZ  1 
ATOM   203  N NH1 . ARG   A 1 50  ? 23.344  5.712   -6.468  1.00 41.09 ? 29  ARG   A NH1 1 
ATOM   204  N NH2 . ARG   A 1 50  ? 21.502  6.914   -5.856  1.00 35.41 ? 29  ARG   A NH2 1 
ATOM   205  N N   . VAL   A 1 51  ? 20.065  -0.441  -2.514  1.00 30.23 ? 30  VAL   A N   1 
ATOM   206  C CA  . VAL   A 1 51  ? 19.721  -0.856  -1.155  1.00 30.87 ? 30  VAL   A CA  1 
ATOM   207  C C   . VAL   A 1 51  ? 20.962  -0.993  -0.267  1.00 29.80 ? 30  VAL   A C   1 
ATOM   208  O O   . VAL   A 1 51  ? 22.036  -1.412  -0.710  1.00 28.81 ? 30  VAL   A O   1 
ATOM   209  C CB  . VAL   A 1 51  ? 18.883  -2.148  -1.178  1.00 30.98 ? 30  VAL   A CB  1 
ATOM   210  C CG1 . VAL   A 1 51  ? 17.559  -1.935  -1.916  1.00 27.99 ? 30  VAL   A CG1 1 
ATOM   211  C CG2 . VAL   A 1 51  ? 19.642  -3.328  -1.764  1.00 35.81 ? 30  VAL   A CG2 1 
ATOM   212  N N   . VAL   A 1 52  ? 20.802  -0.606  1.004   1.00 27.57 ? 31  VAL   A N   1 
ATOM   213  C CA  . VAL   A 1 52  ? 21.700  -0.998  2.084   1.00 25.10 ? 31  VAL   A CA  1 
ATOM   214  C C   . VAL   A 1 52  ? 21.067  -2.183  2.798   1.00 27.60 ? 31  VAL   A C   1 
ATOM   215  O O   . VAL   A 1 52  ? 19.955  -2.073  3.335   1.00 26.57 ? 31  VAL   A O   1 
ATOM   216  C CB  . VAL   A 1 52  ? 21.988  0.136   3.081   1.00 28.08 ? 31  VAL   A CB  1 
ATOM   217  C CG1 . VAL   A 1 52  ? 22.825  -0.326  4.292   1.00 27.29 ? 31  VAL   A CG1 1 
ATOM   218  C CG2 . VAL   A 1 52  ? 22.655  1.305   2.388   1.00 27.43 ? 31  VAL   A CG2 1 
ATOM   219  N N   . ILE   A 1 53  ? 21.777  -3.302  2.722   1.00 23.67 ? 32  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 53  ? 21.459  -4.529  3.423   1.00 25.39 ? 32  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 53  ? 22.159  -4.532  4.793   1.00 28.06 ? 32  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 53  ? 23.336  -4.908  4.913   1.00 25.81 ? 32  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 53  ? 21.877  -5.710  2.548   1.00 26.92 ? 32  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 53  ? 21.232  -5.600  1.172   1.00 31.16 ? 32  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 53  ? 21.585  -7.063  3.205   1.00 28.82 ? 32  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 53  ? 21.945  -6.456  0.148   1.00 34.22 ? 32  ILE   A CD1 1 
ATOM   227  N N   . HIS   A 1 54  ? 21.415  -4.129  5.839   1.00 25.86 ? 33  HIS   A N   1 
ATOM   228  C CA  . HIS   A 1 54  ? 21.913  -4.251  7.209   1.00 25.31 ? 33  HIS   A CA  1 
ATOM   229  C C   . HIS   A 1 54  ? 21.809  -5.704  7.666   1.00 26.34 ? 33  HIS   A C   1 
ATOM   230  O O   . HIS   A 1 54  ? 20.868  -6.423  7.298   1.00 24.78 ? 33  HIS   A O   1 
ATOM   231  C CB  . HIS   A 1 54  ? 21.216  -3.252  8.152   1.00 26.58 ? 33  HIS   A CB  1 
ATOM   232  C CG  . HIS   A 1 54  ? 21.361  -3.712  9.580   1.00 24.93 ? 33  HIS   A CG  1 
ATOM   233  N ND1 . HIS   A 1 54  ? 20.441  -4.561  10.153  1.00 23.90 ? 33  HIS   A ND1 1 
ATOM   234  C CD2 . HIS   A 1 54  ? 22.336  -3.543  10.503  1.00 22.71 ? 33  HIS   A CD2 1 
ATOM   235  C CE1 . HIS   A 1 54  ? 20.855  -4.888  11.376  1.00 24.68 ? 33  HIS   A CE1 1 
ATOM   236  N NE2 . HIS   A 1 54  ? 22.003  -4.271  11.608  1.00 22.41 ? 33  HIS   A NE2 1 
ATOM   237  N N   . TYR   A 1 55  ? 22.790  -6.116  8.481   1.00 26.71 ? 34  TYR   A N   1 
ATOM   238  C CA  . TYR   A 1 55  ? 22.812  -7.438  9.097   1.00 24.71 ? 34  TYR   A CA  1 
ATOM   239  C C   . TYR   A 1 55  ? 23.557  -7.311  10.417  1.00 22.74 ? 34  TYR   A C   1 
ATOM   240  O O   . TYR   A 1 55  ? 24.212  -6.303  10.672  1.00 24.13 ? 34  TYR   A O   1 
ATOM   241  C CB  . TYR   A 1 55  ? 23.421  -8.515  8.188   1.00 25.50 ? 34  TYR   A CB  1 
ATOM   242  C CG  . TYR   A 1 55  ? 24.926  -8.309  8.033   1.00 27.82 ? 34  TYR   A CG  1 
ATOM   243  C CD1 . TYR   A 1 55  ? 25.446  -7.361  7.144   1.00 29.69 ? 34  TYR   A CD1 1 
ATOM   244  C CD2 . TYR   A 1 55  ? 25.819  -9.040  8.813   1.00 29.82 ? 34  TYR   A CD2 1 
ATOM   245  C CE1 . TYR   A 1 55  ? 26.820  -7.151  7.027   1.00 32.73 ? 34  TYR   A CE1 1 
ATOM   246  C CE2 . TYR   A 1 55  ? 27.183  -8.842  8.703   1.00 31.85 ? 34  TYR   A CE2 1 
ATOM   247  C CZ  . TYR   A 1 55  ? 27.683  -7.905  7.810   1.00 34.47 ? 34  TYR   A CZ  1 
ATOM   248  O OH  . TYR   A 1 55  ? 29.028  -7.718  7.738   1.00 36.08 ? 34  TYR   A OH  1 
ATOM   249  N N   . HIS   A 1 56  ? 23.367  -8.306  11.278  1.00 24.17 ? 35  HIS   A N   1 
ATOM   250  C CA  . HIS   A 1 56  ? 24.050  -8.397  12.560  1.00 26.30 ? 35  HIS   A CA  1 
ATOM   251  C C   . HIS   A 1 56  ? 25.027  -9.574  12.508  1.00 28.92 ? 35  HIS   A C   1 
ATOM   252  O O   . HIS   A 1 56  ? 26.219  -9.337  12.349  1.00 29.71 ? 35  HIS   A O   1 
ATOM   253  C CB  . HIS   A 1 56  ? 23.041  -8.483  13.715  1.00 29.40 ? 35  HIS   A CB  1 
ATOM   254  C CG  . HIS   A 1 56  ? 23.681  -8.660  15.058  1.00 30.01 ? 35  HIS   A CG  1 
ATOM   255  N ND1 . HIS   A 1 56  ? 23.126  -9.453  16.041  1.00 33.83 ? 35  HIS   A ND1 1 
ATOM   256  C CD2 . HIS   A 1 56  ? 24.858  -8.219  15.533  1.00 31.28 ? 35  HIS   A CD2 1 
ATOM   257  C CE1 . HIS   A 1 56  ? 23.927  -9.439  17.110  1.00 36.32 ? 35  HIS   A CE1 1 
ATOM   258  N NE2 . HIS   A 1 56  ? 24.981  -8.688  16.816  1.00 35.75 ? 35  HIS   A NE2 1 
ATOM   259  N N   . ASN   A 1 57  ? 24.503  -10.813 12.518  1.00 27.33 ? 36  ASN   A N   1 
ATOM   260  C CA  . ASN   A 1 57  ? 25.320  -12.021 12.518  1.00 34.08 ? 36  ASN   A CA  1 
ATOM   261  C C   . ASN   A 1 57  ? 25.420  -12.687 11.146  1.00 33.12 ? 36  ASN   A C   1 
ATOM   262  O O   . ASN   A 1 57  ? 26.322  -13.495 10.962  1.00 37.63 ? 36  ASN   A O   1 
ATOM   263  C CB  . ASN   A 1 57  ? 24.824  -13.110 13.476  1.00 32.02 ? 36  ASN   A CB  1 
ATOM   264  C CG  . ASN   A 1 57  ? 24.943  -12.703 14.933  1.00 37.91 ? 36  ASN   A CG  1 
ATOM   265  O OD1 . ASN   A 1 57  ? 25.944  -12.092 15.332  1.00 37.90 ? 36  ASN   A OD1 1 
ATOM   266  N ND2 . ASN   A 1 57  ? 23.921  -12.978 15.731  1.00 35.64 ? 36  ASN   A ND2 1 
ATOM   267  N N   . SER   A 1 58  ? 24.508  -12.408 10.200  1.00 31.17 ? 37  SER   A N   1 
ATOM   268  C CA  . SER   A 1 58  ? 24.439  -13.188 8.961   1.00 29.49 ? 37  SER   A CA  1 
ATOM   269  C C   . SER   A 1 58  ? 25.289  -12.577 7.841   1.00 33.01 ? 37  SER   A C   1 
ATOM   270  O O   . SER   A 1 58  ? 24.778  -12.133 6.797   1.00 31.55 ? 37  SER   A O   1 
ATOM   271  C CB  . SER   A 1 58  ? 23.013  -13.383 8.534   1.00 32.04 ? 37  SER   A CB  1 
ATOM   272  O OG  . SER   A 1 58  ? 22.333  -14.124 9.539   1.00 32.21 ? 37  SER   A OG  1 
ATOM   273  N N   . ALA   A 1 59  ? 26.613  -12.553 8.048   1.00 31.37 ? 38  ALA   A N   1 
ATOM   274  C CA  . ALA   A 1 59  ? 27.499  -11.872 7.112   1.00 28.84 ? 38  ALA   A CA  1 
ATOM   275  C C   . ALA   A 1 59  ? 27.459  -12.542 5.735   1.00 28.27 ? 38  ALA   A C   1 
ATOM   276  O O   . ALA   A 1 59  ? 27.354  -11.850 4.728   1.00 31.77 ? 38  ALA   A O   1 
ATOM   277  C CB  . ALA   A 1 59  ? 28.922  -11.785 7.657   1.00 30.69 ? 38  ALA   A CB  1 
ATOM   278  N N   . GLU   A 1 60  ? 27.560  -13.875 5.702   1.00 31.94 ? 39  GLU   A N   1 
ATOM   279  C CA  . GLU   A 1 60  ? 27.679  -14.598 4.444   1.00 36.04 ? 39  GLU   A CA  1 
ATOM   280  C C   . GLU   A 1 60  ? 26.395  -14.370 3.640   1.00 37.20 ? 39  GLU   A C   1 
ATOM   281  O O   . GLU   A 1 60  ? 26.444  -14.068 2.449   1.00 32.55 ? 39  GLU   A O   1 
ATOM   282  C CB  . GLU   A 1 60  ? 27.976  -16.083 4.700   1.00 34.95 ? 39  GLU   A CB  1 
ATOM   283  C CG  . GLU   A 1 60  ? 27.714  -16.974 3.488   0.60 40.50 ? 39  GLU   A CG  1 
ATOM   284  C CD  . GLU   A 1 60  ? 27.871  -18.467 3.730   0.60 49.49 ? 39  GLU   A CD  1 
ATOM   285  O OE1 . GLU   A 1 60  ? 26.862  -19.195 3.611   0.60 53.39 ? 39  GLU   A OE1 1 
ATOM   286  O OE2 . GLU   A 1 60  ? 28.999  -18.905 4.037   0.60 49.00 ? 39  GLU   A OE2 1 
ATOM   287  N N   . ALA   A 1 61  ? 25.237  -14.506 4.308   1.00 31.77 ? 40  ALA   A N   1 
ATOM   288  C CA  . ALA   A 1 61  ? 23.969  -14.345 3.612   1.00 29.76 ? 40  ALA   A CA  1 
ATOM   289  C C   . ALA   A 1 61  ? 23.839  -12.921 3.085   1.00 27.80 ? 40  ALA   A C   1 
ATOM   290  O O   . ALA   A 1 61  ? 23.358  -12.724 1.974   1.00 32.77 ? 40  ALA   A O   1 
ATOM   291  C CB  . ALA   A 1 61  ? 22.795  -14.779 4.475   1.00 27.43 ? 40  ALA   A CB  1 
ATOM   292  N N   . ALA   A 1 62  ? 24.260  -11.938 3.883   1.00 26.63 ? 41  ALA   A N   1 
ATOM   293  C CA  . ALA   A 1 62  ? 24.152  -10.538 3.497   1.00 27.45 ? 41  ALA   A CA  1 
ATOM   294  C C   . ALA   A 1 62  ? 24.971  -10.289 2.227   1.00 31.40 ? 41  ALA   A C   1 
ATOM   295  O O   . ALA   A 1 62  ? 24.508  -9.635  1.295   1.00 30.66 ? 41  ALA   A O   1 
ATOM   296  C CB  . ALA   A 1 62  ? 24.700  -9.686  4.609   1.00 27.58 ? 41  ALA   A CB  1 
ATOM   297  N N   . VAL   A 1 63  ? 26.244  -10.716 2.259   1.00 32.07 ? 42  VAL   A N   1 
ATOM   298  C CA  . VAL   A 1 63  ? 27.163  -10.444 1.150   1.00 30.44 ? 42  VAL   A CA  1 
ATOM   299  C C   . VAL   A 1 63  ? 26.645  -11.164 -0.091  1.00 29.97 ? 42  VAL   A C   1 
ATOM   300  O O   . VAL   A 1 63  ? 26.620  -10.596 -1.187  1.00 32.99 ? 42  VAL   A O   1 
ATOM   301  C CB  . VAL   A 1 63  ? 28.604  -10.888 1.489   1.00 33.10 ? 42  VAL   A CB  1 
ATOM   302  C CG1 . VAL   A 1 63  ? 29.525  -10.958 0.252   1.00 31.05 ? 42  VAL   A CG1 1 
ATOM   303  C CG2 . VAL   A 1 63  ? 29.230  -10.020 2.581   1.00 31.90 ? 42  VAL   A CG2 1 
ATOM   304  N N   . SER   A 1 64  ? 26.181  -12.400 0.112   1.00 28.15 ? 43  SER   A N   1 
ATOM   305  C CA  . SER   A 1 64  ? 25.625  -13.180 -0.978  1.00 31.78 ? 43  SER   A CA  1 
ATOM   306  C C   . SER   A 1 64  ? 24.453  -12.449 -1.655  1.00 37.25 ? 43  SER   A C   1 
ATOM   307  O O   . SER   A 1 64  ? 24.342  -12.437 -2.884  1.00 34.41 ? 43  SER   A O   1 
ATOM   308  C CB  . SER   A 1 64  ? 25.272  -14.577 -0.493  1.00 34.32 ? 43  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 64  ? 24.583  -15.278 -1.517  1.00 37.40 ? 43  SER   A OG  1 
ATOM   310  N N   . LEU   A 1 65  ? 23.579  -11.797 -0.863  1.00 33.25 ? 44  LEU   A N   1 
ATOM   311  C CA  . LEU   A 1 65  ? 22.458  -11.068 -1.441  1.00 30.62 ? 44  LEU   A CA  1 
ATOM   312  C C   . LEU   A 1 65  ? 22.962  -9.855  -2.217  1.00 28.95 ? 44  LEU   A C   1 
ATOM   313  O O   . LEU   A 1 65  ? 22.444  -9.574  -3.298  1.00 33.12 ? 44  LEU   A O   1 
ATOM   314  C CB  . LEU   A 1 65  ? 21.436  -10.683 -0.361  1.00 30.50 ? 44  LEU   A CB  1 
ATOM   315  C CG  . LEU   A 1 65  ? 20.387  -9.630  -0.732  1.00 30.35 ? 44  LEU   A CG  1 
ATOM   316  C CD1 . LEU   A 1 65  ? 19.558  -10.173 -1.890  1.00 27.68 ? 44  LEU   A CD1 1 
ATOM   317  C CD2 . LEU   A 1 65  ? 19.510  -9.390  0.540   1.00 25.78 ? 44  LEU   A CD2 1 
ATOM   318  N N   . ALA   A 1 66  ? 23.917  -9.104  -1.643  1.00 28.37 ? 45  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 66  ? 24.387  -7.868  -2.261  1.00 29.97 ? 45  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 66  ? 25.004  -8.208  -3.616  1.00 30.33 ? 45  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 66  ? 24.831  -7.444  -4.566  1.00 30.22 ? 45  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 66  ? 25.399  -7.119  -1.385  1.00 25.96 ? 45  ALA   A CB  1 
ATOM   323  N N   . ASP   A 1 67  ? 25.725  -9.345  -3.645  1.00 36.34 ? 46  ASP   A N   1 
ATOM   324  C CA  . ASP   A 1 67  ? 26.387  -9.885  -4.831  1.00 38.34 ? 46  ASP   A CA  1 
ATOM   325  C C   . ASP   A 1 67  ? 25.357  -10.141 -5.927  1.00 37.18 ? 46  ASP   A C   1 
ATOM   326  O O   . ASP   A 1 67  ? 25.506  -9.646  -7.043  1.00 38.02 ? 46  ASP   A O   1 
ATOM   327  C CB  . ASP   A 1 67  ? 27.154  -11.158 -4.501  1.00 40.15 ? 46  ASP   A CB  1 
ATOM   328  C CG  . ASP   A 1 67  ? 28.493  -10.933 -3.808  1.00 48.01 ? 46  ASP   A CG  1 
ATOM   329  O OD1 . ASP   A 1 67  ? 28.894  -9.748  -3.683  1.00 52.82 ? 46  ASP   A OD1 1 
ATOM   330  O OD2 . ASP   A 1 67  ? 29.123  -11.930 -3.384  1.00 46.29 ? 46  ASP   A OD2 1 
ATOM   331  N N   . GLU   A 1 68  ? 24.296  -10.892 -5.586  1.00 34.61 ? 47  GLU   A N   1 
ATOM   332  C CA  . GLU   A 1 68  ? 23.220  -11.144 -6.534  1.00 38.92 ? 47  GLU   A CA  1 
ATOM   333  C C   . GLU   A 1 68  ? 22.622  -9.844  -7.071  1.00 38.88 ? 47  GLU   A C   1 
ATOM   334  O O   . GLU   A 1 68  ? 22.361  -9.732  -8.266  1.00 40.24 ? 47  GLU   A O   1 
ATOM   335  C CB  . GLU   A 1 68  ? 22.090  -12.009 -5.987  1.00 37.91 ? 47  GLU   A CB  1 
ATOM   336  C CG  . GLU   A 1 68  ? 22.503  -13.462 -5.804  1.00 36.54 ? 47  GLU   A CG  1 
ATOM   337  C CD  . GLU   A 1 68  ? 21.236  -14.234 -5.464  1.00 44.73 ? 47  GLU   A CD  1 
ATOM   338  O OE1 . GLU   A 1 68  ? 21.141  -14.809 -4.349  1.00 43.77 ? 47  GLU   A OE1 1 
ATOM   339  O OE2 . GLU   A 1 68  ? 20.326  -14.250 -6.326  1.00 46.04 ? 47  GLU   A OE2 1 
ATOM   340  N N   . LEU   A 1 69  ? 22.408  -8.854  -6.200  1.00 32.97 ? 48  LEU   A N   1 
ATOM   341  C CA  . LEU   A 1 69  ? 21.740  -7.640  -6.636  1.00 34.73 ? 48  LEU   A CA  1 
ATOM   342  C C   . LEU   A 1 69  ? 22.661  -6.818  -7.541  1.00 36.48 ? 48  LEU   A C   1 
ATOM   343  O O   . LEU   A 1 69  ? 22.204  -6.159  -8.483  1.00 32.25 ? 48  LEU   A O   1 
ATOM   344  C CB  . LEU   A 1 69  ? 21.313  -6.852  -5.402  1.00 30.82 ? 48  LEU   A CB  1 
ATOM   345  C CG  . LEU   A 1 69  ? 20.250  -7.532  -4.520  1.00 31.81 ? 48  LEU   A CG  1 
ATOM   346  C CD1 . LEU   A 1 69  ? 19.899  -6.603  -3.370  1.00 30.54 ? 48  LEU   A CD1 1 
ATOM   347  C CD2 . LEU   A 1 69  ? 19.017  -7.907  -5.295  1.00 31.96 ? 48  LEU   A CD2 1 
ATOM   348  N N   . ASN   A 1 70  ? 23.953  -6.815  -7.195  1.00 36.17 ? 49  ASN   A N   1 
ATOM   349  C CA  . ASN   A 1 70  ? 24.945  -6.074  -7.972  1.00 37.89 ? 49  ASN   A CA  1 
ATOM   350  C C   . ASN   A 1 70  ? 25.147  -6.728  -9.348  1.00 38.47 ? 49  ASN   A C   1 
ATOM   351  O O   . ASN   A 1 70  ? 25.440  -6.020  -10.307 1.00 34.30 ? 49  ASN   A O   1 
ATOM   352  C CB  . ASN   A 1 70  ? 26.269  -5.892  -7.231  1.00 33.97 ? 49  ASN   A CB  1 
ATOM   353  C CG  . ASN   A 1 70  ? 26.248  -4.839  -6.143  1.00 33.19 ? 49  ASN   A CG  1 
ATOM   354  O OD1 . ASN   A 1 70  ? 25.727  -3.729  -6.327  1.00 34.18 ? 49  ASN   A OD1 1 
ATOM   355  N ND2 . ASN   A 1 70  ? 26.832  -5.166  -4.999  1.00 32.98 ? 49  ASN   A ND2 1 
ATOM   356  N N   . LYS   A 1 71  ? 25.000  -8.065  -9.444  1.00 37.75 ? 50  LYS   A N   1 
ATOM   357  C CA  . LYS   A 1 71  ? 25.120  -8.766  -10.720 1.00 41.75 ? 50  LYS   A CA  1 
ATOM   358  C C   . LYS   A 1 71  ? 23.965  -8.377  -11.637 1.00 49.16 ? 50  LYS   A C   1 
ATOM   359  O O   . LYS   A 1 71  ? 24.081  -8.426  -12.854 1.00 43.82 ? 50  LYS   A O   1 
ATOM   360  C CB  . LYS   A 1 71  ? 25.169  -10.296 -10.584 1.00 46.33 ? 50  LYS   A CB  1 
ATOM   361  C CG  . LYS   A 1 71  ? 26.495  -10.853 -10.075 0.60 42.50 ? 50  LYS   A CG  1 
ATOM   362  C CD  . LYS   A 1 71  ? 26.525  -12.351 -9.790  0.60 47.57 ? 50  LYS   A CD  1 
ATOM   363  C CE  . LYS   A 1 71  ? 27.718  -12.729 -8.956  0.60 48.03 ? 50  LYS   A CE  1 
ATOM   364  N NZ  . LYS   A 1 71  ? 27.825  -14.182 -8.815  0.60 43.78 ? 50  LYS   A NZ  1 
ATOM   365  N N   . GLU   A 1 72  ? 22.834  -7.999  -11.035 1.00 41.84 ? 51  GLU   A N   1 
ATOM   366  C CA  . GLU   A 1 72  ? 21.691  -7.535  -11.783 1.00 38.60 ? 51  GLU   A CA  1 
ATOM   367  C C   . GLU   A 1 72  ? 21.922  -6.096  -12.240 1.00 42.51 ? 51  GLU   A C   1 
ATOM   368  O O   . GLU   A 1 72  ? 21.612  -5.752  -13.384 1.00 41.54 ? 51  GLU   A O   1 
ATOM   369  C CB  . GLU   A 1 72  ? 20.523  -7.647  -10.804 1.00 50.00 ? 51  GLU   A CB  1 
ATOM   370  C CG  . GLU   A 1 72  ? 19.158  -7.665  -11.474 1.00 53.53 ? 51  GLU   A CG  1 
ATOM   371  C CD  . GLU   A 1 72  ? 18.965  -8.928  -12.283 1.00 58.76 ? 51  GLU   A CD  1 
ATOM   372  O OE1 . GLU   A 1 72  ? 19.308  -10.046 -11.815 1.00 55.34 ? 51  GLU   A OE1 1 
ATOM   373  O OE2 . GLU   A 1 72  ? 18.447  -8.751  -13.404 1.00 60.35 ? 51  GLU   A OE2 1 
ATOM   374  N N   . ARG   A 1 73  ? 22.443  -5.246  -11.343 1.00 37.50 ? 52  ARG   A N   1 
ATOM   375  C CA  . ARG   A 1 73  ? 22.723  -3.863  -11.681 1.00 38.36 ? 52  ARG   A CA  1 
ATOM   376  C C   . ARG   A 1 73  ? 23.901  -3.451  -10.824 1.00 45.07 ? 52  ARG   A C   1 
ATOM   377  O O   . ARG   A 1 73  ? 23.833  -3.573  -9.604  1.00 38.15 ? 52  ARG   A O   1 
ATOM   378  C CB  . ARG   A 1 73  ? 21.563  -2.886  -11.442 1.00 43.61 ? 52  ARG   A CB  1 
ATOM   379  C CG  . ARG   A 1 73  ? 20.217  -3.126  -12.118 1.00 44.06 ? 52  ARG   A CG  1 
ATOM   380  C CD  . ARG   A 1 73  ? 19.414  -1.826  -12.229 1.00 43.00 ? 52  ARG   A CD  1 
ATOM   381  N NE  . ARG   A 1 73  ? 19.037  -1.240  -10.937 1.00 45.07 ? 52  ARG   A NE  1 
ATOM   382  C CZ  . ARG   A 1 73  ? 18.194  -1.796  -10.058 1.00 49.93 ? 52  ARG   A CZ  1 
ATOM   383  N NH1 . ARG   A 1 73  ? 17.608  -2.945  -10.373 1.00 39.38 ? 52  ARG   A NH1 1 
ATOM   384  N NH2 . ARG   A 1 73  ? 17.964  -1.215  -8.877  1.00 40.46 ? 52  ARG   A NH2 1 
ATOM   385  N N   . SER   A 1 74  ? 25.003  -3.054  -11.473 1.00 38.64 ? 53  SER   A N   1 
ATOM   386  C CA  . SER   A 1 74  ? 26.246  -2.887  -10.744 1.00 39.02 ? 53  SER   A CA  1 
ATOM   387  C C   . SER   A 1 74  ? 26.140  -1.660  -9.854  1.00 34.87 ? 53  SER   A C   1 
ATOM   388  O O   . SER   A 1 74  ? 25.432  -0.707  -10.197 1.00 34.86 ? 53  SER   A O   1 
ATOM   389  C CB  . SER   A 1 74  ? 27.436  -2.781  -11.692 1.00 44.61 ? 53  SER   A CB  1 
ATOM   390  O OG  . SER   A 1 74  ? 27.151  -1.761  -12.636 1.00 50.46 ? 53  SER   A OG  1 
ATOM   391  N N   . ASN   A 1 75  ? 26.854  -1.717  -8.718  1.00 32.00 ? 54  ASN   A N   1 
ATOM   392  C CA  . ASN   A 1 75  ? 26.935  -0.630  -7.755  1.00 37.75 ? 54  ASN   A CA  1 
ATOM   393  C C   . ASN   A 1 75  ? 25.545  -0.226  -7.241  1.00 38.51 ? 54  ASN   A C   1 
ATOM   394  O O   . ASN   A 1 75  ? 25.279  0.973   -7.069  1.00 33.31 ? 54  ASN   A O   1 
ATOM   395  C CB  . ASN   A 1 75  ? 27.670  0.581   -8.319  1.00 44.71 ? 54  ASN   A CB  1 
ATOM   396  C CG  . ASN   A 1 75  ? 29.108  0.273   -8.663  0.70 45.39 ? 54  ASN   A CG  1 
ATOM   397  O OD1 . ASN   A 1 75  ? 29.498  -0.895  -8.737  0.70 47.62 ? 54  ASN   A OD1 1 
ATOM   398  N ND2 . ASN   A 1 75  ? 29.904  1.301   -8.892  0.70 48.59 ? 54  ASN   A ND2 1 
ATOM   399  N N   . THR   A 1 76  ? 24.668  -1.217  -7.005  1.00 31.44 ? 55  THR   A N   1 
ATOM   400  C CA  . THR   A 1 76  ? 23.344  -0.886  -6.476  1.00 31.45 ? 55  THR   A CA  1 
ATOM   401  C C   . THR   A 1 76  ? 23.055  -1.496  -5.090  1.00 35.97 ? 55  THR   A C   1 
ATOM   402  O O   . THR   A 1 76  ? 22.002  -1.186  -4.529  1.00 35.26 ? 55  THR   A O   1 
ATOM   403  C CB  . THR   A 1 76  ? 22.222  -1.226  -7.461  1.00 31.17 ? 55  THR   A CB  1 
ATOM   404  O OG1 . THR   A 1 76  ? 22.372  -2.632  -7.625  1.00 27.58 ? 55  THR   A OG1 1 
ATOM   405  C CG2 . THR   A 1 76  ? 22.224  -0.374  -8.720  1.00 27.38 ? 55  THR   A CG2 1 
ATOM   406  N N   . ALA   A 1 77  ? 23.934  -2.360  -4.542  1.00 29.74 ? 56  ALA   A N   1 
ATOM   407  C CA  . ALA   A 1 77  ? 23.743  -2.916  -3.201  1.00 33.43 ? 56  ALA   A CA  1 
ATOM   408  C C   . ALA   A 1 77  ? 25.021  -2.810  -2.358  1.00 34.92 ? 56  ALA   A C   1 
ATOM   409  O O   . ALA   A 1 77  ? 26.120  -3.002  -2.871  1.00 30.11 ? 56  ALA   A O   1 
ATOM   410  C CB  . ALA   A 1 77  ? 23.265  -4.356  -3.276  1.00 31.87 ? 56  ALA   A CB  1 
ATOM   411  N N   . VAL   A 1 78  ? 24.872  -2.522  -1.056  1.00 30.19 ? 57  VAL   A N   1 
ATOM   412  C CA  . VAL   A 1 78  ? 25.962  -2.576  -0.080  1.00 30.02 ? 57  VAL   A CA  1 
ATOM   413  C C   . VAL   A 1 78  ? 25.429  -3.236  1.186   1.00 32.63 ? 57  VAL   A C   1 
ATOM   414  O O   . VAL   A 1 78  ? 24.204  -3.300  1.352   1.00 30.73 ? 57  VAL   A O   1 
ATOM   415  C CB  . VAL   A 1 78  ? 26.672  -1.241  0.252   1.00 32.90 ? 57  VAL   A CB  1 
ATOM   416  C CG1 . VAL   A 1 78  ? 27.365  -0.639  -0.975  1.00 31.17 ? 57  VAL   A CG1 1 
ATOM   417  C CG2 . VAL   A 1 78  ? 25.750  -0.214  0.922   1.00 29.55 ? 57  VAL   A CG2 1 
ATOM   418  N N   . VAL   A 1 79  ? 26.347  -3.806  1.991   1.00 29.75 ? 58  VAL   A N   1 
ATOM   419  C CA  . VAL   A 1 79  ? 26.071  -4.372  3.312   1.00 30.10 ? 58  VAL   A CA  1 
ATOM   420  C C   . VAL   A 1 79  ? 26.521  -3.391  4.391   1.00 34.05 ? 58  VAL   A C   1 
ATOM   421  O O   . VAL   A 1 79  ? 27.349  -2.503  4.136   1.00 32.69 ? 58  VAL   A O   1 
ATOM   422  C CB  . VAL   A 1 79  ? 26.618  -5.798  3.562   1.00 33.82 ? 58  VAL   A CB  1 
ATOM   423  C CG1 . VAL   A 1 79  ? 26.119  -6.776  2.509   1.00 29.82 ? 58  VAL   A CG1 1 
ATOM   424  C CG2 . VAL   A 1 79  ? 28.155  -5.866  3.676   1.00 32.15 ? 58  VAL   A CG2 1 
ATOM   425  N N   . CYS   A 1 80  ? 25.956  -3.535  5.606   1.00 30.26 ? 59  CYS   A N   1 
ATOM   426  C CA  . CYS   A 1 80  ? 26.338  -2.693  6.735   1.00 31.29 ? 59  CYS   A CA  1 
ATOM   427  C C   . CYS   A 1 80  ? 26.061  -3.470  8.009   1.00 30.31 ? 59  CYS   A C   1 
ATOM   428  O O   . CYS   A 1 80  ? 24.898  -3.800  8.259   1.00 29.07 ? 59  CYS   A O   1 
ATOM   429  C CB  . CYS   A 1 80  ? 25.486  -1.427  6.788   1.00 29.21 ? 59  CYS   A CB  1 
ATOM   430  S SG  . CYS   A 1 80  ? 25.960  -0.284  8.116   1.00 33.24 ? 59  CYS   A SG  1 
ATOM   431  N N   . GLN   A 1 81  ? 27.117  -3.769  8.788   1.00 27.79 ? 60  GLN   A N   1 
ATOM   432  C CA  . GLN   A 1 81  ? 26.957  -4.620  9.963   1.00 29.96 ? 60  GLN   A CA  1 
ATOM   433  C C   . GLN   A 1 81  ? 26.660  -3.721  11.158  1.00 27.19 ? 60  GLN   A C   1 
ATOM   434  O O   . GLN   A 1 81  ? 27.298  -2.688  11.317  1.00 27.04 ? 60  GLN   A O   1 
ATOM   435  C CB  . GLN   A 1 81  ? 28.207  -5.488  10.169  1.00 32.04 ? 60  GLN   A CB  1 
ATOM   436  C CG  . GLN   A 1 81  ? 28.065  -6.588  11.221  1.00 32.06 ? 60  GLN   A CG  1 
ATOM   437  C CD  . GLN   A 1 81  ? 28.158  -6.094  12.654  1.00 38.19 ? 60  GLN   A CD  1 
ATOM   438  O OE1 . GLN   A 1 81  ? 28.730  -5.033  12.948  1.00 39.32 ? 60  GLN   A OE1 1 
ATOM   439  N NE2 . GLN   A 1 81  ? 27.602  -6.869  13.575  1.00 38.22 ? 60  GLN   A NE2 1 
ATOM   440  N N   . ALA   A 1 82  ? 25.650  -4.081  11.965  1.00 26.80 ? 61  ALA   A N   1 
ATOM   441  C CA  . ALA   A 1 82  ? 25.399  -3.346  13.190  1.00 26.70 ? 61  ALA   A CA  1 
ATOM   442  C C   . ALA   A 1 82  ? 24.619  -4.202  14.187  1.00 28.21 ? 61  ALA   A C   1 
ATOM   443  O O   . ALA   A 1 82  ? 23.697  -4.937  13.802  1.00 25.70 ? 61  ALA   A O   1 
ATOM   444  C CB  . ALA   A 1 82  ? 24.727  -2.012  12.917  1.00 26.18 ? 61  ALA   A CB  1 
ATOM   445  N N   . ASP   A 1 83  ? 25.031  -4.126  15.470  1.00 24.85 ? 62  ASP   A N   1 
ATOM   446  C CA  . ASP   A 1 83  ? 24.249  -4.716  16.552  1.00 27.51 ? 62  ASP   A CA  1 
ATOM   447  C C   . ASP   A 1 83  ? 23.195  -3.687  16.949  1.00 24.99 ? 62  ASP   A C   1 
ATOM   448  O O   . ASP   A 1 83  ? 23.549  -2.529  17.183  1.00 24.06 ? 62  ASP   A O   1 
ATOM   449  C CB  . ASP   A 1 83  ? 25.133  -5.079  17.742  1.00 30.58 ? 62  ASP   A CB  1 
ATOM   450  C CG  . ASP   A 1 83  ? 24.455  -5.847  18.879  1.00 32.66 ? 62  ASP   A CG  1 
ATOM   451  O OD1 . ASP   A 1 83  ? 23.232  -6.079  18.821  1.00 28.07 ? 62  ASP   A OD1 1 
ATOM   452  O OD2 . ASP   A 1 83  ? 25.162  -6.249  19.828  1.00 32.44 ? 62  ASP   A OD2 1 
ATOM   453  N N   . LEU   A 1 84  ? 21.916  -4.102  17.003  1.00 24.38 ? 63  LEU   A N   1 
ATOM   454  C CA  . LEU   A 1 84  ? 20.846  -3.158  17.331  1.00 22.92 ? 63  LEU   A CA  1 
ATOM   455  C C   . LEU   A 1 84  ? 20.299  -3.336  18.753  1.00 24.72 ? 63  LEU   A C   1 
ATOM   456  O O   . LEU   A 1 84  ? 19.229  -2.784  19.052  1.00 22.85 ? 63  LEU   A O   1 
ATOM   457  C CB  . LEU   A 1 84  ? 19.702  -3.148  16.309  1.00 21.44 ? 63  LEU   A CB  1 
ATOM   458  C CG  . LEU   A 1 84  ? 20.085  -2.808  14.860  1.00 24.25 ? 63  LEU   A CG  1 
ATOM   459  C CD1 . LEU   A 1 84  ? 18.930  -2.946  13.867  1.00 24.19 ? 63  LEU   A CD1 1 
ATOM   460  C CD2 . LEU   A 1 84  ? 20.675  -1.419  14.730  1.00 22.77 ? 63  LEU   A CD2 1 
ATOM   461  N N   . THR   A 1 85  ? 21.034  -4.072  19.605  1.00 23.22 ? 64  THR   A N   1 
ATOM   462  C CA  . THR   A 1 85  ? 20.824  -4.171  21.045  1.00 22.91 ? 64  THR   A CA  1 
ATOM   463  C C   . THR   A 1 85  ? 20.898  -2.771  21.635  1.00 21.87 ? 64  THR   A C   1 
ATOM   464  O O   . THR   A 1 85  ? 21.799  -2.019  21.276  1.00 21.90 ? 64  THR   A O   1 
ATOM   465  C CB  . THR   A 1 85  ? 21.915  -5.054  21.668  1.00 27.34 ? 64  THR   A CB  1 
ATOM   466  O OG1 . THR   A 1 85  ? 21.731  -6.334  21.059  1.00 28.05 ? 64  THR   A OG1 1 
ATOM   467  C CG2 . THR   A 1 85  ? 21.657  -5.352  23.134  1.00 25.85 ? 64  THR   A CG2 1 
ATOM   468  N N   . ASN   A 1 86  ? 20.012  -2.444  22.590  1.00 20.80 ? 65  ASN   A N   1 
ATOM   469  C CA  . ASN   A 1 86  ? 20.104  -1.147  23.269  1.00 21.03 ? 65  ASN   A CA  1 
ATOM   470  C C   . ASN   A 1 86  ? 21.432  -1.053  24.049  1.00 21.79 ? 65  ASN   A C   1 
ATOM   471  O O   . ASN   A 1 86  ? 21.869  -2.013  24.684  1.00 22.76 ? 65  ASN   A O   1 
ATOM   472  C CB  . ASN   A 1 86  ? 18.912  -0.955  24.218  1.00 20.98 ? 65  ASN   A CB  1 
ATOM   473  C CG  . ASN   A 1 86  ? 18.797  0.444   24.764  1.00 23.64 ? 65  ASN   A CG  1 
ATOM   474  O OD1 . ASN   A 1 86  ? 18.983  1.423   24.028  1.00 22.46 ? 65  ASN   A OD1 1 
ATOM   475  N ND2 . ASN   A 1 86  ? 18.441  0.577   26.035  1.00 25.21 ? 65  ASN   A ND2 1 
ATOM   476  N N   . SER   A 1 87  ? 22.081  0.119   23.982  1.00 23.58 ? 66  SER   A N   1 
ATOM   477  C CA  . SER   A 1 87  ? 23.279  0.454   24.738  1.00 24.94 ? 66  SER   A CA  1 
ATOM   478  C C   . SER   A 1 87  ? 23.498  1.954   24.557  1.00 23.61 ? 66  SER   A C   1 
ATOM   479  O O   . SER   A 1 87  ? 22.779  2.606   23.792  1.00 19.92 ? 66  SER   A O   1 
ATOM   480  C CB  . SER   A 1 87  ? 24.486  -0.305  24.220  1.00 27.81 ? 66  SER   A CB  1 
ATOM   481  O OG  . SER   A 1 87  ? 24.956  0.315   23.029  1.00 27.26 ? 66  SER   A OG  1 
ATOM   482  N N   . ASN   A 1 88  ? 24.509  2.497   25.231  1.00 24.47 ? 67  ASN   A N   1 
ATOM   483  C CA  . ASN   A 1 88  ? 24.803  3.929   25.102  1.00 23.77 ? 67  ASN   A CA  1 
ATOM   484  C C   . ASN   A 1 88  ? 25.441  4.251   23.747  1.00 23.65 ? 67  ASN   A C   1 
ATOM   485  O O   . ASN   A 1 88  ? 25.538  5.420   23.385  1.00 23.88 ? 67  ASN   A O   1 
ATOM   486  C CB  . ASN   A 1 88  ? 25.631  4.451   26.282  1.00 25.51 ? 67  ASN   A CB  1 
ATOM   487  C CG  . ASN   A 1 88  ? 24.774  4.597   27.527  1.00 27.65 ? 67  ASN   A CG  1 
ATOM   488  O OD1 . ASN   A 1 88  ? 23.551  4.657   27.427  1.00 31.66 ? 67  ASN   A OD1 1 
ATOM   489  N ND2 . ASN   A 1 88  ? 25.372  4.660   28.704  1.00 27.14 ? 67  ASN   A ND2 1 
ATOM   490  N N   . VAL   A 1 89  ? 25.843  3.227   22.991  1.00 21.94 ? 68  VAL   A N   1 
ATOM   491  C CA  . VAL   A 1 89  ? 26.404  3.471   21.661  1.00 22.77 ? 68  VAL   A CA  1 
ATOM   492  C C   . VAL   A 1 89  ? 25.385  3.197   20.555  1.00 23.28 ? 68  VAL   A C   1 
ATOM   493  O O   . VAL   A 1 89  ? 25.669  3.455   19.376  1.00 25.50 ? 68  VAL   A O   1 
ATOM   494  C CB  . VAL   A 1 89  ? 27.710  2.699   21.377  1.00 27.91 ? 68  VAL   A CB  1 
ATOM   495  C CG1 . VAL   A 1 89  ? 28.679  2.933   22.528  1.00 31.49 ? 68  VAL   A CG1 1 
ATOM   496  C CG2 . VAL   A 1 89  ? 27.472  1.198   21.209  1.00 26.68 ? 68  VAL   A CG2 1 
ATOM   497  N N   . LEU   A 1 90  ? 24.197  2.694   20.921  1.00 20.10 ? 69  LEU   A N   1 
ATOM   498  C CA  . LEU   A 1 90  ? 23.199  2.389   19.893  1.00 22.09 ? 69  LEU   A CA  1 
ATOM   499  C C   . LEU   A 1 90  ? 22.946  3.636   19.041  1.00 18.37 ? 69  LEU   A C   1 
ATOM   500  O O   . LEU   A 1 90  ? 22.856  3.535   17.815  1.00 20.14 ? 69  LEU   A O   1 
ATOM   501  C CB  . LEU   A 1 90  ? 21.897  1.768   20.450  1.00 20.88 ? 69  LEU   A CB  1 
ATOM   502  C CG  . LEU   A 1 90  ? 20.882  1.296   19.390  1.00 20.28 ? 69  LEU   A CG  1 
ATOM   503  C CD1 . LEU   A 1 90  ? 21.369  0.144   18.477  1.00 18.07 ? 69  LEU   A CD1 1 
ATOM   504  C CD2 . LEU   A 1 90  ? 19.548  0.859   20.089  1.00 19.25 ? 69  LEU   A CD2 1 
ATOM   505  N N   . PRO   A 1 91  ? 22.794  4.879   19.581  1.00 18.79 ? 70  PRO   A N   1 
ATOM   506  C CA  . PRO   A 1 91  ? 22.633  6.025   18.692  1.00 20.98 ? 70  PRO   A CA  1 
ATOM   507  C C   . PRO   A 1 91  ? 23.697  6.171   17.596  1.00 24.17 ? 70  PRO   A C   1 
ATOM   508  O O   . PRO   A 1 91  ? 23.395  6.409   16.417  1.00 23.95 ? 70  PRO   A O   1 
ATOM   509  C CB  . PRO   A 1 91  ? 22.602  7.236   19.646  1.00 20.18 ? 70  PRO   A CB  1 
ATOM   510  C CG  . PRO   A 1 91  ? 22.028  6.605   20.933  1.00 20.79 ? 70  PRO   A CG  1 
ATOM   511  C CD  . PRO   A 1 91  ? 22.772  5.257   21.002  1.00 19.95 ? 70  PRO   A CD  1 
ATOM   512  N N   . ALA   A 1 92  ? 24.954  6.026   18.001  1.00 22.92 ? 71  ALA   A N   1 
ATOM   513  C CA  . ALA   A 1 92  ? 26.060  6.072   17.056  1.00 23.34 ? 71  ALA   A CA  1 
ATOM   514  C C   . ALA   A 1 92  ? 25.891  4.993   15.996  1.00 21.04 ? 71  ALA   A C   1 
ATOM   515  O O   . ALA   A 1 92  ? 26.060  5.269   14.811  1.00 23.45 ? 71  ALA   A O   1 
ATOM   516  C CB  . ALA   A 1 92  ? 27.389  5.899   17.776  1.00 22.63 ? 71  ALA   A CB  1 
ATOM   517  N N   . SER   A 1 93  ? 25.557  3.768   16.416  1.00 21.20 ? 72  SER   A N   1 
ATOM   518  C CA  . SER   A 1 93  ? 25.381  2.693   15.463  1.00 22.15 ? 72  SER   A CA  1 
ATOM   519  C C   . SER   A 1 93  ? 24.305  2.992   14.410  1.00 26.19 ? 72  SER   A C   1 
ATOM   520  O O   . SER   A 1 93  ? 24.470  2.672   13.219  1.00 23.34 ? 72  SER   A O   1 
ATOM   521  C CB  . SER   A 1 93  ? 25.099  1.413   16.137  1.00 24.13 ? 72  SER   A CB  1 
ATOM   522  O OG  . SER   A 1 93  ? 26.183  1.007   16.956  1.00 28.03 ? 72  SER   A OG  1 
ATOM   523  N N   . CYS   A 1 94  ? 23.164  3.542   14.871  1.00 25.11 ? 73  CYS   A N   1 
ATOM   524  C CA  . CYS   A 1 94  ? 22.048  3.837   13.999  1.00 22.57 ? 73  CYS   A CA  1 
ATOM   525  C C   . CYS   A 1 94  ? 22.461  4.943   13.034  1.00 24.14 ? 73  CYS   A C   1 
ATOM   526  O O   . CYS   A 1 94  ? 22.162  4.899   11.825  1.00 22.04 ? 73  CYS   A O   1 
ATOM   527  C CB  . CYS   A 1 94  ? 20.775  4.105   14.821  1.00 21.44 ? 73  CYS   A CB  1 
ATOM   528  S SG  . CYS   A 1 94  ? 20.220  2.595   15.637  1.00 23.11 ? 73  CYS   A SG  1 
ATOM   529  N N   . GLU   A 1 95  ? 23.096  5.977   13.584  1.00 22.96 ? 74  GLU   A N   1 
ATOM   530  C CA  . GLU   A 1 95  ? 23.555  7.067   12.730  1.00 24.87 ? 74  GLU   A CA  1 
ATOM   531  C C   . GLU   A 1 95  ? 24.482  6.527   11.627  1.00 26.87 ? 74  GLU   A C   1 
ATOM   532  O O   . GLU   A 1 95  ? 24.415  6.990   10.475  1.00 27.46 ? 74  GLU   A O   1 
ATOM   533  C CB  . GLU   A 1 95  ? 24.290  8.098   13.576  1.00 27.48 ? 74  GLU   A CB  1 
ATOM   534  C CG  . GLU   A 1 95  ? 24.741  9.289   12.739  1.00 37.73 ? 74  GLU   A CG  1 
ATOM   535  C CD  . GLU   A 1 95  ? 25.341  10.350  13.625  1.00 48.78 ? 74  GLU   A CD  1 
ATOM   536  O OE1 . GLU   A 1 95  ? 26.518  10.216  14.020  1.00 52.56 ? 74  GLU   A OE1 1 
ATOM   537  O OE2 . GLU   A 1 95  ? 24.590  11.280  13.968  1.00 54.36 ? 74  GLU   A OE2 1 
ATOM   538  N N   . GLU   A 1 96  ? 25.297  5.508   11.972  1.00 26.15 ? 75  GLU   A N   1 
ATOM   539  C CA  . GLU   A 1 96  ? 26.267  4.949   11.039  1.00 28.71 ? 75  GLU   A CA  1 
ATOM   540  C C   . GLU   A 1 96  ? 25.561  4.196   9.905   1.00 28.57 ? 75  GLU   A C   1 
ATOM   541  O O   . GLU   A 1 96  ? 26.037  4.195   8.752   1.00 25.82 ? 75  GLU   A O   1 
ATOM   542  C CB  . GLU   A 1 96  ? 27.280  4.063   11.768  1.00 29.51 ? 75  GLU   A CB  1 
ATOM   543  C CG  . GLU   A 1 96  ? 28.161  3.236   10.827  1.00 30.40 ? 75  GLU   A CG  1 
ATOM   544  C CD  . GLU   A 1 96  ? 28.994  4.055   9.847   1.00 30.65 ? 75  GLU   A CD  1 
ATOM   545  O OE1 . GLU   A 1 96  ? 29.067  5.298   9.947   1.00 27.28 ? 75  GLU   A OE1 1 
ATOM   546  O OE2 . GLU   A 1 96  ? 29.533  3.414   8.928   1.00 30.53 ? 75  GLU   A OE2 1 
ATOM   547  N N   . ILE   A 1 97  ? 24.460  3.488   10.234  1.00 23.97 ? 76  ILE   A N   1 
ATOM   548  C CA  . ILE   A 1 97  ? 23.702  2.769   9.220   1.00 22.29 ? 76  ILE   A CA  1 
ATOM   549  C C   . ILE   A 1 97  ? 23.185  3.779   8.194   1.00 23.17 ? 76  ILE   A C   1 
ATOM   550  O O   . ILE   A 1 97  ? 23.308  3.620   6.968   1.00 25.24 ? 76  ILE   A O   1 
ATOM   551  C CB  . ILE   A 1 97  ? 22.564  1.950   9.870   1.00 25.53 ? 76  ILE   A CB  1 
ATOM   552  C CG1 . ILE   A 1 97  ? 23.114  0.860   10.790  1.00 26.11 ? 76  ILE   A CG1 1 
ATOM   553  C CG2 . ILE   A 1 97  ? 21.663  1.327   8.805   1.00 26.43 ? 76  ILE   A CG2 1 
ATOM   554  C CD1 . ILE   A 1 97  ? 22.048  0.076   11.563  1.00 24.44 ? 76  ILE   A CD1 1 
ATOM   555  N N   . ILE   A 1 98  ? 22.569  4.848   8.681   1.00 23.88 ? 77  ILE   A N   1 
ATOM   556  C CA  . ILE   A 1 98  ? 22.100  5.843   7.737   1.00 25.88 ? 77  ILE   A CA  1 
ATOM   557  C C   . ILE   A 1 98  ? 23.289  6.426   6.954   1.00 28.67 ? 77  ILE   A C   1 
ATOM   558  O O   . ILE   A 1 98  ? 23.201  6.588   5.733   1.00 29.36 ? 77  ILE   A O   1 
ATOM   559  C CB  . ILE   A 1 98  ? 21.287  6.933   8.464   1.00 26.66 ? 77  ILE   A CB  1 
ATOM   560  C CG1 . ILE   A 1 98  ? 20.050  6.301   9.176   1.00 27.31 ? 77  ILE   A CG1 1 
ATOM   561  C CG2 . ILE   A 1 98  ? 20.885  8.037   7.491   1.00 26.46 ? 77  ILE   A CG2 1 
ATOM   562  C CD1 . ILE   A 1 98  ? 19.228  5.337   8.305   1.00 23.84 ? 77  ILE   A CD1 1 
ATOM   563  N N   . ASN   A 1 99  ? 24.370  6.797   7.654   1.00 30.71 ? 78  ASN   A N   1 
ATOM   564  C CA  . ASN   A 1 99  ? 25.560  7.343   7.005   1.00 31.15 ? 78  ASN   A CA  1 
ATOM   565  C C   . ASN   A 1 99  ? 26.050  6.434   5.888   1.00 29.01 ? 78  ASN   A C   1 
ATOM   566  O O   . ASN   A 1 99  ? 26.586  6.919   4.885   1.00 32.89 ? 78  ASN   A O   1 
ATOM   567  C CB  . ASN   A 1 99  ? 26.711  7.507   7.991   1.00 33.12 ? 78  ASN   A CB  1 
ATOM   568  C CG  . ASN   A 1 99  ? 26.487  8.719   8.853   1.00 36.45 ? 78  ASN   A CG  1 
ATOM   569  O OD1 . ASN   A 1 99  ? 25.677  9.591   8.504   1.00 39.91 ? 78  ASN   A OD1 1 
ATOM   570  N ND2 . ASN   A 1 99  ? 27.184  8.777   9.977   1.00 41.20 ? 78  ASN   A ND2 1 
ATOM   571  N N   . SER   A 1 100 ? 25.883  5.123   6.066   1.00 27.10 ? 79  SER   A N   1 
ATOM   572  C CA  . SER   A 1 100 ? 26.357  4.154   5.085   1.00 29.68 ? 79  SER   A CA  1 
ATOM   573  C C   . SER   A 1 100 ? 25.605  4.281   3.770   1.00 31.58 ? 79  SER   A C   1 
ATOM   574  O O   . SER   A 1 100 ? 26.187  4.037   2.715   1.00 29.34 ? 79  SER   A O   1 
ATOM   575  C CB  . SER   A 1 100 ? 26.284  2.718   5.579   1.00 29.03 ? 79  SER   A CB  1 
ATOM   576  O OG  . SER   A 1 100 ? 27.252  2.554   6.601   1.00 40.02 ? 79  SER   A OG  1 
ATOM   577  N N   . CYS   A 1 101 ? 24.292  4.576   3.858   1.00 27.12 ? 80  CYS   A N   1 
ATOM   578  C CA  . CYS   A 1 101 ? 23.488  4.816   2.670   1.00 27.07 ? 80  CYS   A CA  1 
ATOM   579  C C   . CYS   A 1 101 ? 23.933  6.092   1.957   1.00 26.16 ? 80  CYS   A C   1 
ATOM   580  O O   . CYS   A 1 101 ? 23.968  6.145   0.732   1.00 31.72 ? 80  CYS   A O   1 
ATOM   581  C CB  . CYS   A 1 101 ? 22.018  4.967   3.064   1.00 25.15 ? 80  CYS   A CB  1 
ATOM   582  S SG  . CYS   A 1 101 ? 20.917  4.618   1.676   1.00 27.73 ? 80  CYS   A SG  1 
ATOM   583  N N   . PHE   A 1 102 ? 24.196  7.154   2.715   1.00 26.05 ? 81  PHE   A N   1 
ATOM   584  C CA  . PHE   A 1 102 ? 24.685  8.393   2.124   1.00 30.62 ? 81  PHE   A CA  1 
ATOM   585  C C   . PHE   A 1 102 ? 26.079  8.201   1.515   1.00 34.14 ? 81  PHE   A C   1 
ATOM   586  O O   . PHE   A 1 102 ? 26.328  8.712   0.429   1.00 34.75 ? 81  PHE   A O   1 
ATOM   587  C CB  . PHE   A 1 102 ? 24.639  9.561   3.112   1.00 30.57 ? 81  PHE   A CB  1 
ATOM   588  C CG  . PHE   A 1 102 ? 23.252  10.173  3.240   1.00 36.12 ? 81  PHE   A CG  1 
ATOM   589  C CD1 . PHE   A 1 102 ? 22.835  11.160  2.349   1.00 38.10 ? 81  PHE   A CD1 1 
ATOM   590  C CD2 . PHE   A 1 102 ? 22.353  9.743   4.219   1.00 29.71 ? 81  PHE   A CD2 1 
ATOM   591  C CE1 . PHE   A 1 102 ? 21.566  11.715  2.449   1.00 32.57 ? 81  PHE   A CE1 1 
ATOM   592  C CE2 . PHE   A 1 102 ? 21.097  10.320  4.328   1.00 35.13 ? 81  PHE   A CE2 1 
ATOM   593  C CZ  . PHE   A 1 102 ? 20.695  11.299  3.441   1.00 34.52 ? 81  PHE   A CZ  1 
ATOM   594  N N   . ARG   A 1 103 ? 26.947  7.403   2.160   1.00 34.53 ? 82  ARG   A N   1 
ATOM   595  C CA  . ARG   A 1 103 ? 28.280  7.135   1.639   1.00 37.68 ? 82  ARG   A CA  1 
ATOM   596  C C   . ARG   A 1 103 ? 28.188  6.337   0.343   1.00 36.95 ? 82  ARG   A C   1 
ATOM   597  O O   . ARG   A 1 103 ? 28.945  6.585   -0.578  1.00 34.24 ? 82  ARG   A O   1 
ATOM   598  C CB  . ARG   A 1 103 ? 29.240  6.373   2.564   1.00 36.53 ? 82  ARG   A CB  1 
ATOM   599  C CG  . ARG   A 1 103 ? 29.932  7.179   3.654   1.00 47.88 ? 82  ARG   A CG  1 
ATOM   600  C CD  . ARG   A 1 103 ? 31.156  6.434   4.206   1.00 42.08 ? 82  ARG   A CD  1 
ATOM   601  N NE  . ARG   A 1 103 ? 30.856  5.051   4.590   1.00 43.12 ? 82  ARG   A NE  1 
ATOM   602  C CZ  . ARG   A 1 103 ? 30.301  4.695   5.747   1.00 38.05 ? 82  ARG   A CZ  1 
ATOM   603  N NH1 . ARG   A 1 103 ? 29.935  3.438   5.960   1.00 37.34 ? 82  ARG   A NH1 1 
ATOM   604  N NH2 . ARG   A 1 103 ? 30.083  5.614   6.661   1.00 34.99 ? 82  ARG   A NH2 1 
ATOM   605  N N   . ALA   A 1 104 ? 27.303  5.342   0.273   1.00 33.58 ? 83  ALA   A N   1 
ATOM   606  C CA  . ALA   A 1 104 ? 27.291  4.518   -0.925  1.00 31.86 ? 83  ALA   A CA  1 
ATOM   607  C C   . ALA   A 1 104 ? 26.533  5.191   -2.073  1.00 32.73 ? 83  ALA   A C   1 
ATOM   608  O O   . ALA   A 1 104 ? 26.922  5.032   -3.228  1.00 33.63 ? 83  ALA   A O   1 
ATOM   609  C CB  . ALA   A 1 104 ? 26.763  3.127   -0.639  1.00 28.05 ? 83  ALA   A CB  1 
ATOM   610  N N   . PHE   A 1 105 ? 25.444  5.917   -1.775  1.00 31.27 ? 84  PHE   A N   1 
ATOM   611  C CA  . PHE   A 1 105 ? 24.475  6.244   -2.808  1.00 29.47 ? 84  PHE   A CA  1 
ATOM   612  C C   . PHE   A 1 105 ? 24.248  7.739   -2.885  1.00 27.69 ? 84  PHE   A C   1 
ATOM   613  O O   . PHE   A 1 105 ? 23.656  8.190   -3.852  1.00 31.54 ? 84  PHE   A O   1 
ATOM   614  C CB  . PHE   A 1 105 ? 23.130  5.543   -2.624  1.00 26.95 ? 84  PHE   A CB  1 
ATOM   615  C CG  . PHE   A 1 105 ? 23.357  4.046   -2.597  1.00 27.20 ? 84  PHE   A CG  1 
ATOM   616  C CD1 . PHE   A 1 105 ? 24.101  3.424   -3.588  1.00 29.88 ? 84  PHE   A CD1 1 
ATOM   617  C CD2 . PHE   A 1 105 ? 22.859  3.268   -1.552  1.00 27.73 ? 84  PHE   A CD2 1 
ATOM   618  C CE1 . PHE   A 1 105 ? 24.334  2.052   -3.548  1.00 29.35 ? 84  PHE   A CE1 1 
ATOM   619  C CE2 . PHE   A 1 105 ? 23.074  1.892   -1.531  1.00 28.31 ? 84  PHE   A CE2 1 
ATOM   620  C CZ  . PHE   A 1 105 ? 23.809  1.288   -2.529  1.00 31.69 ? 84  PHE   A CZ  1 
ATOM   621  N N   . GLY   A 1 106 ? 24.721  8.495   -1.897  1.00 27.94 ? 85  GLY   A N   1 
ATOM   622  C CA  . GLY   A 1 106 ? 24.530  9.938   -1.939  1.00 28.12 ? 85  GLY   A CA  1 
ATOM   623  C C   . GLY   A 1 106 ? 23.144  10.400  -1.479  1.00 30.88 ? 85  GLY   A C   1 
ATOM   624  O O   . GLY   A 1 106 ? 22.848  11.595  -1.518  1.00 30.41 ? 85  GLY   A O   1 
ATOM   625  N N   . ARG   A 1 107 ? 22.284  9.473   -1.026  1.00 27.18 ? 86  ARG   A N   1 
ATOM   626  C CA  . ARG   A 1 107 ? 20.930  9.874   -0.627  1.00 26.87 ? 86  ARG   A CA  1 
ATOM   627  C C   . ARG   A 1 107 ? 20.325  8.698   0.134   1.00 27.54 ? 86  ARG   A C   1 
ATOM   628  O O   . ARG   A 1 107 ? 20.849  7.573   0.036   1.00 28.10 ? 86  ARG   A O   1 
ATOM   629  C CB  . ARG   A 1 107 ? 20.061  10.163  -1.872  1.00 27.34 ? 86  ARG   A CB  1 
ATOM   630  C CG  . ARG   A 1 107 ? 20.009  8.980   -2.837  1.00 28.87 ? 86  ARG   A CG  1 
ATOM   631  C CD  . ARG   A 1 107 ? 19.373  9.276   -4.217  1.00 33.14 ? 86  ARG   A CD  1 
ATOM   632  N NE  . ARG   A 1 107 ? 17.940  9.571   -4.076  1.00 34.15 ? 86  ARG   A NE  1 
ATOM   633  C CZ  . ARG   A 1 107 ? 17.211  10.270  -4.945  1.00 42.26 ? 86  ARG   A CZ  1 
ATOM   634  N NH1 . ARG   A 1 107 ? 17.736  10.633  -6.118  1.00 37.25 ? 86  ARG   A NH1 1 
ATOM   635  N NH2 . ARG   A 1 107 ? 15.948  10.564  -4.662  1.00 34.06 ? 86  ARG   A NH2 1 
ATOM   636  N N   . CYS   A 1 108 ? 19.214  8.961   0.846   1.00 28.23 ? 87  CYS   A N   1 
ATOM   637  C CA  . CYS   A 1 108 ? 18.498  7.917   1.569   1.00 26.41 ? 87  CYS   A CA  1 
ATOM   638  C C   . CYS   A 1 108 ? 17.005  8.260   1.569   1.00 27.41 ? 87  CYS   A C   1 
ATOM   639  O O   . CYS   A 1 108 ? 16.552  9.229   2.233   1.00 25.71 ? 87  CYS   A O   1 
ATOM   640  C CB  . CYS   A 1 108 ? 19.076  7.728   2.978   1.00 27.77 ? 87  CYS   A CB  1 
ATOM   641  S SG  . CYS   A 1 108 ? 18.319  6.347   3.892   1.00 28.82 ? 87  CYS   A SG  1 
ATOM   642  N N   . ASP   A 1 109 ? 16.259  7.468   0.776   1.00 24.73 ? 88  ASP   A N   1 
ATOM   643  C CA  . ASP   A 1 109 ? 14.869  7.817   0.481   1.00 26.40 ? 88  ASP   A CA  1 
ATOM   644  C C   . ASP   A 1 109 ? 13.887  7.085   1.390   1.00 24.46 ? 88  ASP   A C   1 
ATOM   645  O O   . ASP   A 1 109 ? 12.811  7.615   1.684   1.00 24.52 ? 88  ASP   A O   1 
ATOM   646  C CB  . ASP   A 1 109 ? 14.561  7.590   -0.991  1.00 26.61 ? 88  ASP   A CB  1 
ATOM   647  C CG  . ASP   A 1 109 ? 15.430  8.487   -1.876  1.00 30.64 ? 88  ASP   A CG  1 
ATOM   648  O OD1 . ASP   A 1 109 ? 15.079  9.678   -2.033  1.00 30.25 ? 88  ASP   A OD1 1 
ATOM   649  O OD2 . ASP   A 1 109 ? 16.508  8.021   -2.290  1.00 30.54 ? 88  ASP   A OD2 1 
ATOM   650  N N   . VAL   A 1 110 ? 14.227  5.827   1.701   1.00 24.45 ? 89  VAL   A N   1 
ATOM   651  C CA  . VAL   A 1 110 ? 13.350  4.894   2.397   1.00 23.16 ? 89  VAL   A CA  1 
ATOM   652  C C   . VAL   A 1 110 ? 14.147  4.212   3.516   1.00 23.00 ? 89  VAL   A C   1 
ATOM   653  O O   . VAL   A 1 110 ? 15.296  3.813   3.310   1.00 23.89 ? 89  VAL   A O   1 
ATOM   654  C CB  . VAL   A 1 110 ? 12.816  3.875   1.372   1.00 23.89 ? 89  VAL   A CB  1 
ATOM   655  C CG1 . VAL   A 1 110 ? 12.171  2.629   2.006   1.00 22.77 ? 89  VAL   A CG1 1 
ATOM   656  C CG2 . VAL   A 1 110 ? 11.870  4.520   0.348   1.00 24.36 ? 89  VAL   A CG2 1 
ATOM   657  N N   . LEU   A 1 111 ? 13.532  4.116   4.707   1.00 21.13 ? 90  LEU   A N   1 
ATOM   658  C CA  . LEU   A 1 111 ? 14.017  3.292   5.801   1.00 21.96 ? 90  LEU   A CA  1 
ATOM   659  C C   . LEU   A 1 111 ? 12.976  2.207   6.107   1.00 22.10 ? 90  LEU   A C   1 
ATOM   660  O O   . LEU   A 1 111 ? 11.813  2.524   6.359   1.00 20.19 ? 90  LEU   A O   1 
ATOM   661  C CB  . LEU   A 1 111 ? 14.246  4.187   7.022   1.00 20.33 ? 90  LEU   A CB  1 
ATOM   662  C CG  . LEU   A 1 111 ? 14.516  3.466   8.356   1.00 19.27 ? 90  LEU   A CG  1 
ATOM   663  C CD1 . LEU   A 1 111 ? 15.812  2.653   8.304   1.00 23.22 ? 90  LEU   A CD1 1 
ATOM   664  C CD2 . LEU   A 1 111 ? 14.571  4.523   9.474   1.00 20.02 ? 90  LEU   A CD2 1 
ATOM   665  N N   . VAL   A 1 112 ? 13.407  0.939   6.126   1.00 20.87 ? 91  VAL   A N   1 
ATOM   666  C CA  . VAL   A 1 112 ? 12.566  -0.172  6.537   1.00 20.63 ? 91  VAL   A CA  1 
ATOM   667  C C   . VAL   A 1 112 ? 13.123  -0.782  7.841   1.00 23.98 ? 91  VAL   A C   1 
ATOM   668  O O   . VAL   A 1 112 ? 14.187  -1.405  7.835   1.00 23.13 ? 91  VAL   A O   1 
ATOM   669  C CB  . VAL   A 1 112 ? 12.339  -1.269  5.469   1.00 21.84 ? 91  VAL   A CB  1 
ATOM   670  C CG1 . VAL   A 1 112 ? 11.373  -2.349  5.992   1.00 19.90 ? 91  VAL   A CG1 1 
ATOM   671  C CG2 . VAL   A 1 112 ? 11.779  -0.681  4.167   1.00 21.31 ? 91  VAL   A CG2 1 
ATOM   672  N N   . ASN   A 1 113 ? 12.386  -0.600  8.964   1.00 21.04 ? 92  ASN   A N   1 
ATOM   673  C CA  . ASN   A 1 113 ? 12.745  -1.155  10.253  1.00 19.63 ? 92  ASN   A CA  1 
ATOM   674  C C   . ASN   A 1 113 ? 12.193  -2.565  10.348  1.00 21.43 ? 92  ASN   A C   1 
ATOM   675  O O   . ASN   A 1 113 ? 11.029  -2.762  10.733  1.00 20.52 ? 92  ASN   A O   1 
ATOM   676  C CB  . ASN   A 1 113 ? 12.261  -0.292  11.407  1.00 19.81 ? 92  ASN   A CB  1 
ATOM   677  C CG  . ASN   A 1 113 ? 13.035  0.998   11.489  1.00 21.72 ? 92  ASN   A CG  1 
ATOM   678  O OD1 . ASN   A 1 113 ? 14.266  0.954   11.605  1.00 20.62 ? 92  ASN   A OD1 1 
ATOM   679  N ND2 . ASN   A 1 113 ? 12.341  2.127   11.450  1.00 17.90 ? 92  ASN   A ND2 1 
ATOM   680  N N   . ASN   A 1 114 ? 13.035  -3.545  9.991   1.00 22.83 ? 93  ASN   A N   1 
ATOM   681  C CA  . ASN   A 1 114 ? 12.605  -4.937  9.875   1.00 20.51 ? 93  ASN   A CA  1 
ATOM   682  C C   . ASN   A 1 114 ? 13.284  -5.811  10.932  1.00 21.05 ? 93  ASN   A C   1 
ATOM   683  O O   . ASN   A 1 114 ? 12.673  -6.778  11.392  1.00 20.83 ? 93  ASN   A O   1 
ATOM   684  C CB  . ASN   A 1 114 ? 12.839  -5.475  8.462   1.00 21.63 ? 93  ASN   A CB  1 
ATOM   685  C CG  . ASN   A 1 114 ? 12.764  -6.983  8.390   1.00 22.72 ? 93  ASN   A CG  1 
ATOM   686  O OD1 . ASN   A 1 114 ? 11.667  -7.551  8.273   1.00 22.68 ? 93  ASN   A OD1 1 
ATOM   687  N ND2 . ASN   A 1 114 ? 13.913  -7.657  8.435   1.00 24.10 ? 93  ASN   A ND2 1 
ATOM   688  N N   . ALA   A 1 115 ? 14.543  -5.496  11.304  1.00 21.63 ? 94  ALA   A N   1 
ATOM   689  C CA  . ALA   A 1 115 ? 15.327  -6.299  12.237  1.00 20.81 ? 94  ALA   A CA  1 
ATOM   690  C C   . ALA   A 1 115 ? 14.542  -6.492  13.542  1.00 24.18 ? 94  ALA   A C   1 
ATOM   691  O O   . ALA   A 1 115 ? 13.945  -5.535  14.044  1.00 23.18 ? 94  ALA   A O   1 
ATOM   692  C CB  . ALA   A 1 115 ? 16.673  -5.668  12.502  1.00 20.51 ? 94  ALA   A CB  1 
ATOM   693  N N   . SER   A 1 116 ? 14.563  -7.716  14.082  1.00 22.64 ? 95  SER   A N   1 
ATOM   694  C CA  . SER   A 1 116 ? 13.765  -7.976  15.274  1.00 25.34 ? 95  SER   A CA  1 
ATOM   695  C C   . SER   A 1 116 ? 14.309  -9.160  16.066  1.00 24.32 ? 95  SER   A C   1 
ATOM   696  O O   . SER   A 1 116 ? 14.518  -10.209 15.483  1.00 24.42 ? 95  SER   A O   1 
ATOM   697  C CB  . SER   A 1 116 ? 12.369  -8.280  14.850  1.00 25.01 ? 95  SER   A CB  1 
ATOM   698  O OG  . SER   A 1 116 ? 11.611  -8.611  16.002  1.00 30.64 ? 95  SER   A OG  1 
ATOM   699  N N   . ALA   A 1 117 ? 14.561  -8.985  17.371  1.00 26.04 ? 96  ALA   A N   1 
ATOM   700  C CA  . ALA   A 1 117 ? 14.844  -10.106 18.272  1.00 24.70 ? 96  ALA   A CA  1 
ATOM   701  C C   . ALA   A 1 117 ? 13.507  -10.638 18.769  1.00 25.01 ? 96  ALA   A C   1 
ATOM   702  O O   . ALA   A 1 117 ? 12.583  -9.853  18.966  1.00 20.72 ? 96  ALA   A O   1 
ATOM   703  C CB  . ALA   A 1 117 ? 15.698  -9.647  19.452  1.00 24.78 ? 96  ALA   A CB  1 
ATOM   704  N N   . PHE   A 1 118 ? 13.402  -11.968 18.929  1.00 22.79 ? 97  PHE   A N   1 
ATOM   705  C CA  . PHE   A 1 118 ? 12.128  -12.549 19.302  1.00 25.24 ? 97  PHE   A CA  1 
ATOM   706  C C   . PHE   A 1 118 ? 12.443  -13.779 20.142  1.00 29.00 ? 97  PHE   A C   1 
ATOM   707  O O   . PHE   A 1 118 ? 12.995  -14.721 19.624  1.00 28.34 ? 97  PHE   A O   1 
ATOM   708  C CB  . PHE   A 1 118 ? 11.285  -12.887 18.055  1.00 26.96 ? 97  PHE   A CB  1 
ATOM   709  C CG  . PHE   A 1 118 ? 10.023  -13.704 18.325  1.00 30.37 ? 97  PHE   A CG  1 
ATOM   710  C CD1 . PHE   A 1 118 ? 8.824   -13.093 18.685  1.00 26.85 ? 97  PHE   A CD1 1 
ATOM   711  C CD2 . PHE   A 1 118 ? 10.039  -15.101 18.252  1.00 38.09 ? 97  PHE   A CD2 1 
ATOM   712  C CE1 . PHE   A 1 118 ? 7.678   -13.837 18.941  1.00 29.85 ? 97  PHE   A CE1 1 
ATOM   713  C CE2 . PHE   A 1 118 ? 8.886   -15.856 18.509  1.00 40.54 ? 97  PHE   A CE2 1 
ATOM   714  C CZ  . PHE   A 1 118 ? 7.697   -15.220 18.848  1.00 34.73 ? 97  PHE   A CZ  1 
ATOM   715  N N   . TYR   A 1 119 ? 12.077  -13.785 21.423  1.00 25.85 ? 98  TYR   A N   1 
ATOM   716  C CA  . TYR   A 1 119 ? 12.224  -14.998 22.217  1.00 25.79 ? 98  TYR   A CA  1 
ATOM   717  C C   . TYR   A 1 119 ? 11.469  -14.796 23.525  1.00 24.32 ? 98  TYR   A C   1 
ATOM   718  O O   . TYR   A 1 119 ? 11.194  -13.667 23.932  1.00 23.09 ? 98  TYR   A O   1 
ATOM   719  C CB  . TYR   A 1 119 ? 13.677  -15.421 22.520  1.00 25.51 ? 98  TYR   A CB  1 
ATOM   720  C CG  . TYR   A 1 119 ? 14.579  -14.319 23.044  1.00 23.56 ? 98  TYR   A CG  1 
ATOM   721  C CD1 . TYR   A 1 119 ? 14.611  -14.005 24.403  1.00 27.21 ? 98  TYR   A CD1 1 
ATOM   722  C CD2 . TYR   A 1 119 ? 15.396  -13.586 22.186  1.00 23.58 ? 98  TYR   A CD2 1 
ATOM   723  C CE1 . TYR   A 1 119 ? 15.418  -12.981 24.897  1.00 26.57 ? 98  TYR   A CE1 1 
ATOM   724  C CE2 . TYR   A 1 119 ? 16.238  -12.590 22.675  1.00 27.94 ? 98  TYR   A CE2 1 
ATOM   725  C CZ  . TYR   A 1 119 ? 16.269  -12.299 24.036  1.00 28.68 ? 98  TYR   A CZ  1 
ATOM   726  O OH  . TYR   A 1 119 ? 17.087  -11.307 24.534  1.00 26.45 ? 98  TYR   A OH  1 
ATOM   727  N N   . PRO   A 1 120 ? 11.119  -15.885 24.229  1.00 25.45 ? 99  PRO   A N   1 
ATOM   728  C CA  . PRO   A 1 120 ? 10.329  -15.752 25.454  1.00 27.36 ? 99  PRO   A CA  1 
ATOM   729  C C   . PRO   A 1 120 ? 11.108  -15.105 26.604  1.00 26.92 ? 99  PRO   A C   1 
ATOM   730  O O   . PRO   A 1 120 ? 12.327  -15.283 26.733  1.00 25.43 ? 99  PRO   A O   1 
ATOM   731  C CB  . PRO   A 1 120 ? 9.864   -17.209 25.750  1.00 31.65 ? 99  PRO   A CB  1 
ATOM   732  C CG  . PRO   A 1 120 ? 10.776  -18.090 24.942  1.00 27.04 ? 99  PRO   A CG  1 
ATOM   733  C CD  . PRO   A 1 120 ? 11.450  -17.273 23.867  1.00 27.82 ? 99  PRO   A CD  1 
ATOM   734  N N   . THR   A 1 121 ? 10.391  -14.312 27.415  1.00 23.31 ? 100 THR   A N   1 
ATOM   735  C CA  . THR   A 1 121 ? 10.966  -13.668 28.589  1.00 22.95 ? 100 THR   A CA  1 
ATOM   736  C C   . THR   A 1 121 ? 9.946   -13.799 29.711  1.00 24.43 ? 100 THR   A C   1 
ATOM   737  O O   . THR   A 1 121 ? 9.259   -12.832 30.045  1.00 24.59 ? 100 THR   A O   1 
ATOM   738  C CB  . THR   A 1 121 ? 11.314  -12.209 28.315  1.00 24.49 ? 100 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 121 ? 10.120  -11.528 27.913  1.00 25.78 ? 100 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 121 ? 12.407  -12.088 27.268  1.00 23.51 ? 100 THR   A CG2 1 
ATOM   741  N N   . PRO   A 1 122 ? 9.779   -15.019 30.277  1.00 25.56 ? 101 PRO   A N   1 
ATOM   742  C CA  . PRO   A 1 122 ? 8.730   -15.256 31.269  1.00 25.84 ? 101 PRO   A CA  1 
ATOM   743  C C   . PRO   A 1 122 ? 8.882   -14.316 32.469  1.00 27.84 ? 101 PRO   A C   1 
ATOM   744  O O   . PRO   A 1 122 ? 9.999   -13.980 32.863  1.00 27.73 ? 101 PRO   A O   1 
ATOM   745  C CB  . PRO   A 1 122 ? 8.876   -16.722 31.694  1.00 27.79 ? 101 PRO   A CB  1 
ATOM   746  C CG  . PRO   A 1 122 ? 10.002  -17.269 30.851  1.00 29.76 ? 101 PRO   A CG  1 
ATOM   747  C CD  . PRO   A 1 122 ? 10.610  -16.208 29.981  1.00 26.78 ? 101 PRO   A CD  1 
ATOM   748  N N   . LEU   A 1 123 ? 7.741   -13.912 33.046  1.00 25.15 ? 102 LEU   A N   1 
ATOM   749  C CA  . LEU   A 1 123 ? 7.728   -13.041 34.208  1.00 27.73 ? 102 LEU   A CA  1 
ATOM   750  C C   . LEU   A 1 123 ? 8.139   -13.800 35.476  1.00 32.82 ? 102 LEU   A C   1 
ATOM   751  O O   . LEU   A 1 123 ? 8.779   -13.218 36.360  1.00 32.61 ? 102 LEU   A O   1 
ATOM   752  C CB  . LEU   A 1 123 ? 6.339   -12.409 34.346  1.00 26.42 ? 102 LEU   A CB  1 
ATOM   753  C CG  . LEU   A 1 123 ? 5.997   -11.305 33.332  1.00 24.06 ? 102 LEU   A CG  1 
ATOM   754  C CD1 . LEU   A 1 123 ? 4.544   -10.936 33.461  1.00 21.37 ? 102 LEU   A CD1 1 
ATOM   755  C CD2 . LEU   A 1 123 ? 6.867   -10.075 33.524  1.00 25.29 ? 102 LEU   A CD2 1 
ATOM   756  N N   . VAL   A 1 124 ? 7.732   -15.075 35.569  1.00 34.02 ? 103 VAL   A N   1 
ATOM   757  C CA  . VAL   A 1 124 ? 7.942   -15.911 36.752  1.00 41.95 ? 103 VAL   A CA  1 
ATOM   758  C C   . VAL   A 1 124 ? 8.999   -16.996 36.463  1.00 44.98 ? 103 VAL   A C   1 
ATOM   759  O O   . VAL   A 1 124 ? 8.855   -17.668 35.418  1.00 39.24 ? 103 VAL   A O   1 
ATOM   760  C CB  . VAL   A 1 124 ? 6.625   -16.527 37.267  1.00 45.57 ? 103 VAL   A CB  1 
ATOM   761  C CG1 . VAL   A 1 124 ? 6.852   -17.469 38.450  1.00 52.82 ? 103 VAL   A CG1 1 
ATOM   762  C CG2 . VAL   A 1 124 ? 5.616   -15.450 37.645  1.00 42.24 ? 103 VAL   A CG2 1 
ATOM   763  N N   . GLY   A 1 134 ? 21.857  -18.887 29.199  1.00 72.35 ? 113 GLY   A N   1 
ATOM   764  C CA  . GLY   A 1 134 ? 20.732  -18.019 29.604  1.00 65.73 ? 113 GLY   A CA  1 
ATOM   765  C C   . GLY   A 1 134 ? 21.157  -16.553 29.667  1.00 61.90 ? 113 GLY   A C   1 
ATOM   766  O O   . GLY   A 1 134 ? 22.156  -16.217 30.305  1.00 60.43 ? 113 GLY   A O   1 
ATOM   767  N N   . LYS   A 1 135 ? 20.388  -15.689 28.994  1.00 48.71 ? 114 LYS   A N   1 
ATOM   768  C CA  . LYS   A 1 135 ? 20.624  -14.256 29.022  1.00 40.05 ? 114 LYS   A CA  1 
ATOM   769  C C   . LYS   A 1 135 ? 20.146  -13.684 30.354  1.00 33.93 ? 114 LYS   A C   1 
ATOM   770  O O   . LYS   A 1 135 ? 19.085  -14.083 30.842  1.00 32.68 ? 114 LYS   A O   1 
ATOM   771  C CB  . LYS   A 1 135 ? 19.836  -13.612 27.875  1.00 42.17 ? 114 LYS   A CB  1 
ATOM   772  C CG  . LYS   A 1 135 ? 20.287  -14.100 26.509  1.00 43.93 ? 114 LYS   A CG  1 
ATOM   773  C CD  . LYS   A 1 135 ? 19.653  -13.383 25.330  1.00 45.28 ? 114 LYS   A CD  1 
ATOM   774  C CE  . LYS   A 1 135 ? 20.482  -13.493 24.084  1.00 40.11 ? 114 LYS   A CE  1 
ATOM   775  N NZ  . LYS   A 1 135 ? 19.866  -14.413 23.139  1.00 46.93 ? 114 LYS   A NZ  1 
ATOM   776  N N   . THR   A 1 136 ? 20.893  -12.712 30.900  1.00 30.68 ? 115 THR   A N   1 
ATOM   777  C CA  . THR   A 1 136 ? 20.408  -11.961 32.053  1.00 31.49 ? 115 THR   A CA  1 
ATOM   778  C C   . THR   A 1 136 ? 19.162  -11.167 31.642  1.00 32.06 ? 115 THR   A C   1 
ATOM   779  O O   . THR   A 1 136 ? 18.931  -10.939 30.443  1.00 27.47 ? 115 THR   A O   1 
ATOM   780  C CB  . THR   A 1 136 ? 21.479  -11.025 32.612  1.00 32.03 ? 115 THR   A CB  1 
ATOM   781  O OG1 . THR   A 1 136 ? 21.698  -10.070 31.578  1.00 30.32 ? 115 THR   A OG1 1 
ATOM   782  C CG2 . THR   A 1 136 ? 22.743  -11.745 33.066  1.00 36.98 ? 115 THR   A CG2 1 
ATOM   783  N N   . VAL   A 1 137 ? 18.390  -10.705 32.634  1.00 27.98 ? 116 VAL   A N   1 
ATOM   784  C CA  . VAL   A 1 137 ? 17.211  -9.897  32.323  1.00 29.59 ? 116 VAL   A CA  1 
ATOM   785  C C   . VAL   A 1 137 ? 17.652  -8.568  31.695  1.00 29.10 ? 116 VAL   A C   1 
ATOM   786  O O   . VAL   A 1 137 ? 17.013  -8.059  30.773  1.00 24.47 ? 116 VAL   A O   1 
ATOM   787  C CB  . VAL   A 1 137 ? 16.192  -9.713  33.473  1.00 31.09 ? 116 VAL   A CB  1 
ATOM   788  C CG1 . VAL   A 1 137 ? 16.645  -8.681  34.478  1.00 30.78 ? 116 VAL   A CG1 1 
ATOM   789  C CG2 . VAL   A 1 137 ? 14.833  -9.263  32.948  1.00 34.09 ? 116 VAL   A CG2 1 
ATOM   790  N N   . GLU   A 1 138 ? 18.810  -8.044  32.119  1.00 27.81 ? 117 GLU   A N   1 
ATOM   791  C CA  . GLU   A 1 138 ? 19.349  -6.821  31.518  1.00 31.92 ? 117 GLU   A CA  1 
ATOM   792  C C   . GLU   A 1 138 ? 19.513  -6.990  30.002  1.00 27.45 ? 117 GLU   A C   1 
ATOM   793  O O   . GLU   A 1 138 ? 19.253  -6.061  29.231  1.00 24.37 ? 117 GLU   A O   1 
ATOM   794  C CB  . GLU   A 1 138 ? 20.770  -6.451  31.967  1.00 31.07 ? 117 GLU   A CB  1 
ATOM   795  C CG  . GLU   A 1 138 ? 20.893  -6.007  33.419  1.00 42.28 ? 117 GLU   A CG  1 
ATOM   796  C CD  . GLU   A 1 138 ? 20.836  -7.070  34.514  1.00 47.25 ? 117 GLU   A CD  1 
ATOM   797  O OE1 . GLU   A 1 138 ? 20.551  -8.256  34.255  1.00 40.05 ? 117 GLU   A OE1 1 
ATOM   798  O OE2 . GLU   A 1 138 ? 21.092  -6.685  35.675  1.00 62.43 ? 117 GLU   A OE2 1 
ATOM   799  N N   . THR   A 1 139 ? 19.993  -8.173  29.597  1.00 27.98 ? 118 THR   A N   1 
ATOM   800  C CA  . THR   A 1 139 ? 20.287  -8.480  28.204  1.00 29.44 ? 118 THR   A CA  1 
ATOM   801  C C   . THR   A 1 139 ? 18.983  -8.612  27.416  1.00 25.57 ? 118 THR   A C   1 
ATOM   802  O O   . THR   A 1 139 ? 18.893  -8.163  26.270  1.00 26.19 ? 118 THR   A O   1 
ATOM   803  C CB  . THR   A 1 139 ? 21.105  -9.774  28.109  1.00 30.21 ? 118 THR   A CB  1 
ATOM   804  O OG1 . THR   A 1 139 ? 22.411  -9.443  28.586  1.00 31.22 ? 118 THR   A OG1 1 
ATOM   805  C CG2 . THR   A 1 139 ? 21.221  -10.260 26.677  1.00 28.45 ? 118 THR   A CG2 1 
ATOM   806  N N   . GLN   A 1 140 ? 18.035  -9.345  28.007  1.00 24.32 ? 119 GLN   A N   1 
ATOM   807  C CA  . GLN   A 1 140 ? 16.708  -9.538  27.447  1.00 23.69 ? 119 GLN   A CA  1 
ATOM   808  C C   . GLN   A 1 140 ? 16.057  -8.190  27.154  1.00 21.85 ? 119 GLN   A C   1 
ATOM   809  O O   . GLN   A 1 140 ? 15.565  -8.009  26.043  1.00 24.41 ? 119 GLN   A O   1 
ATOM   810  C CB  . GLN   A 1 140 ? 15.832  -10.338 28.401  1.00 26.56 ? 119 GLN   A CB  1 
ATOM   811  C CG  . GLN   A 1 140 ? 16.277  -11.784 28.597  1.00 32.15 ? 119 GLN   A CG  1 
ATOM   812  C CD  . GLN   A 1 140 ? 15.524  -12.422 29.745  1.00 32.48 ? 119 GLN   A CD  1 
ATOM   813  O OE1 . GLN   A 1 140 ? 14.341  -12.140 29.955  1.00 37.37 ? 119 GLN   A OE1 1 
ATOM   814  N NE2 . GLN   A 1 140 ? 16.203  -13.226 30.552  1.00 33.91 ? 119 GLN   A NE2 1 
ATOM   815  N N   . VAL   A 1 141 ? 16.091  -7.250  28.114  1.00 20.94 ? 120 VAL   A N   1 
ATOM   816  C CA  . VAL   A 1 141 ? 15.507  -5.926  27.866  1.00 23.01 ? 120 VAL   A CA  1 
ATOM   817  C C   . VAL   A 1 141 ? 16.265  -5.211  26.741  1.00 24.77 ? 120 VAL   A C   1 
ATOM   818  O O   . VAL   A 1 141 ? 15.678  -4.666  25.790  1.00 21.04 ? 120 VAL   A O   1 
ATOM   819  C CB  . VAL   A 1 141 ? 15.571  -5.122  29.175  1.00 23.30 ? 120 VAL   A CB  1 
ATOM   820  C CG1 . VAL   A 1 141 ? 15.301  -3.629  28.976  1.00 20.40 ? 120 VAL   A CG1 1 
ATOM   821  C CG2 . VAL   A 1 141 ? 14.637  -5.704  30.232  1.00 19.75 ? 120 VAL   A CG2 1 
ATOM   822  N N   . ALA   A 1 142 ? 17.602  -5.252  26.815  1.00 22.27 ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 142 ? 18.431  -4.573  25.830  1.00 21.51 ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 142 ? 18.135  -5.100  24.419  1.00 22.13 ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 142 ? 18.017  -4.313  23.482  1.00 20.78 ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 142 ? 19.907  -4.743  26.180  1.00 20.81 ? 121 ALA   A CB  1 
ATOM   827  N N   . GLU   A 1 143 ? 18.084  -6.431  24.237  1.00 20.43 ? 122 GLU   A N   1 
ATOM   828  C CA  . GLU   A 1 143 ? 17.897  -6.951  22.892  1.00 23.74 ? 122 GLU   A CA  1 
ATOM   829  C C   . GLU   A 1 143 ? 16.460  -6.746  22.401  1.00 21.95 ? 122 GLU   A C   1 
ATOM   830  O O   . GLU   A 1 143 ? 16.242  -6.336  21.269  1.00 22.24 ? 122 GLU   A O   1 
ATOM   831  C CB  . GLU   A 1 143 ? 18.223  -8.444  22.784  1.00 24.58 ? 122 GLU   A CB  1 
ATOM   832  C CG  . GLU   A 1 143 ? 19.703  -8.698  23.091  1.00 28.17 ? 122 GLU   A CG  1 
ATOM   833  C CD  . GLU   A 1 143 ? 20.143  -10.161 23.094  1.00 31.74 ? 122 GLU   A CD  1 
ATOM   834  O OE1 . GLU   A 1 143 ? 19.261  -11.044 23.121  1.00 32.44 ? 122 GLU   A OE1 1 
ATOM   835  O OE2 . GLU   A 1 143 ? 21.372  -10.415 23.095  1.00 35.63 ? 122 GLU   A OE2 1 
ATOM   836  N N   . LEU   A 1 144 ? 15.473  -7.101  23.222  1.00 20.19 ? 123 LEU   A N   1 
ATOM   837  C CA  . LEU   A 1 144 ? 14.096  -7.085  22.750  1.00 20.16 ? 123 LEU   A CA  1 
ATOM   838  C C   . LEU   A 1 144 ? 13.572  -5.668  22.584  1.00 19.80 ? 123 LEU   A C   1 
ATOM   839  O O   . LEU   A 1 144 ? 12.966  -5.364  21.548  1.00 21.72 ? 123 LEU   A O   1 
ATOM   840  C CB  . LEU   A 1 144 ? 13.193  -7.971  23.602  1.00 22.89 ? 123 LEU   A CB  1 
ATOM   841  C CG  . LEU   A 1 144 ? 13.504  -9.466  23.447  1.00 25.40 ? 123 LEU   A CG  1 
ATOM   842  C CD1 . LEU   A 1 144 ? 12.907  -10.200 24.592  1.00 27.92 ? 123 LEU   A CD1 1 
ATOM   843  C CD2 . LEU   A 1 144 ? 12.876  -9.920  22.127  1.00 28.22 ? 123 LEU   A CD2 1 
ATOM   844  N N   . ILE   A 1 145 ? 13.899  -4.782  23.518  1.00 18.48 ? 124 ILE   A N   1 
ATOM   845  C CA  . ILE   A 1 145 ? 13.460  -3.394  23.384  1.00 20.33 ? 124 ILE   A CA  1 
ATOM   846  C C   . ILE   A 1 145 ? 14.339  -2.615  22.398  1.00 23.36 ? 124 ILE   A C   1 
ATOM   847  O O   . ILE   A 1 145 ? 13.854  -1.758  21.648  1.00 23.17 ? 124 ILE   A O   1 
ATOM   848  C CB  . ILE   A 1 145 ? 13.295  -2.712  24.746  1.00 18.81 ? 124 ILE   A CB  1 
ATOM   849  C CG1 . ILE   A 1 145 ? 12.451  -3.621  25.682  1.00 19.92 ? 124 ILE   A CG1 1 
ATOM   850  C CG2 . ILE   A 1 145 ? 12.700  -1.306  24.596  1.00 20.84 ? 124 ILE   A CG2 1 
ATOM   851  C CD1 . ILE   A 1 145 ? 11.006  -3.831  25.251  1.00 23.94 ? 124 ILE   A CD1 1 
ATOM   852  N N   . GLY   A 1 146 ? 15.649  -2.884  22.417  1.00 21.83 ? 125 GLY   A N   1 
ATOM   853  C CA  . GLY   A 1 146 ? 16.549  -2.239  21.463  1.00 20.71 ? 125 GLY   A CA  1 
ATOM   854  C C   . GLY   A 1 146 ? 16.176  -2.529  20.005  1.00 19.89 ? 125 GLY   A C   1 
ATOM   855  O O   . GLY   A 1 146 ? 15.976  -1.596  19.225  1.00 22.02 ? 125 GLY   A O   1 
ATOM   856  N N   . THR   A 1 147 ? 16.051  -3.808  19.627  1.00 19.06 ? 126 THR   A N   1 
ATOM   857  C CA  . THR   A 1 147 ? 15.868  -4.122  18.211  1.00 21.98 ? 126 THR   A CA  1 
ATOM   858  C C   . THR   A 1 147 ? 14.479  -3.706  17.747  1.00 23.07 ? 126 THR   A C   1 
ATOM   859  O O   . THR   A 1 147 ? 14.331  -3.144  16.669  1.00 22.37 ? 126 THR   A O   1 
ATOM   860  C CB  . THR   A 1 147 ? 16.070  -5.607  17.892  1.00 22.70 ? 126 THR   A CB  1 
ATOM   861  O OG1 . THR   A 1 147 ? 15.108  -6.285  18.682  1.00 26.91 ? 126 THR   A OG1 1 
ATOM   862  C CG2 . THR   A 1 147 ? 17.441  -6.119  18.293  1.00 22.90 ? 126 THR   A CG2 1 
ATOM   863  N N   . ASN   A 1 148 ? 13.474  -3.949  18.594  1.00 20.62 ? 127 ASN   A N   1 
ATOM   864  C CA  . ASN   A 1 148 ? 12.104  -3.795  18.144  1.00 19.77 ? 127 ASN   A CA  1 
ATOM   865  C C   . ASN   A 1 148 ? 11.637  -2.349  18.225  1.00 19.68 ? 127 ASN   A C   1 
ATOM   866  O O   . ASN   A 1 148 ? 10.620  -2.037  17.606  1.00 21.37 ? 127 ASN   A O   1 
ATOM   867  C CB  . ASN   A 1 148 ? 11.181  -4.691  18.951  1.00 22.62 ? 127 ASN   A CB  1 
ATOM   868  C CG  . ASN   A 1 148 ? 11.377  -6.123  18.513  1.00 24.21 ? 127 ASN   A CG  1 
ATOM   869  O OD1 . ASN   A 1 148 ? 11.087  -6.434  17.358  1.00 25.81 ? 127 ASN   A OD1 1 
ATOM   870  N ND2 . ASN   A 1 148 ? 11.837  -7.004  19.388  1.00 23.06 ? 127 ASN   A ND2 1 
ATOM   871  N N   . ALA   A 1 149 ? 12.309  -1.500  19.014  1.00 18.36 ? 128 ALA   A N   1 
ATOM   872  C CA  . ALA   A 1 149 ? 11.745  -0.185  19.299  1.00 17.49 ? 128 ALA   A CA  1 
ATOM   873  C C   . ALA   A 1 149 ? 12.778  0.947   19.334  1.00 19.12 ? 128 ALA   A C   1 
ATOM   874  O O   . ALA   A 1 149 ? 12.607  1.984   18.673  1.00 18.89 ? 128 ALA   A O   1 
ATOM   875  C CB  . ALA   A 1 149 ? 10.975  -0.241  20.617  1.00 18.90 ? 128 ALA   A CB  1 
ATOM   876  N N   . ILE   A 1 150 ? 13.825  0.790   20.153  1.00 20.71 ? 129 ILE   A N   1 
ATOM   877  C CA  . ILE   A 1 150 ? 14.765  1.895   20.344  1.00 19.09 ? 129 ILE   A CA  1 
ATOM   878  C C   . ILE   A 1 150 ? 15.583  2.132   19.078  1.00 17.52 ? 129 ILE   A C   1 
ATOM   879  O O   . ILE   A 1 150 ? 15.776  3.277   18.655  1.00 16.91 ? 129 ILE   A O   1 
ATOM   880  C CB  . ILE   A 1 150 ? 15.637  1.688   21.611  1.00 21.48 ? 129 ILE   A CB  1 
ATOM   881  C CG1 . ILE   A 1 150 ? 14.703  1.652   22.908  1.00 24.33 ? 129 ILE   A CG1 1 
ATOM   882  C CG2 . ILE   A 1 150 ? 16.705  2.802   21.716  1.00 20.80 ? 129 ILE   A CG2 1 
ATOM   883  C CD1 . ILE   A 1 150 ? 15.400  1.181   24.185  1.00 24.68 ? 129 ILE   A CD1 1 
ATOM   884  N N   . ALA   A 1 151 ? 16.077  1.052   18.492  1.00 16.33 ? 130 ALA   A N   1 
ATOM   885  C CA  . ALA   A 1 151 ? 16.826  1.182   17.247  1.00 19.80 ? 130 ALA   A CA  1 
ATOM   886  C C   . ALA   A 1 151 ? 15.941  1.799   16.144  1.00 19.21 ? 130 ALA   A C   1 
ATOM   887  O O   . ALA   A 1 151 ? 16.329  2.804   15.523  1.00 18.17 ? 130 ALA   A O   1 
ATOM   888  C CB  . ALA   A 1 151 ? 17.495  -0.149  16.845  1.00 17.81 ? 130 ALA   A CB  1 
ATOM   889  N N   . PRO   A 1 152 ? 14.679  1.338   15.909  1.00 18.66 ? 131 PRO   A N   1 
ATOM   890  C CA  . PRO   A 1 152 ? 13.805  2.077   15.008  1.00 17.89 ? 131 PRO   A CA  1 
ATOM   891  C C   . PRO   A 1 152 ? 13.673  3.582   15.267  1.00 19.31 ? 131 PRO   A C   1 
ATOM   892  O O   . PRO   A 1 152 ? 13.711  4.371   14.325  1.00 21.86 ? 131 PRO   A O   1 
ATOM   893  C CB  . PRO   A 1 152 ? 12.458  1.280   15.144  1.00 19.11 ? 131 PRO   A CB  1 
ATOM   894  C CG  . PRO   A 1 152 ? 12.960  -0.137  15.303  1.00 19.46 ? 131 PRO   A CG  1 
ATOM   895  C CD  . PRO   A 1 152 ? 14.083  0.050   16.358  1.00 18.57 ? 131 PRO   A CD  1 
ATOM   896  N N   . PHE   A 1 153 ? 13.570  3.982   16.542  1.00 18.07 ? 132 PHE   A N   1 
ATOM   897  C CA  . PHE   A 1 153 ? 13.483  5.400   16.870  1.00 19.29 ? 132 PHE   A CA  1 
ATOM   898  C C   . PHE   A 1 153 ? 14.788  6.128   16.495  1.00 19.89 ? 132 PHE   A C   1 
ATOM   899  O O   . PHE   A 1 153 ? 14.768  7.233   15.942  1.00 20.31 ? 132 PHE   A O   1 
ATOM   900  C CB  . PHE   A 1 153 ? 13.232  5.475   18.379  1.00 18.82 ? 132 PHE   A CB  1 
ATOM   901  C CG  . PHE   A 1 153 ? 13.516  6.862   18.957  1.00 21.80 ? 132 PHE   A CG  1 
ATOM   902  C CD1 . PHE   A 1 153 ? 12.593  7.894   18.825  1.00 23.58 ? 132 PHE   A CD1 1 
ATOM   903  C CD2 . PHE   A 1 153 ? 14.725  7.133   19.593  1.00 21.87 ? 132 PHE   A CD2 1 
ATOM   904  C CE1 . PHE   A 1 153 ? 12.878  9.171   19.294  1.00 24.69 ? 132 PHE   A CE1 1 
ATOM   905  C CE2 . PHE   A 1 153 ? 14.984  8.390   20.110  1.00 24.44 ? 132 PHE   A CE2 1 
ATOM   906  C CZ  . PHE   A 1 153 ? 14.066  9.416   19.945  1.00 24.69 ? 132 PHE   A CZ  1 
ATOM   907  N N   . LEU   A 1 154 ? 15.932  5.567   16.886  1.00 21.34 ? 133 LEU   A N   1 
ATOM   908  C CA  . LEU   A 1 154 ? 17.222  6.211   16.597  1.00 22.28 ? 133 LEU   A CA  1 
ATOM   909  C C   . LEU   A 1 154 ? 17.488  6.254   15.083  1.00 21.40 ? 133 LEU   A C   1 
ATOM   910  O O   . LEU   A 1 154 ? 17.932  7.268   14.551  1.00 21.91 ? 133 LEU   A O   1 
ATOM   911  C CB  . LEU   A 1 154 ? 18.323  5.502   17.377  1.00 23.03 ? 133 LEU   A CB  1 
ATOM   912  C CG  . LEU   A 1 154 ? 18.269  5.679   18.900  1.00 21.58 ? 133 LEU   A CG  1 
ATOM   913  C CD1 . LEU   A 1 154 ? 19.214  4.671   19.542  1.00 20.60 ? 133 LEU   A CD1 1 
ATOM   914  C CD2 . LEU   A 1 154 ? 18.590  7.126   19.333  1.00 20.05 ? 133 LEU   A CD2 1 
ATOM   915  N N   . LEU   A 1 155 ? 17.175  5.170   14.360  1.00 20.38 ? 134 LEU   A N   1 
ATOM   916  C CA  . LEU   A 1 155 ? 17.267  5.196   12.900  1.00 24.02 ? 134 LEU   A CA  1 
ATOM   917  C C   . LEU   A 1 155 ? 16.358  6.261   12.273  1.00 23.30 ? 134 LEU   A C   1 
ATOM   918  O O   . LEU   A 1 155 ? 16.739  6.924   11.285  1.00 23.03 ? 134 LEU   A O   1 
ATOM   919  C CB  . LEU   A 1 155 ? 17.002  3.821   12.298  1.00 20.58 ? 134 LEU   A CB  1 
ATOM   920  C CG  . LEU   A 1 155 ? 18.081  2.771   12.538  1.00 21.40 ? 134 LEU   A CG  1 
ATOM   921  C CD1 . LEU   A 1 155 ? 17.474  1.369   12.459  1.00 15.99 ? 134 LEU   A CD1 1 
ATOM   922  C CD2 . LEU   A 1 155 ? 19.274  2.946   11.537  1.00 21.33 ? 134 LEU   A CD2 1 
ATOM   923  N N   . THR   A 1 156 ? 15.151  6.423   12.842  1.00 20.20 ? 135 THR   A N   1 
ATOM   924  C CA  . THR   A 1 156 ? 14.198  7.422   12.359  1.00 19.03 ? 135 THR   A CA  1 
ATOM   925  C C   . THR   A 1 156 ? 14.798  8.817   12.563  1.00 21.53 ? 135 THR   A C   1 
ATOM   926  O O   . THR   A 1 156 ? 14.689  9.685   11.694  1.00 20.54 ? 135 THR   A O   1 
ATOM   927  C CB  . THR   A 1 156 ? 12.869  7.254   13.115  1.00 20.21 ? 135 THR   A CB  1 
ATOM   928  O OG1 . THR   A 1 156 ? 12.292  6.001   12.738  1.00 19.34 ? 135 THR   A OG1 1 
ATOM   929  C CG2 . THR   A 1 156 ? 11.856  8.320   12.748  1.00 20.51 ? 135 THR   A CG2 1 
ATOM   930  N N   . MET   A 1 157 ? 15.423  9.032   13.733  1.00 21.22 ? 136 MET   A N   1 
ATOM   931  C CA  . MET   A 1 157 ? 16.024  10.321  14.060  1.00 23.75 ? 136 MET   A CA  1 
ATOM   932  C C   . MET   A 1 157 ? 17.133  10.641  13.052  1.00 23.80 ? 136 MET   A C   1 
ATOM   933  O O   . MET   A 1 157 ? 17.160  11.741  12.496  1.00 21.94 ? 136 MET   A O   1 
ATOM   934  C CB  . MET   A 1 157 ? 16.731  10.314  15.427  1.00 24.60 ? 136 MET   A CB  1 
ATOM   935  C CG  . MET   A 1 157 ? 15.859  10.429  16.645  1.00 32.71 ? 136 MET   A CG  1 
ATOM   936  S SD  . MET   A 1 157 ? 16.888  10.855  18.077  1.00 38.94 ? 136 MET   A SD  1 
ATOM   937  C CE  . MET   A 1 157 ? 17.595  12.448  17.683  1.00 29.22 ? 136 MET   A CE  1 
ATOM   938  N N   . SER   A 1 158 ? 18.034  9.672   12.827  1.00 22.96 ? 137 SER   A N   1 
ATOM   939  C CA  . SER   A 1 158 ? 19.147  9.893   11.916  1.00 25.68 ? 137 SER   A CA  1 
ATOM   940  C C   . SER   A 1 158 ? 18.648  10.085  10.479  1.00 26.59 ? 137 SER   A C   1 
ATOM   941  O O   . SER   A 1 158 ? 19.179  10.921  9.750   1.00 23.61 ? 137 SER   A O   1 
ATOM   942  C CB  . SER   A 1 158 ? 20.175  8.789   12.011  1.00 25.41 ? 137 SER   A CB  1 
ATOM   943  O OG  . SER   A 1 158 ? 20.754  8.708   13.311  1.00 28.70 ? 137 SER   A OG  1 
ATOM   944  N N   . PHE   A 1 159 ? 17.642  9.301   10.062  1.00 26.96 ? 138 PHE   A N   1 
ATOM   945  C CA  . PHE   A 1 159 ? 17.067  9.413   8.725   1.00 23.20 ? 138 PHE   A CA  1 
ATOM   946  C C   . PHE   A 1 159 ? 16.523  10.826  8.513   1.00 25.00 ? 138 PHE   A C   1 
ATOM   947  O O   . PHE   A 1 159 ? 16.831  11.457  7.508   1.00 26.66 ? 138 PHE   A O   1 
ATOM   948  C CB  . PHE   A 1 159 ? 15.967  8.360   8.556   1.00 24.50 ? 138 PHE   A CB  1 
ATOM   949  C CG  . PHE   A 1 159 ? 15.229  8.460   7.227   1.00 24.48 ? 138 PHE   A CG  1 
ATOM   950  C CD1 . PHE   A 1 159 ? 14.130  9.306   7.081   1.00 27.00 ? 138 PHE   A CD1 1 
ATOM   951  C CD2 . PHE   A 1 159 ? 15.618  7.680   6.146   1.00 21.48 ? 138 PHE   A CD2 1 
ATOM   952  C CE1 . PHE   A 1 159 ? 13.441  9.386   5.861   1.00 26.12 ? 138 PHE   A CE1 1 
ATOM   953  C CE2 . PHE   A 1 159 ? 14.908  7.735   4.943   1.00 25.08 ? 138 PHE   A CE2 1 
ATOM   954  C CZ  . PHE   A 1 159 ? 13.824  8.598   4.802   1.00 23.69 ? 138 PHE   A CZ  1 
ATOM   955  N N   . ALA   A 1 160 ? 15.739  11.321  9.473   1.00 23.57 ? 139 ALA   A N   1 
ATOM   956  C CA  . ALA   A 1 160 ? 15.150  12.648  9.414   1.00 26.16 ? 139 ALA   A CA  1 
ATOM   957  C C   . ALA   A 1 160 ? 16.230  13.736  9.434   1.00 28.66 ? 139 ALA   A C   1 
ATOM   958  O O   . ALA   A 1 160 ? 16.152  14.669  8.641   1.00 32.56 ? 139 ALA   A O   1 
ATOM   959  C CB  . ALA   A 1 160 ? 14.157  12.859  10.542  1.00 25.97 ? 139 ALA   A CB  1 
ATOM   960  N N   . GLN   A 1 161 ? 17.221  13.628  10.331  1.00 28.48 ? 140 GLN   A N   1 
ATOM   961  C CA  . GLN   A 1 161 ? 18.217  14.691  10.498  1.00 32.92 ? 140 GLN   A CA  1 
ATOM   962  C C   . GLN   A 1 161 ? 19.031  14.854  9.210   1.00 33.98 ? 140 GLN   A C   1 
ATOM   963  O O   . GLN   A 1 161 ? 19.420  15.961  8.851   1.00 32.43 ? 140 GLN   A O   1 
ATOM   964  C CB  . GLN   A 1 161 ? 19.254  14.438  11.602  1.00 35.52 ? 140 GLN   A CB  1 
ATOM   965  C CG  . GLN   A 1 161 ? 18.708  13.860  12.902  0.60 39.14 ? 140 GLN   A CG  1 
ATOM   966  C CD  . GLN   A 1 161 ? 18.420  14.870  13.991  0.60 42.43 ? 140 GLN   A CD  1 
ATOM   967  O OE1 . GLN   A 1 161 ? 18.202  14.494  15.151  0.60 34.34 ? 140 GLN   A OE1 1 
ATOM   968  N NE2 . GLN   A 1 161 ? 18.460  16.152  13.645  0.60 42.82 ? 140 GLN   A NE2 1 
ATOM   969  N N   . ARG   A 1 162 ? 19.310  13.747  8.519   1.00 31.87 ? 141 ARG   A N   1 
ATOM   970  C CA  . ARG   A 1 162 ? 20.039  13.800  7.252   1.00 37.53 ? 141 ARG   A CA  1 
ATOM   971  C C   . ARG   A 1 162 ? 19.245  14.437  6.099   1.00 47.40 ? 141 ARG   A C   1 
ATOM   972  O O   . ARG   A 1 162 ? 19.839  14.789  5.084   1.00 52.24 ? 141 ARG   A O   1 
ATOM   973  C CB  . ARG   A 1 162 ? 20.464  12.387  6.846   1.00 37.34 ? 141 ARG   A CB  1 
ATOM   974  C CG  . ARG   A 1 162 ? 21.668  11.858  7.604   1.00 41.28 ? 141 ARG   A CG  1 
ATOM   975  C CD  . ARG   A 1 162 ? 22.879  12.639  7.089   0.80 47.81 ? 141 ARG   A CD  1 
ATOM   976  N NE  . ARG   A 1 162 ? 24.071  11.789  7.102   0.80 49.15 ? 141 ARG   A NE  1 
ATOM   977  C CZ  . ARG   A 1 162 ? 25.007  11.720  6.166   0.80 44.44 ? 141 ARG   A CZ  1 
ATOM   978  N NH1 . ARG   A 1 162 ? 25.016  12.551  5.138   0.80 40.05 ? 141 ARG   A NH1 1 
ATOM   979  N NH2 . ARG   A 1 162 ? 25.959  10.823  6.292   0.80 45.39 ? 141 ARG   A NH2 1 
ATOM   980  N N   . GLN   A 1 163 ? 17.915  14.584  6.212   1.00 48.84 ? 142 GLN   A N   1 
ATOM   981  C CA  . GLN   A 1 163 ? 17.154  15.204  5.131   1.00 51.55 ? 142 GLN   A CA  1 
ATOM   982  C C   . GLN   A 1 163 ? 17.097  16.727  5.365   1.00 64.74 ? 142 GLN   A C   1 
ATOM   983  O O   . GLN   A 1 163 ? 16.551  17.136  6.429   1.00 66.82 ? 142 GLN   A O   1 
ATOM   984  C CB  . GLN   A 1 163 ? 15.733  14.673  4.901   1.00 45.90 ? 142 GLN   A CB  1 
ATOM   985  C CG  . GLN   A 1 163 ? 15.553  13.173  5.106   1.00 38.53 ? 142 GLN   A CG  1 
ATOM   986  C CD  . GLN   A 1 163 ? 16.221  12.309  4.065   1.00 40.71 ? 142 GLN   A CD  1 
ATOM   987  O OE1 . GLN   A 1 163 ? 16.516  12.756  2.951   1.00 38.65 ? 142 GLN   A OE1 1 
ATOM   988  N NE2 . GLN   A 1 163 ? 16.450  11.052  4.421   1.00 43.50 ? 142 GLN   A NE2 1 
ATOM   989  N N   . SER   A 1 173 ? 10.786  13.917  -4.652  1.00 55.99 ? 152 SER   A N   1 
ATOM   990  C CA  . SER   A 1 173 ? 11.186  12.981  -3.567  1.00 46.33 ? 152 SER   A CA  1 
ATOM   991  C C   . SER   A 1 173 ? 9.953   12.288  -2.994  1.00 48.94 ? 152 SER   A C   1 
ATOM   992  O O   . SER   A 1 173 ? 8.885   12.883  -2.853  1.00 51.33 ? 152 SER   A O   1 
ATOM   993  C CB  . SER   A 1 173 ? 11.949  13.673  -2.477  1.00 46.68 ? 152 SER   A CB  1 
ATOM   994  N N   . ASN   A 1 174 ? 10.117  11.008  -2.667  1.00 41.52 ? 153 ASN   A N   1 
ATOM   995  C CA  . ASN   A 1 174 ? 9.064   10.263  -2.003  1.00 38.75 ? 153 ASN   A CA  1 
ATOM   996  C C   . ASN   A 1 174 ? 9.691   9.569   -0.791  1.00 31.38 ? 153 ASN   A C   1 
ATOM   997  O O   . ASN   A 1 174 ? 10.041  8.384   -0.855  1.00 32.95 ? 153 ASN   A O   1 
ATOM   998  C CB  . ASN   A 1 174 ? 8.341   9.396   -3.032  1.00 37.16 ? 153 ASN   A CB  1 
ATOM   999  C CG  . ASN   A 1 174 ? 7.306   8.498   -2.401  1.00 42.36 ? 153 ASN   A CG  1 
ATOM   1000 O OD1 . ASN   A 1 174 ? 6.854   8.761   -1.282  1.00 34.72 ? 153 ASN   A OD1 1 
ATOM   1001 N ND2 . ASN   A 1 174 ? 6.927   7.442   -3.108  1.00 44.18 ? 153 ASN   A ND2 1 
ATOM   1002 N N   . LEU   A 1 175 ? 9.862   10.337  0.298   1.00 27.93 ? 154 LEU   A N   1 
ATOM   1003 C CA  . LEU   A 1 175 ? 10.562  9.857   1.489   1.00 25.39 ? 154 LEU   A CA  1 
ATOM   1004 C C   . LEU   A 1 175 ? 9.570   9.106   2.374   1.00 22.90 ? 154 LEU   A C   1 
ATOM   1005 O O   . LEU   A 1 175 ? 8.527   9.649   2.707   1.00 23.48 ? 154 LEU   A O   1 
ATOM   1006 C CB  . LEU   A 1 175 ? 11.116  11.042  2.275   1.00 25.31 ? 154 LEU   A CB  1 
ATOM   1007 C CG  . LEU   A 1 175 ? 12.131  11.929  1.544   1.00 27.90 ? 154 LEU   A CG  1 
ATOM   1008 C CD1 . LEU   A 1 175 ? 12.534  13.111  2.438   1.00 29.34 ? 154 LEU   A CD1 1 
ATOM   1009 C CD2 . LEU   A 1 175 ? 13.344  11.107  1.142   1.00 26.29 ? 154 LEU   A CD2 1 
ATOM   1010 N N   . SER   A 1 176 ? 9.904   7.873   2.793   1.00 24.13 ? 155 SER   A N   1 
ATOM   1011 C CA  . SER   A 1 176 ? 9.033   7.277   3.804   1.00 24.11 ? 155 SER   A CA  1 
ATOM   1012 C C   . SER   A 1 176 ? 9.777   6.239   4.651   1.00 23.89 ? 155 SER   A C   1 
ATOM   1013 O O   . SER   A 1 176 ? 10.902  5.814   4.328   1.00 20.22 ? 155 SER   A O   1 
ATOM   1014 C CB  . SER   A 1 176 ? 7.774   6.715   3.170   1.00 27.01 ? 155 SER   A CB  1 
ATOM   1015 O OG  . SER   A 1 176 ? 8.076   5.456   2.582   1.00 27.38 ? 155 SER   A OG  1 
ATOM   1016 N N   . ILE   A 1 177 ? 9.129   5.860   5.761   1.00 21.76 ? 156 ILE   A N   1 
ATOM   1017 C CA  . ILE   A 1 177 ? 9.672   4.873   6.671   1.00 19.98 ? 156 ILE   A CA  1 
ATOM   1018 C C   . ILE   A 1 177 ? 8.603   3.799   6.816   1.00 19.42 ? 156 ILE   A C   1 
ATOM   1019 O O   . ILE   A 1 177 ? 7.426   4.118   6.917   1.00 20.65 ? 156 ILE   A O   1 
ATOM   1020 C CB  . ILE   A 1 177 ? 10.011  5.533   8.027   1.00 21.97 ? 156 ILE   A CB  1 
ATOM   1021 C CG1 . ILE   A 1 177 ? 11.109  6.628   7.896   1.00 22.04 ? 156 ILE   A CG1 1 
ATOM   1022 C CG2 . ILE   A 1 177 ? 10.397  4.462   9.062   1.00 23.02 ? 156 ILE   A CG2 1 
ATOM   1023 C CD1 . ILE   A 1 177 ? 11.319  7.423   9.175   1.00 22.88 ? 156 ILE   A CD1 1 
ATOM   1024 N N   . VAL   A 1 178 ? 9.002   2.525   6.787   1.00 20.46 ? 157 VAL   A N   1 
ATOM   1025 C CA  . VAL   A 1 178 ? 8.023   1.489   7.064   1.00 19.52 ? 157 VAL   A CA  1 
ATOM   1026 C C   . VAL   A 1 178 ? 8.541   0.651   8.234   1.00 18.60 ? 157 VAL   A C   1 
ATOM   1027 O O   . VAL   A 1 178 ? 9.645   0.094   8.164   1.00 20.34 ? 157 VAL   A O   1 
ATOM   1028 C CB  . VAL   A 1 178 ? 7.779   0.594   5.826   1.00 21.08 ? 157 VAL   A CB  1 
ATOM   1029 C CG1 . VAL   A 1 178 ? 6.755   -0.516  6.113   1.00 22.72 ? 157 VAL   A CG1 1 
ATOM   1030 C CG2 . VAL   A 1 178 ? 7.316   1.405   4.618   1.00 19.79 ? 157 VAL   A CG2 1 
ATOM   1031 N N   . ASN   A 1 179 ? 7.690   0.486   9.256   1.00 20.36 ? 158 ASN   A N   1 
ATOM   1032 C CA  . ASN   A 1 179 ? 8.048   -0.290  10.435  1.00 19.39 ? 158 ASN   A CA  1 
ATOM   1033 C C   . ASN   A 1 179 ? 7.388   -1.662  10.369  1.00 19.00 ? 158 ASN   A C   1 
ATOM   1034 O O   . ASN   A 1 179 ? 6.178   -1.756  10.188  1.00 18.62 ? 158 ASN   A O   1 
ATOM   1035 C CB  . ASN   A 1 179 ? 7.632   0.470   11.691  1.00 19.42 ? 158 ASN   A CB  1 
ATOM   1036 C CG  . ASN   A 1 179 ? 8.474   1.709   11.849  1.00 19.29 ? 158 ASN   A CG  1 
ATOM   1037 O OD1 . ASN   A 1 179 ? 9.652   1.649   11.481  1.00 20.73 ? 158 ASN   A OD1 1 
ATOM   1038 N ND2 . ASN   A 1 179 ? 7.928   2.793   12.393  1.00 19.56 ? 158 ASN   A ND2 1 
ATOM   1039 N N   . LEU   A 1 180 ? 8.144   -2.731  10.616  1.00 18.83 ? 159 LEU   A N   1 
ATOM   1040 C CA  . LEU   A 1 180 ? 7.522   -4.054  10.635  1.00 18.43 ? 159 LEU   A CA  1 
ATOM   1041 C C   . LEU   A 1 180 ? 6.958   -4.339  12.032  1.00 20.44 ? 159 LEU   A C   1 
ATOM   1042 O O   . LEU   A 1 180 ? 7.713   -4.494  12.998  1.00 21.65 ? 159 LEU   A O   1 
ATOM   1043 C CB  . LEU   A 1 180 ? 8.533   -5.132  10.205  1.00 19.30 ? 159 LEU   A CB  1 
ATOM   1044 C CG  . LEU   A 1 180 ? 8.645   -5.422  8.698   1.00 19.94 ? 159 LEU   A CG  1 
ATOM   1045 C CD1 . LEU   A 1 180 ? 7.404   -6.198  8.250   1.00 17.39 ? 159 LEU   A CD1 1 
ATOM   1046 C CD2 . LEU   A 1 180 ? 8.827   -4.100  7.932   1.00 18.15 ? 159 LEU   A CD2 1 
ATOM   1047 N N   . CYS   A 1 181 ? 5.624   -4.373  12.138  1.00 20.09 ? 160 CYS   A N   1 
ATOM   1048 C CA  . CYS   A 1 181 ? 4.888   -4.419  13.399  1.00 20.86 ? 160 CYS   A CA  1 
ATOM   1049 C C   . CYS   A 1 181 ? 4.436   -5.869  13.569  1.00 21.99 ? 160 CYS   A C   1 
ATOM   1050 O O   . CYS   A 1 181 ? 5.142   -6.759  13.116  1.00 24.02 ? 160 CYS   A O   1 
ATOM   1051 C CB  . CYS   A 1 181 ? 3.733   -3.414  13.408  1.00 19.51 ? 160 CYS   A CB  1 
ATOM   1052 S SG  . CYS   A 1 181 ? 4.310   -1.682  13.302  1.00 24.79 ? 160 CYS   A SG  1 
ATOM   1053 N N   . ASP   A 1 182 ? 3.336   -6.111  14.283  1.00 20.35 ? 161 ASP   A N   1 
ATOM   1054 C CA  . ASP   A 1 182 ? 2.931   -7.482  14.578  1.00 20.94 ? 161 ASP   A CA  1 
ATOM   1055 C C   . ASP   A 1 182 ? 1.415   -7.448  14.784  1.00 21.95 ? 161 ASP   A C   1 
ATOM   1056 O O   . ASP   A 1 182 ? 0.925   -6.679  15.608  1.00 22.38 ? 161 ASP   A O   1 
ATOM   1057 C CB  . ASP   A 1 182 ? 3.692   -8.033  15.786  1.00 23.82 ? 161 ASP   A CB  1 
ATOM   1058 C CG  . ASP   A 1 182 ? 3.395   -9.497  16.094  1.00 27.81 ? 161 ASP   A CG  1 
ATOM   1059 O OD1 . ASP   A 1 182 ? 2.263   -9.885  15.850  1.00 23.75 ? 161 ASP   A OD1 1 
ATOM   1060 O OD2 . ASP   A 1 182 ? 4.315   -10.265 16.501  1.00 33.18 ? 161 ASP   A OD2 1 
ATOM   1061 N N   . ALA   A 1 183 ? 0.668   -8.206  13.970  1.00 20.54 ? 162 ALA   A N   1 
ATOM   1062 C CA  . ALA   A 1 183 ? -0.791  -8.108  13.969  1.00 21.49 ? 162 ALA   A CA  1 
ATOM   1063 C C   . ALA   A 1 183 ? -1.414  -8.663  15.251  1.00 23.45 ? 162 ALA   A C   1 
ATOM   1064 O O   . ALA   A 1 183 ? -2.605  -8.440  15.515  1.00 21.86 ? 162 ALA   A O   1 
ATOM   1065 C CB  . ALA   A 1 183 ? -1.361  -8.820  12.742  1.00 20.34 ? 162 ALA   A CB  1 
ATOM   1066 N N   . MET   A 1 184 ? -0.621  -9.444  15.986  1.00 21.17 ? 163 MET   A N   1 
ATOM   1067 C CA  . MET   A 1 184 ? -1.098  -10.208 17.121  1.00 23.75 ? 163 MET   A CA  1 
ATOM   1068 C C   . MET   A 1 184 ? -0.674  -9.547  18.442  1.00 23.49 ? 163 MET   A C   1 
ATOM   1069 O O   . MET   A 1 184 ? -0.782  -10.165 19.510  1.00 25.72 ? 163 MET   A O   1 
ATOM   1070 C CB  . MET   A 1 184 ? -0.631  -11.675 16.976  1.00 24.17 ? 163 MET   A CB  1 
ATOM   1071 C CG  . MET   A 1 184 ? -1.155  -12.330 15.668  1.00 24.86 ? 163 MET   A CG  1 
ATOM   1072 S SD  . MET   A 1 184 ? -2.942  -12.553 15.846  1.00 30.59 ? 163 MET   A SD  1 
ATOM   1073 C CE  . MET   A 1 184 ? -3.006  -13.937 16.990  1.00 35.50 ? 163 MET   A CE  1 
ATOM   1074 N N   . VAL   A 1 185 ? -0.376  -8.248  18.414  1.00 22.67 ? 164 VAL   A N   1 
ATOM   1075 C CA  . VAL   A 1 185 ? 0.142   -7.624  19.628  1.00 26.96 ? 164 VAL   A CA  1 
ATOM   1076 C C   . VAL   A 1 185 ? -0.915  -7.527  20.724  1.00 27.77 ? 164 VAL   A C   1 
ATOM   1077 O O   . VAL   A 1 185 ? -0.518  -7.365  21.873  1.00 27.61 ? 164 VAL   A O   1 
ATOM   1078 C CB  . VAL   A 1 185 ? 0.800   -6.242  19.474  1.00 29.06 ? 164 VAL   A CB  1 
ATOM   1079 C CG1 . VAL   A 1 185 ? 2.167   -6.388  18.824  1.00 34.72 ? 164 VAL   A CG1 1 
ATOM   1080 C CG2 . VAL   A 1 185 ? -0.108  -5.285  18.727  1.00 27.55 ? 164 VAL   A CG2 1 
ATOM   1081 N N   . ASP   A 1 186 ? -2.212  -7.520  20.361  1.00 24.43 ? 165 ASP   A N   1 
ATOM   1082 C CA  . ASP   A 1 186 ? -3.272  -7.404  21.353  1.00 24.46 ? 165 ASP   A CA  1 
ATOM   1083 C C   . ASP   A 1 186 ? -3.807  -8.778  21.755  1.00 24.29 ? 165 ASP   A C   1 
ATOM   1084 O O   . ASP   A 1 186 ? -4.678  -8.885  22.627  1.00 23.22 ? 165 ASP   A O   1 
ATOM   1085 C CB  . ASP   A 1 186 ? -4.374  -6.468  20.896  1.00 23.09 ? 165 ASP   A CB  1 
ATOM   1086 C CG  . ASP   A 1 186 ? -3.889  -5.042  20.753  1.00 25.81 ? 165 ASP   A CG  1 
ATOM   1087 O OD1 . ASP   A 1 186 ? -3.111  -4.583  21.610  1.00 27.49 ? 165 ASP   A OD1 1 
ATOM   1088 O OD2 . ASP   A 1 186 ? -4.290  -4.411  19.786  1.00 28.93 ? 165 ASP   A OD2 1 
ATOM   1089 N N   . GLN   A 1 187 ? -3.236  -9.824  21.177  1.00 22.45 ? 166 GLN   A N   1 
ATOM   1090 C CA  . GLN   A 1 187 ? -3.552  -11.189 21.611  1.00 22.40 ? 166 GLN   A CA  1 
ATOM   1091 C C   . GLN   A 1 187 ? -2.230  -11.941 21.681  1.00 22.61 ? 166 GLN   A C   1 
ATOM   1092 O O   . GLN   A 1 187 ? -1.975  -12.843 20.874  1.00 24.34 ? 166 GLN   A O   1 
ATOM   1093 C CB  . GLN   A 1 187 ? -4.454  -11.862 20.574  1.00 27.78 ? 166 GLN   A CB  1 
ATOM   1094 C CG  . GLN   A 1 187 ? -5.806  -11.179 20.396  1.00 33.95 ? 166 GLN   A CG  1 
ATOM   1095 C CD  . GLN   A 1 187 ? -6.139  -10.925 18.938  1.00 38.05 ? 166 GLN   A CD  1 
ATOM   1096 O OE1 . GLN   A 1 187 ? -5.886  -9.841  18.409  1.00 37.53 ? 166 GLN   A OE1 1 
ATOM   1097 N NE2 . GLN   A 1 187 ? -6.670  -11.932 18.268  1.00 36.20 ? 166 GLN   A NE2 1 
ATOM   1098 N N   . PRO   A 1 188 ? -1.334  -11.562 22.630  1.00 23.72 ? 167 PRO   A N   1 
ATOM   1099 C CA  . PRO   A 1 188 ? 0.063   -12.012 22.584  1.00 26.94 ? 167 PRO   A CA  1 
ATOM   1100 C C   . PRO   A 1 188 ? 0.299   -13.465 22.956  1.00 29.49 ? 167 PRO   A C   1 
ATOM   1101 O O   . PRO   A 1 188 ? -0.534  -14.077 23.644  1.00 27.23 ? 167 PRO   A O   1 
ATOM   1102 C CB  . PRO   A 1 188 ? 0.751   -11.053 23.567  1.00 28.46 ? 167 PRO   A CB  1 
ATOM   1103 C CG  . PRO   A 1 188 ? -0.337  -10.701 24.581  1.00 26.58 ? 167 PRO   A CG  1 
ATOM   1104 C CD  . PRO   A 1 188 ? -1.625  -10.654 23.759  1.00 22.69 ? 167 PRO   A CD  1 
HETATM 1105 N N   . CSX   A 1 189 ? 1.435   -13.991 22.481  1.00 27.57 ? 168 CSX   A N   1 
HETATM 1106 C CA  . CSX   A 1 189 ? 1.931   -15.266 22.965  1.00 31.60 ? 168 CSX   A CA  1 
HETATM 1107 C CB  . CSX   A 1 189 ? 3.148   -15.750 22.165  1.00 38.89 ? 168 CSX   A CB  1 
HETATM 1108 S SG  . CSX   A 1 189 ? 2.714   -16.242 20.474  1.00 49.60 ? 168 CSX   A SG  1 
HETATM 1109 C C   . CSX   A 1 189 ? 2.292   -15.122 24.445  1.00 29.17 ? 168 CSX   A C   1 
HETATM 1110 O O   . CSX   A 1 189 ? 2.875   -14.125 24.875  1.00 26.12 ? 168 CSX   A O   1 
HETATM 1111 O OD  . CSX   A 1 189 ? 2.441   -17.718 20.559  1.00 51.22 ? 168 CSX   A OD  1 
ATOM   1112 N N   . MET   A 1 190 ? 1.894   -16.134 25.207  1.00 29.12 ? 169 MET   A N   1 
ATOM   1113 C CA  . MET   A 1 190 ? 2.162   -16.287 26.625  1.00 30.47 ? 169 MET   A CA  1 
ATOM   1114 C C   . MET   A 1 190 ? 3.672   -16.233 26.830  1.00 27.52 ? 169 MET   A C   1 
ATOM   1115 O O   . MET   A 1 190 ? 4.379   -16.895 26.088  1.00 25.11 ? 169 MET   A O   1 
ATOM   1116 C CB  . MET   A 1 190 ? 1.701   -17.709 26.998  1.00 36.20 ? 169 MET   A CB  1 
ATOM   1117 C CG  . MET   A 1 190 ? 2.104   -18.198 28.348  1.00 42.12 ? 169 MET   A CG  1 
ATOM   1118 S SD  . MET   A 1 190 ? 1.163   -17.073 29.388  1.00 48.77 ? 169 MET   A SD  1 
ATOM   1119 C CE  . MET   A 1 190 ? -0.435  -17.882 29.574  1.00 38.82 ? 169 MET   A CE  1 
ATOM   1120 N N   . ALA   A 1 191 ? 4.137   -15.421 27.804  1.00 26.11 ? 170 ALA   A N   1 
ATOM   1121 C CA  . ALA   A 1 191 ? 5.525   -15.291 28.231  1.00 26.26 ? 170 ALA   A CA  1 
ATOM   1122 C C   . ALA   A 1 191 ? 6.375   -14.490 27.242  1.00 24.08 ? 170 ALA   A C   1 
ATOM   1123 O O   . ALA   A 1 191 ? 7.591   -14.595 27.272  1.00 25.93 ? 170 ALA   A O   1 
ATOM   1124 C CB  . ALA   A 1 191 ? 6.163   -16.652 28.599  1.00 27.45 ? 170 ALA   A CB  1 
ATOM   1125 N N   . PHE   A 1 192 ? 5.753   -13.673 26.371  1.00 23.11 ? 171 PHE   A N   1 
ATOM   1126 C CA  . PHE   A 1 192 ? 6.522   -12.819 25.467  1.00 22.66 ? 171 PHE   A CA  1 
ATOM   1127 C C   . PHE   A 1 192 ? 6.338   -11.328 25.778  1.00 22.32 ? 171 PHE   A C   1 
ATOM   1128 O O   . PHE   A 1 192 ? 6.247   -10.526 24.852  1.00 23.18 ? 171 PHE   A O   1 
ATOM   1129 C CB  . PHE   A 1 192 ? 6.207   -13.124 23.995  1.00 23.68 ? 171 PHE   A CB  1 
ATOM   1130 C CG  . PHE   A 1 192 ? 6.845   -14.401 23.447  1.00 24.07 ? 171 PHE   A CG  1 
ATOM   1131 C CD1 . PHE   A 1 192 ? 6.278   -15.639 23.707  1.00 25.84 ? 171 PHE   A CD1 1 
ATOM   1132 C CD2 . PHE   A 1 192 ? 8.011   -14.357 22.672  1.00 26.64 ? 171 PHE   A CD2 1 
ATOM   1133 C CE1 . PHE   A 1 192 ? 6.862   -16.816 23.214  1.00 26.32 ? 171 PHE   A CE1 1 
ATOM   1134 C CE2 . PHE   A 1 192 ? 8.584   -15.531 22.160  1.00 27.68 ? 171 PHE   A CE2 1 
ATOM   1135 C CZ  . PHE   A 1 192 ? 8.011   -16.756 22.446  1.00 27.87 ? 171 PHE   A CZ  1 
ATOM   1136 N N   . SER   A 1 193 ? 6.350   -10.927 27.066  1.00 21.70 ? 172 SER   A N   1 
ATOM   1137 C CA  A SER   A 1 193 ? 6.067   -9.545  27.461  0.70 20.64 ? 172 SER   A CA  1 
ATOM   1138 C CA  B SER   A 1 193 ? 6.038   -9.544  27.414  0.30 20.02 ? 172 SER   A CA  1 
ATOM   1139 C C   . SER   A 1 193 ? 7.017   -8.540  26.801  1.00 21.44 ? 172 SER   A C   1 
ATOM   1140 O O   . SER   A 1 193 ? 6.606   -7.471  26.365  1.00 20.69 ? 172 SER   A O   1 
ATOM   1141 C CB  A SER   A 1 193 ? 6.127   -9.412  28.974  0.70 24.75 ? 172 SER   A CB  1 
ATOM   1142 C CB  B SER   A 1 193 ? 5.925   -9.354  28.905  0.30 20.24 ? 172 SER   A CB  1 
ATOM   1143 O OG  A SER   A 1 193 ? 4.990   -10.018 29.582  0.70 28.25 ? 172 SER   A OG  1 
ATOM   1144 O OG  B SER   A 1 193 ? 7.082   -9.837  29.566  0.30 17.53 ? 172 SER   A OG  1 
ATOM   1145 N N   . LEU   A 1 194 ? 8.331   -8.808  26.851  1.00 20.93 ? 173 LEU   A N   1 
ATOM   1146 C CA  . LEU   A 1 194 ? 9.299   -7.817  26.375  1.00 20.44 ? 173 LEU   A CA  1 
ATOM   1147 C C   . LEU   A 1 194 ? 9.159   -7.646  24.867  1.00 18.51 ? 173 LEU   A C   1 
ATOM   1148 O O   . LEU   A 1 194 ? 9.163   -6.520  24.362  1.00 18.63 ? 173 LEU   A O   1 
ATOM   1149 C CB  . LEU   A 1 194 ? 10.775  -8.038  26.735  1.00 18.79 ? 173 LEU   A CB  1 
ATOM   1150 C CG  . LEU   A 1 194 ? 11.123  -7.782  28.205  1.00 20.28 ? 173 LEU   A CG  1 
ATOM   1151 C CD1 . LEU   A 1 194 ? 12.489  -8.364  28.599  1.00 20.47 ? 173 LEU   A CD1 1 
ATOM   1152 C CD2 . LEU   A 1 194 ? 11.069  -6.265  28.492  1.00 19.11 ? 173 LEU   A CD2 1 
ATOM   1153 N N   . TYR   A 1 195 ? 9.067   -8.757  24.149  1.00 19.30 ? 174 TYR   A N   1 
ATOM   1154 C CA  . TYR   A 1 195 ? 8.807   -8.646  22.714  1.00 19.20 ? 174 TYR   A CA  1 
ATOM   1155 C C   . TYR   A 1 195 ? 7.538   -7.823  22.424  1.00 19.71 ? 174 TYR   A C   1 
ATOM   1156 O O   . TYR   A 1 195 ? 7.578   -6.942  21.564  1.00 20.98 ? 174 TYR   A O   1 
ATOM   1157 C CB  . TYR   A 1 195 ? 8.669   -10.029 22.076  1.00 18.60 ? 174 TYR   A CB  1 
ATOM   1158 C CG  . TYR   A 1 195 ? 8.211   -9.928  20.631  1.00 19.04 ? 174 TYR   A CG  1 
ATOM   1159 C CD1 . TYR   A 1 195 ? 9.111   -9.603  19.611  1.00 18.54 ? 174 TYR   A CD1 1 
ATOM   1160 C CD2 . TYR   A 1 195 ? 6.880   -10.164 20.291  1.00 21.06 ? 174 TYR   A CD2 1 
ATOM   1161 C CE1 . TYR   A 1 195 ? 8.698   -9.529  18.285  1.00 20.94 ? 174 TYR   A CE1 1 
ATOM   1162 C CE2 . TYR   A 1 195 ? 6.460   -10.113 18.964  1.00 24.96 ? 174 TYR   A CE2 1 
ATOM   1163 C CZ  . TYR   A 1 195 ? 7.369   -9.783  17.962  1.00 23.14 ? 174 TYR   A CZ  1 
ATOM   1164 O OH  . TYR   A 1 195 ? 6.910   -9.751  16.672  1.00 23.32 ? 174 TYR   A OH  1 
ATOM   1165 N N   . ASN   A 1 196 ? 6.435   -8.098  23.140  1.00 18.26 ? 175 ASN   A N   1 
ATOM   1166 C CA  A ASN   A 1 196 ? 5.158   -7.413  22.967  0.50 19.13 ? 175 ASN   A CA  1 
ATOM   1167 C CA  B ASN   A 1 196 ? 5.179   -7.399  22.892  0.50 19.44 ? 175 ASN   A CA  1 
ATOM   1168 C C   . ASN   A 1 196 ? 5.311   -5.931  23.296  1.00 18.46 ? 175 ASN   A C   1 
ATOM   1169 O O   . ASN   A 1 196 ? 4.755   -5.059  22.620  1.00 20.20 ? 175 ASN   A O   1 
ATOM   1170 C CB  A ASN   A 1 196 ? 4.078   -8.015  23.865  0.50 18.56 ? 175 ASN   A CB  1 
ATOM   1171 C CB  B ASN   A 1 196 ? 3.960   -8.147  23.438  0.50 20.17 ? 175 ASN   A CB  1 
ATOM   1172 C CG  A ASN   A 1 196 ? 2.680   -7.602  23.460  0.50 21.49 ? 175 ASN   A CG  1 
ATOM   1173 C CG  B ASN   A 1 196 ? 3.642   -9.395  22.631  0.50 22.36 ? 175 ASN   A CG  1 
ATOM   1174 O OD1 A ASN   A 1 196 ? 1.929   -7.040  24.275  0.50 24.14 ? 175 ASN   A OD1 1 
ATOM   1175 O OD1 B ASN   A 1 196 ? 3.042   -9.340  21.545  0.50 24.63 ? 175 ASN   A OD1 1 
ATOM   1176 N ND2 A ASN   A 1 196 ? 2.282   -7.902  22.228  0.50 20.59 ? 175 ASN   A ND2 1 
ATOM   1177 N ND2 B ASN   A 1 196 ? 4.047   -10.546 23.137  0.50 21.10 ? 175 ASN   A ND2 1 
ATOM   1178 N N   . MET   A 1 197 ? 6.064   -5.639  24.364  1.00 17.80 ? 176 MET   A N   1 
ATOM   1179 C CA  . MET   A 1 197 ? 6.261   -4.236  24.723  1.00 18.04 ? 176 MET   A CA  1 
ATOM   1180 C C   . MET   A 1 197 ? 6.941   -3.507  23.568  1.00 18.81 ? 176 MET   A C   1 
ATOM   1181 O O   . MET   A 1 197 ? 6.697   -2.321  23.298  1.00 18.38 ? 176 MET   A O   1 
ATOM   1182 C CB  . MET   A 1 197 ? 7.129   -4.119  25.988  1.00 18.10 ? 176 MET   A CB  1 
ATOM   1183 C CG  . MET   A 1 197 ? 6.370   -4.676  27.213  1.00 18.56 ? 176 MET   A CG  1 
ATOM   1184 S SD  . MET   A 1 197 ? 7.356   -4.837  28.722  1.00 21.25 ? 176 MET   A SD  1 
ATOM   1185 C CE  . MET   A 1 197 ? 7.799   -3.102  28.920  1.00 19.36 ? 176 MET   A CE  1 
ATOM   1186 N N   . GLY   A 1 198 ? 7.945   -4.173  23.015  1.00 17.89 ? 177 GLY   A N   1 
ATOM   1187 C CA  . GLY   A 1 198 ? 8.724   -3.525  21.976  1.00 17.08 ? 177 GLY   A CA  1 
ATOM   1188 C C   . GLY   A 1 198 ? 7.876   -3.239  20.731  1.00 17.08 ? 177 GLY   A C   1 
ATOM   1189 O O   . GLY   A 1 198 ? 7.931   -2.145  20.182  1.00 17.17 ? 177 GLY   A O   1 
ATOM   1190 N N   . LYS   A 1 199 ? 7.068   -4.213  20.305  1.00 17.35 ? 178 LYS   A N   1 
ATOM   1191 C CA  . LYS   A 1 199 ? 6.177   -4.015  19.155  1.00 17.51 ? 178 LYS   A CA  1 
ATOM   1192 C C   . LYS   A 1 199 ? 5.097   -2.975  19.452  1.00 17.25 ? 178 LYS   A C   1 
ATOM   1193 O O   . LYS   A 1 199 ? 4.741   -2.179  18.592  1.00 18.12 ? 178 LYS   A O   1 
ATOM   1194 C CB  . LYS   A 1 199 ? 5.575   -5.347  18.689  1.00 18.23 ? 178 LYS   A CB  1 
ATOM   1195 C CG  . LYS   A 1 199 ? 6.639   -6.285  18.032  1.00 20.11 ? 178 LYS   A CG  1 
ATOM   1196 C CD  . LYS   A 1 199 ? 7.337   -5.625  16.832  1.00 20.74 ? 178 LYS   A CD  1 
ATOM   1197 C CE  . LYS   A 1 199 ? 8.104   -6.678  16.062  1.00 22.24 ? 178 LYS   A CE  1 
ATOM   1198 N NZ  . LYS   A 1 199 ? 8.990   -6.144  15.009  1.00 21.71 ? 178 LYS   A NZ  1 
ATOM   1199 N N   . HIS   A 1 200 ? 4.598   -2.906  20.692  1.00 15.87 ? 179 HIS   A N   1 
ATOM   1200 C CA  . HIS   A 1 200 ? 3.625   -1.862  20.956  1.00 16.51 ? 179 HIS   A CA  1 
ATOM   1201 C C   . HIS   A 1 200 ? 4.348   -0.523  20.918  1.00 18.28 ? 179 HIS   A C   1 
ATOM   1202 O O   . HIS   A 1 200 ? 3.803   0.441   20.418  1.00 19.11 ? 179 HIS   A O   1 
ATOM   1203 C CB  . HIS   A 1 200 ? 3.056   -2.000  22.370  1.00 17.91 ? 179 HIS   A CB  1 
ATOM   1204 C CG  . HIS   A 1 200 ? 1.790   -2.745  22.396  1.00 20.91 ? 179 HIS   A CG  1 
ATOM   1205 N ND1 . HIS   A 1 200 ? 0.560   -2.151  22.265  1.00 23.72 ? 179 HIS   A ND1 1 
ATOM   1206 C CD2 . HIS   A 1 200 ? 1.566   -4.065  22.537  1.00 20.96 ? 179 HIS   A CD2 1 
ATOM   1207 C CE1 . HIS   A 1 200 ? -0.376  -3.074  22.384  1.00 25.43 ? 179 HIS   A CE1 1 
ATOM   1208 N NE2 . HIS   A 1 200 ? 0.223   -4.245  22.532  1.00 23.27 ? 179 HIS   A NE2 1 
ATOM   1209 N N   . ALA   A 1 201 ? 5.571   -0.445  21.473  1.00 18.50 ? 180 ALA   A N   1 
ATOM   1210 C CA  . ALA   A 1 201 ? 6.323   0.816   21.381  1.00 17.48 ? 180 ALA   A CA  1 
ATOM   1211 C C   . ALA   A 1 201 ? 6.480   1.238   19.918  1.00 17.50 ? 180 ALA   A C   1 
ATOM   1212 O O   . ALA   A 1 201 ? 6.557   2.430   19.585  1.00 17.13 ? 180 ALA   A O   1 
ATOM   1213 C CB  . ALA   A 1 201 ? 7.710   0.678   22.043  1.00 16.92 ? 180 ALA   A CB  1 
ATOM   1214 N N   . LEU   A 1 202 ? 6.687   0.246   19.056  1.00 16.74 ? 181 LEU   A N   1 
ATOM   1215 C CA  . LEU   A 1 202 ? 6.900   0.503   17.636  1.00 19.68 ? 181 LEU   A CA  1 
ATOM   1216 C C   . LEU   A 1 202 ? 5.645   1.116   17.005  1.00 20.13 ? 181 LEU   A C   1 
ATOM   1217 O O   . LEU   A 1 202 ? 5.736   1.998   16.144  1.00 20.26 ? 181 LEU   A O   1 
ATOM   1218 C CB  . LEU   A 1 202 ? 7.324   -0.783  16.924  1.00 18.20 ? 181 LEU   A CB  1 
ATOM   1219 C CG  . LEU   A 1 202 ? 7.792   -0.626  15.465  1.00 19.13 ? 181 LEU   A CG  1 
ATOM   1220 C CD1 . LEU   A 1 202 ? 8.946   0.406   15.204  1.00 18.51 ? 181 LEU   A CD1 1 
ATOM   1221 C CD2 . LEU   A 1 202 ? 8.182   -2.006  14.996  1.00 17.68 ? 181 LEU   A CD2 1 
ATOM   1222 N N   . VAL   A 1 203 ? 4.461   0.638   17.433  1.00 19.26 ? 182 VAL   A N   1 
ATOM   1223 C CA  . VAL   A 1 203 ? 3.220   1.272   17.014  1.00 19.07 ? 182 VAL   A CA  1 
ATOM   1224 C C   . VAL   A 1 203 ? 3.235   2.742   17.434  1.00 18.05 ? 182 VAL   A C   1 
ATOM   1225 O O   . VAL   A 1 203 ? 2.847   3.590   16.648  1.00 20.87 ? 182 VAL   A O   1 
ATOM   1226 C CB  . VAL   A 1 203 ? 2.002   0.521   17.586  1.00 20.50 ? 182 VAL   A CB  1 
ATOM   1227 C CG1 . VAL   A 1 203 ? 0.697   1.262   17.312  1.00 20.89 ? 182 VAL   A CG1 1 
ATOM   1228 C CG2 . VAL   A 1 203 ? 1.962   -0.900  17.010  1.00 22.01 ? 182 VAL   A CG2 1 
ATOM   1229 N N   . GLY   A 1 204 ? 3.597   3.029   18.688  1.00 16.46 ? 183 GLY   A N   1 
ATOM   1230 C CA  . GLY   A 1 204 ? 3.648   4.402   19.183  1.00 19.17 ? 183 GLY   A CA  1 
ATOM   1231 C C   . GLY   A 1 204 ? 4.646   5.252   18.383  1.00 18.33 ? 183 GLY   A C   1 
ATOM   1232 O O   . GLY   A 1 204 ? 4.387   6.425   18.086  1.00 20.44 ? 183 GLY   A O   1 
ATOM   1233 N N   . LEU   A 1 205 ? 5.801   4.665   18.051  1.00 18.13 ? 184 LEU   A N   1 
ATOM   1234 C CA  . LEU   A 1 205 ? 6.776   5.371   17.218  1.00 19.50 ? 184 LEU   A CA  1 
ATOM   1235 C C   . LEU   A 1 205 ? 6.172   5.683   15.839  1.00 19.80 ? 184 LEU   A C   1 
ATOM   1236 O O   . LEU   A 1 205 ? 6.323   6.797   15.311  1.00 20.28 ? 184 LEU   A O   1 
ATOM   1237 C CB  . LEU   A 1 205 ? 8.065   4.546   17.047  1.00 19.25 ? 184 LEU   A CB  1 
ATOM   1238 C CG  . LEU   A 1 205 ? 9.096   5.138   16.071  1.00 19.61 ? 184 LEU   A CG  1 
ATOM   1239 C CD1 . LEU   A 1 205 ? 9.598   6.523   16.473  1.00 19.94 ? 184 LEU   A CD1 1 
ATOM   1240 C CD2 . LEU   A 1 205 ? 10.264  4.165   15.885  1.00 20.32 ? 184 LEU   A CD2 1 
ATOM   1241 N N   . THR   A 1 206 ? 5.511   4.686   15.231  1.00 17.68 ? 185 THR   A N   1 
ATOM   1242 C CA  . THR   A 1 206 ? 4.943   4.918   13.901  1.00 18.48 ? 185 THR   A CA  1 
ATOM   1243 C C   . THR   A 1 206 ? 4.025   6.142   13.957  1.00 18.38 ? 185 THR   A C   1 
ATOM   1244 O O   . THR   A 1 206 ? 4.123   7.047   13.136  1.00 18.94 ? 185 THR   A O   1 
ATOM   1245 C CB  . THR   A 1 206 ? 4.196   3.667   13.440  1.00 20.51 ? 185 THR   A CB  1 
ATOM   1246 O OG1 . THR   A 1 206 ? 5.150   2.618   13.501  1.00 19.07 ? 185 THR   A OG1 1 
ATOM   1247 C CG2 . THR   A 1 206 ? 3.658   3.759   12.016  1.00 19.93 ? 185 THR   A CG2 1 
ATOM   1248 N N   . GLN   A 1 207 ? 3.151   6.194   14.964  1.00 17.98 ? 186 GLN   A N   1 
ATOM   1249 C CA  . GLN   A 1 207 ? 2.198   7.294   15.002  1.00 18.66 ? 186 GLN   A CA  1 
ATOM   1250 C C   . GLN   A 1 207 ? 2.899   8.618   15.305  1.00 19.82 ? 186 GLN   A C   1 
ATOM   1251 O O   . GLN   A 1 207 ? 2.583   9.654   14.689  1.00 19.86 ? 186 GLN   A O   1 
ATOM   1252 C CB  . GLN   A 1 207 ? 1.204   6.987   16.131  1.00 21.46 ? 186 GLN   A CB  1 
ATOM   1253 C CG  . GLN   A 1 207 ? 0.305   5.806   15.764  1.00 24.92 ? 186 GLN   A CG  1 
ATOM   1254 C CD  . GLN   A 1 207 ? -0.654  5.387   16.860  1.00 29.55 ? 186 GLN   A CD  1 
ATOM   1255 O OE1 . GLN   A 1 207 ? -1.640  4.717   16.568  1.00 36.26 ? 186 GLN   A OE1 1 
ATOM   1256 N NE2 . GLN   A 1 207 ? -0.376  5.741   18.104  1.00 31.17 ? 186 GLN   A NE2 1 
ATOM   1257 N N   . SER   A 1 208 ? 3.746   8.613   16.358  1.00 18.89 ? 187 SER   A N   1 
ATOM   1258 C CA  . SER   A 1 208 ? 4.435   9.827   16.788  1.00 19.42 ? 187 SER   A CA  1 
ATOM   1259 C C   . SER   A 1 208 ? 5.318   10.381  15.668  1.00 19.32 ? 187 SER   A C   1 
ATOM   1260 O O   . SER   A 1 208 ? 5.324   11.597  15.414  1.00 20.05 ? 187 SER   A O   1 
ATOM   1261 C CB  . SER   A 1 208 ? 5.284   9.559   18.035  1.00 21.26 ? 187 SER   A CB  1 
ATOM   1262 O OG  . SER   A 1 208 ? 4.445   9.496   19.184  1.00 21.84 ? 187 SER   A OG  1 
ATOM   1263 N N   . ALA   A 1 209 ? 6.079   9.499   15.014  1.00 17.09 ? 188 ALA   A N   1 
ATOM   1264 C CA  . ALA   A 1 209 ? 6.931   9.988   13.933  1.00 19.65 ? 188 ALA   A CA  1 
ATOM   1265 C C   . ALA   A 1 209 ? 6.108   10.417  12.705  1.00 20.36 ? 188 ALA   A C   1 
ATOM   1266 O O   . ALA   A 1 209 ? 6.463   11.413  12.056  1.00 21.71 ? 188 ALA   A O   1 
ATOM   1267 C CB  . ALA   A 1 209 ? 7.950   8.949   13.570  1.00 16.52 ? 188 ALA   A CB  1 
ATOM   1268 N N   . ALA   A 1 210 ? 5.022   9.679   12.373  1.00 18.82 ? 189 ALA   A N   1 
ATOM   1269 C CA  . ALA   A 1 210 ? 4.147   10.128  11.281  1.00 19.84 ? 189 ALA   A CA  1 
ATOM   1270 C C   . ALA   A 1 210 ? 3.732   11.573  11.543  1.00 21.30 ? 189 ALA   A C   1 
ATOM   1271 O O   . ALA   A 1 210 ? 3.836   12.430  10.656  1.00 23.17 ? 189 ALA   A O   1 
ATOM   1272 C CB  . ALA   A 1 210 ? 2.894   9.280   11.162  1.00 18.60 ? 189 ALA   A CB  1 
ATOM   1273 N N   . LEU   A 1 211 ? 3.274   11.836  12.768  1.00 21.52 ? 190 LEU   A N   1 
ATOM   1274 C CA  . LEU   A 1 211 ? 2.803   13.173  13.111  1.00 23.12 ? 190 LEU   A CA  1 
ATOM   1275 C C   . LEU   A 1 211 ? 3.911   14.225  12.942  1.00 24.26 ? 190 LEU   A C   1 
ATOM   1276 O O   . LEU   A 1 211 ? 3.692   15.280  12.344  1.00 23.73 ? 190 LEU   A O   1 
ATOM   1277 C CB  . LEU   A 1 211 ? 2.233   13.194  14.527  1.00 23.68 ? 190 LEU   A CB  1 
ATOM   1278 C CG  . LEU   A 1 211 ? 1.860   14.574  15.076  1.00 27.48 ? 190 LEU   A CG  1 
ATOM   1279 C CD1 . LEU   A 1 211 ? 0.580   15.064  14.420  1.00 28.62 ? 190 LEU   A CD1 1 
ATOM   1280 C CD2 . LEU   A 1 211 ? 1.641   14.397  16.580  1.00 32.22 ? 190 LEU   A CD2 1 
ATOM   1281 N N   . GLU   A 1 212 ? 5.096   13.957  13.497  1.00 24.87 ? 191 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 212 ? 6.128   14.985  13.606  1.00 25.42 ? 191 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 212 ? 6.898   15.139  12.291  1.00 24.85 ? 191 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 212 ? 7.403   16.221  12.026  1.00 23.84 ? 191 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 212 ? 7.092   14.571  14.719  1.00 25.95 ? 191 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 212 ? 8.262   15.533  14.940  1.00 29.14 ? 191 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 212 ? 9.133   15.128  16.130  1.00 31.75 ? 191 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 212 ? 10.169  15.802  16.332  1.00 28.44 ? 191 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 212 ? 8.747   14.182  16.884  1.00 27.39 ? 191 GLU   A OE2 1 
ATOM   1290 N N   . LEU   A 1 213 ? 7.012   14.066  11.490  1.00 21.72 ? 192 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 213 ? 7.779   14.141  10.247  1.00 22.03 ? 192 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 213 ? 6.902   14.540  9.052   1.00 25.18 ? 192 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 213 ? 7.441   14.786  7.972   1.00 24.29 ? 192 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 213 ? 8.565   12.868  9.955   1.00 21.88 ? 192 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 213 ? 9.559   12.457  11.055  1.00 23.92 ? 192 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 213 ? 10.309  11.198  10.684  1.00 22.71 ? 192 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 213 ? 10.525  13.600  11.437  1.00 22.61 ? 192 LEU   A CD2 1 
ATOM   1298 N N   . ALA   A 1 214 ? 5.571   14.591  9.242   1.00 22.42 ? 193 ALA   A N   1 
ATOM   1299 C CA  . ALA   A 1 214 ? 4.671   14.964  8.151   1.00 26.86 ? 193 ALA   A CA  1 
ATOM   1300 C C   . ALA   A 1 214 ? 5.078   16.307  7.536   1.00 29.78 ? 193 ALA   A C   1 
ATOM   1301 O O   . ALA   A 1 214 ? 5.140   16.454  6.311   1.00 29.00 ? 193 ALA   A O   1 
ATOM   1302 C CB  . ALA   A 1 214 ? 3.239   15.032  8.618   1.00 23.52 ? 193 ALA   A CB  1 
ATOM   1303 N N   . PRO   A 1 215 ? 5.401   17.337  8.338   1.00 30.87 ? 194 PRO   A N   1 
ATOM   1304 C CA  . PRO   A 1 215 ? 5.779   18.631  7.762   1.00 33.17 ? 194 PRO   A CA  1 
ATOM   1305 C C   . PRO   A 1 215 ? 7.037   18.573  6.886   1.00 38.00 ? 194 PRO   A C   1 
ATOM   1306 O O   . PRO   A 1 215 ? 7.221   19.433  6.028   1.00 41.49 ? 194 PRO   A O   1 
ATOM   1307 C CB  . PRO   A 1 215 ? 5.923   19.553  8.997   1.00 33.66 ? 194 PRO   A CB  1 
ATOM   1308 C CG  . PRO   A 1 215 ? 5.173   18.824  10.096  1.00 34.21 ? 194 PRO   A CG  1 
ATOM   1309 C CD  . PRO   A 1 215 ? 5.413   17.339  9.807   1.00 27.69 ? 194 PRO   A CD  1 
ATOM   1310 N N   . TYR   A 1 216 ? 7.856   17.521  7.031   1.00 31.65 ? 195 TYR   A N   1 
ATOM   1311 C CA  . TYR   A 1 216 ? 9.071   17.386  6.237   1.00 31.55 ? 195 TYR   A CA  1 
ATOM   1312 C C   . TYR   A 1 216 ? 8.801   16.516  5.008   1.00 36.10 ? 195 TYR   A C   1 
ATOM   1313 O O   . TYR   A 1 216 ? 9.703   16.227  4.229   1.00 37.39 ? 195 TYR   A O   1 
ATOM   1314 C CB  . TYR   A 1 216 ? 10.249  16.886  7.094   1.00 41.19 ? 195 TYR   A CB  1 
ATOM   1315 C CG  . TYR   A 1 216 ? 10.546  17.695  8.353   0.70 40.56 ? 195 TYR   A CG  1 
ATOM   1316 C CD1 . TYR   A 1 216 ? 9.612   17.774  9.383   0.70 43.41 ? 195 TYR   A CD1 1 
ATOM   1317 C CD2 . TYR   A 1 216 ? 11.765  18.343  8.543   0.70 48.46 ? 195 TYR   A CD2 1 
ATOM   1318 C CE1 . TYR   A 1 216 ? 9.843   18.511  10.533  0.70 45.80 ? 195 TYR   A CE1 1 
ATOM   1319 C CE2 . TYR   A 1 216 ? 12.020  19.063  9.706   0.70 49.48 ? 195 TYR   A CE2 1 
ATOM   1320 C CZ  . TYR   A 1 216 ? 11.054  19.156  10.697  0.70 51.55 ? 195 TYR   A CZ  1 
ATOM   1321 O OH  . TYR   A 1 216 ? 11.242  19.841  11.868  0.70 52.08 ? 195 TYR   A OH  1 
ATOM   1322 N N   . GLY   A 1 217 ? 7.562   16.052  4.844   1.00 33.84 ? 196 GLY   A N   1 
ATOM   1323 C CA  . GLY   A 1 217 ? 7.244   15.243  3.687   1.00 27.73 ? 196 GLY   A CA  1 
ATOM   1324 C C   . GLY   A 1 217 ? 7.650   13.783  3.886   1.00 29.90 ? 196 GLY   A C   1 
ATOM   1325 O O   . GLY   A 1 217 ? 7.677   13.014  2.930   1.00 33.49 ? 196 GLY   A O   1 
ATOM   1326 N N   . ILE   A 1 218 ? 7.973   13.390  5.122   1.00 23.30 ? 197 ILE   A N   1 
ATOM   1327 C CA  . ILE   A 1 218 ? 8.323   11.985  5.335   1.00 22.24 ? 197 ILE   A CA  1 
ATOM   1328 C C   . ILE   A 1 218 ? 7.109   11.247  5.902   1.00 22.32 ? 197 ILE   A C   1 
ATOM   1329 O O   . ILE   A 1 218 ? 6.633   11.582  6.985   1.00 22.11 ? 197 ILE   A O   1 
ATOM   1330 C CB  . ILE   A 1 218 ? 9.493   11.892  6.325   1.00 23.96 ? 197 ILE   A CB  1 
ATOM   1331 C CG1 . ILE   A 1 218 ? 10.699  12.720  5.798   1.00 25.85 ? 197 ILE   A CG1 1 
ATOM   1332 C CG2 . ILE   A 1 218 ? 9.856   10.425  6.595   1.00 25.46 ? 197 ILE   A CG2 1 
ATOM   1333 C CD1 . ILE   A 1 218 ? 11.765  12.984  6.850   1.00 29.22 ? 197 ILE   A CD1 1 
ATOM   1334 N N   . ARG   A 1 219 ? 6.663   10.201  5.194   1.00 22.11 ? 198 ARG   A N   1 
ATOM   1335 C CA  . ARG   A 1 219 ? 5.522   9.415   5.632   1.00 23.52 ? 198 ARG   A CA  1 
ATOM   1336 C C   . ARG   A 1 219 ? 6.065   8.277   6.485   1.00 22.56 ? 198 ARG   A C   1 
ATOM   1337 O O   . ARG   A 1 219 ? 7.193   7.840   6.263   1.00 23.92 ? 198 ARG   A O   1 
ATOM   1338 C CB  . ARG   A 1 219 ? 4.791   8.846   4.401   1.00 23.20 ? 198 ARG   A CB  1 
ATOM   1339 C CG  . ARG   A 1 219 ? 4.081   9.932   3.607   1.00 22.79 ? 198 ARG   A CG  1 
ATOM   1340 C CD  . ARG   A 1 219 ? 3.372   9.406   2.324   1.00 21.82 ? 198 ARG   A CD  1 
ATOM   1341 N NE  . ARG   A 1 219 ? 4.283   8.648   1.453   1.00 22.05 ? 198 ARG   A NE  1 
ATOM   1342 C CZ  . ARG   A 1 219 ? 4.322   7.325   1.373   1.00 23.00 ? 198 ARG   A CZ  1 
ATOM   1343 N NH1 . ARG   A 1 219 ? 3.490   6.569   2.087   1.00 23.54 ? 198 ARG   A NH1 1 
ATOM   1344 N NH2 . ARG   A 1 219 ? 5.218   6.758   0.600   1.00 22.86 ? 198 ARG   A NH2 1 
ATOM   1345 N N   . VAL   A 1 220 ? 5.292   7.851   7.489   1.00 19.01 ? 199 VAL   A N   1 
ATOM   1346 C CA  . VAL   A 1 220 ? 5.741   6.801   8.387   1.00 18.86 ? 199 VAL   A CA  1 
ATOM   1347 C C   . VAL   A 1 220 ? 4.576   5.829   8.574   1.00 18.42 ? 199 VAL   A C   1 
ATOM   1348 O O   . VAL   A 1 220 ? 3.543   6.206   9.116   1.00 21.23 ? 199 VAL   A O   1 
ATOM   1349 C CB  . VAL   A 1 220 ? 6.221   7.326   9.768   1.00 18.26 ? 199 VAL   A CB  1 
ATOM   1350 C CG1 . VAL   A 1 220 ? 6.757   6.181   10.621  1.00 18.07 ? 199 VAL   A CG1 1 
ATOM   1351 C CG2 . VAL   A 1 220 ? 7.275   8.463   9.696   1.00 18.77 ? 199 VAL   A CG2 1 
ATOM   1352 N N   . ASN   A 1 221 ? 4.766   4.567   8.187   1.00 17.29 ? 200 ASN   A N   1 
ATOM   1353 C CA  . ASN   A 1 221 ? 3.663   3.619   8.185   1.00 19.89 ? 200 ASN   A CA  1 
ATOM   1354 C C   . ASN   A 1 221 ? 4.200   2.286   8.710   1.00 19.97 ? 200 ASN   A C   1 
ATOM   1355 O O   . ASN   A 1 221 ? 5.403   2.130   8.901   1.00 19.71 ? 200 ASN   A O   1 
ATOM   1356 C CB  . ASN   A 1 221 ? 3.103   3.446   6.764   1.00 18.72 ? 200 ASN   A CB  1 
ATOM   1357 C CG  . ASN   A 1 221 ? 2.441   4.732   6.290   1.00 21.40 ? 200 ASN   A CG  1 
ATOM   1358 O OD1 . ASN   A 1 221 ? 1.416   5.140   6.846   1.00 19.50 ? 200 ASN   A OD1 1 
ATOM   1359 N ND2 . ASN   A 1 221 ? 3.019   5.416   5.312   1.00 18.47 ? 200 ASN   A ND2 1 
ATOM   1360 N N   . GLY   A 1 222 ? 3.281   1.343   8.948   1.00 18.99 ? 201 GLY   A N   1 
ATOM   1361 C CA  . GLY   A 1 222 ? 3.647   0.005   9.414   1.00 17.41 ? 201 GLY   A CA  1 
ATOM   1362 C C   . GLY   A 1 222 ? 2.984   -1.067  8.545   1.00 17.34 ? 201 GLY   A C   1 
ATOM   1363 O O   . GLY   A 1 222 ? 1.964   -0.818  7.920   1.00 20.11 ? 201 GLY   A O   1 
ATOM   1364 N N   . VAL   A 1 223 ? 3.618   -2.250  8.504   1.00 18.17 ? 202 VAL   A N   1 
ATOM   1365 C CA  . VAL   A 1 223 ? 3.069   -3.495  8.010   1.00 19.00 ? 202 VAL   A CA  1 
ATOM   1366 C C   . VAL   A 1 223 ? 3.102   -4.473  9.176   1.00 21.77 ? 202 VAL   A C   1 
ATOM   1367 O O   . VAL   A 1 223 ? 4.158   -4.619  9.795   1.00 19.97 ? 202 VAL   A O   1 
ATOM   1368 C CB  . VAL   A 1 223 ? 3.944   -4.026  6.860   1.00 18.92 ? 202 VAL   A CB  1 
ATOM   1369 C CG1 . VAL   A 1 223 ? 3.560   -5.460  6.496   1.00 22.73 ? 202 VAL   A CG1 1 
ATOM   1370 C CG2 . VAL   A 1 223 ? 3.828   -3.112  5.646   1.00 18.92 ? 202 VAL   A CG2 1 
ATOM   1371 N N   . ALA   A 1 224 ? 1.955   -5.147  9.451   1.00 20.35 ? 203 ALA   A N   1 
ATOM   1372 C CA  . ALA   A 1 224 ? 1.846   -6.026  10.601  1.00 19.27 ? 203 ALA   A CA  1 
ATOM   1373 C C   . ALA   A 1 224 ? 1.518   -7.440  10.120  1.00 19.41 ? 203 ALA   A C   1 
ATOM   1374 O O   . ALA   A 1 224 ? 0.350   -7.756  9.883   1.00 18.99 ? 203 ALA   A O   1 
ATOM   1375 C CB  . ALA   A 1 224 ? 0.755   -5.506  11.532  1.00 16.87 ? 203 ALA   A CB  1 
ATOM   1376 N N   . PRO   A 1 225 ? 2.530   -8.343  9.982   1.00 20.20 ? 204 PRO   A N   1 
ATOM   1377 C CA  . PRO   A 1 225 ? 2.270   -9.741  9.629   1.00 19.54 ? 204 PRO   A CA  1 
ATOM   1378 C C   . PRO   A 1 225 ? 1.585   -10.401 10.807  1.00 21.78 ? 204 PRO   A C   1 
ATOM   1379 O O   . PRO   A 1 225 ? 1.744   -9.950  11.955  1.00 20.37 ? 204 PRO   A O   1 
ATOM   1380 C CB  . PRO   A 1 225 ? 3.678   -10.334 9.471   1.00 21.00 ? 204 PRO   A CB  1 
ATOM   1381 C CG  . PRO   A 1 225 ? 4.547   -9.111  9.255   1.00 22.64 ? 204 PRO   A CG  1 
ATOM   1382 C CD  . PRO   A 1 225 ? 3.952   -8.074  10.188  1.00 21.35 ? 204 PRO   A CD  1 
ATOM   1383 N N   . GLY   A 1 226 ? 0.904   -11.513 10.499  1.00 20.91 ? 205 GLY   A N   1 
ATOM   1384 C CA  . GLY   A 1 226 ? 0.433   -12.411 11.537  1.00 21.10 ? 205 GLY   A CA  1 
ATOM   1385 C C   . GLY   A 1 226 ? 1.434   -13.555 11.629  1.00 24.42 ? 205 GLY   A C   1 
ATOM   1386 O O   . GLY   A 1 226 ? 2.392   -13.510 12.396  1.00 28.42 ? 205 GLY   A O   1 
ATOM   1387 N N   . VAL   A 1 227 ? 1.169   -14.590 10.850  1.00 24.54 ? 206 VAL   A N   1 
ATOM   1388 C CA  . VAL   A 1 227 ? 2.136   -15.656 10.750  1.00 28.34 ? 206 VAL   A CA  1 
ATOM   1389 C C   . VAL   A 1 227 ? 2.625   -15.560 9.319   1.00 26.55 ? 206 VAL   A C   1 
ATOM   1390 O O   . VAL   A 1 227 ? 1.826   -15.512 8.383   1.00 27.02 ? 206 VAL   A O   1 
ATOM   1391 C CB  . VAL   A 1 227 ? 1.626   -17.056 11.168  1.00 33.46 ? 206 VAL   A CB  1 
ATOM   1392 C CG1 . VAL   A 1 227 ? 0.492   -17.565 10.313  1.00 30.84 ? 206 VAL   A CG1 1 
ATOM   1393 C CG2 . VAL   A 1 227 ? 2.741   -18.093 11.137  1.00 40.79 ? 206 VAL   A CG2 1 
ATOM   1394 N N   . SER   A 1 228 ? 3.935   -15.369 9.195   1.00 25.53 ? 207 SER   A N   1 
ATOM   1395 C CA  . SER   A 1 228 ? 4.586   -15.383 7.902   1.00 25.43 ? 207 SER   A CA  1 
ATOM   1396 C C   . SER   A 1 228 ? 5.632   -16.487 8.005   1.00 28.70 ? 207 SER   A C   1 
ATOM   1397 O O   . SER   A 1 228 ? 5.364   -17.511 8.642   1.00 28.37 ? 207 SER   A O   1 
ATOM   1398 C CB  . SER   A 1 228 ? 5.165   -14.016 7.600   1.00 24.93 ? 207 SER   A CB  1 
ATOM   1399 O OG  . SER   A 1 228 ? 5.698   -14.012 6.283   1.00 28.45 ? 207 SER   A OG  1 
ATOM   1400 N N   . LEU   A 1 229 ? 6.838   -16.284 7.463   1.00 31.10 ? 208 LEU   A N   1 
ATOM   1401 C CA  . LEU   A 1 229 ? 7.805   -17.384 7.483   1.00 30.03 ? 208 LEU   A CA  1 
ATOM   1402 C C   . LEU   A 1 229 ? 8.036   -17.794 8.929   1.00 32.66 ? 208 LEU   A C   1 
ATOM   1403 O O   . LEU   A 1 229 ? 8.352   -16.950 9.773   1.00 30.61 ? 208 LEU   A O   1 
ATOM   1404 C CB  . LEU   A 1 229 ? 9.137   -17.027 6.822   1.00 32.36 ? 208 LEU   A CB  1 
ATOM   1405 C CG  . LEU   A 1 229 ? 9.048   -16.586 5.362   1.00 38.34 ? 208 LEU   A CG  1 
ATOM   1406 C CD1 . LEU   A 1 229 ? 10.461  -16.201 4.960   1.00 35.72 ? 208 LEU   A CD1 1 
ATOM   1407 C CD2 . LEU   A 1 229 ? 8.474   -17.726 4.496   1.00 41.60 ? 208 LEU   A CD2 1 
ATOM   1408 N N   . LEU   A 1 230 ? 7.863   -19.093 9.186   1.00 30.33 ? 209 LEU   A N   1 
ATOM   1409 C CA  . LEU   A 1 230 ? 8.016   -19.642 10.512  1.00 34.43 ? 209 LEU   A CA  1 
ATOM   1410 C C   . LEU   A 1 230 ? 9.509   -19.720 10.834  1.00 37.30 ? 209 LEU   A C   1 
ATOM   1411 O O   . LEU   A 1 230 ? 10.334  -19.808 9.920   1.00 33.53 ? 209 LEU   A O   1 
ATOM   1412 C CB  . LEU   A 1 230 ? 7.314   -21.005 10.578  1.00 33.51 ? 209 LEU   A CB  1 
ATOM   1413 C CG  . LEU   A 1 230 ? 5.804   -21.025 10.873  1.00 37.58 ? 209 LEU   A CG  1 
ATOM   1414 C CD1 . LEU   A 1 230 ? 5.343   -19.895 11.773  1.00 36.97 ? 209 LEU   A CD1 1 
ATOM   1415 C CD2 . LEU   A 1 230 ? 4.850   -21.226 9.703   1.00 39.76 ? 209 LEU   A CD2 1 
ATOM   1416 N N   . PRO   A 1 231 ? 9.882   -19.661 12.136  1.00 42.68 ? 210 PRO   A N   1 
ATOM   1417 C CA  . PRO   A 1 231 ? 11.271  -19.832 12.576  1.00 44.50 ? 210 PRO   A CA  1 
ATOM   1418 C C   . PRO   A 1 231 ? 11.896  -21.078 11.957  1.00 43.52 ? 210 PRO   A C   1 
ATOM   1419 O O   . PRO   A 1 231 ? 11.221  -22.096 11.796  1.00 33.82 ? 210 PRO   A O   1 
ATOM   1420 C CB  . PRO   A 1 231 ? 11.203  -19.949 14.126  1.00 45.41 ? 210 PRO   A CB  1 
ATOM   1421 C CG  . PRO   A 1 231 ? 9.859   -19.367 14.509  1.00 48.45 ? 210 PRO   A CG  1 
ATOM   1422 C CD  . PRO   A 1 231 ? 8.957   -19.478 13.272  1.00 47.10 ? 210 PRO   A CD  1 
ATOM   1423 N N   . VAL   A 1 232 ? 13.191  -20.976 11.628  1.00 43.96 ? 211 VAL   A N   1 
ATOM   1424 C CA  . VAL   A 1 232 ? 13.919  -22.035 10.938  1.00 51.06 ? 211 VAL   A CA  1 
ATOM   1425 C C   . VAL   A 1 232 ? 13.899  -23.311 11.778  1.00 50.86 ? 211 VAL   A C   1 
ATOM   1426 O O   . VAL   A 1 232 ? 13.742  -24.409 11.244  1.00 47.83 ? 211 VAL   A O   1 
ATOM   1427 C CB  . VAL   A 1 232 ? 15.368  -21.646 10.564  1.00 57.29 ? 211 VAL   A CB  1 
ATOM   1428 C CG1 . VAL   A 1 232 ? 15.483  -21.140 9.132   1.00 59.48 ? 211 VAL   A CG1 1 
ATOM   1429 C CG2 . VAL   A 1 232 ? 15.997  -20.660 11.549  1.00 55.70 ? 211 VAL   A CG2 1 
ATOM   1430 N N   . ALA   A 1 233 ? 14.030  -23.136 13.098  1.00 49.81 ? 212 ALA   A N   1 
ATOM   1431 C CA  . ALA   A 1 233 ? 14.180  -24.245 14.029  1.00 55.98 ? 212 ALA   A CA  1 
ATOM   1432 C C   . ALA   A 1 233 ? 12.820  -24.741 14.528  1.00 50.01 ? 212 ALA   A C   1 
ATOM   1433 O O   . ALA   A 1 233 ? 12.741  -25.616 15.392  1.00 46.67 ? 212 ALA   A O   1 
ATOM   1434 C CB  . ALA   A 1 233 ? 15.093  -23.836 15.172  1.00 55.29 ? 212 ALA   A CB  1 
ATOM   1435 N N   . MET   A 1 234 ? 11.731  -24.192 13.985  1.00 41.02 ? 213 MET   A N   1 
ATOM   1436 C CA  . MET   A 1 234 ? 10.433  -24.703 14.390  1.00 40.76 ? 213 MET   A CA  1 
ATOM   1437 C C   . MET   A 1 234 ? 10.166  -26.005 13.631  1.00 36.57 ? 213 MET   A C   1 
ATOM   1438 O O   . MET   A 1 234 ? 10.386  -26.054 12.428  1.00 38.70 ? 213 MET   A O   1 
ATOM   1439 C CB  . MET   A 1 234 ? 9.332   -23.648 14.185  1.00 37.07 ? 213 MET   A CB  1 
ATOM   1440 C CG  . MET   A 1 234 ? 7.962   -24.108 14.649  1.00 35.56 ? 213 MET   A CG  1 
ATOM   1441 S SD  . MET   A 1 234 ? 6.659   -22.882 14.360  1.00 40.64 ? 213 MET   A SD  1 
ATOM   1442 C CE  . MET   A 1 234 ? 6.981   -21.694 15.674  1.00 42.24 ? 213 MET   A CE  1 
ATOM   1443 N N   . GLY   A 1 235 ? 9.667   -27.032 14.337  1.00 39.13 ? 214 GLY   A N   1 
ATOM   1444 C CA  . GLY   A 1 235 ? 9.285   -28.311 13.746  1.00 41.95 ? 214 GLY   A CA  1 
ATOM   1445 C C   . GLY   A 1 235 ? 8.056   -28.173 12.849  1.00 44.46 ? 214 GLY   A C   1 
ATOM   1446 O O   . GLY   A 1 235 ? 7.188   -27.330 13.097  1.00 42.18 ? 214 GLY   A O   1 
ATOM   1447 N N   . GLU   A 1 236 ? 7.980   -29.032 11.825  1.00 38.36 ? 215 GLU   A N   1 
ATOM   1448 C CA  . GLU   A 1 236 ? 6.903   -29.001 10.842  1.00 41.08 ? 215 GLU   A CA  1 
ATOM   1449 C C   . GLU   A 1 236 ? 5.528   -29.113 11.500  1.00 40.65 ? 215 GLU   A C   1 
ATOM   1450 O O   . GLU   A 1 236 ? 4.602   -28.422 11.082  1.00 36.96 ? 215 GLU   A O   1 
ATOM   1451 C CB  . GLU   A 1 236 ? 7.027   -30.083 9.770   1.00 41.00 ? 215 GLU   A CB  1 
ATOM   1452 C CG  . GLU   A 1 236 ? 6.077   -29.857 8.596   1.00 38.95 ? 215 GLU   A CG  1 
ATOM   1453 C CD  . GLU   A 1 236 ? 6.342   -28.649 7.706   1.00 41.95 ? 215 GLU   A CD  1 
ATOM   1454 O OE1 . GLU   A 1 236 ? 7.421   -28.004 7.760   1.00 39.80 ? 215 GLU   A OE1 1 
ATOM   1455 O OE2 . GLU   A 1 236 ? 5.424   -28.362 6.909   1.00 48.74 ? 215 GLU   A OE2 1 
ATOM   1456 N N   . GLU   A 1 237 ? 5.394   -29.990 12.507  1.00 41.02 ? 216 GLU   A N   1 
ATOM   1457 C CA  . GLU   A 1 237 ? 4.106   -30.196 13.167  1.00 43.35 ? 216 GLU   A CA  1 
ATOM   1458 C C   . GLU   A 1 237 ? 3.664   -28.914 13.880  1.00 43.33 ? 216 GLU   A C   1 
ATOM   1459 O O   . GLU   A 1 237 ? 2.482   -28.592 13.886  1.00 42.13 ? 216 GLU   A O   1 
ATOM   1460 C CB  . GLU   A 1 237 ? 4.081   -31.362 14.164  1.00 46.17 ? 216 GLU   A CB  1 
ATOM   1461 N N   . GLU   A 1 238 ? 4.627   -28.189 14.474  1.00 45.39 ? 217 GLU   A N   1 
ATOM   1462 C CA  . GLU   A 1 238 ? 4.344   -26.939 15.177  1.00 45.96 ? 217 GLU   A CA  1 
ATOM   1463 C C   . GLU   A 1 238 ? 3.993   -25.838 14.167  1.00 40.66 ? 217 GLU   A C   1 
ATOM   1464 O O   . GLU   A 1 238 ? 3.146   -24.987 14.447  1.00 37.47 ? 217 GLU   A O   1 
ATOM   1465 C CB  . GLU   A 1 238 ? 5.485   -26.516 16.111  1.00 43.83 ? 217 GLU   A CB  1 
ATOM   1466 C CG  . GLU   A 1 238 ? 5.115   -25.309 16.968  0.50 40.04 ? 217 GLU   A CG  1 
ATOM   1467 C CD  . GLU   A 1 238 ? 6.151   -24.763 17.933  0.50 43.58 ? 217 GLU   A CD  1 
ATOM   1468 O OE1 . GLU   A 1 238 ? 7.264   -25.329 18.048  0.50 42.82 ? 217 GLU   A OE1 1 
ATOM   1469 O OE2 . GLU   A 1 238 ? 5.823   -23.740 18.576  0.50 42.00 ? 217 GLU   A OE2 1 
ATOM   1470 N N   . LYS   A 1 239 ? 4.663   -25.851 13.002  1.00 35.04 ? 218 LYS   A N   1 
ATOM   1471 C CA  . LYS   A 1 239 ? 4.318   -24.958 11.898  1.00 33.59 ? 218 LYS   A CA  1 
ATOM   1472 C C   . LYS   A 1 239 ? 2.868   -25.162 11.454  1.00 33.08 ? 218 LYS   A C   1 
ATOM   1473 O O   . LYS   A 1 239 ? 2.137   -24.193 11.251  1.00 30.01 ? 218 LYS   A O   1 
ATOM   1474 C CB  . LYS   A 1 239 ? 5.260   -25.064 10.691  1.00 34.86 ? 218 LYS   A CB  1 
ATOM   1475 C CG  . LYS   A 1 239 ? 6.688   -24.612 10.989  1.00 39.27 ? 218 LYS   A CG  1 
ATOM   1476 C CD  . LYS   A 1 239 ? 7.660   -24.728 9.819   1.00 39.00 ? 218 LYS   A CD  1 
ATOM   1477 C CE  . LYS   A 1 239 ? 9.030   -24.192 10.153  1.00 47.39 ? 218 LYS   A CE  1 
ATOM   1478 N NZ  . LYS   A 1 239 ? 10.020  -24.552 9.127   1.00 47.57 ? 218 LYS   A NZ  1 
ATOM   1479 N N   . ASP   A 1 240 ? 2.443   -26.426 11.306  1.00 33.26 ? 219 ASP   A N   1 
ATOM   1480 C CA  . ASP   A 1 240 ? 1.097   -26.687 10.828  1.00 33.95 ? 219 ASP   A CA  1 
ATOM   1481 C C   . ASP   A 1 240 ? 0.035   -26.246 11.831  1.00 35.86 ? 219 ASP   A C   1 
ATOM   1482 O O   . ASP   A 1 240 ? -1.090  -25.943 11.432  1.00 30.83 ? 219 ASP   A O   1 
ATOM   1483 C CB  . ASP   A 1 240 ? 0.918   -28.126 10.375  1.00 40.92 ? 219 ASP   A CB  1 
ATOM   1484 C CG  . ASP   A 1 240 ? 1.618   -28.451 9.061   1.00 45.57 ? 219 ASP   A CG  1 
ATOM   1485 O OD1 . ASP   A 1 240 ? 1.833   -27.516 8.248   1.00 41.65 ? 219 ASP   A OD1 1 
ATOM   1486 O OD2 . ASP   A 1 240 ? 1.978   -29.621 8.885   1.00 45.87 ? 219 ASP   A OD2 1 
ATOM   1487 N N   . LYS   A 1 241 ? 0.352   -26.316 13.131  1.00 37.09 ? 220 LYS   A N   1 
ATOM   1488 C CA  . LYS   A 1 241 ? -0.585  -25.858 14.147  1.00 39.61 ? 220 LYS   A CA  1 
ATOM   1489 C C   . LYS   A 1 241 ? -0.863  -24.365 13.924  1.00 33.31 ? 220 LYS   A C   1 
ATOM   1490 O O   . LYS   A 1 241 ? -2.012  -23.937 13.996  1.00 35.51 ? 220 LYS   A O   1 
ATOM   1491 C CB  . LYS   A 1 241 ? -0.094  -26.235 15.553  1.00 43.28 ? 220 LYS   A CB  1 
ATOM   1492 N N   . TRP   A 1 242 ? 0.178   -23.596 13.569  1.00 32.86 ? 221 TRP   A N   1 
ATOM   1493 C CA  . TRP   A 1 242 ? -0.011  -22.182 13.284  1.00 31.26 ? 221 TRP   A CA  1 
ATOM   1494 C C   . TRP   A 1 242 ? -0.787  -21.983 11.984  1.00 32.97 ? 221 TRP   A C   1 
ATOM   1495 O O   . TRP   A 1 242 ? -1.725  -21.185 11.943  1.00 31.75 ? 221 TRP   A O   1 
ATOM   1496 C CB  . TRP   A 1 242 ? 1.338   -21.468 13.272  1.00 33.86 ? 221 TRP   A CB  1 
ATOM   1497 C CG  . TRP   A 1 242 ? 1.794   -21.147 14.663  1.00 44.97 ? 221 TRP   A CG  1 
ATOM   1498 C CD1 . TRP   A 1 242 ? 2.678   -21.837 15.446  1.00 47.83 ? 221 TRP   A CD1 1 
ATOM   1499 C CD2 . TRP   A 1 242 ? 1.301   -20.052 15.463  1.00 48.64 ? 221 TRP   A CD2 1 
ATOM   1500 N NE1 . TRP   A 1 242 ? 2.794   -21.227 16.665  1.00 49.52 ? 221 TRP   A NE1 1 
ATOM   1501 C CE2 . TRP   A 1 242 ? 1.963   -20.133 16.709  1.00 50.84 ? 221 TRP   A CE2 1 
ATOM   1502 C CE3 . TRP   A 1 242 ? 0.382   -19.019 15.241  1.00 46.19 ? 221 TRP   A CE3 1 
ATOM   1503 C CZ2 . TRP   A 1 242 ? 1.719   -19.218 17.731  1.00 50.80 ? 221 TRP   A CZ2 1 
ATOM   1504 C CZ3 . TRP   A 1 242 ? 0.138   -18.123 16.259  1.00 53.33 ? 221 TRP   A CZ3 1 
ATOM   1505 C CH2 . TRP   A 1 242 ? 0.786   -18.233 17.490  1.00 48.17 ? 221 TRP   A CH2 1 
ATOM   1506 N N   . ARG   A 1 243 ? -0.412  -22.725 10.927  1.00 27.54 ? 222 ARG   A N   1 
ATOM   1507 C CA  . ARG   A 1 243 ? -1.054  -22.590 9.624   1.00 28.62 ? 222 ARG   A CA  1 
ATOM   1508 C C   . ARG   A 1 243 ? -2.569  -22.805 9.710   1.00 28.68 ? 222 ARG   A C   1 
ATOM   1509 O O   . ARG   A 1 243 ? -3.345  -22.095 9.065   1.00 29.19 ? 222 ARG   A O   1 
ATOM   1510 C CB  . ARG   A 1 243 ? -0.444  -23.595 8.631   1.00 25.28 ? 222 ARG   A CB  1 
ATOM   1511 C CG  . ARG   A 1 243 ? 0.995   -23.218 8.358   1.00 27.77 ? 222 ARG   A CG  1 
ATOM   1512 C CD  . ARG   A 1 243 ? 1.617   -24.336 7.554   1.00 29.84 ? 222 ARG   A CD  1 
ATOM   1513 N NE  . ARG   A 1 243 ? 2.934   -23.860 7.136   1.00 28.81 ? 222 ARG   A NE  1 
ATOM   1514 C CZ  . ARG   A 1 243 ? 3.960   -24.662 6.968   1.00 32.08 ? 222 ARG   A CZ  1 
ATOM   1515 N NH1 . ARG   A 1 243 ? 3.845   -25.941 7.298   1.00 30.33 ? 222 ARG   A NH1 1 
ATOM   1516 N NH2 . ARG   A 1 243 ? 5.078   -24.181 6.449   1.00 30.15 ? 222 ARG   A NH2 1 
ATOM   1517 N N   . ARG   A 1 244 ? -2.995  -23.804 10.485  1.00 25.27 ? 223 ARG   A N   1 
ATOM   1518 C CA  . ARG   A 1 244 ? -4.405  -24.161 10.540  1.00 28.70 ? 223 ARG   A CA  1 
ATOM   1519 C C   . ARG   A 1 244 ? -5.259  -23.074 11.214  1.00 29.66 ? 223 ARG   A C   1 
ATOM   1520 O O   . ARG   A 1 244 ? -6.475  -23.117 11.121  1.00 30.64 ? 223 ARG   A O   1 
ATOM   1521 C CB  . ARG   A 1 244 ? -4.677  -25.485 11.267  1.00 33.97 ? 223 ARG   A CB  1 
ATOM   1522 C CG  . ARG   A 1 244 ? -4.424  -26.724 10.417  1.00 42.65 ? 223 ARG   A CG  1 
ATOM   1523 C CD  . ARG   A 1 244 ? -4.822  -28.011 11.137  0.60 42.45 ? 223 ARG   A CD  1 
ATOM   1524 N NE  . ARG   A 1 244 ? -3.928  -28.299 12.267  0.60 45.78 ? 223 ARG   A NE  1 
ATOM   1525 C CZ  . ARG   A 1 244 ? -2.759  -28.941 12.187  0.60 43.84 ? 223 ARG   A CZ  1 
ATOM   1526 N NH1 . ARG   A 1 244 ? -2.356  -29.470 11.043  0.60 41.64 ? 223 ARG   A NH1 1 
ATOM   1527 N NH2 . ARG   A 1 244 ? -2.010  -29.069 13.266  0.60 39.30 ? 223 ARG   A NH2 1 
ATOM   1528 N N   . LYS   A 1 245 ? -4.641  -22.106 11.887  1.00 27.29 ? 224 LYS   A N   1 
ATOM   1529 C CA  . LYS   A 1 245 ? -5.413  -21.077 12.570  1.00 30.66 ? 224 LYS   A CA  1 
ATOM   1530 C C   . LYS   A 1 245 ? -5.785  -19.946 11.602  1.00 27.48 ? 224 LYS   A C   1 
ATOM   1531 O O   . LYS   A 1 245 ? -6.572  -19.066 11.959  1.00 26.97 ? 224 LYS   A O   1 
ATOM   1532 C CB  . LYS   A 1 245 ? -4.525  -20.452 13.659  1.00 28.70 ? 224 LYS   A CB  1 
ATOM   1533 C CG  . LYS   A 1 245 ? -4.186  -21.310 14.905  1.00 36.13 ? 224 LYS   A CG  1 
ATOM   1534 C CD  . LYS   A 1 245 ? -3.058  -20.609 15.681  1.00 40.32 ? 224 LYS   A CD  1 
ATOM   1535 C CE  . LYS   A 1 245 ? -2.444  -21.336 16.864  1.00 46.83 ? 224 LYS   A CE  1 
ATOM   1536 N NZ  . LYS   A 1 245 ? -3.468  -22.066 17.630  1.00 47.28 ? 224 LYS   A NZ  1 
ATOM   1537 N N   . VAL   A 1 246 ? -5.150  -19.899 10.423  1.00 23.79 ? 225 VAL   A N   1 
ATOM   1538 C CA  . VAL   A 1 246 ? -5.342  -18.759 9.522   1.00 22.98 ? 225 VAL   A CA  1 
ATOM   1539 C C   . VAL   A 1 246 ? -6.610  -18.965 8.689   1.00 22.66 ? 225 VAL   A C   1 
ATOM   1540 O O   . VAL   A 1 246 ? -6.632  -19.892 7.857   1.00 25.28 ? 225 VAL   A O   1 
ATOM   1541 C CB  . VAL   A 1 246 ? -4.122  -18.532 8.598   1.00 21.57 ? 225 VAL   A CB  1 
ATOM   1542 C CG1 . VAL   A 1 246 ? -4.390  -17.415 7.567   1.00 21.09 ? 225 VAL   A CG1 1 
ATOM   1543 C CG2 . VAL   A 1 246 ? -2.839  -18.276 9.395   1.00 20.82 ? 225 VAL   A CG2 1 
ATOM   1544 N N   . PRO   A 1 247 ? -7.652  -18.087 8.820   1.00 22.87 ? 226 PRO   A N   1 
ATOM   1545 C CA  . PRO   A 1 247 ? -8.873  -18.162 7.996   1.00 25.43 ? 226 PRO   A CA  1 
ATOM   1546 C C   . PRO   A 1 247 ? -8.659  -18.167 6.480   1.00 24.69 ? 226 PRO   A C   1 
ATOM   1547 O O   . PRO   A 1 247 ? -9.287  -18.931 5.733   1.00 25.76 ? 226 PRO   A O   1 
ATOM   1548 C CB  . PRO   A 1 247 ? -9.658  -16.878 8.438   1.00 24.92 ? 226 PRO   A CB  1 
ATOM   1549 C CG  . PRO   A 1 247 ? -9.183  -16.633 9.845   1.00 21.37 ? 226 PRO   A CG  1 
ATOM   1550 C CD  . PRO   A 1 247 ? -7.696  -16.933 9.751   1.00 22.17 ? 226 PRO   A CD  1 
ATOM   1551 N N   . LEU   A 1 248 ? -7.731  -17.326 6.018   1.00 24.13 ? 227 LEU   A N   1 
ATOM   1552 C CA  . LEU   A 1 248 ? -7.562  -17.158 4.584   1.00 25.98 ? 227 LEU   A CA  1 
ATOM   1553 C C   . LEU   A 1 248 ? -6.552  -18.177 4.065   1.00 24.64 ? 227 LEU   A C   1 
ATOM   1554 O O   . LEU   A 1 248 ? -5.392  -17.842 3.850   1.00 26.91 ? 227 LEU   A O   1 
ATOM   1555 C CB  . LEU   A 1 248 ? -7.137  -15.726 4.225   1.00 24.49 ? 227 LEU   A CB  1 
ATOM   1556 C CG  . LEU   A 1 248 ? -7.306  -15.303 2.756   1.00 26.46 ? 227 LEU   A CG  1 
ATOM   1557 C CD1 . LEU   A 1 248 ? -8.763  -15.236 2.323   1.00 27.38 ? 227 LEU   A CD1 1 
ATOM   1558 C CD2 . LEU   A 1 248 ? -6.648  -13.944 2.515   1.00 24.81 ? 227 LEU   A CD2 1 
ATOM   1559 N N   . GLY   A 1 249 ? -6.997  -19.407 3.822   1.00 28.27 ? 228 GLY   A N   1 
ATOM   1560 C CA  . GLY   A 1 249 ? -6.134  -20.348 3.130   1.00 27.93 ? 228 GLY   A CA  1 
ATOM   1561 C C   . GLY   A 1 249 ? -5.403  -21.328 4.042   1.00 28.01 ? 228 GLY   A C   1 
ATOM   1562 O O   . GLY   A 1 249 ? -4.732  -22.204 3.519   1.00 25.80 ? 228 GLY   A O   1 
ATOM   1563 N N   . ARG   A 1 250 ? -5.452  -21.131 5.380   1.00 29.13 ? 229 ARG   A N   1 
ATOM   1564 C CA  . ARG   A 1 250 ? -4.782  -21.990 6.357   1.00 27.68 ? 229 ARG   A CA  1 
ATOM   1565 C C   . ARG   A 1 250 ? -3.294  -22.134 6.040   1.00 28.71 ? 229 ARG   A C   1 
ATOM   1566 O O   . ARG   A 1 250 ? -2.730  -23.243 6.064   1.00 25.29 ? 229 ARG   A O   1 
ATOM   1567 C CB  . ARG   A 1 250 ? -5.388  -23.397 6.447   1.00 29.60 ? 229 ARG   A CB  1 
ATOM   1568 C CG  . ARG   A 1 250 ? -6.890  -23.443 6.651   1.00 35.32 ? 229 ARG   A CG  1 
ATOM   1569 C CD  . ARG   A 1 250 ? -7.321  -22.994 8.023   1.00 38.33 ? 229 ARG   A CD  1 
ATOM   1570 N NE  . ARG   A 1 250 ? -8.740  -22.604 8.083   1.00 41.76 ? 229 ARG   A NE  1 
ATOM   1571 C CZ  . ARG   A 1 250 ? -9.320  -22.028 9.147   1.00 44.99 ? 229 ARG   A CZ  1 
ATOM   1572 N NH1 . ARG   A 1 250 ? -8.617  -21.761 10.236  1.00 43.62 ? 229 ARG   A NH1 1 
ATOM   1573 N NH2 . ARG   A 1 250 ? -10.600 -21.697 9.122   1.00 44.35 ? 229 ARG   A NH2 1 
ATOM   1574 N N   . ARG   A 1 251 ? -2.653  -20.997 5.746   1.00 23.72 ? 230 ARG   A N   1 
ATOM   1575 C CA  A ARG   A 1 251 ? -1.237  -20.994 5.432   0.50 25.17 ? 230 ARG   A CA  1 
ATOM   1576 C CA  B ARG   A 1 251 ? -1.244  -20.984 5.406   0.50 25.45 ? 230 ARG   A CA  1 
ATOM   1577 C C   . ARG   A 1 251 ? -0.663  -19.662 5.894   1.00 25.09 ? 230 ARG   A C   1 
ATOM   1578 O O   . ARG   A 1 251 ? -1.404  -18.680 6.022   1.00 24.92 ? 230 ARG   A O   1 
ATOM   1579 C CB  A ARG   A 1 251 ? -1.016  -21.205 3.926   0.50 28.25 ? 230 ARG   A CB  1 
ATOM   1580 C CB  B ARG   A 1 251 ? -1.036  -21.251 3.904   0.50 29.03 ? 230 ARG   A CB  1 
ATOM   1581 C CG  A ARG   A 1 251 ? 0.412   -21.477 3.468   0.50 28.73 ? 230 ARG   A CG  1 
ATOM   1582 C CG  B ARG   A 1 251 ? -1.677  -20.338 2.865   0.50 30.58 ? 230 ARG   A CG  1 
ATOM   1583 C CD  A ARG   A 1 251 ? 0.891   -22.906 3.790   0.50 33.27 ? 230 ARG   A CD  1 
ATOM   1584 C CD  B ARG   A 1 251 ? -1.416  -20.766 1.408   0.50 33.95 ? 230 ARG   A CD  1 
ATOM   1585 N NE  A ARG   A 1 251 ? 2.237   -23.179 3.269   0.50 28.35 ? 230 ARG   A NE  1 
ATOM   1586 N NE  B ARG   A 1 251 ? 0.025   -20.956 1.205   0.50 37.98 ? 230 ARG   A NE  1 
ATOM   1587 C CZ  A ARG   A 1 251 ? 2.868   -24.329 3.356   0.50 36.22 ? 230 ARG   A CZ  1 
ATOM   1588 C CZ  B ARG   A 1 251 ? 0.702   -21.547 0.209   0.50 40.37 ? 230 ARG   A CZ  1 
ATOM   1589 N NH1 A ARG   A 1 251 ? 4.017   -24.495 2.718   0.50 38.75 ? 230 ARG   A NH1 1 
ATOM   1590 N NH1 B ARG   A 1 251 ? 0.082   -22.027 -0.852  0.50 36.66 ? 230 ARG   A NH1 1 
ATOM   1591 N NH2 A ARG   A 1 251 ? 2.337   -25.327 4.043   0.50 34.45 ? 230 ARG   A NH2 1 
ATOM   1592 N NH2 B ARG   A 1 251 ? 2.021   -21.644 0.286   0.50 35.89 ? 230 ARG   A NH2 1 
ATOM   1593 N N   . GLU   A 1 252 ? 0.651   -19.663 6.140   1.00 23.54 ? 231 GLU   A N   1 
ATOM   1594 C CA  . GLU   A 1 252 ? 1.412   -18.479 6.524   1.00 24.82 ? 231 GLU   A CA  1 
ATOM   1595 C C   . GLU   A 1 252 ? 1.550   -17.582 5.299   1.00 26.18 ? 231 GLU   A C   1 
ATOM   1596 O O   . GLU   A 1 252 ? 1.512   -18.058 4.173   1.00 23.91 ? 231 GLU   A O   1 
ATOM   1597 C CB  . GLU   A 1 252 ? 2.766   -18.853 7.147   1.00 26.44 ? 231 GLU   A CB  1 
ATOM   1598 C CG  . GLU   A 1 252 ? 3.826   -19.368 6.163   1.00 26.33 ? 231 GLU   A CG  1 
ATOM   1599 C CD  . GLU   A 1 252 ? 3.785   -20.860 5.847   1.00 35.08 ? 231 GLU   A CD  1 
ATOM   1600 O OE1 . GLU   A 1 252 ? 4.876   -21.487 5.668   1.00 34.33 ? 231 GLU   A OE1 1 
ATOM   1601 O OE2 . GLU   A 1 252 ? 2.662   -21.411 5.827   1.00 27.83 ? 231 GLU   A OE2 1 
ATOM   1602 N N   . ALA   A 1 253 ? 1.758   -16.280 5.515   1.00 26.01 ? 232 ALA   A N   1 
ATOM   1603 C CA  . ALA   A 1 253 ? 2.097   -15.373 4.428   1.00 25.99 ? 232 ALA   A CA  1 
ATOM   1604 C C   . ALA   A 1 253 ? 3.501   -15.702 3.898   1.00 24.21 ? 232 ALA   A C   1 
ATOM   1605 O O   . ALA   A 1 253 ? 4.416   -16.007 4.668   1.00 25.26 ? 232 ALA   A O   1 
ATOM   1606 C CB  . ALA   A 1 253 ? 2.133   -13.979 5.004   1.00 23.83 ? 232 ALA   A CB  1 
ATOM   1607 N N   . SER   A 1 254 ? 3.681   -15.588 2.583   1.00 24.11 ? 233 SER   A N   1 
ATOM   1608 C CA  . SER   A 1 254 ? 5.012   -15.628 1.992   1.00 24.73 ? 233 SER   A CA  1 
ATOM   1609 C C   . SER   A 1 254 ? 5.725   -14.336 2.340   1.00 25.08 ? 233 SER   A C   1 
ATOM   1610 O O   . SER   A 1 254 ? 5.081   -13.321 2.610   1.00 25.54 ? 233 SER   A O   1 
ATOM   1611 C CB  . SER   A 1 254 ? 4.944   -15.849 0.478   1.00 23.44 ? 233 SER   A CB  1 
ATOM   1612 O OG  . SER   A 1 254 ? 4.432   -14.694 -0.169  1.00 28.91 ? 233 SER   A OG  1 
ATOM   1613 N N   . ALA   A 1 255 ? 7.055   -14.392 2.354   1.00 25.22 ? 234 ALA   A N   1 
ATOM   1614 C CA  . ALA   A 1 255 ? 7.834   -13.175 2.548   1.00 25.67 ? 234 ALA   A CA  1 
ATOM   1615 C C   . ALA   A 1 255 ? 7.441   -12.132 1.509   1.00 23.19 ? 234 ALA   A C   1 
ATOM   1616 O O   . ALA   A 1 255 ? 7.427   -10.915 1.792   1.00 22.98 ? 234 ALA   A O   1 
ATOM   1617 C CB  . ALA   A 1 255 ? 9.323   -13.490 2.496   1.00 25.77 ? 234 ALA   A CB  1 
ATOM   1618 N N   . GLU   A 1 256 ? 7.175   -12.616 0.284   1.00 22.96 ? 235 GLU   A N   1 
ATOM   1619 C CA  . GLU   A 1 256 ? 6.877   -11.727 -0.828  1.00 23.59 ? 235 GLU   A CA  1 
ATOM   1620 C C   . GLU   A 1 256 ? 5.556   -10.983 -0.589  1.00 21.30 ? 235 GLU   A C   1 
ATOM   1621 O O   . GLU   A 1 256 ? 5.424   -9.790  -0.895  1.00 21.94 ? 235 GLU   A O   1 
ATOM   1622 C CB  . GLU   A 1 256 ? 6.849   -12.549 -2.123  1.00 28.77 ? 235 GLU   A CB  1 
ATOM   1623 C CG  . GLU   A 1 256 ? 6.646   -11.652 -3.338  1.00 41.44 ? 235 GLU   A CG  1 
ATOM   1624 C CD  . GLU   A 1 256 ? 6.641   -12.356 -4.691  1.00 53.42 ? 235 GLU   A CD  1 
ATOM   1625 O OE1 . GLU   A 1 256 ? 5.951   -11.825 -5.566  1.00 58.00 ? 235 GLU   A OE1 1 
ATOM   1626 O OE2 . GLU   A 1 256 ? 7.325   -13.392 -4.896  1.00 68.55 ? 235 GLU   A OE2 1 
ATOM   1627 N N   . GLN   A 1 257 ? 4.579   -11.668 0.003   1.00 22.09 ? 236 GLN   A N   1 
ATOM   1628 C CA  . GLN   A 1 257 ? 3.313   -11.013 0.331   1.00 22.38 ? 236 GLN   A CA  1 
ATOM   1629 C C   . GLN   A 1 257 ? 3.506   -9.875  1.344   1.00 21.72 ? 236 GLN   A C   1 
ATOM   1630 O O   . GLN   A 1 257 ? 2.846   -8.832  1.268   1.00 21.80 ? 236 GLN   A O   1 
ATOM   1631 C CB  . GLN   A 1 257 ? 2.348   -12.091 0.809   1.00 22.95 ? 236 GLN   A CB  1 
ATOM   1632 C CG  . GLN   A 1 257 ? 1.828   -12.955 -0.337  1.00 23.19 ? 236 GLN   A CG  1 
ATOM   1633 C CD  . GLN   A 1 257 ? 0.968   -14.112 0.119   1.00 25.26 ? 236 GLN   A CD  1 
ATOM   1634 O OE1 . GLN   A 1 257 ? 1.186   -14.736 1.162   1.00 27.00 ? 236 GLN   A OE1 1 
ATOM   1635 N NE2 . GLN   A 1 257 ? -0.021  -14.455 -0.693  1.00 28.28 ? 236 GLN   A NE2 1 
ATOM   1636 N N   . ILE   A 1 258 ? 4.379   -10.097 2.337   1.00 21.21 ? 237 ILE   A N   1 
ATOM   1637 C CA  . ILE   A 1 258 ? 4.704   -9.040  3.295   1.00 20.31 ? 237 ILE   A CA  1 
ATOM   1638 C C   . ILE   A 1 258 ? 5.360   -7.895  2.532   1.00 20.33 ? 237 ILE   A C   1 
ATOM   1639 O O   . ILE   A 1 258 ? 5.031   -6.710  2.737   1.00 21.35 ? 237 ILE   A O   1 
ATOM   1640 C CB  . ILE   A 1 258 ? 5.573   -9.587  4.455   1.00 21.08 ? 237 ILE   A CB  1 
ATOM   1641 C CG1 . ILE   A 1 258 ? 4.910   -10.784 5.215   1.00 22.37 ? 237 ILE   A CG1 1 
ATOM   1642 C CG2 . ILE   A 1 258 ? 5.989   -8.462  5.415   1.00 23.70 ? 237 ILE   A CG2 1 
ATOM   1643 C CD1 . ILE   A 1 258 ? 3.474   -10.515 5.673   1.00 20.99 ? 237 ILE   A CD1 1 
ATOM   1644 N N   . ALA   A 1 259 ? 6.357   -8.250  1.694   1.00 19.79 ? 238 ALA   A N   1 
ATOM   1645 C CA  . ALA   A 1 259 ? 7.096   -7.251  0.940   1.00 23.11 ? 238 ALA   A CA  1 
ATOM   1646 C C   . ALA   A 1 259 ? 6.156   -6.449  0.045   1.00 22.09 ? 238 ALA   A C   1 
ATOM   1647 O O   . ALA   A 1 259 ? 6.355   -5.236  -0.138  1.00 22.05 ? 238 ALA   A O   1 
ATOM   1648 C CB  . ALA   A 1 259 ? 8.220   -7.915  0.124   1.00 24.10 ? 238 ALA   A CB  1 
ATOM   1649 N N   . ASP   A 1 260 ? 5.147   -7.136  -0.524  1.00 21.14 ? 239 ASP   A N   1 
ATOM   1650 C CA  . ASP   A 1 260 ? 4.161   -6.436  -1.358  1.00 24.09 ? 239 ASP   A CA  1 
ATOM   1651 C C   . ASP   A 1 260 ? 3.503   -5.267  -0.621  1.00 23.51 ? 239 ASP   A C   1 
ATOM   1652 O O   . ASP   A 1 260 ? 3.261   -4.208  -1.215  1.00 23.78 ? 239 ASP   A O   1 
ATOM   1653 C CB  . ASP   A 1 260 ? 3.023   -7.340  -1.825  1.00 22.68 ? 239 ASP   A CB  1 
ATOM   1654 C CG  . ASP   A 1 260 ? 3.353   -8.241  -3.007  1.00 29.08 ? 239 ASP   A CG  1 
ATOM   1655 O OD1 . ASP   A 1 260 ? 4.265   -7.873  -3.778  1.00 28.49 ? 239 ASP   A OD1 1 
ATOM   1656 O OD2 . ASP   A 1 260 ? 2.717   -9.318  -3.112  1.00 30.66 ? 239 ASP   A OD2 1 
ATOM   1657 N N   . ALA   A 1 261 ? 3.215   -5.435  0.681   1.00 20.92 ? 240 ALA   A N   1 
ATOM   1658 C CA  . ALA   A 1 261 ? 2.559   -4.337  1.376   1.00 22.08 ? 240 ALA   A CA  1 
ATOM   1659 C C   . ALA   A 1 261 ? 3.543   -3.207  1.654   1.00 22.15 ? 240 ALA   A C   1 
ATOM   1660 O O   . ALA   A 1 261 ? 3.150   -2.040  1.645   1.00 19.88 ? 240 ALA   A O   1 
ATOM   1661 C CB  . ALA   A 1 261 ? 1.890   -4.843  2.653   1.00 21.34 ? 240 ALA   A CB  1 
ATOM   1662 N N   . VAL   A 1 262 ? 4.818   -3.560  1.891   1.00 23.21 ? 241 VAL   A N   1 
ATOM   1663 C CA  . VAL   A 1 262 ? 5.881   -2.575  2.094   1.00 23.10 ? 241 VAL   A CA  1 
ATOM   1664 C C   . VAL   A 1 262 ? 6.003   -1.715  0.830   1.00 24.70 ? 241 VAL   A C   1 
ATOM   1665 O O   . VAL   A 1 262 ? 6.121   -0.480  0.883   1.00 22.55 ? 241 VAL   A O   1 
ATOM   1666 C CB  . VAL   A 1 262 ? 7.218   -3.250  2.500   1.00 23.39 ? 241 VAL   A CB  1 
ATOM   1667 C CG1 . VAL   A 1 262 ? 8.326   -2.222  2.725   1.00 22.84 ? 241 VAL   A CG1 1 
ATOM   1668 C CG2 . VAL   A 1 262 ? 7.078   -4.079  3.792   1.00 21.93 ? 241 VAL   A CG2 1 
ATOM   1669 N N   . ILE   A 1 263 ? 6.015   -2.396  -0.321  1.00 25.08 ? 242 ILE   A N   1 
ATOM   1670 C CA  . ILE   A 1 263 ? 6.202   -1.737  -1.611  1.00 24.85 ? 242 ILE   A CA  1 
ATOM   1671 C C   . ILE   A 1 263 ? 5.057   -0.766  -1.874  1.00 23.41 ? 242 ILE   A C   1 
ATOM   1672 O O   . ILE   A 1 263 ? 5.299   0.329   -2.381  1.00 22.43 ? 242 ILE   A O   1 
ATOM   1673 C CB  . ILE   A 1 263 ? 6.302   -2.780  -2.735  1.00 32.78 ? 242 ILE   A CB  1 
ATOM   1674 C CG1 . ILE   A 1 263 ? 7.623   -3.528  -2.656  1.00 41.68 ? 242 ILE   A CG1 1 
ATOM   1675 C CG2 . ILE   A 1 263 ? 6.070   -2.162  -4.114  1.00 33.41 ? 242 ILE   A CG2 1 
ATOM   1676 C CD1 . ILE   A 1 263 ? 8.852   -2.638  -2.638  1.00 44.23 ? 242 ILE   A CD1 1 
ATOM   1677 N N   . PHE   A 1 264 ? 3.825   -1.196  -1.543  1.00 21.51 ? 243 PHE   A N   1 
ATOM   1678 C CA  . PHE   A 1 264 ? 2.690   -0.305  -1.658  1.00 24.07 ? 243 PHE   A CA  1 
ATOM   1679 C C   . PHE   A 1 264 ? 2.955   0.987   -0.883  1.00 22.23 ? 243 PHE   A C   1 
ATOM   1680 O O   . PHE   A 1 264 ? 2.779   2.085   -1.407  1.00 22.09 ? 243 PHE   A O   1 
ATOM   1681 C CB  . PHE   A 1 264 ? 1.376   -1.014  -1.282  1.00 22.72 ? 243 PHE   A CB  1 
ATOM   1682 C CG  . PHE   A 1 264 ? 0.241   -0.000  -1.137  1.00 23.49 ? 243 PHE   A CG  1 
ATOM   1683 C CD1 . PHE   A 1 264 ? -0.304  0.640   -2.253  1.00 22.73 ? 243 PHE   A CD1 1 
ATOM   1684 C CD2 . PHE   A 1 264 ? -0.266  0.328   0.124   1.00 25.01 ? 243 PHE   A CD2 1 
ATOM   1685 C CE1 . PHE   A 1 264 ? -1.334  1.575   -2.106  1.00 24.07 ? 243 PHE   A CE1 1 
ATOM   1686 C CE2 . PHE   A 1 264 ? -1.316  1.239   0.246   1.00 23.54 ? 243 PHE   A CE2 1 
ATOM   1687 C CZ  . PHE   A 1 264 ? -1.849  1.858   -0.864  1.00 22.09 ? 243 PHE   A CZ  1 
ATOM   1688 N N   . LEU   A 1 265 ? 3.311   0.862   0.408   1.00 20.46 ? 244 LEU   A N   1 
ATOM   1689 C CA  . LEU   A 1 265 ? 3.435   2.021   1.275   1.00 21.31 ? 244 LEU   A CA  1 
ATOM   1690 C C   . LEU   A 1 265 ? 4.541   2.963   0.795   1.00 23.24 ? 244 LEU   A C   1 
ATOM   1691 O O   . LEU   A 1 265 ? 4.467   4.166   1.032   1.00 23.65 ? 244 LEU   A O   1 
ATOM   1692 C CB  . LEU   A 1 265 ? 3.630   1.652   2.759   1.00 21.07 ? 244 LEU   A CB  1 
ATOM   1693 C CG  . LEU   A 1 265 ? 2.390   1.020   3.428   1.00 20.79 ? 244 LEU   A CG  1 
ATOM   1694 C CD1 . LEU   A 1 265 ? 2.767   0.241   4.677   1.00 19.51 ? 244 LEU   A CD1 1 
ATOM   1695 C CD2 . LEU   A 1 265 ? 1.341   2.086   3.772   1.00 20.81 ? 244 LEU   A CD2 1 
ATOM   1696 N N   . VAL   A 1 266 ? 5.587   2.422   0.167   1.00 23.97 ? 245 VAL   A N   1 
ATOM   1697 C CA  . VAL   A 1 266 ? 6.661   3.310   -0.275  1.00 23.07 ? 245 VAL   A CA  1 
ATOM   1698 C C   . VAL   A 1 266 ? 6.319   3.977   -1.611  1.00 27.74 ? 245 VAL   A C   1 
ATOM   1699 O O   . VAL   A 1 266 ? 6.889   5.028   -1.932  1.00 26.73 ? 245 VAL   A O   1 
ATOM   1700 C CB  . VAL   A 1 266 ? 8.074   2.681   -0.255  1.00 26.03 ? 245 VAL   A CB  1 
ATOM   1701 C CG1 . VAL   A 1 266 ? 8.471   2.140   1.130   1.00 24.13 ? 245 VAL   A CG1 1 
ATOM   1702 C CG2 . VAL   A 1 266 ? 8.269   1.583   -1.282  1.00 28.91 ? 245 VAL   A CG2 1 
ATOM   1703 N N   . SER   A 1 267 ? 5.373   3.384   -2.364  1.00 25.71 ? 246 SER   A N   1 
ATOM   1704 C CA  . SER   A 1 267 ? 5.018   3.815   -3.719  1.00 27.06 ? 246 SER   A CA  1 
ATOM   1705 C C   . SER   A 1 267 ? 4.224   5.140   -3.738  1.00 28.70 ? 246 SER   A C   1 
ATOM   1706 O O   . SER   A 1 267 ? 3.661   5.573   -2.713  1.00 24.97 ? 246 SER   A O   1 
ATOM   1707 C CB  . SER   A 1 267 ? 4.217   2.712   -4.384  1.00 23.66 ? 246 SER   A CB  1 
ATOM   1708 O OG  . SER   A 1 267 ? 2.844   2.846   -4.007  1.00 24.93 ? 246 SER   A OG  1 
ATOM   1709 N N   . GLY   A 1 268 ? 4.114   5.741   -4.948  1.00 27.91 ? 247 GLY   A N   1 
ATOM   1710 C CA  . GLY   A 1 268 ? 3.251   6.884   -5.253  1.00 27.52 ? 247 GLY   A CA  1 
ATOM   1711 C C   . GLY   A 1 268 ? 1.759   6.621   -4.996  1.00 27.43 ? 247 GLY   A C   1 
ATOM   1712 O O   . GLY   A 1 268 ? 0.974   7.560   -4.869  1.00 31.05 ? 247 GLY   A O   1 
ATOM   1713 N N   . SER   A 1 269 ? 1.357   5.344   -4.871  1.00 22.80 ? 248 SER   A N   1 
ATOM   1714 C CA  . SER   A 1 269 ? -0.045  5.014   -4.689  1.00 23.64 ? 248 SER   A CA  1 
ATOM   1715 C C   . SER   A 1 269 ? -0.433  5.196   -3.222  1.00 24.32 ? 248 SER   A C   1 
ATOM   1716 O O   . SER   A 1 269 ? -1.601  5.017   -2.889  1.00 25.07 ? 248 SER   A O   1 
ATOM   1717 C CB  . SER   A 1 269 ? -0.324  3.564   -5.102  1.00 27.43 ? 248 SER   A CB  1 
ATOM   1718 O OG  . SER   A 1 269 ? -0.139  3.361   -6.496  1.00 36.53 ? 248 SER   A OG  1 
ATOM   1719 N N   . ALA   A 1 270 ? 0.553   5.522   -2.363  1.00 21.73 ? 249 ALA   A N   1 
ATOM   1720 C CA  . ALA   A 1 270 ? 0.342   5.706   -0.930  1.00 23.13 ? 249 ALA   A CA  1 
ATOM   1721 C C   . ALA   A 1 270 ? 0.799   7.080   -0.452  1.00 24.78 ? 249 ALA   A C   1 
ATOM   1722 O O   . ALA   A 1 270 ? 1.017   7.279   0.744   1.00 23.17 ? 249 ALA   A O   1 
ATOM   1723 C CB  . ALA   A 1 270 ? 1.019   4.606   -0.156  1.00 24.47 ? 249 ALA   A CB  1 
ATOM   1724 N N   . GLN   A 1 271 ? 0.791   8.067   -1.362  1.00 25.84 ? 250 GLN   A N   1 
ATOM   1725 C CA  . GLN   A 1 271 ? 1.360   9.382   -1.091  1.00 25.24 ? 250 GLN   A CA  1 
ATOM   1726 C C   . GLN   A 1 271 ? 0.565   10.156  -0.038  1.00 25.82 ? 250 GLN   A C   1 
ATOM   1727 O O   . GLN   A 1 271 ? 1.072   11.151  0.467   1.00 22.90 ? 250 GLN   A O   1 
ATOM   1728 C CB  . GLN   A 1 271 ? 1.520   10.218  -2.372  1.00 33.60 ? 250 GLN   A CB  1 
ATOM   1729 C CG  . GLN   A 1 271 ? 0.182   10.595  -3.006  0.70 40.20 ? 250 GLN   A CG  1 
ATOM   1730 C CD  . GLN   A 1 271 ? 0.219   11.156  -4.419  0.70 39.84 ? 250 GLN   A CD  1 
ATOM   1731 O OE1 . GLN   A 1 271 ? -0.835  11.362  -5.033  0.70 33.98 ? 250 GLN   A OE1 1 
ATOM   1732 N NE2 . GLN   A 1 271 ? 1.409   11.378  -4.960  0.70 33.83 ? 250 GLN   A NE2 1 
ATOM   1733 N N   . TYR   A 1 272 ? -0.680  9.754   0.262   1.00 22.81 ? 251 TYR   A N   1 
ATOM   1734 C CA  . TYR   A 1 272 ? -1.452  10.446  1.283   1.00 23.27 ? 251 TYR   A CA  1 
ATOM   1735 C C   . TYR   A 1 272 ? -1.458  9.601   2.567   1.00 22.61 ? 251 TYR   A C   1 
ATOM   1736 O O   . TYR   A 1 272 ? -2.084  9.970   3.533   1.00 25.07 ? 251 TYR   A O   1 
ATOM   1737 C CB  . TYR   A 1 272 ? -2.888  10.812  0.867   1.00 21.51 ? 251 TYR   A CB  1 
ATOM   1738 C CG  . TYR   A 1 272 ? -3.612  11.888  1.658   1.00 21.39 ? 251 TYR   A CG  1 
ATOM   1739 C CD1 . TYR   A 1 272 ? -3.233  13.224  1.549   1.00 22.31 ? 251 TYR   A CD1 1 
ATOM   1740 C CD2 . TYR   A 1 272 ? -4.712  11.594  2.468   1.00 21.80 ? 251 TYR   A CD2 1 
ATOM   1741 C CE1 . TYR   A 1 272 ? -3.890  14.217  2.252   1.00 21.09 ? 251 TYR   A CE1 1 
ATOM   1742 C CE2 . TYR   A 1 272 ? -5.415  12.594  3.132   1.00 19.96 ? 251 TYR   A CE2 1 
ATOM   1743 C CZ  . TYR   A 1 272 ? -4.993  13.904  3.036   1.00 22.60 ? 251 TYR   A CZ  1 
ATOM   1744 O OH  . TYR   A 1 272 ? -5.662  14.872  3.725   1.00 20.63 ? 251 TYR   A OH  1 
ATOM   1745 N N   . ILE   A 1 273 ? -0.839  8.423   2.570   1.00 20.15 ? 252 ILE   A N   1 
ATOM   1746 C CA  . ILE   A 1 273 ? -0.996  7.535   3.719   1.00 19.91 ? 252 ILE   A CA  1 
ATOM   1747 C C   . ILE   A 1 273 ? 0.174   7.762   4.684   1.00 21.13 ? 252 ILE   A C   1 
ATOM   1748 O O   . ILE   A 1 273 ? 1.344   7.622   4.288   1.00 19.00 ? 252 ILE   A O   1 
ATOM   1749 C CB  . ILE   A 1 273 ? -0.984  6.077   3.225   1.00 19.95 ? 252 ILE   A CB  1 
ATOM   1750 C CG1 . ILE   A 1 273 ? -2.152  5.797   2.201   1.00 20.08 ? 252 ILE   A CG1 1 
ATOM   1751 C CG2 . ILE   A 1 273 ? -0.986  5.112   4.418   1.00 17.91 ? 252 ILE   A CG2 1 
ATOM   1752 C CD1 . ILE   A 1 273 ? -2.250  4.341   1.739   1.00 21.47 ? 252 ILE   A CD1 1 
ATOM   1753 N N   . THR   A 1 274 ? -0.130  8.104   5.944   1.00 20.92 ? 253 THR   A N   1 
ATOM   1754 C CA  . THR   A 1 274 ? 0.908   8.172   6.976   1.00 20.59 ? 253 THR   A CA  1 
ATOM   1755 C C   . THR   A 1 274 ? 0.237   7.918   8.325   1.00 19.00 ? 253 THR   A C   1 
ATOM   1756 O O   . THR   A 1 274 ? -0.923  8.286   8.535   1.00 19.97 ? 253 THR   A O   1 
ATOM   1757 C CB  . THR   A 1 274 ? 1.697   9.490   6.958   1.00 21.37 ? 253 THR   A CB  1 
ATOM   1758 O OG1 . THR   A 1 274 ? 2.885   9.369   7.747   1.00 21.58 ? 253 THR   A OG1 1 
ATOM   1759 C CG2 . THR   A 1 274 ? 0.847   10.689  7.354   1.00 18.79 ? 253 THR   A CG2 1 
ATOM   1760 N N   . GLY   A 1 275 ? 0.975   7.222   9.186   1.00 20.77 ? 254 GLY   A N   1 
ATOM   1761 C CA  . GLY   A 1 275 ? 0.488   6.811   10.483  1.00 20.32 ? 254 GLY   A CA  1 
ATOM   1762 C C   . GLY   A 1 275 ? -0.415  5.586   10.397  1.00 22.28 ? 254 GLY   A C   1 
ATOM   1763 O O   . GLY   A 1 275 ? -1.147  5.329   11.348  1.00 22.22 ? 254 GLY   A O   1 
ATOM   1764 N N   . SER   A 1 276 ? -0.373  4.868   9.260   1.00 20.64 ? 255 SER   A N   1 
ATOM   1765 C CA  . SER   A 1 276 ? -1.214  3.704   9.067   1.00 20.45 ? 255 SER   A CA  1 
ATOM   1766 C C   . SER   A 1 276 ? -0.406  2.428   9.262   1.00 21.66 ? 255 SER   A C   1 
ATOM   1767 O O   . SER   A 1 276 ? 0.749   2.358   8.863   1.00 22.92 ? 255 SER   A O   1 
ATOM   1768 C CB  . SER   A 1 276 ? -1.875  3.687   7.701   1.00 22.25 ? 255 SER   A CB  1 
ATOM   1769 O OG  . SER   A 1 276 ? -2.575  4.911   7.531   1.00 28.63 ? 255 SER   A OG  1 
ATOM   1770 N N   . ILE   A 1 277 ? -1.068  1.417   9.837   1.00 19.72 ? 256 ILE   A N   1 
ATOM   1771 C CA  . ILE   A 1 277 ? -0.448  0.112   9.934   1.00 20.96 ? 256 ILE   A CA  1 
ATOM   1772 C C   . ILE   A 1 277 ? -1.370  -0.857  9.223   1.00 21.83 ? 256 ILE   A C   1 
ATOM   1773 O O   . ILE   A 1 277 ? -2.539  -0.981  9.619   1.00 23.60 ? 256 ILE   A O   1 
ATOM   1774 C CB  . ILE   A 1 277 ? -0.238  -0.258  11.410  1.00 22.06 ? 256 ILE   A CB  1 
ATOM   1775 C CG1 . ILE   A 1 277 ? 0.743   0.767   12.050  1.00 24.30 ? 256 ILE   A CG1 1 
ATOM   1776 C CG2 . ILE   A 1 277 ? 0.236   -1.716  11.517  1.00 22.85 ? 256 ILE   A CG2 1 
ATOM   1777 C CD1 . ILE   A 1 277 ? 0.934   0.633   13.552  1.00 29.87 ? 256 ILE   A CD1 1 
ATOM   1778 N N   . ILE   A 1 278 ? -0.825  -1.520  8.193   1.00 20.52 ? 257 ILE   A N   1 
ATOM   1779 C CA  . ILE   A 1 278 ? -1.592  -2.465  7.405   1.00 21.20 ? 257 ILE   A CA  1 
ATOM   1780 C C   . ILE   A 1 278 ? -1.298  -3.860  7.921   1.00 21.52 ? 257 ILE   A C   1 
ATOM   1781 O O   . ILE   A 1 278 ? -0.162  -4.350  7.787   1.00 19.34 ? 257 ILE   A O   1 
ATOM   1782 C CB  . ILE   A 1 278 ? -1.215  -2.377  5.912   1.00 21.09 ? 257 ILE   A CB  1 
ATOM   1783 C CG1 . ILE   A 1 278 ? -1.387  -0.941  5.356   1.00 19.41 ? 257 ILE   A CG1 1 
ATOM   1784 C CG2 . ILE   A 1 278 ? -1.957  -3.432  5.062   1.00 19.81 ? 257 ILE   A CG2 1 
ATOM   1785 C CD1 . ILE   A 1 278 ? -0.964  -0.825  3.900   1.00 21.80 ? 257 ILE   A CD1 1 
ATOM   1786 N N   . LYS   A 1 279 ? -2.354  -4.504  8.423   1.00 19.37 ? 258 LYS   A N   1 
ATOM   1787 C CA  . LYS   A 1 279 ? -2.266  -5.898  8.793   1.00 21.12 ? 258 LYS   A CA  1 
ATOM   1788 C C   . LYS   A 1 279 ? -2.198  -6.737  7.529   1.00 20.76 ? 258 LYS   A C   1 
ATOM   1789 O O   . LYS   A 1 279 ? -2.957  -6.509  6.593   1.00 24.03 ? 258 LYS   A O   1 
ATOM   1790 C CB  . LYS   A 1 279 ? -3.486  -6.493  9.518   1.00 20.71 ? 258 LYS   A CB  1 
ATOM   1791 C CG  . LYS   A 1 279 ? -3.674  -6.065  10.947  1.00 24.27 ? 258 LYS   A CG  1 
ATOM   1792 C CD  . LYS   A 1 279 ? -4.959  -6.632  11.579  1.00 24.59 ? 258 LYS   A CD  1 
ATOM   1793 C CE  . LYS   A 1 279 ? -6.263  -6.388  10.848  1.00 26.21 ? 258 LYS   A CE  1 
ATOM   1794 N NZ  . LYS   A 1 279 ? -7.418  -7.074  11.456  1.00 24.28 ? 258 LYS   A NZ  1 
ATOM   1795 N N   . VAL   A 1 280 ? -1.303  -7.737  7.535   1.00 21.91 ? 259 VAL   A N   1 
ATOM   1796 C CA  . VAL   A 1 280 ? -1.160  -8.672  6.428   1.00 21.02 ? 259 VAL   A CA  1 
ATOM   1797 C C   . VAL   A 1 280 ? -1.169  -10.041 7.091   1.00 20.45 ? 259 VAL   A C   1 
ATOM   1798 O O   . VAL   A 1 280 ? -0.133  -10.663 7.258   1.00 21.62 ? 259 VAL   A O   1 
ATOM   1799 C CB  . VAL   A 1 280 ? 0.127   -8.436  5.599   1.00 20.59 ? 259 VAL   A CB  1 
ATOM   1800 C CG1 . VAL   A 1 280 ? 0.240   -9.405  4.416   1.00 20.92 ? 259 VAL   A CG1 1 
ATOM   1801 C CG2 . VAL   A 1 280 ? 0.193   -6.990  5.090   1.00 21.89 ? 259 VAL   A CG2 1 
ATOM   1802 N N   . ASP   A 1 281 ? -2.357  -10.473 7.510   1.00 21.16 ? 260 ASP   A N   1 
ATOM   1803 C CA  . ASP   A 1 281 ? -2.434  -11.562 8.467   1.00 21.76 ? 260 ASP   A CA  1 
ATOM   1804 C C   . ASP   A 1 281 ? -3.454  -12.629 8.051   1.00 20.28 ? 260 ASP   A C   1 
ATOM   1805 O O   . ASP   A 1 281 ? -3.695  -13.573 8.803   1.00 19.05 ? 260 ASP   A O   1 
ATOM   1806 C CB  . ASP   A 1 281 ? -2.654  -10.967 9.859   1.00 21.28 ? 260 ASP   A CB  1 
ATOM   1807 C CG  . ASP   A 1 281 ? -4.105  -10.627 10.194  1.00 21.42 ? 260 ASP   A CG  1 
ATOM   1808 O OD1 . ASP   A 1 281 ? -4.908  -10.444 9.256   1.00 21.94 ? 260 ASP   A OD1 1 
ATOM   1809 O OD2 . ASP   A 1 281 ? -4.435  -10.584 11.390  1.00 21.96 ? 260 ASP   A OD2 1 
ATOM   1810 N N   . GLY   A 1 282 ? -4.054  -12.517 6.858   1.00 19.85 ? 261 GLY   A N   1 
ATOM   1811 C CA  . GLY   A 1 282 ? -4.969  -13.579 6.419   1.00 19.17 ? 261 GLY   A CA  1 
ATOM   1812 C C   . GLY   A 1 282 ? -6.165  -13.768 7.351   1.00 19.30 ? 261 GLY   A C   1 
ATOM   1813 O O   . GLY   A 1 282 ? -6.801  -14.828 7.347   1.00 20.10 ? 261 GLY   A O   1 
ATOM   1814 N N   . GLY   A 1 283 ? -6.496  -12.739 8.137   1.00 17.87 ? 262 GLY   A N   1 
ATOM   1815 C CA  . GLY   A 1 283 ? -7.643  -12.846 9.051   1.00 18.84 ? 262 GLY   A CA  1 
ATOM   1816 C C   . GLY   A 1 283 ? -7.278  -13.353 10.457  1.00 20.71 ? 262 GLY   A C   1 
ATOM   1817 O O   . GLY   A 1 283 ? -8.168  -13.479 11.312  1.00 20.17 ? 262 GLY   A O   1 
ATOM   1818 N N   . LEU   A 1 284 ? -5.990  -13.677 10.700  1.00 19.96 ? 263 LEU   A N   1 
ATOM   1819 C CA  . LEU   A 1 284 ? -5.574  -14.368 11.932  1.00 20.91 ? 263 LEU   A CA  1 
ATOM   1820 C C   . LEU   A 1 284 ? -6.004  -13.593 13.192  1.00 19.87 ? 263 LEU   A C   1 
ATOM   1821 O O   . LEU   A 1 284 ? -6.561  -14.166 14.139  1.00 20.90 ? 263 LEU   A O   1 
ATOM   1822 C CB  . LEU   A 1 284 ? -4.067  -14.644 11.964  1.00 20.54 ? 263 LEU   A CB  1 
ATOM   1823 C CG  . LEU   A 1 284 ? -3.507  -15.355 13.208  1.00 22.04 ? 263 LEU   A CG  1 
ATOM   1824 C CD1 . LEU   A 1 284 ? -4.038  -16.806 13.375  1.00 22.09 ? 263 LEU   A CD1 1 
ATOM   1825 C CD2 . LEU   A 1 284 ? -1.996  -15.336 13.165  1.00 25.78 ? 263 LEU   A CD2 1 
ATOM   1826 N N   . SER   A 1 285 ? -5.775  -12.275 13.203  1.00 20.37 ? 264 SER   A N   1 
ATOM   1827 C CA  . SER   A 1 285 ? -6.098  -11.503 14.403  1.00 21.06 ? 264 SER   A CA  1 
ATOM   1828 C C   . SER   A 1 285 ? -7.612  -11.456 14.673  1.00 20.83 ? 264 SER   A C   1 
ATOM   1829 O O   . SER   A 1 285 ? -8.045  -11.027 15.743  1.00 21.27 ? 264 SER   A O   1 
ATOM   1830 C CB  . SER   A 1 285 ? -5.534  -10.089 14.288  1.00 20.99 ? 264 SER   A CB  1 
ATOM   1831 O OG  . SER   A 1 285 ? -6.106  -9.508  13.131  1.00 22.06 ? 264 SER   A OG  1 
ATOM   1832 N N   . LEU   A 1 286 ? -8.444  -11.927 13.749  1.00 19.83 ? 265 LEU   A N   1 
ATOM   1833 C CA  . LEU   A 1 286 ? -9.892  -11.859 13.986  1.00 21.06 ? 265 LEU   A CA  1 
ATOM   1834 C C   . LEU   A 1 286 ? -10.440 -13.114 14.669  1.00 21.66 ? 265 LEU   A C   1 
ATOM   1835 O O   . LEU   A 1 286 ? -11.635 -13.179 14.977  1.00 21.88 ? 265 LEU   A O   1 
ATOM   1836 C CB  . LEU   A 1 286 ? -10.603 -11.656 12.643  1.00 21.67 ? 265 LEU   A CB  1 
ATOM   1837 C CG  . LEU   A 1 286 ? -10.215 -10.409 11.840  1.00 20.81 ? 265 LEU   A CG  1 
ATOM   1838 C CD1 . LEU   A 1 286 ? -10.855 -10.493 10.485  1.00 23.56 ? 265 LEU   A CD1 1 
ATOM   1839 C CD2 . LEU   A 1 286 ? -10.591 -9.111  12.482  1.00 25.48 ? 265 LEU   A CD2 1 
ATOM   1840 N N   . VAL   A 1 287 ? -9.609  -14.142 14.850  1.00 22.49 ? 266 VAL   A N   1 
ATOM   1841 C CA  . VAL   A 1 287 ? -10.121 -15.436 15.298  1.00 22.31 ? 266 VAL   A CA  1 
ATOM   1842 C C   . VAL   A 1 287 ? -10.122 -15.473 16.841  1.00 28.12 ? 266 VAL   A C   1 
ATOM   1843 O O   . VAL   A 1 287 ? -9.078  -15.331 17.475  1.00 28.79 ? 266 VAL   A O   1 
ATOM   1844 C CB  . VAL   A 1 287 ? -9.225  -16.560 14.719  1.00 25.39 ? 266 VAL   A CB  1 
ATOM   1845 C CG1 . VAL   A 1 287 ? -9.688  -17.957 15.166  1.00 26.13 ? 266 VAL   A CG1 1 
ATOM   1846 C CG2 . VAL   A 1 287 ? -9.150  -16.525 13.189  1.00 23.54 ? 266 VAL   A CG2 1 
ATOM   1847 N N   . HIS   A 1 288 ? -11.282 -15.701 17.457  1.00 28.38 ? 267 HIS   A N   1 
ATOM   1848 C CA  . HIS   A 1 288 ? -11.300 -15.833 18.915  1.00 33.26 ? 267 HIS   A CA  1 
ATOM   1849 C C   . HIS   A 1 288 ? -10.646 -17.126 19.406  1.00 34.24 ? 267 HIS   A C   1 
ATOM   1850 O O   . HIS   A 1 288 ? -10.401 -18.070 18.650  1.00 32.85 ? 267 HIS   A O   1 
ATOM   1851 C CB  . HIS   A 1 288 ? -12.728 -15.769 19.470  1.00 34.21 ? 267 HIS   A CB  1 
ATOM   1852 C CG  . HIS   A 1 288 ? -13.600 -16.886 19.012  1.00 37.64 ? 267 HIS   A CG  1 
ATOM   1853 N ND1 . HIS   A 1 288 ? -13.522 -18.164 19.536  1.00 37.10 ? 267 HIS   A ND1 1 
ATOM   1854 C CD2 . HIS   A 1 288 ? -14.573 -16.921 18.081  1.00 38.79 ? 267 HIS   A CD2 1 
ATOM   1855 C CE1 . HIS   A 1 288 ? -14.425 -18.940 18.943  1.00 38.38 ? 267 HIS   A CE1 1 
ATOM   1856 N NE2 . HIS   A 1 288 ? -15.067 -18.213 18.040  1.00 41.24 ? 267 HIS   A NE2 1 
ATOM   1857 N N   . ALA   A 1 289 ? -10.433 -17.175 20.727  1.00 34.04 ? 268 ALA   A N   1 
ATOM   1858 C CA  . ALA   A 1 289 ? -9.847  -18.311 21.410  1.00 33.24 ? 268 ALA   A CA  1 
ATOM   1859 C C   . ALA   A 1 289 ? -10.753 -19.528 21.225  1.00 34.99 ? 268 ALA   A C   1 
ATOM   1860 O O   . ALA   A 1 289 ? -10.205 -20.653 21.252  1.00 42.85 ? 268 ALA   A O   1 
ATOM   1861 C CB  . ALA   A 1 289 ? -9.727  -17.977 22.885  1.00 36.02 ? 268 ALA   A CB  1 
ATOM   1862 O OXT . ALA   A 1 289 ? -11.974 -19.301 21.083  1.00 35.13 ? 268 ALA   A OXT 1 
ATOM   1863 N N   . GLU   B 1 23  ? -10.916 -13.532 -19.809 0.70 53.78 ? 2   GLU   B N   1 
ATOM   1864 C CA  . GLU   B 1 23  ? -12.081 -12.611 -19.740 0.70 50.61 ? 2   GLU   B CA  1 
ATOM   1865 C C   . GLU   B 1 23  ? -11.904 -11.649 -18.559 0.70 44.53 ? 2   GLU   B C   1 
ATOM   1866 O O   . GLU   B 1 23  ? -11.341 -11.994 -17.524 0.70 44.78 ? 2   GLU   B O   1 
ATOM   1867 C CB  . GLU   B 1 23  ? -13.355 -13.453 -19.688 0.70 46.53 ? 2   GLU   B CB  1 
ATOM   1868 C CG  . GLU   B 1 23  ? -14.609 -12.677 -20.078 0.70 54.92 ? 2   GLU   B CG  1 
ATOM   1869 C CD  . GLU   B 1 23  ? -15.867 -13.128 -19.351 0.70 59.17 ? 2   GLU   B CD  1 
ATOM   1870 O OE1 . GLU   B 1 23  ? -15.771 -13.786 -18.278 0.70 45.16 ? 2   GLU   B OE1 1 
ATOM   1871 O OE2 . GLU   B 1 23  ? -16.958 -12.807 -19.885 0.70 60.65 ? 2   GLU   B OE2 1 
ATOM   1872 N N   . ALA   B 1 24  ? -12.394 -10.425 -18.747 1.00 42.00 ? 3   ALA   B N   1 
ATOM   1873 C CA  . ALA   B 1 24  ? -12.239 -9.304  -17.838 1.00 34.25 ? 3   ALA   B CA  1 
ATOM   1874 C C   . ALA   B 1 24  ? -13.079 -9.502  -16.565 1.00 35.69 ? 3   ALA   B C   1 
ATOM   1875 O O   . ALA   B 1 24  ? -14.188 -10.031 -16.605 1.00 34.56 ? 3   ALA   B O   1 
ATOM   1876 C CB  . ALA   B 1 24  ? -12.626 -8.032  -18.588 1.00 31.59 ? 3   ALA   B CB  1 
ATOM   1877 N N   . PRO   B 1 25  ? -12.589 -9.088  -15.375 1.00 32.13 ? 4   PRO   B N   1 
ATOM   1878 C CA  . PRO   B 1 25  ? -13.411 -9.163  -14.164 1.00 26.66 ? 4   PRO   B CA  1 
ATOM   1879 C C   . PRO   B 1 25  ? -14.412 -8.014  -14.145 1.00 25.68 ? 4   PRO   B C   1 
ATOM   1880 O O   . PRO   B 1 25  ? -14.304 -7.090  -14.960 1.00 28.30 ? 4   PRO   B O   1 
ATOM   1881 C CB  . PRO   B 1 25  ? -12.323 -9.063  -13.050 1.00 28.14 ? 4   PRO   B CB  1 
ATOM   1882 C CG  . PRO   B 1 25  ? -11.227 -8.210  -13.660 1.00 29.39 ? 4   PRO   B CG  1 
ATOM   1883 C CD  . PRO   B 1 25  ? -11.211 -8.618  -15.130 1.00 31.30 ? 4   PRO   B CD  1 
ATOM   1884 N N   . ALA   B 1 26  ? -15.367 -8.073  -13.197 1.00 24.01 ? 5   ALA   B N   1 
ATOM   1885 C CA  . ALA   B 1 26  ? -16.401 -7.053  -13.055 1.00 25.59 ? 5   ALA   B CA  1 
ATOM   1886 C C   . ALA   B 1 26  ? -16.550 -6.608  -11.595 1.00 25.47 ? 5   ALA   B C   1 
ATOM   1887 O O   . ALA   B 1 26  ? -16.384 -7.414  -10.669 1.00 23.64 ? 5   ALA   B O   1 
ATOM   1888 C CB  . ALA   B 1 26  ? -17.731 -7.626  -13.561 1.00 23.64 ? 5   ALA   B CB  1 
ATOM   1889 N N   . ALA   B 1 27  ? -16.895 -5.331  -11.408 1.00 23.39 ? 6   ALA   B N   1 
ATOM   1890 C CA  . ALA   B 1 27  ? -17.007 -4.727  -10.079 1.00 22.64 ? 6   ALA   B CA  1 
ATOM   1891 C C   . ALA   B 1 27  ? -18.317 -3.961  -9.974  1.00 23.75 ? 6   ALA   B C   1 
ATOM   1892 O O   . ALA   B 1 27  ? -18.777 -3.355  -10.950 1.00 25.16 ? 6   ALA   B O   1 
ATOM   1893 C CB  . ALA   B 1 27  ? -15.860 -3.757  -9.819  1.00 22.56 ? 6   ALA   B CB  1 
ATOM   1894 N N   . VAL   B 1 28  ? -18.905 -3.981  -8.778  1.00 20.84 ? 7   VAL   B N   1 
ATOM   1895 C CA  . VAL   B 1 28  ? -20.014 -3.099  -8.440  1.00 20.19 ? 7   VAL   B CA  1 
ATOM   1896 C C   . VAL   B 1 28  ? -19.421 -1.998  -7.551  1.00 21.16 ? 7   VAL   B C   1 
ATOM   1897 O O   . VAL   B 1 28  ? -18.758 -2.304  -6.534  1.00 20.66 ? 7   VAL   B O   1 
ATOM   1898 C CB  . VAL   B 1 28  ? -21.096 -3.893  -7.664  1.00 21.06 ? 7   VAL   B CB  1 
ATOM   1899 C CG1 . VAL   B 1 28  ? -22.055 -2.984  -6.906  1.00 19.66 ? 7   VAL   B CG1 1 
ATOM   1900 C CG2 . VAL   B 1 28  ? -21.886 -4.874  -8.547  1.00 23.02 ? 7   VAL   B CG2 1 
ATOM   1901 N N   . VAL   B 1 29  ? -19.703 -0.743  -7.896  1.00 19.29 ? 8   VAL   B N   1 
ATOM   1902 C CA  . VAL   B 1 29  ? -19.333 0.383   -7.048  1.00 20.67 ? 8   VAL   B CA  1 
ATOM   1903 C C   . VAL   B 1 29  ? -20.598 1.164   -6.657  1.00 23.55 ? 8   VAL   B C   1 
ATOM   1904 O O   . VAL   B 1 29  ? -21.319 1.679   -7.524  1.00 21.21 ? 8   VAL   B O   1 
ATOM   1905 C CB  . VAL   B 1 29  ? -18.306 1.333   -7.704  1.00 20.65 ? 8   VAL   B CB  1 
ATOM   1906 C CG1 . VAL   B 1 29  ? -17.861 2.414   -6.702  1.00 19.74 ? 8   VAL   B CG1 1 
ATOM   1907 C CG2 . VAL   B 1 29  ? -17.075 0.586   -8.207  1.00 21.20 ? 8   VAL   B CG2 1 
ATOM   1908 N N   . THR   B 1 30  ? -20.872 1.284   -5.337  1.00 21.96 ? 9   THR   B N   1 
ATOM   1909 C CA  . THR   B 1 30  ? -22.095 1.969   -4.941  1.00 22.00 ? 9   THR   B CA  1 
ATOM   1910 C C   . THR   B 1 30  ? -21.792 3.458   -4.812  1.00 22.15 ? 9   THR   B C   1 
ATOM   1911 O O   . THR   B 1 30  ? -20.664 3.838   -4.559  1.00 23.68 ? 9   THR   B O   1 
ATOM   1912 C CB  . THR   B 1 30  ? -22.765 1.409   -3.683  1.00 21.58 ? 9   THR   B CB  1 
ATOM   1913 O OG1 . THR   B 1 30  ? -21.874 1.587   -2.570  1.00 20.68 ? 9   THR   B OG1 1 
ATOM   1914 C CG2 . THR   B 1 30  ? -23.192 -0.037  -3.881  1.00 19.88 ? 9   THR   B CG2 1 
ATOM   1915 N N   . GLY   B 1 31  ? -22.801 4.289   -5.060  1.00 23.47 ? 10  GLY   B N   1 
ATOM   1916 C CA  . GLY   B 1 31  ? -22.654 5.733   -5.053  1.00 22.92 ? 10  GLY   B CA  1 
ATOM   1917 C C   . GLY   B 1 31  ? -21.517 6.173   -5.973  1.00 24.03 ? 10  GLY   B C   1 
ATOM   1918 O O   . GLY   B 1 31  ? -20.701 7.009   -5.601  1.00 27.39 ? 10  GLY   B O   1 
ATOM   1919 N N   . ALA   B 1 32  ? -21.494 5.669   -7.218  1.00 23.69 ? 11  ALA   B N   1 
ATOM   1920 C CA  . ALA   B 1 32  ? -20.327 5.835   -8.084  1.00 21.24 ? 11  ALA   B CA  1 
ATOM   1921 C C   . ALA   B 1 32  ? -20.492 6.963   -9.111  1.00 24.40 ? 11  ALA   B C   1 
ATOM   1922 O O   . ALA   B 1 32  ? -19.628 7.119   -9.988  1.00 24.14 ? 11  ALA   B O   1 
ATOM   1923 C CB  . ALA   B 1 32  ? -20.013 4.526   -8.774  1.00 22.26 ? 11  ALA   B CB  1 
ATOM   1924 N N   . ALA   B 1 33  ? -21.554 7.770   -8.984  1.00 25.73 ? 12  ALA   B N   1 
ATOM   1925 C CA  . ALA   B 1 33  ? -21.814 8.791   -10.006 1.00 26.48 ? 12  ALA   B CA  1 
ATOM   1926 C C   . ALA   B 1 33  ? -20.779 9.908   -9.950  1.00 29.40 ? 12  ALA   B C   1 
ATOM   1927 O O   . ALA   B 1 33  ? -20.408 10.442  -10.983 1.00 30.23 ? 12  ALA   B O   1 
ATOM   1928 C CB  . ALA   B 1 33  ? -23.206 9.384   -9.832  1.00 29.21 ? 12  ALA   B CB  1 
ATOM   1929 N N   . LYS   B 1 34  ? -20.304 10.243  -8.745  1.00 28.42 ? 13  LYS   B N   1 
ATOM   1930 C CA  . LYS   B 1 34  ? -19.508 11.448  -8.531  1.00 31.21 ? 13  LYS   B CA  1 
ATOM   1931 C C   . LYS   B 1 34  ? -18.425 11.187  -7.476  1.00 31.67 ? 13  LYS   B C   1 
ATOM   1932 O O   . LYS   B 1 34  ? -18.481 10.176  -6.781  1.00 26.12 ? 13  LYS   B O   1 
ATOM   1933 C CB  . LYS   B 1 34  ? -20.464 12.439  -7.849  1.00 34.35 ? 13  LYS   B CB  1 
ATOM   1934 C CG  . LYS   B 1 34  ? -21.398 13.200  -8.766  0.70 37.58 ? 13  LYS   B CG  1 
ATOM   1935 C CD  . LYS   B 1 34  ? -22.329 14.141  -8.018  0.70 37.95 ? 13  LYS   B CD  1 
ATOM   1936 C CE  . LYS   B 1 34  ? -23.174 14.858  -9.031  0.70 42.60 ? 13  LYS   B CE  1 
ATOM   1937 N NZ  . LYS   B 1 34  ? -24.276 15.601  -8.415  0.70 44.17 ? 13  LYS   B NZ  1 
ATOM   1938 N N   . ARG   B 1 35  ? -17.445 12.103  -7.365  1.00 29.91 ? 14  ARG   B N   1 
ATOM   1939 C CA  . ARG   B 1 35  ? -16.546 12.160  -6.212  1.00 29.59 ? 14  ARG   B CA  1 
ATOM   1940 C C   . ARG   B 1 35  ? -15.749 10.858  -6.108  1.00 29.22 ? 14  ARG   B C   1 
ATOM   1941 O O   . ARG   B 1 35  ? -15.132 10.416  -7.077  1.00 27.14 ? 14  ARG   B O   1 
ATOM   1942 C CB  . ARG   B 1 35  ? -17.336 12.652  -4.987  1.00 28.63 ? 14  ARG   B CB  1 
ATOM   1943 C CG  . ARG   B 1 35  ? -17.952 14.031  -5.199  1.00 32.50 ? 14  ARG   B CG  1 
ATOM   1944 C CD  . ARG   B 1 35  ? -19.025 14.415  -4.192  1.00 38.50 ? 14  ARG   B CD  1 
ATOM   1945 N NE  . ARG   B 1 35  ? -18.505 14.281  -2.824  1.00 44.08 ? 14  ARG   B NE  1 
ATOM   1946 C CZ  . ARG   B 1 35  ? -17.564 15.038  -2.212  1.00 48.48 ? 14  ARG   B CZ  1 
ATOM   1947 N NH1 . ARG   B 1 35  ? -17.202 16.222  -2.687  1.00 41.45 ? 14  ARG   B NH1 1 
ATOM   1948 N NH2 . ARG   B 1 35  ? -17.024 14.626  -1.073  1.00 42.54 ? 14  ARG   B NH2 1 
ATOM   1949 N N   . ILE   B 1 36  ? -15.692 10.285  -4.902  1.00 25.94 ? 15  ILE   B N   1 
ATOM   1950 C CA  . ILE   B 1 36  ? -14.754 9.210   -4.641  1.00 24.72 ? 15  ILE   B CA  1 
ATOM   1951 C C   . ILE   B 1 36  ? -15.273 7.949   -5.342  1.00 23.10 ? 15  ILE   B C   1 
ATOM   1952 O O   . ILE   B 1 36  ? -14.498 7.247   -5.970  1.00 23.42 ? 15  ILE   B O   1 
ATOM   1953 C CB  . ILE   B 1 36  ? -14.580 9.036   -3.106  1.00 25.65 ? 15  ILE   B CB  1 
ATOM   1954 C CG1 . ILE   B 1 36  ? -13.685 10.149  -2.516  1.00 26.49 ? 15  ILE   B CG1 1 
ATOM   1955 C CG2 . ILE   B 1 36  ? -14.042 7.639   -2.781  1.00 21.33 ? 15  ILE   B CG2 1 
ATOM   1956 C CD1 . ILE   B 1 36  ? -13.693 10.224  -0.994  1.00 33.36 ? 15  ILE   B CD1 1 
ATOM   1957 N N   . GLY   B 1 37  ? -16.583 7.674   -5.240  1.00 22.61 ? 16  GLY   B N   1 
ATOM   1958 C CA  . GLY   B 1 37  ? -17.153 6.519   -5.936  1.00 23.93 ? 16  GLY   B CA  1 
ATOM   1959 C C   . GLY   B 1 37  ? -16.846 6.535   -7.445  1.00 23.84 ? 16  GLY   B C   1 
ATOM   1960 O O   . GLY   B 1 37  ? -16.453 5.534   -8.069  1.00 20.27 ? 16  GLY   B O   1 
ATOM   1961 N N   . ARG   B 1 38  ? -16.948 7.727   -8.025  1.00 21.61 ? 17  ARG   B N   1 
ATOM   1962 C CA  . ARG   B 1 38  ? -16.578 7.894   -9.423  1.00 25.73 ? 17  ARG   B CA  1 
ATOM   1963 C C   . ARG   B 1 38  ? -15.102 7.558   -9.634  1.00 26.97 ? 17  ARG   B C   1 
ATOM   1964 O O   . ARG   B 1 38  ? -14.744 6.854   -10.583 1.00 24.56 ? 17  ARG   B O   1 
ATOM   1965 C CB  . ARG   B 1 38  ? -16.860 9.350   -9.832  1.00 27.86 ? 17  ARG   B CB  1 
ATOM   1966 C CG  . ARG   B 1 38  ? -16.602 9.566   -11.316 1.00 38.17 ? 17  ARG   B CG  1 
ATOM   1967 C CD  . ARG   B 1 38  ? -16.606 11.046  -11.694 1.00 48.38 ? 17  ARG   B CD  1 
ATOM   1968 N NE  . ARG   B 1 38  ? -16.997 11.253  -13.092 1.00 54.45 ? 17  ARG   B NE  1 
ATOM   1969 C CZ  . ARG   B 1 38  ? -16.209 11.495  -14.127 1.00 55.31 ? 17  ARG   B CZ  1 
ATOM   1970 N NH1 . ARG   B 1 38  ? -14.894 11.460  -13.986 1.00 51.31 ? 17  ARG   B NH1 1 
ATOM   1971 N NH2 . ARG   B 1 38  ? -16.760 11.741  -15.308 1.00 56.37 ? 17  ARG   B NH2 1 
ATOM   1972 N N   . ALA   B 1 39  ? -14.221 8.088   -8.770  1.00 27.43 ? 18  ALA   B N   1 
ATOM   1973 C CA  . ALA   B 1 39  ? -12.791 7.880   -8.986  1.00 22.99 ? 18  ALA   B CA  1 
ATOM   1974 C C   . ALA   B 1 39  ? -12.470 6.399   -8.863  1.00 20.94 ? 18  ALA   B C   1 
ATOM   1975 O O   . ALA   B 1 39  ? -11.589 5.898   -9.565  1.00 21.64 ? 18  ALA   B O   1 
ATOM   1976 C CB  . ALA   B 1 39  ? -11.975 8.675   -7.973  1.00 22.60 ? 18  ALA   B CB  1 
ATOM   1977 N N   . ILE   B 1 40  ? -13.157 5.718   -7.928  1.00 20.15 ? 19  ILE   B N   1 
ATOM   1978 C CA  . ILE   B 1 40  ? -12.984 4.273   -7.798  1.00 19.85 ? 19  ILE   B CA  1 
ATOM   1979 C C   . ILE   B 1 40  ? -13.384 3.543   -9.090  1.00 21.26 ? 19  ILE   B C   1 
ATOM   1980 O O   . ILE   B 1 40  ? -12.616 2.717   -9.597  1.00 22.41 ? 19  ILE   B O   1 
ATOM   1981 C CB  . ILE   B 1 40  ? -13.715 3.730   -6.560  1.00 18.92 ? 19  ILE   B CB  1 
ATOM   1982 C CG1 . ILE   B 1 40  ? -13.069 4.307   -5.248  1.00 19.72 ? 19  ILE   B CG1 1 
ATOM   1983 C CG2 . ILE   B 1 40  ? -13.688 2.191   -6.573  1.00 19.50 ? 19  ILE   B CG2 1 
ATOM   1984 C CD1 . ILE   B 1 40  ? -13.944 4.158   -4.007  1.00 18.66 ? 19  ILE   B CD1 1 
ATOM   1985 N N   . ALA   B 1 41  ? -14.617 3.783   -9.564  1.00 21.30 ? 20  ALA   B N   1 
ATOM   1986 C CA  . ALA   B 1 41  ? -15.113 3.136   -10.786 1.00 22.96 ? 20  ALA   B CA  1 
ATOM   1987 C C   . ALA   B 1 41  ? -14.156 3.340   -11.964 1.00 21.28 ? 20  ALA   B C   1 
ATOM   1988 O O   . ALA   B 1 41  ? -13.860 2.398   -12.672 1.00 22.75 ? 20  ALA   B O   1 
ATOM   1989 C CB  . ALA   B 1 41  ? -16.526 3.591   -11.134 1.00 24.92 ? 20  ALA   B CB  1 
ATOM   1990 N N   . VAL   B 1 42  ? -13.647 4.561   -12.139 1.00 23.91 ? 21  VAL   B N   1 
ATOM   1991 C CA  . VAL   B 1 42  ? -12.754 4.919   -13.243 1.00 22.76 ? 21  VAL   B CA  1 
ATOM   1992 C C   . VAL   B 1 42  ? -11.430 4.173   -13.119 1.00 24.62 ? 21  VAL   B C   1 
ATOM   1993 O O   . VAL   B 1 42  ? -10.932 3.613   -14.097 1.00 22.13 ? 21  VAL   B O   1 
ATOM   1994 C CB  . VAL   B 1 42  ? -12.523 6.452   -13.288 1.00 23.97 ? 21  VAL   B CB  1 
ATOM   1995 C CG1 . VAL   B 1 42  ? -11.369 6.840   -14.214 1.00 25.38 ? 21  VAL   B CG1 1 
ATOM   1996 C CG2 . VAL   B 1 42  ? -13.788 7.203   -13.691 1.00 25.44 ? 21  VAL   B CG2 1 
ATOM   1997 N N   . LYS   B 1 43  ? -10.838 4.141   -11.902 1.00 23.74 ? 22  LYS   B N   1 
ATOM   1998 C CA  . LYS   B 1 43  ? -9.573  3.442   -11.769 1.00 24.46 ? 22  LYS   B CA  1 
ATOM   1999 C C   . LYS   B 1 43  ? -9.760  1.938   -11.955 1.00 23.89 ? 22  LYS   B C   1 
ATOM   2000 O O   . LYS   B 1 43  ? -8.887  1.274   -12.515 1.00 25.08 ? 22  LYS   B O   1 
ATOM   2001 C CB  . LYS   B 1 43  ? -8.910  3.649   -10.391 1.00 27.41 ? 22  LYS   B CB  1 
ATOM   2002 C CG  . LYS   B 1 43  ? -8.363  5.043   -10.191 1.00 29.82 ? 22  LYS   B CG  1 
ATOM   2003 C CD  . LYS   B 1 43  ? -7.041  5.013   -9.421  1.00 31.97 ? 22  LYS   B CD  1 
ATOM   2004 C CE  . LYS   B 1 43  ? -6.521  6.418   -9.478  1.00 33.99 ? 22  LYS   B CE  1 
ATOM   2005 N NZ  . LYS   B 1 43  ? -5.101  6.300   -9.806  1.00 33.91 ? 22  LYS   B NZ  1 
ATOM   2006 N N   . LEU   B 1 44  ? -10.872 1.391   -11.431 1.00 22.58 ? 23  LEU   B N   1 
ATOM   2007 C CA  . LEU   B 1 44  ? -11.105 -0.034  -11.657 1.00 22.50 ? 23  LEU   B CA  1 
ATOM   2008 C C   . LEU   B 1 44  ? -11.212 -0.278  -13.175 1.00 23.74 ? 23  LEU   B C   1 
ATOM   2009 O O   . LEU   B 1 44  ? -10.614 -1.221  -13.723 1.00 25.07 ? 23  LEU   B O   1 
ATOM   2010 C CB  . LEU   B 1 44  ? -12.392 -0.442  -10.934 1.00 23.06 ? 23  LEU   B CB  1 
ATOM   2011 C CG  . LEU   B 1 44  ? -12.253 -0.684  -9.423  1.00 22.60 ? 23  LEU   B CG  1 
ATOM   2012 C CD1 . LEU   B 1 44  ? -13.638 -0.942  -8.826  1.00 22.66 ? 23  LEU   B CD1 1 
ATOM   2013 C CD2 . LEU   B 1 44  ? -11.384 -1.927  -9.249  1.00 23.92 ? 23  LEU   B CD2 1 
ATOM   2014 N N   . HIS   B 1 45  ? -11.977 0.596   -13.844 1.00 23.81 ? 24  HIS   B N   1 
ATOM   2015 C CA  . HIS   B 1 45  ? -12.207 0.475   -15.291 1.00 26.06 ? 24  HIS   B CA  1 
ATOM   2016 C C   . HIS   B 1 45  ? -10.867 0.586   -16.028 1.00 27.80 ? 24  HIS   B C   1 
ATOM   2017 O O   . HIS   B 1 45  ? -10.562 -0.218  -16.911 1.00 27.86 ? 24  HIS   B O   1 
ATOM   2018 C CB  . HIS   B 1 45  ? -13.244 1.518   -15.742 1.00 24.79 ? 24  HIS   B CB  1 
ATOM   2019 C CG  . HIS   B 1 45  ? -13.663 1.371   -17.175 1.00 28.92 ? 24  HIS   B CG  1 
ATOM   2020 N ND1 . HIS   B 1 45  ? -13.111 2.162   -18.167 1.00 28.36 ? 24  HIS   B ND1 1 
ATOM   2021 C CD2 . HIS   B 1 45  ? -14.553 0.540   -17.787 1.00 27.68 ? 24  HIS   B CD2 1 
ATOM   2022 C CE1 . HIS   B 1 45  ? -13.627 1.806   -19.350 1.00 29.66 ? 24  HIS   B CE1 1 
ATOM   2023 N NE2 . HIS   B 1 45  ? -14.522 0.835   -19.155 1.00 27.99 ? 24  HIS   B NE2 1 
ATOM   2024 N N   . GLN   B 1 46  ? -10.034 1.556   -15.635 1.00 28.33 ? 25  GLN   B N   1 
ATOM   2025 C CA  . GLN   B 1 46  ? -8.707  1.717   -16.233 1.00 27.17 ? 25  GLN   B CA  1 
ATOM   2026 C C   . GLN   B 1 46  ? -7.823  0.490   -16.031 1.00 33.01 ? 25  GLN   B C   1 
ATOM   2027 O O   . GLN   B 1 46  ? -6.910  0.267   -16.812 1.00 31.53 ? 25  GLN   B O   1 
ATOM   2028 C CB  . GLN   B 1 46  ? -8.004  2.959   -15.697 1.00 31.37 ? 25  GLN   B CB  1 
ATOM   2029 C CG  . GLN   B 1 46  ? -8.618  4.240   -16.242 1.00 30.46 ? 25  GLN   B CG  1 
ATOM   2030 C CD  . GLN   B 1 46  ? -8.128  5.520   -15.586 1.00 36.19 ? 25  GLN   B CD  1 
ATOM   2031 O OE1 . GLN   B 1 46  ? -7.579  5.539   -14.480 1.00 41.81 ? 25  GLN   B OE1 1 
ATOM   2032 N NE2 . GLN   B 1 46  ? -8.417  6.636   -16.228 1.00 36.09 ? 25  GLN   B NE2 1 
ATOM   2033 N N   . THR   B 1 47  ? -8.072  -0.295  -14.975 1.00 31.68 ? 26  THR   B N   1 
ATOM   2034 C CA  . THR   B 1 47  ? -7.262  -1.454  -14.623 1.00 28.39 ? 26  THR   B CA  1 
ATOM   2035 C C   . THR   B 1 47  ? -7.743  -2.666  -15.408 1.00 29.64 ? 26  THR   B C   1 
ATOM   2036 O O   . THR   B 1 47  ? -7.095  -3.706  -15.375 1.00 32.87 ? 26  THR   B O   1 
ATOM   2037 C CB  . THR   B 1 47  ? -7.440  -1.694  -13.111 1.00 31.88 ? 26  THR   B CB  1 
ATOM   2038 O OG1 . THR   B 1 47  ? -6.929  -0.546  -12.447 1.00 37.55 ? 26  THR   B OG1 1 
ATOM   2039 C CG2 . THR   B 1 47  ? -6.670  -2.874  -12.576 1.00 32.59 ? 26  THR   B CG2 1 
ATOM   2040 N N   . GLY   B 1 48  ? -8.910  -2.560  -16.067 1.00 29.38 ? 27  GLY   B N   1 
ATOM   2041 C CA  . GLY   B 1 48  ? -9.431  -3.633  -16.905 1.00 26.56 ? 27  GLY   B CA  1 
ATOM   2042 C C   . GLY   B 1 48  ? -10.792 -4.172  -16.443 1.00 28.84 ? 27  GLY   B C   1 
ATOM   2043 O O   . GLY   B 1 48  ? -11.286 -5.145  -17.020 1.00 29.26 ? 27  GLY   B O   1 
ATOM   2044 N N   . TYR   B 1 49  ? -11.401 -3.573  -15.402 1.00 23.54 ? 28  TYR   B N   1 
ATOM   2045 C CA  . TYR   B 1 49  ? -12.658 -4.097  -14.858 1.00 26.78 ? 28  TYR   B CA  1 
ATOM   2046 C C   . TYR   B 1 49  ? -13.835 -3.616  -15.704 1.00 26.39 ? 28  TYR   B C   1 
ATOM   2047 O O   . TYR   B 1 49  ? -13.852 -2.474  -16.120 1.00 24.94 ? 28  TYR   B O   1 
ATOM   2048 C CB  . TYR   B 1 49  ? -12.984 -3.676  -13.407 1.00 24.38 ? 28  TYR   B CB  1 
ATOM   2049 C CG  . TYR   B 1 49  ? -12.180 -4.465  -12.374 1.00 25.67 ? 28  TYR   B CG  1 
ATOM   2050 C CD1 . TYR   B 1 49  ? -10.837 -4.174  -12.138 1.00 28.40 ? 28  TYR   B CD1 1 
ATOM   2051 C CD2 . TYR   B 1 49  ? -12.752 -5.533  -11.690 1.00 27.04 ? 28  TYR   B CD2 1 
ATOM   2052 C CE1 . TYR   B 1 49  ? -10.079 -4.915  -11.241 1.00 28.33 ? 28  TYR   B CE1 1 
ATOM   2053 C CE2 . TYR   B 1 49  ? -12.006 -6.275  -10.777 1.00 28.91 ? 28  TYR   B CE2 1 
ATOM   2054 C CZ  . TYR   B 1 49  ? -10.669 -5.963  -10.556 1.00 30.29 ? 28  TYR   B CZ  1 
ATOM   2055 O OH  . TYR   B 1 49  ? -9.926  -6.707  -9.668  1.00 28.82 ? 28  TYR   B OH  1 
ATOM   2056 N N   . ARG   B 1 50  ? -14.886 -4.428  -15.712 1.00 24.76 ? 29  ARG   B N   1 
ATOM   2057 C CA  . ARG   B 1 50  ? -16.179 -3.923  -16.221 1.00 26.74 ? 29  ARG   B CA  1 
ATOM   2058 C C   . ARG   B 1 50  ? -16.878 -3.432  -14.932 1.00 25.21 ? 29  ARG   B C   1 
ATOM   2059 O O   . ARG   B 1 50  ? -16.609 -4.024  -13.886 1.00 25.56 ? 29  ARG   B O   1 
ATOM   2060 C CB  . ARG   B 1 50  ? -16.903 -5.009  -17.015 1.00 26.92 ? 29  ARG   B CB  1 
ATOM   2061 C CG  . ARG   B 1 50  ? -16.132 -5.267  -18.298 1.00 31.02 ? 29  ARG   B CG  1 
ATOM   2062 C CD  . ARG   B 1 50  ? -16.552 -6.539  -18.976 1.00 38.89 ? 29  ARG   B CD  1 
ATOM   2063 N NE  . ARG   B 1 50  ? -16.444 -7.715  -18.109 1.00 36.20 ? 29  ARG   B NE  1 
ATOM   2064 C CZ  . ARG   B 1 50  ? -17.104 -8.826  -18.375 1.00 34.81 ? 29  ARG   B CZ  1 
ATOM   2065 N NH1 . ARG   B 1 50  ? -17.964 -8.840  -19.375 1.00 36.29 ? 29  ARG   B NH1 1 
ATOM   2066 N NH2 . ARG   B 1 50  ? -16.911 -9.908  -17.649 1.00 35.24 ? 29  ARG   B NH2 1 
ATOM   2067 N N   . VAL   B 1 51  ? -17.676 -2.362  -14.978 1.00 24.92 ? 30  VAL   B N   1 
ATOM   2068 C CA  . VAL   B 1 51  ? -18.248 -1.803  -13.752 1.00 22.35 ? 30  VAL   B CA  1 
ATOM   2069 C C   . VAL   B 1 51  ? -19.772 -1.636  -13.816 1.00 24.26 ? 30  VAL   B C   1 
ATOM   2070 O O   . VAL   B 1 51  ? -20.341 -1.319  -14.859 1.00 23.80 ? 30  VAL   B O   1 
ATOM   2071 C CB  . VAL   B 1 51  ? -17.569 -0.433  -13.524 1.00 24.46 ? 30  VAL   B CB  1 
ATOM   2072 C CG1 . VAL   B 1 51  ? -16.087 -0.588  -13.224 1.00 20.97 ? 30  VAL   B CG1 1 
ATOM   2073 C CG2 . VAL   B 1 51  ? -17.739 0.500   -14.718 1.00 27.48 ? 30  VAL   B CG2 1 
ATOM   2074 N N   . VAL   B 1 52  ? -20.434 -1.789  -12.669 1.00 21.73 ? 31  VAL   B N   1 
ATOM   2075 C CA  . VAL   B 1 52  ? -21.780 -1.286  -12.451 1.00 20.10 ? 31  VAL   B CA  1 
ATOM   2076 C C   . VAL   B 1 52  ? -21.629 -0.009  -11.654 1.00 23.18 ? 31  VAL   B C   1 
ATOM   2077 O O   . VAL   B 1 52  ? -21.072 -0.033  -10.542 1.00 23.26 ? 31  VAL   B O   1 
ATOM   2078 C CB  . VAL   B 1 52  ? -22.617 -2.290  -11.640 1.00 19.58 ? 31  VAL   B CB  1 
ATOM   2079 C CG1 . VAL   B 1 52  ? -24.001 -1.735  -11.317 1.00 18.37 ? 31  VAL   B CG1 1 
ATOM   2080 C CG2 . VAL   B 1 52  ? -22.700 -3.653  -12.332 1.00 20.34 ? 31  VAL   B CG2 1 
ATOM   2081 N N   . ILE   B 1 53  ? -22.152 1.082   -12.216 1.00 20.53 ? 32  ILE   B N   1 
ATOM   2082 C CA  . ILE   B 1 53  ? -22.177 2.349   -11.513 1.00 20.22 ? 32  ILE   B CA  1 
ATOM   2083 C C   . ILE   B 1 53  ? -23.523 2.456   -10.819 1.00 23.86 ? 32  ILE   B C   1 
ATOM   2084 O O   . ILE   B 1 53  ? -24.513 2.693   -11.499 1.00 22.50 ? 32  ILE   B O   1 
ATOM   2085 C CB  . ILE   B 1 53  ? -22.012 3.456   -12.556 1.00 21.84 ? 32  ILE   B CB  1 
ATOM   2086 C CG1 . ILE   B 1 53  ? -20.582 3.334   -13.155 1.00 26.54 ? 32  ILE   B CG1 1 
ATOM   2087 C CG2 . ILE   B 1 53  ? -22.237 4.817   -11.924 1.00 20.59 ? 32  ILE   B CG2 1 
ATOM   2088 C CD1 . ILE   B 1 53  ? -20.499 3.826   -14.583 1.00 30.47 ? 32  ILE   B CD1 1 
ATOM   2089 N N   . HIS   B 1 54  ? -23.552 2.255   -9.492  1.00 21.39 ? 33  HIS   B N   1 
ATOM   2090 C CA  . HIS   B 1 54  ? -24.811 2.426   -8.772  1.00 22.90 ? 33  HIS   B CA  1 
ATOM   2091 C C   . HIS   B 1 54  ? -24.957 3.907   -8.452  1.00 23.61 ? 33  HIS   B C   1 
ATOM   2092 O O   . HIS   B 1 54  ? -23.945 4.574   -8.182  1.00 24.94 ? 33  HIS   B O   1 
ATOM   2093 C CB  . HIS   B 1 54  ? -24.892 1.534   -7.528  1.00 23.82 ? 33  HIS   B CB  1 
ATOM   2094 C CG  . HIS   B 1 54  ? -25.837 2.106   -6.534  1.00 25.40 ? 33  HIS   B CG  1 
ATOM   2095 N ND1 . HIS   B 1 54  ? -25.438 3.055   -5.617  1.00 23.98 ? 33  HIS   B ND1 1 
ATOM   2096 C CD2 . HIS   B 1 54  ? -27.163 1.951   -6.376  1.00 23.99 ? 33  HIS   B CD2 1 
ATOM   2097 C CE1 . HIS   B 1 54  ? -26.500 3.434   -4.906  1.00 23.99 ? 33  HIS   B CE1 1 
ATOM   2098 N NE2 . HIS   B 1 54  ? -27.556 2.767   -5.336  1.00 25.03 ? 33  HIS   B NE2 1 
ATOM   2099 N N   . TYR   B 1 55  ? -26.219 4.375   -8.386  1.00 22.35 ? 34  TYR   B N   1 
ATOM   2100 C CA  . TYR   B 1 55  ? -26.463 5.770   -8.030  1.00 22.23 ? 34  TYR   B CA  1 
ATOM   2101 C C   . TYR   B 1 55  ? -27.852 5.918   -7.404  1.00 22.89 ? 34  TYR   B C   1 
ATOM   2102 O O   . TYR   B 1 55  ? -28.673 5.010   -7.447  1.00 22.83 ? 34  TYR   B O   1 
ATOM   2103 C CB  . TYR   B 1 55  ? -26.305 6.701   -9.237  1.00 22.09 ? 34  TYR   B CB  1 
ATOM   2104 C CG  . TYR   B 1 55  ? -27.400 6.496   -10.289 1.00 25.67 ? 34  TYR   B CG  1 
ATOM   2105 C CD1 . TYR   B 1 55  ? -27.368 5.418   -11.184 1.00 27.01 ? 34  TYR   B CD1 1 
ATOM   2106 C CD2 . TYR   B 1 55  ? -28.492 7.365   -10.366 1.00 26.84 ? 34  TYR   B CD2 1 
ATOM   2107 C CE1 . TYR   B 1 55  ? -28.366 5.229   -12.138 1.00 28.44 ? 34  TYR   B CE1 1 
ATOM   2108 C CE2 . TYR   B 1 55  ? -29.498 7.182   -11.313 1.00 27.79 ? 34  TYR   B CE2 1 
ATOM   2109 C CZ  . TYR   B 1 55  ? -29.436 6.121   -12.203 1.00 30.95 ? 34  TYR   B CZ  1 
ATOM   2110 O OH  . TYR   B 1 55  ? -30.465 5.935   -13.105 1.00 32.70 ? 34  TYR   B OH  1 
ATOM   2111 N N   . HIS   B 1 56  ? -28.103 7.093   -6.835  1.00 22.76 ? 35  HIS   B N   1 
ATOM   2112 C CA  . HIS   B 1 56  ? -29.412 7.325   -6.251  1.00 28.55 ? 35  HIS   B CA  1 
ATOM   2113 C C   . HIS   B 1 56  ? -30.030 8.562   -6.901  1.00 30.19 ? 35  HIS   B C   1 
ATOM   2114 O O   . HIS   B 1 56  ? -30.981 8.421   -7.651  1.00 34.60 ? 35  HIS   B O   1 
ATOM   2115 C CB  . HIS   B 1 56  ? -29.290 7.454   -4.728  1.00 33.27 ? 35  HIS   B CB  1 
ATOM   2116 C CG  . HIS   B 1 56  ? -30.595 7.790   -4.096  1.00 34.83 ? 35  HIS   B CG  1 
ATOM   2117 N ND1 . HIS   B 1 56  ? -30.716 8.742   -3.103  1.00 36.48 ? 35  HIS   B ND1 1 
ATOM   2118 C CD2 . HIS   B 1 56  ? -31.832 7.337   -4.349  1.00 33.86 ? 35  HIS   B CD2 1 
ATOM   2119 C CE1 . HIS   B 1 56  ? -31.989 8.823   -2.737  1.00 34.33 ? 35  HIS   B CE1 1 
ATOM   2120 N NE2 . HIS   B 1 56  ? -32.685 7.991   -3.493  1.00 35.55 ? 35  HIS   B NE2 1 
ATOM   2121 N N   . ASN   B 1 57  ? -29.482 9.756   -6.642  1.00 32.96 ? 36  ASN   B N   1 
ATOM   2122 C CA  . ASN   B 1 57  ? -30.066 10.961  -7.220  1.00 37.81 ? 36  ASN   B CA  1 
ATOM   2123 C C   . ASN   B 1 57  ? -29.267 11.520  -8.398  1.00 41.91 ? 36  ASN   B C   1 
ATOM   2124 O O   . ASN   B 1 57  ? -29.797 12.316  -9.159  1.00 41.34 ? 36  ASN   B O   1 
ATOM   2125 C CB  . ASN   B 1 57  ? -30.209 12.088  -6.208  1.00 41.08 ? 36  ASN   B CB  1 
ATOM   2126 C CG  . ASN   B 1 57  ? -31.195 11.736  -5.115  1.00 48.32 ? 36  ASN   B CG  1 
ATOM   2127 O OD1 . ASN   B 1 57  ? -32.295 11.228  -5.388  1.00 43.22 ? 36  ASN   B OD1 1 
ATOM   2128 N ND2 . ASN   B 1 57  ? -30.798 11.962  -3.872  1.00 48.67 ? 36  ASN   B ND2 1 
ATOM   2129 N N   . SER   B 1 58  ? -27.994 11.146  -8.549  1.00 38.85 ? 37  SER   B N   1 
ATOM   2130 C CA  . SER   B 1 58  ? -27.147 11.799  -9.540  1.00 36.05 ? 37  SER   B CA  1 
ATOM   2131 C C   . SER   B 1 58  ? -27.257 11.099  -10.896 1.00 34.75 ? 37  SER   B C   1 
ATOM   2132 O O   . SER   B 1 58  ? -26.284 10.557  -11.429 1.00 30.62 ? 37  SER   B O   1 
ATOM   2133 C CB  . SER   B 1 58  ? -25.722 11.849  -9.038  1.00 39.11 ? 37  SER   B CB  1 
ATOM   2134 O OG  . SER   B 1 58  ? -25.591 12.692  -7.895  1.00 37.70 ? 37  SER   B OG  1 
ATOM   2135 N N   . ALA   B 1 59  ? -28.454 11.137  -11.482 1.00 34.65 ? 38  ALA   B N   1 
ATOM   2136 C CA  . ALA   B 1 59  ? -28.790 10.242  -12.586 1.00 34.36 ? 38  ALA   B CA  1 
ATOM   2137 C C   . ALA   B 1 59  ? -28.060 10.617  -13.886 1.00 33.72 ? 38  ALA   B C   1 
ATOM   2138 O O   . ALA   B 1 59  ? -27.490 9.757   -14.561 1.00 32.15 ? 38  ALA   B O   1 
ATOM   2139 C CB  . ALA   B 1 59  ? -30.302 10.186  -12.749 1.00 34.43 ? 38  ALA   B CB  1 
ATOM   2140 N N   . GLU   B 1 60  ? -28.035 11.914  -14.206 1.00 32.87 ? 39  GLU   B N   1 
ATOM   2141 C CA  . GLU   B 1 60  ? -27.291 12.452  -15.339 1.00 35.05 ? 39  GLU   B CA  1 
ATOM   2142 C C   . GLU   B 1 60  ? -25.795 12.153  -15.209 1.00 37.81 ? 39  GLU   B C   1 
ATOM   2143 O O   . GLU   B 1 60  ? -25.167 11.752  -16.192 1.00 33.45 ? 39  GLU   B O   1 
ATOM   2144 C CB  . GLU   B 1 60  ? -27.657 13.926  -15.523 1.00 35.96 ? 39  GLU   B CB  1 
ATOM   2145 C CG  . GLU   B 1 60  ? -26.691 14.746  -16.372 0.50 37.93 ? 39  GLU   B CG  1 
ATOM   2146 C CD  . GLU   B 1 60  ? -27.003 16.235  -16.292 0.50 43.46 ? 39  GLU   B CD  1 
ATOM   2147 O OE1 . GLU   B 1 60  ? -28.127 16.599  -15.876 0.50 40.42 ? 39  GLU   B OE1 1 
ATOM   2148 O OE2 . GLU   B 1 60  ? -26.109 17.044  -16.625 0.50 46.41 ? 39  GLU   B OE2 1 
ATOM   2149 N N   . ALA   B 1 61  ? -25.212 12.358  -14.011 1.00 30.61 ? 40  ALA   B N   1 
ATOM   2150 C CA  . ALA   B 1 61  ? -23.787 12.113  -13.872 1.00 29.86 ? 40  ALA   B CA  1 
ATOM   2151 C C   . ALA   B 1 61  ? -23.498 10.619  -14.018 1.00 25.66 ? 40  ALA   B C   1 
ATOM   2152 O O   . ALA   B 1 61  ? -22.497 10.238  -14.636 1.00 28.98 ? 40  ALA   B O   1 
ATOM   2153 C CB  . ALA   B 1 61  ? -23.300 12.681  -12.553 1.00 36.07 ? 40  ALA   B CB  1 
ATOM   2154 N N   . ALA   B 1 62  ? -24.391 9.756   -13.502 1.00 23.97 ? 41  ALA   B N   1 
ATOM   2155 C CA  . ALA   B 1 62  ? -24.142 8.318   -13.583 1.00 24.38 ? 41  ALA   B CA  1 
ATOM   2156 C C   . ALA   B 1 62  ? -24.180 7.853   -15.038 1.00 27.02 ? 41  ALA   B C   1 
ATOM   2157 O O   . ALA   B 1 62  ? -23.322 7.062   -15.466 1.00 26.48 ? 41  ALA   B O   1 
ATOM   2158 C CB  . ALA   B 1 62  ? -25.128 7.514   -12.767 1.00 24.41 ? 41  ALA   B CB  1 
ATOM   2159 N N   . VAL   B 1 63  ? -25.207 8.321   -15.767 1.00 24.22 ? 42  VAL   B N   1 
ATOM   2160 C CA  . VAL   B 1 63  ? -25.389 7.840   -17.133 1.00 25.45 ? 42  VAL   B CA  1 
ATOM   2161 C C   . VAL   B 1 63  ? -24.233 8.382   -17.975 1.00 23.72 ? 42  VAL   B C   1 
ATOM   2162 O O   . VAL   B 1 63  ? -23.633 7.638   -18.745 1.00 22.54 ? 42  VAL   B O   1 
ATOM   2163 C CB  . VAL   B 1 63  ? -26.802 8.157   -17.685 1.00 26.82 ? 42  VAL   B CB  1 
ATOM   2164 C CG1 . VAL   B 1 63  ? -26.920 7.990   -19.201 1.00 28.59 ? 42  VAL   B CG1 1 
ATOM   2165 C CG2 . VAL   B 1 63  ? -27.894 7.341   -16.973 1.00 25.42 ? 42  VAL   B CG2 1 
ATOM   2166 N N   . SER   B 1 64  ? -23.890 9.676   -17.813 1.00 25.49 ? 43  SER   B N   1 
ATOM   2167 C CA  . SER   B 1 64  ? -22.773 10.216  -18.587 1.00 31.27 ? 43  SER   B CA  1 
ATOM   2168 C C   . SER   B 1 64  ? -21.444 9.523   -18.289 1.00 29.60 ? 43  SER   B C   1 
ATOM   2169 O O   . SER   B 1 64  ? -20.641 9.376   -19.196 1.00 27.57 ? 43  SER   B O   1 
ATOM   2170 C CB  . SER   B 1 64  ? -22.630 11.729  -18.584 1.00 33.90 ? 43  SER   B CB  1 
ATOM   2171 O OG  . SER   B 1 64  ? -23.061 12.310  -17.374 1.00 48.66 ? 43  SER   B OG  1 
ATOM   2172 N N   . LEU   B 1 65  ? -21.213 9.115   -17.024 1.00 28.30 ? 44  LEU   B N   1 
ATOM   2173 C CA  . LEU   B 1 65  ? -19.984 8.429   -16.663 1.00 26.11 ? 44  LEU   B CA  1 
ATOM   2174 C C   . LEU   B 1 65  ? -19.937 7.097   -17.403 1.00 24.96 ? 44  LEU   B C   1 
ATOM   2175 O O   . LEU   B 1 65  ? -18.939 6.764   -18.064 1.00 23.59 ? 44  LEU   B O   1 
ATOM   2176 C CB  . LEU   B 1 65  ? -19.837 8.229   -15.143 1.00 24.72 ? 44  LEU   B CB  1 
ATOM   2177 C CG  . LEU   B 1 65  ? -18.654 7.345   -14.724 1.00 26.01 ? 44  LEU   B CG  1 
ATOM   2178 C CD1 . LEU   B 1 65  ? -17.331 7.977   -15.148 1.00 24.91 ? 44  LEU   B CD1 1 
ATOM   2179 C CD2 . LEU   B 1 65  ? -18.642 7.057   -13.213 1.00 28.59 ? 44  LEU   B CD2 1 
ATOM   2180 N N   . ALA   B 1 66  ? -21.020 6.320   -17.275 1.00 24.15 ? 45  ALA   B N   1 
ATOM   2181 C CA  . ALA   B 1 66  ? -21.059 5.029   -17.943 1.00 25.48 ? 45  ALA   B CA  1 
ATOM   2182 C C   . ALA   B 1 66  ? -20.875 5.208   -19.457 1.00 25.01 ? 45  ALA   B C   1 
ATOM   2183 O O   . ALA   B 1 66  ? -20.260 4.357   -20.094 1.00 24.31 ? 45  ALA   B O   1 
ATOM   2184 C CB  . ALA   B 1 66  ? -22.339 4.267   -17.605 1.00 28.52 ? 45  ALA   B CB  1 
ATOM   2185 N N   . ASP   B 1 67  ? -21.433 6.288   -20.010 1.00 25.97 ? 46  ASP   B N   1 
ATOM   2186 C CA  . ASP   B 1 67  ? -21.313 6.580   -21.442 1.00 30.13 ? 46  ASP   B CA  1 
ATOM   2187 C C   . ASP   B 1 67  ? -19.837 6.838   -21.818 1.00 31.33 ? 46  ASP   B C   1 
ATOM   2188 O O   . ASP   B 1 67  ? -19.334 6.297   -22.813 1.00 30.26 ? 46  ASP   B O   1 
ATOM   2189 C CB  . ASP   B 1 67  ? -22.182 7.772   -21.804 1.00 27.34 ? 46  ASP   B CB  1 
ATOM   2190 C CG  . ASP   B 1 67  ? -22.256 8.087   -23.294 1.00 31.64 ? 46  ASP   B CG  1 
ATOM   2191 O OD1 . ASP   B 1 67  ? -22.291 7.138   -24.111 1.00 29.76 ? 46  ASP   B OD1 1 
ATOM   2192 O OD2 . ASP   B 1 67  ? -22.253 9.266   -23.619 1.00 31.67 ? 46  ASP   B OD2 1 
ATOM   2193 N N   . GLU   B 1 68  ? -19.141 7.671   -21.018 1.00 28.32 ? 47  GLU   B N   1 
ATOM   2194 C CA  A GLU   B 1 68  ? -17.721 7.968   -21.190 0.40 30.46 ? 47  GLU   B CA  1 
ATOM   2195 C CA  B GLU   B 1 68  ? -17.739 7.948   -21.299 0.60 31.02 ? 47  GLU   B CA  1 
ATOM   2196 C C   . GLU   B 1 68  ? -16.930 6.658   -21.161 1.00 30.52 ? 47  GLU   B C   1 
ATOM   2197 O O   . GLU   B 1 68  ? -16.034 6.398   -21.973 1.00 29.29 ? 47  GLU   B O   1 
ATOM   2198 C CB  A GLU   B 1 68  ? -17.222 8.867   -20.052 0.40 32.20 ? 47  GLU   B CB  1 
ATOM   2199 C CB  B GLU   B 1 68  ? -17.182 9.106   -20.473 0.60 33.82 ? 47  GLU   B CB  1 
ATOM   2200 C CG  A GLU   B 1 68  ? -18.040 10.139  -19.815 0.40 35.67 ? 47  GLU   B CG  1 
ATOM   2201 C CG  B GLU   B 1 68  ? -17.841 10.454  -20.767 0.60 39.30 ? 47  GLU   B CG  1 
ATOM   2202 C CD  A GLU   B 1 68  ? -17.616 11.090  -18.694 0.40 39.16 ? 47  GLU   B CD  1 
ATOM   2203 C CD  B GLU   B 1 68  ? -17.863 11.028  -22.181 0.60 40.58 ? 47  GLU   B CD  1 
ATOM   2204 O OE1 A GLU   B 1 68  ? -16.426 11.464  -18.683 0.40 35.32 ? 47  GLU   B OE1 1 
ATOM   2205 O OE1 B GLU   B 1 68  ? -18.882 11.665  -22.539 0.60 41.38 ? 47  GLU   B OE1 1 
ATOM   2206 O OE2 A GLU   B 1 68  ? -18.463 11.472  -17.838 0.40 39.78 ? 47  GLU   B OE2 1 
ATOM   2207 O OE2 B GLU   B 1 68  ? -16.878 10.843  -22.932 0.60 43.39 ? 47  GLU   B OE2 1 
ATOM   2208 N N   . LEU   B 1 69  ? -17.265 5.806   -20.174 1.00 27.71 ? 48  LEU   B N   1 
ATOM   2209 C CA  . LEU   B 1 69  ? -16.540 4.549   -20.034 1.00 25.68 ? 48  LEU   B CA  1 
ATOM   2210 C C   . LEU   B 1 69  ? -16.784 3.634   -21.236 1.00 29.43 ? 48  LEU   B C   1 
ATOM   2211 O O   . LEU   B 1 69  ? -15.841 2.978   -21.708 1.00 27.67 ? 48  LEU   B O   1 
ATOM   2212 C CB  . LEU   B 1 69  ? -16.869 3.859   -18.714 1.00 25.27 ? 48  LEU   B CB  1 
ATOM   2213 C CG  . LEU   B 1 69  ? -16.444 4.665   -17.471 1.00 28.43 ? 48  LEU   B CG  1 
ATOM   2214 C CD1 . LEU   B 1 69  ? -16.840 3.943   -16.160 1.00 26.60 ? 48  LEU   B CD1 1 
ATOM   2215 C CD2 . LEU   B 1 69  ? -14.950 5.053   -17.551 1.00 24.06 ? 48  LEU   B CD2 1 
ATOM   2216 N N   . ASN   B 1 70  ? -18.052 3.563   -21.697 1.00 28.02 ? 49  ASN   B N   1 
ATOM   2217 C CA  . ASN   B 1 70  ? -18.397 2.686   -22.822 1.00 25.64 ? 49  ASN   B CA  1 
ATOM   2218 C C   . ASN   B 1 70  ? -17.806 3.226   -24.129 1.00 26.44 ? 49  ASN   B C   1 
ATOM   2219 O O   . ASN   B 1 70  ? -17.493 2.455   -25.037 1.00 27.27 ? 49  ASN   B O   1 
ATOM   2220 C CB  . ASN   B 1 70  ? -19.896 2.451   -22.947 1.00 24.65 ? 49  ASN   B CB  1 
ATOM   2221 C CG  . ASN   B 1 70  ? -20.433 1.526   -21.880 1.00 23.53 ? 49  ASN   B CG  1 
ATOM   2222 O OD1 . ASN   B 1 70  ? -19.737 0.590   -21.445 1.00 25.20 ? 49  ASN   B OD1 1 
ATOM   2223 N ND2 . ASN   B 1 70  ? -21.675 1.758   -21.462 1.00 19.96 ? 49  ASN   B ND2 1 
ATOM   2224 N N   . LYS   B 1 71  ? -17.615 4.541   -24.221 1.00 27.28 ? 50  LYS   B N   1 
ATOM   2225 C CA  . LYS   B 1 71  ? -16.889 5.092   -25.355 1.00 31.16 ? 50  LYS   B CA  1 
ATOM   2226 C C   . LYS   B 1 71  ? -15.431 4.622   -25.383 1.00 31.52 ? 50  LYS   B C   1 
ATOM   2227 O O   . LYS   B 1 71  ? -14.894 4.409   -26.466 1.00 32.49 ? 50  LYS   B O   1 
ATOM   2228 C CB  . LYS   B 1 71  ? -17.018 6.610   -25.459 1.00 32.24 ? 50  LYS   B CB  1 
ATOM   2229 C CG  . LYS   B 1 71  ? -18.400 7.087   -25.859 1.00 37.08 ? 50  LYS   B CG  1 
ATOM   2230 C CD  . LYS   B 1 71  ? -18.311 8.608   -25.851 1.00 41.75 ? 50  LYS   B CD  1 
ATOM   2231 C CE  . LYS   B 1 71  ? -19.666 9.172   -25.788 1.00 45.42 ? 50  LYS   B CE  1 
ATOM   2232 N NZ  . LYS   B 1 71  ? -19.576 10.612  -25.560 1.00 46.71 ? 50  LYS   B NZ  1 
ATOM   2233 N N   . GLU   B 1 72  ? -14.814 4.431   -24.210 1.00 30.34 ? 51  GLU   B N   1 
ATOM   2234 C CA  A GLU   B 1 72  ? -13.457 3.923   -24.078 0.50 33.44 ? 51  GLU   B CA  1 
ATOM   2235 C CA  B GLU   B 1 72  ? -13.454 3.938   -24.116 0.50 33.21 ? 51  GLU   B CA  1 
ATOM   2236 C C   . GLU   B 1 72  ? -13.431 2.446   -24.474 1.00 32.20 ? 51  GLU   B C   1 
ATOM   2237 O O   . GLU   B 1 72  ? -12.581 2.014   -25.233 1.00 33.48 ? 51  GLU   B O   1 
ATOM   2238 C CB  A GLU   B 1 72  ? -12.987 4.015   -22.625 0.50 35.50 ? 51  GLU   B CB  1 
ATOM   2239 C CB  B GLU   B 1 72  ? -12.900 4.349   -22.748 0.50 35.01 ? 51  GLU   B CB  1 
ATOM   2240 C CG  A GLU   B 1 72  ? -11.503 4.326   -22.438 0.50 45.19 ? 51  GLU   B CG  1 
ATOM   2241 C CG  B GLU   B 1 72  ? -11.505 4.969   -22.803 0.50 43.78 ? 51  GLU   B CG  1 
ATOM   2242 C CD  A GLU   B 1 72  ? -10.450 3.914   -23.458 0.50 48.32 ? 51  GLU   B CD  1 
ATOM   2243 C CD  B GLU   B 1 72  ? -11.347 6.282   -23.556 0.50 47.20 ? 51  GLU   B CD  1 
ATOM   2244 O OE1 A GLU   B 1 72  ? -10.324 2.738   -23.860 0.50 52.21 ? 51  GLU   B OE1 1 
ATOM   2245 O OE1 B GLU   B 1 72  ? -12.121 7.235   -23.323 0.50 45.47 ? 51  GLU   B OE1 1 
ATOM   2246 O OE2 A GLU   B 1 72  ? -9.707  4.830   -23.837 0.50 48.71 ? 51  GLU   B OE2 1 
ATOM   2247 O OE2 B GLU   B 1 72  ? -10.416 6.363   -24.380 0.50 54.61 ? 51  GLU   B OE2 1 
ATOM   2248 N N   . ARG   B 1 73  ? -14.368 1.650   -23.950 1.00 28.55 ? 52  ARG   B N   1 
ATOM   2249 C CA  . ARG   B 1 73  ? -14.421 0.221   -24.260 1.00 30.05 ? 52  ARG   B CA  1 
ATOM   2250 C C   . ARG   B 1 73  ? -15.875 -0.249  -24.259 1.00 35.06 ? 52  ARG   B C   1 
ATOM   2251 O O   . ARG   B 1 73  ? -16.575 -0.097  -23.250 1.00 27.84 ? 52  ARG   B O   1 
ATOM   2252 C CB  . ARG   B 1 73  ? -13.639 -0.671  -23.280 1.00 32.72 ? 52  ARG   B CB  1 
ATOM   2253 C CG  . ARG   B 1 73  ? -12.149 -0.433  -23.045 1.00 37.00 ? 52  ARG   B CG  1 
ATOM   2254 C CD  . ARG   B 1 73  ? -11.405 -1.666  -22.496 1.00 38.79 ? 52  ARG   B CD  1 
ATOM   2255 N NE  . ARG   B 1 73  ? -11.908 -2.200  -21.220 1.00 34.97 ? 52  ARG   B NE  1 
ATOM   2256 C CZ  . ARG   B 1 73  ? -11.799 -1.604  -20.030 1.00 40.72 ? 52  ARG   B CZ  1 
ATOM   2257 N NH1 . ARG   B 1 73  ? -11.117 -0.468  -19.922 1.00 40.68 ? 52  ARG   B NH1 1 
ATOM   2258 N NH2 . ARG   B 1 73  ? -12.382 -2.149  -18.963 1.00 35.75 ? 52  ARG   B NH2 1 
ATOM   2259 N N   . SER   B 1 74  ? -16.319 -0.866  -25.371 1.00 30.99 ? 53  SER   B N   1 
ATOM   2260 C CA  . SER   B 1 74  ? -17.734 -1.088  -25.621 1.00 33.64 ? 53  SER   B CA  1 
ATOM   2261 C C   . SER   B 1 74  ? -18.367 -1.933  -24.525 1.00 27.67 ? 53  SER   B C   1 
ATOM   2262 O O   . SER   B 1 74  ? -17.835 -2.989  -24.223 1.00 31.94 ? 53  SER   B O   1 
ATOM   2263 C CB  . SER   B 1 74  ? -17.924 -1.769  -26.964 1.00 41.18 ? 53  SER   B CB  1 
ATOM   2264 O OG  . SER   B 1 74  ? -17.859 -0.804  -28.008 1.00 46.66 ? 53  SER   B OG  1 
ATOM   2265 N N   . ASN   B 1 75  ? -19.532 -1.485  -24.023 1.00 28.09 ? 54  ASN   B N   1 
ATOM   2266 C CA  . ASN   B 1 75  ? -20.375 -2.246  -23.100 1.00 28.61 ? 54  ASN   B CA  1 
ATOM   2267 C C   . ASN   B 1 75  ? -19.559 -2.722  -21.887 1.00 29.27 ? 54  ASN   B C   1 
ATOM   2268 O O   . ASN   B 1 75  ? -19.658 -3.881  -21.487 1.00 26.85 ? 54  ASN   B O   1 
ATOM   2269 C CB  . ASN   B 1 75  ? -21.055 -3.446  -23.762 1.00 28.86 ? 54  ASN   B CB  1 
ATOM   2270 C CG  . ASN   B 1 75  ? -22.138 -2.977  -24.704 1.00 38.59 ? 54  ASN   B CG  1 
ATOM   2271 O OD1 . ASN   B 1 75  ? -22.947 -2.125  -24.322 1.00 33.88 ? 54  ASN   B OD1 1 
ATOM   2272 N ND2 . ASN   B 1 75  ? -22.145 -3.483  -25.931 1.00 34.58 ? 54  ASN   B ND2 1 
ATOM   2273 N N   . THR   B 1 76  ? -18.764 -1.824  -21.304 1.00 24.81 ? 55  THR   B N   1 
ATOM   2274 C CA  . THR   B 1 76  ? -17.989 -2.216  -20.121 1.00 24.80 ? 55  THR   B CA  1 
ATOM   2275 C C   . THR   B 1 76  ? -18.548 -1.548  -18.859 1.00 26.15 ? 55  THR   B C   1 
ATOM   2276 O O   . THR   B 1 76  ? -17.953 -1.692  -17.785 1.00 27.33 ? 55  THR   B O   1 
ATOM   2277 C CB  . THR   B 1 76  ? -16.491 -1.930  -20.275 1.00 24.50 ? 55  THR   B CB  1 
ATOM   2278 O OG1 . THR   B 1 76  ? -16.369 -0.563  -20.667 1.00 21.90 ? 55  THR   B OG1 1 
ATOM   2279 C CG2 . THR   B 1 76  ? -15.803 -2.824  -21.292 1.00 24.56 ? 55  THR   B CG2 1 
ATOM   2280 N N   . ALA   B 1 77  ? -19.666 -0.811  -18.990 1.00 22.14 ? 56  ALA   B N   1 
ATOM   2281 C CA  . ALA   B 1 77  ? -20.252 -0.107  -17.863 1.00 21.76 ? 56  ALA   B CA  1 
ATOM   2282 C C   . ALA   B 1 77  ? -21.771 -0.114  -18.021 1.00 24.00 ? 56  ALA   B C   1 
ATOM   2283 O O   . ALA   B 1 77  ? -22.302 0.127   -19.124 1.00 23.61 ? 56  ALA   B O   1 
ATOM   2284 C CB  . ALA   B 1 77  ? -19.726 1.314   -17.798 1.00 20.63 ? 56  ALA   B CB  1 
ATOM   2285 N N   . VAL   B 1 78  ? -22.464 -0.399  -16.911 1.00 24.08 ? 57  VAL   B N   1 
ATOM   2286 C CA  . VAL   B 1 78  ? -23.917 -0.230  -16.815 1.00 23.09 ? 57  VAL   B CA  1 
ATOM   2287 C C   . VAL   B 1 78  ? -24.200 0.624   -15.587 1.00 26.35 ? 57  VAL   B C   1 
ATOM   2288 O O   . VAL   B 1 78  ? -23.326 0.760   -14.717 1.00 22.04 ? 57  VAL   B O   1 
ATOM   2289 C CB  . VAL   B 1 78  ? -24.626 -1.593  -16.707 1.00 25.64 ? 57  VAL   B CB  1 
ATOM   2290 C CG1 . VAL   B 1 78  ? -24.417 -2.394  -17.997 1.00 25.43 ? 57  VAL   B CG1 1 
ATOM   2291 C CG2 . VAL   B 1 78  ? -24.134 -2.409  -15.499 1.00 24.37 ? 57  VAL   B CG2 1 
ATOM   2292 N N   . VAL   B 1 79  ? -25.411 1.192   -15.530 1.00 23.53 ? 58  VAL   B N   1 
ATOM   2293 C CA  . VAL   B 1 79  ? -25.852 1.874   -14.328 1.00 25.72 ? 58  VAL   B CA  1 
ATOM   2294 C C   . VAL   B 1 79  ? -26.971 1.086   -13.655 1.00 27.26 ? 58  VAL   B C   1 
ATOM   2295 O O   . VAL   B 1 79  ? -27.689 0.315   -14.307 1.00 24.52 ? 58  VAL   B O   1 
ATOM   2296 C CB  . VAL   B 1 79  ? -26.293 3.300   -14.702 1.00 28.33 ? 58  VAL   B CB  1 
ATOM   2297 C CG1 . VAL   B 1 79  ? -25.139 4.033   -15.383 1.00 26.75 ? 58  VAL   B CG1 1 
ATOM   2298 C CG2 . VAL   B 1 79  ? -27.562 3.311   -15.546 1.00 25.67 ? 58  VAL   B CG2 1 
ATOM   2299 N N   . CYS   B 1 80  ? -27.094 1.284   -12.328 1.00 24.11 ? 59  CYS   B N   1 
ATOM   2300 C CA  . CYS   B 1 80  ? -28.202 0.716   -11.579 1.00 24.80 ? 59  CYS   B CA  1 
ATOM   2301 C C   . CYS   B 1 80  ? -28.589 1.699   -10.473 1.00 27.56 ? 59  CYS   B C   1 
ATOM   2302 O O   . CYS   B 1 80  ? -27.813 1.913   -9.528  1.00 26.71 ? 59  CYS   B O   1 
ATOM   2303 C CB  . CYS   B 1 80  ? -27.816 -0.667  -11.046 1.00 24.54 ? 59  CYS   B CB  1 
ATOM   2304 S SG  . CYS   B 1 80  ? -29.155 -1.467  -10.106 1.00 28.39 ? 59  CYS   B SG  1 
ATOM   2305 N N   . GLN   B 1 81  ? -29.789 2.279   -10.585 1.00 24.37 ? 60  GLN   B N   1 
ATOM   2306 C CA  A GLN   B 1 81  ? -30.335 3.172   -9.577  0.50 26.32 ? 60  GLN   B CA  1 
ATOM   2307 C CA  B GLN   B 1 81  ? -30.329 3.175   -9.575  0.50 26.64 ? 60  GLN   B CA  1 
ATOM   2308 C C   . GLN   B 1 81  ? -30.933 2.347   -8.433  1.00 28.69 ? 60  GLN   B C   1 
ATOM   2309 O O   . GLN   B 1 81  ? -31.651 1.382   -8.680  1.00 25.29 ? 60  GLN   B O   1 
ATOM   2310 C CB  A GLN   B 1 81  ? -31.418 4.067   -10.187 0.50 26.10 ? 60  GLN   B CB  1 
ATOM   2311 C CB  B GLN   B 1 81  ? -31.336 4.148   -10.202 0.50 27.06 ? 60  GLN   B CB  1 
ATOM   2312 C CG  A GLN   B 1 81  ? -31.886 5.199   -9.272  0.50 26.41 ? 60  GLN   B CG  1 
ATOM   2313 C CG  B GLN   B 1 81  ? -31.840 5.246   -9.262  0.50 27.86 ? 60  GLN   B CG  1 
ATOM   2314 C CD  A GLN   B 1 81  ? -32.900 4.787   -8.224  0.50 28.79 ? 60  GLN   B CD  1 
ATOM   2315 C CD  B GLN   B 1 81  ? -32.810 6.218   -9.907  0.50 32.00 ? 60  GLN   B CD  1 
ATOM   2316 O OE1 A GLN   B 1 81  ? -33.552 3.739   -8.314  0.50 30.96 ? 60  GLN   B OE1 1 
ATOM   2317 O OE1 B GLN   B 1 81  ? -33.736 5.818   -10.624 0.50 32.49 ? 60  GLN   B OE1 1 
ATOM   2318 N NE2 A GLN   B 1 81  ? -33.049 5.622   -7.203  0.50 30.17 ? 60  GLN   B NE2 1 
ATOM   2319 N NE2 B GLN   B 1 81  ? -32.615 7.511   -9.661  0.50 31.42 ? 60  GLN   B NE2 1 
ATOM   2320 N N   . ALA   B 1 82  ? -30.612 2.723   -7.171  1.00 25.85 ? 61  ALA   B N   1 
ATOM   2321 C CA  . ALA   B 1 82  ? -31.332 2.197   -6.014  1.00 24.02 ? 61  ALA   B CA  1 
ATOM   2322 C C   . ALA   B 1 82  ? -31.196 3.132   -4.818  1.00 24.57 ? 61  ALA   B C   1 
ATOM   2323 O O   . ALA   B 1 82  ? -30.125 3.642   -4.538  1.00 23.24 ? 61  ALA   B O   1 
ATOM   2324 C CB  . ALA   B 1 82  ? -30.894 0.788   -5.673  1.00 23.37 ? 61  ALA   B CB  1 
ATOM   2325 N N   . ASP   B 1 83  ? -32.312 3.349   -4.119  1.00 26.64 ? 62  ASP   B N   1 
ATOM   2326 C CA  . ASP   B 1 83  ? -32.290 3.984   -2.813  1.00 27.57 ? 62  ASP   B CA  1 
ATOM   2327 C C   . ASP   B 1 83  ? -31.772 2.955   -1.799  1.00 26.20 ? 62  ASP   B C   1 
ATOM   2328 O O   . ASP   B 1 83  ? -32.270 1.816   -1.718  1.00 24.46 ? 62  ASP   B O   1 
ATOM   2329 C CB  . ASP   B 1 83  ? -33.684 4.514   -2.466  1.00 29.90 ? 62  ASP   B CB  1 
ATOM   2330 C CG  . ASP   B 1 83  ? -33.765 5.324   -1.180  1.00 31.29 ? 62  ASP   B CG  1 
ATOM   2331 O OD1 . ASP   B 1 83  ? -32.696 5.572   -0.567  1.00 30.05 ? 62  ASP   B OD1 1 
ATOM   2332 O OD2 . ASP   B 1 83  ? -34.892 5.738   -0.817  1.00 32.44 ? 62  ASP   B OD2 1 
ATOM   2333 N N   . LEU   B 1 84  ? -30.751 3.344   -1.024  1.00 22.93 ? 63  LEU   B N   1 
ATOM   2334 C CA  . LEU   B 1 84  ? -30.186 2.390   -0.083  1.00 20.73 ? 63  LEU   B CA  1 
ATOM   2335 C C   . LEU   B 1 84  ? -30.645 2.688   1.342   1.00 22.87 ? 63  LEU   B C   1 
ATOM   2336 O O   . LEU   B 1 84  ? -30.072 2.128   2.284   1.00 23.06 ? 63  LEU   B O   1 
ATOM   2337 C CB  . LEU   B 1 84  ? -28.661 2.324   -0.198  1.00 23.06 ? 63  LEU   B CB  1 
ATOM   2338 C CG  . LEU   B 1 84  ? -28.125 1.864   -1.553  1.00 23.33 ? 63  LEU   B CG  1 
ATOM   2339 C CD1 . LEU   B 1 84  ? -26.600 1.878   -1.682  1.00 26.09 ? 63  LEU   B CD1 1 
ATOM   2340 C CD2 . LEU   B 1 84  ? -28.649 0.482   -1.914  1.00 23.63 ? 63  LEU   B CD2 1 
ATOM   2341 N N   . THR   B 1 85  ? -31.670 3.549   1.485   1.00 22.60 ? 64  THR   B N   1 
ATOM   2342 C CA  . THR   B 1 85  ? -32.358 3.713   2.757   1.00 26.32 ? 64  THR   B CA  1 
ATOM   2343 C C   . THR   B 1 85  ? -32.835 2.356   3.280   1.00 27.61 ? 64  THR   B C   1 
ATOM   2344 O O   . THR   B 1 85  ? -33.412 1.579   2.528   1.00 23.61 ? 64  THR   B O   1 
ATOM   2345 C CB  . THR   B 1 85  ? -33.569 4.600   2.529   1.00 26.69 ? 64  THR   B CB  1 
ATOM   2346 O OG1 . THR   B 1 85  ? -32.995 5.792   2.018   1.00 28.20 ? 64  THR   B OG1 1 
ATOM   2347 C CG2 . THR   B 1 85  ? -34.258 4.936   3.843   1.00 28.97 ? 64  THR   B CG2 1 
ATOM   2348 N N   . ASN   B 1 86  ? -32.729 2.132   4.605   1.00 24.78 ? 65  ASN   B N   1 
ATOM   2349 C CA  . ASN   B 1 86  ? -33.264 0.918   5.192   1.00 25.89 ? 65  ASN   B CA  1 
ATOM   2350 C C   . ASN   B 1 86  ? -34.787 0.871   5.015   1.00 28.35 ? 65  ASN   B C   1 
ATOM   2351 O O   . ASN   B 1 86  ? -35.485 1.868   5.178   1.00 27.20 ? 65  ASN   B O   1 
ATOM   2352 C CB  . ASN   B 1 86  ? -32.907 0.790   6.672   1.00 25.44 ? 65  ASN   B CB  1 
ATOM   2353 C CG  . ASN   B 1 86  ? -33.383 -0.520  7.238   1.00 30.50 ? 65  ASN   B CG  1 
ATOM   2354 O OD1 . ASN   B 1 86  ? -33.989 -0.541  8.319   1.00 36.32 ? 65  ASN   B OD1 1 
ATOM   2355 N ND2 . ASN   B 1 86  ? -33.081 -1.612  6.556   1.00 25.09 ? 65  ASN   B ND2 1 
ATOM   2356 N N   . SER   B 1 87  ? -35.294 -0.301  4.634   1.00 28.44 ? 66  SER   B N   1 
ATOM   2357 C CA  . SER   B 1 87  ? -36.722 -0.505  4.470   1.00 31.90 ? 66  SER   B CA  1 
ATOM   2358 C C   . SER   B 1 87  ? -36.919 -2.002  4.297   1.00 30.27 ? 66  SER   B C   1 
ATOM   2359 O O   . SER   B 1 87  ? -35.935 -2.737  4.166   1.00 32.73 ? 66  SER   B O   1 
ATOM   2360 C CB  . SER   B 1 87  ? -37.259 0.227   3.256   1.00 32.64 ? 66  SER   B CB  1 
ATOM   2361 O OG  . SER   B 1 87  ? -36.932 -0.491  2.070   1.00 37.17 ? 66  SER   B OG  1 
ATOM   2362 N N   . ASN   B 1 88  ? -38.178 -2.446  4.219   1.00 30.79 ? 67  ASN   B N   1 
ATOM   2363 C CA  . ASN   B 1 88  ? -38.419 -3.865  3.970   1.00 36.26 ? 67  ASN   B CA  1 
ATOM   2364 C C   . ASN   B 1 88  ? -38.165 -4.237  2.493   1.00 30.94 ? 67  ASN   B C   1 
ATOM   2365 O O   . ASN   B 1 88  ? -38.023 -5.424  2.200   1.00 34.12 ? 67  ASN   B O   1 
ATOM   2366 C CB  . ASN   B 1 88  ? -39.675 -4.399  4.686   1.00 39.39 ? 67  ASN   B CB  1 
ATOM   2367 C CG  . ASN   B 1 88  ? -39.482 -4.582  6.185   0.70 45.03 ? 67  ASN   B CG  1 
ATOM   2368 O OD1 . ASN   B 1 88  ? -38.425 -4.251  6.744   0.70 45.42 ? 67  ASN   B OD1 1 
ATOM   2369 N ND2 . ASN   B 1 88  ? -40.486 -5.113  6.870   0.70 46.37 ? 67  ASN   B ND2 1 
ATOM   2370 N N   . VAL   B 1 89  ? -38.025 -3.257  1.578   1.00 31.13 ? 68  VAL   B N   1 
ATOM   2371 C CA  . VAL   B 1 89  ? -37.633 -3.569  0.192   1.00 32.02 ? 68  VAL   B CA  1 
ATOM   2372 C C   . VAL   B 1 89  ? -36.117 -3.441  -0.047  1.00 34.95 ? 68  VAL   B C   1 
ATOM   2373 O O   . VAL   B 1 89  ? -35.630 -3.656  -1.160  1.00 31.47 ? 68  VAL   B O   1 
ATOM   2374 C CB  . VAL   B 1 89  ? -38.413 -2.829  -0.917  1.00 35.75 ? 68  VAL   B CB  1 
ATOM   2375 C CG1 . VAL   B 1 89  ? -39.919 -2.908  -0.685  1.00 43.66 ? 68  VAL   B CG1 1 
ATOM   2376 C CG2 . VAL   B 1 89  ? -37.978 -1.373  -1.085  1.00 33.01 ? 68  VAL   B CG2 1 
ATOM   2377 N N   . LEU   B 1 90  ? -35.343 -3.074  0.980   1.00 31.51 ? 69  LEU   B N   1 
ATOM   2378 C CA  . LEU   B 1 90  ? -33.923 -2.848  0.744   1.00 28.01 ? 69  LEU   B CA  1 
ATOM   2379 C C   . LEU   B 1 90  ? -33.231 -4.145  0.327   1.00 26.12 ? 69  LEU   B C   1 
ATOM   2380 O O   . LEU   B 1 90  ? -32.398 -4.126  -0.577  1.00 26.72 ? 69  LEU   B O   1 
ATOM   2381 C CB  . LEU   B 1 90  ? -33.234 -2.140  1.926   1.00 26.96 ? 69  LEU   B CB  1 
ATOM   2382 C CG  . LEU   B 1 90  ? -31.720 -1.918  1.773   1.00 23.90 ? 69  LEU   B CG  1 
ATOM   2383 C CD1 . LEU   B 1 90  ? -31.415 -0.991  0.610   1.00 21.70 ? 69  LEU   B CD1 1 
ATOM   2384 C CD2 . LEU   B 1 90  ? -31.084 -1.390  3.067   1.00 21.16 ? 69  LEU   B CD2 1 
ATOM   2385 N N   . PRO   B 1 91  ? -33.512 -5.316  0.947   1.00 26.29 ? 70  PRO   B N   1 
ATOM   2386 C CA  . PRO   B 1 91  ? -32.855 -6.549  0.517   1.00 29.27 ? 70  PRO   B CA  1 
ATOM   2387 C C   . PRO   B 1 91  ? -33.025 -6.854  -0.979  1.00 32.84 ? 70  PRO   B C   1 
ATOM   2388 O O   . PRO   B 1 91  ? -32.068 -7.268  -1.640  1.00 30.75 ? 70  PRO   B O   1 
ATOM   2389 C CB  . PRO   B 1 91  ? -33.485 -7.626  1.439   1.00 28.07 ? 70  PRO   B CB  1 
ATOM   2390 C CG  . PRO   B 1 91  ? -33.945 -6.846  2.682   1.00 25.61 ? 70  PRO   B CG  1 
ATOM   2391 C CD  . PRO   B 1 91  ? -34.437 -5.535  2.077   1.00 27.37 ? 70  PRO   B CD  1 
ATOM   2392 N N   . ALA   B 1 92  ? -34.253 -6.652  -1.494  1.00 33.62 ? 71  ALA   B N   1 
ATOM   2393 C CA  . ALA   B 1 92  ? -34.563 -6.821  -2.913  1.00 33.28 ? 71  ALA   B CA  1 
ATOM   2394 C C   . ALA   B 1 92  ? -33.738 -5.861  -3.771  1.00 31.52 ? 71  ALA   B C   1 
ATOM   2395 O O   . ALA   B 1 92  ? -33.141 -6.291  -4.762  1.00 32.68 ? 71  ALA   B O   1 
ATOM   2396 C CB  . ALA   B 1 92  ? -36.057 -6.662  -3.193  1.00 33.13 ? 71  ALA   B CB  1 
ATOM   2397 N N   . SER   B 1 93  ? -33.698 -4.572  -3.396  1.00 29.07 ? 72  SER   B N   1 
ATOM   2398 C CA  . SER   B 1 93  ? -32.869 -3.637  -4.140  1.00 27.20 ? 72  SER   B CA  1 
ATOM   2399 C C   . SER   B 1 93  ? -31.427 -4.136  -4.213  1.00 29.10 ? 72  SER   B C   1 
ATOM   2400 O O   . SER   B 1 93  ? -30.812 -4.060  -5.264  1.00 25.69 ? 72  SER   B O   1 
ATOM   2401 C CB  . SER   B 1 93  ? -32.902 -2.259  -3.523  1.00 31.58 ? 72  SER   B CB  1 
ATOM   2402 O OG  . SER   B 1 93  ? -34.232 -1.782  -3.437  1.00 30.07 ? 72  SER   B OG  1 
ATOM   2403 N N   . CYS   B 1 94  ? -30.860 -4.576  -3.067  1.00 28.20 ? 73  CYS   B N   1 
ATOM   2404 C CA  . CYS   B 1 94  ? -29.440 -4.920  -3.027  1.00 27.39 ? 73  CYS   B CA  1 
ATOM   2405 C C   . CYS   B 1 94  ? -29.177 -6.140  -3.910  1.00 26.18 ? 73  CYS   B C   1 
ATOM   2406 O O   . CYS   B 1 94  ? -28.185 -6.210  -4.635  1.00 24.45 ? 73  CYS   B O   1 
ATOM   2407 C CB  . CYS   B 1 94  ? -28.972 -5.120  -1.580  1.00 26.38 ? 73  CYS   B CB  1 
ATOM   2408 S SG  . CYS   B 1 94  ? -28.952 -3.563  -0.651  1.00 23.96 ? 73  CYS   B SG  1 
ATOM   2409 N N   . GLU   B 1 95  ? -30.076 -7.117  -3.839  1.00 25.65 ? 74  GLU   B N   1 
ATOM   2410 C CA  . GLU   B 1 95  ? -29.960 -8.314  -4.667  1.00 30.18 ? 74  GLU   B CA  1 
ATOM   2411 C C   . GLU   B 1 95  ? -29.979 -7.915  -6.152  1.00 29.82 ? 74  GLU   B C   1 
ATOM   2412 O O   . GLU   B 1 95  ? -29.223 -8.461  -6.957  1.00 28.90 ? 74  GLU   B O   1 
ATOM   2413 C CB  . GLU   B 1 95  ? -31.092 -9.281  -4.290  1.00 32.67 ? 74  GLU   B CB  1 
ATOM   2414 C CG  . GLU   B 1 95  ? -31.233 -10.477 -5.226  1.00 34.66 ? 74  GLU   B CG  1 
ATOM   2415 C CD  . GLU   B 1 95  ? -30.180 -11.561 -5.100  0.70 43.46 ? 74  GLU   B CD  1 
ATOM   2416 O OE1 . GLU   B 1 95  ? -30.131 -12.416 -6.007  0.70 47.32 ? 74  GLU   B OE1 1 
ATOM   2417 O OE2 . GLU   B 1 95  ? -29.408 -11.560 -4.111  0.70 48.25 ? 74  GLU   B OE2 1 
ATOM   2418 N N   . GLU   B 1 96  ? -30.815 -6.930  -6.499  1.00 27.37 ? 75  GLU   B N   1 
ATOM   2419 C CA  . GLU   B 1 96  ? -30.918 -6.465  -7.882  1.00 29.44 ? 75  GLU   B CA  1 
ATOM   2420 C C   . GLU   B 1 96  ? -29.632 -5.760  -8.331  1.00 27.65 ? 75  GLU   B C   1 
ATOM   2421 O O   . GLU   B 1 96  ? -29.284 -5.819  -9.510  1.00 25.05 ? 75  GLU   B O   1 
ATOM   2422 C CB  . GLU   B 1 96  ? -32.160 -5.598  -8.135  1.00 29.28 ? 75  GLU   B CB  1 
ATOM   2423 C CG  . GLU   B 1 96  ? -32.216 -5.024  -9.556  1.00 34.93 ? 75  GLU   B CG  1 
ATOM   2424 C CD  . GLU   B 1 96  ? -32.259 -6.068  -10.682 1.00 41.58 ? 75  GLU   B CD  1 
ATOM   2425 O OE1 . GLU   B 1 96  ? -32.653 -7.233  -10.410 1.00 43.16 ? 75  GLU   B OE1 1 
ATOM   2426 O OE2 . GLU   B 1 96  ? -31.872 -5.741  -11.832 1.00 43.14 ? 75  GLU   B OE2 1 
ATOM   2427 N N   . ILE   B 1 97  ? -28.960 -5.035  -7.418  1.00 26.14 ? 76  ILE   B N   1 
ATOM   2428 C CA  . ILE   B 1 97  ? -27.710 -4.388  -7.790  1.00 24.94 ? 76  ILE   B CA  1 
ATOM   2429 C C   . ILE   B 1 97  ? -26.699 -5.469  -8.182  1.00 24.92 ? 76  ILE   B C   1 
ATOM   2430 O O   . ILE   B 1 97  ? -25.997 -5.334  -9.198  1.00 24.91 ? 76  ILE   B O   1 
ATOM   2431 C CB  . ILE   B 1 97  ? -27.160 -3.471  -6.674  1.00 24.48 ? 76  ILE   B CB  1 
ATOM   2432 C CG1 . ILE   B 1 97  ? -28.080 -2.279  -6.412  1.00 24.82 ? 76  ILE   B CG1 1 
ATOM   2433 C CG2 . ILE   B 1 97  ? -25.749 -2.989  -7.022  1.00 25.78 ? 76  ILE   B CG2 1 
ATOM   2434 C CD1 . ILE   B 1 97  ? -27.817 -1.556  -5.091  1.00 24.41 ? 76  ILE   B CD1 1 
ATOM   2435 N N   . ILE   B 1 98  ? -26.565 -6.490  -7.325  1.00 23.19 ? 77  ILE   B N   1 
ATOM   2436 C CA  . ILE   B 1 98  ? -25.645 -7.580  -7.633  1.00 25.70 ? 77  ILE   B CA  1 
ATOM   2437 C C   . ILE   B 1 98  ? -26.109 -8.281  -8.916  1.00 27.87 ? 77  ILE   B C   1 
ATOM   2438 O O   . ILE   B 1 98  ? -25.288 -8.623  -9.786  1.00 22.99 ? 77  ILE   B O   1 
ATOM   2439 C CB  . ILE   B 1 98  ? -25.469 -8.558  -6.449  1.00 25.99 ? 77  ILE   B CB  1 
ATOM   2440 C CG1 . ILE   B 1 98  ? -24.901 -7.812  -5.202  1.00 26.58 ? 77  ILE   B CG1 1 
ATOM   2441 C CG2 . ILE   B 1 98  ? -24.586 -9.747  -6.852  1.00 23.37 ? 77  ILE   B CG2 1 
ATOM   2442 C CD1 . ILE   B 1 98  ? -23.547 -7.128  -5.425  1.00 24.50 ? 77  ILE   B CD1 1 
ATOM   2443 N N   . ASN   B 1 99  ? -27.425 -8.507  -9.007  1.00 26.34 ? 78  ASN   B N   1 
ATOM   2444 C CA  . ASN   B 1 99  ? -27.987 -9.169  -10.188 1.00 32.26 ? 78  ASN   B CA  1 
ATOM   2445 C C   . ASN   B 1 99  ? -27.588 -8.436  -11.481 1.00 28.48 ? 78  ASN   B C   1 
ATOM   2446 O O   . ASN   B 1 99  ? -27.257 -9.073  -12.468 1.00 28.26 ? 78  ASN   B O   1 
ATOM   2447 C CB  . ASN   B 1 99  ? -29.472 -9.480  -10.005 1.00 31.51 ? 78  ASN   B CB  1 
ATOM   2448 C CG  . ASN   B 1 99  ? -29.998 -10.272 -11.175 1.00 37.83 ? 78  ASN   B CG  1 
ATOM   2449 O OD1 . ASN   B 1 99  ? -29.511 -11.380 -11.434 1.00 38.27 ? 78  ASN   B OD1 1 
ATOM   2450 N ND2 . ASN   B 1 99  ? -30.958 -9.710  -11.898 1.00 33.96 ? 78  ASN   B ND2 1 
ATOM   2451 N N   . SER   B 1 100 ? -27.608 -7.095  -11.472 1.00 26.52 ? 79  SER   B N   1 
ATOM   2452 C CA  . SER   B 1 100 ? -27.308 -6.287  -12.639 1.00 26.29 ? 79  SER   B CA  1 
ATOM   2453 C C   . SER   B 1 100 ? -25.877 -6.498  -13.127 1.00 29.10 ? 79  SER   B C   1 
ATOM   2454 O O   . SER   B 1 100 ? -25.609 -6.319  -14.319 1.00 24.62 ? 79  SER   B O   1 
ATOM   2455 C CB  . SER   B 1 100 ? -27.507 -4.828  -12.371 1.00 28.60 ? 79  SER   B CB  1 
ATOM   2456 O OG  . SER   B 1 100 ? -28.892 -4.558  -12.249 1.00 32.80 ? 79  SER   B OG  1 
ATOM   2457 N N   . CYS   B 1 101 ? -24.951 -6.810  -12.210 1.00 22.16 ? 80  CYS   B N   1 
ATOM   2458 C CA  . CYS   B 1 101 ? -23.583 -7.132  -12.602 1.00 21.19 ? 80  CYS   B CA  1 
ATOM   2459 C C   . CYS   B 1 101 ? -23.532 -8.494  -13.305 1.00 23.40 ? 80  CYS   B C   1 
ATOM   2460 O O   . CYS   B 1 101 ? -22.780 -8.673  -14.280 1.00 22.07 ? 80  CYS   B O   1 
ATOM   2461 C CB  . CYS   B 1 101 ? -22.666 -7.157  -11.369 1.00 23.13 ? 80  CYS   B CB  1 
ATOM   2462 S SG  . CYS   B 1 101 ? -20.904 -7.065  -11.763 1.00 24.20 ? 80  CYS   B SG  1 
ATOM   2463 N N   . PHE   B 1 102 ? -24.278 -9.476  -12.776 1.00 22.67 ? 81  PHE   B N   1 
ATOM   2464 C CA  . PHE   B 1 102 ? -24.277 -10.793 -13.413 1.00 27.39 ? 81  PHE   B CA  1 
ATOM   2465 C C   . PHE   B 1 102 ? -24.967 -10.725 -14.788 1.00 28.43 ? 81  PHE   B C   1 
ATOM   2466 O O   . PHE   B 1 102 ? -24.476 -11.312 -15.750 1.00 30.77 ? 81  PHE   B O   1 
ATOM   2467 C CB  . PHE   B 1 102 ? -24.863 -11.921 -12.549 1.00 26.01 ? 81  PHE   B CB  1 
ATOM   2468 C CG  . PHE   B 1 102 ? -23.922 -12.389 -11.443 1.00 31.04 ? 81  PHE   B CG  1 
ATOM   2469 C CD1 . PHE   B 1 102 ? -23.883 -11.734 -10.206 1.00 29.50 ? 81  PHE   B CD1 1 
ATOM   2470 C CD2 . PHE   B 1 102 ? -23.057 -13.472 -11.650 1.00 32.45 ? 81  PHE   B CD2 1 
ATOM   2471 C CE1 . PHE   B 1 102 ? -23.001 -12.165 -9.215  1.00 30.27 ? 81  PHE   B CE1 1 
ATOM   2472 C CE2 . PHE   B 1 102 ? -22.168 -13.904 -10.655 1.00 30.81 ? 81  PHE   B CE2 1 
ATOM   2473 C CZ  . PHE   B 1 102 ? -22.138 -13.237 -9.443  1.00 30.82 ? 81  PHE   B CZ  1 
ATOM   2474 N N   . ARG   B 1 103 ? -26.099 -10.004 -14.870 1.00 29.70 ? 82  ARG   B N   1 
ATOM   2475 C CA  . ARG   B 1 103 ? -26.816 -9.784  -16.128 1.00 28.97 ? 82  ARG   B CA  1 
ATOM   2476 C C   . ARG   B 1 103 ? -25.876 -9.145  -17.151 1.00 30.35 ? 82  ARG   B C   1 
ATOM   2477 O O   . ARG   B 1 103 ? -25.787 -9.612  -18.281 1.00 31.66 ? 82  ARG   B O   1 
ATOM   2478 C CB  . ARG   B 1 103 ? -28.072 -8.921  -15.940 1.00 26.18 ? 82  ARG   B CB  1 
ATOM   2479 C CG  . ARG   B 1 103 ? -29.070 -8.866  -17.098 1.00 30.36 ? 82  ARG   B CG  1 
ATOM   2480 C CD  . ARG   B 1 103 ? -30.390 -8.205  -16.664 1.00 32.77 ? 82  ARG   B CD  1 
ATOM   2481 N NE  . ARG   B 1 103 ? -30.090 -6.836  -16.241 1.00 43.89 ? 82  ARG   B NE  1 
ATOM   2482 C CZ  . ARG   B 1 103 ? -30.395 -6.317  -15.046 1.00 44.27 ? 82  ARG   B CZ  1 
ATOM   2483 N NH1 . ARG   B 1 103 ? -31.024 -7.047  -14.129 1.00 42.02 ? 82  ARG   B NH1 1 
ATOM   2484 N NH2 . ARG   B 1 103 ? -30.092 -5.049  -14.810 1.00 39.73 ? 82  ARG   B NH2 1 
ATOM   2485 N N   . ALA   B 1 104 ? -25.179 -8.067  -16.773 1.00 25.35 ? 83  ALA   B N   1 
ATOM   2486 C CA  . ALA   B 1 104 ? -24.335 -7.355  -17.727 1.00 24.83 ? 83  ALA   B CA  1 
ATOM   2487 C C   . ALA   B 1 104 ? -23.100 -8.150  -18.111 1.00 28.61 ? 83  ALA   B C   1 
ATOM   2488 O O   . ALA   B 1 104 ? -22.709 -8.145  -19.278 1.00 27.38 ? 83  ALA   B O   1 
ATOM   2489 C CB  . ALA   B 1 104 ? -23.920 -6.006  -17.188 1.00 24.86 ? 83  ALA   B CB  1 
ATOM   2490 N N   . PHE   B 1 105 ? -22.459 -8.799  -17.134 1.00 27.07 ? 84  PHE   B N   1 
ATOM   2491 C CA  . PHE   B 1 105 ? -21.059 -9.160  -17.337 1.00 25.31 ? 84  PHE   B CA  1 
ATOM   2492 C C   . PHE   B 1 105 ? -20.845 -10.633 -17.010 1.00 25.38 ? 84  PHE   B C   1 
ATOM   2493 O O   . PHE   B 1 105 ? -19.766 -11.154 -17.246 1.00 26.82 ? 84  PHE   B O   1 
ATOM   2494 C CB  . PHE   B 1 105 ? -20.116 -8.282  -16.509 1.00 25.10 ? 84  PHE   B CB  1 
ATOM   2495 C CG  . PHE   B 1 105 ? -20.299 -6.786  -16.714 1.00 25.32 ? 84  PHE   B CG  1 
ATOM   2496 C CD1 . PHE   B 1 105 ? -20.262 -6.231  -17.997 1.00 24.15 ? 84  PHE   B CD1 1 
ATOM   2497 C CD2 . PHE   B 1 105 ? -20.548 -5.952  -15.613 1.00 21.83 ? 84  PHE   B CD2 1 
ATOM   2498 C CE1 . PHE   B 1 105 ? -20.459 -4.868  -18.179 1.00 26.18 ? 84  PHE   B CE1 1 
ATOM   2499 C CE2 . PHE   B 1 105 ? -20.728 -4.582  -15.795 1.00 25.00 ? 84  PHE   B CE2 1 
ATOM   2500 C CZ  . PHE   B 1 105 ? -20.706 -4.038  -17.074 1.00 24.86 ? 84  PHE   B CZ  1 
ATOM   2501 N N   . GLY   B 1 106 ? -21.860 -11.286 -16.449 1.00 27.21 ? 85  GLY   B N   1 
ATOM   2502 C CA  . GLY   B 1 106 ? -21.783 -12.728 -16.268 1.00 28.18 ? 85  GLY   B CA  1 
ATOM   2503 C C   . GLY   B 1 106 ? -20.988 -13.124 -15.021 1.00 29.94 ? 85  GLY   B C   1 
ATOM   2504 O O   . GLY   B 1 106 ? -20.819 -14.311 -14.749 1.00 27.74 ? 85  GLY   B O   1 
ATOM   2505 N N   . ARG   B 1 107 ? -20.529 -12.143 -14.233 1.00 24.99 ? 86  ARG   B N   1 
ATOM   2506 C CA  . ARG   B 1 107 ? -19.755 -12.458 -13.034 1.00 22.68 ? 86  ARG   B CA  1 
ATOM   2507 C C   . ARG   B 1 107 ? -19.696 -11.189 -12.183 1.00 25.40 ? 86  ARG   B C   1 
ATOM   2508 O O   . ARG   B 1 107 ? -20.094 -10.112 -12.652 1.00 23.97 ? 86  ARG   B O   1 
ATOM   2509 C CB  . ARG   B 1 107 ? -18.356 -12.947 -13.454 1.00 23.24 ? 86  ARG   B CB  1 
ATOM   2510 C CG  . ARG   B 1 107 ? -17.603 -11.829 -14.173 1.00 25.58 ? 86  ARG   B CG  1 
ATOM   2511 C CD  . ARG   B 1 107 ? -16.340 -12.359 -14.869 1.00 29.64 ? 86  ARG   B CD  1 
ATOM   2512 N NE  . ARG   B 1 107 ? -15.193 -12.452 -13.959 1.00 32.97 ? 86  ARG   B NE  1 
ATOM   2513 C CZ  . ARG   B 1 107 ? -14.013 -13.014 -14.227 1.00 35.48 ? 86  ARG   B CZ  1 
ATOM   2514 N NH1 . ARG   B 1 107 ? -13.752 -13.528 -15.420 1.00 33.00 ? 86  ARG   B NH1 1 
ATOM   2515 N NH2 . ARG   B 1 107 ? -13.097 -13.088 -13.287 1.00 33.24 ? 86  ARG   B NH2 1 
ATOM   2516 N N   . CYS   B 1 108 ? -19.202 -11.327 -10.935 1.00 24.25 ? 87  CYS   B N   1 
ATOM   2517 C CA  . CYS   B 1 108 ? -19.038 -10.181 -10.033 1.00 26.22 ? 87  CYS   B CA  1 
ATOM   2518 C C   . CYS   B 1 108 ? -17.863 -10.489 -9.103  1.00 24.19 ? 87  CYS   B C   1 
ATOM   2519 O O   . CYS   B 1 108 ? -17.976 -11.355 -8.220  1.00 25.64 ? 87  CYS   B O   1 
ATOM   2520 C CB  . CYS   B 1 108 ? -20.300 -9.921  -9.198  1.00 26.36 ? 87  CYS   B CB  1 
ATOM   2521 S SG  . CYS   B 1 108 ? -20.231 -8.356  -8.255  1.00 29.03 ? 87  CYS   B SG  1 
ATOM   2522 N N   . ASP   B 1 109 ? -16.715 -9.851  -9.387  1.00 23.86 ? 88  ASP   B N   1 
ATOM   2523 C CA  . ASP   B 1 109 ? -15.455 -10.168 -8.725  1.00 25.21 ? 88  ASP   B CA  1 
ATOM   2524 C C   . ASP   B 1 109 ? -15.242 -9.253  -7.520  1.00 25.76 ? 88  ASP   B C   1 
ATOM   2525 O O   . ASP   B 1 109 ? -14.602 -9.676  -6.559  1.00 25.43 ? 88  ASP   B O   1 
ATOM   2526 C CB  . ASP   B 1 109 ? -14.274 -10.039 -9.677  1.00 24.08 ? 88  ASP   B CB  1 
ATOM   2527 C CG  . ASP   B 1 109 ? -14.432 -10.979 -10.868 1.00 30.05 ? 88  ASP   B CG  1 
ATOM   2528 O OD1 . ASP   B 1 109 ? -14.149 -12.178 -10.718 1.00 28.36 ? 88  ASP   B OD1 1 
ATOM   2529 O OD2 . ASP   B 1 109 ? -15.016 -10.546 -11.862 1.00 29.61 ? 88  ASP   B OD2 1 
ATOM   2530 N N   . VAL   B 1 110 ? -15.747 -8.013  -7.606  1.00 22.76 ? 89  VAL   B N   1 
ATOM   2531 C CA  . VAL   B 1 110 ? -15.423 -6.969  -6.631  1.00 21.39 ? 89  VAL   B CA  1 
ATOM   2532 C C   . VAL   B 1 110 ? -16.701 -6.199  -6.295  1.00 22.16 ? 89  VAL   B C   1 
ATOM   2533 O O   . VAL   B 1 110 ? -17.463 -5.861  -7.198  1.00 19.58 ? 89  VAL   B O   1 
ATOM   2534 C CB  . VAL   B 1 110 ? -14.350 -6.033  -7.211  1.00 19.81 ? 89  VAL   B CB  1 
ATOM   2535 C CG1 . VAL   B 1 110 ? -14.196 -4.764  -6.374  1.00 19.96 ? 89  VAL   B CG1 1 
ATOM   2536 C CG2 . VAL   B 1 110 ? -12.989 -6.725  -7.345  1.00 20.41 ? 89  VAL   B CG2 1 
ATOM   2537 N N   . LEU   B 1 111 ? -16.912 -5.933  -4.997  1.00 20.15 ? 90  LEU   B N   1 
ATOM   2538 C CA  . LEU   B 1 111 ? -17.959 -5.053  -4.496  1.00 20.58 ? 90  LEU   B CA  1 
ATOM   2539 C C   . LEU   B 1 111 ? -17.257 -3.945  -3.715  1.00 21.00 ? 90  LEU   B C   1 
ATOM   2540 O O   . LEU   B 1 111 ? -16.464 -4.232  -2.808  1.00 21.85 ? 90  LEU   B O   1 
ATOM   2541 C CB  . LEU   B 1 111 ? -18.901 -5.878  -3.601  1.00 19.01 ? 90  LEU   B CB  1 
ATOM   2542 C CG  . LEU   B 1 111 ? -19.904 -5.087  -2.749  1.00 20.78 ? 90  LEU   B CG  1 
ATOM   2543 C CD1 . LEU   B 1 111 ? -20.839 -4.267  -3.642  1.00 21.15 ? 90  LEU   B CD1 1 
ATOM   2544 C CD2 . LEU   B 1 111 ? -20.722 -5.982  -1.804  1.00 20.31 ? 90  LEU   B CD2 1 
ATOM   2545 N N   . VAL   B 1 112 ? -17.575 -2.691  -4.046  1.00 17.90 ? 91  VAL   B N   1 
ATOM   2546 C CA  . VAL   B 1 112 ? -17.073 -1.543  -3.307  1.00 19.72 ? 91  VAL   B CA  1 
ATOM   2547 C C   . VAL   B 1 112 ? -18.281 -0.867  -2.670  1.00 20.43 ? 91  VAL   B C   1 
ATOM   2548 O O   . VAL   B 1 112 ? -19.123 -0.302  -3.383  1.00 22.43 ? 91  VAL   B O   1 
ATOM   2549 C CB  . VAL   B 1 112 ? -16.251 -0.545  -4.156  1.00 19.51 ? 91  VAL   B CB  1 
ATOM   2550 C CG1 . VAL   B 1 112 ? -15.694 0.581   -3.283  1.00 16.78 ? 91  VAL   B CG1 1 
ATOM   2551 C CG2 . VAL   B 1 112 ? -15.086 -1.229  -4.856  1.00 17.61 ? 91  VAL   B CG2 1 
ATOM   2552 N N   . ASN   B 1 113 ? -18.394 -0.994  -1.336  1.00 18.17 ? 92  ASN   B N   1 
ATOM   2553 C CA  . ASN   B 1 113 ? -19.445 -0.289  -0.604  1.00 17.86 ? 92  ASN   B CA  1 
ATOM   2554 C C   . ASN   B 1 113 ? -18.973 1.131   -0.306  1.00 21.58 ? 92  ASN   B C   1 
ATOM   2555 O O   . ASN   B 1 113 ? -18.309 1.370   0.710   1.00 22.55 ? 92  ASN   B O   1 
ATOM   2556 C CB  . ASN   B 1 113 ? -19.870 -1.003  0.679   1.00 18.31 ? 92  ASN   B CB  1 
ATOM   2557 C CG  . ASN   B 1 113 ? -20.600 -2.298  0.410   1.00 19.66 ? 92  ASN   B CG  1 
ATOM   2558 O OD1 . ASN   B 1 113 ? -21.622 -2.253  -0.286  1.00 23.87 ? 92  ASN   B OD1 1 
ATOM   2559 N ND2 . ASN   B 1 113 ? -20.084 -3.444  0.859   1.00 17.53 ? 92  ASN   B ND2 1 
ATOM   2560 N N   . ASN   B 1 114 ? -19.370 2.067   -1.166  1.00 20.10 ? 93  ASN   B N   1 
ATOM   2561 C CA  . ASN   B 1 114 ? -18.922 3.457   -1.153  1.00 19.87 ? 93  ASN   B CA  1 
ATOM   2562 C C   . ASN   B 1 114 ? -20.044 4.428   -0.786  1.00 21.69 ? 93  ASN   B C   1 
ATOM   2563 O O   . ASN   B 1 114 ? -19.771 5.493   -0.195  1.00 21.61 ? 93  ASN   B O   1 
ATOM   2564 C CB  . ASN   B 1 114 ? -18.218 3.831   -2.462  1.00 20.30 ? 93  ASN   B CB  1 
ATOM   2565 C CG  . ASN   B 1 114 ? -18.052 5.336   -2.600  1.00 23.20 ? 93  ASN   B CG  1 
ATOM   2566 O OD1 . ASN   B 1 114 ? -17.088 5.891   -2.073  1.00 23.50 ? 93  ASN   B OD1 1 
ATOM   2567 N ND2 . ASN   B 1 114 ? -18.964 6.023   -3.289  1.00 21.08 ? 93  ASN   B ND2 1 
ATOM   2568 N N   . ALA   B 1 115 ? -21.295 4.121   -1.198  1.00 22.71 ? 94  ALA   B N   1 
ATOM   2569 C CA  . ALA   B 1 115 ? -22.401 5.063   -0.994  1.00 24.54 ? 94  ALA   B CA  1 
ATOM   2570 C C   . ALA   B 1 115 ? -22.551 5.381   0.484   1.00 25.47 ? 94  ALA   B C   1 
ATOM   2571 O O   . ALA   B 1 115 ? -22.481 4.481   1.336   1.00 24.17 ? 94  ALA   B O   1 
ATOM   2572 C CB  . ALA   B 1 115 ? -23.719 4.509   -1.509  1.00 22.42 ? 94  ALA   B CB  1 
ATOM   2573 N N   . SER   B 1 116 ? -22.861 6.655   0.768   1.00 24.35 ? 95  SER   B N   1 
ATOM   2574 C CA  . SER   B 1 116 ? -22.933 7.079   2.152   1.00 27.56 ? 95  SER   B CA  1 
ATOM   2575 C C   . SER   B 1 116 ? -23.840 8.296   2.290   1.00 26.25 ? 95  SER   B C   1 
ATOM   2576 O O   . SER   B 1 116 ? -23.615 9.280   1.592   1.00 28.14 ? 95  SER   B O   1 
ATOM   2577 C CB  . SER   B 1 116 ? -21.532 7.416   2.637   1.00 28.08 ? 95  SER   B CB  1 
ATOM   2578 O OG  . SER   B 1 116 ? -21.596 7.876   3.983   1.00 30.39 ? 95  SER   B OG  1 
ATOM   2579 N N   . ALA   B 1 117 ? -24.828 8.233   3.204   1.00 26.05 ? 96  ALA   B N   1 
ATOM   2580 C CA  . ALA   B 1 117 ? -25.478 9.436   3.701   1.00 24.53 ? 96  ALA   B CA  1 
ATOM   2581 C C   . ALA   B 1 117 ? -24.658 10.039  4.852   1.00 24.31 ? 96  ALA   B C   1 
ATOM   2582 O O   . ALA   B 1 117 ? -24.145 9.297   5.698   1.00 25.78 ? 96  ALA   B O   1 
ATOM   2583 C CB  . ALA   B 1 117 ? -26.892 9.082   4.134   1.00 28.17 ? 96  ALA   B CB  1 
ATOM   2584 N N   . PHE   B 1 118 ? -24.603 11.381  4.919   1.00 23.59 ? 97  PHE   B N   1 
ATOM   2585 C CA  . PHE   B 1 118 ? -23.848 12.119  5.918   1.00 26.11 ? 97  PHE   B CA  1 
ATOM   2586 C C   . PHE   B 1 118 ? -24.579 13.421  6.232   1.00 28.24 ? 97  PHE   B C   1 
ATOM   2587 O O   . PHE   B 1 118 ? -24.709 14.258  5.358   1.00 28.00 ? 97  PHE   B O   1 
ATOM   2588 C CB  . PHE   B 1 118 ? -22.427 12.406  5.381   1.00 27.87 ? 97  PHE   B CB  1 
ATOM   2589 C CG  . PHE   B 1 118 ? -21.508 13.236  6.276   1.00 33.23 ? 97  PHE   B CG  1 
ATOM   2590 C CD1 . PHE   B 1 118 ? -20.816 12.650  7.347   1.00 33.73 ? 97  PHE   B CD1 1 
ATOM   2591 C CD2 . PHE   B 1 118 ? -21.331 14.611  6.046   1.00 35.96 ? 97  PHE   B CD2 1 
ATOM   2592 C CE1 . PHE   B 1 118 ? -19.987 13.405  8.171   1.00 31.06 ? 97  PHE   B CE1 1 
ATOM   2593 C CE2 . PHE   B 1 118 ? -20.495 15.372  6.862   1.00 34.44 ? 97  PHE   B CE2 1 
ATOM   2594 C CZ  . PHE   B 1 118 ? -19.817 14.763  7.922   1.00 36.33 ? 97  PHE   B CZ  1 
ATOM   2595 N N   . TYR   B 1 119 ? -25.037 13.585  7.480   1.00 25.22 ? 98  TYR   B N   1 
ATOM   2596 C CA  . TYR   B 1 119 ? -25.652 14.816  7.942   1.00 28.60 ? 98  TYR   B CA  1 
ATOM   2597 C C   . TYR   B 1 119 ? -25.855 14.689  9.451   1.00 27.13 ? 98  TYR   B C   1 
ATOM   2598 O O   . TYR   B 1 119 ? -25.911 13.567  9.977   1.00 26.28 ? 98  TYR   B O   1 
ATOM   2599 C CB  . TYR   B 1 119 ? -26.955 15.183  7.218   1.00 26.17 ? 98  TYR   B CB  1 
ATOM   2600 C CG  . TYR   B 1 119 ? -28.025 14.088  7.201   1.00 27.81 ? 98  TYR   B CG  1 
ATOM   2601 C CD1 . TYR   B 1 119 ? -28.912 13.922  8.265   1.00 27.16 ? 98  TYR   B CD1 1 
ATOM   2602 C CD2 . TYR   B 1 119 ? -28.201 13.260  6.090   1.00 27.77 ? 98  TYR   B CD2 1 
ATOM   2603 C CE1 . TYR   B 1 119 ? -29.904 12.939  8.243   1.00 30.18 ? 98  TYR   B CE1 1 
ATOM   2604 C CE2 . TYR   B 1 119 ? -29.174 12.266  6.066   1.00 28.39 ? 98  TYR   B CE2 1 
ATOM   2605 C CZ  . TYR   B 1 119 ? -30.048 12.114  7.131   1.00 28.29 ? 98  TYR   B CZ  1 
ATOM   2606 O OH  . TYR   B 1 119 ? -31.029 11.131  7.089   1.00 26.43 ? 98  TYR   B OH  1 
ATOM   2607 N N   . PRO   B 1 120 ? -25.956 15.824  10.181  1.00 29.22 ? 99  PRO   B N   1 
ATOM   2608 C CA  . PRO   B 1 120 ? -26.071 15.798  11.642  1.00 29.62 ? 99  PRO   B CA  1 
ATOM   2609 C C   . PRO   B 1 120 ? -27.410 15.210  12.060  1.00 28.42 ? 99  PRO   B C   1 
ATOM   2610 O O   . PRO   B 1 120 ? -28.398 15.391  11.359  1.00 29.04 ? 99  PRO   B O   1 
ATOM   2611 C CB  . PRO   B 1 120 ? -25.950 17.271  12.099  1.00 33.60 ? 99  PRO   B CB  1 
ATOM   2612 C CG  . PRO   B 1 120 ? -26.217 18.086  10.842  1.00 34.90 ? 99  PRO   B CG  1 
ATOM   2613 C CD  . PRO   B 1 120 ? -25.928 17.193  9.629   1.00 31.31 ? 99  PRO   B CD  1 
ATOM   2614 N N   . THR   B 1 121 ? -27.400 14.480  13.176  1.00 24.74 ? 100 THR   B N   1 
ATOM   2615 C CA  . THR   B 1 121 ? -28.588 13.966  13.852  1.00 23.35 ? 100 THR   B CA  1 
ATOM   2616 C C   . THR   B 1 121 ? -28.430 14.212  15.347  1.00 25.03 ? 100 THR   B C   1 
ATOM   2617 O O   . THR   B 1 121 ? -28.133 13.281  16.119  1.00 25.43 ? 100 THR   B O   1 
ATOM   2618 C CB  . THR   B 1 121 ? -28.784 12.476  13.573  1.00 26.63 ? 100 THR   B CB  1 
ATOM   2619 O OG1 . THR   B 1 121 ? -27.635 11.807  14.096  1.00 26.23 ? 100 THR   B OG1 1 
ATOM   2620 C CG2 . THR   B 1 121 ? -28.960 12.185  12.087  1.00 23.00 ? 100 THR   B CG2 1 
ATOM   2621 N N   . PRO   B 1 122 ? -28.660 15.464  15.797  1.00 27.16 ? 101 PRO   B N   1 
ATOM   2622 C CA  . PRO   B 1 122 ? -28.408 15.850  17.191  1.00 28.96 ? 101 PRO   B CA  1 
ATOM   2623 C C   . PRO   B 1 122 ? -29.234 14.976  18.131  1.00 30.24 ? 101 PRO   B C   1 
ATOM   2624 O O   . PRO   B 1 122 ? -30.367 14.614  17.796  1.00 29.74 ? 101 PRO   B O   1 
ATOM   2625 C CB  . PRO   B 1 122 ? -28.850 17.339  17.287  1.00 29.35 ? 101 PRO   B CB  1 
ATOM   2626 C CG  . PRO   B 1 122 ? -29.035 17.786  15.859  1.00 31.31 ? 101 PRO   B CG  1 
ATOM   2627 C CD  . PRO   B 1 122 ? -29.205 16.567  14.965  1.00 30.72 ? 101 PRO   B CD  1 
ATOM   2628 N N   . LEU   B 1 123 ? -28.682 14.651  19.313  1.00 24.68 ? 102 LEU   B N   1 
ATOM   2629 C CA  . LEU   B 1 123 ? -29.490 13.916  20.272  1.00 28.20 ? 102 LEU   B CA  1 
ATOM   2630 C C   . LEU   B 1 123 ? -30.500 14.847  20.963  1.00 36.08 ? 102 LEU   B C   1 
ATOM   2631 O O   . LEU   B 1 123 ? -31.509 14.369  21.470  1.00 33.28 ? 102 LEU   B O   1 
ATOM   2632 C CB  . LEU   B 1 123 ? -28.566 13.248  21.283  1.00 26.15 ? 102 LEU   B CB  1 
ATOM   2633 C CG  . LEU   B 1 123 ? -27.688 12.132  20.723  1.00 26.62 ? 102 LEU   B CG  1 
ATOM   2634 C CD1 . LEU   B 1 123 ? -26.557 11.862  21.747  1.00 27.64 ? 102 LEU   B CD1 1 
ATOM   2635 C CD2 . LEU   B 1 123 ? -28.543 10.922  20.559  1.00 24.72 ? 102 LEU   B CD2 1 
ATOM   2636 N N   . VAL   B 1 124 ? -30.205 16.161  21.010  1.00 37.45 ? 103 VAL   B N   1 
ATOM   2637 C CA  . VAL   B 1 124 ? -30.964 17.087  21.840  1.00 45.91 ? 103 VAL   B CA  1 
ATOM   2638 C C   . VAL   B 1 124 ? -31.760 18.069  20.959  1.00 53.36 ? 103 VAL   B C   1 
ATOM   2639 O O   . VAL   B 1 124 ? -31.122 18.754  20.130  1.00 54.13 ? 103 VAL   B O   1 
ATOM   2640 C CB  . VAL   B 1 124 ? -30.046 17.787  22.869  1.00 52.86 ? 103 VAL   B CB  1 
ATOM   2641 C CG1 . VAL   B 1 124 ? -30.649 19.073  23.426  1.00 60.55 ? 103 VAL   B CG1 1 
ATOM   2642 C CG2 . VAL   B 1 124 ? -29.683 16.852  24.019  1.00 50.41 ? 103 VAL   B CG2 1 
ATOM   2643 N N   . GLY   B 1 134 ? -34.805 18.238  8.598   1.00 65.60 ? 113 GLY   B N   1 
ATOM   2644 C CA  . GLY   B 1 134 ? -36.267 18.404  8.460   1.00 65.52 ? 113 GLY   B CA  1 
ATOM   2645 C C   . GLY   B 1 134 ? -36.984 17.055  8.392   1.00 58.94 ? 113 GLY   B C   1 
ATOM   2646 O O   . GLY   B 1 134 ? -38.196 17.005  8.195   1.00 64.70 ? 113 GLY   B O   1 
ATOM   2647 N N   . LYS   B 1 135 ? -36.209 15.977  8.576   1.00 48.68 ? 114 LYS   B N   1 
ATOM   2648 C CA  . LYS   B 1 135 ? -36.655 14.595  8.489   1.00 42.76 ? 114 LYS   B CA  1 
ATOM   2649 C C   . LYS   B 1 135 ? -37.033 14.060  9.868   1.00 37.99 ? 114 LYS   B C   1 
ATOM   2650 O O   . LYS   B 1 135 ? -36.511 14.502  10.890  1.00 37.80 ? 114 LYS   B O   1 
ATOM   2651 C CB  . LYS   B 1 135 ? -35.454 13.801  7.981   1.00 41.93 ? 114 LYS   B CB  1 
ATOM   2652 C CG  . LYS   B 1 135 ? -35.091 14.243  6.573   1.00 47.74 ? 114 LYS   B CG  1 
ATOM   2653 C CD  . LYS   B 1 135 ? -33.712 13.793  6.125   1.00 47.86 ? 114 LYS   B CD  1 
ATOM   2654 C CE  . LYS   B 1 135 ? -33.725 13.691  4.639   1.00 48.69 ? 114 LYS   B CE  1 
ATOM   2655 N NZ  . LYS   B 1 135 ? -32.362 13.450  4.182   1.00 50.29 ? 114 LYS   B NZ  1 
ATOM   2656 N N   . THR   B 1 136 ? -37.908 13.057  9.894   1.00 33.81 ? 115 THR   B N   1 
ATOM   2657 C CA  . THR   B 1 136 ? -38.205 12.441  11.169  1.00 35.03 ? 115 THR   B CA  1 
ATOM   2658 C C   . THR   B 1 136 ? -37.004 11.601  11.608  1.00 32.87 ? 115 THR   B C   1 
ATOM   2659 O O   . THR   B 1 136 ? -36.165 11.190  10.777  1.00 29.34 ? 115 THR   B O   1 
ATOM   2660 C CB  . THR   B 1 136 ? -39.468 11.592  11.065  1.00 34.32 ? 115 THR   B CB  1 
ATOM   2661 O OG1 . THR   B 1 136 ? -39.077 10.553  10.170  1.00 32.06 ? 115 THR   B OG1 1 
ATOM   2662 C CG2 . THR   B 1 136 ? -40.691 12.382  10.621  1.00 38.24 ? 115 THR   B CG2 1 
ATOM   2663 N N   . VAL   B 1 137 ? -36.991 11.301  12.917  1.00 27.66 ? 116 VAL   B N   1 
ATOM   2664 C CA  . VAL   B 1 137 ? -35.922 10.490  13.463  1.00 31.10 ? 116 VAL   B CA  1 
ATOM   2665 C C   . VAL   B 1 137 ? -35.923 9.139   12.748  1.00 29.99 ? 116 VAL   B C   1 
ATOM   2666 O O   . VAL   B 1 137 ? -34.848 8.641   12.409  1.00 26.35 ? 116 VAL   B O   1 
ATOM   2667 C CB  . VAL   B 1 137 ? -35.867 10.365  15.006  1.00 33.06 ? 116 VAL   B CB  1 
ATOM   2668 C CG1 . VAL   B 1 137 ? -37.002 9.526   15.568  1.00 38.73 ? 116 VAL   B CG1 1 
ATOM   2669 C CG2 . VAL   B 1 137 ? -34.552 9.754   15.473  1.00 32.91 ? 116 VAL   B CG2 1 
ATOM   2670 N N   . GLU   B 1 138 ? -37.124 8.558   12.465  1.00 28.12 ? 117 GLU   B N   1 
ATOM   2671 C CA  A GLU   B 1 138 ? -37.136 7.239   11.839  0.70 30.50 ? 117 GLU   B CA  1 
ATOM   2672 C CA  B GLU   B 1 138 ? -37.222 7.268   11.792  0.30 27.21 ? 117 GLU   B CA  1 
ATOM   2673 C C   . GLU   B 1 138 ? -36.512 7.291   10.441  1.00 27.15 ? 117 GLU   B C   1 
ATOM   2674 O O   . GLU   B 1 138 ? -35.908 6.288   10.022  1.00 28.63 ? 117 GLU   B O   1 
ATOM   2675 C CB  A GLU   B 1 138 ? -38.418 6.405   11.972  0.70 33.64 ? 117 GLU   B CB  1 
ATOM   2676 C CB  B GLU   B 1 138 ? -38.645 6.834   11.425  0.30 25.10 ? 117 GLU   B CB  1 
ATOM   2677 C CG  A GLU   B 1 138 ? -39.682 7.139   11.540  0.70 36.30 ? 117 GLU   B CG  1 
ATOM   2678 C CG  B GLU   B 1 138 ? -39.610 6.812   12.603  0.30 23.97 ? 117 GLU   B CG  1 
ATOM   2679 C CD  A GLU   B 1 138 ? -40.172 8.154   12.567  0.70 40.33 ? 117 GLU   B CD  1 
ATOM   2680 C CD  B GLU   B 1 138 ? -40.342 8.139   12.673  0.30 22.38 ? 117 GLU   B CD  1 
ATOM   2681 O OE1 A GLU   B 1 138 ? -41.007 8.983   12.175  0.70 42.22 ? 117 GLU   B OE1 1 
ATOM   2682 O OE1 B GLU   B 1 138 ? -41.336 8.283   11.930  0.30 20.49 ? 117 GLU   B OE1 1 
ATOM   2683 O OE2 A GLU   B 1 138 ? -39.734 8.145   13.742  0.70 45.24 ? 117 GLU   B OE2 1 
ATOM   2684 O OE2 B GLU   B 1 138 ? -39.897 9.028   13.429  0.30 21.55 ? 117 GLU   B OE2 1 
ATOM   2685 N N   . THR   B 1 139 ? -36.599 8.443   9.764   1.00 26.75 ? 118 THR   B N   1 
ATOM   2686 C CA  . THR   B 1 139 ? -36.005 8.649   8.438   1.00 27.68 ? 118 THR   B CA  1 
ATOM   2687 C C   . THR   B 1 139 ? -34.478 8.763   8.545   1.00 27.71 ? 118 THR   B C   1 
ATOM   2688 O O   . THR   B 1 139 ? -33.749 8.180   7.728   1.00 25.88 ? 118 THR   B O   1 
ATOM   2689 C CB  . THR   B 1 139 ? -36.591 9.898   7.759   1.00 30.25 ? 118 THR   B CB  1 
ATOM   2690 O OG1 . THR   B 1 139 ? -37.950 9.604   7.481   1.00 30.83 ? 118 THR   B OG1 1 
ATOM   2691 C CG2 . THR   B 1 139 ? -36.005 10.196  6.390   1.00 29.76 ? 118 THR   B CG2 1 
ATOM   2692 N N   . GLN   B 1 140 ? -34.013 9.563   9.525   1.00 26.21 ? 119 GLN   B N   1 
ATOM   2693 C CA  . GLN   B 1 140 ? -32.587 9.675   9.829   1.00 23.80 ? 119 GLN   B CA  1 
ATOM   2694 C C   . GLN   B 1 140 ? -31.993 8.275   10.070  1.00 24.22 ? 119 GLN   B C   1 
ATOM   2695 O O   . GLN   B 1 140 ? -30.966 7.910   9.483   1.00 25.10 ? 119 GLN   B O   1 
ATOM   2696 C CB  . GLN   B 1 140 ? -32.437 10.563  11.060  1.00 26.85 ? 119 GLN   B CB  1 
ATOM   2697 C CG  . GLN   B 1 140 ? -32.793 12.034  10.832  1.00 27.59 ? 119 GLN   B CG  1 
ATOM   2698 C CD  . GLN   B 1 140 ? -32.906 12.789  12.140  1.00 33.67 ? 119 GLN   B CD  1 
ATOM   2699 O OE1 . GLN   B 1 140 ? -32.175 12.539  13.105  1.00 39.44 ? 119 GLN   B OE1 1 
ATOM   2700 N NE2 . GLN   B 1 140 ? -33.886 13.674  12.239  1.00 39.64 ? 119 GLN   B NE2 1 
ATOM   2701 N N   . VAL   B 1 141 ? -32.635 7.495   10.951  1.00 21.22 ? 120 VAL   B N   1 
ATOM   2702 C CA  . VAL   B 1 141 ? -32.166 6.144   11.225  1.00 21.81 ? 120 VAL   B CA  1 
ATOM   2703 C C   . VAL   B 1 141 ? -32.093 5.368   9.913   1.00 22.67 ? 120 VAL   B C   1 
ATOM   2704 O O   . VAL   B 1 141 ? -31.057 4.766   9.582   1.00 21.15 ? 120 VAL   B O   1 
ATOM   2705 C CB  . VAL   B 1 141 ? -33.044 5.420   12.258  1.00 21.50 ? 120 VAL   B CB  1 
ATOM   2706 C CG1 . VAL   B 1 141 ? -32.714 3.916   12.343  1.00 22.24 ? 120 VAL   B CG1 1 
ATOM   2707 C CG2 . VAL   B 1 141 ? -32.997 6.105   13.634  1.00 20.96 ? 120 VAL   B CG2 1 
ATOM   2708 N N   . ALA   B 1 142 ? -33.216 5.368   9.175   1.00 22.40 ? 121 ALA   B N   1 
ATOM   2709 C CA  . ALA   B 1 142 ? -33.311 4.576   7.950   1.00 22.23 ? 121 ALA   B CA  1 
ATOM   2710 C C   . ALA   B 1 142 ? -32.238 4.992   6.941   1.00 22.18 ? 121 ALA   B C   1 
ATOM   2711 O O   . ALA   B 1 142 ? -31.570 4.150   6.362   1.00 21.16 ? 121 ALA   B O   1 
ATOM   2712 C CB  . ALA   B 1 142 ? -34.745 4.623   7.369   1.00 22.77 ? 121 ALA   B CB  1 
ATOM   2713 N N   . GLU   B 1 143 ? -32.014 6.296   6.738   1.00 21.54 ? 122 GLU   B N   1 
ATOM   2714 C CA  . GLU   B 1 143 ? -31.039 6.674   5.722   1.00 23.13 ? 122 GLU   B CA  1 
ATOM   2715 C C   . GLU   B 1 143 ? -29.582 6.461   6.176   1.00 24.57 ? 122 GLU   B C   1 
ATOM   2716 O O   . GLU   B 1 143 ? -28.717 6.013   5.402   1.00 24.58 ? 122 GLU   B O   1 
ATOM   2717 C CB  . GLU   B 1 143 ? -31.236 8.166   5.439   1.00 23.20 ? 122 GLU   B CB  1 
ATOM   2718 C CG  . GLU   B 1 143 ? -32.571 8.437   4.739   1.00 25.73 ? 122 GLU   B CG  1 
ATOM   2719 C CD  . GLU   B 1 143 ? -32.729 9.903   4.351   1.00 31.47 ? 122 GLU   B CD  1 
ATOM   2720 O OE1 . GLU   B 1 143 ? -31.923 10.751  4.785   1.00 29.09 ? 122 GLU   B OE1 1 
ATOM   2721 O OE2 . GLU   B 1 143 ? -33.683 10.207  3.614   1.00 30.94 ? 122 GLU   B OE2 1 
ATOM   2722 N N   . LEU   B 1 144 ? -29.273 6.808   7.433   1.00 23.64 ? 123 LEU   B N   1 
ATOM   2723 C CA  . LEU   B 1 144 ? -27.877 6.774   7.841   1.00 22.71 ? 123 LEU   B CA  1 
ATOM   2724 C C   . LEU   B 1 144 ? -27.431 5.354   8.145   1.00 22.37 ? 123 LEU   B C   1 
ATOM   2725 O O   . LEU   B 1 144 ? -26.294 5.025   7.823   1.00 24.28 ? 123 LEU   B O   1 
ATOM   2726 C CB  . LEU   B 1 144 ? -27.626 7.753   8.987   1.00 25.05 ? 123 LEU   B CB  1 
ATOM   2727 C CG  . LEU   B 1 144 ? -27.807 9.227   8.586   1.00 25.30 ? 123 LEU   B CG  1 
ATOM   2728 C CD1 . LEU   B 1 144 ? -27.948 10.130  9.781   1.00 29.28 ? 123 LEU   B CD1 1 
ATOM   2729 C CD2 . LEU   B 1 144 ? -26.590 9.697   7.780   1.00 29.82 ? 123 LEU   B CD2 1 
ATOM   2730 N N   . ILE   B 1 145 ? -28.301 4.544   8.769   1.00 20.07 ? 124 ILE   B N   1 
ATOM   2731 C CA  . ILE   B 1 145 ? -27.921 3.173   9.075   1.00 21.85 ? 124 ILE   B CA  1 
ATOM   2732 C C   . ILE   B 1 145 ? -28.061 2.278   7.837   1.00 21.97 ? 124 ILE   B C   1 
ATOM   2733 O O   . ILE   B 1 145 ? -27.210 1.408   7.572   1.00 26.37 ? 124 ILE   B O   1 
ATOM   2734 C CB  . ILE   B 1 145 ? -28.664 2.643   10.308  1.00 21.53 ? 124 ILE   B CB  1 
ATOM   2735 C CG1 . ILE   B 1 145 ? -28.490 3.603   11.540  1.00 22.21 ? 124 ILE   B CG1 1 
ATOM   2736 C CG2 . ILE   B 1 145 ? -28.252 1.197   10.632  1.00 21.79 ? 124 ILE   B CG2 1 
ATOM   2737 C CD1 . ILE   B 1 145 ? -27.055 3.829   11.976  1.00 24.24 ? 124 ILE   B CD1 1 
ATOM   2738 N N   . GLY   B 1 146 ? -29.113 2.505   7.048   1.00 23.21 ? 125 GLY   B N   1 
ATOM   2739 C CA  . GLY   B 1 146 ? -29.280 1.843   5.743   1.00 21.05 ? 125 GLY   B CA  1 
ATOM   2740 C C   . GLY   B 1 146 ? -28.063 1.985   4.825   1.00 20.82 ? 125 GLY   B C   1 
ATOM   2741 O O   . GLY   B 1 146 ? -27.465 0.968   4.440   1.00 22.37 ? 125 GLY   B O   1 
ATOM   2742 N N   . THR   B 1 147 ? -27.685 3.229   4.467   1.00 18.80 ? 126 THR   B N   1 
ATOM   2743 C CA  . THR   B 1 147 ? -26.665 3.431   3.434   1.00 21.84 ? 126 THR   B CA  1 
ATOM   2744 C C   . THR   B 1 147 ? -25.296 2.984   3.947   1.00 25.56 ? 126 THR   B C   1 
ATOM   2745 O O   . THR   B 1 147 ? -24.543 2.359   3.206   1.00 25.55 ? 126 THR   B O   1 
ATOM   2746 C CB  . THR   B 1 147 ? -26.546 4.892   2.952   1.00 25.57 ? 126 THR   B CB  1 
ATOM   2747 O OG1 . THR   B 1 147 ? -26.241 5.650   4.114   1.00 29.22 ? 126 THR   B OG1 1 
ATOM   2748 C CG2 . THR   B 1 147 ? -27.838 5.455   2.367   1.00 23.91 ? 126 THR   B CG2 1 
ATOM   2749 N N   . ASN   B 1 148 ? -24.989 3.308   5.222   1.00 24.45 ? 127 ASN   B N   1 
ATOM   2750 C CA  . ASN   B 1 148 ? -23.645 3.117   5.756   1.00 22.79 ? 127 ASN   B CA  1 
ATOM   2751 C C   . ASN   B 1 148 ? -23.395 1.686   6.239   1.00 23.97 ? 127 ASN   B C   1 
ATOM   2752 O O   . ASN   B 1 148 ? -22.243 1.272   6.348   1.00 25.01 ? 127 ASN   B O   1 
ATOM   2753 C CB  . ASN   B 1 148 ? -23.318 4.170   6.802   1.00 21.27 ? 127 ASN   B CB  1 
ATOM   2754 C CG  . ASN   B 1 148 ? -23.182 5.551   6.203   1.00 25.77 ? 127 ASN   B CG  1 
ATOM   2755 O OD1 . ASN   B 1 148 ? -22.272 5.792   5.409   1.00 31.77 ? 127 ASN   B OD1 1 
ATOM   2756 N ND2 . ASN   B 1 148 ? -23.995 6.499   6.616   1.00 23.88 ? 127 ASN   B ND2 1 
ATOM   2757 N N   . ALA   B 1 149 ? -24.442 0.922   6.551   1.00 22.41 ? 128 ALA   B N   1 
ATOM   2758 C CA  . ALA   B 1 149 ? -24.218 -0.372  7.183   1.00 21.54 ? 128 ALA   B CA  1 
ATOM   2759 C C   . ALA   B 1 149 ? -25.138 -1.461  6.642   1.00 20.83 ? 128 ALA   B C   1 
ATOM   2760 O O   . ALA   B 1 149 ? -24.662 -2.551  6.329   1.00 23.12 ? 128 ALA   B O   1 
ATOM   2761 C CB  . ALA   B 1 149 ? -24.380 -0.287  8.707   1.00 23.14 ? 128 ALA   B CB  1 
ATOM   2762 N N   . ILE   B 1 150 ? -26.455 -1.245  6.736   1.00 20.18 ? 129 ILE   B N   1 
ATOM   2763 C CA  . ILE   B 1 150 ? -27.368 -2.324  6.358   1.00 21.42 ? 129 ILE   B CA  1 
ATOM   2764 C C   . ILE   B 1 150 ? -27.240 -2.705  4.865   1.00 20.58 ? 129 ILE   B C   1 
ATOM   2765 O O   . ILE   B 1 150 ? -27.189 -3.886  4.508   1.00 21.38 ? 129 ILE   B O   1 
ATOM   2766 C CB  . ILE   B 1 150 ? -28.825 -2.017  6.778   1.00 20.76 ? 129 ILE   B CB  1 
ATOM   2767 C CG1 . ILE   B 1 150 ? -28.925 -1.795  8.317   1.00 22.71 ? 129 ILE   B CG1 1 
ATOM   2768 C CG2 . ILE   B 1 150 ? -29.669 -3.221  6.345   1.00 22.63 ? 129 ILE   B CG2 1 
ATOM   2769 C CD1 . ILE   B 1 150 ? -30.282 -1.335  8.853   1.00 22.78 ? 129 ILE   B CD1 1 
ATOM   2770 N N   . ALA   B 1 151 ? -27.231 -1.713  3.982   1.00 20.33 ? 130 ALA   B N   1 
ATOM   2771 C CA  . ALA   B 1 151 ? -27.074 -2.001  2.562   1.00 22.16 ? 130 ALA   B CA  1 
ATOM   2772 C C   . ALA   B 1 151 ? -25.740 -2.722  2.313   1.00 21.71 ? 130 ALA   B C   1 
ATOM   2773 O O   . ALA   B 1 151 ? -25.709 -3.764  1.626   1.00 22.39 ? 130 ALA   B O   1 
ATOM   2774 C CB  . ALA   B 1 151 ? -27.296 -0.742  1.709   1.00 20.85 ? 130 ALA   B CB  1 
ATOM   2775 N N   . PRO   B 1 152 ? -24.579 -2.256  2.857   1.00 21.50 ? 131 PRO   B N   1 
ATOM   2776 C CA  . PRO   B 1 152 ? -23.349 -3.052  2.770   1.00 20.51 ? 131 PRO   B CA  1 
ATOM   2777 C C   . PRO   B 1 152 ? -23.500 -4.520  3.172   1.00 21.18 ? 131 PRO   B C   1 
ATOM   2778 O O   . PRO   B 1 152 ? -22.979 -5.380  2.468   1.00 20.86 ? 131 PRO   B O   1 
ATOM   2779 C CB  . PRO   B 1 152 ? -22.389 -2.239  3.682   1.00 22.28 ? 131 PRO   B CB  1 
ATOM   2780 C CG  . PRO   B 1 152 ? -22.764 -0.791  3.340   1.00 20.10 ? 131 PRO   B CG  1 
ATOM   2781 C CD  . PRO   B 1 152 ? -24.306 -0.895  3.358   1.00 20.79 ? 131 PRO   B CD  1 
ATOM   2782 N N   . PHE   B 1 153 ? -24.224 -4.789  4.281   1.00 19.83 ? 132 PHE   B N   1 
ATOM   2783 C CA  . PHE   B 1 153 ? -24.439 -6.157  4.744   1.00 21.14 ? 132 PHE   B CA  1 
ATOM   2784 C C   . PHE   B 1 153 ? -25.212 -6.954  3.680   1.00 20.20 ? 132 PHE   B C   1 
ATOM   2785 O O   . PHE   B 1 153 ? -24.811 -8.080  3.325   1.00 20.76 ? 132 PHE   B O   1 
ATOM   2786 C CB  . PHE   B 1 153 ? -25.078 -6.151  6.145   1.00 22.98 ? 132 PHE   B CB  1 
ATOM   2787 C CG  . PHE   B 1 153 ? -25.732 -7.477  6.511   1.00 20.78 ? 132 PHE   B CG  1 
ATOM   2788 C CD1 . PHE   B 1 153 ? -24.983 -8.518  7.065   1.00 22.16 ? 132 PHE   B CD1 1 
ATOM   2789 C CD2 . PHE   B 1 153 ? -27.093 -7.672  6.277   1.00 23.59 ? 132 PHE   B CD2 1 
ATOM   2790 C CE1 . PHE   B 1 153 ? -25.580 -9.746  7.353   1.00 22.80 ? 132 PHE   B CE1 1 
ATOM   2791 C CE2 . PHE   B 1 153 ? -27.689 -8.895  6.558   1.00 21.83 ? 132 PHE   B CE2 1 
ATOM   2792 C CZ  . PHE   B 1 153 ? -26.932 -9.929  7.100   1.00 23.52 ? 132 PHE   B CZ  1 
ATOM   2793 N N   . LEU   B 1 154 ? -26.308 -6.363  3.191   1.00 18.53 ? 133 LEU   B N   1 
ATOM   2794 C CA  . LEU   B 1 154 ? -27.199 -7.009  2.229   1.00 21.62 ? 133 LEU   B CA  1 
ATOM   2795 C C   . LEU   B 1 154 ? -26.500 -7.227  0.886   1.00 21.54 ? 133 LEU   B C   1 
ATOM   2796 O O   . LEU   B 1 154 ? -26.598 -8.304  0.315   1.00 22.18 ? 133 LEU   B O   1 
ATOM   2797 C CB  . LEU   B 1 154 ? -28.496 -6.228  2.060   1.00 21.80 ? 133 LEU   B CB  1 
ATOM   2798 C CG  . LEU   B 1 154 ? -29.360 -6.174  3.328   1.00 24.52 ? 133 LEU   B CG  1 
ATOM   2799 C CD1 . LEU   B 1 154 ? -30.413 -5.080  3.171   1.00 21.26 ? 133 LEU   B CD1 1 
ATOM   2800 C CD2 . LEU   B 1 154 ? -29.991 -7.538  3.627   1.00 24.59 ? 133 LEU   B CD2 1 
ATOM   2801 N N   . LEU   B 1 155 ? -25.749 -6.229  0.412   1.00 22.57 ? 134 LEU   B N   1 
ATOM   2802 C CA  . LEU   B 1 155 ? -24.913 -6.425  -0.769  1.00 22.81 ? 134 LEU   B CA  1 
ATOM   2803 C C   . LEU   B 1 155 ? -23.863 -7.530  -0.589  1.00 24.56 ? 134 LEU   B C   1 
ATOM   2804 O O   . LEU   B 1 155 ? -23.585 -8.301  -1.528  1.00 21.19 ? 134 LEU   B O   1 
ATOM   2805 C CB  . LEU   B 1 155 ? -24.293 -5.077  -1.140  1.00 22.76 ? 134 LEU   B CB  1 
ATOM   2806 C CG  . LEU   B 1 155 ? -25.292 -4.017  -1.635  1.00 21.35 ? 134 LEU   B CG  1 
ATOM   2807 C CD1 . LEU   B 1 155 ? -24.691 -2.606  -1.553  1.00 21.41 ? 134 LEU   B CD1 1 
ATOM   2808 C CD2 . LEU   B 1 155 ? -25.681 -4.316  -3.108  1.00 22.22 ? 134 LEU   B CD2 1 
ATOM   2809 N N   . THR   B 1 156 ? -23.238 -7.591  0.609   1.00 23.07 ? 135 THR   B N   1 
ATOM   2810 C CA  . THR   B 1 156 ? -22.210 -8.595  0.890   1.00 21.09 ? 135 THR   B CA  1 
ATOM   2811 C C   . THR   B 1 156 ? -22.865 -9.969  0.798   1.00 22.30 ? 135 THR   B C   1 
ATOM   2812 O O   . THR   B 1 156 ? -22.258 -10.875 0.252   1.00 21.30 ? 135 THR   B O   1 
ATOM   2813 C CB  . THR   B 1 156 ? -21.572 -8.389  2.276   1.00 21.24 ? 135 THR   B CB  1 
ATOM   2814 O OG1 . THR   B 1 156 ? -20.936 -7.099  2.237   1.00 21.07 ? 135 THR   B OG1 1 
ATOM   2815 C CG2 . THR   B 1 156 ? -20.557 -9.476  2.633   1.00 20.22 ? 135 THR   B CG2 1 
ATOM   2816 N N   . MET   B 1 157 ? -24.074 -10.101 1.379   1.00 23.41 ? 136 MET   B N   1 
ATOM   2817 C CA  . MET   B 1 157 ? -24.813 -11.352 1.369   1.00 24.90 ? 136 MET   B CA  1 
ATOM   2818 C C   . MET   B 1 157 ? -25.093 -11.788 -0.075  1.00 26.10 ? 136 MET   B C   1 
ATOM   2819 O O   . MET   B 1 157 ? -24.862 -12.945 -0.414  1.00 23.72 ? 136 MET   B O   1 
ATOM   2820 C CB  . MET   B 1 157 ? -26.136 -11.193 2.147   1.00 25.82 ? 136 MET   B CB  1 
ATOM   2821 C CG  . MET   B 1 157 ? -27.009 -12.435 2.180   1.00 36.32 ? 136 MET   B CG  1 
ATOM   2822 S SD  . MET   B 1 157 ? -28.302 -12.392 3.444   1.00 44.04 ? 136 MET   B SD  1 
ATOM   2823 C CE  . MET   B 1 157 ? -27.859 -10.897 4.307   1.00 32.53 ? 136 MET   B CE  1 
ATOM   2824 N N   . SER   B 1 158 ? -25.614 -10.873 -0.907  1.00 24.11 ? 137 SER   B N   1 
ATOM   2825 C CA  . SER   B 1 158 ? -25.972 -11.209 -2.286  1.00 24.74 ? 137 SER   B CA  1 
ATOM   2826 C C   . SER   B 1 158 ? -24.697 -11.483 -3.075  1.00 26.91 ? 137 SER   B C   1 
ATOM   2827 O O   . SER   B 1 158 ? -24.631 -12.427 -3.858  1.00 26.86 ? 137 SER   B O   1 
ATOM   2828 C CB  . SER   B 1 158 ? -26.769 -10.123 -2.928  1.00 25.02 ? 137 SER   B CB  1 
ATOM   2829 O OG  . SER   B 1 158 ? -28.022 -10.016 -2.256  1.00 31.05 ? 137 SER   B OG  1 
ATOM   2830 N N   . PHE   B 1 159 ? -23.662 -10.675 -2.817  1.00 22.97 ? 138 PHE   B N   1 
ATOM   2831 C CA  . PHE   B 1 159 ? -22.370 -10.901 -3.452  1.00 21.54 ? 138 PHE   B CA  1 
ATOM   2832 C C   . PHE   B 1 159 ? -21.901 -12.326 -3.189  1.00 23.41 ? 138 PHE   B C   1 
ATOM   2833 O O   . PHE   B 1 159 ? -21.533 -13.018 -4.128  1.00 26.35 ? 138 PHE   B O   1 
ATOM   2834 C CB  . PHE   B 1 159 ? -21.311 -9.872  -3.029  1.00 21.15 ? 138 PHE   B CB  1 
ATOM   2835 C CG  . PHE   B 1 159 ? -19.917 -10.071 -3.615  1.00 20.81 ? 138 PHE   B CG  1 
ATOM   2836 C CD1 . PHE   B 1 159 ? -18.995 -10.929 -3.004  1.00 22.46 ? 138 PHE   B CD1 1 
ATOM   2837 C CD2 . PHE   B 1 159 ? -19.542 -9.428  -4.784  1.00 21.87 ? 138 PHE   B CD2 1 
ATOM   2838 C CE1 . PHE   B 1 159 ? -17.714 -11.091 -3.529  1.00 24.50 ? 138 PHE   B CE1 1 
ATOM   2839 C CE2 . PHE   B 1 159 ? -18.261 -9.593  -5.322  1.00 21.16 ? 138 PHE   B CE2 1 
ATOM   2840 C CZ  . PHE   B 1 159 ? -17.357 -10.420 -4.698  1.00 22.60 ? 138 PHE   B CZ  1 
ATOM   2841 N N   . ALA   B 1 160 ? -21.867 -12.734 -1.917  1.00 22.73 ? 139 ALA   B N   1 
ATOM   2842 C CA  . ALA   B 1 160 ? -21.303 -14.028 -1.557  1.00 25.92 ? 139 ALA   B CA  1 
ATOM   2843 C C   . ALA   B 1 160 ? -22.141 -15.168 -2.137  1.00 27.53 ? 139 ALA   B C   1 
ATOM   2844 O O   . ALA   B 1 160 ? -21.598 -16.162 -2.649  1.00 26.65 ? 139 ALA   B O   1 
ATOM   2845 C CB  . ALA   B 1 160 ? -21.231 -14.146 -0.054  1.00 25.32 ? 139 ALA   B CB  1 
ATOM   2846 N N   . GLN   B 1 161 ? -23.464 -15.013 -2.040  1.00 27.98 ? 140 GLN   B N   1 
ATOM   2847 C CA  . GLN   B 1 161 ? -24.353 -16.112 -2.403  1.00 31.30 ? 140 GLN   B CA  1 
ATOM   2848 C C   . GLN   B 1 161 ? -24.324 -16.381 -3.906  1.00 33.14 ? 140 GLN   B C   1 
ATOM   2849 O O   . GLN   B 1 161 ? -24.489 -17.526 -4.319  1.00 32.37 ? 140 GLN   B O   1 
ATOM   2850 C CB  . GLN   B 1 161 ? -25.789 -15.831 -1.984  1.00 29.34 ? 140 GLN   B CB  1 
ATOM   2851 C CG  . GLN   B 1 161 ? -25.978 -16.134 -0.499  1.00 41.20 ? 140 GLN   B CG  1 
ATOM   2852 C CD  . GLN   B 1 161 ? -27.258 -15.577 0.082   0.60 42.03 ? 140 GLN   B CD  1 
ATOM   2853 O OE1 . GLN   B 1 161 ? -27.415 -15.514 1.307   0.60 40.36 ? 140 GLN   B OE1 1 
ATOM   2854 N NE2 . GLN   B 1 161 ? -28.160 -15.141 -0.789  0.60 37.38 ? 140 GLN   B NE2 1 
ATOM   2855 N N   . ARG   B 1 162 ? -24.137 -15.325 -4.705  1.00 29.63 ? 141 ARG   B N   1 
ATOM   2856 C CA  . ARG   B 1 162 ? -24.178 -15.453 -6.159  1.00 34.46 ? 141 ARG   B CA  1 
ATOM   2857 C C   . ARG   B 1 162 ? -22.874 -16.039 -6.708  1.00 35.48 ? 141 ARG   B C   1 
ATOM   2858 O O   . ARG   B 1 162 ? -22.780 -16.328 -7.891  1.00 39.49 ? 141 ARG   B O   1 
ATOM   2859 C CB  . ARG   B 1 162 ? -24.462 -14.102 -6.829  1.00 31.44 ? 141 ARG   B CB  1 
ATOM   2860 C CG  . ARG   B 1 162 ? -25.822 -13.471 -6.569  1.00 37.91 ? 141 ARG   B CG  1 
ATOM   2861 C CD  . ARG   B 1 162 ? -27.041 -14.214 -7.095  1.00 44.91 ? 141 ARG   B CD  1 
ATOM   2862 N NE  . ARG   B 1 162 ? -26.956 -14.293 -8.558  1.00 49.40 ? 141 ARG   B NE  1 
ATOM   2863 C CZ  . ARG   B 1 162 ? -27.553 -13.451 -9.412  1.00 47.17 ? 141 ARG   B CZ  1 
ATOM   2864 N NH1 . ARG   B 1 162 ? -28.332 -12.459 -8.985  1.00 46.45 ? 141 ARG   B NH1 1 
ATOM   2865 N NH2 . ARG   B 1 162 ? -27.348 -13.604 -10.703 1.00 44.47 ? 141 ARG   B NH2 1 
ATOM   2866 N N   . GLN   B 1 163 ? -21.856 -16.226 -5.871  1.00 36.61 ? 142 GLN   B N   1 
ATOM   2867 C CA  . GLN   B 1 163 ? -20.595 -16.745 -6.386  1.00 41.25 ? 142 GLN   B CA  1 
ATOM   2868 C C   . GLN   B 1 163 ? -20.830 -18.123 -7.012  1.00 53.74 ? 142 GLN   B C   1 
ATOM   2869 O O   . GLN   B 1 163 ? -21.423 -19.001 -6.387  1.00 50.64 ? 142 GLN   B O   1 
ATOM   2870 C CB  . GLN   B 1 163 ? -19.419 -16.622 -5.403  1.00 34.69 ? 142 GLN   B CB  1 
ATOM   2871 C CG  . GLN   B 1 163 ? -19.056 -15.179 -5.048  1.00 30.76 ? 142 GLN   B CG  1 
ATOM   2872 C CD  . GLN   B 1 163 ? -18.807 -14.286 -6.256  1.00 31.34 ? 142 GLN   B CD  1 
ATOM   2873 O OE1 . GLN   B 1 163 ? -18.174 -14.694 -7.236  1.00 31.14 ? 142 GLN   B OE1 1 
ATOM   2874 N NE2 . GLN   B 1 163 ? -19.317 -13.059 -6.227  1.00 31.13 ? 142 GLN   B NE2 1 
ATOM   2875 N N   . LYS   B 1 164 ? -20.374 -18.270 -8.267  1.00 63.62 ? 143 LYS   B N   1 
ATOM   2876 C CA  . LYS   B 1 164 ? -20.520 -19.463 -9.092  1.00 63.31 ? 143 LYS   B CA  1 
ATOM   2877 C C   . LYS   B 1 164 ? -19.151 -19.795 -9.718  1.00 65.65 ? 143 LYS   B C   1 
ATOM   2878 O O   . LYS   B 1 164 ? -18.629 -20.885 -9.406  1.00 69.00 ? 143 LYS   B O   1 
ATOM   2879 C CB  . LYS   B 1 164 ? -21.548 -19.238 -10.213 1.00 58.75 ? 143 LYS   B CB  1 
ATOM   2880 C CG  . LYS   B 1 164 ? -22.915 -19.910 -10.056 0.50 51.27 ? 143 LYS   B CG  1 
ATOM   2881 N N   . SER   B 1 173 ? -10.949 -15.958 -9.197  1.00 68.05 ? 152 SER   B N   1 
ATOM   2882 C CA  . SER   B 1 173 ? -9.551  -16.145 -8.722  1.00 62.59 ? 152 SER   B CA  1 
ATOM   2883 C C   . SER   B 1 173 ? -9.164  -15.062 -7.704  1.00 56.83 ? 152 SER   B C   1 
ATOM   2884 O O   . SER   B 1 173 ? -8.305  -15.304 -6.857  1.00 63.68 ? 152 SER   B O   1 
ATOM   2885 C CB  . SER   B 1 173 ? -8.565  -16.214 -9.893  1.00 57.64 ? 152 SER   B CB  1 
ATOM   2886 N N   . ASN   B 1 174 ? -9.760  -13.859 -7.811  1.00 44.44 ? 153 ASN   B N   1 
ATOM   2887 C CA  . ASN   B 1 174 ? -9.450  -12.769 -6.894  1.00 35.58 ? 153 ASN   B CA  1 
ATOM   2888 C C   . ASN   B 1 174 ? -10.714 -11.981 -6.533  1.00 29.43 ? 153 ASN   B C   1 
ATOM   2889 O O   . ASN   B 1 174 ? -10.922 -10.873 -7.013  1.00 27.39 ? 153 ASN   B O   1 
ATOM   2890 C CB  . ASN   B 1 174 ? -8.338  -11.875 -7.430  1.00 41.02 ? 153 ASN   B CB  1 
ATOM   2891 C CG  . ASN   B 1 174 ? -7.769  -10.984 -6.348  1.00 42.14 ? 153 ASN   B CG  1 
ATOM   2892 O OD1 . ASN   B 1 174 ? -8.082  -11.156 -5.165  1.00 43.12 ? 153 ASN   B OD1 1 
ATOM   2893 N ND2 . ASN   B 1 174 ? -6.913  -10.046 -6.723  1.00 48.00 ? 153 ASN   B ND2 1 
ATOM   2894 N N   . LEU   B 1 175 ? -11.518 -12.547 -5.629  1.00 23.76 ? 154 LEU   B N   1 
ATOM   2895 C CA  . LEU   B 1 175 ? -12.780 -11.961 -5.208  1.00 22.20 ? 154 LEU   B CA  1 
ATOM   2896 C C   . LEU   B 1 175 ? -12.538 -11.139 -3.957  1.00 22.39 ? 154 LEU   B C   1 
ATOM   2897 O O   . LEU   B 1 175 ? -11.883 -11.612 -3.016  1.00 23.47 ? 154 LEU   B O   1 
ATOM   2898 C CB  . LEU   B 1 175 ? -13.769 -13.080 -4.884  1.00 22.85 ? 154 LEU   B CB  1 
ATOM   2899 C CG  . LEU   B 1 175 ? -14.013 -14.146 -5.959  1.00 25.82 ? 154 LEU   B CG  1 
ATOM   2900 C CD1 . LEU   B 1 175 ? -14.913 -15.306 -5.443  1.00 25.65 ? 154 LEU   B CD1 1 
ATOM   2901 C CD2 . LEU   B 1 175 ? -14.618 -13.512 -7.213  1.00 26.95 ? 154 LEU   B CD2 1 
ATOM   2902 N N   . SER   B 1 176 ? -13.076 -9.909  -3.954  1.00 24.85 ? 155 SER   B N   1 
ATOM   2903 C CA  . SER   B 1 176 ? -12.930 -9.100  -2.751  1.00 25.48 ? 155 SER   B CA  1 
ATOM   2904 C C   . SER   B 1 176 ? -13.991 -8.007  -2.631  1.00 22.90 ? 155 SER   B C   1 
ATOM   2905 O O   . SER   B 1 176 ? -14.621 -7.572  -3.605  1.00 22.57 ? 155 SER   B O   1 
ATOM   2906 C CB  . SER   B 1 176 ? -11.515 -8.590  -2.589  1.00 29.49 ? 155 SER   B CB  1 
ATOM   2907 O OG  . SER   B 1 176 ? -11.326 -7.375  -3.282  1.00 27.46 ? 155 SER   B OG  1 
ATOM   2908 N N   . ILE   B 1 177 ? -14.172 -7.568  -1.386  1.00 21.51 ? 156 ILE   B N   1 
ATOM   2909 C CA  . ILE   B 1 177 ? -15.069 -6.489  -1.026  1.00 20.75 ? 156 ILE   B CA  1 
ATOM   2910 C C   . ILE   B 1 177 ? -14.233 -5.416  -0.326  1.00 19.88 ? 156 ILE   B C   1 
ATOM   2911 O O   . ILE   B 1 177 ? -13.329 -5.729  0.472   1.00 20.55 ? 156 ILE   B O   1 
ATOM   2912 C CB  . ILE   B 1 177 ? -16.142 -7.071  -0.095  1.00 21.88 ? 156 ILE   B CB  1 
ATOM   2913 C CG1 . ILE   B 1 177 ? -16.858 -8.294  -0.702  1.00 23.73 ? 156 ILE   B CG1 1 
ATOM   2914 C CG2 . ILE   B 1 177 ? -17.133 -5.985  0.348   1.00 20.76 ? 156 ILE   B CG2 1 
ATOM   2915 C CD1 . ILE   B 1 177 ? -18.086 -8.722  0.105   1.00 21.52 ? 156 ILE   B CD1 1 
ATOM   2916 N N   . VAL   B 1 178 ? -14.492 -4.156  -0.677  1.00 18.71 ? 157 VAL   B N   1 
ATOM   2917 C CA  . VAL   B 1 178 ? -13.842 -3.039  -0.016  1.00 18.31 ? 157 VAL   B CA  1 
ATOM   2918 C C   . VAL   B 1 178 ? -14.927 -2.093  0.495   1.00 19.45 ? 157 VAL   B C   1 
ATOM   2919 O O   . VAL   B 1 178 ? -15.775 -1.619  -0.275  1.00 19.65 ? 157 VAL   B O   1 
ATOM   2920 C CB  . VAL   B 1 178 ? -12.906 -2.248  -0.941  1.00 20.43 ? 157 VAL   B CB  1 
ATOM   2921 C CG1 . VAL   B 1 178 ? -12.235 -1.106  -0.189  1.00 18.96 ? 157 VAL   B CG1 1 
ATOM   2922 C CG2 . VAL   B 1 178 ? -11.841 -3.140  -1.595  1.00 25.40 ? 157 VAL   B CG2 1 
ATOM   2923 N N   . ASN   B 1 179 ? -14.880 -1.791  1.803   1.00 19.22 ? 158 ASN   B N   1 
ATOM   2924 C CA  . ASN   B 1 179 ? -15.879 -0.954  2.438   1.00 18.24 ? 158 ASN   B CA  1 
ATOM   2925 C C   . ASN   B 1 179 ? -15.249 0.402   2.745   1.00 19.41 ? 158 ASN   B C   1 
ATOM   2926 O O   . ASN   B 1 179 ? -14.157 0.436   3.302   1.00 20.57 ? 158 ASN   B O   1 
ATOM   2927 C CB  . ASN   B 1 179 ? -16.331 -1.568  3.759   1.00 18.98 ? 158 ASN   B CB  1 
ATOM   2928 C CG  . ASN   B 1 179 ? -17.079 -2.841  3.478   1.00 19.53 ? 158 ASN   B CG  1 
ATOM   2929 O OD1 . ASN   B 1 179 ? -17.724 -2.918  2.431   1.00 18.16 ? 158 ASN   B OD1 1 
ATOM   2930 N ND2 . ASN   B 1 179 ? -17.027 -3.820  4.370   1.00 21.34 ? 158 ASN   B ND2 1 
ATOM   2931 N N   . LEU   B 1 180 ? -15.925 1.497   2.370   1.00 18.59 ? 159 LEU   B N   1 
ATOM   2932 C CA  . LEU   B 1 180 ? -15.443 2.842   2.640   1.00 21.22 ? 159 LEU   B CA  1 
ATOM   2933 C C   . LEU   B 1 180 ? -15.827 3.224   4.075   1.00 22.09 ? 159 LEU   B C   1 
ATOM   2934 O O   . LEU   B 1 180 ? -16.998 3.506   4.354   1.00 22.23 ? 159 LEU   B O   1 
ATOM   2935 C CB  . LEU   B 1 180 ? -15.947 3.849   1.597   1.00 22.18 ? 159 LEU   B CB  1 
ATOM   2936 C CG  . LEU   B 1 180 ? -15.086 3.982   0.330   1.00 22.63 ? 159 LEU   B CG  1 
ATOM   2937 C CD1 . LEU   B 1 180 ? -13.775 4.746   0.599   1.00 20.77 ? 159 LEU   B CD1 1 
ATOM   2938 C CD2 . LEU   B 1 180 ? -14.794 2.610   -0.318  1.00 21.23 ? 159 LEU   B CD2 1 
ATOM   2939 N N   . CYS   B 1 181 ? -14.801 3.199   4.955   1.00 22.04 ? 160 CYS   B N   1 
ATOM   2940 C CA  . CYS   B 1 181 ? -14.923 3.473   6.377   1.00 23.18 ? 160 CYS   B CA  1 
ATOM   2941 C C   . CYS   B 1 181 ? -14.634 4.962   6.614   1.00 24.12 ? 160 CYS   B C   1 
ATOM   2942 O O   . CYS   B 1 181 ? -14.853 5.792   5.729   1.00 25.16 ? 160 CYS   B O   1 
ATOM   2943 C CB  . CYS   B 1 181 ? -14.036 2.502   7.146   1.00 23.33 ? 160 CYS   B CB  1 
ATOM   2944 S SG  . CYS   B 1 181 ? -14.530 0.770   6.875   1.00 26.86 ? 160 CYS   B SG  1 
ATOM   2945 N N   . ASP   B 1 182 ? -14.197 5.315   7.823   1.00 19.91 ? 161 ASP   B N   1 
ATOM   2946 C CA  . ASP   B 1 182 ? -13.962 6.711   8.139   1.00 21.11 ? 161 ASP   B CA  1 
ATOM   2947 C C   . ASP   B 1 182 ? -12.854 6.753   9.190   1.00 21.10 ? 161 ASP   B C   1 
ATOM   2948 O O   . ASP   B 1 182 ? -12.997 6.173   10.262  1.00 20.86 ? 161 ASP   B O   1 
ATOM   2949 C CB  . ASP   B 1 182 ? -15.252 7.356   8.632   1.00 24.51 ? 161 ASP   B CB  1 
ATOM   2950 C CG  . ASP   B 1 182 ? -15.153 8.857   8.872   1.00 32.94 ? 161 ASP   B CG  1 
ATOM   2951 O OD1 . ASP   B 1 182 ? -14.115 9.296   9.406   1.00 30.86 ? 161 ASP   B OD1 1 
ATOM   2952 O OD2 . ASP   B 1 182 ? -16.086 9.596   8.479   1.00 32.81 ? 161 ASP   B OD2 1 
ATOM   2953 N N   . ALA   B 1 183 ? -11.742 7.455   8.907   1.00 22.15 ? 162 ALA   B N   1 
ATOM   2954 C CA  . ALA   B 1 183 ? -10.602 7.426   9.826   1.00 21.55 ? 162 ALA   B CA  1 
ATOM   2955 C C   . ALA   B 1 183 ? -10.925 8.100   11.159  1.00 23.49 ? 162 ALA   B C   1 
ATOM   2956 O O   . ALA   B 1 183 ? -10.184 7.930   12.130  1.00 21.82 ? 162 ALA   B O   1 
ATOM   2957 C CB  . ALA   B 1 183 ? -9.386  8.108   9.162   1.00 19.42 ? 162 ALA   B CB  1 
ATOM   2958 N N   . MET   B 1 184 ? -11.961 8.955   11.175  1.00 22.11 ? 163 MET   B N   1 
ATOM   2959 C CA  . MET   B 1 184 ? -12.227 9.801   12.322  1.00 22.23 ? 163 MET   B CA  1 
ATOM   2960 C C   . MET   B 1 184 ? -13.366 9.260   13.198  1.00 22.75 ? 163 MET   B C   1 
ATOM   2961 O O   . MET   B 1 184 ? -13.862 9.988   14.053  1.00 23.40 ? 163 MET   B O   1 
ATOM   2962 C CB  . MET   B 1 184 ? -12.556 11.231  11.882  1.00 22.51 ? 163 MET   B CB  1 
ATOM   2963 C CG  . MET   B 1 184 ? -11.403 11.912  11.136  1.00 27.58 ? 163 MET   B CG  1 
ATOM   2964 S SD  . MET   B 1 184 ? -9.984  12.080  12.245  1.00 31.15 ? 163 MET   B SD  1 
ATOM   2965 C CE  . MET   B 1 184 ? -10.620 13.438  13.244  1.00 34.27 ? 163 MET   B CE  1 
ATOM   2966 N N   . VAL   B 1 185 ? -13.680 7.963   13.090  1.00 23.67 ? 164 VAL   B N   1 
ATOM   2967 C CA  . VAL   B 1 185 ? -14.833 7.390   13.777  1.00 27.76 ? 164 VAL   B CA  1 
ATOM   2968 C C   . VAL   B 1 185 ? -14.666 7.359   15.295  1.00 28.50 ? 164 VAL   B C   1 
ATOM   2969 O O   . VAL   B 1 185 ? -15.672 7.227   15.995  1.00 25.05 ? 164 VAL   B O   1 
ATOM   2970 C CB  . VAL   B 1 185 ? -15.249 5.993   13.288  1.00 28.94 ? 164 VAL   B CB  1 
ATOM   2971 C CG1 . VAL   B 1 185 ? -15.904 6.116   11.921  1.00 38.49 ? 164 VAL   B CG1 1 
ATOM   2972 C CG2 . VAL   B 1 185 ? -14.103 4.979   13.344  1.00 25.09 ? 164 VAL   B CG2 1 
ATOM   2973 N N   . ASP   B 1 186 ? -13.416 7.399   15.795  1.00 26.03 ? 165 ASP   B N   1 
ATOM   2974 C CA  . ASP   B 1 186 ? -13.201 7.410   17.242  1.00 26.50 ? 165 ASP   B CA  1 
ATOM   2975 C C   . ASP   B 1 186 ? -13.009 8.824   17.784  1.00 25.13 ? 165 ASP   B C   1 
ATOM   2976 O O   . ASP   B 1 186 ? -12.812 9.014   18.993  1.00 23.78 ? 165 ASP   B O   1 
ATOM   2977 C CB  . ASP   B 1 186 ? -12.084 6.471   17.660  1.00 25.94 ? 165 ASP   B CB  1 
ATOM   2978 C CG  . ASP   B 1 186 ? -12.340 5.016   17.319  1.00 29.39 ? 165 ASP   B CG  1 
ATOM   2979 O OD1 . ASP   B 1 186 ? -13.450 4.516   17.609  1.00 26.76 ? 165 ASP   B OD1 1 
ATOM   2980 O OD2 . ASP   B 1 186 ? -11.425 4.413   16.770  1.00 31.45 ? 165 ASP   B OD2 1 
ATOM   2981 N N   . GLN   B 1 187 ? -13.061 9.813   16.898  1.00 22.12 ? 166 GLN   B N   1 
ATOM   2982 C CA  . GLN   B 1 187 ? -12.969 11.207  17.300  1.00 26.02 ? 166 GLN   B CA  1 
ATOM   2983 C C   . GLN   B 1 187 ? -14.064 11.917  16.505  1.00 27.68 ? 166 GLN   B C   1 
ATOM   2984 O O   . GLN   B 1 187 ? -13.784 12.725  15.630  1.00 26.62 ? 166 GLN   B O   1 
ATOM   2985 C CB  . GLN   B 1 187 ? -11.598 11.836  17.004  1.00 26.07 ? 166 GLN   B CB  1 
ATOM   2986 C CG  . GLN   B 1 187 ? -10.445 11.109  17.694  1.00 31.43 ? 166 GLN   B CG  1 
ATOM   2987 C CD  . GLN   B 1 187 ? -9.331  10.731  16.736  1.00 36.19 ? 166 GLN   B CD  1 
ATOM   2988 O OE1 . GLN   B 1 187 ? -9.247  9.594   16.265  1.00 36.36 ? 166 GLN   B OE1 1 
ATOM   2989 N NE2 . GLN   B 1 187 ? -8.449  11.678  16.452  1.00 38.42 ? 166 GLN   B NE2 1 
ATOM   2990 N N   . PRO   B 1 188 ? -15.347 11.559  16.715  1.00 25.83 ? 167 PRO   B N   1 
ATOM   2991 C CA  . PRO   B 1 188 ? -16.387 11.963  15.760  1.00 30.69 ? 167 PRO   B CA  1 
ATOM   2992 C C   . PRO   B 1 188 ? -16.745 13.448  15.780  1.00 27.39 ? 167 PRO   B C   1 
ATOM   2993 O O   . PRO   B 1 188 ? -16.564 14.129  16.788  1.00 30.25 ? 167 PRO   B O   1 
ATOM   2994 C CB  . PRO   B 1 188 ? -17.566 11.101  16.235  1.00 27.40 ? 167 PRO   B CB  1 
ATOM   2995 C CG  . PRO   B 1 188 ? -17.370 11.002  17.721  1.00 26.65 ? 167 PRO   B CG  1 
ATOM   2996 C CD  . PRO   B 1 188 ? -15.847 10.794  17.860  1.00 26.35 ? 167 PRO   B CD  1 
HETATM 2997 N N   . CSX   B 1 189 ? -17.336 13.910  14.677  1.00 27.50 ? 168 CSX   B N   1 
HETATM 2998 C CA  . CSX   B 1 189 ? -17.964 15.223  14.608  1.00 30.79 ? 168 CSX   B CA  1 
HETATM 2999 C CB  . CSX   B 1 189 ? -18.457 15.534  13.186  1.00 37.86 ? 168 CSX   B CB  1 
HETATM 3000 S SG  . CSX   B 1 189 ? -17.069 15.886  12.068  1.00 49.27 ? 168 CSX   B SG  1 
HETATM 3001 C C   . CSX   B 1 189 ? -19.115 15.289  15.611  1.00 29.57 ? 168 CSX   B C   1 
HETATM 3002 O O   . CSX   B 1 189 ? -19.883 14.337  15.766  1.00 25.16 ? 168 CSX   B O   1 
HETATM 3003 O OD  . CSX   B 1 189 ? -16.779 17.336  12.296  1.00 45.64 ? 168 CSX   B OD  1 
ATOM   3004 N N   . MET   B 1 190 ? -19.221 16.426  16.299  1.00 27.98 ? 169 MET   B N   1 
ATOM   3005 C CA  . MET   B 1 190 ? -20.312 16.693  17.234  1.00 32.02 ? 169 MET   B CA  1 
ATOM   3006 C C   . MET   B 1 190 ? -21.662 16.495  16.528  1.00 24.69 ? 169 MET   B C   1 
ATOM   3007 O O   . MET   B 1 190 ? -21.820 16.978  15.416  1.00 26.28 ? 169 MET   B O   1 
ATOM   3008 C CB  . MET   B 1 190 ? -20.243 18.178  17.632  1.00 37.41 ? 169 MET   B CB  1 
ATOM   3009 C CG  . MET   B 1 190 ? -21.357 18.642  18.571  1.00 40.73 ? 169 MET   B CG  1 
ATOM   3010 S SD  . MET   B 1 190 ? -21.203 17.703  20.108  1.00 46.71 ? 169 MET   B SD  1 
ATOM   3011 C CE  . MET   B 1 190 ? -19.704 18.359  20.852  1.00 44.08 ? 169 MET   B CE  1 
ATOM   3012 N N   . ALA   B 1 191 ? -22.625 15.792  17.154  1.00 25.15 ? 170 ALA   B N   1 
ATOM   3013 C CA  . ALA   B 1 191 ? -23.988 15.684  16.641  1.00 26.07 ? 170 ALA   B CA  1 
ATOM   3014 C C   . ALA   B 1 191 ? -24.130 14.743  15.443  1.00 25.97 ? 170 ALA   B C   1 
ATOM   3015 O O   . ALA   B 1 191 ? -25.138 14.817  14.760  1.00 25.42 ? 170 ALA   B O   1 
ATOM   3016 C CB  . ALA   B 1 191 ? -24.584 17.067  16.293  1.00 25.79 ? 170 ALA   B CB  1 
ATOM   3017 N N   . PHE   B 1 192 ? -23.154 13.857  15.189  1.00 23.67 ? 171 PHE   B N   1 
ATOM   3018 C CA  . PHE   B 1 192 ? -23.267 12.885  14.102  1.00 22.32 ? 171 PHE   B CA  1 
ATOM   3019 C C   . PHE   B 1 192 ? -23.340 11.460  14.646  1.00 22.00 ? 171 PHE   B C   1 
ATOM   3020 O O   . PHE   B 1 192 ? -22.734 10.557  14.074  1.00 19.76 ? 171 PHE   B O   1 
ATOM   3021 C CB  . PHE   B 1 192 ? -22.047 13.048  13.192  1.00 23.18 ? 171 PHE   B CB  1 
ATOM   3022 C CG  . PHE   B 1 192 ? -22.129 14.227  12.216  1.00 25.62 ? 171 PHE   B CG  1 
ATOM   3023 C CD1 . PHE   B 1 192 ? -21.829 15.532  12.617  1.00 26.31 ? 171 PHE   B CD1 1 
ATOM   3024 C CD2 . PHE   B 1 192 ? -22.506 14.015  10.882  1.00 29.37 ? 171 PHE   B CD2 1 
ATOM   3025 C CE1 . PHE   B 1 192 ? -21.914 16.593  11.709  1.00 26.98 ? 171 PHE   B CE1 1 
ATOM   3026 C CE2 . PHE   B 1 192 ? -22.571 15.069  9.976   1.00 30.31 ? 171 PHE   B CE2 1 
ATOM   3027 C CZ  . PHE   B 1 192 ? -22.283 16.360  10.389  1.00 28.15 ? 171 PHE   B CZ  1 
ATOM   3028 N N   . SER   B 1 193 ? -24.192 11.221  15.647  1.00 21.06 ? 172 SER   B N   1 
ATOM   3029 C CA  A SER   B 1 193 ? -24.221 9.908   16.275  0.60 22.87 ? 172 SER   B CA  1 
ATOM   3030 C CA  B SER   B 1 193 ? -24.267 9.910   16.288  0.40 21.27 ? 172 SER   B CA  1 
ATOM   3031 C C   . SER   B 1 193 ? -24.643 8.821   15.284  1.00 21.13 ? 172 SER   B C   1 
ATOM   3032 O O   . SER   B 1 193 ? -24.048 7.747   15.263  1.00 20.82 ? 172 SER   B O   1 
ATOM   3033 C CB  A SER   B 1 193 ? -25.103 9.906   17.504  0.60 24.30 ? 172 SER   B CB  1 
ATOM   3034 C CB  B SER   B 1 193 ? -25.246 9.871   17.454  0.40 20.34 ? 172 SER   B CB  1 
ATOM   3035 O OG  A SER   B 1 193 ? -26.371 10.454  17.170  0.60 29.36 ? 172 SER   B OG  1 
ATOM   3036 O OG  B SER   B 1 193 ? -24.837 10.650  18.568  0.40 19.45 ? 172 SER   B OG  1 
ATOM   3037 N N   . LEU   B 1 194 ? -25.708 9.056   14.504  1.00 21.98 ? 173 LEU   B N   1 
ATOM   3038 C CA  . LEU   B 1 194 ? -26.207 8.001   13.608  1.00 20.25 ? 173 LEU   B CA  1 
ATOM   3039 C C   . LEU   B 1 194 ? -25.186 7.656   12.526  1.00 19.36 ? 173 LEU   B C   1 
ATOM   3040 O O   . LEU   B 1 194 ? -24.964 6.476   12.224  1.00 20.74 ? 173 LEU   B O   1 
ATOM   3041 C CB  . LEU   B 1 194 ? -27.594 8.287   13.015  1.00 18.94 ? 173 LEU   B CB  1 
ATOM   3042 C CG  . LEU   B 1 194 ? -28.762 8.098   14.000  1.00 19.06 ? 173 LEU   B CG  1 
ATOM   3043 C CD1 . LEU   B 1 194 ? -30.043 8.722   13.377  1.00 19.54 ? 173 LEU   B CD1 1 
ATOM   3044 C CD2 . LEU   B 1 194 ? -28.924 6.579   14.218  1.00 20.43 ? 173 LEU   B CD2 1 
ATOM   3045 N N   . TYR   B 1 195 ? -24.583 8.682   11.924  1.00 19.54 ? 174 TYR   B N   1 
ATOM   3046 C CA  . TYR   B 1 195 ? -23.532 8.495   10.928  1.00 19.48 ? 174 TYR   B CA  1 
ATOM   3047 C C   . TYR   B 1 195 ? -22.404 7.641   11.518  1.00 20.89 ? 174 TYR   B C   1 
ATOM   3048 O O   . TYR   B 1 195 ? -21.974 6.637   10.931  1.00 20.19 ? 174 TYR   B O   1 
ATOM   3049 C CB  . TYR   B 1 195 ? -23.020 9.846   10.397  1.00 20.50 ? 174 TYR   B CB  1 
ATOM   3050 C CG  . TYR   B 1 195 ? -21.778 9.648   9.533   1.00 21.02 ? 174 TYR   B CG  1 
ATOM   3051 C CD1 . TYR   B 1 195 ? -21.881 9.255   8.198   1.00 21.99 ? 174 TYR   B CD1 1 
ATOM   3052 C CD2 . TYR   B 1 195 ? -20.499 9.839   10.054  1.00 23.43 ? 174 TYR   B CD2 1 
ATOM   3053 C CE1 . TYR   B 1 195 ? -20.742 9.032   7.424   1.00 23.24 ? 174 TYR   B CE1 1 
ATOM   3054 C CE2 . TYR   B 1 195 ? -19.367 9.595   9.304   1.00 22.69 ? 174 TYR   B CE2 1 
ATOM   3055 C CZ  . TYR   B 1 195 ? -19.486 9.205   7.986   1.00 25.41 ? 174 TYR   B CZ  1 
ATOM   3056 O OH  . TYR   B 1 195 ? -18.343 9.009   7.261   1.00 28.28 ? 174 TYR   B OH  1 
ATOM   3057 N N   . ASN   B 1 196 ? -21.946 8.050   12.713  1.00 20.98 ? 175 ASN   B N   1 
ATOM   3058 C CA  A ASN   B 1 196 ? -20.848 7.396   13.400  0.80 21.64 ? 175 ASN   B CA  1 
ATOM   3059 C CA  B ASN   B 1 196 ? -20.832 7.380   13.353  0.20 19.47 ? 175 ASN   B CA  1 
ATOM   3060 C C   . ASN   B 1 196 ? -21.238 5.957   13.719  1.00 20.25 ? 175 ASN   B C   1 
ATOM   3061 O O   . ASN   B 1 196 ? -20.428 5.050   13.577  1.00 19.44 ? 175 ASN   B O   1 
ATOM   3062 C CB  A ASN   B 1 196 ? -20.445 8.176   14.650  0.80 24.66 ? 175 ASN   B CB  1 
ATOM   3063 C CB  B ASN   B 1 196 ? -20.196 8.237   14.443  0.20 18.20 ? 175 ASN   B CB  1 
ATOM   3064 C CG  A ASN   B 1 196 ? -19.100 7.763   15.205  0.80 31.32 ? 175 ASN   B CG  1 
ATOM   3065 C CG  B ASN   B 1 196 ? -19.375 9.355   13.848  0.20 17.45 ? 175 ASN   B CG  1 
ATOM   3066 O OD1 A ASN   B 1 196 ? -19.000 7.311   16.359  0.80 37.74 ? 175 ASN   B OD1 1 
ATOM   3067 O OD1 B ASN   B 1 196 ? -18.283 9.116   13.315  0.20 18.13 ? 175 ASN   B OD1 1 
ATOM   3068 N ND2 A ASN   B 1 196 ? -18.048 7.972   14.428  0.80 26.38 ? 175 ASN   B ND2 1 
ATOM   3069 N ND2 B ASN   B 1 196 ? -19.882 10.576  13.919  0.20 15.94 ? 175 ASN   B ND2 1 
ATOM   3070 N N   . MET   B 1 197 ? -22.489 5.759   14.178  1.00 19.06 ? 176 MET   B N   1 
ATOM   3071 C CA  . MET   B 1 197 ? -22.932 4.386   14.464  1.00 17.63 ? 176 MET   B CA  1 
ATOM   3072 C C   . MET   B 1 197 ? -22.865 3.523   13.198  1.00 18.33 ? 176 MET   B C   1 
ATOM   3073 O O   . MET   B 1 197 ? -22.518 2.331   13.235  1.00 18.09 ? 176 MET   B O   1 
ATOM   3074 C CB  . MET   B 1 197 ? -24.368 4.392   15.012  1.00 18.36 ? 176 MET   B CB  1 
ATOM   3075 C CG  . MET   B 1 197 ? -24.427 4.937   16.442  1.00 21.60 ? 176 MET   B CG  1 
ATOM   3076 S SD  . MET   B 1 197 ? -26.147 5.290   16.894  1.00 22.97 ? 176 MET   B SD  1 
ATOM   3077 C CE  . MET   B 1 197 ? -26.744 3.594   16.894  1.00 20.88 ? 176 MET   B CE  1 
ATOM   3078 N N   . GLY   B 1 198 ? -23.274 4.113   12.073  1.00 18.51 ? 177 GLY   B N   1 
ATOM   3079 C CA  . GLY   B 1 198 ? -23.279 3.409   10.796  1.00 18.54 ? 177 GLY   B CA  1 
ATOM   3080 C C   . GLY   B 1 198 ? -21.862 3.016   10.369  1.00 17.91 ? 177 GLY   B C   1 
ATOM   3081 O O   . GLY   B 1 198 ? -21.616 1.880   9.962   1.00 18.41 ? 177 GLY   B O   1 
ATOM   3082 N N   . LYS   B 1 199 ? -20.919 3.942   10.509  1.00 16.48 ? 178 LYS   B N   1 
ATOM   3083 C CA  . LYS   B 1 199 ? -19.548 3.640   10.108  1.00 16.97 ? 178 LYS   B CA  1 
ATOM   3084 C C   . LYS   B 1 199 ? -18.895 2.618   11.051  1.00 18.10 ? 178 LYS   B C   1 
ATOM   3085 O O   . LYS   B 1 199 ? -18.143 1.778   10.579  1.00 19.30 ? 178 LYS   B O   1 
ATOM   3086 C CB  . LYS   B 1 199 ? -18.706 4.925   10.015  1.00 20.19 ? 178 LYS   B CB  1 
ATOM   3087 C CG  . LYS   B 1 199 ? -19.086 5.783   8.792   1.00 21.43 ? 178 LYS   B CG  1 
ATOM   3088 C CD  . LYS   B 1 199 ? -18.981 5.034   7.466   1.00 20.98 ? 178 LYS   B CD  1 
ATOM   3089 C CE  . LYS   B 1 199 ? -18.976 6.033   6.315   1.00 24.56 ? 178 LYS   B CE  1 
ATOM   3090 N NZ  . LYS   B 1 199 ? -18.907 5.355   5.018   1.00 22.73 ? 178 LYS   B NZ  1 
ATOM   3091 N N   . HIS   B 1 200 ? -19.171 2.690   12.377  1.00 20.02 ? 179 HIS   B N   1 
ATOM   3092 C CA  . HIS   B 1 200 ? -18.699 1.655   13.286  1.00 20.06 ? 179 HIS   B CA  1 
ATOM   3093 C C   . HIS   B 1 200 ? -19.294 0.313   12.887  1.00 18.64 ? 179 HIS   B C   1 
ATOM   3094 O O   . HIS   B 1 200 ? -18.566 -0.688  12.934  1.00 18.18 ? 179 HIS   B O   1 
ATOM   3095 C CB  . HIS   B 1 200 ? -19.043 1.930   14.754  1.00 21.37 ? 179 HIS   B CB  1 
ATOM   3096 C CG  . HIS   B 1 200 ? -18.022 2.758   15.434  1.00 24.11 ? 179 HIS   B CG  1 
ATOM   3097 N ND1 . HIS   B 1 200 ? -16.938 2.205   16.078  1.00 25.12 ? 179 HIS   B ND1 1 
ATOM   3098 C CD2 . HIS   B 1 200 ? -17.900 4.107   15.558  1.00 23.61 ? 179 HIS   B CD2 1 
ATOM   3099 C CE1 . HIS   B 1 200 ? -16.205 3.181   16.610  1.00 24.41 ? 179 HIS   B CE1 1 
ATOM   3100 N NE2 . HIS   B 1 200 ? -16.775 4.342   16.312  1.00 25.04 ? 179 HIS   B NE2 1 
ATOM   3101 N N   . ALA   B 1 201 ? -20.614 0.271   12.599  1.00 18.32 ? 180 ALA   B N   1 
ATOM   3102 C CA  . ALA   B 1 201 ? -21.190 -1.019  12.204  1.00 21.13 ? 180 ALA   B CA  1 
ATOM   3103 C C   . ALA   B 1 201 ? -20.457 -1.583  10.971  1.00 19.08 ? 180 ALA   B C   1 
ATOM   3104 O O   . ALA   B 1 201 ? -20.279 -2.798  10.823  1.00 19.67 ? 180 ALA   B O   1 
ATOM   3105 C CB  . ALA   B 1 201 ? -22.704 -0.887  11.920  1.00 19.28 ? 180 ALA   B CB  1 
ATOM   3106 N N   . LEU   B 1 202 ? -20.061 -0.700  10.059  1.00 17.58 ? 181 LEU   B N   1 
ATOM   3107 C CA  . LEU   B 1 202 ? -19.345 -1.048  8.822   1.00 19.96 ? 181 LEU   B CA  1 
ATOM   3108 C C   . LEU   B 1 202 ? -17.976 -1.669  9.126   1.00 19.38 ? 181 LEU   B C   1 
ATOM   3109 O O   . LEU   B 1 202 ? -17.568 -2.667  8.501   1.00 20.75 ? 181 LEU   B O   1 
ATOM   3110 C CB  . LEU   B 1 202 ? -19.193 0.194   7.932   1.00 20.23 ? 181 LEU   B CB  1 
ATOM   3111 C CG  . LEU   B 1 202 ? -18.703 -0.076  6.498   1.00 22.32 ? 181 LEU   B CG  1 
ATOM   3112 C CD1 . LEU   B 1 202 ? -19.570 -1.132  5.770   1.00 20.47 ? 181 LEU   B CD1 1 
ATOM   3113 C CD2 . LEU   B 1 202 ? -18.591 1.221   5.688   1.00 21.74 ? 181 LEU   B CD2 1 
ATOM   3114 N N   . VAL   B 1 203 ? -17.307 -1.145  10.172  1.00 19.81 ? 182 VAL   B N   1 
ATOM   3115 C CA  . VAL   B 1 203 ? -16.089 -1.783  10.665  1.00 18.47 ? 182 VAL   B CA  1 
ATOM   3116 C C   . VAL   B 1 203 ? -16.430 -3.203  11.081  1.00 17.26 ? 182 VAL   B C   1 
ATOM   3117 O O   . VAL   B 1 203 ? -15.716 -4.146  10.754  1.00 18.87 ? 182 VAL   B O   1 
ATOM   3118 C CB  . VAL   B 1 203 ? -15.371 -1.020  11.797  1.00 22.02 ? 182 VAL   B CB  1 
ATOM   3119 C CG1 . VAL   B 1 203 ? -14.212 -1.816  12.395  1.00 22.71 ? 182 VAL   B CG1 1 
ATOM   3120 C CG2 . VAL   B 1 203 ? -14.876 0.335   11.289  1.00 22.81 ? 182 VAL   B CG2 1 
ATOM   3121 N N   . GLY   B 1 204 ? -17.489 -3.347  11.896  1.00 18.16 ? 183 GLY   B N   1 
ATOM   3122 C CA  . GLY   B 1 204 ? -17.817 -4.676  12.377  1.00 17.95 ? 183 GLY   B CA  1 
ATOM   3123 C C   . GLY   B 1 204 ? -18.128 -5.613  11.219  1.00 17.17 ? 183 GLY   B C   1 
ATOM   3124 O O   . GLY   B 1 204 ? -17.781 -6.794  11.270  1.00 19.65 ? 183 GLY   B O   1 
ATOM   3125 N N   . LEU   B 1 205 ? -18.861 -5.128  10.204  1.00 18.97 ? 184 LEU   B N   1 
ATOM   3126 C CA  . LEU   B 1 205 ? -19.146 -5.972  9.045   1.00 19.41 ? 184 LEU   B CA  1 
ATOM   3127 C C   . LEU   B 1 205 ? -17.861 -6.403  8.311   1.00 19.35 ? 184 LEU   B C   1 
ATOM   3128 O O   . LEU   B 1 205 ? -17.721 -7.577  7.902   1.00 19.19 ? 184 LEU   B O   1 
ATOM   3129 C CB  . LEU   B 1 205 ? -20.096 -5.232  8.097   1.00 18.64 ? 184 LEU   B CB  1 
ATOM   3130 C CG  . LEU   B 1 205 ? -20.345 -5.928  6.748   1.00 19.50 ? 184 LEU   B CG  1 
ATOM   3131 C CD1 . LEU   B 1 205 ? -20.986 -7.330  6.893   1.00 19.18 ? 184 LEU   B CD1 1 
ATOM   3132 C CD2 . LEU   B 1 205 ? -21.142 -5.006  5.824   1.00 19.54 ? 184 LEU   B CD2 1 
ATOM   3133 N N   . THR   B 1 206 ? -16.906 -5.476  8.164   1.00 17.87 ? 185 THR   B N   1 
ATOM   3134 C CA  . THR   B 1 206 ? -15.676 -5.787  7.444   1.00 18.58 ? 185 THR   B CA  1 
ATOM   3135 C C   . THR   B 1 206 ? -14.967 -6.956  8.147   1.00 20.96 ? 185 THR   B C   1 
ATOM   3136 O O   . THR   B 1 206 ? -14.577 -7.959  7.522   1.00 21.62 ? 185 THR   B O   1 
ATOM   3137 C CB  . THR   B 1 206 ? -14.822 -4.515  7.427   1.00 19.36 ? 185 THR   B CB  1 
ATOM   3138 O OG1 . THR   B 1 206 ? -15.535 -3.437  6.841   1.00 21.13 ? 185 THR   B OG1 1 
ATOM   3139 C CG2 . THR   B 1 206 ? -13.506 -4.655  6.672   1.00 18.10 ? 185 THR   B CG2 1 
ATOM   3140 N N   . GLN   B 1 207 ? -14.898 -6.871  9.499   1.00 21.60 ? 186 GLN   B N   1 
ATOM   3141 C CA  . GLN   B 1 207 ? -14.245 -7.925  10.278  1.00 19.07 ? 186 GLN   B CA  1 
ATOM   3142 C C   . GLN   B 1 207 ? -15.030 -9.230  10.194  1.00 19.62 ? 186 GLN   B C   1 
ATOM   3143 O O   . GLN   B 1 207 ? -14.468 -10.282 9.904   1.00 19.69 ? 186 GLN   B O   1 
ATOM   3144 C CB  . GLN   B 1 207 ? -14.084 -7.459  11.729  1.00 18.77 ? 186 GLN   B CB  1 
ATOM   3145 C CG  . GLN   B 1 207 ? -13.051 -6.343  11.806  1.00 23.38 ? 186 GLN   B CG  1 
ATOM   3146 C CD  . GLN   B 1 207 ? -12.833 -5.755  13.186  1.00 29.30 ? 186 GLN   B CD  1 
ATOM   3147 O OE1 . GLN   B 1 207 ? -11.820 -5.085  13.401  1.00 34.79 ? 186 GLN   B OE1 1 
ATOM   3148 N NE2 . GLN   B 1 207 ? -13.765 -5.959  14.104  1.00 30.76 ? 186 GLN   B NE2 1 
ATOM   3149 N N   . SER   B 1 208 ? -16.322 -9.179  10.558  1.00 20.04 ? 187 SER   B N   1 
ATOM   3150 C CA  . SER   B 1 208 ? -17.171 -10.364 10.535  1.00 20.89 ? 187 SER   B CA  1 
ATOM   3151 C C   . SER   B 1 208 ? -17.182 -11.040 9.171   1.00 19.72 ? 187 SER   B C   1 
ATOM   3152 O O   . SER   B 1 208 ? -17.044 -12.267 9.102   1.00 22.05 ? 187 SER   B O   1 
ATOM   3153 C CB  . SER   B 1 208 ? -18.585 -10.033 10.938  1.00 20.94 ? 187 SER   B CB  1 
ATOM   3154 O OG  . SER   B 1 208 ? -18.659 -9.900  12.350  1.00 23.50 ? 187 SER   B OG  1 
ATOM   3155 N N   . ALA   B 1 209 ? -17.359 -10.265 8.089   1.00 18.54 ? 188 ALA   B N   1 
ATOM   3156 C CA  . ALA   B 1 209 ? -17.434 -10.874 6.767   1.00 21.52 ? 188 ALA   B CA  1 
ATOM   3157 C C   . ALA   B 1 209 ? -16.057 -11.375 6.307   1.00 22.10 ? 188 ALA   B C   1 
ATOM   3158 O O   . ALA   B 1 209 ? -15.957 -12.435 5.676   1.00 21.40 ? 188 ALA   B O   1 
ATOM   3159 C CB  . ALA   B 1 209 ? -18.001 -9.869  5.796   1.00 20.46 ? 188 ALA   B CB  1 
ATOM   3160 N N   . ALA   B 1 210 ? -14.976 -10.668 6.685   1.00 19.77 ? 189 ALA   B N   1 
ATOM   3161 C CA  . ALA   B 1 210 ? -13.653 -11.237 6.428   1.00 20.07 ? 189 ALA   B CA  1 
ATOM   3162 C C   . ALA   B 1 210 ? -13.505 -12.637 7.033   1.00 22.03 ? 189 ALA   B C   1 
ATOM   3163 O O   . ALA   B 1 210 ? -12.991 -13.535 6.361   1.00 23.12 ? 189 ALA   B O   1 
ATOM   3164 C CB  . ALA   B 1 210 ? -12.532 -10.334 6.902   1.00 19.77 ? 189 ALA   B CB  1 
ATOM   3165 N N   . LEU   B 1 211 ? -13.910 -12.813 8.306   1.00 20.69 ? 190 LEU   B N   1 
ATOM   3166 C CA  . LEU   B 1 211 ? -13.720 -14.111 8.957   1.00 26.60 ? 190 LEU   B CA  1 
ATOM   3167 C C   . LEU   B 1 211 ? -14.559 -15.178 8.256   1.00 26.30 ? 190 LEU   B C   1 
ATOM   3168 O O   . LEU   B 1 211 ? -14.087 -16.280 7.943   1.00 24.51 ? 190 LEU   B O   1 
ATOM   3169 C CB  . LEU   B 1 211 ? -14.125 -13.982 10.439  1.00 24.58 ? 190 LEU   B CB  1 
ATOM   3170 C CG  . LEU   B 1 211 ? -14.054 -15.268 11.269  1.00 26.96 ? 190 LEU   B CG  1 
ATOM   3171 C CD1 . LEU   B 1 211 ? -12.560 -15.475 11.568  1.00 24.38 ? 190 LEU   B CD1 1 
ATOM   3172 C CD2 . LEU   B 1 211 ? -14.924 -15.117 12.554  1.00 25.07 ? 190 LEU   B CD2 1 
ATOM   3173 N N   . GLU   B 1 212 ? -15.827 -14.828 8.030   1.00 23.88 ? 191 GLU   B N   1 
ATOM   3174 C CA  . GLU   B 1 212 ? -16.800 -15.787 7.520   1.00 25.95 ? 191 GLU   B CA  1 
ATOM   3175 C C   . GLU   B 1 212 ? -16.551 -16.115 6.046   1.00 24.13 ? 191 GLU   B C   1 
ATOM   3176 O O   . GLU   B 1 212 ? -16.852 -17.235 5.620   1.00 24.55 ? 191 GLU   B O   1 
ATOM   3177 C CB  . GLU   B 1 212 ? -18.233 -15.258 7.692   1.00 24.02 ? 191 GLU   B CB  1 
ATOM   3178 C CG  . GLU   B 1 212 ? -19.311 -16.278 7.320   1.00 25.59 ? 191 GLU   B CG  1 
ATOM   3179 C CD  . GLU   B 1 212 ? -20.709 -15.764 7.677   1.00 27.87 ? 191 GLU   B CD  1 
ATOM   3180 O OE1 . GLU   B 1 212 ? -21.685 -16.408 7.231   1.00 28.98 ? 191 GLU   B OE1 1 
ATOM   3181 O OE2 . GLU   B 1 212 ? -20.833 -14.721 8.385   1.00 31.91 ? 191 GLU   B OE2 1 
ATOM   3182 N N   . LEU   B 1 213 ? -16.044 -15.145 5.255   1.00 21.81 ? 192 LEU   B N   1 
ATOM   3183 C CA  . LEU   B 1 213 ? -15.936 -15.366 3.815   1.00 21.52 ? 192 LEU   B CA  1 
ATOM   3184 C C   . LEU   B 1 213 ? -14.550 -15.874 3.414   1.00 23.86 ? 192 LEU   B C   1 
ATOM   3185 O O   . LEU   B 1 213 ? -14.334 -16.247 2.254   1.00 23.61 ? 192 LEU   B O   1 
ATOM   3186 C CB  . LEU   B 1 213 ? -16.387 -14.217 2.915   1.00 19.80 ? 192 LEU   B CB  1 
ATOM   3187 C CG  . LEU   B 1 213 ? -17.825 -13.758 3.179   1.00 21.93 ? 192 LEU   B CG  1 
ATOM   3188 C CD1 . LEU   B 1 213 ? -18.132 -12.538 2.314   1.00 22.26 ? 192 LEU   B CD1 1 
ATOM   3189 C CD2 . LEU   B 1 213 ? -18.815 -14.890 2.893   1.00 21.64 ? 192 LEU   B CD2 1 
ATOM   3190 N N   . ALA   B 1 214 ? -13.625 -15.887 4.374   1.00 21.96 ? 193 ALA   B N   1 
ATOM   3191 C CA  . ALA   B 1 214 ? -12.258 -16.307 4.078   1.00 25.13 ? 193 ALA   B CA  1 
ATOM   3192 C C   . ALA   B 1 214 ? -12.236 -17.723 3.500   1.00 28.80 ? 193 ALA   B C   1 
ATOM   3193 O O   . ALA   B 1 214 ? -11.444 -18.005 2.597   1.00 27.57 ? 193 ALA   B O   1 
ATOM   3194 C CB  . ALA   B 1 214 ? -11.380 -16.217 5.314   1.00 24.03 ? 193 ALA   B CB  1 
ATOM   3195 N N   . PRO   B 1 215 ? -13.058 -18.676 4.004   1.00 31.61 ? 194 PRO   B N   1 
ATOM   3196 C CA  . PRO   B 1 215 ? -13.044 -20.046 3.467   1.00 33.92 ? 194 PRO   B CA  1 
ATOM   3197 C C   . PRO   B 1 215 ? -13.473 -20.141 2.006   1.00 35.14 ? 194 PRO   B C   1 
ATOM   3198 O O   . PRO   B 1 215 ? -13.202 -21.142 1.358   1.00 38.64 ? 194 PRO   B O   1 
ATOM   3199 C CB  . PRO   B 1 215 ? -13.977 -20.853 4.391   1.00 33.55 ? 194 PRO   B CB  1 
ATOM   3200 C CG  . PRO   B 1 215 ? -14.114 -19.995 5.640   1.00 36.23 ? 194 PRO   B CG  1 
ATOM   3201 C CD  . PRO   B 1 215 ? -13.929 -18.554 5.190   1.00 32.07 ? 194 PRO   B CD  1 
ATOM   3202 N N   . TYR   B 1 216 ? -14.116 -19.086 1.488   1.00 34.45 ? 195 TYR   B N   1 
ATOM   3203 C CA  . TYR   B 1 216 ? -14.557 -19.051 0.107   1.00 33.05 ? 195 TYR   B CA  1 
ATOM   3204 C C   . TYR   B 1 216 ? -13.578 -18.229 -0.725  1.00 31.89 ? 195 TYR   B C   1 
ATOM   3205 O O   . TYR   B 1 216 ? -13.802 -18.024 -1.902  1.00 35.00 ? 195 TYR   B O   1 
ATOM   3206 C CB  . TYR   B 1 216 ? -15.941 -18.424 0.035   1.00 35.08 ? 195 TYR   B CB  1 
ATOM   3207 C CG  . TYR   B 1 216 ? -16.996 -19.153 0.854   1.00 42.61 ? 195 TYR   B CG  1 
ATOM   3208 C CD1 . TYR   B 1 216 ? -17.730 -20.201 0.305   1.00 42.94 ? 195 TYR   B CD1 1 
ATOM   3209 C CD2 . TYR   B 1 216 ? -17.273 -18.783 2.167   1.00 43.01 ? 195 TYR   B CD2 1 
ATOM   3210 C CE1 . TYR   B 1 216 ? -18.725 -20.838 1.031   1.00 47.18 ? 195 TYR   B CE1 1 
ATOM   3211 C CE2 . TYR   B 1 216 ? -18.261 -19.414 2.907   1.00 48.84 ? 195 TYR   B CE2 1 
ATOM   3212 C CZ  . TYR   B 1 216 ? -18.990 -20.444 2.332   1.00 53.85 ? 195 TYR   B CZ  1 
ATOM   3213 O OH  . TYR   B 1 216 ? -19.960 -21.086 3.047   1.00 52.99 ? 195 TYR   B OH  1 
ATOM   3214 N N   . GLY   B 1 217 ? -12.485 -17.783 -0.105  1.00 30.64 ? 196 GLY   B N   1 
ATOM   3215 C CA  . GLY   B 1 217 ? -11.461 -17.021 -0.798  1.00 29.95 ? 196 GLY   B CA  1 
ATOM   3216 C C   . GLY   B 1 217 ? -11.904 -15.589 -1.092  1.00 29.37 ? 196 GLY   B C   1 
ATOM   3217 O O   . GLY   B 1 217 ? -11.263 -14.912 -1.876  1.00 32.69 ? 196 GLY   B O   1 
ATOM   3218 N N   . ILE   B 1 218 ? -12.960 -15.103 -0.427  1.00 23.21 ? 197 ILE   B N   1 
ATOM   3219 C CA  . ILE   B 1 218 ? -13.367 -13.717 -0.631  1.00 20.62 ? 197 ILE   B CA  1 
ATOM   3220 C C   . ILE   B 1 218 ? -12.746 -12.866 0.478   1.00 21.78 ? 197 ILE   B C   1 
ATOM   3221 O O   . ILE   B 1 218 ? -13.023 -13.096 1.656   1.00 22.68 ? 197 ILE   B O   1 
ATOM   3222 C CB  . ILE   B 1 218 ? -14.900 -13.607 -0.581  1.00 22.08 ? 197 ILE   B CB  1 
ATOM   3223 C CG1 . ILE   B 1 218 ? -15.553 -14.502 -1.634  1.00 22.21 ? 197 ILE   B CG1 1 
ATOM   3224 C CG2 . ILE   B 1 218 ? -15.335 -12.141 -0.740  1.00 21.25 ? 197 ILE   B CG2 1 
ATOM   3225 C CD1 . ILE   B 1 218 ? -17.062 -14.610 -1.413  1.00 26.06 ? 197 ILE   B CD1 1 
ATOM   3226 N N   . ARG   B 1 219 ? -11.908 -11.902 0.089   1.00 20.18 ? 198 ARG   B N   1 
ATOM   3227 C CA  . ARG   B 1 219 ? -11.258 -11.024 1.057   1.00 22.23 ? 198 ARG   B CA  1 
ATOM   3228 C C   . ARG   B 1 219 ? -12.183 -9.829  1.293   1.00 22.32 ? 198 ARG   B C   1 
ATOM   3229 O O   . ARG   B 1 219 ? -12.909 -9.390  0.387   1.00 20.74 ? 198 ARG   B O   1 
ATOM   3230 C CB  . ARG   B 1 219 ? -9.883  -10.544 0.567   1.00 18.90 ? 198 ARG   B CB  1 
ATOM   3231 C CG  . ARG   B 1 219 ? -8.905  -11.716 0.419   1.00 18.47 ? 198 ARG   B CG  1 
ATOM   3232 C CD  . ARG   B 1 219 ? -7.562  -11.300 -0.170  1.00 21.05 ? 198 ARG   B CD  1 
ATOM   3233 N NE  . ARG   B 1 219 ? -7.687  -10.672 -1.496  1.00 22.37 ? 198 ARG   B NE  1 
ATOM   3234 C CZ  . ARG   B 1 219 ? -7.630  -9.346  -1.710  1.00 23.68 ? 198 ARG   B CZ  1 
ATOM   3235 N NH1 . ARG   B 1 219 ? -7.380  -8.509  -0.714  1.00 22.28 ? 198 ARG   B NH1 1 
ATOM   3236 N NH2 . ARG   B 1 219 ? -7.845  -8.840  -2.911  1.00 22.18 ? 198 ARG   B NH2 1 
ATOM   3237 N N   . VAL   B 1 220 ? -12.145 -9.306  2.519   1.00 19.88 ? 199 VAL   B N   1 
ATOM   3238 C CA  . VAL   B 1 220 ? -13.015 -8.180  2.843   1.00 18.39 ? 199 VAL   B CA  1 
ATOM   3239 C C   . VAL   B 1 220 ? -12.175 -7.168  3.615   1.00 17.92 ? 199 VAL   B C   1 
ATOM   3240 O O   . VAL   B 1 220 ? -11.645 -7.491  4.682   1.00 18.52 ? 199 VAL   B O   1 
ATOM   3241 C CB  . VAL   B 1 220 ? -14.269 -8.605  3.639   1.00 17.88 ? 199 VAL   B CB  1 
ATOM   3242 C CG1 . VAL   B 1 220 ? -15.190 -7.411  3.869   1.00 17.08 ? 199 VAL   B CG1 1 
ATOM   3243 C CG2 . VAL   B 1 220 ? -15.037 -9.759  2.985   1.00 16.15 ? 199 VAL   B CG2 1 
ATOM   3244 N N   . ASN   B 1 221 ? -12.118 -5.924  3.113   1.00 18.67 ? 200 ASN   B N   1 
ATOM   3245 C CA  . ASN   B 1 221 ? -11.210 -4.940  3.677   1.00 18.82 ? 200 ASN   B CA  1 
ATOM   3246 C C   . ASN   B 1 221 ? -11.874 -3.578  3.656   1.00 19.30 ? 200 ASN   B C   1 
ATOM   3247 O O   . ASN   B 1 221 ? -12.970 -3.429  3.136   1.00 20.55 ? 200 ASN   B O   1 
ATOM   3248 C CB  . ASN   B 1 221 ? -9.882  -4.847  2.919   1.00 17.89 ? 200 ASN   B CB  1 
ATOM   3249 C CG  . ASN   B 1 221 ? -9.058  -6.100  3.064   1.00 19.48 ? 200 ASN   B CG  1 
ATOM   3250 O OD1 . ASN   B 1 221 ? -8.573  -6.402  4.162   1.00 20.22 ? 200 ASN   B OD1 1 
ATOM   3251 N ND2 . ASN   B 1 221 ? -8.897  -6.843  1.978   1.00 20.64 ? 200 ASN   B ND2 1 
ATOM   3252 N N   . GLY   B 1 222 ? -11.184 -2.590  4.227   1.00 18.81 ? 201 GLY   B N   1 
ATOM   3253 C CA  . GLY   B 1 222 ? -11.766 -1.262  4.228   1.00 19.00 ? 201 GLY   B CA  1 
ATOM   3254 C C   . GLY   B 1 222 ? -10.709 -0.232  3.866   1.00 20.30 ? 201 GLY   B C   1 
ATOM   3255 O O   . GLY   B 1 222 ? -9.502  -0.475  4.022   1.00 21.70 ? 201 GLY   B O   1 
ATOM   3256 N N   . VAL   B 1 223 ? -11.206 0.924   3.432   1.00 19.16 ? 202 VAL   B N   1 
ATOM   3257 C CA  . VAL   B 1 223 ? -10.396 2.106   3.214   1.00 19.94 ? 202 VAL   B CA  1 
ATOM   3258 C C   . VAL   B 1 223 ? -11.054 3.189   4.043   1.00 20.36 ? 202 VAL   B C   1 
ATOM   3259 O O   . VAL   B 1 223 ? -12.261 3.339   3.952   1.00 21.41 ? 202 VAL   B O   1 
ATOM   3260 C CB  . VAL   B 1 223 ? -10.267 2.500   1.722   1.00 18.59 ? 202 VAL   B CB  1 
ATOM   3261 C CG1 . VAL   B 1 223 ? -9.655  3.886   1.537   1.00 19.11 ? 202 VAL   B CG1 1 
ATOM   3262 C CG2 . VAL   B 1 223 ? -9.476  1.473   0.916   1.00 19.01 ? 202 VAL   B CG2 1 
ATOM   3263 N N   . ALA   B 1 224 ? -10.251 3.926   4.836   1.00 20.70 ? 203 ALA   B N   1 
ATOM   3264 C CA  . ALA   B 1 224 ? -10.801 4.885   5.787   1.00 19.98 ? 203 ALA   B CA  1 
ATOM   3265 C C   . ALA   B 1 224 ? -10.234 6.275   5.499   1.00 21.04 ? 203 ALA   B C   1 
ATOM   3266 O O   . ALA   B 1 224 ? -9.133  6.603   5.971   1.00 20.00 ? 203 ALA   B O   1 
ATOM   3267 C CB  . ALA   B 1 224 ? -10.459 4.452   7.224   1.00 17.80 ? 203 ALA   B CB  1 
ATOM   3268 N N   . PRO   B 1 225 ? -10.936 7.100   4.690   1.00 20.62 ? 204 PRO   B N   1 
ATOM   3269 C CA  . PRO   B 1 225 ? -10.515 8.475   4.429   1.00 21.39 ? 204 PRO   B CA  1 
ATOM   3270 C C   . PRO   B 1 225 ? -10.588 9.333   5.683   1.00 22.86 ? 204 PRO   B C   1 
ATOM   3271 O O   . PRO   B 1 225 ? -11.417 9.111   6.576   1.00 22.64 ? 204 PRO   B O   1 
ATOM   3272 C CB  . PRO   B 1 225 ? -11.543 8.990   3.387   1.00 21.48 ? 204 PRO   B CB  1 
ATOM   3273 C CG  . PRO   B 1 225 ? -12.149 7.711   2.772   1.00 23.76 ? 204 PRO   B CG  1 
ATOM   3274 C CD  . PRO   B 1 225 ? -12.160 6.720   3.941   1.00 23.14 ? 204 PRO   B CD  1 
ATOM   3275 N N   . GLY   B 1 226 ? -9.768  10.384  5.697   1.00 23.46 ? 205 GLY   B N   1 
ATOM   3276 C CA  . GLY   B 1 226 ? -9.907  11.400  6.716   1.00 24.56 ? 205 GLY   B CA  1 
ATOM   3277 C C   . GLY   B 1 226 ? -10.760 12.533  6.162   1.00 32.96 ? 205 GLY   B C   1 
ATOM   3278 O O   . GLY   B 1 226 ? -11.993 12.512  6.229   1.00 35.22 ? 205 GLY   B O   1 
ATOM   3279 N N   . VAL   B 1 227 ? -10.082 13.555  5.658   1.00 29.32 ? 206 VAL   B N   1 
ATOM   3280 C CA  A VAL   B 1 227 ? -10.773 14.536  4.835   0.70 28.70 ? 206 VAL   B CA  1 
ATOM   3281 C CA  B VAL   B 1 227 ? -10.743 14.559  4.843   0.30 27.33 ? 206 VAL   B CA  1 
ATOM   3282 C C   . VAL   B 1 227 ? -10.293 14.336  3.403   1.00 27.41 ? 206 VAL   B C   1 
ATOM   3283 O O   . VAL   B 1 227 ? -9.090  14.317  3.122   1.00 27.14 ? 206 VAL   B O   1 
ATOM   3284 C CB  A VAL   B 1 227 ? -10.704 16.009  5.279   0.70 30.62 ? 206 VAL   B CB  1 
ATOM   3285 C CB  B VAL   B 1 227 ? -10.429 15.989  5.322   0.30 25.72 ? 206 VAL   B CB  1 
ATOM   3286 C CG1 A VAL   B 1 227 ? -11.619 16.291  6.464   0.70 29.65 ? 206 VAL   B CG1 1 
ATOM   3287 C CG1 B VAL   B 1 227 ? -9.060  16.449  4.849   0.30 25.12 ? 206 VAL   B CG1 1 
ATOM   3288 C CG2 A VAL   B 1 227 ? -9.290  16.461  5.583   0.70 30.80 ? 206 VAL   B CG2 1 
ATOM   3289 C CG2 B VAL   B 1 227 ? -11.500 16.978  4.876   0.30 23.59 ? 206 VAL   B CG2 1 
ATOM   3290 N N   . SER   B 1 228 ? -11.265 14.113  2.527   1.00 30.95 ? 207 SER   B N   1 
ATOM   3291 C CA  . SER   B 1 228 ? -11.010 14.009  1.109   1.00 33.41 ? 207 SER   B CA  1 
ATOM   3292 C C   . SER   B 1 228 ? -11.785 15.158  0.459   1.00 41.39 ? 207 SER   B C   1 
ATOM   3293 O O   . SER   B 1 228 ? -11.919 16.211  1.079   1.00 47.44 ? 207 SER   B O   1 
ATOM   3294 C CB  . SER   B 1 228 ? -11.341 12.639  0.591   1.00 30.47 ? 207 SER   B CB  1 
ATOM   3295 O OG  . SER   B 1 228 ? -10.956 12.500  -0.781  1.00 35.62 ? 207 SER   B OG  1 
ATOM   3296 N N   . LEU   B 1 229 ? -12.255 14.977  -0.778  1.00 44.01 ? 208 LEU   B N   1 
ATOM   3297 C CA  . LEU   B 1 229 ? -12.944 16.032  -1.507  1.00 44.19 ? 208 LEU   B CA  1 
ATOM   3298 C C   . LEU   B 1 229 ? -13.992 16.622  -0.587  1.00 44.75 ? 208 LEU   B C   1 
ATOM   3299 O O   . LEU   B 1 229 ? -14.882 15.900  -0.133  1.00 46.19 ? 208 LEU   B O   1 
ATOM   3300 C CB  . LEU   B 1 229 ? -13.640 15.428  -2.722  1.00 45.70 ? 208 LEU   B CB  1 
ATOM   3301 C CG  . LEU   B 1 229 ? -12.738 14.986  -3.876  1.00 53.63 ? 208 LEU   B CG  1 
ATOM   3302 C CD1 . LEU   B 1 229 ? -13.642 14.925  -5.107  1.00 50.39 ? 208 LEU   B CD1 1 
ATOM   3303 C CD2 . LEU   B 1 229 ? -11.515 15.885  -4.101  1.00 53.96 ? 208 LEU   B CD2 1 
ATOM   3304 N N   . LEU   B 1 230 ? -13.834 17.905  -0.267  1.00 37.15 ? 209 LEU   B N   1 
ATOM   3305 C CA  . LEU   B 1 230 ? -14.829 18.568  0.552   1.00 36.70 ? 209 LEU   B CA  1 
ATOM   3306 C C   . LEU   B 1 230 ? -15.967 19.002  -0.370  1.00 44.50 ? 209 LEU   B C   1 
ATOM   3307 O O   . LEU   B 1 230 ? -15.748 19.169  -1.563  1.00 48.38 ? 209 LEU   B O   1 
ATOM   3308 C CB  . LEU   B 1 230 ? -14.143 19.739  1.258   1.00 38.24 ? 209 LEU   B CB  1 
ATOM   3309 C CG  . LEU   B 1 230 ? -13.059 19.342  2.268   1.00 39.79 ? 209 LEU   B CG  1 
ATOM   3310 C CD1 . LEU   B 1 230 ? -11.980 20.388  2.455   1.00 40.33 ? 209 LEU   B CD1 1 
ATOM   3311 C CD2 . LEU   B 1 230 ? -13.744 19.010  3.597   1.00 41.43 ? 209 LEU   B CD2 1 
ATOM   3312 N N   . PRO   B 1 231 ? -17.213 19.179  0.122   1.00 47.49 ? 210 PRO   B N   1 
ATOM   3313 C CA  . PRO   B 1 231 ? -18.300 19.724  -0.713  1.00 50.40 ? 210 PRO   B CA  1 
ATOM   3314 C C   . PRO   B 1 231 ? -17.909 20.944  -1.552  1.00 52.78 ? 210 PRO   B C   1 
ATOM   3315 O O   . PRO   B 1 231 ? -17.276 21.872  -1.037  1.00 46.04 ? 210 PRO   B O   1 
ATOM   3316 C CB  . PRO   B 1 231 ? -19.369 20.082  0.331   1.00 52.28 ? 210 PRO   B CB  1 
ATOM   3317 C CG  . PRO   B 1 231 ? -19.139 19.085  1.457   1.00 49.38 ? 210 PRO   B CG  1 
ATOM   3318 C CD  . PRO   B 1 231 ? -17.637 18.845  1.495   1.00 49.34 ? 210 PRO   B CD  1 
ATOM   3319 N N   . VAL   B 1 232 ? -18.299 20.931  -2.842  1.00 51.98 ? 211 VAL   B N   1 
ATOM   3320 C CA  . VAL   B 1 232 ? -17.965 21.987  -3.795  1.00 57.68 ? 211 VAL   B CA  1 
ATOM   3321 C C   . VAL   B 1 232 ? -18.405 23.347  -3.238  1.00 52.48 ? 211 VAL   B C   1 
ATOM   3322 O O   . VAL   B 1 232 ? -17.664 24.336  -3.342  1.00 47.76 ? 211 VAL   B O   1 
ATOM   3323 C CB  . VAL   B 1 232 ? -18.534 21.734  -5.209  1.00 51.42 ? 211 VAL   B CB  1 
ATOM   3324 N N   . ALA   B 1 233 ? -19.558 23.327  -2.545  1.00 47.64 ? 212 ALA   B N   1 
ATOM   3325 C CA  . ALA   B 1 233 ? -20.295 24.486  -2.061  1.00 49.87 ? 212 ALA   B CA  1 
ATOM   3326 C C   . ALA   B 1 233 ? -19.766 25.037  -0.732  1.00 48.40 ? 212 ALA   B C   1 
ATOM   3327 O O   . ALA   B 1 233 ? -20.046 26.193  -0.403  1.00 39.84 ? 212 ALA   B O   1 
ATOM   3328 C CB  . ALA   B 1 233 ? -21.763 24.130  -1.934  1.00 51.53 ? 212 ALA   B CB  1 
ATOM   3329 N N   . MET   B 1 234 ? -19.044 24.218  0.051   1.00 44.77 ? 213 MET   B N   1 
ATOM   3330 C CA  . MET   B 1 234 ? -18.393 24.694  1.271   1.00 42.47 ? 213 MET   B CA  1 
ATOM   3331 C C   . MET   B 1 234 ? -17.441 25.847  0.925   1.00 38.55 ? 213 MET   B C   1 
ATOM   3332 O O   . MET   B 1 234 ? -16.597 25.709  0.039   1.00 37.34 ? 213 MET   B O   1 
ATOM   3333 C CB  . MET   B 1 234 ? -17.610 23.546  1.941   1.00 41.26 ? 213 MET   B CB  1 
ATOM   3334 C CG  . MET   B 1 234 ? -16.750 23.923  3.158   1.00 44.84 ? 213 MET   B CG  1 
ATOM   3335 S SD  . MET   B 1 234 ? -15.898 22.535  3.961   1.00 43.18 ? 213 MET   B SD  1 
ATOM   3336 C CE  . MET   B 1 234 ? -17.259 21.678  4.784   1.00 47.16 ? 213 MET   B CE  1 
ATOM   3337 N N   . GLY   B 1 235 ? -17.550 26.970  1.645   1.00 37.00 ? 214 GLY   B N   1 
ATOM   3338 C CA  . GLY   B 1 235 ? -16.618 28.088  1.480   1.00 36.12 ? 214 GLY   B CA  1 
ATOM   3339 C C   . GLY   B 1 235 ? -15.158 27.627  1.574   1.00 36.65 ? 214 GLY   B C   1 
ATOM   3340 O O   . GLY   B 1 235 ? -14.844 26.711  2.352   1.00 31.98 ? 214 GLY   B O   1 
ATOM   3341 N N   . GLU   B 1 236 ? -14.270 28.257  0.776   1.00 32.24 ? 215 GLU   B N   1 
ATOM   3342 C CA  . GLU   B 1 236 ? -12.842 27.944  0.826   1.00 36.78 ? 215 GLU   B CA  1 
ATOM   3343 C C   . GLU   B 1 236 ? -12.287 28.154  2.239   1.00 35.30 ? 215 GLU   B C   1 
ATOM   3344 O O   . GLU   B 1 236 ? -11.407 27.403  2.666   1.00 31.88 ? 215 GLU   B O   1 
ATOM   3345 C CB  . GLU   B 1 236 ? -11.979 28.672  -0.219  1.00 32.57 ? 215 GLU   B CB  1 
ATOM   3346 C CG  . GLU   B 1 236 ? -12.218 28.189  -1.645  1.00 34.03 ? 215 GLU   B CG  1 
ATOM   3347 C CD  . GLU   B 1 236 ? -11.775 26.744  -1.835  1.00 37.61 ? 215 GLU   B CD  1 
ATOM   3348 O OE1 . GLU   B 1 236 ? -12.569 25.958  -2.410  1.00 39.62 ? 215 GLU   B OE1 1 
ATOM   3349 O OE2 . GLU   B 1 236 ? -10.644 26.402  -1.388  1.00 33.33 ? 215 GLU   B OE2 1 
ATOM   3350 N N   . GLU   B 1 237 ? -12.783 29.187  2.946   1.00 32.00 ? 216 GLU   B N   1 
ATOM   3351 C CA  . GLU   B 1 237 ? -12.282 29.530  4.275   1.00 34.60 ? 216 GLU   B CA  1 
ATOM   3352 C C   . GLU   B 1 237 ? -12.628 28.413  5.278   1.00 34.81 ? 216 GLU   B C   1 
ATOM   3353 O O   . GLU   B 1 237 ? -11.844 28.121  6.190   1.00 34.32 ? 216 GLU   B O   1 
ATOM   3354 C CB  . GLU   B 1 237 ? -12.714 30.944  4.690   1.00 34.61 ? 216 GLU   B CB  1 
ATOM   3355 C CG  . GLU   B 1 237 ? -14.210 31.074  4.989   0.80 33.31 ? 216 GLU   B CG  1 
ATOM   3356 C CD  . GLU   B 1 237 ? -15.307 30.944  3.931   0.80 37.31 ? 216 GLU   B CD  1 
ATOM   3357 O OE1 . GLU   B 1 237 ? -16.425 30.809  4.449   0.80 35.27 ? 216 GLU   B OE1 1 
ATOM   3358 O OE2 . GLU   B 1 237 ? -15.150 30.968  2.671   0.80 30.02 ? 216 GLU   B OE2 1 
ATOM   3359 N N   . GLU   B 1 238 ? -13.793 27.773  5.087   1.00 31.88 ? 217 GLU   B N   1 
ATOM   3360 C CA  . GLU   B 1 238 ? -14.169 26.592  5.858   1.00 35.25 ? 217 GLU   B CA  1 
ATOM   3361 C C   . GLU   B 1 238 ? -13.302 25.379  5.471   1.00 39.06 ? 217 GLU   B C   1 
ATOM   3362 O O   . GLU   B 1 238 ? -12.819 24.639  6.334   1.00 32.65 ? 217 GLU   B O   1 
ATOM   3363 C CB  . GLU   B 1 238 ? -15.683 26.414  5.726   1.00 39.14 ? 217 GLU   B CB  1 
ATOM   3364 C CG  . GLU   B 1 238 ? -16.229 25.172  6.416   1.00 51.78 ? 217 GLU   B CG  1 
ATOM   3365 C CD  . GLU   B 1 238 ? -16.202 25.183  7.931   1.00 61.25 ? 217 GLU   B CD  1 
ATOM   3366 O OE1 . GLU   B 1 238 ? -16.567 24.134  8.506   1.00 72.93 ? 217 GLU   B OE1 1 
ATOM   3367 O OE2 . GLU   B 1 238 ? -15.843 26.218  8.540   1.00 62.51 ? 217 GLU   B OE2 1 
ATOM   3368 N N   . LYS   B 1 239 ? -13.111 25.158  4.165   1.00 34.21 ? 218 LYS   B N   1 
ATOM   3369 C CA  . LYS   B 1 239 ? -12.315 24.043  3.675   1.00 34.81 ? 218 LYS   B CA  1 
ATOM   3370 C C   . LYS   B 1 239 ? -10.913 24.132  4.276   1.00 35.89 ? 218 LYS   B C   1 
ATOM   3371 O O   . LYS   B 1 239 ? -10.332 23.113  4.662   1.00 32.91 ? 218 LYS   B O   1 
ATOM   3372 C CB  . LYS   B 1 239 ? -12.193 24.021  2.143   1.00 34.23 ? 218 LYS   B CB  1 
ATOM   3373 C CG  . LYS   B 1 239 ? -13.446 23.676  1.318   1.00 31.40 ? 218 LYS   B CG  1 
ATOM   3374 C CD  . LYS   B 1 239 ? -13.085 23.432  -0.147  1.00 35.42 ? 218 LYS   B CD  1 
ATOM   3375 C CE  . LYS   B 1 239 ? -14.194 23.157  -1.156  1.00 34.41 ? 218 LYS   B CE  1 
ATOM   3376 N NZ  . LYS   B 1 239 ? -14.855 24.377  -1.633  1.00 33.99 ? 218 LYS   B NZ  1 
ATOM   3377 N N   . ASP   B 1 240 ? -10.399 25.366  4.366   1.00 31.08 ? 219 ASP   B N   1 
ATOM   3378 C CA  . ASP   B 1 240 ? -9.050  25.609  4.863   1.00 36.70 ? 219 ASP   B CA  1 
ATOM   3379 C C   . ASP   B 1 240 ? -8.901  25.283  6.349   1.00 35.64 ? 219 ASP   B C   1 
ATOM   3380 O O   . ASP   B 1 240 ? -7.794  24.939  6.776   1.00 33.82 ? 219 ASP   B O   1 
ATOM   3381 C CB  . ASP   B 1 240 ? -8.606  27.041  4.629   1.00 39.00 ? 219 ASP   B CB  1 
ATOM   3382 C CG  . ASP   B 1 240 ? -8.178  27.329  3.200   1.00 41.15 ? 219 ASP   B CG  1 
ATOM   3383 O OD1 . ASP   B 1 240 ? -8.119  26.373  2.382   1.00 39.87 ? 219 ASP   B OD1 1 
ATOM   3384 O OD2 . ASP   B 1 240 ? -7.935  28.513  2.915   1.00 42.01 ? 219 ASP   B OD2 1 
ATOM   3385 N N   . LYS   B 1 241 ? -9.987  25.471  7.128   1.00 36.31 ? 220 LYS   B N   1 
ATOM   3386 C CA  . LYS   B 1 241 ? -10.027 25.031  8.522   1.00 36.63 ? 220 LYS   B CA  1 
ATOM   3387 C C   . LYS   B 1 241 ? -9.686  23.539  8.613   1.00 38.24 ? 220 LYS   B C   1 
ATOM   3388 O O   . LYS   B 1 241 ? -8.901  23.132  9.468   1.00 37.44 ? 220 LYS   B O   1 
ATOM   3389 C CB  . LYS   B 1 241 ? -11.353 25.314  9.241   1.00 36.43 ? 220 LYS   B CB  1 
ATOM   3390 C CG  . LYS   B 1 241 ? -11.693 26.771  9.555   1.00 45.55 ? 220 LYS   B CG  1 
ATOM   3391 C CD  . LYS   B 1 241 ? -12.849 26.927  10.542  1.00 44.33 ? 220 LYS   B CD  1 
ATOM   3392 C CE  . LYS   B 1 241 ? -13.059 28.346  10.969  0.50 44.35 ? 220 LYS   B CE  1 
ATOM   3393 N NZ  . LYS   B 1 241 ? -13.262 29.208  9.803   0.50 43.61 ? 220 LYS   B NZ  1 
ATOM   3394 N N   . TRP   B 1 242 ? -10.282 22.719  7.741   1.00 34.82 ? 221 TRP   B N   1 
ATOM   3395 C CA  . TRP   B 1 242 ? -9.988  21.293  7.746   1.00 35.27 ? 221 TRP   B CA  1 
ATOM   3396 C C   . TRP   B 1 242 ? -8.596  21.032  7.201   1.00 34.09 ? 221 TRP   B C   1 
ATOM   3397 O O   . TRP   B 1 242 ? -7.852  20.229  7.756   1.00 32.89 ? 221 TRP   B O   1 
ATOM   3398 C CB  . TRP   B 1 242 ? -11.048 20.517  6.960   1.00 34.80 ? 221 TRP   B CB  1 
ATOM   3399 C CG  . TRP   B 1 242 ? -12.339 20.525  7.722   1.00 48.41 ? 221 TRP   B CG  1 
ATOM   3400 C CD1 . TRP   B 1 242 ? -13.398 21.368  7.547   1.00 50.15 ? 221 TRP   B CD1 1 
ATOM   3401 C CD2 . TRP   B 1 242 ? -12.650 19.701  8.868   1.00 53.65 ? 221 TRP   B CD2 1 
ATOM   3402 N NE1 . TRP   B 1 242 ? -14.355 21.111  8.495   1.00 49.61 ? 221 TRP   B NE1 1 
ATOM   3403 C CE2 . TRP   B 1 242 ? -13.930 20.098  9.316   1.00 53.29 ? 221 TRP   B CE2 1 
ATOM   3404 C CE3 . TRP   B 1 242 ? -11.980 18.670  9.545   1.00 56.30 ? 221 TRP   B CE3 1 
ATOM   3405 C CZ2 . TRP   B 1 242 ? -14.555 19.491  10.406  1.00 54.97 ? 221 TRP   B CZ2 1 
ATOM   3406 C CZ3 . TRP   B 1 242 ? -12.594 18.076  10.628  1.00 60.90 ? 221 TRP   B CZ3 1 
ATOM   3407 C CH2 . TRP   B 1 242 ? -13.862 18.487  11.052  1.00 63.44 ? 221 TRP   B CH2 1 
ATOM   3408 N N   . ARG   B 1 243 ? -8.269  21.680  6.095   1.00 29.29 ? 222 ARG   B N   1 
ATOM   3409 C CA  . ARG   B 1 243 ? -6.964  21.437  5.443   1.00 31.83 ? 222 ARG   B CA  1 
ATOM   3410 C C   . ARG   B 1 243 ? -5.843  21.741  6.436   1.00 30.17 ? 222 ARG   B C   1 
ATOM   3411 O O   . ARG   B 1 243 ? -4.915  20.953  6.515   1.00 31.44 ? 222 ARG   B O   1 
ATOM   3412 C CB  . ARG   B 1 243 ? -6.861  22.316  4.194   1.00 29.39 ? 222 ARG   B CB  1 
ATOM   3413 C CG  . ARG   B 1 243 ? -7.797  21.924  3.064   1.00 29.44 ? 222 ARG   B CG  1 
ATOM   3414 C CD  . ARG   B 1 243 ? -7.767  22.988  1.987   1.00 30.30 ? 222 ARG   B CD  1 
ATOM   3415 N NE  . ARG   B 1 243 ? -8.584  22.599  0.836   1.00 33.52 ? 222 ARG   B NE  1 
ATOM   3416 C CZ  . ARG   B 1 243 ? -9.203  23.433  0.021   1.00 32.90 ? 222 ARG   B CZ  1 
ATOM   3417 N NH1 . ARG   B 1 243 ? -9.235  24.725  0.283   1.00 29.95 ? 222 ARG   B NH1 1 
ATOM   3418 N NH2 . ARG   B 1 243 ? -9.790  22.963  -1.059  1.00 32.67 ? 222 ARG   B NH2 1 
ATOM   3419 N N   . ARG   B 1 244 ? -5.984  22.818  7.200   1.00 29.11 ? 223 ARG   B N   1 
ATOM   3420 C CA  . ARG   B 1 244 ? -4.924  23.235  8.102   1.00 32.71 ? 223 ARG   B CA  1 
ATOM   3421 C C   . ARG   B 1 244 ? -4.654  22.172  9.174   1.00 33.13 ? 223 ARG   B C   1 
ATOM   3422 O O   . ARG   B 1 244 ? -3.573  22.144  9.742   1.00 39.01 ? 223 ARG   B O   1 
ATOM   3423 C CB  . ARG   B 1 244 ? -5.226  24.589  8.763   1.00 35.32 ? 223 ARG   B CB  1 
ATOM   3424 C CG  . ARG   B 1 244 ? -4.812  25.739  7.852   0.50 36.51 ? 223 ARG   B CG  1 
ATOM   3425 C CD  . ARG   B 1 244 ? -4.822  27.103  8.524   0.50 37.12 ? 223 ARG   B CD  1 
ATOM   3426 N NE  . ARG   B 1 244 ? -6.186  27.414  8.963   0.50 40.54 ? 223 ARG   B NE  1 
ATOM   3427 C CZ  . ARG   B 1 244 ? -6.988  28.217  8.279   0.50 36.37 ? 223 ARG   B CZ  1 
ATOM   3428 N NH1 . ARG   B 1 244 ? -6.524  28.846  7.218   0.50 34.38 ? 223 ARG   B NH1 1 
ATOM   3429 N NH2 . ARG   B 1 244 ? -8.247  28.365  8.650   0.50 37.32 ? 223 ARG   B NH2 1 
ATOM   3430 N N   . LYS   B 1 245 ? -5.627  21.313  9.463   1.00 28.28 ? 224 LYS   B N   1 
ATOM   3431 C CA  . LYS   B 1 245 ? -5.429  20.332  10.523  1.00 29.04 ? 224 LYS   B CA  1 
ATOM   3432 C C   . LYS   B 1 245 ? -4.655  19.106  10.029  1.00 24.28 ? 224 LYS   B C   1 
ATOM   3433 O O   . LYS   B 1 245 ? -4.231  18.282  10.839  1.00 28.22 ? 224 LYS   B O   1 
ATOM   3434 C CB  . LYS   B 1 245 ? -6.784  19.801  10.993  1.00 30.28 ? 224 LYS   B CB  1 
ATOM   3435 C CG  . LYS   B 1 245 ? -7.817  20.822  11.470  1.00 33.67 ? 224 LYS   B CG  1 
ATOM   3436 C CD  . LYS   B 1 245 ? -9.118  20.106  11.836  0.70 35.95 ? 224 LYS   B CD  1 
ATOM   3437 C CE  . LYS   B 1 245 ? -10.263 21.049  12.113  0.70 38.83 ? 224 LYS   B CE  1 
ATOM   3438 N NZ  . LYS   B 1 245 ? -9.848  21.996  13.155  0.70 39.39 ? 224 LYS   B NZ  1 
ATOM   3439 N N   . VAL   B 1 246 ? -4.473  18.943  8.713   1.00 23.67 ? 225 VAL   B N   1 
ATOM   3440 C CA  . VAL   B 1 246 ? -3.883  17.704  8.212   1.00 22.38 ? 225 VAL   B CA  1 
ATOM   3441 C C   . VAL   B 1 246 ? -2.358  17.784  8.226   1.00 25.12 ? 225 VAL   B C   1 
ATOM   3442 O O   . VAL   B 1 246 ? -1.768  18.595  7.502   1.00 25.04 ? 225 VAL   B O   1 
ATOM   3443 C CB  . VAL   B 1 246 ? -4.350  17.398  6.772   1.00 24.96 ? 225 VAL   B CB  1 
ATOM   3444 C CG1 . VAL   B 1 246 ? -3.618  16.175  6.227   1.00 20.32 ? 225 VAL   B CG1 1 
ATOM   3445 C CG2 . VAL   B 1 246 ? -5.877  17.294  6.693   1.00 23.85 ? 225 VAL   B CG2 1 
ATOM   3446 N N   . PRO   B 1 247 ? -1.658  16.911  8.995   1.00 24.79 ? 226 PRO   B N   1 
ATOM   3447 C CA  . PRO   B 1 247 ? -0.189  16.958  9.033   1.00 26.14 ? 226 PRO   B CA  1 
ATOM   3448 C C   . PRO   B 1 247 ? 0.506   16.868  7.677   1.00 26.06 ? 226 PRO   B C   1 
ATOM   3449 O O   . PRO   B 1 247 ? 1.452   17.613  7.409   1.00 25.22 ? 226 PRO   B O   1 
ATOM   3450 C CB  . PRO   B 1 247 ? 0.161   15.773  9.960   1.00 23.99 ? 226 PRO   B CB  1 
ATOM   3451 C CG  . PRO   B 1 247 ? -1.040  15.729  10.914  1.00 21.59 ? 226 PRO   B CG  1 
ATOM   3452 C CD  . PRO   B 1 247 ? -2.237  15.953  9.968   1.00 21.45 ? 226 PRO   B CD  1 
ATOM   3453 N N   . LEU   B 1 248 ? 0.055   15.947  6.828   1.00 23.13 ? 227 LEU   B N   1 
ATOM   3454 C CA  . LEU   B 1 248 ? 0.776   15.676  5.597   1.00 27.38 ? 227 LEU   B CA  1 
ATOM   3455 C C   . LEU   B 1 248 ? 0.314   16.631  4.488   1.00 30.20 ? 227 LEU   B C   1 
ATOM   3456 O O   . LEU   B 1 248 ? -0.565  16.295  3.700   1.00 27.61 ? 227 LEU   B O   1 
ATOM   3457 C CB  . LEU   B 1 248 ? 0.632   14.202  5.206   1.00 24.86 ? 227 LEU   B CB  1 
ATOM   3458 C CG  . LEU   B 1 248 ? 1.528   13.749  4.047   1.00 28.17 ? 227 LEU   B CG  1 
ATOM   3459 C CD1 . LEU   B 1 248 ? 3.007   13.760  4.464   1.00 27.41 ? 227 LEU   B CD1 1 
ATOM   3460 C CD2 . LEU   B 1 248 ? 1.085   12.351  3.551   1.00 27.19 ? 227 LEU   B CD2 1 
ATOM   3461 N N   . GLY   B 1 249 ? 0.866   17.849  4.482   1.00 30.31 ? 228 GLY   B N   1 
ATOM   3462 C CA  . GLY   B 1 249 ? 0.692   18.770  3.370   1.00 31.95 ? 228 GLY   B CA  1 
ATOM   3463 C C   . GLY   B 1 249 ? -0.446  19.775  3.541   1.00 30.12 ? 228 GLY   B C   1 
ATOM   3464 O O   . GLY   B 1 249 ? -0.701  20.556  2.633   1.00 26.42 ? 228 GLY   B O   1 
ATOM   3465 N N   . ARG   B 1 250 ? -1.149  19.741  4.685   1.00 27.91 ? 229 ARG   B N   1 
ATOM   3466 C CA  . ARG   B 1 250 ? -2.225  20.663  5.000   1.00 29.04 ? 229 ARG   B CA  1 
ATOM   3467 C C   . ARG   B 1 250 ? -3.205  20.722  3.827   1.00 28.68 ? 229 ARG   B C   1 
ATOM   3468 O O   . ARG   B 1 250 ? -3.638  21.796  3.406   1.00 27.76 ? 229 ARG   B O   1 
ATOM   3469 C CB  . ARG   B 1 250 ? -1.721  22.058  5.427   1.00 32.09 ? 229 ARG   B CB  1 
ATOM   3470 C CG  . ARG   B 1 250 ? -0.507  22.141  6.342   0.60 34.80 ? 229 ARG   B CG  1 
ATOM   3471 C CD  . ARG   B 1 250 ? -0.911  21.575  7.664   0.60 38.04 ? 229 ARG   B CD  1 
ATOM   3472 N NE  . ARG   B 1 250 ? 0.017   21.913  8.748   0.60 42.08 ? 229 ARG   B NE  1 
ATOM   3473 C CZ  . ARG   B 1 250 ? -0.171  21.503  9.994   0.60 43.10 ? 229 ARG   B CZ  1 
ATOM   3474 N NH1 . ARG   B 1 250 ? -1.145  20.656  10.275  0.60 39.84 ? 229 ARG   B NH1 1 
ATOM   3475 N NH2 . ARG   B 1 250 ? 0.626   21.929  10.953  0.60 50.97 ? 229 ARG   B NH2 1 
ATOM   3476 N N   . ARG   B 1 251 ? -3.492  19.546  3.337   1.00 25.81 ? 230 ARG   B N   1 
ATOM   3477 C CA  A ARG   B 1 251 ? -4.493  19.386  2.251   0.50 26.51 ? 230 ARG   B CA  1 
ATOM   3478 C CA  B ARG   B 1 251 ? -4.514  19.400  2.273   0.50 27.43 ? 230 ARG   B CA  1 
ATOM   3479 C C   . ARG   B 1 251 ? -5.358  18.072  2.382   1.00 27.93 ? 230 ARG   B C   1 
ATOM   3480 O O   . ARG   B 1 251 ? -5.041  16.989  3.030   1.00 23.27 ? 230 ARG   B O   1 
ATOM   3481 C CB  A ARG   B 1 251 ? -3.762  19.361  0.907   0.50 25.59 ? 230 ARG   B CB  1 
ATOM   3482 C CB  B ARG   B 1 251 ? -3.804  19.494  0.922   0.50 28.86 ? 230 ARG   B CB  1 
ATOM   3483 C CG  A ARG   B 1 251 ? -3.015  18.059  0.661   0.50 26.18 ? 230 ARG   B CG  1 
ATOM   3484 C CG  B ARG   B 1 251 ? -2.845  18.366  0.580   0.50 33.28 ? 230 ARG   B CG  1 
ATOM   3485 C CD  A ARG   B 1 251 ? -1.932  18.229  -0.386  0.50 27.41 ? 230 ARG   B CD  1 
ATOM   3486 C CD  B ARG   B 1 251 ? -2.540  18.524  -0.892  0.50 36.36 ? 230 ARG   B CD  1 
ATOM   3487 N NE  A ARG   B 1 251 ? -1.221  19.499  -0.206  0.50 31.70 ? 230 ARG   B NE  1 
ATOM   3488 N NE  B ARG   B 1 251 ? -3.793  18.407  -1.646  0.50 40.55 ? 230 ARG   B NE  1 
ATOM   3489 C CZ  A ARG   B 1 251 ? -0.006  19.763  -0.663  0.50 30.85 ? 230 ARG   B CZ  1 
ATOM   3490 C CZ  B ARG   B 1 251 ? -4.272  19.286  -2.516  0.50 42.95 ? 230 ARG   B CZ  1 
ATOM   3491 N NH1 A ARG   B 1 251 ? 0.631   18.874  -1.401  0.50 32.92 ? 230 ARG   B NH1 1 
ATOM   3492 N NH1 B ARG   B 1 251 ? -3.575  20.365  -2.823  0.50 42.71 ? 230 ARG   B NH1 1 
ATOM   3493 N NH2 A ARG   B 1 251 ? 0.565   20.921  -0.383  0.50 30.29 ? 230 ARG   B NH2 1 
ATOM   3494 N NH2 B ARG   B 1 251 ? -5.453  19.081  -3.072  0.50 46.31 ? 230 ARG   B NH2 1 
ATOM   3495 N N   . GLU   B 1 252 ? -6.528  18.145  1.779   1.00 26.62 ? 231 GLU   B N   1 
ATOM   3496 C CA  . GLU   B 1 252 ? -7.453  17.022  1.733   1.00 27.32 ? 231 GLU   B CA  1 
ATOM   3497 C C   . GLU   B 1 252 ? -6.929  16.006  0.718   1.00 26.87 ? 231 GLU   B C   1 
ATOM   3498 O O   . GLU   B 1 252 ? -6.126  16.353  -0.172  1.00 27.76 ? 231 GLU   B O   1 
ATOM   3499 C CB  . GLU   B 1 252 ? -8.886  17.521  1.466   1.00 28.59 ? 231 GLU   B CB  1 
ATOM   3500 C CG  . GLU   B 1 252 ? -9.128  18.006  0.034   1.00 31.25 ? 231 GLU   B CG  1 
ATOM   3501 C CD  . GLU   B 1 252 ? -8.774  19.460  -0.271  1.00 36.12 ? 231 GLU   B CD  1 
ATOM   3502 O OE1 . GLU   B 1 252 ? -9.540  20.046  -1.065  1.00 35.92 ? 231 GLU   B OE1 1 
ATOM   3503 O OE2 . GLU   B 1 252 ? -7.809  20.043  0.279   1.00 32.68 ? 231 GLU   B OE2 1 
ATOM   3504 N N   . ALA   B 1 253 ? -7.312  14.727  0.901   1.00 23.69 ? 232 ALA   B N   1 
ATOM   3505 C CA  . ALA   B 1 253 ? -7.033  13.712  -0.103  1.00 25.49 ? 232 ALA   B CA  1 
ATOM   3506 C C   . ALA   B 1 253 ? -7.819  14.030  -1.378  1.00 27.01 ? 232 ALA   B C   1 
ATOM   3507 O O   . ALA   B 1 253 ? -8.960  14.476  -1.322  1.00 31.00 ? 232 ALA   B O   1 
ATOM   3508 C CB  . ALA   B 1 253 ? -7.415  12.329  0.375   1.00 26.42 ? 232 ALA   B CB  1 
ATOM   3509 N N   . SER   B 1 254 ? -7.179  13.782  -2.517  1.00 25.48 ? 233 SER   B N   1 
ATOM   3510 C CA  . SER   B 1 254 ? -7.894  13.693  -3.769  1.00 24.93 ? 233 SER   B CA  1 
ATOM   3511 C C   . SER   B 1 254 ? -8.734  12.415  -3.746  1.00 27.88 ? 233 SER   B C   1 
ATOM   3512 O O   . SER   B 1 254 ? -8.449  11.460  -3.017  1.00 27.12 ? 233 SER   B O   1 
ATOM   3513 C CB  . SER   B 1 254 ? -6.919  13.748  -4.938  1.00 21.30 ? 233 SER   B CB  1 
ATOM   3514 O OG  . SER   B 1 254 ? -6.214  12.521  -5.103  1.00 24.83 ? 233 SER   B OG  1 
ATOM   3515 N N   . ALA   B 1 255 ? -9.762  12.391  -4.592  1.00 25.86 ? 234 ALA   B N   1 
ATOM   3516 C CA  . ALA   B 1 255 ? -10.568 11.208  -4.772  1.00 24.51 ? 234 ALA   B CA  1 
ATOM   3517 C C   . ALA   B 1 255 ? -9.659  10.103  -5.293  1.00 23.29 ? 234 ALA   B C   1 
ATOM   3518 O O   . ALA   B 1 255 ? -9.848  8.930   -4.957  1.00 22.05 ? 234 ALA   B O   1 
ATOM   3519 C CB  . ALA   B 1 255 ? -11.749 11.503  -5.716  1.00 24.49 ? 234 ALA   B CB  1 
ATOM   3520 N N   . GLU   B 1 256 ? -8.685  10.471  -6.127  1.00 22.68 ? 235 GLU   B N   1 
ATOM   3521 C CA  . GLU   B 1 256 ? -7.852  9.456   -6.757  1.00 24.58 ? 235 GLU   B CA  1 
ATOM   3522 C C   . GLU   B 1 256 ? -6.946  8.771   -5.718  1.00 23.09 ? 235 GLU   B C   1 
ATOM   3523 O O   . GLU   B 1 256 ? -6.655  7.576   -5.830  1.00 22.69 ? 235 GLU   B O   1 
ATOM   3524 C CB  . GLU   B 1 256 ? -7.010  10.066  -7.886  1.00 29.38 ? 235 GLU   B CB  1 
ATOM   3525 C CG  . GLU   B 1 256 ? -7.819  10.557  -9.086  1.00 33.61 ? 235 GLU   B CG  1 
ATOM   3526 C CD  . GLU   B 1 256 ? -8.687  11.804  -8.970  1.00 34.40 ? 235 GLU   B CD  1 
ATOM   3527 O OE1 . GLU   B 1 256 ? -8.713  12.543  -7.944  1.00 31.18 ? 235 GLU   B OE1 1 
ATOM   3528 O OE2 . GLU   B 1 256 ? -9.398  12.022  -9.975  1.00 33.58 ? 235 GLU   B OE2 1 
ATOM   3529 N N   . GLN   B 1 257 ? -6.476  9.544   -4.735  1.00 21.08 ? 236 GLN   B N   1 
ATOM   3530 C CA  . GLN   B 1 257 ? -5.680  9.015   -3.618  1.00 22.95 ? 236 GLN   B CA  1 
ATOM   3531 C C   . GLN   B 1 257 ? -6.457  7.940   -2.852  1.00 22.06 ? 236 GLN   B C   1 
ATOM   3532 O O   . GLN   B 1 257 ? -5.898  6.890   -2.545  1.00 20.16 ? 236 GLN   B O   1 
ATOM   3533 C CB  . GLN   B 1 257 ? -5.162  10.153  -2.728  1.00 24.05 ? 236 GLN   B CB  1 
ATOM   3534 C CG  . GLN   B 1 257 ? -3.989  10.866  -3.400  1.00 23.80 ? 236 GLN   B CG  1 
ATOM   3535 C CD  . GLN   B 1 257 ? -3.541  12.123  -2.697  1.00 24.98 ? 236 GLN   B CD  1 
ATOM   3536 O OE1 . GLN   B 1 257 ? -4.320  12.824  -2.047  1.00 25.64 ? 236 GLN   B OE1 1 
ATOM   3537 N NE2 . GLN   B 1 257 ? -2.267  12.450  -2.904  1.00 26.37 ? 236 GLN   B NE2 1 
ATOM   3538 N N   . ILE   B 1 258 ? -7.747  8.187   -2.597  1.00 22.17 ? 237 ILE   B N   1 
ATOM   3539 C CA  . ILE   B 1 258 ? -8.593  7.192   -1.941  1.00 21.01 ? 237 ILE   B CA  1 
ATOM   3540 C C   . ILE   B 1 258 ? -8.727  5.982   -2.852  1.00 22.21 ? 237 ILE   B C   1 
ATOM   3541 O O   . ILE   B 1 258 ? -8.606  4.853   -2.388  1.00 21.33 ? 237 ILE   B O   1 
ATOM   3542 C CB  . ILE   B 1 258 ? -9.977  7.764   -1.567  1.00 23.33 ? 237 ILE   B CB  1 
ATOM   3543 C CG1 . ILE   B 1 258 ? -9.854  9.028   -0.672  1.00 23.89 ? 237 ILE   B CG1 1 
ATOM   3544 C CG2 . ILE   B 1 258 ? -10.837 6.679   -0.914  1.00 22.20 ? 237 ILE   B CG2 1 
ATOM   3545 C CD1 . ILE   B 1 258 ? -8.978  8.790   0.561   1.00 28.07 ? 237 ILE   B CD1 1 
ATOM   3546 N N   . ALA   B 1 259 ? -9.026  6.212   -4.149  1.00 21.75 ? 238 ALA   B N   1 
ATOM   3547 C CA  . ALA   B 1 259 ? -9.168  5.102   -5.094  1.00 23.28 ? 238 ALA   B CA  1 
ATOM   3548 C C   . ALA   B 1 259 ? -7.898  4.243   -5.169  1.00 21.97 ? 238 ALA   B C   1 
ATOM   3549 O O   . ALA   B 1 259 ? -7.979  3.024   -5.355  1.00 21.34 ? 238 ALA   B O   1 
ATOM   3550 C CB  . ALA   B 1 259 ? -9.569  5.618   -6.506  1.00 20.99 ? 238 ALA   B CB  1 
ATOM   3551 N N   . ASP   B 1 260 ? -6.710  4.861   -5.040  1.00 21.88 ? 239 ASP   B N   1 
ATOM   3552 C CA  . ASP   B 1 260 ? -5.458  4.100   -5.117  1.00 22.38 ? 239 ASP   B CA  1 
ATOM   3553 C C   . ASP   B 1 260 ? -5.395  2.987   -4.063  1.00 21.22 ? 239 ASP   B C   1 
ATOM   3554 O O   . ASP   B 1 260 ? -4.864  1.905   -4.305  1.00 21.64 ? 239 ASP   B O   1 
ATOM   3555 C CB  . ASP   B 1 260 ? -4.218  4.972   -4.946  1.00 23.18 ? 239 ASP   B CB  1 
ATOM   3556 C CG  . ASP   B 1 260 ? -3.894  5.825   -6.167  1.00 31.04 ? 239 ASP   B CG  1 
ATOM   3557 O OD1 . ASP   B 1 260 ? -4.200  5.365   -7.296  1.00 29.40 ? 239 ASP   B OD1 1 
ATOM   3558 O OD2 . ASP   B 1 260 ? -3.334  6.919   -5.983  1.00 29.62 ? 239 ASP   B OD2 1 
ATOM   3559 N N   . ALA   B 1 261 ? -5.929  3.263   -2.879  1.00 22.63 ? 240 ALA   B N   1 
ATOM   3560 C CA  . ALA   B 1 261 ? -5.901  2.263   -1.813  1.00 23.91 ? 240 ALA   B CA  1 
ATOM   3561 C C   . ALA   B 1 261 ? -6.872  1.135   -2.146  1.00 23.23 ? 240 ALA   B C   1 
ATOM   3562 O O   . ALA   B 1 261 ? -6.594  -0.014  -1.824  1.00 22.05 ? 240 ALA   B O   1 
ATOM   3563 C CB  . ALA   B 1 261 ? -6.251  2.925   -0.486  1.00 22.02 ? 240 ALA   B CB  1 
ATOM   3564 N N   . VAL   B 1 262 ? -8.033  1.484   -2.749  1.00 22.51 ? 241 VAL   B N   1 
ATOM   3565 C CA  . VAL   B 1 262 ? -9.006  0.454   -3.100  1.00 22.57 ? 241 VAL   B CA  1 
ATOM   3566 C C   . VAL   B 1 262 ? -8.364  -0.470  -4.131  1.00 21.82 ? 241 VAL   B C   1 
ATOM   3567 O O   . VAL   B 1 262 ? -8.457  -1.701  -4.046  1.00 22.19 ? 241 VAL   B O   1 
ATOM   3568 C CB  . VAL   B 1 262 ? -10.288 1.119   -3.660  1.00 22.87 ? 241 VAL   B CB  1 
ATOM   3569 C CG1 . VAL   B 1 262 ? -11.289 0.085   -4.212  1.00 22.67 ? 241 VAL   B CG1 1 
ATOM   3570 C CG2 . VAL   B 1 262 ? -10.919 2.072   -2.652  1.00 21.78 ? 241 VAL   B CG2 1 
ATOM   3571 N N   . ILE   B 1 263 ? -7.730  0.160   -5.130  1.00 21.24 ? 242 ILE   B N   1 
ATOM   3572 C CA  . ILE   B 1 263 ? -7.045  -0.552  -6.203  1.00 23.22 ? 242 ILE   B CA  1 
ATOM   3573 C C   . ILE   B 1 263 ? -6.007  -1.516  -5.631  1.00 22.87 ? 242 ILE   B C   1 
ATOM   3574 O O   . ILE   B 1 263 ? -5.910  -2.651  -6.077  1.00 23.14 ? 242 ILE   B O   1 
ATOM   3575 C CB  . ILE   B 1 263 ? -6.439  0.453   -7.195  1.00 24.22 ? 242 ILE   B CB  1 
ATOM   3576 C CG1 . ILE   B 1 263 ? -7.537  1.084   -8.057  1.00 28.13 ? 242 ILE   B CG1 1 
ATOM   3577 C CG2 . ILE   B 1 263 ? -5.340  -0.168  -8.054  1.00 25.57 ? 242 ILE   B CG2 1 
ATOM   3578 C CD1 . ILE   B 1 263 ? -8.301  0.095   -8.916  1.00 26.64 ? 242 ILE   B CD1 1 
ATOM   3579 N N   . PHE   B 1 264 ? -5.232  -1.065  -4.635  1.00 21.46 ? 243 PHE   B N   1 
ATOM   3580 C CA  . PHE   B 1 264 ? -4.282  -1.957  -3.988  1.00 18.83 ? 243 PHE   B CA  1 
ATOM   3581 C C   . PHE   B 1 264 ? -5.014  -3.147  -3.362  1.00 20.78 ? 243 PHE   B C   1 
ATOM   3582 O O   . PHE   B 1 264 ? -4.609  -4.289  -3.535  1.00 20.07 ? 243 PHE   B O   1 
ATOM   3583 C CB  . PHE   B 1 264 ? -3.415  -1.185  -2.975  1.00 18.86 ? 243 PHE   B CB  1 
ATOM   3584 C CG  . PHE   B 1 264 ? -2.651  -2.111  -2.024  1.00 20.21 ? 243 PHE   B CG  1 
ATOM   3585 C CD1 . PHE   B 1 264 ? -1.565  -2.860  -2.468  1.00 20.81 ? 243 PHE   B CD1 1 
ATOM   3586 C CD2 . PHE   B 1 264 ? -2.996  -2.182  -0.669  1.00 20.37 ? 243 PHE   B CD2 1 
ATOM   3587 C CE1 . PHE   B 1 264 ? -0.855  -3.675  -1.590  1.00 25.41 ? 243 PHE   B CE1 1 
ATOM   3588 C CE2 . PHE   B 1 264 ? -2.293  -2.987  0.209   1.00 22.42 ? 243 PHE   B CE2 1 
ATOM   3589 C CZ  . PHE   B 1 264 ? -1.229  -3.742  -0.251  1.00 25.13 ? 243 PHE   B CZ  1 
ATOM   3590 N N   . LEU   B 1 265 ? -6.040  -2.874  -2.555  1.00 20.82 ? 244 LEU   B N   1 
ATOM   3591 C CA  . LEU   B 1 265 ? -6.719  -3.946  -1.826  1.00 22.62 ? 244 LEU   B CA  1 
ATOM   3592 C C   . LEU   B 1 265 ? -7.341  -4.973  -2.764  1.00 23.45 ? 244 LEU   B C   1 
ATOM   3593 O O   . LEU   B 1 265 ? -7.460  -6.156  -2.391  1.00 23.57 ? 244 LEU   B O   1 
ATOM   3594 C CB  . LEU   B 1 265 ? -7.746  -3.345  -0.854  1.00 22.86 ? 244 LEU   B CB  1 
ATOM   3595 C CG  . LEU   B 1 265 ? -7.138  -2.706  0.414   1.00 20.49 ? 244 LEU   B CG  1 
ATOM   3596 C CD1 . LEU   B 1 265 ? -8.201  -1.897  1.174   1.00 19.65 ? 244 LEU   B CD1 1 
ATOM   3597 C CD2 . LEU   B 1 265 ? -6.595  -3.826  1.276   1.00 22.00 ? 244 LEU   B CD2 1 
ATOM   3598 N N   . VAL   B 1 266 ? -7.750  -4.540  -3.977  1.00 20.95 ? 245 VAL   B N   1 
ATOM   3599 C CA  . VAL   B 1 266 ? -8.416  -5.510  -4.848  1.00 21.87 ? 245 VAL   B CA  1 
ATOM   3600 C C   . VAL   B 1 266 ? -7.384  -6.318  -5.637  1.00 23.94 ? 245 VAL   B C   1 
ATOM   3601 O O   . VAL   B 1 266 ? -7.726  -7.364  -6.190  1.00 24.88 ? 245 VAL   B O   1 
ATOM   3602 C CB  . VAL   B 1 266 ? -9.503  -4.908  -5.773  1.00 25.20 ? 245 VAL   B CB  1 
ATOM   3603 C CG1 . VAL   B 1 266 ? -10.635 -4.271  -4.970  1.00 21.62 ? 245 VAL   B CG1 1 
ATOM   3604 C CG2 . VAL   B 1 266 ? -8.936  -3.860  -6.722  1.00 23.95 ? 245 VAL   B CG2 1 
ATOM   3605 N N   . SER   B 1 267 ? -6.140  -5.815  -5.699  1.00 23.97 ? 246 SER   B N   1 
ATOM   3606 C CA  . SER   B 1 267 ? -5.083  -6.343  -6.565  1.00 23.97 ? 246 SER   B CA  1 
ATOM   3607 C C   . SER   B 1 267 ? -4.468  -7.634  -6.020  1.00 24.83 ? 246 SER   B C   1 
ATOM   3608 O O   . SER   B 1 267 ? -4.542  -7.941  -4.822  1.00 25.58 ? 246 SER   B O   1 
ATOM   3609 C CB  . SER   B 1 267 ? -3.983  -5.333  -6.746  1.00 23.27 ? 246 SER   B CB  1 
ATOM   3610 O OG  . SER   B 1 267 ? -3.167  -5.314  -5.580  1.00 26.54 ? 246 SER   B OG  1 
ATOM   3611 N N   . GLY   B 1 268 ? -3.717  -8.316  -6.894  1.00 27.65 ? 247 GLY   B N   1 
ATOM   3612 C CA  . GLY   B 1 268 ? -2.881  -9.447  -6.493  1.00 29.43 ? 247 GLY   B CA  1 
ATOM   3613 C C   . GLY   B 1 268 ? -1.775  -9.096  -5.483  1.00 28.68 ? 247 GLY   B C   1 
ATOM   3614 O O   . GLY   B 1 268 ? -1.174  -9.992  -4.898  1.00 31.08 ? 247 GLY   B O   1 
ATOM   3615 N N   . SER   B 1 269 ? -1.508  -7.809  -5.227  1.00 26.38 ? 248 SER   B N   1 
ATOM   3616 C CA  . SER   B 1 269 ? -0.509  -7.449  -4.217  1.00 27.61 ? 248 SER   B CA  1 
ATOM   3617 C C   . SER   B 1 269 ? -1.061  -7.548  -2.788  1.00 27.51 ? 248 SER   B C   1 
ATOM   3618 O O   . SER   B 1 269 ? -0.337  -7.273  -1.824  1.00 28.17 ? 248 SER   B O   1 
ATOM   3619 C CB  . SER   B 1 269 ? 0.017   -6.045  -4.465  1.00 27.72 ? 248 SER   B CB  1 
ATOM   3620 O OG  . SER   B 1 269 ? 0.710   -6.019  -5.703  1.00 32.90 ? 248 SER   B OG  1 
ATOM   3621 N N   . ALA   B 1 270 ? -2.364  -7.836  -2.661  1.00 24.14 ? 249 ALA   B N   1 
ATOM   3622 C CA  . ALA   B 1 270 ? -3.028  -7.834  -1.372  1.00 22.79 ? 249 ALA   B CA  1 
ATOM   3623 C C   . ALA   B 1 270 ? -3.718  -9.170  -1.132  1.00 23.45 ? 249 ALA   B C   1 
ATOM   3624 O O   . ALA   B 1 270 ? -4.634  -9.239  -0.327  1.00 22.25 ? 249 ALA   B O   1 
ATOM   3625 C CB  . ALA   B 1 270 ? -4.004  -6.653  -1.283  1.00 23.14 ? 249 ALA   B CB  1 
ATOM   3626 N N   . GLN   B 1 271 ? -3.209  -10.254 -1.738  1.00 22.43 ? 250 GLN   B N   1 
ATOM   3627 C CA  A GLN   B 1 271 ? -3.880  -11.548 -1.741  0.60 25.18 ? 250 GLN   B CA  1 
ATOM   3628 C CA  B GLN   B 1 271 ? -3.959  -11.504 -1.720  0.40 23.82 ? 250 GLN   B CA  1 
ATOM   3629 C C   . GLN   B 1 271 ? -3.941  -12.203 -0.358  1.00 23.47 ? 250 GLN   B C   1 
ATOM   3630 O O   . GLN   B 1 271 ? -4.675  -13.170 -0.193  1.00 21.33 ? 250 GLN   B O   1 
ATOM   3631 C CB  A GLN   B 1 271 ? -3.206  -12.502 -2.737  0.60 28.16 ? 250 GLN   B CB  1 
ATOM   3632 C CB  B GLN   B 1 271 ? -3.659  -12.443 -2.896  0.40 26.08 ? 250 GLN   B CB  1 
ATOM   3633 C CG  A GLN   B 1 271 ? -1.706  -12.653 -2.524  0.60 35.85 ? 250 GLN   B CG  1 
ATOM   3634 C CG  B GLN   B 1 271 ? -4.341  -11.992 -4.183  0.40 27.09 ? 250 GLN   B CG  1 
ATOM   3635 C CD  A GLN   B 1 271 ? -0.960  -13.291 -3.682  0.60 40.91 ? 250 GLN   B CD  1 
ATOM   3636 C CD  B GLN   B 1 271 ? -4.452  -13.060 -5.248  0.40 28.75 ? 250 GLN   B CD  1 
ATOM   3637 O OE1 A GLN   B 1 271 ? 0.254   -13.494 -3.606  0.60 38.71 ? 250 GLN   B OE1 1 
ATOM   3638 O OE1 B GLN   B 1 271 ? -3.678  -13.071 -6.206  0.40 31.34 ? 250 GLN   B OE1 1 
ATOM   3639 N NE2 A GLN   B 1 271 ? -1.657  -13.587 -4.775  0.60 43.70 ? 250 GLN   B NE2 1 
ATOM   3640 N NE2 B GLN   B 1 271 ? -5.428  -13.949 -5.108  0.40 26.86 ? 250 GLN   B NE2 1 
ATOM   3641 N N   . TYR   B 1 272 ? -3.125  -11.739 0.609   1.00 22.94 ? 251 TYR   B N   1 
ATOM   3642 C CA  . TYR   B 1 272 ? -3.160  -12.314 1.964   1.00 21.06 ? 251 TYR   B CA  1 
ATOM   3643 C C   . TYR   B 1 272 ? -3.849  -11.363 2.941   1.00 22.56 ? 251 TYR   B C   1 
ATOM   3644 O O   . TYR   B 1 272 ? -3.898  -11.636 4.145   1.00 20.53 ? 251 TYR   B O   1 
ATOM   3645 C CB  . TYR   B 1 272 ? -1.736  -12.547 2.496   1.00 19.94 ? 251 TYR   B CB  1 
ATOM   3646 C CG  . TYR   B 1 272 ? -1.623  -13.520 3.666   1.00 21.65 ? 251 TYR   B CG  1 
ATOM   3647 C CD1 . TYR   B 1 272 ? -1.829  -14.886 3.469   1.00 20.88 ? 251 TYR   B CD1 1 
ATOM   3648 C CD2 . TYR   B 1 272 ? -1.259  -13.091 4.945   1.00 20.02 ? 251 TYR   B CD2 1 
ATOM   3649 C CE1 . TYR   B 1 272 ? -1.721  -15.783 4.517   1.00 22.13 ? 251 TYR   B CE1 1 
ATOM   3650 C CE2 . TYR   B 1 272 ? -1.134  -13.981 6.000   1.00 18.82 ? 251 TYR   B CE2 1 
ATOM   3651 C CZ  . TYR   B 1 272 ? -1.386  -15.328 5.783   1.00 21.02 ? 251 TYR   B CZ  1 
ATOM   3652 O OH  . TYR   B 1 272 ? -1.232  -16.222 6.787   1.00 22.09 ? 251 TYR   B OH  1 
ATOM   3653 N N   . ILE   B 1 273 ? -4.299  -10.193 2.440   1.00 20.57 ? 252 ILE   B N   1 
ATOM   3654 C CA  . ILE   B 1 273 ? -4.881  -9.172  3.303   1.00 20.80 ? 252 ILE   B CA  1 
ATOM   3655 C C   . ILE   B 1 273 ? -6.398  -9.334  3.365   1.00 21.81 ? 252 ILE   B C   1 
ATOM   3656 O O   . ILE   B 1 273 ? -7.087  -9.264  2.350   1.00 20.39 ? 252 ILE   B O   1 
ATOM   3657 C CB  . ILE   B 1 273 ? -4.486  -7.755  2.823   1.00 20.39 ? 252 ILE   B CB  1 
ATOM   3658 C CG1 . ILE   B 1 273 ? -2.945  -7.586  2.671   1.00 20.92 ? 252 ILE   B CG1 1 
ATOM   3659 C CG2 . ILE   B 1 273 ? -5.108  -6.679  3.722   1.00 20.91 ? 252 ILE   B CG2 1 
ATOM   3660 C CD1 . ILE   B 1 273 ? -2.548  -6.193  2.171   1.00 20.53 ? 252 ILE   B CD1 1 
ATOM   3661 N N   . THR   B 1 274 ? -6.922  -9.552  4.574   1.00 19.95 ? 253 THR   B N   1 
ATOM   3662 C CA  . THR   B 1 274 ? -8.369  -9.604  4.787   1.00 22.70 ? 253 THR   B CA  1 
ATOM   3663 C C   . THR   B 1 274 ? -8.639  -9.111  6.213   1.00 23.63 ? 253 THR   B C   1 
ATOM   3664 O O   . THR   B 1 274 ? -7.813  -9.351  7.085   1.00 23.92 ? 253 THR   B O   1 
ATOM   3665 C CB  . THR   B 1 274 ? -8.993  -10.965 4.441   1.00 20.82 ? 253 THR   B CB  1 
ATOM   3666 O OG1 . THR   B 1 274 ? -10.409 -10.782 4.306   1.00 22.33 ? 253 THR   B OG1 1 
ATOM   3667 C CG2 . THR   B 1 274 ? -8.662  -12.079 5.431   1.00 18.52 ? 253 THR   B CG2 1 
ATOM   3668 N N   . GLY   B 1 275 ? -9.738  -8.350  6.407   1.00 21.29 ? 254 GLY   B N   1 
ATOM   3669 C CA  . GLY   B 1 275 ? -10.071 -7.824  7.711   1.00 20.56 ? 254 GLY   B CA  1 
ATOM   3670 C C   . GLY   B 1 275 ? -9.292  -6.554  8.044   1.00 21.15 ? 254 GLY   B C   1 
ATOM   3671 O O   . GLY   B 1 275 ? -9.347  -6.107  9.173   1.00 24.48 ? 254 GLY   B O   1 
ATOM   3672 N N   . SER   B 1 276 ? -8.567  -5.973  7.082   1.00 22.31 ? 255 SER   B N   1 
ATOM   3673 C CA  . SER   B 1 276 ? -7.719  -4.831  7.383   1.00 20.42 ? 255 SER   B CA  1 
ATOM   3674 C C   . SER   B 1 276 ? -8.438  -3.585  6.907   1.00 19.94 ? 255 SER   B C   1 
ATOM   3675 O O   . SER   B 1 276 ? -9.074  -3.636  5.860   1.00 19.65 ? 255 SER   B O   1 
ATOM   3676 C CB  . SER   B 1 276 ? -6.360  -4.915  6.645   1.00 23.67 ? 255 SER   B CB  1 
ATOM   3677 O OG  . SER   B 1 276 ? -5.654  -6.107  7.011   1.00 28.20 ? 255 SER   B OG  1 
ATOM   3678 N N   . ILE   B 1 277 ? -8.208  -2.463  7.595   1.00 20.54 ? 256 ILE   B N   1 
ATOM   3679 C CA  . ILE   B 1 277 ? -8.751  -1.185  7.174   1.00 19.91 ? 256 ILE   B CA  1 
ATOM   3680 C C   . ILE   B 1 277 ? -7.571  -0.216  7.076   1.00 23.35 ? 256 ILE   B C   1 
ATOM   3681 O O   . ILE   B 1 277 ? -6.871  0.026   8.058   1.00 25.63 ? 256 ILE   B O   1 
ATOM   3682 C CB  . ILE   B 1 277 ? -9.820  -0.735  8.181   1.00 24.81 ? 256 ILE   B CB  1 
ATOM   3683 C CG1 . ILE   B 1 277 ? -11.024 -1.722  8.182   1.00 24.95 ? 256 ILE   B CG1 1 
ATOM   3684 C CG2 . ILE   B 1 277 ? -10.281 0.705   7.900   1.00 23.82 ? 256 ILE   B CG2 1 
ATOM   3685 C CD1 . ILE   B 1 277 ? -12.033 -1.408  9.273   1.00 28.99 ? 256 ILE   B CD1 1 
ATOM   3686 N N   . ILE   B 1 278 ? -7.310  0.275   5.870   1.00 20.47 ? 257 ILE   B N   1 
ATOM   3687 C CA  . ILE   B 1 278 ? -6.183  1.154   5.620   1.00 20.73 ? 257 ILE   B CA  1 
ATOM   3688 C C   . ILE   B 1 278 ? -6.672  2.590   5.744   1.00 20.94 ? 257 ILE   B C   1 
ATOM   3689 O O   . ILE   B 1 278 ? -7.515  3.015   4.947   1.00 18.78 ? 257 ILE   B O   1 
ATOM   3690 C CB  . ILE   B 1 278 ? -5.657  0.894   4.201   1.00 21.41 ? 257 ILE   B CB  1 
ATOM   3691 C CG1 . ILE   B 1 278 ? -5.231  -0.554  4.041   1.00 21.14 ? 257 ILE   B CG1 1 
ATOM   3692 C CG2 . ILE   B 1 278 ? -4.503  1.851   3.852   1.00 22.90 ? 257 ILE   B CG2 1 
ATOM   3693 C CD1 . ILE   B 1 278 ? -4.731  -0.876  2.643   1.00 23.52 ? 257 ILE   B CD1 1 
ATOM   3694 N N   . LYS   B 1 279 ? -6.123  3.329   6.717   1.00 20.24 ? 258 LYS   B N   1 
ATOM   3695 C CA  . LYS   B 1 279 ? -6.421  4.750   6.818   1.00 22.18 ? 258 LYS   B CA  1 
ATOM   3696 C C   . LYS   B 1 279 ? -5.715  5.482   5.687   1.00 20.67 ? 258 LYS   B C   1 
ATOM   3697 O O   . LYS   B 1 279 ? -4.563  5.182   5.394   1.00 21.18 ? 258 LYS   B O   1 
ATOM   3698 C CB  . LYS   B 1 279 ? -5.866  5.441   8.071   1.00 21.43 ? 258 LYS   B CB  1 
ATOM   3699 C CG  . LYS   B 1 279 ? -6.601  5.210   9.318   1.00 24.29 ? 258 LYS   B CG  1 
ATOM   3700 C CD  . LYS   B 1 279 ? -5.967  5.960   10.489  1.00 27.92 ? 258 LYS   B CD  1 
ATOM   3701 C CE  . LYS   B 1 279 ? -4.568  5.467   10.806  1.00 27.18 ? 258 LYS   B CE  1 
ATOM   3702 N NZ  . LYS   B 1 279 ? -4.026  6.153   11.988  1.00 26.30 ? 258 LYS   B NZ  1 
ATOM   3703 N N   . VAL   B 1 280 ? -6.415  6.450   5.078   1.00 24.25 ? 259 VAL   B N   1 
ATOM   3704 C CA  . VAL   B 1 280 ? -5.830  7.290   4.036   1.00 22.77 ? 259 VAL   B CA  1 
ATOM   3705 C C   . VAL   B 1 280 ? -6.182  8.715   4.420   1.00 23.18 ? 259 VAL   B C   1 
ATOM   3706 O O   . VAL   B 1 280 ? -7.104  9.297   3.852   1.00 24.70 ? 259 VAL   B O   1 
ATOM   3707 C CB  . VAL   B 1 280 ? -6.324  6.961   2.605   1.00 22.59 ? 259 VAL   B CB  1 
ATOM   3708 C CG1 . VAL   B 1 280 ? -5.525  7.720   1.555   1.00 22.57 ? 259 VAL   B CG1 1 
ATOM   3709 C CG2 . VAL   B 1 280 ? -6.169  5.476   2.293   1.00 21.89 ? 259 VAL   B CG2 1 
ATOM   3710 N N   . ASP   B 1 281 ? -5.466  9.240   5.424   1.00 21.30 ? 260 ASP   B N   1 
ATOM   3711 C CA  . ASP   B 1 281 ? -5.950  10.430  6.092   1.00 21.17 ? 260 ASP   B CA  1 
ATOM   3712 C C   . ASP   B 1 281 ? -4.847  11.467  6.299   1.00 20.24 ? 260 ASP   B C   1 
ATOM   3713 O O   . ASP   B 1 281 ? -5.120  12.468  6.944   1.00 21.81 ? 260 ASP   B O   1 
ATOM   3714 C CB  . ASP   B 1 281 ? -6.605  10.073  7.427   1.00 21.06 ? 260 ASP   B CB  1 
ATOM   3715 C CG  . ASP   B 1 281 ? -5.649  9.677   8.550   1.00 21.99 ? 260 ASP   B CG  1 
ATOM   3716 O OD1 . ASP   B 1 281 ? -4.438  9.448   8.282   1.00 21.39 ? 260 ASP   B OD1 1 
ATOM   3717 O OD2 . ASP   B 1 281 ? -6.124  9.627   9.681   1.00 21.51 ? 260 ASP   B OD2 1 
ATOM   3718 N N   . GLY   B 1 282 ? -3.640  11.267  5.739   1.00 20.74 ? 261 GLY   B N   1 
ATOM   3719 C CA  . GLY   B 1 282 ? -2.592  12.272  5.852   1.00 22.78 ? 261 GLY   B CA  1 
ATOM   3720 C C   . GLY   B 1 282 ? -2.203  12.573  7.310   1.00 24.88 ? 261 GLY   B C   1 
ATOM   3721 O O   . GLY   B 1 282 ? -1.680  13.647  7.611   1.00 22.22 ? 261 GLY   B O   1 
ATOM   3722 N N   . GLY   B 1 283 ? -2.489  11.633  8.231   1.00 22.80 ? 262 GLY   B N   1 
ATOM   3723 C CA  . GLY   B 1 283 ? -2.144  11.855  9.635   1.00 18.58 ? 262 GLY   B CA  1 
ATOM   3724 C C   . GLY   B 1 283 ? -3.272  12.522  10.444  1.00 21.17 ? 262 GLY   B C   1 
ATOM   3725 O O   . GLY   B 1 283 ? -3.093  12.795  11.629  1.00 19.34 ? 262 GLY   B O   1 
ATOM   3726 N N   . LEU   B 1 284 ? -4.417  12.826  9.819   1.00 20.37 ? 263 LEU   B N   1 
ATOM   3727 C CA  . LEU   B 1 284 ? -5.459  13.596  10.495  1.00 20.97 ? 263 LEU   B CA  1 
ATOM   3728 C C   . LEU   B 1 284 ? -5.892  12.964  11.823  1.00 21.83 ? 263 LEU   B C   1 
ATOM   3729 O O   . LEU   B 1 284 ? -6.042  13.667  12.827  1.00 21.24 ? 263 LEU   B O   1 
ATOM   3730 C CB  . LEU   B 1 284 ? -6.677  13.811  9.592   1.00 20.90 ? 263 LEU   B CB  1 
ATOM   3731 C CG  . LEU   B 1 284 ? -7.762  14.693  10.224  1.00 25.37 ? 263 LEU   B CG  1 
ATOM   3732 C CD1 . LEU   B 1 284 ? -7.202  16.119  10.447  1.00 23.64 ? 263 LEU   B CD1 1 
ATOM   3733 C CD2 . LEU   B 1 284 ? -9.017  14.714  9.344   1.00 27.61 ? 263 LEU   B CD2 1 
ATOM   3734 N N   . SER   B 1 285 ? -6.092  11.631  11.851  1.00 20.55 ? 264 SER   B N   1 
ATOM   3735 C CA  . SER   B 1 285 ? -6.608  11.015  13.069  1.00 21.53 ? 264 SER   B CA  1 
ATOM   3736 C C   . SER   B 1 285 ? -5.577  10.994  14.209  1.00 22.65 ? 264 SER   B C   1 
ATOM   3737 O O   . SER   B 1 285 ? -5.924  10.557  15.311  1.00 20.80 ? 264 SER   B O   1 
ATOM   3738 C CB  . SER   B 1 285 ? -7.059  9.592   12.778  1.00 21.38 ? 264 SER   B CB  1 
ATOM   3739 O OG  . SER   B 1 285 ? -5.933  8.860   12.289  1.00 22.80 ? 264 SER   B OG  1 
ATOM   3740 N N   . LEU   B 1 286 ? -4.315  11.407  13.942  1.00 21.25 ? 265 LEU   B N   1 
ATOM   3741 C CA  . LEU   B 1 286 ? -3.241  11.474  14.940  1.00 22.04 ? 265 LEU   B CA  1 
ATOM   3742 C C   . LEU   B 1 286 ? -3.248  12.784  15.740  1.00 24.12 ? 265 LEU   B C   1 
ATOM   3743 O O   . LEU   B 1 286 ? -2.486  12.926  16.708  1.00 24.00 ? 265 LEU   B O   1 
ATOM   3744 C CB  . LEU   B 1 286 ? -1.852  11.221  14.334  1.00 21.38 ? 265 LEU   B CB  1 
ATOM   3745 C CG  . LEU   B 1 286 ? -1.677  9.978   13.450  1.00 23.39 ? 265 LEU   B CG  1 
ATOM   3746 C CD1 . LEU   B 1 286 ? -0.339  10.067  12.708  1.00 23.17 ? 265 LEU   B CD1 1 
ATOM   3747 C CD2 . LEU   B 1 286 ? -1.837  8.630   14.120  1.00 26.81 ? 265 LEU   B CD2 1 
ATOM   3748 N N   . VAL   B 1 287 ? -4.050  13.754  15.300  1.00 24.32 ? 266 VAL   B N   1 
ATOM   3749 C CA  . VAL   B 1 287 ? -3.956  15.124  15.772  1.00 22.64 ? 266 VAL   B CA  1 
ATOM   3750 C C   . VAL   B 1 287 ? -4.922  15.273  16.941  1.00 26.90 ? 266 VAL   B C   1 
ATOM   3751 O O   . VAL   B 1 287 ? -6.112  15.026  16.764  1.00 26.97 ? 266 VAL   B O   1 
ATOM   3752 C CB  . VAL   B 1 287 ? -4.218  16.185  14.680  1.00 25.66 ? 266 VAL   B CB  1 
ATOM   3753 C CG1 . VAL   B 1 287 ? -4.087  17.625  15.213  1.00 25.67 ? 266 VAL   B CG1 1 
ATOM   3754 C CG2 . VAL   B 1 287 ? -3.285  15.994  13.482  1.00 22.67 ? 266 VAL   B CG2 1 
ATOM   3755 N N   . HIS   B 1 288 ? -4.395  15.699  18.105  1.00 27.64 ? 267 HIS   B N   1 
ATOM   3756 C CA  . HIS   B 1 288 ? -5.218  15.899  19.295  1.00 30.93 ? 267 HIS   B CA  1 
ATOM   3757 C C   . HIS   B 1 288 ? -5.992  17.206  19.157  1.00 29.27 ? 267 HIS   B C   1 
ATOM   3758 O O   . HIS   B 1 288 ? -5.649  18.055  18.339  1.00 31.70 ? 267 HIS   B O   1 
ATOM   3759 C CB  . HIS   B 1 288 ? -4.392  15.842  20.595  1.00 31.45 ? 267 HIS   B CB  1 
ATOM   3760 C CG  . HIS   B 1 288 ? -3.350  16.926  20.709  1.00 34.44 ? 267 HIS   B CG  1 
ATOM   3761 N ND1 . HIS   B 1 288 ? -3.644  18.271  20.885  1.00 34.17 ? 267 HIS   B ND1 1 
ATOM   3762 C CD2 . HIS   B 1 288 ? -2.004  16.846  20.647  1.00 34.40 ? 267 HIS   B CD2 1 
ATOM   3763 C CE1 . HIS   B 1 288 ? -2.515  18.981  20.907  1.00 33.73 ? 267 HIS   B CE1 1 
ATOM   3764 N NE2 . HIS   B 1 288 ? -1.500  18.132  20.772  1.00 37.26 ? 267 HIS   B NE2 1 
ATOM   3765 N N   . ALA   B 1 289 ? -7.000  17.379  20.010  1.00 26.54 ? 268 ALA   B N   1 
ATOM   3766 C CA  . ALA   B 1 289 ? -7.830  18.571  19.984  1.00 31.98 ? 268 ALA   B CA  1 
ATOM   3767 C C   . ALA   B 1 289 ? -6.979  19.803  20.319  1.00 35.08 ? 268 ALA   B C   1 
ATOM   3768 O O   . ALA   B 1 289 ? -7.424  20.889  19.921  1.00 38.91 ? 268 ALA   B O   1 
ATOM   3769 C CB  . ALA   B 1 289 ? -8.954  18.426  20.984  1.00 35.30 ? 268 ALA   B CB  1 
ATOM   3770 O OXT . ALA   B 1 289 ? -5.931  19.652  20.972  1.00 32.78 ? 268 ALA   B OXT 1 
ATOM   3771 N N   . GLU   C 1 23  ? -4.066  -9.758  58.661  0.70 46.54 ? 2   GLU   C N   1 
ATOM   3772 C CA  . GLU   C 1 23  ? -3.732  -8.318  58.832  0.70 50.98 ? 2   GLU   C CA  1 
ATOM   3773 C C   . GLU   C 1 23  ? -3.877  -7.566  57.503  0.70 45.83 ? 2   GLU   C C   1 
ATOM   3774 O O   . GLU   C 1 23  ? -4.342  -8.104  56.503  0.70 46.86 ? 2   GLU   C O   1 
ATOM   3775 C CB  . GLU   C 1 23  ? -2.409  -8.097  59.580  0.70 53.30 ? 2   GLU   C CB  1 
ATOM   3776 C CG  . GLU   C 1 23  ? -1.324  -9.137  59.308  0.70 59.45 ? 2   GLU   C CG  1 
ATOM   3777 C CD  . GLU   C 1 23  ? -0.792  -9.214  57.888  0.70 61.24 ? 2   GLU   C CD  1 
ATOM   3778 O OE1 . GLU   C 1 23  ? -0.411  -8.148  57.367  0.70 65.71 ? 2   GLU   C OE1 1 
ATOM   3779 O OE2 . GLU   C 1 23  ? -0.734  -10.320 57.304  0.70 59.76 ? 2   GLU   C OE2 1 
ATOM   3780 N N   . ALA   C 1 24  ? -3.474  -6.294  57.523  1.00 43.94 ? 3   ALA   C N   1 
ATOM   3781 C CA  . ALA   C 1 24  ? -3.757  -5.329  56.480  1.00 38.87 ? 3   ALA   C CA  1 
ATOM   3782 C C   . ALA   C 1 24  ? -2.919  -5.656  55.242  1.00 35.70 ? 3   ALA   C C   1 
ATOM   3783 O O   . ALA   C 1 24  ? -1.727  -5.938  55.349  1.00 33.02 ? 3   ALA   C O   1 
ATOM   3784 C CB  . ALA   C 1 24  ? -3.427  -3.946  57.009  1.00 37.22 ? 3   ALA   C CB  1 
ATOM   3785 N N   . PRO   C 1 25  ? -3.491  -5.583  54.021  1.00 33.53 ? 4   PRO   C N   1 
ATOM   3786 C CA  . PRO   C 1 25  ? -2.686  -5.795  52.811  1.00 29.01 ? 4   PRO   C CA  1 
ATOM   3787 C C   . PRO   C 1 25  ? -1.727  -4.620  52.588  1.00 28.83 ? 4   PRO   C C   1 
ATOM   3788 O O   . PRO   C 1 25  ? -1.868  -3.585  53.239  1.00 26.61 ? 4   PRO   C O   1 
ATOM   3789 C CB  . PRO   C 1 25  ? -3.791  -5.959  51.747  1.00 29.60 ? 4   PRO   C CB  1 
ATOM   3790 C CG  . PRO   C 1 25  ? -4.920  -5.048  52.237  1.00 33.25 ? 4   PRO   C CG  1 
ATOM   3791 C CD  . PRO   C 1 25  ? -4.899  -5.254  53.757  1.00 29.06 ? 4   PRO   C CD  1 
ATOM   3792 N N   . ALA   C 1 26  ? -0.703  -4.800  51.713  1.00 25.69 ? 5   ALA   C N   1 
ATOM   3793 C CA  . ALA   C 1 26  ? 0.299   -3.764  51.481  1.00 24.52 ? 5   ALA   C CA  1 
ATOM   3794 C C   . ALA   C 1 26  ? 0.412   -3.455  49.985  1.00 23.35 ? 5   ALA   C C   1 
ATOM   3795 O O   . ALA   C 1 26  ? 0.264   -4.353  49.153  1.00 23.28 ? 5   ALA   C O   1 
ATOM   3796 C CB  . ALA   C 1 26  ? 1.672   -4.203  52.013  1.00 27.31 ? 5   ALA   C CB  1 
ATOM   3797 N N   . ALA   C 1 27  ? 0.716   -2.186  49.677  1.00 22.82 ? 6   ALA   C N   1 
ATOM   3798 C CA  . ALA   C 1 27  ? 0.812   -1.735  48.300  1.00 22.67 ? 6   ALA   C CA  1 
ATOM   3799 C C   . ALA   C 1 27  ? 2.108   -0.957  48.121  1.00 22.76 ? 6   ALA   C C   1 
ATOM   3800 O O   . ALA   C 1 27  ? 2.486   -0.142  48.983  1.00 22.82 ? 6   ALA   C O   1 
ATOM   3801 C CB  . ALA   C 1 27  ? -0.364  -0.885  47.930  1.00 23.56 ? 6   ALA   C CB  1 
ATOM   3802 N N   . VAL   C 1 28  ? 2.740   -1.187  46.964  1.00 19.35 ? 7   VAL   C N   1 
ATOM   3803 C CA  . VAL   C 1 28  ? 3.803   -0.294  46.533  1.00 20.67 ? 7   VAL   C CA  1 
ATOM   3804 C C   . VAL   C 1 28  ? 3.234   0.695   45.520  1.00 20.45 ? 7   VAL   C C   1 
ATOM   3805 O O   . VAL   C 1 28  ? 2.580   0.273   44.556  1.00 20.88 ? 7   VAL   C O   1 
ATOM   3806 C CB  . VAL   C 1 28  ? 4.884   -1.190  45.910  1.00 20.93 ? 7   VAL   C CB  1 
ATOM   3807 C CG1 . VAL   C 1 28  ? 5.909   -0.342  45.152  1.00 19.95 ? 7   VAL   C CG1 1 
ATOM   3808 C CG2 . VAL   C 1 28  ? 5.603   -2.011  46.992  1.00 23.69 ? 7   VAL   C CG2 1 
ATOM   3809 N N   . VAL   C 1 29  ? 3.503   1.996   45.723  1.00 20.03 ? 8   VAL   C N   1 
ATOM   3810 C CA  . VAL   C 1 29  ? 3.145   3.004   44.737  1.00 20.59 ? 8   VAL   C CA  1 
ATOM   3811 C C   . VAL   C 1 29  ? 4.421   3.730   44.308  1.00 23.08 ? 8   VAL   C C   1 
ATOM   3812 O O   . VAL   C 1 29  ? 5.111   4.313   45.152  1.00 21.87 ? 8   VAL   C O   1 
ATOM   3813 C CB  . VAL   C 1 29  ? 2.115   4.029   45.261  1.00 20.53 ? 8   VAL   C CB  1 
ATOM   3814 C CG1 . VAL   C 1 29  ? 1.791   4.991   44.140  1.00 21.20 ? 8   VAL   C CG1 1 
ATOM   3815 C CG2 . VAL   C 1 29  ? 0.820   3.347   45.730  1.00 20.25 ? 8   VAL   C CG2 1 
ATOM   3816 N N   . THR   C 1 30  ? 4.732   3.694   42.998  1.00 21.33 ? 9   THR   C N   1 
ATOM   3817 C CA  . THR   C 1 30  ? 5.937   4.371   42.530  1.00 22.46 ? 9   THR   C CA  1 
ATOM   3818 C C   . THR   C 1 30  ? 5.618   5.845   42.274  1.00 23.52 ? 9   THR   C C   1 
ATOM   3819 O O   . THR   C 1 30  ? 4.483   6.178   41.945  1.00 24.60 ? 9   THR   C O   1 
ATOM   3820 C CB  . THR   C 1 30  ? 6.581   3.680   41.322  1.00 21.45 ? 9   THR   C CB  1 
ATOM   3821 O OG1 . THR   C 1 30  ? 5.678   3.763   40.212  1.00 21.13 ? 9   THR   C OG1 1 
ATOM   3822 C CG2 . THR   C 1 30  ? 6.886   2.227   41.649  1.00 21.00 ? 9   THR   C CG2 1 
ATOM   3823 N N   . GLY   C 1 31  ? 6.619   6.714   42.465  1.00 22.57 ? 10  GLY   C N   1 
ATOM   3824 C CA  . GLY   C 1 31  ? 6.453   8.148   42.289  1.00 21.58 ? 10  GLY   C CA  1 
ATOM   3825 C C   . GLY   C 1 31  ? 5.299   8.660   43.141  1.00 23.04 ? 10  GLY   C C   1 
ATOM   3826 O O   . GLY   C 1 31  ? 4.507   9.462   42.675  1.00 23.71 ? 10  GLY   C O   1 
ATOM   3827 N N   . ALA   C 1 32  ? 5.250   8.264   44.413  1.00 21.59 ? 11  ALA   C N   1 
ATOM   3828 C CA  . ALA   C 1 32  ? 4.070   8.496   45.231  1.00 21.92 ? 11  ALA   C CA  1 
ATOM   3829 C C   . ALA   C 1 32  ? 4.211   9.697   46.170  1.00 21.95 ? 11  ALA   C C   1 
ATOM   3830 O O   . ALA   C 1 32  ? 3.326   9.924   46.984  1.00 23.06 ? 11  ALA   C O   1 
ATOM   3831 C CB  . ALA   C 1 32  ? 3.774   7.236   46.003  1.00 21.14 ? 11  ALA   C CB  1 
ATOM   3832 N N   . ALA   C 1 33  ? 5.267   10.506  46.025  1.00 23.94 ? 12  ALA   C N   1 
ATOM   3833 C CA  . ALA   C 1 33  ? 5.487   11.640  46.921  1.00 26.08 ? 12  ALA   C CA  1 
ATOM   3834 C C   . ALA   C 1 33  ? 4.538   12.811  46.651  1.00 30.91 ? 12  ALA   C C   1 
ATOM   3835 O O   . ALA   C 1 33  ? 4.262   13.603  47.571  1.00 27.05 ? 12  ALA   C O   1 
ATOM   3836 C CB  . ALA   C 1 33  ? 6.937   12.121  46.858  1.00 25.25 ? 12  ALA   C CB  1 
ATOM   3837 N N   . LYS   C 1 34  ? 4.089   12.959  45.393  1.00 28.03 ? 13  LYS   C N   1 
ATOM   3838 C CA  . LYS   C 1 34  ? 3.342   14.155  44.985  1.00 28.81 ? 13  LYS   C CA  1 
ATOM   3839 C C   . LYS   C 1 34  ? 2.231   13.799  43.988  1.00 28.51 ? 13  LYS   C C   1 
ATOM   3840 O O   . LYS   C 1 34  ? 2.163   12.670  43.502  1.00 25.19 ? 13  LYS   C O   1 
ATOM   3841 C CB  . LYS   C 1 34  ? 4.261   15.196  44.326  1.00 29.59 ? 13  LYS   C CB  1 
ATOM   3842 C CG  . LYS   C 1 34  ? 5.334   15.890  45.169  0.50 30.84 ? 13  LYS   C CG  1 
ATOM   3843 C CD  . LYS   C 1 34  ? 6.244   16.766  44.309  0.50 27.58 ? 13  LYS   C CD  1 
ATOM   3844 N N   . ARG   C 1 35  ? 1.308   14.755  43.748  1.00 26.36 ? 14  ARG   C N   1 
ATOM   3845 C CA  . ARG   C 1 35  ? 0.346   14.700  42.654  1.00 24.03 ? 14  ARG   C CA  1 
ATOM   3846 C C   . ARG   C 1 35  ? -0.447  13.394  42.660  1.00 23.87 ? 14  ARG   C C   1 
ATOM   3847 O O   . ARG   C 1 35  ? -1.084  13.035  43.658  1.00 25.28 ? 14  ARG   C O   1 
ATOM   3848 C CB  . ARG   C 1 35  ? 1.097   15.038  41.363  1.00 26.70 ? 14  ARG   C CB  1 
ATOM   3849 C CG  . ARG   C 1 35  ? 1.611   16.471  41.437  1.00 27.51 ? 14  ARG   C CG  1 
ATOM   3850 C CD  . ARG   C 1 35  ? 2.831   16.687  40.537  1.00 32.33 ? 14  ARG   C CD  1 
ATOM   3851 N NE  . ARG   C 1 35  ? 2.436   16.477  39.138  1.00 36.43 ? 14  ARG   C NE  1 
ATOM   3852 C CZ  . ARG   C 1 35  ? 1.664   17.252  38.359  1.00 40.14 ? 14  ARG   C CZ  1 
ATOM   3853 N NH1 . ARG   C 1 35  ? 1.207   18.429  38.795  1.00 34.82 ? 14  ARG   C NH1 1 
ATOM   3854 N NH2 . ARG   C 1 35  ? 1.368   16.830  37.129  1.00 37.75 ? 14  ARG   C NH2 1 
ATOM   3855 N N   . ILE   C 1 36  ? -0.480  12.702  41.509  1.00 21.88 ? 15  ILE   C N   1 
ATOM   3856 C CA  . ILE   C 1 36  ? -1.379  11.560  41.380  1.00 23.53 ? 15  ILE   C CA  1 
ATOM   3857 C C   . ILE   C 1 36  ? -0.900  10.390  42.249  1.00 23.35 ? 15  ILE   C C   1 
ATOM   3858 O O   . ILE   C 1 36  ? -1.701  9.684   42.847  1.00 20.69 ? 15  ILE   C O   1 
ATOM   3859 C CB  . ILE   C 1 36  ? -1.553  11.181  39.890  1.00 24.63 ? 15  ILE   C CB  1 
ATOM   3860 C CG1 . ILE   C 1 36  ? -2.399  12.252  39.171  1.00 22.69 ? 15  ILE   C CG1 1 
ATOM   3861 C CG2 . ILE   C 1 36  ? -2.164  9.781   39.709  1.00 20.89 ? 15  ILE   C CG2 1 
ATOM   3862 C CD1 . ILE   C 1 36  ? -2.265  12.198  37.668  1.00 24.76 ? 15  ILE   C CD1 1 
ATOM   3863 N N   . GLY   C 1 37  ? 0.404   10.099  42.216  1.00 22.04 ? 16  GLY   C N   1 
ATOM   3864 C CA  . GLY   C 1 37  ? 0.902   9.014   43.048  1.00 23.65 ? 16  GLY   C CA  1 
ATOM   3865 C C   . GLY   C 1 37  ? 0.587   9.249   44.534  1.00 23.59 ? 16  GLY   C C   1 
ATOM   3866 O O   . GLY   C 1 37  ? 0.212   8.315   45.233  1.00 20.91 ? 16  GLY   C O   1 
ATOM   3867 N N   . ARG   C 1 38  ? 0.697   10.515  44.990  1.00 21.77 ? 17  ARG   C N   1 
ATOM   3868 C CA  . ARG   C 1 38  ? 0.299   10.862  46.338  1.00 23.80 ? 17  ARG   C CA  1 
ATOM   3869 C C   . ARG   C 1 38  ? -1.171  10.535  46.602  1.00 24.37 ? 17  ARG   C C   1 
ATOM   3870 O O   . ARG   C 1 38  ? -1.482  9.828   47.561  1.00 25.41 ? 17  ARG   C O   1 
ATOM   3871 C CB  . ARG   C 1 38  ? 0.723   12.297  46.668  1.00 27.47 ? 17  ARG   C CB  1 
ATOM   3872 C CG  . ARG   C 1 38  ? 0.336   12.733  48.078  1.00 32.79 ? 17  ARG   C CG  1 
ATOM   3873 C CD  . ARG   C 1 38  ? 0.845   14.189  48.205  1.00 41.25 ? 17  ARG   C CD  1 
ATOM   3874 N NE  . ARG   C 1 38  ? 1.212   14.612  49.561  1.00 49.44 ? 17  ARG   C NE  1 
ATOM   3875 C CZ  . ARG   C 1 38  ? 0.377   14.607  50.593  1.00 51.54 ? 17  ARG   C CZ  1 
ATOM   3876 N NH1 . ARG   C 1 38  ? 0.817   14.935  51.796  1.00 43.44 ? 17  ARG   C NH1 1 
ATOM   3877 N NH2 . ARG   C 1 38  ? -0.886  14.263  50.409  1.00 47.08 ? 17  ARG   C NH2 1 
ATOM   3878 N N   . ALA   C 1 39  ? -2.078  11.003  45.730  1.00 27.16 ? 18  ALA   C N   1 
ATOM   3879 C CA  . ALA   C 1 39  ? -3.499  10.730  45.885  1.00 25.02 ? 18  ALA   C CA  1 
ATOM   3880 C C   . ALA   C 1 39  ? -3.789  9.232   45.930  1.00 24.35 ? 18  ALA   C C   1 
ATOM   3881 O O   . ALA   C 1 39  ? -4.639  8.802   46.698  1.00 22.72 ? 18  ALA   C O   1 
ATOM   3882 C CB  . ALA   C 1 39  ? -4.298  11.405  44.777  1.00 24.41 ? 18  ALA   C CB  1 
ATOM   3883 N N   . ILE   C 1 40  ? -3.133  8.450   45.048  1.00 22.34 ? 19  ILE   C N   1 
ATOM   3884 C CA  . ILE   C 1 40  ? -3.269  6.990   45.055  1.00 20.01 ? 19  ILE   C CA  1 
ATOM   3885 C C   . ILE   C 1 40  ? -2.833  6.408   46.410  1.00 22.74 ? 19  ILE   C C   1 
ATOM   3886 O O   . ILE   C 1 40  ? -3.557  5.584   46.984  1.00 22.13 ? 19  ILE   C O   1 
ATOM   3887 C CB  . ILE   C 1 40  ? -2.481  6.373   43.879  1.00 19.76 ? 19  ILE   C CB  1 
ATOM   3888 C CG1 . ILE   C 1 40  ? -3.120  6.822   42.512  1.00 21.44 ? 19  ILE   C CG1 1 
ATOM   3889 C CG2 . ILE   C 1 40  ? -2.472  4.841   44.004  1.00 17.11 ? 19  ILE   C CG2 1 
ATOM   3890 C CD1 . ILE   C 1 40  ? -2.217  6.587   41.305  1.00 24.38 ? 19  ILE   C CD1 1 
ATOM   3891 N N   . ALA   C 1 41  ? -1.611  6.765   46.863  1.00 23.48 ? 20  ALA   C N   1 
ATOM   3892 C CA  . ALA   C 1 41  ? -1.092  6.293   48.157  1.00 23.96 ? 20  ALA   C CA  1 
ATOM   3893 C C   . ALA   C 1 41  ? -2.079  6.613   49.280  1.00 22.20 ? 20  ALA   C C   1 
ATOM   3894 O O   . ALA   C 1 41  ? -2.455  5.742   50.043  1.00 23.52 ? 20  ALA   C O   1 
ATOM   3895 C CB  . ALA   C 1 41  ? 0.277   6.870   48.486  1.00 21.42 ? 20  ALA   C CB  1 
ATOM   3896 N N   . VAL   C 1 42  ? -2.542  7.849   49.344  1.00 22.05 ? 21  VAL   C N   1 
ATOM   3897 C CA  . VAL   C 1 42  ? -3.506  8.248   50.370  1.00 24.41 ? 21  VAL   C CA  1 
ATOM   3898 C C   . VAL   C 1 42  ? -4.785  7.426   50.305  1.00 27.93 ? 21  VAL   C C   1 
ATOM   3899 O O   . VAL   C 1 42  ? -5.299  6.962   51.336  1.00 27.08 ? 21  VAL   C O   1 
ATOM   3900 C CB  . VAL   C 1 42  ? -3.823  9.752   50.238  1.00 23.61 ? 21  VAL   C CB  1 
ATOM   3901 C CG1 . VAL   C 1 42  ? -4.994  10.161  51.140  1.00 26.03 ? 21  VAL   C CG1 1 
ATOM   3902 C CG2 . VAL   C 1 42  ? -2.569  10.582  50.521  1.00 26.00 ? 21  VAL   C CG2 1 
ATOM   3903 N N   . LYS   C 1 43  ? -5.352  7.310   49.088  1.00 24.47 ? 22  LYS   C N   1 
ATOM   3904 C CA  . LYS   C 1 43  ? -6.601  6.603   48.943  1.00 24.66 ? 22  LYS   C CA  1 
ATOM   3905 C C   . LYS   C 1 43  ? -6.452  5.130   49.341  1.00 24.89 ? 22  LYS   C C   1 
ATOM   3906 O O   . LYS   C 1 43  ? -7.343  4.580   50.011  1.00 23.01 ? 22  LYS   C O   1 
ATOM   3907 C CB  . LYS   C 1 43  ? -7.214  6.933   47.563  1.00 27.07 ? 22  LYS   C CB  1 
ATOM   3908 C CG  . LYS   C 1 43  ? -8.732  6.903   47.582  0.70 30.19 ? 22  LYS   C CG  1 
ATOM   3909 C CD  . LYS   C 1 43  ? -9.417  7.465   46.335  0.70 31.93 ? 22  LYS   C CD  1 
ATOM   3910 C CE  . LYS   C 1 43  ? -9.490  8.948   46.215  0.70 29.62 ? 22  LYS   C CE  1 
ATOM   3911 N NZ  . LYS   C 1 43  ? -10.745 9.422   46.806  0.70 37.71 ? 22  LYS   C NZ  1 
ATOM   3912 N N   . LEU   C 1 44  ? -5.378  4.446   48.878  1.00 23.84 ? 23  LEU   C N   1 
ATOM   3913 C CA  . LEU   C 1 44  ? -5.145  3.060   49.296  1.00 21.75 ? 23  LEU   C CA  1 
ATOM   3914 C C   . LEU   C 1 44  ? -5.022  3.000   50.831  1.00 24.68 ? 23  LEU   C C   1 
ATOM   3915 O O   . LEU   C 1 44  ? -5.585  2.133   51.508  1.00 23.57 ? 23  LEU   C O   1 
ATOM   3916 C CB  . LEU   C 1 44  ? -3.858  2.520   48.651  1.00 22.13 ? 23  LEU   C CB  1 
ATOM   3917 C CG  . LEU   C 1 44  ? -3.966  2.197   47.153  1.00 23.00 ? 23  LEU   C CG  1 
ATOM   3918 C CD1 . LEU   C 1 44  ? -2.604  1.931   46.479  1.00 22.32 ? 23  LEU   C CD1 1 
ATOM   3919 C CD2 . LEU   C 1 44  ? -4.828  0.965   47.048  1.00 23.70 ? 23  LEU   C CD2 1 
ATOM   3920 N N   . HIS   C 1 45  ? -4.279  3.957   51.390  1.00 24.79 ? 24  HIS   C N   1 
ATOM   3921 C CA  . HIS   C 1 45  ? -4.085  3.922   52.844  1.00 24.85 ? 24  HIS   C CA  1 
ATOM   3922 C C   . HIS   C 1 45  ? -5.428  4.110   53.568  1.00 27.88 ? 24  HIS   C C   1 
ATOM   3923 O O   . HIS   C 1 45  ? -5.726  3.426   54.566  1.00 27.96 ? 24  HIS   C O   1 
ATOM   3924 C CB  . HIS   C 1 45  ? -3.057  4.984   53.241  1.00 25.06 ? 24  HIS   C CB  1 
ATOM   3925 C CG  . HIS   C 1 45  ? -2.710  4.935   54.705  1.00 27.41 ? 24  HIS   C CG  1 
ATOM   3926 N ND1 . HIS   C 1 45  ? -3.343  5.731   55.645  1.00 28.76 ? 24  HIS   C ND1 1 
ATOM   3927 C CD2 . HIS   C 1 45  ? -1.786  4.194   55.377  1.00 27.65 ? 24  HIS   C CD2 1 
ATOM   3928 C CE1 . HIS   C 1 45  ? -2.793  5.508   56.842  1.00 27.65 ? 24  HIS   C CE1 1 
ATOM   3929 N NE2 . HIS   C 1 45  ? -1.857  4.563   56.707  1.00 26.96 ? 24  HIS   C NE2 1 
ATOM   3930 N N   . GLN   C 1 46  ? -6.275  4.988   53.017  1.00 28.84 ? 25  GLN   C N   1 
ATOM   3931 C CA  . GLN   C 1 46  ? -7.587  5.243   53.611  1.00 28.20 ? 25  GLN   C CA  1 
ATOM   3932 C C   . GLN   C 1 46  ? -8.489  4.026   53.470  1.00 31.46 ? 25  GLN   C C   1 
ATOM   3933 O O   . GLN   C 1 46  ? -9.419  3.888   54.239  1.00 31.66 ? 25  GLN   C O   1 
ATOM   3934 C CB  . GLN   C 1 46  ? -8.314  6.418   52.976  1.00 28.71 ? 25  GLN   C CB  1 
ATOM   3935 C CG  . GLN   C 1 46  ? -7.629  7.744   53.269  1.00 29.96 ? 25  GLN   C CG  1 
ATOM   3936 C CD  . GLN   C 1 46  ? -8.224  8.898   52.494  1.00 39.91 ? 25  GLN   C CD  1 
ATOM   3937 O OE1 . GLN   C 1 46  ? -8.913  8.694   51.486  1.00 45.09 ? 25  GLN   C OE1 1 
ATOM   3938 N NE2 . GLN   C 1 46  ? -7.946  10.116  52.952  1.00 35.79 ? 25  GLN   C NE2 1 
ATOM   3939 N N   . THR   C 1 47  ? -8.188  3.129   52.522  1.00 30.93 ? 26  THR   C N   1 
ATOM   3940 C CA  . THR   C 1 47  ? -8.990  1.938   52.285  1.00 27.41 ? 26  THR   C CA  1 
ATOM   3941 C C   . THR   C 1 47  ? -8.502  0.808   53.191  1.00 29.52 ? 26  THR   C C   1 
ATOM   3942 O O   . THR   C 1 47  ? -9.139  -0.237  53.281  1.00 31.11 ? 26  THR   C O   1 
ATOM   3943 C CB  . THR   C 1 47  ? -8.893  1.561   50.797  1.00 33.40 ? 26  THR   C CB  1 
ATOM   3944 O OG1 . THR   C 1 47  ? -9.302  2.697   50.036  1.00 33.49 ? 26  THR   C OG1 1 
ATOM   3945 C CG2 . THR   C 1 47  ? -9.862  0.472   50.389  1.00 35.04 ? 26  THR   C CG2 1 
ATOM   3946 N N   . GLY   C 1 48  ? -7.349  1.006   53.841  1.00 29.77 ? 27  GLY   C N   1 
ATOM   3947 C CA  . GLY   C 1 48  ? -6.837  0.042   54.806  1.00 28.24 ? 27  GLY   C CA  1 
ATOM   3948 C C   . GLY   C 1 48  ? -5.522  -0.599  54.371  1.00 29.76 ? 27  GLY   C C   1 
ATOM   3949 O O   . GLY   C 1 48  ? -5.087  -1.557  54.995  1.00 27.45 ? 27  GLY   C O   1 
ATOM   3950 N N   . TYR   C 1 49  ? -4.862  -0.065  53.329  1.00 25.43 ? 28  TYR   C N   1 
ATOM   3951 C CA  . TYR   C 1 49  ? -3.581  -0.645  52.954  1.00 29.42 ? 28  TYR   C CA  1 
ATOM   3952 C C   . TYR   C 1 49  ? -2.451  -0.019  53.771  1.00 26.00 ? 28  TYR   C C   1 
ATOM   3953 O O   . TYR   C 1 49  ? -2.481  1.159   54.091  1.00 26.03 ? 28  TYR   C O   1 
ATOM   3954 C CB  . TYR   C 1 49  ? -3.204  -0.447  51.476  1.00 24.75 ? 28  TYR   C CB  1 
ATOM   3955 C CG  . TYR   C 1 49  ? -3.989  -1.353  50.541  1.00 26.47 ? 28  TYR   C CG  1 
ATOM   3956 C CD1 . TYR   C 1 49  ? -5.319  -1.055  50.203  1.00 30.71 ? 28  TYR   C CD1 1 
ATOM   3957 C CD2 . TYR   C 1 49  ? -3.414  -2.500  50.014  1.00 27.90 ? 28  TYR   C CD2 1 
ATOM   3958 C CE1 . TYR   C 1 49  ? -6.052  -1.873  49.352  1.00 29.67 ? 28  TYR   C CE1 1 
ATOM   3959 C CE2 . TYR   C 1 49  ? -4.139  -3.334  49.169  1.00 30.00 ? 28  TYR   C CE2 1 
ATOM   3960 C CZ  . TYR   C 1 49  ? -5.450  -3.006  48.834  1.00 32.43 ? 28  TYR   C CZ  1 
ATOM   3961 O OH  . TYR   C 1 49  ? -6.177  -3.822  48.037  1.00 31.08 ? 28  TYR   C OH  1 
ATOM   3962 N N   . ARG   C 1 50  ? -1.405  -0.815  54.016  1.00 25.71 ? 29  ARG   C N   1 
ATOM   3963 C CA  . ARG   C 1 50  ? -0.084  -0.270  54.320  1.00 23.82 ? 29  ARG   C CA  1 
ATOM   3964 C C   . ARG   C 1 50  ? 0.616   0.077   53.002  1.00 25.54 ? 29  ARG   C C   1 
ATOM   3965 O O   . ARG   C 1 50  ? 0.389   -0.612  52.019  1.00 25.57 ? 29  ARG   C O   1 
ATOM   3966 C CB  . ARG   C 1 50  ? 0.670   -1.313  55.160  1.00 25.85 ? 29  ARG   C CB  1 
ATOM   3967 C CG  . ARG   C 1 50  ? -0.077  -1.544  56.481  1.00 25.71 ? 29  ARG   C CG  1 
ATOM   3968 C CD  . ARG   C 1 50  ? 0.642   -2.612  57.317  1.00 29.20 ? 29  ARG   C CD  1 
ATOM   3969 N NE  . ARG   C 1 50  ? 0.457   -3.969  56.781  1.00 29.66 ? 29  ARG   C NE  1 
ATOM   3970 C CZ  . ARG   C 1 50  ? 1.121   -5.015  57.242  1.00 30.25 ? 29  ARG   C CZ  1 
ATOM   3971 N NH1 . ARG   C 1 50  ? 0.835   -6.212  56.784  1.00 29.96 ? 29  ARG   C NH1 1 
ATOM   3972 N NH2 . ARG   C 1 50  ? 2.049   -4.861  58.182  1.00 31.22 ? 29  ARG   C NH2 1 
ATOM   3973 N N   . VAL   C 1 51  ? 1.438   1.138   52.978  1.00 23.92 ? 30  VAL   C N   1 
ATOM   3974 C CA  . VAL   C 1 51  ? 1.944   1.645   51.703  1.00 22.94 ? 30  VAL   C CA  1 
ATOM   3975 C C   . VAL   C 1 51  ? 3.456   1.892   51.727  1.00 22.03 ? 30  VAL   C C   1 
ATOM   3976 O O   . VAL   C 1 51  ? 4.007   2.441   52.688  1.00 21.64 ? 30  VAL   C O   1 
ATOM   3977 C CB  . VAL   C 1 51  ? 1.229   2.924   51.215  1.00 24.37 ? 30  VAL   C CB  1 
ATOM   3978 C CG1 . VAL   C 1 51  ? -0.259  2.661   50.959  1.00 26.38 ? 30  VAL   C CG1 1 
ATOM   3979 C CG2 . VAL   C 1 51  ? 1.401   4.121   52.153  1.00 24.43 ? 30  VAL   C CG2 1 
ATOM   3980 N N   . VAL   C 1 52  ? 4.112   1.521   50.625  1.00 19.41 ? 31  VAL   C N   1 
ATOM   3981 C CA  . VAL   C 1 52  ? 5.471   1.958   50.343  1.00 19.10 ? 31  VAL   C CA  1 
ATOM   3982 C C   . VAL   C 1 52  ? 5.388   3.128   49.388  1.00 21.95 ? 31  VAL   C C   1 
ATOM   3983 O O   . VAL   C 1 52  ? 4.871   2.976   48.287  1.00 23.96 ? 31  VAL   C O   1 
ATOM   3984 C CB  . VAL   C 1 52  ? 6.316   0.847   49.701  1.00 20.69 ? 31  VAL   C CB  1 
ATOM   3985 C CG1 . VAL   C 1 52  ? 7.730   1.346   49.325  1.00 19.66 ? 31  VAL   C CG1 1 
ATOM   3986 C CG2 . VAL   C 1 52  ? 6.353   -0.382  50.584  1.00 21.02 ? 31  VAL   C CG2 1 
ATOM   3987 N N   . ILE   C 1 53  ? 5.905   4.276   49.818  1.00 21.01 ? 32  ILE   C N   1 
ATOM   3988 C CA  . ILE   C 1 53  ? 5.923   5.465   48.993  1.00 21.16 ? 32  ILE   C CA  1 
ATOM   3989 C C   . ILE   C 1 53  ? 7.297   5.503   48.332  1.00 24.17 ? 32  ILE   C C   1 
ATOM   3990 O O   . ILE   C 1 53  ? 8.286   5.856   48.995  1.00 24.40 ? 32  ILE   C O   1 
ATOM   3991 C CB  . ILE   C 1 53  ? 5.765   6.663   49.934  1.00 20.55 ? 32  ILE   C CB  1 
ATOM   3992 C CG1 . ILE   C 1 53  ? 4.409   6.582   50.660  1.00 21.62 ? 32  ILE   C CG1 1 
ATOM   3993 C CG2 . ILE   C 1 53  ? 5.946   8.009   49.216  1.00 21.28 ? 32  ILE   C CG2 1 
ATOM   3994 C CD1 . ILE   C 1 53  ? 4.424   7.295   51.988  1.00 23.73 ? 32  ILE   C CD1 1 
ATOM   3995 N N   . HIS   C 1 54  ? 7.346   5.114   47.050  1.00 21.63 ? 33  HIS   C N   1 
ATOM   3996 C CA  . HIS   C 1 54  ? 8.589   5.188   46.294  1.00 21.50 ? 33  HIS   C CA  1 
ATOM   3997 C C   . HIS   C 1 54  ? 8.734   6.645   45.856  1.00 23.22 ? 33  HIS   C C   1 
ATOM   3998 O O   . HIS   C 1 54  ? 7.722   7.293   45.577  1.00 23.35 ? 33  HIS   C O   1 
ATOM   3999 C CB  . HIS   C 1 54  ? 8.599   4.179   45.135  1.00 23.67 ? 33  HIS   C CB  1 
ATOM   4000 C CG  . HIS   C 1 54  ? 9.568   4.645   44.090  1.00 22.44 ? 33  HIS   C CG  1 
ATOM   4001 N ND1 . HIS   C 1 54  ? 9.212   5.562   43.122  1.00 23.59 ? 33  HIS   C ND1 1 
ATOM   4002 C CD2 . HIS   C 1 54  ? 10.890  4.427   43.943  1.00 21.34 ? 33  HIS   C CD2 1 
ATOM   4003 C CE1 . HIS   C 1 54  ? 10.281  5.870   42.375  1.00 22.36 ? 33  HIS   C CE1 1 
ATOM   4004 N NE2 . HIS   C 1 54  ? 11.323  5.181   42.856  1.00 22.74 ? 33  HIS   C NE2 1 
ATOM   4005 N N   . TYR   C 1 55  ? 9.972   7.150   45.804  1.00 20.66 ? 34  TYR   C N   1 
ATOM   4006 C CA  . TYR   C 1 55  ? 10.222  8.475   45.273  1.00 20.98 ? 34  TYR   C CA  1 
ATOM   4007 C C   . TYR   C 1 55  ? 11.608  8.472   44.634  1.00 22.38 ? 34  TYR   C C   1 
ATOM   4008 O O   . TYR   C 1 55  ? 12.395  7.563   44.864  1.00 22.37 ? 34  TYR   C O   1 
ATOM   4009 C CB  . TYR   C 1 55  ? 10.109  9.541   46.372  1.00 23.76 ? 34  TYR   C CB  1 
ATOM   4010 C CG  . TYR   C 1 55  ? 11.323  9.574   47.305  1.00 22.59 ? 34  TYR   C CG  1 
ATOM   4011 C CD1 . TYR   C 1 55  ? 11.411  8.730   48.423  1.00 22.13 ? 34  TYR   C CD1 1 
ATOM   4012 C CD2 . TYR   C 1 55  ? 12.387  10.439  47.030  1.00 27.13 ? 34  TYR   C CD2 1 
ATOM   4013 C CE1 . TYR   C 1 55  ? 12.529  8.754   49.249  1.00 24.56 ? 34  TYR   C CE1 1 
ATOM   4014 C CE2 . TYR   C 1 55  ? 13.511  10.470  47.846  1.00 26.34 ? 34  TYR   C CE2 1 
ATOM   4015 C CZ  . TYR   C 1 55  ? 13.578  9.618   48.944  1.00 25.84 ? 34  TYR   C CZ  1 
ATOM   4016 O OH  . TYR   C 1 55  ? 14.676  9.663   49.746  1.00 25.19 ? 34  TYR   C OH  1 
ATOM   4017 N N   . HIS   C 1 56  ? 11.882  9.509   43.842  1.00 24.25 ? 35  HIS   C N   1 
ATOM   4018 C CA  . HIS   C 1 56  ? 13.181  9.678   43.215  1.00 26.59 ? 35  HIS   C CA  1 
ATOM   4019 C C   . HIS   C 1 56  ? 13.883  10.885  43.829  1.00 28.53 ? 35  HIS   C C   1 
ATOM   4020 O O   . HIS   C 1 56  ? 14.871  10.698  44.521  1.00 28.15 ? 35  HIS   C O   1 
ATOM   4021 C CB  . HIS   C 1 56  ? 13.055  9.729   41.688  1.00 30.50 ? 35  HIS   C CB  1 
ATOM   4022 C CG  . HIS   C 1 56  ? 14.366  9.954   41.005  1.00 31.72 ? 35  HIS   C CG  1 
ATOM   4023 N ND1 . HIS   C 1 56  ? 14.499  10.818  39.942  1.00 33.08 ? 35  HIS   C ND1 1 
ATOM   4024 C CD2 . HIS   C 1 56  ? 15.603  9.528   41.307  1.00 33.64 ? 35  HIS   C CD2 1 
ATOM   4025 C CE1 . HIS   C 1 56  ? 15.773  10.844  39.558  1.00 37.71 ? 35  HIS   C CE1 1 
ATOM   4026 N NE2 . HIS   C 1 56  ? 16.469  10.076  40.393  1.00 36.22 ? 35  HIS   C NE2 1 
ATOM   4027 N N   . ASN   C 1 57  ? 13.362  12.097  43.621  1.00 27.32 ? 36  ASN   C N   1 
ATOM   4028 C CA  . ASN   C 1 57  ? 14.053  13.267  44.122  1.00 32.71 ? 36  ASN   C CA  1 
ATOM   4029 C C   . ASN   C 1 57  ? 13.291  13.944  45.252  1.00 34.06 ? 36  ASN   C C   1 
ATOM   4030 O O   . ASN   C 1 57  ? 13.882  14.759  45.955  1.00 31.70 ? 36  ASN   C O   1 
ATOM   4031 C CB  . ASN   C 1 57  ? 14.203  14.365  43.070  1.00 34.01 ? 36  ASN   C CB  1 
ATOM   4032 C CG  . ASN   C 1 57  ? 15.179  13.991  41.987  1.00 42.17 ? 36  ASN   C CG  1 
ATOM   4033 O OD1 . ASN   C 1 57  ? 16.252  13.455  42.283  1.00 43.48 ? 36  ASN   C OD1 1 
ATOM   4034 N ND2 . ASN   C 1 57  ? 14.790  14.195  40.735  1.00 41.18 ? 36  ASN   C ND2 1 
ATOM   4035 N N   . SER   C 1 58  ? 11.988  13.661  45.394  1.00 31.53 ? 37  SER   C N   1 
ATOM   4036 C CA  . SER   C 1 58  ? 11.158  14.419  46.327  1.00 29.75 ? 37  SER   C CA  1 
ATOM   4037 C C   . SER   C 1 58  ? 11.204  13.828  47.747  1.00 29.22 ? 37  SER   C C   1 
ATOM   4038 O O   . SER   C 1 58  ? 10.187  13.326  48.265  1.00 23.87 ? 37  SER   C O   1 
ATOM   4039 C CB  . SER   C 1 58  ? 9.721   14.498  45.825  1.00 30.68 ? 37  SER   C CB  1 
ATOM   4040 O OG  . SER   C 1 58  ? 9.642   15.214  44.601  1.00 30.43 ? 37  SER   C OG  1 
ATOM   4041 N N   . ALA   C 1 59  ? 12.383  13.913  48.379  1.00 26.87 ? 38  ALA   C N   1 
ATOM   4042 C CA  . ALA   C 1 59  ? 12.607  13.262  49.668  1.00 29.46 ? 38  ALA   C CA  1 
ATOM   4043 C C   . ALA   C 1 59  ? 11.723  13.861  50.763  1.00 29.45 ? 38  ALA   C C   1 
ATOM   4044 O O   . ALA   C 1 59  ? 11.090  13.129  51.524  1.00 26.31 ? 38  ALA   C O   1 
ATOM   4045 C CB  . ALA   C 1 59  ? 14.078  13.305  50.049  1.00 27.48 ? 38  ALA   C CB  1 
ATOM   4046 N N   . GLU   C 1 60  ? 11.704  15.200  50.846  1.00 30.06 ? 39  GLU   C N   1 
ATOM   4047 C CA  A GLU   C 1 60  ? 10.999  15.885  51.915  0.60 33.77 ? 39  GLU   C CA  1 
ATOM   4048 C CA  B GLU   C 1 60  ? 10.998  15.879  51.921  0.40 32.12 ? 39  GLU   C CA  1 
ATOM   4049 C C   . GLU   C 1 60  ? 9.513   15.561  51.798  1.00 31.66 ? 39  GLU   C C   1 
ATOM   4050 O O   . GLU   C 1 60  ? 8.874   15.218  52.795  1.00 28.85 ? 39  GLU   C O   1 
ATOM   4051 C CB  A GLU   C 1 60  ? 11.332  17.379  51.920  0.60 37.27 ? 39  GLU   C CB  1 
ATOM   4052 C CB  B GLU   C 1 60  ? 11.191  17.396  51.993  0.40 33.46 ? 39  GLU   C CB  1 
ATOM   4053 C CG  A GLU   C 1 60  ? 12.826  17.646  52.089  0.60 45.50 ? 39  GLU   C CG  1 
ATOM   4054 C CG  B GLU   C 1 60  ? 10.627  17.986  53.284  0.40 36.21 ? 39  GLU   C CG  1 
ATOM   4055 C CD  A GLU   C 1 60  ? 13.222  19.087  52.354  0.60 49.10 ? 39  GLU   C CD  1 
ATOM   4056 C CD  B GLU   C 1 60  ? 10.300  19.468  53.272  0.40 41.07 ? 39  GLU   C CD  1 
ATOM   4057 O OE1 A GLU   C 1 60  ? 12.391  19.994  52.149  0.60 51.24 ? 39  GLU   C OE1 1 
ATOM   4058 O OE1 B GLU   C 1 60  ? 11.164  20.278  52.881  0.40 44.39 ? 39  GLU   C OE1 1 
ATOM   4059 O OE2 A GLU   C 1 60  ? 14.371  19.292  52.793  0.60 55.70 ? 39  GLU   C OE2 1 
ATOM   4060 O OE2 B GLU   C 1 60  ? 9.171   19.808  53.676  0.40 43.50 ? 39  GLU   C OE2 1 
ATOM   4061 N N   . ALA   C 1 61  ? 8.983   15.631  50.551  1.00 30.49 ? 40  ALA   C N   1 
ATOM   4062 C CA  . ALA   C 1 61  ? 7.560   15.395  50.376  1.00 28.94 ? 40  ALA   C CA  1 
ATOM   4063 C C   . ALA   C 1 61  ? 7.222   13.948  50.724  1.00 24.13 ? 40  ALA   C C   1 
ATOM   4064 O O   . ALA   C 1 61  ? 6.155   13.682  51.259  1.00 25.45 ? 40  ALA   C O   1 
ATOM   4065 C CB  . ALA   C 1 61  ? 7.089   15.787  48.970  1.00 33.03 ? 40  ALA   C CB  1 
ATOM   4066 N N   . ALA   C 1 62  ? 8.102   13.008  50.373  1.00 24.94 ? 41  ALA   C N   1 
ATOM   4067 C CA  . ALA   C 1 62  ? 7.788   11.601  50.615  1.00 22.31 ? 41  ALA   C CA  1 
ATOM   4068 C C   . ALA   C 1 62  ? 7.760   11.330  52.119  1.00 24.67 ? 41  ALA   C C   1 
ATOM   4069 O O   . ALA   C 1 62  ? 6.884   10.621  52.604  1.00 27.06 ? 41  ALA   C O   1 
ATOM   4070 C CB  . ALA   C 1 62  ? 8.839   10.718  49.984  1.00 21.96 ? 41  ALA   C CB  1 
ATOM   4071 N N   . VAL   C 1 63  ? 8.763   11.868  52.828  1.00 25.14 ? 42  VAL   C N   1 
ATOM   4072 C CA  . VAL   C 1 63  ? 8.890   11.591  54.263  1.00 26.93 ? 42  VAL   C CA  1 
ATOM   4073 C C   . VAL   C 1 63  ? 7.699   12.225  54.981  1.00 28.10 ? 42  VAL   C C   1 
ATOM   4074 O O   . VAL   C 1 63  ? 7.094   11.639  55.886  1.00 27.33 ? 42  VAL   C O   1 
ATOM   4075 C CB  . VAL   C 1 63  ? 10.228  12.113  54.836  1.00 25.27 ? 42  VAL   C CB  1 
ATOM   4076 C CG1 . VAL   C 1 63  ? 10.243  11.985  56.372  1.00 26.76 ? 42  VAL   C CG1 1 
ATOM   4077 C CG2 . VAL   C 1 63  ? 11.396  11.335  54.238  1.00 24.24 ? 42  VAL   C CG2 1 
ATOM   4078 N N   . SER   C 1 64  ? 7.369   13.441  54.531  1.00 25.85 ? 43  SER   C N   1 
ATOM   4079 C CA  . SER   C 1 64  ? 6.215   14.148  55.063  1.00 27.66 ? 43  SER   C CA  1 
ATOM   4080 C C   . SER   C 1 64  ? 4.906   13.363  54.881  1.00 27.60 ? 43  SER   C C   1 
ATOM   4081 O O   . SER   C 1 64  ? 4.053   13.317  55.772  1.00 26.98 ? 43  SER   C O   1 
ATOM   4082 C CB  . SER   C 1 64  ? 6.196   15.532  54.429  1.00 29.74 ? 43  SER   C CB  1 
ATOM   4083 O OG  . SER   C 1 64  ? 5.011   16.198  54.810  1.00 38.87 ? 43  SER   C OG  1 
ATOM   4084 N N   . LEU   C 1 65  ? 4.723   12.714  53.715  1.00 27.82 ? 44  LEU   C N   1 
ATOM   4085 C CA  . LEU   C 1 65  ? 3.532   11.916  53.496  1.00 24.09 ? 44  LEU   C CA  1 
ATOM   4086 C C   . LEU   C 1 65  ? 3.530   10.702  54.429  1.00 25.37 ? 44  LEU   C C   1 
ATOM   4087 O O   . LEU   C 1 65  ? 2.497   10.388  55.021  1.00 24.99 ? 44  LEU   C O   1 
ATOM   4088 C CB  . LEU   C 1 65  ? 3.394   11.509  52.019  1.00 26.01 ? 44  LEU   C CB  1 
ATOM   4089 C CG  . LEU   C 1 65  ? 2.260   10.531  51.690  1.00 25.68 ? 44  LEU   C CG  1 
ATOM   4090 C CD1 . LEU   C 1 65  ? 0.903   11.161  51.993  1.00 23.33 ? 44  LEU   C CD1 1 
ATOM   4091 C CD2 . LEU   C 1 65  ? 2.328   10.027  50.217  1.00 26.14 ? 44  LEU   C CD2 1 
ATOM   4092 N N   . ALA   C 1 66  ? 4.668   9.982   54.523  1.00 24.92 ? 45  ALA   C N   1 
ATOM   4093 C CA  . ALA   C 1 66  ? 4.713   8.811   55.400  1.00 24.98 ? 45  ALA   C CA  1 
ATOM   4094 C C   . ALA   C 1 66  ? 4.350   9.190   56.843  1.00 26.95 ? 45  ALA   C C   1 
ATOM   4095 O O   . ALA   C 1 66  ? 3.651   8.446   57.547  1.00 28.14 ? 45  ALA   C O   1 
ATOM   4096 C CB  . ALA   C 1 66  ? 6.082   8.152   55.326  1.00 26.45 ? 45  ALA   C CB  1 
ATOM   4097 N N   . ASP   C 1 67  ? 4.829   10.360  57.262  1.00 26.22 ? 46  ASP   C N   1 
ATOM   4098 C CA  . ASP   C 1 67  ? 4.595   10.865  58.614  1.00 30.41 ? 46  ASP   C CA  1 
ATOM   4099 C C   . ASP   C 1 67  ? 3.092   11.056  58.830  1.00 29.57 ? 46  ASP   C C   1 
ATOM   4100 O O   . ASP   C 1 67  ? 2.517   10.584  59.818  1.00 30.95 ? 46  ASP   C O   1 
ATOM   4101 C CB  . ASP   C 1 67  ? 5.380   12.154  58.845  1.00 32.08 ? 46  ASP   C CB  1 
ATOM   4102 C CG  . ASP   C 1 67  ? 5.100   12.881  60.161  1.00 42.72 ? 46  ASP   C CG  1 
ATOM   4103 O OD1 . ASP   C 1 67  ? 5.242   12.246  61.235  1.00 44.41 ? 46  ASP   C OD1 1 
ATOM   4104 O OD2 . ASP   C 1 67  ? 4.720   14.075  60.108  1.00 40.05 ? 46  ASP   C OD2 1 
ATOM   4105 N N   . GLU   C 1 68  ? 2.452   11.714  57.854  1.00 31.52 ? 47  GLU   C N   1 
ATOM   4106 C CA  . GLU   C 1 68  ? 1.036   12.031  57.932  1.00 31.58 ? 47  GLU   C CA  1 
ATOM   4107 C C   . GLU   C 1 68  ? 0.234   10.732  58.003  1.00 31.01 ? 47  GLU   C C   1 
ATOM   4108 O O   . GLU   C 1 68  ? -0.660  10.611  58.837  1.00 31.36 ? 47  GLU   C O   1 
ATOM   4109 C CB  . GLU   C 1 68  ? 0.644   12.941  56.763  1.00 33.84 ? 47  GLU   C CB  1 
ATOM   4110 C CG  . GLU   C 1 68  ? -0.822  13.369  56.786  0.60 35.12 ? 47  GLU   C CG  1 
ATOM   4111 C CD  . GLU   C 1 68  ? -1.244  14.022  55.481  0.60 39.39 ? 47  GLU   C CD  1 
ATOM   4112 O OE1 . GLU   C 1 68  ? -2.405  13.809  55.063  0.60 43.05 ? 47  GLU   C OE1 1 
ATOM   4113 O OE2 . GLU   C 1 68  ? -0.395  14.703  54.861  0.60 37.57 ? 47  GLU   C OE2 1 
ATOM   4114 N N   . LEU   C 1 69  ? 0.555   9.755   57.139  1.00 26.80 ? 48  LEU   C N   1 
ATOM   4115 C CA  . LEU   C 1 69  ? -0.171  8.488   57.146  1.00 27.31 ? 48  LEU   C CA  1 
ATOM   4116 C C   . LEU   C 1 69  ? 0.051   7.694   58.443  1.00 23.97 ? 48  LEU   C C   1 
ATOM   4117 O O   . LEU   C 1 69  ? -0.881  7.078   58.985  1.00 27.83 ? 48  LEU   C O   1 
ATOM   4118 C CB  . LEU   C 1 69  ? 0.195   7.659   55.910  1.00 27.77 ? 48  LEU   C CB  1 
ATOM   4119 C CG  . LEU   C 1 69  ? -0.168  8.315   54.564  1.00 31.57 ? 48  LEU   C CG  1 
ATOM   4120 C CD1 . LEU   C 1 69  ? 0.091   7.350   53.409  1.00 29.77 ? 48  LEU   C CD1 1 
ATOM   4121 C CD2 . LEU   C 1 69  ? -1.600  8.838   54.560  1.00 28.44 ? 48  LEU   C CD2 1 
ATOM   4122 N N   . ASN   C 1 70  ? 1.294   7.674   58.916  1.00 26.58 ? 49  ASN   C N   1 
ATOM   4123 C CA  . ASN   C 1 70  ? 1.640   6.967   60.146  1.00 28.12 ? 49  ASN   C CA  1 
ATOM   4124 C C   . ASN   C 1 70  ? 0.931   7.564   61.371  1.00 32.04 ? 49  ASN   C C   1 
ATOM   4125 O O   . ASN   C 1 70  ? 0.645   6.831   62.323  1.00 30.46 ? 49  ASN   C O   1 
ATOM   4126 C CB  . ASN   C 1 70  ? 3.149   6.893   60.335  1.00 25.21 ? 49  ASN   C CB  1 
ATOM   4127 C CG  . ASN   C 1 70  ? 3.759   5.788   59.510  1.00 23.95 ? 49  ASN   C CG  1 
ATOM   4128 O OD1 . ASN   C 1 70  ? 3.149   4.719   59.356  1.00 25.08 ? 49  ASN   C OD1 1 
ATOM   4129 N ND2 . ASN   C 1 70  ? 4.960   6.016   59.001  1.00 23.35 ? 49  ASN   C ND2 1 
ATOM   4130 N N   . LYS   C 1 71  ? 0.667   8.878   61.346  1.00 31.75 ? 50  LYS   C N   1 
ATOM   4131 C CA  . LYS   C 1 71  ? -0.120  9.543   62.383  1.00 35.91 ? 50  LYS   C CA  1 
ATOM   4132 C C   . LYS   C 1 71  ? -1.534  8.981   62.432  1.00 37.98 ? 50  LYS   C C   1 
ATOM   4133 O O   . LYS   C 1 71  ? -2.114  8.855   63.503  1.00 35.87 ? 50  LYS   C O   1 
ATOM   4134 C CB  . LYS   C 1 71  ? -0.233  11.065  62.208  1.00 38.97 ? 50  LYS   C CB  1 
ATOM   4135 C CG  . LYS   C 1 71  ? 0.954   11.913  62.673  1.00 38.91 ? 50  LYS   C CG  1 
ATOM   4136 C CD  . LYS   C 1 71  ? 0.785   13.420  62.486  0.50 37.67 ? 50  LYS   C CD  1 
ATOM   4137 N N   . GLU   C 1 72  ? -2.090  8.651   61.263  1.00 35.47 ? 51  GLU   C N   1 
ATOM   4138 C CA  . GLU   C 1 72  ? -3.418  8.076   61.160  1.00 37.25 ? 51  GLU   C CA  1 
ATOM   4139 C C   . GLU   C 1 72  ? -3.397  6.670   61.758  1.00 36.11 ? 51  GLU   C C   1 
ATOM   4140 O O   . GLU   C 1 72  ? -4.254  6.310   62.570  1.00 34.70 ? 51  GLU   C O   1 
ATOM   4141 C CB  . GLU   C 1 72  ? -3.804  8.209   59.677  1.00 37.35 ? 51  GLU   C CB  1 
ATOM   4142 C CG  . GLU   C 1 72  ? -5.278  8.478   59.417  0.70 43.41 ? 51  GLU   C CG  1 
ATOM   4143 C CD  . GLU   C 1 72  ? -5.820  9.644   60.224  0.70 40.16 ? 51  GLU   C CD  1 
ATOM   4144 O OE1 . GLU   C 1 72  ? -5.368  10.808  60.132  0.70 39.29 ? 51  GLU   C OE1 1 
ATOM   4145 O OE2 . GLU   C 1 72  ? -6.731  9.325   60.991  0.70 52.19 ? 51  GLU   C OE2 1 
ATOM   4146 N N   . ARG   C 1 73  ? -2.407  5.861   61.361  1.00 30.09 ? 52  ARG   C N   1 
ATOM   4147 C CA  . ARG   C 1 73  ? -2.259  4.500   61.849  1.00 30.26 ? 52  ARG   C CA  1 
ATOM   4148 C C   . ARG   C 1 73  ? -0.767  4.170   61.903  1.00 35.69 ? 52  ARG   C C   1 
ATOM   4149 O O   . ARG   C 1 73  ? -0.053  4.266   60.896  1.00 28.23 ? 52  ARG   C O   1 
ATOM   4150 C CB  . ARG   C 1 73  ? -2.970  3.402   61.044  1.00 33.53 ? 52  ARG   C CB  1 
ATOM   4151 C CG  . ARG   C 1 73  ? -4.441  3.559   60.683  1.00 40.87 ? 52  ARG   C CG  1 
ATOM   4152 C CD  . ARG   C 1 73  ? -4.994  2.238   60.142  1.00 43.46 ? 52  ARG   C CD  1 
ATOM   4153 N NE  . ARG   C 1 73  ? -4.458  1.817   58.834  1.00 42.83 ? 52  ARG   C NE  1 
ATOM   4154 C CZ  . ARG   C 1 73  ? -4.735  2.320   57.608  1.00 40.31 ? 52  ARG   C CZ  1 
ATOM   4155 N NH1 . ARG   C 1 73  ? -5.524  3.382   57.450  1.00 32.48 ? 52  ARG   C NH1 1 
ATOM   4156 N NH2 . ARG   C 1 73  ? -4.169  1.764   56.540  1.00 35.07 ? 52  ARG   C NH2 1 
ATOM   4157 N N   . SER   C 1 74  ? -0.297  3.761   63.091  1.00 28.82 ? 53  SER   C N   1 
ATOM   4158 C CA  . SER   C 1 74  ? 1.129   3.570   63.303  1.00 30.98 ? 53  SER   C CA  1 
ATOM   4159 C C   . SER   C 1 74  ? 1.676   2.452   62.413  1.00 25.63 ? 53  SER   C C   1 
ATOM   4160 O O   . SER   C 1 74  ? 1.048   1.401   62.286  1.00 24.92 ? 53  SER   C O   1 
ATOM   4161 C CB  . SER   C 1 74  ? 1.371   3.248   64.788  1.00 33.20 ? 53  SER   C CB  1 
ATOM   4162 O OG  . SER   C 1 74  ? 1.010   4.408   65.530  1.00 38.95 ? 53  SER   C OG  1 
ATOM   4163 N N   . ASN   C 1 75  ? 2.885   2.655   61.861  1.00 21.29 ? 54  ASN   C N   1 
ATOM   4164 C CA  . ASN   C 1 75  ? 3.595   1.558   61.208  1.00 20.46 ? 54  ASN   C CA  1 
ATOM   4165 C C   . ASN   C 1 75  ? 2.813   1.101   59.972  1.00 21.68 ? 54  ASN   C C   1 
ATOM   4166 O O   . ASN   C 1 75  ? 2.763   -0.099  59.648  1.00 21.82 ? 54  ASN   C O   1 
ATOM   4167 C CB  . ASN   C 1 75  ? 3.852   0.355   62.117  1.00 23.15 ? 54  ASN   C CB  1 
ATOM   4168 C CG  . ASN   C 1 75  ? 4.714   0.723   63.300  1.00 24.76 ? 54  ASN   C CG  1 
ATOM   4169 O OD1 . ASN   C 1 75  ? 5.749   1.387   63.141  1.00 30.66 ? 54  ASN   C OD1 1 
ATOM   4170 N ND2 . ASN   C 1 75  ? 4.352   0.224   64.468  1.00 22.14 ? 54  ASN   C ND2 1 
ATOM   4171 N N   . THR   C 1 76  ? 2.274   2.063   59.235  1.00 21.05 ? 55  THR   C N   1 
ATOM   4172 C CA  . THR   C 1 76  ? 1.559   1.647   58.024  1.00 23.83 ? 55  THR   C CA  1 
ATOM   4173 C C   . THR   C 1 76  ? 2.110   2.315   56.759  1.00 26.14 ? 55  THR   C C   1 
ATOM   4174 O O   . THR   C 1 76  ? 1.579   2.046   55.697  1.00 29.56 ? 55  THR   C O   1 
ATOM   4175 C CB  . THR   C 1 76  ? 0.054   1.884   58.147  1.00 25.27 ? 55  THR   C CB  1 
ATOM   4176 O OG1 . THR   C 1 76  ? -0.033  3.302   58.284  1.00 24.46 ? 55  THR   C OG1 1 
ATOM   4177 C CG2 . THR   C 1 76  ? -0.602  1.002   59.203  1.00 27.46 ? 55  THR   C CG2 1 
ATOM   4178 N N   . ALA   C 1 77  ? 3.139   3.175   56.853  1.00 23.44 ? 56  ALA   C N   1 
ATOM   4179 C CA  . ALA   C 1 77  ? 3.699   3.837   55.678  1.00 23.76 ? 56  ALA   C CA  1 
ATOM   4180 C C   . ALA   C 1 77  ? 5.224   3.874   55.792  1.00 24.94 ? 56  ALA   C C   1 
ATOM   4181 O O   . ALA   C 1 77  ? 5.758   4.193   56.870  1.00 22.31 ? 56  ALA   C O   1 
ATOM   4182 C CB  . ALA   C 1 77  ? 3.168   5.262   55.529  1.00 21.54 ? 56  ALA   C CB  1 
ATOM   4183 N N   . VAL   C 1 78  ? 5.921   3.610   54.674  1.00 22.51 ? 57  VAL   C N   1 
ATOM   4184 C CA  . VAL   C 1 78  ? 7.382   3.756   54.657  1.00 22.24 ? 57  VAL   C CA  1 
ATOM   4185 C C   . VAL   C 1 78  ? 7.781   4.392   53.334  1.00 25.13 ? 57  VAL   C C   1 
ATOM   4186 O O   . VAL   C 1 78  ? 6.949   4.448   52.427  1.00 24.24 ? 57  VAL   C O   1 
ATOM   4187 C CB  . VAL   C 1 78  ? 8.060   2.370   54.798  1.00 25.78 ? 57  VAL   C CB  1 
ATOM   4188 C CG1 . VAL   C 1 78  ? 7.808   1.711   56.147  1.00 23.90 ? 57  VAL   C CG1 1 
ATOM   4189 C CG2 . VAL   C 1 78  ? 7.658   1.426   53.667  1.00 26.87 ? 57  VAL   C CG2 1 
ATOM   4190 N N   . VAL   C 1 79  ? 9.057   4.800   53.197  1.00 23.86 ? 58  VAL   C N   1 
ATOM   4191 C CA  . VAL   C 1 79  ? 9.536   5.413   51.963  1.00 25.42 ? 58  VAL   C CA  1 
ATOM   4192 C C   . VAL   C 1 79  ? 10.653  4.550   51.379  1.00 24.35 ? 58  VAL   C C   1 
ATOM   4193 O O   . VAL   C 1 79  ? 11.368  3.863   52.114  1.00 23.81 ? 58  VAL   C O   1 
ATOM   4194 C CB  . VAL   C 1 79  ? 9.957   6.901   52.008  1.00 28.85 ? 58  VAL   C CB  1 
ATOM   4195 C CG1 . VAL   C 1 79  ? 8.866   7.774   52.630  1.00 26.33 ? 58  VAL   C CG1 1 
ATOM   4196 C CG2 . VAL   C 1 79  ? 11.300  7.119   52.718  1.00 29.58 ? 58  VAL   C CG2 1 
ATOM   4197 N N   . CYS   C 1 80  ? 10.806  4.626   50.050  1.00 23.11 ? 59  CYS   C N   1 
ATOM   4198 C CA  . CYS   C 1 80  ? 11.838  3.874   49.365  1.00 24.20 ? 59  CYS   C CA  1 
ATOM   4199 C C   . CYS   C 1 80  ? 12.331  4.763   48.226  1.00 27.70 ? 59  CYS   C C   1 
ATOM   4200 O O   . CYS   C 1 80  ? 11.539  5.146   47.363  1.00 25.89 ? 59  CYS   C O   1 
ATOM   4201 C CB  . CYS   C 1 80  ? 11.264  2.577   48.795  1.00 26.27 ? 59  CYS   C CB  1 
ATOM   4202 S SG  . CYS   C 1 80  ? 12.551  1.609   47.955  1.00 36.85 ? 59  CYS   C SG  1 
ATOM   4203 N N   . GLN   C 1 81  ? 13.630  5.097   48.210  1.00 25.45 ? 60  GLN   C N   1 
ATOM   4204 C CA  . GLN   C 1 81  ? 14.149  5.958   47.155  1.00 25.55 ? 60  GLN   C CA  1 
ATOM   4205 C C   . GLN   C 1 81  ? 14.732  5.077   46.052  1.00 25.50 ? 60  GLN   C C   1 
ATOM   4206 O O   . GLN   C 1 81  ? 15.456  4.138   46.360  1.00 22.69 ? 60  GLN   C O   1 
ATOM   4207 C CB  . GLN   C 1 81  ? 15.226  6.885   47.711  1.00 27.37 ? 60  GLN   C CB  1 
ATOM   4208 C CG  . GLN   C 1 81  ? 15.602  8.033   46.781  1.00 25.61 ? 60  GLN   C CG  1 
ATOM   4209 C CD  . GLN   C 1 81  ? 16.646  7.654   45.750  1.00 31.71 ? 60  GLN   C CD  1 
ATOM   4210 O OE1 . GLN   C 1 81  ? 17.416  6.692   45.928  1.00 29.40 ? 60  GLN   C OE1 1 
ATOM   4211 N NE2 . GLN   C 1 81  ? 16.684  8.435   44.676  1.00 26.91 ? 60  GLN   C NE2 1 
ATOM   4212 N N   . ALA   C 1 82  ? 14.421  5.389   44.779  1.00 23.86 ? 61  ALA   C N   1 
ATOM   4213 C CA  . ALA   C 1 82  ? 15.073  4.724   43.655  1.00 24.25 ? 61  ALA   C CA  1 
ATOM   4214 C C   . ALA   C 1 82  ? 14.986  5.559   42.378  1.00 26.00 ? 61  ALA   C C   1 
ATOM   4215 O O   . ALA   C 1 82  ? 13.943  6.145   42.087  1.00 23.48 ? 61  ALA   C O   1 
ATOM   4216 C CB  . ALA   C 1 82  ? 14.494  3.341   43.445  1.00 22.91 ? 61  ALA   C CB  1 
ATOM   4217 N N   . ASP   C 1 83  ? 16.087  5.586   41.603  1.00 23.59 ? 62  ASP   C N   1 
ATOM   4218 C CA  . ASP   C 1 83  ? 16.035  6.108   40.237  1.00 22.39 ? 62  ASP   C CA  1 
ATOM   4219 C C   . ASP   C 1 83  ? 15.517  4.982   39.339  1.00 21.97 ? 62  ASP   C C   1 
ATOM   4220 O O   . ASP   C 1 83  ? 16.011  3.850   39.430  1.00 25.25 ? 62  ASP   C O   1 
ATOM   4221 C CB  . ASP   C 1 83  ? 17.418  6.589   39.813  1.00 26.09 ? 62  ASP   C CB  1 
ATOM   4222 C CG  . ASP   C 1 83  ? 17.543  7.178   38.410  1.00 29.40 ? 62  ASP   C CG  1 
ATOM   4223 O OD1 . ASP   C 1 83  ? 16.510  7.462   37.780  1.00 25.78 ? 62  ASP   C OD1 1 
ATOM   4224 O OD2 . ASP   C 1 83  ? 18.685  7.360   37.962  1.00 32.89 ? 62  ASP   C OD2 1 
ATOM   4225 N N   . LEU   C 1 84  ? 14.500  5.258   38.506  1.00 20.82 ? 63  LEU   C N   1 
ATOM   4226 C CA  . LEU   C 1 84  ? 13.931  4.218   37.657  1.00 21.72 ? 63  LEU   C CA  1 
ATOM   4227 C C   . LEU   C 1 84  ? 14.393  4.361   36.196  1.00 23.45 ? 63  LEU   C C   1 
ATOM   4228 O O   . LEU   C 1 84  ? 13.841  3.714   35.290  1.00 22.46 ? 63  LEU   C O   1 
ATOM   4229 C CB  . LEU   C 1 84  ? 12.410  4.196   37.813  1.00 25.31 ? 63  LEU   C CB  1 
ATOM   4230 C CG  . LEU   C 1 84  ? 11.898  3.851   39.214  1.00 23.37 ? 63  LEU   C CG  1 
ATOM   4231 C CD1 . LEU   C 1 84  ? 10.373  3.889   39.218  1.00 23.37 ? 63  LEU   C CD1 1 
ATOM   4232 C CD2 . LEU   C 1 84  ? 12.362  2.468   39.605  1.00 21.90 ? 63  LEU   C CD2 1 
ATOM   4233 N N   . THR   C 1 85  ? 15.425  5.189   35.983  1.00 22.74 ? 64  THR   C N   1 
ATOM   4234 C CA  . THR   C 1 85  ? 16.145  5.245   34.709  1.00 26.08 ? 64  THR   C CA  1 
ATOM   4235 C C   . THR   C 1 85  ? 16.597  3.848   34.284  1.00 26.31 ? 64  THR   C C   1 
ATOM   4236 O O   . THR   C 1 85  ? 17.123  3.090   35.099  1.00 24.41 ? 64  THR   C O   1 
ATOM   4237 C CB  . THR   C 1 85  ? 17.345  6.193   34.830  1.00 27.71 ? 64  THR   C CB  1 
ATOM   4238 O OG1 . THR   C 1 85  ? 16.759  7.451   35.144  1.00 29.11 ? 64  THR   C OG1 1 
ATOM   4239 C CG2 . THR   C 1 85  ? 18.077  6.398   33.514  1.00 26.97 ? 64  THR   C CG2 1 
ATOM   4240 N N   . ASN   C 1 86  ? 16.499  3.541   32.981  1.00 23.83 ? 65  ASN   C N   1 
ATOM   4241 C CA  . ASN   C 1 86  ? 17.060  2.289   32.483  1.00 24.35 ? 65  ASN   C CA  1 
ATOM   4242 C C   . ASN   C 1 86  ? 18.592  2.267   32.621  1.00 24.66 ? 65  ASN   C C   1 
ATOM   4243 O O   . ASN   C 1 86  ? 19.261  3.261   32.387  1.00 25.63 ? 65  ASN   C O   1 
ATOM   4244 C CB  . ASN   C 1 86  ? 16.681  2.052   31.031  1.00 26.45 ? 65  ASN   C CB  1 
ATOM   4245 C CG  . ASN   C 1 86  ? 16.995  0.637   30.608  1.00 30.12 ? 65  ASN   C CG  1 
ATOM   4246 O OD1 . ASN   C 1 86  ? 16.620  -0.334  31.293  1.00 24.40 ? 65  ASN   C OD1 1 
ATOM   4247 N ND2 . ASN   C 1 86  ? 17.702  0.524   29.489  1.00 27.88 ? 65  ASN   C ND2 1 
ATOM   4248 N N   . SER   C 1 87  ? 19.131  1.131   33.083  1.00 27.24 ? 66  SER   C N   1 
ATOM   4249 C CA  . SER   C 1 87  ? 20.559  0.895   33.275  1.00 29.31 ? 66  SER   C CA  1 
ATOM   4250 C C   . SER   C 1 87  ? 20.720  -0.578  33.623  1.00 29.55 ? 66  SER   C C   1 
ATOM   4251 O O   . SER   C 1 87  ? 19.724  -1.267  33.861  1.00 31.18 ? 66  SER   C O   1 
ATOM   4252 C CB  . SER   C 1 87  ? 21.143  1.705   34.400  1.00 30.25 ? 66  SER   C CB  1 
ATOM   4253 O OG  . SER   C 1 87  ? 20.747  1.125   35.639  1.00 28.62 ? 66  SER   C OG  1 
ATOM   4254 N N   . ASN   C 1 88  ? 21.981  -1.029  33.712  1.00 29.06 ? 67  ASN   C N   1 
ATOM   4255 C CA  A ASN   C 1 88  ? 22.197  -2.422  34.071  0.60 32.57 ? 67  ASN   C CA  1 
ATOM   4256 C CA  B ASN   C 1 88  ? 22.352  -2.378  34.117  0.40 31.30 ? 67  ASN   C CA  1 
ATOM   4257 C C   . ASN   C 1 88  ? 21.957  -2.640  35.573  1.00 28.62 ? 67  ASN   C C   1 
ATOM   4258 O O   . ASN   C 1 88  ? 21.855  -3.775  36.006  1.00 31.45 ? 67  ASN   C O   1 
ATOM   4259 C CB  A ASN   C 1 88  ? 23.488  -2.992  33.463  0.60 34.67 ? 67  ASN   C CB  1 
ATOM   4260 C CB  B ASN   C 1 88  ? 23.827  -2.690  33.829  0.40 29.66 ? 67  ASN   C CB  1 
ATOM   4261 C CG  A ASN   C 1 88  ? 23.352  -3.410  32.011  0.60 36.60 ? 67  ASN   C CG  1 
ATOM   4262 C CG  B ASN   C 1 88  ? 24.820  -1.961  34.712  0.40 31.06 ? 67  ASN   C CG  1 
ATOM   4263 O OD1 A ASN   C 1 88  ? 22.312  -3.195  31.372  0.60 34.75 ? 67  ASN   C OD1 1 
ATOM   4264 O OD1 B ASN   C 1 88  ? 24.579  -0.831  35.143  0.40 31.26 ? 67  ASN   C OD1 1 
ATOM   4265 N ND2 A ASN   C 1 88  ? 24.396  -4.015  31.464  0.60 40.37 ? 67  ASN   C ND2 1 
ATOM   4266 N ND2 B ASN   C 1 88  ? 25.977  -2.564  34.948  0.40 34.26 ? 67  ASN   C ND2 1 
ATOM   4267 N N   . VAL   C 1 89  ? 21.765  -1.578  36.367  1.00 28.86 ? 68  VAL   C N   1 
ATOM   4268 C CA  . VAL   C 1 89  ? 21.415  -1.786  37.782  1.00 31.05 ? 68  VAL   C CA  1 
ATOM   4269 C C   . VAL   C 1 89  ? 19.900  -1.700  38.055  1.00 30.37 ? 68  VAL   C C   1 
ATOM   4270 O O   . VAL   C 1 89  ? 19.461  -1.917  39.196  1.00 26.86 ? 68  VAL   C O   1 
ATOM   4271 C CB  . VAL   C 1 89  ? 22.204  -0.882  38.760  1.00 36.01 ? 68  VAL   C CB  1 
ATOM   4272 C CG1 . VAL   C 1 89  ? 23.699  -0.941  38.459  1.00 34.40 ? 68  VAL   C CG1 1 
ATOM   4273 C CG2 . VAL   C 1 89  ? 21.707  0.569   38.786  1.00 31.50 ? 68  VAL   C CG2 1 
ATOM   4274 N N   . LEU   C 1 90  ? 19.102  -1.363  37.027  1.00 27.09 ? 69  LEU   C N   1 
ATOM   4275 C CA  . LEU   C 1 90  ? 17.677  -1.122  37.206  1.00 25.04 ? 69  LEU   C CA  1 
ATOM   4276 C C   . LEU   C 1 90  ? 16.992  -2.385  37.743  1.00 24.65 ? 69  LEU   C C   1 
ATOM   4277 O O   . LEU   C 1 90  ? 16.161  -2.307  38.654  1.00 28.37 ? 69  LEU   C O   1 
ATOM   4278 C CB  . LEU   C 1 90  ? 17.014  -0.543  35.934  1.00 24.96 ? 69  LEU   C CB  1 
ATOM   4279 C CG  . LEU   C 1 90  ? 15.501  -0.253  36.038  1.00 23.55 ? 69  LEU   C CG  1 
ATOM   4280 C CD1 . LEU   C 1 90  ? 15.178  0.755   37.157  1.00 22.61 ? 69  LEU   C CD1 1 
ATOM   4281 C CD2 . LEU   C 1 90  ? 14.845  0.187   34.699  1.00 21.39 ? 69  LEU   C CD2 1 
ATOM   4282 N N   . PRO   C 1 91  ? 17.303  -3.609  37.245  1.00 23.55 ? 70  PRO   C N   1 
ATOM   4283 C CA  . PRO   C 1 91  ? 16.649  -4.799  37.779  1.00 25.01 ? 70  PRO   C CA  1 
ATOM   4284 C C   . PRO   C 1 91  ? 16.830  -4.983  39.284  1.00 30.14 ? 70  PRO   C C   1 
ATOM   4285 O O   . PRO   C 1 91  ? 15.885  -5.355  39.979  1.00 25.82 ? 70  PRO   C O   1 
ATOM   4286 C CB  . PRO   C 1 91  ? 17.266  -5.936  36.974  1.00 23.23 ? 70  PRO   C CB  1 
ATOM   4287 C CG  . PRO   C 1 91  ? 17.656  -5.260  35.638  1.00 23.98 ? 70  PRO   C CG  1 
ATOM   4288 C CD  . PRO   C 1 91  ? 18.185  -3.898  36.093  1.00 25.20 ? 70  PRO   C CD  1 
ATOM   4289 N N   . ALA   C 1 92  ? 18.068  -4.749  39.762  1.00 27.77 ? 71  ALA   C N   1 
ATOM   4290 C CA  . ALA   C 1 92  ? 18.331  -4.788  41.195  1.00 28.60 ? 71  ALA   C CA  1 
ATOM   4291 C C   . ALA   C 1 92  ? 17.543  -3.700  41.916  1.00 28.09 ? 71  ALA   C C   1 
ATOM   4292 O O   . ALA   C 1 92  ? 17.011  -3.955  42.999  1.00 28.49 ? 71  ALA   C O   1 
ATOM   4293 C CB  . ALA   C 1 92  ? 19.821  -4.631  41.460  1.00 29.62 ? 71  ALA   C CB  1 
ATOM   4294 N N   . SER   C 1 93  ? 17.498  -2.477  41.356  1.00 27.31 ? 72  SER   C N   1 
ATOM   4295 C CA  . SER   C 1 93  ? 16.703  -1.452  42.016  1.00 25.52 ? 72  SER   C CA  1 
ATOM   4296 C C   . SER   C 1 93  ? 15.247  -1.879  42.170  1.00 29.10 ? 72  SER   C C   1 
ATOM   4297 O O   . SER   C 1 93  ? 14.635  -1.588  43.197  1.00 27.02 ? 72  SER   C O   1 
ATOM   4298 C CB  . SER   C 1 93  ? 16.750  -0.110  41.329  1.00 29.39 ? 72  SER   C CB  1 
ATOM   4299 O OG  . SER   C 1 93  ? 18.063  0.414   41.207  1.00 30.74 ? 72  SER   C OG  1 
ATOM   4300 N N   . CYS   C 1 94  ? 14.663  -2.485  41.118  1.00 25.48 ? 73  CYS   C N   1 
ATOM   4301 C CA  . CYS   C 1 94  ? 13.249  -2.829  41.151  1.00 23.18 ? 73  CYS   C CA  1 
ATOM   4302 C C   . CYS   C 1 94  ? 13.010  -3.957  42.149  1.00 23.68 ? 73  CYS   C C   1 
ATOM   4303 O O   . CYS   C 1 94  ? 12.024  -3.944  42.867  1.00 22.18 ? 73  CYS   C O   1 
ATOM   4304 C CB  . CYS   C 1 94  ? 12.709  -3.142  39.751  1.00 21.73 ? 73  CYS   C CB  1 
ATOM   4305 S SG  . CYS   C 1 94  ? 12.733  -1.641  38.726  1.00 23.47 ? 73  CYS   C SG  1 
ATOM   4306 N N   . GLU   C 1 95  ? 13.897  -4.955  42.154  1.00 27.58 ? 74  GLU   C N   1 
ATOM   4307 C CA  A GLU   C 1 95  ? 13.857  -6.021  43.147  0.60 28.68 ? 74  GLU   C CA  1 
ATOM   4308 C CA  B GLU   C 1 95  ? 13.879  -6.014  43.153  0.40 29.85 ? 74  GLU   C CA  1 
ATOM   4309 C C   . GLU   C 1 95  ? 13.810  -5.420  44.559  1.00 28.55 ? 74  GLU   C C   1 
ATOM   4310 O O   . GLU   C 1 95  ? 12.997  -5.854  45.371  1.00 29.03 ? 74  GLU   C O   1 
ATOM   4311 C CB  A GLU   C 1 95  ? 15.085  -6.914  42.958  0.60 32.06 ? 74  GLU   C CB  1 
ATOM   4312 C CB  B GLU   C 1 95  ? 15.124  -6.893  43.030  0.40 34.69 ? 74  GLU   C CB  1 
ATOM   4313 C CG  A GLU   C 1 95  ? 15.253  -7.957  44.054  0.60 38.86 ? 74  GLU   C CG  1 
ATOM   4314 C CG  B GLU   C 1 95  ? 14.804  -8.287  42.512  0.40 43.73 ? 74  GLU   C CG  1 
ATOM   4315 C CD  A GLU   C 1 95  ? 15.000  -9.376  43.603  0.60 51.86 ? 74  GLU   C CD  1 
ATOM   4316 C CD  B GLU   C 1 95  ? 13.887  -8.962  43.512  0.40 51.78 ? 74  GLU   C CD  1 
ATOM   4317 O OE1 A GLU   C 1 95  ? 15.866  -9.920  42.881  0.60 53.55 ? 74  GLU   C OE1 1 
ATOM   4318 O OE1 B GLU   C 1 95  ? 12.756  -8.471  43.709  0.40 55.63 ? 74  GLU   C OE1 1 
ATOM   4319 O OE2 A GLU   C 1 95  ? 13.931  -9.924  43.958  0.60 64.52 ? 74  GLU   C OE2 1 
ATOM   4320 O OE2 B GLU   C 1 95  ? 14.316  -9.967  44.120  0.40 60.36 ? 74  GLU   C OE2 1 
ATOM   4321 N N   . GLU   C 1 96  ? 14.672  -4.422  44.835  1.00 28.16 ? 75  GLU   C N   1 
ATOM   4322 C CA  A GLU   C 1 96  ? 14.795  -3.735  46.123  0.50 28.42 ? 75  GLU   C CA  1 
ATOM   4323 C CA  B GLU   C 1 96  ? 14.750  -3.839  46.164  0.50 28.18 ? 75  GLU   C CA  1 
ATOM   4324 C C   . GLU   C 1 96  ? 13.480  -3.054  46.511  1.00 30.18 ? 75  GLU   C C   1 
ATOM   4325 O O   . GLU   C 1 96  ? 13.107  -3.024  47.690  1.00 24.87 ? 75  GLU   C O   1 
ATOM   4326 C CB  A GLU   C 1 96  ? 15.990  -2.769  46.221  0.50 31.14 ? 75  GLU   C CB  1 
ATOM   4327 C CB  B GLU   C 1 96  ? 16.097  -3.147  46.378  0.50 30.47 ? 75  GLU   C CB  1 
ATOM   4328 C CG  A GLU   C 1 96  ? 15.706  -1.274  46.029  0.50 34.37 ? 75  GLU   C CG  1 
ATOM   4329 C CG  B GLU   C 1 96  ? 17.293  -4.101  46.374  0.50 29.00 ? 75  GLU   C CG  1 
ATOM   4330 C CD  A GLU   C 1 96  ? 16.790  -0.206  46.275  0.50 39.70 ? 75  GLU   C CD  1 
ATOM   4331 C CD  B GLU   C 1 96  ? 17.442  -5.115  47.509  0.50 32.87 ? 75  GLU   C CD  1 
ATOM   4332 O OE1 A GLU   C 1 96  ? 17.116  0.024   47.458  0.50 37.59 ? 75  GLU   C OE1 1 
ATOM   4333 O OE1 B GLU   C 1 96  ? 16.686  -5.136  48.505  0.50 31.91 ? 75  GLU   C OE1 1 
ATOM   4334 O OE2 A GLU   C 1 96  ? 17.327  0.405   45.314  0.50 34.20 ? 75  GLU   C OE2 1 
ATOM   4335 O OE2 B GLU   C 1 96  ? 18.369  -5.933  47.371  0.50 35.82 ? 75  GLU   C OE2 1 
ATOM   4336 N N   . ILE   C 1 97  ? 12.801  -2.428  45.512  1.00 26.08 ? 76  ILE   C N   1 
ATOM   4337 C CA  . ILE   C 1 97  ? 11.559  -1.714  45.820  1.00 23.96 ? 76  ILE   C CA  1 
ATOM   4338 C C   . ILE   C 1 97  ? 10.531  -2.706  46.360  1.00 24.23 ? 76  ILE   C C   1 
ATOM   4339 O O   . ILE   C 1 97  ? 9.847   -2.452  47.373  1.00 28.07 ? 76  ILE   C O   1 
ATOM   4340 C CB  . ILE   C 1 97  ? 11.028  -0.913  44.605  1.00 25.90 ? 76  ILE   C CB  1 
ATOM   4341 C CG1 . ILE   C 1 97  ? 12.020  0.190   44.199  1.00 26.65 ? 76  ILE   C CG1 1 
ATOM   4342 C CG2 . ILE   C 1 97  ? 9.627   -0.325  44.852  1.00 20.97 ? 76  ILE   C CG2 1 
ATOM   4343 C CD1 . ILE   C 1 97  ? 11.679  0.900   42.888  1.00 22.82 ? 76  ILE   C CD1 1 
ATOM   4344 N N   . ILE   C 1 98  ? 10.370  -3.814  45.648  1.00 21.32 ? 77  ILE   C N   1 
ATOM   4345 C CA  . ILE   C 1 98  ? 9.389   -4.823  46.045  1.00 22.79 ? 77  ILE   C CA  1 
ATOM   4346 C C   . ILE   C 1 98  ? 9.807   -5.344  47.427  1.00 28.20 ? 77  ILE   C C   1 
ATOM   4347 O O   . ILE   C 1 98  ? 8.985   -5.527  48.344  1.00 23.20 ? 77  ILE   C O   1 
ATOM   4348 C CB  . ILE   C 1 98  ? 9.266   -5.937  44.974  1.00 20.07 ? 77  ILE   C CB  1 
ATOM   4349 C CG1 . ILE   C 1 98  ? 8.643   -5.368  43.646  1.00 20.15 ? 77  ILE   C CG1 1 
ATOM   4350 C CG2 . ILE   C 1 98  ? 8.449   -7.152  45.460  1.00 20.77 ? 77  ILE   C CG2 1 
ATOM   4351 C CD1 . ILE   C 1 98  ? 7.366   -4.537  43.835  1.00 22.01 ? 77  ILE   C CD1 1 
ATOM   4352 N N   . ASN   C 1 99  ? 11.130  -5.547  47.562  1.00 26.88 ? 78  ASN   C N   1 
ATOM   4353 C CA  . ASN   C 1 99  ? 11.673  -6.144  48.765  1.00 27.60 ? 78  ASN   C CA  1 
ATOM   4354 C C   . ASN   C 1 99  ? 11.390  -5.241  49.954  1.00 27.19 ? 78  ASN   C C   1 
ATOM   4355 O O   . ASN   C 1 99  ? 11.169  -5.729  51.055  1.00 29.87 ? 78  ASN   C O   1 
ATOM   4356 C CB  . ASN   C 1 99  ? 13.166  -6.368  48.605  1.00 29.65 ? 78  ASN   C CB  1 
ATOM   4357 C CG  . ASN   C 1 99  ? 13.421  -7.814  48.872  0.70 35.87 ? 78  ASN   C CG  1 
ATOM   4358 O OD1 . ASN   C 1 99  ? 13.457  -8.234  50.039  0.70 37.62 ? 78  ASN   C OD1 1 
ATOM   4359 N ND2 . ASN   C 1 99  ? 13.478  -8.579  47.797  0.70 34.88 ? 78  ASN   C ND2 1 
ATOM   4360 N N   . SER   C 1 100 ? 11.400  -3.920  49.725  1.00 27.04 ? 79  SER   C N   1 
ATOM   4361 C CA  . SER   C 1 100 ? 11.127  -2.981  50.798  1.00 27.79 ? 79  SER   C CA  1 
ATOM   4362 C C   . SER   C 1 100 ? 9.732   -3.209  51.408  1.00 31.14 ? 79  SER   C C   1 
ATOM   4363 O O   . SER   C 1 100 ? 9.552   -3.055  52.620  1.00 26.04 ? 79  SER   C O   1 
ATOM   4364 C CB  . SER   C 1 100 ? 11.398  -1.557  50.387  1.00 29.98 ? 79  SER   C CB  1 
ATOM   4365 O OG  . SER   C 1 100 ? 10.303  -1.085  49.615  1.00 37.04 ? 79  SER   C OG  1 
ATOM   4366 N N   . CYS   C 1 101 ? 8.743   -3.591  50.584  1.00 24.80 ? 80  CYS   C N   1 
ATOM   4367 C CA  . CYS   C 1 101 ? 7.384   -3.850  51.055  1.00 25.23 ? 80  CYS   C CA  1 
ATOM   4368 C C   . CYS   C 1 101 ? 7.371   -5.106  51.929  1.00 25.80 ? 80  CYS   C C   1 
ATOM   4369 O O   . CYS   C 1 101 ? 6.752   -5.128  52.994  1.00 24.52 ? 80  CYS   C O   1 
ATOM   4370 C CB  . CYS   C 1 101 ? 6.420   -4.019  49.863  1.00 24.58 ? 80  CYS   C CB  1 
ATOM   4371 S SG  . CYS   C 1 101 ? 4.662   -3.896  50.287  1.00 24.46 ? 80  CYS   C SG  1 
ATOM   4372 N N   . PHE   C 1 102 ? 8.092   -6.149  51.501  1.00 25.46 ? 81  PHE   C N   1 
ATOM   4373 C CA  . PHE   C 1 102 ? 8.174   -7.374  52.287  1.00 30.11 ? 81  PHE   C CA  1 
ATOM   4374 C C   . PHE   C 1 102 ? 8.888   -7.157  53.624  1.00 31.34 ? 81  PHE   C C   1 
ATOM   4375 O O   . PHE   C 1 102 ? 8.476   -7.728  54.645  1.00 29.55 ? 81  PHE   C O   1 
ATOM   4376 C CB  . PHE   C 1 102 ? 8.798   -8.540  51.511  1.00 29.53 ? 81  PHE   C CB  1 
ATOM   4377 C CG  . PHE   C 1 102 ? 7.808   -9.132  50.511  1.00 31.30 ? 81  PHE   C CG  1 
ATOM   4378 C CD1 . PHE   C 1 102 ? 6.925   -10.144 50.884  1.00 33.62 ? 81  PHE   C CD1 1 
ATOM   4379 C CD2 . PHE   C 1 102 ? 7.763   -8.676  49.191  1.00 32.94 ? 81  PHE   C CD2 1 
ATOM   4380 C CE1 . PHE   C 1 102 ? 6.012   -10.680 49.969  1.00 31.46 ? 81  PHE   C CE1 1 
ATOM   4381 C CE2 . PHE   C 1 102 ? 6.871   -9.235  48.270  1.00 30.79 ? 81  PHE   C CE2 1 
ATOM   4382 C CZ  . PHE   C 1 102 ? 5.968   -10.200 48.668  1.00 31.20 ? 81  PHE   C CZ  1 
ATOM   4383 N N   . ARG   C 1 103 ? 9.951   -6.338  53.622  1.00 28.60 ? 82  ARG   C N   1 
ATOM   4384 C CA  A ARG   C 1 103 ? 10.754  -6.168  54.826  0.50 27.02 ? 82  ARG   C CA  1 
ATOM   4385 C CA  B ARG   C 1 103 ? 10.754  -6.169  54.825  0.50 27.64 ? 82  ARG   C CA  1 
ATOM   4386 C C   . ARG   C 1 103 ? 9.951   -5.395  55.865  1.00 29.75 ? 82  ARG   C C   1 
ATOM   4387 O O   . ARG   C 1 103 ? 10.048  -5.689  57.060  1.00 28.93 ? 82  ARG   C O   1 
ATOM   4388 C CB  A ARG   C 1 103 ? 12.087  -5.473  54.540  0.50 27.23 ? 82  ARG   C CB  1 
ATOM   4389 C CB  B ARG   C 1 103 ? 12.088  -5.475  54.542  0.50 28.87 ? 82  ARG   C CB  1 
ATOM   4390 C CG  A ARG   C 1 103 ? 12.991  -6.397  53.731  0.50 29.80 ? 82  ARG   C CG  1 
ATOM   4391 C CG  B ARG   C 1 103 ? 12.976  -6.312  53.627  0.50 32.95 ? 82  ARG   C CG  1 
ATOM   4392 C CD  A ARG   C 1 103 ? 14.440  -5.974  53.587  0.50 32.15 ? 82  ARG   C CD  1 
ATOM   4393 C CD  B ARG   C 1 103 ? 12.960  -7.788  54.008  0.50 36.14 ? 82  ARG   C CD  1 
ATOM   4394 N NE  A ARG   C 1 103 ? 15.057  -6.879  52.610  0.50 33.33 ? 82  ARG   C NE  1 
ATOM   4395 N NE  B ARG   C 1 103 ? 13.255  -8.680  52.880  0.50 42.84 ? 82  ARG   C NE  1 
ATOM   4396 C CZ  A ARG   C 1 103 ? 15.936  -7.831  52.892  0.50 33.49 ? 82  ARG   C CZ  1 
ATOM   4397 C CZ  B ARG   C 1 103 ? 12.516  -9.722  52.512  0.50 38.66 ? 82  ARG   C CZ  1 
ATOM   4398 N NH1 A ARG   C 1 103 ? 16.249  -8.744  51.987  0.50 29.66 ? 82  ARG   C NH1 1 
ATOM   4399 N NH1 B ARG   C 1 103 ? 12.867  -10.424 51.452  0.50 43.22 ? 82  ARG   C NH1 1 
ATOM   4400 N NH2 A ARG   C 1 103 ? 16.439  -7.913  54.108  0.50 36.57 ? 82  ARG   C NH2 1 
ATOM   4401 N NH2 B ARG   C 1 103 ? 11.444  -10.064 53.205  0.50 43.14 ? 82  ARG   C NH2 1 
ATOM   4402 N N   . ALA   C 1 104 ? 9.204   -4.375  55.397  1.00 25.81 ? 83  ALA   C N   1 
ATOM   4403 C CA  . ALA   C 1 104 ? 8.383   -3.557  56.281  1.00 26.53 ? 83  ALA   C CA  1 
ATOM   4404 C C   . ALA   C 1 104 ? 7.116   -4.299  56.711  1.00 28.08 ? 83  ALA   C C   1 
ATOM   4405 O O   . ALA   C 1 104 ? 6.740   -4.243  57.882  1.00 27.77 ? 83  ALA   C O   1 
ATOM   4406 C CB  . ALA   C 1 104 ? 8.096   -2.210  55.625  1.00 27.52 ? 83  ALA   C CB  1 
ATOM   4407 N N   . PHE   C 1 105 ? 6.423   -4.984  55.782  1.00 25.69 ? 84  PHE   C N   1 
ATOM   4408 C CA  . PHE   C 1 105 ? 5.036   -5.363  56.026  1.00 23.84 ? 84  PHE   C CA  1 
ATOM   4409 C C   . PHE   C 1 105 ? 4.840   -6.867  55.900  1.00 23.17 ? 84  PHE   C C   1 
ATOM   4410 O O   . PHE   C 1 105 ? 3.761   -7.355  56.217  1.00 26.24 ? 84  PHE   C O   1 
ATOM   4411 C CB  . PHE   C 1 105 ? 4.079   -4.669  55.052  1.00 25.40 ? 84  PHE   C CB  1 
ATOM   4412 C CG  . PHE   C 1 105 ? 4.190   -3.155  55.118  1.00 24.29 ? 84  PHE   C CG  1 
ATOM   4413 C CD1 . PHE   C 1 105 ? 4.142   -2.490  56.344  1.00 24.03 ? 84  PHE   C CD1 1 
ATOM   4414 C CD2 . PHE   C 1 105 ? 4.360   -2.401  53.958  1.00 22.28 ? 84  PHE   C CD2 1 
ATOM   4415 C CE1 . PHE   C 1 105 ? 4.271   -1.103  56.418  1.00 22.56 ? 84  PHE   C CE1 1 
ATOM   4416 C CE2 . PHE   C 1 105 ? 4.467   -1.012  54.034  1.00 22.21 ? 84  PHE   C CE2 1 
ATOM   4417 C CZ  . PHE   C 1 105 ? 4.437   -0.372  55.262  1.00 24.03 ? 84  PHE   C CZ  1 
ATOM   4418 N N   . GLY   C 1 106 ? 5.877   -7.580  55.440  1.00 23.54 ? 85  GLY   C N   1 
ATOM   4419 C CA  . GLY   C 1 106 ? 5.842   -9.038  55.317  1.00 25.01 ? 85  GLY   C CA  1 
ATOM   4420 C C   . GLY   C 1 106 ? 4.945   -9.562  54.178  1.00 29.09 ? 85  GLY   C C   1 
ATOM   4421 O O   . GLY   C 1 106 ? 4.734   -10.770 54.048  1.00 30.76 ? 85  GLY   C O   1 
ATOM   4422 N N   . ARG   C 1 107 ? 4.426   -8.670  53.329  1.00 27.08 ? 86  ARG   C N   1 
ATOM   4423 C CA  . ARG   C 1 107 ? 3.621   -9.087  52.183  1.00 28.16 ? 86  ARG   C CA  1 
ATOM   4424 C C   . ARG   C 1 107 ? 3.572   -7.920  51.189  1.00 24.57 ? 86  ARG   C C   1 
ATOM   4425 O O   . ARG   C 1 107 ? 3.984   -6.791  51.512  1.00 23.07 ? 86  ARG   C O   1 
ATOM   4426 C CB  . ARG   C 1 107 ? 2.185   -9.452  52.608  1.00 26.83 ? 86  ARG   C CB  1 
ATOM   4427 C CG  . ARG   C 1 107 ? 1.509   -8.257  53.273  1.00 28.48 ? 86  ARG   C CG  1 
ATOM   4428 C CD  . ARG   C 1 107 ? 0.211   -8.706  53.946  1.00 32.52 ? 86  ARG   C CD  1 
ATOM   4429 N NE  . ARG   C 1 107 ? -0.824  -9.078  52.971  1.00 28.69 ? 86  ARG   C NE  1 
ATOM   4430 C CZ  . ARG   C 1 107 ? -2.014  -9.616  53.244  1.00 32.14 ? 86  ARG   C CZ  1 
ATOM   4431 N NH1 . ARG   C 1 107 ? -2.314  -9.952  54.493  1.00 31.75 ? 86  ARG   C NH1 1 
ATOM   4432 N NH2 . ARG   C 1 107 ? -2.902  -9.804  52.281  1.00 29.12 ? 86  ARG   C NH2 1 
ATOM   4433 N N   . CYS   C 1 108 ? 3.075   -8.208  49.973  1.00 24.41 ? 87  CYS   C N   1 
ATOM   4434 C CA  . CYS   C 1 108 ? 2.936   -7.193  48.940  1.00 25.75 ? 87  CYS   C CA  1 
ATOM   4435 C C   . CYS   C 1 108 ? 1.774   -7.611  48.040  1.00 27.97 ? 87  CYS   C C   1 
ATOM   4436 O O   . CYS   C 1 108 ? 1.860   -8.632  47.345  1.00 29.40 ? 87  CYS   C O   1 
ATOM   4437 C CB  . CYS   C 1 108 ? 4.218   -7.052  48.105  1.00 25.74 ? 87  CYS   C CB  1 
ATOM   4438 S SG  . CYS   C 1 108 ? 4.100   -5.687  46.905  1.00 26.41 ? 87  CYS   C SG  1 
ATOM   4439 N N   . ASP   C 1 109 ? 0.662   -6.875  48.136  1.00 25.29 ? 88  ASP   C N   1 
ATOM   4440 C CA  . ASP   C 1 109 ? -0.577  -7.344  47.527  1.00 23.68 ? 88  ASP   C CA  1 
ATOM   4441 C C   . ASP   C 1 109 ? -0.862  -6.576  46.229  1.00 23.54 ? 88  ASP   C C   1 
ATOM   4442 O O   . ASP   C 1 109 ? -1.520  -7.109  45.339  1.00 23.92 ? 88  ASP   C O   1 
ATOM   4443 C CB  . ASP   C 1 109 ? -1.744  -7.149  48.485  1.00 22.80 ? 88  ASP   C CB  1 
ATOM   4444 C CG  . ASP   C 1 109 ? -1.562  -7.961  49.762  1.00 28.05 ? 88  ASP   C CG  1 
ATOM   4445 O OD1 . ASP   C 1 109 ? -1.892  -9.164  49.750  1.00 27.63 ? 88  ASP   C OD1 1 
ATOM   4446 O OD2 . ASP   C 1 109 ? -0.922  -7.427  50.691  1.00 29.77 ? 88  ASP   C OD2 1 
ATOM   4447 N N   . VAL   C 1 110 ? -0.431  -5.303  46.185  1.00 21.31 ? 89  VAL   C N   1 
ATOM   4448 C CA  . VAL   C 1 110 ? -0.752  -4.398  45.090  1.00 21.33 ? 89  VAL   C CA  1 
ATOM   4449 C C   . VAL   C 1 110 ? 0.515   -3.646  44.677  1.00 22.90 ? 89  VAL   C C   1 
ATOM   4450 O O   . VAL   C 1 110 ? 1.313   -3.252  45.542  1.00 22.26 ? 89  VAL   C O   1 
ATOM   4451 C CB  . VAL   C 1 110 ? -1.853  -3.426  45.539  1.00 22.50 ? 89  VAL   C CB  1 
ATOM   4452 C CG1 . VAL   C 1 110 ? -1.966  -2.193  44.634  1.00 20.04 ? 89  VAL   C CG1 1 
ATOM   4453 C CG2 . VAL   C 1 110 ? -3.195  -4.131  45.737  1.00 20.90 ? 89  VAL   C CG2 1 
ATOM   4454 N N   . LEU   C 1 111 ? 0.708   -3.512  43.348  1.00 19.19 ? 90  LEU   C N   1 
ATOM   4455 C CA  . LEU   C 1 111 ? 1.754   -2.677  42.768  1.00 20.59 ? 90  LEU   C CA  1 
ATOM   4456 C C   . LEU   C 1 111 ? 1.071   -1.611  41.909  1.00 20.87 ? 90  LEU   C C   1 
ATOM   4457 O O   . LEU   C 1 111 ? 0.273   -1.948  41.036  1.00 21.33 ? 90  LEU   C O   1 
ATOM   4458 C CB  . LEU   C 1 111 ? 2.715   -3.531  41.932  1.00 19.69 ? 90  LEU   C CB  1 
ATOM   4459 C CG  . LEU   C 1 111 ? 3.688   -2.764  41.020  1.00 19.55 ? 90  LEU   C CG  1 
ATOM   4460 C CD1 . LEU   C 1 111 ? 4.600   -1.886  41.868  1.00 17.94 ? 90  LEU   C CD1 1 
ATOM   4461 C CD2 . LEU   C 1 111 ? 4.453   -3.752  40.130  1.00 20.05 ? 90  LEU   C CD2 1 
ATOM   4462 N N   . VAL   C 1 112 ? 1.405   -0.339  42.130  1.00 18.38 ? 91  VAL   C N   1 
ATOM   4463 C CA  . VAL   C 1 112 ? 0.877   0.693   41.264  1.00 19.23 ? 91  VAL   C CA  1 
ATOM   4464 C C   . VAL   C 1 112 ? 2.061   1.325   40.520  1.00 22.35 ? 91  VAL   C C   1 
ATOM   4465 O O   . VAL   C 1 112 ? 2.917   1.964   41.142  1.00 22.52 ? 91  VAL   C O   1 
ATOM   4466 C CB  . VAL   C 1 112 ? 0.040   1.763   42.005  1.00 19.93 ? 91  VAL   C CB  1 
ATOM   4467 C CG1 . VAL   C 1 112 ? -0.436  2.837   41.010  1.00 20.18 ? 91  VAL   C CG1 1 
ATOM   4468 C CG2 . VAL   C 1 112 ? -1.188  1.182   42.730  1.00 19.26 ? 91  VAL   C CG2 1 
ATOM   4469 N N   . ASN   C 1 113 ? 2.125   1.134   39.180  1.00 19.26 ? 92  ASN   C N   1 
ATOM   4470 C CA  . ASN   C 1 113 ? 3.219   1.726   38.428  1.00 20.28 ? 92  ASN   C CA  1 
ATOM   4471 C C   . ASN   C 1 113 ? 2.792   3.116   37.960  1.00 21.04 ? 92  ASN   C C   1 
ATOM   4472 O O   . ASN   C 1 113 ? 2.110   3.258   36.933  1.00 20.96 ? 92  ASN   C O   1 
ATOM   4473 C CB  . ASN   C 1 113 ? 3.604   0.871   37.227  1.00 20.21 ? 92  ASN   C CB  1 
ATOM   4474 C CG  . ASN   C 1 113 ? 4.370   -0.356  37.639  1.00 21.66 ? 92  ASN   C CG  1 
ATOM   4475 O OD1 . ASN   C 1 113 ? 5.432   -0.222  38.267  1.00 19.25 ? 92  ASN   C OD1 1 
ATOM   4476 N ND2 . ASN   C 1 113 ? 3.859   -1.535  37.283  1.00 17.79 ? 92  ASN   C ND2 1 
ATOM   4477 N N   . ASN   C 1 114 ? 3.192   4.127   38.725  1.00 18.95 ? 93  ASN   C N   1 
ATOM   4478 C CA  . ASN   C 1 114 ? 2.741   5.504   38.522  1.00 19.26 ? 93  ASN   C CA  1 
ATOM   4479 C C   . ASN   C 1 114 ? 3.914   6.396   38.104  1.00 21.70 ? 93  ASN   C C   1 
ATOM   4480 O O   . ASN   C 1 114 ? 3.709   7.377   37.382  1.00 21.53 ? 93  ASN   C O   1 
ATOM   4481 C CB  . ASN   C 1 114 ? 2.050   6.005   39.787  1.00 19.30 ? 93  ASN   C CB  1 
ATOM   4482 C CG  . ASN   C 1 114 ? 1.859   7.511   39.798  1.00 22.73 ? 93  ASN   C CG  1 
ATOM   4483 O OD1 . ASN   C 1 114 ? 0.879   8.002   39.228  1.00 22.41 ? 93  ASN   C OD1 1 
ATOM   4484 N ND2 . ASN   C 1 114 ? 2.766   8.257   40.425  1.00 19.24 ? 93  ASN   C ND2 1 
ATOM   4485 N N   . ALA   C 1 115 ? 5.140   6.089   38.559  1.00 21.01 ? 94  ALA   C N   1 
ATOM   4486 C CA  . ALA   C 1 115 ? 6.278   6.977   38.299  1.00 24.53 ? 94  ALA   C CA  1 
ATOM   4487 C C   . ALA   C 1 115 ? 6.481   7.197   36.792  1.00 23.98 ? 94  ALA   C C   1 
ATOM   4488 O O   . ALA   C 1 115 ? 6.369   6.269   35.994  1.00 21.85 ? 94  ALA   C O   1 
ATOM   4489 C CB  . ALA   C 1 115 ? 7.557   6.469   38.964  1.00 21.54 ? 94  ALA   C CB  1 
ATOM   4490 N N   . SER   C 1 116 ? 6.788   8.435   36.393  1.00 22.58 ? 95  SER   C N   1 
ATOM   4491 C CA  . SER   C 1 116 ? 6.882   8.679   34.964  1.00 25.74 ? 95  SER   C CA  1 
ATOM   4492 C C   . SER   C 1 116 ? 7.767   9.890   34.676  1.00 28.85 ? 95  SER   C C   1 
ATOM   4493 O O   . SER   C 1 116 ? 7.565   10.940  35.279  1.00 27.74 ? 95  SER   C O   1 
ATOM   4494 C CB  . SER   C 1 116 ? 5.498   8.910   34.400  1.00 25.25 ? 95  SER   C CB  1 
ATOM   4495 O OG  . SER   C 1 116 ? 5.625   9.390   33.061  1.00 27.08 ? 95  SER   C OG  1 
ATOM   4496 N N   . ALA   C 1 117 ? 8.711   9.748   33.734  1.00 26.61 ? 96  ALA   C N   1 
ATOM   4497 C CA  . ALA   C 1 117 ? 9.373   10.911  33.170  1.00 26.22 ? 96  ALA   C CA  1 
ATOM   4498 C C   . ALA   C 1 117 ? 8.574   11.371  31.953  1.00 25.31 ? 96  ALA   C C   1 
ATOM   4499 O O   . ALA   C 1 117 ? 8.043   10.541  31.201  1.00 22.71 ? 96  ALA   C O   1 
ATOM   4500 C CB  . ALA   C 1 117 ? 10.796  10.565  32.750  1.00 25.66 ? 96  ALA   C CB  1 
ATOM   4501 N N   . PHE   C 1 118 ? 8.593   12.684  31.702  1.00 24.07 ? 97  PHE   C N   1 
ATOM   4502 C CA  . PHE   C 1 118 ? 7.817   13.251  30.612  1.00 25.20 ? 97  PHE   C CA  1 
ATOM   4503 C C   . PHE   C 1 118 ? 8.494   14.547  30.165  1.00 27.77 ? 97  PHE   C C   1 
ATOM   4504 O O   . PHE   C 1 118 ? 8.576   15.485  30.946  1.00 28.20 ? 97  PHE   C O   1 
ATOM   4505 C CB  . PHE   C 1 118 ? 6.406   13.566  31.149  1.00 26.22 ? 97  PHE   C CB  1 
ATOM   4506 C CG  . PHE   C 1 118 ? 5.487   14.300  30.178  1.00 33.68 ? 97  PHE   C CG  1 
ATOM   4507 C CD1 . PHE   C 1 118 ? 4.779   13.613  29.189  1.00 31.76 ? 97  PHE   C CD1 1 
ATOM   4508 C CD2 . PHE   C 1 118 ? 5.296   15.678  30.263  1.00 39.73 ? 97  PHE   C CD2 1 
ATOM   4509 C CE1 . PHE   C 1 118 ? 3.935   14.271  28.299  1.00 33.03 ? 97  PHE   C CE1 1 
ATOM   4510 C CE2 . PHE   C 1 118 ? 4.421   16.337  29.387  1.00 43.80 ? 97  PHE   C CE2 1 
ATOM   4511 C CZ  . PHE   C 1 118 ? 3.744   15.633  28.398  1.00 37.34 ? 97  PHE   C CZ  1 
ATOM   4512 N N   . TYR   C 1 119 ? 8.961   14.601  28.913  1.00 27.29 ? 98  TYR   C N   1 
ATOM   4513 C CA  . TYR   C 1 119 ? 9.534   15.813  28.344  1.00 25.80 ? 98  TYR   C CA  1 
ATOM   4514 C C   . TYR   C 1 119 ? 9.740   15.578  26.846  1.00 26.19 ? 98  TYR   C C   1 
ATOM   4515 O O   . TYR   C 1 119 ? 9.747   14.430  26.392  1.00 25.18 ? 98  TYR   C O   1 
ATOM   4516 C CB  . TYR   C 1 119 ? 10.826  16.185  29.101  1.00 27.51 ? 98  TYR   C CB  1 
ATOM   4517 C CG  . TYR   C 1 119 ? 11.909  15.112  29.182  1.00 25.29 ? 98  TYR   C CG  1 
ATOM   4518 C CD1 . TYR   C 1 119 ? 12.727  14.835  28.091  1.00 27.59 ? 98  TYR   C CD1 1 
ATOM   4519 C CD2 . TYR   C 1 119 ? 12.164  14.447  30.373  1.00 24.96 ? 98  TYR   C CD2 1 
ATOM   4520 C CE1 . TYR   C 1 119 ? 13.738  13.881  28.171  1.00 28.56 ? 98  TYR   C CE1 1 
ATOM   4521 C CE2 . TYR   C 1 119 ? 13.151  13.483  30.469  1.00 26.58 ? 98  TYR   C CE2 1 
ATOM   4522 C CZ  . TYR   C 1 119 ? 13.933  13.195  29.365  1.00 27.68 ? 98  TYR   C CZ  1 
ATOM   4523 O OH  . TYR   C 1 119 ? 14.936  12.277  29.479  1.00 26.75 ? 98  TYR   C OH  1 
ATOM   4524 N N   . PRO   C 1 120 ? 9.862   16.637  26.017  1.00 28.79 ? 99  PRO   C N   1 
ATOM   4525 C CA  . PRO   C 1 120 ? 9.938   16.446  24.567  1.00 28.50 ? 99  PRO   C CA  1 
ATOM   4526 C C   . PRO   C 1 120 ? 11.273  15.822  24.164  1.00 29.88 ? 99  PRO   C C   1 
ATOM   4527 O O   . PRO   C 1 120 ? 12.305  16.102  24.783  1.00 29.13 ? 99  PRO   C O   1 
ATOM   4528 C CB  . PRO   C 1 120 ? 9.741   17.849  23.954  1.00 29.88 ? 99  PRO   C CB  1 
ATOM   4529 C CG  . PRO   C 1 120 ? 9.620   18.800  25.135  1.00 32.27 ? 99  PRO   C CG  1 
ATOM   4530 C CD  . PRO   C 1 120 ? 9.853   18.060  26.433  1.00 28.14 ? 99  PRO   C CD  1 
ATOM   4531 N N   . THR   C 1 121 ? 11.231  14.942  23.149  1.00 23.22 ? 100 THR   C N   1 
ATOM   4532 C CA  . THR   C 1 121 ? 12.412  14.328  22.558  1.00 23.43 ? 100 THR   C CA  1 
ATOM   4533 C C   . THR   C 1 121 ? 12.269  14.437  21.049  1.00 25.41 ? 100 THR   C C   1 
ATOM   4534 O O   . THR   C 1 121 ? 11.906  13.453  20.403  1.00 25.82 ? 100 THR   C O   1 
ATOM   4535 C CB  . THR   C 1 121 ? 12.554  12.866  22.987  1.00 25.19 ? 100 THR   C CB  1 
ATOM   4536 O OG1 . THR   C 1 121 ? 11.374  12.155  22.603  1.00 26.07 ? 100 THR   C OG1 1 
ATOM   4537 C CG2 . THR   C 1 121 ? 12.778  12.730  24.484  1.00 23.40 ? 100 THR   C CG2 1 
ATOM   4538 N N   . PRO   C 1 122 ? 12.524  15.637  20.463  1.00 26.66 ? 101 PRO   C N   1 
ATOM   4539 C CA  . PRO   C 1 122 ? 12.307  15.874  19.036  1.00 26.84 ? 101 PRO   C CA  1 
ATOM   4540 C C   . PRO   C 1 122 ? 13.159  14.912  18.221  1.00 29.02 ? 101 PRO   C C   1 
ATOM   4541 O O   . PRO   C 1 122 ? 14.305  14.586  18.586  1.00 30.31 ? 101 PRO   C O   1 
ATOM   4542 C CB  . PRO   C 1 122 ? 12.644  17.378  18.760  1.00 27.47 ? 101 PRO   C CB  1 
ATOM   4543 C CG  . PRO   C 1 122 ? 12.829  18.002  20.139  1.00 30.74 ? 101 PRO   C CG  1 
ATOM   4544 C CD  . PRO   C 1 122 ? 12.964  16.864  21.178  1.00 31.99 ? 101 PRO   C CD  1 
ATOM   4545 N N   . LEU   C 1 123 ? 12.571  14.456  17.107  1.00 25.58 ? 102 LEU   C N   1 
ATOM   4546 C CA  . LEU   C 1 123 ? 13.262  13.580  16.187  1.00 25.90 ? 102 LEU   C CA  1 
ATOM   4547 C C   . LEU   C 1 123 ? 14.340  14.359  15.440  1.00 34.37 ? 102 LEU   C C   1 
ATOM   4548 O O   . LEU   C 1 123 ? 15.335  13.764  15.034  1.00 34.79 ? 102 LEU   C O   1 
ATOM   4549 C CB  . LEU   C 1 123 ? 12.253  12.947  15.225  1.00 25.31 ? 102 LEU   C CB  1 
ATOM   4550 C CG  . LEU   C 1 123 ? 11.346  11.888  15.853  1.00 21.15 ? 102 LEU   C CG  1 
ATOM   4551 C CD1 . LEU   C 1 123 ? 10.265  11.526  14.841  1.00 21.35 ? 102 LEU   C CD1 1 
ATOM   4552 C CD2 . LEU   C 1 123 ? 12.181  10.651  16.230  1.00 23.07 ? 102 LEU   C CD2 1 
ATOM   4553 N N   . VAL   C 1 124 ? 14.093  15.660  15.243  1.00 37.37 ? 103 VAL   C N   1 
ATOM   4554 C CA  . VAL   C 1 124 ? 15.020  16.587  14.605  1.00 48.14 ? 103 VAL   C CA  1 
ATOM   4555 C C   . VAL   C 1 124 ? 15.418  17.646  15.638  1.00 55.97 ? 103 VAL   C C   1 
ATOM   4556 O O   . VAL   C 1 124 ? 14.717  18.646  15.813  1.00 63.04 ? 103 VAL   C O   1 
ATOM   4557 C CB  . VAL   C 1 124 ? 14.427  17.202  13.318  1.00 50.67 ? 103 VAL   C CB  1 
ATOM   4558 C CG1 . VAL   C 1 124 ? 15.368  18.203  12.659  1.00 60.90 ? 103 VAL   C CG1 1 
ATOM   4559 C CG2 . VAL   C 1 124 ? 14.046  16.137  12.294  1.00 53.03 ? 103 VAL   C CG2 1 
ATOM   4560 N N   . GLN   C 1 125 ? 16.523  17.371  16.346  0.70 50.19 ? 104 GLN   C N   1 
ATOM   4561 C CA  . GLN   C 1 125 ? 17.137  18.254  17.327  0.70 55.84 ? 104 GLN   C CA  1 
ATOM   4562 C C   . GLN   C 1 125 ? 18.407  17.569  17.853  0.70 56.21 ? 104 GLN   C C   1 
ATOM   4563 O O   . GLN   C 1 125 ? 19.465  17.785  17.220  0.70 54.09 ? 104 GLN   C O   1 
ATOM   4564 C CB  . GLN   C 1 125 ? 16.241  18.569  18.529  0.70 56.29 ? 104 GLN   C CB  1 
ATOM   4565 N N   . LYS   C 1 135 ? 20.376  16.958  27.734  1.00 45.91 ? 114 LYS   C N   1 
ATOM   4566 C CA  . LYS   C 1 135 ? 20.479  15.492  27.986  1.00 37.56 ? 114 LYS   C CA  1 
ATOM   4567 C C   . LYS   C 1 135 ? 20.819  14.824  26.663  1.00 35.05 ? 114 LYS   C C   1 
ATOM   4568 O O   . LYS   C 1 135 ? 20.289  15.207  25.629  1.00 35.88 ? 114 LYS   C O   1 
ATOM   4569 C CB  . LYS   C 1 135 ? 19.153  14.886  28.464  1.00 36.81 ? 114 LYS   C CB  1 
ATOM   4570 C CG  . LYS   C 1 135 ? 18.659  15.251  29.855  1.00 39.18 ? 114 LYS   C CG  1 
ATOM   4571 C CD  . LYS   C 1 135 ? 17.160  14.997  29.974  1.00 44.77 ? 114 LYS   C CD  1 
ATOM   4572 C CE  . LYS   C 1 135 ? 16.594  15.301  31.328  1.00 45.63 ? 114 LYS   C CE  1 
ATOM   4573 N NZ  . LYS   C 1 135 ? 17.454  14.632  32.307  1.00 49.35 ? 114 LYS   C NZ  1 
ATOM   4574 N N   . THR   C 1 136 ? 21.703  13.827  26.692  1.00 34.43 ? 115 THR   C N   1 
ATOM   4575 C CA  . THR   C 1 136 ? 22.063  13.132  25.474  1.00 31.14 ? 115 THR   C CA  1 
ATOM   4576 C C   . THR   C 1 136 ? 20.873  12.260  25.062  1.00 31.48 ? 115 THR   C C   1 
ATOM   4577 O O   . THR   C 1 136 ? 19.965  11.998  25.855  1.00 26.52 ? 115 THR   C O   1 
ATOM   4578 C CB  . THR   C 1 136 ? 23.307  12.295  25.740  1.00 34.31 ? 115 THR   C CB  1 
ATOM   4579 O OG1 . THR   C 1 136 ? 22.886  11.327  26.700  1.00 32.08 ? 115 THR   C OG1 1 
ATOM   4580 C CG2 . THR   C 1 136 ? 24.485  13.142  26.203  1.00 38.82 ? 115 THR   C CG2 1 
ATOM   4581 N N   . VAL   C 1 137 ? 20.885  11.817  23.802  1.00 27.83 ? 116 VAL   C N   1 
ATOM   4582 C CA  . VAL   C 1 137 ? 19.791  11.005  23.315  1.00 27.00 ? 116 VAL   C CA  1 
ATOM   4583 C C   . VAL   C 1 137 ? 19.723  9.719   24.131  1.00 25.99 ? 116 VAL   C C   1 
ATOM   4584 O O   . VAL   C 1 137 ? 18.636  9.216   24.414  1.00 24.45 ? 116 VAL   C O   1 
ATOM   4585 C CB  . VAL   C 1 137 ? 19.811  10.751  21.798  1.00 31.48 ? 116 VAL   C CB  1 
ATOM   4586 C CG1 . VAL   C 1 137 ? 18.564  9.981   21.382  1.00 33.55 ? 116 VAL   C CG1 1 
ATOM   4587 C CG2 . VAL   C 1 137 ? 19.809  12.101  21.089  1.00 36.03 ? 116 VAL   C CG2 1 
ATOM   4588 N N   . GLU   C 1 138 ? 20.885  9.185   24.522  1.00 28.20 ? 117 GLU   C N   1 
ATOM   4589 C CA  . GLU   C 1 138 ? 20.862  7.925   25.265  1.00 30.83 ? 117 GLU   C CA  1 
ATOM   4590 C C   . GLU   C 1 138 ? 20.255  8.112   26.661  1.00 27.65 ? 117 GLU   C C   1 
ATOM   4591 O O   . GLU   C 1 138 ? 19.597  7.199   27.180  1.00 29.78 ? 117 GLU   C O   1 
ATOM   4592 C CB  . GLU   C 1 138 ? 22.138  7.081   25.151  1.00 39.25 ? 117 GLU   C CB  1 
ATOM   4593 C CG  . GLU   C 1 138 ? 23.392  7.793   25.640  1.00 38.02 ? 117 GLU   C CG  1 
ATOM   4594 C CD  . GLU   C 1 138 ? 24.118  8.722   24.678  1.00 42.77 ? 117 GLU   C CD  1 
ATOM   4595 O OE1 . GLU   C 1 138 ? 23.647  9.037   23.561  1.00 31.28 ? 117 GLU   C OE1 1 
ATOM   4596 O OE2 . GLU   C 1 138 ? 25.234  9.119   25.093  1.00 47.41 ? 117 GLU   C OE2 1 
ATOM   4597 N N   . THR   C 1 139 ? 20.447  9.299   27.247  1.00 23.77 ? 118 THR   C N   1 
ATOM   4598 C CA  . THR   C 1 139 ? 19.804  9.635   28.512  1.00 25.33 ? 118 THR   C CA  1 
ATOM   4599 C C   . THR   C 1 139 ? 18.289  9.772   28.329  1.00 24.89 ? 118 THR   C C   1 
ATOM   4600 O O   . THR   C 1 139 ? 17.492  9.344   29.186  1.00 23.48 ? 118 THR   C O   1 
ATOM   4601 C CB  . THR   C 1 139 ? 20.425  10.896  29.124  1.00 28.64 ? 118 THR   C CB  1 
ATOM   4602 O OG1 . THR   C 1 139 ? 21.745  10.540  29.506  1.00 33.23 ? 118 THR   C OG1 1 
ATOM   4603 C CG2 . THR   C 1 139 ? 19.729  11.377  30.383  1.00 30.63 ? 118 THR   C CG2 1 
ATOM   4604 N N   . GLN   C 1 140 ? 17.896  10.441  27.239  1.00 25.85 ? 119 GLN   C N   1 
ATOM   4605 C CA  . GLN   C 1 140 ? 16.474  10.589  26.948  1.00 23.64 ? 119 GLN   C CA  1 
ATOM   4606 C C   . GLN   C 1 140 ? 15.819  9.201   26.872  1.00 23.07 ? 119 GLN   C C   1 
ATOM   4607 O O   . GLN   C 1 140 ? 14.768  8.950   27.477  1.00 22.48 ? 119 GLN   C O   1 
ATOM   4608 C CB  . GLN   C 1 140 ? 16.321  11.383  25.657  1.00 24.73 ? 119 GLN   C CB  1 
ATOM   4609 C CG  . GLN   C 1 140 ? 16.771  12.852  25.737  1.00 27.38 ? 119 GLN   C CG  1 
ATOM   4610 C CD  . GLN   C 1 140 ? 16.876  13.475  24.353  1.00 31.24 ? 119 GLN   C CD  1 
ATOM   4611 O OE1 . GLN   C 1 140 ? 16.008  13.267  23.492  1.00 35.09 ? 119 GLN   C OE1 1 
ATOM   4612 N NE2 . GLN   C 1 140 ? 17.981  14.160  24.056  1.00 32.26 ? 119 GLN   C NE2 1 
ATOM   4613 N N   . VAL   C 1 141 ? 16.445  8.292   26.117  1.00 19.62 ? 120 VAL   C N   1 
ATOM   4614 C CA  . VAL   C 1 141 ? 15.931  6.931   26.015  1.00 22.06 ? 120 VAL   C CA  1 
ATOM   4615 C C   . VAL   C 1 141 ? 15.842  6.293   27.412  1.00 24.92 ? 120 VAL   C C   1 
ATOM   4616 O O   . VAL   C 1 141 ? 14.825  5.697   27.779  1.00 22.96 ? 120 VAL   C O   1 
ATOM   4617 C CB  . VAL   C 1 141 ? 16.822  6.088   25.083  1.00 21.38 ? 120 VAL   C CB  1 
ATOM   4618 C CG1 . VAL   C 1 141 ? 16.444  4.598   25.151  1.00 20.86 ? 120 VAL   C CG1 1 
ATOM   4619 C CG2 . VAL   C 1 141 ? 16.743  6.614   23.643  1.00 20.20 ? 120 VAL   C CG2 1 
ATOM   4620 N N   . ALA   C 1 142 ? 16.958  6.313   28.147  1.00 23.71 ? 121 ALA   C N   1 
ATOM   4621 C CA  . ALA   C 1 142 ? 17.010  5.596   29.420  1.00 21.56 ? 121 ALA   C CA  1 
ATOM   4622 C C   . ALA   C 1 142 ? 15.931  6.107   30.372  1.00 20.85 ? 121 ALA   C C   1 
ATOM   4623 O O   . ALA   C 1 142 ? 15.270  5.315   31.051  1.00 24.42 ? 121 ALA   C O   1 
ATOM   4624 C CB  . ALA   C 1 142 ? 18.401  5.696   30.037  1.00 23.40 ? 121 ALA   C CB  1 
ATOM   4625 N N   . GLU   C 1 143 ? 15.775  7.429   30.452  1.00 21.38 ? 122 GLU   C N   1 
ATOM   4626 C CA  . GLU   C 1 143 ? 14.810  7.999   31.386  1.00 23.09 ? 122 GLU   C CA  1 
ATOM   4627 C C   . GLU   C 1 143 ? 13.377  7.692   30.953  1.00 24.42 ? 122 GLU   C C   1 
ATOM   4628 O O   . GLU   C 1 143 ? 12.562  7.239   31.758  1.00 22.55 ? 122 GLU   C O   1 
ATOM   4629 C CB  . GLU   C 1 143 ? 14.961  9.517   31.479  1.00 24.95 ? 122 GLU   C CB  1 
ATOM   4630 C CG  . GLU   C 1 143 ? 16.174  9.889   32.316  1.00 30.42 ? 122 GLU   C CG  1 
ATOM   4631 C CD  . GLU   C 1 143 ? 16.499  11.350  32.529  1.00 32.11 ? 122 GLU   C CD  1 
ATOM   4632 O OE1 . GLU   C 1 143 ? 15.788  12.193  31.961  1.00 29.30 ? 122 GLU   C OE1 1 
ATOM   4633 O OE2 . GLU   C 1 143 ? 17.492  11.624  33.263  1.00 36.23 ? 122 GLU   C OE2 1 
ATOM   4634 N N   . LEU   C 1 144 ? 13.062  8.004   29.691  1.00 22.51 ? 123 LEU   C N   1 
ATOM   4635 C CA  . LEU   C 1 144 ? 11.672  7.931   29.260  1.00 24.24 ? 123 LEU   C CA  1 
ATOM   4636 C C   . LEU   C 1 144 ? 11.199  6.488   29.123  1.00 22.63 ? 123 LEU   C C   1 
ATOM   4637 O O   . LEU   C 1 144 ? 10.084  6.188   29.552  1.00 23.26 ? 123 LEU   C O   1 
ATOM   4638 C CB  . LEU   C 1 144 ? 11.452  8.778   28.013  1.00 24.22 ? 123 LEU   C CB  1 
ATOM   4639 C CG  . LEU   C 1 144 ? 11.460  10.286  28.318  1.00 27.07 ? 123 LEU   C CG  1 
ATOM   4640 C CD1 . LEU   C 1 144 ? 11.698  11.122  27.113  1.00 28.49 ? 123 LEU   C CD1 1 
ATOM   4641 C CD2 . LEU   C 1 144 ? 10.114  10.662  28.892  1.00 27.45 ? 123 LEU   C CD2 1 
ATOM   4642 N N   . ILE   C 1 145 ? 12.030  5.596   28.543  1.00 23.40 ? 124 ILE   C N   1 
ATOM   4643 C CA  . ILE   C 1 145 ? 11.646  4.188   28.374  1.00 20.57 ? 124 ILE   C CA  1 
ATOM   4644 C C   . ILE   C 1 145 ? 11.816  3.419   29.693  1.00 22.79 ? 124 ILE   C C   1 
ATOM   4645 O O   . ILE   C 1 145 ? 11.023  2.532   30.049  1.00 22.64 ? 124 ILE   C O   1 
ATOM   4646 C CB  . ILE   C 1 145 ? 12.396  3.515   27.207  1.00 21.15 ? 124 ILE   C CB  1 
ATOM   4647 C CG1 . ILE   C 1 145 ? 12.298  4.333   25.900  1.00 22.69 ? 124 ILE   C CG1 1 
ATOM   4648 C CG2 . ILE   C 1 145 ? 11.918  2.068   27.011  1.00 19.23 ? 124 ILE   C CG2 1 
ATOM   4649 C CD1 . ILE   C 1 145 ? 10.860  4.530   25.405  1.00 24.55 ? 124 ILE   C CD1 1 
ATOM   4650 N N   . GLY   C 1 146 ? 12.856  3.766   30.454  1.00 21.84 ? 125 GLY   C N   1 
ATOM   4651 C CA  . GLY   C 1 146 ? 13.019  3.119   31.754  1.00 21.89 ? 125 GLY   C CA  1 
ATOM   4652 C C   . GLY   C 1 146 ? 11.838  3.354   32.698  1.00 21.37 ? 125 GLY   C C   1 
ATOM   4653 O O   . GLY   C 1 146 ? 11.288  2.397   33.237  1.00 22.58 ? 125 GLY   C O   1 
ATOM   4654 N N   . THR   C 1 147 ? 11.463  4.633   32.924  1.00 20.05 ? 126 THR   C N   1 
ATOM   4655 C CA  . THR   C 1 147 ? 10.438  4.941   33.920  1.00 22.04 ? 126 THR   C CA  1 
ATOM   4656 C C   . THR   C 1 147 ? 9.061   4.449   33.481  1.00 22.10 ? 126 THR   C C   1 
ATOM   4657 O O   . THR   C 1 147 ? 8.333   3.870   34.285  1.00 22.38 ? 126 THR   C O   1 
ATOM   4658 C CB  . THR   C 1 147 ? 10.414  6.432   34.290  1.00 24.81 ? 126 THR   C CB  1 
ATOM   4659 O OG1 . THR   C 1 147 ? 10.020  7.128   33.109  1.00 27.62 ? 126 THR   C OG1 1 
ATOM   4660 C CG2 . THR   C 1 147 ? 11.772  6.932   34.774  1.00 23.17 ? 126 THR   C CG2 1 
ATOM   4661 N N   . ASN   C 1 148 ? 8.739   4.642   32.191  1.00 21.54 ? 127 ASN   C N   1 
ATOM   4662 C CA  . ASN   C 1 148 ? 7.381   4.447   31.691  1.00 20.93 ? 127 ASN   C CA  1 
ATOM   4663 C C   . ASN   C 1 148 ? 7.136   2.974   31.357  1.00 20.94 ? 127 ASN   C C   1 
ATOM   4664 O O   . ASN   C 1 148 ? 5.988   2.539   31.344  1.00 21.75 ? 127 ASN   C O   1 
ATOM   4665 C CB  . ASN   C 1 148 ? 7.127   5.373   30.512  1.00 20.71 ? 127 ASN   C CB  1 
ATOM   4666 C CG  . ASN   C 1 148 ? 6.925   6.800   30.995  1.00 25.25 ? 127 ASN   C CG  1 
ATOM   4667 O OD1 . ASN   C 1 148 ? 5.973   7.071   31.735  1.00 25.82 ? 127 ASN   C OD1 1 
ATOM   4668 N ND2 . ASN   C 1 148 ? 7.754   7.738   30.567  1.00 21.63 ? 127 ASN   C ND2 1 
ATOM   4669 N N   . ALA   C 1 149 ? 8.201   2.193   31.110  1.00 20.91 ? 128 ALA   C N   1 
ATOM   4670 C CA  . ALA   C 1 149 ? 7.965   0.821   30.670  1.00 18.11 ? 128 ALA   C CA  1 
ATOM   4671 C C   . ALA   C 1 149 ? 8.876   -0.241  31.292  1.00 19.92 ? 128 ALA   C C   1 
ATOM   4672 O O   . ALA   C 1 149 ? 8.410   -1.295  31.727  1.00 19.06 ? 128 ALA   C O   1 
ATOM   4673 C CB  . ALA   C 1 149 ? 8.094   0.791   29.141  1.00 19.67 ? 128 ALA   C CB  1 
ATOM   4674 N N   . ILE   C 1 150 ? 10.198  -0.043  31.209  1.00 21.19 ? 129 ILE   C N   1 
ATOM   4675 C CA  . ILE   C 1 150 ? 11.096  -1.113  31.646  1.00 19.25 ? 129 ILE   C CA  1 
ATOM   4676 C C   . ILE   C 1 150 ? 11.004  -1.273  33.170  1.00 19.90 ? 129 ILE   C C   1 
ATOM   4677 O O   . ILE   C 1 150 ? 10.937  -2.397  33.659  1.00 18.99 ? 129 ILE   C O   1 
ATOM   4678 C CB  . ILE   C 1 150 ? 12.546  -0.826  31.185  1.00 20.14 ? 129 ILE   C CB  1 
ATOM   4679 C CG1 . ILE   C 1 150 ? 12.631  -0.802  29.649  1.00 21.28 ? 129 ILE   C CG1 1 
ATOM   4680 C CG2 . ILE   C 1 150 ? 13.501  -1.882  31.779  1.00 22.33 ? 129 ILE   C CG2 1 
ATOM   4681 C CD1 . ILE   C 1 150 ? 13.914  -0.191  29.100  1.00 24.19 ? 129 ILE   C CD1 1 
ATOM   4682 N N   . ALA   C 1 151 ? 10.997  -0.157  33.916  1.00 17.80 ? 130 ALA   C N   1 
ATOM   4683 C CA  . ALA   C 1 151 ? 10.820  -0.269  35.366  1.00 21.03 ? 130 ALA   C CA  1 
ATOM   4684 C C   . ALA   C 1 151 ? 9.510   -0.979  35.699  1.00 18.78 ? 130 ALA   C C   1 
ATOM   4685 O O   . ALA   C 1 151 ? 9.487   -1.911  36.507  1.00 19.38 ? 130 ALA   C O   1 
ATOM   4686 C CB  . ALA   C 1 151 ? 11.002  1.060   36.097  1.00 19.37 ? 130 ALA   C CB  1 
ATOM   4687 N N   . PRO   C 1 152 ? 8.360   -0.596  35.092  1.00 19.54 ? 131 PRO   C N   1 
ATOM   4688 C CA  . PRO   C 1 152 ? 7.134   -1.360  35.294  1.00 19.06 ? 131 PRO   C CA  1 
ATOM   4689 C C   . PRO   C 1 152 ? 7.218   -2.855  35.005  1.00 19.50 ? 131 PRO   C C   1 
ATOM   4690 O O   . PRO   C 1 152 ? 6.680   -3.626  35.784  1.00 20.91 ? 131 PRO   C O   1 
ATOM   4691 C CB  . PRO   C 1 152 ? 6.160   -0.629  34.347  1.00 19.10 ? 131 PRO   C CB  1 
ATOM   4692 C CG  . PRO   C 1 152 ? 6.577   0.837   34.518  1.00 19.48 ? 131 PRO   C CG  1 
ATOM   4693 C CD  . PRO   C 1 152 ? 8.098   0.712   34.452  1.00 18.08 ? 131 PRO   C CD  1 
ATOM   4694 N N   . PHE   C 1 153 ? 7.937   -3.251  33.936  1.00 18.70 ? 132 PHE   C N   1 
ATOM   4695 C CA  . PHE   C 1 153 ? 8.125   -4.681  33.643  1.00 18.16 ? 132 PHE   C CA  1 
ATOM   4696 C C   . PHE   C 1 153 ? 8.941   -5.355  34.765  1.00 19.95 ? 132 PHE   C C   1 
ATOM   4697 O O   . PHE   C 1 153 ? 8.562   -6.423  35.264  1.00 20.70 ? 132 PHE   C O   1 
ATOM   4698 C CB  . PHE   C 1 153 ? 8.801   -4.784  32.267  1.00 19.11 ? 132 PHE   C CB  1 
ATOM   4699 C CG  . PHE   C 1 153 ? 9.447   -6.139  32.029  1.00 19.31 ? 132 PHE   C CG  1 
ATOM   4700 C CD1 . PHE   C 1 153 ? 8.666   -7.219  31.611  1.00 20.50 ? 132 PHE   C CD1 1 
ATOM   4701 C CD2 . PHE   C 1 153 ? 10.805  -6.337  32.290  1.00 21.22 ? 132 PHE   C CD2 1 
ATOM   4702 C CE1 . PHE   C 1 153 ? 9.243   -8.473  31.419  1.00 20.82 ? 132 PHE   C CE1 1 
ATOM   4703 C CE2 . PHE   C 1 153 ? 11.387  -7.587  32.074  1.00 22.24 ? 132 PHE   C CE2 1 
ATOM   4704 C CZ  . PHE   C 1 153 ? 10.603  -8.655  31.674  1.00 23.52 ? 132 PHE   C CZ  1 
ATOM   4705 N N   . LEU   C 1 154 ? 10.058  -4.746  35.174  1.00 19.55 ? 133 LEU   C N   1 
ATOM   4706 C CA  . LEU   C 1 154 ? 10.953  -5.366  36.161  1.00 19.84 ? 133 LEU   C CA  1 
ATOM   4707 C C   . LEU   C 1 154 ? 10.266  -5.455  37.524  1.00 21.45 ? 133 LEU   C C   1 
ATOM   4708 O O   . LEU   C 1 154 ? 10.355  -6.483  38.207  1.00 21.27 ? 133 LEU   C O   1 
ATOM   4709 C CB  . LEU   C 1 154 ? 12.232  -4.528  36.286  1.00 18.91 ? 133 LEU   C CB  1 
ATOM   4710 C CG  . LEU   C 1 154 ? 13.109  -4.489  35.022  1.00 21.10 ? 133 LEU   C CG  1 
ATOM   4711 C CD1 . LEU   C 1 154 ? 14.162  -3.368  35.140  1.00 21.43 ? 133 LEU   C CD1 1 
ATOM   4712 C CD2 . LEU   C 1 154 ? 13.785  -5.822  34.750  1.00 24.13 ? 133 LEU   C CD2 1 
ATOM   4713 N N   . LEU   C 1 155 ? 9.565   -4.377  37.907  1.00 20.44 ? 134 LEU   C N   1 
ATOM   4714 C CA  . LEU   C 1 155 ? 8.746   -4.401  39.121  1.00 21.05 ? 134 LEU   C CA  1 
ATOM   4715 C C   . LEU   C 1 155 ? 7.704   -5.521  39.079  1.00 23.18 ? 134 LEU   C C   1 
ATOM   4716 O O   . LEU   C 1 155 ? 7.432   -6.194  40.103  1.00 22.95 ? 134 LEU   C O   1 
ATOM   4717 C CB  . LEU   C 1 155 ? 8.100   -3.031  39.365  1.00 18.66 ? 134 LEU   C CB  1 
ATOM   4718 C CG  . LEU   C 1 155 ? 9.055   -1.899  39.753  1.00 19.24 ? 134 LEU   C CG  1 
ATOM   4719 C CD1 . LEU   C 1 155 ? 8.519   -0.472  39.495  1.00 19.30 ? 134 LEU   C CD1 1 
ATOM   4720 C CD2 . LEU   C 1 155 ? 9.518   -1.987  41.250  1.00 19.19 ? 134 LEU   C CD2 1 
ATOM   4721 N N   . THR   C 1 156 ? 7.071   -5.685  37.895  1.00 21.23 ? 135 THR   C N   1 
ATOM   4722 C CA  . THR   C 1 156 ? 6.022   -6.683  37.694  1.00 18.48 ? 135 THR   C CA  1 
ATOM   4723 C C   . THR   C 1 156 ? 6.654   -8.061  37.896  1.00 18.71 ? 135 THR   C C   1 
ATOM   4724 O O   . THR   C 1 156 ? 6.066   -8.931  38.544  1.00 21.04 ? 135 THR   C O   1 
ATOM   4725 C CB  . THR   C 1 156 ? 5.408   -6.545  36.280  1.00 21.22 ? 135 THR   C CB  1 
ATOM   4726 O OG1 . THR   C 1 156 ? 4.759   -5.268  36.208  1.00 20.01 ? 135 THR   C OG1 1 
ATOM   4727 C CG2 . THR   C 1 156 ? 4.349   -7.601  36.001  1.00 19.28 ? 135 THR   C CG2 1 
ATOM   4728 N N   . MET   C 1 157 ? 7.831   -8.277  37.330  1.00 18.71 ? 136 MET   C N   1 
ATOM   4729 C CA  . MET   C 1 157 ? 8.539   -9.574  37.484  1.00 21.82 ? 136 MET   C CA  1 
ATOM   4730 C C   . MET   C 1 157 ? 8.854   -9.814  38.976  1.00 23.53 ? 136 MET   C C   1 
ATOM   4731 O O   . MET   C 1 157 ? 8.553   -10.896 39.477  1.00 22.63 ? 136 MET   C O   1 
ATOM   4732 C CB  . MET   C 1 157 ? 9.834   -9.528  36.667  1.00 24.15 ? 136 MET   C CB  1 
ATOM   4733 C CG  . MET   C 1 157 ? 10.675  -10.766 36.646  1.00 36.45 ? 136 MET   C CG  1 
ATOM   4734 S SD  . MET   C 1 157 ? 11.897  -10.504 35.345  1.00 41.88 ? 136 MET   C SD  1 
ATOM   4735 C CE  . MET   C 1 157 ? 12.145  -12.214 34.857  1.00 39.12 ? 136 MET   C CE  1 
ATOM   4736 N N   . SER   C 1 158 ? 9.432   -8.814  39.642  1.00 22.13 ? 137 SER   C N   1 
ATOM   4737 C CA  . SER   C 1 158 ? 9.802   -8.950  41.067  1.00 23.72 ? 137 SER   C CA  1 
ATOM   4738 C C   . SER   C 1 158 ? 8.571   -9.200  41.942  1.00 25.57 ? 137 SER   C C   1 
ATOM   4739 O O   . SER   C 1 158 ? 8.566   -10.085 42.792  1.00 26.53 ? 137 SER   C O   1 
ATOM   4740 C CB  . SER   C 1 158 ? 10.537  -7.732  41.564  1.00 23.38 ? 137 SER   C CB  1 
ATOM   4741 O OG  . SER   C 1 158 ? 11.826  -7.691  40.959  1.00 31.27 ? 137 SER   C OG  1 
ATOM   4742 N N   . PHE   C 1 159 ? 7.497   -8.433  41.697  1.00 24.40 ? 138 PHE   C N   1 
ATOM   4743 C CA  . PHE   C 1 159 ? 6.214   -8.654  42.360  1.00 23.93 ? 138 PHE   C CA  1 
ATOM   4744 C C   . PHE   C 1 159 ? 5.695   -10.079 42.163  1.00 24.53 ? 138 PHE   C C   1 
ATOM   4745 O O   . PHE   C 1 159 ? 5.324   -10.762 43.125  1.00 26.42 ? 138 PHE   C O   1 
ATOM   4746 C CB  . PHE   C 1 159 ? 5.182   -7.661  41.823  1.00 22.45 ? 138 PHE   C CB  1 
ATOM   4747 C CG  . PHE   C 1 159 ? 3.793   -7.801  42.447  1.00 23.40 ? 138 PHE   C CG  1 
ATOM   4748 C CD1 . PHE   C 1 159 ? 2.826   -8.627  41.865  1.00 24.38 ? 138 PHE   C CD1 1 
ATOM   4749 C CD2 . PHE   C 1 159 ? 3.431   -7.033  43.542  1.00 23.27 ? 138 PHE   C CD2 1 
ATOM   4750 C CE1 . PHE   C 1 159 ? 1.546   -8.729  42.416  1.00 27.05 ? 138 PHE   C CE1 1 
ATOM   4751 C CE2 . PHE   C 1 159 ? 2.149   -7.132  44.097  1.00 21.42 ? 138 PHE   C CE2 1 
ATOM   4752 C CZ  . PHE   C 1 159 ? 1.203   -7.959  43.526  1.00 22.91 ? 138 PHE   C CZ  1 
ATOM   4753 N N   . ALA   C 1 160 ? 5.659   -10.539 40.914  1.00 24.42 ? 139 ALA   C N   1 
ATOM   4754 C CA  . ALA   C 1 160 ? 5.080   -11.831 40.606  1.00 23.96 ? 139 ALA   C CA  1 
ATOM   4755 C C   . ALA   C 1 160 ? 5.916   -12.956 41.225  1.00 29.52 ? 139 ALA   C C   1 
ATOM   4756 O O   . ALA   C 1 160 ? 5.342   -13.912 41.749  1.00 33.12 ? 139 ALA   C O   1 
ATOM   4757 C CB  . ALA   C 1 160 ? 4.922   -11.996 39.092  1.00 26.56 ? 139 ALA   C CB  1 
ATOM   4758 N N   . GLN   C 1 161 ? 7.251   -12.838 41.160  1.00 26.79 ? 140 GLN   C N   1 
ATOM   4759 C CA  . GLN   C 1 161 ? 8.161   -13.905 41.588  1.00 30.04 ? 140 GLN   C CA  1 
ATOM   4760 C C   . GLN   C 1 161 ? 7.996   -14.139 43.092  1.00 34.60 ? 140 GLN   C C   1 
ATOM   4761 O O   . GLN   C 1 161 ? 8.111   -15.270 43.551  1.00 34.61 ? 140 GLN   C O   1 
ATOM   4762 C CB  . GLN   C 1 161 ? 9.613   -13.472 41.370  1.00 30.22 ? 140 GLN   C CB  1 
ATOM   4763 C CG  . GLN   C 1 161 ? 10.596  -14.592 41.046  0.70 41.90 ? 140 GLN   C CG  1 
ATOM   4764 C CD  . GLN   C 1 161 ? 10.468  -15.079 39.621  0.70 47.49 ? 140 GLN   C CD  1 
ATOM   4765 O OE1 . GLN   C 1 161 ? 10.099  -16.231 39.373  0.70 50.81 ? 140 GLN   C OE1 1 
ATOM   4766 N NE2 . GLN   C 1 161 ? 10.745  -14.198 38.667  0.70 51.66 ? 140 GLN   C NE2 1 
ATOM   4767 N N   . ARG   C 1 162 ? 7.701   -13.061 43.840  1.00 33.54 ? 141 ARG   C N   1 
ATOM   4768 C CA  . ARG   C 1 162 ? 7.622   -13.089 45.298  1.00 39.07 ? 141 ARG   C CA  1 
ATOM   4769 C C   . ARG   C 1 162 ? 6.293   -13.675 45.762  1.00 44.74 ? 141 ARG   C C   1 
ATOM   4770 O O   . ARG   C 1 162 ? 6.090   -13.828 46.966  1.00 45.48 ? 141 ARG   C O   1 
ATOM   4771 C CB  . ARG   C 1 162 ? 7.835   -11.737 45.992  1.00 34.01 ? 141 ARG   C CB  1 
ATOM   4772 C CG  . ARG   C 1 162 ? 9.186   -11.066 45.804  0.70 38.18 ? 141 ARG   C CG  1 
ATOM   4773 C CD  . ARG   C 1 162 ? 10.353  -11.753 46.469  0.70 42.74 ? 141 ARG   C CD  1 
ATOM   4774 N NE  . ARG   C 1 162 ? 10.644  -11.108 47.751  0.70 50.25 ? 141 ARG   C NE  1 
ATOM   4775 C CZ  . ARG   C 1 162 ? 10.280  -11.529 48.954  0.70 50.78 ? 141 ARG   C CZ  1 
ATOM   4776 N NH1 . ARG   C 1 162 ? 9.460   -12.558 49.107  0.70 57.65 ? 141 ARG   C NH1 1 
ATOM   4777 N NH2 . ARG   C 1 162 ? 10.714  -10.881 50.013  0.70 50.48 ? 141 ARG   C NH2 1 
ATOM   4778 N N   . GLN   C 1 163 ? 5.406   -14.012 44.819  1.00 45.00 ? 142 GLN   C N   1 
ATOM   4779 C CA  . GLN   C 1 163 ? 4.085   -14.498 45.191  1.00 49.91 ? 142 GLN   C CA  1 
ATOM   4780 C C   . GLN   C 1 163 ? 4.069   -16.030 45.049  1.00 61.20 ? 142 GLN   C C   1 
ATOM   4781 O O   . GLN   C 1 163 ? 4.134   -16.693 46.108  1.00 66.80 ? 142 GLN   C O   1 
ATOM   4782 C CB  . GLN   C 1 163 ? 2.899   -13.914 44.414  1.00 39.85 ? 142 GLN   C CB  1 
ATOM   4783 C CG  . GLN   C 1 163 ? 2.867   -12.394 44.242  1.00 36.24 ? 142 GLN   C CG  1 
ATOM   4784 C CD  . GLN   C 1 163 ? 2.722   -11.533 45.489  1.00 37.22 ? 142 GLN   C CD  1 
ATOM   4785 O OE1 . GLN   C 1 163 ? 2.067   -11.908 46.472  1.00 35.90 ? 142 GLN   C OE1 1 
ATOM   4786 N NE2 . GLN   C 1 163 ? 3.341   -10.351 45.463  1.00 34.36 ? 142 GLN   C NE2 1 
ATOM   4787 N N   . SER   C 1 173 ? -7.075  -13.697 49.176  1.00 54.70 ? 152 SER   C N   1 
ATOM   4788 C CA  . SER   C 1 173 ? -6.026  -13.037 48.343  1.00 50.37 ? 152 SER   C CA  1 
ATOM   4789 C C   . SER   C 1 173 ? -6.668  -12.227 47.212  1.00 44.33 ? 152 SER   C C   1 
ATOM   4790 O O   . SER   C 1 173 ? -7.571  -12.701 46.519  1.00 49.47 ? 152 SER   C O   1 
ATOM   4791 C CB  . SER   C 1 173 ? -5.029  -14.042 47.806  1.00 56.23 ? 152 SER   C CB  1 
ATOM   4792 N N   . ASN   C 1 174 ? -6.198  -10.984 47.054  1.00 41.51 ? 153 ASN   C N   1 
ATOM   4793 C CA  . ASN   C 1 174 ? -6.634  -10.080 45.998  1.00 35.55 ? 153 ASN   C CA  1 
ATOM   4794 C C   . ASN   C 1 174 ? -5.429  -9.296  45.477  1.00 28.46 ? 153 ASN   C C   1 
ATOM   4795 O O   . ASN   C 1 174 ? -5.256  -8.112  45.777  1.00 26.16 ? 153 ASN   C O   1 
ATOM   4796 C CB  . ASN   C 1 174 ? -7.719  -9.132  46.495  1.00 34.55 ? 153 ASN   C CB  1 
ATOM   4797 C CG  . ASN   C 1 174 ? -8.216  -8.207  45.410  1.00 39.09 ? 153 ASN   C CG  1 
ATOM   4798 O OD1 . ASN   C 1 174 ? -8.008  -8.460  44.216  1.00 38.18 ? 153 ASN   C OD1 1 
ATOM   4799 N ND2 . ASN   C 1 174 ? -8.888  -7.137  45.806  1.00 37.62 ? 153 ASN   C ND2 1 
ATOM   4800 N N   . LEU   C 1 175 ? -4.620  -9.988  44.686  1.00 22.69 ? 154 LEU   C N   1 
ATOM   4801 C CA  . LEU   C 1 175 ? -3.356  -9.475  44.170  1.00 24.89 ? 154 LEU   C CA  1 
ATOM   4802 C C   . LEU   C 1 175 ? -3.632  -8.727  42.869  1.00 22.92 ? 154 LEU   C C   1 
ATOM   4803 O O   . LEU   C 1 175 ? -4.354  -9.230  42.014  1.00 22.78 ? 154 LEU   C O   1 
ATOM   4804 C CB  . LEU   C 1 175 ? -2.456  -10.686 43.910  1.00 25.50 ? 154 LEU   C CB  1 
ATOM   4805 C CG  . LEU   C 1 175 ? -2.112  -11.554 45.132  1.00 28.42 ? 154 LEU   C CG  1 
ATOM   4806 C CD1 . LEU   C 1 175 ? -1.287  -12.781 44.716  1.00 26.51 ? 154 LEU   C CD1 1 
ATOM   4807 C CD2 . LEU   C 1 175 ? -1.394  -10.725 46.212  1.00 25.41 ? 154 LEU   C CD2 1 
ATOM   4808 N N   . SER   C 1 176 ? -3.102  -7.505  42.733  1.00 23.91 ? 155 SER   C N   1 
ATOM   4809 C CA  . SER   C 1 176 ? -3.239  -6.904  41.412  1.00 24.22 ? 155 SER   C CA  1 
ATOM   4810 C C   . SER   C 1 176 ? -2.210  -5.794  41.196  1.00 25.19 ? 155 SER   C C   1 
ATOM   4811 O O   . SER   C 1 176 ? -1.546  -5.318  42.139  1.00 21.42 ? 155 SER   C O   1 
ATOM   4812 C CB  . SER   C 1 176 ? -4.654  -6.432  41.124  1.00 25.94 ? 155 SER   C CB  1 
ATOM   4813 O OG  . SER   C 1 176 ? -4.878  -5.156  41.700  1.00 27.75 ? 155 SER   C OG  1 
ATOM   4814 N N   . ILE   C 1 177 ? -2.045  -5.459  39.907  1.00 21.92 ? 156 ILE   C N   1 
ATOM   4815 C CA  . ILE   C 1 177 ? -1.129  -4.426  39.468  1.00 18.74 ? 156 ILE   C CA  1 
ATOM   4816 C C   . ILE   C 1 177 ? -1.967  -3.421  38.682  1.00 19.22 ? 156 ILE   C C   1 
ATOM   4817 O O   . ILE   C 1 177 ? -2.852  -3.832  37.912  1.00 20.20 ? 156 ILE   C O   1 
ATOM   4818 C CB  . ILE   C 1 177 ? -0.037  -5.060  38.595  1.00 20.00 ? 156 ILE   C CB  1 
ATOM   4819 C CG1 . ILE   C 1 177 ? 0.730   -6.165  39.380  1.00 21.54 ? 156 ILE   C CG1 1 
ATOM   4820 C CG2 . ILE   C 1 177 ? 0.907   -3.989  38.071  1.00 18.31 ? 156 ILE   C CG2 1 
ATOM   4821 C CD1 . ILE   C 1 177 ? 1.771   -6.908  38.534  1.00 20.77 ? 156 ILE   C CD1 1 
ATOM   4822 N N   . VAL   C 1 178 ? -1.680  -2.125  38.898  1.00 18.24 ? 157 VAL   C N   1 
ATOM   4823 C CA  . VAL   C 1 178 ? -2.327  -1.083  38.127  1.00 18.64 ? 157 VAL   C CA  1 
ATOM   4824 C C   . VAL   C 1 178 ? -1.249  -0.211  37.512  1.00 21.11 ? 157 VAL   C C   1 
ATOM   4825 O O   . VAL   C 1 178 ? -0.402  0.337   38.234  1.00 18.56 ? 157 VAL   C O   1 
ATOM   4826 C CB  . VAL   C 1 178 ? -3.299  -0.204  38.949  1.00 22.37 ? 157 VAL   C CB  1 
ATOM   4827 C CG1 . VAL   C 1 178 ? -3.889  0.929   38.103  1.00 20.32 ? 157 VAL   C CG1 1 
ATOM   4828 C CG2 . VAL   C 1 178 ? -4.412  -1.028  39.592  1.00 22.00 ? 157 VAL   C CG2 1 
ATOM   4829 N N   . ASN   C 1 179 ? -1.340  -0.046  36.176  1.00 21.14 ? 158 ASN   C N   1 
ATOM   4830 C CA  . ASN   C 1 179 ? -0.351  0.710   35.433  1.00 18.23 ? 158 ASN   C CA  1 
ATOM   4831 C C   . ASN   C 1 179 ? -0.967  2.048   35.045  1.00 18.68 ? 158 ASN   C C   1 
ATOM   4832 O O   . ASN   C 1 179 ? -2.059  2.057   34.489  1.00 20.51 ? 158 ASN   C O   1 
ATOM   4833 C CB  . ASN   C 1 179 ? 0.081   -0.055  34.182  1.00 17.83 ? 158 ASN   C CB  1 
ATOM   4834 C CG  . ASN   C 1 179 ? 0.873   -1.272  34.584  1.00 21.17 ? 158 ASN   C CG  1 
ATOM   4835 O OD1 . ASN   C 1 179 ? 1.543   -1.191  35.619  1.00 18.84 ? 158 ASN   C OD1 1 
ATOM   4836 N ND2 . ASN   C 1 179 ? 0.792   -2.384  33.850  1.00 19.06 ? 158 ASN   C ND2 1 
ATOM   4837 N N   . LEU   C 1 180 ? -0.262  3.157   35.314  1.00 17.85 ? 159 LEU   C N   1 
ATOM   4838 C CA  . LEU   C 1 180 ? -0.765  4.469   34.904  1.00 18.65 ? 159 LEU   C CA  1 
ATOM   4839 C C   . LEU   C 1 180 ? -0.375  4.688   33.449  1.00 17.92 ? 159 LEU   C C   1 
ATOM   4840 O O   . LEU   C 1 180 ? 0.799   4.888   33.145  1.00 20.19 ? 159 LEU   C O   1 
ATOM   4841 C CB  . LEU   C 1 180 ? -0.284  5.623   35.806  1.00 20.08 ? 159 LEU   C CB  1 
ATOM   4842 C CG  . LEU   C 1 180 ? -1.070  5.862   37.103  1.00 22.93 ? 159 LEU   C CG  1 
ATOM   4843 C CD1 . LEU   C 1 180 ? -2.353  6.601   36.758  1.00 23.00 ? 159 LEU   C CD1 1 
ATOM   4844 C CD2 . LEU   C 1 180 ? -1.367  4.539   37.844  1.00 19.18 ? 159 LEU   C CD2 1 
ATOM   4845 N N   . CYS   C 1 181 ? -1.394  4.653   32.573  1.00 20.15 ? 160 CYS   C N   1 
ATOM   4846 C CA  . CYS   C 1 181 ? -1.219  4.757   31.126  1.00 21.13 ? 160 CYS   C CA  1 
ATOM   4847 C C   . CYS   C 1 181 ? -1.510  6.198   30.715  1.00 23.59 ? 160 CYS   C C   1 
ATOM   4848 O O   . CYS   C 1 181 ? -1.275  7.106   31.518  1.00 24.72 ? 160 CYS   C O   1 
ATOM   4849 C CB  . CYS   C 1 181 ? -2.087  3.724   30.426  1.00 21.74 ? 160 CYS   C CB  1 
ATOM   4850 S SG  . CYS   C 1 181 ? -1.582  2.026   30.865  1.00 26.49 ? 160 CYS   C SG  1 
ATOM   4851 N N   . ASP   C 1 182 ? -1.980  6.411   29.474  1.00 20.11 ? 161 ASP   C N   1 
ATOM   4852 C CA  . ASP   C 1 182 ? -2.226  7.763   28.991  1.00 20.28 ? 161 ASP   C CA  1 
ATOM   4853 C C   . ASP   C 1 182 ? -3.331  7.661   27.919  1.00 21.52 ? 161 ASP   C C   1 
ATOM   4854 O O   . ASP   C 1 182 ? -3.180  6.939   26.939  1.00 19.78 ? 161 ASP   C O   1 
ATOM   4855 C CB  . ASP   C 1 182 ? -0.917  8.426   28.533  1.00 23.01 ? 161 ASP   C CB  1 
ATOM   4856 C CG  . ASP   C 1 182 ? -1.069  9.862   28.038  1.00 28.93 ? 161 ASP   C CG  1 
ATOM   4857 O OD1 . ASP   C 1 182 ? -2.142  10.169  27.460  1.00 27.55 ? 161 ASP   C OD1 1 
ATOM   4858 O OD2 . ASP   C 1 182 ? -0.136  10.683  28.251  1.00 29.49 ? 161 ASP   C OD2 1 
ATOM   4859 N N   . ALA   C 1 183 ? -4.469  8.337   28.142  1.00 21.19 ? 162 ALA   C N   1 
ATOM   4860 C CA  . ALA   C 1 183 ? -5.593  8.307   27.226  1.00 20.97 ? 162 ALA   C CA  1 
ATOM   4861 C C   . ALA   C 1 183 ? -5.274  8.876   25.838  1.00 20.37 ? 162 ALA   C C   1 
ATOM   4862 O O   . ALA   C 1 183 ? -6.030  8.593   24.909  1.00 21.04 ? 162 ALA   C O   1 
ATOM   4863 C CB  . ALA   C 1 183 ? -6.801  9.014   27.854  1.00 22.57 ? 162 ALA   C CB  1 
ATOM   4864 N N   . MET   C 1 184 ? -4.212  9.694   25.700  1.00 19.30 ? 163 MET   C N   1 
ATOM   4865 C CA  . MET   C 1 184 ? -3.942  10.454  24.484  1.00 20.78 ? 163 MET   C CA  1 
ATOM   4866 C C   . MET   C 1 184 ? -2.822  9.824   23.651  1.00 22.62 ? 163 MET   C C   1 
ATOM   4867 O O   . MET   C 1 184 ? -2.323  10.458  22.723  1.00 23.80 ? 163 MET   C O   1 
ATOM   4868 C CB  . MET   C 1 184 ? -3.637  11.929  24.795  1.00 22.04 ? 163 MET   C CB  1 
ATOM   4869 C CG  . MET   C 1 184 ? -4.815  12.615  25.492  1.00 25.44 ? 163 MET   C CG  1 
ATOM   4870 S SD  . MET   C 1 184 ? -6.237  12.747  24.379  1.00 29.67 ? 163 MET   C SD  1 
ATOM   4871 C CE  . MET   C 1 184 ? -5.578  13.993  23.267  1.00 32.27 ? 163 MET   C CE  1 
ATOM   4872 N N   . VAL   C 1 185 ? -2.565  8.521   23.862  1.00 22.18 ? 164 VAL   C N   1 
ATOM   4873 C CA  . VAL   C 1 185 ? -1.402  7.875   23.267  1.00 32.32 ? 164 VAL   C CA  1 
ATOM   4874 C C   . VAL   C 1 185 ? -1.561  7.752   21.759  1.00 29.91 ? 164 VAL   C C   1 
ATOM   4875 O O   . VAL   C 1 185 ? -0.545  7.664   21.066  1.00 26.81 ? 164 VAL   C O   1 
ATOM   4876 C CB  . VAL   C 1 185 ? -1.019  6.485   23.817  1.00 32.36 ? 164 VAL   C CB  1 
ATOM   4877 C CG1 . VAL   C 1 185 ? -0.190  6.599   25.094  1.00 38.73 ? 164 VAL   C CG1 1 
ATOM   4878 C CG2 . VAL   C 1 185 ? -2.230  5.579   23.977  1.00 31.04 ? 164 VAL   C CG2 1 
ATOM   4879 N N   . ASP   C 1 186 ? -2.814  7.681   21.277  1.00 25.80 ? 165 ASP   C N   1 
ATOM   4880 C CA  . ASP   C 1 186 ? -3.042  7.575   19.840  1.00 25.03 ? 165 ASP   C CA  1 
ATOM   4881 C C   . ASP   C 1 186 ? -3.205  8.927   19.152  1.00 23.64 ? 165 ASP   C C   1 
ATOM   4882 O O   . ASP   C 1 186 ? -3.407  8.994   17.916  1.00 24.05 ? 165 ASP   C O   1 
ATOM   4883 C CB  . ASP   C 1 186 ? -4.190  6.640   19.529  1.00 25.55 ? 165 ASP   C CB  1 
ATOM   4884 C CG  . ASP   C 1 186 ? -3.875  5.211   19.921  1.00 28.16 ? 165 ASP   C CG  1 
ATOM   4885 O OD1 . ASP   C 1 186 ? -2.721  4.764   19.708  1.00 28.41 ? 165 ASP   C OD1 1 
ATOM   4886 O OD2 . ASP   C 1 186 ? -4.783  4.564   20.417  1.00 31.41 ? 165 ASP   C OD2 1 
ATOM   4887 N N   . GLN   C 1 187 ? -3.160  10.000  19.937  1.00 22.07 ? 166 GLN   C N   1 
ATOM   4888 C CA  . GLN   C 1 187 ? -3.207  11.336  19.374  1.00 24.71 ? 166 GLN   C CA  1 
ATOM   4889 C C   . GLN   C 1 187 ? -2.143  12.116  20.134  1.00 25.58 ? 166 GLN   C C   1 
ATOM   4890 O O   . GLN   C 1 187 ? -2.456  13.016  20.894  1.00 25.18 ? 166 GLN   C O   1 
ATOM   4891 C CB  . GLN   C 1 187 ? -4.573  12.013  19.507  1.00 25.41 ? 166 GLN   C CB  1 
ATOM   4892 C CG  . GLN   C 1 187 ? -5.719  11.213  18.901  1.00 29.47 ? 166 GLN   C CG  1 
ATOM   4893 C CD  . GLN   C 1 187 ? -6.850  10.978  19.892  1.00 36.52 ? 166 GLN   C CD  1 
ATOM   4894 O OE1 . GLN   C 1 187 ? -6.875  9.968   20.602  1.00 36.33 ? 166 GLN   C OE1 1 
ATOM   4895 N NE2 . GLN   C 1 187 ? -7.823  11.882  19.933  1.00 35.46 ? 166 GLN   C NE2 1 
ATOM   4896 N N   . PRO   C 1 188 ? -0.856  11.769  19.934  1.00 26.39 ? 167 PRO   C N   1 
ATOM   4897 C CA  . PRO   C 1 188 ? 0.208   12.236  20.831  1.00 27.78 ? 167 PRO   C CA  1 
ATOM   4898 C C   . PRO   C 1 188 ? 0.596   13.710  20.662  1.00 26.41 ? 167 PRO   C C   1 
ATOM   4899 O O   . PRO   C 1 188 ? 0.361   14.316  19.612  1.00 24.32 ? 167 PRO   C O   1 
ATOM   4900 C CB  . PRO   C 1 188 ? 1.350   11.255  20.498  1.00 24.02 ? 167 PRO   C CB  1 
ATOM   4901 C CG  . PRO   C 1 188 ? 1.166   10.915  19.028  1.00 24.82 ? 167 PRO   C CG  1 
ATOM   4902 C CD  . PRO   C 1 188 ? -0.376  10.911  18.828  1.00 24.28 ? 167 PRO   C CD  1 
HETATM 4903 N N   . CSX   C 1 189 ? 1.169   14.293  21.721  1.00 27.89 ? 168 CSX   C N   1 
HETATM 4904 C CA  . CSX   C 1 189 ? 1.818   15.594  21.620  1.00 28.25 ? 168 CSX   C CA  1 
HETATM 4905 C CB  . CSX   C 1 189 ? 2.350   16.056  22.976  1.00 33.40 ? 168 CSX   C CB  1 
HETATM 4906 S SG  . CSX   C 1 189 ? 0.895   16.378  24.007  1.00 44.98 ? 168 CSX   C SG  1 
HETATM 4907 C C   . CSX   C 1 189 ? 2.976   15.549  20.619  1.00 28.29 ? 168 CSX   C C   1 
HETATM 4908 O O   . CSX   C 1 189 ? 3.732   14.582  20.548  1.00 24.59 ? 168 CSX   C O   1 
HETATM 4909 O OD  . CSX   C 1 189 ? 0.616   17.823  23.771  1.00 41.88 ? 168 CSX   C OD  1 
ATOM   4910 N N   . MET   C 1 190 ? 3.096   16.624  19.832  1.00 26.42 ? 169 MET   C N   1 
ATOM   4911 C CA  . MET   C 1 190 ? 4.175   16.774  18.859  1.00 29.84 ? 169 MET   C CA  1 
ATOM   4912 C C   . MET   C 1 190 ? 5.521   16.687  19.598  1.00 25.13 ? 169 MET   C C   1 
ATOM   4913 O O   . MET   C 1 190 ? 5.667   17.318  20.622  1.00 26.27 ? 169 MET   C O   1 
ATOM   4914 C CB  . MET   C 1 190 ? 3.994   18.166  18.221  1.00 30.96 ? 169 MET   C CB  1 
ATOM   4915 C CG  . MET   C 1 190 ? 5.128   18.635  17.362  1.00 37.68 ? 169 MET   C CG  1 
ATOM   4916 S SD  . MET   C 1 190 ? 5.078   17.504  15.964  1.00 46.46 ? 169 MET   C SD  1 
ATOM   4917 C CE  . MET   C 1 190 ? 3.647   18.011  14.991  1.00 39.36 ? 169 MET   C CE  1 
ATOM   4918 N N   . ALA   C 1 191 ? 6.490   15.914  19.087  1.00 25.43 ? 170 ALA   C N   1 
ATOM   4919 C CA  . ALA   C 1 191 ? 7.847   15.854  19.626  1.00 26.37 ? 170 ALA   C CA  1 
ATOM   4920 C C   . ALA   C 1 191 ? 7.987   15.040  20.918  1.00 24.63 ? 170 ALA   C C   1 
ATOM   4921 O O   . ALA   C 1 191 ? 9.038   15.145  21.557  1.00 25.94 ? 170 ALA   C O   1 
ATOM   4922 C CB  . ALA   C 1 191 ? 8.483   17.237  19.785  1.00 27.13 ? 170 ALA   C CB  1 
ATOM   4923 N N   . PHE   C 1 192 ? 7.003   14.173  21.239  1.00 21.78 ? 171 PHE   C N   1 
ATOM   4924 C CA  . PHE   C 1 192 ? 7.048   13.336  22.434  1.00 21.61 ? 171 PHE   C CA  1 
ATOM   4925 C C   . PHE   C 1 192 ? 7.147   11.850  22.058  1.00 22.70 ? 171 PHE   C C   1 
ATOM   4926 O O   . PHE   C 1 192 ? 6.518   10.992  22.694  1.00 21.95 ? 171 PHE   C O   1 
ATOM   4927 C CB  . PHE   C 1 192 ? 5.857   13.600  23.363  1.00 22.97 ? 171 PHE   C CB  1 
ATOM   4928 C CG  . PHE   C 1 192 ? 5.980   14.870  24.200  1.00 25.62 ? 171 PHE   C CG  1 
ATOM   4929 C CD1 . PHE   C 1 192 ? 5.715   16.131  23.641  1.00 24.70 ? 171 PHE   C CD1 1 
ATOM   4930 C CD2 . PHE   C 1 192 ? 6.343   14.801  25.546  1.00 24.57 ? 171 PHE   C CD2 1 
ATOM   4931 C CE1 . PHE   C 1 192 ? 5.846   17.289  24.418  1.00 30.34 ? 171 PHE   C CE1 1 
ATOM   4932 C CE2 . PHE   C 1 192 ? 6.427   15.960  26.320  1.00 29.89 ? 171 PHE   C CE2 1 
ATOM   4933 C CZ  . PHE   C 1 192 ? 6.172   17.201  25.764  1.00 27.17 ? 171 PHE   C CZ  1 
ATOM   4934 N N   . SER   C 1 193 ? 7.985   11.518  21.066  1.00 21.51 ? 172 SER   C N   1 
ATOM   4935 C CA  A SER   C 1 193 ? 7.993   10.140  20.584  0.60 21.92 ? 172 SER   C CA  1 
ATOM   4936 C CA  B SER   C 1 193 ? 8.035   10.142  20.569  0.40 20.87 ? 172 SER   C CA  1 
ATOM   4937 C C   . SER   C 1 193 ? 8.435   9.171   21.683  1.00 21.36 ? 172 SER   C C   1 
ATOM   4938 O O   . SER   C 1 193 ? 7.846   8.105   21.856  1.00 21.05 ? 172 SER   C O   1 
ATOM   4939 C CB  A SER   C 1 193 ? 8.806   9.991   19.326  0.60 23.48 ? 172 SER   C CB  1 
ATOM   4940 C CB  B SER   C 1 193 ? 8.964   9.979   19.378  0.40 20.47 ? 172 SER   C CB  1 
ATOM   4941 O OG  A SER   C 1 193 ? 10.033  10.703  19.435  0.60 26.35 ? 172 SER   C OG  1 
ATOM   4942 O OG  B SER   C 1 193 ? 8.506   10.625  18.196  0.40 18.91 ? 172 SER   C OG  1 
ATOM   4943 N N   . LEU   C 1 194 ? 9.507   9.490   22.414  1.00 20.33 ? 173 LEU   C N   1 
ATOM   4944 C CA  . LEU   C 1 194 ? 9.975   8.512   23.394  1.00 21.15 ? 173 LEU   C CA  1 
ATOM   4945 C C   . LEU   C 1 194 ? 8.936   8.285   24.500  1.00 17.82 ? 173 LEU   C C   1 
ATOM   4946 O O   . LEU   C 1 194 ? 8.708   7.153   24.932  1.00 20.08 ? 173 LEU   C O   1 
ATOM   4947 C CB  . LEU   C 1 194 ? 11.360  8.822   23.982  1.00 20.71 ? 173 LEU   C CB  1 
ATOM   4948 C CG  . LEU   C 1 194 ? 12.552  8.440   23.083  1.00 21.37 ? 173 LEU   C CG  1 
ATOM   4949 C CD1 . LEU   C 1 194 ? 13.890  9.084   23.613  1.00 21.14 ? 173 LEU   C CD1 1 
ATOM   4950 C CD2 . LEU   C 1 194 ? 12.679  6.945   22.885  1.00 19.02 ? 173 LEU   C CD2 1 
ATOM   4951 N N   . TYR   C 1 195 ? 8.341   9.365   25.002  1.00 19.70 ? 174 TYR   C N   1 
ATOM   4952 C CA  . TYR   C 1 195 ? 7.291   9.239   26.011  1.00 18.60 ? 174 TYR   C CA  1 
ATOM   4953 C C   . TYR   C 1 195 ? 6.159   8.331   25.496  1.00 18.63 ? 174 TYR   C C   1 
ATOM   4954 O O   . TYR   C 1 195 ? 5.688   7.405   26.204  1.00 20.07 ? 174 TYR   C O   1 
ATOM   4955 C CB  . TYR   C 1 195 ? 6.753   10.641  26.338  1.00 19.51 ? 174 TYR   C CB  1 
ATOM   4956 C CG  . TYR   C 1 195 ? 5.523   10.555  27.238  1.00 19.56 ? 174 TYR   C CG  1 
ATOM   4957 C CD1 . TYR   C 1 195 ? 5.644   10.277  28.608  1.00 20.69 ? 174 TYR   C CD1 1 
ATOM   4958 C CD2 . TYR   C 1 195 ? 4.244   10.692  26.704  1.00 19.18 ? 174 TYR   C CD2 1 
ATOM   4959 C CE1 . TYR   C 1 195 ? 4.514   10.157  29.424  1.00 20.94 ? 174 TYR   C CE1 1 
ATOM   4960 C CE2 . TYR   C 1 195 ? 3.114   10.611  27.521  1.00 22.32 ? 174 TYR   C CE2 1 
ATOM   4961 C CZ  . TYR   C 1 195 ? 3.243   10.322  28.876  1.00 22.67 ? 174 TYR   C CZ  1 
ATOM   4962 O OH  . TYR   C 1 195 ? 2.104   10.185  29.663  1.00 23.58 ? 174 TYR   C OH  1 
ATOM   4963 N N   . ASN   C 1 196 ? 5.717   8.577   24.251  1.00 19.24 ? 175 ASN   C N   1 
ATOM   4964 C CA  A ASN   C 1 196 ? 4.612   7.842   23.640  0.50 19.33 ? 175 ASN   C CA  1 
ATOM   4965 C CA  B ASN   C 1 196 ? 4.585   7.819   23.732  0.50 19.99 ? 175 ASN   C CA  1 
ATOM   4966 C C   . ASN   C 1 196 ? 4.991   6.375   23.484  1.00 18.09 ? 175 ASN   C C   1 
ATOM   4967 O O   . ASN   C 1 196 ? 4.197   5.486   23.703  1.00 17.71 ? 175 ASN   C O   1 
ATOM   4968 C CB  A ASN   C 1 196 ? 4.316   8.375   22.240  0.50 19.74 ? 175 ASN   C CB  1 
ATOM   4969 C CB  B ASN   C 1 196 ? 3.946   8.478   22.516  0.50 22.65 ? 175 ASN   C CB  1 
ATOM   4970 C CG  A ASN   C 1 196 ? 2.926   8.013   21.775  0.50 20.41 ? 175 ASN   C CG  1 
ATOM   4971 C CG  B ASN   C 1 196 ? 3.224   9.726   22.947  0.50 23.40 ? 175 ASN   C CG  1 
ATOM   4972 O OD1 A ASN   C 1 196 ? 2.740   7.470   20.675  0.50 26.29 ? 175 ASN   C OD1 1 
ATOM   4973 O OD1 B ASN   C 1 196 ? 2.139   9.635   23.527  0.50 31.15 ? 175 ASN   C OD1 1 
ATOM   4974 N ND2 A ASN   C 1 196 ? 1.928   8.359   22.562  0.50 15.42 ? 175 ASN   C ND2 1 
ATOM   4975 N ND2 B ASN   C 1 196 ? 3.828   10.884  22.735  0.50 22.41 ? 175 ASN   C ND2 1 
ATOM   4976 N N   . MET   C 1 197 ? 6.224   6.141   23.038  1.00 18.73 ? 176 MET   C N   1 
ATOM   4977 C CA  . MET   C 1 197 ? 6.702   4.758   22.952  1.00 18.34 ? 176 MET   C CA  1 
ATOM   4978 C C   . MET   C 1 197 ? 6.591   4.037   24.301  1.00 19.15 ? 176 MET   C C   1 
ATOM   4979 O O   . MET   C 1 197 ? 6.194   2.866   24.360  1.00 17.79 ? 176 MET   C O   1 
ATOM   4980 C CB  . MET   C 1 197 ? 8.147   4.734   22.430  1.00 19.07 ? 176 MET   C CB  1 
ATOM   4981 C CG  . MET   C 1 197 ? 8.240   5.150   20.975  1.00 20.33 ? 176 MET   C CG  1 
ATOM   4982 S SD  . MET   C 1 197 ? 9.952   5.475   20.478  1.00 22.41 ? 176 MET   C SD  1 
ATOM   4983 C CE  . MET   C 1 197 ? 10.549  3.779   20.550  1.00 24.10 ? 176 MET   C CE  1 
ATOM   4984 N N   . GLY   C 1 198 ? 7.045   4.713   25.373  1.00 18.35 ? 177 GLY   C N   1 
ATOM   4985 C CA  . GLY   C 1 198 ? 7.049   4.160   26.724  1.00 18.73 ? 177 GLY   C CA  1 
ATOM   4986 C C   . GLY   C 1 198 ? 5.626   3.793   27.178  1.00 17.31 ? 177 GLY   C C   1 
ATOM   4987 O O   . GLY   C 1 198 ? 5.395   2.702   27.699  1.00 17.03 ? 177 GLY   C O   1 
ATOM   4988 N N   . LYS   C 1 199 ? 4.652   4.661   26.900  1.00 16.39 ? 178 LYS   C N   1 
ATOM   4989 C CA  . LYS   C 1 199 ? 3.269   4.451   27.329  1.00 17.43 ? 178 LYS   C CA  1 
ATOM   4990 C C   . LYS   C 1 199 ? 2.624   3.356   26.479  1.00 17.79 ? 178 LYS   C C   1 
ATOM   4991 O O   . LYS   C 1 199 ? 1.850   2.554   26.985  1.00 18.02 ? 178 LYS   C O   1 
ATOM   4992 C CB  . LYS   C 1 199 ? 2.470   5.763   27.341  1.00 19.45 ? 178 LYS   C CB  1 
ATOM   4993 C CG  . LYS   C 1 199 ? 2.844   6.763   28.472  1.00 21.04 ? 178 LYS   C CG  1 
ATOM   4994 C CD  . LYS   C 1 199 ? 2.761   6.152   29.868  1.00 19.24 ? 178 LYS   C CD  1 
ATOM   4995 C CE  . LYS   C 1 199 ? 2.658   7.222   30.916  1.00 21.28 ? 178 LYS   C CE  1 
ATOM   4996 N NZ  . LYS   C 1 199 ? 2.829   6.766   32.303  1.00 20.76 ? 178 LYS   C NZ  1 
ATOM   4997 N N   . HIS   C 1 200 ? 3.006   3.262   25.190  1.00 18.19 ? 179 HIS   C N   1 
ATOM   4998 C CA  . HIS   C 1 200 ? 2.442   2.186   24.386  1.00 17.69 ? 179 HIS   C CA  1 
ATOM   4999 C C   . HIS   C 1 200 ? 3.011   0.856   24.867  1.00 18.24 ? 179 HIS   C C   1 
ATOM   5000 O O   . HIS   C 1 200 ? 2.273   -0.137  24.918  1.00 18.14 ? 179 HIS   C O   1 
ATOM   5001 C CB  . HIS   C 1 200 ? 2.822   2.352   22.906  1.00 18.32 ? 179 HIS   C CB  1 
ATOM   5002 C CG  . HIS   C 1 200 ? 1.765   3.059   22.129  1.00 21.54 ? 179 HIS   C CG  1 
ATOM   5003 N ND1 . HIS   C 1 200 ? 0.736   2.406   21.489  1.00 23.08 ? 179 HIS   C ND1 1 
ATOM   5004 C CD2 . HIS   C 1 200 ? 1.567   4.375   21.903  1.00 22.52 ? 179 HIS   C CD2 1 
ATOM   5005 C CE1 . HIS   C 1 200 ? -0.051  3.284   20.885  1.00 23.85 ? 179 HIS   C CE1 1 
ATOM   5006 N NE2 . HIS   C 1 200 ? 0.452   4.496   21.107  1.00 25.00 ? 179 HIS   C NE2 1 
ATOM   5007 N N   . ALA   C 1 201 ? 4.334   0.853   25.179  1.00 18.08 ? 180 ALA   C N   1 
ATOM   5008 C CA  . ALA   C 1 201 ? 4.957   -0.348  25.743  1.00 17.97 ? 180 ALA   C CA  1 
ATOM   5009 C C   . ALA   C 1 201 ? 4.250   -0.758  27.032  1.00 17.17 ? 180 ALA   C C   1 
ATOM   5010 O O   . ALA   C 1 201 ? 4.042   -1.944  27.295  1.00 18.40 ? 180 ALA   C O   1 
ATOM   5011 C CB  . ALA   C 1 201 ? 6.454   -0.158  25.974  1.00 17.30 ? 180 ALA   C CB  1 
ATOM   5012 N N   . LEU   C 1 202 ? 3.850   0.241   27.838  1.00 17.70 ? 181 LEU   C N   1 
ATOM   5013 C CA  . LEU   C 1 202 ? 3.108   -0.020  29.081  1.00 18.89 ? 181 LEU   C CA  1 
ATOM   5014 C C   . LEU   C 1 202 ? 1.752   -0.697  28.830  1.00 18.49 ? 181 LEU   C C   1 
ATOM   5015 O O   . LEU   C 1 202 ? 1.319   -1.565  29.613  1.00 19.25 ? 181 LEU   C O   1 
ATOM   5016 C CB  . LEU   C 1 202 ? 2.979   1.277   29.887  1.00 19.29 ? 181 LEU   C CB  1 
ATOM   5017 C CG  . LEU   C 1 202 ? 2.503   1.109   31.339  1.00 22.21 ? 181 LEU   C CG  1 
ATOM   5018 C CD1 . LEU   C 1 202 ? 3.391   0.173   32.220  1.00 22.37 ? 181 LEU   C CD1 1 
ATOM   5019 C CD2 . LEU   C 1 202 ? 2.364   2.524   31.935  1.00 22.02 ? 181 LEU   C CD2 1 
ATOM   5020 N N   . VAL   C 1 203 ? 1.056   -0.292  27.743  1.00 19.47 ? 182 VAL   C N   1 
ATOM   5021 C CA  . VAL   C 1 203 ? -0.166  -0.980  27.335  1.00 19.46 ? 182 VAL   C CA  1 
ATOM   5022 C C   . VAL   C 1 203 ? 0.159   -2.441  27.037  1.00 17.83 ? 182 VAL   C C   1 
ATOM   5023 O O   . VAL   C 1 203 ? -0.554  -3.337  27.470  1.00 19.03 ? 182 VAL   C O   1 
ATOM   5024 C CB  . VAL   C 1 203 ? -0.865  -0.335  26.118  1.00 22.41 ? 182 VAL   C CB  1 
ATOM   5025 C CG1 . VAL   C 1 203 ? -2.071  -1.166  25.656  1.00 22.26 ? 182 VAL   C CG1 1 
ATOM   5026 C CG2 . VAL   C 1 203 ? -1.320  1.089   26.434  1.00 24.68 ? 182 VAL   C CG2 1 
ATOM   5027 N N   . GLY   C 1 204 ? 1.217   -2.668  26.241  1.00 17.77 ? 183 GLY   C N   1 
ATOM   5028 C CA  . GLY   C 1 204 ? 1.639   -4.019  25.915  1.00 17.35 ? 183 GLY   C CA  1 
ATOM   5029 C C   . GLY   C 1 204 ? 1.939   -4.841  27.169  1.00 18.43 ? 183 GLY   C C   1 
ATOM   5030 O O   . GLY   C 1 204 ? 1.537   -6.006  27.248  1.00 19.57 ? 183 GLY   C O   1 
ATOM   5031 N N   . LEU   C 1 205 ? 2.672   -4.239  28.133  1.00 17.49 ? 184 LEU   C N   1 
ATOM   5032 C CA  . LEU   C 1 205 ? 2.965   -4.941  29.369  1.00 16.77 ? 184 LEU   C CA  1 
ATOM   5033 C C   . LEU   C 1 205 ? 1.662   -5.276  30.106  1.00 16.94 ? 184 LEU   C C   1 
ATOM   5034 O O   . LEU   C 1 205 ? 1.513   -6.387  30.636  1.00 19.18 ? 184 LEU   C O   1 
ATOM   5035 C CB  . LEU   C 1 205 ? 3.874   -4.090  30.244  1.00 17.79 ? 184 LEU   C CB  1 
ATOM   5036 C CG  . LEU   C 1 205 ? 4.073   -4.627  31.673  1.00 18.72 ? 184 LEU   C CG  1 
ATOM   5037 C CD1 . LEU   C 1 205 ? 4.743   -6.005  31.643  1.00 19.82 ? 184 LEU   C CD1 1 
ATOM   5038 C CD2 . LEU   C 1 205 ? 4.874   -3.578  32.476  1.00 19.10 ? 184 LEU   C CD2 1 
ATOM   5039 N N   . THR   C 1 206 ? 0.719   -4.322  30.139  1.00 17.04 ? 185 THR   C N   1 
ATOM   5040 C CA  . THR   C 1 206 ? -0.535  -4.574  30.854  1.00 17.58 ? 185 THR   C CA  1 
ATOM   5041 C C   . THR   C 1 206 ? -1.230  -5.817  30.297  1.00 17.91 ? 185 THR   C C   1 
ATOM   5042 O O   . THR   C 1 206 ? -1.706  -6.691  31.048  1.00 19.25 ? 185 THR   C O   1 
ATOM   5043 C CB  . THR   C 1 206 ? -1.465  -3.358  30.791  1.00 17.82 ? 185 THR   C CB  1 
ATOM   5044 O OG1 . THR   C 1 206 ? -0.748  -2.243  31.301  1.00 19.78 ? 185 THR   C OG1 1 
ATOM   5045 C CG2 . THR   C 1 206 ? -2.735  -3.554  31.614  1.00 18.80 ? 185 THR   C CG2 1 
ATOM   5046 N N   . GLN   C 1 207 ? -1.310  -5.885  28.957  1.00 16.74 ? 186 GLN   C N   1 
ATOM   5047 C CA  . GLN   C 1 207 ? -1.971  -7.019  28.327  1.00 18.32 ? 186 GLN   C CA  1 
ATOM   5048 C C   . GLN   C 1 207 ? -1.187  -8.312  28.543  1.00 18.47 ? 186 GLN   C C   1 
ATOM   5049 O O   . GLN   C 1 207 ? -1.783  -9.344  28.876  1.00 19.22 ? 186 GLN   C O   1 
ATOM   5050 C CB  . GLN   C 1 207 ? -2.208  -6.768  26.832  1.00 18.64 ? 186 GLN   C CB  1 
ATOM   5051 C CG  . GLN   C 1 207 ? -3.042  -5.517  26.580  1.00 24.64 ? 186 GLN   C CG  1 
ATOM   5052 C CD  . GLN   C 1 207 ? -3.189  -5.182  25.107  1.00 29.83 ? 186 GLN   C CD  1 
ATOM   5053 O OE1 . GLN   C 1 207 ? -2.287  -5.379  24.280  1.00 33.95 ? 186 GLN   C OE1 1 
ATOM   5054 N NE2 . GLN   C 1 207 ? -4.358  -4.664  24.798  1.00 31.83 ? 186 GLN   C NE2 1 
ATOM   5055 N N   . SER   C 1 208 ? 0.118   -8.287  28.224  1.00 17.97 ? 187 SER   C N   1 
ATOM   5056 C CA  . SER   C 1 208 ? 0.936   -9.501  28.290  1.00 18.45 ? 187 SER   C CA  1 
ATOM   5057 C C   . SER   C 1 208 ? 0.994   -10.049 29.719  1.00 17.24 ? 187 SER   C C   1 
ATOM   5058 O O   . SER   C 1 208 ? 0.861   -11.267 29.947  1.00 20.87 ? 187 SER   C O   1 
ATOM   5059 C CB  . SER   C 1 208 ? 2.363   -9.231  27.804  1.00 20.01 ? 187 SER   C CB  1 
ATOM   5060 O OG  . SER   C 1 208 ? 2.416   -9.135  26.395  1.00 21.26 ? 187 SER   C OG  1 
ATOM   5061 N N   . ALA   C 1 209 ? 1.143   -9.146  30.692  1.00 17.52 ? 188 ALA   C N   1 
ATOM   5062 C CA  . ALA   C 1 209 ? 1.216   -9.577  32.095  1.00 19.73 ? 188 ALA   C CA  1 
ATOM   5063 C C   . ALA   C 1 209 ? -0.150  -10.049 32.604  1.00 20.56 ? 188 ALA   C C   1 
ATOM   5064 O O   . ALA   C 1 209 ? -0.222  -11.027 33.369  1.00 20.31 ? 188 ALA   C O   1 
ATOM   5065 C CB  . ALA   C 1 209 ? 1.790   -8.490  32.966  1.00 17.01 ? 188 ALA   C CB  1 
ATOM   5066 N N   . ALA   C 1 210 ? -1.244  -9.400  32.145  1.00 19.14 ? 189 ALA   C N   1 
ATOM   5067 C CA  . ALA   C 1 210 ? -2.562  -9.883  32.544  1.00 19.82 ? 189 ALA   C CA  1 
ATOM   5068 C C   . ALA   C 1 210 ? -2.721  -11.341 32.111  1.00 21.59 ? 189 ALA   C C   1 
ATOM   5069 O O   . ALA   C 1 210 ? -3.208  -12.187 32.855  1.00 22.54 ? 189 ALA   C O   1 
ATOM   5070 C CB  . ALA   C 1 210 ? -3.663  -9.043  31.899  1.00 20.47 ? 189 ALA   C CB  1 
ATOM   5071 N N   . LEU   C 1 211 ? -2.387  -11.624 30.850  1.00 21.16 ? 190 LEU   C N   1 
ATOM   5072 C CA  . LEU   C 1 211 ? -2.547  -12.980 30.361  1.00 21.01 ? 190 LEU   C CA  1 
ATOM   5073 C C   . LEU   C 1 211 ? -1.661  -13.952 31.147  1.00 22.24 ? 190 LEU   C C   1 
ATOM   5074 O O   . LEU   C 1 211 ? -2.082  -15.061 31.506  1.00 24.11 ? 190 LEU   C O   1 
ATOM   5075 C CB  . LEU   C 1 211 ? -2.167  -12.929 28.872  1.00 24.83 ? 190 LEU   C CB  1 
ATOM   5076 C CG  . LEU   C 1 211 ? -2.141  -14.278 28.140  1.00 26.02 ? 190 LEU   C CG  1 
ATOM   5077 C CD1 . LEU   C 1 211 ? -3.591  -14.697 27.949  1.00 25.61 ? 190 LEU   C CD1 1 
ATOM   5078 C CD2 . LEU   C 1 211 ? -1.414  -14.171 26.778  1.00 28.75 ? 190 LEU   C CD2 1 
ATOM   5079 N N   . GLU   C 1 212 ? -0.387  -13.588 31.344  1.00 23.04 ? 191 GLU   C N   1 
ATOM   5080 C CA  . GLU   C 1 212 ? 0.604   -14.519 31.901  1.00 24.21 ? 191 GLU   C CA  1 
ATOM   5081 C C   . GLU   C 1 212 ? 0.373   -14.734 33.398  1.00 24.19 ? 191 GLU   C C   1 
ATOM   5082 O O   . GLU   C 1 212 ? 0.652   -15.807 33.922  1.00 24.15 ? 191 GLU   C O   1 
ATOM   5083 C CB  . GLU   C 1 212 ? 2.040   -14.042 31.641  1.00 21.64 ? 191 GLU   C CB  1 
ATOM   5084 C CG  . GLU   C 1 212 ? 3.139   -14.988 32.127  1.00 25.37 ? 191 GLU   C CG  1 
ATOM   5085 C CD  . GLU   C 1 212 ? 4.477   -14.486 31.590  1.00 29.29 ? 191 GLU   C CD  1 
ATOM   5086 O OE1 . GLU   C 1 212 ? 5.488   -15.087 31.983  1.00 28.91 ? 191 GLU   C OE1 1 
ATOM   5087 O OE2 . GLU   C 1 212 ? 4.537   -13.508 30.781  1.00 29.05 ? 191 GLU   C OE2 1 
ATOM   5088 N N   . LEU   C 1 213 ? -0.077  -13.694 34.109  1.00 23.45 ? 192 LEU   C N   1 
ATOM   5089 C CA  . LEU   C 1 213 ? -0.226  -13.786 35.559  1.00 21.75 ? 192 LEU   C CA  1 
ATOM   5090 C C   . LEU   C 1 213 ? -1.636  -14.232 35.967  1.00 25.09 ? 192 LEU   C C   1 
ATOM   5091 O O   . LEU   C 1 213 ? -1.866  -14.536 37.135  1.00 25.13 ? 192 LEU   C O   1 
ATOM   5092 C CB  . LEU   C 1 213 ? 0.186   -12.473 36.222  1.00 20.19 ? 192 LEU   C CB  1 
ATOM   5093 C CG  . LEU   C 1 213 ? 1.634   -12.041 35.919  1.00 20.97 ? 192 LEU   C CG  1 
ATOM   5094 C CD1 . LEU   C 1 213 ? 1.930   -10.739 36.625  1.00 20.26 ? 192 LEU   C CD1 1 
ATOM   5095 C CD2 . LEU   C 1 213 ? 2.661   -13.126 36.318  1.00 19.34 ? 192 LEU   C CD2 1 
ATOM   5096 N N   . ALA   C 1 214 ? -2.555  -14.336 35.003  1.00 23.34 ? 193 ALA   C N   1 
ATOM   5097 C CA  . ALA   C 1 214 ? -3.931  -14.689 35.338  1.00 25.17 ? 193 ALA   C CA  1 
ATOM   5098 C C   . ALA   C 1 214 ? -4.011  -16.051 36.026  1.00 30.22 ? 193 ALA   C C   1 
ATOM   5099 O O   . ALA   C 1 214 ? -4.783  -16.215 36.973  1.00 31.22 ? 193 ALA   C O   1 
ATOM   5100 C CB  . ALA   C 1 214 ? -4.795  -14.654 34.103  1.00 25.93 ? 193 ALA   C CB  1 
ATOM   5101 N N   . PRO   C 1 215 ? -3.247  -17.081 35.595  1.00 33.47 ? 194 PRO   C N   1 
ATOM   5102 C CA  . PRO   C 1 215 ? -3.242  -18.359 36.318  1.00 35.79 ? 194 PRO   C CA  1 
ATOM   5103 C C   . PRO   C 1 215 ? -2.839  -18.266 37.795  1.00 40.60 ? 194 PRO   C C   1 
ATOM   5104 O O   . PRO   C 1 215 ? -3.209  -19.132 38.584  1.00 45.20 ? 194 PRO   C O   1 
ATOM   5105 C CB  . PRO   C 1 215 ? -2.288  -19.263 35.479  1.00 39.77 ? 194 PRO   C CB  1 
ATOM   5106 C CG  . PRO   C 1 215 ? -2.234  -18.602 34.096  1.00 38.25 ? 194 PRO   C CG  1 
ATOM   5107 C CD  . PRO   C 1 215 ? -2.382  -17.103 34.396  1.00 34.28 ? 194 PRO   C CD  1 
ATOM   5108 N N   . TYR   C 1 216 ? -2.118  -17.207 38.191  1.00 35.79 ? 195 TYR   C N   1 
ATOM   5109 C CA  . TYR   C 1 216 ? -1.701  -17.050 39.576  1.00 35.41 ? 195 TYR   C CA  1 
ATOM   5110 C C   . TYR   C 1 216 ? -2.691  -16.178 40.346  1.00 37.29 ? 195 TYR   C C   1 
ATOM   5111 O O   . TYR   C 1 216 ? -2.420  -15.809 41.482  1.00 36.73 ? 195 TYR   C O   1 
ATOM   5112 C CB  . TYR   C 1 216 ? -0.348  -16.334 39.663  1.00 36.34 ? 195 TYR   C CB  1 
ATOM   5113 C CG  . TYR   C 1 216 ? 0.765   -17.075 38.948  0.70 38.07 ? 195 TYR   C CG  1 
ATOM   5114 C CD1 . TYR   C 1 216 ? 0.954   -16.930 37.583  0.70 37.40 ? 195 TYR   C CD1 1 
ATOM   5115 C CD2 . TYR   C 1 216 ? 1.594   -17.951 39.635  0.70 42.23 ? 195 TYR   C CD2 1 
ATOM   5116 C CE1 . TYR   C 1 216 ? 1.953   -17.614 36.917  0.70 39.33 ? 195 TYR   C CE1 1 
ATOM   5117 C CE2 . TYR   C 1 216 ? 2.605   -18.635 38.981  0.70 45.35 ? 195 TYR   C CE2 1 
ATOM   5118 C CZ  . TYR   C 1 216 ? 2.776   -18.476 37.617  0.70 42.81 ? 195 TYR   C CZ  1 
ATOM   5119 O OH  . TYR   C 1 216 ? 3.755   -19.153 36.953  0.70 41.90 ? 195 TYR   C OH  1 
ATOM   5120 N N   . GLY   C 1 217 ? -3.782  -15.758 39.699  1.00 33.95 ? 196 GLY   C N   1 
ATOM   5121 C CA  . GLY   C 1 217 ? -4.770  -14.901 40.334  1.00 28.30 ? 196 GLY   C CA  1 
ATOM   5122 C C   . GLY   C 1 217 ? -4.297  -13.447 40.456  1.00 28.66 ? 196 GLY   C C   1 
ATOM   5123 O O   . GLY   C 1 217 ? -4.922  -12.670 41.150  1.00 31.58 ? 196 GLY   C O   1 
ATOM   5124 N N   . ILE   C 1 218 ? -3.217  -13.052 39.761  1.00 22.85 ? 197 ILE   C N   1 
ATOM   5125 C CA  . ILE   C 1 218 ? -2.823  -11.644 39.766  1.00 22.15 ? 197 ILE   C CA  1 
ATOM   5126 C C   . ILE   C 1 218 ? -3.484  -10.955 38.568  1.00 23.22 ? 197 ILE   C C   1 
ATOM   5127 O O   . ILE   C 1 218 ? -3.232  -11.330 37.417  1.00 23.03 ? 197 ILE   C O   1 
ATOM   5128 C CB  . ILE   C 1 218 ? -1.296  -11.505 39.715  1.00 24.26 ? 197 ILE   C CB  1 
ATOM   5129 C CG1 . ILE   C 1 218 ? -0.627  -12.285 40.885  1.00 23.91 ? 197 ILE   C CG1 1 
ATOM   5130 C CG2 . ILE   C 1 218 ? -0.889  -10.031 39.765  1.00 23.76 ? 197 ILE   C CG2 1 
ATOM   5131 C CD1 . ILE   C 1 218 ? 0.853   -12.554 40.649  1.00 24.27 ? 197 ILE   C CD1 1 
ATOM   5132 N N   . ARG   C 1 219 ? -4.316  -9.947  38.861  1.00 22.35 ? 198 ARG   C N   1 
ATOM   5133 C CA  . ARG   C 1 219 ? -4.929  -9.113  37.839  1.00 21.35 ? 198 ARG   C CA  1 
ATOM   5134 C C   . ARG   C 1 219 ? -3.989  -7.972  37.483  1.00 20.59 ? 198 ARG   C C   1 
ATOM   5135 O O   . ARG   C 1 219 ? -3.265  -7.478  38.338  1.00 20.36 ? 198 ARG   C O   1 
ATOM   5136 C CB  . ARG   C 1 219 ? -6.274  -8.560  38.325  1.00 18.89 ? 198 ARG   C CB  1 
ATOM   5137 C CG  . ARG   C 1 219 ? -7.207  -9.751  38.540  1.00 19.56 ? 198 ARG   C CG  1 
ATOM   5138 C CD  . ARG   C 1 219 ? -8.592  -9.353  39.102  1.00 21.18 ? 198 ARG   C CD  1 
ATOM   5139 N NE  . ARG   C 1 219 ? -8.475  -8.573  40.342  1.00 22.50 ? 198 ARG   C NE  1 
ATOM   5140 C CZ  . ARG   C 1 219 ? -8.517  -7.240  40.411  1.00 22.91 ? 198 ARG   C CZ  1 
ATOM   5141 N NH1 . ARG   C 1 219 ? -8.766  -6.500  39.327  1.00 21.35 ? 198 ARG   C NH1 1 
ATOM   5142 N NH2 . ARG   C 1 219 ? -8.305  -6.635  41.567  1.00 22.77 ? 198 ARG   C NH2 1 
ATOM   5143 N N   . VAL   C 1 220 ? -4.036  -7.545  36.209  1.00 19.65 ? 199 VAL   C N   1 
ATOM   5144 C CA  . VAL   C 1 220 ? -3.168  -6.484  35.719  1.00 18.41 ? 199 VAL   C CA  1 
ATOM   5145 C C   . VAL   C 1 220 ? -4.030  -5.557  34.869  1.00 18.51 ? 199 VAL   C C   1 
ATOM   5146 O O   . VAL   C 1 220 ? -4.554  -5.988  33.839  1.00 18.82 ? 199 VAL   C O   1 
ATOM   5147 C CB  . VAL   C 1 220 ? -1.975  -7.029  34.909  1.00 18.28 ? 199 VAL   C CB  1 
ATOM   5148 C CG1 . VAL   C 1 220 ? -1.040  -5.876  34.561  1.00 18.69 ? 199 VAL   C CG1 1 
ATOM   5149 C CG2 . VAL   C 1 220 ? -1.197  -8.125  35.683  1.00 20.15 ? 199 VAL   C CG2 1 
ATOM   5150 N N   . ASN   C 1 221 ? -4.143  -4.280  35.278  1.00 18.01 ? 200 ASN   C N   1 
ATOM   5151 C CA  . ASN   C 1 221 ? -5.045  -3.338  34.634  1.00 18.31 ? 200 ASN   C CA  1 
ATOM   5152 C C   . ASN   C 1 221 ? -4.364  -1.982  34.527  1.00 17.81 ? 200 ASN   C C   1 
ATOM   5153 O O   . ASN   C 1 221 ? -3.271  -1.775  35.079  1.00 17.61 ? 200 ASN   C O   1 
ATOM   5154 C CB  . ASN   C 1 221 ? -6.356  -3.149  35.404  1.00 17.13 ? 200 ASN   C CB  1 
ATOM   5155 C CG  . ASN   C 1 221 ? -7.161  -4.428  35.381  1.00 17.50 ? 200 ASN   C CG  1 
ATOM   5156 O OD1 . ASN   C 1 221 ? -7.618  -4.889  34.322  1.00 20.02 ? 200 ASN   C OD1 1 
ATOM   5157 N ND2 . ASN   C 1 221 ? -7.253  -5.080  36.532  1.00 18.92 ? 200 ASN   C ND2 1 
ATOM   5158 N N   . GLY   C 1 222 ? -5.034  -1.069  33.817  1.00 18.64 ? 201 GLY   C N   1 
ATOM   5159 C CA  . GLY   C 1 222 ? -4.453  0.246   33.586  1.00 16.31 ? 201 GLY   C CA  1 
ATOM   5160 C C   . GLY   C 1 222 ? -5.501  1.311   33.878  1.00 17.04 ? 201 GLY   C C   1 
ATOM   5161 O O   . GLY   C 1 222 ? -6.696  1.071   33.763  1.00 17.36 ? 201 GLY   C O   1 
ATOM   5162 N N   . VAL   C 1 223 ? -5.016  2.510   34.201  1.00 17.96 ? 202 VAL   C N   1 
ATOM   5163 C CA  . VAL   C 1 223 ? -5.845  3.695   34.285  1.00 18.22 ? 202 VAL   C CA  1 
ATOM   5164 C C   . VAL   C 1 223 ? -5.141  4.720   33.400  1.00 18.85 ? 202 VAL   C C   1 
ATOM   5165 O O   . VAL   C 1 223 ? -3.927  4.933   33.521  1.00 18.80 ? 202 VAL   C O   1 
ATOM   5166 C CB  . VAL   C 1 223 ? -5.925  4.199   35.742  1.00 18.85 ? 202 VAL   C CB  1 
ATOM   5167 C CG1 . VAL   C 1 223 ? -6.593  5.580   35.832  1.00 20.16 ? 202 VAL   C CG1 1 
ATOM   5168 C CG2 . VAL   C 1 223 ? -6.701  3.224   36.621  1.00 19.46 ? 202 VAL   C CG2 1 
ATOM   5169 N N   . ALA   C 1 224 ? -5.914  5.344   32.499  1.00 19.74 ? 203 ALA   C N   1 
ATOM   5170 C CA  . ALA   C 1 224 ? -5.341  6.207   31.482  1.00 18.83 ? 203 ALA   C CA  1 
ATOM   5171 C C   . ALA   C 1 224 ? -5.929  7.609   31.680  1.00 20.44 ? 203 ALA   C C   1 
ATOM   5172 O O   . ALA   C 1 224 ? -7.038  7.890   31.229  1.00 20.56 ? 203 ALA   C O   1 
ATOM   5173 C CB  . ALA   C 1 224 ? -5.681  5.640   30.082  1.00 16.99 ? 203 ALA   C CB  1 
ATOM   5174 N N   . PRO   C 1 225 ? -5.223  8.524   32.386  1.00 21.48 ? 204 PRO   C N   1 
ATOM   5175 C CA  . PRO   C 1 225 ? -5.668  9.910   32.491  1.00 22.06 ? 204 PRO   C CA  1 
ATOM   5176 C C   . PRO   C 1 225 ? -5.571  10.620  31.153  1.00 23.66 ? 204 PRO   C C   1 
ATOM   5177 O O   . PRO   C 1 225 ? -4.690  10.306  30.349  1.00 24.03 ? 204 PRO   C O   1 
ATOM   5178 C CB  . PRO   C 1 225 ? -4.688  10.541  33.507  1.00 21.00 ? 204 PRO   C CB  1 
ATOM   5179 C CG  . PRO   C 1 225 ? -4.083  9.349   34.246  1.00 22.74 ? 204 PRO   C CG  1 
ATOM   5180 C CD  . PRO   C 1 225 ? -3.995  8.249   33.174  1.00 21.71 ? 204 PRO   C CD  1 
ATOM   5181 N N   . GLY   C 1 226 ? -6.400  11.663  30.991  1.00 22.69 ? 205 GLY   C N   1 
ATOM   5182 C CA  . GLY   C 1 226 ? -6.225  12.590  29.883  1.00 24.74 ? 205 GLY   C CA  1 
ATOM   5183 C C   . GLY   C 1 226 ? -5.414  13.805  30.322  1.00 29.95 ? 205 GLY   C C   1 
ATOM   5184 O O   . GLY   C 1 226 ? -4.183  13.834  30.245  1.00 35.17 ? 205 GLY   C O   1 
ATOM   5185 N N   . VAL   C 1 227 ? -6.126  14.832  30.762  1.00 28.03 ? 206 VAL   C N   1 
ATOM   5186 C CA  . VAL   C 1 227 ? -5.453  15.904  31.460  1.00 29.65 ? 206 VAL   C CA  1 
ATOM   5187 C C   . VAL   C 1 227 ? -5.908  15.867  32.918  1.00 32.13 ? 206 VAL   C C   1 
ATOM   5188 O O   . VAL   C 1 227 ? -7.101  15.897  33.253  1.00 29.40 ? 206 VAL   C O   1 
ATOM   5189 C CB  . VAL   C 1 227 ? -5.431  17.291  30.790  1.00 34.48 ? 206 VAL   C CB  1 
ATOM   5190 C CG1 . VAL   C 1 227 ? -4.806  17.170  29.406  1.00 35.21 ? 206 VAL   C CG1 1 
ATOM   5191 C CG2 . VAL   C 1 227 ? -6.805  17.925  30.676  1.00 33.47 ? 206 VAL   C CG2 1 
ATOM   5192 N N   . SER   C 1 228 ? -4.914  15.654  33.777  1.00 31.85 ? 207 SER   C N   1 
ATOM   5193 C CA  . SER   C 1 228 ? -5.148  15.704  35.202  1.00 33.82 ? 207 SER   C CA  1 
ATOM   5194 C C   . SER   C 1 228 ? -4.281  16.859  35.677  1.00 38.28 ? 207 SER   C C   1 
ATOM   5195 O O   . SER   C 1 228 ? -4.106  17.820  34.926  1.00 39.34 ? 207 SER   C O   1 
ATOM   5196 C CB  . SER   C 1 228 ? -4.869  14.352  35.865  1.00 28.35 ? 207 SER   C CB  1 
ATOM   5197 O OG  . SER   C 1 228 ? -5.204  14.365  37.259  1.00 31.18 ? 207 SER   C OG  1 
ATOM   5198 N N   . LEU   C 1 229 ? -3.739  16.779  36.889  1.00 41.08 ? 208 LEU   C N   1 
ATOM   5199 C CA  . LEU   C 1 229 ? -2.961  17.899  37.389  1.00 42.47 ? 208 LEU   C CA  1 
ATOM   5200 C C   . LEU   C 1 229 ? -1.945  18.274  36.320  1.00 43.16 ? 208 LEU   C C   1 
ATOM   5201 O O   . LEU   C 1 229 ? -1.226  17.411  35.806  1.00 42.51 ? 208 LEU   C O   1 
ATOM   5202 C CB  . LEU   C 1 229 ? -2.281  17.524  38.702  1.00 42.51 ? 208 LEU   C CB  1 
ATOM   5203 C CG  . LEU   C 1 229 ? -3.217  17.190  39.869  1.00 41.54 ? 208 LEU   C CG  1 
ATOM   5204 C CD1 . LEU   C 1 229 ? -2.321  16.999  41.082  1.00 41.04 ? 208 LEU   C CD1 1 
ATOM   5205 C CD2 . LEU   C 1 229 ? -4.244  18.307  40.118  1.00 42.98 ? 208 LEU   C CD2 1 
ATOM   5206 N N   . LEU   C 1 230 ? -1.933  19.557  35.957  1.00 35.84 ? 209 LEU   C N   1 
ATOM   5207 C CA  . LEU   C 1 230 ? -1.025  20.003  34.909  1.00 44.71 ? 209 LEU   C CA  1 
ATOM   5208 C C   . LEU   C 1 230 ? 0.395   20.201  35.457  1.00 47.09 ? 209 LEU   C C   1 
ATOM   5209 O O   . LEU   C 1 230 ? 0.567   20.365  36.662  1.00 45.71 ? 209 LEU   C O   1 
ATOM   5210 C CB  . LEU   C 1 230 ? -1.665  21.245  34.291  1.00 42.62 ? 209 LEU   C CB  1 
ATOM   5211 C CG  . LEU   C 1 230 ? -2.950  20.921  33.515  1.00 45.65 ? 209 LEU   C CG  1 
ATOM   5212 C CD1 . LEU   C 1 230 ? -3.910  22.071  33.242  1.00 47.48 ? 209 LEU   C CD1 1 
ATOM   5213 C CD2 . LEU   C 1 230 ? -2.611  20.162  32.226  1.00 41.34 ? 209 LEU   C CD2 1 
ATOM   5214 N N   . PRO   C 1 231 ? 1.468   20.124  34.622  1.00 57.94 ? 210 PRO   C N   1 
ATOM   5215 C CA  . PRO   C 1 231 ? 2.831   20.393  35.101  1.00 60.20 ? 210 PRO   C CA  1 
ATOM   5216 C C   . PRO   C 1 231 ? 2.870   21.671  35.945  1.00 61.91 ? 210 PRO   C C   1 
ATOM   5217 O O   . PRO   C 1 231 ? 2.292   22.693  35.561  1.00 55.47 ? 210 PRO   C O   1 
ATOM   5218 C CB  . PRO   C 1 231 ? 3.682   20.510  33.808  1.00 61.57 ? 210 PRO   C CB  1 
ATOM   5219 C CG  . PRO   C 1 231 ? 2.911   19.719  32.764  1.00 58.09 ? 210 PRO   C CG  1 
ATOM   5220 C CD  . PRO   C 1 231 ? 1.438   19.759  33.191  1.00 59.41 ? 210 PRO   C CD  1 
ATOM   5221 N N   . VAL   C 1 232 ? 3.549   21.611  37.099  1.00 57.68 ? 211 VAL   C N   1 
ATOM   5222 C CA  . VAL   C 1 232 ? 3.587   22.752  38.007  1.00 61.08 ? 211 VAL   C CA  1 
ATOM   5223 C C   . VAL   C 1 232 ? 4.233   23.956  37.307  1.00 60.36 ? 211 VAL   C C   1 
ATOM   5224 O O   . VAL   C 1 232 ? 3.864   25.102  37.573  1.00 61.75 ? 211 VAL   C O   1 
ATOM   5225 C CB  . VAL   C 1 232 ? 4.252   22.425  39.361  1.00 57.84 ? 211 VAL   C CB  1 
ATOM   5226 N N   . ALA   C 1 233 ? 5.147   23.672  36.364  1.00 50.34 ? 212 ALA   C N   1 
ATOM   5227 C CA  . ALA   C 1 233 ? 5.946   24.675  35.679  1.00 55.76 ? 212 ALA   C CA  1 
ATOM   5228 C C   . ALA   C 1 233 ? 5.231   25.252  34.451  1.00 55.83 ? 212 ALA   C C   1 
ATOM   5229 O O   . ALA   C 1 233 ? 5.657   26.268  33.903  1.00 51.71 ? 212 ALA   C O   1 
ATOM   5230 C CB  . ALA   C 1 233 ? 7.301   24.085  35.320  1.00 56.12 ? 212 ALA   C CB  1 
ATOM   5231 N N   . MET   C 1 234 ? 4.163   24.591  33.989  1.00 59.84 ? 213 MET   C N   1 
ATOM   5232 C CA  . MET   C 1 234 ? 3.366   25.114  32.885  1.00 55.39 ? 213 MET   C CA  1 
ATOM   5233 C C   . MET   C 1 234 ? 2.603   26.345  33.375  1.00 52.13 ? 213 MET   C C   1 
ATOM   5234 O O   . MET   C 1 234 ? 2.039   26.342  34.469  1.00 53.68 ? 213 MET   C O   1 
ATOM   5235 C CB  . MET   C 1 234 ? 2.379   24.058  32.377  1.00 50.87 ? 213 MET   C CB  1 
ATOM   5236 C CG  . MET   C 1 234 ? 1.382   24.557  31.350  1.00 55.10 ? 213 MET   C CG  1 
ATOM   5237 S SD  . MET   C 1 234 ? 0.154   23.310  30.903  1.00 59.35 ? 213 MET   C SD  1 
ATOM   5238 C CE  . MET   C 1 234 ? 1.157   21.993  30.195  1.00 67.72 ? 213 MET   C CE  1 
ATOM   5239 N N   . GLY   C 1 235 ? 2.604   27.399  32.555  1.00 56.11 ? 214 GLY   C N   1 
ATOM   5240 C CA  . GLY   C 1 235 ? 1.905   28.631  32.873  1.00 55.24 ? 214 GLY   C CA  1 
ATOM   5241 C C   . GLY   C 1 235 ? 0.394   28.424  32.858  1.00 54.06 ? 214 GLY   C C   1 
ATOM   5242 O O   . GLY   C 1 235 ? -0.120  27.585  32.110  1.00 53.15 ? 214 GLY   C O   1 
ATOM   5243 N N   . GLU   C 1 236 ? -0.290  29.239  33.670  1.00 53.83 ? 215 GLU   C N   1 
ATOM   5244 C CA  . GLU   C 1 236 ? -1.737  29.229  33.833  1.00 56.12 ? 215 GLU   C CA  1 
ATOM   5245 C C   . GLU   C 1 236 ? -2.473  29.374  32.495  1.00 50.55 ? 215 GLU   C C   1 
ATOM   5246 O O   . GLU   C 1 236 ? -3.564  28.811  32.344  1.00 46.29 ? 215 GLU   C O   1 
ATOM   5247 C CB  . GLU   C 1 236 ? -2.191  30.252  34.883  1.00 52.55 ? 215 GLU   C CB  1 
ATOM   5248 C CG  . GLU   C 1 236 ? -3.448  29.804  35.622  1.00 58.81 ? 215 GLU   C CG  1 
ATOM   5249 C CD  . GLU   C 1 236 ? -3.274  28.436  36.279  1.00 64.76 ? 215 GLU   C CD  1 
ATOM   5250 O OE1 . GLU   C 1 236 ? -2.126  28.051  36.604  1.00 62.14 ? 215 GLU   C OE1 1 
ATOM   5251 O OE2 . GLU   C 1 236 ? -4.286  27.724  36.433  1.00 63.69 ? 215 GLU   C OE2 1 
ATOM   5252 N N   . GLU   C 1 237 ? -1.893  30.130  31.542  1.00 49.80 ? 216 GLU   C N   1 
ATOM   5253 C CA  . GLU   C 1 237 ? -2.519  30.357  30.241  1.00 50.70 ? 216 GLU   C CA  1 
ATOM   5254 C C   . GLU   C 1 237 ? -2.512  29.075  29.396  1.00 51.64 ? 216 GLU   C C   1 
ATOM   5255 O O   . GLU   C 1 237 ? -3.532  28.725  28.783  1.00 47.74 ? 216 GLU   C O   1 
ATOM   5256 C CB  . GLU   C 1 237 ? -1.899  31.526  29.476  1.00 52.00 ? 216 GLU   C CB  1 
ATOM   5257 N N   . GLU   C 1 238 ? -1.371  28.362  29.371  1.00 44.87 ? 217 GLU   C N   1 
ATOM   5258 C CA  . GLU   C 1 238 ? -1.294  27.094  28.643  1.00 47.26 ? 217 GLU   C CA  1 
ATOM   5259 C C   . GLU   C 1 238 ? -2.216  26.051  29.282  1.00 47.61 ? 217 GLU   C C   1 
ATOM   5260 O O   . GLU   C 1 238 ? -2.809  25.235  28.576  1.00 55.12 ? 217 GLU   C O   1 
ATOM   5261 C CB  . GLU   C 1 238 ? 0.111   26.506  28.446  1.00 44.20 ? 217 GLU   C CB  1 
ATOM   5262 C CG  . GLU   C 1 238 ? 0.211   25.597  27.223  0.60 44.91 ? 217 GLU   C CG  1 
ATOM   5263 N N   . LYS   C 1 239 ? -2.313  26.075  30.620  1.00 50.58 ? 218 LYS   C N   1 
ATOM   5264 C CA  . LYS   C 1 239 ? -3.189  25.177  31.361  1.00 50.00 ? 218 LYS   C CA  1 
ATOM   5265 C C   . LYS   C 1 239 ? -4.641  25.388  30.920  1.00 46.83 ? 218 LYS   C C   1 
ATOM   5266 O O   . LYS   C 1 239 ? -5.367  24.426  30.683  1.00 39.98 ? 218 LYS   C O   1 
ATOM   5267 C CB  . LYS   C 1 239 ? -3.046  25.347  32.878  1.00 49.04 ? 218 LYS   C CB  1 
ATOM   5268 C CG  . LYS   C 1 239 ? -1.724  24.886  33.484  1.00 50.00 ? 218 LYS   C CG  1 
ATOM   5269 C CD  . LYS   C 1 239 ? -1.800  24.882  35.003  1.00 46.65 ? 218 LYS   C CD  1 
ATOM   5270 C CE  . LYS   C 1 239 ? -0.472  24.606  35.642  1.00 47.58 ? 218 LYS   C CE  1 
ATOM   5271 N NZ  . LYS   C 1 239 ? -0.522  25.032  37.041  1.00 47.77 ? 218 LYS   C NZ  1 
ATOM   5272 N N   . ASP   C 1 240 ? -5.053  26.653  30.799  1.00 45.81 ? 219 ASP   C N   1 
ATOM   5273 C CA  . ASP   C 1 240 ? -6.417  27.000  30.420  1.00 45.77 ? 219 ASP   C CA  1 
ATOM   5274 C C   . ASP   C 1 240 ? -6.728  26.462  29.013  1.00 45.11 ? 219 ASP   C C   1 
ATOM   5275 O O   . ASP   C 1 240 ? -7.862  26.058  28.730  1.00 42.58 ? 219 ASP   C O   1 
ATOM   5276 C CB  . ASP   C 1 240 ? -6.708  28.469  30.713  1.00 47.35 ? 219 ASP   C CB  1 
ATOM   5277 C CG  . ASP   C 1 240 ? -7.007  28.842  32.166  1.00 59.10 ? 219 ASP   C CG  1 
ATOM   5278 O OD1 . ASP   C 1 240 ? -7.492  27.970  32.928  1.00 66.16 ? 219 ASP   C OD1 1 
ATOM   5279 O OD2 . ASP   C 1 240 ? -6.764  30.011  32.539  1.00 55.25 ? 219 ASP   C OD2 1 
ATOM   5280 N N   . LYS   C 1 241 ? -5.710  26.430  28.140  1.00 45.32 ? 220 LYS   C N   1 
ATOM   5281 C CA  . LYS   C 1 241 ? -5.868  25.940  26.774  1.00 47.39 ? 220 LYS   C CA  1 
ATOM   5282 C C   . LYS   C 1 241 ? -6.239  24.451  26.786  1.00 45.56 ? 220 LYS   C C   1 
ATOM   5283 O O   . LYS   C 1 241 ? -7.084  24.014  26.006  1.00 40.73 ? 220 LYS   C O   1 
ATOM   5284 C CB  . LYS   C 1 241 ? -4.635  26.257  25.916  1.00 50.63 ? 220 LYS   C CB  1 
ATOM   5285 C CG  . LYS   C 1 241 ? -4.800  26.130  24.405  0.60 50.52 ? 220 LYS   C CG  1 
ATOM   5286 N N   . TRP   C 1 242 ? -5.615  23.670  27.681  1.00 39.85 ? 221 TRP   C N   1 
ATOM   5287 C CA  . TRP   C 1 242 ? -5.954  22.255  27.773  1.00 41.70 ? 221 TRP   C CA  1 
ATOM   5288 C C   . TRP   C 1 242 ? -7.328  22.052  28.420  1.00 39.06 ? 221 TRP   C C   1 
ATOM   5289 O O   . TRP   C 1 242 ? -8.107  21.220  27.954  1.00 35.10 ? 221 TRP   C O   1 
ATOM   5290 C CB  . TRP   C 1 242 ? -4.863  21.457  28.498  1.00 42.26 ? 221 TRP   C CB  1 
ATOM   5291 C CG  . TRP   C 1 242 ? -3.685  21.156  27.612  1.00 47.82 ? 221 TRP   C CG  1 
ATOM   5292 C CD1 . TRP   C 1 242 ? -2.500  21.827  27.539  1.00 49.20 ? 221 TRP   C CD1 1 
ATOM   5293 C CD2 . TRP   C 1 242 ? -3.623  20.106  26.625  1.00 48.57 ? 221 TRP   C CD2 1 
ATOM   5294 N NE1 . TRP   C 1 242 ? -1.696  21.260  26.586  1.00 51.65 ? 221 TRP   C NE1 1 
ATOM   5295 C CE2 . TRP   C 1 242 ? -2.355  20.203  26.010  1.00 56.23 ? 221 TRP   C CE2 1 
ATOM   5296 C CE3 . TRP   C 1 242 ? -4.513  19.107  26.209  1.00 48.39 ? 221 TRP   C CE3 1 
ATOM   5297 C CZ2 . TRP   C 1 242 ? -1.956  19.324  25.003  1.00 56.69 ? 221 TRP   C CZ2 1 
ATOM   5298 C CZ3 . TRP   C 1 242 ? -4.120  18.247  25.207  1.00 50.79 ? 221 TRP   C CZ3 1 
ATOM   5299 C CH2 . TRP   C 1 242 ? -2.855  18.349  24.624  1.00 53.01 ? 221 TRP   C CH2 1 
ATOM   5300 N N   . ARG   C 1 243 ? -7.604  22.814  29.491  1.00 36.77 ? 222 ARG   C N   1 
ATOM   5301 C CA  . ARG   C 1 243 ? -8.851  22.715  30.234  1.00 34.77 ? 222 ARG   C CA  1 
ATOM   5302 C C   . ARG   C 1 243 ? -10.019 22.935  29.276  1.00 34.22 ? 222 ARG   C C   1 
ATOM   5303 O O   . ARG   C 1 243 ? -11.018 22.221  29.336  1.00 29.65 ? 222 ARG   C O   1 
ATOM   5304 C CB  . ARG   C 1 243 ? -8.880  23.773  31.346  1.00 37.07 ? 222 ARG   C CB  1 
ATOM   5305 C CG  . ARG   C 1 243 ? -7.888  23.455  32.455  1.00 38.31 ? 222 ARG   C CG  1 
ATOM   5306 C CD  . ARG   C 1 243 ? -7.868  24.546  33.530  1.00 42.96 ? 222 ARG   C CD  1 
ATOM   5307 N NE  . ARG   C 1 243 ? -7.110  24.147  34.726  1.00 43.02 ? 222 ARG   C NE  1 
ATOM   5308 C CZ  . ARG   C 1 243 ? -6.170  24.895  35.326  1.00 45.37 ? 222 ARG   C CZ  1 
ATOM   5309 N NH1 . ARG   C 1 243 ? -5.913  26.119  34.893  1.00 43.03 ? 222 ARG   C NH1 1 
ATOM   5310 N NH2 . ARG   C 1 243 ? -5.483  24.422  36.355  1.00 44.37 ? 222 ARG   C NH2 1 
ATOM   5311 N N   . ARG   C 1 244 ? -9.880  23.929  28.392  1.00 32.73 ? 223 ARG   C N   1 
ATOM   5312 C CA  . ARG   C 1 244 ? -10.934 24.300  27.442  1.00 37.31 ? 223 ARG   C CA  1 
ATOM   5313 C C   . ARG   C 1 244 ? -11.276 23.182  26.441  1.00 36.81 ? 223 ARG   C C   1 
ATOM   5314 O O   . ARG   C 1 244 ? -12.365 23.161  25.877  1.00 37.06 ? 223 ARG   C O   1 
ATOM   5315 C CB  . ARG   C 1 244 ? -10.648 25.626  26.722  1.00 41.89 ? 223 ARG   C CB  1 
ATOM   5316 C CG  . ARG   C 1 244 ? -11.319 26.787  27.451  0.60 47.16 ? 223 ARG   C CG  1 
ATOM   5317 C CD  . ARG   C 1 244 ? -11.130 28.173  26.839  0.60 44.83 ? 223 ARG   C CD  1 
ATOM   5318 N NE  . ARG   C 1 244 ? -9.718  28.468  26.565  0.60 45.76 ? 223 ARG   C NE  1 
ATOM   5319 C CZ  . ARG   C 1 244 ? -8.858  29.169  27.317  0.60 42.52 ? 223 ARG   C CZ  1 
ATOM   5320 N NH1 . ARG   C 1 244 ? -9.165  29.573  28.542  0.60 42.76 ? 223 ARG   C NH1 1 
ATOM   5321 N NH2 . ARG   C 1 244 ? -7.656  29.420  26.841  0.60 39.06 ? 223 ARG   C NH2 1 
ATOM   5322 N N   . LYS   C 1 245 ? -10.385 22.213  26.247  1.00 35.29 ? 224 LYS   C N   1 
ATOM   5323 C CA  . LYS   C 1 245 ? -10.632 21.159  25.271  1.00 32.19 ? 224 LYS   C CA  1 
ATOM   5324 C C   . LYS   C 1 245 ? -11.478 20.026  25.876  1.00 31.12 ? 224 LYS   C C   1 
ATOM   5325 O O   . LYS   C 1 245 ? -11.994 19.188  25.150  1.00 28.85 ? 224 LYS   C O   1 
ATOM   5326 C CB  . LYS   C 1 245 ? -9.286  20.609  24.792  1.00 36.75 ? 224 LYS   C CB  1 
ATOM   5327 C CG  . LYS   C 1 245 ? -8.221  21.546  24.172  1.00 39.79 ? 224 LYS   C CG  1 
ATOM   5328 C CD  . LYS   C 1 245 ? -6.900  20.781  24.005  1.00 43.45 ? 224 LYS   C CD  1 
ATOM   5329 C CE  . LYS   C 1 245 ? -5.618  21.529  23.671  1.00 43.55 ? 224 LYS   C CE  1 
ATOM   5330 N NZ  . LYS   C 1 245 ? -5.795  22.331  22.461  1.00 43.59 ? 224 LYS   C NZ  1 
ATOM   5331 N N   . VAL   C 1 246 ? -11.613 19.970  27.209  1.00 25.82 ? 225 VAL   C N   1 
ATOM   5332 C CA  . VAL   C 1 246 ? -12.184 18.794  27.848  1.00 25.58 ? 225 VAL   C CA  1 
ATOM   5333 C C   . VAL   C 1 246 ? -13.703 18.907  27.787  1.00 25.72 ? 225 VAL   C C   1 
ATOM   5334 O O   . VAL   C 1 246 ? -14.260 19.842  28.364  1.00 27.74 ? 225 VAL   C O   1 
ATOM   5335 C CB  . VAL   C 1 246 ? -11.713 18.606  29.313  1.00 25.30 ? 225 VAL   C CB  1 
ATOM   5336 C CG1 . VAL   C 1 246 ? -12.432 17.423  29.970  1.00 21.77 ? 225 VAL   C CG1 1 
ATOM   5337 C CG2 . VAL   C 1 246 ? -10.188 18.486  29.414  1.00 25.33 ? 225 VAL   C CG2 1 
ATOM   5338 N N   . PRO   C 1 247 ? -14.424 17.959  27.131  1.00 27.25 ? 226 PRO   C N   1 
ATOM   5339 C CA  . PRO   C 1 247 ? -15.879 18.066  27.024  1.00 25.10 ? 226 PRO   C CA  1 
ATOM   5340 C C   . PRO   C 1 247 ? -16.592 18.051  28.370  1.00 25.94 ? 226 PRO   C C   1 
ATOM   5341 O O   . PRO   C 1 247 ? -17.546 18.803  28.556  1.00 23.39 ? 226 PRO   C O   1 
ATOM   5342 C CB  . PRO   C 1 247 ? -16.284 16.865  26.152  1.00 26.65 ? 226 PRO   C CB  1 
ATOM   5343 C CG  . PRO   C 1 247 ? -15.004 16.574  25.363  1.00 26.61 ? 226 PRO   C CG  1 
ATOM   5344 C CD  . PRO   C 1 247 ? -13.879 16.798  26.383  1.00 24.18 ? 226 PRO   C CD  1 
ATOM   5345 N N   . LEU   C 1 248 ? -16.181 17.148  29.268  1.00 23.90 ? 227 LEU   C N   1 
ATOM   5346 C CA  . LEU   C 1 248 ? -16.879 17.013  30.533  1.00 27.38 ? 227 LEU   C CA  1 
ATOM   5347 C C   . LEU   C 1 248 ? -16.363 18.043  31.543  1.00 30.06 ? 227 LEU   C C   1 
ATOM   5348 O O   . LEU   C 1 248 ? -15.465 17.752  32.328  1.00 31.83 ? 227 LEU   C O   1 
ATOM   5349 C CB  . LEU   C 1 248 ? -16.778 15.585  31.056  1.00 24.93 ? 227 LEU   C CB  1 
ATOM   5350 C CG  . LEU   C 1 248 ? -17.741 15.227  32.195  1.00 26.61 ? 227 LEU   C CG  1 
ATOM   5351 C CD1 . LEU   C 1 248 ? -19.200 15.159  31.716  1.00 24.57 ? 227 LEU   C CD1 1 
ATOM   5352 C CD2 . LEU   C 1 248 ? -17.255 13.886  32.778  1.00 24.90 ? 227 LEU   C CD2 1 
ATOM   5353 N N   . GLY   C 1 249 ? -16.911 19.265  31.467  1.00 29.58 ? 228 GLY   C N   1 
ATOM   5354 C CA  . GLY   C 1 249 ? -16.758 20.285  32.500  1.00 32.36 ? 228 GLY   C CA  1 
ATOM   5355 C C   . GLY   C 1 249 ? -15.617 21.265  32.231  1.00 32.28 ? 228 GLY   C C   1 
ATOM   5356 O O   . GLY   C 1 249 ? -15.339 22.123  33.063  1.00 32.21 ? 228 GLY   C O   1 
ATOM   5357 N N   . ARG   C 1 250 ? -14.913 21.114  31.100  1.00 29.04 ? 229 ARG   C N   1 
ATOM   5358 C CA  . ARG   C 1 250 ? -13.864 22.061  30.717  1.00 32.20 ? 229 ARG   C CA  1 
ATOM   5359 C C   . ARG   C 1 250 ? -12.844 22.264  31.844  1.00 31.51 ? 229 ARG   C C   1 
ATOM   5360 O O   . ARG   C 1 250 ? -12.394 23.388  32.112  1.00 30.58 ? 229 ARG   C O   1 
ATOM   5361 C CB  . ARG   C 1 250 ? -14.460 23.390  30.215  1.00 34.63 ? 229 ARG   C CB  1 
ATOM   5362 C CG  . ARG   C 1 250 ? -15.532 23.229  29.149  0.60 35.80 ? 229 ARG   C CG  1 
ATOM   5363 C CD  . ARG   C 1 250 ? -15.024 23.438  27.743  0.60 37.79 ? 229 ARG   C CD  1 
ATOM   5364 N NE  . ARG   C 1 250 ? -16.014 22.923  26.789  0.60 41.46 ? 229 ARG   C NE  1 
ATOM   5365 C CZ  . ARG   C 1 250 ? -15.812 22.081  25.775  0.60 39.95 ? 229 ARG   C CZ  1 
ATOM   5366 N NH1 . ARG   C 1 250 ? -14.598 21.676  25.458  0.60 38.00 ? 229 ARG   C NH1 1 
ATOM   5367 N NH2 . ARG   C 1 250 ? -16.838 21.668  25.052  0.60 39.74 ? 229 ARG   C NH2 1 
ATOM   5368 N N   . ARG   C 1 251 ? -12.438 21.153  32.468  1.00 29.70 ? 230 ARG   C N   1 
ATOM   5369 C CA  . ARG   C 1 251 ? -11.453 21.169  33.536  1.00 30.92 ? 230 ARG   C CA  1 
ATOM   5370 C C   . ARG   C 1 251 ? -10.680 19.845  33.486  1.00 34.58 ? 230 ARG   C C   1 
ATOM   5371 O O   . ARG   C 1 251 ? -11.151 18.840  32.903  1.00 28.61 ? 230 ARG   C O   1 
ATOM   5372 C CB  . ARG   C 1 251 ? -12.169 21.354  34.889  1.00 29.70 ? 230 ARG   C CB  1 
ATOM   5373 C CG  . ARG   C 1 251 ? -13.214 20.276  35.148  1.00 32.21 ? 230 ARG   C CG  1 
ATOM   5374 C CD  . ARG   C 1 251 ? -14.036 20.307  36.426  0.60 36.63 ? 230 ARG   C CD  1 
ATOM   5375 N NE  . ARG   C 1 251 ? -15.300 20.954  36.060  0.60 39.70 ? 230 ARG   C NE  1 
ATOM   5376 C CZ  . ARG   C 1 251 ? -16.020 21.780  36.803  0.60 44.17 ? 230 ARG   C CZ  1 
ATOM   5377 N NH1 . ARG   C 1 251 ? -15.657 22.037  38.051  0.60 41.00 ? 230 ARG   C NH1 1 
ATOM   5378 N NH2 . ARG   C 1 251 ? -17.131 22.297  36.295  0.60 42.10 ? 230 ARG   C NH2 1 
ATOM   5379 N N   . GLU   C 1 252 ? -9.481  19.868  34.097  1.00 31.26 ? 231 GLU   C N   1 
ATOM   5380 C CA  . GLU   C 1 252 ? -8.663  18.677  34.260  1.00 29.15 ? 231 GLU   C CA  1 
ATOM   5381 C C   . GLU   C 1 252 ? -9.240  17.800  35.374  1.00 27.06 ? 231 GLU   C C   1 
ATOM   5382 O O   . GLU   C 1 252 ? -10.047 18.248  36.197  1.00 28.28 ? 231 GLU   C O   1 
ATOM   5383 C CB  . GLU   C 1 252 ? -7.207  19.107  34.473  1.00 31.42 ? 231 GLU   C CB  1 
ATOM   5384 C CG  . GLU   C 1 252 ? -6.901  19.567  35.897  1.00 37.02 ? 231 GLU   C CG  1 
ATOM   5385 C CD  . GLU   C 1 252 ? -7.093  21.061  36.113  1.00 45.64 ? 231 GLU   C CD  1 
ATOM   5386 O OE1 . GLU   C 1 252 ? -6.248  21.542  36.882  1.00 42.88 ? 231 GLU   C OE1 1 
ATOM   5387 O OE2 . GLU   C 1 252 ? -7.992  21.743  35.532  1.00 46.33 ? 231 GLU   C OE2 1 
ATOM   5388 N N   . ALA   C 1 253 ? -8.864  16.518  35.373  1.00 25.87 ? 232 ALA   C N   1 
ATOM   5389 C CA  . ALA   C 1 253 ? -9.211  15.655  36.489  1.00 28.54 ? 232 ALA   C CA  1 
ATOM   5390 C C   . ALA   C 1 253 ? -8.403  16.065  37.720  1.00 26.64 ? 232 ALA   C C   1 
ATOM   5391 O O   . ALA   C 1 253 ? -7.199  16.356  37.609  1.00 28.96 ? 232 ALA   C O   1 
ATOM   5392 C CB  . ALA   C 1 253 ? -8.890  14.211  36.147  1.00 25.57 ? 232 ALA   C CB  1 
ATOM   5393 N N   . SER   C 1 254 ? -9.040  15.951  38.888  1.00 25.29 ? 233 SER   C N   1 
ATOM   5394 C CA  . SER   C 1 254 ? -8.303  16.015  40.150  1.00 27.72 ? 233 SER   C CA  1 
ATOM   5395 C C   . SER   C 1 254 ? -7.506  14.723  40.313  1.00 28.07 ? 233 SER   C C   1 
ATOM   5396 O O   . SER   C 1 254 ? -7.831  13.707  39.694  1.00 28.07 ? 233 SER   C O   1 
ATOM   5397 C CB  . SER   C 1 254 ? -9.200  16.257  41.337  1.00 26.32 ? 233 SER   C CB  1 
ATOM   5398 O OG  . SER   C 1 254 ? -10.094 15.177  41.523  1.00 29.61 ? 233 SER   C OG  1 
ATOM   5399 N N   . ALA   C 1 255 ? -6.427  14.771  41.109  1.00 24.28 ? 234 ALA   C N   1 
ATOM   5400 C CA  . ALA   C 1 255 ? -5.666  13.548  41.352  1.00 24.82 ? 234 ALA   C CA  1 
ATOM   5401 C C   . ALA   C 1 255 ? -6.586  12.514  42.010  1.00 23.57 ? 234 ALA   C C   1 
ATOM   5402 O O   . ALA   C 1 255 ? -6.472  11.306  41.786  1.00 22.60 ? 234 ALA   C O   1 
ATOM   5403 C CB  . ALA   C 1 255 ? -4.456  13.869  42.241  1.00 24.52 ? 234 ALA   C CB  1 
ATOM   5404 N N   . GLU   C 1 256 ? -7.506  12.986  42.857  1.00 22.41 ? 235 GLU   C N   1 
ATOM   5405 C CA  . GLU   C 1 256 ? -8.435  12.091  43.539  1.00 24.07 ? 235 GLU   C CA  1 
ATOM   5406 C C   . GLU   C 1 256 ? -9.297  11.303  42.540  1.00 22.90 ? 235 GLU   C C   1 
ATOM   5407 O O   . GLU   C 1 256 ? -9.609  10.122  42.747  1.00 21.97 ? 235 GLU   C O   1 
ATOM   5408 C CB  . GLU   C 1 256 ? -9.225  12.917  44.569  1.00 26.78 ? 235 GLU   C CB  1 
ATOM   5409 C CG  . GLU   C 1 256 ? -10.317 12.104  45.249  1.00 37.45 ? 235 GLU   C CG  1 
ATOM   5410 C CD  . GLU   C 1 256 ? -11.253 12.788  46.247  1.00 42.95 ? 235 GLU   C CD  1 
ATOM   5411 O OE1 . GLU   C 1 256 ? -12.195 12.091  46.685  1.00 37.78 ? 235 GLU   C OE1 1 
ATOM   5412 O OE2 . GLU   C 1 256 ? -11.046 13.983  46.581  1.00 40.15 ? 235 GLU   C OE2 1 
ATOM   5413 N N   . GLN   C 1 257 ? -9.728  11.956  41.460  1.00 22.77 ? 236 GLN   C N   1 
ATOM   5414 C CA  . GLN   C 1 257 ? -10.550 11.255  40.473  1.00 24.95 ? 236 GLN   C CA  1 
ATOM   5415 C C   . GLN   C 1 257 ? -9.738  10.151  39.788  1.00 22.71 ? 236 GLN   C C   1 
ATOM   5416 O O   . GLN   C 1 257 ? -10.280 9.092   39.468  1.00 22.79 ? 236 GLN   C O   1 
ATOM   5417 C CB  . GLN   C 1 257 ? -11.083 12.278  39.471  1.00 26.32 ? 236 GLN   C CB  1 
ATOM   5418 C CG  . GLN   C 1 257 ? -12.154 13.158  40.100  1.00 25.59 ? 236 GLN   C CG  1 
ATOM   5419 C CD  . GLN   C 1 257 ? -12.595 14.330  39.248  1.00 28.20 ? 236 GLN   C CD  1 
ATOM   5420 O OE1 . GLN   C 1 257 ? -11.816 15.005  38.558  1.00 27.75 ? 236 GLN   C OE1 1 
ATOM   5421 N NE2 . GLN   C 1 257 ? -13.870 14.635  39.400  1.00 27.05 ? 236 GLN   C NE2 1 
ATOM   5422 N N   . ILE   C 1 258 ? -8.440  10.395  39.564  1.00 22.15 ? 237 ILE   C N   1 
ATOM   5423 C CA  . ILE   C 1 258 ? -7.603  9.343   38.985  1.00 21.72 ? 237 ILE   C CA  1 
ATOM   5424 C C   . ILE   C 1 258 ? -7.477  8.180   39.972  1.00 21.19 ? 237 ILE   C C   1 
ATOM   5425 O O   . ILE   C 1 258 ? -7.643  7.019   39.596  1.00 21.94 ? 237 ILE   C O   1 
ATOM   5426 C CB  . ILE   C 1 258 ? -6.230  9.863   38.525  1.00 22.29 ? 237 ILE   C CB  1 
ATOM   5427 C CG1 . ILE   C 1 258 ? -6.341  11.027  37.532  1.00 25.09 ? 237 ILE   C CG1 1 
ATOM   5428 C CG2 . ILE   C 1 258 ? -5.384  8.715   37.976  1.00 21.28 ? 237 ILE   C CG2 1 
ATOM   5429 C CD1 . ILE   C 1 258 ? -7.207  10.732  36.316  1.00 26.70 ? 237 ILE   C CD1 1 
ATOM   5430 N N   . ALA   C 1 259 ? -7.178  8.507   41.238  1.00 20.48 ? 238 ALA   C N   1 
ATOM   5431 C CA  . ALA   C 1 259 ? -7.046  7.529   42.306  1.00 21.76 ? 238 ALA   C CA  1 
ATOM   5432 C C   . ALA   C 1 259 ? -8.323  6.711   42.486  1.00 21.64 ? 238 ALA   C C   1 
ATOM   5433 O O   . ALA   C 1 259 ? -8.264  5.515   42.811  1.00 22.10 ? 238 ALA   C O   1 
ATOM   5434 C CB  . ALA   C 1 259 ? -6.664  8.238   43.611  1.00 22.88 ? 238 ALA   C CB  1 
ATOM   5435 N N   . ASP   C 1 260 ? -9.488  7.358   42.333  1.00 20.49 ? 239 ASP   C N   1 
ATOM   5436 C CA  . ASP   C 1 260 ? -10.763 6.627   42.391  1.00 22.78 ? 239 ASP   C CA  1 
ATOM   5437 C C   . ASP   C 1 260 ? -10.776 5.427   41.428  1.00 22.47 ? 239 ASP   C C   1 
ATOM   5438 O O   . ASP   C 1 260 ? -11.291 4.350   41.766  1.00 24.19 ? 239 ASP   C O   1 
ATOM   5439 C CB  . ASP   C 1 260 ? -11.976 7.511   42.083  1.00 22.04 ? 239 ASP   C CB  1 
ATOM   5440 C CG  . ASP   C 1 260 ? -12.405 8.458   43.205  1.00 28.57 ? 239 ASP   C CG  1 
ATOM   5441 O OD1 . ASP   C 1 260 ? -12.230 8.088   44.400  1.00 28.82 ? 239 ASP   C OD1 1 
ATOM   5442 O OD2 . ASP   C 1 260 ? -12.955 9.552   42.895  1.00 29.36 ? 239 ASP   C OD2 1 
ATOM   5443 N N   . ALA   C 1 261 ? -10.232 5.597   40.207  1.00 21.08 ? 240 ALA   C N   1 
ATOM   5444 C CA  . ALA   C 1 261 ? -10.329 4.481   39.265  1.00 20.49 ? 240 ALA   C CA  1 
ATOM   5445 C C   . ALA   C 1 261 ? -9.356  3.362   39.668  1.00 20.75 ? 240 ALA   C C   1 
ATOM   5446 O O   . ALA   C 1 261 ? -9.647  2.176   39.471  1.00 21.50 ? 240 ALA   C O   1 
ATOM   5447 C CB  . ALA   C 1 261 ? -10.060 4.952   37.846  1.00 20.54 ? 240 ALA   C CB  1 
ATOM   5448 N N   . VAL   C 1 262 ? -8.180  3.761   40.182  1.00 21.45 ? 241 VAL   C N   1 
ATOM   5449 C CA  . VAL   C 1 262 ? -7.187  2.827   40.710  1.00 22.97 ? 241 VAL   C CA  1 
ATOM   5450 C C   . VAL   C 1 262 ? -7.819  2.001   41.827  1.00 21.59 ? 241 VAL   C C   1 
ATOM   5451 O O   . VAL   C 1 262 ? -7.736  0.770   41.819  1.00 21.24 ? 241 VAL   C O   1 
ATOM   5452 C CB  . VAL   C 1 262 ? -5.906  3.526   41.211  1.00 22.36 ? 241 VAL   C CB  1 
ATOM   5453 C CG1 . VAL   C 1 262 ? -4.965  2.512   41.869  1.00 22.99 ? 241 VAL   C CG1 1 
ATOM   5454 C CG2 . VAL   C 1 262 ? -5.200  4.297   40.103  1.00 21.10 ? 241 VAL   C CG2 1 
ATOM   5455 N N   . ILE   C 1 263 ? -8.454  2.693   42.788  1.00 21.28 ? 242 ILE   C N   1 
ATOM   5456 C CA  . ILE   C 1 263 ? -9.123  2.039   43.910  1.00 23.26 ? 242 ILE   C CA  1 
ATOM   5457 C C   . ILE   C 1 263 ? -10.139 1.001   43.433  1.00 24.12 ? 242 ILE   C C   1 
ATOM   5458 O O   . ILE   C 1 263 ? -10.193 -0.099  43.993  1.00 22.11 ? 242 ILE   C O   1 
ATOM   5459 C CB  . ILE   C 1 263 ? -9.757  3.070   44.875  1.00 29.22 ? 242 ILE   C CB  1 
ATOM   5460 C CG1 . ILE   C 1 263 ? -8.681  3.775   45.701  1.00 35.21 ? 242 ILE   C CG1 1 
ATOM   5461 C CG2 . ILE   C 1 263 ? -10.850 2.460   45.764  1.00 28.88 ? 242 ILE   C CG2 1 
ATOM   5462 C CD1 . ILE   C 1 263 ? -7.717  2.850   46.422  1.00 36.33 ? 242 ILE   C CD1 1 
ATOM   5463 N N   . PHE   C 1 264 ? -10.945 1.359   42.423  1.00 23.58 ? 243 PHE   C N   1 
ATOM   5464 C CA  . PHE   C 1 264 ? -11.925 0.402   41.893  1.00 22.75 ? 243 PHE   C CA  1 
ATOM   5465 C C   . PHE   C 1 264 ? -11.226 -0.867  41.393  1.00 21.08 ? 243 PHE   C C   1 
ATOM   5466 O O   . PHE   C 1 264 ? -11.627 -1.997  41.701  1.00 21.12 ? 243 PHE   C O   1 
ATOM   5467 C CB  . PHE   C 1 264 ? -12.639 1.092   40.724  1.00 22.11 ? 243 PHE   C CB  1 
ATOM   5468 C CG  . PHE   C 1 264 ? -13.464 0.101   39.910  1.00 24.27 ? 243 PHE   C CG  1 
ATOM   5469 C CD1 . PHE   C 1 264 ? -14.548 -0.573  40.498  1.00 24.96 ? 243 PHE   C CD1 1 
ATOM   5470 C CD2 . PHE   C 1 264 ? -13.118 -0.213  38.597  1.00 23.18 ? 243 PHE   C CD2 1 
ATOM   5471 C CE1 . PHE   C 1 264 ? -15.273 -1.512  39.763  1.00 25.96 ? 243 PHE   C CE1 1 
ATOM   5472 C CE2 . PHE   C 1 264 ? -13.869 -1.133  37.863  1.00 23.10 ? 243 PHE   C CE2 1 
ATOM   5473 C CZ  . PHE   C 1 264 ? -14.928 -1.791  38.457  1.00 27.71 ? 243 PHE   C CZ  1 
ATOM   5474 N N   . LEU   C 1 265 ? -10.178 -0.685  40.570  1.00 21.33 ? 244 LEU   C N   1 
ATOM   5475 C CA  . LEU   C 1 265 ? -9.510  -1.819  39.941  1.00 21.34 ? 244 LEU   C CA  1 
ATOM   5476 C C   . LEU   C 1 265 ? -8.850  -2.718  40.989  1.00 24.03 ? 244 LEU   C C   1 
ATOM   5477 O O   . LEU   C 1 265 ? -8.742  -3.934  40.783  1.00 23.97 ? 244 LEU   C O   1 
ATOM   5478 C CB  . LEU   C 1 265 ? -8.480  -1.305  38.926  1.00 23.00 ? 244 LEU   C CB  1 
ATOM   5479 C CG  . LEU   C 1 265 ? -9.088  -0.863  37.586  1.00 22.76 ? 244 LEU   C CG  1 
ATOM   5480 C CD1 . LEU   C 1 265 ? -8.059  -0.066  36.774  1.00 21.10 ? 244 LEU   C CD1 1 
ATOM   5481 C CD2 . LEU   C 1 265 ? -9.564  -2.080  36.815  1.00 22.79 ? 244 LEU   C CD2 1 
ATOM   5482 N N   . VAL   C 1 266 ? -8.421  -2.134  42.125  1.00 21.90 ? 245 VAL   C N   1 
ATOM   5483 C CA  . VAL   C 1 266 ? -7.791  -3.013  43.098  1.00 23.73 ? 245 VAL   C CA  1 
ATOM   5484 C C   . VAL   C 1 266 ? -8.853  -3.717  43.949  1.00 27.04 ? 245 VAL   C C   1 
ATOM   5485 O O   . VAL   C 1 266 ? -8.570  -4.775  44.515  1.00 27.18 ? 245 VAL   C O   1 
ATOM   5486 C CB  . VAL   C 1 266 ? -6.677  -2.383  43.952  1.00 26.31 ? 245 VAL   C CB  1 
ATOM   5487 C CG1 . VAL   C 1 266 ? -5.611  -1.697  43.097  1.00 25.85 ? 245 VAL   C CG1 1 
ATOM   5488 C CG2 . VAL   C 1 266 ? -7.206  -1.452  45.001  1.00 26.08 ? 245 VAL   C CG2 1 
ATOM   5489 N N   . SER   C 1 267 ? -10.072 -3.144  43.990  1.00 24.30 ? 246 SER   C N   1 
ATOM   5490 C CA  . SER   C 1 267 ? -11.141 -3.592  44.876  1.00 25.49 ? 246 SER   C CA  1 
ATOM   5491 C C   . SER   C 1 267 ? -11.684 -4.963  44.485  1.00 25.74 ? 246 SER   C C   1 
ATOM   5492 O O   . SER   C 1 267 ? -11.496 -5.403  43.363  1.00 25.18 ? 246 SER   C O   1 
ATOM   5493 C CB  . SER   C 1 267 ? -12.262 -2.589  44.884  1.00 26.22 ? 246 SER   C CB  1 
ATOM   5494 O OG  . SER   C 1 267 ? -13.073 -2.766  43.728  1.00 22.78 ? 246 SER   C OG  1 
ATOM   5495 N N   . GLY   C 1 268 ? -12.464 -5.585  45.395  1.00 24.25 ? 247 GLY   C N   1 
ATOM   5496 C CA  . GLY   C 1 268 ? -13.220 -6.789  45.064  1.00 26.93 ? 247 GLY   C CA  1 
ATOM   5497 C C   . GLY   C 1 268 ? -14.341 -6.539  44.040  1.00 26.73 ? 247 GLY   C C   1 
ATOM   5498 O O   . GLY   C 1 268 ? -14.905 -7.487  43.501  1.00 29.40 ? 247 GLY   C O   1 
ATOM   5499 N N   . SER   C 1 269 ? -14.630 -5.269  43.715  1.00 25.80 ? 248 SER   C N   1 
ATOM   5500 C CA  . SER   C 1 269 ? -15.627 -4.969  42.689  1.00 28.13 ? 248 SER   C CA  1 
ATOM   5501 C C   . SER   C 1 269 ? -15.093 -5.169  41.266  1.00 26.78 ? 248 SER   C C   1 
ATOM   5502 O O   . SER   C 1 269 ? -15.859 -5.036  40.319  1.00 26.00 ? 248 SER   C O   1 
ATOM   5503 C CB  . SER   C 1 269 ? -16.222 -3.597  42.870  1.00 27.68 ? 248 SER   C CB  1 
ATOM   5504 O OG  . SER   C 1 269 ? -16.915 -3.621  44.101  1.00 31.80 ? 248 SER   C OG  1 
ATOM   5505 N N   . ALA   C 1 270 ? -13.794 -5.519  41.141  1.00 21.99 ? 249 ALA   C N   1 
ATOM   5506 C CA  . ALA   C 1 270 ? -13.124 -5.660  39.860  1.00 23.28 ? 249 ALA   C CA  1 
ATOM   5507 C C   . ALA   C 1 270 ? -12.499 -7.058  39.772  1.00 26.25 ? 249 ALA   C C   1 
ATOM   5508 O O   . ALA   C 1 270 ? -11.603 -7.318  38.993  1.00 23.29 ? 249 ALA   C O   1 
ATOM   5509 C CB  . ALA   C 1 270 ? -12.105 -4.539  39.715  1.00 21.90 ? 249 ALA   C CB  1 
ATOM   5510 N N   . GLN   C 1 271 ? -13.043 -7.994  40.543  1.00 24.76 ? 250 GLN   C N   1 
ATOM   5511 C CA  . GLN   C 1 271 ? -12.443 -9.317  40.699  1.00 29.21 ? 250 GLN   C CA  1 
ATOM   5512 C C   . GLN   C 1 271 ? -12.332 -10.054 39.356  1.00 25.26 ? 250 GLN   C C   1 
ATOM   5513 O O   . GLN   C 1 271 ? -11.585 -11.029 39.228  1.00 25.30 ? 250 GLN   C O   1 
ATOM   5514 C CB  . GLN   C 1 271 ? -13.257 -9.934  41.851  1.00 33.49 ? 250 GLN   C CB  1 
ATOM   5515 C CG  . GLN   C 1 271 ? -13.734 -11.373 41.687  0.70 37.72 ? 250 GLN   C CG  1 
ATOM   5516 C CD  . GLN   C 1 271 ? -14.867 -11.770 42.630  0.70 38.41 ? 250 GLN   C CD  1 
ATOM   5517 O OE1 . GLN   C 1 271 ? -14.718 -12.688 43.442  0.70 41.16 ? 250 GLN   C OE1 1 
ATOM   5518 N NE2 . GLN   C 1 271 ? -16.022 -11.121 42.526  0.70 30.79 ? 250 GLN   C NE2 1 
ATOM   5519 N N   . TYR   C 1 272 ? -13.097 -9.628  38.350  1.00 23.16 ? 251 TYR   C N   1 
ATOM   5520 C CA  . TYR   C 1 272 ? -13.066 -10.383 37.109  1.00 24.20 ? 251 TYR   C CA  1 
ATOM   5521 C C   . TYR   C 1 272 ? -12.362 -9.574  36.023  1.00 21.07 ? 251 TYR   C C   1 
ATOM   5522 O O   . TYR   C 1 272 ? -12.316 -9.982  34.876  1.00 22.24 ? 251 TYR   C O   1 
ATOM   5523 C CB  . TYR   C 1 272 ? -14.474 -10.817 36.690  1.00 23.23 ? 251 TYR   C CB  1 
ATOM   5524 C CG  . TYR   C 1 272 ? -14.561 -11.869 35.593  1.00 26.14 ? 251 TYR   C CG  1 
ATOM   5525 C CD1 . TYR   C 1 272 ? -14.335 -13.205 35.889  1.00 24.98 ? 251 TYR   C CD1 1 
ATOM   5526 C CD2 . TYR   C 1 272 ? -14.897 -11.541 34.262  1.00 23.47 ? 251 TYR   C CD2 1 
ATOM   5527 C CE1 . TYR   C 1 272 ? -14.422 -14.181 34.902  1.00 26.09 ? 251 TYR   C CE1 1 
ATOM   5528 C CE2 . TYR   C 1 272 ? -15.025 -12.526 33.283  1.00 23.07 ? 251 TYR   C CE2 1 
ATOM   5529 C CZ  . TYR   C 1 272 ? -14.759 -13.853 33.597  1.00 23.35 ? 251 TYR   C CZ  1 
ATOM   5530 O OH  . TYR   C 1 272 ? -14.892 -14.870 32.670  1.00 23.03 ? 251 TYR   C OH  1 
ATOM   5531 N N   . ILE   C 1 273 ? -11.895 -8.379  36.378  1.00 20.50 ? 252 ILE   C N   1 
ATOM   5532 C CA  . ILE   C 1 273 ? -11.324 -7.506  35.375  1.00 20.45 ? 252 ILE   C CA  1 
ATOM   5533 C C   . ILE   C 1 273 ? -9.818  -7.724  35.365  1.00 21.16 ? 252 ILE   C C   1 
ATOM   5534 O O   . ILE   C 1 273 ? -9.138  -7.526  36.386  1.00 19.62 ? 252 ILE   C O   1 
ATOM   5535 C CB  . ILE   C 1 273 ? -11.687 -6.051  35.702  1.00 19.87 ? 252 ILE   C CB  1 
ATOM   5536 C CG1 . ILE   C 1 273 ? -13.253 -5.894  35.847  1.00 20.05 ? 252 ILE   C CG1 1 
ATOM   5537 C CG2 . ILE   C 1 273 ? -11.066 -5.086  34.684  1.00 18.70 ? 252 ILE   C CG2 1 
ATOM   5538 C CD1 . ILE   C 1 273 ? -13.672 -4.469  36.229  1.00 22.94 ? 252 ILE   C CD1 1 
ATOM   5539 N N   . THR   C 1 274 ? -9.309  -8.133  34.199  1.00 20.44 ? 253 THR   C N   1 
ATOM   5540 C CA  . THR   C 1 274 ? -7.871  -8.073  33.995  1.00 20.95 ? 253 THR   C CA  1 
ATOM   5541 C C   . THR   C 1 274 ? -7.610  -7.713  32.529  1.00 20.61 ? 253 THR   C C   1 
ATOM   5542 O O   . THR   C 1 274 ? -8.377  -8.090  31.646  1.00 22.57 ? 253 THR   C O   1 
ATOM   5543 C CB  . THR   C 1 274 ? -7.241  -9.383  34.470  1.00 20.27 ? 253 THR   C CB  1 
ATOM   5544 O OG1 . THR   C 1 274 ? -5.846  -9.129  34.561  1.00 19.70 ? 253 THR   C OG1 1 
ATOM   5545 C CG2 . THR   C 1 274 ? -7.483  -10.562 33.529  1.00 20.52 ? 253 THR   C CG2 1 
ATOM   5546 N N   . GLY   C 1 275 ? -6.501  -7.015  32.289  1.00 20.57 ? 254 GLY   C N   1 
ATOM   5547 C CA  . GLY   C 1 275 ? -6.134  -6.620  30.943  1.00 22.85 ? 254 GLY   C CA  1 
ATOM   5548 C C   . GLY   C 1 275 ? -6.952  -5.440  30.422  1.00 23.36 ? 254 GLY   C C   1 
ATOM   5549 O O   . GLY   C 1 275 ? -6.975  -5.189  29.213  1.00 23.67 ? 254 GLY   C O   1 
ATOM   5550 N N   . SER   C 1 276 ? -7.666  -4.749  31.326  1.00 21.63 ? 255 SER   C N   1 
ATOM   5551 C CA  . SER   C 1 276 ? -8.526  -3.652  30.922  1.00 20.70 ? 255 SER   C CA  1 
ATOM   5552 C C   . SER   C 1 276 ? -7.807  -2.358  31.252  1.00 21.57 ? 255 SER   C C   1 
ATOM   5553 O O   . SER   C 1 276 ? -7.127  -2.314  32.270  1.00 19.48 ? 255 SER   C O   1 
ATOM   5554 C CB  . SER   C 1 276 ? -9.845  -3.684  31.651  1.00 20.97 ? 255 SER   C CB  1 
ATOM   5555 O OG  . SER   C 1 276 ? -10.514 -4.890  31.301  1.00 25.95 ? 255 SER   C OG  1 
ATOM   5556 N N   . ILE   C 1 277 ? -8.027  -1.329  30.422  1.00 21.09 ? 256 ILE   C N   1 
ATOM   5557 C CA  . ILE   C 1 277 ? -7.480  -0.007  30.673  1.00 21.19 ? 256 ILE   C CA  1 
ATOM   5558 C C   . ILE   C 1 277 ? -8.649  0.967   30.704  1.00 25.68 ? 256 ILE   C C   1 
ATOM   5559 O O   . ILE   C 1 277 ? -9.315  1.116   29.687  1.00 26.27 ? 256 ILE   C O   1 
ATOM   5560 C CB  . ILE   C 1 277 ? -6.390  0.369   29.640  1.00 24.29 ? 256 ILE   C CB  1 
ATOM   5561 C CG1 . ILE   C 1 277 ? -5.170  -0.612  29.757  1.00 24.13 ? 256 ILE   C CG1 1 
ATOM   5562 C CG2 . ILE   C 1 277 ? -5.938  1.818   29.883  1.00 23.94 ? 256 ILE   C CG2 1 
ATOM   5563 C CD1 . ILE   C 1 277 ? -4.102  -0.447  28.686  1.00 29.13 ? 256 ILE   C CD1 1 
ATOM   5564 N N   . ILE   C 1 278 ? -8.874  1.625   31.853  1.00 21.84 ? 257 ILE   C N   1 
ATOM   5565 C CA  . ILE   C 1 278 ? -10.007 2.527   32.006  1.00 22.26 ? 257 ILE   C CA  1 
ATOM   5566 C C   . ILE   C 1 278 ? -9.538  3.951   31.739  1.00 22.80 ? 257 ILE   C C   1 
ATOM   5567 O O   . ILE   C 1 278 ? -8.690  4.461   32.482  1.00 20.29 ? 257 ILE   C O   1 
ATOM   5568 C CB  . ILE   C 1 278 ? -10.602 2.422   33.422  1.00 23.40 ? 257 ILE   C CB  1 
ATOM   5569 C CG1 . ILE   C 1 278 ? -10.978 0.980   33.759  1.00 23.45 ? 257 ILE   C CG1 1 
ATOM   5570 C CG2 . ILE   C 1 278 ? -11.779 3.401   33.621  1.00 22.78 ? 257 ILE   C CG2 1 
ATOM   5571 C CD1 . ILE   C 1 278 ? -11.510 0.817   35.176  1.00 26.31 ? 257 ILE   C CD1 1 
ATOM   5572 N N   . LYS   C 1 279 ? -10.081 4.596   30.694  1.00 19.82 ? 258 LYS   C N   1 
ATOM   5573 C CA  . LYS   C 1 279 ? -9.743  6.003   30.517  1.00 20.89 ? 258 LYS   C CA  1 
ATOM   5574 C C   . LYS   C 1 279 ? -10.501 6.808   31.561  1.00 21.64 ? 258 LYS   C C   1 
ATOM   5575 O O   . LYS   C 1 279 ? -11.659 6.507   31.856  1.00 20.97 ? 258 LYS   C O   1 
ATOM   5576 C CB  . LYS   C 1 279 ? -10.241 6.622   29.199  1.00 22.70 ? 258 LYS   C CB  1 
ATOM   5577 C CG  . LYS   C 1 279 ? -9.625  6.147   27.924  1.00 26.54 ? 258 LYS   C CG  1 
ATOM   5578 C CD  . LYS   C 1 279 ? -10.217 6.847   26.692  1.00 25.20 ? 258 LYS   C CD  1 
ATOM   5579 C CE  . LYS   C 1 279 ? -11.596 6.323   26.409  1.00 25.05 ? 258 LYS   C CE  1 
ATOM   5580 N NZ  . LYS   C 1 279 ? -12.324 6.918   25.271  1.00 24.02 ? 258 LYS   C NZ  1 
ATOM   5581 N N   . VAL   C 1 280 ? -9.834  7.851   32.065  1.00 23.54 ? 259 VAL   C N   1 
ATOM   5582 C CA  . VAL   C 1 280 ? -10.392 8.792   33.022  1.00 22.62 ? 259 VAL   C CA  1 
ATOM   5583 C C   . VAL   C 1 280 ? -10.009 10.175  32.520  1.00 20.87 ? 259 VAL   C C   1 
ATOM   5584 O O   . VAL   C 1 280 ? -9.059  10.772  33.010  1.00 22.92 ? 259 VAL   C O   1 
ATOM   5585 C CB  . VAL   C 1 280 ? -9.881  8.493   34.451  1.00 22.94 ? 259 VAL   C CB  1 
ATOM   5586 C CG1 . VAL   C 1 280 ? -10.551 9.407   35.490  1.00 22.92 ? 259 VAL   C CG1 1 
ATOM   5587 C CG2 . VAL   C 1 280 ? -10.180 7.041   34.848  1.00 22.44 ? 259 VAL   C CG2 1 
ATOM   5588 N N   . ASP   C 1 281 ? -10.714 10.625  31.466  1.00 21.91 ? 260 ASP   C N   1 
ATOM   5589 C CA  . ASP   C 1 281 ? -10.221 11.691  30.615  1.00 21.18 ? 260 ASP   C CA  1 
ATOM   5590 C C   . ASP   C 1 281 ? -11.297 12.739  30.305  1.00 19.96 ? 260 ASP   C C   1 
ATOM   5591 O O   . ASP   C 1 281 ? -11.032 13.696  29.571  1.00 21.70 ? 260 ASP   C O   1 
ATOM   5592 C CB  . ASP   C 1 281 ? -9.607  11.110  29.344  1.00 21.19 ? 260 ASP   C CB  1 
ATOM   5593 C CG  . ASP   C 1 281 ? -10.583 10.738  28.231  1.00 22.92 ? 260 ASP   C CG  1 
ATOM   5594 O OD1 . ASP   C 1 281 ? -11.795 10.500  28.512  1.00 24.03 ? 260 ASP   C OD1 1 
ATOM   5595 O OD2 . ASP   C 1 281 ? -10.127 10.690  27.083  1.00 20.87 ? 260 ASP   C OD2 1 
ATOM   5596 N N   . GLY   C 1 282 ? -12.493 12.600  30.877  1.00 21.73 ? 261 GLY   C N   1 
ATOM   5597 C CA  . GLY   C 1 282 ? -13.541 13.601  30.670  1.00 22.40 ? 261 GLY   C CA  1 
ATOM   5598 C C   . GLY   C 1 282 ? -13.943 13.761  29.204  1.00 23.07 ? 261 GLY   C C   1 
ATOM   5599 O O   . GLY   C 1 282 ? -14.518 14.786  28.807  1.00 23.35 ? 261 GLY   C O   1 
ATOM   5600 N N   . GLY   C 1 283 ? -13.669 12.726  28.399  1.00 20.87 ? 262 GLY   C N   1 
ATOM   5601 C CA  . GLY   C 1 283 ? -14.020 12.732  26.992  1.00 20.75 ? 262 GLY   C CA  1 
ATOM   5602 C C   . GLY   C 1 283 ? -12.946 13.344  26.087  1.00 22.64 ? 262 GLY   C C   1 
ATOM   5603 O O   . GLY   C 1 283 ? -13.166 13.430  24.877  1.00 22.75 ? 262 GLY   C O   1 
ATOM   5604 N N   . LEU   C 1 284 ? -11.800 13.783  26.632  1.00 21.44 ? 263 LEU   C N   1 
ATOM   5605 C CA  . LEU   C 1 284 ? -10.770 14.498  25.858  1.00 22.39 ? 263 LEU   C CA  1 
ATOM   5606 C C   . LEU   C 1 284 ? -10.319 13.720  24.604  1.00 22.46 ? 263 LEU   C C   1 
ATOM   5607 O O   . LEU   C 1 284 ? -10.162 14.299  23.518  1.00 21.95 ? 263 LEU   C O   1 
ATOM   5608 C CB  . LEU   C 1 284 ? -9.552  14.774  26.743  1.00 22.72 ? 263 LEU   C CB  1 
ATOM   5609 C CG  . LEU   C 1 284 ? -8.380  15.467  26.042  1.00 24.59 ? 263 LEU   C CG  1 
ATOM   5610 C CD1 . LEU   C 1 284 ? -8.808  16.910  25.730  1.00 25.50 ? 263 LEU   C CD1 1 
ATOM   5611 C CD2 . LEU   C 1 284 ? -7.131  15.482  26.938  1.00 26.83 ? 263 LEU   C CD2 1 
ATOM   5612 N N   . SER   C 1 285 ? -10.097 12.397  24.749  1.00 20.46 ? 264 SER   C N   1 
ATOM   5613 C CA  . SER   C 1 285 ? -9.603  11.600  23.631  1.00 22.19 ? 264 SER   C CA  1 
ATOM   5614 C C   . SER   C 1 285 ? -10.626 11.467  22.494  1.00 22.79 ? 264 SER   C C   1 
ATOM   5615 O O   . SER   C 1 285 ? -10.261 10.986  21.424  1.00 23.80 ? 264 SER   C O   1 
ATOM   5616 C CB  . SER   C 1 285 ? -9.168  10.211  24.070  1.00 22.07 ? 264 SER   C CB  1 
ATOM   5617 O OG  . SER   C 1 285 ? -10.280 9.507   24.624  1.00 22.50 ? 264 SER   C OG  1 
ATOM   5618 N N   . LEU   C 1 286 ? -11.896 11.856  22.724  1.00 20.96 ? 265 LEU   C N   1 
ATOM   5619 C CA  . LEU   C 1 286 ? -12.947 11.765  21.711  1.00 23.93 ? 265 LEU   C CA  1 
ATOM   5620 C C   . LEU   C 1 286 ? -12.961 13.004  20.812  1.00 22.67 ? 265 LEU   C C   1 
ATOM   5621 O O   . LEU   C 1 286 ? -13.710 13.019  19.844  1.00 24.39 ? 265 LEU   C O   1 
ATOM   5622 C CB  . LEU   C 1 286 ? -14.313 11.606  22.387  1.00 22.82 ? 265 LEU   C CB  1 
ATOM   5623 C CG  . LEU   C 1 286 ? -14.470 10.368  23.263  1.00 24.05 ? 265 LEU   C CG  1 
ATOM   5624 C CD1 . LEU   C 1 286 ? -15.860 10.404  23.858  1.00 28.29 ? 265 LEU   C CD1 1 
ATOM   5625 C CD2 . LEU   C 1 286 ? -14.142 9.036   22.595  1.00 25.16 ? 265 LEU   C CD2 1 
ATOM   5626 N N   . VAL   C 1 287 ? -12.213 14.057  21.172  1.00 22.63 ? 266 VAL   C N   1 
ATOM   5627 C CA  . VAL   C 1 287 ? -12.314 15.354  20.503  1.00 23.98 ? 266 VAL   C CA  1 
ATOM   5628 C C   . VAL   C 1 287 ? -11.381 15.387  19.287  1.00 27.19 ? 266 VAL   C C   1 
ATOM   5629 O O   . VAL   C 1 287 ? -10.161 15.294  19.437  1.00 27.33 ? 266 VAL   C O   1 
ATOM   5630 C CB  . VAL   C 1 287 ? -12.040 16.532  21.458  1.00 25.58 ? 266 VAL   C CB  1 
ATOM   5631 C CG1 . VAL   C 1 287 ? -12.191 17.906  20.786  1.00 29.02 ? 266 VAL   C CG1 1 
ATOM   5632 C CG2 . VAL   C 1 287 ? -12.912 16.451  22.721  1.00 22.59 ? 266 VAL   C CG2 1 
ATOM   5633 N N   . HIS   C 1 288 ? -11.962 15.612  18.091  1.00 29.66 ? 267 HIS   C N   1 
ATOM   5634 C CA  . HIS   C 1 288 ? -11.170 15.707  16.863  1.00 32.66 ? 267 HIS   C CA  1 
ATOM   5635 C C   . HIS   C 1 288 ? -10.366 17.002  16.818  1.00 32.73 ? 267 HIS   C C   1 
ATOM   5636 O O   . HIS   C 1 288 ? -10.646 17.938  17.551  1.00 31.49 ? 267 HIS   C O   1 
ATOM   5637 C CB  . HIS   C 1 288 ? -12.027 15.541  15.600  1.00 35.92 ? 267 HIS   C CB  1 
ATOM   5638 C CG  . HIS   C 1 288 ? -12.990 16.651  15.362  1.00 36.36 ? 267 HIS   C CG  1 
ATOM   5639 N ND1 . HIS   C 1 288 ? -12.578 17.925  15.010  1.00 34.15 ? 267 HIS   C ND1 1 
ATOM   5640 C CD2 . HIS   C 1 288 ? -14.338 16.694  15.487  1.00 35.54 ? 267 HIS   C CD2 1 
ATOM   5641 C CE1 . HIS   C 1 288 ? -13.647 18.722  14.928  1.00 34.75 ? 267 HIS   C CE1 1 
ATOM   5642 N NE2 . HIS   C 1 288 ? -14.729 17.994  15.212  1.00 37.37 ? 267 HIS   C NE2 1 
ATOM   5643 N N   . ALA   C 1 289 ? -9.380  17.057  15.911  1.00 31.63 ? 268 ALA   C N   1 
ATOM   5644 C CA  . ALA   C 1 289 ? -8.538  18.231  15.726  1.00 34.61 ? 268 ALA   C CA  1 
ATOM   5645 C C   . ALA   C 1 289 ? -9.404  19.429  15.336  1.00 35.80 ? 268 ALA   C C   1 
ATOM   5646 O O   . ALA   C 1 289 ? -9.001  20.565  15.665  1.00 38.92 ? 268 ALA   C O   1 
ATOM   5647 C CB  . ALA   C 1 289 ? -7.534  17.959  14.628  1.00 38.05 ? 268 ALA   C CB  1 
ATOM   5648 O OXT . ALA   C 1 289 ? -10.430 19.170  14.676  1.00 38.00 ? 268 ALA   C OXT 1 
ATOM   5649 N N   . GLU   D 1 23  ? -34.895 12.674  48.006  0.70 48.77 ? 2   GLU   D N   1 
ATOM   5650 C CA  . GLU   D 1 23  ? -35.577 11.717  47.095  0.70 45.87 ? 2   GLU   D CA  1 
ATOM   5651 C C   . GLU   D 1 23  ? -34.524 10.806  46.468  0.70 43.22 ? 2   GLU   D C   1 
ATOM   5652 O O   . GLU   D 1 23  ? -33.393 11.222  46.204  0.70 42.18 ? 2   GLU   D O   1 
ATOM   5653 C CB  . GLU   D 1 23  ? -36.434 12.470  46.075  0.70 50.86 ? 2   GLU   D CB  1 
ATOM   5654 C CG  . GLU   D 1 23  ? -37.476 11.588  45.390  0.70 56.23 ? 2   GLU   D CG  1 
ATOM   5655 C CD  . GLU   D 1 23  ? -38.443 10.847  46.305  0.70 56.96 ? 2   GLU   D CD  1 
ATOM   5656 O OE1 . GLU   D 1 23  ? -39.411 11.483  46.767  0.70 56.33 ? 2   GLU   D OE1 1 
ATOM   5657 O OE2 . GLU   D 1 23  ? -38.232 9.637   46.566  0.70 56.94 ? 2   GLU   D OE2 1 
ATOM   5658 N N   . ALA   D 1 24  ? -34.897 9.539   46.269  1.00 40.09 ? 3   ALA   D N   1 
ATOM   5659 C CA  . ALA   D 1 24  ? -34.000 8.566   45.674  1.00 35.46 ? 3   ALA   D CA  1 
ATOM   5660 C C   . ALA   D 1 24  ? -33.917 8.781   44.153  1.00 37.13 ? 3   ALA   D C   1 
ATOM   5661 O O   . ALA   D 1 24  ? -34.897 9.155   43.500  1.00 37.79 ? 3   ALA   D O   1 
ATOM   5662 C CB  . ALA   D 1 24  ? -34.449 7.179   46.056  1.00 31.85 ? 3   ALA   D CB  1 
ATOM   5663 N N   . PRO   D 1 25  ? -32.721 8.622   43.529  1.00 35.15 ? 4   PRO   D N   1 
ATOM   5664 C CA  . PRO   D 1 25  ? -32.615 8.722   42.066  1.00 29.06 ? 4   PRO   D CA  1 
ATOM   5665 C C   . PRO   D 1 25  ? -33.304 7.522   41.414  1.00 30.25 ? 4   PRO   D C   1 
ATOM   5666 O O   . PRO   D 1 25  ? -33.597 6.540   42.091  1.00 29.31 ? 4   PRO   D O   1 
ATOM   5667 C CB  . PRO   D 1 25  ? -31.083 8.727   41.844  1.00 28.51 ? 4   PRO   D CB  1 
ATOM   5668 C CG  . PRO   D 1 25  ? -30.541 7.900   43.017  1.00 33.37 ? 4   PRO   D CG  1 
ATOM   5669 C CD  . PRO   D 1 25  ? -31.445 8.272   44.195  1.00 30.93 ? 4   PRO   D CD  1 
ATOM   5670 N N   . ALA   D 1 26  ? -33.522 7.588   40.083  1.00 28.19 ? 5   ALA   D N   1 
ATOM   5671 C CA  . ALA   D 1 26  ? -34.221 6.506   39.404  1.00 29.77 ? 5   ALA   D CA  1 
ATOM   5672 C C   . ALA   D 1 26  ? -33.424 6.020   38.189  1.00 23.91 ? 5   ALA   D C   1 
ATOM   5673 O O   . ALA   D 1 26  ? -32.772 6.822   37.512  1.00 25.78 ? 5   ALA   D O   1 
ATOM   5674 C CB  . ALA   D 1 26  ? -35.592 7.005   38.988  1.00 27.72 ? 5   ALA   D CB  1 
ATOM   5675 N N   . ALA   D 1 27  ? -33.508 4.714   37.911  1.00 22.08 ? 6   ALA   D N   1 
ATOM   5676 C CA  . ALA   D 1 27  ? -32.776 4.154   36.770  1.00 24.17 ? 6   ALA   D CA  1 
ATOM   5677 C C   . ALA   D 1 27  ? -33.715 3.322   35.892  1.00 24.57 ? 6   ALA   D C   1 
ATOM   5678 O O   . ALA   D 1 27  ? -34.580 2.616   36.414  1.00 28.54 ? 6   ALA   D O   1 
ATOM   5679 C CB  . ALA   D 1 27  ? -31.631 3.280   37.234  1.00 22.71 ? 6   ALA   D CB  1 
ATOM   5680 N N   . VAL   D 1 28  ? -33.534 3.409   34.564  1.00 22.96 ? 7   VAL   D N   1 
ATOM   5681 C CA  . VAL   D 1 28  ? -34.160 2.476   33.625  1.00 20.90 ? 7   VAL   D CA  1 
ATOM   5682 C C   . VAL   D 1 28  ? -33.132 1.411   33.262  1.00 21.68 ? 7   VAL   D C   1 
ATOM   5683 O O   . VAL   D 1 28  ? -32.023 1.749   32.852  1.00 22.35 ? 7   VAL   D O   1 
ATOM   5684 C CB  . VAL   D 1 28  ? -34.548 3.235   32.330  1.00 22.61 ? 7   VAL   D CB  1 
ATOM   5685 C CG1 . VAL   D 1 28  ? -34.841 2.266   31.169  1.00 21.16 ? 7   VAL   D CG1 1 
ATOM   5686 C CG2 . VAL   D 1 28  ? -35.727 4.175   32.541  1.00 24.60 ? 7   VAL   D CG2 1 
ATOM   5687 N N   . VAL   D 1 29  ? -33.493 0.147   33.389  1.00 21.59 ? 8   VAL   D N   1 
ATOM   5688 C CA  . VAL   D 1 29  ? -32.634 -0.930  32.912  1.00 23.68 ? 8   VAL   D CA  1 
ATOM   5689 C C   . VAL   D 1 29  ? -33.425 -1.713  31.864  1.00 23.55 ? 8   VAL   D C   1 
ATOM   5690 O O   . VAL   D 1 29  ? -34.517 -2.227  32.141  1.00 23.19 ? 8   VAL   D O   1 
ATOM   5691 C CB  . VAL   D 1 29  ? -32.174 -1.862  34.051  1.00 24.10 ? 8   VAL   D CB  1 
ATOM   5692 C CG1 . VAL   D 1 29  ? -31.245 -2.950  33.537  1.00 24.19 ? 8   VAL   D CG1 1 
ATOM   5693 C CG2 . VAL   D 1 29  ? -31.497 -1.083  35.182  1.00 24.81 ? 8   VAL   D CG2 1 
ATOM   5694 N N   . THR   D 1 30  ? -32.912 -1.790  30.631  1.00 23.09 ? 9   THR   D N   1 
ATOM   5695 C CA  . THR   D 1 30  ? -33.633 -2.559  29.607  1.00 22.77 ? 9   THR   D CA  1 
ATOM   5696 C C   . THR   D 1 30  ? -33.290 -4.040  29.734  1.00 22.90 ? 9   THR   D C   1 
ATOM   5697 O O   . THR   D 1 30  ? -32.194 -4.383  30.174  1.00 24.84 ? 9   THR   D O   1 
ATOM   5698 C CB  . THR   D 1 30  ? -33.374 -2.028  28.191  1.00 22.44 ? 9   THR   D CB  1 
ATOM   5699 O OG1 . THR   D 1 30  ? -31.990 -2.234  27.879  1.00 22.88 ? 9   THR   D OG1 1 
ATOM   5700 C CG2 . THR   D 1 30  ? -33.789 -0.575  28.033  1.00 24.48 ? 9   THR   D CG2 1 
ATOM   5701 N N   . GLY   D 1 31  ? -34.214 -4.927  29.315  1.00 25.52 ? 10  GLY   D N   1 
ATOM   5702 C CA  . GLY   D 1 31  ? -34.033 -6.376  29.405  1.00 23.14 ? 10  GLY   D CA  1 
ATOM   5703 C C   . GLY   D 1 31  ? -33.644 -6.831  30.821  1.00 27.96 ? 10  GLY   D C   1 
ATOM   5704 O O   . GLY   D 1 31  ? -32.761 -7.667  31.010  1.00 26.33 ? 10  GLY   D O   1 
ATOM   5705 N N   . ALA   D 1 32  ? -34.316 -6.258  31.823  1.00 22.79 ? 11  ALA   D N   1 
ATOM   5706 C CA  . ALA   D 1 32  ? -33.952 -6.390  33.223  1.00 25.66 ? 11  ALA   D CA  1 
ATOM   5707 C C   . ALA   D 1 32  ? -34.690 -7.546  33.916  1.00 28.88 ? 11  ALA   D C   1 
ATOM   5708 O O   . ALA   D 1 32  ? -34.509 -7.730  35.123  1.00 28.79 ? 11  ALA   D O   1 
ATOM   5709 C CB  . ALA   D 1 32  ? -34.251 -5.076  33.913  1.00 31.09 ? 11  ALA   D CB  1 
ATOM   5710 N N   . ALA   D 1 33  ? -35.470 -8.359  33.181  1.00 28.25 ? 12  ALA   D N   1 
ATOM   5711 C CA  . ALA   D 1 33  ? -36.247 -9.385  33.872  1.00 31.79 ? 12  ALA   D CA  1 
ATOM   5712 C C   . ALA   D 1 33  ? -35.362 -10.539 34.331  1.00 32.90 ? 12  ALA   D C   1 
ATOM   5713 O O   . ALA   D 1 33  ? -35.670 -11.165 35.345  1.00 32.94 ? 12  ALA   D O   1 
ATOM   5714 C CB  . ALA   D 1 33  ? -37.443 -9.878  33.078  1.00 29.81 ? 12  ALA   D CB  1 
ATOM   5715 N N   . LYS   D 1 34  ? -34.273 -10.812 33.599  1.00 29.41 ? 13  LYS   D N   1 
ATOM   5716 C CA  . LYS   D 1 34  ? -33.463 -11.995 33.867  1.00 31.41 ? 13  LYS   D CA  1 
ATOM   5717 C C   . LYS   D 1 34  ? -31.968 -11.670 33.746  1.00 33.11 ? 13  LYS   D C   1 
ATOM   5718 O O   . LYS   D 1 34  ? -31.591 -10.568 33.340  1.00 30.39 ? 13  LYS   D O   1 
ATOM   5719 C CB  . LYS   D 1 34  ? -33.720 -13.096 32.828  1.00 35.72 ? 13  LYS   D CB  1 
ATOM   5720 C CG  . LYS   D 1 34  ? -35.116 -13.714 32.777  1.00 46.23 ? 13  LYS   D CG  1 
ATOM   5721 C CD  . LYS   D 1 34  ? -35.215 -14.673 31.590  1.00 44.89 ? 13  LYS   D CD  1 
ATOM   5722 C CE  . LYS   D 1 34  ? -36.567 -15.328 31.402  1.00 48.93 ? 13  LYS   D CE  1 
ATOM   5723 N N   . ARG   D 1 35  ? -31.140 -12.626 34.192  1.00 31.20 ? 14  ARG   D N   1 
ATOM   5724 C CA  . ARG   D 1 35  ? -29.719 -12.684 33.869  1.00 32.10 ? 14  ARG   D CA  1 
ATOM   5725 C C   . ARG   D 1 35  ? -29.029 -11.379 34.278  1.00 30.90 ? 14  ARG   D C   1 
ATOM   5726 O O   . ARG   D 1 35  ? -29.161 -10.912 35.414  1.00 29.39 ? 14  ARG   D O   1 
ATOM   5727 C CB  . ARG   D 1 35  ? -29.618 -13.083 32.390  1.00 32.59 ? 14  ARG   D CB  1 
ATOM   5728 C CG  . ARG   D 1 35  ? -30.162 -14.493 32.160  1.00 33.28 ? 14  ARG   D CG  1 
ATOM   5729 C CD  . ARG   D 1 35  ? -30.398 -14.922 30.698  1.00 35.11 ? 14  ARG   D CD  1 
ATOM   5730 N NE  . ARG   D 1 35  ? -29.194 -14.876 29.859  1.00 39.36 ? 14  ARG   D NE  1 
ATOM   5731 C CZ  . ARG   D 1 35  ? -28.112 -15.666 29.902  1.00 40.56 ? 14  ARG   D CZ  1 
ATOM   5732 N NH1 . ARG   D 1 35  ? -28.085 -16.735 30.669  1.00 36.09 ? 14  ARG   D NH1 1 
ATOM   5733 N NH2 . ARG   D 1 35  ? -27.042 -15.393 29.160  1.00 42.06 ? 14  ARG   D NH2 1 
ATOM   5734 N N   . ILE   D 1 36  ? -28.293 -10.769 33.341  1.00 25.54 ? 15  ILE   D N   1 
ATOM   5735 C CA  . ILE   D 1 36  ? -27.408 -9.683  33.706  1.00 25.57 ? 15  ILE   D CA  1 
ATOM   5736 C C   . ILE   D 1 36  ? -28.223 -8.416  34.011  1.00 25.62 ? 15  ILE   D C   1 
ATOM   5737 O O   . ILE   D 1 36  ? -27.896 -7.636  34.909  1.00 25.17 ? 15  ILE   D O   1 
ATOM   5738 C CB  . ILE   D 1 36  ? -26.397 -9.476  32.559  1.00 25.44 ? 15  ILE   D CB  1 
ATOM   5739 C CG1 . ILE   D 1 36  ? -25.371 -10.639 32.537  1.00 31.02 ? 15  ILE   D CG1 1 
ATOM   5740 C CG2 . ILE   D 1 36  ? -25.739 -8.095  32.696  1.00 22.19 ? 15  ILE   D CG2 1 
ATOM   5741 C CD1 . ILE   D 1 36  ? -24.474 -10.654 31.306  1.00 34.38 ? 15  ILE   D CD1 1 
ATOM   5742 N N   . GLY   D 1 37  ? -29.278 -8.175  33.233  1.00 24.39 ? 16  GLY   D N   1 
ATOM   5743 C CA  . GLY   D 1 37  ? -30.057 -6.965  33.469  1.00 26.83 ? 16  GLY   D CA  1 
ATOM   5744 C C   . GLY   D 1 37  ? -30.734 -6.988  34.846  1.00 25.61 ? 16  GLY   D C   1 
ATOM   5745 O O   . GLY   D 1 37  ? -30.881 -5.948  35.484  1.00 24.37 ? 16  GLY   D O   1 
ATOM   5746 N N   . ARG   D 1 38  ? -31.177 -8.173  35.264  1.00 25.42 ? 17  ARG   D N   1 
ATOM   5747 C CA  . ARG   D 1 38  ? -31.726 -8.377  36.604  1.00 28.32 ? 17  ARG   D CA  1 
ATOM   5748 C C   . ARG   D 1 38  ? -30.672 -8.059  37.671  1.00 27.07 ? 17  ARG   D C   1 
ATOM   5749 O O   . ARG   D 1 38  ? -30.932 -7.294  38.582  1.00 28.62 ? 17  ARG   D O   1 
ATOM   5750 C CB  . ARG   D 1 38  ? -32.253 -9.813  36.726  1.00 31.84 ? 17  ARG   D CB  1 
ATOM   5751 C CG  . ARG   D 1 38  ? -32.807 -10.037 38.129  1.00 35.58 ? 17  ARG   D CG  1 
ATOM   5752 C CD  . ARG   D 1 38  ? -32.911 -11.494 38.588  1.00 42.56 ? 17  ARG   D CD  1 
ATOM   5753 N NE  . ARG   D 1 38  ? -33.398 -11.443 39.977  0.50 44.93 ? 17  ARG   D NE  1 
ATOM   5754 C CZ  . ARG   D 1 38  ? -32.793 -11.841 41.097  0.50 43.73 ? 17  ARG   D CZ  1 
ATOM   5755 N NH1 . ARG   D 1 38  ? -31.640 -12.488 41.064  0.50 42.95 ? 17  ARG   D NH1 1 
ATOM   5756 N NH2 . ARG   D 1 38  ? -33.387 -11.627 42.261  0.50 49.26 ? 17  ARG   D NH2 1 
ATOM   5757 N N   . ALA   D 1 39  ? -29.447 -8.586  37.513  1.00 26.13 ? 18  ALA   D N   1 
ATOM   5758 C CA  . ALA   D 1 39  ? -28.393 -8.350  38.484  1.00 25.76 ? 18  ALA   D CA  1 
ATOM   5759 C C   . ALA   D 1 39  ? -28.121 -6.847  38.573  1.00 26.65 ? 18  ALA   D C   1 
ATOM   5760 O O   . ALA   D 1 39  ? -27.886 -6.298  39.656  1.00 26.34 ? 18  ALA   D O   1 
ATOM   5761 C CB  . ALA   D 1 39  ? -27.148 -9.159  38.116  1.00 26.85 ? 18  ALA   D CB  1 
ATOM   5762 N N   . ILE   D 1 40  ? -28.204 -6.164  37.417  1.00 23.65 ? 19  ILE   D N   1 
ATOM   5763 C CA  . ILE   D 1 40  ? -27.976 -4.731  37.398  1.00 22.49 ? 19  ILE   D CA  1 
ATOM   5764 C C   . ILE   D 1 40  ? -29.102 -4.000  38.143  1.00 24.05 ? 19  ILE   D C   1 
ATOM   5765 O O   . ILE   D 1 40  ? -28.831 -3.062  38.907  1.00 25.09 ? 19  ILE   D O   1 
ATOM   5766 C CB  . ILE   D 1 40  ? -27.820 -4.237  35.949  1.00 21.75 ? 19  ILE   D CB  1 
ATOM   5767 C CG1 . ILE   D 1 40  ? -26.487 -4.744  35.335  1.00 24.22 ? 19  ILE   D CG1 1 
ATOM   5768 C CG2 . ILE   D 1 40  ? -27.937 -2.707  35.849  1.00 20.81 ? 19  ILE   D CG2 1 
ATOM   5769 C CD1 . ILE   D 1 40  ? -26.392 -4.494  33.831  1.00 21.85 ? 19  ILE   D CD1 1 
ATOM   5770 N N   . ALA   D 1 41  ? -30.364 -4.325  37.821  1.00 25.50 ? 20  ALA   D N   1 
ATOM   5771 C CA  . ALA   D 1 41  ? -31.475 -3.685  38.528  1.00 25.70 ? 20  ALA   D CA  1 
ATOM   5772 C C   . ALA   D 1 41  ? -31.383 -3.949  40.047  1.00 27.62 ? 20  ALA   D C   1 
ATOM   5773 O O   . ALA   D 1 41  ? -31.540 -3.025  40.838  1.00 28.32 ? 20  ALA   D O   1 
ATOM   5774 C CB  . ALA   D 1 41  ? -32.812 -4.077  37.901  1.00 25.29 ? 20  ALA   D CB  1 
ATOM   5775 N N   . VAL   D 1 42  ? -31.095 -5.198  40.461  1.00 26.85 ? 21  VAL   D N   1 
ATOM   5776 C CA  . VAL   D 1 42  ? -30.926 -5.537  41.878  1.00 26.47 ? 21  VAL   D CA  1 
ATOM   5777 C C   . VAL   D 1 42  ? -29.865 -4.650  42.528  1.00 30.53 ? 21  VAL   D C   1 
ATOM   5778 O O   . VAL   D 1 42  ? -30.111 -4.001  43.547  1.00 30.24 ? 21  VAL   D O   1 
ATOM   5779 C CB  . VAL   D 1 42  ? -30.615 -7.035  42.085  1.00 29.66 ? 21  VAL   D CB  1 
ATOM   5780 C CG1 . VAL   D 1 42  ? -30.185 -7.366  43.528  1.00 25.63 ? 21  VAL   D CG1 1 
ATOM   5781 C CG2 . VAL   D 1 42  ? -31.816 -7.880  41.686  1.00 28.00 ? 21  VAL   D CG2 1 
ATOM   5782 N N   . LYS   D 1 43  ? -28.678 -4.552  41.900  1.00 26.17 ? 22  LYS   D N   1 
ATOM   5783 C CA  . LYS   D 1 43  ? -27.591 -3.854  42.552  1.00 25.91 ? 22  LYS   D CA  1 
ATOM   5784 C C   . LYS   D 1 43  ? -27.878 -2.357  42.597  1.00 24.58 ? 22  LYS   D C   1 
ATOM   5785 O O   . LYS   D 1 43  ? -27.505 -1.711  43.569  1.00 25.30 ? 22  LYS   D O   1 
ATOM   5786 C CB  . LYS   D 1 43  ? -26.262 -4.165  41.850  1.00 29.78 ? 22  LYS   D CB  1 
ATOM   5787 C CG  . LYS   D 1 43  ? -25.088 -4.254  42.781  1.00 40.57 ? 22  LYS   D CG  1 
ATOM   5788 C CD  . LYS   D 1 43  ? -23.815 -4.737  42.090  1.00 40.89 ? 22  LYS   D CD  1 
ATOM   5789 C CE  . LYS   D 1 43  ? -23.794 -6.225  41.995  1.00 39.81 ? 22  LYS   D CE  1 
ATOM   5790 N NZ  . LYS   D 1 43  ? -23.395 -6.792  43.286  1.00 45.78 ? 22  LYS   D NZ  1 
ATOM   5791 N N   . LEU   D 1 44  ? -28.459 -1.799  41.525  1.00 23.55 ? 23  LEU   D N   1 
ATOM   5792 C CA  . LEU   D 1 44  ? -28.835 -0.384  41.533  1.00 24.65 ? 23  LEU   D CA  1 
ATOM   5793 C C   . LEU   D 1 44  ? -29.832 -0.109  42.675  1.00 25.92 ? 23  LEU   D C   1 
ATOM   5794 O O   . LEU   D 1 44  ? -29.742 0.884   43.426  1.00 27.11 ? 23  LEU   D O   1 
ATOM   5795 C CB  . LEU   D 1 44  ? -29.429 -0.025  40.167  1.00 24.43 ? 23  LEU   D CB  1 
ATOM   5796 C CG  . LEU   D 1 44  ? -28.395 0.231   39.058  1.00 25.46 ? 23  LEU   D CG  1 
ATOM   5797 C CD1 . LEU   D 1 44  ? -29.141 0.377   37.757  1.00 28.15 ? 23  LEU   D CD1 1 
ATOM   5798 C CD2 . LEU   D 1 44  ? -27.667 1.525   39.361  1.00 25.39 ? 23  LEU   D CD2 1 
ATOM   5799 N N   . HIS   D 1 45  ? -30.774 -1.031  42.806  1.00 24.95 ? 24  HIS   D N   1 
ATOM   5800 C CA  . HIS   D 1 45  ? -31.780 -0.946  43.863  1.00 29.55 ? 24  HIS   D CA  1 
ATOM   5801 C C   . HIS   D 1 45  ? -31.126 -1.026  45.252  1.00 30.72 ? 24  HIS   D C   1 
ATOM   5802 O O   . HIS   D 1 45  ? -31.410 -0.196  46.108  1.00 30.13 ? 24  HIS   D O   1 
ATOM   5803 C CB  . HIS   D 1 45  ? -32.839 -2.035  43.657  1.00 30.52 ? 24  HIS   D CB  1 
ATOM   5804 C CG  . HIS   D 1 45  ? -34.038 -1.818  44.536  1.00 32.52 ? 24  HIS   D CG  1 
ATOM   5805 N ND1 . HIS   D 1 45  ? -34.215 -2.499  45.716  1.00 33.36 ? 24  HIS   D ND1 1 
ATOM   5806 C CD2 . HIS   D 1 45  ? -35.074 -0.979  44.425  1.00 34.67 ? 24  HIS   D CD2 1 
ATOM   5807 C CE1 . HIS   D 1 45  ? -35.363 -2.110  46.272  1.00 38.40 ? 24  HIS   D CE1 1 
ATOM   5808 N NE2 . HIS   D 1 45  ? -35.898 -1.174  45.518  1.00 33.12 ? 24  HIS   D NE2 1 
ATOM   5809 N N   . GLN   D 1 46  ? -30.224 -2.004  45.455  1.00 31.52 ? 25  GLN   D N   1 
ATOM   5810 C CA  . GLN   D 1 46  ? -29.480 -2.127  46.700  1.00 27.97 ? 25  GLN   D CA  1 
ATOM   5811 C C   . GLN   D 1 46  ? -28.666 -0.872  46.972  1.00 35.10 ? 25  GLN   D C   1 
ATOM   5812 O O   . GLN   D 1 46  ? -28.344 -0.604  48.126  1.00 32.50 ? 25  GLN   D O   1 
ATOM   5813 C CB  . GLN   D 1 46  ? -28.594 -3.357  46.723  1.00 30.48 ? 25  GLN   D CB  1 
ATOM   5814 C CG  . GLN   D 1 46  ? -29.399 -4.651  46.743  1.00 29.96 ? 25  GLN   D CG  1 
ATOM   5815 C CD  . GLN   D 1 46  ? -28.522 -5.841  46.487  1.00 34.75 ? 25  GLN   D CD  1 
ATOM   5816 O OE1 . GLN   D 1 46  ? -27.389 -5.689  46.011  1.00 36.93 ? 25  GLN   D OE1 1 
ATOM   5817 N NE2 . GLN   D 1 46  ? -29.073 -7.028  46.715  1.00 40.47 ? 25  GLN   D NE2 1 
ATOM   5818 N N   . THR   D 1 47  ? -28.407 -0.066  45.927  1.00 33.14 ? 26  THR   D N   1 
ATOM   5819 C CA  . THR   D 1 47  ? -27.573 1.108   46.075  1.00 28.89 ? 26  THR   D CA  1 
ATOM   5820 C C   . THR   D 1 47  ? -28.439 2.313   46.405  1.00 31.57 ? 26  THR   D C   1 
ATOM   5821 O O   . THR   D 1 47  ? -27.918 3.383   46.725  1.00 30.67 ? 26  THR   D O   1 
ATOM   5822 C CB  . THR   D 1 47  ? -26.735 1.332   44.810  1.00 31.65 ? 26  THR   D CB  1 
ATOM   5823 O OG1 . THR   D 1 47  ? -25.892 0.192   44.666  1.00 32.06 ? 26  THR   D OG1 1 
ATOM   5824 C CG2 . THR   D 1 47  ? -25.824 2.534   44.930  1.00 34.56 ? 26  THR   D CG2 1 
ATOM   5825 N N   . GLY   D 1 48  ? -29.763 2.148   46.328  1.00 31.73 ? 27  GLY   D N   1 
ATOM   5826 C CA  . GLY   D 1 48  ? -30.639 3.255   46.679  1.00 31.16 ? 27  GLY   D CA  1 
ATOM   5827 C C   . GLY   D 1 48  ? -31.493 3.750   45.514  1.00 35.29 ? 27  GLY   D C   1 
ATOM   5828 O O   . GLY   D 1 48  ? -32.269 4.693   45.688  1.00 31.22 ? 27  GLY   D O   1 
ATOM   5829 N N   . TYR   D 1 49  ? -31.354 3.122   44.331  1.00 30.92 ? 28  TYR   D N   1 
ATOM   5830 C CA  . TYR   D 1 49  ? -32.088 3.590   43.158  1.00 30.86 ? 28  TYR   D CA  1 
ATOM   5831 C C   . TYR   D 1 49  ? -33.477 2.968   43.143  1.00 29.13 ? 28  TYR   D C   1 
ATOM   5832 O O   . TYR   D 1 49  ? -33.641 1.793   43.507  1.00 30.45 ? 28  TYR   D O   1 
ATOM   5833 C CB  . TYR   D 1 49  ? -31.442 3.165   41.831  1.00 28.01 ? 28  TYR   D CB  1 
ATOM   5834 C CG  . TYR   D 1 49  ? -30.249 4.047   41.497  1.00 28.25 ? 28  TYR   D CG  1 
ATOM   5835 C CD1 . TYR   D 1 49  ? -28.991 3.786   42.048  1.00 29.84 ? 28  TYR   D CD1 1 
ATOM   5836 C CD2 . TYR   D 1 49  ? -30.383 5.142   40.643  1.00 27.75 ? 28  TYR   D CD2 1 
ATOM   5837 C CE1 . TYR   D 1 49  ? -27.899 4.585   41.736  1.00 27.25 ? 28  TYR   D CE1 1 
ATOM   5838 C CE2 . TYR   D 1 49  ? -29.297 5.953   40.330  1.00 31.67 ? 28  TYR   D CE2 1 
ATOM   5839 C CZ  . TYR   D 1 49  ? -28.058 5.671   40.889  1.00 32.17 ? 28  TYR   D CZ  1 
ATOM   5840 O OH  . TYR   D 1 49  ? -26.995 6.466   40.605  1.00 30.97 ? 28  TYR   D OH  1 
ATOM   5841 N N   . ARG   D 1 50  ? -34.444 3.772   42.666  1.00 29.23 ? 29  ARG   D N   1 
ATOM   5842 C CA  . ARG   D 1 50  ? -35.719 3.246   42.190  1.00 32.05 ? 29  ARG   D CA  1 
ATOM   5843 C C   . ARG   D 1 50  ? -35.546 2.822   40.726  1.00 32.13 ? 29  ARG   D C   1 
ATOM   5844 O O   . ARG   D 1 50  ? -34.772 3.454   40.010  1.00 29.14 ? 29  ARG   D O   1 
ATOM   5845 C CB  . ARG   D 1 50  ? -36.861 4.259   42.348  1.00 32.33 ? 29  ARG   D CB  1 
ATOM   5846 C CG  . ARG   D 1 50  ? -37.194 4.526   43.810  1.00 32.42 ? 29  ARG   D CG  1 
ATOM   5847 C CD  . ARG   D 1 50  ? -38.109 5.718   43.925  1.00 35.58 ? 29  ARG   D CD  1 
ATOM   5848 N NE  . ARG   D 1 50  ? -37.489 6.967   43.471  1.00 32.98 ? 29  ARG   D NE  1 
ATOM   5849 C CZ  . ARG   D 1 50  ? -38.239 8.053   43.346  1.00 34.88 ? 29  ARG   D CZ  1 
ATOM   5850 N NH1 . ARG   D 1 50  ? -39.543 7.974   43.556  1.00 34.60 ? 29  ARG   D NH1 1 
ATOM   5851 N NH2 . ARG   D 1 50  ? -37.705 9.211   43.010  1.00 34.67 ? 29  ARG   D NH2 1 
ATOM   5852 N N   . VAL   D 1 51  ? -36.226 1.744   40.312  1.00 25.94 ? 30  VAL   D N   1 
ATOM   5853 C CA  . VAL   D 1 51  ? -35.886 1.144   39.025  1.00 28.26 ? 30  VAL   D CA  1 
ATOM   5854 C C   . VAL   D 1 51  ? -37.120 0.883   38.168  1.00 31.00 ? 30  VAL   D C   1 
ATOM   5855 O O   . VAL   D 1 51  ? -38.193 0.531   38.674  1.00 29.81 ? 30  VAL   D O   1 
ATOM   5856 C CB  . VAL   D 1 51  ? -35.076 -0.147  39.212  1.00 31.37 ? 30  VAL   D CB  1 
ATOM   5857 C CG1 . VAL   D 1 51  ? -33.768 0.127   39.958  1.00 31.66 ? 30  VAL   D CG1 1 
ATOM   5858 C CG2 . VAL   D 1 51  ? -35.872 -1.221  39.941  1.00 36.01 ? 30  VAL   D CG2 1 
ATOM   5859 N N   . VAL   D 1 52  ? -36.938 1.067   36.856  1.00 29.11 ? 31  VAL   D N   1 
ATOM   5860 C CA  . VAL   D 1 52  ? -37.853 0.600   35.825  1.00 27.37 ? 31  VAL   D CA  1 
ATOM   5861 C C   . VAL   D 1 52  ? -37.217 -0.622  35.209  1.00 29.34 ? 31  VAL   D C   1 
ATOM   5862 O O   . VAL   D 1 52  ? -36.089 -0.538  34.681  1.00 24.23 ? 31  VAL   D O   1 
ATOM   5863 C CB  . VAL   D 1 52  ? -38.097 1.641   34.724  1.00 26.90 ? 31  VAL   D CB  1 
ATOM   5864 C CG1 . VAL   D 1 52  ? -39.059 1.102   33.641  1.00 27.87 ? 31  VAL   D CG1 1 
ATOM   5865 C CG2 . VAL   D 1 52  ? -38.611 2.942   35.318  1.00 27.03 ? 31  VAL   D CG2 1 
ATOM   5866 N N   . ILE   D 1 53  ? -37.954 -1.725  35.355  1.00 24.73 ? 32  ILE   D N   1 
ATOM   5867 C CA  . ILE   D 1 53  ? -37.556 -3.023  34.872  1.00 26.88 ? 32  ILE   D CA  1 
ATOM   5868 C C   . ILE   D 1 53  ? -38.239 -3.173  33.525  1.00 29.28 ? 32  ILE   D C   1 
ATOM   5869 O O   . ILE   D 1 53  ? -39.428 -3.499  33.481  1.00 26.49 ? 32  ILE   D O   1 
ATOM   5870 C CB  . ILE   D 1 53  ? -38.044 -4.082  35.871  1.00 26.30 ? 32  ILE   D CB  1 
ATOM   5871 C CG1 . ILE   D 1 53  ? -37.333 -3.912  37.224  1.00 30.68 ? 32  ILE   D CG1 1 
ATOM   5872 C CG2 . ILE   D 1 53  ? -37.916 -5.500  35.308  1.00 26.74 ? 32  ILE   D CG2 1 
ATOM   5873 C CD1 . ILE   D 1 53  ? -38.093 -4.451  38.428  1.00 34.06 ? 32  ILE   D CD1 1 
ATOM   5874 N N   . HIS   D 1 54  ? -37.509 -2.861  32.439  1.00 26.05 ? 33  HIS   D N   1 
ATOM   5875 C CA  . HIS   D 1 54  ? -38.049 -3.068  31.104  1.00 25.29 ? 33  HIS   D CA  1 
ATOM   5876 C C   . HIS   D 1 54  ? -37.963 -4.555  30.761  1.00 24.92 ? 33  HIS   D C   1 
ATOM   5877 O O   . HIS   D 1 54  ? -37.006 -5.241  31.131  1.00 27.92 ? 33  HIS   D O   1 
ATOM   5878 C CB  . HIS   D 1 54  ? -37.371 -2.168  30.056  1.00 24.70 ? 33  HIS   D CB  1 
ATOM   5879 C CG  . HIS   D 1 54  ? -37.551 -2.740  28.686  1.00 27.80 ? 33  HIS   D CG  1 
ATOM   5880 N ND1 . HIS   D 1 54  ? -36.647 -3.655  28.187  1.00 29.23 ? 33  HIS   D ND1 1 
ATOM   5881 C CD2 . HIS   D 1 54  ? -38.524 -2.621  27.759  1.00 24.44 ? 33  HIS   D CD2 1 
ATOM   5882 C CE1 . HIS   D 1 54  ? -37.075 -4.072  26.997  1.00 28.61 ? 33  HIS   D CE1 1 
ATOM   5883 N NE2 . HIS   D 1 54  ? -38.207 -3.454  26.717  1.00 25.74 ? 33  HIS   D NE2 1 
ATOM   5884 N N   . TYR   D 1 55  ? -38.938 -5.040  29.990  1.00 25.72 ? 34  TYR   D N   1 
ATOM   5885 C CA  . TYR   D 1 55  ? -38.873 -6.416  29.519  1.00 25.91 ? 34  TYR   D CA  1 
ATOM   5886 C C   . TYR   D 1 55  ? -39.652 -6.488  28.201  1.00 25.27 ? 34  TYR   D C   1 
ATOM   5887 O O   . TYR   D 1 55  ? -40.351 -5.541  27.822  1.00 23.63 ? 34  TYR   D O   1 
ATOM   5888 C CB  . TYR   D 1 55  ? -39.417 -7.376  30.591  1.00 25.76 ? 34  TYR   D CB  1 
ATOM   5889 C CG  . TYR   D 1 55  ? -40.939 -7.236  30.669  1.00 28.59 ? 34  TYR   D CG  1 
ATOM   5890 C CD1 . TYR   D 1 55  ? -41.535 -6.251  31.458  1.00 27.23 ? 34  TYR   D CD1 1 
ATOM   5891 C CD2 . TYR   D 1 55  ? -41.765 -8.030  29.879  1.00 29.73 ? 34  TYR   D CD2 1 
ATOM   5892 C CE1 . TYR   D 1 55  ? -42.917 -6.108  31.508  1.00 30.86 ? 34  TYR   D CE1 1 
ATOM   5893 C CE2 . TYR   D 1 55  ? -43.147 -7.900  29.934  1.00 30.50 ? 34  TYR   D CE2 1 
ATOM   5894 C CZ  . TYR   D 1 55  ? -43.720 -6.936  30.744  1.00 31.54 ? 34  TYR   D CZ  1 
ATOM   5895 O OH  . TYR   D 1 55  ? -45.087 -6.797  30.768  1.00 34.98 ? 34  TYR   D OH  1 
ATOM   5896 N N   . HIS   D 1 56  ? -39.481 -7.609  27.499  1.00 24.80 ? 35  HIS   D N   1 
ATOM   5897 C CA  . HIS   D 1 56  ? -40.160 -7.815  26.230  1.00 30.64 ? 35  HIS   D CA  1 
ATOM   5898 C C   . HIS   D 1 56  ? -41.136 -8.978  26.390  1.00 31.29 ? 35  HIS   D C   1 
ATOM   5899 O O   . HIS   D 1 56  ? -42.340 -8.752  26.424  1.00 35.55 ? 35  HIS   D O   1 
ATOM   5900 C CB  . HIS   D 1 56  ? -39.156 -7.956  25.069  1.00 33.85 ? 35  HIS   D CB  1 
ATOM   5901 C CG  . HIS   D 1 56  ? -39.790 -8.282  23.757  1.00 34.34 ? 35  HIS   D CG  1 
ATOM   5902 N ND1 . HIS   D 1 56  ? -39.260 -9.235  22.913  1.00 36.70 ? 35  HIS   D ND1 1 
ATOM   5903 C CD2 . HIS   D 1 56  ? -40.954 -7.876  23.191  1.00 36.29 ? 35  HIS   D CD2 1 
ATOM   5904 C CE1 . HIS   D 1 56  ? -40.052 -9.368  21.848  1.00 37.58 ? 35  HIS   D CE1 1 
ATOM   5905 N NE2 . HIS   D 1 56  ? -41.089 -8.546  21.992  1.00 36.22 ? 35  HIS   D NE2 1 
ATOM   5906 N N   . ASN   D 1 57  ? -40.604 -10.193 26.540  1.00 28.80 ? 36  ASN   D N   1 
ATOM   5907 C CA  . ASN   D 1 57  ? -41.416 -11.390 26.681  1.00 32.44 ? 36  ASN   D CA  1 
ATOM   5908 C C   . ASN   D 1 57  ? -41.486 -11.869 28.128  1.00 35.82 ? 36  ASN   D C   1 
ATOM   5909 O O   . ASN   D 1 57  ? -42.428 -12.574 28.474  1.00 41.82 ? 36  ASN   D O   1 
ATOM   5910 C CB  . ASN   D 1 57  ? -40.876 -12.561 25.864  1.00 34.45 ? 36  ASN   D CB  1 
ATOM   5911 C CG  . ASN   D 1 57  ? -41.050 -12.316 24.386  1.00 42.47 ? 36  ASN   D CG  1 
ATOM   5912 O OD1 . ASN   D 1 57  ? -42.091 -11.798 23.974  1.00 42.66 ? 36  ASN   D OD1 1 
ATOM   5913 N ND2 . ASN   D 1 57  ? -40.037 -12.626 23.586  1.00 42.28 ? 36  ASN   D ND2 1 
ATOM   5914 N N   . SER   D 1 58  ? -40.517 -11.504 28.978  1.00 30.95 ? 37  SER   D N   1 
ATOM   5915 C CA  . SER   D 1 58  ? -40.462 -12.158 30.276  1.00 34.11 ? 37  SER   D CA  1 
ATOM   5916 C C   . SER   D 1 58  ? -41.315 -11.422 31.322  1.00 31.18 ? 37  SER   D C   1 
ATOM   5917 O O   . SER   D 1 58  ? -40.782 -10.924 32.310  1.00 28.42 ? 37  SER   D O   1 
ATOM   5918 C CB  . SER   D 1 58  ? -39.024 -12.349 30.737  1.00 35.72 ? 37  SER   D CB  1 
ATOM   5919 O OG  . SER   D 1 58  ? -38.323 -13.172 29.824  1.00 33.81 ? 37  SER   D OG  1 
ATOM   5920 N N   . ALA   D 1 59  ? -42.644 -11.380 31.116  1.00 35.19 ? 38  ALA   D N   1 
ATOM   5921 C CA  . ALA   D 1 59  ? -43.563 -10.633 31.966  1.00 32.36 ? 38  ALA   D CA  1 
ATOM   5922 C C   . ALA   D 1 59  ? -43.567 -11.176 33.394  1.00 31.90 ? 38  ALA   D C   1 
ATOM   5923 O O   . ALA   D 1 59  ? -43.452 -10.404 34.340  1.00 31.10 ? 38  ALA   D O   1 
ATOM   5924 C CB  . ALA   D 1 59  ? -44.961 -10.660 31.394  1.00 34.90 ? 38  ALA   D CB  1 
ATOM   5925 N N   . GLU   D 1 60  ? -43.635 -12.509 33.542  1.00 31.91 ? 39  GLU   D N   1 
ATOM   5926 C CA  . GLU   D 1 60  ? -43.714 -13.116 34.869  1.00 35.24 ? 39  GLU   D CA  1 
ATOM   5927 C C   . GLU   D 1 60  ? -42.438 -12.808 35.656  1.00 34.97 ? 39  GLU   D C   1 
ATOM   5928 O O   . GLU   D 1 60  ? -42.508 -12.464 36.834  1.00 32.15 ? 39  GLU   D O   1 
ATOM   5929 C CB  . GLU   D 1 60  ? -43.942 -14.630 34.836  1.00 36.74 ? 39  GLU   D CB  1 
ATOM   5930 C CG  . GLU   D 1 60  ? -45.326 -15.009 34.308  0.50 39.51 ? 39  GLU   D CG  1 
ATOM   5931 C CD  . GLU   D 1 60  ? -45.709 -16.480 34.352  0.50 43.03 ? 39  GLU   D CD  1 
ATOM   5932 O OE1 . GLU   D 1 60  ? -44.820 -17.329 34.571  0.50 42.91 ? 39  GLU   D OE1 1 
ATOM   5933 O OE2 . GLU   D 1 60  ? -46.914 -16.777 34.174  0.50 43.17 ? 39  GLU   D OE2 1 
ATOM   5934 N N   . ALA   D 1 61  ? -41.275 -12.966 35.000  1.00 31.02 ? 40  ALA   D N   1 
ATOM   5935 C CA  . ALA   D 1 61  ? -40.002 -12.758 35.669  1.00 30.51 ? 40  ALA   D CA  1 
ATOM   5936 C C   . ALA   D 1 61  ? -39.869 -11.271 36.006  1.00 27.33 ? 40  ALA   D C   1 
ATOM   5937 O O   . ALA   D 1 61  ? -39.356 -10.903 37.062  1.00 30.41 ? 40  ALA   D O   1 
ATOM   5938 C CB  . ALA   D 1 61  ? -38.847 -13.318 34.821  1.00 29.68 ? 40  ALA   D CB  1 
ATOM   5939 N N   . ALA   D 1 62  ? -40.405 -10.406 35.155  1.00 27.62 ? 41  ALA   D N   1 
ATOM   5940 C CA  . ALA   D 1 62  ? -40.284 -8.980  35.442  1.00 30.02 ? 41  ALA   D CA  1 
ATOM   5941 C C   . ALA   D 1 62  ? -41.107 -8.589  36.677  1.00 33.18 ? 41  ALA   D C   1 
ATOM   5942 O O   . ALA   D 1 62  ? -40.663 -7.799  37.526  1.00 31.72 ? 41  ALA   D O   1 
ATOM   5943 C CB  . ALA   D 1 62  ? -40.716 -8.155  34.240  1.00 29.36 ? 41  ALA   D CB  1 
ATOM   5944 N N   . VAL   D 1 63  ? -42.351 -9.067  36.711  1.00 34.21 ? 42  VAL   D N   1 
ATOM   5945 C CA  . VAL   D 1 63  ? -43.249 -8.735  37.814  1.00 35.47 ? 42  VAL   D CA  1 
ATOM   5946 C C   . VAL   D 1 63  ? -42.707 -9.334  39.117  1.00 33.79 ? 42  VAL   D C   1 
ATOM   5947 O O   . VAL   D 1 63  ? -42.675 -8.669  40.156  1.00 35.46 ? 42  VAL   D O   1 
ATOM   5948 C CB  . VAL   D 1 63  ? -44.709 -9.133  37.481  1.00 37.72 ? 42  VAL   D CB  1 
ATOM   5949 C CG1 . VAL   D 1 63  ? -45.640 -9.093  38.700  1.00 39.68 ? 42  VAL   D CG1 1 
ATOM   5950 C CG2 . VAL   D 1 63  ? -45.282 -8.251  36.376  1.00 35.66 ? 42  VAL   D CG2 1 
ATOM   5951 N N   . SER   D 1 64  ? -42.215 -10.575 39.047  1.00 36.49 ? 43  SER   D N   1 
ATOM   5952 C CA  . SER   D 1 64  ? -41.623 -11.223 40.205  1.00 35.24 ? 43  SER   D CA  1 
ATOM   5953 C C   . SER   D 1 64  ? -40.499 -10.349 40.767  1.00 40.81 ? 43  SER   D C   1 
ATOM   5954 O O   . SER   D 1 64  ? -40.345 -10.191 41.985  1.00 32.34 ? 43  SER   D O   1 
ATOM   5955 C CB  . SER   D 1 64  ? -41.115 -12.584 39.809  1.00 38.14 ? 43  SER   D CB  1 
ATOM   5956 O OG  . SER   D 1 64  ? -40.420 -13.212 40.878  1.00 41.16 ? 43  SER   D OG  1 
ATOM   5957 N N   . LEU   D 1 65  ? -39.700 -9.755  39.865  1.00 36.83 ? 44  LEU   D N   1 
ATOM   5958 C CA  . LEU   D 1 65  ? -38.555 -8.991  40.323  1.00 33.80 ? 44  LEU   D CA  1 
ATOM   5959 C C   . LEU   D 1 65  ? -39.043 -7.696  40.966  1.00 29.14 ? 44  LEU   D C   1 
ATOM   5960 O O   . LEU   D 1 65  ? -38.562 -7.312  42.048  1.00 31.25 ? 44  LEU   D O   1 
ATOM   5961 C CB  . LEU   D 1 65  ? -37.529 -8.758  39.207  1.00 31.79 ? 44  LEU   D CB  1 
ATOM   5962 C CG  . LEU   D 1 65  ? -36.425 -7.757  39.564  1.00 33.62 ? 44  LEU   D CG  1 
ATOM   5963 C CD1 . LEU   D 1 65  ? -35.516 -8.317  40.648  1.00 29.18 ? 44  LEU   D CD1 1 
ATOM   5964 C CD2 . LEU   D 1 65  ? -35.627 -7.300  38.311  1.00 31.02 ? 44  LEU   D CD2 1 
ATOM   5965 N N   . ALA   D 1 66  ? -40.014 -7.040  40.322  1.00 29.42 ? 45  ALA   D N   1 
ATOM   5966 C CA  . ALA   D 1 66  ? -40.558 -5.809  40.877  1.00 30.15 ? 45  ALA   D CA  1 
ATOM   5967 C C   . ALA   D 1 66  ? -41.093 -6.073  42.299  1.00 34.63 ? 45  ALA   D C   1 
ATOM   5968 O O   . ALA   D 1 66  ? -40.886 -5.283  43.219  1.00 31.81 ? 45  ALA   D O   1 
ATOM   5969 C CB  . ALA   D 1 66  ? -41.638 -5.286  39.961  1.00 33.40 ? 45  ALA   D CB  1 
ATOM   5970 N N   . ASP   D 1 67  ? -41.751 -7.227  42.478  1.00 35.82 ? 46  ASP   D N   1 
ATOM   5971 C CA  . ASP   D 1 67  ? -42.355 -7.605  43.757  1.00 38.43 ? 46  ASP   D CA  1 
ATOM   5972 C C   . ASP   D 1 67  ? -41.282 -7.773  44.828  1.00 37.96 ? 46  ASP   D C   1 
ATOM   5973 O O   . ASP   D 1 67  ? -41.435 -7.265  45.931  1.00 38.04 ? 46  ASP   D O   1 
ATOM   5974 C CB  . ASP   D 1 67  ? -43.199 -8.864  43.624  1.00 39.67 ? 46  ASP   D CB  1 
ATOM   5975 C CG  . ASP   D 1 67  ? -44.532 -8.667  42.919  1.00 46.68 ? 46  ASP   D CG  1 
ATOM   5976 O OD1 . ASP   D 1 67  ? -44.831 -7.504  42.551  1.00 47.52 ? 46  ASP   D OD1 1 
ATOM   5977 O OD2 . ASP   D 1 67  ? -45.249 -9.680  42.718  1.00 55.04 ? 46  ASP   D OD2 1 
ATOM   5978 N N   . GLU   D 1 68  ? -40.170 -8.433  44.480  1.00 34.07 ? 47  GLU   D N   1 
ATOM   5979 C CA  . GLU   D 1 68  ? -39.063 -8.575  45.413  1.00 35.43 ? 47  GLU   D CA  1 
ATOM   5980 C C   . GLU   D 1 68  ? -38.506 -7.219  45.835  1.00 37.34 ? 47  GLU   D C   1 
ATOM   5981 O O   . GLU   D 1 68  ? -38.234 -7.014  47.020  1.00 38.20 ? 47  GLU   D O   1 
ATOM   5982 C CB  . GLU   D 1 68  ? -37.922 -9.461  44.922  1.00 37.43 ? 47  GLU   D CB  1 
ATOM   5983 C CG  . GLU   D 1 68  ? -38.346 -10.900 44.636  1.00 40.74 ? 47  GLU   D CG  1 
ATOM   5984 C CD  . GLU   D 1 68  ? -37.170 -11.730 44.144  0.60 43.31 ? 47  GLU   D CD  1 
ATOM   5985 O OE1 . GLU   D 1 68  ? -36.016 -11.278 44.310  0.60 49.18 ? 47  GLU   D OE1 1 
ATOM   5986 O OE2 . GLU   D 1 68  ? -37.403 -12.817 43.584  0.60 43.01 ? 47  GLU   D OE2 1 
ATOM   5987 N N   . LEU   D 1 69  ? -38.303 -6.308  44.877  1.00 34.36 ? 48  LEU   D N   1 
ATOM   5988 C CA  . LEU   D 1 69  ? -37.747 -4.998  45.198  1.00 35.96 ? 48  LEU   D CA  1 
ATOM   5989 C C   . LEU   D 1 69  ? -38.717 -4.136  46.013  1.00 34.84 ? 48  LEU   D C   1 
ATOM   5990 O O   . LEU   D 1 69  ? -38.305 -3.432  46.938  1.00 34.44 ? 48  LEU   D O   1 
ATOM   5991 C CB  . LEU   D 1 69  ? -37.238 -4.272  43.955  1.00 32.04 ? 48  LEU   D CB  1 
ATOM   5992 C CG  . LEU   D 1 69  ? -36.257 -5.094  43.112  1.00 30.38 ? 48  LEU   D CG  1 
ATOM   5993 C CD1 . LEU   D 1 69  ? -35.835 -4.277  41.904  1.00 30.06 ? 48  LEU   D CD1 1 
ATOM   5994 C CD2 . LEU   D 1 69  ? -35.045 -5.515  43.931  1.00 31.72 ? 48  LEU   D CD2 1 
ATOM   5995 N N   . ASN   D 1 70  ? -39.999 -4.149  45.654  1.00 35.26 ? 49  ASN   D N   1 
ATOM   5996 C CA  . ASN   D 1 70  ? -40.968 -3.331  46.379  1.00 37.46 ? 49  ASN   D CA  1 
ATOM   5997 C C   . ASN   D 1 70  ? -41.222 -3.871  47.794  1.00 40.06 ? 49  ASN   D C   1 
ATOM   5998 O O   . ASN   D 1 70  ? -41.543 -3.091  48.690  1.00 36.21 ? 49  ASN   D O   1 
ATOM   5999 C CB  . ASN   D 1 70  ? -42.285 -3.165  45.624  1.00 34.68 ? 49  ASN   D CB  1 
ATOM   6000 C CG  . ASN   D 1 70  ? -42.173 -2.248  44.433  1.00 32.72 ? 49  ASN   D CG  1 
ATOM   6001 O OD1 . ASN   D 1 70  ? -41.651 -1.127  44.517  1.00 33.51 ? 49  ASN   D OD1 1 
ATOM   6002 N ND2 . ASN   D 1 70  ? -42.704 -2.707  43.320  1.00 30.20 ? 49  ASN   D ND2 1 
ATOM   6003 N N   . LYS   D 1 71  ? -41.080 -5.195  47.979  1.00 38.40 ? 50  LYS   D N   1 
ATOM   6004 C CA  A LYS   D 1 71  ? -41.179 -5.811  49.291  0.50 41.27 ? 50  LYS   D CA  1 
ATOM   6005 C CA  B LYS   D 1 71  ? -41.174 -5.817  49.291  0.50 41.56 ? 50  LYS   D CA  1 
ATOM   6006 C C   . LYS   D 1 71  ? -40.052 -5.280  50.172  1.00 45.10 ? 50  LYS   D C   1 
ATOM   6007 O O   . LYS   D 1 71  ? -40.241 -5.083  51.362  1.00 45.92 ? 50  LYS   D O   1 
ATOM   6008 C CB  A LYS   D 1 71  ? -41.129 -7.341  49.195  0.50 40.67 ? 50  LYS   D CB  1 
ATOM   6009 C CB  B LYS   D 1 71  ? -41.084 -7.348  49.224  0.50 41.48 ? 50  LYS   D CB  1 
ATOM   6010 C CG  A LYS   D 1 71  ? -42.442 -8.042  48.846  0.50 36.54 ? 50  LYS   D CG  1 
ATOM   6011 C CG  B LYS   D 1 71  ? -40.862 -8.081  50.552  0.50 38.23 ? 50  LYS   D CG  1 
ATOM   6012 N N   . GLU   D 1 72  ? -38.882 -5.038  49.564  1.00 41.77 ? 51  GLU   D N   1 
ATOM   6013 C CA  . GLU   D 1 72  ? -37.730 -4.548  50.295  1.00 38.83 ? 51  GLU   D CA  1 
ATOM   6014 C C   . GLU   D 1 72  ? -37.926 -3.063  50.586  1.00 39.66 ? 51  GLU   D C   1 
ATOM   6015 O O   . GLU   D 1 72  ? -37.606 -2.582  51.674  1.00 38.59 ? 51  GLU   D O   1 
ATOM   6016 C CB  . GLU   D 1 72  ? -36.447 -4.884  49.528  1.00 40.20 ? 51  GLU   D CB  1 
ATOM   6017 C CG  . GLU   D 1 72  ? -35.185 -4.370  50.204  0.60 40.27 ? 51  GLU   D CG  1 
ATOM   6018 C CD  . GLU   D 1 72  ? -34.810 -5.259  51.367  0.60 39.24 ? 51  GLU   D CD  1 
ATOM   6019 O OE1 . GLU   D 1 72  ? -34.119 -4.734  52.251  0.60 42.62 ? 51  GLU   D OE1 1 
ATOM   6020 O OE2 . GLU   D 1 72  ? -35.168 -6.454  51.369  0.60 38.15 ? 51  GLU   D OE2 1 
ATOM   6021 N N   . ARG   D 1 73  ? -38.421 -2.324  49.598  1.00 35.42 ? 52  ARG   D N   1 
ATOM   6022 C CA  . ARG   D 1 73  ? -38.650 -0.899  49.784  1.00 38.20 ? 52  ARG   D CA  1 
ATOM   6023 C C   . ARG   D 1 73  ? -39.862 -0.526  48.932  1.00 41.73 ? 52  ARG   D C   1 
ATOM   6024 O O   . ARG   D 1 73  ? -39.783 -0.515  47.710  1.00 37.74 ? 52  ARG   D O   1 
ATOM   6025 C CB  . ARG   D 1 73  ? -37.445 -0.031  49.387  1.00 38.03 ? 52  ARG   D CB  1 
ATOM   6026 C CG  . ARG   D 1 73  ? -36.135 -0.013  50.157  1.00 39.85 ? 52  ARG   D CG  1 
ATOM   6027 C CD  . ARG   D 1 73  ? -35.447 1.353   50.020  1.00 41.86 ? 52  ARG   D CD  1 
ATOM   6028 N NE  . ARG   D 1 73  ? -35.048 1.785   48.670  1.00 43.17 ? 52  ARG   D NE  1 
ATOM   6029 C CZ  . ARG   D 1 73  ? -34.229 1.132   47.851  1.00 44.05 ? 52  ARG   D CZ  1 
ATOM   6030 N NH1 . ARG   D 1 73  ? -33.968 1.619   46.643  1.00 41.17 ? 52  ARG   D NH1 1 
ATOM   6031 N NH2 . ARG   D 1 73  ? -33.679 -0.009  48.243  1.00 42.14 ? 52  ARG   D NH2 1 
ATOM   6032 N N   . SER   D 1 74  ? -41.011 -0.249  49.559  1.00 39.68 ? 53  SER   D N   1 
ATOM   6033 C CA  . SER   D 1 74  ? -42.230 -0.112  48.775  1.00 41.00 ? 53  SER   D CA  1 
ATOM   6034 C C   . SER   D 1 74  ? -42.124 1.058   47.790  1.00 36.63 ? 53  SER   D C   1 
ATOM   6035 O O   . SER   D 1 74  ? -41.436 2.052   48.063  1.00 31.95 ? 53  SER   D O   1 
ATOM   6036 C CB  . SER   D 1 74  ? -43.448 0.013   49.670  1.00 51.99 ? 53  SER   D CB  1 
ATOM   6037 O OG  . SER   D 1 74  ? -43.219 1.075   50.582  1.00 50.56 ? 53  SER   D OG  1 
ATOM   6038 N N   . ASN   D 1 75  ? -42.816 0.919   46.637  1.00 32.66 ? 54  ASN   D N   1 
ATOM   6039 C CA  . ASN   D 1 75  ? -42.934 1.984   45.640  1.00 35.03 ? 54  ASN   D CA  1 
ATOM   6040 C C   . ASN   D 1 75  ? -41.578 2.361   45.018  1.00 32.00 ? 54  ASN   D C   1 
ATOM   6041 O O   . ASN   D 1 75  ? -41.335 3.542   44.714  1.00 30.25 ? 54  ASN   D O   1 
ATOM   6042 C CB  . ASN   D 1 75  ? -43.605 3.219   46.231  1.00 37.91 ? 54  ASN   D CB  1 
ATOM   6043 C CG  . ASN   D 1 75  ? -44.940 2.859   46.836  0.70 41.93 ? 54  ASN   D CG  1 
ATOM   6044 O OD1 . ASN   D 1 75  ? -45.811 2.324   46.138  0.70 39.88 ? 54  ASN   D OD1 1 
ATOM   6045 N ND2 . ASN   D 1 75  ? -45.092 3.103   48.128  0.70 39.14 ? 54  ASN   D ND2 1 
ATOM   6046 N N   . THR   D 1 76  ? -40.700 1.358   44.839  1.00 34.24 ? 55  THR   D N   1 
ATOM   6047 C CA  . THR   D 1 76  ? -39.369 1.628   44.307  1.00 33.90 ? 55  THR   D CA  1 
ATOM   6048 C C   . THR   D 1 76  ? -39.121 0.904   42.973  1.00 35.13 ? 55  THR   D C   1 
ATOM   6049 O O   . THR   D 1 76  ? -38.058 1.078   42.362  1.00 31.01 ? 55  THR   D O   1 
ATOM   6050 C CB  . THR   D 1 76  ? -38.277 1.318   45.339  1.00 31.20 ? 55  THR   D CB  1 
ATOM   6051 O OG1 . THR   D 1 76  ? -38.309 -0.068  45.675  1.00 30.32 ? 55  THR   D OG1 1 
ATOM   6052 C CG2 . THR   D 1 76  ? -38.280 2.236   46.551  1.00 35.85 ? 55  THR   D CG2 1 
ATOM   6053 N N   . ALA   D 1 77  ? -40.071 0.075   42.520  1.00 33.36 ? 56  ALA   D N   1 
ATOM   6054 C CA  . ALA   D 1 77  ? -39.890 -0.662  41.275  1.00 34.39 ? 56  ALA   D CA  1 
ATOM   6055 C C   . ALA   D 1 77  ? -41.182 -0.746  40.451  1.00 34.55 ? 56  ALA   D C   1 
ATOM   6056 O O   . ALA   D 1 77  ? -42.285 -0.904  40.975  1.00 32.69 ? 56  ALA   D O   1 
ATOM   6057 C CB  . ALA   D 1 77  ? -39.249 -2.014  41.505  1.00 30.76 ? 56  ALA   D CB  1 
ATOM   6058 N N   . VAL   D 1 78  ? -41.046 -0.582  39.131  1.00 31.50 ? 57  VAL   D N   1 
ATOM   6059 C CA  . VAL   D 1 78  ? -42.154 -0.745  38.188  1.00 32.96 ? 57  VAL   D CA  1 
ATOM   6060 C C   . VAL   D 1 78  ? -41.615 -1.544  37.010  1.00 34.88 ? 57  VAL   D C   1 
ATOM   6061 O O   . VAL   D 1 78  ? -40.394 -1.553  36.791  1.00 31.80 ? 57  VAL   D O   1 
ATOM   6062 C CB  . VAL   D 1 78  ? -42.777 0.574   37.675  1.00 37.90 ? 57  VAL   D CB  1 
ATOM   6063 C CG1 . VAL   D 1 78  ? -43.504 1.350   38.776  1.00 38.88 ? 57  VAL   D CG1 1 
ATOM   6064 C CG2 . VAL   D 1 78  ? -41.771 1.474   36.944  1.00 31.97 ? 57  VAL   D CG2 1 
ATOM   6065 N N   . VAL   D 1 79  ? -42.516 -2.225  36.290  1.00 31.63 ? 58  VAL   D N   1 
ATOM   6066 C CA  . VAL   D 1 79  ? -42.175 -2.861  35.025  1.00 31.95 ? 58  VAL   D CA  1 
ATOM   6067 C C   . VAL   D 1 79  ? -42.644 -1.991  33.848  1.00 33.25 ? 58  VAL   D C   1 
ATOM   6068 O O   . VAL   D 1 79  ? -43.513 -1.140  34.002  1.00 31.02 ? 58  VAL   D O   1 
ATOM   6069 C CB  . VAL   D 1 79  ? -42.658 -4.322  34.893  1.00 31.31 ? 58  VAL   D CB  1 
ATOM   6070 C CG1 . VAL   D 1 79  ? -42.349 -5.102  36.161  1.00 28.78 ? 58  VAL   D CG1 1 
ATOM   6071 C CG2 . VAL   D 1 79  ? -44.154 -4.435  34.552  1.00 30.36 ? 58  VAL   D CG2 1 
ATOM   6072 N N   . CYS   D 1 80  ? -42.058 -2.207  32.653  1.00 29.62 ? 59  CYS   D N   1 
ATOM   6073 C CA  . CYS   D 1 80  ? -42.506 -1.503  31.452  1.00 31.24 ? 59  CYS   D CA  1 
ATOM   6074 C C   . CYS   D 1 80  ? -42.193 -2.375  30.246  1.00 31.01 ? 59  CYS   D C   1 
ATOM   6075 O O   . CYS   D 1 80  ? -41.021 -2.664  30.002  1.00 32.05 ? 59  CYS   D O   1 
ATOM   6076 C CB  . CYS   D 1 80  ? -41.821 -0.138  31.324  1.00 30.36 ? 59  CYS   D CB  1 
ATOM   6077 S SG  . CYS   D 1 80  ? -42.121 0.712   29.752  1.00 33.62 ? 59  CYS   D SG  1 
ATOM   6078 N N   . GLN   D 1 81  ? -43.236 -2.792  29.507  1.00 29.90 ? 60  GLN   D N   1 
ATOM   6079 C CA  . GLN   D 1 81  ? -43.072 -3.755  28.420  1.00 32.77 ? 60  GLN   D CA  1 
ATOM   6080 C C   . GLN   D 1 81  ? -42.785 -3.010  27.115  1.00 28.98 ? 60  GLN   D C   1 
ATOM   6081 O O   . GLN   D 1 81  ? -43.408 -1.992  26.825  1.00 26.60 ? 60  GLN   D O   1 
ATOM   6082 C CB  . GLN   D 1 81  ? -44.326 -4.619  28.234  1.00 36.32 ? 60  GLN   D CB  1 
ATOM   6083 C CG  . GLN   D 1 81  ? -44.125 -5.898  27.420  1.00 36.57 ? 60  GLN   D CG  1 
ATOM   6084 C CD  . GLN   D 1 81  ? -44.123 -5.704  25.919  1.00 38.29 ? 60  GLN   D CD  1 
ATOM   6085 O OE1 . GLN   D 1 81  ? -44.667 -4.736  25.382  1.00 37.42 ? 60  GLN   D OE1 1 
ATOM   6086 N NE2 . GLN   D 1 81  ? -43.507 -6.640  25.210  1.00 40.74 ? 60  GLN   D NE2 1 
ATOM   6087 N N   . ALA   D 1 82  ? -41.837 -3.521  26.310  1.00 29.19 ? 61  ALA   D N   1 
ATOM   6088 C CA  . ALA   D 1 82  ? -41.580 -2.895  25.012  1.00 27.73 ? 61  ALA   D CA  1 
ATOM   6089 C C   . ALA   D 1 82  ? -40.731 -3.805  24.138  1.00 26.13 ? 61  ALA   D C   1 
ATOM   6090 O O   . ALA   D 1 82  ? -39.763 -4.389  24.611  1.00 23.65 ? 61  ALA   D O   1 
ATOM   6091 C CB  . ALA   D 1 82  ? -40.960 -1.515  25.160  1.00 25.87 ? 61  ALA   D CB  1 
ATOM   6092 N N   . ASP   D 1 83  ? -41.154 -3.923  22.873  1.00 26.53 ? 62  ASP   D N   1 
ATOM   6093 C CA  . ASP   D 1 83  ? -40.403 -4.506  21.783  1.00 27.24 ? 62  ASP   D CA  1 
ATOM   6094 C C   . ASP   D 1 83  ? -39.363 -3.489  21.303  1.00 23.69 ? 62  ASP   D C   1 
ATOM   6095 O O   . ASP   D 1 83  ? -39.698 -2.340  20.965  1.00 24.05 ? 62  ASP   D O   1 
ATOM   6096 C CB  . ASP   D 1 83  ? -41.332 -4.925  20.645  1.00 29.75 ? 62  ASP   D CB  1 
ATOM   6097 C CG  . ASP   D 1 83  ? -40.690 -5.868  19.634  1.00 35.24 ? 62  ASP   D CG  1 
ATOM   6098 O OD1 . ASP   D 1 83  ? -39.456 -6.135  19.735  1.00 33.33 ? 62  ASP   D OD1 1 
ATOM   6099 O OD2 . ASP   D 1 83  ? -41.410 -6.337  18.748  1.00 31.73 ? 62  ASP   D OD2 1 
ATOM   6100 N N   . LEU   D 1 84  ? -38.085 -3.922  21.272  1.00 24.24 ? 63  LEU   D N   1 
ATOM   6101 C CA  . LEU   D 1 84  ? -37.010 -3.018  20.883  1.00 22.73 ? 63  LEU   D CA  1 
ATOM   6102 C C   . LEU   D 1 84  ? -36.481 -3.317  19.471  1.00 25.46 ? 63  LEU   D C   1 
ATOM   6103 O O   . LEU   D 1 84  ? -35.477 -2.740  19.065  1.00 23.72 ? 63  LEU   D O   1 
ATOM   6104 C CB  . LEU   D 1 84  ? -35.914 -2.898  21.955  1.00 22.95 ? 63  LEU   D CB  1 
ATOM   6105 C CG  . LEU   D 1 84  ? -36.352 -2.295  23.302  1.00 23.16 ? 63  LEU   D CG  1 
ATOM   6106 C CD1 . LEU   D 1 84  ? -35.220 -2.294  24.339  1.00 26.17 ? 63  LEU   D CD1 1 
ATOM   6107 C CD2 . LEU   D 1 84  ? -36.886 -0.891  23.163  1.00 25.97 ? 63  LEU   D CD2 1 
ATOM   6108 N N   . THR   D 1 85  ? -37.164 -4.199  18.725  1.00 23.81 ? 64  THR   D N   1 
ATOM   6109 C CA  . THR   D 1 85  ? -37.000 -4.367  17.279  1.00 25.15 ? 64  THR   D CA  1 
ATOM   6110 C C   . THR   D 1 85  ? -37.107 -3.035  16.550  1.00 23.94 ? 64  THR   D C   1 
ATOM   6111 O O   . THR   D 1 85  ? -37.990 -2.225  16.839  1.00 24.33 ? 64  THR   D O   1 
ATOM   6112 C CB  . THR   D 1 85  ? -38.081 -5.292  16.702  1.00 29.82 ? 64  THR   D CB  1 
ATOM   6113 O OG1 . THR   D 1 85  ? -38.042 -6.494  17.451  1.00 30.33 ? 64  THR   D OG1 1 
ATOM   6114 C CG2 . THR   D 1 85  ? -37.819 -5.630  15.243  1.00 27.35 ? 64  THR   D CG2 1 
ATOM   6115 N N   . ASN   D 1 86  ? -36.242 -2.834  15.530  1.00 21.49 ? 65  ASN   D N   1 
ATOM   6116 C CA  . ASN   D 1 86  ? -36.316 -1.619  14.744  1.00 20.33 ? 65  ASN   D CA  1 
ATOM   6117 C C   . ASN   D 1 86  ? -37.636 -1.582  13.946  1.00 24.66 ? 65  ASN   D C   1 
ATOM   6118 O O   . ASN   D 1 86  ? -38.091 -2.601  13.420  1.00 22.28 ? 65  ASN   D O   1 
ATOM   6119 C CB  . ASN   D 1 86  ? -35.113 -1.551  13.810  1.00 22.56 ? 65  ASN   D CB  1 
ATOM   6120 C CG  . ASN   D 1 86  ? -35.015 -0.236  13.085  1.00 25.45 ? 65  ASN   D CG  1 
ATOM   6121 O OD1 . ASN   D 1 86  ? -35.191 0.829   13.699  1.00 24.69 ? 65  ASN   D OD1 1 
ATOM   6122 N ND2 . ASN   D 1 86  ? -34.730 -0.282  11.787  1.00 26.83 ? 65  ASN   D ND2 1 
ATOM   6123 N N   . SER   D 1 87  ? -38.254 -0.395  13.876  1.00 22.96 ? 66  SER   D N   1 
ATOM   6124 C CA  . SER   D 1 87  ? -39.442 -0.135  13.075  1.00 23.79 ? 66  SER   D CA  1 
ATOM   6125 C C   . SER   D 1 87  ? -39.688 1.366   13.115  1.00 22.72 ? 66  SER   D C   1 
ATOM   6126 O O   . SER   D 1 87  ? -39.024 2.074   13.868  1.00 22.52 ? 66  SER   D O   1 
ATOM   6127 C CB  . SER   D 1 87  ? -40.654 -0.859  13.588  1.00 29.75 ? 66  SER   D CB  1 
ATOM   6128 O OG  . SER   D 1 87  ? -41.176 -0.155  14.706  1.00 26.92 ? 66  SER   D OG  1 
ATOM   6129 N N   . ASN   D 1 88  ? -40.687 1.835   12.371  1.00 22.00 ? 67  ASN   D N   1 
ATOM   6130 C CA  . ASN   D 1 88  ? -41.017 3.258   12.404  1.00 22.21 ? 67  ASN   D CA  1 
ATOM   6131 C C   . ASN   D 1 88  ? -41.663 3.709   13.720  1.00 22.81 ? 67  ASN   D C   1 
ATOM   6132 O O   . ASN   D 1 88  ? -41.801 4.912   13.939  1.00 24.87 ? 67  ASN   D O   1 
ATOM   6133 C CB  . ASN   D 1 88  ? -41.848 3.641   11.177  1.00 23.40 ? 67  ASN   D CB  1 
ATOM   6134 C CG  . ASN   D 1 88  ? -40.976 3.687   9.946   1.00 27.18 ? 67  ASN   D CG  1 
ATOM   6135 O OD1 . ASN   D 1 88  ? -39.757 3.889   10.055  1.00 27.60 ? 67  ASN   D OD1 1 
ATOM   6136 N ND2 . ASN   D 1 88  ? -41.586 3.552   8.782   1.00 28.30 ? 67  ASN   D ND2 1 
ATOM   6137 N N   . VAL   D 1 89  ? -42.045 2.775   14.596  1.00 21.77 ? 68  VAL   D N   1 
ATOM   6138 C CA  . VAL   D 1 89  ? -42.609 3.174   15.881  1.00 23.36 ? 68  VAL   D CA  1 
ATOM   6139 C C   . VAL   D 1 89  ? -41.615 2.930   17.022  1.00 25.06 ? 68  VAL   D C   1 
ATOM   6140 O O   . VAL   D 1 89  ? -41.888 3.250   18.179  1.00 22.60 ? 68  VAL   D O   1 
ATOM   6141 C CB  . VAL   D 1 89  ? -43.986 2.562   16.201  1.00 26.34 ? 68  VAL   D CB  1 
ATOM   6142 C CG1 . VAL   D 1 89  ? -44.899 2.728   14.994  1.00 25.71 ? 68  VAL   D CG1 1 
ATOM   6143 C CG2 . VAL   D 1 89  ? -43.884 1.097   16.617  1.00 26.72 ? 68  VAL   D CG2 1 
ATOM   6144 N N   . LEU   D 1 90  ? -40.391 2.505   16.692  1.00 22.37 ? 69  LEU   D N   1 
ATOM   6145 C CA  . LEU   D 1 90  ? -39.425 2.272   17.765  1.00 20.80 ? 69  LEU   D CA  1 
ATOM   6146 C C   . LEU   D 1 90  ? -39.128 3.573   18.517  1.00 21.11 ? 69  LEU   D C   1 
ATOM   6147 O O   . LEU   D 1 90  ? -39.001 3.547   19.742  1.00 25.05 ? 69  LEU   D O   1 
ATOM   6148 C CB  . LEU   D 1 90  ? -38.143 1.594   17.242  1.00 19.83 ? 69  LEU   D CB  1 
ATOM   6149 C CG  . LEU   D 1 90  ? -37.103 1.211   18.309  1.00 20.89 ? 69  LEU   D CG  1 
ATOM   6150 C CD1 . LEU   D 1 90  ? -37.596 0.258   19.393  1.00 20.56 ? 69  LEU   D CD1 1 
ATOM   6151 C CD2 . LEU   D 1 90  ? -35.801 0.662   17.650  1.00 20.12 ? 69  LEU   D CD2 1 
ATOM   6152 N N   . PRO   D 1 91  ? -39.020 4.754   17.863  1.00 18.81 ? 70  PRO   D N   1 
ATOM   6153 C CA  . PRO   D 1 91  ? -38.842 6.000   18.614  1.00 21.63 ? 70  PRO   D CA  1 
ATOM   6154 C C   . PRO   D 1 91  ? -39.904 6.249   19.682  1.00 24.98 ? 70  PRO   D C   1 
ATOM   6155 O O   . PRO   D 1 91  ? -39.579 6.663   20.807  1.00 25.20 ? 70  PRO   D O   1 
ATOM   6156 C CB  . PRO   D 1 91  ? -38.831 7.085   17.566  1.00 18.89 ? 70  PRO   D CB  1 
ATOM   6157 C CG  . PRO   D 1 91  ? -38.358 6.344   16.306  1.00 21.08 ? 70  PRO   D CG  1 
ATOM   6158 C CD  . PRO   D 1 91  ? -39.041 4.976   16.421  1.00 19.20 ? 70  PRO   D CD  1 
ATOM   6159 N N   . ALA   D 1 92  ? -41.171 6.016   19.309  1.00 24.57 ? 71  ALA   D N   1 
ATOM   6160 C CA  . ALA   D 1 92  ? -42.264 6.168   20.267  1.00 24.43 ? 71  ALA   D CA  1 
ATOM   6161 C C   . ALA   D 1 92  ? -42.126 5.177   21.421  1.00 21.29 ? 71  ALA   D C   1 
ATOM   6162 O O   . ALA   D 1 92  ? -42.413 5.550   22.558  1.00 23.37 ? 71  ALA   D O   1 
ATOM   6163 C CB  . ALA   D 1 92  ? -43.632 6.068   19.576  1.00 26.89 ? 71  ALA   D CB  1 
ATOM   6164 N N   . SER   D 1 93  ? -41.742 3.919   21.149  1.00 20.37 ? 72  SER   D N   1 
ATOM   6165 C CA  . SER   D 1 93  ? -41.559 2.956   22.213  1.00 22.17 ? 72  SER   D CA  1 
ATOM   6166 C C   . SER   D 1 93  ? -40.439 3.353   23.175  1.00 23.33 ? 72  SER   D C   1 
ATOM   6167 O O   . SER   D 1 93  ? -40.566 3.173   24.385  1.00 23.30 ? 72  SER   D O   1 
ATOM   6168 C CB  . SER   D 1 93  ? -41.275 1.578   21.677  1.00 23.67 ? 72  SER   D CB  1 
ATOM   6169 O OG  . SER   D 1 93  ? -42.349 1.133   20.861  1.00 29.12 ? 72  SER   D OG  1 
ATOM   6170 N N   . CYS   D 1 94  ? -39.307 3.819   22.628  1.00 25.94 ? 73  CYS   D N   1 
ATOM   6171 C CA  . CYS   D 1 94  ? -38.203 4.272   23.467  1.00 24.39 ? 73  CYS   D CA  1 
ATOM   6172 C C   . CYS   D 1 94  ? -38.626 5.488   24.275  1.00 24.24 ? 73  CYS   D C   1 
ATOM   6173 O O   . CYS   D 1 94  ? -38.307 5.600   25.452  1.00 23.03 ? 73  CYS   D O   1 
ATOM   6174 C CB  . CYS   D 1 94  ? -36.982 4.560   22.602  1.00 21.71 ? 73  CYS   D CB  1 
ATOM   6175 S SG  . CYS   D 1 94  ? -36.427 2.974   21.934  1.00 24.00 ? 73  CYS   D SG  1 
ATOM   6176 N N   . GLU   D 1 95  ? -39.359 6.385   23.624  1.00 26.29 ? 74  GLU   D N   1 
ATOM   6177 C CA  . GLU   D 1 95  ? -39.855 7.572   24.300  1.00 27.22 ? 74  GLU   D CA  1 
ATOM   6178 C C   . GLU   D 1 95  ? -40.753 7.164   25.478  1.00 26.77 ? 74  GLU   D C   1 
ATOM   6179 O O   . GLU   D 1 95  ? -40.664 7.758   26.557  1.00 28.68 ? 74  GLU   D O   1 
ATOM   6180 C CB  . GLU   D 1 95  ? -40.611 8.507   23.359  1.00 29.90 ? 74  GLU   D CB  1 
ATOM   6181 C CG  . GLU   D 1 95  ? -41.082 9.742   24.120  1.00 33.07 ? 74  GLU   D CG  1 
ATOM   6182 C CD  . GLU   D 1 95  ? -41.537 10.939  23.324  0.60 36.59 ? 74  GLU   D CD  1 
ATOM   6183 O OE1 . GLU   D 1 95  ? -40.864 11.377  22.370  0.60 37.01 ? 74  GLU   D OE1 1 
ATOM   6184 O OE2 . GLU   D 1 95  ? -42.574 11.466  23.743  0.60 43.67 ? 74  GLU   D OE2 1 
ATOM   6185 N N   . GLU   D 1 96  ? -41.531 6.097   25.294  1.00 26.05 ? 75  GLU   D N   1 
ATOM   6186 C CA  . GLU   D 1 96  ? -42.471 5.656   26.324  1.00 24.56 ? 75  GLU   D CA  1 
ATOM   6187 C C   . GLU   D 1 96  ? -41.721 5.029   27.503  1.00 29.32 ? 75  GLU   D C   1 
ATOM   6188 O O   . GLU   D 1 96  ? -42.134 5.210   28.640  1.00 25.44 ? 75  GLU   D O   1 
ATOM   6189 C CB  . GLU   D 1 96  ? -43.504 4.729   25.691  1.00 25.92 ? 75  GLU   D CB  1 
ATOM   6190 C CG  . GLU   D 1 96  ? -44.426 4.058   26.705  1.00 30.15 ? 75  GLU   D CG  1 
ATOM   6191 C CD  . GLU   D 1 96  ? -45.200 4.999   27.609  1.00 26.88 ? 75  GLU   D CD  1 
ATOM   6192 O OE1 . GLU   D 1 96  ? -45.630 4.424   28.603  1.00 30.98 ? 75  GLU   D OE1 1 
ATOM   6193 O OE2 . GLU   D 1 96  ? -45.327 6.229   27.364  1.00 29.04 ? 75  GLU   D OE2 1 
ATOM   6194 N N   . ILE   D 1 97  ? -40.652 4.247   27.238  1.00 24.92 ? 76  ILE   D N   1 
ATOM   6195 C CA  . ILE   D 1 97  ? -39.862 3.681   28.322  1.00 23.93 ? 76  ILE   D CA  1 
ATOM   6196 C C   . ILE   D 1 97  ? -39.350 4.806   29.219  1.00 23.95 ? 76  ILE   D C   1 
ATOM   6197 O O   . ILE   D 1 97  ? -39.439 4.690   30.445  1.00 26.47 ? 76  ILE   D O   1 
ATOM   6198 C CB  . ILE   D 1 97  ? -38.695 2.819   27.786  1.00 27.79 ? 76  ILE   D CB  1 
ATOM   6199 C CG1 . ILE   D 1 97  ? -39.226 1.598   27.046  1.00 25.89 ? 76  ILE   D CG1 1 
ATOM   6200 C CG2 . ILE   D 1 97  ? -37.772 2.389   28.939  1.00 24.81 ? 76  ILE   D CG2 1 
ATOM   6201 C CD1 . ILE   D 1 97  ? -38.229 0.923   26.107  1.00 24.05 ? 76  ILE   D CD1 1 
ATOM   6202 N N   . ILE   D 1 98  ? -38.770 5.859   28.631  1.00 24.11 ? 77  ILE   D N   1 
ATOM   6203 C CA  . ILE   D 1 98  ? -38.238 6.964   29.430  1.00 25.47 ? 77  ILE   D CA  1 
ATOM   6204 C C   . ILE   D 1 98  ? -39.397 7.648   30.185  1.00 29.53 ? 77  ILE   D C   1 
ATOM   6205 O O   . ILE   D 1 98  ? -39.268 7.954   31.377  1.00 28.40 ? 77  ILE   D O   1 
ATOM   6206 C CB  . ILE   D 1 98  ? -37.394 7.949   28.587  1.00 24.75 ? 77  ILE   D CB  1 
ATOM   6207 C CG1 . ILE   D 1 98  ? -36.117 7.289   27.942  1.00 22.63 ? 77  ILE   D CG1 1 
ATOM   6208 C CG2 . ILE   D 1 98  ? -37.030 9.228   29.354  1.00 25.50 ? 77  ILE   D CG2 1 
ATOM   6209 C CD1 . ILE   D 1 98  ? -35.251 6.503   28.923  1.00 25.32 ? 77  ILE   D CD1 1 
ATOM   6210 N N   . ASN   D 1 99  ? -40.523 7.908   29.490  1.00 27.50 ? 78  ASN   D N   1 
ATOM   6211 C CA  . ASN   D 1 99  ? -41.718 8.495   30.105  1.00 28.64 ? 78  ASN   D CA  1 
ATOM   6212 C C   . ASN   D 1 99  ? -42.221 7.636   31.262  1.00 28.99 ? 78  ASN   D C   1 
ATOM   6213 O O   . ASN   D 1 99  ? -42.694 8.165   32.262  1.00 32.45 ? 78  ASN   D O   1 
ATOM   6214 C CB  . ASN   D 1 99  ? -42.904 8.623   29.141  1.00 29.11 ? 78  ASN   D CB  1 
ATOM   6215 C CG  . ASN   D 1 99  ? -42.718 9.717   28.125  1.00 35.71 ? 78  ASN   D CG  1 
ATOM   6216 O OD1 . ASN   D 1 99  ? -41.964 10.677  28.349  1.00 40.00 ? 78  ASN   D OD1 1 
ATOM   6217 N ND2 . ASN   D 1 99  ? -43.391 9.585   26.993  1.00 36.15 ? 78  ASN   D ND2 1 
ATOM   6218 N N   . SER   D 1 100 ? -42.112 6.309   31.157  1.00 26.47 ? 79  SER   D N   1 
ATOM   6219 C CA  . SER   D 1 100 ? -42.625 5.513   32.247  1.00 27.99 ? 79  SER   D CA  1 
ATOM   6220 C C   . SER   D 1 100 ? -41.797 5.734   33.515  1.00 33.19 ? 79  SER   D C   1 
ATOM   6221 O O   . SER   D 1 100 ? -42.332 5.617   34.608  1.00 30.60 ? 79  SER   D O   1 
ATOM   6222 C CB  . SER   D 1 100 ? -42.712 4.060   31.874  1.00 30.26 ? 79  SER   D CB  1 
ATOM   6223 O OG  . SER   D 1 100 ? -41.389 3.533   31.901  1.00 39.64 ? 79  SER   D OG  1 
ATOM   6224 N N   . CYS   D 1 101 ? -40.506 6.091   33.384  1.00 28.90 ? 80  CYS   D N   1 
ATOM   6225 C CA  . CYS   D 1 101 ? -39.665 6.359   34.551  1.00 29.00 ? 80  CYS   D CA  1 
ATOM   6226 C C   . CYS   D 1 101 ? -40.099 7.675   35.205  1.00 30.00 ? 80  CYS   D C   1 
ATOM   6227 O O   . CYS   D 1 101 ? -40.211 7.756   36.430  1.00 29.95 ? 80  CYS   D O   1 
ATOM   6228 C CB  . CYS   D 1 101 ? -38.173 6.420   34.190  1.00 24.86 ? 80  CYS   D CB  1 
ATOM   6229 S SG  . CYS   D 1 101 ? -37.055 6.381   35.625  1.00 28.57 ? 80  CYS   D SG  1 
ATOM   6230 N N   . PHE   D 1 102 ? -40.346 8.701   34.383  1.00 28.47 ? 81  PHE   D N   1 
ATOM   6231 C CA  . PHE   D 1 102 ? -40.842 9.981   34.871  1.00 31.06 ? 81  PHE   D CA  1 
ATOM   6232 C C   . PHE   D 1 102 ? -42.221 9.835   35.522  1.00 37.24 ? 81  PHE   D C   1 
ATOM   6233 O O   . PHE   D 1 102 ? -42.488 10.472  36.544  1.00 34.72 ? 81  PHE   D O   1 
ATOM   6234 C CB  . PHE   D 1 102 ? -40.843 11.087  33.813  1.00 29.51 ? 81  PHE   D CB  1 
ATOM   6235 C CG  . PHE   D 1 102 ? -39.448 11.644  33.564  1.00 33.86 ? 81  PHE   D CG  1 
ATOM   6236 C CD1 . PHE   D 1 102 ? -38.551 10.968  32.737  1.00 32.25 ? 81  PHE   D CD1 1 
ATOM   6237 C CD2 . PHE   D 1 102 ? -39.010 12.797  34.215  1.00 34.50 ? 81  PHE   D CD2 1 
ATOM   6238 C CE1 . PHE   D 1 102 ? -37.261 11.443  32.538  1.00 27.33 ? 81  PHE   D CE1 1 
ATOM   6239 C CE2 . PHE   D 1 102 ? -37.723 13.285  34.002  1.00 35.09 ? 81  PHE   D CE2 1 
ATOM   6240 C CZ  . PHE   D 1 102 ? -36.849 12.599  33.172  1.00 33.82 ? 81  PHE   D CZ  1 
ATOM   6241 N N   . ARG   D 1 103 ? -43.080 8.993   34.936  1.00 35.48 ? 82  ARG   D N   1 
ATOM   6242 C CA  . ARG   D 1 103 ? -44.438 8.807   35.437  1.00 36.85 ? 82  ARG   D CA  1 
ATOM   6243 C C   . ARG   D 1 103 ? -44.402 8.150   36.824  1.00 36.22 ? 82  ARG   D C   1 
ATOM   6244 O O   . ARG   D 1 103 ? -45.115 8.571   37.727  1.00 31.39 ? 82  ARG   D O   1 
ATOM   6245 C CB  . ARG   D 1 103 ? -45.235 8.006   34.401  1.00 35.35 ? 82  ARG   D CB  1 
ATOM   6246 C CG  . ARG   D 1 103 ? -46.745 8.184   34.326  0.80 40.58 ? 82  ARG   D CG  1 
ATOM   6247 C CD  . ARG   D 1 103 ? -47.305 7.878   32.935  0.80 33.08 ? 82  ARG   D CD  1 
ATOM   6248 N NE  . ARG   D 1 103 ? -47.094 6.450   32.690  0.80 31.50 ? 82  ARG   D NE  1 
ATOM   6249 C CZ  . ARG   D 1 103 ? -46.498 5.931   31.610  0.80 28.55 ? 82  ARG   D CZ  1 
ATOM   6250 N NH1 . ARG   D 1 103 ? -46.297 4.633   31.523  0.80 29.97 ? 82  ARG   D NH1 1 
ATOM   6251 N NH2 . ARG   D 1 103 ? -46.130 6.710   30.624  0.80 26.87 ? 82  ARG   D NH2 1 
ATOM   6252 N N   . ALA   D 1 104 ? -43.568 7.116   37.008  1.00 28.93 ? 83  ALA   D N   1 
ATOM   6253 C CA  . ALA   D 1 104 ? -43.486 6.434   38.292  1.00 33.71 ? 83  ALA   D CA  1 
ATOM   6254 C C   . ALA   D 1 104 ? -42.689 7.231   39.330  1.00 34.94 ? 83  ALA   D C   1 
ATOM   6255 O O   . ALA   D 1 104 ? -43.033 7.178   40.511  1.00 31.73 ? 83  ALA   D O   1 
ATOM   6256 C CB  . ALA   D 1 104 ? -42.910 5.042   38.133  1.00 33.87 ? 83  ALA   D CB  1 
ATOM   6257 N N   . PHE   D 1 105 ? -41.613 7.934   38.916  1.00 31.47 ? 84  PHE   D N   1 
ATOM   6258 C CA  . PHE   D 1 105 ? -40.612 8.332   39.897  1.00 29.06 ? 84  PHE   D CA  1 
ATOM   6259 C C   . PHE   D 1 105 ? -40.364 9.824   39.859  1.00 27.07 ? 84  PHE   D C   1 
ATOM   6260 O O   . PHE   D 1 105 ? -39.723 10.355  40.764  1.00 32.86 ? 84  PHE   D O   1 
ATOM   6261 C CB  . PHE   D 1 105 ? -39.275 7.598   39.768  1.00 27.21 ? 84  PHE   D CB  1 
ATOM   6262 C CG  . PHE   D 1 105 ? -39.473 6.102   39.963  1.00 28.74 ? 84  PHE   D CG  1 
ATOM   6263 C CD1 . PHE   D 1 105 ? -40.196 5.621   41.044  1.00 26.62 ? 84  PHE   D CD1 1 
ATOM   6264 C CD2 . PHE   D 1 105 ? -39.012 5.196   39.015  1.00 28.62 ? 84  PHE   D CD2 1 
ATOM   6265 C CE1 . PHE   D 1 105 ? -40.404 4.265   41.221  1.00 26.43 ? 84  PHE   D CE1 1 
ATOM   6266 C CE2 . PHE   D 1 105 ? -39.201 3.824   39.200  1.00 28.64 ? 84  PHE   D CE2 1 
ATOM   6267 C CZ  . PHE   D 1 105 ? -39.893 3.362   40.301  1.00 31.64 ? 84  PHE   D CZ  1 
ATOM   6268 N N   . GLY   D 1 106 ? -40.858 10.500  38.826  1.00 27.14 ? 85  GLY   D N   1 
ATOM   6269 C CA  . GLY   D 1 106 ? -40.662 11.949  38.766  1.00 28.61 ? 85  GLY   D CA  1 
ATOM   6270 C C   . GLY   D 1 106 ? -39.287 12.378  38.235  1.00 30.50 ? 85  GLY   D C   1 
ATOM   6271 O O   . GLY   D 1 106 ? -38.999 13.573  38.114  1.00 29.44 ? 85  GLY   D O   1 
ATOM   6272 N N   . ARG   D 1 107 ? -38.448 11.409  37.848  1.00 29.82 ? 86  ARG   D N   1 
ATOM   6273 C CA  . ARG   D 1 107 ? -37.106 11.748  37.382  1.00 27.54 ? 86  ARG   D CA  1 
ATOM   6274 C C   . ARG   D 1 107 ? -36.533 10.501  36.722  1.00 26.71 ? 86  ARG   D C   1 
ATOM   6275 O O   . ARG   D 1 107 ? -37.023 9.386   36.963  1.00 25.85 ? 86  ARG   D O   1 
ATOM   6276 C CB  . ARG   D 1 107 ? -36.192 12.201  38.545  1.00 26.47 ? 86  ARG   D CB  1 
ATOM   6277 C CG  . ARG   D 1 107 ? -36.148 11.142  39.646  1.00 30.28 ? 86  ARG   D CG  1 
ATOM   6278 C CD  . ARG   D 1 107 ? -35.477 11.522  40.968  1.00 33.44 ? 86  ARG   D CD  1 
ATOM   6279 N NE  . ARG   D 1 107 ? -34.077 11.953  40.793  1.00 32.66 ? 86  ARG   D NE  1 
ATOM   6280 C CZ  . ARG   D 1 107 ? -33.314 12.535  41.711  1.00 36.09 ? 86  ARG   D CZ  1 
ATOM   6281 N NH1 . ARG   D 1 107 ? -33.845 12.859  42.883  1.00 34.69 ? 86  ARG   D NH1 1 
ATOM   6282 N NH2 . ARG   D 1 107 ? -32.035 12.779  41.471  1.00 33.21 ? 86  ARG   D NH2 1 
ATOM   6283 N N   . CYS   D 1 108 ? -35.432 10.713  35.983  1.00 29.51 ? 87  CYS   D N   1 
ATOM   6284 C CA  . CYS   D 1 108 ? -34.686 9.627   35.368  1.00 26.87 ? 87  CYS   D CA  1 
ATOM   6285 C C   . CYS   D 1 108 ? -33.201 9.995   35.348  1.00 25.79 ? 87  CYS   D C   1 
ATOM   6286 O O   . CYS   D 1 108 ? -32.800 10.896  34.612  1.00 26.93 ? 87  CYS   D O   1 
ATOM   6287 C CB  . CYS   D 1 108 ? -35.171 9.399   33.941  1.00 25.96 ? 87  CYS   D CB  1 
ATOM   6288 S SG  . CYS   D 1 108 ? -34.516 7.847   33.277  1.00 27.85 ? 87  CYS   D SG  1 
ATOM   6289 N N   . ASP   D 1 109 ? -32.417 9.329   36.215  1.00 26.13 ? 88  ASP   D N   1 
ATOM   6290 C CA  . ASP   D 1 109 ? -31.026 9.693   36.463  1.00 25.23 ? 88  ASP   D CA  1 
ATOM   6291 C C   . ASP   D 1 109 ? -30.066 8.779   35.692  1.00 23.01 ? 88  ASP   D C   1 
ATOM   6292 O O   . ASP   D 1 109 ? -29.018 9.237   35.251  1.00 23.89 ? 88  ASP   D O   1 
ATOM   6293 C CB  . ASP   D 1 109 ? -30.741 9.631   37.962  1.00 28.12 ? 88  ASP   D CB  1 
ATOM   6294 C CG  . ASP   D 1 109 ? -31.636 10.567  38.772  1.00 31.64 ? 88  ASP   D CG  1 
ATOM   6295 O OD1 . ASP   D 1 109 ? -31.303 11.780  38.878  1.00 32.35 ? 88  ASP   D OD1 1 
ATOM   6296 O OD2 . ASP   D 1 109 ? -32.702 10.095  39.204  1.00 30.03 ? 88  ASP   D OD2 1 
ATOM   6297 N N   . VAL   D 1 110 ? -30.420 7.486   35.565  1.00 22.61 ? 89  VAL   D N   1 
ATOM   6298 C CA  . VAL   D 1 110 ? -29.575 6.488   34.922  1.00 23.76 ? 89  VAL   D CA  1 
ATOM   6299 C C   . VAL   D 1 110 ? -30.361 5.675   33.888  1.00 26.24 ? 89  VAL   D C   1 
ATOM   6300 O O   . VAL   D 1 110 ? -31.507 5.282   34.108  1.00 25.13 ? 89  VAL   D O   1 
ATOM   6301 C CB  . VAL   D 1 110 ? -28.935 5.578   35.975  1.00 22.10 ? 89  VAL   D CB  1 
ATOM   6302 C CG1 . VAL   D 1 110 ? -28.380 4.298   35.362  1.00 23.68 ? 89  VAL   D CG1 1 
ATOM   6303 C CG2 . VAL   D 1 110 ? -27.889 6.331   36.808  1.00 22.55 ? 89  VAL   D CG2 1 
ATOM   6304 N N   . LEU   D 1 111 ? -29.731 5.457   32.727  1.00 22.82 ? 90  LEU   D N   1 
ATOM   6305 C CA  . LEU   D 1 111 ? -30.233 4.547   31.704  1.00 22.69 ? 90  LEU   D CA  1 
ATOM   6306 C C   . LEU   D 1 111 ? -29.167 3.486   31.460  1.00 23.64 ? 90  LEU   D C   1 
ATOM   6307 O O   . LEU   D 1 111 ? -28.020 3.851   31.185  1.00 22.80 ? 90  LEU   D O   1 
ATOM   6308 C CB  . LEU   D 1 111 ? -30.501 5.335   30.419  1.00 22.85 ? 90  LEU   D CB  1 
ATOM   6309 C CG  . LEU   D 1 111 ? -30.694 4.501   29.138  1.00 21.87 ? 90  LEU   D CG  1 
ATOM   6310 C CD1 . LEU   D 1 111 ? -31.934 3.593   29.247  1.00 20.97 ? 90  LEU   D CD1 1 
ATOM   6311 C CD2 . LEU   D 1 111 ? -30.733 5.361   27.894  1.00 20.40 ? 90  LEU   D CD2 1 
ATOM   6312 N N   . VAL   D 1 112 ? -29.555 2.208   31.581  1.00 21.45 ? 91  VAL   D N   1 
ATOM   6313 C CA  . VAL   D 1 112 ? -28.676 1.082   31.288  1.00 22.96 ? 91  VAL   D CA  1 
ATOM   6314 C C   . VAL   D 1 112 ? -29.231 0.366   30.062  1.00 22.86 ? 91  VAL   D C   1 
ATOM   6315 O O   . VAL   D 1 112 ? -30.302 -0.228  30.141  1.00 21.80 ? 91  VAL   D O   1 
ATOM   6316 C CB  . VAL   D 1 112 ? -28.485 0.087   32.451  1.00 23.64 ? 91  VAL   D CB  1 
ATOM   6317 C CG1 . VAL   D 1 112 ? -27.535 -1.065  32.063  1.00 22.29 ? 91  VAL   D CG1 1 
ATOM   6318 C CG2 . VAL   D 1 112 ? -27.960 0.820   33.692  1.00 21.24 ? 91  VAL   D CG2 1 
ATOM   6319 N N   . ASN   D 1 113 ? -28.511 0.457   28.928  1.00 22.29 ? 92  ASN   D N   1 
ATOM   6320 C CA  . ASN   D 1 113 ? -28.902 -0.223  27.700  1.00 21.63 ? 92  ASN   D CA  1 
ATOM   6321 C C   . ASN   D 1 113 ? -28.355 -1.651  27.712  1.00 22.87 ? 92  ASN   D C   1 
ATOM   6322 O O   . ASN   D 1 113 ? -27.221 -1.898  27.286  1.00 22.43 ? 92  ASN   D O   1 
ATOM   6323 C CB  . ASN   D 1 113 ? -28.454 0.541   26.453  1.00 22.64 ? 92  ASN   D CB  1 
ATOM   6324 C CG  . ASN   D 1 113 ? -29.268 1.793   26.212  1.00 24.86 ? 92  ASN   D CG  1 
ATOM   6325 O OD1 . ASN   D 1 113 ? -30.506 1.714   26.116  1.00 23.48 ? 92  ASN   D OD1 1 
ATOM   6326 N ND2 . ASN   D 1 113 ? -28.604 2.941   26.126  1.00 20.48 ? 92  ASN   D ND2 1 
ATOM   6327 N N   . ASN   D 1 114 ? -29.177 -2.592  28.166  1.00 22.19 ? 93  ASN   D N   1 
ATOM   6328 C CA  . ASN   D 1 114 ? -28.771 -3.969  28.431  1.00 22.87 ? 93  ASN   D CA  1 
ATOM   6329 C C   . ASN   D 1 114 ? -29.446 -4.943  27.456  1.00 24.19 ? 93  ASN   D C   1 
ATOM   6330 O O   . ASN   D 1 114 ? -28.844 -5.966  27.119  1.00 24.11 ? 93  ASN   D O   1 
ATOM   6331 C CB  . ASN   D 1 114 ? -29.071 -4.362  29.890  1.00 25.85 ? 93  ASN   D CB  1 
ATOM   6332 C CG  . ASN   D 1 114 ? -28.901 -5.843  30.161  1.00 26.79 ? 93  ASN   D CG  1 
ATOM   6333 O OD1 . ASN   D 1 114 ? -27.776 -6.319  30.378  1.00 25.69 ? 93  ASN   D OD1 1 
ATOM   6334 N ND2 . ASN   D 1 114 ? -29.987 -6.610  30.100  1.00 25.74 ? 93  ASN   D ND2 1 
ATOM   6335 N N   . ALA   D 1 115 ? -30.717 -4.689  27.073  1.00 25.19 ? 94  ALA   D N   1 
ATOM   6336 C CA  . ALA   D 1 115 ? -31.460 -5.624  26.222  1.00 25.46 ? 94  ALA   D CA  1 
ATOM   6337 C C   . ALA   D 1 115 ? -30.687 -5.921  24.935  1.00 26.76 ? 94  ALA   D C   1 
ATOM   6338 O O   . ALA   D 1 115 ? -30.142 -5.021  24.302  1.00 25.43 ? 94  ALA   D O   1 
ATOM   6339 C CB  . ALA   D 1 115 ? -32.829 -5.072  25.862  1.00 22.93 ? 94  ALA   D CB  1 
ATOM   6340 N N   . SER   D 1 116 ? -30.732 -7.182  24.508  1.00 25.30 ? 95  SER   D N   1 
ATOM   6341 C CA  . SER   D 1 116 ? -29.946 -7.565  23.346  1.00 27.91 ? 95  SER   D CA  1 
ATOM   6342 C C   . SER   D 1 116 ? -30.520 -8.833  22.730  1.00 27.62 ? 95  SER   D C   1 
ATOM   6343 O O   . SER   D 1 116 ? -30.762 -9.808  23.444  1.00 29.77 ? 95  SER   D O   1 
ATOM   6344 C CB  . SER   D 1 116 ? -28.511 -7.760  23.746  1.00 31.04 ? 95  SER   D CB  1 
ATOM   6345 O OG  . SER   D 1 116 ? -27.773 -8.425  22.726  1.00 33.04 ? 95  SER   D OG  1 
ATOM   6346 N N   . ALA   D 1 117 ? -30.715 -8.801  21.406  1.00 27.56 ? 96  ALA   D N   1 
ATOM   6347 C CA  . ALA   D 1 117 ? -31.002 -9.984  20.610  1.00 24.95 ? 96  ALA   D CA  1 
ATOM   6348 C C   . ALA   D 1 117 ? -29.667 -10.575 20.146  1.00 27.45 ? 96  ALA   D C   1 
ATOM   6349 O O   . ALA   D 1 117 ? -28.726 -9.824  19.853  1.00 24.66 ? 96  ALA   D O   1 
ATOM   6350 C CB  . ALA   D 1 117 ? -31.883 -9.578  19.425  1.00 26.18 ? 96  ALA   D CB  1 
ATOM   6351 N N   . PHE   D 1 118 ? -29.581 -11.916 20.103  1.00 24.91 ? 97  PHE   D N   1 
ATOM   6352 C CA  . PHE   D 1 118 ? -28.329 -12.589 19.808  1.00 30.19 ? 97  PHE   D CA  1 
ATOM   6353 C C   . PHE   D 1 118 ? -28.650 -13.938 19.168  1.00 29.48 ? 97  PHE   D C   1 
ATOM   6354 O O   . PHE   D 1 118 ? -29.289 -14.794 19.772  1.00 30.96 ? 97  PHE   D O   1 
ATOM   6355 C CB  . PHE   D 1 118 ? -27.448 -12.744 21.060  1.00 30.95 ? 97  PHE   D CB  1 
ATOM   6356 C CG  . PHE   D 1 118 ? -26.189 -13.597 20.897  1.00 33.50 ? 97  PHE   D CG  1 
ATOM   6357 C CD1 . PHE   D 1 118 ? -26.222 -14.976 21.093  1.00 36.38 ? 97  PHE   D CD1 1 
ATOM   6358 C CD2 . PHE   D 1 118 ? -24.972 -13.018 20.541  1.00 32.61 ? 97  PHE   D CD2 1 
ATOM   6359 C CE1 . PHE   D 1 118 ? -25.067 -15.740 20.951  1.00 38.96 ? 97  PHE   D CE1 1 
ATOM   6360 C CE2 . PHE   D 1 118 ? -23.815 -13.785 20.399  1.00 29.58 ? 97  PHE   D CE2 1 
ATOM   6361 C CZ  . PHE   D 1 118 ? -23.855 -15.143 20.622  1.00 34.83 ? 97  PHE   D CZ  1 
ATOM   6362 N N   . TYR   D 1 119 ? -28.250 -14.083 17.907  1.00 25.80 ? 98  TYR   D N   1 
ATOM   6363 C CA  . TYR   D 1 119 ? -28.451 -15.310 17.154  1.00 26.95 ? 98  TYR   D CA  1 
ATOM   6364 C C   . TYR   D 1 119 ? -27.649 -15.173 15.865  1.00 25.45 ? 98  TYR   D C   1 
ATOM   6365 O O   . TYR   D 1 119 ? -27.352 -14.056 15.441  1.00 25.27 ? 98  TYR   D O   1 
ATOM   6366 C CB  . TYR   D 1 119 ? -29.884 -15.760 16.832  1.00 27.47 ? 98  TYR   D CB  1 
ATOM   6367 C CG  . TYR   D 1 119 ? -30.765 -14.690 16.208  1.00 26.75 ? 98  TYR   D CG  1 
ATOM   6368 C CD1 . TYR   D 1 119 ? -30.838 -14.518 14.827  1.00 26.89 ? 98  TYR   D CD1 1 
ATOM   6369 C CD2 . TYR   D 1 119 ? -31.555 -13.870 17.013  1.00 28.13 ? 98  TYR   D CD2 1 
ATOM   6370 C CE1 . TYR   D 1 119 ? -31.656 -13.547 14.277  1.00 29.15 ? 98  TYR   D CE1 1 
ATOM   6371 C CE2 . TYR   D 1 119 ? -32.384 -12.900 16.471  1.00 28.11 ? 98  TYR   D CE2 1 
ATOM   6372 C CZ  . TYR   D 1 119 ? -32.442 -12.746 15.095  1.00 27.45 ? 98  TYR   D CZ  1 
ATOM   6373 O OH  . TYR   D 1 119 ? -33.231 -11.756 14.573  1.00 26.60 ? 98  TYR   D OH  1 
ATOM   6374 N N   . PRO   D 1 120 ? -27.249 -16.304 15.250  1.00 27.38 ? 99  PRO   D N   1 
ATOM   6375 C CA  . PRO   D 1 120 ? -26.449 -16.284 14.025  1.00 27.20 ? 99  PRO   D CA  1 
ATOM   6376 C C   . PRO   D 1 120 ? -27.294 -15.789 12.857  1.00 28.56 ? 99  PRO   D C   1 
ATOM   6377 O O   . PRO   D 1 120 ? -28.488 -16.083 12.797  1.00 29.91 ? 99  PRO   D O   1 
ATOM   6378 C CB  . PRO   D 1 120 ? -25.978 -17.743 13.802  1.00 26.26 ? 99  PRO   D CB  1 
ATOM   6379 C CG  . PRO   D 1 120 ? -26.824 -18.584 14.756  1.00 26.76 ? 99  PRO   D CG  1 
ATOM   6380 C CD  . PRO   D 1 120 ? -27.529 -17.674 15.731  1.00 27.53 ? 99  PRO   D CD  1 
ATOM   6381 N N   . THR   D 1 121 ? -26.645 -15.056 11.942  1.00 22.91 ? 100 THR   D N   1 
ATOM   6382 C CA  . THR   D 1 121 ? -27.212 -14.589 10.694  1.00 23.22 ? 100 THR   D CA  1 
ATOM   6383 C C   . THR   D 1 121 ? -26.184 -14.848 9.604   1.00 27.41 ? 100 THR   D C   1 
ATOM   6384 O O   . THR   D 1 121 ? -25.500 -13.908 9.193   1.00 25.98 ? 100 THR   D O   1 
ATOM   6385 C CB  . THR   D 1 121 ? -27.502 -13.088 10.806  1.00 26.14 ? 100 THR   D CB  1 
ATOM   6386 O OG1 . THR   D 1 121 ? -26.287 -12.395 11.107  1.00 24.16 ? 100 THR   D OG1 1 
ATOM   6387 C CG2 . THR   D 1 121 ? -28.543 -12.756 11.867  1.00 24.16 ? 100 THR   D CG2 1 
ATOM   6388 N N   . PRO   D 1 122 ? -26.007 -16.114 9.138   1.00 27.25 ? 101 PRO   D N   1 
ATOM   6389 C CA  . PRO   D 1 122 ? -24.962 -16.432 8.167   1.00 29.07 ? 101 PRO   D CA  1 
ATOM   6390 C C   . PRO   D 1 122 ? -25.104 -15.618 6.884   1.00 28.70 ? 101 PRO   D C   1 
ATOM   6391 O O   . PRO   D 1 122 ? -26.209 -15.375 6.423   1.00 26.19 ? 101 PRO   D O   1 
ATOM   6392 C CB  . PRO   D 1 122 ? -25.063 -17.970 7.886   1.00 29.49 ? 101 PRO   D CB  1 
ATOM   6393 C CG  . PRO   D 1 122 ? -26.317 -18.407 8.617   1.00 30.70 ? 101 PRO   D CG  1 
ATOM   6394 C CD  . PRO   D 1 122 ? -26.771 -17.300 9.557   1.00 27.71 ? 101 PRO   D CD  1 
ATOM   6395 N N   . LEU   D 1 123 ? -23.965 -15.256 6.293   1.00 26.98 ? 102 LEU   D N   1 
ATOM   6396 C CA  . LEU   D 1 123 ? -23.938 -14.539 5.033   1.00 28.95 ? 102 LEU   D CA  1 
ATOM   6397 C C   . LEU   D 1 123 ? -24.286 -15.477 3.872   1.00 34.43 ? 102 LEU   D C   1 
ATOM   6398 O O   . LEU   D 1 123 ? -24.808 -15.018 2.862   1.00 33.35 ? 102 LEU   D O   1 
ATOM   6399 C CB  . LEU   D 1 123 ? -22.552 -13.935 4.838   1.00 26.30 ? 102 LEU   D CB  1 
ATOM   6400 C CG  . LEU   D 1 123 ? -22.227 -12.757 5.770   1.00 28.14 ? 102 LEU   D CG  1 
ATOM   6401 C CD1 . LEU   D 1 123 ? -20.773 -12.304 5.603   1.00 22.47 ? 102 LEU   D CD1 1 
ATOM   6402 C CD2 . LEU   D 1 123 ? -23.194 -11.647 5.466   1.00 24.76 ? 102 LEU   D CD2 1 
ATOM   6403 N N   . VAL   D 1 124 ? -23.941 -16.769 4.002   1.00 32.50 ? 103 VAL   D N   1 
ATOM   6404 C CA  . VAL   D 1 124 ? -24.117 -17.718 2.905   1.00 38.83 ? 103 VAL   D CA  1 
ATOM   6405 C C   . VAL   D 1 124 ? -25.084 -18.843 3.319   1.00 42.16 ? 103 VAL   D C   1 
ATOM   6406 O O   . VAL   D 1 124 ? -24.931 -19.318 4.455   1.00 42.74 ? 103 VAL   D O   1 
ATOM   6407 C CB  . VAL   D 1 124 ? -22.770 -18.245 2.371   1.00 38.87 ? 103 VAL   D CB  1 
ATOM   6408 C CG1 . VAL   D 1 124 ? -22.921 -19.532 1.577   1.00 53.57 ? 103 VAL   D CG1 1 
ATOM   6409 C CG2 . VAL   D 1 124 ? -22.096 -17.202 1.498   1.00 38.33 ? 103 VAL   D CG2 1 
ATOM   6410 N N   . GLY   D 1 134 ? -35.770 -19.196 11.258  1.00 73.11 ? 113 GLY   D N   1 
ATOM   6411 C CA  . GLY   D 1 134 ? -36.833 -19.127 10.234  1.00 63.65 ? 113 GLY   D CA  1 
ATOM   6412 C C   . GLY   D 1 134 ? -37.258 -17.687 9.935   1.00 58.56 ? 113 GLY   D C   1 
ATOM   6413 O O   . GLY   D 1 134 ? -38.260 -17.464 9.257   1.00 54.86 ? 113 GLY   D O   1 
ATOM   6414 N N   . LYS   D 1 135 ? -36.487 -16.712 10.438  1.00 50.95 ? 114 LYS   D N   1 
ATOM   6415 C CA  . LYS   D 1 135 ? -36.815 -15.307 10.262  1.00 43.52 ? 114 LYS   D CA  1 
ATOM   6416 C C   . LYS   D 1 135 ? -36.344 -14.846 8.890   1.00 37.32 ? 114 LYS   D C   1 
ATOM   6417 O O   . LYS   D 1 135 ? -35.345 -15.346 8.395   1.00 41.28 ? 114 LYS   D O   1 
ATOM   6418 C CB  . LYS   D 1 135 ? -36.098 -14.519 11.363  1.00 47.25 ? 114 LYS   D CB  1 
ATOM   6419 C CG  . LYS   D 1 135 ? -36.492 -14.889 12.786  1.00 46.20 ? 114 LYS   D CG  1 
ATOM   6420 C CD  . LYS   D 1 135 ? -35.406 -14.419 13.743  1.00 54.69 ? 114 LYS   D CD  1 
ATOM   6421 C CE  . LYS   D 1 135 ? -35.617 -14.819 15.171  1.00 53.04 ? 114 LYS   D CE  1 
ATOM   6422 N NZ  . LYS   D 1 135 ? -36.578 -13.897 15.772  1.00 53.33 ? 114 LYS   D NZ  1 
ATOM   6423 N N   . THR   D 1 136 ? -37.036 -13.864 8.290   1.00 32.21 ? 115 THR   D N   1 
ATOM   6424 C CA  . THR   D 1 136 ? -36.560 -13.241 7.066   1.00 33.17 ? 115 THR   D CA  1 
ATOM   6425 C C   . THR   D 1 136 ? -35.327 -12.400 7.388   1.00 31.30 ? 115 THR   D C   1 
ATOM   6426 O O   . THR   D 1 136 ? -35.086 -12.071 8.554   1.00 28.35 ? 115 THR   D O   1 
ATOM   6427 C CB  . THR   D 1 136 ? -37.618 -12.329 6.449   1.00 32.00 ? 115 THR   D CB  1 
ATOM   6428 O OG1 . THR   D 1 136 ? -37.855 -11.386 7.491   1.00 32.26 ? 115 THR   D OG1 1 
ATOM   6429 C CG2 . THR   D 1 136 ? -38.891 -13.068 6.054   1.00 40.84 ? 115 THR   D CG2 1 
ATOM   6430 N N   . VAL   D 1 137 ? -34.602 -12.008 6.342   1.00 30.50 ? 116 VAL   D N   1 
ATOM   6431 C CA  . VAL   D 1 137 ? -33.414 -11.183 6.561   1.00 30.08 ? 116 VAL   D CA  1 
ATOM   6432 C C   . VAL   D 1 137 ? -33.854 -9.820  7.118   1.00 30.03 ? 116 VAL   D C   1 
ATOM   6433 O O   . VAL   D 1 137 ? -33.193 -9.229  7.971   1.00 28.34 ? 116 VAL   D O   1 
ATOM   6434 C CB  . VAL   D 1 137 ? -32.484 -11.070 5.332   1.00 29.68 ? 116 VAL   D CB  1 
ATOM   6435 C CG1 . VAL   D 1 137 ? -33.180 -10.482 4.108   1.00 36.24 ? 116 VAL   D CG1 1 
ATOM   6436 C CG2 . VAL   D 1 137 ? -31.265 -10.219 5.637   1.00 31.22 ? 116 VAL   D CG2 1 
ATOM   6437 N N   . GLU   D 1 138 ? -35.014 -9.331  6.671   1.00 27.85 ? 117 GLU   D N   1 
ATOM   6438 C CA  . GLU   D 1 138 ? -35.567 -8.072  7.166   1.00 33.09 ? 117 GLU   D CA  1 
ATOM   6439 C C   . GLU   D 1 138 ? -35.767 -8.100  8.683   1.00 28.26 ? 117 GLU   D C   1 
ATOM   6440 O O   . GLU   D 1 138 ? -35.485 -7.107  9.362   1.00 27.93 ? 117 GLU   D O   1 
ATOM   6441 C CB  . GLU   D 1 138 ? -36.811 -7.564  6.415   1.00 37.83 ? 117 GLU   D CB  1 
ATOM   6442 C CG  . GLU   D 1 138 ? -37.568 -8.608  5.605   0.70 39.67 ? 117 GLU   D CG  1 
ATOM   6443 C CD  . GLU   D 1 138 ? -36.929 -9.162  4.340   0.70 36.39 ? 117 GLU   D CD  1 
ATOM   6444 O OE1 . GLU   D 1 138 ? -36.936 -8.541  3.271   0.70 40.81 ? 117 GLU   D OE1 1 
ATOM   6445 O OE2 . GLU   D 1 138 ? -36.395 -10.269 4.439   0.70 39.60 ? 117 GLU   D OE2 1 
ATOM   6446 N N   . THR   D 1 139 ? -36.273 -9.223  9.198   1.00 25.17 ? 118 THR   D N   1 
ATOM   6447 C CA  . THR   D 1 139 ? -36.541 -9.401  10.619  1.00 27.79 ? 118 THR   D CA  1 
ATOM   6448 C C   . THR   D 1 139 ? -35.212 -9.451  11.379  1.00 25.88 ? 118 THR   D C   1 
ATOM   6449 O O   . THR   D 1 139 ? -35.097 -8.838  12.442  1.00 23.59 ? 118 THR   D O   1 
ATOM   6450 C CB  . THR   D 1 139 ? -37.350 -10.682 10.874  1.00 30.45 ? 118 THR   D CB  1 
ATOM   6451 O OG1 . THR   D 1 139 ? -38.624 -10.401 10.311  1.00 33.60 ? 118 THR   D OG1 1 
ATOM   6452 C CG2 . THR   D 1 139 ? -37.537 -10.984 12.356  1.00 31.92 ? 118 THR   D CG2 1 
ATOM   6453 N N   . GLN   D 1 140 ? -34.253 -10.230 10.848  1.00 25.50 ? 119 GLN   D N   1 
ATOM   6454 C CA  . GLN   D 1 140 ? -32.918 -10.390 11.424  1.00 24.51 ? 119 GLN   D CA  1 
ATOM   6455 C C   . GLN   D 1 140 ? -32.264 -9.025  11.633  1.00 23.70 ? 119 GLN   D C   1 
ATOM   6456 O O   . GLN   D 1 140 ? -31.790 -8.728  12.742  1.00 24.10 ? 119 GLN   D O   1 
ATOM   6457 C CB  . GLN   D 1 140 ? -32.049 -11.243 10.509  1.00 27.77 ? 119 GLN   D CB  1 
ATOM   6458 C CG  . GLN   D 1 140 ? -32.406 -12.728 10.523  1.00 29.09 ? 119 GLN   D CG  1 
ATOM   6459 C CD  . GLN   D 1 140 ? -31.748 -13.474 9.379   1.00 34.79 ? 119 GLN   D CD  1 
ATOM   6460 O OE1 . GLN   D 1 140 ? -30.541 -13.362 9.154   1.00 39.33 ? 119 GLN   D OE1 1 
ATOM   6461 N NE2 . GLN   D 1 140 ? -32.534 -14.162 8.570   1.00 39.52 ? 119 GLN   D NE2 1 
ATOM   6462 N N   . VAL   D 1 141 ? -32.310 -8.195  10.590  1.00 21.94 ? 120 VAL   D N   1 
ATOM   6463 C CA  . VAL   D 1 141 ? -31.779 -6.838  10.645  1.00 23.14 ? 120 VAL   D CA  1 
ATOM   6464 C C   . VAL   D 1 141 ? -32.491 -6.020  11.728  1.00 25.81 ? 120 VAL   D C   1 
ATOM   6465 O O   . VAL   D 1 141 ? -31.866 -5.438  12.625  1.00 22.84 ? 120 VAL   D O   1 
ATOM   6466 C CB  . VAL   D 1 141 ? -31.881 -6.149  9.273   1.00 23.03 ? 120 VAL   D CB  1 
ATOM   6467 C CG1 . VAL   D 1 141 ? -31.540 -4.660  9.383   1.00 22.45 ? 120 VAL   D CG1 1 
ATOM   6468 C CG2 . VAL   D 1 141 ? -30.973 -6.815  8.220   1.00 20.42 ? 120 VAL   D CG2 1 
ATOM   6469 N N   . ALA   D 1 142 ? -33.821 -5.941  11.605  1.00 23.79 ? 121 ALA   D N   1 
ATOM   6470 C CA  . ALA   D 1 142 ? -34.638 -5.180  12.549  1.00 21.99 ? 121 ALA   D CA  1 
ATOM   6471 C C   . ALA   D 1 142 ? -34.357 -5.576  14.005  1.00 22.21 ? 121 ALA   D C   1 
ATOM   6472 O O   . ALA   D 1 142 ? -34.208 -4.726  14.863  1.00 21.31 ? 121 ALA   D O   1 
ATOM   6473 C CB  . ALA   D 1 142 ? -36.113 -5.353  12.180  1.00 23.29 ? 121 ALA   D CB  1 
ATOM   6474 N N   . GLU   D 1 143 ? -34.288 -6.876  14.308  1.00 22.02 ? 122 GLU   D N   1 
ATOM   6475 C CA  . GLU   D 1 143 ? -34.100 -7.324  15.676  1.00 23.62 ? 122 GLU   D CA  1 
ATOM   6476 C C   . GLU   D 1 143 ? -32.673 -7.087  16.179  1.00 24.02 ? 122 GLU   D C   1 
ATOM   6477 O O   . GLU   D 1 143 ? -32.488 -6.540  17.263  1.00 22.63 ? 122 GLU   D O   1 
ATOM   6478 C CB  . GLU   D 1 143 ? -34.424 -8.815  15.773  1.00 25.11 ? 122 GLU   D CB  1 
ATOM   6479 C CG  . GLU   D 1 143 ? -35.927 -9.082  15.725  1.00 27.49 ? 122 GLU   D CG  1 
ATOM   6480 C CD  . GLU   D 1 143 ? -36.331 -10.548 15.848  1.00 32.38 ? 122 GLU   D CD  1 
ATOM   6481 O OE1 . GLU   D 1 143 ? -35.474 -11.432 15.820  1.00 31.08 ? 122 GLU   D OE1 1 
ATOM   6482 O OE2 . GLU   D 1 143 ? -37.550 -10.812 15.925  1.00 35.36 ? 122 GLU   D OE2 1 
ATOM   6483 N N   . LEU   D 1 144 ? -31.666 -7.539  15.415  1.00 22.00 ? 123 LEU   D N   1 
ATOM   6484 C CA  . LEU   D 1 144 ? -30.284 -7.436  15.861  1.00 19.62 ? 123 LEU   D CA  1 
ATOM   6485 C C   . LEU   D 1 144 ? -29.786 -5.985  15.843  1.00 21.91 ? 123 LEU   D C   1 
ATOM   6486 O O   . LEU   D 1 144 ? -29.135 -5.556  16.804  1.00 22.28 ? 123 LEU   D O   1 
ATOM   6487 C CB  . LEU   D 1 144 ? -29.412 -8.400  15.050  1.00 21.42 ? 123 LEU   D CB  1 
ATOM   6488 C CG  . LEU   D 1 144 ? -29.732 -9.876  15.302  1.00 22.70 ? 123 LEU   D CG  1 
ATOM   6489 C CD1 . LEU   D 1 144 ? -29.210 -10.749 14.229  1.00 23.96 ? 123 LEU   D CD1 1 
ATOM   6490 C CD2 . LEU   D 1 144 ? -29.059 -10.294 16.628  1.00 27.73 ? 123 LEU   D CD2 1 
ATOM   6491 N N   . ILE   D 1 145 ? -30.106 -5.208  14.806  1.00 18.55 ? 124 ILE   D N   1 
ATOM   6492 C CA  . ILE   D 1 145 ? -29.647 -3.820  14.774  1.00 21.02 ? 124 ILE   D CA  1 
ATOM   6493 C C   . ILE   D 1 145 ? -30.537 -2.950  15.688  1.00 21.93 ? 124 ILE   D C   1 
ATOM   6494 O O   . ILE   D 1 145 ? -30.075 -2.037  16.380  1.00 20.48 ? 124 ILE   D O   1 
ATOM   6495 C CB  . ILE   D 1 145 ? -29.522 -3.265  13.332  1.00 20.07 ? 124 ILE   D CB  1 
ATOM   6496 C CG1 . ILE   D 1 145 ? -28.675 -4.191  12.387  1.00 24.76 ? 124 ILE   D CG1 1 
ATOM   6497 C CG2 . ILE   D 1 145 ? -29.000 -1.816  13.329  1.00 21.92 ? 124 ILE   D CG2 1 
ATOM   6498 C CD1 . ILE   D 1 145 ? -27.241 -4.462  12.820  1.00 24.62 ? 124 ILE   D CD1 1 
ATOM   6499 N N   . GLY   D 1 146 ? -31.835 -3.238  15.763  1.00 23.54 ? 125 GLY   D N   1 
ATOM   6500 C CA  . GLY   D 1 146 ? -32.697 -2.418  16.614  1.00 21.63 ? 125 GLY   D CA  1 
ATOM   6501 C C   . GLY   D 1 146 ? -32.369 -2.572  18.098  1.00 21.96 ? 125 GLY   D C   1 
ATOM   6502 O O   . GLY   D 1 146 ? -32.144 -1.565  18.778  1.00 21.16 ? 125 GLY   D O   1 
ATOM   6503 N N   . THR   D 1 147 ? -32.269 -3.828  18.590  1.00 20.76 ? 126 THR   D N   1 
ATOM   6504 C CA  . THR   D 1 147 ? -32.064 -4.037  20.021  1.00 23.06 ? 126 THR   D CA  1 
ATOM   6505 C C   . THR   D 1 147 ? -30.664 -3.584  20.425  1.00 23.74 ? 126 THR   D C   1 
ATOM   6506 O O   . THR   D 1 147 ? -30.482 -2.937  21.456  1.00 23.49 ? 126 THR   D O   1 
ATOM   6507 C CB  . THR   D 1 147 ? -32.291 -5.477  20.499  1.00 24.62 ? 126 THR   D CB  1 
ATOM   6508 O OG1 . THR   D 1 147 ? -31.280 -6.175  19.777  1.00 28.73 ? 126 THR   D OG1 1 
ATOM   6509 C CG2 . THR   D 1 147 ? -33.668 -6.045  20.194  1.00 25.10 ? 126 THR   D CG2 1 
ATOM   6510 N N   . ASN   D 1 148 ? -29.665 -3.856  19.573  1.00 21.76 ? 127 ASN   D N   1 
ATOM   6511 C CA  . ASN   D 1 148 ? -28.299 -3.692  20.030  1.00 20.46 ? 127 ASN   D CA  1 
ATOM   6512 C C   . ASN   D 1 148 ? -27.848 -2.260  19.786  1.00 21.95 ? 127 ASN   D C   1 
ATOM   6513 O O   . ASN   D 1 148 ? -26.878 -1.846  20.405  1.00 22.14 ? 127 ASN   D O   1 
ATOM   6514 C CB  . ASN   D 1 148 ? -27.359 -4.714  19.400  1.00 22.56 ? 127 ASN   D CB  1 
ATOM   6515 C CG  . ASN   D 1 148 ? -27.587 -6.084  19.985  1.00 23.55 ? 127 ASN   D CG  1 
ATOM   6516 O OD1 . ASN   D 1 148 ? -27.290 -6.269  21.168  1.00 29.40 ? 127 ASN   D OD1 1 
ATOM   6517 N ND2 . ASN   D 1 148 ? -28.063 -7.053  19.216  1.00 22.56 ? 127 ASN   D ND2 1 
ATOM   6518 N N   . ALA   D 1 149 ? -28.542 -1.516  18.915  1.00 18.62 ? 128 ALA   D N   1 
ATOM   6519 C CA  . ALA   D 1 149 ? -27.977 -0.238  18.514  1.00 20.37 ? 128 ALA   D CA  1 
ATOM   6520 C C   . ALA   D 1 149 ? -29.027 0.873   18.430  1.00 19.31 ? 128 ALA   D C   1 
ATOM   6521 O O   . ALA   D 1 149 ? -28.827 1.977   18.944  1.00 22.13 ? 128 ALA   D O   1 
ATOM   6522 C CB  . ALA   D 1 149 ? -27.176 -0.377  17.197  1.00 19.57 ? 128 ALA   D CB  1 
ATOM   6523 N N   . ILE   D 1 150 ? -30.058 0.667   17.623  1.00 20.60 ? 129 ILE   D N   1 
ATOM   6524 C CA  . ILE   D 1 150 ? -30.955 1.797   17.345  1.00 19.98 ? 129 ILE   D CA  1 
ATOM   6525 C C   . ILE   D 1 150 ? -31.801 2.125   18.580  1.00 20.17 ? 129 ILE   D C   1 
ATOM   6526 O O   . ILE   D 1 150 ? -32.010 3.297   18.915  1.00 18.75 ? 129 ILE   D O   1 
ATOM   6527 C CB  . ILE   D 1 150 ? -31.824 1.501   16.101  1.00 20.83 ? 129 ILE   D CB  1 
ATOM   6528 C CG1 . ILE   D 1 150 ? -30.939 1.327   14.831  1.00 22.73 ? 129 ILE   D CG1 1 
ATOM   6529 C CG2 . ILE   D 1 150 ? -32.919 2.568   15.904  1.00 20.15 ? 129 ILE   D CG2 1 
ATOM   6530 C CD1 . ILE   D 1 150 ? -31.668 0.539   13.740  1.00 24.80 ? 129 ILE   D CD1 1 
ATOM   6531 N N   . ALA   D 1 151 ? -32.282 1.084   19.259  1.00 17.57 ? 130 ALA   D N   1 
ATOM   6532 C CA  . ALA   D 1 151 ? -33.004 1.342   20.500  1.00 19.23 ? 130 ALA   D CA  1 
ATOM   6533 C C   . ALA   D 1 151 ? -32.122 2.076   21.526  1.00 20.97 ? 130 ALA   D C   1 
ATOM   6534 O O   . ALA   D 1 151 ? -32.513 3.137   22.066  1.00 22.28 ? 130 ALA   D O   1 
ATOM   6535 C CB  . ALA   D 1 151 ? -33.697 0.067   21.007  1.00 19.15 ? 130 ALA   D CB  1 
ATOM   6536 N N   . PRO   D 1 152 ? -30.856 1.646   21.798  1.00 20.43 ? 131 PRO   D N   1 
ATOM   6537 C CA  . PRO   D 1 152 ? -29.966 2.477   22.609  1.00 18.49 ? 131 PRO   D CA  1 
ATOM   6538 C C   . PRO   D 1 152 ? -29.852 3.941   22.190  1.00 20.68 ? 131 PRO   D C   1 
ATOM   6539 O O   . PRO   D 1 152 ? -29.905 4.830   23.048  1.00 21.83 ? 131 PRO   D O   1 
ATOM   6540 C CB  . PRO   D 1 152 ? -28.619 1.694   22.578  1.00 19.32 ? 131 PRO   D CB  1 
ATOM   6541 C CG  . PRO   D 1 152 ? -29.078 0.268   22.491  1.00 19.61 ? 131 PRO   D CG  1 
ATOM   6542 C CD  . PRO   D 1 152 ? -30.310 0.291   21.542  1.00 19.12 ? 131 PRO   D CD  1 
ATOM   6543 N N   . PHE   D 1 153 ? -29.790 4.202   20.872  1.00 18.48 ? 132 PHE   D N   1 
ATOM   6544 C CA  . PHE   D 1 153 ? -29.700 5.585   20.425  1.00 20.66 ? 132 PHE   D CA  1 
ATOM   6545 C C   . PHE   D 1 153 ? -30.994 6.330   20.793  1.00 20.49 ? 132 PHE   D C   1 
ATOM   6546 O O   . PHE   D 1 153 ? -30.964 7.477   21.243  1.00 22.87 ? 132 PHE   D O   1 
ATOM   6547 C CB  . PHE   D 1 153 ? -29.501 5.510   18.902  1.00 20.65 ? 132 PHE   D CB  1 
ATOM   6548 C CG  . PHE   D 1 153 ? -29.792 6.822   18.175  1.00 20.23 ? 132 PHE   D CG  1 
ATOM   6549 C CD1 . PHE   D 1 153 ? -28.878 7.876   18.221  1.00 20.87 ? 132 PHE   D CD1 1 
ATOM   6550 C CD2 . PHE   D 1 153 ? -30.980 7.007   17.474  1.00 20.94 ? 132 PHE   D CD2 1 
ATOM   6551 C CE1 . PHE   D 1 153 ? -29.152 9.095   17.597  1.00 22.77 ? 132 PHE   D CE1 1 
ATOM   6552 C CE2 . PHE   D 1 153 ? -31.262 8.228   16.847  1.00 22.70 ? 132 PHE   D CE2 1 
ATOM   6553 C CZ  . PHE   D 1 153 ? -30.338 9.270   16.907  1.00 22.08 ? 132 PHE   D CZ  1 
ATOM   6554 N N   . LEU   D 1 154 ? -32.148 5.705   20.520  1.00 22.55 ? 133 LEU   D N   1 
ATOM   6555 C CA  . LEU   D 1 154 ? -33.437 6.380   20.718  1.00 21.13 ? 133 LEU   D CA  1 
ATOM   6556 C C   . LEU   D 1 154 ? -33.710 6.560   22.209  1.00 22.38 ? 133 LEU   D C   1 
ATOM   6557 O O   . LEU   D 1 154 ? -34.200 7.604   22.631  1.00 23.76 ? 133 LEU   D O   1 
ATOM   6558 C CB  . LEU   D 1 154 ? -34.522 5.535   20.042  1.00 20.46 ? 133 LEU   D CB  1 
ATOM   6559 C CG  . LEU   D 1 154 ? -34.473 5.458   18.504  1.00 20.74 ? 133 LEU   D CG  1 
ATOM   6560 C CD1 . LEU   D 1 154 ? -35.452 4.423   17.948  1.00 20.21 ? 133 LEU   D CD1 1 
ATOM   6561 C CD2 . LEU   D 1 154 ? -34.739 6.813   17.822  1.00 20.85 ? 133 LEU   D CD2 1 
ATOM   6562 N N   . LEU   D 1 155 ? -33.326 5.575   23.025  1.00 23.82 ? 134 LEU   D N   1 
ATOM   6563 C CA  . LEU   D 1 155 ? -33.419 5.753   24.472  1.00 22.99 ? 134 LEU   D CA  1 
ATOM   6564 C C   . LEU   D 1 155 ? -32.527 6.884   24.986  1.00 24.15 ? 134 LEU   D C   1 
ATOM   6565 O O   . LEU   D 1 155 ? -32.939 7.669   25.859  1.00 21.34 ? 134 LEU   D O   1 
ATOM   6566 C CB  . LEU   D 1 155 ? -33.168 4.428   25.163  1.00 22.94 ? 134 LEU   D CB  1 
ATOM   6567 C CG  . LEU   D 1 155 ? -34.298 3.423   24.959  1.00 19.72 ? 134 LEU   D CG  1 
ATOM   6568 C CD1 . LEU   D 1 155 ? -33.711 2.019   25.159  1.00 17.99 ? 134 LEU   D CD1 1 
ATOM   6569 C CD2 . LEU   D 1 155 ? -35.481 3.683   25.949  1.00 17.97 ? 134 LEU   D CD2 1 
ATOM   6570 N N   . THR   D 1 156 ? -31.335 6.994   24.384  1.00 22.13 ? 135 THR   D N   1 
ATOM   6571 C CA  . THR   D 1 156 ? -30.370 8.027   24.712  1.00 21.32 ? 135 THR   D CA  1 
ATOM   6572 C C   . THR   D 1 156 ? -30.976 9.392   24.374  1.00 21.74 ? 135 THR   D C   1 
ATOM   6573 O O   . THR   D 1 156 ? -30.879 10.339  25.150  1.00 20.77 ? 135 THR   D O   1 
ATOM   6574 C CB  . THR   D 1 156 ? -29.048 7.766   23.971  1.00 22.60 ? 135 THR   D CB  1 
ATOM   6575 O OG1 . THR   D 1 156 ? -28.472 6.539   24.454  1.00 20.25 ? 135 THR   D OG1 1 
ATOM   6576 C CG2 . THR   D 1 156 ? -28.055 8.893   24.219  1.00 23.65 ? 135 THR   D CG2 1 
ATOM   6577 N N   . MET   D 1 157 ? -31.546 9.507   23.169  1.00 23.46 ? 136 MET   D N   1 
ATOM   6578 C CA  . MET   D 1 157 ? -32.178 10.744  22.718  1.00 25.06 ? 136 MET   D CA  1 
ATOM   6579 C C   . MET   D 1 157 ? -33.312 11.170  23.673  1.00 24.94 ? 136 MET   D C   1 
ATOM   6580 O O   . MET   D 1 157 ? -33.354 12.313  24.136  1.00 24.50 ? 136 MET   D O   1 
ATOM   6581 C CB  . MET   D 1 157 ? -32.692 10.529  21.286  1.00 27.44 ? 136 MET   D CB  1 
ATOM   6582 C CG  . MET   D 1 157 ? -33.433 11.687  20.662  1.00 35.58 ? 136 MET   D CG  1 
ATOM   6583 S SD  . MET   D 1 157 ? -33.464 11.338  18.885  1.00 44.77 ? 136 MET   D SD  1 
ATOM   6584 C CE  . MET   D 1 157 ? -33.208 13.007  18.269  1.00 50.53 ? 136 MET   D CE  1 
ATOM   6585 N N   . SER   D 1 158 ? -34.208 10.242  24.010  1.00 23.37 ? 137 SER   D N   1 
ATOM   6586 C CA  . SER   D 1 158 ? -35.328 10.546  24.898  1.00 23.79 ? 137 SER   D CA  1 
ATOM   6587 C C   . SER   D 1 158 ? -34.836 10.840  26.315  1.00 25.21 ? 137 SER   D C   1 
ATOM   6588 O O   . SER   D 1 158 ? -35.350 11.756  26.968  1.00 24.85 ? 137 SER   D O   1 
ATOM   6589 C CB  . SER   D 1 158 ? -36.325 9.396   24.931  1.00 26.36 ? 137 SER   D CB  1 
ATOM   6590 O OG  . SER   D 1 158 ? -36.977 9.298   23.674  1.00 27.02 ? 137 SER   D OG  1 
ATOM   6591 N N   . PHE   D 1 159 ? -33.879 10.039  26.808  1.00 23.38 ? 138 PHE   D N   1 
ATOM   6592 C CA  . PHE   D 1 159 ? -33.230 10.301  28.093  1.00 25.29 ? 138 PHE   D CA  1 
ATOM   6593 C C   . PHE   D 1 159 ? -32.743 11.749  28.174  1.00 24.44 ? 138 PHE   D C   1 
ATOM   6594 O O   . PHE   D 1 159 ? -33.037 12.449  29.146  1.00 25.73 ? 138 PHE   D O   1 
ATOM   6595 C CB  . PHE   D 1 159 ? -32.157 9.260   28.441  1.00 24.47 ? 138 PHE   D CB  1 
ATOM   6596 C CG  . PHE   D 1 159 ? -31.428 9.512   29.751  1.00 25.66 ? 138 PHE   D CG  1 
ATOM   6597 C CD1 . PHE   D 1 159 ? -30.344 10.394  29.806  1.00 24.63 ? 138 PHE   D CD1 1 
ATOM   6598 C CD2 . PHE   D 1 159 ? -31.831 8.860   30.914  1.00 25.64 ? 138 PHE   D CD2 1 
ATOM   6599 C CE1 . PHE   D 1 159 ? -29.685 10.615  31.016  1.00 24.97 ? 138 PHE   D CE1 1 
ATOM   6600 C CE2 . PHE   D 1 159 ? -31.151 9.065   32.111  1.00 25.55 ? 138 PHE   D CE2 1 
ATOM   6601 C CZ  . PHE   D 1 159 ? -30.092 9.955   32.152  1.00 23.96 ? 138 PHE   D CZ  1 
ATOM   6602 N N   . ALA   D 1 160 ? -32.011 12.208  27.160  1.00 24.24 ? 139 ALA   D N   1 
ATOM   6603 C CA  . ALA   D 1 160 ? -31.378 13.525  27.177  1.00 26.95 ? 139 ALA   D CA  1 
ATOM   6604 C C   . ALA   D 1 160 ? -32.403 14.652  27.012  1.00 30.66 ? 139 ALA   D C   1 
ATOM   6605 O O   . ALA   D 1 160 ? -32.246 15.741  27.586  1.00 31.39 ? 139 ALA   D O   1 
ATOM   6606 C CB  . ALA   D 1 160 ? -30.342 13.638  26.078  1.00 25.80 ? 139 ALA   D CB  1 
ATOM   6607 N N   . GLN   D 1 161 ? -33.416 14.412  26.170  1.00 30.79 ? 140 GLN   D N   1 
ATOM   6608 C CA  . GLN   D 1 161 ? -34.430 15.421  25.867  1.00 28.75 ? 140 GLN   D CA  1 
ATOM   6609 C C   . GLN   D 1 161 ? -35.256 15.721  27.126  1.00 31.85 ? 140 GLN   D C   1 
ATOM   6610 O O   . GLN   D 1 161 ? -35.631 16.866  27.373  1.00 33.38 ? 140 GLN   D O   1 
ATOM   6611 C CB  . GLN   D 1 161 ? -35.348 14.871  24.780  1.00 31.63 ? 140 GLN   D CB  1 
ATOM   6612 C CG  . GLN   D 1 161 ? -35.944 15.933  23.860  0.60 38.65 ? 140 GLN   D CG  1 
ATOM   6613 C CD  . GLN   D 1 161 ? -35.034 16.250  22.694  0.60 44.68 ? 140 GLN   D CD  1 
ATOM   6614 O OE1 . GLN   D 1 161 ? -34.646 17.403  22.471  0.60 48.74 ? 140 GLN   D OE1 1 
ATOM   6615 N NE2 . GLN   D 1 161 ? -34.679 15.219  21.936  0.60 48.24 ? 140 GLN   D NE2 1 
ATOM   6616 N N   . ARG   D 1 162 ? -35.551 14.689  27.925  1.00 33.68 ? 141 ARG   D N   1 
ATOM   6617 C CA  . ARG   D 1 162 ? -36.306 14.879  29.159  1.00 39.97 ? 141 ARG   D CA  1 
ATOM   6618 C C   . ARG   D 1 162 ? -35.470 15.530  30.264  1.00 45.10 ? 141 ARG   D C   1 
ATOM   6619 O O   . ARG   D 1 162 ? -36.023 15.853  31.308  1.00 55.38 ? 141 ARG   D O   1 
ATOM   6620 C CB  . ARG   D 1 162 ? -36.853 13.566  29.727  1.00 36.50 ? 141 ARG   D CB  1 
ATOM   6621 C CG  . ARG   D 1 162 ? -37.882 12.872  28.843  1.00 39.65 ? 141 ARG   D CG  1 
ATOM   6622 C CD  . ARG   D 1 162 ? -39.279 13.481  28.741  0.70 43.80 ? 141 ARG   D CD  1 
ATOM   6623 N NE  . ARG   D 1 162 ? -39.926 13.910  29.987  0.70 43.17 ? 141 ARG   D NE  1 
ATOM   6624 C CZ  . ARG   D 1 162 ? -40.958 13.343  30.615  0.70 42.04 ? 141 ARG   D CZ  1 
ATOM   6625 N NH1 . ARG   D 1 162 ? -41.329 12.111  30.343  0.70 41.42 ? 141 ARG   D NH1 1 
ATOM   6626 N NH2 . ARG   D 1 162 ? -41.600 14.007  31.560  0.70 42.41 ? 141 ARG   D NH2 1 
ATOM   6627 N N   . GLN   D 1 163 ? -34.159 15.741  30.061  1.00 45.33 ? 142 GLN   D N   1 
ATOM   6628 C CA  . GLN   D 1 163 ? -33.340 16.273  31.148  1.00 46.49 ? 142 GLN   D CA  1 
ATOM   6629 C C   . GLN   D 1 163 ? -33.396 17.811  31.133  1.00 58.52 ? 142 GLN   D C   1 
ATOM   6630 O O   . GLN   D 1 163 ? -34.480 18.328  31.484  1.00 65.32 ? 142 GLN   D O   1 
ATOM   6631 C CB  . GLN   D 1 163 ? -31.898 15.759  31.219  1.00 43.03 ? 142 GLN   D CB  1 
ATOM   6632 C CG  . GLN   D 1 163 ? -31.766 14.240  31.281  1.00 41.31 ? 142 GLN   D CG  1 
ATOM   6633 C CD  . GLN   D 1 163 ? -32.433 13.534  32.447  1.00 38.86 ? 142 GLN   D CD  1 
ATOM   6634 O OE1 . GLN   D 1 163 ? -32.596 14.079  33.545  1.00 34.10 ? 142 GLN   D OE1 1 
ATOM   6635 N NE2 . GLN   D 1 163 ? -32.712 12.248  32.255  1.00 38.63 ? 142 GLN   D NE2 1 
ATOM   6636 N N   . SER   D 1 173 ? -28.211 16.110  38.469  1.00 60.33 ? 152 SER   D N   1 
ATOM   6637 C CA  . SER   D 1 173 ? -27.029 15.903  39.347  1.00 59.08 ? 152 SER   D CA  1 
ATOM   6638 C C   . SER   D 1 173 ? -26.031 14.938  38.685  1.00 54.59 ? 152 SER   D C   1 
ATOM   6639 O O   . SER   D 1 173 ? -25.249 15.370  37.834  1.00 67.89 ? 152 SER   D O   1 
ATOM   6640 C CB  . SER   D 1 173 ? -27.456 15.491  40.741  1.00 55.64 ? 152 SER   D CB  1 
ATOM   6641 N N   . ASN   D 1 174 ? -26.080 13.639  39.034  1.00 42.10 ? 153 ASN   D N   1 
ATOM   6642 C CA  . ASN   D 1 174 ? -25.154 12.633  38.513  1.00 36.40 ? 153 ASN   D CA  1 
ATOM   6643 C C   . ASN   D 1 174 ? -25.860 11.749  37.480  1.00 33.62 ? 153 ASN   D C   1 
ATOM   6644 O O   . ASN   D 1 174 ? -26.242 10.596  37.764  1.00 29.95 ? 153 ASN   D O   1 
ATOM   6645 C CB  . ASN   D 1 174 ? -24.558 11.779  39.626  1.00 35.90 ? 153 ASN   D CB  1 
ATOM   6646 C CG  . ASN   D 1 174 ? -23.539 10.781  39.124  1.00 41.05 ? 153 ASN   D CG  1 
ATOM   6647 O OD1 . ASN   D 1 174 ? -22.871 11.008  38.105  1.00 36.71 ? 153 ASN   D OD1 1 
ATOM   6648 N ND2 . ASN   D 1 174 ? -23.401 9.673   39.840  1.00 45.75 ? 153 ASN   D ND2 1 
ATOM   6649 N N   . LEU   D 1 175 ? -26.066 12.330  36.286  1.00 27.79 ? 154 LEU   D N   1 
ATOM   6650 C CA  . LEU   D 1 175 ? -26.782 11.645  35.216  1.00 26.49 ? 154 LEU   D CA  1 
ATOM   6651 C C   . LEU   D 1 175 ? -25.780 10.795  34.436  1.00 25.30 ? 154 LEU   D C   1 
ATOM   6652 O O   . LEU   D 1 175 ? -24.717 11.299  34.077  1.00 22.50 ? 154 LEU   D O   1 
ATOM   6653 C CB  . LEU   D 1 175 ? -27.405 12.716  34.321  1.00 26.97 ? 154 LEU   D CB  1 
ATOM   6654 C CG  . LEU   D 1 175 ? -28.332 13.721  35.021  1.00 30.56 ? 154 LEU   D CG  1 
ATOM   6655 C CD1 . LEU   D 1 175 ? -28.888 14.763  34.049  1.00 31.54 ? 154 LEU   D CD1 1 
ATOM   6656 C CD2 . LEU   D 1 175 ? -29.447 13.040  35.804  1.00 25.46 ? 154 LEU   D CD2 1 
ATOM   6657 N N   . SER   D 1 176 ? -26.115 9.522   34.171  1.00 24.21 ? 155 SER   D N   1 
ATOM   6658 C CA  . SER   D 1 176 ? -25.261 8.794   33.244  1.00 24.39 ? 155 SER   D CA  1 
ATOM   6659 C C   . SER   D 1 176 ? -26.016 7.670   32.532  1.00 23.66 ? 155 SER   D C   1 
ATOM   6660 O O   . SER   D 1 176 ? -27.110 7.249   32.934  1.00 21.70 ? 155 SER   D O   1 
ATOM   6661 C CB  . SER   D 1 176 ? -23.967 8.305   33.926  1.00 26.16 ? 155 SER   D CB  1 
ATOM   6662 O OG  . SER   D 1 176 ? -24.205 7.136   34.701  1.00 25.99 ? 155 SER   D OG  1 
ATOM   6663 N N   . ILE   D 1 177 ? -25.391 7.197   31.443  1.00 23.88 ? 156 ILE   D N   1 
ATOM   6664 C CA  . ILE   D 1 177 ? -25.875 6.088   30.640  1.00 20.64 ? 156 ILE   D CA  1 
ATOM   6665 C C   . ILE   D 1 177 ? -24.779 5.036   30.602  1.00 20.36 ? 156 ILE   D C   1 
ATOM   6666 O O   . ILE   D 1 177 ? -23.591 5.380   30.464  1.00 20.70 ? 156 ILE   D O   1 
ATOM   6667 C CB  . ILE   D 1 177 ? -26.208 6.582   29.204  1.00 21.54 ? 156 ILE   D CB  1 
ATOM   6668 C CG1 . ILE   D 1 177 ? -27.252 7.719   29.193  1.00 22.61 ? 156 ILE   D CG1 1 
ATOM   6669 C CG2 . ILE   D 1 177 ? -26.658 5.421   28.314  1.00 19.37 ? 156 ILE   D CG2 1 
ATOM   6670 C CD1 . ILE   D 1 177 ? -27.510 8.302   27.801  1.00 21.48 ? 156 ILE   D CD1 1 
ATOM   6671 N N   . VAL   D 1 178 ? -25.177 3.759   30.706  1.00 19.76 ? 157 VAL   D N   1 
ATOM   6672 C CA  . VAL   D 1 178 ? -24.204 2.682   30.604  1.00 21.50 ? 157 VAL   D CA  1 
ATOM   6673 C C   . VAL   D 1 178 ? -24.714 1.703   29.546  1.00 20.97 ? 157 VAL   D C   1 
ATOM   6674 O O   . VAL   D 1 178 ? -25.849 1.216   29.663  1.00 21.02 ? 157 VAL   D O   1 
ATOM   6675 C CB  . VAL   D 1 178 ? -23.993 1.921   31.934  1.00 21.92 ? 157 VAL   D CB  1 
ATOM   6676 C CG1 . VAL   D 1 178 ? -23.075 0.715   31.712  1.00 21.58 ? 157 VAL   D CG1 1 
ATOM   6677 C CG2 . VAL   D 1 178 ? -23.493 2.812   33.070  1.00 22.55 ? 157 VAL   D CG2 1 
ATOM   6678 N N   . ASN   D 1 179 ? -23.886 1.452   28.512  1.00 20.41 ? 158 ASN   D N   1 
ATOM   6679 C CA  . ASN   D 1 179 ? -24.232 0.574   27.396  1.00 19.45 ? 158 ASN   D CA  1 
ATOM   6680 C C   . ASN   D 1 179 ? -23.567 -0.788  27.594  1.00 20.56 ? 158 ASN   D C   1 
ATOM   6681 O O   . ASN   D 1 179 ? -22.356 -0.865  27.807  1.00 20.38 ? 158 ASN   D O   1 
ATOM   6682 C CB  . ASN   D 1 179 ? -23.801 1.193   26.062  1.00 19.75 ? 158 ASN   D CB  1 
ATOM   6683 C CG  . ASN   D 1 179 ? -24.649 2.402   25.724  1.00 21.25 ? 158 ASN   D CG  1 
ATOM   6684 O OD1 . ASN   D 1 179 ? -25.821 2.421   26.117  1.00 22.05 ? 158 ASN   D OD1 1 
ATOM   6685 N ND2 . ASN   D 1 179 ? -24.116 3.438   25.084  1.00 21.32 ? 158 ASN   D ND2 1 
ATOM   6686 N N   . LEU   D 1 180 ? -24.335 -1.866  27.482  1.00 18.87 ? 159 LEU   D N   1 
ATOM   6687 C CA  . LEU   D 1 180 ? -23.720 -3.188  27.571  1.00 20.01 ? 159 LEU   D CA  1 
ATOM   6688 C C   . LEU   D 1 180 ? -23.187 -3.568  26.187  1.00 20.28 ? 159 LEU   D C   1 
ATOM   6689 O O   . LEU   D 1 180 ? -23.963 -3.751  25.260  1.00 20.40 ? 159 LEU   D O   1 
ATOM   6690 C CB  . LEU   D 1 180 ? -24.702 -4.238  28.105  1.00 18.57 ? 159 LEU   D CB  1 
ATOM   6691 C CG  . LEU   D 1 180 ? -24.855 -4.365  29.627  1.00 21.69 ? 159 LEU   D CG  1 
ATOM   6692 C CD1 . LEU   D 1 180 ? -23.589 -5.021  30.192  1.00 20.03 ? 159 LEU   D CD1 1 
ATOM   6693 C CD2 . LEU   D 1 180 ? -25.107 -2.996  30.278  1.00 23.33 ? 159 LEU   D CD2 1 
ATOM   6694 N N   . CYS   D 1 181 ? -21.844 -3.604  26.077  1.00 22.36 ? 160 CYS   D N   1 
ATOM   6695 C CA  . CYS   D 1 181 ? -21.113 -3.804  24.832  1.00 22.61 ? 160 CYS   D CA  1 
ATOM   6696 C C   . CYS   D 1 181 ? -20.667 -5.259  24.808  1.00 22.95 ? 160 CYS   D C   1 
ATOM   6697 O O   . CYS   D 1 181 ? -21.360 -6.107  25.360  1.00 26.77 ? 160 CYS   D O   1 
ATOM   6698 C CB  . CYS   D 1 181 ? -19.937 -2.847  24.713  1.00 21.10 ? 160 CYS   D CB  1 
ATOM   6699 S SG  . CYS   D 1 181 ? -20.468 -1.104  24.714  1.00 27.23 ? 160 CYS   D SG  1 
ATOM   6700 N N   . ASP   D 1 182 ? -19.540 -5.548  24.161  1.00 20.91 ? 161 ASP   D N   1 
ATOM   6701 C CA  . ASP   D 1 182 ? -19.110 -6.932  24.069  1.00 20.89 ? 161 ASP   D CA  1 
ATOM   6702 C C   . ASP   D 1 182 ? -17.592 -6.936  23.875  1.00 22.87 ? 161 ASP   D C   1 
ATOM   6703 O O   . ASP   D 1 182 ? -17.111 -6.366  22.887  1.00 22.55 ? 161 ASP   D O   1 
ATOM   6704 C CB  . ASP   D 1 182 ? -19.801 -7.583  22.887  1.00 22.17 ? 161 ASP   D CB  1 
ATOM   6705 C CG  . ASP   D 1 182 ? -19.551 -9.072  22.731  1.00 29.60 ? 161 ASP   D CG  1 
ATOM   6706 O OD1 . ASP   D 1 182 ? -18.384 -9.488  22.878  1.00 27.26 ? 161 ASP   D OD1 1 
ATOM   6707 O OD2 . ASP   D 1 182 ? -20.525 -9.794  22.423  1.00 33.29 ? 161 ASP   D OD2 1 
ATOM   6708 N N   . ALA   D 1 183 ? -16.865 -7.592  24.798  1.00 21.22 ? 162 ALA   D N   1 
ATOM   6709 C CA  . ALA   D 1 183 ? -15.406 -7.596  24.765  1.00 20.74 ? 162 ALA   D CA  1 
ATOM   6710 C C   . ALA   D 1 183 ? -14.834 -8.238  23.499  1.00 21.57 ? 162 ALA   D C   1 
ATOM   6711 O O   . ALA   D 1 183 ? -13.663 -8.010  23.179  1.00 21.83 ? 162 ALA   D O   1 
ATOM   6712 C CB  . ALA   D 1 183 ? -14.834 -8.309  25.992  1.00 21.60 ? 162 ALA   D CB  1 
ATOM   6713 N N   . MET   D 1 184 ? -15.618 -9.059  22.798  1.00 21.26 ? 163 MET   D N   1 
ATOM   6714 C CA  . MET   D 1 184 ? -15.064 -9.920  21.756  1.00 23.99 ? 163 MET   D CA  1 
ATOM   6715 C C   . MET   D 1 184 ? -15.420 -9.406  20.364  1.00 25.00 ? 163 MET   D C   1 
ATOM   6716 O O   . MET   D 1 184 ? -15.292 -10.119 19.371  1.00 27.41 ? 163 MET   D O   1 
ATOM   6717 C CB  . MET   D 1 184 ? -15.539 -11.376 21.941  1.00 25.59 ? 163 MET   D CB  1 
ATOM   6718 C CG  . MET   D 1 184 ? -15.024 -12.013 23.238  1.00 28.65 ? 163 MET   D CG  1 
ATOM   6719 S SD  . MET   D 1 184 ? -13.217 -12.163 23.259  1.00 32.34 ? 163 MET   D SD  1 
ATOM   6720 C CE  . MET   D 1 184 ? -12.962 -13.534 22.121  1.00 36.87 ? 163 MET   D CE  1 
ATOM   6721 N N   . VAL   D 1 185 ? -15.787 -8.137  20.273  1.00 26.82 ? 164 VAL   D N   1 
ATOM   6722 C CA  . VAL   D 1 185 ? -16.383 -7.647  19.033  1.00 32.23 ? 164 VAL   D CA  1 
ATOM   6723 C C   . VAL   D 1 185 ? -15.326 -7.506  17.932  1.00 31.15 ? 164 VAL   D C   1 
ATOM   6724 O O   . VAL   D 1 185 ? -15.663 -7.342  16.759  1.00 28.66 ? 164 VAL   D O   1 
ATOM   6725 C CB  . VAL   D 1 185 ? -17.011 -6.315  19.505  1.00 34.02 ? 164 VAL   D CB  1 
ATOM   6726 C CG1 . VAL   D 1 185 ? -16.053 -5.151  19.496  1.00 30.87 ? 164 VAL   D CG1 1 
ATOM   6727 C CG2 . VAL   D 1 185 ? -18.322 -5.998  18.813  1.00 42.69 ? 164 VAL   D CG2 1 
ATOM   6728 N N   . ASP   D 1 186 ? -14.040 -7.626  18.284  1.00 25.80 ? 165 ASP   D N   1 
ATOM   6729 C CA  . ASP   D 1 186 ? -12.992 -7.563  17.270  1.00 25.08 ? 165 ASP   D CA  1 
ATOM   6730 C C   . ASP   D 1 186 ? -12.455 -8.948  16.967  1.00 25.60 ? 165 ASP   D C   1 
ATOM   6731 O O   . ASP   D 1 186 ? -11.539 -9.098  16.159  1.00 25.32 ? 165 ASP   D O   1 
ATOM   6732 C CB  . ASP   D 1 186 ? -11.862 -6.623  17.645  1.00 26.17 ? 165 ASP   D CB  1 
ATOM   6733 C CG  . ASP   D 1 186 ? -12.268 -5.157  17.662  1.00 29.10 ? 165 ASP   D CG  1 
ATOM   6734 O OD1 . ASP   D 1 186 ? -13.031 -4.751  16.767  1.00 27.57 ? 165 ASP   D OD1 1 
ATOM   6735 O OD2 . ASP   D 1 186 ? -11.829 -4.426  18.575  1.00 31.55 ? 165 ASP   D OD2 1 
ATOM   6736 N N   . GLN   D 1 187 ? -12.976 -9.951  17.677  1.00 23.18 ? 166 GLN   D N   1 
ATOM   6737 C CA  . GLN   D 1 187 ? -12.660 -11.331 17.361  1.00 23.54 ? 166 GLN   D CA  1 
ATOM   6738 C C   . GLN   D 1 187 ? -13.982 -12.090 17.345  1.00 26.53 ? 166 GLN   D C   1 
ATOM   6739 O O   . GLN   D 1 187 ? -14.225 -12.928 18.218  1.00 25.85 ? 166 GLN   D O   1 
ATOM   6740 C CB  . GLN   D 1 187 ? -11.738 -11.936 18.433  1.00 27.74 ? 166 GLN   D CB  1 
ATOM   6741 C CG  . GLN   D 1 187 ? -10.349 -11.294 18.519  1.00 33.82 ? 166 GLN   D CG  1 
ATOM   6742 C CD  . GLN   D 1 187 ? -10.027 -10.892 19.944  1.00 39.93 ? 166 GLN   D CD  1 
ATOM   6743 O OE1 . GLN   D 1 187 ? -10.358 -9.783  20.375  1.00 41.12 ? 166 GLN   D OE1 1 
ATOM   6744 N NE2 . GLN   D 1 187 ? -9.386  -11.787 20.686  1.00 34.65 ? 166 GLN   D NE2 1 
ATOM   6745 N N   . PRO   D 1 188 ? -14.904 -11.792 16.398  1.00 26.66 ? 167 PRO   D N   1 
ATOM   6746 C CA  . PRO   D 1 188 ? -16.293 -12.210 16.583  1.00 28.67 ? 167 PRO   D CA  1 
ATOM   6747 C C   . PRO   D 1 188 ? -16.535 -13.687 16.277  1.00 29.37 ? 167 PRO   D C   1 
ATOM   6748 O O   . PRO   D 1 188 ? -15.761 -14.334 15.552  1.00 28.63 ? 167 PRO   D O   1 
ATOM   6749 C CB  . PRO   D 1 188 ? -17.013 -11.285 15.594  1.00 25.59 ? 167 PRO   D CB  1 
ATOM   6750 C CG  . PRO   D 1 188 ? -16.038 -11.226 14.450  1.00 24.56 ? 167 PRO   D CG  1 
ATOM   6751 C CD  . PRO   D 1 188 ? -14.675 -11.034 15.155  1.00 24.38 ? 167 PRO   D CD  1 
HETATM 6752 N N   . CSX   D 1 189 ? -17.635 -14.193 16.852  1.00 27.27 ? 168 CSX   D N   1 
HETATM 6753 C CA  . CSX   D 1 189 ? -18.210 -15.483 16.503  1.00 32.51 ? 168 CSX   D CA  1 
HETATM 6754 C CB  . CSX   D 1 189 ? -19.495 -15.723 17.293  1.00 35.31 ? 168 CSX   D CB  1 
HETATM 6755 S SG  . CSX   D 1 189 ? -18.958 -16.108 18.984  1.00 48.85 ? 168 CSX   D SG  1 
HETATM 6756 C C   . CSX   D 1 189 ? -18.490 -15.538 15.001  1.00 31.37 ? 168 CSX   D C   1 
HETATM 6757 O O   . CSX   D 1 189 ? -18.987 -14.583 14.413  1.00 27.41 ? 168 CSX   D O   1 
HETATM 6758 O OD  . CSX   D 1 189 ? -18.429 -17.492 18.922  1.00 39.06 ? 168 CSX   D OD  1 
ATOM   6759 N N   . MET   D 1 190 ? -18.136 -16.668 14.391  1.00 31.19 ? 169 MET   D N   1 
ATOM   6760 C CA  . MET   D 1 190 ? -18.415 -16.970 12.989  1.00 32.73 ? 169 MET   D CA  1 
ATOM   6761 C C   . MET   D 1 190 ? -19.929 -16.886 12.748  1.00 27.34 ? 169 MET   D C   1 
ATOM   6762 O O   . MET   D 1 190 ? -20.694 -17.430 13.533  1.00 29.58 ? 169 MET   D O   1 
ATOM   6763 C CB  . MET   D 1 190 ? -17.992 -18.438 12.769  1.00 35.46 ? 169 MET   D CB  1 
ATOM   6764 C CG  . MET   D 1 190 ? -18.383 -18.997 11.424  1.00 44.64 ? 169 MET   D CG  1 
ATOM   6765 S SD  . MET   D 1 190 ? -17.369 -18.089 10.245  1.00 51.12 ? 169 MET   D SD  1 
ATOM   6766 C CE  . MET   D 1 190 ? -15.731 -18.818 10.420  1.00 41.89 ? 169 MET   D CE  1 
ATOM   6767 N N   . ALA   D 1 191 ? -20.362 -16.172 11.701  1.00 28.48 ? 170 ALA   D N   1 
ATOM   6768 C CA  . ALA   D 1 191 ? -21.754 -16.089 11.257  1.00 28.27 ? 170 ALA   D CA  1 
ATOM   6769 C C   . ALA   D 1 191 ? -22.611 -15.170 12.126  1.00 26.06 ? 170 ALA   D C   1 
ATOM   6770 O O   . ALA   D 1 191 ? -23.838 -15.231 12.062  1.00 24.22 ? 170 ALA   D O   1 
ATOM   6771 C CB  . ALA   D 1 191 ? -22.385 -17.475 11.124  1.00 26.56 ? 170 ALA   D CB  1 
ATOM   6772 N N   . PHE   D 1 192 ? -21.977 -14.310 12.935  1.00 24.65 ? 171 PHE   D N   1 
ATOM   6773 C CA  . PHE   D 1 192 ? -22.736 -13.395 13.772  1.00 22.26 ? 171 PHE   D CA  1 
ATOM   6774 C C   . PHE   D 1 192 ? -22.577 -11.971 13.266  1.00 22.73 ? 171 PHE   D C   1 
ATOM   6775 O O   . PHE   D 1 192 ? -22.465 -11.059 14.082  1.00 22.08 ? 171 PHE   D O   1 
ATOM   6776 C CB  . PHE   D 1 192 ? -22.290 -13.527 15.240  1.00 24.03 ? 171 PHE   D CB  1 
ATOM   6777 C CG  . PHE   D 1 192 ? -22.993 -14.697 15.927  1.00 26.96 ? 171 PHE   D CG  1 
ATOM   6778 C CD1 . PHE   D 1 192 ? -22.603 -16.018 15.684  1.00 25.94 ? 171 PHE   D CD1 1 
ATOM   6779 C CD2 . PHE   D 1 192 ? -24.089 -14.472 16.759  1.00 26.84 ? 171 PHE   D CD2 1 
ATOM   6780 C CE1 . PHE   D 1 192 ? -23.270 -17.074 16.304  1.00 26.34 ? 171 PHE   D CE1 1 
ATOM   6781 C CE2 . PHE   D 1 192 ? -24.754 -15.533 17.362  1.00 29.62 ? 171 PHE   D CE2 1 
ATOM   6782 C CZ  . PHE   D 1 192 ? -24.329 -16.836 17.153  1.00 27.88 ? 171 PHE   D CZ  1 
ATOM   6783 N N   . SER   D 1 193 ? -22.640 -11.758 11.943  1.00 20.36 ? 172 SER   D N   1 
ATOM   6784 C CA  . SER   D 1 193 ? -22.269 -10.431 11.447  1.00 21.03 ? 172 SER   D CA  1 
ATOM   6785 C C   . SER   D 1 193 ? -23.251 -9.358  11.909  1.00 20.39 ? 172 SER   D C   1 
ATOM   6786 O O   . SER   D 1 193 ? -22.834 -8.254  12.258  1.00 19.79 ? 172 SER   D O   1 
ATOM   6787 C CB  . SER   D 1 193 ? -22.080 -10.382 9.941   1.00 24.88 ? 172 SER   D CB  1 
ATOM   6788 O OG  . SER   D 1 193 ? -23.221 -10.956 9.323   1.00 33.21 ? 172 SER   D OG  1 
ATOM   6789 N N   . LEU   D 1 194 ? -24.562 -9.647  11.923  1.00 20.09 ? 173 LEU   D N   1 
ATOM   6790 C CA  . LEU   D 1 194 ? -25.495 -8.580  12.297  1.00 20.47 ? 173 LEU   D CA  1 
ATOM   6791 C C   . LEU   D 1 194 ? -25.359 -8.207  13.782  1.00 20.00 ? 173 LEU   D C   1 
ATOM   6792 O O   . LEU   D 1 194 ? -25.382 -7.027  14.180  1.00 21.39 ? 173 LEU   D O   1 
ATOM   6793 C CB  . LEU   D 1 194 ? -26.934 -8.934  11.893  1.00 19.72 ? 173 LEU   D CB  1 
ATOM   6794 C CG  . LEU   D 1 194 ? -27.284 -8.683  10.415  1.00 21.44 ? 173 LEU   D CG  1 
ATOM   6795 C CD1 . LEU   D 1 194 ? -28.686 -9.264  10.167  1.00 21.15 ? 173 LEU   D CD1 1 
ATOM   6796 C CD2 . LEU   D 1 194 ? -27.281 -7.218  9.987   1.00 20.74 ? 173 LEU   D CD2 1 
ATOM   6797 N N   . TYR   D 1 195 ? -25.261 -9.219  14.637  1.00 21.15 ? 174 TYR   D N   1 
ATOM   6798 C CA  . TYR   D 1 195 ? -25.017 -8.981  16.051  1.00 22.14 ? 174 TYR   D CA  1 
ATOM   6799 C C   . TYR   D 1 195 ? -23.759 -8.121  16.223  1.00 20.79 ? 174 TYR   D C   1 
ATOM   6800 O O   . TYR   D 1 195 ? -23.803 -7.116  16.934  1.00 20.62 ? 174 TYR   D O   1 
ATOM   6801 C CB  . TYR   D 1 195 ? -24.909 -10.296 16.831  1.00 20.03 ? 174 TYR   D CB  1 
ATOM   6802 C CG  . TYR   D 1 195 ? -24.442 -10.091 18.259  1.00 24.44 ? 174 TYR   D CG  1 
ATOM   6803 C CD1 . TYR   D 1 195 ? -25.330 -9.680  19.261  1.00 22.67 ? 174 TYR   D CD1 1 
ATOM   6804 C CD2 . TYR   D 1 195 ? -23.090 -10.274 18.592  1.00 23.53 ? 174 TYR   D CD2 1 
ATOM   6805 C CE1 . TYR   D 1 195 ? -24.878 -9.465  20.563  1.00 22.04 ? 174 TYR   D CE1 1 
ATOM   6806 C CE2 . TYR   D 1 195 ? -22.642 -10.098 19.902  1.00 23.19 ? 174 TYR   D CE2 1 
ATOM   6807 C CZ  . TYR   D 1 195 ? -23.539 -9.683  20.873  1.00 23.93 ? 174 TYR   D CZ  1 
ATOM   6808 O OH  . TYR   D 1 195 ? -23.113 -9.514  22.152  1.00 27.12 ? 174 TYR   D OH  1 
ATOM   6809 N N   . ASN   D 1 196 ? -22.666 -8.486  15.528  1.00 20.24 ? 175 ASN   D N   1 
ATOM   6810 C CA  A ASN   D 1 196 ? -21.391 -7.782  15.654  0.60 19.94 ? 175 ASN   D CA  1 
ATOM   6811 C CA  B ASN   D 1 196 ? -21.408 -7.771  15.691  0.40 19.59 ? 175 ASN   D CA  1 
ATOM   6812 C C   . ASN   D 1 196 ? -21.544 -6.342  15.179  1.00 18.78 ? 175 ASN   D C   1 
ATOM   6813 O O   . ASN   D 1 196 ? -20.991 -5.421  15.776  1.00 19.42 ? 175 ASN   D O   1 
ATOM   6814 C CB  A ASN   D 1 196 ? -20.285 -8.467  14.847  0.60 21.23 ? 175 ASN   D CB  1 
ATOM   6815 C CB  B ASN   D 1 196 ? -20.242 -8.544  15.085  0.40 20.44 ? 175 ASN   D CB  1 
ATOM   6816 C CG  A ASN   D 1 196 ? -18.890 -8.098  15.306  0.60 25.75 ? 175 ASN   D CG  1 
ATOM   6817 C CG  B ASN   D 1 196 ? -19.837 -9.687  15.985  0.40 21.49 ? 175 ASN   D CG  1 
ATOM   6818 O OD1 A ASN   D 1 196 ? -18.575 -8.229  16.497  0.60 25.98 ? 175 ASN   D OD1 1 
ATOM   6819 O OD1 B ASN   D 1 196 ? -19.194 -9.470  17.017  0.40 26.34 ? 175 ASN   D OD1 1 
ATOM   6820 N ND2 A ASN   D 1 196 ? -18.027 -7.664  14.388  0.60 25.47 ? 175 ASN   D ND2 1 
ATOM   6821 N ND2 B ASN   D 1 196 ? -20.211 -10.902 15.631  0.40 22.96 ? 175 ASN   D ND2 1 
ATOM   6822 N N   . MET   D 1 197 ? -22.259 -6.167  14.060  1.00 19.76 ? 176 MET   D N   1 
ATOM   6823 C CA  . MET   D 1 197 ? -22.545 -4.823  13.562  1.00 19.19 ? 176 MET   D CA  1 
ATOM   6824 C C   . MET   D 1 197 ? -23.269 -3.990  14.622  1.00 20.23 ? 176 MET   D C   1 
ATOM   6825 O O   . MET   D 1 197 ? -22.957 -2.817  14.795  1.00 19.10 ? 176 MET   D O   1 
ATOM   6826 C CB  . MET   D 1 197 ? -23.406 -4.885  12.293  1.00 18.56 ? 176 MET   D CB  1 
ATOM   6827 C CG  . MET   D 1 197 ? -22.566 -5.385  11.108  1.00 19.09 ? 176 MET   D CG  1 
ATOM   6828 S SD  . MET   D 1 197 ? -23.579 -5.730  9.647   1.00 22.53 ? 176 MET   D SD  1 
ATOM   6829 C CE  . MET   D 1 197 ? -24.131 -4.057  9.295   1.00 22.41 ? 176 MET   D CE  1 
ATOM   6830 N N   . GLY   D 1 198 ? -24.279 -4.571  15.285  1.00 19.94 ? 177 GLY   D N   1 
ATOM   6831 C CA  . GLY   D 1 198 ? -25.004 -3.813  16.298  1.00 20.15 ? 177 GLY   D CA  1 
ATOM   6832 C C   . GLY   D 1 198 ? -24.107 -3.417  17.477  1.00 18.37 ? 177 GLY   D C   1 
ATOM   6833 O O   . GLY   D 1 198 ? -24.117 -2.262  17.906  1.00 19.00 ? 177 GLY   D O   1 
ATOM   6834 N N   . LYS   D 1 199 ? -23.296 -4.356  17.977  1.00 18.29 ? 178 LYS   D N   1 
ATOM   6835 C CA  . LYS   D 1 199 ? -22.416 -4.054  19.104  1.00 18.73 ? 178 LYS   D CA  1 
ATOM   6836 C C   . LYS   D 1 199 ? -21.341 -3.045  18.692  1.00 20.43 ? 178 LYS   D C   1 
ATOM   6837 O O   . LYS   D 1 199 ? -20.964 -2.196  19.484  1.00 20.16 ? 178 LYS   D O   1 
ATOM   6838 C CB  . LYS   D 1 199 ? -21.801 -5.329  19.681  1.00 21.71 ? 178 LYS   D CB  1 
ATOM   6839 C CG  . LYS   D 1 199 ? -22.842 -6.207  20.441  1.00 23.95 ? 178 LYS   D CG  1 
ATOM   6840 C CD  . LYS   D 1 199 ? -23.603 -5.451  21.529  1.00 24.69 ? 178 LYS   D CD  1 
ATOM   6841 C CE  . LYS   D 1 199 ? -24.356 -6.398  22.437  1.00 25.35 ? 178 LYS   D CE  1 
ATOM   6842 N NZ  . LYS   D 1 199 ? -25.133 -5.702  23.456  1.00 24.50 ? 178 LYS   D NZ  1 
ATOM   6843 N N   . HIS   D 1 200 ? -20.858 -3.095  17.439  1.00 19.11 ? 179 HIS   D N   1 
ATOM   6844 C CA  . HIS   D 1 200 ? -19.875 -2.083  17.067  1.00 20.72 ? 179 HIS   D CA  1 
ATOM   6845 C C   . HIS   D 1 200 ? -20.584 -0.745  16.994  1.00 19.13 ? 179 HIS   D C   1 
ATOM   6846 O O   . HIS   D 1 200 ? -20.023 0.282   17.381  1.00 17.83 ? 179 HIS   D O   1 
ATOM   6847 C CB  . HIS   D 1 200 ? -19.294 -2.361  15.670  1.00 20.61 ? 179 HIS   D CB  1 
ATOM   6848 C CG  . HIS   D 1 200 ? -18.041 -3.138  15.731  1.00 24.66 ? 179 HIS   D CG  1 
ATOM   6849 N ND1 . HIS   D 1 200 ? -16.849 -2.444  15.740  1.00 25.55 ? 179 HIS   D ND1 1 
ATOM   6850 C CD2 . HIS   D 1 200 ? -17.736 -4.455  15.796  1.00 23.03 ? 179 HIS   D CD2 1 
ATOM   6851 C CE1 . HIS   D 1 200 ? -15.852 -3.325  15.788  1.00 25.52 ? 179 HIS   D CE1 1 
ATOM   6852 N NE2 . HIS   D 1 200 ? -16.376 -4.546  15.810  1.00 23.11 ? 179 HIS   D NE2 1 
ATOM   6853 N N   . ALA   D 1 201 ? -21.808 -0.754  16.460  1.00 18.75 ? 180 ALA   D N   1 
ATOM   6854 C CA  . ALA   D 1 201 ? -22.557 0.517   16.424  1.00 18.64 ? 180 ALA   D CA  1 
ATOM   6855 C C   . ALA   D 1 201 ? -22.717 1.099   17.831  1.00 19.40 ? 180 ALA   D C   1 
ATOM   6856 O O   . ALA   D 1 201 ? -22.708 2.321   18.041  1.00 20.30 ? 180 ALA   D O   1 
ATOM   6857 C CB  . ALA   D 1 201 ? -23.922 0.322   15.747  1.00 18.44 ? 180 ALA   D CB  1 
ATOM   6858 N N   . LEU   D 1 202 ? -22.896 0.217   18.812  1.00 19.61 ? 181 LEU   D N   1 
ATOM   6859 C CA  . LEU   D 1 202 ? -23.114 0.653   20.195  1.00 21.26 ? 181 LEU   D CA  1 
ATOM   6860 C C   . LEU   D 1 202 ? -21.846 1.323   20.752  1.00 21.95 ? 181 LEU   D C   1 
ATOM   6861 O O   . LEU   D 1 202 ? -21.922 2.326   21.464  1.00 20.87 ? 181 LEU   D O   1 
ATOM   6862 C CB  . LEU   D 1 202 ? -23.541 -0.561  21.009  1.00 20.94 ? 181 LEU   D CB  1 
ATOM   6863 C CG  . LEU   D 1 202 ? -24.030 -0.261  22.437  1.00 22.49 ? 181 LEU   D CG  1 
ATOM   6864 C CD1 . LEU   D 1 202 ? -25.207 0.734   22.429  1.00 19.97 ? 181 LEU   D CD1 1 
ATOM   6865 C CD2 . LEU   D 1 202 ? -24.447 -1.571  23.078  1.00 22.38 ? 181 LEU   D CD2 1 
ATOM   6866 N N   . VAL   D 1 203 ? -20.672 0.838   20.330  1.00 21.60 ? 182 VAL   D N   1 
ATOM   6867 C CA  . VAL   D 1 203 ? -19.430 1.514   20.685  1.00 21.27 ? 182 VAL   D CA  1 
ATOM   6868 C C   . VAL   D 1 203 ? -19.466 2.930   20.118  1.00 20.34 ? 182 VAL   D C   1 
ATOM   6869 O O   . VAL   D 1 203 ? -19.128 3.880   20.813  1.00 20.64 ? 182 VAL   D O   1 
ATOM   6870 C CB  . VAL   D 1 203 ? -18.190 0.735   20.204  1.00 24.43 ? 182 VAL   D CB  1 
ATOM   6871 C CG1 . VAL   D 1 203 ? -16.920 1.546   20.453  1.00 23.81 ? 182 VAL   D CG1 1 
ATOM   6872 C CG2 . VAL   D 1 203 ? -18.116 -0.648  20.867  1.00 22.25 ? 182 VAL   D CG2 1 
ATOM   6873 N N   . GLY   D 1 204 ? -19.873 3.066   18.847  1.00 19.26 ? 183 GLY   D N   1 
ATOM   6874 C CA  . GLY   D 1 204 ? -19.885 4.393   18.237  1.00 19.58 ? 183 GLY   D CA  1 
ATOM   6875 C C   . GLY   D 1 204 ? -20.865 5.346   18.924  1.00 18.22 ? 183 GLY   D C   1 
ATOM   6876 O O   . GLY   D 1 204 ? -20.561 6.516   19.124  1.00 18.90 ? 183 GLY   D O   1 
ATOM   6877 N N   . LEU   D 1 205 ? -22.044 4.843   19.281  1.00 19.75 ? 184 LEU   D N   1 
ATOM   6878 C CA  . LEU   D 1 205 ? -23.002 5.609   20.073  1.00 19.62 ? 184 LEU   D CA  1 
ATOM   6879 C C   . LEU   D 1 205 ? -22.402 6.054   21.423  1.00 19.30 ? 184 LEU   D C   1 
ATOM   6880 O O   . LEU   D 1 205 ? -22.587 7.225   21.836  1.00 21.31 ? 184 LEU   D O   1 
ATOM   6881 C CB  . LEU   D 1 205 ? -24.256 4.758   20.296  1.00 19.13 ? 184 LEU   D CB  1 
ATOM   6882 C CG  . LEU   D 1 205 ? -25.291 5.392   21.250  1.00 20.68 ? 184 LEU   D CG  1 
ATOM   6883 C CD1 . LEU   D 1 205 ? -25.709 6.783   20.738  1.00 19.77 ? 184 LEU   D CD1 1 
ATOM   6884 C CD2 . LEU   D 1 205 ? -26.516 4.515   21.455  1.00 18.41 ? 184 LEU   D CD2 1 
ATOM   6885 N N   . THR   D 1 206 ? -21.733 5.127   22.129  1.00 19.04 ? 185 THR   D N   1 
ATOM   6886 C CA  . THR   D 1 206 ? -21.143 5.416   23.435  1.00 17.62 ? 185 THR   D CA  1 
ATOM   6887 C C   . THR   D 1 206 ? -20.211 6.617   23.288  1.00 19.84 ? 185 THR   D C   1 
ATOM   6888 O O   . THR   D 1 206 ? -20.321 7.601   24.028  1.00 21.19 ? 185 THR   D O   1 
ATOM   6889 C CB  . THR   D 1 206 ? -20.452 4.187   24.024  1.00 21.45 ? 185 THR   D CB  1 
ATOM   6890 O OG1 . THR   D 1 206 ? -21.358 3.085   24.123  1.00 18.55 ? 185 THR   D OG1 1 
ATOM   6891 C CG2 . THR   D 1 206 ? -19.910 4.451   25.425  1.00 21.21 ? 185 THR   D CG2 1 
ATOM   6892 N N   . GLN   D 1 207 ? -19.368 6.596   22.236  1.00 19.75 ? 186 GLN   D N   1 
ATOM   6893 C CA  . GLN   D 1 207 ? -18.424 7.684   22.042  1.00 19.76 ? 186 GLN   D CA  1 
ATOM   6894 C C   . GLN   D 1 207 ? -19.155 8.958   21.620  1.00 20.25 ? 186 GLN   D C   1 
ATOM   6895 O O   . GLN   D 1 207 ? -18.883 10.029  22.168  1.00 21.65 ? 186 GLN   D O   1 
ATOM   6896 C CB  . GLN   D 1 207 ? -17.414 7.313   20.942  1.00 21.37 ? 186 GLN   D CB  1 
ATOM   6897 C CG  . GLN   D 1 207 ? -16.459 6.210   21.390  1.00 24.34 ? 186 GLN   D CG  1 
ATOM   6898 C CD  . GLN   D 1 207 ? -15.624 5.647   20.257  1.00 26.30 ? 186 GLN   D CD  1 
ATOM   6899 O OE1 . GLN   D 1 207 ? -15.973 5.812   19.091  1.00 35.89 ? 186 GLN   D OE1 1 
ATOM   6900 N NE2 . GLN   D 1 207 ? -14.532 4.985   20.577  1.00 27.65 ? 186 GLN   D NE2 1 
ATOM   6901 N N   . SER   D 1 208 ? -19.977 8.885   20.547  1.00 20.52 ? 187 SER   D N   1 
ATOM   6902 C CA  . SER   D 1 208 ? -20.667 10.081  20.042  1.00 21.44 ? 187 SER   D CA  1 
ATOM   6903 C C   . SER   D 1 208 ? -21.549 10.717  21.117  1.00 19.13 ? 187 SER   D C   1 
ATOM   6904 O O   . SER   D 1 208 ? -21.615 11.947  21.218  1.00 18.78 ? 187 SER   D O   1 
ATOM   6905 C CB  . SER   D 1 208 ? -21.520 9.771   18.808  1.00 24.14 ? 187 SER   D CB  1 
ATOM   6906 O OG  . SER   D 1 208 ? -20.699 9.443   17.699  1.00 25.80 ? 187 SER   D OG  1 
ATOM   6907 N N   . ALA   D 1 209 ? -22.288 9.899   21.889  1.00 18.53 ? 188 ALA   D N   1 
ATOM   6908 C CA  . ALA   D 1 209 ? -23.162 10.492  22.896  1.00 21.39 ? 188 ALA   D CA  1 
ATOM   6909 C C   . ALA   D 1 209 ? -22.370 11.046  24.082  1.00 22.92 ? 188 ALA   D C   1 
ATOM   6910 O O   . ALA   D 1 209 ? -22.756 12.063  24.682  1.00 21.81 ? 188 ALA   D O   1 
ATOM   6911 C CB  . ALA   D 1 209 ? -24.194 9.505   23.354  1.00 19.29 ? 188 ALA   D CB  1 
ATOM   6912 N N   . ALA   D 1 210 ? -21.247 10.388  24.430  1.00 20.44 ? 189 ALA   D N   1 
ATOM   6913 C CA  . ALA   D 1 210 ? -20.398 10.967  25.478  1.00 20.17 ? 189 ALA   D CA  1 
ATOM   6914 C C   . ALA   D 1 210 ? -19.970 12.373  25.055  1.00 22.32 ? 189 ALA   D C   1 
ATOM   6915 O O   . ALA   D 1 210 ? -20.006 13.317  25.858  1.00 23.18 ? 189 ALA   D O   1 
ATOM   6916 C CB  . ALA   D 1 210 ? -19.146 10.097  25.706  1.00 20.60 ? 189 ALA   D CB  1 
ATOM   6917 N N   . LEU   D 1 211 ? -19.499 12.516  23.806  1.00 20.07 ? 190 LEU   D N   1 
ATOM   6918 C CA  . LEU   D 1 211 ? -19.010 13.823  23.372  1.00 22.43 ? 190 LEU   D CA  1 
ATOM   6919 C C   . LEU   D 1 211 ? -20.125 14.877  23.437  1.00 25.65 ? 190 LEU   D C   1 
ATOM   6920 O O   . LEU   D 1 211 ? -19.928 15.997  23.910  1.00 27.71 ? 190 LEU   D O   1 
ATOM   6921 C CB  . LEU   D 1 211 ? -18.458 13.658  21.956  1.00 21.73 ? 190 LEU   D CB  1 
ATOM   6922 C CG  . LEU   D 1 211 ? -17.953 14.943  21.293  1.00 29.74 ? 190 LEU   D CG  1 
ATOM   6923 C CD1 . LEU   D 1 211 ? -16.638 15.376  21.943  1.00 32.27 ? 190 LEU   D CD1 1 
ATOM   6924 C CD2 . LEU   D 1 211 ? -17.782 14.762  19.784  1.00 29.96 ? 190 LEU   D CD2 1 
ATOM   6925 N N   . GLU   D 1 212 ? -21.297 14.533  22.887  1.00 27.03 ? 191 GLU   D N   1 
ATOM   6926 C CA  . GLU   D 1 212 ? -22.373 15.497  22.676  1.00 27.31 ? 191 GLU   D CA  1 
ATOM   6927 C C   . GLU   D 1 212 ? -23.095 15.827  23.983  1.00 27.55 ? 191 GLU   D C   1 
ATOM   6928 O O   . GLU   D 1 212 ? -23.578 16.936  24.128  1.00 26.29 ? 191 GLU   D O   1 
ATOM   6929 C CB  . GLU   D 1 212 ? -23.377 14.893  21.692  1.00 24.38 ? 191 GLU   D CB  1 
ATOM   6930 C CG  . GLU   D 1 212 ? -24.392 15.902  21.150  1.00 29.10 ? 191 GLU   D CG  1 
ATOM   6931 C CD  . GLU   D 1 212 ? -25.287 15.262  20.094  1.00 31.51 ? 191 GLU   D CD  1 
ATOM   6932 O OE1 . GLU   D 1 212 ? -26.362 15.847  19.841  1.00 32.37 ? 191 GLU   D OE1 1 
ATOM   6933 O OE2 . GLU   D 1 212 ? -24.927 14.204  19.496  1.00 34.59 ? 191 GLU   D OE2 1 
ATOM   6934 N N   . LEU   D 1 213 ? -23.193 14.858  24.899  1.00 22.82 ? 192 LEU   D N   1 
ATOM   6935 C CA  . LEU   D 1 213 ? -23.953 15.056  26.129  1.00 23.96 ? 192 LEU   D CA  1 
ATOM   6936 C C   . LEU   D 1 213 ? -23.095 15.563  27.290  1.00 24.86 ? 192 LEU   D C   1 
ATOM   6937 O O   . LEU   D 1 213 ? -23.635 16.014  28.299  1.00 25.08 ? 192 LEU   D O   1 
ATOM   6938 C CB  . LEU   D 1 213 ? -24.770 13.820  26.508  1.00 22.78 ? 192 LEU   D CB  1 
ATOM   6939 C CG  . LEU   D 1 213 ? -25.736 13.340  25.414  1.00 22.13 ? 192 LEU   D CG  1 
ATOM   6940 C CD1 . LEU   D 1 213 ? -26.517 12.132  25.936  1.00 22.40 ? 192 LEU   D CD1 1 
ATOM   6941 C CD2 . LEU   D 1 213 ? -26.711 14.461  25.013  1.00 20.05 ? 192 LEU   D CD2 1 
ATOM   6942 N N   . ALA   D 1 214 ? -21.773 15.578  27.105  1.00 22.55 ? 193 ALA   D N   1 
ATOM   6943 C CA  . ALA   D 1 214 ? -20.860 16.056  28.135  1.00 28.11 ? 193 ALA   D CA  1 
ATOM   6944 C C   . ALA   D 1 214 ? -21.240 17.473  28.571  1.00 31.30 ? 193 ALA   D C   1 
ATOM   6945 O O   . ALA   D 1 214 ? -21.299 17.758  29.767  1.00 33.89 ? 193 ALA   D O   1 
ATOM   6946 C CB  . ALA   D 1 214 ? -19.437 16.001  27.619  1.00 25.96 ? 193 ALA   D CB  1 
ATOM   6947 N N   . PRO   D 1 215 ? -21.526 18.411  27.646  1.00 31.71 ? 194 PRO   D N   1 
ATOM   6948 C CA  . PRO   D 1 215 ? -21.855 19.786  28.043  1.00 34.81 ? 194 PRO   D CA  1 
ATOM   6949 C C   . PRO   D 1 215 ? -23.090 19.863  28.932  1.00 36.16 ? 194 PRO   D C   1 
ATOM   6950 O O   . PRO   D 1 215 ? -23.290 20.852  29.620  1.00 39.65 ? 194 PRO   D O   1 
ATOM   6951 C CB  . PRO   D 1 215 ? -22.068 20.494  26.701  1.00 35.54 ? 194 PRO   D CB  1 
ATOM   6952 C CG  . PRO   D 1 215 ? -21.212 19.682  25.743  1.00 36.48 ? 194 PRO   D CG  1 
ATOM   6953 C CD  . PRO   D 1 215 ? -21.467 18.249  26.187  1.00 32.93 ? 194 PRO   D CD  1 
ATOM   6954 N N   . TYR   D 1 216 ? -23.910 18.811  28.929  1.00 36.61 ? 195 TYR   D N   1 
ATOM   6955 C CA  . TYR   D 1 216 ? -25.122 18.772  29.733  1.00 35.49 ? 195 TYR   D CA  1 
ATOM   6956 C C   . TYR   D 1 216 ? -24.868 18.032  31.037  1.00 37.29 ? 195 TYR   D C   1 
ATOM   6957 O O   . TYR   D 1 216 ? -25.805 17.804  31.793  1.00 44.60 ? 195 TYR   D O   1 
ATOM   6958 C CB  . TYR   D 1 216 ? -26.253 18.018  29.026  1.00 41.54 ? 195 TYR   D CB  1 
ATOM   6959 C CG  . TYR   D 1 216 ? -26.702 18.725  27.754  1.00 49.79 ? 195 TYR   D CG  1 
ATOM   6960 C CD1 . TYR   D 1 216 ? -26.039 18.518  26.542  1.00 46.08 ? 195 TYR   D CD1 1 
ATOM   6961 C CD2 . TYR   D 1 216 ? -27.773 19.620  27.774  1.00 50.07 ? 195 TYR   D CD2 1 
ATOM   6962 C CE1 . TYR   D 1 216 ? -26.425 19.176  25.384  1.00 50.66 ? 195 TYR   D CE1 1 
ATOM   6963 C CE2 . TYR   D 1 216 ? -28.170 20.276  26.618  1.00 56.85 ? 195 TYR   D CE2 1 
ATOM   6964 C CZ  . TYR   D 1 216 ? -27.496 20.054  25.428  1.00 56.24 ? 195 TYR   D CZ  1 
ATOM   6965 O OH  . TYR   D 1 216 ? -27.900 20.705  24.303  1.00 57.35 ? 195 TYR   D OH  1 
ATOM   6966 N N   . GLY   D 1 217 ? -23.626 17.599  31.270  1.00 33.45 ? 196 GLY   D N   1 
ATOM   6967 C CA  . GLY   D 1 217 ? -23.322 16.847  32.478  1.00 30.54 ? 196 GLY   D CA  1 
ATOM   6968 C C   . GLY   D 1 217 ? -23.803 15.392  32.467  1.00 31.61 ? 196 GLY   D C   1 
ATOM   6969 O O   . GLY   D 1 217 ? -23.817 14.766  33.514  1.00 32.59 ? 196 GLY   D O   1 
ATOM   6970 N N   . ILE   D 1 218 ? -24.147 14.821  31.300  1.00 26.56 ? 197 ILE   D N   1 
ATOM   6971 C CA  . ILE   D 1 218 ? -24.531 13.404  31.250  1.00 22.46 ? 197 ILE   D CA  1 
ATOM   6972 C C   . ILE   D 1 218 ? -23.310 12.618  30.769  1.00 21.01 ? 197 ILE   D C   1 
ATOM   6973 O O   . ILE   D 1 218 ? -22.761 12.929  29.704  1.00 22.44 ? 197 ILE   D O   1 
ATOM   6974 C CB  . ILE   D 1 218 ? -25.714 13.162  30.288  1.00 22.46 ? 197 ILE   D CB  1 
ATOM   6975 C CG1 . ILE   D 1 218 ? -27.009 14.014  30.659  1.00 24.18 ? 197 ILE   D CG1 1 
ATOM   6976 C CG2 . ILE   D 1 218 ? -26.041 11.658  30.204  1.00 25.28 ? 197 ILE   D CG2 1 
ATOM   6977 C CD1 . ILE   D 1 218 ? -28.074 14.083  29.556  1.00 22.32 ? 197 ILE   D CD1 1 
ATOM   6978 N N   . ARG   D 1 219 ? -22.923 11.597  31.542  1.00 21.09 ? 198 ARG   D N   1 
ATOM   6979 C CA  . ARG   D 1 219 ? -21.775 10.792  31.147  1.00 22.31 ? 198 ARG   D CA  1 
ATOM   6980 C C   . ARG   D 1 219 ? -22.332 9.577   30.403  1.00 22.66 ? 198 ARG   D C   1 
ATOM   6981 O O   . ARG   D 1 219 ? -23.445 9.143   30.686  1.00 22.61 ? 198 ARG   D O   1 
ATOM   6982 C CB  . ARG   D 1 219 ? -20.910 10.372  32.355  1.00 20.52 ? 198 ARG   D CB  1 
ATOM   6983 C CG  . ARG   D 1 219 ? -20.283 11.566  33.087  1.00 20.21 ? 198 ARG   D CG  1 
ATOM   6984 C CD  . ARG   D 1 219 ? -19.511 11.173  34.373  1.00 20.15 ? 198 ARG   D CD  1 
ATOM   6985 N NE  . ARG   D 1 219 ? -20.378 10.506  35.356  1.00 20.93 ? 198 ARG   D NE  1 
ATOM   6986 C CZ  . ARG   D 1 219 ? -20.479 9.187   35.529  1.00 20.55 ? 198 ARG   D CZ  1 
ATOM   6987 N NH1 . ARG   D 1 219 ? -19.682 8.330   34.899  1.00 21.08 ? 198 ARG   D NH1 1 
ATOM   6988 N NH2 . ARG   D 1 219 ? -21.355 8.728   36.388  1.00 21.77 ? 198 ARG   D NH2 1 
ATOM   6989 N N   . VAL   D 1 220 ? -21.532 9.040   29.477  1.00 20.74 ? 199 VAL   D N   1 
ATOM   6990 C CA  . VAL   D 1 220 ? -21.927 7.877   28.712  1.00 17.59 ? 199 VAL   D CA  1 
ATOM   6991 C C   . VAL   D 1 220 ? -20.754 6.907   28.652  1.00 16.93 ? 199 VAL   D C   1 
ATOM   6992 O O   . VAL   D 1 220 ? -19.713 7.239   28.093  1.00 19.18 ? 199 VAL   D O   1 
ATOM   6993 C CB  . VAL   D 1 220 ? -22.396 8.253   27.293  1.00 20.66 ? 199 VAL   D CB  1 
ATOM   6994 C CG1 . VAL   D 1 220 ? -22.972 7.015   26.612  1.00 18.94 ? 199 VAL   D CG1 1 
ATOM   6995 C CG2 . VAL   D 1 220 ? -23.448 9.376   27.297  1.00 22.04 ? 199 VAL   D CG2 1 
ATOM   6996 N N   . ASN   D 1 221 ? -20.982 5.649   29.039  1.00 16.16 ? 200 ASN   D N   1 
ATOM   6997 C CA  . ASN   D 1 221 ? -19.856 4.746   29.158  1.00 17.93 ? 200 ASN   D CA  1 
ATOM   6998 C C   . ASN   D 1 221 ? -20.387 3.365   28.847  1.00 20.34 ? 200 ASN   D C   1 
ATOM   6999 O O   . ASN   D 1 221 ? -21.592 3.223   28.712  1.00 21.09 ? 200 ASN   D O   1 
ATOM   7000 C CB  . ASN   D 1 221 ? -19.311 4.693   30.592  1.00 17.92 ? 200 ASN   D CB  1 
ATOM   7001 C CG  . ASN   D 1 221 ? -18.613 5.985   30.969  1.00 19.46 ? 200 ASN   D CG  1 
ATOM   7002 O OD1 . ASN   D 1 221 ? -17.599 6.296   30.356  1.00 19.35 ? 200 ASN   D OD1 1 
ATOM   7003 N ND2 . ASN   D 1 221 ? -19.130 6.757   31.927  1.00 19.51 ? 200 ASN   D ND2 1 
ATOM   7004 N N   . GLY   D 1 222 ? -19.470 2.397   28.748  1.00 17.87 ? 201 GLY   D N   1 
ATOM   7005 C CA  . GLY   D 1 222 ? -19.826 1.025   28.404  1.00 18.60 ? 201 GLY   D CA  1 
ATOM   7006 C C   . GLY   D 1 222 ? -19.194 0.005   29.352  1.00 18.08 ? 201 GLY   D C   1 
ATOM   7007 O O   . GLY   D 1 222 ? -18.166 0.253   29.975  1.00 21.79 ? 201 GLY   D O   1 
ATOM   7008 N N   . VAL   D 1 223 ? -19.815 -1.185  29.425  1.00 20.15 ? 202 VAL   D N   1 
ATOM   7009 C CA  . VAL   D 1 223 ? -19.286 -2.349  30.107  1.00 18.64 ? 202 VAL   D CA  1 
ATOM   7010 C C   . VAL   D 1 223 ? -19.337 -3.467  29.079  1.00 21.42 ? 202 VAL   D C   1 
ATOM   7011 O O   . VAL   D 1 223 ? -20.390 -3.642  28.459  1.00 21.83 ? 202 VAL   D O   1 
ATOM   7012 C CB  . VAL   D 1 223 ? -20.164 -2.735  31.321  1.00 18.52 ? 202 VAL   D CB  1 
ATOM   7013 C CG1 . VAL   D 1 223 ? -19.765 -4.113  31.902  1.00 19.67 ? 202 VAL   D CG1 1 
ATOM   7014 C CG2 . VAL   D 1 223 ? -20.152 -1.637  32.392  1.00 21.11 ? 202 VAL   D CG2 1 
ATOM   7015 N N   . ALA   D 1 224 ? -18.190 -4.146  28.855  1.00 21.64 ? 203 ALA   D N   1 
ATOM   7016 C CA  . ALA   D 1 224 ? -18.055 -5.132  27.792  1.00 20.71 ? 203 ALA   D CA  1 
ATOM   7017 C C   . ALA   D 1 224 ? -17.749 -6.498  28.397  1.00 20.53 ? 203 ALA   D C   1 
ATOM   7018 O O   . ALA   D 1 224 ? -16.586 -6.830  28.675  1.00 20.50 ? 203 ALA   D O   1 
ATOM   7019 C CB  . ALA   D 1 224 ? -16.974 -4.691  26.790  1.00 20.09 ? 203 ALA   D CB  1 
ATOM   7020 N N   . PRO   D 1 225 ? -18.783 -7.357  28.631  1.00 21.25 ? 204 PRO   D N   1 
ATOM   7021 C CA  . PRO   D 1 225 ? -18.545 -8.720  29.109  1.00 21.37 ? 204 PRO   D CA  1 
ATOM   7022 C C   . PRO   D 1 225 ? -17.812 -9.525  28.051  1.00 23.95 ? 204 PRO   D C   1 
ATOM   7023 O O   . PRO   D 1 225 ? -17.959 -9.262  26.856  1.00 25.69 ? 204 PRO   D O   1 
ATOM   7024 C CB  . PRO   D 1 225 ? -19.930 -9.324  29.379  1.00 21.63 ? 204 PRO   D CB  1 
ATOM   7025 C CG  . PRO   D 1 225 ? -20.861 -8.137  29.352  1.00 24.82 ? 204 PRO   D CG  1 
ATOM   7026 C CD  . PRO   D 1 225 ? -20.214 -7.059  28.469  1.00 24.31 ? 204 PRO   D CD  1 
ATOM   7027 N N   . GLY   D 1 226 ? -17.111 -10.563 28.519  1.00 24.83 ? 205 GLY   D N   1 
ATOM   7028 C CA  . GLY   D 1 226 ? -16.582 -11.570 27.625  1.00 26.40 ? 205 GLY   D CA  1 
ATOM   7029 C C   . GLY   D 1 226 ? -17.589 -12.713 27.585  1.00 32.05 ? 205 GLY   D C   1 
ATOM   7030 O O   . GLY   D 1 226 ? -18.557 -12.676 26.833  1.00 37.13 ? 205 GLY   D O   1 
ATOM   7031 N N   . VAL   D 1 227 ? -17.361 -13.747 28.389  1.00 27.89 ? 206 VAL   D N   1 
ATOM   7032 C CA  A VAL   D 1 227 ? -18.417 -14.723 28.587  0.60 30.90 ? 206 VAL   D CA  1 
ATOM   7033 C CA  B VAL   D 1 227 ? -18.427 -14.712 28.584  0.40 29.77 ? 206 VAL   D CA  1 
ATOM   7034 C C   . VAL   D 1 227 ? -18.912 -14.578 30.023  1.00 31.49 ? 206 VAL   D C   1 
ATOM   7035 O O   . VAL   D 1 227 ? -18.128 -14.646 30.969  1.00 32.02 ? 206 VAL   D O   1 
ATOM   7036 C CB  A VAL   D 1 227 ? -17.980 -16.160 28.258  0.60 34.06 ? 206 VAL   D CB  1 
ATOM   7037 C CB  B VAL   D 1 227 ? -18.089 -16.163 28.200  0.40 30.44 ? 206 VAL   D CB  1 
ATOM   7038 C CG1 A VAL   D 1 227 ? -16.750 -16.550 29.058  0.60 33.47 ? 206 VAL   D CG1 1 
ATOM   7039 C CG1 B VAL   D 1 227 ? -17.686 -16.274 26.735  0.40 28.71 ? 206 VAL   D CG1 1 
ATOM   7040 C CG2 A VAL   D 1 227 ? -19.103 -17.160 28.485  0.60 35.57 ? 206 VAL   D CG2 1 
ATOM   7041 C CG2 B VAL   D 1 227 ? -17.009 -16.738 29.102  0.40 29.84 ? 206 VAL   D CG2 1 
ATOM   7042 N N   . SER   D 1 228 ? -20.209 -14.299 30.149  1.00 32.06 ? 207 SER   D N   1 
ATOM   7043 C CA  . SER   D 1 228 ? -20.876 -14.270 31.425  1.00 34.77 ? 207 SER   D CA  1 
ATOM   7044 C C   . SER   D 1 228 ? -21.889 -15.405 31.392  1.00 42.63 ? 207 SER   D C   1 
ATOM   7045 O O   . SER   D 1 228 ? -21.606 -16.451 30.804  1.00 43.52 ? 207 SER   D O   1 
ATOM   7046 C CB  . SER   D 1 228 ? -21.521 -12.941 31.664  1.00 35.20 ? 207 SER   D CB  1 
ATOM   7047 O OG  . SER   D 1 228 ? -21.922 -12.890 33.027  1.00 35.62 ? 207 SER   D OG  1 
ATOM   7048 N N   . LEU   D 1 229 ? -23.050 -15.202 32.014  1.00 40.86 ? 208 LEU   D N   1 
ATOM   7049 C CA  . LEU   D 1 229 ? -24.019 -16.287 32.121  1.00 47.06 ? 208 LEU   D CA  1 
ATOM   7050 C C   . LEU   D 1 229 ? -24.180 -16.893 30.732  1.00 50.37 ? 208 LEU   D C   1 
ATOM   7051 O O   . LEU   D 1 229 ? -24.477 -16.175 29.771  1.00 51.58 ? 208 LEU   D O   1 
ATOM   7052 C CB  . LEU   D 1 229 ? -25.356 -15.801 32.672  1.00 46.47 ? 208 LEU   D CB  1 
ATOM   7053 C CG  . LEU   D 1 229 ? -25.342 -15.262 34.106  1.00 47.09 ? 208 LEU   D CG  1 
ATOM   7054 C CD1 . LEU   D 1 229 ? -26.784 -15.160 34.577  1.00 43.90 ? 208 LEU   D CD1 1 
ATOM   7055 C CD2 . LEU   D 1 229 ? -24.512 -16.109 35.065  1.00 45.58 ? 208 LEU   D CD2 1 
ATOM   7056 N N   . LEU   D 1 230 ? -23.890 -18.195 30.626  1.00 46.14 ? 209 LEU   D N   1 
ATOM   7057 C CA  . LEU   D 1 230 ? -23.964 -18.868 29.339  1.00 52.77 ? 209 LEU   D CA  1 
ATOM   7058 C C   . LEU   D 1 230 ? -25.428 -19.149 28.978  1.00 58.02 ? 209 LEU   D C   1 
ATOM   7059 O O   . LEU   D 1 230 ? -26.269 -19.230 29.872  1.00 53.85 ? 209 LEU   D O   1 
ATOM   7060 C CB  . LEU   D 1 230 ? -23.074 -20.108 29.416  1.00 51.42 ? 209 LEU   D CB  1 
ATOM   7061 C CG  . LEU   D 1 230 ? -21.572 -19.807 29.548  1.00 48.95 ? 209 LEU   D CG  1 
ATOM   7062 C CD1 . LEU   D 1 230 ? -20.781 -20.875 30.305  1.00 47.38 ? 209 LEU   D CD1 1 
ATOM   7063 C CD2 . LEU   D 1 230 ? -21.003 -19.640 28.166  1.00 42.11 ? 209 LEU   D CD2 1 
ATOM   7064 N N   . PRO   D 1 231 ? -25.787 -19.229 27.670  1.00 67.26 ? 210 PRO   D N   1 
ATOM   7065 C CA  . PRO   D 1 231 ? -27.188 -19.347 27.241  1.00 72.65 ? 210 PRO   D CA  1 
ATOM   7066 C C   . PRO   D 1 231 ? -28.013 -20.462 27.882  1.00 71.42 ? 210 PRO   D C   1 
ATOM   7067 O O   . PRO   D 1 231 ? -27.459 -21.459 28.355  1.00 61.51 ? 210 PRO   D O   1 
ATOM   7068 C CB  . PRO   D 1 231 ? -27.085 -19.511 25.712  1.00 74.85 ? 210 PRO   D CB  1 
ATOM   7069 C CG  . PRO   D 1 231 ? -25.792 -18.817 25.358  1.00 78.49 ? 210 PRO   D CG  1 
ATOM   7070 C CD  . PRO   D 1 231 ? -24.865 -19.154 26.522  1.00 77.88 ? 210 PRO   D CD  1 
ATOM   7071 N N   . VAL   D 1 232 ? -29.342 -20.261 27.878  1.00 76.31 ? 211 VAL   D N   1 
ATOM   7072 C CA  . VAL   D 1 232 ? -30.311 -21.163 28.487  1.00 77.67 ? 211 VAL   D CA  1 
ATOM   7073 C C   . VAL   D 1 232 ? -30.127 -22.569 27.913  1.00 80.83 ? 211 VAL   D C   1 
ATOM   7074 O O   . VAL   D 1 232 ? -30.028 -23.534 28.677  1.00 77.00 ? 211 VAL   D O   1 
ATOM   7075 C CB  . VAL   D 1 232 ? -31.757 -20.654 28.313  1.00 70.04 ? 211 VAL   D CB  1 
ATOM   7076 N N   . ALA   D 1 233 ? -30.051 -22.655 26.572  1.00 78.07 ? 212 ALA   D N   1 
ATOM   7077 C CA  . ALA   D 1 233 ? -29.877 -23.904 25.843  1.00 79.09 ? 212 ALA   D CA  1 
ATOM   7078 C C   . ALA   D 1 233 ? -28.431 -24.044 25.365  1.00 82.34 ? 212 ALA   D C   1 
ATOM   7079 O O   . ALA   D 1 233 ? -28.105 -23.703 24.226  1.00 86.16 ? 212 ALA   D O   1 
ATOM   7080 C CB  . ALA   D 1 233 ? -30.864 -23.989 24.694  1.00 69.52 ? 212 ALA   D CB  1 
ATOM   7081 N N   . MET   D 1 234 ? -27.572 -24.533 26.272  1.00 71.85 ? 213 MET   D N   1 
ATOM   7082 C CA  . MET   D 1 234 ? -26.202 -24.921 25.976  1.00 61.26 ? 213 MET   D CA  1 
ATOM   7083 C C   . MET   D 1 234 ? -25.822 -26.081 26.897  1.00 55.82 ? 213 MET   D C   1 
ATOM   7084 O O   . MET   D 1 234 ? -26.025 -26.019 28.112  1.00 54.34 ? 213 MET   D O   1 
ATOM   7085 C CB  . MET   D 1 234 ? -25.224 -23.747 26.135  1.00 65.77 ? 213 MET   D CB  1 
ATOM   7086 C CG  . MET   D 1 234 ? -23.828 -24.015 25.588  0.60 60.40 ? 213 MET   D CG  1 
ATOM   7087 S SD  . MET   D 1 234 ? -22.623 -22.683 25.785  0.60 57.38 ? 213 MET   D SD  1 
ATOM   7088 C CE  . MET   D 1 234 ? -23.015 -21.551 24.443  0.60 52.80 ? 213 MET   D CE  1 
ATOM   7089 N N   . GLY   D 1 235 ? -25.280 -27.142 26.288  1.00 53.75 ? 214 GLY   D N   1 
ATOM   7090 C CA  . GLY   D 1 235 ? -24.896 -28.355 26.987  1.00 49.29 ? 214 GLY   D CA  1 
ATOM   7091 C C   . GLY   D 1 235 ? -23.700 -28.114 27.902  1.00 48.33 ? 214 GLY   D C   1 
ATOM   7092 O O   . GLY   D 1 235 ? -23.011 -27.106 27.756  1.00 42.65 ? 214 GLY   D O   1 
ATOM   7093 N N   . GLU   D 1 236 ? -23.480 -29.053 28.840  1.00 41.96 ? 215 GLU   D N   1 
ATOM   7094 C CA  . GLU   D 1 236 ? -22.401 -28.976 29.815  1.00 46.33 ? 215 GLU   D CA  1 
ATOM   7095 C C   . GLU   D 1 236 ? -21.055 -28.951 29.085  1.00 46.94 ? 215 GLU   D C   1 
ATOM   7096 O O   . GLU   D 1 236 ? -20.174 -28.174 29.475  1.00 44.27 ? 215 GLU   D O   1 
ATOM   7097 C CB  . GLU   D 1 236 ? -22.430 -30.034 30.929  1.00 41.81 ? 215 GLU   D CB  1 
ATOM   7098 C CG  . GLU   D 1 236 ? -23.624 -29.899 31.873  0.80 37.30 ? 215 GLU   D CG  1 
ATOM   7099 C CD  . GLU   D 1 236 ? -23.598 -28.676 32.780  0.80 43.79 ? 215 GLU   D CD  1 
ATOM   7100 O OE1 . GLU   D 1 236 ? -24.676 -28.303 33.268  0.80 43.01 ? 215 GLU   D OE1 1 
ATOM   7101 O OE2 . GLU   D 1 236 ? -22.510 -28.118 33.059  0.80 43.46 ? 215 GLU   D OE2 1 
ATOM   7102 N N   . GLU   D 1 237 ? -20.913 -29.805 28.050  1.00 47.66 ? 216 GLU   D N   1 
ATOM   7103 C CA  . GLU   D 1 237 ? -19.697 -29.925 27.242  1.00 48.80 ? 216 GLU   D CA  1 
ATOM   7104 C C   . GLU   D 1 237 ? -19.317 -28.555 26.675  1.00 45.15 ? 216 GLU   D C   1 
ATOM   7105 O O   . GLU   D 1 237 ? -18.177 -28.122 26.849  1.00 43.03 ? 216 GLU   D O   1 
ATOM   7106 C CB  . GLU   D 1 237 ? -19.763 -30.989 26.137  1.00 48.65 ? 216 GLU   D CB  1 
ATOM   7107 C CG  . GLU   D 1 237 ? -18.554 -30.996 25.200  1.00 51.33 ? 216 GLU   D CG  1 
ATOM   7108 N N   . GLU   D 1 238 ? -20.301 -27.872 26.066  1.00 42.57 ? 217 GLU   D N   1 
ATOM   7109 C CA  . GLU   D 1 238 ? -20.091 -26.597 25.396  1.00 47.97 ? 217 GLU   D CA  1 
ATOM   7110 C C   . GLU   D 1 238 ? -19.861 -25.461 26.404  1.00 53.07 ? 217 GLU   D C   1 
ATOM   7111 O O   . GLU   D 1 238 ? -19.151 -24.499 26.112  1.00 49.22 ? 217 GLU   D O   1 
ATOM   7112 C CB  . GLU   D 1 238 ? -21.244 -26.308 24.435  1.00 47.08 ? 217 GLU   D CB  1 
ATOM   7113 C CG  . GLU   D 1 238 ? -20.796 -25.536 23.196  1.00 51.21 ? 217 GLU   D CG  1 
ATOM   7114 N N   . LYS   D 1 239 ? -20.483 -25.551 27.585  1.00 50.61 ? 218 LYS   D N   1 
ATOM   7115 C CA  . LYS   D 1 239 ? -20.252 -24.552 28.620  1.00 45.83 ? 218 LYS   D CA  1 
ATOM   7116 C C   . LYS   D 1 239 ? -18.787 -24.628 29.053  1.00 42.89 ? 218 LYS   D C   1 
ATOM   7117 O O   . LYS   D 1 239 ? -18.102 -23.609 29.119  1.00 39.52 ? 218 LYS   D O   1 
ATOM   7118 C CB  . LYS   D 1 239 ? -21.270 -24.652 29.770  1.00 45.12 ? 218 LYS   D CB  1 
ATOM   7119 C CG  . LYS   D 1 239 ? -22.660 -24.121 29.424  0.50 45.64 ? 218 LYS   D CG  1 
ATOM   7120 C CD  . LYS   D 1 239 ? -23.695 -24.124 30.545  0.50 44.23 ? 218 LYS   D CD  1 
ATOM   7121 C CE  . LYS   D 1 239 ? -24.970 -23.508 30.043  0.50 44.67 ? 218 LYS   D CE  1 
ATOM   7122 N NZ  . LYS   D 1 239 ? -26.018 -23.307 31.053  0.50 41.55 ? 218 LYS   D NZ  1 
ATOM   7123 N N   . ASP   D 1 240 ? -18.352 -25.836 29.410  1.00 39.40 ? 219 ASP   D N   1 
ATOM   7124 C CA  A ASP   D 1 240 ? -16.903 -26.028 29.725  0.60 40.65 ? 219 ASP   D CA  1 
ATOM   7125 C CA  B ASP   D 1 240 ? -16.902 -26.036 29.719  0.40 39.36 ? 219 ASP   D CA  1 
ATOM   7126 C C   . ASP   D 1 240 ? -15.854 -25.607 28.642  1.00 37.41 ? 219 ASP   D C   1 
ATOM   7127 O O   . ASP   D 1 240 ? -14.667 -25.086 28.800  1.00 38.18 ? 219 ASP   D O   1 
ATOM   7128 C CB  A ASP   D 1 240 ? -16.683 -27.461 30.182  0.60 43.77 ? 219 ASP   D CB  1 
ATOM   7129 C CB  B ASP   D 1 240 ? -16.640 -27.494 30.065  0.40 39.00 ? 219 ASP   D CB  1 
ATOM   7130 C CG  A ASP   D 1 240 ? -17.536 -27.869 31.374  0.60 44.01 ? 219 ASP   D CG  1 
ATOM   7131 C CG  B ASP   D 1 240 ? -15.184 -27.848 30.330  0.40 40.55 ? 219 ASP   D CG  1 
ATOM   7132 O OD1 A ASP   D 1 240 ? -18.072 -26.962 32.047  0.60 40.97 ? 219 ASP   D OD1 1 
ATOM   7133 O OD1 B ASP   D 1 240 ? -14.695 -27.523 31.431  0.40 38.85 ? 219 ASP   D OD1 1 
ATOM   7134 O OD2 A ASP   D 1 240 ? -17.664 -29.085 31.619  0.60 45.39 ? 219 ASP   D OD2 1 
ATOM   7135 O OD2 B ASP   D 1 240 ? -14.550 -28.440 29.432  0.40 42.35 ? 219 ASP   D OD2 1 
ATOM   7136 N N   . LYS   D 1 241 ? -16.311 -25.776 27.397  1.00 35.70 ? 220 LYS   D N   1 
ATOM   7137 C CA  . LYS   D 1 241 ? -15.462 -25.358 26.284  1.00 37.58 ? 220 LYS   D CA  1 
ATOM   7138 C C   . LYS   D 1 241 ? -15.127 -23.859 26.397  1.00 37.16 ? 220 LYS   D C   1 
ATOM   7139 O O   . LYS   D 1 241 ? -13.956 -23.483 26.279  1.00 36.48 ? 220 LYS   D O   1 
ATOM   7140 C CB  . LYS   D 1 241 ? -16.086 -25.785 24.944  1.00 40.31 ? 220 LYS   D CB  1 
ATOM   7141 C CG  . LYS   D 1 241 ? -15.289 -25.448 23.674  1.00 43.92 ? 220 LYS   D CG  1 
ATOM   7142 C CD  . LYS   D 1 241 ? -15.968 -25.767 22.341  0.50 42.47 ? 220 LYS   D CD  1 
ATOM   7143 C CE  . LYS   D 1 241 ? -16.962 -24.764 21.824  0.50 42.27 ? 220 LYS   D CE  1 
ATOM   7144 N NZ  . LYS   D 1 241 ? -16.326 -23.604 21.188  0.50 44.37 ? 220 LYS   D NZ  1 
ATOM   7145 N N   . TRP   D 1 242 ? -16.149 -23.014 26.647  1.00 33.11 ? 221 TRP   D N   1 
ATOM   7146 C CA  . TRP   D 1 242 ? -15.963 -21.571 26.778  1.00 36.08 ? 221 TRP   D CA  1 
ATOM   7147 C C   . TRP   D 1 242 ? -15.243 -21.216 28.079  1.00 34.29 ? 221 TRP   D C   1 
ATOM   7148 O O   . TRP   D 1 242 ? -14.364 -20.350 28.107  1.00 34.14 ? 221 TRP   D O   1 
ATOM   7149 C CB  . TRP   D 1 242 ? -17.320 -20.855 26.721  1.00 40.08 ? 221 TRP   D CB  1 
ATOM   7150 C CG  . TRP   D 1 242 ? -17.815 -20.718 25.311  1.00 50.77 ? 221 TRP   D CG  1 
ATOM   7151 C CD1 . TRP   D 1 242 ? -18.703 -21.523 24.657  1.00 53.60 ? 221 TRP   D CD1 1 
ATOM   7152 C CD2 . TRP   D 1 242 ? -17.375 -19.725 24.358  1.00 53.05 ? 221 TRP   D CD2 1 
ATOM   7153 N NE1 . TRP   D 1 242 ? -18.862 -21.087 23.369  1.00 56.15 ? 221 TRP   D NE1 1 
ATOM   7154 C CE2 . TRP   D 1 242 ? -18.061 -19.992 23.153  1.00 55.97 ? 221 TRP   D CE2 1 
ATOM   7155 C CE3 . TRP   D 1 242 ? -16.476 -18.652 24.408  1.00 52.52 ? 221 TRP   D CE3 1 
ATOM   7156 C CZ2 . TRP   D 1 242 ? -17.879 -19.210 22.014  1.00 53.59 ? 221 TRP   D CZ2 1 
ATOM   7157 C CZ3 . TRP   D 1 242 ? -16.292 -17.886 23.278  1.00 58.98 ? 221 TRP   D CZ3 1 
ATOM   7158 C CH2 . TRP   D 1 242 ? -16.984 -18.165 22.100  1.00 54.43 ? 221 TRP   D CH2 1 
ATOM   7159 N N   . ARG   D 1 243 ? -15.654 -21.862 29.178  1.00 33.83 ? 222 ARG   D N   1 
ATOM   7160 C CA  . ARG   D 1 243 ? -15.043 -21.611 30.475  1.00 32.62 ? 222 ARG   D CA  1 
ATOM   7161 C C   . ARG   D 1 243 ? -13.528 -21.793 30.385  1.00 30.03 ? 222 ARG   D C   1 
ATOM   7162 O O   . ARG   D 1 243 ? -12.779 -21.002 30.939  1.00 29.46 ? 222 ARG   D O   1 
ATOM   7163 C CB  . ARG   D 1 243 ? -15.704 -22.469 31.563  1.00 34.68 ? 222 ARG   D CB  1 
ATOM   7164 C CG  . ARG   D 1 243 ? -17.159 -22.051 31.749  1.00 34.70 ? 222 ARG   D CG  1 
ATOM   7165 C CD  . ARG   D 1 243 ? -17.715 -22.905 32.888  1.00 45.04 ? 222 ARG   D CD  1 
ATOM   7166 N NE  . ARG   D 1 243 ? -19.130 -22.605 33.124  1.00 46.41 ? 222 ARG   D NE  1 
ATOM   7167 C CZ  . ARG   D 1 243 ? -20.082 -23.520 33.338  1.00 52.18 ? 222 ARG   D CZ  1 
ATOM   7168 N NH1 . ARG   D 1 243 ? -19.761 -24.792 33.491  1.00 48.83 ? 222 ARG   D NH1 1 
ATOM   7169 N NH2 . ARG   D 1 243 ? -21.352 -23.160 33.404  1.00 48.77 ? 222 ARG   D NH2 1 
ATOM   7170 N N   . ARG   D 1 244 ? -13.106 -22.848 29.690  1.00 30.55 ? 223 ARG   D N   1 
ATOM   7171 C CA  . ARG   D 1 244 ? -11.721 -23.264 29.561  1.00 35.38 ? 223 ARG   D CA  1 
ATOM   7172 C C   . ARG   D 1 244 ? -10.859 -22.201 28.869  1.00 32.89 ? 223 ARG   D C   1 
ATOM   7173 O O   . ARG   D 1 244 ? -9.643  -22.207 29.007  1.00 32.62 ? 223 ARG   D O   1 
ATOM   7174 C CB  . ARG   D 1 244 ? -11.766 -24.540 28.717  1.00 42.58 ? 223 ARG   D CB  1 
ATOM   7175 C CG  A ARG   D 1 244 ? -10.668 -25.572 28.923  0.60 50.69 ? 223 ARG   D CG  1 
ATOM   7176 C CD  A ARG   D 1 244 ? -10.623 -26.569 27.760  0.60 52.52 ? 223 ARG   D CD  1 
ATOM   7177 N NE  A ARG   D 1 244 ? -11.890 -27.195 27.363  0.60 51.54 ? 223 ARG   D NE  1 
ATOM   7178 C CZ  A ARG   D 1 244 ? -12.608 -28.059 28.076  0.60 53.03 ? 223 ARG   D CZ  1 
ATOM   7179 N NH1 A ARG   D 1 244 ? -13.720 -28.556 27.571  0.60 50.57 ? 223 ARG   D NH1 1 
ATOM   7180 N NH2 A ARG   D 1 244 ? -12.221 -28.430 29.284  0.60 56.11 ? 223 ARG   D NH2 1 
ATOM   7181 N N   . LYS   D 1 245 ? -11.478 -21.285 28.129  1.00 32.51 ? 224 LYS   D N   1 
ATOM   7182 C CA  . LYS   D 1 245 ? -10.723 -20.285 27.382  1.00 33.04 ? 224 LYS   D CA  1 
ATOM   7183 C C   . LYS   D 1 245 ? -10.361 -19.075 28.256  1.00 29.76 ? 224 LYS   D C   1 
ATOM   7184 O O   . LYS   D 1 245 ? -9.532  -18.259 27.849  1.00 30.45 ? 224 LYS   D O   1 
ATOM   7185 C CB  . LYS   D 1 245 ? -11.520 -19.774 26.165  1.00 36.88 ? 224 LYS   D CB  1 
ATOM   7186 C CG  . LYS   D 1 245 ? -12.139 -20.805 25.186  1.00 38.71 ? 224 LYS   D CG  1 
ATOM   7187 C CD  . LYS   D 1 245 ? -13.061 -20.138 24.160  1.00 38.22 ? 224 LYS   D CD  1 
ATOM   7188 C CE  . LYS   D 1 245 ? -13.889 -21.006 23.220  1.00 38.18 ? 224 LYS   D CE  1 
ATOM   7189 N NZ  . LYS   D 1 245 ? -13.047 -21.938 22.470  1.00 37.14 ? 224 LYS   D NZ  1 
ATOM   7190 N N   . VAL   D 1 246 ? -10.971 -18.942 29.443  1.00 26.45 ? 225 VAL   D N   1 
ATOM   7191 C CA  . VAL   D 1 246 ? -10.834 -17.708 30.216  1.00 24.97 ? 225 VAL   D CA  1 
ATOM   7192 C C   . VAL   D 1 246 ? -9.584  -17.774 31.086  1.00 23.67 ? 225 VAL   D C   1 
ATOM   7193 O O   . VAL   D 1 246 ? -9.526  -18.646 31.967  1.00 22.88 ? 225 VAL   D O   1 
ATOM   7194 C CB  . VAL   D 1 246 ? -12.067 -17.398 31.090  1.00 23.58 ? 225 VAL   D CB  1 
ATOM   7195 C CG1 . VAL   D 1 246 ? -11.875 -16.124 31.919  1.00 22.13 ? 225 VAL   D CG1 1 
ATOM   7196 C CG2 . VAL   D 1 246 ? -13.343 -17.357 30.264  1.00 23.37 ? 225 VAL   D CG2 1 
ATOM   7197 N N   . PRO   D 1 247 ? -8.568  -16.889 30.871  1.00 23.63 ? 226 PRO   D N   1 
ATOM   7198 C CA  . PRO   D 1 247 ? -7.313  -16.925 31.644  1.00 26.43 ? 226 PRO   D CA  1 
ATOM   7199 C C   . PRO   D 1 247 ? -7.527  -16.833 33.162  1.00 25.25 ? 226 PRO   D C   1 
ATOM   7200 O O   . PRO   D 1 247 ? -6.906  -17.576 33.937  1.00 23.52 ? 226 PRO   D O   1 
ATOM   7201 C CB  . PRO   D 1 247 ? -6.466  -15.722 31.103  1.00 25.56 ? 226 PRO   D CB  1 
ATOM   7202 C CG  . PRO   D 1 247 ? -7.050  -15.437 29.732  1.00 25.40 ? 226 PRO   D CG  1 
ATOM   7203 C CD  . PRO   D 1 247 ? -8.516  -15.892 29.784  1.00 23.43 ? 226 PRO   D CD  1 
ATOM   7204 N N   . LEU   D 1 248 ? -8.405  -15.897 33.562  1.00 24.45 ? 227 LEU   D N   1 
ATOM   7205 C CA  . LEU   D 1 248 ? -8.632  -15.565 34.958  1.00 25.09 ? 227 LEU   D CA  1 
ATOM   7206 C C   . LEU   D 1 248 ? -9.678  -16.516 35.510  1.00 26.63 ? 227 LEU   D C   1 
ATOM   7207 O O   . LEU   D 1 248 ? -10.845 -16.163 35.586  1.00 27.05 ? 227 LEU   D O   1 
ATOM   7208 C CB  . LEU   D 1 248 ? -9.080  -14.118 35.168  1.00 24.53 ? 227 LEU   D CB  1 
ATOM   7209 C CG  . LEU   D 1 248 ? -9.037  -13.576 36.614  1.00 27.98 ? 227 LEU   D CG  1 
ATOM   7210 C CD1 . LEU   D 1 248 ? -7.595  -13.429 37.070  1.00 25.50 ? 227 LEU   D CD1 1 
ATOM   7211 C CD2 . LEU   D 1 248 ? -9.680  -12.188 36.657  1.00 24.65 ? 227 LEU   D CD2 1 
ATOM   7212 N N   . GLY   D 1 249 ? -9.225  -17.712 35.898  1.00 28.93 ? 228 GLY   D N   1 
ATOM   7213 C CA  . GLY   D 1 249 ? -10.020 -18.621 36.701  1.00 30.33 ? 228 GLY   D CA  1 
ATOM   7214 C C   . GLY   D 1 249 ? -10.772 -19.668 35.887  1.00 33.03 ? 228 GLY   D C   1 
ATOM   7215 O O   . GLY   D 1 249 ? -11.536 -20.424 36.478  1.00 28.66 ? 228 GLY   D O   1 
ATOM   7216 N N   . ARG   D 1 250 ? -10.609 -19.674 34.548  1.00 28.91 ? 229 ARG   D N   1 
ATOM   7217 C CA  . ARG   D 1 250 ? -11.290 -20.602 33.647  1.00 26.69 ? 229 ARG   D CA  1 
ATOM   7218 C C   . ARG   D 1 250 ? -12.770 -20.724 33.971  1.00 30.84 ? 229 ARG   D C   1 
ATOM   7219 O O   . ARG   D 1 250 ? -13.316 -21.834 34.023  1.00 29.19 ? 229 ARG   D O   1 
ATOM   7220 C CB  . ARG   D 1 250 ? -10.705 -22.014 33.751  1.00 30.74 ? 229 ARG   D CB  1 
ATOM   7221 C CG  . ARG   D 1 250 ? -9.203  -22.001 33.521  1.00 34.06 ? 229 ARG   D CG  1 
ATOM   7222 C CD  . ARG   D 1 250 ? -8.853  -21.589 32.108  1.00 38.39 ? 229 ARG   D CD  1 
ATOM   7223 N NE  . ARG   D 1 250 ? -7.403  -21.372 31.994  1.00 46.30 ? 229 ARG   D NE  1 
ATOM   7224 C CZ  . ARG   D 1 250 ? -6.747  -20.898 30.927  1.00 49.48 ? 229 ARG   D CZ  1 
ATOM   7225 N NH1 . ARG   D 1 250 ? -7.348  -20.776 29.753  1.00 41.13 ? 229 ARG   D NH1 1 
ATOM   7226 N NH2 . ARG   D 1 250 ? -5.469  -20.572 31.045  1.00 47.40 ? 229 ARG   D NH2 1 
ATOM   7227 N N   . ARG   D 1 251 ? -13.424 -19.575 34.159  1.00 26.47 ? 230 ARG   D N   1 
ATOM   7228 C CA  . ARG   D 1 251 ? -14.852 -19.578 34.415  1.00 28.12 ? 230 ARG   D CA  1 
ATOM   7229 C C   . ARG   D 1 251 ? -15.426 -18.294 33.828  1.00 28.43 ? 230 ARG   D C   1 
ATOM   7230 O O   . ARG   D 1 251 ? -14.687 -17.319 33.658  1.00 26.31 ? 230 ARG   D O   1 
ATOM   7231 C CB  . ARG   D 1 251 ? -15.084 -19.611 35.934  1.00 28.14 ? 230 ARG   D CB  1 
ATOM   7232 C CG  . ARG   D 1 251 ? -14.579 -18.412 36.731  1.00 31.72 ? 230 ARG   D CG  1 
ATOM   7233 C CD  . ARG   D 1 251 ? -15.006 -18.425 38.206  1.00 41.30 ? 230 ARG   D CD  1 
ATOM   7234 N NE  . ARG   D 1 251 ? -14.054 -19.243 38.968  1.00 50.24 ? 230 ARG   D NE  1 
ATOM   7235 N N   . GLU   D 1 252 ? -16.738 -18.296 33.579  1.00 24.30 ? 231 GLU   D N   1 
ATOM   7236 C CA  . GLU   D 1 252 ? -17.448 -17.116 33.069  1.00 28.68 ? 231 GLU   D CA  1 
ATOM   7237 C C   . GLU   D 1 252 ? -17.672 -16.100 34.196  1.00 27.78 ? 231 GLU   D C   1 
ATOM   7238 O O   . GLU   D 1 252 ? -17.559 -16.439 35.372  1.00 31.15 ? 231 GLU   D O   1 
ATOM   7239 C CB  . GLU   D 1 252 ? -18.816 -17.514 32.523  1.00 33.54 ? 231 GLU   D CB  1 
ATOM   7240 C CG  . GLU   D 1 252 ? -19.772 -17.992 33.617  1.00 32.79 ? 231 GLU   D CG  1 
ATOM   7241 C CD  . GLU   D 1 252 ? -19.818 -19.486 33.928  1.00 43.83 ? 231 GLU   D CD  1 
ATOM   7242 O OE1 . GLU   D 1 252 ? -20.963 -19.983 34.021  1.00 45.75 ? 231 GLU   D OE1 1 
ATOM   7243 O OE2 . GLU   D 1 252 ? -18.769 -20.165 34.047  1.00 37.42 ? 231 GLU   D OE2 1 
ATOM   7244 N N   . ALA   D 1 253 ? -17.940 -14.830 33.855  1.00 28.15 ? 232 ALA   D N   1 
ATOM   7245 C CA  . ALA   D 1 253 ? -18.297 -13.844 34.868  1.00 28.51 ? 232 ALA   D CA  1 
ATOM   7246 C C   . ALA   D 1 253 ? -19.666 -14.207 35.452  1.00 27.76 ? 232 ALA   D C   1 
ATOM   7247 O O   . ALA   D 1 253 ? -20.537 -14.671 34.737  1.00 27.62 ? 232 ALA   D O   1 
ATOM   7248 C CB  . ALA   D 1 253 ? -18.393 -12.448 34.268  1.00 27.51 ? 232 ALA   D CB  1 
ATOM   7249 N N   . SER   D 1 254 ? -19.867 -13.899 36.735  1.00 31.38 ? 233 SER   D N   1 
ATOM   7250 C CA  . SER   D 1 254 ? -21.202 -13.871 37.307  1.00 28.32 ? 233 SER   D CA  1 
ATOM   7251 C C   . SER   D 1 254 ? -21.927 -12.621 36.810  1.00 31.32 ? 233 SER   D C   1 
ATOM   7252 O O   . SER   D 1 254 ? -21.306 -11.617 36.405  1.00 27.26 ? 233 SER   D O   1 
ATOM   7253 C CB  . SER   D 1 254 ? -21.118 -13.935 38.822  1.00 29.01 ? 233 SER   D CB  1 
ATOM   7254 O OG  . SER   D 1 254 ? -20.731 -12.665 39.345  1.00 31.04 ? 233 SER   D OG  1 
ATOM   7255 N N   . ALA   D 1 255 ? -23.262 -12.674 36.815  1.00 24.32 ? 234 ALA   D N   1 
ATOM   7256 C CA  . ALA   D 1 255 ? -24.003 -11.468 36.483  1.00 26.70 ? 234 ALA   D CA  1 
ATOM   7257 C C   . ALA   D 1 255 ? -23.621 -10.318 37.422  1.00 26.78 ? 234 ALA   D C   1 
ATOM   7258 O O   . ALA   D 1 255 ? -23.585 -9.149  37.017  1.00 27.94 ? 234 ALA   D O   1 
ATOM   7259 C CB  . ALA   D 1 255 ? -25.494 -11.772 36.541  1.00 24.79 ? 234 ALA   D CB  1 
ATOM   7260 N N   . GLU   D 1 256 ? -23.354 -10.650 38.699  1.00 27.37 ? 235 GLU   D N   1 
ATOM   7261 C CA  . GLU   D 1 256 ? -23.066 -9.653  39.730  1.00 28.23 ? 235 GLU   D CA  1 
ATOM   7262 C C   . GLU   D 1 256 ? -21.740 -8.952  39.433  1.00 25.33 ? 235 GLU   D C   1 
ATOM   7263 O O   . GLU   D 1 256 ? -21.585 -7.750  39.679  1.00 24.70 ? 235 GLU   D O   1 
ATOM   7264 C CB  . GLU   D 1 256 ? -23.092 -10.249 41.146  1.00 29.81 ? 235 GLU   D CB  1 
ATOM   7265 C CG  . GLU   D 1 256 ? -24.494 -10.708 41.544  1.00 35.24 ? 235 GLU   D CG  1 
ATOM   7266 C CD  . GLU   D 1 256 ? -25.032 -11.961 40.863  1.00 45.33 ? 235 GLU   D CD  1 
ATOM   7267 O OE1 . GLU   D 1 256 ? -24.258 -12.807 40.320  1.00 41.34 ? 235 GLU   D OE1 1 
ATOM   7268 O OE2 . GLU   D 1 256 ? -26.286 -12.064 40.860  1.00 49.88 ? 235 GLU   D OE2 1 
ATOM   7269 N N   . GLN   D 1 257 ? -20.785 -9.719  38.912  1.00 22.85 ? 236 GLN   D N   1 
ATOM   7270 C CA  . GLN   D 1 257 ? -19.489 -9.153  38.532  1.00 25.17 ? 236 GLN   D CA  1 
ATOM   7271 C C   . GLN   D 1 257 ? -19.657 -8.100  37.428  1.00 23.81 ? 236 GLN   D C   1 
ATOM   7272 O O   . GLN   D 1 257 ? -19.026 -7.036  37.479  1.00 25.32 ? 236 GLN   D O   1 
ATOM   7273 C CB  . GLN   D 1 257 ? -18.524 -10.271 38.152  1.00 25.75 ? 236 GLN   D CB  1 
ATOM   7274 C CG  . GLN   D 1 257 ? -17.989 -11.019 39.374  1.00 30.08 ? 236 GLN   D CG  1 
ATOM   7275 C CD  . GLN   D 1 257 ? -17.181 -12.252 39.026  1.00 26.65 ? 236 GLN   D CD  1 
ATOM   7276 O OE1 . GLN   D 1 257 ? -17.423 -12.969 38.051  1.00 28.27 ? 236 GLN   D OE1 1 
ATOM   7277 N NE2 . GLN   D 1 257 ? -16.205 -12.511 39.872  1.00 29.32 ? 236 GLN   D NE2 1 
ATOM   7278 N N   . ILE   D 1 258 ? -20.530 -8.390  36.456  1.00 22.01 ? 237 ILE   D N   1 
ATOM   7279 C CA  . ILE   D 1 258 ? -20.866 -7.435  35.400  1.00 23.77 ? 237 ILE   D CA  1 
ATOM   7280 C C   . ILE   D 1 258 ? -21.511 -6.199  36.030  1.00 23.52 ? 237 ILE   D C   1 
ATOM   7281 O O   . ILE   D 1 258 ? -21.125 -5.048  35.748  1.00 20.40 ? 237 ILE   D O   1 
ATOM   7282 C CB  . ILE   D 1 258 ? -21.732 -8.054  34.273  1.00 22.84 ? 237 ILE   D CB  1 
ATOM   7283 C CG1 . ILE   D 1 258 ? -21.093 -9.265  33.582  1.00 23.91 ? 237 ILE   D CG1 1 
ATOM   7284 C CG2 . ILE   D 1 258 ? -22.144 -6.997  33.244  1.00 25.78 ? 237 ILE   D CG2 1 
ATOM   7285 C CD1 . ILE   D 1 258 ? -19.635 -9.061  33.154  1.00 25.78 ? 237 ILE   D CD1 1 
ATOM   7286 N N   . ALA   D 1 259 ? -22.476 -6.457  36.923  1.00 21.22 ? 238 ALA   D N   1 
ATOM   7287 C CA  . ALA   D 1 259 ? -23.221 -5.400  37.579  1.00 23.23 ? 238 ALA   D CA  1 
ATOM   7288 C C   . ALA   D 1 259 ? -22.301 -4.480  38.370  1.00 23.89 ? 238 ALA   D C   1 
ATOM   7289 O O   . ALA   D 1 259 ? -22.562 -3.285  38.427  1.00 22.52 ? 238 ALA   D O   1 
ATOM   7290 C CB  . ALA   D 1 259 ? -24.310 -6.015  38.461  1.00 23.73 ? 238 ALA   D CB  1 
ATOM   7291 N N   . ASP   D 1 260 ? -21.273 -5.060  39.024  1.00 23.46 ? 239 ASP   D N   1 
ATOM   7292 C CA  . ASP   D 1 260 ? -20.307 -4.297  39.806  1.00 25.05 ? 239 ASP   D CA  1 
ATOM   7293 C C   . ASP   D 1 260 ? -19.689 -3.179  38.965  1.00 21.92 ? 239 ASP   D C   1 
ATOM   7294 O O   . ASP   D 1 260 ? -19.436 -2.080  39.462  1.00 21.03 ? 239 ASP   D O   1 
ATOM   7295 C CB  . ASP   D 1 260 ? -19.207 -5.196  40.371  1.00 25.70 ? 239 ASP   D CB  1 
ATOM   7296 C CG  . ASP   D 1 260 ? -19.569 -5.964  41.639  1.00 32.37 ? 239 ASP   D CG  1 
ATOM   7297 O OD1 . ASP   D 1 260 ? -20.460 -5.486  42.365  1.00 29.92 ? 239 ASP   D OD1 1 
ATOM   7298 O OD2 . ASP   D 1 260 ? -19.006 -7.073  41.844  1.00 32.02 ? 239 ASP   D OD2 1 
ATOM   7299 N N   . ALA   D 1 261 ? -19.386 -3.476  37.694  1.00 21.42 ? 240 ALA   D N   1 
ATOM   7300 C CA  . ALA   D 1 261 ? -18.760 -2.467  36.845  1.00 22.15 ? 240 ALA   D CA  1 
ATOM   7301 C C   . ALA   D 1 261 ? -19.759 -1.370  36.457  1.00 23.69 ? 240 ALA   D C   1 
ATOM   7302 O O   . ALA   D 1 261 ? -19.390 -0.203  36.334  1.00 22.05 ? 240 ALA   D O   1 
ATOM   7303 C CB  . ALA   D 1 261 ? -18.190 -3.133  35.598  1.00 21.65 ? 240 ALA   D CB  1 
ATOM   7304 N N   . VAL   D 1 262 ? -21.030 -1.740  36.230  1.00 23.81 ? 241 VAL   D N   1 
ATOM   7305 C CA  . VAL   D 1 262 ? -22.084 -0.748  35.995  1.00 24.36 ? 241 VAL   D CA  1 
ATOM   7306 C C   . VAL   D 1 262 ? -22.211 0.208   37.184  1.00 22.93 ? 241 VAL   D C   1 
ATOM   7307 O O   . VAL   D 1 262 ? -22.263 1.431   37.008  1.00 23.53 ? 241 VAL   D O   1 
ATOM   7308 C CB  . VAL   D 1 262 ? -23.429 -1.437  35.682  1.00 25.19 ? 241 VAL   D CB  1 
ATOM   7309 C CG1 . VAL   D 1 262 ? -24.554 -0.442  35.375  1.00 26.03 ? 241 VAL   D CG1 1 
ATOM   7310 C CG2 . VAL   D 1 262 ? -23.288 -2.453  34.560  1.00 25.12 ? 241 VAL   D CG2 1 
ATOM   7311 N N   . ILE   D 1 263 ? -22.250 -0.366  38.400  1.00 24.93 ? 242 ILE   D N   1 
ATOM   7312 C CA  . ILE   D 1 263 ? -22.374 0.378   39.644  1.00 24.21 ? 242 ILE   D CA  1 
ATOM   7313 C C   . ILE   D 1 263 ? -21.237 1.395   39.767  1.00 23.13 ? 242 ILE   D C   1 
ATOM   7314 O O   . ILE   D 1 263 ? -21.473 2.568   40.071  1.00 24.33 ? 242 ILE   D O   1 
ATOM   7315 C CB  . ILE   D 1 263 ? -22.446 -0.610  40.831  1.00 29.03 ? 242 ILE   D CB  1 
ATOM   7316 C CG1 . ILE   D 1 263 ? -23.762 -1.397  40.845  1.00 32.93 ? 242 ILE   D CG1 1 
ATOM   7317 C CG2 . ILE   D 1 263 ? -22.136 0.027   42.189  1.00 28.68 ? 242 ILE   D CG2 1 
ATOM   7318 C CD1 . ILE   D 1 263 ? -24.986 -0.590  40.456  1.00 32.48 ? 242 ILE   D CD1 1 
ATOM   7319 N N   . PHE   D 1 264 ? -20.000 0.933   39.491  1.00 21.28 ? 243 PHE   D N   1 
ATOM   7320 C CA  . PHE   D 1 264 ? -18.850 1.821   39.475  1.00 21.43 ? 243 PHE   D CA  1 
ATOM   7321 C C   . PHE   D 1 264 ? -19.128 3.022   38.563  1.00 22.54 ? 243 PHE   D C   1 
ATOM   7322 O O   . PHE   D 1 264 ? -18.973 4.178   38.992  1.00 22.15 ? 243 PHE   D O   1 
ATOM   7323 C CB  . PHE   D 1 264 ? -17.548 1.079   39.112  1.00 20.23 ? 243 PHE   D CB  1 
ATOM   7324 C CG  . PHE   D 1 264 ? -16.419 2.073   38.888  1.00 22.67 ? 243 PHE   D CG  1 
ATOM   7325 C CD1 . PHE   D 1 264 ? -15.918 2.843   39.949  1.00 22.70 ? 243 PHE   D CD1 1 
ATOM   7326 C CD2 . PHE   D 1 264 ? -15.862 2.239   37.627  1.00 21.61 ? 243 PHE   D CD2 1 
ATOM   7327 C CE1 . PHE   D 1 264 ? -14.894 3.766   39.734  1.00 21.06 ? 243 PHE   D CE1 1 
ATOM   7328 C CE2 . PHE   D 1 264 ? -14.833 3.171   37.415  1.00 21.68 ? 243 PHE   D CE2 1 
ATOM   7329 C CZ  . PHE   D 1 264 ? -14.347 3.922   38.470  1.00 21.48 ? 243 PHE   D CZ  1 
ATOM   7330 N N   . LEU   D 1 265 ? -19.468 2.752   37.286  1.00 22.32 ? 244 LEU   D N   1 
ATOM   7331 C CA  . LEU   D 1 265 ? -19.617 3.816   36.286  1.00 21.51 ? 244 LEU   D CA  1 
ATOM   7332 C C   . LEU   D 1 265 ? -20.744 4.799   36.604  1.00 21.86 ? 244 LEU   D C   1 
ATOM   7333 O O   . LEU   D 1 265 ? -20.666 5.974   36.210  1.00 23.65 ? 244 LEU   D O   1 
ATOM   7334 C CB  . LEU   D 1 265 ? -19.778 3.318   34.851  1.00 22.77 ? 244 LEU   D CB  1 
ATOM   7335 C CG  . LEU   D 1 265 ? -18.537 2.593   34.306  1.00 22.57 ? 244 LEU   D CG  1 
ATOM   7336 C CD1 . LEU   D 1 265 ? -18.939 1.653   33.174  1.00 20.15 ? 244 LEU   D CD1 1 
ATOM   7337 C CD2 . LEU   D 1 265 ? -17.627 3.689   33.802  1.00 20.85 ? 244 LEU   D CD2 1 
ATOM   7338 N N   . VAL   D 1 266 ? -21.783 4.352   37.311  1.00 21.57 ? 245 VAL   D N   1 
ATOM   7339 C CA  . VAL   D 1 266 ? -22.819 5.349   37.618  1.00 24.00 ? 245 VAL   D CA  1 
ATOM   7340 C C   . VAL   D 1 266 ? -22.505 6.104   38.911  1.00 25.13 ? 245 VAL   D C   1 
ATOM   7341 O O   . VAL   D 1 266 ? -23.140 7.142   39.157  1.00 26.71 ? 245 VAL   D O   1 
ATOM   7342 C CB  . VAL   D 1 266 ? -24.257 4.795   37.668  1.00 26.56 ? 245 VAL   D CB  1 
ATOM   7343 C CG1 . VAL   D 1 266 ? -24.579 3.975   36.429  1.00 26.92 ? 245 VAL   D CG1 1 
ATOM   7344 C CG2 . VAL   D 1 266 ? -24.445 3.936   38.903  1.00 29.47 ? 245 VAL   D CG2 1 
ATOM   7345 N N   . SER   D 1 267 ? -21.524 5.614   39.701  1.00 24.23 ? 246 SER   D N   1 
ATOM   7346 C CA  . SER   D 1 267 ? -21.203 6.109   41.047  1.00 24.84 ? 246 SER   D CA  1 
ATOM   7347 C C   . SER   D 1 267 ? -20.491 7.458   40.972  1.00 25.97 ? 246 SER   D C   1 
ATOM   7348 O O   . SER   D 1 267 ? -19.989 7.833   39.907  1.00 26.28 ? 246 SER   D O   1 
ATOM   7349 C CB  . SER   D 1 267 ? -20.296 5.119   41.799  1.00 27.69 ? 246 SER   D CB  1 
ATOM   7350 O OG  . SER   D 1 267 ? -18.931 5.287   41.391  1.00 24.43 ? 246 SER   D OG  1 
ATOM   7351 N N   . GLY   D 1 268 ? -20.346 8.116   42.142  1.00 29.77 ? 247 GLY   D N   1 
ATOM   7352 C CA  . GLY   D 1 268 ? -19.552 9.333   42.302  1.00 29.89 ? 247 GLY   D CA  1 
ATOM   7353 C C   . GLY   D 1 268 ? -18.037 9.098   42.168  1.00 28.17 ? 247 GLY   D C   1 
ATOM   7354 O O   . GLY   D 1 268 ? -17.272 10.043  42.054  1.00 31.92 ? 247 GLY   D O   1 
ATOM   7355 N N   . SER   D 1 269 ? -17.598 7.840   42.119  1.00 26.24 ? 248 SER   D N   1 
ATOM   7356 C CA  . SER   D 1 269 ? -16.180 7.536   41.935  1.00 27.45 ? 248 SER   D CA  1 
ATOM   7357 C C   . SER   D 1 269 ? -15.786 7.550   40.453  1.00 26.66 ? 248 SER   D C   1 
ATOM   7358 O O   . SER   D 1 269 ? -14.597 7.370   40.131  1.00 26.12 ? 248 SER   D O   1 
ATOM   7359 C CB  . SER   D 1 269 ? -15.847 6.211   42.540  1.00 28.87 ? 248 SER   D CB  1 
ATOM   7360 O OG  . SER   D 1 269 ? -16.167 6.248   43.916  1.00 36.07 ? 248 SER   D OG  1 
ATOM   7361 N N   . ALA   D 1 270 ? -16.777 7.753   39.566  1.00 23.60 ? 249 ALA   D N   1 
ATOM   7362 C CA  . ALA   D 1 270 ? -16.569 7.770   38.117  1.00 25.62 ? 249 ALA   D CA  1 
ATOM   7363 C C   . ALA   D 1 270 ? -16.907 9.121   37.475  1.00 24.84 ? 249 ALA   D C   1 
ATOM   7364 O O   . ALA   D 1 270 ? -17.161 9.199   36.283  1.00 21.99 ? 249 ALA   D O   1 
ATOM   7365 C CB  . ALA   D 1 270 ? -17.351 6.625   37.459  1.00 22.51 ? 249 ALA   D CB  1 
ATOM   7366 N N   . GLN   D 1 271 ? -16.852 10.222  38.230  1.00 27.09 ? 250 GLN   D N   1 
ATOM   7367 C CA  . GLN   D 1 271 ? -17.469 11.473  37.786  1.00 26.57 ? 250 GLN   D CA  1 
ATOM   7368 C C   . GLN   D 1 271 ? -16.710 12.169  36.657  1.00 26.30 ? 250 GLN   D C   1 
ATOM   7369 O O   . GLN   D 1 271 ? -17.216 13.148  36.073  1.00 23.00 ? 250 GLN   D O   1 
ATOM   7370 C CB  . GLN   D 1 271 ? -17.525 12.467  38.959  1.00 28.32 ? 250 GLN   D CB  1 
ATOM   7371 C CG  . GLN   D 1 271 ? -18.526 12.077  40.035  0.60 32.18 ? 250 GLN   D CG  1 
ATOM   7372 C CD  . GLN   D 1 271 ? -19.904 12.651  39.816  0.60 34.91 ? 250 GLN   D CD  1 
ATOM   7373 O OE1 . GLN   D 1 271 ? -20.409 13.445  40.617  0.60 37.79 ? 250 GLN   D OE1 1 
ATOM   7374 N NE2 . GLN   D 1 271 ? -20.521 12.262  38.714  0.60 40.10 ? 250 GLN   D NE2 1 
ATOM   7375 N N   . TYR   D 1 272 ? -15.459 11.750  36.404  1.00 22.33 ? 251 TYR   D N   1 
ATOM   7376 C CA  . TYR   D 1 272 ? -14.744 12.304  35.269  1.00 23.23 ? 251 TYR   D CA  1 
ATOM   7377 C C   . TYR   D 1 272 ? -14.695 11.269  34.135  1.00 22.31 ? 251 TYR   D C   1 
ATOM   7378 O O   . TYR   D 1 272 ? -14.033 11.495  33.123  1.00 23.01 ? 251 TYR   D O   1 
ATOM   7379 C CB  . TYR   D 1 272 ? -13.348 12.739  35.740  1.00 22.78 ? 251 TYR   D CB  1 
ATOM   7380 C CG  . TYR   D 1 272 ? -12.588 13.710  34.858  1.00 22.32 ? 251 TYR   D CG  1 
ATOM   7381 C CD1 . TYR   D 1 272 ? -12.944 15.053  34.819  1.00 21.67 ? 251 TYR   D CD1 1 
ATOM   7382 C CD2 . TYR   D 1 272 ? -11.495 13.304  34.080  1.00 20.00 ? 251 TYR   D CD2 1 
ATOM   7383 C CE1 . TYR   D 1 272 ? -12.249 15.957  34.031  1.00 20.09 ? 251 TYR   D CE1 1 
ATOM   7384 C CE2 . TYR   D 1 272 ? -10.793 14.211  33.299  1.00 20.37 ? 251 TYR   D CE2 1 
ATOM   7385 C CZ  . TYR   D 1 272 ? -11.164 15.549  33.277  1.00 21.47 ? 251 TYR   D CZ  1 
ATOM   7386 O OH  . TYR   D 1 272 ? -10.463 16.447  32.508  1.00 20.79 ? 251 TYR   D OH  1 
ATOM   7387 N N   . ILE   D 1 273 ? -15.352 10.119  34.318  1.00 21.34 ? 252 ILE   D N   1 
ATOM   7388 C CA  . ILE   D 1 273 ? -15.260 9.072   33.302  1.00 21.36 ? 252 ILE   D CA  1 
ATOM   7389 C C   . ILE   D 1 273 ? -16.414 9.230   32.310  1.00 21.85 ? 252 ILE   D C   1 
ATOM   7390 O O   . ILE   D 1 273 ? -17.572 9.131   32.694  1.00 21.50 ? 252 ILE   D O   1 
ATOM   7391 C CB  . ILE   D 1 273 ? -15.266 7.685   33.949  1.00 22.59 ? 252 ILE   D CB  1 
ATOM   7392 C CG1 . ILE   D 1 273 ? -14.046 7.553   34.904  1.00 23.30 ? 252 ILE   D CG1 1 
ATOM   7393 C CG2 . ILE   D 1 273 ? -15.313 6.582   32.880  1.00 21.26 ? 252 ILE   D CG2 1 
ATOM   7394 C CD1 . ILE   D 1 273 ? -13.982 6.236   35.659  1.00 20.43 ? 252 ILE   D CD1 1 
ATOM   7395 N N   . THR   D 1 274 ? -16.095 9.471   31.035  1.00 20.75 ? 253 THR   D N   1 
ATOM   7396 C CA  . THR   D 1 274 ? -17.134 9.409   29.999  1.00 21.48 ? 253 THR   D CA  1 
ATOM   7397 C C   . THR   D 1 274 ? -16.486 8.962   28.692  1.00 21.32 ? 253 THR   D C   1 
ATOM   7398 O O   . THR   D 1 274 ? -15.323 9.315   28.422  1.00 20.06 ? 253 THR   D O   1 
ATOM   7399 C CB  . THR   D 1 274 ? -17.862 10.762  29.897  1.00 20.19 ? 253 THR   D CB  1 
ATOM   7400 O OG1 . THR   D 1 274 ? -19.031 10.562  29.116  1.00 21.52 ? 253 THR   D OG1 1 
ATOM   7401 C CG2 . THR   D 1 274 ? -17.018 11.882  29.300  1.00 20.06 ? 253 THR   D CG2 1 
ATOM   7402 N N   . GLY   D 1 275 ? -17.225 8.159   27.902  1.00 20.46 ? 254 GLY   D N   1 
ATOM   7403 C CA  . GLY   D 1 275 ? -16.703 7.664   26.648  1.00 18.94 ? 254 GLY   D CA  1 
ATOM   7404 C C   . GLY   D 1 275 ? -15.809 6.433   26.851  1.00 23.01 ? 254 GLY   D C   1 
ATOM   7405 O O   . GLY   D 1 275 ? -15.066 6.054   25.950  1.00 24.44 ? 254 GLY   D O   1 
ATOM   7406 N N   . SER   D 1 276 ? -15.799 5.866   28.065  1.00 23.07 ? 255 SER   D N   1 
ATOM   7407 C CA  . SER   D 1 276 ? -14.926 4.744   28.372  1.00 22.45 ? 255 SER   D CA  1 
ATOM   7408 C C   . SER   D 1 276 ? -15.763 3.474   28.285  1.00 23.84 ? 255 SER   D C   1 
ATOM   7409 O O   . SER   D 1 276 ? -16.930 3.511   28.661  1.00 22.92 ? 255 SER   D O   1 
ATOM   7410 C CB  . SER   D 1 276 ? -14.299 4.886   29.785  1.00 19.51 ? 255 SER   D CB  1 
ATOM   7411 O OG  . SER   D 1 276 ? -13.497 6.067   29.808  1.00 24.59 ? 255 SER   D OG  1 
ATOM   7412 N N   . ILE   D 1 277 ? -15.139 2.369   27.843  1.00 22.39 ? 256 ILE   D N   1 
ATOM   7413 C CA  . ILE   D 1 277 ? -15.736 1.048   27.849  1.00 22.02 ? 256 ILE   D CA  1 
ATOM   7414 C C   . ILE   D 1 277 ? -14.841 0.135   28.685  1.00 24.38 ? 256 ILE   D C   1 
ATOM   7415 O O   . ILE   D 1 277 ? -13.666 -0.054  28.360  1.00 24.93 ? 256 ILE   D O   1 
ATOM   7416 C CB  . ILE   D 1 277 ? -15.947 0.550   26.401  1.00 23.83 ? 256 ILE   D CB  1 
ATOM   7417 C CG1 . ILE   D 1 277 ? -16.974 1.439   25.697  1.00 25.00 ? 256 ILE   D CG1 1 
ATOM   7418 C CG2 . ILE   D 1 277 ? -16.372 -0.933  26.369  1.00 22.36 ? 256 ILE   D CG2 1 
ATOM   7419 C CD1 . ILE   D 1 277 ? -16.961 1.306   24.189  1.00 31.18 ? 256 ILE   D CD1 1 
ATOM   7420 N N   . ILE   D 1 278 ? -15.391 -0.388  29.793  1.00 20.31 ? 257 ILE   D N   1 
ATOM   7421 C CA  . ILE   D 1 278 ? -14.606 -1.232  30.680  1.00 21.34 ? 257 ILE   D CA  1 
ATOM   7422 C C   . ILE   D 1 278 ? -14.869 -2.679  30.301  1.00 20.01 ? 257 ILE   D C   1 
ATOM   7423 O O   . ILE   D 1 278 ? -15.996 -3.125  30.504  1.00 19.61 ? 257 ILE   D O   1 
ATOM   7424 C CB  . ILE   D 1 278 ? -14.998 -1.014  32.166  1.00 21.92 ? 257 ILE   D CB  1 
ATOM   7425 C CG1 . ILE   D 1 278 ? -14.857 0.454   32.583  1.00 20.64 ? 257 ILE   D CG1 1 
ATOM   7426 C CG2 . ILE   D 1 278 ? -14.142 -1.927  33.057  1.00 23.76 ? 257 ILE   D CG2 1 
ATOM   7427 C CD1 . ILE   D 1 278 ? -15.222 0.745   34.028  1.00 23.10 ? 257 ILE   D CD1 1 
ATOM   7428 N N   . LYS   D 1 279 ? -13.828 -3.422  29.871  1.00 19.13 ? 258 LYS   D N   1 
ATOM   7429 C CA  . LYS   D 1 279 ? -13.989 -4.853  29.631  1.00 20.47 ? 258 LYS   D CA  1 
ATOM   7430 C C   . LYS   D 1 279 ? -14.030 -5.563  30.976  1.00 22.24 ? 258 LYS   D C   1 
ATOM   7431 O O   . LYS   D 1 279 ? -13.282 -5.208  31.875  1.00 22.35 ? 258 LYS   D O   1 
ATOM   7432 C CB  . LYS   D 1 279 ? -12.821 -5.589  28.955  1.00 21.91 ? 258 LYS   D CB  1 
ATOM   7433 C CG  . LYS   D 1 279 ? -12.477 -5.076  27.574  1.00 26.31 ? 258 LYS   D CG  1 
ATOM   7434 C CD  . LYS   D 1 279 ? -11.249 -5.762  26.950  1.00 26.33 ? 258 LYS   D CD  1 
ATOM   7435 C CE  . LYS   D 1 279 ? -9.930  -5.428  27.604  1.00 28.68 ? 258 LYS   D CE  1 
ATOM   7436 N NZ  . LYS   D 1 279 ? -8.795  -6.217  27.077  1.00 28.22 ? 258 LYS   D NZ  1 
ATOM   7437 N N   . VAL   D 1 280 ? -14.928 -6.544  31.086  1.00 21.99 ? 259 VAL   D N   1 
ATOM   7438 C CA  . VAL   D 1 280 ? -15.079 -7.375  32.258  1.00 21.18 ? 259 VAL   D CA  1 
ATOM   7439 C C   . VAL   D 1 280 ? -15.083 -8.820  31.737  1.00 21.31 ? 259 VAL   D C   1 
ATOM   7440 O O   . VAL   D 1 280 ? -16.131 -9.447  31.668  1.00 23.57 ? 259 VAL   D O   1 
ATOM   7441 C CB  . VAL   D 1 280 ? -16.331 -7.011  33.098  1.00 23.30 ? 259 VAL   D CB  1 
ATOM   7442 C CG1 . VAL   D 1 280 ? -16.432 -7.857  34.372  1.00 22.72 ? 259 VAL   D CG1 1 
ATOM   7443 C CG2 . VAL   D 1 280 ? -16.330 -5.531  33.501  1.00 20.71 ? 259 VAL   D CG2 1 
ATOM   7444 N N   . ASP   D 1 281 ? -13.896 -9.348  31.406  1.00 21.87 ? 260 ASP   D N   1 
ATOM   7445 C CA  . ASP   D 1 281 ? -13.800 -10.529 30.550  1.00 22.11 ? 260 ASP   D CA  1 
ATOM   7446 C C   . ASP   D 1 281 ? -12.745 -11.527 31.018  1.00 20.98 ? 260 ASP   D C   1 
ATOM   7447 O O   . ASP   D 1 281 ? -12.506 -12.517 30.320  1.00 20.93 ? 260 ASP   D O   1 
ATOM   7448 C CB  . ASP   D 1 281 ? -13.527 -10.140 29.098  1.00 21.98 ? 260 ASP   D CB  1 
ATOM   7449 C CG  . ASP   D 1 281 ? -12.097 -9.723  28.741  1.00 24.75 ? 260 ASP   D CG  1 
ATOM   7450 O OD1 . ASP   D 1 281 ? -11.261 -9.469  29.648  1.00 22.82 ? 260 ASP   D OD1 1 
ATOM   7451 O OD2 . ASP   D 1 281 ? -11.806 -9.706  27.538  1.00 23.41 ? 260 ASP   D OD2 1 
ATOM   7452 N N   . GLY   D 1 282 ? -12.137 -11.290 32.196  1.00 21.78 ? 261 GLY   D N   1 
ATOM   7453 C CA  . GLY   D 1 282 ? -11.193 -12.241 32.762  1.00 21.13 ? 261 GLY   D CA  1 
ATOM   7454 C C   . GLY   D 1 282 ? -10.032 -12.531 31.812  1.00 23.21 ? 261 GLY   D C   1 
ATOM   7455 O O   . GLY   D 1 282 ? -9.380  -13.593 31.914  1.00 20.52 ? 261 GLY   D O   1 
ATOM   7456 N N   . GLY   D 1 283 ? -9.762  -11.564 30.908  1.00 21.36 ? 262 GLY   D N   1 
ATOM   7457 C CA  . GLY   D 1 283 ? -8.649  -11.675 29.967  1.00 21.23 ? 262 GLY   D CA  1 
ATOM   7458 C C   . GLY   D 1 283 ? -8.980  -12.428 28.667  1.00 20.89 ? 262 GLY   D C   1 
ATOM   7459 O O   . GLY   D 1 283 ? -8.080  -12.690 27.847  1.00 22.60 ? 262 GLY   D O   1 
ATOM   7460 N N   . LEU   D 1 284 ? -10.244 -12.811 28.482  1.00 22.35 ? 263 LEU   D N   1 
ATOM   7461 C CA  . LEU   D 1 284 ? -10.674 -13.613 27.328  1.00 24.39 ? 263 LEU   D CA  1 
ATOM   7462 C C   . LEU   D 1 284 ? -10.220 -12.979 26.006  1.00 20.94 ? 263 LEU   D C   1 
ATOM   7463 O O   . LEU   D 1 284 ? -9.731  -13.670 25.120  1.00 22.41 ? 263 LEU   D O   1 
ATOM   7464 C CB  . LEU   D 1 284 ? -12.194 -13.785 27.288  1.00 24.16 ? 263 LEU   D CB  1 
ATOM   7465 C CG  . LEU   D 1 284 ? -12.733 -14.595 26.103  1.00 26.72 ? 263 LEU   D CG  1 
ATOM   7466 C CD1 . LEU   D 1 284 ? -12.156 -16.024 26.152  1.00 25.98 ? 263 LEU   D CD1 1 
ATOM   7467 C CD2 . LEU   D 1 284 ? -14.274 -14.664 26.160  1.00 27.53 ? 263 LEU   D CD2 1 
ATOM   7468 N N   . SER   D 1 285 ? -10.380 -11.659 25.868  1.00 23.19 ? 264 SER   D N   1 
ATOM   7469 C CA  . SER   D 1 285 ? -10.119 -11.000 24.597  1.00 21.78 ? 264 SER   D CA  1 
ATOM   7470 C C   . SER   D 1 285 ? -8.615  -10.966 24.289  1.00 24.28 ? 264 SER   D C   1 
ATOM   7471 O O   . SER   D 1 285 ? -8.237  -10.600 23.167  1.00 24.30 ? 264 SER   D O   1 
ATOM   7472 C CB  . SER   D 1 285 ? -10.694 -9.608  24.616  1.00 22.81 ? 264 SER   D CB  1 
ATOM   7473 O OG  . SER   D 1 285 ? -10.083 -8.901  25.684  1.00 23.17 ? 264 SER   D OG  1 
ATOM   7474 N N   . LEU   D 1 286 ? -7.770  -11.331 25.272  1.00 20.32 ? 265 LEU   D N   1 
ATOM   7475 C CA  . LEU   D 1 286 ? -6.305  -11.301 25.105  1.00 21.34 ? 265 LEU   D CA  1 
ATOM   7476 C C   . LEU   D 1 286 ? -5.765  -12.598 24.501  1.00 21.26 ? 265 LEU   D C   1 
ATOM   7477 O O   . LEU   D 1 286 ? -4.553  -12.698 24.232  1.00 23.41 ? 265 LEU   D O   1 
ATOM   7478 C CB  . LEU   D 1 286 ? -5.618  -11.040 26.454  1.00 21.68 ? 265 LEU   D CB  1 
ATOM   7479 C CG  . LEU   D 1 286 ? -6.014  -9.713  27.110  1.00 26.67 ? 265 LEU   D CG  1 
ATOM   7480 C CD1 . LEU   D 1 286 ? -5.303  -9.566  28.450  1.00 30.46 ? 265 LEU   D CD1 1 
ATOM   7481 C CD2 . LEU   D 1 286 ? -5.813  -8.550  26.159  1.00 28.19 ? 265 LEU   D CD2 1 
ATOM   7482 N N   . VAL   D 1 287 ? -6.629  -13.622 24.432  1.00 20.58 ? 266 VAL   D N   1 
ATOM   7483 C CA  . VAL   D 1 287 ? -6.240  -14.984 24.055  1.00 22.28 ? 266 VAL   D CA  1 
ATOM   7484 C C   . VAL   D 1 287 ? -6.226  -15.123 22.524  1.00 25.19 ? 266 VAL   D C   1 
ATOM   7485 O O   . VAL   D 1 287 ? -7.256  -14.926 21.886  1.00 24.95 ? 266 VAL   D O   1 
ATOM   7486 C CB  . VAL   D 1 287 ? -7.177  -16.029 24.693  1.00 23.45 ? 266 VAL   D CB  1 
ATOM   7487 C CG1 . VAL   D 1 287 ? -6.691  -17.457 24.441  1.00 24.87 ? 266 VAL   D CG1 1 
ATOM   7488 C CG2 . VAL   D 1 287 ? -7.243  -15.820 26.214  1.00 26.67 ? 266 VAL   D CG2 1 
ATOM   7489 N N   . HIS   D 1 288 ? -5.066  -15.486 21.941  1.00 27.17 ? 267 HIS   D N   1 
ATOM   7490 C CA  . HIS   D 1 288 ? -4.985  -15.683 20.493  1.00 29.66 ? 267 HIS   D CA  1 
ATOM   7491 C C   . HIS   D 1 288 ? -5.573  -17.040 20.113  1.00 31.85 ? 267 HIS   D C   1 
ATOM   7492 O O   . HIS   D 1 288 ? -5.754  -17.896 20.979  1.00 29.66 ? 267 HIS   D O   1 
ATOM   7493 C CB  . HIS   D 1 288 ? -3.551  -15.561 19.964  1.00 32.80 ? 267 HIS   D CB  1 
ATOM   7494 C CG  . HIS   D 1 288 ? -2.636  -16.637 20.457  1.00 33.97 ? 267 HIS   D CG  1 
ATOM   7495 N ND1 . HIS   D 1 288 ? -2.819  -17.975 20.162  1.00 31.84 ? 267 HIS   D ND1 1 
ATOM   7496 C CD2 . HIS   D 1 288 ? -1.555  -16.567 21.251  1.00 34.26 ? 267 HIS   D CD2 1 
ATOM   7497 C CE1 . HIS   D 1 288 ? -1.853  -18.681 20.736  1.00 37.05 ? 267 HIS   D CE1 1 
ATOM   7498 N NE2 . HIS   D 1 288 ? -1.078  -17.846 21.428  1.00 38.13 ? 267 HIS   D NE2 1 
ATOM   7499 N N   . ALA   D 1 289 ? -5.845  -17.222 18.812  1.00 31.72 ? 268 ALA   D N   1 
ATOM   7500 C CA  . ALA   D 1 289 ? -6.458  -18.444 18.304  1.00 35.29 ? 268 ALA   D CA  1 
ATOM   7501 C C   . ALA   D 1 289 ? -5.616  -19.667 18.670  1.00 36.03 ? 268 ALA   D C   1 
ATOM   7502 O O   . ALA   D 1 289 ? -6.234  -20.745 18.783  1.00 43.71 ? 268 ALA   D O   1 
ATOM   7503 C CB  . ALA   D 1 289 ? -6.635  -18.361 16.802  1.00 40.76 ? 268 ALA   D CB  1 
ATOM   7504 O OXT . ALA   D 1 289 ? -4.390  -19.513 18.819  1.00 32.97 ? 268 ALA   D OXT 1 
HETATM 7505 P PA  . NDP   E 2 .   ? 13.645  -12.693 11.896  0.90 29.42 ? 301 NDP   A PA  1 
HETATM 7506 O O1A . NDP   E 2 .   ? 14.128  -13.622 10.843  0.90 28.55 ? 301 NDP   A O1A 1 
HETATM 7507 O O2A . NDP   E 2 .   ? 13.211  -13.288 13.179  0.90 29.04 ? 301 NDP   A O2A 1 
HETATM 7508 O O5B . NDP   E 2 .   ? 14.724  -11.525 12.159  0.90 29.71 ? 301 NDP   A O5B 1 
HETATM 7509 C C5B . NDP   E 2 .   ? 15.175  -10.617 11.128  0.90 28.25 ? 301 NDP   A C5B 1 
HETATM 7510 C C4B . NDP   E 2 .   ? 16.607  -10.229 11.422  0.90 26.99 ? 301 NDP   A C4B 1 
HETATM 7511 O O4B . NDP   E 2 .   ? 16.670  -9.497  12.663  0.90 27.35 ? 301 NDP   A O4B 1 
HETATM 7512 C C3B . NDP   E 2 .   ? 17.611  -11.361 11.724  0.90 30.18 ? 301 NDP   A C3B 1 
HETATM 7513 O O3B . NDP   E 2 .   ? 18.057  -12.008 10.544  0.90 32.03 ? 301 NDP   A O3B 1 
HETATM 7514 C C2B . NDP   E 2 .   ? 18.744  -10.616 12.440  0.90 28.33 ? 301 NDP   A C2B 1 
HETATM 7515 O O2B . NDP   E 2 .   ? 19.875  -10.274 11.607  0.90 26.24 ? 301 NDP   A O2B 1 
HETATM 7516 C C1B . NDP   E 2 .   ? 18.037  -9.336  12.921  0.90 26.74 ? 301 NDP   A C1B 1 
HETATM 7517 N N9A . NDP   E 2 .   ? 18.322  -9.109  14.327  0.90 25.28 ? 301 NDP   A N9A 1 
HETATM 7518 C C8A . NDP   E 2 .   ? 17.997  -9.909  15.401  0.90 24.68 ? 301 NDP   A C8A 1 
HETATM 7519 N N7A . NDP   E 2 .   ? 18.583  -9.529  16.508  0.90 24.39 ? 301 NDP   A N7A 1 
HETATM 7520 C C5A . NDP   E 2 .   ? 19.352  -8.422  16.137  0.90 25.03 ? 301 NDP   A C5A 1 
HETATM 7521 C C6A . NDP   E 2 .   ? 20.239  -7.580  16.850  0.90 25.70 ? 301 NDP   A C6A 1 
HETATM 7522 N N6A . NDP   E 2 .   ? 20.472  -7.691  18.159  0.90 23.92 ? 301 NDP   A N6A 1 
HETATM 7523 N N1A . NDP   E 2 .   ? 20.878  -6.599  16.157  0.90 25.40 ? 301 NDP   A N1A 1 
HETATM 7524 C C2A . NDP   E 2 .   ? 20.629  -6.466  14.844  0.90 24.27 ? 301 NDP   A C2A 1 
HETATM 7525 N N3A . NDP   E 2 .   ? 19.838  -7.211  14.066  0.90 24.67 ? 301 NDP   A N3A 1 
HETATM 7526 C C4A . NDP   E 2 .   ? 19.237  -8.189  14.779  0.90 26.34 ? 301 NDP   A C4A 1 
HETATM 7527 O O3  . NDP   E 2 .   ? 12.425  -11.828 11.299  0.90 29.27 ? 301 NDP   A O3  1 
HETATM 7528 P PN  . NDP   E 2 .   ? 11.310  -12.224 10.206  0.90 27.49 ? 301 NDP   A PN  1 
HETATM 7529 O O1N . NDP   E 2 .   ? 10.681  -13.530 10.576  0.90 26.30 ? 301 NDP   A O1N 1 
HETATM 7530 O O2N . NDP   E 2 .   ? 11.963  -12.150 8.857   0.90 26.55 ? 301 NDP   A O2N 1 
HETATM 7531 O O5D . NDP   E 2 .   ? 10.235  -11.035 10.401  0.90 24.64 ? 301 NDP   A O5D 1 
HETATM 7532 C C5D . NDP   E 2 .   ? 10.478  -9.745  9.833   0.90 22.53 ? 301 NDP   A C5D 1 
HETATM 7533 C C4D . NDP   E 2 .   ? 9.745   -8.701  10.643  0.90 21.41 ? 301 NDP   A C4D 1 
HETATM 7534 O O4D . NDP   E 2 .   ? 8.336   -9.038  10.660  0.90 23.46 ? 301 NDP   A O4D 1 
HETATM 7535 C C3D . NDP   E 2 .   ? 10.180  -8.596  12.121  0.90 22.64 ? 301 NDP   A C3D 1 
HETATM 7536 O O3D . NDP   E 2 .   ? 10.299  -7.256  12.565  0.90 21.11 ? 301 NDP   A O3D 1 
HETATM 7537 C C2D . NDP   E 2 .   ? 9.099   -9.409  12.838  0.90 24.60 ? 301 NDP   A C2D 1 
HETATM 7538 O O2D . NDP   E 2 .   ? 8.944   -9.084  14.216  0.90 23.93 ? 301 NDP   A O2D 1 
HETATM 7539 C C1D . NDP   E 2 .   ? 7.869   -9.094  11.985  0.90 24.63 ? 301 NDP   A C1D 1 
HETATM 7540 N N1N . NDP   E 2 .   ? 6.896   -10.202 12.078  0.90 25.30 ? 301 NDP   A N1N 1 
HETATM 7541 C C2N . NDP   E 2 .   ? 7.186   -11.416 11.515  0.90 23.39 ? 301 NDP   A C2N 1 
HETATM 7542 C C3N . NDP   E 2 .   ? 6.354   -12.482 11.654  0.90 24.91 ? 301 NDP   A C3N 1 
HETATM 7543 C C7N . NDP   E 2 .   ? 6.666   -13.778 11.011  0.90 27.48 ? 301 NDP   A C7N 1 
HETATM 7544 O O7N . NDP   E 2 .   ? 5.806   -14.671 11.061  0.90 28.96 ? 301 NDP   A O7N 1 
HETATM 7545 N N7N . NDP   E 2 .   ? 7.843   -13.988 10.424  0.90 27.13 ? 301 NDP   A N7N 1 
HETATM 7546 C C4N . NDP   E 2 .   ? 5.164   -12.328 12.508  0.90 25.73 ? 301 NDP   A C4N 1 
HETATM 7547 C C5N . NDP   E 2 .   ? 4.936   -11.001 13.065  0.90 26.21 ? 301 NDP   A C5N 1 
HETATM 7548 C C6N . NDP   E 2 .   ? 5.732   -9.997  12.790  0.90 25.19 ? 301 NDP   A C6N 1 
HETATM 7549 P P2B . NDP   E 2 .   ? 21.075  -11.368 11.430  0.90 28.15 ? 301 NDP   A P2B 1 
HETATM 7550 O O1X . NDP   E 2 .   ? 21.996  -10.642 10.438  0.90 26.63 ? 301 NDP   A O1X 1 
HETATM 7551 O O2X . NDP   E 2 .   ? 21.728  -11.537 12.783  0.90 25.34 ? 301 NDP   A O2X 1 
HETATM 7552 O O3X . NDP   E 2 .   ? 20.497  -12.638 10.878  0.90 23.46 ? 301 NDP   A O3X 1 
HETATM 7553 C CAC . A1H0S F 3 .   ? 5.400   -16.028 15.121  0.90 48.67 ? 302 A1H0S A CAC 1 
HETATM 7554 C CAE . A1H0S F 3 .   ? 6.299   -13.449 15.346  0.90 42.65 ? 302 A1H0S A CAE 1 
HETATM 7555 C CAG . A1H0S F 3 .   ? 8.296   -12.571 15.163  0.90 37.67 ? 302 A1H0S A CAG 1 
HETATM 7556 C CAJ . A1H0S F 3 .   ? 10.602  -12.189 14.738  0.90 39.53 ? 302 A1H0S A CAJ 1 
HETATM 7557 C CAO . A1H0S F 3 .   ? 4.984   -17.363 14.982  0.90 52.34 ? 302 A1H0S A CAO 1 
HETATM 7558 C CAP . A1H0S F 3 .   ? 6.715   -15.672 14.798  0.90 49.46 ? 302 A1H0S A CAP 1 
HETATM 7559 C CAD . A1H0S F 3 .   ? 7.173   -14.415 14.941  0.90 44.03 ? 302 A1H0S A CAD 1 
HETATM 7560 N NAF . A1H0S F 3 .   ? 8.373   -13.841 14.650  0.90 40.25 ? 302 A1H0S A NAF 1 
HETATM 7561 C CAL . A1H0S F 3 .   ? 9.661   -14.575 14.328  0.90 41.30 ? 302 A1H0S A CAL 1 
HETATM 7562 C CAM . A1H0S F 3 .   ? 10.118  -15.713 15.268  0.90 41.58 ? 302 A1H0S A CAM 1 
HETATM 7563 C CAN . A1H0S F 3 .   ? 9.537   -15.316 12.982  0.90 37.26 ? 302 A1H0S A CAN 1 
HETATM 7564 N NAQ . A1H0S F 3 .   ? 10.754  -13.544 14.308  0.90 40.23 ? 302 A1H0S A NAQ 1 
HETATM 7565 N NAK . A1H0S F 3 .   ? 11.653  -11.372 14.780  0.90 33.82 ? 302 A1H0S A NAK 1 
HETATM 7566 N NAI . A1H0S F 3 .   ? 9.348   -11.699 15.163  0.90 36.17 ? 302 A1H0S A NAI 1 
HETATM 7567 N NAH . A1H0S F 3 .   ? 7.016   -12.312 15.409  0.90 37.36 ? 302 A1H0S A NAH 1 
HETATM 7568 C CAA . A1H0S F 3 .   ? 5.017   -13.710 15.689  0.90 41.26 ? 302 A1H0S A CAA 1 
HETATM 7569 C CAB . A1H0S F 3 .   ? 4.537   -15.026 15.577  0.90 48.47 ? 302 A1H0S A CAB 1 
HETATM 7570 C CAR . A1H0S F 3 .   ? 3.211   -15.323 15.897  0.90 51.56 ? 302 A1H0S A CAR 1 
HETATM 7571 C C   . ACT   G 4 .   ? 16.457  -16.165 2.567   0.80 23.99 ? 303 ACT   A C   1 
HETATM 7572 O O   . ACT   G 4 .   ? 15.700  -15.710 1.696   0.80 23.50 ? 303 ACT   A O   1 
HETATM 7573 O OXT . ACT   G 4 .   ? 16.111  -16.354 3.750   0.80 23.83 ? 303 ACT   A OXT 1 
HETATM 7574 C CH3 . ACT   G 4 .   ? 17.919  -16.531 2.161   0.80 30.29 ? 303 ACT   A CH3 1 
HETATM 7575 C C   . ACT   H 4 .   ? 19.822  3.273   27.895  0.70 21.31 ? 304 ACT   A C   1 
HETATM 7576 O O   . ACT   H 4 .   ? 20.300  3.983   27.005  0.70 34.21 ? 304 ACT   A O   1 
HETATM 7577 O OXT . ACT   H 4 .   ? 18.650  2.847   27.854  0.70 24.65 ? 304 ACT   A OXT 1 
HETATM 7578 C CH3 . ACT   H 4 .   ? 20.700  2.838   29.061  0.70 32.92 ? 304 ACT   A CH3 1 
HETATM 7579 P PA  . NDP   I 2 .   ? -20.621 11.506  -0.708  0.80 30.55 ? 301 NDP   B PA  1 
HETATM 7580 O O1A . NDP   I 2 .   ? -20.271 12.206  -1.956  0.80 26.08 ? 301 NDP   B O1A 1 
HETATM 7581 O O2A . NDP   I 2 .   ? -21.082 12.274  0.483   0.80 32.52 ? 301 NDP   B O2A 1 
HETATM 7582 O O5B . NDP   I 2 .   ? -21.694 10.337  -1.004  0.80 31.64 ? 301 NDP   B O5B 1 
HETATM 7583 C C5B . NDP   I 2 .   ? -21.409 9.251   -1.934  0.80 33.00 ? 301 NDP   B C5B 1 
HETATM 7584 C C4B . NDP   I 2 .   ? -22.662 8.882   -2.689  0.80 29.93 ? 301 NDP   B C4B 1 
HETATM 7585 O O4B . NDP   I 2 .   ? -23.546 8.180   -1.788  0.80 29.76 ? 301 NDP   B O4B 1 
HETATM 7586 C C3B . NDP   I 2 .   ? -23.541 10.041  -3.188  0.80 32.69 ? 301 NDP   B C3B 1 
HETATM 7587 O O3B . NDP   I 2 .   ? -23.116 10.518  -4.459  0.80 34.49 ? 301 NDP   B O3B 1 
HETATM 7588 C C2B . NDP   I 2 .   ? -24.940 9.424   -3.252  0.80 29.72 ? 301 NDP   B C2B 1 
HETATM 7589 O O2B . NDP   I 2 .   ? -25.364 9.074   -4.595  0.80 29.58 ? 301 NDP   B O2B 1 
HETATM 7590 C C1B . NDP   I 2 .   ? -24.802 8.137   -2.426  0.80 29.61 ? 301 NDP   B C1B 1 
HETATM 7591 N N9A . NDP   I 2 .   ? -25.925 8.020   -1.499  0.80 27.96 ? 301 NDP   B N9A 1 
HETATM 7592 C C8A . NDP   I 2 .   ? -26.286 8.907   -0.515  0.80 26.54 ? 301 NDP   B C8A 1 
HETATM 7593 N N7A . NDP   I 2 .   ? -27.426 8.608   0.056   0.80 28.67 ? 301 NDP   B N7A 1 
HETATM 7594 C C5A . NDP   I 2 .   ? -27.883 7.490   -0.639  0.80 28.58 ? 301 NDP   B C5A 1 
HETATM 7595 C C6A . NDP   I 2 .   ? -29.053 6.707   -0.529  0.80 26.08 ? 301 NDP   B C6A 1 
HETATM 7596 N N6A . NDP   I 2 .   ? -30.011 6.921   0.367   0.80 27.05 ? 301 NDP   B N6A 1 
HETATM 7597 N N1A . NDP   I 2 .   ? -29.198 5.672   -1.394  0.80 24.07 ? 301 NDP   B N1A 1 
HETATM 7598 C C2A . NDP   I 2 .   ? -28.206 5.418   -2.264  0.80 25.79 ? 301 NDP   B C2A 1 
HETATM 7599 N N3A . NDP   I 2 .   ? -27.062 6.078   -2.457  0.80 23.96 ? 301 NDP   B N3A 1 
HETATM 7600 C C4A . NDP   I 2 .   ? -26.972 7.132   -1.619  0.80 26.90 ? 301 NDP   B C4A 1 
HETATM 7601 O O3  . NDP   I 2 .   ? -19.305 10.619  -0.382  0.80 29.52 ? 301 NDP   B O3  1 
HETATM 7602 P PN  . NDP   I 2 .   ? -17.753 10.884  -0.762  0.80 30.33 ? 301 NDP   B PN  1 
HETATM 7603 O O1N . NDP   I 2 .   ? -17.342 12.199  -0.182  0.80 27.12 ? 301 NDP   B O1N 1 
HETATM 7604 O O2N . NDP   I 2 .   ? -17.495 10.663  -2.216  0.80 24.61 ? 301 NDP   B O2N 1 
HETATM 7605 O O5D . NDP   I 2 .   ? -17.049 9.704   0.091   0.80 27.24 ? 301 NDP   B O5D 1 
HETATM 7606 C C5D . NDP   I 2 .   ? -16.937 8.329   -0.378  0.80 23.58 ? 301 NDP   B C5D 1 
HETATM 7607 C C4D . NDP   I 2 .   ? -16.926 7.421   0.825   0.80 24.46 ? 301 NDP   B C4D 1 
HETATM 7608 O O4D . NDP   I 2 .   ? -15.867 7.891   1.706   0.80 25.08 ? 301 NDP   B O4D 1 
HETATM 7609 C C3D . NDP   I 2 .   ? -18.208 7.447   1.685   0.80 26.85 ? 301 NDP   B C3D 1 
HETATM 7610 O O3D . NDP   I 2 .   ? -18.565 6.149   2.149   0.80 26.19 ? 301 NDP   B O3D 1 
HETATM 7611 C C2D . NDP   I 2 .   ? -17.831 8.386   2.834   0.80 25.52 ? 301 NDP   B C2D 1 
HETATM 7612 O O2D . NDP   I 2 .   ? -18.492 8.227   4.083   0.80 26.23 ? 301 NDP   B O2D 1 
HETATM 7613 C C1D . NDP   I 2 .   ? -16.347 8.071   3.013   0.80 24.23 ? 301 NDP   B C1D 1 
HETATM 7614 N N1N . NDP   I 2 .   ? -15.624 9.232   3.610   0.80 26.94 ? 301 NDP   B N1N 1 
HETATM 7615 C C2N . NDP   I 2 .   ? -15.403 10.389  2.896   0.80 26.26 ? 301 NDP   B C2N 1 
HETATM 7616 C C3N . NDP   I 2 .   ? -14.796 11.493  3.480   0.80 27.47 ? 301 NDP   B C3N 1 
HETATM 7617 C C7N . NDP   I 2 .   ? -14.481 12.701  2.684   0.80 26.89 ? 301 NDP   B C7N 1 
HETATM 7618 O O7N . NDP   I 2 .   ? -13.807 13.588  3.213   0.80 27.91 ? 301 NDP   B O7N 1 
HETATM 7619 N N7N . NDP   I 2 .   ? -14.936 12.836  1.444   0.80 30.59 ? 301 NDP   B N7N 1 
HETATM 7620 C C4N . NDP   I 2 .   ? -14.523 11.469  4.947   0.80 25.24 ? 301 NDP   B C4N 1 
HETATM 7621 C C5N . NDP   I 2 .   ? -14.547 10.118  5.520   0.80 26.63 ? 301 NDP   B C5N 1 
HETATM 7622 C C6N . NDP   I 2 .   ? -15.138 9.113   4.900   0.80 27.68 ? 301 NDP   B C6N 1 
HETATM 7623 P P2B . NDP   I 2 .   ? -26.203 10.163  -5.509  0.80 29.29 ? 301 NDP   B P2B 1 
HETATM 7624 O O1X . NDP   I 2 .   ? -25.297 11.343  -5.663  0.80 32.48 ? 301 NDP   B O1X 1 
HETATM 7625 O O2X . NDP   I 2 .   ? -26.371 9.370   -6.800  0.80 23.57 ? 301 NDP   B O2X 1 
HETATM 7626 O O3X . NDP   I 2 .   ? -27.499 10.487  -4.775  0.80 31.59 ? 301 NDP   B O3X 1 
HETATM 7627 C C   . ACT   J 4 .   ? -36.030 2.287   9.760   0.80 22.72 ? 302 ACT   B C   1 
HETATM 7628 O O   . ACT   J 4 .   ? -34.849 1.821   9.718   0.80 27.86 ? 302 ACT   B O   1 
HETATM 7629 O OXT . ACT   J 4 .   ? -36.367 3.143   10.560  0.80 34.33 ? 302 ACT   B OXT 1 
HETATM 7630 C CH3 . ACT   J 4 .   ? -37.076 1.738   8.813   0.80 34.23 ? 302 ACT   B CH3 1 
HETATM 7631 P PA  . NDP   K 2 .   ? 4.460   13.397  37.444  0.90 31.67 ? 301 NDP   C PA  1 
HETATM 7632 O O1A . NDP   K 2 .   ? 4.182   14.279  38.604  0.90 30.51 ? 301 NDP   C O1A 1 
HETATM 7633 O O2A . NDP   K 2 .   ? 4.939   14.003  36.172  0.90 33.61 ? 301 NDP   C O2A 1 
HETATM 7634 O O5B . NDP   K 2 .   ? 5.506   12.234  37.857  0.90 32.98 ? 301 NDP   C O5B 1 
HETATM 7635 C C5B . NDP   K 2 .   ? 5.263   11.357  38.996  0.90 30.52 ? 301 NDP   C C5B 1 
HETATM 7636 C C4B . NDP   K 2 .   ? 6.583   11.013  39.649  0.90 26.32 ? 301 NDP   C C4B 1 
HETATM 7637 O O4B . NDP   K 2 .   ? 7.419   10.244  38.755  0.90 27.43 ? 301 NDP   C O4B 1 
HETATM 7638 C C3B . NDP   K 2 .   ? 7.513   12.188  39.996  0.90 31.16 ? 301 NDP   C C3B 1 
HETATM 7639 O O3B . NDP   K 2 .   ? 7.043   12.804  41.182  0.90 32.95 ? 301 NDP   C O3B 1 
HETATM 7640 C C2B . NDP   K 2 .   ? 8.873   11.493  40.155  0.90 31.43 ? 301 NDP   C C2B 1 
HETATM 7641 O O2B . NDP   K 2 .   ? 9.363   11.241  41.494  0.90 30.20 ? 301 NDP   C O2B 1 
HETATM 7642 C C1B . NDP   K 2 .   ? 8.682   10.173  39.383  0.90 28.43 ? 301 NDP   C C1B 1 
HETATM 7643 N N9A . NDP   K 2 .   ? 9.788   10.018  38.444  0.90 26.43 ? 301 NDP   C N9A 1 
HETATM 7644 C C8A . NDP   K 2 .   ? 10.142  10.818  37.380  0.90 26.12 ? 301 NDP   C C8A 1 
HETATM 7645 N N7A . NDP   K 2 .   ? 11.290  10.475  36.833  0.90 24.77 ? 301 NDP   C N7A 1 
HETATM 7646 C C5A . NDP   K 2 .   ? 11.739  9.408   37.621  0.90 28.15 ? 301 NDP   C C5A 1 
HETATM 7647 C C6A . NDP   K 2 .   ? 12.904  8.608   37.600  0.90 25.02 ? 301 NDP   C C6A 1 
HETATM 7648 N N6A . NDP   K 2 .   ? 13.896  8.753   36.730  0.90 23.41 ? 301 NDP   C N6A 1 
HETATM 7649 N N1A . NDP   K 2 .   ? 13.017  7.631   38.537  0.90 24.02 ? 301 NDP   C N1A 1 
HETATM 7650 C C2A . NDP   K 2 .   ? 12.038  7.476   39.445  0.90 25.95 ? 301 NDP   C C2A 1 
HETATM 7651 N N3A . NDP   K 2 .   ? 10.894  8.156   39.556  0.90 24.56 ? 301 NDP   C N3A 1 
HETATM 7652 C C4A . NDP   K 2 .   ? 10.820  9.131   38.624  0.90 26.90 ? 301 NDP   C C4A 1 
HETATM 7653 O O3  . NDP   K 2 .   ? 3.133   12.553  37.159  0.90 30.50 ? 301 NDP   C O3  1 
HETATM 7654 P PN  . NDP   K 2 .   ? 1.597   12.844  37.435  0.90 28.08 ? 301 NDP   C PN  1 
HETATM 7655 O O1N . NDP   K 2 .   ? 1.224   14.097  36.730  0.90 27.93 ? 301 NDP   C O1N 1 
HETATM 7656 O O2N . NDP   K 2 .   ? 1.330   12.704  38.907  0.90 24.65 ? 301 NDP   C O2N 1 
HETATM 7657 O O5D . NDP   K 2 .   ? 0.944   11.580  36.698  0.90 28.00 ? 301 NDP   C O5D 1 
HETATM 7658 C C5D . NDP   K 2 .   ? 0.965   10.256  37.304  0.90 27.51 ? 301 NDP   C C5D 1 
HETATM 7659 C C4D . NDP   K 2 .   ? 0.901   9.244   36.186  0.90 26.07 ? 301 NDP   C C4D 1 
HETATM 7660 O O4D . NDP   K 2 .   ? -0.235  9.553   35.325  0.90 25.60 ? 301 NDP   C O4D 1 
HETATM 7661 C C3D . NDP   K 2 .   ? 2.146   9.222   35.269  0.90 24.64 ? 301 NDP   C C3D 1 
HETATM 7662 O O3D . NDP   K 2 .   ? 2.484   7.886   34.928  0.90 22.30 ? 301 NDP   C O3D 1 
HETATM 7663 C C2D . NDP   K 2 .   ? 1.676   9.969   34.019  0.90 27.39 ? 301 NDP   C C2D 1 
HETATM 7664 O O2D . NDP   K 2 .   ? 2.336   9.609   32.809  0.90 28.04 ? 301 NDP   C O2D 1 
HETATM 7665 C C1D . NDP   K 2 .   ? 0.188   9.606   33.977  0.90 27.71 ? 301 NDP   C C1D 1 
HETATM 7666 N N1N . NDP   K 2 .   ? -0.568  10.689  33.303  0.90 26.79 ? 301 NDP   C N1N 1 
HETATM 7667 C C2N . NDP   K 2 .   ? -0.795  11.893  33.926  0.90 28.77 ? 301 NDP   C C2N 1 
HETATM 7668 C C3N . NDP   K 2 .   ? -1.380  12.939  33.252  0.90 26.77 ? 301 NDP   C C3N 1 
HETATM 7669 C C7N . NDP   K 2 .   ? -1.632  14.240  33.920  0.90 27.78 ? 301 NDP   C C7N 1 
HETATM 7670 O O7N . NDP   K 2 .   ? -2.313  15.095  33.331  0.90 28.60 ? 301 NDP   C O7N 1 
HETATM 7671 N N7N . NDP   K 2 .   ? -1.002  14.509  35.063  0.90 27.77 ? 301 NDP   C N7N 1 
HETATM 7672 C C4N . NDP   K 2 .   ? -1.694  12.746  31.814  0.90 24.73 ? 301 NDP   C C4N 1 
HETATM 7673 C C5N . NDP   K 2 .   ? -1.624  11.384  31.312  0.90 24.94 ? 301 NDP   C C5N 1 
HETATM 7674 C C6N . NDP   K 2 .   ? -1.037  10.449  32.018  0.90 26.82 ? 301 NDP   C C6N 1 
HETATM 7675 P P2B . NDP   K 2 .   ? 10.066  12.445  42.373  0.90 28.13 ? 301 NDP   C P2B 1 
HETATM 7676 O O1X . NDP   K 2 .   ? 10.166  11.756  43.689  0.90 27.71 ? 301 NDP   C O1X 1 
HETATM 7677 O O2X . NDP   K 2 .   ? 11.388  12.784  41.727  0.90 28.34 ? 301 NDP   C O2X 1 
HETATM 7678 O O3X . NDP   K 2 .   ? 9.117   13.636  42.434  0.90 27.28 ? 301 NDP   C O3X 1 
HETATM 7679 C CAC . A1H0S L 3 .   ? -0.160  16.571  29.843  0.80 49.94 ? 302 A1H0S C CAC 1 
HETATM 7680 C CAE . A1H0S L 3 .   ? 0.726   13.949  30.205  0.80 45.18 ? 302 A1H0S C CAE 1 
HETATM 7681 C CAG . A1H0S L 3 .   ? 2.208   13.084  31.558  0.80 39.33 ? 302 A1H0S C CAG 1 
HETATM 7682 C CAJ . A1H0S L 3 .   ? 3.840   12.710  33.312  0.80 42.03 ? 302 A1H0S C CAJ 1 
HETATM 7683 C CAO . A1H0S L 3 .   ? -0.592  17.915  29.694  0.80 54.98 ? 302 A1H0S C CAO 1 
HETATM 7684 C CAP . A1H0S L 3 .   ? 0.651   16.192  30.939  0.80 50.73 ? 302 A1H0S C CAP 1 
HETATM 7685 C CAD . A1H0S L 3 .   ? 1.116   14.912  31.090  0.80 45.20 ? 302 A1H0S C CAD 1 
HETATM 7686 N NAF . A1H0S L 3 .   ? 1.864   14.312  32.056  0.80 40.58 ? 302 A1H0S C NAF 1 
HETATM 7687 C CAL . A1H0S L 3 .   ? 2.644   14.961  33.157  0.80 41.31 ? 302 A1H0S C CAL 1 
HETATM 7688 C CAM . A1H0S L 3 .   ? 3.411   16.219  32.738  0.80 41.88 ? 302 A1H0S C CAM 1 
HETATM 7689 C CAN . A1H0S L 3 .   ? 1.726   15.502  34.230  0.80 39.56 ? 302 A1H0S C CAN 1 
HETATM 7690 N NAQ . A1H0S L 3 .   ? 3.581   14.009  33.785  0.80 40.39 ? 302 A1H0S C NAQ 1 
HETATM 7691 N NAK . A1H0S L 3 .   ? 4.759   11.962  33.919  0.80 38.14 ? 302 A1H0S C NAK 1 
HETATM 7692 N NAI . A1H0S L 3 .   ? 3.112   12.233  32.217  0.80 41.06 ? 302 A1H0S C NAI 1 
HETATM 7693 N NAH . A1H0S L 3 .   ? 1.341   12.804  30.567  0.80 40.02 ? 302 A1H0S C NAH 1 
HETATM 7694 C CAA . A1H0S L 3 .   ? -0.044  14.253  29.123  0.80 50.49 ? 302 A1H0S C CAA 1 
HETATM 7695 C CAB . A1H0S L 3 .   ? -0.524  15.572  28.915  0.80 52.79 ? 302 A1H0S C CAB 1 
HETATM 7696 C CAR . A1H0S L 3 .   ? -1.330  15.852  27.789  0.80 53.78 ? 302 A1H0S C CAR 1 
HETATM 7697 C C   . ACT   M 4 .   ? 11.748  4.105   55.525  0.80 24.42 ? 303 ACT   C C   1 
HETATM 7698 O O   . ACT   M 4 .   ? 12.837  4.741   55.154  0.80 31.93 ? 303 ACT   C O   1 
HETATM 7699 O OXT . ACT   M 4 .   ? 11.715  2.957   55.791  0.80 29.11 ? 303 ACT   C OXT 1 
HETATM 7700 C CH3 . ACT   M 4 .   ? 10.445  4.770   55.646  0.80 21.81 ? 303 ACT   C CH3 1 
HETATM 7701 P PA  . NDP   N 2 .   ? -29.773 -11.978 27.191  0.90 34.88 ? 301 NDP   D PA  1 
HETATM 7702 O O1A . NDP   N 2 .   ? -30.148 -12.811 28.356  0.90 35.22 ? 301 NDP   D O1A 1 
HETATM 7703 O O2A . NDP   N 2 .   ? -29.452 -12.665 25.915  0.90 38.14 ? 301 NDP   D O2A 1 
HETATM 7704 O O5B . NDP   N 2 .   ? -30.855 -10.834 26.887  0.90 34.38 ? 301 NDP   D O5B 1 
HETATM 7705 C C5B . NDP   N 2 .   ? -31.236 -9.758  27.770  0.90 34.05 ? 301 NDP   D C5B 1 
HETATM 7706 C C4B . NDP   N 2 .   ? -32.678 -9.424  27.465  0.90 31.32 ? 301 NDP   D C4B 1 
HETATM 7707 O O4B . NDP   N 2 .   ? -32.779 -8.733  26.199  0.90 28.85 ? 301 NDP   D O4B 1 
HETATM 7708 C C3B . NDP   N 2 .   ? -33.611 -10.623 27.226  0.90 36.58 ? 301 NDP   D C3B 1 
HETATM 7709 O O3B . NDP   N 2 .   ? -33.957 -11.277 28.442  0.90 40.40 ? 301 NDP   D O3B 1 
HETATM 7710 C C2B . NDP   N 2 .   ? -34.783 -9.985  26.474  0.90 32.03 ? 301 NDP   D C2B 1 
HETATM 7711 O O2B . NDP   N 2 .   ? -35.905 -9.603  27.288  0.90 33.87 ? 301 NDP   D O2B 1 
HETATM 7712 C C1B . NDP   N 2 .   ? -34.147 -8.711  25.888  0.90 30.85 ? 301 NDP   D C1B 1 
HETATM 7713 N N9A . NDP   N 2 .   ? -34.447 -8.593  24.467  0.90 28.79 ? 301 NDP   D N9A 1 
HETATM 7714 C C8A . NDP   N 2 .   ? -34.182 -9.490  23.459  0.90 27.40 ? 301 NDP   D C8A 1 
HETATM 7715 N N7A . NDP   N 2 .   ? -34.810 -9.200  22.346  0.90 28.44 ? 301 NDP   D N7A 1 
HETATM 7716 C C5A . NDP   N 2 .   ? -35.558 -8.067  22.647  0.90 26.50 ? 301 NDP   D C5A 1 
HETATM 7717 C C6A . NDP   N 2 .   ? -36.440 -7.270  21.890  0.90 26.52 ? 301 NDP   D C6A 1 
HETATM 7718 N N6A . NDP   N 2 .   ? -36.714 -7.470  20.600  0.90 28.03 ? 301 NDP   D N6A 1 
HETATM 7719 N N1A . NDP   N 2 .   ? -37.044 -6.232  22.528  0.90 26.51 ? 301 NDP   D N1A 1 
HETATM 7720 C C2A . NDP   N 2 .   ? -36.783 -6.025  23.832  0.90 27.56 ? 301 NDP   D C2A 1 
HETATM 7721 N N3A . NDP   N 2 .   ? -35.960 -6.702  24.639  0.90 24.16 ? 301 NDP   D N3A 1 
HETATM 7722 C C4A . NDP   N 2 .   ? -35.384 -7.723  23.974  0.90 26.56 ? 301 NDP   D C4A 1 
HETATM 7723 O O3  . NDP   N 2 .   ? -28.506 -11.110 27.635  0.90 31.72 ? 301 NDP   D O3  1 
HETATM 7724 P PN  . NDP   N 2 .   ? -27.458 -11.363 28.804  0.90 31.08 ? 301 NDP   D PN  1 
HETATM 7725 O O1N . NDP   N 2 .   ? -26.790 -12.658 28.520  0.90 31.91 ? 301 NDP   D O1N 1 
HETATM 7726 O O2N . NDP   N 2 .   ? -28.189 -11.161 30.092  0.90 28.85 ? 301 NDP   D O2N 1 
HETATM 7727 O O5D . NDP   N 2 .   ? -26.411 -10.155 28.561  0.90 26.93 ? 301 NDP   D O5D 1 
HETATM 7728 C C5D . NDP   N 2 .   ? -26.738 -8.776  28.912  0.90 22.63 ? 301 NDP   D C5D 1 
HETATM 7729 C C4D . NDP   N 2 .   ? -25.977 -7.847  27.983  0.90 21.84 ? 301 NDP   D C4D 1 
HETATM 7730 O O4D . NDP   N 2 .   ? -24.560 -8.207  27.987  0.90 22.96 ? 301 NDP   D O4D 1 
HETATM 7731 C C3D . NDP   N 2 .   ? -26.395 -7.865  26.500  0.90 23.00 ? 301 NDP   D C3D 1 
HETATM 7732 O O3D . NDP   N 2 .   ? -26.392 -6.539  25.972  0.90 26.60 ? 301 NDP   D O3D 1 
HETATM 7733 C C2D . NDP   N 2 .   ? -25.321 -8.751  25.870  0.90 24.84 ? 301 NDP   D C2D 1 
HETATM 7734 O O2D . NDP   N 2 .   ? -25.080 -8.572  24.478  0.90 25.74 ? 301 NDP   D O2D 1 
HETATM 7735 C C1D . NDP   N 2 .   ? -24.088 -8.365  26.675  0.90 23.36 ? 301 NDP   D C1D 1 
HETATM 7736 N N1N . NDP   N 2 .   ? -23.109 -9.486  26.655  0.90 27.88 ? 301 NDP   D N1N 1 
HETATM 7737 C C2N . NDP   N 2 .   ? -23.369 -10.656 27.337  0.90 28.73 ? 301 NDP   D C2N 1 
HETATM 7738 C C3N . NDP   N 2 .   ? -22.486 -11.704 27.325  0.90 29.08 ? 301 NDP   D C3N 1 
HETATM 7739 C C7N . NDP   N 2 .   ? -22.761 -12.916 28.126  0.90 30.37 ? 301 NDP   D C7N 1 
HETATM 7740 O O7N . NDP   N 2 .   ? -21.923 -13.830 28.140  0.90 33.88 ? 301 NDP   D O7N 1 
HETATM 7741 N N7N . NDP   N 2 .   ? -23.912 -13.017 28.786  0.90 30.22 ? 301 NDP   D N7N 1 
HETATM 7742 C C4N . NDP   N 2 .   ? -21.304 -11.612 26.416  0.90 26.50 ? 301 NDP   D C4N 1 
HETATM 7743 C C5N . NDP   N 2 .   ? -21.128 -10.352 25.733  0.90 28.85 ? 301 NDP   D C5N 1 
HETATM 7744 C C6N . NDP   N 2 .   ? -21.959 -9.346  25.918  0.90 29.82 ? 301 NDP   D C6N 1 
HETATM 7745 P P2B . NDP   N 2 .   ? -37.118 -10.663 27.582  0.90 32.81 ? 301 NDP   D P2B 1 
HETATM 7746 O O1X . NDP   N 2 .   ? -36.544 -11.868 28.298  0.90 31.10 ? 301 NDP   D O1X 1 
HETATM 7747 O O2X . NDP   N 2 .   ? -38.039 -9.811  28.458  0.90 31.69 ? 301 NDP   D O2X 1 
HETATM 7748 O O3X . NDP   N 2 .   ? -37.781 -11.061 26.268  0.90 32.23 ? 301 NDP   D O3X 1 
HETATM 7749 C CAC . A1H0S O 3 .   ? -21.391 -15.643 24.199  0.80 51.08 ? 302 A1H0S D CAC 1 
HETATM 7750 C CAE . A1H0S O 3 .   ? -22.279 -13.095 23.697  0.80 45.00 ? 302 A1H0S D CAE 1 
HETATM 7751 C CAG . A1H0S O 3 .   ? -24.244 -12.149 23.843  0.80 39.51 ? 302 A1H0S D CAG 1 
HETATM 7752 C CAJ . A1H0S O 3 .   ? -26.514 -11.650 24.306  0.80 39.46 ? 302 A1H0S D CAJ 1 
HETATM 7753 C CAO . A1H0S O 3 .   ? -21.009 -16.960 24.508  0.80 53.22 ? 302 A1H0S D CAO 1 
HETATM 7754 C CAP . A1H0S O 3 .   ? -22.692 -15.233 24.525  0.80 50.60 ? 302 A1H0S D CAP 1 
HETATM 7755 C CAD . A1H0S O 3 .   ? -23.137 -13.985 24.245  0.80 47.87 ? 302 A1H0S D CAD 1 
HETATM 7756 N NAF . A1H0S O 3 .   ? -24.313 -13.350 24.506  0.80 44.28 ? 302 A1H0S D NAF 1 
HETATM 7757 C CAL . A1H0S O 3 .   ? -25.603 -13.980 24.962  0.80 42.31 ? 302 A1H0S D CAL 1 
HETATM 7758 C CAM . A1H0S O 3 .   ? -26.053 -15.205 24.172  0.80 45.44 ? 302 A1H0S D CAM 1 
HETATM 7759 C CAN . A1H0S O 3 .   ? -25.478 -14.542 26.375  0.80 43.60 ? 302 A1H0S D CAN 1 
HETATM 7760 N NAQ . A1H0S O 3 .   ? -26.687 -12.949 24.883  0.80 38.99 ? 302 A1H0S D NAQ 1 
HETATM 7761 N NAK . A1H0S O 3 .   ? -27.534 -10.824 24.162  0.80 37.30 ? 302 A1H0S D NAK 1 
HETATM 7762 N NAI . A1H0S O 3 .   ? -25.273 -11.227 23.827  0.80 39.34 ? 302 A1H0S D NAI 1 
HETATM 7763 N NAH . A1H0S O 3 .   ? -22.972 -11.966 23.517  0.80 41.59 ? 302 A1H0S D NAH 1 
HETATM 7764 C CAA . A1H0S O 3 .   ? -21.021 -13.418 23.348  0.80 47.22 ? 302 A1H0S D CAA 1 
HETATM 7765 C CAB . A1H0S O 3 .   ? -20.528 -14.707 23.598  0.80 46.82 ? 302 A1H0S D CAB 1 
HETATM 7766 C CAR . A1H0S O 3 .   ? -19.209 -14.994 23.233  0.80 52.14 ? 302 A1H0S D CAR 1 
HETATM 7767 O O   . HOH   P 5 .   ? 29.734  1.152   8.909   1.00 35.45 ? 401 HOH   A O   1 
HETATM 7768 O O   . HOH   P 5 .   ? 22.052  -15.089 -2.208  1.00 41.28 ? 402 HOH   A O   1 
HETATM 7769 O O   . HOH   P 5 .   ? 6.520   10.119  0.741   1.00 35.80 ? 403 HOH   A O   1 
HETATM 7770 O O   . HOH   P 5 .   ? -2.329  11.015  -6.965  1.00 47.30 ? 404 HOH   A O   1 
HETATM 7771 O O   . HOH   P 5 .   ? 11.920  16.999  15.019  1.00 44.94 ? 405 HOH   A O   1 
HETATM 7772 O O   . HOH   P 5 .   ? -7.335  -7.814  18.168  1.00 40.29 ? 406 HOH   A O   1 
HETATM 7773 O O   . HOH   P 5 .   ? -4.028  -24.882 15.166  1.00 50.64 ? 407 HOH   A O   1 
HETATM 7774 O O   . HOH   P 5 .   ? 13.942  -10.825 8.042   1.00 28.57 ? 408 HOH   A O   1 
HETATM 7775 O O   . HOH   P 5 .   ? 16.509  11.711  -1.564  1.00 35.41 ? 409 HOH   A O   1 
HETATM 7776 O O   . HOH   P 5 .   ? 13.480  -3.046  13.884  1.00 25.50 ? 410 HOH   A O   1 
HETATM 7777 O O   . HOH   P 5 .   ? -2.957  -14.822 23.806  1.00 27.36 ? 411 HOH   A O   1 
HETATM 7778 O O   . HOH   P 5 .   ? 3.213   -30.000 6.681   1.00 41.06 ? 412 HOH   A O   1 
HETATM 7779 O O   . HOH   P 5 .   ? 0.099   13.443  -0.146  1.00 49.98 ? 413 HOH   A O   1 
HETATM 7780 O O   . HOH   P 5 .   ? 4.192   11.554  8.080   1.00 22.56 ? 414 HOH   A O   1 
HETATM 7781 O O   . HOH   P 5 .   ? 14.231  -18.031 4.285   1.00 39.65 ? 415 HOH   A O   1 
HETATM 7782 O O   . HOH   P 5 .   ? 23.072  -8.481  22.919  1.00 40.68 ? 416 HOH   A O   1 
HETATM 7783 O O   . HOH   P 5 .   ? 2.068   -12.276 14.881  1.00 42.43 ? 417 HOH   A O   1 
HETATM 7784 O O   . HOH   P 5 .   ? 20.934  -11.070 15.212  1.00 33.54 ? 418 HOH   A O   1 
HETATM 7785 O O   . HOH   P 5 .   ? 21.752  -11.696 -9.854  1.00 42.20 ? 419 HOH   A O   1 
HETATM 7786 O O   . HOH   P 5 .   ? 25.345  3.571   -7.106  1.00 39.21 ? 420 HOH   A O   1 
HETATM 7787 O O   . HOH   P 5 .   ? 13.795  -13.873 1.605   1.00 32.95 ? 421 HOH   A O   1 
HETATM 7788 O O   . HOH   P 5 .   ? 28.400  -7.234  -4.175  1.00 42.61 ? 422 HOH   A O   1 
HETATM 7789 O O   . HOH   P 5 .   ? 15.381  -1.645  12.490  1.00 20.12 ? 423 HOH   A O   1 
HETATM 7790 O O   . HOH   P 5 .   ? 21.915  11.062  13.503  1.00 37.07 ? 424 HOH   A O   1 
HETATM 7791 O O   . HOH   P 5 .   ? 3.159   -11.736 25.965  1.00 24.63 ? 425 HOH   A O   1 
HETATM 7792 O O   . HOH   P 5 .   ? 20.811  -14.173 1.707   1.00 31.94 ? 426 HOH   A O   1 
HETATM 7793 O O   . HOH   P 5 .   ? 19.718  -9.159  36.607  1.00 53.98 ? 427 HOH   A O   1 
HETATM 7794 O O   . HOH   P 5 .   ? -7.263  -6.913  14.102  1.00 35.24 ? 428 HOH   A O   1 
HETATM 7795 O O   . HOH   P 5 .   ? 15.154  -12.796 15.447  1.00 47.17 ? 429 HOH   A O   1 
HETATM 7796 O O   . HOH   P 5 .   ? -7.309  -9.415  9.802   1.00 20.93 ? 430 HOH   A O   1 
HETATM 7797 O O   . HOH   P 5 .   ? 3.791   -15.741 -2.540  1.00 48.66 ? 431 HOH   A O   1 
HETATM 7798 O O   . HOH   P 5 .   ? 11.443  6.761   -2.776  1.00 35.12 ? 432 HOH   A O   1 
HETATM 7799 O O   . HOH   P 5 .   ? 28.437  2.600   2.581   1.00 35.58 ? 433 HOH   A O   1 
HETATM 7800 O O   . HOH   P 5 .   ? 25.205  -0.956  18.582  1.00 28.05 ? 434 HOH   A O   1 
HETATM 7801 O O   . HOH   P 5 .   ? -7.199  -7.974  22.762  1.00 32.22 ? 435 HOH   A O   1 
HETATM 7802 O O   . HOH   P 5 .   ? 18.954  -3.431  29.683  1.00 32.50 ? 436 HOH   A O   1 
HETATM 7803 O O   . HOH   P 5 .   ? 16.937  -7.031  -8.882  1.00 46.18 ? 437 HOH   A O   1 
HETATM 7804 O O   . HOH   P 5 .   ? -3.790  -8.197  17.990  1.00 23.00 ? 438 HOH   A O   1 
HETATM 7805 O O   . HOH   P 5 .   ? 8.577   6.243   -0.093  1.00 31.78 ? 439 HOH   A O   1 
HETATM 7806 O O   . HOH   P 5 .   ? 24.423  -1.413  20.974  1.00 28.68 ? 440 HOH   A O   1 
HETATM 7807 O O   . HOH   P 5 .   ? 1.486   -12.855 7.970   1.00 25.80 ? 441 HOH   A O   1 
HETATM 7808 O O   . HOH   P 5 .   ? -9.299  -20.098 12.280  1.00 46.32 ? 442 HOH   A O   1 
HETATM 7809 O O   . HOH   P 5 .   ? 19.657  -15.121 11.621  1.00 53.79 ? 443 HOH   A O   1 
HETATM 7810 O O   . HOH   P 5 .   ? 7.428   18.723  13.117  1.00 49.22 ? 444 HOH   A O   1 
HETATM 7811 O O   . HOH   P 5 .   ? 0.995   -3.945  15.470  1.00 35.08 ? 445 HOH   A O   1 
HETATM 7812 O O   . HOH   P 5 .   ? 26.503  0.873   12.788  1.00 43.27 ? 446 HOH   A O   1 
HETATM 7813 O O   . HOH   P 5 .   ? -3.697  5.701   -1.226  1.00 21.58 ? 447 HOH   A O   1 
HETATM 7814 O O   . HOH   P 5 .   ? 25.776  1.190   27.310  1.00 36.00 ? 448 HOH   A O   1 
HETATM 7815 O O   . HOH   P 5 .   ? 3.931   18.119  4.453   1.00 36.23 ? 449 HOH   A O   1 
HETATM 7816 O O   . HOH   P 5 .   ? -3.739  -17.477 1.645   1.00 37.45 ? 450 HOH   A O   1 
HETATM 7817 O O   . HOH   P 5 .   ? 20.878  7.860   15.957  1.00 26.01 ? 451 HOH   A O   1 
HETATM 7818 O O   . HOH   P 5 .   ? 7.224   -20.827 7.092   1.00 38.30 ? 452 HOH   A O   1 
HETATM 7819 O O   . HOH   P 5 .   ? 16.783  18.527  8.843   1.00 61.90 ? 453 HOH   A O   1 
HETATM 7820 O O   . HOH   P 5 .   ? 2.095   17.574  12.280  1.00 41.04 ? 454 HOH   A O   1 
HETATM 7821 O O   . HOH   P 5 .   ? -1.257  -14.800 9.413   1.00 21.90 ? 455 HOH   A O   1 
HETATM 7822 O O   . HOH   P 5 .   ? 2.660   -3.788  -3.920  1.00 31.46 ? 456 HOH   A O   1 
HETATM 7823 O O   . HOH   P 5 .   ? 27.463  -2.855  16.079  1.00 37.26 ? 457 HOH   A O   1 
HETATM 7824 O O   B HOH   P 5 .   ? 0.415   -7.166  24.518  0.50 20.16 ? 458 HOH   A O   1 
HETATM 7825 O O   . HOH   P 5 .   ? 15.696  -13.351 18.060  1.00 35.55 ? 459 HOH   A O   1 
HETATM 7826 O O   . HOH   P 5 .   ? 20.285  3.861   23.390  1.00 37.11 ? 460 HOH   A O   1 
HETATM 7827 O O   . HOH   P 5 .   ? 14.051  -19.061 7.103   1.00 37.91 ? 461 HOH   A O   1 
HETATM 7828 O O   . HOH   P 5 .   ? 0.310   -17.370 1.683   1.00 38.34 ? 462 HOH   A O   1 
HETATM 7829 O O   . HOH   P 5 .   ? 16.778  -14.600 10.845  1.00 43.67 ? 463 HOH   A O   1 
HETATM 7830 O O   . HOH   P 5 .   ? 27.544  -0.639  15.103  1.00 33.64 ? 464 HOH   A O   1 
HETATM 7831 O O   . HOH   P 5 .   ? 3.637   -5.522  -5.227  1.00 49.08 ? 465 HOH   A O   1 
HETATM 7832 O O   . HOH   P 5 .   ? 10.884  -4.350  13.906  1.00 34.20 ? 466 HOH   A O   1 
HETATM 7833 O O   . HOH   P 5 .   ? 23.206  -12.079 29.264  1.00 32.49 ? 467 HOH   A O   1 
HETATM 7834 O O   . HOH   P 5 .   ? 12.635  -13.692 31.828  1.00 36.39 ? 468 HOH   A O   1 
HETATM 7835 O O   . HOH   P 5 .   ? 19.104  -11.407 35.304  1.00 41.36 ? 469 HOH   A O   1 
HETATM 7836 O O   . HOH   P 5 .   ? 0.206   -10.387 -2.276  1.00 27.70 ? 470 HOH   A O   1 
HETATM 7837 O O   . HOH   P 5 .   ? 25.835  6.770   20.870  1.00 30.54 ? 471 HOH   A O   1 
HETATM 7838 O O   . HOH   P 5 .   ? 9.568   -11.522 25.093  1.00 22.78 ? 472 HOH   A O   1 
HETATM 7839 O O   . HOH   P 5 .   ? 29.159  -3.642  -7.955  1.00 54.88 ? 473 HOH   A O   1 
HETATM 7840 O O   . HOH   P 5 .   ? -4.703  -2.875  8.781   1.00 26.10 ? 474 HOH   A O   1 
HETATM 7841 O O   . HOH   P 5 .   ? 6.020   13.303  17.630  1.00 24.12 ? 475 HOH   A O   1 
HETATM 7842 O O   . HOH   P 5 .   ? 8.600   12.991  0.192   1.00 36.08 ? 476 HOH   A O   1 
HETATM 7843 O O   . HOH   P 5 .   ? 8.471   3.547   -4.860  1.00 38.95 ? 477 HOH   A O   1 
HETATM 7844 O O   . HOH   P 5 .   ? 3.678   -3.847  16.474  1.00 39.09 ? 478 HOH   A O   1 
HETATM 7845 O O   . HOH   P 5 .   ? 7.086   1.182   -4.506  1.00 39.38 ? 479 HOH   A O   1 
HETATM 7846 O O   . HOH   P 5 .   ? 5.662   4.537   4.484   1.00 25.99 ? 480 HOH   A O   1 
HETATM 7847 O O   . HOH   P 5 .   ? -3.568  1.892   11.245  1.00 27.53 ? 481 HOH   A O   1 
HETATM 7848 O O   . HOH   P 5 .   ? 14.256  -18.336 12.237  1.00 48.21 ? 482 HOH   A O   1 
HETATM 7849 O O   . HOH   P 5 .   ? -4.864  -8.970  6.738   1.00 21.91 ? 483 HOH   A O   1 
HETATM 7850 O O   . HOH   P 5 .   ? -3.825  -5.905  14.729  1.00 38.67 ? 484 HOH   A O   1 
HETATM 7851 O O   . HOH   P 5 .   ? 29.672  -3.076  7.540   1.00 40.65 ? 485 HOH   A O   1 
HETATM 7852 O O   . HOH   P 5 .   ? -2.425  7.963   -1.282  1.00 25.06 ? 486 HOH   A O   1 
HETATM 7853 O O   . HOH   P 5 .   ? 18.141  11.745  0.709   1.00 31.00 ? 487 HOH   A O   1 
HETATM 7854 O O   . HOH   P 5 .   ? 0.295   -18.380 24.133  1.00 49.80 ? 488 HOH   A O   1 
HETATM 7855 O O   . HOH   P 5 .   ? 9.374   5.512   12.548  1.00 21.93 ? 489 HOH   A O   1 
HETATM 7856 O O   . HOH   P 5 .   ? 13.027  -16.250 13.183  1.00 42.53 ? 490 HOH   A O   1 
HETATM 7857 O O   . HOH   P 5 .   ? 20.004  -9.770  8.413   1.00 28.55 ? 491 HOH   A O   1 
HETATM 7858 O O   . HOH   P 5 .   ? 5.606   4.704   -7.299  1.00 39.22 ? 492 HOH   A O   1 
HETATM 7859 O O   . HOH   P 5 .   ? 7.337   -26.181 5.413   1.00 55.92 ? 493 HOH   A O   1 
HETATM 7860 O O   . HOH   P 5 .   ? 17.650  -16.681 30.633  1.00 47.50 ? 494 HOH   A O   1 
HETATM 7861 O O   . HOH   P 5 .   ? 25.058  -15.734 7.027   1.00 37.21 ? 495 HOH   A O   1 
HETATM 7862 O O   . HOH   P 5 .   ? 28.084  7.377   14.112  1.00 41.67 ? 496 HOH   A O   1 
HETATM 7863 O O   . HOH   P 5 .   ? -2.589  3.966   13.607  1.00 29.11 ? 497 HOH   A O   1 
HETATM 7864 O O   . HOH   P 5 .   ? 2.598   3.748   -7.695  1.00 45.11 ? 498 HOH   A O   1 
HETATM 7865 O O   . HOH   P 5 .   ? 27.724  -15.555 8.212   1.00 44.88 ? 499 HOH   A O   1 
HETATM 7866 O O   . HOH   P 5 .   ? 21.491  5.728   -10.221 1.00 50.68 ? 500 HOH   A O   1 
HETATM 7867 O O   . HOH   P 5 .   ? 10.238  -10.415 -2.654  1.00 39.48 ? 501 HOH   A O   1 
HETATM 7868 O O   . HOH   P 5 .   ? 29.055  -3.861  0.460   1.00 38.03 ? 502 HOH   A O   1 
HETATM 7869 O O   . HOH   P 5 .   ? 3.553   -12.133 20.076  1.00 29.45 ? 503 HOH   A O   1 
HETATM 7870 O O   . HOH   P 5 .   ? 23.615  5.853   31.163  1.00 45.34 ? 504 HOH   A O   1 
HETATM 7871 O O   . HOH   P 5 .   ? -3.656  -2.524  12.268  1.00 36.27 ? 505 HOH   A O   1 
HETATM 7872 O O   . HOH   P 5 .   ? 21.302  -0.870  27.704  1.00 43.83 ? 506 HOH   A O   1 
HETATM 7873 O O   . HOH   P 5 .   ? 3.925   -19.817 2.361   1.00 45.63 ? 507 HOH   A O   1 
HETATM 7874 O O   . HOH   P 5 .   ? -12.294 -20.049 16.581  1.00 50.33 ? 508 HOH   A O   1 
HETATM 7875 O O   . HOH   P 5 .   ? 6.231   22.864  5.999   1.00 49.99 ? 509 HOH   A O   1 
HETATM 7876 O O   A HOH   P 5 .   ? 34.169  5.480   6.044   0.60 25.76 ? 510 HOH   A O   1 
HETATM 7877 O O   B HOH   P 5 .   ? 33.984  3.675   6.248   0.40 19.81 ? 510 HOH   A O   1 
HETATM 7878 O O   . HOH   P 5 .   ? 14.063  -1.226  -12.465 1.00 57.83 ? 511 HOH   A O   1 
HETATM 7879 O O   . HOH   P 5 .   ? 25.245  -4.964  -14.621 1.00 60.50 ? 512 HOH   A O   1 
HETATM 7880 O O   . HOH   P 5 .   ? 27.581  8.523   -4.238  1.00 51.14 ? 513 HOH   A O   1 
HETATM 7881 O O   . HOH   P 5 .   ? 18.248  13.223  -3.518  1.00 52.04 ? 514 HOH   A O   1 
HETATM 7882 O O   . HOH   P 5 .   ? -13.430 -17.681 14.729  1.00 39.92 ? 515 HOH   A O   1 
HETATM 7883 O O   . HOH   P 5 .   ? 16.096  -15.682 27.723  1.00 55.05 ? 516 HOH   A O   1 
HETATM 7884 O O   . HOH   P 5 .   ? 5.864   13.914  -0.385  1.00 54.86 ? 517 HOH   A O   1 
HETATM 7885 O O   . HOH   P 5 .   ? 11.076  4.293   -8.223  1.00 49.39 ? 518 HOH   A O   1 
HETATM 7886 O O   . HOH   P 5 .   ? -8.359  -26.372 9.156   1.00 56.41 ? 519 HOH   A O   1 
HETATM 7887 O O   . HOH   P 5 .   ? 6.372   -19.521 2.583   1.00 38.48 ? 520 HOH   A O   1 
HETATM 7888 O O   . HOH   P 5 .   ? 17.300  -13.688 14.337  1.00 47.26 ? 521 HOH   A O   1 
HETATM 7889 O O   . HOH   P 5 .   ? 2.185   -0.881  -5.486  1.00 45.77 ? 522 HOH   A O   1 
HETATM 7890 O O   . HOH   P 5 .   ? 17.741  -10.582 -8.016  1.00 37.02 ? 523 HOH   A O   1 
HETATM 7891 O O   . HOH   P 5 .   ? 29.154  1.560   -3.673  1.00 52.35 ? 524 HOH   A O   1 
HETATM 7892 O O   . HOH   P 5 .   ? -2.120  -4.415  13.585  1.00 39.14 ? 525 HOH   A O   1 
HETATM 7893 O O   . HOH   P 5 .   ? 16.726  -18.332 7.564   1.00 40.13 ? 526 HOH   A O   1 
HETATM 7894 O O   . HOH   P 5 .   ? 20.146  9.808   17.489  1.00 40.57 ? 527 HOH   A O   1 
HETATM 7895 O O   . HOH   P 5 .   ? 6.261   -19.271 19.111  1.00 46.65 ? 528 HOH   A O   1 
HETATM 7896 O O   . HOH   P 5 .   ? 5.954   0.213   -6.707  1.00 44.42 ? 529 HOH   A O   1 
HETATM 7897 O O   . HOH   P 5 .   ? 12.251  -19.244 28.641  1.00 52.93 ? 530 HOH   A O   1 
HETATM 7898 O O   . HOH   P 5 .   ? -11.802 -19.101 12.476  1.00 53.67 ? 531 HOH   A O   1 
HETATM 7899 O O   . HOH   P 5 .   ? -6.051  -5.472  15.380  1.00 44.15 ? 532 HOH   A O   1 
HETATM 7900 O O   . HOH   P 5 .   ? 5.976   -34.494 12.991  1.00 52.11 ? 533 HOH   A O   1 
HETATM 7901 O O   . HOH   P 5 .   ? -1.496  -2.521  16.431  1.00 52.38 ? 534 HOH   A O   1 
HETATM 7902 O O   . HOH   P 5 .   ? 22.444  -18.873 5.537   1.00 52.68 ? 535 HOH   A O   1 
HETATM 7903 O O   . HOH   Q 5 .   ? -35.837 6.824   -10.683 1.00 41.49 ? 401 HOH   B O   1 
HETATM 7904 O O   . HOH   Q 5 .   ? -29.261 -13.135 -2.357  1.00 57.50 ? 402 HOH   B O   1 
HETATM 7905 O O   . HOH   Q 5 .   ? -4.170  5.480   -11.890 1.00 43.73 ? 403 HOH   B O   1 
HETATM 7906 O O   . HOH   Q 5 .   ? -16.100 -0.111  16.095  1.00 42.96 ? 404 HOH   B O   1 
HETATM 7907 O O   . HOH   Q 5 .   ? -8.400  29.648  0.744   1.00 32.76 ? 405 HOH   B O   1 
HETATM 7908 O O   . HOH   Q 5 .   ? -8.017  7.620   17.210  1.00 41.79 ? 406 HOH   B O   1 
HETATM 7909 O O   . HOH   Q 5 .   ? -22.728 -13.432 9.430   1.00 23.55 ? 407 HOH   B O   1 
HETATM 7910 O O   . HOH   Q 5 .   ? -5.657  6.369   13.907  1.00 34.69 ? 408 HOH   B O   1 
HETATM 7911 O O   . HOH   Q 5 .   ? -3.386  8.876   -7.590  1.00 56.75 ? 409 HOH   B O   1 
HETATM 7912 O O   . HOH   Q 5 .   ? -22.231 4.792   -25.072 1.00 33.00 ? 410 HOH   B O   1 
HETATM 7913 O O   . HOH   Q 5 .   ? -13.086 -4.487  -19.649 1.00 45.80 ? 411 HOH   B O   1 
HETATM 7914 O O   . HOH   Q 5 .   ? -11.664 -12.971 4.031   1.00 20.98 ? 412 HOH   B O   1 
HETATM 7915 O O   . HOH   Q 5 .   ? -4.311  12.664  -6.788  1.00 30.93 ? 413 HOH   B O   1 
HETATM 7916 O O   . HOH   Q 5 .   ? -33.128 4.995   -12.962 1.00 34.89 ? 414 HOH   B O   1 
HETATM 7917 O O   . HOH   Q 5 .   ? -22.374 1.955   1.691   1.00 28.05 ? 415 HOH   B O   1 
HETATM 7918 O O   . HOH   Q 5 .   ? -10.017 14.367  -6.715  1.00 39.59 ? 416 HOH   B O   1 
HETATM 7919 O O   . HOH   Q 5 .   ? -30.804 3.622   -14.142 1.00 26.10 ? 417 HOH   B O   1 
HETATM 7920 O O   . HOH   Q 5 .   ? -35.300 0.981   0.741   1.00 27.55 ? 418 HOH   B O   1 
HETATM 7921 O O   . HOH   Q 5 .   ? -8.159  13.996  17.946  1.00 37.17 ? 419 HOH   B O   1 
HETATM 7922 O O   . HOH   Q 5 .   ? -34.381 0.323   -1.877  1.00 32.57 ? 420 HOH   B O   1 
HETATM 7923 O O   . HOH   Q 5 .   ? -15.500 -3.855  -24.946 1.00 50.86 ? 421 HOH   B O   1 
HETATM 7924 O O   . HOH   Q 5 .   ? -14.570 8.143   -23.217 1.00 47.40 ? 422 HOH   B O   1 
HETATM 7925 O O   . HOH   Q 5 .   ? -28.351 10.122  -2.346  1.00 40.15 ? 423 HOH   B O   1 
HETATM 7926 O O   . HOH   Q 5 .   ? -18.638 8.985   -3.842  1.00 26.85 ? 424 HOH   B O   1 
HETATM 7927 O O   . HOH   Q 5 .   ? -16.955 -16.839 -8.068  1.00 40.48 ? 425 HOH   B O   1 
HETATM 7928 O O   . HOH   Q 5 .   ? -40.981 9.533   15.767  1.00 50.73 ? 426 HOH   B O   1 
HETATM 7929 O O   . HOH   Q 5 .   ? -7.258  13.668  5.979   1.00 25.56 ? 427 HOH   B O   1 
HETATM 7930 O O   . HOH   Q 5 .   ? -10.035 -8.441  -5.514  1.00 30.03 ? 428 HOH   B O   1 
HETATM 7931 O O   . HOH   Q 5 .   ? -8.968  5.617   12.505  1.00 41.92 ? 429 HOH   B O   1 
HETATM 7932 O O   . HOH   Q 5 .   ? -13.315 11.660  8.520   1.00 40.56 ? 430 HOH   B O   1 
HETATM 7933 O O   . HOH   Q 5 .   ? -9.026  -15.172 -20.715 1.00 63.80 ? 431 HOH   B O   1 
HETATM 7934 O O   . HOH   Q 5 .   ? -0.664  15.559  1.143   1.00 34.60 ? 432 HOH   B O   1 
HETATM 7935 O O   . HOH   Q 5 .   ? -34.079 -4.035  6.066   1.00 34.69 ? 433 HOH   B O   1 
HETATM 7936 O O   . HOH   Q 5 .   ? -11.183 23.798  -3.177  1.00 34.94 ? 434 HOH   B O   1 
HETATM 7937 O O   . HOH   Q 5 .   ? -15.787 -14.287 -10.838 1.00 31.46 ? 435 HOH   B O   1 
HETATM 7938 O O   . HOH   Q 5 .   ? -14.647 15.113  18.374  1.00 30.04 ? 436 HOH   B O   1 
HETATM 7939 O O   . HOH   Q 5 .   ? -12.851 -18.521 8.724   1.00 38.97 ? 437 HOH   B O   1 
HETATM 7940 O O   . HOH   Q 5 .   ? -10.784 -9.281  -9.161  1.00 33.72 ? 438 HOH   B O   1 
HETATM 7941 O O   . HOH   Q 5 .   ? -7.935  14.930  14.793  1.00 35.02 ? 439 HOH   B O   1 
HETATM 7942 O O   . HOH   Q 5 .   ? -17.479 1.845   -27.756 1.00 36.33 ? 440 HOH   B O   1 
HETATM 7943 O O   . HOH   Q 5 .   ? -11.934 19.206  -1.955  1.00 45.14 ? 441 HOH   B O   1 
HETATM 7944 O O   . HOH   Q 5 .   ? -22.869 0.165   -0.514  1.00 18.29 ? 442 HOH   B O   1 
HETATM 7945 O O   . HOH   Q 5 .   ? -9.090  5.445   15.894  1.00 48.58 ? 443 HOH   B O   1 
HETATM 7946 O O   . HOH   Q 5 .   ? -9.882  29.810  7.061   1.00 43.24 ? 444 HOH   B O   1 
HETATM 7947 O O   . HOH   Q 5 .   ? -9.299  -12.567 -3.212  1.00 32.05 ? 445 HOH   B O   1 
HETATM 7948 O O   . HOH   Q 5 .   ? -8.905  11.441  3.367   1.00 32.34 ? 446 HOH   B O   1 
HETATM 7949 O O   . HOH   Q 5 .   ? -10.698 7.841   14.801  1.00 25.58 ? 447 HOH   B O   1 
HETATM 7950 O O   . HOH   Q 5 .   ? -21.029 12.104  16.780  1.00 25.46 ? 448 HOH   B O   1 
HETATM 7951 O O   . HOH   Q 5 .   ? -13.134 31.937  1.143   1.00 27.58 ? 449 HOH   B O   1 
HETATM 7952 O O   . HOH   Q 5 .   ? -18.861 26.847  4.030   1.00 46.00 ? 450 HOH   B O   1 
HETATM 7953 O O   . HOH   Q 5 .   ? -34.181 -8.299  -6.282  1.00 36.84 ? 451 HOH   B O   1 
HETATM 7954 O O   . HOH   Q 5 .   ? -17.886 -19.493 6.752   1.00 45.53 ? 452 HOH   B O   1 
HETATM 7955 O O   . HOH   Q 5 .   ? -13.284 3.451   10.272  1.00 33.47 ? 453 HOH   B O   1 
HETATM 7956 O O   . HOH   Q 5 .   ? -2.759  1.341   -5.962  1.00 29.14 ? 454 HOH   B O   1 
HETATM 7957 O O   . HOH   Q 5 .   ? -2.996  8.437   10.387  1.00 21.20 ? 455 HOH   B O   1 
HETATM 7958 O O   . HOH   Q 5 .   ? -10.800 8.269   20.718  1.00 28.89 ? 456 HOH   B O   1 
HETATM 7959 O O   . HOH   Q 5 .   ? -3.916  15.537  -1.612  1.00 44.48 ? 457 HOH   B O   1 
HETATM 7960 O O   . HOH   Q 5 .   ? -4.735  1.676   8.670   1.00 24.11 ? 458 HOH   B O   1 
HETATM 7961 O O   . HOH   Q 5 .   ? 0.341   -7.672  0.833   1.00 19.27 ? 459 HOH   B O   1 
HETATM 7962 O O   . HOH   Q 5 .   ? -9.469  -4.698  11.562  1.00 32.82 ? 460 HOH   B O   1 
HETATM 7963 O O   . HOH   Q 5 .   ? -3.116  7.723   6.533   1.00 21.48 ? 461 HOH   B O   1 
HETATM 7964 O O   . HOH   Q 5 .   ? -3.773  -7.723  -9.623  1.00 39.69 ? 462 HOH   B O   1 
HETATM 7965 O O   . HOH   Q 5 .   ? -9.333  -19.623 1.696   1.00 37.88 ? 463 HOH   B O   1 
HETATM 7966 O O   . HOH   Q 5 .   ? -1.727  8.136   -4.024  1.00 30.92 ? 464 HOH   B O   1 
HETATM 7967 O O   . HOH   Q 5 .   ? -36.756 -6.917  0.175   1.00 33.37 ? 465 HOH   B O   1 
HETATM 7968 O O   . HOH   Q 5 .   ? -8.287  27.945  -1.335  1.00 28.63 ? 466 HOH   B O   1 
HETATM 7969 O O   . HOH   Q 5 .   ? -18.228 -13.935 -9.960  1.00 32.60 ? 467 HOH   B O   1 
HETATM 7970 O O   . HOH   Q 5 .   ? -31.963 14.376  15.463  1.00 41.76 ? 468 HOH   B O   1 
HETATM 7971 O O   . HOH   Q 5 .   ? -13.850 11.816  -9.188  1.00 40.15 ? 469 HOH   B O   1 
HETATM 7972 O O   . HOH   Q 5 .   ? -7.886  7.575   -12.524 1.00 38.87 ? 470 HOH   B O   1 
HETATM 7973 O O   . HOH   Q 5 .   ? -39.038 12.516  14.488  1.00 45.92 ? 471 HOH   B O   1 
HETATM 7974 O O   . HOH   Q 5 .   ? -6.502  -14.322 -2.072  1.00 48.40 ? 472 HOH   B O   1 
HETATM 7975 O O   . HOH   Q 5 .   ? -22.863 0.706   -24.774 1.00 43.82 ? 473 HOH   B O   1 
HETATM 7976 O O   . HOH   Q 5 .   ? -23.791 8.124   -6.953  1.00 26.68 ? 474 HOH   B O   1 
HETATM 7977 O O   . HOH   Q 5 .   ? -29.483 0.260   -16.563 1.00 25.05 ? 475 HOH   B O   1 
HETATM 7978 O O   . HOH   Q 5 .   ? -25.951 12.750  2.769   1.00 29.17 ? 476 HOH   B O   1 
HETATM 7979 O O   . HOH   Q 5 .   ? -18.521 -6.605  3.740   1.00 20.57 ? 477 HOH   B O   1 
HETATM 7980 O O   . HOH   Q 5 .   ? -17.398 14.549  -8.901  1.00 45.68 ? 478 HOH   B O   1 
HETATM 7981 O O   . HOH   Q 5 .   ? -19.323 -10.784 -21.025 1.00 51.41 ? 479 HOH   B O   1 
HETATM 7982 O O   . HOH   Q 5 .   ? -29.953 -8.712  -0.288  1.00 35.49 ? 480 HOH   B O   1 
HETATM 7983 O O   . HOH   Q 5 .   ? -23.896 12.265  1.170   1.00 51.36 ? 481 HOH   B O   1 
HETATM 7984 O O   . HOH   Q 5 .   ? -19.079 -13.722 10.588  1.00 29.99 ? 482 HOH   B O   1 
HETATM 7985 O O   . HOH   Q 5 .   ? -10.767 3.717   -18.918 1.00 51.01 ? 483 HOH   B O   1 
HETATM 7986 O O   . HOH   Q 5 .   ? -10.530 -6.252  -0.366  1.00 24.22 ? 484 HOH   B O   1 
HETATM 7987 O O   . HOH   Q 5 .   ? -20.594 10.474  3.078   1.00 50.14 ? 485 HOH   B O   1 
HETATM 7988 O O   . HOH   Q 5 .   ? -7.047  -6.138  -9.613  1.00 32.58 ? 486 HOH   B O   1 
HETATM 7989 O O   . HOH   Q 5 .   ? -10.758 -15.430 -4.726  1.00 41.11 ? 487 HOH   B O   1 
HETATM 7990 O O   . HOH   Q 5 .   ? -11.038 10.064  -11.433 1.00 38.34 ? 488 HOH   B O   1 
HETATM 7991 O O   . HOH   Q 5 .   ? -0.738  -10.023 0.260   1.00 24.47 ? 489 HOH   B O   1 
HETATM 7992 O O   . HOH   Q 5 .   ? -7.205  -2.774  10.372  1.00 25.92 ? 490 HOH   B O   1 
HETATM 7993 O O   . HOH   Q 5 .   ? -2.373  19.633  12.780  1.00 39.74 ? 491 HOH   B O   1 
HETATM 7994 O O   . HOH   Q 5 .   ? -25.430 11.546  12.121  1.00 20.84 ? 492 HOH   B O   1 
HETATM 7995 O O   . HOH   Q 5 .   ? -34.790 2.278   -5.381  1.00 31.61 ? 493 HOH   B O   1 
HETATM 7996 O O   . HOH   Q 5 .   ? -40.750 -2.274  2.722   1.00 55.58 ? 494 HOH   B O   1 
HETATM 7997 O O   . HOH   Q 5 .   ? -27.133 0.192   -17.752 1.00 29.87 ? 495 HOH   B O   1 
HETATM 7998 O O   . HOH   Q 5 .   ? -9.818  7.937   -10.869 1.00 31.45 ? 496 HOH   B O   1 
HETATM 7999 O O   . HOH   Q 5 .   ? -6.159  -3.959  -8.765  1.00 31.20 ? 497 HOH   B O   1 
HETATM 8000 O O   . HOH   Q 5 .   ? -21.904 11.737  -21.943 1.00 44.68 ? 498 HOH   B O   1 
HETATM 8001 O O   . HOH   Q 5 .   ? -15.595 3.355   9.637   1.00 40.20 ? 499 HOH   B O   1 
HETATM 8002 O O   . HOH   Q 5 .   ? -30.454 -2.253  -13.426 1.00 34.11 ? 500 HOH   B O   1 
HETATM 8003 O O   . HOH   Q 5 .   ? -20.083 3.311   3.116   1.00 42.05 ? 501 HOH   B O   1 
HETATM 8004 O O   A HOH   Q 5 .   ? -40.251 -0.596  5.523   0.60 29.65 ? 502 HOH   B O   1 
HETATM 8005 O O   B HOH   Q 5 .   ? -39.780 -0.372  6.994   0.40 24.17 ? 502 HOH   B O   1 
HETATM 8006 O O   . HOH   Q 5 .   ? -26.485 14.139  -11.854 1.00 34.77 ? 503 HOH   B O   1 
HETATM 8007 O O   . HOH   Q 5 .   ? -29.656 13.958  -12.512 1.00 41.77 ? 504 HOH   B O   1 
HETATM 8008 O O   . HOH   Q 5 .   ? -17.891 11.931  11.946  1.00 31.85 ? 505 HOH   B O   1 
HETATM 8009 O O   . HOH   Q 5 .   ? -18.440 11.329  4.818   1.00 50.32 ? 506 HOH   B O   1 
HETATM 8010 O O   . HOH   Q 5 .   ? -24.287 -1.274  -21.548 1.00 37.34 ? 507 HOH   B O   1 
HETATM 8011 O O   . HOH   Q 5 .   ? -3.889  -0.744  -11.457 1.00 44.16 ? 508 HOH   B O   1 
HETATM 8012 O O   . HOH   Q 5 .   ? -7.597  1.741   10.672  1.00 40.50 ? 509 HOH   B O   1 
HETATM 8013 O O   . HOH   Q 5 .   ? -0.774  6.903   -7.983  1.00 50.19 ? 510 HOH   B O   1 
HETATM 8014 O O   . HOH   Q 5 .   ? -30.683 -11.023 -0.429  1.00 47.35 ? 511 HOH   B O   1 
HETATM 8015 O O   . HOH   Q 5 .   ? -10.729 6.413   -18.756 1.00 46.21 ? 512 HOH   B O   1 
HETATM 8016 O O   . HOH   Q 5 .   ? -24.921 16.298  -11.753 1.00 54.96 ? 513 HOH   B O   1 
HETATM 8017 O O   . HOH   Q 5 .   ? -13.480 19.978  -4.103  1.00 50.22 ? 514 HOH   B O   1 
HETATM 8018 O O   . HOH   Q 5 .   ? -15.152 -20.575 -9.147  1.00 52.01 ? 515 HOH   B O   1 
HETATM 8019 O O   . HOH   Q 5 .   ? -13.704 9.349   -18.013 1.00 48.01 ? 516 HOH   B O   1 
HETATM 8020 O O   . HOH   Q 5 .   ? -10.485 31.594  1.785   1.00 35.29 ? 517 HOH   B O   1 
HETATM 8021 O O   . HOH   Q 5 .   ? -15.972 -15.868 -13.298 1.00 42.84 ? 518 HOH   B O   1 
HETATM 8022 O O   . HOH   Q 5 .   ? -4.017  9.695   -10.140 1.00 47.89 ? 519 HOH   B O   1 
HETATM 8023 O O   . HOH   Q 5 .   ? -28.434 12.338  -1.181  1.00 48.31 ? 520 HOH   B O   1 
HETATM 8024 O O   . HOH   Q 5 .   ? -13.374 21.647  12.469  1.00 61.87 ? 521 HOH   B O   1 
HETATM 8025 O O   . HOH   Q 5 .   ? -19.083 -15.354 -18.457 1.00 62.30 ? 522 HOH   B O   1 
HETATM 8026 O O   . HOH   Q 5 .   ? -11.507 -21.331 -1.836  1.00 64.84 ? 523 HOH   B O   1 
HETATM 8027 O O   . HOH   Q 5 .   ? -24.090 17.739  6.186   1.00 57.77 ? 524 HOH   B O   1 
HETATM 8028 O O   . HOH   Q 5 .   ? -34.053 -0.897  -6.973  1.00 33.29 ? 525 HOH   B O   1 
HETATM 8029 O O   . HOH   Q 5 .   ? -33.403 10.270  -0.090  1.00 63.13 ? 526 HOH   B O   1 
HETATM 8030 O O   . HOH   Q 5 .   ? -21.425 -19.741 -1.535  1.00 55.14 ? 527 HOH   B O   1 
HETATM 8031 O O   . HOH   Q 5 .   ? -21.067 16.962  -2.011  1.00 48.68 ? 528 HOH   B O   1 
HETATM 8032 O O   . HOH   Q 5 .   ? -0.735  17.466  17.072  1.00 32.51 ? 529 HOH   B O   1 
HETATM 8033 O O   . HOH   Q 5 .   ? -22.795 -11.993 -20.207 1.00 50.35 ? 530 HOH   B O   1 
HETATM 8034 O O   . HOH   Q 5 .   ? -7.254  -7.138  -13.402 1.00 48.52 ? 531 HOH   B O   1 
HETATM 8035 O O   . HOH   Q 5 .   ? -18.767 13.709  3.439   1.00 55.36 ? 532 HOH   B O   1 
HETATM 8036 O O   . HOH   Q 5 .   ? -26.373 -18.333 -7.788  1.00 50.55 ? 533 HOH   B O   1 
HETATM 8037 O O   A HOH   Q 5 .   ? -1.389  -0.957  -5.900  0.60 25.03 ? 534 HOH   B O   1 
HETATM 8038 O O   B HOH   Q 5 .   ? -1.184  -2.709  -6.223  0.40 27.19 ? 534 HOH   B O   1 
HETATM 8039 O O   . HOH   Q 5 .   ? -7.277  4.870   14.180  1.00 38.34 ? 535 HOH   B O   1 
HETATM 8040 O O   . HOH   Q 5 .   ? -9.311  22.887  -5.237  1.00 42.98 ? 536 HOH   B O   1 
HETATM 8041 O O   . HOH   Q 5 .   ? -9.671  3.630   10.884  1.00 34.81 ? 537 HOH   B O   1 
HETATM 8042 O O   . HOH   Q 5 .   ? -16.953 13.184  6.055   1.00 52.34 ? 538 HOH   B O   1 
HETATM 8043 O O   . HOH   Q 5 .   ? -3.901  -3.200  -9.866  1.00 42.07 ? 539 HOH   B O   1 
HETATM 8044 O O   . HOH   Q 5 .   ? -15.681 17.381  6.738   1.00 57.76 ? 540 HOH   B O   1 
HETATM 8045 O O   A HOH   Q 5 .   ? -28.001 18.938  -20.308 0.50 29.46 ? 541 HOH   B O   1 
HETATM 8046 O O   . HOH   Q 5 .   ? -28.750 16.236  3.992   1.00 49.22 ? 542 HOH   B O   1 
HETATM 8047 O O   . HOH   Q 5 .   ? -11.591 1.969   11.913  1.00 44.73 ? 543 HOH   B O   1 
HETATM 8048 O O   . HOH   Q 5 .   ? -8.172  -18.299 -3.046  1.00 51.78 ? 544 HOH   B O   1 
HETATM 8049 O O   . HOH   Q 5 .   ? -15.422 -24.310 -1.653  1.00 54.43 ? 545 HOH   B O   1 
HETATM 8050 O O   . HOH   Q 5 .   ? -28.973 20.626  9.998   1.00 49.75 ? 546 HOH   B O   1 
HETATM 8051 O O   . HOH   R 5 .   ? 17.965  2.623   44.707  1.00 41.54 ? 401 HOH   C O   1 
HETATM 8052 O O   . HOH   R 5 .   ? 3.180   -2.443  59.882  1.00 34.46 ? 402 HOH   C O   1 
HETATM 8053 O O   . HOH   R 5 .   ? -0.145  0.160   21.766  1.00 38.74 ? 403 HOH   C O   1 
HETATM 8054 O O   . HOH   R 5 .   ? 6.454   -12.479 29.689  1.00 22.05 ? 404 HOH   C O   1 
HETATM 8055 O O   . HOH   R 5 .   ? 1.511   -17.991 33.273  1.00 44.87 ? 405 HOH   C O   1 
HETATM 8056 O O   . HOH   R 5 .   ? 9.639   13.077  19.024  1.00 22.76 ? 406 HOH   C O   1 
HETATM 8057 O O   . HOH   R 5 .   ? 1.153   -14.131 46.947  1.00 49.05 ? 407 HOH   C O   1 
HETATM 8058 O O   . HOH   R 5 .   ? 5.942   -16.964 33.569  1.00 55.94 ? 408 HOH   C O   1 
HETATM 8059 O O   . HOH   R 5 .   ? -3.624  20.826  37.340  1.00 53.08 ? 409 HOH   C O   1 
HETATM 8060 O O   . HOH   R 5 .   ? 3.689   14.744  50.089  1.00 44.65 ? 410 HOH   C O   1 
HETATM 8061 O O   . HOH   R 5 .   ? 6.034   3.754   36.003  1.00 25.72 ? 411 HOH   C O   1 
HETATM 8062 O O   . HOH   R 5 .   ? 5.348   11.970  42.885  1.00 38.21 ? 412 HOH   C O   1 
HETATM 8063 O O   . HOH   R 5 .   ? -1.224  0.704   63.233  1.00 43.85 ? 413 HOH   C O   1 
HETATM 8064 O O   . HOH   R 5 .   ? 2.508   11.337  40.736  1.00 26.09 ? 414 HOH   C O   1 
HETATM 8065 O O   . HOH   R 5 .   ? 18.970  2.821   36.874  1.00 30.47 ? 415 HOH   C O   1 
HETATM 8066 O O   . HOH   R 5 .   ? -1.485  15.032  17.934  1.00 23.38 ? 416 HOH   C O   1 
HETATM 8067 O O   . HOH   R 5 .   ? 6.076   15.615  39.799  1.00 36.65 ? 417 HOH   C O   1 
HETATM 8068 O O   . HOH   R 5 .   ? -6.814  -10.079 42.283  1.00 29.36 ? 418 HOH   C O   1 
HETATM 8069 O O   . HOH   R 5 .   ? -15.685 17.573  34.937  1.00 34.62 ? 419 HOH   C O   1 
HETATM 8070 O O   . HOH   R 5 .   ? 18.283  2.328   39.418  1.00 25.54 ? 420 HOH   C O   1 
HETATM 8071 O O   . HOH   R 5 .   ? -4.508  -11.484 35.123  1.00 21.54 ? 421 HOH   C O   1 
HETATM 8072 O O   . HOH   R 5 .   ? -0.405  -11.305 50.098  1.00 28.86 ? 422 HOH   C O   1 
HETATM 8073 O O   . HOH   R 5 .   ? 19.189  9.794   34.094  1.00 45.81 ? 423 HOH   C O   1 
HETATM 8074 O O   . HOH   R 5 .   ? 12.259  12.315  39.279  1.00 33.02 ? 424 HOH   C O   1 
HETATM 8075 O O   . HOH   R 5 .   ? -2.102  14.724  45.421  1.00 28.26 ? 425 HOH   C O   1 
HETATM 8076 O O   . HOH   R 5 .   ? 6.606   2.158   38.238  1.00 22.64 ? 426 HOH   C O   1 
HETATM 8077 O O   . HOH   R 5 .   ? 18.772  -6.651  53.917  1.00 50.16 ? 427 HOH   C O   1 
HETATM 8078 O O   A HOH   R 5 .   ? 13.228  -10.343 41.424  0.50 26.11 ? 428 HOH   C O   1 
HETATM 8079 O O   . HOH   R 5 .   ? 13.888  2.998   52.223  1.00 24.53 ? 429 HOH   C O   1 
HETATM 8080 O O   . HOH   R 5 .   ? -5.384  8.153   16.336  1.00 31.84 ? 430 HOH   C O   1 
HETATM 8081 O O   . HOH   R 5 .   ? 9.758   -5.148  59.662  1.00 26.73 ? 431 HOH   C O   1 
HETATM 8082 O O   . HOH   R 5 .   ? -15.749 -3.263  46.480  1.00 46.02 ? 432 HOH   C O   1 
HETATM 8083 O O   . HOH   R 5 .   ? 3.993   10.002  61.989  1.00 41.64 ? 433 HOH   C O   1 
HETATM 8084 O O   . HOH   R 5 .   ? 12.282  12.495  35.379  1.00 49.70 ? 434 HOH   C O   1 
HETATM 8085 O O   . HOH   R 5 .   ? -13.875 13.089  48.519  1.00 35.41 ? 435 HOH   C O   1 
HETATM 8086 O O   . HOH   R 5 .   ? 3.806   15.226  57.867  1.00 42.96 ? 436 HOH   C O   1 
HETATM 8087 O O   . HOH   R 5 .   ? -2.984  4.280   27.212  1.00 36.03 ? 437 HOH   C O   1 
HETATM 8088 O O   . HOH   R 5 .   ? -5.383  7.463   55.896  1.00 34.99 ? 438 HOH   C O   1 
HETATM 8089 O O   . HOH   R 5 .   ? 4.792   12.171  19.923  1.00 23.52 ? 439 HOH   C O   1 
HETATM 8090 O O   . HOH   R 5 .   ? -4.064  11.783  55.755  1.00 49.65 ? 440 HOH   C O   1 
HETATM 8091 O O   . HOH   R 5 .   ? -5.472  8.233   22.281  1.00 21.68 ? 441 HOH   C O   1 
HETATM 8092 O O   . HOH   R 5 .   ? -5.932  -5.833  44.108  1.00 29.09 ? 442 HOH   C O   1 
HETATM 8093 O O   . HOH   R 5 .   ? -8.896  15.138  30.436  1.00 25.09 ? 443 HOH   C O   1 
HETATM 8094 O O   . HOH   R 5 .   ? -8.226  14.974  21.321  1.00 28.96 ? 444 HOH   C O   1 
HETATM 8095 O O   . HOH   R 5 .   ? -3.278  -0.591  57.589  1.00 44.80 ? 445 HOH   C O   1 
HETATM 8096 O O   . HOH   R 5 .   ? -13.294 9.310   26.567  1.00 23.07 ? 446 HOH   C O   1 
HETATM 8097 O O   . HOH   R 5 .   ? -2.351  12.587  59.665  1.00 38.54 ? 447 HOH   C O   1 
HETATM 8098 O O   . HOH   R 5 .   ? -6.802  -17.865 37.789  1.00 42.35 ? 448 HOH   C O   1 
HETATM 8099 O O   . HOH   R 5 .   ? -3.686  25.603  38.053  1.00 50.36 ? 449 HOH   C O   1 
HETATM 8100 O O   . HOH   R 5 .   ? 7.631   10.769  44.043  1.00 27.41 ? 450 HOH   C O   1 
HETATM 8101 O O   . HOH   R 5 .   ? 15.927  14.391  20.988  1.00 37.54 ? 451 HOH   C O   1 
HETATM 8102 O O   . HOH   R 5 .   ? -18.681 -11.425 43.170  1.00 45.51 ? 452 HOH   C O   1 
HETATM 8103 O O   . HOH   R 5 .   ? 13.985  -12.908 51.049  1.00 52.46 ? 453 HOH   C O   1 
HETATM 8104 O O   . HOH   R 5 .   ? 7.781   13.668  35.610  1.00 41.89 ? 454 HOH   C O   1 
HETATM 8105 O O   . HOH   R 5 .   ? -5.266  -6.530  48.041  1.00 34.04 ? 455 HOH   C O   1 
HETATM 8106 O O   . HOH   R 5 .   ? -13.292 5.692   45.285  1.00 41.77 ? 456 HOH   C O   1 
HETATM 8107 O O   B HOH   R 5 .   ? 1.606   7.276   19.364  0.50 24.46 ? 457 HOH   C O   1 
HETATM 8108 O O   . HOH   R 5 .   ? -12.298 17.729  37.737  1.00 40.35 ? 458 HOH   C O   1 
HETATM 8109 O O   . HOH   R 5 .   ? -13.909 20.248  23.173  1.00 44.85 ? 459 HOH   C O   1 
HETATM 8110 O O   . HOH   R 5 .   ? -13.457 3.924   43.466  1.00 32.03 ? 460 HOH   C O   1 
HETATM 8111 O O   . HOH   R 5 .   ? -7.322  6.125   24.772  1.00 40.46 ? 461 HOH   C O   1 
HETATM 8112 O O   . HOH   R 5 .   ? 13.614  -6.980  38.925  1.00 39.45 ? 462 HOH   C O   1 
HETATM 8113 O O   . HOH   R 5 .   ? 1.083   17.062  45.325  1.00 38.36 ? 463 HOH   C O   1 
HETATM 8114 O O   . HOH   R 5 .   ? 22.584  13.059  21.940  1.00 38.41 ? 464 HOH   C O   1 
HETATM 8115 O O   . HOH   R 5 .   ? 2.331   -10.859 49.406  1.00 31.83 ? 465 HOH   C O   1 
HETATM 8116 O O   . HOH   R 5 .   ? 20.609  -5.199  38.087  1.00 31.46 ? 466 HOH   C O   1 
HETATM 8117 O O   . HOH   R 5 .   ? 6.138   -2.033  59.516  1.00 36.49 ? 467 HOH   C O   1 
HETATM 8118 O O   . HOH   R 5 .   ? -13.107 8.922   30.437  1.00 20.96 ? 468 HOH   C O   1 
HETATM 8119 O O   . HOH   R 5 .   ? -8.199  7.616   19.791  1.00 42.93 ? 469 HOH   C O   1 
HETATM 8120 O O   . HOH   R 5 .   ? -5.472  -12.578 43.965  1.00 32.24 ? 470 HOH   C O   1 
HETATM 8121 O O   . HOH   R 5 .   ? -8.954  -3.301  47.972  1.00 35.94 ? 471 HOH   C O   1 
HETATM 8122 O O   . HOH   R 5 .   ? 1.046   18.541  19.499  1.00 52.02 ? 472 HOH   C O   1 
HETATM 8123 O O   . HOH   R 5 .   ? 11.399  0.293   54.890  1.00 29.38 ? 473 HOH   C O   1 
HETATM 8124 O O   . HOH   R 5 .   ? -14.568 10.564  40.799  1.00 30.39 ? 474 HOH   C O   1 
HETATM 8125 O O   . HOH   R 5 .   ? -4.584  -9.795  49.128  1.00 40.30 ? 475 HOH   C O   1 
HETATM 8126 O O   . HOH   R 5 .   ? -7.358  13.017  33.367  1.00 32.65 ? 476 HOH   C O   1 
HETATM 8127 O O   . HOH   R 5 .   ? 2.860   -12.845 28.587  1.00 25.10 ? 477 HOH   C O   1 
HETATM 8128 O O   . HOH   R 5 .   ? 17.692  -2.801  32.207  1.00 34.44 ? 478 HOH   C O   1 
HETATM 8129 O O   . HOH   R 5 .   ? -5.906  17.081  42.690  1.00 34.52 ? 479 HOH   C O   1 
HETATM 8130 O O   . HOH   R 5 .   ? 4.733   16.839  36.000  1.00 48.11 ? 480 HOH   C O   1 
HETATM 8131 O O   . HOH   R 5 .   ? 6.137   2.619   59.216  1.00 26.55 ? 481 HOH   C O   1 
HETATM 8132 O O   . HOH   R 5 .   ? -5.729  -4.194  38.777  1.00 22.03 ? 482 HOH   C O   1 
HETATM 8133 O O   . HOH   R 5 .   ? 9.308   12.174  24.575  1.00 21.75 ? 483 HOH   C O   1 
HETATM 8134 O O   . HOH   R 5 .   ? 17.362  11.963  36.113  1.00 52.15 ? 484 HOH   C O   1 
HETATM 8135 O O   . HOH   R 5 .   ? -6.441  10.929  47.402  1.00 35.40 ? 485 HOH   C O   1 
HETATM 8136 O O   . HOH   R 5 .   ? -6.940  -3.863  26.659  1.00 38.77 ? 486 HOH   C O   1 
HETATM 8137 O O   . HOH   R 5 .   ? 9.809   14.288  33.772  1.00 37.18 ? 487 HOH   C O   1 
HETATM 8138 O O   . HOH   R 5 .   ? -0.365  4.108   28.002  1.00 37.35 ? 488 HOH   C O   1 
HETATM 8139 O O   . HOH   R 5 .   ? -9.066  -1.862  27.765  1.00 30.01 ? 489 HOH   C O   1 
HETATM 8140 O O   . HOH   R 5 .   ? 6.045   8.129   60.681  1.00 40.20 ? 490 HOH   C O   1 
HETATM 8141 O O   . HOH   R 5 .   ? 20.421  -0.861  42.354  1.00 39.81 ? 491 HOH   C O   1 
HETATM 8142 O O   . HOH   R 5 .   ? 18.560  4.489   42.708  1.00 41.07 ? 492 HOH   C O   1 
HETATM 8143 O O   . HOH   R 5 .   ? -15.553 -8.065  38.607  1.00 25.79 ? 493 HOH   C O   1 
HETATM 8144 O O   . HOH   R 5 .   ? 18.902  -1.626  27.912  1.00 25.31 ? 494 HOH   C O   1 
HETATM 8145 O O   . HOH   R 5 .   ? 10.342  16.910  48.295  1.00 30.90 ? 495 HOH   C O   1 
HETATM 8146 O O   . HOH   R 5 .   ? 11.847  15.517  40.717  1.00 47.98 ? 496 HOH   C O   1 
HETATM 8147 O O   . HOH   R 5 .   ? -11.606 2.846   28.869  1.00 25.40 ? 497 HOH   C O   1 
HETATM 8148 O O   . HOH   R 5 .   ? 2.238   -4.976  34.690  1.00 21.01 ? 498 HOH   C O   1 
HETATM 8149 O O   . HOH   R 5 .   ? 2.557   -2.125  64.556  1.00 43.02 ? 499 HOH   C O   1 
HETATM 8150 O O   . HOH   R 5 .   ? -7.338  15.456  44.488  1.00 31.60 ? 500 HOH   C O   1 
HETATM 8151 O O   . HOH   R 5 .   ? 16.784  3.628   48.965  1.00 34.26 ? 501 HOH   C O   1 
HETATM 8152 O O   . HOH   R 5 .   ? 18.664  11.796  42.796  1.00 50.78 ? 502 HOH   C O   1 
HETATM 8153 O O   . HOH   R 5 .   ? 2.242   -9.817  56.968  1.00 45.13 ? 503 HOH   C O   1 
HETATM 8154 O O   . HOH   R 5 .   ? 3.715   5.027   34.572  1.00 37.37 ? 504 HOH   C O   1 
HETATM 8155 O O   . HOH   R 5 .   ? -2.463  3.750   65.167  1.00 43.87 ? 505 HOH   C O   1 
HETATM 8156 O O   . HOH   R 5 .   ? -5.303  -10.147 54.202  1.00 53.83 ? 506 HOH   C O   1 
HETATM 8157 O O   . HOH   R 5 .   ? 8.987   -11.693 53.922  1.00 44.92 ? 507 HOH   C O   1 
HETATM 8158 O O   . HOH   R 5 .   ? -13.164 19.641  17.919  1.00 46.50 ? 508 HOH   C O   1 
HETATM 8159 O O   . HOH   R 5 .   ? -9.737  -0.944  46.906  1.00 40.49 ? 509 HOH   C O   1 
HETATM 8160 O O   . HOH   R 5 .   ? -8.562  2.577   27.078  1.00 39.76 ? 510 HOH   C O   1 
HETATM 8161 O O   . HOH   R 5 .   ? 23.955  0.542   31.876  1.00 37.09 ? 511 HOH   C O   1 
HETATM 8162 O O   . HOH   R 5 .   ? -15.309 13.085  41.724  1.00 43.12 ? 512 HOH   C O   1 
HETATM 8163 O O   . HOH   R 5 .   ? 5.047   18.836  37.218  1.00 47.38 ? 513 HOH   C O   1 
HETATM 8164 O O   . HOH   R 5 .   ? 7.359   -18.181 42.585  1.00 56.55 ? 514 HOH   C O   1 
HETATM 8165 O O   . HOH   R 5 .   ? 13.421  17.032  48.842  1.00 40.42 ? 515 HOH   C O   1 
HETATM 8166 O O   . HOH   R 5 .   ? 1.560   12.500  24.886  1.00 27.41 ? 516 HOH   C O   1 
HETATM 8167 O O   . HOH   R 5 .   ? 3.454   28.446  36.962  1.00 54.07 ? 517 HOH   C O   1 
HETATM 8168 O O   . HOH   R 5 .   ? -0.794  28.466  39.959  1.00 48.48 ? 518 HOH   C O   1 
HETATM 8169 O O   . HOH   R 5 .   ? 7.475   18.691  29.605  1.00 51.52 ? 519 HOH   C O   1 
HETATM 8170 O O   . HOH   R 5 .   ? -0.238  -1.901  61.383  1.00 49.44 ? 520 HOH   C O   1 
HETATM 8171 O O   . HOH   R 5 .   ? 13.934  14.007  53.715  1.00 44.33 ? 521 HOH   C O   1 
HETATM 8172 O O   . HOH   R 5 .   ? -5.752  -1.278  24.272  1.00 44.57 ? 522 HOH   C O   1 
HETATM 8173 O O   . HOH   R 5 .   ? -16.056 19.199  22.394  1.00 54.05 ? 523 HOH   C O   1 
HETATM 8174 O O   . HOH   R 5 .   ? -8.370  -3.789  52.462  1.00 54.20 ? 524 HOH   C O   1 
HETATM 8175 O O   . HOH   R 5 .   ? 12.384  13.993  37.556  1.00 46.36 ? 525 HOH   C O   1 
HETATM 8176 O O   . HOH   R 5 .   ? -15.348 17.514  18.897  1.00 39.93 ? 526 HOH   C O   1 
HETATM 8177 O O   . HOH   R 5 .   ? -7.511  19.683  39.951  1.00 45.77 ? 527 HOH   C O   1 
HETATM 8178 O O   . HOH   R 5 .   ? 12.561  -14.929 50.051  1.00 52.08 ? 528 HOH   C O   1 
HETATM 8179 O O   . HOH   R 5 .   ? 15.210  -9.155  38.816  1.00 56.87 ? 529 HOH   C O   1 
HETATM 8180 O O   . HOH   R 5 .   ? -6.468  4.490   26.825  1.00 39.50 ? 530 HOH   C O   1 
HETATM 8181 O O   . HOH   R 5 .   ? 9.036   14.328  37.449  1.00 48.79 ? 531 HOH   C O   1 
HETATM 8182 O O   . HOH   R 5 .   ? 20.395  3.806   40.902  1.00 36.65 ? 532 HOH   C O   1 
HETATM 8183 O O   A HOH   R 5 .   ? -14.861 1.585   43.713  0.50 27.44 ? 533 HOH   C O   1 
HETATM 8184 O O   B HOH   R 5 .   ? -14.797 0.062   44.725  0.50 30.54 ? 533 HOH   C O   1 
HETATM 8185 O O   . HOH   R 5 .   ? -8.903  5.492   23.228  1.00 45.59 ? 534 HOH   C O   1 
HETATM 8186 O O   . HOH   R 5 .   ? 11.754  17.101  33.355  1.00 51.08 ? 535 HOH   C O   1 
HETATM 8187 O O   . HOH   R 5 .   ? -4.524  2.448   24.869  1.00 43.39 ? 536 HOH   C O   1 
HETATM 8188 O O   . HOH   R 5 .   ? 9.651   20.476  20.951  1.00 52.25 ? 537 HOH   C O   1 
HETATM 8189 O O   . HOH   S 5 .   ? -41.392 5.811   44.522  1.00 38.33 ? 401 HOH   D O   1 
HETATM 8190 O O   . HOH   S 5 .   ? -22.742 12.020  35.948  1.00 33.06 ? 402 HOH   D O   1 
HETATM 8191 O O   . HOH   S 5 .   ? -45.995 2.046   28.717  1.00 41.31 ? 403 HOH   D O   1 
HETATM 8192 O O   . HOH   S 5 .   ? -25.861 12.921  17.624  1.00 25.88 ? 404 HOH   D O   1 
HETATM 8193 O O   . HOH   S 5 .   ? -6.677  -19.123 28.006  1.00 49.26 ? 405 HOH   D O   1 
HETATM 8194 O O   . HOH   S 5 .   ? -19.892 -9.267  42.663  1.00 44.92 ? 406 HOH   D O   1 
HETATM 8195 O O   . HOH   S 5 .   ? -23.396 19.027  22.748  1.00 52.41 ? 407 HOH   D O   1 
HETATM 8196 O O   . HOH   S 5 .   ? -8.979  -7.684  20.523  1.00 44.47 ? 408 HOH   D O   1 
HETATM 8197 O O   . HOH   S 5 .   ? -38.328 11.421  23.494  1.00 41.73 ? 409 HOH   D O   1 
HETATM 8198 O O   . HOH   S 5 .   ? -29.756 -2.520  24.236  1.00 25.28 ? 410 HOH   D O   1 
HETATM 8199 O O   . HOH   S 5 .   ? -28.245 12.538  39.749  1.00 55.38 ? 411 HOH   D O   1 
HETATM 8200 O O   . HOH   S 5 .   ? -27.392 8.811   39.711  1.00 40.93 ? 412 HOH   D O   1 
HETATM 8201 O O   . HOH   S 5 .   ? -23.326 -19.413 33.250  1.00 47.92 ? 413 HOH   D O   1 
HETATM 8202 O O   . HOH   S 5 .   ? -32.683 13.742  38.010  1.00 35.52 ? 414 HOH   D O   1 
HETATM 8203 O O   . HOH   S 5 .   ? -8.001  -14.097 19.578  1.00 38.13 ? 415 HOH   D O   1 
HETATM 8204 O O   . HOH   S 5 .   ? -25.208 -4.353  46.194  1.00 58.59 ? 416 HOH   D O   1 
HETATM 8205 O O   . HOH   S 5 .   ? -29.398 -12.320 37.547  1.00 39.29 ? 417 HOH   D O   1 
HETATM 8206 O O   . HOH   S 5 .   ? -30.086 -9.580  30.834  1.00 27.87 ? 418 HOH   D O   1 
HETATM 8207 O O   . HOH   S 5 .   ? -20.300 12.721  28.490  1.00 19.23 ? 419 HOH   D O   1 
HETATM 8208 O O   . HOH   S 5 .   ? -39.330 -8.931  15.880  1.00 45.79 ? 420 HOH   D O   1 
HETATM 8209 O O   . HOH   S 5 .   ? -16.826 -15.482 37.830  1.00 35.90 ? 421 HOH   D O   1 
HETATM 8210 O O   . HOH   S 5 .   ? -19.445 -12.447 12.996  1.00 25.17 ? 422 HOH   D O   1 
HETATM 8211 O O   . HOH   S 5 .   ? -28.173 -10.416 41.573  1.00 35.23 ? 423 HOH   D O   1 
HETATM 8212 O O   . HOH   S 5 .   ? -12.274 -15.644 37.721  1.00 37.05 ? 424 HOH   D O   1 
HETATM 8213 O O   . HOH   S 5 .   ? -12.703 -5.562  23.434  1.00 41.29 ? 425 HOH   D O   1 
HETATM 8214 O O   . HOH   S 5 .   ? -36.276 20.051  30.593  1.00 58.11 ? 426 HOH   D O   1 
HETATM 8215 O O   . HOH   S 5 .   ? -40.567 -1.598  17.011  1.00 31.94 ? 427 HOH   D O   1 
HETATM 8216 O O   . HOH   S 5 .   ? -39.373 -12.888 9.747   1.00 36.73 ? 428 HOH   D O   1 
HETATM 8217 O O   . HOH   S 5 .   ? -9.872  -14.824 22.386  1.00 35.13 ? 429 HOH   D O   1 
HETATM 8218 O O   . HOH   S 5 .   ? -41.360 -0.920  19.433  1.00 28.00 ? 430 HOH   D O   1 
HETATM 8219 O O   . HOH   S 5 .   ? -37.048 -10.667 23.727  1.00 36.86 ? 431 HOH   D O   1 
HETATM 8220 O O   . HOH   S 5 .   ? -8.955  -8.314  28.928  1.00 22.34 ? 432 HOH   D O   1 
HETATM 8221 O O   . HOH   S 5 .   ? -8.942  -8.421  16.013  1.00 34.01 ? 433 HOH   D O   1 
HETATM 8222 O O   . HOH   S 5 .   ? -17.644 -11.577 31.018  1.00 35.27 ? 434 HOH   D O   1 
HETATM 8223 O O   . HOH   S 5 .   ? -22.099 7.574   44.120  1.00 42.75 ? 435 HOH   D O   1 
HETATM 8224 O O   . HOH   S 5 .   ? -19.873 -13.086 41.873  1.00 39.09 ? 436 HOH   D O   1 
HETATM 8225 O O   . HOH   S 5 .   ? -31.444 -12.397 23.861  1.00 46.44 ? 437 HOH   D O   1 
HETATM 8226 O O   . HOH   S 5 .   ? -44.476 4.013   35.052  1.00 35.06 ? 438 HOH   D O   1 
HETATM 8227 O O   . HOH   S 5 .   ? -14.914 -13.751 30.040  1.00 27.10 ? 439 HOH   D O   1 
HETATM 8228 O O   . HOH   S 5 .   ? -31.498 -0.771  25.579  1.00 24.09 ? 440 HOH   D O   1 
HETATM 8229 O O   . HOH   S 5 .   ? -13.245 -15.428 15.488  1.00 30.34 ? 441 HOH   D O   1 
HETATM 8230 O O   . HOH   S 5 .   ? -12.473 -8.042  20.593  1.00 23.70 ? 442 HOH   D O   1 
HETATM 8231 O O   . HOH   S 5 .   ? -43.595 -2.875  22.146  1.00 37.11 ? 443 HOH   D O   1 
HETATM 8232 O O   . HOH   S 5 .   ? -17.289 -3.616  22.867  1.00 35.56 ? 444 HOH   D O   1 
HETATM 8233 O O   . HOH   S 5 .   ? -16.545 -8.152  41.170  1.00 26.84 ? 445 HOH   D O   1 
HETATM 8234 O O   . HOH   S 5 .   ? -18.709 -1.295  42.018  1.00 32.34 ? 446 HOH   D O   1 
HETATM 8235 O O   . HOH   S 5 .   ? -24.726 8.339   37.143  1.00 31.45 ? 447 HOH   D O   1 
HETATM 8236 O O   . HOH   S 5 .   ? -24.739 -14.712 38.358  1.00 38.63 ? 448 HOH   D O   1 
HETATM 8237 O O   B HOH   S 5 .   ? -16.581 -7.710  14.161  0.40 16.12 ? 449 HOH   D O   1 
HETATM 8238 O O   . HOH   S 5 .   ? -16.544 -5.758  37.649  1.00 24.68 ? 450 HOH   D O   1 
HETATM 8239 O O   . HOH   S 5 .   ? -31.895 -13.255 20.931  1.00 38.64 ? 451 HOH   D O   1 
HETATM 8240 O O   . HOH   S 5 .   ? -8.980  -6.216  24.279  1.00 44.23 ? 452 HOH   D O   1 
HETATM 8241 O O   . HOH   S 5 .   ? -24.724 5.864   42.140  1.00 32.36 ? 453 HOH   D O   1 
HETATM 8242 O O   . HOH   S 5 .   ? -35.157 -4.488  8.391   1.00 35.26 ? 454 HOH   D O   1 
HETATM 8243 O O   . HOH   S 5 .   ? -32.650 -4.141  47.416  1.00 42.99 ? 455 HOH   D O   1 
HETATM 8244 O O   . HOH   S 5 .   ? -41.872 0.208   10.365  1.00 32.65 ? 456 HOH   D O   1 
HETATM 8245 O O   . HOH   S 5 .   ? -12.445 7.632   38.292  1.00 25.65 ? 457 HOH   D O   1 
HETATM 8246 O O   . HOH   S 5 .   ? -34.341 13.341  35.753  1.00 38.16 ? 458 HOH   D O   1 
HETATM 8247 O O   . HOH   S 5 .   ? -19.847 19.526  31.481  1.00 39.07 ? 459 HOH   D O   1 
HETATM 8248 O O   . HOH   S 5 .   ? -37.071 8.016   21.053  1.00 32.36 ? 460 HOH   D O   1 
HETATM 8249 O O   . HOH   S 5 .   ? -26.973 -8.125  41.659  1.00 32.66 ? 461 HOH   D O   1 
HETATM 8250 O O   . HOH   S 5 .   ? -18.413 18.418  23.731  1.00 41.48 ? 462 HOH   D O   1 
HETATM 8251 O O   . HOH   S 5 .   ? -36.416 3.404   13.999  1.00 38.89 ? 463 HOH   D O   1 
HETATM 8252 O O   . HOH   S 5 .   ? -11.493 -1.725  29.204  1.00 23.36 ? 464 HOH   D O   1 
HETATM 8253 O O   . HOH   S 5 .   ? -25.652 6.109   24.756  1.00 23.91 ? 465 HOH   D O   1 
HETATM 8254 O O   . HOH   S 5 .   ? -22.272 13.310  18.779  1.00 29.01 ? 466 HOH   D O   1 
HETATM 8255 O O   . HOH   S 5 .   ? -11.343 -7.704  31.915  1.00 19.09 ? 467 HOH   D O   1 
HETATM 8256 O O   . HOH   S 5 .   ? -26.265 -7.671  44.241  1.00 40.51 ? 468 HOH   D O   1 
HETATM 8257 O O   . HOH   S 5 .   ? -36.151 -8.821  30.412  1.00 31.64 ? 469 HOH   D O   1 
HETATM 8258 O O   . HOH   S 5 .   ? -13.747 10.156  38.103  1.00 21.74 ? 470 HOH   D O   1 
HETATM 8259 O O   . HOH   S 5 .   ? -43.699 -0.237  23.027  1.00 37.12 ? 471 HOH   D O   1 
HETATM 8260 O O   . HOH   S 5 .   ? -35.170 -13.385 3.852   1.00 45.36 ? 472 HOH   D O   1 
HETATM 8261 O O   . HOH   S 5 .   ? -41.058 -14.725 32.691  1.00 37.80 ? 473 HOH   D O   1 
HETATM 8262 O O   . HOH   S 5 .   ? -44.198 7.809   23.001  1.00 41.34 ? 474 HOH   D O   1 
HETATM 8263 O O   . HOH   S 5 .   ? -44.804 -1.206  46.878  1.00 47.71 ? 475 HOH   D O   1 
HETATM 8264 O O   . HOH   S 5 .   ? -25.826 -12.021 14.000  1.00 22.46 ? 476 HOH   D O   1 
HETATM 8265 O O   . HOH   S 5 .   ? -21.953 6.036   32.797  1.00 26.21 ? 477 HOH   D O   1 
HETATM 8266 O O   . HOH   S 5 .   ? -4.131  -19.190 23.040  1.00 39.81 ? 478 HOH   D O   1 
HETATM 8267 O O   . HOH   S 5 .   ? -6.149  -14.927 17.024  1.00 36.08 ? 479 HOH   D O   1 
HETATM 8268 O O   . HOH   S 5 .   ? -44.339 -6.738  22.390  1.00 42.37 ? 480 HOH   D O   1 
HETATM 8269 O O   . HOH   S 5 .   ? -20.046 -3.570  21.931  1.00 41.86 ? 481 HOH   D O   1 
HETATM 8270 O O   . HOH   S 5 .   ? -28.910 -15.310 7.620   1.00 37.86 ? 482 HOH   D O   1 
HETATM 8271 O O   . HOH   S 5 .   ? -42.087 6.481   16.532  1.00 33.57 ? 483 HOH   D O   1 
HETATM 8272 O O   . HOH   S 5 .   ? -23.401 3.597   42.096  1.00 33.41 ? 484 HOH   D O   1 
HETATM 8273 O O   . HOH   S 5 .   ? -35.265 -2.661  10.059  1.00 27.09 ? 485 HOH   D O   1 
HETATM 8274 O O   . HOH   S 5 .   ? -12.570 2.685   26.342  1.00 24.73 ? 486 HOH   D O   1 
HETATM 8275 O O   . HOH   S 5 .   ? -32.198 -14.844 35.977  1.00 45.79 ? 487 HOH   D O   1 
HETATM 8276 O O   . HOH   S 5 .   ? -13.471 4.273   24.070  1.00 37.64 ? 488 HOH   D O   1 
HETATM 8277 O O   . HOH   S 5 .   ? -22.814 -29.392 25.213  1.00 53.68 ? 489 HOH   D O   1 
HETATM 8278 O O   . HOH   S 5 .   ? -45.107 -2.720  37.923  1.00 36.72 ? 490 HOH   D O   1 
HETATM 8279 O O   . HOH   S 5 .   ? -43.814 -14.550 31.145  1.00 41.85 ? 491 HOH   D O   1 
HETATM 8280 O O   . HOH   S 5 .   ? -37.735 -1.951  10.253  1.00 39.90 ? 492 HOH   D O   1 
HETATM 8281 O O   . HOH   S 5 .   ? -21.295 -18.818 19.731  1.00 51.33 ? 493 HOH   D O   1 
HETATM 8282 O O   . HOH   S 5 .   ? -32.755 18.855  28.481  1.00 53.85 ? 494 HOH   D O   1 
HETATM 8283 O O   . HOH   S 5 .   ? -29.422 -15.960 26.079  1.00 46.47 ? 495 HOH   D O   1 
HETATM 8284 O O   . HOH   S 5 .   ? -19.734 -12.278 18.706  1.00 29.05 ? 496 HOH   D O   1 
HETATM 8285 O O   . HOH   S 5 .   ? -44.324 -0.177  13.172  1.00 50.10 ? 497 HOH   D O   1 
HETATM 8286 O O   . HOH   S 5 .   ? -20.802 15.638  35.100  1.00 49.33 ? 498 HOH   D O   1 
HETATM 8287 O O   . HOH   S 5 .   ? -33.402 -9.269  45.550  1.00 52.83 ? 499 HOH   D O   1 
HETATM 8288 O O   . HOH   S 5 .   ? -18.239 -6.872  45.284  1.00 50.70 ? 500 HOH   D O   1 
HETATM 8289 O O   . HOH   S 5 .   ? -43.890 11.312  40.646  1.00 47.96 ? 501 HOH   D O   1 
HETATM 8290 O O   . HOH   S 5 .   ? -27.754 -14.211 38.326  1.00 44.89 ? 502 HOH   D O   1 
HETATM 8291 O O   . HOH   S 5 .   ? -45.601 0.106   24.747  1.00 43.07 ? 503 HOH   D O   1 
HETATM 8292 O O   . HOH   S 5 .   ? -29.413 2.262   50.292  1.00 53.39 ? 504 HOH   D O   1 
HETATM 8293 O O   . HOH   S 5 .   ? -42.140 -3.574  15.920  1.00 46.25 ? 505 HOH   D O   1 
HETATM 8294 O O   . HOH   S 5 .   ? -21.335 -17.713 37.149  1.00 51.76 ? 506 HOH   D O   1 
HETATM 8295 O O   . HOH   S 5 .   ? -44.527 3.750   41.640  1.00 47.03 ? 507 HOH   D O   1 
HETATM 8296 O O   . HOH   S 5 .   ? -17.965 0.897   42.848  1.00 36.45 ? 508 HOH   D O   1 
HETATM 8297 O O   . HOH   S 5 .   ? -2.969  -17.244 24.849  1.00 38.15 ? 509 HOH   D O   1 
HETATM 8298 O O   . HOH   S 5 .   ? -33.165 -7.139  46.943  1.00 51.71 ? 510 HOH   D O   1 
HETATM 8299 O O   . HOH   S 5 .   ? -4.208  -18.229 27.908  1.00 52.49 ? 511 HOH   D O   1 
HETATM 8300 O O   . HOH   S 5 .   ? -36.489 9.902   19.617  1.00 41.54 ? 512 HOH   D O   1 
HETATM 8301 O O   . HOH   S 5 .   ? -14.418 -3.711  24.758  1.00 43.26 ? 513 HOH   D O   1 
HETATM 8302 O O   . HOH   S 5 .   ? -8.655  -16.012 39.734  1.00 52.08 ? 514 HOH   D O   1 
HETATM 8303 O O   . HOH   S 5 .   ? -27.307 7.607   44.866  1.00 50.80 ? 515 HOH   D O   1 
HETATM 8304 O O   . HOH   S 5 .   ? -22.047 3.068   44.454  1.00 43.21 ? 516 HOH   D O   1 
HETATM 8305 O O   . HOH   S 5 .   ? -33.215 -17.204 30.161  1.00 52.91 ? 517 HOH   D O   1 
HETATM 8306 O O   . HOH   S 5 .   ? -14.555 -2.004  21.594  1.00 46.18 ? 518 HOH   D O   1 
HETATM 8307 O O   . HOH   S 5 .   ? -9.294  -25.716 32.216  1.00 58.11 ? 519 HOH   D O   1 
HETATM 8308 O O   . HOH   S 5 .   ? -45.000 -2.560  19.106  1.00 47.32 ? 520 HOH   D O   1 
HETATM 8309 O O   . HOH   S 5 .   ? -22.907 -19.113 21.434  1.00 51.31 ? 521 HOH   D O   1 
HETATM 8310 O O   . HOH   S 5 .   ? -24.605 -20.725 11.798  1.00 56.09 ? 522 HOH   D O   1 
# 
