data_8RHX
# 
_entry.id   8RHX 
# 
_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   8RHX         pdb_00008rhx 10.2210/pdb8rhx/pdb 
WWPDB D_1292135418 ?            ?                   
# 
_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                        8RHX 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Crystal Structure of Trypanosoma brucei DHFR in complex with the cofactor and inhibitor P25' 8RHT unspecified 
PDB 'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P25' 8RHU unspecified 
PDB 'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P30' 8RHV unspecified 
PDB 'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P31' 8RHW 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'                                       30800.982 4   ? ? ? ? 
2 non-polymer syn 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 745.421   4   ? ? ? ? 
3 non-polymer syn '1-[4,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]guanidine'   244.081   4   ? ? ? ? 
4 non-polymer syn 'ACETATE ION'                                               59.044    3   ? ? ? ? 
5 water       nat water                                                       18.015    751 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSSGLVPRGSHMMEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVC
QADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFA
QRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKD
KWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
;
_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 '1-[4,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]guanidine'   A1H0T 
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 CYS 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 
A1H0T non-polymer         . '1-[4,6-bis(chloranyl)-1~{H}-benzimidazol-2-yl]guanidine'   ? 'C8 H7 Cl2 N5'      244.081 
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 
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 125 104 104 GLN GLN 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 164 143 143 LYS LYS 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 CYS 189 168 168 CYS CYS 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  -6  VAL VAL B . n 
B 1 16  PRO 16  -5  -5  PRO PRO B . n 
B 1 17  ARG 17  -4  -4  ARG ARG B . n 
B 1 18  GLY 18  -3  -3  GLY GLY B . n 
B 1 19  SER 19  -2  -2  SER SER B . n 
B 1 20  HIS 20  -1  -1  HIS HIS B . n 
B 1 21  MET 21  0   0   MET MET B . n 
B 1 22  MET 22  1   1   MET MET 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 CYS 189 168 168 CYS CYS 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 CYS 189 168 168 CYS CYS 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 125 104 104 GLN GLN 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 CYS 189 168 168 CYS CYS 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        A1H0T 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H0T 
_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 A1H0T 1   302 270 A1H0T D12 A . 
G 4 ACT   1   303 271 ACT   ACT A . 
H 4 ACT   1   304 271 ACT   ACT A . 
I 2 NDP   1   301 269 NDP   NDP B . 
J 3 A1H0T 1   302 270 A1H0T D12 B . 
K 2 NDP   1   301 269 NDP   NDP C . 
L 3 A1H0T 1   302 270 A1H0T D12 C . 
M 4 ACT   1   303 272 ACT   ACT C . 
N 2 NDP   1   301 269 NDP   NDP D . 
O 3 A1H0T 1   302 270 A1H0T D12 D . 
P 5 HOH   1   401 741 HOH   HOH A . 
P 5 HOH   2   402 778 HOH   HOH A . 
P 5 HOH   3   403 632 HOH   HOH A . 
P 5 HOH   4   404 273 HOH   HOH A . 
P 5 HOH   5   405 390 HOH   HOH A . 
P 5 HOH   6   406 451 HOH   HOH A . 
P 5 HOH   7   407 311 HOH   HOH A . 
P 5 HOH   8   408 22  HOH   HOH A . 
P 5 HOH   9   409 288 HOH   HOH A . 
P 5 HOH   10  410 18  HOH   HOH A . 
P 5 HOH   11  411 367 HOH   HOH A . 
P 5 HOH   12  412 609 HOH   HOH A . 
P 5 HOH   13  413 853 HOH   HOH A . 
P 5 HOH   14  414 12  HOH   HOH A . 
P 5 HOH   15  415 524 HOH   HOH A . 
P 5 HOH   16  416 790 HOH   HOH A . 
P 5 HOH   17  417 121 HOH   HOH A . 
P 5 HOH   18  418 263 HOH   HOH A . 
P 5 HOH   19  419 364 HOH   HOH A . 
P 5 HOH   20  420 745 HOH   HOH A . 
P 5 HOH   21  421 251 HOH   HOH A . 
P 5 HOH   22  422 19  HOH   HOH A . 
P 5 HOH   23  423 261 HOH   HOH A . 
P 5 HOH   24  424 127 HOH   HOH A . 
P 5 HOH   25  425 46  HOH   HOH A . 
P 5 HOH   26  426 199 HOH   HOH A . 
P 5 HOH   27  427 89  HOH   HOH A . 
P 5 HOH   28  428 487 HOH   HOH A . 
P 5 HOH   29  429 442 HOH   HOH A . 
P 5 HOH   30  430 700 HOH   HOH A . 
P 5 HOH   31  431 109 HOH   HOH A . 
P 5 HOH   32  432 250 HOH   HOH A . 
P 5 HOH   33  433 10  HOH   HOH A . 
P 5 HOH   34  434 401 HOH   HOH A . 
P 5 HOH   35  435 266 HOH   HOH A . 
P 5 HOH   36  436 172 HOH   HOH A . 
P 5 HOH   37  437 532 HOH   HOH A . 
P 5 HOH   38  438 54  HOH   HOH A . 
P 5 HOH   39  439 687 HOH   HOH A . 
P 5 HOH   40  440 224 HOH   HOH A . 
P 5 HOH   41  441 143 HOH   HOH A . 
P 5 HOH   42  442 283 HOH   HOH A . 
P 5 HOH   43  443 42  HOH   HOH A . 
P 5 HOH   44  444 239 HOH   HOH A . 
P 5 HOH   45  445 238 HOH   HOH A . 
P 5 HOH   46  446 389 HOH   HOH A . 
P 5 HOH   47  447 101 HOH   HOH A . 
P 5 HOH   48  448 298 HOH   HOH A . 
P 5 HOH   49  449 295 HOH   HOH A . 
P 5 HOH   50  450 391 HOH   HOH A . 
P 5 HOH   51  451 201 HOH   HOH A . 
P 5 HOH   52  452 327 HOH   HOH A . 
P 5 HOH   53  453 498 HOH   HOH A . 
P 5 HOH   54  454 111 HOH   HOH A . 
P 5 HOH   55  455 202 HOH   HOH A . 
P 5 HOH   56  456 196 HOH   HOH A . 
P 5 HOH   57  457 95  HOH   HOH A . 
P 5 HOH   58  458 398 HOH   HOH A . 
P 5 HOH   59  459 596 HOH   HOH A . 
P 5 HOH   60  460 194 HOH   HOH A . 
P 5 HOH   61  461 63  HOH   HOH A . 
P 5 HOH   62  462 558 HOH   HOH A . 
P 5 HOH   63  463 336 HOH   HOH A . 
P 5 HOH   64  464 44  HOH   HOH A . 
P 5 HOH   65  465 154 HOH   HOH A . 
P 5 HOH   66  466 4   HOH   HOH A . 
P 5 HOH   67  467 479 HOH   HOH A . 
P 5 HOH   68  468 281 HOH   HOH A . 
P 5 HOH   69  469 788 HOH   HOH A . 
P 5 HOH   70  470 514 HOH   HOH A . 
P 5 HOH   71  471 666 HOH   HOH A . 
P 5 HOH   72  472 413 HOH   HOH A . 
P 5 HOH   73  473 710 HOH   HOH A . 
P 5 HOH   74  474 855 HOH   HOH A . 
P 5 HOH   75  475 236 HOH   HOH A . 
P 5 HOH   76  476 128 HOH   HOH A . 
P 5 HOH   77  477 296 HOH   HOH A . 
P 5 HOH   78  478 492 HOH   HOH A . 
P 5 HOH   79  479 247 HOH   HOH A . 
P 5 HOH   80  480 285 HOH   HOH A . 
P 5 HOH   81  481 23  HOH   HOH A . 
P 5 HOH   82  482 761 HOH   HOH A . 
P 5 HOH   83  483 265 HOH   HOH A . 
P 5 HOH   84  484 223 HOH   HOH A . 
P 5 HOH   85  485 7   HOH   HOH A . 
P 5 HOH   86  486 6   HOH   HOH A . 
P 5 HOH   87  487 144 HOH   HOH A . 
P 5 HOH   88  488 193 HOH   HOH A . 
P 5 HOH   89  489 445 HOH   HOH A . 
P 5 HOH   90  490 304 HOH   HOH A . 
P 5 HOH   91  491 821 HOH   HOH A . 
P 5 HOH   92  492 97  HOH   HOH A . 
P 5 HOH   93  493 435 HOH   HOH A . 
P 5 HOH   94  494 56  HOH   HOH A . 
P 5 HOH   95  495 85  HOH   HOH A . 
P 5 HOH   96  496 731 HOH   HOH A . 
P 5 HOH   97  497 47  HOH   HOH A . 
P 5 HOH   98  498 385 HOH   HOH A . 
P 5 HOH   99  499 603 HOH   HOH A . 
P 5 HOH   100 500 92  HOH   HOH A . 
P 5 HOH   101 501 204 HOH   HOH A . 
P 5 HOH   102 502 623 HOH   HOH A . 
P 5 HOH   103 503 36  HOH   HOH A . 
P 5 HOH   104 504 142 HOH   HOH A . 
P 5 HOH   105 505 198 HOH   HOH A . 
P 5 HOH   106 506 729 HOH   HOH A . 
P 5 HOH   107 507 332 HOH   HOH A . 
P 5 HOH   108 508 692 HOH   HOH A . 
P 5 HOH   109 509 74  HOH   HOH A . 
P 5 HOH   110 510 61  HOH   HOH A . 
P 5 HOH   111 511 375 HOH   HOH A . 
P 5 HOH   112 512 421 HOH   HOH A . 
P 5 HOH   113 513 312 HOH   HOH A . 
P 5 HOH   114 514 677 HOH   HOH A . 
P 5 HOH   115 515 329 HOH   HOH A . 
P 5 HOH   116 516 511 HOH   HOH A . 
P 5 HOH   117 517 307 HOH   HOH A . 
P 5 HOH   118 518 91  HOH   HOH A . 
P 5 HOH   119 519 302 HOH   HOH A . 
P 5 HOH   120 520 28  HOH   HOH A . 
P 5 HOH   121 521 348 HOH   HOH A . 
P 5 HOH   122 522 750 HOH   HOH A . 
P 5 HOH   123 523 303 HOH   HOH A . 
P 5 HOH   124 524 225 HOH   HOH A . 
P 5 HOH   125 525 386 HOH   HOH A . 
P 5 HOH   126 526 149 HOH   HOH A . 
P 5 HOH   127 527 791 HOH   HOH A . 
P 5 HOH   128 528 123 HOH   HOH A . 
P 5 HOH   129 529 126 HOH   HOH A . 
P 5 HOH   130 530 230 HOH   HOH A . 
P 5 HOH   131 531 748 HOH   HOH A . 
P 5 HOH   132 532 372 HOH   HOH A . 
P 5 HOH   133 533 693 HOH   HOH A . 
P 5 HOH   134 534 503 HOH   HOH A . 
P 5 HOH   135 535 734 HOH   HOH A . 
P 5 HOH   136 536 228 HOH   HOH A . 
P 5 HOH   137 537 675 HOH   HOH A . 
P 5 HOH   138 538 472 HOH   HOH A . 
P 5 HOH   139 539 685 HOH   HOH A . 
P 5 HOH   140 540 684 HOH   HOH A . 
P 5 HOH   141 541 712 HOH   HOH A . 
P 5 HOH   142 542 406 HOH   HOH A . 
P 5 HOH   143 543 521 HOH   HOH A . 
P 5 HOH   144 544 466 HOH   HOH A . 
P 5 HOH   145 545 861 HOH   HOH A . 
P 5 HOH   146 546 747 HOH   HOH A . 
P 5 HOH   147 547 659 HOH   HOH A . 
P 5 HOH   148 548 561 HOH   HOH A . 
P 5 HOH   149 549 619 HOH   HOH A . 
P 5 HOH   150 550 815 HOH   HOH A . 
P 5 HOH   151 551 702 HOH   HOH A . 
P 5 HOH   152 552 724 HOH   HOH A . 
P 5 HOH   153 553 740 HOH   HOH A . 
P 5 HOH   154 554 550 HOH   HOH A . 
P 5 HOH   155 555 608 HOH   HOH A . 
P 5 HOH   156 556 670 HOH   HOH A . 
P 5 HOH   157 557 636 HOH   HOH A . 
P 5 HOH   158 558 862 HOH   HOH A . 
P 5 HOH   159 559 326 HOH   HOH A . 
P 5 HOH   160 560 803 HOH   HOH A . 
P 5 HOH   161 561 544 HOH   HOH A . 
P 5 HOH   162 562 473 HOH   HOH A . 
P 5 HOH   163 563 880 HOH   HOH A . 
P 5 HOH   164 564 771 HOH   HOH A . 
P 5 HOH   165 565 744 HOH   HOH A . 
P 5 HOH   166 566 360 HOH   HOH A . 
P 5 HOH   167 567 813 HOH   HOH A . 
P 5 HOH   168 568 637 HOH   HOH A . 
P 5 HOH   169 569 402 HOH   HOH A . 
P 5 HOH   170 570 860 HOH   HOH A . 
P 5 HOH   171 571 652 HOH   HOH A . 
P 5 HOH   172 572 848 HOH   HOH A . 
P 5 HOH   173 573 328 HOH   HOH A . 
P 5 HOH   174 574 591 HOH   HOH A . 
P 5 HOH   175 575 850 HOH   HOH A . 
P 5 HOH   176 576 379 HOH   HOH A . 
P 5 HOH   177 577 352 HOH   HOH A . 
P 5 HOH   178 578 620 HOH   HOH A . 
P 5 HOH   179 579 480 HOH   HOH A . 
P 5 HOH   180 580 760 HOH   HOH A . 
P 5 HOH   181 581 325 HOH   HOH A . 
P 5 HOH   182 582 316 HOH   HOH A . 
P 5 HOH   183 583 682 HOH   HOH A . 
P 5 HOH   184 584 396 HOH   HOH A . 
P 5 HOH   185 585 519 HOH   HOH A . 
P 5 HOH   186 586 895 HOH   HOH A . 
P 5 HOH   187 587 751 HOH   HOH A . 
P 5 HOH   188 588 607 HOH   HOH A . 
P 5 HOH   189 589 404 HOH   HOH A . 
Q 5 HOH   1   401 244 HOH   HOH B . 
Q 5 HOH   2   402 525 HOH   HOH B . 
Q 5 HOH   3   403 449 HOH   HOH B . 
Q 5 HOH   4   404 72  HOH   HOH B . 
Q 5 HOH   5   405 755 HOH   HOH B . 
Q 5 HOH   6   406 25  HOH   HOH B . 
Q 5 HOH   7   407 674 HOH   HOH B . 
Q 5 HOH   8   408 290 HOH   HOH B . 
Q 5 HOH   9   409 270 HOH   HOH B . 
Q 5 HOH   10  410 905 HOH   HOH B . 
Q 5 HOH   11  411 8   HOH   HOH B . 
Q 5 HOH   12  412 152 HOH   HOH B . 
Q 5 HOH   13  413 88  HOH   HOH B . 
Q 5 HOH   14  414 192 HOH   HOH B . 
Q 5 HOH   15  415 864 HOH   HOH B . 
Q 5 HOH   16  416 112 HOH   HOH B . 
Q 5 HOH   17  417 714 HOH   HOH B . 
Q 5 HOH   18  418 151 HOH   HOH B . 
Q 5 HOH   19  419 474 HOH   HOH B . 
Q 5 HOH   20  420 68  HOH   HOH B . 
Q 5 HOH   21  421 255 HOH   HOH B . 
Q 5 HOH   22  422 53  HOH   HOH B . 
Q 5 HOH   23  423 185 HOH   HOH B . 
Q 5 HOH   24  424 373 HOH   HOH B . 
Q 5 HOH   25  425 232 HOH   HOH B . 
Q 5 HOH   26  426 94  HOH   HOH B . 
Q 5 HOH   27  427 775 HOH   HOH B . 
Q 5 HOH   28  428 124 HOH   HOH B . 
Q 5 HOH   29  429 14  HOH   HOH B . 
Q 5 HOH   30  430 264 HOH   HOH B . 
Q 5 HOH   31  431 213 HOH   HOH B . 
Q 5 HOH   32  432 163 HOH   HOH B . 
Q 5 HOH   33  433 208 HOH   HOH B . 
Q 5 HOH   34  434 78  HOH   HOH B . 
Q 5 HOH   35  435 416 HOH   HOH B . 
Q 5 HOH   36  436 718 HOH   HOH B . 
Q 5 HOH   37  437 45  HOH   HOH B . 
Q 5 HOH   38  438 552 HOH   HOH B . 
Q 5 HOH   39  439 701 HOH   HOH B . 
Q 5 HOH   40  440 481 HOH   HOH B . 
Q 5 HOH   41  441 438 HOH   HOH B . 
Q 5 HOH   42  442 186 HOH   HOH B . 
Q 5 HOH   43  443 721 HOH   HOH B . 
Q 5 HOH   44  444 508 HOH   HOH B . 
Q 5 HOH   45  445 253 HOH   HOH B . 
Q 5 HOH   46  446 173 HOH   HOH B . 
Q 5 HOH   47  447 515 HOH   HOH B . 
Q 5 HOH   48  448 252 HOH   HOH B . 
Q 5 HOH   49  449 583 HOH   HOH B . 
Q 5 HOH   50  450 289 HOH   HOH B . 
Q 5 HOH   51  451 419 HOH   HOH B . 
Q 5 HOH   52  452 918 HOH   HOH B . 
Q 5 HOH   53  453 60  HOH   HOH B . 
Q 5 HOH   54  454 906 HOH   HOH B . 
Q 5 HOH   55  455 496 HOH   HOH B . 
Q 5 HOH   56  456 491 HOH   HOH B . 
Q 5 HOH   57  457 184 HOH   HOH B . 
Q 5 HOH   58  458 495 HOH   HOH B . 
Q 5 HOH   59  459 181 HOH   HOH B . 
Q 5 HOH   60  460 117 HOH   HOH B . 
Q 5 HOH   61  461 376 HOH   HOH B . 
Q 5 HOH   62  462 156 HOH   HOH B . 
Q 5 HOH   63  463 324 HOH   HOH B . 
Q 5 HOH   64  464 59  HOH   HOH B . 
Q 5 HOH   65  465 129 HOH   HOH B . 
Q 5 HOH   66  466 407 HOH   HOH B . 
Q 5 HOH   67  467 24  HOH   HOH B . 
Q 5 HOH   68  468 155 HOH   HOH B . 
Q 5 HOH   69  469 16  HOH   HOH B . 
Q 5 HOH   70  470 71  HOH   HOH B . 
Q 5 HOH   71  471 177 HOH   HOH B . 
Q 5 HOH   72  472 150 HOH   HOH B . 
Q 5 HOH   73  473 272 HOH   HOH B . 
Q 5 HOH   74  474 366 HOH   HOH B . 
Q 5 HOH   75  475 411 HOH   HOH B . 
Q 5 HOH   76  476 866 HOH   HOH B . 
Q 5 HOH   77  477 656 HOH   HOH B . 
Q 5 HOH   78  478 437 HOH   HOH B . 
Q 5 HOH   79  479 658 HOH   HOH B . 
Q 5 HOH   80  480 868 HOH   HOH B . 
Q 5 HOH   81  481 57  HOH   HOH B . 
Q 5 HOH   82  482 736 HOH   HOH B . 
Q 5 HOH   83  483 237 HOH   HOH B . 
Q 5 HOH   84  484 405 HOH   HOH B . 
Q 5 HOH   85  485 80  HOH   HOH B . 
Q 5 HOH   86  486 9   HOH   HOH B . 
Q 5 HOH   87  487 588 HOH   HOH B . 
Q 5 HOH   88  488 766 HOH   HOH B . 
Q 5 HOH   89  489 75  HOH   HOH B . 
Q 5 HOH   90  490 277 HOH   HOH B . 
Q 5 HOH   91  491 107 HOH   HOH B . 
Q 5 HOH   92  492 870 HOH   HOH B . 
Q 5 HOH   93  493 665 HOH   HOH B . 
Q 5 HOH   94  494 82  HOH   HOH B . 
Q 5 HOH   95  495 919 HOH   HOH B . 
Q 5 HOH   96  496 922 HOH   HOH B . 
Q 5 HOH   97  497 504 HOH   HOH B . 
Q 5 HOH   98  498 81  HOH   HOH B . 
Q 5 HOH   99  499 735 HOH   HOH B . 
Q 5 HOH   100 500 393 HOH   HOH B . 
Q 5 HOH   101 501 890 HOH   HOH B . 
Q 5 HOH   102 502 654 HOH   HOH B . 
Q 5 HOH   103 503 167 HOH   HOH B . 
Q 5 HOH   104 504 309 HOH   HOH B . 
Q 5 HOH   105 505 43  HOH   HOH B . 
Q 5 HOH   106 506 217 HOH   HOH B . 
Q 5 HOH   107 507 62  HOH   HOH B . 
Q 5 HOH   108 508 131 HOH   HOH B . 
Q 5 HOH   109 509 865 HOH   HOH B . 
Q 5 HOH   110 510 643 HOH   HOH B . 
Q 5 HOH   111 511 783 HOH   HOH B . 
Q 5 HOH   112 512 5   HOH   HOH B . 
Q 5 HOH   113 513 90  HOH   HOH B . 
Q 5 HOH   114 514 79  HOH   HOH B . 
Q 5 HOH   115 515 635 HOH   HOH B . 
Q 5 HOH   116 516 382 HOH   HOH B . 
Q 5 HOH   117 517 207 HOH   HOH B . 
Q 5 HOH   118 518 37  HOH   HOH B . 
Q 5 HOH   119 519 422 HOH   HOH B . 
Q 5 HOH   120 520 197 HOH   HOH B . 
Q 5 HOH   121 521 344 HOH   HOH B . 
Q 5 HOH   122 522 227 HOH   HOH B . 
Q 5 HOH   123 523 346 HOH   HOH B . 
Q 5 HOH   124 524 885 HOH   HOH B . 
Q 5 HOH   125 525 310 HOH   HOH B . 
Q 5 HOH   126 526 917 HOH   HOH B . 
Q 5 HOH   127 527 667 HOH   HOH B . 
Q 5 HOH   128 528 179 HOH   HOH B . 
Q 5 HOH   129 529 130 HOH   HOH B . 
Q 5 HOH   130 530 730 HOH   HOH B . 
Q 5 HOH   131 531 757 HOH   HOH B . 
Q 5 HOH   132 532 403 HOH   HOH B . 
Q 5 HOH   133 533 849 HOH   HOH B . 
Q 5 HOH   134 534 342 HOH   HOH B . 
Q 5 HOH   135 535 392 HOH   HOH B . 
Q 5 HOH   136 536 534 HOH   HOH B . 
Q 5 HOH   137 537 246 HOH   HOH B . 
Q 5 HOH   138 538 646 HOH   HOH B . 
Q 5 HOH   139 539 649 HOH   HOH B . 
Q 5 HOH   140 540 883 HOH   HOH B . 
Q 5 HOH   141 541 297 HOH   HOH B . 
Q 5 HOH   142 542 471 HOH   HOH B . 
Q 5 HOH   143 543 634 HOH   HOH B . 
Q 5 HOH   144 544 483 HOH   HOH B . 
Q 5 HOH   145 545 683 HOH   HOH B . 
Q 5 HOH   146 546 781 HOH   HOH B . 
Q 5 HOH   147 547 518 HOH   HOH B . 
Q 5 HOH   148 548 878 HOH   HOH B . 
Q 5 HOH   149 549 664 HOH   HOH B . 
Q 5 HOH   150 550 686 HOH   HOH B . 
Q 5 HOH   151 551 767 HOH   HOH B . 
Q 5 HOH   152 552 458 HOH   HOH B . 
Q 5 HOH   153 553 725 HOH   HOH B . 
Q 5 HOH   154 554 455 HOH   HOH B . 
Q 5 HOH   155 555 541 HOH   HOH B . 
Q 5 HOH   156 556 292 HOH   HOH B . 
Q 5 HOH   157 557 889 HOH   HOH B . 
Q 5 HOH   158 558 762 HOH   HOH B . 
Q 5 HOH   159 559 337 HOH   HOH B . 
Q 5 HOH   160 560 484 HOH   HOH B . 
Q 5 HOH   161 561 812 HOH   HOH B . 
Q 5 HOH   162 562 556 HOH   HOH B . 
Q 5 HOH   163 563 314 HOH   HOH B . 
Q 5 HOH   164 564 369 HOH   HOH B . 
Q 5 HOH   165 565 559 HOH   HOH B . 
Q 5 HOH   166 566 395 HOH   HOH B . 
Q 5 HOH   167 567 629 HOH   HOH B . 
Q 5 HOH   168 568 728 HOH   HOH B . 
Q 5 HOH   169 569 899 HOH   HOH B . 
Q 5 HOH   170 570 617 HOH   HOH B . 
Q 5 HOH   171 571 743 HOH   HOH B . 
Q 5 HOH   172 572 450 HOH   HOH B . 
Q 5 HOH   173 573 394 HOH   HOH B . 
Q 5 HOH   174 574 799 HOH   HOH B . 
Q 5 HOH   175 575 529 HOH   HOH B . 
Q 5 HOH   176 576 774 HOH   HOH B . 
Q 5 HOH   177 577 802 HOH   HOH B . 
Q 5 HOH   178 578 469 HOH   HOH B . 
Q 5 HOH   179 579 678 HOH   HOH B . 
Q 5 HOH   180 580 808 HOH   HOH B . 
Q 5 HOH   181 581 707 HOH   HOH B . 
Q 5 HOH   182 582 805 HOH   HOH B . 
Q 5 HOH   183 583 801 HOH   HOH B . 
R 5 HOH   1   401 800 HOH   HOH C . 
R 5 HOH   2   402 923 HOH   HOH C . 
R 5 HOH   3   403 533 HOH   HOH C . 
R 5 HOH   4   404 530 HOH   HOH C . 
R 5 HOH   5   405 162 HOH   HOH C . 
R 5 HOH   6   406 428 HOH   HOH C . 
R 5 HOH   7   407 876 HOH   HOH C . 
R 5 HOH   8   408 688 HOH   HOH C . 
R 5 HOH   9   409 55  HOH   HOH C . 
R 5 HOH   10  410 169 HOH   HOH C . 
R 5 HOH   11  411 909 HOH   HOH C . 
R 5 HOH   12  412 26  HOH   HOH C . 
R 5 HOH   13  413 653 HOH   HOH C . 
R 5 HOH   14  414 387 HOH   HOH C . 
R 5 HOH   15  415 77  HOH   HOH C . 
R 5 HOH   16  416 920 HOH   HOH C . 
R 5 HOH   17  417 133 HOH   HOH C . 
R 5 HOH   18  418 166 HOH   HOH C . 
R 5 HOH   19  419 505 HOH   HOH C . 
R 5 HOH   20  420 219 HOH   HOH C . 
R 5 HOH   21  421 3   HOH   HOH C . 
R 5 HOH   22  422 248 HOH   HOH C . 
R 5 HOH   23  423 414 HOH   HOH C . 
R 5 HOH   24  424 823 HOH   HOH C . 
R 5 HOH   25  425 915 HOH   HOH C . 
R 5 HOH   26  426 365 HOH   HOH C . 
R 5 HOH   27  427 742 HOH   HOH C . 
R 5 HOH   28  428 102 HOH   HOH C . 
R 5 HOH   29  429 657 HOH   HOH C . 
R 5 HOH   30  430 444 HOH   HOH C . 
R 5 HOH   31  431 120 HOH   HOH C . 
R 5 HOH   32  432 226 HOH   HOH C . 
R 5 HOH   33  433 40  HOH   HOH C . 
R 5 HOH   34  434 378 HOH   HOH C . 
R 5 HOH   35  435 837 HOH   HOH C . 
R 5 HOH   36  436 30  HOH   HOH C . 
R 5 HOH   37  437 695 HOH   HOH C . 
R 5 HOH   38  438 911 HOH   HOH C . 
R 5 HOH   39  439 773 HOH   HOH C . 
R 5 HOH   40  440 361 HOH   HOH C . 
R 5 HOH   41  441 856 HOH   HOH C . 
R 5 HOH   42  442 235 HOH   HOH C . 
R 5 HOH   43  443 723 HOH   HOH C . 
R 5 HOH   44  444 794 HOH   HOH C . 
R 5 HOH   45  445 400 HOH   HOH C . 
R 5 HOH   46  446 418 HOH   HOH C . 
R 5 HOH   47  447 33  HOH   HOH C . 
R 5 HOH   48  448 93  HOH   HOH C . 
R 5 HOH   49  449 600 HOH   HOH C . 
R 5 HOH   50  450 446 HOH   HOH C . 
R 5 HOH   51  451 222 HOH   HOH C . 
R 5 HOH   52  452 825 HOH   HOH C . 
R 5 HOH   53  453 65  HOH   HOH C . 
R 5 HOH   54  454 249 HOH   HOH C . 
R 5 HOH   55  455 119 HOH   HOH C . 
R 5 HOH   56  456 335 HOH   HOH C . 
R 5 HOH   57  457 448 HOH   HOH C . 
R 5 HOH   58  458 188 HOH   HOH C . 
R 5 HOH   59  459 888 HOH   HOH C . 
R 5 HOH   60  460 331 HOH   HOH C . 
R 5 HOH   61  461 703 HOH   HOH C . 
R 5 HOH   62  462 908 HOH   HOH C . 
R 5 HOH   63  463 221 HOH   HOH C . 
R 5 HOH   64  464 34  HOH   HOH C . 
R 5 HOH   65  465 27  HOH   HOH C . 
R 5 HOH   66  466 441 HOH   HOH C . 
R 5 HOH   67  467 431 HOH   HOH C . 
R 5 HOH   68  468 115 HOH   HOH C . 
R 5 HOH   69  469 697 HOH   HOH C . 
R 5 HOH   70  470 689 HOH   HOH C . 
R 5 HOH   71  471 134 HOH   HOH C . 
R 5 HOH   72  472 676 HOH   HOH C . 
R 5 HOH   73  473 356 HOH   HOH C . 
R 5 HOH   74  474 341 HOH   HOH C . 
R 5 HOH   75  475 409 HOH   HOH C . 
R 5 HOH   76  476 138 HOH   HOH C . 
R 5 HOH   77  477 84  HOH   HOH C . 
R 5 HOH   78  478 114 HOH   HOH C . 
R 5 HOH   79  479 67  HOH   HOH C . 
R 5 HOH   80  480 363 HOH   HOH C . 
R 5 HOH   81  481 921 HOH   HOH C . 
R 5 HOH   82  482 168 HOH   HOH C . 
R 5 HOH   83  483 536 HOH   HOH C . 
R 5 HOH   84  484 98  HOH   HOH C . 
R 5 HOH   85  485 715 HOH   HOH C . 
R 5 HOH   86  486 1   HOH   HOH C . 
R 5 HOH   87  487 640 HOH   HOH C . 
R 5 HOH   88  488 738 HOH   HOH C . 
R 5 HOH   89  489 268 HOH   HOH C . 
R 5 HOH   90  490 452 HOH   HOH C . 
R 5 HOH   91  491 38  HOH   HOH C . 
R 5 HOH   92  492 279 HOH   HOH C . 
R 5 HOH   93  493 339 HOH   HOH C . 
R 5 HOH   94  494 229 HOH   HOH C . 
R 5 HOH   95  495 333 HOH   HOH C . 
R 5 HOH   96  496 614 HOH   HOH C . 
R 5 HOH   97  497 282 HOH   HOH C . 
R 5 HOH   98  498 110 HOH   HOH C . 
R 5 HOH   99  499 76  HOH   HOH C . 
R 5 HOH   100 500 350 HOH   HOH C . 
R 5 HOH   101 501 513 HOH   HOH C . 
R 5 HOH   102 502 301 HOH   HOH C . 
R 5 HOH   103 503 549 HOH   HOH C . 
R 5 HOH   104 504 96  HOH   HOH C . 
R 5 HOH   105 505 11  HOH   HOH C . 
R 5 HOH   106 506 639 HOH   HOH C . 
R 5 HOH   107 507 209 HOH   HOH C . 
R 5 HOH   108 508 103 HOH   HOH C . 
R 5 HOH   109 509 257 HOH   HOH C . 
R 5 HOH   110 510 410 HOH   HOH C . 
R 5 HOH   111 511 817 HOH   HOH C . 
R 5 HOH   112 512 135 HOH   HOH C . 
R 5 HOH   113 513 706 HOH   HOH C . 
R 5 HOH   114 514 461 HOH   HOH C . 
R 5 HOH   115 515 51  HOH   HOH C . 
R 5 HOH   116 516 70  HOH   HOH C . 
R 5 HOH   117 517 717 HOH   HOH C . 
R 5 HOH   118 518 218 HOH   HOH C . 
R 5 HOH   119 519 804 HOH   HOH C . 
R 5 HOH   120 520 274 HOH   HOH C . 
R 5 HOH   121 521 39  HOH   HOH C . 
R 5 HOH   122 522 140 HOH   HOH C . 
R 5 HOH   123 523 136 HOH   HOH C . 
R 5 HOH   124 524 21  HOH   HOH C . 
R 5 HOH   125 525 399 HOH   HOH C . 
R 5 HOH   126 526 383 HOH   HOH C . 
R 5 HOH   127 527 286 HOH   HOH C . 
R 5 HOH   128 528 234 HOH   HOH C . 
R 5 HOH   129 529 276 HOH   HOH C . 
R 5 HOH   130 530 170 HOH   HOH C . 
R 5 HOH   131 531 852 HOH   HOH C . 
R 5 HOH   132 532 319 HOH   HOH C . 
R 5 HOH   133 533 777 HOH   HOH C . 
R 5 HOH   134 534 535 HOH   HOH C . 
R 5 HOH   135 535 527 HOH   HOH C . 
R 5 HOH   136 536 423 HOH   HOH C . 
R 5 HOH   137 537 260 HOH   HOH C . 
R 5 HOH   138 538 602 HOH   HOH C . 
R 5 HOH   139 539 925 HOH   HOH C . 
R 5 HOH   140 540 896 HOH   HOH C . 
R 5 HOH   141 541 502 HOH   HOH C . 
R 5 HOH   142 542 528 HOH   HOH C . 
R 5 HOH   143 543 924 HOH   HOH C . 
R 5 HOH   144 544 668 HOH   HOH C . 
R 5 HOH   145 545 753 HOH   HOH C . 
R 5 HOH   146 546 562 HOH   HOH C . 
R 5 HOH   147 547 713 HOH   HOH C . 
R 5 HOH   148 548 690 HOH   HOH C . 
R 5 HOH   149 549 626 HOH   HOH C . 
R 5 HOH   150 550 647 HOH   HOH C . 
R 5 HOH   151 551 594 HOH   HOH C . 
R 5 HOH   152 552 610 HOH   HOH C . 
R 5 HOH   153 553 477 HOH   HOH C . 
R 5 HOH   154 554 651 HOH   HOH C . 
R 5 HOH   155 555 547 HOH   HOH C . 
R 5 HOH   156 556 806 HOH   HOH C . 
R 5 HOH   157 557 317 HOH   HOH C . 
R 5 HOH   158 558 320 HOH   HOH C . 
R 5 HOH   159 559 644 HOH   HOH C . 
R 5 HOH   160 560 752 HOH   HOH C . 
R 5 HOH   161 561 784 HOH   HOH C . 
R 5 HOH   162 562 694 HOH   HOH C . 
R 5 HOH   163 563 841 HOH   HOH C . 
R 5 HOH   164 564 811 HOH   HOH C . 
R 5 HOH   165 565 907 HOH   HOH C . 
R 5 HOH   166 566 796 HOH   HOH C . 
R 5 HOH   167 567 460 HOH   HOH C . 
R 5 HOH   168 568 478 HOH   HOH C . 
R 5 HOH   169 569 798 HOH   HOH C . 
R 5 HOH   170 570 355 HOH   HOH C . 
R 5 HOH   171 571 891 HOH   HOH C . 
R 5 HOH   172 572 831 HOH   HOH C . 
R 5 HOH   173 573 816 HOH   HOH C . 
R 5 HOH   174 574 453 HOH   HOH C . 
R 5 HOH   175 575 463 HOH   HOH C . 
R 5 HOH   176 576 548 HOH   HOH C . 
R 5 HOH   177 577 681 HOH   HOH C . 
R 5 HOH   178 578 516 HOH   HOH C . 
R 5 HOH   179 579 605 HOH   HOH C . 
R 5 HOH   180 580 732 HOH   HOH C . 
R 5 HOH   181 581 584 HOH   HOH C . 
R 5 HOH   182 582 604 HOH   HOH C . 
R 5 HOH   183 583 851 HOH   HOH C . 
R 5 HOH   184 584 910 HOH   HOH C . 
R 5 HOH   185 585 699 HOH   HOH C . 
R 5 HOH   186 586 631 HOH   HOH C . 
R 5 HOH   187 587 650 HOH   HOH C . 
R 5 HOH   188 588 872 HOH   HOH C . 
R 5 HOH   189 589 857 HOH   HOH C . 
R 5 HOH   190 590 722 HOH   HOH C . 
S 5 HOH   1   401 914 HOH   HOH D . 
S 5 HOH   2   402 240 HOH   HOH D . 
S 5 HOH   3   403 763 HOH   HOH D . 
S 5 HOH   4   404 368 HOH   HOH D . 
S 5 HOH   5   405 50  HOH   HOH D . 
S 5 HOH   6   406 370 HOH   HOH D . 
S 5 HOH   7   407 898 HOH   HOH D . 
S 5 HOH   8   408 52  HOH   HOH D . 
S 5 HOH   9   409 726 HOH   HOH D . 
S 5 HOH   10  410 554 HOH   HOH D . 
S 5 HOH   11  411 698 HOH   HOH D . 
S 5 HOH   12  412 2   HOH   HOH D . 
S 5 HOH   13  413 183 HOH   HOH D . 
S 5 HOH   14  414 388 HOH   HOH D . 
S 5 HOH   15  415 132 HOH   HOH D . 
S 5 HOH   16  416 269 HOH   HOH D . 
S 5 HOH   17  417 680 HOH   HOH D . 
S 5 HOH   18  418 160 HOH   HOH D . 
S 5 HOH   19  419 417 HOH   HOH D . 
S 5 HOH   20  420 756 HOH   HOH D . 
S 5 HOH   21  421 187 HOH   HOH D . 
S 5 HOH   22  422 258 HOH   HOH D . 
S 5 HOH   23  423 66  HOH   HOH D . 
S 5 HOH   24  424 139 HOH   HOH D . 
S 5 HOH   25  425 278 HOH   HOH D . 
S 5 HOH   26  426 205 HOH   HOH D . 
S 5 HOH   27  427 517 HOH   HOH D . 
S 5 HOH   28  428 106 HOH   HOH D . 
S 5 HOH   29  429 17  HOH   HOH D . 
S 5 HOH   30  430 29  HOH   HOH D . 
S 5 HOH   31  431 334 HOH   HOH D . 
S 5 HOH   32  432 241 HOH   HOH D . 
S 5 HOH   33  433 161 HOH   HOH D . 
S 5 HOH   34  434 493 HOH   HOH D . 
S 5 HOH   35  435 64  HOH   HOH D . 
S 5 HOH   36  436 108 HOH   HOH D . 
S 5 HOH   37  437 916 HOH   HOH D . 
S 5 HOH   38  438 499 HOH   HOH D . 
S 5 HOH   39  439 137 HOH   HOH D . 
S 5 HOH   40  440 41  HOH   HOH D . 
S 5 HOH   41  441 526 HOH   HOH D . 
S 5 HOH   42  442 340 HOH   HOH D . 
S 5 HOH   43  443 215 HOH   HOH D . 
S 5 HOH   44  444 146 HOH   HOH D . 
S 5 HOH   45  445 189 HOH   HOH D . 
S 5 HOH   46  446 203 HOH   HOH D . 
S 5 HOH   47  447 200 HOH   HOH D . 
S 5 HOH   48  448 176 HOH   HOH D . 
S 5 HOH   49  449 433 HOH   HOH D . 
S 5 HOH   50  450 214 HOH   HOH D . 
S 5 HOH   51  451 15  HOH   HOH D . 
S 5 HOH   52  452 48  HOH   HOH D . 
S 5 HOH   53  453 262 HOH   HOH D . 
S 5 HOH   54  454 104 HOH   HOH D . 
S 5 HOH   55  455 159 HOH   HOH D . 
S 5 HOH   56  456 178 HOH   HOH D . 
S 5 HOH   57  457 113 HOH   HOH D . 
S 5 HOH   58  458 424 HOH   HOH D . 
S 5 HOH   59  459 415 HOH   HOH D . 
S 5 HOH   60  460 858 HOH   HOH D . 
S 5 HOH   61  461 164 HOH   HOH D . 
S 5 HOH   62  462 380 HOH   HOH D . 
S 5 HOH   63  463 426 HOH   HOH D . 
S 5 HOH   64  464 833 HOH   HOH D . 
S 5 HOH   65  465 430 HOH   HOH D . 
S 5 HOH   66  466 716 HOH   HOH D . 
S 5 HOH   67  467 903 HOH   HOH D . 
S 5 HOH   68  468 275 HOH   HOH D . 
S 5 HOH   69  469 557 HOH   HOH D . 
S 5 HOH   70  470 397 HOH   HOH D . 
S 5 HOH   71  471 733 HOH   HOH D . 
S 5 HOH   72  472 171 HOH   HOH D . 
S 5 HOH   73  473 708 HOH   HOH D . 
S 5 HOH   74  474 35  HOH   HOH D . 
S 5 HOH   75  475 374 HOH   HOH D . 
S 5 HOH   76  476 13  HOH   HOH D . 
S 5 HOH   77  477 354 HOH   HOH D . 
S 5 HOH   78  478 20  HOH   HOH D . 
S 5 HOH   79  479 306 HOH   HOH D . 
S 5 HOH   80  480 358 HOH   HOH D . 
S 5 HOH   81  481 902 HOH   HOH D . 
S 5 HOH   82  482 259 HOH   HOH D . 
S 5 HOH   83  483 357 HOH   HOH D . 
S 5 HOH   84  484 486 HOH   HOH D . 
S 5 HOH   85  485 291 HOH   HOH D . 
S 5 HOH   86  486 153 HOH   HOH D . 
S 5 HOH   87  487 830 HOH   HOH D . 
S 5 HOH   88  488 58  HOH   HOH D . 
S 5 HOH   89  489 141 HOH   HOH D . 
S 5 HOH   90  490 180 HOH   HOH D . 
S 5 HOH   91  491 490 HOH   HOH D . 
S 5 HOH   92  492 287 HOH   HOH D . 
S 5 HOH   93  493 749 HOH   HOH D . 
S 5 HOH   94  494 245 HOH   HOH D . 
S 5 HOH   95  495 779 HOH   HOH D . 
S 5 HOH   96  496 32  HOH   HOH D . 
S 5 HOH   97  497 381 HOH   HOH D . 
S 5 HOH   98  498 598 HOH   HOH D . 
S 5 HOH   99  499 711 HOH   HOH D . 
S 5 HOH   100 500 353 HOH   HOH D . 
S 5 HOH   101 501 174 HOH   HOH D . 
S 5 HOH   102 502 210 HOH   HOH D . 
S 5 HOH   103 503 87  HOH   HOH D . 
S 5 HOH   104 504 231 HOH   HOH D . 
S 5 HOH   105 505 271 HOH   HOH D . 
S 5 HOH   106 506 494 HOH   HOH D . 
S 5 HOH   107 507 488 HOH   HOH D . 
S 5 HOH   108 508 293 HOH   HOH D . 
S 5 HOH   109 509 86  HOH   HOH D . 
S 5 HOH   110 510 212 HOH   HOH D . 
S 5 HOH   111 511 148 HOH   HOH D . 
S 5 HOH   112 512 436 HOH   HOH D . 
S 5 HOH   113 513 321 HOH   HOH D . 
S 5 HOH   114 514 904 HOH   HOH D . 
S 5 HOH   115 515 242 HOH   HOH D . 
S 5 HOH   116 516 122 HOH   HOH D . 
S 5 HOH   117 517 233 HOH   HOH D . 
S 5 HOH   118 518 31  HOH   HOH D . 
S 5 HOH   119 519 440 HOH   HOH D . 
S 5 HOH   120 520 912 HOH   HOH D . 
S 5 HOH   121 521 158 HOH   HOH D . 
S 5 HOH   122 522 759 HOH   HOH D . 
S 5 HOH   123 523 243 HOH   HOH D . 
S 5 HOH   124 524 305 HOH   HOH D . 
S 5 HOH   125 525 709 HOH   HOH D . 
S 5 HOH   126 526 809 HOH   HOH D . 
S 5 HOH   127 527 157 HOH   HOH D . 
S 5 HOH   128 528 284 HOH   HOH D . 
S 5 HOH   129 529 371 HOH   HOH D . 
S 5 HOH   130 530 537 HOH   HOH D . 
S 5 HOH   131 531 901 HOH   HOH D . 
S 5 HOH   132 532 824 HOH   HOH D . 
S 5 HOH   133 533 624 HOH   HOH D . 
S 5 HOH   134 534 454 HOH   HOH D . 
S 5 HOH   135 535 308 HOH   HOH D . 
S 5 HOH   136 536 522 HOH   HOH D . 
S 5 HOH   137 537 520 HOH   HOH D . 
S 5 HOH   138 538 531 HOH   HOH D . 
S 5 HOH   139 539 412 HOH   HOH D . 
S 5 HOH   140 540 832 HOH   HOH D . 
S 5 HOH   141 541 719 HOH   HOH D . 
S 5 HOH   142 542 768 HOH   HOH D . 
S 5 HOH   143 543 662 HOH   HOH D . 
S 5 HOH   144 544 427 HOH   HOH D . 
S 5 HOH   145 545 500 HOH   HOH D . 
S 5 HOH   146 546 439 HOH   HOH D . 
S 5 HOH   147 547 877 HOH   HOH D . 
S 5 HOH   148 548 827 HOH   HOH D . 
S 5 HOH   149 549 672 HOH   HOH D . 
S 5 HOH   150 550 457 HOH   HOH D . 
S 5 HOH   151 551 384 HOH   HOH D . 
S 5 HOH   152 552 836 HOH   HOH D . 
S 5 HOH   153 553 727 HOH   HOH D . 
S 5 HOH   154 554 630 HOH   HOH D . 
S 5 HOH   155 555 582 HOH   HOH D . 
S 5 HOH   156 556 776 HOH   HOH D . 
S 5 HOH   157 557 343 HOH   HOH D . 
S 5 HOH   158 558 869 HOH   HOH D . 
S 5 HOH   159 559 429 HOH   HOH D . 
S 5 HOH   160 560 618 HOH   HOH D . 
S 5 HOH   161 561 616 HOH   HOH D . 
S 5 HOH   162 562 613 HOH   HOH D . 
S 5 HOH   163 563 553 HOH   HOH D . 
S 5 HOH   164 564 512 HOH   HOH D . 
S 5 HOH   165 565 871 HOH   HOH D . 
S 5 HOH   166 566 420 HOH   HOH D . 
S 5 HOH   167 567 705 HOH   HOH D . 
S 5 HOH   168 568 894 HOH   HOH D . 
S 5 HOH   169 569 648 HOH   HOH D . 
S 5 HOH   170 570 330 HOH   HOH D . 
S 5 HOH   171 571 622 HOH   HOH D . 
S 5 HOH   172 572 362 HOH   HOH D . 
S 5 HOH   173 573 671 HOH   HOH D . 
S 5 HOH   174 574 612 HOH   HOH D . 
S 5 HOH   175 575 780 HOH   HOH D . 
S 5 HOH   176 576 359 HOH   HOH D . 
S 5 HOH   177 577 842 HOH   HOH D . 
S 5 HOH   178 578 482 HOH   HOH D . 
S 5 HOH   179 579 523 HOH   HOH D . 
S 5 HOH   180 580 510 HOH   HOH D . 
S 5 HOH   181 581 470 HOH   HOH D . 
S 5 HOH   182 582 611 HOH   HOH D . 
S 5 HOH   183 583 476 HOH   HOH D . 
S 5 HOH   184 584 661 HOH   HOH D . 
S 5 HOH   185 585 628 HOH   HOH D . 
S 5 HOH   186 586 887 HOH   HOH D . 
S 5 HOH   187 587 769 HOH   HOH D . 
S 5 HOH   188 588 691 HOH   HOH D . 
S 5 HOH   189 589 782 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 LYS 50  ? CE  ? A LYS 71  CE  
2  1 Y 1 A LYS 50  ? NZ  ? A LYS 71  NZ  
3  1 Y 1 A GLN 104 ? CG  ? A GLN 125 CG  
4  1 Y 1 A GLN 104 ? CD  ? A GLN 125 CD  
5  1 Y 1 A GLN 104 ? OE1 ? A GLN 125 OE1 
6  1 Y 1 A GLN 104 ? NE2 ? A GLN 125 NE2 
7  1 Y 1 A LYS 143 ? CD  ? A LYS 164 CD  
8  1 Y 1 A LYS 143 ? CE  ? A LYS 164 CE  
9  1 Y 1 A LYS 143 ? NZ  ? A LYS 164 NZ  
10 1 Y 1 A GLU 216 ? CD  ? A GLU 237 CD  
11 1 Y 1 A GLU 216 ? OE1 ? A GLU 237 OE1 
12 1 Y 1 A GLU 216 ? OE2 ? A GLU 237 OE2 
13 1 Y 1 B LYS 143 ? CG  ? B LYS 164 CG  
14 1 Y 1 B LYS 143 ? CD  ? B LYS 164 CD  
15 1 Y 1 B LYS 143 ? CE  ? B LYS 164 CE  
16 1 Y 1 B LYS 143 ? NZ  ? B LYS 164 NZ  
17 1 Y 1 B SER 152 ? OG  ? B SER 173 OG  
18 1 Y 1 B VAL 211 ? CG1 ? B VAL 232 CG1 
19 1 Y 1 B VAL 211 ? CG2 ? B VAL 232 CG2 
20 1 Y 1 C GLU 2   ? CD  ? C GLU 23  CD  
21 1 Y 1 C GLU 2   ? OE1 ? C GLU 23  OE1 
22 1 Y 1 C GLU 2   ? OE2 ? C GLU 23  OE2 
23 1 Y 1 C LYS 50  ? CD  ? C LYS 71  CD  
24 1 Y 1 C LYS 50  ? CE  ? C LYS 71  CE  
25 1 Y 1 C LYS 50  ? NZ  ? C LYS 71  NZ  
26 1 Y 1 C SER 152 ? OG  ? C SER 173 OG  
27 1 Y 1 D LYS 50  ? CG  ? D LYS 71  CG  
28 1 Y 1 D LYS 50  ? CD  ? D LYS 71  CD  
29 1 Y 1 D LYS 50  ? CE  ? D LYS 71  CE  
30 1 Y 1 D LYS 50  ? NZ  ? D LYS 71  NZ  
31 1 Y 1 D GLN 104 ? CG  ? D GLN 125 CG  
32 1 Y 1 D GLN 104 ? CD  ? D GLN 125 CD  
33 1 Y 1 D GLN 104 ? OE1 ? D GLN 125 OE1 
34 1 Y 1 D GLN 104 ? NE2 ? D GLN 125 NE2 
35 1 Y 1 D SER 152 ? OG  ? D SER 173 OG  
36 1 Y 1 D GLU 216 ? CD  ? D GLU 237 CD  
37 1 Y 1 D GLU 216 ? OE1 ? D GLU 237 OE1 
38 1 Y 1 D GLU 216 ? OE2 ? D GLU 237 OE2 
39 1 Y 1 D ARG 230 ? CZ  ? D ARG 251 CZ  
40 1 Y 1 D ARG 230 ? NH1 ? D ARG 251 NH1 
41 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                   115.95 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RHX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.097 
_cell.length_a_esd                 ? 
_cell.length_b                     89.431 
_cell.length_b_esd                 ? 
_cell.length_c                     84.074 
_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                         8RHX 
_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                   8RHX 
_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             1.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.40 
_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         2023-06-22 
_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                    'Si(111)' 
_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   0.88560 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.88560 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          19.0 
_reflns.entry_id                                       8RHX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.48 
_reflns.d_resolution_low                               66.63 
_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                                     163650 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.061 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.047 
_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                                    1.48 
_reflns_shell.d_res_low                                     1.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7985 
_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                               4.1 
_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                               0.726 
_reflns_shell.pdbx_Rpim_I_all                               0.461 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.867 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.555 
_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]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               21.159 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.967 
_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                                 8RHX 
_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                            1.48 
_refine.ls_d_res_low                             66.63 
_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                     155395 
_refine.ls_number_reflns_R_free                  8195 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16426 
_refine.ls_R_factor_R_free                       0.18565 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16310 
_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                       0.066 
_refine.pdbx_overall_ESU_R_Free                  0.066 
_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                             1.257 
_refine.overall_SU_ML                            0.046 
_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                        8RHX 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.15 
_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                       1.48 
_refine_hist.d_res_low                        66.63 
_refine_hist.number_atoms_solvent             751 
_refine_hist.number_atoms_total               8492 
_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        7477 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         264 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  0.012  8195  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.599  1.819  11243 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.933  5.000  1099  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.958  5.000  74    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.189 10.000 1319  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.097  0.200  1334  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  6126  ? 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' ? 1.390  1.856  4128  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.144  3.325  5160  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.015  2.091  4067  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.408  22.95  13179 ? 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                       1.480 
_refine_ls_shell.d_res_low                        1.518 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             613 
_refine_ls_shell.number_reflns_R_work             11324 
_refine_ls_shell.percent_reflns_obs               99.63 
_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                  0.279 
_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                  0.305 
# 
_struct.entry_id                     8RHX 
_struct.title                        'Crystal Structure of Trypanosoma brucei PTR1 in complex with the cofactor and inhibitor P32' 
_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        8RHX 
_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 3 ? 
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 8RHX A 22 ? 289 ? O76290 1 ? 268 ? 1 268 
2 1 8RHX B 22 ? 289 ? O76290 1 ? 268 ? 1 268 
3 1 8RHX C 22 ? 289 ? O76290 1 ? 268 ? 1 268 
4 1 8RHX 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 8RHX MET A 1  ? UNP O76290 ? ? 'initiating methionine' -20 1  
1 8RHX GLY A 2  ? UNP O76290 ? ? 'expression tag'        -19 2  
1 8RHX SER A 3  ? UNP O76290 ? ? 'expression tag'        -18 3  
1 8RHX SER A 4  ? UNP O76290 ? ? 'expression tag'        -17 4  
1 8RHX HIS A 5  ? UNP O76290 ? ? 'expression tag'        -16 5  
1 8RHX HIS A 6  ? UNP O76290 ? ? 'expression tag'        -15 6  
1 8RHX HIS A 7  ? UNP O76290 ? ? 'expression tag'        -14 7  
1 8RHX HIS A 8  ? UNP O76290 ? ? 'expression tag'        -13 8  
1 8RHX HIS A 9  ? UNP O76290 ? ? 'expression tag'        -12 9  
1 8RHX HIS A 10 ? UNP O76290 ? ? 'expression tag'        -11 10 
1 8RHX SER A 11 ? UNP O76290 ? ? 'expression tag'        -10 11 
1 8RHX SER A 12 ? UNP O76290 ? ? 'expression tag'        -9  12 
1 8RHX GLY A 13 ? UNP O76290 ? ? 'expression tag'        -8  13 
1 8RHX LEU A 14 ? UNP O76290 ? ? 'expression tag'        -7  14 
1 8RHX VAL A 15 ? UNP O76290 ? ? 'expression tag'        -6  15 
1 8RHX PRO A 16 ? UNP O76290 ? ? 'expression tag'        -5  16 
1 8RHX ARG A 17 ? UNP O76290 ? ? 'expression tag'        -4  17 
1 8RHX GLY A 18 ? UNP O76290 ? ? 'expression tag'        -3  18 
1 8RHX SER A 19 ? UNP O76290 ? ? 'expression tag'        -2  19 
1 8RHX HIS A 20 ? UNP O76290 ? ? 'expression tag'        -1  20 
1 8RHX MET A 21 ? UNP O76290 ? ? 'expression tag'        0   21 
2 8RHX MET B 1  ? UNP O76290 ? ? 'initiating methionine' -20 22 
2 8RHX GLY B 2  ? UNP O76290 ? ? 'expression tag'        -19 23 
2 8RHX SER B 3  ? UNP O76290 ? ? 'expression tag'        -18 24 
2 8RHX SER B 4  ? UNP O76290 ? ? 'expression tag'        -17 25 
2 8RHX HIS B 5  ? UNP O76290 ? ? 'expression tag'        -16 26 
2 8RHX HIS B 6  ? UNP O76290 ? ? 'expression tag'        -15 27 
2 8RHX HIS B 7  ? UNP O76290 ? ? 'expression tag'        -14 28 
2 8RHX HIS B 8  ? UNP O76290 ? ? 'expression tag'        -13 29 
2 8RHX HIS B 9  ? UNP O76290 ? ? 'expression tag'        -12 30 
2 8RHX HIS B 10 ? UNP O76290 ? ? 'expression tag'        -11 31 
2 8RHX SER B 11 ? UNP O76290 ? ? 'expression tag'        -10 32 
2 8RHX SER B 12 ? UNP O76290 ? ? 'expression tag'        -9  33 
2 8RHX GLY B 13 ? UNP O76290 ? ? 'expression tag'        -8  34 
2 8RHX LEU B 14 ? UNP O76290 ? ? 'expression tag'        -7  35 
2 8RHX VAL B 15 ? UNP O76290 ? ? 'expression tag'        -6  36 
2 8RHX PRO B 16 ? UNP O76290 ? ? 'expression tag'        -5  37 
2 8RHX ARG B 17 ? UNP O76290 ? ? 'expression tag'        -4  38 
2 8RHX GLY B 18 ? UNP O76290 ? ? 'expression tag'        -3  39 
2 8RHX SER B 19 ? UNP O76290 ? ? 'expression tag'        -2  40 
2 8RHX HIS B 20 ? UNP O76290 ? ? 'expression tag'        -1  41 
2 8RHX MET B 21 ? UNP O76290 ? ? 'expression tag'        0   42 
3 8RHX MET C 1  ? UNP O76290 ? ? 'initiating methionine' -20 43 
3 8RHX GLY C 2  ? UNP O76290 ? ? 'expression tag'        -19 44 
3 8RHX SER C 3  ? UNP O76290 ? ? 'expression tag'        -18 45 
3 8RHX SER C 4  ? UNP O76290 ? ? 'expression tag'        -17 46 
3 8RHX HIS C 5  ? UNP O76290 ? ? 'expression tag'        -16 47 
3 8RHX HIS C 6  ? UNP O76290 ? ? 'expression tag'        -15 48 
3 8RHX HIS C 7  ? UNP O76290 ? ? 'expression tag'        -14 49 
3 8RHX HIS C 8  ? UNP O76290 ? ? 'expression tag'        -13 50 
3 8RHX HIS C 9  ? UNP O76290 ? ? 'expression tag'        -12 51 
3 8RHX HIS C 10 ? UNP O76290 ? ? 'expression tag'        -11 52 
3 8RHX SER C 11 ? UNP O76290 ? ? 'expression tag'        -10 53 
3 8RHX SER C 12 ? UNP O76290 ? ? 'expression tag'        -9  54 
3 8RHX GLY C 13 ? UNP O76290 ? ? 'expression tag'        -8  55 
3 8RHX LEU C 14 ? UNP O76290 ? ? 'expression tag'        -7  56 
3 8RHX VAL C 15 ? UNP O76290 ? ? 'expression tag'        -6  57 
3 8RHX PRO C 16 ? UNP O76290 ? ? 'expression tag'        -5  58 
3 8RHX ARG C 17 ? UNP O76290 ? ? 'expression tag'        -4  59 
3 8RHX GLY C 18 ? UNP O76290 ? ? 'expression tag'        -3  60 
3 8RHX SER C 19 ? UNP O76290 ? ? 'expression tag'        -2  61 
3 8RHX HIS C 20 ? UNP O76290 ? ? 'expression tag'        -1  62 
3 8RHX MET C 21 ? UNP O76290 ? ? 'expression tag'        0   63 
4 8RHX MET D 1  ? UNP O76290 ? ? 'initiating methionine' -20 64 
4 8RHX GLY D 2  ? UNP O76290 ? ? 'expression tag'        -19 65 
4 8RHX SER D 3  ? UNP O76290 ? ? 'expression tag'        -18 66 
4 8RHX SER D 4  ? UNP O76290 ? ? 'expression tag'        -17 67 
4 8RHX HIS D 5  ? UNP O76290 ? ? 'expression tag'        -16 68 
4 8RHX HIS D 6  ? UNP O76290 ? ? 'expression tag'        -15 69 
4 8RHX HIS D 7  ? UNP O76290 ? ? 'expression tag'        -14 70 
4 8RHX HIS D 8  ? UNP O76290 ? ? 'expression tag'        -13 71 
4 8RHX HIS D 9  ? UNP O76290 ? ? 'expression tag'        -12 72 
4 8RHX HIS D 10 ? UNP O76290 ? ? 'expression tag'        -11 73 
4 8RHX SER D 11 ? UNP O76290 ? ? 'expression tag'        -10 74 
4 8RHX SER D 12 ? UNP O76290 ? ? 'expression tag'        -9  75 
4 8RHX GLY D 13 ? UNP O76290 ? ? 'expression tag'        -8  76 
4 8RHX LEU D 14 ? UNP O76290 ? ? 'expression tag'        -7  77 
4 8RHX VAL D 15 ? UNP O76290 ? ? 'expression tag'        -6  78 
4 8RHX PRO D 16 ? UNP O76290 ? ? 'expression tag'        -5  79 
4 8RHX ARG D 17 ? UNP O76290 ? ? 'expression tag'        -4  80 
4 8RHX GLY D 18 ? UNP O76290 ? ? 'expression tag'        -3  81 
4 8RHX SER D 19 ? UNP O76290 ? ? 'expression tag'        -2  82 
4 8RHX HIS D 20 ? UNP O76290 ? ? 'expression tag'        -1  83 
4 8RHX 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)' 20310 ? 
1 MORE         -131  ? 
1 'SSA (A^2)'  32510 ? 
# 
_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  ? GLY A 48  ? LYS A 13  GLY A 27  1 ? 15 
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  ? GLY B 48  ? LYS B 13  GLY B 27  1 ? 15 
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 ? GLN B 163 ? ALA B 128 GLN B 142 1 ? 15 
HELX_P HELX_P17 AB8 PHE B 192 ? ALA B 214 ? PHE B 171 ALA B 193 1 ? 23 
HELX_P HELX_P18 AB9 GLY B 235 ? ARG B 244 ? GLY B 214 ARG B 223 1 ? 10 
HELX_P HELX_P19 AC1 SER B 254 ? SER B 267 ? SER B 233 SER B 246 1 ? 14 
HELX_P HELX_P20 AC2 GLY B 268 ? GLN B 271 ? GLY B 247 GLN B 250 5 ? 4  
HELX_P HELX_P21 AC3 GLY B 283 ? VAL B 287 ? GLY B 262 VAL B 266 5 ? 5  
HELX_P HELX_P22 AC4 LYS C 34  ? GLY C 48  ? LYS C 13  GLY C 27  1 ? 15 
HELX_P HELX_P23 AC5 SER C 58  ? ARG C 73  ? SER C 37  ARG C 52  1 ? 16 
HELX_P HELX_P24 AC6 VAL C 89  ? GLY C 106 ? VAL C 68  GLY C 85  1 ? 18 
HELX_P HELX_P25 AC7 THR C 136 ? ALA C 149 ? THR C 115 ALA C 128 1 ? 14 
HELX_P HELX_P26 AC8 ALA C 149 ? GLN C 163 ? ALA C 128 GLN C 142 1 ? 15 
HELX_P HELX_P27 AC9 PHE C 192 ? ALA C 214 ? PHE C 171 ALA C 193 1 ? 23 
HELX_P HELX_P28 AD1 PRO C 215 ? GLY C 217 ? PRO C 194 GLY C 196 5 ? 3  
HELX_P HELX_P29 AD2 GLY C 235 ? ARG C 244 ? GLY C 214 ARG C 223 1 ? 10 
HELX_P HELX_P30 AD3 SER C 254 ? SER C 267 ? SER C 233 SER C 246 1 ? 14 
HELX_P HELX_P31 AD4 GLY C 268 ? GLN C 271 ? GLY C 247 GLN C 250 5 ? 4  
HELX_P HELX_P32 AD5 GLY C 283 ? VAL C 287 ? GLY C 262 VAL C 266 5 ? 5  
HELX_P HELX_P33 AD6 LYS D 34  ? THR D 47  ? LYS D 13  THR D 26  1 ? 14 
HELX_P HELX_P34 AD7 SER D 58  ? ARG D 73  ? SER D 37  ARG D 52  1 ? 16 
HELX_P HELX_P35 AD8 VAL D 89  ? GLY D 106 ? VAL D 68  GLY D 85  1 ? 18 
HELX_P HELX_P36 AD9 THR D 136 ? ALA D 149 ? THR D 115 ALA D 128 1 ? 14 
HELX_P HELX_P37 AE1 ALA D 149 ? ARG D 162 ? ALA D 128 ARG D 141 1 ? 14 
HELX_P HELX_P38 AE2 PHE D 192 ? ALA D 214 ? PHE D 171 ALA D 193 1 ? 23 
HELX_P HELX_P39 AE3 GLY D 235 ? ARG D 244 ? GLY D 214 ARG D 223 1 ? 10 
HELX_P HELX_P40 AE4 SER D 254 ? SER D 267 ? SER D 233 SER D 246 1 ? 14 
HELX_P HELX_P41 AE5 GLY D 268 ? GLN D 271 ? GLY D 247 GLN D 250 5 ? 4  
HELX_P HELX_P42 AE6 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_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 LEU B 175 ? LEU B 180 ? LEU B 154 LEU B 159 
AA2 6 ILE B 218 ? PRO B 225 ? ILE B 197 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 ILE B 278 ? O ILE B 257 
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 ASN D 179 ? N ASN D 158 O ASN D 221 ? O ASN D 200 
AA4 6 7 N ALA D 224 ? N ALA D 203 O ILE D 278 ? O ILE D 257 
# 
_pdbx_entry_details.entry_id                   8RHX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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  ? ? 58.68   -136.00 
2  1 HIS A 35  ? ? -114.00 -72.58  
3  1 ALA A 128 ? ? -137.49 -55.15  
4  1 CYS A 160 ? ? -99.29  -153.70 
5  1 PHE A 171 ? ? -109.60 41.25   
6  1 SER A 207 ? ? -120.35 -135.21 
7  1 ARG B 14  ? ? 57.98   -134.25 
8  1 HIS B 35  ? ? -119.77 -71.63  
9  1 ALA B 128 ? ? -139.36 -55.80  
10 1 CYS B 160 ? ? -95.07  -158.38 
11 1 PHE B 171 ? ? -108.71 44.84   
12 1 SER B 207 ? ? -118.49 -136.69 
13 1 ARG C 14  ? ? 55.09   -132.28 
14 1 HIS C 35  ? ? -112.70 -70.41  
15 1 ALA C 128 ? ? -135.15 -54.75  
16 1 CYS C 160 ? ? -102.98 -154.66 
17 1 SER C 207 ? ? -118.11 -135.90 
18 1 ARG D 14  ? ? 60.37   -134.30 
19 1 ALA D 128 ? ? -136.58 -55.30  
20 1 CYS D 160 ? ? -97.18  -154.01 
21 1 PHE D 171 ? ? -105.89 42.12   
22 1 SER D 207 ? ? -120.41 -133.75 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       590 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.91 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A 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 GLY 105 ? A GLY 126 
24  1 Y 1 A ASP 106 ? A ASP 127 
25  1 Y 1 A HIS 107 ? A HIS 128 
26  1 Y 1 A GLU 108 ? A GLU 129 
27  1 Y 1 A ASP 109 ? A ASP 130 
28  1 Y 1 A ASN 110 ? A ASN 131 
29  1 Y 1 A SER 111 ? A SER 132 
30  1 Y 1 A ASN 112 ? A ASN 133 
31  1 Y 1 A GLY 144 ? A GLY 165 
32  1 Y 1 A THR 145 ? A THR 166 
33  1 Y 1 A ASN 146 ? A ASN 167 
34  1 Y 1 A PRO 147 ? A PRO 168 
35  1 Y 1 A ASN 148 ? A ASN 169 
36  1 Y 1 A CYS 149 ? A CYS 170 
37  1 Y 1 A THR 150 ? A THR 171 
38  1 Y 1 A SER 151 ? A SER 172 
39  1 Y 1 B MET -20 ? B MET 1   
40  1 Y 1 B GLY -19 ? B GLY 2   
41  1 Y 1 B SER -18 ? B SER 3   
42  1 Y 1 B SER -17 ? B SER 4   
43  1 Y 1 B HIS -16 ? B HIS 5   
44  1 Y 1 B HIS -15 ? B HIS 6   
45  1 Y 1 B HIS -14 ? B HIS 7   
46  1 Y 1 B HIS -13 ? B HIS 8   
47  1 Y 1 B HIS -12 ? B HIS 9   
48  1 Y 1 B HIS -11 ? B HIS 10  
49  1 Y 1 B SER -10 ? B SER 11  
50  1 Y 1 B SER -9  ? B SER 12  
51  1 Y 1 B GLY -8  ? B GLY 13  
52  1 Y 1 B LEU -7  ? B LEU 14  
53  1 Y 1 B GLN 104 ? B GLN 125 
54  1 Y 1 B GLY 105 ? B GLY 126 
55  1 Y 1 B ASP 106 ? B ASP 127 
56  1 Y 1 B HIS 107 ? B HIS 128 
57  1 Y 1 B GLU 108 ? B GLU 129 
58  1 Y 1 B ASP 109 ? B ASP 130 
59  1 Y 1 B ASN 110 ? B ASN 131 
60  1 Y 1 B SER 111 ? B SER 132 
61  1 Y 1 B ASN 112 ? B ASN 133 
62  1 Y 1 B GLY 144 ? B GLY 165 
63  1 Y 1 B THR 145 ? B THR 166 
64  1 Y 1 B ASN 146 ? B ASN 167 
65  1 Y 1 B PRO 147 ? B PRO 168 
66  1 Y 1 B ASN 148 ? B ASN 169 
67  1 Y 1 B CYS 149 ? B CYS 170 
68  1 Y 1 B THR 150 ? B THR 171 
69  1 Y 1 B SER 151 ? B SER 172 
70  1 Y 1 C MET -20 ? C MET 1   
71  1 Y 1 C GLY -19 ? C GLY 2   
72  1 Y 1 C SER -18 ? C SER 3   
73  1 Y 1 C SER -17 ? C SER 4   
74  1 Y 1 C HIS -16 ? C HIS 5   
75  1 Y 1 C HIS -15 ? C HIS 6   
76  1 Y 1 C HIS -14 ? C HIS 7   
77  1 Y 1 C HIS -13 ? C HIS 8   
78  1 Y 1 C HIS -12 ? C HIS 9   
79  1 Y 1 C HIS -11 ? C HIS 10  
80  1 Y 1 C SER -10 ? C SER 11  
81  1 Y 1 C SER -9  ? C SER 12  
82  1 Y 1 C GLY -8  ? C GLY 13  
83  1 Y 1 C LEU -7  ? C LEU 14  
84  1 Y 1 C VAL -6  ? C VAL 15  
85  1 Y 1 C PRO -5  ? C PRO 16  
86  1 Y 1 C ARG -4  ? C ARG 17  
87  1 Y 1 C GLY -3  ? C GLY 18  
88  1 Y 1 C SER -2  ? C SER 19  
89  1 Y 1 C HIS -1  ? C HIS 20  
90  1 Y 1 C MET 0   ? C MET 21  
91  1 Y 1 C MET 1   ? C MET 22  
92  1 Y 1 C GLY 105 ? C GLY 126 
93  1 Y 1 C ASP 106 ? C ASP 127 
94  1 Y 1 C HIS 107 ? C HIS 128 
95  1 Y 1 C GLU 108 ? C GLU 129 
96  1 Y 1 C ASP 109 ? C ASP 130 
97  1 Y 1 C ASN 110 ? C ASN 131 
98  1 Y 1 C SER 111 ? C SER 132 
99  1 Y 1 C ASN 112 ? C ASN 133 
100 1 Y 1 C GLY 113 ? C GLY 134 
101 1 Y 1 C LYS 143 ? C LYS 164 
102 1 Y 1 C GLY 144 ? C GLY 165 
103 1 Y 1 C THR 145 ? C THR 166 
104 1 Y 1 C ASN 146 ? C ASN 167 
105 1 Y 1 C PRO 147 ? C PRO 168 
106 1 Y 1 C ASN 148 ? C ASN 169 
107 1 Y 1 C CYS 149 ? C CYS 170 
108 1 Y 1 C THR 150 ? C THR 171 
109 1 Y 1 C SER 151 ? C SER 172 
110 1 Y 1 D MET -20 ? D MET 1   
111 1 Y 1 D GLY -19 ? D GLY 2   
112 1 Y 1 D SER -18 ? D SER 3   
113 1 Y 1 D SER -17 ? D SER 4   
114 1 Y 1 D HIS -16 ? D HIS 5   
115 1 Y 1 D HIS -15 ? D HIS 6   
116 1 Y 1 D HIS -14 ? D HIS 7   
117 1 Y 1 D HIS -13 ? D HIS 8   
118 1 Y 1 D HIS -12 ? D HIS 9   
119 1 Y 1 D HIS -11 ? D HIS 10  
120 1 Y 1 D SER -10 ? D SER 11  
121 1 Y 1 D SER -9  ? D SER 12  
122 1 Y 1 D GLY -8  ? D GLY 13  
123 1 Y 1 D LEU -7  ? D LEU 14  
124 1 Y 1 D VAL -6  ? D VAL 15  
125 1 Y 1 D PRO -5  ? D PRO 16  
126 1 Y 1 D ARG -4  ? D ARG 17  
127 1 Y 1 D GLY -3  ? D GLY 18  
128 1 Y 1 D SER -2  ? D SER 19  
129 1 Y 1 D HIS -1  ? D HIS 20  
130 1 Y 1 D MET 0   ? D MET 21  
131 1 Y 1 D MET 1   ? D MET 22  
132 1 Y 1 D GLY 105 ? D GLY 126 
133 1 Y 1 D ASP 106 ? D ASP 127 
134 1 Y 1 D HIS 107 ? D HIS 128 
135 1 Y 1 D GLU 108 ? D GLU 129 
136 1 Y 1 D ASP 109 ? D ASP 130 
137 1 Y 1 D ASN 110 ? D ASN 131 
138 1 Y 1 D SER 111 ? D SER 132 
139 1 Y 1 D ASN 112 ? D ASN 133 
140 1 Y 1 D LYS 143 ? D LYS 164 
141 1 Y 1 D GLY 144 ? D GLY 165 
142 1 Y 1 D THR 145 ? D THR 166 
143 1 Y 1 D ASN 146 ? D ASN 167 
144 1 Y 1 D PRO 147 ? D PRO 168 
145 1 Y 1 D ASN 148 ? D ASN 169 
146 1 Y 1 D CYS 149 ? D CYS 170 
147 1 Y 1 D THR 150 ? D THR 171 
148 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 
A1H0T NAI  N  Y N 1   
A1H0T CAF  C  Y N 2   
A1H0T CAE  C  Y N 3   
A1H0T CLAH CL N N 4   
A1H0T CAD  C  Y N 5   
A1H0T CAA  C  Y N 6   
A1H0T CLAB CL N N 7   
A1H0T CAG  C  Y N 8   
A1H0T CAC  C  Y N 9   
A1H0T NAK  N  Y N 10  
A1H0T CAJ  C  Y N 11  
A1H0T NAL  N  N N 12  
A1H0T CAM  C  N N 13  
A1H0T NAO  N  N N 14  
A1H0T NAN  N  N N 15  
A1H0T H2   H  N N 16  
A1H0T H3   H  N N 17  
A1H0T H4   H  N N 18  
A1H0T H5   H  N N 19  
A1H0T H6   H  N N 20  
A1H0T H7   H  N N 21  
A1H0T H8   H  N N 22  
ACT   C    C  N N 23  
ACT   O    O  N N 24  
ACT   OXT  O  N N 25  
ACT   CH3  C  N N 26  
ACT   H1   H  N N 27  
ACT   H2   H  N N 28  
ACT   H3   H  N N 29  
ALA   N    N  N N 30  
ALA   CA   C  N S 31  
ALA   C    C  N N 32  
ALA   O    O  N N 33  
ALA   CB   C  N N 34  
ALA   OXT  O  N N 35  
ALA   H    H  N N 36  
ALA   H2   H  N N 37  
ALA   HA   H  N N 38  
ALA   HB1  H  N N 39  
ALA   HB2  H  N N 40  
ALA   HB3  H  N N 41  
ALA   HXT  H  N N 42  
ARG   N    N  N N 43  
ARG   CA   C  N S 44  
ARG   C    C  N N 45  
ARG   O    O  N N 46  
ARG   CB   C  N N 47  
ARG   CG   C  N N 48  
ARG   CD   C  N N 49  
ARG   NE   N  N N 50  
ARG   CZ   C  N N 51  
ARG   NH1  N  N N 52  
ARG   NH2  N  N N 53  
ARG   OXT  O  N N 54  
ARG   H    H  N N 55  
ARG   H2   H  N N 56  
ARG   HA   H  N N 57  
ARG   HB2  H  N N 58  
ARG   HB3  H  N N 59  
ARG   HG2  H  N N 60  
ARG   HG3  H  N N 61  
ARG   HD2  H  N N 62  
ARG   HD3  H  N N 63  
ARG   HE   H  N N 64  
ARG   HH11 H  N N 65  
ARG   HH12 H  N N 66  
ARG   HH21 H  N N 67  
ARG   HH22 H  N N 68  
ARG   HXT  H  N N 69  
ASN   N    N  N N 70  
ASN   CA   C  N S 71  
ASN   C    C  N N 72  
ASN   O    O  N N 73  
ASN   CB   C  N N 74  
ASN   CG   C  N N 75  
ASN   OD1  O  N N 76  
ASN   ND2  N  N N 77  
ASN   OXT  O  N N 78  
ASN   H    H  N N 79  
ASN   H2   H  N N 80  
ASN   HA   H  N N 81  
ASN   HB2  H  N N 82  
ASN   HB3  H  N N 83  
ASN   HD21 H  N N 84  
ASN   HD22 H  N N 85  
ASN   HXT  H  N N 86  
ASP   N    N  N N 87  
ASP   CA   C  N S 88  
ASP   C    C  N N 89  
ASP   O    O  N N 90  
ASP   CB   C  N N 91  
ASP   CG   C  N N 92  
ASP   OD1  O  N N 93  
ASP   OD2  O  N N 94  
ASP   OXT  O  N N 95  
ASP   H    H  N N 96  
ASP   H2   H  N N 97  
ASP   HA   H  N N 98  
ASP   HB2  H  N N 99  
ASP   HB3  H  N N 100 
ASP   HD2  H  N N 101 
ASP   HXT  H  N N 102 
CYS   N    N  N N 103 
CYS   CA   C  N R 104 
CYS   C    C  N N 105 
CYS   O    O  N N 106 
CYS   CB   C  N N 107 
CYS   SG   S  N N 108 
CYS   OXT  O  N N 109 
CYS   H    H  N N 110 
CYS   H2   H  N N 111 
CYS   HA   H  N N 112 
CYS   HB2  H  N N 113 
CYS   HB3  H  N N 114 
CYS   HG   H  N N 115 
CYS   HXT  H  N N 116 
GLN   N    N  N N 117 
GLN   CA   C  N S 118 
GLN   C    C  N N 119 
GLN   O    O  N N 120 
GLN   CB   C  N N 121 
GLN   CG   C  N N 122 
GLN   CD   C  N N 123 
GLN   OE1  O  N N 124 
GLN   NE2  N  N N 125 
GLN   OXT  O  N N 126 
GLN   H    H  N N 127 
GLN   H2   H  N N 128 
GLN   HA   H  N N 129 
GLN   HB2  H  N N 130 
GLN   HB3  H  N N 131 
GLN   HG2  H  N N 132 
GLN   HG3  H  N N 133 
GLN   HE21 H  N N 134 
GLN   HE22 H  N N 135 
GLN   HXT  H  N N 136 
GLU   N    N  N N 137 
GLU   CA   C  N S 138 
GLU   C    C  N N 139 
GLU   O    O  N N 140 
GLU   CB   C  N N 141 
GLU   CG   C  N N 142 
GLU   CD   C  N N 143 
GLU   OE1  O  N N 144 
GLU   OE2  O  N N 145 
GLU   OXT  O  N N 146 
GLU   H    H  N N 147 
GLU   H2   H  N N 148 
GLU   HA   H  N N 149 
GLU   HB2  H  N N 150 
GLU   HB3  H  N N 151 
GLU   HG2  H  N N 152 
GLU   HG3  H  N N 153 
GLU   HE2  H  N N 154 
GLU   HXT  H  N N 155 
GLY   N    N  N N 156 
GLY   CA   C  N N 157 
GLY   C    C  N N 158 
GLY   O    O  N N 159 
GLY   OXT  O  N N 160 
GLY   H    H  N N 161 
GLY   H2   H  N N 162 
GLY   HA2  H  N N 163 
GLY   HA3  H  N N 164 
GLY   HXT  H  N N 165 
HIS   N    N  N N 166 
HIS   CA   C  N S 167 
HIS   C    C  N N 168 
HIS   O    O  N N 169 
HIS   CB   C  N N 170 
HIS   CG   C  Y N 171 
HIS   ND1  N  Y N 172 
HIS   CD2  C  Y N 173 
HIS   CE1  C  Y N 174 
HIS   NE2  N  Y N 175 
HIS   OXT  O  N N 176 
HIS   H    H  N N 177 
HIS   H2   H  N N 178 
HIS   HA   H  N N 179 
HIS   HB2  H  N N 180 
HIS   HB3  H  N N 181 
HIS   HD1  H  N N 182 
HIS   HD2  H  N N 183 
HIS   HE1  H  N N 184 
HIS   HE2  H  N N 185 
HIS   HXT  H  N N 186 
HOH   O    O  N N 187 
HOH   H1   H  N N 188 
HOH   H2   H  N N 189 
ILE   N    N  N N 190 
ILE   CA   C  N S 191 
ILE   C    C  N N 192 
ILE   O    O  N N 193 
ILE   CB   C  N S 194 
ILE   CG1  C  N N 195 
ILE   CG2  C  N N 196 
ILE   CD1  C  N N 197 
ILE   OXT  O  N N 198 
ILE   H    H  N N 199 
ILE   H2   H  N N 200 
ILE   HA   H  N N 201 
ILE   HB   H  N N 202 
ILE   HG12 H  N N 203 
ILE   HG13 H  N N 204 
ILE   HG21 H  N N 205 
ILE   HG22 H  N N 206 
ILE   HG23 H  N N 207 
ILE   HD11 H  N N 208 
ILE   HD12 H  N N 209 
ILE   HD13 H  N N 210 
ILE   HXT  H  N N 211 
LEU   N    N  N N 212 
LEU   CA   C  N S 213 
LEU   C    C  N N 214 
LEU   O    O  N N 215 
LEU   CB   C  N N 216 
LEU   CG   C  N N 217 
LEU   CD1  C  N N 218 
LEU   CD2  C  N N 219 
LEU   OXT  O  N N 220 
LEU   H    H  N N 221 
LEU   H2   H  N N 222 
LEU   HA   H  N N 223 
LEU   HB2  H  N N 224 
LEU   HB3  H  N N 225 
LEU   HG   H  N N 226 
LEU   HD11 H  N N 227 
LEU   HD12 H  N N 228 
LEU   HD13 H  N N 229 
LEU   HD21 H  N N 230 
LEU   HD22 H  N N 231 
LEU   HD23 H  N N 232 
LEU   HXT  H  N N 233 
LYS   N    N  N N 234 
LYS   CA   C  N S 235 
LYS   C    C  N N 236 
LYS   O    O  N N 237 
LYS   CB   C  N N 238 
LYS   CG   C  N N 239 
LYS   CD   C  N N 240 
LYS   CE   C  N N 241 
LYS   NZ   N  N N 242 
LYS   OXT  O  N N 243 
LYS   H    H  N N 244 
LYS   H2   H  N N 245 
LYS   HA   H  N N 246 
LYS   HB2  H  N N 247 
LYS   HB3  H  N N 248 
LYS   HG2  H  N N 249 
LYS   HG3  H  N N 250 
LYS   HD2  H  N N 251 
LYS   HD3  H  N N 252 
LYS   HE2  H  N N 253 
LYS   HE3  H  N N 254 
LYS   HZ1  H  N N 255 
LYS   HZ2  H  N N 256 
LYS   HZ3  H  N N 257 
LYS   HXT  H  N N 258 
MET   N    N  N N 259 
MET   CA   C  N S 260 
MET   C    C  N N 261 
MET   O    O  N N 262 
MET   CB   C  N N 263 
MET   CG   C  N N 264 
MET   SD   S  N N 265 
MET   CE   C  N N 266 
MET   OXT  O  N N 267 
MET   H    H  N N 268 
MET   H2   H  N N 269 
MET   HA   H  N N 270 
MET   HB2  H  N N 271 
MET   HB3  H  N N 272 
MET   HG2  H  N N 273 
MET   HG3  H  N N 274 
MET   HE1  H  N N 275 
MET   HE2  H  N N 276 
MET   HE3  H  N N 277 
MET   HXT  H  N N 278 
NDP   PA   P  N S 279 
NDP   O1A  O  N N 280 
NDP   O2A  O  N N 281 
NDP   O5B  O  N N 282 
NDP   C5B  C  N N 283 
NDP   C4B  C  N R 284 
NDP   O4B  O  N N 285 
NDP   C3B  C  N R 286 
NDP   O3B  O  N N 287 
NDP   C2B  C  N R 288 
NDP   O2B  O  N N 289 
NDP   C1B  C  N R 290 
NDP   N9A  N  Y N 291 
NDP   C8A  C  Y N 292 
NDP   N7A  N  Y N 293 
NDP   C5A  C  Y N 294 
NDP   C6A  C  Y N 295 
NDP   N6A  N  N N 296 
NDP   N1A  N  Y N 297 
NDP   C2A  C  Y N 298 
NDP   N3A  N  Y N 299 
NDP   C4A  C  Y N 300 
NDP   O3   O  N N 301 
NDP   PN   P  N S 302 
NDP   O1N  O  N N 303 
NDP   O2N  O  N N 304 
NDP   O5D  O  N N 305 
NDP   C5D  C  N N 306 
NDP   C4D  C  N R 307 
NDP   O4D  O  N N 308 
NDP   C3D  C  N S 309 
NDP   O3D  O  N N 310 
NDP   C2D  C  N R 311 
NDP   O2D  O  N N 312 
NDP   C1D  C  N R 313 
NDP   N1N  N  N N 314 
NDP   C2N  C  N N 315 
NDP   C3N  C  N N 316 
NDP   C7N  C  N N 317 
NDP   O7N  O  N N 318 
NDP   N7N  N  N N 319 
NDP   C4N  C  N N 320 
NDP   C5N  C  N N 321 
NDP   C6N  C  N N 322 
NDP   P2B  P  N N 323 
NDP   O1X  O  N N 324 
NDP   O2X  O  N N 325 
NDP   O3X  O  N N 326 
NDP   HOA2 H  N N 327 
NDP   H51A H  N N 328 
NDP   H52A H  N N 329 
NDP   H4B  H  N N 330 
NDP   H3B  H  N N 331 
NDP   HO3A H  N N 332 
NDP   H2B  H  N N 333 
NDP   H1B  H  N N 334 
NDP   H8A  H  N N 335 
NDP   H61A H  N N 336 
NDP   H62A H  N N 337 
NDP   H2A  H  N N 338 
NDP   H21N H  N N 339 
NDP   H51N H  N N 340 
NDP   H52N H  N N 341 
NDP   H4D  H  N N 342 
NDP   H3D  H  N N 343 
NDP   HO3N H  N N 344 
NDP   H2D  H  N N 345 
NDP   HO2N H  N N 346 
NDP   H1D  H  N N 347 
NDP   H2N  H  N N 348 
NDP   H71N H  N N 349 
NDP   H72N H  N N 350 
NDP   H41N H  N N 351 
NDP   H42N H  N N 352 
NDP   H5N  H  N N 353 
NDP   H6N  H  N N 354 
NDP   HOP2 H  N N 355 
NDP   HOP3 H  N N 356 
PHE   N    N  N N 357 
PHE   CA   C  N S 358 
PHE   C    C  N N 359 
PHE   O    O  N N 360 
PHE   CB   C  N N 361 
PHE   CG   C  Y N 362 
PHE   CD1  C  Y N 363 
PHE   CD2  C  Y N 364 
PHE   CE1  C  Y N 365 
PHE   CE2  C  Y N 366 
PHE   CZ   C  Y N 367 
PHE   OXT  O  N N 368 
PHE   H    H  N N 369 
PHE   H2   H  N N 370 
PHE   HA   H  N N 371 
PHE   HB2  H  N N 372 
PHE   HB3  H  N N 373 
PHE   HD1  H  N N 374 
PHE   HD2  H  N N 375 
PHE   HE1  H  N N 376 
PHE   HE2  H  N N 377 
PHE   HZ   H  N N 378 
PHE   HXT  H  N N 379 
PRO   N    N  N N 380 
PRO   CA   C  N S 381 
PRO   C    C  N N 382 
PRO   O    O  N N 383 
PRO   CB   C  N N 384 
PRO   CG   C  N N 385 
PRO   CD   C  N N 386 
PRO   OXT  O  N N 387 
PRO   H    H  N N 388 
PRO   HA   H  N N 389 
PRO   HB2  H  N N 390 
PRO   HB3  H  N N 391 
PRO   HG2  H  N N 392 
PRO   HG3  H  N N 393 
PRO   HD2  H  N N 394 
PRO   HD3  H  N N 395 
PRO   HXT  H  N N 396 
SER   N    N  N N 397 
SER   CA   C  N S 398 
SER   C    C  N N 399 
SER   O    O  N N 400 
SER   CB   C  N N 401 
SER   OG   O  N N 402 
SER   OXT  O  N N 403 
SER   H    H  N N 404 
SER   H2   H  N N 405 
SER   HA   H  N N 406 
SER   HB2  H  N N 407 
SER   HB3  H  N N 408 
SER   HG   H  N N 409 
SER   HXT  H  N N 410 
THR   N    N  N N 411 
THR   CA   C  N S 412 
THR   C    C  N N 413 
THR   O    O  N N 414 
THR   CB   C  N R 415 
THR   OG1  O  N N 416 
THR   CG2  C  N N 417 
THR   OXT  O  N N 418 
THR   H    H  N N 419 
THR   H2   H  N N 420 
THR   HA   H  N N 421 
THR   HB   H  N N 422 
THR   HG1  H  N N 423 
THR   HG21 H  N N 424 
THR   HG22 H  N N 425 
THR   HG23 H  N N 426 
THR   HXT  H  N N 427 
TRP   N    N  N N 428 
TRP   CA   C  N S 429 
TRP   C    C  N N 430 
TRP   O    O  N N 431 
TRP   CB   C  N N 432 
TRP   CG   C  Y N 433 
TRP   CD1  C  Y N 434 
TRP   CD2  C  Y N 435 
TRP   NE1  N  Y N 436 
TRP   CE2  C  Y N 437 
TRP   CE3  C  Y N 438 
TRP   CZ2  C  Y N 439 
TRP   CZ3  C  Y N 440 
TRP   CH2  C  Y N 441 
TRP   OXT  O  N N 442 
TRP   H    H  N N 443 
TRP   H2   H  N N 444 
TRP   HA   H  N N 445 
TRP   HB2  H  N N 446 
TRP   HB3  H  N N 447 
TRP   HD1  H  N N 448 
TRP   HE1  H  N N 449 
TRP   HE3  H  N N 450 
TRP   HZ2  H  N N 451 
TRP   HZ3  H  N N 452 
TRP   HH2  H  N N 453 
TRP   HXT  H  N N 454 
TYR   N    N  N N 455 
TYR   CA   C  N S 456 
TYR   C    C  N N 457 
TYR   O    O  N N 458 
TYR   CB   C  N N 459 
TYR   CG   C  Y N 460 
TYR   CD1  C  Y N 461 
TYR   CD2  C  Y N 462 
TYR   CE1  C  Y N 463 
TYR   CE2  C  Y N 464 
TYR   CZ   C  Y N 465 
TYR   OH   O  N N 466 
TYR   OXT  O  N N 467 
TYR   H    H  N N 468 
TYR   H2   H  N N 469 
TYR   HA   H  N N 470 
TYR   HB2  H  N N 471 
TYR   HB3  H  N N 472 
TYR   HD1  H  N N 473 
TYR   HD2  H  N N 474 
TYR   HE1  H  N N 475 
TYR   HE2  H  N N 476 
TYR   HH   H  N N 477 
TYR   HXT  H  N N 478 
VAL   N    N  N N 479 
VAL   CA   C  N S 480 
VAL   C    C  N N 481 
VAL   O    O  N N 482 
VAL   CB   C  N N 483 
VAL   CG1  C  N N 484 
VAL   CG2  C  N N 485 
VAL   OXT  O  N N 486 
VAL   H    H  N N 487 
VAL   H2   H  N N 488 
VAL   HA   H  N N 489 
VAL   HB   H  N N 490 
VAL   HG11 H  N N 491 
VAL   HG12 H  N N 492 
VAL   HG13 H  N N 493 
VAL   HG21 H  N N 494 
VAL   HG22 H  N N 495 
VAL   HG23 H  N N 496 
VAL   HXT  H  N N 497 
# 
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 
A1H0T CLAH CAE  sing N N 1   
A1H0T NAN  CAM  doub N N 2   
A1H0T CAE  CAF  doub Y N 3   
A1H0T CAE  CAD  sing Y N 4   
A1H0T NAI  CAF  sing Y N 5   
A1H0T NAI  CAJ  doub Y N 6   
A1H0T CAM  NAO  sing N N 7   
A1H0T CAM  NAL  sing N N 8   
A1H0T CAF  CAC  sing Y N 9   
A1H0T CAD  CAA  doub Y N 10  
A1H0T CAJ  NAL  sing N N 11  
A1H0T CAJ  NAK  sing Y N 12  
A1H0T CAC  NAK  sing Y N 13  
A1H0T CAC  CAG  doub Y N 14  
A1H0T CAA  CAG  sing Y N 15  
A1H0T CAA  CLAB sing N N 16  
A1H0T CAD  H2   sing N N 17  
A1H0T CAG  H3   sing N N 18  
A1H0T NAK  H4   sing N N 19  
A1H0T NAL  H5   sing N N 20  
A1H0T NAO  H6   sing N N 21  
A1H0T NAO  H7   sing N N 22  
A1H0T NAN  H8   sing N N 23  
ACT   C    O    doub N N 24  
ACT   C    OXT  sing N N 25  
ACT   C    CH3  sing N N 26  
ACT   CH3  H1   sing N N 27  
ACT   CH3  H2   sing N N 28  
ACT   CH3  H3   sing N N 29  
ALA   N    CA   sing N N 30  
ALA   N    H    sing N N 31  
ALA   N    H2   sing N N 32  
ALA   CA   C    sing N N 33  
ALA   CA   CB   sing N N 34  
ALA   CA   HA   sing N N 35  
ALA   C    O    doub N N 36  
ALA   C    OXT  sing N N 37  
ALA   CB   HB1  sing N N 38  
ALA   CB   HB2  sing N N 39  
ALA   CB   HB3  sing N N 40  
ALA   OXT  HXT  sing N N 41  
ARG   N    CA   sing N N 42  
ARG   N    H    sing N N 43  
ARG   N    H2   sing N N 44  
ARG   CA   C    sing N N 45  
ARG   CA   CB   sing N N 46  
ARG   CA   HA   sing N N 47  
ARG   C    O    doub N N 48  
ARG   C    OXT  sing N N 49  
ARG   CB   CG   sing N N 50  
ARG   CB   HB2  sing N N 51  
ARG   CB   HB3  sing N N 52  
ARG   CG   CD   sing N N 53  
ARG   CG   HG2  sing N N 54  
ARG   CG   HG3  sing N N 55  
ARG   CD   NE   sing N N 56  
ARG   CD   HD2  sing N N 57  
ARG   CD   HD3  sing N N 58  
ARG   NE   CZ   sing N N 59  
ARG   NE   HE   sing N N 60  
ARG   CZ   NH1  sing N N 61  
ARG   CZ   NH2  doub N N 62  
ARG   NH1  HH11 sing N N 63  
ARG   NH1  HH12 sing N N 64  
ARG   NH2  HH21 sing N N 65  
ARG   NH2  HH22 sing N N 66  
ARG   OXT  HXT  sing N N 67  
ASN   N    CA   sing N N 68  
ASN   N    H    sing N N 69  
ASN   N    H2   sing N N 70  
ASN   CA   C    sing N N 71  
ASN   CA   CB   sing N N 72  
ASN   CA   HA   sing N N 73  
ASN   C    O    doub N N 74  
ASN   C    OXT  sing N N 75  
ASN   CB   CG   sing N N 76  
ASN   CB   HB2  sing N N 77  
ASN   CB   HB3  sing N N 78  
ASN   CG   OD1  doub N N 79  
ASN   CG   ND2  sing N N 80  
ASN   ND2  HD21 sing N N 81  
ASN   ND2  HD22 sing N N 82  
ASN   OXT  HXT  sing N N 83  
ASP   N    CA   sing N N 84  
ASP   N    H    sing N N 85  
ASP   N    H2   sing N N 86  
ASP   CA   C    sing N N 87  
ASP   CA   CB   sing N N 88  
ASP   CA   HA   sing N N 89  
ASP   C    O    doub N N 90  
ASP   C    OXT  sing N N 91  
ASP   CB   CG   sing N N 92  
ASP   CB   HB2  sing N N 93  
ASP   CB   HB3  sing N N 94  
ASP   CG   OD1  doub N N 95  
ASP   CG   OD2  sing N N 96  
ASP   OD2  HD2  sing N N 97  
ASP   OXT  HXT  sing N N 98  
CYS   N    CA   sing N N 99  
CYS   N    H    sing N N 100 
CYS   N    H2   sing N N 101 
CYS   CA   C    sing N N 102 
CYS   CA   CB   sing N N 103 
CYS   CA   HA   sing N N 104 
CYS   C    O    doub N N 105 
CYS   C    OXT  sing N N 106 
CYS   CB   SG   sing N N 107 
CYS   CB   HB2  sing N N 108 
CYS   CB   HB3  sing N N 109 
CYS   SG   HG   sing N N 110 
CYS   OXT  HXT  sing N N 111 
GLN   N    CA   sing N N 112 
GLN   N    H    sing N N 113 
GLN   N    H2   sing N N 114 
GLN   CA   C    sing N N 115 
GLN   CA   CB   sing N N 116 
GLN   CA   HA   sing N N 117 
GLN   C    O    doub N N 118 
GLN   C    OXT  sing N N 119 
GLN   CB   CG   sing N N 120 
GLN   CB   HB2  sing N N 121 
GLN   CB   HB3  sing N N 122 
GLN   CG   CD   sing N N 123 
GLN   CG   HG2  sing N N 124 
GLN   CG   HG3  sing N N 125 
GLN   CD   OE1  doub N N 126 
GLN   CD   NE2  sing N N 127 
GLN   NE2  HE21 sing N N 128 
GLN   NE2  HE22 sing N N 129 
GLN   OXT  HXT  sing N N 130 
GLU   N    CA   sing N N 131 
GLU   N    H    sing N N 132 
GLU   N    H2   sing N N 133 
GLU   CA   C    sing N N 134 
GLU   CA   CB   sing N N 135 
GLU   CA   HA   sing N N 136 
GLU   C    O    doub N N 137 
GLU   C    OXT  sing N N 138 
GLU   CB   CG   sing N N 139 
GLU   CB   HB2  sing N N 140 
GLU   CB   HB3  sing N N 141 
GLU   CG   CD   sing N N 142 
GLU   CG   HG2  sing N N 143 
GLU   CG   HG3  sing N N 144 
GLU   CD   OE1  doub N N 145 
GLU   CD   OE2  sing N N 146 
GLU   OE2  HE2  sing N N 147 
GLU   OXT  HXT  sing N N 148 
GLY   N    CA   sing N N 149 
GLY   N    H    sing N N 150 
GLY   N    H2   sing N N 151 
GLY   CA   C    sing N N 152 
GLY   CA   HA2  sing N N 153 
GLY   CA   HA3  sing N N 154 
GLY   C    O    doub N N 155 
GLY   C    OXT  sing N N 156 
GLY   OXT  HXT  sing N N 157 
HIS   N    CA   sing N N 158 
HIS   N    H    sing N N 159 
HIS   N    H2   sing N N 160 
HIS   CA   C    sing N N 161 
HIS   CA   CB   sing N N 162 
HIS   CA   HA   sing N N 163 
HIS   C    O    doub N N 164 
HIS   C    OXT  sing N N 165 
HIS   CB   CG   sing N N 166 
HIS   CB   HB2  sing N N 167 
HIS   CB   HB3  sing N N 168 
HIS   CG   ND1  sing Y N 169 
HIS   CG   CD2  doub Y N 170 
HIS   ND1  CE1  doub Y N 171 
HIS   ND1  HD1  sing N N 172 
HIS   CD2  NE2  sing Y N 173 
HIS   CD2  HD2  sing N N 174 
HIS   CE1  NE2  sing Y N 175 
HIS   CE1  HE1  sing N N 176 
HIS   NE2  HE2  sing N N 177 
HIS   OXT  HXT  sing N N 178 
HOH   O    H1   sing N N 179 
HOH   O    H2   sing N N 180 
ILE   N    CA   sing N N 181 
ILE   N    H    sing N N 182 
ILE   N    H2   sing N N 183 
ILE   CA   C    sing N N 184 
ILE   CA   CB   sing N N 185 
ILE   CA   HA   sing N N 186 
ILE   C    O    doub N N 187 
ILE   C    OXT  sing N N 188 
ILE   CB   CG1  sing N N 189 
ILE   CB   CG2  sing N N 190 
ILE   CB   HB   sing N N 191 
ILE   CG1  CD1  sing N N 192 
ILE   CG1  HG12 sing N N 193 
ILE   CG1  HG13 sing N N 194 
ILE   CG2  HG21 sing N N 195 
ILE   CG2  HG22 sing N N 196 
ILE   CG2  HG23 sing N N 197 
ILE   CD1  HD11 sing N N 198 
ILE   CD1  HD12 sing N N 199 
ILE   CD1  HD13 sing N N 200 
ILE   OXT  HXT  sing N N 201 
LEU   N    CA   sing N N 202 
LEU   N    H    sing N N 203 
LEU   N    H2   sing N N 204 
LEU   CA   C    sing N N 205 
LEU   CA   CB   sing N N 206 
LEU   CA   HA   sing N N 207 
LEU   C    O    doub N N 208 
LEU   C    OXT  sing N N 209 
LEU   CB   CG   sing N N 210 
LEU   CB   HB2  sing N N 211 
LEU   CB   HB3  sing N N 212 
LEU   CG   CD1  sing N N 213 
LEU   CG   CD2  sing N N 214 
LEU   CG   HG   sing N N 215 
LEU   CD1  HD11 sing N N 216 
LEU   CD1  HD12 sing N N 217 
LEU   CD1  HD13 sing N N 218 
LEU   CD2  HD21 sing N N 219 
LEU   CD2  HD22 sing N N 220 
LEU   CD2  HD23 sing N N 221 
LEU   OXT  HXT  sing N N 222 
LYS   N    CA   sing N N 223 
LYS   N    H    sing N N 224 
LYS   N    H2   sing N N 225 
LYS   CA   C    sing N N 226 
LYS   CA   CB   sing N N 227 
LYS   CA   HA   sing N N 228 
LYS   C    O    doub N N 229 
LYS   C    OXT  sing N N 230 
LYS   CB   CG   sing N N 231 
LYS   CB   HB2  sing N N 232 
LYS   CB   HB3  sing N N 233 
LYS   CG   CD   sing N N 234 
LYS   CG   HG2  sing N N 235 
LYS   CG   HG3  sing N N 236 
LYS   CD   CE   sing N N 237 
LYS   CD   HD2  sing N N 238 
LYS   CD   HD3  sing N N 239 
LYS   CE   NZ   sing N N 240 
LYS   CE   HE2  sing N N 241 
LYS   CE   HE3  sing N N 242 
LYS   NZ   HZ1  sing N N 243 
LYS   NZ   HZ2  sing N N 244 
LYS   NZ   HZ3  sing N N 245 
LYS   OXT  HXT  sing N N 246 
MET   N    CA   sing N N 247 
MET   N    H    sing N N 248 
MET   N    H2   sing N N 249 
MET   CA   C    sing N N 250 
MET   CA   CB   sing N N 251 
MET   CA   HA   sing N N 252 
MET   C    O    doub N N 253 
MET   C    OXT  sing N N 254 
MET   CB   CG   sing N N 255 
MET   CB   HB2  sing N N 256 
MET   CB   HB3  sing N N 257 
MET   CG   SD   sing N N 258 
MET   CG   HG2  sing N N 259 
MET   CG   HG3  sing N N 260 
MET   SD   CE   sing N N 261 
MET   CE   HE1  sing N N 262 
MET   CE   HE2  sing N N 263 
MET   CE   HE3  sing N N 264 
MET   OXT  HXT  sing N N 265 
NDP   PA   O1A  doub N N 266 
NDP   PA   O2A  sing N N 267 
NDP   PA   O5B  sing N N 268 
NDP   PA   O3   sing N N 269 
NDP   O2A  HOA2 sing N N 270 
NDP   O5B  C5B  sing N N 271 
NDP   C5B  C4B  sing N N 272 
NDP   C5B  H51A sing N N 273 
NDP   C5B  H52A sing N N 274 
NDP   C4B  O4B  sing N N 275 
NDP   C4B  C3B  sing N N 276 
NDP   C4B  H4B  sing N N 277 
NDP   O4B  C1B  sing N N 278 
NDP   C3B  O3B  sing N N 279 
NDP   C3B  C2B  sing N N 280 
NDP   C3B  H3B  sing N N 281 
NDP   O3B  HO3A sing N N 282 
NDP   C2B  O2B  sing N N 283 
NDP   C2B  C1B  sing N N 284 
NDP   C2B  H2B  sing N N 285 
NDP   O2B  P2B  sing N N 286 
NDP   C1B  N9A  sing N N 287 
NDP   C1B  H1B  sing N N 288 
NDP   N9A  C8A  sing Y N 289 
NDP   N9A  C4A  sing Y N 290 
NDP   C8A  N7A  doub Y N 291 
NDP   C8A  H8A  sing N N 292 
NDP   N7A  C5A  sing Y N 293 
NDP   C5A  C6A  sing Y N 294 
NDP   C5A  C4A  doub Y N 295 
NDP   C6A  N6A  sing N N 296 
NDP   C6A  N1A  doub Y N 297 
NDP   N6A  H61A sing N N 298 
NDP   N6A  H62A sing N N 299 
NDP   N1A  C2A  sing Y N 300 
NDP   C2A  N3A  doub Y N 301 
NDP   C2A  H2A  sing N N 302 
NDP   N3A  C4A  sing Y N 303 
NDP   O3   PN   sing N N 304 
NDP   PN   O1N  doub N N 305 
NDP   PN   O2N  sing N N 306 
NDP   PN   O5D  sing N N 307 
NDP   O2N  H21N sing N N 308 
NDP   O5D  C5D  sing N N 309 
NDP   C5D  C4D  sing N N 310 
NDP   C5D  H51N sing N N 311 
NDP   C5D  H52N sing N N 312 
NDP   C4D  O4D  sing N N 313 
NDP   C4D  C3D  sing N N 314 
NDP   C4D  H4D  sing N N 315 
NDP   O4D  C1D  sing N N 316 
NDP   C3D  O3D  sing N N 317 
NDP   C3D  C2D  sing N N 318 
NDP   C3D  H3D  sing N N 319 
NDP   O3D  HO3N sing N N 320 
NDP   C2D  O2D  sing N N 321 
NDP   C2D  C1D  sing N N 322 
NDP   C2D  H2D  sing N N 323 
NDP   O2D  HO2N sing N N 324 
NDP   C1D  N1N  sing N N 325 
NDP   C1D  H1D  sing N N 326 
NDP   N1N  C2N  sing N N 327 
NDP   N1N  C6N  sing N N 328 
NDP   C2N  C3N  doub N N 329 
NDP   C2N  H2N  sing N N 330 
NDP   C3N  C7N  sing N N 331 
NDP   C3N  C4N  sing N N 332 
NDP   C7N  O7N  doub N N 333 
NDP   C7N  N7N  sing N N 334 
NDP   N7N  H71N sing N N 335 
NDP   N7N  H72N sing N N 336 
NDP   C4N  C5N  sing N N 337 
NDP   C4N  H41N sing N N 338 
NDP   C4N  H42N sing N N 339 
NDP   C5N  C6N  doub N N 340 
NDP   C5N  H5N  sing N N 341 
NDP   C6N  H6N  sing N N 342 
NDP   P2B  O1X  doub N N 343 
NDP   P2B  O2X  sing N N 344 
NDP   P2B  O3X  sing N N 345 
NDP   O2X  HOP2 sing N N 346 
NDP   O3X  HOP3 sing N N 347 
PHE   N    CA   sing N N 348 
PHE   N    H    sing N N 349 
PHE   N    H2   sing N N 350 
PHE   CA   C    sing N N 351 
PHE   CA   CB   sing N N 352 
PHE   CA   HA   sing N N 353 
PHE   C    O    doub N N 354 
PHE   C    OXT  sing N N 355 
PHE   CB   CG   sing N N 356 
PHE   CB   HB2  sing N N 357 
PHE   CB   HB3  sing N N 358 
PHE   CG   CD1  doub Y N 359 
PHE   CG   CD2  sing Y N 360 
PHE   CD1  CE1  sing Y N 361 
PHE   CD1  HD1  sing N N 362 
PHE   CD2  CE2  doub Y N 363 
PHE   CD2  HD2  sing N N 364 
PHE   CE1  CZ   doub Y N 365 
PHE   CE1  HE1  sing N N 366 
PHE   CE2  CZ   sing Y N 367 
PHE   CE2  HE2  sing N N 368 
PHE   CZ   HZ   sing N N 369 
PHE   OXT  HXT  sing N N 370 
PRO   N    CA   sing N N 371 
PRO   N    CD   sing N N 372 
PRO   N    H    sing N N 373 
PRO   CA   C    sing N N 374 
PRO   CA   CB   sing N N 375 
PRO   CA   HA   sing N N 376 
PRO   C    O    doub N N 377 
PRO   C    OXT  sing N N 378 
PRO   CB   CG   sing N N 379 
PRO   CB   HB2  sing N N 380 
PRO   CB   HB3  sing N N 381 
PRO   CG   CD   sing N N 382 
PRO   CG   HG2  sing N N 383 
PRO   CG   HG3  sing N N 384 
PRO   CD   HD2  sing N N 385 
PRO   CD   HD3  sing N N 386 
PRO   OXT  HXT  sing N N 387 
SER   N    CA   sing N N 388 
SER   N    H    sing N N 389 
SER   N    H2   sing N N 390 
SER   CA   C    sing N N 391 
SER   CA   CB   sing N N 392 
SER   CA   HA   sing N N 393 
SER   C    O    doub N N 394 
SER   C    OXT  sing N N 395 
SER   CB   OG   sing N N 396 
SER   CB   HB2  sing N N 397 
SER   CB   HB3  sing N N 398 
SER   OG   HG   sing N N 399 
SER   OXT  HXT  sing N N 400 
THR   N    CA   sing N N 401 
THR   N    H    sing N N 402 
THR   N    H2   sing N N 403 
THR   CA   C    sing N N 404 
THR   CA   CB   sing N N 405 
THR   CA   HA   sing N N 406 
THR   C    O    doub N N 407 
THR   C    OXT  sing N N 408 
THR   CB   OG1  sing N N 409 
THR   CB   CG2  sing N N 410 
THR   CB   HB   sing N N 411 
THR   OG1  HG1  sing N N 412 
THR   CG2  HG21 sing N N 413 
THR   CG2  HG22 sing N N 414 
THR   CG2  HG23 sing N N 415 
THR   OXT  HXT  sing N N 416 
TRP   N    CA   sing N N 417 
TRP   N    H    sing N N 418 
TRP   N    H2   sing N N 419 
TRP   CA   C    sing N N 420 
TRP   CA   CB   sing N N 421 
TRP   CA   HA   sing N N 422 
TRP   C    O    doub N N 423 
TRP   C    OXT  sing N N 424 
TRP   CB   CG   sing N N 425 
TRP   CB   HB2  sing N N 426 
TRP   CB   HB3  sing N N 427 
TRP   CG   CD1  doub Y N 428 
TRP   CG   CD2  sing Y N 429 
TRP   CD1  NE1  sing Y N 430 
TRP   CD1  HD1  sing N N 431 
TRP   CD2  CE2  doub Y N 432 
TRP   CD2  CE3  sing Y N 433 
TRP   NE1  CE2  sing Y N 434 
TRP   NE1  HE1  sing N N 435 
TRP   CE2  CZ2  sing Y N 436 
TRP   CE3  CZ3  doub Y N 437 
TRP   CE3  HE3  sing N N 438 
TRP   CZ2  CH2  doub Y N 439 
TRP   CZ2  HZ2  sing N N 440 
TRP   CZ3  CH2  sing Y N 441 
TRP   CZ3  HZ3  sing N N 442 
TRP   CH2  HH2  sing N N 443 
TRP   OXT  HXT  sing N N 444 
TYR   N    CA   sing N N 445 
TYR   N    H    sing N N 446 
TYR   N    H2   sing N N 447 
TYR   CA   C    sing N N 448 
TYR   CA   CB   sing N N 449 
TYR   CA   HA   sing N N 450 
TYR   C    O    doub N N 451 
TYR   C    OXT  sing N N 452 
TYR   CB   CG   sing N N 453 
TYR   CB   HB2  sing N N 454 
TYR   CB   HB3  sing N N 455 
TYR   CG   CD1  doub Y N 456 
TYR   CG   CD2  sing Y N 457 
TYR   CD1  CE1  sing Y N 458 
TYR   CD1  HD1  sing N N 459 
TYR   CD2  CE2  doub Y N 460 
TYR   CD2  HD2  sing N N 461 
TYR   CE1  CZ   doub Y N 462 
TYR   CE1  HE1  sing N N 463 
TYR   CE2  CZ   sing Y N 464 
TYR   CE2  HE2  sing N N 465 
TYR   CZ   OH   sing N N 466 
TYR   OH   HH   sing N N 467 
TYR   OXT  HXT  sing N N 468 
VAL   N    CA   sing N N 469 
VAL   N    H    sing N N 470 
VAL   N    H2   sing N N 471 
VAL   CA   C    sing N N 472 
VAL   CA   CB   sing N N 473 
VAL   CA   HA   sing N N 474 
VAL   C    O    doub N N 475 
VAL   C    OXT  sing N N 476 
VAL   CB   CG1  sing N N 477 
VAL   CB   CG2  sing N N 478 
VAL   CB   HB   sing N N 479 
VAL   CG1  HG11 sing N N 480 
VAL   CG1  HG12 sing N N 481 
VAL   CG1  HG13 sing N N 482 
VAL   CG2  HG21 sing N N 483 
VAL   CG2  HG22 sing N N 484 
VAL   CG2  HG23 sing N N 485 
VAL   OXT  HXT  sing N N 486 
# 
_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                    8RHX 
_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]   0.013496 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006568 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011182 
_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]   0.013228 
_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  
CL 
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  ? -18.709 9.536   -11.621 0.70 40.78 ? 2   GLU   A N    1 
ATOM   2    C  CA   . GLU   A 1 23  ? -17.904 8.508   -10.906 0.70 38.73 ? 2   GLU   A CA   1 
ATOM   3    C  C    . GLU   A 1 23  ? -18.756 7.828   -9.836  0.70 34.53 ? 2   GLU   A C    1 
ATOM   4    O  O    . GLU   A 1 23  ? -19.801 8.339   -9.442  0.70 36.88 ? 2   GLU   A O    1 
ATOM   5    C  CB   . GLU   A 1 23  ? -16.643 9.078   -10.260 0.70 39.73 ? 2   GLU   A CB   1 
ATOM   6    C  CG   . GLU   A 1 23  ? -16.935 10.176  -9.245  0.70 41.09 ? 2   GLU   A CG   1 
ATOM   7    C  CD   . GLU   A 1 23  ? -16.100 10.049  -7.985  0.70 41.82 ? 2   GLU   A CD   1 
ATOM   8    O  OE1  . GLU   A 1 23  ? -15.377 9.039   -7.858  0.70 46.17 ? 2   GLU   A OE1  1 
ATOM   9    O  OE2  . GLU   A 1 23  ? -16.180 10.948  -7.126  0.70 39.76 ? 2   GLU   A OE2  1 
ATOM   10   N  N    . ALA   A 1 24  ? -18.259 6.687   -9.353  1.00 32.44 ? 3   ALA   A N    1 
ATOM   11   C  CA   . ALA   A 1 24  ? -19.068 5.739   -8.605  1.00 27.37 ? 3   ALA   A CA   1 
ATOM   12   C  C    . ALA   A 1 24  ? -19.135 6.131   -7.129  1.00 25.75 ? 3   ALA   A C    1 
ATOM   13   O  O    . ALA   A 1 24  ? -18.133 6.495   -6.525  1.00 25.28 ? 3   ALA   A O    1 
ATOM   14   C  CB   . ALA   A 1 24  ? -18.516 4.345   -8.795  1.00 27.78 ? 3   ALA   A CB   1 
ATOM   15   N  N    . PRO   A 1 25  ? -20.325 6.056   -6.490  1.00 22.82 ? 4   PRO   A N    1 
ATOM   16   C  CA   . PRO   A 1 25  ? -20.410 6.262   -5.045  1.00 21.90 ? 4   PRO   A CA   1 
ATOM   17   C  C    . PRO   A 1 25  ? -19.708 5.112   -4.327  1.00 20.41 ? 4   PRO   A C    1 
ATOM   18   O  O    . PRO   A 1 25  ? -19.431 4.074   -4.926  1.00 21.71 ? 4   PRO   A O    1 
ATOM   19   C  CB   . PRO   A 1 25  ? -21.931 6.251   -4.826  1.00 21.46 ? 4   PRO   A CB   1 
ATOM   20   C  CG   . PRO   A 1 25  ? -22.427 5.286   -5.868  1.00 22.74 ? 4   PRO   A CG   1 
ATOM   21   C  CD   . PRO   A 1 25  ? -21.610 5.691   -7.106  1.00 23.38 ? 4   PRO   A CD   1 
ATOM   22   N  N    . ALA   A 1 26  ? -19.417 5.314   -3.033  1.00 18.61 ? 5   ALA   A N    1 
ATOM   23   C  CA   . ALA   A 1 26  ? -18.712 4.328   -2.225  1.00 17.88 ? 5   ALA   A CA   1 
ATOM   24   C  C    . ALA   A 1 26  ? -19.520 3.997   -0.966  1.00 17.03 ? 5   ALA   A C    1 
ATOM   25   O  O    . ALA   A 1 26  ? -20.235 4.851   -0.454  1.00 18.25 ? 5   ALA   A O    1 
ATOM   26   C  CB   . ALA   A 1 26  ? -17.315 4.845   -1.897  1.00 18.02 ? 5   ALA   A CB   1 
ATOM   27   N  N    . ALA   A 1 27  ? -19.417 2.736   -0.515  1.00 16.18 ? 6   ALA   A N    1 
ATOM   28   C  CA   . ALA   A 1 27  ? -20.119 2.288   0.686   1.00 16.48 ? 6   ALA   A CA   1 
ATOM   29   C  C    . ALA   A 1 27  ? -19.172 1.575   1.637   1.00 17.92 ? 6   ALA   A C    1 
ATOM   30   O  O    . ALA   A 1 27  ? -18.270 0.881   1.195   1.00 18.19 ? 6   ALA   A O    1 
ATOM   31   C  CB   . ALA   A 1 27  ? -21.227 1.327   0.327   1.00 16.81 ? 6   ALA   A CB   1 
ATOM   32   N  N    . VAL   A 1 28  ? -19.426 1.730   2.943   1.00 15.02 ? 7   VAL   A N    1 
ATOM   33   C  CA   . VAL   A 1 28  ? -18.793 0.930   3.979   1.00 15.56 ? 7   VAL   A CA   1 
ATOM   34   C  C    . VAL   A 1 28  ? -19.829 -0.081  4.442   1.00 14.72 ? 7   VAL   A C    1 
ATOM   35   O  O    . VAL   A 1 28  ? -20.947 0.318   4.775   1.00 14.69 ? 7   VAL   A O    1 
ATOM   36   C  CB   . VAL   A 1 28  ? -18.348 1.787   5.179   1.00 15.72 ? 7   VAL   A CB   1 
ATOM   37   C  CG1  . VAL   A 1 28  ? -17.971 0.917   6.380   1.00 16.46 ? 7   VAL   A CG1  1 
ATOM   38   C  CG2  . VAL   A 1 28  ? -17.179 2.706   4.796   1.00 16.45 ? 7   VAL   A CG2  1 
ATOM   39   N  N    . VAL   A 1 29  ? -19.460 -1.364  4.432   1.00 14.09 ? 8   VAL   A N    1 
ATOM   40   C  CA   . VAL   A 1 29  ? -20.299 -2.387  5.042   1.00 14.71 ? 8   VAL   A CA   1 
ATOM   41   C  C    . VAL   A 1 29  ? -19.509 -3.015  6.186   1.00 15.70 ? 8   VAL   A C    1 
ATOM   42   O  O    . VAL   A 1 29  ? -18.434 -3.551  5.952   1.00 15.08 ? 8   VAL   A O    1 
ATOM   43   C  CB   . VAL   A 1 29  ? -20.740 -3.459  4.026   1.00 13.92 ? 8   VAL   A CB   1 
ATOM   44   C  CG1  . VAL   A 1 29  ? -21.678 -4.490  4.661   1.00 14.50 ? 8   VAL   A CG1  1 
ATOM   45   C  CG2  . VAL   A 1 29  ? -21.425 -2.826  2.817   1.00 15.22 ? 8   VAL   A CG2  1 
ATOM   46   N  N    . THR   A 1 30  ? -20.040 -2.977  7.417   1.00 14.99 ? 9   THR   A N    1 
ATOM   47   C  CA   . THR   A 1 30  ? -19.299 -3.604  8.507   1.00 14.35 ? 9   THR   A CA   1 
ATOM   48   C  C    . THR   A 1 30  ? -19.622 -5.093  8.553   1.00 14.87 ? 9   THR   A C    1 
ATOM   49   O  O    . THR   A 1 30  ? -20.725 -5.513  8.220   1.00 15.09 ? 9   THR   A O    1 
ATOM   50   C  CB   . THR   A 1 30  ? -19.520 -2.925  9.855   1.00 14.09 ? 9   THR   A CB   1 
ATOM   51   O  OG1  . THR   A 1 30  ? -20.900 -3.001  10.216  1.00 13.95 ? 9   THR   A OG1  1 
ATOM   52   C  CG2  . THR   A 1 30  ? -19.156 -1.454  9.786   1.00 13.88 ? 9   THR   A CG2  1 
ATOM   53   N  N    . GLY   A 1 31  ? -18.641 -5.879  9.009   1.00 15.23 ? 10  GLY   A N    1 
ATOM   54   C  CA   . GLY   A 1 31  ? -18.789 -7.323  9.082   1.00 15.60 ? 10  GLY   A CA   1 
ATOM   55   C  C    . GLY   A 1 31  ? -19.218 -7.917  7.745   1.00 16.20 ? 10  GLY   A C    1 
ATOM   56   O  O    . GLY   A 1 31  ? -20.133 -8.734  7.705   1.00 16.12 ? 10  GLY   A O    1 
ATOM   57   N  N    . ALA   A 1 32  ? -18.492 -7.546  6.674   1.00 14.75 ? 11  ALA   A N    1 
ATOM   58   C  CA   . ALA   A 1 32  ? -18.916 -7.814  5.306   1.00 15.52 ? 11  ALA   A CA   1 
ATOM   59   C  C    . ALA   A 1 32  ? -18.225 -9.035  4.688   1.00 15.51 ? 11  ALA   A C    1 
ATOM   60   O  O    . ALA   A 1 32  ? -18.473 -9.319  3.518   1.00 17.09 ? 11  ALA   A O    1 
ATOM   61   C  CB   . ALA   A 1 32  ? -18.659 -6.584  4.466   1.00 15.95 ? 11  ALA   A CB   1 
ATOM   62   N  N    . ALA   A 1 33  ? -17.432 -9.774  5.467   1.00 17.03 ? 12  ALA   A N    1 
ATOM   63   C  CA   . ALA   A 1 33  ? -16.695 -10.878 4.853   1.00 18.21 ? 12  ALA   A CA   1 
ATOM   64   C  C    . ALA   A 1 33  ? -17.618 -12.040 4.481   1.00 19.30 ? 12  ALA   A C    1 
ATOM   65   O  O    . ALA   A 1 33  ? -17.326 -12.773 3.537   1.00 19.77 ? 12  ALA   A O    1 
ATOM   66   C  CB   . ALA   A 1 33  ? -15.583 -11.344 5.765   1.00 19.29 ? 12  ALA   A CB   1 
ATOM   67   N  N    . LYS   A 1 34  ? -18.711 -12.234 5.237   1.00 17.48 ? 13  LYS   A N    1 
ATOM   68   C  CA   . LYS   A 1 34  ? -19.503 -13.444 5.081   1.00 17.81 ? 13  LYS   A CA   1 
ATOM   69   C  C    . LYS   A 1 34  ? -20.994 -13.127 5.228   1.00 18.30 ? 13  LYS   A C    1 
ATOM   70   O  O    . LYS   A 1 34  ? -21.380 -12.031 5.630   1.00 17.98 ? 13  LYS   A O    1 
ATOM   71   C  CB   . LYS   A 1 34  ? -19.121 -14.440 6.185   1.00 20.75 ? 13  LYS   A CB   1 
ATOM   72   C  CG   . LYS   A 1 34  ? -17.670 -14.895 6.209   1.00 25.72 ? 13  LYS   A CG   1 
ATOM   73   C  CD   . LYS   A 1 34  ? -17.476 -15.813 7.410   1.00 28.01 ? 13  LYS   A CD   1 
ATOM   74   C  CE   . LYS   A 1 34  ? -16.085 -16.341 7.513   1.00 31.33 ? 13  LYS   A CE   1 
ATOM   75   N  NZ   . LYS   A 1 34  ? -15.903 -16.915 8.851   1.00 35.03 ? 13  LYS   A NZ   1 
ATOM   76   N  N    . ARG   A 1 35  ? -21.832 -14.105 4.881   1.00 16.57 ? 14  ARG   A N    1 
ATOM   77   C  CA   . ARG   A 1 35  ? -23.223 -14.105 5.307   1.00 16.47 ? 14  ARG   A CA   1 
ATOM   78   C  C    . ARG   A 1 35  ? -23.928 -12.839 4.815   1.00 16.50 ? 14  ARG   A C    1 
ATOM   79   O  O    . ARG   A 1 35  ? -23.799 -12.458 3.661   1.00 16.44 ? 14  ARG   A O    1 
ATOM   80   C  CB   . ARG   A 1 35  ? -23.230 -14.410 6.807   1.00 16.13 ? 14  ARG   A CB   1 
ATOM   81   C  CG   . ARG   A 1 35  ? -22.826 -15.848 7.117   1.00 16.63 ? 14  ARG   A CG   1 
ATOM   82   C  CD   . ARG   A 1 35  ? -22.524 -16.060 8.601   1.00 17.17 ? 14  ARG   A CD   1 
ATOM   83   N  NE   . ARG   A 1 35  ? -23.706 -15.785 9.426   1.00 16.87 ? 14  ARG   A NE   1 
ATOM   84   C  CZ   . ARG   A 1 35  ? -24.694 -16.632 9.679   1.00 18.08 ? 14  ARG   A CZ   1 
ATOM   85   N  NH1  . ARG   A 1 35  ? -24.715 -17.830 9.117   1.00 19.66 ? 14  ARG   A NH1  1 
ATOM   86   N  NH2  . ARG   A 1 35  ? -25.679 -16.268 10.492  1.00 18.24 ? 14  ARG   A NH2  1 
ATOM   87   N  N    . ILE   A 1 36  ? -24.722 -12.208 5.687   1.00 15.67 ? 15  ILE   A N    1 
ATOM   88   C  CA   . ILE   A 1 36  ? -25.581 -11.120 5.217   1.00 15.61 ? 15  ILE   A CA   1 
ATOM   89   C  C    . ILE   A 1 36  ? -24.728 -9.915  4.806   1.00 16.17 ? 15  ILE   A C    1 
ATOM   90   O  O    . ILE   A 1 36  ? -25.055 -9.240  3.831   1.00 15.38 ? 15  ILE   A O    1 
ATOM   91   C  CB   . ILE   A 1 36  ? -26.639 -10.766 6.284   1.00 16.09 ? 15  ILE   A CB   1 
ATOM   92   C  CG1  . ILE   A 1 36  ? -27.706 -11.870 6.380   1.00 18.91 ? 15  ILE   A CG1  1 
ATOM   93   C  CG2  . ILE   A 1 36  ? -27.289 -9.404  6.034   1.00 15.72 ? 15  ILE   A CG2  1 
ATOM   94   C  CD1  . ILE   A 1 36  ? -28.594 -11.743 7.605   1.00 18.72 ? 15  ILE   A CD1  1 
ATOM   95   N  N    . GLY   A 1 37  ? -23.644 -9.637  5.540   1.00 15.22 ? 16  GLY   A N    1 
ATOM   96   C  CA   . GLY   A 1 37  ? -22.814 -8.498  5.158   1.00 15.02 ? 16  GLY   A CA   1 
ATOM   97   C  C    . GLY   A 1 37  ? -22.165 -8.666  3.783   1.00 14.86 ? 16  GLY   A C    1 
ATOM   98   O  O    . GLY   A 1 37  ? -22.104 -7.712  3.015   1.00 15.82 ? 16  GLY   A O    1 
ATOM   99   N  N    . ARG   A 1 38  ? -21.726 -9.885  3.469   1.00 15.45 ? 17  ARG   A N    1 
ATOM   100  C  CA   . ARG   A 1 38  ? -21.193 -10.129 2.137   1.00 15.42 ? 17  ARG   A CA   1 
ATOM   101  C  C    . ARG   A 1 38  ? -22.290 -9.913  1.102   1.00 15.02 ? 17  ARG   A C    1 
ATOM   102  O  O    . ARG   A 1 38  ? -22.037 -9.332  0.057   1.00 15.71 ? 17  ARG   A O    1 
ATOM   103  C  CB   . ARG   A 1 38  ? -20.617 -11.546 2.009   1.00 16.34 ? 17  ARG   A CB   1 
ATOM   104  C  CG   . ARG   A 1 38  ? -20.233 -11.895 0.573   1.00 16.77 ? 17  ARG   A CG   1 
ATOM   105  C  CD   . ARG   A 1 38  ? -19.431 -13.208 0.512   1.00 18.52 ? 17  ARG   A CD   1 
ATOM   106  N  NE   . ARG   A 1 38  ? -19.307 -13.556 -0.916  1.00 19.33 ? 17  ARG   A NE   1 
ATOM   107  C  CZ   . ARG   A 1 38  ? -18.216 -14.020 -1.541  1.00 19.42 ? 17  ARG   A CZ   1 
ATOM   108  N  NH1  . ARG   A 1 38  ? -17.097 -14.193 -0.869  1.00 21.67 ? 17  ARG   A NH1  1 
ATOM   109  N  NH2  . ARG   A 1 38  ? -18.255 -14.283 -2.844  1.00 20.30 ? 17  ARG   A NH2  1 
ATOM   110  N  N    . ALA   A 1 39  ? -23.514 -10.399 1.384   1.00 14.75 ? 18  ALA   A N    1 
ATOM   111  C  CA   . ALA   A 1 39  ? -24.572 -10.262 0.397   1.00 15.28 ? 18  ALA   A CA   1 
ATOM   112  C  C    . ALA   A 1 39  ? -24.862 -8.789  0.110   1.00 15.43 ? 18  ALA   A C    1 
ATOM   113  O  O    . ALA   A 1 39  ? -25.114 -8.404  -1.030  1.00 16.53 ? 18  ALA   A O    1 
ATOM   114  C  CB   . ALA   A 1 39  ? -25.810 -10.999 0.868   1.00 17.07 ? 18  ALA   A CB   1 
ATOM   115  N  N    . ILE   A 1 40  ? -24.855 -7.965  1.161   1.00 15.35 ? 19  ILE   A N    1 
ATOM   116  C  CA   . ILE   A 1 40  ? -25.066 -6.534  1.015   1.00 14.95 ? 19  ILE   A CA   1 
ATOM   117  C  C    . ILE   A 1 40  ? -23.923 -5.904  0.208   1.00 15.04 ? 19  ILE   A C    1 
ATOM   118  O  O    . ILE   A 1 40  ? -24.198 -5.099  -0.692  1.00 15.79 ? 19  ILE   A O    1 
ATOM   119  C  CB   . ILE   A 1 40  ? -25.200 -5.888  2.407   1.00 13.95 ? 19  ILE   A CB   1 
ATOM   120  C  CG1  . ILE   A 1 40  ? -26.492 -6.348  3.078   1.00 14.83 ? 19  ILE   A CG1  1 
ATOM   121  C  CG2  . ILE   A 1 40  ? -25.188 -4.359  2.293   1.00 15.40 ? 19  ILE   A CG2  1 
ATOM   122  C  CD1  . ILE   A 1 40  ? -26.547 -6.076  4.578   1.00 14.39 ? 19  ILE   A CD1  1 
ATOM   123  N  N    . ALA   A 1 41  ? -22.667 -6.250  0.548   1.00 16.23 ? 20  ALA   A N    1 
ATOM   124  C  CA   . ALA   A 1 41  ? -21.510 -5.738  -0.179  1.00 15.18 ? 20  ALA   A CA   1 
ATOM   125  C  C    . ALA   A 1 41  ? -21.611 -6.089  -1.666  1.00 16.56 ? 20  ALA   A C    1 
ATOM   126  O  O    . ALA   A 1 41  ? -21.359 -5.247  -2.526  1.00 17.07 ? 20  ALA   A O    1 
ATOM   127  C  CB   . ALA   A 1 41  ? -20.214 -6.242  0.446   1.00 17.24 ? 20  ALA   A CB   1 
ATOM   128  N  N    . VAL   A 1 42  ? -21.937 -7.348  -1.958  1.00 15.51 ? 21  VAL   A N    1 
ATOM   129  C  CA   . VAL   A 1 42  ? -22.015 -7.794  -3.343  1.00 18.11 ? 21  VAL   A CA   1 
ATOM   130  C  C    . VAL   A 1 42  ? -23.124 -7.047  -4.082  1.00 18.43 ? 21  VAL   A C    1 
ATOM   131  O  O    . VAL   A 1 42  ? -22.944 -6.611  -5.218  1.00 18.47 ? 21  VAL   A O    1 
ATOM   132  C  CB   . VAL   A 1 42  ? -22.266 -9.314  -3.355  1.00 18.35 ? 21  VAL   A CB   1 
ATOM   133  C  CG1  . VAL   A 1 42  ? -22.667 -9.824  -4.742  1.00 21.45 ? 21  VAL   A CG1  1 
ATOM   134  C  CG2  . VAL   A 1 42  ? -21.041 -10.068 -2.861  1.00 19.82 ? 21  VAL   A CG2  1 
ATOM   135  N  N    . LYS   A 1 43  ? -24.296 -6.899  -3.445  1.00 17.41 ? 22  LYS   A N    1 
ATOM   136  C  CA   . LYS   A 1 43  ? -25.402 -6.281  -4.143  1.00 18.17 ? 22  LYS   A CA   1 
ATOM   137  C  C    . LYS   A 1 43  ? -25.121 -4.791  -4.350  1.00 17.48 ? 22  LYS   A C    1 
ATOM   138  O  O    . LYS   A 1 43  ? -25.444 -4.263  -5.411  1.00 18.64 ? 22  LYS   A O    1 
ATOM   139  C  CB   . LYS   A 1 43  ? -26.732 -6.614  -3.450  1.00 20.02 ? 22  LYS   A CB   1 
ATOM   140  C  CG   . LYS   A 1 43  ? -27.957 -6.223  -4.288  1.00 26.70 ? 22  LYS   A CG   1 
ATOM   141  C  CD   . LYS   A 1 43  ? -29.271 -6.668  -3.646  1.00 26.94 ? 22  LYS   A CD   1 
ATOM   142  C  CE   . LYS   A 1 43  ? -29.513 -8.138  -3.768  0.60 27.53 ? 22  LYS   A CE   1 
ATOM   143  N  NZ   . LYS   A 1 43  ? -29.836 -8.533  -5.144  0.60 29.32 ? 22  LYS   A NZ   1 
ATOM   144  N  N    . LEU   A 1 44  ? -24.506 -4.119  -3.366  1.00 16.68 ? 23  LEU   A N    1 
ATOM   145  C  CA   . LEU   A 1 44  ? -24.086 -2.736  -3.585  1.00 18.00 ? 23  LEU   A CA   1 
ATOM   146  C  C    . LEU   A 1 44  ? -23.100 -2.660  -4.756  1.00 19.29 ? 23  LEU   A C    1 
ATOM   147  O  O    . LEU   A 1 44  ? -23.219 -1.777  -5.610  1.00 20.07 ? 23  LEU   A O    1 
ATOM   148  C  CB   . LEU   A 1 44  ? -23.473 -2.135  -2.318  1.00 16.24 ? 23  LEU   A CB   1 
ATOM   149  C  CG   . LEU   A 1 44  ? -24.476 -1.850  -1.191  1.00 16.33 ? 23  LEU   A CG   1 
ATOM   150  C  CD1  . LEU   A 1 44  ? -23.721 -1.595  0.093   1.00 16.32 ? 23  LEU   A CD1  1 
ATOM   151  C  CD2  . LEU   A 1 44  ? -25.338 -0.658  -1.569  1.00 18.16 ? 23  LEU   A CD2  1 
ATOM   152  N  N    . HIS   A 1 45  ? -22.126 -3.570  -4.779  1.00 19.12 ? 24  HIS   A N    1 
ATOM   153  C  CA   . HIS   A 1 45  ? -21.109 -3.521  -5.821  1.00 19.70 ? 24  HIS   A CA   1 
ATOM   154  C  C    . HIS   A 1 45  ? -21.749 -3.737  -7.193  1.00 21.57 ? 24  HIS   A C    1 
ATOM   155  O  O    . HIS   A 1 45  ? -21.400 -3.049  -8.150  1.00 22.65 ? 24  HIS   A O    1 
ATOM   156  C  CB   . HIS   A 1 45  ? -20.025 -4.551  -5.522  1.00 21.07 ? 24  HIS   A CB   1 
ATOM   157  C  CG   . HIS   A 1 45  ? -18.849 -4.468  -6.433  1.00 21.24 ? 24  HIS   A CG   1 
ATOM   158  N  ND1  . HIS   A 1 45  ? -18.744 -5.240  -7.571  1.00 23.56 ? 24  HIS   A ND1  1 
ATOM   159  C  CD2  . HIS   A 1 45  ? -17.747 -3.714  -6.370  1.00 23.84 ? 24  HIS   A CD2  1 
ATOM   160  C  CE1  . HIS   A 1 45  ? -17.598 -4.945  -8.173  1.00 22.46 ? 24  HIS   A CE1  1 
ATOM   161  N  NE2  . HIS   A 1 45  ? -16.981 -4.027  -7.460  1.00 22.32 ? 24  HIS   A NE2  1 
ATOM   162  N  N    . GLN   A 1 46  ? -22.696 -4.680  -7.280  1.00 19.41 ? 25  GLN   A N    1 
ATOM   163  C  CA   . GLN   A 1 46  ? -23.388 -4.972  -8.535  1.00 22.30 ? 25  GLN   A CA   1 
ATOM   164  C  C    . GLN   A 1 46  ? -24.231 -3.780  -8.998  1.00 23.54 ? 25  GLN   A C    1 
ATOM   165  O  O    . GLN   A 1 46  ? -24.507 -3.641  -10.188 1.00 26.20 ? 25  GLN   A O    1 
ATOM   166  C  CB   . GLN   A 1 46  ? -24.254 -6.222  -8.389  1.00 22.46 ? 25  GLN   A CB   1 
ATOM   167  C  CG   . GLN   A 1 46  ? -23.428 -7.489  -8.207  1.00 25.26 ? 25  GLN   A CG   1 
ATOM   168  C  CD   . GLN   A 1 46  ? -24.236 -8.742  -7.953  1.00 28.51 ? 25  GLN   A CD   1 
ATOM   169  O  OE1  . GLN   A 1 46  ? -23.778 -9.856  -8.233  1.00 33.41 ? 25  GLN   A OE1  1 
ATOM   170  N  NE2  . GLN   A 1 46  ? -25.439 -8.585  -7.423  1.00 29.93 ? 25  GLN   A NE2  1 
ATOM   171  N  N    . THR   A 1 47  ? -24.658 -2.931  -8.061  1.00 23.52 ? 26  THR   A N    1 
ATOM   172  C  CA   . THR   A 1 47  ? -25.460 -1.754  -8.360  1.00 22.83 ? 26  THR   A CA   1 
ATOM   173  C  C    . THR   A 1 47  ? -24.548 -0.614  -8.810  1.00 24.07 ? 26  THR   A C    1 
ATOM   174  O  O    . THR   A 1 47  ? -25.038 0.411   -9.279  1.00 27.70 ? 26  THR   A O    1 
ATOM   175  C  CB   . THR   A 1 47  ? -26.271 -1.377  -7.109  1.00 26.71 ? 26  THR   A CB   1 
ATOM   176  O  OG1  . THR   A 1 47  ? -27.108 -2.480  -6.770  1.00 28.49 ? 26  THR   A OG1  1 
ATOM   177  C  CG2  . THR   A 1 47  ? -27.113 -0.123  -7.263  1.00 27.76 ? 26  THR   A CG2  1 
ATOM   178  N  N    . GLY   A 1 48  ? -23.229 -0.770  -8.628  1.00 23.06 ? 27  GLY   A N    1 
ATOM   179  C  CA   . GLY   A 1 48  ? -22.283 0.230   -9.105  1.00 23.64 ? 27  GLY   A CA   1 
ATOM   180  C  C    . GLY   A 1 48  ? -21.478 0.922   -8.005  1.00 23.86 ? 27  GLY   A C    1 
ATOM   181  O  O    . GLY   A 1 48  ? -20.729 1.860   -8.288  1.00 24.91 ? 27  GLY   A O    1 
ATOM   182  N  N    . TYR   A 1 49  ? -21.623 0.470   -6.753  1.00 20.72 ? 28  TYR   A N    1 
ATOM   183  C  CA   . TYR   A 1 49  ? -20.845 1.052   -5.664  1.00 18.54 ? 28  TYR   A CA   1 
ATOM   184  C  C    . TYR   A 1 49  ? -19.442 0.454   -5.585  1.00 18.15 ? 28  TYR   A C    1 
ATOM   185  O  O    . TYR   A 1 49  ? -19.247 -0.744  -5.807  1.00 20.16 ? 28  TYR   A O    1 
ATOM   186  C  CB   . TYR   A 1 49  ? -21.502 0.772   -4.307  1.00 18.98 ? 28  TYR   A CB   1 
ATOM   187  C  CG   . TYR   A 1 49  ? -22.699 1.666   -4.034  1.00 18.86 ? 28  TYR   A CG   1 
ATOM   188  C  CD1  . TYR   A 1 49  ? -23.943 1.364   -4.578  1.00 20.19 ? 28  TYR   A CD1  1 
ATOM   189  C  CD2  . TYR   A 1 49  ? -22.580 2.823   -3.273  1.00 19.65 ? 28  TYR   A CD2  1 
ATOM   190  C  CE1  . TYR   A 1 49  ? -25.043 2.170   -4.343  1.00 18.69 ? 28  TYR   A CE1  1 
ATOM   191  C  CE2  . TYR   A 1 49  ? -23.671 3.647   -3.039  1.00 21.20 ? 28  TYR   A CE2  1 
ATOM   192  C  CZ   . TYR   A 1 49  ? -24.896 3.330   -3.601  1.00 20.09 ? 28  TYR   A CZ   1 
ATOM   193  O  OH   . TYR   A 1 49  ? -25.983 4.129   -3.385  1.00 23.63 ? 28  TYR   A OH   1 
ATOM   194  N  N    . ARG   A 1 50  ? -18.493 1.298   -5.171  1.00 19.03 ? 29  ARG   A N    1 
ATOM   195  C  CA   . ARG   A 1 50  ? -17.201 0.882   -4.648  1.00 18.06 ? 29  ARG   A CA   1 
ATOM   196  C  C    . ARG   A 1 50  ? -17.411 0.562   -3.170  1.00 19.20 ? 29  ARG   A C    1 
ATOM   197  O  O    . ARG   A 1 50  ? -18.252 1.198   -2.529  1.00 21.01 ? 29  ARG   A O    1 
ATOM   198  C  CB   . ARG   A 1 50  ? -16.189 2.013   -4.860  1.00 19.91 ? 29  ARG   A CB   1 
ATOM   199  C  CG   . ARG   A 1 50  ? -15.915 2.145   -6.356  1.00 21.42 ? 29  ARG   A CG   1 
ATOM   200  C  CD   . ARG   A 1 50  ? -14.948 3.278   -6.639  1.00 23.83 ? 29  ARG   A CD   1 
ATOM   201  N  NE   . ARG   A 1 50  ? -15.495 4.618   -6.415  1.00 24.18 ? 29  ARG   A NE   1 
ATOM   202  C  CZ   . ARG   A 1 50  ? -14.738 5.701   -6.412  1.00 27.70 ? 29  ARG   A CZ   1 
ATOM   203  N  NH1  . ARG   A 1 50  ? -13.438 5.589   -6.653  1.00 29.84 ? 29  ARG   A NH1  1 
ATOM   204  N  NH2  . ARG   A 1 50  ? -15.270 6.890   -6.161  1.00 26.76 ? 29  ARG   A NH2  1 
ATOM   205  N  N    . VAL   A 1 51  ? -16.720 -0.460  -2.662  1.00 17.95 ? 30  VAL   A N    1 
ATOM   206  C  CA   . VAL   A 1 51  ? -17.054 -0.935  -1.324  1.00 18.19 ? 30  VAL   A CA   1 
ATOM   207  C  C    . VAL   A 1 51  ? -15.820 -1.090  -0.439  1.00 18.82 ? 30  VAL   A C    1 
ATOM   208  O  O    . VAL   A 1 51  ? -14.770 -1.569  -0.879  1.00 19.29 ? 30  VAL   A O    1 
ATOM   209  C  CB   . VAL   A 1 51  ? -17.870 -2.240  -1.368  1.00 18.59 ? 30  VAL   A CB   1 
ATOM   210  C  CG1  . VAL   A 1 51  ? -19.196 -2.047  -2.091  1.00 20.02 ? 30  VAL   A CG1  1 
ATOM   211  C  CG2  . VAL   A 1 51  ? -17.096 -3.419  -1.960  1.00 20.50 ? 30  VAL   A CG2  1 
ATOM   212  N  N    . VAL   A 1 52  ? -15.972 -0.715  0.837   1.00 16.79 ? 31  VAL   A N    1 
ATOM   213  C  CA   . VAL   A 1 52  ? -15.070 -1.101  1.912   1.00 16.57 ? 31  VAL   A CA   1 
ATOM   214  C  C    . VAL   A 1 52  ? -15.672 -2.312  2.615   1.00 16.75 ? 31  VAL   A C    1 
ATOM   215  O  O    . VAL   A 1 52  ? -16.768 -2.214  3.173   1.00 17.57 ? 31  VAL   A O    1 
ATOM   216  C  CB   . VAL   A 1 52  ? -14.861 0.027   2.935   1.00 16.71 ? 31  VAL   A CB   1 
ATOM   217  C  CG1  . VAL   A 1 52  ? -13.987 -0.423  4.106   1.00 18.07 ? 31  VAL   A CG1  1 
ATOM   218  C  CG2  . VAL   A 1 52  ? -14.283 1.277   2.286   1.00 17.59 ? 31  VAL   A CG2  1 
ATOM   219  N  N    . ILE   A 1 53  ? -14.953 -3.439  2.596   1.00 17.05 ? 32  ILE   A N    1 
ATOM   220  C  CA   . ILE   A 1 53  ? -15.353 -4.643  3.306   1.00 17.02 ? 32  ILE   A CA   1 
ATOM   221  C  C    . ILE   A 1 53  ? -14.653 -4.626  4.660   1.00 17.11 ? 32  ILE   A C    1 
ATOM   222  O  O    . ILE   A 1 53  ? -13.477 -4.957  4.766   1.00 17.06 ? 32  ILE   A O    1 
ATOM   223  C  CB   . ILE   A 1 53  ? -14.911 -5.860  2.476   1.00 17.52 ? 32  ILE   A CB   1 
ATOM   224  C  CG1  . ILE   A 1 53  ? -15.531 -5.811  1.089   1.00 20.62 ? 32  ILE   A CG1  1 
ATOM   225  C  CG2  . ILE   A 1 53  ? -15.181 -7.206  3.164   1.00 18.05 ? 32  ILE   A CG2  1 
ATOM   226  C  CD1  . ILE   A 1 53  ? -14.779 -6.622  0.056   1.00 23.57 ? 32  ILE   A CD1  1 
ATOM   227  N  N    . HIS   A 1 54  ? -15.359 -4.202  5.703   1.00 16.35 ? 33  HIS   A N    1 
ATOM   228  C  CA   . HIS   A 1 54  ? -14.828 -4.278  7.051   1.00 16.12 ? 33  HIS   A CA   1 
ATOM   229  C  C    . HIS   A 1 54  ? -14.928 -5.714  7.562   1.00 17.69 ? 33  HIS   A C    1 
ATOM   230  O  O    . HIS   A 1 54  ? -15.877 -6.445  7.271   1.00 18.09 ? 33  HIS   A O    1 
ATOM   231  C  CB   . HIS   A 1 54  ? -15.533 -3.245  7.940   1.00 16.72 ? 33  HIS   A CB   1 
ATOM   232  C  CG   . HIS   A 1 54  ? -15.381 -3.654  9.368   1.00 16.40 ? 33  HIS   A CG   1 
ATOM   233  N  ND1  . HIS   A 1 54  ? -16.291 -4.506  9.963   1.00 15.69 ? 33  HIS   A ND1  1 
ATOM   234  C  CD2  . HIS   A 1 54  ? -14.415 -3.435  10.283  1.00 17.02 ? 33  HIS   A CD2  1 
ATOM   235  C  CE1  . HIS   A 1 54  ? -15.877 -4.794  11.197  1.00 15.74 ? 33  HIS   A CE1  1 
ATOM   236  N  NE2  . HIS   A 1 54  ? -14.739 -4.143  11.413  1.00 16.96 ? 33  HIS   A NE2  1 
ATOM   237  N  N    . TYR   A 1 55  ? -13.912 -6.111  8.336   1.00 17.11 ? 34  TYR   A N    1 
ATOM   238  C  CA   . TYR   A 1 55  ? -13.946 -7.397  9.007   1.00 17.69 ? 34  TYR   A CA   1 
ATOM   239  C  C    . TYR   A 1 55  ? -13.175 -7.271  10.316  1.00 16.48 ? 34  TYR   A C    1 
ATOM   240  O  O    . TYR   A 1 55  ? -12.447 -6.293  10.539  1.00 17.96 ? 34  TYR   A O    1 
ATOM   241  C  CB   . TYR   A 1 55  ? -13.314 -8.456  8.088   1.00 19.10 ? 34  TYR   A CB   1 
ATOM   242  C  CG   . TYR   A 1 55  ? -11.811 -8.280  7.934   1.00 20.04 ? 34  TYR   A CG   1 
ATOM   243  C  CD1  . TYR   A 1 55  ? -11.275 -7.351  7.036   1.00 19.02 ? 34  TYR   A CD1  1 
ATOM   244  C  CD2  . TYR   A 1 55  ? -10.929 -8.993  8.744   1.00 20.34 ? 34  TYR   A CD2  1 
ATOM   245  C  CE1  . TYR   A 1 55  ? -9.898  -7.159  6.929   1.00 21.45 ? 34  TYR   A CE1  1 
ATOM   246  C  CE2  . TYR   A 1 55  ? -9.556  -8.813  8.637   1.00 21.95 ? 34  TYR   A CE2  1 
ATOM   247  C  CZ   . TYR   A 1 55  ? -9.040  -7.896  7.731   1.00 22.70 ? 34  TYR   A CZ   1 
ATOM   248  O  OH   . TYR   A 1 55  ? -7.681  -7.712  7.604   1.00 24.93 ? 34  TYR   A OH   1 
ATOM   249  N  N    . HIS   A 1 56  ? -13.335 -8.303  11.145  1.00 16.67 ? 35  HIS   A N    1 
ATOM   250  C  CA   . HIS   A 1 56  ? -12.625 -8.390  12.406  1.00 18.24 ? 35  HIS   A CA   1 
ATOM   251  C  C    . HIS   A 1 56  ? -11.660 -9.570  12.339  1.00 19.50 ? 35  HIS   A C    1 
ATOM   252  O  O    . HIS   A 1 56  ? -10.451 -9.356  12.218  1.00 20.68 ? 35  HIS   A O    1 
ATOM   253  C  CB   . HIS   A 1 56  ? -13.626 -8.409  13.566  1.00 19.02 ? 35  HIS   A CB   1 
ATOM   254  C  CG   . HIS   A 1 56  ? -12.957 -8.548  14.888  1.00 21.25 ? 35  HIS   A CG   1 
ATOM   255  N  ND1  . HIS   A 1 56  ? -13.522 -9.290  15.900  1.00 23.61 ? 35  HIS   A ND1  1 
ATOM   256  C  CD2  . HIS   A 1 56  ? -11.789 -8.086  15.356  1.00 22.32 ? 35  HIS   A CD2  1 
ATOM   257  C  CE1  . HIS   A 1 56  ? -12.721 -9.254  16.958  1.00 24.55 ? 35  HIS   A CE1  1 
ATOM   258  N  NE2  . HIS   A 1 56  ? -11.666 -8.523  16.648  1.00 23.60 ? 35  HIS   A NE2  1 
ATOM   259  N  N    . ASN   A 1 57  ? -12.202 -10.796 12.389  1.00 18.62 ? 36  ASN   A N    1 
ATOM   260  C  CA   . ASN   A 1 57  ? -11.382 -12.001 12.395  1.00 20.42 ? 36  ASN   A CA   1 
ATOM   261  C  C    . ASN   A 1 57  ? -11.300 -12.654 11.016  1.00 21.08 ? 36  ASN   A C    1 
ATOM   262  O  O    . ASN   A 1 57  ? -10.366 -13.419 10.782  1.00 24.12 ? 36  ASN   A O    1 
ATOM   263  C  CB   . ASN   A 1 57  ? -11.849 -13.039 13.415  1.00 21.51 ? 36  ASN   A CB   1 
ATOM   264  C  CG   . ASN   A 1 57  ? -11.738 -12.557 14.846  1.00 24.28 ? 36  ASN   A CG   1 
ATOM   265  O  OD1  . ASN   A 1 57  ? -10.755 -11.902 15.218  1.00 26.65 ? 36  ASN   A OD1  1 
ATOM   266  N  ND2  . ASN   A 1 57  ? -12.751 -12.836 15.655  1.00 26.98 ? 36  ASN   A ND2  1 
ATOM   267  N  N    . SER   A 1 58  ? -12.234 -12.377 10.098  1.00 19.39 ? 37  SER   A N    1 
ATOM   268  C  CA   . SER   A 1 58  ? -12.353 -13.164 8.876   1.00 20.19 ? 37  SER   A CA   1 
ATOM   269  C  C    . SER   A 1 58  ? -11.510 -12.559 7.746   1.00 19.59 ? 37  SER   A C    1 
ATOM   270  O  O    . SER   A 1 58  ? -12.008 -12.155 6.700   1.00 19.30 ? 37  SER   A O    1 
ATOM   271  C  CB   . SER   A 1 58  ? -13.811 -13.368 8.488   1.00 19.63 ? 37  SER   A CB   1 
ATOM   272  O  OG   . SER   A 1 58  ? -14.473 -14.084 9.519   1.00 21.70 ? 37  SER   A OG   1 
ATOM   273  N  N    . ALA   A 1 59  ? -10.189 -12.540 7.948   1.00 21.42 ? 38  ALA   A N    1 
ATOM   274  C  CA   . ALA   A 1 59  ? -9.291  -11.871 7.022   1.00 20.71 ? 38  ALA   A CA   1 
ATOM   275  C  C    . ALA   A 1 59  ? -9.271  -12.557 5.656   1.00 20.32 ? 38  ALA   A C    1 
ATOM   276  O  O    . ALA   A 1 59  ? -9.354  -11.877 4.633   1.00 21.90 ? 38  ALA   A O    1 
ATOM   277  C  CB   . ALA   A 1 59  ? -7.896  -11.791 7.618   1.00 23.04 ? 38  ALA   A CB   1 
ATOM   278  N  N    . GLU   A 1 60  ? -9.158  -13.892 5.658   1.00 20.91 ? 39  GLU   A N    1 
ATOM   279  C  CA   . GLU   A 1 60  ? -9.050  -14.640 4.414   1.00 24.06 ? 39  GLU   A CA   1 
ATOM   280  C  C    . GLU   A 1 60  ? -10.327 -14.444 3.598   1.00 22.69 ? 39  GLU   A C    1 
ATOM   281  O  O    . GLU   A 1 60  ? -10.269 -14.202 2.397   1.00 22.75 ? 39  GLU   A O    1 
ATOM   282  C  CB   . GLU   A 1 60  ? -8.772  -16.113 4.723   1.00 26.19 ? 39  GLU   A CB   1 
ATOM   283  C  CG   . GLU   A 1 60  ? -9.055  -17.053 3.553   0.60 31.42 ? 39  GLU   A CG   1 
ATOM   284  C  CD   . GLU   A 1 60  ? -8.733  -18.522 3.779   0.60 35.89 ? 39  GLU   A CD   1 
ATOM   285  O  OE1  . GLU   A 1 60  ? -8.066  -19.115 2.905   0.60 38.08 ? 39  GLU   A OE1  1 
ATOM   286  O  OE2  . GLU   A 1 60  ? -9.152  -19.080 4.814   0.60 39.48 ? 39  GLU   A OE2  1 
ATOM   287  N  N    . ALA   A 1 61  ? -11.484 -14.521 4.275   1.00 22.09 ? 40  ALA   A N    1 
ATOM   288  C  CA   . ALA   A 1 61  ? -12.751 -14.370 3.578   1.00 20.30 ? 40  ALA   A CA   1 
ATOM   289  C  C    . ALA   A 1 61  ? -12.907 -12.952 3.034   1.00 19.31 ? 40  ALA   A C    1 
ATOM   290  O  O    . ALA   A 1 61  ? -13.465 -12.773 1.947   1.00 20.49 ? 40  ALA   A O    1 
ATOM   291  C  CB   . ALA   A 1 61  ? -13.914 -14.749 4.479   1.00 21.86 ? 40  ALA   A CB   1 
ATOM   292  N  N    . ALA   A 1 62  ? -12.474 -11.953 3.816   1.00 18.19 ? 41  ALA   A N    1 
ATOM   293  C  CA   . ALA   A 1 62  ? -12.622 -10.564 3.404   1.00 18.45 ? 41  ALA   A CA   1 
ATOM   294  C  C    . ALA   A 1 62  ? -11.815 -10.305 2.130   1.00 20.60 ? 41  ALA   A C    1 
ATOM   295  O  O    . ALA   A 1 62  ? -12.288 -9.655  1.195   1.00 19.76 ? 41  ALA   A O    1 
ATOM   296  C  CB   . ALA   A 1 62  ? -12.207 -9.621  4.525   1.00 18.28 ? 41  ALA   A CB   1 
ATOM   297  N  N    . VAL   A 1 63  ? -10.577 -10.811 2.120   1.00 22.22 ? 42  VAL   A N    1 
ATOM   298  C  CA   . VAL   A 1 63  ? -9.682  -10.558 1.003   1.00 22.93 ? 42  VAL   A CA   1 
ATOM   299  C  C    . VAL   A 1 63  ? -10.177 -11.318 -0.226  1.00 23.18 ? 42  VAL   A C    1 
ATOM   300  O  O    . VAL   A 1 63  ? -10.155 -10.771 -1.326  1.00 23.34 ? 42  VAL   A O    1 
ATOM   301  C  CB   . VAL   A 1 63  ? -8.219  -10.882 1.363   1.00 24.47 ? 42  VAL   A CB   1 
ATOM   302  C  CG1  . VAL   A 1 63  ? -7.316  -10.958 0.136   1.00 25.24 ? 42  VAL   A CG1  1 
ATOM   303  C  CG2  . VAL   A 1 63  ? -7.660  -9.884  2.374   1.00 25.62 ? 42  VAL   A CG2  1 
ATOM   304  N  N    . SER   A 1 64  ? -10.686 -12.537 -0.011  1.00 23.07 ? 43  SER   A N    1 
ATOM   305  C  CA   . SER   A 1 64  ? -11.265 -13.317 -1.089  1.00 23.75 ? 43  SER   A CA   1 
ATOM   306  C  C    . SER   A 1 64  ? -12.417 -12.563 -1.754  1.00 23.57 ? 43  SER   A C    1 
ATOM   307  O  O    . SER   A 1 64  ? -12.540 -12.541 -2.979  1.00 23.82 ? 43  SER   A O    1 
ATOM   308  C  CB   . SER   A 1 64  ? -11.708 -14.667 -0.591  1.00 25.30 ? 43  SER   A CB   1 
ATOM   309  O  OG   . SER   A 1 64  ? -12.133 -15.467 -1.685  1.00 29.00 ? 43  SER   A OG   1 
ATOM   310  N  N    . LEU   A 1 65  ? -13.286 -11.955 -0.932  1.00 21.05 ? 44  LEU   A N    1 
ATOM   311  C  CA   . LEU   A 1 65  ? -14.397 -11.196 -1.476  1.00 20.77 ? 44  LEU   A CA   1 
ATOM   312  C  C    . LEU   A 1 65  ? -13.888 -9.983  -2.262  1.00 21.26 ? 44  LEU   A C    1 
ATOM   313  O  O    . LEU   A 1 65  ? -14.367 -9.735  -3.362  1.00 21.57 ? 44  LEU   A O    1 
ATOM   314  C  CB   . LEU   A 1 65  ? -15.369 -10.805 -0.355  1.00 18.66 ? 44  LEU   A CB   1 
ATOM   315  C  CG   . LEU   A 1 65  ? -16.463 -9.809  -0.768  1.00 19.07 ? 44  LEU   A CG   1 
ATOM   316  C  CD1  . LEU   A 1 65  ? -17.348 -10.378 -1.866  1.00 19.18 ? 44  LEU   A CD1  1 
ATOM   317  C  CD2  . LEU   A 1 65  ? -17.299 -9.393  0.445   1.00 18.68 ? 44  LEU   A CD2  1 
ATOM   318  N  N    . ALA   A 1 66  ? -12.943 -9.219  -1.698  1.00 21.74 ? 45  ALA   A N    1 
ATOM   319  C  CA   . ALA   A 1 66  ? -12.418 -8.023  -2.350  1.00 21.34 ? 45  ALA   A CA   1 
ATOM   320  C  C    . ALA   A 1 66  ? -11.802 -8.372  -3.708  1.00 22.99 ? 45  ALA   A C    1 
ATOM   321  O  O    . ALA   A 1 66  ? -11.996 -7.634  -4.674  1.00 22.38 ? 45  ALA   A O    1 
ATOM   322  C  CB   . ALA   A 1 66  ? -11.421 -7.316  -1.448  1.00 22.02 ? 45  ALA   A CB   1 
ATOM   323  N  N    . ASP   A 1 67  ? -11.111 -9.517  -3.762  1.00 25.11 ? 46  ASP   A N    1 
ATOM   324  C  CA   . ASP   A 1 67  ? -10.483 -10.012 -4.984  1.00 25.77 ? 46  ASP   A CA   1 
ATOM   325  C  C    . ASP   A 1 67  ? -11.525 -10.283 -6.068  1.00 26.19 ? 46  ASP   A C    1 
ATOM   326  O  O    . ASP   A 1 67  ? -11.350 -9.875  -7.218  1.00 27.31 ? 46  ASP   A O    1 
ATOM   327  C  CB   . ASP   A 1 67  ? -9.693  -11.284 -4.723  1.00 28.76 ? 46  ASP   A CB   1 
ATOM   328  C  CG   . ASP   A 1 67  ? -8.341  -11.111 -4.053  1.00 32.28 ? 46  ASP   A CG   1 
ATOM   329  O  OD1  . ASP   A 1 67  ? -7.920  -9.948  -3.877  1.00 34.95 ? 46  ASP   A OD1  1 
ATOM   330  O  OD2  . ASP   A 1 67  ? -7.719  -12.145 -3.701  1.00 36.18 ? 46  ASP   A OD2  1 
ATOM   331  N  N    . GLU   A 1 68  ? -12.603 -10.987 -5.708  1.00 24.79 ? 47  GLU   A N    1 
ATOM   332  C  CA   . GLU   A 1 68  ? -13.682 -11.252 -6.647  1.00 25.94 ? 47  GLU   A CA   1 
ATOM   333  C  C    . GLU   A 1 68  ? -14.263 -9.944  -7.181  1.00 25.46 ? 47  GLU   A C    1 
ATOM   334  O  O    . GLU   A 1 68  ? -14.555 -9.809  -8.373  1.00 25.25 ? 47  GLU   A O    1 
ATOM   335  C  CB   . GLU   A 1 68  ? -14.802 -12.049 -5.986  1.00 27.27 ? 47  GLU   A CB   1 
ATOM   336  C  CG   . GLU   A 1 68  ? -14.471 -13.520 -5.773  1.00 30.62 ? 47  GLU   A CG   1 
ATOM   337  C  CD   . GLU   A 1 68  ? -15.770 -14.262 -5.497  1.00 32.41 ? 47  GLU   A CD   1 
ATOM   338  O  OE1  . GLU   A 1 68  ? -15.901 -14.855 -4.405  1.00 33.94 ? 47  GLU   A OE1  1 
ATOM   339  O  OE2  . GLU   A 1 68  ? -16.647 -14.265 -6.395  1.00 37.82 ? 47  GLU   A OE2  1 
ATOM   340  N  N    . LEU   A 1 69  ? -14.464 -8.969  -6.288  1.00 23.44 ? 48  LEU   A N    1 
ATOM   341  C  CA   . LEU   A 1 69  ? -15.105 -7.739  -6.701  1.00 22.75 ? 48  LEU   A CA   1 
ATOM   342  C  C    . LEU   A 1 69  ? -14.177 -6.923  -7.600  1.00 23.31 ? 48  LEU   A C    1 
ATOM   343  O  O    . LEU   A 1 69  ? -14.635 -6.294  -8.551  1.00 21.72 ? 48  LEU   A O    1 
ATOM   344  C  CB   . LEU   A 1 69  ? -15.555 -6.962  -5.467  1.00 21.94 ? 48  LEU   A CB   1 
ATOM   345  C  CG   . LEU   A 1 69  ? -16.650 -7.639  -4.632  1.00 21.05 ? 48  LEU   A CG   1 
ATOM   346  C  CD1  . LEU   A 1 69  ? -17.059 -6.679  -3.510  1.00 21.78 ? 48  LEU   A CD1  1 
ATOM   347  C  CD2  . LEU   A 1 69  ? -17.852 -8.097  -5.441  1.00 21.86 ? 48  LEU   A CD2  1 
ATOM   348  N  N    . ASN   A 1 70  ? -12.877 -6.949  -7.289  1.00 24.00 ? 49  ASN   A N    1 
ATOM   349  C  CA   . ASN   A 1 70  ? -11.910 -6.207  -8.083  1.00 22.77 ? 49  ASN   A CA   1 
ATOM   350  C  C    . ASN   A 1 70  ? -11.718 -6.864  -9.453  1.00 24.78 ? 49  ASN   A C    1 
ATOM   351  O  O    . ASN   A 1 70  ? -11.352 -6.185  -10.403 1.00 25.23 ? 49  ASN   A O    1 
ATOM   352  C  CB   . ASN   A 1 70  ? -10.601 -6.014  -7.331  1.00 21.52 ? 49  ASN   A CB   1 
ATOM   353  C  CG   . ASN   A 1 70  ? -10.721 -4.933  -6.283  1.00 20.61 ? 49  ASN   A CG   1 
ATOM   354  O  OD1  . ASN   A 1 70  ? -11.315 -3.878  -6.549  1.00 21.64 ? 49  ASN   A OD1  1 
ATOM   355  N  ND2  . ASN   A 1 70  ? -10.170 -5.183  -5.109  1.00 20.19 ? 49  ASN   A ND2  1 
ATOM   356  N  N    . LYS   A 1 71  ? -11.965 -8.172  -9.543  1.00 26.29 ? 50  LYS   A N    1 
ATOM   357  C  CA   A LYS   A 1 71  ? -11.880 -8.900  -10.802 0.50 26.89 ? 50  LYS   A CA   1 
ATOM   358  C  CA   B LYS   A 1 71  ? -11.851 -8.859  -10.818 0.50 26.85 ? 50  LYS   A CA   1 
ATOM   359  C  C    . LYS   A 1 71  ? -13.007 -8.454  -11.732 1.00 28.78 ? 50  LYS   A C    1 
ATOM   360  O  O    . LYS   A 1 71  ? -12.865 -8.475  -12.953 1.00 28.75 ? 50  LYS   A O    1 
ATOM   361  C  CB   A LYS   A 1 71  ? -11.965 -10.406 -10.525 0.50 26.61 ? 50  LYS   A CB   1 
ATOM   362  C  CB   B LYS   A 1 71  ? -11.737 -10.369 -10.586 0.50 26.78 ? 50  LYS   A CB   1 
ATOM   363  C  CG   A LYS   A 1 71  ? -11.943 -11.345 -11.732 0.50 26.55 ? 50  LYS   A CG   1 
ATOM   364  C  CG   B LYS   A 1 71  ? -10.340 -10.839 -10.206 0.50 26.64 ? 50  LYS   A CG   1 
ATOM   365  C  CD   A LYS   A 1 71  ? -12.069 -12.808 -11.326 0.50 26.38 ? 50  LYS   A CD   1 
ATOM   366  C  CD   B LYS   A 1 71  ? -10.298 -12.302 -9.781  0.50 27.14 ? 50  LYS   A CD   1 
ATOM   367  N  N    . GLU   A 1 72  ? -14.150 -8.077  -11.141 1.00 27.50 ? 51  GLU   A N    1 
ATOM   368  C  CA   . GLU   A 1 72  ? -15.299 -7.642  -11.912 1.00 27.33 ? 51  GLU   A CA   1 
ATOM   369  C  C    . GLU   A 1 72  ? -15.087 -6.206  -12.383 1.00 28.70 ? 51  GLU   A C    1 
ATOM   370  O  O    . GLU   A 1 72  ? -15.397 -5.875  -13.530 1.00 30.00 ? 51  GLU   A O    1 
ATOM   371  C  CB   . GLU   A 1 72  ? -16.579 -7.758  -11.079 1.00 31.38 ? 51  GLU   A CB   1 
ATOM   372  C  CG   . GLU   A 1 72  ? -17.827 -8.054  -11.907 0.60 35.71 ? 51  GLU   A CG   1 
ATOM   373  C  CD   . GLU   A 1 72  ? -18.030 -9.508  -12.301 0.60 37.24 ? 51  GLU   A CD   1 
ATOM   374  O  OE1  . GLU   A 1 72  ? -17.251 -10.392 -11.882 0.60 39.43 ? 51  GLU   A OE1  1 
ATOM   375  O  OE2  . GLU   A 1 72  ? -18.998 -9.759  -13.045 0.60 42.07 ? 51  GLU   A OE2  1 
ATOM   376  N  N    . ARG   A 1 73  ? -14.551 -5.357  -11.499 1.00 27.52 ? 52  ARG   A N    1 
ATOM   377  C  CA   . ARG   A 1 73  ? -14.239 -3.976  -11.827 1.00 28.99 ? 52  ARG   A CA   1 
ATOM   378  C  C    . ARG   A 1 73  ? -13.032 -3.561  -10.992 1.00 29.85 ? 52  ARG   A C    1 
ATOM   379  O  O    . ARG   A 1 73  ? -13.091 -3.566  -9.760  1.00 26.55 ? 52  ARG   A O    1 
ATOM   380  C  CB   . ARG   A 1 73  ? -15.406 -2.999  -11.619 1.00 29.83 ? 52  ARG   A CB   1 
ATOM   381  C  CG   . ARG   A 1 73  ? -16.748 -3.282  -12.283 1.00 31.14 ? 52  ARG   A CG   1 
ATOM   382  C  CD   . ARG   A 1 73  ? -17.633 -2.036  -12.243 1.00 30.19 ? 52  ARG   A CD   1 
ATOM   383  N  NE   . ARG   A 1 73  ? -17.964 -1.562  -10.892 1.00 30.33 ? 52  ARG   A NE   1 
ATOM   384  C  CZ   . ARG   A 1 73  ? -18.839 -2.109  -10.044 1.00 30.98 ? 52  ARG   A CZ   1 
ATOM   385  N  NH1  . ARG   A 1 73  ? -19.525 -3.184  -10.389 1.00 28.25 ? 52  ARG   A NH1  1 
ATOM   386  N  NH2  . ARG   A 1 73  ? -19.033 -1.558  -8.852  1.00 27.36 ? 52  ARG   A NH2  1 
ATOM   387  N  N    . SER   A 1 74  ? -11.912 -3.261  -11.665 1.00 29.99 ? 53  SER   A N    1 
ATOM   388  C  CA   . SER   A 1 74  ? -10.657 -3.034  -10.968 1.00 27.52 ? 53  SER   A CA   1 
ATOM   389  C  C    . SER   A 1 74  ? -10.788 -1.819  -10.056 1.00 25.49 ? 53  SER   A C    1 
ATOM   390  O  O    . SER   A 1 74  ? -11.465 -0.858  -10.397 1.00 27.11 ? 53  SER   A O    1 
ATOM   391  C  CB   . SER   A 1 74  ? -9.513  -2.855  -11.948 1.00 32.58 ? 53  SER   A CB   1 
ATOM   392  O  OG   . SER   A 1 74  ? -9.747  -1.683  -12.713 1.00 36.91 ? 53  SER   A OG   1 
ATOM   393  N  N    . ASN   A 1 75  ? -10.143 -1.891  -8.886  1.00 25.94 ? 54  ASN   A N    1 
ATOM   394  C  CA   . ASN   A 1 75  ? -10.038 -0.771  -7.966  1.00 27.02 ? 54  ASN   A CA   1 
ATOM   395  C  C    . ASN   A 1 75  ? -11.404 -0.368  -7.411  1.00 26.50 ? 54  ASN   A C    1 
ATOM   396  O  O    . ASN   A 1 75  ? -11.681 0.823   -7.240  1.00 27.31 ? 54  ASN   A O    1 
ATOM   397  C  CB   . ASN   A 1 75  ? -9.356  0.430   -8.614  1.00 32.12 ? 54  ASN   A CB   1 
ATOM   398  C  CG   . ASN   A 1 75  ? -7.908  0.155   -8.934  0.70 33.33 ? 54  ASN   A CG   1 
ATOM   399  O  OD1  . ASN   A 1 75  ? -7.118  -0.129  -8.029  0.70 36.14 ? 54  ASN   A OD1  1 
ATOM   400  N  ND2  . ASN   A 1 75  ? -7.544  0.233   -10.203 0.70 36.46 ? 54  ASN   A ND2  1 
ATOM   401  N  N    . THR   A 1 76  ? -12.246 -1.363  -7.100  1.00 22.85 ? 55  THR   A N    1 
ATOM   402  C  CA   . THR   A 1 76  ? -13.572 -1.019  -6.613  1.00 21.55 ? 55  THR   A CA   1 
ATOM   403  C  C    . THR   A 1 76  ? -13.846 -1.590  -5.221  1.00 22.48 ? 55  THR   A C    1 
ATOM   404  O  O    . THR   A 1 76  ? -14.938 -1.370  -4.689  1.00 22.80 ? 55  THR   A O    1 
ATOM   405  C  CB   . THR   A 1 76  ? -14.665 -1.412  -7.612  1.00 21.83 ? 55  THR   A CB   1 
ATOM   406  O  OG1  . THR   A 1 76  ? -14.608 -2.824  -7.794  1.00 21.84 ? 55  THR   A OG1  1 
ATOM   407  C  CG2  . THR   A 1 76  ? -14.608 -0.592  -8.891  1.00 23.81 ? 55  THR   A CG2  1 
ATOM   408  N  N    . ALA   A 1 77  ? -12.898 -2.339  -4.653  1.00 20.16 ? 56  ALA   A N    1 
ATOM   409  C  CA   . ALA   A 1 77  ? -13.097 -2.947  -3.343  1.00 19.42 ? 56  ALA   A CA   1 
ATOM   410  C  C    . ALA   A 1 77  ? -11.805 -2.903  -2.527  1.00 21.00 ? 56  ALA   A C    1 
ATOM   411  O  O    . ALA   A 1 77  ? -10.723 -3.202  -3.033  1.00 21.24 ? 56  ALA   A O    1 
ATOM   412  C  CB   . ALA   A 1 77  ? -13.602 -4.373  -3.478  1.00 18.15 ? 56  ALA   A CB   1 
ATOM   413  N  N    . VAL   A 1 78  ? -11.923 -2.553  -1.239  1.00 19.21 ? 57  VAL   A N    1 
ATOM   414  C  CA   . VAL   A 1 78  ? -10.821 -2.643  -0.292  1.00 20.36 ? 57  VAL   A CA   1 
ATOM   415  C  C    . VAL   A 1 78  ? -11.336 -3.306  0.980   1.00 19.71 ? 57  VAL   A C    1 
ATOM   416  O  O    . VAL   A 1 78  ? -12.554 -3.326  1.208   1.00 20.58 ? 57  VAL   A O    1 
ATOM   417  C  CB   . VAL   A 1 78  ? -10.175 -1.286  0.054   1.00 21.55 ? 57  VAL   A CB   1 
ATOM   418  C  CG1  . VAL   A 1 78  ? -9.539  -0.654  -1.179  1.00 23.26 ? 57  VAL   A CG1  1 
ATOM   419  C  CG2  . VAL   A 1 78  ? -11.179 -0.334  0.713   1.00 21.12 ? 57  VAL   A CG2  1 
ATOM   420  N  N    . VAL   A 1 79  ? -10.407 -3.814  1.791   1.00 19.48 ? 58  VAL   A N    1 
ATOM   421  C  CA   . VAL   A 1 79  ? -10.729 -4.396  3.089   1.00 19.80 ? 58  VAL   A CA   1 
ATOM   422  C  C    . VAL   A 1 79  ? -10.262 -3.454  4.190   1.00 22.24 ? 58  VAL   A C    1 
ATOM   423  O  O    . VAL   A 1 79  ? -9.357  -2.638  3.993   1.00 22.19 ? 58  VAL   A O    1 
ATOM   424  C  CB   . VAL   A 1 79  ? -10.196 -5.824  3.343   1.00 21.49 ? 58  VAL   A CB   1 
ATOM   425  C  CG1  . VAL   A 1 79  ? -10.689 -6.801  2.285   1.00 19.88 ? 58  VAL   A CG1  1 
ATOM   426  C  CG2  . VAL   A 1 79  ? -8.668  -5.857  3.491   1.00 22.18 ? 58  VAL   A CG2  1 
ATOM   427  N  N    . CYS   A 1 80  ? -10.906 -3.569  5.361   1.00 20.21 ? 59  CYS   A N    1 
ATOM   428  C  CA   . CYS   A 1 80  ? -10.497 -2.754  6.495   1.00 18.82 ? 59  CYS   A CA   1 
ATOM   429  C  C    . CYS   A 1 80  ? -10.741 -3.533  7.774   1.00 19.15 ? 59  CYS   A C    1 
ATOM   430  O  O    . CYS   A 1 80  ? -11.879 -3.890  8.050   1.00 17.93 ? 59  CYS   A O    1 
ATOM   431  C  CB   . CYS   A 1 80  ? -11.256 -1.425  6.527   1.00 19.79 ? 59  CYS   A CB   1 
ATOM   432  S  SG   . CYS   A 1 80  ? -10.876 -0.338  7.933   1.00 23.74 ? 59  CYS   A SG   1 
ATOM   433  N  N    . GLN   A 1 81  ? -9.685  -3.750  8.566   1.00 18.20 ? 60  GLN   A N    1 
ATOM   434  C  CA   . GLN   A 1 81  ? -9.840  -4.556  9.767   1.00 19.40 ? 60  GLN   A CA   1 
ATOM   435  C  C    . GLN   A 1 81  ? -10.104 -3.651  10.962  1.00 18.67 ? 60  GLN   A C    1 
ATOM   436  O  O    . GLN   A 1 81  ? -9.428  -2.633  11.140  1.00 20.02 ? 60  GLN   A O    1 
ATOM   437  C  CB   . GLN   A 1 81  ? -8.552  -5.338  10.042  1.00 18.98 ? 60  GLN   A CB   1 
ATOM   438  C  CG   . GLN   A 1 81  ? -8.714  -6.464  11.068  1.00 21.08 ? 60  GLN   A CG   1 
ATOM   439  C  CD   . GLN   A 1 81  ? -8.580  -6.030  12.515  1.00 22.82 ? 60  GLN   A CD   1 
ATOM   440  O  OE1  . GLN   A 1 81  ? -7.992  -4.992  12.842  1.00 26.21 ? 60  GLN   A OE1  1 
ATOM   441  N  NE2  . GLN   A 1 81  ? -9.108  -6.846  13.417  1.00 26.36 ? 60  GLN   A NE2  1 
ATOM   442  N  N    . ALA   A 1 82  ? -11.085 -4.039  11.789  1.00 18.15 ? 61  ALA   A N    1 
ATOM   443  C  CA   . ALA   A 1 82  ? -11.285 -3.344  13.054  1.00 17.02 ? 61  ALA   A CA   1 
ATOM   444  C  C    . ALA   A 1 82  ? -12.103 -4.204  14.015  1.00 16.76 ? 61  ALA   A C    1 
ATOM   445  O  O    . ALA   A 1 82  ? -13.063 -4.868  13.617  1.00 18.41 ? 61  ALA   A O    1 
ATOM   446  C  CB   . ALA   A 1 82  ? -11.964 -1.997  12.841  1.00 17.83 ? 61  ALA   A CB   1 
ATOM   447  N  N    . ASP   A 1 83  ? -11.712 -4.160  15.299  1.00 16.37 ? 62  ASP   A N    1 
ATOM   448  C  CA   . ASP   A 1 83  ? -12.527 -4.657  16.394  1.00 17.42 ? 62  ASP   A CA   1 
ATOM   449  C  C    . ASP   A 1 83  ? -13.550 -3.587  16.782  1.00 16.60 ? 62  ASP   A C    1 
ATOM   450  O  O    . ASP   A 1 83  ? -13.180 -2.444  17.055  1.00 17.92 ? 62  ASP   A O    1 
ATOM   451  C  CB   . ASP   A 1 83  ? -11.618 -4.958  17.580  1.00 19.12 ? 62  ASP   A CB   1 
ATOM   452  C  CG   . ASP   A 1 83  ? -12.255 -5.746  18.713  1.00 22.33 ? 62  ASP   A CG   1 
ATOM   453  O  OD1  . ASP   A 1 83  ? -13.467 -5.997  18.650  1.00 20.04 ? 62  ASP   A OD1  1 
ATOM   454  O  OD2  . ASP   A 1 83  ? -11.516 -6.121  19.652  1.00 25.06 ? 62  ASP   A OD2  1 
ATOM   455  N  N    . LEU   A 1 84  ? -14.838 -3.977  16.836  1.00 16.38 ? 63  LEU   A N    1 
ATOM   456  C  CA   . LEU   A 1 84  ? -15.916 -3.049  17.184  1.00 15.74 ? 63  LEU   A CA   1 
ATOM   457  C  C    . LEU   A 1 84  ? -16.435 -3.265  18.608  1.00 16.41 ? 63  LEU   A C    1 
ATOM   458  O  O    . LEU   A 1 84  ? -17.468 -2.703  18.983  1.00 16.86 ? 63  LEU   A O    1 
ATOM   459  C  CB   . LEU   A 1 84  ? -17.023 -3.104  16.124  1.00 15.79 ? 63  LEU   A CB   1 
ATOM   460  C  CG   . LEU   A 1 84  ? -16.592 -2.679  14.714  1.00 16.36 ? 63  LEU   A CG   1 
ATOM   461  C  CD1  . LEU   A 1 84  ? -17.727 -2.940  13.751  1.00 19.39 ? 63  LEU   A CD1  1 
ATOM   462  C  CD2  . LEU   A 1 84  ? -16.115 -1.229  14.623  1.00 18.86 ? 63  LEU   A CD2  1 
ATOM   463  N  N    . THR   A 1 85  ? -15.694 -4.025  19.416  1.00 15.84 ? 64  THR   A N    1 
ATOM   464  C  CA   . THR   A 1 85  ? -15.917 -4.125  20.858  1.00 16.63 ? 64  THR   A CA   1 
ATOM   465  C  C    . THR   A 1 85  ? -15.843 -2.741  21.494  1.00 15.71 ? 64  THR   A C    1 
ATOM   466  O  O    . THR   A 1 85  ? -15.001 -1.909  21.139  1.00 16.21 ? 64  THR   A O    1 
ATOM   467  C  CB   . THR   A 1 85  ? -14.872 -5.040  21.500  1.00 17.71 ? 64  THR   A CB   1 
ATOM   468  O  OG1  . THR   A 1 85  ? -14.989 -6.311  20.871  1.00 20.45 ? 64  THR   A OG1  1 
ATOM   469  C  CG2  . THR   A 1 85  ? -15.139 -5.240  22.982  1.00 18.94 ? 64  THR   A CG2  1 
ATOM   470  N  N    . ASN   A 1 86  ? -16.746 -2.462  22.439  1.00 14.76 ? 65  ASN   A N    1 
ATOM   471  C  CA   . ASN   A 1 86  ? -16.661 -1.190  23.143  1.00 15.19 ? 65  ASN   A CA   1 
ATOM   472  C  C    . ASN   A 1 86  ? -15.344 -1.095  23.919  1.00 16.12 ? 65  ASN   A C    1 
ATOM   473  O  O    . ASN   A 1 86  ? -14.931 -2.046  24.585  1.00 17.33 ? 65  ASN   A O    1 
ATOM   474  C  CB   . ASN   A 1 86  ? -17.843 -1.016  24.096  1.00 15.50 ? 65  ASN   A CB   1 
ATOM   475  C  CG   . ASN   A 1 86  ? -17.983 0.392   24.629  1.00 17.02 ? 65  ASN   A CG   1 
ATOM   476  O  OD1  . ASN   A 1 86  ? -17.767 1.370   23.904  1.00 16.25 ? 65  ASN   A OD1  1 
ATOM   477  N  ND2  . ASN   A 1 86  ? -18.344 0.506   25.901  1.00 18.52 ? 65  ASN   A ND2  1 
ATOM   478  N  N    . SER   A 1 87  ? -14.752 0.105   23.863  1.00 15.33 ? 66  SER   A N    1 
ATOM   479  C  CA   . SER   A 1 87  ? -13.562 0.459   24.624  1.00 15.88 ? 66  SER   A CA   1 
ATOM   480  C  C    . SER   A 1 87  ? -13.332 1.954   24.444  1.00 15.75 ? 66  SER   A C    1 
ATOM   481  O  O    . SER   A 1 87  ? -14.019 2.610   23.655  1.00 16.52 ? 66  SER   A O    1 
ATOM   482  C  CB   . SER   A 1 87  ? -12.344 -0.314  24.158  1.00 17.79 ? 66  SER   A CB   1 
ATOM   483  O  OG   . SER   A 1 87  ? -11.819 0.285   22.971  1.00 18.30 ? 66  SER   A OG   1 
ATOM   484  N  N    . ASN   A 1 88  ? -12.311 2.482   25.135  1.00 17.01 ? 67  ASN   A N    1 
ATOM   485  C  CA   . ASN   A 1 88  ? -12.031 3.907   25.024  1.00 17.35 ? 67  ASN   A CA   1 
ATOM   486  C  C    . ASN   A 1 88  ? -11.362 4.254   23.693  1.00 18.28 ? 67  ASN   A C    1 
ATOM   487  O  O    . ASN   A 1 88  ? -11.256 5.438   23.384  1.00 20.28 ? 67  ASN   A O    1 
ATOM   488  C  CB   . ASN   A 1 88  ? -11.197 4.416   26.197  1.00 18.07 ? 67  ASN   A CB   1 
ATOM   489  C  CG   . ASN   A 1 88  ? -12.013 4.540   27.462  1.00 20.40 ? 67  ASN   A CG   1 
ATOM   490  O  OD1  . ASN   A 1 88  ? -13.246 4.590   27.398  1.00 20.76 ? 67  ASN   A OD1  1 
ATOM   491  N  ND2  . ASN   A 1 88  ? -11.359 4.622   28.609  1.00 21.53 ? 67  ASN   A ND2  1 
ATOM   492  N  N    . VAL   A 1 89  ? -10.982 3.248   22.902  1.00 17.31 ? 68  VAL   A N    1 
ATOM   493  C  CA   A VAL   A 1 89  ? -10.418 3.533   21.587  0.70 16.28 ? 68  VAL   A CA   1 
ATOM   494  C  CA   B VAL   A 1 89  ? -10.375 3.415   21.586  0.30 16.29 ? 68  VAL   A CA   1 
ATOM   495  C  C    . VAL   A 1 89  ? -11.409 3.194   20.477  1.00 16.29 ? 68  VAL   A C    1 
ATOM   496  O  O    . VAL   A 1 89  ? -11.118 3.434   19.312  1.00 16.43 ? 68  VAL   A O    1 
ATOM   497  C  CB   A VAL   A 1 89  ? -9.044  2.898   21.308  0.70 18.07 ? 68  VAL   A CB   1 
ATOM   498  C  CB   B VAL   A 1 89  ? -9.181  2.447   21.433  0.30 16.53 ? 68  VAL   A CB   1 
ATOM   499  C  CG1  A VAL   A 1 89  ? -8.028  3.317   22.365  0.70 19.73 ? 68  VAL   A CG1  1 
ATOM   500  C  CG1  B VAL   A 1 89  ? -8.415  2.669   20.132  0.30 16.18 ? 68  VAL   A CG1  1 
ATOM   501  C  CG2  A VAL   A 1 89  ? -9.138  1.382   21.136  0.70 17.65 ? 68  VAL   A CG2  1 
ATOM   502  C  CG2  B VAL   A 1 89  ? -8.230  2.530   22.620  0.30 17.43 ? 68  VAL   A CG2  1 
ATOM   503  N  N    . LEU   A 1 90  ? -12.615 2.705   20.834  1.00 14.84 ? 69  LEU   A N    1 
ATOM   504  C  CA   . LEU   A 1 90  ? -13.588 2.411   19.783  1.00 14.45 ? 69  LEU   A CA   1 
ATOM   505  C  C    . LEU   A 1 90  ? -13.859 3.654   18.928  1.00 14.35 ? 69  LEU   A C    1 
ATOM   506  O  O    . LEU   A 1 90  ? -13.972 3.502   17.717  1.00 16.05 ? 69  LEU   A O    1 
ATOM   507  C  CB   . LEU   A 1 90  ? -14.857 1.761   20.358  1.00 14.22 ? 69  LEU   A CB   1 
ATOM   508  C  CG   . LEU   A 1 90  ? -15.910 1.424   19.298  1.00 14.78 ? 69  LEU   A CG   1 
ATOM   509  C  CD1  . LEU   A 1 90  ? -15.418 0.355   18.322  1.00 14.26 ? 69  LEU   A CD1  1 
ATOM   510  C  CD2  . LEU   A 1 90  ? -17.177 0.933   19.990  1.00 16.46 ? 69  LEU   A CD2  1 
ATOM   511  N  N    . PRO   A 1 91  ? -13.989 4.896   19.456  1.00 15.24 ? 70  PRO   A N    1 
ATOM   512  C  CA   . PRO   A 1 91  ? -14.172 6.064   18.597  1.00 15.31 ? 70  PRO   A CA   1 
ATOM   513  C  C    . PRO   A 1 91  ? -13.105 6.226   17.514  1.00 15.06 ? 70  PRO   A C    1 
ATOM   514  O  O    . PRO   A 1 91  ? -13.427 6.509   16.367  1.00 15.36 ? 70  PRO   A O    1 
ATOM   515  C  CB   . PRO   A 1 91  ? -14.237 7.249   19.545  1.00 15.73 ? 70  PRO   A CB   1 
ATOM   516  C  CG   . PRO   A 1 91  ? -14.727 6.625   20.832  1.00 16.75 ? 70  PRO   A CG   1 
ATOM   517  C  CD   . PRO   A 1 91  ? -14.079 5.238   20.888  1.00 15.44 ? 70  PRO   A CD   1 
ATOM   518  N  N    . ALA   A 1 92  ? -11.852 5.960   17.879  1.00 15.47 ? 71  ALA   A N    1 
ATOM   519  C  CA   . ALA   A 1 92  ? -10.770 6.049   16.910  1.00 15.50 ? 71  ALA   A CA   1 
ATOM   520  C  C    . ALA   A 1 92  ? -10.884 4.973   15.826  1.00 16.25 ? 71  ALA   A C    1 
ATOM   521  O  O    . ALA   A 1 92  ? -10.624 5.242   14.650  1.00 18.17 ? 71  ALA   A O    1 
ATOM   522  C  CB   . ALA   A 1 92  ? -9.454  5.990   17.661  1.00 15.28 ? 71  ALA   A CB   1 
ATOM   523  N  N    . SER   A 1 93  ? -11.255 3.742   16.212  1.00 16.24 ? 72  SER   A N    1 
ATOM   524  C  CA   . SER   A 1 93  ? -11.412 2.653   15.267  1.00 15.61 ? 72  SER   A CA   1 
ATOM   525  C  C    . SER   A 1 93  ? -12.510 2.977   14.265  1.00 15.84 ? 72  SER   A C    1 
ATOM   526  O  O    . SER   A 1 93  ? -12.394 2.701   13.079  1.00 16.96 ? 72  SER   A O    1 
ATOM   527  C  CB   . SER   A 1 93  ? -11.724 1.356   15.963  1.00 17.12 ? 72  SER   A CB   1 
ATOM   528  O  OG   . SER   A 1 93  ? -10.627 0.925   16.759  1.00 18.40 ? 72  SER   A OG   1 
ATOM   529  N  N    . CYS   A 1 94  ? -13.604 3.558   14.776  1.00 15.53 ? 73  CYS   A N    1 
ATOM   530  C  CA   . CYS   A 1 94  ? -14.719 3.878   13.899  1.00 15.48 ? 73  CYS   A CA   1 
ATOM   531  C  C    . CYS   A 1 94  ? -14.361 5.003   12.930  1.00 15.70 ? 73  CYS   A C    1 
ATOM   532  O  O    . CYS   A 1 94  ? -14.688 4.948   11.740  1.00 15.58 ? 73  CYS   A O    1 
ATOM   533  C  CB   . CYS   A 1 94  ? -15.965 4.168   14.727  1.00 15.02 ? 73  CYS   A CB   1 
ATOM   534  S  SG   . CYS   A 1 94  ? -16.579 2.672   15.533  1.00 15.56 ? 73  CYS   A SG   1 
ATOM   535  N  N    . GLU   A 1 95  ? -13.664 6.019   13.450  1.00 17.21 ? 74  GLU   A N    1 
ATOM   536  C  CA   . GLU   A 1 95  ? -13.183 7.099   12.611  1.00 18.58 ? 74  GLU   A CA   1 
ATOM   537  C  C    . GLU   A 1 95  ? -12.271 6.534   11.521  1.00 17.80 ? 74  GLU   A C    1 
ATOM   538  O  O    . GLU   A 1 95  ? -12.371 6.942   10.361  1.00 18.64 ? 74  GLU   A O    1 
ATOM   539  C  CB   . GLU   A 1 95  ? -12.472 8.136   13.479  1.00 19.05 ? 74  GLU   A CB   1 
ATOM   540  C  CG   . GLU   A 1 95  ? -11.903 9.284   12.652  1.00 23.58 ? 74  GLU   A CG   1 
ATOM   541  C  CD   . GLU   A 1 95  ? -11.404 10.409  13.531  0.70 27.88 ? 74  GLU   A CD   1 
ATOM   542  O  OE1  . GLU   A 1 95  ? -10.184 10.475  13.798  0.70 33.49 ? 74  GLU   A OE1  1 
ATOM   543  O  OE2  . GLU   A 1 95  ? -12.247 11.222  13.948  0.70 30.11 ? 74  GLU   A OE2  1 
ATOM   544  N  N    . GLU   A 1 96  ? -11.459 5.531   11.882  1.00 17.53 ? 75  GLU   A N    1 
ATOM   545  C  CA   . GLU   A 1 96  ? -10.532 4.929   10.937  1.00 18.95 ? 75  GLU   A CA   1 
ATOM   546  C  C    . GLU   A 1 96  ? -11.235 4.153   9.820   1.00 18.46 ? 75  GLU   A C    1 
ATOM   547  O  O    . GLU   A 1 96  ? -10.780 4.166   8.678   1.00 17.69 ? 75  GLU   A O    1 
ATOM   548  C  CB   . GLU   A 1 96  ? -9.483  4.087   11.665  1.00 21.30 ? 75  GLU   A CB   1 
ATOM   549  C  CG   . GLU   A 1 96  ? -8.514  3.435   10.688  1.00 23.10 ? 75  GLU   A CG   1 
ATOM   550  C  CD   . GLU   A 1 96  ? -7.753  4.377   9.761   1.00 20.07 ? 75  GLU   A CD   1 
ATOM   551  O  OE1  . GLU   A 1 96  ? -7.640  5.624   9.934   1.00 24.49 ? 75  GLU   A OE1  1 
ATOM   552  O  OE2  . GLU   A 1 96  ? -7.251  3.761   8.810   1.00 23.58 ? 75  GLU   A OE2  1 
ATOM   553  N  N    . ILE   A 1 97  ? -12.335 3.450   10.138  1.00 15.81 ? 76  ILE   A N    1 
ATOM   554  C  CA   . ILE   A 1 97  ? -13.091 2.759   9.106   1.00 16.00 ? 76  ILE   A CA   1 
ATOM   555  C  C    . ILE   A 1 97  ? -13.595 3.774   8.074   1.00 15.68 ? 76  ILE   A C    1 
ATOM   556  O  O    . ILE   A 1 97  ? -13.487 3.540   6.869   1.00 17.64 ? 76  ILE   A O    1 
ATOM   557  C  CB   . ILE   A 1 97  ? -14.241 1.942   9.735   1.00 16.35 ? 76  ILE   A CB   1 
ATOM   558  C  CG1  . ILE   A 1 97  ? -13.696 0.779   10.552  1.00 17.90 ? 76  ILE   A CG1  1 
ATOM   559  C  CG2  . ILE   A 1 97  ? -15.165 1.400   8.638   1.00 18.74 ? 76  ILE   A CG2  1 
ATOM   560  C  CD1  . ILE   A 1 97  ? -14.725 0.134   11.486  1.00 16.95 ? 76  ILE   A CD1  1 
ATOM   561  N  N    . ILE   A 1 98  ? -14.186 4.883   8.546   1.00 15.92 ? 77  ILE   A N    1 
ATOM   562  C  CA   . ILE   A 1 98  ? -14.687 5.869   7.605   1.00 16.71 ? 77  ILE   A CA   1 
ATOM   563  C  C    . ILE   A 1 98  ? -13.516 6.452   6.811   1.00 16.76 ? 77  ILE   A C    1 
ATOM   564  O  O    . ILE   A 1 98  ? -13.624 6.599   5.592   1.00 18.36 ? 77  ILE   A O    1 
ATOM   565  C  CB   . ILE   A 1 98  ? -15.543 6.941   8.303   1.00 16.27 ? 77  ILE   A CB   1 
ATOM   566  C  CG1  . ILE   A 1 98  ? -16.754 6.313   9.056   1.00 17.40 ? 77  ILE   A CG1  1 
ATOM   567  C  CG2  . ILE   A 1 98  ? -15.998 8.020   7.314   1.00 18.19 ? 77  ILE   A CG2  1 
ATOM   568  C  CD1  . ILE   A 1 98  ? -17.644 5.449   8.170   1.00 17.63 ? 77  ILE   A CD1  1 
ATOM   569  N  N    . ASN   A 1 99  ? -12.410 6.740   7.504   1.00 18.38 ? 78  ASN   A N    1 
ATOM   570  C  CA   . ASN   A 1 99  ? -11.230 7.284   6.846   1.00 20.38 ? 78  ASN   A CA   1 
ATOM   571  C  C    . ASN   A 1 99  ? -10.778 6.359   5.719   1.00 21.36 ? 78  ASN   A C    1 
ATOM   572  O  O    . ASN   A 1 99  ? -10.329 6.856   4.682   1.00 22.13 ? 78  ASN   A O    1 
ATOM   573  C  CB   . ASN   A 1 99  ? -10.064 7.427   7.817   1.00 21.83 ? 78  ASN   A CB   1 
ATOM   574  C  CG   . ASN   A 1 99  ? -10.161 8.592   8.771   1.00 26.92 ? 78  ASN   A CG   1 
ATOM   575  O  OD1  . ASN   A 1 99  ? -10.965 9.511   8.576   1.00 29.31 ? 78  ASN   A OD1  1 
ATOM   576  N  ND2  . ASN   A 1 99  ? -9.306  8.584   9.786   1.00 29.43 ? 78  ASN   A ND2  1 
ATOM   577  N  N    . SER   A 1 100 ? -10.893 5.030   5.909   1.00 19.52 ? 79  SER   A N    1 
ATOM   578  C  CA   A SER   A 1 100 ? -10.392 4.079   4.927   0.60 19.30 ? 79  SER   A CA   1 
ATOM   579  C  CA   B SER   A 1 100 ? -10.415 4.050   4.938   0.40 19.27 ? 79  SER   A CA   1 
ATOM   580  C  C    . SER   A 1 100 ? -11.198 4.162   3.630   1.00 19.66 ? 79  SER   A C    1 
ATOM   581  O  O    . SER   A 1 100 ? -10.667 3.939   2.541   1.00 20.22 ? 79  SER   A O    1 
ATOM   582  C  CB   A SER   A 1 100 ? -10.333 2.676   5.486   0.60 19.96 ? 79  SER   A CB   1 
ATOM   583  C  CB   B SER   A 1 100 ? -10.433 2.623   5.475   0.40 19.45 ? 79  SER   A CB   1 
ATOM   584  O  OG   A SER   A 1 100 ? -9.511  2.667   6.646   0.60 19.90 ? 79  SER   A OG   1 
ATOM   585  O  OG   B SER   A 1 100 ? -11.723 2.025   5.408   0.40 19.38 ? 79  SER   A OG   1 
ATOM   586  N  N    . CYS   A 1 101 ? -12.493 4.489   3.744   1.00 17.31 ? 80  CYS   A N    1 
ATOM   587  C  CA   . CYS   A 1 101 ? -13.318 4.711   2.571   1.00 18.35 ? 80  CYS   A CA   1 
ATOM   588  C  C    . CYS   A 1 101 ? -12.839 5.946   1.813   1.00 18.63 ? 80  CYS   A C    1 
ATOM   589  O  O    . CYS   A 1 101 ? -12.759 5.927   0.579   1.00 21.04 ? 80  CYS   A O    1 
ATOM   590  C  CB   . CYS   A 1 101 ? -14.794 4.789   2.973   1.00 18.36 ? 80  CYS   A CB   1 
ATOM   591  S  SG   . CYS   A 1 101 ? -15.917 4.607   1.570   1.00 19.84 ? 80  CYS   A SG   1 
ATOM   592  N  N    . PHE   A 1 102 ? -12.544 7.022   2.542   1.00 18.86 ? 81  PHE   A N    1 
ATOM   593  C  CA   . PHE   A 1 102 ? -12.090 8.253   1.905   1.00 20.32 ? 81  PHE   A CA   1 
ATOM   594  C  C    . PHE   A 1 102 ? -10.706 8.070   1.287   1.00 22.72 ? 81  PHE   A C    1 
ATOM   595  O  O    . PHE   A 1 102 ? -10.452 8.611   0.215   1.00 22.98 ? 81  PHE   A O    1 
ATOM   596  C  CB   . PHE   A 1 102 ? -12.099 9.430   2.882   1.00 20.58 ? 81  PHE   A CB   1 
ATOM   597  C  CG   . PHE   A 1 102 ? -13.492 10.023  3.018   1.00 21.17 ? 81  PHE   A CG   1 
ATOM   598  C  CD1  . PHE   A 1 102 ? -13.937 11.032  2.165   1.00 23.02 ? 81  PHE   A CD1  1 
ATOM   599  C  CD2  . PHE   A 1 102 ? -14.364 9.573   4.007   1.00 20.90 ? 81  PHE   A CD2  1 
ATOM   600  C  CE1  . PHE   A 1 102 ? -15.206 11.568  2.305   1.00 23.64 ? 81  PHE   A CE1  1 
ATOM   601  C  CE2  . PHE   A 1 102 ? -15.635 10.118  4.140   1.00 22.16 ? 81  PHE   A CE2  1 
ATOM   602  C  CZ   . PHE   A 1 102 ? -16.057 11.110  3.280   1.00 22.25 ? 81  PHE   A CZ   1 
ATOM   603  N  N    . ARG   A 1 103 ? -9.829  7.310   1.957   1.00 22.19 ? 82  ARG   A N    1 
ATOM   604  C  CA   A ARG   A 1 103 ? -8.488  7.068   1.442   0.50 23.14 ? 82  ARG   A CA   1 
ATOM   605  C  CA   B ARG   A 1 103 ? -8.482  7.048   1.459   0.50 22.91 ? 82  ARG   A CA   1 
ATOM   606  C  C    . ARG   A 1 103 ? -8.571  6.307   0.125   1.00 24.04 ? 82  ARG   A C    1 
ATOM   607  O  O    . ARG   A 1 103 ? -7.843  6.614   -0.816  1.00 24.79 ? 82  ARG   A O    1 
ATOM   608  C  CB   A ARG   A 1 103 ? -7.600  6.281   2.410   0.50 23.51 ? 82  ARG   A CB   1 
ATOM   609  C  CB   B ARG   A 1 103 ? -7.682  6.292   2.531   0.50 22.96 ? 82  ARG   A CB   1 
ATOM   610  C  CG   A ARG   A 1 103 ? -7.005  7.129   3.522   0.50 24.07 ? 82  ARG   A CG   1 
ATOM   611  C  CG   B ARG   A 1 103 ? -6.215  5.951   2.298   0.50 23.42 ? 82  ARG   A CG   1 
ATOM   612  C  CD   A ARG   A 1 103 ? -5.831  6.403   4.162   0.50 24.76 ? 82  ARG   A CD   1 
ATOM   613  C  CD   B ARG   A 1 103 ? -5.630  5.204   3.506   0.50 23.82 ? 82  ARG   A CD   1 
ATOM   614  N  NE   A ARG   A 1 103 ? -6.070  4.967   4.365   0.50 24.44 ? 82  ARG   A NE   1 
ATOM   615  N  NE   B ARG   A 1 103 ? -5.868  5.869   4.796   0.50 27.21 ? 82  ARG   A NE   1 
ATOM   616  C  CZ   A ARG   A 1 103 ? -6.575  4.470   5.490   0.50 24.49 ? 82  ARG   A CZ   1 
ATOM   617  C  CZ   B ARG   A 1 103 ? -6.486  5.340   5.852   0.50 24.92 ? 82  ARG   A CZ   1 
ATOM   618  N  NH1  A ARG   A 1 103 ? -6.759  3.168   5.628   0.50 25.62 ? 82  ARG   A NH1  1 
ATOM   619  N  NH1  B ARG   A 1 103 ? -6.739  6.094   6.908   0.50 25.09 ? 82  ARG   A NH1  1 
ATOM   620  N  NH2  A ARG   A 1 103 ? -6.901  5.287   6.475   0.50 23.42 ? 82  ARG   A NH2  1 
ATOM   621  N  NH2  B ARG   A 1 103 ? -6.879  4.077   5.843   0.50 24.56 ? 82  ARG   A NH2  1 
ATOM   622  N  N    . ALA   A 1 104 ? -9.460  5.309   0.055   1.00 23.08 ? 83  ALA   A N    1 
ATOM   623  C  CA   . ALA   A 1 104 ? -9.523  4.454   -1.122  1.00 22.12 ? 83  ALA   A CA   1 
ATOM   624  C  C    . ALA   A 1 104 ? -10.269 5.129   -2.270  1.00 22.09 ? 83  ALA   A C    1 
ATOM   625  O  O    . ALA   A 1 104 ? -9.868  4.992   -3.430  1.00 22.54 ? 83  ALA   A O    1 
ATOM   626  C  CB   . ALA   A 1 104 ? -10.179 3.139   -0.776  1.00 21.44 ? 83  ALA   A CB   1 
ATOM   627  N  N    . PHE   A 1 105 ? -11.370 5.828   -1.950  1.00 21.49 ? 84  PHE   A N    1 
ATOM   628  C  CA   . PHE   A 1 105 ? -12.336 6.172   -2.988  1.00 19.61 ? 84  PHE   A CA   1 
ATOM   629  C  C    . PHE   A 1 105 ? -12.642 7.662   -3.030  1.00 19.19 ? 84  PHE   A C    1 
ATOM   630  O  O    . PHE   A 1 105 ? -13.337 8.111   -3.944  1.00 22.10 ? 84  PHE   A O    1 
ATOM   631  C  CB   . PHE   A 1 105 ? -13.649 5.412   -2.789  1.00 19.01 ? 84  PHE   A CB   1 
ATOM   632  C  CG   . PHE   A 1 105 ? -13.461 3.907   -2.764  1.00 20.51 ? 84  PHE   A CG   1 
ATOM   633  C  CD1  . PHE   A 1 105 ? -12.747 3.244   -3.760  1.00 20.23 ? 84  PHE   A CD1  1 
ATOM   634  C  CD2  . PHE   A 1 105 ? -13.956 3.157   -1.702  1.00 19.95 ? 84  PHE   A CD2  1 
ATOM   635  C  CE1  . PHE   A 1 105 ? -12.581 1.865   -3.713  1.00 21.43 ? 84  PHE   A CE1  1 
ATOM   636  C  CE2  . PHE   A 1 105 ? -13.803 1.777   -1.673  1.00 20.24 ? 84  PHE   A CE2  1 
ATOM   637  C  CZ   . PHE   A 1 105 ? -13.096 1.133   -2.665  1.00 22.53 ? 84  PHE   A CZ   1 
ATOM   638  N  N    . GLY   A 1 106 ? -12.169 8.405   -2.030  1.00 19.31 ? 85  GLY   A N    1 
ATOM   639  C  CA   . GLY   A 1 106 ? -12.317 9.851   -2.014  1.00 18.76 ? 85  GLY   A CA   1 
ATOM   640  C  C    . GLY   A 1 106 ? -13.709 10.338  -1.609  1.00 21.30 ? 85  GLY   A C    1 
ATOM   641  O  O    . GLY   A 1 106 ? -13.995 11.536  -1.669  1.00 22.52 ? 85  GLY   A O    1 
ATOM   642  N  N    . ARG   A 1 107 ? -14.564 9.422   -1.143  1.00 19.85 ? 86  ARG   A N    1 
ATOM   643  C  CA   . ARG   A 1 107 ? -15.912 9.806   -0.753  1.00 18.91 ? 86  ARG   A CA   1 
ATOM   644  C  C    . ARG   A 1 107 ? -16.506 8.625   0.010   1.00 19.29 ? 86  ARG   A C    1 
ATOM   645  O  O    . ARG   A 1 107 ? -15.965 7.516   -0.052  1.00 19.91 ? 86  ARG   A O    1 
ATOM   646  C  CB   . ARG   A 1 107 ? -16.753 10.056  -2.014  1.00 19.29 ? 86  ARG   A CB   1 
ATOM   647  C  CG   . ARG   A 1 107 ? -16.841 8.858   -2.950  1.00 18.95 ? 86  ARG   A CG   1 
ATOM   648  C  CD   . ARG   A 1 107 ? -17.465 9.198   -4.305  1.00 20.87 ? 86  ARG   A CD   1 
ATOM   649  N  NE   . ARG   A 1 107 ? -18.880 9.562   -4.161  1.00 21.85 ? 86  ARG   A NE   1 
ATOM   650  C  CZ   . ARG   A 1 107 ? -19.627 10.102  -5.102  1.00 26.24 ? 86  ARG   A CZ   1 
ATOM   651  N  NH1  . ARG   A 1 107 ? -19.084 10.405  -6.272  1.00 28.51 ? 86  ARG   A NH1  1 
ATOM   652  N  NH2  . ARG   A 1 107 ? -20.903 10.352  -4.868  1.00 26.06 ? 86  ARG   A NH2  1 
ATOM   653  N  N    . CYS   A 1 108 ? -17.605 8.882   0.728   1.00 19.73 ? 87  CYS   A N    1 
ATOM   654  C  CA   . CYS   A 1 108 ? -18.301 7.822   1.432   1.00 18.70 ? 87  CYS   A CA   1 
ATOM   655  C  C    . CYS   A 1 108 ? -19.786 8.181   1.447   1.00 17.33 ? 87  CYS   A C    1 
ATOM   656  O  O    . CYS   A 1 108 ? -20.192 9.101   2.160   1.00 19.44 ? 87  CYS   A O    1 
ATOM   657  C  CB   . CYS   A 1 108 ? -17.787 7.710   2.863   1.00 18.36 ? 87  CYS   A CB   1 
ATOM   658  S  SG   . CYS   A 1 108 ? -18.519 6.299   3.738   1.00 20.73 ? 87  CYS   A SG   1 
ATOM   659  N  N    . ASP   A 1 109 ? -20.577 7.444   0.661   1.00 17.54 ? 88  ASP   A N    1 
ATOM   660  C  CA   . ASP   A 1 109 ? -21.965 7.795   0.392   1.00 17.37 ? 88  ASP   A CA   1 
ATOM   661  C  C    . ASP   A 1 109 ? -22.926 7.007   1.274   1.00 17.31 ? 88  ASP   A C    1 
ATOM   662  O  O    . ASP   A 1 109 ? -24.011 7.488   1.580   1.00 16.30 ? 88  ASP   A O    1 
ATOM   663  C  CB   . ASP   A 1 109 ? -22.274 7.546   -1.076  1.00 17.34 ? 88  ASP   A CB   1 
ATOM   664  C  CG   . ASP   A 1 109 ? -21.431 8.399   -2.007  1.00 20.78 ? 88  ASP   A CG   1 
ATOM   665  O  OD1  . ASP   A 1 109 ? -21.866 9.532   -2.290  1.00 23.02 ? 88  ASP   A OD1  1 
ATOM   666  O  OD2  . ASP   A 1 109 ? -20.319 7.963   -2.343  1.00 20.57 ? 88  ASP   A OD2  1 
ATOM   667  N  N    . VAL   A 1 110 ? -22.560 5.758   1.569   1.00 15.94 ? 89  VAL   A N    1 
ATOM   668  C  CA   . VAL   A 1 110 ? -23.440 4.843   2.284   1.00 16.09 ? 89  VAL   A CA   1 
ATOM   669  C  C    . VAL   A 1 110 ? -22.651 4.139   3.384   1.00 16.12 ? 89  VAL   A C    1 
ATOM   670  O  O    . VAL   A 1 110 ? -21.505 3.726   3.170   1.00 15.54 ? 89  VAL   A O    1 
ATOM   671  C  CB   . VAL   A 1 110 ? -24.030 3.820   1.296   1.00 17.40 ? 89  VAL   A CB   1 
ATOM   672  C  CG1  . VAL   A 1 110 ? -24.676 2.635   2.011   1.00 17.38 ? 89  VAL   A CG1  1 
ATOM   673  C  CG2  . VAL   A 1 110 ? -25.005 4.480   0.323   1.00 17.22 ? 89  VAL   A CG2  1 
ATOM   674  N  N    . LEU   A 1 111 ? -23.270 4.034   4.563   1.00 14.71 ? 90  LEU   A N    1 
ATOM   675  C  CA   . LEU   A 1 111 ? -22.762 3.221   5.658   1.00 14.06 ? 90  LEU   A CA   1 
ATOM   676  C  C    . LEU   A 1 111 ? -23.808 2.165   6.000   1.00 13.07 ? 90  LEU   A C    1 
ATOM   677  O  O    . LEU   A 1 111 ? -24.965 2.509   6.257   1.00 13.70 ? 90  LEU   A O    1 
ATOM   678  C  CB   . LEU   A 1 111 ? -22.538 4.140   6.858   1.00 13.81 ? 90  LEU   A CB   1 
ATOM   679  C  CG   . LEU   A 1 111 ? -22.276 3.445   8.197   1.00 14.22 ? 90  LEU   A CG   1 
ATOM   680  C  CD1  . LEU   A 1 111 ? -20.991 2.600   8.162   1.00 15.07 ? 90  LEU   A CD1  1 
ATOM   681  C  CD2  . LEU   A 1 111 ? -22.220 4.462   9.319   1.00 15.22 ? 90  LEU   A CD2  1 
ATOM   682  N  N    . VAL   A 1 112 ? -23.402 0.894   5.987   1.00 13.43 ? 91  VAL   A N    1 
ATOM   683  C  CA   . VAL   A 1 112 ? -24.278 -0.176  6.457   1.00 13.61 ? 91  VAL   A CA   1 
ATOM   684  C  C    . VAL   A 1 112 ? -23.692 -0.776  7.734   1.00 13.73 ? 91  VAL   A C    1 
ATOM   685  O  O    . VAL   A 1 112 ? -22.594 -1.346  7.730   1.00 14.40 ? 91  VAL   A O    1 
ATOM   686  C  CB   . VAL   A 1 112 ? -24.465 -1.273  5.403   1.00 13.98 ? 91  VAL   A CB   1 
ATOM   687  C  CG1  . VAL   A 1 112 ? -25.414 -2.357  5.941   1.00 15.46 ? 91  VAL   A CG1  1 
ATOM   688  C  CG2  . VAL   A 1 112 ? -24.943 -0.693  4.078   1.00 14.83 ? 91  VAL   A CG2  1 
ATOM   689  N  N    . ASN   A 1 113 ? -24.429 -0.608  8.841   1.00 13.13 ? 92  ASN   A N    1 
ATOM   690  C  CA   . ASN   A 1 113 ? -24.020 -1.152  10.128  1.00 13.17 ? 92  ASN   A CA   1 
ATOM   691  C  C    . ASN   A 1 113 ? -24.577 -2.564  10.290  1.00 13.81 ? 92  ASN   A C    1 
ATOM   692  O  O    . ASN   A 1 113 ? -25.737 -2.744  10.690  1.00 14.33 ? 92  ASN   A O    1 
ATOM   693  C  CB   . ASN   A 1 113 ? -24.516 -0.254  11.247  1.00 14.19 ? 92  ASN   A CB   1 
ATOM   694  C  CG   . ASN   A 1 113 ? -23.709 1.016   11.332  1.00 14.82 ? 92  ASN   A CG   1 
ATOM   695  O  OD1  . ASN   A 1 113 ? -22.490 0.953   11.538  1.00 14.31 ? 92  ASN   A OD1  1 
ATOM   696  N  ND2  . ASN   A 1 113 ? -24.369 2.167   11.324  1.00 14.11 ? 92  ASN   A ND2  1 
ATOM   697  N  N    . ASN   A 1 114 ? -23.771 -3.546  9.878   1.00 13.21 ? 93  ASN   A N    1 
ATOM   698  C  CA   . ASN   A 1 114 ? -24.153 -4.948  9.822   1.00 13.29 ? 93  ASN   A CA   1 
ATOM   699  C  C    . ASN   A 1 114 ? -23.462 -5.776  10.909  1.00 14.68 ? 93  ASN   A C    1 
ATOM   700  O  O    . ASN   A 1 114 ? -24.048 -6.751  11.405  1.00 15.59 ? 93  ASN   A O    1 
ATOM   701  C  CB   . ASN   A 1 114 ? -23.932 -5.474  8.405   1.00 13.89 ? 93  ASN   A CB   1 
ATOM   702  C  CG   . ASN   A 1 114 ? -24.039 -6.976  8.320   1.00 13.95 ? 93  ASN   A CG   1 
ATOM   703  O  OD1  . ASN   A 1 114 ? -25.147 -7.507  8.197   1.00 15.13 ? 93  ASN   A OD1  1 
ATOM   704  N  ND2  . ASN   A 1 114 ? -22.909 -7.665  8.393   1.00 14.21 ? 93  ASN   A ND2  1 
ATOM   705  N  N    . ALA   A 1 115 ? -22.195 -5.471  11.225  1.00 13.02 ? 94  ALA   A N    1 
ATOM   706  C  CA   . ALA   A 1 115 ? -21.428 -6.290  12.164  1.00 14.21 ? 94  ALA   A CA   1 
ATOM   707  C  C    . ALA   A 1 115 ? -22.185 -6.462  13.476  1.00 15.50 ? 94  ALA   A C    1 
ATOM   708  O  O    . ALA   A 1 115 ? -22.751 -5.487  13.975  1.00 16.21 ? 94  ALA   A O    1 
ATOM   709  C  CB   . ALA   A 1 115 ? -20.072 -5.672  12.417  1.00 16.15 ? 94  ALA   A CB   1 
ATOM   710  N  N    . SER   A 1 116 ? -22.134 -7.671  14.052  1.00 15.70 ? 95  SER   A N    1 
ATOM   711  C  CA   . SER   A 1 116 ? -22.920 -7.910  15.255  1.00 16.27 ? 95  SER   A CA   1 
ATOM   712  C  C    . SER   A 1 116 ? -22.422 -9.139  16.009  1.00 17.86 ? 95  SER   A C    1 
ATOM   713  O  O    . SER   A 1 116 ? -22.257 -10.197 15.412  1.00 19.03 ? 95  SER   A O    1 
ATOM   714  C  CB   . SER   A 1 116 ? -24.355 -8.119  14.860  1.00 17.37 ? 95  SER   A CB   1 
ATOM   715  O  OG   . SER   A 1 116 ? -25.136 -8.597  15.947  1.00 18.68 ? 95  SER   A OG   1 
ATOM   716  N  N    . ALA   A 1 117 ? -22.212 -8.985  17.323  1.00 16.59 ? 96  ALA   A N    1 
ATOM   717  C  CA   . ALA   A 1 117 ? -22.078 -10.133 18.215  1.00 15.85 ? 96  ALA   A CA   1 
ATOM   718  C  C    . ALA   A 1 117 ? -23.462 -10.626 18.629  1.00 15.85 ? 96  ALA   A C    1 
ATOM   719  O  O    . ALA   A 1 117 ? -24.390 -9.849  18.830  1.00 17.16 ? 96  ALA   A O    1 
ATOM   720  C  CB   . ALA   A 1 117 ? -21.241 -9.765  19.420  1.00 16.91 ? 96  ALA   A CB   1 
ATOM   721  N  N    . PHE   A 1 118 ? -23.588 -11.952 18.753  1.00 15.64 ? 97  PHE   A N    1 
ATOM   722  C  CA   . PHE   A 1 118 ? -24.859 -12.543 19.100  1.00 16.05 ? 97  PHE   A CA   1 
ATOM   723  C  C    . PHE   A 1 118 ? -24.620 -13.841 19.859  1.00 18.39 ? 97  PHE   A C    1 
ATOM   724  O  O    . PHE   A 1 118 ? -24.171 -14.830 19.281  1.00 20.01 ? 97  PHE   A O    1 
ATOM   725  C  CB   . PHE   A 1 118 ? -25.628 -12.790 17.797  1.00 17.55 ? 97  PHE   A CB   1 
ATOM   726  C  CG   . PHE   A 1 118 ? -26.911 -13.598 17.929  1.00 18.45 ? 97  PHE   A CG   1 
ATOM   727  C  CD1  . PHE   A 1 118 ? -28.032 -13.061 18.549  1.00 18.17 ? 97  PHE   A CD1  1 
ATOM   728  C  CD2  . PHE   A 1 118 ? -27.016 -14.869 17.373  1.00 21.20 ? 97  PHE   A CD2  1 
ATOM   729  C  CE1  . PHE   A 1 118 ? -29.225 -13.760 18.635  1.00 20.16 ? 97  PHE   A CE1  1 
ATOM   730  C  CE2  . PHE   A 1 118 ? -28.213 -15.579 17.473  1.00 21.58 ? 97  PHE   A CE2  1 
ATOM   731  C  CZ   . PHE   A 1 118 ? -29.313 -15.029 18.103  1.00 21.05 ? 97  PHE   A CZ   1 
ATOM   732  N  N    . TYR   A 1 119 ? -24.918 -13.809 21.152  1.00 16.64 ? 98  TYR   A N    1 
ATOM   733  C  CA   . TYR   A 1 119 ? -24.760 -14.985 21.988  1.00 16.66 ? 98  TYR   A CA   1 
ATOM   734  C  C    . TYR   A 1 119 ? -25.511 -14.738 23.285  1.00 16.56 ? 98  TYR   A C    1 
ATOM   735  O  O    . TYR   A 1 119 ? -25.765 -13.592 23.657  1.00 15.87 ? 98  TYR   A O    1 
ATOM   736  C  CB   . TYR   A 1 119 ? -23.287 -15.348 22.242  1.00 17.11 ? 98  TYR   A CB   1 
ATOM   737  C  CG   . TYR   A 1 119 ? -22.402 -14.240 22.795  1.00 16.89 ? 98  TYR   A CG   1 
ATOM   738  C  CD1  . TYR   A 1 119 ? -22.419 -13.925 24.151  1.00 18.01 ? 98  TYR   A CD1  1 
ATOM   739  C  CD2  . TYR   A 1 119 ? -21.518 -13.553 21.969  1.00 19.00 ? 98  TYR   A CD2  1 
ATOM   740  C  CE1  . TYR   A 1 119 ? -21.589 -12.947 24.677  1.00 18.36 ? 98  TYR   A CE1  1 
ATOM   741  C  CE2  . TYR   A 1 119 ? -20.694 -12.564 22.481  1.00 18.27 ? 98  TYR   A CE2  1 
ATOM   742  C  CZ   . TYR   A 1 119 ? -20.710 -12.277 23.838  1.00 18.74 ? 98  TYR   A CZ   1 
ATOM   743  O  OH   . TYR   A 1 119 ? -19.888 -11.317 24.376  1.00 19.17 ? 98  TYR   A OH   1 
ATOM   744  N  N    . PRO   A 1 120 ? -25.915 -15.789 24.015  1.00 17.19 ? 99  PRO   A N    1 
ATOM   745  C  CA   . PRO   A 1 120 ? -26.668 -15.590 25.251  1.00 18.06 ? 99  PRO   A CA   1 
ATOM   746  C  C    . PRO   A 1 120 ? -25.830 -15.056 26.411  1.00 16.23 ? 99  PRO   A C    1 
ATOM   747  O  O    . PRO   A 1 120 ? -24.629 -15.335 26.517  1.00 17.93 ? 99  PRO   A O    1 
ATOM   748  C  CB   . PRO   A 1 120 ? -27.246 -16.981 25.536  1.00 19.66 ? 99  PRO   A CB   1 
ATOM   749  C  CG   . PRO   A 1 120 ? -26.248 -17.906 24.893  1.00 19.74 ? 99  PRO   A CG   1 
ATOM   750  C  CD   . PRO   A 1 120 ? -25.708 -17.210 23.667  1.00 18.08 ? 99  PRO   A CD   1 
ATOM   751  N  N    . THR   A 1 121 ? -26.492 -14.251 27.243  1.00 16.63 ? 100 THR   A N    1 
ATOM   752  C  CA   . THR   A 1 121 ? -25.898 -13.680 28.441  1.00 16.29 ? 100 THR   A CA   1 
ATOM   753  C  C    . THR   A 1 121 ? -26.920 -13.852 29.558  1.00 17.69 ? 100 THR   A C    1 
ATOM   754  O  O    . THR   A 1 121 ? -27.654 -12.920 29.885  1.00 17.56 ? 100 THR   A O    1 
ATOM   755  C  CB   . THR   A 1 121 ? -25.542 -12.207 28.214  1.00 17.68 ? 100 THR   A CB   1 
ATOM   756  O  OG1  . THR   A 1 121 ? -26.710 -11.502 27.789  1.00 18.34 ? 100 THR   A OG1  1 
ATOM   757  C  CG2  . THR   A 1 121 ? -24.458 -12.020 27.165  1.00 18.26 ? 100 THR   A CG2  1 
ATOM   758  N  N    . PRO   A 1 122 ? -27.045 -15.067 30.138  1.00 17.82 ? 101 PRO   A N    1 
ATOM   759  C  CA   . PRO   A 1 122 ? -28.060 -15.317 31.169  1.00 17.22 ? 101 PRO   A CA   1 
ATOM   760  C  C    . PRO   A 1 122 ? -27.914 -14.383 32.368  1.00 17.38 ? 101 PRO   A C    1 
ATOM   761  O  O    . PRO   A 1 122 ? -26.800 -14.023 32.768  1.00 19.10 ? 101 PRO   A O    1 
ATOM   762  C  CB   . PRO   A 1 122 ? -27.890 -16.805 31.580  1.00 19.19 ? 101 PRO   A CB   1 
ATOM   763  C  CG   . PRO   A 1 122 ? -26.934 -17.372 30.549  1.00 21.68 ? 101 PRO   A CG   1 
ATOM   764  C  CD   . PRO   A 1 122 ? -26.217 -16.241 29.829  1.00 19.50 ? 101 PRO   A CD   1 
ATOM   765  N  N    . LEU   A 1 123 ? -29.064 -13.997 32.938  1.00 18.54 ? 102 LEU   A N    1 
ATOM   766  C  CA   . LEU   A 1 123 ? -29.069 -13.113 34.093  1.00 20.19 ? 102 LEU   A CA   1 
ATOM   767  C  C    . LEU   A 1 123 ? -28.676 -13.869 35.357  1.00 23.47 ? 102 LEU   A C    1 
ATOM   768  O  O    . LEU   A 1 123 ? -28.130 -13.257 36.269  1.00 24.34 ? 102 LEU   A O    1 
ATOM   769  C  CB   . LEU   A 1 123 ? -30.444 -12.468 34.262  1.00 19.40 ? 102 LEU   A CB   1 
ATOM   770  C  CG   . LEU   A 1 123 ? -30.834 -11.451 33.185  1.00 18.59 ? 102 LEU   A CG   1 
ATOM   771  C  CD1  . LEU   A 1 123 ? -32.284 -11.019 33.334  1.00 19.57 ? 102 LEU   A CD1  1 
ATOM   772  C  CD2  . LEU   A 1 123 ? -29.938 -10.227 33.291  1.00 21.55 ? 102 LEU   A CD2  1 
ATOM   773  N  N    . VAL   A 1 124 ? -29.029 -15.160 35.416  1.00 25.74 ? 103 VAL   A N    1 
ATOM   774  C  CA   . VAL   A 1 124 ? -28.819 -15.993 36.597  1.00 30.02 ? 103 VAL   A CA   1 
ATOM   775  C  C    . VAL   A 1 124 ? -27.862 -17.130 36.243  1.00 33.46 ? 103 VAL   A C    1 
ATOM   776  O  O    . VAL   A 1 124 ? -27.971 -17.725 35.173  1.00 33.86 ? 103 VAL   A O    1 
ATOM   777  C  CB   . VAL   A 1 124 ? -30.155 -16.525 37.160  1.00 31.55 ? 103 VAL   A CB   1 
ATOM   778  C  CG1  . VAL   A 1 124 ? -29.960 -17.546 38.281  1.00 34.14 ? 103 VAL   A CG1  1 
ATOM   779  C  CG2  . VAL   A 1 124 ? -31.059 -15.393 37.635  1.00 32.46 ? 103 VAL   A CG2  1 
ATOM   780  N  N    . GLN   A 1 125 ? -26.927 -17.416 37.159  0.70 34.72 ? 104 GLN   A N    1 
ATOM   781  C  CA   . GLN   A 1 125 ? -25.981 -18.508 36.992  0.70 38.46 ? 104 GLN   A CA   1 
ATOM   782  C  C    . GLN   A 1 125 ? -26.328 -19.627 37.987  0.70 40.89 ? 104 GLN   A C    1 
ATOM   783  O  O    . GLN   A 1 125 ? -27.195 -20.454 37.627  0.70 45.84 ? 104 GLN   A O    1 
ATOM   784  C  CB   . GLN   A 1 125 ? -24.543 -18.025 37.186  0.70 37.52 ? 104 GLN   A CB   1 
ATOM   785  N  N    . GLY   A 1 134 ? -14.836 -18.943 29.045  0.70 43.30 ? 113 GLY   A N    1 
ATOM   786  C  CA   . GLY   A 1 134 ? -16.007 -18.143 29.455  0.70 40.97 ? 113 GLY   A CA   1 
ATOM   787  C  C    . GLY   A 1 134 ? -15.647 -16.666 29.598  0.70 38.33 ? 113 GLY   A C    1 
ATOM   788  O  O    . GLY   A 1 134 ? -14.746 -16.315 30.355  0.70 41.16 ? 113 GLY   A O    1 
ATOM   789  N  N    . LYS   A 1 135 ? -16.374 -15.812 28.867  1.00 38.00 ? 114 LYS   A N    1 
ATOM   790  C  CA   . LYS   A 1 135 ? -16.154 -14.373 28.869  1.00 31.22 ? 114 LYS   A CA   1 
ATOM   791  C  C    . LYS   A 1 135 ? -16.654 -13.768 30.174  1.00 27.46 ? 114 LYS   A C    1 
ATOM   792  O  O    . LYS   A 1 135 ? -17.672 -14.201 30.709  1.00 26.75 ? 114 LYS   A O    1 
ATOM   793  C  CB   . LYS   A 1 135 ? -16.964 -13.726 27.743  1.00 32.40 ? 114 LYS   A CB   1 
ATOM   794  C  CG   . LYS   A 1 135 ? -16.536 -14.203 26.371  1.00 35.04 ? 114 LYS   A CG   1 
ATOM   795  C  CD   . LYS   A 1 135 ? -17.329 -13.653 25.200  1.00 37.31 ? 114 LYS   A CD   1 
ATOM   796  C  CE   . LYS   A 1 135 ? -16.484 -13.915 24.003  1.00 35.58 ? 114 LYS   A CE   1 
ATOM   797  N  NZ   . LYS   A 1 135 ? -17.250 -13.797 22.769  1.00 37.82 ? 114 LYS   A NZ   1 
ATOM   798  N  N    . THR   A 1 136 ? -15.945 -12.740 30.660  1.00 23.59 ? 115 THR   A N    1 
ATOM   799  C  CA   . THR   A 1 136 ? -16.407 -12.002 31.820  1.00 22.40 ? 115 THR   A CA   1 
ATOM   800  C  C    . THR   A 1 136 ? -17.643 -11.207 31.399  1.00 20.27 ? 115 THR   A C    1 
ATOM   801  O  O    . THR   A 1 136 ? -17.860 -11.002 30.203  1.00 19.66 ? 115 THR   A O    1 
ATOM   802  C  CB   . THR   A 1 136 ? -15.332 -11.048 32.330  1.00 22.71 ? 115 THR   A CB   1 
ATOM   803  O  OG1  . THR   A 1 136 ? -15.076 -10.128 31.270  1.00 23.55 ? 115 THR   A OG1  1 
ATOM   804  C  CG2  . THR   A 1 136 ? -14.054 -11.770 32.727  1.00 24.40 ? 115 THR   A CG2  1 
ATOM   805  N  N    . VAL   A 1 137 ? -18.422 -10.764 32.395  1.00 21.02 ? 116 VAL   A N    1 
ATOM   806  C  CA   . VAL   A 1 137 ? -19.592 -9.943  32.128  1.00 20.14 ? 116 VAL   A CA   1 
ATOM   807  C  C    . VAL   A 1 137 ? -19.143 -8.626  31.488  1.00 20.05 ? 116 VAL   A C    1 
ATOM   808  O  O    . VAL   A 1 137 ? -19.834 -8.117  30.613  1.00 17.26 ? 116 VAL   A O    1 
ATOM   809  C  CB   . VAL   A 1 137 ? -20.519 -9.727  33.344  1.00 22.56 ? 116 VAL   A CB   1 
ATOM   810  C  CG1  . VAL   A 1 137 ? -19.881 -8.846  34.407  1.00 26.29 ? 116 VAL   A CG1  1 
ATOM   811  C  CG2  . VAL   A 1 137 ? -21.879 -9.155  32.952  1.00 23.35 ? 116 VAL   A CG2  1 
ATOM   812  N  N    . GLU   A 1 138 ? -17.957 -8.132  31.860  1.00 20.66 ? 117 GLU   A N    1 
ATOM   813  C  CA   . GLU   A 1 138 ? -17.417 -6.904  31.286  1.00 21.62 ? 117 GLU   A CA   1 
ATOM   814  C  C    . GLU   A 1 138 ? -17.248 -7.065  29.773  1.00 19.39 ? 117 GLU   A C    1 
ATOM   815  O  O    . GLU   A 1 138 ? -17.570 -6.160  29.006  1.00 18.07 ? 117 GLU   A O    1 
ATOM   816  C  CB   . GLU   A 1 138 ? -16.025 -6.539  31.827  1.00 23.93 ? 117 GLU   A CB   1 
ATOM   817  C  CG   . GLU   A 1 138 ? -15.997 -6.139  33.297  1.00 30.68 ? 117 GLU   A CG   1 
ATOM   818  C  CD   . GLU   A 1 138 ? -16.148 -7.225  34.354  1.00 33.67 ? 117 GLU   A CD   1 
ATOM   819  O  OE1  . GLU   A 1 138 ? -16.223 -8.426  34.023  1.00 31.09 ? 117 GLU   A OE1  1 
ATOM   820  O  OE2  . GLU   A 1 138 ? -16.191 -6.842  35.546  1.00 39.49 ? 117 GLU   A OE2  1 
ATOM   821  N  N    . THR   A 1 139 ? -16.701 -8.215  29.362  1.00 18.12 ? 118 THR   A N    1 
ATOM   822  C  CA   . THR   A 1 139 ? -16.457 -8.529  27.962  1.00 19.24 ? 118 THR   A CA   1 
ATOM   823  C  C    . THR   A 1 139 ? -17.797 -8.640  27.233  1.00 17.34 ? 118 THR   A C    1 
ATOM   824  O  O    . THR   A 1 139 ? -17.931 -8.196  26.080  1.00 18.10 ? 118 THR   A O    1 
ATOM   825  C  CB   . THR   A 1 139 ? -15.653 -9.829  27.840  1.00 21.53 ? 118 THR   A CB   1 
ATOM   826  O  OG1  . THR   A 1 139 ? -14.354 -9.476  28.317  1.00 23.07 ? 118 THR   A OG1  1 
ATOM   827  C  CG2  . THR   A 1 139 ? -15.551 -10.323 26.406  1.00 21.94 ? 118 THR   A CG2  1 
ATOM   828  N  N    . GLN   A 1 140 ? -18.761 -9.319  27.868  1.00 15.99 ? 119 GLN   A N    1 
ATOM   829  C  CA   A GLN   A 1 140 ? -20.090 -9.552  27.304  0.70 16.37 ? 119 GLN   A CA   1 
ATOM   830  C  CA   B GLN   A 1 140 ? -20.015 -9.536  27.170  0.30 15.60 ? 119 GLN   A CA   1 
ATOM   831  C  C    . GLN   A 1 140 ? -20.723 -8.207  26.938  1.00 14.57 ? 119 GLN   A C    1 
ATOM   832  O  O    . GLN   A 1 140 ? -21.242 -8.010  25.837  1.00 14.63 ? 119 GLN   A O    1 
ATOM   833  C  CB   A GLN   A 1 140 ? -20.949 -10.279 28.344  0.70 17.31 ? 119 GLN   A CB   1 
ATOM   834  C  CB   B GLN   A 1 140 ? -20.916 -10.549 27.855  0.30 15.85 ? 119 GLN   A CB   1 
ATOM   835  C  CG   A GLN   A 1 140 ? -20.599 -11.754 28.542  0.70 20.42 ? 119 GLN   A CG   1 
ATOM   836  C  CG   B GLN   A 1 140 ? -20.230 -11.884 28.098  0.30 16.52 ? 119 GLN   A CG   1 
ATOM   837  C  CD   A GLN   A 1 140 ? -21.353 -12.378 29.693  0.70 22.75 ? 119 GLN   A CD   1 
ATOM   838  C  CD   B GLN   A 1 140 ? -21.077 -12.747 28.996  0.30 16.62 ? 119 GLN   A CD   1 
ATOM   839  O  OE1  A GLN   A 1 140 ? -22.566 -12.186 29.853  0.70 22.71 ? 119 GLN   A OE1  1 
ATOM   840  O  OE1  B GLN   A 1 140 ? -21.589 -12.279 30.020  0.30 18.65 ? 119 GLN   A OE1  1 
ATOM   841  N  NE2  A GLN   A 1 140 ? -20.630 -13.096 30.540  0.70 22.32 ? 119 GLN   A NE2  1 
ATOM   842  N  NE2  B GLN   A 1 140 ? -21.263 -13.994 28.596  0.30 16.94 ? 119 GLN   A NE2  1 
ATOM   843  N  N    . VAL   A 1 141 ? -20.691 -7.291  27.914  1.00 14.95 ? 120 VAL   A N    1 
ATOM   844  C  CA   . VAL   A 1 141 ? -21.248 -5.966  27.700  1.00 14.91 ? 120 VAL   A CA   1 
ATOM   845  C  C    . VAL   A 1 141 ? -20.499 -5.277  26.562  1.00 14.72 ? 120 VAL   A C    1 
ATOM   846  O  O    . VAL   A 1 141 ? -21.113 -4.730  25.631  1.00 14.31 ? 120 VAL   A O    1 
ATOM   847  C  CB   . VAL   A 1 141 ? -21.133 -5.148  28.998  1.00 13.88 ? 120 VAL   A CB   1 
ATOM   848  C  CG1  . VAL   A 1 141 ? -21.404 -3.664  28.744  1.00 14.94 ? 120 VAL   A CG1  1 
ATOM   849  C  CG2  . VAL   A 1 141 ? -22.062 -5.685  30.090  1.00 14.17 ? 120 VAL   A CG2  1 
ATOM   850  N  N    . ALA   A 1 142 ? -19.159 -5.329  26.615  1.00 15.04 ? 121 ALA   A N    1 
ATOM   851  C  CA   . ALA   A 1 142 ? -18.379 -4.606  25.627  1.00 13.99 ? 121 ALA   A CA   1 
ATOM   852  C  C    . ALA   A 1 142 ? -18.646 -5.106  24.204  1.00 14.07 ? 121 ALA   A C    1 
ATOM   853  O  O    . ALA   A 1 142 ? -18.806 -4.317  23.282  1.00 14.17 ? 121 ALA   A O    1 
ATOM   854  C  CB   . ALA   A 1 142 ? -16.904 -4.670  25.978  1.00 13.74 ? 121 ALA   A CB   1 
ATOM   855  N  N    . GLU   A 1 143 ? -18.711 -6.431  24.025  1.00 13.76 ? 122 GLU   A N    1 
ATOM   856  C  CA   . GLU   A 1 143 ? -18.934 -6.998  22.703  1.00 15.12 ? 122 GLU   A CA   1 
ATOM   857  C  C    . GLU   A 1 143 ? -20.363 -6.738  22.215  1.00 14.71 ? 122 GLU   A C    1 
ATOM   858  O  O    . GLU   A 1 143 ? -20.570 -6.308  21.072  1.00 14.65 ? 122 GLU   A O    1 
ATOM   859  C  CB   . GLU   A 1 143 ? -18.619 -8.498  22.714  1.00 16.34 ? 122 GLU   A CB   1 
ATOM   860  C  CG   . GLU   A 1 143 ? -17.118 -8.740  22.894  1.00 18.02 ? 122 GLU   A CG   1 
ATOM   861  C  CD   . GLU   A 1 143 ? -16.719 -10.199 22.818  1.00 22.40 ? 122 GLU   A CD   1 
ATOM   862  O  OE1  . GLU   A 1 143 ? -17.623 -11.041 22.806  1.00 22.69 ? 122 GLU   A OE1  1 
ATOM   863  O  OE2  . GLU   A 1 143 ? -15.490 -10.471 22.799  1.00 24.53 ? 122 GLU   A OE2  1 
ATOM   864  N  N    . LEU   A 1 144 ? -21.363 -7.019  23.067  1.00 14.31 ? 123 LEU   A N    1 
ATOM   865  C  CA   . LEU   A 1 144 ? -22.743 -7.037  22.591  1.00 14.30 ? 123 LEU   A CA   1 
ATOM   866  C  C    . LEU   A 1 144 ? -23.276 -5.624  22.442  1.00 14.04 ? 123 LEU   A C    1 
ATOM   867  O  O    . LEU   A 1 144 ? -23.902 -5.316  21.425  1.00 14.28 ? 123 LEU   A O    1 
ATOM   868  C  CB   . LEU   A 1 144 ? -23.647 -7.917  23.453  1.00 14.58 ? 123 LEU   A CB   1 
ATOM   869  C  CG   . LEU   A 1 144 ? -23.367 -9.421  23.318  1.00 16.43 ? 123 LEU   A CG   1 
ATOM   870  C  CD1  . LEU   A 1 144 ? -23.891 -10.139 24.539  1.00 18.89 ? 123 LEU   A CD1  1 
ATOM   871  C  CD2  . LEU   A 1 144 ? -24.065 -9.954  22.062  1.00 17.63 ? 123 LEU   A CD2  1 
ATOM   872  N  N    . ILE   A 1 145 ? -22.943 -4.753  23.389  1.00 14.35 ? 124 ILE   A N    1 
ATOM   873  C  CA   . ILE   A 1 145 ? -23.361 -3.363  23.264  1.00 14.20 ? 124 ILE   A CA   1 
ATOM   874  C  C    . ILE   A 1 145 ? -22.456 -2.579  22.311  1.00 14.71 ? 124 ILE   A C    1 
ATOM   875  O  O    . ILE   A 1 145 ? -22.943 -1.726  21.566  1.00 14.74 ? 124 ILE   A O    1 
ATOM   876  C  CB   . ILE   A 1 145 ? -23.463 -2.712  24.649  1.00 13.99 ? 124 ILE   A CB   1 
ATOM   877  C  CG1  . ILE   A 1 145 ? -24.361 -3.540  25.607  1.00 15.92 ? 124 ILE   A CG1  1 
ATOM   878  C  CG2  . ILE   A 1 145 ? -23.939 -1.259  24.495  1.00 15.03 ? 124 ILE   A CG2  1 
ATOM   879  C  CD1  . ILE   A 1 145 ? -25.791 -3.758  25.138  1.00 16.82 ? 124 ILE   A CD1  1 
ATOM   880  N  N    . GLY   A 1 146 ? -21.160 -2.929  22.269  1.00 14.52 ? 125 GLY   A N    1 
ATOM   881  C  CA   . GLY   A 1 146 ? -20.254 -2.271  21.344  1.00 14.69 ? 125 GLY   A CA   1 
ATOM   882  C  C    . GLY   A 1 146 ? -20.649 -2.532  19.891  1.00 14.03 ? 125 GLY   A C    1 
ATOM   883  O  O    . GLY   A 1 146 ? -20.834 -1.616  19.099  1.00 14.77 ? 125 GLY   A O    1 
ATOM   884  N  N    . THR   A 1 147 ? -20.791 -3.803  19.513  1.00 13.10 ? 126 THR   A N    1 
ATOM   885  C  CA   . THR   A 1 147 ? -20.986 -4.079  18.101  1.00 14.10 ? 126 THR   A CA   1 
ATOM   886  C  C    . THR   A 1 147 ? -22.373 -3.633  17.653  1.00 14.65 ? 126 THR   A C    1 
ATOM   887  O  O    . THR   A 1 147 ? -22.531 -3.138  16.539  1.00 15.32 ? 126 THR   A O    1 
ATOM   888  C  CB   . THR   A 1 147 ? -20.774 -5.564  17.796  1.00 13.67 ? 126 THR   A CB   1 
ATOM   889  O  OG1  . THR   A 1 147 ? -21.718 -6.323  18.541  1.00 16.34 ? 126 THR   A OG1  1 
ATOM   890  C  CG2  . THR   A 1 147 ? -19.364 -6.020  18.125  1.00 15.50 ? 126 THR   A CG2  1 
ATOM   891  N  N    . ASN   A 1 148 ? -23.385 -3.842  18.513  1.00 15.36 ? 127 ASN   A N    1 
ATOM   892  C  CA   . ASN   A 1 148 ? -24.749 -3.689  18.038  1.00 14.88 ? 127 ASN   A CA   1 
ATOM   893  C  C    . ASN   A 1 148 ? -25.236 -2.243  18.140  1.00 14.76 ? 127 ASN   A C    1 
ATOM   894  O  O    . ASN   A 1 148 ? -26.241 -1.910  17.497  1.00 16.22 ? 127 ASN   A O    1 
ATOM   895  C  CB   . ASN   A 1 148 ? -25.700 -4.609  18.789  1.00 15.27 ? 127 ASN   A CB   1 
ATOM   896  C  CG   . ASN   A 1 148 ? -25.518 -6.042  18.351  1.00 15.78 ? 127 ASN   A CG   1 
ATOM   897  O  OD1  . ASN   A 1 148 ? -25.853 -6.353  17.205  1.00 17.45 ? 127 ASN   A OD1  1 
ATOM   898  N  ND2  . ASN   A 1 148 ? -25.040 -6.908  19.229  1.00 15.52 ? 127 ASN   A ND2  1 
ATOM   899  N  N    . ALA   A 1 149 ? -24.565 -1.426  18.963  1.00 14.37 ? 128 ALA   A N    1 
ATOM   900  C  CA   . ALA   A 1 149 ? -25.099 -0.098  19.267  1.00 13.55 ? 128 ALA   A CA   1 
ATOM   901  C  C    . ALA   A 1 149 ? -24.032 0.996   19.261  1.00 13.36 ? 128 ALA   A C    1 
ATOM   902  O  O    . ALA   A 1 149 ? -24.170 1.988   18.544  1.00 14.07 ? 128 ALA   A O    1 
ATOM   903  C  CB   . ALA   A 1 149 ? -25.886 -0.111  20.571  1.00 15.70 ? 128 ALA   A CB   1 
ATOM   904  N  N    . ILE   A 1 150 ? -22.968 0.818   20.056  1.00 13.74 ? 129 ILE   A N    1 
ATOM   905  C  CA   . ILE   A 1 150 ? -22.041 1.930   20.218  1.00 13.25 ? 129 ILE   A CA   1 
ATOM   906  C  C    . ILE   A 1 150 ? -21.214 2.131   18.955  1.00 13.08 ? 129 ILE   A C    1 
ATOM   907  O  O    . ILE   A 1 150 ? -21.043 3.271   18.519  1.00 12.87 ? 129 ILE   A O    1 
ATOM   908  C  CB   . ILE   A 1 150 ? -21.157 1.735   21.463  1.00 14.05 ? 129 ILE   A CB   1 
ATOM   909  C  CG1  . ILE   A 1 150 ? -22.053 1.625   22.730  1.00 15.36 ? 129 ILE   A CG1  1 
ATOM   910  C  CG2  . ILE   A 1 150 ? -20.148 2.885   21.582  1.00 14.48 ? 129 ILE   A CG2  1 
ATOM   911  C  CD1  . ILE   A 1 150 ? -21.326 1.250   24.015  1.00 16.97 ? 129 ILE   A CD1  1 
ATOM   912  N  N    . ALA   A 1 151 ? -20.727 1.040   18.360  1.00 12.94 ? 130 ALA   A N    1 
ATOM   913  C  CA   . ALA   A 1 151 ? -19.979 1.203   17.113  1.00 13.66 ? 130 ALA   A CA   1 
ATOM   914  C  C    . ALA   A 1 151 ? -20.866 1.845   16.040  1.00 13.17 ? 130 ALA   A C    1 
ATOM   915  O  O    . ALA   A 1 151 ? -20.434 2.784   15.365  1.00 13.72 ? 130 ALA   A O    1 
ATOM   916  C  CB   . ALA   A 1 151 ? -19.314 -0.092  16.644  1.00 13.51 ? 130 ALA   A CB   1 
ATOM   917  N  N    . PRO   A 1 152 ? -22.136 1.402   15.822  1.00 13.20 ? 131 PRO   A N    1 
ATOM   918  C  CA   . PRO   A 1 152 ? -22.989 2.121   14.877  1.00 13.22 ? 131 PRO   A CA   1 
ATOM   919  C  C    . PRO   A 1 152 ? -23.110 3.620   15.150  1.00 13.00 ? 131 PRO   A C    1 
ATOM   920  O  O    . PRO   A 1 152 ? -23.097 4.422   14.217  1.00 13.67 ? 131 PRO   A O    1 
ATOM   921  C  CB   . PRO   A 1 152 ? -24.321 1.361   15.050  1.00 12.02 ? 131 PRO   A CB   1 
ATOM   922  C  CG   . PRO   A 1 152 ? -23.873 -0.084  15.249  1.00 13.06 ? 131 PRO   A CG   1 
ATOM   923  C  CD   . PRO   A 1 152 ? -22.692 0.083   16.215  1.00 13.78 ? 131 PRO   A CD   1 
ATOM   924  N  N    . PHE   A 1 153 ? -23.188 3.984   16.432  1.00 12.71 ? 132 PHE   A N    1 
ATOM   925  C  CA   . PHE   A 1 153 ? -23.289 5.399   16.789  1.00 13.50 ? 132 PHE   A CA   1 
ATOM   926  C  C    . PHE   A 1 153 ? -22.009 6.127   16.382  1.00 14.16 ? 132 PHE   A C    1 
ATOM   927  O  O    . PHE   A 1 153 ? -22.075 7.215   15.796  1.00 13.35 ? 132 PHE   A O    1 
ATOM   928  C  CB   . PHE   A 1 153 ? -23.599 5.516   18.293  1.00 14.26 ? 132 PHE   A CB   1 
ATOM   929  C  CG   . PHE   A 1 153 ? -23.295 6.896   18.866  1.00 14.74 ? 132 PHE   A CG   1 
ATOM   930  C  CD1  . PHE   A 1 153 ? -24.191 7.949   18.738  1.00 15.16 ? 132 PHE   A CD1  1 
ATOM   931  C  CD2  . PHE   A 1 153 ? -22.091 7.114   19.533  1.00 15.58 ? 132 PHE   A CD2  1 
ATOM   932  C  CE1  . PHE   A 1 153 ? -23.875 9.216   19.222  1.00 15.99 ? 132 PHE   A CE1  1 
ATOM   933  C  CE2  . PHE   A 1 153 ? -21.789 8.369   20.042  1.00 16.28 ? 132 PHE   A CE2  1 
ATOM   934  C  CZ   . PHE   A 1 153 ? -22.672 9.414   19.887  1.00 16.84 ? 132 PHE   A CZ   1 
ATOM   935  N  N    . LEU   A 1 154 ? -20.854 5.554   16.732  1.00 14.57 ? 133 LEU   A N    1 
ATOM   936  C  CA   . LEU   A 1 154 ? -19.585 6.217   16.442  1.00 13.69 ? 133 LEU   A CA   1 
ATOM   937  C  C    . LEU   A 1 154 ? -19.322 6.271   14.937  1.00 14.06 ? 133 LEU   A C    1 
ATOM   938  O  O    . LEU   A 1 154 ? -18.805 7.270   14.434  1.00 14.87 ? 133 LEU   A O    1 
ATOM   939  C  CB   . LEU   A 1 154 ? -18.467 5.517   17.213  1.00 14.91 ? 133 LEU   A CB   1 
ATOM   940  C  CG   . LEU   A 1 154 ? -18.553 5.634   18.742  1.00 14.08 ? 133 LEU   A CG   1 
ATOM   941  C  CD1  . LEU   A 1 154 ? -17.643 4.604   19.405  1.00 14.68 ? 133 LEU   A CD1  1 
ATOM   942  C  CD2  . LEU   A 1 154 ? -18.234 7.053   19.177  1.00 16.47 ? 133 LEU   A CD2  1 
ATOM   943  N  N    . LEU   A 1 155 ? -19.652 5.193   14.214  1.00 13.32 ? 134 LEU   A N    1 
ATOM   944  C  CA   . LEU   A 1 155 ? -19.559 5.202   12.760  1.00 13.95 ? 134 LEU   A CA   1 
ATOM   945  C  C    . LEU   A 1 155 ? -20.463 6.280   12.161  1.00 14.48 ? 134 LEU   A C    1 
ATOM   946  O  O    . LEU   A 1 155 ? -20.091 6.944   11.190  1.00 14.54 ? 134 LEU   A O    1 
ATOM   947  C  CB   . LEU   A 1 155 ? -19.855 3.810   12.193  1.00 13.64 ? 134 LEU   A CB   1 
ATOM   948  C  CG   . LEU   A 1 155 ? -18.751 2.794   12.473  1.00 13.54 ? 134 LEU   A CG   1 
ATOM   949  C  CD1  . LEU   A 1 155 ? -19.274 1.382   12.352  1.00 13.17 ? 134 LEU   A CD1  1 
ATOM   950  C  CD2  . LEU   A 1 155 ? -17.555 2.996   11.526  1.00 14.64 ? 134 LEU   A CD2  1 
ATOM   951  N  N    . THR   A 1 156 ? -21.659 6.434   12.743  1.00 13.98 ? 135 THR   A N    1 
ATOM   952  C  CA   . THR   A 1 156 ? -22.595 7.446   12.273  1.00 13.48 ? 135 THR   A CA   1 
ATOM   953  C  C    . THR   A 1 156 ? -22.000 8.840   12.488  1.00 14.53 ? 135 THR   A C    1 
ATOM   954  O  O    . THR   A 1 156 ? -22.051 9.681   11.590  1.00 15.04 ? 135 THR   A O    1 
ATOM   955  C  CB   . THR   A 1 156 ? -23.937 7.289   12.993  1.00 13.83 ? 135 THR   A CB   1 
ATOM   956  O  OG1  . THR   A 1 156 ? -24.472 6.030   12.592  1.00 13.98 ? 135 THR   A OG1  1 
ATOM   957  C  CG2  . THR   A 1 156 ? -24.940 8.362   12.605  1.00 13.93 ? 135 THR   A CG2  1 
ATOM   958  N  N    . MET   A 1 157 ? -21.408 9.078   13.662  1.00 14.38 ? 136 MET   A N    1 
ATOM   959  C  CA   A MET   A 1 157 ? -20.743 10.349  13.934  0.70 15.86 ? 136 MET   A CA   1 
ATOM   960  C  CA   B MET   A 1 157 ? -20.757 10.353  13.922  0.30 15.56 ? 136 MET   A CA   1 
ATOM   961  C  C    . MET   A 1 157 ? -19.655 10.610  12.891  1.00 15.61 ? 136 MET   A C    1 
ATOM   962  O  O    . MET   A 1 157 ? -19.584 11.697  12.319  1.00 16.02 ? 136 MET   A O    1 
ATOM   963  C  CB   A MET   A 1 157 ? -20.042 10.332  15.294  0.70 16.37 ? 136 MET   A CB   1 
ATOM   964  C  CB   B MET   A 1 157 ? -20.176 10.388  15.338  0.30 15.97 ? 136 MET   A CB   1 
ATOM   965  C  CG   A MET   A 1 157 ? -20.951 10.402  16.502  0.70 17.60 ? 136 MET   A CG   1 
ATOM   966  C  CG   B MET   A 1 157 ? -19.681 11.755  15.756  0.30 16.89 ? 136 MET   A CG   1 
ATOM   967  S  SD   A MET   A 1 157 ? -19.982 10.671  18.001  0.70 22.26 ? 136 MET   A SD   1 
ATOM   968  S  SD   B MET   A 1 157 ? -18.969 11.729  17.411  0.30 18.85 ? 136 MET   A SD   1 
ATOM   969  C  CE   A MET   A 1 157 ? -19.768 12.456  17.986  0.70 20.13 ? 136 MET   A CE   1 
ATOM   970  C  CE   B MET   A 1 157 ? -20.111 10.659  18.295  0.30 18.27 ? 136 MET   A CE   1 
ATOM   971  N  N    . SER   A 1 158 ? -18.775 9.629   12.673  1.00 15.88 ? 137 SER   A N    1 
ATOM   972  C  CA   . SER   A 1 158 ? -17.647 9.820   11.777  1.00 15.69 ? 137 SER   A CA   1 
ATOM   973  C  C    . SER   A 1 158 ? -18.129 10.045  10.342  1.00 17.05 ? 137 SER   A C    1 
ATOM   974  O  O    . SER   A 1 158 ? -17.626 10.915  9.635   1.00 17.14 ? 137 SER   A O    1 
ATOM   975  C  CB   . SER   A 1 158 ? -16.676 8.667   11.882  1.00 16.68 ? 137 SER   A CB   1 
ATOM   976  O  OG   . SER   A 1 158 ? -16.025 8.734   13.145  1.00 19.28 ? 137 SER   A OG   1 
ATOM   977  N  N    . PHE   A 1 159 ? -19.146 9.283   9.908   1.00 15.72 ? 138 PHE   A N    1 
ATOM   978  C  CA   . PHE   A 1 159 ? -19.712 9.442   8.576   1.00 14.99 ? 138 PHE   A CA   1 
ATOM   979  C  C    . PHE   A 1 159 ? -20.242 10.863  8.389   1.00 16.89 ? 138 PHE   A C    1 
ATOM   980  O  O    . PHE   A 1 159 ? -19.967 11.500  7.373   1.00 18.70 ? 138 PHE   A O    1 
ATOM   981  C  CB   . PHE   A 1 159 ? -20.835 8.401   8.438   1.00 14.76 ? 138 PHE   A CB   1 
ATOM   982  C  CG   . PHE   A 1 159 ? -21.559 8.452   7.100   1.00 14.64 ? 138 PHE   A CG   1 
ATOM   983  C  CD1  . PHE   A 1 159 ? -21.144 7.655   6.042   1.00 14.98 ? 138 PHE   A CD1  1 
ATOM   984  C  CD2  . PHE   A 1 159 ? -22.690 9.248   6.920   1.00 16.23 ? 138 PHE   A CD2  1 
ATOM   985  C  CE1  . PHE   A 1 159 ? -21.806 7.691   4.814   1.00 15.82 ? 138 PHE   A CE1  1 
ATOM   986  C  CE2  . PHE   A 1 159 ? -23.342 9.291   5.692   1.00 16.70 ? 138 PHE   A CE2  1 
ATOM   987  C  CZ   . PHE   A 1 159 ? -22.915 8.505   4.652   1.00 16.61 ? 138 PHE   A CZ   1 
ATOM   988  N  N    . ALA   A 1 160 ? -21.028 11.340  9.357   1.00 16.55 ? 139 ALA   A N    1 
ATOM   989  C  CA   . ALA   A 1 160 ? -21.644 12.659  9.283   1.00 17.44 ? 139 ALA   A CA   1 
ATOM   990  C  C    . ALA   A 1 160 ? -20.588 13.765  9.279   1.00 18.62 ? 139 ALA   A C    1 
ATOM   991  O  O    . ALA   A 1 160 ? -20.707 14.722  8.514   1.00 21.98 ? 139 ALA   A O    1 
ATOM   992  C  CB   . ALA   A 1 160 ? -22.634 12.839  10.424  1.00 17.57 ? 139 ALA   A CB   1 
ATOM   993  N  N    . GLN   A 1 161 ? -19.573 13.629  10.140  1.00 19.56 ? 140 GLN   A N    1 
ATOM   994  C  CA   A GLN   A 1 161 ? -18.583 14.688  10.274  0.70 21.03 ? 140 GLN   A CA   1 
ATOM   995  C  CA   B GLN   A 1 161 ? -18.510 14.616  10.310  0.30 20.76 ? 140 GLN   A CA   1 
ATOM   996  C  C    . GLN   A 1 161 ? -17.775 14.838  8.988   1.00 22.62 ? 140 GLN   A C    1 
ATOM   997  O  O    . GLN   A 1 161 ? -17.341 15.946  8.675   1.00 23.68 ? 140 GLN   A O    1 
ATOM   998  C  CB   A GLN   A 1 161 ? -17.755 14.479  11.537  0.70 23.72 ? 140 GLN   A CB   1 
ATOM   999  C  CB   B GLN   A 1 161 ? -17.500 14.124  11.350  0.30 21.04 ? 140 GLN   A CB   1 
ATOM   1000 C  CG   A GLN   A 1 161 ? -18.532 14.854  12.791  0.70 26.52 ? 140 GLN   A CG   1 
ATOM   1001 C  CG   B GLN   A 1 161 ? -16.454 15.162  11.748  0.30 21.79 ? 140 GLN   A CG   1 
ATOM   1002 C  CD   A GLN   A 1 161 ? -17.888 14.346  14.059  0.70 31.11 ? 140 GLN   A CD   1 
ATOM   1003 C  CD   B GLN   A 1 161 ? -17.033 16.307  12.547  0.30 23.03 ? 140 GLN   A CD   1 
ATOM   1004 O  OE1  A GLN   A 1 161 ? -18.549 14.171  15.088  0.70 28.30 ? 140 GLN   A OE1  1 
ATOM   1005 O  OE1  B GLN   A 1 161 ? -17.663 16.107  13.593  0.30 24.64 ? 140 GLN   A OE1  1 
ATOM   1006 N  NE2  A GLN   A 1 161 ? -16.595 14.062  13.979  0.70 32.31 ? 140 GLN   A NE2  1 
ATOM   1007 N  NE2  B GLN   A 1 161 ? -16.824 17.521  12.060  0.30 23.67 ? 140 GLN   A NE2  1 
ATOM   1008 N  N    . ARG   A 1 162 ? -17.613 13.758  8.230   1.00 21.27 ? 141 ARG   A N    1 
ATOM   1009 C  CA   . ARG   A 1 162 ? -16.897 13.819  6.959   1.00 24.33 ? 141 ARG   A CA   1 
ATOM   1010 C  C    . ARG   A 1 162 ? -17.759 14.446  5.864   1.00 30.85 ? 141 ARG   A C    1 
ATOM   1011 O  O    . ARG   A 1 162 ? -17.250 14.706  4.773   1.00 39.34 ? 141 ARG   A O    1 
ATOM   1012 C  CB   . ARG   A 1 162 ? -16.535 12.396  6.532   1.00 25.74 ? 141 ARG   A CB   1 
ATOM   1013 C  CG   . ARG   A 1 162 ? -15.267 11.926  7.217   1.00 30.11 ? 141 ARG   A CG   1 
ATOM   1014 C  CD   . ARG   A 1 162 ? -14.141 12.610  6.465   1.00 35.82 ? 141 ARG   A CD   1 
ATOM   1015 N  NE   . ARG   A 1 162 ? -12.963 11.774  6.677   1.00 37.13 ? 141 ARG   A NE   1 
ATOM   1016 C  CZ   . ARG   A 1 162 ? -11.886 11.759  5.916   1.00 35.85 ? 141 ARG   A CZ   1 
ATOM   1017 N  NH1  . ARG   A 1 162 ? -11.787 12.555  4.864   1.00 36.13 ? 141 ARG   A NH1  1 
ATOM   1018 N  NH2  . ARG   A 1 162 ? -10.915 10.925  6.222   1.00 37.16 ? 141 ARG   A NH2  1 
ATOM   1019 N  N    . GLN   A 1 163 ? -19.050 14.674  6.145   1.00 33.60 ? 142 GLN   A N    1 
ATOM   1020 C  CA   . GLN   A 1 163 ? -19.901 15.429  5.231   1.00 36.63 ? 142 GLN   A CA   1 
ATOM   1021 C  C    . GLN   A 1 163 ? -20.506 16.643  5.947   1.00 44.10 ? 142 GLN   A C    1 
ATOM   1022 O  O    . GLN   A 1 163 ? -21.588 17.094  5.574   1.00 52.33 ? 142 GLN   A O    1 
ATOM   1023 C  CB   . GLN   A 1 163 ? -21.125 14.698  4.670   1.00 31.92 ? 142 GLN   A CB   1 
ATOM   1024 C  CG   . GLN   A 1 163 ? -21.210 13.193  4.917   1.00 25.83 ? 142 GLN   A CG   1 
ATOM   1025 C  CD   . GLN   A 1 163 ? -20.595 12.299  3.861   1.00 28.95 ? 142 GLN   A CD   1 
ATOM   1026 O  OE1  . GLN   A 1 163 ? -20.362 12.684  2.709   1.00 27.62 ? 142 GLN   A OE1  1 
ATOM   1027 N  NE2  . GLN   A 1 163 ? -20.386 11.045  4.237   1.00 26.41 ? 142 GLN   A NE2  1 
ATOM   1028 N  N    . LYS   A 1 164 ? -19.826 17.185  6.968   0.60 43.45 ? 143 LYS   A N    1 
ATOM   1029 C  CA   . LYS   A 1 164 ? -20.398 18.288  7.730   0.60 44.39 ? 143 LYS   A CA   1 
ATOM   1030 C  C    . LYS   A 1 164 ? -20.191 19.623  6.986   0.60 45.04 ? 143 LYS   A C    1 
ATOM   1031 O  O    . LYS   A 1 164 ? -19.050 19.868  6.533   0.60 46.44 ? 143 LYS   A O    1 
ATOM   1032 C  CB   . LYS   A 1 164 ? -19.955 18.293  9.200   0.60 44.54 ? 143 LYS   A CB   1 
ATOM   1033 C  CG   . LYS   A 1 164 ? -18.620 18.952  9.531   0.60 43.50 ? 143 LYS   A CG   1 
ATOM   1034 N  N    . SER   A 1 173 ? -26.382 13.745  -5.116  1.00 47.33 ? 152 SER   A N    1 
ATOM   1035 C  CA   . SER   A 1 173 ? -25.832 12.931  -3.999  1.00 42.43 ? 152 SER   A CA   1 
ATOM   1036 C  C    . SER   A 1 173 ? -26.968 12.236  -3.248  1.00 35.59 ? 152 SER   A C    1 
ATOM   1037 O  O    . SER   A 1 173 ? -28.057 12.785  -3.086  1.00 36.89 ? 152 SER   A O    1 
ATOM   1038 C  CB   . SER   A 1 173 ? -25.001 13.782  -3.079  1.00 46.67 ? 152 SER   A CB   1 
ATOM   1039 O  OG   . SER   A 1 173 ? -24.066 12.976  -2.377  1.00 51.26 ? 152 SER   A OG   1 
ATOM   1040 N  N    . ASN   A 1 174 ? -26.706 11.007  -2.792  1.00 29.56 ? 153 ASN   A N    1 
ATOM   1041 C  CA   . ASN   A 1 174 ? -27.737 10.233  -2.124  1.00 25.11 ? 153 ASN   A CA   1 
ATOM   1042 C  C    . ASN   A 1 174 ? -27.119 9.526   -0.918  1.00 20.05 ? 153 ASN   A C    1 
ATOM   1043 O  O    . ASN   A 1 174 ? -26.809 8.331   -0.987  1.00 21.83 ? 153 ASN   A O    1 
ATOM   1044 C  CB   . ASN   A 1 174 ? -28.377 9.293   -3.136  1.00 24.28 ? 153 ASN   A CB   1 
ATOM   1045 C  CG   . ASN   A 1 174 ? -29.403 8.370   -2.531  1.00 27.01 ? 153 ASN   A CG   1 
ATOM   1046 O  OD1  . ASN   A 1 174 ? -29.959 8.654   -1.461  1.00 24.87 ? 153 ASN   A OD1  1 
ATOM   1047 N  ND2  . ASN   A 1 174 ? -29.643 7.257   -3.216  1.00 32.17 ? 153 ASN   A ND2  1 
ATOM   1048 N  N    . LEU   A 1 175 ? -26.956 10.274  0.177   1.00 17.92 ? 154 LEU   A N    1 
ATOM   1049 C  CA   . LEU   A 1 175 ? -26.240 9.782   1.348   1.00 16.85 ? 154 LEU   A CA   1 
ATOM   1050 C  C    . LEU   A 1 175 ? -27.223 9.051   2.257   1.00 15.77 ? 154 LEU   A C    1 
ATOM   1051 O  O    . LEU   A 1 175 ? -28.292 9.574   2.575   1.00 16.32 ? 154 LEU   A O    1 
ATOM   1052 C  CB   . LEU   A 1 175 ? -25.653 10.959  2.121   1.00 17.81 ? 154 LEU   A CB   1 
ATOM   1053 C  CG   . LEU   A 1 175 ? -24.679 11.873  1.374   1.00 19.81 ? 154 LEU   A CG   1 
ATOM   1054 C  CD1  . LEU   A 1 175 ? -24.279 13.029  2.264   1.00 21.02 ? 154 LEU   A CD1  1 
ATOM   1055 C  CD2  . LEU   A 1 175 ? -23.484 11.091  0.869   1.00 20.34 ? 154 LEU   A CD2  1 
ATOM   1056 N  N    . SER   A 1 176 ? -26.855 7.843   2.695   1.00 15.81 ? 155 SER   A N    1 
ATOM   1057 C  CA   . SER   A 1 176 ? -27.702 7.235   3.710   1.00 16.97 ? 155 SER   A CA   1 
ATOM   1058 C  C    . SER   A 1 176 ? -26.946 6.194   4.530   1.00 15.37 ? 155 SER   A C    1 
ATOM   1059 O  O    . SER   A 1 176 ? -25.861 5.730   4.176   1.00 14.66 ? 155 SER   A O    1 
ATOM   1060 C  CB   . SER   A 1 176 ? -28.985 6.673   3.136   1.00 19.67 ? 155 SER   A CB   1 
ATOM   1061 O  OG   . SER   A 1 176 ? -28.728 5.414   2.531   1.00 20.95 ? 155 SER   A OG   1 
ATOM   1062 N  N    . ILE   A 1 177 ? -27.587 5.852   5.653   1.00 13.86 ? 156 ILE   A N    1 
ATOM   1063 C  CA   . ILE   A 1 177 ? -27.114 4.847   6.588   1.00 13.76 ? 156 ILE   A CA   1 
ATOM   1064 C  C    . ILE   A 1 177 ? -28.224 3.817   6.744   1.00 14.62 ? 156 ILE   A C    1 
ATOM   1065 O  O    . ILE   A 1 177 ? -29.396 4.186   6.854   1.00 13.52 ? 156 ILE   A O    1 
ATOM   1066 C  CB   . ILE   A 1 177 ? -26.751 5.473   7.941   1.00 14.70 ? 156 ILE   A CB   1 
ATOM   1067 C  CG1  . ILE   A 1 177 ? -25.671 6.583   7.761   1.00 14.88 ? 156 ILE   A CG1  1 
ATOM   1068 C  CG2  . ILE   A 1 177 ? -26.369 4.389   8.971   1.00 14.40 ? 156 ILE   A CG2  1 
ATOM   1069 C  CD1  . ILE   A 1 177 ? -25.429 7.418   9.008   1.00 15.16 ? 156 ILE   A CD1  1 
ATOM   1070 N  N    . VAL   A 1 178 ? -27.832 2.534   6.701   1.00 13.67 ? 157 VAL   A N    1 
ATOM   1071 C  CA   . VAL   A 1 178 ? -28.768 1.456   6.988   1.00 13.73 ? 157 VAL   A CA   1 
ATOM   1072 C  C    . VAL   A 1 178 ? -28.230 0.623   8.145   1.00 13.85 ? 157 VAL   A C    1 
ATOM   1073 O  O    . VAL   A 1 178 ? -27.104 0.120   8.083   1.00 13.46 ? 157 VAL   A O    1 
ATOM   1074 C  CB   . VAL   A 1 178 ? -29.012 0.581   5.748   1.00 13.72 ? 157 VAL   A CB   1 
ATOM   1075 C  CG1  . VAL   A 1 178 ? -29.998 -0.543  6.046   1.00 14.78 ? 157 VAL   A CG1  1 
ATOM   1076 C  CG2  . VAL   A 1 178 ? -29.481 1.394   4.551   1.00 14.71 ? 157 VAL   A CG2  1 
ATOM   1077 N  N    . ASN   A 1 179 ? -29.083 0.456   9.164   1.00 12.25 ? 158 ASN   A N    1 
ATOM   1078 C  CA   . ASN   A 1 179 ? -28.731 -0.303  10.360  1.00 12.53 ? 158 ASN   A CA   1 
ATOM   1079 C  C    . ASN   A 1 179 ? -29.417 -1.664  10.304  1.00 13.05 ? 158 ASN   A C    1 
ATOM   1080 O  O    . ASN   A 1 179 ? -30.620 -1.720  10.061  1.00 13.19 ? 158 ASN   A O    1 
ATOM   1081 C  CB   . ASN   A 1 179 ? -29.166 0.483   11.597  1.00 13.26 ? 158 ASN   A CB   1 
ATOM   1082 C  CG   . ASN   A 1 179 ? -28.356 1.752   11.768  1.00 12.68 ? 158 ASN   A CG   1 
ATOM   1083 O  OD1  . ASN   A 1 179 ? -27.183 1.758   11.374  1.00 14.34 ? 158 ASN   A OD1  1 
ATOM   1084 N  ND2  . ASN   A 1 179 ? -28.925 2.814   12.325  1.00 13.28 ? 158 ASN   A ND2  1 
ATOM   1085 N  N    . LEU   A 1 180 ? -28.664 -2.752  10.507  1.00 12.96 ? 159 LEU   A N    1 
ATOM   1086 C  CA   . LEU   A 1 180 ? -29.275 -4.074  10.566  1.00 12.55 ? 159 LEU   A CA   1 
ATOM   1087 C  C    . LEU   A 1 180 ? -29.796 -4.332  11.966  1.00 12.87 ? 159 LEU   A C    1 
ATOM   1088 O  O    . LEU   A 1 180 ? -29.008 -4.436  12.914  1.00 13.57 ? 159 LEU   A O    1 
ATOM   1089 C  CB   . LEU   A 1 180 ? -28.265 -5.152  10.164  1.00 13.22 ? 159 LEU   A CB   1 
ATOM   1090 C  CG   . LEU   A 1 180 ? -28.177 -5.463  8.662   1.00 13.41 ? 159 LEU   A CG   1 
ATOM   1091 C  CD1  . LEU   A 1 180 ? -29.433 -6.161  8.147   1.00 14.94 ? 159 LEU   A CD1  1 
ATOM   1092 C  CD2  . LEU   A 1 180 ? -27.940 -4.193  7.856   1.00 14.28 ? 159 LEU   A CD2  1 
ATOM   1093 N  N    . CYS   A 1 181 ? -31.131 -4.344  12.052  1.00 12.95 ? 160 CYS   A N    1 
ATOM   1094 C  CA   . CYS   A 1 181 ? -31.882 -4.448  13.289  1.00 14.92 ? 160 CYS   A CA   1 
ATOM   1095 C  C    . CYS   A 1 181 ? -32.328 -5.900  13.465  1.00 15.10 ? 160 CYS   A C    1 
ATOM   1096 O  O    . CYS   A 1 181 ? -31.632 -6.813  13.017  1.00 16.38 ? 160 CYS   A O    1 
ATOM   1097 C  CB   . CYS   A 1 181 ? -33.022 -3.436  13.283  1.00 15.07 ? 160 CYS   A CB   1 
ATOM   1098 S  SG   . CYS   A 1 181 ? -32.462 -1.701  13.235  1.00 17.69 ? 160 CYS   A SG   1 
ATOM   1099 N  N    . ASP   A 1 182 ? -33.428 -6.121  14.190  1.00 14.70 ? 161 ASP   A N    1 
ATOM   1100 C  CA   . ASP   A 1 182 ? -33.877 -7.476  14.475  1.00 14.54 ? 161 ASP   A CA   1 
ATOM   1101 C  C    . ASP   A 1 182 ? -35.384 -7.409  14.712  1.00 13.86 ? 161 ASP   A C    1 
ATOM   1102 O  O    . ASP   A 1 182 ? -35.855 -6.651  15.574  1.00 15.10 ? 161 ASP   A O    1 
ATOM   1103 C  CB   . ASP   A 1 182 ? -33.161 -8.002  15.710  1.00 14.55 ? 161 ASP   A CB   1 
ATOM   1104 C  CG   . ASP   A 1 182 ? -33.480 -9.442  16.080  1.00 17.74 ? 161 ASP   A CG   1 
ATOM   1105 O  OD1  . ASP   A 1 182 ? -34.632 -9.843  15.906  1.00 17.11 ? 161 ASP   A OD1  1 
ATOM   1106 O  OD2  . ASP   A 1 182 ? -32.573 -10.140 16.584  1.00 18.51 ? 161 ASP   A OD2  1 
ATOM   1107 N  N    . ALA   A 1 183 ? -36.149 -8.145  13.901  1.00 13.32 ? 162 ALA   A N    1 
ATOM   1108 C  CA   . ALA   A 1 183 ? -37.610 -8.081  13.928  1.00 13.55 ? 162 ALA   A CA   1 
ATOM   1109 C  C    . ALA   A 1 183 ? -38.218 -8.662  15.203  1.00 14.91 ? 162 ALA   A C    1 
ATOM   1110 O  O    . ALA   A 1 183 ? -39.401 -8.416  15.470  1.00 16.32 ? 162 ALA   A O    1 
ATOM   1111 C  CB   . ALA   A 1 183 ? -38.201 -8.762  12.704  1.00 14.61 ? 162 ALA   A CB   1 
ATOM   1112 N  N    . MET   A 1 184 ? -37.422 -9.425  15.960  1.00 14.72 ? 163 MET   A N    1 
ATOM   1113 C  CA   . MET   A 1 184 ? -37.952 -10.203 17.072  1.00 16.21 ? 163 MET   A CA   1 
ATOM   1114 C  C    . MET   A 1 184 ? -37.610 -9.595  18.429  1.00 18.96 ? 163 MET   A C    1 
ATOM   1115 O  O    . MET   A 1 184 ? -37.779 -10.256 19.446  1.00 18.65 ? 163 MET   A O    1 
ATOM   1116 C  CB   . MET   A 1 184 ? -37.449 -11.649 16.950  1.00 17.17 ? 163 MET   A CB   1 
ATOM   1117 C  CG   . MET   A 1 184 ? -37.959 -12.331 15.683  1.00 19.86 ? 163 MET   A CG   1 
ATOM   1118 S  SD   . MET   A 1 184 ? -39.741 -12.581 15.764  1.00 21.02 ? 163 MET   A SD   1 
ATOM   1119 C  CE   . MET   A 1 184 ? -39.741 -14.015 16.857  1.00 23.91 ? 163 MET   A CE   1 
ATOM   1120 N  N    . VAL   A 1 185 ? -37.219 -8.321  18.469  1.00 18.57 ? 164 VAL   A N    1 
ATOM   1121 C  CA   . VAL   A 1 185 ? -36.673 -7.814  19.723  1.00 20.16 ? 164 VAL   A CA   1 
ATOM   1122 C  C    . VAL   A 1 185 ? -37.767 -7.517  20.750  1.00 19.81 ? 164 VAL   A C    1 
ATOM   1123 O  O    . VAL   A 1 185 ? -37.449 -7.273  21.915  1.00 19.08 ? 164 VAL   A O    1 
ATOM   1124 C  CB   . VAL   A 1 185 ? -35.748 -6.610  19.503  1.00 24.24 ? 164 VAL   A CB   1 
ATOM   1125 C  CG1  . VAL   A 1 185 ? -34.503 -7.036  18.735  1.00 23.89 ? 164 VAL   A CG1  1 
ATOM   1126 C  CG2  . VAL   A 1 185 ? -36.494 -5.459  18.851  1.00 24.31 ? 164 VAL   A CG2  1 
ATOM   1127 N  N    . ASP   A 1 186 ? -39.044 -7.570  20.337  1.00 18.07 ? 165 ASP   A N    1 
ATOM   1128 C  CA   . ASP   A 1 186 ? -40.130 -7.451  21.306  1.00 17.96 ? 165 ASP   A CA   1 
ATOM   1129 C  C    . ASP   A 1 186 ? -40.675 -8.816  21.725  1.00 18.44 ? 165 ASP   A C    1 
ATOM   1130 O  O    . ASP   A 1 186 ? -41.593 -8.897  22.558  1.00 20.67 ? 165 ASP   A O    1 
ATOM   1131 C  CB   . ASP   A 1 186 ? -41.239 -6.536  20.812  1.00 18.47 ? 165 ASP   A CB   1 
ATOM   1132 C  CG   . ASP   A 1 186 ? -40.808 -5.092  20.636  1.00 19.37 ? 165 ASP   A CG   1 
ATOM   1133 O  OD1  . ASP   A 1 186 ? -39.994 -4.617  21.455  1.00 21.28 ? 165 ASP   A OD1  1 
ATOM   1134 O  OD2  . ASP   A 1 186 ? -41.295 -4.464  19.675  1.00 23.33 ? 165 ASP   A OD2  1 
ATOM   1135 N  N    . GLN   A 1 187 ? -40.114 -9.889  21.159  1.00 17.08 ? 166 GLN   A N    1 
ATOM   1136 C  CA   . GLN   A 1 187 ? -40.464 -11.252 21.557  1.00 18.43 ? 166 GLN   A CA   1 
ATOM   1137 C  C    . GLN   A 1 187 ? -39.151 -12.015 21.627  1.00 18.60 ? 166 GLN   A C    1 
ATOM   1138 O  O    . GLN   A 1 187 ? -38.892 -12.929 20.831  1.00 19.69 ? 166 GLN   A O    1 
ATOM   1139 C  CB   . GLN   A 1 187 ? -41.428 -11.944 20.585  1.00 20.20 ? 166 GLN   A CB   1 
ATOM   1140 C  CG   . GLN   A 1 187 ? -42.794 -11.273 20.449  1.00 22.92 ? 166 GLN   A CG   1 
ATOM   1141 C  CD   . GLN   A 1 187 ? -43.092 -10.939 18.998  1.00 26.83 ? 166 GLN   A CD   1 
ATOM   1142 O  OE1  . GLN   A 1 187 ? -42.569 -9.967  18.437  1.00 26.78 ? 166 GLN   A OE1  1 
ATOM   1143 N  NE2  . GLN   A 1 187 ? -43.938 -11.741 18.375  1.00 27.98 ? 166 GLN   A NE2  1 
ATOM   1144 N  N    . PRO   A 1 188 ? -38.268 -11.612 22.567  1.00 17.91 ? 167 PRO   A N    1 
ATOM   1145 C  CA   . PRO   A 1 188 ? -36.862 -12.009 22.511  1.00 18.23 ? 167 PRO   A CA   1 
ATOM   1146 C  C    . PRO   A 1 188 ? -36.592 -13.459 22.877  1.00 17.04 ? 167 PRO   A C    1 
ATOM   1147 O  O    . PRO   A 1 188 ? -37.373 -14.080 23.603  1.00 19.25 ? 167 PRO   A O    1 
ATOM   1148 C  CB   . PRO   A 1 188 ? -36.221 -11.037 23.501  1.00 19.32 ? 167 PRO   A CB   1 
ATOM   1149 C  CG   . PRO   A 1 188 ? -37.314 -10.796 24.527  1.00 19.32 ? 167 PRO   A CG   1 
ATOM   1150 C  CD   . PRO   A 1 188 ? -38.562 -10.690 23.682  1.00 17.31 ? 167 PRO   A CD   1 
ATOM   1151 N  N    . CYS   A 1 189 ? -35.447 -13.956 22.393  1.00 17.49 ? 168 CYS   A N    1 
ATOM   1152 C  CA   . CYS   A 1 189 ? -35.026 -15.272 22.836  1.00 20.42 ? 168 CYS   A CA   1 
ATOM   1153 C  C    . CYS   A 1 189 ? -34.604 -15.184 24.298  1.00 18.29 ? 168 CYS   A C    1 
ATOM   1154 O  O    . CYS   A 1 189 ? -34.022 -14.203 24.763  1.00 18.77 ? 168 CYS   A O    1 
ATOM   1155 C  CB   . CYS   A 1 189 ? -33.884 -15.841 22.006  1.00 23.30 ? 168 CYS   A CB   1 
ATOM   1156 S  SG   . CYS   A 1 189 ? -34.439 -16.347 20.353  1.00 32.02 ? 168 CYS   A SG   1 
ATOM   1157 N  N    . MET   A 1 190 ? -34.926 -16.250 25.016  1.00 18.83 ? 169 MET   A N    1 
ATOM   1158 C  CA   . MET   A 1 190 ? -34.601 -16.381 26.420  1.00 20.63 ? 169 MET   A CA   1 
ATOM   1159 C  C    . MET   A 1 190 ? -33.091 -16.255 26.602  1.00 18.09 ? 169 MET   A C    1 
ATOM   1160 O  O    . MET   A 1 190 ? -32.335 -16.887 25.864  1.00 17.57 ? 169 MET   A O    1 
ATOM   1161 C  CB   . MET   A 1 190 ? -34.988 -17.807 26.842  1.00 24.52 ? 169 MET   A CB   1 
ATOM   1162 C  CG   . MET   A 1 190 ? -34.611 -18.164 28.254  1.00 27.74 ? 169 MET   A CG   1 
ATOM   1163 S  SD   . MET   A 1 190 ? -35.552 -17.034 29.295  1.00 32.49 ? 169 MET   A SD   1 
ATOM   1164 C  CE   . MET   A 1 190 ? -37.198 -17.748 29.269  1.00 28.71 ? 169 MET   A CE   1 
ATOM   1165 N  N    . ALA   A 1 191 ? -32.670 -15.434 27.594  1.00 16.44 ? 170 ALA   A N    1 
ATOM   1166 C  CA   . ALA   A 1 191 ? -31.297 -15.280 28.044  1.00 16.84 ? 170 ALA   A CA   1 
ATOM   1167 C  C    . ALA   A 1 191 ? -30.440 -14.467 27.072  1.00 15.21 ? 170 ALA   A C    1 
ATOM   1168 O  O    . ALA   A 1 191 ? -29.211 -14.533 27.135  1.00 16.80 ? 170 ALA   A O    1 
ATOM   1169 C  CB   . ALA   A 1 191 ? -30.668 -16.646 28.355  1.00 18.44 ? 170 ALA   A CB   1 
ATOM   1170 N  N    . PHE   A 1 192 ? -31.068 -13.658 26.191  1.00 14.58 ? 171 PHE   A N    1 
ATOM   1171 C  CA   . PHE   A 1 192 ? -30.328 -12.796 25.273  1.00 14.18 ? 171 PHE   A CA   1 
ATOM   1172 C  C    . PHE   A 1 192 ? -30.471 -11.322 25.655  1.00 14.58 ? 171 PHE   A C    1 
ATOM   1173 O  O    . PHE   A 1 192 ? -30.565 -10.473 24.778  1.00 15.27 ? 171 PHE   A O    1 
ATOM   1174 C  CB   . PHE   A 1 192 ? -30.775 -13.040 23.827  1.00 14.88 ? 171 PHE   A CB   1 
ATOM   1175 C  CG   . PHE   A 1 192 ? -30.144 -14.272 23.189  1.00 15.37 ? 171 PHE   A CG   1 
ATOM   1176 C  CD1  . PHE   A 1 192 ? -30.619 -15.547 23.482  1.00 18.40 ? 171 PHE   A CD1  1 
ATOM   1177 C  CD2  . PHE   A 1 192 ? -29.068 -14.139 22.318  1.00 17.48 ? 171 PHE   A CD2  1 
ATOM   1178 C  CE1  . PHE   A 1 192 ? -30.030 -16.665 22.896  1.00 18.74 ? 171 PHE   A CE1  1 
ATOM   1179 C  CE2  . PHE   A 1 192 ? -28.478 -15.264 21.733  1.00 18.16 ? 171 PHE   A CE2  1 
ATOM   1180 C  CZ   . PHE   A 1 192 ? -28.959 -16.520 22.034  1.00 18.20 ? 171 PHE   A CZ   1 
ATOM   1181 N  N    . SER   A 1 193 ? -30.418 -10.984 26.944  1.00 13.47 ? 172 SER   A N    1 
ATOM   1182 C  CA   A SER   A 1 193 ? -30.695 -9.616  27.388  0.60 14.86 ? 172 SER   A CA   1 
ATOM   1183 C  CA   B SER   A 1 193 ? -30.754 -9.615  27.312  0.40 13.51 ? 172 SER   A CA   1 
ATOM   1184 C  C    . SER   A 1 193 ? -29.781 -8.593  26.724  1.00 15.12 ? 172 SER   A C    1 
ATOM   1185 O  O    . SER   A 1 193 ? -30.237 -7.568  26.238  1.00 13.45 ? 172 SER   A O    1 
ATOM   1186 C  CB   A SER   A 1 193 ? -30.553 -9.480  28.886  0.60 16.87 ? 172 SER   A CB   1 
ATOM   1187 C  CB   B SER   A 1 193 ? -30.893 -9.455  28.797  0.40 13.24 ? 172 SER   A CB   1 
ATOM   1188 O  OG   A SER   A 1 193 ? -31.686 -9.996  29.563  0.60 19.47 ? 172 SER   A OG   1 
ATOM   1189 O  OG   B SER   A 1 193 ? -29.698 -9.888  29.428  0.40 12.11 ? 172 SER   A OG   1 
ATOM   1190 N  N    . LEU   A 1 194 ? -28.459 -8.823  26.791  1.00 13.52 ? 173 LEU   A N    1 
ATOM   1191 C  CA   . LEU   A 1 194 ? -27.532 -7.807  26.307  1.00 13.86 ? 173 LEU   A CA   1 
ATOM   1192 C  C    . LEU   A 1 194 ? -27.670 -7.608  24.803  1.00 13.71 ? 173 LEU   A C    1 
ATOM   1193 O  O    . LEU   A 1 194 ? -27.638 -6.487  24.319  1.00 13.26 ? 173 LEU   A O    1 
ATOM   1194 C  CB   . LEU   A 1 194 ? -26.077 -8.096  26.669  1.00 14.99 ? 173 LEU   A CB   1 
ATOM   1195 C  CG   . LEU   A 1 194 ? -25.718 -7.769  28.115  1.00 14.55 ? 173 LEU   A CG   1 
ATOM   1196 C  CD1  . LEU   A 1 194 ? -24.344 -8.351  28.469  1.00 15.29 ? 173 LEU   A CD1  1 
ATOM   1197 C  CD2  . LEU   A 1 194 ? -25.720 -6.239  28.338  1.00 15.53 ? 173 LEU   A CD2  1 
ATOM   1198 N  N    . TYR   A 1 195 ? -27.819 -8.697  24.053  1.00 12.72 ? 174 TYR   A N    1 
ATOM   1199 C  CA   . TYR   A 1 195 ? -28.063 -8.592  22.623  1.00 13.04 ? 174 TYR   A CA   1 
ATOM   1200 C  C    . TYR   A 1 195 ? -29.320 -7.756  22.356  1.00 13.48 ? 174 TYR   A C    1 
ATOM   1201 O  O    . TYR   A 1 195 ? -29.297 -6.868  21.503  1.00 13.68 ? 174 TYR   A O    1 
ATOM   1202 C  CB   . TYR   A 1 195 ? -28.181 -10.003 22.020  1.00 13.63 ? 174 TYR   A CB   1 
ATOM   1203 C  CG   . TYR   A 1 195 ? -28.651 -9.937  20.576  1.00 13.58 ? 174 TYR   A CG   1 
ATOM   1204 C  CD1  . TYR   A 1 195 ? -27.770 -9.646  19.536  1.00 13.28 ? 174 TYR   A CD1  1 
ATOM   1205 C  CD2  . TYR   A 1 195 ? -29.997 -10.100 20.272  1.00 13.72 ? 174 TYR   A CD2  1 
ATOM   1206 C  CE1  . TYR   A 1 195 ? -28.219 -9.566  18.222  1.00 13.39 ? 174 TYR   A CE1  1 
ATOM   1207 C  CE2  . TYR   A 1 195 ? -30.457 -10.002 18.967  1.00 14.54 ? 174 TYR   A CE2  1 
ATOM   1208 C  CZ   . TYR   A 1 195 ? -29.568 -9.734  17.940  1.00 13.93 ? 174 TYR   A CZ   1 
ATOM   1209 O  OH   . TYR   A 1 195 ? -30.054 -9.625  16.670  1.00 16.23 ? 174 TYR   A OH   1 
ATOM   1210 N  N    . ASN   A 1 196 ? -30.405 -8.051  23.073  1.00 13.46 ? 175 ASN   A N    1 
ATOM   1211 C  CA   A ASN   A 1 196 ? -31.669 -7.358  22.871  0.40 13.58 ? 175 ASN   A CA   1 
ATOM   1212 C  CA   B ASN   A 1 196 ? -31.651 -7.342  22.828  0.60 13.41 ? 175 ASN   A CA   1 
ATOM   1213 C  C    . ASN   A 1 196 ? -31.509 -5.880  23.214  1.00 14.02 ? 175 ASN   A C    1 
ATOM   1214 O  O    . ASN   A 1 196 ? -32.048 -5.016  22.528  1.00 13.93 ? 175 ASN   A O    1 
ATOM   1215 C  CB   A ASN   A 1 196 ? -32.765 -8.005  23.711  0.40 14.42 ? 175 ASN   A CB   1 
ATOM   1216 C  CB   B ASN   A 1 196 ? -32.809 -8.007  23.557  0.60 14.79 ? 175 ASN   A CB   1 
ATOM   1217 C  CG   A ASN   A 1 196 ? -34.140 -7.512  23.334  0.40 15.90 ? 175 ASN   A CG   1 
ATOM   1218 C  CG   B ASN   A 1 196 ? -33.340 -9.146  22.730  0.60 18.26 ? 175 ASN   A CG   1 
ATOM   1219 O  OD1  A ASN   A 1 196 ? -34.965 -7.221  24.205  0.40 17.45 ? 175 ASN   A OD1  1 
ATOM   1220 O  OD1  B ASN   A 1 196 ? -34.079 -8.910  21.764  0.60 20.03 ? 175 ASN   A OD1  1 
ATOM   1221 N  ND2  A ASN   A 1 196 ? -34.413 -7.449  22.043  0.40 17.26 ? 175 ASN   A ND2  1 
ATOM   1222 N  ND2  B ASN   A 1 196 ? -32.948 -10.369 23.060  0.60 17.36 ? 175 ASN   A ND2  1 
ATOM   1223 N  N    . MET   A 1 197 ? -30.777 -5.607  24.291  1.00 13.23 ? 176 MET   A N    1 
ATOM   1224 C  CA   . MET   A 1 197 ? -30.561 -4.213  24.652  1.00 13.57 ? 176 MET   A CA   1 
ATOM   1225 C  C    . MET   A 1 197 ? -29.848 -3.504  23.510  1.00 13.57 ? 176 MET   A C    1 
ATOM   1226 O  O    . MET   A 1 197 ? -30.119 -2.335  23.217  1.00 12.97 ? 176 MET   A O    1 
ATOM   1227 C  CB   . MET   A 1 197 ? -29.705 -4.127  25.916  1.00 13.04 ? 176 MET   A CB   1 
ATOM   1228 C  CG   . MET   A 1 197 ? -30.484 -4.561  27.151  1.00 13.96 ? 176 MET   A CG   1 
ATOM   1229 S  SD   . MET   A 1 197 ? -29.419 -4.779  28.596  1.00 15.49 ? 176 MET   A SD   1 
ATOM   1230 C  CE   . MET   A 1 197 ? -29.032 -3.037  28.826  1.00 16.26 ? 176 MET   A CE   1 
ATOM   1231 N  N    . GLY   A 1 198 ? -28.830 -4.173  22.977  1.00 12.06 ? 177 GLY   A N    1 
ATOM   1232 C  CA   . GLY   A 1 198 ? -28.048 -3.576  21.905  1.00 12.43 ? 177 GLY   A CA   1 
ATOM   1233 C  C    . GLY   A 1 198 ? -28.913 -3.273  20.681  1.00 12.47 ? 177 GLY   A C    1 
ATOM   1234 O  O    . GLY   A 1 198 ? -28.806 -2.204  20.100  1.00 12.63 ? 177 GLY   A O    1 
ATOM   1235 N  N    . LYS   A 1 199 ? -29.762 -4.225  20.287  1.00 11.55 ? 178 LYS   A N    1 
ATOM   1236 C  CA   . LYS   A 1 199 ? -30.620 -4.013  19.121  1.00 12.44 ? 178 LYS   A CA   1 
ATOM   1237 C  C    . LYS   A 1 199 ? -31.694 -2.959  19.382  1.00 12.45 ? 178 LYS   A C    1 
ATOM   1238 O  O    . LYS   A 1 199 ? -32.043 -2.214  18.466  1.00 13.29 ? 178 LYS   A O    1 
ATOM   1239 C  CB   . LYS   A 1 199 ? -31.198 -5.356  18.649  1.00 12.88 ? 178 LYS   A CB   1 
ATOM   1240 C  CG   . LYS   A 1 199 ? -30.159 -6.248  17.988  1.00 13.32 ? 178 LYS   A CG   1 
ATOM   1241 C  CD   . LYS   A 1 199 ? -29.492 -5.618  16.764  1.00 13.92 ? 178 LYS   A CD   1 
ATOM   1242 C  CE   . LYS   A 1 199 ? -28.785 -6.657  15.910  1.00 14.77 ? 178 LYS   A CE   1 
ATOM   1243 N  NZ   . LYS   A 1 199 ? -27.838 -6.098  14.923  1.00 14.49 ? 178 LYS   A NZ   1 
ATOM   1244 N  N    . HIS   A 1 200 ? -32.246 -2.904  20.603  1.00 12.71 ? 179 HIS   A N    1 
ATOM   1245 C  CA   . HIS   A 1 200 ? -33.180 -1.829  20.902  1.00 12.29 ? 179 HIS   A CA   1 
ATOM   1246 C  C    . HIS   A 1 200 ? -32.454 -0.489  20.843  1.00 12.28 ? 179 HIS   A C    1 
ATOM   1247 O  O    . HIS   A 1 200 ? -33.017 0.478   20.316  1.00 12.22 ? 179 HIS   A O    1 
ATOM   1248 C  CB   . HIS   A 1 200 ? -33.805 -2.009  22.292  1.00 13.22 ? 179 HIS   A CB   1 
ATOM   1249 C  CG   . HIS   A 1 200 ? -35.006 -2.871  22.302  1.00 14.72 ? 179 HIS   A CG   1 
ATOM   1250 N  ND1  . HIS   A 1 200 ? -36.281 -2.368  22.192  1.00 17.80 ? 179 HIS   A ND1  1 
ATOM   1251 C  CD2  . HIS   A 1 200 ? -35.117 -4.208  22.428  1.00 15.55 ? 179 HIS   A CD2  1 
ATOM   1252 C  CE1  . HIS   A 1 200 ? -37.139 -3.374  22.279  1.00 16.64 ? 179 HIS   A CE1  1 
ATOM   1253 N  NE2  . HIS   A 1 200 ? -36.462 -4.490  22.435  1.00 17.17 ? 179 HIS   A NE2  1 
ATOM   1254 N  N    . ALA   A 1 201 ? -31.221 -0.420  21.384  1.00 11.92 ? 180 ALA   A N    1 
ATOM   1255 C  CA   . ALA   A 1 201 ? -30.483 0.838   21.304  1.00 11.42 ? 180 ALA   A CA   1 
ATOM   1256 C  C    . ALA   A 1 201 ? -30.274 1.232   19.835  1.00 12.88 ? 180 ALA   A C    1 
ATOM   1257 O  O    . ALA   A 1 201 ? -30.279 2.412   19.496  1.00 13.53 ? 180 ALA   A O    1 
ATOM   1258 C  CB   . ALA   A 1 201 ? -29.160 0.722   22.034  1.00 11.70 ? 180 ALA   A CB   1 
ATOM   1259 N  N    . LEU   A 1 202 ? -30.078 0.259   18.942  1.00 11.63 ? 181 LEU   A N    1 
ATOM   1260 C  CA   . LEU   A 1 202 ? -29.892 0.532   17.520  1.00 13.29 ? 181 LEU   A CA   1 
ATOM   1261 C  C    . LEU   A 1 202 ? -31.153 1.130   16.900  1.00 13.55 ? 181 LEU   A C    1 
ATOM   1262 O  O    . LEU   A 1 202 ? -31.033 2.006   16.034  1.00 13.83 ? 181 LEU   A O    1 
ATOM   1263 C  CB   . LEU   A 1 202 ? -29.437 -0.746  16.811  1.00 12.50 ? 181 LEU   A CB   1 
ATOM   1264 C  CG   . LEU   A 1 202 ? -29.005 -0.569  15.347  1.00 13.17 ? 181 LEU   A CG   1 
ATOM   1265 C  CD1  . LEU   A 1 202 ? -27.822 0.391   15.175  1.00 13.64 ? 181 LEU   A CD1  1 
ATOM   1266 C  CD2  . LEU   A 1 202 ? -28.595 -1.963  14.840  1.00 13.40 ? 181 LEU   A CD2  1 
ATOM   1267 N  N    . VAL   A 1 203 ? -32.347 0.717   17.366  1.00 13.13 ? 182 VAL   A N    1 
ATOM   1268 C  CA   . VAL   A 1 203 ? -33.582 1.347   16.911  1.00 13.63 ? 182 VAL   A CA   1 
ATOM   1269 C  C    . VAL   A 1 203 ? -33.580 2.807   17.366  1.00 13.08 ? 182 VAL   A C    1 
ATOM   1270 O  O    . VAL   A 1 203 ? -33.909 3.714   16.591  1.00 13.81 ? 182 VAL   A O    1 
ATOM   1271 C  CB   . VAL   A 1 203 ? -34.812 0.624   17.485  1.00 15.09 ? 182 VAL   A CB   1 
ATOM   1272 C  CG1  . VAL   A 1 203 ? -36.099 1.368   17.156  1.00 16.23 ? 182 VAL   A CG1  1 
ATOM   1273 C  CG2  . VAL   A 1 203 ? -34.884 -0.799  16.943  1.00 16.28 ? 182 VAL   A CG2  1 
ATOM   1274 N  N    . GLY   A 1 204 ? -33.177 3.041   18.618  1.00 12.47 ? 183 GLY   A N    1 
ATOM   1275 C  CA   . GLY   A 1 204 ? -33.143 4.418   19.101  1.00 13.21 ? 183 GLY   A CA   1 
ATOM   1276 C  C    . GLY   A 1 204 ? -32.160 5.252   18.280  1.00 13.49 ? 183 GLY   A C    1 
ATOM   1277 O  O    . GLY   A 1 204 ? -32.397 6.428   18.004  1.00 14.41 ? 183 GLY   A O    1 
ATOM   1278 N  N    . LEU   A 1 205 ? -31.007 4.681   17.940  1.00 12.85 ? 184 LEU   A N    1 
ATOM   1279 C  CA   . LEU   A 1 205 ? -30.043 5.408   17.120  1.00 12.32 ? 184 LEU   A CA   1 
ATOM   1280 C  C    . LEU   A 1 205 ? -30.619 5.725   15.737  1.00 12.98 ? 184 LEU   A C    1 
ATOM   1281 O  O    . LEU   A 1 205 ? -30.461 6.836   15.228  1.00 13.91 ? 184 LEU   A O    1 
ATOM   1282 C  CB   . LEU   A 1 205 ? -28.749 4.606   16.969  1.00 12.13 ? 184 LEU   A CB   1 
ATOM   1283 C  CG   . LEU   A 1 205 ? -27.740 5.204   15.986  1.00 13.02 ? 184 LEU   A CG   1 
ATOM   1284 C  CD1  . LEU   A 1 205 ? -27.202 6.582   16.391  1.00 14.41 ? 184 LEU   A CD1  1 
ATOM   1285 C  CD2  . LEU   A 1 205 ? -26.631 4.208   15.758  1.00 13.61 ? 184 LEU   A CD2  1 
ATOM   1286 N  N    . THR   A 1 206 ? -31.309 4.754   15.144  1.00 12.94 ? 185 THR   A N    1 
ATOM   1287 C  CA   . THR   A 1 206 ? -31.865 4.935   13.815  1.00 13.01 ? 185 THR   A CA   1 
ATOM   1288 C  C    . THR   A 1 206 ? -32.801 6.149   13.844  1.00 13.20 ? 185 THR   A C    1 
ATOM   1289 O  O    . THR   A 1 206 ? -32.751 7.003   12.953  1.00 13.78 ? 185 THR   A O    1 
ATOM   1290 C  CB   . THR   A 1 206 ? -32.599 3.663   13.390  1.00 13.22 ? 185 THR   A CB   1 
ATOM   1291 O  OG1  . THR   A 1 206 ? -31.665 2.587   13.354  1.00 14.02 ? 185 THR   A OG1  1 
ATOM   1292 C  CG2  . THR   A 1 206 ? -33.183 3.814   12.000  1.00 14.98 ? 185 THR   A CG2  1 
ATOM   1293 N  N    . GLN   A 1 207 ? -33.661 6.221   14.858  1.00 12.72 ? 186 GLN   A N    1 
ATOM   1294 C  CA   . GLN   A 1 207 ? -34.616 7.324   14.928  1.00 12.96 ? 186 GLN   A CA   1 
ATOM   1295 C  C    . GLN   A 1 207 ? -33.924 8.646   15.251  1.00 12.95 ? 186 GLN   A C    1 
ATOM   1296 O  O    . GLN   A 1 207 ? -34.189 9.653   14.593  1.00 13.27 ? 186 GLN   A O    1 
ATOM   1297 C  CB   . GLN   A 1 207 ? -35.639 6.975   16.017  1.00 14.09 ? 186 GLN   A CB   1 
ATOM   1298 C  CG   . GLN   A 1 207 ? -36.493 5.764   15.624  1.00 16.39 ? 186 GLN   A CG   1 
ATOM   1299 C  CD   . GLN   A 1 207 ? -37.545 5.347   16.630  1.00 20.74 ? 186 GLN   A CD   1 
ATOM   1300 O  OE1  . GLN   A 1 207 ? -38.533 4.704   16.244  1.00 25.56 ? 186 GLN   A OE1  1 
ATOM   1301 N  NE2  . GLN   A 1 207 ? -37.347 5.685   17.895  1.00 21.33 ? 186 GLN   A NE2  1 
ATOM   1302 N  N    . SER   A 1 208 ? -33.061 8.659   16.282  1.00 12.56 ? 187 SER   A N    1 
ATOM   1303 C  CA   . SER   A 1 208 ? -32.373 9.890   16.685  1.00 12.82 ? 187 SER   A CA   1 
ATOM   1304 C  C    . SER   A 1 208 ? -31.493 10.442  15.566  1.00 13.62 ? 187 SER   A C    1 
ATOM   1305 O  O    . SER   A 1 208 ? -31.466 11.669  15.306  1.00 14.77 ? 187 SER   A O    1 
ATOM   1306 C  CB   . SER   A 1 208 ? -31.527 9.663   17.921  1.00 13.85 ? 187 SER   A CB   1 
ATOM   1307 O  OG   . SER   A 1 208 ? -32.357 9.562   19.070  1.00 15.59 ? 187 SER   A OG   1 
ATOM   1308 N  N    . ALA   A 1 209 ? -30.741 9.546   14.931  1.00 13.25 ? 188 ALA   A N    1 
ATOM   1309 C  CA   . ALA   A 1 209 ? -29.873 9.998   13.855  1.00 13.47 ? 188 ALA   A CA   1 
ATOM   1310 C  C    . ALA   A 1 209 ? -30.678 10.438  12.628  1.00 13.53 ? 188 ALA   A C    1 
ATOM   1311 O  O    . ALA   A 1 209 ? -30.266 11.355  11.916  1.00 13.96 ? 188 ALA   A O    1 
ATOM   1312 C  CB   . ALA   A 1 209 ? -28.861 8.954   13.503  1.00 13.72 ? 188 ALA   A CB   1 
ATOM   1313 N  N    . ALA   A 1 210 ? -31.789 9.758   12.328  1.00 13.17 ? 189 ALA   A N    1 
ATOM   1314 C  CA   . ALA   A 1 210 ? -32.633 10.204  11.219  1.00 13.21 ? 189 ALA   A CA   1 
ATOM   1315 C  C    . ALA   A 1 210 ? -33.073 11.651  11.458  1.00 14.24 ? 189 ALA   A C    1 
ATOM   1316 O  O    . ALA   A 1 210 ? -33.039 12.481  10.548  1.00 15.38 ? 189 ALA   A O    1 
ATOM   1317 C  CB   . ALA   A 1 210 ? -33.839 9.276   11.032  1.00 13.69 ? 189 ALA   A CB   1 
ATOM   1318 N  N    . LEU   A 1 211 ? -33.516 11.939  12.674  1.00 13.82 ? 190 LEU   A N    1 
ATOM   1319 C  CA   . LEU   A 1 211 ? -33.993 13.277  12.984  1.00 15.25 ? 190 LEU   A CA   1 
ATOM   1320 C  C    . LEU   A 1 211 ? -32.857 14.279  12.829  1.00 15.58 ? 190 LEU   A C    1 
ATOM   1321 O  O    . LEU   A 1 211 ? -33.036 15.345  12.234  1.00 16.97 ? 190 LEU   A O    1 
ATOM   1322 C  CB   . LEU   A 1 211 ? -34.538 13.258  14.409  1.00 15.18 ? 190 LEU   A CB   1 
ATOM   1323 C  CG   . LEU   A 1 211 ? -34.993 14.621  14.955  1.00 17.86 ? 190 LEU   A CG   1 
ATOM   1324 C  CD1  . LEU   A 1 211 ? -36.283 15.078  14.262  1.00 19.73 ? 190 LEU   A CD1  1 
ATOM   1325 C  CD2  . LEU   A 1 211 ? -35.198 14.497  16.456  1.00 18.71 ? 190 LEU   A CD2  1 
ATOM   1326 N  N    . GLU   A 1 212 ? -31.683 13.948  13.371  1.00 15.05 ? 191 GLU   A N    1 
ATOM   1327 C  CA   . GLU   A 1 212 ? -30.623 14.934  13.475  1.00 15.62 ? 191 GLU   A CA   1 
ATOM   1328 C  C    . GLU   A 1 212 ? -29.895 15.122  12.148  1.00 17.72 ? 191 GLU   A C    1 
ATOM   1329 O  O    . GLU   A 1 212 ? -29.408 16.230  11.878  1.00 19.04 ? 191 GLU   A O    1 
ATOM   1330 C  CB   . GLU   A 1 212 ? -29.700 14.494  14.609  1.00 17.35 ? 191 GLU   A CB   1 
ATOM   1331 C  CG   . GLU   A 1 212 ? -28.518 15.424  14.855  1.00 18.47 ? 191 GLU   A CG   1 
ATOM   1332 C  CD   . GLU   A 1 212 ? -27.735 15.039  16.092  1.00 22.13 ? 191 GLU   A CD   1 
ATOM   1333 O  OE1  . GLU   A 1 212 ? -26.676 15.652  16.299  1.00 22.01 ? 191 GLU   A OE1  1 
ATOM   1334 O  OE2  . GLU   A 1 212 ? -28.184 14.121  16.835  1.00 21.90 ? 191 GLU   A OE2  1 
ATOM   1335 N  N    . LEU   A 1 213 ? -29.802 14.064  11.334  1.00 15.71 ? 192 LEU   A N    1 
ATOM   1336 C  CA   . LEU   A 1 213 ? -29.030 14.157  10.098  1.00 15.19 ? 192 LEU   A CA   1 
ATOM   1337 C  C    . LEU   A 1 213 ? -29.890 14.536  8.893   1.00 14.99 ? 192 LEU   A C    1 
ATOM   1338 O  O    . LEU   A 1 213 ? -29.344 14.793  7.824   1.00 16.56 ? 192 LEU   A O    1 
ATOM   1339 C  CB   . LEU   A 1 213 ? -28.262 12.860  9.865   1.00 14.84 ? 192 LEU   A CB   1 
ATOM   1340 C  CG   . LEU   A 1 213 ? -27.262 12.515  10.969  1.00 15.05 ? 192 LEU   A CG   1 
ATOM   1341 C  CD1  . LEU   A 1 213 ? -26.517 11.256  10.554  1.00 15.98 ? 192 LEU   A CD1  1 
ATOM   1342 C  CD2  . LEU   A 1 213 ? -26.288 13.647  11.270  1.00 15.09 ? 192 LEU   A CD2  1 
ATOM   1343 N  N    . ALA   A 1 214 ? -31.213 14.612  9.073   1.00 15.62 ? 193 ALA   A N    1 
ATOM   1344 C  CA   . ALA   A 1 214 ? -32.096 14.941  7.952   1.00 16.28 ? 193 ALA   A CA   1 
ATOM   1345 C  C    . ALA   A 1 214 ? -31.716 16.295  7.351   1.00 19.92 ? 193 ALA   A C    1 
ATOM   1346 O  O    . ALA   A 1 214 ? -31.728 16.427  6.126   1.00 19.64 ? 193 ALA   A O    1 
ATOM   1347 C  CB   . ALA   A 1 214 ? -33.545 14.902  8.388   1.00 18.21 ? 193 ALA   A CB   1 
ATOM   1348 N  N    . PRO   A 1 215 ? -31.360 17.321  8.157   1.00 22.31 ? 194 PRO   A N    1 
ATOM   1349 C  CA   . PRO   A 1 215 ? -30.948 18.607  7.593   1.00 24.73 ? 194 PRO   A CA   1 
ATOM   1350 C  C    . PRO   A 1 215 ? -29.702 18.537  6.711   1.00 25.19 ? 194 PRO   A C    1 
ATOM   1351 O  O    . PRO   A 1 215 ? -29.470 19.447  5.918   1.00 29.24 ? 194 PRO   A O    1 
ATOM   1352 C  CB   . PRO   A 1 215 ? -30.740 19.534  8.811   1.00 28.26 ? 194 PRO   A CB   1 
ATOM   1353 C  CG   . PRO   A 1 215 ? -31.428 18.832  9.958   1.00 29.29 ? 194 PRO   A CG   1 
ATOM   1354 C  CD   . PRO   A 1 215 ? -31.376 17.341  9.631   1.00 23.97 ? 194 PRO   A CD   1 
ATOM   1355 N  N    . TYR   A 1 216 ? -28.902 17.468  6.830   1.00 22.34 ? 195 TYR   A N    1 
ATOM   1356 C  CA   . TYR   A 1 216 ? -27.691 17.313  6.033   1.00 23.65 ? 195 TYR   A CA   1 
ATOM   1357 C  C    . TYR   A 1 216 ? -27.967 16.432  4.814   1.00 24.15 ? 195 TYR   A C    1 
ATOM   1358 O  O    . TYR   A 1 216 ? -27.051 16.127  4.042   1.00 25.72 ? 195 TYR   A O    1 
ATOM   1359 C  CB   . TYR   A 1 216 ? -26.565 16.708  6.884   1.00 28.34 ? 195 TYR   A CB   1 
ATOM   1360 C  CG   . TYR   A 1 216 ? -26.169 17.549  8.091   0.60 28.96 ? 195 TYR   A CG   1 
ATOM   1361 C  CD1  . TYR   A 1 216 ? -26.956 17.561  9.236   0.60 29.05 ? 195 TYR   A CD1  1 
ATOM   1362 C  CD2  . TYR   A 1 216 ? -25.014 18.325  8.094   0.60 31.62 ? 195 TYR   A CD2  1 
ATOM   1363 C  CE1  . TYR   A 1 216 ? -26.624 18.325  10.343  0.60 32.39 ? 195 TYR   A CE1  1 
ATOM   1364 C  CE2  . TYR   A 1 216 ? -24.661 19.084  9.200   0.60 31.95 ? 195 TYR   A CE2  1 
ATOM   1365 C  CZ   . TYR   A 1 216 ? -25.472 19.091  10.324  0.60 33.80 ? 195 TYR   A CZ   1 
ATOM   1366 O  OH   . TYR   A 1 216 ? -25.165 19.824  11.438  0.60 37.22 ? 195 TYR   A OH   1 
ATOM   1367 N  N    . GLY   A 1 217 ? -29.222 15.990  4.669   1.00 20.93 ? 196 GLY   A N    1 
ATOM   1368 C  CA   . GLY   A 1 217 ? -29.631 15.172  3.542   1.00 19.81 ? 196 GLY   A CA   1 
ATOM   1369 C  C    . GLY   A 1 217 ? -29.227 13.713  3.732   1.00 21.69 ? 196 GLY   A C    1 
ATOM   1370 O  O    . GLY   A 1 217 ? -29.203 12.948  2.769   1.00 23.52 ? 196 GLY   A O    1 
ATOM   1371 N  N    . ILE   A 1 218 ? -28.883 13.341  4.970   1.00 16.88 ? 197 ILE   A N    1 
ATOM   1372 C  CA   . ILE   A 1 218 ? -28.483 11.962  5.227   1.00 15.61 ? 197 ILE   A CA   1 
ATOM   1373 C  C    . ILE   A 1 218 ? -29.684 11.206  5.789   1.00 15.86 ? 197 ILE   A C    1 
ATOM   1374 O  O    . ILE   A 1 218 ? -30.159 11.551  6.867   1.00 17.16 ? 197 ILE   A O    1 
ATOM   1375 C  CB   . ILE   A 1 218 ? -27.301 11.865  6.211   1.00 15.68 ? 197 ILE   A CB   1 
ATOM   1376 C  CG1  . ILE   A 1 218 ? -26.065 12.637  5.699   1.00 17.14 ? 197 ILE   A CG1  1 
ATOM   1377 C  CG2  . ILE   A 1 218 ? -26.952 10.393  6.472   1.00 17.32 ? 197 ILE   A CG2  1 
ATOM   1378 C  CD1  . ILE   A 1 218 ? -25.024 12.861  6.789   1.00 18.30 ? 197 ILE   A CD1  1 
ATOM   1379 N  N    . ARG   A 1 219 ? -30.147 10.186  5.050   1.00 14.33 ? 198 ARG   A N    1 
ATOM   1380 C  CA   . ARG   A 1 219 ? -31.267 9.372   5.520   1.00 14.74 ? 198 ARG   A CA   1 
ATOM   1381 C  C    . ARG   A 1 219 ? -30.712 8.252   6.391   1.00 15.31 ? 198 ARG   A C    1 
ATOM   1382 O  O    . ARG   A 1 219 ? -29.582 7.810   6.169   1.00 15.36 ? 198 ARG   A O    1 
ATOM   1383 C  CB   . ARG   A 1 219 ? -32.063 8.810   4.334   1.00 14.17 ? 198 ARG   A CB   1 
ATOM   1384 C  CG   . ARG   A 1 219 ? -32.686 9.941   3.526   1.00 14.27 ? 198 ARG   A CG   1 
ATOM   1385 C  CD   . ARG   A 1 219 ? -33.453 9.437   2.303   1.00 14.67 ? 198 ARG   A CD   1 
ATOM   1386 N  NE   . ARG   A 1 219 ? -32.584 8.674   1.395   1.00 15.36 ? 198 ARG   A NE   1 
ATOM   1387 C  CZ   . ARG   A 1 219 ? -32.539 7.353   1.316   1.00 15.75 ? 198 ARG   A CZ   1 
ATOM   1388 N  NH1  . ARG   A 1 219 ? -33.381 6.611   2.044   1.00 15.61 ? 198 ARG   A NH1  1 
ATOM   1389 N  NH2  . ARG   A 1 219 ? -31.618 6.807   0.540   1.00 17.06 ? 198 ARG   A NH2  1 
ATOM   1390 N  N    . VAL   A 1 220 ? -31.487 7.854   7.413   1.00 13.08 ? 199 VAL   A N    1 
ATOM   1391 C  CA   . VAL   A 1 220 ? -31.044 6.802   8.322   1.00 12.51 ? 199 VAL   A CA   1 
ATOM   1392 C  C    . VAL   A 1 220 ? -32.208 5.848   8.516   1.00 12.44 ? 199 VAL   A C    1 
ATOM   1393 O  O    . VAL   A 1 220 ? -33.245 6.240   9.038   1.00 13.21 ? 199 VAL   A O    1 
ATOM   1394 C  CB   . VAL   A 1 220 ? -30.583 7.335   9.695   1.00 12.69 ? 199 VAL   A CB   1 
ATOM   1395 C  CG1  . VAL   A 1 220 ? -30.003 6.232   10.577  1.00 14.19 ? 199 VAL   A CG1  1 
ATOM   1396 C  CG2  . VAL   A 1 220 ? -29.557 8.463   9.554   1.00 14.30 ? 199 VAL   A CG2  1 
ATOM   1397 N  N    . ASN   A 1 221 ? -32.003 4.583   8.138   1.00 12.10 ? 200 ASN   A N    1 
ATOM   1398 C  CA   . ASN   A 1 221 ? -33.087 3.605   8.143   1.00 12.65 ? 200 ASN   A CA   1 
ATOM   1399 C  C    . ASN   A 1 221 ? -32.552 2.281   8.661   1.00 13.54 ? 200 ASN   A C    1 
ATOM   1400 O  O    . ASN   A 1 221 ? -31.345 2.120   8.858   1.00 13.94 ? 200 ASN   A O    1 
ATOM   1401 C  CB   . ASN   A 1 221 ? -33.668 3.407   6.741   1.00 12.43 ? 200 ASN   A CB   1 
ATOM   1402 C  CG   . ASN   A 1 221 ? -34.365 4.673   6.280   1.00 12.94 ? 200 ASN   A CG   1 
ATOM   1403 O  OD1  . ASN   A 1 221 ? -35.401 5.065   6.834   1.00 13.19 ? 200 ASN   A OD1  1 
ATOM   1404 N  ND2  . ASN   A 1 221 ? -33.812 5.298   5.257   1.00 13.53 ? 200 ASN   A ND2  1 
ATOM   1405 N  N    . GLY   A 1 222 ? -33.483 1.358   8.912   1.00 13.19 ? 201 GLY   A N    1 
ATOM   1406 C  CA   . GLY   A 1 222 ? -33.111 0.020   9.357   1.00 13.13 ? 201 GLY   A CA   1 
ATOM   1407 C  C    . GLY   A 1 222 ? -33.773 -1.079  8.536   1.00 13.46 ? 201 GLY   A C    1 
ATOM   1408 O  O    . GLY   A 1 222 ? -34.835 -0.874  7.939   1.00 13.52 ? 201 GLY   A O    1 
ATOM   1409 N  N    . VAL   A 1 223 ? -33.139 -2.259  8.560   1.00 13.18 ? 202 VAL   A N    1 
ATOM   1410 C  CA   . VAL   A 1 223 ? -33.721 -3.474  8.020   1.00 12.23 ? 202 VAL   A CA   1 
ATOM   1411 C  C    . VAL   A 1 223 ? -33.678 -4.486  9.152   1.00 12.50 ? 202 VAL   A C    1 
ATOM   1412 O  O    . VAL   A 1 223 ? -32.622 -4.647  9.760   1.00 13.70 ? 202 VAL   A O    1 
ATOM   1413 C  CB   . VAL   A 1 223 ? -32.893 -3.987  6.830   1.00 12.55 ? 202 VAL   A CB   1 
ATOM   1414 C  CG1  . VAL   A 1 223 ? -33.323 -5.387  6.410   1.00 13.86 ? 202 VAL   A CG1  1 
ATOM   1415 C  CG2  . VAL   A 1 223 ? -33.038 -3.063  5.639   1.00 13.20 ? 202 VAL   A CG2  1 
ATOM   1416 N  N    . ALA   A 1 224 ? -34.843 -5.086  9.440   1.00 13.27 ? 203 ALA   A N    1 
ATOM   1417 C  CA   . ALA   A 1 224 ? -34.960 -5.975  10.588  1.00 12.46 ? 203 ALA   A CA   1 
ATOM   1418 C  C    . ALA   A 1 224 ? -35.284 -7.382  10.108  1.00 13.55 ? 203 ALA   A C    1 
ATOM   1419 O  O    . ALA   A 1 224 ? -36.459 -7.689  9.871   1.00 13.95 ? 203 ALA   A O    1 
ATOM   1420 C  CB   . ALA   A 1 224 ? -36.057 -5.460  11.507  1.00 12.75 ? 203 ALA   A CB   1 
ATOM   1421 N  N    . PRO   A 1 225 ? -34.283 -8.263  9.951   1.00 13.34 ? 204 PRO   A N    1 
ATOM   1422 C  CA   . PRO   A 1 225 ? -34.576 -9.654  9.619   1.00 13.81 ? 204 PRO   A CA   1 
ATOM   1423 C  C    . PRO   A 1 225 ? -35.287 -10.293 10.796  1.00 15.64 ? 204 PRO   A C    1 
ATOM   1424 O  O    . PRO   A 1 225 ? -35.106 -9.872  11.939  1.00 14.03 ? 204 PRO   A O    1 
ATOM   1425 C  CB   . PRO   A 1 225 ? -33.170 -10.253 9.479   1.00 15.65 ? 204 PRO   A CB   1 
ATOM   1426 C  CG   . PRO   A 1 225 ? -32.279 -9.078  9.189   1.00 15.22 ? 204 PRO   A CG   1 
ATOM   1427 C  CD   . PRO   A 1 225 ? -32.842 -7.991  10.079  1.00 13.84 ? 204 PRO   A CD   1 
ATOM   1428 N  N    . GLY   A 1 226 ? -35.994 -11.387 10.489  1.00 15.59 ? 205 GLY   A N    1 
ATOM   1429 C  CA   . GLY   A 1 226 ? -36.470 -12.309 11.504  1.00 17.64 ? 205 GLY   A CA   1 
ATOM   1430 C  C    . GLY   A 1 226 ? -35.458 -13.439 11.630  1.00 18.32 ? 205 GLY   A C    1 
ATOM   1431 O  O    . GLY   A 1 226 ? -34.486 -13.316 12.370  1.00 20.68 ? 205 GLY   A O    1 
ATOM   1432 N  N    . VAL   A 1 227 ? -35.751 -14.570 10.990  1.00 16.71 ? 206 VAL   A N    1 
ATOM   1433 C  CA   . VAL   A 1 227 ? -34.700 -15.547 10.819  1.00 17.27 ? 206 VAL   A CA   1 
ATOM   1434 C  C    . VAL   A 1 227 ? -34.242 -15.504 9.366   1.00 16.44 ? 206 VAL   A C    1 
ATOM   1435 O  O    . VAL   A 1 227 ? -35.037 -15.573 8.432   1.00 16.88 ? 206 VAL   A O    1 
ATOM   1436 C  CB   . VAL   A 1 227 ? -35.108 -16.960 11.276  1.00 20.99 ? 206 VAL   A CB   1 
ATOM   1437 C  CG1  . VAL   A 1 227 ? -35.404 -16.970 12.766  1.00 23.80 ? 206 VAL   A CG1  1 
ATOM   1438 C  CG2  . VAL   A 1 227 ? -36.307 -17.484 10.519  1.00 21.35 ? 206 VAL   A CG2  1 
ATOM   1439 N  N    . SER   A 1 228 ? -32.933 -15.305 9.218   1.00 16.67 ? 207 SER   A N    1 
ATOM   1440 C  CA   . SER   A 1 228 ? -32.265 -15.385 7.938   1.00 17.58 ? 207 SER   A CA   1 
ATOM   1441 C  C    . SER   A 1 228 ? -31.225 -16.482 8.093   1.00 18.73 ? 207 SER   A C    1 
ATOM   1442 O  O    . SER   A 1 228 ? -31.522 -17.493 8.723   1.00 18.92 ? 207 SER   A O    1 
ATOM   1443 C  CB   . SER   A 1 228 ? -31.654 -14.043 7.549   1.00 17.90 ? 207 SER   A CB   1 
ATOM   1444 O  OG   . SER   A 1 228 ? -31.052 -14.113 6.264   1.00 19.70 ? 207 SER   A OG   1 
ATOM   1445 N  N    . LEU   A 1 229 ? -29.993 -16.257 7.620   1.00 19.03 ? 208 LEU   A N    1 
ATOM   1446 C  CA   . LEU   A 1 229 ? -29.008 -17.331 7.699   1.00 19.22 ? 208 LEU   A CA   1 
ATOM   1447 C  C    . LEU   A 1 229 ? -28.825 -17.768 9.149   1.00 19.42 ? 208 LEU   A C    1 
ATOM   1448 O  O    . LEU   A 1 229 ? -28.485 -16.967 10.020  1.00 18.54 ? 208 LEU   A O    1 
ATOM   1449 C  CB   . LEU   A 1 229 ? -27.676 -16.881 7.101   1.00 21.45 ? 208 LEU   A CB   1 
ATOM   1450 C  CG   . LEU   A 1 229 ? -27.707 -16.501 5.623   1.00 24.83 ? 208 LEU   A CG   1 
ATOM   1451 C  CD1  . LEU   A 1 229 ? -26.311 -16.084 5.167   1.00 24.13 ? 208 LEU   A CD1  1 
ATOM   1452 C  CD2  . LEU   A 1 229 ? -28.228 -17.686 4.812   1.00 29.01 ? 208 LEU   A CD2  1 
ATOM   1453 N  N    . LEU   A 1 230 ? -29.063 -19.066 9.406   1.00 19.07 ? 209 LEU   A N    1 
ATOM   1454 C  CA   . LEU   A 1 230 ? -29.010 -19.580 10.759  1.00 20.97 ? 209 LEU   A CA   1 
ATOM   1455 C  C    . LEU   A 1 230 ? -27.550 -19.723 11.181  1.00 22.43 ? 209 LEU   A C    1 
ATOM   1456 O  O    . LEU   A 1 230 ? -26.648 -19.802 10.330  1.00 21.98 ? 209 LEU   A O    1 
ATOM   1457 C  CB   . LEU   A 1 230 ? -29.763 -20.912 10.833  1.00 22.39 ? 209 LEU   A CB   1 
ATOM   1458 C  CG   . LEU   A 1 230 ? -31.280 -20.889 11.088  1.00 26.85 ? 209 LEU   A CG   1 
ATOM   1459 C  CD1  . LEU   A 1 230 ? -31.886 -19.751 11.921  1.00 27.47 ? 209 LEU   A CD1  1 
ATOM   1460 C  CD2  . LEU   A 1 230 ? -32.139 -21.229 9.874   1.00 27.20 ? 209 LEU   A CD2  1 
ATOM   1461 N  N    . PRO   A 1 231 ? -27.279 -19.788 12.504  1.00 24.52 ? 210 PRO   A N    1 
ATOM   1462 C  CA   . PRO   A 1 231 ? -25.902 -19.814 13.002  1.00 25.27 ? 210 PRO   A CA   1 
ATOM   1463 C  C    . PRO   A 1 231 ? -25.172 -21.029 12.431  1.00 26.18 ? 210 PRO   A C    1 
ATOM   1464 O  O    . PRO   A 1 231 ? -25.769 -22.090 12.264  1.00 26.16 ? 210 PRO   A O    1 
ATOM   1465 C  CB   . PRO   A 1 231 ? -26.078 -19.904 14.525  1.00 26.54 ? 210 PRO   A CB   1 
ATOM   1466 C  CG   . PRO   A 1 231 ? -27.483 -19.386 14.785  1.00 25.32 ? 210 PRO   A CG   1 
ATOM   1467 C  CD   . PRO   A 1 231 ? -28.280 -19.871 13.586  1.00 24.65 ? 210 PRO   A CD   1 
ATOM   1468 N  N    . VAL   A 1 232 ? -23.880 -20.851 12.138  1.00 26.46 ? 211 VAL   A N    1 
ATOM   1469 C  CA   . VAL   A 1 232 ? -23.050 -21.922 11.603  1.00 29.41 ? 211 VAL   A CA   1 
ATOM   1470 C  C    . VAL   A 1 232 ? -23.067 -23.137 12.534  1.00 29.64 ? 211 VAL   A C    1 
ATOM   1471 O  O    . VAL   A 1 232 ? -23.042 -24.269 12.054  1.00 31.05 ? 211 VAL   A O    1 
ATOM   1472 C  CB   . VAL   A 1 232 ? -21.609 -21.458 11.296  1.00 31.88 ? 211 VAL   A CB   1 
ATOM   1473 C  CG1  . VAL   A 1 232 ? -21.581 -20.319 10.283  1.00 33.95 ? 211 VAL   A CG1  1 
ATOM   1474 C  CG2  . VAL   A 1 232 ? -20.849 -21.046 12.551  1.00 35.28 ? 211 VAL   A CG2  1 
ATOM   1475 N  N    . ALA   A 1 233 ? -23.149 -22.899 13.852  1.00 30.10 ? 212 ALA   A N    1 
ATOM   1476 C  CA   . ALA   A 1 233 ? -23.032 -23.956 14.849  1.00 32.21 ? 212 ALA   A CA   1 
ATOM   1477 C  C    . ALA   A 1 233 ? -24.325 -24.761 14.966  1.00 32.94 ? 212 ALA   A C    1 
ATOM   1478 O  O    . ALA   A 1 233 ? -24.337 -25.812 15.607  1.00 34.06 ? 212 ALA   A O    1 
ATOM   1479 C  CB   . ALA   A 1 233 ? -22.647 -23.370 16.196  1.00 35.03 ? 212 ALA   A CB   1 
ATOM   1480 N  N    . MET   A 1 234 ? -25.421 -24.259 14.378  1.00 27.65 ? 213 MET   A N    1 
ATOM   1481 C  CA   . MET   A 1 234 ? -26.719 -24.843 14.681  1.00 27.08 ? 213 MET   A CA   1 
ATOM   1482 C  C    . MET   A 1 234 ? -26.905 -26.110 13.854  1.00 26.02 ? 213 MET   A C    1 
ATOM   1483 O  O    . MET   A 1 234 ? -26.595 -26.104 12.672  1.00 27.95 ? 213 MET   A O    1 
ATOM   1484 C  CB   . MET   A 1 234 ? -27.848 -23.851 14.376  1.00 25.62 ? 213 MET   A CB   1 
ATOM   1485 C  CG   . MET   A 1 234 ? -29.216 -24.357 14.756  1.00 24.80 ? 213 MET   A CG   1 
ATOM   1486 S  SD   . MET   A 1 234 ? -30.455 -23.056 14.572  1.00 26.09 ? 213 MET   A SD   1 
ATOM   1487 C  CE   . MET   A 1 234 ? -30.195 -22.129 16.094  1.00 26.33 ? 213 MET   A CE   1 
ATOM   1488 N  N    . GLY   A 1 235 ? -27.420 -27.173 14.483  1.00 26.85 ? 214 GLY   A N    1 
ATOM   1489 C  CA   . GLY   A 1 235 ? -27.734 -28.413 13.780  1.00 26.92 ? 214 GLY   A CA   1 
ATOM   1490 C  C    . GLY   A 1 235 ? -28.969 -28.235 12.899  1.00 26.37 ? 214 GLY   A C    1 
ATOM   1491 O  O    . GLY   A 1 235 ? -29.784 -27.350 13.150  1.00 24.09 ? 214 GLY   A O    1 
ATOM   1492 N  N    . GLU   A 1 236 ? -29.116 -29.102 11.889  1.00 24.40 ? 215 GLU   A N    1 
ATOM   1493 C  CA   . GLU   A 1 236 ? -30.203 -28.989 10.929  1.00 23.06 ? 215 GLU   A CA   1 
ATOM   1494 C  C    . GLU   A 1 236 ? -31.566 -29.163 11.605  1.00 23.00 ? 215 GLU   A C    1 
ATOM   1495 O  O    . GLU   A 1 236 ? -32.556 -28.545 11.202  1.00 22.37 ? 215 GLU   A O    1 
ATOM   1496 C  CB   . GLU   A 1 236 ? -29.982 -30.008 9.809   1.00 24.34 ? 215 GLU   A CB   1 
ATOM   1497 C  CG   . GLU   A 1 236 ? -30.953 -29.845 8.643   1.00 25.50 ? 215 GLU   A CG   1 
ATOM   1498 C  CD   . GLU   A 1 236 ? -30.689 -28.656 7.739   1.00 28.06 ? 215 GLU   A CD   1 
ATOM   1499 O  OE1  . GLU   A 1 236 ? -29.605 -28.040 7.775   1.00 32.35 ? 215 GLU   A OE1  1 
ATOM   1500 O  OE2  . GLU   A 1 236 ? -31.610 -28.375 6.954   1.00 31.08 ? 215 GLU   A OE2  1 
ATOM   1501 N  N    . GLU   A 1 237 ? -31.639 -30.033 12.618  1.00 25.20 ? 216 GLU   A N    1 
ATOM   1502 C  CA   . GLU   A 1 237 ? -32.912 -30.276 13.275  1.00 25.78 ? 216 GLU   A CA   1 
ATOM   1503 C  C    . GLU   A 1 237 ? -33.391 -28.989 13.953  1.00 23.84 ? 216 GLU   A C    1 
ATOM   1504 O  O    . GLU   A 1 237 ? -34.566 -28.634 13.854  1.00 24.80 ? 216 GLU   A O    1 
ATOM   1505 C  CB   . GLU   A 1 237 ? -32.809 -31.473 14.224  1.00 29.32 ? 216 GLU   A CB   1 
ATOM   1506 C  CG   . GLU   A 1 237 ? -33.906 -31.486 15.282  1.00 31.13 ? 216 GLU   A CG   1 
ATOM   1507 N  N    . GLU   A 1 238 ? -32.451 -28.273 14.576  1.00 24.77 ? 217 GLU   A N    1 
ATOM   1508 C  CA   . GLU   A 1 238 ? -32.762 -27.039 15.281  1.00 23.64 ? 217 GLU   A CA   1 
ATOM   1509 C  C    . GLU   A 1 238 ? -33.087 -25.950 14.261  1.00 22.04 ? 217 GLU   A C    1 
ATOM   1510 O  O    . GLU   A 1 238 ? -34.024 -25.180 14.453  1.00 21.07 ? 217 GLU   A O    1 
ATOM   1511 C  CB   . GLU   A 1 238 ? -31.600 -26.632 16.189  1.00 26.18 ? 217 GLU   A CB   1 
ATOM   1512 C  CG   . GLU   A 1 238 ? -31.942 -25.440 17.083  1.00 29.47 ? 217 GLU   A CG   1 
ATOM   1513 C  CD   . GLU   A 1 238 ? -30.910 -25.115 18.151  0.70 33.59 ? 217 GLU   A CD   1 
ATOM   1514 O  OE1  . GLU   A 1 238 ? -31.122 -24.119 18.879  0.70 34.43 ? 217 GLU   A OE1  1 
ATOM   1515 O  OE2  . GLU   A 1 238 ? -29.898 -25.843 18.264  0.70 33.99 ? 217 GLU   A OE2  1 
ATOM   1516 N  N    . LYS   A 1 239 ? -32.339 -25.923 13.150  1.00 20.80 ? 218 LYS   A N    1 
ATOM   1517 C  CA   . LYS   A 1 239 ? -32.679 -25.003 12.069  1.00 20.57 ? 218 LYS   A CA   1 
ATOM   1518 C  C    . LYS   A 1 239 ? -34.115 -25.207 11.584  1.00 20.22 ? 218 LYS   A C    1 
ATOM   1519 O  O    . LYS   A 1 239 ? -34.840 -24.240 11.343  1.00 19.16 ? 218 LYS   A O    1 
ATOM   1520 C  CB   . LYS   A 1 239 ? -31.751 -25.070 10.856  1.00 20.57 ? 218 LYS   A CB   1 
ATOM   1521 C  CG   . LYS   A 1 239 ? -30.321 -24.651 11.148  1.00 22.64 ? 218 LYS   A CG   1 
ATOM   1522 C  CD   . LYS   A 1 239 ? -29.455 -24.598 9.896   1.00 24.19 ? 218 LYS   A CD   1 
ATOM   1523 C  CE   . LYS   A 1 239 ? -28.026 -24.400 10.294  1.00 29.53 ? 218 LYS   A CE   1 
ATOM   1524 N  NZ   . LYS   A 1 239 ? -27.133 -24.687 9.167   1.00 33.59 ? 218 LYS   A NZ   1 
ATOM   1525 N  N    . ASP   A 1 240 ? -34.540 -26.463 11.407  1.00 19.23 ? 219 ASP   A N    1 
ATOM   1526 C  CA   . ASP   A 1 240 ? -35.877 -26.734 10.911  1.00 20.19 ? 219 ASP   A CA   1 
ATOM   1527 C  C    . ASP   A 1 240 ? -36.950 -26.282 11.901  1.00 20.32 ? 219 ASP   A C    1 
ATOM   1528 O  O    . ASP   A 1 240 ? -38.042 -25.899 11.479  1.00 21.26 ? 219 ASP   A O    1 
ATOM   1529 C  CB   . ASP   A 1 240 ? -36.056 -28.200 10.543  1.00 23.01 ? 219 ASP   A CB   1 
ATOM   1530 C  CG   . ASP   A 1 240 ? -35.401 -28.614 9.232   1.00 27.72 ? 219 ASP   A CG   1 
ATOM   1531 O  OD1  . ASP   A 1 240 ? -35.093 -27.724 8.411   1.00 28.81 ? 219 ASP   A OD1  1 
ATOM   1532 O  OD2  . ASP   A 1 240 ? -35.188 -29.826 9.050   1.00 31.00 ? 219 ASP   A OD2  1 
ATOM   1533 N  N    . LYS   A 1 241 ? -36.644 -26.341 13.209  1.00 20.32 ? 220 LYS   A N    1 
ATOM   1534 C  CA   A LYS   A 1 241 ? -37.583 -25.889 14.225  0.50 20.55 ? 220 LYS   A CA   1 
ATOM   1535 C  CA   B LYS   A 1 241 ? -37.606 -25.897 14.205  0.50 20.92 ? 220 LYS   A CA   1 
ATOM   1536 C  C    . LYS   A 1 241 ? -37.893 -24.410 13.998  1.00 20.59 ? 220 LYS   A C    1 
ATOM   1537 O  O    . LYS   A 1 241 ? -39.049 -23.993 14.113  1.00 22.65 ? 220 LYS   A O    1 
ATOM   1538 C  CB   A LYS   A 1 241 ? -37.023 -26.050 15.642  0.50 20.97 ? 220 LYS   A CB   1 
ATOM   1539 C  CB   B LYS   A 1 241 ? -37.164 -26.257 15.628  0.50 22.27 ? 220 LYS   A CB   1 
ATOM   1540 C  CG   A LYS   A 1 241 ? -38.005 -25.744 16.764  0.30 21.38 ? 220 LYS   A CG   1 
ATOM   1541 C  CG   B LYS   A 1 241 ? -37.067 -27.761 15.847  0.30 22.48 ? 220 LYS   A CG   1 
ATOM   1542 C  CD   A LYS   A 1 241 ? -37.348 -25.908 18.128  0.30 21.95 ? 220 LYS   A CD   1 
ATOM   1543 C  CD   B LYS   A 1 241 ? -36.718 -28.192 17.265  0.30 24.23 ? 220 LYS   A CD   1 
ATOM   1544 C  CE   A LYS   A 1 241 ? -36.145 -25.028 18.262  0.30 21.51 ? 220 LYS   A CE   1 
ATOM   1545 C  CE   B LYS   A 1 241 ? -36.620 -29.684 17.328  0.30 24.75 ? 220 LYS   A CE   1 
ATOM   1546 N  NZ   A LYS   A 1 241 ? -36.530 -23.614 18.280  0.30 22.22 ? 220 LYS   A NZ   1 
ATOM   1547 N  NZ   B LYS   A 1 241 ? -36.100 -30.146 18.616  0.30 26.19 ? 220 LYS   A NZ   1 
ATOM   1548 N  N    . TRP   A 1 242 ? -36.850 -23.644 13.687  1.00 19.88 ? 221 TRP   A N    1 
ATOM   1549 C  CA   . TRP   A 1 242 ? -37.004 -22.212 13.432  1.00 18.79 ? 221 TRP   A CA   1 
ATOM   1550 C  C    . TRP   A 1 242 ? -37.728 -21.968 12.111  1.00 19.77 ? 221 TRP   A C    1 
ATOM   1551 O  O    . TRP   A 1 242 ? -38.664 -21.171 12.034  1.00 19.86 ? 221 TRP   A O    1 
ATOM   1552 C  CB   . TRP   A 1 242 ? -35.655 -21.499 13.507  1.00 21.48 ? 221 TRP   A CB   1 
ATOM   1553 C  CG   . TRP   A 1 242 ? -35.274 -21.264 14.944  1.00 22.46 ? 221 TRP   A CG   1 
ATOM   1554 C  CD1  . TRP   A 1 242 ? -34.493 -22.047 15.741  1.00 24.33 ? 221 TRP   A CD1  1 
ATOM   1555 C  CD2  . TRP   A 1 242 ? -35.764 -20.193 15.780  1.00 25.47 ? 221 TRP   A CD2  1 
ATOM   1556 N  NE1  . TRP   A 1 242 ? -34.429 -21.522 17.009  1.00 26.47 ? 221 TRP   A NE1  1 
ATOM   1557 C  CE2  . TRP   A 1 242 ? -35.203 -20.387 17.059  1.00 25.92 ? 221 TRP   A CE2  1 
ATOM   1558 C  CE3  . TRP   A 1 242 ? -36.606 -19.095 15.561  1.00 25.94 ? 221 TRP   A CE3  1 
ATOM   1559 C  CZ2  . TRP   A 1 242 ? -35.465 -19.518 18.120  1.00 26.26 ? 221 TRP   A CZ2  1 
ATOM   1560 C  CZ3  . TRP   A 1 242 ? -36.867 -18.237 16.612  1.00 27.06 ? 221 TRP   A CZ3  1 
ATOM   1561 C  CH2  . TRP   A 1 242 ? -36.308 -18.456 17.872  1.00 25.92 ? 221 TRP   A CH2  1 
ATOM   1562 N  N    . ARG   A 1 243 ? -37.343 -22.719 11.076  1.00 17.21 ? 222 ARG   A N    1 
ATOM   1563 C  CA   . ARG   A 1 243 ? -37.967 -22.569 9.769   1.00 16.95 ? 222 ARG   A CA   1 
ATOM   1564 C  C    . ARG   A 1 243 ? -39.478 -22.793 9.830   1.00 17.76 ? 222 ARG   A C    1 
ATOM   1565 O  O    . ARG   A 1 243 ? -40.231 -22.067 9.187   1.00 19.71 ? 222 ARG   A O    1 
ATOM   1566 C  CB   . ARG   A 1 243 ? -37.338 -23.533 8.748   1.00 15.96 ? 222 ARG   A CB   1 
ATOM   1567 C  CG   . ARG   A 1 243 ? -35.920 -23.111 8.389   1.00 17.27 ? 222 ARG   A CG   1 
ATOM   1568 C  CD   . ARG   A 1 243 ? -35.290 -24.325 7.687   1.00 17.34 ? 222 ARG   A CD   1 
ATOM   1569 N  NE   . ARG   A 1 243 ? -33.969 -23.972 7.184   1.00 18.50 ? 222 ARG   A NE   1 
ATOM   1570 C  CZ   . ARG   A 1 243 ? -32.906 -24.754 7.111   1.00 18.49 ? 222 ARG   A CZ   1 
ATOM   1571 N  NH1  . ARG   A 1 243 ? -33.000 -26.014 7.513   1.00 21.89 ? 222 ARG   A NH1  1 
ATOM   1572 N  NH2  . ARG   A 1 243 ? -31.785 -24.256 6.612   1.00 20.66 ? 222 ARG   A NH2  1 
ATOM   1573 N  N    . ARG   A 1 244 ? -39.921 -23.796 10.599  1.00 17.97 ? 223 ARG   A N    1 
ATOM   1574 C  CA   . ARG   A 1 244 ? -41.326 -24.177 10.628  1.00 18.89 ? 223 ARG   A CA   1 
ATOM   1575 C  C    . ARG   A 1 244 ? -42.200 -23.115 11.294  1.00 19.58 ? 223 ARG   A C    1 
ATOM   1576 O  O    . ARG   A 1 244 ? -43.419 -23.221 11.238  1.00 21.91 ? 223 ARG   A O    1 
ATOM   1577 C  CB   . ARG   A 1 244 ? -41.549 -25.548 11.284  1.00 23.31 ? 223 ARG   A CB   1 
ATOM   1578 C  CG   . ARG   A 1 244 ? -41.192 -26.642 10.291  0.60 26.74 ? 223 ARG   A CG   1 
ATOM   1579 C  CD   . ARG   A 1 244 ? -41.614 -28.018 10.770  0.60 29.91 ? 223 ARG   A CD   1 
ATOM   1580 N  NE   . ARG   A 1 244 ? -40.927 -28.289 12.036  0.60 33.26 ? 223 ARG   A NE   1 
ATOM   1581 C  CZ   . ARG   A 1 244 ? -39.828 -29.032 12.160  0.60 33.57 ? 223 ARG   A CZ   1 
ATOM   1582 N  NH1  . ARG   A 1 244 ? -39.320 -29.664 11.115  0.60 34.54 ? 223 ARG   A NH1  1 
ATOM   1583 N  NH2  . ARG   A 1 244 ? -39.243 -29.136 13.338  0.60 33.15 ? 223 ARG   A NH2  1 
ATOM   1584 N  N    . LYS   A 1 245 ? -41.577 -22.125 11.942  1.00 19.17 ? 224 LYS   A N    1 
ATOM   1585 C  CA   . LYS   A 1 245 ? -42.334 -21.085 12.632  1.00 19.16 ? 224 LYS   A CA   1 
ATOM   1586 C  C    . LYS   A 1 245 ? -42.703 -19.950 11.672  1.00 18.76 ? 224 LYS   A C    1 
ATOM   1587 O  O    . LYS   A 1 245 ? -43.570 -19.142 11.999  1.00 18.60 ? 224 LYS   A O    1 
ATOM   1588 C  CB   . LYS   A 1 245 ? -41.503 -20.460 13.758  1.00 19.99 ? 224 LYS   A CB   1 
ATOM   1589 C  CG   . LYS   A 1 245 ? -41.031 -21.367 14.916  1.00 23.33 ? 224 LYS   A CG   1 
ATOM   1590 C  CD   . LYS   A 1 245 ? -40.007 -20.582 15.734  1.00 25.02 ? 224 LYS   A CD   1 
ATOM   1591 C  CE   . LYS   A 1 245 ? -39.257 -21.297 16.837  1.00 28.53 ? 224 LYS   A CE   1 
ATOM   1592 N  NZ   . LYS   A 1 245 ? -40.146 -21.921 17.824  1.00 28.74 ? 224 LYS   A NZ   1 
ATOM   1593 N  N    . VAL   A 1 246 ? -42.039 -19.877 10.516  1.00 16.46 ? 225 VAL   A N    1 
ATOM   1594 C  CA   . VAL   A 1 246 ? -42.209 -18.730 9.622   1.00 16.21 ? 225 VAL   A CA   1 
ATOM   1595 C  C    . VAL   A 1 246 ? -43.463 -18.924 8.771   1.00 16.58 ? 225 VAL   A C    1 
ATOM   1596 O  O    . VAL   A 1 246 ? -43.525 -19.831 7.935   1.00 16.54 ? 225 VAL   A O    1 
ATOM   1597 C  CB   . VAL   A 1 246 ? -40.987 -18.540 8.707   1.00 15.11 ? 225 VAL   A CB   1 
ATOM   1598 C  CG1  . VAL   A 1 246 ? -41.197 -17.374 7.729   1.00 15.21 ? 225 VAL   A CG1  1 
ATOM   1599 C  CG2  . VAL   A 1 246 ? -39.675 -18.388 9.483   1.00 16.03 ? 225 VAL   A CG2  1 
ATOM   1600 N  N    . PRO   A 1 247 ? -44.508 -18.069 8.882   1.00 15.50 ? 226 PRO   A N    1 
ATOM   1601 C  CA   . PRO   A 1 247 ? -45.704 -18.226 8.042   1.00 15.53 ? 226 PRO   A CA   1 
ATOM   1602 C  C    . PRO   A 1 247 ? -45.473 -18.270 6.535   1.00 16.10 ? 226 PRO   A C    1 
ATOM   1603 O  O    . PRO   A 1 247 ? -46.119 -19.035 5.821   1.00 16.91 ? 226 PRO   A O    1 
ATOM   1604 C  CB   . PRO   A 1 247 ? -46.530 -16.949 8.405   1.00 16.39 ? 226 PRO   A CB   1 
ATOM   1605 C  CG   . PRO   A 1 247 ? -46.085 -16.622 9.804   1.00 15.42 ? 226 PRO   A CG   1 
ATOM   1606 C  CD   . PRO   A 1 247 ? -44.584 -16.927 9.822   1.00 15.69 ? 226 PRO   A CD   1 
ATOM   1607 N  N    . LEU   A 1 248 ? -44.624 -17.352 6.045   1.00 15.62 ? 227 LEU   A N    1 
ATOM   1608 C  CA   . LEU   A 1 248 ? -44.459 -17.209 4.605   1.00 15.34 ? 227 LEU   A CA   1 
ATOM   1609 C  C    . LEU   A 1 248 ? -43.387 -18.173 4.113   1.00 16.93 ? 227 LEU   A C    1 
ATOM   1610 O  O    . LEU   A 1 248 ? -42.209 -17.834 3.986   1.00 18.94 ? 227 LEU   A O    1 
ATOM   1611 C  CB   . LEU   A 1 248 ? -44.107 -15.755 4.267   1.00 15.84 ? 227 LEU   A CB   1 
ATOM   1612 C  CG   . LEU   A 1 248 ? -44.207 -15.415 2.774   1.00 16.64 ? 227 LEU   A CG   1 
ATOM   1613 C  CD1  . LEU   A 1 248 ? -45.645 -15.414 2.242   1.00 18.15 ? 227 LEU   A CD1  1 
ATOM   1614 C  CD2  . LEU   A 1 248 ? -43.528 -14.077 2.534   1.00 17.17 ? 227 LEU   A CD2  1 
ATOM   1615 N  N    . GLY   A 1 249 ? -43.816 -19.408 3.860   1.00 18.24 ? 228 GLY   A N    1 
ATOM   1616 C  CA   . GLY   A 1 249 ? -42.966 -20.386 3.204   1.00 18.21 ? 228 GLY   A CA   1 
ATOM   1617 C  C    . GLY   A 1 249 ? -42.212 -21.320 4.145   1.00 18.50 ? 228 GLY   A C    1 
ATOM   1618 O  O    . GLY   A 1 249 ? -41.483 -22.172 3.649   1.00 19.06 ? 228 GLY   A O    1 
ATOM   1619 N  N    . ARG   A 1 250 ? -42.317 -21.135 5.474   1.00 17.57 ? 229 ARG   A N    1 
ATOM   1620 C  CA   . ARG   A 1 250 ? -41.669 -22.028 6.426   1.00 17.43 ? 229 ARG   A CA   1 
ATOM   1621 C  C    . ARG   A 1 250 ? -40.185 -22.185 6.102   1.00 17.36 ? 229 ARG   A C    1 
ATOM   1622 O  O    . ARG   A 1 250 ? -39.626 -23.288 6.146   1.00 17.33 ? 229 ARG   A O    1 
ATOM   1623 C  CB   . ARG   A 1 250 ? -42.358 -23.402 6.418   1.00 18.23 ? 229 ARG   A CB   1 
ATOM   1624 C  CG   . ARG   A 1 250 ? -43.859 -23.375 6.637   1.00 23.33 ? 229 ARG   A CG   1 
ATOM   1625 C  CD   . ARG   A 1 250 ? -44.202 -22.966 8.032   1.00 25.43 ? 229 ARG   A CD   1 
ATOM   1626 N  NE   . ARG   A 1 250 ? -45.640 -22.666 8.058   1.00 29.45 ? 229 ARG   A NE   1 
ATOM   1627 C  CZ   . ARG   A 1 250 ? -46.273 -22.053 9.053   1.00 31.67 ? 229 ARG   A CZ   1 
ATOM   1628 N  NH1  . ARG   A 1 250 ? -45.639 -21.766 10.179  1.00 30.21 ? 229 ARG   A NH1  1 
ATOM   1629 N  NH2  . ARG   A 1 250 ? -47.555 -21.746 8.922   1.00 34.52 ? 229 ARG   A NH2  1 
ATOM   1630 N  N    . ARG   A 1 251 ? -39.526 -21.045 5.855   1.00 15.50 ? 230 ARG   A N    1 
ATOM   1631 C  CA   A ARG   A 1 251 ? -38.106 -21.038 5.561   0.50 15.79 ? 230 ARG   A CA   1 
ATOM   1632 C  CA   B ARG   A 1 251 ? -38.107 -21.028 5.533   0.50 15.76 ? 230 ARG   A CA   1 
ATOM   1633 C  C    . ARG   A 1 251 ? -37.540 -19.694 6.001   1.00 15.57 ? 230 ARG   A C    1 
ATOM   1634 O  O    . ARG   A 1 251 ? -38.294 -18.730 6.148   1.00 16.49 ? 230 ARG   A O    1 
ATOM   1635 C  CB   A ARG   A 1 251 ? -37.872 -21.293 4.067   0.50 17.19 ? 230 ARG   A CB   1 
ATOM   1636 C  CB   B ARG   A 1 251 ? -37.863 -21.153 4.022   0.50 16.84 ? 230 ARG   A CB   1 
ATOM   1637 C  CG   A ARG   A 1 251 ? -38.453 -20.293 3.076   0.50 18.29 ? 230 ARG   A CG   1 
ATOM   1638 C  CG   B ARG   A 1 251 ? -36.451 -21.465 3.531   0.50 18.44 ? 230 ARG   A CG   1 
ATOM   1639 C  CD   A ARG   A 1 251 ? -38.259 -20.686 1.605   0.50 22.27 ? 230 ARG   A CD   1 
ATOM   1640 C  CD   B ARG   A 1 251 ? -35.996 -22.885 3.885   0.50 19.51 ? 230 ARG   A CD   1 
ATOM   1641 N  NE   A ARG   A 1 251 ? -36.828 -20.783 1.291   0.50 27.11 ? 230 ARG   A NE   1 
ATOM   1642 N  NE   B ARG   A 1 251 ? -34.663 -23.262 3.389   0.50 18.88 ? 230 ARG   A NE   1 
ATOM   1643 C  CZ   A ARG   A 1 251 ? -36.225 -21.624 0.452   0.50 29.65 ? 230 ARG   A CZ   1 
ATOM   1644 C  CZ   B ARG   A 1 251 ? -34.096 -24.465 3.468   0.50 22.98 ? 230 ARG   A CZ   1 
ATOM   1645 N  NH1  A ARG   A 1 251 ? -36.926 -22.342 -0.405  0.50 28.10 ? 230 ARG   A NH1  1 
ATOM   1646 N  NH1  B ARG   A 1 251 ? -34.698 -25.461 4.097   0.50 22.42 ? 230 ARG   A NH1  1 
ATOM   1647 N  NH2  A ARG   A 1 251 ? -34.904 -21.704 0.449   0.50 29.32 ? 230 ARG   A NH2  1 
ATOM   1648 N  NH2  B ARG   A 1 251 ? -32.916 -24.676 2.901   0.50 22.51 ? 230 ARG   A NH2  1 
ATOM   1649 N  N    . GLU   A 1 252 ? -36.226 -19.675 6.229   1.00 15.83 ? 231 GLU   A N    1 
ATOM   1650 C  CA   . GLU   A 1 252 ? -35.519 -18.470 6.632   1.00 16.51 ? 231 GLU   A CA   1 
ATOM   1651 C  C    . GLU   A 1 252 ? -35.316 -17.587 5.406   1.00 16.33 ? 231 GLU   A C    1 
ATOM   1652 O  O    . GLU   A 1 252 ? -35.333 -18.070 4.275   1.00 16.24 ? 231 GLU   A O    1 
ATOM   1653 C  CB   . GLU   A 1 252 ? -34.186 -18.841 7.297   1.00 16.70 ? 231 GLU   A CB   1 
ATOM   1654 C  CG   . GLU   A 1 252 ? -33.094 -19.353 6.348   1.00 18.51 ? 231 GLU   A CG   1 
ATOM   1655 C  CD   . GLU   A 1 252 ? -33.096 -20.847 6.059   1.00 20.29 ? 231 GLU   A CD   1 
ATOM   1656 O  OE1  . GLU   A 1 252 ? -31.983 -21.437 5.954   1.00 21.38 ? 231 GLU   A OE1  1 
ATOM   1657 O  OE2  . GLU   A 1 252 ? -34.199 -21.418 5.948   1.00 20.50 ? 231 GLU   A OE2  1 
ATOM   1658 N  N    . ALA   A 1 253 ? -35.098 -16.280 5.630   1.00 16.21 ? 232 ALA   A N    1 
ATOM   1659 C  CA   . ALA   A 1 253 ? -34.776 -15.388 4.526   1.00 16.78 ? 232 ALA   A CA   1 
ATOM   1660 C  C    . ALA   A 1 253 ? -33.393 -15.731 3.974   1.00 15.81 ? 232 ALA   A C    1 
ATOM   1661 O  O    . ALA   A 1 253 ? -32.459 -16.015 4.716   1.00 16.62 ? 232 ALA   A O    1 
ATOM   1662 C  CB   . ALA   A 1 253 ? -34.761 -13.944 5.016   1.00 16.86 ? 232 ALA   A CB   1 
ATOM   1663 N  N    . SER   A 1 254 ? -33.242 -15.650 2.661   1.00 14.96 ? 233 SER   A N    1 
ATOM   1664 C  CA   . SER   A 1 254 ? -31.896 -15.705 2.115   1.00 15.44 ? 233 SER   A CA   1 
ATOM   1665 C  C    . SER   A 1 254 ? -31.158 -14.409 2.403   1.00 16.39 ? 233 SER   A C    1 
ATOM   1666 O  O    . SER   A 1 254 ? -31.772 -13.369 2.693   1.00 17.45 ? 233 SER   A O    1 
ATOM   1667 C  CB   . SER   A 1 254 ? -31.918 -15.974 0.647   1.00 17.81 ? 233 SER   A CB   1 
ATOM   1668 O  OG   . SER   A 1 254 ? -32.427 -14.849 -0.046  1.00 19.00 ? 233 SER   A OG   1 
ATOM   1669 N  N    . ALA   A 1 255 ? -29.829 -14.501 2.344   1.00 15.04 ? 234 ALA   A N    1 
ATOM   1670 C  CA   . ALA   A 1 255 ? -29.044 -13.292 2.540   1.00 15.87 ? 234 ALA   A CA   1 
ATOM   1671 C  C    . ALA   A 1 255 ? -29.421 -12.263 1.485   1.00 15.04 ? 234 ALA   A C    1 
ATOM   1672 O  O    . ALA   A 1 255 ? -29.470 -11.061 1.797   1.00 15.29 ? 234 ALA   A O    1 
ATOM   1673 C  CB   . ALA   A 1 255 ? -27.560 -13.595 2.537   1.00 17.23 ? 234 ALA   A CB   1 
ATOM   1674 N  N    . GLU   A 1 256 ? -29.663 -12.705 0.242   1.00 15.25 ? 235 GLU   A N    1 
ATOM   1675 C  CA   . GLU   A 1 256 ? -30.030 -11.802 -0.840  1.00 16.64 ? 235 GLU   A CA   1 
ATOM   1676 C  C    . GLU   A 1 256 ? -31.340 -11.073 -0.534  1.00 16.20 ? 235 GLU   A C    1 
ATOM   1677 O  O    . GLU   A 1 256 ? -31.479 -9.898  -0.864  1.00 16.68 ? 235 GLU   A O    1 
ATOM   1678 C  CB   . GLU   A 1 256 ? -30.102 -12.575 -2.157  1.00 19.44 ? 235 GLU   A CB   1 
ATOM   1679 C  CG   . GLU   A 1 256 ? -30.458 -11.701 -3.356  1.00 25.33 ? 235 GLU   A CG   1 
ATOM   1680 C  CD   . GLU   A 1 256 ? -30.535 -12.416 -4.702  0.70 31.13 ? 235 GLU   A CD   1 
ATOM   1681 O  OE1  . GLU   A 1 256 ? -31.126 -11.841 -5.639  0.70 35.26 ? 235 GLU   A OE1  1 
ATOM   1682 O  OE2  . GLU   A 1 256 ? -29.987 -13.529 -4.835  0.70 37.78 ? 235 GLU   A OE2  1 
ATOM   1683 N  N    . GLN   A 1 257 ? -32.306 -11.747 0.098   1.00 15.64 ? 236 GLN   A N    1 
ATOM   1684 C  CA   . GLN   A 1 257 ? -33.567 -11.084 0.428   1.00 15.13 ? 236 GLN   A CA   1 
ATOM   1685 C  C    . GLN   A 1 257 ? -33.382 -9.939  1.421   1.00 15.52 ? 236 GLN   A C    1 
ATOM   1686 O  O    . GLN   A 1 257 ? -34.041 -8.892  1.306   1.00 15.42 ? 236 GLN   A O    1 
ATOM   1687 C  CB   . GLN   A 1 257 ? -34.559 -12.125 0.937   1.00 15.99 ? 236 GLN   A CB   1 
ATOM   1688 C  CG   . GLN   A 1 257 ? -35.066 -12.998 -0.205  1.00 16.03 ? 236 GLN   A CG   1 
ATOM   1689 C  CD   . GLN   A 1 257 ? -35.907 -14.165 0.254   1.00 18.16 ? 236 GLN   A CD   1 
ATOM   1690 O  OE1  . GLN   A 1 257 ? -35.657 -14.786 1.292   1.00 17.74 ? 236 GLN   A OE1  1 
ATOM   1691 N  NE2  . GLN   A 1 257 ? -36.898 -14.512 -0.561  1.00 21.03 ? 236 GLN   A NE2  1 
ATOM   1692 N  N    . ILE   A 1 258 ? -32.502 -10.145 2.400   1.00 14.12 ? 237 ILE   A N    1 
ATOM   1693 C  CA   . ILE   A 1 258 ? -32.171 -9.055  3.312   1.00 14.15 ? 237 ILE   A CA   1 
ATOM   1694 C  C    . ILE   A 1 258 ? -31.491 -7.930  2.533   1.00 14.18 ? 237 ILE   A C    1 
ATOM   1695 O  O    . ILE   A 1 258 ? -31.810 -6.743  2.703   1.00 13.96 ? 237 ILE   A O    1 
ATOM   1696 C  CB   . ILE   A 1 258 ? -31.312 -9.549  4.486   1.00 13.84 ? 237 ILE   A CB   1 
ATOM   1697 C  CG1  . ILE   A 1 258 ? -31.964 -10.702 5.263   1.00 14.66 ? 237 ILE   A CG1  1 
ATOM   1698 C  CG2  . ILE   A 1 258 ? -30.919 -8.389  5.415   1.00 14.33 ? 237 ILE   A CG2  1 
ATOM   1699 C  CD1  . ILE   A 1 258 ? -33.390 -10.443 5.713   1.00 15.43 ? 237 ILE   A CD1  1 
ATOM   1700 N  N    . ALA   A 1 259 ? -30.504 -8.287  1.705   1.00 14.17 ? 238 ALA   A N    1 
ATOM   1701 C  CA   . ALA   A 1 259 ? -29.775 -7.289  0.935   1.00 14.20 ? 238 ALA   A CA   1 
ATOM   1702 C  C    . ALA   A 1 259 ? -30.705 -6.488  0.019   1.00 14.87 ? 238 ALA   A C    1 
ATOM   1703 O  O    . ALA   A 1 259 ? -30.498 -5.283  -0.160  1.00 15.88 ? 238 ALA   A O    1 
ATOM   1704 C  CB   . ALA   A 1 259 ? -28.660 -7.969  0.157   1.00 15.33 ? 238 ALA   A CB   1 
ATOM   1705 N  N    . ASP   A 1 260 ? -31.735 -7.127  -0.549  1.00 15.18 ? 239 ASP   A N    1 
ATOM   1706 C  CA   . ASP   A 1 260 ? -32.713 -6.435  -1.392  1.00 16.42 ? 239 ASP   A CA   1 
ATOM   1707 C  C    . ASP   A 1 260 ? -33.378 -5.269  -0.654  1.00 16.09 ? 239 ASP   A C    1 
ATOM   1708 O  O    . ASP   A 1 260 ? -33.600 -4.205  -1.243  1.00 15.11 ? 239 ASP   A O    1 
ATOM   1709 C  CB   . ASP   A 1 260 ? -33.819 -7.391  -1.814  1.00 17.57 ? 239 ASP   A CB   1 
ATOM   1710 C  CG   . ASP   A 1 260 ? -33.500 -8.274  -3.010  1.00 22.08 ? 239 ASP   A CG   1 
ATOM   1711 O  OD1  . ASP   A 1 260 ? -32.592 -7.901  -3.791  1.00 24.10 ? 239 ASP   A OD1  1 
ATOM   1712 O  OD2  . ASP   A 1 260 ? -34.124 -9.350  -3.108  1.00 23.59 ? 239 ASP   A OD2  1 
ATOM   1713 N  N    . ALA   A 1 261 ? -33.629 -5.426  0.652   1.00 13.86 ? 240 ALA   A N    1 
ATOM   1714 C  CA   . ALA   A 1 261 ? -34.258 -4.351  1.408   1.00 14.33 ? 240 ALA   A CA   1 
ATOM   1715 C  C    . ALA   A 1 261 ? -33.257 -3.221  1.638   1.00 15.06 ? 240 ALA   A C    1 
ATOM   1716 O  O    . ALA   A 1 261 ? -33.651 -2.051  1.626   1.00 14.34 ? 240 ALA   A O    1 
ATOM   1717 C  CB   . ALA   A 1 261 ? -34.833 -4.888  2.721   1.00 14.83 ? 240 ALA   A CB   1 
ATOM   1718 N  N    . VAL   A 1 262 ? -31.982 -3.574  1.891   1.00 15.61 ? 241 VAL   A N    1 
ATOM   1719 C  CA   . VAL   A 1 262 ? -30.948 -2.564  2.073   1.00 15.59 ? 241 VAL   A CA   1 
ATOM   1720 C  C    . VAL   A 1 262 ? -30.804 -1.742  0.791   1.00 16.00 ? 241 VAL   A C    1 
ATOM   1721 O  O    . VAL   A 1 262 ? -30.770 -0.499  0.822   1.00 16.17 ? 241 VAL   A O    1 
ATOM   1722 C  CB   . VAL   A 1 262 ? -29.612 -3.208  2.493   1.00 16.23 ? 241 VAL   A CB   1 
ATOM   1723 C  CG1  . VAL   A 1 262 ? -28.515 -2.153  2.554   1.00 17.15 ? 241 VAL   A CG1  1 
ATOM   1724 C  CG2  . VAL   A 1 262 ? -29.741 -3.917  3.837   1.00 16.26 ? 241 VAL   A CG2  1 
ATOM   1725 N  N    . ILE   A 1 263 ? -30.789 -2.437  -0.354  1.00 16.41 ? 242 ILE   A N    1 
ATOM   1726 C  CA   . ILE   A 1 263 ? -30.593 -1.769  -1.641  1.00 17.18 ? 242 ILE   A CA   1 
ATOM   1727 C  C    . ILE   A 1 263 ? -31.766 -0.829  -1.934  1.00 16.43 ? 242 ILE   A C    1 
ATOM   1728 O  O    . ILE   A 1 263 ? -31.550 0.284   -2.406  1.00 16.56 ? 242 ILE   A O    1 
ATOM   1729 C  CB   . ILE   A 1 263 ? -30.364 -2.804  -2.762  1.00 20.67 ? 242 ILE   A CB   1 
ATOM   1730 C  CG1  . ILE   A 1 263 ? -28.922 -3.324  -2.743  1.00 25.99 ? 242 ILE   A CG1  1 
ATOM   1731 C  CG2  . ILE   A 1 263 ? -30.761 -2.271  -4.140  1.00 23.37 ? 242 ILE   A CG2  1 
ATOM   1732 C  CD1  . ILE   A 1 263 ? -27.893 -2.330  -3.238  1.00 31.42 ? 242 ILE   A CD1  1 
ATOM   1733 N  N    . PHE   A 1 264 ? -32.994 -1.240  -1.592  1.00 15.19 ? 243 PHE   A N    1 
ATOM   1734 C  CA   . PHE   A 1 264 ? -34.139 -0.348  -1.711  1.00 14.55 ? 243 PHE   A CA   1 
ATOM   1735 C  C    . PHE   A 1 264 ? -33.911 0.941   -0.910  1.00 14.66 ? 243 PHE   A C    1 
ATOM   1736 O  O    . PHE   A 1 264 ? -34.096 2.062   -1.403  1.00 14.95 ? 243 PHE   A O    1 
ATOM   1737 C  CB   . PHE   A 1 264 ? -35.442 -1.062  -1.322  1.00 14.93 ? 243 PHE   A CB   1 
ATOM   1738 C  CG   . PHE   A 1 264 ? -36.593 -0.081  -1.166  1.00 15.20 ? 243 PHE   A CG   1 
ATOM   1739 C  CD1  . PHE   A 1 264 ? -37.143 0.554   -2.284  1.00 15.28 ? 243 PHE   A CD1  1 
ATOM   1740 C  CD2  . PHE   A 1 264 ? -37.115 0.208   0.096   1.00 15.33 ? 243 PHE   A CD2  1 
ATOM   1741 C  CE1  . PHE   A 1 264 ? -38.189 1.474   -2.138  1.00 16.05 ? 243 PHE   A CE1  1 
ATOM   1742 C  CE2  . PHE   A 1 264 ? -38.163 1.119   0.235   1.00 16.15 ? 243 PHE   A CE2  1 
ATOM   1743 C  CZ   . PHE   A 1 264 ? -38.687 1.748   -0.877  1.00 15.81 ? 243 PHE   A CZ   1 
ATOM   1744 N  N    . LEU   A 1 265 ? -33.517 0.783   0.361   1.00 14.41 ? 244 LEU   A N    1 
ATOM   1745 C  CA   . LEU   A 1 265 ? -33.363 1.926   1.240   1.00 14.80 ? 244 LEU   A CA   1 
ATOM   1746 C  C    . LEU   A 1 265 ? -32.260 2.871   0.781   1.00 15.31 ? 244 LEU   A C    1 
ATOM   1747 O  O    . LEU   A 1 265 ? -32.366 4.069   1.043   1.00 16.00 ? 244 LEU   A O    1 
ATOM   1748 C  CB   . LEU   A 1 265 ? -33.147 1.491   2.689   1.00 14.41 ? 244 LEU   A CB   1 
ATOM   1749 C  CG   . LEU   A 1 265 ? -34.422 0.963   3.356   1.00 14.06 ? 244 LEU   A CG   1 
ATOM   1750 C  CD1  . LEU   A 1 265 ? -34.056 0.292   4.662   1.00 15.03 ? 244 LEU   A CD1  1 
ATOM   1751 C  CD2  . LEU   A 1 265 ? -35.387 2.119   3.606   1.00 14.45 ? 244 LEU   A CD2  1 
ATOM   1752 N  N    . VAL   A 1 266 ? -31.225 2.370   0.114   1.00 15.73 ? 245 VAL   A N    1 
ATOM   1753 C  CA   . VAL   A 1 266 ? -30.187 3.292   -0.319  1.00 15.89 ? 245 VAL   A CA   1 
ATOM   1754 C  C    . VAL   A 1 266 ? -30.545 3.941   -1.659  1.00 17.45 ? 245 VAL   A C    1 
ATOM   1755 O  O    . VAL   A 1 266 ? -29.935 4.954   -2.028  1.00 19.57 ? 245 VAL   A O    1 
ATOM   1756 C  CB   . VAL   A 1 266 ? -28.797 2.625   -0.377  1.00 18.89 ? 245 VAL   A CB   1 
ATOM   1757 C  CG1  . VAL   A 1 266 ? -28.418 1.976   0.951   1.00 18.85 ? 245 VAL   A CG1  1 
ATOM   1758 C  CG2  . VAL   A 1 266 ? -28.631 1.630   -1.510  1.00 24.05 ? 245 VAL   A CG2  1 
ATOM   1759 N  N    . SER   A 1 267 ? -31.537 3.376   -2.362  1.00 16.27 ? 246 SER   A N    1 
ATOM   1760 C  CA   . SER   A 1 267 ? -31.858 3.757   -3.734  1.00 17.01 ? 246 SER   A CA   1 
ATOM   1761 C  C    . SER   A 1 267 ? -32.644 5.069   -3.791  1.00 18.87 ? 246 SER   A C    1 
ATOM   1762 O  O    . SER   A 1 267 ? -33.229 5.528   -2.803  1.00 17.42 ? 246 SER   A O    1 
ATOM   1763 C  CB   . SER   A 1 267 ? -32.652 2.657   -4.420  1.00 15.96 ? 246 SER   A CB   1 
ATOM   1764 O  OG   . SER   A 1 267 ? -34.031 2.772   -4.069  1.00 17.32 ? 246 SER   A OG   1 
ATOM   1765 N  N    . GLY   A 1 268 ? -32.740 5.614   -5.012  1.00 19.59 ? 247 GLY   A N    1 
ATOM   1766 C  CA   . GLY   A 1 268 ? -33.594 6.766   -5.282  1.00 20.82 ? 247 GLY   A CA   1 
ATOM   1767 C  C    . GLY   A 1 268 ? -35.081 6.504   -5.025  1.00 19.86 ? 247 GLY   A C    1 
ATOM   1768 O  O    . GLY   A 1 268 ? -35.844 7.448   -4.832  1.00 23.54 ? 247 GLY   A O    1 
ATOM   1769 N  N    . SER   A 1 269 ? -35.494 5.229   -4.971  1.00 18.23 ? 248 SER   A N    1 
ATOM   1770 C  CA   . SER   A 1 269 ? -36.893 4.894   -4.748  1.00 19.02 ? 248 SER   A CA   1 
ATOM   1771 C  C    . SER   A 1 269 ? -37.279 5.070   -3.279  1.00 17.09 ? 248 SER   A C    1 
ATOM   1772 O  O    . SER   A 1 269 ? -38.439 4.818   -2.920  1.00 18.26 ? 248 SER   A O    1 
ATOM   1773 C  CB   . SER   A 1 269 ? -37.203 3.467   -5.194  1.00 21.55 ? 248 SER   A CB   1 
ATOM   1774 O  OG   . SER   A 1 269 ? -36.945 3.328   -6.590  1.00 25.33 ? 248 SER   A OG   1 
ATOM   1775 N  N    . ALA   A 1 270 ? -36.307 5.462   -2.430  1.00 16.84 ? 249 ALA   A N    1 
ATOM   1776 C  CA   . ALA   A 1 270 ? -36.545 5.627   -1.003  1.00 15.79 ? 249 ALA   A CA   1 
ATOM   1777 C  C    . ALA   A 1 270 ? -36.128 7.021   -0.544  1.00 16.11 ? 249 ALA   A C    1 
ATOM   1778 O  O    . ALA   A 1 270 ? -35.825 7.217   0.627   1.00 16.11 ? 249 ALA   A O    1 
ATOM   1779 C  CB   . ALA   A 1 270 ? -35.784 4.566   -0.220  1.00 17.36 ? 249 ALA   A CB   1 
ATOM   1780 N  N    . GLN   A 1 271 ? -36.101 7.989   -1.467  1.00 17.23 ? 250 GLN   A N    1 
ATOM   1781 C  CA   . GLN   A 1 271 ? -35.554 9.309   -1.178  1.00 18.81 ? 250 GLN   A CA   1 
ATOM   1782 C  C    . GLN   A 1 271 ? -36.323 10.076  -0.098  1.00 16.05 ? 250 GLN   A C    1 
ATOM   1783 O  O    . GLN   A 1 271 ? -35.788 11.060  0.416   1.00 17.55 ? 250 GLN   A O    1 
ATOM   1784 C  CB   . GLN   A 1 271 ? -35.514 10.185  -2.435  1.00 23.65 ? 250 GLN   A CB   1 
ATOM   1785 C  CG   A GLN   A 1 271 ? -36.862 10.340  -3.124  0.70 27.70 ? 250 GLN   A CG   1 
ATOM   1786 C  CD   A GLN   A 1 271 ? -36.776 10.851  -4.546  0.70 31.24 ? 250 GLN   A CD   1 
ATOM   1787 O  OE1  A GLN   A 1 271 ? -37.782 10.897  -5.261  0.70 31.52 ? 250 GLN   A OE1  1 
ATOM   1788 N  NE2  A GLN   A 1 271 ? -35.574 11.212  -4.978  0.70 32.59 ? 250 GLN   A NE2  1 
ATOM   1789 N  N    . TYR   A 1 272 ? -37.575 9.702   0.208   1.00 14.39 ? 251 TYR   A N    1 
ATOM   1790 C  CA   . TYR   A 1 272 ? -38.313 10.409  1.255   1.00 14.79 ? 251 TYR   A CA   1 
ATOM   1791 C  C    . TYR   A 1 272 ? -38.361 9.587   2.547   1.00 14.99 ? 251 TYR   A C    1 
ATOM   1792 O  O    . TYR   A 1 272 ? -39.033 9.958   3.496   1.00 16.02 ? 251 TYR   A O    1 
ATOM   1793 C  CB   . TYR   A 1 272 ? -39.737 10.754  0.800   1.00 14.85 ? 251 TYR   A CB   1 
ATOM   1794 C  CG   . TYR   A 1 272 ? -40.471 11.826  1.596   1.00 14.40 ? 251 TYR   A CG   1 
ATOM   1795 C  CD1  . TYR   A 1 272 ? -40.102 13.165  1.506   1.00 14.77 ? 251 TYR   A CD1  1 
ATOM   1796 C  CD2  . TYR   A 1 272 ? -41.555 11.519  2.419   1.00 14.12 ? 251 TYR   A CD2  1 
ATOM   1797 C  CE1  . TYR   A 1 272 ? -40.784 14.157  2.199   1.00 15.57 ? 251 TYR   A CE1  1 
ATOM   1798 C  CE2  . TYR   A 1 272 ? -42.241 12.502  3.119   1.00 14.37 ? 251 TYR   A CE2  1 
ATOM   1799 C  CZ   . TYR   A 1 272 ? -41.859 13.827  3.007   1.00 14.70 ? 251 TYR   A CZ   1 
ATOM   1800 O  OH   . TYR   A 1 272 ? -42.580 14.764  3.685   1.00 15.51 ? 251 TYR   A OH   1 
ATOM   1801 N  N    . ILE   A 1 273 ? -37.721 8.419   2.553   1.00 13.55 ? 252 ILE   A N    1 
ATOM   1802 C  CA   . ILE   A 1 273 ? -37.815 7.518   3.695   1.00 12.76 ? 252 ILE   A CA   1 
ATOM   1803 C  C    . ILE   A 1 273 ? -36.628 7.737   4.630   1.00 12.56 ? 252 ILE   A C    1 
ATOM   1804 O  O    . ILE   A 1 273 ? -35.472 7.563   4.223   1.00 12.48 ? 252 ILE   A O    1 
ATOM   1805 C  CB   . ILE   A 1 273 ? -37.803 6.064   3.213   1.00 12.64 ? 252 ILE   A CB   1 
ATOM   1806 C  CG1  . ILE   A 1 273 ? -38.965 5.806   2.235   1.00 13.12 ? 252 ILE   A CG1  1 
ATOM   1807 C  CG2  . ILE   A 1 273 ? -37.831 5.122   4.422   1.00 13.75 ? 252 ILE   A CG2  1 
ATOM   1808 C  CD1  . ILE   A 1 273 ? -39.080 4.347   1.821   1.00 13.32 ? 252 ILE   A CD1  1 
ATOM   1809 N  N    . THR   A 1 274 ? -36.910 8.118   5.869   1.00 12.45 ? 253 THR   A N    1 
ATOM   1810 C  CA   . THR   A 1 274 ? -35.866 8.217   6.890   1.00 13.02 ? 253 THR   A CA   1 
ATOM   1811 C  C    . THR   A 1 274 ? -36.526 7.921   8.234   1.00 14.20 ? 253 THR   A C    1 
ATOM   1812 O  O    . THR   A 1 274 ? -37.696 8.250   8.469   1.00 14.39 ? 253 THR   A O    1 
ATOM   1813 C  CB   . THR   A 1 274 ? -35.124 9.566   6.864   1.00 14.18 ? 253 THR   A CB   1 
ATOM   1814 O  OG1  . THR   A 1 274 ? -33.938 9.432   7.655   1.00 14.48 ? 253 THR   A OG1  1 
ATOM   1815 C  CG2  . THR   A 1 274 ? -35.946 10.737  7.382   1.00 14.67 ? 253 THR   A CG2  1 
ATOM   1816 N  N    . GLY   A 1 275 ? -35.756 7.242   9.086   1.00 14.56 ? 254 GLY   A N    1 
ATOM   1817 C  CA   . GLY   A 1 275 ? -36.241 6.831   10.393  1.00 14.85 ? 254 GLY   A CA   1 
ATOM   1818 C  C    . GLY   A 1 275 ? -37.127 5.584   10.350  1.00 15.44 ? 254 GLY   A C    1 
ATOM   1819 O  O    . GLY   A 1 275 ? -37.827 5.322   11.330  1.00 16.42 ? 254 GLY   A O    1 
ATOM   1820 N  N    . SER   A 1 276 ? -37.167 4.895   9.204   1.00 14.45 ? 255 SER   A N    1 
ATOM   1821 C  CA   . SER   A 1 276 ? -38.030 3.736   9.033   1.00 13.38 ? 255 SER   A CA   1 
ATOM   1822 C  C    . SER   A 1 276 ? -37.246 2.458   9.253   1.00 14.78 ? 255 SER   A C    1 
ATOM   1823 O  O    . SER   A 1 276 ? -36.119 2.356   8.793   1.00 16.20 ? 255 SER   A O    1 
ATOM   1824 C  CB   . SER   A 1 276 ? -38.626 3.684   7.665   1.00 15.62 ? 255 SER   A CB   1 
ATOM   1825 O  OG   . SER   A 1 276 ? -39.446 4.838   7.493   1.00 17.63 ? 255 SER   A OG   1 
ATOM   1826 N  N    . ILE   A 1 277 ? -37.922 1.472   9.848   1.00 13.97 ? 256 ILE   A N    1 
ATOM   1827 C  CA   . ILE   A 1 277 ? -37.308 0.154   9.933   1.00 15.29 ? 256 ILE   A CA   1 
ATOM   1828 C  C    . ILE   A 1 277 ? -38.190 -0.832  9.192   1.00 16.81 ? 256 ILE   A C    1 
ATOM   1829 O  O    . ILE   A 1 277 ? -39.349 -1.008  9.567   1.00 19.51 ? 256 ILE   A O    1 
ATOM   1830 C  CB   . ILE   A 1 277 ? -37.055 -0.235  11.397  1.00 16.53 ? 256 ILE   A CB   1 
ATOM   1831 C  CG1  . ILE   A 1 277 ? -36.038 0.755   11.996  1.00 19.78 ? 256 ILE   A CG1  1 
ATOM   1832 C  CG2  . ILE   A 1 277 ? -36.564 -1.690  11.458  1.00 17.03 ? 256 ILE   A CG2  1 
ATOM   1833 C  CD1  . ILE   A 1 277 ? -35.788 0.624   13.484  1.00 22.98 ? 256 ILE   A CD1  1 
ATOM   1834 N  N    . ILE   A 1 278 ? -37.640 -1.450  8.146   1.00 14.99 ? 257 ILE   A N    1 
ATOM   1835 C  CA   . ILE   A 1 278 ? -38.400 -2.393  7.338   1.00 15.41 ? 257 ILE   A CA   1 
ATOM   1836 C  C    . ILE   A 1 278 ? -38.150 -3.801  7.873   1.00 14.58 ? 257 ILE   A C    1 
ATOM   1837 O  O    . ILE   A 1 278 ? -37.017 -4.288  7.807   1.00 13.77 ? 257 ILE   A O    1 
ATOM   1838 C  CB   . ILE   A 1 278 ? -37.980 -2.351  5.854   1.00 16.23 ? 257 ILE   A CB   1 
ATOM   1839 C  CG1  . ILE   A 1 278 ? -38.128 -0.954  5.217   1.00 17.62 ? 257 ILE   A CG1  1 
ATOM   1840 C  CG2  . ILE   A 1 278 ? -38.719 -3.415  5.031   1.00 18.70 ? 257 ILE   A CG2  1 
ATOM   1841 C  CD1  . ILE   A 1 278 ? -37.631 -0.896  3.774   1.00 18.24 ? 257 ILE   A CD1  1 
ATOM   1842 N  N    . LYS   A 1 279 ? -39.215 -4.432  8.366   1.00 14.29 ? 258 LYS   A N    1 
ATOM   1843 C  CA   A LYS   A 1 279 ? -39.138 -5.831  8.771   0.70 14.54 ? 258 LYS   A CA   1 
ATOM   1844 C  CA   B LYS   A 1 279 ? -39.171 -5.819  8.776   0.30 13.64 ? 258 LYS   A CA   1 
ATOM   1845 C  C    . LYS   A 1 279 ? -39.102 -6.703  7.533   1.00 14.28 ? 258 LYS   A C    1 
ATOM   1846 O  O    . LYS   A 1 279 ? -39.889 -6.525  6.596   1.00 15.66 ? 258 LYS   A O    1 
ATOM   1847 C  CB   A LYS   A 1 279 ? -40.307 -6.441  9.559   0.70 16.80 ? 258 LYS   A CB   1 
ATOM   1848 C  CB   B LYS   A 1 279 ? -40.441 -5.966  9.619   0.30 13.01 ? 258 LYS   A CB   1 
ATOM   1849 C  CG   A LYS   A 1 279 ? -40.555 -5.850  10.919  0.70 17.45 ? 258 LYS   A CG   1 
ATOM   1850 C  CG   B LYS   A 1 279 ? -40.668 -7.329  10.207  0.30 11.70 ? 258 LYS   A CG   1 
ATOM   1851 C  CD   A LYS   A 1 279 ? -41.711 -6.592  11.594  0.70 18.23 ? 258 LYS   A CD   1 
ATOM   1852 C  CD   B LYS   A 1 279 ? -41.948 -7.326  11.031  0.30 11.43 ? 258 LYS   A CD   1 
ATOM   1853 C  CE   A LYS   A 1 279 ? -43.062 -6.279  10.996  0.70 18.08 ? 258 LYS   A CE   1 
ATOM   1854 C  CE   B LYS   A 1 279 ? -43.125 -6.814  10.254  0.30 11.70 ? 258 LYS   A CE   1 
ATOM   1855 N  NZ   A LYS   A 1 279 ? -44.210 -6.957  11.626  0.70 18.84 ? 258 LYS   A NZ   1 
ATOM   1856 N  NZ   B LYS   A 1 279 ? -44.401 -7.113  10.914  0.30 11.60 ? 258 LYS   A NZ   1 
ATOM   1857 N  N    . VAL   A 1 280 ? -38.171 -7.659  7.542   1.00 14.14 ? 259 VAL   A N    1 
ATOM   1858 C  CA   . VAL   A 1 280 ? -38.061 -8.644  6.477   1.00 14.57 ? 259 VAL   A CA   1 
ATOM   1859 C  C    . VAL   A 1 280 ? -38.040 -10.022 7.126   1.00 14.26 ? 259 VAL   A C    1 
ATOM   1860 O  O    . VAL   A 1 280 ? -36.975 -10.609 7.324   1.00 15.81 ? 259 VAL   A O    1 
ATOM   1861 C  CB   . VAL   A 1 280 ? -36.825 -8.409  5.591   1.00 15.10 ? 259 VAL   A CB   1 
ATOM   1862 C  CG1  . VAL   A 1 280 ? -36.761 -9.385  4.415   1.00 15.90 ? 259 VAL   A CG1  1 
ATOM   1863 C  CG2  . VAL   A 1 280 ? -36.772 -6.960  5.099   1.00 16.31 ? 259 VAL   A CG2  1 
ATOM   1864 N  N    . ASP   A 1 281 ? -39.228 -10.469 7.521   1.00 13.91 ? 260 ASP   A N    1 
ATOM   1865 C  CA   . ASP   A 1 281 ? -39.310 -11.574 8.472   1.00 13.17 ? 260 ASP   A CA   1 
ATOM   1866 C  C    . ASP   A 1 281 ? -40.331 -12.647 8.094   1.00 13.31 ? 260 ASP   A C    1 
ATOM   1867 O  O    . ASP   A 1 281 ? -40.535 -13.577 8.877   1.00 14.07 ? 260 ASP   A O    1 
ATOM   1868 C  CB   . ASP   A 1 281 ? -39.575 -11.061 9.884   1.00 14.22 ? 260 ASP   A CB   1 
ATOM   1869 C  CG   . ASP   A 1 281 ? -41.018 -10.678 10.208  1.00 14.11 ? 260 ASP   A CG   1 
ATOM   1870 O  OD1  . ASP   A 1 281 ? -41.826 -10.497 9.266   1.00 14.59 ? 260 ASP   A OD1  1 
ATOM   1871 O  OD2  . ASP   A 1 281 ? -41.332 -10.593 11.415  1.00 15.83 ? 260 ASP   A OD2  1 
ATOM   1872 N  N    . GLY   A 1 282 ? -40.960 -12.568 6.913   1.00 13.51 ? 261 GLY   A N    1 
ATOM   1873 C  CA   . GLY   A 1 282 ? -41.839 -13.661 6.498   1.00 12.84 ? 261 GLY   A CA   1 
ATOM   1874 C  C    . GLY   A 1 282 ? -43.048 -13.811 7.422   1.00 13.29 ? 261 GLY   A C    1 
ATOM   1875 O  O    . GLY   A 1 282 ? -43.698 -14.851 7.409   1.00 14.50 ? 261 GLY   A O    1 
ATOM   1876 N  N    . GLY   A 1 283 ? -43.376 -12.766 8.189   1.00 12.60 ? 262 GLY   A N    1 
ATOM   1877 C  CA   . GLY   A 1 283 ? -44.474 -12.846 9.153   1.00 12.97 ? 262 GLY   A CA   1 
ATOM   1878 C  C    . GLY   A 1 283 ? -44.114 -13.420 10.537  1.00 13.37 ? 262 GLY   A C    1 
ATOM   1879 O  O    . GLY   A 1 283 ? -45.016 -13.573 11.374  1.00 14.88 ? 262 GLY   A O    1 
ATOM   1880 N  N    . LEU   A 1 284 ? -42.831 -13.747 10.789  1.00 13.86 ? 263 LEU   A N    1 
ATOM   1881 C  CA   . LEU   A 1 284 ? -42.443 -14.431 12.024  1.00 13.96 ? 263 LEU   A CA   1 
ATOM   1882 C  C    . LEU   A 1 284 ? -42.903 -13.686 13.274  1.00 14.80 ? 263 LEU   A C    1 
ATOM   1883 O  O    . LEU   A 1 284 ? -43.411 -14.287 14.226  1.00 15.96 ? 263 LEU   A O    1 
ATOM   1884 C  CB   . LEU   A 1 284 ? -40.935 -14.659 12.034  1.00 14.98 ? 263 LEU   A CB   1 
ATOM   1885 C  CG   . LEU   A 1 284 ? -40.426 -15.399 13.275  1.00 15.82 ? 263 LEU   A CG   1 
ATOM   1886 C  CD1  . LEU   A 1 284 ? -41.075 -16.793 13.409  1.00 18.12 ? 263 LEU   A CD1  1 
ATOM   1887 C  CD2  . LEU   A 1 284 ? -38.907 -15.476 13.210  1.00 18.93 ? 263 LEU   A CD2  1 
ATOM   1888 N  N    . SER   A 1 285 ? -42.729 -12.367 13.259  1.00 14.93 ? 264 SER   A N    1 
ATOM   1889 C  CA   . SER   A 1 285 ? -43.034 -11.564 14.433  1.00 15.83 ? 264 SER   A CA   1 
ATOM   1890 C  C    . SER   A 1 285 ? -44.540 -11.469 14.710  1.00 15.24 ? 264 SER   A C    1 
ATOM   1891 O  O    . SER   A 1 285 ? -44.906 -11.013 15.791  1.00 18.00 ? 264 SER   A O    1 
ATOM   1892 C  CB   . SER   A 1 285 ? -42.400 -10.197 14.328  1.00 15.95 ? 264 SER   A CB   1 
ATOM   1893 O  OG   . SER   A 1 285 ? -42.981 -9.494  13.240  1.00 17.79 ? 264 SER   A OG   1 
ATOM   1894 N  N    . LEU   A 1 286 ? -45.389 -11.905 13.774  1.00 14.98 ? 265 LEU   A N    1 
ATOM   1895 C  CA   . LEU   A 1 286 ? -46.839 -11.912 13.960  1.00 16.16 ? 265 LEU   A CA   1 
ATOM   1896 C  C    . LEU   A 1 286 ? -47.317 -13.188 14.651  1.00 15.82 ? 265 LEU   A C    1 
ATOM   1897 O  O    . LEU   A 1 286 ? -48.510 -13.304 14.920  1.00 16.91 ? 265 LEU   A O    1 
ATOM   1898 C  CB   . LEU   A 1 286 ? -47.538 -11.773 12.603  1.00 18.48 ? 265 LEU   A CB   1 
ATOM   1899 C  CG   . LEU   A 1 286 ? -47.128 -10.568 11.756  1.00 21.86 ? 265 LEU   A CG   1 
ATOM   1900 C  CD1  . LEU   A 1 286 ? -47.851 -10.671 10.426  1.00 23.26 ? 265 LEU   A CD1  1 
ATOM   1901 C  CD2  . LEU   A 1 286 ? -47.441 -9.271  12.471  1.00 24.15 ? 265 LEU   A CD2  1 
ATOM   1902 N  N    . VAL   A 1 287 ? -46.431 -14.160 14.901  1.00 15.66 ? 266 VAL   A N    1 
ATOM   1903 C  CA   . VAL   A 1 287 ? -46.890 -15.475 15.339  1.00 16.18 ? 266 VAL   A CA   1 
ATOM   1904 C  C    . VAL   A 1 287 ? -46.849 -15.544 16.870  1.00 17.94 ? 266 VAL   A C    1 
ATOM   1905 O  O    . VAL   A 1 287 ? -45.783 -15.404 17.476  1.00 19.23 ? 266 VAL   A O    1 
ATOM   1906 C  CB   . VAL   A 1 287 ? -46.021 -16.596 14.738  1.00 15.99 ? 266 VAL   A CB   1 
ATOM   1907 C  CG1  . VAL   A 1 287 ? -46.472 -17.981 15.202  1.00 18.38 ? 266 VAL   A CG1  1 
ATOM   1908 C  CG2  . VAL   A 1 287 ? -46.012 -16.545 13.214  1.00 16.50 ? 266 VAL   A CG2  1 
ATOM   1909 N  N    . HIS   A 1 288 ? -48.003 -15.837 17.484  1.00 18.48 ? 267 HIS   A N    1 
ATOM   1910 C  CA   . HIS   A 1 288 ? -48.073 -15.924 18.941  1.00 18.84 ? 267 HIS   A CA   1 
ATOM   1911 C  C    . HIS   A 1 288 ? -47.442 -17.232 19.432  1.00 20.53 ? 267 HIS   A C    1 
ATOM   1912 O  O    . HIS   A 1 288 ? -47.257 -18.177 18.668  1.00 21.79 ? 267 HIS   A O    1 
ATOM   1913 C  CB   . HIS   A 1 288 ? -49.517 -15.747 19.436  1.00 20.28 ? 267 HIS   A CB   1 
ATOM   1914 C  CG   . HIS   A 1 288 ? -50.474 -16.827 19.034  1.00 20.94 ? 267 HIS   A CG   1 
ATOM   1915 N  ND1  . HIS   A 1 288 ? -50.379 -18.123 19.506  1.00 22.87 ? 267 HIS   A ND1  1 
ATOM   1916 C  CD2  . HIS   A 1 288 ? -51.536 -16.810 18.202  1.00 23.07 ? 267 HIS   A CD2  1 
ATOM   1917 C  CE1  . HIS   A 1 288 ? -51.347 -18.858 18.967  1.00 22.99 ? 267 HIS   A CE1  1 
ATOM   1918 N  NE2  . HIS   A 1 288 ? -52.073 -18.085 18.176  1.00 25.22 ? 267 HIS   A NE2  1 
ATOM   1919 N  N    . ALA   A 1 289 ? -47.187 -17.286 20.748  1.00 21.23 ? 268 ALA   A N    1 
ATOM   1920 C  CA   . ALA   A 1 289 ? -46.641 -18.451 21.429  1.00 25.34 ? 268 ALA   A CA   1 
ATOM   1921 C  C    . ALA   A 1 289 ? -47.535 -19.679 21.233  1.00 27.12 ? 268 ALA   A C    1 
ATOM   1922 O  O    . ALA   A 1 289 ? -46.972 -20.804 21.278  1.00 30.43 ? 268 ALA   A O    1 
ATOM   1923 C  CB   . ALA   A 1 289 ? -46.514 -18.143 22.900  1.00 25.36 ? 268 ALA   A CB   1 
ATOM   1924 O  OXT  . ALA   A 1 289 ? -48.758 -19.491 21.110  1.00 26.89 ? 268 ALA   A OXT  1 
ATOM   1925 N  N    . VAL   B 1 15  ? -64.023 -16.035 -18.135 0.70 40.80 ? -6  VAL   B N    1 
ATOM   1926 C  CA   . VAL   B 1 15  ? -63.285 -14.808 -18.570 0.70 37.62 ? -6  VAL   B CA   1 
ATOM   1927 C  C    . VAL   B 1 15  ? -63.394 -14.716 -20.089 0.70 34.54 ? -6  VAL   B C    1 
ATOM   1928 O  O    . VAL   B 1 15  ? -62.974 -15.642 -20.782 0.70 34.75 ? -6  VAL   B O    1 
ATOM   1929 C  CB   . VAL   B 1 15  ? -61.812 -14.884 -18.117 0.70 35.70 ? -6  VAL   B CB   1 
ATOM   1930 C  CG1  . VAL   B 1 15  ? -60.944 -13.804 -18.760 0.70 33.94 ? -6  VAL   B CG1  1 
ATOM   1931 C  CG2  . VAL   B 1 15  ? -61.685 -14.867 -16.597 0.70 35.26 ? -6  VAL   B CG2  1 
ATOM   1932 N  N    . PRO   B 1 16  ? -63.961 -13.625 -20.664 0.70 32.63 ? -5  PRO   B N    1 
ATOM   1933 C  CA   . PRO   B 1 16  ? -64.073 -13.520 -22.122 0.70 29.52 ? -5  PRO   B CA   1 
ATOM   1934 C  C    . PRO   B 1 16  ? -62.686 -13.585 -22.756 0.70 28.43 ? -5  PRO   B C    1 
ATOM   1935 O  O    . PRO   B 1 16  ? -61.723 -13.071 -22.191 0.70 29.61 ? -5  PRO   B O    1 
ATOM   1936 C  CB   . PRO   B 1 16  ? -64.766 -12.161 -22.369 0.70 29.29 ? -5  PRO   B CB   1 
ATOM   1937 C  CG   . PRO   B 1 16  ? -65.384 -11.797 -21.035 0.70 29.50 ? -5  PRO   B CG   1 
ATOM   1938 C  CD   . PRO   B 1 16  ? -64.525 -12.457 -19.962 0.70 30.98 ? -5  PRO   B CD   1 
ATOM   1939 N  N    . ARG   B 1 17  ? -62.593 -14.227 -23.931 0.70 27.67 ? -4  ARG   B N    1 
ATOM   1940 C  CA   . ARG   B 1 17  ? -61.370 -14.241 -24.724 0.70 26.81 ? -4  ARG   B CA   1 
ATOM   1941 C  C    . ARG   B 1 17  ? -60.835 -12.816 -24.872 0.70 26.07 ? -4  ARG   B C    1 
ATOM   1942 O  O    . ARG   B 1 17  ? -61.607 -11.865 -25.007 0.70 25.72 ? -4  ARG   B O    1 
ATOM   1943 C  CB   . ARG   B 1 17  ? -61.644 -14.838 -26.114 1.00 30.93 ? -4  ARG   B CB   1 
ATOM   1944 C  CG   . ARG   B 1 17  ? -60.555 -14.677 -27.168 0.50 31.62 ? -4  ARG   B CG   1 
ATOM   1945 C  CD   . ARG   B 1 17  ? -60.804 -15.477 -28.445 0.50 32.71 ? -4  ARG   B CD   1 
ATOM   1946 N  NE   . ARG   B 1 17  ? -61.864 -14.945 -29.310 0.50 34.88 ? -4  ARG   B NE   1 
ATOM   1947 C  CZ   . ARG   B 1 17  ? -61.782 -13.853 -30.069 0.50 34.64 ? -4  ARG   B CZ   1 
ATOM   1948 N  NH1  . ARG   B 1 17  ? -60.665 -13.145 -30.105 0.50 33.22 ? -4  ARG   B NH1  1 
ATOM   1949 N  NH2  . ARG   B 1 17  ? -62.818 -13.487 -30.808 0.50 34.59 ? -4  ARG   B NH2  1 
ATOM   1950 N  N    . GLY   B 1 18  ? -59.506 -12.684 -24.844 0.70 24.42 ? -3  GLY   B N    1 
ATOM   1951 C  CA   . GLY   B 1 18  ? -58.833 -11.420 -25.096 0.70 24.13 ? -3  GLY   B CA   1 
ATOM   1952 C  C    . GLY   B 1 18  ? -58.404 -10.726 -23.803 0.70 25.02 ? -3  GLY   B C    1 
ATOM   1953 O  O    . GLY   B 1 18  ? -58.180 -9.515  -23.800 0.70 25.17 ? -3  GLY   B O    1 
ATOM   1954 N  N    . SER   B 1 19  ? -58.291 -11.506 -22.716 0.70 25.85 ? -2  SER   B N    1 
ATOM   1955 C  CA   . SER   B 1 19  ? -57.886 -10.997 -21.411 0.70 25.97 ? -2  SER   B CA   1 
ATOM   1956 C  C    . SER   B 1 19  ? -56.366 -10.861 -21.317 0.70 26.79 ? -2  SER   B C    1 
ATOM   1957 O  O    . SER   B 1 19  ? -55.870 -10.125 -20.466 0.70 26.93 ? -2  SER   B O    1 
ATOM   1958 C  CB   . SER   B 1 19  ? -58.431 -11.846 -20.281 0.70 25.22 ? -2  SER   B CB   1 
ATOM   1959 O  OG   . SER   B 1 19  ? -57.726 -13.080 -20.172 0.70 24.54 ? -2  SER   B OG   1 
ATOM   1960 N  N    . HIS   B 1 20  ? -55.636 -11.573 -22.192 0.70 26.85 ? -1  HIS   B N    1 
ATOM   1961 C  CA   . HIS   B 1 20  ? -54.179 -11.589 -22.207 0.70 28.60 ? -1  HIS   B CA   1 
ATOM   1962 C  C    . HIS   B 1 20  ? -53.639 -12.014 -20.842 0.70 28.48 ? -1  HIS   B C    1 
ATOM   1963 O  O    . HIS   B 1 20  ? -52.567 -11.579 -20.428 0.70 28.43 ? -1  HIS   B O    1 
ATOM   1964 C  CB   . HIS   B 1 20  ? -53.625 -10.235 -22.671 0.70 30.24 ? -1  HIS   B CB   1 
ATOM   1965 C  CG   . HIS   B 1 20  ? -53.915 -9.966  -24.111 0.50 30.97 ? -1  HIS   B CG   1 
ATOM   1966 N  ND1  . HIS   B 1 20  ? -53.143 -10.485 -25.127 0.50 32.46 ? -1  HIS   B ND1  1 
ATOM   1967 C  CD2  . HIS   B 1 20  ? -54.893 -9.268  -24.703 0.50 32.10 ? -1  HIS   B CD2  1 
ATOM   1968 C  CE1  . HIS   B 1 20  ? -53.639 -10.098 -26.294 0.50 33.08 ? -1  HIS   B CE1  1 
ATOM   1969 N  NE2  . HIS   B 1 20  ? -54.704 -9.360  -26.058 0.50 32.59 ? -1  HIS   B NE2  1 
ATOM   1970 N  N    . MET   B 1 21  ? -54.387 -12.884 -20.163 0.70 29.51 ? 0   MET   B N    1 
ATOM   1971 C  CA   . MET   B 1 21  ? -54.096 -13.234 -18.782 0.70 29.41 ? 0   MET   B CA   1 
ATOM   1972 C  C    . MET   B 1 21  ? -52.717 -13.882 -18.655 0.70 29.84 ? 0   MET   B C    1 
ATOM   1973 O  O    . MET   B 1 21  ? -52.140 -13.879 -17.578 0.70 27.99 ? 0   MET   B O    1 
ATOM   1974 C  CB   . MET   B 1 21  ? -55.178 -14.157 -18.213 0.70 30.80 ? 0   MET   B CB   1 
ATOM   1975 C  CG   . MET   B 1 21  ? -55.340 -15.445 -18.995 0.70 32.91 ? 0   MET   B CG   1 
ATOM   1976 S  SD   . MET   B 1 21  ? -56.635 -16.494 -18.310 0.70 38.70 ? 0   MET   B SD   1 
ATOM   1977 C  CE   . MET   B 1 21  ? -55.869 -16.913 -16.737 0.70 34.82 ? 0   MET   B CE   1 
ATOM   1978 N  N    . MET   B 1 22  ? -52.177 -14.426 -19.754 0.70 31.06 ? 1   MET   B N    1 
ATOM   1979 C  CA   . MET   B 1 22  ? -50.924 -15.161 -19.664 0.70 32.89 ? 1   MET   B CA   1 
ATOM   1980 C  C    . MET   B 1 22  ? -49.747 -14.191 -19.731 0.70 32.65 ? 1   MET   B C    1 
ATOM   1981 O  O    . MET   B 1 22  ? -48.619 -14.541 -19.388 0.70 35.08 ? 1   MET   B O    1 
ATOM   1982 C  CB   . MET   B 1 22  ? -50.822 -16.185 -20.800 0.70 35.67 ? 1   MET   B CB   1 
ATOM   1983 C  CG   . MET   B 1 22  ? -50.505 -17.590 -20.331 0.50 40.34 ? 1   MET   B CG   1 
ATOM   1984 S  SD   . MET   B 1 22  ? -51.689 -18.154 -19.091 0.50 43.40 ? 1   MET   B SD   1 
ATOM   1985 C  CE   . MET   B 1 22  ? -50.949 -17.544 -17.569 0.50 42.54 ? 1   MET   B CE   1 
ATOM   1986 N  N    . GLU   B 1 23  ? -50.021 -12.966 -20.177 0.70 31.22 ? 2   GLU   B N    1 
ATOM   1987 C  CA   . GLU   B 1 23  ? -48.952 -12.114 -20.662 0.70 30.61 ? 2   GLU   B CA   1 
ATOM   1988 C  C    . GLU   B 1 23  ? -48.473 -11.150 -19.580 0.70 29.28 ? 2   GLU   B C    1 
ATOM   1989 O  O    . GLU   B 1 23  ? -47.320 -10.732 -19.618 0.70 30.99 ? 2   GLU   B O    1 
ATOM   1990 C  CB   . GLU   B 1 23  ? -49.379 -11.353 -21.916 0.70 33.53 ? 2   GLU   B CB   1 
ATOM   1991 C  CG   . GLU   B 1 23  ? -49.460 -12.240 -23.155 0.50 37.52 ? 2   GLU   B CG   1 
ATOM   1992 C  CD   . GLU   B 1 23  ? -49.792 -11.492 -24.431 0.50 41.61 ? 2   GLU   B CD   1 
ATOM   1993 O  OE1  . GLU   B 1 23  ? -50.089 -10.279 -24.359 0.50 43.94 ? 2   GLU   B OE1  1 
ATOM   1994 O  OE2  . GLU   B 1 23  ? -49.738 -12.127 -25.507 0.50 44.78 ? 2   GLU   B OE2  1 
ATOM   1995 N  N    . ALA   B 1 24  ? -49.357 -10.793 -18.638 1.00 25.52 ? 3   ALA   B N    1 
ATOM   1996 C  CA   . ALA   B 1 24  ? -49.057 -9.695  -17.728 1.00 23.81 ? 3   ALA   B CA   1 
ATOM   1997 C  C    . ALA   B 1 24  ? -49.931 -9.794  -16.484 1.00 21.49 ? 3   ALA   B C    1 
ATOM   1998 O  O    . ALA   B 1 24  ? -51.063 -10.265 -16.552 1.00 23.52 ? 3   ALA   B O    1 
ATOM   1999 C  CB   . ALA   B 1 24  ? -49.284 -8.364  -18.403 1.00 22.99 ? 3   ALA   B CB   1 
ATOM   2000 N  N    . PRO   B 1 25  ? -49.441 -9.346  -15.306 1.00 18.95 ? 4   PRO   B N    1 
ATOM   2001 C  CA   . PRO   B 1 25  ? -50.287 -9.321  -14.114 1.00 18.33 ? 4   PRO   B CA   1 
ATOM   2002 C  C    . PRO   B 1 25  ? -51.258 -8.150  -14.102 1.00 17.72 ? 4   PRO   B C    1 
ATOM   2003 O  O    . PRO   B 1 25  ? -51.224 -7.281  -14.979 1.00 18.86 ? 4   PRO   B O    1 
ATOM   2004 C  CB   . PRO   B 1 25  ? -49.252 -9.237  -12.990 1.00 18.30 ? 4   PRO   B CB   1 
ATOM   2005 C  CG   . PRO   B 1 25  ? -48.129 -8.416  -13.597 1.00 20.31 ? 4   PRO   B CG   1 
ATOM   2006 C  CD   . PRO   B 1 25  ? -48.081 -8.832  -15.074 1.00 19.65 ? 4   PRO   B CD   1 
ATOM   2007 N  N    . ALA   B 1 26  ? -52.196 -8.197  -13.155 1.00 17.19 ? 5   ALA   B N    1 
ATOM   2008 C  CA   . ALA   B 1 26  ? -53.213 -7.165  -13.051 1.00 16.23 ? 5   ALA   B CA   1 
ATOM   2009 C  C    . ALA   B 1 26  ? -53.343 -6.717  -11.603 1.00 16.86 ? 5   ALA   B C    1 
ATOM   2010 O  O    . ALA   B 1 26  ? -53.136 -7.503  -10.686 1.00 16.87 ? 5   ALA   B O    1 
ATOM   2011 C  CB   . ALA   B 1 26  ? -54.555 -7.662  -13.571 1.00 17.24 ? 5   ALA   B CB   1 
ATOM   2012 N  N    . ALA   B 1 27  ? -53.742 -5.454  -11.423 1.00 15.83 ? 6   ALA   B N    1 
ATOM   2013 C  CA   . ALA   B 1 27  ? -53.869 -4.876  -10.093 1.00 15.27 ? 6   ALA   B CA   1 
ATOM   2014 C  C    . ALA   B 1 27  ? -55.161 -4.077  -9.985  1.00 15.29 ? 6   ALA   B C    1 
ATOM   2015 O  O    . ALA   B 1 27  ? -55.578 -3.445  -10.958 1.00 17.07 ? 6   ALA   B O    1 
ATOM   2016 C  CB   . ALA   B 1 27  ? -52.704 -3.933  -9.861  1.00 16.80 ? 6   ALA   B CB   1 
ATOM   2017 N  N    . VAL   B 1 28  ? -55.770 -4.069  -8.797  1.00 15.30 ? 7   VAL   B N    1 
ATOM   2018 C  CA   . VAL   B 1 28  ? -56.867 -3.169  -8.455  1.00 14.94 ? 7   VAL   B CA   1 
ATOM   2019 C  C    . VAL   B 1 28  ? -56.283 -2.078  -7.566  1.00 15.29 ? 7   VAL   B C    1 
ATOM   2020 O  O    . VAL   B 1 28  ? -55.635 -2.415  -6.567  1.00 15.39 ? 7   VAL   B O    1 
ATOM   2021 C  CB   . VAL   B 1 28  ? -57.977 -3.904  -7.672  1.00 15.22 ? 7   VAL   B CB   1 
ATOM   2022 C  CG1  . VAL   B 1 28  ? -58.966 -2.943  -7.015  1.00 17.05 ? 7   VAL   B CG1  1 
ATOM   2023 C  CG2  . VAL   B 1 28  ? -58.686 -4.958  -8.516  1.00 16.13 ? 7   VAL   B CG2  1 
ATOM   2024 N  N    . VAL   B 1 29  ? -56.562 -0.801  -7.877  1.00 14.37 ? 8   VAL   B N    1 
ATOM   2025 C  CA   . VAL   B 1 29  ? -56.193 0.311   -7.013  1.00 14.34 ? 8   VAL   B CA   1 
ATOM   2026 C  C    . VAL   B 1 29  ? -57.459 1.066   -6.641  1.00 14.65 ? 8   VAL   B C    1 
ATOM   2027 O  O    . VAL   B 1 29  ? -58.169 1.553   -7.527  1.00 15.01 ? 8   VAL   B O    1 
ATOM   2028 C  CB   . VAL   B 1 29  ? -55.187 1.259   -7.682  1.00 13.53 ? 8   VAL   B CB   1 
ATOM   2029 C  CG1  . VAL   B 1 29  ? -54.772 2.391   -6.728  1.00 15.64 ? 8   VAL   B CG1  1 
ATOM   2030 C  CG2  . VAL   B 1 29  ? -53.950 0.521   -8.201  1.00 14.47 ? 8   VAL   B CG2  1 
ATOM   2031 N  N    . THR   B 1 30  ? -57.779 1.133   -5.345  1.00 14.57 ? 9   THR   B N    1 
ATOM   2032 C  CA   . THR   B 1 30  ? -58.987 1.853   -4.981  1.00 13.78 ? 9   THR   B CA   1 
ATOM   2033 C  C    . THR   B 1 30  ? -58.672 3.342   -4.865  1.00 15.24 ? 9   THR   B C    1 
ATOM   2034 O  O    . THR   B 1 30  ? -57.544 3.735   -4.562  1.00 15.85 ? 9   THR   B O    1 
ATOM   2035 C  CB   . THR   B 1 30  ? -59.653 1.306   -3.714  1.00 15.45 ? 9   THR   B CB   1 
ATOM   2036 O  OG1  . THR   B 1 30  ? -58.779 1.465   -2.590  1.00 13.66 ? 9   THR   B OG1  1 
ATOM   2037 C  CG2  . THR   B 1 30  ? -60.026 -0.159  -3.855  1.00 15.25 ? 9   THR   B CG2  1 
ATOM   2038 N  N    . GLY   B 1 31  ? -59.688 4.160   -5.137  1.00 13.96 ? 10  GLY   B N    1 
ATOM   2039 C  CA   . GLY   B 1 31  ? -59.548 5.612   -5.062  1.00 15.42 ? 10  GLY   B CA   1 
ATOM   2040 C  C    . GLY   B 1 31  ? -58.424 6.084   -5.983  1.00 15.94 ? 10  GLY   B C    1 
ATOM   2041 O  O    . GLY   B 1 31  ? -57.580 6.884   -5.588  1.00 17.13 ? 10  GLY   B O    1 
ATOM   2042 N  N    . ALA   B 1 32  ? -58.449 5.649   -7.253  1.00 16.17 ? 11  ALA   B N    1 
ATOM   2043 C  CA   . ALA   B 1 32  ? -57.273 5.793   -8.107  1.00 15.10 ? 11  ALA   B CA   1 
ATOM   2044 C  C    . ALA   B 1 32  ? -57.406 6.899   -9.157  1.00 17.68 ? 11  ALA   B C    1 
ATOM   2045 O  O    . ALA   B 1 32  ? -56.524 6.999   -10.008 1.00 17.79 ? 11  ALA   B O    1 
ATOM   2046 C  CB   . ALA   B 1 32  ? -56.951 4.479   -8.791  1.00 16.89 ? 11  ALA   B CB   1 
ATOM   2047 N  N    . ALA   B 1 33  ? -58.456 7.722   -9.066  1.00 18.10 ? 12  ALA   B N    1 
ATOM   2048 C  CA   . ALA   B 1 33  ? -58.673 8.733   -10.100 1.00 19.98 ? 12  ALA   B CA   1 
ATOM   2049 C  C    . ALA   B 1 33  ? -57.647 9.859   -9.988  1.00 21.06 ? 12  ALA   B C    1 
ATOM   2050 O  O    . ALA   B 1 33  ? -57.299 10.470  -10.998 1.00 22.00 ? 12  ALA   B O    1 
ATOM   2051 C  CB   . ALA   B 1 33  ? -60.075 9.281   -10.035 1.00 19.80 ? 12  ALA   B CB   1 
ATOM   2052 N  N    . LYS   B 1 34  ? -57.177 10.156  -8.769  1.00 19.78 ? 13  LYS   B N    1 
ATOM   2053 C  CA   . LYS   B 1 34  ? -56.355 11.341  -8.570  1.00 22.50 ? 13  LYS   B CA   1 
ATOM   2054 C  C    . LYS   B 1 34  ? -55.292 11.090  -7.504  1.00 21.81 ? 13  LYS   B C    1 
ATOM   2055 O  O    . LYS   B 1 34  ? -55.329 10.062  -6.823  1.00 21.86 ? 13  LYS   B O    1 
ATOM   2056 C  CB   . LYS   B 1 34  ? -57.232 12.487  -8.057  1.00 26.12 ? 13  LYS   B CB   1 
ATOM   2057 C  CG   . LYS   B 1 34  ? -58.361 12.968  -8.953  1.00 28.60 ? 13  LYS   B CG   1 
ATOM   2058 C  CD   . LYS   B 1 34  ? -59.167 14.052  -8.249  0.70 29.33 ? 13  LYS   B CD   1 
ATOM   2059 C  CE   . LYS   B 1 34  ? -60.363 14.408  -9.073  0.70 31.59 ? 13  LYS   B CE   1 
ATOM   2060 N  NZ   . LYS   B 1 34  ? -61.172 15.460  -8.453  0.70 31.67 ? 13  LYS   B NZ   1 
ATOM   2061 N  N    . ARG   B 1 35  ? -54.345 12.035  -7.385  1.00 20.03 ? 14  ARG   B N    1 
ATOM   2062 C  CA   . ARG   B 1 35  ? -53.454 12.091  -6.231  1.00 20.16 ? 14  ARG   B CA   1 
ATOM   2063 C  C    . ARG   B 1 35  ? -52.669 10.781  -6.077  1.00 20.15 ? 14  ARG   B C    1 
ATOM   2064 O  O    . ARG   B 1 35  ? -52.034 10.315  -7.028  1.00 18.78 ? 14  ARG   B O    1 
ATOM   2065 C  CB   . ARG   B 1 35  ? -54.225 12.638  -5.021  1.00 22.61 ? 14  ARG   B CB   1 
ATOM   2066 C  CG   . ARG   B 1 35  ? -54.748 14.063  -5.206  1.00 21.69 ? 14  ARG   B CG   1 
ATOM   2067 C  CD   . ARG   B 1 35  ? -55.864 14.397  -4.231  0.80 22.67 ? 14  ARG   B CD   1 
ATOM   2068 N  NE   . ARG   B 1 35  ? -55.444 14.235  -2.836  0.80 22.27 ? 14  ARG   B NE   1 
ATOM   2069 C  CZ   . ARG   B 1 35  ? -54.718 15.105  -2.126  0.80 22.64 ? 14  ARG   B CZ   1 
ATOM   2070 N  NH1  . ARG   B 1 35  ? -54.319 16.251  -2.660  0.80 21.80 ? 14  ARG   B NH1  1 
ATOM   2071 N  NH2  . ARG   B 1 35  ? -54.419 14.839  -0.862  0.80 22.22 ? 14  ARG   B NH2  1 
ATOM   2072 N  N    . ILE   B 1 36  ? -52.595 10.248  -4.843  1.00 19.16 ? 15  ILE   B N    1 
ATOM   2073 C  CA   . ILE   B 1 36  ? -51.701 9.124   -4.605  1.00 17.42 ? 15  ILE   B CA   1 
ATOM   2074 C  C    . ILE   B 1 36  ? -52.179 7.876   -5.343  1.00 16.94 ? 15  ILE   B C    1 
ATOM   2075 O  O    . ILE   B 1 36  ? -51.357 7.149   -5.884  1.00 15.71 ? 15  ILE   B O    1 
ATOM   2076 C  CB   . ILE   B 1 36  ? -51.519 8.884   -3.091  1.00 17.81 ? 15  ILE   B CB   1 
ATOM   2077 C  CG1  . ILE   B 1 36  ? -50.726 10.018  -2.472  1.00 21.01 ? 15  ILE   B CG1  1 
ATOM   2078 C  CG2  . ILE   B 1 36  ? -50.901 7.521   -2.786  1.00 17.36 ? 15  ILE   B CG2  1 
ATOM   2079 C  CD1  . ILE   B 1 36  ? -50.708 9.965   -0.956  1.00 23.47 ? 15  ILE   B CD1  1 
ATOM   2080 N  N    . GLY   B 1 37  ? -53.491 7.622   -5.316  1.00 16.39 ? 16  GLY   B N    1 
ATOM   2081 C  CA   . GLY   B 1 37  ? -54.016 6.438   -5.988  1.00 17.97 ? 16  GLY   B CA   1 
ATOM   2082 C  C    . GLY   B 1 37  ? -53.703 6.464   -7.488  1.00 17.21 ? 16  GLY   B C    1 
ATOM   2083 O  O    . GLY   B 1 37  ? -53.315 5.455   -8.072  1.00 16.36 ? 16  GLY   B O    1 
ATOM   2084 N  N    . ARG   B 1 38  ? -53.794 7.659   -8.089  1.00 16.26 ? 17  ARG   B N    1 
ATOM   2085 C  CA   . ARG   B 1 38  ? -53.480 7.783   -9.504  1.00 17.77 ? 17  ARG   B CA   1 
ATOM   2086 C  C    . ARG   B 1 38  ? -52.008 7.453   -9.739  1.00 17.03 ? 17  ARG   B C    1 
ATOM   2087 O  O    . ARG   B 1 38  ? -51.654 6.753   -10.675 1.00 17.42 ? 17  ARG   B O    1 
ATOM   2088 C  CB   . ARG   B 1 38  ? -53.772 9.209   -9.983  1.00 19.09 ? 17  ARG   B CB   1 
ATOM   2089 C  CG   . ARG   B 1 38  ? -53.373 9.496   -11.425 1.00 22.66 ? 17  ARG   B CG   1 
ATOM   2090 C  CD   . ARG   B 1 38  ? -53.773 10.955  -11.664 1.00 24.15 ? 17  ARG   B CD   1 
ATOM   2091 N  NE   . ARG   B 1 38  ? -54.286 11.178  -13.019 0.70 30.22 ? 17  ARG   B NE   1 
ATOM   2092 C  CZ   . ARG   B 1 38  ? -53.516 11.157  -14.091 0.70 29.27 ? 17  ARG   B CZ   1 
ATOM   2093 N  NH1  . ARG   B 1 38  ? -52.210 11.041  -13.941 0.70 31.56 ? 17  ARG   B NH1  1 
ATOM   2094 N  NH2  . ARG   B 1 38  ? -54.065 11.247  -15.295 0.70 29.70 ? 17  ARG   B NH2  1 
ATOM   2095 N  N    . ALA   B 1 39  ? -51.131 7.969   -8.864  1.00 16.62 ? 18  ALA   B N    1 
ATOM   2096 C  CA   . ALA   B 1 39  ? -49.705 7.775   -9.042  1.00 15.38 ? 18  ALA   B CA   1 
ATOM   2097 C  C    . ALA   B 1 39  ? -49.361 6.295   -8.912  1.00 14.31 ? 18  ALA   B C    1 
ATOM   2098 O  O    . ALA   B 1 39  ? -48.478 5.794   -9.607  1.00 15.45 ? 18  ALA   B O    1 
ATOM   2099 C  CB   . ALA   B 1 39  ? -48.948 8.585   -8.004  1.00 15.96 ? 18  ALA   B CB   1 
ATOM   2100 N  N    . ILE   B 1 40  ? -50.058 5.601   -7.990  1.00 14.06 ? 19  ILE   B N    1 
ATOM   2101 C  CA   . ILE   B 1 40  ? -49.827 4.173   -7.821  1.00 13.60 ? 19  ILE   B CA   1 
ATOM   2102 C  C    . ILE   B 1 40  ? -50.256 3.428   -9.086  1.00 14.71 ? 19  ILE   B C    1 
ATOM   2103 O  O    . ILE   B 1 40  ? -49.521 2.584   -9.573  1.00 14.93 ? 19  ILE   B O    1 
ATOM   2104 C  CB   . ILE   B 1 40  ? -50.535 3.637   -6.566  1.00 13.40 ? 19  ILE   B CB   1 
ATOM   2105 C  CG1  . ILE   B 1 40  ? -49.891 4.215   -5.290  1.00 14.76 ? 19  ILE   B CG1  1 
ATOM   2106 C  CG2  . ILE   B 1 40  ? -50.497 2.107   -6.554  1.00 14.33 ? 19  ILE   B CG2  1 
ATOM   2107 C  CD1  . ILE   B 1 40  ? -50.742 4.057   -4.049  1.00 16.22 ? 19  ILE   B CD1  1 
ATOM   2108 N  N    . ALA   B 1 41  ? -51.460 3.730   -9.591  1.00 15.06 ? 20  ALA   B N    1 
ATOM   2109 C  CA   . ALA   B 1 41  ? -51.968 3.066   -10.782 1.00 15.49 ? 20  ALA   B CA   1 
ATOM   2110 C  C    . ALA   B 1 41  ? -51.045 3.286   -11.976 1.00 15.86 ? 20  ALA   B C    1 
ATOM   2111 O  O    . ALA   B 1 41  ? -50.744 2.345   -12.697 1.00 16.64 ? 20  ALA   B O    1 
ATOM   2112 C  CB   . ALA   B 1 41  ? -53.383 3.527   -11.078 1.00 16.57 ? 20  ALA   B CB   1 
ATOM   2113 N  N    . VAL   B 1 42  ? -50.584 4.530   -12.137 1.00 16.66 ? 21  VAL   B N    1 
ATOM   2114 C  CA   . VAL   B 1 42  ? -49.663 4.863   -13.216 1.00 15.88 ? 21  VAL   B CA   1 
ATOM   2115 C  C    . VAL   B 1 42  ? -48.352 4.095   -13.079 1.00 16.50 ? 21  VAL   B C    1 
ATOM   2116 O  O    . VAL   B 1 42  ? -47.856 3.536   -14.043 1.00 16.87 ? 21  VAL   B O    1 
ATOM   2117 C  CB   . VAL   B 1 42  ? -49.422 6.375   -13.323 1.00 15.78 ? 21  VAL   B CB   1 
ATOM   2118 C  CG1  . VAL   B 1 42  ? -48.269 6.675   -14.271 1.00 17.37 ? 21  VAL   B CG1  1 
ATOM   2119 C  CG2  . VAL   B 1 42  ? -50.687 7.146   -13.701 1.00 17.22 ? 21  VAL   B CG2  1 
ATOM   2120 N  N    . LYS   B 1 43  ? -47.759 4.054   -11.871 1.00 16.47 ? 22  LYS   B N    1 
ATOM   2121 C  CA   . LYS   B 1 43  ? -46.500 3.334   -11.726 1.00 15.99 ? 22  LYS   B CA   1 
ATOM   2122 C  C    . LYS   B 1 43  ? -46.672 1.835   -11.935 1.00 15.82 ? 22  LYS   B C    1 
ATOM   2123 O  O    . LYS   B 1 43  ? -45.784 1.208   -12.495 1.00 17.40 ? 22  LYS   B O    1 
ATOM   2124 C  CB   . LYS   B 1 43  ? -45.839 3.598   -10.366 1.00 18.91 ? 22  LYS   B CB   1 
ATOM   2125 C  CG   . LYS   B 1 43  ? -45.132 4.935   -10.313 1.00 22.11 ? 22  LYS   B CG   1 
ATOM   2126 C  CD   . LYS   B 1 43  ? -44.004 4.935   -9.276  1.00 23.55 ? 22  LYS   B CD   1 
ATOM   2127 C  CE   . LYS   B 1 43  ? -43.541 6.342   -9.146  1.00 26.13 ? 22  LYS   B CE   1 
ATOM   2128 N  NZ   . LYS   B 1 43  ? -42.422 6.598   -10.052 1.00 30.74 ? 22  LYS   B NZ   1 
ATOM   2129 N  N    . LEU   B 1 44  ? -47.784 1.263   -11.454 1.00 15.79 ? 23  LEU   B N    1 
ATOM   2130 C  CA   . LEU   B 1 44  ? -48.009 -0.154  -11.691 1.00 15.55 ? 23  LEU   B CA   1 
ATOM   2131 C  C    . LEU   B 1 44  ? -48.129 -0.383  -13.198 1.00 16.50 ? 23  LEU   B C    1 
ATOM   2132 O  O    . LEU   B 1 44  ? -47.565 -1.328  -13.723 1.00 16.89 ? 23  LEU   B O    1 
ATOM   2133 C  CB   . LEU   B 1 44  ? -49.282 -0.572  -10.969 1.00 15.80 ? 23  LEU   B CB   1 
ATOM   2134 C  CG   . LEU   B 1 44  ? -49.110 -0.778  -9.461  1.00 14.87 ? 23  LEU   B CG   1 
ATOM   2135 C  CD1  . LEU   B 1 44  ? -50.488 -0.865  -8.816  1.00 16.41 ? 23  LEU   B CD1  1 
ATOM   2136 C  CD2  . LEU   B 1 44  ? -48.312 -2.052  -9.202  1.00 18.10 ? 23  LEU   B CD2  1 
ATOM   2137 N  N    . HIS   B 1 45  ? -48.872 0.492   -13.880 1.00 16.34 ? 24  HIS   B N    1 
ATOM   2138 C  CA   . HIS   B 1 45  ? -49.068 0.341   -15.319 1.00 17.69 ? 24  HIS   B CA   1 
ATOM   2139 C  C    . HIS   B 1 45  ? -47.724 0.448   -16.042 1.00 18.57 ? 24  HIS   B C    1 
ATOM   2140 O  O    . HIS   B 1 45  ? -47.414 -0.342  -16.941 1.00 18.25 ? 24  HIS   B O    1 
ATOM   2141 C  CB   . HIS   B 1 45  ? -50.060 1.404   -15.802 1.00 17.33 ? 24  HIS   B CB   1 
ATOM   2142 C  CG   . HIS   B 1 45  ? -50.466 1.202   -17.222 1.00 19.79 ? 24  HIS   B CG   1 
ATOM   2143 N  ND1  . HIS   B 1 45  ? -49.806 1.827   -18.258 1.00 20.42 ? 24  HIS   B ND1  1 
ATOM   2144 C  CD2  . HIS   B 1 45  ? -51.424 0.442   -17.774 1.00 19.25 ? 24  HIS   B CD2  1 
ATOM   2145 C  CE1  . HIS   B 1 45  ? -50.361 1.458   -19.412 1.00 19.33 ? 24  HIS   B CE1  1 
ATOM   2146 N  NE2  . HIS   B 1 45  ? -51.353 0.635   -19.144 1.00 18.86 ? 24  HIS   B NE2  1 
ATOM   2147 N  N    . GLN   B 1 46  ? -46.900 1.421   -15.629 1.00 18.66 ? 25  GLN   B N    1 
ATOM   2148 C  CA   . GLN   B 1 46  ? -45.573 1.602   -16.208 1.00 19.14 ? 25  GLN   B CA   1 
ATOM   2149 C  C    . GLN   B 1 46  ? -44.676 0.388   -15.989 1.00 22.33 ? 25  GLN   B C    1 
ATOM   2150 O  O    . GLN   B 1 46  ? -43.774 0.147   -16.789 1.00 24.04 ? 25  GLN   B O    1 
ATOM   2151 C  CB   . GLN   B 1 46  ? -44.901 2.864   -15.673 1.00 20.77 ? 25  GLN   B CB   1 
ATOM   2152 C  CG   . GLN   B 1 46  ? -45.528 4.131   -16.229 1.00 23.04 ? 25  GLN   B CG   1 
ATOM   2153 C  CD   . GLN   B 1 46  ? -45.039 5.398   -15.570 1.00 26.86 ? 25  GLN   B CD   1 
ATOM   2154 O  OE1  . GLN   B 1 46  ? -44.510 5.387   -14.449 1.00 28.57 ? 25  GLN   B OE1  1 
ATOM   2155 N  NE2  . GLN   B 1 46  ? -45.270 6.511   -16.247 1.00 28.51 ? 25  GLN   B NE2  1 
ATOM   2156 N  N    . THR   B 1 47  ? -44.909 -0.354  -14.899 1.00 21.12 ? 26  THR   B N    1 
ATOM   2157 C  CA   . THR   B 1 47  ? -44.152 -1.543  -14.535 1.00 21.88 ? 26  THR   B CA   1 
ATOM   2158 C  C    . THR   B 1 47  ? -44.622 -2.738  -15.361 1.00 22.62 ? 26  THR   B C    1 
ATOM   2159 O  O    . THR   B 1 47  ? -43.944 -3.758  -15.391 1.00 24.77 ? 26  THR   B O    1 
ATOM   2160 C  CB   . THR   B 1 47  ? -44.337 -1.793  -13.030 1.00 22.85 ? 26  THR   B CB   1 
ATOM   2161 O  OG1  . THR   B 1 47  ? -43.816 -0.644  -12.371 1.00 26.74 ? 26  THR   B OG1  1 
ATOM   2162 C  CG2  . THR   B 1 47  ? -43.612 -3.019  -12.512 1.00 26.35 ? 26  THR   B CG2  1 
ATOM   2163 N  N    . GLY   B 1 48  ? -45.796 -2.641  -16.009 1.00 22.06 ? 27  GLY   B N    1 
ATOM   2164 C  CA   . GLY   B 1 48  ? -46.287 -3.746  -16.832 1.00 20.12 ? 27  GLY   B CA   1 
ATOM   2165 C  C    . GLY   B 1 48  ? -47.628 -4.330  -16.365 1.00 20.59 ? 27  GLY   B C    1 
ATOM   2166 O  O    . GLY   B 1 48  ? -48.103 -5.319  -16.933 1.00 20.15 ? 27  GLY   B O    1 
ATOM   2167 N  N    . TYR   B 1 49  ? -48.228 -3.752  -15.316 1.00 18.20 ? 28  TYR   B N    1 
ATOM   2168 C  CA   . TYR   B 1 49  ? -49.514 -4.245  -14.833 1.00 17.91 ? 28  TYR   B CA   1 
ATOM   2169 C  C    . TYR   B 1 49  ? -50.658 -3.704  -15.683 1.00 17.75 ? 28  TYR   B C    1 
ATOM   2170 O  O    . TYR   B 1 49  ? -50.627 -2.554  -16.109 1.00 18.43 ? 28  TYR   B O    1 
ATOM   2171 C  CB   . TYR   B 1 49  ? -49.825 -3.796  -13.394 1.00 17.36 ? 28  TYR   B CB   1 
ATOM   2172 C  CG   . TYR   B 1 49  ? -49.044 -4.583  -12.352 1.00 17.99 ? 28  TYR   B CG   1 
ATOM   2173 C  CD1  . TYR   B 1 49  ? -47.707 -4.290  -12.106 1.00 18.51 ? 28  TYR   B CD1  1 
ATOM   2174 C  CD2  . TYR   B 1 49  ? -49.627 -5.647  -11.660 1.00 19.33 ? 28  TYR   B CD2  1 
ATOM   2175 C  CE1  . TYR   B 1 49  ? -46.980 -4.997  -11.162 1.00 18.86 ? 28  TYR   B CE1  1 
ATOM   2176 C  CE2  . TYR   B 1 49  ? -48.901 -6.377  -10.727 1.00 19.69 ? 28  TYR   B CE2  1 
ATOM   2177 C  CZ   . TYR   B 1 49  ? -47.569 -6.058  -10.505 1.00 19.88 ? 28  TYR   B CZ   1 
ATOM   2178 O  OH   . TYR   B 1 49  ? -46.818 -6.754  -9.594  1.00 21.89 ? 28  TYR   B OH   1 
ATOM   2179 N  N    . ARG   B 1 50  ? -51.701 -4.526  -15.834 1.00 16.87 ? 29  ARG   B N    1 
ATOM   2180 C  CA   . ARG   B 1 50  ? -53.010 -3.993  -16.177 1.00 16.94 ? 29  ARG   B CA   1 
ATOM   2181 C  C    . ARG   B 1 50  ? -53.660 -3.510  -14.880 1.00 16.80 ? 29  ARG   B C    1 
ATOM   2182 O  O    . ARG   B 1 50  ? -53.377 -4.052  -13.805 1.00 17.53 ? 29  ARG   B O    1 
ATOM   2183 C  CB   . ARG   B 1 50  ? -53.899 -5.041  -16.853 1.00 17.96 ? 29  ARG   B CB   1 
ATOM   2184 C  CG   . ARG   B 1 50  ? -53.493 -5.399  -18.276 1.00 20.11 ? 29  ARG   B CG   1 
ATOM   2185 C  CD   . ARG   B 1 50  ? -52.400 -6.436  -18.323 1.00 21.94 ? 29  ARG   B CD   1 
ATOM   2186 N  NE   . ARG   B 1 50  ? -52.760 -7.718  -17.697 1.00 21.96 ? 29  ARG   B NE   1 
ATOM   2187 C  CZ   . ARG   B 1 50  ? -53.621 -8.646  -18.116 1.00 22.95 ? 29  ARG   B CZ   1 
ATOM   2188 N  NH1  . ARG   B 1 50  ? -54.428 -8.456  -19.146 1.00 25.40 ? 29  ARG   B NH1  1 
ATOM   2189 N  NH2  . ARG   B 1 50  ? -53.689 -9.797  -17.464 1.00 23.49 ? 29  ARG   B NH2  1 
ATOM   2190 N  N    . VAL   B 1 51  ? -54.523 -2.487  -14.967 1.00 15.46 ? 30  VAL   B N    1 
ATOM   2191 C  CA   . VAL   B 1 51  ? -55.083 -1.899  -13.753 1.00 15.76 ? 30  VAL   B CA   1 
ATOM   2192 C  C    . VAL   B 1 51  ? -56.596 -1.700  -13.836 1.00 15.22 ? 30  VAL   B C    1 
ATOM   2193 O  O    . VAL   B 1 51  ? -57.139 -1.314  -14.883 1.00 15.46 ? 30  VAL   B O    1 
ATOM   2194 C  CB   . VAL   B 1 51  ? -54.399 -0.555  -13.427 1.00 16.18 ? 30  VAL   B CB   1 
ATOM   2195 C  CG1  . VAL   B 1 51  ? -52.908 -0.736  -13.212 1.00 15.35 ? 30  VAL   B CG1  1 
ATOM   2196 C  CG2  . VAL   B 1 51  ? -54.626 0.499   -14.509 1.00 17.47 ? 30  VAL   B CG2  1 
ATOM   2197 N  N    . VAL   B 1 52  ? -57.268 -1.930  -12.706 1.00 14.10 ? 31  VAL   B N    1 
ATOM   2198 C  CA   . VAL   B 1 52  ? -58.612 -1.435  -12.430 1.00 14.54 ? 31  VAL   B CA   1 
ATOM   2199 C  C    . VAL   B 1 52  ? -58.495 -0.138  -11.638 1.00 15.78 ? 31  VAL   B C    1 
ATOM   2200 O  O    . VAL   B 1 52  ? -57.947 -0.128  -10.522 1.00 15.63 ? 31  VAL   B O    1 
ATOM   2201 C  CB   . VAL   B 1 52  ? -59.459 -2.446  -11.636 1.00 15.91 ? 31  VAL   B CB   1 
ATOM   2202 C  CG1  . VAL   B 1 52  ? -60.836 -1.876  -11.303 1.00 16.65 ? 31  VAL   B CG1  1 
ATOM   2203 C  CG2  . VAL   B 1 52  ? -59.542 -3.796  -12.335 1.00 16.80 ? 31  VAL   B CG2  1 
ATOM   2204 N  N    . ILE   B 1 53  ? -59.030 0.947   -12.208 1.00 14.86 ? 32  ILE   B N    1 
ATOM   2205 C  CA   . ILE   B 1 53  ? -59.085 2.236   -11.544 1.00 16.01 ? 32  ILE   B CA   1 
ATOM   2206 C  C    . ILE   B 1 53  ? -60.443 2.353   -10.868 1.00 16.21 ? 32  ILE   B C    1 
ATOM   2207 O  O    . ILE   B 1 53  ? -61.445 2.603   -11.538 1.00 16.07 ? 32  ILE   B O    1 
ATOM   2208 C  CB   . ILE   B 1 53  ? -58.870 3.328   -12.601 1.00 17.80 ? 32  ILE   B CB   1 
ATOM   2209 C  CG1  . ILE   B 1 53  ? -57.469 3.183   -13.200 1.00 21.54 ? 32  ILE   B CG1  1 
ATOM   2210 C  CG2  . ILE   B 1 53  ? -59.105 4.720   -12.008 1.00 18.72 ? 32  ILE   B CG2  1 
ATOM   2211 C  CD1  . ILE   B 1 53  ? -57.259 3.918   -14.503 1.00 26.03 ? 32  ILE   B CD1  1 
ATOM   2212 N  N    . HIS   B 1 54  ? -60.476 2.130   -9.554  1.00 14.83 ? 33  HIS   B N    1 
ATOM   2213 C  CA   . HIS   B 1 54  ? -61.724 2.314   -8.834  1.00 15.20 ? 33  HIS   B CA   1 
ATOM   2214 C  C    . HIS   B 1 54  ? -61.874 3.790   -8.497  1.00 16.28 ? 33  HIS   B C    1 
ATOM   2215 O  O    . HIS   B 1 54  ? -60.887 4.487   -8.248  1.00 16.64 ? 33  HIS   B O    1 
ATOM   2216 C  CB   . HIS   B 1 54  ? -61.744 1.434   -7.581  1.00 16.34 ? 33  HIS   B CB   1 
ATOM   2217 C  CG   . HIS   B 1 54  ? -62.704 1.966   -6.582  1.00 16.17 ? 33  HIS   B CG   1 
ATOM   2218 N  ND1  . HIS   B 1 54  ? -62.264 2.842   -5.613  1.00 15.94 ? 33  HIS   B ND1  1 
ATOM   2219 C  CD2  . HIS   B 1 54  ? -64.029 1.810   -6.392  1.00 16.35 ? 33  HIS   B CD2  1 
ATOM   2220 C  CE1  . HIS   B 1 54  ? -63.303 3.227   -4.881  1.00 17.09 ? 33  HIS   B CE1  1 
ATOM   2221 N  NE2  . HIS   B 1 54  ? -64.378 2.602   -5.335  1.00 16.84 ? 33  HIS   B NE2  1 
ATOM   2222 N  N    . TYR   B 1 55  ? -63.131 4.242   -8.443  1.00 15.81 ? 34  TYR   B N    1 
ATOM   2223 C  CA   . TYR   B 1 55  ? -63.401 5.623   -8.077  1.00 16.67 ? 34  TYR   B CA   1 
ATOM   2224 C  C    . TYR   B 1 55  ? -64.808 5.711   -7.501  1.00 16.06 ? 34  TYR   B C    1 
ATOM   2225 O  O    . TYR   B 1 55  ? -65.557 4.742   -7.570  1.00 16.60 ? 34  TYR   B O    1 
ATOM   2226 C  CB   . TYR   B 1 55  ? -63.257 6.536   -9.297  1.00 16.94 ? 34  TYR   B CB   1 
ATOM   2227 C  CG   . TYR   B 1 55  ? -64.340 6.334   -10.347 1.00 18.07 ? 34  TYR   B CG   1 
ATOM   2228 C  CD1  . TYR   B 1 55  ? -64.315 5.249   -11.222 1.00 17.97 ? 34  TYR   B CD1  1 
ATOM   2229 C  CD2  . TYR   B 1 55  ? -65.420 7.206   -10.400 1.00 19.37 ? 34  TYR   B CD2  1 
ATOM   2230 C  CE1  . TYR   B 1 55  ? -65.314 5.058   -12.171 1.00 19.86 ? 34  TYR   B CE1  1 
ATOM   2231 C  CE2  . TYR   B 1 55  ? -66.421 7.028   -11.341 1.00 19.13 ? 34  TYR   B CE2  1 
ATOM   2232 C  CZ   . TYR   B 1 55  ? -66.360 5.970   -12.233 1.00 20.10 ? 34  TYR   B CZ   1 
ATOM   2233 O  OH   . TYR   B 1 55  ? -67.381 5.836   -13.125 1.00 23.84 ? 34  TYR   B OH   1 
ATOM   2234 N  N    . HIS   B 1 56  ? -65.114 6.872   -6.907  1.00 18.07 ? 35  HIS   B N    1 
ATOM   2235 C  CA   . HIS   B 1 56  ? -66.423 7.107   -6.337  1.00 20.97 ? 35  HIS   B CA   1 
ATOM   2236 C  C    . HIS   B 1 56  ? -67.050 8.303   -7.048  1.00 20.93 ? 35  HIS   B C    1 
ATOM   2237 O  O    . HIS   B 1 56  ? -67.961 8.098   -7.849  1.00 25.85 ? 35  HIS   B O    1 
ATOM   2238 C  CB   . HIS   B 1 56  ? -66.338 7.203   -4.809  1.00 21.70 ? 35  HIS   B CB   1 
ATOM   2239 C  CG   . HIS   B 1 56  ? -67.651 7.502   -4.175  1.00 24.87 ? 35  HIS   B CG   1 
ATOM   2240 N  ND1  . HIS   B 1 56  ? -67.764 8.391   -3.126  1.00 28.35 ? 35  HIS   B ND1  1 
ATOM   2241 C  CD2  . HIS   B 1 56  ? -68.879 7.051   -4.432  1.00 24.50 ? 35  HIS   B CD2  1 
ATOM   2242 C  CE1  . HIS   B 1 56  ? -69.037 8.481   -2.774  1.00 27.36 ? 35  HIS   B CE1  1 
ATOM   2243 N  NE2  . HIS   B 1 56  ? -69.736 7.662   -3.547  1.00 29.29 ? 35  HIS   B NE2  1 
ATOM   2244 N  N    . ASN   B 1 57  ? -66.550 9.516   -6.794  1.00 24.07 ? 36  ASN   B N    1 
ATOM   2245 C  CA   . ASN   B 1 57  ? -67.176 10.701  -7.374  1.00 28.44 ? 36  ASN   B CA   1 
ATOM   2246 C  C    . ASN   B 1 57  ? -66.376 11.278  -8.539  1.00 31.75 ? 36  ASN   B C    1 
ATOM   2247 O  O    . ASN   B 1 57  ? -66.878 12.149  -9.247  1.00 35.17 ? 36  ASN   B O    1 
ATOM   2248 C  CB   . ASN   B 1 57  ? -67.407 11.803  -6.351  1.00 28.22 ? 36  ASN   B CB   1 
ATOM   2249 C  CG   . ASN   B 1 57  ? -68.427 11.420  -5.303  1.00 31.41 ? 36  ASN   B CG   1 
ATOM   2250 O  OD1  . ASN   B 1 57  ? -69.487 10.865  -5.626  1.00 32.32 ? 36  ASN   B OD1  1 
ATOM   2251 N  ND2  . ASN   B 1 57  ? -68.107 11.680  -4.046  1.00 31.98 ? 36  ASN   B ND2  1 
ATOM   2252 N  N    . SER   B 1 58  ? -65.134 10.823  -8.741  1.00 29.19 ? 37  SER   B N    1 
ATOM   2253 C  CA   . SER   B 1 58  ? -64.267 11.503  -9.692  1.00 29.00 ? 37  SER   B CA   1 
ATOM   2254 C  C    . SER   B 1 58  ? -64.297 10.792  -11.045 1.00 28.27 ? 37  SER   B C    1 
ATOM   2255 O  O    . SER   B 1 58  ? -63.274 10.311  -11.539 1.00 25.30 ? 37  SER   B O    1 
ATOM   2256 C  CB   . SER   B 1 58  ? -62.858 11.661  -9.144  1.00 26.77 ? 37  SER   B CB   1 
ATOM   2257 O  OG   . SER   B 1 58  ? -62.819 12.528  -8.016  1.00 28.28 ? 37  SER   B OG   1 
ATOM   2258 N  N    . ALA   B 1 59  ? -65.492 10.755  -11.651 1.00 28.06 ? 38  ALA   B N    1 
ATOM   2259 C  CA   . ALA   B 1 59  ? -65.772 9.955   -12.834 1.00 27.49 ? 38  ALA   B CA   1 
ATOM   2260 C  C    . ALA   B 1 59  ? -64.958 10.413  -14.045 1.00 24.12 ? 38  ALA   B C    1 
ATOM   2261 O  O    . ALA   B 1 59  ? -64.337 9.586   -14.717 1.00 23.76 ? 38  ALA   B O    1 
ATOM   2262 C  CB   . ALA   B 1 59  ? -67.258 9.945   -13.113 1.00 27.87 ? 38  ALA   B CB   1 
ATOM   2263 N  N    . GLU   B 1 60  ? -64.941 11.727  -14.295 1.00 24.67 ? 39  GLU   B N    1 
ATOM   2264 C  CA   . GLU   B 1 60  ? -64.194 12.266  -15.422 1.00 24.56 ? 39  GLU   B CA   1 
ATOM   2265 C  C    . GLU   B 1 60  ? -62.705 11.953  -15.269 1.00 24.53 ? 39  GLU   B C    1 
ATOM   2266 O  O    . GLU   B 1 60  ? -62.070 11.517  -16.225 1.00 22.94 ? 39  GLU   B O    1 
ATOM   2267 C  CB   . GLU   B 1 60  ? -64.432 13.772  -15.537 1.00 26.76 ? 39  GLU   B CB   1 
ATOM   2268 C  CG   . GLU   B 1 60  ? -63.577 14.443  -16.607 1.00 31.67 ? 39  GLU   B CG   1 
ATOM   2269 C  CD   A GLU   B 1 60  ? -64.098 15.835  -16.900 0.50 32.92 ? 39  GLU   B CD   1 
ATOM   2270 O  OE1  A GLU   B 1 60  ? -64.264 16.618  -15.942 0.50 33.39 ? 39  GLU   B OE1  1 
ATOM   2271 O  OE2  A GLU   B 1 60  ? -64.345 16.122  -18.089 0.50 31.72 ? 39  GLU   B OE2  1 
ATOM   2272 N  N    . ALA   B 1 61  ? -62.150 12.184  -14.069 1.00 21.72 ? 40  ALA   B N    1 
ATOM   2273 C  CA   . ALA   B 1 61  ? -60.731 11.943  -13.830 1.00 20.27 ? 40  ALA   B CA   1 
ATOM   2274 C  C    . ALA   B 1 61  ? -60.404 10.459  -13.996 1.00 19.30 ? 40  ALA   B C    1 
ATOM   2275 O  O    . ALA   B 1 61  ? -59.359 10.113  -14.546 1.00 19.44 ? 40  ALA   B O    1 
ATOM   2276 C  CB   . ALA   B 1 61  ? -60.345 12.427  -12.442 1.00 21.21 ? 40  ALA   B CB   1 
ATOM   2277 N  N    . ALA   B 1 62  ? -61.285 9.578   -13.519 1.00 19.24 ? 41  ALA   B N    1 
ATOM   2278 C  CA   . ALA   B 1 62  ? -61.032 8.143   -13.624 1.00 18.46 ? 41  ALA   B CA   1 
ATOM   2279 C  C    . ALA   B 1 62  ? -61.049 7.659   -15.071 1.00 18.52 ? 41  ALA   B C    1 
ATOM   2280 O  O    . ALA   B 1 62  ? -60.149 6.935   -15.507 1.00 17.33 ? 41  ALA   B O    1 
ATOM   2281 C  CB   . ALA   B 1 62  ? -62.041 7.378   -12.799 1.00 19.26 ? 41  ALA   B CB   1 
ATOM   2282 N  N    . VAL   B 1 63  ? -62.097 8.067   -15.800 1.00 18.40 ? 42  VAL   B N    1 
ATOM   2283 C  CA   . VAL   B 1 63  ? -62.226 7.696   -17.200 1.00 18.84 ? 42  VAL   B CA   1 
ATOM   2284 C  C    . VAL   B 1 63  ? -61.070 8.270   -18.018 1.00 18.02 ? 42  VAL   B C    1 
ATOM   2285 O  O    . VAL   B 1 63  ? -60.505 7.547   -18.836 1.00 18.56 ? 42  VAL   B O    1 
ATOM   2286 C  CB   . VAL   B 1 63  ? -63.610 8.030   -17.787 1.00 18.74 ? 42  VAL   B CB   1 
ATOM   2287 C  CG1  . VAL   B 1 63  ? -63.665 7.865   -19.304 1.00 20.25 ? 42  VAL   B CG1  1 
ATOM   2288 C  CG2  . VAL   B 1 63  ? -64.675 7.162   -17.121 1.00 21.33 ? 42  VAL   B CG2  1 
ATOM   2289 N  N    . SER   B 1 64  ? -60.705 9.538   -17.770 1.00 18.49 ? 43  SER   B N    1 
ATOM   2290 C  CA   A SER   B 1 64  ? -59.589 10.188  -18.450 0.70 19.27 ? 43  SER   B CA   1 
ATOM   2291 C  CA   B SER   B 1 64  ? -59.608 10.135  -18.513 0.30 17.98 ? 43  SER   B CA   1 
ATOM   2292 C  C    . SER   B 1 64  ? -58.287 9.423   -18.215 1.00 18.34 ? 43  SER   B C    1 
ATOM   2293 O  O    . SER   B 1 64  ? -57.485 9.214   -19.119 1.00 18.30 ? 43  SER   B O    1 
ATOM   2294 C  CB   A SER   B 1 64  ? -59.421 11.628  -17.986 0.70 22.15 ? 43  SER   B CB   1 
ATOM   2295 C  CB   B SER   B 1 64  ? -59.524 11.624  -18.291 0.30 17.92 ? 43  SER   B CB   1 
ATOM   2296 O  OG   A SER   B 1 64  ? -60.585 12.407  -18.214 0.70 28.11 ? 43  SER   B OG   1 
ATOM   2297 O  OG   B SER   B 1 64  ? -58.393 12.175  -18.951 0.30 18.72 ? 43  SER   B OG   1 
ATOM   2298 N  N    . LEU   B 1 65  ? -58.045 9.040   -16.952 1.00 17.22 ? 44  LEU   B N    1 
ATOM   2299 C  CA   . LEU   B 1 65  ? -56.825 8.308   -16.633 1.00 17.31 ? 44  LEU   B CA   1 
ATOM   2300 C  C    . LEU   B 1 65  ? -56.767 6.981   -17.382 1.00 16.65 ? 44  LEU   B C    1 
ATOM   2301 O  O    . LEU   B 1 65  ? -55.767 6.640   -18.024 1.00 16.93 ? 44  LEU   B O    1 
ATOM   2302 C  CB   . LEU   B 1 65  ? -56.706 8.064   -15.125 1.00 17.88 ? 44  LEU   B CB   1 
ATOM   2303 C  CG   . LEU   B 1 65  ? -55.572 7.117   -14.711 1.00 19.08 ? 44  LEU   B CG   1 
ATOM   2304 C  CD1  . LEU   B 1 65  ? -54.205 7.649   -15.115 1.00 20.42 ? 44  LEU   B CD1  1 
ATOM   2305 C  CD2  . LEU   B 1 65  ? -55.627 6.963   -13.202 1.00 21.65 ? 44  LEU   B CD2  1 
ATOM   2306 N  N    . ALA   B 1 66  ? -57.862 6.219   -17.305 1.00 16.83 ? 45  ALA   B N    1 
ATOM   2307 C  CA   . ALA   B 1 66  ? -57.888 4.923   -17.964 1.00 15.94 ? 45  ALA   B CA   1 
ATOM   2308 C  C    . ALA   B 1 66  ? -57.705 5.076   -19.480 1.00 17.42 ? 45  ALA   B C    1 
ATOM   2309 O  O    . ALA   B 1 66  ? -57.048 4.238   -20.100 1.00 18.18 ? 45  ALA   B O    1 
ATOM   2310 C  CB   . ALA   B 1 66  ? -59.155 4.181   -17.605 1.00 16.85 ? 45  ALA   B CB   1 
ATOM   2311 N  N    . ASP   B 1 67  ? -58.224 6.182   -20.029 1.00 17.43 ? 46  ASP   B N    1 
ATOM   2312 C  CA   . ASP   B 1 67  ? -58.103 6.468   -21.455 1.00 18.34 ? 46  ASP   B CA   1 
ATOM   2313 C  C    . ASP   B 1 67  ? -56.630 6.669   -21.797 1.00 18.49 ? 46  ASP   B C    1 
ATOM   2314 O  O    . ASP   B 1 67  ? -56.129 6.092   -22.769 1.00 18.57 ? 46  ASP   B O    1 
ATOM   2315 C  CB   . ASP   B 1 67  ? -58.974 7.661   -21.826 1.00 19.11 ? 46  ASP   B CB   1 
ATOM   2316 C  CG   . ASP   B 1 67  ? -59.026 8.054   -23.298 1.00 23.36 ? 46  ASP   B CG   1 
ATOM   2317 O  OD1  . ASP   B 1 67  ? -58.987 7.164   -24.162 1.00 26.95 ? 46  ASP   B OD1  1 
ATOM   2318 O  OD2  . ASP   B 1 67  ? -59.146 9.251   -23.550 1.00 29.51 ? 46  ASP   B OD2  1 
ATOM   2319 N  N    . GLU   B 1 68  ? -55.938 7.488   -20.997 1.00 18.16 ? 47  GLU   B N    1 
ATOM   2320 C  CA   . GLU   B 1 68  ? -54.514 7.732   -21.232 1.00 20.23 ? 47  GLU   B CA   1 
ATOM   2321 C  C    . GLU   B 1 68  ? -53.696 6.440   -21.154 1.00 20.59 ? 47  GLU   B C    1 
ATOM   2322 O  O    . GLU   B 1 68  ? -52.798 6.213   -21.963 1.00 19.68 ? 47  GLU   B O    1 
ATOM   2323 C  CB   . GLU   B 1 68  ? -53.963 8.742   -20.227 1.00 23.36 ? 47  GLU   B CB   1 
ATOM   2324 C  CG   A GLU   B 1 68  ? -54.528 10.149  -20.395 0.50 25.70 ? 47  GLU   B CG   1 
ATOM   2325 C  CD   A GLU   B 1 68  ? -54.013 11.119  -19.349 0.50 30.86 ? 47  GLU   B CD   1 
ATOM   2326 O  OE1  A GLU   B 1 68  ? -52.937 10.850  -18.767 0.50 33.55 ? 47  GLU   B OE1  1 
ATOM   2327 O  OE2  A GLU   B 1 68  ? -54.704 12.131  -19.093 0.50 34.07 ? 47  GLU   B OE2  1 
ATOM   2328 N  N    . LEU   B 1 69  ? -54.002 5.570   -20.180 1.00 17.61 ? 48  LEU   B N    1 
ATOM   2329 C  CA   . LEU   B 1 69  ? -53.287 4.313   -20.044 1.00 17.16 ? 48  LEU   B CA   1 
ATOM   2330 C  C    . LEU   B 1 69  ? -53.576 3.396   -21.230 1.00 18.55 ? 48  LEU   B C    1 
ATOM   2331 O  O    . LEU   B 1 69  ? -52.664 2.738   -21.712 1.00 17.30 ? 48  LEU   B O    1 
ATOM   2332 C  CB   . LEU   B 1 69  ? -53.617 3.660   -18.699 1.00 17.86 ? 48  LEU   B CB   1 
ATOM   2333 C  CG   . LEU   B 1 69  ? -53.208 4.476   -17.471 1.00 19.51 ? 48  LEU   B CG   1 
ATOM   2334 C  CD1  . LEU   B 1 69  ? -53.608 3.684   -16.222 1.00 20.03 ? 48  LEU   B CD1  1 
ATOM   2335 C  CD2  . LEU   B 1 69  ? -51.709 4.806   -17.506 1.00 18.85 ? 48  LEU   B CD2  1 
ATOM   2336 N  N    . ASN   B 1 70  ? -54.828 3.383   -21.709 1.00 18.22 ? 49  ASN   B N    1 
ATOM   2337 C  CA   . ASN   B 1 70  ? -55.203 2.547   -22.842 1.00 18.23 ? 49  ASN   B CA   1 
ATOM   2338 C  C    . ASN   B 1 70  ? -54.552 3.053   -24.135 1.00 18.88 ? 49  ASN   B C    1 
ATOM   2339 O  O    . ASN   B 1 70  ? -54.222 2.258   -25.015 1.00 19.47 ? 49  ASN   B O    1 
ATOM   2340 C  CB   . ASN   B 1 70  ? -56.718 2.432   -22.926 1.00 17.81 ? 49  ASN   B CB   1 
ATOM   2341 C  CG   . ASN   B 1 70  ? -57.252 1.444   -21.913 1.00 17.72 ? 49  ASN   B CG   1 
ATOM   2342 O  OD1  . ASN   B 1 70  ? -56.531 0.541   -21.492 1.00 19.24 ? 49  ASN   B OD1  1 
ATOM   2343 N  ND2  . ASN   B 1 70  ? -58.492 1.609   -21.495 1.00 16.61 ? 49  ASN   B ND2  1 
ATOM   2344 N  N    . LYS   B 1 71  ? -54.360 4.371   -24.235 1.00 20.68 ? 50  LYS   B N    1 
ATOM   2345 C  CA   . LYS   B 1 71  ? -53.660 4.934   -25.380 1.00 21.35 ? 50  LYS   B CA   1 
ATOM   2346 C  C    . LYS   B 1 71  ? -52.200 4.485   -25.388 1.00 23.59 ? 50  LYS   B C    1 
ATOM   2347 O  O    . LYS   B 1 71  ? -51.611 4.338   -26.459 1.00 27.25 ? 50  LYS   B O    1 
ATOM   2348 C  CB   . LYS   B 1 71  ? -53.807 6.456   -25.426 1.00 21.98 ? 50  LYS   B CB   1 
ATOM   2349 C  CG   . LYS   B 1 71  ? -55.166 6.909   -25.930 1.00 23.89 ? 50  LYS   B CG   1 
ATOM   2350 C  CD   . LYS   B 1 71  ? -55.194 8.423   -25.783 1.00 30.08 ? 50  LYS   B CD   1 
ATOM   2351 C  CE   . LYS   B 1 71  ? -56.498 9.007   -26.145 1.00 33.15 ? 50  LYS   B CE   1 
ATOM   2352 N  NZ   . LYS   B 1 71  ? -56.644 10.301  -25.464 1.00 35.55 ? 50  LYS   B NZ   1 
ATOM   2353 N  N    . GLU   B 1 72  ? -51.615 4.246   -24.207 1.00 23.46 ? 51  GLU   B N    1 
ATOM   2354 C  CA   A GLU   B 1 72  ? -50.265 3.712   -24.119 0.50 23.64 ? 51  GLU   B CA   1 
ATOM   2355 C  CA   B GLU   B 1 72  ? -50.265 3.714   -24.124 0.50 23.45 ? 51  GLU   B CA   1 
ATOM   2356 C  C    . GLU   B 1 72  ? -50.240 2.243   -24.543 1.00 22.90 ? 51  GLU   B C    1 
ATOM   2357 O  O    . GLU   B 1 72  ? -49.390 1.841   -25.340 1.00 25.36 ? 51  GLU   B O    1 
ATOM   2358 C  CB   A GLU   B 1 72  ? -49.684 3.899   -22.716 0.50 24.68 ? 51  GLU   B CB   1 
ATOM   2359 C  CB   B GLU   B 1 72  ? -49.665 3.947   -22.737 0.50 24.16 ? 51  GLU   B CB   1 
ATOM   2360 C  CG   A GLU   B 1 72  ? -48.260 3.367   -22.572 0.50 28.58 ? 51  GLU   B CG   1 
ATOM   2361 C  CG   B GLU   B 1 72  ? -49.551 5.425   -22.381 0.50 27.30 ? 51  GLU   B CG   1 
ATOM   2362 C  CD   A GLU   B 1 72  ? -47.228 4.175   -23.334 0.50 30.87 ? 51  GLU   B CD   1 
ATOM   2363 C  CD   B GLU   B 1 72  ? -48.650 6.227   -23.302 0.50 30.93 ? 51  GLU   B CD   1 
ATOM   2364 O  OE1  A GLU   B 1 72  ? -47.213 5.410   -23.140 0.50 32.14 ? 51  GLU   B OE1  1 
ATOM   2365 O  OE1  B GLU   B 1 72  ? -47.796 5.621   -23.988 0.50 30.89 ? 51  GLU   B OE1  1 
ATOM   2366 O  OE2  A GLU   B 1 72  ? -46.440 3.580   -24.103 0.50 33.07 ? 51  GLU   B OE2  1 
ATOM   2367 O  OE2  B GLU   B 1 72  ? -48.824 7.462   -23.352 0.50 32.34 ? 51  GLU   B OE2  1 
ATOM   2368 N  N    . ARG   B 1 73  ? -51.140 1.423   -23.981 1.00 21.20 ? 52  ARG   B N    1 
ATOM   2369 C  CA   . ARG   B 1 73  ? -51.213 -0.002  -24.296 1.00 21.64 ? 52  ARG   B CA   1 
ATOM   2370 C  C    . ARG   B 1 73  ? -52.681 -0.420  -24.292 1.00 22.14 ? 52  ARG   B C    1 
ATOM   2371 O  O    . ARG   B 1 73  ? -53.354 -0.309  -23.272 1.00 21.19 ? 52  ARG   B O    1 
ATOM   2372 C  CB   . ARG   B 1 73  ? -50.482 -0.899  -23.282 1.00 24.58 ? 52  ARG   B CB   1 
ATOM   2373 C  CG   . ARG   B 1 73  ? -48.997 -0.645  -23.067 1.00 28.10 ? 52  ARG   B CG   1 
ATOM   2374 C  CD   . ARG   B 1 73  ? -48.274 -1.829  -22.425 1.00 28.35 ? 52  ARG   B CD   1 
ATOM   2375 N  NE   . ARG   B 1 73  ? -48.798 -2.291  -21.136 1.00 27.10 ? 52  ARG   B NE   1 
ATOM   2376 C  CZ   . ARG   B 1 73  ? -48.601 -1.728  -19.943 1.00 30.87 ? 52  ARG   B CZ   1 
ATOM   2377 N  NH1  . ARG   B 1 73  ? -47.885 -0.620  -19.829 1.00 29.66 ? 52  ARG   B NH1  1 
ATOM   2378 N  NH2  . ARG   B 1 73  ? -49.129 -2.293  -18.870 1.00 28.88 ? 52  ARG   B NH2  1 
ATOM   2379 N  N    . SER   B 1 74  ? -53.202 -0.887  -25.436 1.00 22.37 ? 53  SER   B N    1 
ATOM   2380 C  CA   . SER   B 1 74  ? -54.646 -1.066  -25.572 1.00 23.39 ? 53  SER   B CA   1 
ATOM   2381 C  C    . SER   B 1 74  ? -55.235 -1.996  -24.510 1.00 20.02 ? 53  SER   B C    1 
ATOM   2382 O  O    . SER   B 1 74  ? -54.687 -3.062  -24.257 1.00 21.22 ? 53  SER   B O    1 
ATOM   2383 C  CB   . SER   B 1 74  ? -55.004 -1.608  -26.944 1.00 29.90 ? 53  SER   B CB   1 
ATOM   2384 O  OG   . SER   B 1 74  ? -54.297 -0.932  -27.976 1.00 34.72 ? 53  SER   B OG   1 
ATOM   2385 N  N    . ASN   B 1 75  ? -56.398 -1.605  -23.966 1.00 22.76 ? 54  ASN   B N    1 
ATOM   2386 C  CA   . ASN   B 1 75  ? -57.213 -2.431  -23.078 1.00 21.55 ? 54  ASN   B CA   1 
ATOM   2387 C  C    . ASN   B 1 75  ? -56.424 -2.939  -21.871 1.00 20.68 ? 54  ASN   B C    1 
ATOM   2388 O  O    . ASN   B 1 75  ? -56.613 -4.078  -21.435 1.00 19.58 ? 54  ASN   B O    1 
ATOM   2389 C  CB   . ASN   B 1 75  ? -57.882 -3.591  -23.810 1.00 22.06 ? 54  ASN   B CB   1 
ATOM   2390 C  CG   . ASN   B 1 75  ? -59.015 -3.080  -24.665 1.00 23.67 ? 54  ASN   B CG   1 
ATOM   2391 O  OD1  . ASN   B 1 75  ? -59.860 -2.314  -24.191 1.00 25.70 ? 54  ASN   B OD1  1 
ATOM   2392 N  ND2  . ASN   B 1 75  ? -59.069 -3.511  -25.917 1.00 21.97 ? 54  ASN   B ND2  1 
ATOM   2393 N  N    . THR   B 1 76  ? -55.583 -2.064  -21.317 1.00 17.79 ? 55  THR   B N    1 
ATOM   2394 C  CA   . THR   B 1 76  ? -54.829 -2.398  -20.106 1.00 16.74 ? 55  THR   B CA   1 
ATOM   2395 C  C    . THR   B 1 76  ? -55.355 -1.638  -18.889 1.00 17.37 ? 55  THR   B C    1 
ATOM   2396 O  O    . THR   B 1 76  ? -54.789 -1.774  -17.803 1.00 17.18 ? 55  THR   B O    1 
ATOM   2397 C  CB   . THR   B 1 76  ? -53.336 -2.136  -20.311 1.00 16.84 ? 55  THR   B CB   1 
ATOM   2398 O  OG1  . THR   B 1 76  ? -53.176 -0.752  -20.639 1.00 17.85 ? 55  THR   B OG1  1 
ATOM   2399 C  CG2  . THR   B 1 76  ? -52.726 -3.072  -21.336 1.00 18.97 ? 55  THR   B CG2  1 
ATOM   2400 N  N    . ALA   B 1 77  ? -56.435 -0.857  -19.041 1.00 15.59 ? 56  ALA   B N    1 
ATOM   2401 C  CA   . ALA   B 1 77  ? -57.054 -0.177  -17.916 1.00 15.53 ? 56  ALA   B CA   1 
ATOM   2402 C  C    . ALA   B 1 77  ? -58.569 -0.218  -18.058 1.00 15.66 ? 56  ALA   B C    1 
ATOM   2403 O  O    . ALA   B 1 77  ? -59.125 -0.030  -19.154 1.00 16.50 ? 56  ALA   B O    1 
ATOM   2404 C  CB   . ALA   B 1 77  ? -56.571 1.267   -17.809 1.00 15.63 ? 56  ALA   B CB   1 
ATOM   2405 N  N    . VAL   B 1 78  ? -59.235 -0.449  -16.933 1.00 15.85 ? 57  VAL   B N    1 
ATOM   2406 C  CA   . VAL   B 1 78  ? -60.687 -0.368  -16.838 1.00 16.05 ? 57  VAL   B CA   1 
ATOM   2407 C  C    . VAL   B 1 78  ? -61.027 0.481   -15.616 1.00 17.14 ? 57  VAL   B C    1 
ATOM   2408 O  O    . VAL   B 1 78  ? -60.205 0.636   -14.710 1.00 17.04 ? 57  VAL   B O    1 
ATOM   2409 C  CB   . VAL   B 1 78  ? -61.416 -1.726  -16.782 1.00 17.77 ? 57  VAL   B CB   1 
ATOM   2410 C  CG1  . VAL   B 1 78  ? -61.274 -2.536  -18.076 1.00 17.73 ? 57  VAL   B CG1  1 
ATOM   2411 C  CG2  . VAL   B 1 78  ? -61.024 -2.548  -15.554 1.00 18.10 ? 57  VAL   B CG2  1 
ATOM   2412 N  N    . VAL   B 1 79  ? -62.255 0.990   -15.564 1.00 17.41 ? 58  VAL   B N    1 
ATOM   2413 C  CA   . VAL   B 1 79  ? -62.706 1.727   -14.397 1.00 17.57 ? 58  VAL   B CA   1 
ATOM   2414 C  C    . VAL   B 1 79  ? -63.829 0.947   -13.726 1.00 18.21 ? 58  VAL   B C    1 
ATOM   2415 O  O    . VAL   B 1 79  ? -64.529 0.172   -14.382 1.00 18.40 ? 58  VAL   B O    1 
ATOM   2416 C  CB   . VAL   B 1 79  ? -63.160 3.162   -14.741 1.00 19.19 ? 58  VAL   B CB   1 
ATOM   2417 C  CG1  . VAL   B 1 79  ? -62.011 3.971   -15.339 1.00 18.30 ? 58  VAL   B CG1  1 
ATOM   2418 C  CG2  . VAL   B 1 79  ? -64.357 3.171   -15.693 1.00 21.54 ? 58  VAL   B CG2  1 
ATOM   2419 N  N    . CYS   B 1 80  ? -63.970 1.167   -12.411 1.00 16.32 ? 59  CYS   B N    1 
ATOM   2420 C  CA   . CYS   B 1 80  ? -65.042 0.564   -11.645 1.00 17.22 ? 59  CYS   B CA   1 
ATOM   2421 C  C    . CYS   B 1 80  ? -65.449 1.540   -10.546 1.00 17.85 ? 59  CYS   B C    1 
ATOM   2422 O  O    . CYS   B 1 80  ? -64.670 1.815   -9.636  1.00 17.84 ? 59  CYS   B O    1 
ATOM   2423 C  CB   . CYS   B 1 80  ? -64.625 -0.815  -11.137 1.00 17.57 ? 59  CYS   B CB   1 
ATOM   2424 S  SG   . CYS   B 1 80  ? -65.944 -1.639  -10.210 1.00 22.57 ? 59  CYS   B SG   1 
ATOM   2425 N  N    . GLN   B 1 81  ? -66.701 2.004   -10.602 1.00 17.59 ? 60  GLN   B N    1 
ATOM   2426 C  CA   . GLN   B 1 81  ? -67.224 2.921   -9.612  1.00 18.37 ? 60  GLN   B CA   1 
ATOM   2427 C  C    . GLN   B 1 81  ? -67.863 2.117   -8.481  1.00 20.59 ? 60  GLN   B C    1 
ATOM   2428 O  O    . GLN   B 1 81  ? -68.563 1.131   -8.721  1.00 20.65 ? 60  GLN   B O    1 
ATOM   2429 C  CB   . GLN   B 1 81  ? -68.258 3.832   -10.277 1.00 20.10 ? 60  GLN   B CB   1 
ATOM   2430 C  CG   . GLN   B 1 81  ? -68.701 4.980   -9.381  1.00 21.80 ? 60  GLN   B CG   1 
ATOM   2431 C  CD   . GLN   B 1 81  ? -69.794 4.612   -8.403  1.00 25.98 ? 60  GLN   B CD   1 
ATOM   2432 O  OE1  . GLN   B 1 81  ? -70.435 3.552   -8.473  1.00 26.85 ? 60  GLN   B OE1  1 
ATOM   2433 N  NE2  . GLN   B 1 81  ? -70.013 5.516   -7.463  1.00 30.10 ? 60  GLN   B NE2  1 
ATOM   2434 N  N    . ALA   B 1 82  ? -67.556 2.533   -7.243  1.00 18.71 ? 61  ALA   B N    1 
ATOM   2435 C  CA   . ALA   B 1 82  ? -68.238 1.993   -6.078  1.00 18.02 ? 61  ALA   B CA   1 
ATOM   2436 C  C    . ALA   B 1 82  ? -68.105 2.964   -4.917  1.00 18.14 ? 61  ALA   B C    1 
ATOM   2437 O  O    . ALA   B 1 82  ? -67.045 3.530   -4.667  1.00 19.99 ? 61  ALA   B O    1 
ATOM   2438 C  CB   . ALA   B 1 82  ? -67.674 0.633   -5.717  1.00 18.18 ? 61  ALA   B CB   1 
ATOM   2439 N  N    . ASP   B 1 83  ? -69.210 3.140   -4.194  1.00 19.39 ? 62  ASP   B N    1 
ATOM   2440 C  CA   . ASP   B 1 83  ? -69.177 3.775   -2.890  1.00 18.58 ? 62  ASP   B CA   1 
ATOM   2441 C  C    . ASP   B 1 83  ? -68.660 2.756   -1.876  1.00 18.65 ? 62  ASP   B C    1 
ATOM   2442 O  O    . ASP   B 1 83  ? -69.181 1.636   -1.796  1.00 18.91 ? 62  ASP   B O    1 
ATOM   2443 C  CB   . ASP   B 1 83  ? -70.581 4.255   -2.544  1.00 20.62 ? 62  ASP   B CB   1 
ATOM   2444 C  CG   . ASP   B 1 83  ? -70.736 5.099   -1.289  1.00 22.78 ? 62  ASP   B CG   1 
ATOM   2445 O  OD1  . ASP   B 1 83  ? -69.723 5.346   -0.613  1.00 22.20 ? 62  ASP   B OD1  1 
ATOM   2446 O  OD2  . ASP   B 1 83  ? -71.884 5.523   -1.016  1.00 26.63 ? 62  ASP   B OD2  1 
ATOM   2447 N  N    . LEU   B 1 84  ? -67.633 3.156   -1.099  1.00 16.31 ? 63  LEU   B N    1 
ATOM   2448 C  CA   . LEU   B 1 84  ? -67.009 2.248   -0.142  1.00 16.94 ? 63  LEU   B CA   1 
ATOM   2449 C  C    . LEU   B 1 84  ? -67.478 2.549   1.281   1.00 18.44 ? 63  LEU   B C    1 
ATOM   2450 O  O    . LEU   B 1 84  ? -66.921 2.003   2.240   1.00 18.80 ? 63  LEU   B O    1 
ATOM   2451 C  CB   . LEU   B 1 84  ? -65.483 2.213   -0.286  1.00 16.73 ? 63  LEU   B CB   1 
ATOM   2452 C  CG   . LEU   B 1 84  ? -64.958 1.691   -1.627  1.00 18.14 ? 63  LEU   B CG   1 
ATOM   2453 C  CD1  . LEU   B 1 84  ? -63.433 1.696   -1.673  1.00 20.26 ? 63  LEU   B CD1  1 
ATOM   2454 C  CD2  . LEU   B 1 84  ? -65.468 0.291   -1.974  1.00 18.80 ? 63  LEU   B CD2  1 
ATOM   2455 N  N    . THR   B 1 85  ? -68.544 3.356   1.405   1.00 16.38 ? 64  THR   B N    1 
ATOM   2456 C  CA   . THR   B 1 85  ? -69.211 3.602   2.678   1.00 17.84 ? 64  THR   B CA   1 
ATOM   2457 C  C    . THR   B 1 85  ? -69.742 2.272   3.216   1.00 19.38 ? 64  THR   B C    1 
ATOM   2458 O  O    . THR   B 1 85  ? -70.244 1.435   2.459   1.00 20.03 ? 64  THR   B O    1 
ATOM   2459 C  CB   . THR   B 1 85  ? -70.364 4.589   2.492   1.00 18.11 ? 64  THR   B CB   1 
ATOM   2460 O  OG1  . THR   B 1 85  ? -69.879 5.819   1.958   1.00 21.28 ? 64  THR   B OG1  1 
ATOM   2461 C  CG2  . THR   B 1 85  ? -71.045 4.931   3.813   1.00 20.32 ? 64  THR   B CG2  1 
ATOM   2462 N  N    . ASN   B 1 86  ? -69.650 2.086   4.545   1.00 17.42 ? 65  ASN   B N    1 
ATOM   2463 C  CA   . ASN   B 1 86  ? -70.181 0.878   5.143   1.00 19.24 ? 65  ASN   B CA   1 
ATOM   2464 C  C    . ASN   B 1 86  ? -71.697 0.856   4.984   1.00 19.97 ? 65  ASN   B C    1 
ATOM   2465 O  O    . ASN   B 1 86  ? -72.384 1.850   5.219   1.00 20.89 ? 65  ASN   B O    1 
ATOM   2466 C  CB   . ASN   B 1 86  ? -69.793 0.775   6.616   1.00 18.36 ? 65  ASN   B CB   1 
ATOM   2467 C  CG   . ASN   B 1 86  ? -70.210 -0.538  7.235   1.00 21.68 ? 65  ASN   B CG   1 
ATOM   2468 O  OD1  . ASN   B 1 86  ? -70.804 -0.552  8.328   1.00 25.54 ? 65  ASN   B OD1  1 
ATOM   2469 N  ND2  . ASN   B 1 86  ? -69.893 -1.636  6.573   1.00 19.04 ? 65  ASN   B ND2  1 
ATOM   2470 N  N    . SER   B 1 87  ? -72.190 -0.331  4.626   1.00 21.34 ? 66  SER   B N    1 
ATOM   2471 C  CA   . SER   B 1 87  ? -73.602 -0.606  4.473   1.00 21.13 ? 66  SER   B CA   1 
ATOM   2472 C  C    . SER   B 1 87  ? -73.747 -2.105  4.226   1.00 21.85 ? 66  SER   B C    1 
ATOM   2473 O  O    . SER   B 1 87  ? -72.761 -2.827  4.094   1.00 24.71 ? 66  SER   B O    1 
ATOM   2474 C  CB   . SER   B 1 87  ? -74.204 0.186   3.346   1.00 23.72 ? 66  SER   B CB   1 
ATOM   2475 O  OG   . SER   B 1 87  ? -73.887 -0.436  2.107   1.00 24.93 ? 66  SER   B OG   1 
ATOM   2476 N  N    . ASN   B 1 88  ? -75.001 -2.557  4.156   1.00 25.03 ? 67  ASN   B N    1 
ATOM   2477 C  CA   A ASN   B 1 88  ? -75.248 -3.980  3.990   0.70 26.93 ? 67  ASN   B CA   1 
ATOM   2478 C  CA   B ASN   B 1 88  ? -75.336 -3.959  3.960   0.30 25.91 ? 67  ASN   B CA   1 
ATOM   2479 C  C    . ASN   B 1 88  ? -74.992 -4.406  2.539   1.00 26.59 ? 67  ASN   B C    1 
ATOM   2480 O  O    . ASN   B 1 88  ? -74.911 -5.605  2.267   1.00 29.93 ? 67  ASN   B O    1 
ATOM   2481 C  CB   A ASN   B 1 88  ? -76.607 -4.398  4.553   0.70 30.45 ? 67  ASN   B CB   1 
ATOM   2482 C  CB   B ASN   B 1 88  ? -76.783 -4.255  4.352   0.30 26.18 ? 67  ASN   B CB   1 
ATOM   2483 C  CG   A ASN   B 1 88  ? -76.637 -4.515  6.062   0.70 32.58 ? 67  ASN   B CG   1 
ATOM   2484 C  CG   B ASN   B 1 88  ? -77.721 -3.099  4.092   0.30 26.44 ? 67  ASN   B CG   1 
ATOM   2485 O  OD1  A ASN   B 1 88  ? -75.605 -4.411  6.735   0.70 32.34 ? 67  ASN   B OD1  1 
ATOM   2486 O  OD1  B ASN   B 1 88  ? -77.938 -2.706  2.939   0.30 25.86 ? 67  ASN   B OD1  1 
ATOM   2487 N  ND2  A ASN   B 1 88  ? -77.818 -4.750  6.619   0.70 37.61 ? 67  ASN   B ND2  1 
ATOM   2488 N  ND2  B ASN   B 1 88  ? -78.288 -2.544  5.153   0.30 27.09 ? 67  ASN   B ND2  1 
ATOM   2489 N  N    . VAL   B 1 89  ? -74.807 -3.437  1.628   1.00 25.96 ? 68  VAL   B N    1 
ATOM   2490 C  CA   . VAL   B 1 89  ? -74.487 -3.755  0.236   1.00 25.94 ? 68  VAL   B CA   1 
ATOM   2491 C  C    . VAL   B 1 89  ? -72.981 -3.651  -0.028  1.00 25.72 ? 68  VAL   B C    1 
ATOM   2492 O  O    . VAL   B 1 89  ? -72.512 -3.975  -1.119  1.00 24.50 ? 68  VAL   B O    1 
ATOM   2493 C  CB   . VAL   B 1 89  ? -75.247 -2.954  -0.839  1.00 28.81 ? 68  VAL   B CB   1 
ATOM   2494 C  CG1  . VAL   B 1 89  ? -76.761 -3.077  -0.693  1.00 32.50 ? 68  VAL   B CG1  1 
ATOM   2495 C  CG2  . VAL   B 1 89  ? -74.818 -1.492  -0.898  1.00 28.70 ? 68  VAL   B CG2  1 
ATOM   2496 N  N    . LEU   B 1 90  ? -72.215 -3.166  0.952   1.00 22.39 ? 69  LEU   B N    1 
ATOM   2497 C  CA   . LEU   B 1 90  ? -70.785 -3.000  0.722   1.00 20.15 ? 69  LEU   B CA   1 
ATOM   2498 C  C    . LEU   B 1 90  ? -70.095 -4.317  0.349   1.00 19.74 ? 69  LEU   B C    1 
ATOM   2499 O  O    . LEU   B 1 90  ? -69.237 -4.305  -0.531  1.00 19.23 ? 69  LEU   B O    1 
ATOM   2500 C  CB   . LEU   B 1 90  ? -70.132 -2.273  1.900   1.00 19.12 ? 69  LEU   B CB   1 
ATOM   2501 C  CG   . LEU   B 1 90  ? -68.622 -2.042  1.772   1.00 17.86 ? 69  LEU   B CG   1 
ATOM   2502 C  CD1  . LEU   B 1 90  ? -68.285 -1.128  0.601   1.00 19.12 ? 69  LEU   B CD1  1 
ATOM   2503 C  CD2  . LEU   B 1 90  ? -68.075 -1.465  3.067   1.00 18.29 ? 69  LEU   B CD2  1 
ATOM   2504 N  N    . PRO   B 1 91  ? -70.379 -5.496  0.968   1.00 19.45 ? 70  PRO   B N    1 
ATOM   2505 C  CA   . PRO   B 1 91  ? -69.732 -6.745  0.545   1.00 21.06 ? 70  PRO   B CA   1 
ATOM   2506 C  C    . PRO   B 1 91  ? -69.909 -7.032  -0.948  1.00 22.23 ? 70  PRO   B C    1 
ATOM   2507 O  O    . PRO   B 1 91  ? -68.968 -7.413  -1.646  1.00 20.74 ? 70  PRO   B O    1 
ATOM   2508 C  CB   . PRO   B 1 91  ? -70.393 -7.821  1.437   1.00 22.14 ? 70  PRO   B CB   1 
ATOM   2509 C  CG   . PRO   B 1 91  ? -70.779 -7.057  2.678   1.00 20.09 ? 70  PRO   B CG   1 
ATOM   2510 C  CD   . PRO   B 1 91  ? -71.212 -5.686  2.174   1.00 20.25 ? 70  PRO   B CD   1 
ATOM   2511 N  N    . ALA   B 1 92  ? -71.130 -6.820  -1.437  1.00 23.40 ? 71  ALA   B N    1 
ATOM   2512 C  CA   . ALA   B 1 92  ? -71.401 -7.026  -2.850  1.00 23.00 ? 71  ALA   B CA   1 
ATOM   2513 C  C    . ALA   B 1 92  ? -70.619 -6.034  -3.709  1.00 22.34 ? 71  ALA   B C    1 
ATOM   2514 O  O    . ALA   B 1 92  ? -70.114 -6.420  -4.760  1.00 23.91 ? 71  ALA   B O    1 
ATOM   2515 C  CB   . ALA   B 1 92  ? -72.889 -6.956  -3.134  1.00 24.27 ? 71  ALA   B CB   1 
ATOM   2516 N  N    . SER   B 1 93  ? -70.521 -4.765  -3.283  1.00 21.21 ? 72  SER   B N    1 
ATOM   2517 C  CA   . SER   B 1 93  ? -69.763 -3.774  -4.039  1.00 19.41 ? 72  SER   B CA   1 
ATOM   2518 C  C    . SER   B 1 93  ? -68.297 -4.186  -4.155  1.00 21.03 ? 72  SER   B C    1 
ATOM   2519 O  O    . SER   B 1 93  ? -67.669 -4.055  -5.206  1.00 21.04 ? 72  SER   B O    1 
ATOM   2520 C  CB   . SER   B 1 93  ? -69.867 -2.393  -3.427  1.00 22.71 ? 72  SER   B CB   1 
ATOM   2521 O  OG   . SER   B 1 93  ? -71.184 -1.862  -3.527  1.00 23.69 ? 72  SER   B OG   1 
ATOM   2522 N  N    . CYS   B 1 94  ? -67.744 -4.674  -3.039  1.00 19.19 ? 73  CYS   B N    1 
ATOM   2523 C  CA   . CYS   B 1 94  ? -66.340 -5.059  -3.027  1.00 18.82 ? 73  CYS   B CA   1 
ATOM   2524 C  C    . CYS   B 1 94  ? -66.106 -6.293  -3.893  1.00 18.56 ? 73  CYS   B C    1 
ATOM   2525 O  O    . CYS   B 1 94  ? -65.093 -6.364  -4.585  1.00 17.88 ? 73  CYS   B O    1 
ATOM   2526 C  CB   . CYS   B 1 94  ? -65.849 -5.240  -1.596  1.00 17.44 ? 73  CYS   B CB   1 
ATOM   2527 S  SG   . CYS   B 1 94  ? -65.821 -3.682  -0.666  1.00 18.81 ? 73  CYS   B SG   1 
ATOM   2528 N  N    . GLU   B 1 95  ? -67.004 -7.285  -3.825  1.00 20.58 ? 74  GLU   B N    1 
ATOM   2529 C  CA   . GLU   B 1 95  ? -66.904 -8.447  -4.693  1.00 20.34 ? 74  GLU   B CA   1 
ATOM   2530 C  C    . GLU   B 1 95  ? -66.889 -7.995  -6.156  1.00 19.95 ? 74  GLU   B C    1 
ATOM   2531 O  O    . GLU   B 1 95  ? -66.090 -8.498  -6.954  1.00 20.91 ? 74  GLU   B O    1 
ATOM   2532 C  CB   . GLU   B 1 95  ? -68.068 -9.396  -4.387  1.00 22.56 ? 74  GLU   B CB   1 
ATOM   2533 C  CG   . GLU   B 1 95  ? -68.080 -10.645 -5.270  1.00 26.02 ? 74  GLU   B CG   1 
ATOM   2534 C  CD   A GLU   B 1 95  ? -67.028 -11.727 -5.079  0.50 26.55 ? 74  GLU   B CD   1 
ATOM   2535 O  OE1  A GLU   B 1 95  ? -66.209 -11.668 -4.133  0.50 26.87 ? 74  GLU   B OE1  1 
ATOM   2536 O  OE2  A GLU   B 1 95  ? -67.025 -12.654 -5.913  0.50 29.04 ? 74  GLU   B OE2  1 
ATOM   2537 N  N    . GLU   B 1 96  ? -67.723 -6.999  -6.482  1.00 20.49 ? 75  GLU   B N    1 
ATOM   2538 C  CA   . GLU   B 1 96  ? -67.811 -6.545  -7.864  1.00 22.51 ? 75  GLU   B CA   1 
ATOM   2539 C  C    . GLU   B 1 96  ? -66.519 -5.868  -8.324  1.00 21.15 ? 75  GLU   B C    1 
ATOM   2540 O  O    . GLU   B 1 96  ? -66.141 -5.980  -9.484  1.00 19.43 ? 75  GLU   B O    1 
ATOM   2541 C  CB   . GLU   B 1 96  ? -69.063 -5.708  -8.134  1.00 26.23 ? 75  GLU   B CB   1 
ATOM   2542 C  CG   . GLU   B 1 96  ? -69.155 -5.218  -9.579  1.00 29.10 ? 75  GLU   B CG   1 
ATOM   2543 C  CD   . GLU   B 1 96  ? -69.115 -6.255  -10.697 1.00 32.66 ? 75  GLU   B CD   1 
ATOM   2544 O  OE1  . GLU   B 1 96  ? -69.303 -7.475  -10.468 1.00 33.77 ? 75  GLU   B OE1  1 
ATOM   2545 O  OE2  . GLU   B 1 96  ? -68.848 -5.811  -11.832 1.00 32.85 ? 75  GLU   B OE2  1 
ATOM   2546 N  N    . ILE   B 1 97  ? -65.841 -5.149  -7.423  1.00 18.42 ? 76  ILE   B N    1 
ATOM   2547 C  CA   . ILE   B 1 97  ? -64.585 -4.530  -7.825  1.00 17.61 ? 76  ILE   B CA   1 
ATOM   2548 C  C    . ILE   B 1 97  ? -63.578 -5.609  -8.211  1.00 18.37 ? 76  ILE   B C    1 
ATOM   2549 O  O    . ILE   B 1 97  ? -62.871 -5.494  -9.219  1.00 18.07 ? 76  ILE   B O    1 
ATOM   2550 C  CB   . ILE   B 1 97  ? -64.046 -3.638  -6.692  1.00 16.95 ? 76  ILE   B CB   1 
ATOM   2551 C  CG1  . ILE   B 1 97  ? -64.941 -2.416  -6.452  1.00 17.53 ? 76  ILE   B CG1  1 
ATOM   2552 C  CG2  . ILE   B 1 97  ? -62.598 -3.237  -6.973  1.00 18.53 ? 76  ILE   B CG2  1 
ATOM   2553 C  CD1  . ILE   B 1 97  ? -64.649 -1.665  -5.156  1.00 19.10 ? 76  ILE   B CD1  1 
ATOM   2554 N  N    . ILE   B 1 98  ? -63.433 -6.628  -7.351  1.00 17.44 ? 77  ILE   B N    1 
ATOM   2555 C  CA   . ILE   B 1 98  ? -62.515 -7.717  -7.651  1.00 17.06 ? 77  ILE   B CA   1 
ATOM   2556 C  C    . ILE   B 1 98  ? -62.965 -8.447  -8.920  1.00 19.18 ? 77  ILE   B C    1 
ATOM   2557 O  O    . ILE   B 1 98  ? -62.140 -8.759  -9.783  1.00 17.80 ? 77  ILE   B O    1 
ATOM   2558 C  CB   . ILE   B 1 98  ? -62.326 -8.672  -6.453  1.00 17.88 ? 77  ILE   B CB   1 
ATOM   2559 C  CG1  . ILE   B 1 98  ? -61.806 -7.916  -5.216  1.00 18.45 ? 77  ILE   B CG1  1 
ATOM   2560 C  CG2  . ILE   B 1 98  ? -61.411 -9.841  -6.835  1.00 17.20 ? 77  ILE   B CG2  1 
ATOM   2561 C  CD1  . ILE   B 1 98  ? -60.501 -7.166  -5.455  1.00 20.16 ? 77  ILE   B CD1  1 
ATOM   2562 N  N    . ASN   B 1 99  ? -64.272 -8.678  -9.027  1.00 19.68 ? 78  ASN   B N    1 
ATOM   2563 C  CA   . ASN   B 1 99  ? -64.831 -9.334  -10.204 1.00 20.93 ? 78  ASN   B CA   1 
ATOM   2564 C  C    . ASN   B 1 99  ? -64.444 -8.574  -11.471 1.00 19.77 ? 78  ASN   B C    1 
ATOM   2565 O  O    . ASN   B 1 99  ? -64.182 -9.194  -12.496 1.00 20.49 ? 78  ASN   B O    1 
ATOM   2566 C  CB   . ASN   B 1 99  ? -66.344 -9.451  -10.082 1.00 21.58 ? 78  ASN   B CB   1 
ATOM   2567 C  CG   . ASN   B 1 99  ? -66.906 -10.295 -11.199 1.00 26.11 ? 78  ASN   B CG   1 
ATOM   2568 O  OD1  . ASN   B 1 99  ? -66.510 -11.461 -11.347 1.00 26.74 ? 78  ASN   B OD1  1 
ATOM   2569 N  ND2  . ASN   B 1 99  ? -67.799 -9.709  -11.985 1.00 28.55 ? 78  ASN   B ND2  1 
ATOM   2570 N  N    . SER   B 1 100 ? -64.432 -7.241  -11.409 1.00 18.86 ? 79  SER   B N    1 
ATOM   2571 C  CA   . SER   B 1 100 ? -64.146 -6.439  -12.590 1.00 18.23 ? 79  SER   B CA   1 
ATOM   2572 C  C    . SER   B 1 100 ? -62.715 -6.658  -13.082 1.00 17.86 ? 79  SER   B C    1 
ATOM   2573 O  O    . SER   B 1 100 ? -62.439 -6.591  -14.281 1.00 19.68 ? 79  SER   B O    1 
ATOM   2574 C  CB   . SER   B 1 100 ? -64.420 -4.992  -12.337 1.00 19.83 ? 79  SER   B CB   1 
ATOM   2575 O  OG   . SER   B 1 100 ? -65.813 -4.818  -12.127 1.00 24.89 ? 79  SER   B OG   1 
ATOM   2576 N  N    . CYS   B 1 101 ? -61.795 -6.953  -12.158 1.00 16.26 ? 80  CYS   B N    1 
ATOM   2577 C  CA   . CYS   B 1 101 ? -60.431 -7.244  -12.541 1.00 16.42 ? 80  CYS   B CA   1 
ATOM   2578 C  C    . CYS   B 1 101 ? -60.367 -8.582  -13.279 1.00 16.70 ? 80  CYS   B C    1 
ATOM   2579 O  O    . CYS   B 1 101 ? -59.644 -8.703  -14.274 1.00 17.29 ? 80  CYS   B O    1 
ATOM   2580 C  CB   . CYS   B 1 101 ? -59.527 -7.261  -11.304 1.00 17.31 ? 80  CYS   B CB   1 
ATOM   2581 S  SG   . CYS   B 1 101 ? -57.774 -7.110  -11.712 1.00 17.87 ? 80  CYS   B SG   1 
ATOM   2582 N  N    . PHE   B 1 102 ? -61.108 -9.581  -12.778 1.00 17.91 ? 81  PHE   B N    1 
ATOM   2583 C  CA   . PHE   B 1 102 ? -61.105 -10.886 -13.419 1.00 18.70 ? 81  PHE   B CA   1 
ATOM   2584 C  C    . PHE   B 1 102 ? -61.773 -10.808 -14.792 1.00 20.07 ? 81  PHE   B C    1 
ATOM   2585 O  O    . PHE   B 1 102 ? -61.271 -11.400 -15.746 1.00 19.77 ? 81  PHE   B O    1 
ATOM   2586 C  CB   . PHE   B 1 102 ? -61.729 -11.957 -12.518 1.00 19.80 ? 81  PHE   B CB   1 
ATOM   2587 C  CG   . PHE   B 1 102 ? -60.756 -12.461 -11.460 1.00 21.61 ? 81  PHE   B CG   1 
ATOM   2588 C  CD1  . PHE   B 1 102 ? -59.915 -13.548 -11.720 1.00 22.97 ? 81  PHE   B CD1  1 
ATOM   2589 C  CD2  . PHE   B 1 102 ? -60.697 -11.858 -10.205 1.00 22.43 ? 81  PHE   B CD2  1 
ATOM   2590 C  CE1  . PHE   B 1 102 ? -59.026 -14.006 -10.756 1.00 23.54 ? 81  PHE   B CE1  1 
ATOM   2591 C  CE2  . PHE   B 1 102 ? -59.786 -12.296 -9.254  1.00 23.95 ? 81  PHE   B CE2  1 
ATOM   2592 C  CZ   . PHE   B 1 102 ? -58.966 -13.378 -9.524  1.00 23.37 ? 81  PHE   B CZ   1 
ATOM   2593 N  N    . ARG   B 1 103 ? -62.889 -10.077 -14.879 1.00 18.05 ? 82  ARG   B N    1 
ATOM   2594 C  CA   A ARG   B 1 103 ? -63.609 -9.908  -16.138 0.70 19.13 ? 82  ARG   B CA   1 
ATOM   2595 C  CA   B ARG   B 1 103 ? -63.603 -9.916  -16.139 0.30 18.35 ? 82  ARG   B CA   1 
ATOM   2596 C  C    . ARG   B 1 103 ? -62.664 -9.316  -17.185 1.00 20.52 ? 82  ARG   B C    1 
ATOM   2597 O  O    . ARG   B 1 103 ? -62.595 -9.792  -18.321 1.00 22.82 ? 82  ARG   B O    1 
ATOM   2598 C  CB   A ARG   B 1 103 ? -64.842 -9.017  -15.929 0.70 19.14 ? 82  ARG   B CB   1 
ATOM   2599 C  CB   B ARG   B 1 103 ? -64.838 -9.022  -15.964 0.30 16.59 ? 82  ARG   B CB   1 
ATOM   2600 C  CG   A ARG   B 1 103 ? -65.660 -8.793  -17.199 0.70 22.63 ? 82  ARG   B CG   1 
ATOM   2601 C  CG   B ARG   B 1 103 ? -65.613 -8.830  -17.262 0.30 15.75 ? 82  ARG   B CG   1 
ATOM   2602 C  CD   A ARG   B 1 103 ? -67.025 -8.186  -16.925 0.70 25.64 ? 82  ARG   B CD   1 
ATOM   2603 C  CD   B ARG   B 1 103 ? -66.609 -7.693  -17.150 0.30 14.67 ? 82  ARG   B CD   1 
ATOM   2604 N  NE   A ARG   B 1 103 ? -66.978 -6.836  -16.352 0.70 31.65 ? 82  ARG   B NE   1 
ATOM   2605 N  NE   B ARG   B 1 103 ? -67.631 -7.954  -16.129 0.30 15.49 ? 82  ARG   B NE   1 
ATOM   2606 C  CZ   A ARG   B 1 103 ? -67.287 -6.545  -15.088 0.70 34.96 ? 82  ARG   B CZ   1 
ATOM   2607 C  CZ   B ARG   B 1 103 ? -67.753 -7.253  -15.002 0.30 16.58 ? 82  ARG   B CZ   1 
ATOM   2608 N  NH1  A ARG   B 1 103 ? -67.731 -7.490  -14.271 0.70 36.69 ? 82  ARG   B NH1  1 
ATOM   2609 N  NH1  B ARG   B 1 103 ? -66.956 -6.220  -14.767 0.30 15.40 ? 82  ARG   B NH1  1 
ATOM   2610 N  NH2  A ARG   B 1 103 ? -67.145 -5.310  -14.642 0.70 35.25 ? 82  ARG   B NH2  1 
ATOM   2611 N  NH2  B ARG   B 1 103 ? -68.682 -7.576  -14.118 0.30 16.74 ? 82  ARG   B NH2  1 
ATOM   2612 N  N    . ALA   B 1 104 ? -61.948 -8.250  -16.808 1.00 18.75 ? 83  ALA   B N    1 
ATOM   2613 C  CA   . ALA   B 1 104 ? -61.136 -7.533  -17.777 1.00 18.18 ? 83  ALA   B CA   1 
ATOM   2614 C  C    . ALA   B 1 104 ? -59.854 -8.280  -18.104 1.00 19.14 ? 83  ALA   B C    1 
ATOM   2615 O  O    . ALA   B 1 104 ? -59.421 -8.281  -19.258 1.00 20.11 ? 83  ALA   B O    1 
ATOM   2616 C  CB   . ALA   B 1 104 ? -60.825 -6.130  -17.292 1.00 19.60 ? 83  ALA   B CB   1 
ATOM   2617 N  N    . PHE   B 1 105 ? -59.225 -8.906  -17.095 1.00 17.81 ? 84  PHE   B N    1 
ATOM   2618 C  CA   . PHE   B 1 105 ? -57.826 -9.268  -17.283 1.00 16.96 ? 84  PHE   B CA   1 
ATOM   2619 C  C    . PHE   B 1 105 ? -57.571 -10.736 -16.976 1.00 17.98 ? 84  PHE   B C    1 
ATOM   2620 O  O    . PHE   B 1 105 ? -56.448 -11.192 -17.163 1.00 20.10 ? 84  PHE   B O    1 
ATOM   2621 C  CB   . PHE   B 1 105 ? -56.941 -8.400  -16.383 1.00 18.30 ? 84  PHE   B CB   1 
ATOM   2622 C  CG   . PHE   B 1 105 ? -57.094 -6.910  -16.623 1.00 17.24 ? 84  PHE   B CG   1 
ATOM   2623 C  CD1  . PHE   B 1 105 ? -57.051 -6.382  -17.917 1.00 17.68 ? 84  PHE   B CD1  1 
ATOM   2624 C  CD2  . PHE   B 1 105 ? -57.388 -6.050  -15.570 1.00 17.61 ? 84  PHE   B CD2  1 
ATOM   2625 C  CE1  . PHE   B 1 105 ? -57.216 -5.022  -18.124 1.00 16.34 ? 84  PHE   B CE1  1 
ATOM   2626 C  CE2  . PHE   B 1 105 ? -57.551 -4.692  -15.783 1.00 17.07 ? 84  PHE   B CE2  1 
ATOM   2627 C  CZ   . PHE   B 1 105 ? -57.475 -4.173  -17.067 1.00 17.00 ? 84  PHE   B CZ   1 
ATOM   2628 N  N    . GLY   B 1 106 ? -58.580 -11.420 -16.428 1.00 17.83 ? 85  GLY   B N    1 
ATOM   2629 C  CA   . GLY   B 1 106 ? -58.499 -12.864 -16.225 1.00 19.22 ? 85  GLY   B CA   1 
ATOM   2630 C  C    . GLY   B 1 106 ? -57.735 -13.278 -14.964 1.00 19.41 ? 85  GLY   B C    1 
ATOM   2631 O  O    . GLY   B 1 106 ? -57.534 -14.479 -14.724 1.00 20.28 ? 85  GLY   B O    1 
ATOM   2632 N  N    . ARG   B 1 107 ? -57.334 -12.298 -14.146 1.00 18.83 ? 86  ARG   B N    1 
ATOM   2633 C  CA   . ARG   B 1 107 ? -56.518 -12.564 -12.966 1.00 16.84 ? 86  ARG   B CA   1 
ATOM   2634 C  C    . ARG   B 1 107 ? -56.486 -11.287 -12.125 1.00 19.77 ? 86  ARG   B C    1 
ATOM   2635 O  O    . ARG   B 1 107 ? -56.793 -10.212 -12.630 1.00 19.31 ? 86  ARG   B O    1 
ATOM   2636 C  CB   . ARG   B 1 107 ? -55.120 -12.979 -13.433 1.00 17.81 ? 86  ARG   B CB   1 
ATOM   2637 C  CG   . ARG   B 1 107 ? -54.370 -11.901 -14.206 1.00 19.16 ? 86  ARG   B CG   1 
ATOM   2638 C  CD   . ARG   B 1 107 ? -53.112 -12.427 -14.870 1.00 18.80 ? 86  ARG   B CD   1 
ATOM   2639 N  NE   . ARG   B 1 107 ? -52.029 -12.607 -13.900 1.00 19.22 ? 86  ARG   B NE   1 
ATOM   2640 C  CZ   . ARG   B 1 107 ? -50.829 -13.118 -14.169 1.00 22.49 ? 86  ARG   B CZ   1 
ATOM   2641 N  NH1  . ARG   B 1 107 ? -50.574 -13.671 -15.344 1.00 24.99 ? 86  ARG   B NH1  1 
ATOM   2642 N  NH2  . ARG   B 1 107 ? -49.887 -13.116 -13.239 1.00 22.44 ? 86  ARG   B NH2  1 
ATOM   2643 N  N    . CYS   B 1 108 ? -56.100 -11.414 -10.851 1.00 18.51 ? 87  CYS   B N    1 
ATOM   2644 C  CA   . CYS   B 1 108 ? -55.924 -10.260 -9.981  1.00 17.52 ? 87  CYS   B CA   1 
ATOM   2645 C  C    . CYS   B 1 108 ? -54.758 -10.578 -9.055  1.00 17.75 ? 87  CYS   B C    1 
ATOM   2646 O  O    . CYS   B 1 108 ? -54.899 -11.387 -8.125  1.00 18.43 ? 87  CYS   B O    1 
ATOM   2647 C  CB   . CYS   B 1 108 ? -57.190 -9.983  -9.178  1.00 17.49 ? 87  CYS   B CB   1 
ATOM   2648 S  SG   . CYS   B 1 108 ? -57.072 -8.447  -8.218  1.00 20.62 ? 87  CYS   B SG   1 
ATOM   2649 N  N    . ASP   B 1 109 ? -53.611 -9.948  -9.330  1.00 16.56 ? 88  ASP   B N    1 
ATOM   2650 C  CA   . ASP   B 1 109 ? -52.381 -10.277 -8.631  1.00 16.88 ? 88  ASP   B CA   1 
ATOM   2651 C  C    . ASP   B 1 109 ? -52.132 -9.353  -7.453  1.00 16.85 ? 88  ASP   B C    1 
ATOM   2652 O  O    . ASP   B 1 109 ? -51.465 -9.738  -6.490  1.00 15.70 ? 88  ASP   B O    1 
ATOM   2653 C  CB   . ASP   B 1 109 ? -51.204 -10.181 -9.577  1.00 17.49 ? 88  ASP   B CB   1 
ATOM   2654 C  CG   . ASP   B 1 109 ? -51.351 -11.125 -10.759 1.00 18.62 ? 88  ASP   B CG   1 
ATOM   2655 O  OD1  . ASP   B 1 109 ? -51.997 -10.739 -11.757 1.00 18.54 ? 88  ASP   B OD1  1 
ATOM   2656 O  OD2  . ASP   B 1 109 ? -50.860 -12.277 -10.635 1.00 20.69 ? 88  ASP   B OD2  1 
ATOM   2657 N  N    . VAL   B 1 110 ? -52.580 -8.103  -7.582  1.00 15.68 ? 89  VAL   B N    1 
ATOM   2658 C  CA   . VAL   B 1 110 ? -52.303 -7.091  -6.570  1.00 15.25 ? 89  VAL   B CA   1 
ATOM   2659 C  C    . VAL   B 1 110 ? -53.568 -6.305  -6.246  1.00 16.15 ? 89  VAL   B C    1 
ATOM   2660 O  O    . VAL   B 1 110 ? -54.314 -5.911  -7.149  1.00 14.68 ? 89  VAL   B O    1 
ATOM   2661 C  CB   . VAL   B 1 110 ? -51.234 -6.131  -7.125  1.00 15.66 ? 89  VAL   B CB   1 
ATOM   2662 C  CG1  . VAL   B 1 110 ? -51.137 -4.820  -6.335  1.00 16.62 ? 89  VAL   B CG1  1 
ATOM   2663 C  CG2  . VAL   B 1 110 ? -49.869 -6.799  -7.278  1.00 15.91 ? 89  VAL   B CG2  1 
ATOM   2664 N  N    . LEU   B 1 111 ? -53.790 -6.054  -4.952  1.00 14.48 ? 90  LEU   B N    1 
ATOM   2665 C  CA   . LEU   B 1 111 ? -54.838 -5.158  -4.486  1.00 13.98 ? 90  LEU   B CA   1 
ATOM   2666 C  C    . LEU   B 1 111 ? -54.177 -4.041  -3.692  1.00 14.32 ? 90  LEU   B C    1 
ATOM   2667 O  O    . LEU   B 1 111 ? -53.422 -4.326  -2.767  1.00 14.10 ? 90  LEU   B O    1 
ATOM   2668 C  CB   . LEU   B 1 111 ? -55.809 -5.926  -3.580  1.00 13.88 ? 90  LEU   B CB   1 
ATOM   2669 C  CG   . LEU   B 1 111 ? -56.787 -5.090  -2.749  1.00 15.55 ? 90  LEU   B CG   1 
ATOM   2670 C  CD1  . LEU   B 1 111 ? -57.724 -4.308  -3.663  1.00 16.96 ? 90  LEU   B CD1  1 
ATOM   2671 C  CD2  . LEU   B 1 111 ? -57.568 -6.044  -1.841  1.00 15.60 ? 90  LEU   B CD2  1 
ATOM   2672 N  N    . VAL   B 1 112 ? -54.462 -2.779  -4.047  1.00 12.84 ? 91  VAL   B N    1 
ATOM   2673 C  CA   . VAL   B 1 112 ? -53.959 -1.638  -3.307  1.00 13.75 ? 91  VAL   B CA   1 
ATOM   2674 C  C    . VAL   B 1 112 ? -55.160 -0.932  -2.698  1.00 13.58 ? 91  VAL   B C    1 
ATOM   2675 O  O    . VAL   B 1 112 ? -55.999 -0.370  -3.405  1.00 14.73 ? 91  VAL   B O    1 
ATOM   2676 C  CB   . VAL   B 1 112 ? -53.141 -0.651  -4.161  1.00 13.12 ? 91  VAL   B CB   1 
ATOM   2677 C  CG1  . VAL   B 1 112 ? -52.647 0.523   -3.322  1.00 15.15 ? 91  VAL   B CG1  1 
ATOM   2678 C  CG2  . VAL   B 1 112 ? -51.963 -1.328  -4.858  1.00 14.15 ? 91  VAL   B CG2  1 
ATOM   2679 N  N    . ASN   B 1 113 ? -55.241 -0.989  -1.363  1.00 13.13 ? 92  ASN   B N    1 
ATOM   2680 C  CA   . ASN   B 1 113 ? -56.322 -0.344  -0.640  1.00 13.59 ? 92  ASN   B CA   1 
ATOM   2681 C  C    . ASN   B 1 113 ? -55.875 1.083   -0.326  1.00 14.99 ? 92  ASN   B C    1 
ATOM   2682 O  O    . ASN   B 1 113 ? -55.249 1.345   0.706   1.00 13.95 ? 92  ASN   B O    1 
ATOM   2683 C  CB   . ASN   B 1 113 ? -56.677 -1.095  0.640   1.00 14.66 ? 92  ASN   B CB   1 
ATOM   2684 C  CG   . ASN   B 1 113 ? -57.457 -2.359  0.378   1.00 15.79 ? 92  ASN   B CG   1 
ATOM   2685 O  OD1  . ASN   B 1 113 ? -58.520 -2.321  -0.272  1.00 15.82 ? 92  ASN   B OD1  1 
ATOM   2686 N  ND2  . ASN   B 1 113 ? -56.965 -3.482  0.886   1.00 16.05 ? 92  ASN   B ND2  1 
ATOM   2687 N  N    . ASN   B 1 114 ? -56.235 2.011   -1.215  1.00 14.14 ? 93  ASN   B N    1 
ATOM   2688 C  CA   . ASN   B 1 114 ? -55.816 3.408   -1.152  1.00 14.24 ? 93  ASN   B CA   1 
ATOM   2689 C  C    . ASN   B 1 114 ? -56.972 4.344   -0.814  1.00 15.98 ? 93  ASN   B C    1 
ATOM   2690 O  O    . ASN   B 1 114 ? -56.735 5.382   -0.195  1.00 16.25 ? 93  ASN   B O    1 
ATOM   2691 C  CB   . ASN   B 1 114 ? -55.109 3.772   -2.458  1.00 14.40 ? 93  ASN   B CB   1 
ATOM   2692 C  CG   . ASN   B 1 114 ? -54.912 5.264   -2.602  1.00 15.36 ? 93  ASN   B CG   1 
ATOM   2693 O  OD1  . ASN   B 1 114 ? -53.926 5.805   -2.089  1.00 16.42 ? 93  ASN   B OD1  1 
ATOM   2694 N  ND2  . ASN   B 1 114 ? -55.833 5.943   -3.285  1.00 14.40 ? 93  ASN   B ND2  1 
ATOM   2695 N  N    . ALA   B 1 115 ? -58.201 4.033   -1.269  1.00 15.52 ? 94  ALA   B N    1 
ATOM   2696 C  CA   . ALA   B 1 115 ? -59.350 4.917   -1.051  1.00 16.58 ? 94  ALA   B CA   1 
ATOM   2697 C  C    . ALA   B 1 115 ? -59.512 5.254   0.429   1.00 17.53 ? 94  ALA   B C    1 
ATOM   2698 O  O    . ALA   B 1 115 ? -59.381 4.386   1.293   1.00 18.91 ? 94  ALA   B O    1 
ATOM   2699 C  CB   . ALA   B 1 115 ? -60.636 4.291   -1.574  1.00 17.08 ? 94  ALA   B CB   1 
ATOM   2700 N  N    . SER   B 1 116 ? -59.863 6.509   0.715   1.00 17.95 ? 95  SER   B N    1 
ATOM   2701 C  CA   . SER   B 1 116 ? -59.928 6.908   2.110   1.00 18.53 ? 95  SER   B CA   1 
ATOM   2702 C  C    . SER   B 1 116 ? -60.758 8.171   2.295   1.00 19.40 ? 95  SER   B C    1 
ATOM   2703 O  O    . SER   B 1 116 ? -60.479 9.180   1.650   1.00 22.56 ? 95  SER   B O    1 
ATOM   2704 C  CB   . SER   B 1 116 ? -58.525 7.174   2.585   1.00 18.58 ? 95  SER   B CB   1 
ATOM   2705 O  OG   . SER   B 1 116 ? -58.545 7.704   3.900   1.00 19.81 ? 95  SER   B OG   1 
ATOM   2706 N  N    . ALA   B 1 117 ? -61.712 8.134   3.235   1.00 19.64 ? 96  ALA   B N    1 
ATOM   2707 C  CA   . ALA   B 1 117 ? -62.338 9.373   3.678   1.00 18.00 ? 96  ALA   B CA   1 
ATOM   2708 C  C    . ALA   B 1 117 ? -61.501 9.960   4.814   1.00 18.38 ? 96  ALA   B C    1 
ATOM   2709 O  O    . ALA   B 1 117 ? -60.937 9.222   5.620   1.00 17.42 ? 96  ALA   B O    1 
ATOM   2710 C  CB   . ALA   B 1 117 ? -63.763 9.112   4.143   1.00 19.59 ? 96  ALA   B CB   1 
ATOM   2711 N  N    . PHE   B 1 118 ? -61.426 11.298  4.873   1.00 17.84 ? 97  PHE   B N    1 
ATOM   2712 C  CA   . PHE   B 1 118 ? -60.593 11.977  5.839   1.00 18.83 ? 97  PHE   B CA   1 
ATOM   2713 C  C    . PHE   B 1 118 ? -61.225 13.326  6.151   1.00 20.82 ? 97  PHE   B C    1 
ATOM   2714 O  O    . PHE   B 1 118 ? -61.236 14.194  5.282   1.00 21.70 ? 97  PHE   B O    1 
ATOM   2715 C  CB   . PHE   B 1 118 ? -59.196 12.194  5.230   1.00 21.03 ? 97  PHE   B CB   1 
ATOM   2716 C  CG   . PHE   B 1 118 ? -58.228 13.003  6.088   1.00 22.25 ? 97  PHE   B CG   1 
ATOM   2717 C  CD1  . PHE   B 1 118 ? -57.751 12.503  7.300   1.00 22.38 ? 97  PHE   B CD1  1 
ATOM   2718 C  CD2  . PHE   B 1 118 ? -57.774 14.254  5.672   1.00 24.29 ? 97  PHE   B CD2  1 
ATOM   2719 C  CE1  . PHE   B 1 118 ? -56.859 13.222  8.086   1.00 23.44 ? 97  PHE   B CE1  1 
ATOM   2720 C  CE2  . PHE   B 1 118 ? -56.883 14.978  6.463   1.00 24.66 ? 97  PHE   B CE2  1 
ATOM   2721 C  CZ   . PHE   B 1 118 ? -56.423 14.464  7.662   1.00 25.57 ? 97  PHE   B CZ   1 
ATOM   2722 N  N    . TYR   B 1 119 ? -61.783 13.450  7.363   1.00 17.98 ? 98  TYR   B N    1 
ATOM   2723 C  CA   . TYR   B 1 119 ? -62.363 14.703  7.820   1.00 18.05 ? 98  TYR   B CA   1 
ATOM   2724 C  C    . TYR   B 1 119 ? -62.565 14.600  9.329   1.00 18.71 ? 98  TYR   B C    1 
ATOM   2725 O  O    . TYR   B 1 119 ? -62.669 13.504  9.884   1.00 16.98 ? 98  TYR   B O    1 
ATOM   2726 C  CB   . TYR   B 1 119 ? -63.655 15.049  7.065   1.00 19.41 ? 98  TYR   B CB   1 
ATOM   2727 C  CG   . TYR   B 1 119 ? -64.749 13.991  7.084   1.00 18.08 ? 98  TYR   B CG   1 
ATOM   2728 C  CD1  . TYR   B 1 119 ? -65.595 13.860  8.179   1.00 19.18 ? 98  TYR   B CD1  1 
ATOM   2729 C  CD2  . TYR   B 1 119 ? -64.976 13.165  5.978   1.00 19.82 ? 98  TYR   B CD2  1 
ATOM   2730 C  CE1  . TYR   B 1 119 ? -66.605 12.906  8.187   1.00 20.18 ? 98  TYR   B CE1  1 
ATOM   2731 C  CE2  . TYR   B 1 119 ? -65.991 12.215  5.975   1.00 18.80 ? 98  TYR   B CE2  1 
ATOM   2732 C  CZ   . TYR   B 1 119 ? -66.810 12.088  7.085   1.00 19.67 ? 98  TYR   B CZ   1 
ATOM   2733 O  OH   . TYR   B 1 119 ? -67.847 11.185  7.103   1.00 20.01 ? 98  TYR   B OH   1 
ATOM   2734 N  N    . PRO   B 1 120 ? -62.657 15.734  10.049  1.00 19.36 ? 99  PRO   B N    1 
ATOM   2735 C  CA   . PRO   B 1 120 ? -62.811 15.702  11.503  1.00 19.39 ? 99  PRO   B CA   1 
ATOM   2736 C  C    . PRO   B 1 120 ? -64.187 15.182  11.921  1.00 18.53 ? 99  PRO   B C    1 
ATOM   2737 O  O    . PRO   B 1 120 ? -65.203 15.425  11.249  1.00 19.55 ? 99  PRO   B O    1 
ATOM   2738 C  CB   . PRO   B 1 120 ? -62.573 17.150  11.981  1.00 22.10 ? 99  PRO   B CB   1 
ATOM   2739 C  CG   . PRO   B 1 120 ? -62.575 17.985  10.719  1.00 22.86 ? 99  PRO   B CG   1 
ATOM   2740 C  CD   . PRO   B 1 120 ? -62.562 17.093  9.491   1.00 21.66 ? 99  PRO   B CD   1 
ATOM   2741 N  N    . THR   B 1 121 ? -64.186 14.462  13.047  1.00 17.59 ? 100 THR   B N    1 
ATOM   2742 C  CA   . THR   B 1 121 ? -65.384 13.990  13.724  1.00 18.67 ? 100 THR   B CA   1 
ATOM   2743 C  C    . THR   B 1 121 ? -65.232 14.273  15.218  1.00 18.50 ? 100 THR   B C    1 
ATOM   2744 O  O    . THR   B 1 121 ? -64.933 13.381  16.017  1.00 17.57 ? 100 THR   B O    1 
ATOM   2745 C  CB   . THR   B 1 121 ? -65.574 12.492  13.466  1.00 18.40 ? 100 THR   B CB   1 
ATOM   2746 O  OG1  . THR   B 1 121 ? -64.447 11.752  13.951  1.00 18.73 ? 100 THR   B OG1  1 
ATOM   2747 C  CG2  . THR   B 1 121 ? -65.782 12.189  11.992  1.00 19.06 ? 100 THR   B CG2  1 
ATOM   2748 N  N    . PRO   B 1 122 ? -65.420 15.533  15.659  1.00 19.26 ? 101 PRO   B N    1 
ATOM   2749 C  CA   . PRO   B 1 122 ? -65.230 15.893  17.062  1.00 19.78 ? 101 PRO   B CA   1 
ATOM   2750 C  C    . PRO   B 1 122 ? -66.118 15.082  17.997  1.00 21.15 ? 101 PRO   B C    1 
ATOM   2751 O  O    . PRO   B 1 122 ? -67.265 14.767  17.664  1.00 21.47 ? 101 PRO   B O    1 
ATOM   2752 C  CB   . PRO   B 1 122 ? -65.601 17.396  17.142  1.00 21.56 ? 101 PRO   B CB   1 
ATOM   2753 C  CG   . PRO   B 1 122 ? -65.741 17.856  15.718  1.00 23.87 ? 101 PRO   B CG   1 
ATOM   2754 C  CD   . PRO   B 1 122 ? -65.929 16.642  14.835  1.00 21.64 ? 101 PRO   B CD   1 
ATOM   2755 N  N    . LEU   B 1 123 ? -65.580 14.776  19.183  1.00 19.51 ? 102 LEU   B N    1 
ATOM   2756 C  CA   . LEU   B 1 123 ? -66.341 14.026  20.164  1.00 21.21 ? 102 LEU   B CA   1 
ATOM   2757 C  C    . LEU   B 1 123 ? -67.359 14.933  20.840  1.00 25.56 ? 102 LEU   B C    1 
ATOM   2758 O  O    . LEU   B 1 123 ? -68.378 14.442  21.311  1.00 27.85 ? 102 LEU   B O    1 
ATOM   2759 C  CB   . LEU   B 1 123 ? -65.398 13.418  21.197  1.00 19.94 ? 102 LEU   B CB   1 
ATOM   2760 C  CG   . LEU   B 1 123 ? -64.488 12.317  20.663  1.00 18.86 ? 102 LEU   B CG   1 
ATOM   2761 C  CD1  . LEU   B 1 123 ? -63.409 12.004  21.694  1.00 19.22 ? 102 LEU   B CD1  1 
ATOM   2762 C  CD2  . LEU   B 1 123 ? -65.327 11.089  20.408  1.00 19.71 ? 102 LEU   B CD2  1 
ATOM   2763 N  N    . VAL   B 1 124 ? -67.034 16.226  20.917  1.00 27.52 ? 103 VAL   B N    1 
ATOM   2764 C  CA   . VAL   B 1 124 ? -67.854 17.180  21.650  1.00 36.80 ? 103 VAL   B CA   1 
ATOM   2765 C  C    . VAL   B 1 124 ? -68.285 18.295  20.683  1.00 37.96 ? 103 VAL   B C    1 
ATOM   2766 O  O    . VAL   B 1 124 ? -67.373 18.846  20.029  1.00 41.66 ? 103 VAL   B O    1 
ATOM   2767 C  CB   . VAL   B 1 124 ? -67.065 17.734  22.857  1.00 39.69 ? 103 VAL   B CB   1 
ATOM   2768 C  CG1  . VAL   B 1 124 ? -67.693 18.997  23.436  1.00 45.54 ? 103 VAL   B CG1  1 
ATOM   2769 C  CG2  . VAL   B 1 124 ? -66.894 16.688  23.954  1.00 39.76 ? 103 VAL   B CG2  1 
ATOM   2770 N  N    . GLY   B 1 134 ? -72.669 18.771  8.494   0.70 43.12 ? 113 GLY   B N    1 
ATOM   2771 C  CA   . GLY   B 1 134 ? -74.004 18.390  7.990   0.70 43.88 ? 113 GLY   B CA   1 
ATOM   2772 C  C    . GLY   B 1 134 ? -74.283 16.901  8.184   0.70 40.91 ? 113 GLY   B C    1 
ATOM   2773 O  O    . GLY   B 1 134 ? -75.442 16.491  8.218   0.70 44.80 ? 113 GLY   B O    1 
ATOM   2774 N  N    . LYS   B 1 135 ? -73.214 16.103  8.316   1.00 37.60 ? 114 LYS   B N    1 
ATOM   2775 C  CA   . LYS   B 1 135 ? -73.331 14.651  8.351   1.00 33.31 ? 114 LYS   B CA   1 
ATOM   2776 C  C    . LYS   B 1 135 ? -73.738 14.174  9.744   1.00 30.59 ? 114 LYS   B C    1 
ATOM   2777 O  O    . LYS   B 1 135 ? -73.199 14.628  10.752  1.00 29.78 ? 114 LYS   B O    1 
ATOM   2778 C  CB   . LYS   B 1 135 ? -72.038 13.975  7.881   1.00 33.18 ? 114 LYS   B CB   1 
ATOM   2779 C  CG   . LYS   B 1 135 ? -71.715 14.268  6.415   1.00 38.72 ? 114 LYS   B CG   1 
ATOM   2780 C  CD   . LYS   B 1 135 ? -70.418 13.674  5.885   1.00 39.21 ? 114 LYS   B CD   1 
ATOM   2781 C  CE   . LYS   B 1 135 ? -70.390 13.728  4.391   1.00 37.62 ? 114 LYS   B CE   1 
ATOM   2782 N  NZ   . LYS   B 1 135 ? -69.093 13.255  3.914   1.00 42.17 ? 114 LYS   B NZ   1 
ATOM   2783 N  N    . THR   B 1 136 ? -74.688 13.231  9.783   1.00 28.50 ? 115 THR   B N    1 
ATOM   2784 C  CA   . THR   B 1 136 ? -75.039 12.567  11.030  1.00 25.93 ? 115 THR   B CA   1 
ATOM   2785 C  C    . THR   B 1 136 ? -73.846 11.725  11.472  1.00 23.53 ? 115 THR   B C    1 
ATOM   2786 O  O    . THR   B 1 136 ? -72.996 11.376  10.644  1.00 21.42 ? 115 THR   B O    1 
ATOM   2787 C  CB   . THR   B 1 136 ? -76.276 11.685  10.867  1.00 29.03 ? 115 THR   B CB   1 
ATOM   2788 O  OG1  . THR   B 1 136 ? -75.944 10.605  9.998   1.00 27.90 ? 115 THR   B OG1  1 
ATOM   2789 C  CG2  . THR   B 1 136 ? -77.471 12.448  10.326  1.00 31.17 ? 115 THR   B CG2  1 
ATOM   2790 N  N    . VAL   B 1 137 ? -73.821 11.378  12.767  1.00 20.76 ? 116 VAL   B N    1 
ATOM   2791 C  CA   A VAL   B 1 137 ? -72.733 10.576  13.304  0.70 20.66 ? 116 VAL   B CA   1 
ATOM   2792 C  CA   B VAL   B 1 137 ? -72.714 10.586  13.284  0.30 20.64 ? 116 VAL   B CA   1 
ATOM   2793 C  C    . VAL   B 1 137 ? -72.740 9.214   12.616  1.00 20.11 ? 116 VAL   B C    1 
ATOM   2794 O  O    . VAL   B 1 137 ? -71.686 8.635   12.346  1.00 18.84 ? 116 VAL   B O    1 
ATOM   2795 C  CB   A VAL   B 1 137 ? -72.711 10.462  14.842  0.70 20.29 ? 116 VAL   B CB   1 
ATOM   2796 C  CB   B VAL   B 1 137 ? -72.549 10.469  14.815  0.30 20.51 ? 116 VAL   B CB   1 
ATOM   2797 C  CG1  A VAL   B 1 137 ? -73.960 9.811   15.420  0.70 22.75 ? 116 VAL   B CG1  1 
ATOM   2798 C  CG1  B VAL   B 1 137 ? -72.912 11.760  15.542  0.30 20.04 ? 116 VAL   B CG1  1 
ATOM   2799 C  CG2  A VAL   B 1 137 ? -71.440 9.776   15.336  0.70 19.24 ? 116 VAL   B CG2  1 
ATOM   2800 C  CG2  B VAL   B 1 137 ? -73.286 9.272   15.401  0.30 20.70 ? 116 VAL   B CG2  1 
ATOM   2801 N  N    . GLU   B 1 138 ? -73.936 8.689   12.326  1.00 21.03 ? 117 GLU   B N    1 
ATOM   2802 C  CA   . GLU   B 1 138 ? -73.934 7.366   11.715  1.00 22.09 ? 117 GLU   B CA   1 
ATOM   2803 C  C    . GLU   B 1 138 ? -73.323 7.408   10.311  1.00 19.68 ? 117 GLU   B C    1 
ATOM   2804 O  O    . GLU   B 1 138 ? -72.675 6.438   9.911   1.00 18.56 ? 117 GLU   B O    1 
ATOM   2805 C  CB   . GLU   B 1 138 ? -75.232 6.558   11.857  1.00 28.02 ? 117 GLU   B CB   1 
ATOM   2806 C  CG   . GLU   B 1 138 ? -76.460 7.253   11.286  1.00 31.02 ? 117 GLU   B CG   1 
ATOM   2807 C  CD   . GLU   B 1 138 ? -77.162 8.288   12.155  1.00 35.79 ? 117 GLU   B CD   1 
ATOM   2808 O  OE1  . GLU   B 1 138 ? -76.587 8.850   13.115  1.00 28.44 ? 117 GLU   B OE1  1 
ATOM   2809 O  OE2  . GLU   B 1 138 ? -78.359 8.502   11.864  1.00 39.25 ? 117 GLU   B OE2  1 
ATOM   2810 N  N    . THR   B 1 139 ? -73.499 8.517   9.579   1.00 19.88 ? 118 THR   B N    1 
ATOM   2811 C  CA   . THR   B 1 139 ? -72.870 8.668   8.275   1.00 21.37 ? 118 THR   B CA   1 
ATOM   2812 C  C    . THR   B 1 139 ? -71.350 8.755   8.436   1.00 19.76 ? 118 THR   B C    1 
ATOM   2813 O  O    . THR   B 1 139 ? -70.613 8.184   7.618   1.00 19.33 ? 118 THR   B O    1 
ATOM   2814 C  CB   . THR   B 1 139 ? -73.402 9.890   7.521   1.00 24.67 ? 118 THR   B CB   1 
ATOM   2815 O  OG1  . THR   B 1 139 ? -74.764 9.573   7.255   1.00 27.84 ? 118 THR   B OG1  1 
ATOM   2816 C  CG2  . THR   B 1 139 ? -72.650 10.131  6.225   1.00 24.46 ? 118 THR   B CG2  1 
ATOM   2817 N  N    . GLN   B 1 140 ? -70.908 9.501   9.462   1.00 17.45 ? 119 GLN   B N    1 
ATOM   2818 C  CA   . GLN   B 1 140 ? -69.489 9.685   9.760   1.00 17.24 ? 119 GLN   B CA   1 
ATOM   2819 C  C    . GLN   B 1 140 ? -68.860 8.309   9.993   1.00 16.26 ? 119 GLN   B C    1 
ATOM   2820 O  O    . GLN   B 1 140 ? -67.799 8.015   9.428   1.00 16.59 ? 119 GLN   B O    1 
ATOM   2821 C  CB   . GLN   B 1 140 ? -69.284 10.584  10.976  1.00 17.78 ? 119 GLN   B CB   1 
ATOM   2822 C  CG   . GLN   B 1 140 ? -69.737 12.032  10.768  1.00 21.89 ? 119 GLN   B CG   1 
ATOM   2823 C  CD   . GLN   B 1 140 ? -69.837 12.785  12.075  1.00 25.87 ? 119 GLN   B CD   1 
ATOM   2824 O  OE1  . GLN   B 1 140 ? -69.010 12.633  12.984  1.00 29.13 ? 119 GLN   B OE1  1 
ATOM   2825 N  NE2  . GLN   B 1 140 ? -70.904 13.557  12.232  1.00 29.85 ? 119 GLN   B NE2  1 
ATOM   2826 N  N    . VAL   B 1 141 ? -69.490 7.497   10.852  1.00 16.09 ? 120 VAL   B N    1 
ATOM   2827 C  CA   . VAL   B 1 141 ? -68.984 6.160   11.126  1.00 16.01 ? 120 VAL   B CA   1 
ATOM   2828 C  C    . VAL   B 1 141 ? -68.944 5.354   9.833   1.00 15.31 ? 120 VAL   B C    1 
ATOM   2829 O  O    . VAL   B 1 141 ? -67.936 4.734   9.510   1.00 16.54 ? 120 VAL   B O    1 
ATOM   2830 C  CB   . VAL   B 1 141 ? -69.879 5.468   12.164  1.00 15.45 ? 120 VAL   B CB   1 
ATOM   2831 C  CG1  . VAL   B 1 141 ? -69.612 3.964   12.219  1.00 16.94 ? 120 VAL   B CG1  1 
ATOM   2832 C  CG2  . VAL   B 1 141 ? -69.761 6.118   13.539  1.00 15.93 ? 120 VAL   B CG2  1 
ATOM   2833 N  N    . ALA   B 1 142 ? -70.030 5.410   9.056   1.00 16.70 ? 121 ALA   B N    1 
ATOM   2834 C  CA   . ALA   B 1 142 ? -70.130 4.563   7.875   1.00 16.38 ? 121 ALA   B CA   1 
ATOM   2835 C  C    . ALA   B 1 142 ? -69.052 4.938   6.853   1.00 16.87 ? 121 ALA   B C    1 
ATOM   2836 O  O    . ALA   B 1 142 ? -68.401 4.075   6.277   1.00 16.70 ? 121 ALA   B O    1 
ATOM   2837 C  CB   . ALA   B 1 142 ? -71.514 4.703   7.281   1.00 16.49 ? 121 ALA   B CB   1 
ATOM   2838 N  N    . GLU   B 1 143 ? -68.839 6.238   6.647   1.00 17.44 ? 122 GLU   B N    1 
ATOM   2839 C  CA   . GLU   B 1 143 ? -67.849 6.669   5.662   1.00 17.23 ? 122 GLU   B CA   1 
ATOM   2840 C  C    . GLU   B 1 143 ? -66.407 6.422   6.110   1.00 16.40 ? 122 GLU   B C    1 
ATOM   2841 O  O    . GLU   B 1 143 ? -65.588 5.913   5.342   1.00 17.44 ? 122 GLU   B O    1 
ATOM   2842 C  CB   . GLU   B 1 143 ? -68.032 8.156   5.389   1.00 18.21 ? 122 GLU   B CB   1 
ATOM   2843 C  CG   . GLU   B 1 143 ? -69.301 8.416   4.584   1.00 19.96 ? 122 GLU   B CG   1 
ATOM   2844 C  CD   . GLU   B 1 143 ? -69.520 9.860   4.183   1.00 22.72 ? 122 GLU   B CD   1 
ATOM   2845 O  OE1  . GLU   B 1 143 ? -68.779 10.758  4.621   1.00 24.57 ? 122 GLU   B OE1  1 
ATOM   2846 O  OE2  . GLU   B 1 143 ? -70.486 10.076  3.412   1.00 24.34 ? 122 GLU   B OE2  1 
ATOM   2847 N  N    . LEU   B 1 144 ? -66.092 6.800   7.354   1.00 15.50 ? 123 LEU   B N    1 
ATOM   2848 C  CA   . LEU   B 1 144 ? -64.704 6.748   7.794   1.00 15.57 ? 123 LEU   B CA   1 
ATOM   2849 C  C    . LEU   B 1 144 ? -64.287 5.318   8.097   1.00 15.97 ? 123 LEU   B C    1 
ATOM   2850 O  O    . LEU   B 1 144 ? -63.174 4.950   7.731   1.00 16.51 ? 123 LEU   B O    1 
ATOM   2851 C  CB   . LEU   B 1 144 ? -64.445 7.722   8.939   1.00 15.78 ? 123 LEU   B CB   1 
ATOM   2852 C  CG   . LEU   B 1 144 ? -64.521 9.198   8.531   1.00 17.37 ? 123 LEU   B CG   1 
ATOM   2853 C  CD1  . LEU   B 1 144 ? -64.703 10.048  9.744   1.00 20.17 ? 123 LEU   B CD1  1 
ATOM   2854 C  CD2  . LEU   B 1 144 ? -63.241 9.631   7.823   1.00 21.12 ? 123 LEU   B CD2  1 
ATOM   2855 N  N    . ILE   B 1 145 ? -65.163 4.541   8.748   1.00 16.20 ? 124 ILE   B N    1 
ATOM   2856 C  CA   . ILE   B 1 145 ? -64.785 3.172   9.063   1.00 16.35 ? 124 ILE   B CA   1 
ATOM   2857 C  C    . ILE   B 1 145 ? -64.986 2.294   7.834   1.00 18.27 ? 124 ILE   B C    1 
ATOM   2858 O  O    . ILE   B 1 145 ? -64.189 1.386   7.609   1.00 16.67 ? 124 ILE   B O    1 
ATOM   2859 C  CB   . ILE   B 1 145 ? -65.533 2.677   10.313  1.00 15.21 ? 124 ILE   B CB   1 
ATOM   2860 C  CG1  . ILE   B 1 145 ? -65.360 3.639   11.507  1.00 14.47 ? 124 ILE   B CG1  1 
ATOM   2861 C  CG2  . ILE   B 1 145 ? -65.156 1.230   10.665  1.00 16.07 ? 124 ILE   B CG2  1 
ATOM   2862 C  CD1  . ILE   B 1 145 ? -63.923 3.814   11.972  1.00 17.18 ? 124 ILE   B CD1  1 
ATOM   2863 N  N    . GLY   B 1 146 ? -65.990 2.612   7.004   1.00 17.39 ? 125 GLY   B N    1 
ATOM   2864 C  CA   . GLY   B 1 146 ? -66.182 1.881   5.758   1.00 17.27 ? 125 GLY   B CA   1 
ATOM   2865 C  C    . GLY   B 1 146 ? -64.978 1.996   4.823   1.00 16.70 ? 125 GLY   B C    1 
ATOM   2866 O  O    . GLY   B 1 146 ? -64.377 1.002   4.425   1.00 16.25 ? 125 GLY   B O    1 
ATOM   2867 N  N    . THR   B 1 147 ? -64.608 3.225   4.456   1.00 15.74 ? 126 THR   B N    1 
ATOM   2868 C  CA   . THR   B 1 147 ? -63.550 3.366   3.467   1.00 16.24 ? 126 THR   B CA   1 
ATOM   2869 C  C    . THR   B 1 147 ? -62.198 2.890   3.997   1.00 16.54 ? 126 THR   B C    1 
ATOM   2870 O  O    . THR   B 1 147 ? -61.446 2.251   3.262   1.00 16.34 ? 126 THR   B O    1 
ATOM   2871 C  CB   . THR   B 1 147 ? -63.450 4.813   2.969   1.00 17.80 ? 126 THR   B CB   1 
ATOM   2872 O  OG1  . THR   B 1 147 ? -63.038 5.627   4.061   1.00 20.94 ? 126 THR   B OG1  1 
ATOM   2873 C  CG2  . THR   B 1 147 ? -64.775 5.322   2.428   1.00 16.82 ? 126 THR   B CG2  1 
ATOM   2874 N  N    . ASN   B 1 148 ? -61.890 3.205   5.268   1.00 15.24 ? 127 ASN   B N    1 
ATOM   2875 C  CA   . ASN   B 1 148 ? -60.532 3.019   5.756   1.00 15.87 ? 127 ASN   B CA   1 
ATOM   2876 C  C    . ASN   B 1 148 ? -60.269 1.604   6.251   1.00 16.26 ? 127 ASN   B C    1 
ATOM   2877 O  O    . ASN   B 1 148 ? -59.105 1.220   6.377   1.00 17.39 ? 127 ASN   B O    1 
ATOM   2878 C  CB   . ASN   B 1 148 ? -60.160 4.034   6.828   1.00 16.75 ? 127 ASN   B CB   1 
ATOM   2879 C  CG   . ASN   B 1 148 ? -59.939 5.398   6.226   1.00 18.51 ? 127 ASN   B CG   1 
ATOM   2880 O  OD1  . ASN   B 1 148 ? -58.938 5.610   5.521   1.00 21.43 ? 127 ASN   B OD1  1 
ATOM   2881 N  ND2  . ASN   B 1 148 ? -60.799 6.346   6.549   1.00 17.81 ? 127 ASN   B ND2  1 
ATOM   2882 N  N    . ALA   B 1 149 ? -61.340 0.857   6.555   1.00 16.01 ? 128 ALA   B N    1 
ATOM   2883 C  CA   . ALA   B 1 149 ? -61.139 -0.420  7.227   1.00 15.30 ? 128 ALA   B CA   1 
ATOM   2884 C  C    . ALA   B 1 149 ? -62.045 -1.527  6.701   1.00 14.76 ? 128 ALA   B C    1 
ATOM   2885 O  O    . ALA   B 1 149 ? -61.554 -2.609  6.365   1.00 14.84 ? 128 ALA   B O    1 
ATOM   2886 C  CB   . ALA   B 1 149 ? -61.348 -0.237  8.721   1.00 16.79 ? 128 ALA   B CB   1 
ATOM   2887 N  N    . ILE   B 1 150 ? -63.368 -1.304  6.718   1.00 14.62 ? 129 ILE   B N    1 
ATOM   2888 C  CA   . ILE   B 1 150 ? -64.262 -2.400  6.351   1.00 15.29 ? 129 ILE   B CA   1 
ATOM   2889 C  C    . ILE   B 1 150 ? -64.140 -2.762  4.866   1.00 15.41 ? 129 ILE   B C    1 
ATOM   2890 O  O    . ILE   B 1 150 ? -64.066 -3.946  4.516   1.00 15.35 ? 129 ILE   B O    1 
ATOM   2891 C  CB   . ILE   B 1 150 ? -65.713 -2.083  6.751   1.00 15.14 ? 129 ILE   B CB   1 
ATOM   2892 C  CG1  . ILE   B 1 150 ? -65.810 -1.905  8.282   1.00 16.32 ? 129 ILE   B CG1  1 
ATOM   2893 C  CG2  . ILE   B 1 150 ? -66.643 -3.209  6.282   1.00 16.33 ? 129 ILE   B CG2  1 
ATOM   2894 C  CD1  . ILE   B 1 150 ? -67.122 -1.316  8.768   1.00 20.57 ? 129 ILE   B CD1  1 
ATOM   2895 N  N    . ALA   B 1 151 ? -64.090 -1.746  4.008   1.00 15.08 ? 130 ALA   B N    1 
ATOM   2896 C  CA   . ALA   B 1 151 ? -63.951 -2.022  2.587   1.00 15.32 ? 130 ALA   B CA   1 
ATOM   2897 C  C    . ALA   B 1 151 ? -62.633 -2.740  2.321   1.00 16.02 ? 130 ALA   B C    1 
ATOM   2898 O  O    . ALA   B 1 151 ? -62.625 -3.758  1.623   1.00 14.36 ? 130 ALA   B O    1 
ATOM   2899 C  CB   . ALA   B 1 151 ? -64.152 -0.790  1.732   1.00 15.79 ? 130 ALA   B CB   1 
ATOM   2900 N  N    . PRO   B 1 152 ? -61.476 -2.320  2.893   1.00 13.94 ? 131 PRO   B N    1 
ATOM   2901 C  CA   . PRO   B 1 152 ? -60.263 -3.121  2.746   1.00 13.89 ? 131 PRO   B CA   1 
ATOM   2902 C  C    . PRO   B 1 152 ? -60.412 -4.571  3.183   1.00 13.87 ? 131 PRO   B C    1 
ATOM   2903 O  O    . PRO   B 1 152 ? -59.850 -5.445  2.537   1.00 15.03 ? 131 PRO   B O    1 
ATOM   2904 C  CB   . PRO   B 1 152 ? -59.219 -2.338  3.578   1.00 14.60 ? 131 PRO   B CB   1 
ATOM   2905 C  CG   . PRO   B 1 152 ? -59.677 -0.886  3.404   1.00 15.36 ? 131 PRO   B CG   1 
ATOM   2906 C  CD   . PRO   B 1 152 ? -61.206 -0.978  3.441   1.00 14.63 ? 131 PRO   B CD   1 
ATOM   2907 N  N    . PHE   B 1 153 ? -61.123 -4.797  4.292   1.00 13.74 ? 132 PHE   B N    1 
ATOM   2908 C  CA   . PHE   B 1 153 ? -61.344 -6.161  4.756   1.00 14.07 ? 132 PHE   B CA   1 
ATOM   2909 C  C    . PHE   B 1 153 ? -62.131 -6.954  3.710   1.00 14.19 ? 132 PHE   B C    1 
ATOM   2910 O  O    . PHE   B 1 153 ? -61.741 -8.085  3.384   1.00 14.17 ? 132 PHE   B O    1 
ATOM   2911 C  CB   . PHE   B 1 153 ? -62.035 -6.131  6.123   1.00 15.07 ? 132 PHE   B CB   1 
ATOM   2912 C  CG   . PHE   B 1 153 ? -62.638 -7.472  6.508   1.00 15.75 ? 132 PHE   B CG   1 
ATOM   2913 C  CD1  . PHE   B 1 153 ? -61.872 -8.470  7.103   1.00 15.90 ? 132 PHE   B CD1  1 
ATOM   2914 C  CD2  . PHE   B 1 153 ? -64.000 -7.702  6.301   1.00 17.43 ? 132 PHE   B CD2  1 
ATOM   2915 C  CE1  . PHE   B 1 153 ? -62.431 -9.713  7.405   1.00 16.13 ? 132 PHE   B CE1  1 
ATOM   2916 C  CE2  . PHE   B 1 153 ? -64.551 -8.930  6.620   1.00 17.67 ? 132 PHE   B CE2  1 
ATOM   2917 C  CZ   . PHE   B 1 153 ? -63.770 -9.923  7.176   1.00 17.15 ? 132 PHE   B CZ   1 
ATOM   2918 N  N    . LEU   B 1 154 ? -63.251 -6.396  3.239   1.00 14.48 ? 133 LEU   B N    1 
ATOM   2919 C  CA   . LEU   B 1 154 ? -64.105 -7.094  2.283   1.00 15.05 ? 133 LEU   B CA   1 
ATOM   2920 C  C    . LEU   B 1 154 ? -63.387 -7.321  0.950   1.00 15.12 ? 133 LEU   B C    1 
ATOM   2921 O  O    . LEU   B 1 154 ? -63.500 -8.384  0.342   1.00 16.12 ? 133 LEU   B O    1 
ATOM   2922 C  CB   . LEU   B 1 154 ? -65.426 -6.346  2.130   1.00 14.96 ? 133 LEU   B CB   1 
ATOM   2923 C  CG   . LEU   B 1 154 ? -66.294 -6.288  3.393   1.00 16.13 ? 133 LEU   B CG   1 
ATOM   2924 C  CD1  . LEU   B 1 154 ? -67.348 -5.209  3.216   1.00 16.84 ? 133 LEU   B CD1  1 
ATOM   2925 C  CD2  . LEU   B 1 154 ? -66.908 -7.660  3.679   1.00 18.28 ? 133 LEU   B CD2  1 
ATOM   2926 N  N    . LEU   B 1 155 ? -62.609 -6.340  0.489   1.00 14.70 ? 134 LEU   B N    1 
ATOM   2927 C  CA   . LEU   B 1 155 ? -61.811 -6.484  -0.718  1.00 14.32 ? 134 LEU   B CA   1 
ATOM   2928 C  C    . LEU   B 1 155 ? -60.745 -7.566  -0.560  1.00 14.79 ? 134 LEU   B C    1 
ATOM   2929 O  O    . LEU   B 1 155 ? -60.464 -8.334  -1.482  1.00 14.96 ? 134 LEU   B O    1 
ATOM   2930 C  CB   . LEU   B 1 155 ? -61.191 -5.132  -1.059  1.00 14.51 ? 134 LEU   B CB   1 
ATOM   2931 C  CG   . LEU   B 1 155 ? -62.185 -4.111  -1.631  1.00 14.99 ? 134 LEU   B CG   1 
ATOM   2932 C  CD1  . LEU   B 1 155 ? -61.574 -2.713  -1.558  1.00 15.55 ? 134 LEU   B CD1  1 
ATOM   2933 C  CD2  . LEU   B 1 155 ? -62.581 -4.478  -3.079  1.00 15.65 ? 134 LEU   B CD2  1 
ATOM   2934 N  N    . THR   B 1 156 ? -60.129 -7.613  0.628   1.00 14.14 ? 135 THR   B N    1 
ATOM   2935 C  CA   . THR   B 1 156 ? -59.134 -8.631  0.937   1.00 13.97 ? 135 THR   B CA   1 
ATOM   2936 C  C    . THR   B 1 156 ? -59.788 -10.008 0.864   1.00 14.51 ? 135 THR   B C    1 
ATOM   2937 O  O    . THR   B 1 156 ? -59.164 -10.918 0.336   1.00 16.01 ? 135 THR   B O    1 
ATOM   2938 C  CB   . THR   B 1 156 ? -58.518 -8.392  2.320   1.00 14.60 ? 135 THR   B CB   1 
ATOM   2939 O  OG1  . THR   B 1 156 ? -57.814 -7.144  2.256   1.00 15.54 ? 135 THR   B OG1  1 
ATOM   2940 C  CG2  . THR   B 1 156 ? -57.514 -9.461  2.730   1.00 14.27 ? 135 THR   B CG2  1 
ATOM   2941 N  N    . MET   B 1 157 ? -60.996 -10.148 1.427   1.00 15.29 ? 136 MET   B N    1 
ATOM   2942 C  CA   A MET   B 1 157 ? -61.680 -11.440 1.424   0.60 16.43 ? 136 MET   B CA   1 
ATOM   2943 C  CA   B MET   B 1 157 ? -61.668 -11.440 1.426   0.40 15.87 ? 136 MET   B CA   1 
ATOM   2944 C  C    . MET   B 1 157 ? -61.956 -11.860 -0.017  1.00 17.05 ? 136 MET   B C    1 
ATOM   2945 O  O    . MET   B 1 157 ? -61.683 -12.991 -0.402  1.00 17.12 ? 136 MET   B O    1 
ATOM   2946 C  CB   A MET   B 1 157 ? -63.062 -11.365 2.081   0.60 19.30 ? 136 MET   B CB   1 
ATOM   2947 C  CB   B MET   B 1 157 ? -62.946 -11.365 2.270   0.40 16.82 ? 136 MET   B CB   1 
ATOM   2948 C  CG   A MET   B 1 157 ? -63.078 -11.306 3.590   0.60 21.46 ? 136 MET   B CG   1 
ATOM   2949 C  CG   B MET   B 1 157 ? -63.847 -12.576 2.182   0.40 16.90 ? 136 MET   B CG   1 
ATOM   2950 S  SD   A MET   B 1 157 ? -64.777 -11.503 4.177   0.60 25.12 ? 136 MET   B SD   1 
ATOM   2951 S  SD   B MET   B 1 157 ? -65.295 -12.387 3.244   0.40 19.59 ? 136 MET   B SD   1 
ATOM   2952 C  CE   A MET   B 1 157 ? -64.962 -13.287 4.074   0.60 24.37 ? 136 MET   B CE   1 
ATOM   2953 C  CE   B MET   B 1 157 ? -64.450 -12.588 4.817   0.40 19.33 ? 136 MET   B CE   1 
ATOM   2954 N  N    . SER   B 1 158 ? -62.508 -10.937 -0.808  1.00 16.68 ? 137 SER   B N    1 
ATOM   2955 C  CA   . SER   B 1 158 ? -62.851 -11.248 -2.190  1.00 17.36 ? 137 SER   B CA   1 
ATOM   2956 C  C    . SER   B 1 158 ? -61.590 -11.564 -2.995  1.00 17.76 ? 137 SER   B C    1 
ATOM   2957 O  O    . SER   B 1 158 ? -61.574 -12.508 -3.774  1.00 18.37 ? 137 SER   B O    1 
ATOM   2958 C  CB   . SER   B 1 158 ? -63.643 -10.158 -2.843  1.00 17.24 ? 137 SER   B CB   1 
ATOM   2959 O  OG   . SER   B 1 158 ? -64.941 -10.093 -2.272  1.00 23.22 ? 137 SER   B OG   1 
ATOM   2960 N  N    . PHE   B 1 159 ? -60.519 -10.787 -2.790  1.00 16.88 ? 138 PHE   B N    1 
ATOM   2961 C  CA   . PHE   B 1 159 ? -59.262 -11.030 -3.478  1.00 16.27 ? 138 PHE   B CA   1 
ATOM   2962 C  C    . PHE   B 1 159 ? -58.744 -12.432 -3.156  1.00 17.64 ? 138 PHE   B C    1 
ATOM   2963 O  O    . PHE   B 1 159 ? -58.360 -13.174 -4.052  1.00 17.90 ? 138 PHE   B O    1 
ATOM   2964 C  CB   . PHE   B 1 159 ? -58.280 -9.937  -3.054  1.00 15.83 ? 138 PHE   B CB   1 
ATOM   2965 C  CG   . PHE   B 1 159 ? -56.870 -10.147 -3.583  1.00 14.89 ? 138 PHE   B CG   1 
ATOM   2966 C  CD1  . PHE   B 1 159 ? -55.954 -10.956 -2.914  1.00 15.32 ? 138 PHE   B CD1  1 
ATOM   2967 C  CD2  . PHE   B 1 159 ? -56.447 -9.531  -4.757  1.00 15.42 ? 138 PHE   B CD2  1 
ATOM   2968 C  CE1  . PHE   B 1 159 ? -54.658 -11.113 -3.409  1.00 16.24 ? 138 PHE   B CE1  1 
ATOM   2969 C  CE2  . PHE   B 1 159 ? -55.150 -9.680  -5.240  1.00 15.28 ? 138 PHE   B CE2  1 
ATOM   2970 C  CZ   . PHE   B 1 159 ? -54.255 -10.487 -4.568  1.00 17.22 ? 138 PHE   B CZ   1 
ATOM   2971 N  N    . ALA   B 1 160 ? -58.752 -12.808 -1.876  1.00 16.38 ? 139 ALA   B N    1 
ATOM   2972 C  CA   . ALA   B 1 160 ? -58.201 -14.099 -1.489  1.00 17.83 ? 139 ALA   B CA   1 
ATOM   2973 C  C    . ALA   B 1 160 ? -59.058 -15.249 -2.029  1.00 18.66 ? 139 ALA   B C    1 
ATOM   2974 O  O    . ALA   B 1 160 ? -58.501 -16.235 -2.505  1.00 20.61 ? 139 ALA   B O    1 
ATOM   2975 C  CB   . ALA   B 1 160 ? -58.052 -14.155 0.024   1.00 18.05 ? 139 ALA   B CB   1 
ATOM   2976 N  N    . GLN   B 1 161 ? -60.388 -15.099 -1.970  1.00 19.73 ? 140 GLN   B N    1 
ATOM   2977 C  CA   A GLN   B 1 161 ? -61.264 -16.212 -2.306  0.60 21.36 ? 140 GLN   B CA   1 
ATOM   2978 C  CA   B GLN   B 1 161 ? -61.306 -16.180 -2.315  0.40 21.01 ? 140 GLN   B CA   1 
ATOM   2979 C  C    . GLN   B 1 161 ? -61.208 -16.491 -3.803  1.00 23.01 ? 140 GLN   B C    1 
ATOM   2980 O  O    . GLN   B 1 161 ? -61.373 -17.641 -4.214  1.00 24.16 ? 140 GLN   B O    1 
ATOM   2981 C  CB   A GLN   B 1 161 ? -62.672 -15.946 -1.786  0.60 23.40 ? 140 GLN   B CB   1 
ATOM   2982 C  CB   B GLN   B 1 161 ? -62.775 -15.817 -2.102  0.40 21.42 ? 140 GLN   B CB   1 
ATOM   2983 C  CG   A GLN   B 1 161 ? -62.726 -15.968 -0.262  0.60 25.71 ? 140 GLN   B CG   1 
ATOM   2984 C  CG   B GLN   B 1 161 ? -63.722 -17.000 -2.292  0.40 22.72 ? 140 GLN   B CG   1 
ATOM   2985 C  CD   A GLN   B 1 161 ? -64.090 -15.676 0.318   0.60 30.05 ? 140 GLN   B CD   1 
ATOM   2986 C  CD   B GLN   B 1 161 ? -63.487 -18.102 -1.283  0.40 23.83 ? 140 GLN   B CD   1 
ATOM   2987 O  OE1  A GLN   B 1 161 ? -64.261 -15.651 1.542   0.60 29.69 ? 140 GLN   B OE1  1 
ATOM   2988 O  OE1  B GLN   B 1 161 ? -63.455 -17.863 -0.071  0.40 23.64 ? 140 GLN   B OE1  1 
ATOM   2989 N  NE2  A GLN   B 1 161 ? -65.071 -15.460 -0.550  0.60 31.77 ? 140 GLN   B NE2  1 
ATOM   2990 N  NE2  B GLN   B 1 161 ? -63.300 -19.320 -1.774  0.40 25.63 ? 140 GLN   B NE2  1 
ATOM   2991 N  N    . ARG   B 1 162 ? -60.961 -15.440 -4.587  1.00 23.91 ? 141 ARG   B N    1 
ATOM   2992 C  CA   . ARG   B 1 162 ? -61.053 -15.524 -6.040  1.00 27.76 ? 141 ARG   B CA   1 
ATOM   2993 C  C    . ARG   B 1 162 ? -59.778 -16.103 -6.639  1.00 29.96 ? 141 ARG   B C    1 
ATOM   2994 O  O    . ARG   B 1 162 ? -59.746 -16.412 -7.833  1.00 34.12 ? 141 ARG   B O    1 
ATOM   2995 C  CB   . ARG   B 1 162 ? -61.345 -14.162 -6.689  1.00 27.09 ? 141 ARG   B CB   1 
ATOM   2996 C  CG   . ARG   B 1 162 ? -62.747 -13.602 -6.496  1.00 29.83 ? 141 ARG   B CG   1 
ATOM   2997 C  CD   . ARG   B 1 162 ? -63.835 -14.348 -7.266  0.60 28.97 ? 141 ARG   B CD   1 
ATOM   2998 N  NE   . ARG   B 1 162 ? -63.623 -14.341 -8.719  0.60 29.05 ? 141 ARG   B NE   1 
ATOM   2999 C  CZ   . ARG   B 1 162 ? -64.309 -13.602 -9.586  0.60 28.26 ? 141 ARG   B CZ   1 
ATOM   3000 N  NH1  . ARG   B 1 162 ? -65.116 -12.648 -9.157  0.60 28.16 ? 141 ARG   B NH1  1 
ATOM   3001 N  NH2  . ARG   B 1 162 ? -64.158 -13.804 -10.880 0.60 31.24 ? 141 ARG   B NH2  1 
ATOM   3002 N  N    . GLN   B 1 163 ? -58.734 -16.268 -5.826  1.00 30.48 ? 142 GLN   B N    1 
ATOM   3003 C  CA   . GLN   B 1 163 ? -57.485 -16.801 -6.338  1.00 34.64 ? 142 GLN   B CA   1 
ATOM   3004 C  C    . GLN   B 1 163 ? -57.741 -18.179 -6.954  1.00 42.15 ? 142 GLN   B C    1 
ATOM   3005 O  O    . GLN   B 1 163 ? -58.351 -19.044 -6.326  1.00 42.92 ? 142 GLN   B O    1 
ATOM   3006 C  CB   . GLN   B 1 163 ? -56.339 -16.649 -5.332  1.00 30.11 ? 142 GLN   B CB   1 
ATOM   3007 C  CG   . GLN   B 1 163 ? -55.992 -15.192 -5.014  1.00 24.66 ? 142 GLN   B CG   1 
ATOM   3008 C  CD   . GLN   B 1 163 ? -55.761 -14.336 -6.246  1.00 25.70 ? 142 GLN   B CD   1 
ATOM   3009 O  OE1  . GLN   B 1 163 ? -55.134 -14.777 -7.215  1.00 23.06 ? 142 GLN   B OE1  1 
ATOM   3010 N  NE2  . GLN   B 1 163 ? -56.276 -13.108 -6.237  1.00 24.85 ? 142 GLN   B NE2  1 
ATOM   3011 N  N    . LYS   B 1 164 ? -57.308 -18.339 -8.212  0.70 41.15 ? 143 LYS   B N    1 
ATOM   3012 C  CA   . LYS   B 1 164 ? -57.499 -19.560 -8.977  0.70 42.99 ? 143 LYS   B CA   1 
ATOM   3013 C  C    . LYS   B 1 164 ? -56.132 -20.223 -9.212  0.70 44.57 ? 143 LYS   B C    1 
ATOM   3014 O  O    . LYS   B 1 164 ? -56.077 -21.463 -9.072  0.70 48.18 ? 143 LYS   B O    1 
ATOM   3015 C  CB   . LYS   B 1 164 ? -58.188 -19.258 -10.313 0.70 40.57 ? 143 LYS   B CB   1 
ATOM   3016 N  N    . SER   B 1 173 ? -46.018 -16.547 -9.897  1.00 44.38 ? 152 SER   B N    1 
ATOM   3017 C  CA   . SER   B 1 173 ? -47.047 -15.988 -8.978  1.00 40.89 ? 152 SER   B CA   1 
ATOM   3018 C  C    . SER   B 1 173 ? -46.377 -15.084 -7.947  1.00 34.40 ? 152 SER   B C    1 
ATOM   3019 O  O    . SER   B 1 173 ? -45.481 -15.515 -7.225  1.00 38.83 ? 152 SER   B O    1 
ATOM   3020 C  CB   . SER   B 1 173 ? -47.827 -17.091 -8.302  1.00 43.60 ? 152 SER   B CB   1 
ATOM   3021 N  N    . ASN   B 1 174 ? -46.796 -13.813 -7.916  1.00 28.60 ? 153 ASN   B N    1 
ATOM   3022 C  CA   . ASN   B 1 174 ? -46.337 -12.901 -6.885  1.00 24.26 ? 153 ASN   B CA   1 
ATOM   3023 C  C    . ASN   B 1 174 ? -47.545 -12.091 -6.431  1.00 19.91 ? 153 ASN   B C    1 
ATOM   3024 O  O    . ASN   B 1 174 ? -47.751 -10.981 -6.913  1.00 20.63 ? 153 ASN   B O    1 
ATOM   3025 C  CB   . ASN   B 1 174 ? -45.245 -11.982 -7.429  1.00 25.70 ? 153 ASN   B CB   1 
ATOM   3026 C  CG   . ASN   B 1 174 ? -44.658 -11.033 -6.411  1.00 28.04 ? 153 ASN   B CG   1 
ATOM   3027 O  OD1  . ASN   B 1 174 ? -44.941 -11.120 -5.210  1.00 27.15 ? 153 ASN   B OD1  1 
ATOM   3028 N  ND2  . ASN   B 1 174 ? -43.823 -10.116 -6.879  1.00 34.50 ? 153 ASN   B ND2  1 
ATOM   3029 N  N    . LEU   B 1 175 ? -48.377 -12.682 -5.565  1.00 16.68 ? 154 LEU   B N    1 
ATOM   3030 C  CA   . LEU   B 1 175 ? -49.625 -12.053 -5.157  1.00 15.19 ? 154 LEU   B CA   1 
ATOM   3031 C  C    . LEU   B 1 175 ? -49.380 -11.198 -3.922  1.00 16.50 ? 154 LEU   B C    1 
ATOM   3032 O  O    . LEU   B 1 175 ? -48.729 -11.639 -2.967  1.00 16.79 ? 154 LEU   B O    1 
ATOM   3033 C  CB   . LEU   B 1 175 ? -50.645 -13.134 -4.805  1.00 16.97 ? 154 LEU   B CB   1 
ATOM   3034 C  CG   . LEU   B 1 175 ? -50.919 -14.182 -5.892  1.00 18.73 ? 154 LEU   B CG   1 
ATOM   3035 C  CD1  . LEU   B 1 175 ? -51.796 -15.284 -5.328  1.00 21.33 ? 154 LEU   B CD1  1 
ATOM   3036 C  CD2  . LEU   B 1 175 ? -51.613 -13.517 -7.077  1.00 19.16 ? 154 LEU   B CD2  1 
ATOM   3037 N  N    . SER   B 1 176 ? -49.905 -9.966  -3.934  1.00 15.60 ? 155 SER   B N    1 
ATOM   3038 C  CA   . SER   B 1 176 ? -49.822 -9.183  -2.709  1.00 16.82 ? 155 SER   B CA   1 
ATOM   3039 C  C    . SER   B 1 176 ? -50.885 -8.090  -2.607  1.00 15.60 ? 155 SER   B C    1 
ATOM   3040 O  O    . SER   B 1 176 ? -51.555 -7.733  -3.575  1.00 16.32 ? 155 SER   B O    1 
ATOM   3041 C  CB   . SER   B 1 176 ? -48.427 -8.695  -2.433  1.00 22.40 ? 155 SER   B CB   1 
ATOM   3042 O  OG   . SER   B 1 176 ? -48.150 -7.528  -3.186  1.00 21.18 ? 155 SER   B OG   1 
ATOM   3043 N  N    . ILE   B 1 177 ? -51.072 -7.642  -1.363  1.00 14.75 ? 156 ILE   B N    1 
ATOM   3044 C  CA   . ILE   B 1 177 ? -51.973 -6.573  -0.999  1.00 14.40 ? 156 ILE   B CA   1 
ATOM   3045 C  C    . ILE   B 1 177 ? -51.116 -5.500  -0.335  1.00 13.88 ? 156 ILE   B C    1 
ATOM   3046 O  O    . ILE   B 1 177 ? -50.223 -5.811  0.448   1.00 13.92 ? 156 ILE   B O    1 
ATOM   3047 C  CB   . ILE   B 1 177 ? -53.065 -7.110  -0.060  1.00 14.51 ? 156 ILE   B CB   1 
ATOM   3048 C  CG1  . ILE   B 1 177 ? -53.813 -8.291  -0.717  1.00 16.57 ? 156 ILE   B CG1  1 
ATOM   3049 C  CG2  . ILE   B 1 177 ? -53.996 -5.992  0.411   1.00 15.38 ? 156 ILE   B CG2  1 
ATOM   3050 C  CD1  . ILE   B 1 177 ? -54.925 -8.886  0.130   1.00 17.68 ? 156 ILE   B CD1  1 
ATOM   3051 N  N    . VAL   B 1 178 ? -51.375 -4.236  -0.693  1.00 13.28 ? 157 VAL   B N    1 
ATOM   3052 C  CA   . VAL   B 1 178 ? -50.748 -3.105  -0.018  1.00 13.91 ? 157 VAL   B CA   1 
ATOM   3053 C  C    . VAL   B 1 178 ? -51.842 -2.177  0.489   1.00 13.87 ? 157 VAL   B C    1 
ATOM   3054 O  O    . VAL   B 1 178 ? -52.672 -1.700  -0.287  1.00 14.12 ? 157 VAL   B O    1 
ATOM   3055 C  CB   . VAL   B 1 178 ? -49.794 -2.309  -0.928  1.00 13.84 ? 157 VAL   B CB   1 
ATOM   3056 C  CG1  . VAL   B 1 178 ? -49.152 -1.143  -0.169  1.00 14.34 ? 157 VAL   B CG1  1 
ATOM   3057 C  CG2  . VAL   B 1 178 ? -48.717 -3.209  -1.539  1.00 15.52 ? 157 VAL   B CG2  1 
ATOM   3058 N  N    . ASN   B 1 179 ? -51.771 -1.871  1.786   1.00 13.10 ? 158 ASN   B N    1 
ATOM   3059 C  CA   . ASN   B 1 179 ? -52.746 -1.017  2.440   1.00 12.92 ? 158 ASN   B CA   1 
ATOM   3060 C  C    . ASN   B 1 179 ? -52.104 0.342   2.705   1.00 13.23 ? 158 ASN   B C    1 
ATOM   3061 O  O    . ASN   B 1 179 ? -50.992 0.390   3.235   1.00 12.71 ? 158 ASN   B O    1 
ATOM   3062 C  CB   . ASN   B 1 179 ? -53.206 -1.670  3.743   1.00 13.36 ? 158 ASN   B CB   1 
ATOM   3063 C  CG   . ASN   B 1 179 ? -53.998 -2.929  3.482   1.00 14.56 ? 158 ASN   B CG   1 
ATOM   3064 O  OD1  . ASN   B 1 179 ? -54.673 -3.025  2.446   1.00 14.80 ? 158 ASN   B OD1  1 
ATOM   3065 N  ND2  . ASN   B 1 179 ? -53.914 -3.902  4.381   1.00 15.22 ? 158 ASN   B ND2  1 
ATOM   3066 N  N    . LEU   B 1 180 ? -52.796 1.433   2.329   1.00 12.83 ? 159 LEU   B N    1 
ATOM   3067 C  CA   . LEU   B 1 180 ? -52.283 2.773   2.596   1.00 14.16 ? 159 LEU   B CA   1 
ATOM   3068 C  C    . LEU   B 1 180 ? -52.698 3.174   4.004   1.00 14.61 ? 159 LEU   B C    1 
ATOM   3069 O  O    . LEU   B 1 180 ? -53.878 3.396   4.282   1.00 15.39 ? 159 LEU   B O    1 
ATOM   3070 C  CB   . LEU   B 1 180 ? -52.818 3.784   1.581   1.00 14.50 ? 159 LEU   B CB   1 
ATOM   3071 C  CG   . LEU   B 1 180 ? -51.991 3.923   0.301   1.00 15.21 ? 159 LEU   B CG   1 
ATOM   3072 C  CD1  . LEU   B 1 180 ? -50.692 4.678   0.572   1.00 15.95 ? 159 LEU   B CD1  1 
ATOM   3073 C  CD2  . LEU   B 1 180 ? -51.685 2.565   -0.325  1.00 16.51 ? 159 LEU   B CD2  1 
ATOM   3074 N  N    . CYS   B 1 181 ? -51.690 3.171   4.890   1.00 14.34 ? 160 CYS   B N    1 
ATOM   3075 C  CA   . CYS   B 1 181 ? -51.797 3.452   6.310   1.00 15.62 ? 160 CYS   B CA   1 
ATOM   3076 C  C    . CYS   B 1 181 ? -51.475 4.929   6.545   1.00 15.86 ? 160 CYS   B C    1 
ATOM   3077 O  O    . CYS   B 1 181 ? -51.709 5.751   5.667   1.00 18.63 ? 160 CYS   B O    1 
ATOM   3078 C  CB   . CYS   B 1 181 ? -50.912 2.477   7.071   1.00 15.96 ? 160 CYS   B CB   1 
ATOM   3079 S  SG   . CYS   B 1 181 ? -51.440 0.753   6.844   1.00 18.97 ? 160 CYS   B SG   1 
ATOM   3080 N  N    . ASP   B 1 182 ? -51.089 5.281   7.773   1.00 15.51 ? 161 ASP   B N    1 
ATOM   3081 C  CA   . ASP   B 1 182 ? -50.840 6.674   8.107   1.00 15.33 ? 161 ASP   B CA   1 
ATOM   3082 C  C    . ASP   B 1 182 ? -49.743 6.689   9.165   1.00 14.87 ? 161 ASP   B C    1 
ATOM   3083 O  O    . ASP   B 1 182 ? -49.890 6.069   10.225  1.00 16.03 ? 161 ASP   B O    1 
ATOM   3084 C  CB   . ASP   B 1 182 ? -52.126 7.352   8.576   1.00 16.43 ? 161 ASP   B CB   1 
ATOM   3085 C  CG   . ASP   B 1 182 ? -51.993 8.844   8.844   1.00 20.09 ? 161 ASP   B CG   1 
ATOM   3086 O  OD1  . ASP   B 1 182 ? -50.929 9.234   9.334   1.00 19.04 ? 161 ASP   B OD1  1 
ATOM   3087 O  OD2  . ASP   B 1 182 ? -52.959 9.602   8.579   1.00 21.32 ? 161 ASP   B OD2  1 
ATOM   3088 N  N    . ALA   B 1 183 ? -48.608 7.336   8.861   1.00 13.29 ? 162 ALA   B N    1 
ATOM   3089 C  CA   . ALA   B 1 183 ? -47.488 7.318   9.796   1.00 13.66 ? 162 ALA   B CA   1 
ATOM   3090 C  C    . ALA   B 1 183 ? -47.793 8.038   11.107  1.00 15.14 ? 162 ALA   B C    1 
ATOM   3091 O  O    . ALA   B 1 183 ? -47.038 7.862   12.066  1.00 15.86 ? 162 ALA   B O    1 
ATOM   3092 C  CB   . ALA   B 1 183 ? -46.245 7.931   9.160   1.00 14.59 ? 162 ALA   B CB   1 
ATOM   3093 N  N    . MET   B 1 184 ? -48.848 8.872   11.139  1.00 14.94 ? 163 MET   B N    1 
ATOM   3094 C  CA   . MET   B 1 184 ? -49.071 9.708   12.313  1.00 16.77 ? 163 MET   B CA   1 
ATOM   3095 C  C    . MET   B 1 184 ? -50.213 9.213   13.199  1.00 17.36 ? 163 MET   B C    1 
ATOM   3096 O  O    . MET   B 1 184 ? -50.712 9.971   14.027  1.00 20.00 ? 163 MET   B O    1 
ATOM   3097 C  CB   . MET   B 1 184 ? -49.334 11.149  11.868  1.00 18.12 ? 163 MET   B CB   1 
ATOM   3098 C  CG   . MET   B 1 184 ? -48.186 11.751  11.087  1.00 21.46 ? 163 MET   B CG   1 
ATOM   3099 S  SD   . MET   B 1 184 ? -46.753 12.011  12.148  1.00 24.06 ? 163 MET   B SD   1 
ATOM   3100 C  CE   . MET   B 1 184 ? -47.285 13.527  12.956  1.00 27.12 ? 163 MET   B CE   1 
ATOM   3101 N  N    . VAL   B 1 185 ? -50.582 7.943   13.065  1.00 19.31 ? 164 VAL   B N    1 
ATOM   3102 C  CA   . VAL   B 1 185 ? -51.759 7.466   13.773  1.00 21.88 ? 164 VAL   B CA   1 
ATOM   3103 C  C    . VAL   B 1 185 ? -51.511 7.340   15.278  1.00 20.55 ? 164 VAL   B C    1 
ATOM   3104 O  O    . VAL   B 1 185 ? -52.479 7.225   16.026  1.00 20.26 ? 164 VAL   B O    1 
ATOM   3105 C  CB   . VAL   B 1 185 ? -52.284 6.143   13.210  1.00 23.79 ? 164 VAL   B CB   1 
ATOM   3106 C  CG1  . VAL   B 1 185 ? -52.891 6.360   11.827  1.00 25.93 ? 164 VAL   B CG1  1 
ATOM   3107 C  CG2  . VAL   B 1 185 ? -51.210 5.062   13.263  1.00 22.93 ? 164 VAL   B CG2  1 
ATOM   3108 N  N    . ASP   B 1 186 ? -50.244 7.388   15.728  1.00 18.92 ? 165 ASP   B N    1 
ATOM   3109 C  CA   . ASP   B 1 186 ? -49.975 7.451   17.164  1.00 18.46 ? 165 ASP   B CA   1 
ATOM   3110 C  C    . ASP   B 1 186 ? -49.807 8.871   17.700  1.00 18.37 ? 165 ASP   B C    1 
ATOM   3111 O  O    . ASP   B 1 186 ? -49.608 9.039   18.909  1.00 18.43 ? 165 ASP   B O    1 
ATOM   3112 C  CB   . ASP   B 1 186 ? -48.834 6.536   17.557  1.00 19.42 ? 165 ASP   B CB   1 
ATOM   3113 C  CG   . ASP   B 1 186 ? -49.113 5.073   17.274  1.00 21.18 ? 165 ASP   B CG   1 
ATOM   3114 O  OD1  . ASP   B 1 186 ? -50.238 4.618   17.554  1.00 21.32 ? 165 ASP   B OD1  1 
ATOM   3115 O  OD2  . ASP   B 1 186 ? -48.176 4.402   16.802  1.00 26.79 ? 165 ASP   B OD2  1 
ATOM   3116 N  N    . GLN   B 1 187 ? -49.897 9.879   16.827  1.00 17.30 ? 166 GLN   B N    1 
ATOM   3117 C  CA   . GLN   B 1 187 ? -49.806 11.282  17.189  1.00 18.17 ? 166 GLN   B CA   1 
ATOM   3118 C  C    . GLN   B 1 187 ? -50.853 12.000  16.342  1.00 18.71 ? 166 GLN   B C    1 
ATOM   3119 O  O    . GLN   B 1 187 ? -50.527 12.827  15.487  1.00 20.01 ? 166 GLN   B O    1 
ATOM   3120 C  CB   . GLN   B 1 187 ? -48.424 11.887  16.920  1.00 21.51 ? 166 GLN   B CB   1 
ATOM   3121 C  CG   . GLN   B 1 187 ? -47.276 11.204  17.658  1.00 25.80 ? 166 GLN   B CG   1 
ATOM   3122 C  CD   . GLN   B 1 187 ? -46.152 10.781  16.732  1.00 29.73 ? 166 GLN   B CD   1 
ATOM   3123 O  OE1  . GLN   B 1 187 ? -46.184 9.691   16.151  1.00 28.81 ? 166 GLN   B OE1  1 
ATOM   3124 N  NE2  . GLN   B 1 187 ? -45.124 11.613  16.603  1.00 28.53 ? 166 GLN   B NE2  1 
ATOM   3125 N  N    . PRO   B 1 188 ? -52.143 11.666  16.550  1.00 19.45 ? 167 PRO   B N    1 
ATOM   3126 C  CA   . PRO   B 1 188 ? -53.191 12.018  15.591  1.00 18.86 ? 167 PRO   B CA   1 
ATOM   3127 C  C    . PRO   B 1 188 ? -53.570 13.492  15.619  1.00 18.24 ? 167 PRO   B C    1 
ATOM   3128 O  O    . PRO   B 1 188 ? -53.371 14.181  16.624  1.00 20.43 ? 167 PRO   B O    1 
ATOM   3129 C  CB   . PRO   B 1 188 ? -54.350 11.143  16.088  1.00 20.74 ? 167 PRO   B CB   1 
ATOM   3130 C  CG   . PRO   B 1 188 ? -54.129 11.060  17.576  1.00 18.27 ? 167 PRO   B CG   1 
ATOM   3131 C  CD   . PRO   B 1 188 ? -52.628 10.827  17.656  1.00 19.72 ? 167 PRO   B CD   1 
ATOM   3132 N  N    . CYS   B 1 189 ? -54.154 13.931  14.503  1.00 19.41 ? 168 CYS   B N    1 
ATOM   3133 C  CA   . CYS   B 1 189 ? -54.736 15.265  14.483  1.00 20.63 ? 168 CYS   B CA   1 
ATOM   3134 C  C    . CYS   B 1 189 ? -55.918 15.301  15.445  1.00 19.35 ? 168 CYS   B C    1 
ATOM   3135 O  O    . CYS   B 1 189 ? -56.685 14.341  15.586  1.00 19.54 ? 168 CYS   B O    1 
ATOM   3136 C  CB   . CYS   B 1 189 ? -55.159 15.670  13.080  1.00 23.91 ? 168 CYS   B CB   1 
ATOM   3137 S  SG   . CYS   B 1 189 ? -53.740 16.011  12.004  1.00 31.66 ? 168 CYS   B SG   1 
ATOM   3138 N  N    . MET   B 1 190 ? -56.055 16.461  16.088  1.00 20.43 ? 169 MET   B N    1 
ATOM   3139 C  CA   . MET   B 1 190 ? -57.131 16.727  17.018  1.00 20.41 ? 169 MET   B CA   1 
ATOM   3140 C  C    . MET   B 1 190 ? -58.460 16.573  16.283  1.00 18.63 ? 169 MET   B C    1 
ATOM   3141 O  O    . MET   B 1 190 ? -58.632 17.125  15.196  1.00 20.40 ? 169 MET   B O    1 
ATOM   3142 C  CB   . MET   B 1 190 ? -57.013 18.191  17.472  1.00 23.79 ? 169 MET   B CB   1 
ATOM   3143 C  CG   . MET   B 1 190 ? -58.131 18.645  18.375  1.00 28.06 ? 169 MET   B CG   1 
ATOM   3144 S  SD   . MET   B 1 190 ? -58.046 17.679  19.895  1.00 31.06 ? 169 MET   B SD   1 
ATOM   3145 C  CE   . MET   B 1 190 ? -56.587 18.384  20.673  1.00 29.76 ? 169 MET   B CE   1 
ATOM   3146 N  N    . ALA   B 1 191 ? -59.381 15.812  16.898  1.00 17.88 ? 170 ALA   B N    1 
ATOM   3147 C  CA   . ALA   B 1 191 ? -60.774 15.680  16.485  1.00 17.94 ? 170 ALA   B CA   1 
ATOM   3148 C  C    . ALA   B 1 191 ? -60.946 14.746  15.288  1.00 17.39 ? 170 ALA   B C    1 
ATOM   3149 O  O    . ALA   B 1 191 ? -61.991 14.775  14.636  1.00 18.37 ? 170 ALA   B O    1 
ATOM   3150 C  CB   . ALA   B 1 191 ? -61.434 17.040  16.234  1.00 19.92 ? 170 ALA   B CB   1 
ATOM   3151 N  N    . PHE   B 1 192 ? -59.931 13.897  15.016  1.00 15.99 ? 171 PHE   B N    1 
ATOM   3152 C  CA   . PHE   B 1 192 ? -60.011 12.927  13.935  1.00 15.16 ? 171 PHE   B CA   1 
ATOM   3153 C  C    . PHE   B 1 192 ? -60.150 11.508  14.492  1.00 15.15 ? 171 PHE   B C    1 
ATOM   3154 O  O    . PHE   B 1 192 ? -59.545 10.595  13.936  1.00 15.00 ? 171 PHE   B O    1 
ATOM   3155 C  CB   . PHE   B 1 192 ? -58.786 13.070  13.022  1.00 15.45 ? 171 PHE   B CB   1 
ATOM   3156 C  CG   . PHE   B 1 192 ? -58.845 14.215  12.023  1.00 17.50 ? 171 PHE   B CG   1 
ATOM   3157 C  CD1  . PHE   B 1 192 ? -58.605 15.532  12.416  1.00 19.88 ? 171 PHE   B CD1  1 
ATOM   3158 C  CD2  . PHE   B 1 192 ? -59.142 13.968  10.683  1.00 19.83 ? 171 PHE   B CD2  1 
ATOM   3159 C  CE1  . PHE   B 1 192 ? -58.683 16.572  11.488  1.00 20.29 ? 171 PHE   B CE1  1 
ATOM   3160 C  CE2  . PHE   B 1 192 ? -59.187 15.009  9.756   1.00 22.03 ? 171 PHE   B CE2  1 
ATOM   3161 C  CZ   . PHE   B 1 192 ? -58.965 16.307  10.166  1.00 21.73 ? 171 PHE   B CZ   1 
ATOM   3162 N  N    . SER   B 1 193 ? -61.016 11.292  15.497  1.00 13.96 ? 172 SER   B N    1 
ATOM   3163 C  CA   A SER   B 1 193 ? -61.054 9.981   16.138  0.60 15.36 ? 172 SER   B CA   1 
ATOM   3164 C  CA   B SER   B 1 193 ? -61.111 9.988   16.154  0.40 14.60 ? 172 SER   B CA   1 
ATOM   3165 C  C    . SER   B 1 193 ? -61.494 8.883   15.170  1.00 15.51 ? 172 SER   B C    1 
ATOM   3166 O  O    . SER   B 1 193 ? -60.880 7.814   15.136  1.00 14.53 ? 172 SER   B O    1 
ATOM   3167 C  CB   A SER   B 1 193 ? -61.894 9.971   17.385  0.60 17.69 ? 172 SER   B CB   1 
ATOM   3168 C  CB   B SER   B 1 193 ? -62.064 9.983   17.338  0.40 15.08 ? 172 SER   B CB   1 
ATOM   3169 O  OG   A SER   B 1 193 ? -63.180 10.475  17.065  0.60 19.66 ? 172 SER   B OG   1 
ATOM   3170 O  OG   B SER   B 1 193 ? -61.542 10.689  18.454  0.40 14.53 ? 172 SER   B OG   1 
ATOM   3171 N  N    . LEU   B 1 194 ? -62.567 9.097   14.402  1.00 14.57 ? 173 LEU   B N    1 
ATOM   3172 C  CA   . LEU   B 1 194 ? -63.050 8.028   13.528  1.00 13.99 ? 173 LEU   B CA   1 
ATOM   3173 C  C    . LEU   B 1 194 ? -62.031 7.687   12.441  1.00 14.17 ? 173 LEU   B C    1 
ATOM   3174 O  O    . LEU   B 1 194 ? -61.806 6.513   12.140  1.00 13.89 ? 173 LEU   B O    1 
ATOM   3175 C  CB   . LEU   B 1 194 ? -64.438 8.342   12.961  1.00 14.33 ? 173 LEU   B CB   1 
ATOM   3176 C  CG   . LEU   B 1 194 ? -65.583 8.061   13.932  1.00 15.41 ? 173 LEU   B CG   1 
ATOM   3177 C  CD1  . LEU   B 1 194 ? -66.840 8.667   13.315  1.00 17.18 ? 173 LEU   B CD1  1 
ATOM   3178 C  CD2  . LEU   B 1 194 ? -65.746 6.555   14.150  1.00 15.46 ? 173 LEU   B CD2  1 
ATOM   3179 N  N    . TYR   B 1 195 ? -61.385 8.704   11.852  1.00 13.41 ? 174 TYR   B N    1 
ATOM   3180 C  CA   . TYR   B 1 195 ? -60.350 8.464   10.862  1.00 13.90 ? 174 TYR   B CA   1 
ATOM   3181 C  C    . TYR   B 1 195 ? -59.219 7.642   11.484  1.00 13.75 ? 174 TYR   B C    1 
ATOM   3182 O  O    . TYR   B 1 195 ? -58.776 6.659   10.911  1.00 13.54 ? 174 TYR   B O    1 
ATOM   3183 C  CB   . TYR   B 1 195 ? -59.816 9.818   10.371  1.00 14.21 ? 174 TYR   B CB   1 
ATOM   3184 C  CG   . TYR   B 1 195 ? -58.589 9.614   9.497   1.00 14.83 ? 174 TYR   B CG   1 
ATOM   3185 C  CD1  . TYR   B 1 195 ? -58.694 9.170   8.173   1.00 14.98 ? 174 TYR   B CD1  1 
ATOM   3186 C  CD2  . TYR   B 1 195 ? -57.325 9.810   10.034  1.00 15.14 ? 174 TYR   B CD2  1 
ATOM   3187 C  CE1  . TYR   B 1 195 ? -57.563 8.937   7.401   1.00 15.70 ? 174 TYR   B CE1  1 
ATOM   3188 C  CE2  . TYR   B 1 195 ? -56.191 9.595   9.264   1.00 15.99 ? 174 TYR   B CE2  1 
ATOM   3189 C  CZ   . TYR   B 1 195 ? -56.310 9.163   7.952   1.00 15.95 ? 174 TYR   B CZ   1 
ATOM   3190 O  OH   . TYR   B 1 195 ? -55.155 8.957   7.247   1.00 17.73 ? 174 TYR   B OH   1 
ATOM   3191 N  N    . ASN   B 1 196 ? -58.780 8.011   12.688  1.00 13.74 ? 175 ASN   B N    1 
ATOM   3192 C  CA   A ASN   B 1 196 ? -57.672 7.346   13.361  0.50 14.09 ? 175 ASN   B CA   1 
ATOM   3193 C  CA   B ASN   B 1 196 ? -57.669 7.329   13.329  0.50 13.90 ? 175 ASN   B CA   1 
ATOM   3194 C  C    . ASN   B 1 196 ? -58.066 5.904   13.693  1.00 13.23 ? 175 ASN   B C    1 
ATOM   3195 O  O    . ASN   B 1 196 ? -57.259 4.983   13.546  1.00 14.88 ? 175 ASN   B O    1 
ATOM   3196 C  CB   A ASN   B 1 196 ? -57.247 8.151   14.584  0.50 15.90 ? 175 ASN   B CB   1 
ATOM   3197 C  CB   B ASN   B 1 196 ? -57.148 8.153   14.493  0.50 15.28 ? 175 ASN   B CB   1 
ATOM   3198 C  CG   A ASN   B 1 196 ? -55.948 7.667   15.182  0.50 17.38 ? 175 ASN   B CG   1 
ATOM   3199 C  CG   B ASN   B 1 196 ? -56.218 9.214   13.971  0.50 16.71 ? 175 ASN   B CG   1 
ATOM   3200 O  OD1  A ASN   B 1 196 ? -55.880 7.393   16.387  0.50 20.48 ? 175 ASN   B OD1  1 
ATOM   3201 O  OD1  B ASN   B 1 196 ? -55.069 8.896   13.637  0.50 18.39 ? 175 ASN   B OD1  1 
ATOM   3202 N  ND2  A ASN   B 1 196 ? -54.910 7.584   14.367  0.50 17.02 ? 175 ASN   B ND2  1 
ATOM   3203 N  ND2  B ASN   B 1 196 ? -56.689 10.453  13.898  0.50 15.18 ? 175 ASN   B ND2  1 
ATOM   3204 N  N    . MET   B 1 197 ? -59.307 5.723   14.137  1.00 13.40 ? 176 MET   B N    1 
ATOM   3205 C  CA   . MET   B 1 197 ? -59.776 4.369   14.415  1.00 13.33 ? 176 MET   B CA   1 
ATOM   3206 C  C    . MET   B 1 197 ? -59.701 3.517   13.162  1.00 13.83 ? 176 MET   B C    1 
ATOM   3207 O  O    . MET   B 1 197 ? -59.298 2.353   13.225  1.00 13.61 ? 176 MET   B O    1 
ATOM   3208 C  CB   . MET   B 1 197 ? -61.234 4.390   14.880  1.00 12.87 ? 176 MET   B CB   1 
ATOM   3209 C  CG   . MET   B 1 197 ? -61.337 4.924   16.294  1.00 14.40 ? 176 MET   B CG   1 
ATOM   3210 S  SD   . MET   B 1 197 ? -63.026 5.319   16.803  1.00 15.42 ? 176 MET   B SD   1 
ATOM   3211 C  CE   . MET   B 1 197 ? -63.720 3.659   16.841  1.00 17.12 ? 176 MET   B CE   1 
ATOM   3212 N  N    . GLY   B 1 198 ? -60.136 4.080   12.026  1.00 13.20 ? 177 GLY   B N    1 
ATOM   3213 C  CA   . GLY   B 1 198 ? -60.106 3.379   10.751  1.00 13.21 ? 177 GLY   B CA   1 
ATOM   3214 C  C    . GLY   B 1 198 ? -58.694 2.970   10.348  1.00 13.06 ? 177 GLY   B C    1 
ATOM   3215 O  O    . GLY   B 1 198 ? -58.463 1.820   9.976   1.00 13.05 ? 177 GLY   B O    1 
ATOM   3216 N  N    . LYS   B 1 199 ? -57.740 3.902   10.468  1.00 12.92 ? 178 LYS   B N    1 
ATOM   3217 C  CA   . LYS   B 1 199 ? -56.364 3.613   10.092  1.00 13.39 ? 178 LYS   B CA   1 
ATOM   3218 C  C    . LYS   B 1 199 ? -55.733 2.594   11.046  1.00 12.94 ? 178 LYS   B C    1 
ATOM   3219 O  O    . LYS   B 1 199 ? -54.980 1.740   10.589  1.00 13.62 ? 178 LYS   B O    1 
ATOM   3220 C  CB   . LYS   B 1 199 ? -55.529 4.895   9.925   1.00 13.65 ? 178 LYS   B CB   1 
ATOM   3221 C  CG   . LYS   B 1 199 ? -55.959 5.718   8.727   1.00 15.83 ? 178 LYS   B CG   1 
ATOM   3222 C  CD   . LYS   B 1 199 ? -55.837 4.984   7.403   1.00 15.79 ? 178 LYS   B CD   1 
ATOM   3223 C  CE   . LYS   B 1 199 ? -55.861 5.896   6.186   1.00 18.30 ? 178 LYS   B CE   1 
ATOM   3224 N  NZ   . LYS   B 1 199 ? -55.922 5.197   4.904   1.00 19.48 ? 178 LYS   B NZ   1 
ATOM   3225 N  N    . HIS   B 1 200 ? -56.034 2.677   12.354  1.00 13.32 ? 179 HIS   B N    1 
ATOM   3226 C  CA   . HIS   B 1 200 ? -55.518 1.650   13.247  1.00 12.75 ? 179 HIS   B CA   1 
ATOM   3227 C  C    . HIS   B 1 200 ? -56.141 0.306   12.886  1.00 13.95 ? 179 HIS   B C    1 
ATOM   3228 O  O    . HIS   B 1 200 ? -55.420 -0.695  12.891  1.00 13.04 ? 179 HIS   B O    1 
ATOM   3229 C  CB   . HIS   B 1 200 ? -55.834 1.969   14.719  1.00 14.88 ? 179 HIS   B CB   1 
ATOM   3230 C  CG   . HIS   B 1 200 ? -54.842 2.846   15.388  1.00 16.28 ? 179 HIS   B CG   1 
ATOM   3231 N  ND1  . HIS   B 1 200 ? -53.773 2.345   16.101  1.00 19.57 ? 179 HIS   B ND1  1 
ATOM   3232 C  CD2  . HIS   B 1 200 ? -54.755 4.190   15.448  1.00 18.42 ? 179 HIS   B CD2  1 
ATOM   3233 C  CE1  . HIS   B 1 200 ? -53.070 3.367   16.588  1.00 17.91 ? 179 HIS   B CE1  1 
ATOM   3234 N  NE2  . HIS   B 1 200 ? -53.655 4.484   16.210  1.00 18.20 ? 179 HIS   B NE2  1 
ATOM   3235 N  N    . ALA   B 1 201 ? -57.457 0.268   12.590  1.00 13.14 ? 180 ALA   B N    1 
ATOM   3236 C  CA   . ALA   B 1 201 ? -58.029 -1.022  12.197  1.00 13.97 ? 180 ALA   B CA   1 
ATOM   3237 C  C    . ALA   B 1 201 ? -57.309 -1.572  10.964  1.00 13.91 ? 180 ALA   B C    1 
ATOM   3238 O  O    . ALA   B 1 201 ? -57.129 -2.787  10.807  1.00 13.21 ? 180 ALA   B O    1 
ATOM   3239 C  CB   . ALA   B 1 201 ? -59.523 -0.899  11.926  1.00 14.07 ? 180 ALA   B CB   1 
ATOM   3240 N  N    . LEU   B 1 202 ? -56.903 -0.687  10.055  1.00 13.34 ? 181 LEU   B N    1 
ATOM   3241 C  CA   . LEU   B 1 202 ? -56.232 -1.122  8.839   1.00 13.65 ? 181 LEU   B CA   1 
ATOM   3242 C  C    . LEU   B 1 202 ? -54.862 -1.747  9.141   1.00 13.27 ? 181 LEU   B C    1 
ATOM   3243 O  O    . LEU   B 1 202 ? -54.456 -2.702  8.480   1.00 14.09 ? 181 LEU   B O    1 
ATOM   3244 C  CB   . LEU   B 1 202 ? -56.115 0.091   7.914   1.00 14.90 ? 181 LEU   B CB   1 
ATOM   3245 C  CG   . LEU   B 1 202 ? -55.598 -0.232  6.508   1.00 15.27 ? 181 LEU   B CG   1 
ATOM   3246 C  CD1  . LEU   B 1 202 ? -56.490 -1.242  5.785   1.00 16.25 ? 181 LEU   B CD1  1 
ATOM   3247 C  CD2  . LEU   B 1 202 ? -55.506 1.072   5.717   1.00 18.13 ? 181 LEU   B CD2  1 
ATOM   3248 N  N    . VAL   B 1 203 ? -54.164 -1.266  10.180  1.00 13.40 ? 182 VAL   B N    1 
ATOM   3249 C  CA   . VAL   B 1 203 ? -52.944 -1.918  10.647  1.00 13.94 ? 182 VAL   B CA   1 
ATOM   3250 C  C    . VAL   B 1 203 ? -53.275 -3.339  11.095  1.00 13.20 ? 182 VAL   B C    1 
ATOM   3251 O  O    . VAL   B 1 203 ? -52.546 -4.276  10.759  1.00 14.67 ? 182 VAL   B O    1 
ATOM   3252 C  CB   . VAL   B 1 203 ? -52.250 -1.120  11.763  1.00 14.42 ? 182 VAL   B CB   1 
ATOM   3253 C  CG1  . VAL   B 1 203 ? -51.047 -1.868  12.341  1.00 15.85 ? 182 VAL   B CG1  1 
ATOM   3254 C  CG2  . VAL   B 1 203 ? -51.816 0.236   11.227  1.00 16.87 ? 182 VAL   B CG2  1 
ATOM   3255 N  N    . GLY   B 1 204 ? -54.354 -3.466  11.881  1.00 13.70 ? 183 GLY   B N    1 
ATOM   3256 C  CA   . GLY   B 1 204 ? -54.788 -4.761  12.374  1.00 14.13 ? 183 GLY   B CA   1 
ATOM   3257 C  C    . GLY   B 1 204 ? -55.056 -5.697  11.213  1.00 14.74 ? 183 GLY   B C    1 
ATOM   3258 O  O    . GLY   B 1 204 ? -54.688 -6.874  11.249  1.00 15.28 ? 183 GLY   B O    1 
ATOM   3259 N  N    . LEU   B 1 205 ? -55.749 -5.191  10.187  1.00 13.54 ? 184 LEU   B N    1 
ATOM   3260 C  CA   . LEU   B 1 205 ? -56.050 -6.025  9.036   1.00 12.96 ? 184 LEU   B CA   1 
ATOM   3261 C  C    . LEU   B 1 205 ? -54.766 -6.445  8.323   1.00 13.49 ? 184 LEU   B C    1 
ATOM   3262 O  O    . LEU   B 1 205 ? -54.620 -7.605  7.938   1.00 13.78 ? 184 LEU   B O    1 
ATOM   3263 C  CB   . LEU   B 1 205 ? -56.956 -5.263  8.072   1.00 13.40 ? 184 LEU   B CB   1 
ATOM   3264 C  CG   . LEU   B 1 205 ? -57.206 -5.982  6.744   1.00 14.81 ? 184 LEU   B CG   1 
ATOM   3265 C  CD1  . LEU   B 1 205 ? -57.900 -7.340  6.905   1.00 15.49 ? 184 LEU   B CD1  1 
ATOM   3266 C  CD2  . LEU   B 1 205 ? -58.010 -5.067  5.840   1.00 15.18 ? 184 LEU   B CD2  1 
ATOM   3267 N  N    . THR   B 1 206 ? -53.816 -5.510  8.162   1.00 12.24 ? 185 THR   B N    1 
ATOM   3268 C  CA   . THR   B 1 206 ? -52.558 -5.811  7.502   1.00 12.28 ? 185 THR   B CA   1 
ATOM   3269 C  C    . THR   B 1 206 ? -51.872 -6.989  8.207   1.00 12.77 ? 185 THR   B C    1 
ATOM   3270 O  O    . THR   B 1 206 ? -51.456 -7.961  7.567   1.00 14.65 ? 185 THR   B O    1 
ATOM   3271 C  CB   . THR   B 1 206 ? -51.677 -4.565  7.474   1.00 13.56 ? 185 THR   B CB   1 
ATOM   3272 O  OG1  . THR   B 1 206 ? -52.353 -3.512  6.792   1.00 13.45 ? 185 THR   B OG1  1 
ATOM   3273 C  CG2  . THR   B 1 206 ? -50.362 -4.819  6.757   1.00 14.05 ? 185 THR   B CG2  1 
ATOM   3274 N  N    . GLN   B 1 207 ? -51.810 -6.933  9.547   1.00 13.63 ? 186 GLN   B N    1 
ATOM   3275 C  CA   . GLN   B 1 207 ? -51.156 -7.989  10.301  1.00 13.75 ? 186 GLN   B CA   1 
ATOM   3276 C  C    . GLN   B 1 207 ? -51.948 -9.281  10.242  1.00 13.83 ? 186 GLN   B C    1 
ATOM   3277 O  O    . GLN   B 1 207 ? -51.371 -10.345 10.005  1.00 13.82 ? 186 GLN   B O    1 
ATOM   3278 C  CB   . GLN   B 1 207 ? -50.975 -7.529  11.751  1.00 14.27 ? 186 GLN   B CB   1 
ATOM   3279 C  CG   . GLN   B 1 207 ? -50.025 -6.341  11.789  1.00 16.11 ? 186 GLN   B CG   1 
ATOM   3280 C  CD   . GLN   B 1 207 ? -49.758 -5.773  13.166  1.00 20.74 ? 186 GLN   B CD   1 
ATOM   3281 O  OE1  . GLN   B 1 207 ? -48.727 -5.115  13.352  1.00 27.55 ? 186 GLN   B OE1  1 
ATOM   3282 N  NE2  . GLN   B 1 207 ? -50.680 -5.965  14.096  1.00 21.04 ? 186 GLN   B NE2  1 
ATOM   3283 N  N    . SER   B 1 208 ? -53.251 -9.201  10.531  1.00 13.10 ? 187 SER   B N    1 
ATOM   3284 C  CA   . SER   B 1 208 ? -54.058 -10.415 10.575  1.00 13.42 ? 187 SER   B CA   1 
ATOM   3285 C  C    . SER   B 1 208 ? -54.086 -11.096 9.211   1.00 14.25 ? 187 SER   B C    1 
ATOM   3286 O  O    . SER   B 1 208 ? -53.990 -12.331 9.129   1.00 14.08 ? 187 SER   B O    1 
ATOM   3287 C  CB   . SER   B 1 208 ? -55.466 -10.111 11.030  1.00 14.55 ? 187 SER   B CB   1 
ATOM   3288 O  OG   . SER   B 1 208 ? -55.501 -9.858  12.428  1.00 16.32 ? 187 SER   B OG   1 
ATOM   3289 N  N    . ALA   B 1 209 ? -54.228 -10.307 8.135   1.00 13.79 ? 188 ALA   B N    1 
ATOM   3290 C  CA   . ALA   B 1 209 ? -54.299 -10.893 6.802   1.00 13.53 ? 188 ALA   B CA   1 
ATOM   3291 C  C    . ALA   B 1 209 ? -52.937 -11.446 6.373   1.00 14.58 ? 188 ALA   B C    1 
ATOM   3292 O  O    . ALA   B 1 209 ? -52.873 -12.495 5.730   1.00 15.15 ? 188 ALA   B O    1 
ATOM   3293 C  CB   . ALA   B 1 209 ? -54.886 -9.893  5.819   1.00 14.64 ? 188 ALA   B CB   1 
ATOM   3294 N  N    . ALA   B 1 210 ? -51.842 -10.782 6.763   1.00 14.01 ? 189 ALA   B N    1 
ATOM   3295 C  CA   . ALA   B 1 210 ? -50.517 -11.316 6.456   1.00 12.99 ? 189 ALA   B CA   1 
ATOM   3296 C  C    . ALA   B 1 210 ? -50.387 -12.712 7.048   1.00 14.31 ? 189 ALA   B C    1 
ATOM   3297 O  O    . ALA   B 1 210 ? -49.959 -13.631 6.356   1.00 14.87 ? 189 ALA   B O    1 
ATOM   3298 C  CB   . ALA   B 1 210 ? -49.435 -10.388 6.991   1.00 13.52 ? 189 ALA   B CB   1 
ATOM   3299 N  N    . LEU   B 1 211 ? -50.805 -12.882 8.306   1.00 14.48 ? 190 LEU   B N    1 
ATOM   3300 C  CA   . LEU   B 1 211 ? -50.647 -14.187 8.937   1.00 15.66 ? 190 LEU   B CA   1 
ATOM   3301 C  C    . LEU   B 1 211 ? -51.515 -15.236 8.239   1.00 15.77 ? 190 LEU   B C    1 
ATOM   3302 O  O    . LEU   B 1 211 ? -51.063 -16.355 7.976   1.00 16.98 ? 190 LEU   B O    1 
ATOM   3303 C  CB   . LEU   B 1 211 ? -51.054 -14.021 10.406  1.00 17.12 ? 190 LEU   B CB   1 
ATOM   3304 C  CG   . LEU   B 1 211 ? -51.041 -15.287 11.274  1.00 19.89 ? 190 LEU   B CG   1 
ATOM   3305 C  CD1  . LEU   B 1 211 ? -49.596 -15.614 11.636  1.00 20.44 ? 190 LEU   B CD1  1 
ATOM   3306 C  CD2  . LEU   B 1 211 ? -51.862 -14.995 12.524  1.00 21.12 ? 190 LEU   B CD2  1 
ATOM   3307 N  N    . GLU   B 1 212 ? -52.777 -14.887 7.978   1.00 15.25 ? 191 GLU   B N    1 
ATOM   3308 C  CA   . GLU   B 1 212 ? -53.756 -15.854 7.490   1.00 16.01 ? 191 GLU   B CA   1 
ATOM   3309 C  C    . GLU   B 1 212 ? -53.530 -16.209 6.021   1.00 18.80 ? 191 GLU   B C    1 
ATOM   3310 O  O    . GLU   B 1 212 ? -53.799 -17.346 5.615   1.00 19.90 ? 191 GLU   B O    1 
ATOM   3311 C  CB   . GLU   B 1 212 ? -55.154 -15.273 7.698   1.00 16.83 ? 191 GLU   B CB   1 
ATOM   3312 C  CG   . GLU   B 1 212 ? -56.273 -16.233 7.309   1.00 20.18 ? 191 GLU   B CG   1 
ATOM   3313 C  CD   . GLU   B 1 212 ? -57.620 -15.727 7.781   1.00 22.33 ? 191 GLU   B CD   1 
ATOM   3314 O  OE1  . GLU   B 1 212 ? -58.606 -16.410 7.460   1.00 22.25 ? 191 GLU   B OE1  1 
ATOM   3315 O  OE2  . GLU   B 1 212 ? -57.669 -14.686 8.490   1.00 22.46 ? 191 GLU   B OE2  1 
ATOM   3316 N  N    . LEU   B 1 213 ? -53.043 -15.258 5.217   1.00 16.59 ? 192 LEU   B N    1 
ATOM   3317 C  CA   . LEU   B 1 213 ? -52.905 -15.481 3.779   1.00 15.13 ? 192 LEU   B CA   1 
ATOM   3318 C  C    . LEU   B 1 213 ? -51.502 -15.957 3.396   1.00 17.13 ? 192 LEU   B C    1 
ATOM   3319 O  O    . LEU   B 1 213 ? -51.291 -16.380 2.261   1.00 18.00 ? 192 LEU   B O    1 
ATOM   3320 C  CB   . LEU   B 1 213 ? -53.303 -14.215 3.017   1.00 15.09 ? 192 LEU   B CB   1 
ATOM   3321 C  CG   . LEU   B 1 213 ? -54.757 -13.792 3.237   1.00 14.84 ? 192 LEU   B CG   1 
ATOM   3322 C  CD1  . LEU   B 1 213 ? -55.054 -12.542 2.419   1.00 15.35 ? 192 LEU   B CD1  1 
ATOM   3323 C  CD2  . LEU   B 1 213 ? -55.758 -14.902 2.899   1.00 15.18 ? 192 LEU   B CD2  1 
ATOM   3324 N  N    . ALA   B 1 214 ? -50.552 -15.907 4.333   1.00 17.48 ? 193 ALA   B N    1 
ATOM   3325 C  CA   . ALA   B 1 214 ? -49.202 -16.379 4.047   1.00 18.52 ? 193 ALA   B CA   1 
ATOM   3326 C  C    . ALA   B 1 214 ? -49.214 -17.794 3.464   1.00 19.73 ? 193 ALA   B C    1 
ATOM   3327 O  O    . ALA   B 1 214 ? -48.431 -18.065 2.553   1.00 20.39 ? 193 ALA   B O    1 
ATOM   3328 C  CB   . ALA   B 1 214 ? -48.351 -16.327 5.300   1.00 20.09 ? 193 ALA   B CB   1 
ATOM   3329 N  N    . PRO   B 1 215 ? -50.030 -18.756 3.967   1.00 22.43 ? 194 PRO   B N    1 
ATOM   3330 C  CA   . PRO   B 1 215 ? -50.007 -20.116 3.412   1.00 26.07 ? 194 PRO   B CA   1 
ATOM   3331 C  C    . PRO   B 1 215 ? -50.444 -20.225 1.953   1.00 28.09 ? 194 PRO   B C    1 
ATOM   3332 O  O    . PRO   B 1 215 ? -50.214 -21.252 1.316   1.00 29.40 ? 194 PRO   B O    1 
ATOM   3333 C  CB   . PRO   B 1 215 ? -50.916 -20.944 4.329   1.00 27.12 ? 194 PRO   B CB   1 
ATOM   3334 C  CG   . PRO   B 1 215 ? -51.144 -20.083 5.546   1.00 26.07 ? 194 PRO   B CG   1 
ATOM   3335 C  CD   . PRO   B 1 215 ? -50.950 -18.637 5.113   1.00 22.98 ? 194 PRO   B CD   1 
ATOM   3336 N  N    . TYR   B 1 216 ? -51.081 -19.165 1.440   1.00 25.06 ? 195 TYR   B N    1 
ATOM   3337 C  CA   . TYR   B 1 216 ? -51.544 -19.088 0.065   1.00 25.27 ? 195 TYR   B CA   1 
ATOM   3338 C  C    . TYR   B 1 216 ? -50.533 -18.303 -0.770  1.00 23.93 ? 195 TYR   B C    1 
ATOM   3339 O  O    . TYR   B 1 216 ? -50.724 -18.111 -1.971  1.00 28.01 ? 195 TYR   B O    1 
ATOM   3340 C  CB   . TYR   B 1 216 ? -52.911 -18.399 0.005   1.00 26.38 ? 195 TYR   B CB   1 
ATOM   3341 C  CG   . TYR   B 1 216 ? -54.031 -19.087 0.773   0.70 29.53 ? 195 TYR   B CG   1 
ATOM   3342 C  CD1  . TYR   B 1 216 ? -54.805 -20.075 0.175   0.70 32.58 ? 195 TYR   B CD1  1 
ATOM   3343 C  CD2  . TYR   B 1 216 ? -54.317 -18.744 2.089   0.70 28.69 ? 195 TYR   B CD2  1 
ATOM   3344 C  CE1  . TYR   B 1 216 ? -55.830 -20.698 0.865   0.70 33.49 ? 195 TYR   B CE1  1 
ATOM   3345 C  CE2  . TYR   B 1 216 ? -55.339 -19.361 2.793   0.70 33.28 ? 195 TYR   B CE2  1 
ATOM   3346 C  CZ   . TYR   B 1 216 ? -56.097 -20.343 2.176   0.70 35.42 ? 195 TYR   B CZ   1 
ATOM   3347 O  OH   . TYR   B 1 216 ? -57.113 -20.962 2.845   0.70 38.19 ? 195 TYR   B OH   1 
ATOM   3348 N  N    . GLY   B 1 217 ? -49.456 -17.842 -0.129  1.00 22.82 ? 196 GLY   B N    1 
ATOM   3349 C  CA   . GLY   B 1 217 ? -48.410 -17.109 -0.824  1.00 21.74 ? 196 GLY   B CA   1 
ATOM   3350 C  C    . GLY   B 1 217 ? -48.810 -15.663 -1.108  1.00 21.81 ? 196 GLY   B C    1 
ATOM   3351 O  O    . GLY   B 1 217 ? -48.175 -15.004 -1.922  1.00 23.78 ? 196 GLY   B O    1 
ATOM   3352 N  N    . ILE   B 1 218 ? -49.857 -15.175 -0.436  1.00 17.13 ? 197 ILE   B N    1 
ATOM   3353 C  CA   . ILE   B 1 218 ? -50.264 -13.778 -0.581  1.00 15.71 ? 197 ILE   B CA   1 
ATOM   3354 C  C    . ILE   B 1 218 ? -49.626 -12.943 0.532   1.00 15.35 ? 197 ILE   B C    1 
ATOM   3355 O  O    . ILE   B 1 218 ? -49.900 -13.155 1.713   1.00 16.91 ? 197 ILE   B O    1 
ATOM   3356 C  CB   . ILE   B 1 218 ? -51.795 -13.641 -0.509  1.00 15.47 ? 197 ILE   B CB   1 
ATOM   3357 C  CG1  . ILE   B 1 218 ? -52.468 -14.532 -1.572  1.00 17.52 ? 197 ILE   B CG1  1 
ATOM   3358 C  CG2  . ILE   B 1 218 ? -52.195 -12.167 -0.655  1.00 15.40 ? 197 ILE   B CG2  1 
ATOM   3359 C  CD1  . ILE   B 1 218 ? -53.966 -14.729 -1.376  1.00 20.58 ? 197 ILE   B CD1  1 
ATOM   3360 N  N    . ARG   B 1 219 ? -48.838 -11.946 0.131   1.00 14.82 ? 198 ARG   B N    1 
ATOM   3361 C  CA   . ARG   B 1 219 ? -48.173 -11.057 1.073   1.00 14.16 ? 198 ARG   B CA   1 
ATOM   3362 C  C    . ARG   B 1 219 ? -49.099 -9.867  1.326   1.00 14.01 ? 198 ARG   B C    1 
ATOM   3363 O  O    . ARG   B 1 219 ? -49.859 -9.459  0.439   1.00 14.85 ? 198 ARG   B O    1 
ATOM   3364 C  CB   . ARG   B 1 219 ? -46.809 -10.606 0.537   1.00 13.96 ? 198 ARG   B CB   1 
ATOM   3365 C  CG   . ARG   B 1 219 ? -45.837 -11.765 0.360   1.00 13.88 ? 198 ARG   B CG   1 
ATOM   3366 C  CD   . ARG   B 1 219 ? -44.458 -11.375 -0.119  1.00 14.45 ? 198 ARG   B CD   1 
ATOM   3367 N  NE   . ARG   B 1 219 ? -44.574 -10.747 -1.440  1.00 15.05 ? 198 ARG   B NE   1 
ATOM   3368 C  CZ   . ARG   B 1 219 ? -44.526 -9.437  -1.668  1.00 15.63 ? 198 ARG   B CZ   1 
ATOM   3369 N  NH1  . ARG   B 1 219 ? -44.297 -8.559  -0.696  1.00 14.98 ? 198 ARG   B NH1  1 
ATOM   3370 N  NH2  . ARG   B 1 219 ? -44.739 -9.014  -2.905  1.00 17.13 ? 198 ARG   B NH2  1 
ATOM   3371 N  N    . VAL   B 1 220 ? -49.061 -9.346  2.548   1.00 12.10 ? 199 VAL   B N    1 
ATOM   3372 C  CA   . VAL   B 1 220 ? -49.917 -8.217  2.888   1.00 12.47 ? 199 VAL   B CA   1 
ATOM   3373 C  C    . VAL   B 1 220 ? -49.075 -7.213  3.660   1.00 12.87 ? 199 VAL   B C    1 
ATOM   3374 O  O    . VAL   B 1 220 ? -48.602 -7.520  4.756   1.00 13.13 ? 199 VAL   B O    1 
ATOM   3375 C  CB   . VAL   B 1 220 ? -51.142 -8.651  3.711   1.00 12.68 ? 199 VAL   B CB   1 
ATOM   3376 C  CG1  . VAL   B 1 220 ? -52.106 -7.492  3.972   1.00 13.73 ? 199 VAL   B CG1  1 
ATOM   3377 C  CG2  . VAL   B 1 220 ? -51.891 -9.811  3.054   1.00 13.49 ? 199 VAL   B CG2  1 
ATOM   3378 N  N    . ASN   B 1 221 ? -48.927 -6.003  3.112   1.00 13.58 ? 200 ASN   B N    1 
ATOM   3379 C  CA   . ASN   B 1 221 ? -48.053 -4.999  3.676   1.00 14.34 ? 200 ASN   B CA   1 
ATOM   3380 C  C    . ASN   B 1 221 ? -48.743 -3.645  3.633   1.00 13.42 ? 200 ASN   B C    1 
ATOM   3381 O  O    . ASN   B 1 221 ? -49.838 -3.508  3.089   1.00 14.45 ? 200 ASN   B O    1 
ATOM   3382 C  CB   . ASN   B 1 221 ? -46.732 -4.944  2.919   1.00 13.17 ? 200 ASN   B CB   1 
ATOM   3383 C  CG   . ASN   B 1 221 ? -45.950 -6.227  3.099   1.00 13.33 ? 200 ASN   B CG   1 
ATOM   3384 O  OD1  . ASN   B 1 221 ? -45.463 -6.523  4.201   1.00 13.04 ? 200 ASN   B OD1  1 
ATOM   3385 N  ND2  . ASN   B 1 221 ? -45.814 -6.975  2.014   1.00 14.16 ? 200 ASN   B ND2  1 
ATOM   3386 N  N    . GLY   B 1 222 ? -48.108 -2.666  4.274   1.00 13.41 ? 201 GLY   B N    1 
ATOM   3387 C  CA   . GLY   B 1 222 ? -48.657 -1.322  4.238   1.00 13.43 ? 201 GLY   B CA   1 
ATOM   3388 C  C    . GLY   B 1 222 ? -47.581 -0.301  3.894   1.00 13.31 ? 201 GLY   B C    1 
ATOM   3389 O  O    . GLY   B 1 222 ? -46.374 -0.524  4.091   1.00 14.02 ? 201 GLY   B O    1 
ATOM   3390 N  N    . VAL   B 1 223 ? -48.069 0.842   3.402   1.00 12.69 ? 202 VAL   B N    1 
ATOM   3391 C  CA   . VAL   B 1 223 ? -47.252 2.034   3.212   1.00 13.06 ? 202 VAL   B CA   1 
ATOM   3392 C  C    . VAL   B 1 223 ? -47.924 3.135   3.998   1.00 13.19 ? 202 VAL   B C    1 
ATOM   3393 O  O    . VAL   B 1 223 ? -49.126 3.355   3.859   1.00 14.37 ? 202 VAL   B O    1 
ATOM   3394 C  CB   . VAL   B 1 223 ? -47.121 2.424   1.722   1.00 13.52 ? 202 VAL   B CB   1 
ATOM   3395 C  CG1  . VAL   B 1 223 ? -46.405 3.761   1.548   1.00 13.91 ? 202 VAL   B CG1  1 
ATOM   3396 C  CG2  . VAL   B 1 223 ? -46.369 1.354   0.942   1.00 14.79 ? 202 VAL   B CG2  1 
ATOM   3397 N  N    . ALA   B 1 224 ? -47.130 3.803   4.840   1.00 13.55 ? 203 ALA   B N    1 
ATOM   3398 C  CA   . ALA   B 1 224 ? -47.661 4.795   5.766   1.00 14.26 ? 203 ALA   B CA   1 
ATOM   3399 C  C    . ALA   B 1 224 ? -47.087 6.176   5.442   1.00 13.53 ? 203 ALA   B C    1 
ATOM   3400 O  O    . ALA   B 1 224 ? -46.018 6.540   5.924   1.00 13.57 ? 203 ALA   B O    1 
ATOM   3401 C  CB   . ALA   B 1 224 ? -47.337 4.395   7.199   1.00 14.40 ? 203 ALA   B CB   1 
ATOM   3402 N  N    . PRO   B 1 225 ? -47.782 7.005   4.636   1.00 14.31 ? 204 PRO   B N    1 
ATOM   3403 C  CA   . PRO   B 1 225 ? -47.304 8.369   4.394   1.00 14.84 ? 204 PRO   B CA   1 
ATOM   3404 C  C    . PRO   B 1 225 ? -47.424 9.186   5.669   1.00 15.98 ? 204 PRO   B C    1 
ATOM   3405 O  O    . PRO   B 1 225 ? -48.261 8.916   6.536   1.00 16.36 ? 204 PRO   B O    1 
ATOM   3406 C  CB   . PRO   B 1 225 ? -48.286 8.912   3.358   1.00 15.13 ? 204 PRO   B CB   1 
ATOM   3407 C  CG   . PRO   B 1 225 ? -48.926 7.678   2.760   1.00 16.28 ? 204 PRO   B CG   1 
ATOM   3408 C  CD   . PRO   B 1 225 ? -49.032 6.689   3.922   1.00 15.19 ? 204 PRO   B CD   1 
ATOM   3409 N  N    . GLY   B 1 226 ? -46.629 10.257  5.700   1.00 15.53 ? 205 GLY   B N    1 
ATOM   3410 C  CA   . GLY   B 1 226 ? -46.791 11.284  6.709   1.00 17.03 ? 205 GLY   B CA   1 
ATOM   3411 C  C    . GLY   B 1 226 ? -47.634 12.415  6.140   1.00 18.75 ? 205 GLY   B C    1 
ATOM   3412 O  O    . GLY   B 1 226 ? -48.862 12.376  6.217   1.00 21.97 ? 205 GLY   B O    1 
ATOM   3413 N  N    . VAL   B 1 227 ? -46.974 13.457  5.646   1.00 16.58 ? 206 VAL   B N    1 
ATOM   3414 C  CA   A VAL   B 1 227 ? -47.661 14.447  4.837   0.50 17.43 ? 206 VAL   B CA   1 
ATOM   3415 C  CA   B VAL   B 1 227 ? -47.687 14.425  4.830   0.50 17.31 ? 206 VAL   B CA   1 
ATOM   3416 C  C    . VAL   B 1 227 ? -47.214 14.239  3.394   1.00 17.23 ? 206 VAL   B C    1 
ATOM   3417 O  O    . VAL   B 1 227 ? -46.015 14.251  3.108   1.00 17.80 ? 206 VAL   B O    1 
ATOM   3418 C  CB   A VAL   B 1 227 ? -47.429 15.891  5.327   0.50 18.90 ? 206 VAL   B CB   1 
ATOM   3419 C  CB   B VAL   B 1 227 ? -47.631 15.901  5.267   0.50 18.93 ? 206 VAL   B CB   1 
ATOM   3420 C  CG1  A VAL   B 1 227 ? -45.965 16.206  5.594   0.50 21.77 ? 206 VAL   B CG1  1 
ATOM   3421 C  CG1  B VAL   B 1 227 ? -48.290 16.133  6.624   0.50 18.99 ? 206 VAL   B CG1  1 
ATOM   3422 C  CG2  A VAL   B 1 227 ? -48.028 16.918  4.376   0.50 19.08 ? 206 VAL   B CG2  1 
ATOM   3423 C  CG2  B VAL   B 1 227 ? -46.222 16.472  5.228   0.50 19.94 ? 206 VAL   B CG2  1 
ATOM   3424 N  N    . SER   B 1 228 ? -48.180 13.995  2.518   1.00 18.57 ? 207 SER   B N    1 
ATOM   3425 C  CA   . SER   B 1 228 ? -47.905 13.887  1.104   1.00 18.71 ? 207 SER   B CA   1 
ATOM   3426 C  C    . SER   B 1 228 ? -48.709 15.009  0.464   1.00 20.35 ? 207 SER   B C    1 
ATOM   3427 O  O    . SER   B 1 228 ? -48.765 16.097  1.032   1.00 23.13 ? 207 SER   B O    1 
ATOM   3428 C  CB   . SER   B 1 228 ? -48.254 12.527  0.561   1.00 20.91 ? 207 SER   B CB   1 
ATOM   3429 O  OG   . SER   B 1 228 ? -47.924 12.434  -0.819  1.00 21.91 ? 207 SER   B OG   1 
ATOM   3430 N  N    . LEU   B 1 229 ? -49.381 14.741  -0.655  1.00 23.23 ? 208 LEU   B N    1 
ATOM   3431 C  CA   . LEU   B 1 229 ? -50.105 15.813  -1.324  1.00 24.50 ? 208 LEU   B CA   1 
ATOM   3432 C  C    . LEU   B 1 229 ? -51.144 16.394  -0.373  1.00 24.92 ? 208 LEU   B C    1 
ATOM   3433 O  O    . LEU   B 1 229 ? -51.971 15.668  0.177   1.00 24.90 ? 208 LEU   B O    1 
ATOM   3434 C  CB   . LEU   B 1 229 ? -50.735 15.255  -2.600  1.00 26.40 ? 208 LEU   B CB   1 
ATOM   3435 C  CG   . LEU   B 1 229 ? -49.755 14.769  -3.672  1.00 27.10 ? 208 LEU   B CG   1 
ATOM   3436 C  CD1  . LEU   B 1 229 ? -50.530 14.511  -4.964  1.00 29.85 ? 208 LEU   B CD1  1 
ATOM   3437 C  CD2  . LEU   B 1 229 ? -48.602 15.733  -3.936  1.00 29.96 ? 208 LEU   B CD2  1 
ATOM   3438 N  N    . LEU   B 1 230 ? -51.075 17.714  -0.150  1.00 25.01 ? 209 LEU   B N    1 
ATOM   3439 C  CA   . LEU   B 1 230 ? -52.008 18.385  0.736   1.00 27.05 ? 209 LEU   B CA   1 
ATOM   3440 C  C    . LEU   B 1 230 ? -53.234 18.779  -0.088  1.00 30.72 ? 209 LEU   B C    1 
ATOM   3441 O  O    . LEU   B 1 230 ? -53.166 18.732  -1.306  1.00 32.37 ? 209 LEU   B O    1 
ATOM   3442 C  CB   . LEU   B 1 230 ? -51.232 19.578  1.297   1.00 27.38 ? 209 LEU   B CB   1 
ATOM   3443 C  CG   . LEU   B 1 230 ? -50.087 19.199  2.246   1.00 28.27 ? 209 LEU   B CG   1 
ATOM   3444 C  CD1  . LEU   B 1 230 ? -48.987 20.237  2.328   1.00 30.08 ? 209 LEU   B CD1  1 
ATOM   3445 C  CD2  . LEU   B 1 230 ? -50.646 18.911  3.641   1.00 30.83 ? 209 LEU   B CD2  1 
ATOM   3446 N  N    . PRO   B 1 231 ? -54.401 19.117  0.505   1.00 37.59 ? 210 PRO   B N    1 
ATOM   3447 C  CA   . PRO   B 1 231 ? -55.525 19.621  -0.300  1.00 41.56 ? 210 PRO   B CA   1 
ATOM   3448 C  C    . PRO   B 1 231 ? -55.135 20.753  -1.253  1.00 44.12 ? 210 PRO   B C    1 
ATOM   3449 O  O    . PRO   B 1 231 ? -54.454 21.692  -0.846  1.00 36.26 ? 210 PRO   B O    1 
ATOM   3450 C  CB   . PRO   B 1 231 ? -56.522 20.075  0.780   1.00 43.11 ? 210 PRO   B CB   1 
ATOM   3451 C  CG   . PRO   B 1 231 ? -56.240 19.151  1.945   1.00 40.28 ? 210 PRO   B CG   1 
ATOM   3452 C  CD   . PRO   B 1 231 ? -54.724 18.974  1.935   1.00 40.15 ? 210 PRO   B CD   1 
ATOM   3453 N  N    . VAL   B 1 232 ? -55.568 20.661  -2.523  1.00 46.78 ? 211 VAL   B N    1 
ATOM   3454 C  CA   . VAL   B 1 232 ? -55.240 21.663  -3.532  1.00 48.23 ? 211 VAL   B CA   1 
ATOM   3455 C  C    . VAL   B 1 232 ? -55.749 23.027  -3.061  1.00 45.37 ? 211 VAL   B C    1 
ATOM   3456 O  O    . VAL   B 1 232 ? -55.139 24.062  -3.346  1.00 48.46 ? 211 VAL   B O    1 
ATOM   3457 C  CB   . VAL   B 1 232 ? -55.789 21.319  -4.933  1.00 50.59 ? 211 VAL   B CB   1 
ATOM   3458 N  N    . ALA   B 1 233 ? -56.847 22.981  -2.296  1.00 43.67 ? 212 ALA   B N    1 
ATOM   3459 C  CA   . ALA   B 1 233 ? -57.589 24.142  -1.829  1.00 40.32 ? 212 ALA   B CA   1 
ATOM   3460 C  C    . ALA   B 1 233 ? -56.947 24.772  -0.593  1.00 35.97 ? 212 ALA   B C    1 
ATOM   3461 O  O    . ALA   B 1 233 ? -57.201 25.946  -0.325  1.00 31.21 ? 212 ALA   B O    1 
ATOM   3462 C  CB   . ALA   B 1 233 ? -59.022 23.743  -1.537  1.00 43.34 ? 212 ALA   B CB   1 
ATOM   3463 N  N    . MET   B 1 234 ? -56.178 23.979  0.178   1.00 29.18 ? 213 MET   B N    1 
ATOM   3464 C  CA   . MET   B 1 234 ? -55.506 24.456  1.382   1.00 25.35 ? 213 MET   B CA   1 
ATOM   3465 C  C    . MET   B 1 234 ? -54.562 25.591  0.994   1.00 24.59 ? 213 MET   B C    1 
ATOM   3466 O  O    . MET   B 1 234 ? -53.788 25.441  0.054   1.00 25.12 ? 213 MET   B O    1 
ATOM   3467 C  CB   . MET   B 1 234 ? -54.705 23.323  2.048   1.00 25.29 ? 213 MET   B CB   1 
ATOM   3468 C  CG   . MET   B 1 234 ? -53.975 23.715  3.328   1.00 26.59 ? 213 MET   B CG   1 
ATOM   3469 S  SD   . MET   B 1 234 ? -52.996 22.393  4.079   1.00 28.18 ? 213 MET   B SD   1 
ATOM   3470 C  CE   . MET   B 1 234 ? -54.250 21.562  5.069   1.00 28.71 ? 213 MET   B CE   1 
ATOM   3471 N  N    . GLY   B 1 235 ? -54.633 26.711  1.732   1.00 21.00 ? 214 GLY   B N    1 
ATOM   3472 C  CA   . GLY   B 1 235 ? -53.730 27.833  1.525   1.00 20.13 ? 214 GLY   B CA   1 
ATOM   3473 C  C    . GLY   B 1 235 ? -52.271 27.385  1.584   1.00 20.54 ? 214 GLY   B C    1 
ATOM   3474 O  O    . GLY   B 1 235 ? -51.905 26.553  2.408   1.00 19.29 ? 214 GLY   B O    1 
ATOM   3475 N  N    . GLU   B 1 236 ? -51.433 27.960  0.713   1.00 19.87 ? 215 GLU   B N    1 
ATOM   3476 C  CA   . GLU   B 1 236 ? -50.006 27.664  0.774   1.00 19.83 ? 215 GLU   B CA   1 
ATOM   3477 C  C    . GLU   B 1 236 ? -49.446 27.953  2.169   1.00 19.19 ? 215 GLU   B C    1 
ATOM   3478 O  O    . GLU   B 1 236 ? -48.497 27.304  2.616   1.00 19.09 ? 215 GLU   B O    1 
ATOM   3479 C  CB   . GLU   B 1 236 ? -49.202 28.406  -0.299  1.00 19.44 ? 215 GLU   B CB   1 
ATOM   3480 C  CG   . GLU   B 1 236 ? -49.417 27.869  -1.715  1.00 20.27 ? 215 GLU   B CG   1 
ATOM   3481 C  CD   . GLU   B 1 236 ? -48.916 26.452  -1.942  1.00 20.90 ? 215 GLU   B CD   1 
ATOM   3482 O  OE1  . GLU   B 1 236 ? -49.651 25.666  -2.560  1.00 23.74 ? 215 GLU   B OE1  1 
ATOM   3483 O  OE2  . GLU   B 1 236 ? -47.783 26.141  -1.500  1.00 20.44 ? 215 GLU   B OE2  1 
ATOM   3484 N  N    . GLU   B 1 237 ? -49.996 28.971  2.852   1.00 18.96 ? 216 GLU   B N    1 
ATOM   3485 C  CA   . GLU   B 1 237 ? -49.471 29.341  4.162   1.00 20.19 ? 216 GLU   B CA   1 
ATOM   3486 C  C    . GLU   B 1 237 ? -49.763 28.248  5.188   1.00 20.43 ? 216 GLU   B C    1 
ATOM   3487 O  O    . GLU   B 1 237 ? -48.976 28.068  6.121   1.00 21.52 ? 216 GLU   B O    1 
ATOM   3488 C  CB   . GLU   B 1 237 ? -49.915 30.722  4.656   1.00 21.46 ? 216 GLU   B CB   1 
ATOM   3489 C  CG   . GLU   B 1 237 ? -51.404 30.822  4.989   1.00 22.76 ? 216 GLU   B CG   1 
ATOM   3490 C  CD   . GLU   B 1 237 ? -52.490 30.782  3.919   1.00 24.40 ? 216 GLU   B CD   1 
ATOM   3491 O  OE1  . GLU   B 1 237 ? -53.643 30.754  4.394   1.00 28.26 ? 216 GLU   B OE1  1 
ATOM   3492 O  OE2  . GLU   B 1 237 ? -52.284 30.818  2.682   1.00 23.03 ? 216 GLU   B OE2  1 
ATOM   3493 N  N    . GLU   B 1 238 ? -50.882 27.528  5.004   1.00 20.43 ? 217 GLU   B N    1 
ATOM   3494 C  CA   . GLU   B 1 238 ? -51.215 26.412  5.875   1.00 20.85 ? 217 GLU   B CA   1 
ATOM   3495 C  C    . GLU   B 1 238 ? -50.391 25.187  5.479   1.00 20.74 ? 217 GLU   B C    1 
ATOM   3496 O  O    . GLU   B 1 238 ? -49.862 24.489  6.350   1.00 20.87 ? 217 GLU   B O    1 
ATOM   3497 C  CB   . GLU   B 1 238 ? -52.722 26.147  5.898   1.00 23.70 ? 217 GLU   B CB   1 
ATOM   3498 C  CG   . GLU   B 1 238 ? -53.121 25.128  6.963   1.00 27.37 ? 217 GLU   B CG   1 
ATOM   3499 C  CD   . GLU   B 1 238 ? -53.090 25.597  8.411   0.60 31.67 ? 217 GLU   B CD   1 
ATOM   3500 O  OE1  . GLU   B 1 238 ? -53.197 24.701  9.273   0.60 36.07 ? 217 GLU   B OE1  1 
ATOM   3501 O  OE2  . GLU   B 1 238 ? -52.980 26.816  8.699   0.60 33.95 ? 217 GLU   B OE2  1 
ATOM   3502 N  N    . LYS   B 1 239 ? -50.257 24.952  4.168   1.00 18.71 ? 218 LYS   B N    1 
ATOM   3503 C  CA   . LYS   B 1 239 ? -49.383 23.887  3.691   1.00 18.74 ? 218 LYS   B CA   1 
ATOM   3504 C  C    . LYS   B 1 239 ? -47.980 24.065  4.271   1.00 21.07 ? 218 LYS   B C    1 
ATOM   3505 O  O    . LYS   B 1 239 ? -47.347 23.095  4.685   1.00 19.52 ? 218 LYS   B O    1 
ATOM   3506 C  CB   . LYS   B 1 239 ? -49.283 23.865  2.162   1.00 18.71 ? 218 LYS   B CB   1 
ATOM   3507 C  CG   . LYS   B 1 239 ? -50.544 23.511  1.381   1.00 19.82 ? 218 LYS   B CG   1 
ATOM   3508 C  CD   . LYS   B 1 239 ? -50.189 23.184  -0.065  1.00 22.31 ? 218 LYS   B CD   1 
ATOM   3509 C  CE   . LYS   B 1 239 ? -51.367 22.832  -0.933  1.00 24.55 ? 218 LYS   B CE   1 
ATOM   3510 N  NZ   . LYS   B 1 239 ? -51.977 24.035  -1.514  1.00 27.56 ? 218 LYS   B NZ   1 
ATOM   3511 N  N    . ASP   B 1 240 ? -47.490 25.311  4.324   1.00 18.83 ? 219 ASP   B N    1 
ATOM   3512 C  CA   . ASP   B 1 240 ? -46.144 25.544  4.821   1.00 20.77 ? 219 ASP   B CA   1 
ATOM   3513 C  C    . ASP   B 1 240 ? -45.983 25.219  6.303   1.00 20.14 ? 219 ASP   B C    1 
ATOM   3514 O  O    . ASP   B 1 240 ? -44.878 24.868  6.724   1.00 21.93 ? 219 ASP   B O    1 
ATOM   3515 C  CB   . ASP   B 1 240 ? -45.746 26.999  4.646   1.00 21.45 ? 219 ASP   B CB   1 
ATOM   3516 C  CG   . ASP   B 1 240 ? -45.253 27.327  3.253   1.00 25.21 ? 219 ASP   B CG   1 
ATOM   3517 O  OD1  . ASP   B 1 240 ? -45.043 26.382  2.446   1.00 26.25 ? 219 ASP   B OD1  1 
ATOM   3518 O  OD2  . ASP   B 1 240 ? -45.096 28.540  2.987   1.00 24.94 ? 219 ASP   B OD2  1 
ATOM   3519 N  N    . LYS   B 1 241 ? -47.065 25.354  7.082   1.00 20.35 ? 220 LYS   B N    1 
ATOM   3520 C  CA   . LYS   B 1 241 ? -47.034 24.975  8.488   1.00 20.54 ? 220 LYS   B CA   1 
ATOM   3521 C  C    . LYS   B 1 241 ? -46.696 23.491  8.589   1.00 20.88 ? 220 LYS   B C    1 
ATOM   3522 O  O    . LYS   B 1 241 ? -45.937 23.102  9.473   1.00 24.55 ? 220 LYS   B O    1 
ATOM   3523 C  CB   . LYS   B 1 241 ? -48.323 25.296  9.251   1.00 24.20 ? 220 LYS   B CB   1 
ATOM   3524 C  CG   . LYS   B 1 241 ? -48.578 26.798  9.384   1.00 25.01 ? 220 LYS   B CG   1 
ATOM   3525 C  CD   . LYS   B 1 241 ? -49.761 27.168  10.270  0.60 27.29 ? 220 LYS   B CD   1 
ATOM   3526 C  CE   . LYS   B 1 241 ? -50.050 28.640  10.259  0.60 28.61 ? 220 LYS   B CE   1 
ATOM   3527 N  NZ   . LYS   B 1 241 ? -50.923 28.995  11.385  0.60 31.06 ? 220 LYS   B NZ   1 
ATOM   3528 N  N    . TRP   B 1 242 ? -47.239 22.689  7.670   1.00 21.42 ? 221 TRP   B N    1 
ATOM   3529 C  CA   . TRP   B 1 242 ? -46.954 21.257  7.698   1.00 21.10 ? 221 TRP   B CA   1 
ATOM   3530 C  C    . TRP   B 1 242 ? -45.580 20.947  7.120   1.00 19.92 ? 221 TRP   B C    1 
ATOM   3531 O  O    . TRP   B 1 242 ? -44.824 20.150  7.671   1.00 20.09 ? 221 TRP   B O    1 
ATOM   3532 C  CB   . TRP   B 1 242 ? -48.048 20.489  6.954   1.00 23.98 ? 221 TRP   B CB   1 
ATOM   3533 C  CG   . TRP   B 1 242 ? -49.291 20.450  7.793   1.00 29.40 ? 221 TRP   B CG   1 
ATOM   3534 C  CD1  . TRP   B 1 242 ? -50.348 21.310  7.740   1.00 31.56 ? 221 TRP   B CD1  1 
ATOM   3535 C  CD2  . TRP   B 1 242 ? -49.559 19.537  8.879   1.00 32.19 ? 221 TRP   B CD2  1 
ATOM   3536 N  NE1  . TRP   B 1 242 ? -51.269 20.981  8.701   1.00 33.21 ? 221 TRP   B NE1  1 
ATOM   3537 C  CE2  . TRP   B 1 242 ? -50.816 19.898  9.409   1.00 33.33 ? 221 TRP   B CE2  1 
ATOM   3538 C  CE3  . TRP   B 1 242 ? -48.870 18.452  9.437   1.00 34.79 ? 221 TRP   B CE3  1 
ATOM   3539 C  CZ2  . TRP   B 1 242 ? -51.392 19.208  10.477  1.00 35.01 ? 221 TRP   B CZ2  1 
ATOM   3540 C  CZ3  . TRP   B 1 242 ? -49.442 17.764  10.488  1.00 34.60 ? 221 TRP   B CZ3  1 
ATOM   3541 C  CH2  . TRP   B 1 242 ? -50.684 18.146  10.998  1.00 35.46 ? 221 TRP   B CH2  1 
ATOM   3542 N  N    . ARG   B 1 243 ? -45.248 21.597  6.007   1.00 18.24 ? 222 ARG   B N    1 
ATOM   3543 C  CA   . ARG   B 1 243 ? -43.968 21.354  5.367   1.00 19.23 ? 222 ARG   B CA   1 
ATOM   3544 C  C    . ARG   B 1 243 ? -42.815 21.637  6.326   1.00 20.56 ? 222 ARG   B C    1 
ATOM   3545 O  O    . ARG   B 1 243 ? -41.824 20.917  6.328   1.00 20.56 ? 222 ARG   B O    1 
ATOM   3546 C  CB   . ARG   B 1 243 ? -43.844 22.235  4.118   1.00 18.52 ? 222 ARG   B CB   1 
ATOM   3547 C  CG   . ARG   B 1 243 ? -44.791 21.804  3.012   1.00 18.35 ? 222 ARG   B CG   1 
ATOM   3548 C  CD   . ARG   B 1 243 ? -44.814 22.927  1.989   1.00 19.46 ? 222 ARG   B CD   1 
ATOM   3549 N  NE   . ARG   B 1 243 ? -45.566 22.495  0.810   1.00 20.78 ? 222 ARG   B NE   1 
ATOM   3550 C  CZ   . ARG   B 1 243 ? -46.208 23.304  -0.023  1.00 18.70 ? 222 ARG   B CZ   1 
ATOM   3551 N  NH1  . ARG   B 1 243 ? -46.295 24.597  0.272   1.00 21.08 ? 222 ARG   B NH1  1 
ATOM   3552 N  NH2  . ARG   B 1 243 ? -46.754 22.780  -1.095  1.00 20.59 ? 222 ARG   B NH2  1 
ATOM   3553 N  N    . ARG   B 1 244 ? -42.932 22.698  7.130   1.00 20.66 ? 223 ARG   B N    1 
ATOM   3554 C  CA   . ARG   B 1 244 ? -41.816 23.115  7.964   1.00 22.87 ? 223 ARG   B CA   1 
ATOM   3555 C  C    . ARG   B 1 244 ? -41.540 22.099  9.068   1.00 23.33 ? 223 ARG   B C    1 
ATOM   3556 O  O    . ARG   B 1 244 ? -40.475 22.161  9.681   1.00 25.26 ? 223 ARG   B O    1 
ATOM   3557 C  CB   . ARG   B 1 244 ? -42.037 24.490  8.603   1.00 27.36 ? 223 ARG   B CB   1 
ATOM   3558 C  CG   . ARG   B 1 244 ? -41.620 25.578  7.625   0.60 30.26 ? 223 ARG   B CG   1 
ATOM   3559 C  CD   . ARG   B 1 244 ? -41.609 26.946  8.273   0.60 32.78 ? 223 ARG   B CD   1 
ATOM   3560 N  NE   . ARG   B 1 244 ? -42.973 27.328  8.649   0.60 35.04 ? 223 ARG   B NE   1 
ATOM   3561 C  CZ   . ARG   B 1 244 ? -43.735 28.122  7.902   0.60 34.38 ? 223 ARG   B CZ   1 
ATOM   3562 N  NH1  . ARG   B 1 244 ? -43.284 28.574  6.744   0.60 35.31 ? 223 ARG   B NH1  1 
ATOM   3563 N  NH2  . ARG   B 1 244 ? -44.954 28.424  8.301   0.60 31.30 ? 223 ARG   B NH2  1 
ATOM   3564 N  N    . LYS   B 1 245 ? -42.500 21.200  9.320   1.00 21.38 ? 224 LYS   B N    1 
ATOM   3565 C  CA   . LYS   B 1 245 ? -42.359 20.225  10.393  1.00 22.48 ? 224 LYS   B CA   1 
ATOM   3566 C  C    . LYS   B 1 245 ? -41.532 19.028  9.927   1.00 20.05 ? 224 LYS   B C    1 
ATOM   3567 O  O    . LYS   B 1 245 ? -41.098 18.225  10.763  1.00 21.08 ? 224 LYS   B O    1 
ATOM   3568 C  CB   . LYS   B 1 245 ? -43.717 19.666  10.832  1.00 24.39 ? 224 LYS   B CB   1 
ATOM   3569 C  CG   . LYS   B 1 245 ? -44.771 20.674  11.316  1.00 27.49 ? 224 LYS   B CG   1 
ATOM   3570 C  CD   . LYS   B 1 245 ? -46.098 19.972  11.591  1.00 30.54 ? 224 LYS   B CD   1 
ATOM   3571 C  CE   . LYS   B 1 245 ? -47.310 20.850  11.807  1.00 33.66 ? 224 LYS   B CE   1 
ATOM   3572 N  NZ   . LYS   B 1 245 ? -47.149 21.685  12.999  1.00 35.97 ? 224 LYS   B NZ   1 
ATOM   3573 N  N    . VAL   B 1 246 ? -41.323 18.888  8.613   1.00 17.44 ? 225 VAL   B N    1 
ATOM   3574 C  CA   . VAL   B 1 246 ? -40.747 17.662  8.069   1.00 15.31 ? 225 VAL   B CA   1 
ATOM   3575 C  C    . VAL   B 1 246 ? -39.224 17.757  8.083   1.00 15.87 ? 225 VAL   B C    1 
ATOM   3576 O  O    . VAL   B 1 246 ? -38.634 18.599  7.389   1.00 16.69 ? 225 VAL   B O    1 
ATOM   3577 C  CB   . VAL   B 1 246 ? -41.222 17.359  6.638   1.00 14.74 ? 225 VAL   B CB   1 
ATOM   3578 C  CG1  . VAL   B 1 246 ? -40.566 16.076  6.112   1.00 14.76 ? 225 VAL   B CG1  1 
ATOM   3579 C  CG2  . VAL   B 1 246 ? -42.752 17.315  6.546   1.00 16.91 ? 225 VAL   B CG2  1 
ATOM   3580 N  N    . PRO   B 1 247 ? -38.507 16.891  8.844   1.00 15.18 ? 226 PRO   B N    1 
ATOM   3581 C  CA   . PRO   B 1 247 ? -37.046 16.987  8.893   1.00 16.34 ? 226 PRO   B CA   1 
ATOM   3582 C  C    . PRO   B 1 247 ? -36.327 16.897  7.553   1.00 16.97 ? 226 PRO   B C    1 
ATOM   3583 O  O    . PRO   B 1 247 ? -35.375 17.656  7.301   1.00 16.93 ? 226 PRO   B O    1 
ATOM   3584 C  CB   . PRO   B 1 247 ? -36.660 15.819  9.825   1.00 16.87 ? 226 PRO   B CB   1 
ATOM   3585 C  CG   . PRO   B 1 247 ? -37.884 15.617  10.697  1.00 17.04 ? 226 PRO   B CG   1 
ATOM   3586 C  CD   . PRO   B 1 247 ? -39.071 15.885  9.771   1.00 16.69 ? 226 PRO   B CD   1 
ATOM   3587 N  N    . LEU   B 1 248 ? -36.774 15.964  6.714   1.00 15.52 ? 227 LEU   B N    1 
ATOM   3588 C  CA   . LEU   B 1 248 ? -36.073 15.673  5.475   1.00 15.78 ? 227 LEU   B CA   1 
ATOM   3589 C  C    . LEU   B 1 248 ? -36.593 16.587  4.370   1.00 16.69 ? 227 LEU   B C    1 
ATOM   3590 O  O    . LEU   B 1 248 ? -37.507 16.245  3.632   1.00 18.38 ? 227 LEU   B O    1 
ATOM   3591 C  CB   . LEU   B 1 248 ? -36.214 14.192  5.129   1.00 15.85 ? 227 LEU   B CB   1 
ATOM   3592 C  CG   . LEU   B 1 248 ? -35.298 13.721  3.995   1.00 16.26 ? 227 LEU   B CG   1 
ATOM   3593 C  CD1  . LEU   B 1 248 ? -33.830 13.648  4.414   1.00 18.79 ? 227 LEU   B CD1  1 
ATOM   3594 C  CD2  . LEU   B 1 248 ? -35.783 12.346  3.517   1.00 16.31 ? 227 LEU   B CD2  1 
ATOM   3595 N  N    . GLY   B 1 249 ? -35.995 17.784  4.310   1.00 17.01 ? 228 GLY   B N    1 
ATOM   3596 C  CA   . GLY   B 1 249 ? -36.241 18.682  3.195   1.00 18.57 ? 228 GLY   B CA   1 
ATOM   3597 C  C    . GLY   B 1 249 ? -37.385 19.675  3.396   1.00 17.63 ? 228 GLY   B C    1 
ATOM   3598 O  O    . GLY   B 1 249 ? -37.613 20.476  2.491   1.00 18.14 ? 228 GLY   B O    1 
ATOM   3599 N  N    . ARG   B 1 250 ? -38.094 19.637  4.539   1.00 16.20 ? 229 ARG   B N    1 
ATOM   3600 C  CA   . ARG   B 1 250 ? -39.133 20.608  4.850   1.00 17.04 ? 229 ARG   B CA   1 
ATOM   3601 C  C    . ARG   B 1 250 ? -40.112 20.684  3.681   1.00 17.66 ? 229 ARG   B C    1 
ATOM   3602 O  O    . ARG   B 1 250 ? -40.485 21.766  3.217   1.00 18.06 ? 229 ARG   B O    1 
ATOM   3603 C  CB   . ARG   B 1 250 ? -38.517 21.986  5.146   1.00 18.99 ? 229 ARG   B CB   1 
ATOM   3604 C  CG   . ARG   B 1 250 ? -37.497 21.975  6.275   1.00 23.34 ? 229 ARG   B CG   1 
ATOM   3605 C  CD   . ARG   B 1 250 ? -38.038 21.794  7.663   0.70 25.71 ? 229 ARG   B CD   1 
ATOM   3606 N  NE   . ARG   B 1 250 ? -36.887 21.606  8.555   0.70 28.55 ? 229 ARG   B NE   1 
ATOM   3607 C  CZ   . ARG   B 1 250 ? -36.972 21.054  9.758   0.70 29.18 ? 229 ARG   B CZ   1 
ATOM   3608 N  NH1  . ARG   B 1 250 ? -38.148 20.693  10.223  0.70 27.85 ? 229 ARG   B NH1  1 
ATOM   3609 N  NH2  . ARG   B 1 250 ? -35.885 20.857  10.487  0.70 31.38 ? 229 ARG   B NH2  1 
ATOM   3610 N  N    . ARG   B 1 251 ? -40.521 19.501  3.217   1.00 16.34 ? 230 ARG   B N    1 
ATOM   3611 C  CA   A ARG   B 1 251 ? -41.474 19.386  2.128   0.50 16.28 ? 230 ARG   B CA   1 
ATOM   3612 C  CA   B ARG   B 1 251 ? -41.470 19.385  2.124   0.50 16.48 ? 230 ARG   B CA   1 
ATOM   3613 C  C    . ARG   B 1 251 ? -42.302 18.118  2.315   1.00 17.03 ? 230 ARG   B C    1 
ATOM   3614 O  O    . ARG   B 1 251 ? -41.866 17.172  2.990   1.00 16.12 ? 230 ARG   B O    1 
ATOM   3615 C  CB   A ARG   B 1 251 ? -40.750 19.320  0.775   0.50 16.90 ? 230 ARG   B CB   1 
ATOM   3616 C  CB   B ARG   B 1 251 ? -40.714 19.305  0.790   0.50 17.47 ? 230 ARG   B CB   1 
ATOM   3617 C  CG   A ARG   B 1 251 ? -39.609 18.314  0.677   0.50 18.60 ? 230 ARG   B CG   1 
ATOM   3618 C  CG   B ARG   B 1 251 ? -39.980 17.996  0.525   0.50 19.85 ? 230 ARG   B CG   1 
ATOM   3619 C  CD   A ARG   B 1 251 ? -39.125 18.111  -0.759  0.50 21.17 ? 230 ARG   B CD   1 
ATOM   3620 C  CD   B ARG   B 1 251 ? -38.886 18.100  -0.529  0.50 22.46 ? 230 ARG   B CD   1 
ATOM   3621 N  NE   A ARG   B 1 251 ? -40.036 17.228  -1.496  0.50 21.70 ? 230 ARG   B NE   1 
ATOM   3622 N  NE   B ARG   B 1 251 ? -38.027 19.221  -0.137  0.50 23.39 ? 230 ARG   B NE   1 
ATOM   3623 C  CZ   A ARG   B 1 251 ? -39.991 15.897  -1.399  0.50 23.55 ? 230 ARG   B CZ   1 
ATOM   3624 C  CZ   B ARG   B 1 251 ? -36.909 19.625  -0.719  0.50 25.73 ? 230 ARG   B CZ   1 
ATOM   3625 N  NH1  A ARG   B 1 251 ? -39.008 15.300  -0.746  0.50 26.62 ? 230 ARG   B NH1  1 
ATOM   3626 N  NH1  B ARG   B 1 251 ? -36.289 20.690  -0.242  0.50 24.11 ? 230 ARG   B NH1  1 
ATOM   3627 N  NH2  A ARG   B 1 251 ? -40.890 15.178  -2.020  0.50 20.97 ? 230 ARG   B NH2  1 
ATOM   3628 N  NH2  B ARG   B 1 251 ? -36.428 18.984  -1.768  0.50 27.04 ? 230 ARG   B NH2  1 
ATOM   3629 N  N    . GLU   B 1 252 ? -43.489 18.121  1.696   1.00 17.01 ? 231 GLU   B N    1 
ATOM   3630 C  CA   . GLU   B 1 252 ? -44.354 16.943  1.712   1.00 16.60 ? 231 GLU   B CA   1 
ATOM   3631 C  C    . GLU   B 1 252 ? -43.841 15.929  0.692   1.00 17.07 ? 231 GLU   B C    1 
ATOM   3632 O  O    . GLU   B 1 252 ? -43.090 16.247  -0.234  1.00 18.70 ? 231 GLU   B O    1 
ATOM   3633 C  CB   . GLU   B 1 252 ? -45.800 17.345  1.388   1.00 16.65 ? 231 GLU   B CB   1 
ATOM   3634 C  CG   . GLU   B 1 252 ? -46.016 17.797  -0.063  1.00 19.03 ? 231 GLU   B CG   1 
ATOM   3635 C  CD   . GLU   B 1 252 ? -45.775 19.282  -0.341  1.00 20.84 ? 231 GLU   B CD   1 
ATOM   3636 O  OE1  . GLU   B 1 252 ? -46.584 19.857  -1.109  1.00 22.44 ? 231 GLU   B OE1  1 
ATOM   3637 O  OE2  . GLU   B 1 252 ? -44.821 19.887  0.182   1.00 20.65 ? 231 GLU   B OE2  1 
ATOM   3638 N  N    . ALA   B 1 253 ? -44.236 14.656  0.858   1.00 16.34 ? 232 ALA   B N    1 
ATOM   3639 C  CA   . ALA   B 1 253 ? -43.885 13.671  -0.156  1.00 15.76 ? 232 ALA   B CA   1 
ATOM   3640 C  C    . ALA   B 1 253 ? -44.668 13.942  -1.435  1.00 16.03 ? 232 ALA   B C    1 
ATOM   3641 O  O    . ALA   B 1 253 ? -45.844 14.306  -1.381  1.00 17.83 ? 232 ALA   B O    1 
ATOM   3642 C  CB   . ALA   B 1 253 ? -44.254 12.263  0.299   1.00 16.99 ? 232 ALA   B CB   1 
ATOM   3643 N  N    . SER   B 1 254 ? -44.033 13.660  -2.575  1.00 15.49 ? 233 SER   B N    1 
ATOM   3644 C  CA   . SER   B 1 254 ? -44.818 13.597  -3.794  1.00 15.95 ? 233 SER   B CA   1 
ATOM   3645 C  C    . SER   B 1 254 ? -45.661 12.327  -3.795  1.00 15.61 ? 233 SER   B C    1 
ATOM   3646 O  O    . SER   B 1 254 ? -45.325 11.351  -3.105  1.00 16.26 ? 233 SER   B O    1 
ATOM   3647 C  CB   . SER   B 1 254 ? -43.922 13.617  -5.007  1.00 16.87 ? 233 SER   B CB   1 
ATOM   3648 O  OG   . SER   B 1 254 ? -43.162 12.425  -5.154  1.00 17.88 ? 233 SER   B OG   1 
ATOM   3649 N  N    . ALA   B 1 255 ? -46.702 12.306  -4.641  1.00 14.84 ? 234 ALA   B N    1 
ATOM   3650 C  CA   . ALA   B 1 255 ? -47.459 11.074  -4.781  1.00 15.48 ? 234 ALA   B CA   1 
ATOM   3651 C  C    . ALA   B 1 255 ? -46.562 9.971   -5.331  1.00 15.60 ? 234 ALA   B C    1 
ATOM   3652 O  O    . ALA   B 1 255 ? -46.750 8.802   -4.977  1.00 15.18 ? 234 ALA   B O    1 
ATOM   3653 C  CB   . ALA   B 1 255 ? -48.670 11.303  -5.684  1.00 17.38 ? 234 ALA   B CB   1 
ATOM   3654 N  N    . GLU   B 1 256 ? -45.616 10.317  -6.213  1.00 15.06 ? 235 GLU   B N    1 
ATOM   3655 C  CA   . GLU   B 1 256 ? -44.718 9.339   -6.809  1.00 15.69 ? 235 GLU   B CA   1 
ATOM   3656 C  C    . GLU   B 1 256 ? -43.817 8.691   -5.753  1.00 14.98 ? 235 GLU   B C    1 
ATOM   3657 O  O    . GLU   B 1 256 ? -43.500 7.505   -5.889  1.00 15.65 ? 235 GLU   B O    1 
ATOM   3658 C  CB   . GLU   B 1 256 ? -43.883 10.003  -7.907  1.00 17.19 ? 235 GLU   B CB   1 
ATOM   3659 C  CG   . GLU   B 1 256 ? -44.719 10.411  -9.124  1.00 19.42 ? 235 GLU   B CG   1 
ATOM   3660 C  CD   . GLU   B 1 256 ? -45.607 11.651  -9.039  1.00 21.57 ? 235 GLU   B CD   1 
ATOM   3661 O  OE1  . GLU   B 1 256 ? -45.631 12.385  -8.030  1.00 22.34 ? 235 GLU   B OE1  1 
ATOM   3662 O  OE2  . GLU   B 1 256 ? -46.322 11.894  -10.053 1.00 24.22 ? 235 GLU   B OE2  1 
ATOM   3663 N  N    . GLN   B 1 257 ? -43.384 9.452   -4.726  1.00 15.34 ? 236 GLN   B N    1 
ATOM   3664 C  CA   . GLN   B 1 257 ? -42.535 8.889   -3.676  1.00 15.25 ? 236 GLN   B CA   1 
ATOM   3665 C  C    . GLN   B 1 257 ? -43.315 7.841   -2.893  1.00 14.71 ? 236 GLN   B C    1 
ATOM   3666 O  O    . GLN   B 1 257 ? -42.763 6.788   -2.546  1.00 15.35 ? 236 GLN   B O    1 
ATOM   3667 C  CB   . GLN   B 1 257 ? -41.970 10.004  -2.796  1.00 16.27 ? 236 GLN   B CB   1 
ATOM   3668 C  CG   . GLN   B 1 257 ? -40.885 10.772  -3.537  1.00 16.61 ? 236 GLN   B CG   1 
ATOM   3669 C  CD   . GLN   B 1 257 ? -40.462 12.026  -2.811  1.00 17.46 ? 236 GLN   B CD   1 
ATOM   3670 O  OE1  . GLN   B 1 257 ? -41.247 12.703  -2.139  1.00 17.95 ? 236 GLN   B OE1  1 
ATOM   3671 N  NE2  . GLN   B 1 257 ? -39.186 12.352  -2.960  1.00 20.25 ? 236 GLN   B NE2  1 
ATOM   3672 N  N    . ILE   B 1 258 ? -44.596 8.114   -2.631  1.00 14.23 ? 237 ILE   B N    1 
ATOM   3673 C  CA   . ILE   B 1 258 ? -45.429 7.111   -1.972  1.00 13.45 ? 237 ILE   B CA   1 
ATOM   3674 C  C    . ILE   B 1 258 ? -45.552 5.901   -2.886  1.00 14.75 ? 237 ILE   B C    1 
ATOM   3675 O  O    . ILE   B 1 258 ? -45.412 4.755   -2.439  1.00 15.52 ? 237 ILE   B O    1 
ATOM   3676 C  CB   . ILE   B 1 258 ? -46.807 7.685   -1.601  1.00 13.47 ? 237 ILE   B CB   1 
ATOM   3677 C  CG1  . ILE   B 1 258 ? -46.687 8.951   -0.719  1.00 14.83 ? 237 ILE   B CG1  1 
ATOM   3678 C  CG2  . ILE   B 1 258 ? -47.694 6.617   -0.949  1.00 15.70 ? 237 ILE   B CG2  1 
ATOM   3679 C  CD1  . ILE   B 1 258 ? -45.859 8.766   0.547   1.00 16.29 ? 237 ILE   B CD1  1 
ATOM   3680 N  N    . ALA   B 1 259 ? -45.866 6.144   -4.169  1.00 14.97 ? 238 ALA   B N    1 
ATOM   3681 C  CA   . ALA   B 1 259 ? -45.993 5.032   -5.105  1.00 14.95 ? 238 ALA   B CA   1 
ATOM   3682 C  C    . ALA   B 1 259 ? -44.724 4.183   -5.208  1.00 14.34 ? 238 ALA   B C    1 
ATOM   3683 O  O    . ALA   B 1 259 ? -44.819 2.969   -5.389  1.00 14.90 ? 238 ALA   B O    1 
ATOM   3684 C  CB   . ALA   B 1 259 ? -46.440 5.549   -6.476  1.00 14.53 ? 238 ALA   B CB   1 
ATOM   3685 N  N    . ASP   B 1 260 ? -43.528 4.798   -5.111  1.00 14.87 ? 239 ASP   B N    1 
ATOM   3686 C  CA   . ASP   B 1 260 ? -42.285 4.028   -5.141  1.00 16.49 ? 239 ASP   B CA   1 
ATOM   3687 C  C    . ASP   B 1 260 ? -42.229 2.928   -4.074  1.00 15.19 ? 239 ASP   B C    1 
ATOM   3688 O  O    . ASP   B 1 260 ? -41.691 1.840   -4.335  1.00 16.34 ? 239 ASP   B O    1 
ATOM   3689 C  CB   . ASP   B 1 260 ? -41.074 4.932   -4.979  1.00 17.33 ? 239 ASP   B CB   1 
ATOM   3690 C  CG   . ASP   B 1 260 ? -40.703 5.722   -6.229  1.00 21.71 ? 239 ASP   B CG   1 
ATOM   3691 O  OD1  . ASP   B 1 260 ? -41.048 5.268   -7.352  1.00 21.77 ? 239 ASP   B OD1  1 
ATOM   3692 O  OD2  . ASP   B 1 260 ? -40.103 6.804   -6.063  1.00 23.26 ? 239 ASP   B OD2  1 
ATOM   3693 N  N    . ALA   B 1 261 ? -42.797 3.203   -2.888  1.00 14.55 ? 240 ALA   B N    1 
ATOM   3694 C  CA   . ALA   B 1 261 ? -42.765 2.216   -1.815  1.00 15.27 ? 240 ALA   B CA   1 
ATOM   3695 C  C    . ALA   B 1 261 ? -43.756 1.102   -2.128  1.00 14.95 ? 240 ALA   B C    1 
ATOM   3696 O  O    . ALA   B 1 261 ? -43.491 -0.067  -1.813  1.00 13.99 ? 240 ALA   B O    1 
ATOM   3697 C  CB   . ALA   B 1 261 ? -43.081 2.868   -0.477  1.00 15.25 ? 240 ALA   B CB   1 
ATOM   3698 N  N    . VAL   B 1 262 ? -44.916 1.455   -2.723  1.00 14.98 ? 241 VAL   B N    1 
ATOM   3699 C  CA   . VAL   B 1 262 ? -45.867 0.427   -3.131  1.00 15.44 ? 241 VAL   B CA   1 
ATOM   3700 C  C    . VAL   B 1 262 ? -45.218 -0.493  -4.166  1.00 15.24 ? 241 VAL   B C    1 
ATOM   3701 O  O    . VAL   B 1 262 ? -45.332 -1.724  -4.088  1.00 15.51 ? 241 VAL   B O    1 
ATOM   3702 C  CB   . VAL   B 1 262 ? -47.162 1.043   -3.696  1.00 15.69 ? 241 VAL   B CB   1 
ATOM   3703 C  CG1  . VAL   B 1 262 ? -48.098 -0.049  -4.223  1.00 17.25 ? 241 VAL   B CG1  1 
ATOM   3704 C  CG2  . VAL   B 1 262 ? -47.840 1.922   -2.665  1.00 16.61 ? 241 VAL   B CG2  1 
ATOM   3705 N  N    . ILE   B 1 263 ? -44.532 0.100   -5.154  1.00 14.79 ? 242 ILE   B N    1 
ATOM   3706 C  CA   . ILE   B 1 263 ? -43.865 -0.656  -6.208  1.00 17.07 ? 242 ILE   B CA   1 
ATOM   3707 C  C    . ILE   B 1 263 ? -42.844 -1.626  -5.607  1.00 15.55 ? 242 ILE   B C    1 
ATOM   3708 O  O    . ILE   B 1 263 ? -42.802 -2.794  -5.994  1.00 16.17 ? 242 ILE   B O    1 
ATOM   3709 C  CB   . ILE   B 1 263 ? -43.234 0.281   -7.255  1.00 17.44 ? 242 ILE   B CB   1 
ATOM   3710 C  CG1  . ILE   B 1 263 ? -44.309 0.963   -8.107  1.00 21.32 ? 242 ILE   B CG1  1 
ATOM   3711 C  CG2  . ILE   B 1 263 ? -42.209 -0.473  -8.111  1.00 18.79 ? 242 ILE   B CG2  1 
ATOM   3712 C  CD1  . ILE   B 1 263 ? -45.145 0.020   -8.947  1.00 21.52 ? 242 ILE   B CD1  1 
ATOM   3713 N  N    . PHE   B 1 264 ? -42.050 -1.165  -4.628  1.00 14.69 ? 243 PHE   B N    1 
ATOM   3714 C  CA   . PHE   B 1 264 ? -41.113 -2.049  -3.958  1.00 14.00 ? 243 PHE   B CA   1 
ATOM   3715 C  C    . PHE   B 1 264 ? -41.848 -3.231  -3.330  1.00 13.75 ? 243 PHE   B C    1 
ATOM   3716 O  O    . PHE   B 1 264 ? -41.457 -4.387  -3.513  1.00 14.12 ? 243 PHE   B O    1 
ATOM   3717 C  CB   . PHE   B 1 264 ? -40.296 -1.261  -2.921  1.00 14.73 ? 243 PHE   B CB   1 
ATOM   3718 C  CG   . PHE   B 1 264 ? -39.498 -2.190  -2.014  1.00 15.27 ? 243 PHE   B CG   1 
ATOM   3719 C  CD1  . PHE   B 1 264 ? -38.403 -2.898  -2.511  1.00 16.90 ? 243 PHE   B CD1  1 
ATOM   3720 C  CD2  . PHE   B 1 264 ? -39.831 -2.315  -0.665  1.00 14.69 ? 243 PHE   B CD2  1 
ATOM   3721 C  CE1  . PHE   B 1 264 ? -37.680 -3.765  -1.704  1.00 17.27 ? 243 PHE   B CE1  1 
ATOM   3722 C  CE2  . PHE   B 1 264 ? -39.107 -3.193  0.146   1.00 16.01 ? 243 PHE   B CE2  1 
ATOM   3723 C  CZ   . PHE   B 1 264 ? -38.025 -3.893  -0.376  1.00 16.21 ? 243 PHE   B CZ   1 
ATOM   3724 N  N    . LEU   B 1 265 ? -42.917 -2.952  -2.584  1.00 13.99 ? 244 LEU   B N    1 
ATOM   3725 C  CA   . LEU   B 1 265 ? -43.592 -4.014  -1.854  1.00 13.77 ? 244 LEU   B CA   1 
ATOM   3726 C  C    . LEU   B 1 265 ? -44.235 -5.058  -2.765  1.00 15.09 ? 244 LEU   B C    1 
ATOM   3727 O  O    . LEU   B 1 265 ? -44.364 -6.215  -2.372  1.00 15.50 ? 244 LEU   B O    1 
ATOM   3728 C  CB   . LEU   B 1 265 ? -44.608 -3.442  -0.873  1.00 14.45 ? 244 LEU   B CB   1 
ATOM   3729 C  CG   . LEU   B 1 265 ? -43.977 -2.816  0.377   1.00 14.04 ? 244 LEU   B CG   1 
ATOM   3730 C  CD1  . LEU   B 1 265 ? -45.077 -2.033  1.086   1.00 14.42 ? 244 LEU   B CD1  1 
ATOM   3731 C  CD2  . LEU   B 1 265 ? -43.439 -3.936  1.257   1.00 15.45 ? 244 LEU   B CD2  1 
ATOM   3732 N  N    . VAL   B 1 266 ? -44.635 -4.656  -3.968  1.00 15.60 ? 245 VAL   B N    1 
ATOM   3733 C  CA   . VAL   B 1 266 ? -45.265 -5.630  -4.851  1.00 16.51 ? 245 VAL   B CA   1 
ATOM   3734 C  C    . VAL   B 1 266 ? -44.230 -6.396  -5.681  1.00 17.66 ? 245 VAL   B C    1 
ATOM   3735 O  O    . VAL   B 1 266 ? -44.586 -7.390  -6.307  1.00 20.68 ? 245 VAL   B O    1 
ATOM   3736 C  CB   . VAL   B 1 266 ? -46.382 -5.042  -5.736  1.00 18.64 ? 245 VAL   B CB   1 
ATOM   3737 C  CG1  . VAL   B 1 266 ? -47.433 -4.335  -4.892  1.00 18.34 ? 245 VAL   B CG1  1 
ATOM   3738 C  CG2  . VAL   B 1 266 ? -45.853 -4.109  -6.816  1.00 20.21 ? 245 VAL   B CG2  1 
ATOM   3739 N  N    . SER   B 1 267 ? -42.975 -5.935  -5.676  1.00 16.09 ? 246 SER   B N    1 
ATOM   3740 C  CA   . SER   B 1 267 ? -41.910 -6.439  -6.534  1.00 15.87 ? 246 SER   B CA   1 
ATOM   3741 C  C    . SER   B 1 267 ? -41.301 -7.735  -6.006  1.00 18.37 ? 246 SER   B C    1 
ATOM   3742 O  O    . SER   B 1 267 ? -41.462 -8.123  -4.844  1.00 17.87 ? 246 SER   B O    1 
ATOM   3743 C  CB   . SER   B 1 267 ? -40.803 -5.426  -6.689  1.00 16.88 ? 246 SER   B CB   1 
ATOM   3744 O  OG   . SER   B 1 267 ? -39.960 -5.415  -5.537  1.00 17.28 ? 246 SER   B OG   1 
ATOM   3745 N  N    . GLY   B 1 268 ? -40.477 -8.321  -6.884  1.00 18.95 ? 247 GLY   B N    1 
ATOM   3746 C  CA   . GLY   B 1 268 ? -39.709 -9.516  -6.559  1.00 22.02 ? 247 GLY   B CA   1 
ATOM   3747 C  C    . GLY   B 1 268 ? -38.605 -9.252  -5.533  1.00 22.03 ? 247 GLY   B C    1 
ATOM   3748 O  O    . GLY   B 1 268 ? -37.960 -10.192 -5.075  1.00 27.81 ? 247 GLY   B O    1 
ATOM   3749 N  N    . SER   B 1 269 ? -38.371 -7.986  -5.189  1.00 17.95 ? 248 SER   B N    1 
ATOM   3750 C  CA   . SER   B 1 269 ? -37.352 -7.600  -4.224  1.00 19.05 ? 248 SER   B CA   1 
ATOM   3751 C  C    . SER   B 1 269 ? -37.917 -7.607  -2.801  1.00 17.13 ? 248 SER   B C    1 
ATOM   3752 O  O    . SER   B 1 269 ? -37.190 -7.302  -1.847  1.00 18.45 ? 248 SER   B O    1 
ATOM   3753 C  CB   . SER   B 1 269 ? -36.798 -6.228  -4.563  1.00 21.33 ? 248 SER   B CB   1 
ATOM   3754 O  OG   . SER   B 1 269 ? -36.156 -6.236  -5.838  1.00 25.49 ? 248 SER   B OG   1 
ATOM   3755 N  N    . ALA   B 1 270 ? -39.219 -7.910  -2.670  1.00 16.30 ? 249 ALA   B N    1 
ATOM   3756 C  CA   . ALA   B 1 270 ? -39.914 -7.890  -1.386  1.00 16.02 ? 249 ALA   B CA   1 
ATOM   3757 C  C    . ALA   B 1 270 ? -40.576 -9.234  -1.094  1.00 15.05 ? 249 ALA   B C    1 
ATOM   3758 O  O    . ALA   B 1 270 ? -41.511 -9.307  -0.299  1.00 14.74 ? 249 ALA   B O    1 
ATOM   3759 C  CB   . ALA   B 1 270 ? -40.930 -6.749  -1.330  1.00 16.17 ? 249 ALA   B CB   1 
ATOM   3760 N  N    . GLN   B 1 271 ? -40.056 -10.323 -1.677  1.00 16.89 ? 250 GLN   B N    1 
ATOM   3761 C  CA   A GLN   B 1 271 ? -40.775 -11.589 -1.661  0.60 18.44 ? 250 GLN   B CA   1 
ATOM   3762 C  CA   B GLN   B 1 271 ? -40.759 -11.599 -1.669  0.40 17.78 ? 250 GLN   B CA   1 
ATOM   3763 C  C    . GLN   B 1 271 ? -40.806 -12.244 -0.280  1.00 16.41 ? 250 GLN   B C    1 
ATOM   3764 O  O    . GLN   B 1 271 ? -41.565 -13.200 -0.085  1.00 15.84 ? 250 GLN   B O    1 
ATOM   3765 C  CB   A GLN   B 1 271 ? -40.187 -12.551 -2.694  0.60 23.25 ? 250 GLN   B CB   1 
ATOM   3766 C  CB   B GLN   B 1 271 ? -40.120 -12.542 -2.690  0.40 20.95 ? 250 GLN   B CB   1 
ATOM   3767 C  CG   A GLN   B 1 271 ? -39.978 -11.873 -4.042  0.60 26.76 ? 250 GLN   B CG   1 
ATOM   3768 C  CG   B GLN   B 1 271 ? -38.654 -12.838 -2.404  0.40 23.65 ? 250 GLN   B CG   1 
ATOM   3769 C  CD   A GLN   B 1 271 ? -39.945 -12.810 -5.228  0.60 30.67 ? 250 GLN   B CD   1 
ATOM   3770 C  CD   B GLN   B 1 271 ? -37.839 -13.165 -3.637  0.40 23.79 ? 250 GLN   B CD   1 
ATOM   3771 O  OE1  A GLN   B 1 271 ? -40.981 -13.332 -5.652  0.60 33.67 ? 250 GLN   B OE1  1 
ATOM   3772 O  OE1  B GLN   B 1 271 ? -36.637 -13.431 -3.556  0.40 22.66 ? 250 GLN   B OE1  1 
ATOM   3773 N  NE2  A GLN   B 1 271 ? -38.763 -12.980 -5.806  0.60 34.05 ? 250 GLN   B NE2  1 
ATOM   3774 N  NE2  B GLN   B 1 271 ? -38.479 -13.132 -4.797  0.40 26.46 ? 250 GLN   B NE2  1 
ATOM   3775 N  N    . TYR   B 1 272 ? -39.999 -11.746 0.677   1.00 14.29 ? 251 TYR   B N    1 
ATOM   3776 C  CA   . TYR   B 1 272 ? -39.995 -12.295 2.035   1.00 14.07 ? 251 TYR   B CA   1 
ATOM   3777 C  C    . TYR   B 1 272 ? -40.709 -11.356 3.010   1.00 14.68 ? 251 TYR   B C    1 
ATOM   3778 O  O    . TYR   B 1 272 ? -40.762 -11.604 4.222   1.00 14.59 ? 251 TYR   B O    1 
ATOM   3779 C  CB   . TYR   B 1 272 ? -38.578 -12.603 2.540   1.00 14.46 ? 251 TYR   B CB   1 
ATOM   3780 C  CG   . TYR   B 1 272 ? -38.492 -13.555 3.727   1.00 14.19 ? 251 TYR   B CG   1 
ATOM   3781 C  CD1  . TYR   B 1 272 ? -38.673 -14.920 3.544   1.00 14.73 ? 251 TYR   B CD1  1 
ATOM   3782 C  CD2  . TYR   B 1 272 ? -38.194 -13.113 5.015   1.00 14.14 ? 251 TYR   B CD2  1 
ATOM   3783 C  CE1  . TYR   B 1 272 ? -38.566 -15.802 4.604   1.00 14.91 ? 251 TYR   B CE1  1 
ATOM   3784 C  CE2  . TYR   B 1 272 ? -38.060 -13.989 6.082   1.00 13.08 ? 251 TYR   B CE2  1 
ATOM   3785 C  CZ   . TYR   B 1 272 ? -38.250 -15.346 5.873   1.00 13.40 ? 251 TYR   B CZ   1 
ATOM   3786 O  OH   . TYR   B 1 272 ? -38.088 -16.200 6.932   1.00 14.51 ? 251 TYR   B OH   1 
ATOM   3787 N  N    . ILE   B 1 273 ? -41.202 -10.234 2.485   1.00 13.78 ? 252 ILE   B N    1 
ATOM   3788 C  CA   . ILE   B 1 273 ? -41.783 -9.206  3.338   1.00 12.93 ? 252 ILE   B CA   1 
ATOM   3789 C  C    . ILE   B 1 273 ? -43.295 -9.382  3.386   1.00 12.76 ? 252 ILE   B C    1 
ATOM   3790 O  O    . ILE   B 1 273 ? -43.982 -9.311  2.364   1.00 12.88 ? 252 ILE   B O    1 
ATOM   3791 C  CB   . ILE   B 1 273 ? -41.422 -7.793  2.839   1.00 12.65 ? 252 ILE   B CB   1 
ATOM   3792 C  CG1  . ILE   B 1 273 ? -39.892 -7.603  2.700   1.00 12.96 ? 252 ILE   B CG1  1 
ATOM   3793 C  CG2  . ILE   B 1 273 ? -42.060 -6.700  3.706   1.00 13.76 ? 252 ILE   B CG2  1 
ATOM   3794 C  CD1  . ILE   B 1 273 ? -39.474 -6.203  2.253   1.00 14.30 ? 252 ILE   B CD1  1 
ATOM   3795 N  N    . THR   B 1 274 ? -43.802 -9.633  4.586   1.00 12.74 ? 253 THR   B N    1 
ATOM   3796 C  CA   . THR   B 1 274 ? -45.236 -9.646  4.826   1.00 12.99 ? 253 THR   B CA   1 
ATOM   3797 C  C    . THR   B 1 274 ? -45.501 -9.155  6.244   1.00 13.79 ? 253 THR   B C    1 
ATOM   3798 O  O    . THR   B 1 274 ? -44.706 -9.410  7.153   1.00 14.58 ? 253 THR   B O    1 
ATOM   3799 C  CB   . THR   B 1 274 ? -45.855 -11.015 4.506   1.00 13.70 ? 253 THR   B CB   1 
ATOM   3800 O  OG1  . THR   B 1 274 ? -47.275 -10.839 4.404   1.00 12.58 ? 253 THR   B OG1  1 
ATOM   3801 C  CG2  . THR   B 1 274 ? -45.505 -12.086 5.534   1.00 15.03 ? 253 THR   B CG2  1 
ATOM   3802 N  N    . GLY   B 1 275 ? -46.614 -8.430  6.399   1.00 13.22 ? 254 GLY   B N    1 
ATOM   3803 C  CA   . GLY   B 1 275 ? -46.991 -7.866  7.687   1.00 14.07 ? 254 GLY   B CA   1 
ATOM   3804 C  C    . GLY   B 1 275 ? -46.218 -6.599  8.053   1.00 14.90 ? 254 GLY   B C    1 
ATOM   3805 O  O    . GLY   B 1 275 ? -46.253 -6.213  9.223   1.00 17.33 ? 254 GLY   B O    1 
ATOM   3806 N  N    . SER   B 1 276 ? -45.471 -6.030  7.098   1.00 15.05 ? 255 SER   B N    1 
ATOM   3807 C  CA   . SER   B 1 276 ? -44.619 -4.875  7.342   1.00 15.23 ? 255 SER   B CA   1 
ATOM   3808 C  C    . SER   B 1 276 ? -45.335 -3.612  6.904   1.00 14.93 ? 255 SER   B C    1 
ATOM   3809 O  O    . SER   B 1 276 ? -45.995 -3.615  5.875   1.00 16.25 ? 255 SER   B O    1 
ATOM   3810 C  CB   . SER   B 1 276 ? -43.309 -4.979  6.615   1.00 16.96 ? 255 SER   B CB   1 
ATOM   3811 O  OG   . SER   B 1 276 ? -42.628 -6.145  7.083   1.00 19.74 ? 255 SER   B OG   1 
ATOM   3812 N  N    . ILE   B 1 277 ? -45.120 -2.532  7.651   1.00 14.84 ? 256 ILE   B N    1 
ATOM   3813 C  CA   . ILE   B 1 277 ? -45.645 -1.250  7.220   1.00 16.19 ? 256 ILE   B CA   1 
ATOM   3814 C  C    . ILE   B 1 277 ? -44.455 -0.310  7.068   1.00 16.52 ? 256 ILE   B C    1 
ATOM   3815 O  O    . ILE   B 1 277 ? -43.734 -0.070  8.041   1.00 20.24 ? 256 ILE   B O    1 
ATOM   3816 C  CB   . ILE   B 1 277 ? -46.711 -0.736  8.205   1.00 17.74 ? 256 ILE   B CB   1 
ATOM   3817 C  CG1  . ILE   B 1 277 ? -47.933 -1.673  8.226   1.00 19.60 ? 256 ILE   B CG1  1 
ATOM   3818 C  CG2  . ILE   B 1 277 ? -47.103 0.711   7.844   1.00 17.97 ? 256 ILE   B CG2  1 
ATOM   3819 C  CD1  . ILE   B 1 277 ? -48.869 -1.438  9.396   1.00 23.95 ? 256 ILE   B CD1  1 
ATOM   3820 N  N    . ILE   B 1 278 ? -44.242 0.181   5.845   1.00 15.43 ? 257 ILE   B N    1 
ATOM   3821 C  CA   . ILE   B 1 278 ? -43.105 1.048   5.549   1.00 15.18 ? 257 ILE   B CA   1 
ATOM   3822 C  C    . ILE   B 1 278 ? -43.559 2.502   5.686   1.00 14.94 ? 257 ILE   B C    1 
ATOM   3823 O  O    . ILE   B 1 278 ? -44.421 2.955   4.929   1.00 15.30 ? 257 ILE   B O    1 
ATOM   3824 C  CB   . ILE   B 1 278 ? -42.564 0.774   4.135   1.00 16.98 ? 257 ILE   B CB   1 
ATOM   3825 C  CG1  . ILE   B 1 278 ? -42.080 -0.681  3.967   1.00 18.26 ? 257 ILE   B CG1  1 
ATOM   3826 C  CG2  . ILE   B 1 278 ? -41.445 1.768   3.801   1.00 19.60 ? 257 ILE   B CG2  1 
ATOM   3827 C  CD1  . ILE   B 1 278 ? -41.585 -0.973  2.556   1.00 20.23 ? 257 ILE   B CD1  1 
ATOM   3828 N  N    . LYS   B 1 279 ? -42.997 3.217   6.664   1.00 14.47 ? 258 LYS   B N    1 
ATOM   3829 C  CA   . LYS   B 1 279 ? -43.259 4.651   6.774   1.00 15.93 ? 258 LYS   B CA   1 
ATOM   3830 C  C    . LYS   B 1 279 ? -42.530 5.387   5.662   1.00 15.54 ? 258 LYS   B C    1 
ATOM   3831 O  O    . LYS   B 1 279 ? -41.359 5.110   5.387   1.00 15.81 ? 258 LYS   B O    1 
ATOM   3832 C  CB   . LYS   B 1 279 ? -42.725 5.278   8.067   1.00 19.17 ? 258 LYS   B CB   1 
ATOM   3833 C  CG   . LYS   B 1 279 ? -43.462 5.020   9.346   1.00 21.20 ? 258 LYS   B CG   1 
ATOM   3834 C  CD   . LYS   B 1 279 ? -42.804 5.874   10.443  1.00 20.81 ? 258 LYS   B CD   1 
ATOM   3835 C  CE   . LYS   B 1 279 ? -41.354 5.482   10.710  1.00 21.61 ? 258 LYS   B CE   1 
ATOM   3836 N  NZ   . LYS   B 1 279 ? -40.745 6.219   11.833  1.00 21.54 ? 258 LYS   B NZ   1 
ATOM   3837 N  N    . VAL   B 1 280 ? -43.245 6.310   5.009   1.00 14.84 ? 259 VAL   B N    1 
ATOM   3838 C  CA   . VAL   B 1 280 ? -42.659 7.180   4.002   1.00 13.81 ? 259 VAL   B CA   1 
ATOM   3839 C  C    . VAL   B 1 280 ? -43.023 8.608   4.388   1.00 14.72 ? 259 VAL   B C    1 
ATOM   3840 O  O    . VAL   B 1 280 ? -43.965 9.172   3.832   1.00 15.89 ? 259 VAL   B O    1 
ATOM   3841 C  CB   . VAL   B 1 280 ? -43.152 6.832   2.583   1.00 14.82 ? 259 VAL   B CB   1 
ATOM   3842 C  CG1  . VAL   B 1 280 ? -42.403 7.633   1.540   1.00 15.83 ? 259 VAL   B CG1  1 
ATOM   3843 C  CG2  . VAL   B 1 280 ? -42.979 5.337   2.311   1.00 14.55 ? 259 VAL   B CG2  1 
ATOM   3844 N  N    . ASP   B 1 281 ? -42.311 9.122   5.401   1.00 13.59 ? 260 ASP   B N    1 
ATOM   3845 C  CA   . ASP   B 1 281 ? -42.766 10.335  6.061   1.00 13.77 ? 260 ASP   B CA   1 
ATOM   3846 C  C    . ASP   B 1 281 ? -41.669 11.378  6.237   1.00 13.32 ? 260 ASP   B C    1 
ATOM   3847 O  O    . ASP   B 1 281 ? -41.935 12.383  6.881   1.00 14.23 ? 260 ASP   B O    1 
ATOM   3848 C  CB   . ASP   B 1 281 ? -43.427 10.012  7.394   1.00 15.27 ? 260 ASP   B CB   1 
ATOM   3849 C  CG   . ASP   B 1 281 ? -42.475 9.634   8.516   1.00 15.41 ? 260 ASP   B CG   1 
ATOM   3850 O  OD1  . ASP   B 1 281 ? -41.264 9.414   8.242   1.00 15.05 ? 260 ASP   B OD1  1 
ATOM   3851 O  OD2  . ASP   B 1 281 ? -42.915 9.660   9.672   1.00 15.36 ? 260 ASP   B OD2  1 
ATOM   3852 N  N    . GLY   B 1 282 ? -40.458 11.166  5.695   1.00 13.12 ? 261 GLY   B N    1 
ATOM   3853 C  CA   . GLY   B 1 282 ? -39.467 12.243  5.781   1.00 13.96 ? 261 GLY   B CA   1 
ATOM   3854 C  C    . GLY   B 1 282 ? -39.045 12.547  7.228   1.00 13.72 ? 261 GLY   B C    1 
ATOM   3855 O  O    . GLY   B 1 282 ? -38.471 13.600  7.519   1.00 14.31 ? 261 GLY   B O    1 
ATOM   3856 N  N    . GLY   B 1 283 ? -39.332 11.623  8.156   1.00 13.61 ? 262 GLY   B N    1 
ATOM   3857 C  CA   . GLY   B 1 283 ? -39.013 11.838  9.558   1.00 13.19 ? 262 GLY   B CA   1 
ATOM   3858 C  C    . GLY   B 1 283 ? -40.120 12.524  10.377  1.00 13.22 ? 262 GLY   B C    1 
ATOM   3859 O  O    . GLY   B 1 283 ? -39.933 12.742  11.575  1.00 14.14 ? 262 GLY   B O    1 
ATOM   3860 N  N    . LEU   B 1 284 ? -41.277 12.841  9.774   1.00 13.37 ? 263 LEU   B N    1 
ATOM   3861 C  CA   . LEU   B 1 284 ? -42.291 13.632  10.466  1.00 14.45 ? 263 LEU   B CA   1 
ATOM   3862 C  C    . LEU   B 1 284 ? -42.716 13.008  11.797  1.00 14.52 ? 263 LEU   B C    1 
ATOM   3863 O  O    . LEU   B 1 284 ? -42.899 13.711  12.790  1.00 15.49 ? 263 LEU   B O    1 
ATOM   3864 C  CB   . LEU   B 1 284 ? -43.505 13.822  9.561   1.00 15.20 ? 263 LEU   B CB   1 
ATOM   3865 C  CG   . LEU   B 1 284 ? -44.645 14.619  10.201  1.00 16.94 ? 263 LEU   B CG   1 
ATOM   3866 C  CD1  . LEU   B 1 284 ? -44.134 16.042  10.463  1.00 19.10 ? 263 LEU   B CD1  1 
ATOM   3867 C  CD2  . LEU   B 1 284 ? -45.832 14.608  9.254   1.00 20.54 ? 263 LEU   B CD2  1 
ATOM   3868 N  N    . SER   B 1 285 ? -42.868 11.680  11.800  1.00 14.19 ? 264 SER   B N    1 
ATOM   3869 C  CA   . SER   B 1 285 ? -43.354 11.006  12.994  1.00 15.26 ? 264 SER   B CA   1 
ATOM   3870 C  C    . SER   B 1 285 ? -42.336 11.002  14.138  1.00 15.96 ? 264 SER   B C    1 
ATOM   3871 O  O    . SER   B 1 285 ? -42.701 10.657  15.270  1.00 18.50 ? 264 SER   B O    1 
ATOM   3872 C  CB   . SER   B 1 285 ? -43.838 9.621   12.688  1.00 16.27 ? 264 SER   B CB   1 
ATOM   3873 O  OG   . SER   B 1 285 ? -42.772 8.804   12.227  1.00 18.44 ? 264 SER   B OG   1 
ATOM   3874 N  N    . LEU   B 1 286 ? -41.095 11.416  13.862  1.00 14.76 ? 265 LEU   B N    1 
ATOM   3875 C  CA   . LEU   B 1 286 ? -40.059 11.483  14.886  1.00 14.88 ? 265 LEU   B CA   1 
ATOM   3876 C  C    . LEU   B 1 286 ? -40.040 12.826  15.615  1.00 16.06 ? 265 LEU   B C    1 
ATOM   3877 O  O    . LEU   B 1 286 ? -39.262 12.954  16.557  1.00 16.24 ? 265 LEU   B O    1 
ATOM   3878 C  CB   . LEU   B 1 286 ? -38.693 11.267  14.237  1.00 16.21 ? 265 LEU   B CB   1 
ATOM   3879 C  CG   . LEU   B 1 286 ? -38.535 10.024  13.364  1.00 18.25 ? 265 LEU   B CG   1 
ATOM   3880 C  CD1  . LEU   B 1 286 ? -37.171 10.094  12.684  1.00 19.39 ? 265 LEU   B CD1  1 
ATOM   3881 C  CD2  . LEU   B 1 286 ? -38.733 8.751   14.167  1.00 21.41 ? 265 LEU   B CD2  1 
ATOM   3882 N  N    . VAL   B 1 287 ? -40.843 13.801  15.180  1.00 15.78 ? 266 VAL   B N    1 
ATOM   3883 C  CA   . VAL   B 1 287 ? -40.751 15.181  15.639  1.00 15.94 ? 266 VAL   B CA   1 
ATOM   3884 C  C    . VAL   B 1 287 ? -41.717 15.374  16.809  1.00 18.11 ? 266 VAL   B C    1 
ATOM   3885 O  O    . VAL   B 1 287 ? -42.932 15.217  16.675  1.00 19.07 ? 266 VAL   B O    1 
ATOM   3886 C  CB   . VAL   B 1 287 ? -41.072 16.162  14.496  1.00 17.25 ? 266 VAL   B CB   1 
ATOM   3887 C  CG1  . VAL   B 1 287 ? -40.970 17.611  14.973  1.00 18.50 ? 266 VAL   B CG1  1 
ATOM   3888 C  CG2  . VAL   B 1 287 ? -40.131 15.957  13.324  1.00 16.63 ? 266 VAL   B CG2  1 
ATOM   3889 N  N    . HIS   B 1 288 ? -41.159 15.760  17.960  1.00 17.91 ? 267 HIS   B N    1 
ATOM   3890 C  CA   . HIS   B 1 288 ? -42.002 15.989  19.122  1.00 18.35 ? 267 HIS   B CA   1 
ATOM   3891 C  C    . HIS   B 1 288 ? -42.782 17.305  19.014  1.00 19.94 ? 267 HIS   B C    1 
ATOM   3892 O  O    . HIS   B 1 288 ? -42.437 18.199  18.247  1.00 20.60 ? 267 HIS   B O    1 
ATOM   3893 C  CB   . HIS   B 1 288 ? -41.158 15.951  20.404  1.00 19.48 ? 267 HIS   B CB   1 
ATOM   3894 C  CG   . HIS   B 1 288 ? -40.120 17.021  20.552  1.00 20.11 ? 267 HIS   B CG   1 
ATOM   3895 N  ND1  . HIS   B 1 288 ? -40.403 18.366  20.737  1.00 20.85 ? 267 HIS   B ND1  1 
ATOM   3896 C  CD2  . HIS   B 1 288 ? -38.784 16.923  20.534  1.00 22.07 ? 267 HIS   B CD2  1 
ATOM   3897 C  CE1  . HIS   B 1 288 ? -39.265 19.044  20.840  1.00 22.52 ? 267 HIS   B CE1  1 
ATOM   3898 N  NE2  . HIS   B 1 288 ? -38.267 18.191  20.701  1.00 23.76 ? 267 HIS   B NE2  1 
ATOM   3899 N  N    . ALA   B 1 289 ? -43.800 17.439  19.867  1.00 21.43 ? 268 ALA   B N    1 
ATOM   3900 C  CA   . ALA   B 1 289 ? -44.612 18.646  19.931  1.00 23.99 ? 268 ALA   B CA   1 
ATOM   3901 C  C    . ALA   B 1 289 ? -43.757 19.878  20.246  1.00 25.10 ? 268 ALA   B C    1 
ATOM   3902 O  O    . ALA   B 1 289 ? -44.217 20.973  19.835  1.00 27.42 ? 268 ALA   B O    1 
ATOM   3903 C  CB   . ALA   B 1 289 ? -45.673 18.477  20.993  1.00 25.82 ? 268 ALA   B CB   1 
ATOM   3904 O  OXT  . ALA   B 1 289 ? -42.728 19.734  20.932  1.00 24.88 ? 268 ALA   B OXT  1 
ATOM   3905 N  N    . GLU   C 1 23  ? -41.268 -9.459  58.743  0.70 36.36 ? 2   GLU   C N    1 
ATOM   3906 C  CA   . GLU   C 1 23  ? -40.305 -8.331  58.605  0.70 35.97 ? 2   GLU   C CA   1 
ATOM   3907 C  C    . GLU   C 1 23  ? -40.647 -7.505  57.364  0.70 33.07 ? 2   GLU   C C    1 
ATOM   3908 O  O    . GLU   C 1 23  ? -41.303 -7.982  56.441  0.70 35.10 ? 2   GLU   C O    1 
ATOM   3909 C  CB   . GLU   C 1 23  ? -38.851 -8.792  58.737  0.70 36.47 ? 2   GLU   C CB   1 
ATOM   3910 C  CG   . GLU   C 1 23  ? -38.159 -9.116  57.414  0.70 35.89 ? 2   GLU   C CG   1 
ATOM   3911 N  N    . ALA   C 1 24  ? -40.209 -6.242  57.388  1.00 29.34 ? 3   ALA   C N    1 
ATOM   3912 C  CA   . ALA   C 1 24  ? -40.516 -5.270  56.359  1.00 25.42 ? 3   ALA   C CA   1 
ATOM   3913 C  C    . ALA   C 1 24  ? -39.697 -5.607  55.114  1.00 25.11 ? 3   ALA   C C    1 
ATOM   3914 O  O    . ALA   C 1 24  ? -38.511 -5.920  55.212  1.00 24.47 ? 3   ALA   C O    1 
ATOM   3915 C  CB   . ALA   C 1 24  ? -40.199 -3.882  56.871  1.00 24.63 ? 3   ALA   C CB   1 
ATOM   3916 N  N    . PRO   C 1 25  ? -40.287 -5.515  53.901  1.00 23.42 ? 4   PRO   C N    1 
ATOM   3917 C  CA   . PRO   C 1 25  ? -39.516 -5.780  52.685  1.00 21.71 ? 4   PRO   C CA   1 
ATOM   3918 C  C    . PRO   C 1 25  ? -38.562 -4.612  52.456  1.00 20.33 ? 4   PRO   C C    1 
ATOM   3919 O  O    . PRO   C 1 25  ? -38.674 -3.568  53.107  1.00 20.48 ? 4   PRO   C O    1 
ATOM   3920 C  CB   . PRO   C 1 25  ? -40.609 -5.885  51.620  1.00 21.28 ? 4   PRO   C CB   1 
ATOM   3921 C  CG   . PRO   C 1 25  ? -41.687 -4.938  52.112  1.00 22.55 ? 4   PRO   C CG   1 
ATOM   3922 C  CD   . PRO   C 1 25  ? -41.681 -5.114  53.635  1.00 23.06 ? 4   PRO   C CD   1 
ATOM   3923 N  N    . ALA   C 1 26  ? -37.588 -4.814  51.557  1.00 17.26 ? 5   ALA   C N    1 
ATOM   3924 C  CA   . ALA   C 1 26  ? -36.574 -3.798  51.338  1.00 16.64 ? 5   ALA   C CA   1 
ATOM   3925 C  C    . ALA   C 1 26  ? -36.456 -3.479  49.852  1.00 16.37 ? 5   ALA   C C    1 
ATOM   3926 O  O    . ALA   C 1 26  ? -36.669 -4.345  49.023  1.00 17.48 ? 5   ALA   C O    1 
ATOM   3927 C  CB   . ALA   C 1 26  ? -35.245 -4.262  51.895  1.00 18.08 ? 5   ALA   C CB   1 
ATOM   3928 N  N    . ALA   C 1 27  ? -36.141 -2.213  49.557  1.00 15.45 ? 6   ALA   C N    1 
ATOM   3929 C  CA   . ALA   C 1 27  ? -36.009 -1.760  48.179  1.00 15.48 ? 6   ALA   C CA   1 
ATOM   3930 C  C    . ALA   C 1 27  ? -34.708 -0.987  48.006  1.00 15.95 ? 6   ALA   C C    1 
ATOM   3931 O  O    . ALA   C 1 27  ? -34.322 -0.190  48.873  1.00 17.07 ? 6   ALA   C O    1 
ATOM   3932 C  CB   . ALA   C 1 27  ? -37.182 -0.877  47.832  1.00 16.28 ? 6   ALA   C CB   1 
ATOM   3933 N  N    . VAL   C 1 28  ? -34.091 -1.153  46.822  1.00 14.35 ? 7   VAL   C N    1 
ATOM   3934 C  CA   . VAL   C 1 28  ? -32.997 -0.293  46.392  1.00 14.35 ? 7   VAL   C CA   1 
ATOM   3935 C  C    . VAL   C 1 28  ? -33.553 0.693   45.378  1.00 13.82 ? 7   VAL   C C    1 
ATOM   3936 O  O    . VAL   C 1 28  ? -34.204 0.242   44.439  1.00 14.68 ? 7   VAL   C O    1 
ATOM   3937 C  CB   . VAL   C 1 28  ? -31.902 -1.153  45.736  1.00 14.63 ? 7   VAL   C CB   1 
ATOM   3938 C  CG1  . VAL   C 1 28  ? -30.871 -0.276  45.031  1.00 16.88 ? 7   VAL   C CG1  1 
ATOM   3939 C  CG2  . VAL   C 1 28  ? -31.208 -2.005  46.804  1.00 16.97 ? 7   VAL   C CG2  1 
ATOM   3940 N  N    . VAL   C 1 29  ? -33.292 1.997   45.570  1.00 13.69 ? 8   VAL   C N    1 
ATOM   3941 C  CA   . VAL   C 1 29  ? -33.656 3.003   44.579  1.00 14.14 ? 8   VAL   C CA   1 
ATOM   3942 C  C    . VAL   C 1 29  ? -32.370 3.693   44.140  1.00 14.10 ? 8   VAL   C C    1 
ATOM   3943 O  O    . VAL   C 1 29  ? -31.671 4.275   44.968  1.00 14.24 ? 8   VAL   C O    1 
ATOM   3944 C  CB   . VAL   C 1 29  ? -34.664 4.037   45.114  1.00 14.32 ? 8   VAL   C CB   1 
ATOM   3945 C  CG1  . VAL   C 1 29  ? -35.056 5.025   44.018  1.00 15.93 ? 8   VAL   C CG1  1 
ATOM   3946 C  CG2  . VAL   C 1 29  ? -35.915 3.342   45.670  1.00 15.22 ? 8   VAL   C CG2  1 
ATOM   3947 N  N    . THR   C 1 30  ? -32.041 3.641   42.841  1.00 14.07 ? 9   THR   C N    1 
ATOM   3948 C  CA   . THR   C 1 30  ? -30.851 4.348   42.375  1.00 14.02 ? 9   THR   C CA   1 
ATOM   3949 C  C    . THR   C 1 30  ? -31.144 5.828   42.117  1.00 15.29 ? 9   THR   C C    1 
ATOM   3950 O  O    . THR   C 1 30  ? -32.249 6.192   41.718  1.00 15.67 ? 9   THR   C O    1 
ATOM   3951 C  CB   . THR   C 1 30  ? -30.193 3.679   41.170  1.00 14.68 ? 9   THR   C CB   1 
ATOM   3952 O  OG1  . THR   C 1 30  ? -31.098 3.711   40.058  1.00 13.80 ? 9   THR   C OG1  1 
ATOM   3953 C  CG2  . THR   C 1 30  ? -29.804 2.242   41.475  1.00 14.84 ? 9   THR   C CG2  1 
ATOM   3954 N  N    . GLY   C 1 31  ? -30.124 6.666   42.324  1.00 15.03 ? 10  GLY   C N    1 
ATOM   3955 C  CA   . GLY   C 1 31  ? -30.279 8.101   42.129  1.00 15.98 ? 10  GLY   C CA   1 
ATOM   3956 C  C    . GLY   C 1 31  ? -31.421 8.665   42.970  1.00 17.21 ? 10  GLY   C C    1 
ATOM   3957 O  O    . GLY   C 1 31  ? -32.222 9.456   42.478  1.00 17.81 ? 10  GLY   C O    1 
ATOM   3958 N  N    . ALA   C 1 32  ? -31.450 8.304   44.264  1.00 15.87 ? 11  ALA   C N    1 
ATOM   3959 C  CA   . ALA   C 1 32  ? -32.620 8.558   45.091  1.00 15.85 ? 11  ALA   C CA   1 
ATOM   3960 C  C    . ALA   C 1 32  ? -32.485 9.787   45.993  1.00 16.43 ? 11  ALA   C C    1 
ATOM   3961 O  O    . ALA   C 1 32  ? -33.390 10.017  46.788  1.00 17.14 ? 11  ALA   C O    1 
ATOM   3962 C  CB   . ALA   C 1 32  ? -32.928 7.325   45.908  1.00 17.63 ? 11  ALA   C CB   1 
ATOM   3963 N  N    . ALA   C 1 33  ? -31.412 10.581  45.869  1.00 17.72 ? 12  ALA   C N    1 
ATOM   3964 C  CA   . ALA   C 1 33  ? -31.205 11.701  46.788  1.00 18.99 ? 12  ALA   C CA   1 
ATOM   3965 C  C    . ALA   C 1 33  ? -32.155 12.854  46.484  1.00 19.40 ? 12  ALA   C C    1 
ATOM   3966 O  O    . ALA   C 1 33  ? -32.519 13.604  47.395  1.00 21.80 ? 12  ALA   C O    1 
ATOM   3967 C  CB   . ALA   C 1 33  ? -29.774 12.183  46.747  1.00 19.40 ? 12  ALA   C CB   1 
ATOM   3968 N  N    . LYS   C 1 34  ? -32.536 13.016  45.209  1.00 20.09 ? 13  LYS   C N    1 
ATOM   3969 C  CA   . LYS   C 1 34  ? -33.340 14.170  44.837  1.00 22.65 ? 13  LYS   C CA   1 
ATOM   3970 C  C    . LYS   C 1 34  ? -34.422 13.793  43.826  1.00 21.52 ? 13  LYS   C C    1 
ATOM   3971 O  O    . LYS   C 1 34  ? -34.451 12.669  43.312  1.00 19.70 ? 13  LYS   C O    1 
ATOM   3972 C  CB   . LYS   C 1 34  ? -32.425 15.211  44.184  1.00 25.13 ? 13  LYS   C CB   1 
ATOM   3973 C  CG   . LYS   C 1 34  ? -31.282 15.710  45.056  1.00 27.82 ? 13  LYS   C CG   1 
ATOM   3974 C  CD   . LYS   C 1 34  ? -30.419 16.739  44.339  1.00 29.71 ? 13  LYS   C CD   1 
ATOM   3975 C  CE   . LYS   C 1 34  ? -29.417 17.307  45.291  0.60 31.69 ? 13  LYS   C CE   1 
ATOM   3976 N  NZ   . LYS   C 1 34  ? -28.707 18.430  44.675  0.60 32.26 ? 13  LYS   C NZ   1 
ATOM   3977 N  N    . ARG   C 1 35  ? -35.323 14.753  43.575  1.00 19.56 ? 14  ARG   C N    1 
ATOM   3978 C  CA   . ARG   C 1 35  ? -36.246 14.715  42.443  1.00 18.86 ? 14  ARG   C CA   1 
ATOM   3979 C  C    . ARG   C 1 35  ? -37.065 13.421  42.437  1.00 17.81 ? 14  ARG   C C    1 
ATOM   3980 O  O    . ARG   C 1 35  ? -37.711 13.053  43.415  1.00 19.01 ? 14  ARG   C O    1 
ATOM   3981 C  CB   . ARG   C 1 35  ? -35.425 15.040  41.188  1.00 19.09 ? 14  ARG   C CB   1 
ATOM   3982 C  CG   . ARG   C 1 35  ? -34.928 16.484  41.194  1.00 20.09 ? 14  ARG   C CG   1 
ATOM   3983 C  CD   . ARG   C 1 35  ? -33.865 16.784  40.157  1.00 19.82 ? 14  ARG   C CD   1 
ATOM   3984 N  NE   . ARG   C 1 35  ? -34.293 16.414  38.801  1.00 19.83 ? 14  ARG   C NE   1 
ATOM   3985 C  CZ   . ARG   C 1 35  ? -34.869 17.207  37.906  1.00 20.17 ? 14  ARG   C CZ   1 
ATOM   3986 N  NH1  . ARG   C 1 35  ? -35.191 18.468  38.216  1.00 20.08 ? 14  ARG   C NH1  1 
ATOM   3987 N  NH2  . ARG   C 1 35  ? -35.165 16.724  36.703  1.00 20.72 ? 14  ARG   C NH2  1 
ATOM   3988 N  N    . ILE   C 1 36  ? -37.141 12.765  41.269  1.00 17.18 ? 15  ILE   C N    1 
ATOM   3989 C  CA   . ILE   C 1 36  ? -38.072 11.654  41.149  1.00 16.66 ? 15  ILE   C CA   1 
ATOM   3990 C  C    . ILE   C 1 36  ? -37.632 10.482  42.032  1.00 15.57 ? 15  ILE   C C    1 
ATOM   3991 O  O    . ILE   C 1 36  ? -38.469 9.849   42.673  1.00 15.27 ? 15  ILE   C O    1 
ATOM   3992 C  CB   . ILE   C 1 36  ? -38.260 11.276  39.666  1.00 17.55 ? 15  ILE   C CB   1 
ATOM   3993 C  CG1  . ILE   C 1 36  ? -39.085 12.359  38.957  1.00 18.92 ? 15  ILE   C CG1  1 
ATOM   3994 C  CG2  . ILE   C 1 36  ? -38.888 9.890   39.498  1.00 18.32 ? 15  ILE   C CG2  1 
ATOM   3995 C  CD1  . ILE   C 1 36  ? -39.094 12.216  37.446  1.00 18.80 ? 15  ILE   C CD1  1 
ATOM   3996 N  N    . GLY   C 1 37  ? -36.327 10.194  42.045  1.00 15.40 ? 16  GLY   C N    1 
ATOM   3997 C  CA   . GLY   C 1 37  ? -35.830 9.076   42.843  1.00 16.42 ? 16  GLY   C CA   1 
ATOM   3998 C  C    . GLY   C 1 37  ? -36.115 9.274   44.336  1.00 14.85 ? 16  GLY   C C    1 
ATOM   3999 O  O    . GLY   C 1 37  ? -36.514 8.337   45.025  1.00 15.70 ? 16  GLY   C O    1 
ATOM   4000 N  N    . ARG   C 1 38  ? -35.991 10.526  44.805  1.00 15.06 ? 17  ARG   C N    1 
ATOM   4001 C  CA   . ARG   C 1 38  ? -36.340 10.845  46.183  1.00 16.26 ? 17  ARG   C CA   1 
ATOM   4002 C  C    . ARG   C 1 38  ? -37.821 10.581  46.446  1.00 16.12 ? 17  ARG   C C    1 
ATOM   4003 O  O    . ARG   C 1 38  ? -38.176 9.955   47.440  1.00 17.44 ? 17  ARG   C O    1 
ATOM   4004 C  CB   . ARG   C 1 38  ? -35.975 12.299  46.477  1.00 17.72 ? 17  ARG   C CB   1 
ATOM   4005 C  CG   . ARG   C 1 38  ? -36.235 12.623  47.939  1.00 21.49 ? 17  ARG   C CG   1 
ATOM   4006 C  CD   . ARG   C 1 38  ? -35.878 14.110  48.048  1.00 23.69 ? 17  ARG   C CD   1 
ATOM   4007 N  NE   . ARG   C 1 38  ? -35.482 14.471  49.413  1.00 30.85 ? 17  ARG   C NE   1 
ATOM   4008 C  CZ   . ARG   C 1 38  ? -36.312 14.538  50.450  1.00 31.55 ? 17  ARG   C CZ   1 
ATOM   4009 N  NH1  . ARG   C 1 38  ? -35.841 14.864  51.645  1.00 29.99 ? 17  ARG   C NH1  1 
ATOM   4010 N  NH2  . ARG   C 1 38  ? -37.599 14.279  50.291  1.00 32.85 ? 17  ARG   C NH2  1 
ATOM   4011 N  N    . ALA   C 1 39  ? -38.697 11.003  45.531  1.00 15.49 ? 18  ALA   C N    1 
ATOM   4012 C  CA   . ALA   C 1 39  ? -40.120 10.780  45.739  1.00 15.67 ? 18  ALA   C CA   1 
ATOM   4013 C  C    . ALA   C 1 39  ? -40.475 9.295   45.767  1.00 16.18 ? 18  ALA   C C    1 
ATOM   4014 O  O    . ALA   C 1 39  ? -41.347 8.869   46.521  1.00 16.94 ? 18  ALA   C O    1 
ATOM   4015 C  CB   . ALA   C 1 39  ? -40.909 11.524  44.678  1.00 16.24 ? 18  ALA   C CB   1 
ATOM   4016 N  N    . ILE   C 1 40  ? -39.783 8.503   44.929  1.00 15.21 ? 19  ILE   C N    1 
ATOM   4017 C  CA   . ILE   C 1 40  ? -40.007 7.063   44.922  1.00 15.08 ? 19  ILE   C CA   1 
ATOM   4018 C  C    . ILE   C 1 40  ? -39.590 6.457   46.271  1.00 15.20 ? 19  ILE   C C    1 
ATOM   4019 O  O    . ILE   C 1 40  ? -40.307 5.616   46.820  1.00 16.70 ? 19  ILE   C O    1 
ATOM   4020 C  CB   . ILE   C 1 40  ? -39.293 6.420   43.715  1.00 14.22 ? 19  ILE   C CB   1 
ATOM   4021 C  CG1  . ILE   C 1 40  ? -39.958 6.844   42.396  1.00 14.82 ? 19  ILE   C CG1  1 
ATOM   4022 C  CG2  . ILE   C 1 40  ? -39.289 4.890   43.837  1.00 14.23 ? 19  ILE   C CG2  1 
ATOM   4023 C  CD1  . ILE   C 1 40  ? -39.104 6.576   41.165  1.00 16.43 ? 19  ILE   C CD1  1 
ATOM   4024 N  N    . ALA   C 1 41  ? -38.378 6.807   46.736  1.00 15.95 ? 20  ALA   C N    1 
ATOM   4025 C  CA   . ALA   C 1 41  ? -37.868 6.297   48.004  1.00 15.69 ? 20  ALA   C CA   1 
ATOM   4026 C  C    . ALA   C 1 41  ? -38.821 6.620   49.150  1.00 16.70 ? 20  ALA   C C    1 
ATOM   4027 O  O    . ALA   C 1 41  ? -39.123 5.741   49.957  1.00 16.99 ? 20  ALA   C O    1 
ATOM   4028 C  CB   . ALA   C 1 41  ? -36.467 6.816   48.266  1.00 16.60 ? 20  ALA   C CB   1 
ATOM   4029 N  N    . VAL   C 1 42  ? -39.287 7.881   49.166  1.00 16.57 ? 21  VAL   C N    1 
ATOM   4030 C  CA   . VAL   C 1 42  ? -40.222 8.340   50.184  1.00 17.91 ? 21  VAL   C CA   1 
ATOM   4031 C  C    . VAL   C 1 42  ? -41.512 7.531   50.125  1.00 18.49 ? 21  VAL   C C    1 
ATOM   4032 O  O    . VAL   C 1 42  ? -42.004 7.071   51.151  1.00 18.33 ? 21  VAL   C O    1 
ATOM   4033 C  CB   . VAL   C 1 42  ? -40.484 9.855   50.075  1.00 18.37 ? 21  VAL   C CB   1 
ATOM   4034 C  CG1  . VAL   C 1 42  ? -41.691 10.281  50.922  1.00 18.71 ? 21  VAL   C CG1  1 
ATOM   4035 C  CG2  . VAL   C 1 42  ? -39.250 10.655  50.456  1.00 19.59 ? 21  VAL   C CG2  1 
ATOM   4036 N  N    . LYS   C 1 43  ? -42.089 7.362   48.922  1.00 18.63 ? 22  LYS   C N    1 
ATOM   4037 C  CA   A LYS   C 1 43  ? -43.360 6.667   48.830  0.70 17.69 ? 22  LYS   C CA   1 
ATOM   4038 C  CA   B LYS   C 1 43  ? -43.351 6.652   48.786  0.30 18.22 ? 22  LYS   C CA   1 
ATOM   4039 C  C    . LYS   C 1 43  ? -43.205 5.180   49.172  1.00 17.73 ? 22  LYS   C C    1 
ATOM   4040 O  O    . LYS   C 1 43  ? -44.075 4.610   49.825  1.00 19.86 ? 22  LYS   C O    1 
ATOM   4041 C  CB   A LYS   C 1 43  ? -44.053 6.934   47.485  0.70 19.73 ? 22  LYS   C CB   1 
ATOM   4042 C  CB   B LYS   C 1 43  ? -43.959 6.813   47.387  0.30 19.20 ? 22  LYS   C CB   1 
ATOM   4043 C  CG   A LYS   C 1 43  ? -45.557 6.670   47.512  0.70 22.18 ? 22  LYS   C CG   1 
ATOM   4044 C  CG   B LYS   C 1 43  ? -44.875 8.016   47.278  0.30 20.34 ? 22  LYS   C CG   1 
ATOM   4045 C  CD   A LYS   C 1 43  ? -46.310 7.227   46.302  0.70 26.64 ? 22  LYS   C CD   1 
ATOM   4046 C  CD   B LYS   C 1 43  ? -45.897 7.929   46.151  0.30 22.67 ? 22  LYS   C CD   1 
ATOM   4047 C  CE   A LYS   C 1 43  ? -46.326 8.724   46.178  0.70 27.54 ? 22  LYS   C CE   1 
ATOM   4048 C  CE   B LYS   C 1 43  ? -47.147 8.656   46.518  0.30 25.07 ? 22  LYS   C CE   1 
ATOM   4049 N  NZ   A LYS   C 1 43  ? -47.314 9.365   47.056  0.70 31.35 ? 22  LYS   C NZ   1 
ATOM   4050 N  NZ   B LYS   C 1 43  ? -47.849 7.990   47.619  0.30 26.99 ? 22  LYS   C NZ   1 
ATOM   4051 N  N    . LEU   C 1 44  ? -42.116 4.533   48.733  1.00 17.06 ? 23  LEU   C N    1 
ATOM   4052 C  CA   . LEU   C 1 44  ? -41.872 3.150   49.127  1.00 16.12 ? 23  LEU   C CA   1 
ATOM   4053 C  C    . LEU   C 1 44  ? -41.766 3.062   50.659  1.00 16.17 ? 23  LEU   C C    1 
ATOM   4054 O  O    . LEU   C 1 44  ? -42.322 2.144   51.276  1.00 16.66 ? 23  LEU   C O    1 
ATOM   4055 C  CB   . LEU   C 1 44  ? -40.576 2.647   48.479  1.00 15.57 ? 23  LEU   C CB   1 
ATOM   4056 C  CG   . LEU   C 1 44  ? -40.687 2.301   46.987  1.00 16.04 ? 23  LEU   C CG   1 
ATOM   4057 C  CD1  . LEU   C 1 44  ? -39.293 2.028   46.441  1.00 16.30 ? 23  LEU   C CD1  1 
ATOM   4058 C  CD2  . LEU   C 1 44  ? -41.574 1.085   46.792  1.00 18.61 ? 23  LEU   C CD2  1 
ATOM   4059 N  N    . HIS   C 1 45  ? -41.060 4.026   51.257  1.00 17.66 ? 24  HIS   C N    1 
ATOM   4060 C  CA   . HIS   C 1 45  ? -40.876 4.027   52.707  1.00 17.46 ? 24  HIS   C CA   1 
ATOM   4061 C  C    . HIS   C 1 45  ? -42.232 4.168   53.408  1.00 19.29 ? 24  HIS   C C    1 
ATOM   4062 O  O    . HIS   C 1 45  ? -42.486 3.516   54.427  1.00 19.32 ? 24  HIS   C O    1 
ATOM   4063 C  CB   . HIS   C 1 45  ? -39.870 5.108   53.110  1.00 18.33 ? 24  HIS   C CB   1 
ATOM   4064 C  CG   . HIS   C 1 45  ? -39.491 5.016   54.557  1.00 18.14 ? 24  HIS   C CG   1 
ATOM   4065 N  ND1  . HIS   C 1 45  ? -40.176 5.707   55.538  1.00 21.23 ? 24  HIS   C ND1  1 
ATOM   4066 C  CD2  . HIS   C 1 45  ? -38.537 4.284   55.183  1.00 18.61 ? 24  HIS   C CD2  1 
ATOM   4067 C  CE1  . HIS   C 1 45  ? -39.629 5.422   56.721  1.00 20.07 ? 24  HIS   C CE1  1 
ATOM   4068 N  NE2  . HIS   C 1 45  ? -38.639 4.558   56.532  1.00 19.91 ? 24  HIS   C NE2  1 
ATOM   4069 N  N    . GLN   C 1 46  ? -43.082 5.061   52.880  1.00 20.04 ? 25  GLN   C N    1 
ATOM   4070 C  CA   . GLN   C 1 46  ? -44.383 5.314   53.492  1.00 21.26 ? 25  GLN   C CA   1 
ATOM   4071 C  C    . GLN   C 1 46  ? -45.288 4.092   53.380  1.00 22.93 ? 25  GLN   C C    1 
ATOM   4072 O  O    . GLN   C 1 46  ? -46.220 3.950   54.168  1.00 24.57 ? 25  GLN   C O    1 
ATOM   4073 C  CB   . GLN   C 1 46  ? -45.078 6.519   52.861  1.00 20.70 ? 25  GLN   C CB   1 
ATOM   4074 C  CG   . GLN   C 1 46  ? -44.393 7.846   53.166  1.00 22.67 ? 25  GLN   C CG   1 
ATOM   4075 C  CD   . GLN   C 1 46  ? -44.894 9.026   52.365  1.00 28.01 ? 25  GLN   C CD   1 
ATOM   4076 O  OE1  . GLN   C 1 46  ? -45.495 8.876   51.294  1.00 30.44 ? 25  GLN   C OE1  1 
ATOM   4077 N  NE2  . GLN   C 1 46  ? -44.589 10.218  52.857  1.00 28.86 ? 25  GLN   C NE2  1 
ATOM   4078 N  N    . THR   C 1 47  ? -45.037 3.234   52.384  1.00 21.62 ? 26  THR   C N    1 
ATOM   4079 C  CA   . THR   C 1 47  ? -45.823 2.039   52.117  1.00 21.68 ? 26  THR   C CA   1 
ATOM   4080 C  C    . THR   C 1 47  ? -45.329 0.902   53.014  1.00 22.08 ? 26  THR   C C    1 
ATOM   4081 O  O    . THR   C 1 47  ? -45.973 -0.143  53.106  1.00 25.43 ? 26  THR   C O    1 
ATOM   4082 C  CB   . THR   C 1 47  ? -45.688 1.711   50.623  1.00 24.98 ? 26  THR   C CB   1 
ATOM   4083 O  OG1  . THR   C 1 47  ? -46.183 2.833   49.894  1.00 25.93 ? 26  THR   C OG1  1 
ATOM   4084 C  CG2  . THR   C 1 47  ? -46.476 0.489   50.185  1.00 28.68 ? 26  THR   C CG2  1 
ATOM   4085 N  N    . GLY   C 1 48  ? -44.162 1.085   53.657  1.00 20.79 ? 27  GLY   C N    1 
ATOM   4086 C  CA   . GLY   C 1 48  ? -43.675 0.094   54.608  1.00 21.08 ? 27  GLY   C CA   1 
ATOM   4087 C  C    . GLY   C 1 48  ? -42.326 -0.537  54.255  1.00 21.23 ? 27  GLY   C C    1 
ATOM   4088 O  O    . GLY   C 1 48  ? -41.897 -1.457  54.942  1.00 22.43 ? 27  GLY   C O    1 
ATOM   4089 N  N    . TYR   C 1 49  ? -41.682 -0.083  53.169  1.00 19.58 ? 28  TYR   C N    1 
ATOM   4090 C  CA   . TYR   C 1 49  ? -40.396 -0.637  52.782  1.00 18.60 ? 28  TYR   C CA   1 
ATOM   4091 C  C    . TYR   C 1 49  ? -39.262 0.023   53.558  1.00 16.76 ? 28  TYR   C C    1 
ATOM   4092 O  O    . TYR   C 1 49  ? -39.320 1.226   53.832  1.00 18.29 ? 28  TYR   C O    1 
ATOM   4093 C  CB   . TYR   C 1 49  ? -40.087 -0.373  51.299  1.00 17.91 ? 28  TYR   C CB   1 
ATOM   4094 C  CG   . TYR   C 1 49  ? -40.880 -1.275  50.370  1.00 18.80 ? 28  TYR   C CG   1 
ATOM   4095 C  CD1  . TYR   C 1 49  ? -42.195 -0.964  50.019  1.00 21.10 ? 28  TYR   C CD1  1 
ATOM   4096 C  CD2  . TYR   C 1 49  ? -40.320 -2.445  49.869  1.00 19.20 ? 28  TYR   C CD2  1 
ATOM   4097 C  CE1  . TYR   C 1 49  ? -42.932 -1.796  49.191  1.00 21.99 ? 28  TYR   C CE1  1 
ATOM   4098 C  CE2  . TYR   C 1 49  ? -41.052 -3.286  49.046  1.00 22.22 ? 28  TYR   C CE2  1 
ATOM   4099 C  CZ   . TYR   C 1 49  ? -42.357 -2.961  48.717  1.00 21.82 ? 28  TYR   C CZ   1 
ATOM   4100 O  OH   . TYR   C 1 49  ? -43.060 -3.802  47.900  1.00 24.22 ? 28  TYR   C OH   1 
ATOM   4101 N  N    . ARG   C 1 50  ? -38.210 -0.771  53.802  1.00 17.16 ? 29  ARG   C N    1 
ATOM   4102 C  CA   . ARG   C 1 50  ? -36.890 -0.273  54.174  1.00 16.92 ? 29  ARG   C CA   1 
ATOM   4103 C  C    . ARG   C 1 50  ? -36.172 0.033   52.862  1.00 16.52 ? 29  ARG   C C    1 
ATOM   4104 O  O    . ARG   C 1 50  ? -36.405 -0.666  51.864  1.00 18.23 ? 29  ARG   C O    1 
ATOM   4105 C  CB   . ARG   C 1 50  ? -36.140 -1.349  54.969  1.00 17.31 ? 29  ARG   C CB   1 
ATOM   4106 C  CG   . ARG   C 1 50  ? -36.836 -1.552  56.308  1.00 17.96 ? 29  ARG   C CG   1 
ATOM   4107 C  CD   . ARG   C 1 50  ? -36.181 -2.637  57.128  1.00 22.03 ? 29  ARG   C CD   1 
ATOM   4108 N  NE   . ARG   C 1 50  ? -36.386 -3.998  56.623  1.00 21.61 ? 29  ARG   C NE   1 
ATOM   4109 C  CZ   . ARG   C 1 50  ? -35.763 -5.049  57.132  1.00 22.60 ? 29  ARG   C CZ   1 
ATOM   4110 N  NH1  . ARG   C 1 50  ? -34.843 -4.895  58.079  1.00 22.48 ? 29  ARG   C NH1  1 
ATOM   4111 N  NH2  . ARG   C 1 50  ? -36.064 -6.261  56.695  1.00 24.30 ? 29  ARG   C NH2  1 
ATOM   4112 N  N    . VAL   C 1 51  ? -35.385 1.115   52.838  1.00 16.37 ? 30  VAL   C N    1 
ATOM   4113 C  CA   A VAL   C 1 51  ? -34.879 1.609   51.560  0.70 15.74 ? 30  VAL   C CA   1 
ATOM   4114 C  CA   B VAL   C 1 51  ? -34.889 1.630   51.568  0.30 16.16 ? 30  VAL   C CA   1 
ATOM   4115 C  C    . VAL   C 1 51  ? -33.373 1.829   51.599  1.00 16.33 ? 30  VAL   C C    1 
ATOM   4116 O  O    . VAL   C 1 51  ? -32.836 2.344   52.569  1.00 16.24 ? 30  VAL   C O    1 
ATOM   4117 C  CB   A VAL   C 1 51  ? -35.563 2.890   51.044  0.70 15.60 ? 30  VAL   C CB   1 
ATOM   4118 C  CB   B VAL   C 1 51  ? -35.638 2.930   51.199  0.30 16.38 ? 30  VAL   C CB   1 
ATOM   4119 C  CG1  A VAL   C 1 51  ? -37.057 2.658   50.831  0.70 13.73 ? 30  VAL   C CG1  1 
ATOM   4120 C  CG1  B VAL   C 1 51  ? -35.699 3.941   52.342  0.30 16.80 ? 30  VAL   C CG1  1 
ATOM   4121 C  CG2  A VAL   C 1 51  ? -35.314 4.113   51.924  0.70 17.42 ? 30  VAL   C CG2  1 
ATOM   4122 C  CG2  B VAL   C 1 51  ? -35.123 3.574   49.917  0.30 16.09 ? 30  VAL   C CG2  1 
ATOM   4123 N  N    . VAL   C 1 52  ? -32.717 1.472   50.484  1.00 14.28 ? 31  VAL   C N    1 
ATOM   4124 C  CA   . VAL   C 1 52  ? -31.348 1.865   50.191  1.00 14.22 ? 31  VAL   C CA   1 
ATOM   4125 C  C    . VAL   C 1 52  ? -31.415 3.049   49.247  1.00 14.33 ? 31  VAL   C C    1 
ATOM   4126 O  O    . VAL   C 1 52  ? -31.943 2.921   48.138  1.00 15.29 ? 31  VAL   C O    1 
ATOM   4127 C  CB   . VAL   C 1 52  ? -30.528 0.749   49.531  1.00 13.09 ? 31  VAL   C CB   1 
ATOM   4128 C  CG1  . VAL   C 1 52  ? -29.137 1.248   49.131  1.00 15.17 ? 31  VAL   C CG1  1 
ATOM   4129 C  CG2  . VAL   C 1 52  ? -30.435 -0.461  50.435  1.00 15.61 ? 31  VAL   C CG2  1 
ATOM   4130 N  N    . ILE   C 1 53  ? -30.901 4.185   49.702  1.00 15.50 ? 32  ILE   C N    1 
ATOM   4131 C  CA   . ILE   C 1 53  ? -30.824 5.399   48.915  1.00 15.59 ? 32  ILE   C CA   1 
ATOM   4132 C  C    . ILE   C 1 53  ? -29.461 5.431   48.237  1.00 15.63 ? 32  ILE   C C    1 
ATOM   4133 O  O    . ILE   C 1 53  ? -28.451 5.779   48.853  1.00 16.35 ? 32  ILE   C O    1 
ATOM   4134 C  CB   . ILE   C 1 53  ? -30.998 6.602   49.849  1.00 16.07 ? 32  ILE   C CB   1 
ATOM   4135 C  CG1  . ILE   C 1 53  ? -32.336 6.549   50.561  1.00 16.36 ? 32  ILE   C CG1  1 
ATOM   4136 C  CG2  . ILE   C 1 53  ? -30.785 7.932   49.115  1.00 16.92 ? 32  ILE   C CG2  1 
ATOM   4137 C  CD1  . ILE   C 1 53  ? -32.311 7.256   51.907  1.00 17.69 ? 32  ILE   C CD1  1 
ATOM   4138 N  N    . HIS   C 1 54  ? -29.425 5.052   46.959  1.00 14.72 ? 33  HIS   C N    1 
ATOM   4139 C  CA   . HIS   C 1 54  ? -28.185 5.146   46.213  1.00 14.10 ? 33  HIS   C CA   1 
ATOM   4140 C  C    . HIS   C 1 54  ? -28.011 6.591   45.733  1.00 14.97 ? 33  HIS   C C    1 
ATOM   4141 O  O    . HIS   C 1 54  ? -28.977 7.283   45.388  1.00 15.63 ? 33  HIS   C O    1 
ATOM   4142 C  CB   . HIS   C 1 54  ? -28.144 4.138   45.053  1.00 14.97 ? 33  HIS   C CB   1 
ATOM   4143 C  CG   . HIS   C 1 54  ? -27.165 4.581   44.019  1.00 14.98 ? 33  HIS   C CG   1 
ATOM   4144 N  ND1  . HIS   C 1 54  ? -27.556 5.427   43.001  1.00 15.62 ? 33  HIS   C ND1  1 
ATOM   4145 C  CD2  . HIS   C 1 54  ? -25.836 4.419   43.888  1.00 16.09 ? 33  HIS   C CD2  1 
ATOM   4146 C  CE1  . HIS   C 1 54  ? -26.500 5.724   42.250  1.00 15.40 ? 33  HIS   C CE1  1 
ATOM   4147 N  NE2  . HIS   C 1 54  ? -25.444 5.120   42.777  1.00 16.42 ? 33  HIS   C NE2  1 
ATOM   4148 N  N    . TYR   C 1 55  ? -26.757 7.054   45.718  1.00 14.95 ? 34  TYR   C N    1 
ATOM   4149 C  CA   . TYR   C 1 55  ? -26.468 8.357   45.141  1.00 14.67 ? 34  TYR   C CA   1 
ATOM   4150 C  C    . TYR   C 1 55  ? -25.070 8.325   44.525  1.00 15.98 ? 34  TYR   C C    1 
ATOM   4151 O  O    . TYR   C 1 55  ? -24.288 7.406   44.770  1.00 16.06 ? 34  TYR   C O    1 
ATOM   4152 C  CB   . TYR   C 1 55  ? -26.625 9.454   46.211  1.00 16.04 ? 34  TYR   C CB   1 
ATOM   4153 C  CG   . TYR   C 1 55  ? -25.437 9.513   47.161  1.00 15.57 ? 34  TYR   C CG   1 
ATOM   4154 C  CD1  . TYR   C 1 55  ? -25.355 8.684   48.278  1.00 16.53 ? 34  TYR   C CD1  1 
ATOM   4155 C  CD2  . TYR   C 1 55  ? -24.351 10.344  46.874  1.00 16.04 ? 34  TYR   C CD2  1 
ATOM   4156 C  CE1  . TYR   C 1 55  ? -24.237 8.696   49.099  1.00 16.90 ? 34  TYR   C CE1  1 
ATOM   4157 C  CE2  . TYR   C 1 55  ? -23.231 10.379  47.692  1.00 17.92 ? 34  TYR   C CE2  1 
ATOM   4158 C  CZ   . TYR   C 1 55  ? -23.180 9.551   48.805  1.00 17.52 ? 34  TYR   C CZ   1 
ATOM   4159 O  OH   . TYR   C 1 55  ? -22.072 9.606   49.597  1.00 19.53 ? 34  TYR   C OH   1 
ATOM   4160 N  N    . HIS   C 1 56  ? -24.752 9.370   43.748  1.00 16.36 ? 35  HIS   C N    1 
ATOM   4161 C  CA   . HIS   C 1 56  ? -23.444 9.516   43.147  1.00 16.86 ? 35  HIS   C CA   1 
ATOM   4162 C  C    . HIS   C 1 56  ? -22.741 10.716  43.780  1.00 17.24 ? 35  HIS   C C    1 
ATOM   4163 O  O    . HIS   C 1 56  ? -21.812 10.537  44.566  1.00 18.30 ? 35  HIS   C O    1 
ATOM   4164 C  CB   . HIS   C 1 56  ? -23.568 9.605   41.623  1.00 18.76 ? 35  HIS   C CB   1 
ATOM   4165 C  CG   . HIS   C 1 56  ? -22.247 9.778   40.964  1.00 20.19 ? 35  HIS   C CG   1 
ATOM   4166 N  ND1  . HIS   C 1 56  ? -22.139 10.534  39.818  1.00 22.92 ? 35  HIS   C ND1  1 
ATOM   4167 C  CD2  . HIS   C 1 56  ? -21.018 9.352   41.265  1.00 22.01 ? 35  HIS   C CD2  1 
ATOM   4168 C  CE1  . HIS   C 1 56  ? -20.870 10.542  39.429  1.00 22.42 ? 35  HIS   C CE1  1 
ATOM   4169 N  NE2  . HIS   C 1 56  ? -20.169 9.833   40.292  1.00 22.79 ? 35  HIS   C NE2  1 
ATOM   4170 N  N    . ASN   C 1 57  ? -23.216 11.927  43.477  1.00 19.17 ? 36  ASN   C N    1 
ATOM   4171 C  CA   . ASN   C 1 57  ? -22.575 13.135  43.985  1.00 20.48 ? 36  ASN   C CA   1 
ATOM   4172 C  C    . ASN   C 1 57  ? -23.346 13.798  45.127  1.00 20.47 ? 36  ASN   C C    1 
ATOM   4173 O  O    . ASN   C 1 57  ? -22.742 14.576  45.882  1.00 22.84 ? 36  ASN   C O    1 
ATOM   4174 C  CB   . ASN   C 1 57  ? -22.405 14.194  42.901  1.00 22.25 ? 36  ASN   C CB   1 
ATOM   4175 C  CG   . ASN   C 1 57  ? -21.429 13.773  41.825  1.00 27.43 ? 36  ASN   C CG   1 
ATOM   4176 O  OD1  . ASN   C 1 57  ? -20.383 13.190  42.126  1.00 30.64 ? 36  ASN   C OD1  1 
ATOM   4177 N  ND2  . ASN   C 1 57  ? -21.765 14.038  40.568  1.00 30.92 ? 36  ASN   C ND2  1 
ATOM   4178 N  N    . SER   C 1 58  ? -24.652 13.537  45.266  1.00 18.60 ? 37  SER   C N    1 
ATOM   4179 C  CA   . SER   C 1 58  ? -25.484 14.312  46.181  1.00 18.93 ? 37  SER   C CA   1 
ATOM   4180 C  C    . SER   C 1 58  ? -25.474 13.704  47.587  1.00 18.49 ? 37  SER   C C    1 
ATOM   4181 O  O    . SER   C 1 58  ? -26.519 13.269  48.081  1.00 17.92 ? 37  SER   C O    1 
ATOM   4182 C  CB   . SER   C 1 58  ? -26.901 14.456  45.652  1.00 20.26 ? 37  SER   C CB   1 
ATOM   4183 O  OG   . SER   C 1 58  ? -26.909 15.169  44.419  1.00 20.81 ? 37  SER   C OG   1 
ATOM   4184 N  N    . ALA   C 1 59  ? -24.302 13.758  48.243  1.00 19.24 ? 38  ALA   C N    1 
ATOM   4185 C  CA   . ALA   C 1 59  ? -24.096 13.104  49.534  1.00 20.27 ? 38  ALA   C CA   1 
ATOM   4186 C  C    . ALA   C 1 59  ? -24.941 13.725  50.645  1.00 20.20 ? 38  ALA   C C    1 
ATOM   4187 O  O    . ALA   C 1 59  ? -25.607 13.003  51.396  1.00 20.82 ? 38  ALA   C O    1 
ATOM   4188 C  CB   . ALA   C 1 59  ? -22.623 13.069  49.889  1.00 20.15 ? 38  ALA   C CB   1 
ATOM   4189 N  N    . GLU   C 1 60  ? -24.939 15.064  50.715  1.00 22.22 ? 39  GLU   C N    1 
ATOM   4190 C  CA   A GLU   C 1 60  ? -25.676 15.787  51.738  0.60 23.52 ? 39  GLU   C CA   1 
ATOM   4191 C  CA   B GLU   C 1 60  ? -25.677 15.799  51.729  0.40 22.32 ? 39  GLU   C CA   1 
ATOM   4192 C  C    . GLU   C 1 60  ? -27.166 15.474  51.643  1.00 20.53 ? 39  GLU   C C    1 
ATOM   4193 O  O    . GLU   C 1 60  ? -27.801 15.180  52.650  1.00 20.61 ? 39  GLU   C O    1 
ATOM   4194 C  CB   A GLU   C 1 60  ? -25.366 17.285  51.707  0.60 26.97 ? 39  GLU   C CB   1 
ATOM   4195 C  CB   B GLU   C 1 60  ? -25.426 17.302  51.605  0.40 23.83 ? 39  GLU   C CB   1 
ATOM   4196 C  CG   A GLU   C 1 60  ? -23.931 17.603  52.116  0.60 31.52 ? 39  GLU   C CG   1 
ATOM   4197 C  CG   B GLU   C 1 60  ? -26.184 18.122  52.644  0.40 25.87 ? 39  GLU   C CG   1 
ATOM   4198 C  CD   A GLU   C 1 60  ? -23.695 19.081  52.381  0.60 37.37 ? 39  GLU   C CD   1 
ATOM   4199 C  CD   B GLU   C 1 60  ? -25.894 19.606  52.516  0.40 28.45 ? 39  GLU   C CD   1 
ATOM   4200 O  OE1  A GLU   C 1 60  ? -24.238 19.591  53.382  0.60 41.23 ? 39  GLU   C OE1  1 
ATOM   4201 O  OE1  B GLU   C 1 60  ? -24.912 19.963  51.827  0.40 28.06 ? 39  GLU   C OE1  1 
ATOM   4202 O  OE2  A GLU   C 1 60  ? -22.983 19.728  51.584  0.60 40.45 ? 39  GLU   C OE2  1 
ATOM   4203 O  OE2  B GLU   C 1 60  ? -26.660 20.398  53.096  0.40 29.79 ? 39  GLU   C OE2  1 
ATOM   4204 N  N    . ALA   C 1 61  ? -27.724 15.513  50.417  1.00 19.68 ? 40  ALA   C N    1 
ATOM   4205 C  CA   . ALA   C 1 61  ? -29.141 15.249  50.244  1.00 18.36 ? 40  ALA   C CA   1 
ATOM   4206 C  C    . ALA   C 1 61  ? -29.497 13.795  50.564  1.00 18.30 ? 40  ALA   C C    1 
ATOM   4207 O  O    . ALA   C 1 61  ? -30.573 13.533  51.093  1.00 19.18 ? 40  ALA   C O    1 
ATOM   4208 C  CB   . ALA   C 1 61  ? -29.576 15.638  48.835  1.00 19.31 ? 40  ALA   C CB   1 
ATOM   4209 N  N    . ALA   C 1 62  ? -28.607 12.862  50.208  1.00 18.53 ? 41  ALA   C N    1 
ATOM   4210 C  CA   . ALA   C 1 62  ? -28.851 11.454  50.474  1.00 17.56 ? 41  ALA   C CA   1 
ATOM   4211 C  C    . ALA   C 1 62  ? -28.924 11.211  51.985  1.00 17.85 ? 41  ALA   C C    1 
ATOM   4212 O  O    . ALA   C 1 62  ? -29.852 10.552  52.482  1.00 18.29 ? 41  ALA   C O    1 
ATOM   4213 C  CB   . ALA   C 1 62  ? -27.781 10.615  49.821  1.00 17.33 ? 41  ALA   C CB   1 
ATOM   4214 N  N    . VAL   C 1 63  ? -27.949 11.779  52.702  1.00 19.03 ? 42  VAL   C N    1 
ATOM   4215 C  CA   . VAL   C 1 63  ? -27.884 11.570  54.141  1.00 19.64 ? 42  VAL   C CA   1 
ATOM   4216 C  C    . VAL   C 1 63  ? -29.066 12.241  54.837  1.00 19.78 ? 42  VAL   C C    1 
ATOM   4217 O  O    . VAL   C 1 63  ? -29.653 11.680  55.761  1.00 21.50 ? 42  VAL   C O    1 
ATOM   4218 C  CB   . VAL   C 1 63  ? -26.518 12.020  54.688  1.00 20.74 ? 42  VAL   C CB   1 
ATOM   4219 C  CG1  . VAL   C 1 63  ? -26.512 12.024  56.216  1.00 22.55 ? 42  VAL   C CG1  1 
ATOM   4220 C  CG2  . VAL   C 1 63  ? -25.407 11.120  54.154  1.00 21.79 ? 42  VAL   C CG2  1 
ATOM   4221 N  N    . SER   C 1 64  ? -29.437 13.435  54.360  1.00 19.79 ? 43  SER   C N    1 
ATOM   4222 C  CA   . SER   C 1 64  ? -30.573 14.126  54.941  1.00 21.76 ? 43  SER   C CA   1 
ATOM   4223 C  C    . SER   C 1 64  ? -31.857 13.318  54.737  1.00 22.15 ? 43  SER   C C    1 
ATOM   4224 O  O    . SER   C 1 64  ? -32.724 13.252  55.607  1.00 21.74 ? 43  SER   C O    1 
ATOM   4225 C  CB   . SER   C 1 64  ? -30.654 15.531  54.375  1.00 25.71 ? 43  SER   C CB   1 
ATOM   4226 O  OG   . SER   C 1 64  ? -31.867 16.143  54.782  1.00 32.68 ? 43  SER   C OG   1 
ATOM   4227 N  N    . LEU   C 1 65  ? -31.978 12.656  53.576  1.00 20.13 ? 44  LEU   C N    1 
ATOM   4228 C  CA   . LEU   C 1 65  ? -33.153 11.839  53.338  1.00 18.71 ? 44  LEU   C CA   1 
ATOM   4229 C  C    . LEU   C 1 65  ? -33.163 10.635  54.276  1.00 18.72 ? 44  LEU   C C    1 
ATOM   4230 O  O    . LEU   C 1 65  ? -34.204 10.304  54.848  1.00 19.57 ? 44  LEU   C O    1 
ATOM   4231 C  CB   . LEU   C 1 65  ? -33.221 11.387  51.877  1.00 20.07 ? 44  LEU   C CB   1 
ATOM   4232 C  CG   . LEU   C 1 65  ? -34.382 10.443  51.547  1.00 19.21 ? 44  LEU   C CG   1 
ATOM   4233 C  CD1  . LEU   C 1 65  ? -35.748 11.073  51.836  1.00 20.88 ? 44  LEU   C CD1  1 
ATOM   4234 C  CD2  . LEU   C 1 65  ? -34.272 10.001  50.073  1.00 21.44 ? 44  LEU   C CD2  1 
ATOM   4235 N  N    . ALA   C 1 66  ? -32.005 9.967   54.394  1.00 18.66 ? 45  ALA   C N    1 
ATOM   4236 C  CA   . ALA   C 1 66  ? -31.905 8.814   55.281  1.00 19.35 ? 45  ALA   C CA   1 
ATOM   4237 C  C    . ALA   C 1 66  ? -32.270 9.214   56.712  1.00 20.10 ? 45  ALA   C C    1 
ATOM   4238 O  O    . ALA   C 1 66  ? -33.022 8.497   57.375  1.00 21.64 ? 45  ALA   C O    1 
ATOM   4239 C  CB   . ALA   C 1 66  ? -30.521 8.197   55.213  1.00 21.01 ? 45  ALA   C CB   1 
ATOM   4240 N  N    . ASP   C 1 67  ? -31.792 10.388  57.139  1.00 20.88 ? 46  ASP   C N    1 
ATOM   4241 C  CA   . ASP   C 1 67  ? -32.098 10.913  58.466  1.00 23.14 ? 46  ASP   C CA   1 
ATOM   4242 C  C    . ASP   C 1 67  ? -33.613 11.070  58.638  1.00 23.32 ? 46  ASP   C C    1 
ATOM   4243 O  O    . ASP   C 1 67  ? -34.203 10.596  59.619  1.00 23.21 ? 46  ASP   C O    1 
ATOM   4244 C  CB   . ASP   C 1 67  ? -31.297 12.180  58.722  1.00 26.13 ? 46  ASP   C CB   1 
ATOM   4245 C  CG   . ASP   C 1 67  ? -31.592 12.897  60.031  1.00 32.01 ? 46  ASP   C CG   1 
ATOM   4246 O  OD1  . ASP   C 1 67  ? -31.447 12.256  61.085  1.00 36.68 ? 46  ASP   C OD1  1 
ATOM   4247 O  OD2  . ASP   C 1 67  ? -31.960 14.092  59.982  1.00 33.90 ? 46  ASP   C OD2  1 
ATOM   4248 N  N    . GLU   C 1 68  ? -34.259 11.727  57.666  1.00 23.88 ? 47  GLU   C N    1 
ATOM   4249 C  CA   . GLU   C 1 68  ? -35.689 11.993  57.698  1.00 23.94 ? 47  GLU   C CA   1 
ATOM   4250 C  C    . GLU   C 1 68  ? -36.482 10.689  57.800  1.00 24.81 ? 47  GLU   C C    1 
ATOM   4251 O  O    . GLU   C 1 68  ? -37.404 10.587  58.601  1.00 24.05 ? 47  GLU   C O    1 
ATOM   4252 C  CB   . GLU   C 1 68  ? -36.081 12.849  56.491  1.00 26.53 ? 47  GLU   C CB   1 
ATOM   4253 C  CG   . GLU   C 1 68  ? -37.587 13.065  56.361  1.00 33.10 ? 47  GLU   C CG   1 
ATOM   4254 C  CD   . GLU   C 1 68  ? -38.004 13.672  55.030  1.00 40.56 ? 47  GLU   C CD   1 
ATOM   4255 O  OE1  . GLU   C 1 68  ? -39.050 13.257  54.469  1.00 43.26 ? 47  GLU   C OE1  1 
ATOM   4256 O  OE2  . GLU   C 1 68  ? -37.246 14.543  54.542  1.00 42.40 ? 47  GLU   C OE2  1 
ATOM   4257 N  N    . LEU   C 1 69  ? -36.126 9.679   56.990  1.00 20.53 ? 48  LEU   C N    1 
ATOM   4258 C  CA   . LEU   C 1 69  ? -36.864 8.427   56.993  1.00 20.76 ? 48  LEU   C CA   1 
ATOM   4259 C  C    . LEU   C 1 69  ? -36.639 7.654   58.296  1.00 19.80 ? 48  LEU   C C    1 
ATOM   4260 O  O    . LEU   C 1 69  ? -37.575 7.043   58.805  1.00 21.47 ? 48  LEU   C O    1 
ATOM   4261 C  CB   . LEU   C 1 69  ? -36.525 7.604   55.748  1.00 19.87 ? 48  LEU   C CB   1 
ATOM   4262 C  CG   . LEU   C 1 69  ? -36.836 8.307   54.418  1.00 21.48 ? 48  LEU   C CG   1 
ATOM   4263 C  CD1  . LEU   C 1 69  ? -36.538 7.353   53.249  1.00 21.09 ? 48  LEU   C CD1  1 
ATOM   4264 C  CD2  . LEU   C 1 69  ? -38.279 8.824   54.329  1.00 22.68 ? 48  LEU   C CD2  1 
ATOM   4265 N  N    . ASN   C 1 70  ? -35.401 7.689   58.818  1.00 22.23 ? 49  ASN   C N    1 
ATOM   4266 C  CA   . ASN   C 1 70  ? -35.047 6.968   60.043  1.00 21.43 ? 49  ASN   C CA   1 
ATOM   4267 C  C    . ASN   C 1 70  ? -35.763 7.563   61.258  1.00 24.56 ? 49  ASN   C C    1 
ATOM   4268 O  O    . ASN   C 1 70  ? -36.015 6.847   62.233  1.00 23.89 ? 49  ASN   C O    1 
ATOM   4269 C  CB   . ASN   C 1 70  ? -33.539 6.850   60.242  1.00 20.48 ? 49  ASN   C CB   1 
ATOM   4270 C  CG   . ASN   C 1 70  ? -32.917 5.796   59.351  1.00 19.93 ? 49  ASN   C CG   1 
ATOM   4271 O  OD1  . ASN   C 1 70  ? -33.518 4.738   59.111  1.00 22.04 ? 49  ASN   C OD1  1 
ATOM   4272 N  ND2  . ASN   C 1 70  ? -31.745 6.086   58.816  1.00 17.85 ? 49  ASN   C ND2  1 
ATOM   4273 N  N    . LYS   C 1 71  ? -36.100 8.856   61.179  1.00 26.12 ? 50  LYS   C N    1 
ATOM   4274 C  CA   . LYS   C 1 71  ? -36.854 9.518   62.241  1.00 28.43 ? 50  LYS   C CA   1 
ATOM   4275 C  C    . LYS   C 1 71  ? -38.288 8.998   62.284  1.00 31.48 ? 50  LYS   C C    1 
ATOM   4276 O  O    . LYS   C 1 71  ? -38.873 8.901   63.361  1.00 31.72 ? 50  LYS   C O    1 
ATOM   4277 C  CB   . LYS   C 1 71  ? -36.882 11.040  62.069  1.00 29.96 ? 50  LYS   C CB   1 
ATOM   4278 C  CG   . LYS   C 1 71  ? -35.614 11.756  62.489  1.00 31.89 ? 50  LYS   C CG   1 
ATOM   4279 N  N    . GLU   C 1 72  ? -38.854 8.684   61.112  1.00 28.72 ? 51  GLU   C N    1 
ATOM   4280 C  CA   A GLU   C 1 72  ? -40.189 8.114   61.017  0.40 28.72 ? 51  GLU   C CA   1 
ATOM   4281 C  CA   B GLU   C 1 72  ? -40.190 8.119   61.032  0.60 28.70 ? 51  GLU   C CA   1 
ATOM   4282 C  C    . GLU   C 1 72  ? -40.184 6.697   61.588  1.00 28.02 ? 51  GLU   C C    1 
ATOM   4283 O  O    . GLU   C 1 72  ? -41.070 6.331   62.357  1.00 29.72 ? 51  GLU   C O    1 
ATOM   4284 C  CB   A GLU   C 1 72  ? -40.679 8.120   59.567  0.40 30.61 ? 51  GLU   C CB   1 
ATOM   4285 C  CB   B GLU   C 1 72  ? -40.711 8.160   59.595  0.60 31.22 ? 51  GLU   C CB   1 
ATOM   4286 C  CG   A GLU   C 1 72  ? -42.061 7.499   59.382  0.40 31.77 ? 51  GLU   C CG   1 
ATOM   4287 C  CG   B GLU   C 1 72  ? -40.836 9.578   59.046  0.60 32.93 ? 51  GLU   C CG   1 
ATOM   4288 C  CD   A GLU   C 1 72  ? -43.172 8.288   60.053  0.40 34.33 ? 51  GLU   C CD   1 
ATOM   4289 C  CD   B GLU   C 1 72  ? -41.776 10.464  59.846  0.60 35.24 ? 51  GLU   C CD   1 
ATOM   4290 O  OE1  A GLU   C 1 72  ? -42.847 9.283   60.732  0.40 35.02 ? 51  GLU   C OE1  1 
ATOM   4291 O  OE1  B GLU   C 1 72  ? -41.393 11.606  60.160  0.60 37.42 ? 51  GLU   C OE1  1 
ATOM   4292 O  OE2  A GLU   C 1 72  ? -44.356 7.920   59.893  0.40 36.17 ? 51  GLU   C OE2  1 
ATOM   4293 O  OE2  B GLU   C 1 72  ? -42.888 9.999   60.163  0.60 37.51 ? 51  GLU   C OE2  1 
ATOM   4294 N  N    . ARG   C 1 73  ? -39.188 5.892   61.184  1.00 23.95 ? 52  ARG   C N    1 
ATOM   4295 C  CA   . ARG   C 1 73  ? -39.089 4.512   61.636  1.00 23.47 ? 52  ARG   C CA   1 
ATOM   4296 C  C    . ARG   C 1 73  ? -37.614 4.122   61.702  1.00 23.18 ? 52  ARG   C C    1 
ATOM   4297 O  O    . ARG   C 1 73  ? -36.909 4.125   60.682  1.00 20.04 ? 52  ARG   C O    1 
ATOM   4298 C  CB   . ARG   C 1 73  ? -39.833 3.453   60.807  1.00 25.25 ? 52  ARG   C CB   1 
ATOM   4299 C  CG   . ARG   C 1 73  ? -41.311 3.670   60.501  1.00 27.75 ? 52  ARG   C CG   1 
ATOM   4300 C  CD   . ARG   C 1 73  ? -41.933 2.402   59.943  1.00 27.55 ? 52  ARG   C CD   1 
ATOM   4301 N  NE   . ARG   C 1 73  ? -41.335 1.905   58.693  1.00 27.66 ? 52  ARG   C NE   1 
ATOM   4302 C  CZ   . ARG   C 1 73  ? -41.526 2.420   57.468  1.00 29.05 ? 52  ARG   C CZ   1 
ATOM   4303 N  NH1  . ARG   C 1 73  ? -42.260 3.509   57.306  1.00 28.75 ? 52  ARG   C NH1  1 
ATOM   4304 N  NH2  . ARG   C 1 73  ? -40.974 1.832   56.416  1.00 27.31 ? 52  ARG   C NH2  1 
ATOM   4305 N  N    . SER   C 1 74  ? -37.144 3.788   62.911  1.00 21.74 ? 53  SER   C N    1 
ATOM   4306 C  CA   . SER   C 1 74  ? -35.721 3.536   63.115  1.00 21.24 ? 53  SER   C CA   1 
ATOM   4307 C  C    . SER   C 1 74  ? -35.217 2.374   62.256  1.00 18.86 ? 53  SER   C C    1 
ATOM   4308 O  O    . SER   C 1 74  ? -35.902 1.364   62.108  1.00 19.10 ? 53  SER   C O    1 
ATOM   4309 C  CB   . SER   C 1 74  ? -35.446 3.255   64.582  1.00 22.80 ? 53  SER   C CB   1 
ATOM   4310 O  OG   . SER   C 1 74  ? -35.913 4.342   65.372  1.00 30.54 ? 53  SER   C OG   1 
ATOM   4311 N  N    . ASN   C 1 75  ? -33.994 2.514   61.720  1.00 18.18 ? 54  ASN   C N    1 
ATOM   4312 C  CA   . ASN   C 1 75  ? -33.319 1.409   61.051  1.00 16.91 ? 54  ASN   C CA   1 
ATOM   4313 C  C    . ASN   C 1 75  ? -34.054 0.995   59.770  1.00 16.93 ? 54  ASN   C C    1 
ATOM   4314 O  O    . ASN   C 1 75  ? -34.113 -0.191  59.438  1.00 18.79 ? 54  ASN   C O    1 
ATOM   4315 C  CB   . ASN   C 1 75  ? -33.056 0.215   61.965  1.00 16.51 ? 54  ASN   C CB   1 
ATOM   4316 C  CG   . ASN   C 1 75  ? -32.158 0.605   63.115  1.00 18.70 ? 54  ASN   C CG   1 
ATOM   4317 O  OD1  . ASN   C 1 75  ? -31.159 1.295   62.896  1.00 19.48 ? 54  ASN   C OD1  1 
ATOM   4318 N  ND2  . ASN   C 1 75  ? -32.514 0.221   64.335  1.00 21.66 ? 54  ASN   C ND2  1 
ATOM   4319 N  N    . THR   C 1 76  ? -34.556 1.985   59.029  1.00 16.48 ? 55  THR   C N    1 
ATOM   4320 C  CA   . THR   C 1 76  ? -35.311 1.644   57.821  1.00 16.91 ? 55  THR   C CA   1 
ATOM   4321 C  C    . THR   C 1 76  ? -34.735 2.305   56.572  1.00 17.15 ? 55  THR   C C    1 
ATOM   4322 O  O    . THR   C 1 76  ? -35.320 2.153   55.499  1.00 18.18 ? 55  THR   C O    1 
ATOM   4323 C  CB   . THR   C 1 76  ? -36.806 1.948   57.966  1.00 18.27 ? 55  THR   C CB   1 
ATOM   4324 O  OG1  . THR   C 1 76  ? -36.947 3.343   58.195  1.00 19.07 ? 55  THR   C OG1  1 
ATOM   4325 C  CG2  . THR   C 1 76  ? -37.488 1.113   59.035  1.00 21.48 ? 55  THR   C CG2  1 
ATOM   4326 N  N    . ALA   C 1 77  ? -33.624 3.044   56.678  1.00 16.70 ? 56  ALA   C N    1 
ATOM   4327 C  CA   . ALA   C 1 77  ? -33.053 3.711   55.516  1.00 16.09 ? 56  ALA   C CA   1 
ATOM   4328 C  C    . ALA   C 1 77  ? -31.536 3.780   55.647  1.00 16.68 ? 56  ALA   C C    1 
ATOM   4329 O  O    . ALA   C 1 77  ? -31.012 4.048   56.725  1.00 16.89 ? 56  ALA   C O    1 
ATOM   4330 C  CB   . ALA   C 1 77  ? -33.634 5.114   55.369  1.00 15.52 ? 56  ALA   C CB   1 
ATOM   4331 N  N    . VAL   C 1 78  ? -30.828 3.512   54.544  1.00 16.19 ? 57  VAL   C N    1 
ATOM   4332 C  CA   . VAL   C 1 78  ? -29.381 3.654   54.481  1.00 16.17 ? 57  VAL   C CA   1 
ATOM   4333 C  C    . VAL   C 1 78  ? -29.023 4.324   53.159  1.00 15.88 ? 57  VAL   C C    1 
ATOM   4334 O  O    . VAL   C 1 78  ? -29.877 4.388   52.262  1.00 17.06 ? 57  VAL   C O    1 
ATOM   4335 C  CB   . VAL   C 1 78  ? -28.719 2.260   54.596  1.00 15.97 ? 57  VAL   C CB   1 
ATOM   4336 C  CG1  . VAL   C 1 78  ? -28.999 1.598   55.936  1.00 17.90 ? 57  VAL   C CG1  1 
ATOM   4337 C  CG2  . VAL   C 1 78  ? -29.109 1.308   53.460  1.00 17.64 ? 57  VAL   C CG2  1 
ATOM   4338 N  N    . VAL   C 1 79  ? -27.749 4.747   53.033  1.00 16.04 ? 58  VAL   C N    1 
ATOM   4339 C  CA   . VAL   C 1 79  ? -27.226 5.332   51.806  1.00 16.75 ? 58  VAL   C CA   1 
ATOM   4340 C  C    . VAL   C 1 79  ? -26.126 4.435   51.244  1.00 15.95 ? 58  VAL   C C    1 
ATOM   4341 O  O    . VAL   C 1 79  ? -25.444 3.710   51.971  1.00 17.36 ? 58  VAL   C O    1 
ATOM   4342 C  CB   . VAL   C 1 79  ? -26.752 6.805   51.851  1.00 18.05 ? 58  VAL   C CB   1 
ATOM   4343 C  CG1  . VAL   C 1 79  ? -27.820 7.696   52.477  1.00 18.11 ? 58  VAL   C CG1  1 
ATOM   4344 C  CG2  . VAL   C 1 79  ? -25.443 6.957   52.622  1.00 20.25 ? 58  VAL   C CG2  1 
ATOM   4345 N  N    . CYS   C 1 80  ? -25.965 4.491   49.906  1.00 16.14 ? 59  CYS   C N    1 
ATOM   4346 C  CA   . CYS   C 1 80  ? -24.925 3.743   49.226  1.00 16.49 ? 59  CYS   C CA   1 
ATOM   4347 C  C    . CYS   C 1 80  ? -24.423 4.611   48.077  1.00 18.05 ? 59  CYS   C C    1 
ATOM   4348 O  O    . CYS   C 1 80  ? -25.185 4.955   47.179  1.00 20.29 ? 59  CYS   C O    1 
ATOM   4349 C  CB   . CYS   C 1 80  ? -25.470 2.419   48.705  1.00 19.72 ? 59  CYS   C CB   1 
ATOM   4350 S  SG   . CYS   C 1 80  ? -24.207 1.461   47.824  1.00 25.51 ? 59  CYS   C SG   1 
ATOM   4351 N  N    . GLN   C 1 81  ? -23.142 4.955   48.081  1.00 17.31 ? 60  GLN   C N    1 
ATOM   4352 C  CA   . GLN   C 1 81  ? -22.624 5.799   47.021  1.00 16.51 ? 60  GLN   C CA   1 
ATOM   4353 C  C    . GLN   C 1 81  ? -22.034 4.920   45.926  1.00 17.18 ? 60  GLN   C C    1 
ATOM   4354 O  O    . GLN   C 1 81  ? -21.343 3.948   46.220  1.00 17.34 ? 60  GLN   C O    1 
ATOM   4355 C  CB   . GLN   C 1 81  ? -21.515 6.660   47.616  1.00 17.60 ? 60  GLN   C CB   1 
ATOM   4356 C  CG   . GLN   C 1 81  ? -21.090 7.802   46.698  1.00 18.66 ? 60  GLN   C CG   1 
ATOM   4357 C  CD   . GLN   C 1 81  ? -20.048 7.422   45.662  1.00 19.50 ? 60  GLN   C CD   1 
ATOM   4358 O  OE1  . GLN   C 1 81  ? -19.289 6.450   45.801  1.00 21.14 ? 60  GLN   C OE1  1 
ATOM   4359 N  NE2  . GLN   C 1 81  ? -20.018 8.200   44.586  1.00 20.31 ? 60  GLN   C NE2  1 
ATOM   4360 N  N    . ALA   C 1 82  ? -22.333 5.252   44.656  1.00 15.95 ? 61  ALA   C N    1 
ATOM   4361 C  CA   . ALA   C 1 82  ? -21.609 4.623   43.560  1.00 15.76 ? 61  ALA   C CA   1 
ATOM   4362 C  C    . ALA   C 1 82  ? -21.770 5.417   42.266  1.00 16.16 ? 61  ALA   C C    1 
ATOM   4363 O  O    . ALA   C 1 82  ? -22.830 5.967   41.987  1.00 16.20 ? 61  ALA   C O    1 
ATOM   4364 C  CB   . ALA   C 1 82  ? -22.082 3.197   43.345  1.00 17.05 ? 61  ALA   C CB   1 
ATOM   4365 N  N    . ASP   C 1 83  ? -20.677 5.451   41.480  1.00 16.50 ? 62  ASP   C N    1 
ATOM   4366 C  CA   . ASP   C 1 83  ? -20.702 5.948   40.111  1.00 16.22 ? 62  ASP   C CA   1 
ATOM   4367 C  C    . ASP   C 1 83  ? -21.212 4.812   39.230  1.00 15.98 ? 62  ASP   C C    1 
ATOM   4368 O  O    . ASP   C 1 83  ? -20.697 3.681   39.286  1.00 18.12 ? 62  ASP   C O    1 
ATOM   4369 C  CB   . ASP   C 1 83  ? -19.291 6.335   39.683  1.00 17.03 ? 62  ASP   C CB   1 
ATOM   4370 C  CG   . ASP   C 1 83  ? -19.159 7.056   38.348  1.00 21.14 ? 62  ASP   C CG   1 
ATOM   4371 O  OD1  . ASP   C 1 83  ? -20.174 7.240   37.670  1.00 18.96 ? 62  ASP   C OD1  1 
ATOM   4372 O  OD2  . ASP   C 1 83  ? -18.007 7.384   37.970  1.00 25.19 ? 62  ASP   C OD2  1 
ATOM   4373 N  N    . LEU   C 1 84  ? -22.229 5.116   38.410  1.00 15.74 ? 63  LEU   C N    1 
ATOM   4374 C  CA   . LEU   C 1 84  ? -22.820 4.116   37.524  1.00 15.16 ? 63  LEU   C CA   1 
ATOM   4375 C  C    . LEU   C 1 84  ? -22.387 4.308   36.068  1.00 15.44 ? 63  LEU   C C    1 
ATOM   4376 O  O    . LEU   C 1 84  ? -22.959 3.664   35.170  1.00 15.81 ? 63  LEU   C O    1 
ATOM   4377 C  CB   . LEU   C 1 84  ? -24.341 4.081   37.679  1.00 15.84 ? 63  LEU   C CB   1 
ATOM   4378 C  CG   . LEU   C 1 84  ? -24.828 3.676   39.078  1.00 15.51 ? 63  LEU   C CG   1 
ATOM   4379 C  CD1  . LEU   C 1 84  ? -26.333 3.839   39.049  1.00 18.06 ? 63  LEU   C CD1  1 
ATOM   4380 C  CD2  . LEU   C 1 84  ? -24.420 2.253   39.443  1.00 15.90 ? 63  LEU   C CD2  1 
ATOM   4381 N  N    . THR   C 1 85  ? -21.340 5.125   35.866  1.00 15.50 ? 64  THR   C N    1 
ATOM   4382 C  CA   . THR   C 1 85  ? -20.670 5.225   34.573  1.00 16.77 ? 64  THR   C CA   1 
ATOM   4383 C  C    . THR   C 1 85  ? -20.168 3.842   34.146  1.00 16.63 ? 64  THR   C C    1 
ATOM   4384 O  O    . THR   C 1 85  ? -19.678 3.072   34.976  1.00 18.09 ? 64  THR   C O    1 
ATOM   4385 C  CB   . THR   C 1 85  ? -19.497 6.196   34.664  1.00 17.41 ? 64  THR   C CB   1 
ATOM   4386 O  OG1  . THR   C 1 85  ? -20.028 7.454   35.068  1.00 19.55 ? 64  THR   C OG1  1 
ATOM   4387 C  CG2  . THR   C 1 85  ? -18.847 6.417   33.303  1.00 19.32 ? 64  THR   C CG2  1 
ATOM   4388 N  N    . ASN   C 1 86  ? -20.258 3.538   32.841  1.00 16.95 ? 65  ASN   C N    1 
ATOM   4389 C  CA   . ASN   C 1 86  ? -19.769 2.249   32.362  1.00 16.18 ? 65  ASN   C CA   1 
ATOM   4390 C  C    . ASN   C 1 86  ? -18.249 2.202   32.500  1.00 18.54 ? 65  ASN   C C    1 
ATOM   4391 O  O    . ASN   C 1 86  ? -17.560 3.189   32.236  1.00 19.53 ? 65  ASN   C O    1 
ATOM   4392 C  CB   . ASN   C 1 86  ? -20.148 2.030   30.899  1.00 17.23 ? 65  ASN   C CB   1 
ATOM   4393 C  CG   . ASN   C 1 86  ? -19.770 0.640   30.449  1.00 19.44 ? 65  ASN   C CG   1 
ATOM   4394 O  OD1  . ASN   C 1 86  ? -20.052 -0.334  31.158  1.00 19.38 ? 65  ASN   C OD1  1 
ATOM   4395 N  ND2  . ASN   C 1 86  ? -19.134 0.526   29.287  1.00 19.56 ? 65  ASN   C ND2  1 
ATOM   4396 N  N    . SER   C 1 87  ? -17.744 1.055   32.963  1.00 19.13 ? 66  SER   C N    1 
ATOM   4397 C  CA   . SER   C 1 87  ? -16.315 0.818   33.129  1.00 20.65 ? 66  SER   C CA   1 
ATOM   4398 C  C    . SER   C 1 87  ? -16.126 -0.654  33.473  1.00 19.71 ? 66  SER   C C    1 
ATOM   4399 O  O    . SER   C 1 87  ? -17.091 -1.378  33.690  1.00 21.85 ? 66  SER   C O    1 
ATOM   4400 C  CB   . SER   C 1 87  ? -15.728 1.660   34.222  1.00 22.00 ? 66  SER   C CB   1 
ATOM   4401 O  OG   . SER   C 1 87  ? -16.048 1.079   35.480  1.00 21.35 ? 66  SER   C OG   1 
ATOM   4402 N  N    . ASN   C 1 88  ? -14.870 -1.095  33.566  1.00 23.20 ? 67  ASN   C N    1 
ATOM   4403 C  CA   A ASN   C 1 88  ? -14.638 -2.493  33.898  0.70 24.06 ? 67  ASN   C CA   1 
ATOM   4404 C  CA   B ASN   C 1 88  ? -14.569 -2.476  33.921  0.30 23.67 ? 67  ASN   C CA   1 
ATOM   4405 C  C    . ASN   C 1 88  ? -14.910 -2.768  35.385  1.00 24.35 ? 67  ASN   C C    1 
ATOM   4406 O  O    . ASN   C 1 88  ? -14.989 -3.926  35.792  1.00 27.60 ? 67  ASN   C O    1 
ATOM   4407 C  CB   A ASN   C 1 88  ? -13.291 -2.981  33.367  0.70 26.97 ? 67  ASN   C CB   1 
ATOM   4408 C  CB   B ASN   C 1 88  ? -13.141 -2.872  33.550  0.30 24.17 ? 67  ASN   C CB   1 
ATOM   4409 C  CG   A ASN   C 1 88  ? -13.319 -3.335  31.895  0.70 29.01 ? 67  ASN   C CG   1 
ATOM   4410 C  CG   B ASN   C 1 88  ? -12.131 -1.781  33.813  0.30 24.89 ? 67  ASN   C CG   1 
ATOM   4411 O  OD1  A ASN   C 1 88  ? -14.373 -3.322  31.247  0.70 27.90 ? 67  ASN   C OD1  1 
ATOM   4412 O  OD1  B ASN   C 1 88  ? -12.152 -1.143  34.872  0.30 22.96 ? 67  ASN   C OD1  1 
ATOM   4413 N  ND2  A ASN   C 1 88  ? -12.162 -3.674  31.346  0.70 32.87 ? 67  ASN   C ND2  1 
ATOM   4414 N  ND2  B ASN   C 1 88  ? -11.247 -1.544  32.852  0.30 26.96 ? 67  ASN   C ND2  1 
ATOM   4415 N  N    . VAL   C 1 89  ? -15.120 -1.721  36.192  1.00 22.97 ? 68  VAL   C N    1 
ATOM   4416 C  CA   . VAL   C 1 89  ? -15.408 -1.905  37.613  1.00 22.58 ? 68  VAL   C CA   1 
ATOM   4417 C  C    . VAL   C 1 89  ? -16.906 -1.781  37.902  1.00 21.91 ? 68  VAL   C C    1 
ATOM   4418 O  O    . VAL   C 1 89  ? -17.347 -1.978  39.042  1.00 22.38 ? 68  VAL   C O    1 
ATOM   4419 C  CB   . VAL   C 1 89  ? -14.588 -0.976  38.536  1.00 23.41 ? 68  VAL   C CB   1 
ATOM   4420 C  CG1  . VAL   C 1 89  ? -13.088 -1.066  38.249  1.00 26.35 ? 68  VAL   C CG1  1 
ATOM   4421 C  CG2  . VAL   C 1 89  ? -15.045 0.483   38.515  1.00 24.03 ? 68  VAL   C CG2  1 
ATOM   4422 N  N    . LEU   C 1 90  ? -17.696 -1.441  36.877  1.00 18.65 ? 69  LEU   C N    1 
ATOM   4423 C  CA   . LEU   C 1 90  ? -19.117 -1.232  37.113  1.00 18.25 ? 69  LEU   C CA   1 
ATOM   4424 C  C    . LEU   C 1 90  ? -19.802 -2.508  37.604  1.00 18.30 ? 69  LEU   C C    1 
ATOM   4425 O  O    . LEU   C 1 90  ? -20.659 -2.424  38.488  1.00 19.01 ? 69  LEU   C O    1 
ATOM   4426 C  CB   . LEU   C 1 90  ? -19.804 -0.641  35.880  1.00 16.69 ? 69  LEU   C CB   1 
ATOM   4427 C  CG   . LEU   C 1 90  ? -21.298 -0.329  36.045  1.00 15.43 ? 69  LEU   C CG   1 
ATOM   4428 C  CD1  . LEU   C 1 90  ? -21.556 0.727   37.136  1.00 16.56 ? 69  LEU   C CD1  1 
ATOM   4429 C  CD2  . LEU   C 1 90  ? -21.875 0.118   34.683  1.00 16.34 ? 69  LEU   C CD2  1 
ATOM   4430 N  N    . PRO   C 1 91  ? -19.523 -3.728  37.072  1.00 18.61 ? 70  PRO   C N    1 
ATOM   4431 C  CA   . PRO   C 1 91  ? -20.185 -4.919  37.592  1.00 18.91 ? 70  PRO   C CA   1 
ATOM   4432 C  C    . PRO   C 1 91  ? -20.007 -5.069  39.106  1.00 20.41 ? 70  PRO   C C    1 
ATOM   4433 O  O    . PRO   C 1 91  ? -20.974 -5.361  39.816  1.00 19.69 ? 70  PRO   C O    1 
ATOM   4434 C  CB   . PRO   C 1 91  ? -19.561 -6.061  36.786  1.00 19.04 ? 70  PRO   C CB   1 
ATOM   4435 C  CG   . PRO   C 1 91  ? -19.193 -5.389  35.473  1.00 20.11 ? 70  PRO   C CG   1 
ATOM   4436 C  CD   . PRO   C 1 91  ? -18.658 -4.033  35.912  1.00 18.96 ? 70  PRO   C CD   1 
ATOM   4437 N  N    . ALA   C 1 92  ? -18.775 -4.867  39.582  1.00 19.66 ? 71  ALA   C N    1 
ATOM   4438 C  CA   . ALA   C 1 92  ? -18.487 -4.924  41.010  1.00 20.93 ? 71  ALA   C CA   1 
ATOM   4439 C  C    . ALA   C 1 92  ? -19.272 -3.870  41.800  1.00 20.63 ? 71  ALA   C C    1 
ATOM   4440 O  O    . ALA   C 1 92  ? -19.833 -4.188  42.851  1.00 21.95 ? 71  ALA   C O    1 
ATOM   4441 C  CB   . ALA   C 1 92  ? -16.985 -4.829  41.233  1.00 22.14 ? 71  ALA   C CB   1 
ATOM   4442 N  N    . SER   C 1 93  ? -19.344 -2.634  41.289  1.00 19.09 ? 72  SER   C N    1 
ATOM   4443 C  CA   . SER   C 1 93  ? -20.086 -1.569  41.949  1.00 18.28 ? 72  SER   C CA   1 
ATOM   4444 C  C    . SER   C 1 93  ? -21.555 -1.960  42.099  1.00 19.25 ? 72  SER   C C    1 
ATOM   4445 O  O    . SER   C 1 93  ? -22.186 -1.716  43.132  1.00 19.24 ? 72  SER   C O    1 
ATOM   4446 C  CB   . SER   C 1 93  ? -19.984 -0.260  41.207  1.00 20.99 ? 72  SER   C CB   1 
ATOM   4447 O  OG   . SER   C 1 93  ? -18.653 0.244   41.135  1.00 23.06 ? 72  SER   C OG   1 
ATOM   4448 N  N    . CYS   C 1 94  ? -22.120 -2.529  41.028  1.00 16.85 ? 73  CYS   C N    1 
ATOM   4449 C  CA   . CYS   C 1 94  ? -23.537 -2.878  41.058  1.00 17.34 ? 73  CYS   C CA   1 
ATOM   4450 C  C    . CYS   C 1 94  ? -23.822 -4.031  42.024  1.00 17.63 ? 73  CYS   C C    1 
ATOM   4451 O  O    . CYS   C 1 94  ? -24.845 -4.028  42.714  1.00 17.47 ? 73  CYS   C O    1 
ATOM   4452 C  CB   . CYS   C 1 94  ? -24.023 -3.200  39.645  1.00 16.65 ? 73  CYS   C CB   1 
ATOM   4453 S  SG   . CYS   C 1 94  ? -24.093 -1.712  38.615  1.00 17.22 ? 73  CYS   C SG   1 
ATOM   4454 N  N    . GLU   C 1 95  ? -22.923 -5.019  42.069  1.00 19.51 ? 74  GLU   C N    1 
ATOM   4455 C  CA   . GLU   C 1 95  ? -23.009 -6.085  43.055  1.00 19.72 ? 74  GLU   C CA   1 
ATOM   4456 C  C    . GLU   C 1 95  ? -23.010 -5.483  44.466  1.00 18.31 ? 74  GLU   C C    1 
ATOM   4457 O  O    . GLU   C 1 95  ? -23.803 -5.922  45.302  1.00 19.51 ? 74  GLU   C O    1 
ATOM   4458 C  CB   . GLU   C 1 95  ? -21.868 -7.075  42.815  1.00 21.03 ? 74  GLU   C CB   1 
ATOM   4459 C  CG   . GLU   C 1 95  ? -21.766 -8.145  43.903  1.00 26.05 ? 74  GLU   C CG   1 
ATOM   4460 C  CD   . GLU   C 1 95  ? -22.763 -9.279  43.770  0.60 30.33 ? 74  GLU   C CD   1 
ATOM   4461 O  OE1  . GLU   C 1 95  ? -23.556 -9.271  42.801  0.60 31.52 ? 74  GLU   C OE1  1 
ATOM   4462 O  OE2  . GLU   C 1 95  ? -22.745 -10.181 44.637  0.60 32.91 ? 74  GLU   C OE2  1 
ATOM   4463 N  N    . GLU   C 1 96  ? -22.173 -4.452  44.690  1.00 18.41 ? 75  GLU   C N    1 
ATOM   4464 C  CA   A GLU   C 1 96  ? -22.059 -3.881  46.023  0.60 18.56 ? 75  GLU   C CA   1 
ATOM   4465 C  CA   B GLU   C 1 96  ? -21.998 -3.738  45.954  0.40 19.27 ? 75  GLU   C CA   1 
ATOM   4466 C  C    . GLU   C 1 96  ? -23.320 -3.093  46.372  1.00 19.32 ? 75  GLU   C C    1 
ATOM   4467 O  O    . GLU   C 1 96  ? -23.703 -3.086  47.541  1.00 18.75 ? 75  GLU   C O    1 
ATOM   4468 C  CB   A GLU   C 1 96  ? -20.742 -3.154  46.301  0.60 18.76 ? 75  GLU   C CB   1 
ATOM   4469 C  CB   B GLU   C 1 96  ? -20.927 -2.654  45.743  0.40 20.72 ? 75  GLU   C CB   1 
ATOM   4470 C  CG   A GLU   C 1 96  ? -19.529 -4.080  46.285  0.60 22.03 ? 75  GLU   C CG   1 
ATOM   4471 C  CG   B GLU   C 1 96  ? -21.011 -1.436  46.663  0.40 22.87 ? 75  GLU   C CG   1 
ATOM   4472 C  CD   A GLU   C 1 96  ? -19.444 -5.176  47.343  0.60 25.04 ? 75  GLU   C CD   1 
ATOM   4473 C  CD   B GLU   C 1 96  ? -20.623 -0.074  46.094  0.40 24.55 ? 75  GLU   C CD   1 
ATOM   4474 O  OE1  A GLU   C 1 96  ? -18.582 -6.049  47.128  0.60 29.03 ? 75  GLU   C OE1  1 
ATOM   4475 O  OE1  B GLU   C 1 96  ? -19.489 0.134   45.587  0.40 23.68 ? 75  GLU   C OE1  1 
ATOM   4476 O  OE2  A GLU   C 1 96  ? -20.168 -5.195  48.371  0.60 24.72 ? 75  GLU   C OE2  1 
ATOM   4477 O  OE2  B GLU   C 1 96  ? -21.497 0.811   46.183  0.40 25.22 ? 75  GLU   C OE2  1 
ATOM   4478 N  N    . ILE   C 1 97  ? -24.006 -2.494  45.373  1.00 17.09 ? 76  ILE   C N    1 
ATOM   4479 C  CA   . ILE   C 1 97  ? -25.237 -1.779  45.687  1.00 16.54 ? 76  ILE   C CA   1 
ATOM   4480 C  C    . ILE   C 1 97  ? -26.281 -2.768  46.206  1.00 15.84 ? 76  ILE   C C    1 
ATOM   4481 O  O    . ILE   C 1 97  ? -26.967 -2.508  47.202  1.00 17.10 ? 76  ILE   C O    1 
ATOM   4482 C  CB   . ILE   C 1 97  ? -25.733 -0.988  44.453  1.00 15.22 ? 76  ILE   C CB   1 
ATOM   4483 C  CG1  . ILE   C 1 97  ? -24.778 0.180   44.110  1.00 18.23 ? 76  ILE   C CG1  1 
ATOM   4484 C  CG2  . ILE   C 1 97  ? -27.152 -0.467  44.698  1.00 17.50 ? 76  ILE   C CG2  1 
ATOM   4485 C  CD1  . ILE   C 1 97  ? -25.069 0.842   42.770  1.00 17.83 ? 76  ILE   C CD1  1 
ATOM   4486 N  N    . ILE   C 1 98  ? -26.441 -3.895  45.504  1.00 16.59 ? 77  ILE   C N    1 
ATOM   4487 C  CA   . ILE   C 1 98  ? -27.396 -4.908  45.942  1.00 16.28 ? 77  ILE   C CA   1 
ATOM   4488 C  C    . ILE   C 1 98  ? -26.961 -5.443  47.313  1.00 16.82 ? 77  ILE   C C    1 
ATOM   4489 O  O    . ILE   C 1 98  ? -27.775 -5.613  48.220  1.00 16.66 ? 77  ILE   C O    1 
ATOM   4490 C  CB   . ILE   C 1 98  ? -27.593 -6.008  44.872  1.00 16.25 ? 77  ILE   C CB   1 
ATOM   4491 C  CG1  . ILE   C 1 98  ? -28.139 -5.408  43.546  1.00 16.87 ? 77  ILE   C CG1  1 
ATOM   4492 C  CG2  . ILE   C 1 98  ? -28.497 -7.134  45.384  1.00 17.86 ? 77  ILE   C CG2  1 
ATOM   4493 C  CD1  . ILE   C 1 98  ? -29.429 -4.606  43.697  1.00 16.48 ? 77  ILE   C CD1  1 
ATOM   4494 N  N    . ASN   C 1 99  ? -25.658 -5.686  47.459  1.00 17.38 ? 78  ASN   C N    1 
ATOM   4495 C  CA   A ASN   C 1 99  ? -25.135 -6.238  48.701  0.70 17.60 ? 78  ASN   C CA   1 
ATOM   4496 C  CA   B ASN   C 1 99  ? -25.098 -6.203  48.697  0.30 18.13 ? 78  ASN   C CA   1 
ATOM   4497 C  C    . ASN   C 1 99  ? -25.452 -5.288  49.857  1.00 18.33 ? 78  ASN   C C    1 
ATOM   4498 O  O    . ASN   C 1 99  ? -25.659 -5.751  50.981  1.00 19.75 ? 78  ASN   C O    1 
ATOM   4499 C  CB   A ASN   C 1 99  ? -23.663 -6.597  48.513  0.70 17.98 ? 78  ASN   C CB   1 
ATOM   4500 C  CB   B ASN   C 1 99  ? -23.578 -6.240  48.649  0.30 18.80 ? 78  ASN   C CB   1 
ATOM   4501 C  CG   A ASN   C 1 99  ? -23.092 -7.509  49.574  0.70 18.82 ? 78  ASN   C CG   1 
ATOM   4502 C  CG   B ASN   C 1 99  ? -23.094 -7.475  47.938  0.30 19.20 ? 78  ASN   C CG   1 
ATOM   4503 O  OD1  A ASN   C 1 99  ? -23.746 -8.473  49.980  0.70 17.90 ? 78  ASN   C OD1  1 
ATOM   4504 O  OD1  B ASN   C 1 99  ? -23.881 -8.397  47.713  0.30 20.67 ? 78  ASN   C OD1  1 
ATOM   4505 N  ND2  A ASN   C 1 99  ? -21.856 -7.252  49.986  0.70 20.65 ? 78  ASN   C ND2  1 
ATOM   4506 N  ND2  B ASN   C 1 99  ? -21.813 -7.514  47.601  0.30 20.43 ? 78  ASN   C ND2  1 
ATOM   4507 N  N    . SER   C 1 100 ? -25.488 -3.970  49.598  1.00 18.13 ? 79  SER   C N    1 
ATOM   4508 C  CA   A SER   C 1 100 ? -25.717 -3.038  50.690  0.70 18.09 ? 79  SER   C CA   1 
ATOM   4509 C  CA   B SER   C 1 100 ? -25.750 -2.997  50.652  0.30 17.67 ? 79  SER   C CA   1 
ATOM   4510 C  C    . SER   C 1 100 ? -27.105 -3.255  51.301  1.00 18.95 ? 79  SER   C C    1 
ATOM   4511 O  O    . SER   C 1 100 ? -27.282 -3.059  52.500  1.00 19.32 ? 79  SER   C O    1 
ATOM   4512 C  CB   A SER   C 1 100 ? -25.527 -1.607  50.255  0.70 18.52 ? 79  SER   C CB   1 
ATOM   4513 C  CB   B SER   C 1 100 ? -25.715 -1.590  50.134  0.30 16.84 ? 79  SER   C CB   1 
ATOM   4514 O  OG   A SER   C 1 100 ? -26.642 -1.157  49.497  0.70 19.88 ? 79  SER   C OG   1 
ATOM   4515 O  OG   B SER   C 1 100 ? -24.396 -1.202  49.799  0.30 15.54 ? 79  SER   C OG   1 
ATOM   4516 N  N    . CYS   C 1 101 ? -28.087 -3.628  50.469  1.00 16.96 ? 80  CYS   C N    1 
ATOM   4517 C  CA   . CYS   C 1 101 ? -29.440 -3.920  50.928  1.00 16.74 ? 80  CYS   C CA   1 
ATOM   4518 C  C    . CYS   C 1 101 ? -29.419 -5.165  51.829  1.00 16.63 ? 80  CYS   C C    1 
ATOM   4519 O  O    . CYS   C 1 101 ? -30.067 -5.186  52.881  1.00 17.91 ? 80  CYS   C O    1 
ATOM   4520 C  CB   . CYS   C 1 101 ? -30.374 -3.991  49.714  1.00 17.64 ? 80  CYS   C CB   1 
ATOM   4521 S  SG   . CYS   C 1 101 ? -32.132 -3.868  50.134  1.00 18.47 ? 80  CYS   C SG   1 
ATOM   4522 N  N    . PHE   C 1 102 ? -28.705 -6.216  51.412  1.00 18.01 ? 81  PHE   C N    1 
ATOM   4523 C  CA   . PHE   C 1 102 ? -28.635 -7.420  52.227  1.00 18.45 ? 81  PHE   C CA   1 
ATOM   4524 C  C    . PHE   C 1 102 ? -27.883 -7.172  53.533  1.00 18.82 ? 81  PHE   C C    1 
ATOM   4525 O  O    . PHE   C 1 102 ? -28.279 -7.750  54.547  1.00 18.95 ? 81  PHE   C O    1 
ATOM   4526 C  CB   . PHE   C 1 102 ? -28.024 -8.610  51.479  1.00 18.63 ? 81  PHE   C CB   1 
ATOM   4527 C  CG   . PHE   C 1 102 ? -28.997 -9.189  50.464  1.00 18.90 ? 81  PHE   C CG   1 
ATOM   4528 C  CD1  . PHE   C 1 102 ? -29.044 -8.701  49.164  1.00 19.35 ? 81  PHE   C CD1  1 
ATOM   4529 C  CD2  . PHE   C 1 102 ? -29.885 -10.200 50.822  1.00 19.83 ? 81  PHE   C CD2  1 
ATOM   4530 C  CE1  . PHE   C 1 102 ? -29.964 -9.206  48.252  1.00 20.58 ? 81  PHE   C CE1  1 
ATOM   4531 C  CE2  . PHE   C 1 102 ? -30.794 -10.712 49.909  1.00 20.60 ? 81  PHE   C CE2  1 
ATOM   4532 C  CZ   . PHE   C 1 102 ? -30.838 -10.214 48.622  1.00 20.59 ? 81  PHE   C CZ   1 
ATOM   4533 N  N    . ARG   C 1 103 ? -26.807 -6.365  53.489  1.00 17.75 ? 82  ARG   C N    1 
ATOM   4534 C  CA   . ARG   C 1 103 ? -25.998 -6.093  54.686  1.00 18.03 ? 82  ARG   C CA   1 
ATOM   4535 C  C    . ARG   C 1 103 ? -26.854 -5.381  55.732  1.00 20.33 ? 82  ARG   C C    1 
ATOM   4536 O  O    . ARG   C 1 103 ? -26.723 -5.667  56.926  1.00 19.49 ? 82  ARG   C O    1 
ATOM   4537 C  CB   . ARG   C 1 103 ? -24.770 -5.217  54.394  1.00 19.24 ? 82  ARG   C CB   1 
ATOM   4538 C  CG   . ARG   C 1 103 ? -23.442 -5.841  53.964  1.00 23.24 ? 82  ARG   C CG   1 
ATOM   4539 C  CD   . ARG   C 1 103 ? -23.510 -7.176  53.226  1.00 23.23 ? 82  ARG   C CD   1 
ATOM   4540 N  NE   . ARG   C 1 103 ? -23.697 -8.343  54.096  1.00 25.53 ? 82  ARG   C NE   1 
ATOM   4541 C  CZ   . ARG   C 1 103 ? -24.052 -9.556  53.681  1.00 29.52 ? 82  ARG   C CZ   1 
ATOM   4542 N  NH1  . ARG   C 1 103 ? -24.281 -9.773  52.391  1.00 25.95 ? 82  ARG   C NH1  1 
ATOM   4543 N  NH2  . ARG   C 1 103 ? -24.182 -10.545 54.559  1.00 28.65 ? 82  ARG   C NH2  1 
ATOM   4544 N  N    . ALA   C 1 104 ? -27.691 -4.431  55.288  1.00 18.96 ? 83  ALA   C N    1 
ATOM   4545 C  CA   . ALA   C 1 104 ? -28.497 -3.610  56.185  1.00 18.67 ? 83  ALA   C CA   1 
ATOM   4546 C  C    . ALA   C 1 104 ? -29.763 -4.345  56.622  1.00 20.35 ? 83  ALA   C C    1 
ATOM   4547 O  O    . ALA   C 1 104 ? -30.126 -4.299  57.791  1.00 20.47 ? 83  ALA   C O    1 
ATOM   4548 C  CB   . ALA   C 1 104 ? -28.825 -2.275  55.536  1.00 19.09 ? 83  ALA   C CB   1 
ATOM   4549 N  N    . PHE   C 1 105 ? -30.454 -5.012  55.678  1.00 18.03 ? 84  PHE   C N    1 
ATOM   4550 C  CA   . PHE   C 1 105 ? -31.845 -5.403  55.890  1.00 17.49 ? 84  PHE   C CA   1 
ATOM   4551 C  C    . PHE   C 1 105 ? -32.074 -6.906  55.730  1.00 17.22 ? 84  PHE   C C    1 
ATOM   4552 O  O    . PHE   C 1 105 ? -33.167 -7.398  56.038  1.00 19.97 ? 84  PHE   C O    1 
ATOM   4553 C  CB   . PHE   C 1 105 ? -32.751 -4.642  54.915  1.00 16.95 ? 84  PHE   C CB   1 
ATOM   4554 C  CG   . PHE   C 1 105 ? -32.637 -3.128  54.996  1.00 17.02 ? 84  PHE   C CG   1 
ATOM   4555 C  CD1  . PHE   C 1 105 ? -32.692 -2.451  56.217  1.00 16.38 ? 84  PHE   C CD1  1 
ATOM   4556 C  CD2  . PHE   C 1 105 ? -32.467 -2.380  53.837  1.00 15.63 ? 84  PHE   C CD2  1 
ATOM   4557 C  CE1  . PHE   C 1 105 ? -32.609 -1.062  56.276  1.00 17.07 ? 84  PHE   C CE1  1 
ATOM   4558 C  CE2  . PHE   C 1 105 ? -32.380 -0.995  53.897  1.00 16.05 ? 84  PHE   C CE2  1 
ATOM   4559 C  CZ   . PHE   C 1 105 ? -32.446 -0.333  55.116  1.00 18.06 ? 84  PHE   C CZ   1 
ATOM   4560 N  N    . GLY   C 1 106 ? -31.069 -7.621  55.217  1.00 17.98 ? 85  GLY   C N    1 
ATOM   4561 C  CA   . GLY   C 1 106 ? -31.136 -9.075  55.172  1.00 17.56 ? 85  GLY   C CA   1 
ATOM   4562 C  C    . GLY   C 1 106 ? -31.941 -9.627  53.988  1.00 19.22 ? 85  GLY   C C    1 
ATOM   4563 O  O    . GLY   C 1 106 ? -32.096 -10.843 53.846  1.00 20.82 ? 85  GLY   C O    1 
ATOM   4564 N  N    . ARG   C 1 107 ? -32.444 -8.735  53.133  1.00 17.03 ? 86  ARG   C N    1 
ATOM   4565 C  CA   . ARG   C 1 107 ? -33.290 -9.134  52.018  1.00 18.61 ? 86  ARG   C CA   1 
ATOM   4566 C  C    . ARG   C 1 107 ? -33.300 -7.981  51.026  1.00 17.79 ? 86  ARG   C C    1 
ATOM   4567 O  O    . ARG   C 1 107 ? -32.950 -6.856  51.386  1.00 17.98 ? 86  ARG   C O    1 
ATOM   4568 C  CB   . ARG   C 1 107 ? -34.712 -9.407  52.529  1.00 18.88 ? 86  ARG   C CB   1 
ATOM   4569 C  CG   . ARG   C 1 107 ? -35.410 -8.221  53.190  1.00 20.45 ? 86  ARG   C CG   1 
ATOM   4570 C  CD   . ARG   C 1 107 ? -36.714 -8.630  53.848  1.00 22.54 ? 86  ARG   C CD   1 
ATOM   4571 N  NE   . ARG   C 1 107 ? -37.751 -9.057  52.901  1.00 21.47 ? 86  ARG   C NE   1 
ATOM   4572 C  CZ   . ARG   C 1 107 ? -38.917 -9.601  53.220  1.00 26.14 ? 86  ARG   C CZ   1 
ATOM   4573 N  NH1  . ARG   C 1 107 ? -39.223 -9.846  54.487  1.00 29.39 ? 86  ARG   C NH1  1 
ATOM   4574 N  NH2  . ARG   C 1 107 ? -39.778 -9.928  52.276  1.00 23.42 ? 86  ARG   C NH2  1 
ATOM   4575 N  N    . CYS   C 1 108 ? -33.759 -8.261  49.795  1.00 18.20 ? 87  CYS   C N    1 
ATOM   4576 C  CA   . CYS   C 1 108 ? -33.918 -7.209  48.799  1.00 16.99 ? 87  CYS   C CA   1 
ATOM   4577 C  C    . CYS   C 1 108 ? -35.080 -7.607  47.894  1.00 17.41 ? 87  CYS   C C    1 
ATOM   4578 O  O    . CYS   C 1 108 ? -34.942 -8.558  47.115  1.00 19.21 ? 87  CYS   C O    1 
ATOM   4579 C  CB   . CYS   C 1 108 ? -32.639 -7.055  47.981  1.00 17.28 ? 87  CYS   C CB   1 
ATOM   4580 S  SG   . CYS   C 1 108 ? -32.727 -5.676  46.803  1.00 19.88 ? 87  CYS   C SG   1 
ATOM   4581 N  N    . ASP   C 1 109 ? -36.211 -6.912  48.035  1.00 16.30 ? 88  ASP   C N    1 
ATOM   4582 C  CA   . ASP   C 1 109 ? -37.452 -7.310  47.379  1.00 16.24 ? 88  ASP   C CA   1 
ATOM   4583 C  C    . ASP   C 1 109 ? -37.713 -6.531  46.094  1.00 15.68 ? 88  ASP   C C    1 
ATOM   4584 O  O    . ASP   C 1 109 ? -38.360 -7.055  45.188  1.00 15.43 ? 88  ASP   C O    1 
ATOM   4585 C  CB   . ASP   C 1 109 ? -38.633 -7.129  48.309  1.00 16.92 ? 88  ASP   C CB   1 
ATOM   4586 C  CG   . ASP   C 1 109 ? -38.473 -7.967  49.562  1.00 20.21 ? 88  ASP   C CG   1 
ATOM   4587 O  OD1  . ASP   C 1 109 ? -37.792 -7.488  50.480  1.00 21.23 ? 88  ASP   C OD1  1 
ATOM   4588 O  OD2  . ASP   C 1 109 ? -38.892 -9.142  49.523  1.00 21.39 ? 88  ASP   C OD2  1 
ATOM   4589 N  N    . VAL   C 1 110 ? -37.279 -5.264  46.051  1.00 15.25 ? 89  VAL   C N    1 
ATOM   4590 C  CA   . VAL   C 1 110 ? -37.587 -4.373  44.944  1.00 15.40 ? 89  VAL   C CA   1 
ATOM   4591 C  C    . VAL   C 1 110 ? -36.315 -3.631  44.543  1.00 16.01 ? 89  VAL   C C    1 
ATOM   4592 O  O    . VAL   C 1 110 ? -35.554 -3.168  45.404  1.00 15.04 ? 89  VAL   C O    1 
ATOM   4593 C  CB   . VAL   C 1 110 ? -38.651 -3.365  45.409  1.00 16.50 ? 89  VAL   C CB   1 
ATOM   4594 C  CG1  . VAL   C 1 110 ? -38.756 -2.138  44.493  1.00 16.76 ? 89  VAL   C CG1  1 
ATOM   4595 C  CG2  . VAL   C 1 110 ? -40.017 -4.021  45.578  1.00 16.86 ? 89  VAL   C CG2  1 
ATOM   4596 N  N    . LEU   C 1 111 ? -36.127 -3.507  43.223  1.00 13.68 ? 90  LEU   C N    1 
ATOM   4597 C  CA   . LEU   C 1 111 ? -35.094 -2.670  42.650  1.00 14.05 ? 90  LEU   C CA   1 
ATOM   4598 C  C    . LEU   C 1 111 ? -35.772 -1.630  41.769  1.00 13.07 ? 90  LEU   C C    1 
ATOM   4599 O  O    . LEU   C 1 111 ? -36.532 -2.014  40.878  1.00 13.59 ? 90  LEU   C O    1 
ATOM   4600 C  CB   . LEU   C 1 111 ? -34.137 -3.531  41.829  1.00 13.88 ? 90  LEU   C CB   1 
ATOM   4601 C  CG   . LEU   C 1 111 ? -33.154 -2.757  40.946  1.00 14.32 ? 90  LEU   C CG   1 
ATOM   4602 C  CD1  . LEU   C 1 111 ? -32.157 -1.912  41.721  1.00 15.28 ? 90  LEU   C CD1  1 
ATOM   4603 C  CD2  . LEU   C 1 111 ? -32.409 -3.754  40.082  1.00 15.32 ? 90  LEU   C CD2  1 
ATOM   4604 N  N    . VAL   C 1 112 ? -35.449 -0.338  41.980  1.00 13.10 ? 91  VAL   C N    1 
ATOM   4605 C  CA   . VAL   C 1 112 ? -35.929 0.735   41.110  1.00 13.03 ? 91  VAL   C CA   1 
ATOM   4606 C  C    . VAL   C 1 112 ? -34.717 1.352   40.411  1.00 13.34 ? 91  VAL   C C    1 
ATOM   4607 O  O    . VAL   C 1 112 ? -33.861 1.972   41.048  1.00 14.29 ? 91  VAL   C O    1 
ATOM   4608 C  CB   . VAL   C 1 112 ? -36.766 1.799   41.840  1.00 13.96 ? 91  VAL   C CB   1 
ATOM   4609 C  CG1  . VAL   C 1 112 ? -37.216 2.890   40.875  1.00 15.15 ? 91  VAL   C CG1  1 
ATOM   4610 C  CG2  . VAL   C 1 112 ? -37.966 1.181   42.547  1.00 14.78 ? 91  VAL   C CG2  1 
ATOM   4611 N  N    . ASN   C 1 113 ? -34.620 1.128   39.092  1.00 12.80 ? 92  ASN   C N    1 
ATOM   4612 C  CA   . ASN   C 1 113 ? -33.550 1.732   38.314  1.00 13.24 ? 92  ASN   C CA   1 
ATOM   4613 C  C    . ASN   C 1 113 ? -33.968 3.124   37.844  1.00 14.51 ? 92  ASN   C C    1 
ATOM   4614 O  O    . ASN   C 1 113 ? -34.630 3.267   36.808  1.00 14.63 ? 92  ASN   C O    1 
ATOM   4615 C  CB   . ASN   C 1 113 ? -33.202 0.857   37.117  1.00 14.53 ? 92  ASN   C CB   1 
ATOM   4616 C  CG   . ASN   C 1 113 ? -32.453 -0.395  37.511  1.00 14.64 ? 92  ASN   C CG   1 
ATOM   4617 O  OD1  . ASN   C 1 113 ? -31.397 -0.292  38.135  1.00 14.40 ? 92  ASN   C OD1  1 
ATOM   4618 N  ND2  . ASN   C 1 113 ? -32.960 -1.571  37.147  1.00 14.01 ? 92  ASN   C ND2  1 
ATOM   4619 N  N    . ASN   C 1 114 ? -33.563 4.135   38.604  1.00 13.94 ? 93  ASN   C N    1 
ATOM   4620 C  CA   . ASN   C 1 114 ? -33.973 5.517   38.403  1.00 13.64 ? 93  ASN   C CA   1 
ATOM   4621 C  C    . ASN   C 1 114 ? -32.804 6.397   37.961  1.00 15.86 ? 93  ASN   C C    1 
ATOM   4622 O  O    . ASN   C 1 114 ? -33.046 7.351   37.226  1.00 15.48 ? 93  ASN   C O    1 
ATOM   4623 C  CB   . ASN   C 1 114 ? -34.659 6.022   39.668  1.00 14.23 ? 93  ASN   C CB   1 
ATOM   4624 C  CG   . ASN   C 1 114 ? -34.884 7.515   39.658  1.00 14.74 ? 93  ASN   C CG   1 
ATOM   4625 O  OD1  . ASN   C 1 114 ? -35.890 7.996   39.130  1.00 15.47 ? 93  ASN   C OD1  1 
ATOM   4626 N  ND2  . ASN   C 1 114 ? -33.975 8.249   40.281  1.00 14.43 ? 93  ASN   C ND2  1 
ATOM   4627 N  N    . ALA   C 1 115 ? -31.578 6.123   38.433  1.00 15.22 ? 94  ALA   C N    1 
ATOM   4628 C  CA   . ALA   C 1 115 ? -30.451 7.026   38.171  1.00 15.99 ? 94  ALA   C CA   1 
ATOM   4629 C  C    . ALA   C 1 115 ? -30.259 7.189   36.667  1.00 17.13 ? 94  ALA   C C    1 
ATOM   4630 O  O    . ALA   C 1 115 ? -30.390 6.225   35.912  1.00 17.08 ? 94  ALA   C O    1 
ATOM   4631 C  CB   . ALA   C 1 115 ? -29.171 6.519   38.802  1.00 16.12 ? 94  ALA   C CB   1 
ATOM   4632 N  N    . SER   C 1 116 ? -29.884 8.405   36.242  1.00 17.09 ? 95  SER   C N    1 
ATOM   4633 C  CA   . SER   C 1 116 ? -29.819 8.652   34.811  1.00 17.47 ? 95  SER   C CA   1 
ATOM   4634 C  C    . SER   C 1 116 ? -29.006 9.898   34.515  1.00 18.05 ? 95  SER   C C    1 
ATOM   4635 O  O    . SER   C 1 116 ? -29.297 10.967  35.059  1.00 20.17 ? 95  SER   C O    1 
ATOM   4636 C  CB   . SER   C 1 116 ? -31.215 8.842   34.269  1.00 17.22 ? 95  SER   C CB   1 
ATOM   4637 O  OG   . SER   C 1 116 ? -31.177 9.260   32.903  1.00 19.04 ? 95  SER   C OG   1 
ATOM   4638 N  N    . ALA   C 1 117 ? -28.040 9.760   33.608  1.00 18.33 ? 96  ALA   C N    1 
ATOM   4639 C  CA   . ALA   C 1 117 ? -27.435 10.923  32.988  1.00 16.86 ? 96  ALA   C CA   1 
ATOM   4640 C  C    . ALA   C 1 117 ? -28.296 11.383  31.812  1.00 16.66 ? 96  ALA   C C    1 
ATOM   4641 O  O    . ALA   C 1 117 ? -28.877 10.587  31.083  1.00 16.40 ? 96  ALA   C O    1 
ATOM   4642 C  CB   . ALA   C 1 117 ? -26.026 10.572  32.529  1.00 17.12 ? 96  ALA   C CB   1 
ATOM   4643 N  N    . PHE   C 1 118 ? -28.338 12.703  31.603  1.00 16.80 ? 97  PHE   C N    1 
ATOM   4644 C  CA   . PHE   C 1 118 ? -29.187 13.267  30.571  1.00 16.45 ? 97  PHE   C CA   1 
ATOM   4645 C  C    . PHE   C 1 118 ? -28.567 14.573  30.089  1.00 18.62 ? 97  PHE   C C    1 
ATOM   4646 O  O    . PHE   C 1 118 ? -28.627 15.581  30.798  1.00 20.14 ? 97  PHE   C O    1 
ATOM   4647 C  CB   . PHE   C 1 118 ? -30.594 13.527  31.139  1.00 18.24 ? 97  PHE   C CB   1 
ATOM   4648 C  CG   . PHE   C 1 118 ? -31.587 14.269  30.247  1.00 20.53 ? 97  PHE   C CG   1 
ATOM   4649 C  CD1  . PHE   C 1 118 ? -32.132 13.660  29.122  1.00 21.08 ? 97  PHE   C CD1  1 
ATOM   4650 C  CD2  . PHE   C 1 118 ? -32.018 15.556  30.565  1.00 24.09 ? 97  PHE   C CD2  1 
ATOM   4651 C  CE1  . PHE   C 1 118 ? -33.055 14.303  28.312  1.00 23.34 ? 97  PHE   C CE1  1 
ATOM   4652 C  CE2  . PHE   C 1 118 ? -32.957 16.198  29.764  1.00 23.68 ? 97  PHE   C CE2  1 
ATOM   4653 C  CZ   . PHE   C 1 118 ? -33.478 15.576  28.640  1.00 24.39 ? 97  PHE   C CZ   1 
ATOM   4654 N  N    . TYR   C 1 119 ? -28.003 14.544  28.878  1.00 17.39 ? 98  TYR   C N    1 
ATOM   4655 C  CA   . TYR   C 1 119 ? -27.454 15.733  28.253  1.00 16.82 ? 98  TYR   C CA   1 
ATOM   4656 C  C    . TYR   C 1 119 ? -27.249 15.451  26.772  1.00 18.08 ? 98  TYR   C C    1 
ATOM   4657 O  O    . TYR   C 1 119 ? -27.187 14.288  26.344  1.00 16.84 ? 98  TYR   C O    1 
ATOM   4658 C  CB   . TYR   C 1 119 ? -26.148 16.140  28.948  1.00 18.20 ? 98  TYR   C CB   1 
ATOM   4659 C  CG   . TYR   C 1 119 ? -25.054 15.082  29.043  1.00 18.59 ? 98  TYR   C CG   1 
ATOM   4660 C  CD1  . TYR   C 1 119 ? -24.199 14.830  27.980  1.00 19.76 ? 98  TYR   C CD1  1 
ATOM   4661 C  CD2  . TYR   C 1 119 ? -24.832 14.408  30.236  1.00 20.11 ? 98  TYR   C CD2  1 
ATOM   4662 C  CE1  . TYR   C 1 119 ? -23.188 13.885  28.073  1.00 20.08 ? 98  TYR   C CE1  1 
ATOM   4663 C  CE2  . TYR   C 1 119 ? -23.823 13.464  30.351  1.00 19.13 ? 98  TYR   C CE2  1 
ATOM   4664 C  CZ   . TYR   C 1 119 ? -22.989 13.220  29.271  1.00 19.61 ? 98  TYR   C CZ   1 
ATOM   4665 O  OH   . TYR   C 1 119 ? -21.972 12.317  29.383  1.00 21.33 ? 98  TYR   C OH   1 
ATOM   4666 N  N    . PRO   C 1 120 ? -27.134 16.498  25.939  1.00 17.54 ? 99  PRO   C N    1 
ATOM   4667 C  CA   . PRO   C 1 120 ? -27.009 16.284  24.501  1.00 18.44 ? 99  PRO   C CA   1 
ATOM   4668 C  C    . PRO   C 1 120 ? -25.626 15.781  24.102  1.00 18.93 ? 99  PRO   C C    1 
ATOM   4669 O  O    . PRO   C 1 120 ? -24.615 16.103  24.741  1.00 20.91 ? 99  PRO   C O    1 
ATOM   4670 C  CB   . PRO   C 1 120 ? -27.340 17.621  23.858  1.00 20.25 ? 99  PRO   C CB   1 
ATOM   4671 C  CG   . PRO   C 1 120 ? -27.279 18.621  24.990  1.00 21.10 ? 99  PRO   C CG   1 
ATOM   4672 C  CD   . PRO   C 1 120 ? -27.237 17.919  26.331  1.00 18.96 ? 99  PRO   C CD   1 
ATOM   4673 N  N    . THR   C 1 121 ? -25.631 14.942  23.061  1.00 17.04 ? 100 THR   C N    1 
ATOM   4674 C  CA   . THR   C 1 121 ? -24.433 14.368  22.480  1.00 17.60 ? 100 THR   C CA   1 
ATOM   4675 C  C    . THR   C 1 121 ? -24.582 14.483  20.970  1.00 18.29 ? 100 THR   C C    1 
ATOM   4676 O  O    . THR   C 1 121 ? -24.920 13.509  20.298  1.00 17.71 ? 100 THR   C O    1 
ATOM   4677 C  CB   . THR   C 1 121 ? -24.264 12.912  22.913  1.00 17.89 ? 100 THR   C CB   1 
ATOM   4678 O  OG1  . THR   C 1 121 ? -25.433 12.186  22.531  1.00 18.44 ? 100 THR   C OG1  1 
ATOM   4679 C  CG2  . THR   C 1 121 ? -24.051 12.790  24.408  1.00 17.95 ? 100 THR   C CG2  1 
ATOM   4680 N  N    . PRO   C 1 122 ? -24.338 15.671  20.374  1.00 17.40 ? 101 PRO   C N    1 
ATOM   4681 C  CA   . PRO   C 1 122 ? -24.532 15.863  18.939  1.00 17.88 ? 101 PRO   C CA   1 
ATOM   4682 C  C    . PRO   C 1 122 ? -23.693 14.887  18.114  1.00 18.58 ? 101 PRO   C C    1 
ATOM   4683 O  O    . PRO   C 1 122 ? -22.559 14.546  18.477  1.00 19.78 ? 101 PRO   C O    1 
ATOM   4684 C  CB   . PRO   C 1 122 ? -24.114 17.340  18.681  1.00 19.04 ? 101 PRO   C CB   1 
ATOM   4685 C  CG   . PRO   C 1 122 ? -24.110 17.987  20.042  1.00 20.85 ? 101 PRO   C CG   1 
ATOM   4686 C  CD   . PRO   C 1 122 ? -23.893 16.896  21.070  1.00 19.27 ? 101 PRO   C CD   1 
ATOM   4687 N  N    . LEU   C 1 123 ? -24.238 14.486  16.961  1.00 18.67 ? 102 LEU   C N    1 
ATOM   4688 C  CA   . LEU   C 1 123 ? -23.508 13.588  16.087  1.00 19.01 ? 102 LEU   C CA   1 
ATOM   4689 C  C    . LEU   C 1 123 ? -22.368 14.312  15.386  1.00 23.35 ? 102 LEU   C C    1 
ATOM   4690 O  O    . LEU   C 1 123 ? -21.391 13.688  14.995  1.00 25.48 ? 102 LEU   C O    1 
ATOM   4691 C  CB   . LEU   C 1 123 ? -24.465 12.977  15.069  1.00 19.14 ? 102 LEU   C CB   1 
ATOM   4692 C  CG   . LEU   C 1 123 ? -25.452 11.982  15.678  1.00 17.92 ? 102 LEU   C CG   1 
ATOM   4693 C  CD1  . LEU   C 1 123 ? -26.543 11.642  14.666  1.00 17.70 ? 102 LEU   C CD1  1 
ATOM   4694 C  CD2  . LEU   C 1 123 ? -24.691 10.719  16.080  1.00 19.36 ? 102 LEU   C CD2  1 
ATOM   4695 N  N    . VAL   C 1 124 ? -22.537 15.620  15.197  1.00 26.30 ? 103 VAL   C N    1 
ATOM   4696 C  CA   . VAL   C 1 124 ? -21.469 16.436  14.650  1.00 31.34 ? 103 VAL   C CA   1 
ATOM   4697 C  C    . VAL   C 1 124 ? -20.996 17.360  15.769  1.00 33.78 ? 103 VAL   C C    1 
ATOM   4698 O  O    . VAL   C 1 124 ? -21.662 18.347  16.082  1.00 33.45 ? 103 VAL   C O    1 
ATOM   4699 C  CB   . VAL   C 1 124 ? -21.966 17.191  13.401  1.00 33.17 ? 103 VAL   C CB   1 
ATOM   4700 C  CG1  . VAL   C 1 124 ? -20.865 18.035  12.762  1.00 36.59 ? 103 VAL   C CG1  1 
ATOM   4701 C  CG2  . VAL   C 1 124 ? -22.554 16.235  12.365  1.00 34.11 ? 103 VAL   C CG2  1 
ATOM   4702 N  N    . GLN   C 1 125 ? -19.857 16.987  16.369  0.70 31.40 ? 104 GLN   C N    1 
ATOM   4703 C  CA   . GLN   C 1 125 ? -19.237 17.698  17.476  0.70 33.98 ? 104 GLN   C CA   1 
ATOM   4704 C  C    . GLN   C 1 125 ? -17.983 18.436  16.974  0.70 36.62 ? 104 GLN   C C    1 
ATOM   4705 O  O    . GLN   C 1 125 ? -18.124 19.170  15.970  0.70 38.47 ? 104 GLN   C O    1 
ATOM   4706 C  CB   . GLN   C 1 125 ? -18.951 16.711  18.609  0.70 32.82 ? 104 GLN   C CB   1 
ATOM   4707 C  CG   . GLN   C 1 125 ? -20.197 16.378  19.427  0.70 30.33 ? 104 GLN   C CG   1 
ATOM   4708 C  CD   . GLN   C 1 125 ? -20.000 15.352  20.526  0.70 29.61 ? 104 GLN   C CD   1 
ATOM   4709 O  OE1  . GLN   C 1 125 ? -20.916 14.588  20.868  0.70 24.58 ? 104 GLN   C OE1  1 
ATOM   4710 N  NE2  . GLN   C 1 125 ? -18.824 15.368  21.141  0.70 27.53 ? 104 GLN   C NE2  1 
ATOM   4711 N  N    . LYS   C 1 135 ? -16.501 17.018  27.635  1.00 31.18 ? 114 LYS   C N    1 
ATOM   4712 C  CA   . LYS   C 1 135 ? -16.359 15.547  27.821  1.00 27.11 ? 114 LYS   C CA   1 
ATOM   4713 C  C    . LYS   C 1 135 ? -15.968 14.896  26.500  1.00 24.30 ? 114 LYS   C C    1 
ATOM   4714 O  O    . LYS   C 1 135 ? -16.516 15.243  25.459  1.00 26.54 ? 114 LYS   C O    1 
ATOM   4715 C  CB   . LYS   C 1 135 ? -17.693 14.935  28.264  1.00 29.40 ? 114 LYS   C CB   1 
ATOM   4716 C  CG   . LYS   C 1 135 ? -18.153 15.384  29.639  1.00 30.93 ? 114 LYS   C CG   1 
ATOM   4717 C  CD   A LYS   C 1 135 ? -19.489 14.852  30.133  0.60 30.06 ? 114 LYS   C CD   1 
ATOM   4718 C  CE   A LYS   C 1 135 ? -19.494 14.983  31.621  0.60 27.82 ? 114 LYS   C CE   1 
ATOM   4719 N  NZ   A LYS   C 1 135 ? -20.846 14.791  32.133  0.60 28.48 ? 114 LYS   C NZ   1 
ATOM   4720 N  N    . THR   C 1 136 ? -15.058 13.914  26.556  1.00 23.48 ? 115 THR   C N    1 
ATOM   4721 C  CA   . THR   C 1 136 ? -14.714 13.097  25.404  1.00 21.36 ? 115 THR   C CA   1 
ATOM   4722 C  C    . THR   C 1 136 ? -15.936 12.265  25.006  1.00 19.12 ? 115 THR   C C    1 
ATOM   4723 O  O    . THR   C 1 136 ? -16.828 12.029  25.823  1.00 18.95 ? 115 THR   C O    1 
ATOM   4724 C  CB   . THR   C 1 136 ? -13.513 12.192  25.679  1.00 26.03 ? 115 THR   C CB   1 
ATOM   4725 O  OG1  . THR   C 1 136 ? -13.916 11.249  26.666  1.00 25.35 ? 115 THR   C OG1  1 
ATOM   4726 C  CG2  . THR   C 1 136 ? -12.282 12.956  26.142  1.00 28.45 ? 115 THR   C CG2  1 
ATOM   4727 N  N    . VAL   C 1 137 ? -15.959 11.833  23.747  1.00 19.15 ? 116 VAL   C N    1 
ATOM   4728 C  CA   A VAL   C 1 137 ? -17.051 11.007  23.254  0.60 18.33 ? 116 VAL   C CA   1 
ATOM   4729 C  CA   B VAL   C 1 137 ? -17.079 11.027  23.284  0.40 17.84 ? 116 VAL   C CA   1 
ATOM   4730 C  C    . VAL   C 1 137 ? -17.097 9.711   24.063  1.00 17.27 ? 116 VAL   C C    1 
ATOM   4731 O  O    . VAL   C 1 137 ? -18.177 9.226   24.405  1.00 16.69 ? 116 VAL   C O    1 
ATOM   4732 C  CB   A VAL   C 1 137 ? -16.937 10.768  21.735  0.60 21.13 ? 116 VAL   C CB   1 
ATOM   4733 C  CB   B VAL   C 1 137 ? -17.246 10.820  21.762  0.40 18.90 ? 116 VAL   C CB   1 
ATOM   4734 C  CG1  A VAL   C 1 137 ? -17.945 9.740   21.238  0.60 21.96 ? 116 VAL   C CG1  1 
ATOM   4735 C  CG1  B VAL   C 1 137 ? -16.167 9.919   21.179  0.40 19.47 ? 116 VAL   C CG1  1 
ATOM   4736 C  CG2  A VAL   C 1 137 ? -17.102 12.073  20.968  0.60 21.65 ? 116 VAL   C CG2  1 
ATOM   4737 C  CG2  B VAL   C 1 137 ? -18.637 10.302  21.403  0.40 18.26 ? 116 VAL   C CG2  1 
ATOM   4738 N  N    . GLU   C 1 138 ? -15.927 9.148   24.389  1.00 18.78 ? 117 GLU   C N    1 
ATOM   4739 C  CA   . GLU   C 1 138 ? -15.974 7.906   25.157  1.00 19.54 ? 117 GLU   C CA   1 
ATOM   4740 C  C    . GLU   C 1 138 ? -16.567 8.133   26.557  1.00 18.83 ? 117 GLU   C C    1 
ATOM   4741 O  O    . GLU   C 1 138 ? -17.245 7.237   27.063  1.00 19.05 ? 117 GLU   C O    1 
ATOM   4742 C  CB   . GLU   C 1 138 ? -14.679 7.093   25.133  1.00 24.80 ? 117 GLU   C CB   1 
ATOM   4743 C  CG   . GLU   C 1 138 ? -13.484 7.869   25.669  1.00 25.01 ? 117 GLU   C CG   1 
ATOM   4744 C  CD   . GLU   C 1 138 ? -12.779 8.783   24.677  0.70 27.30 ? 117 GLU   C CD   1 
ATOM   4745 O  OE1  . GLU   C 1 138 ? -11.688 9.245   25.071  0.87 31.98 ? 117 GLU   C OE1  1 
ATOM   4746 O  OE2  . GLU   C 1 138 ? -13.266 9.037   23.555  0.70 23.03 ? 117 GLU   C OE2  1 
ATOM   4747 N  N    . THR   C 1 139 ? -16.350 9.315   27.171  1.00 17.49 ? 118 THR   C N    1 
ATOM   4748 C  CA   . THR   C 1 139 ? -16.979 9.629   28.452  1.00 18.25 ? 118 THR   C CA   1 
ATOM   4749 C  C    . THR   C 1 139 ? -18.497 9.720   28.286  1.00 16.31 ? 118 THR   C C    1 
ATOM   4750 O  O    . THR   C 1 139 ? -19.274 9.258   29.128  1.00 16.76 ? 118 THR   C O    1 
ATOM   4751 C  CB   . THR   C 1 139 ? -16.451 10.955  29.005  1.00 21.40 ? 118 THR   C CB   1 
ATOM   4752 O  OG1  . THR   C 1 139 ? -15.085 10.680  29.309  1.00 24.91 ? 118 THR   C OG1  1 
ATOM   4753 C  CG2  . THR   C 1 139 ? -17.196 11.382  30.255  1.00 21.31 ? 118 THR   C CG2  1 
ATOM   4754 N  N    . GLN   C 1 140 ? -18.925 10.354  27.191  1.00 16.27 ? 119 GLN   C N    1 
ATOM   4755 C  CA   A GLN   C 1 140 ? -20.346 10.533  26.900  0.70 15.27 ? 119 GLN   C CA   1 
ATOM   4756 C  CA   B GLN   C 1 140 ? -20.347 10.526  26.941  0.30 15.34 ? 119 GLN   C CA   1 
ATOM   4757 C  C    . GLN   C 1 140 ? -21.015 9.165   26.793  1.00 15.01 ? 119 GLN   C C    1 
ATOM   4758 O  O    . GLN   C 1 140 ? -22.076 8.941   27.377  1.00 15.29 ? 119 GLN   C O    1 
ATOM   4759 C  CB   A GLN   C 1 140 ? -20.495 11.301  25.580  0.70 16.82 ? 119 GLN   C CB   1 
ATOM   4760 C  CB   B GLN   C 1 140 ? -20.565 11.387  25.701  0.30 15.80 ? 119 GLN   C CB   1 
ATOM   4761 C  CG   A GLN   C 1 140 ? -20.072 12.770  25.639  0.70 20.03 ? 119 GLN   C CG   1 
ATOM   4762 C  CG   B GLN   C 1 140 ? -20.035 12.807  25.855  0.30 16.48 ? 119 GLN   C CG   1 
ATOM   4763 C  CD   A GLN   C 1 140 ? -19.947 13.436  24.282  0.70 21.62 ? 119 GLN   C CD   1 
ATOM   4764 C  CD   B GLN   C 1 140 ? -20.503 13.706  24.738  0.30 16.53 ? 119 GLN   C CD   1 
ATOM   4765 O  OE1  A GLN   C 1 140 ? -18.937 14.083  23.974  0.70 23.70 ? 119 GLN   C OE1  1 
ATOM   4766 O  OE1  B GLN   C 1 140 ? -20.914 14.849  24.962  0.30 17.67 ? 119 GLN   C OE1  1 
ATOM   4767 N  NE2  A GLN   C 1 140 ? -20.971 13.314  23.448  0.70 20.79 ? 119 GLN   C NE2  1 
ATOM   4768 N  NE2  B GLN   C 1 140 ? -20.440 13.192  23.517  0.30 16.88 ? 119 GLN   C NE2  1 
ATOM   4769 N  N    . VAL   C 1 141 ? -20.399 8.270   25.999  1.00 15.18 ? 120 VAL   C N    1 
ATOM   4770 C  CA   . VAL   C 1 141 ? -20.877 6.897   25.880  1.00 14.47 ? 120 VAL   C CA   1 
ATOM   4771 C  C    . VAL   C 1 141 ? -20.943 6.259   27.278  1.00 14.17 ? 120 VAL   C C    1 
ATOM   4772 O  O    . VAL   C 1 141 ? -21.968 5.672   27.650  1.00 14.11 ? 120 VAL   C O    1 
ATOM   4773 C  CB   . VAL   C 1 141 ? -19.967 6.078   24.945  1.00 14.21 ? 120 VAL   C CB   1 
ATOM   4774 C  CG1  . VAL   C 1 141 ? -20.278 4.577   25.041  1.00 14.47 ? 120 VAL   C CG1  1 
ATOM   4775 C  CG2  . VAL   C 1 141 ? -20.047 6.545   23.495  1.00 14.67 ? 120 VAL   C CG2  1 
ATOM   4776 N  N    . ALA   C 1 142 ? -19.840 6.330   28.035  1.00 14.74 ? 121 ALA   C N    1 
ATOM   4777 C  CA   . ALA   C 1 142 ? -19.790 5.646   29.324  1.00 13.82 ? 121 ALA   C CA   1 
ATOM   4778 C  C    . ALA   C 1 142 ? -20.887 6.118   30.271  1.00 14.09 ? 121 ALA   C C    1 
ATOM   4779 O  O    . ALA   C 1 142 ? -21.528 5.306   30.919  1.00 15.54 ? 121 ALA   C O    1 
ATOM   4780 C  CB   . ALA   C 1 142 ? -18.427 5.807   29.957  1.00 15.84 ? 121 ALA   C CB   1 
ATOM   4781 N  N    . GLU   C 1 143 ? -21.102 7.434   30.326  1.00 14.27 ? 122 GLU   C N    1 
ATOM   4782 C  CA   . GLU   C 1 143 ? -22.061 7.992   31.270  1.00 14.99 ? 122 GLU   C CA   1 
ATOM   4783 C  C    . GLU   C 1 143 ? -23.491 7.688   30.826  1.00 15.12 ? 122 GLU   C C    1 
ATOM   4784 O  O    . GLU   C 1 143 ? -24.313 7.230   31.633  1.00 16.02 ? 122 GLU   C O    1 
ATOM   4785 C  CB   . GLU   C 1 143 ? -21.834 9.501   31.379  1.00 15.83 ? 122 GLU   C CB   1 
ATOM   4786 C  CG   . GLU   C 1 143 ? -20.542 9.825   32.123  1.00 18.31 ? 122 GLU   C CG   1 
ATOM   4787 C  CD   . GLU   C 1 143 ? -20.323 11.299  32.406  1.00 21.57 ? 122 GLU   C CD   1 
ATOM   4788 O  OE1  . GLU   C 1 143 ? -21.086 12.096  31.840  1.00 22.26 ? 122 GLU   C OE1  1 
ATOM   4789 O  OE2  . GLU   C 1 143 ? -19.412 11.635  33.221  1.00 24.09 ? 122 GLU   C OE2  1 
ATOM   4790 N  N    . LEU   C 1 144 ? -23.798 7.959   29.551  1.00 14.95 ? 123 LEU   C N    1 
ATOM   4791 C  CA   . LEU   C 1 144 ? -25.187 7.866   29.123  1.00 15.19 ? 123 LEU   C CA   1 
ATOM   4792 C  C    . LEU   C 1 144 ? -25.617 6.413   28.974  1.00 15.00 ? 123 LEU   C C    1 
ATOM   4793 O  O    . LEU   C 1 144 ? -26.729 6.083   29.360  1.00 15.97 ? 123 LEU   C O    1 
ATOM   4794 C  CB   . LEU   C 1 144 ? -25.383 8.665   27.844  1.00 15.80 ? 123 LEU   C CB   1 
ATOM   4795 C  CG   . LEU   C 1 144 ? -25.359 10.176  28.102  1.00 17.63 ? 123 LEU   C CG   1 
ATOM   4796 C  CD1  . LEU   C 1 144 ? -25.059 10.927  26.852  1.00 19.74 ? 123 LEU   C CD1  1 
ATOM   4797 C  CD2  . LEU   C 1 144 ? -26.697 10.643  28.694  1.00 20.76 ? 123 LEU   C CD2  1 
ATOM   4798 N  N    . ILE   C 1 145 ? -24.763 5.549   28.421  1.00 14.88 ? 124 ILE   C N    1 
ATOM   4799 C  CA   . ILE   C 1 145 ? -25.156 4.157   28.245  1.00 14.91 ? 124 ILE   C CA   1 
ATOM   4800 C  C    . ILE   C 1 145 ? -24.958 3.410   29.564  1.00 15.88 ? 124 ILE   C C    1 
ATOM   4801 O  O    . ILE   C 1 145 ? -25.744 2.520   29.894  1.00 15.33 ? 124 ILE   C O    1 
ATOM   4802 C  CB   . ILE   C 1 145 ? -24.368 3.520   27.082  1.00 14.07 ? 124 ILE   C CB   1 
ATOM   4803 C  CG1  . ILE   C 1 145 ? -24.491 4.304   25.781  1.00 15.58 ? 124 ILE   C CG1  1 
ATOM   4804 C  CG2  . ILE   C 1 145 ? -24.777 2.054   26.886  1.00 13.93 ? 124 ILE   C CG2  1 
ATOM   4805 C  CD1  . ILE   C 1 145 ? -25.937 4.451   25.313  1.00 17.71 ? 124 ILE   C CD1  1 
ATOM   4806 N  N    . GLY   C 1 146 ? -23.943 3.801   30.355  1.00 15.03 ? 125 GLY   C N    1 
ATOM   4807 C  CA   . GLY   C 1 146 ? -23.753 3.207   31.668  1.00 15.67 ? 125 GLY   C CA   1 
ATOM   4808 C  C    . GLY   C 1 146 ? -24.953 3.420   32.585  1.00 15.30 ? 125 GLY   C C    1 
ATOM   4809 O  O    . GLY   C 1 146 ? -25.549 2.472   33.078  1.00 15.81 ? 125 GLY   C O    1 
ATOM   4810 N  N    . THR   C 1 147 ? -25.320 4.684   32.826  1.00 14.55 ? 126 THR   C N    1 
ATOM   4811 C  CA   . THR   C 1 147 ? -26.368 4.947   33.799  1.00 15.47 ? 126 THR   C CA   1 
ATOM   4812 C  C    . THR   C 1 147 ? -27.727 4.432   33.331  1.00 15.70 ? 126 THR   C C    1 
ATOM   4813 O  O    . THR   C 1 147 ? -28.491 3.894   34.126  1.00 16.54 ? 126 THR   C O    1 
ATOM   4814 C  CB   . THR   C 1 147 ? -26.448 6.440   34.154  1.00 16.68 ? 126 THR   C CB   1 
ATOM   4815 O  OG1  . THR   C 1 147 ? -26.799 7.127   32.959  1.00 17.95 ? 126 THR   C OG1  1 
ATOM   4816 C  CG2  . THR   C 1 147 ? -25.128 6.983   34.686  1.00 17.48 ? 126 THR   C CG2  1 
ATOM   4817 N  N    . ASN   C 1 148 ? -28.050 4.616   32.041  1.00 15.35 ? 127 ASN   C N    1 
ATOM   4818 C  CA   . ASN   C 1 148 ? -29.401 4.364   31.569  1.00 15.39 ? 127 ASN   C CA   1 
ATOM   4819 C  C    . ASN   C 1 148 ? -29.652 2.899   31.213  1.00 15.22 ? 127 ASN   C C    1 
ATOM   4820 O  O    . ASN   C 1 148 ? -30.813 2.486   31.145  1.00 15.98 ? 127 ASN   C O    1 
ATOM   4821 C  CB   . ASN   C 1 148 ? -29.739 5.249   30.378  1.00 14.99 ? 127 ASN   C CB   1 
ATOM   4822 C  CG   . ASN   C 1 148 ? -29.945 6.670   30.847  1.00 17.10 ? 127 ASN   C CG   1 
ATOM   4823 O  OD1  . ASN   C 1 148 ? -30.940 6.942   31.534  1.00 18.71 ? 127 ASN   C OD1  1 
ATOM   4824 N  ND2  . ASN   C 1 148 ? -29.081 7.576   30.427  1.00 16.58 ? 127 ASN   C ND2  1 
ATOM   4825 N  N    . ALA   C 1 149 ? -28.582 2.137   30.931  1.00 14.58 ? 128 ALA   C N    1 
ATOM   4826 C  CA   . ALA   C 1 149 ? -28.791 0.782   30.425  1.00 14.27 ? 128 ALA   C CA   1 
ATOM   4827 C  C    . ALA   C 1 149 ? -27.895 -0.263  31.094  1.00 14.25 ? 128 ALA   C C    1 
ATOM   4828 O  O    . ALA   C 1 149 ? -28.391 -1.298  31.549  1.00 14.08 ? 128 ALA   C O    1 
ATOM   4829 C  CB   . ALA   C 1 149 ? -28.577 0.765   28.916  1.00 15.53 ? 128 ALA   C CB   1 
ATOM   4830 N  N    . ILE   C 1 150 ? -26.568 -0.038  31.071  1.00 14.01 ? 129 ILE   C N    1 
ATOM   4831 C  CA   . ILE   C 1 150 ? -25.651 -1.093  31.513  1.00 13.63 ? 129 ILE   C CA   1 
ATOM   4832 C  C    . ILE   C 1 150 ? -25.775 -1.300  33.026  1.00 14.45 ? 129 ILE   C C    1 
ATOM   4833 O  O    . ILE   C 1 150 ? -25.896 -2.424  33.496  1.00 13.91 ? 129 ILE   C O    1 
ATOM   4834 C  CB   . ILE   C 1 150 ? -24.203 -0.808  31.070  1.00 14.81 ? 129 ILE   C CB   1 
ATOM   4835 C  CG1  . ILE   C 1 150 ? -24.108 -0.775  29.530  1.00 16.09 ? 129 ILE   C CG1  1 
ATOM   4836 C  CG2  . ILE   C 1 150 ? -23.289 -1.897  31.641  1.00 14.54 ? 129 ILE   C CG2  1 
ATOM   4837 C  CD1  . ILE   C 1 150 ? -22.756 -0.334  28.987  1.00 18.61 ? 129 ILE   C CD1  1 
ATOM   4838 N  N    . ALA   C 1 151 ? -25.801 -0.210  33.796  1.00 13.59 ? 130 ALA   C N    1 
ATOM   4839 C  CA   . ALA   C 1 151 ? -25.942 -0.367  35.241  1.00 13.22 ? 130 ALA   C CA   1 
ATOM   4840 C  C    . ALA   C 1 151 ? -27.282 -1.025  35.577  1.00 14.06 ? 130 ALA   C C    1 
ATOM   4841 O  O    . ALA   C 1 151 ? -27.324 -1.973  36.362  1.00 14.32 ? 130 ALA   C O    1 
ATOM   4842 C  CB   . ALA   C 1 151 ? -25.712 0.960   35.951  1.00 14.08 ? 130 ALA   C CB   1 
ATOM   4843 N  N    . PRO   C 1 152 ? -28.425 -0.639  34.966  1.00 13.74 ? 131 PRO   C N    1 
ATOM   4844 C  CA   . PRO   C 1 152 ? -29.662 -1.395  35.187  1.00 12.93 ? 131 PRO   C CA   1 
ATOM   4845 C  C    . PRO   C 1 152 ? -29.534 -2.890  34.912  1.00 13.06 ? 131 PRO   C C    1 
ATOM   4846 O  O    . PRO   C 1 152 ? -30.086 -3.685  35.655  1.00 13.64 ? 131 PRO   C O    1 
ATOM   4847 C  CB   . PRO   C 1 152 ? -30.687 -0.690  34.271  1.00 12.73 ? 131 PRO   C CB   1 
ATOM   4848 C  CG   . PRO   C 1 152 ? -30.190 0.753   34.313  1.00 13.29 ? 131 PRO   C CG   1 
ATOM   4849 C  CD   . PRO   C 1 152 ? -28.659 0.654   34.290  1.00 13.39 ? 131 PRO   C CD   1 
ATOM   4850 N  N    . PHE   C 1 153 ? -28.822 -3.266  33.843  1.00 12.80 ? 132 PHE   C N    1 
ATOM   4851 C  CA   . PHE   C 1 153 ? -28.621 -4.672  33.528  1.00 12.84 ? 132 PHE   C CA   1 
ATOM   4852 C  C    . PHE   C 1 153 ? -27.841 -5.364  34.649  1.00 13.53 ? 132 PHE   C C    1 
ATOM   4853 O  O    . PHE   C 1 153 ? -28.218 -6.453  35.079  1.00 13.82 ? 132 PHE   C O    1 
ATOM   4854 C  CB   . PHE   C 1 153 ? -27.979 -4.828  32.139  1.00 14.14 ? 132 PHE   C CB   1 
ATOM   4855 C  CG   . PHE   C 1 153 ? -27.338 -6.186  31.893  1.00 14.40 ? 132 PHE   C CG   1 
ATOM   4856 C  CD1  . PHE   C 1 153 ? -28.095 -7.275  31.466  1.00 15.06 ? 132 PHE   C CD1  1 
ATOM   4857 C  CD2  . PHE   C 1 153 ? -25.969 -6.356  32.118  1.00 15.80 ? 132 PHE   C CD2  1 
ATOM   4858 C  CE1  . PHE   C 1 153 ? -27.497 -8.527  31.305  1.00 14.72 ? 132 PHE   C CE1  1 
ATOM   4859 C  CE2  . PHE   C 1 153 ? -25.378 -7.589  31.928  1.00 16.47 ? 132 PHE   C CE2  1 
ATOM   4860 C  CZ   . PHE   C 1 153 ? -26.133 -8.665  31.514  1.00 16.61 ? 132 PHE   C CZ   1 
ATOM   4861 N  N    . LEU   C 1 154 ? -26.720 -4.760  35.054  1.00 13.63 ? 133 LEU   C N    1 
ATOM   4862 C  CA   . LEU   C 1 154 ? -25.855 -5.374  36.053  1.00 13.69 ? 133 LEU   C CA   1 
ATOM   4863 C  C    . LEU   C 1 154 ? -26.564 -5.459  37.397  1.00 14.13 ? 133 LEU   C C    1 
ATOM   4864 O  O    . LEU   C 1 154 ? -26.420 -6.463  38.093  1.00 14.52 ? 133 LEU   C O    1 
ATOM   4865 C  CB   . LEU   C 1 154 ? -24.534 -4.615  36.131  1.00 14.47 ? 133 LEU   C CB   1 
ATOM   4866 C  CG   . LEU   C 1 154 ? -23.667 -4.670  34.871  1.00 14.95 ? 133 LEU   C CG   1 
ATOM   4867 C  CD1  . LEU   C 1 154 ? -22.588 -3.615  34.983  1.00 16.04 ? 133 LEU   C CD1  1 
ATOM   4868 C  CD2  . LEU   C 1 154 ? -23.089 -6.077  34.637  1.00 15.98 ? 133 LEU   C CD2  1 
ATOM   4869 N  N    . LEU   C 1 155 ? -27.309 -4.406  37.767  1.00 13.63 ? 134 LEU   C N    1 
ATOM   4870 C  CA   . LEU   C 1 155 ? -28.113 -4.426  38.981  1.00 14.36 ? 134 LEU   C CA   1 
ATOM   4871 C  C    . LEU   C 1 155 ? -29.170 -5.526  38.918  1.00 13.72 ? 134 LEU   C C    1 
ATOM   4872 O  O    . LEU   C 1 155 ? -29.445 -6.192  39.922  1.00 14.68 ? 134 LEU   C O    1 
ATOM   4873 C  CB   . LEU   C 1 155 ? -28.717 -3.039  39.207  1.00 13.69 ? 134 LEU   C CB   1 
ATOM   4874 C  CG   . LEU   C 1 155 ? -27.697 -1.973  39.602  1.00 14.08 ? 134 LEU   C CG   1 
ATOM   4875 C  CD1  . LEU   C 1 155 ? -28.266 -0.567  39.397  1.00 15.30 ? 134 LEU   C CD1  1 
ATOM   4876 C  CD2  . LEU   C 1 155 ? -27.294 -2.154  41.061  1.00 15.07 ? 134 LEU   C CD2  1 
ATOM   4877 N  N    . THR   C 1 156 ? -29.756 -5.729  37.720  1.00 14.08 ? 135 THR   C N    1 
ATOM   4878 C  CA   . THR   C 1 156 ? -30.794 -6.734  37.535  1.00 13.16 ? 135 THR   C CA   1 
ATOM   4879 C  C    . THR   C 1 156 ? -30.178 -8.111  37.742  1.00 14.09 ? 135 THR   C C    1 
ATOM   4880 O  O    . THR   C 1 156 ? -30.785 -8.952  38.395  1.00 16.00 ? 135 THR   C O    1 
ATOM   4881 C  CB   . THR   C 1 156 ? -31.434 -6.640  36.138  1.00 13.33 ? 135 THR   C CB   1 
ATOM   4882 O  OG1  . THR   C 1 156 ? -32.115 -5.384  36.153  1.00 15.17 ? 135 THR   C OG1  1 
ATOM   4883 C  CG2  . THR   C 1 156 ? -32.453 -7.738  35.879  1.00 14.18 ? 135 THR   C CG2  1 
ATOM   4884 N  N    . MET   C 1 157 ? -28.998 -8.318  37.166  1.00 14.60 ? 136 MET   C N    1 
ATOM   4885 C  CA   A MET   C 1 157 ? -28.285 -9.571  37.332  0.70 15.96 ? 136 MET   C CA   1 
ATOM   4886 C  CA   B MET   C 1 157 ? -28.243 -9.554  37.334  0.30 14.93 ? 136 MET   C CA   1 
ATOM   4887 C  C    . MET   C 1 157 ? -27.997 -9.842  38.816  1.00 16.02 ? 136 MET   C C    1 
ATOM   4888 O  O    . MET   C 1 157 ? -28.261 -10.949 39.310  1.00 16.63 ? 136 MET   C O    1 
ATOM   4889 C  CB   A MET   C 1 157 ? -26.980 -9.475  36.538  0.70 19.96 ? 136 MET   C CB   1 
ATOM   4890 C  CB   B MET   C 1 157 ? -26.874 -9.453  36.650  0.30 15.00 ? 136 MET   C CB   1 
ATOM   4891 C  CG   A MET   C 1 157 ? -26.208 -10.756 36.481  0.70 22.50 ? 136 MET   C CG   1 
ATOM   4892 C  CG   B MET   C 1 157 ? -26.880 -9.789  35.176  0.30 14.02 ? 136 MET   C CG   1 
ATOM   4893 S  SD   A MET   C 1 157 ? -24.794 -10.448 35.401  0.70 31.57 ? 136 MET   C SD   1 
ATOM   4894 S  SD   B MET   C 1 157 ? -25.196 -9.867  34.533  0.30 14.82 ? 136 MET   C SD   1 
ATOM   4895 C  CE   A MET   C 1 157 ? -24.684 -12.110 34.731  0.70 30.49 ? 136 MET   C CE   1 
ATOM   4896 C  CE   B MET   C 1 157 ? -24.525 -10.924 35.825  0.30 13.82 ? 136 MET   C CE   1 
ATOM   4897 N  N    . SER   C 1 158 ? -27.457 -8.845  39.532  1.00 16.55 ? 137 SER   C N    1 
ATOM   4898 C  CA   . SER   C 1 158 ? -27.096 -9.041  40.934  1.00 15.44 ? 137 SER   C CA   1 
ATOM   4899 C  C    . SER   C 1 158 ? -28.340 -9.302  41.784  1.00 16.92 ? 137 SER   C C    1 
ATOM   4900 O  O    . SER   C 1 158 ? -28.322 -10.135 42.684  1.00 17.99 ? 137 SER   C O    1 
ATOM   4901 C  CB   . SER   C 1 158 ? -26.336 -7.865  41.462  1.00 17.58 ? 137 SER   C CB   1 
ATOM   4902 O  OG   . SER   C 1 158 ? -25.038 -7.853  40.884  1.00 21.89 ? 137 SER   C OG   1 
ATOM   4903 N  N    . PHE   C 1 159 ? -29.427 -8.578  41.490  1.00 16.45 ? 138 PHE   C N    1 
ATOM   4904 C  CA   . PHE   C 1 159 ? -30.679 -8.737  42.211  1.00 16.53 ? 138 PHE   C CA   1 
ATOM   4905 C  C    . PHE   C 1 159 ? -31.199 -10.156 42.011  1.00 18.47 ? 138 PHE   C C    1 
ATOM   4906 O  O    . PHE   C 1 159 ? -31.626 -10.802 42.962  1.00 19.06 ? 138 PHE   C O    1 
ATOM   4907 C  CB   . PHE   C 1 159 ? -31.681 -7.697  41.685  1.00 16.02 ? 138 PHE   C CB   1 
ATOM   4908 C  CG   . PHE   C 1 159 ? -33.076 -7.776  42.300  1.00 14.84 ? 138 PHE   C CG   1 
ATOM   4909 C  CD1  . PHE   C 1 159 ? -34.040 -8.624  41.759  1.00 16.17 ? 138 PHE   C CD1  1 
ATOM   4910 C  CD2  . PHE   C 1 159 ? -33.420 -7.005  43.405  1.00 15.86 ? 138 PHE   C CD2  1 
ATOM   4911 C  CE1  . PHE   C 1 159 ? -35.312 -8.705  42.318  1.00 17.01 ? 138 PHE   C CE1  1 
ATOM   4912 C  CE2  . PHE   C 1 159 ? -34.705 -7.068  43.957  1.00 16.41 ? 138 PHE   C CE2  1 
ATOM   4913 C  CZ   . PHE   C 1 159 ? -35.641 -7.928  43.426  1.00 16.91 ? 138 PHE   C CZ   1 
ATOM   4914 N  N    . ALA   C 1 160 ? -31.210 -10.604 40.755  1.00 17.38 ? 139 ALA   C N    1 
ATOM   4915 C  CA   . ALA   C 1 160 ? -31.758 -11.901 40.414  1.00 18.61 ? 139 ALA   C CA   1 
ATOM   4916 C  C    . ALA   C 1 160 ? -30.937 -13.012 41.053  1.00 20.43 ? 139 ALA   C C    1 
ATOM   4917 O  O    . ALA   C 1 160 ? -31.532 -13.975 41.527  1.00 23.90 ? 139 ALA   C O    1 
ATOM   4918 C  CB   . ALA   C 1 160 ? -31.833 -12.073 38.908  1.00 18.65 ? 139 ALA   C CB   1 
ATOM   4919 N  N    . GLN   C 1 161 ? -29.603 -12.868 41.052  1.00 19.75 ? 140 GLN   C N    1 
ATOM   4920 C  CA   A GLN   C 1 161 ? -28.735 -13.952 41.485  0.50 22.84 ? 140 GLN   C CA   1 
ATOM   4921 C  CA   B GLN   C 1 161 ? -28.705 -13.931 41.494  0.50 21.82 ? 140 GLN   C CA   1 
ATOM   4922 C  C    . GLN   C 1 161 ? -29.005 -14.301 42.946  1.00 25.46 ? 140 GLN   C C    1 
ATOM   4923 O  O    . GLN   C 1 161 ? -28.777 -15.437 43.360  1.00 27.30 ? 140 GLN   C O    1 
ATOM   4924 C  CB   A GLN   C 1 161 ? -27.265 -13.658 41.195  0.50 24.69 ? 140 GLN   C CB   1 
ATOM   4925 C  CB   B GLN   C 1 161 ? -27.234 -13.561 41.287  0.50 21.94 ? 140 GLN   C CB   1 
ATOM   4926 C  CG   A GLN   C 1 161 ? -26.887 -13.837 39.730  0.50 27.55 ? 140 GLN   C CG   1 
ATOM   4927 C  CG   B GLN   C 1 161 ? -26.246 -14.700 41.533  0.50 22.13 ? 140 GLN   C CG   1 
ATOM   4928 C  CD   A GLN   C 1 161 ? -25.393 -13.927 39.524  0.50 30.19 ? 140 GLN   C CD   1 
ATOM   4929 C  CD   B GLN   C 1 161 ? -26.403 -15.856 40.569  0.50 23.73 ? 140 GLN   C CD   1 
ATOM   4930 O  OE1  A GLN   C 1 161 ? -24.648 -12.969 39.756  0.50 35.08 ? 140 GLN   C OE1  1 
ATOM   4931 O  OE1  B GLN   C 1 161 ? -26.607 -15.672 39.363  0.50 24.89 ? 140 GLN   C OE1  1 
ATOM   4932 N  NE2  A GLN   C 1 161 ? -24.941 -15.093 39.087  0.50 34.71 ? 140 GLN   C NE2  1 
ATOM   4933 N  NE2  B GLN   C 1 161 ? -26.302 -17.069 41.094  0.50 24.73 ? 140 GLN   C NE2  1 
ATOM   4934 N  N    . ARG   C 1 162 ? -29.509 -13.331 43.710  1.00 26.04 ? 141 ARG   C N    1 
ATOM   4935 C  CA   . ARG   C 1 162 ? -29.905 -13.558 45.096  1.00 28.48 ? 141 ARG   C CA   1 
ATOM   4936 C  C    . ARG   C 1 162 ? -31.184 -14.384 45.205  1.00 33.91 ? 141 ARG   C C    1 
ATOM   4937 O  O    . ARG   C 1 162 ? -31.392 -15.089 46.195  1.00 37.31 ? 141 ARG   C O    1 
ATOM   4938 C  CB   . ARG   C 1 162 ? -30.230 -12.193 45.690  1.00 27.25 ? 141 ARG   C CB   1 
ATOM   4939 C  CG   . ARG   C 1 162 ? -28.947 -11.391 45.797  1.00 24.83 ? 141 ARG   C CG   1 
ATOM   4940 C  CD   A ARG   C 1 162 ? -28.180 -11.932 46.969  0.70 25.71 ? 141 ARG   C CD   1 
ATOM   4941 N  NE   A ARG   C 1 162 ? -26.996 -11.077 47.034  0.70 25.97 ? 141 ARG   C NE   1 
ATOM   4942 C  CZ   A ARG   C 1 162 ? -26.225 -10.918 48.096  0.70 25.31 ? 141 ARG   C CZ   1 
ATOM   4943 N  NH1  A ARG   C 1 162 ? -26.503 -11.556 49.219  0.70 27.31 ? 141 ARG   C NH1  1 
ATOM   4944 N  NH2  A ARG   C 1 162 ? -25.203 -10.082 48.021  0.70 26.27 ? 141 ARG   C NH2  1 
ATOM   4945 N  N    . GLN   C 1 163 ? -32.046 -14.311 44.190  1.00 36.86 ? 142 GLN   C N    1 
ATOM   4946 C  CA   . GLN   C 1 163 ? -33.398 -14.814 44.369  1.00 40.44 ? 142 GLN   C CA   1 
ATOM   4947 C  C    . GLN   C 1 163 ? -33.628 -15.993 43.405  1.00 47.30 ? 142 GLN   C C    1 
ATOM   4948 O  O    . GLN   C 1 163 ? -33.451 -17.150 43.849  1.00 53.71 ? 142 GLN   C O    1 
ATOM   4949 C  CB   . GLN   C 1 163 ? -34.457 -13.731 44.138  1.00 35.79 ? 142 GLN   C CB   1 
ATOM   4950 C  CG   . GLN   C 1 163 ? -33.958 -12.288 44.096  1.00 29.25 ? 142 GLN   C CG   1 
ATOM   4951 C  CD   . GLN   C 1 163 ? -34.038 -11.462 45.372  1.00 29.32 ? 142 GLN   C CD   1 
ATOM   4952 O  OE1  . GLN   C 1 163 ? -34.587 -11.878 46.403  1.00 26.79 ? 142 GLN   C OE1  1 
ATOM   4953 N  NE2  . GLN   C 1 163 ? -33.498 -10.245 45.307  1.00 25.86 ? 142 GLN   C NE2  1 
ATOM   4954 N  N    . SER   C 1 173 ? -43.827 -13.997 48.691  1.00 40.53 ? 152 SER   C N    1 
ATOM   4955 C  CA   . SER   C 1 173 ? -42.865 -12.949 48.257  1.00 35.37 ? 152 SER   C CA   1 
ATOM   4956 C  C    . SER   C 1 173 ? -43.491 -12.130 47.132  1.00 30.91 ? 152 SER   C C    1 
ATOM   4957 O  O    . SER   C 1 173 ? -44.394 -12.602 46.436  1.00 32.64 ? 152 SER   C O    1 
ATOM   4958 C  CB   . SER   C 1 173 ? -41.546 -13.557 47.838  1.00 38.92 ? 152 SER   C CB   1 
ATOM   4959 N  N    . ASN   C 1 174 ? -43.052 -10.872 47.018  1.00 26.36 ? 153 ASN   C N    1 
ATOM   4960 C  CA   . ASN   C 1 174 ? -43.513 -9.984  45.964  1.00 22.46 ? 153 ASN   C CA   1 
ATOM   4961 C  C    . ASN   C 1 174 ? -42.318 -9.231  45.389  1.00 19.15 ? 153 ASN   C C    1 
ATOM   4962 O  O    . ASN   C 1 174 ? -42.099 -8.053  45.684  1.00 19.56 ? 153 ASN   C O    1 
ATOM   4963 C  CB   . ASN   C 1 174 ? -44.560 -9.021  46.503  1.00 24.58 ? 153 ASN   C CB   1 
ATOM   4964 C  CG   . ASN   C 1 174 ? -45.077 -8.067  45.457  1.00 26.60 ? 153 ASN   C CG   1 
ATOM   4965 O  OD1  . ASN   C 1 174 ? -44.978 -8.336  44.256  1.00 24.62 ? 153 ASN   C OD1  1 
ATOM   4966 N  ND2  . ASN   C 1 174 ? -45.640 -6.952  45.904  1.00 27.52 ? 153 ASN   C ND2  1 
ATOM   4967 N  N    . LEU   C 1 175 ? -41.528 -9.934  44.585  1.00 17.19 ? 154 LEU   C N    1 
ATOM   4968 C  CA   . LEU   C 1 175 ? -40.270 -9.382  44.094  1.00 16.56 ? 154 LEU   C CA   1 
ATOM   4969 C  C    . LEU   C 1 175 ? -40.510 -8.670  42.773  1.00 15.55 ? 154 LEU   C C    1 
ATOM   4970 O  O    . LEU   C 1 175 ? -41.208 -9.182  41.909  1.00 16.12 ? 154 LEU   C O    1 
ATOM   4971 C  CB   . LEU   C 1 175 ? -39.304 -10.540 43.861  1.00 17.84 ? 154 LEU   C CB   1 
ATOM   4972 C  CG   . LEU   C 1 175 ? -39.062 -11.473 45.053  1.00 21.62 ? 154 LEU   C CG   1 
ATOM   4973 C  CD1  . LEU   C 1 175 ? -38.238 -12.665 44.597  1.00 21.13 ? 154 LEU   C CD1  1 
ATOM   4974 C  CD2  . LEU   C 1 175 ? -38.359 -10.682 46.143  1.00 22.15 ? 154 LEU   C CD2  1 
ATOM   4975 N  N    . SER   C 1 176 ? -39.962 -7.461  42.627  1.00 14.47 ? 155 SER   C N    1 
ATOM   4976 C  CA   . SER   C 1 176 ? -40.088 -6.851  41.308  1.00 15.66 ? 155 SER   C CA   1 
ATOM   4977 C  C    . SER   C 1 176 ? -39.029 -5.783  41.082  1.00 15.44 ? 155 SER   C C    1 
ATOM   4978 O  O    . SER   C 1 176 ? -38.355 -5.336  42.009  1.00 15.24 ? 155 SER   C O    1 
ATOM   4979 C  CB   . SER   C 1 176 ? -41.474 -6.318  41.034  1.00 19.62 ? 155 SER   C CB   1 
ATOM   4980 O  OG   . SER   C 1 176 ? -41.655 -5.058  41.659  1.00 20.31 ? 155 SER   C OG   1 
ATOM   4981 N  N    . ILE   C 1 177 ? -38.849 -5.460  39.788  1.00 13.93 ? 156 ILE   C N    1 
ATOM   4982 C  CA   . ILE   C 1 177 ? -37.951 -4.424  39.323  1.00 13.82 ? 156 ILE   C CA   1 
ATOM   4983 C  C    . ILE   C 1 177 ? -38.801 -3.421  38.554  1.00 12.78 ? 156 ILE   C C    1 
ATOM   4984 O  O    . ILE   C 1 177 ? -39.692 -3.826  37.797  1.00 13.52 ? 156 ILE   C O    1 
ATOM   4985 C  CB   . ILE   C 1 177 ? -36.844 -5.014  38.433  1.00 13.82 ? 156 ILE   C CB   1 
ATOM   4986 C  CG1  . ILE   C 1 177 ? -36.066 -6.100  39.202  1.00 15.38 ? 156 ILE   C CG1  1 
ATOM   4987 C  CG2  . ILE   C 1 177 ? -35.924 -3.906  37.925  1.00 15.02 ? 156 ILE   C CG2  1 
ATOM   4988 C  CD1  . ILE   C 1 177 ? -35.045 -6.841  38.358  1.00 16.27 ? 156 ILE   C CD1  1 
ATOM   4989 N  N    . VAL   C 1 178 ? -38.539 -2.131  38.807  1.00 13.06 ? 157 VAL   C N    1 
ATOM   4990 C  CA   . VAL   C 1 178 ? -39.167 -1.063  38.043  1.00 13.08 ? 157 VAL   C CA   1 
ATOM   4991 C  C    . VAL   C 1 178 ? -38.084 -0.196  37.423  1.00 13.14 ? 157 VAL   C C    1 
ATOM   4992 O  O    . VAL   C 1 178 ? -37.220 0.333   38.117  1.00 13.96 ? 157 VAL   C O    1 
ATOM   4993 C  CB   . VAL   C 1 178 ? -40.114 -0.204  38.883  1.00 14.79 ? 157 VAL   C CB   1 
ATOM   4994 C  CG1  . VAL   C 1 178 ? -40.762 0.855   37.990  1.00 15.11 ? 157 VAL   C CG1  1 
ATOM   4995 C  CG2  . VAL   C 1 178 ? -41.190 -1.089  39.507  1.00 15.47 ? 157 VAL   C CG2  1 
ATOM   4996 N  N    . ASN   C 1 179 ? -38.164 -0.060  36.093  1.00 12.33 ? 158 ASN   C N    1 
ATOM   4997 C  CA   . ASN   C 1 179 ? -37.184 0.718   35.332  1.00 12.84 ? 158 ASN   C CA   1 
ATOM   4998 C  C    . ASN   C 1 179 ? -37.830 2.042   34.936  1.00 14.37 ? 158 ASN   C C    1 
ATOM   4999 O  O    . ASN   C 1 179 ? -38.950 2.040   34.405  1.00 14.09 ? 158 ASN   C O    1 
ATOM   5000 C  CB   . ASN   C 1 179 ? -36.786 -0.079  34.087  1.00 13.43 ? 158 ASN   C CB   1 
ATOM   5001 C  CG   . ASN   C 1 179 ? -35.947 -1.264  34.482  1.00 14.15 ? 158 ASN   C CG   1 
ATOM   5002 O  OD1  . ASN   C 1 179 ? -35.272 -1.212  35.515  1.00 13.95 ? 158 ASN   C OD1  1 
ATOM   5003 N  ND2  . ASN   C 1 179 ? -35.972 -2.326  33.703  1.00 14.07 ? 158 ASN   C ND2  1 
ATOM   5004 N  N    . LEU   C 1 180 ? -37.109 3.152   35.174  1.00 13.35 ? 159 LEU   C N    1 
ATOM   5005 C  CA   . LEU   C 1 180 ? -37.572 4.472   34.763  1.00 13.46 ? 159 LEU   C CA   1 
ATOM   5006 C  C    . LEU   C 1 180 ? -37.165 4.709   33.317  1.00 13.66 ? 159 LEU   C C    1 
ATOM   5007 O  O    . LEU   C 1 180 ? -35.982 4.850   33.011  1.00 14.34 ? 159 LEU   C O    1 
ATOM   5008 C  CB   . LEU   C 1 180 ? -37.040 5.569   35.687  1.00 13.87 ? 159 LEU   C CB   1 
ATOM   5009 C  CG   . LEU   C 1 180 ? -37.881 5.820   36.945  1.00 14.91 ? 159 LEU   C CG   1 
ATOM   5010 C  CD1  . LEU   C 1 180 ? -39.148 6.601   36.612  1.00 15.79 ? 159 LEU   C CD1  1 
ATOM   5011 C  CD2  . LEU   C 1 180 ? -38.253 4.546   37.694  1.00 16.26 ? 159 LEU   C CD2  1 
ATOM   5012 N  N    . CYS   C 1 181 ? -38.185 4.720   32.463  1.00 13.86 ? 160 CYS   C N    1 
ATOM   5013 C  CA   . CYS   C 1 181 ? -38.053 4.777   31.021  1.00 15.17 ? 160 CYS   C CA   1 
ATOM   5014 C  C    . CYS   C 1 181 ? -38.371 6.213   30.619  1.00 15.01 ? 160 CYS   C C    1 
ATOM   5015 O  O    . CYS   C 1 181 ? -38.121 7.141   31.390  1.00 17.66 ? 160 CYS   C O    1 
ATOM   5016 C  CB   . CYS   C 1 181 ? -38.964 3.730   30.392  1.00 15.24 ? 160 CYS   C CB   1 
ATOM   5017 S  SG   . CYS   C 1 181 ? -38.455 2.018   30.769  1.00 18.51 ? 160 CYS   C SG   1 
ATOM   5018 N  N    . ASP   C 1 182 ? -38.823 6.406   29.372  1.00 15.63 ? 161 ASP   C N    1 
ATOM   5019 C  CA   . ASP   C 1 182 ? -39.056 7.758   28.881  1.00 14.56 ? 161 ASP   C CA   1 
ATOM   5020 C  C    . ASP   C 1 182 ? -40.133 7.670   27.805  1.00 14.69 ? 161 ASP   C C    1 
ATOM   5021 O  O    . ASP   C 1 182 ? -39.967 6.958   26.823  1.00 15.14 ? 161 ASP   C O    1 
ATOM   5022 C  CB   . ASP   C 1 182 ? -37.745 8.348   28.363  1.00 16.94 ? 161 ASP   C CB   1 
ATOM   5023 C  CG   . ASP   C 1 182 ? -37.825 9.782   27.869  1.00 19.15 ? 161 ASP   C CG   1 
ATOM   5024 O  OD1  . ASP   C 1 182 ? -38.885 10.142  27.328  1.00 18.72 ? 161 ASP   C OD1  1 
ATOM   5025 O  OD2  . ASP   C 1 182 ? -36.804 10.500  27.959  1.00 19.83 ? 161 ASP   C OD2  1 
ATOM   5026 N  N    . ALA   C 1 183 ? -41.276 8.326   28.027  1.00 13.40 ? 162 ALA   C N    1 
ATOM   5027 C  CA   . ALA   C 1 183 ? -42.401 8.229   27.104  1.00 14.05 ? 162 ALA   C CA   1 
ATOM   5028 C  C    . ALA   C 1 183 ? -42.112 8.855   25.739  1.00 13.84 ? 162 ALA   C C    1 
ATOM   5029 O  O    . ALA   C 1 183 ? -42.880 8.595   24.810  1.00 15.46 ? 162 ALA   C O    1 
ATOM   5030 C  CB   . ALA   C 1 183 ? -43.614 8.891   27.727  1.00 14.78 ? 162 ALA   C CB   1 
ATOM   5031 N  N    . MET   C 1 184 ? -41.041 9.655   25.614  1.00 14.42 ? 163 MET   C N    1 
ATOM   5032 C  CA   . MET   C 1 184 ? -40.808 10.441  24.408  1.00 15.22 ? 163 MET   C CA   1 
ATOM   5033 C  C    . MET   C 1 184 ? -39.686 9.863   23.539  1.00 16.91 ? 163 MET   C C    1 
ATOM   5034 O  O    . MET   C 1 184 ? -39.237 10.515  22.597  1.00 18.48 ? 163 MET   C O    1 
ATOM   5035 C  CB   . MET   C 1 184 ? -40.529 11.903  24.786  1.00 16.99 ? 163 MET   C CB   1 
ATOM   5036 C  CG   . MET   C 1 184 ? -41.685 12.613  25.490  1.00 18.40 ? 163 MET   C CG   1 
ATOM   5037 S  SD   . MET   C 1 184 ? -43.061 12.791  24.341  1.00 21.66 ? 163 MET   C SD   1 
ATOM   5038 C  CE   . MET   C 1 184 ? -42.373 14.097  23.318  1.00 23.33 ? 163 MET   C CE   1 
ATOM   5039 N  N    . VAL   C 1 185 ? -39.307 8.604   23.764  1.00 17.92 ? 164 VAL   C N    1 
ATOM   5040 C  CA   . VAL   C 1 185 ? -38.120 8.101   23.079  1.00 19.98 ? 164 VAL   C CA   1 
ATOM   5041 C  C    . VAL   C 1 185 ? -38.354 7.806   21.598  1.00 18.50 ? 164 VAL   C C    1 
ATOM   5042 O  O    . VAL   C 1 185 ? -37.379 7.584   20.871  1.00 19.07 ? 164 VAL   C O    1 
ATOM   5043 C  CB   . VAL   C 1 185 ? -37.498 6.860   23.745  1.00 21.81 ? 164 VAL   C CB   1 
ATOM   5044 C  CG1  . VAL   C 1 185 ? -36.881 7.215   25.095  1.00 25.26 ? 164 VAL   C CG1  1 
ATOM   5045 C  CG2  . VAL   C 1 185 ? -38.491 5.709   23.838  1.00 23.84 ? 164 VAL   C CG2  1 
ATOM   5046 N  N    . ASP   C 1 186 ? -39.618 7.746   21.160  1.00 16.43 ? 165 ASP   C N    1 
ATOM   5047 C  CA   . ASP   C 1 186 ? -39.884 7.608   19.733  1.00 17.72 ? 165 ASP   C CA   1 
ATOM   5048 C  C    . ASP   C 1 186 ? -40.071 8.957   19.045  1.00 17.26 ? 165 ASP   C C    1 
ATOM   5049 O  O    . ASP   C 1 186 ? -40.295 9.004   17.826  1.00 18.75 ? 165 ASP   C O    1 
ATOM   5050 C  CB   . ASP   C 1 186 ? -41.042 6.665   19.459  1.00 17.18 ? 165 ASP   C CB   1 
ATOM   5051 C  CG   . ASP   C 1 186 ? -40.773 5.234   19.881  1.00 20.14 ? 165 ASP   C CG   1 
ATOM   5052 O  OD1  . ASP   C 1 186 ? -39.640 4.785   19.699  1.00 19.19 ? 165 ASP   C OD1  1 
ATOM   5053 O  OD2  . ASP   C 1 186 ? -41.722 4.597   20.395  1.00 23.94 ? 165 ASP   C OD2  1 
ATOM   5054 N  N    . GLN   C 1 187 ? -40.032 10.044  19.823  1.00 16.28 ? 166 GLN   C N    1 
ATOM   5055 C  CA   . GLN   C 1 187 ? -40.053 11.384  19.250  1.00 18.15 ? 166 GLN   C CA   1 
ATOM   5056 C  C    . GLN   C 1 187 ? -38.968 12.173  19.969  1.00 17.65 ? 166 GLN   C C    1 
ATOM   5057 O  O    . GLN   C 1 187 ? -39.242 13.116  20.703  1.00 19.73 ? 166 GLN   C O    1 
ATOM   5058 C  CB   . GLN   C 1 187 ? -41.413 12.063  19.426  1.00 19.78 ? 166 GLN   C CB   1 
ATOM   5059 C  CG   . GLN   C 1 187 ? -42.558 11.317  18.755  1.00 23.57 ? 166 GLN   C CG   1 
ATOM   5060 C  CD   . GLN   C 1 187 ? -43.659 10.996  19.743  1.00 28.64 ? 166 GLN   C CD   1 
ATOM   5061 O  OE1  . GLN   C 1 187 ? -43.571 10.025  20.498  1.00 25.32 ? 166 GLN   C OE1  1 
ATOM   5062 N  NE2  . GLN   C 1 187 ? -44.704 11.808  19.763  1.00 27.65 ? 166 GLN   C NE2  1 
ATOM   5063 N  N    . PRO   C 1 188 ? -37.694 11.806  19.749  1.00 18.34 ? 167 PRO   C N    1 
ATOM   5064 C  CA   . PRO   C 1 188 ? -36.616 12.272  20.629  1.00 18.57 ? 167 PRO   C CA   1 
ATOM   5065 C  C    . PRO   C 1 188 ? -36.249 13.749  20.498  1.00 17.31 ? 167 PRO   C C    1 
ATOM   5066 O  O    . PRO   C 1 188 ? -36.440 14.358  19.449  1.00 18.81 ? 167 PRO   C O    1 
ATOM   5067 C  CB   . PRO   C 1 188 ? -35.469 11.354  20.195  1.00 19.22 ? 167 PRO   C CB   1 
ATOM   5068 C  CG   . PRO   C 1 188 ? -35.739 11.078  18.744  1.00 19.28 ? 167 PRO   C CG   1 
ATOM   5069 C  CD   . PRO   C 1 188 ? -37.254 10.866  18.711  1.00 17.55 ? 167 PRO   C CD   1 
ATOM   5070 N  N    . CYS   C 1 189 ? -35.676 14.295  21.568  1.00 18.33 ? 168 CYS   C N    1 
ATOM   5071 C  CA   . CYS   C 1 189 ? -35.104 15.626  21.449  1.00 18.57 ? 168 CYS   C CA   1 
ATOM   5072 C  C    . CYS   C 1 189 ? -33.895 15.587  20.515  1.00 18.88 ? 168 CYS   C C    1 
ATOM   5073 O  O    . CYS   C 1 189 ? -33.113 14.631  20.490  1.00 17.82 ? 168 CYS   C O    1 
ATOM   5074 C  CB   . CYS   C 1 189 ? -34.709 16.162  22.812  1.00 21.62 ? 168 CYS   C CB   1 
ATOM   5075 S  SG   . CYS   C 1 189 ? -36.155 16.664  23.787  1.00 30.41 ? 168 CYS   C SG   1 
ATOM   5076 N  N    . MET   C 1 190 ? -33.775 16.662  19.731  1.00 19.16 ? 169 MET   C N    1 
ATOM   5077 C  CA   . MET   C 1 190 ? -32.657 16.836  18.820  1.00 19.41 ? 169 MET   C CA   1 
ATOM   5078 C  C    . MET   C 1 190 ? -31.339 16.703  19.591  1.00 17.81 ? 169 MET   C C    1 
ATOM   5079 O  O    . MET   C 1 190 ? -31.155 17.341  20.628  1.00 18.49 ? 169 MET   C O    1 
ATOM   5080 C  CB   . MET   C 1 190 ? -32.737 18.251  18.222  1.00 21.15 ? 169 MET   C CB   1 
ATOM   5081 C  CG   . MET   C 1 190 ? -31.586 18.598  17.310  1.00 24.97 ? 169 MET   C CG   1 
ATOM   5082 S  SD   . MET   C 1 190 ? -31.595 17.431  15.935  1.00 28.77 ? 169 MET   C SD   1 
ATOM   5083 C  CE   . MET   C 1 190 ? -33.058 17.945  15.025  1.00 30.50 ? 169 MET   C CE   1 
ATOM   5084 N  N    . ALA   C 1 191 ? -30.408 15.895  19.055  1.00 16.53 ? 170 ALA   C N    1 
ATOM   5085 C  CA   . ALA   C 1 191 ? -29.035 15.786  19.547  1.00 16.81 ? 170 ALA   C CA   1 
ATOM   5086 C  C    . ALA   C 1 191 ? -28.896 14.995  20.849  1.00 16.92 ? 170 ALA   C C    1 
ATOM   5087 O  O    . ALA   C 1 191 ? -27.849 15.045  21.500  1.00 17.43 ? 170 ALA   C O    1 
ATOM   5088 C  CB   . ALA   C 1 191 ? -28.363 17.166  19.622  1.00 20.10 ? 170 ALA   C CB   1 
ATOM   5089 N  N    . PHE   C 1 192 ? -29.897 14.155  21.168  1.00 14.91 ? 171 PHE   C N    1 
ATOM   5090 C  CA   . PHE   C 1 192 ? -29.815 13.307  22.355  1.00 14.93 ? 171 PHE   C CA   1 
ATOM   5091 C  C    . PHE   C 1 192 ? -29.702 11.838  21.960  1.00 15.09 ? 171 PHE   C C    1 
ATOM   5092 O  O    . PHE   C 1 192 ? -30.311 10.993  22.613  1.00 15.45 ? 171 PHE   C O    1 
ATOM   5093 C  CB   . PHE   C 1 192 ? -31.046 13.482  23.252  1.00 16.95 ? 171 PHE   C CB   1 
ATOM   5094 C  CG   . PHE   C 1 192 ? -30.991 14.729  24.129  1.00 17.20 ? 171 PHE   C CG   1 
ATOM   5095 C  CD1  . PHE   C 1 192 ? -31.252 15.986  23.591  1.00 18.38 ? 171 PHE   C CD1  1 
ATOM   5096 C  CD2  . PHE   C 1 192 ? -30.663 14.631  25.478  1.00 18.06 ? 171 PHE   C CD2  1 
ATOM   5097 C  CE1  . PHE   C 1 192 ? -31.189 17.117  24.394  1.00 19.43 ? 171 PHE   C CE1  1 
ATOM   5098 C  CE2  . PHE   C 1 192 ? -30.602 15.769  26.278  1.00 19.97 ? 171 PHE   C CE2  1 
ATOM   5099 C  CZ   . PHE   C 1 192 ? -30.869 17.011  25.731  1.00 19.34 ? 171 PHE   C CZ   1 
ATOM   5100 N  N    . SER   C 1 193 ? -28.845 11.512  20.990  1.00 13.91 ? 172 SER   C N    1 
ATOM   5101 C  CA   A SER   C 1 193 ? -28.753 10.141  20.475  0.70 14.66 ? 172 SER   C CA   1 
ATOM   5102 C  CA   B SER   C 1 193 ? -28.822 10.142  20.496  0.30 13.54 ? 172 SER   C CA   1 
ATOM   5103 C  C    . SER   C 1 193 ? -28.367 9.163   21.576  1.00 14.41 ? 172 SER   C C    1 
ATOM   5104 O  O    . SER   C 1 193 ? -28.971 8.098   21.716  1.00 13.66 ? 172 SER   C O    1 
ATOM   5105 C  CB   A SER   C 1 193 ? -27.756 10.012  19.337  0.70 16.39 ? 172 SER   C CB   1 
ATOM   5106 C  CB   B SER   C 1 193 ? -28.022 10.005  19.229  0.30 12.93 ? 172 SER   C CB   1 
ATOM   5107 O  OG   A SER   C 1 193 ? -28.240 10.538  18.114  0.70 18.42 ? 172 SER   C OG   1 
ATOM   5108 O  OG   B SER   C 1 193 ? -26.709 10.499  19.440  0.30 12.01 ? 172 SER   C OG   1 
ATOM   5109 N  N    . LEU   C 1 194 ? -27.303 9.471   22.327  1.00 13.45 ? 173 LEU   C N    1 
ATOM   5110 C  CA   . LEU   C 1 194 ? -26.848 8.490   23.308  1.00 14.33 ? 173 LEU   C CA   1 
ATOM   5111 C  C    . LEU   C 1 194 ? -27.872 8.248   24.415  1.00 12.66 ? 173 LEU   C C    1 
ATOM   5112 O  O    . LEU   C 1 194 ? -28.083 7.103   24.824  1.00 13.63 ? 173 LEU   C O    1 
ATOM   5113 C  CB   . LEU   C 1 194 ? -25.470 8.828   23.876  1.00 14.50 ? 173 LEU   C CB   1 
ATOM   5114 C  CG   . LEU   C 1 194 ? -24.327 8.519   22.913  1.00 14.42 ? 173 LEU   C CG   1 
ATOM   5115 C  CD1  . LEU   C 1 194 ? -23.061 9.179   23.449  1.00 16.33 ? 173 LEU   C CD1  1 
ATOM   5116 C  CD2  . LEU   C 1 194 ? -24.098 7.012   22.761  1.00 15.29 ? 173 LEU   C CD2  1 
ATOM   5117 N  N    . TYR   C 1 195 ? -28.487 9.321   24.923  1.00 12.96 ? 174 TYR   C N    1 
ATOM   5118 C  CA   . TYR   C 1 195 ? -29.535 9.196   25.917  1.00 12.63 ? 174 TYR   C CA   1 
ATOM   5119 C  C    . TYR   C 1 195 ? -30.653 8.307   25.365  1.00 12.85 ? 174 TYR   C C    1 
ATOM   5120 O  O    . TYR   C 1 195 ? -31.112 7.378   26.029  1.00 13.55 ? 174 TYR   C O    1 
ATOM   5121 C  CB   . TYR   C 1 195 ? -30.007 10.613  26.287  1.00 13.61 ? 174 TYR   C CB   1 
ATOM   5122 C  CG   . TYR   C 1 195 ? -31.246 10.507  27.164  1.00 14.01 ? 174 TYR   C CG   1 
ATOM   5123 C  CD1  . TYR   C 1 195 ? -31.177 10.246  28.541  1.00 14.04 ? 174 TYR   C CD1  1 
ATOM   5124 C  CD2  . TYR   C 1 195 ? -32.498 10.572  26.565  1.00 13.94 ? 174 TYR   C CD2  1 
ATOM   5125 C  CE1  . TYR   C 1 195 ? -32.339 10.128  29.305  1.00 14.66 ? 174 TYR   C CE1  1 
ATOM   5126 C  CE2  . TYR   C 1 195 ? -33.656 10.465  27.318  1.00 14.80 ? 174 TYR   C CE2  1 
ATOM   5127 C  CZ   . TYR   C 1 195 ? -33.575 10.228  28.682  1.00 15.17 ? 174 TYR   C CZ   1 
ATOM   5128 O  OH   . TYR   C 1 195 ? -34.739 10.090  29.388  1.00 17.37 ? 174 TYR   C OH   1 
ATOM   5129 N  N    . ASN   C 1 196 ? -31.057 8.557   24.119  1.00 13.41 ? 175 ASN   C N    1 
ATOM   5130 C  CA   A ASN   C 1 196 ? -32.182 7.822   23.564  0.70 13.78 ? 175 ASN   C CA   1 
ATOM   5131 C  CA   B ASN   C 1 196 ? -32.160 7.847   23.489  0.30 13.25 ? 175 ASN   C CA   1 
ATOM   5132 C  C    . ASN   C 1 196 ? -31.806 6.368   23.350  1.00 13.06 ? 175 ASN   C C    1 
ATOM   5133 O  O    . ASN   C 1 196 ? -32.642 5.489   23.565  1.00 14.10 ? 175 ASN   C O    1 
ATOM   5134 C  CB   A ASN   C 1 196 ? -32.701 8.453   22.284  0.70 16.16 ? 175 ASN   C CB   1 
ATOM   5135 C  CB   B ASN   C 1 196 ? -32.474 8.479   22.138  0.30 13.69 ? 175 ASN   C CB   1 
ATOM   5136 C  CG   A ASN   C 1 196 ? -33.680 9.548   22.614  0.70 20.22 ? 175 ASN   C CG   1 
ATOM   5137 C  CG   B ASN   C 1 196 ? -33.802 8.026   21.583  0.30 14.43 ? 175 ASN   C CG   1 
ATOM   5138 O  OD1  A ASN   C 1 196 ? -34.854 9.275   22.895  0.70 24.72 ? 175 ASN   C OD1  1 
ATOM   5139 O  OD1  B ASN   C 1 196 ? -33.860 7.428   20.503  0.30 15.40 ? 175 ASN   C OD1  1 
ATOM   5140 N  ND2  A ASN   C 1 196 ? -33.221 10.786  22.585  0.70 17.95 ? 175 ASN   C ND2  1 
ATOM   5141 N  ND2  B ASN   C 1 196 ? -34.878 8.310   22.293  0.30 14.02 ? 175 ASN   C ND2  1 
ATOM   5142 N  N    . MET   C 1 197 ? -30.554 6.118   22.946  1.00 12.49 ? 176 MET   C N    1 
ATOM   5143 C  CA   . MET   C 1 197 ? -30.092 4.740   22.826  1.00 12.82 ? 176 MET   C CA   1 
ATOM   5144 C  C    . MET   C 1 197 ? -30.185 4.034   24.177  1.00 13.06 ? 176 MET   C C    1 
ATOM   5145 O  O    . MET   C 1 197 ? -30.585 2.858   24.233  1.00 12.62 ? 176 MET   C O    1 
ATOM   5146 C  CB   . MET   C 1 197 ? -28.643 4.693   22.338  1.00 13.10 ? 176 MET   C CB   1 
ATOM   5147 C  CG   . MET   C 1 197 ? -28.523 5.132   20.895  1.00 14.29 ? 176 MET   C CG   1 
ATOM   5148 S  SD   . MET   C 1 197 ? -26.838 5.439   20.339  1.00 14.83 ? 176 MET   C SD   1 
ATOM   5149 C  CE   . MET   C 1 197 ? -26.339 3.714   20.303  1.00 17.42 ? 176 MET   C CE   1 
ATOM   5150 N  N    . GLY   C 1 198 ? -29.767 4.721   25.251  1.00 13.40 ? 177 GLY   C N    1 
ATOM   5151 C  CA   . GLY   C 1 198 ? -29.756 4.123   26.577  1.00 13.15 ? 177 GLY   C CA   1 
ATOM   5152 C  C    . GLY   C 1 198 ? -31.180 3.771   27.015  1.00 13.03 ? 177 GLY   C C    1 
ATOM   5153 O  O    . GLY   C 1 198 ? -31.438 2.676   27.517  1.00 12.65 ? 177 GLY   C O    1 
ATOM   5154 N  N    . LYS   C 1 199 ? -32.123 4.685   26.767  1.00 12.73 ? 178 LYS   C N    1 
ATOM   5155 C  CA   . LYS   C 1 199 ? -33.497 4.455   27.189  1.00 12.92 ? 178 LYS   C CA   1 
ATOM   5156 C  C    . LYS   C 1 199 ? -34.157 3.364   26.340  1.00 12.92 ? 178 LYS   C C    1 
ATOM   5157 O  O    . LYS   C 1 199 ? -34.962 2.610   26.876  1.00 12.72 ? 178 LYS   C O    1 
ATOM   5158 C  CB   . LYS   C 1 199 ? -34.320 5.746   27.273  1.00 13.22 ? 178 LYS   C CB   1 
ATOM   5159 C  CG   . LYS   C 1 199 ? -33.893 6.699   28.380  1.00 13.86 ? 178 LYS   C CG   1 
ATOM   5160 C  CD   . LYS   C 1 199 ? -33.997 6.100   29.775  1.00 14.58 ? 178 LYS   C CD   1 
ATOM   5161 C  CE   . LYS   C 1 199 ? -34.033 7.176   30.824  1.00 16.21 ? 178 LYS   C CE   1 
ATOM   5162 N  NZ   . LYS   C 1 199 ? -33.964 6.595   32.165  1.00 16.43 ? 178 LYS   C NZ   1 
ATOM   5163 N  N    . HIS   C 1 200 ? -33.845 3.297   25.038  1.00 12.33 ? 179 HIS   C N    1 
ATOM   5164 C  CA   . HIS   C 1 200 ? -34.378 2.194   24.248  1.00 11.85 ? 179 HIS   C CA   1 
ATOM   5165 C  C    . HIS   C 1 200 ? -33.791 0.889   24.759  1.00 12.30 ? 179 HIS   C C    1 
ATOM   5166 O  O    . HIS   C 1 200 ? -34.513 -0.113  24.810  1.00 11.84 ? 179 HIS   C O    1 
ATOM   5167 C  CB   . HIS   C 1 200 ? -34.022 2.366   22.768  1.00 12.39 ? 179 HIS   C CB   1 
ATOM   5168 C  CG   . HIS   C 1 200 ? -35.004 3.207   22.052  1.00 14.58 ? 179 HIS   C CG   1 
ATOM   5169 N  ND1  . HIS   C 1 200 ? -36.080 2.634   21.406  1.00 17.37 ? 179 HIS   C ND1  1 
ATOM   5170 C  CD2  . HIS   C 1 200 ? -35.132 4.560   21.900  1.00 15.98 ? 179 HIS   C CD2  1 
ATOM   5171 C  CE1  . HIS   C 1 200 ? -36.809 3.592   20.839  1.00 16.61 ? 179 HIS   C CE1  1 
ATOM   5172 N  NE2  . HIS   C 1 200 ? -36.243 4.762   21.103  1.00 18.14 ? 179 HIS   C NE2  1 
ATOM   5173 N  N    . ALA   C 1 201 ? -32.487 0.892   25.097  1.00 12.18 ? 180 ALA   C N    1 
ATOM   5174 C  CA   . ALA   C 1 201 ? -31.889 -0.329  25.635  1.00 11.67 ? 180 ALA   C CA   1 
ATOM   5175 C  C    . ALA   C 1 201 ? -32.607 -0.758  26.916  1.00 11.80 ? 180 ALA   C C    1 
ATOM   5176 O  O    . ALA   C 1 201 ? -32.801 -1.956  27.142  1.00 13.30 ? 180 ALA   C O    1 
ATOM   5177 C  CB   . ALA   C 1 201 ? -30.395 -0.194  25.842  1.00 11.69 ? 180 ALA   C CB   1 
ATOM   5178 N  N    . LEU   C 1 202 ? -33.005 0.223   27.740  1.00 11.97 ? 181 LEU   C N    1 
ATOM   5179 C  CA   . LEU   C 1 202 ? -33.711 -0.056  28.982  1.00 12.83 ? 181 LEU   C CA   1 
ATOM   5180 C  C    . LEU   C 1 202 ? -35.080 -0.702  28.730  1.00 13.10 ? 181 LEU   C C    1 
ATOM   5181 O  O    . LEU   C 1 202 ? -35.488 -1.598  29.478  1.00 13.43 ? 181 LEU   C O    1 
ATOM   5182 C  CB   . LEU   C 1 202 ? -33.774 1.241   29.802  1.00 12.55 ? 181 LEU   C CB   1 
ATOM   5183 C  CG   . LEU   C 1 202 ? -34.339 1.041   31.211  1.00 14.54 ? 181 LEU   C CG   1 
ATOM   5184 C  CD1  . LEU   C 1 202 ? -33.479 0.113   32.043  1.00 13.95 ? 181 LEU   C CD1  1 
ATOM   5185 C  CD2  . LEU   C 1 202 ? -34.374 2.432   31.808  1.00 15.16 ? 181 LEU   C CD2  1 
ATOM   5186 N  N    . VAL   C 1 203 ? -35.767 -0.353  27.629  1.00 13.73 ? 182 VAL   C N    1 
ATOM   5187 C  CA   . VAL   C 1 203 ? -37.007 -1.031  27.247  1.00 13.44 ? 182 VAL   C CA   1 
ATOM   5188 C  C    . VAL   C 1 203 ? -36.683 -2.486  26.923  1.00 13.04 ? 182 VAL   C C    1 
ATOM   5189 O  O    . VAL   C 1 203 ? -37.385 -3.407  27.352  1.00 14.03 ? 182 VAL   C O    1 
ATOM   5190 C  CB   . VAL   C 1 203 ? -37.700 -0.345  26.053  1.00 14.60 ? 182 VAL   C CB   1 
ATOM   5191 C  CG1  . VAL   C 1 203 ? -38.896 -1.173  25.564  1.00 15.74 ? 182 VAL   C CG1  1 
ATOM   5192 C  CG2  . VAL   C 1 203 ? -38.114 1.085   26.410  1.00 17.90 ? 182 VAL   C CG2  1 
ATOM   5193 N  N    . GLY   C 1 204 ? -35.601 -2.685  26.164  1.00 12.85 ? 183 GLY   C N    1 
ATOM   5194 C  CA   . GLY   C 1 204 ? -35.214 -4.042  25.816  1.00 12.52 ? 183 GLY   C CA   1 
ATOM   5195 C  C    . GLY   C 1 204 ? -34.904 -4.856  27.070  1.00 13.16 ? 183 GLY   C C    1 
ATOM   5196 O  O    . GLY   C 1 204 ? -35.270 -6.040  27.156  1.00 13.61 ? 183 GLY   C O    1 
ATOM   5197 N  N    . LEU   C 1 205 ? -34.213 -4.248  28.033  1.00 13.33 ? 184 LEU   C N    1 
ATOM   5198 C  CA   . LEU   C 1 205 ? -33.904 -4.958  29.262  1.00 13.15 ? 184 LEU   C CA   1 
ATOM   5199 C  C    . LEU   C 1 205 ? -35.195 -5.310  29.995  1.00 12.97 ? 184 LEU   C C    1 
ATOM   5200 O  O    . LEU   C 1 205 ? -35.315 -6.403  30.550  1.00 14.29 ? 184 LEU   C O    1 
ATOM   5201 C  CB   . LEU   C 1 205 ? -32.997 -4.115  30.153  1.00 13.90 ? 184 LEU   C CB   1 
ATOM   5202 C  CG   . LEU   C 1 205 ? -32.737 -4.698  31.546  1.00 14.27 ? 184 LEU   C CG   1 
ATOM   5203 C  CD1  . LEU   C 1 205 ? -32.001 -6.044  31.506  1.00 15.32 ? 184 LEU   C CD1  1 
ATOM   5204 C  CD2  . LEU   C 1 205 ? -31.978 -3.644  32.393  1.00 14.94 ? 184 LEU   C CD2  1 
ATOM   5205 N  N    . THR   C 1 206 ? -36.139 -4.365  30.049  1.00 12.66 ? 185 THR   C N    1 
ATOM   5206 C  CA   . THR   C 1 206 ? -37.387 -4.581  30.766  1.00 12.51 ? 185 THR   C CA   1 
ATOM   5207 C  C    . THR   C 1 206 ? -38.077 -5.828  30.205  1.00 13.04 ? 185 THR   C C    1 
ATOM   5208 O  O    . THR   C 1 206 ? -38.541 -6.682  30.955  1.00 14.88 ? 185 THR   C O    1 
ATOM   5209 C  CB   . THR   C 1 206 ? -38.283 -3.348  30.679  1.00 12.48 ? 185 THR   C CB   1 
ATOM   5210 O  OG1  . THR   C 1 206 ? -37.609 -2.224  31.242  1.00 13.50 ? 185 THR   C OG1  1 
ATOM   5211 C  CG2  . THR   C 1 206 ? -39.560 -3.534  31.475  1.00 13.62 ? 185 THR   C CG2  1 
ATOM   5212 N  N    . GLN   C 1 207 ? -38.130 -5.929  28.870  1.00 12.23 ? 186 GLN   C N    1 
ATOM   5213 C  CA   . GLN   C 1 207 ? -38.795 -7.041  28.204  1.00 12.88 ? 186 GLN   C CA   1 
ATOM   5214 C  C    . GLN   C 1 207 ? -38.037 -8.352  28.403  1.00 12.36 ? 186 GLN   C C    1 
ATOM   5215 O  O    . GLN   C 1 207 ? -38.650 -9.363  28.754  1.00 14.07 ? 186 GLN   C O    1 
ATOM   5216 C  CB   . GLN   C 1 207 ? -38.964 -6.709  26.720  1.00 13.87 ? 186 GLN   C CB   1 
ATOM   5217 C  CG   . GLN   C 1 207 ? -39.916 -5.528  26.540  1.00 16.56 ? 186 GLN   C CG   1 
ATOM   5218 C  CD   . GLN   C 1 207 ? -40.144 -5.132  25.097  1.00 22.56 ? 186 GLN   C CD   1 
ATOM   5219 O  OE1  . GLN   C 1 207 ? -41.184 -4.550  24.760  1.00 28.59 ? 186 GLN   C OE1  1 
ATOM   5220 N  NE2  . GLN   C 1 207 ? -39.192 -5.447  24.243  1.00 21.21 ? 186 GLN   C NE2  1 
ATOM   5221 N  N    . SER   C 1 208 ? -36.726 -8.340  28.114  1.00 13.26 ? 187 SER   C N    1 
ATOM   5222 C  CA   . SER   C 1 208 ? -35.906 -9.546  28.205  1.00 12.29 ? 187 SER   C CA   1 
ATOM   5223 C  C    . SER   C 1 208 ? -35.866 -10.059 29.641  1.00 13.09 ? 187 SER   C C    1 
ATOM   5224 O  O    . SER   C 1 208 ? -35.948 -11.279 29.856  1.00 13.61 ? 187 SER   C O    1 
ATOM   5225 C  CB   . SER   C 1 208 ? -34.488 -9.267  27.731  1.00 13.82 ? 187 SER   C CB   1 
ATOM   5226 O  OG   . SER   C 1 208 ? -34.461 -9.202  26.316  1.00 16.11 ? 187 SER   C OG   1 
ATOM   5227 N  N    . ALA   C 1 209 ? -35.709 -9.162  30.622  1.00 13.17 ? 188 ALA   C N    1 
ATOM   5228 C  CA   . ALA   C 1 209 ? -35.653 -9.587  32.022  1.00 12.34 ? 188 ALA   C CA   1 
ATOM   5229 C  C    . ALA   C 1 209 ? -37.024 -10.074 32.514  1.00 13.40 ? 188 ALA   C C    1 
ATOM   5230 O  O    . ALA   C 1 209 ? -37.105 -11.002 33.330  1.00 14.53 ? 188 ALA   C O    1 
ATOM   5231 C  CB   . ALA   C 1 209 ? -35.096 -8.466  32.897  1.00 14.08 ? 188 ALA   C CB   1 
ATOM   5232 N  N    . ALA   C 1 210 ? -38.107 -9.439  32.058  1.00 13.52 ? 189 ALA   C N    1 
ATOM   5233 C  CA   . ALA   C 1 210 ? -39.442 -9.903  32.425  1.00 13.56 ? 189 ALA   C CA   1 
ATOM   5234 C  C    . ALA   C 1 210 ? -39.584 -11.363 32.000  1.00 14.93 ? 189 ALA   C C    1 
ATOM   5235 O  O    . ALA   C 1 210 ? -40.028 -12.215 32.774  1.00 15.43 ? 189 ALA   C O    1 
ATOM   5236 C  CB   . ALA   C 1 210 ? -40.498 -9.023  31.794  1.00 13.96 ? 189 ALA   C CB   1 
ATOM   5237 N  N    . LEU   C 1 211 ? -39.199 -11.649 30.760  1.00 15.19 ? 190 LEU   C N    1 
ATOM   5238 C  CA   . LEU   C 1 211 ? -39.327 -13.012 30.262  1.00 15.76 ? 190 LEU   C CA   1 
ATOM   5239 C  C    . LEU   C 1 211 ? -38.496 -14.002 31.076  1.00 16.95 ? 190 LEU   C C    1 
ATOM   5240 O  O    . LEU   C 1 211 ? -38.972 -15.089 31.452  1.00 18.47 ? 190 LEU   C O    1 
ATOM   5241 C  CB   . LEU   C 1 211 ? -38.889 -12.993 28.798  1.00 17.61 ? 190 LEU   C CB   1 
ATOM   5242 C  CG   . LEU   C 1 211 ? -38.964 -14.336 28.074  1.00 20.04 ? 190 LEU   C CG   1 
ATOM   5243 C  CD1  . LEU   C 1 211 ? -40.416 -14.719 27.857  1.00 19.07 ? 190 LEU   C CD1  1 
ATOM   5244 C  CD2  . LEU   C 1 211 ? -38.243 -14.201 26.743  1.00 21.26 ? 190 LEU   C CD2  1 
ATOM   5245 N  N    . GLU   C 1 212 ? -37.234 -13.635 31.321  1.00 16.18 ? 191 GLU   C N    1 
ATOM   5246 C  CA   . GLU   C 1 212 ? -36.259 -14.553 31.887  1.00 16.56 ? 191 GLU   C CA   1 
ATOM   5247 C  C    . GLU   C 1 212 ? -36.456 -14.723 33.389  1.00 16.61 ? 191 GLU   C C    1 
ATOM   5248 O  O    . GLU   C 1 212 ? -36.143 -15.793 33.915  1.00 19.10 ? 191 GLU   C O    1 
ATOM   5249 C  CB   . GLU   C 1 212 ? -34.863 -14.045 31.531  1.00 17.01 ? 191 GLU   C CB   1 
ATOM   5250 C  CG   . GLU   C 1 212 ? -33.735 -14.914 32.080  1.00 19.46 ? 191 GLU   C CG   1 
ATOM   5251 C  CD   . GLU   C 1 212 ? -32.390 -14.485 31.534  1.00 22.89 ? 191 GLU   C CD   1 
ATOM   5252 O  OE1  . GLU   C 1 212 ? -31.379 -15.092 31.929  1.00 22.92 ? 191 GLU   C OE1  1 
ATOM   5253 O  OE2  . GLU   C 1 212 ? -32.361 -13.563 30.679  1.00 23.56 ? 191 GLU   C OE2  1 
ATOM   5254 N  N    . LEU   C 1 213 ? -36.988 -13.706 34.077  1.00 15.55 ? 192 LEU   C N    1 
ATOM   5255 C  CA   . LEU   C 1 213 ? -37.111 -13.799 35.528  1.00 14.77 ? 192 LEU   C CA   1 
ATOM   5256 C  C    . LEU   C 1 213 ? -38.512 -14.220 35.972  1.00 16.22 ? 192 LEU   C C    1 
ATOM   5257 O  O    . LEU   C 1 213 ? -38.720 -14.474 37.162  1.00 16.50 ? 192 LEU   C O    1 
ATOM   5258 C  CB   . LEU   C 1 213 ? -36.682 -12.477 36.148  1.00 14.43 ? 192 LEU   C CB   1 
ATOM   5259 C  CG   . LEU   C 1 213 ? -35.237 -12.084 35.838  1.00 14.17 ? 192 LEU   C CG   1 
ATOM   5260 C  CD1  . LEU   C 1 213 ? -34.943 -10.744 36.501  1.00 15.23 ? 192 LEU   C CD1  1 
ATOM   5261 C  CD2  . LEU   C 1 213 ? -34.202 -13.152 36.228  1.00 15.26 ? 192 LEU   C CD2  1 
ATOM   5262 N  N    . ALA   C 1 214 ? -39.442 -14.332 35.021  1.00 16.70 ? 193 ALA   C N    1 
ATOM   5263 C  CA   . ALA   C 1 214 ? -40.802 -14.773 35.326  1.00 16.50 ? 193 ALA   C CA   1 
ATOM   5264 C  C    . ALA   C 1 214 ? -40.802 -16.105 36.074  1.00 19.55 ? 193 ALA   C C    1 
ATOM   5265 O  O    . ALA   C 1 214 ? -41.569 -16.247 37.035  1.00 19.02 ? 193 ALA   C O    1 
ATOM   5266 C  CB   . ALA   C 1 214 ? -41.660 -14.789 34.082  1.00 19.27 ? 193 ALA   C CB   1 
ATOM   5267 N  N    . PRO   C 1 215 ? -39.959 -17.105 35.721  1.00 22.01 ? 194 PRO   C N    1 
ATOM   5268 C  CA   . PRO   C 1 215 ? -39.986 -18.386 36.431  1.00 24.06 ? 194 PRO   C CA   1 
ATOM   5269 C  C    . PRO   C 1 215 ? -39.656 -18.269 37.920  1.00 26.22 ? 194 PRO   C C    1 
ATOM   5270 O  O    . PRO   C 1 215 ? -40.040 -19.140 38.699  1.00 26.87 ? 194 PRO   C O    1 
ATOM   5271 C  CB   . PRO   C 1 215 ? -38.958 -19.251 35.674  1.00 26.01 ? 194 PRO   C CB   1 
ATOM   5272 C  CG   . PRO   C 1 215 ? -38.796 -18.581 34.326  1.00 26.12 ? 194 PRO   C CG   1 
ATOM   5273 C  CD   . PRO   C 1 215 ? -38.967 -17.102 34.627  1.00 23.76 ? 194 PRO   C CD   1 
ATOM   5274 N  N    . TYR   C 1 216 ? -38.958 -17.187 38.315  1.00 24.88 ? 195 TYR   C N    1 
ATOM   5275 C  CA   . TYR   C 1 216 ? -38.558 -16.963 39.697  1.00 24.49 ? 195 TYR   C CA   1 
ATOM   5276 C  C    . TYR   C 1 216 ? -39.560 -16.067 40.419  1.00 24.21 ? 195 TYR   C C    1 
ATOM   5277 O  O    . TYR   C 1 216 ? -39.346 -15.719 41.582  1.00 25.46 ? 195 TYR   C O    1 
ATOM   5278 C  CB   . TYR   C 1 216 ? -37.212 -16.237 39.781  1.00 26.72 ? 195 TYR   C CB   1 
ATOM   5279 C  CG   . TYR   C 1 216 ? -36.103 -17.006 39.090  1.00 30.63 ? 195 TYR   C CG   1 
ATOM   5280 C  CD1  . TYR   C 1 216 ? -35.461 -18.060 39.735  1.00 33.05 ? 195 TYR   C CD1  1 
ATOM   5281 C  CD2  . TYR   C 1 216 ? -35.724 -16.704 37.788  1.00 31.39 ? 195 TYR   C CD2  1 
ATOM   5282 C  CE1  . TYR   C 1 216 ? -34.456 -18.772 39.103  1.00 35.63 ? 195 TYR   C CE1  1 
ATOM   5283 C  CE2  . TYR   C 1 216 ? -34.723 -17.412 37.147  1.00 32.78 ? 195 TYR   C CE2  1 
ATOM   5284 C  CZ   . TYR   C 1 216 ? -34.082 -18.442 37.812  1.00 36.26 ? 195 TYR   C CZ   1 
ATOM   5285 O  OH   . TYR   C 1 216 ? -33.090 -19.139 37.191  1.00 35.36 ? 195 TYR   C OH   1 
ATOM   5286 N  N    . GLY   C 1 217 ? -40.622 -15.671 39.709  1.00 21.88 ? 196 GLY   C N    1 
ATOM   5287 C  CA   . GLY   C 1 217 ? -41.661 -14.816 40.257  1.00 21.13 ? 196 GLY   C CA   1 
ATOM   5288 C  C    . GLY   C 1 217 ? -41.235 -13.352 40.345  1.00 20.83 ? 196 GLY   C C    1 
ATOM   5289 O  O    . GLY   C 1 217 ? -41.911 -12.582 41.029  1.00 22.98 ? 196 GLY   C O    1 
ATOM   5290 N  N    . ILE   C 1 218 ? -40.142 -12.962 39.662  1.00 17.70 ? 197 ILE   C N    1 
ATOM   5291 C  CA   . ILE   C 1 218 ? -39.684 -11.572 39.694  1.00 15.43 ? 197 ILE   C CA   1 
ATOM   5292 C  C    . ILE   C 1 218 ? -40.340 -10.847 38.525  1.00 15.23 ? 197 ILE   C C    1 
ATOM   5293 O  O    . ILE   C 1 218 ? -40.039 -11.183 37.390  1.00 17.22 ? 197 ILE   C O    1 
ATOM   5294 C  CB   . ILE   C 1 218 ? -38.154 -11.456 39.595  1.00 15.64 ? 197 ILE   C CB   1 
ATOM   5295 C  CG1  . ILE   C 1 218 ? -37.460 -12.182 40.781  1.00 15.84 ? 197 ILE   C CG1  1 
ATOM   5296 C  CG2  . ILE   C 1 218 ? -37.758 -9.976  39.533  1.00 16.55 ? 197 ILE   C CG2  1 
ATOM   5297 C  CD1  . ILE   C 1 218 ? -35.974 -12.416 40.577  1.00 17.64 ? 197 ILE   C CD1  1 
ATOM   5298 N  N    . ARG   C 1 219 ? -41.183 -9.842  38.811  1.00 14.37 ? 198 ARG   C N    1 
ATOM   5299 C  CA   . ARG   C 1 219 ? -41.810 -9.083  37.741  1.00 13.93 ? 198 ARG   C CA   1 
ATOM   5300 C  C    . ARG   C 1 219 ? -40.880 -7.929  37.376  1.00 14.58 ? 198 ARG   C C    1 
ATOM   5301 O  O    . ARG   C 1 219 ? -40.134 -7.462  38.217  1.00 15.30 ? 198 ARG   C O    1 
ATOM   5302 C  CB   . ARG   C 1 219 ? -43.172 -8.555  38.210  1.00 14.48 ? 198 ARG   C CB   1 
ATOM   5303 C  CG   . ARG   C 1 219 ? -44.110 -9.716  38.522  1.00 14.53 ? 198 ARG   C CG   1 
ATOM   5304 C  CD   . ARG   C 1 219 ? -45.478 -9.252  39.011  1.00 15.31 ? 198 ARG   C CD   1 
ATOM   5305 N  NE   . ARG   C 1 219 ? -45.375 -8.469  40.249  1.00 15.07 ? 198 ARG   C NE   1 
ATOM   5306 C  CZ   . ARG   C 1 219 ? -45.382 -7.134  40.320  1.00 15.53 ? 198 ARG   C CZ   1 
ATOM   5307 N  NH1  . ARG   C 1 219 ? -45.636 -6.382  39.249  1.00 16.01 ? 198 ARG   C NH1  1 
ATOM   5308 N  NH2  . ARG   C 1 219 ? -45.130 -6.557  41.491  1.00 17.05 ? 198 ARG   C NH2  1 
ATOM   5309 N  N    . VAL   C 1 220 ? -40.878 -7.545  36.095  1.00 12.93 ? 199 VAL   C N    1 
ATOM   5310 C  CA   . VAL   C 1 220 ? -40.015 -6.463  35.640  1.00 12.87 ? 199 VAL   C CA   1 
ATOM   5311 C  C    . VAL   C 1 220 ? -40.850 -5.543  34.763  1.00 12.33 ? 199 VAL   C C    1 
ATOM   5312 O  O    . VAL   C 1 220 ? -41.350 -5.975  33.723  1.00 13.60 ? 199 VAL   C O    1 
ATOM   5313 C  CB   . VAL   C 1 220 ? -38.811 -6.996  34.841  1.00 12.51 ? 199 VAL   C CB   1 
ATOM   5314 C  CG1  . VAL   C 1 220 ? -37.865 -5.866  34.445  1.00 13.35 ? 199 VAL   C CG1  1 
ATOM   5315 C  CG2  . VAL   C 1 220 ? -38.027 -8.044  35.626  1.00 13.89 ? 199 VAL   C CG2  1 
ATOM   5316 N  N    . ASN   C 1 221 ? -40.973 -4.268  35.195  1.00 13.54 ? 200 ASN   C N    1 
ATOM   5317 C  CA   . ASN   C 1 221 ? -41.860 -3.324  34.523  1.00 13.31 ? 200 ASN   C CA   1 
ATOM   5318 C  C    . ASN   C 1 221 ? -41.178 -1.969  34.424  1.00 14.05 ? 200 ASN   C C    1 
ATOM   5319 O  O    . ASN   C 1 221 ? -40.110 -1.777  35.002  1.00 14.21 ? 200 ASN   C O    1 
ATOM   5320 C  CB   . ASN   C 1 221 ? -43.190 -3.185  35.267  1.00 13.45 ? 200 ASN   C CB   1 
ATOM   5321 C  CG   . ASN   C 1 221 ? -43.957 -4.487  35.247  1.00 13.18 ? 200 ASN   C CG   1 
ATOM   5322 O  OD1  . ASN   C 1 221 ? -44.441 -4.914  34.195  1.00 13.75 ? 200 ASN   C OD1  1 
ATOM   5323 N  ND2  . ASN   C 1 221 ? -44.109 -5.104  36.410  1.00 13.84 ? 200 ASN   C ND2  1 
ATOM   5324 N  N    . GLY   C 1 222 ? -41.816 -1.050  33.687  1.00 13.28 ? 201 GLY   C N    1 
ATOM   5325 C  CA   . GLY   C 1 222 ? -41.256 0.285   33.500  1.00 13.67 ? 201 GLY   C CA   1 
ATOM   5326 C  C    . GLY   C 1 222 ? -42.321 1.334   33.765  1.00 13.24 ? 201 GLY   C C    1 
ATOM   5327 O  O    . GLY   C 1 222 ? -43.524 1.073   33.626  1.00 13.84 ? 201 GLY   C O    1 
ATOM   5328 N  N    . VAL   C 1 223 ? -41.843 2.520   34.123  1.00 12.40 ? 202 VAL   C N    1 
ATOM   5329 C  CA   . VAL   C 1 223 ? -42.668 3.713   34.212  1.00 13.31 ? 202 VAL   C CA   1 
ATOM   5330 C  C    . VAL   C 1 223 ? -42.001 4.744   33.331  1.00 13.06 ? 202 VAL   C C    1 
ATOM   5331 O  O    . VAL   C 1 223 ? -40.804 4.979   33.479  1.00 14.18 ? 202 VAL   C O    1 
ATOM   5332 C  CB   . VAL   C 1 223 ? -42.752 4.240   35.653  1.00 13.21 ? 202 VAL   C CB   1 
ATOM   5333 C  CG1  . VAL   C 1 223 ? -43.422 5.622   35.694  1.00 14.95 ? 202 VAL   C CG1  1 
ATOM   5334 C  CG2  . VAL   C 1 223 ? -43.526 3.250   36.498  1.00 15.08 ? 202 VAL   C CG2  1 
ATOM   5335 N  N    . ALA   C 1 224 ? -42.788 5.318   32.401  1.00 14.15 ? 203 ALA   C N    1 
ATOM   5336 C  CA   . ALA   C 1 224 ? -42.228 6.189   31.378  1.00 14.76 ? 203 ALA   C CA   1 
ATOM   5337 C  C    . ALA   C 1 224 ? -42.812 7.588   31.562  1.00 14.93 ? 203 ALA   C C    1 
ATOM   5338 O  O    . ALA   C 1 224 ? -43.896 7.872   31.051  1.00 14.96 ? 203 ALA   C O    1 
ATOM   5339 C  CB   . ALA   C 1 224 ? -42.554 5.613   29.994  1.00 13.85 ? 203 ALA   C CB   1 
ATOM   5340 N  N    . PRO   C 1 225 ? -42.124 8.498   32.292  1.00 13.97 ? 204 PRO   C N    1 
ATOM   5341 C  CA   . PRO   C 1 225 ? -42.570 9.892   32.376  1.00 14.84 ? 204 PRO   C CA   1 
ATOM   5342 C  C    . PRO   C 1 225 ? -42.456 10.531  30.997  1.00 16.63 ? 204 PRO   C C    1 
ATOM   5343 O  O    . PRO   C 1 225 ? -41.625 10.135  30.166  1.00 15.59 ? 204 PRO   C O    1 
ATOM   5344 C  CB   . PRO   C 1 225 ? -41.571 10.544  33.352  1.00 14.94 ? 204 PRO   C CB   1 
ATOM   5345 C  CG   . PRO   C 1 225 ? -40.887 9.383   34.046  1.00 15.44 ? 204 PRO   C CG   1 
ATOM   5346 C  CD   . PRO   C 1 225 ? -40.858 8.260   33.018  1.00 14.21 ? 204 PRO   C CD   1 
ATOM   5347 N  N    . GLY   C 1 226 ? -43.239 11.604  30.809  1.00 17.44 ? 205 GLY   C N    1 
ATOM   5348 C  CA   . GLY   C 1 226 ? -43.028 12.495  29.681  1.00 19.26 ? 205 GLY   C CA   1 
ATOM   5349 C  C    . GLY   C 1 226 ? -42.178 13.680  30.113  1.00 20.55 ? 205 GLY   C C    1 
ATOM   5350 O  O    . GLY   C 1 226 ? -40.946 13.602  30.098  1.00 23.32 ? 205 GLY   C O    1 
ATOM   5351 N  N    . VAL   C 1 227 ? -42.842 14.780  30.464  1.00 18.82 ? 206 VAL   C N    1 
ATOM   5352 C  CA   . VAL   C 1 227 ? -42.162 15.809  31.227  1.00 19.14 ? 206 VAL   C CA   1 
ATOM   5353 C  C    . VAL   C 1 227 ? -42.661 15.772  32.668  1.00 19.56 ? 206 VAL   C C    1 
ATOM   5354 O  O    . VAL   C 1 227 ? -43.861 15.856  32.957  1.00 19.68 ? 206 VAL   C O    1 
ATOM   5355 C  CB   . VAL   C 1 227 ? -42.187 17.224  30.615  1.00 22.88 ? 206 VAL   C CB   1 
ATOM   5356 C  CG1  . VAL   C 1 227 ? -41.482 17.236  29.265  1.00 24.00 ? 206 VAL   C CG1  1 
ATOM   5357 C  CG2  . VAL   C 1 227 ? -43.592 17.803  30.510  1.00 22.27 ? 206 VAL   C CG2  1 
ATOM   5358 N  N    . SER   C 1 228 ? -41.694 15.606  33.568  1.00 19.52 ? 207 SER   C N    1 
ATOM   5359 C  CA   . SER   C 1 228 ? -41.907 15.696  34.994  1.00 20.85 ? 207 SER   C CA   1 
ATOM   5360 C  C    . SER   C 1 228 ? -41.038 16.858  35.452  1.00 24.01 ? 207 SER   C C    1 
ATOM   5361 O  O    . SER   C 1 228 ? -40.987 17.870  34.754  1.00 24.47 ? 207 SER   C O    1 
ATOM   5362 C  CB   . SER   C 1 228 ? -41.599 14.373  35.659  1.00 20.01 ? 207 SER   C CB   1 
ATOM   5363 O  OG   . SER   C 1 228 ? -41.845 14.414  37.057  1.00 20.20 ? 207 SER   C OG   1 
ATOM   5364 N  N    . LEU   C 1 229 ? -40.313 16.704  36.564  1.00 23.58 ? 208 LEU   C N    1 
ATOM   5365 C  CA   . LEU   C 1 229 ? -39.487 17.813  37.026  1.00 22.67 ? 208 LEU   C CA   1 
ATOM   5366 C  C    . LEU   C 1 229 ? -38.501 18.215  35.930  1.00 22.45 ? 208 LEU   C C    1 
ATOM   5367 O  O    . LEU   C 1 229 ? -37.687 17.414  35.478  1.00 20.36 ? 208 LEU   C O    1 
ATOM   5368 C  CB   . LEU   C 1 229 ? -38.764 17.423  38.313  1.00 22.15 ? 208 LEU   C CB   1 
ATOM   5369 C  CG   . LEU   C 1 229 ? -39.659 16.985  39.478  1.00 23.89 ? 208 LEU   C CG   1 
ATOM   5370 C  CD1  . LEU   C 1 229 ? -38.824 16.722  40.721  1.00 23.89 ? 208 LEU   C CD1  1 
ATOM   5371 C  CD2  . LEU   C 1 229 ? -40.754 17.997  39.758  1.00 24.62 ? 208 LEU   C CD2  1 
ATOM   5372 N  N    . LEU   C 1 230 ? -38.560 19.483  35.522  1.00 20.88 ? 209 LEU   C N    1 
ATOM   5373 C  CA   . LEU   C 1 230 ? -37.718 19.946  34.435  1.00 22.94 ? 209 LEU   C CA   1 
ATOM   5374 C  C    . LEU   C 1 230 ? -36.303 20.201  34.949  1.00 23.27 ? 209 LEU   C C    1 
ATOM   5375 O  O    . LEU   C 1 230 ? -36.093 20.255  36.162  1.00 23.76 ? 209 LEU   C O    1 
ATOM   5376 C  CB   . LEU   C 1 230 ? -38.408 21.156  33.800  1.00 24.03 ? 209 LEU   C CB   1 
ATOM   5377 C  CG   . LEU   C 1 230 ? -39.706 20.796  33.058  1.00 28.03 ? 209 LEU   C CG   1 
ATOM   5378 C  CD1  . LEU   C 1 230 ? -40.642 21.966  32.860  1.00 30.33 ? 209 LEU   C CD1  1 
ATOM   5379 C  CD2  . LEU   C 1 230 ? -39.385 20.137  31.717  1.00 29.25 ? 209 LEU   C CD2  1 
ATOM   5380 N  N    . PRO   C 1 231 ? -35.293 20.309  34.048  1.00 25.13 ? 210 PRO   C N    1 
ATOM   5381 C  CA   . PRO   C 1 231 ? -33.892 20.414  34.463  1.00 27.33 ? 210 PRO   C CA   1 
ATOM   5382 C  C    . PRO   C 1 231 ? -33.683 21.661  35.318  1.00 27.95 ? 210 PRO   C C    1 
ATOM   5383 O  O    . PRO   C 1 231 ? -34.253 22.718  35.049  1.00 26.06 ? 210 PRO   C O    1 
ATOM   5384 C  CB   . PRO   C 1 231 ? -33.129 20.453  33.118  1.00 28.77 ? 210 PRO   C CB   1 
ATOM   5385 C  CG   . PRO   C 1 231 ? -34.075 19.754  32.153  1.00 28.25 ? 210 PRO   C CG   1 
ATOM   5386 C  CD   . PRO   C 1 231 ? -35.435 20.294  32.580  1.00 27.24 ? 210 PRO   C CD   1 
ATOM   5387 N  N    . VAL   C 1 232 ? -32.904 21.500  36.392  1.00 29.26 ? 211 VAL   C N    1 
ATOM   5388 C  CA   . VAL   C 1 232 ? -32.669 22.584  37.334  1.00 35.01 ? 211 VAL   C CA   1 
ATOM   5389 C  C    . VAL   C 1 232 ? -32.075 23.803  36.629  1.00 35.18 ? 211 VAL   C C    1 
ATOM   5390 O  O    . VAL   C 1 232 ? -32.361 24.933  37.019  1.00 35.26 ? 211 VAL   C O    1 
ATOM   5391 C  CB   . VAL   C 1 232 ? -31.844 22.093  38.543  1.00 39.55 ? 211 VAL   C CB   1 
ATOM   5392 C  CG1  . VAL   C 1 232 ? -30.726 23.050  38.946  1.00 43.65 ? 211 VAL   C CG1  1 
ATOM   5393 C  CG2  . VAL   C 1 232 ? -32.754 21.773  39.722  1.00 44.14 ? 211 VAL   C CG2  1 
ATOM   5394 N  N    . ALA   C 1 233 ? -31.299 23.572  35.565  1.00 33.15 ? 212 ALA   C N    1 
ATOM   5395 C  CA   . ALA   C 1 233 ? -30.614 24.652  34.869  1.00 35.53 ? 212 ALA   C CA   1 
ATOM   5396 C  C    . ALA   C 1 233 ? -31.538 25.388  33.896  1.00 33.83 ? 212 ALA   C C    1 
ATOM   5397 O  O    . ALA   C 1 233 ? -31.172 26.439  33.378  1.00 33.63 ? 212 ALA   C O    1 
ATOM   5398 C  CB   . ALA   C 1 233 ? -29.383 24.117  34.165  1.00 38.98 ? 212 ALA   C CB   1 
ATOM   5399 N  N    . MET   C 1 234 ? -32.741 24.851  33.656  1.00 28.26 ? 213 MET   C N    1 
ATOM   5400 C  CA   . MET   C 1 234 ? -33.587 25.384  32.599  1.00 26.19 ? 213 MET   C CA   1 
ATOM   5401 C  C    . MET   C 1 234 ? -34.295 26.636  33.116  1.00 25.61 ? 213 MET   C C    1 
ATOM   5402 O  O    . MET   C 1 234 ? -34.852 26.620  34.206  1.00 27.31 ? 213 MET   C O    1 
ATOM   5403 C  CB   . MET   C 1 234 ? -34.605 24.336  32.129  1.00 26.08 ? 213 MET   C CB   1 
ATOM   5404 C  CG   . MET   C 1 234 ? -35.487 24.813  30.987  1.00 26.67 ? 213 MET   C CG   1 
ATOM   5405 S  SD   . MET   C 1 234 ? -36.592 23.528  30.362  1.00 27.55 ? 213 MET   C SD   1 
ATOM   5406 C  CE   . MET   C 1 234 ? -35.450 22.583  29.342  1.00 29.63 ? 213 MET   C CE   1 
ATOM   5407 N  N    . GLY   C 1 235 ? -34.281 27.713  32.321  1.00 28.01 ? 214 GLY   C N    1 
ATOM   5408 C  CA   . GLY   C 1 235 ? -35.041 28.907  32.670  1.00 27.30 ? 214 GLY   C CA   1 
ATOM   5409 C  C    . GLY   C 1 235 ? -36.544 28.625  32.663  1.00 26.67 ? 214 GLY   C C    1 
ATOM   5410 O  O    . GLY   C 1 235 ? -37.001 27.724  31.962  1.00 25.63 ? 214 GLY   C O    1 
ATOM   5411 N  N    . GLU   C 1 236 ? -37.304 29.430  33.417  1.00 24.89 ? 215 GLU   C N    1 
ATOM   5412 C  CA   A GLU   C 1 236 ? -38.745 29.256  33.550  0.50 26.50 ? 215 GLU   C CA   1 
ATOM   5413 C  CA   B GLU   C 1 236 ? -38.744 29.245  33.547  0.50 24.45 ? 215 GLU   C CA   1 
ATOM   5414 C  C    . GLU   C 1 236 ? -39.455 29.472  32.213  1.00 25.04 ? 215 GLU   C C    1 
ATOM   5415 O  O    . GLU   C 1 236 ? -40.493 28.867  31.958  1.00 25.42 ? 215 GLU   C O    1 
ATOM   5416 C  CB   A GLU   C 1 236 ? -39.357 30.188  34.598  0.50 29.63 ? 215 GLU   C CB   1 
ATOM   5417 C  CB   B GLU   C 1 236 ? -39.343 30.146  34.628  0.50 24.08 ? 215 GLU   C CB   1 
ATOM   5418 C  CG   A GLU   C 1 236 ? -40.509 29.520  35.339  0.50 34.59 ? 215 GLU   C CG   1 
ATOM   5419 C  CG   B GLU   C 1 236 ? -38.896 29.767  36.036  0.50 24.21 ? 215 GLU   C CG   1 
ATOM   5420 C  CD   A GLU   C 1 236 ? -39.886 28.328  36.042  0.50 37.39 ? 215 GLU   C CD   1 
ATOM   5421 C  CD   B GLU   C 1 236 ? -39.319 28.362  36.427  0.50 25.12 ? 215 GLU   C CD   1 
ATOM   5422 O  OE1  A GLU   C 1 236 ? -38.763 28.518  36.562  0.50 40.13 ? 215 GLU   C OE1  1 
ATOM   5423 O  OE1  B GLU   C 1 236 ? -40.460 28.001  36.077  0.50 25.88 ? 215 GLU   C OE1  1 
ATOM   5424 O  OE2  A GLU   C 1 236 ? -40.474 27.225  36.048  0.50 40.04 ? 215 GLU   C OE2  1 
ATOM   5425 O  OE2  B GLU   C 1 236 ? -38.527 27.644  37.076  0.50 25.77 ? 215 GLU   C OE2  1 
ATOM   5426 N  N    . GLU   C 1 237 ? -38.924 30.372  31.371  1.00 24.97 ? 216 GLU   C N    1 
ATOM   5427 C  CA   . GLU   C 1 237 ? -39.539 30.623  30.074  1.00 26.77 ? 216 GLU   C CA   1 
ATOM   5428 C  C    . GLU   C 1 237 ? -39.539 29.334  29.245  1.00 25.90 ? 216 GLU   C C    1 
ATOM   5429 O  O    . GLU   C 1 237 ? -40.544 28.959  28.622  1.00 27.01 ? 216 GLU   C O    1 
ATOM   5430 C  CB   . GLU   C 1 237 ? -38.782 31.765  29.391  1.00 30.26 ? 216 GLU   C CB   1 
ATOM   5431 C  CG   . GLU   C 1 237 ? -39.367 32.214  28.055  0.50 32.04 ? 216 GLU   C CG   1 
ATOM   5432 C  CD   . GLU   C 1 237 ? -38.573 33.300  27.338  0.50 35.51 ? 216 GLU   C CD   1 
ATOM   5433 O  OE1  . GLU   C 1 237 ? -39.060 33.773  26.288  0.50 37.00 ? 216 GLU   C OE1  1 
ATOM   5434 O  OE2  . GLU   C 1 237 ? -37.471 33.672  27.802  0.50 36.45 ? 216 GLU   C OE2  1 
ATOM   5435 N  N    . GLU   C 1 238 ? -38.394 28.652  29.250  1.00 24.12 ? 217 GLU   C N    1 
ATOM   5436 C  CA   . GLU   C 1 238 ? -38.246 27.417  28.497  1.00 25.64 ? 217 GLU   C CA   1 
ATOM   5437 C  C    . GLU   C 1 238 ? -39.059 26.297  29.147  1.00 23.67 ? 217 GLU   C C    1 
ATOM   5438 O  O    . GLU   C 1 238 ? -39.676 25.490  28.453  1.00 23.47 ? 217 GLU   C O    1 
ATOM   5439 C  CB   . GLU   C 1 238 ? -36.765 27.064  28.403  1.00 29.18 ? 217 GLU   C CB   1 
ATOM   5440 C  CG   . GLU   C 1 238 ? -36.484 25.872  27.494  1.00 30.38 ? 217 GLU   C CG   1 
ATOM   5441 C  CD   . GLU   C 1 238 ? -34.995 25.638  27.307  0.70 33.74 ? 217 GLU   C CD   1 
ATOM   5442 O  OE1  . GLU   C 1 238 ? -34.178 26.236  28.044  0.70 36.43 ? 217 GLU   C OE1  1 
ATOM   5443 O  OE2  . GLU   C 1 238 ? -34.652 24.856  26.399  0.70 36.12 ? 217 GLU   C OE2  1 
ATOM   5444 N  N    . LYS   C 1 239 ? -39.077 26.257  30.483  1.00 22.46 ? 218 LYS   C N    1 
ATOM   5445 C  CA   . LYS   C 1 239 ? -39.913 25.291  31.187  1.00 22.66 ? 218 LYS   C CA   1 
ATOM   5446 C  C    . LYS   C 1 239 ? -41.367 25.457  30.749  1.00 22.96 ? 218 LYS   C C    1 
ATOM   5447 O  O    . LYS   C 1 239 ? -42.081 24.485  30.517  1.00 21.90 ? 218 LYS   C O    1 
ATOM   5448 C  CB   . LYS   C 1 239 ? -39.833 25.427  32.711  1.00 22.10 ? 218 LYS   C CB   1 
ATOM   5449 C  CG   . LYS   C 1 239 ? -38.517 24.982  33.328  1.00 22.01 ? 218 LYS   C CG   1 
ATOM   5450 C  CD   . LYS   C 1 239 ? -38.594 24.892  34.849  1.00 24.55 ? 218 LYS   C CD   1 
ATOM   5451 C  CE   . LYS   C 1 239 ? -37.316 24.404  35.455  1.00 29.65 ? 218 LYS   C CE   1 
ATOM   5452 N  NZ   . LYS   C 1 239 ? -37.192 24.836  36.850  1.00 38.84 ? 218 LYS   C NZ   1 
ATOM   5453 N  N    . ASP   C 1 240 ? -41.814 26.710  30.650  1.00 22.65 ? 219 ASP   C N    1 
ATOM   5454 C  CA   . ASP   C 1 240 ? -43.194 26.988  30.302  1.00 23.19 ? 219 ASP   C CA   1 
ATOM   5455 C  C    . ASP   C 1 240 ? -43.512 26.517  28.883  1.00 23.35 ? 219 ASP   C C    1 
ATOM   5456 O  O    . ASP   C 1 240 ? -44.639 26.105  28.617  1.00 25.40 ? 219 ASP   C O    1 
ATOM   5457 C  CB   . ASP   C 1 240 ? -43.521 28.461  30.496  1.00 24.96 ? 219 ASP   C CB   1 
ATOM   5458 C  CG   . ASP   C 1 240 ? -43.716 28.903  31.939  1.00 28.73 ? 219 ASP   C CG   1 
ATOM   5459 O  OD1  . ASP   C 1 240 ? -43.899 28.030  32.820  1.00 29.20 ? 219 ASP   C OD1  1 
ATOM   5460 O  OD2  . ASP   C 1 240 ? -43.691 30.131  32.178  1.00 28.43 ? 219 ASP   C OD2  1 
ATOM   5461 N  N    . LYS   C 1 241 ? -42.524 26.561  27.981  1.00 23.12 ? 220 LYS   C N    1 
ATOM   5462 C  CA   . LYS   C 1 241 ? -42.748 26.119  26.613  1.00 23.61 ? 220 LYS   C CA   1 
ATOM   5463 C  C    . LYS   C 1 241 ? -43.058 24.623  26.636  1.00 23.80 ? 220 LYS   C C    1 
ATOM   5464 O  O    . LYS   C 1 241 ? -43.921 24.154  25.899  1.00 25.45 ? 220 LYS   C O    1 
ATOM   5465 C  CB   . LYS   C 1 241 ? -41.558 26.442  25.705  1.00 26.57 ? 220 LYS   C CB   1 
ATOM   5466 C  CG   . LYS   C 1 241 ? -41.341 27.934  25.478  0.60 27.65 ? 220 LYS   C CG   1 
ATOM   5467 C  CD   . LYS   C 1 241 ? -40.202 28.230  24.510  0.60 29.96 ? 220 LYS   C CD   1 
ATOM   5468 C  CE   . LYS   C 1 241 ? -39.911 29.695  24.437  0.60 31.52 ? 220 LYS   C CE   1 
ATOM   5469 N  NZ   . LYS   C 1 241 ? -38.903 29.964  23.412  0.60 33.84 ? 220 LYS   C NZ   1 
ATOM   5470 N  N    . TRP   C 1 242 ? -42.393 23.896  27.541  1.00 21.38 ? 221 TRP   C N    1 
ATOM   5471 C  CA   . TRP   C 1 242 ? -42.687 22.472  27.635  1.00 21.68 ? 221 TRP   C CA   1 
ATOM   5472 C  C    . TRP   C 1 242 ? -44.046 22.216  28.283  1.00 20.85 ? 221 TRP   C C    1 
ATOM   5473 O  O    . TRP   C 1 242 ? -44.800 21.353  27.828  1.00 23.56 ? 221 TRP   C O    1 
ATOM   5474 C  CB   . TRP   C 1 242 ? -41.566 21.734  28.372  1.00 22.97 ? 221 TRP   C CB   1 
ATOM   5475 C  CG   . TRP   C 1 242 ? -40.391 21.517  27.464  1.00 24.31 ? 221 TRP   C CG   1 
ATOM   5476 C  CD1  . TRP   C 1 242 ? -39.317 22.341  27.289  1.00 26.44 ? 221 TRP   C CD1  1 
ATOM   5477 C  CD2  . TRP   C 1 242 ? -40.240 20.432  26.525  1.00 26.63 ? 221 TRP   C CD2  1 
ATOM   5478 N  NE1  . TRP   C 1 242 ? -38.475 21.814  26.341  1.00 29.05 ? 221 TRP   C NE1  1 
ATOM   5479 C  CE2  . TRP   C 1 242 ? -39.018 20.653  25.852  1.00 28.39 ? 221 TRP   C CE2  1 
ATOM   5480 C  CE3  . TRP   C 1 242 ? -41.003 19.299  26.210  1.00 27.49 ? 221 TRP   C CE3  1 
ATOM   5481 C  CZ2  . TRP   C 1 242 ? -38.550 19.777  24.873  1.00 28.07 ? 221 TRP   C CZ2  1 
ATOM   5482 C  CZ3  . TRP   C 1 242 ? -40.540 18.434  25.241  1.00 30.12 ? 221 TRP   C CZ3  1 
ATOM   5483 C  CH2  . TRP   C 1 242 ? -39.329 18.677  24.587  1.00 28.19 ? 221 TRP   C CH2  1 
ATOM   5484 N  N    . ARG   C 1 243 ? -44.345 22.947  29.360  1.00 19.66 ? 222 ARG   C N    1 
ATOM   5485 C  CA   . ARG   C 1 243 ? -45.597 22.779  30.085  1.00 20.03 ? 222 ARG   C CA   1 
ATOM   5486 C  C    . ARG   C 1 243 ? -46.780 22.960  29.130  1.00 21.07 ? 222 ARG   C C    1 
ATOM   5487 O  O    . ARG   C 1 243 ? -47.755 22.206  29.189  1.00 21.53 ? 222 ARG   C O    1 
ATOM   5488 C  CB   . ARG   C 1 243 ? -45.643 23.774  31.255  1.00 22.18 ? 222 ARG   C CB   1 
ATOM   5489 C  CG   . ARG   C 1 243 ? -44.688 23.425  32.388  1.00 22.57 ? 222 ARG   C CG   1 
ATOM   5490 C  CD   . ARG   C 1 243 ? -44.599 24.610  33.334  1.00 24.53 ? 222 ARG   C CD   1 
ATOM   5491 N  NE   . ARG   C 1 243 ? -43.817 24.257  34.519  1.00 24.76 ? 222 ARG   C NE   1 
ATOM   5492 C  CZ   . ARG   C 1 243 ? -42.883 25.017  35.075  1.00 26.17 ? 222 ARG   C CZ   1 
ATOM   5493 N  NH1  . ARG   C 1 243 ? -42.645 26.225  34.586  1.00 26.51 ? 222 ARG   C NH1  1 
ATOM   5494 N  NH2  . ARG   C 1 243 ? -42.221 24.570  36.129  1.00 27.21 ? 222 ARG   C NH2  1 
ATOM   5495 N  N    . ARG   C 1 244 ? -46.684 23.970  28.252  1.00 22.09 ? 223 ARG   C N    1 
ATOM   5496 C  CA   . ARG   C 1 244 ? -47.760 24.337  27.344  1.00 23.15 ? 223 ARG   C CA   1 
ATOM   5497 C  C    . ARG   C 1 244 ? -48.074 23.228  26.335  1.00 22.60 ? 223 ARG   C C    1 
ATOM   5498 O  O    . ARG   C 1 244 ? -49.159 23.242  25.769  1.00 23.46 ? 223 ARG   C O    1 
ATOM   5499 C  CB   . ARG   C 1 244 ? -47.520 25.685  26.650  1.00 23.39 ? 223 ARG   C CB   1 
ATOM   5500 C  CG   . ARG   C 1 244 ? -47.860 26.813  27.614  0.60 27.11 ? 223 ARG   C CG   1 
ATOM   5501 C  CD   . ARG   C 1 244 ? -47.874 28.185  26.977  0.60 29.35 ? 223 ARG   C CD   1 
ATOM   5502 N  NE   . ARG   C 1 244 ? -46.516 28.594  26.614  0.60 30.84 ? 223 ARG   C NE   1 
ATOM   5503 C  CZ   . ARG   C 1 244 ? -45.727 29.378  27.348  0.60 28.96 ? 223 ARG   C CZ   1 
ATOM   5504 N  NH1  . ARG   C 1 244 ? -46.082 29.749  28.566  0.60 31.56 ? 223 ARG   C NH1  1 
ATOM   5505 N  NH2  . ARG   C 1 244 ? -44.566 29.754  26.862  0.60 28.22 ? 223 ARG   C NH2  1 
ATOM   5506 N  N    . LYS   C 1 245 ? -47.163 22.258  26.143  1.00 20.83 ? 224 LYS   C N    1 
ATOM   5507 C  CA   . LYS   C 1 245 ? -47.359 21.187  25.172  1.00 21.69 ? 224 LYS   C CA   1 
ATOM   5508 C  C    . LYS   C 1 245 ? -48.216 20.057  25.745  1.00 19.38 ? 224 LYS   C C    1 
ATOM   5509 O  O    . LYS   C 1 245 ? -48.727 19.233  24.988  1.00 19.65 ? 224 LYS   C O    1 
ATOM   5510 C  CB   . LYS   C 1 245 ? -46.019 20.594  24.732  1.00 22.72 ? 224 LYS   C CB   1 
ATOM   5511 C  CG   . LYS   C 1 245 ? -44.968 21.533  24.122  1.00 24.86 ? 224 LYS   C CG   1 
ATOM   5512 C  CD   . LYS   C 1 245 ? -43.643 20.783  23.998  1.00 26.98 ? 224 LYS   C CD   1 
ATOM   5513 C  CE   . LYS   C 1 245 ? -42.446 21.629  23.645  1.00 28.86 ? 224 LYS   C CE   1 
ATOM   5514 N  NZ   . LYS   C 1 245 ? -42.583 22.258  22.327  1.00 31.30 ? 224 LYS   C NZ   1 
ATOM   5515 N  N    . VAL   C 1 246 ? -48.374 20.008  27.071  1.00 18.33 ? 225 VAL   C N    1 
ATOM   5516 C  CA   . VAL   C 1 246 ? -48.997 18.840  27.692  1.00 16.77 ? 225 VAL   C CA   1 
ATOM   5517 C  C    . VAL   C 1 246 ? -50.517 18.953  27.673  1.00 16.89 ? 225 VAL   C C    1 
ATOM   5518 O  O    . VAL   C 1 246 ? -51.089 19.855  28.300  1.00 17.97 ? 225 VAL   C O    1 
ATOM   5519 C  CB   . VAL   C 1 246 ? -48.529 18.651  29.147  1.00 16.07 ? 225 VAL   C CB   1 
ATOM   5520 C  CG1  . VAL   C 1 246 ? -49.233 17.447  29.776  1.00 16.41 ? 225 VAL   C CG1  1 
ATOM   5521 C  CG2  . VAL   C 1 246 ? -47.011 18.499  29.231  1.00 18.12 ? 225 VAL   C CG2  1 
ATOM   5522 N  N    . PRO   C 1 247 ? -51.241 18.034  26.994  1.00 17.51 ? 226 PRO   C N    1 
ATOM   5523 C  CA   . PRO   C 1 247 ? -52.700 18.128  26.916  1.00 17.52 ? 226 PRO   C CA   1 
ATOM   5524 C  C    . PRO   C 1 247 ? -53.431 18.140  28.255  1.00 18.83 ? 226 PRO   C C    1 
ATOM   5525 O  O    . PRO   C 1 247 ? -54.377 18.915  28.438  1.00 17.87 ? 226 PRO   C O    1 
ATOM   5526 C  CB   . PRO   C 1 247 ? -53.116 16.929  26.045  1.00 18.22 ? 226 PRO   C CB   1 
ATOM   5527 C  CG   . PRO   C 1 247 ? -51.856 16.596  25.258  1.00 18.59 ? 226 PRO   C CG   1 
ATOM   5528 C  CD   . PRO   C 1 247 ? -50.686 16.916  26.195  1.00 16.75 ? 226 PRO   C CD   1 
ATOM   5529 N  N    . LEU   C 1 248 ? -52.978 17.293  29.192  1.00 17.39 ? 227 LEU   C N    1 
ATOM   5530 C  CA   . LEU   C 1 248 ? -53.692 17.152  30.453  1.00 17.90 ? 227 LEU   C CA   1 
ATOM   5531 C  C    . LEU   C 1 248 ? -53.166 18.180  31.452  1.00 19.49 ? 227 LEU   C C    1 
ATOM   5532 O  O    . LEU   C 1 248 ? -52.279 17.900  32.244  1.00 20.95 ? 227 LEU   C O    1 
ATOM   5533 C  CB   . LEU   C 1 248 ? -53.573 15.713  30.968  1.00 18.18 ? 227 LEU   C CB   1 
ATOM   5534 C  CG   . LEU   C 1 248 ? -54.514 15.323  32.116  1.00 18.80 ? 227 LEU   C CG   1 
ATOM   5535 C  CD1  . LEU   C 1 248 ? -55.964 15.255  31.653  1.00 19.53 ? 227 LEU   C CD1  1 
ATOM   5536 C  CD2  . LEU   C 1 248 ? -54.015 13.970  32.628  1.00 19.75 ? 227 LEU   C CD2  1 
ATOM   5537 N  N    . GLY   C 1 249 ? -53.719 19.394  31.401  1.00 20.00 ? 228 GLY   C N    1 
ATOM   5538 C  CA   . GLY   C 1 249 ? -53.465 20.364  32.461  1.00 19.37 ? 228 GLY   C CA   1 
ATOM   5539 C  C    . GLY   C 1 249 ? -52.328 21.339  32.162  1.00 20.91 ? 228 GLY   C C    1 
ATOM   5540 O  O    . GLY   C 1 249 ? -52.056 22.217  32.982  1.00 22.86 ? 228 GLY   C O    1 
ATOM   5541 N  N    . ARG   C 1 250 ? -51.644 21.184  31.019  1.00 19.67 ? 229 ARG   C N    1 
ATOM   5542 C  CA   . ARG   C 1 250 ? -50.606 22.120  30.593  1.00 20.46 ? 229 ARG   C CA   1 
ATOM   5543 C  C    . ARG   C 1 250 ? -49.582 22.327  31.716  1.00 20.08 ? 229 ARG   C C    1 
ATOM   5544 O  O    . ARG   C 1 250 ? -49.192 23.456  32.057  1.00 20.87 ? 229 ARG   C O    1 
ATOM   5545 C  CB   . ARG   C 1 250 ? -51.210 23.459  30.147  1.00 21.72 ? 229 ARG   C CB   1 
ATOM   5546 C  CG   . ARG   C 1 250 ? -52.234 23.380  29.027  1.00 26.31 ? 229 ARG   C CG   1 
ATOM   5547 C  CD   . ARG   C 1 250 ? -51.638 23.048  27.680  1.00 31.37 ? 229 ARG   C CD   1 
ATOM   5548 N  NE   . ARG   C 1 250 ? -52.743 22.643  26.799  1.00 36.31 ? 229 ARG   C NE   1 
ATOM   5549 C  CZ   . ARG   C 1 250 ? -52.639 21.974  25.654  1.00 36.76 ? 229 ARG   C CZ   1 
ATOM   5550 N  NH1  . ARG   C 1 250 ? -51.457 21.741  25.108  1.00 34.80 ? 229 ARG   C NH1  1 
ATOM   5551 N  NH2  . ARG   C 1 250 ? -53.735 21.544  25.049  1.00 36.51 ? 229 ARG   C NH2  1 
ATOM   5552 N  N    . ARG   C 1 251 ? -49.131 21.207  32.293  1.00 19.27 ? 230 ARG   C N    1 
ATOM   5553 C  CA   A ARG   C 1 251 ? -48.157 21.237  33.369  0.60 19.38 ? 230 ARG   C CA   1 
ATOM   5554 C  CA   B ARG   C 1 251 ? -48.165 21.232  33.379  0.40 19.04 ? 230 ARG   C CA   1 
ATOM   5555 C  C    . ARG   C 1 251 ? -47.374 19.933  33.333  1.00 18.54 ? 230 ARG   C C    1 
ATOM   5556 O  O    . ARG   C 1 251 ? -47.858 18.949  32.771  1.00 17.82 ? 230 ARG   C O    1 
ATOM   5557 C  CB   A ARG   C 1 251 ? -48.880 21.326  34.721  0.60 21.34 ? 230 ARG   C CB   1 
ATOM   5558 C  CB   B ARG   C 1 251 ? -48.837 21.332  34.758  0.40 19.88 ? 230 ARG   C CB   1 
ATOM   5559 C  CG   A ARG   C 1 251 ? -49.929 20.238  34.917  0.60 23.80 ? 230 ARG   C CG   1 
ATOM   5560 C  CG   B ARG   C 1 251 ? -49.786 20.196  35.121  0.40 21.03 ? 230 ARG   C CG   1 
ATOM   5561 C  CD   A ARG   C 1 251 ? -50.839 20.484  36.114  0.60 27.82 ? 230 ARG   C CD   1 
ATOM   5562 C  CD   B ARG   C 1 251 ? -50.330 20.248  36.553  0.40 22.43 ? 230 ARG   C CD   1 
ATOM   5563 N  NE   A ARG   C 1 251 ? -51.520 21.778  35.997  0.60 30.95 ? 230 ARG   C NE   1 
ATOM   5564 N  NE   B ARG   C 1 251 ? -49.486 19.615  37.574  0.40 23.91 ? 230 ARG   C NE   1 
ATOM   5565 C  CZ   A ARG   C 1 251 ? -52.831 21.990  36.082  0.60 33.89 ? 230 ARG   C CZ   1 
ATOM   5566 C  CZ   B ARG   C 1 251 ? -49.412 18.312  37.842  0.40 25.60 ? 230 ARG   C CZ   1 
ATOM   5567 N  NH1  A ARG   C 1 251 ? -53.287 23.228  36.089  0.60 34.69 ? 230 ARG   C NH1  1 
ATOM   5568 N  NH1  B ARG   C 1 251 ? -48.621 17.881  38.806  0.40 25.77 ? 230 ARG   C NH1  1 
ATOM   5569 N  NH2  A ARG   C 1 251 ? -53.677 20.981  36.197  0.60 36.33 ? 230 ARG   C NH2  1 
ATOM   5570 N  NH2  B ARG   C 1 251 ? -50.140 17.443  37.162  0.40 26.40 ? 230 ARG   C NH2  1 
ATOM   5571 N  N    . GLU   C 1 252 ? -46.189 19.950  33.960  1.00 18.79 ? 231 GLU   C N    1 
ATOM   5572 C  CA   . GLU   C 1 252 ? -45.417 18.727  34.122  1.00 18.62 ? 231 GLU   C CA   1 
ATOM   5573 C  C    . GLU   C 1 252 ? -45.990 17.865  35.251  1.00 18.88 ? 231 GLU   C C    1 
ATOM   5574 O  O    . GLU   C 1 252 ? -46.726 18.342  36.117  1.00 20.12 ? 231 GLU   C O    1 
ATOM   5575 C  CB   . GLU   C 1 252 ? -43.947 19.103  34.335  1.00 21.16 ? 231 GLU   C CB   1 
ATOM   5576 C  CG   . GLU   C 1 252 ? -43.642 19.647  35.731  1.00 21.78 ? 231 GLU   C CG   1 
ATOM   5577 C  CD   . GLU   C 1 252 ? -43.893 21.141  35.901  1.00 25.47 ? 231 GLU   C CD   1 
ATOM   5578 O  OE1  . GLU   C 1 252 ? -43.054 21.758  36.590  1.00 27.81 ? 231 GLU   C OE1  1 
ATOM   5579 O  OE2  . GLU   C 1 252 ? -44.869 21.701  35.345  1.00 24.84 ? 231 GLU   C OE2  1 
ATOM   5580 N  N    . ALA   C 1 253 ? -45.662 16.566  35.210  1.00 18.15 ? 232 ALA   C N    1 
ATOM   5581 C  CA   . ALA   C 1 253 ? -45.963 15.653  36.307  1.00 18.79 ? 232 ALA   C CA   1 
ATOM   5582 C  C    . ALA   C 1 253 ? -45.176 16.034  37.558  1.00 17.84 ? 232 ALA   C C    1 
ATOM   5583 O  O    . ALA   C 1 253 ? -43.981 16.320  37.488  1.00 19.07 ? 232 ALA   C O    1 
ATOM   5584 C  CB   . ALA   C 1 253 ? -45.583 14.233  35.928  1.00 19.17 ? 232 ALA   C CB   1 
ATOM   5585 N  N    . SER   C 1 254 ? -45.838 15.954  38.709  1.00 18.46 ? 233 SER   C N    1 
ATOM   5586 C  CA   . SER   C 1 254 ? -45.057 16.024  39.935  1.00 18.26 ? 233 SER   C CA   1 
ATOM   5587 C  C    . SER   C 1 254 ? -44.256 14.729  40.099  1.00 18.48 ? 233 SER   C C    1 
ATOM   5588 O  O    . SER   C 1 254 ? -44.605 13.672  39.548  1.00 18.59 ? 233 SER   C O    1 
ATOM   5589 C  CB   . SER   C 1 254 ? -45.924 16.297  41.134  1.00 20.64 ? 233 SER   C CB   1 
ATOM   5590 O  OG   . SER   C 1 254 ? -46.736 15.165  41.398  1.00 21.12 ? 233 SER   C OG   1 
ATOM   5591 N  N    . ALA   C 1 255 ? -43.175 14.806  40.884  1.00 17.12 ? 234 ALA   C N    1 
ATOM   5592 C  CA   . ALA   C 1 255 ? -42.428 13.593  41.189  1.00 16.31 ? 234 ALA   C CA   1 
ATOM   5593 C  C    . ALA   C 1 255 ? -43.340 12.559  41.848  1.00 16.38 ? 234 ALA   C C    1 
ATOM   5594 O  O    . ALA   C 1 255 ? -43.197 11.354  41.617  1.00 16.82 ? 234 ALA   C O    1 
ATOM   5595 C  CB   . ALA   C 1 255 ? -41.249 13.937  42.083  1.00 17.64 ? 234 ALA   C CB   1 
ATOM   5596 N  N    . GLU   C 1 256 ? -44.275 13.035  42.692  1.00 16.21 ? 235 GLU   C N    1 
ATOM   5597 C  CA   A GLU   C 1 256 ? -45.234 12.201  43.401  0.50 16.65 ? 235 GLU   C CA   1 
ATOM   5598 C  CA   B GLU   C 1 256 ? -45.202 12.173  43.402  0.50 17.42 ? 235 GLU   C CA   1 
ATOM   5599 C  C    . GLU   C 1 256 ? -46.073 11.400  42.408  1.00 16.89 ? 235 GLU   C C    1 
ATOM   5600 O  O    . GLU   C 1 256 ? -46.355 10.234  42.639  1.00 16.15 ? 235 GLU   C O    1 
ATOM   5601 C  CB   A GLU   C 1 256 ? -46.147 13.056  44.283  0.50 17.19 ? 235 GLU   C CB   1 
ATOM   5602 C  CB   B GLU   C 1 256 ? -45.958 13.008  44.437  0.50 19.44 ? 235 GLU   C CB   1 
ATOM   5603 C  CG   A GLU   C 1 256 ? -47.175 12.236  45.056  0.50 16.77 ? 235 GLU   C CG   1 
ATOM   5604 C  CG   B GLU   C 1 256 ? -45.049 13.626  45.500  0.50 20.91 ? 235 GLU   C CG   1 
ATOM   5605 C  CD   A GLU   C 1 256 ? -48.097 12.994  46.002  0.50 18.44 ? 235 GLU   C CD   1 
ATOM   5606 C  CD   B GLU   C 1 256 ? -43.959 14.647  45.156  0.50 21.94 ? 235 GLU   C CD   1 
ATOM   5607 O  OE1  A GLU   C 1 256 ? -47.885 14.194  46.257  0.50 18.81 ? 235 GLU   C OE1  1 
ATOM   5608 O  OE1  B GLU   C 1 256 ? -42.906 14.562  45.834  0.50 25.53 ? 235 GLU   C OE1  1 
ATOM   5609 O  OE2  A GLU   C 1 256 ? -49.046 12.360  46.485  0.50 18.68 ? 235 GLU   C OE2  1 
ATOM   5610 O  OE2  B GLU   C 1 256 ? -44.120 15.517  44.256  0.50 19.03 ? 235 GLU   C OE2  1 
ATOM   5611 N  N    . GLN   C 1 257 ? -46.466 12.034  41.299  1.00 16.35 ? 236 GLN   C N    1 
ATOM   5612 C  CA   . GLN   C 1 257 ? -47.310 11.341  40.331  1.00 15.99 ? 236 GLN   C CA   1 
ATOM   5613 C  C    . GLN   C 1 257 ? -46.532 10.207  39.656  1.00 14.62 ? 236 GLN   C C    1 
ATOM   5614 O  O    . GLN   C 1 257 ? -47.064 9.110   39.419  1.00 16.27 ? 236 GLN   C O    1 
ATOM   5615 C  CB   . GLN   C 1 257 ? -47.872 12.335  39.314  1.00 16.66 ? 236 GLN   C CB   1 
ATOM   5616 C  CG   . GLN   C 1 257 ? -48.929 13.228  39.950  1.00 18.25 ? 236 GLN   C CG   1 
ATOM   5617 C  CD   . GLN   C 1 257 ? -49.395 14.357  39.058  1.00 19.05 ? 236 GLN   C CD   1 
ATOM   5618 O  OE1  . GLN   C 1 257 ? -48.614 15.005  38.358  1.00 20.59 ? 236 GLN   C OE1  1 
ATOM   5619 N  NE2  . GLN   C 1 257 ? -50.691 14.611  39.112  1.00 21.33 ? 236 GLN   C NE2  1 
ATOM   5620 N  N    . ILE   C 1 258 ? -45.242 10.432  39.399  1.00 15.28 ? 237 ILE   C N    1 
ATOM   5621 C  CA   . ILE   C 1 258 ? -44.427 9.351   38.842  1.00 14.71 ? 237 ILE   C CA   1 
ATOM   5622 C  C    . ILE   C 1 258 ? -44.289 8.224   39.872  1.00 15.94 ? 237 ILE   C C    1 
ATOM   5623 O  O    . ILE   C 1 258 ? -44.435 7.033   39.567  1.00 16.22 ? 237 ILE   C O    1 
ATOM   5624 C  CB   . ILE   C 1 258 ? -43.057 9.897   38.406  1.00 14.87 ? 237 ILE   C CB   1 
ATOM   5625 C  CG1  . ILE   C 1 258 ? -43.186 11.046  37.404  1.00 15.72 ? 237 ILE   C CG1  1 
ATOM   5626 C  CG2  . ILE   C 1 258 ? -42.175 8.779   37.850  1.00 14.84 ? 237 ILE   C CG2  1 
ATOM   5627 C  CD1  . ILE   C 1 258 ? -43.966 10.734  36.138  1.00 18.01 ? 237 ILE   C CD1  1 
ATOM   5628 N  N    . ALA   C 1 259 ? -44.007 8.604   41.124  1.00 14.40 ? 238 ALA   C N    1 
ATOM   5629 C  CA   . ALA   C 1 259 ? -43.887 7.636   42.204  1.00 14.51 ? 238 ALA   C CA   1 
ATOM   5630 C  C    . ALA   C 1 259 ? -45.156 6.802   42.376  1.00 14.98 ? 238 ALA   C C    1 
ATOM   5631 O  O    . ALA   C 1 259 ? -45.056 5.610   42.662  1.00 15.99 ? 238 ALA   C O    1 
ATOM   5632 C  CB   . ALA   C 1 259 ? -43.466 8.322   43.495  1.00 14.60 ? 238 ALA   C CB   1 
ATOM   5633 N  N    . ASP   C 1 260 ? -46.342 7.400   42.202  1.00 15.14 ? 239 ASP   C N    1 
ATOM   5634 C  CA   . ASP   C 1 260 ? -47.596 6.661   42.306  1.00 15.61 ? 239 ASP   C CA   1 
ATOM   5635 C  C    . ASP   C 1 260 ? -47.621 5.466   41.339  1.00 15.28 ? 239 ASP   C C    1 
ATOM   5636 O  O    . ASP   C 1 260 ? -48.165 4.410   41.681  1.00 16.69 ? 239 ASP   C O    1 
ATOM   5637 C  CB   . ASP   C 1 260 ? -48.791 7.557   42.012  1.00 16.29 ? 239 ASP   C CB   1 
ATOM   5638 C  CG   . ASP   C 1 260 ? -49.215 8.531   43.105  1.00 19.93 ? 239 ASP   C CG   1 
ATOM   5639 O  OD1  . ASP   C 1 260 ? -48.945 8.259   44.295  1.00 23.18 ? 239 ASP   C OD1  1 
ATOM   5640 O  OD2  . ASP   C 1 260 ? -49.833 9.561   42.755  1.00 21.43 ? 239 ASP   C OD2  1 
ATOM   5641 N  N    . ALA   C 1 261 ? -47.087 5.623   40.116  1.00 14.66 ? 240 ALA   C N    1 
ATOM   5642 C  CA   . ALA   C 1 261 ? -47.120 4.510   39.169  1.00 14.61 ? 240 ALA   C CA   1 
ATOM   5643 C  C    . ALA   C 1 261 ? -46.120 3.430   39.582  1.00 15.01 ? 240 ALA   C C    1 
ATOM   5644 O  O    . ALA   C 1 261 ? -46.373 2.237   39.390  1.00 14.19 ? 240 ALA   C O    1 
ATOM   5645 C  CB   . ALA   C 1 261 ? -46.872 4.983   37.744  1.00 15.01 ? 240 ALA   C CB   1 
ATOM   5646 N  N    . VAL   C 1 262 ? -44.975 3.840   40.137  1.00 14.91 ? 241 VAL   C N    1 
ATOM   5647 C  CA   . VAL   C 1 262 ? -44.012 2.872   40.647  1.00 15.83 ? 241 VAL   C CA   1 
ATOM   5648 C  C    . VAL   C 1 262 ? -44.650 2.050   41.767  1.00 15.73 ? 241 VAL   C C    1 
ATOM   5649 O  O    . VAL   C 1 262 ? -44.555 0.812   41.792  1.00 16.39 ? 241 VAL   C O    1 
ATOM   5650 C  CB   . VAL   C 1 262 ? -42.739 3.589   41.132  1.00 15.86 ? 241 VAL   C CB   1 
ATOM   5651 C  CG1  . VAL   C 1 262 ? -41.778 2.578   41.758  1.00 17.61 ? 241 VAL   C CG1  1 
ATOM   5652 C  CG2  . VAL   C 1 262 ? -42.061 4.327   39.983  1.00 16.57 ? 241 VAL   C CG2  1 
ATOM   5653 N  N    . ILE   C 1 263 ? -45.295 2.739   42.713  1.00 16.67 ? 242 ILE   C N    1 
ATOM   5654 C  CA   . ILE   C 1 263 ? -45.967 2.084   43.835  1.00 18.61 ? 242 ILE   C CA   1 
ATOM   5655 C  C    . ILE   C 1 263 ? -47.002 1.078   43.336  1.00 17.31 ? 242 ILE   C C    1 
ATOM   5656 O  O    . ILE   C 1 263 ? -47.058 -0.039  43.848  1.00 17.10 ? 242 ILE   C O    1 
ATOM   5657 C  CB   . ILE   C 1 263 ? -46.588 3.095   44.821  1.00 21.61 ? 242 ILE   C CB   1 
ATOM   5658 C  CG1  . ILE   C 1 263 ? -45.515 3.865   45.589  1.00 27.05 ? 242 ILE   C CG1  1 
ATOM   5659 C  CG2  . ILE   C 1 263 ? -47.602 2.416   45.753  1.00 22.37 ? 242 ILE   C CG2  1 
ATOM   5660 C  CD1  . ILE   C 1 263 ? -44.436 3.007   46.216  1.00 30.31 ? 242 ILE   C CD1  1 
ATOM   5661 N  N    . PHE   C 1 264 ? -47.798 1.440   42.315  1.00 15.71 ? 243 PHE   C N    1 
ATOM   5662 C  CA   . PHE   C 1 264 ? -48.767 0.499   41.767  1.00 15.19 ? 243 PHE   C CA   1 
ATOM   5663 C  C    . PHE   C 1 264 ? -48.052 -0.758  41.269  1.00 14.67 ? 243 PHE   C C    1 
ATOM   5664 O  O    . PHE   C 1 264 ? -48.449 -1.883  41.574  1.00 14.71 ? 243 PHE   C O    1 
ATOM   5665 C  CB   . PHE   C 1 264 ? -49.499 1.173   40.597  1.00 15.39 ? 243 PHE   C CB   1 
ATOM   5666 C  CG   . PHE   C 1 264 ? -50.326 0.171   39.800  1.00 15.91 ? 243 PHE   C CG   1 
ATOM   5667 C  CD1  . PHE   C 1 264 ? -51.441 -0.457  40.367  1.00 18.29 ? 243 PHE   C CD1  1 
ATOM   5668 C  CD2  . PHE   C 1 264 ? -49.950 -0.163  38.499  1.00 16.76 ? 243 PHE   C CD2  1 
ATOM   5669 C  CE1  . PHE   C 1 264 ? -52.159 -1.400  39.636  1.00 18.73 ? 243 PHE   C CE1  1 
ATOM   5670 C  CE2  . PHE   C 1 264 ? -50.695 -1.071  37.761  1.00 16.74 ? 243 PHE   C CE2  1 
ATOM   5671 C  CZ   . PHE   C 1 264 ? -51.781 -1.699  38.341  1.00 18.61 ? 243 PHE   C CZ   1 
ATOM   5672 N  N    . LEU   C 1 265 ? -46.966 -0.559  40.513  1.00 14.93 ? 244 LEU   C N    1 
ATOM   5673 C  CA   . LEU   C 1 265 ? -46.316 -1.699  39.886  1.00 14.77 ? 244 LEU   C CA   1 
ATOM   5674 C  C    . LEU   C 1 265 ? -45.655 -2.629  40.901  1.00 15.95 ? 244 LEU   C C    1 
ATOM   5675 O  O    . LEU   C 1 265 ? -45.546 -3.832  40.645  1.00 16.06 ? 244 LEU   C O    1 
ATOM   5676 C  CB   . LEU   C 1 265 ? -45.306 -1.230  38.841  1.00 14.51 ? 244 LEU   C CB   1 
ATOM   5677 C  CG   . LEU   C 1 265 ? -45.932 -0.724  37.540  1.00 14.82 ? 244 LEU   C CG   1 
ATOM   5678 C  CD1  . LEU   C 1 265 ? -44.819 -0.055  36.750  1.00 15.49 ? 244 LEU   C CD1  1 
ATOM   5679 C  CD2  . LEU   C 1 265 ? -46.454 -1.954  36.795  1.00 15.86 ? 244 LEU   C CD2  1 
ATOM   5680 N  N    . VAL   C 1 266 ? -45.209 -2.101  42.047  1.00 14.89 ? 245 VAL   C N    1 
ATOM   5681 C  CA   . VAL   C 1 266 ? -44.592 -2.975  43.036  1.00 16.79 ? 245 VAL   C CA   1 
ATOM   5682 C  C    . VAL   C 1 266 ? -45.663 -3.684  43.873  1.00 18.49 ? 245 VAL   C C    1 
ATOM   5683 O  O    . VAL   C 1 266 ? -45.364 -4.681  44.543  1.00 20.31 ? 245 VAL   C O    1 
ATOM   5684 C  CB   . VAL   C 1 266 ? -43.553 -2.252  43.914  1.00 18.57 ? 245 VAL   C CB   1 
ATOM   5685 C  CG1  . VAL   C 1 266 ? -42.433 -1.649  43.076  1.00 17.65 ? 245 VAL   C CG1  1 
ATOM   5686 C  CG2  . VAL   C 1 266 ? -44.177 -1.207  44.821  1.00 23.52 ? 245 VAL   C CG2  1 
ATOM   5687 N  N    . SER   C 1 267 ? -46.897 -3.148  43.860  1.00 16.41 ? 246 SER   C N    1 
ATOM   5688 C  CA   . SER   C 1 267 ? -47.974 -3.576  44.751  1.00 16.45 ? 246 SER   C CA   1 
ATOM   5689 C  C    . SER   C 1 267 ? -48.564 -4.931  44.359  1.00 18.52 ? 246 SER   C C    1 
ATOM   5690 O  O    . SER   C 1 267 ? -48.387 -5.406  43.236  1.00 18.71 ? 246 SER   C O    1 
ATOM   5691 C  CB   . SER   C 1 267 ? -49.094 -2.542  44.823  1.00 16.38 ? 246 SER   C CB   1 
ATOM   5692 O  OG   . SER   C 1 267 ? -49.963 -2.660  43.698  1.00 17.09 ? 246 SER   C OG   1 
ATOM   5693 N  N    . GLY   C 1 268 ? -49.379 -5.466  45.283  1.00 19.95 ? 247 GLY   C N    1 
ATOM   5694 C  CA   . GLY   C 1 268 ? -50.189 -6.650  45.032  1.00 20.62 ? 247 GLY   C CA   1 
ATOM   5695 C  C    . GLY   C 1 268 ? -51.243 -6.442  43.938  1.00 20.85 ? 247 GLY   C C    1 
ATOM   5696 O  O    . GLY   C 1 268 ? -51.739 -7.417  43.366  1.00 24.60 ? 247 GLY   C O    1 
ATOM   5697 N  N    . SER   C 1 269 ? -51.571 -5.185  43.609  1.00 19.33 ? 248 SER   C N    1 
ATOM   5698 C  CA   . SER   C 1 269 ? -52.549 -4.906  42.568  1.00 18.91 ? 248 SER   C CA   1 
ATOM   5699 C  C    . SER   C 1 269 ? -51.976 -5.093  41.165  1.00 17.09 ? 248 SER   C C    1 
ATOM   5700 O  O    . SER   C 1 269 ? -52.715 -4.931  40.192  1.00 18.57 ? 248 SER   C O    1 
ATOM   5701 C  CB   . SER   C 1 269 ? -53.086 -3.516  42.695  1.00 21.65 ? 248 SER   C CB   1 
ATOM   5702 O  OG   . SER   C 1 269 ? -53.872 -3.442  43.871  1.00 26.96 ? 248 SER   C OG   1 
ATOM   5703 N  N    . ALA   C 1 270 ? -50.667 -5.396  41.079  1.00 16.58 ? 249 ALA   C N    1 
ATOM   5704 C  CA   . ALA   C 1 270 ? -49.986 -5.560  39.802  1.00 15.56 ? 249 ALA   C CA   1 
ATOM   5705 C  C    . ALA   C 1 270 ? -49.350 -6.949  39.687  1.00 16.50 ? 249 ALA   C C    1 
ATOM   5706 O  O    . ALA   C 1 270 ? -48.404 -7.146  38.930  1.00 15.79 ? 249 ALA   C O    1 
ATOM   5707 C  CB   . ALA   C 1 270 ? -48.943 -4.467  39.633  1.00 16.02 ? 249 ALA   C CB   1 
ATOM   5708 N  N    . GLN   C 1 271 ? -49.890 -7.930  40.413  1.00 17.98 ? 250 GLN   C N    1 
ATOM   5709 C  CA   . GLN   C 1 271 ? -49.277 -9.249  40.553  1.00 18.38 ? 250 GLN   C CA   1 
ATOM   5710 C  C    . GLN   C 1 271 ? -49.198 -10.031 39.236  1.00 16.65 ? 250 GLN   C C    1 
ATOM   5711 O  O    . GLN   C 1 271 ? -48.393 -10.960 39.133  1.00 17.85 ? 250 GLN   C O    1 
ATOM   5712 C  CB   . GLN   C 1 271 ? -50.090 -9.898  41.687  1.00 23.78 ? 250 GLN   C CB   1 
ATOM   5713 C  CG   . GLN   C 1 271 ? -50.479 -11.364 41.535  0.60 28.62 ? 250 GLN   C CG   1 
ATOM   5714 C  CD   . GLN   C 1 271 ? -51.663 -11.743 42.409  0.60 31.25 ? 250 GLN   C CD   1 
ATOM   5715 O  OE1  . GLN   C 1 271 ? -52.739 -11.134 42.351  0.60 31.90 ? 250 GLN   C OE1  1 
ATOM   5716 N  NE2  . GLN   C 1 271 ? -51.476 -12.760 43.238  0.60 33.76 ? 250 GLN   C NE2  1 
ATOM   5717 N  N    . TYR   C 1 272 ? -50.016 -9.678  38.234  1.00 15.78 ? 251 TYR   C N    1 
ATOM   5718 C  CA   . TYR   C 1 272 ? -49.967 -10.399 36.973  1.00 15.94 ? 251 TYR   C CA   1 
ATOM   5719 C  C    . TYR   C 1 272 ? -49.257 -9.557  35.914  1.00 15.65 ? 251 TYR   C C    1 
ATOM   5720 O  O    . TYR   C 1 272 ? -49.208 -9.960  34.753  1.00 17.16 ? 251 TYR   C O    1 
ATOM   5721 C  CB   . TYR   C 1 272 ? -51.394 -10.743 36.532  1.00 16.52 ? 251 TYR   C CB   1 
ATOM   5722 C  CG   . TYR   C 1 272 ? -51.499 -11.823 35.463  1.00 16.36 ? 251 TYR   C CG   1 
ATOM   5723 C  CD1  . TYR   C 1 272 ? -51.283 -13.155 35.782  1.00 17.05 ? 251 TYR   C CD1  1 
ATOM   5724 C  CD2  . TYR   C 1 272 ? -51.790 -11.518 34.130  1.00 16.41 ? 251 TYR   C CD2  1 
ATOM   5725 C  CE1  . TYR   C 1 272 ? -51.355 -14.147 34.813  1.00 16.76 ? 251 TYR   C CE1  1 
ATOM   5726 C  CE2  . TYR   C 1 272 ? -51.906 -12.508 33.165  1.00 16.31 ? 251 TYR   C CE2  1 
ATOM   5727 C  CZ   . TYR   C 1 272 ? -51.687 -13.829 33.508  1.00 16.47 ? 251 TYR   C CZ   1 
ATOM   5728 O  OH   . TYR   C 1 272 ? -51.833 -14.782 32.540  1.00 16.97 ? 251 TYR   C OH   1 
ATOM   5729 N  N    . ILE   C 1 273 ? -48.770 -8.371  36.304  1.00 14.95 ? 252 ILE   C N    1 
ATOM   5730 C  CA   . ILE   C 1 273 ? -48.181 -7.467  35.323  1.00 13.94 ? 252 ILE   C CA   1 
ATOM   5731 C  C    . ILE   C 1 273 ? -46.663 -7.670  35.284  1.00 13.88 ? 252 ILE   C C    1 
ATOM   5732 O  O    . ILE   C 1 273 ? -45.982 -7.465  36.286  1.00 14.08 ? 252 ILE   C O    1 
ATOM   5733 C  CB   . ILE   C 1 273 ? -48.533 -6.013  35.667  1.00 13.43 ? 252 ILE   C CB   1 
ATOM   5734 C  CG1  . ILE   C 1 273 ? -50.039 -5.802  35.745  1.00 14.00 ? 252 ILE   C CG1  1 
ATOM   5735 C  CG2  . ILE   C 1 273 ? -47.878 -5.039  34.687  1.00 13.71 ? 252 ILE   C CG2  1 
ATOM   5736 C  CD1  . ILE   C 1 273 ? -50.437 -4.372  36.099  1.00 14.76 ? 252 ILE   C CD1  1 
ATOM   5737 N  N    . THR   C 1 274 ? -46.135 -8.043  34.113  1.00 13.50 ? 253 THR   C N    1 
ATOM   5738 C  CA   . THR   C 1 274 ? -44.693 -8.062  33.901  1.00 13.34 ? 253 THR   C CA   1 
ATOM   5739 C  C    . THR   C 1 274 ? -44.430 -7.712  32.442  1.00 13.45 ? 253 THR   C C    1 
ATOM   5740 O  O    . THR   C 1 274 ? -45.213 -8.095  31.563  1.00 15.68 ? 253 THR   C O    1 
ATOM   5741 C  CB   . THR   C 1 274 ? -44.080 -9.399  34.358  1.00 13.33 ? 253 THR   C CB   1 
ATOM   5742 O  OG1  . THR   C 1 274 ? -42.670 -9.216  34.444  1.00 13.92 ? 253 THR   C OG1  1 
ATOM   5743 C  CG2  . THR   C 1 274 ? -44.380 -10.558 33.425  1.00 15.26 ? 253 THR   C CG2  1 
ATOM   5744 N  N    . GLY   C 1 275 ? -43.308 -7.013  32.217  1.00 13.15 ? 254 GLY   C N    1 
ATOM   5745 C  CA   . GLY   C 1 275 ? -42.902 -6.590  30.888  1.00 14.67 ? 254 GLY   C CA   1 
ATOM   5746 C  C    . GLY   C 1 275 ? -43.710 -5.414  30.345  1.00 14.81 ? 254 GLY   C C    1 
ATOM   5747 O  O    . GLY   C 1 275 ? -43.695 -5.164  29.128  1.00 16.80 ? 254 GLY   C O    1 
ATOM   5748 N  N    . SER   C 1 276 ? -44.461 -4.748  31.230  1.00 14.92 ? 255 SER   C N    1 
ATOM   5749 C  CA   . SER   C 1 276 ? -45.296 -3.612  30.859  1.00 15.47 ? 255 SER   C CA   1 
ATOM   5750 C  C    . SER   C 1 276 ? -44.578 -2.313  31.182  1.00 16.39 ? 255 SER   C C    1 
ATOM   5751 O  O    . SER   C 1 276 ? -43.913 -2.217  32.206  1.00 17.09 ? 255 SER   C O    1 
ATOM   5752 C  CB   . SER   C 1 276 ? -46.592 -3.622  31.592  1.00 16.51 ? 255 SER   C CB   1 
ATOM   5753 O  OG   . SER   C 1 276 ? -47.355 -4.766  31.246  1.00 19.94 ? 255 SER   C OG   1 
ATOM   5754 N  N    . ILE   C 1 277 ? -44.806 -1.313  30.328  1.00 16.13 ? 256 ILE   C N    1 
ATOM   5755 C  CA   . ILE   C 1 277 ? -44.283 0.016   30.584  1.00 16.49 ? 256 ILE   C CA   1 
ATOM   5756 C  C    . ILE   C 1 277 ? -45.458 0.980   30.642  1.00 16.69 ? 256 ILE   C C    1 
ATOM   5757 O  O    . ILE   C 1 277 ? -46.176 1.112   29.654  1.00 19.80 ? 256 ILE   C O    1 
ATOM   5758 C  CB   . ILE   C 1 277 ? -43.237 0.419   29.530  1.00 17.50 ? 256 ILE   C CB   1 
ATOM   5759 C  CG1  . ILE   C 1 277 ? -42.014 -0.503  29.622  1.00 21.14 ? 256 ILE   C CG1  1 
ATOM   5760 C  CG2  . ILE   C 1 277 ? -42.850 1.892   29.741  1.00 19.58 ? 256 ILE   C CG2  1 
ATOM   5761 C  CD1  . ILE   C 1 277 ? -40.971 -0.273  28.545  1.00 24.23 ? 256 ILE   C CD1  1 
ATOM   5762 N  N    . ILE   C 1 278 ? -45.655 1.614   31.803  1.00 15.74 ? 257 ILE   C N    1 
ATOM   5763 C  CA   . ILE   C 1 278 ? -46.795 2.498   31.995  1.00 15.97 ? 257 ILE   C CA   1 
ATOM   5764 C  C    . ILE   C 1 278 ? -46.355 3.929   31.711  1.00 15.39 ? 257 ILE   C C    1 
ATOM   5765 O  O    . ILE   C 1 278 ? -45.484 4.459   32.403  1.00 15.77 ? 257 ILE   C O    1 
ATOM   5766 C  CB   . ILE   C 1 278 ? -47.364 2.382   33.420  1.00 17.72 ? 257 ILE   C CB   1 
ATOM   5767 C  CG1  . ILE   C 1 278 ? -47.828 0.959   33.762  1.00 19.32 ? 257 ILE   C CG1  1 
ATOM   5768 C  CG2  . ILE   C 1 278 ? -48.483 3.410   33.633  1.00 19.17 ? 257 ILE   C CG2  1 
ATOM   5769 C  CD1  . ILE   C 1 278 ? -48.391 0.882   35.164  1.00 21.31 ? 257 ILE   C CD1  1 
ATOM   5770 N  N    . LYS   C 1 279 ? -46.927 4.532   30.663  1.00 15.09 ? 258 LYS   C N    1 
ATOM   5771 C  CA   . LYS   C 1 279 ? -46.627 5.932   30.390  1.00 15.41 ? 258 LYS   C CA   1 
ATOM   5772 C  C    . LYS   C 1 279 ? -47.370 6.803   31.387  1.00 15.92 ? 258 LYS   C C    1 
ATOM   5773 O  O    . LYS   C 1 279 ? -48.541 6.557   31.674  1.00 16.38 ? 258 LYS   C O    1 
ATOM   5774 C  CB   . LYS   C 1 279 ? -47.189 6.397   29.040  1.00 19.48 ? 258 LYS   C CB   1 
ATOM   5775 C  CG   . LYS   C 1 279 ? -46.498 6.058   27.753  1.00 24.30 ? 258 LYS   C CG   1 
ATOM   5776 C  CD   . LYS   C 1 279 ? -47.211 6.891   26.682  1.00 20.63 ? 258 LYS   C CD   1 
ATOM   5777 C  CE   . LYS   C 1 279 ? -48.602 6.398   26.357  1.00 22.04 ? 258 LYS   C CE   1 
ATOM   5778 N  NZ   . LYS   C 1 279 ? -49.243 7.049   25.197  1.00 21.92 ? 258 LYS   C NZ   1 
ATOM   5779 N  N    . VAL   C 1 280 ? -46.674 7.826   31.897  1.00 15.15 ? 259 VAL   C N    1 
ATOM   5780 C  CA   . VAL   C 1 280 ? -47.225 8.783   32.842  1.00 14.79 ? 259 VAL   C CA   1 
ATOM   5781 C  C    . VAL   C 1 280 ? -46.884 10.170  32.317  1.00 15.22 ? 259 VAL   C C    1 
ATOM   5782 O  O    . VAL   C 1 280 ? -45.949 10.792  32.812  1.00 16.13 ? 259 VAL   C O    1 
ATOM   5783 C  CB   . VAL   C 1 280 ? -46.732 8.567   34.286  1.00 14.61 ? 259 VAL   C CB   1 
ATOM   5784 C  CG1  . VAL   C 1 280 ? -47.421 9.530   35.243  1.00 17.08 ? 259 VAL   C CG1  1 
ATOM   5785 C  CG2  . VAL   C 1 280 ? -46.973 7.133   34.735  1.00 16.05 ? 259 VAL   C CG2  1 
ATOM   5786 N  N    . ASP   C 1 281 ? -47.589 10.587  31.255  1.00 14.81 ? 260 ASP   C N    1 
ATOM   5787 C  CA   . ASP   C 1 281 ? -47.089 11.694  30.462  1.00 14.60 ? 260 ASP   C CA   1 
ATOM   5788 C  C    . ASP   C 1 281 ? -48.157 12.746  30.146  1.00 14.77 ? 260 ASP   C C    1 
ATOM   5789 O  O    . ASP   C 1 281 ? -47.878 13.662  29.372  1.00 14.85 ? 260 ASP   C O    1 
ATOM   5790 C  CB   . ASP   C 1 281 ? -46.437 11.208  29.177  1.00 15.26 ? 260 ASP   C CB   1 
ATOM   5791 C  CG   . ASP   C 1 281 ? -47.395 10.768  28.075  1.00 16.42 ? 260 ASP   C CG   1 
ATOM   5792 O  OD1  . ASP   C 1 281 ? -48.606 10.580  28.370  1.00 16.31 ? 260 ASP   C OD1  1 
ATOM   5793 O  OD2  . ASP   C 1 281 ? -46.951 10.699  26.915  1.00 16.13 ? 260 ASP   C OD2  1 
ATOM   5794 N  N    . GLY   C 1 282 ? -49.371 12.613  30.692  1.00 14.81 ? 261 GLY   C N    1 
ATOM   5795 C  CA   . GLY   C 1 282 ? -50.344 13.684  30.483  1.00 15.06 ? 261 GLY   C CA   1 
ATOM   5796 C  C    . GLY   C 1 282 ? -50.765 13.844  29.026  1.00 15.72 ? 261 GLY   C C    1 
ATOM   5797 O  O    . GLY   C 1 282 ? -51.333 14.880  28.650  1.00 15.11 ? 261 GLY   C O    1 
ATOM   5798 N  N    . GLY   C 1 283 ? -50.518 12.799  28.223  1.00 15.26 ? 262 GLY   C N    1 
ATOM   5799 C  CA   . GLY   C 1 283 ? -50.836 12.799  26.803  1.00 15.52 ? 262 GLY   C CA   1 
ATOM   5800 C  C    . GLY   C 1 283 ? -49.772 13.443  25.913  1.00 15.13 ? 262 GLY   C C    1 
ATOM   5801 O  O    . GLY   C 1 283 ? -49.985 13.540  24.709  1.00 15.20 ? 262 GLY   C O    1 
ATOM   5802 N  N    . LEU   C 1 284 ? -48.615 13.838  26.477  1.00 14.33 ? 263 LEU   C N    1 
ATOM   5803 C  CA   . LEU   C 1 284 ? -47.590 14.539  25.698  1.00 14.89 ? 263 LEU   C CA   1 
ATOM   5804 C  C    . LEU   C 1 284 ? -47.129 13.759  24.460  1.00 15.06 ? 263 LEU   C C    1 
ATOM   5805 O  O    . LEU   C 1 284 ? -46.958 14.340  23.381  1.00 15.53 ? 263 LEU   C O    1 
ATOM   5806 C  CB   . LEU   C 1 284 ? -46.396 14.859  26.591  1.00 16.08 ? 263 LEU   C CB   1 
ATOM   5807 C  CG   . LEU   C 1 284 ? -45.254 15.583  25.882  1.00 17.12 ? 263 LEU   C CG   1 
ATOM   5808 C  CD1  . LEU   C 1 284 ? -45.723 16.974  25.454  1.00 19.66 ? 263 LEU   C CD1  1 
ATOM   5809 C  CD2  . LEU   C 1 284 ? -44.104 15.694  26.860  1.00 18.56 ? 263 LEU   C CD2  1 
ATOM   5810 N  N    . SER   C 1 285 ? -46.952 12.437  24.596  1.00 15.09 ? 264 SER   C N    1 
ATOM   5811 C  CA   . SER   C 1 285 ? -46.469 11.632  23.484  1.00 15.70 ? 264 SER   C CA   1 
ATOM   5812 C  C    . SER   C 1 285 ? -47.487 11.502  22.352  1.00 16.34 ? 264 SER   C C    1 
ATOM   5813 O  O    . SER   C 1 285 ? -47.126 10.996  21.293  1.00 17.63 ? 264 SER   C O    1 
ATOM   5814 C  CB   . SER   C 1 285 ? -46.026 10.268  23.943  1.00 16.87 ? 264 SER   C CB   1 
ATOM   5815 O  OG   . SER   C 1 285 ? -47.116 9.540   24.493  1.00 18.19 ? 264 SER   C OG   1 
ATOM   5816 N  N    . LEU   C 1 286 ? -48.736 11.919  22.589  1.00 15.79 ? 265 LEU   C N    1 
ATOM   5817 C  CA   . LEU   C 1 286 ? -49.783 11.867  21.571  1.00 16.87 ? 265 LEU   C CA   1 
ATOM   5818 C  C    . LEU   C 1 286 ? -49.780 13.112  20.687  1.00 16.90 ? 265 LEU   C C    1 
ATOM   5819 O  O    . LEU   C 1 286 ? -50.558 13.177  19.733  1.00 18.67 ? 265 LEU   C O    1 
ATOM   5820 C  CB   . LEU   C 1 286 ? -51.160 11.741  22.228  1.00 17.08 ? 265 LEU   C CB   1 
ATOM   5821 C  CG   . LEU   C 1 286 ? -51.345 10.556  23.168  1.00 19.30 ? 265 LEU   C CG   1 
ATOM   5822 C  CD1  . LEU   C 1 286 ? -52.721 10.681  23.824  1.00 20.91 ? 265 LEU   C CD1  1 
ATOM   5823 C  CD2  . LEU   C 1 286 ? -51.113 9.225   22.482  1.00 20.23 ? 265 LEU   C CD2  1 
ATOM   5824 N  N    . VAL   C 1 287 ? -48.999 14.134  21.035  1.00 17.09 ? 266 VAL   C N    1 
ATOM   5825 C  CA   . VAL   C 1 287 ? -49.144 15.425  20.377  1.00 18.69 ? 266 VAL   C CA   1 
ATOM   5826 C  C    . VAL   C 1 287 ? -48.188 15.479  19.188  1.00 18.46 ? 266 VAL   C C    1 
ATOM   5827 O  O    . VAL   C 1 287 ? -46.971 15.365  19.368  1.00 19.38 ? 266 VAL   C O    1 
ATOM   5828 C  CB   . VAL   C 1 287 ? -48.839 16.587  21.341  1.00 17.93 ? 266 VAL   C CB   1 
ATOM   5829 C  CG1  . VAL   C 1 287 ? -48.928 17.955  20.655  1.00 18.99 ? 266 VAL   C CG1  1 
ATOM   5830 C  CG2  . VAL   C 1 287 ? -49.744 16.564  22.567  1.00 18.06 ? 266 VAL   C CG2  1 
ATOM   5831 N  N    . HIS   C 1 288 ? -48.731 15.737  17.992  1.00 19.24 ? 267 HIS   C N    1 
ATOM   5832 C  CA   . HIS   C 1 288 ? -47.888 15.841  16.807  1.00 19.93 ? 267 HIS   C CA   1 
ATOM   5833 C  C    . HIS   C 1 288 ? -47.097 17.153  16.789  1.00 21.82 ? 267 HIS   C C    1 
ATOM   5834 O  O    . HIS   C 1 288 ? -47.399 18.091  17.524  1.00 22.28 ? 267 HIS   C O    1 
ATOM   5835 C  CB   . HIS   C 1 288 ? -48.726 15.632  15.535  1.00 22.43 ? 267 HIS   C CB   1 
ATOM   5836 C  CG   . HIS   C 1 288 ? -49.717 16.720  15.248  1.00 24.32 ? 267 HIS   C CG   1 
ATOM   5837 N  ND1  . HIS   C 1 288 ? -49.380 18.010  14.893  1.00 24.24 ? 267 HIS   C ND1  1 
ATOM   5838 C  CD2  . HIS   C 1 288 ? -51.057 16.690  15.295  1.00 25.88 ? 267 HIS   C CD2  1 
ATOM   5839 C  CE1  . HIS   C 1 288 ? -50.484 18.727  14.730  1.00 25.00 ? 267 HIS   C CE1  1 
ATOM   5840 N  NE2  . HIS   C 1 288 ? -51.519 17.942  14.965  1.00 25.58 ? 267 HIS   C NE2  1 
ATOM   5841 N  N    . ALA   C 1 289 ? -46.104 17.210  15.890  1.00 22.91 ? 268 ALA   C N    1 
ATOM   5842 C  CA   . ALA   C 1 289 ? -45.248 18.368  15.666  1.00 25.34 ? 268 ALA   C CA   1 
ATOM   5843 C  C    . ALA   C 1 289 ? -46.095 19.591  15.312  1.00 28.08 ? 268 ALA   C C    1 
ATOM   5844 O  O    . ALA   C 1 289 ? -45.633 20.709  15.643  1.00 32.57 ? 268 ALA   C O    1 
ATOM   5845 C  CB   . ALA   C 1 289 ? -44.288 18.063  14.536  1.00 26.62 ? 268 ALA   C CB   1 
ATOM   5846 O  OXT  . ALA   C 1 289 ? -47.142 19.392  14.662  1.00 29.07 ? 268 ALA   C OXT  1 
ATOM   5847 N  N    . GLU   D 1 23  ? -71.231 12.774  48.141  0.70 44.92 ? 2   GLU   D N    1 
ATOM   5848 C  CA   . GLU   D 1 23  ? -72.082 11.745  47.484  0.70 42.58 ? 2   GLU   D CA   1 
ATOM   5849 C  C    . GLU   D 1 23  ? -71.230 10.926  46.517  0.70 38.02 ? 2   GLU   D C    1 
ATOM   5850 O  O    . GLU   D 1 23  ? -70.176 11.374  46.070  0.70 38.19 ? 2   GLU   D O    1 
ATOM   5851 C  CB   . GLU   D 1 23  ? -73.267 12.365  46.746  0.70 44.82 ? 2   GLU   D CB   1 
ATOM   5852 C  CG   . GLU   D 1 23  ? -72.845 13.237  45.568  0.70 46.83 ? 2   GLU   D CG   1 
ATOM   5853 C  CD   . GLU   D 1 23  ? -73.781 13.121  44.382  0.70 47.74 ? 2   GLU   D CD   1 
ATOM   5854 O  OE1  . GLU   D 1 23  ? -73.434 13.666  43.317  0.70 49.14 ? 2   GLU   D OE1  1 
ATOM   5855 O  OE2  . GLU   D 1 23  ? -74.850 12.490  44.518  0.70 51.01 ? 2   GLU   D OE2  1 
ATOM   5856 N  N    . ALA   D 1 24  ? -71.715 9.729   46.181  1.00 33.86 ? 3   ALA   D N    1 
ATOM   5857 C  CA   . ALA   D 1 24  ? -70.851 8.746   45.551  1.00 29.11 ? 3   ALA   D CA   1 
ATOM   5858 C  C    . ALA   D 1 24  ? -70.764 8.981   44.043  1.00 28.01 ? 3   ALA   D C    1 
ATOM   5859 O  O    . ALA   D 1 24  ? -71.752 9.299   43.386  1.00 26.64 ? 3   ALA   D O    1 
ATOM   5860 C  CB   . ALA   D 1 24  ? -71.328 7.351   45.879  1.00 27.61 ? 3   ALA   D CB   1 
ATOM   5861 N  N    . PRO   D 1 25  ? -69.573 8.793   43.428  1.00 23.97 ? 4   PRO   D N    1 
ATOM   5862 C  CA   . PRO   D 1 25  ? -69.470 8.891   41.971  1.00 21.68 ? 4   PRO   D CA   1 
ATOM   5863 C  C    . PRO   D 1 25  ? -70.140 7.673   41.347  1.00 20.69 ? 4   PRO   D C    1 
ATOM   5864 O  O    . PRO   D 1 25  ? -70.429 6.694   42.034  1.00 21.13 ? 4   PRO   D O    1 
ATOM   5865 C  CB   . PRO   D 1 25  ? -67.959 8.907   41.751  1.00 23.20 ? 4   PRO   D CB   1 
ATOM   5866 C  CG   . PRO   D 1 25  ? -67.425 8.050   42.881  1.00 23.17 ? 4   PRO   D CG   1 
ATOM   5867 C  CD   . PRO   D 1 25  ? -68.328 8.346   44.082  1.00 23.95 ? 4   PRO   D CD   1 
ATOM   5868 N  N    . ALA   D 1 26  ? -70.407 7.749   40.040  1.00 18.57 ? 5   ALA   D N    1 
ATOM   5869 C  CA   . ALA   D 1 26  ? -71.095 6.661   39.364  1.00 19.70 ? 5   ALA   D CA   1 
ATOM   5870 C  C    . ALA   D 1 26  ? -70.294 6.208   38.145  1.00 18.46 ? 5   ALA   D C    1 
ATOM   5871 O  O    . ALA   D 1 26  ? -69.598 7.020   37.520  1.00 18.63 ? 5   ALA   D O    1 
ATOM   5872 C  CB   . ALA   D 1 26  ? -72.499 7.091   38.976  1.00 19.43 ? 5   ALA   D CB   1 
ATOM   5873 N  N    . ALA   D 1 27  ? -70.386 4.899   37.855  1.00 17.78 ? 6   ALA   D N    1 
ATOM   5874 C  CA   . ALA   D 1 27  ? -69.684 4.308   36.718  1.00 18.20 ? 6   ALA   D CA   1 
ATOM   5875 C  C    . ALA   D 1 27  ? -70.643 3.510   35.834  1.00 18.08 ? 6   ALA   D C    1 
ATOM   5876 O  O    . ALA   D 1 27  ? -71.549 2.848   36.334  1.00 20.24 ? 6   ALA   D O    1 
ATOM   5877 C  CB   . ALA   D 1 27  ? -68.582 3.407   37.216  1.00 18.15 ? 6   ALA   D CB   1 
ATOM   5878 N  N    . VAL   D 1 28  ? -70.413 3.522   34.515  1.00 16.53 ? 7   VAL   D N    1 
ATOM   5879 C  CA   . VAL   D 1 28  ? -71.059 2.597   33.587  1.00 15.56 ? 7   VAL   D CA   1 
ATOM   5880 C  C    . VAL   D 1 28  ? -70.036 1.540   33.217  1.00 15.43 ? 7   VAL   D C    1 
ATOM   5881 O  O    . VAL   D 1 28  ? -68.922 1.886   32.809  1.00 16.74 ? 7   VAL   D O    1 
ATOM   5882 C  CB   . VAL   D 1 28  ? -71.507 3.336   32.311  1.00 17.24 ? 7   VAL   D CB   1 
ATOM   5883 C  CG1  . VAL   D 1 28  ? -71.884 2.368   31.191  1.00 17.28 ? 7   VAL   D CG1  1 
ATOM   5884 C  CG2  . VAL   D 1 28  ? -72.659 4.284   32.591  1.00 17.45 ? 7   VAL   D CG2  1 
ATOM   5885 N  N    . VAL   D 1 29  ? -70.420 0.273   33.360  1.00 15.19 ? 8   VAL   D N    1 
ATOM   5886 C  CA   . VAL   D 1 29  ? -69.581 -0.815  32.878  1.00 16.18 ? 8   VAL   D CA   1 
ATOM   5887 C  C    . VAL   D 1 29  ? -70.364 -1.575  31.811  1.00 16.60 ? 8   VAL   D C    1 
ATOM   5888 O  O    . VAL   D 1 29  ? -71.448 -2.106  32.077  1.00 15.78 ? 8   VAL   D O    1 
ATOM   5889 C  CB   . VAL   D 1 29  ? -69.119 -1.758  34.002  1.00 16.22 ? 8   VAL   D CB   1 
ATOM   5890 C  CG1  . VAL   D 1 29  ? -68.205 -2.865  33.475  1.00 17.99 ? 8   VAL   D CG1  1 
ATOM   5891 C  CG2  . VAL   D 1 29  ? -68.411 -0.954  35.087  1.00 16.75 ? 8   VAL   D CG2  1 
ATOM   5892 N  N    . THR   D 1 30  ? -69.818 -1.634  30.591  1.00 15.09 ? 9   THR   D N    1 
ATOM   5893 C  CA   . THR   D 1 30  ? -70.524 -2.380  29.557  1.00 15.73 ? 9   THR   D CA   1 
ATOM   5894 C  C    . THR   D 1 30  ? -70.223 -3.862  29.678  1.00 16.96 ? 9   THR   D C    1 
ATOM   5895 O  O    . THR   D 1 30  ? -69.143 -4.239  30.102  1.00 16.91 ? 9   THR   D O    1 
ATOM   5896 C  CB   . THR   D 1 30  ? -70.340 -1.848  28.141  1.00 14.49 ? 9   THR   D CB   1 
ATOM   5897 O  OG1  . THR   D 1 30  ? -68.965 -1.996  27.796  1.00 14.54 ? 9   THR   D OG1  1 
ATOM   5898 C  CG2  . THR   D 1 30  ? -70.716 -0.379  28.037  1.00 15.87 ? 9   THR   D CG2  1 
ATOM   5899 N  N    . GLY   D 1 31  ? -71.202 -4.697  29.320  1.00 16.44 ? 10  GLY   D N    1 
ATOM   5900 C  CA   . GLY   D 1 31  ? -71.020 -6.138  29.405  1.00 17.52 ? 10  GLY   D CA   1 
ATOM   5901 C  C    . GLY   D 1 31  ? -70.651 -6.588  30.823  1.00 18.52 ? 10  GLY   D C    1 
ATOM   5902 O  O    . GLY   D 1 31  ? -69.730 -7.382  31.011  1.00 18.03 ? 10  GLY   D O    1 
ATOM   5903 N  N    . ALA   D 1 32  ? -71.406 -6.108  31.824  1.00 17.55 ? 11  ALA   D N    1 
ATOM   5904 C  CA   . ALA   D 1 32  ? -70.982 -6.210  33.213  1.00 16.94 ? 11  ALA   D CA   1 
ATOM   5905 C  C    . ALA   D 1 32  ? -71.628 -7.386  33.949  1.00 18.60 ? 11  ALA   D C    1 
ATOM   5906 O  O    . ALA   D 1 32  ? -71.364 -7.536  35.134  1.00 19.00 ? 11  ALA   D O    1 
ATOM   5907 C  CB   . ALA   D 1 32  ? -71.268 -4.905  33.936  1.00 17.92 ? 11  ALA   D CB   1 
ATOM   5908 N  N    . ALA   D 1 33  ? -72.420 -8.220  33.264  1.00 18.24 ? 12  ALA   D N    1 
ATOM   5909 C  CA   . ALA   D 1 33  ? -73.199 -9.218  33.986  1.00 20.01 ? 12  ALA   D CA   1 
ATOM   5910 C  C    . ALA   D 1 33  ? -72.334 -10.407 34.375  1.00 21.54 ? 12  ALA   D C    1 
ATOM   5911 O  O    . ALA   D 1 33  ? -72.641 -11.077 35.360  1.00 22.48 ? 12  ALA   D O    1 
ATOM   5912 C  CB   . ALA   D 1 33  ? -74.388 -9.673  33.188  1.00 20.63 ? 12  ALA   D CB   1 
ATOM   5913 N  N    . LYS   D 1 34  ? -71.255 -10.643 33.622  1.00 21.45 ? 13  LYS   D N    1 
ATOM   5914 C  CA   . LYS   D 1 34  ? -70.448 -11.831 33.851  1.00 21.61 ? 13  LYS   D CA   1 
ATOM   5915 C  C    . LYS   D 1 34  ? -68.960 -11.518 33.704  1.00 22.59 ? 13  LYS   D C    1 
ATOM   5916 O  O    . LYS   D 1 34  ? -68.586 -10.455 33.215  1.00 20.89 ? 13  LYS   D O    1 
ATOM   5917 C  CB   . LYS   D 1 34  ? -70.798 -12.872 32.780  1.00 23.70 ? 13  LYS   D CB   1 
ATOM   5918 C  CG   . LYS   D 1 34  ? -72.247 -13.371 32.792  1.00 27.86 ? 13  LYS   D CG   1 
ATOM   5919 C  CD   . LYS   D 1 34  ? -72.513 -14.344 31.651  1.00 31.19 ? 13  LYS   D CD   1 
ATOM   5920 C  CE   . LYS   D 1 34  ? -73.901 -14.902 31.718  0.70 33.10 ? 13  LYS   D CE   1 
ATOM   5921 N  NZ   . LYS   D 1 34  ? -74.147 -15.876 30.652  0.70 37.01 ? 13  LYS   D NZ   1 
ATOM   5922 N  N    . ARG   D 1 35  ? -68.131 -12.459 34.161  1.00 20.80 ? 14  ARG   D N    1 
ATOM   5923 C  CA   . ARG   D 1 35  ? -66.731 -12.532 33.765  1.00 20.33 ? 14  ARG   D CA   1 
ATOM   5924 C  C    . ARG   D 1 35  ? -66.008 -11.241 34.173  1.00 19.89 ? 14  ARG   D C    1 
ATOM   5925 O  O    . ARG   D 1 35  ? -66.123 -10.775 35.313  1.00 20.76 ? 14  ARG   D O    1 
ATOM   5926 C  CB   . ARG   D 1 35  ? -66.660 -13.013 32.306  1.00 20.27 ? 14  ARG   D CB   1 
ATOM   5927 C  CG   . ARG   D 1 35  ? -67.106 -14.467 32.153  1.00 20.03 ? 14  ARG   D CG   1 
ATOM   5928 C  CD   . ARG   D 1 35  ? -67.349 -14.860 30.706  1.00 20.52 ? 14  ARG   D CD   1 
ATOM   5929 N  NE   . ARG   D 1 35  ? -66.171 -14.663 29.851  1.00 21.45 ? 14  ARG   D NE   1 
ATOM   5930 C  CZ   . ARG   D 1 35  ? -65.165 -15.524 29.689  1.00 22.05 ? 14  ARG   D CZ   1 
ATOM   5931 N  NH1  . ARG   D 1 35  ? -65.155 -16.694 30.315  1.00 22.60 ? 14  ARG   D NH1  1 
ATOM   5932 N  NH2  . ARG   D 1 35  ? -64.169 -15.213 28.871  1.00 21.28 ? 14  ARG   D NH2  1 
ATOM   5933 N  N    . ILE   D 1 36  ? -65.208 -10.682 33.255  1.00 18.64 ? 15  ILE   D N    1 
ATOM   5934 C  CA   . ILE   D 1 36  ? -64.345 -9.578  33.628  1.00 18.31 ? 15  ILE   D CA   1 
ATOM   5935 C  C    . ILE   D 1 36  ? -65.163 -8.327  33.956  1.00 16.60 ? 15  ILE   D C    1 
ATOM   5936 O  O    . ILE   D 1 36  ? -64.843 -7.623  34.916  1.00 17.35 ? 15  ILE   D O    1 
ATOM   5937 C  CB   . ILE   D 1 36  ? -63.284 -9.341  32.537  1.00 17.58 ? 15  ILE   D CB   1 
ATOM   5938 C  CG1  . ILE   D 1 36  ? -62.277 -10.510 32.523  1.00 19.73 ? 15  ILE   D CG1  1 
ATOM   5939 C  CG2  . ILE   D 1 36  ? -62.594 -7.981  32.739  1.00 17.40 ? 15  ILE   D CG2  1 
ATOM   5940 C  CD1  . ILE   D 1 36  ? -61.400 -10.562 31.283  1.00 19.90 ? 15  ILE   D CD1  1 
ATOM   5941 N  N    . GLY   D 1 37  ? -66.218 -8.061  33.176  1.00 17.00 ? 16  GLY   D N    1 
ATOM   5942 C  CA   . GLY   D 1 37  ? -66.996 -6.861  33.429  1.00 16.97 ? 16  GLY   D CA   1 
ATOM   5943 C  C    . GLY   D 1 37  ? -67.678 -6.912  34.796  1.00 17.12 ? 16  GLY   D C    1 
ATOM   5944 O  O    . GLY   D 1 37  ? -67.774 -5.891  35.472  1.00 17.17 ? 16  GLY   D O    1 
ATOM   5945 N  N    . ARG   D 1 38  ? -68.085 -8.117  35.209  1.00 16.83 ? 17  ARG   D N    1 
ATOM   5946 C  CA   . ARG   D 1 38  ? -68.675 -8.282  36.529  1.00 17.90 ? 17  ARG   D CA   1 
ATOM   5947 C  C    . ARG   D 1 38  ? -67.643 -7.958  37.609  1.00 17.59 ? 17  ARG   D C    1 
ATOM   5948 O  O    . ARG   D 1 38  ? -67.954 -7.230  38.543  1.00 19.34 ? 17  ARG   D O    1 
ATOM   5949 C  CB   . ARG   D 1 38  ? -69.242 -9.699  36.684  1.00 18.86 ? 17  ARG   D CB   1 
ATOM   5950 C  CG   . ARG   D 1 38  ? -69.870 -9.895  38.057  1.00 22.31 ? 17  ARG   D CG   1 
ATOM   5951 C  CD   . ARG   D 1 38  ? -70.356 -11.341 38.183  1.00 25.29 ? 17  ARG   D CD   1 
ATOM   5952 N  NE   A ARG   D 1 38  ? -71.474 -11.455 39.125  0.50 25.54 ? 17  ARG   D NE   1 
ATOM   5953 C  CZ   A ARG   D 1 38  ? -71.390 -11.250 40.432  0.50 27.56 ? 17  ARG   D CZ   1 
ATOM   5954 N  NH1  A ARG   D 1 38  ? -70.221 -10.985 40.995  0.50 28.44 ? 17  ARG   D NH1  1 
ATOM   5955 N  NH2  A ARG   D 1 38  ? -72.482 -11.324 41.172  0.50 27.36 ? 17  ARG   D NH2  1 
ATOM   5956 N  N    . ALA   D 1 39  ? -66.409 -8.483  37.480  1.00 17.68 ? 18  ALA   D N    1 
ATOM   5957 C  CA   . ALA   D 1 39  ? -65.357 -8.214  38.448  1.00 17.09 ? 18  ALA   D CA   1 
ATOM   5958 C  C    . ALA   D 1 39  ? -65.055 -6.718  38.524  1.00 16.00 ? 18  ALA   D C    1 
ATOM   5959 O  O    . ALA   D 1 39  ? -64.741 -6.198  39.591  1.00 18.19 ? 18  ALA   D O    1 
ATOM   5960 C  CB   . ALA   D 1 39  ? -64.109 -9.005  38.085  1.00 17.54 ? 18  ALA   D CB   1 
ATOM   5961 N  N    . ILE   D 1 40  ? -65.095 -6.049  37.369  1.00 15.97 ? 19  ILE   D N    1 
ATOM   5962 C  CA   . ILE   D 1 40  ? -64.839 -4.619  37.324  1.00 15.05 ? 19  ILE   D CA   1 
ATOM   5963 C  C    . ILE   D 1 40  ? -65.948 -3.868  38.066  1.00 16.42 ? 19  ILE   D C    1 
ATOM   5964 O  O    . ILE   D 1 40  ? -65.666 -2.982  38.867  1.00 17.29 ? 19  ILE   D O    1 
ATOM   5965 C  CB   . ILE   D 1 40  ? -64.676 -4.159  35.869  1.00 15.02 ? 19  ILE   D CB   1 
ATOM   5966 C  CG1  . ILE   D 1 40  ? -63.370 -4.690  35.274  1.00 15.39 ? 19  ILE   D CG1  1 
ATOM   5967 C  CG2  . ILE   D 1 40  ? -64.719 -2.630  35.794  1.00 16.24 ? 19  ILE   D CG2  1 
ATOM   5968 C  CD1  . ILE   D 1 40  ? -63.249 -4.450  33.776  1.00 15.57 ? 19  ILE   D CD1  1 
ATOM   5969 N  N    . ALA   D 1 41  ? -67.210 -4.212  37.779  1.00 17.39 ? 20  ALA   D N    1 
ATOM   5970 C  CA   . ALA   D 1 41  ? -68.333 -3.554  38.447  1.00 18.06 ? 20  ALA   D CA   1 
ATOM   5971 C  C    . ALA   D 1 41  ? -68.273 -3.752  39.972  1.00 18.07 ? 20  ALA   D C    1 
ATOM   5972 O  O    . ALA   D 1 41  ? -68.453 -2.807  40.734  1.00 18.25 ? 20  ALA   D O    1 
ATOM   5973 C  CB   . ALA   D 1 41  ? -69.647 -4.027  37.856  1.00 18.22 ? 20  ALA   D CB   1 
ATOM   5974 N  N    . VAL   D 1 42  ? -67.982 -4.977  40.403  1.00 17.93 ? 21  VAL   D N    1 
ATOM   5975 C  CA   . VAL   D 1 42  ? -67.859 -5.286  41.821  1.00 18.81 ? 21  VAL   D CA   1 
ATOM   5976 C  C    . VAL   D 1 42  ? -66.760 -4.435  42.460  1.00 18.72 ? 21  VAL   D C    1 
ATOM   5977 O  O    . VAL   D 1 42  ? -66.965 -3.818  43.499  1.00 19.39 ? 21  VAL   D O    1 
ATOM   5978 C  CB   . VAL   D 1 42  ? -67.612 -6.787  42.040  1.00 19.72 ? 21  VAL   D CB   1 
ATOM   5979 C  CG1  . VAL   D 1 42  ? -67.181 -7.078  43.477  1.00 20.99 ? 21  VAL   D CG1  1 
ATOM   5980 C  CG2  . VAL   D 1 42  ? -68.823 -7.615  41.650  1.00 20.78 ? 21  VAL   D CG2  1 
ATOM   5981 N  N    . LYS   D 1 43  ? -65.571 -4.401  41.847  1.00 18.61 ? 22  LYS   D N    1 
ATOM   5982 C  CA   A LYS   D 1 43  ? -64.459 -3.694  42.451  0.70 19.15 ? 22  LYS   D CA   1 
ATOM   5983 C  CA   B LYS   D 1 43  ? -64.449 -3.689  42.432  0.30 18.33 ? 22  LYS   D CA   1 
ATOM   5984 C  C    . LYS   D 1 43  ? -64.743 -2.195  42.493  1.00 17.94 ? 22  LYS   D C    1 
ATOM   5985 O  O    . LYS   D 1 43  ? -64.395 -1.540  43.471  1.00 19.57 ? 22  LYS   D O    1 
ATOM   5986 C  CB   A LYS   D 1 43  ? -63.145 -4.072  41.750  0.70 21.63 ? 22  LYS   D CB   1 
ATOM   5987 C  CB   B LYS   D 1 43  ? -63.142 -4.005  41.697  0.30 18.40 ? 22  LYS   D CB   1 
ATOM   5988 C  CG   A LYS   D 1 43  ? -61.919 -3.908  42.640  0.70 25.01 ? 22  LYS   D CG   1 
ATOM   5989 C  CG   B LYS   D 1 43  ? -62.563 -5.360  42.065  0.30 18.26 ? 22  LYS   D CG   1 
ATOM   5990 C  CD   A LYS   D 1 43  ? -60.634 -4.541  42.118  0.70 25.50 ? 22  LYS   D CD   1 
ATOM   5991 C  CD   B LYS   D 1 43  ? -61.079 -5.418  41.726  0.30 19.85 ? 22  LYS   D CD   1 
ATOM   5992 C  CE   A LYS   D 1 43  ? -60.622 -6.029  42.277  0.70 27.02 ? 22  LYS   D CE   1 
ATOM   5993 C  CE   B LYS   D 1 43  ? -60.367 -6.635  42.213  0.30 20.22 ? 22  LYS   D CE   1 
ATOM   5994 N  NZ   A LYS   D 1 43  ? -60.467 -6.477  43.666  0.70 29.70 ? 22  LYS   D NZ   1 
ATOM   5995 N  NZ   B LYS   D 1 43  ? -59.689 -6.395  43.491  0.30 19.66 ? 22  LYS   D NZ   1 
ATOM   5996 N  N    . LEU   D 1 44  ? -65.374 -1.659  41.432  1.00 18.89 ? 23  LEU   D N    1 
ATOM   5997 C  CA   . LEU   D 1 44  ? -65.772 -0.259  41.437  1.00 18.47 ? 23  LEU   D CA   1 
ATOM   5998 C  C    . LEU   D 1 44  ? -66.738 -0.002  42.593  1.00 19.48 ? 23  LEU   D C    1 
ATOM   5999 O  O    . LEU   D 1 44  ? -66.599 0.990   43.304  1.00 20.16 ? 23  LEU   D O    1 
ATOM   6000 C  CB   . LEU   D 1 44  ? -66.379 0.188   40.105  1.00 18.08 ? 23  LEU   D CB   1 
ATOM   6001 C  CG   . LEU   D 1 44  ? -65.358 0.380   38.980  1.00 17.27 ? 23  LEU   D CG   1 
ATOM   6002 C  CD1  . LEU   D 1 44  ? -66.099 0.521   37.685  1.00 19.73 ? 23  LEU   D CD1  1 
ATOM   6003 C  CD2  . LEU   D 1 44  ? -64.492 1.616   39.215  1.00 19.60 ? 23  LEU   D CD2  1 
ATOM   6004 N  N    . HIS   D 1 45  ? -67.717 -0.891  42.755  1.00 20.02 ? 24  HIS   D N    1 
ATOM   6005 C  CA   . HIS   D 1 45  ? -68.711 -0.730  43.813  1.00 19.55 ? 24  HIS   D CA   1 
ATOM   6006 C  C    . HIS   D 1 45  ? -68.031 -0.766  45.184  1.00 20.24 ? 24  HIS   D C    1 
ATOM   6007 O  O    . HIS   D 1 45  ? -68.329 0.051   46.061  1.00 21.98 ? 24  HIS   D O    1 
ATOM   6008 C  CB   . HIS   D 1 45  ? -69.781 -1.815  43.670  1.00 18.93 ? 24  HIS   D CB   1 
ATOM   6009 C  CG   . HIS   D 1 45  ? -70.958 -1.618  44.566  1.00 21.19 ? 24  HIS   D CG   1 
ATOM   6010 N  ND1  . HIS   D 1 45  ? -71.088 -2.248  45.782  1.00 24.30 ? 24  HIS   D ND1  1 
ATOM   6011 C  CD2  . HIS   D 1 45  ? -72.038 -0.862  44.410  1.00 22.11 ? 24  HIS   D CD2  1 
ATOM   6012 C  CE1  . HIS   D 1 45  ? -72.247 -1.879  46.329  1.00 23.01 ? 24  HIS   D CE1  1 
ATOM   6013 N  NE2  . HIS   D 1 45  ? -72.839 -1.032  45.529  1.00 22.51 ? 24  HIS   D NE2  1 
ATOM   6014 N  N    . GLN   D 1 46  ? -67.070 -1.686  45.335  1.00 20.93 ? 25  GLN   D N    1 
ATOM   6015 C  CA   . GLN   D 1 46  ? -66.332 -1.837  46.586  1.00 21.45 ? 25  GLN   D CA   1 
ATOM   6016 C  C    . GLN   D 1 46  ? -65.497 -0.590  46.881  1.00 24.74 ? 25  GLN   D C    1 
ATOM   6017 O  O    . GLN   D 1 46  ? -65.228 -0.288  48.043  1.00 26.53 ? 25  GLN   D O    1 
ATOM   6018 C  CB   . GLN   D 1 46  ? -65.470 -3.096  46.555  1.00 22.07 ? 25  GLN   D CB   1 
ATOM   6019 C  CG   . GLN   D 1 46  ? -66.267 -4.392  46.586  1.00 24.43 ? 25  GLN   D CG   1 
ATOM   6020 C  CD   . GLN   D 1 46  ? -65.418 -5.613  46.348  1.00 26.58 ? 25  GLN   D CD   1 
ATOM   6021 O  OE1  . GLN   D 1 46  ? -64.321 -5.543  45.783  1.00 28.36 ? 25  GLN   D OE1  1 
ATOM   6022 N  NE2  . GLN   D 1 46  ? -65.961 -6.761  46.723  1.00 29.46 ? 25  GLN   D NE2  1 
ATOM   6023 N  N    . THR   D 1 47  ? -65.126 0.157   45.829  1.00 23.43 ? 26  THR   D N    1 
ATOM   6024 C  CA   . THR   D 1 47  ? -64.332 1.370   45.940  1.00 23.99 ? 26  THR   D CA   1 
ATOM   6025 C  C    . THR   D 1 47  ? -65.242 2.555   46.276  1.00 24.90 ? 26  THR   D C    1 
ATOM   6026 O  O    . THR   D 1 47  ? -64.749 3.635   46.589  1.00 27.26 ? 26  THR   D O    1 
ATOM   6027 C  CB   . THR   D 1 47  ? -63.558 1.573   44.632  1.00 25.75 ? 26  THR   D CB   1 
ATOM   6028 O  OG1  . THR   D 1 47  ? -62.701 0.450   44.451  1.00 27.03 ? 26  THR   D OG1  1 
ATOM   6029 C  CG2  . THR   D 1 47  ? -62.674 2.807   44.609  1.00 27.52 ? 26  THR   D CG2  1 
ATOM   6030 N  N    . GLY   D 1 48  ? -66.570 2.354   46.206  1.00 23.77 ? 27  GLY   D N    1 
ATOM   6031 C  CA   . GLY   D 1 48  ? -67.530 3.378   46.602  1.00 24.21 ? 27  GLY   D CA   1 
ATOM   6032 C  C    . GLY   D 1 48  ? -68.359 3.948   45.448  1.00 25.11 ? 27  GLY   D C    1 
ATOM   6033 O  O    . GLY   D 1 48  ? -69.102 4.919   45.624  1.00 24.04 ? 27  GLY   D O    1 
ATOM   6034 N  N    . TYR   D 1 49  ? -68.243 3.348   44.259  1.00 22.25 ? 28  TYR   D N    1 
ATOM   6035 C  CA   . TYR   D 1 49  ? -68.989 3.847   43.112  1.00 21.71 ? 28  TYR   D CA   1 
ATOM   6036 C  C    . TYR   D 1 49  ? -70.387 3.241   43.084  1.00 19.99 ? 28  TYR   D C    1 
ATOM   6037 O  O    . TYR   D 1 49  ? -70.570 2.073   43.423  1.00 21.50 ? 28  TYR   D O    1 
ATOM   6038 C  CB   . TYR   D 1 49  ? -68.353 3.430   41.778  1.00 21.08 ? 28  TYR   D CB   1 
ATOM   6039 C  CG   . TYR   D 1 49  ? -67.123 4.248   41.410  1.00 20.85 ? 28  TYR   D CG   1 
ATOM   6040 C  CD1  . TYR   D 1 49  ? -65.869 3.948   41.946  1.00 20.64 ? 28  TYR   D CD1  1 
ATOM   6041 C  CD2  . TYR   D 1 49  ? -67.226 5.321   40.533  1.00 19.91 ? 28  TYR   D CD2  1 
ATOM   6042 C  CE1  . TYR   D 1 49  ? -64.752 4.699   41.604  1.00 20.13 ? 28  TYR   D CE1  1 
ATOM   6043 C  CE2  . TYR   D 1 49  ? -66.117 6.081   40.192  1.00 21.48 ? 28  TYR   D CE2  1 
ATOM   6044 C  CZ   . TYR   D 1 49  ? -64.880 5.772   40.739  1.00 21.60 ? 28  TYR   D CZ   1 
ATOM   6045 O  OH   . TYR   D 1 49  ? -63.778 6.524   40.415  1.00 24.65 ? 28  TYR   D OH   1 
ATOM   6046 N  N    . ARG   D 1 50  ? -71.331 4.041   42.590  1.00 18.73 ? 29  ARG   D N    1 
ATOM   6047 C  CA   . ARG   D 1 50  ? -72.616 3.539   42.115  1.00 20.28 ? 29  ARG   D CA   1 
ATOM   6048 C  C    . ARG   D 1 50  ? -72.437 3.078   40.670  1.00 20.17 ? 29  ARG   D C    1 
ATOM   6049 O  O    . ARG   D 1 50  ? -71.624 3.654   39.953  1.00 20.77 ? 29  ARG   D O    1 
ATOM   6050 C  CB   . ARG   D 1 50  ? -73.663 4.650   42.191  1.00 22.28 ? 29  ARG   D CB   1 
ATOM   6051 C  CG   . ARG   D 1 50  ? -73.911 4.944   43.664  1.00 24.61 ? 29  ARG   D CG   1 
ATOM   6052 C  CD   . ARG   D 1 50  ? -74.927 6.070   43.803  1.00 25.90 ? 29  ARG   D CD   1 
ATOM   6053 N  NE   . ARG   D 1 50  ? -74.404 7.367   43.361  1.00 26.75 ? 29  ARG   D NE   1 
ATOM   6054 C  CZ   . ARG   D 1 50  ? -75.136 8.469   43.240  1.00 28.08 ? 29  ARG   D CZ   1 
ATOM   6055 N  NH1  . ARG   D 1 50  ? -76.453 8.414   43.422  1.00 28.44 ? 29  ARG   D NH1  1 
ATOM   6056 N  NH2  . ARG   D 1 50  ? -74.551 9.616   42.937  1.00 26.42 ? 29  ARG   D NH2  1 
ATOM   6057 N  N    . VAL   D 1 51  ? -73.122 1.993   40.282  1.00 20.58 ? 30  VAL   D N    1 
ATOM   6058 C  CA   . VAL   D 1 51  ? -72.800 1.336   39.021  1.00 20.12 ? 30  VAL   D CA   1 
ATOM   6059 C  C    . VAL   D 1 51  ? -74.040 1.091   38.167  1.00 21.15 ? 30  VAL   D C    1 
ATOM   6060 O  O    . VAL   D 1 51  ? -75.091 0.683   38.664  1.00 20.21 ? 30  VAL   D O    1 
ATOM   6061 C  CB   . VAL   D 1 51  ? -71.995 0.036   39.217  1.00 20.74 ? 30  VAL   D CB   1 
ATOM   6062 C  CG1  . VAL   D 1 51  ? -70.627 0.320   39.827  1.00 20.78 ? 30  VAL   D CG1  1 
ATOM   6063 C  CG2  . VAL   D 1 51  ? -72.733 -1.006  40.047  1.00 24.14 ? 30  VAL   D CG2  1 
ATOM   6064 N  N    . VAL   D 1 52  ? -73.874 1.305   36.857  1.00 18.93 ? 31  VAL   D N    1 
ATOM   6065 C  CA   . VAL   D 1 52  ? -74.771 0.813   35.819  1.00 17.96 ? 31  VAL   D CA   1 
ATOM   6066 C  C    . VAL   D 1 52  ? -74.181 -0.464  35.230  1.00 19.42 ? 31  VAL   D C    1 
ATOM   6067 O  O    . VAL   D 1 52  ? -73.060 -0.454  34.707  1.00 19.81 ? 31  VAL   D O    1 
ATOM   6068 C  CB   . VAL   D 1 52  ? -75.056 1.817   34.690  1.00 17.25 ? 31  VAL   D CB   1 
ATOM   6069 C  CG1  . VAL   D 1 52  ? -75.968 1.219   33.619  1.00 19.27 ? 31  VAL   D CG1  1 
ATOM   6070 C  CG2  . VAL   D 1 52  ? -75.635 3.125   35.220  1.00 18.88 ? 31  VAL   D CG2  1 
ATOM   6071 N  N    . ILE   D 1 53  ? -74.933 -1.562  35.365  1.00 18.13 ? 32  ILE   D N    1 
ATOM   6072 C  CA   . ILE   D 1 53  ? -74.555 -2.863  34.854  1.00 18.48 ? 32  ILE   D CA   1 
ATOM   6073 C  C    . ILE   D 1 53  ? -75.238 -2.989  33.502  1.00 19.44 ? 32  ILE   D C    1 
ATOM   6074 O  O    . ILE   D 1 53  ? -76.426 -3.294  33.423  1.00 19.36 ? 32  ILE   D O    1 
ATOM   6075 C  CB   . ILE   D 1 53  ? -75.019 -3.952  35.838  1.00 19.51 ? 32  ILE   D CB   1 
ATOM   6076 C  CG1  . ILE   D 1 53  ? -74.408 -3.708  37.217  1.00 20.62 ? 32  ILE   D CG1  1 
ATOM   6077 C  CG2  . ILE   D 1 53  ? -74.742 -5.379  35.346  1.00 19.42 ? 32  ILE   D CG2  1 
ATOM   6078 C  CD1  . ILE   D 1 53  ? -75.163 -4.373  38.358  1.00 24.69 ? 32  ILE   D CD1  1 
ATOM   6079 N  N    . HIS   D 1 54  ? -74.503 -2.691  32.437  1.00 16.57 ? 33  HIS   D N    1 
ATOM   6080 C  CA   . HIS   D 1 54  ? -75.022 -2.899  31.104  1.00 16.20 ? 33  HIS   D CA   1 
ATOM   6081 C  C    . HIS   D 1 54  ? -74.966 -4.392  30.763  1.00 17.26 ? 33  HIS   D C    1 
ATOM   6082 O  O    . HIS   D 1 54  ? -74.009 -5.095  31.104  1.00 17.96 ? 33  HIS   D O    1 
ATOM   6083 C  CB   . HIS   D 1 54  ? -74.277 -2.010  30.095  1.00 16.92 ? 33  HIS   D CB   1 
ATOM   6084 C  CG   . HIS   D 1 54  ? -74.468 -2.563  28.725  1.00 16.28 ? 33  HIS   D CG   1 
ATOM   6085 N  ND1  . HIS   D 1 54  ? -73.592 -3.488  28.196  1.00 17.13 ? 33  HIS   D ND1  1 
ATOM   6086 C  CD2  . HIS   D 1 54  ? -75.478 -2.438  27.836  1.00 17.49 ? 33  HIS   D CD2  1 
ATOM   6087 C  CE1  . HIS   D 1 54  ? -74.065 -3.901  27.017  1.00 17.91 ? 33  HIS   D CE1  1 
ATOM   6088 N  NE2  . HIS   D 1 54  ? -75.198 -3.258  26.775  1.00 17.16 ? 33  HIS   D NE2  1 
ATOM   6089 N  N    . TYR   D 1 55  ? -75.989 -4.863  30.041  1.00 17.06 ? 34  TYR   D N    1 
ATOM   6090 C  CA   . TYR   D 1 55  ? -75.963 -6.220  29.522  1.00 16.95 ? 34  TYR   D CA   1 
ATOM   6091 C  C    . TYR   D 1 55  ? -76.717 -6.255  28.195  1.00 17.57 ? 34  TYR   D C    1 
ATOM   6092 O  O    . TYR   D 1 55  ? -77.430 -5.314  27.831  1.00 17.80 ? 34  TYR   D O    1 
ATOM   6093 C  CB   . TYR   D 1 55  ? -76.585 -7.201  30.528  1.00 19.14 ? 34  TYR   D CB   1 
ATOM   6094 C  CG   . TYR   D 1 55  ? -78.091 -6.998  30.661  1.00 20.49 ? 34  TYR   D CG   1 
ATOM   6095 C  CD1  . TYR   D 1 55  ? -78.607 -5.979  31.456  1.00 21.04 ? 34  TYR   D CD1  1 
ATOM   6096 C  CD2  . TYR   D 1 55  ? -78.984 -7.782  29.931  1.00 21.63 ? 34  TYR   D CD2  1 
ATOM   6097 C  CE1  . TYR   D 1 55  ? -79.976 -5.761  31.561  1.00 22.05 ? 34  TYR   D CE1  1 
ATOM   6098 C  CE2  . TYR   D 1 55  ? -80.353 -7.571  30.020  1.00 22.31 ? 34  TYR   D CE2  1 
ATOM   6099 C  CZ   . TYR   D 1 55  ? -80.844 -6.561  30.835  1.00 24.34 ? 34  TYR   D CZ   1 
ATOM   6100 O  OH   . TYR   D 1 55  ? -82.196 -6.355  30.921  1.00 27.21 ? 34  TYR   D OH   1 
ATOM   6101 N  N    . HIS   D 1 56  ? -76.558 -7.375  27.488  1.00 17.70 ? 35  HIS   D N    1 
ATOM   6102 C  CA   . HIS   D 1 56  ? -77.284 -7.544  26.243  1.00 20.61 ? 35  HIS   D CA   1 
ATOM   6103 C  C    . HIS   D 1 56  ? -78.237 -8.728  26.383  1.00 21.56 ? 35  HIS   D C    1 
ATOM   6104 O  O    . HIS   D 1 56  ? -79.449 -8.529  26.418  1.00 24.21 ? 35  HIS   D O    1 
ATOM   6105 C  CB   . HIS   D 1 56  ? -76.313 -7.693  25.070  1.00 20.79 ? 35  HIS   D CB   1 
ATOM   6106 C  CG   . HIS   D 1 56  ? -76.995 -7.965  23.777  1.00 23.64 ? 35  HIS   D CG   1 
ATOM   6107 N  ND1  . HIS   D 1 56  ? -76.401 -8.850  22.910  1.00 23.00 ? 35  HIS   D ND1  1 
ATOM   6108 C  CD2  . HIS   D 1 56  ? -78.135 -7.569  23.200  1.00 23.04 ? 35  HIS   D CD2  1 
ATOM   6109 C  CE1  . HIS   D 1 56  ? -77.161 -8.977  21.831  1.00 25.47 ? 35  HIS   D CE1  1 
ATOM   6110 N  NE2  . HIS   D 1 56  ? -78.223 -8.214  21.982  1.00 26.57 ? 35  HIS   D NE2  1 
ATOM   6111 N  N    . ASN   D 1 57  ? -77.677 -9.939  26.488  1.00 20.57 ? 36  ASN   D N    1 
ATOM   6112 C  CA   . ASN   D 1 57  ? -78.495 -11.134 26.643  1.00 23.11 ? 36  ASN   D CA   1 
ATOM   6113 C  C    . ASN   D 1 57  ? -78.624 -11.594 28.095  1.00 24.24 ? 36  ASN   D C    1 
ATOM   6114 O  O    . ASN   D 1 57  ? -79.599 -12.270 28.430  1.00 25.55 ? 36  ASN   D O    1 
ATOM   6115 C  CB   . ASN   D 1 57  ? -77.996 -12.289 25.781  1.00 23.85 ? 36  ASN   D CB   1 
ATOM   6116 C  CG   . ASN   D 1 57  ? -78.169 -11.993 24.307  1.00 28.16 ? 36  ASN   D CG   1 
ATOM   6117 O  OD1  . ASN   D 1 57  ? -79.179 -11.405 23.902  1.00 28.85 ? 36  ASN   D OD1  1 
ATOM   6118 N  ND2  . ASN   D 1 57  ? -77.198 -12.382 23.495  1.00 30.03 ? 36  ASN   D ND2  1 
ATOM   6119 N  N    . SER   D 1 58  ? -77.663 -11.249 28.965  1.00 21.16 ? 37  SER   D N    1 
ATOM   6120 C  CA   . SER   D 1 58  ? -77.557 -11.914 30.257  1.00 22.10 ? 37  SER   D CA   1 
ATOM   6121 C  C    . SER   D 1 58  ? -78.377 -11.190 31.324  1.00 22.09 ? 37  SER   D C    1 
ATOM   6122 O  O    . SER   D 1 58  ? -77.826 -10.662 32.292  1.00 20.80 ? 37  SER   D O    1 
ATOM   6123 C  CB   . SER   D 1 58  ? -76.111 -12.059 30.670  1.00 22.22 ? 37  SER   D CB   1 
ATOM   6124 O  OG   . SER   D 1 58  ? -75.472 -12.991 29.809  1.00 23.81 ? 37  SER   D OG   1 
ATOM   6125 N  N    . ALA   D 1 59  ? -79.705 -11.205 31.167  1.00 21.89 ? 38  ALA   D N    1 
ATOM   6126 C  CA   . ALA   D 1 59  ? -80.579 -10.415 32.011  1.00 22.06 ? 38  ALA   D CA   1 
ATOM   6127 C  C    . ALA   D 1 59  ? -80.578 -10.938 33.446  1.00 21.62 ? 38  ALA   D C    1 
ATOM   6128 O  O    . ALA   D 1 59  ? -80.507 -10.155 34.386  1.00 24.20 ? 38  ALA   D O    1 
ATOM   6129 C  CB   . ALA   D 1 59  ? -81.978 -10.424 31.435  1.00 24.79 ? 38  ALA   D CB   1 
ATOM   6130 N  N    . GLU   D 1 60  ? -80.686 -12.260 33.595  1.00 23.92 ? 39  GLU   D N    1 
ATOM   6131 C  CA   . GLU   D 1 60  ? -80.765 -12.854 34.919  1.00 24.68 ? 39  GLU   D CA   1 
ATOM   6132 C  C    . GLU   D 1 60  ? -79.487 -12.547 35.698  1.00 22.33 ? 39  GLU   D C    1 
ATOM   6133 O  O    . GLU   D 1 60  ? -79.542 -12.165 36.869  1.00 22.18 ? 39  GLU   D O    1 
ATOM   6134 C  CB   . GLU   D 1 60  ? -81.048 -14.351 34.795  1.00 25.67 ? 39  GLU   D CB   1 
ATOM   6135 C  CG   . GLU   D 1 60  ? -82.492 -14.660 34.397  1.00 29.63 ? 39  GLU   D CG   1 
ATOM   6136 C  CD   . GLU   D 1 60  ? -82.846 -16.138 34.331  0.50 32.49 ? 39  GLU   D CD   1 
ATOM   6137 O  OE1  . GLU   D 1 60  ? -81.971 -16.989 34.593  0.50 33.64 ? 39  GLU   D OE1  1 
ATOM   6138 O  OE2  . GLU   D 1 60  ? -84.013 -16.440 34.009  0.50 34.75 ? 39  GLU   D OE2  1 
ATOM   6139 N  N    . ALA   D 1 61  ? -78.335 -12.696 35.035  1.00 21.81 ? 40  ALA   D N    1 
ATOM   6140 C  CA   . ALA   D 1 61  ? -77.061 -12.448 35.691  1.00 21.82 ? 40  ALA   D CA   1 
ATOM   6141 C  C    . ALA   D 1 61  ? -76.912 -10.972 36.072  1.00 20.04 ? 40  ALA   D C    1 
ATOM   6142 O  O    . ALA   D 1 61  ? -76.371 -10.651 37.131  1.00 20.88 ? 40  ALA   D O    1 
ATOM   6143 C  CB   . ALA   D 1 61  ? -75.927 -12.918 34.803  1.00 21.84 ? 40  ALA   D CB   1 
ATOM   6144 N  N    . ALA   D 1 62  ? -77.366 -10.074 35.198  1.00 19.68 ? 41  ALA   D N    1 
ATOM   6145 C  CA   . ALA   D 1 62  ? -77.261 -8.647  35.467  1.00 19.46 ? 41  ALA   D CA   1 
ATOM   6146 C  C    . ALA   D 1 62  ? -78.095 -8.264  36.691  1.00 20.36 ? 41  ALA   D C    1 
ATOM   6147 O  O    . ALA   D 1 62  ? -77.639 -7.511  37.550  1.00 21.23 ? 41  ALA   D O    1 
ATOM   6148 C  CB   . ALA   D 1 62  ? -77.704 -7.860  34.250  1.00 18.85 ? 41  ALA   D CB   1 
ATOM   6149 N  N    . VAL   D 1 63  ? -79.322 -8.796  36.761  1.00 21.05 ? 42  VAL   D N    1 
ATOM   6150 C  CA   . VAL   D 1 63  ? -80.198 -8.453  37.871  1.00 23.70 ? 42  VAL   D CA   1 
ATOM   6151 C  C    . VAL   D 1 63  ? -79.660 -9.064  39.165  1.00 22.35 ? 42  VAL   D C    1 
ATOM   6152 O  O    . VAL   D 1 63  ? -79.751 -8.440  40.217  1.00 23.18 ? 42  VAL   D O    1 
ATOM   6153 C  CB   . VAL   D 1 63  ? -81.639 -8.889  37.536  1.00 24.52 ? 42  VAL   D CB   1 
ATOM   6154 C  CG1  . VAL   D 1 63  ? -82.570 -8.796  38.742  1.00 28.95 ? 42  VAL   D CG1  1 
ATOM   6155 C  CG2  . VAL   D 1 63  ? -82.193 -8.086  36.362  1.00 25.73 ? 42  VAL   D CG2  1 
ATOM   6156 N  N    . SER   D 1 64  ? -79.090 -10.272 39.068  1.00 22.67 ? 43  SER   D N    1 
ATOM   6157 C  CA   . SER   D 1 64  ? -78.518 -10.968 40.214  1.00 22.00 ? 43  SER   D CA   1 
ATOM   6158 C  C    . SER   D 1 64  ? -77.389 -10.137 40.815  1.00 23.67 ? 43  SER   D C    1 
ATOM   6159 O  O    . SER   D 1 64  ? -77.293 -9.943  42.031  1.00 22.18 ? 43  SER   D O    1 
ATOM   6160 C  CB   . SER   D 1 64  ? -78.016 -12.334 39.798  1.00 23.45 ? 43  SER   D CB   1 
ATOM   6161 O  OG   . SER   D 1 64  ? -77.503 -13.054 40.916  1.00 27.88 ? 43  SER   D OG   1 
ATOM   6162 N  N    . LEU   D 1 65  ? -76.504 -9.655  39.935  1.00 19.75 ? 44  LEU   D N    1 
ATOM   6163 C  CA   . LEU   D 1 65  ? -75.433 -8.785  40.383  1.00 20.59 ? 44  LEU   D CA   1 
ATOM   6164 C  C    . LEU   D 1 65  ? -75.971 -7.496  41.003  1.00 19.83 ? 44  LEU   D C    1 
ATOM   6165 O  O    . LEU   D 1 65  ? -75.502 -7.086  42.071  1.00 20.03 ? 44  LEU   D O    1 
ATOM   6166 C  CB   . LEU   D 1 65  ? -74.508 -8.502  39.201  1.00 20.67 ? 44  LEU   D CB   1 
ATOM   6167 C  CG   . LEU   D 1 65  ? -73.385 -7.507  39.507  1.00 22.36 ? 44  LEU   D CG   1 
ATOM   6168 C  CD1  . LEU   D 1 65  ? -72.465 -7.960  40.629  1.00 22.89 ? 44  LEU   D CD1  1 
ATOM   6169 C  CD2  . LEU   D 1 65  ? -72.595 -7.291  38.223  1.00 24.34 ? 44  LEU   D CD2  1 
ATOM   6170 N  N    . ALA   D 1 66  ? -76.936 -6.844  40.337  1.00 21.10 ? 45  ALA   D N    1 
ATOM   6171 C  CA   . ALA   D 1 66  ? -77.463 -5.600  40.878  1.00 20.59 ? 45  ALA   D CA   1 
ATOM   6172 C  C    . ALA   D 1 66  ? -78.045 -5.837  42.279  1.00 21.36 ? 45  ALA   D C    1 
ATOM   6173 O  O    . ALA   D 1 66  ? -77.826 -5.038  43.186  1.00 23.09 ? 45  ALA   D O    1 
ATOM   6174 C  CB   . ALA   D 1 66  ? -78.465 -4.998  39.933  1.00 20.96 ? 45  ALA   D CB   1 
ATOM   6175 N  N    . ASP   D 1 67  ? -78.706 -6.992  42.455  1.00 21.99 ? 46  ASP   D N    1 
ATOM   6176 C  CA   . ASP   D 1 67  ? -79.302 -7.352  43.739  1.00 24.45 ? 46  ASP   D CA   1 
ATOM   6177 C  C    . ASP   D 1 67  ? -78.219 -7.498  44.810  1.00 25.94 ? 46  ASP   D C    1 
ATOM   6178 O  O    . ASP   D 1 67  ? -78.367 -6.978  45.913  1.00 25.86 ? 46  ASP   D O    1 
ATOM   6179 C  CB   . ASP   D 1 67  ? -80.133 -8.622  43.626  1.00 27.66 ? 46  ASP   D CB   1 
ATOM   6180 C  CG   . ASP   D 1 67  ? -81.468 -8.499  42.908  1.00 34.02 ? 46  ASP   D CG   1 
ATOM   6181 O  OD1  . ASP   D 1 67  ? -81.909 -7.352  42.655  1.00 35.83 ? 46  ASP   D OD1  1 
ATOM   6182 O  OD2  . ASP   D 1 67  ? -82.060 -9.559  42.606  1.00 37.84 ? 46  ASP   D OD2  1 
ATOM   6183 N  N    . GLU   D 1 68  ? -77.125 -8.202  44.484  1.00 23.19 ? 47  GLU   D N    1 
ATOM   6184 C  CA   . GLU   D 1 68  ? -76.020 -8.373  45.413  1.00 25.21 ? 47  GLU   D CA   1 
ATOM   6185 C  C    . GLU   D 1 68  ? -75.422 -7.022  45.812  1.00 24.28 ? 47  GLU   D C    1 
ATOM   6186 O  O    . GLU   D 1 68  ? -75.073 -6.816  46.976  1.00 25.62 ? 47  GLU   D O    1 
ATOM   6187 C  CB   . GLU   D 1 68  ? -74.941 -9.302  44.858  1.00 26.58 ? 47  GLU   D CB   1 
ATOM   6188 C  CG   . GLU   D 1 68  ? -75.391 -10.757 44.722  1.00 32.02 ? 47  GLU   D CG   1 
ATOM   6189 C  CD   . GLU   D 1 68  ? -74.329 -11.612 44.051  1.00 37.63 ? 47  GLU   D CD   1 
ATOM   6190 O  OE1  . GLU   D 1 68  ? -73.292 -11.029 43.662  1.00 43.12 ? 47  GLU   D OE1  1 
ATOM   6191 O  OE2  . GLU   D 1 68  ? -74.514 -12.843 43.934  1.00 33.82 ? 47  GLU   D OE2  1 
ATOM   6192 N  N    . LEU   D 1 69  ? -75.268 -6.105  44.851  1.00 22.40 ? 48  LEU   D N    1 
ATOM   6193 C  CA   . LEU   D 1 69  ? -74.648 -4.826  45.157  1.00 23.44 ? 48  LEU   D CA   1 
ATOM   6194 C  C    . LEU   D 1 69  ? -75.595 -3.940  45.966  1.00 23.96 ? 48  LEU   D C    1 
ATOM   6195 O  O    . LEU   D 1 69  ? -75.158 -3.219  46.863  1.00 22.98 ? 48  LEU   D O    1 
ATOM   6196 C  CB   . LEU   D 1 69  ? -74.184 -4.149  43.869  1.00 23.46 ? 48  LEU   D CB   1 
ATOM   6197 C  CG   . LEU   D 1 69  ? -73.159 -4.932  43.044  1.00 23.29 ? 48  LEU   D CG   1 
ATOM   6198 C  CD1  . LEU   D 1 69  ? -72.766 -4.012  41.892  1.00 23.98 ? 48  LEU   D CD1  1 
ATOM   6199 C  CD2  . LEU   D 1 69  ? -71.955 -5.283  43.895  1.00 23.52 ? 48  LEU   D CD2  1 
ATOM   6200 N  N    . ASN   D 1 70  ? -76.887 -4.006  45.647  1.00 23.40 ? 49  ASN   D N    1 
ATOM   6201 C  CA   . ASN   D 1 70  ? -77.866 -3.212  46.375  1.00 25.98 ? 49  ASN   D CA   1 
ATOM   6202 C  C    . ASN   D 1 70  ? -78.056 -3.738  47.798  1.00 26.47 ? 49  ASN   D C    1 
ATOM   6203 O  O    . ASN   D 1 70  ? -78.406 -2.964  48.682  1.00 27.55 ? 49  ASN   D O    1 
ATOM   6204 C  CB   . ASN   D 1 70  ? -79.192 -3.115  45.631  1.00 23.07 ? 49  ASN   D CB   1 
ATOM   6205 C  CG   . ASN   D 1 70  ? -79.109 -2.170  44.455  1.00 23.29 ? 49  ASN   D CG   1 
ATOM   6206 O  OD1  . ASN   D 1 70  ? -78.534 -1.077  44.569  1.00 24.11 ? 49  ASN   D OD1  1 
ATOM   6207 N  ND2  . ASN   D 1 70  ? -79.661 -2.579  43.325  1.00 24.28 ? 49  ASN   D ND2  1 
ATOM   6208 N  N    . LYS   D 1 71  ? -77.840 -5.046  48.001  1.00 26.65 ? 50  LYS   D N    1 
ATOM   6209 C  CA   . LYS   D 1 71  ? -77.918 -5.636  49.331  1.00 28.36 ? 50  LYS   D CA   1 
ATOM   6210 C  C    . LYS   D 1 71  ? -76.796 -5.067  50.200  1.00 31.88 ? 50  LYS   D C    1 
ATOM   6211 O  O    . LYS   D 1 71  ? -76.984 -4.865  51.399  1.00 32.58 ? 50  LYS   D O    1 
ATOM   6212 C  CB   . LYS   D 1 71  ? -77.932 -7.170  49.268  1.00 27.67 ? 50  LYS   D CB   1 
ATOM   6213 N  N    . GLU   D 1 72  ? -75.649 -4.761  49.578  1.00 29.76 ? 51  GLU   D N    1 
ATOM   6214 C  CA   A GLU   D 1 72  ? -74.487 -4.228  50.268  0.60 30.15 ? 51  GLU   D CA   1 
ATOM   6215 C  CA   B GLU   D 1 72  ? -74.502 -4.238  50.300  0.40 29.60 ? 51  GLU   D CA   1 
ATOM   6216 C  C    . GLU   D 1 72  ? -74.716 -2.754  50.593  1.00 28.78 ? 51  GLU   D C    1 
ATOM   6217 O  O    . GLU   D 1 72  ? -74.479 -2.308  51.716  1.00 30.30 ? 51  GLU   D O    1 
ATOM   6218 C  CB   A GLU   D 1 72  ? -73.260 -4.442  49.377  0.60 31.54 ? 51  GLU   D CB   1 
ATOM   6219 C  CB   B GLU   D 1 72  ? -73.194 -4.555  49.570  0.40 30.26 ? 51  GLU   D CB   1 
ATOM   6220 C  CG   A GLU   D 1 72  ? -71.952 -3.936  49.979  0.60 35.00 ? 51  GLU   D CG   1 
ATOM   6221 C  CG   B GLU   D 1 72  ? -72.943 -6.053  49.420  0.40 32.31 ? 51  GLU   D CG   1 
ATOM   6222 C  CD   A GLU   D 1 72  ? -71.657 -4.484  51.362  0.60 37.55 ? 51  GLU   D CD   1 
ATOM   6223 C  CD   B GLU   D 1 72  ? -72.839 -6.801  50.736  0.40 32.96 ? 51  GLU   D CD   1 
ATOM   6224 O  OE1  A GLU   D 1 72  ? -71.375 -3.659  52.258  0.60 41.69 ? 51  GLU   D OE1  1 
ATOM   6225 O  OE1  B GLU   D 1 72  ? -71.840 -6.571  51.443  0.40 33.02 ? 51  GLU   D OE1  1 
ATOM   6226 O  OE2  A GLU   D 1 72  ? -71.729 -5.718  51.544  0.60 38.71 ? 51  GLU   D OE2  1 
ATOM   6227 O  OE2  B GLU   D 1 72  ? -73.747 -7.596  51.066  0.40 35.38 ? 51  GLU   D OE2  1 
ATOM   6228 N  N    . ARG   D 1 73  ? -75.161 -1.990  49.585  1.00 26.00 ? 52  ARG   D N    1 
ATOM   6229 C  CA   . ARG   D 1 73  ? -75.474 -0.577  49.761  1.00 26.26 ? 52  ARG   D CA   1 
ATOM   6230 C  C    . ARG   D 1 73  ? -76.718 -0.242  48.939  1.00 27.60 ? 52  ARG   D C    1 
ATOM   6231 O  O    . ARG   D 1 73  ? -76.699 -0.263  47.712  1.00 26.06 ? 52  ARG   D O    1 
ATOM   6232 C  CB   . ARG   D 1 73  ? -74.327 0.372   49.386  1.00 27.52 ? 52  ARG   D CB   1 
ATOM   6233 C  CG   . ARG   D 1 73  ? -73.000 0.239   50.122  1.00 29.76 ? 52  ARG   D CG   1 
ATOM   6234 C  CD   . ARG   D 1 73  ? -72.146 1.498   50.000  1.00 30.62 ? 52  ARG   D CD   1 
ATOM   6235 N  NE   . ARG   D 1 73  ? -71.877 1.879   48.608  1.00 32.35 ? 52  ARG   D NE   1 
ATOM   6236 C  CZ   . ARG   D 1 73  ? -71.003 1.272   47.804  1.00 32.25 ? 52  ARG   D CZ   1 
ATOM   6237 N  NH1  . ARG   D 1 73  ? -70.832 1.709   46.564  1.00 32.53 ? 52  ARG   D NH1  1 
ATOM   6238 N  NH2  . ARG   D 1 73  ? -70.298 0.249   48.250  1.00 31.33 ? 52  ARG   D NH2  1 
ATOM   6239 N  N    . SER   D 1 74  ? -77.827 0.057   49.616  1.00 28.29 ? 53  SER   D N    1 
ATOM   6240 C  CA   A SER   D 1 74  ? -79.081 0.280   48.917  0.60 27.90 ? 53  SER   D CA   1 
ATOM   6241 C  CA   B SER   D 1 74  ? -79.092 0.308   48.943  0.40 26.97 ? 53  SER   D CA   1 
ATOM   6242 C  C    . SER   D 1 74  ? -78.930 1.377   47.862  1.00 25.39 ? 53  SER   D C    1 
ATOM   6243 O  O    . SER   D 1 74  ? -78.238 2.375   48.071  1.00 27.83 ? 53  SER   D O    1 
ATOM   6244 C  CB   A SER   D 1 74  ? -80.191 0.602   49.891  0.60 29.87 ? 53  SER   D CB   1 
ATOM   6245 C  CB   B SER   D 1 74  ? -80.155 0.714   49.939  0.40 27.03 ? 53  SER   D CB   1 
ATOM   6246 O  OG   A SER   D 1 74  ? -79.929 1.836   50.545  0.60 30.32 ? 53  SER   D OG   1 
ATOM   6247 O  OG   B SER   D 1 74  ? -80.196 -0.185  51.039  0.40 25.56 ? 53  SER   D OG   1 
ATOM   6248 N  N    . ASN   D 1 75  ? -79.586 1.167   46.710  1.00 26.85 ? 54  ASN   D N    1 
ATOM   6249 C  CA   . ASN   D 1 75  ? -79.749 2.175   45.671  1.00 26.97 ? 54  ASN   D CA   1 
ATOM   6250 C  C    . ASN   D 1 75  ? -78.422 2.557   45.011  1.00 25.73 ? 54  ASN   D C    1 
ATOM   6251 O  O    . ASN   D 1 75  ? -78.219 3.727   44.667  1.00 27.05 ? 54  ASN   D O    1 
ATOM   6252 C  CB   . ASN   D 1 75  ? -80.423 3.435   46.208  1.00 29.33 ? 54  ASN   D CB   1 
ATOM   6253 C  CG   . ASN   D 1 75  ? -81.746 3.122   46.865  1.00 36.75 ? 54  ASN   D CG   1 
ATOM   6254 O  OD1  . ASN   D 1 75  ? -82.561 2.385   46.298  1.00 36.10 ? 54  ASN   D OD1  1 
ATOM   6255 N  ND2  . ASN   D 1 75  ? -81.949 3.616   48.078  1.00 40.54 ? 54  ASN   D ND2  1 
ATOM   6256 N  N    . THR   D 1 76  ? -77.533 1.573   44.827  1.00 23.60 ? 55  THR   D N    1 
ATOM   6257 C  CA   . THR   D 1 76  ? -76.225 1.893   44.266  1.00 23.23 ? 55  THR   D CA   1 
ATOM   6258 C  C    . THR   D 1 76  ? -75.993 1.174   42.937  1.00 22.41 ? 55  THR   D C    1 
ATOM   6259 O  O    . THR   D 1 76  ? -74.912 1.321   42.365  1.00 22.49 ? 55  THR   D O    1 
ATOM   6260 C  CB   . THR   D 1 76  ? -75.102 1.579   45.257  1.00 21.90 ? 55  THR   D CB   1 
ATOM   6261 O  OG1  . THR   D 1 76  ? -75.229 0.223   45.678  1.00 24.63 ? 55  THR   D OG1  1 
ATOM   6262 C  CG2  . THR   D 1 76  ? -75.094 2.537   46.433  1.00 25.43 ? 55  THR   D CG2  1 
ATOM   6263 N  N    . ALA   D 1 77  ? -76.935 0.328   42.500  1.00 21.33 ? 56  ALA   D N    1 
ATOM   6264 C  CA   . ALA   D 1 77  ? -76.736 -0.448  41.282  1.00 21.45 ? 56  ALA   D CA   1 
ATOM   6265 C  C    . ALA   D 1 77  ? -78.030 -0.502  40.469  1.00 22.71 ? 56  ALA   D C    1 
ATOM   6266 O  O    . ALA   D 1 77  ? -79.105 -0.701  41.015  1.00 22.41 ? 56  ALA   D O    1 
ATOM   6267 C  CB   . ALA   D 1 77  ? -76.219 -1.848  41.580  1.00 22.11 ? 56  ALA   D CB   1 
ATOM   6268 N  N    . VAL   D 1 78  ? -77.912 -0.326  39.146  1.00 21.23 ? 57  VAL   D N    1 
ATOM   6269 C  CA   . VAL   D 1 78  ? -79.032 -0.488  38.226  1.00 21.38 ? 57  VAL   D CA   1 
ATOM   6270 C  C    . VAL   D 1 78  ? -78.537 -1.285  37.025  1.00 21.88 ? 57  VAL   D C    1 
ATOM   6271 O  O    . VAL   D 1 78  ? -77.332 -1.355  36.783  1.00 21.43 ? 57  VAL   D O    1 
ATOM   6272 C  CB   . VAL   D 1 78  ? -79.680 0.839   37.773  1.00 22.60 ? 57  VAL   D CB   1 
ATOM   6273 C  CG1  . VAL   D 1 78  ? -80.258 1.617   38.950  1.00 22.98 ? 57  VAL   D CG1  1 
ATOM   6274 C  CG2  . VAL   D 1 78  ? -78.737 1.727   36.956  1.00 21.92 ? 57  VAL   D CG2  1 
ATOM   6275 N  N    . VAL   D 1 79  ? -79.472 -1.876  36.283  1.00 20.22 ? 58  VAL   D N    1 
ATOM   6276 C  CA   . VAL   D 1 79  ? -79.134 -2.573  35.052  1.00 20.29 ? 58  VAL   D CA   1 
ATOM   6277 C  C    . VAL   D 1 79  ? -79.595 -1.738  33.857  1.00 21.95 ? 58  VAL   D C    1 
ATOM   6278 O  O    . VAL   D 1 79  ? -80.514 -0.913  33.956  1.00 22.41 ? 58  VAL   D O    1 
ATOM   6279 C  CB   . VAL   D 1 79  ? -79.664 -4.022  34.978  1.00 22.09 ? 58  VAL   D CB   1 
ATOM   6280 C  CG1  . VAL   D 1 79  ? -79.224 -4.850  36.182  1.00 20.41 ? 58  VAL   D CG1  1 
ATOM   6281 C  CG2  . VAL   D 1 79  ? -81.183 -4.065  34.809  1.00 22.24 ? 58  VAL   D CG2  1 
ATOM   6282 N  N    . CYS   D 1 80  ? -78.944 -1.966  32.710  1.00 18.89 ? 59  CYS   D N    1 
ATOM   6283 C  CA   . CYS   D 1 80  ? -79.343 -1.292  31.484  1.00 21.12 ? 59  CYS   D CA   1 
ATOM   6284 C  C    . CYS   D 1 80  ? -79.106 -2.229  30.300  1.00 20.39 ? 59  CYS   D C    1 
ATOM   6285 O  O    . CYS   D 1 80  ? -77.966 -2.592  30.020  1.00 21.21 ? 59  CYS   D O    1 
ATOM   6286 C  CB   . CYS   D 1 80  ? -78.601 0.037   31.325  1.00 21.66 ? 59  CYS   D CB   1 
ATOM   6287 S  SG   . CYS   D 1 80  ? -78.982 0.872   29.761  1.00 25.09 ? 59  CYS   D SG   1 
ATOM   6288 N  N    . GLN   D 1 81  ? -80.168 -2.591  29.563  1.00 20.24 ? 60  GLN   D N    1 
ATOM   6289 C  CA   . GLN   D 1 81  ? -80.029 -3.497  28.430  1.00 20.85 ? 60  GLN   D CA   1 
ATOM   6290 C  C    . GLN   D 1 81  ? -79.753 -2.722  27.144  1.00 19.87 ? 60  GLN   D C    1 
ATOM   6291 O  O    . GLN   D 1 81  ? -80.419 -1.735  26.849  1.00 21.17 ? 60  GLN   D O    1 
ATOM   6292 C  CB   . GLN   D 1 81  ? -81.317 -4.296  28.200  1.00 21.97 ? 60  GLN   D CB   1 
ATOM   6293 C  CG   . GLN   D 1 81  ? -81.176 -5.528  27.305  1.00 23.28 ? 60  GLN   D CG   1 
ATOM   6294 C  CD   . GLN   D 1 81  ? -81.215 -5.260  25.815  1.00 26.15 ? 60  GLN   D CD   1 
ATOM   6295 O  OE1  . GLN   D 1 81  ? -81.775 -4.268  25.333  1.00 30.39 ? 60  GLN   D OE1  1 
ATOM   6296 N  NE2  . GLN   D 1 81  ? -80.616 -6.170  25.059  1.00 26.95 ? 60  GLN   D NE2  1 
ATOM   6297 N  N    . ALA   D 1 82  ? -78.763 -3.188  26.366  1.00 18.61 ? 61  ALA   D N    1 
ATOM   6298 C  CA   . ALA   D 1 82  ? -78.560 -2.621  25.041  1.00 18.84 ? 61  ALA   D CA   1 
ATOM   6299 C  C    . ALA   D 1 82  ? -77.752 -3.575  24.174  1.00 17.20 ? 61  ALA   D C    1 
ATOM   6300 O  O    . ALA   D 1 82  ? -76.824 -4.228  24.649  1.00 17.84 ? 61  ALA   D O    1 
ATOM   6301 C  CB   . ALA   D 1 82  ? -77.900 -1.256  25.115  1.00 19.47 ? 61  ALA   D CB   1 
ATOM   6302 N  N    . ASP   D 1 83  ? -78.121 -3.600  22.887  1.00 18.37 ? 62  ASP   D N    1 
ATOM   6303 C  CA   . ASP   D 1 83  ? -77.351 -4.284  21.861  1.00 18.63 ? 62  ASP   D CA   1 
ATOM   6304 C  C    . ASP   D 1 83  ? -76.333 -3.287  21.324  1.00 18.17 ? 62  ASP   D C    1 
ATOM   6305 O  O    . ASP   D 1 83  ? -76.697 -2.161  20.947  1.00 20.06 ? 62  ASP   D O    1 
ATOM   6306 C  CB   . ASP   D 1 83  ? -78.260 -4.693  20.710  1.00 19.60 ? 62  ASP   D CB   1 
ATOM   6307 C  CG   . ASP   D 1 83  ? -77.645 -5.587  19.639  1.00 22.52 ? 62  ASP   D CG   1 
ATOM   6308 O  OD1  . ASP   D 1 83  ? -76.423 -5.845  19.691  1.00 21.63 ? 62  ASP   D OD1  1 
ATOM   6309 O  OD2  . ASP   D 1 83  ? -78.399 -6.032  18.742  1.00 26.28 ? 62  ASP   D OD2  1 
ATOM   6310 N  N    . LEU   D 1 84  ? -75.053 -3.693  21.324  1.00 16.71 ? 63  LEU   D N    1 
ATOM   6311 C  CA   . LEU   D 1 84  ? -73.999 -2.784  20.889  1.00 16.60 ? 63  LEU   D CA   1 
ATOM   6312 C  C    . LEU   D 1 84  ? -73.498 -3.145  19.487  1.00 17.27 ? 63  LEU   D C    1 
ATOM   6313 O  O    . LEU   D 1 84  ? -72.476 -2.622  19.046  1.00 17.57 ? 63  LEU   D O    1 
ATOM   6314 C  CB   . LEU   D 1 84  ? -72.883 -2.743  21.941  1.00 16.70 ? 63  LEU   D CB   1 
ATOM   6315 C  CG   . LEU   D 1 84  ? -73.288 -2.157  23.301  1.00 17.39 ? 63  LEU   D CG   1 
ATOM   6316 C  CD1  . LEU   D 1 84  ? -72.141 -2.242  24.316  1.00 19.81 ? 63  LEU   D CD1  1 
ATOM   6317 C  CD2  . LEU   D 1 84  ? -73.809 -0.733  23.228  1.00 18.01 ? 63  LEU   D CD2  1 
ATOM   6318 N  N    . THR   D 1 85  ? -74.226 -4.008  18.763  1.00 15.59 ? 64  THR   D N    1 
ATOM   6319 C  CA   . THR   D 1 85  ? -73.963 -4.242  17.349  1.00 16.49 ? 64  THR   D CA   1 
ATOM   6320 C  C    . THR   D 1 85  ? -74.053 -2.937  16.551  1.00 17.46 ? 64  THR   D C    1 
ATOM   6321 O  O    . THR   D 1 85  ? -74.916 -2.085  16.798  1.00 17.05 ? 64  THR   D O    1 
ATOM   6322 C  CB   . THR   D 1 85  ? -74.976 -5.259  16.818  1.00 19.22 ? 64  THR   D CB   1 
ATOM   6323 O  OG1  . THR   D 1 85  ? -74.856 -6.449  17.588  1.00 23.84 ? 64  THR   D OG1  1 
ATOM   6324 C  CG2  . THR   D 1 85  ? -74.663 -5.639  15.383  1.00 19.74 ? 64  THR   D CG2  1 
ATOM   6325 N  N    . ASN   D 1 86  ? -73.153 -2.757  15.570  1.00 15.93 ? 65  ASN   D N    1 
ATOM   6326 C  CA   . ASN   D 1 86  ? -73.240 -1.568  14.736  1.00 15.07 ? 65  ASN   D CA   1 
ATOM   6327 C  C    . ASN   D 1 86  ? -74.543 -1.564  13.921  1.00 16.25 ? 65  ASN   D C    1 
ATOM   6328 O  O    . ASN   D 1 86  ? -74.951 -2.596  13.377  1.00 17.46 ? 65  ASN   D O    1 
ATOM   6329 C  CB   . ASN   D 1 86  ? -72.049 -1.525  13.780  1.00 16.15 ? 65  ASN   D CB   1 
ATOM   6330 C  CG   . ASN   D 1 86  ? -71.894 -0.186  13.093  1.00 16.54 ? 65  ASN   D CG   1 
ATOM   6331 O  OD1  . ASN   D 1 86  ? -72.137 0.872   13.696  1.00 16.74 ? 65  ASN   D OD1  1 
ATOM   6332 N  ND2  . ASN   D 1 86  ? -71.526 -0.210  11.818  1.00 17.76 ? 65  ASN   D ND2  1 
ATOM   6333 N  N    . SER   D 1 87  ? -75.151 -0.372  13.851  1.00 16.26 ? 66  SER   D N    1 
ATOM   6334 C  CA   . SER   D 1 87  ? -76.330 -0.052  13.054  1.00 16.04 ? 66  SER   D CA   1 
ATOM   6335 C  C    . SER   D 1 87  ? -76.531 1.459   13.093  1.00 16.64 ? 66  SER   D C    1 
ATOM   6336 O  O    . SER   D 1 87  ? -75.872 2.166   13.847  1.00 16.90 ? 66  SER   D O    1 
ATOM   6337 C  CB   . SER   D 1 87  ? -77.564 -0.738  13.592  1.00 17.83 ? 66  SER   D CB   1 
ATOM   6338 O  OG   . SER   D 1 87  ? -78.055 -0.036  14.730  1.00 19.66 ? 66  SER   D OG   1 
ATOM   6339 N  N    . ASN   D 1 88  ? -77.534 1.920   12.333  1.00 16.92 ? 67  ASN   D N    1 
ATOM   6340 C  CA   . ASN   D 1 88  ? -77.867 3.331   12.326  1.00 17.44 ? 67  ASN   D CA   1 
ATOM   6341 C  C    . ASN   D 1 88  ? -78.537 3.788   13.621  1.00 18.95 ? 67  ASN   D C    1 
ATOM   6342 O  O    . ASN   D 1 88  ? -78.649 4.996   13.817  1.00 20.63 ? 67  ASN   D O    1 
ATOM   6343 C  CB   . ASN   D 1 88  ? -78.697 3.689   11.096  1.00 18.12 ? 67  ASN   D CB   1 
ATOM   6344 C  CG   . ASN   D 1 88  ? -77.863 3.729   9.840   1.00 20.78 ? 67  ASN   D CG   1 
ATOM   6345 O  OD1  . ASN   D 1 88  ? -76.631 3.786   9.911   1.00 22.95 ? 67  ASN   D OD1  1 
ATOM   6346 N  ND2  . ASN   D 1 88  ? -78.508 3.711   8.689   1.00 22.20 ? 67  ASN   D ND2  1 
ATOM   6347 N  N    . VAL   D 1 89  ? -78.913 2.865   14.517  1.00 17.65 ? 68  VAL   D N    1 
ATOM   6348 C  CA   . VAL   D 1 89  ? -79.475 3.274   15.798  1.00 18.58 ? 68  VAL   D CA   1 
ATOM   6349 C  C    . VAL   D 1 89  ? -78.486 3.058   16.941  1.00 18.16 ? 68  VAL   D C    1 
ATOM   6350 O  O    . VAL   D 1 89  ? -78.782 3.376   18.087  1.00 18.43 ? 68  VAL   D O    1 
ATOM   6351 C  CB   . VAL   D 1 89  ? -80.842 2.641   16.118  1.00 21.07 ? 68  VAL   D CB   1 
ATOM   6352 C  CG1  . VAL   D 1 89  ? -81.826 2.945   14.996  1.00 25.10 ? 68  VAL   D CG1  1 
ATOM   6353 C  CG2  . VAL   D 1 89  ? -80.726 1.144   16.376  1.00 22.59 ? 68  VAL   D CG2  1 
ATOM   6354 N  N    . LEU   D 1 90  ? -77.297 2.528   16.640  1.00 16.87 ? 69  LEU   D N    1 
ATOM   6355 C  CA   . LEU   D 1 90  ? -76.302 2.377   17.694  1.00 14.78 ? 69  LEU   D CA   1 
ATOM   6356 C  C    . LEU   D 1 90  ? -76.014 3.701   18.415  1.00 14.94 ? 69  LEU   D C    1 
ATOM   6357 O  O    . LEU   D 1 90  ? -75.864 3.679   19.629  1.00 14.94 ? 69  LEU   D O    1 
ATOM   6358 C  CB   . LEU   D 1 90  ? -75.040 1.693   17.160  1.00 14.40 ? 69  LEU   D CB   1 
ATOM   6359 C  CG   . LEU   D 1 90  ? -73.992 1.391   18.238  1.00 14.90 ? 69  LEU   D CG   1 
ATOM   6360 C  CD1  . LEU   D 1 90  ? -74.491 0.462   19.326  1.00 15.91 ? 69  LEU   D CD1  1 
ATOM   6361 C  CD2  . LEU   D 1 90  ? -72.730 0.812   17.577  1.00 16.54 ? 69  LEU   D CD2  1 
ATOM   6362 N  N    . PRO   D 1 91  ? -75.904 4.882   17.766  1.00 15.28 ? 70  PRO   D N    1 
ATOM   6363 C  CA   . PRO   D 1 91  ? -75.708 6.131   18.497  1.00 16.30 ? 70  PRO   D CA   1 
ATOM   6364 C  C    . PRO   D 1 91  ? -76.770 6.384   19.564  1.00 16.45 ? 70  PRO   D C    1 
ATOM   6365 O  O    . PRO   D 1 91  ? -76.445 6.775   20.680  1.00 17.31 ? 70  PRO   D O    1 
ATOM   6366 C  CB   . PRO   D 1 91  ? -75.691 7.199   17.414  1.00 15.88 ? 70  PRO   D CB   1 
ATOM   6367 C  CG   . PRO   D 1 91  ? -75.196 6.454   16.198  1.00 15.92 ? 70  PRO   D CG   1 
ATOM   6368 C  CD   . PRO   D 1 91  ? -75.831 5.073   16.309  1.00 15.79 ? 70  PRO   D CD   1 
ATOM   6369 N  N    . ALA   D 1 92  ? -78.028 6.098   19.220  1.00 16.87 ? 71  ALA   D N    1 
ATOM   6370 C  CA   . ALA   D 1 92  ? -79.120 6.266   20.172  1.00 16.68 ? 71  ALA   D CA   1 
ATOM   6371 C  C    . ALA   D 1 92  ? -78.994 5.298   21.343  1.00 16.36 ? 71  ALA   D C    1 
ATOM   6372 O  O    . ALA   D 1 92  ? -79.279 5.669   22.484  1.00 19.81 ? 71  ALA   D O    1 
ATOM   6373 C  CB   . ALA   D 1 92  ? -80.456 6.103   19.457  1.00 17.44 ? 71  ALA   D CB   1 
ATOM   6374 N  N    . SER   D 1 93  ? -78.606 4.048   21.059  1.00 16.07 ? 72  SER   D N    1 
ATOM   6375 C  CA   . SER   D 1 93  ? -78.464 3.075   22.125  1.00 15.88 ? 72  SER   D CA   1 
ATOM   6376 C  C    . SER   D 1 93  ? -77.371 3.509   23.101  1.00 17.80 ? 72  SER   D C    1 
ATOM   6377 O  O    . SER   D 1 93  ? -77.498 3.363   24.311  1.00 17.47 ? 72  SER   D O    1 
ATOM   6378 C  CB   . SER   D 1 93  ? -78.154 1.697   21.582  1.00 17.94 ? 72  SER   D CB   1 
ATOM   6379 O  OG   . SER   D 1 93  ? -79.279 1.156   20.894  1.00 20.17 ? 72  SER   D OG   1 
ATOM   6380 N  N    . CYS   D 1 94  ? -76.265 4.025   22.560  1.00 17.23 ? 73  CYS   D N    1 
ATOM   6381 C  CA   . CYS   D 1 94  ? -75.165 4.423   23.424  1.00 16.31 ? 73  CYS   D CA   1 
ATOM   6382 C  C    . CYS   D 1 94  ? -75.529 5.663   24.244  1.00 16.53 ? 73  CYS   D C    1 
ATOM   6383 O  O    . CYS   D 1 94  ? -75.149 5.783   25.410  1.00 15.90 ? 73  CYS   D O    1 
ATOM   6384 C  CB   . CYS   D 1 94  ? -73.906 4.629   22.582  1.00 15.64 ? 73  CYS   D CB   1 
ATOM   6385 S  SG   . CYS   D 1 94  ? -73.293 3.073   21.878  1.00 16.61 ? 73  CYS   D SG   1 
ATOM   6386 N  N    . GLU   D 1 95  ? -76.247 6.595   23.617  1.00 18.37 ? 74  GLU   D N    1 
ATOM   6387 C  CA   . GLU   D 1 95  ? -76.694 7.779   24.321  1.00 18.95 ? 74  GLU   D CA   1 
ATOM   6388 C  C    . GLU   D 1 95  ? -77.608 7.354   25.472  1.00 18.79 ? 74  GLU   D C    1 
ATOM   6389 O  O    . GLU   D 1 95  ? -77.501 7.898   26.565  1.00 19.37 ? 74  GLU   D O    1 
ATOM   6390 C  CB   . GLU   D 1 95  ? -77.402 8.712   23.341  1.00 21.73 ? 74  GLU   D CB   1 
ATOM   6391 C  CG   . GLU   D 1 95  ? -77.881 9.990   24.026  1.00 27.77 ? 74  GLU   D CG   1 
ATOM   6392 C  CD   . GLU   D 1 95  ? -78.434 11.034  23.076  1.00 36.91 ? 74  GLU   D CD   1 
ATOM   6393 O  OE1  . GLU   D 1 95  ? -77.658 11.604  22.279  1.00 41.20 ? 74  GLU   D OE1  1 
ATOM   6394 O  OE2  . GLU   D 1 95  ? -79.653 11.288  23.140  1.00 45.49 ? 74  GLU   D OE2  1 
ATOM   6395 N  N    . GLU   D 1 96  ? -78.428 6.321   25.240  1.00 17.94 ? 75  GLU   D N    1 
ATOM   6396 C  CA   . GLU   D 1 96  ? -79.356 5.832   26.250  1.00 19.99 ? 75  GLU   D CA   1 
ATOM   6397 C  C    . GLU   D 1 96  ? -78.611 5.200   27.427  1.00 18.55 ? 75  GLU   D C    1 
ATOM   6398 O  O    . GLU   D 1 96  ? -79.038 5.299   28.573  1.00 19.35 ? 75  GLU   D O    1 
ATOM   6399 C  CB   . GLU   D 1 96  ? -80.334 4.842   25.612  1.00 20.89 ? 75  GLU   D CB   1 
ATOM   6400 C  CG   . GLU   D 1 96  ? -81.348 4.278   26.600  1.00 23.44 ? 75  GLU   D CG   1 
ATOM   6401 C  CD   . GLU   D 1 96  ? -82.124 5.274   27.451  1.00 22.55 ? 75  GLU   D CD   1 
ATOM   6402 O  OE1  . GLU   D 1 96  ? -82.609 4.751   28.463  1.00 24.41 ? 75  GLU   D OE1  1 
ATOM   6403 O  OE2  . GLU   D 1 96  ? -82.251 6.484   27.157  1.00 25.92 ? 75  GLU   D OE2  1 
ATOM   6404 N  N    . ILE   D 1 97  ? -77.508 4.492   27.154  1.00 18.29 ? 76  ILE   D N    1 
ATOM   6405 C  CA   . ILE   D 1 97  ? -76.772 3.866   28.247  1.00 16.87 ? 76  ILE   D CA   1 
ATOM   6406 C  C    . ILE   D 1 97  ? -76.236 4.937   29.193  1.00 17.44 ? 76  ILE   D C    1 
ATOM   6407 O  O    . ILE   D 1 97  ? -76.308 4.801   30.423  1.00 18.04 ? 76  ILE   D O    1 
ATOM   6408 C  CB   . ILE   D 1 97  ? -75.636 2.980   27.701  1.00 16.87 ? 76  ILE   D CB   1 
ATOM   6409 C  CG1  . ILE   D 1 97  ? -76.180 1.698   27.074  1.00 17.74 ? 76  ILE   D CG1  1 
ATOM   6410 C  CG2  . ILE   D 1 97  ? -74.640 2.651   28.816  1.00 18.14 ? 76  ILE   D CG2  1 
ATOM   6411 C  CD1  . ILE   D 1 97  ? -75.165 0.976   26.197  1.00 16.35 ? 76  ILE   D CD1  1 
ATOM   6412 N  N    . ILE   D 1 98  ? -75.651 5.987   28.608  1.00 17.41 ? 77  ILE   D N    1 
ATOM   6413 C  CA   . ILE   D 1 98  ? -75.146 7.079   29.431  1.00 18.44 ? 77  ILE   D CA   1 
ATOM   6414 C  C    . ILE   D 1 98  ? -76.310 7.758   30.165  1.00 18.90 ? 77  ILE   D C    1 
ATOM   6415 O  O    . ILE   D 1 98  ? -76.184 8.048   31.358  1.00 18.16 ? 77  ILE   D O    1 
ATOM   6416 C  CB   . ILE   D 1 98  ? -74.296 8.059   28.606  1.00 18.36 ? 77  ILE   D CB   1 
ATOM   6417 C  CG1  . ILE   D 1 98  ? -73.098 7.365   27.920  1.00 18.45 ? 77  ILE   D CG1  1 
ATOM   6418 C  CG2  . ILE   D 1 98  ? -73.838 9.244   29.467  1.00 19.29 ? 77  ILE   D CG2  1 
ATOM   6419 C  CD1  . ILE   D 1 98  ? -72.133 6.686   28.891  1.00 19.16 ? 77  ILE   D CD1  1 
ATOM   6420 N  N    . ASN   D 1 99  ? -77.430 7.977   29.453  1.00 20.18 ? 78  ASN   D N    1 
ATOM   6421 C  CA   . ASN   D 1 99  ? -78.625 8.583   30.031  1.00 21.44 ? 78  ASN   D CA   1 
ATOM   6422 C  C    . ASN   D 1 99  ? -79.069 7.802   31.262  1.00 21.40 ? 78  ASN   D C    1 
ATOM   6423 O  O    . ASN   D 1 99  ? -79.508 8.401   32.258  1.00 22.50 ? 78  ASN   D O    1 
ATOM   6424 C  CB   . ASN   D 1 99  ? -79.808 8.570   29.065  1.00 22.21 ? 78  ASN   D CB   1 
ATOM   6425 C  CG   . ASN   D 1 99  ? -79.742 9.619   27.981  1.00 28.62 ? 78  ASN   D CG   1 
ATOM   6426 O  OD1  . ASN   D 1 99  ? -78.920 10.540  28.029  1.00 29.67 ? 78  ASN   D OD1  1 
ATOM   6427 N  ND2  . ASN   D 1 99  ? -80.605 9.486   26.983  1.00 33.80 ? 78  ASN   D ND2  1 
ATOM   6428 N  N    . SER   D 1 100 ? -78.991 6.469   31.182  1.00 20.04 ? 79  SER   D N    1 
ATOM   6429 C  CA   A SER   D 1 100 ? -79.444 5.596   32.255  0.60 20.43 ? 79  SER   D CA   1 
ATOM   6430 C  CA   B SER   D 1 100 ? -79.461 5.618   32.259  0.40 19.50 ? 79  SER   D CA   1 
ATOM   6431 C  C    . SER   D 1 100 ? -78.657 5.898   33.527  1.00 19.72 ? 79  SER   D C    1 
ATOM   6432 O  O    . SER   D 1 100 ? -79.187 5.833   34.628  1.00 22.07 ? 79  SER   D O    1 
ATOM   6433 C  CB   A SER   D 1 100 ? -79.383 4.119   31.883  0.60 20.27 ? 79  SER   D CB   1 
ATOM   6434 C  CB   B SER   D 1 100 ? -79.449 4.165   31.854  0.40 18.12 ? 79  SER   D CB   1 
ATOM   6435 O  OG   A SER   D 1 100 ? -78.066 3.591   31.988  0.60 22.66 ? 79  SER   D OG   1 
ATOM   6436 O  OG   B SER   D 1 100 ? -80.272 3.990   30.708  0.40 17.12 ? 79  SER   D OG   1 
ATOM   6437 N  N    . CYS   D 1 101 ? -77.382 6.273   33.369  1.00 18.98 ? 80  CYS   D N    1 
ATOM   6438 C  CA   . CYS   D 1 101 ? -76.552 6.558   34.529  1.00 18.77 ? 80  CYS   D CA   1 
ATOM   6439 C  C    . CYS   D 1 101 ? -76.993 7.877   35.160  1.00 19.91 ? 80  CYS   D C    1 
ATOM   6440 O  O    . CYS   D 1 101 ? -77.101 7.947   36.384  1.00 21.05 ? 80  CYS   D O    1 
ATOM   6441 C  CB   . CYS   D 1 101 ? -75.069 6.584   34.143  1.00 18.47 ? 80  CYS   D CB   1 
ATOM   6442 S  SG   . CYS   D 1 101 ? -73.926 6.496   35.552  1.00 20.57 ? 80  CYS   D SG   1 
ATOM   6443 N  N    . PHE   D 1 102 ? -77.251 8.890   34.320  1.00 20.62 ? 81  PHE   D N    1 
ATOM   6444 C  CA   . PHE   D 1 102 ? -77.720 10.174  34.821  1.00 22.22 ? 81  PHE   D CA   1 
ATOM   6445 C  C    . PHE   D 1 102 ? -79.103 10.013  35.457  1.00 24.43 ? 81  PHE   D C    1 
ATOM   6446 O  O    . PHE   D 1 102 ? -79.381 10.660  36.470  1.00 24.26 ? 81  PHE   D O    1 
ATOM   6447 C  CB   . PHE   D 1 102 ? -77.704 11.263  33.742  1.00 21.22 ? 81  PHE   D CB   1 
ATOM   6448 C  CG   . PHE   D 1 102 ? -76.312 11.823  33.494  1.00 23.60 ? 81  PHE   D CG   1 
ATOM   6449 C  CD1  . PHE   D 1 102 ? -75.452 11.220  32.581  1.00 20.90 ? 81  PHE   D CD1  1 
ATOM   6450 C  CD2  . PHE   D 1 102 ? -75.842 12.928  34.198  1.00 22.66 ? 81  PHE   D CD2  1 
ATOM   6451 C  CE1  . PHE   D 1 102 ? -74.171 11.714  32.375  1.00 22.89 ? 81  PHE   D CE1  1 
ATOM   6452 C  CE2  . PHE   D 1 102 ? -74.569 13.437  33.969  1.00 23.18 ? 81  PHE   D CE2  1 
ATOM   6453 C  CZ   . PHE   D 1 102 ? -73.726 12.824  33.069  1.00 23.46 ? 81  PHE   D CZ   1 
ATOM   6454 N  N    . ARG   D 1 103 ? -79.957 9.167   34.858  1.00 22.90 ? 82  ARG   D N    1 
ATOM   6455 C  CA   A ARG   D 1 103 ? -81.321 8.950   35.333  0.50 24.13 ? 82  ARG   D CA   1 
ATOM   6456 C  CA   B ARG   D 1 103 ? -81.318 8.983   35.342  0.50 24.64 ? 82  ARG   D CA   1 
ATOM   6457 C  C    . ARG   D 1 103 ? -81.293 8.346   36.735  1.00 24.32 ? 82  ARG   D C    1 
ATOM   6458 O  O    . ARG   D 1 103 ? -82.054 8.756   37.622  1.00 26.61 ? 82  ARG   D O    1 
ATOM   6459 C  CB   A ARG   D 1 103 ? -82.085 8.000   34.402  0.50 24.87 ? 82  ARG   D CB   1 
ATOM   6460 C  CB   B ARG   D 1 103 ? -82.098 8.195   34.282  0.50 26.27 ? 82  ARG   D CB   1 
ATOM   6461 C  CG   A ARG   D 1 103 ? -83.463 7.497   34.817  0.50 25.96 ? 82  ARG   D CG   1 
ATOM   6462 C  CG   B ARG   D 1 103 ? -83.620 8.238   34.296  0.50 28.61 ? 82  ARG   D CG   1 
ATOM   6463 C  CD   A ARG   D 1 103 ? -84.080 6.650   33.698  0.50 26.66 ? 82  ARG   D CD   1 
ATOM   6464 C  CD   B ARG   D 1 103 ? -84.211 7.643   33.018  0.50 28.01 ? 82  ARG   D CD   1 
ATOM   6465 N  NE   A ARG   D 1 103 ? -83.927 7.299   32.388  0.50 27.36 ? 82  ARG   D NE   1 
ATOM   6466 N  NE   B ARG   D 1 103 ? -83.824 6.247   32.770  0.50 27.09 ? 82  ARG   D NE   1 
ATOM   6467 C  CZ   A ARG   D 1 103 ? -83.354 6.760   31.312  0.50 25.86 ? 82  ARG   D CZ   1 
ATOM   6468 C  CZ   B ARG   D 1 103 ? -83.255 5.798   31.655  0.50 25.87 ? 82  ARG   D CZ   1 
ATOM   6469 N  NH1  A ARG   D 1 103 ? -83.031 5.479   31.296  0.50 25.74 ? 82  ARG   D NH1  1 
ATOM   6470 N  NH1  B ARG   D 1 103 ? -82.946 4.518   31.533  0.50 25.64 ? 82  ARG   D NH1  1 
ATOM   6471 N  NH2  A ARG   D 1 103 ? -83.132 7.501   30.238  0.50 25.70 ? 82  ARG   D NH2  1 
ATOM   6472 N  NH2  B ARG   D 1 103 ? -82.997 6.629   30.662  0.50 24.45 ? 82  ARG   D NH2  1 
ATOM   6473 N  N    . ALA   D 1 104 ? -80.425 7.346   36.928  1.00 22.56 ? 83  ALA   D N    1 
ATOM   6474 C  CA   . ALA   D 1 104 ? -80.298 6.652   38.200  1.00 22.93 ? 83  ALA   D CA   1 
ATOM   6475 C  C    . ALA   D 1 104 ? -79.580 7.485   39.262  1.00 22.34 ? 83  ALA   D C    1 
ATOM   6476 O  O    . ALA   D 1 104 ? -79.984 7.470   40.436  1.00 24.74 ? 83  ALA   D O    1 
ATOM   6477 C  CB   . ALA   D 1 104 ? -79.619 5.311   38.011  1.00 26.00 ? 83  ALA   D CB   1 
ATOM   6478 N  N    . PHE   D 1 105 ? -78.456 8.119   38.890  1.00 21.48 ? 84  PHE   D N    1 
ATOM   6479 C  CA   . PHE   D 1 105 ? -77.497 8.576   39.890  1.00 20.74 ? 84  PHE   D CA   1 
ATOM   6480 C  C    . PHE   D 1 105 ? -77.203 10.070  39.800  1.00 20.36 ? 84  PHE   D C    1 
ATOM   6481 O  O    . PHE   D 1 105 ? -76.553 10.627  40.686  1.00 24.27 ? 84  PHE   D O    1 
ATOM   6482 C  CB   . PHE   D 1 105 ? -76.183 7.802   39.734  1.00 20.52 ? 84  PHE   D CB   1 
ATOM   6483 C  CG   . PHE   D 1 105 ? -76.351 6.304   39.917  1.00 21.49 ? 84  PHE   D CG   1 
ATOM   6484 C  CD1  . PHE   D 1 105 ? -77.068 5.787   40.993  1.00 21.09 ? 84  PHE   D CD1  1 
ATOM   6485 C  CD2  . PHE   D 1 105 ? -75.844 5.414   38.978  1.00 19.37 ? 84  PHE   D CD2  1 
ATOM   6486 C  CE1  . PHE   D 1 105 ? -77.245 4.421   41.137  1.00 21.28 ? 84  PHE   D CE1  1 
ATOM   6487 C  CE2  . PHE   D 1 105 ? -76.009 4.047   39.141  1.00 20.28 ? 84  PHE   D CE2  1 
ATOM   6488 C  CZ   . PHE   D 1 105 ? -76.695 3.548   40.227  1.00 22.31 ? 84  PHE   D CZ   1 
ATOM   6489 N  N    . GLY   D 1 106 ? -77.635 10.714  38.717  1.00 20.95 ? 85  GLY   D N    1 
ATOM   6490 C  CA   . GLY   D 1 106 ? -77.492 12.158  38.583  1.00 20.89 ? 85  GLY   D CA   1 
ATOM   6491 C  C    . GLY   D 1 106 ? -76.112 12.612  38.097  1.00 24.12 ? 85  GLY   D C    1 
ATOM   6492 O  O    . GLY   D 1 106 ? -75.833 13.811  38.024  1.00 25.38 ? 85  GLY   D O    1 
ATOM   6493 N  N    . ARG   D 1 107 ? -75.258 11.649  37.739  1.00 22.18 ? 86  ARG   D N    1 
ATOM   6494 C  CA   . ARG   D 1 107 ? -73.901 11.952  37.308  1.00 21.61 ? 86  ARG   D CA   1 
ATOM   6495 C  C    . ARG   D 1 107 ? -73.327 10.705  36.646  1.00 19.99 ? 86  ARG   D C    1 
ATOM   6496 O  O    . ARG   D 1 107 ? -73.873 9.614   36.815  1.00 20.08 ? 86  ARG   D O    1 
ATOM   6497 C  CB   . ARG   D 1 107 ? -73.039 12.346  38.516  1.00 22.11 ? 86  ARG   D CB   1 
ATOM   6498 C  CG   . ARG   D 1 107 ? -72.974 11.266  39.590  1.00 23.11 ? 86  ARG   D CG   1 
ATOM   6499 C  CD   . ARG   D 1 107 ? -72.304 11.757  40.863  1.00 23.35 ? 86  ARG   D CD   1 
ATOM   6500 N  NE   . ARG   D 1 107 ? -70.892 12.126  40.704  1.00 23.34 ? 86  ARG   D NE   1 
ATOM   6501 C  CZ   . ARG   D 1 107 ? -70.132 12.723  41.610  1.00 26.87 ? 86  ARG   D CZ   1 
ATOM   6502 N  NH1  . ARG   D 1 107 ? -70.676 13.182  42.729  1.00 30.67 ? 86  ARG   D NH1  1 
ATOM   6503 N  NH2  . ARG   D 1 107 ? -68.838 12.901  41.379  1.00 28.17 ? 86  ARG   D NH2  1 
ATOM   6504 N  N    . CYS   D 1 108 ? -72.224 10.887  35.902  1.00 19.91 ? 87  CYS   D N    1 
ATOM   6505 C  CA   . CYS   D 1 108 ? -71.531 9.749   35.318  1.00 18.87 ? 87  CYS   D CA   1 
ATOM   6506 C  C    . CYS   D 1 108 ? -70.050 10.106  35.297  1.00 19.22 ? 87  CYS   D C    1 
ATOM   6507 O  O    . CYS   D 1 108 ? -69.640 11.006  34.574  1.00 20.44 ? 87  CYS   D O    1 
ATOM   6508 C  CB   . CYS   D 1 108 ? -72.022 9.496   33.897  1.00 20.08 ? 87  CYS   D CB   1 
ATOM   6509 S  SG   . CYS   D 1 108 ? -71.340 7.973   33.186  1.00 22.03 ? 87  CYS   D SG   1 
ATOM   6510 N  N    . ASP   D 1 109 ? -69.273 9.452   36.166  1.00 17.85 ? 88  ASP   D N    1 
ATOM   6511 C  CA   . ASP   D 1 109 ? -67.890 9.855   36.333  1.00 17.84 ? 88  ASP   D CA   1 
ATOM   6512 C  C    . ASP   D 1 109 ? -66.945 8.935   35.573  1.00 17.36 ? 88  ASP   D C    1 
ATOM   6513 O  O    . ASP   D 1 109 ? -65.858 9.365   35.215  1.00 16.80 ? 88  ASP   D O    1 
ATOM   6514 C  CB   . ASP   D 1 109 ? -67.549 9.773   37.808  1.00 19.60 ? 88  ASP   D CB   1 
ATOM   6515 C  CG   . ASP   D 1 109 ? -68.410 10.719  38.629  1.00 21.70 ? 88  ASP   D CG   1 
ATOM   6516 O  OD1  . ASP   D 1 109 ? -67.970 11.877  38.778  1.00 23.18 ? 88  ASP   D OD1  1 
ATOM   6517 O  OD2  . ASP   D 1 109 ? -69.526 10.306  39.028  1.00 21.76 ? 88  ASP   D OD2  1 
ATOM   6518 N  N    . VAL   D 1 110 ? -67.343 7.671   35.406  1.00 17.87 ? 89  VAL   D N    1 
ATOM   6519 C  CA   . VAL   D 1 110 ? -66.470 6.655   34.835  1.00 17.32 ? 89  VAL   D CA   1 
ATOM   6520 C  C    . VAL   D 1 110 ? -67.239 5.828   33.811  1.00 17.20 ? 89  VAL   D C    1 
ATOM   6521 O  O    . VAL   D 1 110 ? -68.365 5.410   34.071  1.00 16.18 ? 89  VAL   D O    1 
ATOM   6522 C  CB   . VAL   D 1 110 ? -65.868 5.749   35.928  1.00 16.75 ? 89  VAL   D CB   1 
ATOM   6523 C  CG1  . VAL   D 1 110 ? -65.235 4.492   35.341  1.00 17.03 ? 89  VAL   D CG1  1 
ATOM   6524 C  CG2  . VAL   D 1 110 ? -64.846 6.495   36.785  1.00 18.52 ? 89  VAL   D CG2  1 
ATOM   6525 N  N    . LEU   D 1 111 ? -66.585 5.578   32.663  1.00 15.75 ? 90  LEU   D N    1 
ATOM   6526 C  CA   . LEU   D 1 111 ? -67.091 4.684   31.630  1.00 14.58 ? 90  LEU   D CA   1 
ATOM   6527 C  C    . LEU   D 1 111 ? -66.055 3.596   31.409  1.00 14.03 ? 90  LEU   D C    1 
ATOM   6528 O  O    . LEU   D 1 111 ? -64.907 3.937   31.155  1.00 14.74 ? 90  LEU   D O    1 
ATOM   6529 C  CB   . LEU   D 1 111 ? -67.319 5.459   30.328  1.00 14.46 ? 90  LEU   D CB   1 
ATOM   6530 C  CG   . LEU   D 1 111 ? -67.594 4.623   29.071  1.00 15.59 ? 90  LEU   D CG   1 
ATOM   6531 C  CD1  . LEU   D 1 111 ? -68.900 3.844   29.192  1.00 16.99 ? 90  LEU   D CD1  1 
ATOM   6532 C  CD2  . LEU   D 1 111 ? -67.617 5.503   27.842  1.00 16.17 ? 90  LEU   D CD2  1 
ATOM   6533 N  N    . VAL   D 1 112 ? -66.462 2.326   31.542  1.00 14.33 ? 91  VAL   D N    1 
ATOM   6534 C  CA   . VAL   D 1 112 ? -65.583 1.204   31.224  1.00 14.96 ? 91  VAL   D CA   1 
ATOM   6535 C  C    . VAL   D 1 112 ? -66.168 0.475   30.018  1.00 14.99 ? 91  VAL   D C    1 
ATOM   6536 O  O    . VAL   D 1 112 ? -67.263 -0.087  30.101  1.00 15.46 ? 91  VAL   D O    1 
ATOM   6537 C  CB   . VAL   D 1 112 ? -65.391 0.251   32.420  1.00 15.58 ? 91  VAL   D CB   1 
ATOM   6538 C  CG1  . VAL   D 1 112 ? -64.428 -0.878  32.031  1.00 17.42 ? 91  VAL   D CG1  1 
ATOM   6539 C  CG2  . VAL   D 1 112 ? -64.880 1.020   33.640  1.00 17.27 ? 91  VAL   D CG2  1 
ATOM   6540 N  N    . ASN   D 1 113 ? -65.447 0.546   28.884  1.00 14.43 ? 92  ASN   D N    1 
ATOM   6541 C  CA   . ASN   D 1 113 ? -65.848 -0.128  27.658  1.00 13.64 ? 92  ASN   D CA   1 
ATOM   6542 C  C    . ASN   D 1 113 ? -65.298 -1.551  27.679  1.00 14.73 ? 92  ASN   D C    1 
ATOM   6543 O  O    . ASN   D 1 113 ? -64.153 -1.792  27.259  1.00 15.32 ? 92  ASN   D O    1 
ATOM   6544 C  CB   . ASN   D 1 113 ? -65.366 0.653   26.442  1.00 14.39 ? 92  ASN   D CB   1 
ATOM   6545 C  CG   . ASN   D 1 113 ? -66.164 1.920   26.219  1.00 16.15 ? 92  ASN   D CG   1 
ATOM   6546 O  OD1  . ASN   D 1 113 ? -67.394 1.851   26.092  1.00 16.60 ? 92  ASN   D OD1  1 
ATOM   6547 N  ND2  . ASN   D 1 113 ? -65.512 3.069   26.120  1.00 15.39 ? 92  ASN   D ND2  1 
ATOM   6548 N  N    . ASN   D 1 114 ? -66.114 -2.484  28.163  1.00 13.88 ? 93  ASN   D N    1 
ATOM   6549 C  CA   . ASN   D 1 114 ? -65.694 -3.861  28.387  1.00 14.67 ? 93  ASN   D CA   1 
ATOM   6550 C  C    . ASN   D 1 114 ? -66.391 -4.831  27.426  1.00 16.20 ? 93  ASN   D C    1 
ATOM   6551 O  O    . ASN   D 1 114 ? -65.813 -5.850  27.050  1.00 16.74 ? 93  ASN   D O    1 
ATOM   6552 C  CB   . ASN   D 1 114 ? -65.938 -4.254  29.848  1.00 15.87 ? 93  ASN   D CB   1 
ATOM   6553 C  CG   . ASN   D 1 114 ? -65.800 -5.738  30.082  1.00 16.41 ? 93  ASN   D CG   1 
ATOM   6554 O  OD1  . ASN   D 1 114 ? -64.691 -6.229  30.295  1.00 17.31 ? 93  ASN   D OD1  1 
ATOM   6555 N  ND2  . ASN   D 1 114 ? -66.921 -6.452  30.078  1.00 17.28 ? 93  ASN   D ND2  1 
ATOM   6556 N  N    . ALA   D 1 115 ? -67.654 -4.572  27.045  1.00 15.28 ? 94  ALA   D N    1 
ATOM   6557 C  CA   . ALA   D 1 115 ? -68.419 -5.517  26.233  1.00 16.66 ? 94  ALA   D CA   1 
ATOM   6558 C  C    . ALA   D 1 115 ? -67.696 -5.782  24.912  1.00 17.45 ? 94  ALA   D C    1 
ATOM   6559 O  O    . ALA   D 1 115 ? -67.129 -4.883  24.309  1.00 18.36 ? 94  ALA   D O    1 
ATOM   6560 C  CB   . ALA   D 1 115 ? -69.811 -4.984  25.959  1.00 16.33 ? 94  ALA   D CB   1 
ATOM   6561 N  N    . SER   D 1 116 ? -67.759 -7.029  24.444  1.00 18.03 ? 95  SER   D N    1 
ATOM   6562 C  CA   . SER   D 1 116 ? -66.946 -7.416  23.309  1.00 19.09 ? 95  SER   D CA   1 
ATOM   6563 C  C    . SER   D 1 116 ? -67.458 -8.719  22.709  1.00 19.50 ? 95  SER   D C    1 
ATOM   6564 O  O    . SER   D 1 116 ? -67.672 -9.694  23.433  1.00 21.16 ? 95  SER   D O    1 
ATOM   6565 C  CB   . SER   D 1 116 ? -65.530 -7.593  23.755  1.00 19.56 ? 95  SER   D CB   1 
ATOM   6566 O  OG   . SER   D 1 116 ? -64.767 -8.180  22.703  1.00 20.01 ? 95  SER   D OG   1 
ATOM   6567 N  N    . ALA   D 1 117 ? -67.633 -8.710  21.384  1.00 17.71 ? 96  ALA   D N    1 
ATOM   6568 C  CA   . ALA   D 1 117 ? -67.832 -9.921  20.609  1.00 16.40 ? 96  ALA   D CA   1 
ATOM   6569 C  C    . ALA   D 1 117 ? -66.461 -10.467 20.210  1.00 17.42 ? 96  ALA   D C    1 
ATOM   6570 O  O    . ALA   D 1 117 ? -65.535 -9.703  19.929  1.00 17.64 ? 96  ALA   D O    1 
ATOM   6571 C  CB   . ALA   D 1 117 ? -68.658 -9.611  19.385  1.00 18.34 ? 96  ALA   D CB   1 
ATOM   6572 N  N    . PHE   D 1 118 ? -66.340 -11.802 20.212  1.00 17.73 ? 97  PHE   D N    1 
ATOM   6573 C  CA   . PHE   D 1 118 ? -65.069 -12.461 19.970  1.00 18.42 ? 97  PHE   D CA   1 
ATOM   6574 C  C    . PHE   D 1 118 ? -65.331 -13.835 19.362  1.00 18.87 ? 97  PHE   D C    1 
ATOM   6575 O  O    . PHE   D 1 118 ? -65.803 -14.753 20.035  1.00 22.00 ? 97  PHE   D O    1 
ATOM   6576 C  CB   . PHE   D 1 118 ? -64.282 -12.602 21.278  1.00 19.51 ? 97  PHE   D CB   1 
ATOM   6577 C  CG   . PHE   D 1 118 ? -62.991 -13.411 21.226  1.00 21.46 ? 97  PHE   D CG   1 
ATOM   6578 C  CD1  . PHE   D 1 118 ? -61.881 -12.919 20.550  1.00 22.26 ? 97  PHE   D CD1  1 
ATOM   6579 C  CD2  . PHE   D 1 118 ? -62.869 -14.642 21.863  1.00 24.41 ? 97  PHE   D CD2  1 
ATOM   6580 C  CE1  . PHE   D 1 118 ? -60.683 -13.616 20.500  1.00 23.81 ? 97  PHE   D CE1  1 
ATOM   6581 C  CE2  . PHE   D 1 118 ? -61.663 -15.338 21.818  1.00 26.09 ? 97  PHE   D CE2  1 
ATOM   6582 C  CZ   . PHE   D 1 118 ? -60.576 -14.838 21.128  1.00 24.64 ? 97  PHE   D CZ   1 
ATOM   6583 N  N    . TYR   D 1 119 ? -65.049 -13.946 18.070  1.00 17.50 ? 98  TYR   D N    1 
ATOM   6584 C  CA   . TYR   D 1 119 ? -65.193 -15.199 17.348  1.00 18.04 ? 98  TYR   D CA   1 
ATOM   6585 C  C    . TYR   D 1 119 ? -64.440 -15.079 16.034  1.00 18.89 ? 98  TYR   D C    1 
ATOM   6586 O  O    . TYR   D 1 119 ? -64.175 -13.975 15.546  1.00 17.31 ? 98  TYR   D O    1 
ATOM   6587 C  CB   . TYR   D 1 119 ? -66.654 -15.589 17.105  1.00 18.29 ? 98  TYR   D CB   1 
ATOM   6588 C  CG   . TYR   D 1 119 ? -67.526 -14.544 16.430  1.00 17.59 ? 98  TYR   D CG   1 
ATOM   6589 C  CD1  . TYR   D 1 119 ? -67.538 -14.388 15.049  1.00 17.54 ? 98  TYR   D CD1  1 
ATOM   6590 C  CD2  . TYR   D 1 119 ? -68.415 -13.780 17.185  1.00 18.75 ? 98  TYR   D CD2  1 
ATOM   6591 C  CE1  . TYR   D 1 119 ? -68.376 -13.458 14.449  1.00 19.67 ? 98  TYR   D CE1  1 
ATOM   6592 C  CE2  . TYR   D 1 119 ? -69.244 -12.836 16.602  1.00 18.67 ? 98  TYR   D CE2  1 
ATOM   6593 C  CZ   . TYR   D 1 119 ? -69.228 -12.689 15.224  1.00 18.48 ? 98  TYR   D CZ   1 
ATOM   6594 O  OH   . TYR   D 1 119 ? -70.052 -11.773 14.639  1.00 20.70 ? 98  TYR   D OH   1 
ATOM   6595 N  N    . PRO   D 1 120 ? -64.034 -16.214 15.437  1.00 18.29 ? 99  PRO   D N    1 
ATOM   6596 C  CA   . PRO   D 1 120 ? -63.327 -16.170 14.167  1.00 18.76 ? 99  PRO   D CA   1 
ATOM   6597 C  C    . PRO   D 1 120 ? -64.199 -15.729 12.997  1.00 18.42 ? 99  PRO   D C    1 
ATOM   6598 O  O    . PRO   D 1 120 ? -65.402 -16.005 12.943  1.00 18.92 ? 99  PRO   D O    1 
ATOM   6599 C  CB   . PRO   D 1 120 ? -62.770 -17.570 13.964  1.00 20.72 ? 99  PRO   D CB   1 
ATOM   6600 C  CG   . PRO   D 1 120 ? -63.677 -18.442 14.804  1.00 20.49 ? 99  PRO   D CG   1 
ATOM   6601 C  CD   . PRO   D 1 120 ? -64.206 -17.588 15.945  1.00 20.59 ? 99  PRO   D CD   1 
ATOM   6602 N  N    . THR   D 1 121 ? -63.530 -15.048 12.061  1.00 17.80 ? 100 THR   D N    1 
ATOM   6603 C  CA   . THR   D 1 121 ? -64.090 -14.567 10.810  1.00 17.57 ? 100 THR   D CA   1 
ATOM   6604 C  C    . THR   D 1 121 ? -63.072 -14.855 9.705   1.00 18.87 ? 100 THR   D C    1 
ATOM   6605 O  O    . THR   D 1 121 ? -62.343 -13.964 9.273   1.00 18.54 ? 100 THR   D O    1 
ATOM   6606 C  CB   . THR   D 1 121 ? -64.444 -13.075 10.914  1.00 17.05 ? 100 THR   D CB   1 
ATOM   6607 O  OG1  . THR   D 1 121 ? -63.251 -12.339 11.209  1.00 18.25 ? 100 THR   D OG1  1 
ATOM   6608 C  CG2  . THR   D 1 121 ? -65.510 -12.786 11.963  1.00 18.24 ? 100 THR   D CG2  1 
ATOM   6609 N  N    . PRO   D 1 122 ? -62.946 -16.114 9.216   1.00 18.40 ? 101 PRO   D N    1 
ATOM   6610 C  CA   . PRO   D 1 122 ? -61.921 -16.453 8.226   1.00 19.04 ? 101 PRO   D CA   1 
ATOM   6611 C  C    . PRO   D 1 122 ? -62.074 -15.640 6.945   1.00 19.72 ? 101 PRO   D C    1 
ATOM   6612 O  O    . PRO   D 1 122 ? -63.185 -15.347 6.522   1.00 20.56 ? 101 PRO   D O    1 
ATOM   6613 C  CB   . PRO   D 1 122 ? -62.070 -17.977 7.959   1.00 20.95 ? 101 PRO   D CB   1 
ATOM   6614 C  CG   . PRO   D 1 122 ? -63.019 -18.451 9.024   1.00 22.73 ? 101 PRO   D CG   1 
ATOM   6615 C  CD   . PRO   D 1 122 ? -63.775 -17.270 9.590   1.00 21.38 ? 101 PRO   D CD   1 
ATOM   6616 N  N    . LEU   D 1 123 ? -60.938 -15.294 6.331   1.00 19.59 ? 102 LEU   D N    1 
ATOM   6617 C  CA   . LEU   D 1 123 ? -60.948 -14.569 5.073   1.00 19.52 ? 102 LEU   D CA   1 
ATOM   6618 C  C    . LEU   D 1 123 ? -61.286 -15.493 3.907   1.00 22.58 ? 102 LEU   D C    1 
ATOM   6619 O  O    . LEU   D 1 123 ? -61.758 -15.009 2.880   1.00 24.75 ? 102 LEU   D O    1 
ATOM   6620 C  CB   . LEU   D 1 123 ? -59.574 -13.939 4.865   1.00 19.34 ? 102 LEU   D CB   1 
ATOM   6621 C  CG   . LEU   D 1 123 ? -59.197 -12.801 5.816   1.00 20.21 ? 102 LEU   D CG   1 
ATOM   6622 C  CD1  . LEU   D 1 123 ? -57.732 -12.425 5.661   1.00 22.50 ? 102 LEU   D CD1  1 
ATOM   6623 C  CD2  . LEU   D 1 123 ? -60.047 -11.614 5.467   1.00 21.41 ? 102 LEU   D CD2  1 
ATOM   6624 N  N    . VAL   D 1 124 ? -60.975 -16.789 4.042   1.00 25.41 ? 103 VAL   D N    1 
ATOM   6625 C  CA   . VAL   D 1 124 ? -61.146 -17.741 2.948   1.00 30.16 ? 103 VAL   D CA   1 
ATOM   6626 C  C    . VAL   D 1 124 ? -62.029 -18.882 3.446   1.00 36.19 ? 103 VAL   D C    1 
ATOM   6627 O  O    . VAL   D 1 124 ? -61.799 -19.402 4.534   1.00 36.77 ? 103 VAL   D O    1 
ATOM   6628 C  CB   . VAL   D 1 124 ? -59.807 -18.237 2.361   1.00 30.32 ? 103 VAL   D CB   1 
ATOM   6629 C  CG1  . VAL   D 1 124 ? -59.981 -19.320 1.299   1.00 31.00 ? 103 VAL   D CG1  1 
ATOM   6630 C  CG2  . VAL   D 1 124 ? -58.994 -17.092 1.767   1.00 31.20 ? 103 VAL   D CG2  1 
ATOM   6631 N  N    . GLN   D 1 125 ? -63.039 -19.238 2.639   0.70 38.67 ? 104 GLN   D N    1 
ATOM   6632 C  CA   . GLN   D 1 125 ? -64.065 -20.197 3.021   0.70 42.99 ? 104 GLN   D CA   1 
ATOM   6633 C  C    . GLN   D 1 125 ? -63.639 -21.612 2.594   0.70 45.59 ? 104 GLN   D C    1 
ATOM   6634 O  O    . GLN   D 1 125 ? -62.420 -21.885 2.658   0.70 48.23 ? 104 GLN   D O    1 
ATOM   6635 C  CB   . GLN   D 1 125 ? -65.408 -19.821 2.393   0.70 42.94 ? 104 GLN   D CB   1 
ATOM   6636 N  N    . GLY   D 1 134 ? -73.088 -19.518 10.922  0.70 44.81 ? 113 GLY   D N    1 
ATOM   6637 C  CA   . GLY   D 1 134 ? -74.326 -19.212 10.179  0.70 43.19 ? 113 GLY   D CA   1 
ATOM   6638 C  C    . GLY   D 1 134 ? -74.502 -17.713 9.944   0.70 40.41 ? 113 GLY   D C    1 
ATOM   6639 O  O    . GLY   D 1 134 ? -75.452 -17.298 9.284   0.70 41.59 ? 113 GLY   D O    1 
ATOM   6640 N  N    . LYS   D 1 135 ? -73.579 -16.905 10.479  1.00 38.51 ? 114 LYS   D N    1 
ATOM   6641 C  CA   . LYS   D 1 135 ? -73.712 -15.456 10.410  1.00 33.99 ? 114 LYS   D CA   1 
ATOM   6642 C  C    . LYS   D 1 135 ? -73.167 -14.939 9.082   1.00 29.45 ? 114 LYS   D C    1 
ATOM   6643 O  O    . LYS   D 1 135 ? -72.121 -15.391 8.633   1.00 29.25 ? 114 LYS   D O    1 
ATOM   6644 C  CB   . LYS   D 1 135 ? -72.939 -14.780 11.548  1.00 33.12 ? 114 LYS   D CB   1 
ATOM   6645 C  CG   . LYS   D 1 135 ? -73.463 -15.102 12.933  1.00 35.46 ? 114 LYS   D CG   1 
ATOM   6646 C  CD   . LYS   D 1 135 ? -72.934 -14.125 13.970  1.00 37.63 ? 114 LYS   D CD   1 
ATOM   6647 C  CE   . LYS   D 1 135 ? -73.116 -14.707 15.329  1.00 37.42 ? 114 LYS   D CE   1 
ATOM   6648 N  NZ   . LYS   D 1 135 ? -72.801 -13.756 16.389  1.00 39.59 ? 114 LYS   D NZ   1 
ATOM   6649 N  N    . THR   D 1 136 ? -73.871 -13.965 8.492   1.00 26.49 ? 115 THR   D N    1 
ATOM   6650 C  CA   . THR   D 1 136 ? -73.440 -13.302 7.271   1.00 25.40 ? 115 THR   D CA   1 
ATOM   6651 C  C    . THR   D 1 136 ? -72.235 -12.419 7.585   1.00 22.45 ? 115 THR   D C    1 
ATOM   6652 O  O    . THR   D 1 136 ? -72.032 -12.054 8.743   1.00 22.76 ? 115 THR   D O    1 
ATOM   6653 C  CB   . THR   D 1 136 ? -74.562 -12.446 6.686   1.00 27.01 ? 115 THR   D CB   1 
ATOM   6654 O  OG1  . THR   D 1 136 ? -74.834 -11.357 7.563   1.00 26.87 ? 115 THR   D OG1  1 
ATOM   6655 C  CG2  . THR   D 1 136 ? -75.835 -13.240 6.442   1.00 29.67 ? 115 THR   D CG2  1 
ATOM   6656 N  N    . VAL   D 1 137 ? -71.490 -12.055 6.540   1.00 21.06 ? 116 VAL   D N    1 
ATOM   6657 C  CA   A VAL   D 1 137 ? -70.318 -11.212 6.731   0.50 21.12 ? 116 VAL   D CA   1 
ATOM   6658 C  CA   B VAL   D 1 137 ? -70.323 -11.199 6.693   0.50 21.66 ? 116 VAL   D CA   1 
ATOM   6659 C  C    . VAL   D 1 137 ? -70.775 -9.841  7.230   1.00 21.75 ? 116 VAL   D C    1 
ATOM   6660 O  O    . VAL   D 1 137 ? -70.088 -9.225  8.054   1.00 20.22 ? 116 VAL   D O    1 
ATOM   6661 C  CB   A VAL   D 1 137 ? -69.334 -11.126 5.544   0.50 20.63 ? 116 VAL   D CB   1 
ATOM   6662 C  CB   B VAL   D 1 137 ? -69.593 -11.097 5.341   0.50 21.98 ? 116 VAL   D CB   1 
ATOM   6663 C  CG1  A VAL   D 1 137 ? -69.908 -10.366 4.351   0.50 22.39 ? 116 VAL   D CG1  1 
ATOM   6664 C  CG1  B VAL   D 1 137 ? -68.483 -10.055 5.364   0.50 22.28 ? 116 VAL   D CG1  1 
ATOM   6665 C  CG2  A VAL   D 1 137 ? -67.985 -10.549 5.965   0.50 19.55 ? 116 VAL   D CG2  1 
ATOM   6666 C  CG2  B VAL   D 1 137 ? -69.057 -12.455 4.900   0.50 22.93 ? 116 VAL   D CG2  1 
ATOM   6667 N  N    . GLU   D 1 138 ? -71.952 -9.387  6.777   1.00 21.63 ? 117 GLU   D N    1 
ATOM   6668 C  CA   . GLU   D 1 138 ? -72.531 -8.130  7.252   1.00 22.01 ? 117 GLU   D CA   1 
ATOM   6669 C  C    . GLU   D 1 138 ? -72.674 -8.156  8.776   1.00 19.63 ? 117 GLU   D C    1 
ATOM   6670 O  O    . GLU   D 1 138 ? -72.298 -7.200  9.461   1.00 18.54 ? 117 GLU   D O    1 
ATOM   6671 C  CB   . GLU   D 1 138 ? -73.902 -7.819  6.632   1.00 23.59 ? 117 GLU   D CB   1 
ATOM   6672 C  CG   . GLU   D 1 138 ? -73.882 -7.583  5.124   0.70 26.04 ? 117 GLU   D CG   1 
ATOM   6673 C  CD   . GLU   D 1 138 ? -73.758 -8.789  4.206   0.70 27.52 ? 117 GLU   D CD   1 
ATOM   6674 O  OE1  . GLU   D 1 138 ? -73.703 -8.598  2.971   0.70 33.57 ? 117 GLU   D OE1  1 
ATOM   6675 O  OE2  . GLU   D 1 138 ? -73.723 -9.922  4.708   0.70 26.22 ? 117 GLU   D OE2  1 
ATOM   6676 N  N    . THR   D 1 139 ? -73.200 -9.264  9.309   1.00 19.39 ? 118 THR   D N    1 
ATOM   6677 C  CA   . THR   D 1 139 ? -73.436 -9.399  10.737  1.00 20.96 ? 118 THR   D CA   1 
ATOM   6678 C  C    . THR   D 1 139 ? -72.099 -9.442  11.478  1.00 18.42 ? 118 THR   D C    1 
ATOM   6679 O  O    . THR   D 1 139 ? -71.976 -8.878  12.567  1.00 18.78 ? 118 THR   D O    1 
ATOM   6680 C  CB   . THR   D 1 139 ? -74.242 -10.669 11.036  1.00 23.92 ? 118 THR   D CB   1 
ATOM   6681 O  OG1  . THR   D 1 139 ? -75.554 -10.361 10.581  1.00 26.31 ? 118 THR   D OG1  1 
ATOM   6682 C  CG2  . THR   D 1 139 ? -74.345 -10.938 12.527  1.00 25.57 ? 118 THR   D CG2  1 
ATOM   6683 N  N    . GLN   D 1 140 ? -71.137 -10.193 10.923  1.00 18.45 ? 119 GLN   D N    1 
ATOM   6684 C  CA   A GLN   D 1 140 ? -69.813 -10.354 11.521  0.70 17.85 ? 119 GLN   D CA   1 
ATOM   6685 C  CA   B GLN   D 1 140 ? -69.834 -10.344 11.553  0.30 17.41 ? 119 GLN   D CA   1 
ATOM   6686 C  C    . GLN   D 1 140 ? -69.172 -8.975  11.698  1.00 16.73 ? 119 GLN   D C    1 
ATOM   6687 O  O    . GLN   D 1 140 ? -68.630 -8.671  12.762  1.00 16.21 ? 119 GLN   D O    1 
ATOM   6688 C  CB   A GLN   D 1 140 ? -68.943 -11.203 10.590  0.70 18.27 ? 119 GLN   D CB   1 
ATOM   6689 C  CB   B GLN   D 1 140 ? -68.981 -11.359 10.793  0.30 17.37 ? 119 GLN   D CB   1 
ATOM   6690 C  CG   A GLN   D 1 140 ? -69.279 -12.694 10.524  0.70 20.27 ? 119 GLN   D CG   1 
ATOM   6691 C  CG   B GLN   D 1 140 ? -69.578 -12.763 10.792  0.30 17.32 ? 119 GLN   D CG   1 
ATOM   6692 C  CD   A GLN   D 1 140 ? -68.595 -13.382 9.360   0.70 20.38 ? 119 GLN   D CD   1 
ATOM   6693 C  CD   B GLN   D 1 140 ? -68.682 -13.802 10.158  0.30 17.33 ? 119 GLN   D CD   1 
ATOM   6694 O  OE1  A GLN   D 1 140 ? -67.447 -13.078 9.002   0.70 23.46 ? 119 GLN   D OE1  1 
ATOM   6695 O  OE1  B GLN   D 1 140 ? -67.596 -13.506 9.649   0.30 17.73 ? 119 GLN   D OE1  1 
ATOM   6696 N  NE2  A GLN   D 1 140 ? -69.302 -14.295 8.710   0.70 24.72 ? 119 GLN   D NE2  1 
ATOM   6697 N  NE2  B GLN   D 1 140 ? -69.123 -15.050 10.203  0.30 18.33 ? 119 GLN   D NE2  1 
ATOM   6698 N  N    . VAL   D 1 141 ? -69.216 -8.166  10.634  1.00 16.55 ? 120 VAL   D N    1 
ATOM   6699 C  CA   . VAL   D 1 141 ? -68.679 -6.811  10.680  1.00 15.88 ? 120 VAL   D CA   1 
ATOM   6700 C  C    . VAL   D 1 141 ? -69.400 -6.006  11.759  1.00 15.68 ? 120 VAL   D C    1 
ATOM   6701 O  O    . VAL   D 1 141 ? -68.761 -5.385  12.618  1.00 14.92 ? 120 VAL   D O    1 
ATOM   6702 C  CB   . VAL   D 1 141 ? -68.782 -6.115  9.313   1.00 17.06 ? 120 VAL   D CB   1 
ATOM   6703 C  CG1  . VAL   D 1 141 ? -68.521 -4.611  9.395   1.00 16.68 ? 120 VAL   D CG1  1 
ATOM   6704 C  CG2  . VAL   D 1 141 ? -67.849 -6.747  8.282   1.00 16.95 ? 120 VAL   D CG2  1 
ATOM   6705 N  N    . ALA   D 1 142 ? -70.739 -6.018  11.705  1.00 15.87 ? 121 ALA   D N    1 
ATOM   6706 C  CA   . ALA   D 1 142 ? -71.525 -5.211  12.623  1.00 16.49 ? 121 ALA   D CA   1 
ATOM   6707 C  C    . ALA   D 1 142 ? -71.237 -5.551  14.086  1.00 15.19 ? 121 ALA   D C    1 
ATOM   6708 O  O    . ALA   D 1 142 ? -71.088 -4.664  14.923  1.00 15.03 ? 121 ALA   D O    1 
ATOM   6709 C  CB   . ALA   D 1 142 ? -73.001 -5.389  12.318  1.00 14.96 ? 121 ALA   D CB   1 
ATOM   6710 N  N    . GLU   D 1 143 ? -71.181 -6.846  14.397  1.00 15.67 ? 122 GLU   D N    1 
ATOM   6711 C  CA   . GLU   D 1 143 ? -70.968 -7.309  15.756  1.00 16.07 ? 122 GLU   D CA   1 
ATOM   6712 C  C    . GLU   D 1 143 ? -69.550 -7.012  16.248  1.00 16.23 ? 122 GLU   D C    1 
ATOM   6713 O  O    . GLU   D 1 143 ? -69.367 -6.498  17.353  1.00 15.61 ? 122 GLU   D O    1 
ATOM   6714 C  CB   . GLU   D 1 143 ? -71.278 -8.800  15.888  1.00 17.12 ? 122 GLU   D CB   1 
ATOM   6715 C  CG   . GLU   D 1 143 ? -72.780 -9.064  15.756  1.00 20.06 ? 122 GLU   D CG   1 
ATOM   6716 C  CD   . GLU   D 1 143 ? -73.200 -10.500 16.004  1.00 22.56 ? 122 GLU   D CD   1 
ATOM   6717 O  OE1  . GLU   D 1 143 ? -72.311 -11.368 16.040  1.00 23.78 ? 122 GLU   D OE1  1 
ATOM   6718 O  OE2  . GLU   D 1 143 ? -74.426 -10.745 16.182  1.00 23.76 ? 122 GLU   D OE2  1 
ATOM   6719 N  N    . LEU   D 1 144 ? -68.555 -7.382  15.444  1.00 15.14 ? 123 LEU   D N    1 
ATOM   6720 C  CA   . LEU   D 1 144 ? -67.181 -7.333  15.909  1.00 15.21 ? 123 LEU   D CA   1 
ATOM   6721 C  C    . LEU   D 1 144 ? -66.658 -5.900  15.922  1.00 15.02 ? 123 LEU   D C    1 
ATOM   6722 O  O    . LEU   D 1 144 ? -66.002 -5.502  16.891  1.00 14.98 ? 123 LEU   D O    1 
ATOM   6723 C  CB   . LEU   D 1 144 ? -66.304 -8.300  15.112  1.00 15.44 ? 123 LEU   D CB   1 
ATOM   6724 C  CG   . LEU   D 1 144 ? -66.595 -9.773  15.426  1.00 18.61 ? 123 LEU   D CG   1 
ATOM   6725 C  CD1  . LEU   D 1 144 ? -66.041 -10.604 14.309  1.00 20.00 ? 123 LEU   D CD1  1 
ATOM   6726 C  CD2  . LEU   D 1 144 ? -65.958 -10.177 16.758  1.00 20.77 ? 123 LEU   D CD2  1 
ATOM   6727 N  N    . ILE   D 1 145 ? -66.950 -5.157  14.855  1.00 15.13 ? 124 ILE   D N    1 
ATOM   6728 C  CA   . ILE   D 1 145 ? -66.519 -3.772  14.803  1.00 14.95 ? 124 ILE   D CA   1 
ATOM   6729 C  C    . ILE   D 1 145 ? -67.427 -2.908  15.682  1.00 16.85 ? 124 ILE   D C    1 
ATOM   6730 O  O    . ILE   D 1 145 ? -66.959 -1.967  16.324  1.00 15.79 ? 124 ILE   D O    1 
ATOM   6731 C  CB   . ILE   D 1 145 ? -66.429 -3.292  13.345  1.00 15.15 ? 124 ILE   D CB   1 
ATOM   6732 C  CG1  . ILE   D 1 145 ? -65.547 -4.228  12.492  1.00 15.71 ? 124 ILE   D CG1  1 
ATOM   6733 C  CG2  . ILE   D 1 145 ? -65.952 -1.836  13.295  1.00 16.31 ? 124 ILE   D CG2  1 
ATOM   6734 C  CD1  . ILE   D 1 145 ? -64.109 -4.366  12.965  1.00 16.30 ? 124 ILE   D CD1  1 
ATOM   6735 N  N    . GLY   D 1 146 ? -68.721 -3.244  15.763  1.00 15.56 ? 125 GLY   D N    1 
ATOM   6736 C  CA   . GLY   D 1 146 ? -69.613 -2.454  16.604  1.00 15.94 ? 125 GLY   D CA   1 
ATOM   6737 C  C    . GLY   D 1 146 ? -69.229 -2.554  18.082  1.00 14.35 ? 125 GLY   D C    1 
ATOM   6738 O  O    . GLY   D 1 146 ? -69.024 -1.557  18.766  1.00 15.63 ? 125 GLY   D O    1 
ATOM   6739 N  N    . THR   D 1 147 ? -69.163 -3.780  18.612  1.00 14.50 ? 126 THR   D N    1 
ATOM   6740 C  CA   . THR   D 1 147 ? -68.942 -3.907  20.051  1.00 15.00 ? 126 THR   D CA   1 
ATOM   6741 C  C    . THR   D 1 147 ? -67.552 -3.419  20.444  1.00 16.64 ? 126 THR   D C    1 
ATOM   6742 O  O    . THR   D 1 147 ? -67.376 -2.799  21.488  1.00 16.76 ? 126 THR   D O    1 
ATOM   6743 C  CB   . THR   D 1 147 ? -69.126 -5.343  20.541  1.00 16.38 ? 126 THR   D CB   1 
ATOM   6744 O  OG1  . THR   D 1 147 ? -68.179 -6.168  19.872  1.00 18.70 ? 126 THR   D OG1  1 
ATOM   6745 C  CG2  . THR   D 1 147 ? -70.523 -5.864  20.277  1.00 17.65 ? 126 THR   D CG2  1 
ATOM   6746 N  N    . ASN   D 1 148 ? -66.550 -3.721  19.613  1.00 15.85 ? 127 ASN   D N    1 
ATOM   6747 C  CA   . ASN   D 1 148 ? -65.177 -3.545  20.058  1.00 14.71 ? 127 ASN   D CA   1 
ATOM   6748 C  C    . ASN   D 1 148 ? -64.674 -2.124  19.806  1.00 15.25 ? 127 ASN   D C    1 
ATOM   6749 O  O    . ASN   D 1 148 ? -63.693 -1.723  20.437  1.00 16.20 ? 127 ASN   D O    1 
ATOM   6750 C  CB   . ASN   D 1 148 ? -64.254 -4.570  19.419  1.00 15.19 ? 127 ASN   D CB   1 
ATOM   6751 C  CG   . ASN   D 1 148 ? -64.402 -5.941  20.017  1.00 17.04 ? 127 ASN   D CG   1 
ATOM   6752 O  OD1  . ASN   D 1 148 ? -64.078 -6.132  21.199  1.00 19.04 ? 127 ASN   D OD1  1 
ATOM   6753 N  ND2  . ASN   D 1 148 ? -64.845 -6.899  19.221  1.00 16.88 ? 127 ASN   D ND2  1 
ATOM   6754 N  N    . ALA   D 1 149 ? -65.328 -1.391  18.886  1.00 14.22 ? 128 ALA   D N    1 
ATOM   6755 C  CA   . ALA   D 1 149 ? -64.799 -0.099  18.462  1.00 14.60 ? 128 ALA   D CA   1 
ATOM   6756 C  C    . ALA   D 1 149 ? -65.869 0.978   18.356  1.00 13.81 ? 128 ALA   D C    1 
ATOM   6757 O  O    . ALA   D 1 149 ? -65.691 2.069   18.913  1.00 13.95 ? 128 ALA   D O    1 
ATOM   6758 C  CB   . ALA   D 1 149 ? -64.032 -0.225  17.145  1.00 16.32 ? 128 ALA   D CB   1 
ATOM   6759 N  N    . ILE   D 1 150 ? -66.921 0.717   17.572  1.00 13.64 ? 129 ILE   D N    1 
ATOM   6760 C  CA   . ILE   D 1 150 ? -67.848 1.811   17.289  1.00 14.04 ? 129 ILE   D CA   1 
ATOM   6761 C  C    . ILE   D 1 150 ? -68.673 2.179   18.529  1.00 14.32 ? 129 ILE   D C    1 
ATOM   6762 O  O    . ILE   D 1 150 ? -68.828 3.379   18.826  1.00 14.37 ? 129 ILE   D O    1 
ATOM   6763 C  CB   . ILE   D 1 150 ? -68.724 1.522   16.053  1.00 15.05 ? 129 ILE   D CB   1 
ATOM   6764 C  CG1  . ILE   D 1 150 ? -67.852 1.352   14.770  1.00 16.17 ? 129 ILE   D CG1  1 
ATOM   6765 C  CG2  . ILE   D 1 150 ? -69.742 2.653   15.876  1.00 15.92 ? 129 ILE   D CG2  1 
ATOM   6766 C  CD1  . ILE   D 1 150 ? -68.544 0.613   13.620  1.00 18.42 ? 129 ILE   D CD1  1 
ATOM   6767 N  N    . ALA   D 1 151 ? -69.158 1.179   19.275  1.00 13.64 ? 130 ALA   D N    1 
ATOM   6768 C  CA   . ALA   D 1 151 ? -69.919 1.478   20.479  1.00 14.13 ? 130 ALA   D CA   1 
ATOM   6769 C  C    . ALA   D 1 151 ? -69.020 2.206   21.485  1.00 13.86 ? 130 ALA   D C    1 
ATOM   6770 O  O    . ALA   D 1 151 ? -69.423 3.243   22.018  1.00 14.12 ? 130 ALA   D O    1 
ATOM   6771 C  CB   . ALA   D 1 151 ? -70.619 0.239   21.040  1.00 13.93 ? 130 ALA   D CB   1 
ATOM   6772 N  N    . PRO   D 1 152 ? -67.761 1.770   21.752  1.00 13.93 ? 131 PRO   D N    1 
ATOM   6773 C  CA   . PRO   D 1 152 ? -66.864 2.567   22.590  1.00 12.84 ? 131 PRO   D CA   1 
ATOM   6774 C  C    . PRO   D 1 152 ? -66.753 4.021   22.145  1.00 12.12 ? 131 PRO   D C    1 
ATOM   6775 O  O    . PRO   D 1 152 ? -66.784 4.916   22.993  1.00 13.81 ? 131 PRO   D O    1 
ATOM   6776 C  CB   . PRO   D 1 152 ? -65.525 1.798   22.492  1.00 13.48 ? 131 PRO   D CB   1 
ATOM   6777 C  CG   . PRO   D 1 152 ? -66.017 0.356   22.461  1.00 14.24 ? 131 PRO   D CG   1 
ATOM   6778 C  CD   . PRO   D 1 152 ? -67.188 0.440   21.450  1.00 14.13 ? 131 PRO   D CD   1 
ATOM   6779 N  N    . PHE   D 1 153 ? -66.665 4.246   20.825  1.00 11.93 ? 132 PHE   D N    1 
ATOM   6780 C  CA   . PHE   D 1 153 ? -66.572 5.625   20.349  1.00 13.20 ? 132 PHE   D CA   1 
ATOM   6781 C  C    . PHE   D 1 153 ? -67.848 6.404   20.683  1.00 13.76 ? 132 PHE   D C    1 
ATOM   6782 O  O    . PHE   D 1 153 ? -67.787 7.555   21.144  1.00 14.15 ? 132 PHE   D O    1 
ATOM   6783 C  CB   . PHE   D 1 153 ? -66.286 5.609   18.841  1.00 13.57 ? 132 PHE   D CB   1 
ATOM   6784 C  CG   . PHE   D 1 153 ? -66.605 6.926   18.146  1.00 14.42 ? 132 PHE   D CG   1 
ATOM   6785 C  CD1  . PHE   D 1 153 ? -65.711 7.992   18.168  1.00 15.83 ? 132 PHE   D CD1  1 
ATOM   6786 C  CD2  . PHE   D 1 153 ? -67.797 7.072   17.437  1.00 14.73 ? 132 PHE   D CD2  1 
ATOM   6787 C  CE1  . PHE   D 1 153 ? -66.022 9.206   17.553  1.00 16.14 ? 132 PHE   D CE1  1 
ATOM   6788 C  CE2  . PHE   D 1 153 ? -68.095 8.281   16.799  1.00 16.06 ? 132 PHE   D CE2  1 
ATOM   6789 C  CZ   . PHE   D 1 153 ? -67.213 9.337   16.858  1.00 17.12 ? 132 PHE   D CZ   1 
ATOM   6790 N  N    . LEU   D 1 154 ? -69.006 5.805   20.399  1.00 14.12 ? 133 LEU   D N    1 
ATOM   6791 C  CA   . LEU   D 1 154 ? -70.268 6.519   20.616  1.00 14.63 ? 133 LEU   D CA   1 
ATOM   6792 C  C    . LEU   D 1 154 ? -70.543 6.745   22.099  1.00 14.50 ? 133 LEU   D C    1 
ATOM   6793 O  O    . LEU   D 1 154 ? -71.051 7.803   22.491  1.00 15.29 ? 133 LEU   D O    1 
ATOM   6794 C  CB   . LEU   D 1 154 ? -71.383 5.715   19.954  1.00 14.19 ? 133 LEU   D CB   1 
ATOM   6795 C  CG   . LEU   D 1 154 ? -71.347 5.657   18.421  1.00 14.50 ? 133 LEU   D CG   1 
ATOM   6796 C  CD1  . LEU   D 1 154 ? -72.243 4.536   17.887  1.00 15.65 ? 133 LEU   D CD1  1 
ATOM   6797 C  CD2  . LEU   D 1 154 ? -71.575 7.004   17.696  1.00 16.42 ? 133 LEU   D CD2  1 
ATOM   6798 N  N    . LEU   D 1 155 ? -70.197 5.765   22.944  1.00 14.13 ? 134 LEU   D N    1 
ATOM   6799 C  CA   . LEU   D 1 155 ? -70.317 5.909   24.387  1.00 14.61 ? 134 LEU   D CA   1 
ATOM   6800 C  C    . LEU   D 1 155 ? -69.400 7.018   24.886  1.00 15.09 ? 134 LEU   D C    1 
ATOM   6801 O  O    . LEU   D 1 155 ? -69.766 7.767   25.784  1.00 15.75 ? 134 LEU   D O    1 
ATOM   6802 C  CB   . LEU   D 1 155 ? -70.016 4.587   25.078  1.00 14.27 ? 134 LEU   D CB   1 
ATOM   6803 C  CG   . LEU   D 1 155 ? -71.093 3.522   24.873  1.00 14.58 ? 134 LEU   D CG   1 
ATOM   6804 C  CD1  . LEU   D 1 155 ? -70.538 2.123   25.133  1.00 14.28 ? 134 LEU   D CD1  1 
ATOM   6805 C  CD2  . LEU   D 1 155 ? -72.270 3.830   25.826  1.00 15.54 ? 134 LEU   D CD2  1 
ATOM   6806 N  N    . THR   D 1 156 ? -68.197 7.099   24.296  1.00 14.72 ? 135 THR   D N    1 
ATOM   6807 C  CA   . THR   D 1 156 ? -67.254 8.155   24.647  1.00 14.60 ? 135 THR   D CA   1 
ATOM   6808 C  C    . THR   D 1 156 ? -67.841 9.518   24.287  1.00 15.26 ? 135 THR   D C    1 
ATOM   6809 O  O    . THR   D 1 156 ? -67.731 10.453  25.083  1.00 15.23 ? 135 THR   D O    1 
ATOM   6810 C  CB   . THR   D 1 156 ? -65.921 7.922   23.924  1.00 15.00 ? 135 THR   D CB   1 
ATOM   6811 O  OG1  . THR   D 1 156 ? -65.360 6.712   24.430  1.00 15.59 ? 135 THR   D OG1  1 
ATOM   6812 C  CG2  . THR   D 1 156 ? -64.919 9.039   24.162  1.00 15.00 ? 135 THR   D CG2  1 
ATOM   6813 N  N    . MET   D 1 157 ? -68.425 9.626   23.082  1.00 15.00 ? 136 MET   D N    1 
ATOM   6814 C  CA   A MET   D 1 157 ? -69.050 10.875  22.664  0.70 15.84 ? 136 MET   D CA   1 
ATOM   6815 C  CA   B MET   D 1 157 ? -69.088 10.849  22.634  0.30 15.14 ? 136 MET   D CA   1 
ATOM   6816 C  C    . MET   D 1 157 ? -70.175 11.250  23.628  1.00 16.31 ? 136 MET   D C    1 
ATOM   6817 O  O    . MET   D 1 157 ? -70.225 12.394  24.096  1.00 16.99 ? 136 MET   D O    1 
ATOM   6818 C  CB   A MET   D 1 157 ? -69.578 10.751  21.233  0.70 18.26 ? 136 MET   D CB   1 
ATOM   6819 C  CB   B MET   D 1 157 ? -69.792 10.669  21.281  0.30 14.80 ? 136 MET   D CB   1 
ATOM   6820 C  CG   A MET   D 1 157 ? -70.343 11.948  20.748  0.70 21.93 ? 136 MET   D CG   1 
ATOM   6821 C  CG   B MET   D 1 157 ? -68.888 10.709  20.067  0.30 14.51 ? 136 MET   D CG   1 
ATOM   6822 S  SD   A MET   D 1 157 ? -70.776 11.626  19.029  0.70 27.99 ? 136 MET   D SD   1 
ATOM   6823 S  SD   B MET   D 1 157 ? -69.817 10.835  18.525  0.30 14.80 ? 136 MET   D SD   1 
ATOM   6824 C  CE   A MET   D 1 157 ? -69.360 12.299  18.152  0.70 25.48 ? 136 MET   D CE   1 
ATOM   6825 C  CE   B MET   D 1 157 ? -70.511 12.484  18.702  0.30 15.13 ? 136 MET   D CE   1 
ATOM   6826 N  N    . SER   D 1 158 ? -71.058 10.295  23.944  1.00 16.51 ? 137 SER   D N    1 
ATOM   6827 C  CA   . SER   D 1 158 ? -72.185 10.606  24.814  1.00 16.88 ? 137 SER   D CA   1 
ATOM   6828 C  C    . SER   D 1 158 ? -71.698 10.981  26.214  1.00 18.35 ? 137 SER   D C    1 
ATOM   6829 O  O    . SER   D 1 158 ? -72.222 11.908  26.831  1.00 19.66 ? 137 SER   D O    1 
ATOM   6830 C  CB   . SER   D 1 158 ? -73.176 9.458   24.837  1.00 18.42 ? 137 SER   D CB   1 
ATOM   6831 O  OG   . SER   D 1 158 ? -73.854 9.419   23.589  1.00 19.68 ? 137 SER   D OG   1 
ATOM   6832 N  N    . PHE   D 1 159 ? -70.675 10.271  26.717  1.00 17.13 ? 138 PHE   D N    1 
ATOM   6833 C  CA   . PHE   D 1 159 ? -70.138 10.537  28.041  1.00 15.70 ? 138 PHE   D CA   1 
ATOM   6834 C  C    . PHE   D 1 159 ? -69.592 11.959  28.090  1.00 17.78 ? 138 PHE   D C    1 
ATOM   6835 O  O    . PHE   D 1 159 ? -69.849 12.690  29.053  1.00 19.00 ? 138 PHE   D O    1 
ATOM   6836 C  CB   . PHE   D 1 159 ? -69.020 9.523   28.311  1.00 16.59 ? 138 PHE   D CB   1 
ATOM   6837 C  CG   . PHE   D 1 159 ? -68.281 9.724   29.627  1.00 16.11 ? 138 PHE   D CG   1 
ATOM   6838 C  CD1  . PHE   D 1 159 ? -67.169 10.562  29.699  1.00 16.50 ? 138 PHE   D CD1  1 
ATOM   6839 C  CD2  . PHE   D 1 159 ? -68.695 9.074   30.788  1.00 16.32 ? 138 PHE   D CD2  1 
ATOM   6840 C  CE1  . PHE   D 1 159 ? -66.498 10.740  30.907  1.00 18.45 ? 138 PHE   D CE1  1 
ATOM   6841 C  CE2  . PHE   D 1 159 ? -68.011 9.238   31.993  1.00 16.99 ? 138 PHE   D CE2  1 
ATOM   6842 C  CZ   . PHE   D 1 159 ? -66.904 10.077  32.042  1.00 17.95 ? 138 PHE   D CZ   1 
ATOM   6843 N  N    . ALA   D 1 160 ? -68.829 12.341  27.062  1.00 16.64 ? 139 ALA   D N    1 
ATOM   6844 C  CA   . ALA   D 1 160 ? -68.204 13.659  27.038  1.00 18.44 ? 139 ALA   D CA   1 
ATOM   6845 C  C    . ALA   D 1 160 ? -69.258 14.753  26.934  1.00 19.69 ? 139 ALA   D C    1 
ATOM   6846 O  O    . ALA   D 1 160 ? -69.152 15.781  27.614  1.00 20.96 ? 139 ALA   D O    1 
ATOM   6847 C  CB   . ALA   D 1 160 ? -67.211 13.757  25.896  1.00 19.25 ? 139 ALA   D CB   1 
ATOM   6848 N  N    . GLN   D 1 161 ? -70.269 14.522  26.084  1.00 19.83 ? 140 GLN   D N    1 
ATOM   6849 C  CA   A GLN   D 1 161 ? -71.292 15.522  25.793  0.50 21.42 ? 140 GLN   D CA   1 
ATOM   6850 C  CA   B GLN   D 1 161 ? -71.255 15.554  25.808  0.50 21.31 ? 140 GLN   D CA   1 
ATOM   6851 C  C    . GLN   D 1 161 ? -72.108 15.816  27.047  1.00 22.91 ? 140 GLN   D C    1 
ATOM   6852 O  O    . GLN   D 1 161 ? -72.516 16.957  27.277  1.00 23.59 ? 140 GLN   D O    1 
ATOM   6853 C  CB   A GLN   D 1 161 ? -72.290 15.073  24.725  0.50 23.12 ? 140 GLN   D CB   1 
ATOM   6854 C  CB   B GLN   D 1 161 ? -72.001 15.223  24.518  0.50 22.87 ? 140 GLN   D CB   1 
ATOM   6855 C  CG   A GLN   D 1 161 ? -73.178 16.202  24.203  0.50 24.42 ? 140 GLN   D CG   1 
ATOM   6856 C  CG   B GLN   D 1 161 ? -71.210 15.605  23.272  0.50 23.52 ? 140 GLN   D CG   1 
ATOM   6857 C  CD   A GLN   D 1 161 ? -72.396 17.267  23.462  0.50 27.13 ? 140 GLN   D CD   1 
ATOM   6858 C  CD   B GLN   D 1 161 ? -71.858 15.169  21.977  0.50 27.31 ? 140 GLN   D CD   1 
ATOM   6859 O  OE1  A GLN   D 1 161 ? -71.525 16.964  22.640  0.50 29.61 ? 140 GLN   D OE1  1 
ATOM   6860 O  OE1  B GLN   D 1 161 ? -71.182 14.771  21.023  0.50 25.50 ? 140 GLN   D OE1  1 
ATOM   6861 N  NE2  A GLN   D 1 161 ? -72.678 18.529  23.756  0.50 29.08 ? 140 GLN   D NE2  1 
ATOM   6862 N  NE2  B GLN   D 1 161 ? -73.178 15.277  21.914  0.50 28.69 ? 140 GLN   D NE2  1 
ATOM   6863 N  N    . ARG   D 1 162 ? -72.338 14.784  27.855  1.00 22.61 ? 141 ARG   D N    1 
ATOM   6864 C  CA   . ARG   D 1 162 ? -73.229 14.901  29.004  1.00 27.90 ? 141 ARG   D CA   1 
ATOM   6865 C  C    . ARG   D 1 162 ? -72.538 15.544  30.204  1.00 30.60 ? 141 ARG   D C    1 
ATOM   6866 O  O    . ARG   D 1 162 ? -73.208 15.815  31.204  1.00 36.29 ? 141 ARG   D O    1 
ATOM   6867 C  CB   . ARG   D 1 162 ? -73.765 13.534  29.446  1.00 27.70 ? 141 ARG   D CB   1 
ATOM   6868 C  CG   A ARG   D 1 162 ? -74.791 12.893  28.521  0.60 28.93 ? 141 ARG   D CG   1 
ATOM   6869 C  CD   A ARG   D 1 162 ? -76.155 13.577  28.448  0.60 32.59 ? 141 ARG   D CD   1 
ATOM   6870 N  NE   A ARG   D 1 162 ? -76.700 13.932  29.763  0.60 33.22 ? 141 ARG   D NE   1 
ATOM   6871 C  CZ   A ARG   D 1 162 ? -77.762 13.418  30.381  0.60 33.14 ? 141 ARG   D CZ   1 
ATOM   6872 N  NH1  A ARG   D 1 162 ? -78.386 12.353  29.917  0.60 33.25 ? 141 ARG   D NH1  1 
ATOM   6873 N  NH2  A ARG   D 1 162 ? -78.185 13.978  31.497  0.60 32.13 ? 141 ARG   D NH2  1 
ATOM   6874 N  N    . GLN   D 1 163 ? -71.221 15.781  30.114  1.00 29.73 ? 142 GLN   D N    1 
ATOM   6875 C  CA   . GLN   D 1 163 ? -70.453 16.338  31.220  1.00 31.75 ? 142 GLN   D CA   1 
ATOM   6876 C  C    . GLN   D 1 163 ? -70.722 17.850  31.330  1.00 40.62 ? 142 GLN   D C    1 
ATOM   6877 O  O    . GLN   D 1 163 ? -71.828 18.178  31.810  1.00 46.59 ? 142 GLN   D O    1 
ATOM   6878 C  CB   . GLN   D 1 163 ? -68.950 16.087  31.100  1.00 29.77 ? 142 GLN   D CB   1 
ATOM   6879 C  CG   . GLN   D 1 163 ? -68.546 14.622  31.219  1.00 26.92 ? 142 GLN   D CG   1 
ATOM   6880 C  CD   . GLN   D 1 163 ? -69.152 13.879  32.389  1.00 26.64 ? 142 GLN   D CD   1 
ATOM   6881 O  OE1  . GLN   D 1 163 ? -69.333 14.412  33.494  1.00 24.76 ? 142 GLN   D OE1  1 
ATOM   6882 N  NE2  . GLN   D 1 163 ? -69.459 12.608  32.154  1.00 23.38 ? 142 GLN   D NE2  1 
ATOM   6883 N  N    . SER   D 1 173 ? -64.759 16.591  39.204  1.00 46.79 ? 152 SER   D N    1 
ATOM   6884 C  CA   . SER   D 1 173 ? -64.172 15.478  39.995  1.00 42.14 ? 152 SER   D CA   1 
ATOM   6885 C  C    . SER   D 1 173 ? -63.052 14.799  39.205  1.00 38.50 ? 152 SER   D C    1 
ATOM   6886 O  O    . SER   D 1 173 ? -62.128 15.464  38.742  1.00 42.87 ? 152 SER   D O    1 
ATOM   6887 C  CB   . SER   D 1 173 ? -65.235 14.501  40.433  1.00 49.04 ? 152 SER   D CB   1 
ATOM   6888 N  N    . ASN   D 1 174 ? -63.157 13.474  39.053  1.00 28.64 ? 153 ASN   D N    1 
ATOM   6889 C  CA   . ASN   D 1 174 ? -62.095 12.642  38.507  1.00 25.48 ? 153 ASN   D CA   1 
ATOM   6890 C  C    . ASN   D 1 174 ? -62.708 11.780  37.408  1.00 21.30 ? 153 ASN   D C    1 
ATOM   6891 O  O    . ASN   D 1 174 ? -63.081 10.624  37.637  1.00 20.89 ? 153 ASN   D O    1 
ATOM   6892 C  CB   . ASN   D 1 174 ? -61.373 11.894  39.623  1.00 27.26 ? 153 ASN   D CB   1 
ATOM   6893 C  CG   . ASN   D 1 174 ? -60.414 10.849  39.109  1.00 29.23 ? 153 ASN   D CG   1 
ATOM   6894 O  OD1  . ASN   D 1 174 ? -59.816 11.023  38.042  1.00 28.10 ? 153 ASN   D OD1  1 
ATOM   6895 N  ND2  . ASN   D 1 174 ? -60.283 9.752   39.843  1.00 35.70 ? 153 ASN   D ND2  1 
ATOM   6896 N  N    . LEU   D 1 175 ? -62.868 12.392  36.234  1.00 19.21 ? 154 LEU   D N    1 
ATOM   6897 C  CA   . LEU   D 1 175 ? -63.619 11.748  35.163  1.00 17.60 ? 154 LEU   D CA   1 
ATOM   6898 C  C    . LEU   D 1 175 ? -62.662 10.894  34.340  1.00 16.87 ? 154 LEU   D C    1 
ATOM   6899 O  O    . LEU   D 1 175 ? -61.584 11.361  33.976  1.00 17.08 ? 154 LEU   D O    1 
ATOM   6900 C  CB   . LEU   D 1 175 ? -64.237 12.832  34.283  1.00 19.04 ? 154 LEU   D CB   1 
ATOM   6901 C  CG   . LEU   D 1 175 ? -65.182 13.814  34.988  1.00 21.18 ? 154 LEU   D CG   1 
ATOM   6902 C  CD1  . LEU   D 1 175 ? -65.566 14.918  34.014  1.00 23.05 ? 154 LEU   D CD1  1 
ATOM   6903 C  CD2  . LEU   D 1 175 ? -66.412 13.098  35.499  1.00 21.90 ? 154 LEU   D CD2  1 
ATOM   6904 N  N    . SER   D 1 176 ? -63.047 9.644   34.054  1.00 16.21 ? 155 SER   D N    1 
ATOM   6905 C  CA   . SER   D 1 176 ? -62.173 8.912   33.147  1.00 16.99 ? 155 SER   D CA   1 
ATOM   6906 C  C    . SER   D 1 176 ? -62.894 7.768   32.444  1.00 16.05 ? 155 SER   D C    1 
ATOM   6907 O  O    . SER   D 1 176 ? -63.976 7.328   32.850  1.00 15.33 ? 155 SER   D O    1 
ATOM   6908 C  CB   . SER   D 1 176 ? -60.894 8.452   33.817  1.00 20.35 ? 155 SER   D CB   1 
ATOM   6909 O  OG   . SER   D 1 176 ? -61.103 7.267   34.565  1.00 19.74 ? 155 SER   D OG   1 
ATOM   6910 N  N    . ILE   D 1 177 ? -62.246 7.317   31.363  1.00 14.77 ? 156 ILE   D N    1 
ATOM   6911 C  CA   . ILE   D 1 177 ? -62.739 6.233   30.532  1.00 14.61 ? 156 ILE   D CA   1 
ATOM   6912 C  C    . ILE   D 1 177 ? -61.660 5.175   30.510  1.00 13.62 ? 156 ILE   D C    1 
ATOM   6913 O  O    . ILE   D 1 177 ? -60.487 5.515   30.390  1.00 14.48 ? 156 ILE   D O    1 
ATOM   6914 C  CB   . ILE   D 1 177 ? -63.079 6.688   29.100  1.00 14.56 ? 156 ILE   D CB   1 
ATOM   6915 C  CG1  . ILE   D 1 177 ? -64.147 7.805   29.121  1.00 15.52 ? 156 ILE   D CG1  1 
ATOM   6916 C  CG2  . ILE   D 1 177 ? -63.486 5.491   28.229  1.00 15.09 ? 156 ILE   D CG2  1 
ATOM   6917 C  CD1  . ILE   D 1 177 ? -64.436 8.408   27.759  1.00 15.37 ? 156 ILE   D CD1  1 
ATOM   6918 N  N    . VAL   D 1 178 ? -62.063 3.902   30.652  1.00 13.22 ? 157 VAL   D N    1 
ATOM   6919 C  CA   . VAL   D 1 178 ? -61.113 2.809   30.521  1.00 14.65 ? 157 VAL   D CA   1 
ATOM   6920 C  C    . VAL   D 1 178 ? -61.643 1.852   29.459  1.00 14.63 ? 157 VAL   D C    1 
ATOM   6921 O  O    . VAL   D 1 178 ? -62.759 1.342   29.589  1.00 14.44 ? 157 VAL   D O    1 
ATOM   6922 C  CB   . VAL   D 1 178 ? -60.882 2.050   31.842  1.00 14.96 ? 157 VAL   D CB   1 
ATOM   6923 C  CG1  . VAL   D 1 178 ? -59.957 0.844   31.630  1.00 15.61 ? 157 VAL   D CG1  1 
ATOM   6924 C  CG2  . VAL   D 1 178 ? -60.336 2.950   32.949  1.00 15.07 ? 157 VAL   D CG2  1 
ATOM   6925 N  N    . ASN   D 1 179 ? -60.800 1.557   28.463  1.00 13.97 ? 158 ASN   D N    1 
ATOM   6926 C  CA   . ASN   D 1 179 ? -61.137 0.672   27.355  1.00 13.24 ? 158 ASN   D CA   1 
ATOM   6927 C  C    . ASN   D 1 179 ? -60.458 -0.678  27.542  1.00 13.76 ? 158 ASN   D C    1 
ATOM   6928 O  O    . ASN   D 1 179 ? -59.254 -0.714  27.808  1.00 15.05 ? 158 ASN   D O    1 
ATOM   6929 C  CB   . ASN   D 1 179 ? -60.722 1.300   26.026  1.00 13.77 ? 158 ASN   D CB   1 
ATOM   6930 C  CG   . ASN   D 1 179 ? -61.544 2.525   25.716  1.00 15.22 ? 158 ASN   D CG   1 
ATOM   6931 O  OD1  . ASN   D 1 179 ? -62.713 2.574   26.108  1.00 15.17 ? 158 ASN   D OD1  1 
ATOM   6932 N  ND2  . ASN   D 1 179 ? -60.957 3.510   25.056  1.00 14.71 ? 158 ASN   D ND2  1 
ATOM   6933 N  N    . LEU   D 1 180 ? -61.226 -1.767  27.432  1.00 13.21 ? 159 LEU   D N    1 
ATOM   6934 C  CA   . LEU   D 1 180 ? -60.641 -3.101  27.535  1.00 13.92 ? 159 LEU   D CA   1 
ATOM   6935 C  C    . LEU   D 1 180 ? -60.091 -3.504  26.180  1.00 13.81 ? 159 LEU   D C    1 
ATOM   6936 O  O    . LEU   D 1 180 ? -60.846 -3.732  25.236  1.00 15.02 ? 159 LEU   D O    1 
ATOM   6937 C  CB   . LEU   D 1 180 ? -61.638 -4.137  28.055  1.00 14.72 ? 159 LEU   D CB   1 
ATOM   6938 C  CG   . LEU   D 1 180 ? -61.723 -4.272  29.578  1.00 15.43 ? 159 LEU   D CG   1 
ATOM   6939 C  CD1  . LEU   D 1 180 ? -60.487 -4.978  30.125  1.00 16.20 ? 159 LEU   D CD1  1 
ATOM   6940 C  CD2  . LEU   D 1 180 ? -61.874 -2.916  30.270  1.00 16.51 ? 159 LEU   D CD2  1 
ATOM   6941 N  N    . CYS   D 1 181 ? -58.751 -3.505  26.124  1.00 13.96 ? 160 CYS   D N    1 
ATOM   6942 C  CA   . CYS   D 1 181 ? -58.001 -3.732  24.893  1.00 16.08 ? 160 CYS   D CA   1 
ATOM   6943 C  C    . CYS   D 1 181 ? -57.587 -5.204  24.844  1.00 17.22 ? 160 CYS   D C    1 
ATOM   6944 O  O    . CYS   D 1 181 ? -58.269 -6.053  25.419  1.00 18.78 ? 160 CYS   D O    1 
ATOM   6945 C  CB   . CYS   D 1 181 ? -56.851 -2.742  24.771  1.00 16.43 ? 160 CYS   D CB   1 
ATOM   6946 S  SG   . CYS   D 1 181 ? -57.424 -1.016  24.650  1.00 19.38 ? 160 CYS   D SG   1 
ATOM   6947 N  N    . ASP   D 1 182 ? -56.492 -5.507  24.131  1.00 15.04 ? 161 ASP   D N    1 
ATOM   6948 C  CA   . ASP   D 1 182 ? -56.037 -6.886  24.013  1.00 15.88 ? 161 ASP   D CA   1 
ATOM   6949 C  C    . ASP   D 1 182 ? -54.520 -6.856  23.837  1.00 15.75 ? 161 ASP   D C    1 
ATOM   6950 O  O    . ASP   D 1 182 ? -54.031 -6.227  22.902  1.00 16.34 ? 161 ASP   D O    1 
ATOM   6951 C  CB   . ASP   D 1 182 ? -56.781 -7.578  22.883  1.00 17.21 ? 161 ASP   D CB   1 
ATOM   6952 C  CG   . ASP   D 1 182 ? -56.460 -9.052  22.699  1.00 19.69 ? 161 ASP   D CG   1 
ATOM   6953 O  OD1  . ASP   D 1 182 ? -55.298 -9.423  22.920  1.00 20.04 ? 161 ASP   D OD1  1 
ATOM   6954 O  OD2  . ASP   D 1 182 ? -57.375 -9.789  22.271  1.00 19.57 ? 161 ASP   D OD2  1 
ATOM   6955 N  N    . ALA   D 1 183 ? -53.779 -7.515  24.742  1.00 13.89 ? 162 ALA   D N    1 
ATOM   6956 C  CA   . ALA   D 1 183 ? -52.322 -7.462  24.679  1.00 14.66 ? 162 ALA   D CA   1 
ATOM   6957 C  C    . ALA   D 1 183 ? -51.724 -8.167  23.455  1.00 14.75 ? 162 ALA   D C    1 
ATOM   6958 O  O    . ALA   D 1 183 ? -50.534 -7.962  23.166  1.00 15.99 ? 162 ALA   D O    1 
ATOM   6959 C  CB   . ALA   D 1 183 ? -51.720 -8.033  25.943  1.00 15.39 ? 162 ALA   D CB   1 
ATOM   6960 N  N    . MET   D 1 184 ? -52.529 -8.997  22.778  1.00 15.98 ? 163 MET   D N    1 
ATOM   6961 C  CA   . MET   D 1 184 ? -52.033 -9.915  21.761  1.00 16.56 ? 163 MET   D CA   1 
ATOM   6962 C  C    . MET   D 1 184 ? -52.368 -9.459  20.340  1.00 19.53 ? 163 MET   D C    1 
ATOM   6963 O  O    . MET   D 1 184 ? -52.186 -10.216 19.387  1.00 20.67 ? 163 MET   D O    1 
ATOM   6964 C  CB   . MET   D 1 184 ? -52.544 -11.339 22.041  1.00 18.57 ? 163 MET   D CB   1 
ATOM   6965 C  CG   . MET   D 1 184 ? -51.987 -11.928 23.326  1.00 19.87 ? 163 MET   D CG   1 
ATOM   6966 S  SD   . MET   D 1 184 ? -50.196 -12.143 23.262  1.00 22.39 ? 163 MET   D SD   1 
ATOM   6967 C  CE   . MET   D 1 184 ? -50.062 -13.557 22.164  1.00 23.44 ? 163 MET   D CE   1 
ATOM   6968 N  N    . VAL   D 1 185 ? -52.778 -8.201  20.175  1.00 19.38 ? 164 VAL   D N    1 
ATOM   6969 C  CA   . VAL   D 1 185 ? -53.301 -7.775  18.880  1.00 21.82 ? 164 VAL   D CA   1 
ATOM   6970 C  C    . VAL   D 1 185 ? -52.192 -7.621  17.835  1.00 20.62 ? 164 VAL   D C    1 
ATOM   6971 O  O    . VAL   D 1 185 ? -52.488 -7.485  16.650  1.00 20.62 ? 164 VAL   D O    1 
ATOM   6972 C  CB   . VAL   D 1 185 ? -54.127 -6.479  18.946  1.00 24.29 ? 164 VAL   D CB   1 
ATOM   6973 C  CG1  . VAL   D 1 185 ? -55.467 -6.690  19.644  1.00 29.22 ? 164 VAL   D CG1  1 
ATOM   6974 C  CG2  . VAL   D 1 185 ? -53.314 -5.349  19.553  1.00 23.99 ? 164 VAL   D CG2  1 
ATOM   6975 N  N    . ASP   D 1 186 ? -50.922 -7.618  18.250  1.00 19.43 ? 165 ASP   D N    1 
ATOM   6976 C  CA   . ASP   D 1 186 ? -49.870 -7.595  17.243  1.00 17.93 ? 165 ASP   D CA   1 
ATOM   6977 C  C    . ASP   D 1 186 ? -49.330 -8.990  16.984  1.00 19.79 ? 165 ASP   D C    1 
ATOM   6978 O  O    . ASP   D 1 186 ? -48.413 -9.146  16.176  1.00 20.41 ? 165 ASP   D O    1 
ATOM   6979 C  CB   . ASP   D 1 186 ? -48.754 -6.636  17.616  1.00 19.00 ? 165 ASP   D CB   1 
ATOM   6980 C  CG   . ASP   D 1 186 ? -49.156 -5.171  17.632  1.00 20.97 ? 165 ASP   D CG   1 
ATOM   6981 O  OD1  . ASP   D 1 186 ? -49.900 -4.735  16.721  1.00 22.87 ? 165 ASP   D OD1  1 
ATOM   6982 O  OD2  . ASP   D 1 186 ? -48.708 -4.469  18.573  1.00 24.04 ? 165 ASP   D OD2  1 
ATOM   6983 N  N    . GLN   D 1 187 ? -49.891 -9.994  17.664  1.00 18.39 ? 166 GLN   D N    1 
ATOM   6984 C  CA   . GLN   D 1 187 ? -49.553 -11.382 17.383  1.00 18.60 ? 166 GLN   D CA   1 
ATOM   6985 C  C    . GLN   D 1 187 ? -50.858 -12.161 17.373  1.00 19.41 ? 166 GLN   D C    1 
ATOM   6986 O  O    . GLN   D 1 187 ? -51.094 -13.018 18.226  1.00 20.30 ? 166 GLN   D O    1 
ATOM   6987 C  CB   . GLN   D 1 187 ? -48.617 -11.997 18.427  1.00 22.17 ? 166 GLN   D CB   1 
ATOM   6988 C  CG   . GLN   D 1 187 ? -47.252 -11.325 18.509  1.00 26.09 ? 166 GLN   D CG   1 
ATOM   6989 C  CD   . GLN   D 1 187 ? -46.966 -10.846 19.918  1.00 29.08 ? 166 GLN   D CD   1 
ATOM   6990 O  OE1  . GLN   D 1 187 ? -47.406 -9.767  20.327  1.00 28.68 ? 166 GLN   D OE1  1 
ATOM   6991 N  NE2  . GLN   D 1 187 ? -46.212 -11.635 20.668  1.00 29.43 ? 166 GLN   D NE2  1 
ATOM   6992 N  N    . PRO   D 1 188 ? -51.731 -11.860 16.392  1.00 18.93 ? 167 PRO   D N    1 
ATOM   6993 C  CA   . PRO   D 1 188 ? -53.140 -12.256 16.478  1.00 19.85 ? 167 PRO   D CA   1 
ATOM   6994 C  C    . PRO   D 1 188 ? -53.383 -13.754 16.302  1.00 18.19 ? 167 PRO   D C    1 
ATOM   6995 O  O    . PRO   D 1 188 ? -52.605 -14.450 15.655  1.00 20.83 ? 167 PRO   D O    1 
ATOM   6996 C  CB   . PRO   D 1 188 ? -53.761 -11.447 15.330  1.00 21.15 ? 167 PRO   D CB   1 
ATOM   6997 C  CG   . PRO   D 1 188 ? -52.655 -11.283 14.331  1.00 20.69 ? 167 PRO   D CG   1 
ATOM   6998 C  CD   . PRO   D 1 188 ? -51.419 -11.057 15.202  1.00 19.62 ? 167 PRO   D CD   1 
ATOM   6999 N  N    . CYS   D 1 189 ? -54.513 -14.214 16.846  1.00 19.59 ? 168 CYS   D N    1 
ATOM   7000 C  CA   . CYS   D 1 189 ? -54.956 -15.564 16.547  1.00 20.79 ? 168 CYS   D CA   1 
ATOM   7001 C  C    . CYS   D 1 189 ? -55.382 -15.646 15.087  1.00 19.93 ? 168 CYS   D C    1 
ATOM   7002 O  O    . CYS   D 1 189 ? -55.977 -14.724 14.538  1.00 18.89 ? 168 CYS   D O    1 
ATOM   7003 C  CB   . CYS   D 1 189 ? -56.127 -15.973 17.429  1.00 24.22 ? 168 CYS   D CB   1 
ATOM   7004 S  SG   . CYS   D 1 189 ? -55.561 -16.447 19.084  1.00 31.74 ? 168 CYS   D SG   1 
ATOM   7005 N  N    . MET   D 1 190 ? -55.086 -16.796 14.484  1.00 20.33 ? 169 MET   D N    1 
ATOM   7006 C  CA   . MET   D 1 190 ? -55.415 -17.082 13.101  1.00 21.18 ? 169 MET   D CA   1 
ATOM   7007 C  C    . MET   D 1 190 ? -56.924 -16.934 12.909  1.00 18.49 ? 169 MET   D C    1 
ATOM   7008 O  O    . MET   D 1 190 ? -57.698 -17.467 13.698  1.00 19.29 ? 169 MET   D O    1 
ATOM   7009 C  CB   . MET   D 1 190 ? -55.042 -18.556 12.854  1.00 22.87 ? 169 MET   D CB   1 
ATOM   7010 C  CG   . MET   D 1 190 ? -55.334 -19.049 11.461  1.00 25.99 ? 169 MET   D CG   1 
ATOM   7011 S  SD   . MET   D 1 190 ? -54.403 -18.021 10.305  1.00 31.56 ? 169 MET   D SD   1 
ATOM   7012 C  CE   . MET   D 1 190 ? -52.710 -18.598 10.489  1.00 30.03 ? 169 MET   D CE   1 
ATOM   7013 N  N    . ALA   D 1 191 ? -57.323 -16.203 11.858  1.00 18.12 ? 170 ALA   D N    1 
ATOM   7014 C  CA   . ALA   D 1 191 ? -58.692 -16.077 11.366  1.00 18.27 ? 170 ALA   D CA   1 
ATOM   7015 C  C    . ALA   D 1 191 ? -59.564 -15.182 12.244  1.00 17.79 ? 170 ALA   D C    1 
ATOM   7016 O  O    . ALA   D 1 191 ? -60.798 -15.219 12.137  1.00 17.77 ? 170 ALA   D O    1 
ATOM   7017 C  CB   . ALA   D 1 191 ? -59.320 -17.453 11.164  1.00 19.61 ? 170 ALA   D CB   1 
ATOM   7018 N  N    . PHE   D 1 192 ? -58.919 -14.333 13.067  1.00 15.63 ? 171 PHE   D N    1 
ATOM   7019 C  CA   . PHE   D 1 192 ? -59.631 -13.349 13.874  1.00 14.27 ? 171 PHE   D CA   1 
ATOM   7020 C  C    . PHE   D 1 192 ? -59.462 -11.936 13.310  1.00 14.50 ? 171 PHE   D C    1 
ATOM   7021 O  O    . PHE   D 1 192 ? -59.373 -10.988 14.086  1.00 15.72 ? 171 PHE   D O    1 
ATOM   7022 C  CB   . PHE   D 1 192 ? -59.162 -13.461 15.330  1.00 14.71 ? 171 PHE   D CB   1 
ATOM   7023 C  CG   . PHE   D 1 192 ? -59.810 -14.599 16.100  1.00 16.62 ? 171 PHE   D CG   1 
ATOM   7024 C  CD1  . PHE   D 1 192 ? -59.364 -15.906 15.940  1.00 18.07 ? 171 PHE   D CD1  1 
ATOM   7025 C  CD2  . PHE   D 1 192 ? -60.866 -14.350 16.973  1.00 17.01 ? 171 PHE   D CD2  1 
ATOM   7026 C  CE1  . PHE   D 1 192 ? -59.963 -16.949 16.642  1.00 20.55 ? 171 PHE   D CE1  1 
ATOM   7027 C  CE2  . PHE   D 1 192 ? -61.462 -15.396 17.674  1.00 19.36 ? 171 PHE   D CE2  1 
ATOM   7028 C  CZ   . PHE   D 1 192 ? -61.001 -16.690 17.513  1.00 20.18 ? 171 PHE   D CZ   1 
ATOM   7029 N  N    . SER   D 1 193 ? -59.537 -11.747 11.988  1.00 14.08 ? 172 SER   D N    1 
ATOM   7030 C  CA   A SER   D 1 193 ? -59.215 -10.424 11.461  0.70 14.61 ? 172 SER   D CA   1 
ATOM   7031 C  CA   B SER   D 1 193 ? -59.262 -10.438 11.394  0.30 14.27 ? 172 SER   D CA   1 
ATOM   7032 C  C    . SER   D 1 193 ? -60.179 -9.341  11.938  1.00 15.02 ? 172 SER   D C    1 
ATOM   7033 O  O    . SER   D 1 193 ? -59.721 -8.265  12.316  1.00 14.38 ? 172 SER   D O    1 
ATOM   7034 C  CB   A SER   D 1 193 ? -59.084 -10.422 9.972   0.70 16.49 ? 172 SER   D CB   1 
ATOM   7035 C  CB   B SER   D 1 193 ? -59.314 -10.464 9.883   0.30 14.48 ? 172 SER   D CB   1 
ATOM   7036 O  OG   A SER   D 1 193 ? -60.266 -10.948 9.391   0.70 17.79 ? 172 SER   D OG   1 
ATOM   7037 O  OG   B SER   D 1 193 ? -58.146 -11.044 9.317   0.30 13.86 ? 172 SER   D OG   1 
ATOM   7038 N  N    . LEU   D 1 194 ? -61.497 -9.593  11.934  1.00 14.54 ? 173 LEU   D N    1 
ATOM   7039 C  CA   . LEU   D 1 194 ? -62.405 -8.509  12.300  1.00 15.16 ? 173 LEU   D CA   1 
ATOM   7040 C  C    . LEU   D 1 194 ? -62.272 -8.141  13.779  1.00 14.93 ? 173 LEU   D C    1 
ATOM   7041 O  O    . LEU   D 1 194 ? -62.298 -6.971  14.157  1.00 14.64 ? 173 LEU   D O    1 
ATOM   7042 C  CB   . LEU   D 1 194 ? -63.839 -8.887  11.931  1.00 15.57 ? 173 LEU   D CB   1 
ATOM   7043 C  CG   . LEU   D 1 194 ? -64.197 -8.683  10.457  1.00 15.87 ? 173 LEU   D CG   1 
ATOM   7044 C  CD1  . LEU   D 1 194 ? -65.597 -9.279  10.264  1.00 16.33 ? 173 LEU   D CD1  1 
ATOM   7045 C  CD2  . LEU   D 1 194 ? -64.218 -7.192  10.078  1.00 16.07 ? 173 LEU   D CD2  1 
ATOM   7046 N  N    . TYR   D 1 195 ? -62.132 -9.144  14.639  1.00 14.44 ? 174 TYR   D N    1 
ATOM   7047 C  CA   . TYR   D 1 195 ? -61.890 -8.881  16.048  1.00 14.43 ? 174 TYR   D CA   1 
ATOM   7048 C  C    . TYR   D 1 195 ? -60.633 -8.021  16.210  1.00 14.49 ? 174 TYR   D C    1 
ATOM   7049 O  O    . TYR   D 1 195 ? -60.634 -7.052  16.967  1.00 14.27 ? 174 TYR   D O    1 
ATOM   7050 C  CB   . TYR   D 1 195 ? -61.780 -10.232 16.772  1.00 13.97 ? 174 TYR   D CB   1 
ATOM   7051 C  CG   . TYR   D 1 195 ? -61.304 -10.024 18.204  1.00 14.94 ? 174 TYR   D CG   1 
ATOM   7052 C  CD1  . TYR   D 1 195 ? -62.173 -9.626  19.212  1.00 14.14 ? 174 TYR   D CD1  1 
ATOM   7053 C  CD2  . TYR   D 1 195 ? -59.955 -10.149 18.520  1.00 14.87 ? 174 TYR   D CD2  1 
ATOM   7054 C  CE1  . TYR   D 1 195 ? -61.718 -9.422  20.511  1.00 15.70 ? 174 TYR   D CE1  1 
ATOM   7055 C  CE2  . TYR   D 1 195 ? -59.483 -9.921  19.805  1.00 15.11 ? 174 TYR   D CE2  1 
ATOM   7056 C  CZ   . TYR   D 1 195 ? -60.364 -9.541  20.801  1.00 16.66 ? 174 TYR   D CZ   1 
ATOM   7057 O  OH   . TYR   D 1 195 ? -59.894 -9.306  22.066  1.00 19.28 ? 174 TYR   D OH   1 
ATOM   7058 N  N    . ASN   D 1 196 ? -59.553 -8.381  15.511  1.00 14.55 ? 175 ASN   D N    1 
ATOM   7059 C  CA   A ASN   D 1 196 ? -58.279 -7.694  15.646  0.40 14.41 ? 175 ASN   D CA   1 
ATOM   7060 C  CA   B ASN   D 1 196 ? -58.288 -7.678  15.675  0.60 14.57 ? 175 ASN   D CA   1 
ATOM   7061 C  C    . ASN   D 1 196 ? -58.423 -6.251  15.166  1.00 13.56 ? 175 ASN   D C    1 
ATOM   7062 O  O    . ASN   D 1 196 ? -57.865 -5.325  15.758  1.00 14.08 ? 175 ASN   D O    1 
ATOM   7063 C  CB   A ASN   D 1 196 ? -57.191 -8.449  14.892  0.40 15.69 ? 175 ASN   D CB   1 
ATOM   7064 C  CB   B ASN   D 1 196 ? -57.130 -8.419  15.019  0.60 16.50 ? 175 ASN   D CB   1 
ATOM   7065 C  CG   A ASN   D 1 196 ? -55.817 -7.948  15.250  0.40 17.27 ? 175 ASN   D CG   1 
ATOM   7066 C  CG   B ASN   D 1 196 ? -56.556 -9.436  15.969  0.60 19.87 ? 175 ASN   D CG   1 
ATOM   7067 O  OD1  A ASN   D 1 196 ? -55.489 -7.856  16.437  0.40 18.33 ? 175 ASN   D OD1  1 
ATOM   7068 O  OD1  B ASN   D 1 196 ? -55.732 -9.086  16.822  0.60 21.10 ? 175 ASN   D OD1  1 
ATOM   7069 N  ND2  A ASN   D 1 196 ? -55.016 -7.612  14.251  0.40 17.88 ? 175 ASN   D ND2  1 
ATOM   7070 N  ND2  B ASN   D 1 196 ? -56.985 -10.685 15.855  0.60 19.08 ? 175 ASN   D ND2  1 
ATOM   7071 N  N    . MET   D 1 197 ? -59.126 -6.088  14.044  1.00 13.58 ? 176 MET   D N    1 
ATOM   7072 C  CA   . MET   D 1 197 ? -59.398 -4.754  13.521  1.00 12.93 ? 176 MET   D CA   1 
ATOM   7073 C  C    . MET   D 1 197 ? -60.127 -3.923  14.568  1.00 13.49 ? 176 MET   D C    1 
ATOM   7074 O  O    . MET   D 1 197 ? -59.792 -2.758  14.779  1.00 13.40 ? 176 MET   D O    1 
ATOM   7075 C  CB   . MET   D 1 197 ? -60.264 -4.856  12.262  1.00 13.56 ? 176 MET   D CB   1 
ATOM   7076 C  CG   . MET   D 1 197 ? -59.452 -5.384  11.088  1.00 14.72 ? 176 MET   D CG   1 
ATOM   7077 S  SD   . MET   D 1 197 ? -60.513 -5.750  9.676   1.00 16.28 ? 176 MET   D SD   1 
ATOM   7078 C  CE   . MET   D 1 197 ? -60.887 -4.052  9.242   1.00 18.66 ? 176 MET   D CE   1 
ATOM   7079 N  N    . GLY   D 1 198 ? -61.128 -4.520  15.210  1.00 13.17 ? 177 GLY   D N    1 
ATOM   7080 C  CA   . GLY   D 1 198 ? -61.888 -3.833  16.238  1.00 13.82 ? 177 GLY   D CA   1 
ATOM   7081 C  C    . GLY   D 1 198 ? -60.994 -3.392  17.392  1.00 13.13 ? 177 GLY   D C    1 
ATOM   7082 O  O    . GLY   D 1 198 ? -61.059 -2.234  17.843  1.00 13.42 ? 177 GLY   D O    1 
ATOM   7083 N  N    . LYS   D 1 199 ? -60.167 -4.308  17.897  1.00 13.77 ? 178 LYS   D N    1 
ATOM   7084 C  CA   . LYS   D 1 199 ? -59.325 -3.967  19.039  1.00 13.53 ? 178 LYS   D CA   1 
ATOM   7085 C  C    . LYS   D 1 199 ? -58.229 -2.967  18.653  1.00 13.55 ? 178 LYS   D C    1 
ATOM   7086 O  O    . LYS   D 1 199 ? -57.871 -2.124  19.478  1.00 13.85 ? 178 LYS   D O    1 
ATOM   7087 C  CB   . LYS   D 1 199 ? -58.743 -5.235  19.673  1.00 13.83 ? 178 LYS   D CB   1 
ATOM   7088 C  CG   . LYS   D 1 199 ? -59.804 -6.056  20.400  1.00 15.42 ? 178 LYS   D CG   1 
ATOM   7089 C  CD   . LYS   D 1 199 ? -60.459 -5.297  21.549  1.00 15.33 ? 178 LYS   D CD   1 
ATOM   7090 C  CE   . LYS   D 1 199 ? -61.145 -6.259  22.489  1.00 17.08 ? 178 LYS   D CE   1 
ATOM   7091 N  NZ   . LYS   D 1 199 ? -62.051 -5.552  23.388  1.00 17.39 ? 178 LYS   D NZ   1 
ATOM   7092 N  N    . HIS   D 1 200 ? -57.700 -3.039  17.419  1.00 12.90 ? 179 HIS   D N    1 
ATOM   7093 C  CA   . HIS   D 1 200 ? -56.743 -2.010  17.030  1.00 12.13 ? 179 HIS   D CA   1 
ATOM   7094 C  C    . HIS   D 1 200 ? -57.464 -0.669  16.950  1.00 12.68 ? 179 HIS   D C    1 
ATOM   7095 O  O    . HIS   D 1 200 ? -56.892 0.351   17.358  1.00 13.22 ? 179 HIS   D O    1 
ATOM   7096 C  CB   . HIS   D 1 200 ? -56.131 -2.332  15.666  1.00 13.84 ? 179 HIS   D CB   1 
ATOM   7097 C  CG   . HIS   D 1 200 ? -54.915 -3.172  15.738  1.00 16.54 ? 179 HIS   D CG   1 
ATOM   7098 N  ND1  . HIS   D 1 200 ? -53.650 -2.636  15.750  1.00 18.99 ? 179 HIS   D ND1  1 
ATOM   7099 C  CD2  . HIS   D 1 200 ? -54.770 -4.516  15.777  1.00 17.61 ? 179 HIS   D CD2  1 
ATOM   7100 C  CE1  . HIS   D 1 200 ? -52.770 -3.628  15.793  1.00 19.09 ? 179 HIS   D CE1  1 
ATOM   7101 N  NE2  . HIS   D 1 200 ? -53.428 -4.772  15.803  1.00 18.69 ? 179 HIS   D NE2  1 
ATOM   7102 N  N    . ALA   D 1 201 ? -58.699 -0.653  16.403  1.00 12.41 ? 180 ALA   D N    1 
ATOM   7103 C  CA   . ALA   D 1 201 ? -59.429 0.617   16.370  1.00 12.53 ? 180 ALA   D CA   1 
ATOM   7104 C  C    . ALA   D 1 201 ? -59.608 1.185   17.780  1.00 13.07 ? 180 ALA   D C    1 
ATOM   7105 O  O    . ALA   D 1 201 ? -59.566 2.411   17.984  1.00 13.16 ? 180 ALA   D O    1 
ATOM   7106 C  CB   . ALA   D 1 201 ? -60.766 0.430   15.684  1.00 13.25 ? 180 ALA   D CB   1 
ATOM   7107 N  N    . LEU   D 1 202 ? -59.793 0.296   18.758  1.00 13.15 ? 181 LEU   D N    1 
ATOM   7108 C  CA   . LEU   D 1 202 ? -60.000 0.699   20.141  1.00 14.40 ? 181 LEU   D CA   1 
ATOM   7109 C  C    . LEU   D 1 202 ? -58.744 1.382   20.701  1.00 13.91 ? 181 LEU   D C    1 
ATOM   7110 O  O    . LEU   D 1 202 ? -58.856 2.351   21.451  1.00 14.39 ? 181 LEU   D O    1 
ATOM   7111 C  CB   . LEU   D 1 202 ? -60.455 -0.492  20.988  1.00 14.81 ? 181 LEU   D CB   1 
ATOM   7112 C  CG   . LEU   D 1 202 ? -60.904 -0.149  22.414  1.00 14.76 ? 181 LEU   D CG   1 
ATOM   7113 C  CD1  . LEU   D 1 202 ? -62.064 0.856   22.460  1.00 15.12 ? 181 LEU   D CD1  1 
ATOM   7114 C  CD2  . LEU   D 1 202 ? -61.300 -1.485  23.084  1.00 16.38 ? 181 LEU   D CD2  1 
ATOM   7115 N  N    . VAL   D 1 203 ? -57.545 0.950   20.268  1.00 13.31 ? 182 VAL   D N    1 
ATOM   7116 C  CA   . VAL   D 1 203 ? -56.309 1.628   20.641  1.00 14.21 ? 182 VAL   D CA   1 
ATOM   7117 C  C    . VAL   D 1 203 ? -56.329 3.030   20.041  1.00 12.85 ? 182 VAL   D C    1 
ATOM   7118 O  O    . VAL   D 1 203 ? -55.985 3.995   20.724  1.00 14.31 ? 182 VAL   D O    1 
ATOM   7119 C  CB   . VAL   D 1 203 ? -55.078 0.841   20.146  1.00 14.86 ? 182 VAL   D CB   1 
ATOM   7120 C  CG1  . VAL   D 1 203 ? -53.780 1.644   20.342  1.00 16.20 ? 182 VAL   D CG1  1 
ATOM   7121 C  CG2  . VAL   D 1 203 ? -54.997 -0.509  20.859  1.00 16.09 ? 182 VAL   D CG2  1 
ATOM   7122 N  N    . GLY   D 1 204 ? -56.702 3.138   18.754  1.00 13.15 ? 183 GLY   D N    1 
ATOM   7123 C  CA   . GLY   D 1 204 ? -56.785 4.455   18.137  1.00 13.92 ? 183 GLY   D CA   1 
ATOM   7124 C  C    . GLY   D 1 204 ? -57.736 5.380   18.882  1.00 13.54 ? 183 GLY   D C    1 
ATOM   7125 O  O    . GLY   D 1 204 ? -57.439 6.549   19.065  1.00 13.92 ? 183 GLY   D O    1 
ATOM   7126 N  N    . LEU   D 1 205 ? -58.888 4.859   19.291  1.00 13.36 ? 184 LEU   D N    1 
ATOM   7127 C  CA   . LEU   D 1 205 ? -59.868 5.642   20.030  1.00 13.57 ? 184 LEU   D CA   1 
ATOM   7128 C  C    . LEU   D 1 205 ? -59.266 6.110   21.348  1.00 13.45 ? 184 LEU   D C    1 
ATOM   7129 O  O    . LEU   D 1 205 ? -59.424 7.281   21.734  1.00 14.49 ? 184 LEU   D O    1 
ATOM   7130 C  CB   . LEU   D 1 205 ? -61.145 4.856   20.297  1.00 13.91 ? 184 LEU   D CB   1 
ATOM   7131 C  CG   . LEU   D 1 205 ? -62.170 5.556   21.191  1.00 14.81 ? 184 LEU   D CG   1 
ATOM   7132 C  CD1  . LEU   D 1 205 ? -62.717 6.881   20.619  1.00 15.77 ? 184 LEU   D CD1  1 
ATOM   7133 C  CD2  . LEU   D 1 205 ? -63.306 4.605   21.473  1.00 15.97 ? 184 LEU   D CD2  1 
ATOM   7134 N  N    . THR   D 1 206 ? -58.596 5.190   22.049  1.00 13.29 ? 185 THR   D N    1 
ATOM   7135 C  CA   . THR   D 1 206 ? -58.005 5.518   23.340  1.00 13.18 ? 185 THR   D CA   1 
ATOM   7136 C  C    . THR   D 1 206 ? -57.076 6.718   23.180  1.00 13.73 ? 185 THR   D C    1 
ATOM   7137 O  O    . THR   D 1 206 ? -57.136 7.677   23.969  1.00 14.09 ? 185 THR   D O    1 
ATOM   7138 C  CB   . THR   D 1 206 ? -57.282 4.303   23.914  1.00 14.14 ? 185 THR   D CB   1 
ATOM   7139 O  OG1  . THR   D 1 206 ? -58.216 3.239   24.069  1.00 14.63 ? 185 THR   D OG1  1 
ATOM   7140 C  CG2  . THR   D 1 206 ? -56.737 4.602   25.305  1.00 14.57 ? 185 THR   D CG2  1 
ATOM   7141 N  N    . GLN   D 1 207 ? -56.208 6.666   22.156  1.00 13.10 ? 186 GLN   D N    1 
ATOM   7142 C  CA   . GLN   D 1 207 ? -55.273 7.759   21.927  1.00 15.05 ? 186 GLN   D CA   1 
ATOM   7143 C  C    . GLN   D 1 207 ? -55.987 9.034   21.497  1.00 13.68 ? 186 GLN   D C    1 
ATOM   7144 O  O    . GLN   D 1 207 ? -55.683 10.107  22.029  1.00 14.24 ? 186 GLN   D O    1 
ATOM   7145 C  CB   . GLN   D 1 207 ? -54.254 7.323   20.881  1.00 15.66 ? 186 GLN   D CB   1 
ATOM   7146 C  CG   . GLN   D 1 207 ? -53.406 6.157   21.379  1.00 19.39 ? 186 GLN   D CG   1 
ATOM   7147 C  CD   . GLN   D 1 207 ? -52.457 5.606   20.339  1.00 22.65 ? 186 GLN   D CD   1 
ATOM   7148 O  OE1  . GLN   D 1 207 ? -51.464 4.958   20.691  1.00 29.74 ? 186 GLN   D OE1  1 
ATOM   7149 N  NE2  . GLN   D 1 207 ? -52.731 5.877   19.075  1.00 24.98 ? 186 GLN   D NE2  1 
ATOM   7150 N  N    . SER   D 1 208 ? -56.873 8.950   20.488  1.00 14.04 ? 187 SER   D N    1 
ATOM   7151 C  CA   . SER   D 1 208 ? -57.510 10.146  19.946  1.00 13.79 ? 187 SER   D CA   1 
ATOM   7152 C  C    . SER   D 1 208 ? -58.387 10.817  20.999  1.00 13.84 ? 187 SER   D C    1 
ATOM   7153 O  O    . SER   D 1 208 ? -58.398 12.059  21.110  1.00 14.47 ? 187 SER   D O    1 
ATOM   7154 C  CB   . SER   D 1 208 ? -58.329 9.835   18.696  1.00 15.46 ? 187 SER   D CB   1 
ATOM   7155 O  OG   . SER   D 1 208 ? -57.531 9.547   17.553  1.00 17.04 ? 187 SER   D OG   1 
ATOM   7156 N  N    . ALA   D 1 209 ? -59.148 10.009  21.737  1.00 13.84 ? 188 ALA   D N    1 
ATOM   7157 C  CA   . ALA   D 1 209 ? -60.009 10.564  22.772  1.00 14.20 ? 188 ALA   D CA   1 
ATOM   7158 C  C    . ALA   D 1 209 ? -59.202 11.113  23.949  1.00 14.78 ? 188 ALA   D C    1 
ATOM   7159 O  O    . ALA   D 1 209 ? -59.572 12.137  24.525  1.00 15.39 ? 188 ALA   D O    1 
ATOM   7160 C  CB   . ALA   D 1 209 ? -61.061 9.562   23.210  1.00 15.55 ? 188 ALA   D CB   1 
ATOM   7161 N  N    . ALA   D 1 210 ? -58.066 10.496  24.297  1.00 14.44 ? 189 ALA   D N    1 
ATOM   7162 C  CA   . ALA   D 1 210 ? -57.229 11.073  25.348  1.00 14.05 ? 189 ALA   D CA   1 
ATOM   7163 C  C    . ALA   D 1 210 ? -56.791 12.476  24.935  1.00 14.38 ? 189 ALA   D C    1 
ATOM   7164 O  O    . ALA   D 1 210 ? -56.840 13.415  25.733  1.00 15.33 ? 189 ALA   D O    1 
ATOM   7165 C  CB   . ALA   D 1 210 ? -56.019 10.179  25.618  1.00 14.83 ? 189 ALA   D CB   1 
ATOM   7166 N  N    . LEU   D 1 211 ? -56.344 12.624  23.682  1.00 15.28 ? 190 LEU   D N    1 
ATOM   7167 C  CA   . LEU   D 1 211 ? -55.859 13.925  23.241  1.00 16.19 ? 190 LEU   D CA   1 
ATOM   7168 C  C    . LEU   D 1 211 ? -56.986 14.958  23.274  1.00 17.78 ? 190 LEU   D C    1 
ATOM   7169 O  O    . LEU   D 1 211 ? -56.812 16.092  23.737  1.00 20.00 ? 190 LEU   D O    1 
ATOM   7170 C  CB   . LEU   D 1 211 ? -55.338 13.704  21.824  1.00 17.14 ? 190 LEU   D CB   1 
ATOM   7171 C  CG   . LEU   D 1 211 ? -54.844 14.963  21.106  1.00 20.01 ? 190 LEU   D CG   1 
ATOM   7172 C  CD1  . LEU   D 1 211 ? -53.554 15.469  21.754  1.00 21.73 ? 190 LEU   D CD1  1 
ATOM   7173 C  CD2  . LEU   D 1 211 ? -54.622 14.680  19.635  1.00 20.91 ? 190 LEU   D CD2  1 
ATOM   7174 N  N    . GLU   D 1 212 ? -58.154 14.568  22.759  1.00 16.76 ? 191 GLU   D N    1 
ATOM   7175 C  CA   . GLU   D 1 212 ? -59.244 15.517  22.559  1.00 16.70 ? 191 GLU   D CA   1 
ATOM   7176 C  C    . GLU   D 1 212 ? -59.965 15.867  23.858  1.00 17.57 ? 191 GLU   D C    1 
ATOM   7177 O  O    . GLU   D 1 212 ? -60.464 16.996  23.982  1.00 18.72 ? 191 GLU   D O    1 
ATOM   7178 C  CB   . GLU   D 1 212 ? -60.215 14.941  21.532  1.00 18.14 ? 191 GLU   D CB   1 
ATOM   7179 C  CG   . GLU   D 1 212 ? -61.316 15.915  21.127  1.00 20.32 ? 191 GLU   D CG   1 
ATOM   7180 C  CD   . GLU   D 1 212 ? -62.141 15.346  19.993  1.00 24.10 ? 191 GLU   D CD   1 
ATOM   7181 O  OE1  . GLU   D 1 212 ? -63.169 15.966  19.656  1.00 25.18 ? 191 GLU   D OE1  1 
ATOM   7182 O  OE2  . GLU   D 1 212 ? -61.727 14.306  19.419  1.00 24.54 ? 191 GLU   D OE2  1 
ATOM   7183 N  N    . LEU   D 1 213 ? -60.026 14.929  24.808  1.00 15.85 ? 192 LEU   D N    1 
ATOM   7184 C  CA   . LEU   D 1 213 ? -60.796 15.131  26.031  1.00 15.62 ? 192 LEU   D CA   1 
ATOM   7185 C  C    . LEU   D 1 213 ? -59.951 15.667  27.191  1.00 16.03 ? 192 LEU   D C    1 
ATOM   7186 O  O    . LEU   D 1 213 ? -60.511 16.083  28.208  1.00 18.01 ? 192 LEU   D O    1 
ATOM   7187 C  CB   . LEU   D 1 213 ? -61.589 13.875  26.410  1.00 15.29 ? 192 LEU   D CB   1 
ATOM   7188 C  CG   . LEU   D 1 213 ? -62.573 13.413  25.328  1.00 15.99 ? 192 LEU   D CG   1 
ATOM   7189 C  CD1  . LEU   D 1 213 ? -63.316 12.182  25.825  1.00 17.11 ? 192 LEU   D CD1  1 
ATOM   7190 C  CD2  . LEU   D 1 213 ? -63.543 14.549  24.984  1.00 16.30 ? 192 LEU   D CD2  1 
ATOM   7191 N  N    . ALA   D 1 214 ? -58.623 15.653  27.041  1.00 16.81 ? 193 ALA   D N    1 
ATOM   7192 C  CA   . ALA   D 1 214 ? -57.715 16.151  28.072  1.00 17.80 ? 193 ALA   D CA   1 
ATOM   7193 C  C    . ALA   D 1 214 ? -58.049 17.589  28.497  1.00 20.84 ? 193 ALA   D C    1 
ATOM   7194 O  O    . ALA   D 1 214 ? -57.997 17.884  29.695  1.00 21.49 ? 193 ALA   D O    1 
ATOM   7195 C  CB   . ALA   D 1 214 ? -56.291 16.026  27.579  1.00 19.40 ? 193 ALA   D CB   1 
ATOM   7196 N  N    . PRO   D 1 215 ? -58.361 18.540  27.579  1.00 23.24 ? 194 PRO   D N    1 
ATOM   7197 C  CA   . PRO   D 1 215 ? -58.728 19.900  28.000  1.00 25.73 ? 194 PRO   D CA   1 
ATOM   7198 C  C    . PRO   D 1 215 ? -59.999 19.950  28.849  1.00 27.02 ? 194 PRO   D C    1 
ATOM   7199 O  O    . PRO   D 1 215 ? -60.275 20.949  29.519  1.00 30.34 ? 194 PRO   D O    1 
ATOM   7200 C  CB   . PRO   D 1 215 ? -58.866 20.668  26.680  1.00 28.11 ? 194 PRO   D CB   1 
ATOM   7201 C  CG   . PRO   D 1 215 ? -58.106 19.831  25.674  1.00 29.00 ? 194 PRO   D CG   1 
ATOM   7202 C  CD   . PRO   D 1 215 ? -58.351 18.392  26.113  1.00 25.59 ? 194 PRO   D CD   1 
ATOM   7203 N  N    . TYR   D 1 216 ? -60.776 18.862  28.854  1.00 25.63 ? 195 TYR   D N    1 
ATOM   7204 C  CA   . TYR   D 1 216 ? -61.993 18.815  29.652  1.00 26.60 ? 195 TYR   D CA   1 
ATOM   7205 C  C    . TYR   D 1 216 ? -61.755 18.051  30.952  1.00 25.81 ? 195 TYR   D C    1 
ATOM   7206 O  O    . TYR   D 1 216 ? -62.695 17.814  31.710  1.00 28.46 ? 195 TYR   D O    1 
ATOM   7207 C  CB   . TYR   D 1 216 ? -63.173 18.197  28.898  1.00 26.92 ? 195 TYR   D CB   1 
ATOM   7208 C  CG   . TYR   D 1 216 ? -63.497 18.901  27.590  0.70 28.47 ? 195 TYR   D CG   1 
ATOM   7209 C  CD1  . TYR   D 1 216 ? -64.339 20.010  27.566  0.70 30.59 ? 195 TYR   D CD1  1 
ATOM   7210 C  CD2  . TYR   D 1 216 ? -62.942 18.473  26.391  0.70 28.07 ? 195 TYR   D CD2  1 
ATOM   7211 C  CE1  . TYR   D 1 216 ? -64.627 20.661  26.378  0.70 32.07 ? 195 TYR   D CE1  1 
ATOM   7212 C  CE2  . TYR   D 1 216 ? -63.220 19.120  25.200  0.70 30.97 ? 195 TYR   D CE2  1 
ATOM   7213 C  CZ   . TYR   D 1 216 ? -64.065 20.215  25.196  0.70 32.94 ? 195 TYR   D CZ   1 
ATOM   7214 O  OH   . TYR   D 1 216 ? -64.344 20.852  24.024  0.70 34.61 ? 195 TYR   D OH   1 
ATOM   7215 N  N    . GLY   D 1 217 ? -60.504 17.632  31.186  1.00 24.09 ? 196 GLY   D N    1 
ATOM   7216 C  CA   . GLY   D 1 217 ? -60.133 16.901  32.390  1.00 22.59 ? 196 GLY   D CA   1 
ATOM   7217 C  C    . GLY   D 1 217 ? -60.595 15.440  32.383  1.00 21.52 ? 196 GLY   D C    1 
ATOM   7218 O  O    . GLY   D 1 217 ? -60.609 14.807  33.440  1.00 24.16 ? 196 GLY   D O    1 
ATOM   7219 N  N    . ILE   D 1 218 ? -60.975 14.906  31.204  1.00 16.90 ? 197 ILE   D N    1 
ATOM   7220 C  CA   . ILE   D 1 218 ? -61.364 13.500  31.088  1.00 16.36 ? 197 ILE   D CA   1 
ATOM   7221 C  C    . ILE   D 1 218 ? -60.139 12.721  30.611  1.00 15.20 ? 197 ILE   D C    1 
ATOM   7222 O  O    . ILE   D 1 218 ? -59.638 12.971  29.523  1.00 17.68 ? 197 ILE   D O    1 
ATOM   7223 C  CB   . ILE   D 1 218 ? -62.549 13.272  30.117  1.00 15.49 ? 197 ILE   D CB   1 
ATOM   7224 C  CG1  . ILE   D 1 218 ? -63.823 14.069  30.531  1.00 18.34 ? 197 ILE   D CG1  1 
ATOM   7225 C  CG2  . ILE   D 1 218 ? -62.850 11.772  30.002  1.00 16.84 ? 197 ILE   D CG2  1 
ATOM   7226 C  CD1  . ILE   D 1 218 ? -64.850 14.204  29.414  1.00 19.17 ? 197 ILE   D CD1  1 
ATOM   7227 N  N    . ARG   D 1 219 ? -59.729 11.743  31.419  1.00 15.73 ? 198 ARG   D N    1 
ATOM   7228 C  CA   . ARG   D 1 219 ? -58.618 10.877  31.052  1.00 14.22 ? 198 ARG   D CA   1 
ATOM   7229 C  C    . ARG   D 1 219 ? -59.181 9.676   30.307  1.00 14.92 ? 198 ARG   D C    1 
ATOM   7230 O  O    . ARG   D 1 219 ? -60.295 9.243   30.588  1.00 15.94 ? 198 ARG   D O    1 
ATOM   7231 C  CB   . ARG   D 1 219 ? -57.851 10.472  32.317  1.00 14.27 ? 198 ARG   D CB   1 
ATOM   7232 C  CG   . ARG   D 1 219 ? -57.185 11.676  32.976  1.00 15.37 ? 198 ARG   D CG   1 
ATOM   7233 C  CD   . ARG   D 1 219 ? -56.437 11.321  34.264  1.00 14.28 ? 198 ARG   D CD   1 
ATOM   7234 N  NE   . ARG   D 1 219 ? -57.285 10.628  35.240  1.00 16.26 ? 198 ARG   D NE   1 
ATOM   7235 C  CZ   . ARG   D 1 219 ? -57.342 9.326   35.423  1.00 16.64 ? 198 ARG   D CZ   1 
ATOM   7236 N  NH1  . ARG   D 1 219 ? -56.504 8.516   34.801  1.00 16.35 ? 198 ARG   D NH1  1 
ATOM   7237 N  NH2  . ARG   D 1 219 ? -58.239 8.839   36.255  1.00 18.98 ? 198 ARG   D NH2  1 
ATOM   7238 N  N    . VAL   D 1 220 ? -58.390 9.148   29.380  1.00 13.43 ? 199 VAL   D N    1 
ATOM   7239 C  CA   . VAL   D 1 220 ? -58.818 7.985   28.612  1.00 12.65 ? 199 VAL   D CA   1 
ATOM   7240 C  C    . VAL   D 1 220 ? -57.661 7.001   28.534  1.00 12.97 ? 199 VAL   D C    1 
ATOM   7241 O  O    . VAL   D 1 220 ? -56.625 7.332   27.957  1.00 14.20 ? 199 VAL   D O    1 
ATOM   7242 C  CB   . VAL   D 1 220 ? -59.314 8.376   27.203  1.00 13.04 ? 199 VAL   D CB   1 
ATOM   7243 C  CG1  . VAL   D 1 220 ? -59.883 7.170   26.461  1.00 14.68 ? 199 VAL   D CG1  1 
ATOM   7244 C  CG2  . VAL   D 1 220 ? -60.340 9.526   27.240  1.00 13.67 ? 199 VAL   D CG2  1 
ATOM   7245 N  N    . ASN   D 1 221 ? -57.876 5.770   29.021  1.00 13.59 ? 200 ASN   D N    1 
ATOM   7246 C  CA   . ASN   D 1 221 ? -56.782 4.818   29.124  1.00 13.27 ? 200 ASN   D CA   1 
ATOM   7247 C  C    . ASN   D 1 221 ? -57.337 3.450   28.775  1.00 14.90 ? 200 ASN   D C    1 
ATOM   7248 O  O    . ASN   D 1 221 ? -58.540 3.281   28.593  1.00 14.33 ? 200 ASN   D O    1 
ATOM   7249 C  CB   . ASN   D 1 221 ? -56.182 4.790   30.533  1.00 13.07 ? 200 ASN   D CB   1 
ATOM   7250 C  CG   . ASN   D 1 221 ? -55.506 6.099   30.881  1.00 13.70 ? 200 ASN   D CG   1 
ATOM   7251 O  OD1  . ASN   D 1 221 ? -54.463 6.424   30.294  1.00 14.01 ? 200 ASN   D OD1  1 
ATOM   7252 N  ND2  . ASN   D 1 221 ? -56.066 6.838   31.834  1.00 14.40 ? 200 ASN   D ND2  1 
ATOM   7253 N  N    . GLY   D 1 222 ? -56.429 2.479   28.663  1.00 13.80 ? 201 GLY   D N    1 
ATOM   7254 C  CA   . GLY   D 1 222 ? -56.870 1.120   28.409  1.00 14.15 ? 201 GLY   D CA   1 
ATOM   7255 C  C    . GLY   D 1 222 ? -56.174 0.115   29.315  1.00 13.36 ? 201 GLY   D C    1 
ATOM   7256 O  O    . GLY   D 1 222 ? -55.091 0.350   29.857  1.00 14.49 ? 201 GLY   D O    1 
ATOM   7257 N  N    . VAL   D 1 223 ? -56.793 -1.060  29.404  1.00 13.32 ? 202 VAL   D N    1 
ATOM   7258 C  CA   . VAL   D 1 223 ? -56.207 -2.215  30.068  1.00 12.92 ? 202 VAL   D CA   1 
ATOM   7259 C  C    . VAL   D 1 223 ? -56.227 -3.342  29.050  1.00 13.61 ? 202 VAL   D C    1 
ATOM   7260 O  O    . VAL   D 1 223 ? -57.275 -3.592  28.457  1.00 14.77 ? 202 VAL   D O    1 
ATOM   7261 C  CB   . VAL   D 1 223 ? -57.027 -2.617  31.312  1.00 14.22 ? 202 VAL   D CB   1 
ATOM   7262 C  CG1  . VAL   D 1 223 ? -56.554 -3.954  31.878  1.00 14.45 ? 202 VAL   D CG1  1 
ATOM   7263 C  CG2  . VAL   D 1 223 ? -56.916 -1.545  32.377  1.00 14.69 ? 202 VAL   D CG2  1 
ATOM   7264 N  N    . ALA   D 1 224 ? -55.066 -3.976  28.834  1.00 14.30 ? 203 ALA   D N    1 
ATOM   7265 C  CA   . ALA   D 1 224 ? -54.951 -4.989  27.793  1.00 14.22 ? 203 ALA   D CA   1 
ATOM   7266 C  C    . ALA   D 1 224 ? -54.634 -6.351  28.403  1.00 14.20 ? 203 ALA   D C    1 
ATOM   7267 O  O    . ALA   D 1 224 ? -53.473 -6.673  28.655  1.00 14.95 ? 203 ALA   D O    1 
ATOM   7268 C  CB   . ALA   D 1 224 ? -53.891 -4.578  26.793  1.00 13.22 ? 203 ALA   D CB   1 
ATOM   7269 N  N    . PRO   D 1 225 ? -55.646 -7.208  28.642  1.00 14.34 ? 204 PRO   D N    1 
ATOM   7270 C  CA   . PRO   D 1 225 ? -55.372 -8.560  29.109  1.00 15.54 ? 204 PRO   D CA   1 
ATOM   7271 C  C    . PRO   D 1 225 ? -54.685 -9.339  28.007  1.00 16.90 ? 204 PRO   D C    1 
ATOM   7272 O  O    . PRO   D 1 225 ? -54.841 -9.050  26.820  1.00 17.06 ? 204 PRO   D O    1 
ATOM   7273 C  CB   . PRO   D 1 225 ? -56.768 -9.134  29.361  1.00 15.74 ? 204 PRO   D CB   1 
ATOM   7274 C  CG   . PRO   D 1 225 ? -57.659 -7.921  29.485  1.00 17.24 ? 204 PRO   D CG   1 
ATOM   7275 C  CD   . PRO   D 1 225 ? -57.084 -6.956  28.466  1.00 15.25 ? 204 PRO   D CD   1 
ATOM   7276 N  N    . GLY   D 1 226 ? -53.995 -10.397 28.441  1.00 17.26 ? 205 GLY   D N    1 
ATOM   7277 C  CA   . GLY   D 1 226 ? -53.507 -11.406 27.523  1.00 19.11 ? 205 GLY   D CA   1 
ATOM   7278 C  C    . GLY   D 1 226 ? -54.492 -12.566 27.487  1.00 21.18 ? 205 GLY   D C    1 
ATOM   7279 O  O    . GLY   D 1 226 ? -55.477 -12.537 26.739  1.00 24.72 ? 205 GLY   D O    1 
ATOM   7280 N  N    . VAL   D 1 227 ? -54.216 -13.595 28.286  1.00 18.28 ? 206 VAL   D N    1 
ATOM   7281 C  CA   . VAL   D 1 227 ? -55.278 -14.554 28.519  1.00 18.83 ? 206 VAL   D CA   1 
ATOM   7282 C  C    . VAL   D 1 227 ? -55.758 -14.391 29.949  1.00 19.03 ? 206 VAL   D C    1 
ATOM   7283 O  O    . VAL   D 1 227 ? -54.979 -14.390 30.902  1.00 20.17 ? 206 VAL   D O    1 
ATOM   7284 C  CB   . VAL   D 1 227 ? -54.893 -16.006 28.200  1.00 22.49 ? 206 VAL   D CB   1 
ATOM   7285 C  CG1  . VAL   D 1 227 ? -54.709 -16.203 26.697  1.00 25.11 ? 206 VAL   D CG1  1 
ATOM   7286 C  CG2  . VAL   D 1 227 ? -53.652 -16.429 28.960  1.00 23.12 ? 206 VAL   D CG2  1 
ATOM   7287 N  N    . SER   D 1 228 ? -57.061 -14.172 30.063  1.00 19.43 ? 207 SER   D N    1 
ATOM   7288 C  CA   . SER   D 1 228 ? -57.720 -14.083 31.344  1.00 21.23 ? 207 SER   D CA   1 
ATOM   7289 C  C    . SER   D 1 228 ? -58.756 -15.191 31.320  1.00 22.68 ? 207 SER   D C    1 
ATOM   7290 O  O    . SER   D 1 228 ? -58.427 -16.287 30.874  1.00 23.56 ? 207 SER   D O    1 
ATOM   7291 C  CB   . SER   D 1 228 ? -58.311 -12.709 31.561  1.00 20.40 ? 207 SER   D CB   1 
ATOM   7292 O  OG   . SER   D 1 228 ? -58.885 -12.581 32.857  1.00 21.33 ? 207 SER   D OG   1 
ATOM   7293 N  N    . LEU   D 1 229 ? -59.988 -14.899 31.730  1.00 22.55 ? 208 LEU   D N    1 
ATOM   7294 C  CA   . LEU   D 1 229 ? -60.982 -15.964 31.769  1.00 24.15 ? 208 LEU   D CA   1 
ATOM   7295 C  C    . LEU   D 1 229 ? -61.134 -16.574 30.378  1.00 23.74 ? 208 LEU   D C    1 
ATOM   7296 O  O    . LEU   D 1 229 ? -61.521 -15.897 29.432  1.00 23.74 ? 208 LEU   D O    1 
ATOM   7297 C  CB   . LEU   D 1 229 ? -62.317 -15.437 32.287  1.00 25.32 ? 208 LEU   D CB   1 
ATOM   7298 C  CG   . LEU   D 1 229 ? -62.303 -14.827 33.692  1.00 26.55 ? 208 LEU   D CG   1 
ATOM   7299 C  CD1  . LEU   D 1 229 ? -63.742 -14.586 34.144  1.00 28.44 ? 208 LEU   D CD1  1 
ATOM   7300 C  CD2  . LEU   D 1 229 ? -61.571 -15.691 34.703  1.00 28.85 ? 208 LEU   D CD2  1 
ATOM   7301 N  N    . LEU   D 1 230 ? -60.882 -17.886 30.285  1.00 23.67 ? 209 LEU   D N    1 
ATOM   7302 C  CA   . LEU   D 1 230 ? -60.892 -18.560 29.003  1.00 22.71 ? 209 LEU   D CA   1 
ATOM   7303 C  C    . LEU   D 1 230 ? -62.327 -18.799 28.544  1.00 25.70 ? 209 LEU   D C    1 
ATOM   7304 O  O    . LEU   D 1 230 ? -63.255 -18.757 29.354  1.00 26.59 ? 209 LEU   D O    1 
ATOM   7305 C  CB   . LEU   D 1 230 ? -60.056 -19.834 29.135  1.00 28.10 ? 209 LEU   D CB   1 
ATOM   7306 C  CG   . LEU   D 1 230 ? -58.557 -19.551 29.300  1.00 30.69 ? 209 LEU   D CG   1 
ATOM   7307 C  CD1  . LEU   D 1 230 ? -57.747 -20.720 29.846  1.00 32.43 ? 209 LEU   D CD1  1 
ATOM   7308 C  CD2  . LEU   D 1 230 ? -57.975 -19.065 27.987  1.00 32.45 ? 209 LEU   D CD2  1 
ATOM   7309 N  N    . PRO   D 1 231 ? -62.551 -19.028 27.230  1.00 26.70 ? 210 PRO   D N    1 
ATOM   7310 C  CA   . PRO   D 1 231 ? -63.904 -19.143 26.693  1.00 28.89 ? 210 PRO   D CA   1 
ATOM   7311 C  C    . PRO   D 1 231 ? -64.650 -20.293 27.362  1.00 30.64 ? 210 PRO   D C    1 
ATOM   7312 O  O    . PRO   D 1 231 ? -64.060 -21.319 27.698  1.00 32.17 ? 210 PRO   D O    1 
ATOM   7313 C  CB   . PRO   D 1 231 ? -63.710 -19.352 25.183  1.00 28.93 ? 210 PRO   D CB   1 
ATOM   7314 C  CG   . PRO   D 1 231 ? -62.299 -18.876 24.925  1.00 28.80 ? 210 PRO   D CG   1 
ATOM   7315 C  CD   . PRO   D 1 231 ? -61.518 -19.198 26.189  1.00 27.57 ? 210 PRO   D CD   1 
ATOM   7316 N  N    . VAL   D 1 232 ? -65.957 -20.089 27.556  1.00 33.06 ? 211 VAL   D N    1 
ATOM   7317 C  CA   . VAL   D 1 232 ? -66.789 -21.011 28.312  1.00 35.56 ? 211 VAL   D CA   1 
ATOM   7318 C  C    . VAL   D 1 232 ? -66.812 -22.380 27.622  1.00 36.67 ? 211 VAL   D C    1 
ATOM   7319 O  O    . VAL   D 1 232 ? -66.923 -23.408 28.288  1.00 39.22 ? 211 VAL   D O    1 
ATOM   7320 C  CB   . VAL   D 1 232 ? -68.202 -20.429 28.544  1.00 39.48 ? 211 VAL   D CB   1 
ATOM   7321 C  CG1  . VAL   D 1 232 ? -68.172 -19.183 29.429  1.00 41.70 ? 211 VAL   D CG1  1 
ATOM   7322 C  CG2  . VAL   D 1 232 ? -68.924 -20.118 27.240  1.00 43.11 ? 211 VAL   D CG2  1 
ATOM   7323 N  N    . ALA   D 1 233 ? -66.667 -22.381 26.292  1.00 35.76 ? 212 ALA   D N    1 
ATOM   7324 C  CA   . ALA   D 1 233 ? -66.823 -23.572 25.468  1.00 38.42 ? 212 ALA   D CA   1 
ATOM   7325 C  C    . ALA   D 1 233 ? -65.549 -24.418 25.465  1.00 39.05 ? 212 ALA   D C    1 
ATOM   7326 O  O    . ALA   D 1 233 ? -65.564 -25.570 25.026  1.00 39.27 ? 212 ALA   D O    1 
ATOM   7327 C  CB   . ALA   D 1 233 ? -67.195 -23.163 24.061  1.00 37.73 ? 212 ALA   D CB   1 
ATOM   7328 N  N    . MET   D 1 234 ? -64.448 -23.838 25.958  1.00 35.34 ? 213 MET   D N    1 
ATOM   7329 C  CA   . MET   D 1 234 ? -63.134 -24.443 25.807  1.00 32.68 ? 213 MET   D CA   1 
ATOM   7330 C  C    . MET   D 1 234 ? -62.955 -25.580 26.812  1.00 30.52 ? 213 MET   D C    1 
ATOM   7331 O  O    . MET   D 1 234 ? -63.222 -25.420 27.997  1.00 29.81 ? 213 MET   D O    1 
ATOM   7332 C  CB   . MET   D 1 234 ? -62.038 -23.387 25.987  1.00 32.33 ? 213 MET   D CB   1 
ATOM   7333 C  CG   . MET   D 1 234 ? -60.671 -23.866 25.553  1.00 33.77 ? 213 MET   D CG   1 
ATOM   7334 S  SD   . MET   D 1 234 ? -59.393 -22.600 25.699  1.00 33.48 ? 213 MET   D SD   1 
ATOM   7335 C  CE   . MET   D 1 234 ? -59.640 -21.690 24.168  1.00 31.88 ? 213 MET   D CE   1 
ATOM   7336 N  N    . GLY   D 1 235 ? -62.480 -26.731 26.321  1.00 30.63 ? 214 GLY   D N    1 
ATOM   7337 C  CA   . GLY   D 1 235 ? -62.258 -27.897 27.160  1.00 28.33 ? 214 GLY   D CA   1 
ATOM   7338 C  C    . GLY   D 1 235 ? -60.973 -27.768 27.976  1.00 28.90 ? 214 GLY   D C    1 
ATOM   7339 O  O    . GLY   D 1 235 ? -60.161 -26.871 27.737  1.00 28.01 ? 214 GLY   D O    1 
ATOM   7340 N  N    . GLU   D 1 236 ? -60.784 -28.690 28.928  1.00 25.99 ? 215 GLU   D N    1 
ATOM   7341 C  CA   . GLU   D 1 236 ? -59.693 -28.596 29.883  1.00 26.34 ? 215 GLU   D CA   1 
ATOM   7342 C  C    . GLU   D 1 236 ? -58.335 -28.647 29.177  1.00 27.11 ? 215 GLU   D C    1 
ATOM   7343 O  O    . GLU   D 1 236 ? -57.413 -27.939 29.587  1.00 28.44 ? 215 GLU   D O    1 
ATOM   7344 C  CB   . GLU   D 1 236 ? -59.800 -29.681 30.960  1.00 29.78 ? 215 GLU   D CB   1 
ATOM   7345 C  CG   . GLU   D 1 236 ? -61.010 -29.519 31.877  1.00 30.31 ? 215 GLU   D CG   1 
ATOM   7346 C  CD   . GLU   D 1 236 ? -60.951 -28.358 32.859  1.00 34.92 ? 215 GLU   D CD   1 
ATOM   7347 O  OE1  . GLU   D 1 236 ? -61.991 -28.097 33.495  1.00 34.18 ? 215 GLU   D OE1  1 
ATOM   7348 O  OE2  . GLU   D 1 236 ? -59.879 -27.723 33.009  1.00 35.82 ? 215 GLU   D OE2  1 
ATOM   7349 N  N    . GLU   D 1 237 ? -58.200 -29.510 28.154  1.00 28.60 ? 216 GLU   D N    1 
ATOM   7350 C  CA   . GLU   D 1 237 ? -56.901 -29.735 27.522  1.00 28.88 ? 216 GLU   D CA   1 
ATOM   7351 C  C    . GLU   D 1 237 ? -56.449 -28.450 26.830  1.00 28.86 ? 216 GLU   D C    1 
ATOM   7352 O  O    . GLU   D 1 237 ? -55.305 -28.017 26.991  1.00 26.64 ? 216 GLU   D O    1 
ATOM   7353 C  CB   . GLU   D 1 237 ? -56.905 -30.903 26.532  1.00 31.63 ? 216 GLU   D CB   1 
ATOM   7354 C  CG   . GLU   D 1 237 ? -55.517 -31.271 26.014  0.50 31.16 ? 216 GLU   D CG   1 
ATOM   7355 N  N    . GLU   D 1 238 ? -57.382 -27.846 26.096  1.00 28.81 ? 217 GLU   D N    1 
ATOM   7356 C  CA   . GLU   D 1 238 ? -57.124 -26.614 25.369  1.00 27.66 ? 217 GLU   D CA   1 
ATOM   7357 C  C    . GLU   D 1 238 ? -56.828 -25.468 26.340  1.00 26.61 ? 217 GLU   D C    1 
ATOM   7358 O  O    . GLU   D 1 238 ? -55.914 -24.679 26.093  1.00 26.18 ? 217 GLU   D O    1 
ATOM   7359 C  CB   . GLU   D 1 238 ? -58.273 -26.310 24.412  1.00 29.85 ? 217 GLU   D CB   1 
ATOM   7360 C  CG   . GLU   D 1 238 ? -57.929 -25.240 23.379  0.50 30.05 ? 217 GLU   D CG   1 
ATOM   7361 C  CD   . GLU   D 1 238 ? -59.038 -24.980 22.375  0.50 33.55 ? 217 GLU   D CD   1 
ATOM   7362 O  OE1  . GLU   D 1 238 ? -60.167 -25.475 22.583  0.50 33.30 ? 217 GLU   D OE1  1 
ATOM   7363 O  OE2  . GLU   D 1 238 ? -58.764 -24.298 21.365  0.50 33.67 ? 217 GLU   D OE2  1 
ATOM   7364 N  N    . LYS   D 1 239 ? -57.592 -25.371 27.440  1.00 24.82 ? 218 LYS   D N    1 
ATOM   7365 C  CA   . LYS   D 1 239 ? -57.333 -24.334 28.431  1.00 24.54 ? 218 LYS   D CA   1 
ATOM   7366 C  C    . LYS   D 1 239 ? -55.913 -24.473 28.978  1.00 25.44 ? 218 LYS   D C    1 
ATOM   7367 O  O    . LYS   D 1 239 ? -55.209 -23.477 29.159  1.00 24.27 ? 218 LYS   D O    1 
ATOM   7368 C  CB   . LYS   D 1 239 ? -58.363 -24.335 29.567  1.00 26.93 ? 218 LYS   D CB   1 
ATOM   7369 C  CG   . LYS   D 1 239 ? -59.746 -23.794 29.200  1.00 28.02 ? 218 LYS   D CG   1 
ATOM   7370 C  CD   . LYS   D 1 239 ? -60.627 -23.727 30.438  1.00 33.37 ? 218 LYS   D CD   1 
ATOM   7371 C  CE   . LYS   D 1 239 ? -61.996 -23.226 30.128  0.50 32.86 ? 218 LYS   D CE   1 
ATOM   7372 N  NZ   . LYS   D 1 239 ? -62.904 -23.687 31.181  0.50 33.24 ? 218 LYS   D NZ   1 
ATOM   7373 N  N    . ASP   D 1 240 ? -55.478 -25.717 29.230  1.00 24.25 ? 219 ASP   D N    1 
ATOM   7374 C  CA   . ASP   D 1 240 ? -54.148 -25.923 29.776  1.00 25.90 ? 219 ASP   D CA   1 
ATOM   7375 C  C    . ASP   D 1 240 ? -53.082 -25.548 28.745  1.00 24.77 ? 219 ASP   D C    1 
ATOM   7376 O  O    . ASP   D 1 240 ? -52.029 -25.036 29.118  1.00 25.53 ? 219 ASP   D O    1 
ATOM   7377 C  CB   . ASP   D 1 240 ? -54.011 -27.292 30.431  1.00 28.85 ? 219 ASP   D CB   1 
ATOM   7378 C  CG   . ASP   D 1 240 ? -54.691 -27.447 31.788  0.70 31.98 ? 219 ASP   D CG   1 
ATOM   7379 O  OD1  . ASP   D 1 240 ? -54.948 -26.417 32.460  0.70 32.53 ? 219 ASP   D OD1  1 
ATOM   7380 O  OD2  . ASP   D 1 240 ? -54.988 -28.604 32.160  0.70 36.21 ? 219 ASP   D OD2  1 
ATOM   7381 N  N    . LYS   D 1 241 ? -53.366 -25.768 27.455  1.00 24.36 ? 220 LYS   D N    1 
ATOM   7382 C  CA   . LYS   D 1 241 ? -52.437 -25.391 26.394  1.00 24.36 ? 220 LYS   D CA   1 
ATOM   7383 C  C    . LYS   D 1 241 ? -52.125 -23.893 26.466  1.00 25.77 ? 220 LYS   D C    1 
ATOM   7384 O  O    . LYS   D 1 241 ? -50.967 -23.493 26.341  1.00 26.52 ? 220 LYS   D O    1 
ATOM   7385 C  CB   . LYS   D 1 241 ? -52.982 -25.792 25.019  1.00 28.33 ? 220 LYS   D CB   1 
ATOM   7386 C  CG   . LYS   D 1 241 ? -52.069 -25.478 23.840  0.60 30.66 ? 220 LYS   D CG   1 
ATOM   7387 C  CD   . LYS   D 1 241 ? -52.648 -25.732 22.453  0.60 34.06 ? 220 LYS   D CD   1 
ATOM   7388 C  CE   . LYS   D 1 241 ? -53.772 -24.805 22.113  0.60 36.34 ? 220 LYS   D CE   1 
ATOM   7389 N  NZ   . LYS   D 1 241 ? -54.062 -24.801 20.677  0.60 38.79 ? 220 LYS   D NZ   1 
ATOM   7390 N  N    . TRP   D 1 242 ? -53.167 -23.079 26.658  1.00 23.72 ? 221 TRP   D N    1 
ATOM   7391 C  CA   . TRP   D 1 242 ? -52.993 -21.637 26.739  1.00 22.97 ? 221 TRP   D CA   1 
ATOM   7392 C  C    . TRP   D 1 242 ? -52.322 -21.218 28.041  1.00 22.14 ? 221 TRP   D C    1 
ATOM   7393 O  O    . TRP   D 1 242 ? -51.481 -20.313 28.052  1.00 21.00 ? 221 TRP   D O    1 
ATOM   7394 C  CB   . TRP   D 1 242 ? -54.334 -20.921 26.563  1.00 24.12 ? 221 TRP   D CB   1 
ATOM   7395 C  CG   . TRP   D 1 242 ? -54.719 -20.869 25.112  1.00 25.19 ? 221 TRP   D CG   1 
ATOM   7396 C  CD1  . TRP   D 1 242 ? -55.490 -21.756 24.415  1.00 27.38 ? 221 TRP   D CD1  1 
ATOM   7397 C  CD2  . TRP   D 1 242 ? -54.244 -19.899 24.152  1.00 27.48 ? 221 TRP   D CD2  1 
ATOM   7398 N  NE1  . TRP   D 1 242 ? -55.560 -21.380 23.098  1.00 29.78 ? 221 TRP   D NE1  1 
ATOM   7399 C  CE2  . TRP   D 1 242 ? -54.804 -20.254 22.905  1.00 28.98 ? 221 TRP   D CE2  1 
ATOM   7400 C  CE3  . TRP   D 1 242 ? -53.421 -18.768 24.229  1.00 30.06 ? 221 TRP   D CE3  1 
ATOM   7401 C  CZ2  . TRP   D 1 242 ? -54.558 -19.518 21.746  1.00 30.50 ? 221 TRP   D CZ2  1 
ATOM   7402 C  CZ3  . TRP   D 1 242 ? -53.170 -18.051 23.080  1.00 31.46 ? 221 TRP   D CZ3  1 
ATOM   7403 C  CH2  . TRP   D 1 242 ? -53.732 -18.424 21.860  1.00 32.72 ? 221 TRP   D CH2  1 
ATOM   7404 N  N    . ARG   D 1 243 ? -52.735 -21.836 29.147  1.00 22.15 ? 222 ARG   D N    1 
ATOM   7405 C  CA   . ARG   D 1 243 ? -52.115 -21.511 30.419  1.00 21.83 ? 222 ARG   D CA   1 
ATOM   7406 C  C    . ARG   D 1 243 ? -50.604 -21.714 30.353  1.00 21.39 ? 222 ARG   D C    1 
ATOM   7407 O  O    . ARG   D 1 243 ? -49.858 -20.912 30.914  1.00 21.39 ? 222 ARG   D O    1 
ATOM   7408 C  CB   . ARG   D 1 243 ? -52.694 -22.379 31.539  1.00 23.09 ? 222 ARG   D CB   1 
ATOM   7409 C  CG   . ARG   D 1 243 ? -54.150 -22.010 31.752  1.00 23.53 ? 222 ARG   D CG   1 
ATOM   7410 C  CD   . ARG   D 1 243 ? -54.741 -23.040 32.699  1.00 26.09 ? 222 ARG   D CD   1 
ATOM   7411 N  NE   . ARG   D 1 243 ? -56.071 -22.586 33.108  1.00 28.62 ? 222 ARG   D NE   1 
ATOM   7412 C  CZ   . ARG   D 1 243 ? -57.142 -23.362 33.183  1.00 31.62 ? 222 ARG   D CZ   1 
ATOM   7413 N  NH1  . ARG   D 1 243 ? -57.072 -24.638 32.833  1.00 32.83 ? 222 ARG   D NH1  1 
ATOM   7414 N  NH2  . ARG   D 1 243 ? -58.271 -22.852 33.636  1.00 32.53 ? 222 ARG   D NH2  1 
ATOM   7415 N  N    . ARG   D 1 244 ? -50.162 -22.786 29.681  1.00 22.58 ? 223 ARG   D N    1 
ATOM   7416 C  CA   . ARG   D 1 244 ? -48.755 -23.170 29.680  1.00 23.62 ? 223 ARG   D CA   1 
ATOM   7417 C  C    . ARG   D 1 244 ? -47.895 -22.169 28.908  1.00 22.51 ? 223 ARG   D C    1 
ATOM   7418 O  O    . ARG   D 1 244 ? -46.667 -22.213 28.994  1.00 26.03 ? 223 ARG   D O    1 
ATOM   7419 C  CB   . ARG   D 1 244 ? -48.526 -24.595 29.159  1.00 26.39 ? 223 ARG   D CB   1 
ATOM   7420 C  CG   . ARG   D 1 244 ? -48.881 -25.691 30.156  0.50 28.07 ? 223 ARG   D CG   1 
ATOM   7421 C  CD   . ARG   D 1 244 ? -48.507 -27.076 29.650  0.50 29.52 ? 223 ARG   D CD   1 
ATOM   7422 N  NE   . ARG   D 1 244 ? -49.048 -27.311 28.308  0.50 32.52 ? 223 ARG   D NE   1 
ATOM   7423 C  CZ   . ARG   D 1 244 ? -50.047 -28.141 28.042  0.50 32.31 ? 223 ARG   D CZ   1 
ATOM   7424 N  NH1  . ARG   D 1 244 ? -50.487 -28.272 26.804  0.50 32.57 ? 223 ARG   D NH1  1 
ATOM   7425 N  NH2  . ARG   D 1 244 ? -50.607 -28.825 29.021  0.50 33.84 ? 223 ARG   D NH2  1 
ATOM   7426 N  N    . LYS   D 1 245 ? -48.537 -21.258 28.175  1.00 21.99 ? 224 LYS   D N    1 
ATOM   7427 C  CA   . LYS   D 1 245 ? -47.784 -20.293 27.388  1.00 19.96 ? 224 LYS   D CA   1 
ATOM   7428 C  C    . LYS   D 1 245 ? -47.360 -19.097 28.244  1.00 19.25 ? 224 LYS   D C    1 
ATOM   7429 O  O    . LYS   D 1 245 ? -46.501 -18.338 27.813  1.00 19.15 ? 224 LYS   D O    1 
ATOM   7430 C  CB   . LYS   D 1 245 ? -48.615 -19.751 26.222  1.00 22.45 ? 224 LYS   D CB   1 
ATOM   7431 C  CG   . LYS   D 1 245 ? -49.088 -20.780 25.188  1.00 24.60 ? 224 LYS   D CG   1 
ATOM   7432 C  CD   . LYS   D 1 245 ? -50.082 -20.161 24.208  1.00 26.82 ? 224 LYS   D CD   1 
ATOM   7433 C  CE   . LYS   D 1 245 ? -50.774 -21.125 23.277  1.00 29.45 ? 224 LYS   D CE   1 
ATOM   7434 N  NZ   . LYS   D 1 245 ? -49.839 -21.782 22.355  1.00 29.67 ? 224 LYS   D NZ   1 
ATOM   7435 N  N    . VAL   D 1 246 ? -47.968 -18.901 29.418  1.00 17.67 ? 225 VAL   D N    1 
ATOM   7436 C  CA   . VAL   D 1 246 ? -47.786 -17.635 30.127  1.00 16.67 ? 225 VAL   D CA   1 
ATOM   7437 C  C    . VAL   D 1 246 ? -46.552 -17.716 31.027  1.00 17.13 ? 225 VAL   D C    1 
ATOM   7438 O  O    . VAL   D 1 246 ? -46.502 -18.551 31.944  1.00 17.60 ? 225 VAL   D O    1 
ATOM   7439 C  CB   . VAL   D 1 246 ? -49.031 -17.322 30.983  1.00 15.76 ? 225 VAL   D CB   1 
ATOM   7440 C  CG1  . VAL   D 1 246 ? -48.817 -16.063 31.831  1.00 18.04 ? 225 VAL   D CG1  1 
ATOM   7441 C  CG2  . VAL   D 1 246 ? -50.299 -17.198 30.148  1.00 16.49 ? 225 VAL   D CG2  1 
ATOM   7442 N  N    . PRO   D 1 247 ? -45.511 -16.876 30.818  1.00 16.99 ? 226 PRO   D N    1 
ATOM   7443 C  CA   . PRO   D 1 247 ? -44.282 -16.956 31.619  1.00 17.63 ? 226 PRO   D CA   1 
ATOM   7444 C  C    . PRO   D 1 247 ? -44.482 -16.823 33.128  1.00 17.07 ? 226 PRO   D C    1 
ATOM   7445 O  O    . PRO   D 1 247 ? -43.847 -17.545 33.908  1.00 17.41 ? 226 PRO   D O    1 
ATOM   7446 C  CB   . PRO   D 1 247 ? -43.430 -15.780 31.074  1.00 17.35 ? 226 PRO   D CB   1 
ATOM   7447 C  CG   . PRO   D 1 247 ? -43.888 -15.649 29.642  1.00 17.63 ? 226 PRO   D CG   1 
ATOM   7448 C  CD   . PRO   D 1 247 ? -45.400 -15.877 29.728  1.00 16.13 ? 226 PRO   D CD   1 
ATOM   7449 N  N    . LEU   D 1 248 ? -45.353 -15.882 33.516  1.00 16.10 ? 227 LEU   D N    1 
ATOM   7450 C  CA   . LEU   D 1 248 ? -45.536 -15.571 34.927  1.00 15.93 ? 227 LEU   D CA   1 
ATOM   7451 C  C    . LEU   D 1 248 ? -46.623 -16.469 35.492  1.00 19.37 ? 227 LEU   D C    1 
ATOM   7452 O  O    . LEU   D 1 248 ? -47.790 -16.097 35.532  1.00 20.53 ? 227 LEU   D O    1 
ATOM   7453 C  CB   . LEU   D 1 248 ? -45.911 -14.097 35.101  1.00 16.55 ? 227 LEU   D CB   1 
ATOM   7454 C  CG   . LEU   D 1 248 ? -45.806 -13.571 36.536  1.00 16.99 ? 227 LEU   D CG   1 
ATOM   7455 C  CD1  . LEU   D 1 248 ? -44.356 -13.427 36.977  1.00 18.60 ? 227 LEU   D CD1  1 
ATOM   7456 C  CD2  . LEU   D 1 248 ? -46.480 -12.206 36.554  1.00 19.09 ? 227 LEU   D CD2  1 
ATOM   7457 N  N    . GLY   D 1 249 ? -46.220 -17.673 35.899  1.00 20.11 ? 228 GLY   D N    1 
ATOM   7458 C  CA   . GLY   D 1 249 ? -47.127 -18.507 36.676  1.00 20.44 ? 228 GLY   D CA   1 
ATOM   7459 C  C    . GLY   D 1 249 ? -47.833 -19.588 35.864  1.00 21.02 ? 228 GLY   D C    1 
ATOM   7460 O  O    . GLY   D 1 249 ? -48.569 -20.387 36.445  1.00 21.18 ? 228 GLY   D O    1 
ATOM   7461 N  N    . ARG   D 1 250 ? -47.669 -19.579 34.533  1.00 19.54 ? 229 ARG   D N    1 
ATOM   7462 C  CA   . ARG   D 1 250 ? -48.305 -20.558 33.660  1.00 19.02 ? 229 ARG   D CA   1 
ATOM   7463 C  C    . ARG   D 1 250 ? -49.797 -20.687 33.968  1.00 19.54 ? 229 ARG   D C    1 
ATOM   7464 O  O    . ARG   D 1 250 ? -50.344 -21.790 34.072  1.00 19.53 ? 229 ARG   D O    1 
ATOM   7465 C  CB   . ARG   D 1 250 ? -47.585 -21.901 33.834  1.00 19.76 ? 229 ARG   D CB   1 
ATOM   7466 C  CG   . ARG   D 1 250 ? -46.090 -21.786 33.585  1.00 21.84 ? 229 ARG   D CG   1 
ATOM   7467 C  CD   . ARG   D 1 250 ? -45.772 -21.575 32.125  1.00 24.71 ? 229 ARG   D CD   1 
ATOM   7468 N  NE   . ARG   D 1 250 ? -44.346 -21.249 32.011  1.00 27.97 ? 229 ARG   D NE   1 
ATOM   7469 C  CZ   . ARG   D 1 250 ? -43.759 -20.816 30.900  1.00 28.99 ? 229 ARG   D CZ   1 
ATOM   7470 N  NH1  . ARG   D 1 250 ? -44.438 -20.733 29.770  1.00 27.75 ? 229 ARG   D NH1  1 
ATOM   7471 N  NH2  . ARG   D 1 250 ? -42.476 -20.493 30.925  1.00 31.93 ? 229 ARG   D NH2  1 
ATOM   7472 N  N    . ARG   D 1 251 ? -50.453 -19.535 34.115  1.00 18.14 ? 230 ARG   D N    1 
ATOM   7473 C  CA   . ARG   D 1 251 ? -51.874 -19.480 34.393  1.00 19.28 ? 230 ARG   D CA   1 
ATOM   7474 C  C    . ARG   D 1 251 ? -52.431 -18.213 33.761  1.00 18.66 ? 230 ARG   D C    1 
ATOM   7475 O  O    . ARG   D 1 251 ? -51.679 -17.278 33.504  1.00 19.59 ? 230 ARG   D O    1 
ATOM   7476 C  CB   . ARG   D 1 251 ? -52.139 -19.455 35.903  1.00 21.68 ? 230 ARG   D CB   1 
ATOM   7477 C  CG   . ARG   D 1 251 ? -51.542 -18.285 36.671  1.00 24.56 ? 230 ARG   D CG   1 
ATOM   7478 C  CD   . ARG   D 1 251 ? -51.980 -18.336 38.134  1.00 30.38 ? 230 ARG   D CD   1 
ATOM   7479 N  NE   . ARG   D 1 251 ? -51.185 -19.303 38.899  1.00 36.52 ? 230 ARG   D NE   1 
ATOM   7480 N  N    . GLU   D 1 252 ? -53.744 -18.202 33.551  1.00 19.03 ? 231 GLU   D N    1 
ATOM   7481 C  CA   . GLU   D 1 252 ? -54.443 -17.021 33.066  1.00 18.14 ? 231 GLU   D CA   1 
ATOM   7482 C  C    . GLU   D 1 252 ? -54.624 -16.008 34.203  1.00 18.08 ? 231 GLU   D C    1 
ATOM   7483 O  O    . GLU   D 1 252 ? -54.571 -16.354 35.387  1.00 19.39 ? 231 GLU   D O    1 
ATOM   7484 C  CB   . GLU   D 1 252 ? -55.794 -17.445 32.476  1.00 20.50 ? 231 GLU   D CB   1 
ATOM   7485 C  CG   . GLU   D 1 252 ? -56.830 -17.887 33.514  1.00 22.34 ? 231 GLU   D CG   1 
ATOM   7486 C  CD   . GLU   D 1 252 ? -56.810 -19.371 33.861  1.00 26.60 ? 231 GLU   D CD   1 
ATOM   7487 O  OE1  . GLU   D 1 252 ? -57.915 -19.957 33.941  1.00 27.39 ? 231 GLU   D OE1  1 
ATOM   7488 O  OE2  . GLU   D 1 252 ? -55.712 -19.945 34.037  1.00 24.69 ? 231 GLU   D OE2  1 
ATOM   7489 N  N    . ALA   D 1 253 ? -54.852 -14.737 33.827  1.00 17.60 ? 232 ALA   D N    1 
ATOM   7490 C  CA   . ALA   D 1 253 ? -55.216 -13.720 34.795  1.00 19.20 ? 232 ALA   D CA   1 
ATOM   7491 C  C    . ALA   D 1 253 ? -56.591 -14.050 35.370  1.00 18.25 ? 232 ALA   D C    1 
ATOM   7492 O  O    . ALA   D 1 253 ? -57.501 -14.458 34.659  1.00 19.50 ? 232 ALA   D O    1 
ATOM   7493 C  CB   . ALA   D 1 253 ? -55.253 -12.345 34.157  1.00 18.22 ? 232 ALA   D CB   1 
ATOM   7494 N  N    . SER   D 1 254 ? -56.745 -13.797 36.663  1.00 19.71 ? 233 SER   D N    1 
ATOM   7495 C  CA   . SER   D 1 254 ? -58.093 -13.778 37.200  1.00 18.38 ? 233 SER   D CA   1 
ATOM   7496 C  C    . SER   D 1 254 ? -58.810 -12.517 36.720  1.00 19.63 ? 233 SER   D C    1 
ATOM   7497 O  O    . SER   D 1 254 ? -58.179 -11.527 36.330  1.00 19.47 ? 233 SER   D O    1 
ATOM   7498 C  CB   . SER   D 1 254 ? -58.050 -13.839 38.692  1.00 19.72 ? 233 SER   D CB   1 
ATOM   7499 O  OG   . SER   D 1 254 ? -57.608 -12.597 39.219  1.00 21.61 ? 233 SER   D OG   1 
ATOM   7500 N  N    . ALA   D 1 255 ? -60.143 -12.532 36.807  1.00 17.39 ? 234 ALA   D N    1 
ATOM   7501 C  CA   . ALA   D 1 255 ? -60.885 -11.338 36.444  1.00 18.65 ? 234 ALA   D CA   1 
ATOM   7502 C  C    . ALA   D 1 255 ? -60.532 -10.212 37.405  1.00 18.97 ? 234 ALA   D C    1 
ATOM   7503 O  O    . ALA   D 1 255 ? -60.508 -9.041  37.008  1.00 17.64 ? 234 ALA   D O    1 
ATOM   7504 C  CB   . ALA   D 1 255 ? -62.371 -11.641 36.434  1.00 18.62 ? 234 ALA   D CB   1 
ATOM   7505 N  N    . GLU   D 1 256 ? -60.249 -10.558 38.671  1.00 18.47 ? 235 GLU   D N    1 
ATOM   7506 C  CA   . GLU   D 1 256 ? -59.953 -9.551  39.682  1.00 18.74 ? 235 GLU   D CA   1 
ATOM   7507 C  C    . GLU   D 1 256 ? -58.633 -8.843  39.367  1.00 17.85 ? 235 GLU   D C    1 
ATOM   7508 O  O    . GLU   D 1 256 ? -58.509 -7.652  39.638  1.00 18.11 ? 235 GLU   D O    1 
ATOM   7509 C  CB   . GLU   D 1 256 ? -59.944 -10.169 41.082  1.00 21.45 ? 235 GLU   D CB   1 
ATOM   7510 C  CG   . GLU   D 1 256 ? -61.326 -10.694 41.483  1.00 25.45 ? 235 GLU   D CG   1 
ATOM   7511 C  CD   . GLU   D 1 256 ? -61.894 -11.942 40.815  1.00 31.16 ? 235 GLU   D CD   1 
ATOM   7512 O  OE1  . GLU   D 1 256 ? -61.135 -12.783 40.277  1.00 28.26 ? 235 GLU   D OE1  1 
ATOM   7513 O  OE2  . GLU   D 1 256 ? -63.146 -12.060 40.819  1.00 33.52 ? 235 GLU   D OE2  1 
ATOM   7514 N  N    . GLN   D 1 257 ? -57.653 -9.581  38.834  1.00 17.37 ? 236 GLN   D N    1 
ATOM   7515 C  CA   . GLN   D 1 257 ? -56.371 -9.007  38.442  1.00 16.64 ? 236 GLN   D CA   1 
ATOM   7516 C  C    . GLN   D 1 257 ? -56.557 -7.947  37.357  1.00 16.77 ? 236 GLN   D C    1 
ATOM   7517 O  O    . GLN   D 1 257 ? -55.935 -6.877  37.401  1.00 17.25 ? 236 GLN   D O    1 
ATOM   7518 C  CB   . GLN   D 1 257 ? -55.416 -10.135 38.046  1.00 16.70 ? 236 GLN   D CB   1 
ATOM   7519 C  CG   . GLN   D 1 257 ? -54.812 -10.808 39.273  1.00 17.51 ? 236 GLN   D CG   1 
ATOM   7520 C  CD   . GLN   D 1 257 ? -54.097 -12.108 38.980  1.00 18.85 ? 236 GLN   D CD   1 
ATOM   7521 O  OE1  . GLN   D 1 257 ? -54.355 -12.780 37.983  1.00 19.62 ? 236 GLN   D OE1  1 
ATOM   7522 N  NE2  . GLN   D 1 257 ? -53.163 -12.442 39.853  1.00 20.73 ? 236 GLN   D NE2  1 
ATOM   7523 N  N    . ILE   D 1 258 ? -57.443 -8.235  36.406  1.00 16.13 ? 237 ILE   D N    1 
ATOM   7524 C  CA   . ILE   D 1 258 ? -57.746 -7.279  35.352  1.00 15.43 ? 237 ILE   D CA   1 
ATOM   7525 C  C    . ILE   D 1 258 ? -58.422 -6.070  35.985  1.00 16.42 ? 237 ILE   D C    1 
ATOM   7526 O  O    . ILE   D 1 258 ? -58.038 -4.926  35.707  1.00 15.45 ? 237 ILE   D O    1 
ATOM   7527 C  CB   . ILE   D 1 258 ? -58.602 -7.914  34.237  1.00 15.71 ? 237 ILE   D CB   1 
ATOM   7528 C  CG1  . ILE   D 1 258 ? -57.946 -9.141  33.600  1.00 16.02 ? 237 ILE   D CG1  1 
ATOM   7529 C  CG2  . ILE   D 1 258 ? -58.942 -6.887  33.154  1.00 16.87 ? 237 ILE   D CG2  1 
ATOM   7530 C  CD1  . ILE   D 1 258 ? -56.512 -8.918  33.132  1.00 17.42 ? 237 ILE   D CD1  1 
ATOM   7531 N  N    . ALA   D 1 259 ? -59.393 -6.330  36.876  1.00 15.53 ? 238 ALA   D N    1 
ATOM   7532 C  CA   . ALA   D 1 259 ? -60.115 -5.249  37.542  1.00 16.18 ? 238 ALA   D CA   1 
ATOM   7533 C  C    . ALA   D 1 259 ? -59.192 -4.343  38.357  1.00 16.14 ? 238 ALA   D C    1 
ATOM   7534 O  O    . ALA   D 1 259 ? -59.383 -3.123  38.398  1.00 16.16 ? 238 ALA   D O    1 
ATOM   7535 C  CB   . ALA   D 1 259 ? -61.217 -5.856  38.402  1.00 15.63 ? 238 ALA   D CB   1 
ATOM   7536 N  N    . ASP   D 1 260 ? -58.149 -4.916  38.971  1.00 17.00 ? 239 ASP   D N    1 
ATOM   7537 C  CA   . ASP   D 1 260 ? -57.198 -4.148  39.763  1.00 17.20 ? 239 ASP   D CA   1 
ATOM   7538 C  C    . ASP   D 1 260 ? -56.538 -3.053  38.922  1.00 14.80 ? 239 ASP   D C    1 
ATOM   7539 O  O    . ASP   D 1 260 ? -56.292 -1.957  39.418  1.00 16.37 ? 239 ASP   D O    1 
ATOM   7540 C  CB   . ASP   D 1 260 ? -56.080 -5.034  40.287  1.00 18.55 ? 239 ASP   D CB   1 
ATOM   7541 C  CG   . ASP   D 1 260 ? -56.424 -5.837  41.530  1.00 23.64 ? 239 ASP   D CG   1 
ATOM   7542 O  OD1  . ASP   D 1 260 ? -57.355 -5.423  42.252  1.00 23.56 ? 239 ASP   D OD1  1 
ATOM   7543 O  OD2  . ASP   D 1 260 ? -55.786 -6.898  41.736  1.00 24.40 ? 239 ASP   D OD2  1 
ATOM   7544 N  N    . ALA   D 1 261 ? -56.255 -3.352  37.641  1.00 14.56 ? 240 ALA   D N    1 
ATOM   7545 C  CA   . ALA   D 1 261 ? -55.644 -2.351  36.769  1.00 15.44 ? 240 ALA   D CA   1 
ATOM   7546 C  C    . ALA   D 1 261 ? -56.651 -1.270  36.383  1.00 16.55 ? 240 ALA   D C    1 
ATOM   7547 O  O    . ALA   D 1 261 ? -56.292 -0.096  36.268  1.00 15.74 ? 240 ALA   D O    1 
ATOM   7548 C  CB   . ALA   D 1 261 ? -55.059 -3.022  35.532  1.00 15.96 ? 240 ALA   D CB   1 
ATOM   7549 N  N    . VAL   D 1 262 ? -57.920 -1.657  36.163  1.00 15.56 ? 241 VAL   D N    1 
ATOM   7550 C  CA   . VAL   D 1 262 ? -58.948 -0.656  35.911  1.00 16.47 ? 241 VAL   D CA   1 
ATOM   7551 C  C    . VAL   D 1 262 ? -59.084 0.273   37.115  1.00 15.95 ? 241 VAL   D C    1 
ATOM   7552 O  O    . VAL   D 1 262 ? -59.182 1.498   36.937  1.00 15.85 ? 241 VAL   D O    1 
ATOM   7553 C  CB   . VAL   D 1 262 ? -60.288 -1.350  35.604  1.00 16.09 ? 241 VAL   D CB   1 
ATOM   7554 C  CG1  . VAL   D 1 262 ? -61.414 -0.321  35.487  1.00 17.42 ? 241 VAL   D CG1  1 
ATOM   7555 C  CG2  . VAL   D 1 262 ? -60.211 -2.245  34.375  1.00 17.04 ? 241 VAL   D CG2  1 
ATOM   7556 N  N    . ILE   D 1 263 ? -59.120 -0.298  38.339  1.00 16.19 ? 242 ILE   D N    1 
ATOM   7557 C  CA   . ILE   D 1 263 ? -59.227 0.483   39.562  1.00 17.97 ? 242 ILE   D CA   1 
ATOM   7558 C  C    . ILE   D 1 263 ? -58.078 1.494   39.661  1.00 16.57 ? 242 ILE   D C    1 
ATOM   7559 O  O    . ILE   D 1 263 ? -58.279 2.664   40.009  1.00 16.95 ? 242 ILE   D O    1 
ATOM   7560 C  CB   . ILE   D 1 263 ? -59.314 -0.438  40.796  1.00 21.06 ? 242 ILE   D CB   1 
ATOM   7561 C  CG1  . ILE   D 1 263 ? -60.625 -1.235  40.837  1.00 25.00 ? 242 ILE   D CG1  1 
ATOM   7562 C  CG2  . ILE   D 1 263 ? -59.068 0.324   42.097  1.00 22.00 ? 242 ILE   D CG2  1 
ATOM   7563 C  CD1  . ILE   D 1 263 ? -61.891 -0.402  40.892  1.00 28.23 ? 242 ILE   D CD1  1 
ATOM   7564 N  N    . PHE   D 1 264 ? -56.845 1.068   39.369  1.00 15.40 ? 243 PHE   D N    1 
ATOM   7565 C  CA   . PHE   D 1 264 ? -55.729 2.002   39.416  1.00 15.59 ? 243 PHE   D CA   1 
ATOM   7566 C  C    . PHE   D 1 264 ? -55.971 3.175   38.470  1.00 14.13 ? 243 PHE   D C    1 
ATOM   7567 O  O    . PHE   D 1 264 ? -55.772 4.338   38.841  1.00 14.83 ? 243 PHE   D O    1 
ATOM   7568 C  CB   . PHE   D 1 264 ? -54.444 1.248   39.051  1.00 15.69 ? 243 PHE   D CB   1 
ATOM   7569 C  CG   . PHE   D 1 264 ? -53.270 2.191   38.820  1.00 15.78 ? 243 PHE   D CG   1 
ATOM   7570 C  CD1  . PHE   D 1 264 ? -52.713 2.921   39.873  1.00 15.80 ? 243 PHE   D CD1  1 
ATOM   7571 C  CD2  . PHE   D 1 264 ? -52.742 2.346   37.538  1.00 15.94 ? 243 PHE   D CD2  1 
ATOM   7572 C  CE1  . PHE   D 1 264 ? -51.665 3.806   39.617  1.00 17.84 ? 243 PHE   D CE1  1 
ATOM   7573 C  CE2  . PHE   D 1 264 ? -51.682 3.213   37.291  1.00 17.19 ? 243 PHE   D CE2  1 
ATOM   7574 C  CZ   . PHE   D 1 264 ? -51.143 3.935   38.342  1.00 17.35 ? 243 PHE   D CZ   1 
ATOM   7575 N  N    . LEU   D 1 265 ? -56.370 2.860   37.233  1.00 15.44 ? 244 LEU   D N    1 
ATOM   7576 C  CA   . LEU   D 1 265 ? -56.517 3.876   36.202  1.00 14.74 ? 244 LEU   D CA   1 
ATOM   7577 C  C    . LEU   D 1 265 ? -57.601 4.899   36.528  1.00 15.45 ? 244 LEU   D C    1 
ATOM   7578 O  O    . LEU   D 1 265 ? -57.477 6.050   36.133  1.00 16.72 ? 244 LEU   D O    1 
ATOM   7579 C  CB   . LEU   D 1 265 ? -56.733 3.285   34.812  1.00 15.15 ? 244 LEU   D CB   1 
ATOM   7580 C  CG   . LEU   D 1 265 ? -55.474 2.679   34.187  1.00 15.52 ? 244 LEU   D CG   1 
ATOM   7581 C  CD1  . LEU   D 1 265 ? -55.885 1.818   33.010  1.00 15.38 ? 244 LEU   D CD1  1 
ATOM   7582 C  CD2  . LEU   D 1 265 ? -54.525 3.791   33.747  1.00 16.51 ? 244 LEU   D CD2  1 
ATOM   7583 N  N    . VAL   D 1 266 ? -58.648 4.505   37.258  1.00 15.73 ? 245 VAL   D N    1 
ATOM   7584 C  CA   . VAL   D 1 266 ? -59.676 5.498   37.559  1.00 17.26 ? 245 VAL   D CA   1 
ATOM   7585 C  C    . VAL   D 1 266 ? -59.354 6.268   38.844  1.00 18.07 ? 245 VAL   D C    1 
ATOM   7586 O  O    . VAL   D 1 266 ? -60.024 7.266   39.136  1.00 21.01 ? 245 VAL   D O    1 
ATOM   7587 C  CB   . VAL   D 1 266 ? -61.097 4.885   37.608  1.00 17.80 ? 245 VAL   D CB   1 
ATOM   7588 C  CG1  . VAL   D 1 266 ? -61.402 4.104   36.337  1.00 18.12 ? 245 VAL   D CG1  1 
ATOM   7589 C  CG2  . VAL   D 1 266 ? -61.333 4.047   38.853  1.00 21.93 ? 245 VAL   D CG2  1 
ATOM   7590 N  N    . SER   D 1 267 ? -58.343 5.813   39.600  1.00 17.99 ? 246 SER   D N    1 
ATOM   7591 C  CA   . SER   D 1 267 ? -58.025 6.317   40.933  1.00 17.25 ? 246 SER   D CA   1 
ATOM   7592 C  C    . SER   D 1 267 ? -57.279 7.645   40.882  1.00 20.33 ? 246 SER   D C    1 
ATOM   7593 O  O    . SER   D 1 267 ? -56.739 8.042   39.848  1.00 20.31 ? 246 SER   D O    1 
ATOM   7594 C  CB   . SER   D 1 267 ? -57.188 5.314   41.697  1.00 19.20 ? 246 SER   D CB   1 
ATOM   7595 O  OG   . SER   D 1 267 ? -55.818 5.388   41.310  1.00 19.95 ? 246 SER   D OG   1 
ATOM   7596 N  N    . GLY   D 1 268 ? -57.146 8.240   42.075  1.00 20.74 ? 247 GLY   D N    1 
ATOM   7597 C  CA   . GLY   D 1 268 ? -56.349 9.442   42.254  1.00 22.81 ? 247 GLY   D CA   1 
ATOM   7598 C  C    . GLY   D 1 268 ? -54.856 9.194   42.042  1.00 22.01 ? 247 GLY   D C    1 
ATOM   7599 O  O    . GLY   D 1 268 ? -54.111 10.158  41.949  1.00 26.40 ? 247 GLY   D O    1 
ATOM   7600 N  N    . SER   D 1 269 ? -54.426 7.924   41.990  1.00 20.75 ? 248 SER   D N    1 
ATOM   7601 C  CA   . SER   D 1 269 ? -53.022 7.572   41.810  1.00 20.67 ? 248 SER   D CA   1 
ATOM   7602 C  C    . SER   D 1 269 ? -52.638 7.584   40.330  1.00 19.62 ? 248 SER   D C    1 
ATOM   7603 O  O    . SER   D 1 269 ? -51.484 7.309   39.997  1.00 19.87 ? 248 SER   D O    1 
ATOM   7604 C  CB   . SER   D 1 269 ? -52.727 6.228   42.390  1.00 24.40 ? 248 SER   D CB   1 
ATOM   7605 O  OG   . SER   D 1 269 ? -52.852 6.305   43.804  1.00 28.18 ? 248 SER   D OG   1 
ATOM   7606 N  N    . ALA   D 1 270 ? -53.603 7.905   39.455  1.00 18.15 ? 249 ALA   D N    1 
ATOM   7607 C  CA   . ALA   D 1 270 ? -53.351 7.904   38.017  1.00 16.93 ? 249 ALA   D CA   1 
ATOM   7608 C  C    . ALA   D 1 270 ? -53.745 9.230   37.373  1.00 15.85 ? 249 ALA   D C    1 
ATOM   7609 O  O    . ALA   D 1 270 ? -54.064 9.266   36.192  1.00 16.67 ? 249 ALA   D O    1 
ATOM   7610 C  CB   . ALA   D 1 270 ? -54.115 6.773   37.360  1.00 17.13 ? 249 ALA   D CB   1 
ATOM   7611 N  N    . GLN   D 1 271 ? -53.720 10.325  38.142  1.00 16.92 ? 250 GLN   D N    1 
ATOM   7612 C  CA   . GLN   D 1 271 ? -54.298 11.575  37.676  1.00 17.91 ? 250 GLN   D CA   1 
ATOM   7613 C  C    . GLN   D 1 271 ? -53.507 12.226  36.542  1.00 17.40 ? 250 GLN   D C    1 
ATOM   7614 O  O    . GLN   D 1 271 ? -54.019 13.148  35.920  1.00 18.39 ? 250 GLN   D O    1 
ATOM   7615 C  CB   . GLN   D 1 271 ? -54.419 12.521  38.873  1.00 22.92 ? 250 GLN   D CB   1 
ATOM   7616 C  CG   . GLN   D 1 271 ? -55.505 12.071  39.847  0.60 25.43 ? 250 GLN   D CG   1 
ATOM   7617 C  CD   . GLN   D 1 271 ? -56.827 12.796  39.703  0.60 31.76 ? 250 GLN   D CD   1 
ATOM   7618 O  OE1  . GLN   D 1 271 ? -57.322 13.053  38.600  0.60 33.76 ? 250 GLN   D OE1  1 
ATOM   7619 N  NE2  . GLN   D 1 271 ? -57.409 13.152  40.838  0.60 33.87 ? 250 GLN   D NE2  1 
ATOM   7620 N  N    . TYR   D 1 272 ? -52.268 11.790  36.290  1.00 16.44 ? 251 TYR   D N    1 
ATOM   7621 C  CA   . TYR   D 1 272 ? -51.527 12.358  35.175  1.00 16.45 ? 251 TYR   D CA   1 
ATOM   7622 C  C    . TYR   D 1 272 ? -51.478 11.365  34.015  1.00 16.06 ? 251 TYR   D C    1 
ATOM   7623 O  O    . TYR   D 1 272 ? -50.801 11.616  33.025  1.00 16.41 ? 251 TYR   D O    1 
ATOM   7624 C  CB   . TYR   D 1 272 ? -50.106 12.729  35.610  1.00 16.50 ? 251 TYR   D CB   1 
ATOM   7625 C  CG   . TYR   D 1 272 ? -49.367 13.700  34.700  1.00 16.00 ? 251 TYR   D CG   1 
ATOM   7626 C  CD1  . TYR   D 1 272 ? -49.697 15.047  34.704  1.00 15.82 ? 251 TYR   D CD1  1 
ATOM   7627 C  CD2  . TYR   D 1 272 ? -48.318 13.294  33.884  1.00 15.49 ? 251 TYR   D CD2  1 
ATOM   7628 C  CE1  . TYR   D 1 272 ? -49.023 15.960  33.913  1.00 16.45 ? 251 TYR   D CE1  1 
ATOM   7629 C  CE2  . TYR   D 1 272 ? -47.626 14.199  33.095  1.00 15.27 ? 251 TYR   D CE2  1 
ATOM   7630 C  CZ   . TYR   D 1 272 ? -47.978 15.542  33.110  1.00 16.47 ? 251 TYR   D CZ   1 
ATOM   7631 O  OH   . TYR   D 1 272 ? -47.241 16.391  32.338  1.00 17.00 ? 251 TYR   D OH   1 
ATOM   7632 N  N    . ILE   D 1 273 ? -52.154 10.218  34.162  1.00 14.64 ? 252 ILE   D N    1 
ATOM   7633 C  CA   . ILE   D 1 273 ? -52.077 9.184   33.131  1.00 14.23 ? 252 ILE   D CA   1 
ATOM   7634 C  C    . ILE   D 1 273 ? -53.257 9.322   32.172  1.00 14.49 ? 252 ILE   D C    1 
ATOM   7635 O  O    . ILE   D 1 273 ? -54.424 9.244   32.583  1.00 13.78 ? 252 ILE   D O    1 
ATOM   7636 C  CB   . ILE   D 1 273 ? -52.073 7.792   33.775  1.00 14.57 ? 252 ILE   D CB   1 
ATOM   7637 C  CG1  . ILE   D 1 273 ? -50.914 7.659   34.776  1.00 15.78 ? 252 ILE   D CG1  1 
ATOM   7638 C  CG2  . ILE   D 1 273 ? -52.012 6.696   32.707  1.00 15.33 ? 252 ILE   D CG2  1 
ATOM   7639 C  CD1  . ILE   D 1 273 ? -50.826 6.283   35.415  1.00 16.35 ? 252 ILE   D CD1  1 
ATOM   7640 N  N    . THR   D 1 274 ? -52.949 9.551   30.893  1.00 13.04 ? 253 THR   D N    1 
ATOM   7641 C  CA   . THR   D 1 274 ? -53.988 9.534   29.865  1.00 13.37 ? 253 THR   D CA   1 
ATOM   7642 C  C    . THR   D 1 274 ? -53.353 9.067   28.567  1.00 14.51 ? 253 THR   D C    1 
ATOM   7643 O  O    . THR   D 1 274 ? -52.190 9.407   28.275  1.00 14.81 ? 253 THR   D O    1 
ATOM   7644 C  CB   . THR   D 1 274 ? -54.725 10.877  29.729  1.00 14.29 ? 253 THR   D CB   1 
ATOM   7645 O  OG1  . THR   D 1 274 ? -55.908 10.665  28.946  1.00 14.25 ? 253 THR   D OG1  1 
ATOM   7646 C  CG2  . THR   D 1 274 ? -53.887 11.977  29.089  1.00 15.31 ? 253 THR   D CG2  1 
ATOM   7647 N  N    . GLY   D 1 275 ? -54.120 8.264   27.819  1.00 14.34 ? 254 GLY   D N    1 
ATOM   7648 C  CA   . GLY   D 1 275 ? -53.641 7.735   26.555  1.00 14.75 ? 254 GLY   D CA   1 
ATOM   7649 C  C    . GLY   D 1 275 ? -52.727 6.527   26.739  1.00 14.97 ? 254 GLY   D C    1 
ATOM   7650 O  O    . GLY   D 1 275 ? -52.035 6.164   25.789  1.00 16.20 ? 254 GLY   D O    1 
ATOM   7651 N  N    . SER   D 1 276 ? -52.680 5.980   27.954  1.00 15.36 ? 255 SER   D N    1 
ATOM   7652 C  CA   . SER   D 1 276 ? -51.846 4.821   28.249  1.00 15.17 ? 255 SER   D CA   1 
ATOM   7653 C  C    . SER   D 1 276 ? -52.674 3.547   28.180  1.00 15.34 ? 255 SER   D C    1 
ATOM   7654 O  O    . SER   D 1 276 ? -53.820 3.522   28.626  1.00 16.04 ? 255 SER   D O    1 
ATOM   7655 C  CB   . SER   D 1 276 ? -51.216 4.949   29.612  1.00 16.51 ? 255 SER   D CB   1 
ATOM   7656 O  OG   . SER   D 1 276 ? -50.376 6.101   29.657  1.00 17.48 ? 255 SER   D OG   1 
ATOM   7657 N  N    . ILE   D 1 277 ? -52.028 2.477   27.720  1.00 14.91 ? 256 ILE   D N    1 
ATOM   7658 C  CA   . ILE   D 1 277 ? -52.621 1.145   27.767  1.00 16.15 ? 256 ILE   D CA   1 
ATOM   7659 C  C    . ILE   D 1 277 ? -51.727 0.250   28.616  1.00 16.78 ? 256 ILE   D C    1 
ATOM   7660 O  O    . ILE   D 1 277 ? -50.566 0.065   28.270  1.00 20.55 ? 256 ILE   D O    1 
ATOM   7661 C  CB   . ILE   D 1 277 ? -52.832 0.594   26.347  1.00 18.58 ? 256 ILE   D CB   1 
ATOM   7662 C  CG1  . ILE   D 1 277 ? -53.857 1.465   25.615  1.00 21.00 ? 256 ILE   D CG1  1 
ATOM   7663 C  CG2  . ILE   D 1 277 ? -53.275 -0.878  26.400  1.00 19.07 ? 256 ILE   D CG2  1 
ATOM   7664 C  CD1  . ILE   D 1 277 ? -53.926 1.243   24.120  1.00 25.27 ? 256 ILE   D CD1  1 
ATOM   7665 N  N    . ILE   D 1 278 ? -52.258 -0.242  29.740  1.00 16.62 ? 257 ILE   D N    1 
ATOM   7666 C  CA   . ILE   D 1 278 ? -51.507 -1.096  30.649  1.00 15.88 ? 257 ILE   D CA   1 
ATOM   7667 C  C    . ILE   D 1 278 ? -51.761 -2.541  30.238  1.00 16.36 ? 257 ILE   D C    1 
ATOM   7668 O  O    . ILE   D 1 278 ? -52.886 -3.027  30.339  1.00 14.96 ? 257 ILE   D O    1 
ATOM   7669 C  CB   . ILE   D 1 278 ? -51.938 -0.850  32.108  1.00 16.87 ? 257 ILE   D CB   1 
ATOM   7670 C  CG1  . ILE   D 1 278 ? -51.733 0.615   32.529  1.00 18.73 ? 257 ILE   D CG1  1 
ATOM   7671 C  CG2  . ILE   D 1 278 ? -51.206 -1.823  33.046  1.00 18.31 ? 257 ILE   D CG2  1 
ATOM   7672 C  CD1  . ILE   D 1 278 ? -52.200 0.899   33.947  1.00 19.45 ? 257 ILE   D CD1  1 
ATOM   7673 N  N    . LYS   D 1 279 ? -50.703 -3.235  29.805  1.00 15.07 ? 258 LYS   D N    1 
ATOM   7674 C  CA   . LYS   D 1 279 ? -50.801 -4.671  29.573  1.00 16.31 ? 258 LYS   D CA   1 
ATOM   7675 C  C    . LYS   D 1 279 ? -50.850 -5.419  30.900  1.00 15.77 ? 258 LYS   D C    1 
ATOM   7676 O  O    . LYS   D 1 279 ? -50.073 -5.153  31.817  1.00 16.14 ? 258 LYS   D O    1 
ATOM   7677 C  CB   . LYS   D 1 279 ? -49.623 -5.332  28.847  1.00 19.08 ? 258 LYS   D CB   1 
ATOM   7678 C  CG   . LYS   D 1 279 ? -49.357 -4.965  27.415  1.00 21.73 ? 258 LYS   D CG   1 
ATOM   7679 C  CD   . LYS   D 1 279 ? -48.172 -5.834  26.975  1.00 20.51 ? 258 LYS   D CD   1 
ATOM   7680 C  CE   . LYS   D 1 279 ? -46.874 -5.509  27.691  1.00 23.13 ? 258 LYS   D CE   1 
ATOM   7681 N  NZ   . LYS   D 1 279 ? -45.700 -6.168  27.077  1.00 20.86 ? 258 LYS   D NZ   1 
ATOM   7682 N  N    . VAL   D 1 280 ? -51.788 -6.370  30.984  1.00 15.40 ? 259 VAL   D N    1 
ATOM   7683 C  CA   . VAL   D 1 280 ? -51.905 -7.220  32.160  1.00 14.89 ? 259 VAL   D CA   1 
ATOM   7684 C  C    . VAL   D 1 280 ? -51.913 -8.663  31.628  1.00 15.04 ? 259 VAL   D C    1 
ATOM   7685 O  O    . VAL   D 1 280 ? -52.967 -9.296  31.532  1.00 16.48 ? 259 VAL   D O    1 
ATOM   7686 C  CB   . VAL   D 1 280 ? -53.139 -6.884  33.036  1.00 16.44 ? 259 VAL   D CB   1 
ATOM   7687 C  CG1  . VAL   D 1 280 ? -53.186 -7.730  34.320  1.00 16.83 ? 259 VAL   D CG1  1 
ATOM   7688 C  CG2  . VAL   D 1 280 ? -53.193 -5.391  33.406  1.00 17.13 ? 259 VAL   D CG2  1 
ATOM   7689 N  N    . ASP   D 1 281 ? -50.714 -9.155  31.279  1.00 14.45 ? 260 ASP   D N    1 
ATOM   7690 C  CA   . ASP   D 1 281 ? -50.630 -10.360 30.473  1.00 14.82 ? 260 ASP   D CA   1 
ATOM   7691 C  C    . ASP   D 1 281 ? -49.612 -11.381 30.972  1.00 14.49 ? 260 ASP   D C    1 
ATOM   7692 O  O    . ASP   D 1 281 ? -49.417 -12.384 30.287  1.00 15.00 ? 260 ASP   D O    1 
ATOM   7693 C  CB   . ASP   D 1 281 ? -50.371 -10.042 29.007  1.00 15.15 ? 260 ASP   D CB   1 
ATOM   7694 C  CG   . ASP   D 1 281 ? -48.936 -9.667  28.655  1.00 17.51 ? 260 ASP   D CG   1 
ATOM   7695 O  OD1  . ASP   D 1 281 ? -48.142 -9.398  29.578  1.00 16.72 ? 260 ASP   D OD1  1 
ATOM   7696 O  OD2  . ASP   D 1 281 ? -48.623 -9.714  27.457  1.00 17.30 ? 260 ASP   D OD2  1 
ATOM   7697 N  N    . GLY   D 1 282 ? -48.989 -11.164 32.136  1.00 14.55 ? 261 GLY   D N    1 
ATOM   7698 C  CA   . GLY   D 1 282 ? -48.112 -12.203 32.670  1.00 15.16 ? 261 GLY   D CA   1 
ATOM   7699 C  C    . GLY   D 1 282 ? -46.918 -12.474 31.758  1.00 15.44 ? 261 GLY   D C    1 
ATOM   7700 O  O    . GLY   D 1 282 ? -46.289 -13.534 31.856  1.00 15.21 ? 261 GLY   D O    1 
ATOM   7701 N  N    . GLY   D 1 283 ? -46.634 -11.531 30.842  1.00 14.21 ? 262 GLY   D N    1 
ATOM   7702 C  CA   . GLY   D 1 283 ? -45.519 -11.726 29.923  1.00 13.87 ? 262 GLY   D CA   1 
ATOM   7703 C  C    . GLY   D 1 283 ? -45.890 -12.438 28.613  1.00 14.70 ? 262 GLY   D C    1 
ATOM   7704 O  O    . GLY   D 1 283 ? -45.000 -12.663 27.791  1.00 14.96 ? 262 GLY   D O    1 
ATOM   7705 N  N    . LEU   D 1 284 ? -47.168 -12.807 28.417  1.00 13.84 ? 263 LEU   D N    1 
ATOM   7706 C  CA   . LEU   D 1 284 ? -47.543 -13.600 27.239  1.00 15.72 ? 263 LEU   D CA   1 
ATOM   7707 C  C    . LEU   D 1 284 ? -47.091 -12.970 25.917  1.00 15.97 ? 263 LEU   D C    1 
ATOM   7708 O  O    . LEU   D 1 284 ? -46.616 -13.680 25.023  1.00 16.42 ? 263 LEU   D O    1 
ATOM   7709 C  CB   . LEU   D 1 284 ? -49.048 -13.839 27.239  1.00 16.14 ? 263 LEU   D CB   1 
ATOM   7710 C  CG   . LEU   D 1 284 ? -49.577 -14.711 26.092  1.00 17.42 ? 263 LEU   D CG   1 
ATOM   7711 C  CD1  . LEU   D 1 284 ? -49.015 -16.143 26.133  1.00 19.54 ? 263 LEU   D CD1  1 
ATOM   7712 C  CD2  . LEU   D 1 284 ? -51.094 -14.699 26.201  1.00 19.13 ? 263 LEU   D CD2  1 
ATOM   7713 N  N    . SER   D 1 285 ? -47.248 -11.642 25.786  1.00 15.96 ? 264 SER   D N    1 
ATOM   7714 C  CA   . SER   D 1 285 ? -46.935 -10.977 24.530  1.00 15.67 ? 264 SER   D CA   1 
ATOM   7715 C  C    . SER   D 1 285 ? -45.430 -10.955 24.244  1.00 16.69 ? 264 SER   D C    1 
ATOM   7716 O  O    . SER   D 1 285 ? -45.031 -10.641 23.119  1.00 17.74 ? 264 SER   D O    1 
ATOM   7717 C  CB   . SER   D 1 285 ? -47.540 -9.601  24.487  1.00 16.55 ? 264 SER   D CB   1 
ATOM   7718 O  OG   . SER   D 1 285 ? -46.966 -8.804  25.506  1.00 19.24 ? 264 SER   D OG   1 
ATOM   7719 N  N    . LEU   D 1 286 ? -44.607 -11.318 25.239  1.00 14.92 ? 265 LEU   D N    1 
ATOM   7720 C  CA   . LEU   D 1 286 ? -43.158 -11.316 25.055  1.00 15.63 ? 265 LEU   D CA   1 
ATOM   7721 C  C    . LEU   D 1 286 ? -42.648 -12.645 24.494  1.00 15.49 ? 265 LEU   D C    1 
ATOM   7722 O  O    . LEU   D 1 286 ? -41.445 -12.764 24.235  1.00 17.31 ? 265 LEU   D O    1 
ATOM   7723 C  CB   . LEU   D 1 286 ? -42.443 -11.018 26.380  1.00 18.01 ? 265 LEU   D CB   1 
ATOM   7724 C  CG   . LEU   D 1 286 ? -42.829 -9.709  27.069  1.00 21.21 ? 265 LEU   D CG   1 
ATOM   7725 C  CD1  . LEU   D 1 286 ? -42.100 -9.706  28.396  1.00 22.37 ? 265 LEU   D CD1  1 
ATOM   7726 C  CD2  . LEU   D 1 286 ? -42.484 -8.515  26.195  1.00 23.36 ? 265 LEU   D CD2  1 
ATOM   7727 N  N    . VAL   D 1 287 ? -43.522 -13.654 24.391  1.00 15.05 ? 266 VAL   D N    1 
ATOM   7728 C  CA   . VAL   D 1 287 ? -43.130 -15.022 24.059  1.00 16.45 ? 266 VAL   D CA   1 
ATOM   7729 C  C    . VAL   D 1 287 ? -43.167 -15.231 22.542  1.00 16.92 ? 266 VAL   D C    1 
ATOM   7730 O  O    . VAL   D 1 287 ? -44.228 -15.134 21.925  1.00 18.26 ? 266 VAL   D O    1 
ATOM   7731 C  CB   . VAL   D 1 287 ? -44.064 -16.035 24.751  1.00 17.75 ? 266 VAL   D CB   1 
ATOM   7732 C  CG1  . VAL   D 1 287 ? -43.650 -17.482 24.463  1.00 17.80 ? 266 VAL   D CG1  1 
ATOM   7733 C  CG2  . VAL   D 1 287 ? -44.079 -15.805 26.254  1.00 17.79 ? 266 VAL   D CG2  1 
ATOM   7734 N  N    . HIS   D 1 288 ? -42.000 -15.533 21.946  1.00 16.40 ? 267 HIS   D N    1 
ATOM   7735 C  CA   . HIS   D 1 288 ? -41.955 -15.790 20.511  1.00 17.58 ? 267 HIS   D CA   1 
ATOM   7736 C  C    . HIS   D 1 288 ? -42.572 -17.145 20.146  1.00 18.96 ? 267 HIS   D C    1 
ATOM   7737 O  O    . HIS   D 1 288 ? -42.748 -18.006 21.002  1.00 21.33 ? 267 HIS   D O    1 
ATOM   7738 C  CB   . HIS   D 1 288 ? -40.523 -15.734 19.965  1.00 19.04 ? 267 HIS   D CB   1 
ATOM   7739 C  CG   . HIS   D 1 288 ? -39.587 -16.790 20.480  1.00 21.27 ? 267 HIS   D CG   1 
ATOM   7740 N  ND1  . HIS   D 1 288 ? -39.664 -18.131 20.152  1.00 22.06 ? 267 HIS   D ND1  1 
ATOM   7741 C  CD2  . HIS   D 1 288 ? -38.547 -16.672 21.316  1.00 21.65 ? 267 HIS   D CD2  1 
ATOM   7742 C  CE1  . HIS   D 1 288 ? -38.700 -18.792 20.788  1.00 23.76 ? 267 HIS   D CE1  1 
ATOM   7743 N  NE2  . HIS   D 1 288 ? -37.999 -17.922 21.494  1.00 24.46 ? 267 HIS   D NE2  1 
ATOM   7744 N  N    . ALA   D 1 289 ? -42.832 -17.322 18.838  1.00 20.70 ? 268 ALA   D N    1 
ATOM   7745 C  CA   . ALA   D 1 289 ? -43.399 -18.539 18.265  1.00 22.30 ? 268 ALA   D CA   1 
ATOM   7746 C  C    . ALA   D 1 289 ? -42.585 -19.770 18.667  1.00 24.27 ? 268 ALA   D C    1 
ATOM   7747 O  O    . ALA   D 1 289 ? -43.212 -20.850 18.773  1.00 29.66 ? 268 ALA   D O    1 
ATOM   7748 C  CB   . ALA   D 1 289 ? -43.403 -18.423 16.757  1.00 24.35 ? 268 ALA   D CB   1 
ATOM   7749 O  OXT  . ALA   D 1 289 ? -41.355 -19.635 18.815  1.00 24.14 ? 268 ALA   D OXT  1 
HETATM 7750 P  PA   . NDP   E 2 .   ? -23.033 -12.603 11.830  1.00 18.42 ? 301 NDP   A PA   1 
HETATM 7751 O  O1A  . NDP   E 2 .   ? -22.569 -13.508 10.735  1.00 19.38 ? 301 NDP   A O1A  1 
HETATM 7752 O  O2A  . NDP   E 2 .   ? -23.370 -13.177 13.156  1.00 18.48 ? 301 NDP   A O2A  1 
HETATM 7753 O  O5B  . NDP   E 2 .   ? -21.951 -11.470 12.076  1.00 17.55 ? 301 NDP   A O5B  1 
HETATM 7754 C  C5B  . NDP   E 2 .   ? -21.498 -10.620 11.009  1.00 18.94 ? 301 NDP   A C5B  1 
HETATM 7755 C  C4B  . NDP   E 2 .   ? -20.076 -10.215 11.305  1.00 18.88 ? 301 NDP   A C4B  1 
HETATM 7756 O  O4B  . NDP   E 2 .   ? -20.009 -9.439  12.524  1.00 16.59 ? 301 NDP   A O4B  1 
HETATM 7757 C  C3B  . NDP   E 2 .   ? -19.085 -11.344 11.618  1.00 18.72 ? 301 NDP   A C3B  1 
HETATM 7758 O  O3B  . NDP   E 2 .   ? -18.625 -11.999 10.436  1.00 22.00 ? 301 NDP   A O3B  1 
HETATM 7759 C  C2B  . NDP   E 2 .   ? -17.954 -10.589 12.319  1.00 18.17 ? 301 NDP   A C2B  1 
HETATM 7760 O  O2B  . NDP   E 2 .   ? -16.842 -10.270 11.470  1.00 17.48 ? 301 NDP   A O2B  1 
HETATM 7761 C  C1B  . NDP   E 2 .   ? -18.637 -9.285  12.773  1.00 17.13 ? 301 NDP   A C1B  1 
HETATM 7762 N  N9A  . NDP   E 2 .   ? -18.357 -9.022  14.176  1.00 17.89 ? 301 NDP   A N9A  1 
HETATM 7763 C  C8A  . NDP   E 2 .   ? -18.723 -9.770  15.273  1.00 17.56 ? 301 NDP   A C8A  1 
HETATM 7764 N  N7A  . NDP   E 2 .   ? -18.175 -9.356  16.390  1.00 17.80 ? 301 NDP   A N7A  1 
HETATM 7765 C  C5A  . NDP   E 2 .   ? -17.376 -8.282  15.995  1.00 18.01 ? 301 NDP   A C5A  1 
HETATM 7766 C  C6A  . NDP   E 2 .   ? -16.518 -7.418  16.703  1.00 18.17 ? 301 NDP   A C6A  1 
HETATM 7767 N  N6A  . NDP   E 2 .   ? -16.279 -7.503  18.014  1.00 19.88 ? 301 NDP   A N6A  1 
HETATM 7768 N  N1A  . NDP   E 2 .   ? -15.876 -6.465  15.996  1.00 16.39 ? 301 NDP   A N1A  1 
HETATM 7769 C  C2A  . NDP   E 2 .   ? -16.095 -6.361  14.680  1.00 17.79 ? 301 NDP   A C2A  1 
HETATM 7770 N  N3A  . NDP   E 2 .   ? -16.881 -7.110  13.910  1.00 18.11 ? 301 NDP   A N3A  1 
HETATM 7771 C  C4A  . NDP   E 2 .   ? -17.484 -8.069  14.631  1.00 17.18 ? 301 NDP   A C4A  1 
HETATM 7772 O  O3   . NDP   E 2 .   ? -24.248 -11.758 11.238  1.00 16.92 ? 301 NDP   A O3   1 
HETATM 7773 P  PN   . NDP   E 2 .   ? -25.394 -12.217 10.215  1.00 17.10 ? 301 NDP   A PN   1 
HETATM 7774 O  O1N  . NDP   E 2 .   ? -26.025 -13.481 10.676  1.00 16.97 ? 301 NDP   A O1N  1 
HETATM 7775 O  O2N  . NDP   E 2 .   ? -24.870 -12.173 8.824   1.00 18.18 ? 301 NDP   A O2N  1 
HETATM 7776 O  O5D  . NDP   E 2 .   ? -26.455 -11.033 10.431  1.00 15.81 ? 301 NDP   A O5D  1 
HETATM 7777 C  C5D  . NDP   E 2 .   ? -26.184 -9.745  9.837   1.00 15.38 ? 301 NDP   A C5D  1 
HETATM 7778 C  C4D  . NDP   E 2 .   ? -26.928 -8.698  10.622  1.00 15.08 ? 301 NDP   A C4D  1 
HETATM 7779 O  O4D  . NDP   E 2 .   ? -28.350 -8.999  10.600  1.00 15.68 ? 301 NDP   A O4D  1 
HETATM 7780 C  C3D  . NDP   E 2 .   ? -26.523 -8.570  12.100  1.00 14.33 ? 301 NDP   A C3D  1 
HETATM 7781 O  O3D  . NDP   E 2 .   ? -26.614 -7.206  12.509  1.00 14.34 ? 301 NDP   A O3D  1 
HETATM 7782 C  C2D  . NDP   E 2 .   ? -27.634 -9.355  12.785  1.00 14.88 ? 301 NDP   A C2D  1 
HETATM 7783 O  O2D  . NDP   E 2 .   ? -27.860 -9.095  14.166  1.00 15.84 ? 301 NDP   A O2D  1 
HETATM 7784 C  C1D  . NDP   E 2 .   ? -28.851 -9.058  11.911  1.00 15.20 ? 301 NDP   A C1D  1 
HETATM 7785 N  N1N  . NDP   E 2 .   ? -29.806 -10.184 11.995  1.00 14.96 ? 301 NDP   A N1N  1 
HETATM 7786 C  C2N  . NDP   E 2 .   ? -29.467 -11.416 11.487  1.00 15.18 ? 301 NDP   A C2N  1 
HETATM 7787 C  C3N  . NDP   E 2 .   ? -30.326 -12.461 11.607  1.00 15.54 ? 301 NDP   A C3N  1 
HETATM 7788 C  C7N  . NDP   E 2 .   ? -30.020 -13.808 11.085  1.00 16.46 ? 301 NDP   A C7N  1 
HETATM 7789 O  O7N  . NDP   E 2 .   ? -30.948 -14.626 11.062  1.00 18.62 ? 301 NDP   A O7N  1 
HETATM 7790 N  N7N  . NDP   E 2 .   ? -28.793 -14.119 10.682  1.00 15.72 ? 301 NDP   A N7N  1 
HETATM 7791 C  C4N  . NDP   E 2 .   ? -31.599 -12.285 12.328  1.00 16.60 ? 301 NDP   A C4N  1 
HETATM 7792 C  C5N  . NDP   E 2 .   ? -31.873 -10.935 12.839  1.00 16.05 ? 301 NDP   A C5N  1 
HETATM 7793 C  C6N  . NDP   E 2 .   ? -31.002 -9.972  12.667  1.00 15.92 ? 301 NDP   A C6N  1 
HETATM 7794 P  P2B  . NDP   E 2 .   ? -15.596 -11.308 11.328  1.00 19.92 ? 301 NDP   A P2B  1 
HETATM 7795 O  O1X  . NDP   E 2 .   ? -14.706 -10.641 10.313  1.00 19.14 ? 301 NDP   A O1X  1 
HETATM 7796 O  O2X  . NDP   E 2 .   ? -14.969 -11.460 12.703  1.00 20.02 ? 301 NDP   A O2X  1 
HETATM 7797 O  O3X  . NDP   E 2 .   ? -16.165 -12.602 10.851  1.00 19.48 ? 301 NDP   A O3X  1 
HETATM 7798 N  NAI  . A1H0T F 3 .   ? -28.811 -13.757 14.393  1.00 20.32 ? 302 A1H0T A NAI  1 
HETATM 7799 C  CAF  . A1H0T F 3 .   ? -30.075 -14.136 14.609  1.00 22.10 ? 302 A1H0T A CAF  1 
HETATM 7800 C  CAE  . A1H0T F 3 .   ? -30.723 -15.264 14.321  1.00 24.91 ? 302 A1H0T A CAE  1 
HETATM 7801 CL CLAH . A1H0T F 3 .   ? -29.849 -16.579 13.460  1.00 29.83 ? 302 A1H0T A CLAH 1 
HETATM 7802 C  CAD  . A1H0T F 3 .   ? -32.062 -15.413 14.652  1.00 25.86 ? 302 A1H0T A CAD  1 
HETATM 7803 C  CAA  . A1H0T F 3 .   ? -32.726 -14.379 15.288  1.00 26.35 ? 302 A1H0T A CAA  1 
HETATM 7804 CL CLAB . A1H0T F 3 .   ? -34.458 -14.562 15.720  1.00 33.32 ? 302 A1H0T A CLAB 1 
HETATM 7805 C  CAG  . A1H0T F 3 .   ? -32.025 -13.213 15.589  1.00 23.82 ? 302 A1H0T A CAG  1 
HETATM 7806 C  CAC  . A1H0T F 3 .   ? -30.731 -13.131 15.244  1.00 20.82 ? 302 A1H0T A CAC  1 
HETATM 7807 N  NAK  . A1H0T F 3 .   ? -29.859 -12.123 15.418  1.00 18.37 ? 302 A1H0T A NAK  1 
HETATM 7808 C  CAJ  . A1H0T F 3 .   ? -28.693 -12.521 14.904  1.00 18.52 ? 302 A1H0T A CAJ  1 
HETATM 7809 N  NAL  . A1H0T F 3 .   ? -27.596 -11.765 14.918  1.00 17.79 ? 302 A1H0T A NAL  1 
HETATM 7810 C  CAM  . A1H0T F 3 .   ? -26.377 -12.108 14.519  1.00 18.95 ? 302 A1H0T A CAM  1 
HETATM 7811 N  NAO  . A1H0T F 3 .   ? -25.391 -11.213 14.611  1.00 17.80 ? 302 A1H0T A NAO  1 
HETATM 7812 N  NAN  . A1H0T F 3 .   ? -26.132 -13.339 13.995  1.00 20.05 ? 302 A1H0T A NAN  1 
HETATM 7813 C  C    . ACT   G 4 .   ? -20.472 -16.304 2.590   1.00 21.21 ? 303 ACT   A C    1 
HETATM 7814 O  O    . ACT   G 4 .   ? -21.184 -15.815 1.688   1.00 20.90 ? 303 ACT   A O    1 
HETATM 7815 O  OXT  . ACT   G 4 .   ? -20.830 -16.496 3.767   1.00 21.63 ? 303 ACT   A OXT  1 
HETATM 7816 C  CH3  . ACT   G 4 .   ? -19.051 -16.739 2.191   1.00 24.77 ? 303 ACT   A CH3  1 
HETATM 7817 C  C    . ACT   H 4 .   ? -16.974 3.371   27.762  0.80 12.15 ? 304 ACT   A C    1 
HETATM 7818 O  O    . ACT   H 4 .   ? -16.574 4.057   26.801  0.80 27.60 ? 304 ACT   A O    1 
HETATM 7819 O  OXT  . ACT   H 4 .   ? -18.188 2.850   27.760  0.80 17.14 ? 304 ACT   A OXT  1 
HETATM 7820 C  CH3  . ACT   H 4 .   ? -16.063 3.105   28.969  0.80 24.32 ? 304 ACT   A CH3  1 
HETATM 7821 P  PA   . NDP   I 2 .   ? -57.620 11.342  -1.049  0.80 20.20 ? 301 NDP   B PA   1 
HETATM 7822 O  O1A  . NDP   I 2 .   ? -57.319 12.079  -2.303  0.80 21.95 ? 301 NDP   B O1A  1 
HETATM 7823 O  O2A  . NDP   I 2 .   ? -58.092 12.112  0.124   0.80 20.71 ? 301 NDP   B O2A  1 
HETATM 7824 O  O5B  . NDP   I 2 .   ? -58.700 10.185  -1.308  0.80 20.06 ? 301 NDP   B O5B  1 
HETATM 7825 C  C5B  . NDP   I 2 .   ? -58.416 9.116   -2.230  0.80 21.55 ? 301 NDP   B C5B  1 
HETATM 7826 C  C4B  . NDP   I 2 .   ? -59.712 8.727   -2.886  0.80 19.53 ? 301 NDP   B C4B  1 
HETATM 7827 O  O4B  . NDP   I 2 .   ? -60.556 8.074   -1.911  0.80 18.04 ? 301 NDP   B O4B  1 
HETATM 7828 C  C3B  . NDP   I 2 .   ? -60.606 9.870   -3.389  0.80 21.08 ? 301 NDP   B C3B  1 
HETATM 7829 O  O3B  . NDP   I 2 .   ? -60.159 10.348  -4.654  0.80 23.32 ? 301 NDP   B O3B  1 
HETATM 7830 C  C2B  . NDP   I 2 .   ? -61.992 9.220   -3.415  0.80 20.06 ? 301 NDP   B C2B  1 
HETATM 7831 O  O2B  . NDP   I 2 .   ? -62.471 8.840   -4.711  0.80 20.12 ? 301 NDP   B O2B  1 
HETATM 7832 C  C1B  . NDP   I 2 .   ? -61.808 7.974   -2.539  0.80 18.98 ? 301 NDP   B C1B  1 
HETATM 7833 N  N9A  . NDP   I 2 .   ? -62.894 7.878   -1.577  0.80 19.48 ? 301 NDP   B N9A  1 
HETATM 7834 C  C8A  . NDP   I 2 .   ? -63.219 8.751   -0.567  0.80 20.75 ? 301 NDP   B C8A  1 
HETATM 7835 N  N7A  . NDP   I 2 .   ? -64.354 8.457   0.016   0.80 20.77 ? 301 NDP   B N7A  1 
HETATM 7836 C  C5A  . NDP   I 2 .   ? -64.812 7.335   -0.671  0.80 20.51 ? 301 NDP   B C5A  1 
HETATM 7837 C  C6A  . NDP   I 2 .   ? -65.974 6.545   -0.551  0.80 20.60 ? 301 NDP   B C6A  1 
HETATM 7838 N  N6A  . NDP   I 2 .   ? -66.912 6.765   0.363   0.80 22.12 ? 301 NDP   B N6A  1 
HETATM 7839 N  N1A  . NDP   I 2 .   ? -66.123 5.510   -1.415  0.80 19.13 ? 301 NDP   B N1A  1 
HETATM 7840 C  C2A  . NDP   I 2 .   ? -65.162 5.284   -2.323  0.80 17.67 ? 301 NDP   B C2A  1 
HETATM 7841 N  N3A  . NDP   I 2 .   ? -64.023 5.951   -2.525  0.80 18.73 ? 301 NDP   B N3A  1 
HETATM 7842 C  C4A  . NDP   I 2 .   ? -63.925 6.986   -1.674  0.80 19.38 ? 301 NDP   B C4A  1 
HETATM 7843 O  O3   . NDP   I 2 .   ? -56.307 10.496  -0.645  0.80 18.72 ? 301 NDP   B O3   1 
HETATM 7844 P  PN   . NDP   I 2 .   ? -54.753 10.846  -0.842  0.80 18.76 ? 301 NDP   B PN   1 
HETATM 7845 O  O1N  . NDP   I 2 .   ? -54.492 12.165  -0.197  0.80 18.86 ? 301 NDP   B O1N  1 
HETATM 7846 O  O2N  . NDP   I 2 .   ? -54.386 10.639  -2.263  0.80 18.32 ? 301 NDP   B O2N  1 
HETATM 7847 O  O5D  . NDP   I 2 .   ? -54.070 9.697   0.068   0.80 17.52 ? 301 NDP   B O5D  1 
HETATM 7848 C  C5D  . NDP   I 2 .   ? -53.976 8.337   -0.429  0.80 16.91 ? 301 NDP   B C5D  1 
HETATM 7849 C  C4D  . NDP   I 2 .   ? -53.918 7.400   0.755   0.80 17.33 ? 301 NDP   B C4D  1 
HETATM 7850 O  O4D  . NDP   I 2 .   ? -52.789 7.749   1.602   0.80 16.65 ? 301 NDP   B O4D  1 
HETATM 7851 C  C3D  . NDP   I 2 .   ? -55.147 7.414   1.677   0.80 17.59 ? 301 NDP   B C3D  1 
HETATM 7852 O  O3D  . NDP   I 2 .   ? -55.424 6.108   2.162   0.80 16.19 ? 301 NDP   B O3D  1 
HETATM 7853 C  C2D  . NDP   I 2 .   ? -54.696 8.303   2.828   0.80 17.61 ? 301 NDP   B C2D  1 
HETATM 7854 O  O2D  . NDP   I 2 .   ? -55.305 8.109   4.098   0.80 18.55 ? 301 NDP   B O2D  1 
HETATM 7855 C  C1D  . NDP   I 2 .   ? -53.212 7.981   2.916   0.80 17.45 ? 301 NDP   B C1D  1 
HETATM 7856 N  N1N  . NDP   I 2 .   ? -52.462 9.142   3.469   0.80 18.14 ? 301 NDP   B N1N  1 
HETATM 7857 C  C2N  . NDP   I 2 .   ? -52.358 10.320  2.765   0.80 17.81 ? 301 NDP   B C2N  1 
HETATM 7858 C  C3N  . NDP   I 2 .   ? -51.708 11.411  3.295   0.80 17.99 ? 301 NDP   B C3N  1 
HETATM 7859 C  C7N  . NDP   I 2 .   ? -51.542 12.667  2.533   0.80 17.94 ? 301 NDP   B C7N  1 
HETATM 7860 O  O7N  . NDP   I 2 .   ? -50.813 13.536  3.021   0.80 19.54 ? 301 NDP   B O7N  1 
HETATM 7861 N  N7N  . NDP   I 2 .   ? -52.195 12.869  1.395   0.80 17.56 ? 301 NDP   B N7N  1 
HETATM 7862 C  C4N  . NDP   I 2 .   ? -51.127 11.297  4.650   0.80 18.29 ? 301 NDP   B C4N  1 
HETATM 7863 C  C5N  . NDP   I 2 .   ? -51.328 10.015  5.334   0.80 17.89 ? 301 NDP   B C5N  1 
HETATM 7864 C  C6N  . NDP   I 2 .   ? -51.952 9.024   4.741   0.80 17.42 ? 301 NDP   B C6N  1 
HETATM 7865 P  P2B  . NDP   I 2 .   ? -63.257 9.930   -5.655  0.80 20.76 ? 301 NDP   B P2B  1 
HETATM 7866 O  O1X  . NDP   I 2 .   ? -62.426 11.184  -5.788  0.80 22.20 ? 301 NDP   B O1X  1 
HETATM 7867 O  O2X  . NDP   I 2 .   ? -63.385 9.156   -6.935  0.80 19.74 ? 301 NDP   B O2X  1 
HETATM 7868 O  O3X  . NDP   I 2 .   ? -64.590 10.194  -4.971  0.80 23.24 ? 301 NDP   B O3X  1 
HETATM 7869 N  NAI  . A1H0T J 3 .   ? -54.614 12.918  4.284   0.80 23.95 ? 302 A1H0T B NAI  1 
HETATM 7870 C  CAF  . A1H0T J 3 .   ? -53.731 13.396  5.175   0.80 26.22 ? 302 A1H0T B CAF  1 
HETATM 7871 C  CAE  . A1H0T J 3 .   ? -53.027 14.542  5.194   0.80 30.88 ? 302 A1H0T B CAE  1 
HETATM 7872 CL CLAH . A1H0T J 3 .   ? -53.256 15.670  3.838   0.80 37.17 ? 302 A1H0T B CLAH 1 
HETATM 7873 C  CAD  . A1H0T J 3 .   ? -52.163 14.819  6.267   0.80 30.69 ? 302 A1H0T B CAD  1 
HETATM 7874 C  CAA  . A1H0T J 3 .   ? -52.043 13.877  7.295   0.80 33.86 ? 302 A1H0T B CAA  1 
HETATM 7875 CL CLAB . A1H0T J 3 .   ? -50.967 14.112  8.727   0.80 41.12 ? 302 A1H0T B CLAB 1 
HETATM 7876 C  CAG  . A1H0T J 3 .   ? -52.801 12.706  7.220   0.80 29.95 ? 302 A1H0T B CAG  1 
HETATM 7877 C  CAC  . A1H0T J 3 .   ? -53.612 12.496  6.169   0.80 25.70 ? 302 A1H0T B CAC  1 
HETATM 7878 N  NAK  . A1H0T J 3 .   ? -54.396 11.449  5.897   0.80 21.56 ? 302 A1H0T B NAK  1 
HETATM 7879 C  CAJ  . A1H0T J 3 .   ? -55.004 11.713  4.753   0.80 21.73 ? 302 A1H0T B CAJ  1 
HETATM 7880 N  NAL  . A1H0T J 3 .   ? -55.889 10.864  4.224   0.80 20.03 ? 302 A1H0T B NAL  1 
HETATM 7881 C  CAM  . A1H0T J 3 .   ? -56.673 11.094  3.170   0.80 20.38 ? 302 A1H0T B CAM  1 
HETATM 7882 N  NAO  . A1H0T J 3 .   ? -57.559 10.177  2.753   0.80 20.37 ? 302 A1H0T B NAO  1 
HETATM 7883 N  NAN  . A1H0T J 3 .   ? -56.529 12.216  2.443   0.80 20.08 ? 302 A1H0T B NAN  1 
HETATM 7884 P  PA   . NDP   K 2 .   ? -32.149 13.299  37.380  0.90 18.02 ? 301 NDP   C PA   1 
HETATM 7885 O  O1A  . NDP   K 2 .   ? -32.460 14.200  38.534  0.90 20.71 ? 301 NDP   C O1A  1 
HETATM 7886 O  O2A  . NDP   K 2 .   ? -31.669 13.878  36.108  0.90 18.74 ? 301 NDP   C O2A  1 
HETATM 7887 O  O5B  . NDP   K 2 .   ? -31.060 12.196  37.801  0.90 18.67 ? 301 NDP   C O5B  1 
HETATM 7888 C  C5B  . NDP   K 2 .   ? -31.363 11.340  38.932  0.90 19.46 ? 301 NDP   C C5B  1 
HETATM 7889 C  C4B  . NDP   K 2 .   ? -30.062 11.004  39.612  0.90 19.06 ? 301 NDP   C C4B  1 
HETATM 7890 O  O4B  . NDP   K 2 .   ? -29.244 10.224  38.711  0.90 16.37 ? 301 NDP   C O4B  1 
HETATM 7891 C  C3B  . NDP   K 2 .   ? -29.137 12.187  39.925  0.90 19.16 ? 301 NDP   C C3B  1 
HETATM 7892 O  O3B  . NDP   K 2 .   ? -29.585 12.865  41.094  0.90 22.47 ? 301 NDP   C O3B  1 
HETATM 7893 C  C2B  . NDP   K 2 .   ? -27.765 11.513  40.046  0.90 18.53 ? 301 NDP   C C2B  1 
HETATM 7894 O  O2B  . NDP   K 2 .   ? -27.325 11.260  41.399  0.90 17.76 ? 301 NDP   C O2B  1 
HETATM 7895 C  C1B  . NDP   K 2 .   ? -27.972 10.181  39.312  0.90 16.93 ? 301 NDP   C C1B  1 
HETATM 7896 N  N9A  . NDP   K 2 .   ? -26.900 9.965   38.353  0.90 16.51 ? 301 NDP   C N9A  1 
HETATM 7897 C  C8A  . NDP   K 2 .   ? -26.538 10.741  37.277  0.90 18.14 ? 301 NDP   C C8A  1 
HETATM 7898 N  N7A  . NDP   K 2 .   ? -25.410 10.369  36.731  0.90 18.18 ? 301 NDP   C N7A  1 
HETATM 7899 C  C5A  . NDP   K 2 .   ? -24.986 9.300   37.520  0.90 17.99 ? 301 NDP   C C5A  1 
HETATM 7900 C  C6A  . NDP   K 2 .   ? -23.845 8.475   37.472  0.90 18.37 ? 301 NDP   C C6A  1 
HETATM 7901 N  N6A  . NDP   K 2 .   ? -22.885 8.606   36.568  0.90 19.03 ? 301 NDP   C N6A  1 
HETATM 7902 N  N1A  . NDP   K 2 .   ? -23.728 7.508   38.414  0.90 16.35 ? 301 NDP   C N1A  1 
HETATM 7903 C  C2A  . NDP   K 2 .   ? -24.703 7.376   39.323  0.90 16.57 ? 301 NDP   C C2A  1 
HETATM 7904 N  N3A  . NDP   K 2 .   ? -25.826 8.083   39.461  0.90 16.42 ? 301 NDP   C N3A  1 
HETATM 7905 C  C4A  . NDP   K 2 .   ? -25.887 9.059   38.537  0.90 17.09 ? 301 NDP   C C4A  1 
HETATM 7906 O  O3   . NDP   K 2 .   ? -33.455 12.393  37.146  0.90 17.69 ? 301 NDP   C O3   1 
HETATM 7907 P  PN   . NDP   K 2 .   ? -34.998 12.796  37.274  0.90 17.08 ? 301 NDP   C PN   1 
HETATM 7908 O  O1N  . NDP   K 2 .   ? -35.251 14.034  36.484  0.90 19.02 ? 301 NDP   C O1N  1 
HETATM 7909 O  O2N  . NDP   K 2 .   ? -35.367 12.719  38.705  0.90 16.55 ? 301 NDP   C O2N  1 
HETATM 7910 O  O5D  . NDP   K 2 .   ? -35.688 11.571  36.492  0.90 17.38 ? 301 NDP   C O5D  1 
HETATM 7911 C  C5D  . NDP   K 2 .   ? -35.737 10.278  37.153  0.90 17.41 ? 301 NDP   C C5D  1 
HETATM 7912 C  C4D  . NDP   K 2 .   ? -35.812 9.211   36.085  0.90 15.65 ? 301 NDP   C C4D  1 
HETATM 7913 O  O4D  . NDP   K 2 .   ? -36.966 9.447   35.230  0.90 16.05 ? 301 NDP   C O4D  1 
HETATM 7914 C  C3D  . NDP   K 2 .   ? -34.603 9.140   35.138  0.90 16.42 ? 301 NDP   C C3D  1 
HETATM 7915 O  O3D  . NDP   K 2 .   ? -34.386 7.785   34.791  0.90 15.02 ? 301 NDP   C O3D  1 
HETATM 7916 C  C2D  . NDP   K 2 .   ? -35.092 9.853   33.888  0.90 16.54 ? 301 NDP   C C2D  1 
HETATM 7917 O  O2D  . NDP   K 2 .   ? -34.436 9.541   32.650  0.90 17.21 ? 301 NDP   C O2D  1 
HETATM 7918 C  C1D  . NDP   K 2 .   ? -36.576 9.491   33.882  0.90 15.88 ? 301 NDP   C C1D  1 
HETATM 7919 N  N1N  . NDP   K 2 .   ? -37.354 10.577  33.230  0.90 16.14 ? 301 NDP   C N1N  1 
HETATM 7920 C  C2N  . NDP   K 2 .   ? -37.415 11.830  33.792  0.90 16.30 ? 301 NDP   C C2N  1 
HETATM 7921 C  C3N  . NDP   K 2 .   ? -38.083 12.855  33.164  0.90 15.86 ? 301 NDP   C C3N  1 
HETATM 7922 C  C7N  . NDP   K 2 .   ? -38.215 14.204  33.746  0.90 17.54 ? 301 NDP   C C7N  1 
HETATM 7923 O  O7N  . NDP   K 2 .   ? -39.013 14.979  33.206  0.90 18.84 ? 301 NDP   C O7N  1 
HETATM 7924 N  N7N  . NDP   K 2 .   ? -37.495 14.564  34.800  0.90 17.88 ? 301 NDP   C N7N  1 
HETATM 7925 C  C4N  . NDP   K 2 .   ? -38.694 12.629  31.849  0.90 16.85 ? 301 NDP   C C4N  1 
HETATM 7926 C  C5N  . NDP   K 2 .   ? -38.511 11.296  31.313  0.90 15.60 ? 301 NDP   C C5N  1 
HETATM 7927 C  C6N  . NDP   K 2 .   ? -37.912 10.341  31.990  0.90 16.34 ? 301 NDP   C C6N  1 
HETATM 7928 P  P2B  . NDP   K 2 .   ? -26.550 12.401  42.249  0.90 19.24 ? 301 NDP   C P2B  1 
HETATM 7929 O  O1X  . NDP   K 2 .   ? -26.433 11.774  43.616  0.90 18.79 ? 301 NDP   C O1X  1 
HETATM 7930 O  O2X  . NDP   K 2 .   ? -25.211 12.638  41.609  0.90 18.54 ? 301 NDP   C O2X  1 
HETATM 7931 O  O3X  . NDP   K 2 .   ? -27.394 13.646  42.271  0.90 19.59 ? 301 NDP   C O3X  1 
HETATM 7932 N  NAI  . A1H0T L 3 .   ? -35.244 14.260  31.864  0.90 20.18 ? 302 A1H0T C NAI  1 
HETATM 7933 C  CAF  . A1H0T L 3 .   ? -36.133 14.589  30.916  0.90 21.70 ? 302 A1H0T C CAF  1 
HETATM 7934 C  CAE  . A1H0T L 3 .   ? -36.886 15.682  30.748  0.90 25.00 ? 302 A1H0T C CAE  1 
HETATM 7935 CL CLAH . A1H0T L 3 .   ? -36.775 17.049  31.867  0.90 29.99 ? 302 A1H0T C CLAH 1 
HETATM 7936 C  CAD  . A1H0T L 3 .   ? -37.751 15.790  29.668  0.90 25.26 ? 302 A1H0T C CAD  1 
HETATM 7937 C  CAA  . A1H0T L 3 .   ? -37.859 14.733  28.777  0.90 25.72 ? 302 A1H0T C CAA  1 
HETATM 7938 CL CLAB . A1H0T L 3 .   ? -38.963 14.862  27.410  0.90 32.16 ? 302 A1H0T C CLAB 1 
HETATM 7939 C  CAG  . A1H0T L 3 .   ? -37.076 13.599  28.976  0.90 22.60 ? 302 A1H0T C CAG  1 
HETATM 7940 C  CAC  . A1H0T L 3 .   ? -36.246 13.558  30.041  0.90 19.95 ? 302 A1H0T C CAC  1 
HETATM 7941 N  NAK  . A1H0T L 3 .   ? -35.434 12.581  30.438  0.90 17.66 ? 302 A1H0T C NAK  1 
HETATM 7942 C  CAJ  . A1H0T L 3 .   ? -34.824 13.008  31.547  0.90 17.86 ? 302 A1H0T C CAJ  1 
HETATM 7943 N  NAL  . A1H0T L 3 .   ? -33.905 12.311  32.212  0.90 17.90 ? 302 A1H0T C NAL  1 
HETATM 7944 C  CAM  . A1H0T L 3 .   ? -33.200 12.694  33.273  0.90 17.65 ? 302 A1H0T C CAM  1 
HETATM 7945 N  NAO  . A1H0T L 3 .   ? -33.390 13.926  33.814  0.90 19.33 ? 302 A1H0T C NAO  1 
HETATM 7946 N  NAN  . A1H0T L 3 .   ? -32.232 11.895  33.778  0.90 17.90 ? 302 A1H0T C NAN  1 
HETATM 7947 C  C    A ACT   M 4 .   ? -25.065 3.729   55.629  0.50 13.22 ? 303 ACT   C C    1 
HETATM 7948 C  C    B ACT   M 4 .   ? -24.679 -0.208  54.446  0.50 19.59 ? 303 ACT   C C    1 
HETATM 7949 O  O    A ACT   M 4 .   ? -24.035 4.195   55.029  0.50 21.97 ? 303 ACT   C O    1 
HETATM 7950 O  O    B ACT   M 4 .   ? -23.752 -1.027  54.090  0.50 21.77 ? 303 ACT   C O    1 
HETATM 7951 O  OXT  A ACT   M 4 .   ? -26.219 4.230   55.544  0.50 16.27 ? 303 ACT   C OXT  1 
HETATM 7952 O  OXT  B ACT   M 4 .   ? -25.826 -0.577  54.814  0.50 23.56 ? 303 ACT   C OXT  1 
HETATM 7953 C  CH3  A ACT   M 4 .   ? -24.875 2.507   56.514  0.50 20.06 ? 303 ACT   C CH3  1 
HETATM 7954 C  CH3  B ACT   M 4 .   ? -24.379 1.271   54.499  0.50 22.90 ? 303 ACT   C CH3  1 
HETATM 7955 P  PA   . NDP   N 2 .   ? -66.868 -11.757 27.187  1.00 21.18 ? 301 NDP   D PA   1 
HETATM 7956 O  O1A  . NDP   N 2 .   ? -67.324 -12.578 28.348  1.00 22.55 ? 301 NDP   D O1A  1 
HETATM 7957 O  O2A  . NDP   N 2 .   ? -66.462 -12.445 25.934  1.00 21.48 ? 301 NDP   D O2A  1 
HETATM 7958 O  O5B  . NDP   N 2 .   ? -67.969 -10.647 26.832  1.00 21.35 ? 301 NDP   D O5B  1 
HETATM 7959 C  C5B  . NDP   N 2 .   ? -68.403 -9.696  27.828  1.00 22.26 ? 301 NDP   D C5B  1 
HETATM 7960 C  C4B  . NDP   N 2 .   ? -69.824 -9.291  27.529  1.00 20.65 ? 301 NDP   D C4B  1 
HETATM 7961 O  O4B  . NDP   N 2 .   ? -69.890 -8.636  26.245  1.00 19.05 ? 301 NDP   D O4B  1 
HETATM 7962 C  C3B  . NDP   N 2 .   ? -70.818 -10.441 27.333  1.00 21.94 ? 301 NDP   D C3B  1 
HETATM 7963 O  O3B  . NDP   N 2 .   ? -71.223 -11.004 28.576  1.00 24.47 ? 301 NDP   D O3B  1 
HETATM 7964 C  C2B  . NDP   N 2 .   ? -71.939 -9.766  26.539  1.00 20.60 ? 301 NDP   D C2B  1 
HETATM 7965 O  O2B  . NDP   N 2 .   ? -73.071 -9.359  27.318  1.00 21.21 ? 301 NDP   D O2B  1 
HETATM 7966 C  C1B  . NDP   N 2 .   ? -71.255 -8.518  25.953  1.00 19.08 ? 301 NDP   D C1B  1 
HETATM 7967 N  N9A  . NDP   N 2 .   ? -71.510 -8.413  24.521  1.00 20.31 ? 301 NDP   D N9A  1 
HETATM 7968 C  C8A  . NDP   N 2 .   ? -71.145 -9.269  23.509  1.00 20.04 ? 301 NDP   D C8A  1 
HETATM 7969 N  N7A  . NDP   N 2 .   ? -71.705 -8.973  22.359  1.00 20.89 ? 301 NDP   D N7A  1 
HETATM 7970 C  C5A  . NDP   N 2 .   ? -72.505 -7.870  22.633  1.00 20.58 ? 301 NDP   D C5A  1 
HETATM 7971 C  C6A  . NDP   N 2 .   ? -73.370 -7.084  21.838  1.00 20.35 ? 301 NDP   D C6A  1 
HETATM 7972 N  N6A  . NDP   N 2 .   ? -73.594 -7.279  20.538  1.00 23.12 ? 301 NDP   D N6A  1 
HETATM 7973 N  N1A  . NDP   N 2 .   ? -74.015 -6.064  22.449  1.00 19.27 ? 301 NDP   D N1A  1 
HETATM 7974 C  C2A  . NDP   N 2 .   ? -73.789 -5.836  23.750  1.00 20.72 ? 301 NDP   D C2A  1 
HETATM 7975 N  N3A  . NDP   N 2 .   ? -72.998 -6.500  24.592  1.00 19.65 ? 301 NDP   D N3A  1 
HETATM 7976 C  C4A  . NDP   N 2 .   ? -72.389 -7.518  23.965  1.00 19.63 ? 301 NDP   D C4A  1 
HETATM 7977 O  O3   . NDP   N 2 .   ? -65.689 -10.821 27.734  1.00 20.42 ? 301 NDP   D O3   1 
HETATM 7978 P  PN   . NDP   N 2 .   ? -64.537 -11.190 28.773  1.00 19.88 ? 301 NDP   D PN   1 
HETATM 7979 O  O1N  . NDP   N 2 .   ? -63.886 -12.478 28.375  1.00 20.30 ? 301 NDP   D O1N  1 
HETATM 7980 O  O2N  . NDP   N 2 .   ? -65.033 -11.007 30.175  1.00 20.19 ? 301 NDP   D O2N  1 
HETATM 7981 O  O5D  . NDP   N 2 .   ? -63.465 -10.045 28.404  1.00 18.77 ? 301 NDP   D O5D  1 
HETATM 7982 C  C5D  . NDP   N 2 .   ? -63.707 -8.687  28.852  1.00 17.97 ? 301 NDP   D C5D  1 
HETATM 7983 C  C4D  . NDP   N 2 .   ? -62.977 -7.721  27.945  1.00 16.90 ? 301 NDP   D C4D  1 
HETATM 7984 O  O4D  . NDP   N 2 .   ? -61.548 -8.009  27.990  1.00 17.50 ? 301 NDP   D O4D  1 
HETATM 7985 C  C3D  . NDP   N 2 .   ? -63.369 -7.746  26.458  1.00 17.06 ? 301 NDP   D C3D  1 
HETATM 7986 O  O3D  . NDP   N 2 .   ? -63.275 -6.459  25.860  1.00 16.95 ? 301 NDP   D O3D  1 
HETATM 7987 C  C2D  . NDP   N 2 .   ? -62.294 -8.651  25.875  1.00 17.37 ? 301 NDP   D C2D  1 
HETATM 7988 O  O2D  . NDP   N 2 .   ? -62.022 -8.446  24.497  1.00 19.17 ? 301 NDP   D O2D  1 
HETATM 7989 C  C1D  . NDP   N 2 .   ? -61.068 -8.252  26.686  1.00 17.76 ? 301 NDP   D C1D  1 
HETATM 7990 N  N1N  . NDP   N 2 .   ? -60.110 -9.392  26.728  1.00 17.54 ? 301 NDP   D N1N  1 
HETATM 7991 C  C2N  . NDP   N 2 .   ? -60.447 -10.572 27.352  1.00 18.14 ? 301 NDP   D C2N  1 
HETATM 7992 C  C3N  . NDP   N 2 .   ? -59.574 -11.631 27.375  1.00 18.76 ? 301 NDP   D C3N  1 
HETATM 7993 C  C7N  . NDP   N 2 .   ? -59.881 -12.878 28.081  1.00 20.50 ? 301 NDP   D C7N  1 
HETATM 7994 O  O7N  . NDP   N 2 .   ? -58.968 -13.707 28.197  1.00 21.74 ? 301 NDP   D O7N  1 
HETATM 7995 N  N7N  . NDP   N 2 .   ? -61.107 -13.101 28.538  1.00 20.08 ? 301 NDP   D N7N  1 
HETATM 7996 C  C4N  . NDP   N 2 .   ? -58.279 -11.527 26.649  1.00 19.59 ? 301 NDP   D C4N  1 
HETATM 7997 C  C5N  . NDP   N 2 .   ? -58.036 -10.250 25.995  1.00 18.52 ? 301 NDP   D C5N  1 
HETATM 7998 C  C6N  . NDP   N 2 .   ? -58.907 -9.261  26.064  1.00 18.58 ? 301 NDP   D C6N  1 
HETATM 7999 P  P2B  . NDP   N 2 .   ? -74.304 -10.398 27.577  1.00 22.32 ? 301 NDP   D P2B  1 
HETATM 8000 O  O1X  . NDP   N 2 .   ? -73.698 -11.665 28.158  1.00 23.02 ? 301 NDP   D O1X  1 
HETATM 8001 O  O2X  . NDP   N 2 .   ? -75.201 -9.628  28.521  1.00 21.61 ? 301 NDP   D O2X  1 
HETATM 8002 O  O3X  . NDP   N 2 .   ? -74.953 -10.645 26.236  1.00 22.32 ? 301 NDP   D O3X  1 
HETATM 8003 N  NAI  . A1H0T O 3 .   ? -61.090 -13.211 24.763  1.00 23.02 ? 302 A1H0T D NAI  1 
HETATM 8004 C  CAF  . A1H0T O 3 .   ? -59.830 -13.610 24.573  1.00 25.04 ? 302 A1H0T D CAF  1 
HETATM 8005 C  CAE  . A1H0T O 3 .   ? -59.171 -14.703 24.981  1.00 28.61 ? 302 A1H0T D CAE  1 
HETATM 8006 CL CLAH . A1H0T O 3 .   ? -60.033 -15.899 25.932  1.00 33.34 ? 302 A1H0T D CLAH 1 
HETATM 8007 C  CAD  . A1H0T O 3 .   ? -57.828 -14.891 24.667  1.00 29.81 ? 302 A1H0T D CAD  1 
HETATM 8008 C  CAA  . A1H0T O 3 .   ? -57.181 -13.912 23.913  1.00 29.63 ? 302 A1H0T D CAA  1 
HETATM 8009 CL CLAB . A1H0T O 3 .   ? -55.462 -14.063 23.481  1.00 37.01 ? 302 A1H0T D CLAB 1 
HETATM 8010 C  CAG  . A1H0T O 3 .   ? -57.893 -12.788 23.519  1.00 26.68 ? 302 A1H0T D CAG  1 
HETATM 8011 C  CAC  . A1H0T O 3 .   ? -59.191 -12.672 23.853  1.00 22.94 ? 302 A1H0T D CAC  1 
HETATM 8012 N  NAK  . A1H0T O 3 .   ? -60.048 -11.684 23.607  1.00 20.93 ? 302 A1H0T D NAK  1 
HETATM 8013 C  CAJ  . A1H0T O 3 .   ? -61.212 -12.012 24.139  1.00 21.15 ? 302 A1H0T D CAJ  1 
HETATM 8014 N  NAL  . A1H0T O 3 .   ? -62.300 -11.226 24.035  1.00 20.35 ? 302 A1H0T D NAL  1 
HETATM 8015 C  CAM  . A1H0T O 3 .   ? -63.534 -11.499 24.487  1.00 19.79 ? 302 A1H0T D CAM  1 
HETATM 8016 N  NAO  . A1H0T O 3 .   ? -63.755 -12.657 25.138  1.00 20.34 ? 302 A1H0T D NAO  1 
HETATM 8017 N  NAN  . A1H0T O 3 .   ? -64.550 -10.657 24.280  1.00 19.96 ? 302 A1H0T D NAN  1 
HETATM 8018 O  O    . HOH   P 5 .   ? -27.656 -14.052 -4.286  1.00 32.85 ? 401 HOH   A O    1 
HETATM 8019 O  O    . HOH   P 5 .   ? -16.302 11.944  15.234  1.00 39.31 ? 402 HOH   A O    1 
HETATM 8020 O  O    . HOH   P 5 .   ? -33.086 -22.632 19.206  1.00 37.24 ? 403 HOH   A O    1 
HETATM 8021 O  O    . HOH   P 5 .   ? -14.802 -15.327 -2.212  1.00 27.04 ? 404 HOH   A O    1 
HETATM 8022 O  O    . HOH   P 5 .   ? -33.697 -29.706 6.550   1.00 37.87 ? 405 HOH   A O    1 
HETATM 8023 O  O    . HOH   P 5 .   ? -8.351  -7.523  -4.368  1.00 37.92 ? 406 HOH   A O    1 
HETATM 8024 O  O    . HOH   P 5 .   ? -7.001  1.237   8.776   1.00 36.60 ? 407 HOH   A O    1 
HETATM 8025 O  O    . HOH   P 5 .   ? -44.295 -9.450  9.929   1.00 17.82 ? 408 HOH   A O    1 
HETATM 8026 O  O    . HOH   P 5 .   ? -32.700 -21.900 -0.797  1.00 30.99 ? 409 HOH   A O    1 
HETATM 8027 O  O    . HOH   P 5 .   ? -23.284 -2.994  13.781  1.00 18.70 ? 410 HOH   A O    1 
HETATM 8028 O  O    . HOH   P 5 .   ? -24.882 17.053  15.126  1.00 34.51 ? 411 HOH   A O    1 
HETATM 8029 O  O    . HOH   P 5 .   ? -35.090 -12.060 14.698  1.00 40.70 ? 412 HOH   A O    1 
HETATM 8030 O  O    . HOH   P 5 .   ? -9.068  9.624   5.004   1.00 46.07 ? 413 HOH   A O    1 
HETATM 8031 O  O    . HOH   P 5 .   ? -32.620 11.616  7.972   1.00 15.73 ? 414 HOH   A O    1 
HETATM 8032 O  O    . HOH   P 5 .   ? -34.966 -31.685 10.815  1.00 41.63 ? 415 HOH   A O    1 
HETATM 8033 O  O    . HOH   P 5 .   ? -13.392 9.999   9.282   1.00 40.24 ? 416 HOH   A O    1 
HETATM 8034 O  O    . HOH   P 5 .   ? -11.546 -0.967  18.418  1.00 21.72 ? 417 HOH   A O    1 
HETATM 8035 O  O    . HOH   P 5 .   ? -13.813 -8.506  22.513  1.00 32.70 ? 418 HOH   A O    1 
HETATM 8036 O  O    . HOH   P 5 .   ? -44.246 -6.998  14.230  1.00 31.58 ? 419 HOH   A O    1 
HETATM 8037 O  O    . HOH   P 5 .   ? -26.035 -21.437 8.395   1.00 41.57 ? 420 HOH   A O    1 
HETATM 8038 O  O    . HOH   P 5 .   ? -19.237 -18.098 5.085   1.00 30.10 ? 421 HOH   A O    1 
HETATM 8039 O  O    . HOH   P 5 .   ? -27.208 13.034  19.008  1.00 17.34 ? 422 HOH   A O    1 
HETATM 8040 O  O    . HOH   P 5 .   ? -14.765 11.074  13.242  1.00 34.26 ? 423 HOH   A O    1 
HETATM 8041 O  O    . HOH   P 5 .   ? -16.031 -14.089 1.677   1.00 23.06 ? 424 HOH   A O    1 
HETATM 8042 O  O    . HOH   P 5 .   ? -39.848 -14.935 23.787  1.00 19.45 ? 425 HOH   A O    1 
HETATM 8043 O  O    . HOH   P 5 .   ? -15.669 -10.827 15.164  1.00 25.11 ? 426 HOH   A O    1 
HETATM 8044 O  O    . HOH   P 5 .   ? -23.087 -13.858 1.542   1.00 19.22 ? 427 HOH   A O    1 
HETATM 8045 O  O    . HOH   P 5 .   ? -28.328 -27.580 17.049  1.00 34.23 ? 428 HOH   A O    1 
HETATM 8046 O  O    . HOH   P 5 .   ? -29.447 18.620  12.994  1.00 34.70 ? 429 HOH   A O    1 
HETATM 8047 O  O    . HOH   P 5 .   ? -8.733  -14.580 -3.799  1.00 46.60 ? 430 HOH   A O    1 
HETATM 8048 O  O    . HOH   P 5 .   ? -45.006 -14.006 19.580  1.00 24.56 ? 431 HOH   A O    1 
HETATM 8049 O  O    . HOH   P 5 .   ? -12.401 -1.347  20.970  1.00 21.27 ? 432 HOH   A O    1 
HETATM 8050 O  O    . HOH   P 5 .   ? -21.410 -1.532  12.359  1.00 15.93 ? 433 HOH   A O    1 
HETATM 8051 O  O    . HOH   P 5 .   ? -41.163 -25.075 15.302  1.00 37.68 ? 434 HOH   A O    1 
HETATM 8052 O  O    . HOH   P 5 .   ? -19.208 -11.212 7.958   1.00 27.79 ? 435 HOH   A O    1 
HETATM 8053 O  O    . HOH   P 5 .   ? -21.727 -12.796 15.227  1.00 24.37 ? 436 HOH   A O    1 
HETATM 8054 O  O    . HOH   P 5 .   ? -29.329 -25.827 6.324   1.00 39.15 ? 437 HOH   A O    1 
HETATM 8055 O  O    . HOH   P 5 .   ? -22.762 -10.762 8.000   1.00 16.35 ? 438 HOH   A O    1 
HETATM 8056 O  O    . HOH   P 5 .   ? -36.731 -30.203 13.584  1.00 41.52 ? 439 HOH   A O    1 
HETATM 8057 O  O    . HOH   P 5 .   ? -32.992 18.135  4.480   1.00 27.21 ? 440 HOH   A O    1 
HETATM 8058 O  O    . HOH   P 5 .   ? -25.442 6.714   -2.884  1.00 25.42 ? 441 HOH   A O    1 
HETATM 8059 O  O    . HOH   P 5 .   ? -44.078 -7.873  22.689  1.00 28.88 ? 442 HOH   A O    1 
HETATM 8060 O  O    . HOH   P 5 .   ? -33.627 -11.822 25.960  1.00 18.69 ? 443 HOH   A O    1 
HETATM 8061 O  O    . HOH   P 5 .   ? -20.106 -14.617 10.732  1.00 25.65 ? 444 HOH   A O    1 
HETATM 8062 O  O    . HOH   P 5 .   ? -9.268  -0.392  14.831  1.00 32.62 ? 445 HOH   A O    1 
HETATM 8063 O  O    . HOH   P 5 .   ? -44.254 -7.873  18.137  1.00 35.53 ? 446 HOH   A O    1 
HETATM 8064 O  O    . HOH   P 5 .   ? -29.615 -20.793 7.109   1.00 24.17 ? 447 HOH   A O    1 
HETATM 8065 O  O    . HOH   P 5 .   ? -32.655 -15.529 -2.663  1.00 38.27 ? 448 HOH   A O    1 
HETATM 8066 O  O    . HOH   P 5 .   ? -15.235 -11.843 -10.041 1.00 32.52 ? 449 HOH   A O    1 
HETATM 8067 O  O    . HOH   P 5 .   ? -46.286 -20.174 12.294  1.00 33.32 ? 450 HOH   A O    1 
HETATM 8068 O  O    . HOH   P 5 .   ? -35.907 -3.927  15.393  1.00 28.83 ? 451 HOH   A O    1 
HETATM 8069 O  O    . HOH   P 5 .   ? -11.485 3.551   -7.197  1.00 32.48 ? 452 HOH   A O    1 
HETATM 8070 O  O    B HOH   P 5 .   ? -40.738 -22.167 1.016   0.50 32.20 ? 453 HOH   A O    1 
HETATM 8071 O  O    . HOH   P 5 .   ? -28.232 6.182   -0.067  1.00 21.98 ? 454 HOH   A O    1 
HETATM 8072 O  O    . HOH   P 5 .   ? -20.279 11.685  -1.680  1.00 26.30 ? 455 HOH   A O    1 
HETATM 8073 O  O    . HOH   P 5 .   ? -17.809 -3.503  29.654  1.00 25.99 ? 456 HOH   A O    1 
HETATM 8074 O  O    . HOH   P 5 .   ? -40.568 -8.129  17.940  1.00 19.00 ? 457 HOH   A O    1 
HETATM 8075 O  O    . HOH   P 5 .   ? -40.506 -17.631 1.838   1.00 29.74 ? 458 HOH   A O    1 
HETATM 8076 O  O    B HOH   P 5 .   ? -36.466 -7.059  24.484  0.60 17.90 ? 459 HOH   A O    1 
HETATM 8077 O  O    . HOH   P 5 .   ? -30.345 10.284  0.733   1.00 25.43 ? 460 HOH   A O    1 
HETATM 8078 O  O    . HOH   P 5 .   ? -35.348 -12.715 8.075   1.00 20.68 ? 461 HOH   A O    1 
HETATM 8079 O  O    . HOH   P 5 .   ? -22.558 -17.079 25.919  1.00 37.66 ? 462 HOH   A O    1 
HETATM 8080 O  O    . HOH   P 5 .   ? -36.562 -17.365 1.769   1.00 31.92 ? 463 HOH   A O    1 
HETATM 8081 O  O    . HOH   P 5 .   ? -36.512 -7.703  0.857   1.00 16.25 ? 464 HOH   A O    1 
HETATM 8082 O  O    . HOH   P 5 .   ? -43.070 -15.071 16.967  1.00 22.86 ? 465 HOH   A O    1 
HETATM 8083 O  O    . HOH   P 5 .   ? -38.135 -14.829 9.516   1.00 15.59 ? 466 HOH   A O    1 
HETATM 8084 O  O    . HOH   P 5 .   ? -17.851 0.943   -9.158  1.00 39.28 ? 467 HOH   A O    1 
HETATM 8085 O  O    . HOH   P 5 .   ? -24.046 -13.720 31.664  1.00 30.04 ? 468 HOH   A O    1 
HETATM 8086 O  O    . HOH   P 5 .   ? -42.771 -5.732  17.661  1.00 39.07 ? 469 HOH   A O    1 
HETATM 8087 O  O    . HOH   P 5 .   ? -34.447 17.746  11.939  1.00 34.21 ? 470 HOH   A O    1 
HETATM 8088 O  O    . HOH   P 5 .   ? -24.383 9.266   -3.489  1.00 39.16 ? 471 HOH   A O    1 
HETATM 8089 O  O    . HOH   P 5 .   ? -8.041  -14.756 0.792   1.00 35.42 ? 472 HOH   A O    1 
HETATM 8090 O  O    . HOH   P 5 .   ? -5.523  8.184   -0.654  1.00 42.15 ? 473 HOH   A O    1 
HETATM 8091 O  O    . HOH   P 5 .   ? -40.786 -2.085  22.380  1.00 44.53 ? 474 HOH   A O    1 
HETATM 8092 O  O    . HOH   P 5 .   ? -34.299 -3.879  -3.950  1.00 25.76 ? 475 HOH   A O    1 
HETATM 8093 O  O    . HOH   P 5 .   ? -28.048 12.920  0.199   1.00 23.66 ? 476 HOH   A O    1 
HETATM 8094 O  O    . HOH   P 5 .   ? -10.219 0.957   12.632  1.00 29.87 ? 477 HOH   A O    1 
HETATM 8095 O  O    . HOH   P 5 .   ? -20.117 -7.379  -8.807  1.00 35.46 ? 478 HOH   A O    1 
HETATM 8096 O  O    . HOH   P 5 .   ? -39.237 4.044   13.586  1.00 33.33 ? 479 HOH   A O    1 
HETATM 8097 O  O    . HOH   P 5 .   ? -16.240 -5.327  37.937  1.00 27.54 ? 480 HOH   A O    1 
HETATM 8098 O  O    . HOH   P 5 .   ? -30.830 13.293  17.536  1.00 18.74 ? 481 HOH   A O    1 
HETATM 8099 O  O    . HOH   P 5 .   ? -39.886 -25.947 7.095   1.00 40.78 ? 482 HOH   A O    1 
HETATM 8100 O  O    . HOH   P 5 .   ? -31.133 4.679   -7.154  1.00 35.45 ? 483 HOH   A O    1 
HETATM 8101 O  O    . HOH   P 5 .   ? -28.354 3.378   -4.759  1.00 30.33 ? 484 HOH   A O    1 
HETATM 8102 O  O    . HOH   P 5 .   ? -27.325 -11.529 25.014  1.00 15.54 ? 485 HOH   A O    1 
HETATM 8103 O  O    . HOH   P 5 .   ? -41.758 -9.034  6.829   1.00 14.25 ? 486 HOH   A O    1 
HETATM 8104 O  O    . HOH   P 5 .   ? -8.328  2.330   2.374   1.00 30.33 ? 487 HOH   A O    1 
HETATM 8105 O  O    . HOH   P 5 .   ? -9.270  -2.815  15.911  1.00 28.71 ? 488 HOH   A O    1 
HETATM 8106 O  O    . HOH   P 5 .   ? -9.572  -8.005  18.521  1.00 39.05 ? 489 HOH   A O    1 
HETATM 8107 O  O    . HOH   P 5 .   ? -53.787 -18.879 16.027  1.00 38.06 ? 490 HOH   A O    1 
HETATM 8108 O  O    . HOH   P 5 .   ? -5.299  -9.678  -2.742  1.00 52.26 ? 491 HOH   A O    1 
HETATM 8109 O  O    . HOH   P 5 .   ? -18.790 11.629  0.544   1.00 23.13 ? 492 HOH   A O    1 
HETATM 8110 O  O    . HOH   P 5 .   ? -8.201  -3.989  -8.556  1.00 36.04 ? 493 HOH   A O    1 
HETATM 8111 O  O    . HOH   P 5 .   ? -25.841 -4.423  13.701  1.00 23.38 ? 494 HOH   A O    1 
HETATM 8112 O  O    . HOH   P 5 .   ? -16.658 -9.749  8.391   1.00 22.53 ? 495 HOH   A O    1 
HETATM 8113 O  O    . HOH   P 5 .   ? -11.239 -14.346 -4.811  1.00 37.43 ? 496 HOH   A O    1 
HETATM 8114 O  O    . HOH   P 5 .   ? -39.347 8.023   -1.326  1.00 17.15 ? 497 HOH   A O    1 
HETATM 8115 O  O    . HOH   P 5 .   ? -33.235 -5.596  -5.410  1.00 39.80 ? 498 HOH   A O    1 
HETATM 8116 O  O    . HOH   P 5 .   ? -12.801 -8.480  31.950  1.00 43.31 ? 499 HOH   A O    1 
HETATM 8117 O  O    . HOH   P 5 .   ? -15.966 7.824   15.888  1.00 22.88 ? 500 HOH   A O    1 
HETATM 8118 O  O    . HOH   P 5 .   ? -11.100 1.129   27.387  1.00 26.74 ? 501 HOH   A O    1 
HETATM 8119 O  O    . HOH   P 5 .   ? -16.565 3.966   23.419  1.00 28.37 ? 502 HOH   A O    1 
HETATM 8120 O  O    . HOH   P 5 .   ? -27.304 5.430   12.431  1.00 17.02 ? 503 HOH   A O    1 
HETATM 8121 O  O    . HOH   P 5 .   ? -40.450 1.904   11.203  1.00 25.79 ? 504 HOH   A O    1 
HETATM 8122 O  O    . HOH   P 5 .   ? -21.326 -13.554 17.896  1.00 24.81 ? 505 HOH   A O    1 
HETATM 8123 O  O    . HOH   P 5 .   ? -40.138 -24.717 3.276   1.00 40.24 ? 506 HOH   A O    1 
HETATM 8124 O  O    . HOH   P 5 .   ? -17.617 -10.050 19.155  1.00 29.17 ? 507 HOH   A O    1 
HETATM 8125 O  O    . HOH   P 5 .   ? -22.599 -20.326 15.091  1.00 43.08 ? 508 HOH   A O    1 
HETATM 8126 O  O    . HOH   P 5 .   ? -22.953 -19.144 7.212   1.00 24.03 ? 509 HOH   A O    1 
HETATM 8127 O  O    . HOH   P 5 .   ? -18.007 -1.722  27.741  1.00 20.97 ? 510 HOH   A O    1 
HETATM 8128 O  O    . HOH   P 5 .   ? -48.987 -19.699 16.890  1.00 35.78 ? 511 HOH   A O    1 
HETATM 8129 O  O    . HOH   P 5 .   ? -36.956 -14.354 19.184  1.00 29.28 ? 512 HOH   A O    1 
HETATM 8130 O  O    A HOH   P 5 .   ? -40.749 -5.912  14.833  0.70 28.71 ? 513 HOH   A O    1 
HETATM 8131 O  O    B HOH   P 5 .   ? -42.813 -5.429  15.213  0.30 17.54 ? 513 HOH   A O    1 
HETATM 8132 O  O    . HOH   P 5 .   ? -26.572 -10.534 -5.566  1.00 40.06 ? 514 HOH   A O    1 
HETATM 8133 O  O    . HOH   P 5 .   ? -33.184 -3.868  16.342  1.00 29.25 ? 515 HOH   A O    1 
HETATM 8134 O  O    . HOH   P 5 .   ? -8.672  7.305   13.954  1.00 33.66 ? 516 HOH   A O    1 
HETATM 8135 O  O    . HOH   P 5 .   ? -13.550 -12.223 28.940  1.00 28.88 ? 517 HOH   A O    1 
HETATM 8136 O  O    . HOH   P 5 .   ? -36.688 -10.519 -2.301  1.00 23.31 ? 518 HOH   A O    1 
HETATM 8137 O  O    B HOH   P 5 .   ? -14.740 6.324   29.233  0.40 20.92 ? 519 HOH   A O    1 
HETATM 8138 O  O    . HOH   P 5 .   ? -31.127 4.425   4.435   1.00 18.12 ? 520 HOH   A O    1 
HETATM 8139 O  O    . HOH   P 5 .   ? -17.736 -11.822 35.053  1.00 32.39 ? 521 HOH   A O    1 
HETATM 8140 O  O    . HOH   P 5 .   ? -12.036 -3.149  -14.603 1.00 44.98 ? 522 HOH   A O    1 
HETATM 8141 O  O    . HOH   P 5 .   ? -6.989  -2.891  7.753   1.00 29.32 ? 523 HOH   A O    1 
HETATM 8142 O  O    . HOH   P 5 .   ? -29.717 0.982   -4.604  1.00 27.58 ? 524 HOH   A O    1 
HETATM 8143 O  O    . HOH   P 5 .   ? -8.571  -6.827  16.314  1.00 33.42 ? 525 HOH   A O    1 
HETATM 8144 O  O    A HOH   P 5 .   ? -7.723  -3.898  0.561   0.60 24.38 ? 526 HOH   A O    1 
HETATM 8145 O  O    B HOH   P 5 .   ? -7.951  -5.073  -0.188  0.40 26.65 ? 526 HOH   A O    1 
HETATM 8146 O  O    . HOH   P 5 .   ? -29.953 -2.354  -7.578  1.00 43.34 ? 527 HOH   A O    1 
HETATM 8147 O  O    . HOH   P 5 .   ? -41.608 -2.717  8.699   1.00 22.98 ? 528 HOH   A O    1 
HETATM 8148 O  O    . HOH   P 5 .   ? -11.763 -15.796 6.952   1.00 23.14 ? 529 HOH   A O    1 
HETATM 8149 O  O    . HOH   P 5 .   ? -8.729  -15.569 8.088   1.00 33.53 ? 530 HOH   A O    1 
HETATM 8150 O  O    . HOH   P 5 .   ? -26.968 -27.632 9.623   1.00 45.71 ? 531 HOH   A O    1 
HETATM 8151 O  O    . HOH   P 5 .   ? -26.598 -10.518 -2.551  1.00 31.74 ? 532 HOH   A O    1 
HETATM 8152 O  O    . HOH   P 5 .   ? -13.050 -16.092 11.242  1.00 41.09 ? 533 HOH   A O    1 
HETATM 8153 O  O    . HOH   P 5 .   ? -14.918 11.636  10.719  1.00 33.09 ? 534 HOH   A O    1 
HETATM 8154 O  O    . HOH   P 5 .   ? -14.974 -14.273 13.780  1.00 40.89 ? 535 HOH   A O    1 
HETATM 8155 O  O    . HOH   P 5 .   ? -10.964 6.858   20.707  1.00 26.90 ? 536 HOH   A O    1 
HETATM 8156 O  O    . HOH   P 5 .   ? -34.169 3.930   -7.792  1.00 46.41 ? 537 HOH   A O    1 
HETATM 8157 O  O    . HOH   P 5 .   ? -30.004 -29.693 15.830  1.00 35.71 ? 538 HOH   A O    1 
HETATM 8158 O  O    . HOH   P 5 .   ? -29.653 -32.464 12.600  1.00 32.99 ? 539 HOH   A O    1 
HETATM 8159 O  O    A HOH   P 5 .   ? -13.097 -12.443 18.755  0.60 36.86 ? 540 HOH   A O    1 
HETATM 8160 O  O    B HOH   P 5 .   ? -14.774 -10.821 19.288  0.40 32.34 ? 540 HOH   A O    1 
HETATM 8161 O  O    . HOH   P 5 .   ? -11.382 7.974   -6.706  1.00 50.78 ? 541 HOH   A O    1 
HETATM 8162 O  O    . HOH   P 5 .   ? -15.500 -0.877  27.466  1.00 38.18 ? 542 HOH   A O    1 
HETATM 8163 O  O    . HOH   P 5 .   ? -30.653 22.363  5.571   1.00 45.91 ? 543 HOH   A O    1 
HETATM 8164 O  O    . HOH   P 5 .   ? -40.150 -2.384  12.310  1.00 31.74 ? 544 HOH   A O    1 
HETATM 8165 O  O    B HOH   P 5 .   ? -37.801 -22.713 19.818  0.50 34.83 ? 545 HOH   A O    1 
HETATM 8166 O  O    A HOH   P 5 .   ? -21.783 -15.184 28.059  0.30 22.10 ? 546 HOH   A O    1 
HETATM 8167 O  O    B HOH   P 5 .   ? -20.408 -15.856 26.752  0.30 21.26 ? 546 HOH   A O    1 
HETATM 8168 O  O    . HOH   P 5 .   ? -31.096 12.729  0.093   1.00 50.13 ? 547 HOH   A O    1 
HETATM 8169 O  O    B HOH   P 5 .   ? -30.304 -21.132 3.096   0.40 22.22 ? 548 HOH   A O    1 
HETATM 8170 O  O    . HOH   P 5 .   ? -25.677 -17.775 19.681  1.00 47.47 ? 549 HOH   A O    1 
HETATM 8171 O  O    . HOH   P 5 .   ? -8.750  0.012   24.325  1.00 41.25 ? 550 HOH   A O    1 
HETATM 8172 O  O    . HOH   P 5 .   ? -12.181 9.916   17.068  1.00 49.44 ? 551 HOH   A O    1 
HETATM 8173 O  O    . HOH   P 5 .   ? -28.039 18.762  16.386  1.00 41.61 ? 552 HOH   A O    1 
HETATM 8174 O  O    . HOH   P 5 .   ? -7.074  -0.051  6.668   1.00 41.79 ? 553 HOH   A O    1 
HETATM 8175 O  O    . HOH   P 5 .   ? -33.152 -12.068 19.942  1.00 16.47 ? 554 HOH   A O    1 
HETATM 8176 O  O    . HOH   P 5 .   ? -23.265 -16.770 13.136  1.00 33.41 ? 555 HOH   A O    1 
HETATM 8177 O  O    A HOH   P 5 .   ? -13.277 6.675   30.930  0.60 33.61 ? 556 HOH   A O    1 
HETATM 8178 O  O    B HOH   P 5 .   ? -12.978 4.888   31.194  0.40 21.61 ? 556 HOH   A O    1 
HETATM 8179 O  O    . HOH   P 5 .   ? -9.401  8.488   -4.405  1.00 49.71 ? 557 HOH   A O    1 
HETATM 8180 O  O    . HOH   P 5 .   ? -7.225  -3.465  -6.426  1.00 47.28 ? 558 HOH   A O    1 
HETATM 8181 O  O    . HOH   P 5 .   ? -17.155 -12.873 16.404  1.00 30.46 ? 559 HOH   A O    1 
HETATM 8182 O  O    . HOH   P 5 .   ? -40.632 -0.241  12.911  1.00 43.54 ? 560 HOH   A O    1 
HETATM 8183 O  O    A HOH   P 5 .   ? -30.909 -19.356 3.076   0.60 15.39 ? 561 HOH   A O    1 
HETATM 8184 O  O    B HOH   P 5 .   ? -32.840 -19.806 2.454   0.40 25.53 ? 561 HOH   A O    1 
HETATM 8185 O  O    . HOH   P 5 .   ? -11.019 -3.395  22.187  1.00 37.57 ? 562 HOH   A O    1 
HETATM 8186 O  O    . HOH   P 5 .   ? -25.156 -8.468  -11.459 1.00 51.29 ? 563 HOH   A O    1 
HETATM 8187 O  O    . HOH   P 5 .   ? -29.663 -27.023 3.952   1.00 52.97 ? 564 HOH   A O    1 
HETATM 8188 O  O    . HOH   P 5 .   ? -32.729 -32.651 9.842   1.00 39.64 ? 565 HOH   A O    1 
HETATM 8189 O  O    . HOH   P 5 .   ? -50.275 -17.988 14.755  1.00 32.10 ? 566 HOH   A O    1 
HETATM 8190 O  O    . HOH   P 5 .   ? -26.591 -22.389 17.582  1.00 51.82 ? 567 HOH   A O    1 
HETATM 8191 O  O    . HOH   P 5 .   ? -5.476  -13.115 4.669   1.00 42.04 ? 568 HOH   A O    1 
HETATM 8192 O  O    . HOH   P 5 .   ? -18.793 -12.466 18.687  1.00 39.89 ? 569 HOH   A O    1 
HETATM 8193 O  O    . HOH   P 5 .   ? -14.552 -18.984 5.673   1.00 49.23 ? 570 HOH   A O    1 
HETATM 8194 O  O    . HOH   P 5 .   ? -7.998  1.460   -4.034  1.00 51.81 ? 571 HOH   A O    1 
HETATM 8195 O  O    . HOH   P 5 .   ? -19.673 -17.277 10.387  1.00 37.42 ? 572 HOH   A O    1 
HETATM 8196 O  O    . HOH   P 5 .   ? -19.117 -13.213 14.566  1.00 26.31 ? 573 HOH   A O    1 
HETATM 8197 O  O    . HOH   P 5 .   ? -18.792 -10.934 -7.698  1.00 34.98 ? 574 HOH   A O    1 
HETATM 8198 O  O    . HOH   P 5 .   ? -17.244 13.746  0.091   1.00 45.48 ? 575 HOH   A O    1 
HETATM 8199 O  O    A HOH   P 5 .   ? -35.526 -1.496  -4.945  0.60 21.18 ? 576 HOH   A O    1 
HETATM 8200 O  O    B HOH   P 5 .   ? -34.186 -1.089  -5.372  0.40 21.93 ? 576 HOH   A O    1 
HETATM 8201 O  O    . HOH   P 5 .   ? -38.835 -4.332  13.507  1.00 34.68 ? 577 HOH   A O    1 
HETATM 8202 O  O    . HOH   P 5 .   ? -25.923 4.486   -8.098  1.00 45.92 ? 578 HOH   A O    1 
HETATM 8203 O  O    . HOH   P 5 .   ? -48.840 -18.927 11.971  1.00 42.00 ? 579 HOH   A O    1 
HETATM 8204 O  O    . HOH   P 5 .   ? -10.994 -11.637 30.169  1.00 42.17 ? 580 HOH   A O    1 
HETATM 8205 O  O    . HOH   P 5 .   ? -16.675 9.862   17.380  1.00 32.36 ? 581 HOH   A O    1 
HETATM 8206 O  O    . HOH   P 5 .   ? -20.088 -18.469 7.671   1.00 27.80 ? 582 HOH   A O    1 
HETATM 8207 O  O    . HOH   P 5 .   ? -25.127 -19.399 28.304  1.00 45.27 ? 583 HOH   A O    1 
HETATM 8208 O  O    . HOH   P 5 .   ? -30.947 0.163   -6.879  1.00 34.95 ? 584 HOH   A O    1 
HETATM 8209 O  O    . HOH   P 5 .   ? -23.508 -21.666 7.016   1.00 36.72 ? 585 HOH   A O    1 
HETATM 8210 O  O    . HOH   P 5 .   ? -31.256 -4.762  -7.236  1.00 47.13 ? 586 HOH   A O    1 
HETATM 8211 O  O    . HOH   P 5 .   ? -34.656 -10.626 -8.245  1.00 57.55 ? 587 HOH   A O    1 
HETATM 8212 O  O    . HOH   P 5 .   ? -31.154 -18.852 18.974  1.00 45.42 ? 588 HOH   A O    1 
HETATM 8213 O  O    . HOH   P 5 .   ? -38.334 -2.363  16.231  1.00 47.27 ? 589 HOH   A O    1 
HETATM 8214 O  O    . HOH   Q 5 .   ? -37.503 15.578  1.006   1.00 25.66 ? 401 HOH   B O    1 
HETATM 8215 O  O    . HOH   Q 5 .   ? -64.185 15.764  -20.469 1.00 36.69 ? 402 HOH   B O    1 
HETATM 8216 O  O    . HOH   Q 5 .   ? -58.385 9.447   -6.160  1.00 37.48 ? 403 HOH   B O    1 
HETATM 8217 O  O    . HOH   Q 5 .   ? -59.112 1.915   1.653   1.00 21.81 ? 404 HOH   B O    1 
HETATM 8218 O  O    . HOH   Q 5 .   ? -69.524 8.337   -9.862  1.00 35.53 ? 405 HOH   B O    1 
HETATM 8219 O  O    . HOH   Q 5 .   ? -59.685 -13.522 9.569   1.00 18.04 ? 406 HOH   B O    1 
HETATM 8220 O  O    . HOH   Q 5 .   ? -53.764 22.196  9.201   1.00 40.73 ? 407 HOH   B O    1 
HETATM 8221 O  O    . HOH   Q 5 .   ? -47.443 14.043  -10.910 1.00 28.37 ? 408 HOH   B O    1 
HETATM 8222 O  O    . HOH   Q 5 .   ? -48.328 23.631  -3.417  1.00 26.37 ? 409 HOH   B O    1 
HETATM 8223 O  O    . HOH   Q 5 .   ? -58.912 13.244  -3.959  1.00 40.75 ? 410 HOH   B O    1 
HETATM 8224 O  O    . HOH   Q 5 .   ? -48.582 -13.042 4.064   1.00 16.53 ? 411 HOH   B O    1 
HETATM 8225 O  O    . HOH   Q 5 .   ? -45.635 29.525  0.657   1.00 22.16 ? 412 HOH   B O    1 
HETATM 8226 O  O    . HOH   Q 5 .   ? -67.701 3.493   -14.195 1.00 24.01 ? 413 HOH   B O    1 
HETATM 8227 O  O    . HOH   Q 5 .   ? -46.977 14.270  -6.848  1.00 26.79 ? 414 HOH   B O    1 
HETATM 8228 O  O    . HOH   Q 5 .   ? -58.437 -14.321 -22.351 1.00 39.37 ? 415 HOH   B O    1 
HETATM 8229 O  O    . HOH   Q 5 .   ? -51.596 15.222  18.225  1.00 21.20 ? 416 HOH   B O    1 
HETATM 8230 O  O    . HOH   Q 5 .   ? -45.933 5.408   15.900  1.00 40.60 ? 417 HOH   B O    1 
HETATM 8231 O  O    . HOH   Q 5 .   ? -41.223 12.594  -6.906  1.00 26.63 ? 418 HOH   B O    1 
HETATM 8232 O  O    . HOH   Q 5 .   ? -57.088 11.541  -13.380 1.00 39.85 ? 419 HOH   B O    1 
HETATM 8233 O  O    . HOH   Q 5 .   ? -47.550 7.922   14.773  1.00 20.64 ? 420 HOH   B O    1 
HETATM 8234 O  O    . HOH   Q 5 .   ? -58.893 4.682   -25.035 1.00 25.24 ? 421 HOH   B O    1 
HETATM 8235 O  O    . HOH   Q 5 .   ? -55.594 8.984   -3.921  1.00 19.12 ? 422 HOH   B O    1 
HETATM 8236 O  O    . HOH   Q 5 .   ? -72.156 0.937   0.664   1.00 24.36 ? 423 HOH   B O    1 
HETATM 8237 O  O    . HOH   Q 5 .   ? -47.102 29.721  7.004   1.00 34.88 ? 424 HOH   B O    1 
HETATM 8238 O  O    . HOH   Q 5 .   ? -65.484 9.814   -2.504  1.00 31.26 ? 425 HOH   B O    1 
HETATM 8239 O  O    . HOH   Q 5 .   ? -44.903 14.116  18.067  1.00 24.39 ? 426 HOH   B O    1 
HETATM 8240 O  O    . HOH   Q 5 .   ? -72.353 8.296   2.793   1.00 42.27 ? 427 HOH   B O    1 
HETATM 8241 O  O    . HOH   Q 5 .   ? -71.417 0.199   -1.867  1.00 25.45 ? 428 HOH   B O    1 
HETATM 8242 O  O    . HOH   Q 5 .   ? -59.757 0.181   -0.478  1.00 14.97 ? 429 HOH   B O    1 
HETATM 8243 O  O    . HOH   Q 5 .   ? -51.159 26.680  -4.503  1.00 26.24 ? 430 HOH   B O    1 
HETATM 8244 O  O    . HOH   Q 5 .   ? -47.733 8.300   20.651  1.00 26.72 ? 431 HOH   B O    1 
HETATM 8245 O  O    . HOH   Q 5 .   ? -70.911 -4.054  6.085   1.00 27.68 ? 432 HOH   B O    1 
HETATM 8246 O  O    . HOH   Q 5 .   ? -53.988 -17.108 -7.888  1.00 29.43 ? 433 HOH   B O    1 
HETATM 8247 O  O    . HOH   Q 5 .   ? -50.399 31.715  0.986   1.00 22.05 ? 434 HOH   B O    1 
HETATM 8248 O  O    . HOH   Q 5 .   ? -71.285 -8.206  -6.396  1.00 31.58 ? 435 HOH   B O    1 
HETATM 8249 O  O    . HOH   Q 5 .   ? -55.042 29.127  6.021   1.00 35.48 ? 436 HOH   B O    1 
HETATM 8250 O  O    . HOH   Q 5 .   ? -57.820 12.116  16.594  1.00 20.21 ? 437 HOH   B O    1 
HETATM 8251 O  O    . HOH   Q 5 .   ? -69.456 12.100  -10.033 1.00 41.95 ? 438 HOH   B O    1 
HETATM 8252 O  O    . HOH   Q 5 .   ? -40.417 -7.655  -9.497  1.00 35.75 ? 439 HOH   B O    1 
HETATM 8253 O  O    . HOH   Q 5 .   ? -50.034 11.655  8.551   1.00 38.52 ? 440 HOH   B O    1 
HETATM 8254 O  O    . HOH   Q 5 .   ? -69.699 -9.388  -8.606  1.00 38.00 ? 441 HOH   B O    1 
HETATM 8255 O  O    . HOH   Q 5 .   ? -49.713 -18.587 8.672   1.00 32.29 ? 442 HOH   B O    1 
HETATM 8256 O  O    . HOH   Q 5 .   ? -37.434 -6.323  -8.216  1.00 44.07 ? 443 HOH   B O    1 
HETATM 8257 O  O    . HOH   Q 5 .   ? -64.885 -2.501  -14.565 1.00 37.70 ? 444 HOH   B O    1 
HETATM 8258 O  O    . HOH   Q 5 .   ? -47.665 3.342   -18.915 1.00 39.03 ? 445 HOH   B O    1 
HETATM 8259 O  O    . HOH   Q 5 .   ? -49.143 19.216  -1.720  1.00 31.05 ? 446 HOH   B O    1 
HETATM 8260 O  O    . HOH   Q 5 .   ? -51.442 8.226   -23.165 1.00 34.45 ? 447 HOH   B O    1 
HETATM 8261 O  O    . HOH   Q 5 .   ? -60.685 11.770  0.882   1.00 28.42 ? 448 HOH   B O    1 
HETATM 8262 O  O    B HOH   Q 5 .   ? -54.769 7.345   17.471  0.50 19.81 ? 449 HOH   B O    1 
HETATM 8263 O  O    . HOH   Q 5 .   ? -52.319 -4.252  -24.840 1.00 39.83 ? 450 HOH   B O    1 
HETATM 8264 O  O    . HOH   Q 5 .   ? -42.457 6.320   13.938  1.00 32.41 ? 451 HOH   B O    1 
HETATM 8265 O  O    B HOH   Q 5 .   ? -55.755 11.744  -17.363 0.50 26.36 ? 452 HOH   B O    1 
HETATM 8266 O  O    . HOH   Q 5 .   ? -45.607 11.291  3.354   1.00 20.33 ? 453 HOH   B O    1 
HETATM 8267 O  O    . HOH   Q 5 .   ? -61.838 13.166  -4.015  1.00 45.20 ? 454 HOH   B O    1 
HETATM 8268 O  O    . HOH   Q 5 .   ? -54.594 -19.678 6.791   1.00 34.21 ? 455 HOH   B O    1 
HETATM 8269 O  O    . HOH   Q 5 .   ? -37.048 13.429  -0.380  1.00 38.10 ? 456 HOH   B O    1 
HETATM 8270 O  O    . HOH   Q 5 .   ? -44.714 7.426   -12.635 1.00 30.84 ? 457 HOH   B O    1 
HETATM 8271 O  O    . HOH   Q 5 .   ? -39.078 19.461  12.483  1.00 31.96 ? 458 HOH   B O    1 
HETATM 8272 O  O    . HOH   Q 5 .   ? -50.935 11.761  -9.078  1.00 27.74 ? 459 HOH   B O    1 
HETATM 8273 O  O    . HOH   Q 5 .   ? -52.578 -14.411 -10.765 1.00 24.54 ? 460 HOH   B O    1 
HETATM 8274 O  O    . HOH   Q 5 .   ? -44.642 7.684   17.209  1.00 38.74 ? 461 HOH   B O    1 
HETATM 8275 O  O    . HOH   Q 5 .   ? -46.951 -8.531  -5.505  1.00 21.45 ? 462 HOH   B O    1 
HETATM 8276 O  O    . HOH   Q 5 .   ? -58.522 27.785  -1.882  1.00 27.42 ? 463 HOH   B O    1 
HETATM 8277 O  O    . HOH   Q 5 .   ? -44.756 14.820  14.654  1.00 25.38 ? 464 HOH   B O    1 
HETATM 8278 O  O    . HOH   Q 5 .   ? -39.641 1.298   -6.090  1.00 23.62 ? 465 HOH   B O    1 
HETATM 8279 O  O    . HOH   Q 5 .   ? -54.118 1.811   -27.729 1.00 33.04 ? 466 HOH   B O    1 
HETATM 8280 O  O    . HOH   Q 5 .   ? -39.808 8.432   10.362  1.00 17.77 ? 467 HOH   B O    1 
HETATM 8281 O  O    . HOH   Q 5 .   ? -49.929 3.313   10.262  1.00 30.29 ? 468 HOH   B O    1 
HETATM 8282 O  O    . HOH   Q 5 .   ? -44.151 13.673  5.868   1.00 15.41 ? 469 HOH   B O    1 
HETATM 8283 O  O    . HOH   Q 5 .   ? -45.484 27.676  -1.433  1.00 19.26 ? 470 HOH   B O    1 
HETATM 8284 O  O    . HOH   Q 5 .   ? -47.619 -9.453  -9.232  1.00 23.61 ? 471 HOH   B O    1 
HETATM 8285 O  O    . HOH   Q 5 .   ? -47.659 -15.342 -4.633  1.00 23.54 ? 472 HOH   B O    1 
HETATM 8286 O  O    . HOH   Q 5 .   ? -46.071 -12.618 -3.151  1.00 23.62 ? 473 HOH   B O    1 
HETATM 8287 O  O    . HOH   Q 5 .   ? -46.425 -4.709  11.566  1.00 29.64 ? 474 HOH   B O    1 
HETATM 8288 O  O    . HOH   Q 5 .   ? -46.189 -19.656 2.079   1.00 32.69 ? 475 HOH   B O    1 
HETATM 8289 O  O    . HOH   Q 5 .   ? -49.875 -4.716  -20.055 1.00 46.46 ? 476 HOH   B O    1 
HETATM 8290 O  O    . HOH   Q 5 .   ? -58.920 11.543  -21.960 1.00 37.69 ? 477 HOH   B O    1 
HETATM 8291 O  O    . HOH   Q 5 .   ? -42.918 21.422  -1.185  1.00 34.82 ? 478 HOH   B O    1 
HETATM 8292 O  O    . HOH   Q 5 .   ? -70.018 4.920   -12.859 1.00 25.95 ? 479 HOH   B O    1 
HETATM 8293 O  O    A HOH   Q 5 .   ? -50.974 9.074   -17.840 0.40 32.39 ? 480 HOH   B O    1 
HETATM 8294 O  O    B HOH   Q 5 .   ? -49.546 8.084   -17.808 0.40 29.05 ? 480 HOH   B O    1 
HETATM 8295 O  O    . HOH   Q 5 .   ? -40.576 5.637   -1.216  1.00 17.28 ? 481 HOH   B O    1 
HETATM 8296 O  O    . HOH   Q 5 .   ? -75.676 12.710  14.403  1.00 39.22 ? 482 HOH   B O    1 
HETATM 8297 O  O    . HOH   Q 5 .   ? -45.634 5.472   12.528  1.00 32.21 ? 483 HOH   B O    1 
HETATM 8298 O  O    . HOH   Q 5 .   ? -35.851 18.556  19.311  1.00 33.67 ? 484 HOH   B O    1 
HETATM 8299 O  O    . HOH   Q 5 .   ? -55.212 -14.045 -9.932  1.00 21.22 ? 485 HOH   B O    1 
HETATM 8300 O  O    . HOH   Q 5 .   ? -39.906 7.678   6.488   1.00 14.27 ? 486 HOH   B O    1 
HETATM 8301 O  O    . HOH   Q 5 .   ? -66.493 9.257   1.669   1.00 42.75 ? 487 HOH   B O    1 
HETATM 8302 O  O    . HOH   Q 5 .   ? -43.410 -14.751 -1.551  1.00 43.60 ? 488 HOH   B O    1 
HETATM 8303 O  O    . HOH   Q 5 .   ? -38.589 8.067   -4.041  1.00 20.61 ? 489 HOH   B O    1 
HETATM 8304 O  O    . HOH   Q 5 .   ? -44.037 -6.262  -9.537  1.00 28.57 ? 490 HOH   B O    1 
HETATM 8305 O  O    . HOH   Q 5 .   ? -56.749 3.387   2.886   1.00 25.60 ? 491 HOH   B O    1 
HETATM 8306 O  O    . HOH   Q 5 .   ? -43.740 -18.126 -10.491 1.00 51.05 ? 492 HOH   B O    1 
HETATM 8307 O  O    A HOH   Q 5 .   ? -71.571 1.802   9.714   0.50 12.35 ? 493 HOH   B O    1 
HETATM 8308 O  O    B HOH   Q 5 .   ? -73.065 2.462   9.644   0.50 5.63  ? 493 HOH   B O    1 
HETATM 8309 O  O    . HOH   Q 5 .   ? -66.372 0.052   -16.544 1.00 23.20 ? 494 HOH   B O    1 
HETATM 8310 O  O    A HOH   Q 5 .   ? -67.790 -16.286 -0.395  0.50 35.30 ? 495 HOH   B O    1 
HETATM 8311 O  O    A HOH   Q 5 .   ? -56.023 -0.844  -30.242 0.30 20.50 ? 496 HOH   B O    1 
HETATM 8312 O  O    . HOH   Q 5 .   ? -66.801 -8.718  -0.312  1.00 30.55 ? 497 HOH   B O    1 
HETATM 8313 O  O    . HOH   Q 5 .   ? -37.635 -10.174 0.326   1.00 18.30 ? 498 HOH   B O    1 
HETATM 8314 O  O    . HOH   Q 5 .   ? -69.045 -10.599 -14.405 1.00 44.02 ? 499 HOH   B O    1 
HETATM 8315 O  O    . HOH   Q 5 .   ? -68.743 14.424  15.235  1.00 33.26 ? 500 HOH   B O    1 
HETATM 8316 O  O    . HOH   Q 5 .   ? -74.471 3.812   5.242   1.00 43.27 ? 501 HOH   B O    1 
HETATM 8317 O  O    . HOH   Q 5 .   ? -51.831 0.482   -28.331 1.00 56.69 ? 502 HOH   B O    1 
HETATM 8318 O  O    . HOH   Q 5 .   ? -73.682 -7.155  0.187   1.00 28.51 ? 503 HOH   B O    1 
HETATM 8319 O  O    . HOH   Q 5 .   ? -54.276 14.268  -9.205  1.00 33.45 ? 504 HOH   B O    1 
HETATM 8320 O  O    . HOH   Q 5 .   ? -55.415 -6.534  3.732   1.00 16.94 ? 505 HOH   B O    1 
HETATM 8321 O  O    . HOH   Q 5 .   ? -47.955 10.035  -11.531 1.00 28.08 ? 506 HOH   B O    1 
HETATM 8322 O  O    . HOH   Q 5 .   ? -55.981 -13.794 10.665  1.00 20.47 ? 507 HOH   B O    1 
HETATM 8323 O  O    . HOH   Q 5 .   ? -43.966 -2.813  10.297  1.00 23.62 ? 508 HOH   B O    1 
HETATM 8324 O  O    . HOH   Q 5 .   ? -56.051 -13.189 -24.570 1.00 44.42 ? 509 HOH   B O    1 
HETATM 8325 O  O    A HOH   Q 5 .   ? -40.250 9.416   -7.327  0.70 34.81 ? 510 HOH   B O    1 
HETATM 8326 O  O    B HOH   Q 5 .   ? -39.025 11.016  -6.934  0.30 21.93 ? 510 HOH   B O    1 
HETATM 8327 O  O    . HOH   Q 5 .   ? -40.044 -15.655 0.252   1.00 41.62 ? 511 HOH   B O    1 
HETATM 8328 O  O    . HOH   Q 5 .   ? -62.280 11.559  12.014  1.00 15.65 ? 512 HOH   B O    1 
HETATM 8329 O  O    . HOH   Q 5 .   ? -46.803 7.828   -10.845 1.00 21.50 ? 513 HOH   B O    1 
HETATM 8330 O  O    . HOH   Q 5 .   ? -60.734 7.958   -7.065  1.00 22.53 ? 514 HOH   B O    1 
HETATM 8331 O  O    . HOH   Q 5 .   ? -40.620 24.604  3.864   1.00 43.13 ? 515 HOH   B O    1 
HETATM 8332 O  O    . HOH   Q 5 .   ? -56.086 26.877  4.254   1.00 30.46 ? 516 HOH   B O    1 
HETATM 8333 O  O    . HOH   Q 5 .   ? -41.441 1.662   8.583   1.00 20.70 ? 517 HOH   B O    1 
HETATM 8334 O  O    . HOH   Q 5 .   ? -47.371 -6.221  -0.352  1.00 17.46 ? 518 HOH   B O    1 
HETATM 8335 O  O    B HOH   Q 5 .   ? -66.037 -12.790 -2.669  0.50 33.27 ? 519 HOH   B O    1 
HETATM 8336 O  O    . HOH   Q 5 .   ? -62.767 12.690  2.658   1.00 27.01 ? 520 HOH   B O    1 
HETATM 8337 O  O    . HOH   Q 5 .   ? -57.418 0.404   -25.863 1.00 31.38 ? 521 HOH   B O    1 
HETATM 8338 O  O    . HOH   Q 5 .   ? -63.446 13.758  -11.939 1.00 27.71 ? 522 HOH   B O    1 
HETATM 8339 O  O    . HOH   Q 5 .   ? -39.818 19.400  17.600  1.00 30.77 ? 523 HOH   B O    1 
HETATM 8340 O  O    . HOH   Q 5 .   ? -57.213 18.554  -3.779  1.00 42.85 ? 524 HOH   B O    1 
HETATM 8341 O  O    . HOH   Q 5 .   ? -63.886 0.052   -17.848 1.00 24.51 ? 525 HOH   B O    1 
HETATM 8342 O  O    . HOH   Q 5 .   ? -50.376 11.026  -11.605 1.00 37.86 ? 526 HOH   B O    1 
HETATM 8343 O  O    . HOH   Q 5 .   ? -41.262 9.328   -10.207 1.00 41.52 ? 527 HOH   B O    1 
HETATM 8344 O  O    . HOH   Q 5 .   ? -43.016 -3.868  -8.756  1.00 24.59 ? 528 HOH   B O    1 
HETATM 8345 O  O    . HOH   Q 5 .   ? -71.691 1.829   -5.173  1.00 26.97 ? 529 HOH   B O    1 
HETATM 8346 O  O    . HOH   Q 5 .   ? -35.629 19.201  21.628  1.00 50.93 ? 530 HOH   B O    1 
HETATM 8347 O  O    . HOH   Q 5 .   ? -58.340 27.159  2.140   1.00 36.98 ? 531 HOH   B O    1 
HETATM 8348 O  O    A HOH   Q 5 .   ? -77.205 -0.810  5.187   0.50 26.39 ? 532 HOH   B O    1 
HETATM 8349 O  O    B HOH   Q 5 .   ? -76.869 -0.330  6.759   0.50 32.96 ? 532 HOH   B O    1 
HETATM 8350 O  O    . HOH   Q 5 .   ? -73.638 -3.450  -4.183  1.00 39.18 ? 533 HOH   B O    1 
HETATM 8351 O  O    . HOH   Q 5 .   ? -54.898 -6.626  -21.501 1.00 38.37 ? 534 HOH   B O    1 
HETATM 8352 O  O    . HOH   Q 5 .   ? -50.938 14.139  12.795  1.00 33.97 ? 535 HOH   B O    1 
HETATM 8353 O  O    . HOH   Q 5 .   ? -40.911 -0.759  -11.521 1.00 35.45 ? 536 HOH   B O    1 
HETATM 8354 O  O    . HOH   Q 5 .   ? -52.398 3.361   9.773   1.00 29.68 ? 537 HOH   B O    1 
HETATM 8355 O  O    . HOH   Q 5 .   ? -44.392 1.609   10.521  1.00 38.79 ? 538 HOH   B O    1 
HETATM 8356 O  O    . HOH   Q 5 .   ? -37.869 6.762   -8.226  1.00 45.75 ? 539 HOH   B O    1 
HETATM 8357 O  O    . HOH   Q 5 .   ? -45.507 9.352   -14.929 1.00 50.53 ? 540 HOH   B O    1 
HETATM 8358 O  O    . HOH   Q 5 .   ? -66.332 13.950  -12.555 1.00 37.79 ? 541 HOH   B O    1 
HETATM 8359 O  O    . HOH   Q 5 .   ? -56.299 -16.450 -10.542 1.00 39.78 ? 542 HOH   B O    1 
HETATM 8360 O  O    A HOH   Q 5 .   ? -50.268 22.080  13.516  0.60 35.69 ? 543 HOH   B O    1 
HETATM 8361 O  O    B HOH   Q 5 .   ? -50.587 22.974  11.798  0.40 32.86 ? 543 HOH   B O    1 
HETATM 8362 O  O    . HOH   Q 5 .   ? -67.306 -2.293  -13.443 1.00 34.91 ? 544 HOH   B O    1 
HETATM 8363 O  O    . HOH   Q 5 .   ? -61.456 14.928  -20.039 1.00 40.48 ? 545 HOH   B O    1 
HETATM 8364 O  O    . HOH   Q 5 .   ? -71.210 14.831  15.226  1.00 51.01 ? 546 HOH   B O    1 
HETATM 8365 O  O    A HOH   Q 5 .   ? -73.111 3.320   10.845  0.50 36.68 ? 547 HOH   B O    1 
HETATM 8366 O  O    . HOH   Q 5 .   ? -63.277 15.240  2.889   1.00 48.00 ? 548 HOH   B O    1 
HETATM 8367 O  O    . HOH   Q 5 .   ? -60.512 17.465  5.964   1.00 50.56 ? 549 HOH   B O    1 
HETATM 8368 O  O    . HOH   Q 5 .   ? -79.515 -6.776  4.444   1.00 46.89 ? 550 HOH   B O    1 
HETATM 8369 O  O    . HOH   Q 5 .   ? -58.145 15.515  0.554   1.00 53.79 ? 551 HOH   B O    1 
HETATM 8370 O  O    . HOH   Q 5 .   ? -54.519 11.769  11.568  1.00 20.59 ? 552 HOH   B O    1 
HETATM 8371 O  O    . HOH   Q 5 .   ? -47.756 6.372   -18.631 1.00 50.61 ? 553 HOH   B O    1 
HETATM 8372 O  O    . HOH   Q 5 .   ? -52.993 -15.873 -13.285 1.00 36.16 ? 554 HOH   B O    1 
HETATM 8373 O  O    A HOH   Q 5 .   ? -71.019 -0.892  -6.848  0.60 28.00 ? 555 HOH   B O    1 
HETATM 8374 O  O    B HOH   Q 5 .   ? -71.539 0.457   -8.220  0.40 25.54 ? 555 HOH   B O    1 
HETATM 8375 O  O    . HOH   Q 5 .   ? -47.655 31.364  1.716   1.00 20.71 ? 556 HOH   B O    1 
HETATM 8376 O  O    . HOH   Q 5 .   ? -68.143 -10.842 -0.700  1.00 45.81 ? 557 HOH   B O    1 
HETATM 8377 O  O    . HOH   Q 5 .   ? -43.061 -5.429  -18.554 1.00 52.57 ? 558 HOH   B O    1 
HETATM 8378 O  O    . HOH   Q 5 .   ? -65.199 11.957  -0.994  1.00 33.53 ? 559 HOH   B O    1 
HETATM 8379 O  O    . HOH   Q 5 .   ? -65.283 11.580  1.901   1.00 43.89 ? 560 HOH   B O    1 
HETATM 8380 O  O    . HOH   Q 5 .   ? -57.956 16.796  -1.641  1.00 46.95 ? 561 HOH   B O    1 
HETATM 8381 O  O    . HOH   Q 5 .   ? -49.272 13.893  -8.468  1.00 40.04 ? 562 HOH   B O    1 
HETATM 8382 O  O    . HOH   Q 5 .   ? -37.525 17.730  16.865  1.00 25.09 ? 563 HOH   B O    1 
HETATM 8383 O  O    A HOH   Q 5 .   ? -38.225 -1.284  -5.826  0.60 22.60 ? 564 HOH   B O    1 
HETATM 8384 O  O    B HOH   Q 5 .   ? -37.989 -3.220  -6.317  0.40 26.02 ? 564 HOH   B O    1 
HETATM 8385 O  O    . HOH   Q 5 .   ? -73.502 1.504   -3.337  1.00 37.19 ? 565 HOH   B O    1 
HETATM 8386 O  O    . HOH   Q 5 .   ? -57.753 27.003  -4.531  1.00 35.38 ? 566 HOH   B O    1 
HETATM 8387 O  O    . HOH   Q 5 .   ? -53.842 17.903  7.776   1.00 53.30 ? 567 HOH   B O    1 
HETATM 8388 O  O    . HOH   Q 5 .   ? -45.525 2.769   -20.095 1.00 46.60 ? 568 HOH   B O    1 
HETATM 8389 O  O    . HOH   Q 5 .   ? -49.156 13.735  -13.065 1.00 39.61 ? 569 HOH   B O    1 
HETATM 8390 O  O    . HOH   Q 5 .   ? -44.280 -7.496  -13.569 1.00 49.86 ? 570 HOH   B O    1 
HETATM 8391 O  O    . HOH   Q 5 .   ? -51.997 -16.638 -9.276  1.00 42.72 ? 571 HOH   B O    1 
HETATM 8392 O  O    . HOH   Q 5 .   ? -46.498 3.633   10.589  1.00 34.90 ? 572 HOH   B O    1 
HETATM 8393 O  O    . HOH   Q 5 .   ? -62.449 12.143  -1.371  1.00 32.71 ? 573 HOH   B O    1 
HETATM 8394 O  O    . HOH   Q 5 .   ? -37.064 18.471  13.849  1.00 43.46 ? 574 HOH   B O    1 
HETATM 8395 O  O    . HOH   Q 5 .   ? -67.094 -10.465 1.549   1.00 41.29 ? 575 HOH   B O    1 
HETATM 8396 O  O    . HOH   Q 5 .   ? -44.133 4.753   14.138  1.00 38.22 ? 576 HOH   B O    1 
HETATM 8397 O  O    . HOH   Q 5 .   ? -43.215 9.875   -12.872 1.00 43.50 ? 577 HOH   B O    1 
HETATM 8398 O  O    . HOH   Q 5 .   ? -40.667 -3.287  -9.909  1.00 34.38 ? 578 HOH   B O    1 
HETATM 8399 O  O    . HOH   Q 5 .   ? -65.838 16.340  4.323   1.00 45.21 ? 579 HOH   B O    1 
HETATM 8400 O  O    . HOH   Q 5 .   ? -62.299 20.021  14.220  1.00 46.01 ? 580 HOH   B O    1 
HETATM 8401 O  O    . HOH   Q 5 .   ? -59.265 20.278  11.503  1.00 44.50 ? 581 HOH   B O    1 
HETATM 8402 O  O    . HOH   Q 5 .   ? -50.597 9.504   -27.781 1.00 58.77 ? 582 HOH   B O    1 
HETATM 8403 O  O    . HOH   Q 5 .   ? -46.991 0.304   12.124  1.00 54.50 ? 583 HOH   B O    1 
HETATM 8404 O  O    . HOH   R 5 .   ? -47.492 7.593   50.750  1.00 47.49 ? 401 HOH   C O    1 
HETATM 8405 O  O    . HOH   R 5 .   ? -35.849 22.949  25.471  0.70 34.11 ? 402 HOH   C O    1 
HETATM 8406 O  O    . HOH   R 5 .   ? -35.688 -14.060 46.703  1.00 45.89 ? 403 HOH   C O    1 
HETATM 8407 O  O    . HOH   R 5 .   ? -25.238 -8.771  45.681  0.70 34.49 ? 404 HOH   C O    1 
HETATM 8408 O  O    . HOH   R 5 .   ? -31.522 11.855  42.816  1.00 28.31 ? 405 HOH   C O    1 
HETATM 8409 O  O    . HOH   R 5 .   ? -30.865 -16.869 33.648  1.00 33.75 ? 406 HOH   C O    1 
HETATM 8410 O  O    . HOH   R 5 .   ? -36.588 22.111  37.810  1.00 49.91 ? 407 HOH   C O    1 
HETATM 8411 O  O    . HOH   R 5 .   ? -18.198 4.284   46.527  1.00 37.24 ? 408 HOH   C O    1 
HETATM 8412 O  O    . HOH   R 5 .   ? -30.748 3.720   35.822  1.00 19.22 ? 409 HOH   C O    1 
HETATM 8413 O  O    . HOH   R 5 .   ? -33.587 -2.665  59.669  1.00 29.15 ? 410 HOH   C O    1 
HETATM 8414 O  O    A HOH   R 5 .   ? -35.254 6.756   64.688  0.50 27.45 ? 411 HOH   C O    1 
HETATM 8415 O  O    B HOH   R 5 .   ? -33.862 6.147   64.798  0.50 31.40 ? 411 HOH   C O    1 
HETATM 8416 O  O    . HOH   R 5 .   ? -30.316 -12.471 29.540  1.00 17.32 ? 412 HOH   C O    1 
HETATM 8417 O  O    . HOH   R 5 .   ? -50.488 11.743  43.974  1.00 49.76 ? 413 HOH   C O    1 
HETATM 8418 O  O    . HOH   R 5 .   ? -18.881 2.501   44.743  1.00 42.35 ? 414 HOH   C O    1 
HETATM 8419 O  O    . HOH   R 5 .   ? -38.236 15.236  17.805  1.00 18.68 ? 415 HOH   C O    1 
HETATM 8420 O  O    . HOH   R 5 .   ? -17.708 2.656   36.698  1.00 23.84 ? 416 HOH   C O    1 
HETATM 8421 O  O    . HOH   R 5 .   ? -24.333 12.071  39.230  1.00 24.98 ? 417 HOH   C O    1 
HETATM 8422 O  O    . HOH   R 5 .   ? -29.003 13.527  35.454  1.00 22.91 ? 418 HOH   C O    1 
HETATM 8423 O  O    . HOH   R 5 .   ? -32.893 9.853   61.753  1.00 32.80 ? 419 HOH   C O    1 
HETATM 8424 O  O    . HOH   R 5 .   ? -36.933 0.164   21.366  1.00 35.14 ? 420 HOH   C O    1 
HETATM 8425 O  O    . HOH   R 5 .   ? -41.397 -11.425 35.023  1.00 15.71 ? 421 HOH   C O    1 
HETATM 8426 O  O    . HOH   R 5 .   ? -50.690 13.282  48.305  1.00 28.05 ? 422 HOH   C O    1 
HETATM 8427 O  O    . HOH   R 5 .   ? -32.887 14.502  49.830  1.00 31.45 ? 423 HOH   C O    1 
HETATM 8428 O  O    . HOH   R 5 .   ? -47.410 -8.147  43.279  1.00 33.89 ? 424 HOH   C O    1 
HETATM 8429 O  O    B HOH   R 5 .   ? -25.868 -13.654 37.847  0.50 22.71 ? 425 HOH   C O    1 
HETATM 8430 O  O    . HOH   R 5 .   ? -44.359 -12.403 41.980  1.00 40.03 ? 426 HOH   C O    1 
HETATM 8431 O  O    . HOH   R 5 .   ? -43.983 5.649   21.250  1.00 37.98 ? 427 HOH   C O    1 
HETATM 8432 O  O    . HOH   R 5 .   ? -42.282 8.367   22.093  1.00 19.65 ? 428 HOH   C O    1 
HETATM 8433 O  O    . HOH   R 5 .   ? -32.973 -12.812 52.324  1.00 45.87 ? 429 HOH   C O    1 
HETATM 8434 O  O    . HOH   R 5 .   ? -38.216 0.629   63.144  1.00 42.73 ? 430 HOH   C O    1 
HETATM 8435 O  O    . HOH   R 5 .   ? -18.530 2.163   39.307  1.00 21.62 ? 431 HOH   C O    1 
HETATM 8436 O  O    . HOH   R 5 .   ? -40.448 25.568  38.111  1.00 42.64 ? 432 HOH   C O    1 
HETATM 8437 O  O    . HOH   R 5 .   ? -34.169 11.348  40.627  1.00 16.42 ? 433 HOH   C O    1 
HETATM 8438 O  O    . HOH   R 5 .   ? -18.065 9.679   34.400  1.00 38.72 ? 434 HOH   C O    1 
HETATM 8439 O  O    . HOH   R 5 .   ? -42.360 30.945  27.733  1.00 49.27 ? 435 HOH   C O    1 
HETATM 8440 O  O    . HOH   R 5 .   ? -30.121 2.221   38.076  1.00 17.17 ? 436 HOH   C O    1 
HETATM 8441 O  O    . HOH   R 5 .   ? -46.468 16.536  45.022  1.00 41.61 ? 437 HOH   C O    1 
HETATM 8442 O  O    . HOH   R 5 .   ? -44.883 28.159  24.542  1.00 54.20 ? 438 HOH   C O    1 
HETATM 8443 O  O    . HOH   R 5 .   ? -42.557 31.992  30.626  1.00 44.93 ? 439 HOH   C O    1 
HETATM 8444 O  O    . HOH   R 5 .   ? -54.117 18.400  15.422  1.00 40.52 ? 440 HOH   C O    1 
HETATM 8445 O  O    . HOH   R 5 .   ? -48.599 -0.512  52.717  1.00 48.84 ? 441 HOH   C O    1 
HETATM 8446 O  O    . HOH   R 5 .   ? -30.515 15.531  39.830  1.00 26.26 ? 442 HOH   C O    1 
HETATM 8447 O  O    . HOH   R 5 .   ? -33.315 28.180  29.694  1.00 38.18 ? 443 HOH   C O    1 
HETATM 8448 O  O    . HOH   R 5 .   ? -45.232 25.383  23.882  1.00 38.26 ? 444 HOH   C O    1 
HETATM 8449 O  O    . HOH   R 5 .   ? -35.304 -18.202 33.019  1.00 33.99 ? 445 HOH   C O    1 
HETATM 8450 O  O    . HOH   R 5 .   ? -43.754 -17.759 37.537  1.00 31.50 ? 446 HOH   C O    1 
HETATM 8451 O  O    . HOH   R 5 .   ? -32.012 12.251  19.823  1.00 17.97 ? 447 HOH   C O    1 
HETATM 8452 O  O    . HOH   R 5 .   ? -26.979 -5.114  59.564  1.00 22.08 ? 448 HOH   C O    1 
HETATM 8453 O  O    . HOH   R 5 .   ? -50.544 20.250  23.038  1.00 28.54 ? 449 HOH   C O    1 
HETATM 8454 O  O    . HOH   R 5 .   ? -38.971 12.634  59.501  1.00 39.16 ? 450 HOH   C O    1 
HETATM 8455 O  O    A HOH   R 5 .   ? -48.886 17.607  37.584  0.50 22.54 ? 451 HOH   C O    1 
HETATM 8456 O  O    . HOH   R 5 .   ? -41.578 -9.727  48.991  1.00 39.59 ? 452 HOH   C O    1 
HETATM 8457 O  O    . HOH   R 5 .   ? -45.091 15.077  21.309  1.00 22.70 ? 453 HOH   C O    1 
HETATM 8458 O  O    . HOH   R 5 .   ? -30.762 -2.266  59.481  1.00 24.81 ? 454 HOH   C O    1 
HETATM 8459 O  O    . HOH   R 5 .   ? -22.854 2.885   52.053  1.00 22.21 ? 455 HOH   C O    1 
HETATM 8460 O  O    . HOH   R 5 .   ? -50.256 3.937   43.355  1.00 28.85 ? 456 HOH   C O    1 
HETATM 8461 O  O    . HOH   R 5 .   ? -25.981 -10.713 43.946  1.00 36.60 ? 457 HOH   C O    1 
HETATM 8462 O  O    . HOH   R 5 .   ? -42.229 7.944   16.231  1.00 27.48 ? 458 HOH   C O    1 
HETATM 8463 O  O    . HOH   R 5 .   ? -55.112 21.409  27.614  1.00 39.96 ? 459 HOH   C O    1 
HETATM 8464 O  O    . HOH   R 5 .   ? -42.192 7.523   55.833  1.00 30.73 ? 460 HOH   C O    1 
HETATM 8465 O  O    . HOH   R 5 .   ? -39.861 14.305  52.082  1.00 41.03 ? 461 HOH   C O    1 
HETATM 8466 O  O    . HOH   R 5 .   ? -33.076 15.099  57.587  1.00 38.29 ? 462 HOH   C O    1 
HETATM 8467 O  O    . HOH   R 5 .   ? -39.788 4.244   27.069  1.00 28.04 ? 463 HOH   C O    1 
HETATM 8468 O  O    . HOH   R 5 .   ? -50.108 9.404   26.403  1.00 20.42 ? 464 HOH   C O    1 
HETATM 8469 O  O    . HOH   R 5 .   ? -45.688 15.043  30.273  1.00 18.38 ? 465 HOH   C O    1 
HETATM 8470 O  O    . HOH   R 5 .   ? -11.902 9.937   27.992  1.00 46.21 ? 466 HOH   C O    1 
HETATM 8471 O  O    . HOH   R 5 .   ? -52.319 17.545  34.970  1.00 31.47 ? 467 HOH   C O    1 
HETATM 8472 O  O    . HOH   R 5 .   ? -45.743 -3.237  47.691  1.00 28.76 ? 468 HOH   C O    1 
HETATM 8473 O  O    . HOH   R 5 .   ? -28.107 -13.777 49.472  1.00 42.36 ? 469 HOH   C O    1 
HETATM 8474 O  O    A HOH   R 5 .   ? -35.022 7.395   19.454  0.70 20.25 ? 470 HOH   C O    1 
HETATM 8475 O  O    . HOH   R 5 .   ? -38.765 14.779  45.289  1.00 24.56 ? 471 HOH   C O    1 
HETATM 8476 O  O    . HOH   R 5 .   ? -41.848 13.056  47.888  1.00 38.37 ? 472 HOH   C O    1 
HETATM 8477 O  O    . HOH   R 5 .   ? -40.262 -17.433 30.778  1.00 33.62 ? 473 HOH   C O    1 
HETATM 8478 O  O    . HOH   R 5 .   ? -30.739 7.976   60.564  1.00 36.17 ? 474 HOH   C O    1 
HETATM 8479 O  O    . HOH   R 5 .   ? -47.536 7.031   23.019  1.00 33.91 ? 475 HOH   C O    1 
HETATM 8480 O  O    . HOH   R 5 .   ? -42.228 -6.451  47.943  1.00 25.47 ? 476 HOH   C O    1 
HETATM 8481 O  O    . HOH   R 5 .   ? -44.216 12.938  33.144  1.00 21.70 ? 477 HOH   C O    1 
HETATM 8482 O  O    . HOH   R 5 .   ? -42.843 -5.813  44.056  1.00 21.13 ? 478 HOH   C O    1 
HETATM 8483 O  O    . HOH   R 5 .   ? -43.853 -10.002 42.241  1.00 18.53 ? 479 HOH   C O    1 
HETATM 8484 O  O    . HOH   R 5 .   ? -40.157 -0.597  57.520  1.00 34.38 ? 480 HOH   C O    1 
HETATM 8485 O  O    . HOH   R 5 .   ? -18.438 11.350  42.917  1.00 46.98 ? 481 HOH   C O    1 
HETATM 8486 O  O    . HOH   R 5 .   ? -37.147 -11.298 49.907  1.00 24.89 ? 482 HOH   C O    1 
HETATM 8487 O  O    . HOH   R 5 .   ? -17.393 9.517   40.494  1.00 44.61 ? 483 HOH   C O    1 
HETATM 8488 O  O    . HOH   R 5 .   ? -53.385 -5.689  37.579  1.00 19.80 ? 484 HOH   C O    1 
HETATM 8489 O  O    . HOH   R 5 .   ? -19.928 11.527  46.391  1.00 38.94 ? 485 HOH   C O    1 
HETATM 8490 O  O    . HOH   R 5 .   ? -49.955 9.077   30.316  1.00 14.74 ? 486 HOH   C O    1 
HETATM 8491 O  O    . HOH   R 5 .   ? -34.371 -7.333  59.392  1.00 44.34 ? 487 HOH   C O    1 
HETATM 8492 O  O    . HOH   R 5 .   ? -46.460 -12.342 40.633  1.00 41.09 ? 488 HOH   C O    1 
HETATM 8493 O  O    . HOH   R 5 .   ? -18.990 -2.801  31.989  1.00 26.81 ? 489 HOH   C O    1 
HETATM 8494 O  O    . HOH   R 5 .   ? -49.372 -4.675  47.983  1.00 36.71 ? 490 HOH   C O    1 
HETATM 8495 O  O    . HOH   R 5 .   ? -33.984 -12.898 28.479  1.00 20.19 ? 491 HOH   C O    1 
HETATM 8496 O  O    . HOH   R 5 .   ? -43.604 -3.991  26.572  1.00 29.65 ? 492 HOH   C O    1 
HETATM 8497 O  O    . HOH   R 5 .   ? -22.432 0.611   50.710  1.00 32.10 ? 493 HOH   C O    1 
HETATM 8498 O  O    . HOH   R 5 .   ? -40.289 21.260  36.895  1.00 29.75 ? 494 HOH   C O    1 
HETATM 8499 O  O    . HOH   R 5 .   ? -44.105 6.054   24.543  1.00 32.50 ? 495 HOH   C O    1 
HETATM 8500 O  O    . HOH   R 5 .   ? -30.756 2.395   59.013  1.00 19.93 ? 496 HOH   C O    1 
HETATM 8501 O  O    . HOH   R 5 .   ? -12.872 0.662   32.126  1.00 37.10 ? 497 HOH   C O    1 
HETATM 8502 O  O    . HOH   R 5 .   ? -51.390 10.548  40.600  1.00 22.33 ? 498 HOH   C O    1 
HETATM 8503 O  O    . HOH   R 5 .   ? -49.295 7.794   38.244  1.00 18.78 ? 499 HOH   C O    1 
HETATM 8504 O  O    . HOH   R 5 .   ? -14.087 13.346  29.305  1.00 31.06 ? 500 HOH   C O    1 
HETATM 8505 O  O    . HOH   R 5 .   ? -32.855 19.384  21.654  1.00 39.59 ? 501 HOH   C O    1 
HETATM 8506 O  O    . HOH   R 5 .   ? -39.011 3.607   65.064  1.00 36.38 ? 502 HOH   C O    1 
HETATM 8507 O  O    . HOH   R 5 .   ? -45.153 7.770   19.737  1.00 35.01 ? 503 HOH   C O    1 
HETATM 8508 O  O    . HOH   R 5 .   ? -32.991 4.950   34.292  1.00 26.18 ? 504 HOH   C O    1 
HETATM 8509 O  O    . HOH   R 5 .   ? -27.566 12.177  24.437  1.00 15.39 ? 505 HOH   C O    1 
HETATM 8510 O  O    . HOH   R 5 .   ? -24.855 15.345  40.742  1.00 46.67 ? 506 HOH   C O    1 
HETATM 8511 O  O    . HOH   R 5 .   ? -19.973 3.341   48.667  1.00 27.38 ? 507 HOH   C O    1 
HETATM 8512 O  O    . HOH   R 5 .   ? -27.175 14.376  33.640  1.00 25.75 ? 508 HOH   C O    1 
HETATM 8513 O  O    . HOH   R 5 .   ? -43.231 10.897  47.330  1.00 31.66 ? 509 HOH   C O    1 
HETATM 8514 O  O    . HOH   R 5 .   ? -38.712 14.540  23.155  1.00 27.60 ? 510 HOH   C O    1 
HETATM 8515 O  O    . HOH   R 5 .   ? -48.732 25.981  30.738  1.00 46.32 ? 511 HOH   C O    1 
HETATM 8516 O  O    . HOH   R 5 .   ? -42.559 17.231  42.537  1.00 25.67 ? 512 HOH   C O    1 
HETATM 8517 O  O    . HOH   R 5 .   ? -17.927 8.357   42.602  1.00 35.34 ? 513 HOH   C O    1 
HETATM 8518 O  O    . HOH   R 5 .   ? -18.184 4.425   42.514  1.00 32.68 ? 514 HOH   C O    1 
HETATM 8519 O  O    . HOH   R 5 .   ? -52.395 -8.038  38.438  1.00 17.87 ? 515 HOH   C O    1 
HETATM 8520 O  O    . HOH   R 5 .   ? -29.068 10.617  43.960  1.00 20.79 ? 516 HOH   C O    1 
HETATM 8521 O  O    . HOH   R 5 .   ? -45.261 10.625  48.990  1.00 38.25 ? 517 HOH   C O    1 
HETATM 8522 O  O    . HOH   R 5 .   ? -42.330 -12.654 43.900  1.00 25.26 ? 518 HOH   C O    1 
HETATM 8523 O  O    . HOH   R 5 .   ? -51.352 24.904  33.833  1.00 45.70 ? 519 HOH   C O    1 
HETATM 8524 O  O    . HOH   R 5 .   ? -35.413 17.236  45.084  1.00 32.97 ? 520 HOH   C O    1 
HETATM 8525 O  O    . HOH   R 5 .   ? -34.566 -4.943  34.646  1.00 16.77 ? 521 HOH   C O    1 
HETATM 8526 O  O    . HOH   R 5 .   ? -48.493 2.818   28.907  1.00 22.75 ? 522 HOH   C O    1 
HETATM 8527 O  O    . HOH   R 5 .   ? -34.523 -11.062 49.199  1.00 24.32 ? 523 HOH   C O    1 
HETATM 8528 O  O    . HOH   R 5 .   ? -42.467 -4.152  38.640  1.00 16.43 ? 524 HOH   C O    1 
HETATM 8529 O  O    . HOH   R 5 .   ? -13.958 12.931  21.923  1.00 30.35 ? 525 HOH   C O    1 
HETATM 8530 O  O    . HOH   R 5 .   ? -16.175 -1.076  41.956  1.00 34.39 ? 526 HOH   C O    1 
HETATM 8531 O  O    . HOH   R 5 .   ? -46.817 -0.796  46.664  1.00 27.38 ? 527 HOH   C O    1 
HETATM 8532 O  O    A HOH   R 5 .   ? -23.255 -6.963  38.738  0.60 19.76 ? 528 HOH   C O    1 
HETATM 8533 O  O    B HOH   R 5 .   ? -22.448 -8.765  39.060  0.40 28.37 ? 528 HOH   C O    1 
HETATM 8534 O  O    . HOH   R 5 .   ? -45.956 -1.857  27.666  1.00 26.51 ? 529 HOH   C O    1 
HETATM 8535 O  O    . HOH   R 5 .   ? -26.411 16.825  48.116  1.00 24.43 ? 530 HOH   C O    1 
HETATM 8536 O  O    . HOH   R 5 .   ? -37.779 28.851  39.675  1.00 54.42 ? 531 HOH   C O    1 
HETATM 8537 O  O    . HOH   R 5 .   ? -37.294 4.168   27.831  1.00 29.64 ? 532 HOH   C O    1 
HETATM 8538 O  O    . HOH   R 5 .   ? -23.275 11.041  34.746  1.00 38.22 ? 533 HOH   C O    1 
HETATM 8539 O  O    . HOH   R 5 .   ? -50.042 19.482  17.824  1.00 35.34 ? 534 HOH   C O    1 
HETATM 8540 O  O    . HOH   R 5 .   ? -20.044 17.345  26.413  1.00 56.43 ? 535 HOH   C O    1 
HETATM 8541 O  O    . HOH   R 5 .   ? -55.681 -11.335 43.070  1.00 44.68 ? 536 HOH   C O    1 
HETATM 8542 O  O    . HOH   R 5 .   ? -23.362 16.863  48.847  1.00 32.43 ? 537 HOH   C O    1 
HETATM 8543 O  O    . HOH   R 5 .   ? -35.061 19.937  40.907  1.00 35.10 ? 538 HOH   C O    1 
HETATM 8544 O  O    . HOH   R 5 .   ? -52.143 13.261  41.461  1.00 33.05 ? 539 HOH   C O    1 
HETATM 8545 O  O    . HOH   R 5 .   ? -39.276 13.850  47.711  1.00 39.12 ? 540 HOH   C O    1 
HETATM 8546 O  O    . HOH   R 5 .   ? -46.920 27.635  32.152  1.00 54.46 ? 541 HOH   C O    1 
HETATM 8547 O  O    . HOH   R 5 .   ? -39.501 22.436  21.871  1.00 50.27 ? 542 HOH   C O    1 
HETATM 8548 O  O    B HOH   R 5 .   ? -41.861 32.021  33.863  0.50 29.06 ? 543 HOH   C O    1 
HETATM 8549 O  O    . HOH   R 5 .   ? -41.865 8.732   64.270  1.00 51.12 ? 544 HOH   C O    1 
HETATM 8550 O  O    A HOH   R 5 .   ? -15.304 5.323   31.766  0.50 29.88 ? 545 HOH   C O    1 
HETATM 8551 O  O    . HOH   R 5 .   ? -45.489 2.711   27.027  1.00 36.81 ? 546 HOH   C O    1 
HETATM 8552 O  O    A HOH   R 5 .   ? -21.543 16.446  23.831  0.40 28.50 ? 547 HOH   C O    1 
HETATM 8553 O  O    . HOH   R 5 .   ? -51.779 -0.174  44.951  1.00 47.58 ? 548 HOH   C O    1 
HETATM 8554 O  O    . HOH   R 5 .   ? -42.345 10.429  55.307  1.00 46.85 ? 549 HOH   C O    1 
HETATM 8555 O  O    . HOH   R 5 .   ? -53.918 19.401  13.126  1.00 46.18 ? 550 HOH   C O    1 
HETATM 8556 O  O    . HOH   R 5 .   ? -45.415 0.514   26.388  1.00 41.50 ? 551 HOH   C O    1 
HETATM 8557 O  O    . HOH   R 5 .   ? -35.266 12.384  24.884  1.00 17.19 ? 552 HOH   C O    1 
HETATM 8558 O  O    . HOH   R 5 .   ? -16.002 4.654   36.961  1.00 45.17 ? 553 HOH   C O    1 
HETATM 8559 O  O    . HOH   R 5 .   ? -29.748 18.584  29.239  1.00 46.12 ? 554 HOH   C O    1 
HETATM 8560 O  O    . HOH   R 5 .   ? -31.444 17.493  36.155  1.00 36.41 ? 555 HOH   C O    1 
HETATM 8561 O  O    . HOH   R 5 .   ? -22.801 13.870  53.547  1.00 43.75 ? 556 HOH   C O    1 
HETATM 8562 O  O    . HOH   R 5 .   ? -24.616 13.962  37.244  1.00 28.73 ? 557 HOH   C O    1 
HETATM 8563 O  O    . HOH   R 5 .   ? -52.108 17.861  18.682  1.00 29.35 ? 558 HOH   C O    1 
HETATM 8564 O  O    . HOH   R 5 .   ? -45.391 -3.722  52.026  1.00 56.34 ? 559 HOH   C O    1 
HETATM 8565 O  O    . HOH   R 5 .   ? -36.777 -15.977 45.296  1.00 45.79 ? 560 HOH   C O    1 
HETATM 8566 O  O    . HOH   R 5 .   ? -28.083 19.152  49.306  1.00 49.50 ? 561 HOH   C O    1 
HETATM 8567 O  O    . HOH   R 5 .   ? -56.548 18.640  33.891  1.00 50.13 ? 562 HOH   C O    1 
HETATM 8568 O  O    . HOH   R 5 .   ? -46.735 1.095   56.719  1.00 57.75 ? 563 HOH   C O    1 
HETATM 8569 O  O    . HOH   R 5 .   ? -28.226 16.048  39.293  1.00 56.70 ? 564 HOH   C O    1 
HETATM 8570 O  O    B HOH   R 5 .   ? -28.894 15.833  57.449  0.50 38.31 ? 565 HOH   C O    1 
HETATM 8571 O  O    . HOH   R 5 .   ? -33.391 -13.303 49.904  1.00 39.87 ? 566 HOH   C O    1 
HETATM 8572 O  O    . HOH   R 5 .   ? -51.562 1.576   43.576  1.00 30.39 ? 567 HOH   C O    1 
HETATM 8573 O  O    . HOH   R 5 .   ? -16.376 3.472   40.707  1.00 33.80 ? 568 HOH   C O    1 
HETATM 8574 O  O    . HOH   R 5 .   ? -23.993 17.420  31.905  1.00 49.58 ? 569 HOH   C O    1 
HETATM 8575 O  O    . HOH   R 5 .   ? -27.387 14.081  37.592  1.00 30.47 ? 570 HOH   C O    1 
HETATM 8576 O  O    . HOH   R 5 .   ? -44.301 19.467  40.513  1.00 45.56 ? 571 HOH   C O    1 
HETATM 8577 O  O    . HOH   R 5 .   ? -15.231 5.995   34.397  1.00 47.03 ? 572 HOH   C O    1 
HETATM 8578 O  O    . HOH   R 5 .   ? -13.890 -4.889  39.779  1.00 37.00 ? 573 HOH   C O    1 
HETATM 8579 O  O    . HOH   R 5 .   ? -52.838 18.988  21.771  1.00 37.07 ? 574 HOH   C O    1 
HETATM 8580 O  O    . HOH   R 5 .   ? -43.473 4.523   26.810  1.00 31.96 ? 575 HOH   C O    1 
HETATM 8581 O  O    . HOH   R 5 .   ? -30.682 18.131  40.307  1.00 41.72 ? 576 HOH   C O    1 
HETATM 8582 O  O    . HOH   R 5 .   ? -45.821 5.442   22.978  1.00 33.34 ? 577 HOH   C O    1 
HETATM 8583 O  O    . HOH   R 5 .   ? -38.578 -2.061  59.976  1.00 44.45 ? 578 HOH   C O    1 
HETATM 8584 O  O    . HOH   R 5 .   ? -49.234 -0.177  47.767  1.00 34.85 ? 579 HOH   C O    1 
HETATM 8585 O  O    . HOH   R 5 .   ? -42.372 14.090  50.282  1.00 45.97 ? 580 HOH   C O    1 
HETATM 8586 O  O    . HOH   R 5 .   ? -35.845 18.621  28.144  1.00 39.01 ? 581 HOH   C O    1 
HETATM 8587 O  O    . HOH   R 5 .   ? -13.858 -3.276  41.734  1.00 41.65 ? 582 HOH   C O    1 
HETATM 8588 O  O    . HOH   R 5 .   ? -24.655 20.004  27.822  1.00 50.63 ? 583 HOH   C O    1 
HETATM 8589 O  O    B HOH   R 5 .   ? -21.698 16.981  29.787  0.40 32.76 ? 584 HOH   C O    1 
HETATM 8590 O  O    . HOH   R 5 .   ? -32.566 19.535  42.064  1.00 42.08 ? 585 HOH   C O    1 
HETATM 8591 O  O    . HOH   R 5 .   ? -41.400 2.504   24.747  1.00 48.31 ? 586 HOH   C O    1 
HETATM 8592 O  O    . HOH   R 5 .   ? -30.459 20.725  24.178  1.00 40.39 ? 587 HOH   C O    1 
HETATM 8593 O  O    . HOH   R 5 .   ? -27.240 20.369  20.925  1.00 46.14 ? 588 HOH   C O    1 
HETATM 8594 O  O    . HOH   R 5 .   ? -55.788 1.301   45.587  1.00 52.29 ? 589 HOH   C O    1 
HETATM 8595 O  O    . HOH   R 5 .   ? -19.314 22.651  20.591  1.00 49.79 ? 590 HOH   C O    1 
HETATM 8596 O  O    . HOH   S 5 .   ? -65.982 -23.986 30.455  1.00 50.69 ? 401 HOH   D O    1 
HETATM 8597 O  O    . HOH   S 5 .   ? -70.813 -10.052 30.784  1.00 30.64 ? 402 HOH   D O    1 
HETATM 8598 O  O    . HOH   S 5 .   ? -82.911 9.930   30.128  1.00 45.20 ? 403 HOH   D O    1 
HETATM 8599 O  O    . HOH   S 5 .   ? -82.877 2.304   28.682  1.00 34.52 ? 404 HOH   D O    1 
HETATM 8600 O  O    . HOH   S 5 .   ? -66.648 -2.411  24.200  1.00 19.44 ? 405 HOH   D O    1 
HETATM 8601 O  O    . HOH   S 5 .   ? -76.061 -8.835  16.449  1.00 35.79 ? 406 HOH   D O    1 
HETATM 8602 O  O    . HOH   S 5 .   ? -48.797 -24.468 25.477  1.00 47.91 ? 407 HOH   D O    1 
HETATM 8603 O  O    . HOH   S 5 .   ? -62.603 13.056  17.394  1.00 19.49 ? 408 HOH   D O    1 
HETATM 8604 O  O    . HOH   S 5 .   ? -81.811 -11.881 41.558  1.00 44.10 ? 409 HOH   D O    1 
HETATM 8605 O  O    . HOH   S 5 .   ? -81.502 -4.798  42.844  1.00 35.74 ? 410 HOH   D O    1 
HETATM 8606 O  O    . HOH   S 5 .   ? -63.358 18.547  19.912  1.00 41.98 ? 411 HOH   D O    1 
HETATM 8607 O  O    . HOH   S 5 .   ? -57.205 12.855  28.399  1.00 16.17 ? 412 HOH   D O    1 
HETATM 8608 O  O    . HOH   S 5 .   ? -69.458 13.898  38.041  1.00 28.85 ? 413 HOH   D O    1 
HETATM 8609 O  O    . HOH   S 5 .   ? -69.558 -3.603  47.423  1.00 35.54 ? 414 HOH   D O    1 
HETATM 8610 O  O    . HOH   S 5 .   ? -78.274 -0.764  19.369  1.00 22.98 ? 415 HOH   D O    1 
HETATM 8611 O  O    . HOH   S 5 .   ? -71.922 4.114   46.648  1.00 39.55 ? 416 HOH   D O    1 
HETATM 8612 O  O    . HOH   S 5 .   ? -74.582 -8.777  48.853  1.00 44.41 ? 417 HOH   D O    1 
HETATM 8613 O  O    . HOH   S 5 .   ? -50.132 -15.419 15.573  1.00 21.50 ? 418 HOH   D O    1 
HETATM 8614 O  O    . HOH   S 5 .   ? -56.896 -9.134  42.649  1.00 40.78 ? 419 HOH   D O    1 
HETATM 8615 O  O    . HOH   S 5 .   ? -73.828 -13.861 26.664  1.00 47.25 ? 420 HOH   D O    1 
HETATM 8616 O  O    . HOH   S 5 .   ? -74.264 -10.447 23.675  1.00 26.83 ? 421 HOH   D O    1 
HETATM 8617 O  O    . HOH   S 5 .   ? -68.196 -12.286 23.737  1.00 24.53 ? 422 HOH   D O    1 
HETATM 8618 O  O    . HOH   S 5 .   ? -49.379 -7.994  20.589  1.00 20.66 ? 423 HOH   D O    1 
HETATM 8619 O  O    . HOH   S 5 .   ? -77.524 -1.529  16.923  1.00 21.73 ? 424 HOH   D O    1 
HETATM 8620 O  O    . HOH   S 5 .   ? -52.766 -0.112  15.778  1.00 33.66 ? 425 HOH   D O    1 
HETATM 8621 O  O    . HOH   S 5 .   ? -45.898 -8.258  15.959  1.00 27.40 ? 426 HOH   D O    1 
HETATM 8622 O  O    . HOH   S 5 .   ? -68.778 16.685  34.793  1.00 33.03 ? 427 HOH   D O    1 
HETATM 8623 O  O    . HOH   S 5 .   ? -53.782 -15.393 37.878  1.00 27.26 ? 428 HOH   D O    1 
HETATM 8624 O  O    . HOH   S 5 .   ? -68.460 -0.736  25.480  1.00 17.43 ? 429 HOH   D O    1 
HETATM 8625 O  O    . HOH   S 5 .   ? -56.287 -12.508 13.049  1.00 18.78 ? 430 HOH   D O    1 
HETATM 8626 O  O    . HOH   S 5 .   ? -56.670 19.651  31.228  1.00 30.97 ? 431 HOH   D O    1 
HETATM 8627 O  O    . HOH   S 5 .   ? -55.563 -1.290  41.920  1.00 26.40 ? 432 HOH   D O    1 
HETATM 8628 O  O    . HOH   S 5 .   ? -64.374 9.064   39.750  1.00 27.39 ? 433 HOH   D O    1 
HETATM 8629 O  O    . HOH   S 5 .   ? -75.057 11.790  23.135  1.00 37.37 ? 434 HOH   D O    1 
HETATM 8630 O  O    . HOH   S 5 .   ? -67.111 -9.404  30.831  1.00 17.75 ? 435 HOH   D O    1 
HETATM 8631 O  O    . HOH   S 5 .   ? -54.628 -11.365 30.983  1.00 23.56 ? 436 HOH   D O    1 
HETATM 8632 O  O    . HOH   S 5 .   ? -60.358 -4.959  45.912  1.00 55.30 ? 437 HOH   D O    1 
HETATM 8633 O  O    . HOH   S 5 .   ? -83.869 -7.631  29.191  1.00 41.78 ? 438 HOH   D O    1 
HETATM 8634 O  O    . HOH   S 5 .   ? -66.422 -12.279 37.566  1.00 26.45 ? 439 HOH   D O    1 
HETATM 8635 O  O    . HOH   S 5 .   ? -45.728 -8.402  28.795  1.00 19.84 ? 440 HOH   D O    1 
HETATM 8636 O  O    . HOH   S 5 .   ? -68.666 6.439   47.846  1.00 42.46 ? 441 HOH   D O    1 
HETATM 8637 O  O    . HOH   S 5 .   ? -74.781 -12.893 40.983  1.00 32.26 ? 442 HOH   D O    1 
HETATM 8638 O  O    . HOH   S 5 .   ? -54.217 -3.504  22.797  1.00 30.00 ? 443 HOH   D O    1 
HETATM 8639 O  O    . HOH   S 5 .   ? -69.878 -13.536 28.540  1.00 28.85 ? 444 HOH   D O    1 
HETATM 8640 O  O    . HOH   S 5 .   ? -56.850 -13.086 41.807  1.00 32.07 ? 445 HOH   D O    1 
HETATM 8641 O  O    . HOH   S 5 .   ? -49.426 -15.611 37.677  1.00 31.43 ? 446 HOH   D O    1 
HETATM 8642 O  O    B HOH   S 5 .   ? -53.510 -7.703  14.115  0.60 19.19 ? 447 HOH   D O    1 
HETATM 8643 O  O    . HOH   S 5 .   ? -53.403 -8.088  41.084  1.00 22.23 ? 448 HOH   D O    1 
HETATM 8644 O  O    . HOH   S 5 .   ? -75.150 -14.519 46.012  1.00 36.04 ? 449 HOH   D O    1 
HETATM 8645 O  O    . HOH   S 5 .   ? -78.425 6.447   44.318  1.00 31.40 ? 450 HOH   D O    1 
HETATM 8646 O  O    . HOH   S 5 .   ? -51.788 -13.688 29.796  1.00 16.41 ? 451 HOH   D O    1 
HETATM 8647 O  O    . HOH   S 5 .   ? -46.919 -14.753 22.347  1.00 23.03 ? 452 HOH   D O    1 
HETATM 8648 O  O    . HOH   S 5 .   ? -60.302 -19.313 32.734  1.00 32.95 ? 453 HOH   D O    1 
HETATM 8649 O  O    . HOH   S 5 .   ? -59.561 12.428  35.687  1.00 24.04 ? 454 HOH   D O    1 
HETATM 8650 O  O    . HOH   S 5 .   ? -61.709 15.040  35.955  1.00 25.44 ? 455 HOH   D O    1 
HETATM 8651 O  O    . HOH   S 5 .   ? -55.268 18.373  23.798  1.00 31.89 ? 456 HOH   D O    1 
HETATM 8652 O  O    . HOH   S 5 .   ? -61.581 8.312   37.074  1.00 21.20 ? 457 HOH   D O    1 
HETATM 8653 O  O    . HOH   S 5 .   ? -60.158 19.329  22.536  1.00 34.49 ? 458 HOH   D O    1 
HETATM 8654 O  O    . HOH   S 5 .   ? -81.717 -12.734 38.479  1.00 32.74 ? 459 HOH   D O    1 
HETATM 8655 O  O    . HOH   S 5 .   ? -61.602 9.105   42.189  1.00 49.22 ? 460 HOH   D O    1 
HETATM 8656 O  O    . HOH   S 5 .   ? -61.569 6.191   42.051  1.00 30.66 ? 461 HOH   D O    1 
HETATM 8657 O  O    . HOH   S 5 .   ? -43.800 -19.331 27.461  1.00 29.97 ? 462 HOH   D O    1 
HETATM 8658 O  O    . HOH   S 5 .   ? -45.717 -7.563  20.415  1.00 38.19 ? 463 HOH   D O    1 
HETATM 8659 O  O    . HOH   S 5 .   ? -53.229 15.766  36.418  1.00 42.27 ? 464 HOH   D O    1 
HETATM 8660 O  O    . HOH   S 5 .   ? -84.649 7.895   27.334  1.00 38.83 ? 465 HOH   D O    1 
HETATM 8661 O  O    . HOH   S 5 .   ? -72.382 -13.640 36.432  1.00 37.70 ? 466 HOH   D O    1 
HETATM 8662 O  O    . HOH   S 5 .   ? -47.226 -5.495  20.704  1.00 37.21 ? 467 HOH   D O    1 
HETATM 8663 O  O    . HOH   S 5 .   ? -65.237 -10.359 41.554  1.00 31.37 ? 468 HOH   D O    1 
HETATM 8664 O  O    . HOH   S 5 .   ? -41.122 -19.264 22.895  1.00 36.46 ? 469 HOH   D O    1 
HETATM 8665 O  O    . HOH   S 5 .   ? -74.001 -11.931 37.878  1.00 40.30 ? 470 HOH   D O    1 
HETATM 8666 O  O    . HOH   S 5 .   ? -70.395 -17.571 8.961   1.00 44.77 ? 471 HOH   D O    1 
HETATM 8667 O  O    . HOH   S 5 .   ? -73.968 8.074   20.946  1.00 23.75 ? 472 HOH   D O    1 
HETATM 8668 O  O    . HOH   S 5 .   ? -55.458 5.785   44.717  1.00 45.91 ? 473 HOH   D O    1 
HETATM 8669 O  O    . HOH   S 5 .   ? -58.956 13.407  18.708  1.00 20.72 ? 474 HOH   D O    1 
HETATM 8670 O  O    . HOH   S 5 .   ? -81.426 -6.284  22.367  1.00 36.61 ? 475 HOH   D O    1 
HETATM 8671 O  O    . HOH   S 5 .   ? -48.199 -7.687  31.812  1.00 15.19 ? 476 HOH   D O    1 
HETATM 8672 O  O    . HOH   S 5 .   ? -63.192 -7.584  44.197  1.00 36.25 ? 477 HOH   D O    1 
HETATM 8673 O  O    . HOH   S 5 .   ? -62.660 -12.079 13.958  1.00 16.26 ? 478 HOH   D O    1 
HETATM 8674 O  O    . HOH   S 5 .   ? -80.639 -0.035  23.064  1.00 30.63 ? 479 HOH   D O    1 
HETATM 8675 O  O    . HOH   S 5 .   ? -65.850 -15.049 7.760   1.00 31.61 ? 480 HOH   D O    1 
HETATM 8676 O  O    . HOH   S 5 .   ? -67.438 -16.923 8.926   1.00 44.98 ? 481 HOH   D O    1 
HETATM 8677 O  O    . HOH   S 5 .   ? -61.631 -14.616 38.185  1.00 27.39 ? 482 HOH   D O    1 
HETATM 8678 O  O    . HOH   S 5 .   ? -49.365 -5.405  23.463  1.00 33.00 ? 483 HOH   D O    1 
HETATM 8679 O  O    . HOH   S 5 .   ? -76.987 -9.742  6.697   1.00 41.20 ? 484 HOH   D O    1 
HETATM 8680 O  O    . HOH   S 5 .   ? -73.252 3.452   14.088  1.00 31.84 ? 485 HOH   D O    1 
HETATM 8681 O  O    . HOH   S 5 .   ? -72.175 -4.545  8.465   1.00 25.61 ? 486 HOH   D O    1 
HETATM 8682 O  O    . HOH   S 5 .   ? -82.214 -12.313 27.310  1.00 45.20 ? 487 HOH   D O    1 
HETATM 8683 O  O    . HOH   S 5 .   ? -50.544 10.266  37.964  1.00 18.42 ? 488 HOH   D O    1 
HETATM 8684 O  O    . HOH   S 5 .   ? -63.928 -3.763  24.560  1.00 27.31 ? 489 HOH   D O    1 
HETATM 8685 O  O    . HOH   S 5 .   ? -71.000 13.660  35.675  1.00 26.03 ? 490 HOH   D O    1 
HETATM 8686 O  O    . HOH   S 5 .   ? -75.090 5.287   8.047   1.00 40.01 ? 491 HOH   D O    1 
HETATM 8687 O  O    . HOH   S 5 .   ? -36.322 -18.463 23.733  1.00 37.70 ? 492 HOH   D O    1 
HETATM 8688 O  O    . HOH   S 5 .   ? -52.974 -29.582 27.546  1.00 43.67 ? 493 HOH   D O    1 
HETATM 8689 O  O    . HOH   S 5 .   ? -45.715 -6.451  24.221  1.00 30.41 ? 494 HOH   D O    1 
HETATM 8690 O  O    . HOH   S 5 .   ? -78.057 -8.836  18.234  1.00 42.55 ? 495 HOH   D O    1 
HETATM 8691 O  O    . HOH   S 5 .   ? -62.551 6.130   24.647  1.00 16.98 ? 496 HOH   D O    1 
HETATM 8692 O  O    . HOH   S 5 .   ? -58.781 7.433   44.301  1.00 42.24 ? 497 HOH   D O    1 
HETATM 8693 O  O    . HOH   S 5 .   ? -59.994 0.400   45.427  1.00 44.52 ? 498 HOH   D O    1 
HETATM 8694 O  O    . HOH   S 5 .   ? -73.127 20.371  30.443  1.00 59.32 ? 499 HOH   D O    1 
HETATM 8695 O  O    . HOH   S 5 .   ? -81.130 7.853   22.901  1.00 32.62 ? 500 HOH   D O    1 
HETATM 8696 O  O    . HOH   S 5 .   ? -49.520 2.805   26.314  1.00 23.87 ? 501 HOH   D O    1 
HETATM 8697 O  O    . HOH   S 5 .   ? -50.528 4.611   23.863  1.00 34.53 ? 502 HOH   D O    1 
HETATM 8698 O  O    . HOH   S 5 .   ? -48.369 -1.612  29.234  1.00 20.93 ? 503 HOH   D O    1 
HETATM 8699 O  O    A HOH   S 5 .   ? -81.967 -2.162  37.739  0.60 22.94 ? 504 HOH   D O    1 
HETATM 8700 O  O    B HOH   S 5 .   ? -81.881 -3.299  38.924  0.40 24.35 ? 504 HOH   D O    1 
HETATM 8701 O  O    . HOH   S 5 .   ? -80.698 -2.485  22.147  1.00 34.64 ? 505 HOH   D O    1 
HETATM 8702 O  O    . HOH   S 5 .   ? -58.887 14.868  35.781  1.00 46.72 ? 506 HOH   D O    1 
HETATM 8703 O  O    . HOH   S 5 .   ? -81.660 -0.872  46.696  1.00 37.22 ? 507 HOH   D O    1 
HETATM 8704 O  O    . HOH   S 5 .   ? -72.105 -13.376 4.022   1.00 34.44 ? 508 HOH   D O    1 
HETATM 8705 O  O    . HOH   S 5 .   ? -71.948 -2.573  10.173  1.00 23.59 ? 509 HOH   D O    1 
HETATM 8706 O  O    . HOH   S 5 .   ? -68.672 -13.247 21.217  1.00 24.97 ? 510 HOH   D O    1 
HETATM 8707 O  O    A HOH   S 5 .   ? -63.923 -8.073  41.678  0.70 20.47 ? 511 HOH   D O    1 
HETATM 8708 O  O    . HOH   S 5 .   ? -79.732 1.661   25.140  1.00 34.36 ? 512 HOH   D O    1 
HETATM 8709 O  O    . HOH   S 5 .   ? -81.469 4.047   35.052  1.00 28.76 ? 513 HOH   D O    1 
HETATM 8710 O  O    . HOH   S 5 .   ? -50.322 5.820   45.206  1.00 39.66 ? 514 HOH   D O    1 
HETATM 8711 O  O    . HOH   S 5 .   ? -66.838 -17.879 32.405  1.00 32.16 ? 515 HOH   D O    1 
HETATM 8712 O  O    . HOH   S 5 .   ? -78.738 0.319   10.190  1.00 27.88 ? 516 HOH   D O    1 
HETATM 8713 O  O    . HOH   S 5 .   ? -78.158 -14.272 32.565  1.00 27.37 ? 517 HOH   D O    1 
HETATM 8714 O  O    . HOH   S 5 .   ? -58.771 6.023   32.725  1.00 17.08 ? 518 HOH   D O    1 
HETATM 8715 O  O    . HOH   S 5 .   ? -53.011 -14.363 20.014  1.00 30.83 ? 519 HOH   D O    1 
HETATM 8716 O  O    . HOH   S 5 .   ? -66.296 -1.931  50.244  1.00 49.05 ? 520 HOH   D O    1 
HETATM 8717 O  O    . HOH   S 5 .   ? -73.297 -8.324  30.355  1.00 21.74 ? 521 HOH   D O    1 
HETATM 8718 O  O    . HOH   S 5 .   ? -51.296 -14.722 39.556  1.00 40.56 ? 522 HOH   D O    1 
HETATM 8719 O  O    . HOH   S 5 .   ? -76.345 -13.139 9.917   1.00 31.51 ? 523 HOH   D O    1 
HETATM 8720 O  O    . HOH   S 5 .   ? -56.567 -3.589  21.700  1.00 28.42 ? 524 HOH   D O    1 
HETATM 8721 O  O    . HOH   S 5 .   ? -55.944 -21.325 36.653  1.00 38.16 ? 525 HOH   D O    1 
HETATM 8722 O  O    . HOH   S 5 .   ? -56.397 14.903  35.652  1.00 43.40 ? 526 HOH   D O    1 
HETATM 8723 O  O    . HOH   S 5 .   ? -60.147 3.694   42.080  1.00 26.26 ? 527 HOH   D O    1 
HETATM 8724 O  O    . HOH   S 5 .   ? -80.978 -14.180 31.340  1.00 34.99 ? 528 HOH   D O    1 
HETATM 8725 O  O    . HOH   S 5 .   ? -82.891 -1.507  30.158  1.00 30.77 ? 529 HOH   D O    1 
HETATM 8726 O  O    . HOH   S 5 .   ? -77.683 0.067   52.641  1.00 43.62 ? 530 HOH   D O    1 
HETATM 8727 O  O    . HOH   S 5 .   ? -59.072 -9.174  44.427  1.00 51.85 ? 531 HOH   D O    1 
HETATM 8728 O  O    . HOH   S 5 .   ? -48.715 -2.447  15.145  1.00 48.33 ? 532 HOH   D O    1 
HETATM 8729 O  O    A HOH   S 5 .   ? -69.298 -15.021 35.283  0.70 30.55 ? 533 HOH   D O    1 
HETATM 8730 O  O    B HOH   S 5 .   ? -70.529 -16.251 34.302  0.30 25.54 ? 533 HOH   D O    1 
HETATM 8731 O  O    . HOH   S 5 .   ? -59.891 -29.312 25.229  1.00 34.76 ? 534 HOH   D O    1 
HETATM 8732 O  O    . HOH   S 5 .   ? -78.993 6.610   16.388  1.00 26.29 ? 535 HOH   D O    1 
HETATM 8733 O  O    . HOH   S 5 .   ? -72.157 -9.869  19.490  1.00 38.31 ? 536 HOH   D O    1 
HETATM 8734 O  O    B HOH   S 5 .   ? -75.035 12.346  25.754  0.40 21.41 ? 537 HOH   D O    1 
HETATM 8735 O  O    . HOH   S 5 .   ? -51.996 -22.561 20.288  1.00 43.57 ? 538 HOH   D O    1 
HETATM 8736 O  O    . HOH   S 5 .   ? -76.816 4.227   6.143   1.00 44.33 ? 539 HOH   D O    1 
HETATM 8737 O  O    . HOH   S 5 .   ? -67.359 -11.157 39.812  1.00 40.90 ? 540 HOH   D O    1 
HETATM 8738 O  O    . HOH   S 5 .   ? -67.179 -19.914 24.479  1.00 47.06 ? 541 HOH   D O    1 
HETATM 8739 O  O    . HOH   S 5 .   ? -84.879 -9.556  41.290  1.00 58.45 ? 542 HOH   D O    1 
HETATM 8740 O  O    . HOH   S 5 .   ? -49.739 -1.633  25.791  1.00 38.89 ? 543 HOH   D O    1 
HETATM 8741 O  O    A HOH   S 5 .   ? -70.660 -16.110 16.092  0.50 29.12 ? 544 HOH   D O    1 
HETATM 8742 O  O    B HOH   S 5 .   ? -69.475 -17.547 16.474  0.50 33.58 ? 544 HOH   D O    1 
HETATM 8743 O  O    . HOH   S 5 .   ? -82.480 -0.342  44.593  1.00 36.89 ? 545 HOH   D O    1 
HETATM 8744 O  O    . HOH   S 5 .   ? -74.666 -1.964  10.226  1.00 34.75 ? 546 HOH   D O    1 
HETATM 8745 O  O    . HOH   S 5 .   ? -48.189 4.764   20.927  1.00 46.94 ? 547 HOH   D O    1 
HETATM 8746 O  O    . HOH   S 5 .   ? -54.913 -6.866  45.015  1.00 45.62 ? 548 HOH   D O    1 
HETATM 8747 O  O    . HOH   S 5 .   ? -55.693 2.907   43.695  1.00 46.61 ? 549 HOH   D O    1 
HETATM 8748 O  O    . HOH   S 5 .   ? -56.770 -12.139 18.982  1.00 20.64 ? 550 HOH   D O    1 
HETATM 8749 O  O    . HOH   S 5 .   ? -81.172 -0.294  13.217  1.00 40.99 ? 551 HOH   D O    1 
HETATM 8750 O  O    . HOH   S 5 .   ? -78.003 9.805   19.302  1.00 44.13 ? 552 HOH   D O    1 
HETATM 8751 O  O    . HOH   S 5 .   ? -64.094 -17.800 19.752  1.00 45.63 ? 553 HOH   D O    1 
HETATM 8752 O  O    . HOH   S 5 .   ? -80.818 11.190  40.279  1.00 44.54 ? 554 HOH   D O    1 
HETATM 8753 O  O    . HOH   S 5 .   ? -66.588 -16.059 25.973  1.00 37.84 ? 555 HOH   D O    1 
HETATM 8754 O  O    . HOH   S 5 .   ? -68.624 -2.749  49.640  1.00 47.29 ? 556 HOH   D O    1 
HETATM 8755 O  O    . HOH   S 5 .   ? -72.876 -12.496 22.572  1.00 29.83 ? 557 HOH   D O    1 
HETATM 8756 O  O    . HOH   S 5 .   ? -66.796 2.418   50.057  1.00 51.40 ? 558 HOH   D O    1 
HETATM 8757 O  O    . HOH   S 5 .   ? -78.828 -3.590  15.597  1.00 43.63 ? 559 HOH   D O    1 
HETATM 8758 O  O    . HOH   S 5 .   ? -64.189 6.952   44.832  1.00 52.77 ? 560 HOH   D O    1 
HETATM 8759 O  O    . HOH   S 5 .   ? -78.087 -15.585 37.730  1.00 37.88 ? 561 HOH   D O    1 
HETATM 8760 O  O    . HOH   S 5 .   ? -81.502 4.146   41.546  1.00 42.77 ? 562 HOH   D O    1 
HETATM 8761 O  O    . HOH   S 5 .   ? -71.254 -12.176 20.276  1.00 40.10 ? 563 HOH   D O    1 
HETATM 8762 O  O    . HOH   S 5 .   ? -64.430 -14.315 37.976  1.00 44.11 ? 564 HOH   D O    1 
HETATM 8763 O  O    . HOH   S 5 .   ? -70.369 -8.912  45.079  1.00 41.11 ? 565 HOH   D O    1 
HETATM 8764 O  O    . HOH   S 5 .   ? -72.285 15.949  35.497  1.00 35.76 ? 566 HOH   D O    1 
HETATM 8765 O  O    . HOH   S 5 .   ? -56.105 -19.728 16.859  1.00 55.34 ? 567 HOH   D O    1 
HETATM 8766 O  O    . HOH   S 5 .   ? -68.089 16.265  37.177  1.00 45.75 ? 568 HOH   D O    1 
HETATM 8767 O  O    . HOH   S 5 .   ? -45.332 -16.421 39.519  1.00 42.22 ? 569 HOH   D O    1 
HETATM 8768 O  O    . HOH   S 5 .   ? -39.801 -17.461 24.960  1.00 27.18 ? 570 HOH   D O    1 
HETATM 8769 O  O    A HOH   S 5 .   ? -58.700 -17.639 37.028  0.50 30.08 ? 571 HOH   D O    1 
HETATM 8770 O  O    B HOH   S 5 .   ? -57.076 -17.714 37.348  0.30 32.38 ? 571 HOH   D O    1 
HETATM 8771 O  O    . HOH   S 5 .   ? -54.452 1.143   42.669  1.00 32.48 ? 572 HOH   D O    1 
HETATM 8772 O  O    . HOH   S 5 .   ? -68.311 16.961  41.367  1.00 53.17 ? 573 HOH   D O    1 
HETATM 8773 O  O    . HOH   S 5 .   ? -70.096 -6.963  46.700  1.00 47.68 ? 574 HOH   D O    1 
HETATM 8774 O  O    . HOH   S 5 .   ? -59.439 -2.061  44.912  1.00 46.61 ? 575 HOH   D O    1 
HETATM 8775 O  O    . HOH   S 5 .   ? -70.891 -12.649 24.482  1.00 32.27 ? 576 HOH   D O    1 
HETATM 8776 O  O    . HOH   S 5 .   ? -64.750 18.019  43.238  1.00 54.49 ? 577 HOH   D O    1 
HETATM 8777 O  O    . HOH   S 5 .   ? -41.177 -18.239 27.510  1.00 40.71 ? 578 HOH   D O    1 
HETATM 8778 O  O    . HOH   S 5 .   ? -46.973 -4.938  23.158  1.00 32.89 ? 579 HOH   D O    1 
HETATM 8779 O  O    . HOH   S 5 .   ? -73.224 10.052  19.381  1.00 34.51 ? 580 HOH   D O    1 
HETATM 8780 O  O    . HOH   S 5 .   ? -51.104 -3.694  24.876  1.00 35.00 ? 581 HOH   D O    1 
HETATM 8781 O  O    A HOH   S 5 .   ? -58.295 -18.048 22.328  0.70 38.76 ? 582 HOH   D O    1 
HETATM 8782 O  O    B HOH   S 5 .   ? -58.913 -18.429 20.241  0.30 28.60 ? 582 HOH   D O    1 
HETATM 8783 O  O    . HOH   S 5 .   ? -58.797 3.125   44.409  1.00 36.23 ? 583 HOH   D O    1 
HETATM 8784 O  O    . HOH   S 5 .   ? -81.275 -2.472  19.092  1.00 38.07 ? 584 HOH   D O    1 
HETATM 8785 O  O    . HOH   S 5 .   ? -51.456 -2.063  21.421  1.00 42.27 ? 585 HOH   D O    1 
HETATM 8786 O  O    . HOH   S 5 .   ? -84.486 -11.957 36.571  1.00 47.60 ? 586 HOH   D O    1 
HETATM 8787 O  O    . HOH   S 5 .   ? -69.657 -17.335 32.121  1.00 43.65 ? 587 HOH   D O    1 
HETATM 8788 O  O    . HOH   S 5 .   ? -60.470 -20.631 16.259  1.00 41.69 ? 588 HOH   D O    1 
HETATM 8789 O  O    . HOH   S 5 .   ? -50.642 -0.004  22.521  1.00 46.99 ? 589 HOH   D O    1 
# 
