data_8EN1
# 
_entry.id   8EN1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.367 
_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   8EN1         pdb_00008en1 10.2210/pdb8en1/pdb 
WWPDB D_1000267421 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8EN1 
_pdbx_database_status.recvd_initial_deposition_date   2022-09-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kher, G.'        1 ? 
'Sabin, C.'       2 ? 
'Pancera, M.'     3 ? 
'Koromyslova, A.' 4 ? 
'Hansman, G.'     5 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of GII.4 norovirus in complex with Nanobody 30' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kher, G.'        1 ? 
primary 'Sabin, C.'       2 ? 
primary 'Pancera, M.'     3 ? 
primary 'Koromyslova, A.' 4 ? 
primary 'Hansman, G.'     5 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.240 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8EN1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     117.767 
_cell.length_a_esd                 ? 
_cell.length_b                     62.443 
_cell.length_b_esd                 ? 
_cell.length_c                     121.396 
_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                         8EN1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'GII.4 P domain' 35103.141 2   ? ? ? ? 
2 polymer man 'Nanobody 30'    15303.775 2   ? ? ? ? 
3 water   nat water            18.015    273 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;TKPFSVPVLTVEEMTNSRFPIPLEKLFTGPSSAFVVQPQNGRCTTDGVLLGTTQLSPVNICTFRGDVTHITGSRNYTMNL
ASQNWNDYDPTEEIPAPLGTPDFVGKIQGVLTQTTRTDGSTRGHKATVYTGSADFAPKLGRVQFETDTDRDFEANQNTKF
TPVGVIQDGGTTHRNEPQQWVLPSYSGRNTHNVHLAPAVAPTFPGEQLLFFRSTMPGCSGYPNMDLDCLLPQEWVQYFYQ
EAAPAQSDVALLRFVNPDTGRVLFECKLHKSGYVTVAHTGQHDLVIPPNGYFRFDSWVNQFYTLAPMGNGTGRRRAV
;
;TKPFSVPVLTVEEMTNSRFPIPLEKLFTGPSSAFVVQPQNGRCTTDGVLLGTTQLSPVNICTFRGDVTHITGSRNYTMNL
ASQNWNDYDPTEEIPAPLGTPDFVGKIQGVLTQTTRTDGSTRGHKATVYTGSADFAPKLGRVQFETDTDRDFEANQNTKF
TPVGVIQDGGTTHRNEPQQWVLPSYSGRNTHNVHLAPAVAPTFPGEQLLFFRSTMPGCSGYPNMDLDCLLPQEWVQYFYQ
EAAPAQSDVALLRFVNPDTGRVLFECKLHKSGYVTVAHTGQHDLVIPPNGYFRFDSWVNQFYTLAPMGNGTGRRRAV
;
A,B ? 
2 'polypeptide(L)' no no 
;QVQLQESGGGLVQAGGSLNLACVSSGRTFSTWLMGWFRQAPGKEREFVASIDWRSSSTTYADSVKGRFTISRDNAKNTMY
LQMTGLKPEDTAVYYCASDRDHYSGTYYGRRFVEEYDYWGQGTQVTVSSHHHHHH
;
;QVQLQESGGGLVQAGGSLNLACVSSGRTFSTWLMGWFRQAPGKEREFVASIDWRSSSTTYADSVKGRFTISRDNAKNTMY
LQMTGLKPEDTAVYYCASDRDHYSGTYYGRRFVEEYDYWGQGTQVTVSSHHHHHH
;
C,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   LYS n 
1 3   PRO n 
1 4   PHE n 
1 5   SER n 
1 6   VAL n 
1 7   PRO n 
1 8   VAL n 
1 9   LEU n 
1 10  THR n 
1 11  VAL n 
1 12  GLU n 
1 13  GLU n 
1 14  MET n 
1 15  THR n 
1 16  ASN n 
1 17  SER n 
1 18  ARG n 
1 19  PHE n 
1 20  PRO n 
1 21  ILE n 
1 22  PRO n 
1 23  LEU n 
1 24  GLU n 
1 25  LYS n 
1 26  LEU n 
1 27  PHE n 
1 28  THR n 
1 29  GLY n 
1 30  PRO n 
1 31  SER n 
1 32  SER n 
1 33  ALA n 
1 34  PHE n 
1 35  VAL n 
1 36  VAL n 
1 37  GLN n 
1 38  PRO n 
1 39  GLN n 
1 40  ASN n 
1 41  GLY n 
1 42  ARG n 
1 43  CYS n 
1 44  THR n 
1 45  THR n 
1 46  ASP n 
1 47  GLY n 
1 48  VAL n 
1 49  LEU n 
1 50  LEU n 
1 51  GLY n 
1 52  THR n 
1 53  THR n 
1 54  GLN n 
1 55  LEU n 
1 56  SER n 
1 57  PRO n 
1 58  VAL n 
1 59  ASN n 
1 60  ILE n 
1 61  CYS n 
1 62  THR n 
1 63  PHE n 
1 64  ARG n 
1 65  GLY n 
1 66  ASP n 
1 67  VAL n 
1 68  THR n 
1 69  HIS n 
1 70  ILE n 
1 71  THR n 
1 72  GLY n 
1 73  SER n 
1 74  ARG n 
1 75  ASN n 
1 76  TYR n 
1 77  THR n 
1 78  MET n 
1 79  ASN n 
1 80  LEU n 
1 81  ALA n 
1 82  SER n 
1 83  GLN n 
1 84  ASN n 
1 85  TRP n 
1 86  ASN n 
1 87  ASP n 
1 88  TYR n 
1 89  ASP n 
1 90  PRO n 
1 91  THR n 
1 92  GLU n 
1 93  GLU n 
1 94  ILE n 
1 95  PRO n 
1 96  ALA n 
1 97  PRO n 
1 98  LEU n 
1 99  GLY n 
1 100 THR n 
1 101 PRO n 
1 102 ASP n 
1 103 PHE n 
1 104 VAL n 
1 105 GLY n 
1 106 LYS n 
1 107 ILE n 
1 108 GLN n 
1 109 GLY n 
1 110 VAL n 
1 111 LEU n 
1 112 THR n 
1 113 GLN n 
1 114 THR n 
1 115 THR n 
1 116 ARG n 
1 117 THR n 
1 118 ASP n 
1 119 GLY n 
1 120 SER n 
1 121 THR n 
1 122 ARG n 
1 123 GLY n 
1 124 HIS n 
1 125 LYS n 
1 126 ALA n 
1 127 THR n 
1 128 VAL n 
1 129 TYR n 
1 130 THR n 
1 131 GLY n 
1 132 SER n 
1 133 ALA n 
1 134 ASP n 
1 135 PHE n 
1 136 ALA n 
1 137 PRO n 
1 138 LYS n 
1 139 LEU n 
1 140 GLY n 
1 141 ARG n 
1 142 VAL n 
1 143 GLN n 
1 144 PHE n 
1 145 GLU n 
1 146 THR n 
1 147 ASP n 
1 148 THR n 
1 149 ASP n 
1 150 ARG n 
1 151 ASP n 
1 152 PHE n 
1 153 GLU n 
1 154 ALA n 
1 155 ASN n 
1 156 GLN n 
1 157 ASN n 
1 158 THR n 
1 159 LYS n 
1 160 PHE n 
1 161 THR n 
1 162 PRO n 
1 163 VAL n 
1 164 GLY n 
1 165 VAL n 
1 166 ILE n 
1 167 GLN n 
1 168 ASP n 
1 169 GLY n 
1 170 GLY n 
1 171 THR n 
1 172 THR n 
1 173 HIS n 
1 174 ARG n 
1 175 ASN n 
1 176 GLU n 
1 177 PRO n 
1 178 GLN n 
1 179 GLN n 
1 180 TRP n 
1 181 VAL n 
1 182 LEU n 
1 183 PRO n 
1 184 SER n 
1 185 TYR n 
1 186 SER n 
1 187 GLY n 
1 188 ARG n 
1 189 ASN n 
1 190 THR n 
1 191 HIS n 
1 192 ASN n 
1 193 VAL n 
1 194 HIS n 
1 195 LEU n 
1 196 ALA n 
1 197 PRO n 
1 198 ALA n 
1 199 VAL n 
1 200 ALA n 
1 201 PRO n 
1 202 THR n 
1 203 PHE n 
1 204 PRO n 
1 205 GLY n 
1 206 GLU n 
1 207 GLN n 
1 208 LEU n 
1 209 LEU n 
1 210 PHE n 
1 211 PHE n 
1 212 ARG n 
1 213 SER n 
1 214 THR n 
1 215 MET n 
1 216 PRO n 
1 217 GLY n 
1 218 CYS n 
1 219 SER n 
1 220 GLY n 
1 221 TYR n 
1 222 PRO n 
1 223 ASN n 
1 224 MET n 
1 225 ASP n 
1 226 LEU n 
1 227 ASP n 
1 228 CYS n 
1 229 LEU n 
1 230 LEU n 
1 231 PRO n 
1 232 GLN n 
1 233 GLU n 
1 234 TRP n 
1 235 VAL n 
1 236 GLN n 
1 237 TYR n 
1 238 PHE n 
1 239 TYR n 
1 240 GLN n 
1 241 GLU n 
1 242 ALA n 
1 243 ALA n 
1 244 PRO n 
1 245 ALA n 
1 246 GLN n 
1 247 SER n 
1 248 ASP n 
1 249 VAL n 
1 250 ALA n 
1 251 LEU n 
1 252 LEU n 
1 253 ARG n 
1 254 PHE n 
1 255 VAL n 
1 256 ASN n 
1 257 PRO n 
1 258 ASP n 
1 259 THR n 
1 260 GLY n 
1 261 ARG n 
1 262 VAL n 
1 263 LEU n 
1 264 PHE n 
1 265 GLU n 
1 266 CYS n 
1 267 LYS n 
1 268 LEU n 
1 269 HIS n 
1 270 LYS n 
1 271 SER n 
1 272 GLY n 
1 273 TYR n 
1 274 VAL n 
1 275 THR n 
1 276 VAL n 
1 277 ALA n 
1 278 HIS n 
1 279 THR n 
1 280 GLY n 
1 281 GLN n 
1 282 HIS n 
1 283 ASP n 
1 284 LEU n 
1 285 VAL n 
1 286 ILE n 
1 287 PRO n 
1 288 PRO n 
1 289 ASN n 
1 290 GLY n 
1 291 TYR n 
1 292 PHE n 
1 293 ARG n 
1 294 PHE n 
1 295 ASP n 
1 296 SER n 
1 297 TRP n 
1 298 VAL n 
1 299 ASN n 
1 300 GLN n 
1 301 PHE n 
1 302 TYR n 
1 303 THR n 
1 304 LEU n 
1 305 ALA n 
1 306 PRO n 
1 307 MET n 
1 308 GLY n 
1 309 ASN n 
1 310 GLY n 
1 311 THR n 
1 312 GLY n 
1 313 ARG n 
1 314 ARG n 
1 315 ARG n 
1 316 ALA n 
1 317 VAL n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  ALA n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ASN n 
2 20  LEU n 
2 21  ALA n 
2 22  CYS n 
2 23  VAL n 
2 24  SER n 
2 25  SER n 
2 26  GLY n 
2 27  ARG n 
2 28  THR n 
2 29  PHE n 
2 30  SER n 
2 31  THR n 
2 32  TRP n 
2 33  LEU n 
2 34  MET n 
2 35  GLY n 
2 36  TRP n 
2 37  PHE n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLU n 
2 45  ARG n 
2 46  GLU n 
2 47  PHE n 
2 48  VAL n 
2 49  ALA n 
2 50  SER n 
2 51  ILE n 
2 52  ASP n 
2 53  TRP n 
2 54  ARG n 
2 55  SER n 
2 56  SER n 
2 57  SER n 
2 58  THR n 
2 59  THR n 
2 60  TYR n 
2 61  ALA n 
2 62  ASP n 
2 63  SER n 
2 64  VAL n 
2 65  LYS n 
2 66  GLY n 
2 67  ARG n 
2 68  PHE n 
2 69  THR n 
2 70  ILE n 
2 71  SER n 
2 72  ARG n 
2 73  ASP n 
2 74  ASN n 
2 75  ALA n 
2 76  LYS n 
2 77  ASN n 
2 78  THR n 
2 79  MET n 
2 80  TYR n 
2 81  LEU n 
2 82  GLN n 
2 83  MET n 
2 84  THR n 
2 85  GLY n 
2 86  LEU n 
2 87  LYS n 
2 88  PRO n 
2 89  GLU n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  SER n 
2 99  ASP n 
2 100 ARG n 
2 101 ASP n 
2 102 HIS n 
2 103 TYR n 
2 104 SER n 
2 105 GLY n 
2 106 THR n 
2 107 TYR n 
2 108 TYR n 
2 109 GLY n 
2 110 ARG n 
2 111 ARG n 
2 112 PHE n 
2 113 VAL n 
2 114 GLU n 
2 115 GLU n 
2 116 TYR n 
2 117 ASP n 
2 118 TYR n 
2 119 TRP n 
2 120 GLY n 
2 121 GLN n 
2 122 GLY n 
2 123 THR n 
2 124 GLN n 
2 125 VAL n 
2 126 THR n 
2 127 VAL n 
2 128 SER n 
2 129 SER n 
2 130 HIS n 
2 131 HIS n 
2 132 HIS n 
2 133 HIS n 
2 134 HIS n 
2 135 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 317 ? ? ? ? ? ? ? ? ? Norovirus       142786 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 135 ? ? ? ? ? ? ? ? ? 'Vicugna pacos' 30538  ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP K4LM89_9CALI K4LM89 ? 1 
;TKPFSVPVLTVEEMTNSRFPIPLEKLFTGPSSAFVVQPQNGRCTTDGVLLGTTQLSPVNICTFRGDVTHITGSRNYTMNL
ASQNWNDYDPTEEIPAPLGTPDFVGKIQGVLTQTTRTDGSTRGHKATVYTGSADFAPKLGRVQFETDTDRDFEANQNTKF
TPVGVIQDGGTTHRNEPQQWVLPSYSGRNTHNVHLAPAVAPTFPGEQLLFFRSTMPGCSGYPNMDLDCLLPQEWVQYFYQ
EAAPAQSDVALLRFVNPDTGRVLFECKLHKSGYVTVAHTGQHDLVIPPNGYFRFDSWVNQFYTLAPMGNGTGRRRAV
;
224 
2 PDB 8EN1         8EN1   ? 2 ? 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 8EN1 A 1 ? 317 ? K4LM89 224 ? 540 ? 224 540 
2 1 8EN1 B 1 ? 317 ? K4LM89 224 ? 540 ? 224 540 
3 2 8EN1 C 1 ? 135 ? 8EN1   1   ? 135 ? 1   135 
4 2 8EN1 D 1 ? 135 ? 8EN1   1   ? 135 ? 1   135 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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 
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 
# 
_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                   8EN1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.05 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '(0.2 M calcium chloride and 20% [w/v] PEG3350)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-10-22 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97626 
_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 ID13' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97626 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID13 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          27.700 
_reflns.entry_id                                       8EN1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.400 
_reflns.d_resolution_low                               57.750 
_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                                     34103 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.800 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.000 
_reflns.pdbx_Rmerge_I_obs                              0.167 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.500 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           605 
_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                                0.187 
_reflns.pdbx_Rpim_I_all                                0.082 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       169376 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.977 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_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.pdbx_CC_split_method                           ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_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 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_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 
2.400 2.490  ? ? 16172 ? ? ? 3538 98.700 ? ? ? ? 0.554 ? ? ? ? ? ? ? ? 4.600 ? ? ? 2.100 0.629 0.292 ? 1 1 0.748 ? ? ? ? ? ? ? ? ? 
? 
8.970 57.750 ? ? 3364  ? ? ? 693  99.000 ? ? ? ? 0.097 ? ? ? ? ? ? ? ? 4.900 ? ? ? 8.800 0.108 0.045 ? 2 1 0.985 ? ? ? ? ? ? ? ? ? 
? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                70.380 
_refine.B_iso_mean                               28.3294 
_refine.B_iso_min                                8.660 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8EN1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.4000 
_refine.ls_d_res_low                             57.7500 
_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                     34056 
_refine.ls_number_reflns_R_free                  3844 
_refine.ls_number_reflns_R_work                  61742 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.8800 
_refine.ls_percent_reflns_R_free                 5.8600 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2099 
_refine.ls_R_factor_R_free                       0.2635 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2066 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.340 
_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                      4X7E 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 27.0000 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2900 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.4000 
_refine_hist.d_res_low                        57.7500 
_refine_hist.number_atoms_solvent             273 
_refine_hist.number_atoms_total               7163 
_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       877 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          27.28 
_refine_hist.pdbx_number_atoms_protein        6890 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.4000 2.4300  2375 . 145 2230 97.0000  . . . 0.3627 0.0000 0.2973 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.4300 2.4600  2355 . 129 2226 97.0000  . . . 0.3198 0.0000 0.2732 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.4600 2.5000  2443 . 148 2295 99.0000  . . . 0.3485 0.0000 0.2672 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.5000 2.5300  2430 . 145 2285 99.0000  . . . 0.2454 0.0000 0.2634 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.5300 2.5700  2483 . 133 2350 100.0000 . . . 0.3770 0.0000 0.2659 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.5700 2.6100  2412 . 151 2261 99.0000  . . . 0.3300 0.0000 0.2621 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.6100 2.6500  2424 . 135 2289 99.0000  . . . 0.2655 0.0000 0.2680 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.6500 2.7000  2458 . 142 2316 100.0000 . . . 0.3734 0.0000 0.2629 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.7000 2.7500  2462 . 156 2306 100.0000 . . . 0.2839 0.0000 0.2681 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.7500 2.8000  2453 . 133 2320 99.0000  . . . 0.3419 0.0000 0.2481 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.8000 2.8600  2447 . 136 2311 100.0000 . . . 0.3116 0.0000 0.2517 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.8600 2.9200  2418 . 145 2273 99.0000  . . . 0.2970 0.0000 0.2466 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.9200 2.9900  2431 . 137 2294 99.0000  . . . 0.3391 0.0000 0.2478 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 2.9900 3.0600  2443 . 148 2295 99.0000  . . . 0.2401 0.0000 0.2289 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.0600 3.1400  2420 . 151 2269 97.0000  . . . 0.2710 0.0000 0.2254 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.1400 3.2400  2364 . 134 2230 97.0000  . . . 0.3016 0.0000 0.2087 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.2400 3.3400  2437 . 143 2294 100.0000 . . . 0.2513 0.0000 0.2030 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.3400 3.4600  2481 . 146 2335 100.0000 . . . 0.2605 0.0000 0.2111 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.4600 3.6000  2419 . 137 2282 100.0000 . . . 0.2464 0.0000 0.1915 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.6000 3.7600  2459 . 142 2317 99.0000  . . . 0.2562 0.0000 0.1963 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.7600 3.9600  2409 . 146 2263 99.0000  . . . 0.2187 0.0000 0.1784 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 3.9600 4.2100  2470 . 141 2329 99.0000  . . . 0.2301 0.0000 0.1635 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 4.2100 4.5300  2413 . 148 2265 98.0000  . . . 0.2218 0.0000 0.1475 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 4.5400 4.9900  2360 . 140 2220 98.0000  . . . 0.2512 0.0000 0.1480 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 4.9900 5.7100  2482 . 154 2328 99.0000  . . . 0.1873 0.0000 0.1714 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 5.7100 7.1900  2432 . 144 2288 99.0000  . . . 0.2183 0.0000 0.1839 . . . . . . . 27 . . . 
'X-RAY DIFFRACTION' 7.2000 57.7500 2406 . 135 2271 98.0000  . . . 0.2315 0.0000 0.1837 . . . . . . . 27 . . . 
# 
_struct.entry_id                     8EN1 
_struct.title                        'Structure of GII.4 norovirus in complex with Nanobody 30' 
_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        8EN1 
_struct_keywords.text            'norovirus, Nanobody, inhibitor, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
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 THR A 10  ? MET A 14  ? THR A 233 MET A 237 5 ? 5  
HELX_P HELX_P2  AA2 ALA A 136 ? LEU A 139 ? ALA A 359 LEU A 362 5 ? 4  
HELX_P HELX_P3  AA3 PRO A 231 ? ALA A 242 ? PRO A 454 ALA A 465 1 ? 12 
HELX_P HELX_P4  AA4 THR B 10  ? MET B 14  ? THR B 233 MET B 237 5 ? 5  
HELX_P HELX_P5  AA5 ALA B 136 ? LEU B 139 ? ALA B 359 LEU B 362 5 ? 4  
HELX_P HELX_P6  AA6 PRO B 231 ? ALA B 242 ? PRO B 454 ALA B 465 1 ? 12 
HELX_P HELX_P7  AA7 ASN C 74  ? LYS C 76  ? ASN C 74  LYS C 76  5 ? 3  
HELX_P HELX_P8  AA8 LYS C 87  ? THR C 91  ? LYS C 87  THR C 91  5 ? 5  
HELX_P HELX_P9  AA9 PHE C 112 ? TYR C 116 ? PHE C 112 TYR C 116 5 ? 5  
HELX_P HELX_P10 AB1 ASP D 62  ? LYS D 65  ? ASP D 62  LYS D 65  5 ? 4  
HELX_P HELX_P11 AB2 LYS D 87  ? THR D 91  ? LYS D 87  THR D 91  5 ? 5  
HELX_P HELX_P12 AB3 PHE D 112 ? TYR D 116 ? PHE D 112 TYR D 116 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? C CYS 22 SG ? ? ? 1_555 C CYS 96 SG ? ? C CYS 22 C CYS 96 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2 disulf ? ? D CYS 22 SG ? ? ? 1_555 D CYS 96 SG ? ? D CYS 22 D CYS 96 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 176 A . ? GLU 399 A PRO 177 A ? PRO 400 A 1 -2.94 
2 GLU 176 B . ? GLU 399 B PRO 177 B ? PRO 400 B 1 -0.58 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8  ? 
AA2 ? 14 ? 
AA3 ? 8  ? 
AA4 ? 4  ? 
AA5 ? 7  ? 
AA6 ? 4  ? 
AA7 ? 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  ? anti-parallel 
AA1 1  7  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 2  6  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 4  8  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 1  6  ? anti-parallel 
AA2 2  5  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 3  6  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 4  14 ? anti-parallel 
AA2 6  7  ? parallel      
AA2 7  11 ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 8  13 ? anti-parallel 
AA2 9  12 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 10 13 ? anti-parallel 
AA2 11 12 ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 1  7  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 2  6  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA3 4  8  ? anti-parallel 
AA3 5  6  ? anti-parallel 
AA4 1  2  ? anti-parallel 
AA4 2  3  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA5 1  7  ? parallel      
AA5 2  3  ? anti-parallel 
AA5 2  5  ? anti-parallel 
AA5 3  4  ? anti-parallel 
AA5 5  6  ? anti-parallel 
AA5 5  7  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA6 2  3  ? anti-parallel 
AA6 3  4  ? anti-parallel 
AA7 1  7  ? parallel      
AA7 2  3  ? anti-parallel 
AA7 2  5  ? anti-parallel 
AA7 3  4  ? anti-parallel 
AA7 5  6  ? anti-parallel 
AA7 5  7  ? anti-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  LYS A 25  ? THR A 28  ? LYS A 248 THR A 251 
AA1 2  GLN A 207 ? THR A 214 ? GLN A 430 THR A 437 
AA1 3  ASP A 225 ? CYS A 228 ? ASP A 448 CYS A 451 
AA1 4  VAL A 249 ? VAL A 255 ? VAL A 472 VAL A 478 
AA1 5  VAL A 262 ? HIS A 269 ? VAL A 485 HIS A 492 
AA1 6  TYR A 273 ? VAL A 276 ? TYR A 496 VAL A 499 
AA1 7  LEU A 284 ? ILE A 286 ? LEU A 507 ILE A 509 
AA1 8  TYR A 291 ? VAL A 298 ? TYR A 514 VAL A 521 
AA2 1  PHE A 63  ? HIS A 69  ? PHE A 286 HIS A 292 
AA2 2  ASN A 75  ? ALA A 81  ? ASN A 298 ALA A 304 
AA2 3  LYS A 106 ? THR A 114 ? LYS A 329 THR A 337 
AA2 4  THR A 121 ? TYR A 129 ? THR A 344 TYR A 352 
AA2 5  ARG A 141 ? THR A 146 ? ARG A 364 THR A 369 
AA2 6  ASN A 157 ? ILE A 166 ? ASN A 380 ILE A 389 
AA2 7  GLY A 217 ? GLY A 220 ? GLY A 440 GLY A 443 
AA2 8  PHE B 63  ? HIS B 69  ? PHE B 286 HIS B 292 
AA2 9  ASN B 75  ? ALA B 81  ? ASN B 298 ALA B 304 
AA2 10 LYS B 106 ? THR B 114 ? LYS B 329 THR B 337 
AA2 11 THR B 121 ? TYR B 129 ? THR B 344 TYR B 352 
AA2 12 ARG B 141 ? THR B 146 ? ARG B 364 THR B 369 
AA2 13 ASN B 157 ? VAL B 165 ? ASN B 380 VAL B 388 
AA2 14 SER B 219 ? GLY B 220 ? SER B 442 GLY B 443 
AA3 1  LYS B 25  ? THR B 28  ? LYS B 248 THR B 251 
AA3 2  GLN B 207 ? THR B 214 ? GLN B 430 THR B 437 
AA3 3  ASP B 225 ? CYS B 228 ? ASP B 448 CYS B 451 
AA3 4  VAL B 249 ? VAL B 255 ? VAL B 472 VAL B 478 
AA3 5  VAL B 262 ? HIS B 269 ? VAL B 485 HIS B 492 
AA3 6  TYR B 273 ? VAL B 276 ? TYR B 496 VAL B 499 
AA3 7  LEU B 284 ? ILE B 286 ? LEU B 507 ILE B 509 
AA3 8  TYR B 291 ? VAL B 298 ? TYR B 514 VAL B 521 
AA4 1  VAL C 2   ? SER C 7   ? VAL C 2   SER C 7   
AA4 2  LEU C 18  ? GLY C 26  ? LEU C 18  GLY C 26  
AA4 3  THR C 78  ? MET C 83  ? THR C 78  MET C 83  
AA4 4  THR C 69  ? ASP C 73  ? THR C 69  ASP C 73  
AA5 1  LEU C 11  ? GLN C 13  ? LEU C 11  GLN C 13  
AA5 2  LEU C 33  ? GLN C 39  ? LEU C 33  GLN C 39  
AA5 3  GLU C 46  ? ILE C 51  ? GLU C 46  ILE C 51  
AA5 4  THR C 58  ? TYR C 60  ? THR C 58  TYR C 60  
AA5 5  ALA C 92  ? ASP C 99  ? ALA C 92  ASP C 99  
AA5 6  TYR C 118 ? TRP C 119 ? TYR C 118 TRP C 119 
AA5 7  THR C 123 ? SER C 128 ? THR C 123 SER C 128 
AA6 1  VAL D 2   ? SER D 7   ? VAL D 2   SER D 7   
AA6 2  LEU D 18  ? GLY D 26  ? LEU D 18  GLY D 26  
AA6 3  THR D 78  ? MET D 83  ? THR D 78  MET D 83  
AA6 4  PHE D 68  ? ASP D 73  ? PHE D 68  ASP D 73  
AA7 1  LEU D 11  ? GLN D 13  ? LEU D 11  GLN D 13  
AA7 2  LEU D 33  ? GLN D 39  ? LEU D 33  GLN D 39  
AA7 3  GLU D 46  ? ILE D 51  ? GLU D 46  ILE D 51  
AA7 4  THR D 58  ? TYR D 60  ? THR D 58  TYR D 60  
AA7 5  ALA D 92  ? ASP D 99  ? ALA D 92  ASP D 99  
AA7 6  TYR D 118 ? TRP D 119 ? TYR D 118 TRP D 119 
AA7 7  THR D 123 ? SER D 128 ? THR D 123 SER D 128 
# 
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  N PHE A 27  ? N PHE A 250 O PHE A 210 ? O PHE A 433 
AA1 1  7  N LEU A 26  ? N LEU A 249 O ILE A 286 ? O ILE A 509 
AA1 2  3  N PHE A 211 ? N PHE A 434 O CYS A 228 ? O CYS A 451 
AA1 2  6  N LEU A 209 ? N LEU A 432 O VAL A 274 ? O VAL A 497 
AA1 4  5  N ALA A 250 ? N ALA A 473 O LEU A 268 ? O LEU A 491 
AA1 4  8  N VAL A 249 ? N VAL A 472 O VAL A 298 ? O VAL A 521 
AA1 5  6  N HIS A 269 ? N HIS A 492 O TYR A 273 ? O TYR A 496 
AA2 1  2  N ARG A 64  ? N ARG A 287 O ALA A 81  ? O ALA A 304 
AA2 1  6  N PHE A 63  ? N PHE A 286 O PHE A 160 ? O PHE A 383 
AA2 2  5  N MET A 78  ? N MET A 301 O VAL A 142 ? O VAL A 365 
AA2 3  4  N LEU A 111 ? N LEU A 334 O HIS A 124 ? O HIS A 347 
AA2 3  6  N THR A 112 ? N THR A 335 O LYS A 159 ? O LYS A 382 
AA2 4  5  N THR A 127 ? N THR A 350 O GLU A 145 ? O GLU A 368 
AA2 4  14 N THR A 121 ? N THR A 344 O GLY B 220 ? O GLY B 443 
AA2 6  7  N VAL A 165 ? N VAL A 388 O CYS A 218 ? O CYS A 441 
AA2 7  11 N GLY A 220 ? N GLY A 443 O THR B 121 ? O THR B 344 
AA2 8  9  N ARG B 64  ? N ARG B 287 O ALA B 81  ? O ALA B 304 
AA2 8  13 N GLY B 65  ? N GLY B 288 O THR B 158 ? O THR B 381 
AA2 9  12 N MET B 78  ? N MET B 301 O VAL B 142 ? O VAL B 365 
AA2 10 11 N GLY B 109 ? N GLY B 332 O ALA B 126 ? O ALA B 349 
AA2 10 13 N GLN B 108 ? N GLN B 331 O GLY B 164 ? O GLY B 387 
AA2 11 12 N THR B 127 ? N THR B 350 O GLU B 145 ? O GLU B 368 
AA3 1  2  N PHE B 27  ? N PHE B 250 O PHE B 210 ? O PHE B 433 
AA3 1  7  N LEU B 26  ? N LEU B 249 O ILE B 286 ? O ILE B 509 
AA3 2  3  N SER B 213 ? N SER B 436 O LEU B 226 ? O LEU B 449 
AA3 2  6  N LEU B 209 ? N LEU B 432 O VAL B 274 ? O VAL B 497 
AA3 4  5  N ALA B 250 ? N ALA B 473 O LEU B 268 ? O LEU B 491 
AA3 4  8  N VAL B 255 ? N VAL B 478 O TYR B 291 ? O TYR B 514 
AA3 5  6  N HIS B 269 ? N HIS B 492 O TYR B 273 ? O TYR B 496 
AA4 1  2  N GLN C 5   ? N GLN C 5   O VAL C 23  ? O VAL C 23  
AA4 2  3  N LEU C 18  ? N LEU C 18  O MET C 83  ? O MET C 83  
AA4 3  4  O TYR C 80  ? O TYR C 80  N SER C 71  ? N SER C 71  
AA5 1  7  N VAL C 12  ? N VAL C 12  O THR C 126 ? O THR C 126 
AA5 2  3  N TRP C 36  ? N TRP C 36  O ALA C 49  ? O ALA C 49  
AA5 2  5  N PHE C 37  ? N PHE C 37  O TYR C 95  ? O TYR C 95  
AA5 3  4  N SER C 50  ? N SER C 50  O THR C 59  ? O THR C 59  
AA5 5  6  N SER C 98  ? N SER C 98  O TYR C 118 ? O TYR C 118 
AA5 5  7  N TYR C 94  ? N TYR C 94  O THR C 123 ? O THR C 123 
AA6 1  2  N GLN D 5   ? N GLN D 5   O VAL D 23  ? O VAL D 23  
AA6 2  3  N LEU D 18  ? N LEU D 18  O MET D 83  ? O MET D 83  
AA6 3  4  O TYR D 80  ? O TYR D 80  N SER D 71  ? N SER D 71  
AA7 1  7  N VAL D 12  ? N VAL D 12  O SER D 128 ? O SER D 128 
AA7 2  3  N TRP D 36  ? N TRP D 36  O ALA D 49  ? O ALA D 49  
AA7 2  5  N LEU D 33  ? N LEU D 33  O ASP D 99  ? O ASP D 99  
AA7 3  4  N SER D 50  ? N SER D 50  O THR D 59  ? O THR D 59  
AA7 5  6  N SER D 98  ? N SER D 98  O TYR D 118 ? O TYR D 118 
AA7 5  7  N TYR D 94  ? N TYR D 94  O THR D 123 ? O THR D 123 
# 
_atom_sites.entry_id                    8EN1 
_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.fract_transf_matrix[1][1]   0.008491 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001687 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016015 
_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]   0.008399 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CA  ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . THR A 1 1   ? 1.018   39.238  -16.714 1.00 50.87 ?  224 THR A N   1 
ATOM   2    C CA  . THR A 1 1   ? 0.735   37.830  -16.960 1.00 50.63 ?  224 THR A CA  1 
ATOM   3    C C   . THR A 1 1   ? 0.952   37.479  -18.428 1.00 44.42 ?  224 THR A C   1 
ATOM   4    O O   . THR A 1 1   ? 0.440   38.157  -19.320 1.00 46.07 ?  224 THR A O   1 
ATOM   5    C CB  . THR A 1 1   ? -0.705  37.466  -16.555 1.00 50.88 ?  224 THR A CB  1 
ATOM   6    O OG1 . THR A 1 1   ? -1.631  38.242  -17.325 1.00 52.20 ?  224 THR A OG1 1 
ATOM   7    C CG2 . THR A 1 1   ? -0.924  37.744  -15.076 1.00 44.85 ?  224 THR A CG2 1 
ATOM   8    N N   . LYS A 1 2   ? 1.717   36.418  -18.665 1.00 42.89 ?  225 LYS A N   1 
ATOM   9    C CA  . LYS A 1 2   ? 2.022   36.005  -20.026 1.00 41.35 ?  225 LYS A CA  1 
ATOM   10   C C   . LYS A 1 2   ? 0.735   35.641  -20.764 1.00 38.95 ?  225 LYS A C   1 
ATOM   11   O O   . LYS A 1 2   ? -0.142  34.980  -20.195 1.00 36.81 ?  225 LYS A O   1 
ATOM   12   C CB  . LYS A 1 2   ? 2.981   34.813  -20.018 1.00 41.20 ?  225 LYS A CB  1 
ATOM   13   C CG  . LYS A 1 2   ? 2.985   33.997  -21.302 1.00 42.22 ?  225 LYS A CG  1 
ATOM   14   C CD  . LYS A 1 2   ? 3.692   32.665  -21.111 1.00 40.15 ?  225 LYS A CD  1 
ATOM   15   C CE  . LYS A 1 2   ? 5.202   32.833  -21.119 1.00 38.75 ?  225 LYS A CE  1 
ATOM   16   N NZ  . LYS A 1 2   ? 5.756   32.822  -22.502 1.00 39.19 ?  225 LYS A NZ  1 
ATOM   17   N N   . PRO A 1 3   ? 0.583   36.064  -22.018 1.00 38.37 ?  226 PRO A N   1 
ATOM   18   C CA  . PRO A 1 3   ? -0.633  35.724  -22.769 1.00 34.87 ?  226 PRO A CA  1 
ATOM   19   C C   . PRO A 1 3   ? -0.750  34.223  -22.991 1.00 31.83 ?  226 PRO A C   1 
ATOM   20   O O   . PRO A 1 3   ? 0.195   33.565  -23.431 1.00 34.10 ?  226 PRO A O   1 
ATOM   21   C CB  . PRO A 1 3   ? -0.460  36.480  -24.093 1.00 33.66 ?  226 PRO A CB  1 
ATOM   22   C CG  . PRO A 1 3   ? 0.998   36.796  -24.181 1.00 34.08 ?  226 PRO A CG  1 
ATOM   23   C CD  . PRO A 1 3   ? 1.475   36.957  -22.774 1.00 37.55 ?  226 PRO A CD  1 
ATOM   24   N N   . PHE A 1 4   ? -1.924  33.686  -22.673 1.00 27.38 ?  227 PHE A N   1 
ATOM   25   C CA  . PHE A 1 4   ? -2.207  32.281  -22.919 1.00 29.82 ?  227 PHE A CA  1 
ATOM   26   C C   . PHE A 1 4   ? -2.387  32.030  -24.411 1.00 30.24 ?  227 PHE A C   1 
ATOM   27   O O   . PHE A 1 4   ? -2.770  32.923  -25.172 1.00 31.96 ?  227 PHE A O   1 
ATOM   28   C CB  . PHE A 1 4   ? -3.464  31.856  -22.158 1.00 27.70 ?  227 PHE A CB  1 
ATOM   29   C CG  . PHE A 1 4   ? -3.847  30.418  -22.363 1.00 25.86 ?  227 PHE A CG  1 
ATOM   30   C CD1 . PHE A 1 4   ? -3.075  29.397  -21.834 1.00 25.76 ?  227 PHE A CD1 1 
ATOM   31   C CD2 . PHE A 1 4   ? -4.978  30.088  -23.092 1.00 24.59 ?  227 PHE A CD2 1 
ATOM   32   C CE1 . PHE A 1 4   ? -3.427  28.073  -22.024 1.00 23.69 ?  227 PHE A CE1 1 
ATOM   33   C CE2 . PHE A 1 4   ? -5.334  28.767  -23.287 1.00 24.52 ?  227 PHE A CE2 1 
ATOM   34   C CZ  . PHE A 1 4   ? -4.557  27.758  -22.753 1.00 24.58 ?  227 PHE A CZ  1 
ATOM   35   N N   . SER A 1 5   ? -2.096  30.800  -24.830 1.00 27.53 ?  228 SER A N   1 
ATOM   36   C CA  . SER A 1 5   ? -2.296  30.405  -26.218 1.00 25.91 ?  228 SER A CA  1 
ATOM   37   C C   . SER A 1 5   ? -2.296  28.885  -26.307 1.00 28.60 ?  228 SER A C   1 
ATOM   38   O O   . SER A 1 5   ? -2.028  28.181  -25.331 1.00 23.43 ?  228 SER A O   1 
ATOM   39   C CB  . SER A 1 5   ? -1.227  31.007  -27.138 1.00 24.16 ?  228 SER A CB  1 
ATOM   40   O OG  . SER A 1 5   ? 0.015   30.346  -26.987 1.00 28.06 ?  228 SER A OG  1 
ATOM   41   N N   . VAL A 1 6   ? -2.597  28.395  -27.505 1.00 26.75 ?  229 VAL A N   1 
ATOM   42   C CA  . VAL A 1 6   ? -2.755  26.970  -27.780 1.00 22.86 ?  229 VAL A CA  1 
ATOM   43   C C   . VAL A 1 6   ? -1.918  26.636  -29.012 1.00 24.18 ?  229 VAL A C   1 
ATOM   44   O O   . VAL A 1 6   ? -1.804  27.473  -29.919 1.00 21.22 ?  229 VAL A O   1 
ATOM   45   C CB  . VAL A 1 6   ? -4.242  26.620  -27.968 1.00 24.64 ?  229 VAL A CB  1 
ATOM   46   C CG1 . VAL A 1 6   ? -4.422  25.300  -28.694 1.00 26.49 ?  229 VAL A CG1 1 
ATOM   47   C CG2 . VAL A 1 6   ? -4.952  26.589  -26.618 1.00 23.31 ?  229 VAL A CG2 1 
ATOM   48   N N   . PRO A 1 7   ? -1.287  25.460  -29.076 1.00 24.87 ?  230 PRO A N   1 
ATOM   49   C CA  . PRO A 1 7   ? -0.533  25.093  -30.281 1.00 25.53 ?  230 PRO A CA  1 
ATOM   50   C C   . PRO A 1 7   ? -1.409  25.111  -31.526 1.00 22.79 ?  230 PRO A C   1 
ATOM   51   O O   . PRO A 1 7   ? -2.608  24.833  -31.474 1.00 21.70 ?  230 PRO A O   1 
ATOM   52   C CB  . PRO A 1 7   ? -0.039  23.676  -29.968 1.00 21.69 ?  230 PRO A CB  1 
ATOM   53   C CG  . PRO A 1 7   ? 0.021   23.632  -28.488 1.00 25.14 ?  230 PRO A CG  1 
ATOM   54   C CD  . PRO A 1 7   ? -1.151  24.441  -28.020 1.00 20.87 ?  230 PRO A CD  1 
ATOM   55   N N   . VAL A 1 8   ? -0.791  25.446  -32.660 1.00 21.71 ?  231 VAL A N   1 
ATOM   56   C CA  . VAL A 1 8   ? -1.511  25.570  -33.922 1.00 23.44 ?  231 VAL A CA  1 
ATOM   57   C C   . VAL A 1 8   ? -1.370  24.323  -34.788 1.00 24.07 ?  231 VAL A C   1 
ATOM   58   O O   . VAL A 1 8   ? -1.747  24.346  -35.963 1.00 26.93 ?  231 VAL A O   1 
ATOM   59   C CB  . VAL A 1 8   ? -1.066  26.820  -34.697 1.00 27.22 ?  231 VAL A CB  1 
ATOM   60   C CG1 . VAL A 1 8   ? -1.296  28.069  -33.863 1.00 23.98 ?  231 VAL A CG1 1 
ATOM   61   C CG2 . VAL A 1 8   ? 0.390   26.702  -35.105 1.00 24.61 ?  231 VAL A CG2 1 
ATOM   62   N N   . LEU A 1 9   ? -0.830  23.237  -34.240 1.00 24.19 ?  232 LEU A N   1 
ATOM   63   C CA  . LEU A 1 9   ? -0.811  21.977  -34.969 1.00 25.63 ?  232 LEU A CA  1 
ATOM   64   C C   . LEU A 1 9   ? -2.235  21.488  -35.194 1.00 23.03 ?  232 LEU A C   1 
ATOM   65   O O   . LEU A 1 9   ? -3.097  21.618  -34.322 1.00 24.27 ?  232 LEU A O   1 
ATOM   66   C CB  . LEU A 1 9   ? -0.018  20.921  -34.196 1.00 25.33 ?  232 LEU A CB  1 
ATOM   67   C CG  . LEU A 1 9   ? 1.486   21.116  -33.997 1.00 25.38 ?  232 LEU A CG  1 
ATOM   68   C CD1 . LEU A 1 9   ? 2.025   20.104  -32.994 1.00 24.15 ?  232 LEU A CD1 1 
ATOM   69   C CD2 . LEU A 1 9   ? 2.223   21.007  -35.321 1.00 22.67 ?  232 LEU A CD2 1 
ATOM   70   N N   . THR A 1 10  ? -2.486  20.929  -36.374 1.00 20.90 ?  233 THR A N   1 
ATOM   71   C CA  . THR A 1 10  ? -3.773  20.293  -36.590 1.00 23.03 ?  233 THR A CA  1 
ATOM   72   C C   . THR A 1 10  ? -3.856  19.009  -35.770 1.00 21.13 ?  233 THR A C   1 
ATOM   73   O O   . THR A 1 10  ? -2.841  18.432  -35.366 1.00 20.50 ?  233 THR A O   1 
ATOM   74   C CB  . THR A 1 10  ? -4.001  19.990  -38.074 1.00 24.49 ?  233 THR A CB  1 
ATOM   75   O OG1 . THR A 1 10  ? -3.080  18.984  -38.511 1.00 22.65 ?  233 THR A OG1 1 
ATOM   76   C CG2 . THR A 1 10  ? -3.810  21.247  -38.914 1.00 22.31 ?  233 THR A CG2 1 
ATOM   77   N N   . VAL A 1 11  ? -5.092  18.576  -35.506 1.00 21.01 ?  234 VAL A N   1 
ATOM   78   C CA  . VAL A 1 11  ? -5.311  17.331  -34.771 1.00 19.24 ?  234 VAL A CA  1 
ATOM   79   C C   . VAL A 1 11  ? -4.565  16.188  -35.442 1.00 18.56 ?  234 VAL A C   1 
ATOM   80   O O   . VAL A 1 11  ? -3.931  15.357  -34.779 1.00 20.34 ?  234 VAL A O   1 
ATOM   81   C CB  . VAL A 1 11  ? -6.820  17.036  -34.663 1.00 19.34 ?  234 VAL A CB  1 
ATOM   82   C CG1 . VAL A 1 11  ? -7.055  15.621  -34.157 1.00 17.09 ?  234 VAL A CG1 1 
ATOM   83   C CG2 . VAL A 1 11  ? -7.503  18.058  -33.764 1.00 19.98 ?  234 VAL A CG2 1 
ATOM   84   N N   . GLU A 1 12  ? -4.608  16.151  -36.775 1.00 19.54 ?  235 GLU A N   1 
ATOM   85   C CA  . GLU A 1 12  ? -3.907  15.140  -37.556 1.00 21.62 ?  235 GLU A CA  1 
ATOM   86   C C   . GLU A 1 12  ? -2.403  15.139  -37.300 1.00 20.65 ?  235 GLU A C   1 
ATOM   87   O O   . GLU A 1 12  ? -1.748  14.115  -37.523 1.00 22.45 ?  235 GLU A O   1 
ATOM   88   C CB  . GLU A 1 12  ? -4.201  15.382  -39.038 1.00 22.48 ?  235 GLU A CB  1 
ATOM   89   C CG  . GLU A 1 12  ? -3.742  14.306  -39.998 1.00 23.07 ?  235 GLU A CG  1 
ATOM   90   C CD  . GLU A 1 12  ? -4.395  14.459  -41.359 1.00 21.95 ?  235 GLU A CD  1 
ATOM   91   O OE1 . GLU A 1 12  ? -4.579  15.614  -41.799 1.00 26.96 ?  235 GLU A OE1 1 
ATOM   92   O OE2 . GLU A 1 12  ? -4.725  13.432  -41.987 1.00 23.98 -1 235 GLU A OE2 1 
ATOM   93   N N   . GLU A 1 13  ? -1.844  16.253  -36.828 1.00 19.80 ?  236 GLU A N   1 
ATOM   94   C CA  . GLU A 1 13  ? -0.409  16.390  -36.614 1.00 20.54 ?  236 GLU A CA  1 
ATOM   95   C C   . GLU A 1 13  ? 0.002   16.181  -35.161 1.00 23.04 ?  236 GLU A C   1 
ATOM   96   O O   . GLU A 1 13  ? 1.165   16.418  -34.821 1.00 22.58 ?  236 GLU A O   1 
ATOM   97   C CB  . GLU A 1 13  ? 0.063   17.769  -37.080 1.00 22.41 ?  236 GLU A CB  1 
ATOM   98   C CG  . GLU A 1 13  ? -0.072  18.021  -38.571 1.00 23.87 ?  236 GLU A CG  1 
ATOM   99   C CD  . GLU A 1 13  ? -0.142  19.502  -38.900 1.00 25.56 ?  236 GLU A CD  1 
ATOM   100  O OE1 . GLU A 1 13  ? -0.344  20.310  -37.967 1.00 25.90 ?  236 GLU A OE1 1 
ATOM   101  O OE2 . GLU A 1 13  ? 0.002   19.859  -40.088 1.00 26.72 -1 236 GLU A OE2 1 
ATOM   102  N N   . MET A 1 14  ? -0.912  15.750  -34.298 1.00 20.16 ?  237 MET A N   1 
ATOM   103  C CA  . MET A 1 14  ? -0.642  15.667  -32.871 1.00 21.17 ?  237 MET A CA  1 
ATOM   104  C C   . MET A 1 14  ? -0.780  14.229  -32.383 1.00 22.78 ?  237 MET A C   1 
ATOM   105  O O   . MET A 1 14  ? -1.240  13.339  -33.104 1.00 22.21 ?  237 MET A O   1 
ATOM   106  C CB  . MET A 1 14  ? -1.567  16.607  -32.088 1.00 20.38 ?  237 MET A CB  1 
ATOM   107  C CG  . MET A 1 14  ? -1.115  18.060  -32.146 1.00 20.77 ?  237 MET A CG  1 
ATOM   108  S SD  . MET A 1 14  ? -2.084  19.181  -31.121 1.00 19.71 ?  237 MET A SD  1 
ATOM   109  C CE  . MET A 1 14  ? -3.688  19.062  -31.906 1.00 18.04 ?  237 MET A CE  1 
ATOM   110  N N   . THR A 1 15  ? -0.372  14.014  -31.134 1.00 19.68 ?  238 THR A N   1 
ATOM   111  C CA  . THR A 1 15  ? -0.206  12.682  -30.571 1.00 18.54 ?  238 THR A CA  1 
ATOM   112  C C   . THR A 1 15  ? -1.184  12.446  -29.429 1.00 20.49 ?  238 THR A C   1 
ATOM   113  O O   . THR A 1 15  ? -1.410  13.331  -28.597 1.00 18.42 ?  238 THR A O   1 
ATOM   114  C CB  . THR A 1 15  ? 1.227   12.480  -30.060 1.00 18.59 ?  238 THR A CB  1 
ATOM   115  O OG1 . THR A 1 15  ? 2.156   13.015  -31.010 1.00 19.54 ?  238 THR A OG1 1 
ATOM   116  C CG2 . THR A 1 15  ? 1.520   11.002  -29.844 1.00 20.20 ?  238 THR A CG2 1 
ATOM   117  N N   . ASN A 1 16  ? -1.758  11.245  -29.400 1.00 21.09 ?  239 ASN A N   1 
ATOM   118  C CA  . ASN A 1 16  ? -2.528  10.804  -28.246 1.00 20.40 ?  239 ASN A CA  1 
ATOM   119  C C   . ASN A 1 16  ? -1.653  10.836  -26.999 1.00 16.52 ?  239 ASN A C   1 
ATOM   120  O O   . ASN A 1 16  ? -0.472  10.479  -27.040 1.00 19.64 ?  239 ASN A O   1 
ATOM   121  C CB  . ASN A 1 16  ? -3.069  9.392   -28.483 1.00 19.84 ?  239 ASN A CB  1 
ATOM   122  C CG  . ASN A 1 16  ? -4.197  9.026   -27.536 1.00 20.20 ?  239 ASN A CG  1 
ATOM   123  O OD1 . ASN A 1 16  ? -4.015  8.992   -26.319 1.00 24.37 ?  239 ASN A OD1 1 
ATOM   124  N ND2 . ASN A 1 16  ? -5.368  8.737   -28.093 1.00 21.29 ?  239 ASN A ND2 1 
ATOM   125  N N   . SER A 1 17  ? -2.234  11.275  -25.887 1.00 18.14 ?  240 SER A N   1 
ATOM   126  C CA  . SER A 1 17  ? -1.499  11.425  -24.640 1.00 19.59 ?  240 SER A CA  1 
ATOM   127  C C   . SER A 1 17  ? -1.637  10.222  -23.716 1.00 20.67 ?  240 SER A C   1 
ATOM   128  O O   . SER A 1 17  ? -1.055  10.228  -22.626 1.00 16.20 ?  240 SER A O   1 
ATOM   129  C CB  . SER A 1 17  ? -1.953  12.692  -23.910 1.00 17.58 ?  240 SER A CB  1 
ATOM   130  O OG  . SER A 1 17  ? -3.342  12.653  -23.633 1.00 19.99 ?  240 SER A OG  1 
ATOM   131  N N   . ARG A 1 18  ? -2.384  9.194   -24.120 1.00 17.64 ?  241 ARG A N   1 
ATOM   132  C CA  . ARG A 1 18  ? -2.543  7.991   -23.315 1.00 17.51 ?  241 ARG A CA  1 
ATOM   133  C C   . ARG A 1 18  ? -1.930  6.751   -23.952 1.00 20.82 ?  241 ARG A C   1 
ATOM   134  O O   . ARG A 1 18  ? -1.933  5.689   -23.321 1.00 22.25 ?  241 ARG A O   1 
ATOM   135  C CB  . ARG A 1 18  ? -4.031  7.738   -23.033 1.00 18.09 ?  241 ARG A CB  1 
ATOM   136  C CG  . ARG A 1 18  ? -4.696  8.860   -22.251 1.00 19.21 ?  241 ARG A CG  1 
ATOM   137  C CD  . ARG A 1 18  ? -6.182  8.616   -22.058 1.00 18.47 ?  241 ARG A CD  1 
ATOM   138  N NE  . ARG A 1 18  ? -6.450  7.378   -21.335 1.00 18.96 ?  241 ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 18  ? -7.563  6.668   -21.456 1.00 19.14 ?  241 ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 18  ? -8.543  7.049   -22.258 1.00 21.10 ?  241 ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 18  ? -7.696  5.546   -20.754 1.00 19.17 ?  241 ARG A NH2 1 
ATOM   142  N N   . PHE A 1 19  ? -1.402  6.861   -25.177 1.00 19.43 ?  242 PHE A N   1 
ATOM   143  C CA  . PHE A 1 19  ? -0.742  5.774   -25.889 1.00 17.08 ?  242 PHE A CA  1 
ATOM   144  C C   . PHE A 1 19  ? 0.071   6.397   -27.008 1.00 19.40 ?  242 PHE A C   1 
ATOM   145  O O   . PHE A 1 19  ? -0.421  7.326   -27.664 1.00 20.88 ?  242 PHE A O   1 
ATOM   146  C CB  . PHE A 1 19  ? -1.756  4.774   -26.456 1.00 17.80 ?  242 PHE A CB  1 
ATOM   147  C CG  . PHE A 1 19  ? -1.211  3.389   -26.651 1.00 18.75 ?  242 PHE A CG  1 
ATOM   148  C CD1 . PHE A 1 19  ? -1.193  2.484   -25.602 1.00 18.70 ?  242 PHE A CD1 1 
ATOM   149  C CD2 . PHE A 1 19  ? -0.745  2.981   -27.890 1.00 22.61 ?  242 PHE A CD2 1 
ATOM   150  C CE1 . PHE A 1 19  ? -0.702  1.205   -25.780 1.00 19.87 ?  242 PHE A CE1 1 
ATOM   151  C CE2 . PHE A 1 19  ? -0.253  1.703   -28.074 1.00 19.97 ?  242 PHE A CE2 1 
ATOM   152  C CZ  . PHE A 1 19  ? -0.232  0.814   -27.018 1.00 18.17 ?  242 PHE A CZ  1 
ATOM   153  N N   . PRO A 1 20  ? 1.297   5.932   -27.258 1.00 18.87 ?  243 PRO A N   1 
ATOM   154  C CA  . PRO A 1 20  ? 2.148   6.591   -28.263 1.00 20.40 ?  243 PRO A CA  1 
ATOM   155  C C   . PRO A 1 20  ? 1.697   6.338   -29.694 1.00 21.09 ?  243 PRO A C   1 
ATOM   156  O O   . PRO A 1 20  ? 2.356   5.612   -30.445 1.00 21.41 ?  243 PRO A O   1 
ATOM   157  C CB  . PRO A 1 20  ? 3.534   5.989   -27.999 1.00 20.79 ?  243 PRO A CB  1 
ATOM   158  C CG  . PRO A 1 20  ? 3.268   4.680   -27.336 1.00 20.85 ?  243 PRO A CG  1 
ATOM   159  C CD  . PRO A 1 20  ? 1.980   4.817   -26.578 1.00 19.94 ?  243 PRO A CD  1 
ATOM   160  N N   . ILE A 1 21  ? 0.576   6.940   -30.079 1.00 20.27 ?  244 ILE A N   1 
ATOM   161  C CA  . ILE A 1 21  ? 0.066   6.867   -31.448 1.00 22.44 ?  244 ILE A CA  1 
ATOM   162  C C   . ILE A 1 21  ? -0.505  8.223   -31.828 1.00 22.19 ?  244 ILE A C   1 
ATOM   163  O O   . ILE A 1 21  ? -0.898  9.014   -30.959 1.00 19.72 ?  244 ILE A O   1 
ATOM   164  C CB  . ILE A 1 21  ? -1.011  5.773   -31.607 1.00 23.25 ?  244 ILE A CB  1 
ATOM   165  C CG1 . ILE A 1 21  ? -2.058  5.877   -30.497 1.00 22.15 ?  244 ILE A CG1 1 
ATOM   166  C CG2 . ILE A 1 21  ? -0.373  4.387   -31.645 1.00 19.48 ?  244 ILE A CG2 1 
ATOM   167  C CD1 . ILE A 1 21  ? -2.953  4.663   -30.395 1.00 19.58 ?  244 ILE A CD1 1 
ATOM   168  N N   . PRO A 1 22  ? -0.551  8.529   -33.124 1.00 21.54 ?  245 PRO A N   1 
ATOM   169  C CA  . PRO A 1 22  ? -1.076  9.831   -33.546 1.00 23.14 ?  245 PRO A CA  1 
ATOM   170  C C   . PRO A 1 22  ? -2.576  9.928   -33.324 1.00 22.03 ?  245 PRO A C   1 
ATOM   171  O O   . PRO A 1 22  ? -3.298  8.930   -33.275 1.00 24.56 ?  245 PRO A O   1 
ATOM   172  C CB  . PRO A 1 22  ? -0.737  9.899   -35.042 1.00 20.64 ?  245 PRO A CB  1 
ATOM   173  C CG  . PRO A 1 22  ? 0.148   8.732   -35.319 1.00 22.23 ?  245 PRO A CG  1 
ATOM   174  C CD  . PRO A 1 22  ? -0.133  7.711   -34.275 1.00 21.99 ?  245 PRO A CD  1 
ATOM   175  N N   . LEU A 1 23  ? -3.040  11.166  -33.179 1.00 19.12 ?  246 LEU A N   1 
ATOM   176  C CA  . LEU A 1 23  ? -4.470  11.419  -33.124 1.00 20.69 ?  246 LEU A CA  1 
ATOM   177  C C   . LEU A 1 23  ? -5.082  11.255  -34.509 1.00 19.58 ?  246 LEU A C   1 
ATOM   178  O O   . LEU A 1 23  ? -4.451  11.540  -35.530 1.00 20.93 ?  246 LEU A O   1 
ATOM   179  C CB  . LEU A 1 23  ? -4.748  12.822  -32.586 1.00 18.89 ?  246 LEU A CB  1 
ATOM   180  C CG  . LEU A 1 23  ? -4.413  13.054  -31.111 1.00 19.28 ?  246 LEU A CG  1 
ATOM   181  C CD1 . LEU A 1 23  ? -4.576  14.521  -30.742 1.00 18.58 ?  246 LEU A CD1 1 
ATOM   182  C CD2 . LEU A 1 23  ? -5.277  12.174  -30.221 1.00 18.80 ?  246 LEU A CD2 1 
ATOM   183  N N   . GLU A 1 24  ? -6.328  10.780  -34.541 1.00 20.78 ?  247 GLU A N   1 
ATOM   184  C CA  . GLU A 1 24  ? -7.005  10.504  -35.798 1.00 19.25 ?  247 GLU A CA  1 
ATOM   185  C C   . GLU A 1 24  ? -8.302  11.271  -36.000 1.00 20.50 ?  247 GLU A C   1 
ATOM   186  O O   . GLU A 1 24  ? -8.721  11.428  -37.151 1.00 19.63 ?  247 GLU A O   1 
ATOM   187  C CB  . GLU A 1 24  ? -7.308  9.002   -35.932 1.00 17.38 ?  247 GLU A CB  1 
ATOM   188  C CG  . GLU A 1 24  ? -6.275  8.095   -35.294 1.00 22.29 ?  247 GLU A CG  1 
ATOM   189  C CD  . GLU A 1 24  ? -6.710  6.644   -35.282 1.00 24.76 ?  247 GLU A CD  1 
ATOM   190  O OE1 . GLU A 1 24  ? -7.933  6.390   -35.276 1.00 22.85 ?  247 GLU A OE1 1 
ATOM   191  O OE2 . GLU A 1 24  ? -5.830  5.758   -35.279 1.00 24.94 -1 247 GLU A OE2 1 
ATOM   192  N N   . LYS A 1 25  ? -8.947  11.743  -34.936 1.00 20.72 ?  248 LYS A N   1 
ATOM   193  C CA  . LYS A 1 25  ? -10.226 12.431  -35.058 1.00 19.44 ?  248 LYS A CA  1 
ATOM   194  C C   . LYS A 1 25  ? -10.610 12.994  -33.698 1.00 19.67 ?  248 LYS A C   1 
ATOM   195  O O   . LYS A 1 25  ? -9.935  12.761  -32.691 1.00 18.73 ?  248 LYS A O   1 
ATOM   196  C CB  . LYS A 1 25  ? -11.324 11.498  -35.579 1.00 19.67 ?  248 LYS A CB  1 
ATOM   197  C CG  . LYS A 1 25  ? -11.450 10.193  -34.810 1.00 21.27 ?  248 LYS A CG  1 
ATOM   198  C CD  . LYS A 1 25  ? -11.577 9.013   -35.757 1.00 20.16 ?  248 LYS A CD  1 
ATOM   199  C CE  . LYS A 1 25  ? -12.001 7.757   -35.020 1.00 21.52 ?  248 LYS A CE  1 
ATOM   200  N NZ  . LYS A 1 25  ? -12.077 6.589   -35.941 1.00 17.62 ?  248 LYS A NZ  1 
ATOM   201  N N   . LEU A 1 26  ? -11.706 13.746  -33.685 1.00 19.28 ?  249 LEU A N   1 
ATOM   202  C CA  . LEU A 1 26  ? -12.340 14.204  -32.461 1.00 19.59 ?  249 LEU A CA  1 
ATOM   203  C C   . LEU A 1 26  ? -13.622 13.418  -32.224 1.00 21.55 ?  249 LEU A C   1 
ATOM   204  O O   . LEU A 1 26  ? -14.222 12.867  -33.151 1.00 18.88 ?  249 LEU A O   1 
ATOM   205  C CB  . LEU A 1 26  ? -12.641 15.706  -32.514 1.00 17.82 ?  249 LEU A CB  1 
ATOM   206  C CG  . LEU A 1 26  ? -11.437 16.622  -32.733 1.00 17.92 ?  249 LEU A CG  1 
ATOM   207  C CD1 . LEU A 1 26  ? -11.888 18.030  -33.084 1.00 18.77 ?  249 LEU A CD1 1 
ATOM   208  C CD2 . LEU A 1 26  ? -10.550 16.631  -31.499 1.00 17.35 ?  249 LEU A CD2 1 
ATOM   209  N N   . PHE A 1 27  ? -14.035 13.372  -30.962 1.00 19.64 ?  250 PHE A N   1 
ATOM   210  C CA  . PHE A 1 27  ? -15.187 12.578  -30.563 1.00 18.87 ?  250 PHE A CA  1 
ATOM   211  C C   . PHE A 1 27  ? -15.908 13.298  -29.435 1.00 20.63 ?  250 PHE A C   1 
ATOM   212  O O   . PHE A 1 27  ? -15.266 13.778  -28.497 1.00 24.18 ?  250 PHE A O   1 
ATOM   213  C CB  . PHE A 1 27  ? -14.749 11.176  -30.120 1.00 17.54 ?  250 PHE A CB  1 
ATOM   214  C CG  . PHE A 1 27  ? -15.879 10.288  -29.673 1.00 20.35 ?  250 PHE A CG  1 
ATOM   215  C CD1 . PHE A 1 27  ? -16.350 10.341  -28.369 1.00 21.44 ?  250 PHE A CD1 1 
ATOM   216  C CD2 . PHE A 1 27  ? -16.451 9.381   -30.549 1.00 20.56 ?  250 PHE A CD2 1 
ATOM   217  C CE1 . PHE A 1 27  ? -17.379 9.522   -27.955 1.00 23.36 ?  250 PHE A CE1 1 
ATOM   218  C CE2 . PHE A 1 27  ? -17.478 8.558   -30.139 1.00 19.64 ?  250 PHE A CE2 1 
ATOM   219  C CZ  . PHE A 1 27  ? -17.941 8.628   -28.839 1.00 20.92 ?  250 PHE A CZ  1 
ATOM   220  N N   . THR A 1 28  ? -17.232 13.375  -29.534 1.00 19.18 ?  251 THR A N   1 
ATOM   221  C CA  . THR A 1 28  ? -18.058 13.857  -28.439 1.00 20.29 ?  251 THR A CA  1 
ATOM   222  C C   . THR A 1 28  ? -19.303 12.989  -28.352 1.00 21.50 ?  251 THR A C   1 
ATOM   223  O O   . THR A 1 28  ? -19.784 12.458  -29.357 1.00 20.29 ?  251 THR A O   1 
ATOM   224  C CB  . THR A 1 28  ? -18.452 15.333  -28.604 1.00 22.84 ?  251 THR A CB  1 
ATOM   225  O OG1 . THR A 1 28  ? -19.340 15.713  -27.545 1.00 21.64 ?  251 THR A OG1 1 
ATOM   226  C CG2 . THR A 1 28  ? -19.138 15.561  -29.941 1.00 22.20 ?  251 THR A CG2 1 
ATOM   227  N N   . GLY A 1 29  ? -19.811 12.842  -27.135 1.00 23.17 ?  252 GLY A N   1 
ATOM   228  C CA  . GLY A 1 29  ? -20.962 12.013  -26.881 1.00 23.69 ?  252 GLY A CA  1 
ATOM   229  C C   . GLY A 1 29  ? -21.213 11.882  -25.396 1.00 21.99 ?  252 GLY A C   1 
ATOM   230  O O   . GLY A 1 29  ? -20.456 12.399  -24.569 1.00 22.80 ?  252 GLY A O   1 
ATOM   231  N N   . PRO A 1 30  ? -22.286 11.188  -25.025 1.00 24.60 ?  253 PRO A N   1 
ATOM   232  C CA  . PRO A 1 30  ? -22.580 11.003  -23.599 1.00 27.61 ?  253 PRO A CA  1 
ATOM   233  C C   . PRO A 1 30  ? -21.575 10.058  -22.956 1.00 26.24 ?  253 PRO A C   1 
ATOM   234  O O   . PRO A 1 30  ? -21.292 8.978   -23.479 1.00 30.49 ?  253 PRO A O   1 
ATOM   235  C CB  . PRO A 1 30  ? -23.994 10.411  -23.599 1.00 28.86 ?  253 PRO A CB  1 
ATOM   236  C CG  . PRO A 1 30  ? -24.124 9.747   -24.928 1.00 28.08 ?  253 PRO A CG  1 
ATOM   237  C CD  . PRO A 1 30  ? -23.276 10.527  -25.894 1.00 25.95 ?  253 PRO A CD  1 
ATOM   238  N N   . SER A 1 31  ? -21.022 10.487  -21.821 1.00 26.05 ?  254 SER A N   1 
ATOM   239  C CA  . SER A 1 31  ? -20.161 9.646   -20.998 1.00 29.45 ?  254 SER A CA  1 
ATOM   240  C C   . SER A 1 31  ? -20.762 9.424   -19.616 1.00 30.93 ?  254 SER A C   1 
ATOM   241  O O   . SER A 1 31  ? -20.030 9.160   -18.657 1.00 30.49 ?  254 SER A O   1 
ATOM   242  C CB  . SER A 1 31  ? -18.761 10.255  -20.879 1.00 25.31 ?  254 SER A CB  1 
ATOM   243  O OG  . SER A 1 31  ? -18.810 11.542  -20.289 1.00 27.69 ?  254 SER A OG  1 
ATOM   244  N N   . SER A 1 32  ? -22.090 9.524   -19.502 1.00 34.78 ?  255 SER A N   1 
ATOM   245  C CA  . SER A 1 32  ? -22.745 9.432   -18.201 1.00 36.16 ?  255 SER A CA  1 
ATOM   246  C C   . SER A 1 32  ? -22.550 8.064   -17.561 1.00 30.13 ?  255 SER A C   1 
ATOM   247  O O   . SER A 1 32  ? -22.528 7.953   -16.330 1.00 35.04 ?  255 SER A O   1 
ATOM   248  C CB  . SER A 1 32  ? -24.237 9.737   -18.347 1.00 34.44 ?  255 SER A CB  1 
ATOM   249  O OG  . SER A 1 32  ? -24.452 11.066  -18.788 1.00 37.08 ?  255 SER A OG  1 
ATOM   250  N N   . ALA A 1 33  ? -22.406 7.015   -18.371 1.00 30.28 ?  256 ALA A N   1 
ATOM   251  C CA  . ALA A 1 33  ? -22.279 5.661   -17.849 1.00 30.71 ?  256 ALA A CA  1 
ATOM   252  C C   . ALA A 1 33  ? -20.883 5.344   -17.329 1.00 30.78 ?  256 ALA A C   1 
ATOM   253  O O   . ALA A 1 33  ? -20.697 4.286   -16.717 1.00 32.79 ?  256 ALA A O   1 
ATOM   254  C CB  . ALA A 1 33  ? -22.664 4.645   -18.927 1.00 25.92 ?  256 ALA A CB  1 
ATOM   255  N N   . PHE A 1 34  ? -19.906 6.219   -17.548 1.00 29.47 ?  257 PHE A N   1 
ATOM   256  C CA  . PHE A 1 34  ? -18.533 5.974   -17.138 1.00 26.95 ?  257 PHE A CA  1 
ATOM   257  C C   . PHE A 1 34  ? -18.079 7.019   -16.128 1.00 24.75 ?  257 PHE A C   1 
ATOM   258  O O   . PHE A 1 34  ? -18.652 8.107   -16.021 1.00 26.79 ?  257 PHE A O   1 
ATOM   259  C CB  . PHE A 1 34  ? -17.573 6.000   -18.337 1.00 27.36 ?  257 PHE A CB  1 
ATOM   260  C CG  . PHE A 1 34  ? -17.971 5.093   -19.460 1.00 28.58 ?  257 PHE A CG  1 
ATOM   261  C CD1 . PHE A 1 34  ? -17.969 3.718   -19.296 1.00 29.64 ?  257 PHE A CD1 1 
ATOM   262  C CD2 . PHE A 1 34  ? -18.343 5.617   -20.688 1.00 30.31 ?  257 PHE A CD2 1 
ATOM   263  C CE1 . PHE A 1 34  ? -18.334 2.882   -20.335 1.00 32.48 ?  257 PHE A CE1 1 
ATOM   264  C CE2 . PHE A 1 34  ? -18.709 4.788   -21.730 1.00 33.16 ?  257 PHE A CE2 1 
ATOM   265  C CZ  . PHE A 1 34  ? -18.705 3.418   -21.554 1.00 33.71 ?  257 PHE A CZ  1 
ATOM   266  N N   . VAL A 1 35  ? -17.036 6.665   -15.385 1.00 19.71 ?  258 VAL A N   1 
ATOM   267  C CA  . VAL A 1 35  ? -16.234 7.636   -14.652 1.00 22.36 ?  258 VAL A CA  1 
ATOM   268  C C   . VAL A 1 35  ? -15.035 7.962   -15.535 1.00 24.22 ?  258 VAL A C   1 
ATOM   269  O O   . VAL A 1 35  ? -14.163 7.116   -15.750 1.00 25.92 ?  258 VAL A O   1 
ATOM   270  C CB  . VAL A 1 35  ? -15.792 7.103   -13.285 1.00 22.09 ?  258 VAL A CB  1 
ATOM   271  C CG1 . VAL A 1 35  ? -15.237 8.235   -12.429 1.00 22.92 ?  258 VAL A CG1 1 
ATOM   272  C CG2 . VAL A 1 35  ? -16.949 6.417   -12.580 1.00 17.10 ?  258 VAL A CG2 1 
ATOM   273  N N   . VAL A 1 36  ? -15.003 9.180   -16.069 1.00 20.25 ?  259 VAL A N   1 
ATOM   274  C CA  . VAL A 1 36  ? -13.926 9.606   -16.963 1.00 22.24 ?  259 VAL A CA  1 
ATOM   275  C C   . VAL A 1 36  ? -12.823 10.165  -16.069 1.00 22.94 ?  259 VAL A C   1 
ATOM   276  O O   . VAL A 1 36  ? -12.819 11.342  -15.708 1.00 23.21 ?  259 VAL A O   1 
ATOM   277  C CB  . VAL A 1 36  ? -14.407 10.616  -18.001 1.00 21.81 ?  259 VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 36  ? -13.254 11.038  -18.898 1.00 20.72 ?  259 VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 36  ? -15.543 10.027  -18.824 1.00 19.94 ?  259 VAL A CG2 1 
ATOM   280  N N   . GLN A 1 37  ? -11.872 9.304   -15.707 1.00 22.90 ?  260 GLN A N   1 
ATOM   281  C CA  . GLN A 1 37  ? -10.772 9.680   -14.817 1.00 22.52 ?  260 GLN A CA  1 
ATOM   282  C C   . GLN A 1 37  ? -9.451  9.125   -15.342 1.00 22.28 ?  260 GLN A C   1 
ATOM   283  O O   . GLN A 1 37  ? -8.791  8.320   -14.679 1.00 20.28 ?  260 GLN A O   1 
ATOM   284  C CB  . GLN A 1 37  ? -11.048 9.189   -13.396 1.00 20.52 ?  260 GLN A CB  1 
ATOM   285  C CG  . GLN A 1 37  ? -10.275 9.921   -12.312 1.00 25.12 ?  260 GLN A CG  1 
ATOM   286  C CD  . GLN A 1 37  ? -10.771 9.589   -10.916 1.00 22.39 ?  260 GLN A CD  1 
ATOM   287  O OE1 . GLN A 1 37  ? -11.324 8.515   -10.679 1.00 23.64 ?  260 GLN A OE1 1 
ATOM   288  N NE2 . GLN A 1 37  ? -10.574 10.513  -9.984  1.00 22.97 ?  260 GLN A NE2 1 
ATOM   289  N N   . PRO A 1 38  ? -9.023  9.548   -16.532 1.00 22.28 ?  261 PRO A N   1 
ATOM   290  C CA  . PRO A 1 38  ? -7.712  9.113   -17.022 1.00 21.11 ?  261 PRO A CA  1 
ATOM   291  C C   . PRO A 1 38  ? -6.599  9.799   -16.248 1.00 19.44 ?  261 PRO A C   1 
ATOM   292  O O   . PRO A 1 38  ? -6.749  10.923  -15.763 1.00 17.78 ?  261 PRO A O   1 
ATOM   293  C CB  . PRO A 1 38  ? -7.718  9.542   -18.492 1.00 16.95 ?  261 PRO A CB  1 
ATOM   294  C CG  . PRO A 1 38  ? -8.625  10.716  -18.524 1.00 20.66 ?  261 PRO A CG  1 
ATOM   295  C CD  . PRO A 1 38  ? -9.675  10.481  -17.470 1.00 19.41 ?  261 PRO A CD  1 
ATOM   296  N N   . GLN A 1 39  ? -5.473  9.101   -16.122 1.00 19.53 ?  262 GLN A N   1 
ATOM   297  C CA  . GLN A 1 39  ? -4.334  9.624   -15.378 1.00 19.05 ?  262 GLN A CA  1 
ATOM   298  C C   . GLN A 1 39  ? -3.244  10.196  -16.271 1.00 18.76 ?  262 GLN A C   1 
ATOM   299  O O   . GLN A 1 39  ? -2.526  11.106  -15.845 1.00 18.12 ?  262 GLN A O   1 
ATOM   300  C CB  . GLN A 1 39  ? -3.737  8.533   -14.482 1.00 17.78 ?  262 GLN A CB  1 
ATOM   301  C CG  . GLN A 1 39  ? -4.683  8.052   -13.395 1.00 15.83 ?  262 GLN A CG  1 
ATOM   302  C CD  . GLN A 1 39  ? -5.428  9.191   -12.724 1.00 18.72 ?  262 GLN A CD  1 
ATOM   303  O OE1 . GLN A 1 39  ? -4.821  10.078  -12.123 1.00 22.02 ?  262 GLN A OE1 1 
ATOM   304  N NE2 . GLN A 1 39  ? -6.752  9.172   -12.825 1.00 22.21 ?  262 GLN A NE2 1 
ATOM   305  N N   . ASN A 1 40  ? -3.102  9.690   -17.490 1.00 18.76 ?  263 ASN A N   1 
ATOM   306  C CA  . ASN A 1 40  ? -2.169  10.260  -18.448 1.00 19.84 ?  263 ASN A CA  1 
ATOM   307  C C   . ASN A 1 40  ? -2.866  11.335  -19.272 1.00 19.17 ?  263 ASN A C   1 
ATOM   308  O O   . ASN A 1 40  ? -4.085  11.310  -19.459 1.00 19.30 ?  263 ASN A O   1 
ATOM   309  C CB  . ASN A 1 40  ? -1.595  9.178   -19.364 1.00 17.28 ?  263 ASN A CB  1 
ATOM   310  C CG  . ASN A 1 40  ? -0.655  8.237   -18.634 1.00 19.29 ?  263 ASN A CG  1 
ATOM   311  O OD1 . ASN A 1 40  ? 0.273   8.673   -17.952 1.00 21.62 ?  263 ASN A OD1 1 
ATOM   312  N ND2 . ASN A 1 40  ? -0.889  6.937   -18.775 1.00 17.47 ?  263 ASN A ND2 1 
ATOM   313  N N   . GLY A 1 41  ? -2.076  12.288  -19.758 1.00 18.72 ?  264 GLY A N   1 
ATOM   314  C CA  . GLY A 1 41  ? -2.631  13.396  -20.511 1.00 18.58 ?  264 GLY A CA  1 
ATOM   315  C C   . GLY A 1 41  ? -3.429  14.372  -19.679 1.00 18.87 ?  264 GLY A C   1 
ATOM   316  O O   . GLY A 1 41  ? -4.356  15.004  -20.196 1.00 20.36 ?  264 GLY A O   1 
ATOM   317  N N   . ARG A 1 42  ? -3.097  14.511  -18.399 1.00 17.97 ?  265 ARG A N   1 
ATOM   318  C CA  . ARG A 1 42  ? -3.774  15.434  -17.497 1.00 19.25 ?  265 ARG A CA  1 
ATOM   319  C C   . ARG A 1 42  ? -2.825  16.575  -17.163 1.00 20.54 ?  265 ARG A C   1 
ATOM   320  O O   . ARG A 1 42  ? -1.714  16.341  -16.676 1.00 17.13 ?  265 ARG A O   1 
ATOM   321  C CB  . ARG A 1 42  ? -4.234  14.723  -16.226 1.00 17.94 ?  265 ARG A CB  1 
ATOM   322  C CG  . ARG A 1 42  ? -5.142  13.537  -16.485 1.00 18.78 ?  265 ARG A CG  1 
ATOM   323  C CD  . ARG A 1 42  ? -6.494  13.978  -17.018 1.00 14.98 ?  265 ARG A CD  1 
ATOM   324  N NE  . ARG A 1 42  ? -7.165  14.914  -16.123 1.00 16.92 ?  265 ARG A NE  1 
ATOM   325  C CZ  . ARG A 1 42  ? -8.073  14.567  -15.221 1.00 19.00 ?  265 ARG A CZ  1 
ATOM   326  N NH1 . ARG A 1 42  ? -8.440  13.306  -15.059 1.00 17.29 ?  265 ARG A NH1 1 
ATOM   327  N NH2 . ARG A 1 42  ? -8.625  15.508  -14.461 1.00 17.84 ?  265 ARG A NH2 1 
ATOM   328  N N   . CYS A 1 43  ? -3.266  17.803  -17.423 1.00 23.10 ?  266 CYS A N   1 
ATOM   329  C CA  . CYS A 1 43  ? -2.430  18.977  -17.224 1.00 19.95 ?  266 CYS A CA  1 
ATOM   330  C C   . CYS A 1 43  ? -3.322  20.206  -17.166 1.00 19.74 ?  266 CYS A C   1 
ATOM   331  O O   . CYS A 1 43  ? -4.269  20.325  -17.946 1.00 21.45 ?  266 CYS A O   1 
ATOM   332  C CB  . CYS A 1 43  ? -1.399  19.118  -18.350 1.00 22.02 ?  266 CYS A CB  1 
ATOM   333  S SG  . CYS A 1 43  ? -0.319  20.561  -18.212 1.00 25.27 ?  266 CYS A SG  1 
ATOM   334  N N   . THR A 1 44  ? -3.018  21.110  -16.241 1.00 19.35 ?  267 THR A N   1 
ATOM   335  C CA  . THR A 1 44  ? -3.745  22.367  -16.188 1.00 22.53 ?  267 THR A CA  1 
ATOM   336  C C   . THR A 1 44  ? -3.263  23.300  -17.296 1.00 22.38 ?  267 THR A C   1 
ATOM   337  O O   . THR A 1 44  ? -2.151  23.170  -17.816 1.00 20.48 ?  267 THR A O   1 
ATOM   338  C CB  . THR A 1 44  ? -3.576  23.041  -14.826 1.00 22.82 ?  267 THR A CB  1 
ATOM   339  O OG1 . THR A 1 44  ? -2.208  23.430  -14.649 1.00 19.81 ?  267 THR A OG1 1 
ATOM   340  C CG2 . THR A 1 44  ? -3.981  22.094  -13.707 1.00 20.26 ?  267 THR A CG2 1 
ATOM   341  N N   . THR A 1 45  ? -4.124  24.254  -17.656 1.00 20.05 ?  268 THR A N   1 
ATOM   342  C CA  . THR A 1 45  ? -3.786  25.191  -18.720 1.00 22.57 ?  268 THR A CA  1 
ATOM   343  C C   . THR A 1 45  ? -2.623  26.103  -18.346 1.00 25.20 ?  268 THR A C   1 
ATOM   344  O O   . THR A 1 45  ? -1.961  26.635  -19.244 1.00 24.31 ?  268 THR A O   1 
ATOM   345  C CB  . THR A 1 45  ? -5.008  26.030  -19.102 1.00 23.58 ?  268 THR A CB  1 
ATOM   346  O OG1 . THR A 1 45  ? -5.514  26.703  -17.943 1.00 25.01 ?  268 THR A OG1 1 
ATOM   347  C CG2 . THR A 1 45  ? -6.100  25.144  -19.685 1.00 20.02 ?  268 THR A CG2 1 
ATOM   348  N N   . ASP A 1 46  ? -2.355  26.295  -17.054 1.00 25.78 ?  269 ASP A N   1 
ATOM   349  C CA  . ASP A 1 46  ? -1.194  27.059  -16.616 1.00 26.31 ?  269 ASP A CA  1 
ATOM   350  C C   . ASP A 1 46  ? -0.002  26.170  -16.272 1.00 25.17 ?  269 ASP A C   1 
ATOM   351  O O   . ASP A 1 46  ? 0.953   26.644  -15.649 1.00 30.82 ?  269 ASP A O   1 
ATOM   352  C CB  . ASP A 1 46  ? -1.555  27.963  -15.431 1.00 29.38 ?  269 ASP A CB  1 
ATOM   353  C CG  . ASP A 1 46  ? -2.263  27.225  -14.315 1.00 32.83 ?  269 ASP A CG  1 
ATOM   354  O OD1 . ASP A 1 46  ? -2.447  25.997  -14.428 1.00 34.31 ?  269 ASP A OD1 1 
ATOM   355  O OD2 . ASP A 1 46  ? -2.642  27.882  -13.322 1.00 29.04 -1 269 ASP A OD2 1 
ATOM   356  N N   . GLY A 1 47  ? -0.043  24.897  -16.651 1.00 25.07 ?  270 GLY A N   1 
ATOM   357  C CA  . GLY A 1 47  ? 1.141   24.070  -16.718 1.00 25.54 ?  270 GLY A CA  1 
ATOM   358  C C   . GLY A 1 47  ? 1.438   23.156  -15.549 1.00 23.75 ?  270 GLY A C   1 
ATOM   359  O O   . GLY A 1 47  ? 2.612   22.835  -15.329 1.00 23.04 ?  270 GLY A O   1 
ATOM   360  N N   . VAL A 1 48  ? 0.430   22.711  -14.807 1.00 22.45 ?  271 VAL A N   1 
ATOM   361  C CA  . VAL A 1 48  ? 0.633   21.806  -13.680 1.00 21.82 ?  271 VAL A CA  1 
ATOM   362  C C   . VAL A 1 48  ? 0.279   20.396  -14.137 1.00 21.33 ?  271 VAL A C   1 
ATOM   363  O O   . VAL A 1 48  ? -0.886  20.098  -14.423 1.00 23.52 ?  271 VAL A O   1 
ATOM   364  C CB  . VAL A 1 48  ? -0.196  22.220  -12.457 1.00 23.14 ?  271 VAL A CB  1 
ATOM   365  C CG1 . VAL A 1 48  ? 0.141   21.332  -11.266 1.00 22.51 ?  271 VAL A CG1 1 
ATOM   366  C CG2 . VAL A 1 48  ? 0.046   23.683  -12.121 1.00 20.42 ?  271 VAL A CG2 1 
ATOM   367  N N   . LEU A 1 49  ? 1.284   19.526  -14.205 1.00 20.44 ?  272 LEU A N   1 
ATOM   368  C CA  . LEU A 1 49  ? 1.052   18.139  -14.581 1.00 21.16 ?  272 LEU A CA  1 
ATOM   369  C C   . LEU A 1 49  ? 0.373   17.390  -13.440 1.00 19.83 ?  272 LEU A C   1 
ATOM   370  O O   . LEU A 1 49  ? 0.734   17.548  -12.271 1.00 19.79 ?  272 LEU A O   1 
ATOM   371  C CB  . LEU A 1 49  ? 2.372   17.461  -14.948 1.00 19.76 ?  272 LEU A CB  1 
ATOM   372  C CG  . LEU A 1 49  ? 3.239   18.188  -15.979 1.00 23.47 ?  272 LEU A CG  1 
ATOM   373  C CD1 . LEU A 1 49  ? 4.581   17.492  -16.147 1.00 22.03 ?  272 LEU A CD1 1 
ATOM   374  C CD2 . LEU A 1 49  ? 2.514   18.290  -17.311 1.00 19.43 ?  272 LEU A CD2 1 
ATOM   375  N N   . LEU A 1 50  ? -0.617  16.573  -13.785 1.00 18.22 ?  273 LEU A N   1 
ATOM   376  C CA  . LEU A 1 50  ? -1.421  15.854  -12.808 1.00 17.20 ?  273 LEU A CA  1 
ATOM   377  C C   . LEU A 1 50  ? -1.358  14.355  -13.072 1.00 19.66 ?  273 LEU A C   1 
ATOM   378  O O   . LEU A 1 50  ? -0.831  13.899  -14.090 1.00 19.43 ?  273 LEU A O   1 
ATOM   379  C CB  . LEU A 1 50  ? -2.880  16.326  -12.839 1.00 21.05 ?  273 LEU A CB  1 
ATOM   380  C CG  . LEU A 1 50  ? -3.133  17.832  -12.919 1.00 22.04 ?  273 LEU A CG  1 
ATOM   381  C CD1 . LEU A 1 50  ? -4.544  18.101  -13.420 1.00 19.44 ?  273 LEU A CD1 1 
ATOM   382  C CD2 . LEU A 1 50  ? -2.909  18.481  -11.565 1.00 16.83 ?  273 LEU A CD2 1 
ATOM   383  N N   . GLY A 1 51  ? -1.912  13.592  -12.132 1.00 20.40 ?  274 GLY A N   1 
ATOM   384  C CA  . GLY A 1 51  ? -1.994  12.149  -12.297 1.00 18.35 ?  274 GLY A CA  1 
ATOM   385  C C   . GLY A 1 51  ? -0.623  11.525  -12.462 1.00 22.48 ?  274 GLY A C   1 
ATOM   386  O O   . GLY A 1 51  ? 0.298   11.768  -11.674 1.00 23.87 ?  274 GLY A O   1 
ATOM   387  N N   . THR A 1 52  ? -0.483  10.705  -13.503 1.00 16.57 ?  275 THR A N   1 
ATOM   388  C CA  . THR A 1 52  ? 0.781   10.072  -13.856 1.00 17.86 ?  275 THR A CA  1 
ATOM   389  C C   . THR A 1 52  ? 1.366   10.665  -15.135 1.00 19.08 ?  275 THR A C   1 
ATOM   390  O O   . THR A 1 52  ? 2.056   9.975   -15.889 1.00 21.54 ?  275 THR A O   1 
ATOM   391  C CB  . THR A 1 52  ? 0.601   8.563   -14.014 1.00 19.92 ?  275 THR A CB  1 
ATOM   392  O OG1 . THR A 1 52  ? -0.153  8.295   -15.204 1.00 17.77 ?  275 THR A OG1 1 
ATOM   393  C CG2 . THR A 1 52  ? -0.136  7.984   -12.816 1.00 17.49 ?  275 THR A CG2 1 
ATOM   394  N N   . THR A 1 53  ? 1.102   11.945  -15.385 1.00 16.82 ?  276 THR A N   1 
ATOM   395  C CA  . THR A 1 53  ? 1.417   12.566  -16.664 1.00 18.72 ?  276 THR A CA  1 
ATOM   396  C C   . THR A 1 53  ? 2.855   13.070  -16.686 1.00 19.81 ?  276 THR A C   1 
ATOM   397  O O   . THR A 1 53  ? 3.263   13.845  -15.815 1.00 21.34 ?  276 THR A O   1 
ATOM   398  C CB  . THR A 1 53  ? 0.456   13.722  -16.949 1.00 20.12 ?  276 THR A CB  1 
ATOM   399  O OG1 . THR A 1 53  ? -0.863  13.207  -17.168 1.00 19.11 ?  276 THR A OG1 1 
ATOM   400  C CG2 . THR A 1 53  ? 0.903   14.502  -18.176 1.00 18.19 ?  276 THR A CG2 1 
ATOM   401  N N   . GLN A 1 54  ? 3.612   12.628  -17.684 1.00 17.76 ?  277 GLN A N   1 
ATOM   402  C CA  . GLN A 1 54  ? 4.941   13.142  -17.979 1.00 19.29 ?  277 GLN A CA  1 
ATOM   403  C C   . GLN A 1 54  ? 4.946   13.721  -19.394 1.00 21.21 ?  277 GLN A C   1 
ATOM   404  O O   . GLN A 1 54  ? 3.918   13.761  -20.075 1.00 20.01 ?  277 GLN A O   1 
ATOM   405  C CB  . GLN A 1 54  ? 6.000   12.051  -17.793 1.00 22.12 ?  277 GLN A CB  1 
ATOM   406  C CG  . GLN A 1 54  ? 5.684   10.736  -18.480 1.00 18.56 ?  277 GLN A CG  1 
ATOM   407  C CD  . GLN A 1 54  ? 5.981   10.773  -19.962 1.00 19.74 ?  277 GLN A CD  1 
ATOM   408  O OE1 . GLN A 1 54  ? 7.080   11.141  -20.374 1.00 19.67 ?  277 GLN A OE1 1 
ATOM   409  N NE2 . GLN A 1 54  ? 5.001   10.395  -20.773 1.00 20.60 ?  277 GLN A NE2 1 
ATOM   410  N N   . LEU A 1 55  ? 6.121   14.165  -19.842 1.00 21.53 ?  278 LEU A N   1 
ATOM   411  C CA  . LEU A 1 55  ? 6.205   15.024  -21.018 1.00 22.39 ?  278 LEU A CA  1 
ATOM   412  C C   . LEU A 1 55  ? 6.567   14.301  -22.309 1.00 22.14 ?  278 LEU A C   1 
ATOM   413  O O   . LEU A 1 55  ? 6.377   14.875  -23.387 1.00 23.48 ?  278 LEU A O   1 
ATOM   414  C CB  . LEU A 1 55  ? 7.224   16.143  -20.776 1.00 23.11 ?  278 LEU A CB  1 
ATOM   415  C CG  . LEU A 1 55  ? 6.753   17.259  -19.840 1.00 26.93 ?  278 LEU A CG  1 
ATOM   416  C CD1 . LEU A 1 55  ? 7.930   18.087  -19.350 1.00 23.72 ?  278 LEU A CD1 1 
ATOM   417  C CD2 . LEU A 1 55  ? 5.723   18.138  -20.533 1.00 23.55 ?  278 LEU A CD2 1 
ATOM   418  N N   . SER A 1 56  ? 7.076   13.080  -22.244 1.00 24.56 ?  279 SER A N   1 
ATOM   419  C CA  . SER A 1 56  ? 7.524   12.417  -23.467 1.00 23.11 ?  279 SER A CA  1 
ATOM   420  C C   . SER A 1 56  ? 6.352   11.727  -24.157 1.00 23.61 ?  279 SER A C   1 
ATOM   421  O O   . SER A 1 56  ? 5.624   10.963  -23.516 1.00 24.08 ?  279 SER A O   1 
ATOM   422  C CB  . SER A 1 56  ? 8.621   11.402  -23.163 1.00 21.31 ?  279 SER A CB  1 
ATOM   423  O OG  . SER A 1 56  ? 8.757   10.470  -24.221 1.00 21.57 ?  279 SER A OG  1 
ATOM   424  N N   . PRO A 1 57  ? 6.140   11.967  -25.455 1.00 23.23 ?  280 PRO A N   1 
ATOM   425  C CA  . PRO A 1 57  ? 5.057   11.260  -26.154 1.00 23.25 ?  280 PRO A CA  1 
ATOM   426  C C   . PRO A 1 57  ? 5.338   9.780   -26.344 1.00 22.47 ?  280 PRO A C   1 
ATOM   427  O O   . PRO A 1 57  ? 4.390   8.996   -26.483 1.00 26.08 ?  280 PRO A O   1 
ATOM   428  C CB  . PRO A 1 57  ? 4.965   11.995  -27.498 1.00 17.95 ?  280 PRO A CB  1 
ATOM   429  C CG  . PRO A 1 57  ? 6.320   12.587  -27.702 1.00 19.01 ?  280 PRO A CG  1 
ATOM   430  C CD  . PRO A 1 57  ? 6.885   12.880  -26.340 1.00 20.81 ?  280 PRO A CD  1 
ATOM   431  N N   . VAL A 1 58  ? 6.612   9.372   -26.353 1.00 19.99 ?  281 VAL A N   1 
ATOM   432  C CA  . VAL A 1 58  ? 6.960   7.965   -26.537 1.00 19.71 ?  281 VAL A CA  1 
ATOM   433  C C   . VAL A 1 58  ? 7.141   7.223   -25.220 1.00 24.26 ?  281 VAL A C   1 
ATOM   434  O O   . VAL A 1 58  ? 7.185   5.983   -25.223 1.00 23.79 ?  281 VAL A O   1 
ATOM   435  C CB  . VAL A 1 58  ? 8.237   7.814   -27.389 1.00 22.12 ?  281 VAL A CB  1 
ATOM   436  C CG1 . VAL A 1 58  ? 7.937   8.115   -28.848 1.00 22.12 ?  281 VAL A CG1 1 
ATOM   437  C CG2 . VAL A 1 58  ? 9.347   8.722   -26.870 1.00 23.35 ?  281 VAL A CG2 1 
ATOM   438  N N   . ASN A 1 59  ? 7.248   7.932   -24.097 1.00 20.82 ?  282 ASN A N   1 
ATOM   439  C CA  . ASN A 1 59  ? 7.339   7.302   -22.779 1.00 23.64 ?  282 ASN A CA  1 
ATOM   440  C C   . ASN A 1 59  ? 5.972   7.077   -22.154 1.00 25.41 ?  282 ASN A C   1 
ATOM   441  O O   . ASN A 1 59  ? 5.786   7.280   -20.950 1.00 22.99 ?  282 ASN A O   1 
ATOM   442  C CB  . ASN A 1 59  ? 8.223   8.136   -21.858 1.00 23.14 ?  282 ASN A CB  1 
ATOM   443  C CG  . ASN A 1 59  ? 9.697   7.861   -22.063 1.00 20.92 ?  282 ASN A CG  1 
ATOM   444  O OD1 . ASN A 1 59  ? 10.073  6.988   -22.845 1.00 22.71 ?  282 ASN A OD1 1 
ATOM   445  N ND2 . ASN A 1 59  ? 10.542  8.598   -21.353 1.00 20.10 ?  282 ASN A ND2 1 
ATOM   446  N N   . ILE A 1 60  ? 4.995   6.658   -22.952 1.00 22.87 ?  283 ILE A N   1 
ATOM   447  C CA  . ILE A 1 60  ? 3.646   6.380   -22.481 1.00 22.36 ?  283 ILE A CA  1 
ATOM   448  C C   . ILE A 1 60  ? 3.386   4.892   -22.655 1.00 21.42 ?  283 ILE A C   1 
ATOM   449  O O   . ILE A 1 60  ? 3.581   4.348   -23.749 1.00 23.44 ?  283 ILE A O   1 
ATOM   450  C CB  . ILE A 1 60  ? 2.598   7.221   -23.231 1.00 22.21 ?  283 ILE A CB  1 
ATOM   451  C CG1 . ILE A 1 60  ? 3.008   8.695   -23.217 1.00 23.17 ?  283 ILE A CG1 1 
ATOM   452  C CG2 . ILE A 1 60  ? 1.230   7.046   -22.598 1.00 20.97 ?  283 ILE A CG2 1 
ATOM   453  C CD1 . ILE A 1 60  ? 2.063   9.604   -23.963 1.00 22.39 ?  283 ILE A CD1 1 
ATOM   454  N N   . CYS A 1 61  ? 2.958   4.240   -21.573 1.00 20.35 ?  284 CYS A N   1 
ATOM   455  C CA  . CYS A 1 61  ? 2.780   2.790   -21.501 1.00 20.58 ?  284 CYS A CA  1 
ATOM   456  C C   . CYS A 1 61  ? 4.095   2.036   -21.682 1.00 21.37 ?  284 CYS A C   1 
ATOM   457  O O   . CYS A 1 61  ? 4.089   0.834   -21.968 1.00 21.51 ?  284 CYS A O   1 
ATOM   458  C CB  . CYS A 1 61  ? 1.739   2.297   -22.513 1.00 20.67 ?  284 CYS A CB  1 
ATOM   459  S SG  . CYS A 1 61  ? 0.052   2.850   -22.169 1.00 19.61 ?  284 CYS A SG  1 
ATOM   460  N N   . THR A 1 62  ? 5.223   2.721   -21.520 1.00 19.06 ?  285 THR A N   1 
ATOM   461  C CA  . THR A 1 62  ? 6.532   2.085   -21.520 1.00 19.86 ?  285 THR A CA  1 
ATOM   462  C C   . THR A 1 62  ? 6.919   1.696   -20.099 1.00 20.14 ?  285 THR A C   1 
ATOM   463  O O   . THR A 1 62  ? 6.495   2.323   -19.125 1.00 19.91 ?  285 THR A O   1 
ATOM   464  C CB  . THR A 1 62  ? 7.600   3.017   -22.101 1.00 22.46 ?  285 THR A CB  1 
ATOM   465  O OG1 . THR A 1 62  ? 7.447   4.328   -21.542 1.00 20.97 ?  285 THR A OG1 1 
ATOM   466  C CG2 . THR A 1 62  ? 7.485   3.100   -23.614 1.00 20.42 ?  285 THR A CG2 1 
ATOM   467  N N   . PHE A 1 63  ? 7.733   0.649   -19.989 1.00 20.63 ?  286 PHE A N   1 
ATOM   468  C CA  . PHE A 1 63  ? 8.253   0.196   -18.706 1.00 21.26 ?  286 PHE A CA  1 
ATOM   469  C C   . PHE A 1 63  ? 9.762   0.033   -18.799 1.00 21.84 ?  286 PHE A C   1 
ATOM   470  O O   . PHE A 1 63  ? 10.280  -0.467  -19.801 1.00 22.58 ?  286 PHE A O   1 
ATOM   471  C CB  . PHE A 1 63  ? 7.616   -1.129  -18.267 1.00 20.34 ?  286 PHE A CB  1 
ATOM   472  C CG  . PHE A 1 63  ? 6.162   -1.017  -17.908 1.00 21.32 ?  286 PHE A CG  1 
ATOM   473  C CD1 . PHE A 1 63  ? 5.780   -0.595  -16.645 1.00 19.92 ?  286 PHE A CD1 1 
ATOM   474  C CD2 . PHE A 1 63  ? 5.179   -1.355  -18.823 1.00 23.20 ?  286 PHE A CD2 1 
ATOM   475  C CE1 . PHE A 1 63  ? 4.445   -0.498  -16.306 1.00 19.83 ?  286 PHE A CE1 1 
ATOM   476  C CE2 . PHE A 1 63  ? 3.842   -1.260  -18.488 1.00 25.82 ?  286 PHE A CE2 1 
ATOM   477  C CZ  . PHE A 1 63  ? 3.476   -0.833  -17.228 1.00 22.61 ?  286 PHE A CZ  1 
ATOM   478  N N   . ARG A 1 64  ? 10.462  0.457   -17.749 1.00 19.90 ?  287 ARG A N   1 
ATOM   479  C CA  . ARG A 1 64  ? 11.911  0.347   -17.674 1.00 18.75 ?  287 ARG A CA  1 
ATOM   480  C C   . ARG A 1 64  ? 12.314  -0.185  -16.307 1.00 23.07 ?  287 ARG A C   1 
ATOM   481  O O   . ARG A 1 64  ? 11.689  0.142   -15.294 1.00 21.95 ?  287 ARG A O   1 
ATOM   482  C CB  . ARG A 1 64  ? 12.591  1.699   -17.930 1.00 20.54 ?  287 ARG A CB  1 
ATOM   483  C CG  . ARG A 1 64  ? 12.494  2.186   -19.365 1.00 21.91 ?  287 ARG A CG  1 
ATOM   484  C CD  . ARG A 1 64  ? 13.079  3.580   -19.512 1.00 23.21 ?  287 ARG A CD  1 
ATOM   485  N NE  . ARG A 1 64  ? 13.304  3.932   -20.909 1.00 24.71 ?  287 ARG A NE  1 
ATOM   486  C CZ  . ARG A 1 64  ? 12.419  4.555   -21.675 1.00 23.57 ?  287 ARG A CZ  1 
ATOM   487  N NH1 . ARG A 1 64  ? 11.234  4.916   -21.209 1.00 21.43 ?  287 ARG A NH1 1 
ATOM   488  N NH2 . ARG A 1 64  ? 12.729  4.821   -22.941 1.00 21.87 ?  287 ARG A NH2 1 
ATOM   489  N N   . GLY A 1 65  ? 13.359  -1.002  -16.285 1.00 23.47 ?  288 GLY A N   1 
ATOM   490  C CA  . GLY A 1 65  ? 13.866  -1.565  -15.042 1.00 20.87 ?  288 GLY A CA  1 
ATOM   491  C C   . GLY A 1 65  ? 14.708  -2.801  -15.321 1.00 23.83 ?  288 GLY A C   1 
ATOM   492  O O   . GLY A 1 65  ? 15.301  -2.934  -16.392 1.00 23.59 ?  288 GLY A O   1 
ATOM   493  N N   . ASP A 1 66  ? 14.752  -3.688  -14.330 1.00 24.56 ?  289 ASP A N   1 
ATOM   494  C CA  . ASP A 1 66  ? 15.387  -4.989  -14.465 1.00 23.91 ?  289 ASP A CA  1 
ATOM   495  C C   . ASP A 1 66  ? 14.354  -6.075  -14.195 1.00 23.06 ?  289 ASP A C   1 
ATOM   496  O O   . ASP A 1 66  ? 13.315  -5.830  -13.575 1.00 22.68 ?  289 ASP A O   1 
ATOM   497  C CB  . ASP A 1 66  ? 16.589  -5.131  -13.519 1.00 23.51 ?  289 ASP A CB  1 
ATOM   498  C CG  . ASP A 1 66  ? 16.179  -5.303  -12.070 1.00 27.86 ?  289 ASP A CG  1 
ATOM   499  O OD1 . ASP A 1 66  ? 15.910  -6.451  -11.656 1.00 31.25 ?  289 ASP A OD1 1 
ATOM   500  O OD2 . ASP A 1 66  ? 16.128  -4.289  -11.344 1.00 27.75 -1 289 ASP A OD2 1 
ATOM   501  N N   . VAL A 1 67  ? 14.641  -7.285  -14.667 1.00 23.32 ?  290 VAL A N   1 
ATOM   502  C CA  . VAL A 1 67  ? 13.652  -8.354  -14.658 1.00 27.21 ?  290 VAL A CA  1 
ATOM   503  C C   . VAL A 1 67  ? 14.159  -9.539  -13.849 1.00 27.44 ?  290 VAL A C   1 
ATOM   504  O O   . VAL A 1 67  ? 15.363  -9.797  -13.762 1.00 27.47 ?  290 VAL A O   1 
ATOM   505  C CB  . VAL A 1 67  ? 13.279  -8.794  -16.090 1.00 21.18 ?  290 VAL A CB  1 
ATOM   506  C CG1 . VAL A 1 67  ? 12.462  -7.712  -16.774 1.00 18.95 ?  290 VAL A CG1 1 
ATOM   507  C CG2 . VAL A 1 67  ? 14.532  -9.112  -16.887 1.00 19.56 ?  290 VAL A CG2 1 
ATOM   508  N N   . THR A 1 68  ? 13.211  -10.264 -13.256 1.00 29.96 ?  291 THR A N   1 
ATOM   509  C CA  . THR A 1 68  ? 13.476  -11.480 -12.500 1.00 28.46 ?  291 THR A CA  1 
ATOM   510  C C   . THR A 1 68  ? 12.544  -12.570 -13.005 1.00 27.07 ?  291 THR A C   1 
ATOM   511  O O   . THR A 1 68  ? 11.328  -12.367 -13.072 1.00 29.80 ?  291 THR A O   1 
ATOM   512  C CB  . THR A 1 68  ? 13.268  -11.261 -10.996 1.00 27.72 ?  291 THR A CB  1 
ATOM   513  O OG1 . THR A 1 68  ? 14.229  -10.316 -10.509 1.00 33.64 ?  291 THR A OG1 1 
ATOM   514  C CG2 . THR A 1 68  ? 13.419  -12.571 -10.235 1.00 28.34 ?  291 THR A CG2 1 
ATOM   515  N N   . HIS A 1 69  ? 13.110  -13.720 -13.362 1.00 28.87 ?  292 HIS A N   1 
ATOM   516  C CA  . HIS A 1 69  ? 12.315  -14.810 -13.907 1.00 33.08 ?  292 HIS A CA  1 
ATOM   517  C C   . HIS A 1 69  ? 11.538  -15.520 -12.805 1.00 33.32 ?  292 HIS A C   1 
ATOM   518  O O   . HIS A 1 69  ? 12.033  -15.700 -11.689 1.00 32.30 ?  292 HIS A O   1 
ATOM   519  C CB  . HIS A 1 69  ? 13.206  -15.812 -14.641 1.00 31.95 ?  292 HIS A CB  1 
ATOM   520  C CG  . HIS A 1 69  ? 12.450  -16.943 -15.267 1.00 33.09 ?  292 HIS A CG  1 
ATOM   521  N ND1 . HIS A 1 69  ? 12.628  -18.257 -14.890 1.00 38.81 ?  292 HIS A ND1 1 
ATOM   522  C CD2 . HIS A 1 69  ? 11.511  -16.956 -16.242 1.00 34.70 ?  292 HIS A CD2 1 
ATOM   523  C CE1 . HIS A 1 69  ? 11.832  -19.030 -15.607 1.00 38.15 ?  292 HIS A CE1 1 
ATOM   524  N NE2 . HIS A 1 69  ? 11.144  -18.265 -16.435 1.00 36.94 ?  292 HIS A NE2 1 
ATOM   525  N N   . ILE A 1 70  ? 10.312  -15.919 -13.129 1.00 34.31 ?  293 ILE A N   1 
ATOM   526  C CA  . ILE A 1 70  ? 9.470   -16.711 -12.240 1.00 36.22 ?  293 ILE A CA  1 
ATOM   527  C C   . ILE A 1 70  ? 9.540   -18.157 -12.711 1.00 39.36 ?  293 ILE A C   1 
ATOM   528  O O   . ILE A 1 70  ? 9.102   -18.478 -13.823 1.00 39.63 ?  293 ILE A O   1 
ATOM   529  C CB  . ILE A 1 70  ? 8.024   -16.190 -12.227 1.00 37.48 ?  293 ILE A CB  1 
ATOM   530  C CG1 . ILE A 1 70  ? 7.985   -14.761 -11.682 1.00 33.51 ?  293 ILE A CG1 1 
ATOM   531  C CG2 . ILE A 1 70  ? 7.134   -17.096 -11.393 1.00 33.52 ?  293 ILE A CG2 1 
ATOM   532  C CD1 . ILE A 1 70  ? 6.997   -13.861 -12.390 1.00 30.42 ?  293 ILE A CD1 1 
ATOM   533  N N   . THR A 1 71  ? 10.095  -19.028 -11.869 1.00 39.22 ?  294 THR A N   1 
ATOM   534  C CA  . THR A 1 71  ? 10.388  -20.394 -12.283 1.00 44.27 ?  294 THR A CA  1 
ATOM   535  C C   . THR A 1 71  ? 9.110   -21.156 -12.617 1.00 41.03 ?  294 THR A C   1 
ATOM   536  O O   . THR A 1 71  ? 8.040   -20.904 -12.055 1.00 41.94 ?  294 THR A O   1 
ATOM   537  C CB  . THR A 1 71  ? 11.161  -21.130 -11.188 1.00 48.90 ?  294 THR A CB  1 
ATOM   538  O OG1 . THR A 1 71  ? 10.389  -21.144 -9.981  1.00 42.82 ?  294 THR A OG1 1 
ATOM   539  C CG2 . THR A 1 71  ? 12.492  -20.440 -10.927 1.00 42.42 ?  294 THR A CG2 1 
ATOM   540  N N   . GLY A 1 72  ? 9.237   -22.103 -13.543 1.00 40.18 ?  295 GLY A N   1 
ATOM   541  C CA  . GLY A 1 72  ? 8.083   -22.836 -14.024 1.00 37.81 ?  295 GLY A CA  1 
ATOM   542  C C   . GLY A 1 72  ? 7.133   -21.999 -14.848 1.00 40.92 ?  295 GLY A C   1 
ATOM   543  O O   . GLY A 1 72  ? 5.935   -22.295 -14.893 1.00 41.86 ?  295 GLY A O   1 
ATOM   544  N N   . SER A 1 73  ? 7.637   -20.959 -15.507 1.00 38.32 ?  296 SER A N   1 
ATOM   545  C CA  . SER A 1 73  ? 6.786   -20.038 -16.243 1.00 39.07 ?  296 SER A CA  1 
ATOM   546  C C   . SER A 1 73  ? 7.598   -19.366 -17.339 1.00 37.49 ?  296 SER A C   1 
ATOM   547  O O   . SER A 1 73  ? 8.826   -19.470 -17.390 1.00 38.07 ?  296 SER A O   1 
ATOM   548  C CB  . SER A 1 73  ? 6.178   -18.980 -15.317 1.00 37.02 ?  296 SER A CB  1 
ATOM   549  O OG  . SER A 1 73  ? 7.124   -17.963 -15.031 1.00 34.00 ?  296 SER A OG  1 
ATOM   550  N N   . ARG A 1 74  ? 6.884   -18.680 -18.230 1.00 36.28 ?  297 ARG A N   1 
ATOM   551  C CA  . ARG A 1 74  ? 7.477   -17.731 -19.162 1.00 36.35 ?  297 ARG A CA  1 
ATOM   552  C C   . ARG A 1 74  ? 7.174   -16.295 -18.754 1.00 32.99 ?  297 ARG A C   1 
ATOM   553  O O   . ARG A 1 74  ? 7.202   -15.390 -19.594 1.00 31.31 ?  297 ARG A O   1 
ATOM   554  C CB  . ARG A 1 74  ? 6.992   -18.000 -20.586 1.00 35.10 ?  297 ARG A CB  1 
ATOM   555  C CG  . ARG A 1 74  ? 7.662   -19.192 -21.249 1.00 36.11 ?  297 ARG A CG  1 
ATOM   556  C CD  . ARG A 1 74  ? 6.765   -19.812 -22.305 1.00 40.01 ?  297 ARG A CD  1 
ATOM   557  N NE  . ARG A 1 74  ? 7.503   -20.147 -23.517 1.00 47.23 ?  297 ARG A NE  1 
ATOM   558  C CZ  . ARG A 1 74  ? 7.307   -21.245 -24.233 1.00 53.80 ?  297 ARG A CZ  1 
ATOM   559  N NH1 . ARG A 1 74  ? 6.398   -22.142 -23.889 1.00 54.26 ?  297 ARG A NH1 1 
ATOM   560  N NH2 . ARG A 1 74  ? 8.042   -21.449 -25.323 1.00 56.97 ?  297 ARG A NH2 1 
ATOM   561  N N   . ASN A 1 75  ? 6.876   -16.079 -17.477 1.00 32.39 ?  298 ASN A N   1 
ATOM   562  C CA  . ASN A 1 75  ? 6.531   -14.773 -16.943 1.00 31.16 ?  298 ASN A CA  1 
ATOM   563  C C   . ASN A 1 75  ? 7.741   -14.144 -16.264 1.00 27.59 ?  298 ASN A C   1 
ATOM   564  O O   . ASN A 1 75  ? 8.569   -14.832 -15.663 1.00 32.65 ?  298 ASN A O   1 
ATOM   565  C CB  . ASN A 1 75  ? 5.377   -14.885 -15.946 1.00 32.95 ?  298 ASN A CB  1 
ATOM   566  C CG  . ASN A 1 75  ? 4.101   -15.387 -16.588 1.00 35.15 ?  298 ASN A CG  1 
ATOM   567  O OD1 . ASN A 1 75  ? 3.955   -15.360 -17.809 1.00 30.72 ?  298 ASN A OD1 1 
ATOM   568  N ND2 . ASN A 1 75  ? 3.169   -15.855 -15.765 1.00 39.99 ?  298 ASN A ND2 1 
ATOM   569  N N   . TYR A 1 76  ? 7.831   -12.822 -16.364 1.00 27.39 ?  299 TYR A N   1 
ATOM   570  C CA  . TYR A 1 76  ? 8.925   -12.070 -15.772 1.00 28.64 ?  299 TYR A CA  1 
ATOM   571  C C   . TYR A 1 76  ? 8.376   -10.943 -14.914 1.00 27.39 ?  299 TYR A C   1 
ATOM   572  O O   . TYR A 1 76  ? 7.446   -10.238 -15.316 1.00 24.59 ?  299 TYR A O   1 
ATOM   573  C CB  . TYR A 1 76  ? 9.857   -11.494 -16.845 1.00 27.15 ?  299 TYR A CB  1 
ATOM   574  C CG  . TYR A 1 76  ? 10.785  -12.514 -17.460 1.00 28.55 ?  299 TYR A CG  1 
ATOM   575  C CD1 . TYR A 1 76  ? 10.387  -13.275 -18.551 1.00 27.45 ?  299 TYR A CD1 1 
ATOM   576  C CD2 . TYR A 1 76  ? 12.057  -12.723 -16.944 1.00 26.63 ?  299 TYR A CD2 1 
ATOM   577  C CE1 . TYR A 1 76  ? 11.232  -14.210 -19.115 1.00 29.62 ?  299 TYR A CE1 1 
ATOM   578  C CE2 . TYR A 1 76  ? 12.910  -13.658 -17.500 1.00 29.32 ?  299 TYR A CE2 1 
ATOM   579  C CZ  . TYR A 1 76  ? 12.491  -14.399 -18.587 1.00 31.82 ?  299 TYR A CZ  1 
ATOM   580  O OH  . TYR A 1 76  ? 13.332  -15.332 -19.148 1.00 30.98 ?  299 TYR A OH  1 
ATOM   581  N N   . THR A 1 77  ? 8.952   -10.790 -13.725 1.00 26.93 ?  300 THR A N   1 
ATOM   582  C CA  . THR A 1 77  ? 8.685   -9.641  -12.872 1.00 25.53 ?  300 THR A CA  1 
ATOM   583  C C   . THR A 1 77  ? 9.677   -8.539  -13.214 1.00 25.08 ?  300 THR A C   1 
ATOM   584  O O   . THR A 1 77  ? 10.884  -8.787  -13.285 1.00 23.02 ?  300 THR A O   1 
ATOM   585  C CB  . THR A 1 77  ? 8.807   -10.014 -11.393 1.00 26.27 ?  300 THR A CB  1 
ATOM   586  O OG1 . THR A 1 77  ? 7.752   -10.913 -11.031 1.00 31.00 ?  300 THR A OG1 1 
ATOM   587  C CG2 . THR A 1 77  ? 8.734   -8.768  -10.517 1.00 25.75 ?  300 THR A CG2 1 
ATOM   588  N N   . MET A 1 78  ? 9.171   -7.331  -13.435 1.00 25.54 ?  301 MET A N   1 
ATOM   589  C CA  . MET A 1 78  ? 10.017  -6.171  -13.669 1.00 24.24 ?  301 MET A CA  1 
ATOM   590  C C   . MET A 1 78  ? 10.014  -5.298  -12.424 1.00 26.31 ?  301 MET A C   1 
ATOM   591  O O   . MET A 1 78  ? 8.968   -4.766  -12.037 1.00 26.07 ?  301 MET A O   1 
ATOM   592  C CB  . MET A 1 78  ? 9.555   -5.365  -14.882 1.00 22.32 ?  301 MET A CB  1 
ATOM   593  C CG  . MET A 1 78  ? 10.410  -4.130  -15.128 1.00 22.69 ?  301 MET A CG  1 
ATOM   594  S SD  . MET A 1 78  ? 9.897   -3.159  -16.555 1.00 25.54 ?  301 MET A SD  1 
ATOM   595  C CE  . MET A 1 78  ? 11.230  -3.500  -17.700 1.00 21.63 ?  301 MET A CE  1 
ATOM   596  N N   . ASN A 1 79  ? 11.178  -5.165  -11.796 1.00 24.35 ?  302 ASN A N   1 
ATOM   597  C CA  . ASN A 1 79  ? 11.367  -4.175  -10.746 1.00 24.19 ?  302 ASN A CA  1 
ATOM   598  C C   . ASN A 1 79  ? 11.596  -2.822  -11.406 1.00 25.95 ?  302 ASN A C   1 
ATOM   599  O O   . ASN A 1 79  ? 12.581  -2.636  -12.130 1.00 26.50 ?  302 ASN A O   1 
ATOM   600  C CB  . ASN A 1 79  ? 12.535  -4.566  -9.846  1.00 24.34 ?  302 ASN A CB  1 
ATOM   601  C CG  . ASN A 1 79  ? 12.438  -6.001  -9.365  1.00 27.98 ?  302 ASN A CG  1 
ATOM   602  O OD1 . ASN A 1 79  ? 11.614  -6.326  -8.510  1.00 25.27 ?  302 ASN A OD1 1 
ATOM   603  N ND2 . ASN A 1 79  ? 13.275  -6.869  -9.920  1.00 29.01 ?  302 ASN A ND2 1 
ATOM   604  N N   . LEU A 1 80  ? 10.687  -1.884  -11.162 1.00 25.53 ?  303 LEU A N   1 
ATOM   605  C CA  . LEU A 1 80  ? 10.582  -0.698  -11.998 1.00 23.54 ?  303 LEU A CA  1 
ATOM   606  C C   . LEU A 1 80  ? 11.561  0.393   -11.588 1.00 25.16 ?  303 LEU A C   1 
ATOM   607  O O   . LEU A 1 80  ? 11.761  0.665   -10.400 1.00 25.90 ?  303 LEU A O   1 
ATOM   608  C CB  . LEU A 1 80  ? 9.158   -0.145  -11.952 1.00 19.97 ?  303 LEU A CB  1 
ATOM   609  C CG  . LEU A 1 80  ? 8.085   -1.009  -12.613 1.00 20.58 ?  303 LEU A CG  1 
ATOM   610  C CD1 . LEU A 1 80  ? 6.698   -0.493  -12.273 1.00 21.13 ?  303 LEU A CD1 1 
ATOM   611  C CD2 . LEU A 1 80  ? 8.288   -1.050  -14.118 1.00 22.10 ?  303 LEU A CD2 1 
ATOM   612  N N   . ALA A 1 81  ? 12.172  1.012   -12.590 1.00 24.55 ?  304 ALA A N   1 
ATOM   613  C CA  . ALA A 1 81  ? 12.786  2.322   -12.464 1.00 24.54 ?  304 ALA A CA  1 
ATOM   614  C C   . ALA A 1 81  ? 11.876  3.354   -13.121 1.00 25.81 ?  304 ALA A C   1 
ATOM   615  O O   . ALA A 1 81  ? 10.937  3.016   -13.845 1.00 22.66 ?  304 ALA A O   1 
ATOM   616  C CB  . ALA A 1 81  ? 14.178  2.337   -13.101 1.00 21.46 ?  304 ALA A CB  1 
ATOM   617  N N   . SER A 1 82  ? 12.154  4.626   -12.854 1.00 25.59 ?  305 SER A N   1 
ATOM   618  C CA  . SER A 1 82  ? 11.382  5.677   -13.497 1.00 21.92 ?  305 SER A CA  1 
ATOM   619  C C   . SER A 1 82  ? 11.743  5.756   -14.982 1.00 23.22 ?  305 SER A C   1 
ATOM   620  O O   . SER A 1 82  ? 12.675  5.104   -15.460 1.00 23.65 ?  305 SER A O   1 
ATOM   621  C CB  . SER A 1 82  ? 11.612  7.018   -12.798 1.00 21.77 ?  305 SER A CB  1 
ATOM   622  O OG  . SER A 1 82  ? 12.896  7.540   -13.086 1.00 27.51 ?  305 SER A OG  1 
ATOM   623  N N   . GLN A 1 83  ? 10.982  6.571   -15.719 1.00 23.47 ?  306 GLN A N   1 
ATOM   624  C CA  . GLN A 1 83  ? 11.145  6.627   -17.169 1.00 22.92 ?  306 GLN A CA  1 
ATOM   625  C C   . GLN A 1 83  ? 12.525  7.120   -17.591 1.00 23.48 ?  306 GLN A C   1 
ATOM   626  O O   . GLN A 1 83  ? 12.903  6.939   -18.753 1.00 24.99 ?  306 GLN A O   1 
ATOM   627  C CB  . GLN A 1 83  ? 10.069  7.522   -17.788 1.00 18.58 ?  306 GLN A CB  1 
ATOM   628  C CG  . GLN A 1 83  ? 8.646   6.991   -17.666 1.00 22.97 ?  306 GLN A CG  1 
ATOM   629  C CD  . GLN A 1 83  ? 8.405   5.716   -18.461 1.00 23.67 ?  306 GLN A CD  1 
ATOM   630  O OE1 . GLN A 1 83  ? 9.186   5.358   -19.343 1.00 24.21 ?  306 GLN A OE1 1 
ATOM   631  N NE2 . GLN A 1 83  ? 7.307   5.032   -18.157 1.00 18.02 ?  306 GLN A NE2 1 
ATOM   632  N N   . ASN A 1 84  ? 13.284  7.738   -16.684 1.00 25.38 ?  307 ASN A N   1 
ATOM   633  C CA  . ASN A 1 84  ? 14.634  8.204   -16.980 1.00 25.59 ?  307 ASN A CA  1 
ATOM   634  C C   . ASN A 1 84  ? 15.697  7.413   -16.225 1.00 22.82 ?  307 ASN A C   1 
ATOM   635  O O   . ASN A 1 84  ? 16.806  7.914   -16.015 1.00 24.34 ?  307 ASN A O   1 
ATOM   636  C CB  . ASN A 1 84  ? 14.762  9.696   -16.672 1.00 23.23 ?  307 ASN A CB  1 
ATOM   637  C CG  . ASN A 1 84  ? 14.327  10.040  -15.263 1.00 31.98 ?  307 ASN A CG  1 
ATOM   638  O OD1 . ASN A 1 84  ? 13.178  9.812   -14.882 1.00 31.67 ?  307 ASN A OD1 1 
ATOM   639  N ND2 . ASN A 1 84  ? 15.245  10.593  -14.479 1.00 30.00 ?  307 ASN A ND2 1 
ATOM   640  N N   . TRP A 1 85  ? 15.369  6.189   -15.806 1.00 23.95 ?  308 TRP A N   1 
ATOM   641  C CA  . TRP A 1 85  ? 16.280  5.260   -15.141 1.00 26.24 ?  308 TRP A CA  1 
ATOM   642  C C   . TRP A 1 85  ? 16.728  5.742   -13.766 1.00 27.69 ?  308 TRP A C   1 
ATOM   643  O O   . TRP A 1 85  ? 17.763  5.297   -13.259 1.00 26.38 ?  308 TRP A O   1 
ATOM   644  C CB  . TRP A 1 85  ? 17.500  4.951   -16.014 1.00 26.26 ?  308 TRP A CB  1 
ATOM   645  C CG  . TRP A 1 85  ? 17.139  4.342   -17.333 1.00 25.55 ?  308 TRP A CG  1 
ATOM   646  C CD1 . TRP A 1 85  ? 17.044  4.983   -18.532 1.00 23.60 ?  308 TRP A CD1 1 
ATOM   647  C CD2 . TRP A 1 85  ? 16.815  2.970   -17.584 1.00 23.08 ?  308 TRP A CD2 1 
ATOM   648  N NE1 . TRP A 1 85  ? 16.686  4.094   -19.516 1.00 25.66 ?  308 TRP A NE1 1 
ATOM   649  C CE2 . TRP A 1 85  ? 16.539  2.851   -18.960 1.00 23.73 ?  308 TRP A CE2 1 
ATOM   650  C CE3 . TRP A 1 85  ? 16.733  1.830   -16.780 1.00 24.90 ?  308 TRP A CE3 1 
ATOM   651  C CZ2 . TRP A 1 85  ? 16.189  1.637   -19.549 1.00 21.04 ?  308 TRP A CZ2 1 
ATOM   652  C CZ3 . TRP A 1 85  ? 16.386  0.626   -17.366 1.00 24.35 ?  308 TRP A CZ3 1 
ATOM   653  C CH2 . TRP A 1 85  ? 16.117  0.539   -18.737 1.00 22.67 ?  308 TRP A CH2 1 
ATOM   654  N N   . ASN A 1 86  ? 15.973  6.644   -13.146 1.00 26.18 ?  309 ASN A N   1 
ATOM   655  C CA  . ASN A 1 86  ? 16.184  6.944   -11.740 1.00 24.53 ?  309 ASN A CA  1 
ATOM   656  C C   . ASN A 1 86  ? 15.523  5.876   -10.875 1.00 25.54 ?  309 ASN A C   1 
ATOM   657  O O   . ASN A 1 86  ? 14.610  5.166   -11.309 1.00 27.87 ?  309 ASN A O   1 
ATOM   658  C CB  . ASN A 1 86  ? 15.620  8.320   -11.381 1.00 26.96 ?  309 ASN A CB  1 
ATOM   659  C CG  . ASN A 1 86  ? 16.545  9.455   -11.769 1.00 30.91 ?  309 ASN A CG  1 
ATOM   660  O OD1 . ASN A 1 86  ? 16.153  10.622  -11.756 1.00 33.74 ?  309 ASN A OD1 1 
ATOM   661  N ND2 . ASN A 1 86  ? 17.782  9.118   -12.115 1.00 26.62 ?  309 ASN A ND2 1 
ATOM   662  N N   . ASP A 1 87  ? 16.008  5.756   -9.640  1.00 27.31 ?  310 ASP A N   1 
ATOM   663  C CA  . ASP A 1 87  ? 15.316  4.944   -8.649  1.00 26.12 ?  310 ASP A CA  1 
ATOM   664  C C   . ASP A 1 87  ? 13.864  5.390   -8.549  1.00 24.07 ?  310 ASP A C   1 
ATOM   665  O O   . ASP A 1 87  ? 13.569  6.588   -8.530  1.00 22.62 ?  310 ASP A O   1 
ATOM   666  C CB  . ASP A 1 87  ? 15.992  5.071   -7.281  1.00 25.59 ?  310 ASP A CB  1 
ATOM   667  C CG  . ASP A 1 87  ? 17.336  4.375   -7.220  1.00 28.12 ?  310 ASP A CG  1 
ATOM   668  O OD1 . ASP A 1 87  ? 17.627  3.551   -8.112  1.00 30.77 -1 310 ASP A OD1 1 
ATOM   669  O OD2 . ASP A 1 87  ? 18.104  4.653   -6.274  1.00 27.40 ?  310 ASP A OD2 1 
ATOM   670  N N   . TYR A 1 88  ? 12.952  4.425   -8.509  1.00 25.39 ?  311 TYR A N   1 
ATOM   671  C CA  . TYR A 1 88  ? 11.540  4.733   -8.337  1.00 26.27 ?  311 TYR A CA  1 
ATOM   672  C C   . TYR A 1 88  ? 11.206  4.702   -6.852  1.00 24.18 ?  311 TYR A C   1 
ATOM   673  O O   . TYR A 1 88  ? 11.380  3.672   -6.192  1.00 25.76 ?  311 TYR A O   1 
ATOM   674  C CB  . TYR A 1 88  ? 10.647  3.759   -9.102  1.00 25.18 ?  311 TYR A CB  1 
ATOM   675  C CG  . TYR A 1 88  ? 9.202   3.874   -8.679  1.00 25.64 ?  311 TYR A CG  1 
ATOM   676  C CD1 . TYR A 1 88  ? 8.470   5.021   -8.960  1.00 23.11 ?  311 TYR A CD1 1 
ATOM   677  C CD2 . TYR A 1 88  ? 8.575   2.851   -7.981  1.00 24.34 ?  311 TYR A CD2 1 
ATOM   678  C CE1 . TYR A 1 88  ? 7.153   5.142   -8.566  1.00 21.38 ?  311 TYR A CE1 1 
ATOM   679  C CE2 . TYR A 1 88  ? 7.256   2.962   -7.585  1.00 23.80 ?  311 TYR A CE2 1 
ATOM   680  C CZ  . TYR A 1 88  ? 6.550   4.109   -7.881  1.00 22.25 ?  311 TYR A CZ  1 
ATOM   681  O OH  . TYR A 1 88  ? 5.237   4.224   -7.489  1.00 24.45 ?  311 TYR A OH  1 
ATOM   682  N N   . ASP A 1 89  ? 10.723  5.829   -6.332  1.00 25.42 ?  312 ASP A N   1 
ATOM   683  C CA  . ASP A 1 89  ? 10.378  5.940   -4.925  1.00 27.91 ?  312 ASP A CA  1 
ATOM   684  C C   . ASP A 1 89  ? 8.877   5.760   -4.763  1.00 27.23 ?  312 ASP A C   1 
ATOM   685  O O   . ASP A 1 89  ? 8.107   6.597   -5.258  1.00 27.64 ?  312 ASP A O   1 
ATOM   686  C CB  . ASP A 1 89  ? 10.817  7.294   -4.373  1.00 24.63 ?  312 ASP A CB  1 
ATOM   687  C CG  . ASP A 1 89  ? 10.475  7.469   -2.908  1.00 32.36 ?  312 ASP A CG  1 
ATOM   688  O OD1 . ASP A 1 89  ? 10.209  6.458   -2.223  1.00 32.17 ?  312 ASP A OD1 1 
ATOM   689  O OD2 . ASP A 1 89  ? 10.471  8.626   -2.437  1.00 38.60 -1 312 ASP A OD2 1 
ATOM   690  N N   . PRO A 1 90  ? 8.411   4.705   -4.087  1.00 28.65 ?  313 PRO A N   1 
ATOM   691  C CA  . PRO A 1 90  ? 6.961   4.501   -3.943  1.00 24.39 ?  313 PRO A CA  1 
ATOM   692  C C   . PRO A 1 90  ? 6.266   5.536   -3.069  1.00 26.71 ?  313 PRO A C   1 
ATOM   693  O O   . PRO A 1 90  ? 5.029   5.532   -3.017  1.00 25.02 ?  313 PRO A O   1 
ATOM   694  C CB  . PRO A 1 90  ? 6.864   3.102   -3.316  1.00 27.01 ?  313 PRO A CB  1 
ATOM   695  C CG  . PRO A 1 90  ? 8.183   2.450   -3.623  1.00 26.23 ?  313 PRO A CG  1 
ATOM   696  C CD  . PRO A 1 90  ? 9.179   3.564   -3.565  1.00 26.88 ?  313 PRO A CD  1 
ATOM   697  N N   . THR A 1 91  ? 7.001   6.414   -2.387  1.00 27.12 ?  314 THR A N   1 
ATOM   698  C CA  . THR A 1 91  ? 6.397   7.392   -1.492  1.00 27.58 ?  314 THR A CA  1 
ATOM   699  C C   . THR A 1 91  ? 6.165   8.747   -2.149  1.00 26.33 ?  314 THR A C   1 
ATOM   700  O O   . THR A 1 91  ? 5.591   9.635   -1.510  1.00 24.94 ?  314 THR A O   1 
ATOM   701  C CB  . THR A 1 91  ? 7.255   7.568   -0.233  1.00 27.71 ?  314 THR A CB  1 
ATOM   702  O OG1 . THR A 1 91  ? 8.604   7.880   -0.603  1.00 30.31 ?  314 THR A OG1 1 
ATOM   703  C CG2 . THR A 1 91  ? 7.244   6.295   0.601   1.00 25.26 ?  314 THR A CG2 1 
ATOM   704  N N   . GLU A 1 92  ? 6.591   8.933   -3.398  1.00 25.59 ?  315 GLU A N   1 
ATOM   705  C CA  . GLU A 1 92  ? 6.246   10.152  -4.115  1.00 27.80 ?  315 GLU A CA  1 
ATOM   706  C C   . GLU A 1 92  ? 4.731   10.245  -4.274  1.00 26.14 ?  315 GLU A C   1 
ATOM   707  O O   . GLU A 1 92  ? 4.036   9.235   -4.414  1.00 26.16 ?  315 GLU A O   1 
ATOM   708  C CB  . GLU A 1 92  ? 6.936   10.188  -5.483  1.00 27.77 ?  315 GLU A CB  1 
ATOM   709  C CG  . GLU A 1 92  ? 6.547   11.384  -6.352  1.00 35.37 ?  315 GLU A CG  1 
ATOM   710  C CD  . GLU A 1 92  ? 7.548   11.673  -7.457  1.00 43.87 ?  315 GLU A CD  1 
ATOM   711  O OE1 . GLU A 1 92  ? 8.571   10.961  -7.539  1.00 44.04 ?  315 GLU A OE1 1 
ATOM   712  O OE2 . GLU A 1 92  ? 7.307   12.613  -8.246  1.00 43.59 -1 315 GLU A OE2 1 
ATOM   713  N N   . GLU A 1 93  ? 4.217   11.475  -4.239  1.00 27.80 ?  316 GLU A N   1 
ATOM   714  C CA  . GLU A 1 93  ? 2.773   11.720  -4.223  1.00 28.84 ?  316 GLU A CA  1 
ATOM   715  C C   . GLU A 1 93  ? 2.192   11.597  -5.635  1.00 26.11 ?  316 GLU A C   1 
ATOM   716  O O   . GLU A 1 93  ? 1.694   12.554  -6.230  1.00 25.82 ?  316 GLU A O   1 
ATOM   717  C CB  . GLU A 1 93  ? 2.479   13.089  -3.625  1.00 30.29 ?  316 GLU A CB  1 
ATOM   718  C CG  . GLU A 1 93  ? 2.924   13.254  -2.180  1.00 31.75 ?  316 GLU A CG  1 
ATOM   719  C CD  . GLU A 1 93  ? 2.218   14.404  -1.488  1.00 39.61 ?  316 GLU A CD  1 
ATOM   720  O OE1 . GLU A 1 93  ? 1.971   15.435  -2.149  1.00 37.67 ?  316 GLU A OE1 1 
ATOM   721  O OE2 . GLU A 1 93  ? 1.911   14.279  -0.283  1.00 40.93 -1 316 GLU A OE2 1 
ATOM   722  N N   . ILE A 1 94  ? 2.248   10.379  -6.165  1.00 27.02 ?  317 ILE A N   1 
ATOM   723  C CA  . ILE A 1 94  ? 1.666   10.072  -7.473  1.00 24.68 ?  317 ILE A CA  1 
ATOM   724  C C   . ILE A 1 94  ? 0.977   8.717   -7.406  1.00 24.47 ?  317 ILE A C   1 
ATOM   725  O O   . ILE A 1 94  ? 1.286   7.886   -6.541  1.00 24.92 ?  317 ILE A O   1 
ATOM   726  C CB  . ILE A 1 94  ? 2.726   10.074  -8.596  1.00 25.46 ?  317 ILE A CB  1 
ATOM   727  C CG1 . ILE A 1 94  ? 3.857   9.095   -8.275  1.00 24.60 ?  317 ILE A CG1 1 
ATOM   728  C CG2 . ILE A 1 94  ? 3.259   11.484  -8.840  1.00 25.99 ?  317 ILE A CG2 1 
ATOM   729  C CD1 . ILE A 1 94  ? 5.049   9.221   -9.201  1.00 24.21 ?  317 ILE A CD1 1 
ATOM   730  N N   . PRO A 1 95  ? 0.019   8.470   -8.309  1.00 24.90 ?  318 PRO A N   1 
ATOM   731  C CA  . PRO A 1 95  ? -0.669  7.167   -8.291  1.00 21.61 ?  318 PRO A CA  1 
ATOM   732  C C   . PRO A 1 95  ? 0.225   6.007   -8.684  1.00 19.83 ?  318 PRO A C   1 
ATOM   733  O O   . PRO A 1 95  ? 0.005   4.884   -8.212  1.00 17.98 ?  318 PRO A O   1 
ATOM   734  C CB  . PRO A 1 95  ? -1.812  7.354   -9.301  1.00 20.19 ?  318 PRO A CB  1 
ATOM   735  C CG  . PRO A 1 95  ? -1.945  8.829   -9.484  1.00 20.04 ?  318 PRO A CG  1 
ATOM   736  C CD  . PRO A 1 95  ? -0.570  9.382   -9.304  1.00 22.19 ?  318 PRO A CD  1 
ATOM   737  N N   . ALA A 1 96  ? 1.222   6.243   -9.530  1.00 21.03 ?  319 ALA A N   1 
ATOM   738  C CA  . ALA A 1 96  ? 2.060   5.198   -10.102 1.00 20.32 ?  319 ALA A CA  1 
ATOM   739  C C   . ALA A 1 96  ? 3.246   5.862   -10.791 1.00 20.26 ?  319 ALA A C   1 
ATOM   740  O O   . ALA A 1 96  ? 3.262   7.094   -10.917 1.00 19.69 ?  319 ALA A O   1 
ATOM   741  C CB  . ALA A 1 96  ? 1.248   4.347   -11.082 1.00 20.23 ?  319 ALA A CB  1 
ATOM   742  N N   . PRO A 1 97  ? 4.262   5.112   -11.228 1.00 20.94 ?  320 PRO A N   1 
ATOM   743  C CA  . PRO A 1 97  ? 5.338   5.730   -12.010 1.00 18.86 ?  320 PRO A CA  1 
ATOM   744  C C   . PRO A 1 97  ? 4.776   6.465   -13.217 1.00 21.63 ?  320 PRO A C   1 
ATOM   745  O O   . PRO A 1 97  ? 3.839   6.000   -13.869 1.00 21.72 ?  320 PRO A O   1 
ATOM   746  C CB  . PRO A 1 97  ? 6.208   4.539   -12.425 1.00 20.73 ?  320 PRO A CB  1 
ATOM   747  C CG  . PRO A 1 97  ? 5.957   3.513   -11.394 1.00 23.27 ?  320 PRO A CG  1 
ATOM   748  C CD  . PRO A 1 97  ? 4.538   3.691   -10.946 1.00 22.87 ?  320 PRO A CD  1 
ATOM   749  N N   . LEU A 1 98  ? 5.346   7.635   -13.496 1.00 21.02 ?  321 LEU A N   1 
ATOM   750  C CA  . LEU A 1 98  ? 4.834   8.483   -14.564 1.00 18.96 ?  321 LEU A CA  1 
ATOM   751  C C   . LEU A 1 98  ? 4.849   7.738   -15.892 1.00 20.08 ?  321 LEU A C   1 
ATOM   752  O O   . LEU A 1 98  ? 5.834   7.081   -16.239 1.00 20.03 ?  321 LEU A O   1 
ATOM   753  C CB  . LEU A 1 98  ? 5.663   9.764   -14.654 1.00 17.96 ?  321 LEU A CB  1 
ATOM   754  C CG  . LEU A 1 98  ? 5.654   10.629  -13.391 1.00 18.43 ?  321 LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 98  ? 6.324   11.971  -13.638 1.00 21.47 ?  321 LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 98  ? 4.235   10.823  -12.878 1.00 17.72 ?  321 LEU A CD2 1 
ATOM   757  N N   . GLY A 1 99  ? 3.744   7.830   -16.627 1.00 21.42 ?  322 GLY A N   1 
ATOM   758  C CA  . GLY A 1 99  ? 3.580   7.096   -17.862 1.00 20.56 ?  322 GLY A CA  1 
ATOM   759  C C   . GLY A 1 99  ? 2.942   5.732   -17.713 1.00 21.19 ?  322 GLY A C   1 
ATOM   760  O O   . GLY A 1 99  ? 2.748   5.045   -18.725 1.00 18.29 ?  322 GLY A O   1 
ATOM   761  N N   . THR A 1 100 ? 2.620   5.319   -16.490 1.00 24.75 ?  323 THR A N   1 
ATOM   762  C CA  . THR A 1 100 ? 1.977   4.033   -16.267 1.00 22.15 ?  323 THR A CA  1 
ATOM   763  C C   . THR A 1 100 ? 0.639   3.985   -17.002 1.00 19.99 ?  323 THR A C   1 
ATOM   764  O O   . THR A 1 100 ? -0.081  4.990   -17.041 1.00 20.91 ?  323 THR A O   1 
ATOM   765  C CB  . THR A 1 100 ? 1.771   3.806   -14.765 1.00 19.49 ?  323 THR A CB  1 
ATOM   766  O OG1 . THR A 1 100 ? 3.041   3.605   -14.132 1.00 21.26 ?  323 THR A OG1 1 
ATOM   767  C CG2 . THR A 1 100 ? 0.880   2.602   -14.493 1.00 17.77 ?  323 THR A CG2 1 
ATOM   768  N N   . PRO A 1 101 ? 0.290   2.855   -17.621 1.00 20.34 ?  324 PRO A N   1 
ATOM   769  C CA  . PRO A 1 101 ? -1.017  2.749   -18.283 1.00 20.92 ?  324 PRO A CA  1 
ATOM   770  C C   . PRO A 1 101 ? -2.157  3.052   -17.321 1.00 19.92 ?  324 PRO A C   1 
ATOM   771  O O   . PRO A 1 101 ? -2.120  2.681   -16.146 1.00 20.43 ?  324 PRO A O   1 
ATOM   772  C CB  . PRO A 1 101 ? -1.058  1.294   -18.764 1.00 19.26 ?  324 PRO A CB  1 
ATOM   773  C CG  . PRO A 1 101 ? 0.366   0.871   -18.847 1.00 17.41 ?  324 PRO A CG  1 
ATOM   774  C CD  . PRO A 1 101 ? 1.122   1.655   -17.821 1.00 21.77 ?  324 PRO A CD  1 
ATOM   775  N N   . ASP A 1 102 ? -3.176  3.744   -17.832 1.00 17.26 ?  325 ASP A N   1 
ATOM   776  C CA  . ASP A 1 102 ? -4.298  4.201   -17.022 1.00 17.33 ?  325 ASP A CA  1 
ATOM   777  C C   . ASP A 1 102 ? -5.607  3.509   -17.395 1.00 19.62 ?  325 ASP A C   1 
ATOM   778  O O   . ASP A 1 102 ? -6.684  4.089   -17.244 1.00 21.86 ?  325 ASP A O   1 
ATOM   779  C CB  . ASP A 1 102 ? -4.446  5.721   -17.121 1.00 17.57 ?  325 ASP A CB  1 
ATOM   780  C CG  . ASP A 1 102 ? -4.769  6.201   -18.534 1.00 20.89 ?  325 ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 102 ? -5.015  5.368   -19.433 1.00 18.35 ?  325 ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 102 ? -4.780  7.432   -18.745 1.00 21.08 -1 325 ASP A OD2 1 
ATOM   783  N N   . PHE A 1 103 ? -5.532  2.273   -17.883 1.00 16.70 ?  326 PHE A N   1 
ATOM   784  C CA  . PHE A 1 103 ? -6.732  1.539   -18.252 1.00 19.33 ?  326 PHE A CA  1 
ATOM   785  C C   . PHE A 1 103 ? -6.468  0.046   -18.139 1.00 19.80 ?  326 PHE A C   1 
ATOM   786  O O   . PHE A 1 103 ? -5.327  -0.410  -18.254 1.00 19.16 ?  326 PHE A O   1 
ATOM   787  C CB  . PHE A 1 103 ? -7.204  1.902   -19.668 1.00 17.52 ?  326 PHE A CB  1 
ATOM   788  C CG  . PHE A 1 103 ? -6.193  1.619   -20.745 1.00 16.07 ?  326 PHE A CG  1 
ATOM   789  C CD1 . PHE A 1 103 ? -6.106  0.363   -21.325 1.00 19.40 ?  326 PHE A CD1 1 
ATOM   790  C CD2 . PHE A 1 103 ? -5.335  2.613   -21.182 1.00 17.99 ?  326 PHE A CD2 1 
ATOM   791  C CE1 . PHE A 1 103 ? -5.178  0.105   -22.317 1.00 20.82 ?  326 PHE A CE1 1 
ATOM   792  C CE2 . PHE A 1 103 ? -4.405  2.361   -22.173 1.00 19.73 ?  326 PHE A CE2 1 
ATOM   793  C CZ  . PHE A 1 103 ? -4.327  1.106   -22.742 1.00 19.75 ?  326 PHE A CZ  1 
ATOM   794  N N   . VAL A 1 104 ? -7.538  -0.710  -17.918 1.00 21.60 ?  327 VAL A N   1 
ATOM   795  C CA  . VAL A 1 104 ? -7.452  -2.154  -17.741 1.00 21.44 ?  327 VAL A CA  1 
ATOM   796  C C   . VAL A 1 104 ? -7.479  -2.827  -19.106 1.00 24.15 ?  327 VAL A C   1 
ATOM   797  O O   . VAL A 1 104 ? -8.377  -2.574  -19.918 1.00 23.96 ?  327 VAL A O   1 
ATOM   798  C CB  . VAL A 1 104 ? -8.594  -2.667  -16.849 1.00 22.71 ?  327 VAL A CB  1 
ATOM   799  C CG1 . VAL A 1 104 ? -8.631  -4.186  -16.863 1.00 20.87 ?  327 VAL A CG1 1 
ATOM   800  C CG2 . VAL A 1 104 ? -8.430  -2.148  -15.428 1.00 23.42 ?  327 VAL A CG2 1 
ATOM   801  N N   . GLY A 1 105 ? -6.496  -3.683  -19.357 1.00 24.99 ?  328 GLY A N   1 
ATOM   802  C CA  . GLY A 1 105 ? -6.422  -4.399  -20.614 1.00 21.43 ?  328 GLY A CA  1 
ATOM   803  C C   . GLY A 1 105 ? -5.103  -5.129  -20.733 1.00 23.37 ?  328 GLY A C   1 
ATOM   804  O O   . GLY A 1 105 ? -4.217  -5.012  -19.880 1.00 20.84 ?  328 GLY A O   1 
ATOM   805  N N   . LYS A 1 106 ? -4.990  -5.896  -21.816 1.00 18.28 ?  329 LYS A N   1 
ATOM   806  C CA  . LYS A 1 106 ? -3.779  -6.649  -22.126 1.00 21.78 ?  329 LYS A CA  1 
ATOM   807  C C   . LYS A 1 106 ? -3.031  -5.914  -23.232 1.00 22.32 ?  329 LYS A C   1 
ATOM   808  O O   . LYS A 1 106 ? -3.476  -5.890  -24.384 1.00 22.74 ?  329 LYS A O   1 
ATOM   809  C CB  . LYS A 1 106 ? -4.115  -8.080  -22.539 1.00 21.56 ?  329 LYS A CB  1 
ATOM   810  C CG  . LYS A 1 106 ? -5.329  -8.647  -21.834 1.00 23.46 ?  329 LYS A CG  1 
ATOM   811  C CD  . LYS A 1 106 ? -5.306  -10.164 -21.775 1.00 26.85 ?  329 LYS A CD  1 
ATOM   812  C CE  . LYS A 1 106 ? -6.260  -10.679 -20.707 1.00 27.92 ?  329 LYS A CE  1 
ATOM   813  N NZ  . LYS A 1 106 ? -7.534  -11.185 -21.290 1.00 31.80 ?  329 LYS A NZ  1 
ATOM   814  N N   . ILE A 1 107 ? -1.898  -5.315  -22.878 1.00 20.85 ?  330 ILE A N   1 
ATOM   815  C CA  . ILE A 1 107 ? -1.106  -4.509  -23.798 1.00 20.26 ?  330 ILE A CA  1 
ATOM   816  C C   . ILE A 1 107 ? 0.058   -5.355  -24.295 1.00 18.93 ?  330 ILE A C   1 
ATOM   817  O O   . ILE A 1 107 ? 0.879   -5.827  -23.500 1.00 22.98 ?  330 ILE A O   1 
ATOM   818  C CB  . ILE A 1 107 ? -0.608  -3.220  -23.126 1.00 18.59 ?  330 ILE A CB  1 
ATOM   819  C CG1 . ILE A 1 107 ? -1.796  -2.357  -22.693 1.00 17.27 ?  330 ILE A CG1 1 
ATOM   820  C CG2 . ILE A 1 107 ? 0.308   -2.449  -24.064 1.00 19.79 ?  330 ILE A CG2 1 
ATOM   821  C CD1 . ILE A 1 107 ? -1.457  -1.342  -21.624 1.00 20.34 ?  330 ILE A CD1 1 
ATOM   822  N N   . GLN A 1 108 ? 0.129   -5.546  -25.608 1.00 20.05 ?  331 GLN A N   1 
ATOM   823  C CA  . GLN A 1 108 ? 1.180   -6.335  -26.230 1.00 20.06 ?  331 GLN A CA  1 
ATOM   824  C C   . GLN A 1 108 ? 2.294   -5.426  -26.732 1.00 21.15 ?  331 GLN A C   1 
ATOM   825  O O   . GLN A 1 108 ? 2.036   -4.334  -27.248 1.00 20.18 ?  331 GLN A O   1 
ATOM   826  C CB  . GLN A 1 108 ? 0.626   -7.167  -27.388 1.00 20.66 ?  331 GLN A CB  1 
ATOM   827  C CG  . GLN A 1 108 ? 1.477   -8.373  -27.739 1.00 23.03 ?  331 GLN A CG  1 
ATOM   828  C CD  . GLN A 1 108 ? 0.654   -9.542  -28.238 1.00 28.65 ?  331 GLN A CD  1 
ATOM   829  O OE1 . GLN A 1 108 ? 0.448   -9.702  -29.441 1.00 26.21 ?  331 GLN A OE1 1 
ATOM   830  N NE2 . GLN A 1 108 ? 0.176   -10.367 -27.313 1.00 28.16 ?  331 GLN A NE2 1 
ATOM   831  N N   . GLY A 1 109 ? 3.522   -5.881  -26.577 1.00 21.82 ?  332 GLY A N   1 
ATOM   832  C CA  . GLY A 1 109 ? 4.679   -5.140  -27.039 1.00 20.72 ?  332 GLY A CA  1 
ATOM   833  C C   . GLY A 1 109 ? 5.887   -6.044  -27.125 1.00 23.53 ?  332 GLY A C   1 
ATOM   834  O O   . GLY A 1 109 ? 5.770   -7.239  -27.404 1.00 25.07 ?  332 GLY A O   1 
ATOM   835  N N   . VAL A 1 110 ? 7.062   -5.466  -26.885 1.00 23.36 ?  333 VAL A N   1 
ATOM   836  C CA  . VAL A 1 110 ? 8.325   -6.193  -26.941 1.00 22.99 ?  333 VAL A CA  1 
ATOM   837  C C   . VAL A 1 110 ? 9.163   -5.822  -25.726 1.00 22.27 ?  333 VAL A C   1 
ATOM   838  O O   . VAL A 1 110 ? 9.232   -4.649  -25.341 1.00 20.60 ?  333 VAL A O   1 
ATOM   839  C CB  . VAL A 1 110 ? 9.102   -5.896  -28.244 1.00 21.60 ?  333 VAL A CB  1 
ATOM   840  C CG1 . VAL A 1 110 ? 10.439  -6.625  -28.249 1.00 21.35 ?  333 VAL A CG1 1 
ATOM   841  C CG2 . VAL A 1 110 ? 8.282   -6.288  -29.462 1.00 22.38 ?  333 VAL A CG2 1 
ATOM   842  N N   . LEU A 1 111 ? 9.792   -6.825  -25.119 1.00 23.63 ?  334 LEU A N   1 
ATOM   843  C CA  . LEU A 1 111 ? 10.781  -6.621  -24.069 1.00 21.90 ?  334 LEU A CA  1 
ATOM   844  C C   . LEU A 1 111 ? 12.169  -6.681  -24.696 1.00 24.59 ?  334 LEU A C   1 
ATOM   845  O O   . LEU A 1 111 ? 12.539  -7.699  -25.290 1.00 26.36 ?  334 LEU A O   1 
ATOM   846  C CB  . LEU A 1 111 ? 10.648  -7.675  -22.970 1.00 21.83 ?  334 LEU A CB  1 
ATOM   847  C CG  . LEU A 1 111 ? 9.715   -7.399  -21.791 1.00 21.35 ?  334 LEU A CG  1 
ATOM   848  C CD1 . LEU A 1 111 ? 9.702   -8.595  -20.853 1.00 22.88 ?  334 LEU A CD1 1 
ATOM   849  C CD2 . LEU A 1 111 ? 10.133  -6.138  -21.052 1.00 20.41 ?  334 LEU A CD2 1 
ATOM   850  N N   . THR A 1 112 ? 12.927  -5.597  -24.569 1.00 24.19 ?  335 THR A N   1 
ATOM   851  C CA  . THR A 1 112 ? 14.290  -5.530  -25.072 1.00 26.59 ?  335 THR A CA  1 
ATOM   852  C C   . THR A 1 112 ? 15.268  -5.453  -23.907 1.00 27.70 ?  335 THR A C   1 
ATOM   853  O O   . THR A 1 112 ? 14.958  -4.898  -22.849 1.00 23.61 ?  335 THR A O   1 
ATOM   854  C CB  . THR A 1 112 ? 14.487  -4.325  -25.999 1.00 25.59 ?  335 THR A CB  1 
ATOM   855  O OG1 . THR A 1 112 ? 13.965  -3.146  -25.375 1.00 27.05 ?  335 THR A OG1 1 
ATOM   856  C CG2 . THR A 1 112 ? 13.772  -4.551  -27.324 1.00 24.27 ?  335 THR A CG2 1 
ATOM   857  N N   . GLN A 1 113 ? 16.456  -6.019  -24.109 1.00 22.46 ?  336 GLN A N   1 
ATOM   858  C CA  . GLN A 1 113 ? 17.462  -6.066  -23.059 1.00 25.72 ?  336 GLN A CA  1 
ATOM   859  C C   . GLN A 1 113 ? 18.845  -5.923  -23.672 1.00 28.35 ?  336 GLN A C   1 
ATOM   860  O O   . GLN A 1 113 ? 19.136  -6.524  -24.709 1.00 27.07 ?  336 GLN A O   1 
ATOM   861  C CB  . GLN A 1 113 ? 17.376  -7.372  -22.262 1.00 25.73 ?  336 GLN A CB  1 
ATOM   862  C CG  . GLN A 1 113 ? 17.966  -7.285  -20.867 1.00 27.21 ?  336 GLN A CG  1 
ATOM   863  C CD  . GLN A 1 113 ? 18.093  -8.641  -20.205 1.00 27.24 ?  336 GLN A CD  1 
ATOM   864  O OE1 . GLN A 1 113 ? 18.871  -9.488  -20.643 1.00 28.72 ?  336 GLN A OE1 1 
ATOM   865  N NE2 . GLN A 1 113 ? 17.323  -8.856  -19.145 1.00 27.36 ?  336 GLN A NE2 1 
ATOM   866  N N   . THR A 1 114 ? 19.690  -5.125  -23.024 1.00 23.69 ?  337 THR A N   1 
ATOM   867  C CA  . THR A 1 114 ? 21.085  -4.963  -23.406 1.00 24.70 ?  337 THR A CA  1 
ATOM   868  C C   . THR A 1 114 ? 21.963  -5.325  -22.219 1.00 26.41 ?  337 THR A C   1 
ATOM   869  O O   . THR A 1 114 ? 21.760  -4.812  -21.113 1.00 25.42 ?  337 THR A O   1 
ATOM   870  C CB  . THR A 1 114 ? 21.383  -3.529  -23.860 1.00 24.73 ?  337 THR A CB  1 
ATOM   871  O OG1 . THR A 1 114 ? 20.546  -3.189  -24.972 1.00 26.76 ?  337 THR A OG1 1 
ATOM   872  C CG2 . THR A 1 114 ? 22.846  -3.388  -24.265 1.00 23.42 ?  337 THR A CG2 1 
ATOM   873  N N   . THR A 1 115 ? 22.926  -6.213  -22.444 1.00 27.40 ?  338 THR A N   1 
ATOM   874  C CA  . THR A 1 115 ? 23.905  -6.566  -21.426 1.00 29.79 ?  338 THR A CA  1 
ATOM   875  C C   . THR A 1 115 ? 25.071  -5.590  -21.515 1.00 29.25 ?  338 THR A C   1 
ATOM   876  O O   . THR A 1 115 ? 25.697  -5.458  -22.572 1.00 27.69 ?  338 THR A O   1 
ATOM   877  C CB  . THR A 1 115 ? 24.385  -8.005  -21.603 1.00 31.46 ?  338 THR A CB  1 
ATOM   878  O OG1 . THR A 1 115 ? 23.320  -8.908  -21.278 1.00 31.55 ?  338 THR A OG1 1 
ATOM   879  C CG2 . THR A 1 115 ? 25.569  -8.283  -20.690 1.00 27.86 ?  338 THR A CG2 1 
ATOM   880  N N   . ARG A 1 116 ? 25.360  -4.907  -20.408 1.00 31.20 ?  339 ARG A N   1 
ATOM   881  C CA  . ARG A 1 116 ? 26.355  -3.842  -20.402 1.00 30.77 ?  339 ARG A CA  1 
ATOM   882  C C   . ARG A 1 116 ? 27.791  -4.350  -20.453 1.00 28.84 ?  339 ARG A C   1 
ATOM   883  O O   . ARG A 1 116 ? 28.704  -3.541  -20.648 1.00 31.99 ?  339 ARG A O   1 
ATOM   884  C CB  . ARG A 1 116 ? 26.169  -2.963  -19.164 1.00 30.91 ?  339 ARG A CB  1 
ATOM   885  C CG  . ARG A 1 116 ? 26.770  -3.544  -17.899 1.00 33.34 ?  339 ARG A CG  1 
ATOM   886  C CD  . ARG A 1 116 ? 26.334  -2.760  -16.672 1.00 29.99 ?  339 ARG A CD  1 
ATOM   887  N NE  . ARG A 1 116 ? 25.172  -3.367  -16.036 1.00 31.32 ?  339 ARG A NE  1 
ATOM   888  C CZ  . ARG A 1 116 ? 23.992  -2.776  -15.912 1.00 29.53 ?  339 ARG A CZ  1 
ATOM   889  N NH1 . ARG A 1 116 ? 23.785  -1.546  -16.353 1.00 33.61 ?  339 ARG A NH1 1 
ATOM   890  N NH2 . ARG A 1 116 ? 22.994  -3.435  -15.331 1.00 28.77 ?  339 ARG A NH2 1 
ATOM   891  N N   . THR A 1 117 ? 28.017  -5.655  -20.283 1.00 30.58 ?  340 THR A N   1 
ATOM   892  C CA  . THR A 1 117 ? 29.376  -6.183  -20.292 1.00 33.73 ?  340 THR A CA  1 
ATOM   893  C C   . THR A 1 117 ? 29.912  -6.411  -21.699 1.00 31.08 ?  340 THR A C   1 
ATOM   894  O O   . THR A 1 117 ? 31.133  -6.484  -21.877 1.00 33.19 ?  340 THR A O   1 
ATOM   895  C CB  . THR A 1 117 ? 29.448  -7.492  -19.501 1.00 31.74 ?  340 THR A CB  1 
ATOM   896  O OG1 . THR A 1 117 ? 29.097  -8.591  -20.350 1.00 36.29 ?  340 THR A OG1 1 
ATOM   897  C CG2 . THR A 1 117 ? 28.499  -7.450  -18.311 1.00 32.75 ?  340 THR A CG2 1 
ATOM   898  N N   . ASP A 1 118 ? 29.036  -6.522  -22.695 1.00 28.96 ?  341 ASP A N   1 
ATOM   899  C CA  . ASP A 1 118 ? 29.499  -6.714  -24.064 1.00 30.84 ?  341 ASP A CA  1 
ATOM   900  C C   . ASP A 1 118 ? 28.549  -6.170  -25.122 1.00 29.24 ?  341 ASP A C   1 
ATOM   901  O O   . ASP A 1 118 ? 28.822  -6.359  -26.311 1.00 26.39 ?  341 ASP A O   1 
ATOM   902  C CB  . ASP A 1 118 ? 29.763  -8.206  -24.326 1.00 27.01 ?  341 ASP A CB  1 
ATOM   903  C CG  . ASP A 1 118 ? 28.519  -9.060  -24.181 1.00 28.36 ?  341 ASP A CG  1 
ATOM   904  O OD1 . ASP A 1 118 ? 27.502  -8.565  -23.653 1.00 28.95 ?  341 ASP A OD1 1 
ATOM   905  O OD2 . ASP A 1 118 ? 28.561  -10.235 -24.603 1.00 32.81 -1 341 ASP A OD2 1 
ATOM   906  N N   . GLY A 1 119 ? 27.452  -5.512  -24.750 1.00 24.56 ?  342 GLY A N   1 
ATOM   907  C CA  . GLY A 1 119 ? 26.555  -4.962  -25.745 1.00 23.85 ?  342 GLY A CA  1 
ATOM   908  C C   . GLY A 1 119 ? 25.726  -5.978  -26.495 1.00 25.68 ?  342 GLY A C   1 
ATOM   909  O O   . GLY A 1 119 ? 25.258  -5.684  -27.597 1.00 30.08 ?  342 GLY A O   1 
ATOM   910  N N   . SER A 1 120 ? 25.540  -7.173  -25.939 1.00 26.66 ?  343 SER A N   1 
ATOM   911  C CA  . SER A 1 120 ? 24.640  -8.151  -26.532 1.00 28.54 ?  343 SER A CA  1 
ATOM   912  C C   . SER A 1 120 ? 23.200  -7.782  -26.204 1.00 26.12 ?  343 SER A C   1 
ATOM   913  O O   . SER A 1 120 ? 22.903  -7.310  -25.102 1.00 25.74 ?  343 SER A O   1 
ATOM   914  C CB  . SER A 1 120 ? 24.954  -9.560  -26.024 1.00 26.14 ?  343 SER A CB  1 
ATOM   915  O OG  . SER A 1 120 ? 24.529  -9.734  -24.683 1.00 30.66 ?  343 SER A OG  1 
ATOM   916  N N   . THR A 1 121 ? 22.307  -7.985  -27.171 1.00 29.97 ?  344 THR A N   1 
ATOM   917  C CA  . THR A 1 121 ? 20.921  -7.560  -27.046 1.00 28.10 ?  344 THR A CA  1 
ATOM   918  C C   . THR A 1 121 ? 19.978  -8.694  -27.424 1.00 27.38 ?  344 THR A C   1 
ATOM   919  O O   . THR A 1 121 ? 20.372  -9.678  -28.056 1.00 24.62 ?  344 THR A O   1 
ATOM   920  C CB  . THR A 1 121 ? 20.625  -6.331  -27.920 1.00 27.95 ?  344 THR A CB  1 
ATOM   921  O OG1 . THR A 1 121 ? 20.722  -6.690  -29.303 1.00 29.44 ?  344 THR A OG1 1 
ATOM   922  C CG2 . THR A 1 121 ? 21.604  -5.204  -27.619 1.00 24.49 ?  344 THR A CG2 1 
ATOM   923  N N   . ARG A 1 122 ? 18.716  -8.538  -27.028 1.00 27.61 ?  345 ARG A N   1 
ATOM   924  C CA  . ARG A 1 122 ? 17.687  -9.524  -27.321 1.00 26.31 ?  345 ARG A CA  1 
ATOM   925  C C   . ARG A 1 122 ? 16.321  -8.868  -27.191 1.00 25.04 ?  345 ARG A C   1 
ATOM   926  O O   . ARG A 1 122 ? 16.143  -7.917  -26.424 1.00 23.76 ?  345 ARG A O   1 
ATOM   927  C CB  . ARG A 1 122 ? 17.784  -10.736 -26.389 1.00 20.04 ?  345 ARG A CB  1 
ATOM   928  C CG  . ARG A 1 122 ? 17.558  -10.400 -24.927 1.00 27.26 ?  345 ARG A CG  1 
ATOM   929  C CD  . ARG A 1 122 ? 18.466  -11.214 -24.026 1.00 28.30 ?  345 ARG A CD  1 
ATOM   930  N NE  . ARG A 1 122 ? 19.867  -11.095 -24.410 1.00 29.21 ?  345 ARG A NE  1 
ATOM   931  C CZ  . ARG A 1 122 ? 20.774  -10.410 -23.728 1.00 28.30 ?  345 ARG A CZ  1 
ATOM   932  N NH1 . ARG A 1 122 ? 20.461  -9.764  -22.617 1.00 26.13 ?  345 ARG A NH1 1 
ATOM   933  N NH2 . ARG A 1 122 ? 22.027  -10.370 -24.173 1.00 24.39 ?  345 ARG A NH2 1 
ATOM   934  N N   . GLY A 1 123 ? 15.363  -9.388  -27.952 1.00 25.49 ?  346 GLY A N   1 
ATOM   935  C CA  . GLY A 1 123 ? 13.995  -8.913  -27.894 1.00 26.23 ?  346 GLY A CA  1 
ATOM   936  C C   . GLY A 1 123 ? 13.002  -10.056 -27.921 1.00 28.08 ?  346 GLY A C   1 
ATOM   937  O O   . GLY A 1 123 ? 13.222  -11.057 -28.610 1.00 29.66 ?  346 GLY A O   1 
ATOM   938  N N   . HIS A 1 124 ? 11.908  -9.926  -27.175 1.00 24.99 ?  347 HIS A N   1 
ATOM   939  C CA  . HIS A 1 124 ? 10.903  -10.975 -27.100 1.00 26.35 ?  347 HIS A CA  1 
ATOM   940  C C   . HIS A 1 124 ? 9.518   -10.355 -27.018 1.00 26.61 ?  347 HIS A C   1 
ATOM   941  O O   . HIS A 1 124 ? 9.332   -9.312  -26.384 1.00 25.11 ?  347 HIS A O   1 
ATOM   942  C CB  . HIS A 1 124 ? 11.134  -11.889 -25.890 1.00 28.97 ?  347 HIS A CB  1 
ATOM   943  C CG  . HIS A 1 124 ? 12.347  -12.756 -26.012 1.00 30.18 ?  347 HIS A CG  1 
ATOM   944  N ND1 . HIS A 1 124 ? 12.335  -13.964 -26.675 1.00 28.35 ?  347 HIS A ND1 1 
ATOM   945  C CD2 . HIS A 1 124 ? 13.611  -12.590 -25.556 1.00 28.53 ?  347 HIS A CD2 1 
ATOM   946  C CE1 . HIS A 1 124 ? 13.539  -14.505 -26.623 1.00 29.16 ?  347 HIS A CE1 1 
ATOM   947  N NE2 . HIS A 1 124 ? 14.332  -13.692 -25.949 1.00 31.35 ?  347 HIS A NE2 1 
ATOM   948  N N   . LYS A 1 125 ? 8.553   -11.000 -27.671 1.00 27.30 ?  348 LYS A N   1 
ATOM   949  C CA  . LYS A 1 125 ? 7.161   -10.598 -27.536 1.00 26.78 ?  348 LYS A CA  1 
ATOM   950  C C   . LYS A 1 125 ? 6.735   -10.706 -26.079 1.00 25.73 ?  348 LYS A C   1 
ATOM   951  O O   . LYS A 1 125 ? 7.017   -11.704 -25.410 1.00 24.79 ?  348 LYS A O   1 
ATOM   952  C CB  . LYS A 1 125 ? 6.271   -11.473 -28.421 1.00 27.48 ?  348 LYS A CB  1 
ATOM   953  C CG  . LYS A 1 125 ? 4.784   -11.377 -28.111 1.00 26.99 ?  348 LYS A CG  1 
ATOM   954  C CD  . LYS A 1 125 ? 3.955   -12.136 -29.138 1.00 30.23 ?  348 LYS A CD  1 
ATOM   955  C CE  . LYS A 1 125 ? 2.602   -12.536 -28.572 1.00 33.24 ?  348 LYS A CE  1 
ATOM   956  N NZ  . LYS A 1 125 ? 1.905   -13.522 -29.445 1.00 36.92 ?  348 LYS A NZ  1 
ATOM   957  N N   . ALA A 1 126 ? 6.069   -9.669  -25.581 1.00 22.34 ?  349 ALA A N   1 
ATOM   958  C CA  . ALA A 1 126 ? 5.664   -9.625  -24.186 1.00 22.07 ?  349 ALA A CA  1 
ATOM   959  C C   . ALA A 1 126 ? 4.288   -8.991  -24.072 1.00 20.49 ?  349 ALA A C   1 
ATOM   960  O O   . ALA A 1 126 ? 3.953   -8.070  -24.823 1.00 20.63 ?  349 ALA A O   1 
ATOM   961  C CB  . ALA A 1 126 ? 6.673   -8.846  -23.334 1.00 22.45 ?  349 ALA A CB  1 
ATOM   962  N N   . THR A 1 127 ? 3.495   -9.495  -23.130 1.00 22.28 ?  350 THR A N   1 
ATOM   963  C CA  . THR A 1 127 ? 2.179   -8.954  -22.827 1.00 21.66 ?  350 THR A CA  1 
ATOM   964  C C   . THR A 1 127 ? 2.095   -8.663  -21.337 1.00 21.99 ?  350 THR A C   1 
ATOM   965  O O   . THR A 1 127 ? 2.511   -9.482  -20.512 1.00 22.61 ?  350 THR A O   1 
ATOM   966  C CB  . THR A 1 127 ? 1.057   -9.924  -23.228 1.00 21.14 ?  350 THR A CB  1 
ATOM   967  O OG1 . THR A 1 127 ? 1.307   -10.433 -24.544 1.00 22.49 ?  350 THR A OG1 1 
ATOM   968  C CG2 . THR A 1 127 ? -0.294  -9.221  -23.208 1.00 20.99 ?  350 THR A CG2 1 
ATOM   969  N N   . VAL A 1 128 ? 1.566   -7.491  -20.998 1.00 21.66 ?  351 VAL A N   1 
ATOM   970  C CA  . VAL A 1 128 ? 1.287   -7.117  -19.618 1.00 23.28 ?  351 VAL A CA  1 
ATOM   971  C C   . VAL A 1 128 ? -0.218  -6.936  -19.482 1.00 24.03 ?  351 VAL A C   1 
ATOM   972  O O   . VAL A 1 128 ? -0.851  -6.298  -20.332 1.00 25.02 ?  351 VAL A O   1 
ATOM   973  C CB  . VAL A 1 128 ? 2.048   -5.842  -19.202 1.00 23.40 ?  351 VAL A CB  1 
ATOM   974  C CG1 . VAL A 1 128 ? 1.793   -4.703  -20.185 1.00 24.30 ?  351 VAL A CG1 1 
ATOM   975  C CG2 . VAL A 1 128 ? 1.676   -5.431  -17.781 1.00 23.31 ?  351 VAL A CG2 1 
ATOM   976  N N   . TYR A 1 129 ? -0.791  -7.524  -18.438 1.00 24.92 ?  352 TYR A N   1 
ATOM   977  C CA  . TYR A 1 129 ? -2.222  -7.425  -18.168 1.00 28.23 ?  352 TYR A CA  1 
ATOM   978  C C   . TYR A 1 129 ? -2.405  -6.506  -16.965 1.00 25.34 ?  352 TYR A C   1 
ATOM   979  O O   . TYR A 1 129 ? -2.245  -6.930  -15.817 1.00 25.42 ?  352 TYR A O   1 
ATOM   980  C CB  . TYR A 1 129 ? -2.834  -8.802  -17.927 1.00 26.15 ?  352 TYR A CB  1 
ATOM   981  C CG  . TYR A 1 129 ? -4.272  -8.742  -17.473 1.00 31.15 ?  352 TYR A CG  1 
ATOM   982  C CD1 . TYR A 1 129 ? -5.169  -7.862  -18.063 1.00 27.23 ?  352 TYR A CD1 1 
ATOM   983  C CD2 . TYR A 1 129 ? -4.734  -9.565  -16.456 1.00 32.22 ?  352 TYR A CD2 1 
ATOM   984  C CE1 . TYR A 1 129 ? -6.482  -7.799  -17.651 1.00 30.24 ?  352 TYR A CE1 1 
ATOM   985  C CE2 . TYR A 1 129 ? -6.047  -9.510  -16.036 1.00 31.82 ?  352 TYR A CE2 1 
ATOM   986  C CZ  . TYR A 1 129 ? -6.917  -8.626  -16.638 1.00 32.10 ?  352 TYR A CZ  1 
ATOM   987  O OH  . TYR A 1 129 ? -8.227  -8.568  -16.225 1.00 36.25 ?  352 TYR A OH  1 
ATOM   988  N N   . THR A 1 130 ? -2.754  -5.246  -17.237 1.00 23.88 ?  353 THR A N   1 
ATOM   989  C CA  . THR A 1 130 ? -2.892  -4.226  -16.203 1.00 24.74 ?  353 THR A CA  1 
ATOM   990  C C   . THR A 1 130 ? -4.080  -4.459  -15.278 1.00 26.17 ?  353 THR A C   1 
ATOM   991  O O   . THR A 1 130 ? -4.277  -3.663  -14.352 1.00 25.25 ?  353 THR A O   1 
ATOM   992  C CB  . THR A 1 130 ? -3.008  -2.844  -16.844 1.00 23.76 ?  353 THR A CB  1 
ATOM   993  O OG1 . THR A 1 130 ? -4.359  -2.634  -17.268 1.00 20.43 ?  353 THR A OG1 1 
ATOM   994  C CG2 . THR A 1 130 ? -2.081  -2.733  -18.043 1.00 23.66 ?  353 THR A CG2 1 
ATOM   995  N N   . GLY A 1 131 ? -4.874  -5.501  -15.505 1.00 24.89 ?  354 GLY A N   1 
ATOM   996  C CA  . GLY A 1 131 ? -5.906  -5.915  -14.581 1.00 26.83 ?  354 GLY A CA  1 
ATOM   997  C C   . GLY A 1 131 ? -5.532  -7.051  -13.652 1.00 27.53 ?  354 GLY A C   1 
ATOM   998  O O   . GLY A 1 131 ? -6.322  -7.380  -12.760 1.00 29.71 ?  354 GLY A O   1 
ATOM   999  N N   . SER A 1 132 ? -4.356  -7.655  -13.822 1.00 26.84 ?  355 SER A N   1 
ATOM   1000 C CA  . SER A 1 132 ? -3.953  -8.800  -13.016 1.00 31.16 ?  355 SER A CA  1 
ATOM   1001 C C   . SER A 1 132 ? -3.575  -8.377  -11.600 1.00 32.25 ?  355 SER A C   1 
ATOM   1002 O O   . SER A 1 132 ? -3.153  -7.243  -11.357 1.00 30.57 ?  355 SER A O   1 
ATOM   1003 C CB  . SER A 1 132 ? -2.777  -9.527  -13.668 1.00 30.34 ?  355 SER A CB  1 
ATOM   1004 O OG  . SER A 1 132 ? -1.546  -9.149  -13.077 1.00 37.56 ?  355 SER A OG  1 
ATOM   1005 N N   . ALA A 1 133 ? -3.719  -9.320  -10.663 1.00 33.76 ?  356 ALA A N   1 
ATOM   1006 C CA  . ALA A 1 133 ? -3.417  -9.036  -9.264  1.00 36.86 ?  356 ALA A CA  1 
ATOM   1007 C C   . ALA A 1 133 ? -1.963  -8.626  -9.070  1.00 33.28 ?  356 ALA A C   1 
ATOM   1008 O O   . ALA A 1 133 ? -1.657  -7.831  -8.174  1.00 34.85 ?  356 ALA A O   1 
ATOM   1009 C CB  . ALA A 1 133 ? -3.744  -10.254 -8.399  1.00 39.32 ?  356 ALA A CB  1 
ATOM   1010 N N   . ASP A 1 134 ? -1.057  -9.146  -9.897  1.00 34.21 ?  357 ASP A N   1 
ATOM   1011 C CA  . ASP A 1 134 ? 0.358   -8.816  -9.807  1.00 34.19 ?  357 ASP A CA  1 
ATOM   1012 C C   . ASP A 1 134 ? 0.733   -7.591  -10.633 1.00 29.89 ?  357 ASP A C   1 
ATOM   1013 O O   . ASP A 1 134 ? 1.906   -7.433  -10.991 1.00 30.37 ?  357 ASP A O   1 
ATOM   1014 C CB  . ASP A 1 134 ? 1.209   -10.017 -10.225 1.00 39.35 ?  357 ASP A CB  1 
ATOM   1015 C CG  . ASP A 1 134 ? 0.623   -11.335 -9.761  1.00 45.33 ?  357 ASP A CG  1 
ATOM   1016 O OD1 . ASP A 1 134 ? 0.704   -11.626 -8.548  1.00 46.69 ?  357 ASP A OD1 1 
ATOM   1017 O OD2 . ASP A 1 134 ? 0.088   -12.082 -10.607 1.00 45.80 -1 357 ASP A OD2 1 
ATOM   1018 N N   . PHE A 1 135 ? -0.228  -6.730  -10.950 1.00 27.87 ?  358 PHE A N   1 
ATOM   1019 C CA  . PHE A 1 135 ? 0.050   -5.443  -11.583 1.00 27.38 ?  358 PHE A CA  1 
ATOM   1020 C C   . PHE A 1 135 ? 0.068   -4.402  -10.471 1.00 22.75 ?  358 PHE A C   1 
ATOM   1021 O O   . PHE A 1 135 ? -0.984  -3.953  -10.009 1.00 24.13 ?  358 PHE A O   1 
ATOM   1022 C CB  . PHE A 1 135 ? -0.985  -5.112  -12.653 1.00 25.14 ?  358 PHE A CB  1 
ATOM   1023 C CG  . PHE A 1 135 ? -0.718  -3.821  -13.378 1.00 21.72 ?  358 PHE A CG  1 
ATOM   1024 C CD1 . PHE A 1 135 ? 0.235   -3.757  -14.382 1.00 23.67 ?  358 PHE A CD1 1 
ATOM   1025 C CD2 . PHE A 1 135 ? -1.420  -2.671  -13.055 1.00 22.96 ?  358 PHE A CD2 1 
ATOM   1026 C CE1 . PHE A 1 135 ? 0.483   -2.570  -15.051 1.00 19.73 ?  358 PHE A CE1 1 
ATOM   1027 C CE2 . PHE A 1 135 ? -1.177  -1.481  -13.721 1.00 23.13 ?  358 PHE A CE2 1 
ATOM   1028 C CZ  . PHE A 1 135 ? -0.223  -1.431  -14.719 1.00 19.88 ?  358 PHE A CZ  1 
ATOM   1029 N N   . ALA A 1 136 ? 1.267   -4.026  -10.027 1.00 23.15 ?  359 ALA A N   1 
ATOM   1030 C CA  . ALA A 1 136 ? 1.426   -3.109  -8.897  1.00 26.07 ?  359 ALA A CA  1 
ATOM   1031 C C   . ALA A 1 136 ? 2.531   -2.098  -9.182  1.00 24.64 ?  359 ALA A C   1 
ATOM   1032 O O   . ALA A 1 136 ? 3.548   -2.056  -8.484  1.00 25.15 ?  359 ALA A O   1 
ATOM   1033 C CB  . ALA A 1 136 ? 1.717   -3.892  -7.616  1.00 23.93 ?  359 ALA A CB  1 
ATOM   1034 N N   . PRO A 1 137 ? 2.358   -1.251  -10.205 1.00 22.96 ?  360 PRO A N   1 
ATOM   1035 C CA  . PRO A 1 137 ? 3.410   -0.264  -10.502 1.00 22.64 ?  360 PRO A CA  1 
ATOM   1036 C C   . PRO A 1 137 ? 3.650   0.718   -9.370  1.00 22.17 ?  360 PRO A C   1 
ATOM   1037 O O   . PRO A 1 137 ? 4.795   1.145   -9.168  1.00 21.71 ?  360 PRO A O   1 
ATOM   1038 C CB  . PRO A 1 137 ? 2.890   0.443   -11.762 1.00 20.35 ?  360 PRO A CB  1 
ATOM   1039 C CG  . PRO A 1 137 ? 1.423   0.209   -11.757 1.00 20.89 ?  360 PRO A CG  1 
ATOM   1040 C CD  . PRO A 1 137 ? 1.224   -1.141  -11.139 1.00 22.30 ?  360 PRO A CD  1 
ATOM   1041 N N   . LYS A 1 138 ? 2.607   1.086   -8.619  1.00 20.07 ?  361 LYS A N   1 
ATOM   1042 C CA  . LYS A 1 138 ? 2.789   1.981   -7.480  1.00 21.03 ?  361 LYS A CA  1 
ATOM   1043 C C   . LYS A 1 138 ? 3.745   1.386   -6.452  1.00 24.52 ?  361 LYS A C   1 
ATOM   1044 O O   . LYS A 1 138 ? 4.470   2.126   -5.775  1.00 23.31 ?  361 LYS A O   1 
ATOM   1045 C CB  . LYS A 1 138 ? 1.433   2.294   -6.845  1.00 20.53 ?  361 LYS A CB  1 
ATOM   1046 C CG  . LYS A 1 138 ? 1.490   3.077   -5.541  1.00 22.22 ?  361 LYS A CG  1 
ATOM   1047 C CD  . LYS A 1 138 ? 2.063   4.470   -5.732  1.00 21.70 ?  361 LYS A CD  1 
ATOM   1048 C CE  . LYS A 1 138 ? 1.956   5.277   -4.446  1.00 20.92 ?  361 LYS A CE  1 
ATOM   1049 N NZ  . LYS A 1 138 ? 2.749   6.536   -4.495  1.00 23.93 ?  361 LYS A NZ  1 
ATOM   1050 N N   . LEU A 1 139 ? 3.772   0.061   -6.329  1.00 24.16 ?  362 LEU A N   1 
ATOM   1051 C CA  . LEU A 1 139 ? 4.745   -0.624  -5.490  1.00 22.49 ?  362 LEU A CA  1 
ATOM   1052 C C   . LEU A 1 139 ? 6.060   -0.885  -6.212  1.00 23.25 ?  362 LEU A C   1 
ATOM   1053 O O   . LEU A 1 139 ? 6.991   -1.418  -5.600  1.00 23.98 ?  362 LEU A O   1 
ATOM   1054 C CB  . LEU A 1 139 ? 4.166   -1.950  -4.982  1.00 21.59 ?  362 LEU A CB  1 
ATOM   1055 C CG  . LEU A 1 139 ? 2.917   -1.883  -4.101  1.00 21.07 ?  362 LEU A CG  1 
ATOM   1056 C CD1 . LEU A 1 139 ? 2.501   -3.277  -3.655  1.00 22.73 ?  362 LEU A CD1 1 
ATOM   1057 C CD2 . LEU A 1 139 ? 3.151   -0.983  -2.899  1.00 23.60 ?  362 LEU A CD2 1 
ATOM   1058 N N   . GLY A 1 140 ? 6.157   -0.525  -7.492  1.00 24.45 ?  363 GLY A N   1 
ATOM   1059 C CA  . GLY A 1 140 ? 7.358   -0.769  -8.267  1.00 23.29 ?  363 GLY A CA  1 
ATOM   1060 C C   . GLY A 1 140 ? 7.475   -2.160  -8.843  1.00 24.16 ?  363 GLY A C   1 
ATOM   1061 O O   . GLY A 1 140 ? 8.592   -2.614  -9.109  1.00 23.84 ?  363 GLY A O   1 
ATOM   1062 N N   . ARG A 1 141 ? 6.353   -2.846  -9.066  1.00 26.23 ?  364 ARG A N   1 
ATOM   1063 C CA  . ARG A 1 141 ? 6.353   -4.263  -9.420  1.00 27.45 ?  364 ARG A CA  1 
ATOM   1064 C C   . ARG A 1 141 ? 5.311   -4.516  -10.500 1.00 27.64 ?  364 ARG A C   1 
ATOM   1065 O O   . ARG A 1 141 ? 4.131   -4.216  -10.303 1.00 25.83 ?  364 ARG A O   1 
ATOM   1066 C CB  . ARG A 1 141 ? 6.068   -5.122  -8.183  1.00 27.88 ?  364 ARG A CB  1 
ATOM   1067 C CG  . ARG A 1 141 ? 6.699   -6.501  -8.209  1.00 32.60 ?  364 ARG A CG  1 
ATOM   1068 C CD  . ARG A 1 141 ? 6.696   -7.158  -6.830  1.00 33.01 ?  364 ARG A CD  1 
ATOM   1069 N NE  . ARG A 1 141 ? 5.713   -6.587  -5.915  1.00 36.43 ?  364 ARG A NE  1 
ATOM   1070 C CZ  . ARG A 1 141 ? 4.452   -6.987  -5.820  1.00 37.77 ?  364 ARG A CZ  1 
ATOM   1071 N NH1 . ARG A 1 141 ? 3.966   -7.934  -6.607  1.00 31.59 ?  364 ARG A NH1 1 
ATOM   1072 N NH2 . ARG A 1 141 ? 3.659   -6.425  -4.912  1.00 38.25 ?  364 ARG A NH2 1 
ATOM   1073 N N   . VAL A 1 142 ? 5.741   -5.078  -11.631 1.00 25.93 ?  365 VAL A N   1 
ATOM   1074 C CA  . VAL A 1 142 ? 4.855   -5.392  -12.747 1.00 24.26 ?  365 VAL A CA  1 
ATOM   1075 C C   . VAL A 1 142 ? 5.299   -6.720  -13.352 1.00 25.71 ?  365 VAL A C   1 
ATOM   1076 O O   . VAL A 1 142 ? 6.492   -7.035  -13.394 1.00 26.51 ?  365 VAL A O   1 
ATOM   1077 C CB  . VAL A 1 142 ? 4.846   -4.256  -13.804 1.00 21.74 ?  365 VAL A CB  1 
ATOM   1078 C CG1 . VAL A 1 142 ? 4.373   -4.753  -15.168 1.00 25.10 ?  365 VAL A CG1 1 
ATOM   1079 C CG2 . VAL A 1 142 ? 3.973   -3.100  -13.334 1.00 22.32 ?  365 VAL A CG2 1 
ATOM   1080 N N   . GLN A 1 143 ? 4.326   -7.509  -13.807 1.00 23.03 ?  366 GLN A N   1 
ATOM   1081 C CA  . GLN A 1 143 ? 4.571   -8.836  -14.359 1.00 26.97 ?  366 GLN A CA  1 
ATOM   1082 C C   . GLN A 1 143 ? 4.301   -8.843  -15.859 1.00 25.14 ?  366 GLN A C   1 
ATOM   1083 O O   . GLN A 1 143 ? 3.283   -8.313  -16.315 1.00 22.39 ?  366 GLN A O   1 
ATOM   1084 C CB  . GLN A 1 143 ? 3.698   -9.881  -13.661 1.00 27.22 ?  366 GLN A CB  1 
ATOM   1085 C CG  . GLN A 1 143 ? 4.188   -11.308 -13.830 1.00 32.11 ?  366 GLN A CG  1 
ATOM   1086 C CD  . GLN A 1 143 ? 3.428   -12.289 -12.961 1.00 38.32 ?  366 GLN A CD  1 
ATOM   1087 O OE1 . GLN A 1 143 ? 2.809   -13.229 -13.461 1.00 37.04 ?  366 GLN A OE1 1 
ATOM   1088 N NE2 . GLN A 1 143 ? 3.474   -12.077 -11.651 1.00 33.57 ?  366 GLN A NE2 1 
ATOM   1089 N N   . PHE A 1 144 ? 5.210   -9.457  -16.617 1.00 22.91 ?  367 PHE A N   1 
ATOM   1090 C CA  . PHE A 1 144 ? 5.105   -9.567  -18.066 1.00 22.84 ?  367 PHE A CA  1 
ATOM   1091 C C   . PHE A 1 144 ? 5.017   -11.031 -18.474 1.00 26.14 ?  367 PHE A C   1 
ATOM   1092 O O   . PHE A 1 144 ? 5.697   -11.886 -17.900 1.00 26.02 ?  367 PHE A O   1 
ATOM   1093 C CB  . PHE A 1 144 ? 6.310   -8.926  -18.765 1.00 21.66 ?  367 PHE A CB  1 
ATOM   1094 C CG  . PHE A 1 144 ? 6.338   -7.428  -18.687 1.00 25.57 ?  367 PHE A CG  1 
ATOM   1095 C CD1 . PHE A 1 144 ? 5.633   -6.662  -19.601 1.00 21.65 ?  367 PHE A CD1 1 
ATOM   1096 C CD2 . PHE A 1 144 ? 7.083   -6.785  -17.712 1.00 23.49 ?  367 PHE A CD2 1 
ATOM   1097 C CE1 . PHE A 1 144 ? 5.662   -5.282  -19.537 1.00 23.89 ?  367 PHE A CE1 1 
ATOM   1098 C CE2 . PHE A 1 144 ? 7.115   -5.405  -17.643 1.00 22.84 ?  367 PHE A CE2 1 
ATOM   1099 C CZ  . PHE A 1 144 ? 6.404   -4.653  -18.557 1.00 22.12 ?  367 PHE A CZ  1 
ATOM   1100 N N   . GLU A 1 145 ? 4.187   -11.312 -19.475 1.00 22.67 ?  368 GLU A N   1 
ATOM   1101 C CA  . GLU A 1 145 ? 4.072   -12.642 -20.062 1.00 25.76 ?  368 GLU A CA  1 
ATOM   1102 C C   . GLU A 1 145 ? 4.809   -12.651 -21.395 1.00 25.77 ?  368 GLU A C   1 
ATOM   1103 O O   . GLU A 1 145 ? 4.430   -11.926 -22.321 1.00 26.52 ?  368 GLU A O   1 
ATOM   1104 C CB  . GLU A 1 145 ? 2.604   -13.028 -20.253 1.00 25.63 ?  368 GLU A CB  1 
ATOM   1105 C CG  . GLU A 1 145 ? 2.377   -14.482 -20.644 1.00 28.86 ?  368 GLU A CG  1 
ATOM   1106 C CD  . GLU A 1 145 ? 1.014   -14.710 -21.278 1.00 40.91 ?  368 GLU A CD  1 
ATOM   1107 O OE1 . GLU A 1 145 ? 0.060   -13.985 -20.923 1.00 43.06 ?  368 GLU A OE1 1 
ATOM   1108 O OE2 . GLU A 1 145 ? 0.896   -15.613 -22.133 1.00 37.80 -1 368 GLU A OE2 1 
ATOM   1109 N N   . THR A 1 146 ? 5.858   -13.463 -21.492 1.00 26.34 ?  369 THR A N   1 
ATOM   1110 C CA  . THR A 1 146 ? 6.706   -13.512 -22.677 1.00 27.84 ?  369 THR A CA  1 
ATOM   1111 C C   . THR A 1 146 ? 6.666   -14.910 -23.297 1.00 28.15 ?  369 THR A C   1 
ATOM   1112 O O   . THR A 1 146 ? 5.902   -15.784 -22.874 1.00 29.60 ?  369 THR A O   1 
ATOM   1113 C CB  . THR A 1 146 ? 8.143   -13.105 -22.337 1.00 28.72 ?  369 THR A CB  1 
ATOM   1114 O OG1 . THR A 1 146 ? 8.882   -14.259 -21.917 1.00 33.13 ?  369 THR A OG1 1 
ATOM   1115 C CG2 . THR A 1 146 ? 8.161   -12.066 -21.225 1.00 25.23 ?  369 THR A CG2 1 
ATOM   1116 N N   . ASP A 1 147 ? 7.509   -15.113 -24.311 1.00 28.15 ?  370 ASP A N   1 
ATOM   1117 C CA  . ASP A 1 147 ? 7.598   -16.374 -25.037 1.00 32.42 ?  370 ASP A CA  1 
ATOM   1118 C C   . ASP A 1 147 ? 8.906   -17.107 -24.752 1.00 33.38 ?  370 ASP A C   1 
ATOM   1119 O O   . ASP A 1 147 ? 9.380   -17.888 -25.581 1.00 34.67 ?  370 ASP A O   1 
ATOM   1120 C CB  . ASP A 1 147 ? 7.445   -16.140 -26.540 1.00 31.01 ?  370 ASP A CB  1 
ATOM   1121 C CG  . ASP A 1 147 ? 8.476   -15.167 -27.092 1.00 35.14 ?  370 ASP A CG  1 
ATOM   1122 O OD1 . ASP A 1 147 ? 9.207   -14.545 -26.293 1.00 34.54 ?  370 ASP A OD1 1 
ATOM   1123 O OD2 . ASP A 1 147 ? 8.559   -15.030 -28.331 1.00 40.18 -1 370 ASP A OD2 1 
ATOM   1124 N N   . THR A 1 148 ? 9.507   -16.861 -23.591 1.00 32.32 ?  371 THR A N   1 
ATOM   1125 C CA  . THR A 1 148 ? 10.765  -17.505 -23.251 1.00 34.49 ?  371 THR A CA  1 
ATOM   1126 C C   . THR A 1 148 ? 10.866  -17.661 -21.742 1.00 36.03 ?  371 THR A C   1 
ATOM   1127 O O   . THR A 1 148 ? 10.226  -16.938 -20.973 1.00 34.00 ?  371 THR A O   1 
ATOM   1128 C CB  . THR A 1 148 ? 11.971  -16.722 -23.785 1.00 35.09 ?  371 THR A CB  1 
ATOM   1129 O OG1 . THR A 1 148 ? 13.176  -17.441 -23.492 1.00 35.45 ?  371 THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 148 ? 12.040  -15.343 -23.147 1.00 32.56 ?  371 THR A CG2 1 
ATOM   1131 N N   . ASP A 1 149 ? 11.691  -18.623 -21.332 1.00 36.40 ?  372 ASP A N   1 
ATOM   1132 C CA  . ASP A 1 149 ? 11.895  -18.945 -19.927 1.00 38.87 ?  372 ASP A CA  1 
ATOM   1133 C C   . ASP A 1 149 ? 13.360  -18.866 -19.521 1.00 35.32 ?  372 ASP A C   1 
ATOM   1134 O O   . ASP A 1 149 ? 13.717  -19.353 -18.442 1.00 39.37 ?  372 ASP A O   1 
ATOM   1135 C CB  . ASP A 1 149 ? 11.353  -20.346 -19.624 1.00 36.48 ?  372 ASP A CB  1 
ATOM   1136 C CG  . ASP A 1 149 ? 11.854  -21.389 -20.611 1.00 42.11 ?  372 ASP A CG  1 
ATOM   1137 O OD1 . ASP A 1 149 ? 11.351  -21.421 -21.754 1.00 47.30 ?  372 ASP A OD1 1 
ATOM   1138 O OD2 . ASP A 1 149 ? 12.758  -22.171 -20.247 1.00 46.57 -1 372 ASP A OD2 1 
ATOM   1139 N N   . ARG A 1 150 ? 14.218  -18.264 -20.345 1.00 34.42 ?  373 ARG A N   1 
ATOM   1140 C CA  . ARG A 1 150 ? 15.652  -18.390 -20.118 1.00 33.69 ?  373 ARG A CA  1 
ATOM   1141 C C   . ARG A 1 150 ? 16.473  -17.221 -20.656 1.00 34.84 ?  373 ARG A C   1 
ATOM   1142 O O   . ARG A 1 150 ? 17.541  -16.918 -20.116 1.00 34.44 ?  373 ARG A O   1 
ATOM   1143 C CB  . ARG A 1 150 ? 16.151  -19.696 -20.744 1.00 35.95 ?  373 ARG A CB  1 
ATOM   1144 C CG  . ARG A 1 150 ? 16.226  -19.662 -22.266 1.00 38.04 ?  373 ARG A CG  1 
ATOM   1145 C CD  . ARG A 1 150 ? 16.499  -21.036 -22.851 1.00 40.60 ?  373 ARG A CD  1 
ATOM   1146 N NE  . ARG A 1 150 ? 15.525  -22.023 -22.401 1.00 46.54 ?  373 ARG A NE  1 
ATOM   1147 C CZ  . ARG A 1 150 ? 15.828  -23.263 -22.046 1.00 47.13 ?  373 ARG A CZ  1 
ATOM   1148 N NH1 . ARG A 1 150 ? 17.074  -23.707 -22.079 1.00 42.77 ?  373 ARG A NH1 1 
ATOM   1149 N NH2 . ARG A 1 150 ? 14.856  -24.079 -21.646 1.00 43.59 ?  373 ARG A NH2 1 
ATOM   1150 N N   . ASP A 1 151 ? 15.996  -16.556 -21.711 1.00 32.82 ?  374 ASP A N   1 
ATOM   1151 C CA  . ASP A 1 151 ? 16.879  -15.672 -22.465 1.00 31.85 ?  374 ASP A CA  1 
ATOM   1152 C C   . ASP A 1 151 ? 17.186  -14.366 -21.744 1.00 31.34 ?  374 ASP A C   1 
ATOM   1153 O O   . ASP A 1 151 ? 18.189  -13.722 -22.068 1.00 32.10 ?  374 ASP A O   1 
ATOM   1154 C CB  . ASP A 1 151 ? 16.285  -15.368 -23.841 1.00 32.69 ?  374 ASP A CB  1 
ATOM   1155 C CG  . ASP A 1 151 ? 17.345  -14.968 -24.852 1.00 33.16 ?  374 ASP A CG  1 
ATOM   1156 O OD1 . ASP A 1 151 ? 18.502  -15.416 -24.709 1.00 33.49 ?  374 ASP A OD1 1 
ATOM   1157 O OD2 . ASP A 1 151 ? 17.024  -14.204 -25.785 1.00 35.88 -1 374 ASP A OD2 1 
ATOM   1158 N N   . PHE A 1 152 ? 16.363  -13.958 -20.785 1.00 26.36 ?  375 PHE A N   1 
ATOM   1159 C CA  . PHE A 1 152 ? 16.575  -12.691 -20.102 1.00 27.09 ?  375 PHE A CA  1 
ATOM   1160 C C   . PHE A 1 152 ? 17.478  -12.875 -18.891 1.00 30.41 ?  375 PHE A C   1 
ATOM   1161 O O   . PHE A 1 152 ? 17.363  -13.859 -18.154 1.00 27.53 ?  375 PHE A O   1 
ATOM   1162 C CB  . PHE A 1 152 ? 15.241  -12.075 -19.682 1.00 25.86 ?  375 PHE A CB  1 
ATOM   1163 C CG  . PHE A 1 152 ? 14.491  -11.437 -20.814 1.00 24.40 ?  375 PHE A CG  1 
ATOM   1164 C CD1 . PHE A 1 152 ? 14.992  -10.311 -21.446 1.00 24.63 ?  375 PHE A CD1 1 
ATOM   1165 C CD2 . PHE A 1 152 ? 13.289  -11.966 -21.251 1.00 29.41 ?  375 PHE A CD2 1 
ATOM   1166 C CE1 . PHE A 1 152 ? 14.306  -9.722  -22.492 1.00 25.89 ?  375 PHE A CE1 1 
ATOM   1167 C CE2 . PHE A 1 152 ? 12.598  -11.382 -22.296 1.00 29.70 ?  375 PHE A CE2 1 
ATOM   1168 C CZ  . PHE A 1 152 ? 13.107  -10.259 -22.917 1.00 26.19 ?  375 PHE A CZ  1 
ATOM   1169 N N   . GLU A 1 153 ? 18.383  -11.923 -18.697 1.00 28.00 ?  376 GLU A N   1 
ATOM   1170 C CA  . GLU A 1 153 ? 19.330  -11.946 -17.595 1.00 29.91 ?  376 GLU A CA  1 
ATOM   1171 C C   . GLU A 1 153 ? 18.897  -10.974 -16.506 1.00 29.37 ?  376 GLU A C   1 
ATOM   1172 O O   . GLU A 1 153 ? 18.240  -9.964  -16.772 1.00 27.57 ?  376 GLU A O   1 
ATOM   1173 C CB  . GLU A 1 153 ? 20.738  -11.584 -18.071 1.00 30.80 ?  376 GLU A CB  1 
ATOM   1174 C CG  . GLU A 1 153 ? 21.097  -12.115 -19.447 1.00 32.76 ?  376 GLU A CG  1 
ATOM   1175 C CD  . GLU A 1 153 ? 22.508  -11.745 -19.862 1.00 37.26 ?  376 GLU A CD  1 
ATOM   1176 O OE1 . GLU A 1 153 ? 23.178  -11.006 -19.109 1.00 38.10 ?  376 GLU A OE1 1 
ATOM   1177 O OE2 . GLU A 1 153 ? 22.948  -12.192 -20.943 1.00 37.40 -1 376 GLU A OE2 1 
ATOM   1178 N N   . ALA A 1 154 ? 19.281  -11.287 -15.274 1.00 27.81 ?  377 ALA A N   1 
ATOM   1179 C CA  . ALA A 1 154 ? 19.000  -10.401 -14.159 1.00 28.66 ?  377 ALA A CA  1 
ATOM   1180 C C   . ALA A 1 154 ? 19.992  -9.241  -14.136 1.00 29.41 ?  377 ALA A C   1 
ATOM   1181 O O   . ALA A 1 154 ? 21.104  -9.327  -14.665 1.00 30.11 ?  377 ALA A O   1 
ATOM   1182 C CB  . ALA A 1 154 ? 19.054  -11.164 -12.836 1.00 27.13 ?  377 ALA A CB  1 
ATOM   1183 N N   . ASN A 1 155 ? 19.560  -8.139  -13.520 1.00 31.22 ?  378 ASN A N   1 
ATOM   1184 C CA  . ASN A 1 155 ? 20.413  -6.975  -13.272 1.00 29.21 ?  378 ASN A CA  1 
ATOM   1185 C C   . ASN A 1 155 ? 20.942  -6.370  -14.572 1.00 27.98 ?  378 ASN A C   1 
ATOM   1186 O O   . ASN A 1 155 ? 22.084  -5.912  -14.645 1.00 26.70 ?  378 ASN A O   1 
ATOM   1187 C CB  . ASN A 1 155 ? 21.566  -7.330  -12.330 1.00 31.47 ?  378 ASN A CB  1 
ATOM   1188 C CG  . ASN A 1 155 ? 21.084  -7.780  -10.965 1.00 33.42 ?  378 ASN A CG  1 
ATOM   1189 O OD1 . ASN A 1 155 ? 21.428  -8.867  -10.500 1.00 36.38 ?  378 ASN A OD1 1 
ATOM   1190 N ND2 . ASN A 1 155 ? 20.283  -6.944  -10.314 1.00 32.08 ?  378 ASN A ND2 1 
ATOM   1191 N N   . GLN A 1 156 ? 20.106  -6.365  -15.608 1.00 29.13 ?  379 GLN A N   1 
ATOM   1192 C CA  . GLN A 1 156 ? 20.439  -5.737  -16.877 1.00 28.30 ?  379 GLN A CA  1 
ATOM   1193 C C   . GLN A 1 156 ? 19.287  -4.844  -17.313 1.00 26.12 ?  379 GLN A C   1 
ATOM   1194 O O   . GLN A 1 156 ? 18.119  -5.133  -17.037 1.00 23.67 ?  379 GLN A O   1 
ATOM   1195 C CB  . GLN A 1 156 ? 20.743  -6.776  -17.967 1.00 29.70 ?  379 GLN A CB  1 
ATOM   1196 C CG  . GLN A 1 156 ? 21.867  -7.744  -17.617 1.00 27.54 ?  379 GLN A CG  1 
ATOM   1197 C CD  . GLN A 1 156 ? 23.202  -7.050  -17.418 1.00 26.22 ?  379 GLN A CD  1 
ATOM   1198 O OE1 . GLN A 1 156 ? 23.506  -6.058  -18.079 1.00 26.96 ?  379 GLN A OE1 1 
ATOM   1199 N NE2 . GLN A 1 156 ? 24.010  -7.575  -16.504 1.00 27.52 ?  379 GLN A NE2 1 
ATOM   1200 N N   . ASN A 1 157 ? 19.629  -3.752  -17.996 1.00 25.34 ?  380 ASN A N   1 
ATOM   1201 C CA  . ASN A 1 157 ? 18.627  -2.780  -18.417 1.00 23.59 ?  380 ASN A CA  1 
ATOM   1202 C C   . ASN A 1 157 ? 17.607  -3.424  -19.348 1.00 23.57 ?  380 ASN A C   1 
ATOM   1203 O O   . ASN A 1 157 ? 17.968  -4.097  -20.318 1.00 21.43 ?  380 ASN A O   1 
ATOM   1204 C CB  . ASN A 1 157 ? 19.301  -1.594  -19.105 1.00 25.67 ?  380 ASN A CB  1 
ATOM   1205 C CG  . ASN A 1 157 ? 20.231  -0.834  -18.179 1.00 28.58 ?  380 ASN A CG  1 
ATOM   1206 O OD1 . ASN A 1 157 ? 20.058  -0.847  -16.959 1.00 27.75 ?  380 ASN A OD1 1 
ATOM   1207 N ND2 . ASN A 1 157 ? 21.225  -0.167  -18.755 1.00 26.47 ?  380 ASN A ND2 1 
ATOM   1208 N N   . THR A 1 158 ? 16.327  -3.211  -19.049 1.00 22.95 ?  381 THR A N   1 
ATOM   1209 C CA  . THR A 1 158 ? 15.236  -3.824  -19.791 1.00 25.45 ?  381 THR A CA  1 
ATOM   1210 C C   . THR A 1 158 ? 14.157  -2.783  -20.050 1.00 22.44 ?  381 THR A C   1 
ATOM   1211 O O   . THR A 1 158 ? 13.814  -2.002  -19.158 1.00 22.06 ?  381 THR A O   1 
ATOM   1212 C CB  . THR A 1 158 ? 14.648  -5.017  -19.023 1.00 25.80 ?  381 THR A CB  1 
ATOM   1213 O OG1 . THR A 1 158 ? 15.714  -5.841  -18.532 1.00 24.27 ?  381 THR A OG1 1 
ATOM   1214 C CG2 . THR A 1 158 ? 13.751  -5.849  -19.926 1.00 23.79 ?  381 THR A CG2 1 
ATOM   1215 N N   . LYS A 1 159 ? 13.623  -2.776  -21.271 1.00 20.21 ?  382 LYS A N   1 
ATOM   1216 C CA  . LYS A 1 159 ? 12.606  -1.812  -21.673 1.00 20.89 ?  382 LYS A CA  1 
ATOM   1217 C C   . LYS A 1 159 ? 11.446  -2.526  -22.348 1.00 22.48 ?  382 LYS A C   1 
ATOM   1218 O O   . LYS A 1 159 ? 11.656  -3.392  -23.203 1.00 18.00 ?  382 LYS A O   1 
ATOM   1219 C CB  . LYS A 1 159 ? 13.179  -0.755  -22.625 1.00 18.86 ?  382 LYS A CB  1 
ATOM   1220 C CG  . LYS A 1 159 ? 12.103  0.048   -23.343 1.00 19.84 ?  382 LYS A CG  1 
ATOM   1221 C CD  . LYS A 1 159 ? 12.679  1.111   -24.258 1.00 21.72 ?  382 LYS A CD  1 
ATOM   1222 C CE  . LYS A 1 159 ? 11.561  1.930   -24.888 1.00 22.85 ?  382 LYS A CE  1 
ATOM   1223 N NZ  . LYS A 1 159 ? 12.046  2.812   -25.983 1.00 23.16 ?  382 LYS A NZ  1 
ATOM   1224 N N   . PHE A 1 160 ? 10.226  -2.154  -21.969 1.00 23.11 ?  383 PHE A N   1 
ATOM   1225 C CA  . PHE A 1 160 ? 9.018   -2.592  -22.656 1.00 20.25 ?  383 PHE A CA  1 
ATOM   1226 C C   . PHE A 1 160 ? 8.545   -1.478  -23.580 1.00 19.88 ?  383 PHE A C   1 
ATOM   1227 O O   . PHE A 1 160 ? 8.303   -0.353  -23.129 1.00 19.73 ?  383 PHE A O   1 
ATOM   1228 C CB  . PHE A 1 160 ? 7.915   -2.960  -21.665 1.00 19.84 ?  383 PHE A CB  1 
ATOM   1229 C CG  . PHE A 1 160 ? 6.655   -3.448  -22.321 1.00 21.75 ?  383 PHE A CG  1 
ATOM   1230 C CD1 . PHE A 1 160 ? 6.642   -4.639  -23.026 1.00 22.16 ?  383 PHE A CD1 1 
ATOM   1231 C CD2 . PHE A 1 160 ? 5.488   -2.704  -22.251 1.00 21.23 ?  383 PHE A CD2 1 
ATOM   1232 C CE1 . PHE A 1 160 ? 5.486   -5.087  -23.637 1.00 23.37 ?  383 PHE A CE1 1 
ATOM   1233 C CE2 . PHE A 1 160 ? 4.329   -3.146  -22.861 1.00 19.20 ?  383 PHE A CE2 1 
ATOM   1234 C CZ  . PHE A 1 160 ? 4.328   -4.339  -23.555 1.00 23.84 ?  383 PHE A CZ  1 
ATOM   1235 N N   . THR A 1 161 ? 8.427   -1.787  -24.871 1.00 19.99 ?  384 THR A N   1 
ATOM   1236 C CA  . THR A 1 161 ? 7.837   -0.863  -25.828 1.00 19.90 ?  384 THR A CA  1 
ATOM   1237 C C   . THR A 1 161 ? 6.434   -1.334  -26.161 1.00 19.65 ?  384 THR A C   1 
ATOM   1238 O O   . THR A 1 161 ? 6.272   -2.477  -26.615 1.00 19.54 ?  384 THR A O   1 
ATOM   1239 C CB  . THR A 1 161 ? 8.676   -0.779  -27.099 1.00 19.51 ?  384 THR A CB  1 
ATOM   1240 O OG1 . THR A 1 161 ? 10.016  -0.394  -26.769 1.00 20.30 ?  384 THR A OG1 1 
ATOM   1241 C CG2 . THR A 1 161 ? 8.081   0.239   -28.064 1.00 19.04 ?  384 THR A CG2 1 
ATOM   1242 N N   . PRO A 1 162 ? 5.402   -0.523  -25.953 1.00 20.55 ?  385 PRO A N   1 
ATOM   1243 C CA  . PRO A 1 162 ? 4.050   -0.953  -26.308 1.00 21.23 ?  385 PRO A CA  1 
ATOM   1244 C C   . PRO A 1 162 ? 3.819   -0.878  -27.807 1.00 20.61 ?  385 PRO A C   1 
ATOM   1245 O O   . PRO A 1 162 ? 4.373   -0.028  -28.509 1.00 24.01 ?  385 PRO A O   1 
ATOM   1246 C CB  . PRO A 1 162 ? 3.161   0.045   -25.558 1.00 18.99 ?  385 PRO A CB  1 
ATOM   1247 C CG  . PRO A 1 162 ? 3.977   1.293   -25.524 1.00 19.04 ?  385 PRO A CG  1 
ATOM   1248 C CD  . PRO A 1 162 ? 5.427   0.859   -25.443 1.00 20.53 ?  385 PRO A CD  1 
ATOM   1249 N N   . VAL A 1 163 ? 2.995   -1.802  -28.297 1.00 19.93 ?  386 VAL A N   1 
ATOM   1250 C CA  . VAL A 1 163 ? 2.604   -1.855  -29.700 1.00 21.74 ?  386 VAL A CA  1 
ATOM   1251 C C   . VAL A 1 163 ? 1.095   -1.721  -29.858 1.00 18.79 ?  386 VAL A C   1 
ATOM   1252 O O   . VAL A 1 163 ? 0.609   -0.849  -30.587 1.00 19.89 ?  386 VAL A O   1 
ATOM   1253 C CB  . VAL A 1 163 ? 3.111   -3.149  -30.377 1.00 19.31 ?  386 VAL A CB  1 
ATOM   1254 C CG1 . VAL A 1 163 ? 2.414   -3.360  -31.714 1.00 18.10 ?  386 VAL A CG1 1 
ATOM   1255 C CG2 . VAL A 1 163 ? 4.619   -3.099  -30.558 1.00 19.11 ?  386 VAL A CG2 1 
ATOM   1256 N N   . GLY A 1 164 ? 0.339   -2.567  -29.173 1.00 17.72 ?  387 GLY A N   1 
ATOM   1257 C CA  . GLY A 1 164 ? -1.101  -2.523  -29.267 1.00 19.59 ?  387 GLY A CA  1 
ATOM   1258 C C   . GLY A 1 164 ? -1.755  -3.308  -28.153 1.00 19.97 ?  387 GLY A C   1 
ATOM   1259 O O   . GLY A 1 164 ? -1.158  -3.543  -27.102 1.00 21.13 ?  387 GLY A O   1 
ATOM   1260 N N   . VAL A 1 165 ? -3.000  -3.718  -28.402 1.00 20.53 ?  388 VAL A N   1 
ATOM   1261 C CA  . VAL A 1 165 ? -3.823  -4.385  -27.403 1.00 23.53 ?  388 VAL A CA  1 
ATOM   1262 C C   . VAL A 1 165 ? -4.429  -5.640  -28.017 1.00 22.81 ?  388 VAL A C   1 
ATOM   1263 O O   . VAL A 1 165 ? -4.536  -5.777  -29.238 1.00 22.08 ?  388 VAL A O   1 
ATOM   1264 C CB  . VAL A 1 165 ? -4.932  -3.459  -26.862 1.00 23.12 ?  388 VAL A CB  1 
ATOM   1265 C CG1 . VAL A 1 165 ? -4.319  -2.267  -26.139 1.00 16.96 ?  388 VAL A CG1 1 
ATOM   1266 C CG2 . VAL A 1 165 ? -5.822  -2.990  -27.999 1.00 18.01 ?  388 VAL A CG2 1 
ATOM   1267 N N   . ILE A 1 166 ? -4.829  -6.569  -27.146 1.00 21.61 ?  389 ILE A N   1 
ATOM   1268 C CA  . ILE A 1 166 ? -5.424  -7.826  -27.573 1.00 23.60 ?  389 ILE A CA  1 
ATOM   1269 C C   . ILE A 1 166 ? -6.701  -8.083  -26.786 1.00 23.85 ?  389 ILE A C   1 
ATOM   1270 O O   . ILE A 1 166 ? -6.905  -7.566  -25.686 1.00 21.83 ?  389 ILE A O   1 
ATOM   1271 C CB  . ILE A 1 166 ? -4.465  -9.027  -27.414 1.00 21.93 ?  389 ILE A CB  1 
ATOM   1272 C CG1 . ILE A 1 166 ? -4.033  -9.179  -25.954 1.00 21.25 ?  389 ILE A CG1 1 
ATOM   1273 C CG2 . ILE A 1 166 ? -3.263  -8.882  -28.326 1.00 19.10 ?  389 ILE A CG2 1 
ATOM   1274 C CD1 . ILE A 1 166 ? -2.963  -10.229 -25.734 1.00 19.41 ?  389 ILE A CD1 1 
ATOM   1275 N N   . GLN A 1 167 ? -7.568  -8.892  -27.386 1.00 26.69 ?  390 GLN A N   1 
ATOM   1276 C CA  . GLN A 1 167 ? -8.721  -9.488  -26.732 1.00 29.45 ?  390 GLN A CA  1 
ATOM   1277 C C   . GLN A 1 167 ? -8.662  -10.985 -26.988 1.00 28.97 ?  390 GLN A C   1 
ATOM   1278 O O   . GLN A 1 167 ? -8.278  -11.414 -28.079 1.00 30.00 ?  390 GLN A O   1 
ATOM   1279 C CB  . GLN A 1 167 ? -10.034 -8.908  -27.264 1.00 25.19 ?  390 GLN A CB  1 
ATOM   1280 C CG  . GLN A 1 167 ? -11.280 -9.496  -26.633 1.00 27.27 ?  390 GLN A CG  1 
ATOM   1281 C CD  . GLN A 1 167 ? -12.090 -10.334 -27.605 1.00 28.23 ?  390 GLN A CD  1 
ATOM   1282 O OE1 . GLN A 1 167 ? -11.586 -10.768 -28.642 1.00 24.10 ?  390 GLN A OE1 1 
ATOM   1283 N NE2 . GLN A 1 167 ? -13.356 -10.559 -27.276 1.00 27.63 ?  390 GLN A NE2 1 
ATOM   1284 N N   . ASP A 1 168 ? -9.023  -11.783 -25.987 1.00 31.53 ?  391 ASP A N   1 
ATOM   1285 C CA  . ASP A 1 168 ? -8.899  -13.225 -26.159 1.00 39.53 ?  391 ASP A CA  1 
ATOM   1286 C C   . ASP A 1 168 ? -10.197 -13.959 -25.854 1.00 41.83 ?  391 ASP A C   1 
ATOM   1287 O O   . ASP A 1 168 ? -11.259 -13.343 -25.711 1.00 42.04 ?  391 ASP A O   1 
ATOM   1288 C CB  . ASP A 1 168 ? -7.781  -13.783 -25.275 1.00 40.24 ?  391 ASP A CB  1 
ATOM   1289 C CG  . ASP A 1 168 ? -7.742  -13.138 -23.906 1.00 39.42 ?  391 ASP A CG  1 
ATOM   1290 O OD1 . ASP A 1 168 ? -8.782  -12.606 -23.461 1.00 48.26 ?  391 ASP A OD1 1 
ATOM   1291 O OD2 . ASP A 1 168 ? -6.670  -13.175 -23.267 1.00 36.67 -1 391 ASP A OD2 1 
ATOM   1292 N N   . GLY A 1 169 ? -10.107 -15.284 -25.774 1.00 47.66 ?  392 GLY A N   1 
ATOM   1293 C CA  . GLY A 1 169 ? -11.200 -16.126 -25.333 1.00 41.56 ?  392 GLY A CA  1 
ATOM   1294 C C   . GLY A 1 169 ? -12.440 -16.113 -26.199 1.00 40.71 ?  392 GLY A C   1 
ATOM   1295 O O   . GLY A 1 169 ? -12.543 -15.355 -27.169 1.00 44.02 ?  392 GLY A O   1 
ATOM   1296 N N   . GLY A 1 170 ? -13.386 -16.979 -25.852 1.00 38.10 ?  393 GLY A N   1 
ATOM   1297 C CA  . GLY A 1 170 ? -14.706 -16.948 -26.438 1.00 32.13 ?  393 GLY A CA  1 
ATOM   1298 C C   . GLY A 1 170 ? -15.645 -16.115 -25.592 1.00 35.37 ?  393 GLY A C   1 
ATOM   1299 O O   . GLY A 1 170 ? -16.548 -16.646 -24.939 1.00 36.13 ?  393 GLY A O   1 
ATOM   1300 N N   . THR A 1 171 ? -15.410 -14.809 -25.565 1.00 32.87 ?  394 THR A N   1 
ATOM   1301 C CA  . THR A 1 171 ? -16.304 -13.845 -24.942 1.00 30.87 ?  394 THR A CA  1 
ATOM   1302 C C   . THR A 1 171 ? -16.791 -12.869 -26.008 1.00 27.53 ?  394 THR A C   1 
ATOM   1303 O O   . THR A 1 171 ? -16.368 -12.920 -27.167 1.00 27.11 ?  394 THR A O   1 
ATOM   1304 C CB  . THR A 1 171 ? -15.615 -13.100 -23.792 1.00 33.38 ?  394 THR A CB  1 
ATOM   1305 O OG1 . THR A 1 171 ? -14.746 -12.090 -24.320 1.00 36.76 ?  394 THR A OG1 1 
ATOM   1306 C CG2 . THR A 1 171 ? -14.806 -14.062 -22.932 1.00 33.19 ?  394 THR A CG2 1 
ATOM   1307 N N   . THR A 1 172 ? -17.691 -11.976 -25.606 1.00 28.05 ?  395 THR A N   1 
ATOM   1308 C CA  . THR A 1 172 ? -18.242 -11.004 -26.539 1.00 29.95 ?  395 THR A CA  1 
ATOM   1309 C C   . THR A 1 172 ? -17.135 -10.133 -27.122 1.00 28.48 ?  395 THR A C   1 
ATOM   1310 O O   . THR A 1 172 ? -16.109 -9.879  -26.486 1.00 26.81 ?  395 THR A O   1 
ATOM   1311 C CB  . THR A 1 172 ? -19.286 -10.126 -25.847 1.00 27.25 ?  395 THR A CB  1 
ATOM   1312 O OG1 . THR A 1 172 ? -18.777 -9.682  -24.584 1.00 30.56 ?  395 THR A OG1 1 
ATOM   1313 C CG2 . THR A 1 172 ? -20.574 -10.906 -25.627 1.00 28.91 ?  395 THR A CG2 1 
ATOM   1314 N N   . HIS A 1 173 ? -17.349 -9.686  -28.355 1.00 24.47 ?  396 HIS A N   1 
ATOM   1315 C CA  . HIS A 1 173 ? -16.359 -8.862  -29.030 1.00 25.14 ?  396 HIS A CA  1 
ATOM   1316 C C   . HIS A 1 173 ? -16.316 -7.463  -28.428 1.00 24.19 ?  396 HIS A C   1 
ATOM   1317 O O   . HIS A 1 173 ? -17.324 -6.936  -27.946 1.00 25.35 ?  396 HIS A O   1 
ATOM   1318 C CB  . HIS A 1 173 ? -16.666 -8.772  -30.522 1.00 21.24 ?  396 HIS A CB  1 
ATOM   1319 C CG  . HIS A 1 173 ? -16.315 -10.009 -31.286 1.00 25.59 ?  396 HIS A CG  1 
ATOM   1320 N ND1 . HIS A 1 173 ? -16.580 -10.150 -32.631 1.00 23.86 ?  396 HIS A ND1 1 
ATOM   1321 C CD2 . HIS A 1 173 ? -15.723 -11.163 -30.896 1.00 25.86 ?  396 HIS A CD2 1 
ATOM   1322 C CE1 . HIS A 1 173 ? -16.164 -11.335 -33.038 1.00 21.21 ?  396 HIS A CE1 1 
ATOM   1323 N NE2 . HIS A 1 173 ? -15.642 -11.971 -32.004 1.00 25.82 ?  396 HIS A NE2 1 
ATOM   1324 N N   . ARG A 1 174 ? -15.123 -6.867  -28.458 1.00 23.39 ?  397 ARG A N   1 
ATOM   1325 C CA  . ARG A 1 174 ? -14.868 -5.510  -27.980 1.00 27.11 ?  397 ARG A CA  1 
ATOM   1326 C C   . ARG A 1 174 ? -15.163 -5.344  -26.490 1.00 24.31 ?  397 ARG A C   1 
ATOM   1327 O O   . ARG A 1 174 ? -15.447 -4.233  -26.033 1.00 23.31 ?  397 ARG A O   1 
ATOM   1328 C CB  . ARG A 1 174 ? -15.661 -4.480  -28.793 1.00 25.05 ?  397 ARG A CB  1 
ATOM   1329 C CG  . ARG A 1 174 ? -14.946 -4.003  -30.043 1.00 24.35 ?  397 ARG A CG  1 
ATOM   1330 C CD  . ARG A 1 174 ? -15.931 -3.405  -31.032 1.00 25.98 ?  397 ARG A CD  1 
ATOM   1331 N NE  . ARG A 1 174 ? -16.614 -4.439  -31.801 1.00 33.82 ?  397 ARG A NE  1 
ATOM   1332 C CZ  . ARG A 1 174 ? -17.932 -4.579  -31.866 1.00 31.68 ?  397 ARG A CZ  1 
ATOM   1333 N NH1 . ARG A 1 174 ? -18.748 -3.757  -31.226 1.00 33.45 ?  397 ARG A NH1 1 
ATOM   1334 N NH2 . ARG A 1 174 ? -18.443 -5.568  -32.593 1.00 30.69 ?  397 ARG A NH2 1 
ATOM   1335 N N   . ASN A 1 175 ? -15.095 -6.429  -25.719 1.00 27.44 ?  398 ASN A N   1 
ATOM   1336 C CA  . ASN A 1 175 ? -15.258 -6.380  -24.270 1.00 24.93 ?  398 ASN A CA  1 
ATOM   1337 C C   . ASN A 1 175 ? -14.014 -5.875  -23.555 1.00 24.70 ?  398 ASN A C   1 
ATOM   1338 O O   . ASN A 1 175 ? -14.038 -5.724  -22.328 1.00 28.98 ?  398 ASN A O   1 
ATOM   1339 C CB  . ASN A 1 175 ? -15.599 -7.772  -23.734 1.00 24.15 ?  398 ASN A CB  1 
ATOM   1340 C CG  . ASN A 1 175 ? -14.501 -8.782  -24.016 1.00 29.80 ?  398 ASN A CG  1 
ATOM   1341 O OD1 . ASN A 1 175 ? -13.814 -8.691  -25.031 1.00 30.79 ?  398 ASN A OD1 1 
ATOM   1342 N ND2 . ASN A 1 175 ? -14.324 -9.743  -23.115 1.00 26.39 ?  398 ASN A ND2 1 
ATOM   1343 N N   . GLU A 1 176 ? -12.944 -5.601  -24.291 1.00 24.79 ?  399 GLU A N   1 
ATOM   1344 C CA  . GLU A 1 176 ? -11.609 -5.469  -23.731 1.00 23.39 ?  399 GLU A CA  1 
ATOM   1345 C C   . GLU A 1 176 ? -10.711 -4.775  -24.747 1.00 22.74 ?  399 GLU A C   1 
ATOM   1346 O O   . GLU A 1 176 ? -10.754 -5.124  -25.932 1.00 24.80 ?  399 GLU A O   1 
ATOM   1347 C CB  . GLU A 1 176 ? -11.071 -6.858  -23.387 1.00 23.71 ?  399 GLU A CB  1 
ATOM   1348 C CG  . GLU A 1 176 ? -10.248 -6.952  -22.127 1.00 34.09 ?  399 GLU A CG  1 
ATOM   1349 C CD  . GLU A 1 176 ? -9.249  -8.089  -22.190 1.00 36.32 ?  399 GLU A CD  1 
ATOM   1350 O OE1 . GLU A 1 176 ? -9.425  -8.992  -23.039 1.00 30.01 ?  399 GLU A OE1 1 
ATOM   1351 O OE2 . GLU A 1 176 ? -8.305  -8.093  -21.376 1.00 32.97 ?  399 GLU A OE2 1 
ATOM   1352 N N   . PRO A 1 177 ? -9.887  -3.794  -24.348 1.00 26.10 ?  400 PRO A N   1 
ATOM   1353 C CA  . PRO A 1 177 ? -9.725  -3.191  -23.017 1.00 24.23 ?  400 PRO A CA  1 
ATOM   1354 C C   . PRO A 1 177 ? -10.922 -2.349  -22.579 1.00 20.17 ?  400 PRO A C   1 
ATOM   1355 O O   . PRO A 1 177 ? -11.832 -2.093  -23.368 1.00 20.57 ?  400 PRO A O   1 
ATOM   1356 C CB  . PRO A 1 177 ? -8.492  -2.286  -23.164 1.00 20.98 ?  400 PRO A CB  1 
ATOM   1357 C CG  . PRO A 1 177 ? -8.010  -2.418  -24.547 1.00 19.85 ?  400 PRO A CG  1 
ATOM   1358 C CD  . PRO A 1 177 ? -8.861  -3.359  -25.311 1.00 20.96 ?  400 PRO A CD  1 
ATOM   1359 N N   . GLN A 1 178 ? -10.906 -1.924  -21.319 1.00 23.84 ?  401 GLN A N   1 
ATOM   1360 C CA  . GLN A 1 178 ? -11.902 -1.013  -20.760 1.00 24.63 ?  401 GLN A CA  1 
ATOM   1361 C C   . GLN A 1 178 ? -11.185 0.306   -20.488 1.00 20.23 ?  401 GLN A C   1 
ATOM   1362 O O   . GLN A 1 178 ? -10.526 0.464   -19.456 1.00 17.84 ?  401 GLN A O   1 
ATOM   1363 C CB  . GLN A 1 178 ? -12.525 -1.598  -19.496 1.00 21.10 ?  401 GLN A CB  1 
ATOM   1364 C CG  . GLN A 1 178 ? -13.486 -2.747  -19.761 1.00 20.59 ?  401 GLN A CG  1 
ATOM   1365 C CD  . GLN A 1 178 ? -13.868 -3.493  -18.497 1.00 28.63 ?  401 GLN A CD  1 
ATOM   1366 O OE1 . GLN A 1 178 ? -13.174 -4.418  -18.075 1.00 32.62 ?  401 GLN A OE1 1 
ATOM   1367 N NE2 . GLN A 1 178 ? -14.981 -3.097  -17.889 1.00 25.82 ?  401 GLN A NE2 1 
ATOM   1368 N N   . GLN A 1 179 ? -11.317 1.253   -21.419 1.00 17.57 ?  402 GLN A N   1 
ATOM   1369 C CA  . GLN A 1 179 ? -10.485 2.451   -21.407 1.00 18.91 ?  402 GLN A CA  1 
ATOM   1370 C C   . GLN A 1 179 ? -10.835 3.425   -20.288 1.00 19.17 ?  402 GLN A C   1 
ATOM   1371 O O   . GLN A 1 179 ? -10.059 4.354   -20.043 1.00 16.36 ?  402 GLN A O   1 
ATOM   1372 C CB  . GLN A 1 179 ? -10.577 3.162   -22.759 1.00 19.58 ?  402 GLN A CB  1 
ATOM   1373 C CG  . GLN A 1 179 ? -11.814 4.026   -22.943 1.00 19.02 ?  402 GLN A CG  1 
ATOM   1374 C CD  . GLN A 1 179 ? -11.633 5.070   -24.029 1.00 20.77 ?  402 GLN A CD  1 
ATOM   1375 O OE1 . GLN A 1 179 ? -10.700 5.872   -23.985 1.00 19.60 ?  402 GLN A OE1 1 
ATOM   1376 N NE2 . GLN A 1 179 ? -12.522 5.059   -25.015 1.00 20.69 ?  402 GLN A NE2 1 
ATOM   1377 N N   . TRP A 1 180 ? -11.965 3.243   -19.603 1.00 17.15 ?  403 TRP A N   1 
ATOM   1378 C CA  . TRP A 1 180 ? -12.359 4.132   -18.516 1.00 18.63 ?  403 TRP A CA  1 
ATOM   1379 C C   . TRP A 1 180 ? -12.350 3.434   -17.161 1.00 21.58 ?  403 TRP A C   1 
ATOM   1380 O O   . TRP A 1 180 ? -12.968 3.923   -16.210 1.00 22.12 ?  403 TRP A O   1 
ATOM   1381 C CB  . TRP A 1 180 ? -13.734 4.739   -18.795 1.00 19.48 ?  403 TRP A CB  1 
ATOM   1382 C CG  . TRP A 1 180 ? -13.766 5.600   -20.023 1.00 20.22 ?  403 TRP A CG  1 
ATOM   1383 C CD1 . TRP A 1 180 ? -14.618 5.484   -21.083 1.00 21.54 ?  403 TRP A CD1 1 
ATOM   1384 C CD2 . TRP A 1 180 ? -12.902 6.706   -20.323 1.00 19.50 ?  403 TRP A CD2 1 
ATOM   1385 N NE1 . TRP A 1 180 ? -14.342 6.448   -22.021 1.00 20.38 ?  403 TRP A NE1 1 
ATOM   1386 C CE2 . TRP A 1 180 ? -13.293 7.211   -21.580 1.00 20.53 ?  403 TRP A CE2 1 
ATOM   1387 C CE3 . TRP A 1 180 ? -11.839 7.319   -19.651 1.00 19.16 ?  403 TRP A CE3 1 
ATOM   1388 C CZ2 . TRP A 1 180 ? -12.658 8.298   -22.177 1.00 19.14 ?  403 TRP A CZ2 1 
ATOM   1389 C CZ3 . TRP A 1 180 ? -11.210 8.396   -20.246 1.00 20.15 ?  403 TRP A CZ3 1 
ATOM   1390 C CH2 . TRP A 1 180 ? -11.622 8.875   -21.496 1.00 21.82 ?  403 TRP A CH2 1 
ATOM   1391 N N   . VAL A 1 181 ? -11.658 2.304   -17.054 1.00 18.76 ?  404 VAL A N   1 
ATOM   1392 C CA  . VAL A 1 181 ? -11.523 1.572   -15.801 1.00 20.76 ?  404 VAL A CA  1 
ATOM   1393 C C   . VAL A 1 181 ? -10.062 1.656   -15.383 1.00 19.97 ?  404 VAL A C   1 
ATOM   1394 O O   . VAL A 1 181 ? -9.190  1.036   -16.005 1.00 18.26 ?  404 VAL A O   1 
ATOM   1395 C CB  . VAL A 1 181 ? -11.982 0.114   -15.934 1.00 21.18 ?  404 VAL A CB  1 
ATOM   1396 C CG1 . VAL A 1 181 ? -11.727 -0.639  -14.638 1.00 15.63 ?  404 VAL A CG1 1 
ATOM   1397 C CG2 . VAL A 1 181 ? -13.454 0.056   -16.309 1.00 20.43 ?  404 VAL A CG2 1 
ATOM   1398 N N   . LEU A 1 182 ? -9.794  2.426   -14.335 1.00 22.62 ?  405 LEU A N   1 
ATOM   1399 C CA  . LEU A 1 182 ? -8.428  2.583   -13.865 1.00 24.34 ?  405 LEU A CA  1 
ATOM   1400 C C   . LEU A 1 182 ? -7.933  1.282   -13.241 1.00 21.23 ?  405 LEU A C   1 
ATOM   1401 O O   . LEU A 1 182 ? -8.682  0.610   -12.524 1.00 23.05 ?  405 LEU A O   1 
ATOM   1402 C CB  . LEU A 1 182 ? -8.338  3.712   -12.841 1.00 24.24 ?  405 LEU A CB  1 
ATOM   1403 C CG  . LEU A 1 182 ? -8.429  5.138   -13.381 1.00 23.65 ?  405 LEU A CG  1 
ATOM   1404 C CD1 . LEU A 1 182 ? -8.690  6.119   -12.249 1.00 23.11 ?  405 LEU A CD1 1 
ATOM   1405 C CD2 . LEU A 1 182 ? -7.159  5.497   -14.130 1.00 21.12 ?  405 LEU A CD2 1 
ATOM   1406 N N   . PRO A 1 183 ? -6.685  0.899   -13.492 1.00 21.76 ?  406 PRO A N   1 
ATOM   1407 C CA  . PRO A 1 183 ? -6.126  -0.264  -12.800 1.00 21.45 ?  406 PRO A CA  1 
ATOM   1408 C C   . PRO A 1 183 ? -5.899  0.047   -11.330 1.00 18.96 ?  406 PRO A C   1 
ATOM   1409 O O   . PRO A 1 183 ? -5.818  1.204   -10.912 1.00 18.63 ?  406 PRO A O   1 
ATOM   1410 C CB  . PRO A 1 183 ? -4.797  -0.527  -13.521 1.00 22.31 ?  406 PRO A CB  1 
ATOM   1411 C CG  . PRO A 1 183 ? -4.617  0.578   -14.519 1.00 20.13 ?  406 PRO A CG  1 
ATOM   1412 C CD  . PRO A 1 183 ? -5.709  1.581   -14.357 1.00 20.31 ?  406 PRO A CD  1 
ATOM   1413 N N   . SER A 1 184 ? -5.818  -1.016  -10.535 1.00 22.52 ?  407 SER A N   1 
ATOM   1414 C CA  . SER A 1 184 ? -5.391  -0.893  -9.146  1.00 25.32 ?  407 SER A CA  1 
ATOM   1415 C C   . SER A 1 184 ? -3.872  -0.778  -9.141  1.00 23.14 ?  407 SER A C   1 
ATOM   1416 O O   . SER A 1 184 ? -3.167  -1.772  -9.341  1.00 25.47 ?  407 SER A O   1 
ATOM   1417 C CB  . SER A 1 184 ? -5.865  -2.086  -8.322  1.00 22.53 ?  407 SER A CB  1 
ATOM   1418 O OG  . SER A 1 184 ? -6.759  -2.902  -9.059  1.00 30.71 ?  407 SER A OG  1 
ATOM   1419 N N   . TYR A 1 185 ? -3.366  0.439   -8.927  1.00 21.73 ?  408 TYR A N   1 
ATOM   1420 C CA  . TYR A 1 185 ? -1.941  0.693   -9.097  1.00 22.43 ?  408 TYR A CA  1 
ATOM   1421 C C   . TYR A 1 185 ? -1.083  -0.025  -8.062  1.00 20.86 ?  408 TYR A C   1 
ATOM   1422 O O   . TYR A 1 185 ? 0.123   -0.181  -8.282  1.00 21.64 ?  408 TYR A O   1 
ATOM   1423 C CB  . TYR A 1 185 ? -1.672  2.200   -9.057  1.00 21.66 ?  408 TYR A CB  1 
ATOM   1424 C CG  . TYR A 1 185 ? -2.189  2.936   -10.277 1.00 21.29 ?  408 TYR A CG  1 
ATOM   1425 C CD1 . TYR A 1 185 ? -1.724  2.624   -11.548 1.00 21.86 ?  408 TYR A CD1 1 
ATOM   1426 C CD2 . TYR A 1 185 ? -3.145  3.938   -10.158 1.00 17.89 ?  408 TYR A CD2 1 
ATOM   1427 C CE1 . TYR A 1 185 ? -2.191  3.290   -12.666 1.00 19.83 ?  408 TYR A CE1 1 
ATOM   1428 C CE2 . TYR A 1 185 ? -3.620  4.610   -11.272 1.00 21.16 ?  408 TYR A CE2 1 
ATOM   1429 C CZ  . TYR A 1 185 ? -3.139  4.281   -12.523 1.00 21.41 ?  408 TYR A CZ  1 
ATOM   1430 O OH  . TYR A 1 185 ? -3.605  4.943   -13.637 1.00 16.68 ?  408 TYR A OH  1 
ATOM   1431 N N   . SER A 1 186 ? -1.668  -0.477  -6.951  1.00 21.91 ?  409 SER A N   1 
ATOM   1432 C CA  . SER A 1 186 ? -0.924  -1.165  -5.902  1.00 26.13 ?  409 SER A CA  1 
ATOM   1433 C C   . SER A 1 186 ? -1.322  -2.631  -5.763  1.00 25.04 ?  409 SER A C   1 
ATOM   1434 O O   . SER A 1 186 ? -1.034  -3.252  -4.735  1.00 23.86 ?  409 SER A O   1 
ATOM   1435 C CB  . SER A 1 186 ? -1.100  -0.446  -4.564  1.00 25.19 ?  409 SER A CB  1 
ATOM   1436 O OG  . SER A 1 186 ? -0.306  0.723   -4.503  1.00 24.53 ?  409 SER A OG  1 
ATOM   1437 N N   . GLY A 1 187 ? -1.972  -3.196  -6.772  1.00 23.16 ?  410 GLY A N   1 
ATOM   1438 C CA  . GLY A 1 187 ? -2.377  -4.583  -6.714  1.00 23.24 ?  410 GLY A CA  1 
ATOM   1439 C C   . GLY A 1 187 ? -3.802  -4.758  -6.234  1.00 27.41 ?  410 GLY A C   1 
ATOM   1440 O O   . GLY A 1 187 ? -4.560  -3.804  -6.032  1.00 31.34 ?  410 GLY A O   1 
ATOM   1441 N N   . ARG A 1 188 ? -4.162  -6.022  -6.031  1.00 36.51 ?  411 ARG A N   1 
ATOM   1442 C CA  . ARG A 1 188 ? -5.541  -6.376  -5.718  1.00 37.97 ?  411 ARG A CA  1 
ATOM   1443 C C   . ARG A 1 188 ? -5.949  -5.843  -4.348  1.00 37.84 ?  411 ARG A C   1 
ATOM   1444 O O   . ARG A 1 188 ? -5.207  -5.979  -3.369  1.00 36.99 ?  411 ARG A O   1 
ATOM   1445 C CB  . ARG A 1 188 ? -5.716  -7.893  -5.772  1.00 38.95 ?  411 ARG A CB  1 
ATOM   1446 C CG  . ARG A 1 188 ? -7.151  -8.363  -5.603  1.00 44.18 ?  411 ARG A CG  1 
ATOM   1447 C CD  . ARG A 1 188 ? -7.984  -8.071  -6.843  1.00 45.66 ?  411 ARG A CD  1 
ATOM   1448 N NE  . ARG A 1 188 ? -7.524  -8.816  -8.010  1.00 45.15 ?  411 ARG A NE  1 
ATOM   1449 C CZ  . ARG A 1 188 ? -7.096  -8.258  -9.135  1.00 43.40 ?  411 ARG A CZ  1 
ATOM   1450 N NH1 . ARG A 1 188 ? -7.048  -6.944  -9.280  1.00 37.97 ?  411 ARG A NH1 1 
ATOM   1451 N NH2 . ARG A 1 188 ? -6.709  -9.039  -10.140 1.00 39.78 ?  411 ARG A NH2 1 
ATOM   1452 N N   . ASN A 1 189 ? -7.130  -5.222  -4.295  1.00 41.05 ?  412 ASN A N   1 
ATOM   1453 C CA  . ASN A 1 189 ? -7.839  -4.756  -3.095  1.00 40.41 ?  412 ASN A CA  1 
ATOM   1454 C C   . ASN A 1 189 ? -7.281  -3.468  -2.499  1.00 39.30 ?  412 ASN A C   1 
ATOM   1455 O O   . ASN A 1 189 ? -7.676  -3.107  -1.379  1.00 40.02 ?  412 ASN A O   1 
ATOM   1456 C CB  . ASN A 1 189 ? -7.876  -5.820  -1.993  1.00 39.19 ?  412 ASN A CB  1 
ATOM   1457 C CG  . ASN A 1 189 ? -9.126  -6.672  -2.049  1.00 45.45 ?  412 ASN A CG  1 
ATOM   1458 O OD1 . ASN A 1 189 ? -9.474  -7.215  -3.098  1.00 45.08 ?  412 ASN A OD1 1 
ATOM   1459 N ND2 . ASN A 1 189 ? -9.813  -6.790  -0.919  1.00 45.21 ?  412 ASN A ND2 1 
ATOM   1460 N N   . THR A 1 190 ? -6.402  -2.755  -3.194  1.00 34.06 ?  413 THR A N   1 
ATOM   1461 C CA  . THR A 1 190 ? -5.854  -1.506  -2.687  1.00 32.80 ?  413 THR A CA  1 
ATOM   1462 C C   . THR A 1 190 ? -6.547  -0.314  -3.338  1.00 33.48 ?  413 THR A C   1 
ATOM   1463 O O   . THR A 1 190 ? -7.066  -0.404  -4.453  1.00 32.62 ?  413 THR A O   1 
ATOM   1464 C CB  . THR A 1 190 ? -4.346  -1.425  -2.933  1.00 31.04 ?  413 THR A CB  1 
ATOM   1465 O OG1 . THR A 1 190 ? -4.070  -1.687  -4.315  1.00 27.20 ?  413 THR A OG1 1 
ATOM   1466 C CG2 . THR A 1 190 ? -3.611  -2.440  -2.071  1.00 28.15 ?  413 THR A CG2 1 
ATOM   1467 N N   . HIS A 1 191 ? -6.551  0.809   -2.623  1.00 31.99 ?  414 HIS A N   1 
ATOM   1468 C CA  . HIS A 1 191 ? -7.137  2.044   -3.124  1.00 30.21 ?  414 HIS A CA  1 
ATOM   1469 C C   . HIS A 1 191 ? -6.088  2.861   -3.867  1.00 28.00 ?  414 HIS A C   1 
ATOM   1470 O O   . HIS A 1 191 ? -4.931  2.942   -3.444  1.00 28.36 ?  414 HIS A O   1 
ATOM   1471 C CB  . HIS A 1 191 ? -7.721  2.877   -1.980  1.00 32.52 ?  414 HIS A CB  1 
ATOM   1472 C CG  . HIS A 1 191 ? -8.708  2.139   -1.131  1.00 33.69 ?  414 HIS A CG  1 
ATOM   1473 N ND1 . HIS A 1 191 ? -10.071 2.287   -1.275  1.00 34.49 ?  414 HIS A ND1 1 
ATOM   1474 C CD2 . HIS A 1 191 ? -8.531  1.257   -0.118  1.00 31.81 ?  414 HIS A CD2 1 
ATOM   1475 C CE1 . HIS A 1 191 ? -10.691 1.523   -0.393  1.00 36.33 ?  414 HIS A CE1 1 
ATOM   1476 N NE2 . HIS A 1 191 ? -9.779  0.888   0.321   1.00 36.05 ?  414 HIS A NE2 1 
ATOM   1477 N N   . ASN A 1 192 ? -6.499  3.465   -4.980  1.00 25.67 ?  415 ASN A N   1 
ATOM   1478 C CA  . ASN A 1 192 ? -5.623  4.378   -5.697  1.00 25.27 ?  415 ASN A CA  1 
ATOM   1479 C C   . ASN A 1 192 ? -5.495  5.691   -4.933  1.00 26.08 ?  415 ASN A C   1 
ATOM   1480 O O   . ASN A 1 192 ? -6.376  6.072   -4.158  1.00 26.52 ?  415 ASN A O   1 
ATOM   1481 C CB  . ASN A 1 192 ? -6.156  4.636   -7.106  1.00 22.19 ?  415 ASN A CB  1 
ATOM   1482 C CG  . ASN A 1 192 ? -6.004  3.431   -8.013  1.00 23.92 ?  415 ASN A CG  1 
ATOM   1483 O OD1 . ASN A 1 192 ? -5.166  2.562   -7.773  1.00 22.65 ?  415 ASN A OD1 1 
ATOM   1484 N ND2 . ASN A 1 192 ? -6.816  3.373   -9.063  1.00 20.28 ?  415 ASN A ND2 1 
ATOM   1485 N N   . VAL A 1 193 ? -4.380  6.387   -5.154  1.00 20.36 ?  416 VAL A N   1 
ATOM   1486 C CA  . VAL A 1 193 ? -4.074  7.612   -4.428  1.00 21.10 ?  416 VAL A CA  1 
ATOM   1487 C C   . VAL A 1 193 ? -3.591  8.677   -5.401  1.00 24.56 ?  416 VAL A C   1 
ATOM   1488 O O   . VAL A 1 193 ? -3.046  8.372   -6.467  1.00 23.57 ?  416 VAL A O   1 
ATOM   1489 C CB  . VAL A 1 193 ? -3.017  7.377   -3.323  1.00 21.80 ?  416 VAL A CB  1 
ATOM   1490 C CG1 . VAL A 1 193 ? -3.598  6.541   -2.191  1.00 20.29 ?  416 VAL A CG1 1 
ATOM   1491 C CG2 . VAL A 1 193 ? -1.777  6.711   -3.904  1.00 17.87 ?  416 VAL A CG2 1 
ATOM   1492 N N   . HIS A 1 194 ? -3.807  9.942   -5.024  1.00 24.73 ?  417 HIS A N   1 
ATOM   1493 C CA  . HIS A 1 194 ? -3.252  11.097  -5.734  1.00 21.59 ?  417 HIS A CA  1 
ATOM   1494 C C   . HIS A 1 194 ? -3.703  11.138  -7.193  1.00 21.44 ?  417 HIS A C   1 
ATOM   1495 O O   . HIS A 1 194 ? -2.941  11.513  -8.088  1.00 26.76 ?  417 HIS A O   1 
ATOM   1496 C CB  . HIS A 1 194 ? -1.725  11.114  -5.635  1.00 22.27 ?  417 HIS A CB  1 
ATOM   1497 C CG  . HIS A 1 194 ? -1.213  11.216  -4.232  1.00 25.91 ?  417 HIS A CG  1 
ATOM   1498 N ND1 . HIS A 1 194 ? -1.600  12.218  -3.368  1.00 26.12 ?  417 HIS A ND1 1 
ATOM   1499 C CD2 . HIS A 1 194 ? -0.350  10.435  -3.539  1.00 27.63 ?  417 HIS A CD2 1 
ATOM   1500 C CE1 . HIS A 1 194 ? -0.994  12.054  -2.206  1.00 26.77 ?  417 HIS A CE1 1 
ATOM   1501 N NE2 . HIS A 1 194 ? -0.229  10.979  -2.283  1.00 27.44 ?  417 HIS A NE2 1 
ATOM   1502 N N   . LEU A 1 195 ? -4.954  10.760  -7.435  1.00 19.73 ?  418 LEU A N   1 
ATOM   1503 C CA  . LEU A 1 195 ? -5.480  10.710  -8.791  1.00 21.14 ?  418 LEU A CA  1 
ATOM   1504 C C   . LEU A 1 195 ? -5.845  12.100  -9.289  1.00 21.46 ?  418 LEU A C   1 
ATOM   1505 O O   . LEU A 1 195 ? -6.313  12.950  -8.525  1.00 20.33 ?  418 LEU A O   1 
ATOM   1506 C CB  . LEU A 1 195 ? -6.718  9.815   -8.858  1.00 18.64 ?  418 LEU A CB  1 
ATOM   1507 C CG  . LEU A 1 195 ? -6.584  8.328   -8.539  1.00 23.45 ?  418 LEU A CG  1 
ATOM   1508 C CD1 . LEU A 1 195 ? -7.962  7.690   -8.473  1.00 22.77 ?  418 LEU A CD1 1 
ATOM   1509 C CD2 . LEU A 1 195 ? -5.719  7.637   -9.577  1.00 23.42 ?  418 LEU A CD2 1 
ATOM   1510 N N   . ALA A 1 196 ? -5.625  12.327  -10.578 1.00 25.36 ?  419 ALA A N   1 
ATOM   1511 C CA  . ALA A 1 196 ? -6.263  13.453  -11.235 1.00 20.38 ?  419 ALA A CA  1 
ATOM   1512 C C   . ALA A 1 196 ? -7.777  13.272  -11.155 1.00 20.12 ?  419 ALA A C   1 
ATOM   1513 O O   . ALA A 1 196 ? -8.271  12.145  -11.275 1.00 19.28 ?  419 ALA A O   1 
ATOM   1514 C CB  . ALA A 1 196 ? -5.810  13.555  -12.692 1.00 17.79 ?  419 ALA A CB  1 
ATOM   1515 N N   . PRO A 1 197 ? -8.540  14.340  -10.938 1.00 19.99 ?  420 PRO A N   1 
ATOM   1516 C CA  . PRO A 1 197 ? -9.975  14.170  -10.687 1.00 20.78 ?  420 PRO A CA  1 
ATOM   1517 C C   . PRO A 1 197 ? -10.722 13.709  -11.927 1.00 23.86 ?  420 PRO A C   1 
ATOM   1518 O O   . PRO A 1 197 ? -10.310 13.957  -13.063 1.00 21.47 ?  420 PRO A O   1 
ATOM   1519 C CB  . PRO A 1 197 ? -10.433 15.567  -10.256 1.00 20.92 ?  420 PRO A CB  1 
ATOM   1520 C CG  . PRO A 1 197 ? -9.435  16.499  -10.842 1.00 20.42 ?  420 PRO A CG  1 
ATOM   1521 C CD  . PRO A 1 197 ? -8.134  15.756  -10.958 1.00 19.35 ?  420 PRO A CD  1 
ATOM   1522 N N   . ALA A 1 198 ? -11.836 13.018  -11.692 1.00 21.04 ?  421 ALA A N   1 
ATOM   1523 C CA  . ALA A 1 198 ? -12.737 12.676  -12.780 1.00 23.83 ?  421 ALA A CA  1 
ATOM   1524 C C   . ALA A 1 198 ? -13.346 13.943  -13.366 1.00 25.52 ?  421 ALA A C   1 
ATOM   1525 O O   . ALA A 1 198 ? -13.488 14.964  -12.686 1.00 24.95 ?  421 ALA A O   1 
ATOM   1526 C CB  . ALA A 1 198 ? -13.840 11.736  -12.291 1.00 21.42 ?  421 ALA A CB  1 
ATOM   1527 N N   . VAL A 1 199 ? -13.700 13.879  -14.646 1.00 20.12 ?  422 VAL A N   1 
ATOM   1528 C CA  . VAL A 1 199 ? -14.263 15.026  -15.344 1.00 19.27 ?  422 VAL A CA  1 
ATOM   1529 C C   . VAL A 1 199 ? -15.622 14.646  -15.912 1.00 23.16 ?  422 VAL A C   1 
ATOM   1530 O O   . VAL A 1 199 ? -15.878 13.487  -16.259 1.00 21.53 ?  422 VAL A O   1 
ATOM   1531 C CB  . VAL A 1 199 ? -13.328 15.544  -16.460 1.00 22.67 ?  422 VAL A CB  1 
ATOM   1532 C CG1 . VAL A 1 199 ? -11.980 15.948  -15.881 1.00 19.53 ?  422 VAL A CG1 1 
ATOM   1533 C CG2 . VAL A 1 199 ? -13.154 14.493  -17.545 1.00 22.89 ?  422 VAL A CG2 1 
ATOM   1534 N N   . ALA A 1 200 ? -16.501 15.641  -15.996 1.00 22.83 ?  423 ALA A N   1 
ATOM   1535 C CA  . ALA A 1 200 ? -17.838 15.465  -16.542 1.00 24.41 ?  423 ALA A CA  1 
ATOM   1536 C C   . ALA A 1 200 ? -18.368 16.831  -16.938 1.00 28.44 ?  423 ALA A C   1 
ATOM   1537 O O   . ALA A 1 200 ? -17.997 17.834  -16.318 1.00 25.60 ?  423 ALA A O   1 
ATOM   1538 C CB  . ALA A 1 200 ? -18.776 14.800  -15.524 1.00 18.71 ?  423 ALA A CB  1 
ATOM   1539 N N   . PRO A 1 201 ? -19.212 16.911  -17.965 1.00 27.05 ?  424 PRO A N   1 
ATOM   1540 C CA  . PRO A 1 201 ? -19.834 18.197  -18.297 1.00 26.48 ?  424 PRO A CA  1 
ATOM   1541 C C   . PRO A 1 201 ? -20.711 18.685  -17.154 1.00 34.18 ?  424 PRO A C   1 
ATOM   1542 O O   . PRO A 1 201 ? -21.427 17.908  -16.519 1.00 34.77 ?  424 PRO A O   1 
ATOM   1543 C CB  . PRO A 1 201 ? -20.662 17.884  -19.550 1.00 27.05 ?  424 PRO A CB  1 
ATOM   1544 C CG  . PRO A 1 201 ? -20.821 16.398  -19.558 1.00 27.74 ?  424 PRO A CG  1 
ATOM   1545 C CD  . PRO A 1 201 ? -19.596 15.845  -18.905 1.00 29.13 ?  424 PRO A CD  1 
ATOM   1546 N N   . THR A 1 202 ? -20.640 19.989  -16.889 1.00 36.56 ?  425 THR A N   1 
ATOM   1547 C CA  . THR A 1 202 ? -21.428 20.616  -15.833 1.00 34.85 ?  425 THR A CA  1 
ATOM   1548 C C   . THR A 1 202 ? -22.556 21.450  -16.431 1.00 38.77 ?  425 THR A C   1 
ATOM   1549 O O   . THR A 1 202 ? -23.730 21.142  -16.214 1.00 38.02 ?  425 THR A O   1 
ATOM   1550 C CB  . THR A 1 202 ? -20.533 21.469  -14.930 1.00 34.60 ?  425 THR A CB  1 
ATOM   1551 O OG1 . THR A 1 202 ? -19.633 22.241  -15.736 1.00 31.99 ?  425 THR A OG1 1 
ATOM   1552 C CG2 . THR A 1 202 ? -19.730 20.584  -13.990 1.00 30.59 ?  425 THR A CG2 1 
ATOM   1553 N N   . PHE A 1 203 ? -22.227 22.507  -17.169 1.00 36.05 ?  426 PHE A N   1 
ATOM   1554 C CA  . PHE A 1 203 ? -23.235 23.321  -17.834 1.00 36.27 ?  426 PHE A CA  1 
ATOM   1555 C C   . PHE A 1 203 ? -24.103 22.435  -18.725 1.00 37.86 ?  426 PHE A C   1 
ATOM   1556 O O   . PHE A 1 203 ? -23.565 21.654  -19.523 1.00 38.51 ?  426 PHE A O   1 
ATOM   1557 C CB  . PHE A 1 203 ? -22.553 24.412  -18.662 1.00 33.92 ?  426 PHE A CB  1 
ATOM   1558 C CG  . PHE A 1 203 ? -23.401 25.631  -18.898 1.00 40.07 ?  426 PHE A CG  1 
ATOM   1559 C CD1 . PHE A 1 203 ? -24.106 26.221  -17.861 1.00 40.17 ?  426 PHE A CD1 1 
ATOM   1560 C CD2 . PHE A 1 203 ? -23.470 26.203  -20.158 1.00 36.80 ?  426 PHE A CD2 1 
ATOM   1561 C CE1 . PHE A 1 203 ? -24.884 27.345  -18.084 1.00 35.02 ?  426 PHE A CE1 1 
ATOM   1562 C CE2 . PHE A 1 203 ? -24.241 27.326  -20.387 1.00 34.23 ?  426 PHE A CE2 1 
ATOM   1563 C CZ  . PHE A 1 203 ? -24.949 27.899  -19.348 1.00 34.59 ?  426 PHE A CZ  1 
ATOM   1564 N N   . PRO A 1 204 ? -25.429 22.518  -18.625 1.00 40.14 ?  427 PRO A N   1 
ATOM   1565 C CA  . PRO A 1 204 ? -26.276 21.599  -19.391 1.00 38.09 ?  427 PRO A CA  1 
ATOM   1566 C C   . PRO A 1 204 ? -26.308 21.960  -20.867 1.00 37.02 ?  427 PRO A C   1 
ATOM   1567 O O   . PRO A 1 204 ? -26.116 23.114  -21.259 1.00 38.51 ?  427 PRO A O   1 
ATOM   1568 C CB  . PRO A 1 204 ? -27.656 21.757  -18.743 1.00 37.52 ?  427 PRO A CB  1 
ATOM   1569 C CG  . PRO A 1 204 ? -27.618 23.072  -18.014 1.00 38.90 ?  427 PRO A CG  1 
ATOM   1570 C CD  . PRO A 1 204 ? -26.213 23.615  -18.037 1.00 39.13 ?  427 PRO A CD  1 
ATOM   1571 N N   . GLY A 1 205 ? -26.563 20.944  -21.688 1.00 31.63 ?  428 GLY A N   1 
ATOM   1572 C CA  . GLY A 1 205 ? -26.412 21.074  -23.120 1.00 26.64 ?  428 GLY A CA  1 
ATOM   1573 C C   . GLY A 1 205 ? -24.993 20.916  -23.612 1.00 30.92 ?  428 GLY A C   1 
ATOM   1574 O O   . GLY A 1 205 ? -24.724 21.199  -24.785 1.00 27.58 ?  428 GLY A O   1 
ATOM   1575 N N   . GLU A 1 206 ? -24.077 20.479  -22.752 1.00 28.16 ?  429 GLU A N   1 
ATOM   1576 C CA  . GLU A 1 206 ? -22.677 20.307  -23.102 1.00 28.11 ?  429 GLU A CA  1 
ATOM   1577 C C   . GLU A 1 206 ? -22.245 18.871  -22.840 1.00 25.18 ?  429 GLU A C   1 
ATOM   1578 O O   . GLU A 1 206 ? -22.825 18.171  -22.004 1.00 24.40 ?  429 GLU A O   1 
ATOM   1579 C CB  . GLU A 1 206 ? -21.780 21.269  -22.311 1.00 27.14 ?  429 GLU A CB  1 
ATOM   1580 C CG  . GLU A 1 206 ? -22.026 22.738  -22.610 1.00 30.20 ?  429 GLU A CG  1 
ATOM   1581 C CD  . GLU A 1 206 ? -20.932 23.635  -22.065 1.00 31.65 ?  429 GLU A CD  1 
ATOM   1582 O OE1 . GLU A 1 206 ? -19.939 23.104  -21.524 1.00 32.77 ?  429 GLU A OE1 1 
ATOM   1583 O OE2 . GLU A 1 206 ? -21.064 24.872  -22.183 1.00 34.78 -1 429 GLU A OE2 1 
ATOM   1584 N N   . GLN A 1 207 ? -21.219 18.441  -23.569 1.00 25.97 ?  430 GLN A N   1 
ATOM   1585 C CA  . GLN A 1 207 ? -20.633 17.121  -23.401 1.00 24.52 ?  430 GLN A CA  1 
ATOM   1586 C C   . GLN A 1 207 ? -19.126 17.232  -23.578 1.00 23.52 ?  430 GLN A C   1 
ATOM   1587 O O   . GLN A 1 207 ? -18.617 18.208  -24.135 1.00 20.38 ?  430 GLN A O   1 
ATOM   1588 C CB  . GLN A 1 207 ? -21.214 16.109  -24.399 1.00 22.22 ?  430 GLN A CB  1 
ATOM   1589 C CG  . GLN A 1 207 ? -22.508 15.453  -23.945 1.00 21.27 ?  430 GLN A CG  1 
ATOM   1590 C CD  . GLN A 1 207 ? -23.192 14.686  -25.061 1.00 24.72 ?  430 GLN A CD  1 
ATOM   1591 O OE1 . GLN A 1 207 ? -22.668 14.582  -26.170 1.00 25.16 ?  430 GLN A OE1 1 
ATOM   1592 N NE2 . GLN A 1 207 ? -24.368 14.142  -24.771 1.00 22.49 ?  430 GLN A NE2 1 
ATOM   1593 N N   . LEU A 1 208 ? -18.415 16.218  -23.094 1.00 23.89 ?  431 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 208 ? -16.963 16.211  -23.196 1.00 21.13 ?  431 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 208 ? -16.525 16.027  -24.645 1.00 22.90 ?  431 LEU A C   1 
ATOM   1596 O O   . LEU A 1 208 ? -17.172 15.331  -25.432 1.00 21.53 ?  431 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 208 ? -16.369 15.099  -22.331 1.00 20.38 ?  431 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 208 ? -16.584 15.181  -20.819 1.00 27.27 ?  431 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 208 ? -16.076 13.919  -20.134 1.00 23.23 ?  431 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 208 ? -15.907 16.414  -20.245 1.00 24.10 ?  431 LEU A CD2 1 
ATOM   1601 N N   . LEU A 1 209 ? -15.412 16.667  -24.995 1.00 24.39 ?  432 LEU A N   1 
ATOM   1602 C CA  . LEU A 1 209 ? -14.785 16.509  -26.300 1.00 22.97 ?  432 LEU A CA  1 
ATOM   1603 C C   . LEU A 1 209 ? -13.480 15.745  -26.127 1.00 22.88 ?  432 LEU A C   1 
ATOM   1604 O O   . LEU A 1 209 ? -12.625 16.142  -25.328 1.00 23.61 ?  432 LEU A O   1 
ATOM   1605 C CB  . LEU A 1 209 ? -14.526 17.862  -26.963 1.00 20.42 ?  432 LEU A CB  1 
ATOM   1606 C CG  . LEU A 1 209 ? -13.886 17.783  -28.352 1.00 24.24 ?  432 LEU A CG  1 
ATOM   1607 C CD1 . LEU A 1 209 ? -14.909 17.351  -29.392 1.00 21.34 ?  432 LEU A CD1 1 
ATOM   1608 C CD2 . LEU A 1 209 ? -13.253 19.111  -28.740 1.00 22.98 ?  432 LEU A CD2 1 
ATOM   1609 N N   . PHE A 1 210 ? -13.332 14.656  -26.872 1.00 23.02 ?  433 PHE A N   1 
ATOM   1610 C CA  . PHE A 1 210 ? -12.201 13.755  -26.727 1.00 20.09 ?  433 PHE A CA  1 
ATOM   1611 C C   . PHE A 1 210 ? -11.318 13.781  -27.968 1.00 21.31 ?  433 PHE A C   1 
ATOM   1612 O O   . PHE A 1 210 ? -11.801 13.924  -29.095 1.00 19.11 ?  433 PHE A O   1 
ATOM   1613 C CB  . PHE A 1 210 ? -12.674 12.322  -26.473 1.00 18.11 ?  433 PHE A CB  1 
ATOM   1614 C CG  . PHE A 1 210 ? -13.405 12.143  -25.174 1.00 22.62 ?  433 PHE A CG  1 
ATOM   1615 C CD1 . PHE A 1 210 ? -12.719 12.137  -23.971 1.00 21.36 ?  433 PHE A CD1 1 
ATOM   1616 C CD2 . PHE A 1 210 ? -14.779 11.971  -25.156 1.00 22.77 ?  433 PHE A CD2 1 
ATOM   1617 C CE1 . PHE A 1 210 ? -13.390 11.969  -22.775 1.00 21.88 ?  433 PHE A CE1 1 
ATOM   1618 C CE2 . PHE A 1 210 ? -15.455 11.802  -23.962 1.00 21.11 ?  433 PHE A CE2 1 
ATOM   1619 C CZ  . PHE A 1 210 ? -14.760 11.801  -22.771 1.00 20.86 ?  433 PHE A CZ  1 
ATOM   1620 N N   . PHE A 1 211 ? -10.014 13.637  -27.745 1.00 19.02 ?  434 PHE A N   1 
ATOM   1621 C CA  . PHE A 1 211 ? -9.038  13.470  -28.816 1.00 18.89 ?  434 PHE A CA  1 
ATOM   1622 C C   . PHE A 1 211 ? -8.776  11.974  -28.957 1.00 20.51 ?  434 PHE A C   1 
ATOM   1623 O O   . PHE A 1 211 ? -8.172  11.357  -28.073 1.00 18.00 ?  434 PHE A O   1 
ATOM   1624 C CB  . PHE A 1 211 ? -7.758  14.246  -28.511 1.00 19.24 ?  434 PHE A CB  1 
ATOM   1625 C CG  . PHE A 1 211 ? -7.970  15.727  -28.340 1.00 19.33 ?  434 PHE A CG  1 
ATOM   1626 C CD1 . PHE A 1 211 ? -8.403  16.247  -27.130 1.00 19.95 ?  434 PHE A CD1 1 
ATOM   1627 C CD2 . PHE A 1 211 ? -7.735  16.600  -29.389 1.00 21.24 ?  434 PHE A CD2 1 
ATOM   1628 C CE1 . PHE A 1 211 ? -8.599  17.607  -26.972 1.00 21.55 ?  434 PHE A CE1 1 
ATOM   1629 C CE2 . PHE A 1 211 ? -7.929  17.961  -29.237 1.00 19.43 ?  434 PHE A CE2 1 
ATOM   1630 C CZ  . PHE A 1 211 ? -8.361  18.464  -28.027 1.00 19.66 ?  434 PHE A CZ  1 
ATOM   1631 N N   . ARG A 1 212 ? -9.233  11.394  -30.063 1.00 18.04 ?  435 ARG A N   1 
ATOM   1632 C CA  . ARG A 1 212 ? -9.374  9.951   -30.195 1.00 20.82 ?  435 ARG A CA  1 
ATOM   1633 C C   . ARG A 1 212 ? -8.344  9.369   -31.156 1.00 21.47 ?  435 ARG A C   1 
ATOM   1634 O O   . ARG A 1 212 ? -8.061  9.948   -32.210 1.00 17.04 ?  435 ARG A O   1 
ATOM   1635 C CB  . ARG A 1 212 ? -10.786 9.595   -30.676 1.00 20.58 ?  435 ARG A CB  1 
ATOM   1636 C CG  . ARG A 1 212 ? -10.929 8.188   -31.236 1.00 19.97 ?  435 ARG A CG  1 
ATOM   1637 C CD  . ARG A 1 212 ? -12.387 7.772   -31.333 1.00 18.65 ?  435 ARG A CD  1 
ATOM   1638 N NE  . ARG A 1 212 ? -12.999 7.616   -30.020 1.00 21.82 ?  435 ARG A NE  1 
ATOM   1639 C CZ  . ARG A 1 212 ? -14.124 6.951   -29.793 1.00 19.18 ?  435 ARG A CZ  1 
ATOM   1640 N NH1 . ARG A 1 212 ? -14.790 6.364   -30.774 1.00 17.46 ?  435 ARG A NH1 1 
ATOM   1641 N NH2 . ARG A 1 212 ? -14.593 6.874   -28.551 1.00 17.73 ?  435 ARG A NH2 1 
ATOM   1642 N N   . SER A 1 213 ? -7.792  8.218   -30.780 1.00 20.91 ?  436 SER A N   1 
ATOM   1643 C CA  . SER A 1 213 ? -6.966  7.393   -31.647 1.00 20.39 ?  436 SER A CA  1 
ATOM   1644 C C   . SER A 1 213 ? -7.545  5.985   -31.694 1.00 19.35 ?  436 SER A C   1 
ATOM   1645 O O   . SER A 1 213 ? -8.503  5.655   -30.990 1.00 18.12 ?  436 SER A O   1 
ATOM   1646 C CB  . SER A 1 213 ? -5.511  7.349   -31.160 1.00 19.46 ?  436 SER A CB  1 
ATOM   1647 O OG  . SER A 1 213 ? -4.958  8.649   -31.061 1.00 21.42 ?  436 SER A OG  1 
ATOM   1648 N N   . THR A 1 214 ? -6.952  5.148   -32.540 1.00 20.34 ?  437 THR A N   1 
ATOM   1649 C CA  . THR A 1 214 ? -7.288  3.730   -32.616 1.00 20.92 ?  437 THR A CA  1 
ATOM   1650 C C   . THR A 1 214 ? -6.031  2.936   -32.292 1.00 20.55 ?  437 THR A C   1 
ATOM   1651 O O   . THR A 1 214 ? -5.058  2.969   -33.054 1.00 22.66 ?  437 THR A O   1 
ATOM   1652 C CB  . THR A 1 214 ? -7.835  3.351   -33.993 1.00 22.08 ?  437 THR A CB  1 
ATOM   1653 O OG1 . THR A 1 214 ? -8.835  4.296   -34.394 1.00 22.25 ?  437 THR A OG1 1 
ATOM   1654 C CG2 . THR A 1 214 ? -8.446  1.957   -33.954 1.00 18.06 ?  437 THR A CG2 1 
ATOM   1655 N N   . MET A 1 215 ? -6.045  2.241   -31.164 1.00 22.86 ?  438 MET A N   1 
ATOM   1656 C CA  . MET A 1 215 ? -4.907  1.412   -30.793 1.00 20.70 ?  438 MET A CA  1 
ATOM   1657 C C   . MET A 1 215 ? -4.768  0.263   -31.784 1.00 19.73 ?  438 MET A C   1 
ATOM   1658 O O   . MET A 1 215 ? -5.774  -0.359  -32.145 1.00 18.94 ?  438 MET A O   1 
ATOM   1659 C CB  . MET A 1 215 ? -5.072  0.870   -29.376 1.00 18.87 ?  438 MET A CB  1 
ATOM   1660 C CG  . MET A 1 215 ? -4.516  1.779   -28.291 1.00 21.52 ?  438 MET A CG  1 
ATOM   1661 S SD  . MET A 1 215 ? -5.242  1.487   -26.664 1.00 23.23 ?  438 MET A SD  1 
ATOM   1662 C CE  . MET A 1 215 ? -6.959  1.211   -27.097 1.00 25.45 ?  438 MET A CE  1 
ATOM   1663 N N   . PRO A 1 216 ? -3.562  -0.031  -32.267 1.00 19.84 ?  439 PRO A N   1 
ATOM   1664 C CA  . PRO A 1 216 ? -3.388  -1.217  -33.113 1.00 16.55 ?  439 PRO A CA  1 
ATOM   1665 C C   . PRO A 1 216 ? -3.798  -2.479  -32.370 1.00 20.63 ?  439 PRO A C   1 
ATOM   1666 O O   . PRO A 1 216 ? -3.574  -2.614  -31.165 1.00 22.05 ?  439 PRO A O   1 
ATOM   1667 C CB  . PRO A 1 216 ? -1.888  -1.211  -33.429 1.00 16.35 ?  439 PRO A CB  1 
ATOM   1668 C CG  . PRO A 1 216 ? -1.481  0.212   -33.299 1.00 16.93 ?  439 PRO A CG  1 
ATOM   1669 C CD  . PRO A 1 216 ? -2.341  0.790   -32.204 1.00 18.10 ?  439 PRO A CD  1 
ATOM   1670 N N   . GLY A 1 217 ? -4.417  -3.401  -33.097 1.00 18.98 ?  440 GLY A N   1 
ATOM   1671 C CA  . GLY A 1 217 ? -4.821  -4.681  -32.542 1.00 22.18 ?  440 GLY A CA  1 
ATOM   1672 C C   . GLY A 1 217 ? -3.815  -5.759  -32.902 1.00 20.38 ?  440 GLY A C   1 
ATOM   1673 O O   . GLY A 1 217 ? -3.304  -5.798  -34.021 1.00 22.38 ?  440 GLY A O   1 
ATOM   1674 N N   . CYS A 1 218 ? -3.533  -6.635  -31.937 1.00 20.76 ?  441 CYS A N   1 
ATOM   1675 C CA  . CYS A 1 218 ? -2.556  -7.693  -32.142 1.00 22.69 ?  441 CYS A CA  1 
ATOM   1676 C C   . CYS A 1 218 ? -3.148  -9.094  -32.129 1.00 21.46 ?  441 CYS A C   1 
ATOM   1677 O O   . CYS A 1 218 ? -2.489  -10.026 -32.596 1.00 23.60 ?  441 CYS A O   1 
ATOM   1678 C CB  . CYS A 1 218 ? -1.449  -7.610  -31.080 1.00 20.21 ?  441 CYS A CB  1 
ATOM   1679 S SG  . CYS A 1 218 ? -0.447  -6.103  -31.156 1.00 23.03 ?  441 CYS A SG  1 
ATOM   1680 N N   . SER A 1 219 ? -4.364  -9.265  -31.615 1.00 19.08 ?  442 SER A N   1 
ATOM   1681 C CA  . SER A 1 219 ? -5.024  -10.561 -31.575 1.00 20.51 ?  442 SER A CA  1 
ATOM   1682 C C   . SER A 1 219 ? -6.439  -10.363 -31.060 1.00 22.11 ?  442 SER A C   1 
ATOM   1683 O O   . SER A 1 219 ? -6.678  -9.511  -30.202 1.00 22.39 ?  442 SER A O   1 
ATOM   1684 C CB  . SER A 1 219 ? -4.277  -11.557 -30.675 1.00 23.75 ?  442 SER A CB  1 
ATOM   1685 O OG  . SER A 1 219 ? -4.826  -12.860 -30.791 1.00 31.34 ?  442 SER A OG  1 
ATOM   1686 N N   . GLY A 1 220 ? -7.363  -11.153 -31.595 1.00 20.67 ?  443 GLY A N   1 
ATOM   1687 C CA  . GLY A 1 220 ? -8.729  -11.145 -31.110 1.00 20.03 ?  443 GLY A CA  1 
ATOM   1688 C C   . GLY A 1 220 ? -9.547  -9.986  -31.653 1.00 24.41 ?  443 GLY A C   1 
ATOM   1689 O O   . GLY A 1 220 ? -9.296  -9.462  -32.741 1.00 24.25 ?  443 GLY A O   1 
ATOM   1690 N N   . TYR A 1 221 ? -10.540 -9.581  -30.863 1.00 23.88 ?  444 TYR A N   1 
ATOM   1691 C CA  . TYR A 1 221 ? -11.511 -8.558  -31.251 1.00 22.08 ?  444 TYR A CA  1 
ATOM   1692 C C   . TYR A 1 221 ? -11.567 -7.476  -30.181 1.00 22.47 ?  444 TYR A C   1 
ATOM   1693 O O   . TYR A 1 221 ? -12.596 -7.291  -29.519 1.00 20.17 ?  444 TYR A O   1 
ATOM   1694 C CB  . TYR A 1 221 ? -12.892 -9.180  -31.464 1.00 23.10 ?  444 TYR A CB  1 
ATOM   1695 C CG  . TYR A 1 221 ? -12.926 -10.229 -32.548 1.00 23.63 ?  444 TYR A CG  1 
ATOM   1696 C CD1 . TYR A 1 221 ? -12.523 -11.534 -32.291 1.00 21.81 ?  444 TYR A CD1 1 
ATOM   1697 C CD2 . TYR A 1 221 ? -13.354 -9.915  -33.830 1.00 22.47 ?  444 TYR A CD2 1 
ATOM   1698 C CE1 . TYR A 1 221 ? -12.550 -12.496 -33.279 1.00 23.75 ?  444 TYR A CE1 1 
ATOM   1699 C CE2 . TYR A 1 221 ? -13.388 -10.874 -34.825 1.00 19.94 ?  444 TYR A CE2 1 
ATOM   1700 C CZ  . TYR A 1 221 ? -12.982 -12.161 -34.544 1.00 21.25 ?  444 TYR A CZ  1 
ATOM   1701 O OH  . TYR A 1 221 ? -13.009 -13.121 -35.529 1.00 26.94 ?  444 TYR A OH  1 
ATOM   1702 N N   . PRO A 1 222 ? -10.488 -6.722  -30.002 1.00 21.77 ?  445 PRO A N   1 
ATOM   1703 C CA  . PRO A 1 222 ? -10.431 -5.769  -28.892 1.00 21.24 ?  445 PRO A CA  1 
ATOM   1704 C C   . PRO A 1 222 ? -11.193 -4.485  -29.187 1.00 22.33 ?  445 PRO A C   1 
ATOM   1705 O O   . PRO A 1 222 ? -11.520 -4.163  -30.330 1.00 19.04 ?  445 PRO A O   1 
ATOM   1706 C CB  . PRO A 1 222 ? -8.933  -5.487  -28.734 1.00 21.34 ?  445 PRO A CB  1 
ATOM   1707 C CG  . PRO A 1 222 ? -8.317  -5.839  -30.053 1.00 21.61 ?  445 PRO A CG  1 
ATOM   1708 C CD  . PRO A 1 222 ? -9.290  -6.658  -30.857 1.00 20.34 ?  445 PRO A CD  1 
ATOM   1709 N N   . ASN A 1 223 ? -11.480 -3.754  -28.111 1.00 19.81 ?  446 ASN A N   1 
ATOM   1710 C CA  . ASN A 1 223 ? -11.996 -2.392  -28.202 1.00 20.88 ?  446 ASN A CA  1 
ATOM   1711 C C   . ASN A 1 223 ? -10.799 -1.456  -28.311 1.00 20.46 ?  446 ASN A C   1 
ATOM   1712 O O   . ASN A 1 223 ? -10.089 -1.227  -27.326 1.00 22.31 ?  446 ASN A O   1 
ATOM   1713 C CB  . ASN A 1 223 ? -12.859 -2.051  -26.989 1.00 21.59 ?  446 ASN A CB  1 
ATOM   1714 C CG  . ASN A 1 223 ? -13.619 -0.744  -27.157 1.00 22.58 ?  446 ASN A CG  1 
ATOM   1715 O OD1 . ASN A 1 223 ? -13.295 0.074   -28.019 1.00 21.04 ?  446 ASN A OD1 1 
ATOM   1716 N ND2 . ASN A 1 223 ? -14.635 -0.542  -26.326 1.00 23.83 ?  446 ASN A ND2 1 
ATOM   1717 N N   . MET A 1 224 ? -10.573 -0.918  -29.505 1.00 20.07 ?  447 MET A N   1 
ATOM   1718 C CA  . MET A 1 224 ? -9.371  -0.151  -29.798 1.00 21.91 ?  447 MET A CA  1 
ATOM   1719 C C   . MET A 1 224 ? -9.588  1.354   -29.705 1.00 24.15 ?  447 MET A C   1 
ATOM   1720 O O   . MET A 1 224 ? -8.672  2.121   -30.021 1.00 22.03 ?  447 MET A O   1 
ATOM   1721 C CB  . MET A 1 224 ? -8.844  -0.533  -31.182 1.00 18.23 ?  447 MET A CB  1 
ATOM   1722 C CG  . MET A 1 224 ? -8.497  -2.013  -31.298 1.00 22.70 ?  447 MET A CG  1 
ATOM   1723 S SD  . MET A 1 224 ? -7.938  -2.519  -32.935 1.00 21.85 ?  447 MET A SD  1 
ATOM   1724 C CE  . MET A 1 224 ? -9.499  -2.674  -33.798 1.00 17.41 ?  447 MET A CE  1 
ATOM   1725 N N   . ASP A 1 225 ? -10.768 1.794   -29.275 1.00 21.80 ?  448 ASP A N   1 
ATOM   1726 C CA  . ASP A 1 225 ? -11.005 3.217   -29.070 1.00 21.19 ?  448 ASP A CA  1 
ATOM   1727 C C   . ASP A 1 225 ? -10.194 3.712   -27.881 1.00 24.80 ?  448 ASP A C   1 
ATOM   1728 O O   . ASP A 1 225 ? -10.187 3.087   -26.817 1.00 25.62 ?  448 ASP A O   1 
ATOM   1729 C CB  . ASP A 1 225 ? -12.491 3.485   -28.837 1.00 21.32 ?  448 ASP A CB  1 
ATOM   1730 C CG  . ASP A 1 225 ? -13.356 3.025   -29.991 1.00 24.13 ?  448 ASP A CG  1 
ATOM   1731 O OD1 . ASP A 1 225 ? -12.871 3.035   -31.142 1.00 22.87 ?  448 ASP A OD1 1 
ATOM   1732 O OD2 . ASP A 1 225 ? -14.523 2.653   -29.747 1.00 28.16 -1 448 ASP A OD2 1 
ATOM   1733 N N   . LEU A 1 226 ? -9.504  4.836   -28.060 1.00 21.15 ?  449 LEU A N   1 
ATOM   1734 C CA  . LEU A 1 226 ? -8.734  5.441   -26.977 1.00 19.99 ?  449 LEU A CA  1 
ATOM   1735 C C   . LEU A 1 226 ? -8.888  6.952   -27.053 1.00 21.07 ?  449 LEU A C   1 
ATOM   1736 O O   . LEU A 1 226 ? -8.299  7.599   -27.925 1.00 18.96 ?  449 LEU A O   1 
ATOM   1737 C CB  . LEU A 1 226 ? -7.262  5.047   -27.041 1.00 18.31 ?  449 LEU A CB  1 
ATOM   1738 C CG  . LEU A 1 226 ? -6.514  5.541   -25.804 1.00 20.21 ?  449 LEU A CG  1 
ATOM   1739 C CD1 . LEU A 1 226 ? -6.870  4.696   -24.592 1.00 18.06 ?  449 LEU A CD1 1 
ATOM   1740 C CD2 . LEU A 1 226 ? -5.034  5.533   -26.048 1.00 19.62 ?  449 LEU A CD2 1 
ATOM   1741 N N   . ASP A 1 227 ? -9.663  7.506   -26.130 1.00 19.07 ?  450 ASP A N   1 
ATOM   1742 C CA  . ASP A 1 227 ? -9.920  8.934   -26.057 1.00 17.93 ?  450 ASP A CA  1 
ATOM   1743 C C   . ASP A 1 227 ? -9.054  9.563   -24.973 1.00 22.50 ?  450 ASP A C   1 
ATOM   1744 O O   . ASP A 1 227 ? -8.882  8.989   -23.894 1.00 23.97 ?  450 ASP A O   1 
ATOM   1745 C CB  . ASP A 1 227 ? -11.396 9.193   -25.759 1.00 19.38 ?  450 ASP A CB  1 
ATOM   1746 C CG  . ASP A 1 227 ? -12.320 8.513   -26.750 1.00 20.99 ?  450 ASP A CG  1 
ATOM   1747 O OD1 . ASP A 1 227 ? -12.151 8.726   -27.968 1.00 17.51 ?  450 ASP A OD1 1 
ATOM   1748 O OD2 . ASP A 1 227 ? -13.213 7.759   -26.310 1.00 22.14 -1 450 ASP A OD2 1 
ATOM   1749 N N   . CYS A 1 228 ? -8.510  10.742  -25.264 1.00 19.15 ?  451 CYS A N   1 
ATOM   1750 C CA  . CYS A 1 228 ? -7.721  11.487  -24.296 1.00 17.72 ?  451 CYS A CA  1 
ATOM   1751 C C   . CYS A 1 228 ? -8.249  12.912  -24.203 1.00 18.80 ?  451 CYS A C   1 
ATOM   1752 O O   . CYS A 1 228 ? -8.875  13.430  -25.131 1.00 18.72 ?  451 CYS A O   1 
ATOM   1753 C CB  . CYS A 1 228 ? -6.226  11.488  -24.653 1.00 20.14 ?  451 CYS A CB  1 
ATOM   1754 S SG  . CYS A 1 228 ? -5.756  12.565  -26.022 1.00 22.99 ?  451 CYS A SG  1 
ATOM   1755 N N   . LEU A 1 229 ? -7.988  13.542  -23.057 1.00 20.09 ?  452 LEU A N   1 
ATOM   1756 C CA  . LEU A 1 229 ? -8.549  14.861  -22.788 1.00 18.46 ?  452 LEU A CA  1 
ATOM   1757 C C   . LEU A 1 229 ? -7.746  15.977  -23.441 1.00 17.89 ?  452 LEU A C   1 
ATOM   1758 O O   . LEU A 1 229 ? -8.316  17.012  -23.805 1.00 18.94 ?  452 LEU A O   1 
ATOM   1759 C CB  . LEU A 1 229 ? -8.641  15.089  -21.279 1.00 17.96 ?  452 LEU A CB  1 
ATOM   1760 C CG  . LEU A 1 229 ? -9.421  14.008  -20.528 1.00 21.23 ?  452 LEU A CG  1 
ATOM   1761 C CD1 . LEU A 1 229 ? -9.473  14.303  -19.038 1.00 16.89 ?  452 LEU A CD1 1 
ATOM   1762 C CD2 . LEU A 1 229 ? -10.823 13.872  -21.101 1.00 18.64 ?  452 LEU A CD2 1 
ATOM   1763 N N   . LEU A 1 230 ? -6.434  15.796  -23.591 1.00 16.93 ?  453 LEU A N   1 
ATOM   1764 C CA  . LEU A 1 230 ? -5.577  16.795  -24.204 1.00 16.05 ?  453 LEU A CA  1 
ATOM   1765 C C   . LEU A 1 230 ? -4.551  16.093  -25.081 1.00 17.27 ?  453 LEU A C   1 
ATOM   1766 O O   . LEU A 1 230 ? -4.042  15.026  -24.704 1.00 17.56 ?  453 LEU A O   1 
ATOM   1767 C CB  . LEU A 1 230 ? -4.850  17.650  -23.155 1.00 16.02 ?  453 LEU A CB  1 
ATOM   1768 C CG  . LEU A 1 230 ? -5.670  18.215  -21.994 1.00 19.38 ?  453 LEU A CG  1 
ATOM   1769 C CD1 . LEU A 1 230 ? -4.786  18.452  -20.778 1.00 22.81 ?  453 LEU A CD1 1 
ATOM   1770 C CD2 . LEU A 1 230 ? -6.373  19.496  -22.410 1.00 15.89 ?  453 LEU A CD2 1 
ATOM   1771 N N   . PRO A 1 231 ? -4.232  16.653  -26.247 1.00 19.84 ?  454 PRO A N   1 
ATOM   1772 C CA  . PRO A 1 231 ? -3.117  16.112  -27.030 1.00 19.33 ?  454 PRO A CA  1 
ATOM   1773 C C   . PRO A 1 231 ? -1.820  16.253  -26.251 1.00 19.76 ?  454 PRO A C   1 
ATOM   1774 O O   . PRO A 1 231 ? -1.634  17.199  -25.483 1.00 19.03 ?  454 PRO A O   1 
ATOM   1775 C CB  . PRO A 1 231 ? -3.107  16.971  -28.303 1.00 19.81 ?  454 PRO A CB  1 
ATOM   1776 C CG  . PRO A 1 231 ? -4.341  17.812  -28.258 1.00 19.92 ?  454 PRO A CG  1 
ATOM   1777 C CD  . PRO A 1 231 ? -4.817  17.863  -26.847 1.00 21.21 ?  454 PRO A CD  1 
ATOM   1778 N N   . GLN A 1 232 ? -0.921  15.285  -26.445 1.00 18.58 ?  455 GLN A N   1 
ATOM   1779 C CA  . GLN A 1 232 ? 0.336   15.299  -25.703 1.00 18.95 ?  455 GLN A CA  1 
ATOM   1780 C C   . GLN A 1 232 ? 1.148   16.553  -26.006 1.00 20.88 ?  455 GLN A C   1 
ATOM   1781 O O   . GLN A 1 232 ? 1.924   17.011  -25.159 1.00 20.58 ?  455 GLN A O   1 
ATOM   1782 C CB  . GLN A 1 232 ? 1.145   14.037  -26.013 1.00 17.59 ?  455 GLN A CB  1 
ATOM   1783 C CG  . GLN A 1 232 ? 2.458   13.931  -25.246 1.00 19.67 ?  455 GLN A CG  1 
ATOM   1784 C CD  . GLN A 1 232 ? 2.266   13.920  -23.738 1.00 22.21 ?  455 GLN A CD  1 
ATOM   1785 O OE1 . GLN A 1 232 ? 1.207   13.543  -23.234 1.00 20.56 ?  455 GLN A OE1 1 
ATOM   1786 N NE2 . GLN A 1 232 ? 3.295   14.342  -23.010 1.00 22.71 ?  455 GLN A NE2 1 
ATOM   1787 N N   . GLU A 1 233 ? 0.972   17.130  -27.197 1.00 20.07 ?  456 GLU A N   1 
ATOM   1788 C CA  . GLU A 1 233 ? 1.641   18.387  -27.513 1.00 21.26 ?  456 GLU A CA  1 
ATOM   1789 C C   . GLU A 1 233 ? 1.069   19.538  -26.694 1.00 21.94 ?  456 GLU A C   1 
ATOM   1790 O O   . GLU A 1 233 ? 1.804   20.453  -26.302 1.00 20.11 ?  456 GLU A O   1 
ATOM   1791 C CB  . GLU A 1 233 ? 1.528   18.678  -29.009 1.00 19.75 ?  456 GLU A CB  1 
ATOM   1792 C CG  . GLU A 1 233 ? 2.484   17.868  -29.866 1.00 19.64 ?  456 GLU A CG  1 
ATOM   1793 C CD  . GLU A 1 233 ? 1.949   16.487  -30.192 1.00 21.57 ?  456 GLU A CD  1 
ATOM   1794 O OE1 . GLU A 1 233 ? 0.826   16.162  -29.749 1.00 19.06 ?  456 GLU A OE1 1 
ATOM   1795 O OE2 . GLU A 1 233 ? 2.654   15.726  -30.887 1.00 19.82 -1 456 GLU A OE2 1 
ATOM   1796 N N   . TRP A 1 234 ? -0.240  19.514  -26.429 1.00 21.60 ?  457 TRP A N   1 
ATOM   1797 C CA  . TRP A 1 234 ? -0.835  20.528  -25.563 1.00 21.29 ?  457 TRP A CA  1 
ATOM   1798 C C   . TRP A 1 234 ? -0.284  20.426  -24.147 1.00 21.02 ?  457 TRP A C   1 
ATOM   1799 O O   . TRP A 1 234 ? -0.065  21.446  -23.482 1.00 18.56 ?  457 TRP A O   1 
ATOM   1800 C CB  . TRP A 1 234 ? -2.358  20.390  -25.552 1.00 20.03 ?  457 TRP A CB  1 
ATOM   1801 C CG  . TRP A 1 234 ? -3.029  20.902  -26.788 1.00 21.58 ?  457 TRP A CG  1 
ATOM   1802 C CD1 . TRP A 1 234 ? -2.467  21.063  -28.021 1.00 20.83 ?  457 TRP A CD1 1 
ATOM   1803 C CD2 . TRP A 1 234 ? -4.396  21.312  -26.914 1.00 21.42 ?  457 TRP A CD2 1 
ATOM   1804 N NE1 . TRP A 1 234 ? -3.398  21.550  -28.906 1.00 22.94 ?  457 TRP A NE1 1 
ATOM   1805 C CE2 . TRP A 1 234 ? -4.591  21.711  -28.251 1.00 21.89 ?  457 TRP A CE2 1 
ATOM   1806 C CE3 . TRP A 1 234 ? -5.475  21.380  -26.027 1.00 23.44 ?  457 TRP A CE3 1 
ATOM   1807 C CZ2 . TRP A 1 234 ? -5.818  22.170  -28.721 1.00 21.73 ?  457 TRP A CZ2 1 
ATOM   1808 C CZ3 . TRP A 1 234 ? -6.693  21.839  -26.496 1.00 19.29 ?  457 TRP A CZ3 1 
ATOM   1809 C CH2 . TRP A 1 234 ? -6.854  22.230  -27.830 1.00 20.85 ?  457 TRP A CH2 1 
ATOM   1810 N N   . VAL A 1 235 ? -0.059  19.200  -23.668 1.00 20.04 ?  458 VAL A N   1 
ATOM   1811 C CA  . VAL A 1 235 ? 0.561   19.007  -22.360 1.00 20.08 ?  458 VAL A CA  1 
ATOM   1812 C C   . VAL A 1 235 ? 1.957   19.615  -22.342 1.00 21.25 ?  458 VAL A C   1 
ATOM   1813 O O   . VAL A 1 235 ? 2.352   20.278  -21.374 1.00 17.99 ?  458 VAL A O   1 
ATOM   1814 C CB  . VAL A 1 235 ? 0.588   17.509  -22.000 1.00 18.47 ?  458 VAL A CB  1 
ATOM   1815 C CG1 . VAL A 1 235 ? 1.506   17.255  -20.813 1.00 21.01 ?  458 VAL A CG1 1 
ATOM   1816 C CG2 . VAL A 1 235 ? -0.820  17.003  -21.714 1.00 20.97 ?  458 VAL A CG2 1 
ATOM   1817 N N   . GLN A 1 236 ? 2.722   19.410  -23.417 1.00 21.21 ?  459 GLN A N   1 
ATOM   1818 C CA  . GLN A 1 236 ? 4.070   19.963  -23.492 1.00 20.15 ?  459 GLN A CA  1 
ATOM   1819 C C   . GLN A 1 236 ? 4.042   21.486  -23.549 1.00 22.04 ?  459 GLN A C   1 
ATOM   1820 O O   . GLN A 1 236 ? 4.913   22.151  -22.976 1.00 23.28 ?  459 GLN A O   1 
ATOM   1821 C CB  . GLN A 1 236 ? 4.795   19.403  -24.715 1.00 20.48 ?  459 GLN A CB  1 
ATOM   1822 C CG  . GLN A 1 236 ? 5.455   18.055  -24.500 1.00 22.41 ?  459 GLN A CG  1 
ATOM   1823 C CD  . GLN A 1 236 ? 5.873   17.402  -25.804 1.00 23.61 ?  459 GLN A CD  1 
ATOM   1824 O OE1 . GLN A 1 236 ? 6.919   16.757  -25.882 1.00 21.84 ?  459 GLN A OE1 1 
ATOM   1825 N NE2 . GLN A 1 236 ? 5.055   17.568  -26.837 1.00 25.27 ?  459 GLN A NE2 1 
ATOM   1826 N N   . TYR A 1 237 ? 3.046   22.053  -24.231 1.00 21.33 ?  460 TYR A N   1 
ATOM   1827 C CA  . TYR A 1 237 ? 3.009   23.493  -24.461 1.00 20.15 ?  460 TYR A CA  1 
ATOM   1828 C C   . TYR A 1 237 ? 2.580   24.253  -23.211 1.00 21.08 ?  460 TYR A C   1 
ATOM   1829 O O   . TYR A 1 237 ? 3.191   25.266  -22.854 1.00 21.00 ?  460 TYR A O   1 
ATOM   1830 C CB  . TYR A 1 237 ? 2.071   23.803  -25.627 1.00 21.13 ?  460 TYR A CB  1 
ATOM   1831 C CG  . TYR A 1 237 ? 2.062   25.250  -26.063 1.00 23.84 ?  460 TYR A CG  1 
ATOM   1832 C CD1 . TYR A 1 237 ? 3.155   25.809  -26.712 1.00 23.56 ?  460 TYR A CD1 1 
ATOM   1833 C CD2 . TYR A 1 237 ? 0.954   26.056  -25.835 1.00 24.84 ?  460 TYR A CD2 1 
ATOM   1834 C CE1 . TYR A 1 237 ? 3.146   27.132  -27.118 1.00 25.40 ?  460 TYR A CE1 1 
ATOM   1835 C CE2 . TYR A 1 237 ? 0.935   27.376  -26.238 1.00 26.01 ?  460 TYR A CE2 1 
ATOM   1836 C CZ  . TYR A 1 237 ? 2.032   27.910  -26.878 1.00 25.56 ?  460 TYR A CZ  1 
ATOM   1837 O OH  . TYR A 1 237 ? 2.012   29.227  -27.277 1.00 29.70 ?  460 TYR A OH  1 
ATOM   1838 N N   . PHE A 1 238 ? 1.524   23.784  -22.540 1.00 21.27 ?  461 PHE A N   1 
ATOM   1839 C CA  . PHE A 1 238 ? 1.079   24.445  -21.316 1.00 23.60 ?  461 PHE A CA  1 
ATOM   1840 C C   . PHE A 1 238 ? 2.158   24.402  -20.243 1.00 23.83 ?  461 PHE A C   1 
ATOM   1841 O O   . PHE A 1 238 ? 2.362   25.383  -19.519 1.00 26.42 ?  461 PHE A O   1 
ATOM   1842 C CB  . PHE A 1 238 ? -0.206  23.800  -20.798 1.00 23.96 ?  461 PHE A CB  1 
ATOM   1843 C CG  . PHE A 1 238 ? -1.347  23.847  -21.770 1.00 25.26 ?  461 PHE A CG  1 
ATOM   1844 C CD1 . PHE A 1 238 ? -1.495  24.914  -22.642 1.00 22.94 ?  461 PHE A CD1 1 
ATOM   1845 C CD2 . PHE A 1 238 ? -2.284  22.829  -21.799 1.00 24.39 ?  461 PHE A CD2 1 
ATOM   1846 C CE1 . PHE A 1 238 ? -2.551  24.956  -23.533 1.00 23.66 ?  461 PHE A CE1 1 
ATOM   1847 C CE2 . PHE A 1 238 ? -3.341  22.865  -22.686 1.00 22.36 ?  461 PHE A CE2 1 
ATOM   1848 C CZ  . PHE A 1 238 ? -3.475  23.930  -23.554 1.00 23.80 ?  461 PHE A CZ  1 
ATOM   1849 N N   . TYR A 1 239 ? 2.857   23.270  -20.123 1.00 24.35 ?  462 TYR A N   1 
ATOM   1850 C CA  . TYR A 1 239 ? 3.931   23.173  -19.141 1.00 21.67 ?  462 TYR A CA  1 
ATOM   1851 C C   . TYR A 1 239 ? 5.036   24.178  -19.435 1.00 25.82 ?  462 TYR A C   1 
ATOM   1852 O O   . TYR A 1 239 ? 5.603   24.778  -18.514 1.00 25.16 ?  462 TYR A O   1 
ATOM   1853 C CB  . TYR A 1 239 ? 4.504   21.757  -19.114 1.00 22.18 ?  462 TYR A CB  1 
ATOM   1854 C CG  . TYR A 1 239 ? 5.839   21.697  -18.413 1.00 24.13 ?  462 TYR A CG  1 
ATOM   1855 C CD1 . TYR A 1 239 ? 5.912   21.746  -17.029 1.00 25.96 ?  462 TYR A CD1 1 
ATOM   1856 C CD2 . TYR A 1 239 ? 7.026   21.620  -19.131 1.00 22.52 ?  462 TYR A CD2 1 
ATOM   1857 C CE1 . TYR A 1 239 ? 7.123   21.706  -16.377 1.00 28.66 ?  462 TYR A CE1 1 
ATOM   1858 C CE2 . TYR A 1 239 ? 8.246   21.581  -18.486 1.00 27.78 ?  462 TYR A CE2 1 
ATOM   1859 C CZ  . TYR A 1 239 ? 8.286   21.624  -17.108 1.00 33.54 ?  462 TYR A CZ  1 
ATOM   1860 O OH  . TYR A 1 239 ? 9.491   21.585  -16.449 1.00 34.09 ?  462 TYR A OH  1 
ATOM   1861 N N   . GLN A 1 240 ? 5.361   24.369  -20.715 1.00 23.33 ?  463 GLN A N   1 
ATOM   1862 C CA  . GLN A 1 240 ? 6.422   25.300  -21.081 1.00 24.07 ?  463 GLN A CA  1 
ATOM   1863 C C   . GLN A 1 240 ? 6.000   26.740  -20.826 1.00 25.89 ?  463 GLN A C   1 
ATOM   1864 O O   . GLN A 1 240 ? 6.704   27.494  -20.145 1.00 26.67 ?  463 GLN A O   1 
ATOM   1865 C CB  . GLN A 1 240 ? 6.799   25.108  -22.548 1.00 22.98 ?  463 GLN A CB  1 
ATOM   1866 C CG  . GLN A 1 240 ? 7.666   23.899  -22.826 1.00 24.40 ?  463 GLN A CG  1 
ATOM   1867 C CD  . GLN A 1 240 ? 7.931   23.729  -24.305 1.00 27.35 ?  463 GLN A CD  1 
ATOM   1868 O OE1 . GLN A 1 240 ? 8.717   24.471  -24.889 1.00 28.61 ?  463 GLN A OE1 1 
ATOM   1869 N NE2 . GLN A 1 240 ? 7.273   22.754  -24.921 1.00 24.50 ?  463 GLN A NE2 1 
ATOM   1870 N N   . GLU A 1 241 ? 4.847   27.140  -21.368 1.00 28.46 ?  464 GLU A N   1 
ATOM   1871 C CA  . GLU A 1 241 ? 4.427   28.534  -21.273 1.00 30.62 ?  464 GLU A CA  1 
ATOM   1872 C C   . GLU A 1 241 ? 4.040   28.906  -19.847 1.00 30.05 ?  464 GLU A C   1 
ATOM   1873 O O   . GLU A 1 241 ? 4.432   29.970  -19.353 1.00 31.89 ?  464 GLU A O   1 
ATOM   1874 C CB  . GLU A 1 241 ? 3.266   28.794  -22.233 1.00 29.14 ?  464 GLU A CB  1 
ATOM   1875 C CG  . GLU A 1 241 ? 3.631   28.626  -23.701 1.00 27.30 ?  464 GLU A CG  1 
ATOM   1876 C CD  . GLU A 1 241 ? 4.689   29.612  -24.154 1.00 32.57 ?  464 GLU A CD  1 
ATOM   1877 O OE1 . GLU A 1 241 ? 4.545   30.817  -23.860 1.00 37.09 ?  464 GLU A OE1 1 
ATOM   1878 O OE2 . GLU A 1 241 ? 5.666   29.183  -24.804 1.00 37.62 -1 464 GLU A OE2 1 
ATOM   1879 N N   . ALA A 1 242 ? 3.277   28.042  -19.174 1.00 27.48 ?  465 ALA A N   1 
ATOM   1880 C CA  . ALA A 1 242 ? 2.808   28.291  -17.809 1.00 28.47 ?  465 ALA A CA  1 
ATOM   1881 C C   . ALA A 1 242 ? 2.095   29.637  -17.710 1.00 31.85 ?  465 ALA A C   1 
ATOM   1882 O O   . ALA A 1 242 ? 2.303   30.412  -16.773 1.00 36.36 ?  465 ALA A O   1 
ATOM   1883 C CB  . ALA A 1 242 ? 3.958   28.204  -16.804 1.00 29.72 ?  465 ALA A CB  1 
ATOM   1884 N N   . ALA A 1 243 ? 1.249   29.916  -18.691 1.00 30.24 ?  466 ALA A N   1 
ATOM   1885 C CA  . ALA A 1 243 ? 0.553   31.195  -18.746 1.00 33.07 ?  466 ALA A CA  1 
ATOM   1886 C C   . ALA A 1 243 ? -0.562  31.229  -17.707 1.00 32.18 ?  466 ALA A C   1 
ATOM   1887 O O   . ALA A 1 243 ? -1.351  30.282  -17.625 1.00 31.18 ?  466 ALA A O   1 
ATOM   1888 C CB  . ALA A 1 243 ? -0.017  31.433  -20.139 1.00 29.76 ?  466 ALA A CB  1 
ATOM   1889 N N   . PRO A 1 244 ? -0.660  32.290  -16.908 1.00 33.50 ?  467 PRO A N   1 
ATOM   1890 C CA  . PRO A 1 244 ? -1.690  32.337  -15.863 1.00 31.83 ?  467 PRO A CA  1 
ATOM   1891 C C   . PRO A 1 244 ? -3.091  32.321  -16.456 1.00 31.10 ?  467 PRO A C   1 
ATOM   1892 O O   . PRO A 1 244 ? -3.367  32.966  -17.470 1.00 32.47 ?  467 PRO A O   1 
ATOM   1893 C CB  . PRO A 1 244 ? -1.400  33.657  -15.138 1.00 33.21 ?  467 PRO A CB  1 
ATOM   1894 C CG  . PRO A 1 244 ? 0.021   33.985  -15.483 1.00 36.01 ?  467 PRO A CG  1 
ATOM   1895 C CD  . PRO A 1 244 ? 0.217   33.471  -16.875 1.00 35.97 ?  467 PRO A CD  1 
ATOM   1896 N N   . ALA A 1 245 ? -3.980  31.574  -15.805 1.00 29.92 ?  468 ALA A N   1 
ATOM   1897 C CA  . ALA A 1 245 ? -5.351  31.413  -16.276 1.00 30.26 ?  468 ALA A CA  1 
ATOM   1898 C C   . ALA A 1 245 ? -6.177  32.617  -15.839 1.00 31.12 ?  468 ALA A C   1 
ATOM   1899 O O   . ALA A 1 245 ? -6.501  32.761  -14.656 1.00 30.02 ?  468 ALA A O   1 
ATOM   1900 C CB  . ALA A 1 245 ? -5.947  30.115  -15.742 1.00 23.04 ?  468 ALA A CB  1 
ATOM   1901 N N   . GLN A 1 246 ? -6.526  33.481  -16.797 1.00 29.07 ?  469 GLN A N   1 
ATOM   1902 C CA  . GLN A 1 246 ? -7.314  34.666  -16.481 1.00 30.42 ?  469 GLN A CA  1 
ATOM   1903 C C   . GLN A 1 246 ? -8.720  34.322  -16.012 1.00 30.57 ?  469 GLN A C   1 
ATOM   1904 O O   . GLN A 1 246 ? -9.355  35.144  -15.344 1.00 33.31 ?  469 GLN A O   1 
ATOM   1905 C CB  . GLN A 1 246 ? -7.394  35.590  -17.697 1.00 29.77 ?  469 GLN A CB  1 
ATOM   1906 C CG  . GLN A 1 246 ? -6.117  36.364  -17.989 1.00 30.71 ?  469 GLN A CG  1 
ATOM   1907 C CD  . GLN A 1 246 ? -5.505  37.000  -16.752 1.00 41.09 ?  469 GLN A CD  1 
ATOM   1908 O OE1 . GLN A 1 246 ? -4.291  36.946  -16.555 1.00 40.98 ?  469 GLN A OE1 1 
ATOM   1909 N NE2 . GLN A 1 246 ? -6.337  37.632  -15.929 1.00 44.23 ?  469 GLN A NE2 1 
ATOM   1910 N N   . SER A 1 247 ? -9.220  33.137  -16.352 1.00 27.99 ?  470 SER A N   1 
ATOM   1911 C CA  . SER A 1 247 ? -10.539 32.700  -15.924 1.00 27.32 ?  470 SER A CA  1 
ATOM   1912 C C   . SER A 1 247 ? -10.543 31.180  -15.860 1.00 25.73 ?  470 SER A C   1 
ATOM   1913 O O   . SER A 1 247 ? -9.525  30.524  -16.101 1.00 27.77 ?  470 SER A O   1 
ATOM   1914 C CB  . SER A 1 247 ? -11.628 33.228  -16.863 1.00 30.08 ?  470 SER A CB  1 
ATOM   1915 O OG  . SER A 1 247 ? -11.767 32.395  -18.001 1.00 30.55 ?  470 SER A OG  1 
ATOM   1916 N N   . ASP A 1 248 ? -11.703 30.618  -15.530 1.00 27.06 ?  471 ASP A N   1 
ATOM   1917 C CA  . ASP A 1 248 ? -11.835 29.171  -15.449 1.00 25.46 ?  471 ASP A CA  1 
ATOM   1918 C C   . ASP A 1 248 ? -12.007 28.512  -16.810 1.00 26.55 ?  471 ASP A C   1 
ATOM   1919 O O   . ASP A 1 248 ? -11.875 27.287  -16.906 1.00 25.58 ?  471 ASP A O   1 
ATOM   1920 C CB  . ASP A 1 248 ? -13.021 28.799  -14.556 1.00 27.22 ?  471 ASP A CB  1 
ATOM   1921 C CG  . ASP A 1 248 ? -14.308 29.475  -14.987 1.00 35.50 ?  471 ASP A CG  1 
ATOM   1922 O OD1 . ASP A 1 248 ? -14.254 30.643  -15.426 1.00 34.01 -1 471 ASP A OD1 1 
ATOM   1923 O OD2 . ASP A 1 248 ? -15.376 28.837  -14.881 1.00 38.21 ?  471 ASP A OD2 1 
ATOM   1924 N N   . VAL A 1 249 ? -12.299 29.282  -17.858 1.00 25.50 ?  472 VAL A N   1 
ATOM   1925 C CA  . VAL A 1 249 ? -12.651 28.722  -19.159 1.00 23.35 ?  472 VAL A CA  1 
ATOM   1926 C C   . VAL A 1 249 ? -11.993 29.552  -20.254 1.00 26.39 ?  472 VAL A C   1 
ATOM   1927 O O   . VAL A 1 249 ? -12.200 30.769  -20.325 1.00 27.52 ?  472 VAL A O   1 
ATOM   1928 C CB  . VAL A 1 249 ? -14.173 28.679  -19.378 1.00 24.58 ?  472 VAL A CB  1 
ATOM   1929 C CG1 . VAL A 1 249 ? -14.480 28.186  -20.771 1.00 27.57 ?  472 VAL A CG1 1 
ATOM   1930 C CG2 . VAL A 1 249 ? -14.845 27.790  -18.342 1.00 26.16 ?  472 VAL A CG2 1 
ATOM   1931 N N   . ALA A 1 250 ? -11.217 28.898  -21.113 1.00 21.21 ?  473 ALA A N   1 
ATOM   1932 C CA  . ALA A 1 250 ? -10.689 29.512  -22.322 1.00 21.09 ?  473 ALA A CA  1 
ATOM   1933 C C   . ALA A 1 250 ? -11.553 29.097  -23.505 1.00 24.88 ?  473 ALA A C   1 
ATOM   1934 O O   . ALA A 1 250 ? -11.847 27.909  -23.677 1.00 24.67 ?  473 ALA A O   1 
ATOM   1935 C CB  . ALA A 1 250 ? -9.234  29.104  -22.560 1.00 21.78 ?  473 ALA A CB  1 
ATOM   1936 N N   . LEU A 1 251 ? -11.968 30.073  -24.308 1.00 24.10 ?  474 LEU A N   1 
ATOM   1937 C CA  . LEU A 1 251 ? -12.782 29.805  -25.487 1.00 23.68 ?  474 LEU A CA  1 
ATOM   1938 C C   . LEU A 1 251 ? -11.870 29.561  -26.682 1.00 24.10 ?  474 LEU A C   1 
ATOM   1939 O O   . LEU A 1 251 ? -11.076 30.434  -27.053 1.00 25.22 ?  474 LEU A O   1 
ATOM   1940 C CB  . LEU A 1 251 ? -13.737 30.961  -25.770 1.00 21.53 ?  474 LEU A CB  1 
ATOM   1941 C CG  . LEU A 1 251 ? -14.416 30.889  -27.140 1.00 24.73 ?  474 LEU A CG  1 
ATOM   1942 C CD1 . LEU A 1 251 ? -15.541 29.863  -27.132 1.00 26.63 ?  474 LEU A CD1 1 
ATOM   1943 C CD2 . LEU A 1 251 ? -14.931 32.254  -27.562 1.00 24.79 ?  474 LEU A CD2 1 
ATOM   1944 N N   . LEU A 1 252 ? -11.982 28.379  -27.279 1.00 21.79 ?  475 LEU A N   1 
ATOM   1945 C CA  . LEU A 1 252 ? -11.209 28.016  -28.455 1.00 22.45 ?  475 LEU A CA  1 
ATOM   1946 C C   . LEU A 1 252 ? -12.116 27.906  -29.673 1.00 23.34 ?  475 LEU A C   1 
ATOM   1947 O O   . LEU A 1 252 ? -13.331 27.723  -29.562 1.00 23.61 ?  475 LEU A O   1 
ATOM   1948 C CB  . LEU A 1 252 ? -10.463 26.693  -28.249 1.00 22.04 ?  475 LEU A CB  1 
ATOM   1949 C CG  . LEU A 1 252 ? -9.662  26.486  -26.964 1.00 21.18 ?  475 LEU A CG  1 
ATOM   1950 C CD1 . LEU A 1 252 ? -8.987  25.124  -26.991 1.00 19.23 ?  475 LEU A CD1 1 
ATOM   1951 C CD2 . LEU A 1 252 ? -8.637  27.592  -26.777 1.00 19.32 ?  475 LEU A CD2 1 
ATOM   1952 N N   . ARG A 1 253 ? -11.499 28.017  -30.845 1.00 22.07 ?  476 ARG A N   1 
ATOM   1953 C CA  . ARG A 1 253 ? -12.187 27.882  -32.119 1.00 22.23 ?  476 ARG A CA  1 
ATOM   1954 C C   . ARG A 1 253 ? -11.459 26.862  -32.981 1.00 24.39 ?  476 ARG A C   1 
ATOM   1955 O O   . ARG A 1 253 ? -10.227 26.863  -33.056 1.00 22.03 ?  476 ARG A O   1 
ATOM   1956 C CB  . ARG A 1 253 ? -12.278 29.231  -32.847 1.00 24.21 ?  476 ARG A CB  1 
ATOM   1957 C CG  . ARG A 1 253 ? -12.997 30.317  -32.057 1.00 26.89 ?  476 ARG A CG  1 
ATOM   1958 C CD  . ARG A 1 253 ? -14.490 30.285  -32.333 1.00 28.54 ?  476 ARG A CD  1 
ATOM   1959 N NE  . ARG A 1 253 ? -15.279 31.085  -31.401 1.00 28.44 ?  476 ARG A NE  1 
ATOM   1960 C CZ  . ARG A 1 253 ? -15.307 32.411  -31.362 1.00 25.57 ?  476 ARG A CZ  1 
ATOM   1961 N NH1 . ARG A 1 253 ? -14.554 33.144  -32.164 1.00 27.28 ?  476 ARG A NH1 1 
ATOM   1962 N NH2 . ARG A 1 253 ? -16.120 33.016  -30.501 1.00 27.29 ?  476 ARG A NH2 1 
ATOM   1963 N N   . PHE A 1 254 ? -12.227 25.988  -33.622 1.00 22.77 ?  477 PHE A N   1 
ATOM   1964 C CA  . PHE A 1 254 ? -11.683 24.965  -34.506 1.00 21.59 ?  477 PHE A CA  1 
ATOM   1965 C C   . PHE A 1 254 ? -11.692 25.501  -35.933 1.00 24.24 ?  477 PHE A C   1 
ATOM   1966 O O   . PHE A 1 254 ? -12.759 25.790  -36.486 1.00 25.40 ?  477 PHE A O   1 
ATOM   1967 C CB  . PHE A 1 254 ? -12.503 23.681  -34.396 1.00 21.50 ?  477 PHE A CB  1 
ATOM   1968 C CG  . PHE A 1 254 ? -11.833 22.471  -34.982 1.00 20.87 ?  477 PHE A CG  1 
ATOM   1969 C CD1 . PHE A 1 254 ? -10.696 21.935  -34.398 1.00 21.30 ?  477 PHE A CD1 1 
ATOM   1970 C CD2 . PHE A 1 254 ? -12.358 21.852  -36.105 1.00 22.42 ?  477 PHE A CD2 1 
ATOM   1971 C CE1 . PHE A 1 254 ? -10.089 20.813  -34.932 1.00 21.17 ?  477 PHE A CE1 1 
ATOM   1972 C CE2 . PHE A 1 254 ? -11.757 20.731  -36.642 1.00 22.03 ?  477 PHE A CE2 1 
ATOM   1973 C CZ  . PHE A 1 254 ? -10.623 20.210  -36.054 1.00 21.69 ?  477 PHE A CZ  1 
ATOM   1974 N N   . VAL A 1 255 ? -10.508 25.634  -36.526 1.00 25.93 ?  478 VAL A N   1 
ATOM   1975 C CA  . VAL A 1 255 ? -10.344 26.318  -37.803 1.00 23.75 ?  478 VAL A CA  1 
ATOM   1976 C C   . VAL A 1 255 ? -9.649  25.381  -38.780 1.00 25.55 ?  478 VAL A C   1 
ATOM   1977 O O   . VAL A 1 255 ? -8.558  24.874  -38.492 1.00 22.86 ?  478 VAL A O   1 
ATOM   1978 C CB  . VAL A 1 255 ? -9.544  27.624  -37.652 1.00 25.78 ?  478 VAL A CB  1 
ATOM   1979 C CG1 . VAL A 1 255 ? -9.389  28.308  -38.998 1.00 26.85 ?  478 VAL A CG1 1 
ATOM   1980 C CG2 . VAL A 1 255 ? -10.217 28.549  -36.647 1.00 25.85 ?  478 VAL A CG2 1 
ATOM   1981 N N   . ASN A 1 256 ? -10.273 25.158  -39.930 1.00 25.17 ?  479 ASN A N   1 
ATOM   1982 C CA  . ASN A 1 256 ? -9.616  24.442  -41.016 1.00 23.58 ?  479 ASN A CA  1 
ATOM   1983 C C   . ASN A 1 256 ? -8.536  25.337  -41.611 1.00 24.99 ?  479 ASN A C   1 
ATOM   1984 O O   . ASN A 1 256 ? -8.844  26.453  -42.049 1.00 27.53 ?  479 ASN A O   1 
ATOM   1985 C CB  . ASN A 1 256 ? -10.630 24.037  -42.082 1.00 23.43 ?  479 ASN A CB  1 
ATOM   1986 C CG  . ASN A 1 256 ? -9.977  23.436  -43.310 1.00 24.48 ?  479 ASN A CG  1 
ATOM   1987 O OD1 . ASN A 1 256 ? -9.842  24.096  -44.341 1.00 24.93 ?  479 ASN A OD1 1 
ATOM   1988 N ND2 . ASN A 1 256 ? -9.567  22.177  -43.207 1.00 19.99 ?  479 ASN A ND2 1 
ATOM   1989 N N   . PRO A 1 257 ? -7.274  24.903  -41.650 1.00 24.08 ?  480 PRO A N   1 
ATOM   1990 C CA  . PRO A 1 257 ? -6.196  25.823  -42.049 1.00 28.86 ?  480 PRO A CA  1 
ATOM   1991 C C   . PRO A 1 257 ? -6.165  26.142  -43.535 1.00 29.51 ?  480 PRO A C   1 
ATOM   1992 O O   . PRO A 1 257 ? -5.583  27.167  -43.912 1.00 32.92 ?  480 PRO A O   1 
ATOM   1993 C CB  . PRO A 1 257 ? -4.929  25.078  -41.612 1.00 24.30 ?  480 PRO A CB  1 
ATOM   1994 C CG  . PRO A 1 257 ? -5.309  23.638  -41.722 1.00 19.68 ?  480 PRO A CG  1 
ATOM   1995 C CD  . PRO A 1 257 ? -6.758  23.568  -41.300 1.00 24.35 ?  480 PRO A CD  1 
ATOM   1996 N N   . ASP A 1 258 ? -6.762  25.309  -44.389 1.00 28.25 ?  481 ASP A N   1 
ATOM   1997 C CA  . ASP A 1 258 ? -6.729  25.582  -45.823 1.00 32.81 ?  481 ASP A CA  1 
ATOM   1998 C C   . ASP A 1 258 ? -7.832  26.548  -46.238 1.00 31.41 ?  481 ASP A C   1 
ATOM   1999 O O   . ASP A 1 258 ? -7.608  27.422  -47.084 1.00 34.44 ?  481 ASP A O   1 
ATOM   2000 C CB  . ASP A 1 258 ? -6.836  24.277  -46.612 1.00 31.36 ?  481 ASP A CB  1 
ATOM   2001 C CG  . ASP A 1 258 ? -5.509  23.556  -46.720 1.00 35.63 ?  481 ASP A CG  1 
ATOM   2002 O OD1 . ASP A 1 258 ? -4.576  23.930  -45.980 1.00 41.72 ?  481 ASP A OD1 1 
ATOM   2003 O OD2 . ASP A 1 258 ? -5.393  22.628  -47.548 1.00 37.22 -1 481 ASP A OD2 1 
ATOM   2004 N N   . THR A 1 259 ? -9.022  26.410  -45.657 1.00 29.79 ?  482 THR A N   1 
ATOM   2005 C CA  . THR A 1 259 ? -10.132 27.298  -45.971 1.00 26.96 ?  482 THR A CA  1 
ATOM   2006 C C   . THR A 1 259 ? -10.213 28.503  -45.045 1.00 29.70 ?  482 THR A C   1 
ATOM   2007 O O   . THR A 1 259 ? -10.843 29.503  -45.407 1.00 31.51 ?  482 THR A O   1 
ATOM   2008 C CB  . THR A 1 259 ? -11.461 26.537  -45.899 1.00 28.56 ?  482 THR A CB  1 
ATOM   2009 O OG1 . THR A 1 259 ? -11.648 26.026  -44.572 1.00 28.42 ?  482 THR A OG1 1 
ATOM   2010 C CG2 . THR A 1 259 ? -11.472 25.384  -46.887 1.00 25.90 ?  482 THR A CG2 1 
ATOM   2011 N N   . GLY A 1 260 ? -9.593  28.435  -43.869 1.00 29.40 ?  483 GLY A N   1 
ATOM   2012 C CA  . GLY A 1 260 ? -9.809  29.438  -42.850 1.00 26.78 ?  483 GLY A CA  1 
ATOM   2013 C C   . GLY A 1 260 ? -11.182 29.406  -42.221 1.00 29.15 ?  483 GLY A C   1 
ATOM   2014 O O   . GLY A 1 260 ? -11.479 30.260  -41.377 1.00 31.70 ?  483 GLY A O   1 
ATOM   2015 N N   . ARG A 1 261 ? -12.026 28.451  -42.603 1.00 26.98 ?  484 ARG A N   1 
ATOM   2016 C CA  . ARG A 1 261 ? -13.373 28.366  -42.062 1.00 27.08 ?  484 ARG A CA  1 
ATOM   2017 C C   . ARG A 1 261 ? -13.343 27.949  -40.599 1.00 28.72 ?  484 ARG A C   1 
ATOM   2018 O O   . ARG A 1 261 ? -12.576 27.067  -40.201 1.00 26.91 ?  484 ARG A O   1 
ATOM   2019 C CB  . ARG A 1 261 ? -14.205 27.367  -42.867 1.00 30.00 ?  484 ARG A CB  1 
ATOM   2020 C CG  . ARG A 1 261 ? -15.658 27.766  -43.051 1.00 40.45 ?  484 ARG A CG  1 
ATOM   2021 C CD  . ARG A 1 261 ? -16.410 26.733  -43.872 1.00 41.31 ?  484 ARG A CD  1 
ATOM   2022 N NE  . ARG A 1 261 ? -17.489 27.338  -44.643 1.00 48.64 ?  484 ARG A NE  1 
ATOM   2023 C CZ  . ARG A 1 261 ? -17.351 27.817  -45.871 1.00 58.11 ?  484 ARG A CZ  1 
ATOM   2024 N NH1 . ARG A 1 261 ? -16.193 27.760  -46.508 1.00 55.02 ?  484 ARG A NH1 1 
ATOM   2025 N NH2 . ARG A 1 261 ? -18.401 28.364  -46.476 1.00 61.32 ?  484 ARG A NH2 1 
ATOM   2026 N N   . VAL A 1 262 ? -14.180 28.599  -39.798 1.00 28.17 ?  485 VAL A N   1 
ATOM   2027 C CA  . VAL A 1 262 ? -14.407 28.199  -38.415 1.00 28.51 ?  485 VAL A CA  1 
ATOM   2028 C C   . VAL A 1 262 ? -15.480 27.120  -38.420 1.00 27.25 ?  485 VAL A C   1 
ATOM   2029 O O   . VAL A 1 262 ? -16.581 27.332  -38.939 1.00 27.79 ?  485 VAL A O   1 
ATOM   2030 C CB  . VAL A 1 262 ? -14.827 29.394  -37.548 1.00 29.50 ?  485 VAL A CB  1 
ATOM   2031 C CG1 . VAL A 1 262 ? -14.984 28.969  -36.095 1.00 26.20 ?  485 VAL A CG1 1 
ATOM   2032 C CG2 . VAL A 1 262 ? -13.813 30.521  -37.673 1.00 28.40 ?  485 VAL A CG2 1 
ATOM   2033 N N   . LEU A 1 263 ? -15.158 25.957  -37.855 1.00 24.47 ?  486 LEU A N   1 
ATOM   2034 C CA  . LEU A 1 263 ? -16.059 24.815  -37.918 1.00 23.61 ?  486 LEU A CA  1 
ATOM   2035 C C   . LEU A 1 263 ? -16.837 24.568  -36.632 1.00 24.46 ?  486 LEU A C   1 
ATOM   2036 O O   . LEU A 1 263 ? -17.962 24.063  -36.707 1.00 18.95 ?  486 LEU A O   1 
ATOM   2037 C CB  . LEU A 1 263 ? -15.288 23.548  -38.310 1.00 23.77 ?  486 LEU A CB  1 
ATOM   2038 C CG  . LEU A 1 263 ? -14.552 23.650  -39.650 1.00 24.75 ?  486 LEU A CG  1 
ATOM   2039 C CD1 . LEU A 1 263 ? -13.241 22.881  -39.612 1.00 24.45 ?  486 LEU A CD1 1 
ATOM   2040 C CD2 . LEU A 1 263 ? -15.433 23.174  -40.801 1.00 24.19 ?  486 LEU A CD2 1 
ATOM   2041 N N   . PHE A 1 264 ? -16.294 24.904  -35.461 1.00 22.91 ?  487 PHE A N   1 
ATOM   2042 C CA  . PHE A 1 264 ? -17.094 24.864  -34.236 1.00 23.01 ?  487 PHE A CA  1 
ATOM   2043 C C   . PHE A 1 264 ? -16.388 25.635  -33.123 1.00 23.61 ?  487 PHE A C   1 
ATOM   2044 O O   . PHE A 1 264 ? -15.282 26.158  -33.293 1.00 22.67 ?  487 PHE A O   1 
ATOM   2045 C CB  . PHE A 1 264 ? -17.417 23.428  -33.795 1.00 23.99 ?  487 PHE A CB  1 
ATOM   2046 C CG  . PHE A 1 264 ? -16.231 22.632  -33.313 1.00 24.67 ?  487 PHE A CG  1 
ATOM   2047 C CD1 . PHE A 1 264 ? -15.798 22.721  -31.997 1.00 23.18 ?  487 PHE A CD1 1 
ATOM   2048 C CD2 . PHE A 1 264 ? -15.593 21.742  -34.160 1.00 22.17 ?  487 PHE A CD2 1 
ATOM   2049 C CE1 . PHE A 1 264 ? -14.725 21.972  -31.551 1.00 24.07 ?  487 PHE A CE1 1 
ATOM   2050 C CE2 . PHE A 1 264 ? -14.525 20.985  -33.716 1.00 23.52 ?  487 PHE A CE2 1 
ATOM   2051 C CZ  . PHE A 1 264 ? -14.088 21.103  -32.412 1.00 22.31 ?  487 PHE A CZ  1 
ATOM   2052 N N   . GLU A 1 265 ? -17.061 25.693  -31.972 1.00 25.87 ?  488 GLU A N   1 
ATOM   2053 C CA  . GLU A 1 265 ? -16.622 26.388  -30.771 1.00 23.55 ?  488 GLU A CA  1 
ATOM   2054 C C   . GLU A 1 265 ? -16.471 25.380  -29.639 1.00 21.77 ?  488 GLU A C   1 
ATOM   2055 O O   . GLU A 1 265 ? -17.150 24.350  -29.619 1.00 23.48 ?  488 GLU A O   1 
ATOM   2056 C CB  . GLU A 1 265 ? -17.643 27.456  -30.355 1.00 25.98 ?  488 GLU A CB  1 
ATOM   2057 C CG  . GLU A 1 265 ? -17.360 28.859  -30.839 1.00 27.43 ?  488 GLU A CG  1 
ATOM   2058 C CD  . GLU A 1 265 ? -18.297 29.882  -30.222 1.00 28.19 ?  488 GLU A CD  1 
ATOM   2059 O OE1 . GLU A 1 265 ? -19.403 29.487  -29.795 1.00 24.97 ?  488 GLU A OE1 1 
ATOM   2060 O OE2 . GLU A 1 265 ? -17.929 31.075  -30.155 1.00 32.50 -1 488 GLU A OE2 1 
ATOM   2061 N N   . CYS A 1 266 ? -15.600 25.684  -28.678 1.00 24.42 ?  489 CYS A N   1 
ATOM   2062 C CA  . CYS A 1 266 ? -15.459 24.807  -27.522 1.00 23.20 ?  489 CYS A CA  1 
ATOM   2063 C C   . CYS A 1 266 ? -14.836 25.575  -26.365 1.00 25.23 ?  489 CYS A C   1 
ATOM   2064 O O   . CYS A 1 266 ? -14.273 26.659  -26.535 1.00 23.69 ?  489 CYS A O   1 
ATOM   2065 C CB  . CYS A 1 266 ? -14.631 23.561  -27.857 1.00 20.60 ?  489 CYS A CB  1 
ATOM   2066 S SG  . CYS A 1 266 ? -12.878 23.862  -28.152 1.00 23.65 ?  489 CYS A SG  1 
ATOM   2067 N N   . LYS A 1 267 ? -14.946 24.982  -25.178 1.00 25.06 ?  490 LYS A N   1 
ATOM   2068 C CA  . LYS A 1 267 ? -14.442 25.548  -23.934 1.00 23.79 ?  490 LYS A CA  1 
ATOM   2069 C C   . LYS A 1 267 ? -13.278 24.707  -23.428 1.00 24.11 ?  490 LYS A C   1 
ATOM   2070 O O   . LYS A 1 267 ? -13.441 23.509  -23.175 1.00 23.21 ?  490 LYS A O   1 
ATOM   2071 C CB  . LYS A 1 267 ? -15.535 25.591  -22.868 1.00 24.56 ?  490 LYS A CB  1 
ATOM   2072 C CG  . LYS A 1 267 ? -16.714 26.491  -23.153 1.00 25.12 ?  490 LYS A CG  1 
ATOM   2073 C CD  . LYS A 1 267 ? -17.891 26.049  -22.301 1.00 29.55 ?  490 LYS A CD  1 
ATOM   2074 C CE  . LYS A 1 267 ? -18.705 27.226  -21.814 1.00 27.91 ?  490 LYS A CE  1 
ATOM   2075 N NZ  . LYS A 1 267 ? -19.611 26.836  -20.695 1.00 29.54 ?  490 LYS A NZ  1 
ATOM   2076 N N   . LEU A 1 268 ? -12.118 25.335  -23.265 1.00 18.84 ?  491 LEU A N   1 
ATOM   2077 C CA  . LEU A 1 268 ? -10.994 24.711  -22.579 1.00 23.24 ?  491 LEU A CA  1 
ATOM   2078 C C   . LEU A 1 268 ? -11.057 25.103  -21.108 1.00 24.08 ?  491 LEU A C   1 
ATOM   2079 O O   . LEU A 1 268 ? -11.016 26.293  -20.775 1.00 23.78 ?  491 LEU A O   1 
ATOM   2080 C CB  . LEU A 1 268 ? -9.666  25.139  -23.203 1.00 22.42 ?  491 LEU A CB  1 
ATOM   2081 C CG  . LEU A 1 268 ? -8.367  24.592  -22.602 1.00 22.45 ?  491 LEU A CG  1 
ATOM   2082 C CD1 . LEU A 1 268 ? -8.481  23.110  -22.270 1.00 20.52 ?  491 LEU A CD1 1 
ATOM   2083 C CD2 . LEU A 1 268 ? -7.200  24.840  -23.547 1.00 23.02 ?  491 LEU A CD2 1 
ATOM   2084 N N   . HIS A 1 269 ? -11.171 24.110  -20.233 1.00 21.00 ?  492 HIS A N   1 
ATOM   2085 C CA  . HIS A 1 269 ? -11.273 24.364  -18.805 1.00 25.59 ?  492 HIS A CA  1 
ATOM   2086 C C   . HIS A 1 269 ? -9.888  24.414  -18.173 1.00 22.96 ?  492 HIS A C   1 
ATOM   2087 O O   . HIS A 1 269 ? -8.964  23.715  -18.598 1.00 20.38 ?  492 HIS A O   1 
ATOM   2088 C CB  . HIS A 1 269 ? -12.133 23.297  -18.127 1.00 23.23 ?  492 HIS A CB  1 
ATOM   2089 C CG  . HIS A 1 269 ? -13.544 23.257  -18.626 1.00 24.81 ?  492 HIS A CG  1 
ATOM   2090 N ND1 . HIS A 1 269 ? -14.573 23.933  -18.006 1.00 25.19 ?  492 HIS A ND1 1 
ATOM   2091 C CD2 . HIS A 1 269 ? -14.097 22.628  -19.690 1.00 26.86 ?  492 HIS A CD2 1 
ATOM   2092 C CE1 . HIS A 1 269 ? -15.698 23.720  -18.664 1.00 24.39 ?  492 HIS A CE1 1 
ATOM   2093 N NE2 . HIS A 1 269 ? -15.437 22.930  -19.690 1.00 26.67 ?  492 HIS A NE2 1 
ATOM   2094 N N   . LYS A 1 270 ? -9.758  25.261  -17.145 1.00 22.84 ?  493 LYS A N   1 
ATOM   2095 C CA  . LYS A 1 270 ? -8.464  25.487  -16.508 1.00 23.54 ?  493 LYS A CA  1 
ATOM   2096 C C   . LYS A 1 270 ? -7.822  24.184  -16.049 1.00 22.81 ?  493 LYS A C   1 
ATOM   2097 O O   . LYS A 1 270 ? -6.598  24.023  -16.129 1.00 21.16 ?  493 LYS A O   1 
ATOM   2098 C CB  . LYS A 1 270 ? -8.626  26.442  -15.324 1.00 25.67 ?  493 LYS A CB  1 
ATOM   2099 C CG  . LYS A 1 270 ? -7.311  26.956  -14.763 1.00 27.21 ?  493 LYS A CG  1 
ATOM   2100 C CD  . LYS A 1 270 ? -7.485  27.534  -13.366 1.00 27.78 ?  493 LYS A CD  1 
ATOM   2101 C CE  . LYS A 1 270 ? -6.325  27.144  -12.460 1.00 33.14 ?  493 LYS A CE  1 
ATOM   2102 N NZ  . LYS A 1 270 ? -6.338  27.900  -11.177 1.00 38.51 ?  493 LYS A NZ  1 
ATOM   2103 N N   . SER A 1 271 ? -8.630  23.239  -15.575 1.00 21.11 ?  494 SER A N   1 
ATOM   2104 C CA  . SER A 1 271 ? -8.119  21.967  -15.081 1.00 22.49 ?  494 SER A CA  1 
ATOM   2105 C C   . SER A 1 271 ? -7.749  20.992  -16.194 1.00 22.95 ?  494 SER A C   1 
ATOM   2106 O O   . SER A 1 271 ? -7.290  19.885  -15.893 1.00 23.64 ?  494 SER A O   1 
ATOM   2107 C CB  . SER A 1 271 ? -9.144  21.326  -14.142 1.00 20.31 ?  494 SER A CB  1 
ATOM   2108 O OG  . SER A 1 271 ? -10.448 21.396  -14.688 1.00 21.18 ?  494 SER A OG  1 
ATOM   2109 N N   . GLY A 1 272 ? -7.943  21.361  -17.458 1.00 20.65 ?  495 GLY A N   1 
ATOM   2110 C CA  . GLY A 1 272 ? -7.407  20.581  -18.557 1.00 20.80 ?  495 GLY A CA  1 
ATOM   2111 C C   . GLY A 1 272 ? -8.346  19.578  -19.197 1.00 19.76 ?  495 GLY A C   1 
ATOM   2112 O O   . GLY A 1 272 ? -8.026  18.388  -19.273 1.00 19.48 ?  495 GLY A O   1 
ATOM   2113 N N   . TYR A 1 273 ? -9.500  20.042  -19.667 1.00 19.08 ?  496 TYR A N   1 
ATOM   2114 C CA  . TYR A 1 273 ? -10.389 19.217  -20.476 1.00 20.92 ?  496 TYR A CA  1 
ATOM   2115 C C   . TYR A 1 273 ? -11.313 20.142  -21.255 1.00 22.57 ?  496 TYR A C   1 
ATOM   2116 O O   . TYR A 1 273 ? -11.414 21.337  -20.967 1.00 23.33 ?  496 TYR A O   1 
ATOM   2117 C CB  . TYR A 1 273 ? -11.177 18.214  -19.623 1.00 21.12 ?  496 TYR A CB  1 
ATOM   2118 C CG  . TYR A 1 273 ? -12.182 18.831  -18.682 1.00 23.39 ?  496 TYR A CG  1 
ATOM   2119 C CD1 . TYR A 1 273 ? -11.777 19.440  -17.501 1.00 19.52 ?  496 TYR A CD1 1 
ATOM   2120 C CD2 . TYR A 1 273 ? -13.540 18.795  -18.970 1.00 23.33 ?  496 TYR A CD2 1 
ATOM   2121 C CE1 . TYR A 1 273 ? -12.696 20.001  -16.637 1.00 18.65 ?  496 TYR A CE1 1 
ATOM   2122 C CE2 . TYR A 1 273 ? -14.466 19.353  -18.112 1.00 25.03 ?  496 TYR A CE2 1 
ATOM   2123 C CZ  . TYR A 1 273 ? -14.039 19.955  -16.947 1.00 23.16 ?  496 TYR A CZ  1 
ATOM   2124 O OH  . TYR A 1 273 ? -14.957 20.514  -16.089 1.00 22.42 ?  496 TYR A OH  1 
ATOM   2125 N N   . VAL A 1 274 ? -11.984 19.575  -22.256 1.00 20.44 ?  497 VAL A N   1 
ATOM   2126 C CA  . VAL A 1 274 ? -12.732 20.351  -23.238 1.00 22.18 ?  497 VAL A CA  1 
ATOM   2127 C C   . VAL A 1 274 ? -14.175 19.868  -23.281 1.00 21.88 ?  497 VAL A C   1 
ATOM   2128 O O   . VAL A 1 274 ? -14.438 18.660  -23.282 1.00 23.56 ?  497 VAL A O   1 
ATOM   2129 C CB  . VAL A 1 274 ? -12.088 20.256  -24.638 1.00 22.58 ?  497 VAL A CB  1 
ATOM   2130 C CG1 . VAL A 1 274 ? -12.886 21.059  -25.653 1.00 20.04 ?  497 VAL A CG1 1 
ATOM   2131 C CG2 . VAL A 1 274 ? -10.643 20.729  -24.591 1.00 22.38 ?  497 VAL A CG2 1 
ATOM   2132 N N   . THR A 1 275 ? -15.108 20.817  -23.320 1.00 20.87 ?  498 THR A N   1 
ATOM   2133 C CA  . THR A 1 275 ? -16.521 20.538  -23.516 1.00 21.91 ?  498 THR A CA  1 
ATOM   2134 C C   . THR A 1 275 ? -17.021 21.268  -24.756 1.00 22.00 ?  498 THR A C   1 
ATOM   2135 O O   . THR A 1 275 ? -16.527 22.345  -25.104 1.00 23.35 ?  498 THR A O   1 
ATOM   2136 C CB  . THR A 1 275 ? -17.360 20.958  -22.299 1.00 21.41 ?  498 THR A CB  1 
ATOM   2137 O OG1 . THR A 1 275 ? -17.199 22.363  -22.066 1.00 22.19 ?  498 THR A OG1 1 
ATOM   2138 C CG2 . THR A 1 275 ? -16.929 20.189  -21.060 1.00 21.55 ?  498 THR A CG2 1 
ATOM   2139 N N   . VAL A 1 276 ? -18.004 20.665  -25.425 1.00 20.78 ?  499 VAL A N   1 
ATOM   2140 C CA  . VAL A 1 276 ? -18.637 21.251  -26.598 1.00 22.36 ?  499 VAL A CA  1 
ATOM   2141 C C   . VAL A 1 276 ? -20.146 21.204  -26.405 1.00 21.32 ?  499 VAL A C   1 
ATOM   2142 O O   . VAL A 1 276 ? -20.668 20.470  -25.564 1.00 20.41 ?  499 VAL A O   1 
ATOM   2143 C CB  . VAL A 1 276 ? -18.245 20.532  -27.908 1.00 21.31 ?  499 VAL A CB  1 
ATOM   2144 C CG1 . VAL A 1 276 ? -16.771 20.735  -28.212 1.00 20.85 ?  499 VAL A CG1 1 
ATOM   2145 C CG2 . VAL A 1 276 ? -18.584 19.050  -27.828 1.00 24.34 ?  499 VAL A CG2 1 
ATOM   2146 N N   . ALA A 1 277 ? -20.848 22.007  -27.205 1.00 21.29 ?  500 ALA A N   1 
ATOM   2147 C CA  . ALA A 1 277 ? -22.310 22.011  -27.204 1.00 25.43 ?  500 ALA A CA  1 
ATOM   2148 C C   . ALA A 1 277 ? -22.792 20.900  -28.132 1.00 22.83 ?  500 ALA A C   1 
ATOM   2149 O O   . ALA A 1 277 ? -23.125 21.112  -29.300 1.00 27.09 ?  500 ALA A O   1 
ATOM   2150 C CB  . ALA A 1 277 ? -22.848 23.375  -27.619 1.00 24.36 ?  500 ALA A CB  1 
ATOM   2151 N N   . HIS A 1 278 ? -22.808 19.681  -27.594 1.00 22.54 ?  501 HIS A N   1 
ATOM   2152 C CA  . HIS A 1 278 ? -23.345 18.520  -28.288 1.00 22.42 ?  501 HIS A CA  1 
ATOM   2153 C C   . HIS A 1 278 ? -24.281 17.779  -27.347 1.00 23.07 ?  501 HIS A C   1 
ATOM   2154 O O   . HIS A 1 278 ? -23.997 17.645  -26.153 1.00 25.93 ?  501 HIS A O   1 
ATOM   2155 C CB  . HIS A 1 278 ? -22.234 17.586  -28.784 1.00 23.56 ?  501 HIS A CB  1 
ATOM   2156 C CG  . HIS A 1 278 ? -22.742 16.367  -29.491 1.00 24.98 ?  501 HIS A CG  1 
ATOM   2157 N ND1 . HIS A 1 278 ? -22.832 15.135  -28.879 1.00 27.07 ?  501 HIS A ND1 1 
ATOM   2158 C CD2 . HIS A 1 278 ? -23.199 16.194  -30.754 1.00 23.84 ?  501 HIS A CD2 1 
ATOM   2159 C CE1 . HIS A 1 278 ? -23.316 14.255  -29.737 1.00 25.15 ?  501 HIS A CE1 1 
ATOM   2160 N NE2 . HIS A 1 278 ? -23.548 14.872  -30.882 1.00 21.98 ?  501 HIS A NE2 1 
ATOM   2161 N N   . THR A 1 279 ? -25.392 17.294  -27.891 1.00 25.04 ?  502 THR A N   1 
ATOM   2162 C CA  . THR A 1 279 ? -26.509 16.813  -27.095 1.00 22.57 ?  502 THR A CA  1 
ATOM   2163 C C   . THR A 1 279 ? -26.978 15.470  -27.642 1.00 22.57 ?  502 THR A C   1 
ATOM   2164 O O   . THR A 1 279 ? -26.756 15.141  -28.810 1.00 25.88 ?  502 THR A O   1 
ATOM   2165 C CB  . THR A 1 279 ? -27.649 17.854  -27.102 1.00 25.58 ?  502 THR A CB  1 
ATOM   2166 O OG1 . THR A 1 279 ? -27.262 18.987  -26.315 1.00 32.29 ?  502 THR A OG1 1 
ATOM   2167 C CG2 . THR A 1 279 ? -28.943 17.289  -26.538 1.00 24.01 ?  502 THR A CG2 1 
ATOM   2168 N N   . GLY A 1 280 ? -27.602 14.679  -26.780 1.00 22.60 ?  503 GLY A N   1 
ATOM   2169 C CA  . GLY A 1 280 ? -28.241 13.455  -27.208 1.00 25.18 ?  503 GLY A CA  1 
ATOM   2170 C C   . GLY A 1 280 ? -27.434 12.232  -26.838 1.00 25.15 ?  503 GLY A C   1 
ATOM   2171 O O   . GLY A 1 280 ? -26.395 12.296  -26.174 1.00 24.15 ?  503 GLY A O   1 
ATOM   2172 N N   . GLN A 1 281 ? -27.933 11.087  -27.295 1.00 25.16 ?  504 GLN A N   1 
ATOM   2173 C CA  . GLN A 1 281 ? -27.339 9.807   -26.944 1.00 25.17 ?  504 GLN A CA  1 
ATOM   2174 C C   . GLN A 1 281 ? -26.432 9.237   -28.026 1.00 24.90 ?  504 GLN A C   1 
ATOM   2175 O O   . GLN A 1 281 ? -25.717 8.268   -27.754 1.00 27.83 ?  504 GLN A O   1 
ATOM   2176 C CB  . GLN A 1 281 ? -28.436 8.790   -26.607 1.00 25.08 ?  504 GLN A CB  1 
ATOM   2177 C CG  . GLN A 1 281 ? -28.935 8.885   -25.173 1.00 26.82 ?  504 GLN A CG  1 
ATOM   2178 C CD  . GLN A 1 281 ? -27.803 8.948   -24.161 1.00 35.58 ?  504 GLN A CD  1 
ATOM   2179 O OE1 . GLN A 1 281 ? -27.764 9.842   -23.315 1.00 34.33 ?  504 GLN A OE1 1 
ATOM   2180 N NE2 . GLN A 1 281 ? -26.882 7.994   -24.238 1.00 32.95 ?  504 GLN A NE2 1 
ATOM   2181 N N   . HIS A 1 282 ? -26.430 9.801   -29.232 1.00 26.46 ?  505 HIS A N   1 
ATOM   2182 C CA  . HIS A 1 282 ? -25.516 9.321   -30.258 1.00 28.67 ?  505 HIS A CA  1 
ATOM   2183 C C   . HIS A 1 282 ? -24.171 10.034  -30.159 1.00 26.30 ?  505 HIS A C   1 
ATOM   2184 O O   . HIS A 1 282 ? -24.011 11.037  -29.459 1.00 25.56 ?  505 HIS A O   1 
ATOM   2185 C CB  . HIS A 1 282 ? -26.086 9.519   -31.662 1.00 29.24 ?  505 HIS A CB  1 
ATOM   2186 C CG  . HIS A 1 282 ? -27.463 8.970   -31.856 1.00 31.48 ?  505 HIS A CG  1 
ATOM   2187 N ND1 . HIS A 1 282 ? -28.592 9.606   -31.385 1.00 30.69 ?  505 HIS A ND1 1 
ATOM   2188 C CD2 . HIS A 1 282 ? -27.898 7.863   -32.503 1.00 30.58 ?  505 HIS A CD2 1 
ATOM   2189 C CE1 . HIS A 1 282 ? -29.660 8.905   -31.718 1.00 32.29 ?  505 HIS A CE1 1 
ATOM   2190 N NE2 . HIS A 1 282 ? -29.267 7.842   -32.397 1.00 36.79 ?  505 HIS A NE2 1 
ATOM   2191 N N   . ASP A 1 283 ? -23.203 9.509   -30.899 1.00 25.59 ?  506 ASP A N   1 
ATOM   2192 C CA  . ASP A 1 283 ? -21.850 10.037  -30.935 1.00 22.05 ?  506 ASP A CA  1 
ATOM   2193 C C   . ASP A 1 283 ? -21.641 10.868  -32.194 1.00 23.03 ?  506 ASP A C   1 
ATOM   2194 O O   . ASP A 1 283 ? -22.279 10.638  -33.225 1.00 20.92 ?  506 ASP A O   1 
ATOM   2195 C CB  . ASP A 1 283 ? -20.832 8.898   -30.899 1.00 23.46 ?  506 ASP A CB  1 
ATOM   2196 C CG  . ASP A 1 283 ? -20.968 8.033   -29.663 1.00 29.82 ?  506 ASP A CG  1 
ATOM   2197 O OD1 . ASP A 1 283 ? -21.413 8.551   -28.617 1.00 34.23 ?  506 ASP A OD1 1 
ATOM   2198 O OD2 . ASP A 1 283 ? -20.612 6.837   -29.733 1.00 32.57 -1 506 ASP A OD2 1 
ATOM   2199 N N   . LEU A 1 284 ? -20.734 11.838  -32.102 1.00 20.38 ?  507 LEU A N   1 
ATOM   2200 C CA  . LEU A 1 284 ? -20.343 12.658  -33.242 1.00 19.88 ?  507 LEU A CA  1 
ATOM   2201 C C   . LEU A 1 284 ? -18.833 12.574  -33.405 1.00 22.48 ?  507 LEU A C   1 
ATOM   2202 O O   . LEU A 1 284 ? -18.085 12.886  -32.472 1.00 18.89 ?  507 LEU A O   1 
ATOM   2203 C CB  . LEU A 1 284 ? -20.794 14.109  -33.067 1.00 19.15 ?  507 LEU A CB  1 
ATOM   2204 C CG  . LEU A 1 284 ? -20.542 15.017  -34.272 1.00 19.43 ?  507 LEU A CG  1 
ATOM   2205 C CD1 . LEU A 1 284 ? -21.426 14.613  -35.438 1.00 22.36 ?  507 LEU A CD1 1 
ATOM   2206 C CD2 . LEU A 1 284 ? -20.799 16.462  -33.904 1.00 22.94 ?  507 LEU A CD2 1 
ATOM   2207 N N   . VAL A 1 285 ? -18.392 12.143  -34.584 1.00 22.23 ?  508 VAL A N   1 
ATOM   2208 C CA  . VAL A 1 285 ? -16.978 12.010  -34.912 1.00 18.40 ?  508 VAL A CA  1 
ATOM   2209 C C   . VAL A 1 285 ? -16.600 13.139  -35.861 1.00 21.97 ?  508 VAL A C   1 
ATOM   2210 O O   . VAL A 1 285 ? -17.385 13.509  -36.743 1.00 24.39 ?  508 VAL A O   1 
ATOM   2211 C CB  . VAL A 1 285 ? -16.678 10.629  -35.530 1.00 19.70 ?  508 VAL A CB  1 
ATOM   2212 C CG1 . VAL A 1 285 ? -15.256 10.566  -36.064 1.00 19.07 ?  508 VAL A CG1 1 
ATOM   2213 C CG2 . VAL A 1 285 ? -16.909 9.535   -34.501 1.00 18.47 ?  508 VAL A CG2 1 
ATOM   2214 N N   . ILE A 1 286 ? -15.401 13.694  -35.674 1.00 21.73 ?  509 ILE A N   1 
ATOM   2215 C CA  . ILE A 1 286 ? -14.950 14.864  -36.411 1.00 22.43 ?  509 ILE A CA  1 
ATOM   2216 C C   . ILE A 1 286 ? -13.601 14.557  -37.050 1.00 20.72 ?  509 ILE A C   1 
ATOM   2217 O O   . ILE A 1 286 ? -12.636 14.262  -36.339 1.00 21.40 ?  509 ILE A O   1 
ATOM   2218 C CB  . ILE A 1 286 ? -14.835 16.104  -35.507 1.00 22.87 ?  509 ILE A CB  1 
ATOM   2219 C CG1 . ILE A 1 286 ? -16.187 16.418  -34.865 1.00 21.38 ?  509 ILE A CG1 1 
ATOM   2220 C CG2 . ILE A 1 286 ? -14.322 17.293  -36.307 1.00 20.68 ?  509 ILE A CG2 1 
ATOM   2221 C CD1 . ILE A 1 286 ? -16.316 15.883  -33.448 1.00 22.49 ?  509 ILE A CD1 1 
ATOM   2222 N N   . PRO A 1 287 ? -13.479 14.611  -38.375 1.00 21.17 ?  510 PRO A N   1 
ATOM   2223 C CA  . PRO A 1 287 ? -12.171 14.415  -39.025 1.00 21.53 ?  510 PRO A CA  1 
ATOM   2224 C C   . PRO A 1 287 ? -11.135 15.390  -38.494 1.00 21.65 ?  510 PRO A C   1 
ATOM   2225 O O   . PRO A 1 287 ? -11.484 16.452  -37.956 1.00 20.71 ?  510 PRO A O   1 
ATOM   2226 C CB  . PRO A 1 287 ? -12.474 14.672  -40.509 1.00 18.74 ?  510 PRO A CB  1 
ATOM   2227 C CG  . PRO A 1 287 ? -13.921 14.353  -40.662 1.00 20.78 ?  510 PRO A CG  1 
ATOM   2228 C CD  . PRO A 1 287 ? -14.591 14.633  -39.341 1.00 23.25 ?  510 PRO A CD  1 
ATOM   2229 N N   . PRO A 1 288 ? -9.841  15.068  -38.628 1.00 20.18 ?  511 PRO A N   1 
ATOM   2230 C CA  . PRO A 1 288 ? -8.810  15.837  -37.917 1.00 21.68 ?  511 PRO A CA  1 
ATOM   2231 C C   . PRO A 1 288 ? -8.185  16.968  -38.720 1.00 23.04 ?  511 PRO A C   1 
ATOM   2232 O O   . PRO A 1 288 ? -7.024  17.316  -38.483 1.00 20.26 ?  511 PRO A O   1 
ATOM   2233 C CB  . PRO A 1 288 ? -7.765  14.763  -37.602 1.00 21.52 ?  511 PRO A CB  1 
ATOM   2234 C CG  . PRO A 1 288 ? -7.819  13.888  -38.821 1.00 20.27 ?  511 PRO A CG  1 
ATOM   2235 C CD  . PRO A 1 288 ? -9.279  13.852  -39.244 1.00 19.81 ?  511 PRO A CD  1 
ATOM   2236 N N   . ASN A 1 289 ? -8.920  17.556  -39.660 1.00 24.02 ?  512 ASN A N   1 
ATOM   2237 C CA  . ASN A 1 289 ? -8.352  18.588  -40.530 1.00 22.78 ?  512 ASN A CA  1 
ATOM   2238 C C   . ASN A 1 289 ? -8.619  19.987  -39.966 1.00 22.67 ?  512 ASN A C   1 
ATOM   2239 O O   . ASN A 1 289 ? -9.268  20.829  -40.585 1.00 20.32 ?  512 ASN A O   1 
ATOM   2240 C CB  . ASN A 1 289 ? -8.901  18.448  -41.944 1.00 21.02 ?  512 ASN A CB  1 
ATOM   2241 C CG  . ASN A 1 289 ? -10.415 18.465  -41.986 1.00 23.67 ?  512 ASN A CG  1 
ATOM   2242 O OD1 . ASN A 1 289 ? -11.079 18.064  -41.030 1.00 21.85 ?  512 ASN A OD1 1 
ATOM   2243 N ND2 . ASN A 1 289 ? -10.971 18.942  -43.095 1.00 21.44 ?  512 ASN A ND2 1 
ATOM   2244 N N   . GLY A 1 290 ? -8.091  20.233  -38.772 1.00 21.06 ?  513 GLY A N   1 
ATOM   2245 C CA  . GLY A 1 290 ? -8.266  21.531  -38.148 1.00 21.85 ?  513 GLY A CA  1 
ATOM   2246 C C   . GLY A 1 290 ? -7.390  21.692  -36.928 1.00 21.94 ?  513 GLY A C   1 
ATOM   2247 O O   . GLY A 1 290 ? -6.914  20.713  -36.343 1.00 22.43 ?  513 GLY A O   1 
ATOM   2248 N N   . TYR A 1 291 ? -7.189  22.953  -36.549 1.00 24.01 ?  514 TYR A N   1 
ATOM   2249 C CA  . TYR A 1 291 ? -6.400  23.318  -35.383 1.00 21.66 ?  514 TYR A CA  1 
ATOM   2250 C C   . TYR A 1 291 ? -7.232  24.209  -34.472 1.00 20.01 ?  514 TYR A C   1 
ATOM   2251 O O   . TYR A 1 291 ? -8.208  24.831  -34.899 1.00 21.70 ?  514 TYR A O   1 
ATOM   2252 C CB  . TYR A 1 291 ? -5.097  24.028  -35.788 1.00 23.47 ?  514 TYR A CB  1 
ATOM   2253 C CG  . TYR A 1 291 ? -5.282  25.465  -36.230 1.00 21.57 ?  514 TYR A CG  1 
ATOM   2254 C CD1 . TYR A 1 291 ? -5.574  25.770  -37.553 1.00 24.03 ?  514 TYR A CD1 1 
ATOM   2255 C CD2 . TYR A 1 291 ? -5.166  26.514  -35.326 1.00 23.04 ?  514 TYR A CD2 1 
ATOM   2256 C CE1 . TYR A 1 291 ? -5.746  27.079  -37.964 1.00 26.25 ?  514 TYR A CE1 1 
ATOM   2257 C CE2 . TYR A 1 291 ? -5.337  27.826  -35.727 1.00 23.52 ?  514 TYR A CE2 1 
ATOM   2258 C CZ  . TYR A 1 291 ? -5.626  28.102  -37.046 1.00 26.33 ?  514 TYR A CZ  1 
ATOM   2259 O OH  . TYR A 1 291 ? -5.797  29.406  -37.451 1.00 27.30 ?  514 TYR A OH  1 
ATOM   2260 N N   . PHE A 1 292 ? -6.833  24.269  -33.206 1.00 20.97 ?  515 PHE A N   1 
ATOM   2261 C CA  . PHE A 1 292 ? -7.542  25.049  -32.201 1.00 21.07 ?  515 PHE A CA  1 
ATOM   2262 C C   . PHE A 1 292 ? -6.883  26.412  -32.029 1.00 21.92 ?  515 PHE A C   1 
ATOM   2263 O O   . PHE A 1 292 ? -5.655  26.531  -32.081 1.00 20.67 ?  515 PHE A O   1 
ATOM   2264 C CB  . PHE A 1 292 ? -7.580  24.307  -30.865 1.00 20.84 ?  515 PHE A CB  1 
ATOM   2265 C CG  . PHE A 1 292 ? -8.462  23.091  -30.875 1.00 21.11 ?  515 PHE A CG  1 
ATOM   2266 C CD1 . PHE A 1 292 ? -7.992  21.881  -31.361 1.00 19.51 ?  515 PHE A CD1 1 
ATOM   2267 C CD2 . PHE A 1 292 ? -9.762  23.158  -30.403 1.00 21.70 ?  515 PHE A CD2 1 
ATOM   2268 C CE1 . PHE A 1 292 ? -8.802  20.761  -31.374 1.00 18.93 ?  515 PHE A CE1 1 
ATOM   2269 C CE2 . PHE A 1 292 ? -10.577 22.042  -30.413 1.00 21.00 ?  515 PHE A CE2 1 
ATOM   2270 C CZ  . PHE A 1 292 ? -10.096 20.842  -30.899 1.00 20.48 ?  515 PHE A CZ  1 
ATOM   2271 N N   . ARG A 1 293 ? -7.708  27.436  -31.820 1.00 23.53 ?  516 ARG A N   1 
ATOM   2272 C CA  . ARG A 1 293 ? -7.252  28.820  -31.745 1.00 26.94 ?  516 ARG A CA  1 
ATOM   2273 C C   . ARG A 1 293 ? -7.894  29.493  -30.542 1.00 26.86 ?  516 ARG A C   1 
ATOM   2274 O O   . ARG A 1 293 ? -9.124  29.548  -30.444 1.00 24.49 ?  516 ARG A O   1 
ATOM   2275 C CB  . ARG A 1 293 ? -7.595  29.576  -33.033 1.00 23.02 ?  516 ARG A CB  1 
ATOM   2276 C CG  . ARG A 1 293 ? -7.236  31.052  -33.014 1.00 23.79 ?  516 ARG A CG  1 
ATOM   2277 C CD  . ARG A 1 293 ? -7.720  31.755  -34.277 1.00 23.28 ?  516 ARG A CD  1 
ATOM   2278 N NE  . ARG A 1 293 ? -9.150  32.039  -34.240 1.00 23.95 ?  516 ARG A NE  1 
ATOM   2279 C CZ  . ARG A 1 293 ? -9.906  32.220  -35.315 1.00 23.03 ?  516 ARG A CZ  1 
ATOM   2280 N NH1 . ARG A 1 293 ? -9.402  32.148  -36.536 1.00 18.26 ?  516 ARG A NH1 1 
ATOM   2281 N NH2 . ARG A 1 293 ? -11.202 32.479  -35.161 1.00 23.77 ?  516 ARG A NH2 1 
ATOM   2282 N N   . PHE A 1 294 ? -7.066  30.007  -29.635 1.00 26.03 ?  517 PHE A N   1 
ATOM   2283 C CA  . PHE A 1 294 ? -7.564  30.725  -28.469 1.00 25.40 ?  517 PHE A CA  1 
ATOM   2284 C C   . PHE A 1 294 ? -8.014  32.121  -28.877 1.00 27.06 ?  517 PHE A C   1 
ATOM   2285 O O   . PHE A 1 294 ? -7.256  32.868  -29.504 1.00 27.66 ?  517 PHE A O   1 
ATOM   2286 C CB  . PHE A 1 294 ? -6.483  30.808  -27.393 1.00 24.81 ?  517 PHE A CB  1 
ATOM   2287 C CG  . PHE A 1 294 ? -6.860  31.667  -26.220 1.00 28.66 ?  517 PHE A CG  1 
ATOM   2288 C CD1 . PHE A 1 294 ? -7.998  31.392  -25.480 1.00 26.38 ?  517 PHE A CD1 1 
ATOM   2289 C CD2 . PHE A 1 294 ? -6.077  32.751  -25.858 1.00 26.66 ?  517 PHE A CD2 1 
ATOM   2290 C CE1 . PHE A 1 294 ? -8.347  32.180  -24.400 1.00 27.10 ?  517 PHE A CE1 1 
ATOM   2291 C CE2 . PHE A 1 294 ? -6.422  33.544  -24.778 1.00 26.97 ?  517 PHE A CE2 1 
ATOM   2292 C CZ  . PHE A 1 294 ? -7.559  33.258  -24.049 1.00 27.03 ?  517 PHE A CZ  1 
ATOM   2293 N N   . ASP A 1 295 ? -9.246  32.477  -28.520 1.00 23.92 ?  518 ASP A N   1 
ATOM   2294 C CA  . ASP A 1 295 ? -9.822  33.753  -28.930 1.00 31.61 ?  518 ASP A CA  1 
ATOM   2295 C C   . ASP A 1 295 ? -10.087 34.710  -27.778 1.00 30.45 ?  518 ASP A C   1 
ATOM   2296 O O   . ASP A 1 295 ? -9.891  35.918  -27.941 1.00 36.08 ?  518 ASP A O   1 
ATOM   2297 C CB  . ASP A 1 295 ? -11.120 33.522  -29.713 1.00 28.00 ?  518 ASP A CB  1 
ATOM   2298 C CG  . ASP A 1 295 ? -10.863 33.188  -31.170 1.00 29.62 ?  518 ASP A CG  1 
ATOM   2299 O OD1 . ASP A 1 295 ? -9.681  33.177  -31.574 1.00 29.65 ?  518 ASP A OD1 1 
ATOM   2300 O OD2 . ASP A 1 295 ? -11.836 32.953  -31.916 1.00 35.67 -1 518 ASP A OD2 1 
ATOM   2301 N N   . SER A 1 296 ? -10.524 34.216  -26.621 1.00 27.83 ?  519 SER A N   1 
ATOM   2302 C CA  . SER A 1 296 ? -10.726 35.069  -25.455 1.00 29.13 ?  519 SER A CA  1 
ATOM   2303 C C   . SER A 1 296 ? -11.011 34.200  -24.240 1.00 29.45 ?  519 SER A C   1 
ATOM   2304 O O   . SER A 1 296 ? -11.444 33.050  -24.360 1.00 26.71 ?  519 SER A O   1 
ATOM   2305 C CB  . SER A 1 296 ? -11.873 36.066  -25.660 1.00 29.35 ?  519 SER A CB  1 
ATOM   2306 O OG  . SER A 1 296 ? -13.128 35.453  -25.422 1.00 34.53 ?  519 SER A OG  1 
ATOM   2307 N N   . TRP A 1 297 ? -10.759 34.775  -23.065 1.00 30.95 ?  520 TRP A N   1 
ATOM   2308 C CA  . TRP A 1 297 ? -11.167 34.165  -21.810 1.00 27.08 ?  520 TRP A CA  1 
ATOM   2309 C C   . TRP A 1 297 ? -12.653 34.397  -21.580 1.00 28.50 ?  520 TRP A C   1 
ATOM   2310 O O   . TRP A 1 297 ? -13.172 35.490  -21.822 1.00 31.11 ?  520 TRP A O   1 
ATOM   2311 C CB  . TRP A 1 297 ? -10.365 34.743  -20.643 1.00 29.93 ?  520 TRP A CB  1 
ATOM   2312 C CG  . TRP A 1 297 ? -8.929  34.331  -20.635 1.00 28.52 ?  520 TRP A CG  1 
ATOM   2313 C CD1 . TRP A 1 297 ? -7.860  35.073  -21.044 1.00 28.31 ?  520 TRP A CD1 1 
ATOM   2314 C CD2 . TRP A 1 297 ? -8.403  33.073  -20.197 1.00 26.86 ?  520 TRP A CD2 1 
ATOM   2315 N NE1 . TRP A 1 297 ? -6.699  34.354  -20.886 1.00 30.52 ?  520 TRP A NE1 1 
ATOM   2316 C CE2 . TRP A 1 297 ? -7.006  33.123  -20.368 1.00 26.76 ?  520 TRP A CE2 1 
ATOM   2317 C CE3 . TRP A 1 297 ? -8.979  31.910  -19.677 1.00 24.37 ?  520 TRP A CE3 1 
ATOM   2318 C CZ2 . TRP A 1 297 ? -6.177  32.054  -20.037 1.00 27.59 ?  520 TRP A CZ2 1 
ATOM   2319 C CZ3 . TRP A 1 297 ? -8.153  30.850  -19.350 1.00 26.81 ?  520 TRP A CZ3 1 
ATOM   2320 C CH2 . TRP A 1 297 ? -6.767  30.929  -19.532 1.00 27.72 ?  520 TRP A CH2 1 
ATOM   2321 N N   . VAL A 1 298 ? -13.340 33.353  -21.123 1.00 26.22 ?  521 VAL A N   1 
ATOM   2322 C CA  . VAL A 1 298 ? -14.756 33.439  -20.786 1.00 23.51 ?  521 VAL A CA  1 
ATOM   2323 C C   . VAL A 1 298 ? -14.965 32.733  -19.455 1.00 25.63 ?  521 VAL A C   1 
ATOM   2324 O O   . VAL A 1 298 ? -13.999 32.324  -18.802 1.00 29.72 ?  521 VAL A O   1 
ATOM   2325 C CB  . VAL A 1 298 ? -15.640 32.828  -21.890 1.00 27.36 ?  521 VAL A CB  1 
ATOM   2326 C CG1 . VAL A 1 298 ? -15.460 33.574  -23.206 1.00 24.93 ?  521 VAL A CG1 1 
ATOM   2327 C CG2 . VAL A 1 298 ? -15.318 31.359  -22.070 1.00 25.17 ?  521 VAL A CG2 1 
ATOM   2328 N N   . ASN A 1 299 ? -16.216 32.589  -19.036 1.00 30.33 ?  522 ASN A N   1 
ATOM   2329 C CA  . ASN A 1 299 ? -16.547 31.835  -17.836 1.00 28.83 ?  522 ASN A CA  1 
ATOM   2330 C C   . ASN A 1 299 ? -17.344 30.589  -18.214 1.00 32.76 ?  522 ASN A C   1 
ATOM   2331 O O   . ASN A 1 299 ? -17.678 30.363  -19.381 1.00 31.46 ?  522 ASN A O   1 
ATOM   2332 C CB  . ASN A 1 299 ? -17.297 32.714  -16.827 1.00 27.66 ?  522 ASN A CB  1 
ATOM   2333 C CG  . ASN A 1 299 ? -18.595 33.282  -17.378 1.00 29.93 ?  522 ASN A CG  1 
ATOM   2334 O OD1 . ASN A 1 299 ? -19.414 32.565  -17.953 1.00 31.77 ?  522 ASN A OD1 1 
ATOM   2335 N ND2 . ASN A 1 299 ? -18.793 34.582  -17.189 1.00 26.95 ?  522 ASN A ND2 1 
ATOM   2336 N N   . GLN A 1 300 ? -17.650 29.774  -17.204 1.00 33.82 ?  523 GLN A N   1 
ATOM   2337 C CA  . GLN A 1 300 ? -18.341 28.511  -17.434 1.00 33.61 ?  523 GLN A CA  1 
ATOM   2338 C C   . GLN A 1 300 ? -19.781 28.692  -17.894 1.00 31.60 ?  523 GLN A C   1 
ATOM   2339 O O   . GLN A 1 300 ? -20.406 27.710  -18.307 1.00 30.81 ?  523 GLN A O   1 
ATOM   2340 C CB  . GLN A 1 300 ? -18.312 27.661  -16.163 1.00 32.27 ?  523 GLN A CB  1 
ATOM   2341 C CG  . GLN A 1 300 ? -18.516 28.445  -14.879 1.00 35.54 ?  523 GLN A CG  1 
ATOM   2342 C CD  . GLN A 1 300 ? -19.164 27.614  -13.791 1.00 39.44 ?  523 GLN A CD  1 
ATOM   2343 O OE1 . GLN A 1 300 ? -19.586 26.483  -14.029 1.00 37.66 ?  523 GLN A OE1 1 
ATOM   2344 N NE2 . GLN A 1 300 ? -19.238 28.167  -12.586 1.00 40.19 ?  523 GLN A NE2 1 
ATOM   2345 N N   . PHE A 1 301 ? -20.320 29.907  -17.838 1.00 29.50 ?  524 PHE A N   1 
ATOM   2346 C CA  . PHE A 1 301 ? -21.695 30.158  -18.244 1.00 31.17 ?  524 PHE A CA  1 
ATOM   2347 C C   . PHE A 1 301 ? -21.815 30.623  -19.689 1.00 31.77 ?  524 PHE A C   1 
ATOM   2348 O O   . PHE A 1 301 ? -22.936 30.835  -20.163 1.00 32.17 ?  524 PHE A O   1 
ATOM   2349 C CB  . PHE A 1 301 ? -22.338 31.186  -17.310 1.00 30.62 ?  524 PHE A CB  1 
ATOM   2350 C CG  . PHE A 1 301 ? -22.536 30.685  -15.909 1.00 32.27 ?  524 PHE A CG  1 
ATOM   2351 C CD1 . PHE A 1 301 ? -23.444 29.673  -15.643 1.00 33.40 ?  524 PHE A CD1 1 
ATOM   2352 C CD2 . PHE A 1 301 ? -21.810 31.220  -14.858 1.00 32.10 ?  524 PHE A CD2 1 
ATOM   2353 C CE1 . PHE A 1 301 ? -23.627 29.208  -14.354 1.00 32.75 ?  524 PHE A CE1 1 
ATOM   2354 C CE2 . PHE A 1 301 ? -21.989 30.759  -13.567 1.00 33.81 ?  524 PHE A CE2 1 
ATOM   2355 C CZ  . PHE A 1 301 ? -22.898 29.751  -13.315 1.00 32.94 ?  524 PHE A CZ  1 
ATOM   2356 N N   . TYR A 1 302 ? -20.696 30.794  -20.392 1.00 31.92 ?  525 TYR A N   1 
ATOM   2357 C CA  . TYR A 1 302 ? -20.740 31.093  -21.818 1.00 27.03 ?  525 TYR A CA  1 
ATOM   2358 C C   . TYR A 1 302 ? -21.513 30.005  -22.552 1.00 27.73 ?  525 TYR A C   1 
ATOM   2359 O O   . TYR A 1 302 ? -21.313 28.813  -22.308 1.00 31.21 ?  525 TYR A O   1 
ATOM   2360 C CB  . TYR A 1 302 ? -19.318 31.209  -22.370 1.00 26.39 ?  525 TYR A CB  1 
ATOM   2361 C CG  . TYR A 1 302 ? -19.221 31.789  -23.764 1.00 26.78 ?  525 TYR A CG  1 
ATOM   2362 C CD1 . TYR A 1 302 ? -19.342 30.975  -24.884 1.00 28.32 ?  525 TYR A CD1 1 
ATOM   2363 C CD2 . TYR A 1 302 ? -18.993 33.144  -23.961 1.00 24.90 ?  525 TYR A CD2 1 
ATOM   2364 C CE1 . TYR A 1 302 ? -19.249 31.497  -26.160 1.00 28.37 ?  525 TYR A CE1 1 
ATOM   2365 C CE2 . TYR A 1 302 ? -18.897 33.675  -25.235 1.00 25.64 ?  525 TYR A CE2 1 
ATOM   2366 C CZ  . TYR A 1 302 ? -19.026 32.847  -26.329 1.00 26.54 ?  525 TYR A CZ  1 
ATOM   2367 O OH  . TYR A 1 302 ? -18.932 33.370  -27.598 1.00 31.60 ?  525 TYR A OH  1 
ATOM   2368 N N   . THR A 1 303 ? -22.412 30.416  -23.441 1.00 27.46 ?  526 THR A N   1 
ATOM   2369 C CA  . THR A 1 303 ? -23.251 29.486  -24.184 1.00 26.88 ?  526 THR A CA  1 
ATOM   2370 C C   . THR A 1 303 ? -22.627 29.234  -25.550 1.00 26.22 ?  526 THR A C   1 
ATOM   2371 O O   . THR A 1 303 ? -22.456 30.168  -26.342 1.00 21.71 ?  526 THR A O   1 
ATOM   2372 C CB  . THR A 1 303 ? -24.675 30.023  -24.328 1.00 23.74 ?  526 THR A CB  1 
ATOM   2373 O OG1 . THR A 1 303 ? -25.274 30.136  -23.031 1.00 27.75 ?  526 THR A OG1 1 
ATOM   2374 C CG2 . THR A 1 303 ? -25.512 29.083  -25.181 1.00 22.98 ?  526 THR A CG2 1 
ATOM   2375 N N   . LEU A 1 304 ? -22.292 27.977  -25.820 1.00 26.31 ?  527 LEU A N   1 
ATOM   2376 C CA  . LEU A 1 304 ? -21.623 27.610  -27.058 1.00 25.77 ?  527 LEU A CA  1 
ATOM   2377 C C   . LEU A 1 304 ? -22.629 27.413  -28.184 1.00 25.33 ?  527 LEU A C   1 
ATOM   2378 O O   . LEU A 1 304 ? -23.766 26.984  -27.967 1.00 24.02 ?  527 LEU A O   1 
ATOM   2379 C CB  . LEU A 1 304 ? -20.816 26.325  -26.872 1.00 25.63 ?  527 LEU A CB  1 
ATOM   2380 C CG  . LEU A 1 304 ? -19.563 26.379  -25.998 1.00 26.35 ?  527 LEU A CG  1 
ATOM   2381 C CD1 . LEU A 1 304 ? -19.018 24.976  -25.778 1.00 24.27 ?  527 LEU A CD1 1 
ATOM   2382 C CD2 . LEU A 1 304 ? -18.508 27.275  -26.625 1.00 25.36 ?  527 LEU A CD2 1 
ATOM   2383 N N   . ALA A 1 305 ? -22.196 27.731  -29.394 1.00 26.03 ?  528 ALA A N   1 
ATOM   2384 C CA  . ALA A 1 305 ? -22.983 27.393  -30.570 1.00 26.98 ?  528 ALA A CA  1 
ATOM   2385 C C   . ALA A 1 305 ? -22.944 25.884  -30.777 1.00 27.63 ?  528 ALA A C   1 
ATOM   2386 O O   . ALA A 1 305 ? -21.855 25.298  -30.807 1.00 27.10 ?  528 ALA A O   1 
ATOM   2387 C CB  . ALA A 1 305 ? -22.447 28.113  -31.805 1.00 21.33 ?  528 ALA A CB  1 
ATOM   2388 N N   . PRO A 1 306 ? -24.094 25.221  -30.888 1.00 27.19 ?  529 PRO A N   1 
ATOM   2389 C CA  . PRO A 1 306 ? -24.091 23.782  -31.173 1.00 27.65 ?  529 PRO A CA  1 
ATOM   2390 C C   . PRO A 1 306 ? -23.299 23.475  -32.436 1.00 27.01 ?  529 PRO A C   1 
ATOM   2391 O O   . PRO A 1 306 ? -23.328 24.227  -33.411 1.00 31.17 ?  529 PRO A O   1 
ATOM   2392 C CB  . PRO A 1 306 ? -25.577 23.452  -31.342 1.00 26.90 ?  529 PRO A CB  1 
ATOM   2393 C CG  . PRO A 1 306 ? -26.281 24.481  -30.525 1.00 26.70 ?  529 PRO A CG  1 
ATOM   2394 C CD  . PRO A 1 306 ? -25.445 25.731  -30.597 1.00 26.89 ?  529 PRO A CD  1 
ATOM   2395 N N   . MET A 1 307 ? -22.577 22.361  -32.406 1.00 32.11 ?  530 MET A N   1 
ATOM   2396 C CA  . MET A 1 307 ? -21.686 22.001  -33.499 1.00 35.28 ?  530 MET A CA  1 
ATOM   2397 C C   . MET A 1 307 ? -22.287 20.912  -34.380 1.00 30.31 ?  530 MET A C   1 
ATOM   2398 O O   . MET A 1 307 ? -23.108 20.116  -33.926 1.00 35.48 ?  530 MET A O   1 
ATOM   2399 C CB  . MET A 1 307 ? -20.336 21.553  -32.941 1.00 31.26 ?  530 MET A CB  1 
ATOM   2400 C CG  . MET A 1 307 ? -20.398 20.276  -32.123 1.00 32.00 ?  530 MET A CG  1 
ATOM   2401 S SD  . MET A 1 307 ? -18.807 19.881  -31.383 1.00 42.50 ?  530 MET A SD  1 
ATOM   2402 C CE  . MET A 1 307 ? -18.272 18.559  -32.453 1.00 28.48 ?  530 MET A CE  1 
ATOM   2403 N N   . THR B 1 1   ? 7.176   41.267  -37.213 1.00 51.24 ?  224 THR B N   1 
ATOM   2404 C CA  . THR B 1 1   ? 8.016   40.078  -37.288 1.00 50.60 ?  224 THR B CA  1 
ATOM   2405 C C   . THR B 1 1   ? 8.053   39.373  -35.934 1.00 44.11 ?  224 THR B C   1 
ATOM   2406 O O   . THR B 1 1   ? 8.385   39.979  -34.914 1.00 41.55 ?  224 THR B O   1 
ATOM   2407 C CB  . THR B 1 1   ? 9.448   40.428  -37.745 1.00 47.64 ?  224 THR B CB  1 
ATOM   2408 O OG1 . THR B 1 1   ? 9.480   40.532  -39.174 1.00 57.20 ?  224 THR B OG1 1 
ATOM   2409 C CG2 . THR B 1 1   ? 10.438  39.359  -37.302 1.00 44.66 ?  224 THR B CG2 1 
ATOM   2410 N N   . LYS B 1 2   ? 7.702   38.093  -35.935 1.00 42.45 ?  225 LYS B N   1 
ATOM   2411 C CA  . LYS B 1 2   ? 7.589   37.346  -34.689 1.00 37.31 ?  225 LYS B CA  1 
ATOM   2412 C C   . LYS B 1 2   ? 8.972   37.057  -34.117 1.00 37.48 ?  225 LYS B C   1 
ATOM   2413 O O   . LYS B 1 2   ? 9.869   36.634  -34.857 1.00 37.67 ?  225 LYS B O   1 
ATOM   2414 C CB  . LYS B 1 2   ? 6.833   36.040  -34.922 1.00 37.29 ?  225 LYS B CB  1 
ATOM   2415 C CG  . LYS B 1 2   ? 6.154   35.488  -33.681 1.00 36.73 ?  225 LYS B CG  1 
ATOM   2416 C CD  . LYS B 1 2   ? 5.896   33.998  -33.815 1.00 36.35 ?  225 LYS B CD  1 
ATOM   2417 C CE  . LYS B 1 2   ? 4.476   33.724  -34.281 1.00 41.68 ?  225 LYS B CE  1 
ATOM   2418 N NZ  . LYS B 1 2   ? 3.682   33.011  -33.242 1.00 41.69 ?  225 LYS B NZ  1 
ATOM   2419 N N   . PRO B 1 3   ? 9.187   37.269  -32.819 1.00 32.91 ?  226 PRO B N   1 
ATOM   2420 C CA  . PRO B 1 3   ? 10.489  36.945  -32.227 1.00 29.90 ?  226 PRO B CA  1 
ATOM   2421 C C   . PRO B 1 3   ? 10.750  35.447  -32.254 1.00 32.77 ?  226 PRO B C   1 
ATOM   2422 O O   . PRO B 1 3   ? 9.845   34.633  -32.057 1.00 35.39 ?  226 PRO B O   1 
ATOM   2423 C CB  . PRO B 1 3   ? 10.365  37.471  -30.792 1.00 31.45 ?  226 PRO B CB  1 
ATOM   2424 C CG  . PRO B 1 3   ? 8.890   37.489  -30.528 1.00 33.76 ?  226 PRO B CG  1 
ATOM   2425 C CD  . PRO B 1 3   ? 8.268   37.869  -31.838 1.00 31.38 ?  226 PRO B CD  1 
ATOM   2426 N N   . PHE B 1 4   ? 12.004  35.088  -32.509 1.00 30.06 ?  227 PHE B N   1 
ATOM   2427 C CA  . PHE B 1 4   ? 12.410  33.692  -32.515 1.00 28.70 ?  227 PHE B CA  1 
ATOM   2428 C C   . PHE B 1 4   ? 12.553  33.177  -31.089 1.00 28.74 ?  227 PHE B C   1 
ATOM   2429 O O   . PHE B 1 4   ? 12.834  33.936  -30.157 1.00 31.58 ?  227 PHE B O   1 
ATOM   2430 C CB  . PHE B 1 4   ? 13.729  33.526  -33.271 1.00 26.77 ?  227 PHE B CB  1 
ATOM   2431 C CG  . PHE B 1 4   ? 14.202  32.104  -33.367 1.00 28.54 ?  227 PHE B CG  1 
ATOM   2432 C CD1 . PHE B 1 4   ? 13.631  31.231  -34.277 1.00 25.71 ?  227 PHE B CD1 1 
ATOM   2433 C CD2 . PHE B 1 4   ? 15.219  31.642  -32.548 1.00 26.10 ?  227 PHE B CD2 1 
ATOM   2434 C CE1 . PHE B 1 4   ? 14.065  29.922  -34.369 1.00 25.60 ?  227 PHE B CE1 1 
ATOM   2435 C CE2 . PHE B 1 4   ? 15.658  30.334  -32.634 1.00 27.38 ?  227 PHE B CE2 1 
ATOM   2436 C CZ  . PHE B 1 4   ? 15.080  29.473  -33.545 1.00 25.62 ?  227 PHE B CZ  1 
ATOM   2437 N N   . SER B 1 5   ? 12.352  31.872  -30.924 1.00 25.63 ?  228 SER B N   1 
ATOM   2438 C CA  . SER B 1 5   ? 12.494  31.239  -29.619 1.00 25.79 ?  228 SER B CA  1 
ATOM   2439 C C   . SER B 1 5   ? 12.597  29.733  -29.810 1.00 27.15 ?  228 SER B C   1 
ATOM   2440 O O   . SER B 1 5   ? 12.179  29.190  -30.838 1.00 26.82 ?  228 SER B O   1 
ATOM   2441 C CB  . SER B 1 5   ? 11.326  31.588  -28.690 1.00 24.09 ?  228 SER B CB  1 
ATOM   2442 O OG  . SER B 1 5   ? 10.150  30.892  -29.062 1.00 24.81 ?  228 SER B OG  1 
ATOM   2443 N N   . VAL B 1 6   ? 13.164  29.069  -28.806 1.00 26.56 ?  229 VAL B N   1 
ATOM   2444 C CA  . VAL B 1 6   ? 13.307  27.615  -28.818 1.00 23.20 ?  229 VAL B CA  1 
ATOM   2445 C C   . VAL B 1 6   ? 12.571  27.044  -27.613 1.00 25.39 ?  229 VAL B C   1 
ATOM   2446 O O   . VAL B 1 6   ? 12.474  27.716  -26.575 1.00 26.26 ?  229 VAL B O   1 
ATOM   2447 C CB  . VAL B 1 6   ? 14.785  27.198  -28.821 1.00 25.17 ?  229 VAL B CB  1 
ATOM   2448 C CG1 . VAL B 1 6   ? 15.460  27.698  -30.081 1.00 24.67 ?  229 VAL B CG1 1 
ATOM   2449 C CG2 . VAL B 1 6   ? 15.502  27.723  -27.587 1.00 32.58 ?  229 VAL B CG2 1 
ATOM   2450 N N   . PRO B 1 7   ? 12.026  25.830  -27.706 1.00 26.93 ?  230 PRO B N   1 
ATOM   2451 C CA  . PRO B 1 7   ? 11.329  25.245  -26.556 1.00 26.60 ?  230 PRO B CA  1 
ATOM   2452 C C   . PRO B 1 7   ? 12.241  25.154  -25.340 1.00 26.86 ?  230 PRO B C   1 
ATOM   2453 O O   . PRO B 1 7   ? 13.464  25.056  -25.459 1.00 27.45 ?  230 PRO B O   1 
ATOM   2454 C CB  . PRO B 1 7   ? 10.918  23.858  -27.061 1.00 22.84 ?  230 PRO B CB  1 
ATOM   2455 C CG  . PRO B 1 7   ? 10.837  24.002  -28.536 1.00 23.05 ?  230 PRO B CG  1 
ATOM   2456 C CD  . PRO B 1 7   ? 11.874  25.018  -28.927 1.00 24.70 ?  230 PRO B CD  1 
ATOM   2457 N N   . VAL B 1 8   ? 11.629  25.203  -24.157 1.00 25.17 ?  231 VAL B N   1 
ATOM   2458 C CA  . VAL B 1 8   ? 12.372  25.229  -22.904 1.00 28.78 ?  231 VAL B CA  1 
ATOM   2459 C C   . VAL B 1 8   ? 12.420  23.859  -22.237 1.00 25.84 ?  231 VAL B C   1 
ATOM   2460 O O   . VAL B 1 8   ? 12.890  23.747  -21.101 1.00 35.07 ?  231 VAL B O   1 
ATOM   2461 C CB  . VAL B 1 8   ? 11.804  26.283  -21.939 1.00 30.82 ?  231 VAL B CB  1 
ATOM   2462 C CG1 . VAL B 1 8   ? 12.060  27.684  -22.471 1.00 32.57 ?  231 VAL B CG1 1 
ATOM   2463 C CG2 . VAL B 1 8   ? 10.319  26.055  -21.710 1.00 32.57 ?  231 VAL B CG2 1 
ATOM   2464 N N   . LEU B 1 9   ? 11.941  22.816  -22.907 1.00 24.60 ?  232 LEU B N   1 
ATOM   2465 C CA  . LEU B 1 9   ? 12.081  21.472  -22.367 1.00 22.34 ?  232 LEU B CA  1 
ATOM   2466 C C   . LEU B 1 9   ? 13.549  21.068  -22.354 1.00 23.53 ?  232 LEU B C   1 
ATOM   2467 O O   . LEU B 1 9   ? 14.298  21.361  -23.290 1.00 22.48 ?  232 LEU B O   1 
ATOM   2468 C CB  . LEU B 1 9   ? 11.273  20.467  -23.188 1.00 21.84 ?  232 LEU B CB  1 
ATOM   2469 C CG  . LEU B 1 9   ? 9.796   20.763  -23.446 1.00 22.14 ?  232 LEU B CG  1 
ATOM   2470 C CD1 . LEU B 1 9   ? 9.367   20.160  -24.773 1.00 18.45 ?  232 LEU B CD1 1 
ATOM   2471 C CD2 . LEU B 1 9   ? 8.941   20.230  -22.309 1.00 19.35 ?  232 LEU B CD2 1 
ATOM   2472 N N   . THR B 1 10  ? 13.964  20.405  -21.280 1.00 22.36 ?  233 THR B N   1 
ATOM   2473 C CA  . THR B 1 10  ? 15.315  19.874  -21.237 1.00 22.91 ?  233 THR B CA  1 
ATOM   2474 C C   . THR B 1 10  ? 15.461  18.738  -22.247 1.00 23.77 ?  233 THR B C   1 
ATOM   2475 O O   . THR B 1 10  ? 14.478  18.135  -22.688 1.00 24.63 ?  233 THR B O   1 
ATOM   2476 C CB  . THR B 1 10  ? 15.664  19.379  -19.832 1.00 24.98 ?  233 THR B CB  1 
ATOM   2477 O OG1 . THR B 1 10  ? 14.731  18.368  -19.431 1.00 22.38 ?  233 THR B OG1 1 
ATOM   2478 C CG2 . THR B 1 10  ? 15.619  20.528  -18.834 1.00 23.10 ?  233 THR B CG2 1 
ATOM   2479 N N   . VAL B 1 11  ? 16.714  18.461  -22.621 1.00 23.38 ?  234 VAL B N   1 
ATOM   2480 C CA  . VAL B 1 11  ? 16.999  17.377  -23.561 1.00 22.77 ?  234 VAL B CA  1 
ATOM   2481 C C   . VAL B 1 11  ? 16.371  16.077  -23.077 1.00 23.91 ?  234 VAL B C   1 
ATOM   2482 O O   . VAL B 1 11  ? 15.840  15.288  -23.869 1.00 24.04 ?  234 VAL B O   1 
ATOM   2483 C CB  . VAL B 1 11  ? 18.521  17.232  -23.760 1.00 20.42 ?  234 VAL B CB  1 
ATOM   2484 C CG1 . VAL B 1 11  ? 18.844  15.982  -24.570 1.00 22.14 ?  234 VAL B CG1 1 
ATOM   2485 C CG2 . VAL B 1 11  ? 19.093  18.471  -24.428 1.00 20.09 ?  234 VAL B CG2 1 
ATOM   2486 N N   . GLU B 1 12  ? 16.400  15.851  -21.760 1.00 25.68 ?  235 GLU B N   1 
ATOM   2487 C CA  . GLU B 1 12  ? 15.816  14.648  -21.175 1.00 23.70 ?  235 GLU B CA  1 
ATOM   2488 C C   . GLU B 1 12  ? 14.338  14.501  -21.512 1.00 25.00 ?  235 GLU B C   1 
ATOM   2489 O O   . GLU B 1 12  ? 13.821  13.379  -21.553 1.00 23.70 ?  235 GLU B O   1 
ATOM   2490 C CB  . GLU B 1 12  ? 16.001  14.677  -19.658 1.00 24.04 ?  235 GLU B CB  1 
ATOM   2491 C CG  . GLU B 1 12  ? 16.607  13.422  -19.064 1.00 28.42 ?  235 GLU B CG  1 
ATOM   2492 C CD  . GLU B 1 12  ? 16.590  13.440  -17.548 1.00 27.02 ?  235 GLU B CD  1 
ATOM   2493 O OE1 . GLU B 1 12  ? 16.267  14.500  -16.971 1.00 24.60 ?  235 GLU B OE1 1 
ATOM   2494 O OE2 . GLU B 1 12  ? 16.910  12.401  -16.935 1.00 32.51 ?  235 GLU B OE2 1 
ATOM   2495 N N   . GLU B 1 13  ? 13.644  15.610  -21.755 1.00 23.60 ?  236 GLU B N   1 
ATOM   2496 C CA  . GLU B 1 13  ? 12.202  15.600  -21.949 1.00 21.99 ?  236 GLU B CA  1 
ATOM   2497 C C   . GLU B 1 13  ? 11.790  15.588  -23.415 1.00 25.84 ?  236 GLU B C   1 
ATOM   2498 O O   . GLU B 1 13  ? 10.590  15.570  -23.704 1.00 28.99 ?  236 GLU B O   1 
ATOM   2499 C CB  . GLU B 1 13  ? 11.577  16.812  -21.253 1.00 22.80 ?  236 GLU B CB  1 
ATOM   2500 C CG  . GLU B 1 13  ? 11.640  16.737  -19.743 1.00 24.82 ?  236 GLU B CG  1 
ATOM   2501 C CD  . GLU B 1 13  ? 11.736  18.101  -19.098 1.00 30.83 ?  236 GLU B CD  1 
ATOM   2502 O OE1 . GLU B 1 13  ? 11.810  19.108  -19.834 1.00 30.24 ?  236 GLU B OE1 1 
ATOM   2503 O OE2 . GLU B 1 13  ? 11.750  18.161  -17.852 1.00 31.95 ?  236 GLU B OE2 1 
ATOM   2504 N N   . MET B 1 14  ? 12.743  15.591  -24.340 1.00 24.71 ?  237 MET B N   1 
ATOM   2505 C CA  . MET B 1 14  ? 12.449  15.690  -25.762 1.00 22.76 ?  237 MET B CA  1 
ATOM   2506 C C   . MET B 1 14  ? 12.727  14.365  -26.462 1.00 23.49 ?  237 MET B C   1 
ATOM   2507 O O   . MET B 1 14  ? 13.375  13.464  -25.921 1.00 25.42 ?  237 MET B O   1 
ATOM   2508 C CB  . MET B 1 14  ? 13.255  16.827  -26.398 1.00 19.72 ?  237 MET B CB  1 
ATOM   2509 C CG  . MET B 1 14  ? 12.797  18.207  -25.952 1.00 21.26 ?  237 MET B CG  1 
ATOM   2510 S SD  . MET B 1 14  ? 13.613  19.557  -26.820 1.00 22.78 ?  237 MET B SD  1 
ATOM   2511 C CE  . MET B 1 14  ? 15.155  19.655  -25.918 1.00 18.21 ?  237 MET B CE  1 
ATOM   2512 N N   . THR B 1 15  ? 12.225  14.261  -27.690 1.00 21.73 ?  238 THR B N   1 
ATOM   2513 C CA  . THR B 1 15  ? 12.214  13.016  -28.444 1.00 23.76 ?  238 THR B CA  1 
ATOM   2514 C C   . THR B 1 15  ? 13.183  13.092  -29.618 1.00 21.22 ?  238 THR B C   1 
ATOM   2515 O O   . THR B 1 15  ? 13.349  14.150  -30.232 1.00 21.39 ?  238 THR B O   1 
ATOM   2516 C CB  . THR B 1 15  ? 10.804  12.709  -28.960 1.00 19.90 ?  238 THR B CB  1 
ATOM   2517 O OG1 . THR B 1 15  ? 9.849   12.965  -27.923 1.00 22.39 ?  238 THR B OG1 1 
ATOM   2518 C CG2 . THR B 1 15  ? 10.691  11.256  -29.394 1.00 20.34 ?  238 THR B CG2 1 
ATOM   2519 N N   . ASN B 1 16  ? 13.818  11.962  -29.921 1.00 21.99 ?  239 ASN B N   1 
ATOM   2520 C CA  . ASN B 1 16  ? 14.661  11.869  -31.105 1.00 21.35 ?  239 ASN B CA  1 
ATOM   2521 C C   . ASN B 1 16  ? 13.806  11.951  -32.362 1.00 21.22 ?  239 ASN B C   1 
ATOM   2522 O O   . ASN B 1 16  ? 12.718  11.373  -32.434 1.00 18.23 ?  239 ASN B O   1 
ATOM   2523 C CB  . ASN B 1 16  ? 15.458  10.564  -31.092 1.00 21.82 ?  239 ASN B CB  1 
ATOM   2524 C CG  . ASN B 1 16  ? 16.647  10.596  -32.035 1.00 23.20 ?  239 ASN B CG  1 
ATOM   2525 O OD1 . ASN B 1 16  ? 16.489  10.715  -33.251 1.00 20.27 ?  239 ASN B OD1 1 
ATOM   2526 N ND2 . ASN B 1 16  ? 17.848  10.489  -31.475 1.00 20.73 ?  239 ASN B ND2 1 
ATOM   2527 N N   . SER B 1 17  ? 14.304  12.676  -33.358 1.00 21.94 ?  240 SER B N   1 
ATOM   2528 C CA  . SER B 1 17  ? 13.554  12.917  -34.582 1.00 22.28 ?  240 SER B CA  1 
ATOM   2529 C C   . SER B 1 17  ? 13.892  11.937  -35.698 1.00 21.18 ?  240 SER B C   1 
ATOM   2530 O O   . SER B 1 17  ? 13.382  12.092  -36.812 1.00 17.36 ?  240 SER B O   1 
ATOM   2531 C CB  . SER B 1 17  ? 13.793  14.350  -35.062 1.00 19.80 ?  240 SER B CB  1 
ATOM   2532 O OG  . SER B 1 17  ? 15.167  14.573  -35.321 1.00 19.65 ?  240 SER B OG  1 
ATOM   2533 N N   . ARG B 1 18  ? 14.732  10.938  -35.433 1.00 19.67 ?  241 ARG B N   1 
ATOM   2534 C CA  . ARG B 1 18  ? 15.064  9.917   -36.417 1.00 22.47 ?  241 ARG B CA  1 
ATOM   2535 C C   . ARG B 1 18  ? 14.589  8.531   -36.003 1.00 21.98 ?  241 ARG B C   1 
ATOM   2536 O O   . ARG B 1 18  ? 14.791  7.569   -36.752 1.00 21.91 ?  241 ARG B O   1 
ATOM   2537 C CB  . ARG B 1 18  ? 16.578  9.904   -36.671 1.00 19.14 ?  241 ARG B CB  1 
ATOM   2538 C CG  . ARG B 1 18  ? 17.091  11.172  -37.344 1.00 19.55 ?  241 ARG B CG  1 
ATOM   2539 C CD  . ARG B 1 18  ? 18.584  11.112  -37.634 1.00 17.33 ?  241 ARG B CD  1 
ATOM   2540 N NE  . ARG B 1 18  ? 18.928  10.063  -38.587 1.00 20.74 ?  241 ARG B NE  1 
ATOM   2541 C CZ  . ARG B 1 18  ? 20.102  9.449   -38.632 1.00 23.66 ?  241 ARG B CZ  1 
ATOM   2542 N NH1 . ARG B 1 18  ? 21.079  9.761   -37.797 1.00 19.34 ?  241 ARG B NH1 1 
ATOM   2543 N NH2 . ARG B 1 18  ? 20.302  8.498   -39.541 1.00 23.93 ?  241 ARG B NH2 1 
ATOM   2544 N N   . PHE B 1 19  ? 13.953  8.412   -34.836 1.00 21.98 ?  242 PHE B N   1 
ATOM   2545 C CA  . PHE B 1 19  ? 13.411  7.177   -34.282 1.00 20.41 ?  242 PHE B CA  1 
ATOM   2546 C C   . PHE B 1 19  ? 12.545  7.554   -33.085 1.00 19.65 ?  242 PHE B C   1 
ATOM   2547 O O   . PHE B 1 19  ? 12.887  8.490   -32.350 1.00 23.55 ?  242 PHE B O   1 
ATOM   2548 C CB  . PHE B 1 19  ? 14.537  6.223   -33.875 1.00 21.15 ?  242 PHE B CB  1 
ATOM   2549 C CG  . PHE B 1 19  ? 14.167  4.766   -33.934 1.00 22.41 ?  242 PHE B CG  1 
ATOM   2550 C CD1 . PHE B 1 19  ? 14.218  4.071   -35.132 1.00 20.23 ?  242 PHE B CD1 1 
ATOM   2551 C CD2 . PHE B 1 19  ? 13.804  4.083   -32.785 1.00 21.65 ?  242 PHE B CD2 1 
ATOM   2552 C CE1 . PHE B 1 19  ? 13.890  2.728   -35.187 1.00 18.85 ?  242 PHE B CE1 1 
ATOM   2553 C CE2 . PHE B 1 19  ? 13.474  2.741   -32.832 1.00 21.65 ?  242 PHE B CE2 1 
ATOM   2554 C CZ  . PHE B 1 19  ? 13.518  2.062   -34.035 1.00 23.58 ?  242 PHE B CZ  1 
ATOM   2555 N N   . PRO B 1 20  ? 11.421  6.875   -32.856 1.00 20.94 ?  243 PRO B N   1 
ATOM   2556 C CA  . PRO B 1 20  ? 10.521  7.292   -31.756 1.00 21.09 ?  243 PRO B CA  1 
ATOM   2557 C C   . PRO B 1 20  ? 11.019  6.860   -30.380 1.00 22.29 ?  243 PRO B C   1 
ATOM   2558 O O   . PRO B 1 20  ? 10.450  5.994   -29.708 1.00 21.57 ?  243 PRO B O   1 
ATOM   2559 C CB  . PRO B 1 20  ? 9.198   6.621   -32.142 1.00 20.10 ?  243 PRO B CB  1 
ATOM   2560 C CG  . PRO B 1 20  ? 9.593   5.422   -32.932 1.00 21.13 ?  243 PRO B CG  1 
ATOM   2561 C CD  . PRO B 1 20  ? 10.875  5.753   -33.639 1.00 21.42 ?  243 PRO B CD  1 
ATOM   2562 N N   . ILE B 1 21  ? 12.106  7.485   -29.932 1.00 22.26 ?  244 ILE B N   1 
ATOM   2563 C CA  . ILE B 1 21  ? 12.679  7.205   -28.612 1.00 19.22 ?  244 ILE B CA  1 
ATOM   2564 C C   . ILE B 1 21  ? 13.170  8.503   -27.995 1.00 20.37 ?  244 ILE B C   1 
ATOM   2565 O O   . ILE B 1 21  ? 13.499  9.465   -28.700 1.00 21.16 ?  244 ILE B O   1 
ATOM   2566 C CB  . ILE B 1 21  ? 13.844  6.194   -28.697 1.00 19.67 ?  244 ILE B CB  1 
ATOM   2567 C CG1 . ILE B 1 21  ? 14.841  6.616   -29.776 1.00 21.51 ?  244 ILE B CG1 1 
ATOM   2568 C CG2 . ILE B 1 21  ? 13.321  4.782   -28.951 1.00 17.78 ?  244 ILE B CG2 1 
ATOM   2569 C CD1 . ILE B 1 21  ? 15.990  5.650   -29.953 1.00 19.64 ?  244 ILE B CD1 1 
ATOM   2570 N N   . PRO B 1 22  ? 13.220  8.559   -26.661 1.00 23.53 ?  245 PRO B N   1 
ATOM   2571 C CA  . PRO B 1 22  ? 13.642  9.802   -26.001 1.00 22.54 ?  245 PRO B CA  1 
ATOM   2572 C C   . PRO B 1 22  ? 15.106  10.122  -26.261 1.00 22.80 ?  245 PRO B C   1 
ATOM   2573 O O   . PRO B 1 22  ? 15.931  9.234   -26.489 1.00 22.92 ?  245 PRO B O   1 
ATOM   2574 C CB  . PRO B 1 22  ? 13.401  9.519   -24.511 1.00 18.44 ?  245 PRO B CB  1 
ATOM   2575 C CG  . PRO B 1 22  ? 12.521  8.317   -24.467 1.00 21.56 ?  245 PRO B CG  1 
ATOM   2576 C CD  . PRO B 1 22  ? 12.854  7.521   -25.683 1.00 21.16 ?  245 PRO B CD  1 
ATOM   2577 N N   . LEU B 1 23  ? 15.420  11.415  -26.229 1.00 20.50 ?  246 LEU B N   1 
ATOM   2578 C CA  . LEU B 1 23  ? 16.812  11.841  -26.238 1.00 22.22 ?  246 LEU B CA  1 
ATOM   2579 C C   . LEU B 1 23  ? 17.456  11.508  -24.898 1.00 23.31 ?  246 LEU B C   1 
ATOM   2580 O O   . LEU B 1 23  ? 16.810  11.575  -23.849 1.00 23.56 ?  246 LEU B O   1 
ATOM   2581 C CB  . LEU B 1 23  ? 16.915  13.342  -26.515 1.00 20.95 ?  246 LEU B CB  1 
ATOM   2582 C CG  . LEU B 1 23  ? 16.517  13.828  -27.910 1.00 22.31 ?  246 LEU B CG  1 
ATOM   2583 C CD1 . LEU B 1 23  ? 16.656  15.340  -28.007 1.00 18.49 ?  246 LEU B CD1 1 
ATOM   2584 C CD2 . LEU B 1 23  ? 17.360  13.145  -28.973 1.00 18.71 ?  246 LEU B CD2 1 
ATOM   2585 N N   . GLU B 1 24  ? 18.737  11.140  -24.933 1.00 22.66 ?  247 GLU B N   1 
ATOM   2586 C CA  . GLU B 1 24  ? 19.441  10.723  -23.729 1.00 21.38 ?  247 GLU B CA  1 
ATOM   2587 C C   . GLU B 1 24  ? 20.649  11.575  -23.379 1.00 21.82 ?  247 GLU B C   1 
ATOM   2588 O O   . GLU B 1 24  ? 21.075  11.548  -22.219 1.00 24.16 ?  247 GLU B O   1 
ATOM   2589 C CB  . GLU B 1 24  ? 19.905  9.263   -23.848 1.00 25.34 ?  247 GLU B CB  1 
ATOM   2590 C CG  . GLU B 1 24  ? 18.786  8.241   -23.792 1.00 27.67 ?  247 GLU B CG  1 
ATOM   2591 C CD  . GLU B 1 24  ? 19.137  6.964   -24.527 1.00 29.40 ?  247 GLU B CD  1 
ATOM   2592 O OE1 . GLU B 1 24  ? 20.337  6.620   -24.577 1.00 30.62 ?  247 GLU B OE1 1 
ATOM   2593 O OE2 . GLU B 1 24  ? 18.216  6.303   -25.050 1.00 29.29 ?  247 GLU B OE2 1 
ATOM   2594 N N   . LYS B 1 25  ? 21.218  12.309  -24.331 1.00 21.93 ?  248 LYS B N   1 
ATOM   2595 C CA  . LYS B 1 25  ? 22.422  13.093  -24.079 1.00 21.22 ?  248 LYS B CA  1 
ATOM   2596 C C   . LYS B 1 25  ? 22.714  13.952  -25.300 1.00 22.80 ?  248 LYS B C   1 
ATOM   2597 O O   . LYS B 1 25  ? 22.055  13.843  -26.338 1.00 23.94 ?  248 LYS B O   1 
ATOM   2598 C CB  . LYS B 1 25  ? 23.622  12.197  -23.759 1.00 21.97 ?  248 LYS B CB  1 
ATOM   2599 C CG  . LYS B 1 25  ? 23.772  11.001  -24.686 1.00 21.22 ?  248 LYS B CG  1 
ATOM   2600 C CD  . LYS B 1 25  ? 24.113  9.746   -23.902 1.00 24.34 ?  248 LYS B CD  1 
ATOM   2601 C CE  . LYS B 1 25  ? 24.588  8.630   -24.816 1.00 28.54 ?  248 LYS B CE  1 
ATOM   2602 N NZ  . LYS B 1 25  ? 24.703  7.335   -24.091 1.00 26.87 ?  248 LYS B NZ  1 
ATOM   2603 N N   . LEU B 1 26  ? 23.714  14.816  -25.155 1.00 20.94 ?  249 LEU B N   1 
ATOM   2604 C CA  . LEU B 1 26  ? 24.291  15.562  -26.260 1.00 19.84 ?  249 LEU B CA  1 
ATOM   2605 C C   . LEU B 1 26  ? 25.645  14.963  -26.614 1.00 21.04 ?  249 LEU B C   1 
ATOM   2606 O O   . LEU B 1 26  ? 26.311  14.351  -25.774 1.00 22.54 ?  249 LEU B O   1 
ATOM   2607 C CB  . LEU B 1 26  ? 24.445  17.046  -25.912 1.00 23.38 ?  249 LEU B CB  1 
ATOM   2608 C CG  . LEU B 1 26  ? 23.170  17.779  -25.485 1.00 24.26 ?  249 LEU B CG  1 
ATOM   2609 C CD1 . LEU B 1 26  ? 23.487  19.193  -25.020 1.00 20.84 ?  249 LEU B CD1 1 
ATOM   2610 C CD2 . LEU B 1 26  ? 22.151  17.798  -26.616 1.00 20.68 ?  249 LEU B CD2 1 
ATOM   2611 N N   . PHE B 1 27  ? 26.046  15.140  -27.870 1.00 22.29 ?  250 PHE B N   1 
ATOM   2612 C CA  . PHE B 1 27  ? 27.276  14.538  -28.365 1.00 22.22 ?  250 PHE B CA  1 
ATOM   2613 C C   . PHE B 1 27  ? 27.926  15.491  -29.353 1.00 23.69 ?  250 PHE B C   1 
ATOM   2614 O O   . PHE B 1 27  ? 27.251  16.026  -30.237 1.00 25.20 ?  250 PHE B O   1 
ATOM   2615 C CB  . PHE B 1 27  ? 26.989  13.178  -29.022 1.00 23.68 ?  250 PHE B CB  1 
ATOM   2616 C CG  . PHE B 1 27  ? 28.195  12.522  -29.645 1.00 26.28 ?  250 PHE B CG  1 
ATOM   2617 C CD1 . PHE B 1 27  ? 28.636  12.886  -30.910 1.00 24.80 ?  250 PHE B CD1 1 
ATOM   2618 C CD2 . PHE B 1 27  ? 28.881  11.528  -28.966 1.00 25.17 ?  250 PHE B CD2 1 
ATOM   2619 C CE1 . PHE B 1 27  ? 29.741  12.279  -31.478 1.00 25.07 ?  250 PHE B CE1 1 
ATOM   2620 C CE2 . PHE B 1 27  ? 29.984  10.916  -29.530 1.00 25.87 ?  250 PHE B CE2 1 
ATOM   2621 C CZ  . PHE B 1 27  ? 30.415  11.292  -30.787 1.00 24.87 ?  250 PHE B CZ  1 
ATOM   2622 N N   . THR B 1 28  ? 29.232  15.696  -29.201 1.00 22.75 ?  251 THR B N   1 
ATOM   2623 C CA  . THR B 1 28  ? 30.005  16.471  -30.157 1.00 23.91 ?  251 THR B CA  1 
ATOM   2624 C C   . THR B 1 28  ? 31.371  15.827  -30.337 1.00 27.06 ?  251 THR B C   1 
ATOM   2625 O O   . THR B 1 28  ? 31.946  15.285  -29.388 1.00 30.69 ?  251 THR B O   1 
ATOM   2626 C CB  . THR B 1 28  ? 30.159  17.937  -29.720 1.00 24.81 ?  251 THR B CB  1 
ATOM   2627 O OG1 . THR B 1 28  ? 30.966  18.639  -30.675 1.00 25.72 ?  251 THR B OG1 1 
ATOM   2628 C CG2 . THR B 1 28  ? 30.803  18.031  -28.345 1.00 26.87 ?  251 THR B CG2 1 
ATOM   2629 N N   . GLY B 1 29  ? 31.873  15.880  -31.565 1.00 26.44 ?  252 GLY B N   1 
ATOM   2630 C CA  . GLY B 1 29  ? 33.144  15.295  -31.914 1.00 31.05 ?  252 GLY B CA  1 
ATOM   2631 C C   . GLY B 1 29  ? 33.405  15.450  -33.397 1.00 33.59 ?  252 GLY B C   1 
ATOM   2632 O O   . GLY B 1 29  ? 32.578  15.990  -34.138 1.00 33.57 ?  252 GLY B O   1 
ATOM   2633 N N   . PRO B 1 30  ? 34.564  14.989  -33.863 1.00 35.01 ?  253 PRO B N   1 
ATOM   2634 C CA  . PRO B 1 30  ? 34.855  15.060  -35.302 1.00 33.83 ?  253 PRO B CA  1 
ATOM   2635 C C   . PRO B 1 30  ? 33.958  14.109  -36.084 1.00 33.23 ?  253 PRO B C   1 
ATOM   2636 O O   . PRO B 1 30  ? 33.791  12.945  -35.714 1.00 34.70 ?  253 PRO B O   1 
ATOM   2637 C CB  . PRO B 1 30  ? 36.330  14.651  -35.391 1.00 33.37 ?  253 PRO B CB  1 
ATOM   2638 C CG  . PRO B 1 30  ? 36.587  13.873  -34.139 1.00 38.82 ?  253 PRO B CG  1 
ATOM   2639 C CD  . PRO B 1 30  ? 35.707  14.477  -33.087 1.00 35.61 ?  253 PRO B CD  1 
ATOM   2640 N N   . SER B 1 31  ? 33.368  14.623  -37.168 1.00 37.67 ?  254 SER B N   1 
ATOM   2641 C CA  . SER B 1 31  ? 32.534  13.822  -38.057 1.00 36.80 ?  254 SER B CA  1 
ATOM   2642 C C   . SER B 1 31  ? 32.925  14.016  -39.518 1.00 37.64 ?  254 SER B C   1 
ATOM   2643 O O   . SER B 1 31  ? 32.126  13.722  -40.413 1.00 36.63 ?  254 SER B O   1 
ATOM   2644 C CB  . SER B 1 31  ? 31.051  14.150  -37.860 1.00 32.16 ?  254 SER B CB  1 
ATOM   2645 O OG  . SER B 1 31  ? 30.759  15.467  -38.295 1.00 31.34 ?  254 SER B OG  1 
ATOM   2646 N N   . SER B 1 32  ? 34.140  14.508  -39.772 1.00 37.79 ?  255 SER B N   1 
ATOM   2647 C CA  . SER B 1 32  ? 34.604  14.704  -41.140 1.00 35.48 ?  255 SER B CA  1 
ATOM   2648 C C   . SER B 1 32  ? 34.712  13.393  -41.905 1.00 37.81 ?  255 SER B C   1 
ATOM   2649 O O   . SER B 1 32  ? 34.719  13.407  -43.140 1.00 40.67 ?  255 SER B O   1 
ATOM   2650 C CB  . SER B 1 32  ? 35.958  15.419  -41.135 1.00 35.52 ?  255 SER B CB  1 
ATOM   2651 O OG  . SER B 1 32  ? 36.735  15.037  -40.012 1.00 41.59 ?  255 SER B OG  1 
ATOM   2652 N N   . ALA B 1 33  ? 34.797  12.263  -41.202 1.00 37.37 ?  256 ALA B N   1 
ATOM   2653 C CA  . ALA B 1 33  ? 34.885  10.974  -41.874 1.00 36.64 ?  256 ALA B CA  1 
ATOM   2654 C C   . ALA B 1 33  ? 33.549  10.535  -42.455 1.00 39.77 ?  256 ALA B C   1 
ATOM   2655 O O   . ALA B 1 33  ? 33.529  9.724   -43.388 1.00 40.24 ?  256 ALA B O   1 
ATOM   2656 C CB  . ALA B 1 33  ? 35.412  9.913   -40.907 1.00 34.69 ?  256 ALA B CB  1 
ATOM   2657 N N   . PHE B 1 34  ? 32.442  11.050  -41.935 1.00 39.43 ?  257 PHE B N   1 
ATOM   2658 C CA  . PHE B 1 34  ? 31.114  10.699  -42.411 1.00 35.53 ?  257 PHE B CA  1 
ATOM   2659 C C   . PHE B 1 34  ? 30.552  11.798  -43.304 1.00 33.91 ?  257 PHE B C   1 
ATOM   2660 O O   . PHE B 1 34  ? 31.033  12.934  -43.320 1.00 36.38 ?  257 PHE B O   1 
ATOM   2661 C CB  . PHE B 1 34  ? 30.155  10.465  -41.240 1.00 32.29 ?  257 PHE B CB  1 
ATOM   2662 C CG  . PHE B 1 34  ? 30.560  9.344   -40.328 1.00 35.47 ?  257 PHE B CG  1 
ATOM   2663 C CD1 . PHE B 1 34  ? 30.427  8.023   -40.726 1.00 36.12 ?  257 PHE B CD1 1 
ATOM   2664 C CD2 . PHE B 1 34  ? 31.056  9.612   -39.063 1.00 36.87 ?  257 PHE B CD2 1 
ATOM   2665 C CE1 . PHE B 1 34  ? 30.793  6.991   -39.881 1.00 34.68 ?  257 PHE B CE1 1 
ATOM   2666 C CE2 . PHE B 1 34  ? 31.423  8.585   -38.214 1.00 33.80 ?  257 PHE B CE2 1 
ATOM   2667 C CZ  . PHE B 1 34  ? 31.292  7.273   -38.623 1.00 35.74 ?  257 PHE B CZ  1 
ATOM   2668 N N   . VAL B 1 35  ? 29.520  11.435  -44.055 1.00 33.10 ?  258 VAL B N   1 
ATOM   2669 C CA  . VAL B 1 35  ? 28.647  12.392  -44.721 1.00 30.74 ?  258 VAL B CA  1 
ATOM   2670 C C   . VAL B 1 35  ? 27.387  12.484  -43.875 1.00 28.29 ?  258 VAL B C   1 
ATOM   2671 O O   . VAL B 1 35  ? 26.595  11.537  -43.816 1.00 26.74 ?  258 VAL B O   1 
ATOM   2672 C CB  . VAL B 1 35  ? 28.327  11.975  -46.162 1.00 36.04 ?  258 VAL B CB  1 
ATOM   2673 C CG1 . VAL B 1 35  ? 27.625  13.109  -46.897 1.00 32.57 ?  258 VAL B CG1 1 
ATOM   2674 C CG2 . VAL B 1 35  ? 29.597  11.566  -46.888 1.00 35.91 ?  258 VAL B CG2 1 
ATOM   2675 N N   . VAL B 1 36  ? 27.205  13.616  -43.201 1.00 25.38 ?  259 VAL B N   1 
ATOM   2676 C CA  . VAL B 1 36  ? 26.092  13.805  -42.279 1.00 24.05 ?  259 VAL B CA  1 
ATOM   2677 C C   . VAL B 1 36  ? 24.938  14.398  -43.079 1.00 23.90 ?  259 VAL B C   1 
ATOM   2678 O O   . VAL B 1 36  ? 24.853  15.612  -43.266 1.00 26.64 ?  259 VAL B O   1 
ATOM   2679 C CB  . VAL B 1 36  ? 26.481  14.696  -41.100 1.00 25.46 ?  259 VAL B CB  1 
ATOM   2680 C CG1 . VAL B 1 36  ? 25.317  14.832  -40.135 1.00 22.17 ?  259 VAL B CG1 1 
ATOM   2681 C CG2 . VAL B 1 36  ? 27.704  14.128  -40.402 1.00 24.41 ?  259 VAL B CG2 1 
ATOM   2682 N N   . GLN B 1 37  ? 24.037  13.534  -43.546 1.00 23.98 ?  260 GLN B N   1 
ATOM   2683 C CA  . GLN B 1 37  ? 22.907  13.951  -44.379 1.00 20.72 ?  260 GLN B CA  1 
ATOM   2684 C C   . GLN B 1 37  ? 21.648  13.170  -44.011 1.00 23.11 ?  260 GLN B C   1 
ATOM   2685 O O   . GLN B 1 37  ? 21.059  12.485  -44.853 1.00 22.47 ?  260 GLN B O   1 
ATOM   2686 C CB  . GLN B 1 37  ? 23.250  13.762  -45.857 1.00 21.67 ?  260 GLN B CB  1 
ATOM   2687 C CG  . GLN B 1 37  ? 22.457  14.626  -46.816 1.00 25.13 ?  260 GLN B CG  1 
ATOM   2688 C CD  . GLN B 1 37  ? 23.032  14.598  -48.220 1.00 25.22 ?  260 GLN B CD  1 
ATOM   2689 O OE1 . GLN B 1 37  ? 24.115  14.057  -48.448 1.00 27.15 ?  260 GLN B OE1 1 
ATOM   2690 N NE2 . GLN B 1 37  ? 22.308  15.180  -49.169 1.00 21.24 ?  260 GLN B NE2 1 
ATOM   2691 N N   . PRO B 1 38  ? 21.190  13.262  -42.759 1.00 21.37 ?  261 PRO B N   1 
ATOM   2692 C CA  . PRO B 1 38  ? 19.921  12.614  -42.413 1.00 18.54 ?  261 PRO B CA  1 
ATOM   2693 C C   . PRO B 1 38  ? 18.754  13.340  -43.061 1.00 17.76 ?  261 PRO B C   1 
ATOM   2694 O O   . PRO B 1 38  ? 18.816  14.539  -43.342 1.00 16.24 ?  261 PRO B O   1 
ATOM   2695 C CB  . PRO B 1 38  ? 19.871  12.724  -40.886 1.00 18.17 ?  261 PRO B CB  1 
ATOM   2696 C CG  . PRO B 1 38  ? 20.628  13.964  -40.601 1.00 16.64 ?  261 PRO B CG  1 
ATOM   2697 C CD  . PRO B 1 38  ? 21.764  13.963  -41.595 1.00 17.53 ?  261 PRO B CD  1 
ATOM   2698 N N   . GLN B 1 39  ? 17.683  12.592  -43.317 1.00 18.97 ?  262 GLN B N   1 
ATOM   2699 C CA  . GLN B 1 39  ? 16.506  13.160  -43.958 1.00 20.45 ?  262 GLN B CA  1 
ATOM   2700 C C   . GLN B 1 39  ? 15.355  13.403  -42.994 1.00 21.62 ?  262 GLN B C   1 
ATOM   2701 O O   . GLN B 1 39  ? 14.435  14.157  -43.331 1.00 18.52 ?  262 GLN B O   1 
ATOM   2702 C CB  . GLN B 1 39  ? 16.033  12.254  -45.102 1.00 19.06 ?  262 GLN B CB  1 
ATOM   2703 C CG  . GLN B 1 39  ? 17.071  12.073  -46.195 1.00 18.28 ?  262 GLN B CG  1 
ATOM   2704 C CD  . GLN B 1 39  ? 17.514  13.395  -46.796 1.00 21.88 ?  262 GLN B CD  1 
ATOM   2705 O OE1 . GLN B 1 39  ? 16.703  14.147  -47.334 1.00 24.78 ?  262 GLN B OE1 1 
ATOM   2706 N NE2 . GLN B 1 39  ? 18.807  13.685  -46.703 1.00 21.34 ?  262 GLN B NE2 1 
ATOM   2707 N N   . ASN B 1 40  ? 15.382  12.790  -41.818 1.00 19.45 ?  263 ASN B N   1 
ATOM   2708 C CA  . ASN B 1 40  ? 14.400  13.054  -40.780 1.00 18.94 ?  263 ASN B CA  1 
ATOM   2709 C C   . ASN B 1 40  ? 14.987  14.014  -39.753 1.00 20.24 ?  263 ASN B C   1 
ATOM   2710 O O   . ASN B 1 40  ? 16.203  14.068  -39.549 1.00 19.93 ?  263 ASN B O   1 
ATOM   2711 C CB  . ASN B 1 40  ? 13.955  11.756  -40.103 1.00 20.11 ?  263 ASN B CB  1 
ATOM   2712 C CG  . ASN B 1 40  ? 13.067  10.910  -40.996 1.00 18.12 ?  263 ASN B CG  1 
ATOM   2713 O OD1 . ASN B 1 40  ? 12.192  11.427  -41.691 1.00 18.56 ?  263 ASN B OD1 1 
ATOM   2714 N ND2 . ASN B 1 40  ? 13.292  9.601   -40.985 1.00 16.54 ?  263 ASN B ND2 1 
ATOM   2715 N N   . GLY B 1 41  ? 14.110  14.777  -39.112 1.00 19.23 ?  264 GLY B N   1 
ATOM   2716 C CA  . GLY B 1 41  ? 14.566  15.834  -38.227 1.00 19.36 ?  264 GLY B CA  1 
ATOM   2717 C C   . GLY B 1 41  ? 15.240  16.967  -38.968 1.00 19.04 ?  264 GLY B C   1 
ATOM   2718 O O   . GLY B 1 41  ? 16.227  17.527  -38.475 1.00 20.36 ?  264 GLY B O   1 
ATOM   2719 N N   . ARG B 1 42  ? 14.734  17.313  -40.149 1.00 17.85 ?  265 ARG B N   1 
ATOM   2720 C CA  . ARG B 1 42  ? 15.295  18.373  -40.977 1.00 20.19 ?  265 ARG B CA  1 
ATOM   2721 C C   . ARG B 1 42  ? 14.277  19.498  -41.078 1.00 21.67 ?  265 ARG B C   1 
ATOM   2722 O O   . ARG B 1 42  ? 13.189  19.309  -41.633 1.00 20.32 ?  265 ARG B O   1 
ATOM   2723 C CB  . ARG B 1 42  ? 15.666  17.847  -42.365 1.00 20.04 ?  265 ARG B CB  1 
ATOM   2724 C CG  . ARG B 1 42  ? 16.740  16.772  -42.345 1.00 19.27 ?  265 ARG B CG  1 
ATOM   2725 C CD  . ARG B 1 42  ? 17.981  17.245  -41.603 1.00 17.89 ?  265 ARG B CD  1 
ATOM   2726 N NE  . ARG B 1 42  ? 18.644  18.343  -42.296 1.00 22.44 ?  265 ARG B NE  1 
ATOM   2727 C CZ  . ARG B 1 42  ? 19.604  18.189  -43.197 1.00 21.98 ?  265 ARG B CZ  1 
ATOM   2728 N NH1 . ARG B 1 42  ? 20.047  16.990  -43.538 1.00 18.37 ?  265 ARG B NH1 1 
ATOM   2729 N NH2 . ARG B 1 42  ? 20.134  19.266  -43.771 1.00 22.78 ?  265 ARG B NH2 1 
ATOM   2730 N N   . CYS B 1 43  ? 14.633  20.662  -40.544 1.00 22.40 ?  266 CYS B N   1 
ATOM   2731 C CA  . CYS B 1 43  ? 13.724  21.797  -40.490 1.00 21.89 ?  266 CYS B CA  1 
ATOM   2732 C C   . CYS B 1 43  ? 14.542  23.067  -40.325 1.00 23.71 ?  266 CYS B C   1 
ATOM   2733 O O   . CYS B 1 43  ? 15.492  23.098  -39.540 1.00 23.33 ?  266 CYS B O   1 
ATOM   2734 C CB  . CYS B 1 43  ? 12.726  21.652  -39.333 1.00 19.95 ?  266 CYS B CB  1 
ATOM   2735 S SG  . CYS B 1 43  ? 11.399  22.880  -39.305 1.00 25.04 ?  266 CYS B SG  1 
ATOM   2736 N N   . THR B 1 44  ? 14.175  24.103  -41.073 1.00 23.36 ?  267 THR B N   1 
ATOM   2737 C CA  . THR B 1 44  ? 14.812  25.396  -40.894 1.00 23.79 ?  267 THR B CA  1 
ATOM   2738 C C   . THR B 1 44  ? 14.202  26.119  -39.697 1.00 25.55 ?  267 THR B C   1 
ATOM   2739 O O   . THR B 1 44  ? 13.131  25.759  -39.200 1.00 24.36 ?  267 THR B O   1 
ATOM   2740 C CB  . THR B 1 44  ? 14.676  26.252  -42.152 1.00 25.68 ?  267 THR B CB  1 
ATOM   2741 O OG1 . THR B 1 44  ? 13.380  26.862  -42.182 1.00 24.67 ?  267 THR B OG1 1 
ATOM   2742 C CG2 . THR B 1 44  ? 14.862  25.400  -43.396 1.00 23.30 ?  267 THR B CG2 1 
ATOM   2743 N N   . THR B 1 45  ? 14.904  27.154  -39.232 1.00 23.71 ?  268 THR B N   1 
ATOM   2744 C CA  . THR B 1 45  ? 14.463  27.854  -38.032 1.00 23.79 ?  268 THR B CA  1 
ATOM   2745 C C   . THR B 1 45  ? 13.164  28.620  -38.246 1.00 24.26 ?  268 THR B C   1 
ATOM   2746 O O   . THR B 1 45  ? 12.449  28.877  -37.271 1.00 23.09 ?  268 THR B O   1 
ATOM   2747 C CB  . THR B 1 45  ? 15.555  28.805  -37.533 1.00 24.67 ?  268 THR B CB  1 
ATOM   2748 O OG1 . THR B 1 45  ? 15.828  29.796  -38.531 1.00 30.02 ?  268 THR B OG1 1 
ATOM   2749 C CG2 . THR B 1 45  ? 16.830  28.035  -37.212 1.00 24.38 ?  268 THR B CG2 1 
ATOM   2750 N N   . ASP B 1 46  ? 12.836  28.986  -39.484 1.00 27.20 ?  269 ASP B N   1 
ATOM   2751 C CA  . ASP B 1 46  ? 11.555  29.615  -39.775 1.00 28.76 ?  269 ASP B CA  1 
ATOM   2752 C C   . ASP B 1 46  ? 10.480  28.605  -40.164 1.00 28.64 ?  269 ASP B C   1 
ATOM   2753 O O   . ASP B 1 46  ? 9.420   29.004  -40.656 1.00 29.07 ?  269 ASP B O   1 
ATOM   2754 C CB  . ASP B 1 46  ? 11.711  30.682  -40.866 1.00 29.06 ?  269 ASP B CB  1 
ATOM   2755 C CG  . ASP B 1 46  ? 12.356  30.151  -42.133 1.00 34.72 ?  269 ASP B CG  1 
ATOM   2756 O OD1 . ASP B 1 46  ? 12.497  28.918  -42.274 1.00 31.43 ?  269 ASP B OD1 1 
ATOM   2757 O OD2 . ASP B 1 46  ? 12.719  30.978  -42.996 1.00 33.91 ?  269 ASP B OD2 1 
ATOM   2758 N N   . GLY B 1 47  ? 10.738  27.314  -39.969 1.00 26.00 ?  270 GLY B N   1 
ATOM   2759 C CA  . GLY B 1 47  ? 9.688   26.318  -40.016 1.00 26.22 ?  270 GLY B CA  1 
ATOM   2760 C C   . GLY B 1 47  ? 9.416   25.674  -41.354 1.00 26.48 ?  270 GLY B C   1 
ATOM   2761 O O   . GLY B 1 47  ? 8.275   25.273  -41.611 1.00 26.17 ?  270 GLY B O   1 
ATOM   2762 N N   . VAL B 1 48  ? 10.420  25.549  -42.215 1.00 26.67 ?  271 VAL B N   1 
ATOM   2763 C CA  . VAL B 1 48  ? 10.269  24.871  -43.497 1.00 25.49 ?  271 VAL B CA  1 
ATOM   2764 C C   . VAL B 1 48  ? 10.793  23.450  -43.346 1.00 22.97 ?  271 VAL B C   1 
ATOM   2765 O O   . VAL B 1 48  ? 11.988  23.243  -43.102 1.00 21.58 ?  271 VAL B O   1 
ATOM   2766 C CB  . VAL B 1 48  ? 11.003  25.616  -44.623 1.00 28.57 ?  271 VAL B CB  1 
ATOM   2767 C CG1 . VAL B 1 48  ? 10.971  24.796  -45.904 1.00 23.18 ?  271 VAL B CG1 1 
ATOM   2768 C CG2 . VAL B 1 48  ? 10.379  26.986  -44.846 1.00 26.07 ?  271 VAL B CG2 1 
ATOM   2769 N N   . LEU B 1 49  ? 9.901   22.472  -43.486 1.00 21.85 ?  272 LEU B N   1 
ATOM   2770 C CA  . LEU B 1 49  ? 10.293  21.075  -43.381 1.00 21.11 ?  272 LEU B CA  1 
ATOM   2771 C C   . LEU B 1 49  ? 11.102  20.649  -44.602 1.00 22.76 ?  272 LEU B C   1 
ATOM   2772 O O   . LEU B 1 49  ? 10.851  21.088  -45.728 1.00 22.91 ?  272 LEU B O   1 
ATOM   2773 C CB  . LEU B 1 49  ? 9.063   20.180  -43.234 1.00 20.17 ?  272 LEU B CB  1 
ATOM   2774 C CG  . LEU B 1 49  ? 8.133   20.460  -42.050 1.00 23.81 ?  272 LEU B CG  1 
ATOM   2775 C CD1 . LEU B 1 49  ? 6.955   19.497  -42.052 1.00 20.66 ?  272 LEU B CD1 1 
ATOM   2776 C CD2 . LEU B 1 49  ? 8.886   20.391  -40.729 1.00 19.80 ?  272 LEU B CD2 1 
ATOM   2777 N N   . LEU B 1 50  ? 12.077  19.774  -44.366 1.00 17.68 ?  273 LEU B N   1 
ATOM   2778 C CA  . LEU B 1 50  ? 12.989  19.315  -45.401 1.00 16.83 ?  273 LEU B CA  1 
ATOM   2779 C C   . LEU B 1 50  ? 13.044  17.793  -45.405 1.00 21.12 ?  273 LEU B C   1 
ATOM   2780 O O   . LEU B 1 50  ? 12.574  17.127  -44.478 1.00 21.80 ?  273 LEU B O   1 
ATOM   2781 C CB  . LEU B 1 50  ? 14.395  19.896  -45.199 1.00 19.91 ?  273 LEU B CB  1 
ATOM   2782 C CG  . LEU B 1 50  ? 14.491  21.421  -45.115 1.00 22.83 ?  273 LEU B CG  1 
ATOM   2783 C CD1 . LEU B 1 50  ? 15.766  21.840  -44.402 1.00 19.73 ?  273 LEU B CD1 1 
ATOM   2784 C CD2 . LEU B 1 50  ? 14.415  22.045  -46.502 1.00 22.28 ?  273 LEU B CD2 1 
ATOM   2785 N N   . GLY B 1 51  ? 13.628  17.251  -46.473 1.00 18.52 ?  274 GLY B N   1 
ATOM   2786 C CA  . GLY B 1 51  ? 13.835  15.813  -46.567 1.00 20.41 ?  274 GLY B CA  1 
ATOM   2787 C C   . GLY B 1 51  ? 12.530  15.046  -46.498 1.00 21.26 ?  274 GLY B C   1 
ATOM   2788 O O   . GLY B 1 51  ? 11.573  15.329  -47.227 1.00 21.15 ?  274 GLY B O   1 
ATOM   2789 N N   . THR B 1 52  ? 12.491  14.051  -45.612 1.00 19.68 ?  275 THR B N   1 
ATOM   2790 C CA  . THR B 1 52  ? 11.288  13.272  -45.350 1.00 19.81 ?  275 THR B CA  1 
ATOM   2791 C C   . THR B 1 52  ? 10.681  13.602  -43.992 1.00 19.42 ?  275 THR B C   1 
ATOM   2792 O O   . THR B 1 52  ? 9.943   12.787  -43.429 1.00 20.69 ?  275 THR B O   1 
ATOM   2793 C CB  . THR B 1 52  ? 11.591  11.776  -45.437 1.00 20.31 ?  275 THR B CB  1 
ATOM   2794 O OG1 . THR B 1 52  ? 12.448  11.399  -44.351 1.00 19.35 ?  275 THR B OG1 1 
ATOM   2795 C CG2 . THR B 1 52  ? 12.275  11.444  -46.753 1.00 16.50 ?  275 THR B CG2 1 
ATOM   2796 N N   . THR B 1 53  ? 10.976  14.784  -43.457 1.00 21.71 ?  276 THR B N   1 
ATOM   2797 C CA  . THR B 1 53  ? 10.605  15.124  -42.091 1.00 23.78 ?  276 THR B CA  1 
ATOM   2798 C C   . THR B 1 53  ? 9.132   15.505  -42.004 1.00 23.70 ?  276 THR B C   1 
ATOM   2799 O O   . THR B 1 53  ? 8.659   16.371  -42.747 1.00 23.37 ?  276 THR B O   1 
ATOM   2800 C CB  . THR B 1 53  ? 11.472  16.274  -41.578 1.00 20.79 ?  276 THR B CB  1 
ATOM   2801 O OG1 . THR B 1 53  ? 12.852  15.892  -41.626 1.00 20.04 ?  276 THR B OG1 1 
ATOM   2802 C CG2 . THR B 1 53  ? 11.097  16.630  -40.147 1.00 18.85 ?  276 THR B CG2 1 
ATOM   2803 N N   . GLN B 1 54  ? 8.413   14.858  -41.094 1.00 22.82 ?  277 GLN B N   1 
ATOM   2804 C CA  . GLN B 1 54  ? 7.037   15.205  -40.771 1.00 22.38 ?  277 GLN B CA  1 
ATOM   2805 C C   . GLN B 1 54  ? 6.957   15.586  -39.291 1.00 22.41 ?  277 GLN B C   1 
ATOM   2806 O O   . GLN B 1 54  ? 7.974   15.688  -38.598 1.00 20.52 ?  277 GLN B O   1 
ATOM   2807 C CB  . GLN B 1 54  ? 6.091   14.058  -41.136 1.00 21.80 ?  277 GLN B CB  1 
ATOM   2808 C CG  . GLN B 1 54  ? 6.590   12.681  -40.740 1.00 20.49 ?  277 GLN B CG  1 
ATOM   2809 C CD  . GLN B 1 54  ? 6.288   12.350  -39.295 1.00 21.90 ?  277 GLN B CD  1 
ATOM   2810 O OE1 . GLN B 1 54  ? 5.129   12.322  -38.883 1.00 19.08 ?  277 GLN B OE1 1 
ATOM   2811 N NE2 . GLN B 1 54  ? 7.332   12.092  -38.516 1.00 23.98 ?  277 GLN B NE2 1 
ATOM   2812 N N   . LEU B 1 55  ? 5.733   15.787  -38.803 1.00 21.71 ?  278 LEU B N   1 
ATOM   2813 C CA  . LEU B 1 55  ? 5.525   16.428  -37.512 1.00 23.28 ?  278 LEU B CA  1 
ATOM   2814 C C   . LEU B 1 55  ? 5.271   15.459  -36.365 1.00 25.21 ?  278 LEU B C   1 
ATOM   2815 O O   . LEU B 1 55  ? 5.422   15.852  -35.203 1.00 21.11 ?  278 LEU B O   1 
ATOM   2816 C CB  . LEU B 1 55  ? 4.353   17.410  -37.605 1.00 21.68 ?  278 LEU B CB  1 
ATOM   2817 C CG  . LEU B 1 55  ? 4.619   18.600  -38.528 1.00 23.84 ?  278 LEU B CG  1 
ATOM   2818 C CD1 . LEU B 1 55  ? 3.326   19.304  -38.894 1.00 26.68 ?  278 LEU B CD1 1 
ATOM   2819 C CD2 . LEU B 1 55  ? 5.595   19.568  -37.879 1.00 26.70 ?  278 LEU B CD2 1 
ATOM   2820 N N   . SER B 1 56  ? 4.896   14.218  -36.648 1.00 24.74 ?  279 SER B N   1 
ATOM   2821 C CA  . SER B 1 56  ? 4.569   13.318  -35.550 1.00 20.17 ?  279 SER B CA  1 
ATOM   2822 C C   . SER B 1 56  ? 5.840   12.702  -34.965 1.00 21.46 ?  279 SER B C   1 
ATOM   2823 O O   . SER B 1 56  ? 6.747   12.321  -35.710 1.00 21.66 ?  279 SER B O   1 
ATOM   2824 C CB  . SER B 1 56  ? 3.631   12.212  -36.023 1.00 20.60 ?  279 SER B CB  1 
ATOM   2825 O OG  . SER B 1 56  ? 3.607   11.142  -35.096 1.00 21.78 ?  279 SER B OG  1 
ATOM   2826 N N   . PRO B 1 57  ? 5.932   12.597  -33.635 1.00 21.94 ?  280 PRO B N   1 
ATOM   2827 C CA  . PRO B 1 57  ? 7.086   11.917  -33.034 1.00 21.01 ?  280 PRO B CA  1 
ATOM   2828 C C   . PRO B 1 57  ? 6.965   10.405  -33.038 1.00 21.00 ?  280 PRO B C   1 
ATOM   2829 O O   . PRO B 1 57  ? 7.976   9.721   -32.829 1.00 22.11 ?  280 PRO B O   1 
ATOM   2830 C CB  . PRO B 1 57  ? 7.109   12.463  -31.600 1.00 18.56 ?  280 PRO B CB  1 
ATOM   2831 C CG  . PRO B 1 57  ? 5.683   12.828  -31.311 1.00 19.10 ?  280 PRO B CG  1 
ATOM   2832 C CD  . PRO B 1 57  ? 4.970   13.068  -32.623 1.00 20.30 ?  280 PRO B CD  1 
ATOM   2833 N N   . VAL B 1 58  ? 5.767   9.863   -33.268 1.00 18.72 ?  281 VAL B N   1 
ATOM   2834 C CA  . VAL B 1 58  ? 5.567   8.417   -33.279 1.00 21.00 ?  281 VAL B CA  1 
ATOM   2835 C C   . VAL B 1 58  ? 5.489   7.843   -34.687 1.00 24.10 ?  281 VAL B C   1 
ATOM   2836 O O   . VAL B 1 58  ? 5.583   6.614   -34.846 1.00 26.07 ?  281 VAL B O   1 
ATOM   2837 C CB  . VAL B 1 58  ? 4.303   8.025   -32.483 1.00 22.77 ?  281 VAL B CB  1 
ATOM   2838 C CG1 . VAL B 1 58  ? 4.551   8.180   -30.989 1.00 22.62 ?  281 VAL B CG1 1 
ATOM   2839 C CG2 . VAL B 1 58  ? 3.115   8.866   -32.919 1.00 19.73 ?  281 VAL B CG2 1 
ATOM   2840 N N   . ASN B 1 59  ? 5.320   8.680   -35.709 1.00 23.28 ?  282 ASN B N   1 
ATOM   2841 C CA  . ASN B 1 59  ? 5.301   8.225   -37.100 1.00 23.52 ?  282 ASN B CA  1 
ATOM   2842 C C   . ASN B 1 59  ? 6.669   8.314   -37.755 1.00 24.68 ?  282 ASN B C   1 
ATOM   2843 O O   . ASN B 1 59  ? 6.787   8.708   -38.919 1.00 28.26 ?  282 ASN B O   1 
ATOM   2844 C CB  . ASN B 1 59  ? 4.269   9.015   -37.898 1.00 23.56 ?  282 ASN B CB  1 
ATOM   2845 C CG  . ASN B 1 59  ? 2.848   8.596   -37.588 1.00 24.96 ?  282 ASN B CG  1 
ATOM   2846 O OD1 . ASN B 1 59  ? 2.617   7.565   -36.953 1.00 26.77 ?  282 ASN B OD1 1 
ATOM   2847 N ND2 . ASN B 1 59  ? 1.885   9.385   -38.049 1.00 27.42 ?  282 ASN B ND2 1 
ATOM   2848 N N   . ILE B 1 60  ? 7.723   7.964   -37.026 1.00 22.16 ?  283 ILE B N   1 
ATOM   2849 C CA  . ILE B 1 60  ? 9.074   7.896   -37.567 1.00 24.24 ?  283 ILE B CA  1 
ATOM   2850 C C   . ILE B 1 60  ? 9.449   6.426   -37.662 1.00 24.73 ?  283 ILE B C   1 
ATOM   2851 O O   . ILE B 1 60  ? 9.361   5.691   -36.669 1.00 27.15 ?  283 ILE B O   1 
ATOM   2852 C CB  . ILE B 1 60  ? 10.075  8.675   -36.703 1.00 25.00 ?  283 ILE B CB  1 
ATOM   2853 C CG1 . ILE B 1 60  ? 9.576   10.104  -36.478 1.00 25.35 ?  283 ILE B CG1 1 
ATOM   2854 C CG2 . ILE B 1 60  ? 11.444  8.688   -37.364 1.00 23.20 ?  283 ILE B CG2 1 
ATOM   2855 C CD1 . ILE B 1 60  ? 10.512  10.947  -35.651 1.00 22.80 ?  283 ILE B CD1 1 
ATOM   2856 N N   . CYS B 1 61  ? 9.851   6.001   -38.861 1.00 23.77 ?  284 CYS B N   1 
ATOM   2857 C CA  . CYS B 1 61  ? 10.151  4.604   -39.173 1.00 22.34 ?  284 CYS B CA  1 
ATOM   2858 C C   . CYS B 1 61  ? 8.917   3.711   -39.062 1.00 23.09 ?  284 CYS B C   1 
ATOM   2859 O O   . CYS B 1 61  ? 9.035   2.511   -38.804 1.00 24.06 ?  284 CYS B O   1 
ATOM   2860 C CB  . CYS B 1 61  ? 11.282  4.057   -38.295 1.00 24.53 ?  284 CYS B CB  1 
ATOM   2861 S SG  . CYS B 1 61  ? 12.872  4.867   -38.560 1.00 25.27 ?  284 CYS B SG  1 
ATOM   2862 N N   . THR B 1 62  ? 7.729   4.285   -39.248 1.00 22.23 ?  285 THR B N   1 
ATOM   2863 C CA  . THR B 1 62  ? 6.490   3.528   -39.360 1.00 22.92 ?  285 THR B CA  1 
ATOM   2864 C C   . THR B 1 62  ? 6.085   3.426   -40.825 1.00 25.10 ?  285 THR B C   1 
ATOM   2865 O O   . THR B 1 62  ? 6.447   4.271   -41.647 1.00 23.80 ?  285 THR B O   1 
ATOM   2866 C CB  . THR B 1 62  ? 5.351   4.182   -38.568 1.00 24.51 ?  285 THR B CB  1 
ATOM   2867 O OG1 . THR B 1 62  ? 5.191   5.542   -38.991 1.00 26.97 ?  285 THR B OG1 1 
ATOM   2868 C CG2 . THR B 1 62  ? 5.629   4.157   -37.078 1.00 22.40 ?  285 THR B CG2 1 
ATOM   2869 N N   . PHE B 1 63  ? 5.323   2.383   -41.145 1.00 25.15 ?  286 PHE B N   1 
ATOM   2870 C CA  . PHE B 1 63  ? 4.776   2.200   -42.481 1.00 21.25 ?  286 PHE B CA  1 
ATOM   2871 C C   . PHE B 1 63  ? 3.300   1.848   -42.382 1.00 23.25 ?  286 PHE B C   1 
ATOM   2872 O O   . PHE B 1 63  ? 2.865   1.191   -41.432 1.00 22.09 ?  286 PHE B O   1 
ATOM   2873 C CB  . PHE B 1 63  ? 5.518   1.106   -43.262 1.00 22.41 ?  286 PHE B CB  1 
ATOM   2874 C CG  . PHE B 1 63  ? 6.976   1.391   -43.475 1.00 24.08 ?  286 PHE B CG  1 
ATOM   2875 C CD1 . PHE B 1 63  ? 7.386   2.255   -44.477 1.00 26.12 ?  286 PHE B CD1 1 
ATOM   2876 C CD2 . PHE B 1 63  ? 7.937   0.783   -42.686 1.00 25.05 ?  286 PHE B CD2 1 
ATOM   2877 C CE1 . PHE B 1 63  ? 8.727   2.515   -44.681 1.00 25.18 ?  286 PHE B CE1 1 
ATOM   2878 C CE2 . PHE B 1 63  ? 9.280   1.039   -42.885 1.00 25.53 ?  286 PHE B CE2 1 
ATOM   2879 C CZ  . PHE B 1 63  ? 9.675   1.905   -43.884 1.00 23.81 ?  286 PHE B CZ  1 
ATOM   2880 N N   . ARG B 1 64  ? 2.530   2.296   -43.372 1.00 20.96 ?  287 ARG B N   1 
ATOM   2881 C CA  . ARG B 1 64  ? 1.097   2.044   -43.419 1.00 22.17 ?  287 ARG B CA  1 
ATOM   2882 C C   . ARG B 1 64  ? 0.680   1.723   -44.845 1.00 21.50 ?  287 ARG B C   1 
ATOM   2883 O O   . ARG B 1 64  ? 1.223   2.284   -45.801 1.00 21.16 ?  287 ARG B O   1 
ATOM   2884 C CB  . ARG B 1 64  ? 0.294   3.246   -42.903 1.00 23.14 ?  287 ARG B CB  1 
ATOM   2885 C CG  . ARG B 1 64  ? 0.529   3.570   -41.440 1.00 23.13 ?  287 ARG B CG  1 
ATOM   2886 C CD  . ARG B 1 64  ? -0.154  4.867   -41.048 1.00 20.74 ?  287 ARG B CD  1 
ATOM   2887 N NE  . ARG B 1 64  ? -0.434  4.918   -39.619 1.00 22.69 ?  287 ARG B NE  1 
ATOM   2888 C CZ  . ARG B 1 64  ? 0.466   5.214   -38.691 1.00 26.34 ?  287 ARG B CZ  1 
ATOM   2889 N NH1 . ARG B 1 64  ? 1.717   5.503   -39.008 1.00 22.74 ?  287 ARG B NH1 1 
ATOM   2890 N NH2 . ARG B 1 64  ? 0.101   5.220   -37.412 1.00 25.77 ?  287 ARG B NH2 1 
ATOM   2891 N N   . GLY B 1 65  ? -0.287  0.826   -44.979 1.00 22.13 ?  288 GLY B N   1 
ATOM   2892 C CA  . GLY B 1 65  ? -0.810  0.453   -46.285 1.00 20.77 ?  288 GLY B CA  1 
ATOM   2893 C C   . GLY B 1 65  ? -1.462  -0.920  -46.226 1.00 21.88 ?  288 GLY B C   1 
ATOM   2894 O O   . GLY B 1 65  ? -1.995  -1.323  -45.192 1.00 22.99 ?  288 GLY B O   1 
ATOM   2895 N N   . ASP B 1 66  ? -1.414  -1.612  -47.361 1.00 21.85 ?  289 ASP B N   1 
ATOM   2896 C CA  . ASP B 1 66  ? -1.879  -2.985  -47.473 1.00 23.72 ?  289 ASP B CA  1 
ATOM   2897 C C   . ASP B 1 66  ? -0.721  -3.866  -47.921 1.00 23.33 ?  289 ASP B C   1 
ATOM   2898 O O   . ASP B 1 66  ? 0.283   -3.382  -48.449 1.00 24.06 ?  289 ASP B O   1 
ATOM   2899 C CB  . ASP B 1 66  ? -3.057  -3.100  -48.452 1.00 24.45 ?  289 ASP B CB  1 
ATOM   2900 C CG  . ASP B 1 66  ? -2.730  -2.554  -49.828 1.00 22.98 ?  289 ASP B CG  1 
ATOM   2901 O OD1 . ASP B 1 66  ? -2.007  -3.234  -50.586 1.00 26.61 ?  289 ASP B OD1 1 
ATOM   2902 O OD2 . ASP B 1 66  ? -3.194  -1.441  -50.151 1.00 25.67 ?  289 ASP B OD2 1 
ATOM   2903 N N   . VAL B 1 67  ? -0.863  -5.172  -47.706 1.00 22.38 ?  290 VAL B N   1 
ATOM   2904 C CA  . VAL B 1 67  ? 0.231   -6.102  -47.949 1.00 24.35 ?  290 VAL B CA  1 
ATOM   2905 C C   . VAL B 1 67  ? -0.203  -7.179  -48.934 1.00 25.36 ?  290 VAL B C   1 
ATOM   2906 O O   . VAL B 1 67  ? -1.373  -7.572  -48.991 1.00 21.75 ?  290 VAL B O   1 
ATOM   2907 C CB  . VAL B 1 67  ? 0.742   -6.742  -46.639 1.00 20.42 ?  290 VAL B CB  1 
ATOM   2908 C CG1 . VAL B 1 67  ? 1.443   -5.700  -45.784 1.00 22.33 ?  290 VAL B CG1 1 
ATOM   2909 C CG2 . VAL B 1 67  ? -0.406  -7.385  -45.876 1.00 18.64 ?  290 VAL B CG2 1 
ATOM   2910 N N   . THR B 1 68  ? 0.765   -7.650  -49.716 1.00 24.34 ?  291 THR B N   1 
ATOM   2911 C CA  . THR B 1 68  ? 0.600   -8.778  -50.622 1.00 24.55 ?  291 THR B CA  1 
ATOM   2912 C C   . THR B 1 68  ? 1.637   -9.831  -50.263 1.00 26.27 ?  291 THR B C   1 
ATOM   2913 O O   . THR B 1 68  ? 2.830   -9.522  -50.170 1.00 26.55 ?  291 THR B O   1 
ATOM   2914 C CB  . THR B 1 68  ? 0.763   -8.352  -52.085 1.00 24.71 ?  291 THR B CB  1 
ATOM   2915 O OG1 . THR B 1 68  ? -0.183  -7.322  -52.397 1.00 29.76 ?  291 THR B OG1 1 
ATOM   2916 C CG2 . THR B 1 68  ? 0.544   -9.538  -53.016 1.00 28.21 ?  291 THR B CG2 1 
ATOM   2917 N N   . HIS B 1 69  ? 1.186   -11.065 -50.057 1.00 27.54 ?  292 HIS B N   1 
ATOM   2918 C CA  . HIS B 1 69  ? 2.099   -12.121 -49.642 1.00 28.39 ?  292 HIS B CA  1 
ATOM   2919 C C   . HIS B 1 69  ? 2.973   -12.564 -50.807 1.00 31.67 ?  292 HIS B C   1 
ATOM   2920 O O   . HIS B 1 69  ? 2.477   -12.829 -51.906 1.00 31.60 ?  292 HIS B O   1 
ATOM   2921 C CB  . HIS B 1 69  ? 1.329   -13.318 -49.087 1.00 29.44 ?  292 HIS B CB  1 
ATOM   2922 C CG  . HIS B 1 69  ? 2.213   -14.440 -48.638 1.00 29.78 ?  292 HIS B CG  1 
ATOM   2923 N ND1 . HIS B 1 69  ? 2.047   -15.739 -49.067 1.00 33.56 ?  292 HIS B ND1 1 
ATOM   2924 C CD2 . HIS B 1 69  ? 3.284   -14.452 -47.809 1.00 34.30 ?  292 HIS B CD2 1 
ATOM   2925 C CE1 . HIS B 1 69  ? 2.972   -16.505 -48.515 1.00 36.35 ?  292 HIS B CE1 1 
ATOM   2926 N NE2 . HIS B 1 69  ? 3.735   -15.748 -47.747 1.00 39.45 ?  292 HIS B NE2 1 
ATOM   2927 N N   . ILE B 1 70  ? 4.277   -12.642 -50.561 1.00 34.63 ?  293 ILE B N   1 
ATOM   2928 C CA  . ILE B 1 70  ? 5.217   -13.183 -51.537 1.00 33.80 ?  293 ILE B CA  1 
ATOM   2929 C C   . ILE B 1 70  ? 5.213   -14.700 -51.382 1.00 36.46 ?  293 ILE B C   1 
ATOM   2930 O O   . ILE B 1 70  ? 5.702   -15.232 -50.382 1.00 36.12 ?  293 ILE B O   1 
ATOM   2931 C CB  . ILE B 1 70  ? 6.622   -12.602 -51.349 1.00 32.15 ?  293 ILE B CB  1 
ATOM   2932 C CG1 . ILE B 1 70  ? 6.533   -11.122 -50.971 1.00 30.71 ?  293 ILE B CG1 1 
ATOM   2933 C CG2 . ILE B 1 70  ? 7.446   -12.781 -52.613 1.00 36.06 ?  293 ILE B CG2 1 
ATOM   2934 C CD1 . ILE B 1 70  ? 7.874   -10.468 -50.735 1.00 27.76 ?  293 ILE B CD1 1 
ATOM   2935 N N   . THR B 1 71  ? 4.651   -15.396 -52.369 1.00 39.42 ?  294 THR B N   1 
ATOM   2936 C CA  . THR B 1 71  ? 4.437   -16.834 -52.260 1.00 39.25 ?  294 THR B CA  1 
ATOM   2937 C C   . THR B 1 71  ? 5.754   -17.576 -52.068 1.00 40.80 ?  294 THR B C   1 
ATOM   2938 O O   . THR B 1 71  ? 6.793   -17.190 -52.611 1.00 41.71 ?  294 THR B O   1 
ATOM   2939 C CB  . THR B 1 71  ? 3.722   -17.358 -53.507 1.00 40.89 ?  294 THR B CB  1 
ATOM   2940 O OG1 . THR B 1 71  ? 4.547   -17.143 -54.659 1.00 42.87 ?  294 THR B OG1 1 
ATOM   2941 C CG2 . THR B 1 71  ? 2.391   -16.646 -53.700 1.00 33.47 ?  294 THR B CG2 1 
ATOM   2942 N N   . GLY B 1 72  ? 5.701   -18.651 -51.283 1.00 40.38 ?  295 GLY B N   1 
ATOM   2943 C CA  . GLY B 1 72  ? 6.879   -19.451 -51.021 1.00 40.46 ?  295 GLY B CA  1 
ATOM   2944 C C   . GLY B 1 72  ? 7.818   -18.888 -49.982 1.00 42.35 ?  295 GLY B C   1 
ATOM   2945 O O   . GLY B 1 72  ? 8.992   -19.271 -49.953 1.00 43.05 ?  295 GLY B O   1 
ATOM   2946 N N   . SER B 1 73  ? 7.341   -17.992 -49.121 1.00 42.04 ?  296 SER B N   1 
ATOM   2947 C CA  . SER B 1 73  ? 8.194   -17.359 -48.126 1.00 36.94 ?  296 SER B CA  1 
ATOM   2948 C C   . SER B 1 73  ? 7.322   -16.797 -47.014 1.00 35.81 ?  296 SER B C   1 
ATOM   2949 O O   . SER B 1 73  ? 6.092   -16.789 -47.101 1.00 35.03 ?  296 SER B O   1 
ATOM   2950 C CB  . SER B 1 73  ? 9.054   -16.256 -48.751 1.00 34.40 ?  296 SER B CB  1 
ATOM   2951 O OG  . SER B 1 73  ? 8.304   -15.065 -48.924 1.00 30.84 ?  296 SER B OG  1 
ATOM   2952 N N   . ARG B 1 74  ? 7.985   -16.325 -45.958 1.00 35.48 ?  297 ARG B N   1 
ATOM   2953 C CA  . ARG B 1 74  ? 7.331   -15.607 -44.874 1.00 31.98 ?  297 ARG B CA  1 
ATOM   2954 C C   . ARG B 1 74  ? 7.423   -14.096 -45.052 1.00 28.91 ?  297 ARG B C   1 
ATOM   2955 O O   . ARG B 1 74  ? 7.340   -13.354 -44.068 1.00 29.68 ?  297 ARG B O   1 
ATOM   2956 C CB  . ARG B 1 74  ? 7.930   -16.018 -43.527 1.00 34.20 ?  297 ARG B CB  1 
ATOM   2957 C CG  . ARG B 1 74  ? 7.496   -17.390 -43.032 1.00 36.00 ?  297 ARG B CG  1 
ATOM   2958 C CD  . ARG B 1 74  ? 8.324   -17.820 -41.827 1.00 38.19 ?  297 ARG B CD  1 
ATOM   2959 N NE  . ARG B 1 74  ? 8.312   -19.264 -41.615 1.00 46.25 ?  297 ARG B NE  1 
ATOM   2960 C CZ  . ARG B 1 74  ? 7.278   -19.952 -41.148 1.00 44.82 ?  297 ARG B CZ  1 
ATOM   2961 N NH1 . ARG B 1 74  ? 6.140   -19.360 -40.826 1.00 42.52 ?  297 ARG B NH1 1 
ATOM   2962 N NH2 . ARG B 1 74  ? 7.392   -21.269 -40.996 1.00 50.16 ?  297 ARG B NH2 1 
ATOM   2963 N N   . ASN B 1 75  ? 7.591   -13.629 -46.286 1.00 28.77 ?  298 ASN B N   1 
ATOM   2964 C CA  . ASN B 1 75  ? 7.805   -12.221 -46.579 1.00 28.57 ?  298 ASN B CA  1 
ATOM   2965 C C   . ASN B 1 75  ? 6.548   -11.600 -47.173 1.00 28.69 ?  298 ASN B C   1 
ATOM   2966 O O   . ASN B 1 75  ? 5.722   -12.285 -47.783 1.00 29.84 ?  298 ASN B O   1 
ATOM   2967 C CB  . ASN B 1 75  ? 8.980   -12.037 -47.544 1.00 29.47 ?  298 ASN B CB  1 
ATOM   2968 C CG  . ASN B 1 75  ? 10.308  -12.435 -46.928 1.00 32.11 ?  298 ASN B CG  1 
ATOM   2969 O OD1 . ASN B 1 75  ? 10.396  -12.694 -45.729 1.00 31.49 ?  298 ASN B OD1 1 
ATOM   2970 N ND2 . ASN B 1 75  ? 11.349  -12.489 -47.751 1.00 33.22 ?  298 ASN B ND2 1 
ATOM   2971 N N   . TYR B 1 76  ? 6.414   -10.287 -46.991 1.00 28.30 ?  299 TYR B N   1 
ATOM   2972 C CA  . TYR B 1 76  ? 5.271   -9.542  -47.495 1.00 25.42 ?  299 TYR B CA  1 
ATOM   2973 C C   . TYR B 1 76  ? 5.743   -8.237  -48.114 1.00 28.15 ?  299 TYR B C   1 
ATOM   2974 O O   . TYR B 1 76  ? 6.673   -7.601  -47.609 1.00 27.60 ?  299 TYR B O   1 
ATOM   2975 C CB  . TYR B 1 76  ? 4.256   -9.243  -46.383 1.00 22.41 ?  299 TYR B CB  1 
ATOM   2976 C CG  . TYR B 1 76  ? 3.477   -10.448 -45.911 1.00 27.32 ?  299 TYR B CG  1 
ATOM   2977 C CD1 . TYR B 1 76  ? 4.007   -11.317 -44.966 1.00 26.72 ?  299 TYR B CD1 1 
ATOM   2978 C CD2 . TYR B 1 76  ? 2.207   -10.713 -46.405 1.00 24.08 ?  299 TYR B CD2 1 
ATOM   2979 C CE1 . TYR B 1 76  ? 3.297   -12.419 -44.530 1.00 27.68 ?  299 TYR B CE1 1 
ATOM   2980 C CE2 . TYR B 1 76  ? 1.489   -11.812 -45.976 1.00 27.91 ?  299 TYR B CE2 1 
ATOM   2981 C CZ  . TYR B 1 76  ? 2.038   -12.662 -45.039 1.00 30.82 ?  299 TYR B CZ  1 
ATOM   2982 O OH  . TYR B 1 76  ? 1.324   -13.757 -44.610 1.00 28.11 ?  299 TYR B OH  1 
ATOM   2983 N N   . THR B 1 77  ? 5.099   -7.847  -49.210 1.00 24.29 ?  300 THR B N   1 
ATOM   2984 C CA  . THR B 1 77  ? 5.301   -6.541  -49.822 1.00 24.31 ?  300 THR B CA  1 
ATOM   2985 C C   . THR B 1 77  ? 4.181   -5.613  -49.376 1.00 24.70 ?  300 THR B C   1 
ATOM   2986 O O   . THR B 1 77  ? 3.000   -5.935  -49.546 1.00 23.66 ?  300 THR B O   1 
ATOM   2987 C CB  . THR B 1 77  ? 5.317   -6.641  -51.349 1.00 25.45 ?  300 THR B CB  1 
ATOM   2988 O OG1 . THR B 1 77  ? 6.473   -7.375  -51.774 1.00 30.27 ?  300 THR B OG1 1 
ATOM   2989 C CG2 . THR B 1 77  ? 5.337   -5.253  -51.978 1.00 22.03 ?  300 THR B CG2 1 
ATOM   2990 N N   . MET B 1 78  ? 4.545   -4.472  -48.801 1.00 25.53 ?  301 MET B N   1 
ATOM   2991 C CA  . MET B 1 78  ? 3.569   -3.480  -48.366 1.00 25.03 ?  301 MET B CA  1 
ATOM   2992 C C   . MET B 1 78  ? 3.478   -2.383  -49.418 1.00 24.15 ?  301 MET B C   1 
ATOM   2993 O O   . MET B 1 78  ? 4.438   -1.636  -49.632 1.00 24.55 ?  301 MET B O   1 
ATOM   2994 C CB  . MET B 1 78  ? 3.930   -2.893  -47.003 1.00 23.24 ?  301 MET B CB  1 
ATOM   2995 C CG  . MET B 1 78  ? 2.843   -1.978  -46.452 1.00 22.79 ?  301 MET B CG  1 
ATOM   2996 S SD  . MET B 1 78  ? 3.328   -1.044  -44.990 1.00 25.38 ?  301 MET B SD  1 
ATOM   2997 C CE  . MET B 1 78  ? 2.686   -2.091  -43.689 1.00 16.20 ?  301 MET B CE  1 
ATOM   2998 N N   . ASN B 1 79  ? 2.328   -2.298  -50.079 1.00 25.63 ?  302 ASN B N   1 
ATOM   2999 C CA  . ASN B 1 79  ? 2.020   -1.159  -50.931 1.00 21.38 ?  302 ASN B CA  1 
ATOM   3000 C C   . ASN B 1 79  ? 1.656   0.018   -50.036 1.00 22.46 ?  302 ASN B C   1 
ATOM   3001 O O   . ASN B 1 79  ? 0.683   -0.047  -49.277 1.00 24.24 ?  302 ASN B O   1 
ATOM   3002 C CB  . ASN B 1 79  ? 0.886   -1.503  -51.891 1.00 25.02 ?  302 ASN B CB  1 
ATOM   3003 C CG  . ASN B 1 79  ? 1.085   -2.848  -52.563 1.00 27.06 ?  302 ASN B CG  1 
ATOM   3004 O OD1 . ASN B 1 79  ? 0.525   -3.858  -52.135 1.00 24.71 ?  302 ASN B OD1 1 
ATOM   3005 N ND2 . ASN B 1 79  ? 1.894   -2.869  -53.617 1.00 23.19 ?  302 ASN B ND2 1 
ATOM   3006 N N   . LEU B 1 80  ? 2.440   1.087   -50.119 1.00 23.74 ?  303 LEU B N   1 
ATOM   3007 C CA  . LEU B 1 80  ? 2.428   2.114   -49.090 1.00 20.53 ?  303 LEU B CA  1 
ATOM   3008 C C   . LEU B 1 80  ? 1.315   3.131   -49.297 1.00 22.00 ?  303 LEU B C   1 
ATOM   3009 O O   . LEU B 1 80  ? 0.973   3.490   -50.428 1.00 22.85 ?  303 LEU B O   1 
ATOM   3010 C CB  . LEU B 1 80  ? 3.772   2.839   -49.049 1.00 22.19 ?  303 LEU B CB  1 
ATOM   3011 C CG  . LEU B 1 80  ? 4.973   2.024   -48.571 1.00 21.11 ?  303 LEU B CG  1 
ATOM   3012 C CD1 . LEU B 1 80  ? 6.265   2.771   -48.855 1.00 19.76 ?  303 LEU B CD1 1 
ATOM   3013 C CD2 . LEU B 1 80  ? 4.847   1.700   -47.090 1.00 24.26 ?  303 LEU B CD2 1 
ATOM   3014 N N   . ALA B 1 81  ? 0.748   3.580   -48.186 1.00 18.67 ?  304 ALA B N   1 
ATOM   3015 C CA  . ALA B 1 81  ? 0.004   4.824   -48.099 1.00 20.03 ?  304 ALA B CA  1 
ATOM   3016 C C   . ALA B 1 81  ? 0.819   5.813   -47.277 1.00 19.29 ?  304 ALA B C   1 
ATOM   3017 O O   . ALA B 1 81  ? 1.794   5.447   -46.615 1.00 15.72 ?  304 ALA B O   1 
ATOM   3018 C CB  . ALA B 1 81  ? -1.376  4.599   -47.471 1.00 18.95 ?  304 ALA B CB  1 
ATOM   3019 N N   . SER B 1 82  ? 0.425   7.081   -47.330 1.00 23.67 ?  305 SER B N   1 
ATOM   3020 C CA  . SER B 1 82  ? 1.077   8.062   -46.481 1.00 20.66 ?  305 SER B CA  1 
ATOM   3021 C C   . SER B 1 82  ? 0.723   7.796   -45.018 1.00 21.71 ?  305 SER B C   1 
ATOM   3022 O O   . SER B 1 82  ? -0.143  6.977   -44.697 1.00 22.20 ?  305 SER B O   1 
ATOM   3023 C CB  . SER B 1 82  ? 0.683   9.481   -46.890 1.00 20.82 ?  305 SER B CB  1 
ATOM   3024 O OG  . SER B 1 82  ? -0.688  9.727   -46.634 1.00 25.02 ?  305 SER B OG  1 
ATOM   3025 N N   . GLN B 1 83  ? 1.415   8.500   -44.119 1.00 20.40 ?  306 GLN B N   1 
ATOM   3026 C CA  . GLN B 1 83  ? 1.217   8.258   -42.693 1.00 22.64 ?  306 GLN B CA  1 
ATOM   3027 C C   . GLN B 1 83  ? -0.200  8.604   -42.250 1.00 21.63 ?  306 GLN B C   1 
ATOM   3028 O O   . GLN B 1 83  ? -0.694  8.045   -41.264 1.00 22.39 ?  306 GLN B O   1 
ATOM   3029 C CB  . GLN B 1 83  ? 2.242   9.047   -41.877 1.00 21.56 ?  306 GLN B CB  1 
ATOM   3030 C CG  . GLN B 1 83  ? 3.689   8.788   -42.276 1.00 23.77 ?  306 GLN B CG  1 
ATOM   3031 C CD  . GLN B 1 83  ? 4.253   7.514   -41.670 1.00 25.91 ?  306 GLN B CD  1 
ATOM   3032 O OE1 . GLN B 1 83  ? 3.512   6.611   -41.280 1.00 27.20 ?  306 GLN B OE1 1 
ATOM   3033 N NE2 . GLN B 1 83  ? 5.577   7.436   -41.589 1.00 24.42 ?  306 GLN B NE2 1 
ATOM   3034 N N   . ASN B 1 84  ? -0.869  9.512   -42.961 1.00 22.74 ?  307 ASN B N   1 
ATOM   3035 C CA  . ASN B 1 84  ? -2.258  9.852   -42.684 1.00 24.00 ?  307 ASN B CA  1 
ATOM   3036 C C   . ASN B 1 84  ? -3.231  9.066   -43.558 1.00 23.20 ?  307 ASN B C   1 
ATOM   3037 O O   . ASN B 1 84  ? -4.382  9.483   -43.725 1.00 24.25 ?  307 ASN B O   1 
ATOM   3038 C CB  . ASN B 1 84  ? -2.480  11.356  -42.853 1.00 21.86 ?  307 ASN B CB  1 
ATOM   3039 C CG  . ASN B 1 84  ? -2.452  11.793  -44.304 1.00 30.69 ?  307 ASN B CG  1 
ATOM   3040 O OD1 . ASN B 1 84  ? -3.475  12.190  -44.862 1.00 33.89 ?  307 ASN B OD1 1 
ATOM   3041 N ND2 . ASN B 1 84  ? -1.279  11.728  -44.923 1.00 31.57 ?  307 ASN B ND2 1 
ATOM   3042 N N   . TRP B 1 85  ? -2.781  7.943   -44.123 1.00 22.12 ?  308 TRP B N   1 
ATOM   3043 C CA  . TRP B 1 85  ? -3.596  7.005   -44.892 1.00 23.97 ?  308 TRP B CA  1 
ATOM   3044 C C   . TRP B 1 85  ? -4.103  7.582   -46.209 1.00 23.36 ?  308 TRP B C   1 
ATOM   3045 O O   . TRP B 1 85  ? -5.081  7.076   -46.769 1.00 23.96 ?  308 TRP B O   1 
ATOM   3046 C CB  . TRP B 1 85  ? -4.777  6.480   -44.067 1.00 24.69 ?  308 TRP B CB  1 
ATOM   3047 C CG  . TRP B 1 85  ? -4.366  5.618   -42.914 1.00 24.31 ?  308 TRP B CG  1 
ATOM   3048 C CD1 . TRP B 1 85  ? -4.382  5.955   -41.593 1.00 23.26 ?  308 TRP B CD1 1 
ATOM   3049 C CD2 . TRP B 1 85  ? -3.873  4.274   -42.981 1.00 23.76 ?  308 TRP B CD2 1 
ATOM   3050 N NE1 . TRP B 1 85  ? -3.932  4.903   -40.832 1.00 24.65 ?  308 TRP B NE1 1 
ATOM   3051 C CE2 . TRP B 1 85  ? -3.612  3.860   -41.660 1.00 20.09 ?  308 TRP B CE2 1 
ATOM   3052 C CE3 . TRP B 1 85  ? -3.623  3.383   -44.028 1.00 24.65 ?  308 TRP B CE3 1 
ATOM   3053 C CZ2 . TRP B 1 85  ? -3.118  2.592   -41.360 1.00 23.99 ?  308 TRP B CZ2 1 
ATOM   3054 C CZ3 . TRP B 1 85  ? -3.136  2.124   -43.729 1.00 23.26 ?  308 TRP B CZ3 1 
ATOM   3055 C CH2 . TRP B 1 85  ? -2.888  1.740   -42.406 1.00 22.99 ?  308 TRP B CH2 1 
ATOM   3056 N N   . ASN B 1 86  ? -3.466  8.626   -46.727 1.00 22.47 ?  309 ASN B N   1 
ATOM   3057 C CA  . ASN B 1 86  ? -3.782  9.083   -48.069 1.00 22.53 ?  309 ASN B CA  1 
ATOM   3058 C C   . ASN B 1 86  ? -3.032  8.246   -49.099 1.00 23.79 ?  309 ASN B C   1 
ATOM   3059 O O   . ASN B 1 86  ? -2.064  7.548   -48.784 1.00 22.02 ?  309 ASN B O   1 
ATOM   3060 C CB  . ASN B 1 86  ? -3.426  10.560  -48.249 1.00 23.21 ?  309 ASN B CB  1 
ATOM   3061 C CG  . ASN B 1 86  ? -4.445  11.486  -47.623 1.00 27.12 ?  309 ASN B CG  1 
ATOM   3062 O OD1 . ASN B 1 86  ? -5.582  11.091  -47.370 1.00 27.93 ?  309 ASN B OD1 1 
ATOM   3063 N ND2 . ASN B 1 86  ? -4.046  12.729  -47.377 1.00 23.88 ?  309 ASN B ND2 1 
ATOM   3064 N N   . ASP B 1 87  ? -3.501  8.311   -50.342 1.00 21.54 ?  310 ASP B N   1 
ATOM   3065 C CA  . ASP B 1 87  ? -2.737  7.745   -51.444 1.00 23.45 ?  310 ASP B CA  1 
ATOM   3066 C C   . ASP B 1 87  ? -1.358  8.387   -51.482 1.00 22.42 ?  310 ASP B C   1 
ATOM   3067 O O   . ASP B 1 87  ? -1.231  9.614   -51.434 1.00 18.43 ?  310 ASP B O   1 
ATOM   3068 C CB  . ASP B 1 87  ? -3.457  7.968   -52.775 1.00 19.21 ?  310 ASP B CB  1 
ATOM   3069 C CG  . ASP B 1 87  ? -4.717  7.138   -52.908 1.00 20.69 ?  310 ASP B CG  1 
ATOM   3070 O OD1 . ASP B 1 87  ? -4.775  6.041   -52.318 1.00 25.36 ?  310 ASP B OD1 1 
ATOM   3071 O OD2 . ASP B 1 87  ? -5.648  7.584   -53.609 1.00 24.98 ?  310 ASP B OD2 1 
ATOM   3072 N N   . TYR B 1 88  ? -0.322  7.557   -51.541 1.00 24.07 ?  311 TYR B N   1 
ATOM   3073 C CA  . TYR B 1 88  ? 1.030   8.082   -51.658 1.00 23.41 ?  311 TYR B CA  1 
ATOM   3074 C C   . TYR B 1 88  ? 1.252   8.609   -53.069 1.00 19.24 ?  311 TYR B C   1 
ATOM   3075 O O   . TYR B 1 88  ? 0.979   7.914   -54.052 1.00 22.93 ?  311 TYR B O   1 
ATOM   3076 C CB  . TYR B 1 88  ? 2.056   7.002   -51.321 1.00 21.11 ?  311 TYR B CB  1 
ATOM   3077 C CG  . TYR B 1 88  ? 3.469   7.353   -51.732 1.00 22.40 ?  311 TYR B CG  1 
ATOM   3078 C CD1 . TYR B 1 88  ? 4.086   8.505   -51.257 1.00 17.63 ?  311 TYR B CD1 1 
ATOM   3079 C CD2 . TYR B 1 88  ? 4.187   6.535   -52.594 1.00 21.91 ?  311 TYR B CD2 1 
ATOM   3080 C CE1 . TYR B 1 88  ? 5.376   8.831   -51.630 1.00 16.45 ?  311 TYR B CE1 1 
ATOM   3081 C CE2 . TYR B 1 88  ? 5.477   6.852   -52.972 1.00 21.92 ?  311 TYR B CE2 1 
ATOM   3082 C CZ  . TYR B 1 88  ? 6.066   8.001   -52.487 1.00 20.77 ?  311 TYR B CZ  1 
ATOM   3083 O OH  . TYR B 1 88  ? 7.351   8.322   -52.861 1.00 23.19 ?  311 TYR B OH  1 
ATOM   3084 N N   . ASP B 1 89  ? 1.732   9.850   -53.168 1.00 19.18 ?  312 ASP B N   1 
ATOM   3085 C CA  . ASP B 1 89  ? 2.023   10.460  -54.457 1.00 24.35 ?  312 ASP B CA  1 
ATOM   3086 C C   . ASP B 1 89  ? 3.526   10.395  -54.693 1.00 23.00 ?  312 ASP B C   1 
ATOM   3087 O O   . ASP B 1 89  ? 4.271   11.224  -54.148 1.00 22.71 ?  312 ASP B O   1 
ATOM   3088 C CB  . ASP B 1 89  ? 1.531   11.909  -54.498 1.00 24.16 ?  312 ASP B CB  1 
ATOM   3089 C CG  . ASP B 1 89  ? 1.728   12.562  -55.859 1.00 27.17 ?  312 ASP B CG  1 
ATOM   3090 O OD1 . ASP B 1 89  ? 2.221   11.890  -56.791 1.00 25.36 ?  312 ASP B OD1 1 
ATOM   3091 O OD2 . ASP B 1 89  ? 1.385   13.755  -55.996 1.00 29.31 ?  312 ASP B OD2 1 
ATOM   3092 N N   . PRO B 1 90  ? 4.022   9.444   -55.490 1.00 23.45 ?  313 PRO B N   1 
ATOM   3093 C CA  . PRO B 1 90  ? 5.473   9.352   -55.719 1.00 21.82 ?  313 PRO B CA  1 
ATOM   3094 C C   . PRO B 1 90  ? 6.047   10.517  -56.508 1.00 22.64 ?  313 PRO B C   1 
ATOM   3095 O O   . PRO B 1 90  ? 7.276   10.624  -56.603 1.00 21.27 ?  313 PRO B O   1 
ATOM   3096 C CB  . PRO B 1 90  ? 5.624   8.034   -56.494 1.00 24.87 ?  313 PRO B CB  1 
ATOM   3097 C CG  . PRO B 1 90  ? 4.327   7.298   -56.281 1.00 23.79 ?  313 PRO B CG  1 
ATOM   3098 C CD  . PRO B 1 90  ? 3.292   8.367   -56.174 1.00 23.58 ?  313 PRO B CD  1 
ATOM   3099 N N   . THR B 1 91  ? 5.213   11.383  -57.077 1.00 26.32 ?  314 THR B N   1 
ATOM   3100 C CA  . THR B 1 91  ? 5.692   12.534  -57.829 1.00 24.07 ?  314 THR B CA  1 
ATOM   3101 C C   . THR B 1 91  ? 5.899   13.767  -56.960 1.00 22.29 ?  314 THR B C   1 
ATOM   3102 O O   . THR B 1 91  ? 6.270   14.821  -57.486 1.00 25.93 ?  314 THR B O   1 
ATOM   3103 C CB  . THR B 1 91  ? 4.727   12.868  -58.973 1.00 23.19 ?  314 THR B CB  1 
ATOM   3104 O OG1 . THR B 1 91  ? 3.588   13.567  -58.455 1.00 26.73 ?  314 THR B OG1 1 
ATOM   3105 C CG2 . THR B 1 91  ? 4.268   11.597  -59.670 1.00 21.36 ?  314 THR B CG2 1 
ATOM   3106 N N   . GLU B 1 92  ? 5.662   13.667  -55.655 1.00 25.84 ?  315 GLU B N   1 
ATOM   3107 C CA  . GLU B 1 92  ? 5.997   14.761  -54.756 1.00 26.37 ?  315 GLU B CA  1 
ATOM   3108 C C   . GLU B 1 92  ? 7.507   14.961  -54.715 1.00 24.06 ?  315 GLU B C   1 
ATOM   3109 O O   . GLU B 1 92  ? 8.286   14.009  -54.812 1.00 21.53 ?  315 GLU B O   1 
ATOM   3110 C CB  . GLU B 1 92  ? 5.464   14.490  -53.349 1.00 27.14 ?  315 GLU B CB  1 
ATOM   3111 C CG  . GLU B 1 92  ? 4.234   15.307  -52.982 1.00 30.65 ?  315 GLU B CG  1 
ATOM   3112 C CD  . GLU B 1 92  ? 3.435   14.688  -51.851 1.00 40.30 ?  315 GLU B CD  1 
ATOM   3113 O OE1 . GLU B 1 92  ? 4.016   14.445  -50.772 1.00 35.00 ?  315 GLU B OE1 1 
ATOM   3114 O OE2 . GLU B 1 92  ? 2.224   14.446  -52.041 1.00 44.96 ?  315 GLU B OE2 1 
ATOM   3115 N N   . GLU B 1 93  ? 7.920   16.220  -54.566 1.00 24.69 ?  316 GLU B N   1 
ATOM   3116 C CA  . GLU B 1 93  ? 9.338   16.581  -54.584 1.00 24.18 ?  316 GLU B CA  1 
ATOM   3117 C C   . GLU B 1 93  ? 9.999   16.243  -53.244 1.00 24.32 ?  316 GLU B C   1 
ATOM   3118 O O   . GLU B 1 93  ? 10.574  17.088  -52.559 1.00 28.29 ?  316 GLU B O   1 
ATOM   3119 C CB  . GLU B 1 93  ? 9.496   18.055  -54.932 1.00 27.47 ?  316 GLU B CB  1 
ATOM   3120 C CG  . GLU B 1 93  ? 8.641   18.504  -56.111 1.00 30.90 ?  316 GLU B CG  1 
ATOM   3121 C CD  . GLU B 1 93  ? 9.372   19.451  -57.045 1.00 37.67 ?  316 GLU B CD  1 
ATOM   3122 O OE1 . GLU B 1 93  ? 9.521   20.640  -56.691 1.00 34.16 ?  316 GLU B OE1 1 
ATOM   3123 O OE2 . GLU B 1 93  ? 9.795   19.007  -58.134 1.00 35.06 ?  316 GLU B OE2 1 
ATOM   3124 N N   . ILE B 1 94  ? 9.906   14.967  -52.883 1.00 22.05 ?  317 ILE B N   1 
ATOM   3125 C CA  . ILE B 1 94  ? 10.491  14.451  -51.647 1.00 21.53 ?  317 ILE B CA  1 
ATOM   3126 C C   . ILE B 1 94  ? 11.298  13.205  -51.989 1.00 21.64 ?  317 ILE B C   1 
ATOM   3127 O O   . ILE B 1 94  ? 11.092  12.587  -53.046 1.00 16.63 ?  317 ILE B O   1 
ATOM   3128 C CB  . ILE B 1 94  ? 9.406   14.146  -50.586 1.00 21.75 ?  317 ILE B CB  1 
ATOM   3129 C CG1 . ILE B 1 94  ? 8.365   13.172  -51.141 1.00 19.67 ?  317 ILE B CG1 1 
ATOM   3130 C CG2 . ILE B 1 94  ? 8.746   15.432  -50.107 1.00 20.24 ?  317 ILE B CG2 1 
ATOM   3131 C CD1 . ILE B 1 94  ? 7.261   12.841  -50.159 1.00 18.54 ?  317 ILE B CD1 1 
ATOM   3132 N N   . PRO B 1 95  ? 12.241  12.815  -51.122 1.00 22.34 ?  318 PRO B N   1 
ATOM   3133 C CA  . PRO B 1 95  ? 13.036  11.612  -51.421 1.00 22.47 ?  318 PRO B CA  1 
ATOM   3134 C C   . PRO B 1 95  ? 12.264  10.320  -51.240 1.00 20.49 ?  318 PRO B C   1 
ATOM   3135 O O   . PRO B 1 95  ? 12.590  9.321   -51.895 1.00 18.51 ?  318 PRO B O   1 
ATOM   3136 C CB  . PRO B 1 95  ? 14.212  11.702  -50.432 1.00 22.00 ?  318 PRO B CB  1 
ATOM   3137 C CG  . PRO B 1 95  ? 14.097  13.043  -49.764 1.00 22.36 ?  318 PRO B CG  1 
ATOM   3138 C CD  . PRO B 1 95  ? 12.672  13.457  -49.870 1.00 20.41 ?  318 PRO B CD  1 
ATOM   3139 N N   . ALA B 1 96  ? 11.256  10.312  -50.374 1.00 16.49 ?  319 ALA B N   1 
ATOM   3140 C CA  . ALA B 1 96  ? 10.505  9.119   -50.008 1.00 18.71 ?  319 ALA B CA  1 
ATOM   3141 C C   . ALA B 1 96  ? 9.296   9.557   -49.191 1.00 19.24 ?  319 ALA B C   1 
ATOM   3142 O O   . ALA B 1 96  ? 9.226   10.726  -48.790 1.00 18.00 ?  319 ALA B O   1 
ATOM   3143 C CB  . ALA B 1 96  ? 11.389  8.149   -49.219 1.00 22.78 ?  319 ALA B CB  1 
ATOM   3144 N N   . PRO B 1 97  ? 8.322   8.679   -48.942 1.00 17.86 ?  320 PRO B N   1 
ATOM   3145 C CA  . PRO B 1 97  ? 7.212   9.047   -48.054 1.00 18.62 ?  320 PRO B CA  1 
ATOM   3146 C C   . PRO B 1 97  ? 7.721   9.602   -46.731 1.00 20.15 ?  320 PRO B C   1 
ATOM   3147 O O   . PRO B 1 97  ? 8.701   9.112   -46.165 1.00 22.28 ?  320 PRO B O   1 
ATOM   3148 C CB  . PRO B 1 97  ? 6.452   7.727   -47.859 1.00 19.33 ?  320 PRO B CB  1 
ATOM   3149 C CG  . PRO B 1 97  ? 7.223   6.672   -48.620 1.00 20.56 ?  320 PRO B CG  1 
ATOM   3150 C CD  . PRO B 1 97  ? 8.085   7.385   -49.601 1.00 20.24 ?  320 PRO B CD  1 
ATOM   3151 N N   . LEU B 1 98  ? 7.054   10.651  -46.253 1.00 19.04 ?  321 LEU B N   1 
ATOM   3152 C CA  . LEU B 1 98  ? 7.477   11.328  -45.034 1.00 20.29 ?  321 LEU B CA  1 
ATOM   3153 C C   . LEU B 1 98  ? 7.513   10.353  -43.864 1.00 23.38 ?  321 LEU B C   1 
ATOM   3154 O O   . LEU B 1 98  ? 6.563   9.599   -43.638 1.00 24.18 ?  321 LEU B O   1 
ATOM   3155 C CB  . LEU B 1 98  ? 6.534   12.492  -44.728 1.00 20.69 ?  321 LEU B CB  1 
ATOM   3156 C CG  . LEU B 1 98  ? 6.356   13.536  -45.833 1.00 21.08 ?  321 LEU B CG  1 
ATOM   3157 C CD1 . LEU B 1 98  ? 5.570   14.734  -45.321 1.00 18.46 ?  321 LEU B CD1 1 
ATOM   3158 C CD2 . LEU B 1 98  ? 7.702   13.976  -46.392 1.00 17.48 ?  321 LEU B CD2 1 
ATOM   3159 N N   . GLY B 1 99  ? 8.618   10.367  -43.122 1.00 23.25 ?  322 GLY B N   1 
ATOM   3160 C CA  . GLY B 1 99  ? 8.815   9.447   -42.023 1.00 21.10 ?  322 GLY B CA  1 
ATOM   3161 C C   . GLY B 1 99  ? 9.596   8.198   -42.365 1.00 22.89 ?  322 GLY B C   1 
ATOM   3162 O O   . GLY B 1 99  ? 9.831   7.372   -41.473 1.00 23.18 ?  322 GLY B O   1 
ATOM   3163 N N   . THR B 1 100 ? 10.002  8.033   -43.620 1.00 22.26 ?  323 THR B N   1 
ATOM   3164 C CA  . THR B 1 100 ? 10.774  6.866   -44.019 1.00 19.98 ?  323 THR B CA  1 
ATOM   3165 C C   . THR B 1 100 ? 12.093  6.824   -43.248 1.00 19.46 ?  323 THR B C   1 
ATOM   3166 O O   . THR B 1 100 ? 12.684  7.876   -42.976 1.00 19.69 ?  323 THR B O   1 
ATOM   3167 C CB  . THR B 1 100 ? 11.040  6.908   -45.527 1.00 21.61 ?  323 THR B CB  1 
ATOM   3168 O OG1 . THR B 1 100 ? 9.795   7.015   -46.229 1.00 23.63 ?  323 THR B OG1 1 
ATOM   3169 C CG2 . THR B 1 100 ? 11.774  5.661   -46.000 1.00 16.67 ?  323 THR B CG2 1 
ATOM   3170 N N   . PRO B 1 101 ? 12.562  5.639   -42.849 1.00 20.08 ?  324 PRO B N   1 
ATOM   3171 C CA  . PRO B 1 101 ? 13.897  5.543   -42.246 1.00 22.27 ?  324 PRO B CA  1 
ATOM   3172 C C   . PRO B 1 101 ? 14.961  6.131   -43.161 1.00 21.30 ?  324 PRO B C   1 
ATOM   3173 O O   . PRO B 1 101 ? 14.929  5.951   -44.380 1.00 22.50 ?  324 PRO B O   1 
ATOM   3174 C CB  . PRO B 1 101 ? 14.090  4.035   -42.057 1.00 19.67 ?  324 PRO B CB  1 
ATOM   3175 C CG  . PRO B 1 101 ? 12.710  3.505   -41.905 1.00 19.44 ?  324 PRO B CG  1 
ATOM   3176 C CD  . PRO B 1 101 ? 11.833  4.360   -42.779 1.00 20.26 ?  324 PRO B CD  1 
ATOM   3177 N N   . ASP B 1 102 ? 15.909  6.848   -42.557 1.00 22.97 ?  325 ASP B N   1 
ATOM   3178 C CA  . ASP B 1 102 ? 16.977  7.513   -43.291 1.00 23.75 ?  325 ASP B CA  1 
ATOM   3179 C C   . ASP B 1 102 ? 18.341  6.882   -43.021 1.00 22.13 ?  325 ASP B C   1 
ATOM   3180 O O   . ASP B 1 102 ? 19.367  7.565   -43.068 1.00 23.70 ?  325 ASP B O   1 
ATOM   3181 C CB  . ASP B 1 102 ? 17.004  9.007   -42.964 1.00 21.04 ?  325 ASP B CB  1 
ATOM   3182 C CG  . ASP B 1 102 ? 17.285  9.286   -41.496 1.00 21.89 ?  325 ASP B CG  1 
ATOM   3183 O OD1 . ASP B 1 102 ? 17.303  8.333   -40.688 1.00 22.86 ?  325 ASP B OD1 1 
ATOM   3184 O OD2 . ASP B 1 102 ? 17.490  10.468  -41.148 1.00 24.61 ?  325 ASP B OD2 1 
ATOM   3185 N N   . PHE B 1 103 ? 18.370  5.582   -42.736 1.00 18.24 ?  326 PHE B N   1 
ATOM   3186 C CA  . PHE B 1 103 ? 19.631  4.896   -42.502 1.00 21.97 ?  326 PHE B CA  1 
ATOM   3187 C C   . PHE B 1 103 ? 19.503  3.440   -42.919 1.00 23.59 ?  326 PHE B C   1 
ATOM   3188 O O   . PHE B 1 103 ? 18.424  2.846   -42.839 1.00 25.15 ?  326 PHE B O   1 
ATOM   3189 C CB  . PHE B 1 103 ? 20.073  4.993   -41.033 1.00 23.73 ?  326 PHE B CB  1 
ATOM   3190 C CG  . PHE B 1 103 ? 19.113  4.365   -40.060 1.00 21.61 ?  326 PHE B CG  1 
ATOM   3191 C CD1 . PHE B 1 103 ? 18.046  5.088   -39.552 1.00 23.05 ?  326 PHE B CD1 1 
ATOM   3192 C CD2 . PHE B 1 103 ? 19.289  3.055   -39.640 1.00 20.84 ?  326 PHE B CD2 1 
ATOM   3193 C CE1 . PHE B 1 103 ? 17.167  4.514   -38.652 1.00 20.79 ?  326 PHE B CE1 1 
ATOM   3194 C CE2 . PHE B 1 103 ? 18.413  2.476   -38.742 1.00 20.54 ?  326 PHE B CE2 1 
ATOM   3195 C CZ  . PHE B 1 103 ? 17.351  3.207   -38.247 1.00 19.99 ?  326 PHE B CZ  1 
ATOM   3196 N N   . VAL B 1 104 ? 20.620  2.874   -43.366 1.00 25.75 ?  327 VAL B N   1 
ATOM   3197 C CA  . VAL B 1 104 ? 20.676  1.462   -43.726 1.00 26.17 ?  327 VAL B CA  1 
ATOM   3198 C C   . VAL B 1 104 ? 20.804  0.635   -42.454 1.00 22.99 ?  327 VAL B C   1 
ATOM   3199 O O   . VAL B 1 104 ? 21.647  0.920   -41.595 1.00 25.03 ?  327 VAL B O   1 
ATOM   3200 C CB  . VAL B 1 104 ? 21.842  1.190   -44.689 1.00 27.24 ?  327 VAL B CB  1 
ATOM   3201 C CG1 . VAL B 1 104 ? 22.123  -0.302  -44.780 1.00 23.73 ?  327 VAL B CG1 1 
ATOM   3202 C CG2 . VAL B 1 104 ? 21.534  1.761   -46.065 1.00 21.67 ?  327 VAL B CG2 1 
ATOM   3203 N N   . GLY B 1 105 ? 19.965  -0.384  -42.328 1.00 23.80 ?  328 GLY B N   1 
ATOM   3204 C CA  . GLY B 1 105 ? 20.002  -1.243  -41.162 1.00 24.29 ?  328 GLY B CA  1 
ATOM   3205 C C   . GLY B 1 105 ? 18.795  -2.149  -41.135 1.00 22.86 ?  328 GLY B C   1 
ATOM   3206 O O   . GLY B 1 105 ? 17.881  -2.044  -41.959 1.00 23.62 ?  328 GLY B O   1 
ATOM   3207 N N   . LYS B 1 106 ? 18.809  -3.057  -40.164 1.00 23.10 ?  329 LYS B N   1 
ATOM   3208 C CA  . LYS B 1 106 ? 17.721  -4.004  -39.948 1.00 24.86 ?  329 LYS B CA  1 
ATOM   3209 C C   . LYS B 1 106 ? 16.877  -3.510  -38.779 1.00 23.71 ?  329 LYS B C   1 
ATOM   3210 O O   . LYS B 1 106 ? 17.320  -3.542  -37.626 1.00 27.06 ?  329 LYS B O   1 
ATOM   3211 C CB  . LYS B 1 106 ? 18.265  -5.408  -39.696 1.00 26.36 ?  329 LYS B CB  1 
ATOM   3212 C CG  . LYS B 1 106 ? 19.225  -5.893  -40.771 1.00 29.59 ?  329 LYS B CG  1 
ATOM   3213 C CD  . LYS B 1 106 ? 19.742  -7.293  -40.485 1.00 36.46 ?  329 LYS B CD  1 
ATOM   3214 C CE  . LYS B 1 106 ? 21.194  -7.413  -40.909 1.00 42.79 ?  329 LYS B CE  1 
ATOM   3215 N NZ  . LYS B 1 106 ? 21.729  -8.798  -40.846 1.00 43.80 ?  329 LYS B NZ  1 
ATOM   3216 N N   . ILE B 1 107 ? 15.666  -3.052  -39.079 1.00 24.17 ?  330 ILE B N   1 
ATOM   3217 C CA  . ILE B 1 107 ? 14.764  -2.478  -38.088 1.00 26.36 ?  330 ILE B CA  1 
ATOM   3218 C C   . ILE B 1 107 ? 13.713  -3.521  -37.738 1.00 24.80 ?  330 ILE B C   1 
ATOM   3219 O O   . ILE B 1 107 ? 12.997  -4.014  -38.619 1.00 22.56 ?  330 ILE B O   1 
ATOM   3220 C CB  . ILE B 1 107 ? 14.113  -1.187  -38.606 1.00 21.13 ?  330 ILE B CB  1 
ATOM   3221 C CG1 . ILE B 1 107 ? 15.188  -0.148  -38.930 1.00 22.39 ?  330 ILE B CG1 1 
ATOM   3222 C CG2 . ILE B 1 107 ? 13.123  -0.640  -37.589 1.00 19.95 ?  330 ILE B CG2 1 
ATOM   3223 C CD1 . ILE B 1 107 ? 14.695  0.992   -39.790 1.00 21.67 ?  330 ILE B CD1 1 
ATOM   3224 N N   . GLN B 1 108 ? 13.617  -3.856  -36.455 1.00 23.93 ?  331 GLN B N   1 
ATOM   3225 C CA  . GLN B 1 108 ? 12.685  -4.866  -35.976 1.00 22.95 ?  331 GLN B CA  1 
ATOM   3226 C C   . GLN B 1 108 ? 11.471  -4.207  -35.337 1.00 24.28 ?  331 GLN B C   1 
ATOM   3227 O O   . GLN B 1 108 ? 11.585  -3.165  -34.684 1.00 25.00 ?  331 GLN B O   1 
ATOM   3228 C CB  . GLN B 1 108 ? 13.361  -5.797  -34.968 1.00 22.51 ?  331 GLN B CB  1 
ATOM   3229 C CG  . GLN B 1 108 ? 12.553  -7.042  -34.635 1.00 25.30 ?  331 GLN B CG  1 
ATOM   3230 C CD  . GLN B 1 108 ? 13.411  -8.288  -34.545 1.00 27.87 ?  331 GLN B CD  1 
ATOM   3231 O OE1 . GLN B 1 108 ? 13.861  -8.669  -33.464 1.00 27.69 ?  331 GLN B OE1 1 
ATOM   3232 N NE2 . GLN B 1 108 ? 13.645  -8.929  -35.684 1.00 29.66 ?  331 GLN B NE2 1 
ATOM   3233 N N   . GLY B 1 109 ? 10.309  -4.824  -35.530 1.00 24.08 ?  332 GLY B N   1 
ATOM   3234 C CA  . GLY B 1 109 ? 9.077   -4.319  -34.961 1.00 23.70 ?  332 GLY B CA  1 
ATOM   3235 C C   . GLY B 1 109 ? 7.935   -5.308  -35.074 1.00 25.17 ?  332 GLY B C   1 
ATOM   3236 O O   . GLY B 1 109 ? 8.149   -6.522  -35.018 1.00 24.38 ?  332 GLY B O   1 
ATOM   3237 N N   . VAL B 1 110 ? 6.716   -4.800  -35.232 1.00 23.68 ?  333 VAL B N   1 
ATOM   3238 C CA  . VAL B 1 110 ? 5.523   -5.632  -35.330 1.00 25.33 ?  333 VAL B CA  1 
ATOM   3239 C C   . VAL B 1 110 ? 4.655   -5.116  -36.469 1.00 22.53 ?  333 VAL B C   1 
ATOM   3240 O O   . VAL B 1 110 ? 4.469   -3.904  -36.622 1.00 22.89 ?  333 VAL B O   1 
ATOM   3241 C CB  . VAL B 1 110 ? 4.725   -5.649  -34.007 1.00 21.60 ?  333 VAL B CB  1 
ATOM   3242 C CG1 . VAL B 1 110 ? 3.440   -6.451  -34.167 1.00 20.40 ?  333 VAL B CG1 1 
ATOM   3243 C CG2 . VAL B 1 110 ? 5.567   -6.215  -32.873 1.00 20.79 ?  333 VAL B CG2 1 
ATOM   3244 N N   . LEU B 1 111 ? 4.135   -6.039  -37.274 1.00 22.53 ?  334 LEU B N   1 
ATOM   3245 C CA  . LEU B 1 111 ? 3.113   -5.737  -38.268 1.00 20.55 ?  334 LEU B CA  1 
ATOM   3246 C C   . LEU B 1 111 ? 1.749   -6.067  -37.675 1.00 23.21 ?  334 LEU B C   1 
ATOM   3247 O O   . LEU B 1 111 ? 1.465   -7.233  -37.383 1.00 24.53 ?  334 LEU B O   1 
ATOM   3248 C CB  . LEU B 1 111 ? 3.334   -6.533  -39.555 1.00 22.79 ?  334 LEU B CB  1 
ATOM   3249 C CG  . LEU B 1 111 ? 4.221   -5.957  -40.659 1.00 23.73 ?  334 LEU B CG  1 
ATOM   3250 C CD1 . LEU B 1 111 ? 4.356   -6.964  -41.793 1.00 21.25 ?  334 LEU B CD1 1 
ATOM   3251 C CD2 . LEU B 1 111 ? 3.661   -4.641  -41.172 1.00 20.28 ?  334 LEU B CD2 1 
ATOM   3252 N N   . THR B 1 112 ? 0.916   -5.049  -37.492 1.00 23.99 ?  335 THR B N   1 
ATOM   3253 C CA  . THR B 1 112 ? -0.457  -5.241  -37.051 1.00 22.74 ?  335 THR B CA  1 
ATOM   3254 C C   . THR B 1 112 ? -1.412  -4.933  -38.197 1.00 24.28 ?  335 THR B C   1 
ATOM   3255 O O   . THR B 1 112 ? -1.094  -4.173  -39.116 1.00 21.37 ?  335 THR B O   1 
ATOM   3256 C CB  . THR B 1 112 ? -0.785  -4.364  -35.836 1.00 21.77 ?  335 THR B CB  1 
ATOM   3257 O OG1 . THR B 1 112 ? -0.572  -2.984  -36.159 1.00 22.21 ?  335 THR B OG1 1 
ATOM   3258 C CG2 . THR B 1 112 ? 0.088   -4.748  -34.648 1.00 21.96 ?  335 THR B CG2 1 
ATOM   3259 N N   . GLN B 1 113 ? -2.595  -5.542  -38.136 1.00 22.68 ?  336 GLN B N   1 
ATOM   3260 C CA  . GLN B 1 113 ? -3.569  -5.420  -39.209 1.00 24.69 ?  336 GLN B CA  1 
ATOM   3261 C C   . GLN B 1 113 ? -4.969  -5.585  -38.636 1.00 22.95 ?  336 GLN B C   1 
ATOM   3262 O O   . GLN B 1 113 ? -5.189  -6.410  -37.745 1.00 20.38 ?  336 GLN B O   1 
ATOM   3263 C CB  . GLN B 1 113 ? -3.310  -6.461  -40.307 1.00 23.96 ?  336 GLN B CB  1 
ATOM   3264 C CG  . GLN B 1 113 ? -4.391  -6.544  -41.370 1.00 23.98 ?  336 GLN B CG  1 
ATOM   3265 C CD  . GLN B 1 113 ? -4.064  -7.551  -42.453 1.00 22.74 ?  336 GLN B CD  1 
ATOM   3266 O OE1 . GLN B 1 113 ? -4.475  -8.709  -42.384 1.00 22.30 ?  336 GLN B OE1 1 
ATOM   3267 N NE2 . GLN B 1 113 ? -3.320  -7.114  -43.463 1.00 19.79 ?  336 GLN B NE2 1 
ATOM   3268 N N   . THR B 1 114 ? -5.908  -4.790  -39.146 1.00 19.44 ?  337 THR B N   1 
ATOM   3269 C CA  . THR B 1 114 ? -7.307  -4.853  -38.746 1.00 22.91 ?  337 THR B CA  1 
ATOM   3270 C C   . THR B 1 114 ? -8.170  -5.124  -39.969 1.00 23.01 ?  337 THR B C   1 
ATOM   3271 O O   . THR B 1 114 ? -8.053  -4.426  -40.982 1.00 23.13 ?  337 THR B O   1 
ATOM   3272 C CB  . THR B 1 114 ? -7.754  -3.551  -38.069 1.00 21.64 ?  337 THR B CB  1 
ATOM   3273 O OG1 . THR B 1 114 ? -7.000  -3.347  -36.868 1.00 22.58 ?  337 THR B OG1 1 
ATOM   3274 C CG2 . THR B 1 114 ? -9.238  -3.606  -37.728 1.00 19.79 ?  337 THR B CG2 1 
ATOM   3275 N N   . THR B 1 115 ? -9.024  -6.140  -39.877 1.00 22.53 ?  338 THR B N   1 
ATOM   3276 C CA  . THR B 1 115 ? -10.011 -6.398  -40.916 1.00 22.70 ?  338 THR B CA  1 
ATOM   3277 C C   . THR B 1 115 ? -11.232 -5.517  -40.679 1.00 23.87 ?  338 THR B C   1 
ATOM   3278 O O   . THR B 1 115 ? -11.827 -5.546  -39.597 1.00 22.31 ?  338 THR B O   1 
ATOM   3279 C CB  . THR B 1 115 ? -10.407 -7.874  -40.929 1.00 24.24 ?  338 THR B CB  1 
ATOM   3280 O OG1 . THR B 1 115 ? -9.229  -8.685  -41.016 1.00 23.57 ?  338 THR B OG1 1 
ATOM   3281 C CG2 . THR B 1 115 ? -11.309 -8.171  -42.117 1.00 22.07 ?  338 THR B CG2 1 
ATOM   3282 N N   . ARG B 1 116 ? -11.603 -4.732  -41.690 1.00 25.51 ?  339 ARG B N   1 
ATOM   3283 C CA  . ARG B 1 116 ? -12.613 -3.695  -41.513 1.00 24.91 ?  339 ARG B CA  1 
ATOM   3284 C C   . ARG B 1 116 ? -14.037 -4.233  -41.449 1.00 24.65 ?  339 ARG B C   1 
ATOM   3285 O O   . ARG B 1 116 ? -14.952 -3.463  -41.137 1.00 26.46 ?  339 ARG B O   1 
ATOM   3286 C CB  . ARG B 1 116 ? -12.507 -2.663  -42.638 1.00 23.18 ?  339 ARG B CB  1 
ATOM   3287 C CG  . ARG B 1 116 ? -13.204 -3.062  -43.926 1.00 28.04 ?  339 ARG B CG  1 
ATOM   3288 C CD  . ARG B 1 116 ? -12.836 -2.110  -45.051 1.00 27.98 ?  339 ARG B CD  1 
ATOM   3289 N NE  . ARG B 1 116 ? -11.566 -2.475  -45.666 1.00 29.23 ?  339 ARG B NE  1 
ATOM   3290 C CZ  . ARG B 1 116 ? -10.521 -1.666  -45.763 1.00 23.97 ?  339 ARG B CZ  1 
ATOM   3291 N NH1 . ARG B 1 116 ? -10.562 -0.426  -45.304 1.00 31.34 ?  339 ARG B NH1 1 
ATOM   3292 N NH2 . ARG B 1 116 ? -9.407  -2.111  -46.337 1.00 25.44 ?  339 ARG B NH2 1 
ATOM   3293 N N   . THR B 1 117 ? -14.254 -5.518  -41.730 1.00 23.95 ?  340 THR B N   1 
ATOM   3294 C CA  . THR B 1 117 ? -15.605 -6.065  -41.659 1.00 25.61 ?  340 THR B CA  1 
ATOM   3295 C C   . THR B 1 117 ? -15.999 -6.382  -40.220 1.00 24.87 ?  340 THR B C   1 
ATOM   3296 O O   . THR B 1 117 ? -16.999 -5.866  -39.710 1.00 26.37 ?  340 THR B O   1 
ATOM   3297 C CB  . THR B 1 117 ? -15.723 -7.316  -42.536 1.00 27.07 ?  340 THR B CB  1 
ATOM   3298 O OG1 . THR B 1 117 ? -14.560 -8.135  -42.371 1.00 32.12 ?  340 THR B OG1 1 
ATOM   3299 C CG2 . THR B 1 117 ? -15.868 -6.932  -44.002 1.00 24.66 ?  340 THR B CG2 1 
ATOM   3300 N N   . ASP B 1 118 ? -15.218 -7.225  -39.546 1.00 24.05 ?  341 ASP B N   1 
ATOM   3301 C CA  . ASP B 1 118 ? -15.553 -7.691  -38.207 1.00 23.55 ?  341 ASP B CA  1 
ATOM   3302 C C   . ASP B 1 118 ? -14.658 -7.113  -37.119 1.00 24.04 ?  341 ASP B C   1 
ATOM   3303 O O   . ASP B 1 118 ? -14.894 -7.383  -35.937 1.00 20.88 ?  341 ASP B O   1 
ATOM   3304 C CB  . ASP B 1 118 ? -15.501 -9.224  -38.154 1.00 22.95 ?  341 ASP B CB  1 
ATOM   3305 C CG  . ASP B 1 118 ? -14.181 -9.787  -38.656 1.00 23.56 ?  341 ASP B CG  1 
ATOM   3306 O OD1 . ASP B 1 118 ? -13.214 -9.013  -38.821 1.00 25.54 ?  341 ASP B OD1 1 
ATOM   3307 O OD2 . ASP B 1 118 ? -14.109 -11.013 -38.882 1.00 25.63 ?  341 ASP B OD2 1 
ATOM   3308 N N   . GLY B 1 119 ? -13.641 -6.335  -37.479 1.00 22.61 ?  342 GLY B N   1 
ATOM   3309 C CA  . GLY B 1 119 ? -12.731 -5.817  -36.477 1.00 22.03 ?  342 GLY B CA  1 
ATOM   3310 C C   . GLY B 1 119 ? -11.774 -6.837  -35.905 1.00 22.21 ?  342 GLY B C   1 
ATOM   3311 O O   . GLY B 1 119 ? -11.242 -6.626  -34.812 1.00 23.41 ?  342 GLY B O   1 
ATOM   3312 N N   . SER B 1 120 ? -11.550 -7.946  -36.604 1.00 21.26 ?  343 SER B N   1 
ATOM   3313 C CA  . SER B 1 120 ? -10.546 -8.908  -36.174 1.00 23.60 ?  343 SER B CA  1 
ATOM   3314 C C   . SER B 1 120 ? -9.150  -8.352  -36.423 1.00 22.57 ?  343 SER B C   1 
ATOM   3315 O O   . SER B 1 120 ? -8.904  -7.640  -37.401 1.00 18.29 ?  343 SER B O   1 
ATOM   3316 C CB  . SER B 1 120 ? -10.725 -10.237 -36.907 1.00 20.13 ?  343 SER B CB  1 
ATOM   3317 O OG  . SER B 1 120 ? -10.503 -10.087 -38.298 1.00 21.18 ?  343 SER B OG  1 
ATOM   3318 N N   . THR B 1 121 ? -8.229  -8.677  -35.519 1.00 22.36 ?  344 THR B N   1 
ATOM   3319 C CA  . THR B 1 121 ? -6.891  -8.109  -35.536 1.00 23.32 ?  344 THR B CA  1 
ATOM   3320 C C   . THR B 1 121 ? -5.847  -9.216  -35.495 1.00 23.73 ?  344 THR B C   1 
ATOM   3321 O O   . THR B 1 121 ? -6.142  -10.369 -35.170 1.00 22.71 ?  344 THR B O   1 
ATOM   3322 C CB  . THR B 1 121 ? -6.675  -7.150  -34.358 1.00 23.71 ?  344 THR B CB  1 
ATOM   3323 O OG1 . THR B 1 121 ? -6.696  -7.887  -33.130 1.00 20.86 ?  344 THR B OG1 1 
ATOM   3324 C CG2 . THR B 1 121 ? -7.764  -6.084  -34.325 1.00 21.29 ?  344 THR B CG2 1 
ATOM   3325 N N   . ARG B 1 122 ? -4.612  -8.844  -35.829 1.00 25.58 ?  345 ARG B N   1 
ATOM   3326 C CA  . ARG B 1 122 ? -3.497  -9.780  -35.836 1.00 23.39 ?  345 ARG B CA  1 
ATOM   3327 C C   . ARG B 1 122 ? -2.192  -8.998  -35.832 1.00 25.41 ?  345 ARG B C   1 
ATOM   3328 O O   . ARG B 1 122 ? -2.109  -7.902  -36.392 1.00 22.63 ?  345 ARG B O   1 
ATOM   3329 C CB  . ARG B 1 122 ? -3.552  -10.715 -37.050 1.00 20.63 ?  345 ARG B CB  1 
ATOM   3330 C CG  . ARG B 1 122 ? -3.694  -9.997  -38.381 1.00 23.90 ?  345 ARG B CG  1 
ATOM   3331 C CD  . ARG B 1 122 ? -4.336  -10.898 -39.422 1.00 24.86 ?  345 ARG B CD  1 
ATOM   3332 N NE  . ARG B 1 122 ? -5.713  -11.230 -39.073 1.00 26.34 ?  345 ARG B NE  1 
ATOM   3333 C CZ  . ARG B 1 122 ? -6.755  -10.442 -39.299 1.00 23.67 ?  345 ARG B CZ  1 
ATOM   3334 N NH1 . ARG B 1 122 ? -6.617  -9.265  -39.888 1.00 23.93 ?  345 ARG B NH1 1 
ATOM   3335 N NH2 . ARG B 1 122 ? -7.966  -10.844 -38.924 1.00 19.86 ?  345 ARG B NH2 1 
ATOM   3336 N N   . GLY B 1 123 ? -1.177  -9.578  -35.195 1.00 25.16 ?  346 GLY B N   1 
ATOM   3337 C CA  . GLY B 1 123 ? 0.138   -8.971  -35.126 1.00 23.29 ?  346 GLY B CA  1 
ATOM   3338 C C   . GLY B 1 123 ? 1.252   -9.995  -35.188 1.00 27.06 ?  346 GLY B C   1 
ATOM   3339 O O   . GLY B 1 123 ? 1.140   -11.072 -34.594 1.00 28.84 ?  346 GLY B O   1 
ATOM   3340 N N   . HIS B 1 124 ? 2.335   -9.679  -35.896 1.00 24.77 ?  347 HIS B N   1 
ATOM   3341 C CA  . HIS B 1 124 ? 3.419   -10.630 -36.095 1.00 25.62 ?  347 HIS B CA  1 
ATOM   3342 C C   . HIS B 1 124 ? 4.762   -9.918  -36.050 1.00 24.86 ?  347 HIS B C   1 
ATOM   3343 O O   . HIS B 1 124 ? 4.886   -8.764  -36.468 1.00 25.20 ?  347 HIS B O   1 
ATOM   3344 C CB  . HIS B 1 124 ? 3.273   -11.374 -37.429 1.00 25.41 ?  347 HIS B CB  1 
ATOM   3345 C CG  . HIS B 1 124 ? 2.098   -12.301 -37.479 1.00 30.04 ?  347 HIS B CG  1 
ATOM   3346 N ND1 . HIS B 1 124 ? 2.126   -13.568 -36.937 1.00 28.85 ?  347 HIS B ND1 1 
ATOM   3347 C CD2 . HIS B 1 124 ? 0.862   -12.145 -38.008 1.00 29.11 ?  347 HIS B CD2 1 
ATOM   3348 C CE1 . HIS B 1 124 ? 0.957   -14.153 -37.130 1.00 28.03 ?  347 HIS B CE1 1 
ATOM   3349 N NE2 . HIS B 1 124 ? 0.172   -13.310 -37.777 1.00 30.75 ?  347 HIS B NE2 1 
ATOM   3350 N N   . LYS B 1 125 ? 5.766   -10.626 -35.530 1.00 27.10 ?  348 LYS B N   1 
ATOM   3351 C CA  . LYS B 1 125 ? 7.141   -10.149 -35.585 1.00 25.92 ?  348 LYS B CA  1 
ATOM   3352 C C   . LYS B 1 125 ? 7.532   -9.855  -37.026 1.00 25.33 ?  348 LYS B C   1 
ATOM   3353 O O   . LYS B 1 125 ? 7.192   -10.609 -37.942 1.00 24.50 ?  348 LYS B O   1 
ATOM   3354 C CB  . LYS B 1 125 ? 8.085   -11.198 -34.988 1.00 24.00 ?  348 LYS B CB  1 
ATOM   3355 C CG  . LYS B 1 125 ? 9.401   -10.650 -34.459 1.00 28.43 ?  348 LYS B CG  1 
ATOM   3356 C CD  . LYS B 1 125 ? 10.136  -11.706 -33.644 1.00 29.52 ?  348 LYS B CD  1 
ATOM   3357 C CE  . LYS B 1 125 ? 9.901   -11.526 -32.154 1.00 32.81 ?  348 LYS B CE  1 
ATOM   3358 N NZ  . LYS B 1 125 ? 11.112  -11.007 -31.460 1.00 34.95 ?  348 LYS B NZ  1 
ATOM   3359 N N   . ALA B 1 126 ? 8.241   -8.748  -37.230 1.00 23.90 ?  349 ALA B N   1 
ATOM   3360 C CA  . ALA B 1 126 ? 8.600   -8.332  -38.577 1.00 23.92 ?  349 ALA B CA  1 
ATOM   3361 C C   . ALA B 1 126 ? 9.896   -7.539  -38.549 1.00 24.46 ?  349 ALA B C   1 
ATOM   3362 O O   . ALA B 1 126 ? 10.150  -6.776  -37.614 1.00 24.91 ?  349 ALA B O   1 
ATOM   3363 C CB  . ALA B 1 126 ? 7.487   -7.495  -39.218 1.00 23.16 ?  349 ALA B CB  1 
ATOM   3364 N N   . THR B 1 127 ? 10.709  -7.731  -39.585 1.00 21.58 ?  350 THR B N   1 
ATOM   3365 C CA  . THR B 1 127 ? 11.941  -6.984  -39.781 1.00 24.35 ?  350 THR B CA  1 
ATOM   3366 C C   . THR B 1 127 ? 11.939  -6.390  -41.180 1.00 24.22 ?  350 THR B C   1 
ATOM   3367 O O   . THR B 1 127 ? 11.540  -7.052  -42.142 1.00 24.65 ?  350 THR B O   1 
ATOM   3368 C CB  . THR B 1 127 ? 13.181  -7.875  -39.599 1.00 25.31 ?  350 THR B CB  1 
ATOM   3369 O OG1 . THR B 1 127 ? 13.174  -8.453  -38.288 1.00 28.09 ?  350 THR B OG1 1 
ATOM   3370 C CG2 . THR B 1 127 ? 14.458  -7.066  -39.784 1.00 27.36 ?  350 THR B CG2 1 
ATOM   3371 N N   . VAL B 1 128 ? 12.367  -5.135  -41.286 1.00 23.97 ?  351 VAL B N   1 
ATOM   3372 C CA  . VAL B 1 128 ? 12.593  -4.487  -42.571 1.00 26.36 ?  351 VAL B CA  1 
ATOM   3373 C C   . VAL B 1 128 ? 14.076  -4.166  -42.678 1.00 25.52 ?  351 VAL B C   1 
ATOM   3374 O O   . VAL B 1 128 ? 14.656  -3.561  -41.769 1.00 24.30 ?  351 VAL B O   1 
ATOM   3375 C CB  . VAL B 1 128 ? 11.731  -3.220  -42.741 1.00 23.32 ?  351 VAL B CB  1 
ATOM   3376 C CG1 . VAL B 1 128 ? 11.839  -2.315  -41.519 1.00 22.48 ?  351 VAL B CG1 1 
ATOM   3377 C CG2 . VAL B 1 128 ? 12.126  -2.473  -44.010 1.00 24.91 ?  351 VAL B CG2 1 
ATOM   3378 N N   . TYR B 1 129 ? 14.693  -4.599  -43.772 1.00 27.06 ?  352 TYR B N   1 
ATOM   3379 C CA  . TYR B 1 129 ? 16.094  -4.308  -44.058 1.00 27.09 ?  352 TYR B CA  1 
ATOM   3380 C C   . TYR B 1 129 ? 16.117  -3.151  -45.051 1.00 24.93 ?  352 TYR B C   1 
ATOM   3381 O O   . TYR B 1 129 ? 15.850  -3.335  -46.241 1.00 25.03 ?  352 TYR B O   1 
ATOM   3382 C CB  . TYR B 1 129 ? 16.805  -5.543  -44.601 1.00 25.61 ?  352 TYR B CB  1 
ATOM   3383 C CG  . TYR B 1 129 ? 18.236  -5.302  -45.023 1.00 25.79 ?  352 TYR B CG  1 
ATOM   3384 C CD1 . TYR B 1 129 ? 19.079  -4.499  -44.267 1.00 27.11 ?  352 TYR B CD1 1 
ATOM   3385 C CD2 . TYR B 1 129 ? 18.746  -5.886  -46.175 1.00 27.78 ?  352 TYR B CD2 1 
ATOM   3386 C CE1 . TYR B 1 129 ? 20.389  -4.279  -44.649 1.00 28.41 ?  352 TYR B CE1 1 
ATOM   3387 C CE2 . TYR B 1 129 ? 20.053  -5.672  -46.566 1.00 28.95 ?  352 TYR B CE2 1 
ATOM   3388 C CZ  . TYR B 1 129 ? 20.870  -4.869  -45.800 1.00 31.80 ?  352 TYR B CZ  1 
ATOM   3389 O OH  . TYR B 1 129 ? 22.172  -4.655  -46.187 1.00 37.44 ?  352 TYR B OH  1 
ATOM   3390 N N   . THR B 1 130 ? 16.429  -1.952  -44.556 1.00 24.71 ?  353 THR B N   1 
ATOM   3391 C CA  . THR B 1 130 ? 16.407  -0.757  -45.393 1.00 24.96 ?  353 THR B CA  1 
ATOM   3392 C C   . THR B 1 130 ? 17.519  -0.733  -46.434 1.00 26.53 ?  353 THR B C   1 
ATOM   3393 O O   . THR B 1 130 ? 17.538  0.180   -47.267 1.00 27.81 ?  353 THR B O   1 
ATOM   3394 C CB  . THR B 1 130 ? 16.483  0.497   -44.522 1.00 27.15 ?  353 THR B CB  1 
ATOM   3395 O OG1 . THR B 1 130 ? 17.679  0.463   -43.736 1.00 23.16 ?  353 THR B OG1 1 
ATOM   3396 C CG2 . THR B 1 130 ? 15.279  0.573   -43.597 1.00 23.96 ?  353 THR B CG2 1 
ATOM   3397 N N   . GLY B 1 131 ? 18.437  -1.694  -46.408 1.00 24.90 ?  354 GLY B N   1 
ATOM   3398 C CA  . GLY B 1 131 ? 19.410  -1.872  -47.462 1.00 25.10 ?  354 GLY B CA  1 
ATOM   3399 C C   . GLY B 1 131 ? 19.030  -2.904  -48.499 1.00 27.24 ?  354 GLY B C   1 
ATOM   3400 O O   . GLY B 1 131 ? 19.789  -3.115  -49.451 1.00 27.45 ?  354 GLY B O   1 
ATOM   3401 N N   . SER B 1 132 ? 17.873  -3.545  -48.351 1.00 22.90 ?  355 SER B N   1 
ATOM   3402 C CA  . SER B 1 132 ? 17.471  -4.611  -49.258 1.00 27.40 ?  355 SER B CA  1 
ATOM   3403 C C   . SER B 1 132 ? 17.126  -4.058  -50.636 1.00 33.26 ?  355 SER B C   1 
ATOM   3404 O O   . SER B 1 132 ? 16.712  -2.904  -50.786 1.00 30.30 ?  355 SER B O   1 
ATOM   3405 C CB  . SER B 1 132 ? 16.275  -5.374  -48.686 1.00 28.47 ?  355 SER B CB  1 
ATOM   3406 O OG  . SER B 1 132 ? 15.370  -5.761  -49.705 1.00 37.94 ?  355 SER B OG  1 
ATOM   3407 N N   . ALA B 1 133 ? 17.298  -4.908  -51.653 1.00 31.18 ?  356 ALA B N   1 
ATOM   3408 C CA  . ALA B 1 133 ? 17.036  -4.493  -53.026 1.00 30.63 ?  356 ALA B CA  1 
ATOM   3409 C C   . ALA B 1 133 ? 15.575  -4.122  -53.236 1.00 28.82 ?  356 ALA B C   1 
ATOM   3410 O O   . ALA B 1 133 ? 15.264  -3.285  -54.091 1.00 26.22 ?  356 ALA B O   1 
ATOM   3411 C CB  . ALA B 1 133 ? 17.448  -5.601  -53.995 1.00 30.29 ?  356 ALA B CB  1 
ATOM   3412 N N   . ASP B 1 134 ? 14.666  -4.728  -52.472 1.00 32.62 ?  357 ASP B N   1 
ATOM   3413 C CA  . ASP B 1 134 ? 13.245  -4.429  -52.567 1.00 29.87 ?  357 ASP B CA  1 
ATOM   3414 C C   . ASP B 1 134 ? 12.790  -3.417  -51.521 1.00 28.43 ?  357 ASP B C   1 
ATOM   3415 O O   . ASP B 1 134 ? 11.594  -3.342  -51.218 1.00 30.67 ?  357 ASP B O   1 
ATOM   3416 C CB  . ASP B 1 134 ? 12.424  -5.715  -52.464 1.00 36.97 ?  357 ASP B CB  1 
ATOM   3417 C CG  . ASP B 1 134 ? 12.686  -6.664  -53.619 1.00 41.44 ?  357 ASP B CG  1 
ATOM   3418 O OD1 . ASP B 1 134 ? 12.631  -6.213  -54.783 1.00 44.08 ?  357 ASP B OD1 1 
ATOM   3419 O OD2 . ASP B 1 134 ? 12.954  -7.857  -53.365 1.00 51.02 ?  357 ASP B OD2 1 
ATOM   3420 N N   . PHE B 1 135 ? 13.717  -2.644  -50.960 1.00 27.44 ?  358 PHE B N   1 
ATOM   3421 C CA  . PHE B 1 135 ? 13.365  -1.473  -50.159 1.00 26.42 ?  358 PHE B CA  1 
ATOM   3422 C C   . PHE B 1 135 ? 13.295  -0.292  -51.117 1.00 22.93 ?  358 PHE B C   1 
ATOM   3423 O O   . PHE B 1 135 ? 14.292  0.378   -51.389 1.00 23.25 ?  358 PHE B O   1 
ATOM   3424 C CB  . PHE B 1 135 ? 14.373  -1.238  -49.042 1.00 24.07 ?  358 PHE B CB  1 
ATOM   3425 C CG  . PHE B 1 135 ? 14.044  -0.057  -48.171 1.00 22.60 ?  358 PHE B CG  1 
ATOM   3426 C CD1 . PHE B 1 135 ? 13.034  -0.137  -47.226 1.00 22.94 ?  358 PHE B CD1 1 
ATOM   3427 C CD2 . PHE B 1 135 ? 14.735  1.137   -48.305 1.00 24.09 ?  358 PHE B CD2 1 
ATOM   3428 C CE1 . PHE B 1 135 ? 12.725  0.948   -46.425 1.00 18.63 ?  358 PHE B CE1 1 
ATOM   3429 C CE2 . PHE B 1 135 ? 14.430  2.225   -47.507 1.00 23.38 ?  358 PHE B CE2 1 
ATOM   3430 C CZ  . PHE B 1 135 ? 13.423  2.130   -46.567 1.00 20.87 ?  358 PHE B CZ  1 
ATOM   3431 N N   . ALA B 1 136 ? 12.101  -0.042  -51.649 1.00 23.06 ?  359 ALA B N   1 
ATOM   3432 C CA  . ALA B 1 136 ? 11.871  1.044   -52.602 1.00 23.58 ?  359 ALA B CA  1 
ATOM   3433 C C   . ALA B 1 136 ? 10.717  1.924   -52.133 1.00 22.19 ?  359 ALA B C   1 
ATOM   3434 O O   . ALA B 1 136 ? 9.681   2.016   -52.798 1.00 23.44 ?  359 ALA B O   1 
ATOM   3435 C CB  . ALA B 1 136 ? 11.599  0.483   -53.996 1.00 21.49 ?  359 ALA B CB  1 
ATOM   3436 N N   . PRO B 1 137 ? 10.863  2.591   -50.982 1.00 21.84 ?  360 PRO B N   1 
ATOM   3437 C CA  . PRO B 1 137 ? 9.747   3.401   -50.468 1.00 20.18 ?  360 PRO B CA  1 
ATOM   3438 C C   . PRO B 1 137 ? 9.314   4.513   -51.407 1.00 19.99 ?  360 PRO B C   1 
ATOM   3439 O O   . PRO B 1 137 ? 8.117   4.819   -51.470 1.00 18.11 ?  360 PRO B O   1 
ATOM   3440 C CB  . PRO B 1 137 ? 10.301  3.960   -49.149 1.00 20.42 ?  360 PRO B CB  1 
ATOM   3441 C CG  . PRO B 1 137 ? 11.787  3.881   -49.300 1.00 22.92 ?  360 PRO B CG  1 
ATOM   3442 C CD  . PRO B 1 137 ? 12.013  2.620   -50.063 1.00 22.68 ?  360 PRO B CD  1 
ATOM   3443 N N   . LYS B 1 138 ? 10.246  5.122   -52.146 1.00 21.90 ?  361 LYS B N   1 
ATOM   3444 C CA  . LYS B 1 138 ? 9.875   6.208   -53.049 1.00 21.57 ?  361 LYS B CA  1 
ATOM   3445 C C   . LYS B 1 138 ? 8.971   5.717   -54.174 1.00 21.63 ?  361 LYS B C   1 
ATOM   3446 O O   . LYS B 1 138 ? 8.106   6.467   -54.643 1.00 22.35 ?  361 LYS B O   1 
ATOM   3447 C CB  . LYS B 1 138 ? 11.133  6.877   -53.610 1.00 22.43 ?  361 LYS B CB  1 
ATOM   3448 C CG  . LYS B 1 138 ? 10.893  7.793   -54.804 1.00 19.62 ?  361 LYS B CG  1 
ATOM   3449 C CD  . LYS B 1 138 ? 10.223  9.098   -54.390 1.00 20.88 ?  361 LYS B CD  1 
ATOM   3450 C CE  . LYS B 1 138 ? 10.491  10.200  -55.407 1.00 20.72 ?  361 LYS B CE  1 
ATOM   3451 N NZ  . LYS B 1 138 ? 9.689   11.427  -55.136 1.00 19.39 ?  361 LYS B NZ  1 
ATOM   3452 N N   . LEU B 1 139 ? 9.140   4.469   -54.610 1.00 19.82 ?  362 LEU B N   1 
ATOM   3453 C CA  . LEU B 1 139 ? 8.223   3.874   -55.574 1.00 21.79 ?  362 LEU B CA  1 
ATOM   3454 C C   . LEU B 1 139 ? 6.939   3.367   -54.928 1.00 21.46 ?  362 LEU B C   1 
ATOM   3455 O O   . LEU B 1 139 ? 6.053   2.888   -55.642 1.00 26.71 ?  362 LEU B O   1 
ATOM   3456 C CB  . LEU B 1 139 ? 8.907   2.727   -56.326 1.00 19.45 ?  362 LEU B CB  1 
ATOM   3457 C CG  . LEU B 1 139 ? 10.193  3.045   -57.091 1.00 21.32 ?  362 LEU B CG  1 
ATOM   3458 C CD1 . LEU B 1 139 ? 10.694  1.810   -57.826 1.00 18.32 ?  362 LEU B CD1 1 
ATOM   3459 C CD2 . LEU B 1 139 ? 9.982   4.200   -58.059 1.00 20.73 ?  362 LEU B CD2 1 
ATOM   3460 N N   . GLY B 1 140 ? 6.820   3.461   -53.607 1.00 18.82 ?  363 GLY B N   1 
ATOM   3461 C CA  . GLY B 1 140 ? 5.619   3.039   -52.915 1.00 19.25 ?  363 GLY B CA  1 
ATOM   3462 C C   . GLY B 1 140 ? 5.612   1.604   -52.444 1.00 22.36 ?  363 GLY B C   1 
ATOM   3463 O O   . GLY B 1 140 ? 4.540   1.086   -52.110 1.00 22.03 ?  363 GLY B O   1 
ATOM   3464 N N   . ARG B 1 141 ? 6.771   0.947   -52.386 1.00 20.95 ?  364 ARG B N   1 
ATOM   3465 C CA  . ARG B 1 141 ? 6.842   -0.478  -52.088 1.00 22.59 ?  364 ARG B CA  1 
ATOM   3466 C C   . ARG B 1 141 ? 7.957   -0.751  -51.091 1.00 24.54 ?  364 ARG B C   1 
ATOM   3467 O O   . ARG B 1 141 ? 9.087   -0.294  -51.281 1.00 24.39 ?  364 ARG B O   1 
ATOM   3468 C CB  . ARG B 1 141 ? 7.084   -1.287  -53.366 1.00 24.82 ?  364 ARG B CB  1 
ATOM   3469 C CG  . ARG B 1 141 ? 5.825   -1.717  -54.091 1.00 31.42 ?  364 ARG B CG  1 
ATOM   3470 C CD  . ARG B 1 141 ? 6.156   -2.700  -55.203 1.00 33.56 ?  364 ARG B CD  1 
ATOM   3471 N NE  . ARG B 1 141 ? 7.516   -2.522  -55.701 1.00 32.06 ?  364 ARG B NE  1 
ATOM   3472 C CZ  . ARG B 1 141 ? 7.832   -1.833  -56.789 1.00 37.56 ?  364 ARG B CZ  1 
ATOM   3473 N NH1 . ARG B 1 141 ? 6.907   -1.239  -57.525 1.00 37.53 ?  364 ARG B NH1 1 
ATOM   3474 N NH2 . ARG B 1 141 ? 9.110   -1.739  -57.149 1.00 33.36 ?  364 ARG B NH2 1 
ATOM   3475 N N   . VAL B 1 142 ? 7.642   -1.508  -50.040 1.00 21.71 ?  365 VAL B N   1 
ATOM   3476 C CA  . VAL B 1 142 ? 8.624   -1.945  -49.053 1.00 23.50 ?  365 VAL B CA  1 
ATOM   3477 C C   . VAL B 1 142 ? 8.332   -3.402  -48.716 1.00 23.19 ?  365 VAL B C   1 
ATOM   3478 O O   . VAL B 1 142 ? 7.178   -3.841  -48.730 1.00 24.71 ?  365 VAL B O   1 
ATOM   3479 C CB  . VAL B 1 142 ? 8.605   -1.049  -47.786 1.00 22.19 ?  365 VAL B CB  1 
ATOM   3480 C CG1 . VAL B 1 142 ? 9.405   -1.671  -46.645 1.00 24.00 ?  365 VAL B CG1 1 
ATOM   3481 C CG2 . VAL B 1 142 ? 9.146   0.338   -48.104 1.00 24.91 ?  365 VAL B CG2 1 
ATOM   3482 N N   . GLN B 1 143 ? 9.390   -4.161  -48.435 1.00 22.88 ?  366 GLN B N   1 
ATOM   3483 C CA  . GLN B 1 143 ? 9.289   -5.582  -48.133 1.00 28.00 ?  366 GLN B CA  1 
ATOM   3484 C C   . GLN B 1 143 ? 9.608   -5.840  -46.665 1.00 25.99 ?  366 GLN B C   1 
ATOM   3485 O O   . GLN B 1 143 ? 10.556  -5.270  -46.115 1.00 20.88 ?  366 GLN B O   1 
ATOM   3486 C CB  . GLN B 1 143 ? 10.236  -6.392  -49.022 1.00 30.08 ?  366 GLN B CB  1 
ATOM   3487 C CG  . GLN B 1 143 ? 10.201  -7.889  -48.771 1.00 31.40 ?  366 GLN B CG  1 
ATOM   3488 C CD  . GLN B 1 143 ? 10.844  -8.678  -49.892 1.00 38.33 ?  366 GLN B CD  1 
ATOM   3489 O OE1 . GLN B 1 143 ? 10.503  -8.506  -51.063 1.00 38.87 ?  366 GLN B OE1 1 
ATOM   3490 N NE2 . GLN B 1 143 ? 11.781  -9.550  -49.540 1.00 41.16 ?  366 GLN B NE2 1 
ATOM   3491 N N   . PHE B 1 144 ? 8.812   -6.705  -46.037 1.00 26.38 ?  367 PHE B N   1 
ATOM   3492 C CA  . PHE B 1 144 ? 9.014   -7.119  -44.655 1.00 24.28 ?  367 PHE B CA  1 
ATOM   3493 C C   . PHE B 1 144 ? 9.218   -8.626  -44.588 1.00 25.10 ?  367 PHE B C   1 
ATOM   3494 O O   . PHE B 1 144 ? 8.583   -9.380  -45.331 1.00 23.72 ?  367 PHE B O   1 
ATOM   3495 C CB  . PHE B 1 144 ? 7.820   -6.744  -43.766 1.00 23.08 ?  367 PHE B CB  1 
ATOM   3496 C CG  . PHE B 1 144 ? 7.574   -5.268  -43.654 1.00 23.40 ?  367 PHE B CG  1 
ATOM   3497 C CD1 . PHE B 1 144 ? 8.210   -4.519  -42.678 1.00 21.79 ?  367 PHE B CD1 1 
ATOM   3498 C CD2 . PHE B 1 144 ? 6.684   -4.635  -44.505 1.00 21.65 ?  367 PHE B CD2 1 
ATOM   3499 C CE1 . PHE B 1 144 ? 7.977   -3.162  -42.564 1.00 21.86 ?  367 PHE B CE1 1 
ATOM   3500 C CE2 . PHE B 1 144 ? 6.446   -3.277  -44.396 1.00 23.30 ?  367 PHE B CE2 1 
ATOM   3501 C CZ  . PHE B 1 144 ? 7.094   -2.540  -43.424 1.00 20.78 ?  367 PHE B CZ  1 
ATOM   3502 N N   . GLU B 1 145 ? 10.102  -9.059  -43.692 1.00 27.89 ?  368 GLU B N   1 
ATOM   3503 C CA  . GLU B 1 145 ? 10.237  -10.466 -43.335 1.00 25.88 ?  368 GLU B CA  1 
ATOM   3504 C C   . GLU B 1 145 ? 9.512   -10.694 -42.015 1.00 23.56 ?  368 GLU B C   1 
ATOM   3505 O O   . GLU B 1 145 ? 9.850   -10.070 -41.004 1.00 28.12 ?  368 GLU B O   1 
ATOM   3506 C CB  . GLU B 1 145 ? 11.704  -10.879 -43.219 1.00 26.77 ?  368 GLU B CB  1 
ATOM   3507 C CG  . GLU B 1 145 ? 12.642  -10.199 -44.201 1.00 32.90 ?  368 GLU B CG  1 
ATOM   3508 C CD  . GLU B 1 145 ? 13.918  -10.992 -44.424 1.00 43.02 ?  368 GLU B CD  1 
ATOM   3509 O OE1 . GLU B 1 145 ? 14.794  -10.974 -43.533 1.00 42.35 ?  368 GLU B OE1 1 
ATOM   3510 O OE2 . GLU B 1 145 ? 14.043  -11.640 -45.486 1.00 43.76 ?  368 GLU B OE2 1 
ATOM   3511 N N   . THR B 1 146 ? 8.521   -11.580 -42.025 1.00 25.75 ?  369 THR B N   1 
ATOM   3512 C CA  . THR B 1 146 ? 7.689   -11.838 -40.862 1.00 26.34 ?  369 THR B CA  1 
ATOM   3513 C C   . THR B 1 146 ? 7.932   -13.255 -40.342 1.00 29.45 ?  369 THR B C   1 
ATOM   3514 O O   . THR B 1 146 ? 8.903   -13.922 -40.716 1.00 31.96 ?  369 THR B O   1 
ATOM   3515 C CB  . THR B 1 146 ? 6.214   -11.613 -41.208 1.00 24.93 ?  369 THR B CB  1 
ATOM   3516 O OG1 . THR B 1 146 ? 5.721   -12.729 -41.960 1.00 25.29 ?  369 THR B OG1 1 
ATOM   3517 C CG2 . THR B 1 146 ? 6.046   -10.342 -42.028 1.00 25.64 ?  369 THR B CG2 1 
ATOM   3518 N N   . ASP B 1 147 ? 7.039   -13.712 -39.462 1.00 25.34 ?  370 ASP B N   1 
ATOM   3519 C CA  . ASP B 1 147 ? 7.080   -15.066 -38.921 1.00 29.34 ?  370 ASP B CA  1 
ATOM   3520 C C   . ASP B 1 147 ? 5.850   -15.865 -39.339 1.00 31.01 ?  370 ASP B C   1 
ATOM   3521 O O   . ASP B 1 147 ? 5.436   -16.794 -38.643 1.00 31.13 ?  370 ASP B O   1 
ATOM   3522 C CB  . ASP B 1 147 ? 7.217   -15.042 -37.397 1.00 30.30 ?  370 ASP B CB  1 
ATOM   3523 C CG  . ASP B 1 147 ? 6.049   -14.351 -36.707 1.00 32.59 ?  370 ASP B CG  1 
ATOM   3524 O OD1 . ASP B 1 147 ? 5.136   -13.859 -37.402 1.00 32.79 ?  370 ASP B OD1 1 
ATOM   3525 O OD2 . ASP B 1 147 ? 6.045   -14.304 -35.459 1.00 29.59 ?  370 ASP B OD2 1 
ATOM   3526 N N   . THR B 1 148 ? 5.254   -15.507 -40.474 1.00 31.21 ?  371 THR B N   1 
ATOM   3527 C CA  . THR B 1 148 ? 4.047   -16.166 -40.947 1.00 31.29 ?  371 THR B CA  1 
ATOM   3528 C C   . THR B 1 148 ? 4.037   -16.159 -42.467 1.00 30.34 ?  371 THR B C   1 
ATOM   3529 O O   . THR B 1 148 ? 4.682   -15.327 -43.110 1.00 31.29 ?  371 THR B O   1 
ATOM   3530 C CB  . THR B 1 148 ? 2.779   -15.488 -40.411 1.00 29.65 ?  371 THR B CB  1 
ATOM   3531 O OG1 . THR B 1 148 ? 1.623   -16.184 -40.893 1.00 29.48 ?  371 THR B OG1 1 
ATOM   3532 C CG2 . THR B 1 148 ? 2.716   -14.036 -40.867 1.00 27.81 ?  371 THR B CG2 1 
ATOM   3533 N N   . ASP B 1 149 ? 3.288   -17.105 -43.036 1.00 31.25 ?  372 ASP B N   1 
ATOM   3534 C CA  . ASP B 1 149 ? 3.113   -17.192 -44.481 1.00 32.59 ?  372 ASP B CA  1 
ATOM   3535 C C   . ASP B 1 149 ? 1.641   -17.282 -44.865 1.00 33.39 ?  372 ASP B C   1 
ATOM   3536 O O   . ASP B 1 149 ? 1.324   -17.725 -45.974 1.00 35.82 ?  372 ASP B O   1 
ATOM   3537 C CB  . ASP B 1 149 ? 3.876   -18.392 -45.050 1.00 33.31 ?  372 ASP B CB  1 
ATOM   3538 C CG  . ASP B 1 149 ? 3.417   -19.710 -44.454 1.00 38.37 ?  372 ASP B CG  1 
ATOM   3539 O OD1 . ASP B 1 149 ? 3.212   -19.771 -43.224 1.00 43.15 ?  372 ASP B OD1 1 
ATOM   3540 O OD2 . ASP B 1 149 ? 3.255   -20.685 -45.219 1.00 37.65 ?  372 ASP B OD2 1 
ATOM   3541 N N   . ARG B 1 150 ? 0.734   -16.867 -43.980 1.00 30.69 ?  373 ARG B N   1 
ATOM   3542 C CA  . ARG B 1 150 ? -0.687  -17.080 -44.225 1.00 32.13 ?  373 ARG B CA  1 
ATOM   3543 C C   . ARG B 1 150 ? -1.578  -16.095 -43.474 1.00 30.40 ?  373 ARG B C   1 
ATOM   3544 O O   . ARG B 1 150 ? -2.652  -15.732 -43.966 1.00 33.28 ?  373 ARG B O   1 
ATOM   3545 C CB  . ARG B 1 150 ? -1.068  -18.514 -43.845 1.00 32.20 ?  373 ARG B CB  1 
ATOM   3546 C CG  . ARG B 1 150 ? -0.324  -19.050 -42.628 1.00 36.54 ?  373 ARG B CG  1 
ATOM   3547 C CD  . ARG B 1 150 ? -0.756  -20.468 -42.294 1.00 34.55 ?  373 ARG B CD  1 
ATOM   3548 N NE  . ARG B 1 150 ? -0.408  -21.408 -43.353 1.00 42.73 ?  373 ARG B NE  1 
ATOM   3549 C CZ  . ARG B 1 150 ? 0.736   -22.076 -43.418 1.00 44.69 ?  373 ARG B CZ  1 
ATOM   3550 N NH1 . ARG B 1 150 ? 1.673   -21.933 -42.495 1.00 47.90 ?  373 ARG B NH1 1 
ATOM   3551 N NH2 . ARG B 1 150 ? 0.945   -22.908 -44.434 1.00 39.51 ?  373 ARG B NH2 1 
ATOM   3552 N N   . ASP B 1 151 ? -1.153  -15.656 -42.291 1.00 28.08 ?  374 ASP B N   1 
ATOM   3553 C CA  . ASP B 1 151 ? -2.024  -14.875 -41.409 1.00 28.80 ?  374 ASP B CA  1 
ATOM   3554 C C   . ASP B 1 151 ? -1.869  -13.373 -41.659 1.00 32.13 ?  374 ASP B C   1 
ATOM   3555 O O   . ASP B 1 151 ? -1.497  -12.594 -40.783 1.00 38.08 ?  374 ASP B O   1 
ATOM   3556 C CB  . ASP B 1 151 ? -1.750  -15.222 -39.951 1.00 27.43 ?  374 ASP B CB  1 
ATOM   3557 C CG  . ASP B 1 151 ? -2.903  -14.844 -39.043 1.00 27.80 ?  374 ASP B CG  1 
ATOM   3558 O OD1 . ASP B 1 151 ? -3.993  -15.435 -39.193 1.00 27.89 ?  374 ASP B OD1 1 
ATOM   3559 O OD2 . ASP B 1 151 ? -2.724  -13.956 -38.183 1.00 31.25 ?  374 ASP B OD2 1 
ATOM   3560 N N   . PHE B 1 152 ? -2.180  -12.978 -42.891 1.00 25.93 ?  375 PHE B N   1 
ATOM   3561 C CA  . PHE B 1 152 ? -2.291  -11.566 -43.252 1.00 24.33 ?  375 PHE B CA  1 
ATOM   3562 C C   . PHE B 1 152 ? -3.197  -11.474 -44.467 1.00 28.64 ?  375 PHE B C   1 
ATOM   3563 O O   . PHE B 1 152 ? -2.916  -12.100 -45.493 1.00 24.74 ?  375 PHE B O   1 
ATOM   3564 C CB  . PHE B 1 152 ? -0.922  -10.947 -43.547 1.00 24.58 ?  375 PHE B CB  1 
ATOM   3565 C CG  . PHE B 1 152 ? -0.240  -10.369 -42.338 1.00 26.84 ?  375 PHE B CG  1 
ATOM   3566 C CD1 . PHE B 1 152 ? -0.831  -9.345  -41.615 1.00 26.78 ?  375 PHE B CD1 1 
ATOM   3567 C CD2 . PHE B 1 152 ? 0.996   -10.842 -41.931 1.00 26.54 ?  375 PHE B CD2 1 
ATOM   3568 C CE1 . PHE B 1 152 ? -0.204  -8.809  -40.505 1.00 27.64 ?  375 PHE B CE1 1 
ATOM   3569 C CE2 . PHE B 1 152 ? 1.628   -10.311 -40.823 1.00 28.22 ?  375 PHE B CE2 1 
ATOM   3570 C CZ  . PHE B 1 152 ? 1.027   -9.293  -40.109 1.00 29.93 ?  375 PHE B CZ  1 
ATOM   3571 N N   . GLU B 1 153 ? -4.278  -10.708 -44.355 1.00 26.93 ?  376 GLU B N   1 
ATOM   3572 C CA  . GLU B 1 153 ? -5.233  -10.572 -45.442 1.00 23.56 ?  376 GLU B CA  1 
ATOM   3573 C C   . GLU B 1 153 ? -4.835  -9.433  -46.370 1.00 25.72 ?  376 GLU B C   1 
ATOM   3574 O O   . GLU B 1 153 ? -4.202  -8.457  -45.956 1.00 24.39 ?  376 GLU B O   1 
ATOM   3575 C CB  . GLU B 1 153 ? -6.642  -10.325 -44.901 1.00 22.63 ?  376 GLU B CB  1 
ATOM   3576 C CG  . GLU B 1 153 ? -7.157  -11.411 -43.977 1.00 24.03 ?  376 GLU B CG  1 
ATOM   3577 C CD  . GLU B 1 153 ? -8.377  -10.971 -43.193 1.00 31.77 ?  376 GLU B CD  1 
ATOM   3578 O OE1 . GLU B 1 153 ? -9.002  -9.963  -43.586 1.00 35.37 ?  376 GLU B OE1 1 
ATOM   3579 O OE2 . GLU B 1 153 ? -8.711  -11.631 -42.187 1.00 29.09 ?  376 GLU B OE2 1 
ATOM   3580 N N   . ALA B 1 154 ? -5.216  -9.565  -47.636 1.00 25.16 ?  377 ALA B N   1 
ATOM   3581 C CA  . ALA B 1 154 ? -4.978  -8.510  -48.607 1.00 23.52 ?  377 ALA B CA  1 
ATOM   3582 C C   . ALA B 1 154 ? -6.063  -7.445  -48.508 1.00 22.51 ?  377 ALA B C   1 
ATOM   3583 O O   . ALA B 1 154 ? -7.198  -7.718  -48.108 1.00 23.37 ?  377 ALA B O   1 
ATOM   3584 C CB  . ALA B 1 154 ? -4.930  -9.080  -50.025 1.00 26.14 ?  377 ALA B CB  1 
ATOM   3585 N N   . ASN B 1 155 ? -5.691  -6.215  -48.871 1.00 22.68 ?  378 ASN B N   1 
ATOM   3586 C CA  . ASN B 1 155 ? -6.611  -5.075  -48.887 1.00 25.92 ?  378 ASN B CA  1 
ATOM   3587 C C   . ASN B 1 155 ? -7.179  -4.788  -47.498 1.00 26.77 ?  378 ASN B C   1 
ATOM   3588 O O   . ASN B 1 155 ? -8.370  -4.514  -47.338 1.00 26.55 ?  378 ASN B O   1 
ATOM   3589 C CB  . ASN B 1 155 ? -7.739  -5.286  -49.901 1.00 26.27 ?  378 ASN B CB  1 
ATOM   3590 C CG  . ASN B 1 155 ? -7.229  -5.406  -51.323 1.00 26.67 ?  378 ASN B CG  1 
ATOM   3591 O OD1 . ASN B 1 155 ? -7.547  -6.362  -52.030 1.00 31.14 ?  378 ASN B OD1 1 
ATOM   3592 N ND2 . ASN B 1 155 ? -6.433  -4.432  -51.750 1.00 24.42 ?  378 ASN B ND2 1 
ATOM   3593 N N   . GLN B 1 156 ? -6.320  -4.846  -46.483 1.00 25.71 ?  379 GLN B N   1 
ATOM   3594 C CA  . GLN B 1 156 ? -6.694  -4.495  -45.121 1.00 25.12 ?  379 GLN B CA  1 
ATOM   3595 C C   . GLN B 1 156 ? -5.633  -3.580  -44.531 1.00 23.35 ?  379 GLN B C   1 
ATOM   3596 O O   . GLN B 1 156 ? -4.442  -3.733  -44.818 1.00 22.54 ?  379 GLN B O   1 
ATOM   3597 C CB  . GLN B 1 156 ? -6.865  -5.742  -44.241 1.00 24.79 ?  379 GLN B CB  1 
ATOM   3598 C CG  . GLN B 1 156 ? -7.987  -6.679  -44.678 1.00 25.04 ?  379 GLN B CG  1 
ATOM   3599 C CD  . GLN B 1 156 ? -9.364  -6.037  -44.613 1.00 24.25 ?  379 GLN B CD  1 
ATOM   3600 O OE1 . GLN B 1 156 ? -9.570  -5.041  -43.919 1.00 24.04 ?  379 GLN B OE1 1 
ATOM   3601 N NE2 . GLN B 1 156 ? -10.317 -6.614  -45.335 1.00 22.41 ?  379 GLN B NE2 1 
ATOM   3602 N N   . ASN B 1 157 ? -6.067  -2.599  -43.750 1.00 23.61 ?  380 ASN B N   1 
ATOM   3603 C CA  . ASN B 1 157 ? -5.171  -1.628  -43.070 1.00 22.64 ?  380 ASN B CA  1 
ATOM   3604 C C   . ASN B 1 157 ? -4.077  -2.347  -42.284 1.00 23.62 ?  380 ASN B C   1 
ATOM   3605 O O   . ASN B 1 157 ? -4.405  -3.084  -41.354 1.00 21.77 ?  380 ASN B O   1 
ATOM   3606 C CB  . ASN B 1 157 ? -5.988  -0.701  -42.173 1.00 23.11 ?  380 ASN B CB  1 
ATOM   3607 C CG  . ASN B 1 157 ? -6.764  0.362   -42.916 1.00 27.19 ?  380 ASN B CG  1 
ATOM   3608 O OD1 . ASN B 1 157 ? -7.375  0.097   -43.945 1.00 24.27 ?  380 ASN B OD1 1 
ATOM   3609 N ND2 . ASN B 1 157 ? -6.748  1.574   -42.395 1.00 28.35 ?  380 ASN B ND2 1 
ATOM   3610 N N   . THR B 1 158 ? -2.823  -2.121  -42.662 1.00 22.07 ?  381 THR B N   1 
ATOM   3611 C CA  . THR B 1 158 ? -1.681  -2.763  -42.026 1.00 22.60 ?  381 THR B CA  1 
ATOM   3612 C C   . THR B 1 158 ? -0.662  -1.707  -41.621 1.00 20.25 ?  381 THR B C   1 
ATOM   3613 O O   . THR B 1 158 ? -0.396  -0.768  -42.377 1.00 19.56 ?  381 THR B O   1 
ATOM   3614 C CB  . THR B 1 158 ? -1.032  -3.793  -42.963 1.00 21.83 ?  381 THR B CB  1 
ATOM   3615 O OG1 . THR B 1 158 ? -2.053  -4.587  -43.580 1.00 22.16 ?  381 THR B OG1 1 
ATOM   3616 C CG2 . THR B 1 158 ? -0.090  -4.703  -42.190 1.00 21.62 ?  381 THR B CG2 1 
ATOM   3617 N N   . LYS B 1 159 ? -0.093  -1.867  -40.427 1.00 18.84 ?  382 LYS B N   1 
ATOM   3618 C CA  . LYS B 1 159 ? 0.853   -0.909  -39.873 1.00 22.06 ?  382 LYS B CA  1 
ATOM   3619 C C   . LYS B 1 159 ? 2.093   -1.629  -39.366 1.00 21.19 ?  382 LYS B C   1 
ATOM   3620 O O   . LYS B 1 159 ? 2.000   -2.730  -38.814 1.00 18.33 ?  382 LYS B O   1 
ATOM   3621 C CB  . LYS B 1 159 ? 0.222   -0.104  -38.725 1.00 19.29 ?  382 LYS B CB  1 
ATOM   3622 C CG  . LYS B 1 159 ? 1.155   0.919   -38.091 1.00 20.27 ?  382 LYS B CG  1 
ATOM   3623 C CD  . LYS B 1 159 ? 0.502   1.621   -36.912 1.00 21.97 ?  382 LYS B CD  1 
ATOM   3624 C CE  . LYS B 1 159 ? 1.538   2.339   -36.060 1.00 23.57 ?  382 LYS B CE  1 
ATOM   3625 N NZ  . LYS B 1 159 ? 1.011   2.695   -34.714 1.00 24.72 ?  382 LYS B NZ  1 
ATOM   3626 N N   . PHE B 1 160 ? 3.251   -1.003  -39.555 1.00 23.01 ?  383 PHE B N   1 
ATOM   3627 C CA  . PHE B 1 160 ? 4.507   -1.461  -38.973 1.00 24.05 ?  383 PHE B CA  1 
ATOM   3628 C C   . PHE B 1 160 ? 4.912   -0.494  -37.869 1.00 23.07 ?  383 PHE B C   1 
ATOM   3629 O O   . PHE B 1 160 ? 5.098   0.701   -38.124 1.00 23.82 ?  383 PHE B O   1 
ATOM   3630 C CB  . PHE B 1 160 ? 5.611   -1.558  -40.026 1.00 21.34 ?  383 PHE B CB  1 
ATOM   3631 C CG  . PHE B 1 160 ? 6.963   -1.883  -39.453 1.00 20.99 ?  383 PHE B CG  1 
ATOM   3632 C CD1 . PHE B 1 160 ? 7.266   -3.173  -39.048 1.00 23.19 ?  383 PHE B CD1 1 
ATOM   3633 C CD2 . PHE B 1 160 ? 7.924   -0.897  -39.308 1.00 21.05 ?  383 PHE B CD2 1 
ATOM   3634 C CE1 . PHE B 1 160 ? 8.507   -3.475  -38.516 1.00 22.75 ?  383 PHE B CE1 1 
ATOM   3635 C CE2 . PHE B 1 160 ? 9.167   -1.192  -38.776 1.00 23.45 ?  383 PHE B CE2 1 
ATOM   3636 C CZ  . PHE B 1 160 ? 9.458   -2.483  -38.380 1.00 22.95 ?  383 PHE B CZ  1 
ATOM   3637 N N   . THR B 1 161 ? 5.045   -1.011  -36.648 1.00 20.72 ?  384 THR B N   1 
ATOM   3638 C CA  . THR B 1 161 ? 5.512   -0.212  -35.527 1.00 21.89 ?  384 THR B CA  1 
ATOM   3639 C C   . THR B 1 161 ? 6.960   -0.562  -35.235 1.00 23.18 ?  384 THR B C   1 
ATOM   3640 O O   . THR B 1 161 ? 7.248   -1.724  -34.907 1.00 22.60 ?  384 THR B O   1 
ATOM   3641 C CB  . THR B 1 161 ? 4.655   -0.458  -34.290 1.00 23.26 ?  384 THR B CB  1 
ATOM   3642 O OG1 . THR B 1 161 ? 3.319   -0.001  -34.532 1.00 25.46 ?  384 THR B OG1 1 
ATOM   3643 C CG2 . THR B 1 161 ? 5.229   0.280   -33.089 1.00 22.14 ?  384 THR B CG2 1 
ATOM   3644 N N   . PRO B 1 162 ? 7.894   0.379   -35.337 1.00 22.82 ?  385 PRO B N   1 
ATOM   3645 C CA  . PRO B 1 162 ? 9.291   0.055   -35.044 1.00 23.77 ?  385 PRO B CA  1 
ATOM   3646 C C   . PRO B 1 162 ? 9.512   -0.100  -33.550 1.00 20.71 ?  385 PRO B C   1 
ATOM   3647 O O   . PRO B 1 162 ? 8.854   0.543   -32.728 1.00 22.26 ?  385 PRO B O   1 
ATOM   3648 C CB  . PRO B 1 162 ? 10.054  1.263   -35.596 1.00 22.73 ?  385 PRO B CB  1 
ATOM   3649 C CG  . PRO B 1 162 ? 9.093   2.390   -35.427 1.00 21.80 ?  385 PRO B CG  1 
ATOM   3650 C CD  . PRO B 1 162 ? 7.720   1.803   -35.668 1.00 23.38 ?  385 PRO B CD  1 
ATOM   3651 N N   . VAL B 1 163 ? 10.447  -0.981  -33.202 1.00 22.15 ?  386 VAL B N   1 
ATOM   3652 C CA  . VAL B 1 163 ? 10.860  -1.199  -31.822 1.00 23.60 ?  386 VAL B CA  1 
ATOM   3653 C C   . VAL B 1 163 ? 12.352  -0.948  -31.644 1.00 22.45 ?  386 VAL B C   1 
ATOM   3654 O O   . VAL B 1 163 ? 12.764  -0.147  -30.800 1.00 25.51 ?  386 VAL B O   1 
ATOM   3655 C CB  . VAL B 1 163 ? 10.484  -2.617  -31.337 1.00 23.54 ?  386 VAL B CB  1 
ATOM   3656 C CG1 . VAL B 1 163 ? 11.014  -2.852  -29.932 1.00 22.89 ?  386 VAL B CG1 1 
ATOM   3657 C CG2 . VAL B 1 163 ? 8.976   -2.811  -31.381 1.00 23.70 ?  386 VAL B CG2 1 
ATOM   3658 N N   . GLY B 1 164 ? 13.177  -1.617  -32.439 1.00 22.15 ?  387 GLY B N   1 
ATOM   3659 C CA  . GLY B 1 164 ? 14.604  -1.429  -32.347 1.00 23.86 ?  387 GLY B CA  1 
ATOM   3660 C C   . GLY B 1 164 ? 15.315  -1.968  -33.566 1.00 24.74 ?  387 GLY B C   1 
ATOM   3661 O O   . GLY B 1 164 ? 14.698  -2.278  -34.587 1.00 24.28 ?  387 GLY B O   1 
ATOM   3662 N N   . VAL B 1 165 ? 16.634  -2.070  -33.443 1.00 24.09 ?  388 VAL B N   1 
ATOM   3663 C CA  . VAL B 1 165 ? 17.487  -2.579  -34.507 1.00 24.54 ?  388 VAL B CA  1 
ATOM   3664 C C   . VAL B 1 165 ? 18.027  -3.937  -34.091 1.00 28.09 ?  388 VAL B C   1 
ATOM   3665 O O   . VAL B 1 165 ? 18.221  -4.218  -32.903 1.00 26.66 ?  388 VAL B O   1 
ATOM   3666 C CB  . VAL B 1 165 ? 18.639  -1.605  -34.832 1.00 22.00 ?  388 VAL B CB  1 
ATOM   3667 C CG1 . VAL B 1 165 ? 18.089  -0.316  -35.417 1.00 23.99 ?  388 VAL B CG1 1 
ATOM   3668 C CG2 . VAL B 1 165 ? 19.465  -1.321  -33.587 1.00 22.34 ?  388 VAL B CG2 1 
ATOM   3669 N N   . ILE B 1 166 ? 18.256  -4.794  -35.083 1.00 28.44 ?  389 ILE B N   1 
ATOM   3670 C CA  . ILE B 1 166 ? 18.894  -6.078  -34.830 1.00 27.56 ?  389 ILE B CA  1 
ATOM   3671 C C   . ILE B 1 166 ? 20.221  -6.129  -35.567 1.00 28.88 ?  389 ILE B C   1 
ATOM   3672 O O   . ILE B 1 166 ? 20.667  -5.132  -36.147 1.00 29.60 ?  389 ILE B O   1 
ATOM   3673 C CB  . ILE B 1 166 ? 17.999  -7.264  -35.233 1.00 28.76 ?  389 ILE B CB  1 
ATOM   3674 C CG1 . ILE B 1 166 ? 17.890  -7.378  -36.754 1.00 27.92 ?  389 ILE B CG1 1 
ATOM   3675 C CG2 . ILE B 1 166 ? 16.637  -7.122  -34.609 1.00 28.98 ?  389 ILE B CG2 1 
ATOM   3676 C CD1 . ILE B 1 166 ? 16.759  -8.274  -37.214 1.00 28.57 ?  389 ILE B CD1 1 
ATOM   3677 N N   . GLN B 1 167 ? 20.847  -7.301  -35.561 1.00 36.67 ?  390 GLN B N   1 
ATOM   3678 C CA  . GLN B 1 167 ? 22.216  -7.421  -36.025 1.00 34.71 ?  390 GLN B CA  1 
ATOM   3679 C C   . GLN B 1 167 ? 22.575  -8.896  -36.169 1.00 36.34 ?  390 GLN B C   1 
ATOM   3680 O O   . GLN B 1 167 ? 22.714  -9.608  -35.169 1.00 34.93 ?  390 GLN B O   1 
ATOM   3681 C CB  . GLN B 1 167 ? 23.138  -6.690  -35.043 1.00 33.89 ?  390 GLN B CB  1 
ATOM   3682 C CG  . GLN B 1 167 ? 24.554  -6.498  -35.503 1.00 35.31 ?  390 GLN B CG  1 
ATOM   3683 C CD  . GLN B 1 167 ? 25.290  -7.796  -35.563 1.00 44.63 ?  390 GLN B CD  1 
ATOM   3684 O OE1 . GLN B 1 167 ? 25.296  -8.557  -34.594 1.00 44.40 ?  390 GLN B OE1 1 
ATOM   3685 N NE2 . GLN B 1 167 ? 25.894  -8.081  -36.708 1.00 50.88 ?  390 GLN B NE2 1 
ATOM   3686 N N   . ASP B 1 168 ? 22.719  -9.366  -37.416 1.00 40.54 ?  391 ASP B N   1 
ATOM   3687 C CA  . ASP B 1 168 ? 23.118  -10.750 -37.655 1.00 44.16 ?  391 ASP B CA  1 
ATOM   3688 C C   . ASP B 1 168 ? 23.929  -10.890 -38.941 1.00 48.21 ?  391 ASP B C   1 
ATOM   3689 O O   . ASP B 1 168 ? 23.952  -11.970 -39.541 1.00 51.08 ?  391 ASP B O   1 
ATOM   3690 C CB  . ASP B 1 168 ? 21.890  -11.675 -37.698 1.00 40.82 ?  391 ASP B CB  1 
ATOM   3691 C CG  . ASP B 1 168 ? 20.757  -11.106 -38.530 1.00 45.15 ?  391 ASP B CG  1 
ATOM   3692 O OD1 . ASP B 1 168 ? 21.012  -10.172 -39.312 1.00 45.92 ?  391 ASP B OD1 1 
ATOM   3693 O OD2 . ASP B 1 168 ? 19.611  -11.588 -38.401 1.00 41.92 ?  391 ASP B OD2 1 
ATOM   3694 N N   . GLY B 1 169 ? 24.598  -9.822  -39.372 1.00 51.71 ?  392 GLY B N   1 
ATOM   3695 C CA  . GLY B 1 169 ? 25.412  -9.863  -40.572 1.00 53.51 ?  392 GLY B CA  1 
ATOM   3696 C C   . GLY B 1 169 ? 26.870  -10.159 -40.288 1.00 52.35 ?  392 GLY B C   1 
ATOM   3697 O O   . GLY B 1 169 ? 27.425  -11.138 -40.794 1.00 52.94 ?  392 GLY B O   1 
ATOM   3698 N N   . GLY B 1 170 ? 27.503  -9.290  -39.508 1.00 52.59 ?  393 GLY B N   1 
ATOM   3699 C CA  . GLY B 1 170 ? 28.890  -9.535  -39.073 1.00 55.76 ?  393 GLY B CA  1 
ATOM   3700 C C   . GLY B 1 170 ? 28.923  -9.970  -37.620 1.00 56.78 ?  393 GLY B C   1 
ATOM   3701 O O   . GLY B 1 170 ? 29.971  -9.836  -37.003 1.00 60.66 ?  393 GLY B O   1 
ATOM   3702 N N   . THR B 1 171 ? 27.815  -10.500 -37.097 1.00 58.80 ?  394 THR B N   1 
ATOM   3703 C CA  . THR B 1 171 ? 27.686  -10.915 -35.667 1.00 58.78 ?  394 THR B CA  1 
ATOM   3704 C C   . THR B 1 171 ? 28.321  -9.885  -34.718 1.00 59.45 ?  394 THR B C   1 
ATOM   3705 O O   . THR B 1 171 ? 27.974  -8.716  -34.839 1.00 58.64 ?  394 THR B O   1 
ATOM   3706 C CB  . THR B 1 171 ? 27.877  -12.424 -35.433 1.00 60.46 ?  394 THR B CB  1 
ATOM   3707 O OG1 . THR B 1 171 ? 27.681  -12.671 -34.040 1.00 60.28 ?  394 THR B OG1 1 
ATOM   3708 C CG2 . THR B 1 171 ? 29.213  -12.980 -35.879 1.00 58.17 ?  394 THR B CG2 1 
ATOM   3709 N N   . THR B 1 172 ? 29.110  -10.218 -33.631 1.00 52.66 ?  395 THR B N   1 
ATOM   3710 C CA  . THR B 1 172 ? 29.601  -9.209  -32.580 1.00 51.46 ?  395 THR B CA  1 
ATOM   3711 C C   . THR B 1 172 ? 29.953  -7.848  -33.199 1.00 56.11 ?  395 THR B C   1 
ATOM   3712 O O   . THR B 1 172 ? 29.795  -6.841  -32.507 1.00 55.65 ?  395 THR B O   1 
ATOM   3713 C CB  . THR B 1 172 ? 30.606  -9.628  -31.453 1.00 51.08 ?  395 THR B CB  1 
ATOM   3714 O OG1 . THR B 1 172 ? 30.180  -10.925 -31.040 1.00 52.23 ?  395 THR B OG1 1 
ATOM   3715 C CG2 . THR B 1 172 ? 30.714  -8.715  -30.251 1.00 46.08 ?  395 THR B CG2 1 
ATOM   3716 N N   . HIS B 1 173 ? 30.389  -7.813  -34.455 1.00 55.04 ?  396 HIS B N   1 
ATOM   3717 C CA  . HIS B 1 173 ? 30.673  -6.535  -35.151 1.00 52.53 ?  396 HIS B CA  1 
ATOM   3718 C C   . HIS B 1 173 ? 29.666  -5.450  -34.793 1.00 50.06 ?  396 HIS B C   1 
ATOM   3719 O O   . HIS B 1 173 ? 28.468  -5.737  -34.806 1.00 52.37 ?  396 HIS B O   1 
ATOM   3720 C CB  . HIS B 1 173 ? 30.542  -6.747  -36.662 1.00 56.40 ?  396 HIS B CB  1 
ATOM   3721 C CG  . HIS B 1 173 ? 31.847  -6.953  -37.351 1.00 60.45 ?  396 HIS B CG  1 
ATOM   3722 N ND1 . HIS B 1 173 ? 31.989  -7.811  -38.422 1.00 59.41 ?  396 HIS B ND1 1 
ATOM   3723 C CD2 . HIS B 1 173 ? 33.068  -6.427  -37.120 1.00 54.45 ?  396 HIS B CD2 1 
ATOM   3724 C CE1 . HIS B 1 173 ? 33.241  -7.803  -38.824 1.00 56.82 ?  396 HIS B CE1 1 
ATOM   3725 N NE2 . HIS B 1 173 ? 33.923  -6.960  -38.041 1.00 60.06 ?  396 HIS B NE2 1 
ATOM   3726 N N   . ARG B 1 174 ? 30.131  -4.232  -34.551 1.00 47.76 ?  397 ARG B N   1 
ATOM   3727 C CA  . ARG B 1 174 ? 29.215  -3.113  -34.365 1.00 43.95 ?  397 ARG B CA  1 
ATOM   3728 C C   . ARG B 1 174 ? 29.008  -2.370  -35.681 1.00 41.34 ?  397 ARG B C   1 
ATOM   3729 O O   . ARG B 1 174 ? 28.747  -1.165  -35.700 1.00 39.71 ?  397 ARG B O   1 
ATOM   3730 C CB  . ARG B 1 174 ? 29.717  -2.176  -33.270 1.00 45.86 ?  397 ARG B CB  1 
ATOM   3731 C CG  . ARG B 1 174 ? 29.944  -2.879  -31.939 1.00 43.33 ?  397 ARG B CG  1 
ATOM   3732 C CD  . ARG B 1 174 ? 30.460  -1.933  -30.868 1.00 43.73 ?  397 ARG B CD  1 
ATOM   3733 N NE  . ARG B 1 174 ? 30.357  -0.534  -31.264 1.00 49.04 ?  397 ARG B NE  1 
ATOM   3734 C CZ  . ARG B 1 174 ? 29.318  0.246   -30.999 1.00 47.75 ?  397 ARG B CZ  1 
ATOM   3735 N NH1 . ARG B 1 174 ? 28.265  -0.204  -30.336 1.00 41.47 ?  397 ARG B NH1 1 
ATOM   3736 N NH2 . ARG B 1 174 ? 29.334  1.510   -31.413 1.00 42.82 ?  397 ARG B NH2 1 
ATOM   3737 N N   . ASN B 1 175 ? 29.115  -3.101  -36.788 1.00 44.71 ?  398 ASN B N   1 
ATOM   3738 C CA  . ASN B 1 175 ? 29.136  -2.541  -38.131 1.00 43.66 ?  398 ASN B CA  1 
ATOM   3739 C C   . ASN B 1 175 ? 27.749  -2.258  -38.688 1.00 40.54 ?  398 ASN B C   1 
ATOM   3740 O O   . ASN B 1 175 ? 27.643  -1.814  -39.835 1.00 39.57 ?  398 ASN B O   1 
ATOM   3741 C CB  . ASN B 1 175 ? 29.883  -3.493  -39.070 1.00 42.78 ?  398 ASN B CB  1 
ATOM   3742 C CG  . ASN B 1 175 ? 30.526  -2.775  -40.237 1.00 50.40 ?  398 ASN B CG  1 
ATOM   3743 O OD1 . ASN B 1 175 ? 30.966  -1.632  -40.109 1.00 52.33 ?  398 ASN B OD1 1 
ATOM   3744 N ND2 . ASN B 1 175 ? 30.592  -3.444  -41.383 1.00 48.99 ?  398 ASN B ND2 1 
ATOM   3745 N N   . GLU B 1 176 ? 26.689  -2.503  -37.922 1.00 36.74 ?  399 GLU B N   1 
ATOM   3746 C CA  . GLU B 1 176 ? 25.340  -2.250  -38.405 1.00 34.65 ?  399 GLU B CA  1 
ATOM   3747 C C   . GLU B 1 176 ? 24.418  -2.075  -37.208 1.00 32.41 ?  399 GLU B C   1 
ATOM   3748 O O   . GLU B 1 176 ? 24.637  -2.707  -36.168 1.00 33.84 ?  399 GLU B O   1 
ATOM   3749 C CB  . GLU B 1 176 ? 24.850  -3.392  -39.305 1.00 35.56 ?  399 GLU B CB  1 
ATOM   3750 C CG  . GLU B 1 176 ? 24.646  -4.699  -38.584 1.00 38.29 ?  399 GLU B CG  1 
ATOM   3751 C CD  . GLU B 1 176 ? 23.668  -5.582  -39.306 1.00 43.17 ?  399 GLU B CD  1 
ATOM   3752 O OE1 . GLU B 1 176 ? 22.831  -5.028  -40.050 1.00 39.28 ?  399 GLU B OE1 1 
ATOM   3753 O OE2 . GLU B 1 176 ? 23.727  -6.816  -39.126 1.00 41.11 ?  399 GLU B OE2 1 
ATOM   3754 N N   . PRO B 1 177 ? 23.389  -1.213  -37.310 1.00 28.41 ?  400 PRO B N   1 
ATOM   3755 C CA  . PRO B 1 177 ? 23.077  -0.401  -38.493 1.00 26.05 ?  400 PRO B CA  1 
ATOM   3756 C C   . PRO B 1 177 ? 24.088  0.718   -38.721 1.00 27.33 ?  400 PRO B C   1 
ATOM   3757 O O   . PRO B 1 177 ? 24.952  0.949   -37.876 1.00 31.14 ?  400 PRO B O   1 
ATOM   3758 C CB  . PRO B 1 177 ? 21.695  0.169   -38.169 1.00 25.36 ?  400 PRO B CB  1 
ATOM   3759 C CG  . PRO B 1 177 ? 21.667  0.242   -36.688 1.00 26.14 ?  400 PRO B CG  1 
ATOM   3760 C CD  . PRO B 1 177 ? 22.447  -0.955  -36.206 1.00 28.89 ?  400 PRO B CD  1 
ATOM   3761 N N   . GLN B 1 178 ? 23.986  1.389   -39.862 1.00 26.84 ?  401 GLN B N   1 
ATOM   3762 C CA  . GLN B 1 178 ? 24.923  2.438   -40.255 1.00 26.56 ?  401 GLN B CA  1 
ATOM   3763 C C   . GLN B 1 178 ? 24.126  3.732   -40.387 1.00 26.52 ?  401 GLN B C   1 
ATOM   3764 O O   . GLN B 1 178 ? 23.483  3.976   -41.413 1.00 25.19 ?  401 GLN B O   1 
ATOM   3765 C CB  . GLN B 1 178 ? 25.643  2.052   -41.544 1.00 28.94 ?  401 GLN B CB  1 
ATOM   3766 C CG  . GLN B 1 178 ? 26.258  0.655   -41.467 1.00 31.22 ?  401 GLN B CG  1 
ATOM   3767 C CD  . GLN B 1 178 ? 26.509  0.029   -42.824 1.00 45.32 ?  401 GLN B CD  1 
ATOM   3768 O OE1 . GLN B 1 178 ? 27.450  0.396   -43.527 1.00 45.66 ?  401 GLN B OE1 1 
ATOM   3769 N NE2 . GLN B 1 178 ? 25.665  -0.928  -43.198 1.00 41.53 ?  401 GLN B NE2 1 
ATOM   3770 N N   . GLN B 1 179 ? 24.179  4.560   -39.340 1.00 23.29 ?  402 GLN B N   1 
ATOM   3771 C CA  . GLN B 1 179 ? 23.243  5.670   -39.198 1.00 25.14 ?  402 GLN B CA  1 
ATOM   3772 C C   . GLN B 1 179 ? 23.507  6.807   -40.176 1.00 25.27 ?  402 GLN B C   1 
ATOM   3773 O O   . GLN B 1 179 ? 22.624  7.648   -40.373 1.00 24.06 ?  402 GLN B O   1 
ATOM   3774 C CB  . GLN B 1 179 ? 23.279  6.201   -37.763 1.00 24.11 ?  402 GLN B CB  1 
ATOM   3775 C CG  . GLN B 1 179 ? 24.554  6.943   -37.393 1.00 23.74 ?  402 GLN B CG  1 
ATOM   3776 C CD  . GLN B 1 179 ? 24.373  7.836   -36.180 1.00 25.30 ?  402 GLN B CD  1 
ATOM   3777 O OE1 . GLN B 1 179 ? 23.335  8.477   -36.018 1.00 23.63 ?  402 GLN B OE1 1 
ATOM   3778 N NE2 . GLN B 1 179 ? 25.385  7.881   -35.320 1.00 28.17 ?  402 GLN B NE2 1 
ATOM   3779 N N   . TRP B 1 180 ? 24.689  6.862   -40.791 1.00 26.50 ?  403 TRP B N   1 
ATOM   3780 C CA  . TRP B 1 180 ? 25.014  7.927   -41.731 1.00 25.92 ?  403 TRP B CA  1 
ATOM   3781 C C   . TRP B 1 180 ? 25.064  7.435   -43.174 1.00 26.36 ?  403 TRP B C   1 
ATOM   3782 O O   . TRP B 1 180 ? 25.698  8.072   -44.021 1.00 28.29 ?  403 TRP B O   1 
ATOM   3783 C CB  . TRP B 1 180 ? 26.337  8.593   -41.351 1.00 25.83 ?  403 TRP B CB  1 
ATOM   3784 C CG  . TRP B 1 180 ? 26.348  9.207   -39.978 1.00 27.95 ?  403 TRP B CG  1 
ATOM   3785 C CD1 . TRP B 1 180 ? 27.243  8.955   -38.979 1.00 25.61 ?  403 TRP B CD1 1 
ATOM   3786 C CD2 . TRP B 1 180 ? 25.430  10.180  -39.456 1.00 23.47 ?  403 TRP B CD2 1 
ATOM   3787 N NE1 . TRP B 1 180 ? 26.940  9.705   -37.869 1.00 24.84 ?  403 TRP B NE1 1 
ATOM   3788 C CE2 . TRP B 1 180 ? 25.832  10.465  -38.135 1.00 22.50 ?  403 TRP B CE2 1 
ATOM   3789 C CE3 . TRP B 1 180 ? 24.308  10.836  -39.975 1.00 23.28 ?  403 TRP B CE3 1 
ATOM   3790 C CZ2 . TRP B 1 180 ? 25.153  11.376  -37.327 1.00 22.11 ?  403 TRP B CZ2 1 
ATOM   3791 C CZ3 . TRP B 1 180 ? 23.635  11.740  -39.170 1.00 21.61 ?  403 TRP B CZ3 1 
ATOM   3792 C CH2 . TRP B 1 180 ? 24.060  12.001  -37.862 1.00 20.29 ?  403 TRP B CH2 1 
ATOM   3793 N N   . VAL B 1 181 ? 24.410  6.316   -43.471 1.00 23.01 ?  404 VAL B N   1 
ATOM   3794 C CA  . VAL B 1 181 ? 24.320  5.784   -44.827 1.00 25.15 ?  404 VAL B CA  1 
ATOM   3795 C C   . VAL B 1 181 ? 22.855  5.802   -45.236 1.00 25.07 ?  404 VAL B C   1 
ATOM   3796 O O   . VAL B 1 181 ? 22.032  5.088   -44.650 1.00 23.13 ?  404 VAL B O   1 
ATOM   3797 C CB  . VAL B 1 181 ? 24.898  4.365   -44.931 1.00 27.46 ?  404 VAL B CB  1 
ATOM   3798 C CG1 . VAL B 1 181 ? 24.749  3.839   -46.353 1.00 23.34 ?  404 VAL B CG1 1 
ATOM   3799 C CG2 . VAL B 1 181 ? 26.355  4.353   -44.504 1.00 21.19 ?  404 VAL B CG2 1 
ATOM   3800 N N   . LEU B 1 182 ? 22.533  6.613   -46.237 1.00 21.48 ?  405 LEU B N   1 
ATOM   3801 C CA  . LEU B 1 182 ? 21.155  6.712   -46.686 1.00 21.15 ?  405 LEU B CA  1 
ATOM   3802 C C   . LEU B 1 182 ? 20.767  5.469   -47.481 1.00 22.40 ?  405 LEU B C   1 
ATOM   3803 O O   . LEU B 1 182 ? 21.590  4.921   -48.222 1.00 21.72 ?  405 LEU B O   1 
ATOM   3804 C CB  . LEU B 1 182 ? 20.955  7.956   -47.547 1.00 20.72 ?  405 LEU B CB  1 
ATOM   3805 C CG  . LEU B 1 182 ? 21.181  9.301   -46.859 1.00 23.61 ?  405 LEU B CG  1 
ATOM   3806 C CD1 . LEU B 1 182 ? 21.224  10.425  -47.882 1.00 19.90 ?  405 LEU B CD1 1 
ATOM   3807 C CD2 . LEU B 1 182 ? 20.094  9.547   -45.827 1.00 21.26 ?  405 LEU B CD2 1 
ATOM   3808 N N   . PRO B 1 183 ? 19.533  4.996   -47.344 1.00 23.01 ?  406 PRO B N   1 
ATOM   3809 C CA  . PRO B 1 183 ? 19.059  3.924   -48.221 1.00 25.70 ?  406 PRO B CA  1 
ATOM   3810 C C   . PRO B 1 183 ? 18.933  4.416   -49.653 1.00 23.89 ?  406 PRO B C   1 
ATOM   3811 O O   . PRO B 1 183 ? 18.919  5.616   -49.934 1.00 20.03 ?  406 PRO B O   1 
ATOM   3812 C CB  . PRO B 1 183 ? 17.684  3.563   -47.643 1.00 27.69 ?  406 PRO B CB  1 
ATOM   3813 C CG  . PRO B 1 183 ? 17.661  4.154   -46.267 1.00 24.40 ?  406 PRO B CG  1 
ATOM   3814 C CD  . PRO B 1 183 ? 18.534  5.367   -46.330 1.00 22.11 ?  406 PRO B CD  1 
ATOM   3815 N N   . SER B 1 184 ? 18.849  3.458   -50.570 1.00 24.26 ?  407 SER B N   1 
ATOM   3816 C CA  . SER B 1 184 ? 18.463  3.755   -51.945 1.00 24.01 ?  407 SER B CA  1 
ATOM   3817 C C   . SER B 1 184 ? 16.941  3.777   -51.979 1.00 22.91 ?  407 SER B C   1 
ATOM   3818 O O   . SER B 1 184 ? 16.294  2.731   -52.067 1.00 22.61 ?  407 SER B O   1 
ATOM   3819 C CB  . SER B 1 184 ? 19.045  2.729   -52.910 1.00 24.55 ?  407 SER B CB  1 
ATOM   3820 O OG  . SER B 1 184 ? 20.199  2.108   -52.368 1.00 34.81 ?  407 SER B OG  1 
ATOM   3821 N N   . TYR B 1 185 ? 16.366  4.981   -51.891 1.00 22.99 ?  408 TYR B N   1 
ATOM   3822 C CA  . TYR B 1 185 ? 14.927  5.112   -51.670 1.00 23.11 ?  408 TYR B CA  1 
ATOM   3823 C C   . TYR B 1 185 ? 14.110  4.498   -52.799 1.00 22.58 ?  408 TYR B C   1 
ATOM   3824 O O   . TYR B 1 185 ? 12.981  4.052   -52.572 1.00 20.10 ?  408 TYR B O   1 
ATOM   3825 C CB  . TYR B 1 185 ? 14.550  6.584   -51.493 1.00 19.64 ?  408 TYR B CB  1 
ATOM   3826 C CG  . TYR B 1 185 ? 14.963  7.181   -50.165 1.00 21.48 ?  408 TYR B CG  1 
ATOM   3827 C CD1 . TYR B 1 185 ? 14.644  6.554   -48.967 1.00 20.28 ?  408 TYR B CD1 1 
ATOM   3828 C CD2 . TYR B 1 185 ? 15.662  8.380   -50.110 1.00 21.27 ?  408 TYR B CD2 1 
ATOM   3829 C CE1 . TYR B 1 185 ? 15.017  7.101   -47.752 1.00 20.02 ?  408 TYR B CE1 1 
ATOM   3830 C CE2 . TYR B 1 185 ? 16.039  8.934   -48.901 1.00 22.18 ?  408 TYR B CE2 1 
ATOM   3831 C CZ  . TYR B 1 185 ? 15.713  8.291   -47.725 1.00 21.52 ?  408 TYR B CZ  1 
ATOM   3832 O OH  . TYR B 1 185 ? 16.086  8.840   -46.519 1.00 22.17 ?  408 TYR B OH  1 
ATOM   3833 N N   . SER B 1 186 ? 14.642  4.473   -54.018 1.00 20.06 ?  409 SER B N   1 
ATOM   3834 C CA  . SER B 1 186 ? 13.934  3.878   -55.142 1.00 25.79 ?  409 SER B CA  1 
ATOM   3835 C C   . SER B 1 186 ? 14.377  2.449   -55.423 1.00 26.04 ?  409 SER B C   1 
ATOM   3836 O O   . SER B 1 186 ? 14.035  1.900   -56.475 1.00 22.85 ?  409 SER B O   1 
ATOM   3837 C CB  . SER B 1 186 ? 14.103  4.740   -56.394 1.00 24.12 ?  409 SER B CB  1 
ATOM   3838 O OG  . SER B 1 186 ? 13.255  5.874   -56.340 1.00 22.21 ?  409 SER B OG  1 
ATOM   3839 N N   . GLY B 1 187 ? 15.126  1.837   -54.511 1.00 27.60 ?  410 GLY B N   1 
ATOM   3840 C CA  . GLY B 1 187 ? 15.517  0.447   -54.642 1.00 26.16 ?  410 GLY B CA  1 
ATOM   3841 C C   . GLY B 1 187 ? 16.950  0.288   -55.112 1.00 26.56 ?  410 GLY B C   1 
ATOM   3842 O O   . GLY B 1 187 ? 17.699  1.251   -55.303 1.00 27.06 ?  410 GLY B O   1 
ATOM   3843 N N   . ARG B 1 188 ? 17.315  -0.980  -55.301 1.00 27.68 ?  411 ARG B N   1 
ATOM   3844 C CA  . ARG B 1 188 ? 18.659  -1.349  -55.728 1.00 32.20 ?  411 ARG B CA  1 
ATOM   3845 C C   . ARG B 1 188 ? 19.081  -0.577  -56.971 1.00 34.27 ?  411 ARG B C   1 
ATOM   3846 O O   . ARG B 1 188 ? 18.346  -0.516  -57.961 1.00 33.76 ?  411 ARG B O   1 
ATOM   3847 C CB  . ARG B 1 188 ? 18.713  -2.853  -56.007 1.00 33.61 ?  411 ARG B CB  1 
ATOM   3848 C CG  . ARG B 1 188 ? 20.105  -3.401  -56.280 1.00 35.70 ?  411 ARG B CG  1 
ATOM   3849 C CD  . ARG B 1 188 ? 21.057  -3.114  -55.133 1.00 38.06 ?  411 ARG B CD  1 
ATOM   3850 N NE  . ARG B 1 188 ? 21.210  -4.270  -54.258 1.00 44.25 ?  411 ARG B NE  1 
ATOM   3851 C CZ  . ARG B 1 188 ? 21.064  -4.236  -52.940 1.00 40.93 ?  411 ARG B CZ  1 
ATOM   3852 N NH1 . ARG B 1 188 ? 20.771  -3.112  -52.306 1.00 41.18 ?  411 ARG B NH1 1 
ATOM   3853 N NH2 . ARG B 1 188 ? 21.216  -5.357  -52.241 1.00 39.60 ?  411 ARG B NH2 1 
ATOM   3854 N N   . ASN B 1 189 ? 20.271  0.024   -56.901 1.00 32.93 ?  412 ASN B N   1 
ATOM   3855 C CA  . ASN B 1 189 ? 20.918  0.660   -58.050 1.00 34.34 ?  412 ASN B CA  1 
ATOM   3856 C C   . ASN B 1 189 ? 20.108  1.842   -58.582 1.00 33.67 ?  412 ASN B C   1 
ATOM   3857 O O   . ASN B 1 189 ? 19.984  2.038   -59.792 1.00 34.93 ?  412 ASN B O   1 
ATOM   3858 C CB  . ASN B 1 189 ? 21.188  -0.358  -59.161 1.00 37.64 ?  412 ASN B CB  1 
ATOM   3859 C CG  . ASN B 1 189 ? 22.287  -1.335  -58.797 1.00 41.93 ?  412 ASN B CG  1 
ATOM   3860 O OD1 . ASN B 1 189 ? 23.267  -0.971  -58.148 1.00 41.32 ?  412 ASN B OD1 1 
ATOM   3861 N ND2 . ASN B 1 189 ? 22.126  -2.588  -59.209 1.00 40.32 ?  412 ASN B ND2 1 
ATOM   3862 N N   . THR B 1 190 ? 19.558  2.640   -57.673 1.00 33.03 ?  413 THR B N   1 
ATOM   3863 C CA  . THR B 1 190 ? 18.884  3.883   -58.017 1.00 28.32 ?  413 THR B CA  1 
ATOM   3864 C C   . THR B 1 190 ? 19.514  5.032   -57.241 1.00 28.09 ?  413 THR B C   1 
ATOM   3865 O O   . THR B 1 190 ? 20.263  4.831   -56.282 1.00 28.16 ?  413 THR B O   1 
ATOM   3866 C CB  . THR B 1 190 ? 17.379  3.807   -57.729 1.00 31.59 ?  413 THR B CB  1 
ATOM   3867 O OG1 . THR B 1 190 ? 17.166  3.672   -56.318 1.00 26.81 ?  413 THR B OG1 1 
ATOM   3868 C CG2 . THR B 1 190 ? 16.752  2.625   -58.454 1.00 27.92 ?  413 THR B CG2 1 
ATOM   3869 N N   . HIS B 1 191 ? 19.203  6.253   -57.665 1.00 28.05 ?  414 HIS B N   1 
ATOM   3870 C CA  . HIS B 1 191 ? 19.782  7.454   -57.083 1.00 27.93 ?  414 HIS B CA  1 
ATOM   3871 C C   . HIS B 1 191 ? 18.705  8.283   -56.396 1.00 28.69 ?  414 HIS B C   1 
ATOM   3872 O O   . HIS B 1 191 ? 17.596  8.437   -56.918 1.00 25.11 ?  414 HIS B O   1 
ATOM   3873 C CB  . HIS B 1 191 ? 20.495  8.287   -58.152 1.00 25.79 ?  414 HIS B CB  1 
ATOM   3874 C CG  . HIS B 1 191 ? 21.585  7.545   -58.863 1.00 31.51 ?  414 HIS B CG  1 
ATOM   3875 N ND1 . HIS B 1 191 ? 21.398  6.939   -60.086 1.00 31.70 ?  414 HIS B ND1 1 
ATOM   3876 C CD2 . HIS B 1 191 ? 22.872  7.307   -58.519 1.00 32.92 ?  414 HIS B CD2 1 
ATOM   3877 C CE1 . HIS B 1 191 ? 22.524  6.363   -60.467 1.00 28.31 ?  414 HIS B CE1 1 
ATOM   3878 N NE2 . HIS B 1 191 ? 23.434  6.571   -59.534 1.00 32.21 ?  414 HIS B NE2 1 
ATOM   3879 N N   . ASN B 1 192 ? 19.041  8.815   -55.223 1.00 27.61 ?  415 ASN B N   1 
ATOM   3880 C CA  . ASN B 1 192 ? 18.090  9.568   -54.420 1.00 25.05 ?  415 ASN B CA  1 
ATOM   3881 C C   . ASN B 1 192 ? 17.876  10.962  -54.997 1.00 22.96 ?  415 ASN B C   1 
ATOM   3882 O O   . ASN B 1 192 ? 18.739  11.514  -55.686 1.00 23.37 ?  415 ASN B O   1 
ATOM   3883 C CB  . ASN B 1 192 ? 18.578  9.669   -52.976 1.00 20.86 ?  415 ASN B CB  1 
ATOM   3884 C CG  . ASN B 1 192 ? 18.646  8.320   -52.289 1.00 22.34 ?  415 ASN B CG  1 
ATOM   3885 O OD1 . ASN B 1 192 ? 17.952  7.379   -52.673 1.00 22.35 ?  415 ASN B OD1 1 
ATOM   3886 N ND2 . ASN B 1 192 ? 19.492  8.217   -51.270 1.00 24.03 ?  415 ASN B ND2 1 
ATOM   3887 N N   . VAL B 1 193 ? 16.709  11.534  -54.703 1.00 19.27 ?  416 VAL B N   1 
ATOM   3888 C CA  . VAL B 1 193 ? 16.318  12.835  -55.229 1.00 23.74 ?  416 VAL B CA  1 
ATOM   3889 C C   . VAL B 1 193 ? 15.764  13.695  -54.101 1.00 22.89 ?  416 VAL B C   1 
ATOM   3890 O O   . VAL B 1 193 ? 15.210  13.188  -53.121 1.00 20.51 ?  416 VAL B O   1 
ATOM   3891 C CB  . VAL B 1 193 ? 15.280  12.705  -56.368 1.00 18.00 ?  416 VAL B CB  1 
ATOM   3892 C CG1 . VAL B 1 193 ? 15.890  12.002  -57.573 1.00 19.02 ?  416 VAL B CG1 1 
ATOM   3893 C CG2 . VAL B 1 193 ? 14.047  11.958  -55.882 1.00 16.16 ?  416 VAL B CG2 1 
ATOM   3894 N N   . HIS B 1 194 ? 15.930  15.013  -54.249 1.00 22.25 ?  417 HIS B N   1 
ATOM   3895 C CA  . HIS B 1 194 ? 15.338  16.006  -53.346 1.00 22.68 ?  417 HIS B CA  1 
ATOM   3896 C C   . HIS B 1 194 ? 15.812  15.829  -51.906 1.00 23.78 ?  417 HIS B C   1 
ATOM   3897 O O   . HIS B 1 194 ? 15.051  16.023  -50.955 1.00 23.68 ?  417 HIS B O   1 
ATOM   3898 C CB  . HIS B 1 194 ? 13.810  15.973  -53.413 1.00 20.62 ?  417 HIS B CB  1 
ATOM   3899 C CG  . HIS B 1 194 ? 13.265  16.004  -54.805 1.00 26.84 ?  417 HIS B CG  1 
ATOM   3900 N ND1 . HIS B 1 194 ? 13.414  17.091  -55.638 1.00 26.12 ?  417 HIS B ND1 1 
ATOM   3901 C CD2 . HIS B 1 194 ? 12.568  15.082  -55.509 1.00 25.35 ?  417 HIS B CD2 1 
ATOM   3902 C CE1 . HIS B 1 194 ? 12.834  16.837  -56.798 1.00 24.73 ?  417 HIS B CE1 1 
ATOM   3903 N NE2 . HIS B 1 194 ? 12.313  15.624  -56.745 1.00 23.55 ?  417 HIS B NE2 1 
ATOM   3904 N N   . LEU B 1 195 ? 17.079  15.465  -51.738 1.00 20.22 ?  418 LEU B N   1 
ATOM   3905 C CA  . LEU B 1 195 ? 17.628  15.300  -50.400 1.00 23.75 ?  418 LEU B CA  1 
ATOM   3906 C C   . LEU B 1 195 ? 17.781  16.646  -49.706 1.00 24.59 ?  418 LEU B C   1 
ATOM   3907 O O   . LEU B 1 195 ? 18.113  17.655  -50.335 1.00 23.31 ?  418 LEU B O   1 
ATOM   3908 C CB  . LEU B 1 195 ? 18.989  14.605  -50.458 1.00 20.58 ?  418 LEU B CB  1 
ATOM   3909 C CG  . LEU B 1 195 ? 19.060  13.148  -50.912 1.00 21.21 ?  418 LEU B CG  1 
ATOM   3910 C CD1 . LEU B 1 195 ? 20.495  12.647  -50.832 1.00 20.30 ?  418 LEU B CD1 1 
ATOM   3911 C CD2 . LEU B 1 195 ? 18.135  12.283  -50.074 1.00 21.27 ?  418 LEU B CD2 1 
ATOM   3912 N N   . ALA B 1 196 ? 17.528  16.659  -48.403 1.00 25.97 ?  419 ALA B N   1 
ATOM   3913 C CA  . ALA B 1 196 ? 18.024  17.751  -47.587 1.00 21.68 ?  419 ALA B CA  1 
ATOM   3914 C C   . ALA B 1 196 ? 19.550  17.731  -47.631 1.00 21.71 ?  419 ALA B C   1 
ATOM   3915 O O   . ALA B 1 196 ? 20.153  16.652  -47.629 1.00 23.20 ?  419 ALA B O   1 
ATOM   3916 C CB  . ALA B 1 196 ? 17.529  17.624  -46.145 1.00 20.17 ?  419 ALA B CB  1 
ATOM   3917 N N   . PRO B 1 197 ? 20.203  18.887  -47.692 1.00 22.21 ?  420 PRO B N   1 
ATOM   3918 C CA  . PRO B 1 197 ? 21.653  18.898  -47.904 1.00 21.19 ?  420 PRO B CA  1 
ATOM   3919 C C   . PRO B 1 197 ? 22.405  18.312  -46.720 1.00 22.91 ?  420 PRO B C   1 
ATOM   3920 O O   . PRO B 1 197 ? 21.910  18.251  -45.592 1.00 20.64 ?  420 PRO B O   1 
ATOM   3921 C CB  . PRO B 1 197 ? 21.976  20.385  -48.084 1.00 20.86 ?  420 PRO B CB  1 
ATOM   3922 C CG  . PRO B 1 197 ? 20.885  21.093  -47.357 1.00 17.69 ?  420 PRO B CG  1 
ATOM   3923 C CD  . PRO B 1 197 ? 19.655  20.244  -47.517 1.00 18.33 ?  420 PRO B CD  1 
ATOM   3924 N N   . ALA B 1 198 ? 23.622  17.858  -47.003 1.00 22.09 ?  421 ALA B N   1 
ATOM   3925 C CA  . ALA B 1 198 ? 24.521  17.446  -45.941 1.00 25.55 ?  421 ALA B CA  1 
ATOM   3926 C C   . ALA B 1 198 ? 25.017  18.670  -45.179 1.00 25.82 ?  421 ALA B C   1 
ATOM   3927 O O   . ALA B 1 198 ? 25.039  19.791  -45.694 1.00 23.91 ?  421 ALA B O   1 
ATOM   3928 C CB  . ALA B 1 198 ? 25.701  16.655  -46.507 1.00 24.30 ?  421 ALA B CB  1 
ATOM   3929 N N   . VAL B 1 199 ? 25.412  18.446  -43.931 1.00 27.34 ?  422 VAL B N   1 
ATOM   3930 C CA  . VAL B 1 199 ? 25.825  19.530  -43.051 1.00 26.78 ?  422 VAL B CA  1 
ATOM   3931 C C   . VAL B 1 199 ? 27.229  19.251  -42.539 1.00 27.81 ?  422 VAL B C   1 
ATOM   3932 O O   . VAL B 1 199 ? 27.664  18.099  -42.445 1.00 25.74 ?  422 VAL B O   1 
ATOM   3933 C CB  . VAL B 1 199 ? 24.839  19.719  -41.879 1.00 25.97 ?  422 VAL B CB  1 
ATOM   3934 C CG1 . VAL B 1 199 ? 23.537  20.324  -42.381 1.00 24.73 ?  422 VAL B CG1 1 
ATOM   3935 C CG2 . VAL B 1 199 ? 24.586  18.394  -41.181 1.00 24.98 ?  422 VAL B CG2 1 
ATOM   3936 N N   . ALA B 1 200 ? 27.937  20.326  -42.207 1.00 28.79 ?  423 ALA B N   1 
ATOM   3937 C CA  . ALA B 1 200 ? 29.301  20.245  -41.707 1.00 27.23 ?  423 ALA B CA  1 
ATOM   3938 C C   . ALA B 1 200 ? 29.650  21.576  -41.059 1.00 30.08 ?  423 ALA B C   1 
ATOM   3939 O O   . ALA B 1 200 ? 29.049  22.606  -41.389 1.00 31.72 ?  423 ALA B O   1 
ATOM   3940 C CB  . ALA B 1 200 ? 30.292  19.916  -42.835 1.00 21.94 ?  423 ALA B CB  1 
ATOM   3941 N N   . PRO B 1 201 ? 30.600  21.588  -40.126 1.00 30.49 ?  424 PRO B N   1 
ATOM   3942 C CA  . PRO B 1 201 ? 31.043  22.863  -39.552 1.00 31.52 ?  424 PRO B CA  1 
ATOM   3943 C C   . PRO B 1 201 ? 31.756  23.714  -40.591 1.00 35.31 ?  424 PRO B C   1 
ATOM   3944 O O   . PRO B 1 201 ? 32.557  23.218  -41.387 1.00 34.26 ?  424 PRO B O   1 
ATOM   3945 C CB  . PRO B 1 201 ? 31.995  22.445  -38.425 1.00 30.68 ?  424 PRO B CB  1 
ATOM   3946 C CG  . PRO B 1 201 ? 31.733  20.999  -38.187 1.00 30.30 ?  424 PRO B CG  1 
ATOM   3947 C CD  . PRO B 1 201 ? 31.199  20.424  -39.452 1.00 31.66 ?  424 PRO B CD  1 
ATOM   3948 N N   . THR B 1 202 ? 31.450  25.010  -40.579 1.00 36.81 ?  425 THR B N   1 
ATOM   3949 C CA  . THR B 1 202 ? 32.073  25.976  -41.475 1.00 39.01 ?  425 THR B CA  1 
ATOM   3950 C C   . THR B 1 202 ? 33.137  26.810  -40.774 1.00 40.77 ?  425 THR B C   1 
ATOM   3951 O O   . THR B 1 202 ? 34.243  26.978  -41.297 1.00 48.01 ?  425 THR B O   1 
ATOM   3952 C CB  . THR B 1 202 ? 31.009  26.902  -42.077 1.00 42.54 ?  425 THR B CB  1 
ATOM   3953 O OG1 . THR B 1 202 ? 30.088  27.299  -41.054 1.00 44.36 ?  425 THR B OG1 1 
ATOM   3954 C CG2 . THR B 1 202 ? 30.250  26.192  -43.186 1.00 40.20 ?  425 THR B CG2 1 
ATOM   3955 N N   . PHE B 1 203 ? 32.820  27.330  -39.594 1.00 36.17 ?  426 PHE B N   1 
ATOM   3956 C CA  . PHE B 1 203 ? 33.749  28.189  -38.877 1.00 38.49 ?  426 PHE B CA  1 
ATOM   3957 C C   . PHE B 1 203 ? 34.939  27.378  -38.371 1.00 38.00 ?  426 PHE B C   1 
ATOM   3958 O O   . PHE B 1 203 ? 34.771  26.237  -37.926 1.00 36.24 ?  426 PHE B O   1 
ATOM   3959 C CB  . PHE B 1 203 ? 33.042  28.864  -37.703 1.00 36.42 ?  426 PHE B CB  1 
ATOM   3960 C CG  . PHE B 1 203 ? 33.533  30.251  -37.413 1.00 40.89 ?  426 PHE B CG  1 
ATOM   3961 C CD1 . PHE B 1 203 ? 33.553  31.216  -38.406 1.00 43.67 ?  426 PHE B CD1 1 
ATOM   3962 C CD2 . PHE B 1 203 ? 33.966  30.594  -36.142 1.00 40.48 ?  426 PHE B CD2 1 
ATOM   3963 C CE1 . PHE B 1 203 ? 34.002  32.495  -38.139 1.00 46.83 ?  426 PHE B CE1 1 
ATOM   3964 C CE2 . PHE B 1 203 ? 34.414  31.872  -35.869 1.00 40.16 ?  426 PHE B CE2 1 
ATOM   3965 C CZ  . PHE B 1 203 ? 34.432  32.824  -36.868 1.00 40.33 ?  426 PHE B CZ  1 
ATOM   3966 N N   . PRO B 1 204 ? 36.150  27.930  -38.431 1.00 36.17 ?  427 PRO B N   1 
ATOM   3967 C CA  . PRO B 1 204 ? 37.301  27.237  -37.843 1.00 34.70 ?  427 PRO B CA  1 
ATOM   3968 C C   . PRO B 1 204 ? 37.128  27.072  -36.341 1.00 35.82 ?  427 PRO B C   1 
ATOM   3969 O O   . PRO B 1 204 ? 36.670  27.980  -35.644 1.00 37.41 ?  427 PRO B O   1 
ATOM   3970 C CB  . PRO B 1 204 ? 38.483  28.155  -38.177 1.00 31.69 ?  427 PRO B CB  1 
ATOM   3971 C CG  . PRO B 1 204 ? 38.010  29.007  -39.310 1.00 36.26 ?  427 PRO B CG  1 
ATOM   3972 C CD  . PRO B 1 204 ? 36.537  29.177  -39.111 1.00 36.31 ?  427 PRO B CD  1 
ATOM   3973 N N   . GLY B 1 205 ? 37.493  25.892  -35.847 1.00 30.16 ?  428 GLY B N   1 
ATOM   3974 C CA  . GLY B 1 205 ? 37.379  25.609  -34.432 1.00 29.79 ?  428 GLY B CA  1 
ATOM   3975 C C   . GLY B 1 205 ? 36.015  25.151  -33.975 1.00 33.24 ?  428 GLY B C   1 
ATOM   3976 O O   . GLY B 1 205 ? 35.679  25.330  -32.800 1.00 34.10 ?  428 GLY B O   1 
ATOM   3977 N N   . GLU B 1 206 ? 35.218  24.552  -34.858 1.00 29.32 ?  429 GLU B N   1 
ATOM   3978 C CA  . GLU B 1 206 ? 33.852  24.185  -34.520 1.00 31.24 ?  429 GLU B CA  1 
ATOM   3979 C C   . GLU B 1 206 ? 33.539  22.782  -35.019 1.00 31.30 ?  429 GLU B C   1 
ATOM   3980 O O   . GLU B 1 206 ? 34.112  22.310  -36.005 1.00 27.50 ?  429 GLU B O   1 
ATOM   3981 C CB  . GLU B 1 206 ? 32.847  25.190  -35.100 1.00 28.82 ?  429 GLU B CB  1 
ATOM   3982 C CG  . GLU B 1 206 ? 32.657  26.425  -34.233 1.00 30.75 ?  429 GLU B CG  1 
ATOM   3983 C CD  . GLU B 1 206 ? 31.671  27.413  -34.821 1.00 33.28 ?  429 GLU B CD  1 
ATOM   3984 O OE1 . GLU B 1 206 ? 30.917  27.029  -35.740 1.00 34.49 ?  429 GLU B OE1 1 
ATOM   3985 O OE2 . GLU B 1 206 ? 31.651  28.575  -34.364 1.00 34.11 ?  429 GLU B OE2 1 
ATOM   3986 N N   . GLN B 1 207 ? 32.621  22.120  -34.317 1.00 31.69 ?  430 GLN B N   1 
ATOM   3987 C CA  . GLN B 1 207 ? 32.155  20.787  -34.674 1.00 30.10 ?  430 GLN B CA  1 
ATOM   3988 C C   . GLN B 1 207 ? 30.641  20.736  -34.533 1.00 25.23 ?  430 GLN B C   1 
ATOM   3989 O O   . GLN B 1 207 ? 30.026  21.601  -33.906 1.00 23.51 ?  430 GLN B O   1 
ATOM   3990 C CB  . GLN B 1 207 ? 32.801  19.703  -33.800 1.00 28.91 ?  430 GLN B CB  1 
ATOM   3991 C CG  . GLN B 1 207 ? 34.235  19.371  -34.170 1.00 31.13 ?  430 GLN B CG  1 
ATOM   3992 C CD  . GLN B 1 207 ? 34.918  18.519  -33.119 1.00 34.69 ?  430 GLN B CD  1 
ATOM   3993 O OE1 . GLN B 1 207 ? 34.358  18.260  -32.054 1.00 34.35 ?  430 GLN B OE1 1 
ATOM   3994 N NE2 . GLN B 1 207 ? 36.143  18.093  -33.406 1.00 35.00 ?  430 GLN B NE2 1 
ATOM   3995 N N   . LEU B 1 208 ? 30.045  19.705  -35.126 1.00 24.71 ?  431 LEU B N   1 
ATOM   3996 C CA  . LEU B 1 208 ? 28.603  19.526  -35.032 1.00 25.21 ?  431 LEU B CA  1 
ATOM   3997 C C   . LEU B 1 208 ? 28.205  19.085  -33.629 1.00 23.83 ?  431 LEU B C   1 
ATOM   3998 O O   . LEU B 1 208 ? 28.907  18.304  -32.982 1.00 21.84 ?  431 LEU B O   1 
ATOM   3999 C CB  . LEU B 1 208 ? 28.124  18.494  -36.054 1.00 22.40 ?  431 LEU B CB  1 
ATOM   4000 C CG  . LEU B 1 208 ? 28.135  18.893  -37.530 1.00 25.23 ?  431 LEU B CG  1 
ATOM   4001 C CD1 . LEU B 1 208 ? 27.917  17.674  -38.413 1.00 23.40 ?  431 LEU B CD1 1 
ATOM   4002 C CD2 . LEU B 1 208 ? 27.081  19.954  -37.810 1.00 24.98 ?  431 LEU B CD2 1 
ATOM   4003 N N   . LEU B 1 209 ? 27.071  19.596  -33.160 1.00 24.73 ?  432 LEU B N   1 
ATOM   4004 C CA  . LEU B 1 209 ? 26.458  19.144  -31.920 1.00 22.89 ?  432 LEU B CA  1 
ATOM   4005 C C   . LEU B 1 209 ? 25.291  18.227  -32.259 1.00 22.27 ?  432 LEU B C   1 
ATOM   4006 O O   . LEU B 1 209 ? 24.432  18.585  -33.072 1.00 22.68 ?  432 LEU B O   1 
ATOM   4007 C CB  . LEU B 1 209 ? 25.979  20.325  -31.073 1.00 24.35 ?  432 LEU B CB  1 
ATOM   4008 C CG  . LEU B 1 209 ? 25.368  19.970  -29.714 1.00 25.72 ?  432 LEU B CG  1 
ATOM   4009 C CD1 . LEU B 1 209 ? 26.449  19.570  -28.720 1.00 21.66 ?  432 LEU B CD1 1 
ATOM   4010 C CD2 . LEU B 1 209 ? 24.535  21.121  -29.170 1.00 22.03 ?  432 LEU B CD2 1 
ATOM   4011 N N   . PHE B 1 210 ? 25.268  17.048  -31.647 1.00 25.34 ?  433 PHE B N   1 
ATOM   4012 C CA  . PHE B 1 210 ? 24.260  16.043  -31.940 1.00 22.18 ?  433 PHE B CA  1 
ATOM   4013 C C   . PHE B 1 210 ? 23.385  15.792  -30.721 1.00 22.84 ?  433 PHE B C   1 
ATOM   4014 O O   . PHE B 1 210 ? 23.840  15.879  -29.576 1.00 21.53 ?  433 PHE B O   1 
ATOM   4015 C CB  . PHE B 1 210 ? 24.898  14.724  -32.392 1.00 21.37 ?  433 PHE B CB  1 
ATOM   4016 C CG  . PHE B 1 210 ? 25.583  14.808  -33.725 1.00 19.96 ?  433 PHE B CG  1 
ATOM   4017 C CD1 . PHE B 1 210 ? 24.848  14.788  -34.899 1.00 23.39 ?  433 PHE B CD1 1 
ATOM   4018 C CD2 . PHE B 1 210 ? 26.961  14.900  -33.805 1.00 21.66 ?  433 PHE B CD2 1 
ATOM   4019 C CE1 . PHE B 1 210 ? 25.475  14.862  -36.127 1.00 22.71 ?  433 PHE B CE1 1 
ATOM   4020 C CE2 . PHE B 1 210 ? 27.595  14.974  -35.030 1.00 22.27 ?  433 PHE B CE2 1 
ATOM   4021 C CZ  . PHE B 1 210 ? 26.851  14.955  -36.193 1.00 22.81 ?  433 PHE B CZ  1 
ATOM   4022 N N   . PHE B 1 211 ? 22.120  15.481  -30.986 1.00 19.33 ?  434 PHE B N   1 
ATOM   4023 C CA  . PHE B 1 211 ? 21.168  15.070  -29.961 1.00 19.83 ?  434 PHE B CA  1 
ATOM   4024 C C   . PHE B 1 211 ? 21.051  13.553  -30.056 1.00 21.82 ?  434 PHE B C   1 
ATOM   4025 O O   . PHE B 1 211 ? 20.515  13.026  -31.036 1.00 20.11 ?  434 PHE B O   1 
ATOM   4026 C CB  . PHE B 1 211 ? 19.817  15.759  -30.156 1.00 22.47 ?  434 PHE B CB  1 
ATOM   4027 C CG  . PHE B 1 211 ? 19.882  17.266  -30.099 1.00 19.76 ?  434 PHE B CG  1 
ATOM   4028 C CD1 . PHE B 1 211 ? 20.467  17.996  -31.124 1.00 19.96 ?  434 PHE B CD1 1 
ATOM   4029 C CD2 . PHE B 1 211 ? 19.354  17.952  -29.017 1.00 19.90 ?  434 PHE B CD2 1 
ATOM   4030 C CE1 . PHE B 1 211 ? 20.526  19.377  -31.068 1.00 21.07 ?  434 PHE B CE1 1 
ATOM   4031 C CE2 . PHE B 1 211 ? 19.410  19.333  -28.956 1.00 18.08 ?  434 PHE B CE2 1 
ATOM   4032 C CZ  . PHE B 1 211 ? 19.997  20.046  -29.983 1.00 18.61 ?  434 PHE B CZ  1 
ATOM   4033 N N   . ARG B 1 212 ? 21.562  12.855  -29.046 1.00 20.33 ?  435 ARG B N   1 
ATOM   4034 C CA  . ARG B 1 212 ? 21.853  11.432  -29.143 1.00 19.39 ?  435 ARG B CA  1 
ATOM   4035 C C   . ARG B 1 212 ? 20.874  10.601  -28.323 1.00 22.85 ?  435 ARG B C   1 
ATOM   4036 O O   . ARG B 1 212 ? 20.529  10.958  -27.192 1.00 22.41 ?  435 ARG B O   1 
ATOM   4037 C CB  . ARG B 1 212 ? 23.284  11.145  -28.678 1.00 23.19 ?  435 ARG B CB  1 
ATOM   4038 C CG  . ARG B 1 212 ? 23.558  9.682   -28.364 1.00 21.49 ?  435 ARG B CG  1 
ATOM   4039 C CD  . ARG B 1 212 ? 25.044  9.375   -28.376 1.00 23.06 ?  435 ARG B CD  1 
ATOM   4040 N NE  . ARG B 1 212 ? 25.634  9.556   -29.697 1.00 21.46 ?  435 ARG B NE  1 
ATOM   4041 C CZ  . ARG B 1 212 ? 26.820  9.083   -30.056 1.00 23.63 ?  435 ARG B CZ  1 
ATOM   4042 N NH1 . ARG B 1 212 ? 27.572  8.393   -29.216 1.00 22.67 ?  435 ARG B NH1 1 
ATOM   4043 N NH2 . ARG B 1 212 ? 27.262  9.310   -31.290 1.00 23.68 ?  435 ARG B NH2 1 
ATOM   4044 N N   . SER B 1 213 ? 20.436  9.488   -28.908 1.00 24.15 ?  436 SER B N   1 
ATOM   4045 C CA  . SER B 1 213 ? 19.689  8.449   -28.217 1.00 23.89 ?  436 SER B CA  1 
ATOM   4046 C C   . SER B 1 213 ? 20.369  7.110   -28.470 1.00 25.28 ?  436 SER B C   1 
ATOM   4047 O O   . SER B 1 213 ? 21.262  6.990   -29.314 1.00 23.14 ?  436 SER B O   1 
ATOM   4048 C CB  . SER B 1 213 ? 18.226  8.400   -28.679 1.00 23.12 ?  436 SER B CB  1 
ATOM   4049 O OG  . SER B 1 213 ? 17.598  9.661   -28.538 1.00 26.60 ?  436 SER B OG  1 
ATOM   4050 N N   . THR B 1 214 ? 19.941  6.094   -27.726 1.00 26.28 ?  437 THR B N   1 
ATOM   4051 C CA  . THR B 1 214 ? 20.424  4.727   -27.901 1.00 24.69 ?  437 THR B CA  1 
ATOM   4052 C C   . THR B 1 214 ? 19.245  3.866   -28.333 1.00 21.99 ?  437 THR B C   1 
ATOM   4053 O O   . THR B 1 214 ? 18.309  3.651   -27.554 1.00 25.92 ?  437 THR B O   1 
ATOM   4054 C CB  . THR B 1 214 ? 21.057  4.188   -26.618 1.00 24.73 ?  437 THR B CB  1 
ATOM   4055 O OG1 . THR B 1 214 ? 22.076  5.090   -26.170 1.00 31.89 ?  437 THR B OG1 1 
ATOM   4056 C CG2 . THR B 1 214 ? 21.675  2.819   -26.864 1.00 23.71 ?  437 THR B CG2 1 
ATOM   4057 N N   . MET B 1 215 ? 19.288  3.384   -29.570 1.00 25.09 ?  438 MET B N   1 
ATOM   4058 C CA  . MET B 1 215 ? 18.205  2.559   -30.080 1.00 24.84 ?  438 MET B CA  1 
ATOM   4059 C C   . MET B 1 215 ? 18.162  1.230   -29.330 1.00 25.83 ?  438 MET B C   1 
ATOM   4060 O O   . MET B 1 215 ? 19.209  0.654   -29.027 1.00 25.89 ?  438 MET B O   1 
ATOM   4061 C CB  . MET B 1 215 ? 18.383  2.309   -31.577 1.00 20.82 ?  438 MET B CB  1 
ATOM   4062 C CG  . MET B 1 215 ? 18.206  3.548   -32.441 1.00 25.75 ?  438 MET B CG  1 
ATOM   4063 S SD  . MET B 1 215 ? 17.992  3.164   -34.192 1.00 25.74 ?  438 MET B SD  1 
ATOM   4064 C CE  . MET B 1 215 ? 19.693  2.917   -34.697 1.00 24.05 ?  438 MET B CE  1 
ATOM   4065 N N   . PRO B 1 216 ? 16.975  0.734   -28.990 1.00 25.89 ?  439 PRO B N   1 
ATOM   4066 C CA  . PRO B 1 216 ? 16.888  -0.605  -28.398 1.00 23.44 ?  439 PRO B CA  1 
ATOM   4067 C C   . PRO B 1 216 ? 17.419  -1.658  -29.358 1.00 23.03 ?  439 PRO B C   1 
ATOM   4068 O O   . PRO B 1 216 ? 17.190  -1.598  -30.568 1.00 23.86 ?  439 PRO B O   1 
ATOM   4069 C CB  . PRO B 1 216 ? 15.388  -0.781  -28.140 1.00 22.11 ?  439 PRO B CB  1 
ATOM   4070 C CG  . PRO B 1 216 ? 14.876  0.614   -27.983 1.00 22.53 ?  439 PRO B CG  1 
ATOM   4071 C CD  . PRO B 1 216 ? 15.687  1.447   -28.938 1.00 23.09 ?  439 PRO B CD  1 
ATOM   4072 N N   . GLY B 1 217 ? 18.153  -2.619  -28.809 1.00 25.04 ?  440 GLY B N   1 
ATOM   4073 C CA  . GLY B 1 217 ? 18.655  -3.746  -29.575 1.00 24.20 ?  440 GLY B CA  1 
ATOM   4074 C C   . GLY B 1 217 ? 17.772  -4.960  -29.354 1.00 24.50 ?  440 GLY B C   1 
ATOM   4075 O O   . GLY B 1 217 ? 17.371  -5.252  -28.227 1.00 24.68 ?  440 GLY B O   1 
ATOM   4076 N N   . CYS B 1 218 ? 17.465  -5.661  -30.444 1.00 25.06 ?  441 CYS B N   1 
ATOM   4077 C CA  . CYS B 1 218 ? 16.590  -6.820  -30.381 1.00 26.61 ?  441 CYS B CA  1 
ATOM   4078 C C   . CYS B 1 218 ? 17.299  -8.136  -30.669 1.00 27.04 ?  441 CYS B C   1 
ATOM   4079 O O   . CYS B 1 218 ? 16.708  -9.196  -30.433 1.00 28.89 ?  441 CYS B O   1 
ATOM   4080 C CB  . CYS B 1 218 ? 15.417  -6.653  -31.359 1.00 26.49 ?  441 CYS B CB  1 
ATOM   4081 S SG  . CYS B 1 218 ? 14.295  -5.288  -30.971 1.00 26.51 ?  441 CYS B SG  1 
ATOM   4082 N N   . SER B 1 219 ? 18.538  -8.101  -31.160 1.00 26.08 ?  442 SER B N   1 
ATOM   4083 C CA  . SER B 1 219 ? 19.284  -9.313  -31.470 1.00 25.87 ?  442 SER B CA  1 
ATOM   4084 C C   . SER B 1 219 ? 20.726  -8.951  -31.797 1.00 27.38 ?  442 SER B C   1 
ATOM   4085 O O   . SER B 1 219 ? 20.984  -7.914  -32.411 1.00 26.10 ?  442 SER B O   1 
ATOM   4086 C CB  . SER B 1 219 ? 18.654  -10.068 -32.649 1.00 28.73 ?  442 SER B CB  1 
ATOM   4087 O OG  . SER B 1 219 ? 18.988  -11.443 -32.606 1.00 27.22 ?  442 SER B OG  1 
ATOM   4088 N N   . GLY B 1 220 ? 21.656  -9.814  -31.389 1.00 28.33 ?  443 GLY B N   1 
ATOM   4089 C CA  . GLY B 1 220 ? 23.045  -9.638  -31.785 1.00 28.94 ?  443 GLY B CA  1 
ATOM   4090 C C   . GLY B 1 220 ? 23.722  -8.491  -31.057 1.00 30.34 ?  443 GLY B C   1 
ATOM   4091 O O   . GLY B 1 220 ? 23.465  -8.226  -29.877 1.00 31.00 ?  443 GLY B O   1 
ATOM   4092 N N   . TYR B 1 221 ? 24.605  -7.798  -31.774 1.00 28.94 ?  444 TYR B N   1 
ATOM   4093 C CA  . TYR B 1 221 ? 25.439  -6.733  -31.214 1.00 31.54 ?  444 TYR B CA  1 
ATOM   4094 C C   . TYR B 1 221 ? 25.364  -5.506  -32.116 1.00 31.94 ?  444 TYR B C   1 
ATOM   4095 O O   . TYR B 1 221 ? 26.338  -5.155  -32.791 1.00 33.35 ?  444 TYR B O   1 
ATOM   4096 C CB  . TYR B 1 221 ? 26.886  -7.203  -31.065 1.00 32.65 ?  444 TYR B CB  1 
ATOM   4097 C CG  . TYR B 1 221 ? 27.086  -8.360  -30.112 1.00 35.80 ?  444 TYR B CG  1 
ATOM   4098 C CD1 . TYR B 1 221 ? 26.853  -9.669  -30.517 1.00 37.33 ?  444 TYR B CD1 1 
ATOM   4099 C CD2 . TYR B 1 221 ? 27.539  -8.147  -28.817 1.00 34.77 ?  444 TYR B CD2 1 
ATOM   4100 C CE1 . TYR B 1 221 ? 27.046  -10.731 -29.653 1.00 36.68 ?  444 TYR B CE1 1 
ATOM   4101 C CE2 . TYR B 1 221 ? 27.742  -9.202  -27.950 1.00 33.67 ?  444 TYR B CE2 1 
ATOM   4102 C CZ  . TYR B 1 221 ? 27.491  -10.491 -28.370 1.00 36.28 ?  444 TYR B CZ  1 
ATOM   4103 O OH  . TYR B 1 221 ? 27.688  -11.542 -27.504 1.00 34.96 ?  444 TYR B OH  1 
ATOM   4104 N N   . PRO B 1 222 ? 24.225  -4.821  -32.141 1.00 32.54 ?  445 PRO B N   1 
ATOM   4105 C CA  . PRO B 1 222 ? 24.064  -3.693  -33.060 1.00 30.96 ?  445 PRO B CA  1 
ATOM   4106 C C   . PRO B 1 222 ? 24.725  -2.425  -32.538 1.00 30.34 ?  445 PRO B C   1 
ATOM   4107 O O   . PRO B 1 222 ? 24.983  -2.264  -31.344 1.00 28.28 ?  445 PRO B O   1 
ATOM   4108 C CB  . PRO B 1 222 ? 22.544  -3.524  -33.140 1.00 28.81 ?  445 PRO B CB  1 
ATOM   4109 C CG  . PRO B 1 222 ? 22.065  -3.969  -31.799 1.00 29.22 ?  445 PRO B CG  1 
ATOM   4110 C CD  . PRO B 1 222 ? 23.021  -5.038  -31.317 1.00 29.98 ?  445 PRO B CD  1 
ATOM   4111 N N   . ASN B 1 223 ? 25.005  -1.520  -33.474 1.00 31.23 ?  446 ASN B N   1 
ATOM   4112 C CA  . ASN B 1 223 ? 25.466  -0.170  -33.149 1.00 33.25 ?  446 ASN B CA  1 
ATOM   4113 C C   . ASN B 1 223 ? 24.225  0.691   -32.959 1.00 27.87 ?  446 ASN B C   1 
ATOM   4114 O O   . ASN B 1 223 ? 23.585  1.105   -33.929 1.00 28.90 ?  446 ASN B O   1 
ATOM   4115 C CB  . ASN B 1 223 ? 26.372  0.381   -34.243 1.00 33.45 ?  446 ASN B CB  1 
ATOM   4116 C CG  . ASN B 1 223 ? 26.893  1.771   -33.925 1.00 32.33 ?  446 ASN B CG  1 
ATOM   4117 O OD1 . ASN B 1 223 ? 26.818  2.231   -32.785 1.00 34.14 ?  446 ASN B OD1 1 
ATOM   4118 N ND2 . ASN B 1 223 ? 27.427  2.448   -34.935 1.00 30.36 ?  446 ASN B ND2 1 
ATOM   4119 N N   . MET B 1 224 ? 23.885  0.963   -31.704 1.00 26.67 ?  447 MET B N   1 
ATOM   4120 C CA  . MET B 1 224 ? 22.609  1.566   -31.356 1.00 27.22 ?  447 MET B CA  1 
ATOM   4121 C C   . MET B 1 224 ? 22.672  3.080   -31.200 1.00 25.32 ?  447 MET B C   1 
ATOM   4122 O O   . MET B 1 224 ? 21.664  3.691   -30.830 1.00 26.29 ?  447 MET B O   1 
ATOM   4123 C CB  . MET B 1 224 ? 22.079  0.929   -30.069 1.00 21.50 ?  447 MET B CB  1 
ATOM   4124 C CG  . MET B 1 224 ? 21.910  -0.582  -30.164 1.00 26.36 ?  447 MET B CG  1 
ATOM   4125 S SD  . MET B 1 224 ? 21.604  -1.370  -28.571 1.00 29.44 ?  447 MET B SD  1 
ATOM   4126 C CE  . MET B 1 224 ? 23.277  -1.741  -28.051 1.00 21.11 ?  447 MET B CE  1 
ATOM   4127 N N   . ASP B 1 225 ? 23.816  3.700   -31.477 1.00 25.66 ?  448 ASP B N   1 
ATOM   4128 C CA  . ASP B 1 225 ? 23.919  5.150   -31.387 1.00 27.92 ?  448 ASP B CA  1 
ATOM   4129 C C   . ASP B 1 225 ? 23.107  5.802   -32.499 1.00 28.18 ?  448 ASP B C   1 
ATOM   4130 O O   . ASP B 1 225 ? 23.253  5.456   -33.675 1.00 25.41 ?  448 ASP B O   1 
ATOM   4131 C CB  . ASP B 1 225 ? 25.379  5.588   -31.477 1.00 27.36 ?  448 ASP B CB  1 
ATOM   4132 C CG  . ASP B 1 225 ? 26.222  5.051   -30.337 1.00 31.14 ?  448 ASP B CG  1 
ATOM   4133 O OD1 . ASP B 1 225 ? 25.674  4.846   -29.233 1.00 31.47 ?  448 ASP B OD1 1 
ATOM   4134 O OD2 . ASP B 1 225 ? 27.434  4.833   -30.547 1.00 35.97 ?  448 ASP B OD2 1 
ATOM   4135 N N   . LEU B 1 226 ? 22.245  6.746   -32.127 1.00 26.73 ?  449 LEU B N   1 
ATOM   4136 C CA  . LEU B 1 226 ? 21.429  7.479   -33.090 1.00 22.33 ?  449 LEU B CA  1 
ATOM   4137 C C   . LEU B 1 226 ? 21.502  8.965   -32.774 1.00 23.15 ?  449 LEU B C   1 
ATOM   4138 O O   . LEU B 1 226 ? 20.995  9.410   -31.739 1.00 23.68 ?  449 LEU B O   1 
ATOM   4139 C CB  . LEU B 1 226 ? 19.980  7.001   -33.076 1.00 24.14 ?  449 LEU B CB  1 
ATOM   4140 C CG  . LEU B 1 226 ? 19.210  7.552   -34.275 1.00 23.32 ?  449 LEU B CG  1 
ATOM   4141 C CD1 . LEU B 1 226 ? 19.633  6.848   -35.558 1.00 23.30 ?  449 LEU B CD1 1 
ATOM   4142 C CD2 . LEU B 1 226 ? 17.725  7.437   -34.055 1.00 20.33 ?  449 LEU B CD2 1 
ATOM   4143 N N   . ASP B 1 227 ? 22.117  9.726   -33.671 1.00 21.60 ?  450 ASP B N   1 
ATOM   4144 C CA  . ASP B 1 227 ? 22.263  11.166  -33.526 1.00 21.03 ?  450 ASP B CA  1 
ATOM   4145 C C   . ASP B 1 227 ? 21.342  11.870  -34.512 1.00 21.52 ?  450 ASP B C   1 
ATOM   4146 O O   . ASP B 1 227 ? 21.317  11.527  -35.699 1.00 21.89 ?  450 ASP B O   1 
ATOM   4147 C CB  . ASP B 1 227 ? 23.713  11.592  -33.764 1.00 21.90 ?  450 ASP B CB  1 
ATOM   4148 C CG  . ASP B 1 227 ? 24.666  11.019  -32.734 1.00 25.77 ?  450 ASP B CG  1 
ATOM   4149 O OD1 . ASP B 1 227 ? 24.663  11.505  -31.582 1.00 22.37 ?  450 ASP B OD1 1 
ATOM   4150 O OD2 . ASP B 1 227 ? 25.418  10.083  -33.077 1.00 21.94 ?  450 ASP B OD2 1 
ATOM   4151 N N   . CYS B 1 228 ? 20.585  12.844  -34.017 1.00 22.31 ?  451 CYS B N   1 
ATOM   4152 C CA  . CYS B 1 228 ? 19.741  13.685  -34.849 1.00 21.63 ?  451 CYS B CA  1 
ATOM   4153 C C   . CYS B 1 228 ? 20.208  15.131  -34.745 1.00 21.52 ?  451 CYS B C   1 
ATOM   4154 O O   . CYS B 1 228 ? 20.882  15.521  -33.788 1.00 19.40 ?  451 CYS B O   1 
ATOM   4155 C CB  . CYS B 1 228 ? 18.263  13.571  -34.448 1.00 22.54 ?  451 CYS B CB  1 
ATOM   4156 S SG  . CYS B 1 228 ? 17.856  14.260  -32.827 1.00 20.75 ?  451 CYS B SG  1 
ATOM   4157 N N   . LEU B 1 229 ? 19.846  15.927  -35.753 1.00 20.73 ?  452 LEU B N   1 
ATOM   4158 C CA  . LEU B 1 229 ? 20.268  17.321  -35.792 1.00 19.07 ?  452 LEU B CA  1 
ATOM   4159 C C   . LEU B 1 229 ? 19.367  18.235  -34.974 1.00 19.76 ?  452 LEU B C   1 
ATOM   4160 O O   . LEU B 1 229 ? 19.820  19.299  -34.539 1.00 20.70 ?  452 LEU B O   1 
ATOM   4161 C CB  . LEU B 1 229 ? 20.317  17.819  -37.237 1.00 20.56 ?  452 LEU B CB  1 
ATOM   4162 C CG  . LEU B 1 229 ? 21.296  17.107  -38.170 1.00 20.74 ?  452 LEU B CG  1 
ATOM   4163 C CD1 . LEU B 1 229 ? 21.355  17.817  -39.514 1.00 20.88 ?  452 LEU B CD1 1 
ATOM   4164 C CD2 . LEU B 1 229 ? 22.678  17.017  -37.541 1.00 14.35 ?  452 LEU B CD2 1 
ATOM   4165 N N   . LEU B 1 230 ? 18.109  17.850  -34.760 1.00 19.41 ?  453 LEU B N   1 
ATOM   4166 C CA  . LEU B 1 230 ? 17.160  18.669  -34.031 1.00 19.53 ?  453 LEU B CA  1 
ATOM   4167 C C   . LEU B 1 230 ? 16.236  17.751  -33.250 1.00 19.53 ?  453 LEU B C   1 
ATOM   4168 O O   . LEU B 1 230 ? 15.863  16.684  -33.761 1.00 22.40 ?  453 LEU B O   1 
ATOM   4169 C CB  . LEU B 1 230 ? 16.329  19.555  -34.966 1.00 19.71 ?  453 LEU B CB  1 
ATOM   4170 C CG  . LEU B 1 230 ? 17.048  20.641  -35.766 1.00 21.32 ?  453 LEU B CG  1 
ATOM   4171 C CD1 . LEU B 1 230 ? 16.190  21.094  -36.938 1.00 20.93 ?  453 LEU B CD1 1 
ATOM   4172 C CD2 . LEU B 1 230 ? 17.401  21.816  -34.871 1.00 18.60 ?  453 LEU B CD2 1 
ATOM   4173 N N   . PRO B 1 231 ? 15.863  18.117  -32.026 1.00 18.94 ?  454 PRO B N   1 
ATOM   4174 C CA  . PRO B 1 231 ? 14.779  17.397  -31.353 1.00 18.71 ?  454 PRO B CA  1 
ATOM   4175 C C   . PRO B 1 231 ? 13.503  17.509  -32.170 1.00 18.26 ?  454 PRO B C   1 
ATOM   4176 O O   . PRO B 1 231 ? 13.239  18.535  -32.801 1.00 18.58 ?  454 PRO B O   1 
ATOM   4177 C CB  . PRO B 1 231 ? 14.656  18.119  -30.006 1.00 18.19 ?  454 PRO B CB  1 
ATOM   4178 C CG  . PRO B 1 231 ? 15.991  18.766  -29.802 1.00 19.68 ?  454 PRO B CG  1 
ATOM   4179 C CD  . PRO B 1 231 ? 16.435  19.174  -31.176 1.00 19.78 ?  454 PRO B CD  1 
ATOM   4180 N N   . GLN B 1 232 ? 12.713  16.433  -32.173 1.00 20.83 ?  455 GLN B N   1 
ATOM   4181 C CA  . GLN B 1 232 ? 11.438  16.472  -32.878 1.00 20.91 ?  455 GLN B CA  1 
ATOM   4182 C C   . GLN B 1 232 ? 10.519  17.550  -32.317 1.00 18.95 ?  455 GLN B C   1 
ATOM   4183 O O   . GLN B 1 232 ? 9.648   18.050  -33.038 1.00 19.53 ?  455 GLN B O   1 
ATOM   4184 C CB  . GLN B 1 232 ? 10.763  15.097  -32.821 1.00 20.18 ?  455 GLN B CB  1 
ATOM   4185 C CG  . GLN B 1 232 ? 9.416   15.016  -33.533 1.00 20.95 ?  455 GLN B CG  1 
ATOM   4186 C CD  . GLN B 1 232 ? 9.522   15.231  -35.034 1.00 19.87 ?  455 GLN B CD  1 
ATOM   4187 O OE1 . GLN B 1 232 ? 10.603  15.137  -35.616 1.00 18.78 ?  455 GLN B OE1 1 
ATOM   4188 N NE2 . GLN B 1 232 ? 8.394   15.528  -35.667 1.00 23.07 ?  455 GLN B NE2 1 
ATOM   4189 N N   . GLU B 1 233 ? 10.713  17.939  -31.055 1.00 20.98 ?  456 GLU B N   1 
ATOM   4190 C CA  . GLU B 1 233 ? 9.937   19.036  -30.487 1.00 22.37 ?  456 GLU B CA  1 
ATOM   4191 C C   . GLU B 1 233 ? 10.362  20.382  -31.061 1.00 19.09 ?  456 GLU B C   1 
ATOM   4192 O O   . GLU B 1 233 ? 9.546   21.308  -31.128 1.00 17.97 ?  456 GLU B O   1 
ATOM   4193 C CB  . GLU B 1 233 ? 10.068  19.034  -28.964 1.00 18.02 ?  456 GLU B CB  1 
ATOM   4194 C CG  . GLU B 1 233 ? 9.174   18.015  -28.272 1.00 19.73 ?  456 GLU B CG  1 
ATOM   4195 C CD  . GLU B 1 233 ? 9.870   16.687  -28.039 1.00 22.63 ?  456 GLU B CD  1 
ATOM   4196 O OE1 . GLU B 1 233 ? 10.920  16.442  -28.671 1.00 21.10 ?  456 GLU B OE1 1 
ATOM   4197 O OE2 . GLU B 1 233 ? 9.364   15.884  -27.228 1.00 24.88 ?  456 GLU B OE2 1 
ATOM   4198 N N   . TRP B 1 234 ? 11.627  20.515  -31.473 1.00 17.64 ?  457 TRP B N   1 
ATOM   4199 C CA  . TRP B 1 234 ? 12.058  21.745  -32.131 1.00 20.17 ?  457 TRP B CA  1 
ATOM   4200 C C   . TRP B 1 234 ? 11.477  21.848  -33.535 1.00 21.05 ?  457 TRP B C   1 
ATOM   4201 O O   . TRP B 1 234 ? 11.060  22.931  -33.962 1.00 20.88 ?  457 TRP B O   1 
ATOM   4202 C CB  . TRP B 1 234 ? 13.585  21.818  -32.181 1.00 19.64 ?  457 TRP B CB  1 
ATOM   4203 C CG  . TRP B 1 234 ? 14.231  22.066  -30.852 1.00 20.38 ?  457 TRP B CG  1 
ATOM   4204 C CD1 . TRP B 1 234 ? 13.681  21.859  -29.620 1.00 19.77 ?  457 TRP B CD1 1 
ATOM   4205 C CD2 . TRP B 1 234 ? 15.548  22.581  -30.621 1.00 21.80 ?  457 TRP B CD2 1 
ATOM   4206 N NE1 . TRP B 1 234 ? 14.577  22.205  -28.638 1.00 24.48 ?  457 TRP B NE1 1 
ATOM   4207 C CE2 . TRP B 1 234 ? 15.731  22.652  -29.226 1.00 22.68 ?  457 TRP B CE2 1 
ATOM   4208 C CE3 . TRP B 1 234 ? 16.593  22.985  -31.460 1.00 20.89 ?  457 TRP B CE3 1 
ATOM   4209 C CZ2 . TRP B 1 234 ? 16.913  23.111  -28.650 1.00 19.84 ?  457 TRP B CZ2 1 
ATOM   4210 C CZ3 . TRP B 1 234 ? 17.766  23.441  -30.886 1.00 19.10 ?  457 TRP B CZ3 1 
ATOM   4211 C CH2 . TRP B 1 234 ? 17.916  23.500  -29.495 1.00 19.11 ?  457 TRP B CH2 1 
ATOM   4212 N N   . VAL B 1 235 ? 11.452  20.731  -34.268 1.00 20.44 ?  458 VAL B N   1 
ATOM   4213 C CA  . VAL B 1 235 ? 10.801  20.700  -35.576 1.00 20.53 ?  458 VAL B CA  1 
ATOM   4214 C C   . VAL B 1 235 ? 9.351   21.144  -35.450 1.00 20.42 ?  458 VAL B C   1 
ATOM   4215 O O   . VAL B 1 235 ? 8.865   21.979  -36.222 1.00 19.87 ?  458 VAL B O   1 
ATOM   4216 C CB  . VAL B 1 235 ? 10.905  19.292  -36.192 1.00 21.31 ?  458 VAL B CB  1 
ATOM   4217 C CG1 . VAL B 1 235 ? 10.107  19.215  -37.485 1.00 17.26 ?  458 VAL B CG1 1 
ATOM   4218 C CG2 . VAL B 1 235 ? 12.360  18.918  -36.431 1.00 19.60 ?  458 VAL B CG2 1 
ATOM   4219 N N   . GLN B 1 236 ? 8.642   20.592  -34.461 1.00 19.59 ?  459 GLN B N   1 
ATOM   4220 C CA  . GLN B 1 236 ? 7.257   20.983  -34.219 1.00 20.34 ?  459 GLN B CA  1 
ATOM   4221 C C   . GLN B 1 236 ? 7.153   22.471  -33.912 1.00 21.86 ?  459 GLN B C   1 
ATOM   4222 O O   . GLN B 1 236 ? 6.292   23.171  -34.457 1.00 21.69 ?  459 GLN B O   1 
ATOM   4223 C CB  . GLN B 1 236 ? 6.677   20.163  -33.067 1.00 19.46 ?  459 GLN B CB  1 
ATOM   4224 C CG  . GLN B 1 236 ? 6.120   18.810  -33.464 1.00 22.31 ?  459 GLN B CG  1 
ATOM   4225 C CD  . GLN B 1 236 ? 5.693   17.990  -32.262 1.00 21.75 ?  459 GLN B CD  1 
ATOM   4226 O OE1 . GLN B 1 236 ? 6.243   18.134  -31.171 1.00 25.02 ?  459 GLN B OE1 1 
ATOM   4227 N NE2 . GLN B 1 236 ? 4.703   17.127  -32.455 1.00 21.44 ?  459 GLN B NE2 1 
ATOM   4228 N N   . TYR B 1 237 ? 8.029   22.970  -33.039 1.00 21.35 ?  460 TYR B N   1 
ATOM   4229 C CA  . TYR B 1 237 ? 7.945   24.364  -32.616 1.00 21.47 ?  460 TYR B CA  1 
ATOM   4230 C C   . TYR B 1 237 ? 8.237   25.314  -33.771 1.00 22.87 ?  460 TYR B C   1 
ATOM   4231 O O   . TYR B 1 237 ? 7.510   26.291  -33.983 1.00 23.57 ?  460 TYR B O   1 
ATOM   4232 C CB  . TYR B 1 237 ? 8.908   24.619  -31.459 1.00 21.31 ?  460 TYR B CB  1 
ATOM   4233 C CG  . TYR B 1 237 ? 8.577   25.856  -30.660 1.00 23.42 ?  460 TYR B CG  1 
ATOM   4234 C CD1 . TYR B 1 237 ? 7.400   25.939  -29.928 1.00 24.88 ?  460 TYR B CD1 1 
ATOM   4235 C CD2 . TYR B 1 237 ? 9.437   26.946  -30.644 1.00 23.37 ?  460 TYR B CD2 1 
ATOM   4236 C CE1 . TYR B 1 237 ? 7.091   27.070  -29.197 1.00 26.35 ?  460 TYR B CE1 1 
ATOM   4237 C CE2 . TYR B 1 237 ? 9.136   28.081  -29.918 1.00 27.66 ?  460 TYR B CE2 1 
ATOM   4238 C CZ  . TYR B 1 237 ? 7.962   28.138  -29.196 1.00 28.65 ?  460 TYR B CZ  1 
ATOM   4239 O OH  . TYR B 1 237 ? 7.659   29.268  -28.471 1.00 29.88 ?  460 TYR B OH  1 
ATOM   4240 N N   . PHE B 1 238 ? 9.305   25.047  -34.526 1.00 23.00 ?  461 PHE B N   1 
ATOM   4241 C CA  . PHE B 1 238 ? 9.662   25.929  -35.633 1.00 22.18 ?  461 PHE B CA  1 
ATOM   4242 C C   . PHE B 1 238 ? 8.571   25.946  -36.696 1.00 24.66 ?  461 PHE B C   1 
ATOM   4243 O O   . PHE B 1 238 ? 8.299   26.990  -37.301 1.00 28.16 ?  461 PHE B O   1 
ATOM   4244 C CB  . PHE B 1 238 ? 10.999  25.500  -36.240 1.00 23.42 ?  461 PHE B CB  1 
ATOM   4245 C CG  . PHE B 1 238 ? 12.151  25.546  -35.274 1.00 23.73 ?  461 PHE B CG  1 
ATOM   4246 C CD1 . PHE B 1 238 ? 12.134  26.407  -34.188 1.00 21.84 ?  461 PHE B CD1 1 
ATOM   4247 C CD2 . PHE B 1 238 ? 13.255  24.730  -35.458 1.00 22.33 ?  461 PHE B CD2 1 
ATOM   4248 C CE1 . PHE B 1 238 ? 13.195  26.449  -33.302 1.00 22.66 ?  461 PHE B CE1 1 
ATOM   4249 C CE2 . PHE B 1 238 ? 14.318  24.768  -34.576 1.00 22.67 ?  461 PHE B CE2 1 
ATOM   4250 C CZ  . PHE B 1 238 ? 14.289  25.629  -33.497 1.00 24.04 ?  461 PHE B CZ  1 
ATOM   4251 N N   . TYR B 1 239 ? 7.925   24.800  -36.926 1.00 22.75 ?  462 TYR B N   1 
ATOM   4252 C CA  . TYR B 1 239 ? 6.865   24.727  -37.926 1.00 26.41 ?  462 TYR B CA  1 
ATOM   4253 C C   . TYR B 1 239 ? 5.661   25.570  -37.519 1.00 26.62 ?  462 TYR B C   1 
ATOM   4254 O O   . TYR B 1 239 ? 5.001   26.172  -38.374 1.00 25.08 ?  462 TYR B O   1 
ATOM   4255 C CB  . TYR B 1 239 ? 6.462   23.268  -38.147 1.00 23.80 ?  462 TYR B CB  1 
ATOM   4256 C CG  . TYR B 1 239 ? 5.226   23.075  -39.002 1.00 24.65 ?  462 TYR B CG  1 
ATOM   4257 C CD1 . TYR B 1 239 ? 5.320   23.004  -40.385 1.00 24.34 ?  462 TYR B CD1 1 
ATOM   4258 C CD2 . TYR B 1 239 ? 3.968   22.944  -38.424 1.00 27.44 ?  462 TYR B CD2 1 
ATOM   4259 C CE1 . TYR B 1 239 ? 4.197   22.822  -41.172 1.00 23.07 ?  462 TYR B CE1 1 
ATOM   4260 C CE2 . TYR B 1 239 ? 2.838   22.764  -39.203 1.00 26.54 ?  462 TYR B CE2 1 
ATOM   4261 C CZ  . TYR B 1 239 ? 2.958   22.702  -40.576 1.00 27.09 ?  462 TYR B CZ  1 
ATOM   4262 O OH  . TYR B 1 239 ? 1.838   22.520  -41.355 1.00 24.72 ?  462 TYR B OH  1 
ATOM   4263 N N   . GLN B 1 240 ? 5.360   25.622  -36.221 1.00 22.44 ?  463 GLN B N   1 
ATOM   4264 C CA  . GLN B 1 240 ? 4.233   26.416  -35.743 1.00 23.05 ?  463 GLN B CA  1 
ATOM   4265 C C   . GLN B 1 240 ? 4.584   27.896  -35.678 1.00 26.33 ?  463 GLN B C   1 
ATOM   4266 O O   . GLN B 1 240 ? 3.833   28.743  -36.173 1.00 27.08 ?  463 GLN B O   1 
ATOM   4267 C CB  . GLN B 1 240 ? 3.795   25.928  -34.364 1.00 25.75 ?  463 GLN B CB  1 
ATOM   4268 C CG  . GLN B 1 240 ? 3.290   24.508  -34.334 1.00 27.18 ?  463 GLN B CG  1 
ATOM   4269 C CD  . GLN B 1 240 ? 3.075   24.014  -32.923 1.00 28.60 ?  463 GLN B CD  1 
ATOM   4270 O OE1 . GLN B 1 240 ? 4.019   23.640  -32.228 1.00 28.81 ?  463 GLN B OE1 1 
ATOM   4271 N NE2 . GLN B 1 240 ? 1.826   24.029  -32.483 1.00 28.63 ?  463 GLN B NE2 1 
ATOM   4272 N N   . GLU B 1 241 ? 5.719   28.221  -35.057 1.00 27.88 ?  464 GLU B N   1 
ATOM   4273 C CA  . GLU B 1 241 ? 6.091   29.617  -34.863 1.00 30.58 ?  464 GLU B CA  1 
ATOM   4274 C C   . GLU B 1 241 ? 6.355   30.309  -36.194 1.00 30.74 ?  464 GLU B C   1 
ATOM   4275 O O   . GLU B 1 241 ? 5.850   31.410  -36.441 1.00 28.81 ?  464 GLU B O   1 
ATOM   4276 C CB  . GLU B 1 241 ? 7.315   29.705  -33.952 1.00 29.26 ?  464 GLU B CB  1 
ATOM   4277 C CG  . GLU B 1 241 ? 7.002   29.515  -32.477 1.00 28.94 ?  464 GLU B CG  1 
ATOM   4278 C CD  . GLU B 1 241 ? 5.770   30.282  -32.037 1.00 32.60 ?  464 GLU B CD  1 
ATOM   4279 O OE1 . GLU B 1 241 ? 5.894   31.491  -31.752 1.00 36.53 ?  464 GLU B OE1 1 
ATOM   4280 O OE2 . GLU B 1 241 ? 4.679   29.676  -31.972 1.00 35.45 ?  464 GLU B OE2 1 
ATOM   4281 N N   . ALA B 1 242 ? 7.141   29.672  -37.064 1.00 30.37 ?  465 ALA B N   1 
ATOM   4282 C CA  . ALA B 1 242 ? 7.498   30.226  -38.370 1.00 29.14 ?  465 ALA B CA  1 
ATOM   4283 C C   . ALA B 1 242 ? 8.047   31.644  -38.233 1.00 28.35 ?  465 ALA B C   1 
ATOM   4284 O O   . ALA B 1 242 ? 7.661   32.564  -38.957 1.00 31.10 ?  465 ALA B O   1 
ATOM   4285 C CB  . ALA B 1 242 ? 6.306   30.187  -39.328 1.00 27.44 ?  465 ALA B CB  1 
ATOM   4286 N N   . ALA B 1 243 ? 8.955   31.818  -37.281 1.00 29.51 ?  466 ALA B N   1 
ATOM   4287 C CA  . ALA B 1 243 ? 9.499   33.143  -37.022 1.00 29.76 ?  466 ALA B CA  1 
ATOM   4288 C C   . ALA B 1 243 ? 10.607  33.463  -38.023 1.00 29.17 ?  466 ALA B C   1 
ATOM   4289 O O   . ALA B 1 243 ? 11.458  32.613  -38.300 1.00 31.41 ?  466 ALA B O   1 
ATOM   4290 C CB  . ALA B 1 243 ? 10.038  33.233  -35.596 1.00 30.63 ?  466 ALA B CB  1 
ATOM   4291 N N   . PRO B 1 244 ? 10.614  34.671  -38.587 1.00 31.41 ?  467 PRO B N   1 
ATOM   4292 C CA  . PRO B 1 244 ? 11.662  35.026  -39.552 1.00 31.36 ?  467 PRO B CA  1 
ATOM   4293 C C   . PRO B 1 244 ? 13.036  35.033  -38.900 1.00 31.92 ?  467 PRO B C   1 
ATOM   4294 O O   . PRO B 1 244 ? 13.200  35.455  -37.753 1.00 34.12 ?  467 PRO B O   1 
ATOM   4295 C CB  . PRO B 1 244 ? 11.257  36.429  -40.021 1.00 29.30 ?  467 PRO B CB  1 
ATOM   4296 C CG  . PRO B 1 244 ? 9.818   36.574  -39.657 1.00 32.63 ?  467 PRO B CG  1 
ATOM   4297 C CD  . PRO B 1 244 ? 9.600   35.728  -38.442 1.00 32.33 ?  467 PRO B CD  1 
ATOM   4298 N N   . ALA B 1 245 ? 14.028  34.556  -39.646 1.00 29.86 ?  468 ALA B N   1 
ATOM   4299 C CA  . ALA B 1 245 ? 15.409  34.531  -39.181 1.00 29.83 ?  468 ALA B CA  1 
ATOM   4300 C C   . ALA B 1 245 ? 16.055  35.874  -39.501 1.00 32.12 ?  468 ALA B C   1 
ATOM   4301 O O   . ALA B 1 245 ? 16.260  36.210  -40.672 1.00 35.30 ?  468 ALA B O   1 
ATOM   4302 C CB  . ALA B 1 245 ? 16.177  33.380  -39.826 1.00 29.52 ?  468 ALA B CB  1 
ATOM   4303 N N   . GLN B 1 246 ? 16.369  36.645  -38.461 1.00 31.05 ?  469 GLN B N   1 
ATOM   4304 C CA  . GLN B 1 246 ? 17.047  37.925  -38.620 1.00 32.48 ?  469 GLN B CA  1 
ATOM   4305 C C   . GLN B 1 246 ? 18.523  37.768  -38.952 1.00 33.98 ?  469 GLN B C   1 
ATOM   4306 O O   . GLN B 1 246 ? 19.202  38.772  -39.193 1.00 34.30 ?  469 GLN B O   1 
ATOM   4307 C CB  . GLN B 1 246 ? 16.901  38.756  -37.344 1.00 33.06 ?  469 GLN B CB  1 
ATOM   4308 C CG  . GLN B 1 246 ? 15.489  38.811  -36.791 1.00 34.22 ?  469 GLN B CG  1 
ATOM   4309 C CD  . GLN B 1 246 ? 14.586  39.744  -37.572 1.00 41.59 ?  469 GLN B CD  1 
ATOM   4310 O OE1 . GLN B 1 246 ? 14.360  39.557  -38.768 1.00 39.92 ?  469 GLN B OE1 1 
ATOM   4311 N NE2 . GLN B 1 246 ? 14.068  40.762  -36.897 1.00 45.63 ?  469 GLN B NE2 1 
ATOM   4312 N N   . SER B 1 247 ? 19.024  36.539  -38.971 1.00 30.21 ?  470 SER B N   1 
ATOM   4313 C CA  . SER B 1 247 ? 20.436  36.249  -39.154 1.00 28.10 ?  470 SER B CA  1 
ATOM   4314 C C   . SER B 1 247 ? 20.557  34.770  -39.483 1.00 32.95 ?  470 SER B C   1 
ATOM   4315 O O   . SER B 1 247 ? 19.627  33.992  -39.254 1.00 36.08 ?  470 SER B O   1 
ATOM   4316 C CB  . SER B 1 247 ? 21.247  36.603  -37.902 1.00 32.44 ?  470 SER B CB  1 
ATOM   4317 O OG  . SER B 1 247 ? 22.610  36.257  -38.054 1.00 36.10 ?  470 SER B OG  1 
ATOM   4318 N N   . ASP B 1 248 ? 21.709  34.390  -40.028 1.00 32.09 ?  471 ASP B N   1 
ATOM   4319 C CA  . ASP B 1 248 ? 21.923  32.992  -40.372 1.00 30.21 ?  471 ASP B CA  1 
ATOM   4320 C C   . ASP B 1 248 ? 22.239  32.124  -39.163 1.00 29.15 ?  471 ASP B C   1 
ATOM   4321 O O   . ASP B 1 248 ? 22.271  30.896  -39.295 1.00 26.50 ?  471 ASP B O   1 
ATOM   4322 C CB  . ASP B 1 248 ? 23.052  32.864  -41.396 1.00 32.48 ?  471 ASP B CB  1 
ATOM   4323 C CG  . ASP B 1 248 ? 22.634  33.307  -42.781 1.00 38.52 ?  471 ASP B CG  1 
ATOM   4324 O OD1 . ASP B 1 248 ? 21.465  33.714  -42.950 1.00 38.91 ?  471 ASP B OD1 1 
ATOM   4325 O OD2 . ASP B 1 248 ? 23.473  33.243  -43.704 1.00 47.57 ?  471 ASP B OD2 1 
ATOM   4326 N N   . VAL B 1 249 ? 22.463  32.722  -37.993 1.00 32.91 ?  472 VAL B N   1 
ATOM   4327 C CA  . VAL B 1 249 ? 22.950  31.993  -36.828 1.00 28.26 ?  472 VAL B CA  1 
ATOM   4328 C C   . VAL B 1 249 ? 22.277  32.548  -35.581 1.00 31.32 ?  472 VAL B C   1 
ATOM   4329 O O   . VAL B 1 249 ? 22.461  33.723  -35.243 1.00 30.70 ?  472 VAL B O   1 
ATOM   4330 C CB  . VAL B 1 249 ? 24.480  32.086  -36.691 1.00 29.20 ?  472 VAL B CB  1 
ATOM   4331 C CG1 . VAL B 1 249 ? 24.906  31.650  -35.308 1.00 32.77 ?  472 VAL B CG1 1 
ATOM   4332 C CG2 . VAL B 1 249 ? 25.166  31.241  -37.755 1.00 31.32 ?  472 VAL B CG2 1 
ATOM   4333 N N   . ALA B 1 250 ? 21.508  31.707  -34.894 1.00 27.46 ?  473 ALA B N   1 
ATOM   4334 C CA  . ALA B 1 250 ? 20.954  32.051  -33.593 1.00 27.86 ?  473 ALA B CA  1 
ATOM   4335 C C   . ALA B 1 250 ? 21.907  31.580  -32.502 1.00 28.59 ?  473 ALA B C   1 
ATOM   4336 O O   . ALA B 1 250 ? 22.372  30.435  -32.527 1.00 28.75 ?  473 ALA B O   1 
ATOM   4337 C CB  . ALA B 1 250 ? 19.575  31.419  -33.402 1.00 23.99 ?  473 ALA B CB  1 
ATOM   4338 N N   . LEU B 1 251 ? 22.201  32.463  -31.553 1.00 25.80 ?  474 LEU B N   1 
ATOM   4339 C CA  . LEU B 1 251 ? 23.079  32.133  -30.439 1.00 24.75 ?  474 LEU B CA  1 
ATOM   4340 C C   . LEU B 1 251 ? 22.245  31.557  -29.301 1.00 24.78 ?  474 LEU B C   1 
ATOM   4341 O O   . LEU B 1 251 ? 21.400  32.255  -28.728 1.00 24.92 ?  474 LEU B O   1 
ATOM   4342 C CB  . LEU B 1 251 ? 23.854  33.365  -29.974 1.00 24.69 ?  474 LEU B CB  1 
ATOM   4343 C CG  . LEU B 1 251 ? 24.648  33.222  -28.673 1.00 23.33 ?  474 LEU B CG  1 
ATOM   4344 C CD1 . LEU B 1 251 ? 25.662  32.091  -28.779 1.00 23.56 ?  474 LEU B CD1 1 
ATOM   4345 C CD2 . LEU B 1 251 ? 25.334  34.531  -28.311 1.00 27.10 ?  474 LEU B CD2 1 
ATOM   4346 N N   . LEU B 1 252 ? 22.474  30.287  -28.984 1.00 21.62 ?  475 LEU B N   1 
ATOM   4347 C CA  . LEU B 1 252 ? 21.802  29.615  -27.884 1.00 23.96 ?  475 LEU B CA  1 
ATOM   4348 C C   . LEU B 1 252 ? 22.776  29.387  -26.737 1.00 26.70 ?  475 LEU B C   1 
ATOM   4349 O O   . LEU B 1 252 ? 23.998  29.412  -26.911 1.00 27.59 ?  475 LEU B O   1 
ATOM   4350 C CB  . LEU B 1 252 ? 21.205  28.273  -28.325 1.00 23.65 ?  475 LEU B CB  1 
ATOM   4351 C CG  . LEU B 1 252 ? 20.391  28.203  -29.619 1.00 21.98 ?  475 LEU B CG  1 
ATOM   4352 C CD1 . LEU B 1 252 ? 19.744  26.832  -29.749 1.00 20.96 ?  475 LEU B CD1 1 
ATOM   4353 C CD2 . LEU B 1 252 ? 19.341  29.300  -29.671 1.00 18.47 ?  475 LEU B CD2 1 
ATOM   4354 N N   . ARG B 1 253 ? 22.214  29.164  -25.552 1.00 25.32 ?  476 ARG B N   1 
ATOM   4355 C CA  . ARG B 1 253 ? 22.988  28.864  -24.356 1.00 25.47 ?  476 ARG B CA  1 
ATOM   4356 C C   . ARG B 1 253 ? 22.353  27.682  -23.640 1.00 27.46 ?  476 ARG B C   1 
ATOM   4357 O O   . ARG B 1 253 ? 21.138  27.665  -23.418 1.00 25.70 ?  476 ARG B O   1 
ATOM   4358 C CB  . ARG B 1 253 ? 23.066  30.079  -23.424 1.00 27.20 ?  476 ARG B CB  1 
ATOM   4359 C CG  . ARG B 1 253 ? 23.620  31.333  -24.086 1.00 29.35 ?  476 ARG B CG  1 
ATOM   4360 C CD  . ARG B 1 253 ? 24.822  31.876  -23.332 1.00 32.46 ?  476 ARG B CD  1 
ATOM   4361 N NE  . ARG B 1 253 ? 25.633  32.766  -24.155 1.00 32.69 ?  476 ARG B NE  1 
ATOM   4362 C CZ  . ARG B 1 253 ? 25.417  34.067  -24.293 1.00 32.05 ?  476 ARG B CZ  1 
ATOM   4363 N NH1 . ARG B 1 253 ? 24.403  34.667  -23.691 1.00 31.29 ?  476 ARG B NH1 1 
ATOM   4364 N NH2 . ARG B 1 253 ? 26.239  34.785  -25.053 1.00 36.92 ?  476 ARG B NH2 1 
ATOM   4365 N N   . PHE B 1 254 ? 23.175  26.697  -23.290 1.00 28.90 ?  477 PHE B N   1 
ATOM   4366 C CA  . PHE B 1 254 ? 22.714  25.495  -22.607 1.00 24.67 ?  477 PHE B CA  1 
ATOM   4367 C C   . PHE B 1 254 ? 22.702  25.755  -21.105 1.00 26.69 ?  477 PHE B C   1 
ATOM   4368 O O   . PHE B 1 254 ? 23.751  26.019  -20.508 1.00 27.07 ?  477 PHE B O   1 
ATOM   4369 C CB  . PHE B 1 254 ? 23.619  24.314  -22.949 1.00 25.06 ?  477 PHE B CB  1 
ATOM   4370 C CG  . PHE B 1 254 ? 23.057  22.981  -22.556 1.00 25.06 ?  477 PHE B CG  1 
ATOM   4371 C CD1 . PHE B 1 254 ? 21.898  22.502  -23.144 1.00 22.76 ?  477 PHE B CD1 1 
ATOM   4372 C CD2 . PHE B 1 254 ? 23.693  22.200  -21.606 1.00 25.00 ?  477 PHE B CD2 1 
ATOM   4373 C CE1 . PHE B 1 254 ? 21.382  21.272  -22.787 1.00 23.63 ?  477 PHE B CE1 1 
ATOM   4374 C CE2 . PHE B 1 254 ? 23.183  20.968  -21.247 1.00 23.60 ?  477 PHE B CE2 1 
ATOM   4375 C CZ  . PHE B 1 254 ? 22.027  20.504  -21.838 1.00 26.04 ?  477 PHE B CZ  1 
ATOM   4376 N N   . VAL B 1 255 ? 21.520  25.672  -20.496 1.00 28.20 ?  478 VAL B N   1 
ATOM   4377 C CA  . VAL B 1 255 ? 21.313  26.108  -19.119 1.00 26.17 ?  478 VAL B CA  1 
ATOM   4378 C C   . VAL B 1 255 ? 20.727  24.959  -18.310 1.00 26.37 ?  478 VAL B C   1 
ATOM   4379 O O   . VAL B 1 255 ? 19.769  24.313  -18.745 1.00 21.63 ?  478 VAL B O   1 
ATOM   4380 C CB  . VAL B 1 255 ? 20.389  27.339  -19.051 1.00 26.31 ?  478 VAL B CB  1 
ATOM   4381 C CG1 . VAL B 1 255 ? 20.148  27.748  -17.606 1.00 28.35 ?  478 VAL B CG1 1 
ATOM   4382 C CG2 . VAL B 1 255 ? 20.981  28.491  -19.847 1.00 26.18 ?  478 VAL B CG2 1 
ATOM   4383 N N   . ASN B 1 256 ? 21.295  24.714  -17.135 1.00 26.37 ?  479 ASN B N   1 
ATOM   4384 C CA  . ASN B 1 256 ? 20.729  23.744  -16.206 1.00 27.86 ?  479 ASN B CA  1 
ATOM   4385 C C   . ASN B 1 256 ? 19.641  24.413  -15.373 1.00 26.14 ?  479 ASN B C   1 
ATOM   4386 O O   . ASN B 1 256 ? 19.942  25.345  -14.617 1.00 24.89 ?  479 ASN B O   1 
ATOM   4387 C CB  . ASN B 1 256 ? 21.815  23.178  -15.302 1.00 26.01 ?  479 ASN B CB  1 
ATOM   4388 C CG  . ASN B 1 256 ? 21.250  22.396  -14.135 1.00 27.57 ?  479 ASN B CG  1 
ATOM   4389 O OD1 . ASN B 1 256 ? 21.219  22.882  -13.006 1.00 30.50 ?  479 ASN B OD1 1 
ATOM   4390 N ND2 . ASN B 1 256 ? 20.797  21.177  -14.402 1.00 26.17 ?  479 ASN B ND2 1 
ATOM   4391 N N   . PRO B 1 257 ? 18.379  23.981  -15.477 1.00 27.99 ?  480 PRO B N   1 
ATOM   4392 C CA  . PRO B 1 257 ? 17.300  24.720  -14.793 1.00 29.55 ?  480 PRO B CA  1 
ATOM   4393 C C   . PRO B 1 257 ? 17.401  24.718  -13.275 1.00 29.93 ?  480 PRO B C   1 
ATOM   4394 O O   . PRO B 1 257 ? 17.058  25.724  -12.640 1.00 27.64 ?  480 PRO B O   1 
ATOM   4395 C CB  . PRO B 1 257 ? 16.025  24.006  -15.270 1.00 29.20 ?  480 PRO B CB  1 
ATOM   4396 C CG  . PRO B 1 257 ? 16.483  22.687  -15.813 1.00 27.39 ?  480 PRO B CG  1 
ATOM   4397 C CD  . PRO B 1 257 ? 17.860  22.913  -16.346 1.00 26.51 ?  480 PRO B CD  1 
ATOM   4398 N N   . ASP B 1 258 ? 17.850  23.614  -12.669 1.00 30.67 ?  481 ASP B N   1 
ATOM   4399 C CA  . ASP B 1 258 ? 17.910  23.532  -11.211 1.00 32.31 ?  481 ASP B CA  1 
ATOM   4400 C C   . ASP B 1 258 ? 18.829  24.583  -10.609 1.00 33.76 ?  481 ASP B C   1 
ATOM   4401 O O   . ASP B 1 258 ? 18.682  24.924  -9.430  1.00 34.53 ?  481 ASP B O   1 
ATOM   4402 C CB  . ASP B 1 258 ? 18.377  22.143  -10.779 1.00 30.64 ?  481 ASP B CB  1 
ATOM   4403 C CG  . ASP B 1 258 ? 17.693  21.036  -11.548 1.00 39.53 ?  481 ASP B CG  1 
ATOM   4404 O OD1 . ASP B 1 258 ? 17.847  20.989  -12.787 1.00 34.68 ?  481 ASP B OD1 1 
ATOM   4405 O OD2 . ASP B 1 258 ? 17.000  20.213  -10.913 1.00 44.13 ?  481 ASP B OD2 1 
ATOM   4406 N N   . THR B 1 259 ? 19.763  25.101  -11.390 1.00 29.98 ?  482 THR B N   1 
ATOM   4407 C CA  . THR B 1 259 ? 20.755  26.052  -10.922 1.00 29.75 ?  482 THR B CA  1 
ATOM   4408 C C   . THR B 1 259 ? 20.748  27.368  -11.678 1.00 31.42 ?  482 THR B C   1 
ATOM   4409 O O   . THR B 1 259 ? 21.116  28.396  -11.103 1.00 30.23 ?  482 THR B O   1 
ATOM   4410 C CB  . THR B 1 259 ? 22.154  25.431  -11.027 1.00 30.75 ?  482 THR B CB  1 
ATOM   4411 O OG1 . THR B 1 259 ? 22.375  24.991  -12.373 1.00 33.06 ?  482 THR B OG1 1 
ATOM   4412 C CG2 . THR B 1 259 ? 22.295  24.260  -10.078 1.00 30.62 ?  482 THR B CG2 1 
ATOM   4413 N N   . GLY B 1 260 ? 20.330  27.368  -12.941 1.00 25.64 ?  483 GLY B N   1 
ATOM   4414 C CA  . GLY B 1 260 ? 20.465  28.525  -13.793 1.00 26.89 ?  483 GLY B CA  1 
ATOM   4415 C C   . GLY B 1 260 ? 21.830  28.695  -14.422 1.00 27.33 ?  483 GLY B C   1 
ATOM   4416 O O   . GLY B 1 260 ? 22.046  29.686  -15.130 1.00 29.11 ?  483 GLY B O   1 
ATOM   4417 N N   . ARG B 1 261 ? 22.755  27.766  -14.194 1.00 26.47 ?  484 ARG B N   1 
ATOM   4418 C CA  . ARG B 1 261 ? 24.096  27.897  -14.746 1.00 27.35 ?  484 ARG B CA  1 
ATOM   4419 C C   . ARG B 1 261 ? 24.103  27.632  -16.243 1.00 25.52 ?  484 ARG B C   1 
ATOM   4420 O O   . ARG B 1 261 ? 23.435  26.719  -16.737 1.00 27.86 ?  484 ARG B O   1 
ATOM   4421 C CB  . ARG B 1 261 ? 25.060  26.932  -14.062 1.00 30.77 ?  484 ARG B CB  1 
ATOM   4422 C CG  . ARG B 1 261 ? 24.889  26.843  -12.573 1.00 36.56 ?  484 ARG B CG  1 
ATOM   4423 C CD  . ARG B 1 261 ? 25.922  25.924  -11.959 1.00 39.70 ?  484 ARG B CD  1 
ATOM   4424 N NE  . ARG B 1 261 ? 27.267  26.456  -12.114 1.00 41.75 ?  484 ARG B NE  1 
ATOM   4425 C CZ  . ARG B 1 261 ? 28.140  26.562  -11.124 1.00 45.84 ?  484 ARG B CZ  1 
ATOM   4426 N NH1 . ARG B 1 261 ? 27.861  26.120  -9.909  1.00 44.93 ?  484 ARG B NH1 1 
ATOM   4427 N NH2 . ARG B 1 261 ? 29.315  27.140  -11.354 1.00 47.03 ?  484 ARG B NH2 1 
ATOM   4428 N N   . VAL B 1 262 ? 24.877  28.437  -16.959 1.00 21.83 ?  485 VAL B N   1 
ATOM   4429 C CA  . VAL B 1 262 ? 25.161  28.183  -18.365 1.00 25.26 ?  485 VAL B CA  1 
ATOM   4430 C C   . VAL B 1 262 ? 26.310  27.187  -18.439 1.00 27.16 ?  485 VAL B C   1 
ATOM   4431 O O   . VAL B 1 262 ? 27.388  27.426  -17.885 1.00 23.81 ?  485 VAL B O   1 
ATOM   4432 C CB  . VAL B 1 262 ? 25.505  29.484  -19.102 1.00 27.05 ?  485 VAL B CB  1 
ATOM   4433 C CG1 . VAL B 1 262 ? 25.663  29.220  -20.588 1.00 26.26 ?  485 VAL B CG1 1 
ATOM   4434 C CG2 . VAL B 1 262 ? 24.434  30.535  -18.847 1.00 21.68 ?  485 VAL B CG2 1 
ATOM   4435 N N   . LEU B 1 263 ? 26.077  26.060  -19.109 1.00 26.85 ?  486 LEU B N   1 
ATOM   4436 C CA  . LEU B 1 263 ? 27.109  25.039  -19.229 1.00 25.90 ?  486 LEU B CA  1 
ATOM   4437 C C   . LEU B 1 263 ? 27.964  25.206  -20.478 1.00 23.10 ?  486 LEU B C   1 
ATOM   4438 O O   . LEU B 1 263 ? 29.153  24.869  -20.445 1.00 21.88 ?  486 LEU B O   1 
ATOM   4439 C CB  . LEU B 1 263 ? 26.481  23.643  -19.207 1.00 25.38 ?  486 LEU B CB  1 
ATOM   4440 C CG  . LEU B 1 263 ? 25.655  23.315  -17.960 1.00 25.65 ?  486 LEU B CG  1 
ATOM   4441 C CD1 . LEU B 1 263 ? 24.826  22.059  -18.175 1.00 25.20 ?  486 LEU B CD1 1 
ATOM   4442 C CD2 . LEU B 1 263 ? 26.555  23.168  -16.740 1.00 24.26 ?  486 LEU B CD2 1 
ATOM   4443 N N   . PHE B 1 264 ? 27.399  25.716  -21.569 1.00 25.69 ?  487 PHE B N   1 
ATOM   4444 C CA  . PHE B 1 264 ? 28.184  26.046  -22.757 1.00 24.98 ?  487 PHE B CA  1 
ATOM   4445 C C   . PHE B 1 264 ? 27.343  26.921  -23.682 1.00 27.25 ?  487 PHE B C   1 
ATOM   4446 O O   . PHE B 1 264 ? 26.189  27.250  -23.391 1.00 24.99 ?  487 PHE B O   1 
ATOM   4447 C CB  . PHE B 1 264 ? 28.690  24.792  -23.481 1.00 25.75 ?  487 PHE B CB  1 
ATOM   4448 C CG  . PHE B 1 264 ? 27.602  23.933  -24.066 1.00 24.83 ?  487 PHE B CG  1 
ATOM   4449 C CD1 . PHE B 1 264 ? 27.123  24.167  -25.345 1.00 27.18 ?  487 PHE B CD1 1 
ATOM   4450 C CD2 . PHE B 1 264 ? 27.087  22.866  -23.350 1.00 23.65 ?  487 PHE B CD2 1 
ATOM   4451 C CE1 . PHE B 1 264 ? 26.132  23.371  -25.889 1.00 25.42 ?  487 PHE B CE1 1 
ATOM   4452 C CE2 . PHE B 1 264 ? 26.101  22.063  -23.892 1.00 25.72 ?  487 PHE B CE2 1 
ATOM   4453 C CZ  . PHE B 1 264 ? 25.621  22.317  -25.161 1.00 24.02 ?  487 PHE B CZ  1 
ATOM   4454 N N   . GLU B 1 265 ? 27.949  27.289  -24.809 1.00 25.40 ?  488 GLU B N   1 
ATOM   4455 C CA  . GLU B 1 265 ? 27.366  28.141  -25.833 1.00 24.65 ?  488 GLU B CA  1 
ATOM   4456 C C   . GLU B 1 265 ? 27.321  27.371  -27.147 1.00 24.84 ?  488 GLU B C   1 
ATOM   4457 O O   . GLU B 1 265 ? 28.095  26.433  -27.359 1.00 26.25 ?  488 GLU B O   1 
ATOM   4458 C CB  . GLU B 1 265 ? 28.197  29.419  -26.004 1.00 26.51 ?  488 GLU B CB  1 
ATOM   4459 C CG  . GLU B 1 265 ? 27.432  30.720  -25.909 1.00 29.36 ?  488 GLU B CG  1 
ATOM   4460 C CD  . GLU B 1 265 ? 28.359  31.921  -25.934 1.00 30.79 ?  488 GLU B CD  1 
ATOM   4461 O OE1 . GLU B 1 265 ? 29.478  31.795  -26.476 1.00 33.12 ?  488 GLU B OE1 1 
ATOM   4462 O OE2 . GLU B 1 265 ? 27.979  32.986  -25.406 1.00 34.13 ?  488 GLU B OE2 1 
ATOM   4463 N N   . CYS B 1 266 ? 26.421  27.774  -28.042 1.00 24.37 ?  489 CYS B N   1 
ATOM   4464 C CA  . CYS B 1 266 ? 26.325  27.088  -29.325 1.00 26.84 ?  489 CYS B CA  1 
ATOM   4465 C C   . CYS B 1 266 ? 25.592  27.960  -30.334 1.00 25.22 ?  489 CYS B C   1 
ATOM   4466 O O   . CYS B 1 266 ? 24.844  28.873  -29.974 1.00 25.24 ?  489 CYS B O   1 
ATOM   4467 C CB  . CYS B 1 266 ? 25.622  25.732  -29.188 1.00 24.79 ?  489 CYS B CB  1 
ATOM   4468 S SG  . CYS B 1 266 ? 23.842  25.822  -28.902 1.00 25.61 ?  489 CYS B SG  1 
ATOM   4469 N N   . LYS B 1 267 ? 25.818  27.650  -31.609 1.00 26.03 ?  490 LYS B N   1 
ATOM   4470 C CA  . LYS B 1 267 ? 25.194  28.337  -32.733 1.00 26.84 ?  490 LYS B CA  1 
ATOM   4471 C C   . LYS B 1 267 ? 24.129  27.437  -33.342 1.00 24.71 ?  490 LYS B C   1 
ATOM   4472 O O   . LYS B 1 267 ? 24.425  26.306  -33.741 1.00 21.85 ?  490 LYS B O   1 
ATOM   4473 C CB  . LYS B 1 267 ? 26.223  28.693  -33.804 1.00 25.15 ?  490 LYS B CB  1 
ATOM   4474 C CG  . LYS B 1 267 ? 27.227  29.757  -33.435 1.00 29.02 ?  490 LYS B CG  1 
ATOM   4475 C CD  . LYS B 1 267 ? 28.168  29.970  -34.608 1.00 33.00 ?  490 LYS B CD  1 
ATOM   4476 C CE  . LYS B 1 267 ? 29.284  30.928  -34.271 1.00 32.01 ?  490 LYS B CE  1 
ATOM   4477 N NZ  . LYS B 1 267 ? 30.260  31.044  -35.392 1.00 38.02 ?  490 LYS B NZ  1 
ATOM   4478 N N   . LEU B 1 268 ? 22.903  27.942  -33.432 1.00 25.11 ?  491 LEU B N   1 
ATOM   4479 C CA  . LEU B 1 268 ? 21.846  27.286  -34.190 1.00 23.57 ?  491 LEU B CA  1 
ATOM   4480 C C   . LEU B 1 268 ? 21.769  27.944  -35.561 1.00 25.71 ?  491 LEU B C   1 
ATOM   4481 O O   . LEU B 1 268 ? 21.488  29.144  -35.664 1.00 26.03 ?  491 LEU B O   1 
ATOM   4482 C CB  . LEU B 1 268 ? 20.501  27.374  -33.470 1.00 22.78 ?  491 LEU B CB  1 
ATOM   4483 C CG  . LEU B 1 268 ? 19.297  26.857  -34.264 1.00 23.21 ?  491 LEU B CG  1 
ATOM   4484 C CD1 . LEU B 1 268 ? 19.546  25.446  -34.784 1.00 19.80 ?  491 LEU B CD1 1 
ATOM   4485 C CD2 . LEU B 1 268 ? 18.033  26.901  -33.421 1.00 22.31 ?  491 LEU B CD2 1 
ATOM   4486 N N   . HIS B 1 269 ? 22.023  27.164  -36.606 1.00 25.41 ?  492 HIS B N   1 
ATOM   4487 C CA  . HIS B 1 269 ? 22.078  27.692  -37.960 1.00 26.27 ?  492 HIS B CA  1 
ATOM   4488 C C   . HIS B 1 269 ? 20.698  27.670  -38.604 1.00 23.75 ?  492 HIS B C   1 
ATOM   4489 O O   . HIS B 1 269 ? 19.900  26.759  -38.364 1.00 21.18 ?  492 HIS B O   1 
ATOM   4490 C CB  . HIS B 1 269 ? 23.075  26.896  -38.803 1.00 24.89 ?  492 HIS B CB  1 
ATOM   4491 C CG  . HIS B 1 269 ? 24.460  26.881  -38.235 1.00 26.65 ?  492 HIS B CG  1 
ATOM   4492 N ND1 . HIS B 1 269 ? 25.436  27.771  -38.629 1.00 27.20 ?  492 HIS B ND1 1 
ATOM   4493 C CD2 . HIS B 1 269 ? 25.028  26.093  -37.292 1.00 26.35 ?  492 HIS B CD2 1 
ATOM   4494 C CE1 . HIS B 1 269 ? 26.547  27.528  -37.958 1.00 30.41 ?  492 HIS B CE1 1 
ATOM   4495 N NE2 . HIS B 1 269 ? 26.327  26.515  -37.140 1.00 28.66 ?  492 HIS B NE2 1 
ATOM   4496 N N   . LYS B 1 270 ? 20.432  28.689  -39.423 1.00 27.51 ?  493 LYS B N   1 
ATOM   4497 C CA  . LYS B 1 270 ? 19.155  28.890  -40.101 1.00 24.77 ?  493 LYS B CA  1 
ATOM   4498 C C   . LYS B 1 270 ? 18.635  27.618  -40.760 1.00 25.55 ?  493 LYS B C   1 
ATOM   4499 O O   . LYS B 1 270 ? 17.432  27.340  -40.720 1.00 23.46 ?  493 LYS B O   1 
ATOM   4500 C CB  . LYS B 1 270 ? 19.299  29.999  -41.146 1.00 29.20 ?  493 LYS B CB  1 
ATOM   4501 C CG  . LYS B 1 270 ? 17.995  30.621  -41.617 1.00 31.28 ?  493 LYS B CG  1 
ATOM   4502 C CD  . LYS B 1 270 ? 18.160  31.211  -43.011 1.00 35.05 ?  493 LYS B CD  1 
ATOM   4503 C CE  . LYS B 1 270 ? 17.210  32.374  -43.249 1.00 39.49 ?  493 LYS B CE  1 
ATOM   4504 N NZ  . LYS B 1 270 ? 17.648  33.219  -44.396 1.00 38.76 ?  493 LYS B NZ  1 
ATOM   4505 N N   . SER B 1 271 ? 19.533  26.837  -41.361 1.00 22.91 ?  494 SER B N   1 
ATOM   4506 C CA  . SER B 1 271 ? 19.142  25.646  -42.104 1.00 26.58 ?  494 SER B CA  1 
ATOM   4507 C C   . SER B 1 271 ? 18.775  24.466  -41.212 1.00 23.87 ?  494 SER B C   1 
ATOM   4508 O O   . SER B 1 271 ? 18.280  23.457  -41.726 1.00 23.87 ?  494 SER B O   1 
ATOM   4509 C CB  . SER B 1 271 ? 20.263  25.237  -43.063 1.00 27.82 ?  494 SER B CB  1 
ATOM   4510 O OG  . SER B 1 271 ? 21.394  26.074  -42.907 1.00 29.39 ?  494 SER B OG  1 
ATOM   4511 N N   . GLY B 1 272 ? 19.010  24.555  -39.905 1.00 22.84 ?  495 GLY B N   1 
ATOM   4512 C CA  . GLY B 1 272 ? 18.528  23.534  -38.995 1.00 24.88 ?  495 GLY B CA  1 
ATOM   4513 C C   . GLY B 1 272 ? 19.563  22.552  -38.488 1.00 23.44 ?  495 GLY B C   1 
ATOM   4514 O O   . GLY B 1 272 ? 19.365  21.336  -38.572 1.00 20.98 ?  495 GLY B O   1 
ATOM   4515 N N   . TYR B 1 273 ? 20.669  23.064  -37.956 1.00 22.40 ?  496 TYR B N   1 
ATOM   4516 C CA  . TYR B 1 273 ? 21.652  22.232  -37.275 1.00 21.19 ?  496 TYR B CA  1 
ATOM   4517 C C   . TYR B 1 273 ? 22.433  23.117  -36.314 1.00 20.31 ?  496 TYR B C   1 
ATOM   4518 O O   . TYR B 1 273 ? 22.350  24.347  -36.366 1.00 23.72 ?  496 TYR B O   1 
ATOM   4519 C CB  . TYR B 1 273 ? 22.578  21.514  -38.266 1.00 25.34 ?  496 TYR B CB  1 
ATOM   4520 C CG  . TYR B 1 273 ? 23.470  22.429  -39.070 1.00 27.73 ?  496 TYR B CG  1 
ATOM   4521 C CD1 . TYR B 1 273 ? 23.003  23.055  -40.218 1.00 26.91 ?  496 TYR B CD1 1 
ATOM   4522 C CD2 . TYR B 1 273 ? 24.786  22.658  -38.687 1.00 26.07 ?  496 TYR B CD2 1 
ATOM   4523 C CE1 . TYR B 1 273 ? 23.818  23.887  -40.958 1.00 26.83 ?  496 TYR B CE1 1 
ATOM   4524 C CE2 . TYR B 1 273 ? 25.608  23.489  -39.421 1.00 25.02 ?  496 TYR B CE2 1 
ATOM   4525 C CZ  . TYR B 1 273 ? 25.119  24.101  -40.555 1.00 28.58 ?  496 TYR B CZ  1 
ATOM   4526 O OH  . TYR B 1 273 ? 25.932  24.930  -41.291 1.00 38.37 ?  496 TYR B OH  1 
ATOM   4527 N N   . VAL B 1 274 ? 23.188  22.474  -35.427 1.00 20.31 ?  497 VAL B N   1 
ATOM   4528 C CA  . VAL B 1 274 ? 23.857  23.154  -34.323 1.00 22.74 ?  497 VAL B CA  1 
ATOM   4529 C C   . VAL B 1 274 ? 25.345  22.838  -34.366 1.00 23.22 ?  497 VAL B C   1 
ATOM   4530 O O   . VAL B 1 274 ? 25.742  21.712  -34.686 1.00 24.75 ?  497 VAL B O   1 
ATOM   4531 C CB  . VAL B 1 274 ? 23.253  22.744  -32.962 1.00 20.53 ?  497 VAL B CB  1 
ATOM   4532 C CG1 . VAL B 1 274 ? 23.859  23.567  -31.835 1.00 21.42 ?  497 VAL B CG1 1 
ATOM   4533 C CG2 . VAL B 1 274 ? 21.738  22.891  -32.981 1.00 18.27 ?  497 VAL B CG2 1 
ATOM   4534 N N   . THR B 1 275 ? 26.169  23.837  -34.046 1.00 25.69 ?  498 THR B N   1 
ATOM   4535 C CA  . THR B 1 275 ? 27.609  23.665  -33.925 1.00 25.23 ?  498 THR B CA  1 
ATOM   4536 C C   . THR B 1 275 ? 28.093  24.293  -32.626 1.00 25.99 ?  498 THR B C   1 
ATOM   4537 O O   . THR B 1 275 ? 27.487  25.234  -32.106 1.00 24.88 ?  498 THR B O   1 
ATOM   4538 C CB  . THR B 1 275 ? 28.371  24.286  -35.110 1.00 25.16 ?  498 THR B CB  1 
ATOM   4539 O OG1 . THR B 1 275 ? 28.010  25.665  -35.250 1.00 24.75 ?  498 THR B OG1 1 
ATOM   4540 C CG2 . THR B 1 275 ? 28.057  23.543  -36.402 1.00 25.41 ?  498 THR B CG2 1 
ATOM   4541 N N   . VAL B 1 276 ? 29.198  23.757  -32.107 1.00 25.15 ?  499 VAL B N   1 
ATOM   4542 C CA  . VAL B 1 276 ? 29.816  24.232  -30.878 1.00 26.71 ?  499 VAL B CA  1 
ATOM   4543 C C   . VAL B 1 276 ? 31.300  24.454  -31.142 1.00 25.06 ?  499 VAL B C   1 
ATOM   4544 O O   . VAL B 1 276 ? 31.849  24.002  -32.146 1.00 25.53 ?  499 VAL B O   1 
ATOM   4545 C CB  . VAL B 1 276 ? 29.624  23.246  -29.708 1.00 27.83 ?  499 VAL B CB  1 
ATOM   4546 C CG1 . VAL B 1 276 ? 28.182  23.244  -29.237 1.00 25.91 ?  499 VAL B CG1 1 
ATOM   4547 C CG2 . VAL B 1 276 ? 30.059  21.849  -30.121 1.00 25.24 ?  499 VAL B CG2 1 
ATOM   4548 N N   . ALA B 1 277 ? 31.949  25.155  -30.215 1.00 25.27 ?  500 ALA B N   1 
ATOM   4549 C CA  . ALA B 1 277 ? 33.394  25.380  -30.270 1.00 28.33 ?  500 ALA B CA  1 
ATOM   4550 C C   . ALA B 1 277 ? 34.086  24.229  -29.546 1.00 33.92 ?  500 ALA B C   1 
ATOM   4551 O O   . ALA B 1 277 ? 34.239  24.248  -28.322 1.00 35.38 ?  500 ALA B O   1 
ATOM   4552 C CB  . ALA B 1 277 ? 33.756  26.728  -29.660 1.00 28.35 ?  500 ALA B CB  1 
ATOM   4553 N N   . HIS B 1 278 ? 34.512  23.227  -30.314 1.00 30.51 ?  501 HIS B N   1 
ATOM   4554 C CA  . HIS B 1 278 ? 35.137  22.017  -29.791 1.00 35.47 ?  501 HIS B CA  1 
ATOM   4555 C C   . HIS B 1 278 ? 35.913  21.392  -30.940 1.00 34.43 ?  501 HIS B C   1 
ATOM   4556 O O   . HIS B 1 278 ? 35.384  21.308  -32.050 1.00 37.23 ?  501 HIS B O   1 
ATOM   4557 C CB  . HIS B 1 278 ? 34.077  21.050  -29.246 1.00 32.27 ?  501 HIS B CB  1 
ATOM   4558 C CG  . HIS B 1 278 ? 34.637  19.764  -28.727 1.00 34.72 ?  501 HIS B CG  1 
ATOM   4559 N ND1 . HIS B 1 278 ? 34.718  18.624  -29.496 1.00 34.85 ?  501 HIS B ND1 1 
ATOM   4560 C CD2 . HIS B 1 278 ? 35.130  19.434  -27.510 1.00 34.79 ?  501 HIS B CD2 1 
ATOM   4561 C CE1 . HIS B 1 278 ? 35.247  17.649  -28.779 1.00 31.57 ?  501 HIS B CE1 1 
ATOM   4562 N NE2 . HIS B 1 278 ? 35.505  18.113  -27.570 1.00 33.01 ?  501 HIS B NE2 1 
ATOM   4563 N N   . THR B 1 279 ? 37.167  20.975  -30.694 1.00 38.31 ?  502 THR B N   1 
ATOM   4564 C CA  . THR B 1 279 ? 38.018  20.621  -31.829 1.00 43.84 ?  502 THR B CA  1 
ATOM   4565 C C   . THR B 1 279 ? 39.100  19.599  -31.496 1.00 42.43 ?  502 THR B C   1 
ATOM   4566 O O   . THR B 1 279 ? 40.155  19.588  -32.141 1.00 48.09 ?  502 THR B O   1 
ATOM   4567 C CB  . THR B 1 279 ? 38.673  21.874  -32.426 1.00 42.59 ?  502 THR B CB  1 
ATOM   4568 O OG1 . THR B 1 279 ? 38.621  22.950  -31.478 1.00 39.79 ?  502 THR B OG1 1 
ATOM   4569 C CG2 . THR B 1 279 ? 37.939  22.279  -33.680 1.00 38.42 ?  502 THR B CG2 1 
ATOM   4570 N N   . GLY B 1 280 ? 38.860  18.729  -30.525 1.00 40.89 ?  503 GLY B N   1 
ATOM   4571 C CA  . GLY B 1 280 ? 39.694  17.561  -30.358 1.00 48.31 ?  503 GLY B CA  1 
ATOM   4572 C C   . GLY B 1 280 ? 39.328  16.485  -31.363 1.00 39.67 ?  503 GLY B C   1 
ATOM   4573 O O   . GLY B 1 280 ? 38.373  16.600  -32.132 1.00 36.44 ?  503 GLY B O   1 
ATOM   4574 N N   . GLN B 1 281 ? 40.130  15.426  -31.376 1.00 41.51 ?  504 GLN B N   1 
ATOM   4575 C CA  . GLN B 1 281 ? 39.719  14.194  -32.031 1.00 41.61 ?  504 GLN B CA  1 
ATOM   4576 C C   . GLN B 1 281 ? 38.935  13.294  -31.091 1.00 42.36 ?  504 GLN B C   1 
ATOM   4577 O O   . GLN B 1 281 ? 38.512  12.207  -31.497 1.00 43.41 ?  504 GLN B O   1 
ATOM   4578 C CB  . GLN B 1 281 ? 40.933  13.439  -32.587 1.00 41.51 ?  504 GLN B CB  1 
ATOM   4579 C CG  . GLN B 1 281 ? 41.334  13.853  -34.000 1.00 41.10 ?  504 GLN B CG  1 
ATOM   4580 C CD  . GLN B 1 281 ? 40.397  13.307  -35.067 1.00 48.46 ?  504 GLN B CD  1 
ATOM   4581 O OE1 . GLN B 1 281 ? 40.107  12.111  -35.105 1.00 53.52 ?  504 GLN B OE1 1 
ATOM   4582 N NE2 . GLN B 1 281 ? 39.921  14.188  -35.941 1.00 45.42 ?  504 GLN B NE2 1 
ATOM   4583 N N   . HIS B 1 282 ? 38.729  13.731  -29.853 1.00 39.66 ?  505 HIS B N   1 
ATOM   4584 C CA  . HIS B 1 282 ? 38.013  12.976  -28.839 1.00 39.53 ?  505 HIS B CA  1 
ATOM   4585 C C   . HIS B 1 282 ? 36.557  13.417  -28.781 1.00 35.54 ?  505 HIS B C   1 
ATOM   4586 O O   . HIS B 1 282 ? 36.227  14.578  -29.035 1.00 34.69 ?  505 HIS B O   1 
ATOM   4587 C CB  . HIS B 1 282 ? 38.662  13.162  -27.467 1.00 41.99 ?  505 HIS B CB  1 
ATOM   4588 C CG  . HIS B 1 282 ? 40.021  12.545  -27.352 1.00 46.94 ?  505 HIS B CG  1 
ATOM   4589 N ND1 . HIS B 1 282 ? 41.142  13.274  -27.019 1.00 51.50 ?  505 HIS B ND1 1 
ATOM   4590 C CD2 . HIS B 1 282 ? 40.437  11.268  -27.518 1.00 50.58 ?  505 HIS B CD2 1 
ATOM   4591 C CE1 . HIS B 1 282 ? 42.192  12.472  -26.988 1.00 53.21 ?  505 HIS B CE1 1 
ATOM   4592 N NE2 . HIS B 1 282 ? 41.791  11.250  -27.287 1.00 53.51 ?  505 HIS B NE2 1 
ATOM   4593 N N   . ASP B 1 283 ? 35.688  12.474  -28.436 1.00 36.22 ?  506 ASP B N   1 
ATOM   4594 C CA  . ASP B 1 283 ? 34.272  12.764  -28.297 1.00 32.61 ?  506 ASP B CA  1 
ATOM   4595 C C   . ASP B 1 283 ? 33.983  13.379  -26.932 1.00 30.22 ?  506 ASP B C   1 
ATOM   4596 O O   . ASP B 1 283 ? 34.746  13.228  -25.974 1.00 30.73 ?  506 ASP B O   1 
ATOM   4597 C CB  . ASP B 1 283 ? 33.442  11.494  -28.482 1.00 33.42 ?  506 ASP B CB  1 
ATOM   4598 C CG  . ASP B 1 283 ? 33.747  10.780  -29.784 1.00 35.52 ?  506 ASP B CG  1 
ATOM   4599 O OD1 . ASP B 1 283 ? 34.133  11.456  -30.761 1.00 37.83 ?  506 ASP B OD1 1 
ATOM   4600 O OD2 . ASP B 1 283 ? 33.603  9.541   -29.829 1.00 37.19 ?  506 ASP B OD2 1 
ATOM   4601 N N   . LEU B 1 284 ? 32.858  14.085  -26.855 1.00 31.33 ?  507 LEU B N   1 
ATOM   4602 C CA  . LEU B 1 284 ? 32.375  14.671  -25.611 1.00 27.82 ?  507 LEU B CA  1 
ATOM   4603 C C   . LEU B 1 284 ? 30.885  14.392  -25.502 1.00 27.40 ?  507 LEU B C   1 
ATOM   4604 O O   . LEU B 1 284 ? 30.117  14.745  -26.404 1.00 25.30 ?  507 LEU B O   1 
ATOM   4605 C CB  . LEU B 1 284 ? 32.651  16.177  -25.559 1.00 25.00 ?  507 LEU B CB  1 
ATOM   4606 C CG  . LEU B 1 284 ? 32.025  16.942  -24.391 1.00 27.05 ?  507 LEU B CG  1 
ATOM   4607 C CD1 . LEU B 1 284 ? 32.830  16.738  -23.117 1.00 30.17 ?  507 LEU B CD1 1 
ATOM   4608 C CD2 . LEU B 1 284 ? 31.904  18.422  -24.720 1.00 29.78 ?  507 LEU B CD2 1 
ATOM   4609 N N   . VAL B 1 285 ? 30.480  13.752  -24.408 1.00 25.11 ?  508 VAL B N   1 
ATOM   4610 C CA  . VAL B 1 285 ? 29.086  13.415  -24.150 1.00 22.79 ?  508 VAL B CA  1 
ATOM   4611 C C   . VAL B 1 285 ? 28.605  14.241  -22.966 1.00 22.10 ?  508 VAL B C   1 
ATOM   4612 O O   . VAL B 1 285 ? 29.307  14.362  -21.955 1.00 24.38 ?  508 VAL B O   1 
ATOM   4613 C CB  . VAL B 1 285 ? 28.907  11.907  -23.887 1.00 23.33 ?  508 VAL B CB  1 
ATOM   4614 C CG1 . VAL B 1 285 ? 27.472  11.596  -23.491 1.00 24.68 ?  508 VAL B CG1 1 
ATOM   4615 C CG2 . VAL B 1 285 ? 29.309  11.106  -25.116 1.00 23.80 ?  508 VAL B CG2 1 
ATOM   4616 N N   . ILE B 1 286 ? 27.411  14.808  -23.095 1.00 19.85 ?  509 ILE B N   1 
ATOM   4617 C CA  . ILE B 1 286 ? 26.852  15.723  -22.109 1.00 24.82 ?  509 ILE B CA  1 
ATOM   4618 C C   . ILE B 1 286 ? 25.548  15.133  -21.584 1.00 23.48 ?  509 ILE B C   1 
ATOM   4619 O O   . ILE B 1 286 ? 24.643  14.841  -22.370 1.00 22.03 ?  509 ILE B O   1 
ATOM   4620 C CB  . ILE B 1 286 ? 26.612  17.122  -22.699 1.00 23.35 ?  509 ILE B CB  1 
ATOM   4621 C CG1 . ILE B 1 286 ? 27.944  17.781  -23.050 1.00 24.98 ?  509 ILE B CG1 1 
ATOM   4622 C CG2 . ILE B 1 286 ? 25.828  17.985  -21.725 1.00 22.57 ?  509 ILE B CG2 1 
ATOM   4623 C CD1 . ILE B 1 286 ? 27.803  18.915  -24.019 1.00 27.45 ?  509 ILE B CD1 1 
ATOM   4624 N N   . PRO B 1 287 ? 25.414  14.926  -20.275 1.00 24.79 ?  510 PRO B N   1 
ATOM   4625 C CA  . PRO B 1 287 ? 24.135  14.478  -19.734 1.00 26.36 ?  510 PRO B CA  1 
ATOM   4626 C C   . PRO B 1 287 ? 23.032  15.460  -20.067 1.00 24.73 ?  510 PRO B C   1 
ATOM   4627 O O   . PRO B 1 287 ? 23.282  16.664  -20.265 1.00 24.50 ?  510 PRO B O   1 
ATOM   4628 C CB  . PRO B 1 287 ? 24.401  14.414  -18.224 1.00 27.13 ?  510 PRO B CB  1 
ATOM   4629 C CG  . PRO B 1 287 ? 25.853  14.072  -18.139 1.00 26.20 ?  510 PRO B CG  1 
ATOM   4630 C CD  . PRO B 1 287 ? 26.512  14.771  -19.307 1.00 26.53 ?  510 PRO B CD  1 
ATOM   4631 N N   . PRO B 1 288 ? 21.781  14.992  -20.126 1.00 24.57 ?  511 PRO B N   1 
ATOM   4632 C CA  . PRO B 1 288 ? 20.708  15.808  -20.706 1.00 24.91 ?  511 PRO B CA  1 
ATOM   4633 C C   . PRO B 1 288 ? 19.969  16.680  -19.703 1.00 27.79 ?  511 PRO B C   1 
ATOM   4634 O O   . PRO B 1 288 ? 18.793  16.997  -19.913 1.00 27.23 ?  511 PRO B O   1 
ATOM   4635 C CB  . PRO B 1 288 ? 19.772  14.748  -21.292 1.00 23.35 ?  511 PRO B CB  1 
ATOM   4636 C CG  . PRO B 1 288 ? 19.882  13.624  -20.301 1.00 25.95 ?  511 PRO B CG  1 
ATOM   4637 C CD  . PRO B 1 288 ? 21.304  13.644  -19.767 1.00 24.63 ?  511 PRO B CD  1 
ATOM   4638 N N   . ASN B 1 289 ? 20.629  17.077  -18.618 1.00 25.15 ?  512 ASN B N   1 
ATOM   4639 C CA  . ASN B 1 289 ? 19.969  17.853  -17.567 1.00 25.34 ?  512 ASN B CA  1 
ATOM   4640 C C   . ASN B 1 289 ? 20.077  19.354  -17.847 1.00 26.29 ?  512 ASN B C   1 
ATOM   4641 O O   . ASN B 1 289 ? 20.567  20.143  -17.040 1.00 28.58 ?  512 ASN B O   1 
ATOM   4642 C CB  . ASN B 1 289 ? 20.550  17.493  -16.204 1.00 26.09 ?  512 ASN B CB  1 
ATOM   4643 C CG  . ASN B 1 289 ? 22.028  17.809  -16.095 1.00 26.39 ?  512 ASN B CG  1 
ATOM   4644 O OD1 . ASN B 1 289 ? 22.793  17.588  -17.034 1.00 30.67 ?  512 ASN B OD1 1 
ATOM   4645 N ND2 . ASN B 1 289 ? 22.438  18.333  -14.945 1.00 27.59 ?  512 ASN B ND2 1 
ATOM   4646 N N   . GLY B 1 290 ? 19.588  19.746  -19.018 1.00 25.85 ?  513 GLY B N   1 
ATOM   4647 C CA  . GLY B 1 290 ? 19.618  21.145  -19.396 1.00 22.90 ?  513 GLY B CA  1 
ATOM   4648 C C   . GLY B 1 290 ? 18.750  21.411  -20.602 1.00 22.22 ?  513 GLY B C   1 
ATOM   4649 O O   . GLY B 1 290 ? 18.446  20.508  -21.388 1.00 21.87 ?  513 GLY B O   1 
ATOM   4650 N N   . TYR B 1 291 ? 18.356  22.673  -20.736 1.00 23.49 ?  514 TYR B N   1 
ATOM   4651 C CA  . TYR B 1 291 ? 17.568  23.163  -21.857 1.00 21.76 ?  514 TYR B CA  1 
ATOM   4652 C C   . TYR B 1 291 ? 18.345  24.251  -22.589 1.00 25.51 ?  514 TYR B C   1 
ATOM   4653 O O   . TYR B 1 291 ? 19.348  24.774  -22.095 1.00 24.36 ?  514 TYR B O   1 
ATOM   4654 C CB  . TYR B 1 291 ? 16.208  23.695  -21.383 1.00 22.89 ?  514 TYR B CB  1 
ATOM   4655 C CG  . TYR B 1 291 ? 16.280  25.018  -20.652 1.00 25.65 ?  514 TYR B CG  1 
ATOM   4656 C CD1 . TYR B 1 291 ? 16.578  25.069  -19.296 1.00 25.86 ?  514 TYR B CD1 1 
ATOM   4657 C CD2 . TYR B 1 291 ? 16.039  26.216  -21.315 1.00 26.23 ?  514 TYR B CD2 1 
ATOM   4658 C CE1 . TYR B 1 291 ? 16.643  26.274  -18.623 1.00 26.45 ?  514 TYR B CE1 1 
ATOM   4659 C CE2 . TYR B 1 291 ? 16.103  27.425  -20.651 1.00 26.45 ?  514 TYR B CE2 1 
ATOM   4660 C CZ  . TYR B 1 291 ? 16.404  27.449  -19.306 1.00 30.05 ?  514 TYR B CZ  1 
ATOM   4661 O OH  . TYR B 1 291 ? 16.466  28.652  -18.641 1.00 30.06 ?  514 TYR B OH  1 
ATOM   4662 N N   . PHE B 1 292 ? 17.866  24.594  -23.782 1.00 20.61 ?  515 PHE B N   1 
ATOM   4663 C CA  . PHE B 1 292 ? 18.497  25.602  -24.622 1.00 23.63 ?  515 PHE B CA  1 
ATOM   4664 C C   . PHE B 1 292 ? 17.714  26.907  -24.552 1.00 23.10 ?  515 PHE B C   1 
ATOM   4665 O O   . PHE B 1 292 ? 16.481  26.902  -24.508 1.00 23.50 ?  515 PHE B O   1 
ATOM   4666 C CB  . PHE B 1 292 ? 18.592  25.123  -26.072 1.00 21.38 ?  515 PHE B CB  1 
ATOM   4667 C CG  . PHE B 1 292 ? 19.529  23.965  -26.269 1.00 19.44 ?  515 PHE B CG  1 
ATOM   4668 C CD1 . PHE B 1 292 ? 19.119  22.670  -25.994 1.00 18.51 ?  515 PHE B CD1 1 
ATOM   4669 C CD2 . PHE B 1 292 ? 20.820  24.171  -26.726 1.00 22.82 ?  515 PHE B CD2 1 
ATOM   4670 C CE1 . PHE B 1 292 ? 19.979  21.603  -26.172 1.00 22.24 ?  515 PHE B CE1 1 
ATOM   4671 C CE2 . PHE B 1 292 ? 21.685  23.107  -26.907 1.00 21.12 ?  515 PHE B CE2 1 
ATOM   4672 C CZ  . PHE B 1 292 ? 21.263  21.821  -26.630 1.00 19.81 ?  515 PHE B CZ  1 
ATOM   4673 N N   . ARG B 1 293 ? 18.439  28.025  -24.546 1.00 25.16 ?  516 ARG B N   1 
ATOM   4674 C CA  . ARG B 1 293 ? 17.845  29.348  -24.379 1.00 26.65 ?  516 ARG B CA  1 
ATOM   4675 C C   . ARG B 1 293 ? 18.363  30.270  -25.474 1.00 26.76 ?  516 ARG B C   1 
ATOM   4676 O O   . ARG B 1 293 ? 19.559  30.581  -25.516 1.00 26.34 ?  516 ARG B O   1 
ATOM   4677 C CB  . ARG B 1 293 ? 18.159  29.918  -22.996 1.00 29.11 ?  516 ARG B CB  1 
ATOM   4678 C CG  . ARG B 1 293 ? 17.366  31.162  -22.634 1.00 28.52 ?  516 ARG B CG  1 
ATOM   4679 C CD  . ARG B 1 293 ? 17.787  31.691  -21.274 1.00 29.74 ?  516 ARG B CD  1 
ATOM   4680 N NE  . ARG B 1 293 ? 19.196  32.065  -21.260 1.00 32.90 ?  516 ARG B NE  1 
ATOM   4681 C CZ  . ARG B 1 293 ? 19.933  32.171  -20.162 1.00 34.55 ?  516 ARG B CZ  1 
ATOM   4682 N NH1 . ARG B 1 293 ? 19.425  31.939  -18.963 1.00 30.86 ?  516 ARG B NH1 1 
ATOM   4683 N NH2 . ARG B 1 293 ? 21.212  32.518  -20.271 1.00 31.12 ?  516 ARG B NH2 1 
ATOM   4684 N N   . PHE B 1 294 ? 17.465  30.703  -26.356 1.00 25.84 ?  517 PHE B N   1 
ATOM   4685 C CA  . PHE B 1 294 ? 17.812  31.690  -27.369 1.00 24.81 ?  517 PHE B CA  1 
ATOM   4686 C C   . PHE B 1 294 ? 18.099  33.030  -26.704 1.00 24.15 ?  517 PHE B C   1 
ATOM   4687 O O   . PHE B 1 294 ? 17.283  33.537  -25.930 1.00 24.33 ?  517 PHE B O   1 
ATOM   4688 C CB  . PHE B 1 294 ? 16.672  31.824  -28.380 1.00 26.57 ?  517 PHE B CB  1 
ATOM   4689 C CG  . PHE B 1 294 ? 16.863  32.932  -29.376 1.00 27.26 ?  517 PHE B CG  1 
ATOM   4690 C CD1 . PHE B 1 294 ? 17.940  32.926  -30.247 1.00 28.64 ?  517 PHE B CD1 1 
ATOM   4691 C CD2 . PHE B 1 294 ? 15.959  33.980  -29.444 1.00 26.81 ?  517 PHE B CD2 1 
ATOM   4692 C CE1 . PHE B 1 294 ? 18.113  33.944  -31.166 1.00 26.67 ?  517 PHE B CE1 1 
ATOM   4693 C CE2 . PHE B 1 294 ? 16.127  35.001  -30.360 1.00 30.16 ?  517 PHE B CE2 1 
ATOM   4694 C CZ  . PHE B 1 294 ? 17.205  34.983  -31.222 1.00 28.22 ?  517 PHE B CZ  1 
ATOM   4695 N N   . ASP B 1 295 ? 19.265  33.598  -26.994 1.00 24.42 ?  518 ASP B N   1 
ATOM   4696 C CA  . ASP B 1 295 ? 19.680  34.856  -26.385 1.00 27.89 ?  518 ASP B CA  1 
ATOM   4697 C C   . ASP B 1 295 ? 19.760  36.010  -27.366 1.00 30.68 ?  518 ASP B C   1 
ATOM   4698 O O   . ASP B 1 295 ? 19.345  37.123  -27.026 1.00 31.92 ?  518 ASP B O   1 
ATOM   4699 C CB  . ASP B 1 295 ? 21.036  34.691  -25.694 1.00 27.69 ?  518 ASP B CB  1 
ATOM   4700 C CG  . ASP B 1 295 ? 20.917  34.025  -24.348 1.00 31.94 ?  518 ASP B CG  1 
ATOM   4701 O OD1 . ASP B 1 295 ? 19.805  33.562  -24.013 1.00 33.87 ?  518 ASP B OD1 1 
ATOM   4702 O OD2 . ASP B 1 295 ? 21.928  33.978  -23.620 1.00 34.58 ?  518 ASP B OD2 1 
ATOM   4703 N N   . SER B 1 296 ? 20.287  35.773  -28.573 1.00 30.25 ?  519 SER B N   1 
ATOM   4704 C CA  . SER B 1 296 ? 20.341  36.798  -29.612 1.00 29.86 ?  519 SER B CA  1 
ATOM   4705 C C   . SER B 1 296 ? 20.767  36.249  -30.972 1.00 30.74 ?  519 SER B C   1 
ATOM   4706 O O   . SER B 1 296 ? 21.454  35.225  -31.054 1.00 28.84 ?  519 SER B O   1 
ATOM   4707 C CB  . SER B 1 296 ? 21.300  37.917  -29.204 1.00 33.69 ?  519 SER B CB  1 
ATOM   4708 O OG  . SER B 1 296 ? 22.598  37.685  -29.724 1.00 35.99 ?  519 SER B OG  1 
ATOM   4709 N N   . TRP B 1 297 ? 20.375  36.925  -32.048 1.00 31.67 ?  520 TRP B N   1 
ATOM   4710 C CA  . TRP B 1 297 ? 20.942  36.613  -33.352 1.00 29.37 ?  520 TRP B CA  1 
ATOM   4711 C C   . TRP B 1 297 ? 22.351  37.186  -33.452 1.00 30.23 ?  520 TRP B C   1 
ATOM   4712 O O   . TRP B 1 297 ? 22.650  38.252  -32.910 1.00 34.18 ?  520 TRP B O   1 
ATOM   4713 C CB  . TRP B 1 297 ? 20.070  37.177  -34.474 1.00 29.80 ?  520 TRP B CB  1 
ATOM   4714 C CG  . TRP B 1 297 ? 18.708  36.572  -34.552 1.00 29.19 ?  520 TRP B CG  1 
ATOM   4715 C CD1 . TRP B 1 297 ? 17.561  37.065  -34.005 1.00 28.55 ?  520 TRP B CD1 1 
ATOM   4716 C CD2 . TRP B 1 297 ? 18.345  35.367  -35.232 1.00 28.00 ?  520 TRP B CD2 1 
ATOM   4717 N NE1 . TRP B 1 297 ? 16.505  36.235  -34.294 1.00 26.03 ?  520 TRP B NE1 1 
ATOM   4718 C CE2 . TRP B 1 297 ? 16.960  35.185  -35.048 1.00 28.95 ?  520 TRP B CE2 1 
ATOM   4719 C CE3 . TRP B 1 297 ? 19.056  34.421  -35.976 1.00 29.17 ?  520 TRP B CE3 1 
ATOM   4720 C CZ2 . TRP B 1 297 ? 16.274  34.098  -35.580 1.00 26.40 ?  520 TRP B CZ2 1 
ATOM   4721 C CZ3 . TRP B 1 297 ? 18.374  33.343  -36.502 1.00 28.79 ?  520 TRP B CZ3 1 
ATOM   4722 C CH2 . TRP B 1 297 ? 16.997  33.189  -36.302 1.00 26.83 ?  520 TRP B CH2 1 
ATOM   4723 N N   . VAL B 1 298 ? 23.230  36.456  -34.135 1.00 31.05 ?  521 VAL B N   1 
ATOM   4724 C CA  . VAL B 1 298 ? 24.594  36.894  -34.399 1.00 31.76 ?  521 VAL B CA  1 
ATOM   4725 C C   . VAL B 1 298 ? 24.939  36.547  -35.843 1.00 36.36 ?  521 VAL B C   1 
ATOM   4726 O O   . VAL B 1 298 ? 24.146  35.935  -36.563 1.00 36.76 ?  521 VAL B O   1 
ATOM   4727 C CB  . VAL B 1 298 ? 25.618  36.261  -33.432 1.00 31.46 ?  521 VAL B CB  1 
ATOM   4728 C CG1 . VAL B 1 298 ? 25.239  36.521  -31.979 1.00 31.85 ?  521 VAL B CG1 1 
ATOM   4729 C CG2 . VAL B 1 298 ? 25.736  34.775  -33.695 1.00 35.17 ?  521 VAL B CG2 1 
ATOM   4730 N N   . ASN B 1 299 ? 26.134  36.941  -36.266 1.00 36.31 ?  522 ASN B N   1 
ATOM   4731 C CA  . ASN B 1 299 ? 26.619  36.603  -37.594 1.00 38.96 ?  522 ASN B CA  1 
ATOM   4732 C C   . ASN B 1 299 ? 27.433  35.311  -37.550 1.00 44.33 ?  522 ASN B C   1 
ATOM   4733 O O   . ASN B 1 299 ? 27.735  34.769  -36.485 1.00 44.20 ?  522 ASN B O   1 
ATOM   4734 C CB  . ASN B 1 299 ? 27.457  37.747  -38.166 1.00 43.53 ?  522 ASN B CB  1 
ATOM   4735 C CG  . ASN B 1 299 ? 26.629  38.731  -38.969 1.00 49.40 ?  522 ASN B CG  1 
ATOM   4736 O OD1 . ASN B 1 299 ? 26.516  39.903  -38.609 1.00 49.70 ?  522 ASN B OD1 1 
ATOM   4737 N ND2 . ASN B 1 299 ? 26.043  38.258  -40.063 1.00 45.80 ?  522 ASN B ND2 1 
ATOM   4738 N N   . GLN B 1 300 ? 27.786  34.815  -38.738 1.00 44.02 ?  523 GLN B N   1 
ATOM   4739 C CA  . GLN B 1 300 ? 28.638  33.636  -38.847 1.00 45.95 ?  523 GLN B CA  1 
ATOM   4740 C C   . GLN B 1 300 ? 30.037  33.877  -38.287 1.00 48.43 ?  523 GLN B C   1 
ATOM   4741 O O   . GLN B 1 300 ? 30.769  32.911  -38.045 1.00 47.04 ?  523 GLN B O   1 
ATOM   4742 C CB  . GLN B 1 300 ? 28.706  33.198  -40.318 1.00 47.23 ?  523 GLN B CB  1 
ATOM   4743 C CG  . GLN B 1 300 ? 29.465  31.904  -40.591 1.00 52.96 ?  523 GLN B CG  1 
ATOM   4744 C CD  . GLN B 1 300 ? 28.759  30.677  -40.047 1.00 54.32 ?  523 GLN B CD  1 
ATOM   4745 O OE1 . GLN B 1 300 ? 29.270  29.998  -39.155 1.00 47.99 ?  523 GLN B OE1 1 
ATOM   4746 N NE2 . GLN B 1 300 ? 27.580  30.384  -40.584 1.00 48.76 ?  523 GLN B NE2 1 
ATOM   4747 N N   . PHE B 1 301 ? 30.412  35.132  -38.051 1.00 43.70 ?  524 PHE B N   1 
ATOM   4748 C CA  . PHE B 1 301 ? 31.744  35.493  -37.587 1.00 44.12 ?  524 PHE B CA  1 
ATOM   4749 C C   . PHE B 1 301 ? 31.875  35.421  -36.073 1.00 45.08 ?  524 PHE B C   1 
ATOM   4750 O O   . PHE B 1 301 ? 32.965  35.666  -35.546 1.00 49.19 ?  524 PHE B O   1 
ATOM   4751 C CB  . PHE B 1 301 ? 32.098  36.906  -38.055 1.00 44.49 ?  524 PHE B CB  1 
ATOM   4752 C CG  . PHE B 1 301 ? 31.479  37.279  -39.367 1.00 49.02 ?  524 PHE B CG  1 
ATOM   4753 C CD1 . PHE B 1 301 ? 31.518  36.409  -40.444 1.00 48.15 ?  524 PHE B CD1 1 
ATOM   4754 C CD2 . PHE B 1 301 ? 30.822  38.489  -39.512 1.00 49.15 ?  524 PHE B CD2 1 
ATOM   4755 C CE1 . PHE B 1 301 ? 30.927  36.743  -41.633 1.00 45.16 ?  524 PHE B CE1 1 
ATOM   4756 C CE2 . PHE B 1 301 ? 30.237  38.832  -40.707 1.00 43.77 ?  524 PHE B CE2 1 
ATOM   4757 C CZ  . PHE B 1 301 ? 30.288  37.959  -41.766 1.00 47.93 ?  524 PHE B CZ  1 
ATOM   4758 N N   . TYR B 1 302 ? 30.792  35.106  -35.370 1.00 42.29 ?  525 TYR B N   1 
ATOM   4759 C CA  . TYR B 1 302 ? 30.825  35.022  -33.918 1.00 37.71 ?  525 TYR B CA  1 
ATOM   4760 C C   . TYR B 1 302 ? 31.739  33.886  -33.475 1.00 36.84 ?  525 TYR B C   1 
ATOM   4761 O O   . TYR B 1 302 ? 31.729  32.797  -34.055 1.00 38.49 ?  525 TYR B O   1 
ATOM   4762 C CB  . TYR B 1 302 ? 29.406  34.814  -33.385 1.00 35.67 ?  525 TYR B CB  1 
ATOM   4763 C CG  . TYR B 1 302 ? 29.236  35.016  -31.897 1.00 33.25 ?  525 TYR B CG  1 
ATOM   4764 C CD1 . TYR B 1 302 ? 29.564  34.013  -30.994 1.00 34.75 ?  525 TYR B CD1 1 
ATOM   4765 C CD2 . TYR B 1 302 ? 28.732  36.209  -31.396 1.00 32.83 ?  525 TYR B CD2 1 
ATOM   4766 C CE1 . TYR B 1 302 ? 29.401  34.196  -29.634 1.00 31.12 ?  525 TYR B CE1 1 
ATOM   4767 C CE2 . TYR B 1 302 ? 28.566  36.401  -30.038 1.00 30.84 ?  525 TYR B CE2 1 
ATOM   4768 C CZ  . TYR B 1 302 ? 28.902  35.391  -29.162 1.00 30.78 ?  525 TYR B CZ  1 
ATOM   4769 O OH  . TYR B 1 302 ? 28.739  35.578  -27.809 1.00 38.35 ?  525 TYR B OH  1 
ATOM   4770 N N   . THR B 1 303 ? 32.548  34.149  -32.453 1.00 35.96 ?  526 THR B N   1 
ATOM   4771 C CA  . THR B 1 303 ? 33.450  33.150  -31.894 1.00 35.08 ?  526 THR B CA  1 
ATOM   4772 C C   . THR B 1 303 ? 32.877  32.656  -30.572 1.00 33.07 ?  526 THR B C   1 
ATOM   4773 O O   . THR B 1 303 ? 32.744  33.431  -29.619 1.00 31.55 ?  526 THR B O   1 
ATOM   4774 C CB  . THR B 1 303 ? 34.854  33.722  -31.693 1.00 32.31 ?  526 THR B CB  1 
ATOM   4775 O OG1 . THR B 1 303 ? 35.353  34.216  -32.942 1.00 36.21 ?  526 THR B OG1 1 
ATOM   4776 C CG2 . THR B 1 303 ? 35.794  32.645  -31.171 1.00 33.33 ?  526 THR B CG2 1 
ATOM   4777 N N   . LEU B 1 304 ? 32.539  31.371  -30.519 1.00 32.54 ?  527 LEU B N   1 
ATOM   4778 C CA  . LEU B 1 304 ? 31.911  30.799  -29.339 1.00 30.98 ?  527 LEU B CA  1 
ATOM   4779 C C   . LEU B 1 304 ? 32.945  30.484  -28.267 1.00 34.83 ?  527 LEU B C   1 
ATOM   4780 O O   . LEU B 1 304 ? 34.119  30.236  -28.555 1.00 35.19 ?  527 LEU B O   1 
ATOM   4781 C CB  . LEU B 1 304 ? 31.152  29.521  -29.697 1.00 29.60 ?  527 LEU B CB  1 
ATOM   4782 C CG  . LEU B 1 304 ? 29.895  29.648  -30.555 1.00 29.19 ?  527 LEU B CG  1 
ATOM   4783 C CD1 . LEU B 1 304 ? 29.670  28.354  -31.316 1.00 25.50 ?  527 LEU B CD1 1 
ATOM   4784 C CD2 . LEU B 1 304 ? 28.687  29.994  -29.698 1.00 26.83 ?  527 LEU B CD2 1 
ATOM   4785 N N   . ALA B 1 305 ? 32.492  30.494  -27.021 1.00 35.11 ?  528 ALA B N   1 
ATOM   4786 C CA  . ALA B 1 305 ? 33.340  30.059  -25.922 1.00 32.93 ?  528 ALA B CA  1 
ATOM   4787 C C   . ALA B 1 305 ? 33.566  28.555  -26.025 1.00 36.10 ?  528 ALA B C   1 
ATOM   4788 O O   . ALA B 1 305 ? 32.600  27.799  -26.187 1.00 36.39 ?  528 ALA B O   1 
ATOM   4789 C CB  . ALA B 1 305 ? 32.706  30.412  -24.580 1.00 25.58 ?  528 ALA B CB  1 
ATOM   4790 N N   . PRO B 1 306 ? 34.807  28.085  -25.949 1.00 38.33 ?  529 PRO B N   1 
ATOM   4791 C CA  . PRO B 1 306 ? 35.061  26.647  -26.080 1.00 35.96 ?  529 PRO B CA  1 
ATOM   4792 C C   . PRO B 1 306 ? 34.486  25.866  -24.909 1.00 37.81 ?  529 PRO B C   1 
ATOM   4793 O O   . PRO B 1 306 ? 34.198  26.405  -23.838 1.00 42.10 ?  529 PRO B O   1 
ATOM   4794 C CB  . PRO B 1 306 ? 36.591  26.556  -26.108 1.00 40.47 ?  529 PRO B CB  1 
ATOM   4795 C CG  . PRO B 1 306 ? 37.053  27.799  -25.415 1.00 41.41 ?  529 PRO B CG  1 
ATOM   4796 C CD  . PRO B 1 306 ? 36.049  28.855  -25.771 1.00 37.48 ?  529 PRO B CD  1 
ATOM   4797 N N   . MET B 1 307 ? 34.315  24.568  -25.135 1.00 41.01 ?  530 MET B N   1 
ATOM   4798 C CA  . MET B 1 307 ? 33.835  23.666  -24.096 1.00 42.46 ?  530 MET B CA  1 
ATOM   4799 C C   . MET B 1 307 ? 34.776  22.477  -23.944 1.00 45.21 ?  530 MET B C   1 
ATOM   4800 O O   . MET B 1 307 ? 35.382  22.026  -24.917 1.00 45.63 ?  530 MET B O   1 
ATOM   4801 C CB  . MET B 1 307 ? 32.420  23.182  -24.410 1.00 35.71 ?  530 MET B CB  1 
ATOM   4802 C CG  . MET B 1 307 ? 32.287  22.496  -25.756 1.00 40.66 ?  530 MET B CG  1 
ATOM   4803 S SD  . MET B 1 307 ? 30.620  22.634  -26.414 1.00 45.54 ?  530 MET B SD  1 
ATOM   4804 C CE  . MET B 1 307 ? 29.770  21.452  -25.382 1.00 32.38 ?  530 MET B CE  1 
ATOM   4805 N N   . GLN C 2 1   ? -28.850 9.815   -35.413 1.00 33.77 ?  1   GLN C N   1 
ATOM   4806 C CA  . GLN C 2 1   ? -28.683 11.264  -35.457 1.00 32.28 ?  1   GLN C CA  1 
ATOM   4807 C C   . GLN C 2 1   ? -28.487 11.786  -36.872 1.00 30.19 ?  1   GLN C C   1 
ATOM   4808 O O   . GLN C 2 1   ? -28.481 12.994  -37.090 1.00 35.11 ?  1   GLN C O   1 
ATOM   4809 C CB  . GLN C 2 1   ? -27.496 11.697  -34.592 1.00 31.66 ?  1   GLN C CB  1 
ATOM   4810 C CG  . GLN C 2 1   ? -27.871 12.192  -33.211 1.00 25.69 ?  1   GLN C CG  1 
ATOM   4811 C CD  . GLN C 2 1   ? -26.658 12.598  -32.396 1.00 39.11 ?  1   GLN C CD  1 
ATOM   4812 O OE1 . GLN C 2 1   ? -25.554 12.727  -32.926 1.00 35.82 ?  1   GLN C OE1 1 
ATOM   4813 N NE2 . GLN C 2 1   ? -26.852 12.773  -31.092 1.00 35.07 ?  1   GLN C NE2 1 
ATOM   4814 N N   . VAL C 2 2   ? -28.324 10.880  -37.832 1.00 29.55 ?  2   VAL C N   1 
ATOM   4815 C CA  . VAL C 2 2   ? -28.028 11.245  -39.213 1.00 31.48 ?  2   VAL C CA  1 
ATOM   4816 C C   . VAL C 2 2   ? -28.962 10.475  -40.136 1.00 28.72 ?  2   VAL C C   1 
ATOM   4817 O O   . VAL C 2 2   ? -29.149 9.264   -39.967 1.00 29.95 ?  2   VAL C O   1 
ATOM   4818 C CB  . VAL C 2 2   ? -26.556 10.958  -39.575 1.00 30.51 ?  2   VAL C CB  1 
ATOM   4819 C CG1 . VAL C 2 2   ? -26.330 11.107  -41.074 1.00 30.54 ?  2   VAL C CG1 1 
ATOM   4820 C CG2 . VAL C 2 2   ? -25.623 11.875  -38.796 1.00 27.43 ?  2   VAL C CG2 1 
ATOM   4821 N N   . GLN C 2 3   ? -29.550 11.175  -41.104 1.00 30.66 ?  3   GLN C N   1 
ATOM   4822 C CA  . GLN C 2 3   ? -30.305 10.540  -42.176 1.00 31.60 ?  3   GLN C CA  1 
ATOM   4823 C C   . GLN C 2 3   ? -29.900 11.161  -43.505 1.00 28.74 ?  3   GLN C C   1 
ATOM   4824 O O   . GLN C 2 3   ? -29.906 12.388  -43.655 1.00 32.09 ?  3   GLN C O   1 
ATOM   4825 C CB  . GLN C 2 3   ? -31.823 10.655  -41.959 1.00 31.04 ?  3   GLN C CB  1 
ATOM   4826 C CG  . GLN C 2 3   ? -32.384 12.069  -41.891 1.00 36.67 ?  3   GLN C CG  1 
ATOM   4827 C CD  . GLN C 2 3   ? -33.802 12.148  -42.431 1.00 47.87 ?  3   GLN C CD  1 
ATOM   4828 O OE1 . GLN C 2 3   ? -34.751 11.699  -41.787 1.00 47.83 ?  3   GLN C OE1 1 
ATOM   4829 N NE2 . GLN C 2 3   ? -33.951 12.717  -43.622 1.00 45.53 ?  3   GLN C NE2 1 
ATOM   4830 N N   . LEU C 2 4   ? -29.519 10.311  -44.453 1.00 28.06 ?  4   LEU C N   1 
ATOM   4831 C CA  . LEU C 2 4   ? -29.225 10.712  -45.822 1.00 29.77 ?  4   LEU C CA  1 
ATOM   4832 C C   . LEU C 2 4   ? -30.391 10.268  -46.692 1.00 31.67 ?  4   LEU C C   1 
ATOM   4833 O O   . LEU C 2 4   ? -30.755 9.088   -46.686 1.00 29.89 ?  4   LEU C O   1 
ATOM   4834 C CB  . LEU C 2 4   ? -27.919 10.088  -46.315 1.00 27.46 ?  4   LEU C CB  1 
ATOM   4835 C CG  . LEU C 2 4   ? -26.656 10.272  -45.470 1.00 28.01 ?  4   LEU C CG  1 
ATOM   4836 C CD1 . LEU C 2 4   ? -25.552 9.346   -45.959 1.00 22.98 ?  4   LEU C CD1 1 
ATOM   4837 C CD2 . LEU C 2 4   ? -26.189 11.719  -45.490 1.00 29.59 ?  4   LEU C CD2 1 
ATOM   4838 N N   . GLN C 2 5   ? -30.984 11.207  -47.424 1.00 31.79 ?  5   GLN C N   1 
ATOM   4839 C CA  . GLN C 2 5   ? -32.136 10.919  -48.271 1.00 35.00 ?  5   GLN C CA  1 
ATOM   4840 C C   . GLN C 2 5   ? -31.766 11.227  -49.714 1.00 31.90 ?  5   GLN C C   1 
ATOM   4841 O O   . GLN C 2 5   ? -31.525 12.387  -50.065 1.00 34.16 ?  5   GLN C O   1 
ATOM   4842 C CB  . GLN C 2 5   ? -33.358 11.725  -47.834 1.00 32.67 ?  5   GLN C CB  1 
ATOM   4843 C CG  . GLN C 2 5   ? -34.572 11.509  -48.720 1.00 39.00 ?  5   GLN C CG  1 
ATOM   4844 C CD  . GLN C 2 5   ? -35.095 10.088  -48.642 1.00 41.22 ?  5   GLN C CD  1 
ATOM   4845 O OE1 . GLN C 2 5   ? -34.900 9.291   -49.561 1.00 42.57 ?  5   GLN C OE1 1 
ATOM   4846 N NE2 . GLN C 2 5   ? -35.760 9.761   -47.540 1.00 42.72 ?  5   GLN C NE2 1 
ATOM   4847 N N   . GLU C 2 6   ? -31.719 10.192  -50.546 1.00 30.09 ?  6   GLU C N   1 
ATOM   4848 C CA  . GLU C 2 6   ? -31.449 10.356  -51.964 1.00 34.47 ?  6   GLU C CA  1 
ATOM   4849 C C   . GLU C 2 6   ? -32.748 10.313  -52.758 1.00 31.04 ?  6   GLU C C   1 
ATOM   4850 O O   . GLU C 2 6   ? -33.698 9.613   -52.396 1.00 30.56 ?  6   GLU C O   1 
ATOM   4851 C CB  . GLU C 2 6   ? -30.479 9.289   -52.481 1.00 31.55 ?  6   GLU C CB  1 
ATOM   4852 C CG  . GLU C 2 6   ? -30.810 7.871   -52.071 1.00 31.09 ?  6   GLU C CG  1 
ATOM   4853 C CD  . GLU C 2 6   ? -30.268 7.517   -50.702 1.00 31.48 ?  6   GLU C CD  1 
ATOM   4854 O OE1 . GLU C 2 6   ? -29.098 7.086   -50.617 1.00 29.72 ?  6   GLU C OE1 1 
ATOM   4855 O OE2 . GLU C 2 6   ? -31.011 7.675   -49.711 1.00 32.98 -1 6   GLU C OE2 1 
ATOM   4856 N N   . SER C 2 7   ? -32.780 11.080  -53.847 1.00 30.24 ?  7   SER C N   1 
ATOM   4857 C CA  . SER C 2 7   ? -33.977 11.240  -54.659 1.00 30.47 ?  7   SER C CA  1 
ATOM   4858 C C   . SER C 2 7   ? -33.582 11.302  -56.128 1.00 33.09 ?  7   SER C C   1 
ATOM   4859 O O   . SER C 2 7   ? -32.405 11.187  -56.486 1.00 32.61 ?  7   SER C O   1 
ATOM   4860 C CB  . SER C 2 7   ? -34.763 12.491  -54.246 1.00 27.70 ?  7   SER C CB  1 
ATOM   4861 O OG  . SER C 2 7   ? -34.000 13.665  -54.465 1.00 28.03 ?  7   SER C OG  1 
ATOM   4862 N N   . GLY C 2 8   ? -34.582 11.502  -56.982 1.00 33.94 ?  8   GLY C N   1 
ATOM   4863 C CA  . GLY C 2 8   ? -34.382 11.417  -58.411 1.00 31.55 ?  8   GLY C CA  1 
ATOM   4864 C C   . GLY C 2 8   ? -34.269 9.977   -58.868 1.00 34.48 ?  8   GLY C C   1 
ATOM   4865 O O   . GLY C 2 8   ? -34.274 9.029   -58.081 1.00 35.31 ?  8   GLY C O   1 
ATOM   4866 N N   . GLY C 2 9   ? -34.173 9.816   -60.183 1.00 31.44 ?  9   GLY C N   1 
ATOM   4867 C CA  . GLY C 2 9   ? -33.984 8.502   -60.760 1.00 39.79 ?  9   GLY C CA  1 
ATOM   4868 C C   . GLY C 2 9   ? -35.230 7.642   -60.772 1.00 35.95 ?  9   GLY C C   1 
ATOM   4869 O O   . GLY C 2 9   ? -35.990 7.611   -59.799 1.00 38.18 ?  9   GLY C O   1 
ATOM   4870 N N   . GLY C 2 10  ? -35.444 6.936   -61.877 1.00 38.60 ?  10  GLY C N   1 
ATOM   4871 C CA  . GLY C 2 10  ? -36.572 6.038   -62.010 1.00 37.54 ?  10  GLY C CA  1 
ATOM   4872 C C   . GLY C 2 10  ? -36.419 5.114   -63.199 1.00 38.72 ?  10  GLY C C   1 
ATOM   4873 O O   . GLY C 2 10  ? -35.556 4.232   -63.202 1.00 38.51 ?  10  GLY C O   1 
ATOM   4874 N N   . LEU C 2 11  ? -37.246 5.316   -64.221 1.00 34.59 ?  11  LEU C N   1 
ATOM   4875 C CA  . LEU C 2 11  ? -37.216 4.520   -65.441 1.00 32.63 ?  11  LEU C CA  1 
ATOM   4876 C C   . LEU C 2 11  ? -36.694 5.390   -66.577 1.00 36.15 ?  11  LEU C C   1 
ATOM   4877 O O   . LEU C 2 11  ? -37.240 6.467   -66.839 1.00 39.24 ?  11  LEU C O   1 
ATOM   4878 C CB  . LEU C 2 11  ? -38.607 3.972   -65.767 1.00 35.66 ?  11  LEU C CB  1 
ATOM   4879 C CG  . LEU C 2 11  ? -38.758 2.875   -66.828 1.00 35.59 ?  11  LEU C CG  1 
ATOM   4880 C CD1 . LEU C 2 11  ? -38.865 3.457   -68.234 1.00 40.13 ?  11  LEU C CD1 1 
ATOM   4881 C CD2 . LEU C 2 11  ? -37.616 1.872   -66.743 1.00 35.57 ?  11  LEU C CD2 1 
ATOM   4882 N N   . VAL C 2 12  ? -35.643 4.921   -67.247 1.00 37.58 ?  12  VAL C N   1 
ATOM   4883 C CA  . VAL C 2 12  ? -35.033 5.637   -68.360 1.00 37.52 ?  12  VAL C CA  1 
ATOM   4884 C C   . VAL C 2 12  ? -34.656 4.627   -69.436 1.00 35.16 ?  12  VAL C C   1 
ATOM   4885 O O   . VAL C 2 12  ? -34.289 3.486   -69.142 1.00 36.22 ?  12  VAL C O   1 
ATOM   4886 C CB  . VAL C 2 12  ? -33.808 6.464   -67.895 1.00 39.33 ?  12  VAL C CB  1 
ATOM   4887 C CG1 . VAL C 2 12  ? -32.899 6.823   -69.055 1.00 42.43 ?  12  VAL C CG1 1 
ATOM   4888 C CG2 . VAL C 2 12  ? -34.270 7.729   -67.202 1.00 43.38 ?  12  VAL C CG2 1 
ATOM   4889 N N   . GLN C 2 13  ? -34.784 5.044   -70.692 1.00 36.60 ?  13  GLN C N   1 
ATOM   4890 C CA  . GLN C 2 13  ? -34.396 4.205   -71.815 1.00 40.11 ?  13  GLN C CA  1 
ATOM   4891 C C   . GLN C 2 13  ? -32.879 4.172   -71.967 1.00 34.46 ?  13  GLN C C   1 
ATOM   4892 O O   . GLN C 2 13  ? -32.177 5.120   -71.605 1.00 34.50 ?  13  GLN C O   1 
ATOM   4893 C CB  . GLN C 2 13  ? -35.031 4.717   -73.107 1.00 37.65 ?  13  GLN C CB  1 
ATOM   4894 C CG  . GLN C 2 13  ? -36.545 4.672   -73.118 1.00 41.69 ?  13  GLN C CG  1 
ATOM   4895 C CD  . GLN C 2 13  ? -37.087 3.995   -74.357 1.00 48.62 ?  13  GLN C CD  1 
ATOM   4896 O OE1 . GLN C 2 13  ? -37.543 4.655   -75.290 1.00 49.18 ?  13  GLN C OE1 1 
ATOM   4897 N NE2 . GLN C 2 13  ? -37.033 2.668   -74.377 1.00 49.95 ?  13  GLN C NE2 1 
ATOM   4898 N N   . ALA C 2 14  ? -32.381 3.063   -72.513 1.00 32.87 ?  14  ALA C N   1 
ATOM   4899 C CA  . ALA C 2 14  ? -30.958 2.926   -72.802 1.00 29.81 ?  14  ALA C CA  1 
ATOM   4900 C C   . ALA C 2 14  ? -30.475 4.089   -73.655 1.00 28.05 ?  14  ALA C C   1 
ATOM   4901 O O   . ALA C 2 14  ? -31.010 4.344   -74.738 1.00 34.34 ?  14  ALA C O   1 
ATOM   4902 C CB  . ALA C 2 14  ? -30.692 1.596   -73.509 1.00 28.87 ?  14  ALA C CB  1 
ATOM   4903 N N   . GLY C 2 15  ? -29.467 4.800   -73.156 1.00 32.02 ?  15  GLY C N   1 
ATOM   4904 C CA  . GLY C 2 15  ? -28.972 6.008   -73.783 1.00 27.12 ?  15  GLY C CA  1 
ATOM   4905 C C   . GLY C 2 15  ? -29.355 7.287   -73.068 1.00 31.69 ?  15  GLY C C   1 
ATOM   4906 O O   . GLY C 2 15  ? -28.778 8.339   -73.372 1.00 31.01 ?  15  GLY C O   1 
ATOM   4907 N N   . GLY C 2 16  ? -30.291 7.234   -72.119 1.00 31.11 ?  16  GLY C N   1 
ATOM   4908 C CA  . GLY C 2 16  ? -30.808 8.422   -71.474 1.00 34.95 ?  16  GLY C CA  1 
ATOM   4909 C C   . GLY C 2 16  ? -29.996 8.854   -70.265 1.00 35.15 ?  16  GLY C C   1 
ATOM   4910 O O   . GLY C 2 16  ? -28.935 8.310   -69.955 1.00 31.32 ?  16  GLY C O   1 
ATOM   4911 N N   . SER C 2 17  ? -30.528 9.855   -69.564 1.00 35.31 ?  17  SER C N   1 
ATOM   4912 C CA  . SER C 2 17  ? -29.814 10.529  -68.491 1.00 28.83 ?  17  SER C CA  1 
ATOM   4913 C C   . SER C 2 17  ? -30.701 10.663  -67.259 1.00 37.01 ?  17  SER C C   1 
ATOM   4914 O O   . SER C 2 17  ? -31.932 10.632  -67.344 1.00 36.44 ?  17  SER C O   1 
ATOM   4915 C CB  . SER C 2 17  ? -29.332 11.918  -68.937 1.00 29.87 ?  17  SER C CB  1 
ATOM   4916 O OG  . SER C 2 17  ? -28.252 11.818  -69.848 1.00 37.16 ?  17  SER C OG  1 
ATOM   4917 N N   . LEU C 2 18  ? -30.050 10.819  -66.106 1.00 34.53 ?  18  LEU C N   1 
ATOM   4918 C CA  . LEU C 2 18  ? -30.734 11.027  -64.838 1.00 32.86 ?  18  LEU C CA  1 
ATOM   4919 C C   . LEU C 2 18  ? -29.873 11.913  -63.950 1.00 33.60 ?  18  LEU C C   1 
ATOM   4920 O O   . LEU C 2 18  ? -28.660 12.029  -64.145 1.00 32.02 ?  18  LEU C O   1 
ATOM   4921 C CB  . LEU C 2 18  ? -31.031 9.706   -64.119 1.00 31.82 ?  18  LEU C CB  1 
ATOM   4922 C CG  . LEU C 2 18  ? -32.277 8.928   -64.534 1.00 37.47 ?  18  LEU C CG  1 
ATOM   4923 C CD1 . LEU C 2 18  ? -32.237 7.515   -63.967 1.00 35.54 ?  18  LEU C CD1 1 
ATOM   4924 C CD2 . LEU C 2 18  ? -33.543 9.654   -64.103 1.00 34.28 ?  18  LEU C CD2 1 
ATOM   4925 N N   . ASN C 2 19  ? -30.516 12.530  -62.961 1.00 32.06 ?  19  ASN C N   1 
ATOM   4926 C CA  . ASN C 2 19  ? -29.845 13.402  -62.001 1.00 33.61 ?  19  ASN C CA  1 
ATOM   4927 C C   . ASN C 2 19  ? -30.271 12.996  -60.597 1.00 30.86 ?  19  ASN C C   1 
ATOM   4928 O O   . ASN C 2 19  ? -31.406 13.262  -60.188 1.00 31.15 ?  19  ASN C O   1 
ATOM   4929 C CB  . ASN C 2 19  ? -30.171 14.872  -62.263 1.00 35.30 ?  19  ASN C CB  1 
ATOM   4930 C CG  . ASN C 2 19  ? -29.237 15.507  -63.274 1.00 39.47 ?  19  ASN C CG  1 
ATOM   4931 O OD1 . ASN C 2 19  ? -28.502 14.816  -63.979 1.00 41.93 ?  19  ASN C OD1 1 
ATOM   4932 N ND2 . ASN C 2 19  ? -29.257 16.833  -63.346 1.00 43.36 ?  19  ASN C ND2 1 
ATOM   4933 N N   . LEU C 2 20  ? -29.367 12.357  -59.862 1.00 30.90 ?  20  LEU C N   1 
ATOM   4934 C CA  . LEU C 2 20  ? -29.636 11.958  -58.489 1.00 30.00 ?  20  LEU C CA  1 
ATOM   4935 C C   . LEU C 2 20  ? -29.193 13.048  -57.522 1.00 28.70 ?  20  LEU C C   1 
ATOM   4936 O O   . LEU C 2 20  ? -28.245 13.793  -57.783 1.00 27.31 ?  20  LEU C O   1 
ATOM   4937 C CB  . LEU C 2 20  ? -28.923 10.646  -58.154 1.00 29.48 ?  20  LEU C CB  1 
ATOM   4938 C CG  . LEU C 2 20  ? -29.124 9.477   -59.120 1.00 29.08 ?  20  LEU C CG  1 
ATOM   4939 C CD1 . LEU C 2 20  ? -28.509 8.209   -58.553 1.00 25.83 ?  20  LEU C CD1 1 
ATOM   4940 C CD2 . LEU C 2 20  ? -30.600 9.268   -59.424 1.00 28.50 ?  20  LEU C CD2 1 
ATOM   4941 N N   . ALA C 2 21  ? -29.897 13.135  -56.397 1.00 29.48 ?  21  ALA C N   1 
ATOM   4942 C CA  . ALA C 2 21  ? -29.575 14.074  -55.334 1.00 26.81 ?  21  ALA C CA  1 
ATOM   4943 C C   . ALA C 2 21  ? -29.620 13.343  -54.001 1.00 29.55 ?  21  ALA C C   1 
ATOM   4944 O O   . ALA C 2 21  ? -30.326 12.345  -53.857 1.00 27.33 ?  21  ALA C O   1 
ATOM   4945 C CB  . ALA C 2 21  ? -30.543 15.264  -55.316 1.00 24.20 ?  21  ALA C CB  1 
ATOM   4946 N N   . CYS C 2 22  ? -28.856 13.842  -53.031 1.00 31.68 ?  22  CYS C N   1 
ATOM   4947 C CA  . CYS C 2 22  ? -28.798 13.249  -51.697 1.00 28.97 ?  22  CYS C CA  1 
ATOM   4948 C C   . CYS C 2 22  ? -28.700 14.370  -50.674 1.00 30.21 ?  22  CYS C C   1 
ATOM   4949 O O   . CYS C 2 22  ? -27.755 15.161  -50.713 1.00 26.86 ?  22  CYS C O   1 
ATOM   4950 C CB  . CYS C 2 22  ? -27.608 12.291  -51.566 1.00 27.61 ?  22  CYS C CB  1 
ATOM   4951 S SG  . CYS C 2 22  ? -27.217 11.788  -49.868 1.00 30.16 ?  22  CYS C SG  1 
ATOM   4952 N N   . VAL C 2 23  ? -29.664 14.431  -49.756 1.00 28.61 ?  23  VAL C N   1 
ATOM   4953 C CA  . VAL C 2 23  ? -29.776 15.519  -48.790 1.00 31.64 ?  23  VAL C CA  1 
ATOM   4954 C C   . VAL C 2 23  ? -29.391 14.999  -47.411 1.00 30.95 ?  23  VAL C C   1 
ATOM   4955 O O   . VAL C 2 23  ? -29.887 13.953  -46.974 1.00 31.98 ?  23  VAL C O   1 
ATOM   4956 C CB  . VAL C 2 23  ? -31.195 16.113  -48.778 1.00 34.37 ?  23  VAL C CB  1 
ATOM   4957 C CG1 . VAL C 2 23  ? -31.327 17.161  -47.684 1.00 30.85 ?  23  VAL C CG1 1 
ATOM   4958 C CG2 . VAL C 2 23  ? -31.530 16.711  -50.136 1.00 29.48 ?  23  VAL C CG2 1 
ATOM   4959 N N   . SER C 2 24  ? -28.514 15.732  -46.726 1.00 33.97 ?  24  SER C N   1 
ATOM   4960 C CA  . SER C 2 24  ? -28.079 15.374  -45.382 1.00 32.71 ?  24  SER C CA  1 
ATOM   4961 C C   . SER C 2 24  ? -28.953 16.063  -44.342 1.00 33.81 ?  24  SER C C   1 
ATOM   4962 O O   . SER C 2 24  ? -29.380 17.206  -44.531 1.00 34.27 ?  24  SER C O   1 
ATOM   4963 C CB  . SER C 2 24  ? -26.615 15.762  -45.167 1.00 30.15 ?  24  SER C CB  1 
ATOM   4964 O OG  . SER C 2 24  ? -25.744 14.917  -45.898 1.00 40.95 ?  24  SER C OG  1 
ATOM   4965 N N   . SER C 2 25  ? -29.218 15.360  -43.242 1.00 32.13 ?  25  SER C N   1 
ATOM   4966 C CA  . SER C 2 25  ? -30.018 15.912  -42.157 1.00 30.26 ?  25  SER C CA  1 
ATOM   4967 C C   . SER C 2 25  ? -29.540 15.331  -40.835 1.00 32.94 ?  25  SER C C   1 
ATOM   4968 O O   . SER C 2 25  ? -28.931 14.259  -40.787 1.00 29.62 ?  25  SER C O   1 
ATOM   4969 C CB  . SER C 2 25  ? -31.514 15.630  -42.351 1.00 32.45 ?  25  SER C CB  1 
ATOM   4970 O OG  . SER C 2 25  ? -31.875 15.662  -43.721 1.00 45.76 ?  25  SER C OG  1 
ATOM   4971 N N   . GLY C 2 26  ? -29.827 16.054  -39.760 1.00 32.25 ?  26  GLY C N   1 
ATOM   4972 C CA  . GLY C 2 26  ? -29.486 15.616  -38.423 1.00 30.59 ?  26  GLY C CA  1 
ATOM   4973 C C   . GLY C 2 26  ? -28.202 16.230  -37.902 1.00 30.73 ?  26  GLY C C   1 
ATOM   4974 O O   . GLY C 2 26  ? -27.730 17.269  -38.368 1.00 29.80 ?  26  GLY C O   1 
ATOM   4975 N N   . ARG C 2 27  ? -27.632 15.561  -36.901 1.00 29.82 ?  27  ARG C N   1 
ATOM   4976 C CA  . ARG C 2 27  ? -26.373 15.998  -36.297 1.00 29.28 ?  27  ARG C CA  1 
ATOM   4977 C C   . ARG C 2 27  ? -25.238 15.567  -37.218 1.00 30.16 ?  27  ARG C C   1 
ATOM   4978 O O   . ARG C 2 27  ? -24.626 14.511  -37.050 1.00 30.16 ?  27  ARG C O   1 
ATOM   4979 C CB  . ARG C 2 27  ? -26.222 15.434  -34.888 1.00 31.28 ?  27  ARG C CB  1 
ATOM   4980 C CG  . ARG C 2 27  ? -27.149 16.095  -33.868 1.00 29.97 ?  27  ARG C CG  1 
ATOM   4981 C CD  . ARG C 2 27  ? -26.665 15.878  -32.440 1.00 29.17 ?  27  ARG C CD  1 
ATOM   4982 N NE  . ARG C 2 27  ? -27.564 16.451  -31.443 1.00 27.27 ?  27  ARG C NE  1 
ATOM   4983 C CZ  . ARG C 2 27  ? -28.708 15.903  -31.054 1.00 29.37 ?  27  ARG C CZ  1 
ATOM   4984 N NH1 . ARG C 2 27  ? -29.147 14.770  -31.579 1.00 31.48 ?  27  ARG C NH1 1 
ATOM   4985 N NH2 . ARG C 2 27  ? -29.429 16.506  -30.114 1.00 27.17 ?  27  ARG C NH2 1 
ATOM   4986 N N   . THR C 2 28  ? -24.964 16.409  -38.209 1.00 30.04 ?  28  THR C N   1 
ATOM   4987 C CA  . THR C 2 28  ? -23.998 16.164  -39.269 1.00 26.56 ?  28  THR C CA  1 
ATOM   4988 C C   . THR C 2 28  ? -22.780 17.060  -39.060 1.00 25.95 ?  28  THR C C   1 
ATOM   4989 O O   . THR C 2 28  ? -22.813 18.020  -38.285 1.00 27.05 ?  28  THR C O   1 
ATOM   4990 C CB  . THR C 2 28  ? -24.654 16.422  -40.637 1.00 28.33 ?  28  THR C CB  1 
ATOM   4991 O OG1 . THR C 2 28  ? -25.849 15.641  -40.744 1.00 34.23 ?  28  THR C OG1 1 
ATOM   4992 C CG2 . THR C 2 28  ? -23.735 16.045  -41.795 1.00 32.86 ?  28  THR C CG2 1 
ATOM   4993 N N   . PHE C 2 29  ? -21.681 16.720  -39.737 1.00 21.97 ?  29  PHE C N   1 
ATOM   4994 C CA  . PHE C 2 29  ? -20.504 17.576  -39.778 1.00 22.79 ?  29  PHE C CA  1 
ATOM   4995 C C   . PHE C 2 29  ? -20.022 17.693  -41.218 1.00 22.40 ?  29  PHE C C   1 
ATOM   4996 O O   . PHE C 2 29  ? -19.938 16.695  -41.939 1.00 21.83 ?  29  PHE C O   1 
ATOM   4997 C CB  . PHE C 2 29  ? -19.387 17.046  -38.872 1.00 23.21 ?  29  PHE C CB  1 
ATOM   4998 C CG  . PHE C 2 29  ? -18.496 18.124  -38.325 1.00 19.65 ?  29  PHE C CG  1 
ATOM   4999 C CD1 . PHE C 2 29  ? -18.885 18.869  -37.224 1.00 18.82 ?  29  PHE C CD1 1 
ATOM   5000 C CD2 . PHE C 2 29  ? -17.273 18.395  -38.912 1.00 20.26 ?  29  PHE C CD2 1 
ATOM   5001 C CE1 . PHE C 2 29  ? -18.068 19.866  -36.718 1.00 21.71 ?  29  PHE C CE1 1 
ATOM   5002 C CE2 . PHE C 2 29  ? -16.451 19.389  -38.412 1.00 21.34 ?  29  PHE C CE2 1 
ATOM   5003 C CZ  . PHE C 2 29  ? -16.849 20.125  -37.314 1.00 19.03 ?  29  PHE C CZ  1 
ATOM   5004 N N   . SER C 2 30  ? -19.689 18.921  -41.621 1.00 25.14 ?  30  SER C N   1 
ATOM   5005 C CA  . SER C 2 30  ? -19.530 19.255  -43.033 1.00 25.07 ?  30  SER C CA  1 
ATOM   5006 C C   . SER C 2 30  ? -18.270 18.681  -43.671 1.00 27.68 ?  30  SER C C   1 
ATOM   5007 O O   . SER C 2 30  ? -18.175 18.686  -44.902 1.00 25.22 ?  30  SER C O   1 
ATOM   5008 C CB  . SER C 2 30  ? -19.540 20.776  -43.210 1.00 23.51 ?  30  SER C CB  1 
ATOM   5009 O OG  . SER C 2 30  ? -18.465 21.380  -42.511 1.00 28.13 ?  30  SER C OG  1 
ATOM   5010 N N   . THR C 2 31  ? -17.310 18.192  -42.891 1.00 22.99 ?  31  THR C N   1 
ATOM   5011 C CA  . THR C 2 31  ? -16.048 17.722  -43.452 1.00 21.72 ?  31  THR C CA  1 
ATOM   5012 C C   . THR C 2 31  ? -16.071 16.252  -43.848 1.00 22.51 ?  31  THR C C   1 
ATOM   5013 O O   . THR C 2 31  ? -15.055 15.745  -44.337 1.00 26.11 ?  31  THR C O   1 
ATOM   5014 C CB  . THR C 2 31  ? -14.904 17.952  -42.459 1.00 21.13 ?  31  THR C CB  1 
ATOM   5015 O OG1 . THR C 2 31  ? -15.326 17.564  -41.146 1.00 20.45 ?  31  THR C OG1 1 
ATOM   5016 C CG2 . THR C 2 31  ? -14.495 19.416  -42.444 1.00 20.26 ?  31  THR C CG2 1 
ATOM   5017 N N   . TRP C 2 32  ? -17.191 15.560  -43.660 1.00 20.13 ?  32  TRP C N   1 
ATOM   5018 C CA  . TRP C 2 32  ? -17.237 14.122  -43.897 1.00 22.68 ?  32  TRP C CA  1 
ATOM   5019 C C   . TRP C 2 32  ? -17.074 13.804  -45.379 1.00 22.47 ?  32  TRP C C   1 
ATOM   5020 O O   . TRP C 2 32  ? -17.734 14.405  -46.232 1.00 24.43 ?  32  TRP C O   1 
ATOM   5021 C CB  . TRP C 2 32  ? -18.554 13.543  -43.384 1.00 19.33 ?  32  TRP C CB  1 
ATOM   5022 C CG  . TRP C 2 32  ? -18.675 13.543  -41.895 1.00 23.03 ?  32  TRP C CG  1 
ATOM   5023 C CD1 . TRP C 2 32  ? -17.670 13.728  -40.990 1.00 19.56 ?  32  TRP C CD1 1 
ATOM   5024 C CD2 . TRP C 2 32  ? -19.870 13.340  -41.133 1.00 20.66 ?  32  TRP C CD2 1 
ATOM   5025 N NE1 . TRP C 2 32  ? -18.167 13.655  -39.711 1.00 20.62 ?  32  TRP C NE1 1 
ATOM   5026 C CE2 . TRP C 2 32  ? -19.515 13.418  -39.771 1.00 20.82 ?  32  TRP C CE2 1 
ATOM   5027 C CE3 . TRP C 2 32  ? -21.206 13.102  -41.469 1.00 20.15 ?  32  TRP C CE3 1 
ATOM   5028 C CZ2 . TRP C 2 32  ? -20.447 13.266  -38.747 1.00 22.65 ?  32  TRP C CZ2 1 
ATOM   5029 C CZ3 . TRP C 2 32  ? -22.130 12.951  -40.451 1.00 23.37 ?  32  TRP C CZ3 1 
ATOM   5030 C CH2 . TRP C 2 32  ? -21.747 13.033  -39.107 1.00 23.43 ?  32  TRP C CH2 1 
ATOM   5031 N N   . LEU C 2 33  ? -16.194 12.851  -45.680 1.00 20.82 ?  33  LEU C N   1 
ATOM   5032 C CA  . LEU C 2 33  ? -16.083 12.333  -47.036 1.00 22.21 ?  33  LEU C CA  1 
ATOM   5033 C C   . LEU C 2 33  ? -17.358 11.587  -47.410 1.00 22.47 ?  33  LEU C C   1 
ATOM   5034 O O   . LEU C 2 33  ? -17.929 10.855  -46.598 1.00 24.14 ?  33  LEU C O   1 
ATOM   5035 C CB  . LEU C 2 33  ? -14.872 11.408  -47.154 1.00 19.68 ?  33  LEU C CB  1 
ATOM   5036 C CG  . LEU C 2 33  ? -14.693 10.642  -48.468 1.00 27.29 ?  33  LEU C CG  1 
ATOM   5037 C CD1 . LEU C 2 33  ? -14.284 11.585  -49.589 1.00 24.23 ?  33  LEU C CD1 1 
ATOM   5038 C CD2 . LEU C 2 33  ? -13.672 9.527   -48.301 1.00 21.28 ?  33  LEU C CD2 1 
ATOM   5039 N N   . MET C 2 34  ? -17.812 11.784  -48.647 1.00 20.51 ?  34  MET C N   1 
ATOM   5040 C CA  . MET C 2 34  ? -19.079 11.229  -49.096 1.00 22.69 ?  34  MET C CA  1 
ATOM   5041 C C   . MET C 2 34  ? -18.901 10.593  -50.467 1.00 23.20 ?  34  MET C C   1 
ATOM   5042 O O   . MET C 2 34  ? -17.951 10.892  -51.195 1.00 23.79 ?  34  MET C O   1 
ATOM   5043 C CB  . MET C 2 34  ? -20.173 12.302  -49.152 1.00 26.64 ?  34  MET C CB  1 
ATOM   5044 C CG  . MET C 2 34  ? -20.485 12.948  -47.812 1.00 28.49 ?  34  MET C CG  1 
ATOM   5045 S SD  . MET C 2 34  ? -21.717 14.254  -47.965 1.00 25.39 ?  34  MET C SD  1 
ATOM   5046 C CE  . MET C 2 34  ? -23.141 13.307  -48.498 1.00 22.31 ?  34  MET C CE  1 
ATOM   5047 N N   . GLY C 2 35  ? -19.835 9.712   -50.816 1.00 23.49 ?  35  GLY C N   1 
ATOM   5048 C CA  . GLY C 2 35  ? -19.750 9.034   -52.093 1.00 22.31 ?  35  GLY C CA  1 
ATOM   5049 C C   . GLY C 2 35  ? -21.061 8.389   -52.484 1.00 22.84 ?  35  GLY C C   1 
ATOM   5050 O O   . GLY C 2 35  ? -22.041 8.406   -51.737 1.00 22.53 ?  35  GLY C O   1 
ATOM   5051 N N   . TRP C 2 36  ? -21.058 7.813   -53.684 1.00 24.29 ?  36  TRP C N   1 
ATOM   5052 C CA  . TRP C 2 36  ? -22.206 7.113   -54.241 1.00 23.19 ?  36  TRP C CA  1 
ATOM   5053 C C   . TRP C 2 36  ? -21.882 5.634   -54.401 1.00 22.68 ?  36  TRP C C   1 
ATOM   5054 O O   . TRP C 2 36  ? -20.771 5.271   -54.799 1.00 21.71 ?  36  TRP C O   1 
ATOM   5055 C CB  . TRP C 2 36  ? -22.607 7.704   -55.597 1.00 21.81 ?  36  TRP C CB  1 
ATOM   5056 C CG  . TRP C 2 36  ? -23.342 9.004   -55.497 1.00 24.79 ?  36  TRP C CG  1 
ATOM   5057 C CD1 . TRP C 2 36  ? -22.818 10.256  -55.640 1.00 21.78 ?  36  TRP C CD1 1 
ATOM   5058 C CD2 . TRP C 2 36  ? -24.739 9.182   -55.235 1.00 27.50 ?  36  TRP C CD2 1 
ATOM   5059 N NE1 . TRP C 2 36  ? -23.801 11.201  -55.481 1.00 25.58 ?  36  TRP C NE1 1 
ATOM   5060 C CE2 . TRP C 2 36  ? -24.990 10.568  -55.232 1.00 27.61 ?  36  TRP C CE2 1 
ATOM   5061 C CE3 . TRP C 2 36  ? -25.802 8.303   -55.002 1.00 25.07 ?  36  TRP C CE3 1 
ATOM   5062 C CZ2 . TRP C 2 36  ? -26.260 11.096  -55.005 1.00 29.28 ?  36  TRP C CZ2 1 
ATOM   5063 C CZ3 . TRP C 2 36  ? -27.061 8.829   -54.777 1.00 26.96 ?  36  TRP C CZ3 1 
ATOM   5064 C CH2 . TRP C 2 36  ? -27.279 10.212  -54.780 1.00 28.65 ?  36  TRP C CH2 1 
ATOM   5065 N N   . PHE C 2 37  ? -22.857 4.785   -54.085 1.00 24.00 ?  37  PHE C N   1 
ATOM   5066 C CA  . PHE C 2 37  ? -22.737 3.345   -54.255 1.00 25.08 ?  37  PHE C CA  1 
ATOM   5067 C C   . PHE C 2 37  ? -23.988 2.823   -54.947 1.00 23.55 ?  37  PHE C C   1 
ATOM   5068 O O   . PHE C 2 37  ? -25.022 3.495   -54.992 1.00 20.79 ?  37  PHE C O   1 
ATOM   5069 C CB  . PHE C 2 37  ? -22.534 2.628   -52.911 1.00 22.74 ?  37  PHE C CB  1 
ATOM   5070 C CG  . PHE C 2 37  ? -21.173 2.839   -52.308 1.00 23.77 ?  37  PHE C CG  1 
ATOM   5071 C CD1 . PHE C 2 37  ? -20.899 3.973   -51.559 1.00 23.34 ?  37  PHE C CD1 1 
ATOM   5072 C CD2 . PHE C 2 37  ? -20.168 1.905   -52.490 1.00 22.72 ?  37  PHE C CD2 1 
ATOM   5073 C CE1 . PHE C 2 37  ? -19.648 4.169   -51.004 1.00 21.13 ?  37  PHE C CE1 1 
ATOM   5074 C CE2 . PHE C 2 37  ? -18.913 2.097   -51.939 1.00 22.39 ?  37  PHE C CE2 1 
ATOM   5075 C CZ  . PHE C 2 37  ? -18.654 3.230   -51.194 1.00 22.62 ?  37  PHE C CZ  1 
ATOM   5076 N N   . ARG C 2 38  ? -23.888 1.613   -55.492 1.00 24.03 ?  38  ARG C N   1 
ATOM   5077 C CA  . ARG C 2 38  ? -25.022 1.004   -56.169 1.00 27.09 ?  38  ARG C CA  1 
ATOM   5078 C C   . ARG C 2 38  ? -24.996 -0.501  -55.949 1.00 28.60 ?  38  ARG C C   1 
ATOM   5079 O O   . ARG C 2 38  ? -23.929 -1.113  -55.849 1.00 31.01 ?  38  ARG C O   1 
ATOM   5080 C CB  . ARG C 2 38  ? -25.032 1.333   -57.669 1.00 22.54 ?  38  ARG C CB  1 
ATOM   5081 C CG  . ARG C 2 38  ? -23.969 0.618   -58.486 1.00 24.82 ?  38  ARG C CG  1 
ATOM   5082 C CD  . ARG C 2 38  ? -23.985 1.082   -59.933 1.00 24.36 ?  38  ARG C CD  1 
ATOM   5083 N NE  . ARG C 2 38  ? -22.847 0.571   -60.687 1.00 24.63 ?  38  ARG C NE  1 
ATOM   5084 C CZ  . ARG C 2 38  ? -22.626 0.821   -61.970 1.00 33.12 ?  38  ARG C CZ  1 
ATOM   5085 N NH1 . ARG C 2 38  ? -23.450 1.574   -62.679 1.00 33.01 ?  38  ARG C NH1 1 
ATOM   5086 N NH2 . ARG C 2 38  ? -21.551 0.302   -62.557 1.00 34.54 ?  38  ARG C NH2 1 
ATOM   5087 N N   . GLN C 2 39  ? -26.188 -1.089  -55.867 1.00 28.31 ?  39  GLN C N   1 
ATOM   5088 C CA  . GLN C 2 39  ? -26.341 -2.521  -55.645 1.00 32.60 ?  39  GLN C CA  1 
ATOM   5089 C C   . GLN C 2 39  ? -27.543 -3.026  -56.427 1.00 32.83 ?  39  GLN C C   1 
ATOM   5090 O O   . GLN C 2 39  ? -28.632 -2.450  -56.338 1.00 30.05 ?  39  GLN C O   1 
ATOM   5091 C CB  . GLN C 2 39  ? -26.514 -2.840  -54.155 1.00 29.28 ?  39  GLN C CB  1 
ATOM   5092 C CG  . GLN C 2 39  ? -26.511 -4.327  -53.837 1.00 31.83 ?  39  GLN C CG  1 
ATOM   5093 C CD  . GLN C 2 39  ? -26.234 -4.610  -52.373 1.00 36.51 ?  39  GLN C CD  1 
ATOM   5094 O OE1 . GLN C 2 39  ? -26.167 -3.694  -51.553 1.00 37.13 ?  39  GLN C OE1 1 
ATOM   5095 N NE2 . GLN C 2 39  ? -26.069 -5.885  -52.037 1.00 37.37 ?  39  GLN C NE2 1 
ATOM   5096 N N   . ALA C 2 40  ? -27.341 -4.094  -57.190 1.00 32.08 ?  40  ALA C N   1 
ATOM   5097 C CA  . ALA C 2 40  ? -28.397 -4.767  -57.925 1.00 37.33 ?  40  ALA C CA  1 
ATOM   5098 C C   . ALA C 2 40  ? -28.871 -5.997  -57.160 1.00 41.09 ?  40  ALA C C   1 
ATOM   5099 O O   . ALA C 2 40  ? -28.122 -6.554  -56.350 1.00 41.64 ?  40  ALA C O   1 
ATOM   5100 C CB  . ALA C 2 40  ? -27.909 -5.183  -59.316 1.00 34.88 ?  40  ALA C CB  1 
ATOM   5101 N N   . PRO C 2 41  ? -30.115 -6.423  -57.375 1.00 43.42 ?  41  PRO C N   1 
ATOM   5102 C CA  . PRO C 2 41  ? -30.620 -7.616  -56.680 1.00 42.96 ?  41  PRO C CA  1 
ATOM   5103 C C   . PRO C 2 41  ? -29.706 -8.818  -56.872 1.00 40.66 ?  41  PRO C C   1 
ATOM   5104 O O   . PRO C 2 41  ? -29.292 -9.138  -57.989 1.00 38.79 ?  41  PRO C O   1 
ATOM   5105 C CB  . PRO C 2 41  ? -31.993 -7.850  -57.320 1.00 41.53 ?  41  PRO C CB  1 
ATOM   5106 C CG  . PRO C 2 41  ? -32.370 -6.574  -57.984 1.00 42.52 ?  41  PRO C CG  1 
ATOM   5107 C CD  . PRO C 2 41  ? -31.182 -5.667  -58.053 1.00 44.19 ?  41  PRO C CD  1 
ATOM   5108 N N   . GLY C 2 42  ? -29.383 -9.481  -55.764 1.00 39.77 ?  42  GLY C N   1 
ATOM   5109 C CA  . GLY C 2 42  ? -28.561 -10.673 -55.805 1.00 41.55 ?  42  GLY C CA  1 
ATOM   5110 C C   . GLY C 2 42  ? -27.090 -10.445 -56.060 1.00 47.73 ?  42  GLY C C   1 
ATOM   5111 O O   . GLY C 2 42  ? -26.354 -11.419 -56.245 1.00 49.93 ?  42  GLY C O   1 
ATOM   5112 N N   . LYS C 2 43  ? -26.633 -9.199  -56.075 1.00 43.71 ?  43  LYS C N   1 
ATOM   5113 C CA  . LYS C 2 43  ? -25.235 -8.879  -56.327 1.00 41.41 ?  43  LYS C CA  1 
ATOM   5114 C C   . LYS C 2 43  ? -24.659 -8.097  -55.150 1.00 43.00 ?  43  LYS C C   1 
ATOM   5115 O O   . LYS C 2 43  ? -25.343 -7.816  -54.162 1.00 44.46 ?  43  LYS C O   1 
ATOM   5116 C CB  . LYS C 2 43  ? -25.081 -8.101  -57.638 1.00 39.63 ?  43  LYS C CB  1 
ATOM   5117 C CG  . LYS C 2 43  ? -24.701 -8.975  -58.826 1.00 44.08 ?  43  LYS C CG  1 
ATOM   5118 C CD  . LYS C 2 43  ? -24.436 -8.145  -60.072 1.00 43.05 ?  43  LYS C CD  1 
ATOM   5119 C CE  . LYS C 2 43  ? -22.949 -8.088  -60.389 1.00 46.97 ?  43  LYS C CE  1 
ATOM   5120 N NZ  . LYS C 2 43  ? -22.506 -9.258  -61.199 1.00 46.16 ?  43  LYS C NZ  1 
ATOM   5121 N N   . GLU C 2 44  ? -23.382 -7.746  -55.268 1.00 37.70 ?  44  GLU C N   1 
ATOM   5122 C CA  . GLU C 2 44  ? -22.637 -7.078  -54.213 1.00 38.93 ?  44  GLU C CA  1 
ATOM   5123 C C   . GLU C 2 44  ? -22.660 -5.567  -54.418 1.00 38.03 ?  44  GLU C C   1 
ATOM   5124 O O   . GLU C 2 44  ? -22.651 -5.076  -55.550 1.00 33.77 ?  44  GLU C O   1 
ATOM   5125 C CB  . GLU C 2 44  ? -21.192 -7.582  -54.180 1.00 38.45 ?  44  GLU C CB  1 
ATOM   5126 C CG  . GLU C 2 44  ? -20.419 -7.226  -52.921 1.00 45.07 ?  44  GLU C CG  1 
ATOM   5127 C CD  . GLU C 2 44  ? -19.349 -8.252  -52.592 1.00 55.06 ?  44  GLU C CD  1 
ATOM   5128 O OE1 . GLU C 2 44  ? -18.612 -8.661  -53.515 1.00 54.62 ?  44  GLU C OE1 1 
ATOM   5129 O OE2 . GLU C 2 44  ? -19.244 -8.648  -51.412 1.00 58.86 -1 44  GLU C OE2 1 
ATOM   5130 N N   . ARG C 2 45  ? -22.694 -4.833  -53.307 1.00 34.54 ?  45  ARG C N   1 
ATOM   5131 C CA  . ARG C 2 45  ? -22.657 -3.378  -53.372 1.00 31.68 ?  45  ARG C CA  1 
ATOM   5132 C C   . ARG C 2 45  ? -21.284 -2.915  -53.843 1.00 28.88 ?  45  ARG C C   1 
ATOM   5133 O O   . ARG C 2 45  ? -20.255 -3.393  -53.355 1.00 30.10 ?  45  ARG C O   1 
ATOM   5134 C CB  . ARG C 2 45  ? -22.989 -2.774  -52.008 1.00 29.33 ?  45  ARG C CB  1 
ATOM   5135 C CG  . ARG C 2 45  ? -23.401 -1.311  -52.066 1.00 29.51 ?  45  ARG C CG  1 
ATOM   5136 C CD  . ARG C 2 45  ? -23.898 -0.809  -50.719 1.00 28.91 ?  45  ARG C CD  1 
ATOM   5137 N NE  . ARG C 2 45  ? -25.179 -1.399  -50.350 1.00 30.52 ?  45  ARG C NE  1 
ATOM   5138 C CZ  . ARG C 2 45  ? -26.117 -0.776  -49.649 1.00 28.57 ?  45  ARG C CZ  1 
ATOM   5139 N NH1 . ARG C 2 45  ? -25.955 0.468   -49.230 1.00 26.41 ?  45  ARG C NH1 1 
ATOM   5140 N NH2 . ARG C 2 45  ? -27.247 -1.416  -49.364 1.00 28.39 ?  45  ARG C NH2 1 
ATOM   5141 N N   . GLU C 2 46  ? -21.267 -1.980  -54.792 1.00 27.01 ?  46  GLU C N   1 
ATOM   5142 C CA  . GLU C 2 46  ? -20.039 -1.578  -55.461 1.00 27.47 ?  46  GLU C CA  1 
ATOM   5143 C C   . GLU C 2 46  ? -19.901 -0.062  -55.477 1.00 24.35 ?  46  GLU C C   1 
ATOM   5144 O O   . GLU C 2 46  ? -20.890 0.675   -55.437 1.00 23.96 ?  46  GLU C O   1 
ATOM   5145 C CB  . GLU C 2 46  ? -19.990 -2.125  -56.893 1.00 25.66 ?  46  GLU C CB  1 
ATOM   5146 C CG  . GLU C 2 46  ? -21.163 -1.705  -57.758 1.00 31.08 ?  46  GLU C CG  1 
ATOM   5147 C CD  . GLU C 2 46  ? -20.968 -2.073  -59.215 1.00 37.65 ?  46  GLU C CD  1 
ATOM   5148 O OE1 . GLU C 2 46  ? -20.738 -3.268  -59.500 1.00 38.81 ?  46  GLU C OE1 1 
ATOM   5149 O OE2 . GLU C 2 46  ? -21.042 -1.169  -60.074 1.00 33.27 -1 46  GLU C OE2 1 
ATOM   5150 N N   . PHE C 2 47  ? -18.651 0.388   -55.553 1.00 24.99 ?  47  PHE C N   1 
ATOM   5151 C CA  . PHE C 2 47  ? -18.332 1.809   -55.503 1.00 22.82 ?  47  PHE C CA  1 
ATOM   5152 C C   . PHE C 2 47  ? -18.664 2.486   -56.828 1.00 22.53 ?  47  PHE C C   1 
ATOM   5153 O O   . PHE C 2 47  ? -18.496 1.904   -57.901 1.00 23.92 ?  47  PHE C O   1 
ATOM   5154 C CB  . PHE C 2 47  ? -16.851 1.987   -55.163 1.00 21.01 ?  47  PHE C CB  1 
ATOM   5155 C CG  . PHE C 2 47  ? -16.340 3.386   -55.344 1.00 20.84 ?  47  PHE C CG  1 
ATOM   5156 C CD1 . PHE C 2 47  ? -16.607 4.364   -54.401 1.00 21.41 ?  47  PHE C CD1 1 
ATOM   5157 C CD2 . PHE C 2 47  ? -15.574 3.718   -56.449 1.00 23.23 ?  47  PHE C CD2 1 
ATOM   5158 C CE1 . PHE C 2 47  ? -16.129 5.650   -54.564 1.00 21.89 ?  47  PHE C CE1 1 
ATOM   5159 C CE2 . PHE C 2 47  ? -15.094 5.001   -56.618 1.00 21.31 ?  47  PHE C CE2 1 
ATOM   5160 C CZ  . PHE C 2 47  ? -15.371 5.968   -55.673 1.00 22.12 ?  47  PHE C CZ  1 
ATOM   5161 N N   . VAL C 2 48  ? -19.140 3.726   -56.749 1.00 21.89 ?  48  VAL C N   1 
ATOM   5162 C CA  . VAL C 2 48  ? -19.524 4.471   -57.943 1.00 20.70 ?  48  VAL C CA  1 
ATOM   5163 C C   . VAL C 2 48  ? -18.695 5.744   -58.047 1.00 23.39 ?  48  VAL C C   1 
ATOM   5164 O O   . VAL C 2 48  ? -18.020 5.976   -59.056 1.00 24.52 ?  48  VAL C O   1 
ATOM   5165 C CB  . VAL C 2 48  ? -21.029 4.798   -57.946 1.00 21.78 ?  48  VAL C CB  1 
ATOM   5166 C CG1 . VAL C 2 48  ? -21.389 5.619   -59.172 1.00 20.86 ?  48  VAL C CG1 1 
ATOM   5167 C CG2 . VAL C 2 48  ? -21.845 3.518   -57.904 1.00 21.71 ?  48  VAL C CG2 1 
ATOM   5168 N N   . ALA C 2 49  ? -18.741 6.574   -57.008 1.00 20.79 ?  49  ALA C N   1 
ATOM   5169 C CA  . ALA C 2 49  ? -18.030 7.844   -57.029 1.00 21.39 ?  49  ALA C CA  1 
ATOM   5170 C C   . ALA C 2 49  ? -17.870 8.360   -55.606 1.00 20.75 ?  49  ALA C C   1 
ATOM   5171 O O   . ALA C 2 49  ? -18.602 7.964   -54.696 1.00 19.65 ?  49  ALA C O   1 
ATOM   5172 C CB  . ALA C 2 49  ? -18.756 8.878   -57.894 1.00 19.84 ?  49  ALA C CB  1 
ATOM   5173 N N   . SER C 2 50  ? -16.897 9.255   -55.429 1.00 20.42 ?  50  SER C N   1 
ATOM   5174 C CA  . SER C 2 50  ? -16.656 9.913   -54.152 1.00 23.15 ?  50  SER C CA  1 
ATOM   5175 C C   . SER C 2 50  ? -16.155 11.329  -54.403 1.00 22.48 ?  50  SER C C   1 
ATOM   5176 O O   . SER C 2 50  ? -15.579 11.630  -55.452 1.00 21.07 ?  50  SER C O   1 
ATOM   5177 C CB  . SER C 2 50  ? -15.642 9.146   -53.290 1.00 19.55 ?  50  SER C CB  1 
ATOM   5178 O OG  . SER C 2 50  ? -14.331 9.256   -53.816 1.00 19.50 ?  50  SER C OG  1 
ATOM   5179 N N   . ILE C 2 51  ? -16.379 12.200  -53.421 1.00 21.88 ?  51  ILE C N   1 
ATOM   5180 C CA  . ILE C 2 51  ? -15.914 13.581  -53.494 1.00 22.92 ?  51  ILE C CA  1 
ATOM   5181 C C   . ILE C 2 51  ? -15.782 14.113  -52.073 1.00 23.45 ?  51  ILE C C   1 
ATOM   5182 O O   . ILE C 2 51  ? -16.577 13.776  -51.191 1.00 24.41 ?  51  ILE C O   1 
ATOM   5183 C CB  . ILE C 2 51  ? -16.859 14.454  -54.355 1.00 25.55 ?  51  ILE C CB  1 
ATOM   5184 C CG1 . ILE C 2 51  ? -16.251 15.840  -54.587 1.00 25.46 ?  51  ILE C CG1 1 
ATOM   5185 C CG2 . ILE C 2 51  ? -18.235 14.570  -53.713 1.00 26.33 ?  51  ILE C CG2 1 
ATOM   5186 C CD1 . ILE C 2 51  ? -17.128 16.767  -55.401 1.00 29.36 ?  51  ILE C CD1 1 
ATOM   5187 N N   . ASP C 2 52  ? -14.762 14.940  -51.856 1.00 24.27 ?  52  ASP C N   1 
ATOM   5188 C CA  . ASP C 2 52  ? -14.493 15.506  -50.544 1.00 25.45 ?  52  ASP C CA  1 
ATOM   5189 C C   . ASP C 2 52  ? -15.351 16.750  -50.315 1.00 26.70 ?  52  ASP C C   1 
ATOM   5190 O O   . ASP C 2 52  ? -16.083 17.208  -51.197 1.00 28.40 ?  52  ASP C O   1 
ATOM   5191 C CB  . ASP C 2 52  ? -13.007 15.829  -50.404 1.00 25.20 ?  52  ASP C CB  1 
ATOM   5192 C CG  . ASP C 2 52  ? -12.491 16.687  -51.540 1.00 29.46 ?  52  ASP C CG  1 
ATOM   5193 O OD1 . ASP C 2 52  ? -12.643 17.924  -51.469 1.00 31.09 -1 52  ASP C OD1 1 
ATOM   5194 O OD2 . ASP C 2 52  ? -11.938 16.125  -52.507 1.00 30.31 ?  52  ASP C OD2 1 
ATOM   5195 N N   . TRP C 2 53  ? -15.249 17.313  -49.108 1.00 24.68 ?  53  TRP C N   1 
ATOM   5196 C CA  . TRP C 2 53  ? -16.077 18.456  -48.737 1.00 25.17 ?  53  TRP C CA  1 
ATOM   5197 C C   . TRP C 2 53  ? -15.682 19.736  -49.462 1.00 26.27 ?  53  TRP C C   1 
ATOM   5198 O O   . TRP C 2 53  ? -16.473 20.685  -49.490 1.00 22.66 ?  53  TRP C O   1 
ATOM   5199 C CB  . TRP C 2 53  ? -16.015 18.675  -47.225 1.00 25.04 ?  53  TRP C CB  1 
ATOM   5200 C CG  . TRP C 2 53  ? -14.764 19.356  -46.753 1.00 24.87 ?  53  TRP C CG  1 
ATOM   5201 C CD1 . TRP C 2 53  ? -13.482 18.907  -46.888 1.00 23.78 ?  53  TRP C CD1 1 
ATOM   5202 C CD2 . TRP C 2 53  ? -14.680 20.605  -46.058 1.00 23.18 ?  53  TRP C CD2 1 
ATOM   5203 N NE1 . TRP C 2 53  ? -12.605 19.802  -46.323 1.00 23.14 ?  53  TRP C NE1 1 
ATOM   5204 C CE2 . TRP C 2 53  ? -13.316 20.854  -45.807 1.00 23.98 ?  53  TRP C CE2 1 
ATOM   5205 C CE3 . TRP C 2 53  ? -15.626 21.539  -45.625 1.00 23.60 ?  53  TRP C CE3 1 
ATOM   5206 C CZ2 . TRP C 2 53  ? -12.875 21.997  -45.144 1.00 22.50 ?  53  TRP C CZ2 1 
ATOM   5207 C CZ3 . TRP C 2 53  ? -15.187 22.673  -44.967 1.00 26.97 ?  53  TRP C CZ3 1 
ATOM   5208 C CH2 . TRP C 2 53  ? -13.824 22.893  -44.733 1.00 24.50 ?  53  TRP C CH2 1 
ATOM   5209 N N   . ARG C 2 54  ? -14.485 19.789  -50.044 1.00 26.96 ?  54  ARG C N   1 
ATOM   5210 C CA  . ARG C 2 54  ? -14.024 20.962  -50.773 1.00 26.38 ?  54  ARG C CA  1 
ATOM   5211 C C   . ARG C 2 54  ? -14.102 20.782  -52.283 1.00 25.21 ?  54  ARG C C   1 
ATOM   5212 O O   . ARG C 2 54  ? -13.615 21.643  -53.023 1.00 28.86 ?  54  ARG C O   1 
ATOM   5213 C CB  . ARG C 2 54  ? -12.590 21.308  -50.367 1.00 27.98 ?  54  ARG C CB  1 
ATOM   5214 C CG  . ARG C 2 54  ? -12.483 22.147  -49.106 1.00 26.90 ?  54  ARG C CG  1 
ATOM   5215 C CD  . ARG C 2 54  ? -11.159 21.912  -48.396 1.00 30.64 ?  54  ARG C CD  1 
ATOM   5216 N NE  . ARG C 2 54  ? -10.040 22.535  -49.094 1.00 34.27 ?  54  ARG C NE  1 
ATOM   5217 C CZ  . ARG C 2 54  ? -8.797  22.074  -49.076 1.00 36.40 ?  54  ARG C CZ  1 
ATOM   5218 N NH1 . ARG C 2 54  ? -8.476  20.979  -48.406 1.00 39.53 ?  54  ARG C NH1 1 
ATOM   5219 N NH2 . ARG C 2 54  ? -7.853  22.728  -49.746 1.00 36.58 ?  54  ARG C NH2 1 
ATOM   5220 N N   . SER C 2 55  ? -14.698 19.682  -52.751 1.00 26.76 ?  55  SER C N   1 
ATOM   5221 C CA  . SER C 2 55  ? -14.750 19.351  -54.178 1.00 27.57 ?  55  SER C CA  1 
ATOM   5222 C C   . SER C 2 55  ? -13.353 19.317  -54.792 1.00 30.53 ?  55  SER C C   1 
ATOM   5223 O O   . SER C 2 55  ? -13.180 19.537  -55.994 1.00 31.64 ?  55  SER C O   1 
ATOM   5224 C CB  . SER C 2 55  ? -15.655 20.320  -54.944 1.00 24.10 ?  55  SER C CB  1 
ATOM   5225 O OG  . SER C 2 55  ? -16.970 20.316  -54.418 1.00 25.99 ?  55  SER C OG  1 
ATOM   5226 N N   . SER C 2 56  ? -12.346 19.032  -53.963 1.00 30.11 ?  56  SER C N   1 
ATOM   5227 C CA  . SER C 2 56  ? -10.963 19.033  -54.425 1.00 30.19 ?  56  SER C CA  1 
ATOM   5228 C C   . SER C 2 56  ? -10.629 17.775  -55.218 1.00 31.52 ?  56  SER C C   1 
ATOM   5229 O O   . SER C 2 56  ? -9.946  17.851  -56.244 1.00 35.09 ?  56  SER C O   1 
ATOM   5230 C CB  . SER C 2 56  ? -10.014 19.170  -53.233 1.00 31.91 ?  56  SER C CB  1 
ATOM   5231 O OG  . SER C 2 56  ? -10.205 20.400  -52.557 1.00 40.24 ?  56  SER C OG  1 
ATOM   5232 N N   . SER C 2 57  ? -11.099 16.615  -54.762 1.00 29.69 ?  57  SER C N   1 
ATOM   5233 C CA  . SER C 2 57  ? -10.701 15.330  -55.327 1.00 28.53 ?  57  SER C CA  1 
ATOM   5234 C C   . SER C 2 57  ? -11.943 14.514  -55.650 1.00 27.67 ?  57  SER C C   1 
ATOM   5235 O O   . SER C 2 57  ? -12.728 14.192  -54.752 1.00 29.03 ?  57  SER C O   1 
ATOM   5236 C CB  . SER C 2 57  ? -9.795  14.568  -54.356 1.00 26.96 ?  57  SER C CB  1 
ATOM   5237 O OG  . SER C 2 57  ? -8.448  14.988  -54.481 1.00 32.15 ?  57  SER C OG  1 
ATOM   5238 N N   . THR C 2 58  ? -12.113 14.180  -56.926 1.00 24.58 ?  58  THR C N   1 
ATOM   5239 C CA  . THR C 2 58  ? -13.204 13.337  -57.390 1.00 25.63 ?  58  THR C CA  1 
ATOM   5240 C C   . THR C 2 58  ? -12.651 11.978  -57.796 1.00 23.98 ?  58  THR C C   1 
ATOM   5241 O O   . THR C 2 58  ? -11.555 11.886  -58.359 1.00 23.19 ?  58  THR C O   1 
ATOM   5242 C CB  . THR C 2 58  ? -13.943 13.978  -58.571 1.00 25.88 ?  58  THR C CB  1 
ATOM   5243 O OG1 . THR C 2 58  ? -12.996 14.407  -59.557 1.00 28.56 ?  58  THR C OG1 1 
ATOM   5244 C CG2 . THR C 2 58  ? -14.759 15.179  -58.105 1.00 27.75 ?  58  THR C CG2 1 
ATOM   5245 N N   . THR C 2 59  ? -13.407 10.925  -57.498 1.00 22.33 ?  59  THR C N   1 
ATOM   5246 C CA  . THR C 2 59  ? -13.009 9.559   -57.802 1.00 22.47 ?  59  THR C CA  1 
ATOM   5247 C C   . THR C 2 59  ? -14.174 8.842   -58.466 1.00 22.13 ?  59  THR C C   1 
ATOM   5248 O O   . THR C 2 59  ? -15.325 9.004   -58.052 1.00 22.24 ?  59  THR C O   1 
ATOM   5249 C CB  . THR C 2 59  ? -12.580 8.806   -56.535 1.00 21.69 ?  59  THR C CB  1 
ATOM   5250 O OG1 . THR C 2 59  ? -11.722 9.643   -55.750 1.00 22.37 ?  59  THR C OG1 1 
ATOM   5251 C CG2 . THR C 2 59  ? -11.841 7.527   -56.895 1.00 18.88 ?  59  THR C CG2 1 
ATOM   5252 N N   . TYR C 2 60  ? -13.875 8.057   -59.498 1.00 22.03 ?  60  TYR C N   1 
ATOM   5253 C CA  . TYR C 2 60  ? -14.898 7.358   -60.262 1.00 22.30 ?  60  TYR C CA  1 
ATOM   5254 C C   . TYR C 2 60  ? -14.490 5.913   -60.491 1.00 22.68 ?  60  TYR C C   1 
ATOM   5255 O O   . TYR C 2 60  ? -13.318 5.621   -60.746 1.00 22.56 ?  60  TYR C O   1 
ATOM   5256 C CB  . TYR C 2 60  ? -15.145 8.026   -61.619 1.00 21.35 ?  60  TYR C CB  1 
ATOM   5257 C CG  . TYR C 2 60  ? -15.712 9.419   -61.531 1.00 20.59 ?  60  TYR C CG  1 
ATOM   5258 C CD1 . TYR C 2 60  ? -17.057 9.627   -61.256 1.00 22.66 ?  60  TYR C CD1 1 
ATOM   5259 C CD2 . TYR C 2 60  ? -14.904 10.529  -61.729 1.00 23.43 ?  60  TYR C CD2 1 
ATOM   5260 C CE1 . TYR C 2 60  ? -17.580 10.901  -61.177 1.00 22.38 ?  60  TYR C CE1 1 
ATOM   5261 C CE2 . TYR C 2 60  ? -15.417 11.806  -61.652 1.00 27.67 ?  60  TYR C CE2 1 
ATOM   5262 C CZ  . TYR C 2 60  ? -16.755 11.988  -61.376 1.00 25.30 ?  60  TYR C CZ  1 
ATOM   5263 O OH  . TYR C 2 60  ? -17.267 13.261  -61.298 1.00 28.61 ?  60  TYR C OH  1 
ATOM   5264 N N   . ALA C 2 61  ? -15.466 5.013   -60.401 1.00 23.80 ?  61  ALA C N   1 
ATOM   5265 C CA  . ALA C 2 61  ? -15.252 3.649   -60.855 1.00 26.45 ?  61  ALA C CA  1 
ATOM   5266 C C   . ALA C 2 61  ? -14.982 3.643   -62.354 1.00 25.40 ?  61  ALA C C   1 
ATOM   5267 O O   . ALA C 2 61  ? -15.460 4.507   -63.095 1.00 26.19 ?  61  ALA C O   1 
ATOM   5268 C CB  . ALA C 2 61  ? -16.467 2.778   -60.531 1.00 19.69 ?  61  ALA C CB  1 
ATOM   5269 N N   . ASP C 2 62  ? -14.196 2.660   -62.799 1.00 23.68 ?  62  ASP C N   1 
ATOM   5270 C CA  . ASP C 2 62  ? -13.848 2.580   -64.215 1.00 29.87 ?  62  ASP C CA  1 
ATOM   5271 C C   . ASP C 2 62  ? -15.092 2.459   -65.086 1.00 31.28 ?  62  ASP C C   1 
ATOM   5272 O O   . ASP C 2 62  ? -15.133 2.989   -66.202 1.00 29.13 ?  62  ASP C O   1 
ATOM   5273 C CB  . ASP C 2 62  ? -12.911 1.396   -64.458 1.00 34.57 ?  62  ASP C CB  1 
ATOM   5274 C CG  . ASP C 2 62  ? -11.499 1.657   -63.971 1.00 33.56 ?  62  ASP C CG  1 
ATOM   5275 O OD1 . ASP C 2 62  ? -11.302 2.613   -63.192 1.00 35.60 ?  62  ASP C OD1 1 
ATOM   5276 O OD2 . ASP C 2 62  ? -10.587 0.901   -64.366 1.00 33.96 -1 62  ASP C OD2 1 
ATOM   5277 N N   . SER C 2 63  ? -16.123 1.780   -64.585 1.00 31.02 ?  63  SER C N   1 
ATOM   5278 C CA  . SER C 2 63  ? -17.321 1.488   -65.361 1.00 27.24 ?  63  SER C CA  1 
ATOM   5279 C C   . SER C 2 63  ? -18.253 2.684   -65.517 1.00 28.75 ?  63  SER C C   1 
ATOM   5280 O O   . SER C 2 63  ? -19.272 2.562   -66.206 1.00 32.19 ?  63  SER C O   1 
ATOM   5281 C CB  . SER C 2 63  ? -18.082 0.325   -64.720 1.00 26.02 ?  63  SER C CB  1 
ATOM   5282 O OG  . SER C 2 63  ? -18.568 0.681   -63.437 1.00 29.66 ?  63  SER C OG  1 
ATOM   5283 N N   . VAL C 2 64  ? -17.947 3.827   -64.898 1.00 26.29 ?  64  VAL C N   1 
ATOM   5284 C CA  . VAL C 2 64  ? -18.788 5.013   -64.998 1.00 28.73 ?  64  VAL C CA  1 
ATOM   5285 C C   . VAL C 2 64  ? -18.014 6.255   -65.407 1.00 28.33 ?  64  VAL C C   1 
ATOM   5286 O O   . VAL C 2 64  ? -18.621 7.309   -65.603 1.00 28.59 ?  64  VAL C O   1 
ATOM   5287 C CB  . VAL C 2 64  ? -19.550 5.279   -63.681 1.00 25.23 ?  64  VAL C CB  1 
ATOM   5288 C CG1 . VAL C 2 64  ? -20.374 4.065   -63.275 1.00 25.94 ?  64  VAL C CG1 1 
ATOM   5289 C CG2 . VAL C 2 64  ? -18.583 5.680   -62.575 1.00 27.02 ?  64  VAL C CG2 1 
ATOM   5290 N N   . LYS C 2 65  ? -16.692 6.172   -65.542 1.00 28.84 ?  65  LYS C N   1 
ATOM   5291 C CA  . LYS C 2 65  ? -15.900 7.351   -65.866 1.00 32.97 ?  65  LYS C CA  1 
ATOM   5292 C C   . LYS C 2 65  ? -16.238 7.860   -67.262 1.00 30.93 ?  65  LYS C C   1 
ATOM   5293 O O   . LYS C 2 65  ? -16.363 7.084   -68.214 1.00 32.42 ?  65  LYS C O   1 
ATOM   5294 C CB  . LYS C 2 65  ? -14.409 7.036   -65.767 1.00 32.99 ?  65  LYS C CB  1 
ATOM   5295 C CG  . LYS C 2 65  ? -13.516 8.266   -65.818 1.00 37.47 ?  65  LYS C CG  1 
ATOM   5296 C CD  . LYS C 2 65  ? -12.084 7.898   -66.163 1.00 42.09 ?  65  LYS C CD  1 
ATOM   5297 C CE  . LYS C 2 65  ? -11.804 8.106   -67.643 1.00 43.06 ?  65  LYS C CE  1 
ATOM   5298 N NZ  . LYS C 2 65  ? -10.825 9.203   -67.873 1.00 51.22 ?  65  LYS C NZ  1 
ATOM   5299 N N   . GLY C 2 66  ? -16.387 9.178   -67.377 1.00 30.93 ?  66  GLY C N   1 
ATOM   5300 C CA  . GLY C 2 66  ? -16.777 9.796   -68.627 1.00 32.90 ?  66  GLY C CA  1 
ATOM   5301 C C   . GLY C 2 66  ? -18.267 10.057  -68.701 1.00 34.27 ?  66  GLY C C   1 
ATOM   5302 O O   . GLY C 2 66  ? -18.702 11.089  -69.221 1.00 40.54 ?  66  GLY C O   1 
ATOM   5303 N N   . ARG C 2 67  ? -19.061 9.126   -68.172 1.00 34.27 ?  67  ARG C N   1 
ATOM   5304 C CA  . ARG C 2 67  ? -20.514 9.235   -68.217 1.00 31.01 ?  67  ARG C CA  1 
ATOM   5305 C C   . ARG C 2 67  ? -21.086 9.949   -66.999 1.00 31.99 ?  67  ARG C C   1 
ATOM   5306 O O   . ARG C 2 67  ? -22.044 10.719  -67.128 1.00 31.52 ?  67  ARG C O   1 
ATOM   5307 C CB  . ARG C 2 67  ? -21.140 7.842   -68.339 1.00 30.31 ?  67  ARG C CB  1 
ATOM   5308 C CG  . ARG C 2 67  ? -20.510 6.969   -69.412 1.00 29.27 ?  67  ARG C CG  1 
ATOM   5309 C CD  . ARG C 2 67  ? -21.326 5.709   -69.660 1.00 26.20 ?  67  ARG C CD  1 
ATOM   5310 N NE  . ARG C 2 67  ? -21.170 4.728   -68.592 1.00 33.19 ?  67  ARG C NE  1 
ATOM   5311 C CZ  . ARG C 2 67  ? -22.177 4.143   -67.957 1.00 33.03 ?  67  ARG C CZ  1 
ATOM   5312 N NH1 . ARG C 2 67  ? -23.436 4.417   -68.257 1.00 29.57 ?  67  ARG C NH1 1 
ATOM   5313 N NH2 . ARG C 2 67  ? -21.913 3.260   -66.997 1.00 29.62 ?  67  ARG C NH2 1 
ATOM   5314 N N   . PHE C 2 68  ? -20.522 9.710   -65.819 1.00 31.24 ?  68  PHE C N   1 
ATOM   5315 C CA  . PHE C 2 68  ? -21.070 10.222  -64.572 1.00 28.01 ?  68  PHE C CA  1 
ATOM   5316 C C   . PHE C 2 68  ? -20.257 11.416  -64.081 1.00 26.73 ?  68  PHE C C   1 
ATOM   5317 O O   . PHE C 2 68  ? -19.080 11.577  -64.410 1.00 30.71 ?  68  PHE C O   1 
ATOM   5318 C CB  . PHE C 2 68  ? -21.094 9.131   -63.493 1.00 29.31 ?  68  PHE C CB  1 
ATOM   5319 C CG  . PHE C 2 68  ? -22.087 8.020   -63.751 1.00 27.47 ?  68  PHE C CG  1 
ATOM   5320 C CD1 . PHE C 2 68  ? -22.708 7.880   -64.983 1.00 29.16 ?  68  PHE C CD1 1 
ATOM   5321 C CD2 . PHE C 2 68  ? -22.396 7.113   -62.750 1.00 26.74 ?  68  PHE C CD2 1 
ATOM   5322 C CE1 . PHE C 2 68  ? -23.610 6.858   -65.212 1.00 27.02 ?  68  PHE C CE1 1 
ATOM   5323 C CE2 . PHE C 2 68  ? -23.300 6.089   -62.974 1.00 28.43 ?  68  PHE C CE2 1 
ATOM   5324 C CZ  . PHE C 2 68  ? -23.907 5.963   -64.207 1.00 28.95 ?  68  PHE C CZ  1 
ATOM   5325 N N   . THR C 2 69  ? -20.908 12.258  -63.279 1.00 27.23 ?  69  THR C N   1 
ATOM   5326 C CA  . THR C 2 69  ? -20.263 13.423  -62.681 1.00 28.62 ?  69  THR C CA  1 
ATOM   5327 C C   . THR C 2 69  ? -20.777 13.590  -61.261 1.00 28.94 ?  69  THR C C   1 
ATOM   5328 O O   . THR C 2 69  ? -21.981 13.772  -61.054 1.00 31.36 ?  69  THR C O   1 
ATOM   5329 C CB  . THR C 2 69  ? -20.529 14.695  -63.494 1.00 32.22 ?  69  THR C CB  1 
ATOM   5330 O OG1 . THR C 2 69  ? -20.076 14.512  -64.840 1.00 28.64 ?  69  THR C OG1 1 
ATOM   5331 C CG2 . THR C 2 69  ? -19.803 15.883  -62.877 1.00 27.52 ?  69  THR C CG2 1 
ATOM   5332 N N   . ILE C 2 70  ? -19.874 13.533  -60.292 1.00 26.59 ?  70  ILE C N   1 
ATOM   5333 C CA  . ILE C 2 70  ? -20.226 13.745  -58.893 1.00 26.76 ?  70  ILE C CA  1 
ATOM   5334 C C   . ILE C 2 70  ? -19.987 15.208  -58.545 1.00 23.29 ?  70  ILE C C   1 
ATOM   5335 O O   . ILE C 2 70  ? -19.031 15.832  -59.023 1.00 24.06 ?  70  ILE C O   1 
ATOM   5336 C CB  . ILE C 2 70  ? -19.429 12.798  -57.975 1.00 24.33 ?  70  ILE C CB  1 
ATOM   5337 C CG1 . ILE C 2 70  ? -19.978 12.841  -56.548 1.00 22.23 ?  70  ILE C CG1 1 
ATOM   5338 C CG2 . ILE C 2 70  ? -17.943 13.128  -58.007 1.00 22.47 ?  70  ILE C CG2 1 
ATOM   5339 C CD1 . ILE C 2 70  ? -19.461 11.733  -55.659 1.00 21.59 ?  70  ILE C CD1 1 
ATOM   5340 N N   . SER C 2 71  ? -20.874 15.768  -57.724 1.00 22.18 ?  71  SER C N   1 
ATOM   5341 C CA  . SER C 2 71  ? -20.816 17.179  -57.373 1.00 25.23 ?  71  SER C CA  1 
ATOM   5342 C C   . SER C 2 71  ? -21.402 17.370  -55.983 1.00 26.34 ?  71  SER C C   1 
ATOM   5343 O O   . SER C 2 71  ? -22.269 16.606  -55.548 1.00 24.71 ?  71  SER C O   1 
ATOM   5344 C CB  . SER C 2 71  ? -21.559 18.038  -58.404 1.00 26.65 ?  71  SER C CB  1 
ATOM   5345 O OG  . SER C 2 71  ? -22.813 18.470  -57.905 1.00 30.36 ?  71  SER C OG  1 
ATOM   5346 N N   . ARG C 2 72  ? -20.926 18.404  -55.290 1.00 26.68 ?  72  ARG C N   1 
ATOM   5347 C CA  . ARG C 2 72  ? -21.266 18.612  -53.889 1.00 29.66 ?  72  ARG C CA  1 
ATOM   5348 C C   . ARG C 2 72  ? -21.531 20.086  -53.627 1.00 26.78 ?  72  ARG C C   1 
ATOM   5349 O O   . ARG C 2 72  ? -20.760 20.947  -54.060 1.00 26.29 ?  72  ARG C O   1 
ATOM   5350 C CB  . ARG C 2 72  ? -20.142 18.104  -52.977 1.00 26.80 ?  72  ARG C CB  1 
ATOM   5351 C CG  . ARG C 2 72  ? -20.554 17.886  -51.533 1.00 28.13 ?  72  ARG C CG  1 
ATOM   5352 C CD  . ARG C 2 72  ? -19.584 16.950  -50.831 1.00 26.74 ?  72  ARG C CD  1 
ATOM   5353 N NE  . ARG C 2 72  ? -19.735 16.985  -49.381 1.00 27.60 ?  72  ARG C NE  1 
ATOM   5354 C CZ  . ARG C 2 72  ? -18.991 16.285  -48.535 1.00 27.06 ?  72  ARG C CZ  1 
ATOM   5355 N NH1 . ARG C 2 72  ? -18.034 15.477  -48.961 1.00 25.50 ?  72  ARG C NH1 1 
ATOM   5356 N NH2 . ARG C 2 72  ? -19.212 16.400  -47.229 1.00 25.79 ?  72  ARG C NH2 1 
ATOM   5357 N N   . ASP C 2 73  ? -22.621 20.365  -52.911 1.00 29.54 ?  73  ASP C N   1 
ATOM   5358 C CA  . ASP C 2 73  ? -23.025 21.720  -52.535 1.00 31.25 ?  73  ASP C CA  1 
ATOM   5359 C C   . ASP C 2 73  ? -23.250 21.698  -51.025 1.00 34.25 ?  73  ASP C C   1 
ATOM   5360 O O   . ASP C 2 73  ? -24.324 21.307  -50.558 1.00 33.79 ?  73  ASP C O   1 
ATOM   5361 C CB  . ASP C 2 73  ? -24.280 22.147  -53.297 1.00 30.38 ?  73  ASP C CB  1 
ATOM   5362 C CG  . ASP C 2 73  ? -24.775 23.539  -52.915 1.00 35.57 ?  73  ASP C CG  1 
ATOM   5363 O OD1 . ASP C 2 73  ? -24.271 24.141  -51.944 1.00 36.68 ?  73  ASP C OD1 1 
ATOM   5364 O OD2 . ASP C 2 73  ? -25.686 24.039  -53.608 1.00 39.76 -1 73  ASP C OD2 1 
ATOM   5365 N N   . ASN C 2 74  ? -22.240 22.130  -50.266 1.00 33.73 ?  74  ASN C N   1 
ATOM   5366 C CA  . ASN C 2 74  ? -22.297 22.003  -48.812 1.00 35.15 ?  74  ASN C CA  1 
ATOM   5367 C C   . ASN C 2 74  ? -23.337 22.938  -48.204 1.00 37.26 ?  74  ASN C C   1 
ATOM   5368 O O   . ASN C 2 74  ? -23.983 22.590  -47.210 1.00 36.78 ?  74  ASN C O   1 
ATOM   5369 C CB  . ASN C 2 74  ? -20.918 22.272  -48.210 1.00 36.18 ?  74  ASN C CB  1 
ATOM   5370 C CG  . ASN C 2 74  ? -20.151 20.997  -47.919 1.00 37.24 ?  74  ASN C CG  1 
ATOM   5371 O OD1 . ASN C 2 74  ? -20.193 20.475  -46.805 1.00 40.71 ?  74  ASN C OD1 1 
ATOM   5372 N ND2 . ASN C 2 74  ? -19.445 20.489  -48.922 1.00 32.69 ?  74  ASN C ND2 1 
ATOM   5373 N N   . ALA C 2 75  ? -23.510 24.131  -48.780 1.00 36.72 ?  75  ALA C N   1 
ATOM   5374 C CA  . ALA C 2 75  ? -24.466 25.082  -48.221 1.00 35.69 ?  75  ALA C CA  1 
ATOM   5375 C C   . ALA C 2 75  ? -25.896 24.577  -48.344 1.00 37.41 ?  75  ALA C C   1 
ATOM   5376 O O   . ALA C 2 75  ? -26.762 24.964  -47.550 1.00 38.18 ?  75  ALA C O   1 
ATOM   5377 C CB  . ALA C 2 75  ? -24.320 26.443  -48.901 1.00 34.36 ?  75  ALA C CB  1 
ATOM   5378 N N   . LYS C 2 76  ? -26.162 23.721  -49.325 1.00 36.92 ?  76  LYS C N   1 
ATOM   5379 C CA  . LYS C 2 76  ? -27.470 23.107  -49.491 1.00 37.05 ?  76  LYS C CA  1 
ATOM   5380 C C   . LYS C 2 76  ? -27.542 21.707  -48.895 1.00 37.26 ?  76  LYS C C   1 
ATOM   5381 O O   . LYS C 2 76  ? -28.595 21.067  -48.982 1.00 35.74 ?  76  LYS C O   1 
ATOM   5382 C CB  . LYS C 2 76  ? -27.844 23.060  -50.975 1.00 38.81 ?  76  LYS C CB  1 
ATOM   5383 C CG  . LYS C 2 76  ? -28.642 24.263  -51.453 1.00 38.14 ?  76  LYS C CG  1 
ATOM   5384 C CD  . LYS C 2 76  ? -27.734 25.420  -51.837 1.00 40.58 ?  76  LYS C CD  1 
ATOM   5385 C CE  . LYS C 2 76  ? -28.382 26.761  -51.526 1.00 47.73 ?  76  LYS C CE  1 
ATOM   5386 N NZ  . LYS C 2 76  ? -27.367 27.819  -51.260 1.00 42.70 ?  76  LYS C NZ  1 
ATOM   5387 N N   . ASN C 2 77  ? -26.450 21.223  -48.296 1.00 35.91 ?  77  ASN C N   1 
ATOM   5388 C CA  . ASN C 2 77  ? -26.396 19.894  -47.685 1.00 36.09 ?  77  ASN C CA  1 
ATOM   5389 C C   . ASN C 2 77  ? -26.795 18.808  -48.682 1.00 32.54 ?  77  ASN C C   1 
ATOM   5390 O O   . ASN C 2 77  ? -27.487 17.848  -48.338 1.00 32.64 ?  77  ASN C O   1 
ATOM   5391 C CB  . ASN C 2 77  ? -27.272 19.825  -46.430 1.00 36.51 ?  77  ASN C CB  1 
ATOM   5392 C CG  . ASN C 2 77  ? -26.577 20.379  -45.202 1.00 39.64 ?  77  ASN C CG  1 
ATOM   5393 O OD1 . ASN C 2 77  ? -25.589 19.820  -44.727 1.00 39.44 ?  77  ASN C OD1 1 
ATOM   5394 N ND2 . ASN C 2 77  ? -27.093 21.487  -44.681 1.00 35.79 ?  77  ASN C ND2 1 
ATOM   5395 N N   . THR C 2 78  ? -26.352 18.957  -49.929 1.00 32.65 ?  78  THR C N   1 
ATOM   5396 C CA  . THR C 2 78  ? -26.790 18.090  -51.012 1.00 33.02 ?  78  THR C CA  1 
ATOM   5397 C C   . THR C 2 78  ? -25.603 17.631  -51.848 1.00 31.12 ?  78  THR C C   1 
ATOM   5398 O O   . THR C 2 78  ? -24.722 18.426  -52.185 1.00 26.87 ?  78  THR C O   1 
ATOM   5399 C CB  . THR C 2 78  ? -27.812 18.801  -51.912 1.00 31.11 ?  78  THR C CB  1 
ATOM   5400 O OG1 . THR C 2 78  ? -28.893 19.294  -51.110 1.00 33.02 ?  78  THR C OG1 1 
ATOM   5401 C CG2 . THR C 2 78  ? -28.367 17.843  -52.956 1.00 28.21 ?  78  THR C CG2 1 
ATOM   5402 N N   . MET C 2 79  ? -25.592 16.340  -52.173 1.00 28.28 ?  79  MET C N   1 
ATOM   5403 C CA  . MET C 2 79  ? -24.643 15.753  -53.106 1.00 28.30 ?  79  MET C CA  1 
ATOM   5404 C C   . MET C 2 79  ? -25.388 15.302  -54.357 1.00 29.10 ?  79  MET C C   1 
ATOM   5405 O O   . MET C 2 79  ? -26.534 14.848  -54.283 1.00 31.36 ?  79  MET C O   1 
ATOM   5406 C CB  . MET C 2 79  ? -23.907 14.569  -52.468 1.00 28.10 ?  79  MET C CB  1 
ATOM   5407 C CG  . MET C 2 79  ? -22.839 13.936  -53.348 1.00 31.25 ?  79  MET C CG  1 
ATOM   5408 S SD  . MET C 2 79  ? -21.834 12.732  -52.458 1.00 32.03 ?  79  MET C SD  1 
ATOM   5409 C CE  . MET C 2 79  ? -23.076 11.524  -52.007 1.00 25.00 ?  79  MET C CE  1 
ATOM   5410 N N   . TYR C 2 80  ? -24.735 15.434  -55.510 1.00 28.90 ?  80  TYR C N   1 
ATOM   5411 C CA  . TYR C 2 80  ? -25.362 15.157  -56.794 1.00 29.04 ?  80  TYR C CA  1 
ATOM   5412 C C   . TYR C 2 80  ? -24.575 14.110  -57.570 1.00 27.75 ?  80  TYR C C   1 
ATOM   5413 O O   . TYR C 2 80  ? -23.367 13.943  -57.378 1.00 25.78 ?  80  TYR C O   1 
ATOM   5414 C CB  . TYR C 2 80  ? -25.478 16.430  -57.642 1.00 28.31 ?  80  TYR C CB  1 
ATOM   5415 C CG  . TYR C 2 80  ? -26.168 17.584  -56.952 1.00 29.87 ?  80  TYR C CG  1 
ATOM   5416 C CD1 . TYR C 2 80  ? -25.452 18.480  -56.168 1.00 31.08 ?  80  TYR C CD1 1 
ATOM   5417 C CD2 . TYR C 2 80  ? -27.535 17.785  -57.091 1.00 31.96 ?  80  TYR C CD2 1 
ATOM   5418 C CE1 . TYR C 2 80  ? -26.078 19.539  -55.539 1.00 32.68 ?  80  TYR C CE1 1 
ATOM   5419 C CE2 . TYR C 2 80  ? -28.171 18.841  -56.466 1.00 31.64 ?  80  TYR C CE2 1 
ATOM   5420 C CZ  . TYR C 2 80  ? -27.436 19.716  -55.692 1.00 33.79 ?  80  TYR C CZ  1 
ATOM   5421 O OH  . TYR C 2 80  ? -28.064 20.769  -55.067 1.00 36.35 ?  80  TYR C OH  1 
ATOM   5422 N N   . LEU C 2 81  ? -25.277 13.409  -58.460 1.00 28.03 ?  81  LEU C N   1 
ATOM   5423 C CA  . LEU C 2 81  ? -24.659 12.468  -59.396 1.00 30.82 ?  81  LEU C CA  1 
ATOM   5424 C C   . LEU C 2 81  ? -25.392 12.596  -60.728 1.00 30.83 ?  81  LEU C C   1 
ATOM   5425 O O   . LEU C 2 81  ? -26.501 12.075  -60.884 1.00 26.38 ?  81  LEU C O   1 
ATOM   5426 C CB  . LEU C 2 81  ? -24.704 11.036  -58.877 1.00 29.90 ?  81  LEU C CB  1 
ATOM   5427 C CG  . LEU C 2 81  ? -23.954 10.026  -59.751 1.00 29.02 ?  81  LEU C CG  1 
ATOM   5428 C CD1 . LEU C 2 81  ? -22.453 10.140  -59.536 1.00 25.14 ?  81  LEU C CD1 1 
ATOM   5429 C CD2 . LEU C 2 81  ? -24.434 8.606   -59.489 1.00 28.23 ?  81  LEU C CD2 1 
ATOM   5430 N N   . GLN C 2 82  ? -24.774 13.291  -61.679 1.00 36.96 ?  82  GLN C N   1 
ATOM   5431 C CA  . GLN C 2 82  ? -25.327 13.442  -63.018 1.00 30.74 ?  82  GLN C CA  1 
ATOM   5432 C C   . GLN C 2 82  ? -24.898 12.252  -63.868 1.00 30.80 ?  82  GLN C C   1 
ATOM   5433 O O   . GLN C 2 82  ? -23.700 12.045  -64.092 1.00 28.40 ?  82  GLN C O   1 
ATOM   5434 C CB  . GLN C 2 82  ? -24.863 14.752  -63.653 1.00 33.75 ?  82  GLN C CB  1 
ATOM   5435 C CG  . GLN C 2 82  ? -25.174 15.991  -62.830 1.00 34.24 ?  82  GLN C CG  1 
ATOM   5436 C CD  . GLN C 2 82  ? -23.931 16.792  -62.494 1.00 43.64 ?  82  GLN C CD  1 
ATOM   5437 O OE1 . GLN C 2 82  ? -23.332 17.424  -63.364 1.00 45.32 ?  82  GLN C OE1 1 
ATOM   5438 N NE2 . GLN C 2 82  ? -23.537 16.770  -61.225 1.00 40.34 ?  82  GLN C NE2 1 
ATOM   5439 N N   . MET C 2 83  ? -25.869 11.475  -64.335 1.00 32.19 ?  83  MET C N   1 
ATOM   5440 C CA  . MET C 2 83  ? -25.611 10.275  -65.116 1.00 29.87 ?  83  MET C CA  1 
ATOM   5441 C C   . MET C 2 83  ? -26.021 10.494  -66.566 1.00 32.75 ?  83  MET C C   1 
ATOM   5442 O O   . MET C 2 83  ? -27.073 11.080  -66.841 1.00 32.78 ?  83  MET C O   1 
ATOM   5443 C CB  . MET C 2 83  ? -26.364 9.072   -64.539 1.00 33.01 ?  83  MET C CB  1 
ATOM   5444 C CG  . MET C 2 83  ? -26.127 8.846   -63.054 1.00 31.43 ?  83  MET C CG  1 
ATOM   5445 S SD  . MET C 2 83  ? -26.844 7.305   -62.448 1.00 32.30 ?  83  MET C SD  1 
ATOM   5446 C CE  . MET C 2 83  ? -28.571 7.758   -62.319 1.00 29.24 ?  83  MET C CE  1 
ATOM   5447 N N   . THR C 2 84  ? -25.181 10.030  -67.490 1.00 33.00 ?  84  THR C N   1 
ATOM   5448 C CA  . THR C 2 84  ? -25.466 10.068  -68.918 1.00 30.16 ?  84  THR C CA  1 
ATOM   5449 C C   . THR C 2 84  ? -25.101 8.725   -69.537 1.00 32.79 ?  84  THR C C   1 
ATOM   5450 O O   . THR C 2 84  ? -24.400 7.907   -68.934 1.00 31.62 ?  84  THR C O   1 
ATOM   5451 C CB  . THR C 2 84  ? -24.699 11.194  -69.630 1.00 31.38 ?  84  THR C CB  1 
ATOM   5452 O OG1 . THR C 2 84  ? -23.289 10.981  -69.491 1.00 28.09 ?  84  THR C OG1 1 
ATOM   5453 C CG2 . THR C 2 84  ? -25.068 12.558  -69.058 1.00 31.84 ?  84  THR C CG2 1 
ATOM   5454 N N   . GLY C 2 85  ? -25.582 8.509   -70.758 1.00 31.28 ?  85  GLY C N   1 
ATOM   5455 C CA  . GLY C 2 85  ? -25.277 7.288   -71.492 1.00 28.27 ?  85  GLY C CA  1 
ATOM   5456 C C   . GLY C 2 85  ? -25.654 6.019   -70.760 1.00 32.36 ?  85  GLY C C   1 
ATOM   5457 O O   . GLY C 2 85  ? -24.905 5.035   -70.801 1.00 33.85 ?  85  GLY C O   1 
ATOM   5458 N N   . LEU C 2 86  ? -26.807 6.018   -70.097 1.00 33.39 ?  86  LEU C N   1 
ATOM   5459 C CA  . LEU C 2 86  ? -27.174 4.910   -69.226 1.00 31.71 ?  86  LEU C CA  1 
ATOM   5460 C C   . LEU C 2 86  ? -27.436 3.641   -70.027 1.00 32.98 ?  86  LEU C C   1 
ATOM   5461 O O   . LEU C 2 86  ? -28.220 3.640   -70.980 1.00 34.53 ?  86  LEU C O   1 
ATOM   5462 C CB  . LEU C 2 86  ? -28.404 5.275   -68.399 1.00 29.97 ?  86  LEU C CB  1 
ATOM   5463 C CG  . LEU C 2 86  ? -28.132 6.211   -67.221 1.00 33.05 ?  86  LEU C CG  1 
ATOM   5464 C CD1 . LEU C 2 86  ? -29.428 6.791   -66.677 1.00 31.14 ?  86  LEU C CD1 1 
ATOM   5465 C CD2 . LEU C 2 86  ? -27.362 5.482   -66.129 1.00 29.21 ?  86  LEU C CD2 1 
ATOM   5466 N N   . LYS C 2 87  ? -26.776 2.568   -69.635 1.00 29.28 ?  87  LYS C N   1 
ATOM   5467 C CA  . LYS C 2 87  ? -26.996 1.236   -70.163 1.00 30.73 ?  87  LYS C CA  1 
ATOM   5468 C C   . LYS C 2 87  ? -27.804 0.412   -69.176 1.00 31.54 ?  87  LYS C C   1 
ATOM   5469 O O   . LYS C 2 87  ? -27.851 0.728   -67.983 1.00 32.36 ?  87  LYS C O   1 
ATOM   5470 C CB  . LYS C 2 87  ? -25.656 0.545   -70.439 1.00 30.57 ?  87  LYS C CB  1 
ATOM   5471 C CG  . LYS C 2 87  ? -24.725 1.285   -71.397 1.00 33.00 ?  87  LYS C CG  1 
ATOM   5472 C CD  . LYS C 2 87  ? -25.178 1.169   -72.851 1.00 37.70 ?  87  LYS C CD  1 
ATOM   5473 C CE  . LYS C 2 87  ? -26.023 2.358   -73.292 1.00 37.35 ?  87  LYS C CE  1 
ATOM   5474 N NZ  . LYS C 2 87  ? -26.344 2.303   -74.745 1.00 39.59 ?  87  LYS C NZ  1 
ATOM   5475 N N   . PRO C 2 88  ? -28.473 -0.649  -69.637 1.00 31.80 ?  88  PRO C N   1 
ATOM   5476 C CA  . PRO C 2 88  ? -29.144 -1.552  -68.687 1.00 33.93 ?  88  PRO C CA  1 
ATOM   5477 C C   . PRO C 2 88  ? -28.220 -2.096  -67.606 1.00 31.00 ?  88  PRO C C   1 
ATOM   5478 O O   . PRO C 2 88  ? -28.713 -2.518  -66.552 1.00 27.62 ?  88  PRO C O   1 
ATOM   5479 C CB  . PRO C 2 88  ? -29.673 -2.671  -69.592 1.00 28.68 ?  88  PRO C CB  1 
ATOM   5480 C CG  . PRO C 2 88  ? -29.921 -1.995  -70.890 1.00 29.91 ?  88  PRO C CG  1 
ATOM   5481 C CD  . PRO C 2 88  ? -28.801 -0.987  -71.035 1.00 29.78 ?  88  PRO C CD  1 
ATOM   5482 N N   . GLU C 2 89  ? -26.902 -2.096  -67.832 1.00 32.05 ?  89  GLU C N   1 
ATOM   5483 C CA  . GLU C 2 89  ? -25.953 -2.509  -66.800 1.00 34.33 ?  89  GLU C CA  1 
ATOM   5484 C C   . GLU C 2 89  ? -26.072 -1.656  -65.545 1.00 34.32 ?  89  GLU C C   1 
ATOM   5485 O O   . GLU C 2 89  ? -25.777 -2.130  -64.442 1.00 32.61 ?  89  GLU C O   1 
ATOM   5486 C CB  . GLU C 2 89  ? -24.528 -2.421  -67.343 1.00 36.85 ?  89  GLU C CB  1 
ATOM   5487 C CG  . GLU C 2 89  ? -24.015 -3.702  -67.948 1.00 37.61 ?  89  GLU C CG  1 
ATOM   5488 C CD  . GLU C 2 89  ? -22.574 -3.979  -67.591 1.00 38.02 ?  89  GLU C CD  1 
ATOM   5489 O OE1 . GLU C 2 89  ? -21.684 -3.346  -68.196 1.00 38.72 ?  89  GLU C OE1 1 
ATOM   5490 O OE2 . GLU C 2 89  ? -22.335 -4.832  -66.712 1.00 46.52 -1 89  GLU C OE2 1 
ATOM   5491 N N   . ASP C 2 90  ? -26.488 -0.400  -65.692 1.00 30.29 ?  90  ASP C N   1 
ATOM   5492 C CA  . ASP C 2 90  ? -26.533 0.536   -64.578 1.00 30.93 ?  90  ASP C CA  1 
ATOM   5493 C C   . ASP C 2 90  ? -27.788 0.396   -63.726 1.00 30.60 ?  90  ASP C C   1 
ATOM   5494 O O   . ASP C 2 90  ? -27.981 1.197   -62.804 1.00 33.58 ?  90  ASP C O   1 
ATOM   5495 C CB  . ASP C 2 90  ? -26.416 1.968   -65.105 1.00 29.78 ?  90  ASP C CB  1 
ATOM   5496 C CG  . ASP C 2 90  ? -25.213 2.158   -66.010 1.00 32.08 ?  90  ASP C CG  1 
ATOM   5497 O OD1 . ASP C 2 90  ? -24.089 1.806   -65.593 1.00 32.80 ?  90  ASP C OD1 1 
ATOM   5498 O OD2 . ASP C 2 90  ? -25.392 2.653   -67.143 1.00 31.47 -1 90  ASP C OD2 1 
ATOM   5499 N N   . THR C 2 91  ? -28.638 -0.590  -64.004 1.00 26.42 ?  91  THR C N   1 
ATOM   5500 C CA  . THR C 2 91  ? -29.834 -0.809  -63.200 1.00 30.92 ?  91  THR C CA  1 
ATOM   5501 C C   . THR C 2 91  ? -29.441 -1.289  -61.809 1.00 31.12 ?  91  THR C C   1 
ATOM   5502 O O   . THR C 2 91  ? -28.809 -2.342  -61.666 1.00 31.25 ?  91  THR C O   1 
ATOM   5503 C CB  . THR C 2 91  ? -30.747 -1.830  -63.874 1.00 30.40 ?  91  THR C CB  1 
ATOM   5504 O OG1 . THR C 2 91  ? -31.145 -1.344  -65.162 1.00 31.67 ?  91  THR C OG1 1 
ATOM   5505 C CG2 . THR C 2 91  ? -31.983 -2.078  -63.024 1.00 31.09 ?  91  THR C CG2 1 
ATOM   5506 N N   . ALA C 2 92  ? -29.822 -0.525  -60.787 1.00 28.57 ?  92  ALA C N   1 
ATOM   5507 C CA  . ALA C 2 92  ? -29.493 -0.840  -59.401 1.00 29.49 ?  92  ALA C CA  1 
ATOM   5508 C C   . ALA C 2 92  ? -30.177 0.178   -58.497 1.00 29.79 ?  92  ALA C C   1 
ATOM   5509 O O   . ALA C 2 92  ? -30.737 1.176   -58.961 1.00 26.17 ?  92  ALA C O   1 
ATOM   5510 C CB  . ALA C 2 92  ? -27.983 -0.830  -59.150 1.00 26.84 ?  92  ALA C CB  1 
ATOM   5511 N N   . VAL C 2 93  ? -30.133 -0.099  -57.198 1.00 28.73 ?  93  VAL C N   1 
ATOM   5512 C CA  . VAL C 2 93  ? -30.439 0.907   -56.187 1.00 29.34 ?  93  VAL C CA  1 
ATOM   5513 C C   . VAL C 2 93  ? -29.183 1.731   -55.946 1.00 26.95 ?  93  VAL C C   1 
ATOM   5514 O O   . VAL C 2 93  ? -28.100 1.177   -55.724 1.00 26.36 ?  93  VAL C O   1 
ATOM   5515 C CB  . VAL C 2 93  ? -30.925 0.250   -54.885 1.00 29.13 ?  93  VAL C CB  1 
ATOM   5516 C CG1 . VAL C 2 93  ? -31.674 1.260   -54.028 1.00 28.98 ?  93  VAL C CG1 1 
ATOM   5517 C CG2 . VAL C 2 93  ? -31.799 -0.958  -55.187 1.00 33.11 ?  93  VAL C CG2 1 
ATOM   5518 N N   . TYR C 2 94  ? -29.315 3.051   -56.000 1.00 27.37 ?  94  TYR C N   1 
ATOM   5519 C CA  . TYR C 2 94  ? -28.185 3.950   -55.806 1.00 26.58 ?  94  TYR C CA  1 
ATOM   5520 C C   . TYR C 2 94  ? -28.267 4.562   -54.414 1.00 24.54 ?  94  TYR C C   1 
ATOM   5521 O O   . TYR C 2 94  ? -29.275 5.185   -54.064 1.00 26.38 ?  94  TYR C O   1 
ATOM   5522 C CB  . TYR C 2 94  ? -28.156 5.034   -56.883 1.00 22.91 ?  94  TYR C CB  1 
ATOM   5523 C CG  . TYR C 2 94  ? -27.588 4.553   -58.199 1.00 24.93 ?  94  TYR C CG  1 
ATOM   5524 C CD1 . TYR C 2 94  ? -28.324 3.722   -59.033 1.00 26.25 ?  94  TYR C CD1 1 
ATOM   5525 C CD2 . TYR C 2 94  ? -26.309 4.918   -58.600 1.00 21.58 ?  94  TYR C CD2 1 
ATOM   5526 C CE1 . TYR C 2 94  ? -27.807 3.275   -60.234 1.00 25.98 ?  94  TYR C CE1 1 
ATOM   5527 C CE2 . TYR C 2 94  ? -25.783 4.476   -59.798 1.00 23.22 ?  94  TYR C CE2 1 
ATOM   5528 C CZ  . TYR C 2 94  ? -26.536 3.655   -60.610 1.00 30.08 ?  94  TYR C CZ  1 
ATOM   5529 O OH  . TYR C 2 94  ? -26.014 3.213   -61.805 1.00 31.91 ?  94  TYR C OH  1 
ATOM   5530 N N   . TYR C 2 95  ? -27.212 4.377   -53.626 1.00 24.14 ?  95  TYR C N   1 
ATOM   5531 C CA  . TYR C 2 95  ? -27.145 4.873   -52.260 1.00 26.74 ?  95  TYR C CA  1 
ATOM   5532 C C   . TYR C 2 95  ? -26.052 5.925   -52.147 1.00 24.42 ?  95  TYR C C   1 
ATOM   5533 O O   . TYR C 2 95  ? -24.980 5.785   -52.744 1.00 22.45 ?  95  TYR C O   1 
ATOM   5534 C CB  . TYR C 2 95  ? -26.850 3.745   -51.260 1.00 22.48 ?  95  TYR C CB  1 
ATOM   5535 C CG  . TYR C 2 95  ? -27.660 2.480   -51.440 1.00 25.83 ?  95  TYR C CG  1 
ATOM   5536 C CD1 . TYR C 2 95  ? -27.275 1.508   -52.354 1.00 27.38 ?  95  TYR C CD1 1 
ATOM   5537 C CD2 . TYR C 2 95  ? -28.791 2.243   -50.670 1.00 24.65 ?  95  TYR C CD2 1 
ATOM   5538 C CE1 . TYR C 2 95  ? -28.006 0.345   -52.512 1.00 29.08 ?  95  TYR C CE1 1 
ATOM   5539 C CE2 . TYR C 2 95  ? -29.527 1.085   -50.819 1.00 26.39 ?  95  TYR C CE2 1 
ATOM   5540 C CZ  . TYR C 2 95  ? -29.131 0.139   -51.740 1.00 29.30 ?  95  TYR C CZ  1 
ATOM   5541 O OH  . TYR C 2 95  ? -29.864 -1.015  -51.891 1.00 29.46 ?  95  TYR C OH  1 
ATOM   5542 N N   . CYS C 2 96  ? -26.324 6.973   -51.377 1.00 22.77 ?  96  CYS C N   1 
ATOM   5543 C CA  . CYS C 2 96  ? -25.289 7.901   -50.952 1.00 24.14 ?  96  CYS C CA  1 
ATOM   5544 C C   . CYS C 2 96  ? -24.837 7.530   -49.544 1.00 23.65 ?  96  CYS C C   1 
ATOM   5545 O O   . CYS C 2 96  ? -25.631 7.066   -48.722 1.00 22.06 ?  96  CYS C O   1 
ATOM   5546 C CB  . CYS C 2 96  ? -25.780 9.353   -50.997 1.00 26.20 ?  96  CYS C CB  1 
ATOM   5547 S SG  . CYS C 2 96  ? -27.187 9.753   -49.931 1.00 35.71 ?  96  CYS C SG  1 
ATOM   5548 N N   . ALA C 2 97  ? -23.543 7.713   -49.283 1.00 20.96 ?  97  ALA C N   1 
ATOM   5549 C CA  . ALA C 2 97  ? -22.943 7.308   -48.019 1.00 22.59 ?  97  ALA C CA  1 
ATOM   5550 C C   . ALA C 2 97  ? -21.957 8.370   -47.556 1.00 22.91 ?  97  ALA C C   1 
ATOM   5551 O O   . ALA C 2 97  ? -21.538 9.236   -48.327 1.00 21.49 ?  97  ALA C O   1 
ATOM   5552 C CB  . ALA C 2 97  ? -22.241 5.948   -48.132 1.00 20.64 ?  97  ALA C CB  1 
ATOM   5553 N N   . SER C 2 98  ? -21.577 8.286   -46.282 1.00 19.70 ?  98  SER C N   1 
ATOM   5554 C CA  . SER C 2 98  ? -20.727 9.302   -45.675 1.00 24.80 ?  98  SER C CA  1 
ATOM   5555 C C   . SER C 2 98  ? -19.831 8.662   -44.625 1.00 22.88 ?  98  SER C C   1 
ATOM   5556 O O   . SER C 2 98  ? -20.307 7.900   -43.778 1.00 21.92 ?  98  SER C O   1 
ATOM   5557 C CB  . SER C 2 98  ? -21.572 10.418  -45.047 1.00 23.68 ?  98  SER C CB  1 
ATOM   5558 O OG  . SER C 2 98  ? -22.423 11.019  -46.009 1.00 33.87 ?  98  SER C OG  1 
ATOM   5559 N N   . ASP C 2 99  ? -18.540 8.984   -44.684 1.00 19.94 ?  99  ASP C N   1 
ATOM   5560 C CA  . ASP C 2 99  ? -17.543 8.471   -43.750 1.00 22.82 ?  99  ASP C CA  1 
ATOM   5561 C C   . ASP C 2 99  ? -17.214 9.569   -42.744 1.00 22.47 ?  99  ASP C C   1 
ATOM   5562 O O   . ASP C 2 99  ? -16.594 10.578  -43.097 1.00 19.29 ?  99  ASP C O   1 
ATOM   5563 C CB  . ASP C 2 99  ? -16.291 8.015   -44.499 1.00 20.06 ?  99  ASP C CB  1 
ATOM   5564 C CG  . ASP C 2 99  ? -15.259 7.378   -43.587 1.00 24.10 ?  99  ASP C CG  1 
ATOM   5565 O OD1 . ASP C 2 99  ? -15.580 7.108   -42.411 1.00 23.32 ?  99  ASP C OD1 1 
ATOM   5566 O OD2 . ASP C 2 99  ? -14.121 7.145   -44.049 1.00 22.22 -1 99  ASP C OD2 1 
ATOM   5567 N N   . ARG C 2 100 ? -17.628 9.370   -41.490 1.00 20.89 ?  100 ARG C N   1 
ATOM   5568 C CA  . ARG C 2 100 ? -17.378 10.352  -40.441 1.00 23.18 ?  100 ARG C CA  1 
ATOM   5569 C C   . ARG C 2 100 ? -15.921 10.396  -39.997 1.00 22.97 ?  100 ARG C C   1 
ATOM   5570 O O   . ARG C 2 100 ? -15.526 11.361  -39.334 1.00 22.93 ?  100 ARG C O   1 
ATOM   5571 C CB  . ARG C 2 100 ? -18.263 10.066  -39.227 1.00 22.74 ?  100 ARG C CB  1 
ATOM   5572 C CG  . ARG C 2 100 ? -17.913 8.780   -38.498 1.00 23.24 ?  100 ARG C CG  1 
ATOM   5573 C CD  . ARG C 2 100 ? -19.018 8.373   -37.539 1.00 24.81 ?  100 ARG C CD  1 
ATOM   5574 N NE  . ARG C 2 100 ? -18.553 7.403   -36.555 1.00 26.82 ?  100 ARG C NE  1 
ATOM   5575 C CZ  . ARG C 2 100 ? -19.187 7.119   -35.426 1.00 29.36 ?  100 ARG C CZ  1 
ATOM   5576 N NH1 . ARG C 2 100 ? -20.326 7.710   -35.104 1.00 26.07 ?  100 ARG C NH1 1 
ATOM   5577 N NH2 . ARG C 2 100 ? -18.664 6.219   -34.598 1.00 28.18 ?  100 ARG C NH2 1 
ATOM   5578 N N   . ASP C 2 101 ? -15.118 9.389   -40.341 1.00 21.65 ?  101 ASP C N   1 
ATOM   5579 C CA  . ASP C 2 101 ? -13.741 9.316   -39.871 1.00 21.92 ?  101 ASP C CA  1 
ATOM   5580 C C   . ASP C 2 101 ? -12.751 10.042  -40.771 1.00 23.34 ?  101 ASP C C   1 
ATOM   5581 O O   . ASP C 2 101 ? -11.632 10.327  -40.328 1.00 24.18 ?  101 ASP C O   1 
ATOM   5582 C CB  . ASP C 2 101 ? -13.302 7.853   -39.739 1.00 18.28 ?  101 ASP C CB  1 
ATOM   5583 C CG  . ASP C 2 101 ? -14.259 7.030   -38.902 1.00 19.97 ?  101 ASP C CG  1 
ATOM   5584 O OD1 . ASP C 2 101 ? -14.230 7.163   -37.661 1.00 20.82 ?  101 ASP C OD1 1 
ATOM   5585 O OD2 . ASP C 2 101 ? -15.039 6.247   -39.485 1.00 20.25 -1 101 ASP C OD2 1 
ATOM   5586 N N   . HIS C 2 102 ? -13.123 10.350  -42.011 1.00 19.40 ?  102 HIS C N   1 
ATOM   5587 C CA  . HIS C 2 102 ? -12.158 10.820  -42.991 1.00 20.15 ?  102 HIS C CA  1 
ATOM   5588 C C   . HIS C 2 102 ? -12.690 12.025  -43.753 1.00 22.87 ?  102 HIS C C   1 
ATOM   5589 O O   . HIS C 2 102 ? -13.901 12.209  -43.906 1.00 21.35 ?  102 HIS C O   1 
ATOM   5590 C CB  . HIS C 2 102 ? -11.788 9.697   -43.965 1.00 21.92 ?  102 HIS C CB  1 
ATOM   5591 C CG  . HIS C 2 102 ? -11.059 8.564   -43.313 1.00 23.13 ?  102 HIS C CG  1 
ATOM   5592 N ND1 . HIS C 2 102 ? -11.655 7.350   -43.046 1.00 21.76 ?  102 HIS C ND1 1 
ATOM   5593 C CD2 . HIS C 2 102 ? -9.789  8.468   -42.855 1.00 22.62 ?  102 HIS C CD2 1 
ATOM   5594 C CE1 . HIS C 2 102 ? -10.781 6.553   -42.459 1.00 19.97 ?  102 HIS C CE1 1 
ATOM   5595 N NE2 . HIS C 2 102 ? -9.640  7.206   -42.333 1.00 22.34 ?  102 HIS C NE2 1 
ATOM   5596 N N   . TYR C 2 103 ? -11.752 12.844  -44.228 1.00 22.00 ?  103 TYR C N   1 
ATOM   5597 C CA  . TYR C 2 103 ? -12.051 14.052  -44.985 1.00 21.25 ?  103 TYR C CA  1 
ATOM   5598 C C   . TYR C 2 103 ? -11.345 14.124  -46.327 1.00 22.80 ?  103 TYR C C   1 
ATOM   5599 O O   . TYR C 2 103 ? -11.794 14.881  -47.196 1.00 23.43 ?  103 TYR C O   1 
ATOM   5600 C CB  . TYR C 2 103 ? -11.666 15.297  -44.171 1.00 22.67 ?  103 TYR C CB  1 
ATOM   5601 C CG  . TYR C 2 103 ? -10.168 15.494  -44.050 1.00 21.20 ?  103 TYR C CG  1 
ATOM   5602 C CD1 . TYR C 2 103 ? -9.442  14.836  -43.065 1.00 23.19 ?  103 TYR C CD1 1 
ATOM   5603 C CD2 . TYR C 2 103 ? -9.481  16.337  -44.917 1.00 24.30 ?  103 TYR C CD2 1 
ATOM   5604 C CE1 . TYR C 2 103 ? -8.075  15.008  -42.949 1.00 23.70 ?  103 TYR C CE1 1 
ATOM   5605 C CE2 . TYR C 2 103 ? -8.114  16.514  -44.809 1.00 25.77 ?  103 TYR C CE2 1 
ATOM   5606 C CZ  . TYR C 2 103 ? -7.417  15.848  -43.823 1.00 28.00 ?  103 TYR C CZ  1 
ATOM   5607 O OH  . TYR C 2 103 ? -6.057  16.026  -43.713 1.00 31.34 ?  103 TYR C OH  1 
ATOM   5608 N N   . SER C 2 104 ? -10.261 13.379  -46.526 1.00 21.64 ?  104 SER C N   1 
ATOM   5609 C CA  . SER C 2 104 ? -9.445  13.520  -47.722 1.00 22.01 ?  104 SER C CA  1 
ATOM   5610 C C   . SER C 2 104 ? -10.066 12.770  -48.892 1.00 23.44 ?  104 SER C C   1 
ATOM   5611 O O   . SER C 2 104 ? -10.366 11.576  -48.790 1.00 22.31 ?  104 SER C O   1 
ATOM   5612 C CB  . SER C 2 104 ? -8.031  13.008  -47.456 1.00 20.63 ?  104 SER C CB  1 
ATOM   5613 O OG  . SER C 2 104 ? -7.355  12.715  -48.667 1.00 21.12 ?  104 SER C OG  1 
ATOM   5614 N N   . GLY C 2 105 ? -10.248 13.475  -50.009 1.00 22.56 ?  105 GLY C N   1 
ATOM   5615 C CA  . GLY C 2 105 ? -10.687 12.841  -51.239 1.00 22.18 ?  105 GLY C CA  1 
ATOM   5616 C C   . GLY C 2 105 ? -9.694  11.848  -51.808 1.00 22.44 ?  105 GLY C C   1 
ATOM   5617 O O   . GLY C 2 105 ? -10.013 11.175  -52.795 1.00 18.89 ?  105 GLY C O   1 
ATOM   5618 N N   . THR C 2 106 ? -8.499  11.752  -51.222 1.00 20.28 ?  106 THR C N   1 
ATOM   5619 C CA  . THR C 2 106 ? -7.515  10.745  -51.590 1.00 21.38 ?  106 THR C CA  1 
ATOM   5620 C C   . THR C 2 106 ? -7.306  9.720   -50.481 1.00 22.30 ?  106 THR C C   1 
ATOM   5621 O O   . THR C 2 106 ? -6.306  8.993   -50.498 1.00 23.26 ?  106 THR C O   1 
ATOM   5622 C CB  . THR C 2 106 ? -6.182  11.399  -51.959 1.00 21.89 ?  106 THR C CB  1 
ATOM   5623 O OG1 . THR C 2 106 ? -5.637  12.065  -50.813 1.00 24.20 ?  106 THR C OG1 1 
ATOM   5624 C CG2 . THR C 2 106 ? -6.372  12.402  -53.087 1.00 17.97 ?  106 THR C CG2 1 
ATOM   5625 N N   . TYR C 2 107 ? -8.217  9.660   -49.509 1.00 23.36 ?  107 TYR C N   1 
ATOM   5626 C CA  . TYR C 2 107 ? -8.176  8.593   -48.517 1.00 21.12 ?  107 TYR C CA  1 
ATOM   5627 C C   . TYR C 2 107 ? -8.157  7.248   -49.224 1.00 20.95 ?  107 TYR C C   1 
ATOM   5628 O O   . TYR C 2 107 ? -9.073  6.920   -49.981 1.00 23.53 ?  107 TYR C O   1 
ATOM   5629 C CB  . TYR C 2 107 ? -9.377  8.683   -47.574 1.00 20.21 ?  107 TYR C CB  1 
ATOM   5630 C CG  . TYR C 2 107 ? -9.574  7.432   -46.745 1.00 22.45 ?  107 TYR C CG  1 
ATOM   5631 C CD1 . TYR C 2 107 ? -8.586  6.997   -45.870 1.00 22.34 ?  107 TYR C CD1 1 
ATOM   5632 C CD2 . TYR C 2 107 ? -10.738 6.682   -46.843 1.00 20.34 ?  107 TYR C CD2 1 
ATOM   5633 C CE1 . TYR C 2 107 ? -8.754  5.853   -45.114 1.00 22.70 ?  107 TYR C CE1 1 
ATOM   5634 C CE2 . TYR C 2 107 ? -10.917 5.537   -46.089 1.00 20.96 ?  107 TYR C CE2 1 
ATOM   5635 C CZ  . TYR C 2 107 ? -9.920  5.127   -45.227 1.00 24.88 ?  107 TYR C CZ  1 
ATOM   5636 O OH  . TYR C 2 107 ? -10.089 3.989   -44.472 1.00 21.50 ?  107 TYR C OH  1 
ATOM   5637 N N   . TYR C 2 108 ? -7.101  6.474   -48.981 1.00 22.83 ?  108 TYR C N   1 
ATOM   5638 C CA  . TYR C 2 108 ? -6.807  5.309   -49.805 1.00 24.67 ?  108 TYR C CA  1 
ATOM   5639 C C   . TYR C 2 108 ? -7.857  4.207   -49.700 1.00 23.11 ?  108 TYR C C   1 
ATOM   5640 O O   . TYR C 2 108 ? -7.848  3.296   -50.534 1.00 23.55 ?  108 TYR C O   1 
ATOM   5641 C CB  . TYR C 2 108 ? -5.427  4.764   -49.437 1.00 24.62 ?  108 TYR C CB  1 
ATOM   5642 C CG  . TYR C 2 108 ? -5.443  3.625   -48.448 1.00 28.25 ?  108 TYR C CG  1 
ATOM   5643 C CD1 . TYR C 2 108 ? -5.868  3.816   -47.139 1.00 26.65 ?  108 TYR C CD1 1 
ATOM   5644 C CD2 . TYR C 2 108 ? -5.008  2.361   -48.818 1.00 24.95 ?  108 TYR C CD2 1 
ATOM   5645 C CE1 . TYR C 2 108 ? -5.880  2.771   -46.237 1.00 25.61 ?  108 TYR C CE1 1 
ATOM   5646 C CE2 . TYR C 2 108 ? -5.009  1.315   -47.923 1.00 24.47 ?  108 TYR C CE2 1 
ATOM   5647 C CZ  . TYR C 2 108 ? -5.442  1.524   -46.633 1.00 24.83 ?  108 TYR C CZ  1 
ATOM   5648 O OH  . TYR C 2 108 ? -5.441  0.475   -45.744 1.00 23.81 ?  108 TYR C OH  1 
ATOM   5649 N N   . GLY C 2 109 ? -8.752  4.261   -48.715 1.00 23.75 ?  109 GLY C N   1 
ATOM   5650 C CA  . GLY C 2 109 ? -9.799  3.263   -48.602 1.00 22.97 ?  109 GLY C CA  1 
ATOM   5651 C C   . GLY C 2 109 ? -11.175 3.780   -48.973 1.00 23.19 ?  109 GLY C C   1 
ATOM   5652 O O   . GLY C 2 109 ? -12.191 3.194   -48.586 1.00 25.12 ?  109 GLY C O   1 
ATOM   5653 N N   . ARG C 2 110 ? -11.221 4.869   -49.743 1.00 21.93 ?  110 ARG C N   1 
ATOM   5654 C CA  . ARG C 2 110 ? -12.480 5.557   -50.009 1.00 22.10 ?  110 ARG C CA  1 
ATOM   5655 C C   . ARG C 2 110 ? -13.440 4.758   -50.881 1.00 21.29 ?  110 ARG C C   1 
ATOM   5656 O O   . ARG C 2 110 ? -14.611 5.139   -50.980 1.00 20.24 ?  110 ARG C O   1 
ATOM   5657 C CB  . ARG C 2 110 ? -12.209 6.916   -50.659 1.00 22.97 ?  110 ARG C CB  1 
ATOM   5658 C CG  . ARG C 2 110 ? -11.584 6.846   -52.047 1.00 20.17 ?  110 ARG C CG  1 
ATOM   5659 C CD  . ARG C 2 110 ? -11.023 8.202   -52.442 1.00 18.47 ?  110 ARG C CD  1 
ATOM   5660 N NE  . ARG C 2 110 ? -10.268 8.165   -53.689 1.00 20.08 ?  110 ARG C NE  1 
ATOM   5661 C CZ  . ARG C 2 110 ? -8.966  7.928   -53.771 1.00 19.96 ?  110 ARG C CZ  1 
ATOM   5662 N NH1 . ARG C 2 110 ? -8.244  7.662   -52.695 1.00 23.45 ?  110 ARG C NH1 1 
ATOM   5663 N NH2 . ARG C 2 110 ? -8.374  7.959   -54.961 1.00 17.79 ?  110 ARG C NH2 1 
ATOM   5664 N N   . ARG C 2 111 ? -12.991 3.674   -51.512 1.00 19.02 ?  111 ARG C N   1 
ATOM   5665 C CA  . ARG C 2 111 ? -13.881 2.860   -52.328 1.00 20.07 ?  111 ARG C CA  1 
ATOM   5666 C C   . ARG C 2 111 ? -14.489 1.687   -51.570 1.00 23.15 ?  111 ARG C C   1 
ATOM   5667 O O   . ARG C 2 111 ? -15.412 1.050   -52.089 1.00 23.08 ?  111 ARG C O   1 
ATOM   5668 C CB  . ARG C 2 111 ? -13.149 2.328   -53.565 1.00 20.25 ?  111 ARG C CB  1 
ATOM   5669 C CG  . ARG C 2 111 ? -12.440 3.383   -54.395 1.00 19.24 ?  111 ARG C CG  1 
ATOM   5670 C CD  . ARG C 2 111 ? -11.513 2.724   -55.405 1.00 19.10 ?  111 ARG C CD  1 
ATOM   5671 N NE  . ARG C 2 111 ? -10.805 3.694   -56.231 1.00 18.98 ?  111 ARG C NE  1 
ATOM   5672 C CZ  . ARG C 2 111 ? -9.687  4.308   -55.869 1.00 21.65 ?  111 ARG C CZ  1 
ATOM   5673 N NH1 . ARG C 2 111 ? -9.126  4.084   -54.691 1.00 23.36 ?  111 ARG C NH1 1 
ATOM   5674 N NH2 . ARG C 2 111 ? -9.118  5.168   -56.708 1.00 20.73 ?  111 ARG C NH2 1 
ATOM   5675 N N   . PHE C 2 112 ? -14.002 1.383   -50.369 1.00 21.19 ?  112 PHE C N   1 
ATOM   5676 C CA  . PHE C 2 112 ? -14.537 0.267   -49.603 1.00 23.74 ?  112 PHE C CA  1 
ATOM   5677 C C   . PHE C 2 112 ? -15.865 0.646   -48.962 1.00 23.33 ?  112 PHE C C   1 
ATOM   5678 O O   . PHE C 2 112 ? -16.022 1.746   -48.423 1.00 21.28 ?  112 PHE C O   1 
ATOM   5679 C CB  . PHE C 2 112 ? -13.542 -0.176  -48.530 1.00 24.98 ?  112 PHE C CB  1 
ATOM   5680 C CG  . PHE C 2 112 ? -12.247 -0.701  -49.083 1.00 23.95 ?  112 PHE C CG  1 
ATOM   5681 C CD1 . PHE C 2 112 ? -12.237 -1.771  -49.962 1.00 22.75 ?  112 PHE C CD1 1 
ATOM   5682 C CD2 . PHE C 2 112 ? -11.040 -0.129  -48.718 1.00 21.91 ?  112 PHE C CD2 1 
ATOM   5683 C CE1 . PHE C 2 112 ? -11.047 -2.259  -50.470 1.00 22.12 ?  112 PHE C CE1 1 
ATOM   5684 C CE2 . PHE C 2 112 ? -9.847  -0.612  -49.222 1.00 19.78 ?  112 PHE C CE2 1 
ATOM   5685 C CZ  . PHE C 2 112 ? -9.851  -1.678  -50.098 1.00 24.58 ?  112 PHE C CZ  1 
ATOM   5686 N N   . VAL C 2 113 ? -16.825 -0.279  -49.025 1.00 25.74 ?  113 VAL C N   1 
ATOM   5687 C CA  . VAL C 2 113 ? -18.155 -0.020  -48.480 1.00 25.91 ?  113 VAL C CA  1 
ATOM   5688 C C   . VAL C 2 113 ? -18.095 0.130   -46.965 1.00 23.77 ?  113 VAL C C   1 
ATOM   5689 O O   . VAL C 2 113 ? -18.708 1.039   -46.391 1.00 23.83 ?  113 VAL C O   1 
ATOM   5690 C CB  . VAL C 2 113 ? -19.126 -1.140  -48.898 1.00 22.96 ?  113 VAL C CB  1 
ATOM   5691 C CG1 . VAL C 2 113 ? -20.283 -1.247  -47.914 1.00 22.70 ?  113 VAL C CG1 1 
ATOM   5692 C CG2 . VAL C 2 113 ? -19.642 -0.903  -50.306 1.00 23.22 ?  113 VAL C CG2 1 
ATOM   5693 N N   . GLU C 2 114 ? -17.349 -0.750  -46.295 1.00 21.77 ?  114 GLU C N   1 
ATOM   5694 C CA  . GLU C 2 114 ? -17.354 -0.819  -44.839 1.00 26.12 ?  114 GLU C CA  1 
ATOM   5695 C C   . GLU C 2 114 ? -16.687 0.378   -44.174 1.00 26.05 ?  114 GLU C C   1 
ATOM   5696 O O   . GLU C 2 114 ? -16.737 0.484   -42.943 1.00 26.89 ?  114 GLU C O   1 
ATOM   5697 C CB  . GLU C 2 114 ? -16.676 -2.114  -44.386 1.00 27.22 ?  114 GLU C CB  1 
ATOM   5698 C CG  . GLU C 2 114 ? -17.044 -3.325  -45.233 1.00 29.10 ?  114 GLU C CG  1 
ATOM   5699 C CD  . GLU C 2 114 ? -16.049 -3.582  -46.350 1.00 33.57 ?  114 GLU C CD  1 
ATOM   5700 O OE1 . GLU C 2 114 ? -15.957 -2.742  -47.270 1.00 29.82 ?  114 GLU C OE1 1 
ATOM   5701 O OE2 . GLU C 2 114 ? -15.356 -4.621  -46.306 1.00 40.78 -1 114 GLU C OE2 1 
ATOM   5702 N N   . GLU C 2 115 ? -16.069 1.276   -44.943 1.00 25.34 ?  115 GLU C N   1 
ATOM   5703 C CA  . GLU C 2 115 ? -15.488 2.480   -44.364 1.00 25.62 ?  115 GLU C CA  1 
ATOM   5704 C C   . GLU C 2 115 ? -16.519 3.575   -44.129 1.00 23.67 ?  115 GLU C C   1 
ATOM   5705 O O   . GLU C 2 115 ? -16.291 4.451   -43.289 1.00 24.53 ?  115 GLU C O   1 
ATOM   5706 C CB  . GLU C 2 115 ? -14.370 3.016   -45.261 1.00 25.61 ?  115 GLU C CB  1 
ATOM   5707 C CG  . GLU C 2 115 ? -13.122 2.152   -45.272 1.00 27.81 ?  115 GLU C CG  1 
ATOM   5708 C CD  . GLU C 2 115 ? -12.424 2.119   -43.926 1.00 25.88 ?  115 GLU C CD  1 
ATOM   5709 O OE1 . GLU C 2 115 ? -12.543 3.104   -43.165 1.00 30.23 ?  115 GLU C OE1 1 
ATOM   5710 O OE2 . GLU C 2 115 ? -11.756 1.108   -43.629 1.00 25.58 -1 115 GLU C OE2 1 
ATOM   5711 N N   . TYR C 2 116 ? -17.641 3.545   -44.841 1.00 21.99 ?  116 TYR C N   1 
ATOM   5712 C CA  . TYR C 2 116 ? -18.665 4.569   -44.703 1.00 25.24 ?  116 TYR C CA  1 
ATOM   5713 C C   . TYR C 2 116 ? -19.632 4.197   -43.588 1.00 23.02 ?  116 TYR C C   1 
ATOM   5714 O O   . TYR C 2 116 ? -19.998 3.029   -43.428 1.00 25.01 ?  116 TYR C O   1 
ATOM   5715 C CB  . TYR C 2 116 ? -19.409 4.766   -46.025 1.00 22.82 ?  116 TYR C CB  1 
ATOM   5716 C CG  . TYR C 2 116 ? -18.541 5.397   -47.089 1.00 21.26 ?  116 TYR C CG  1 
ATOM   5717 C CD1 . TYR C 2 116 ? -17.602 4.644   -47.783 1.00 20.66 ?  116 TYR C CD1 1 
ATOM   5718 C CD2 . TYR C 2 116 ? -18.641 6.750   -47.382 1.00 19.99 ?  116 TYR C CD2 1 
ATOM   5719 C CE1 . TYR C 2 116 ? -16.799 5.217   -48.747 1.00 18.72 ?  116 TYR C CE1 1 
ATOM   5720 C CE2 . TYR C 2 116 ? -17.842 7.332   -48.345 1.00 18.11 ?  116 TYR C CE2 1 
ATOM   5721 C CZ  . TYR C 2 116 ? -16.923 6.561   -49.025 1.00 18.74 ?  116 TYR C CZ  1 
ATOM   5722 O OH  . TYR C 2 116 ? -16.125 7.137   -49.985 1.00 19.34 ?  116 TYR C OH  1 
ATOM   5723 N N   . ASP C 2 117 ? -20.045 5.205   -42.819 1.00 21.65 ?  117 ASP C N   1 
ATOM   5724 C CA  . ASP C 2 117 ? -20.754 4.983   -41.569 1.00 24.63 ?  117 ASP C CA  1 
ATOM   5725 C C   . ASP C 2 117 ? -22.225 5.372   -41.605 1.00 25.40 ?  117 ASP C C   1 
ATOM   5726 O O   . ASP C 2 117 ? -22.979 4.936   -40.730 1.00 25.07 ?  117 ASP C O   1 
ATOM   5727 C CB  . ASP C 2 117 ? -20.062 5.754   -40.435 1.00 24.39 ?  117 ASP C CB  1 
ATOM   5728 C CG  . ASP C 2 117 ? -18.629 5.303   -40.219 1.00 23.98 ?  117 ASP C CG  1 
ATOM   5729 O OD1 . ASP C 2 117 ? -18.418 4.299   -39.507 1.00 34.34 ?  117 ASP C OD1 1 
ATOM   5730 O OD2 . ASP C 2 117 ? -17.713 5.944   -40.776 1.00 21.51 -1 117 ASP C OD2 1 
ATOM   5731 N N   . TYR C 2 118 ? -22.651 6.173   -42.578 1.00 26.89 ?  118 TYR C N   1 
ATOM   5732 C CA  . TYR C 2 118 ? -24.043 6.579   -42.699 1.00 25.30 ?  118 TYR C CA  1 
ATOM   5733 C C   . TYR C 2 118 ? -24.520 6.315   -44.117 1.00 26.40 ?  118 TYR C C   1 
ATOM   5734 O O   . TYR C 2 118 ? -23.808 6.603   -45.083 1.00 25.82 ?  118 TYR C O   1 
ATOM   5735 C CB  . TYR C 2 118 ? -24.224 8.056   -42.335 1.00 22.97 ?  118 TYR C CB  1 
ATOM   5736 C CG  . TYR C 2 118 ? -23.707 8.387   -40.956 1.00 24.69 ?  118 TYR C CG  1 
ATOM   5737 C CD1 . TYR C 2 118 ? -24.282 7.819   -39.827 1.00 26.90 ?  118 TYR C CD1 1 
ATOM   5738 C CD2 . TYR C 2 118 ? -22.635 9.252   -40.782 1.00 24.78 ?  118 TYR C CD2 1 
ATOM   5739 C CE1 . TYR C 2 118 ? -23.811 8.110   -38.562 1.00 27.43 ?  118 TYR C CE1 1 
ATOM   5740 C CE2 . TYR C 2 118 ? -22.156 9.549   -39.519 1.00 25.55 ?  118 TYR C CE2 1 
ATOM   5741 C CZ  . TYR C 2 118 ? -22.748 8.975   -38.413 1.00 27.95 ?  118 TYR C CZ  1 
ATOM   5742 O OH  . TYR C 2 118 ? -22.279 9.265   -37.153 1.00 34.49 ?  118 TYR C OH  1 
ATOM   5743 N N   . TRP C 2 119 ? -25.725 5.763   -44.238 1.00 26.41 ?  119 TRP C N   1 
ATOM   5744 C CA  . TRP C 2 119 ? -26.242 5.319   -45.523 1.00 24.93 ?  119 TRP C CA  1 
ATOM   5745 C C   . TRP C 2 119 ? -27.699 5.725   -45.671 1.00 26.83 ?  119 TRP C C   1 
ATOM   5746 O O   . TRP C 2 119 ? -28.458 5.717   -44.699 1.00 23.75 ?  119 TRP C O   1 
ATOM   5747 C CB  . TRP C 2 119 ? -26.121 3.799   -45.674 1.00 22.19 ?  119 TRP C CB  1 
ATOM   5748 C CG  . TRP C 2 119 ? -24.713 3.310   -45.745 1.00 24.50 ?  119 TRP C CG  1 
ATOM   5749 C CD1 . TRP C 2 119 ? -23.865 3.093   -44.699 1.00 25.42 ?  119 TRP C CD1 1 
ATOM   5750 C CD2 . TRP C 2 119 ? -23.988 2.965   -46.929 1.00 24.73 ?  119 TRP C CD2 1 
ATOM   5751 N NE1 . TRP C 2 119 ? -22.654 2.637   -45.160 1.00 26.75 ?  119 TRP C NE1 1 
ATOM   5752 C CE2 . TRP C 2 119 ? -22.704 2.550   -46.526 1.00 24.44 ?  119 TRP C CE2 1 
ATOM   5753 C CE3 . TRP C 2 119 ? -24.299 2.970   -48.292 1.00 26.84 ?  119 TRP C CE3 1 
ATOM   5754 C CZ2 . TRP C 2 119 ? -21.732 2.142   -47.437 1.00 24.47 ?  119 TRP C CZ2 1 
ATOM   5755 C CZ3 . TRP C 2 119 ? -23.335 2.564   -49.194 1.00 25.21 ?  119 TRP C CZ3 1 
ATOM   5756 C CH2 . TRP C 2 119 ? -22.066 2.156   -48.763 1.00 25.69 ?  119 TRP C CH2 1 
ATOM   5757 N N   . GLY C 2 120 ? -28.083 6.072   -46.897 1.00 29.45 ?  120 GLY C N   1 
ATOM   5758 C CA  . GLY C 2 120 ? -29.474 6.323   -47.198 1.00 29.38 ?  120 GLY C CA  1 
ATOM   5759 C C   . GLY C 2 120 ? -30.205 5.060   -47.608 1.00 29.34 ?  120 GLY C C   1 
ATOM   5760 O O   . GLY C 2 120 ? -29.609 4.007   -47.822 1.00 26.66 ?  120 GLY C O   1 
ATOM   5761 N N   . GLN C 2 121 ? -31.528 5.180   -47.714 1.00 29.98 ?  121 GLN C N   1 
ATOM   5762 C CA  . GLN C 2 121 ? -32.345 4.047   -48.128 1.00 32.20 ?  121 GLN C CA  1 
ATOM   5763 C C   . GLN C 2 121 ? -32.246 3.756   -49.619 1.00 28.83 ?  121 GLN C C   1 
ATOM   5764 O O   . GLN C 2 121 ? -32.668 2.678   -50.050 1.00 30.23 ?  121 GLN C O   1 
ATOM   5765 C CB  . GLN C 2 121 ? -33.808 4.280   -47.741 1.00 32.09 ?  121 GLN C CB  1 
ATOM   5766 C CG  . GLN C 2 121 ? -34.101 4.001   -46.276 1.00 33.12 ?  121 GLN C CG  1 
ATOM   5767 C CD  . GLN C 2 121 ? -33.834 2.556   -45.899 1.00 32.44 ?  121 GLN C CD  1 
ATOM   5768 O OE1 . GLN C 2 121 ? -32.849 2.248   -45.226 1.00 31.63 ?  121 GLN C OE1 1 
ATOM   5769 N NE2 . GLN C 2 121 ? -34.705 1.657   -46.346 1.00 34.21 ?  121 GLN C NE2 1 
ATOM   5770 N N   . GLY C 2 122 ? -31.706 4.677   -50.407 1.00 28.13 ?  122 GLY C N   1 
ATOM   5771 C CA  . GLY C 2 122 ? -31.477 4.435   -51.815 1.00 29.69 ?  122 GLY C CA  1 
ATOM   5772 C C   . GLY C 2 122 ? -32.632 4.888   -52.692 1.00 30.17 ?  122 GLY C C   1 
ATOM   5773 O O   . GLY C 2 122 ? -33.776 5.017   -52.260 1.00 29.24 ?  122 GLY C O   1 
ATOM   5774 N N   . THR C 2 123 ? -32.303 5.143   -53.957 1.00 29.70 ?  123 THR C N   1 
ATOM   5775 C CA  . THR C 2 123 ? -33.283 5.430   -54.992 1.00 28.56 ?  123 THR C CA  1 
ATOM   5776 C C   . THR C 2 123 ? -33.081 4.447   -56.135 1.00 30.56 ?  123 THR C C   1 
ATOM   5777 O O   . THR C 2 123 ? -31.943 4.111   -56.483 1.00 28.91 ?  123 THR C O   1 
ATOM   5778 C CB  . THR C 2 123 ? -33.174 6.882   -55.494 1.00 27.24 ?  123 THR C CB  1 
ATOM   5779 O OG1 . THR C 2 123 ? -34.130 7.106   -56.538 1.00 31.45 ?  123 THR C OG1 1 
ATOM   5780 C CG2 . THR C 2 123 ? -31.773 7.178   -56.014 1.00 25.44 ?  123 THR C CG2 1 
ATOM   5781 N N   . GLN C 2 124 ? -34.187 3.970   -56.702 1.00 30.47 ?  124 GLN C N   1 
ATOM   5782 C CA  . GLN C 2 124 ? -34.143 2.935   -57.725 1.00 30.20 ?  124 GLN C CA  1 
ATOM   5783 C C   . GLN C 2 124 ? -33.924 3.556   -59.097 1.00 31.72 ?  124 GLN C C   1 
ATOM   5784 O O   . GLN C 2 124 ? -34.625 4.498   -59.480 1.00 36.57 ?  124 GLN C O   1 
ATOM   5785 C CB  . GLN C 2 124 ? -35.431 2.111   -57.721 1.00 33.65 ?  124 GLN C CB  1 
ATOM   5786 C CG  . GLN C 2 124 ? -35.512 1.090   -58.850 1.00 32.12 ?  124 GLN C CG  1 
ATOM   5787 C CD  . GLN C 2 124 ? -34.621 -0.114  -58.608 1.00 33.96 ?  124 GLN C CD  1 
ATOM   5788 O OE1 . GLN C 2 124 ? -34.601 -0.675  -57.513 1.00 34.38 ?  124 GLN C OE1 1 
ATOM   5789 N NE2 . GLN C 2 124 ? -33.872 -0.513  -59.631 1.00 29.42 ?  124 GLN C NE2 1 
ATOM   5790 N N   . VAL C 2 125 ? -32.946 3.027   -59.826 1.00 29.22 ?  125 VAL C N   1 
ATOM   5791 C CA  . VAL C 2 125 ? -32.686 3.399   -61.210 1.00 29.76 ?  125 VAL C CA  1 
ATOM   5792 C C   . VAL C 2 125 ? -32.881 2.158   -62.067 1.00 32.76 ?  125 VAL C C   1 
ATOM   5793 O O   . VAL C 2 125 ? -32.271 1.114   -61.804 1.00 34.27 ?  125 VAL C O   1 
ATOM   5794 C CB  . VAL C 2 125 ? -31.270 3.974   -61.395 1.00 26.91 ?  125 VAL C CB  1 
ATOM   5795 C CG1 . VAL C 2 125 ? -30.961 4.155   -62.874 1.00 32.12 ?  125 VAL C CG1 1 
ATOM   5796 C CG2 . VAL C 2 125 ? -31.133 5.294   -60.653 1.00 27.16 ?  125 VAL C CG2 1 
ATOM   5797 N N   . THR C 2 126 ? -33.735 2.268   -63.082 1.00 32.86 ?  126 THR C N   1 
ATOM   5798 C CA  . THR C 2 126 ? -34.039 1.159   -63.980 1.00 31.42 ?  126 THR C CA  1 
ATOM   5799 C C   . THR C 2 126 ? -33.835 1.632   -65.412 1.00 31.88 ?  126 THR C C   1 
ATOM   5800 O O   . THR C 2 126 ? -34.562 2.510   -65.888 1.00 35.77 ?  126 THR C O   1 
ATOM   5801 C CB  . THR C 2 126 ? -35.468 0.654   -63.775 1.00 33.95 ?  126 THR C CB  1 
ATOM   5802 O OG1 . THR C 2 126 ? -35.660 0.301   -62.399 1.00 33.96 ?  126 THR C OG1 1 
ATOM   5803 C CG2 . THR C 2 126 ? -35.733 -0.565  -64.646 1.00 31.10 ?  126 THR C CG2 1 
ATOM   5804 N N   . VAL C 2 127 ? -32.847 1.060   -66.092 1.00 31.66 ?  127 VAL C N   1 
ATOM   5805 C CA  . VAL C 2 127 ? -32.600 1.341   -67.500 1.00 33.22 ?  127 VAL C CA  1 
ATOM   5806 C C   . VAL C 2 127 ? -33.128 0.170   -68.315 1.00 38.28 ?  127 VAL C C   1 
ATOM   5807 O O   . VAL C 2 127 ? -32.758 -0.985  -68.071 1.00 35.92 ?  127 VAL C O   1 
ATOM   5808 C CB  . VAL C 2 127 ? -31.106 1.580   -67.775 1.00 32.08 ?  127 VAL C CB  1 
ATOM   5809 C CG1 . VAL C 2 127 ? -30.876 1.772   -69.264 1.00 31.78 ?  127 VAL C CG1 1 
ATOM   5810 C CG2 . VAL C 2 127 ? -30.614 2.786   -66.994 1.00 30.68 ?  127 VAL C CG2 1 
ATOM   5811 N N   . SER C 2 128 ? -33.997 0.465   -69.276 1.00 35.61 ?  128 SER C N   1 
ATOM   5812 C CA  . SER C 2 128 ? -34.695 -0.554  -70.048 1.00 39.64 ?  128 SER C CA  1 
ATOM   5813 C C   . SER C 2 128 ? -34.062 -0.677  -71.428 1.00 36.73 ?  128 SER C C   1 
ATOM   5814 O O   . SER C 2 128 ? -33.965 0.313   -72.162 1.00 38.29 ?  128 SER C O   1 
ATOM   5815 C CB  . SER C 2 128 ? -36.180 -0.213  -70.170 1.00 38.63 ?  128 SER C CB  1 
ATOM   5816 O OG  . SER C 2 128 ? -36.369 0.944   -70.966 1.00 34.08 ?  128 SER C OG  1 
ATOM   5817 N N   . SER C 2 129 ? -33.636 -1.887  -71.775 1.00 32.93 ?  129 SER C N   1 
ATOM   5818 C CA  . SER C 2 129 ? -33.139 -2.145  -73.116 1.00 40.23 ?  129 SER C CA  1 
ATOM   5819 C C   . SER C 2 129 ? -34.283 -2.090  -74.125 1.00 43.58 ?  129 SER C C   1 
ATOM   5820 O O   . SER C 2 129 ? -35.464 -2.176  -73.776 1.00 40.47 ?  129 SER C O   1 
ATOM   5821 C CB  . SER C 2 129 ? -32.450 -3.509  -73.179 1.00 37.63 ?  129 SER C CB  1 
ATOM   5822 O OG  . SER C 2 129 ? -32.113 -3.854  -74.511 1.00 38.65 ?  129 SER C OG  1 
ATOM   5823 N N   . HIS C 2 130 ? -33.916 -1.939  -75.399 1.00 40.75 ?  130 HIS C N   1 
ATOM   5824 C CA  . HIS C 2 130 ? -34.903 -2.025  -76.468 1.00 46.52 ?  130 HIS C CA  1 
ATOM   5825 C C   . HIS C 2 130 ? -35.486 -3.424  -76.601 1.00 42.11 ?  130 HIS C C   1 
ATOM   5826 O O   . HIS C 2 130 ? -36.513 -3.592  -77.268 1.00 40.43 ?  130 HIS C O   1 
ATOM   5827 C CB  . HIS C 2 130 ? -34.276 -1.595  -77.795 1.00 48.81 ?  130 HIS C CB  1 
ATOM   5828 C CG  . HIS C 2 130 ? -34.055 -0.119  -77.909 1.00 57.17 ?  130 HIS C CG  1 
ATOM   5829 N ND1 . HIS C 2 130 ? -35.090 0.790   -77.938 1.00 57.09 ?  130 HIS C ND1 1 
ATOM   5830 C CD2 . HIS C 2 130 ? -32.915 0.607   -77.994 1.00 59.30 ?  130 HIS C CD2 1 
ATOM   5831 C CE1 . HIS C 2 130 ? -34.598 2.012   -78.040 1.00 61.35 ?  130 HIS C CE1 1 
ATOM   5832 N NE2 . HIS C 2 130 ? -33.281 1.929   -78.076 1.00 63.04 ?  130 HIS C NE2 1 
ATOM   5833 N N   . HIS C 2 131 ? -34.860 -4.419  -75.977 1.00 40.11 ?  131 HIS C N   1 
ATOM   5834 C CA  . HIS C 2 131 ? -35.284 -5.814  -76.027 1.00 39.20 ?  131 HIS C CA  1 
ATOM   5835 C C   . HIS C 2 131 ? -35.681 -6.223  -74.614 1.00 42.06 ?  131 HIS C C   1 
ATOM   5836 O O   . HIS C 2 131 ? -34.819 -6.375  -73.741 1.00 43.39 ?  131 HIS C O   1 
ATOM   5837 C CB  . HIS C 2 131 ? -34.158 -6.689  -76.576 1.00 36.59 ?  131 HIS C CB  1 
ATOM   5838 C CG  . HIS C 2 131 ? -34.403 -8.158  -76.444 1.00 37.15 ?  131 HIS C CG  1 
ATOM   5839 N ND1 . HIS C 2 131 ? -34.801 -8.940  -77.505 1.00 35.70 ?  131 HIS C ND1 1 
ATOM   5840 C CD2 . HIS C 2 131 ? -34.284 -8.993  -75.384 1.00 36.28 ?  131 HIS C CD2 1 
ATOM   5841 C CE1 . HIS C 2 131 ? -34.926 -10.192 -77.103 1.00 35.51 ?  131 HIS C CE1 1 
ATOM   5842 N NE2 . HIS C 2 131 ? -34.621 -10.251 -75.820 1.00 36.29 ?  131 HIS C NE2 1 
ATOM   5843 N N   . HIS C 2 132 ? -36.980 -6.403  -74.391 1.00 42.08 ?  132 HIS C N   1 
ATOM   5844 C CA  . HIS C 2 132 ? -37.499 -6.598  -73.045 1.00 41.78 ?  132 HIS C CA  1 
ATOM   5845 C C   . HIS C 2 132 ? -37.292 -8.031  -72.566 1.00 44.19 ?  132 HIS C C   1 
ATOM   5846 O O   . HIS C 2 132 ? -37.254 -8.978  -73.357 1.00 42.26 ?  132 HIS C O   1 
ATOM   5847 C CB  . HIS C 2 132 ? -38.985 -6.243  -72.988 1.00 42.95 ?  132 HIS C CB  1 
ATOM   5848 C CG  . HIS C 2 132 ? -39.277 -4.808  -73.300 1.00 47.70 ?  132 HIS C CG  1 
ATOM   5849 N ND1 . HIS C 2 132 ? -39.023 -4.246  -74.533 1.00 46.83 ?  132 HIS C ND1 1 
ATOM   5850 C CD2 . HIS C 2 132 ? -39.798 -3.819  -72.536 1.00 50.82 ?  132 HIS C CD2 1 
ATOM   5851 C CE1 . HIS C 2 132 ? -39.377 -2.973  -74.516 1.00 46.70 ?  132 HIS C CE1 1 
ATOM   5852 N NE2 . HIS C 2 132 ? -39.850 -2.689  -73.316 1.00 50.11 ?  132 HIS C NE2 1 
ATOM   5853 N N   . HIS C 2 133 ? -37.158 -8.174  -71.248 1.00 48.80 ?  133 HIS C N   1 
ATOM   5854 C CA  . HIS C 2 133 ? -37.021 -9.487  -70.632 1.00 47.85 ?  133 HIS C CA  1 
ATOM   5855 C C   . HIS C 2 133 ? -38.250 -10.344 -70.914 1.00 48.03 ?  133 HIS C C   1 
ATOM   5856 O O   . HIS C 2 133 ? -39.356 -9.838  -71.121 1.00 46.70 ?  133 HIS C O   1 
ATOM   5857 C CB  . HIS C 2 133 ? -36.835 -9.347  -69.119 1.00 50.84 ?  133 HIS C CB  1 
ATOM   5858 C CG  . HIS C 2 133 ? -35.404 -9.292  -68.681 1.00 56.30 ?  133 HIS C CG  1 
ATOM   5859 N ND1 . HIS C 2 133 ? -34.934 -8.340  -67.802 1.00 59.68 ?  133 HIS C ND1 1 
ATOM   5860 C CD2 . HIS C 2 133 ? -34.344 -10.077 -68.987 1.00 58.15 ?  133 HIS C CD2 1 
ATOM   5861 C CE1 . HIS C 2 133 ? -33.644 -8.537  -67.591 1.00 61.71 ?  133 HIS C CE1 1 
ATOM   5862 N NE2 . HIS C 2 133 ? -33.262 -9.585  -68.299 1.00 63.21 ?  133 HIS C NE2 1 
ATOM   5863 N N   . HIS C 2 134 ? -38.044 -11.658 -70.915 1.00 44.92 ?  134 HIS C N   1 
ATOM   5864 C CA  . HIS C 2 134 ? -39.139 -12.615 -71.041 1.00 42.25 ?  134 HIS C CA  1 
ATOM   5865 C C   . HIS C 2 134 ? -38.667 -14.015 -70.666 1.00 42.90 ?  134 HIS C C   1 
ATOM   5866 O O   . HIS C 2 134 ? -37.485 -14.337 -70.796 1.00 43.48 ?  134 HIS C O   1 
ATOM   5867 C CB  . HIS C 2 134 ? -39.714 -12.614 -72.461 1.00 41.32 ?  134 HIS C CB  1 
ATOM   5868 C CG  . HIS C 2 134 ? -38.745 -13.065 -73.508 1.00 39.82 ?  134 HIS C CG  1 
ATOM   5869 N ND1 . HIS C 2 134 ? -37.960 -12.186 -74.223 1.00 39.39 ?  134 HIS C ND1 1 
ATOM   5870 C CD2 . HIS C 2 134 ? -38.436 -14.301 -73.965 1.00 35.95 ?  134 HIS C CD2 1 
ATOM   5871 C CE1 . HIS C 2 134 ? -37.209 -12.861 -75.074 1.00 36.50 ?  134 HIS C CE1 1 
ATOM   5872 N NE2 . HIS C 2 134 ? -37.478 -14.147 -74.937 1.00 34.91 ?  134 HIS C NE2 1 
ATOM   5873 N N   . GLN D 2 1   ? 42.740  13.489  -23.529 1.00 52.36 ?  1   GLN D N   1 
ATOM   5874 C CA  . GLN D 2 1   ? 41.348  13.791  -23.216 1.00 53.57 ?  1   GLN D CA  1 
ATOM   5875 C C   . GLN D 2 1   ? 41.151  14.055  -21.720 1.00 52.93 ?  1   GLN D C   1 
ATOM   5876 O O   . GLN D 2 1   ? 41.607  15.074  -21.201 1.00 58.30 ?  1   GLN D O   1 
ATOM   5877 C CB  . GLN D 2 1   ? 40.437  12.653  -23.704 1.00 56.94 ?  1   GLN D CB  1 
ATOM   5878 C CG  . GLN D 2 1   ? 40.935  11.245  -23.386 1.00 59.69 ?  1   GLN D CG  1 
ATOM   5879 C CD  . GLN D 2 1   ? 39.821  10.216  -23.420 1.00 58.05 ?  1   GLN D CD  1 
ATOM   5880 O OE1 . GLN D 2 1   ? 39.759  9.325   -22.574 1.00 59.59 ?  1   GLN D OE1 1 
ATOM   5881 N NE2 . GLN D 2 1   ? 38.936  10.331  -24.406 1.00 53.02 ?  1   GLN D NE2 1 
ATOM   5882 N N   . VAL D 2 2   ? 40.471  13.139  -21.036 1.00 50.38 ?  2   VAL D N   1 
ATOM   5883 C CA  . VAL D 2 2   ? 40.169  13.261  -19.615 1.00 50.33 ?  2   VAL D CA  1 
ATOM   5884 C C   . VAL D 2 2   ? 41.198  12.464  -18.826 1.00 52.03 ?  2   VAL D C   1 
ATOM   5885 O O   . VAL D 2 2   ? 41.524  11.325  -19.186 1.00 55.33 ?  2   VAL D O   1 
ATOM   5886 C CB  . VAL D 2 2   ? 38.741  12.772  -19.312 1.00 46.11 ?  2   VAL D CB  1 
ATOM   5887 C CG1 . VAL D 2 2   ? 38.582  12.421  -17.838 1.00 43.62 ?  2   VAL D CG1 1 
ATOM   5888 C CG2 . VAL D 2 2   ? 37.723  13.821  -19.730 1.00 45.47 ?  2   VAL D CG2 1 
ATOM   5889 N N   . GLN D 2 3   ? 41.718  13.062  -17.756 1.00 49.26 ?  3   GLN D N   1 
ATOM   5890 C CA  . GLN D 2 3   ? 42.639  12.400  -16.843 1.00 48.76 ?  3   GLN D CA  1 
ATOM   5891 C C   . GLN D 2 3   ? 42.070  12.459  -15.433 1.00 47.91 ?  3   GLN D C   1 
ATOM   5892 O O   . GLN D 2 3   ? 41.697  13.536  -14.956 1.00 44.93 ?  3   GLN D O   1 
ATOM   5893 C CB  . GLN D 2 3   ? 44.025  13.050  -16.884 1.00 49.84 ?  3   GLN D CB  1 
ATOM   5894 C CG  . GLN D 2 3   ? 44.900  12.719  -15.684 1.00 54.17 ?  3   GLN D CG  1 
ATOM   5895 C CD  . GLN D 2 3   ? 46.273  12.215  -16.084 1.00 59.07 ?  3   GLN D CD  1 
ATOM   5896 O OE1 . GLN D 2 3   ? 46.896  12.741  -17.007 1.00 60.23 ?  3   GLN D OE1 1 
ATOM   5897 N NE2 . GLN D 2 3   ? 46.751  11.187  -15.391 1.00 56.88 ?  3   GLN D NE2 1 
ATOM   5898 N N   . LEU D 2 4   ? 42.003  11.305  -14.773 1.00 46.01 ?  4   LEU D N   1 
ATOM   5899 C CA  . LEU D 2 4   ? 41.537  11.206  -13.397 1.00 44.48 ?  4   LEU D CA  1 
ATOM   5900 C C   . LEU D 2 4   ? 42.699  10.760  -12.521 1.00 46.66 ?  4   LEU D C   1 
ATOM   5901 O O   . LEU D 2 4   ? 43.336  9.738   -12.801 1.00 46.35 ?  4   LEU D O   1 
ATOM   5902 C CB  . LEU D 2 4   ? 40.362  10.232  -13.278 1.00 43.05 ?  4   LEU D CB  1 
ATOM   5903 C CG  . LEU D 2 4   ? 38.978  10.889  -13.262 1.00 45.62 ?  4   LEU D CG  1 
ATOM   5904 C CD1 . LEU D 2 4   ? 37.898  9.897   -12.855 1.00 38.64 ?  4   LEU D CD1 1 
ATOM   5905 C CD2 . LEU D 2 4   ? 38.967  12.107  -12.354 1.00 46.33 ?  4   LEU D CD2 1 
ATOM   5906 N N   . GLN D 2 5   ? 42.968  11.524  -11.463 1.00 43.71 ?  5   GLN D N   1 
ATOM   5907 C CA  . GLN D 2 5   ? 44.170  11.366  -10.648 1.00 44.68 ?  5   GLN D CA  1 
ATOM   5908 C C   . GLN D 2 5   ? 43.772  11.376  -9.178  1.00 41.12 ?  5   GLN D C   1 
ATOM   5909 O O   . GLN D 2 5   ? 43.380  12.421  -8.648  1.00 42.37 ?  5   GLN D O   1 
ATOM   5910 C CB  . GLN D 2 5   ? 45.169  12.484  -10.950 1.00 47.84 ?  5   GLN D CB  1 
ATOM   5911 C CG  . GLN D 2 5   ? 46.513  12.375  -10.250 1.00 48.20 ?  5   GLN D CG  1 
ATOM   5912 C CD  . GLN D 2 5   ? 47.277  11.124  -10.622 1.00 57.21 ?  5   GLN D CD  1 
ATOM   5913 O OE1 . GLN D 2 5   ? 47.023  10.044  -10.091 1.00 59.28 ?  5   GLN D OE1 1 
ATOM   5914 N NE2 . GLN D 2 5   ? 48.215  11.261  -11.552 1.00 60.69 ?  5   GLN D NE2 1 
ATOM   5915 N N   . GLU D 2 6   ? 43.876  10.224  -8.519  1.00 37.97 ?  6   GLU D N   1 
ATOM   5916 C CA  . GLU D 2 6   ? 43.511  10.094  -7.117  1.00 40.66 ?  6   GLU D CA  1 
ATOM   5917 C C   . GLU D 2 6   ? 44.754  9.929   -6.249  1.00 39.51 ?  6   GLU D C   1 
ATOM   5918 O O   . GLU D 2 6   ? 45.745  9.317   -6.660  1.00 37.88 ?  6   GLU D O   1 
ATOM   5919 C CB  . GLU D 2 6   ? 42.555  8.915   -6.891  1.00 40.97 ?  6   GLU D CB  1 
ATOM   5920 C CG  . GLU D 2 6   ? 43.082  7.561   -7.334  1.00 40.56 ?  6   GLU D CG  1 
ATOM   5921 C CD  . GLU D 2 6   ? 42.810  7.283   -8.796  1.00 40.95 ?  6   GLU D CD  1 
ATOM   5922 O OE1 . GLU D 2 6   ? 41.709  6.781   -9.108  1.00 37.57 ?  6   GLU D OE1 1 
ATOM   5923 O OE2 . GLU D 2 6   ? 43.698  7.557   -9.630  1.00 42.61 ?  6   GLU D OE2 1 
ATOM   5924 N N   . SER D 2 7   ? 44.683  10.477  -5.037  1.00 36.40 ?  7   SER D N   1 
ATOM   5925 C CA  . SER D 2 7   ? 45.829  10.547  -4.142  1.00 36.25 ?  7   SER D CA  1 
ATOM   5926 C C   . SER D 2 7   ? 45.376  10.364  -2.700  1.00 39.35 ?  7   SER D C   1 
ATOM   5927 O O   . SER D 2 7   ? 44.187  10.450  -2.381  1.00 37.73 ?  7   SER D O   1 
ATOM   5928 C CB  . SER D 2 7   ? 46.567  11.885  -4.286  1.00 34.58 ?  7   SER D CB  1 
ATOM   5929 O OG  . SER D 2 7   ? 45.772  12.959  -3.807  1.00 34.08 ?  7   SER D OG  1 
ATOM   5930 N N   . GLY D 2 8   ? 46.349  10.114  -1.827  1.00 38.37 ?  8   GLY D N   1 
ATOM   5931 C CA  . GLY D 2 8   ? 46.119  10.073  -0.398  1.00 34.77 ?  8   GLY D CA  1 
ATOM   5932 C C   . GLY D 2 8   ? 46.103  8.697   0.242   1.00 37.72 ?  8   GLY D C   1 
ATOM   5933 O O   . GLY D 2 8   ? 45.646  8.585   1.389   1.00 39.14 ?  8   GLY D O   1 
ATOM   5934 N N   . GLY D 2 9   ? 46.580  7.666   -0.436  1.00 37.35 ?  9   GLY D N   1 
ATOM   5935 C CA  . GLY D 2 9   ? 46.559  6.317   0.090   1.00 42.30 ?  9   GLY D CA  1 
ATOM   5936 C C   . GLY D 2 9   ? 47.888  5.909   0.687   1.00 38.25 ?  9   GLY D C   1 
ATOM   5937 O O   . GLY D 2 9   ? 48.897  5.820   -0.017  1.00 44.87 ?  9   GLY D O   1 
ATOM   5938 N N   . GLY D 2 10  ? 47.883  5.646   1.992   1.00 37.75 ?  10  GLY D N   1 
ATOM   5939 C CA  . GLY D 2 10  ? 49.072  5.174   2.673   1.00 37.07 ?  10  GLY D CA  1 
ATOM   5940 C C   . GLY D 2 10  ? 48.858  3.847   3.371   1.00 39.78 ?  10  GLY D C   1 
ATOM   5941 O O   . GLY D 2 10  ? 47.948  3.092   3.016   1.00 39.71 ?  10  GLY D O   1 
ATOM   5942 N N   . LEU D 2 11  ? 49.701  3.542   4.352   1.00 40.23 ?  11  LEU D N   1 
ATOM   5943 C CA  . LEU D 2 11  ? 49.507  2.393   5.223   1.00 39.96 ?  11  LEU D CA  1 
ATOM   5944 C C   . LEU D 2 11  ? 48.974  2.878   6.563   1.00 41.49 ?  11  LEU D C   1 
ATOM   5945 O O   . LEU D 2 11  ? 49.386  3.929   7.062   1.00 43.82 ?  11  LEU D O   1 
ATOM   5946 C CB  . LEU D 2 11  ? 50.810  1.615   5.420   1.00 37.86 ?  11  LEU D CB  1 
ATOM   5947 C CG  . LEU D 2 11  ? 50.668  0.230   6.060   1.00 40.52 ?  11  LEU D CG  1 
ATOM   5948 C CD1 . LEU D 2 11  ? 51.596  -0.771  5.388   1.00 46.88 ?  11  LEU D CD1 1 
ATOM   5949 C CD2 . LEU D 2 11  ? 50.931  0.284   7.560   1.00 44.51 ?  11  LEU D CD2 1 
ATOM   5950 N N   . VAL D 2 12  ? 48.050  2.111   7.143   1.00 38.97 ?  12  VAL D N   1 
ATOM   5951 C CA  . VAL D 2 12  ? 47.364  2.524   8.359   1.00 44.83 ?  12  VAL D CA  1 
ATOM   5952 C C   . VAL D 2 12  ? 47.161  1.324   9.274   1.00 45.78 ?  12  VAL D C   1 
ATOM   5953 O O   . VAL D 2 12  ? 47.174  0.168   8.844   1.00 45.41 ?  12  VAL D O   1 
ATOM   5954 C CB  . VAL D 2 12  ? 46.006  3.201   8.052   1.00 40.21 ?  12  VAL D CB  1 
ATOM   5955 C CG1 . VAL D 2 12  ? 44.904  2.161   7.918   1.00 40.64 ?  12  VAL D CG1 1 
ATOM   5956 C CG2 . VAL D 2 12  ? 45.661  4.230   9.123   1.00 44.71 ?  12  VAL D CG2 1 
ATOM   5957 N N   . GLN D 2 13  ? 46.990  1.624   10.558  1.00 45.54 ?  13  GLN D N   1 
ATOM   5958 C CA  . GLN D 2 13  ? 46.598  0.630   11.541  1.00 46.56 ?  13  GLN D CA  1 
ATOM   5959 C C   . GLN D 2 13  ? 45.093  0.406   11.480  1.00 43.83 ?  13  GLN D C   1 
ATOM   5960 O O   . GLN D 2 13  ? 44.329  1.292   11.084  1.00 43.64 ?  13  GLN D O   1 
ATOM   5961 C CB  . GLN D 2 13  ? 46.998  1.081   12.946  1.00 53.37 ?  13  GLN D CB  1 
ATOM   5962 C CG  . GLN D 2 13  ? 48.445  0.806   13.311  1.00 54.01 ?  13  GLN D CG  1 
ATOM   5963 C CD  . GLN D 2 13  ? 48.680  -0.638  13.700  1.00 56.48 ?  13  GLN D CD  1 
ATOM   5964 O OE1 . GLN D 2 13  ? 48.989  -1.479  12.855  1.00 57.03 ?  13  GLN D OE1 1 
ATOM   5965 N NE2 . GLN D 2 13  ? 48.527  -0.936  14.985  1.00 55.12 ?  13  GLN D NE2 1 
ATOM   5966 N N   . ALA D 2 14  ? 44.672  -0.796  11.871  1.00 43.17 ?  14  ALA D N   1 
ATOM   5967 C CA  . ALA D 2 14  ? 43.249  -1.090  11.971  1.00 42.26 ?  14  ALA D CA  1 
ATOM   5968 C C   . ALA D 2 14  ? 42.573  -0.088  12.897  1.00 42.12 ?  14  ALA D C   1 
ATOM   5969 O O   . ALA D 2 14  ? 43.080  0.223   13.977  1.00 43.61 ?  14  ALA D O   1 
ATOM   5970 C CB  . ALA D 2 14  ? 43.034  -2.516  12.481  1.00 38.44 ?  14  ALA D CB  1 
ATOM   5971 N N   . GLY D 2 15  ? 41.430  0.429   12.459  1.00 44.09 ?  15  GLY D N   1 
ATOM   5972 C CA  . GLY D 2 15  ? 40.758  1.479   13.194  1.00 40.05 ?  15  GLY D CA  1 
ATOM   5973 C C   . GLY D 2 15  ? 41.239  2.877   12.885  1.00 43.99 ?  15  GLY D C   1 
ATOM   5974 O O   . GLY D 2 15  ? 40.795  3.827   13.541  1.00 43.79 ?  15  GLY D O   1 
ATOM   5975 N N   . GLY D 2 16  ? 42.131  3.038   11.902  1.00 41.09 ?  16  GLY D N   1 
ATOM   5976 C CA  . GLY D 2 16  ? 42.674  4.335   11.565  1.00 39.42 ?  16  GLY D CA  1 
ATOM   5977 C C   . GLY D 2 16  ? 41.810  5.097   10.576  1.00 43.36 ?  16  GLY D C   1 
ATOM   5978 O O   . GLY D 2 16  ? 40.716  4.680   10.199  1.00 39.96 ?  16  GLY D O   1 
ATOM   5979 N N   . SER D 2 17  ? 42.329  6.246   10.151  1.00 45.09 ?  17  SER D N   1 
ATOM   5980 C CA  . SER D 2 17  ? 41.622  7.128   9.235   1.00 40.75 ?  17  SER D CA  1 
ATOM   5981 C C   . SER D 2 17  ? 42.499  7.438   8.030   1.00 39.64 ?  17  SER D C   1 
ATOM   5982 O O   . SER D 2 17  ? 43.720  7.262   8.058   1.00 40.39 ?  17  SER D O   1 
ATOM   5983 C CB  . SER D 2 17  ? 41.196  8.435   9.923   1.00 37.98 ?  17  SER D CB  1 
ATOM   5984 O OG  . SER D 2 17  ? 40.085  8.228   10.781  1.00 42.38 ?  17  SER D OG  1 
ATOM   5985 N N   . LEU D 2 18  ? 41.851  7.909   6.966   1.00 37.44 ?  18  LEU D N   1 
ATOM   5986 C CA  . LEU D 2 18  ? 42.520  8.226   5.712   1.00 38.13 ?  18  LEU D CA  1 
ATOM   5987 C C   . LEU D 2 18  ? 41.595  9.110   4.888   1.00 38.43 ?  18  LEU D C   1 
ATOM   5988 O O   . LEU D 2 18  ? 40.380  8.907   4.888   1.00 37.42 ?  18  LEU D O   1 
ATOM   5989 C CB  . LEU D 2 18  ? 42.879  6.955   4.933   1.00 36.25 ?  18  LEU D CB  1 
ATOM   5990 C CG  . LEU D 2 18  ? 44.332  6.471   4.963   1.00 39.37 ?  18  LEU D CG  1 
ATOM   5991 C CD1 . LEU D 2 18  ? 44.609  5.554   3.783   1.00 39.22 ?  18  LEU D CD1 1 
ATOM   5992 C CD2 . LEU D 2 18  ? 45.300  7.642   4.970   1.00 34.82 ?  18  LEU D CD2 1 
ATOM   5993 N N   . ASN D 2 19  ? 42.171  10.084  4.189   1.00 36.55 ?  19  ASN D N   1 
ATOM   5994 C CA  . ASN D 2 19  ? 41.400  11.038  3.394   1.00 37.38 ?  19  ASN D CA  1 
ATOM   5995 C C   . ASN D 2 19  ? 41.871  10.968  1.945   1.00 36.04 ?  19  ASN D C   1 
ATOM   5996 O O   . ASN D 2 19  ? 42.920  11.519  1.598   1.00 36.72 ?  19  ASN D O   1 
ATOM   5997 C CB  . ASN D 2 19  ? 41.531  12.450  3.957   1.00 35.71 ?  19  ASN D CB  1 
ATOM   5998 C CG  . ASN D 2 19  ? 40.723  12.648  5.224   1.00 40.35 ?  19  ASN D CG  1 
ATOM   5999 O OD1 . ASN D 2 19  ? 39.619  12.119  5.359   1.00 37.61 ?  19  ASN D OD1 1 
ATOM   6000 N ND2 . ASN D 2 19  ? 41.269  13.414  6.161   1.00 42.26 ?  19  ASN D ND2 1 
ATOM   6001 N N   . LEU D 2 20  ? 41.092  10.296  1.102   1.00 34.20 ?  20  LEU D N   1 
ATOM   6002 C CA  . LEU D 2 20  ? 41.416  10.194  -0.312  1.00 36.36 ?  20  LEU D CA  1 
ATOM   6003 C C   . LEU D 2 20  ? 40.906  11.411  -1.073  1.00 37.46 ?  20  LEU D C   1 
ATOM   6004 O O   . LEU D 2 20  ? 39.888  12.013  -0.721  1.00 36.63 ?  20  LEU D O   1 
ATOM   6005 C CB  . LEU D 2 20  ? 40.815  8.925   -0.917  1.00 33.45 ?  20  LEU D CB  1 
ATOM   6006 C CG  . LEU D 2 20  ? 41.346  7.590   -0.394  1.00 33.88 ?  20  LEU D CG  1 
ATOM   6007 C CD1 . LEU D 2 20  ? 40.852  6.442   -1.260  1.00 32.84 ?  20  LEU D CD1 1 
ATOM   6008 C CD2 . LEU D 2 20  ? 42.863  7.597   -0.318  1.00 36.33 ?  20  LEU D CD2 1 
ATOM   6009 N N   . ALA D 2 21  ? 41.631  11.767  -2.129  1.00 35.33 ?  21  ALA D N   1 
ATOM   6010 C CA  . ALA D 2 21  ? 41.260  12.865  -3.005  1.00 36.59 ?  21  ALA D CA  1 
ATOM   6011 C C   . ALA D 2 21  ? 41.354  12.400  -4.450  1.00 36.69 ?  21  ALA D C   1 
ATOM   6012 O O   . ALA D 2 21  ? 42.063  11.444  -4.769  1.00 36.27 ?  21  ALA D O   1 
ATOM   6013 C CB  . ALA D 2 21  ? 42.152  14.094  -2.783  1.00 34.89 ?  21  ALA D CB  1 
ATOM   6014 N N   . CYS D 2 22  ? 40.621  13.085  -5.324  1.00 35.14 ?  22  CYS D N   1 
ATOM   6015 C CA  . CYS D 2 22  ? 40.614  12.778  -6.749  1.00 37.38 ?  22  CYS D CA  1 
ATOM   6016 C C   . CYS D 2 22  ? 40.475  14.072  -7.533  1.00 34.25 ?  22  CYS D C   1 
ATOM   6017 O O   . CYS D 2 22  ? 39.549  14.847  -7.286  1.00 30.53 ?  22  CYS D O   1 
ATOM   6018 C CB  . CYS D 2 22  ? 39.473  11.819  -7.109  1.00 34.57 ?  22  CYS D CB  1 
ATOM   6019 S SG  . CYS D 2 22  ? 39.062  11.814  -8.868  1.00 45.51 ?  22  CYS D SG  1 
ATOM   6020 N N   . VAL D 2 23  ? 41.385  14.299  -8.478  1.00 35.57 ?  23  VAL D N   1 
ATOM   6021 C CA  . VAL D 2 23  ? 41.423  15.528  -9.263  1.00 40.84 ?  23  VAL D CA  1 
ATOM   6022 C C   . VAL D 2 23  ? 41.152  15.185  -10.721 1.00 37.62 ?  23  VAL D C   1 
ATOM   6023 O O   . VAL D 2 23  ? 41.812  14.307  -11.290 1.00 38.58 ?  23  VAL D O   1 
ATOM   6024 C CB  . VAL D 2 23  ? 42.772  16.255  -9.117  1.00 38.55 ?  23  VAL D CB  1 
ATOM   6025 C CG1 . VAL D 2 23  ? 42.648  17.697  -9.582  1.00 34.75 ?  23  VAL D CG1 1 
ATOM   6026 C CG2 . VAL D 2 23  ? 43.255  16.193  -7.676  1.00 37.06 ?  23  VAL D CG2 1 
ATOM   6027 N N   . SER D 2 24  ? 40.192  15.882  -11.324 1.00 36.68 ?  24  SER D N   1 
ATOM   6028 C CA  . SER D 2 24  ? 39.814  15.664  -12.714 1.00 42.07 ?  24  SER D CA  1 
ATOM   6029 C C   . SER D 2 24  ? 40.501  16.693  -13.602 1.00 39.15 ?  24  SER D C   1 
ATOM   6030 O O   . SER D 2 24  ? 40.513  17.886  -13.281 1.00 35.15 ?  24  SER D O   1 
ATOM   6031 C CB  . SER D 2 24  ? 38.296  15.747  -12.886 1.00 39.15 ?  24  SER D CB  1 
ATOM   6032 O OG  . SER D 2 24  ? 37.758  16.850  -12.176 1.00 39.27 ?  24  SER D OG  1 
ATOM   6033 N N   . SER D 2 25  ? 41.065  16.231  -14.717 1.00 43.86 ?  25  SER D N   1 
ATOM   6034 C CA  . SER D 2 25  ? 41.782  17.091  -15.647 1.00 46.02 ?  25  SER D CA  1 
ATOM   6035 C C   . SER D 2 25  ? 41.286  16.853  -17.067 1.00 47.53 ?  25  SER D C   1 
ATOM   6036 O O   . SER D 2 25  ? 40.733  15.798  -17.387 1.00 49.20 ?  25  SER D O   1 
ATOM   6037 C CB  . SER D 2 25  ? 43.297  16.846  -15.587 1.00 46.61 ?  25  SER D CB  1 
ATOM   6038 O OG  . SER D 2 25  ? 43.686  16.356  -14.317 1.00 48.03 ?  25  SER D OG  1 
ATOM   6039 N N   . GLY D 2 26  ? 41.495  17.853  -17.922 1.00 51.21 ?  26  GLY D N   1 
ATOM   6040 C CA  . GLY D 2 26  ? 41.239  17.701  -19.342 1.00 53.02 ?  26  GLY D CA  1 
ATOM   6041 C C   . GLY D 2 26  ? 39.839  18.069  -19.791 1.00 52.87 ?  26  GLY D C   1 
ATOM   6042 O O   . GLY D 2 26  ? 39.227  18.992  -19.245 1.00 57.48 ?  26  GLY D O   1 
ATOM   6043 N N   . ARG D 2 27  ? 39.324  17.348  -20.791 1.00 49.43 ?  27  ARG D N   1 
ATOM   6044 C CA  . ARG D 2 27  ? 38.007  17.622  -21.358 1.00 51.92 ?  27  ARG D CA  1 
ATOM   6045 C C   . ARG D 2 27  ? 36.892  17.125  -20.455 1.00 46.98 ?  27  ARG D C   1 
ATOM   6046 O O   . ARG D 2 27  ? 36.005  16.396  -20.913 1.00 48.61 ?  27  ARG D O   1 
ATOM   6047 C CB  . ARG D 2 27  ? 37.829  16.948  -22.718 1.00 56.90 ?  27  ARG D CB  1 
ATOM   6048 C CG  . ARG D 2 27  ? 39.081  16.714  -23.502 1.00 54.60 ?  27  ARG D CG  1 
ATOM   6049 C CD  . ARG D 2 27  ? 38.737  16.559  -24.965 1.00 56.79 ?  27  ARG D CD  1 
ATOM   6050 N NE  . ARG D 2 27  ? 39.874  16.900  -25.802 1.00 59.72 ?  27  ARG D NE  1 
ATOM   6051 C CZ  . ARG D 2 27  ? 40.145  18.132  -26.200 1.00 62.00 ?  27  ARG D CZ  1 
ATOM   6052 N NH1 . ARG D 2 27  ? 39.365  19.149  -25.867 1.00 57.07 ?  27  ARG D NH1 1 
ATOM   6053 N NH2 . ARG D 2 27  ? 41.237  18.352  -26.925 1.00 58.64 ?  27  ARG D NH2 1 
ATOM   6054 N N   . THR D 2 28  ? 36.924  17.483  -19.180 1.00 46.08 ?  28  THR D N   1 
ATOM   6055 C CA  . THR D 2 28  ? 35.828  17.069  -18.327 1.00 44.84 ?  28  THR D CA  1 
ATOM   6056 C C   . THR D 2 28  ? 34.602  17.932  -18.603 1.00 41.31 ?  28  THR D C   1 
ATOM   6057 O O   . THR D 2 28  ? 34.672  18.974  -19.263 1.00 45.72 ?  28  THR D O   1 
ATOM   6058 C CB  . THR D 2 28  ? 36.221  17.151  -16.853 1.00 41.92 ?  28  THR D CB  1 
ATOM   6059 O OG1 . THR D 2 28  ? 36.071  18.498  -16.391 1.00 46.32 ?  28  THR D OG1 1 
ATOM   6060 C CG2 . THR D 2 28  ? 37.663  16.697  -16.652 1.00 43.11 ?  28  THR D CG2 1 
ATOM   6061 N N   . PHE D 2 29  ? 33.461  17.474  -18.102 1.00 37.77 ?  29  PHE D N   1 
ATOM   6062 C CA  . PHE D 2 29  ? 32.232  18.250  -18.128 1.00 34.28 ?  29  PHE D CA  1 
ATOM   6063 C C   . PHE D 2 29  ? 31.665  18.268  -16.717 1.00 32.39 ?  29  PHE D C   1 
ATOM   6064 O O   . PHE D 2 29  ? 31.565  17.218  -16.074 1.00 31.82 ?  29  PHE D O   1 
ATOM   6065 C CB  . PHE D 2 29  ? 31.224  17.671  -19.124 1.00 30.66 ?  29  PHE D CB  1 
ATOM   6066 C CG  . PHE D 2 29  ? 30.208  18.667  -19.599 1.00 29.20 ?  29  PHE D CG  1 
ATOM   6067 C CD1 . PHE D 2 29  ? 30.511  19.553  -20.620 1.00 28.10 ?  29  PHE D CD1 1 
ATOM   6068 C CD2 . PHE D 2 29  ? 28.952  18.720  -19.025 1.00 29.30 ?  29  PHE D CD2 1 
ATOM   6069 C CE1 . PHE D 2 29  ? 29.577  20.473  -21.057 1.00 25.14 ?  29  PHE D CE1 1 
ATOM   6070 C CE2 . PHE D 2 29  ? 28.013  19.636  -19.457 1.00 27.80 ?  29  PHE D CE2 1 
ATOM   6071 C CZ  . PHE D 2 29  ? 28.326  20.514  -20.475 1.00 27.92 ?  29  PHE D CZ  1 
ATOM   6072 N N   . SER D 2 30  ? 31.294  19.460  -16.244 1.00 28.67 ?  30  SER D N   1 
ATOM   6073 C CA  . SER D 2 30  ? 30.987  19.684  -14.833 1.00 32.09 ?  30  SER D CA  1 
ATOM   6074 C C   . SER D 2 30  ? 29.836  18.836  -14.303 1.00 30.23 ?  30  SER D C   1 
ATOM   6075 O O   . SER D 2 30  ? 29.697  18.721  -13.081 1.00 29.87 ?  30  SER D O   1 
ATOM   6076 C CB  . SER D 2 30  ? 30.661  21.163  -14.602 1.00 28.45 ?  30  SER D CB  1 
ATOM   6077 O OG  . SER D 2 30  ? 29.540  21.569  -15.370 1.00 35.64 ?  30  SER D OG  1 
ATOM   6078 N N   . THR D 2 31  ? 29.016  18.240  -15.169 1.00 30.41 ?  31  THR D N   1 
ATOM   6079 C CA  . THR D 2 31  ? 27.755  17.637  -14.751 1.00 28.87 ?  31  THR D CA  1 
ATOM   6080 C C   . THR D 2 31  ? 27.780  16.112  -14.704 1.00 25.78 ?  31  THR D C   1 
ATOM   6081 O O   . THR D 2 31  ? 26.749  15.501  -14.397 1.00 25.74 ?  31  THR D O   1 
ATOM   6082 C CB  . THR D 2 31  ? 26.622  18.121  -15.673 1.00 25.87 ?  31  THR D CB  1 
ATOM   6083 O OG1 . THR D 2 31  ? 25.358  18.004  -15.007 1.00 32.41 ?  31  THR D OG1 1 
ATOM   6084 C CG2 . THR D 2 31  ? 26.591  17.329  -16.958 1.00 22.65 ?  31  THR D CG2 1 
ATOM   6085 N N   . TRP D 2 32  ? 28.922  15.480  -14.971 1.00 24.63 ?  32  TRP D N   1 
ATOM   6086 C CA  . TRP D 2 32  ? 28.995  14.024  -14.955 1.00 24.49 ?  32  TRP D CA  1 
ATOM   6087 C C   . TRP D 2 32  ? 28.808  13.471  -13.544 1.00 26.32 ?  32  TRP D C   1 
ATOM   6088 O O   . TRP D 2 32  ? 29.212  14.083  -12.551 1.00 28.07 ?  32  TRP D O   1 
ATOM   6089 C CB  . TRP D 2 32  ? 30.340  13.543  -15.503 1.00 24.19 ?  32  TRP D CB  1 
ATOM   6090 C CG  . TRP D 2 32  ? 30.565  13.837  -16.951 1.00 29.47 ?  32  TRP D CG  1 
ATOM   6091 C CD1 . TRP D 2 32  ? 29.624  14.179  -17.877 1.00 27.51 ?  32  TRP D CD1 1 
ATOM   6092 C CD2 . TRP D 2 32  ? 31.817  13.802  -17.644 1.00 30.62 ?  32  TRP D CD2 1 
ATOM   6093 N NE1 . TRP D 2 32  ? 30.214  14.363  -19.104 1.00 27.06 ?  32  TRP D NE1 1 
ATOM   6094 C CE2 . TRP D 2 32  ? 31.560  14.138  -18.987 1.00 29.41 ?  32  TRP D CE2 1 
ATOM   6095 C CE3 . TRP D 2 32  ? 33.132  13.521  -17.258 1.00 28.65 ?  32  TRP D CE3 1 
ATOM   6096 C CZ2 . TRP D 2 32  ? 32.569  14.201  -19.947 1.00 31.30 ?  32  TRP D CZ2 1 
ATOM   6097 C CZ3 . TRP D 2 32  ? 34.131  13.585  -18.211 1.00 31.88 ?  32  TRP D CZ3 1 
ATOM   6098 C CH2 . TRP D 2 32  ? 33.844  13.923  -19.540 1.00 31.53 ?  32  TRP D CH2 1 
ATOM   6099 N N   . LEU D 2 33  ? 28.193  12.293  -13.468 1.00 25.55 ?  33  LEU D N   1 
ATOM   6100 C CA  . LEU D 2 33  ? 28.107  11.564  -12.210 1.00 25.11 ?  33  LEU D CA  1 
ATOM   6101 C C   . LEU D 2 33  ? 29.465  10.962  -11.865 1.00 27.30 ?  33  LEU D C   1 
ATOM   6102 O O   . LEU D 2 33  ? 30.201  10.512  -12.747 1.00 28.13 ?  33  LEU D O   1 
ATOM   6103 C CB  . LEU D 2 33  ? 27.049  10.464  -12.312 1.00 23.89 ?  33  LEU D CB  1 
ATOM   6104 C CG  . LEU D 2 33  ? 26.845  9.522   -11.123 1.00 27.72 ?  33  LEU D CG  1 
ATOM   6105 C CD1 . LEU D 2 33  ? 26.244  10.261  -9.936  1.00 22.88 ?  33  LEU D CD1 1 
ATOM   6106 C CD2 . LEU D 2 33  ? 25.973  8.340   -11.525 1.00 21.89 ?  33  LEU D CD2 1 
ATOM   6107 N N   . MET D 2 34  ? 29.799  10.953  -10.575 1.00 25.94 ?  34  MET D N   1 
ATOM   6108 C CA  . MET D 2 34  ? 31.104  10.498  -10.116 1.00 27.24 ?  34  MET D CA  1 
ATOM   6109 C C   . MET D 2 34  ? 30.940  9.544   -8.939  1.00 28.70 ?  34  MET D C   1 
ATOM   6110 O O   . MET D 2 34  ? 29.916  9.542   -8.252  1.00 30.23 ?  34  MET D O   1 
ATOM   6111 C CB  . MET D 2 34  ? 31.994  11.682  -9.715  1.00 27.05 ?  34  MET D CB  1 
ATOM   6112 C CG  . MET D 2 34  ? 32.754  12.299  -10.876 1.00 30.18 ?  34  MET D CG  1 
ATOM   6113 S SD  . MET D 2 34  ? 33.839  13.654  -10.392 1.00 36.11 ?  34  MET D SD  1 
ATOM   6114 C CE  . MET D 2 34  ? 35.323  12.754  -9.957  1.00 36.28 ?  34  MET D CE  1 
ATOM   6115 N N   . GLY D 2 35  ? 31.970  8.733   -8.709  1.00 28.49 ?  35  GLY D N   1 
ATOM   6116 C CA  . GLY D 2 35  ? 31.923  7.770   -7.622  1.00 28.13 ?  35  GLY D CA  1 
ATOM   6117 C C   . GLY D 2 35  ? 33.274  7.138   -7.369  1.00 30.16 ?  35  GLY D C   1 
ATOM   6118 O O   . GLY D 2 35  ? 34.216  7.289   -8.152  1.00 31.68 ?  35  GLY D O   1 
ATOM   6119 N N   . TRP D 2 36  ? 33.350  6.419   -6.250  1.00 28.86 ?  36  TRP D N   1 
ATOM   6120 C CA  . TRP D 2 36  ? 34.550  5.710   -5.827  1.00 29.11 ?  36  TRP D CA  1 
ATOM   6121 C C   . TRP D 2 36  ? 34.323  4.205   -5.905  1.00 25.68 ?  36  TRP D C   1 
ATOM   6122 O O   . TRP D 2 36  ? 33.254  3.710   -5.532  1.00 25.31 ?  36  TRP D O   1 
ATOM   6123 C CB  . TRP D 2 36  ? 34.944  6.084   -4.393  1.00 28.18 ?  36  TRP D CB  1 
ATOM   6124 C CG  . TRP D 2 36  ? 35.537  7.454   -4.223  1.00 30.04 ?  36  TRP D CG  1 
ATOM   6125 C CD1 . TRP D 2 36  ? 34.883  8.585   -3.832  1.00 30.64 ?  36  TRP D CD1 1 
ATOM   6126 C CD2 . TRP D 2 36  ? 36.909  7.828   -4.409  1.00 32.78 ?  36  TRP D CD2 1 
ATOM   6127 N NE1 . TRP D 2 36  ? 35.758  9.643   -3.775  1.00 30.15 ?  36  TRP D NE1 1 
ATOM   6128 C CE2 . TRP D 2 36  ? 37.008  9.204   -4.124  1.00 31.65 ?  36  TRP D CE2 1 
ATOM   6129 C CE3 . TRP D 2 36  ? 38.060  7.134   -4.794  1.00 30.86 ?  36  TRP D CE3 1 
ATOM   6130 C CZ2 . TRP D 2 36  ? 38.212  9.901   -4.213  1.00 32.72 ?  36  TRP D CZ2 1 
ATOM   6131 C CZ3 . TRP D 2 36  ? 39.255  7.827   -4.882  1.00 31.80 ?  36  TRP D CZ3 1 
ATOM   6132 C CH2 . TRP D 2 36  ? 39.321  9.196   -4.593  1.00 33.25 ?  36  TRP D CH2 1 
ATOM   6133 N N   . PHE D 2 37  ? 35.333  3.483   -6.385  1.00 29.22 ?  37  PHE D N   1 
ATOM   6134 C CA  . PHE D 2 37  ? 35.333  2.027   -6.418  1.00 31.17 ?  37  PHE D CA  1 
ATOM   6135 C C   . PHE D 2 37  ? 36.631  1.520   -5.804  1.00 33.58 ?  37  PHE D C   1 
ATOM   6136 O O   . PHE D 2 37  ? 37.559  2.289   -5.540  1.00 32.71 ?  37  PHE D O   1 
ATOM   6137 C CB  . PHE D 2 37  ? 35.179  1.481   -7.847  1.00 32.11 ?  37  PHE D CB  1 
ATOM   6138 C CG  . PHE D 2 37  ? 33.876  1.841   -8.511  1.00 31.58 ?  37  PHE D CG  1 
ATOM   6139 C CD1 . PHE D 2 37  ? 33.614  3.140   -8.915  1.00 28.23 ?  37  PHE D CD1 1 
ATOM   6140 C CD2 . PHE D 2 37  ? 32.913  0.871   -8.734  1.00 32.26 ?  37  PHE D CD2 1 
ATOM   6141 C CE1 . PHE D 2 37  ? 32.417  3.462   -9.524  1.00 27.20 ?  37  PHE D CE1 1 
ATOM   6142 C CE2 . PHE D 2 37  ? 31.716  1.187   -9.343  1.00 30.67 ?  37  PHE D CE2 1 
ATOM   6143 C CZ  . PHE D 2 37  ? 31.468  2.483   -9.737  1.00 28.75 ?  37  PHE D CZ  1 
ATOM   6144 N N   . ARG D 2 38  ? 36.700  0.208   -5.580  1.00 31.75 ?  38  ARG D N   1 
ATOM   6145 C CA  . ARG D 2 38  ? 37.911  -0.393  -5.041  1.00 36.99 ?  38  ARG D CA  1 
ATOM   6146 C C   . ARG D 2 38  ? 38.053  -1.822  -5.552  1.00 39.03 ?  38  ARG D C   1 
ATOM   6147 O O   . ARG D 2 38  ? 37.065  -2.473  -5.903  1.00 36.90 ?  38  ARG D O   1 
ATOM   6148 C CB  . ARG D 2 38  ? 37.930  -0.381  -3.507  1.00 33.84 ?  38  ARG D CB  1 
ATOM   6149 C CG  . ARG D 2 38  ? 36.959  -1.348  -2.844  1.00 35.31 ?  38  ARG D CG  1 
ATOM   6150 C CD  . ARG D 2 38  ? 36.838  -1.051  -1.356  1.00 36.13 ?  38  ARG D CD  1 
ATOM   6151 N NE  . ARG D 2 38  ? 35.865  -1.911  -0.693  1.00 36.07 ?  38  ARG D NE  1 
ATOM   6152 C CZ  . ARG D 2 38  ? 35.683  -1.961  0.620   1.00 37.13 ?  38  ARG D CZ  1 
ATOM   6153 N NH1 . ARG D 2 38  ? 36.398  -1.217  1.447   1.00 34.79 ?  38  ARG D NH1 1 
ATOM   6154 N NH2 . ARG D 2 38  ? 34.758  -2.778  1.115   1.00 38.20 ?  38  ARG D NH2 1 
ATOM   6155 N N   . GLN D 2 39  ? 39.299  -2.298  -5.591  1.00 38.08 ?  39  GLN D N   1 
ATOM   6156 C CA  . GLN D 2 39  ? 39.605  -3.651  -6.036  1.00 39.76 ?  39  GLN D CA  1 
ATOM   6157 C C   . GLN D 2 39  ? 40.767  -4.200  -5.235  1.00 42.74 ?  39  GLN D C   1 
ATOM   6158 O O   . GLN D 2 39  ? 41.852  -3.608  -5.215  1.00 40.31 ?  39  GLN D O   1 
ATOM   6159 C CB  . GLN D 2 39  ? 39.932  -3.700  -7.532  1.00 38.98 ?  39  GLN D CB  1 
ATOM   6160 C CG  . GLN D 2 39  ? 39.862  -5.106  -8.127  1.00 44.53 ?  39  GLN D CG  1 
ATOM   6161 C CD  . GLN D 2 39  ? 40.263  -5.148  -9.590  1.00 42.22 ?  39  GLN D CD  1 
ATOM   6162 O OE1 . GLN D 2 39  ? 41.131  -4.391  -10.033 1.00 42.92 ?  39  GLN D OE1 1 
ATOM   6163 N NE2 . GLN D 2 39  ? 39.632  -6.032  -10.349 1.00 42.88 ?  39  GLN D NE2 1 
ATOM   6164 N N   . ALA D 2 40  ? 40.543  -5.338  -4.580  1.00 44.68 ?  40  ALA D N   1 
ATOM   6165 C CA  . ALA D 2 40  ? 41.625  -6.115  -3.960  1.00 47.47 ?  40  ALA D CA  1 
ATOM   6166 C C   . ALA D 2 40  ? 42.177  -7.129  -4.937  1.00 50.46 ?  40  ALA D C   1 
ATOM   6167 O O   . ALA D 2 40  ? 41.428  -7.719  -5.746  1.00 51.27 ?  40  ALA D O   1 
ATOM   6168 C CB  . ALA D 2 40  ? 41.099  -6.858  -2.744  1.00 47.23 ?  40  ALA D CB  1 
ATOM   6169 N N   . PRO D 2 41  ? 43.459  -7.409  -4.781  1.00 53.86 ?  41  PRO D N   1 
ATOM   6170 C CA  . PRO D 2 41  ? 44.097  -8.412  -5.615  1.00 53.23 ?  41  PRO D CA  1 
ATOM   6171 C C   . PRO D 2 41  ? 43.298  -9.728  -5.613  1.00 54.82 ?  41  PRO D C   1 
ATOM   6172 O O   . PRO D 2 41  ? 42.919  -10.220 -4.550  1.00 52.38 ?  41  PRO D O   1 
ATOM   6173 C CB  . PRO D 2 41  ? 45.452  -8.615  -4.915  1.00 52.85 ?  41  PRO D CB  1 
ATOM   6174 C CG  . PRO D 2 41  ? 45.465  -7.384  -3.714  1.00 52.84 ?  41  PRO D CG  1 
ATOM   6175 C CD  . PRO D 2 41  ? 44.476  -6.463  -4.311  1.00 57.22 ?  41  PRO D CD  1 
ATOM   6176 N N   . GLY D 2 42  ? 42.967  -10.271 -6.814  1.00 53.32 ?  42  GLY D N   1 
ATOM   6177 C CA  . GLY D 2 42  ? 42.250  -11.542 -7.046  1.00 52.48 ?  42  GLY D CA  1 
ATOM   6178 C C   . GLY D 2 42  ? 40.748  -11.468 -6.924  1.00 51.67 ?  42  GLY D C   1 
ATOM   6179 O O   . GLY D 2 42  ? 40.070  -12.476 -7.165  1.00 52.42 ?  42  GLY D O   1 
ATOM   6180 N N   . LYS D 2 43  ? 40.212  -10.320 -6.546  1.00 51.79 ?  43  LYS D N   1 
ATOM   6181 C CA  . LYS D 2 43  ? 38.791  -10.140 -6.354  1.00 50.64 ?  43  LYS D CA  1 
ATOM   6182 C C   . LYS D 2 43  ? 38.248  -9.212  -7.428  1.00 53.20 ?  43  LYS D C   1 
ATOM   6183 O O   . LYS D 2 43  ? 38.991  -8.576  -8.185  1.00 51.22 ?  43  LYS D O   1 
ATOM   6184 C CB  . LYS D 2 43  ? 38.512  -9.585  -4.956  1.00 50.57 ?  43  LYS D CB  1 
ATOM   6185 C CG  . LYS D 2 43  ? 38.443  -10.650 -3.871  1.00 48.55 ?  43  LYS D CG  1 
ATOM   6186 C CD  . LYS D 2 43  ? 37.688  -10.151 -2.648  1.00 47.51 ?  43  LYS D CD  1 
ATOM   6187 C CE  . LYS D 2 43  ? 37.968  -11.016 -1.429  1.00 50.09 ?  43  LYS D CE  1 
ATOM   6188 N NZ  . LYS D 2 43  ? 36.716  -11.527 -0.805  1.00 50.00 ?  43  LYS D NZ  1 
ATOM   6189 N N   . GLU D 2 44  ? 36.926  -9.153  -7.487  1.00 50.04 ?  44  GLU D N   1 
ATOM   6190 C CA  . GLU D 2 44  ? 36.250  -8.280  -8.427  1.00 52.14 ?  44  GLU D CA  1 
ATOM   6191 C C   . GLU D 2 44  ? 36.184  -6.861  -7.879  1.00 47.01 ?  44  GLU D C   1 
ATOM   6192 O O   . GLU D 2 44  ? 36.148  -6.641  -6.664  1.00 48.19 ?  44  GLU D O   1 
ATOM   6193 C CB  . GLU D 2 44  ? 34.839  -8.794  -8.715  1.00 54.64 ?  44  GLU D CB  1 
ATOM   6194 C CG  . GLU D 2 44  ? 34.791  -10.046 -9.576  1.00 53.44 ?  44  GLU D CG  1 
ATOM   6195 C CD  . GLU D 2 44  ? 33.897  -9.884  -10.790 1.00 68.11 ?  44  GLU D CD  1 
ATOM   6196 O OE1 . GLU D 2 44  ? 32.745  -9.430  -10.627 1.00 70.38 ?  44  GLU D OE1 1 
ATOM   6197 O OE2 . GLU D 2 44  ? 34.347  -10.214 -11.909 1.00 68.67 ?  44  GLU D OE2 1 
ATOM   6198 N N   . ARG D 2 45  ? 36.178  -5.894  -8.791  1.00 43.78 ?  45  ARG D N   1 
ATOM   6199 C CA  . ARG D 2 45  ? 36.004  -4.504  -8.397  1.00 44.45 ?  45  ARG D CA  1 
ATOM   6200 C C   . ARG D 2 45  ? 34.607  -4.298  -7.829  1.00 43.33 ?  45  ARG D C   1 
ATOM   6201 O O   . ARG D 2 45  ? 33.627  -4.855  -8.332  1.00 44.93 ?  45  ARG D O   1 
ATOM   6202 C CB  . ARG D 2 45  ? 36.230  -3.576  -9.590  1.00 44.82 ?  45  ARG D CB  1 
ATOM   6203 C CG  . ARG D 2 45  ? 36.781  -2.211  -9.214  1.00 39.85 ?  45  ARG D CG  1 
ATOM   6204 C CD  . ARG D 2 45  ? 36.943  -1.325  -10.437 1.00 44.21 ?  45  ARG D CD  1 
ATOM   6205 N NE  . ARG D 2 45  ? 38.346  -1.118  -10.775 1.00 43.14 ?  45  ARG D NE  1 
ATOM   6206 C CZ  . ARG D 2 45  ? 38.926  -1.581  -11.874 1.00 46.76 ?  45  ARG D CZ  1 
ATOM   6207 N NH1 . ARG D 2 45  ? 38.249  -2.276  -12.773 1.00 49.82 ?  45  ARG D NH1 1 
ATOM   6208 N NH2 . ARG D 2 45  ? 40.219  -1.340  -12.075 1.00 46.25 ?  45  ARG D NH2 1 
ATOM   6209 N N   . GLU D 2 46  ? 34.515  -3.497  -6.770  1.00 36.50 ?  46  GLU D N   1 
ATOM   6210 C CA  . GLU D 2 46  ? 33.251  -3.290  -6.080  1.00 38.48 ?  46  GLU D CA  1 
ATOM   6211 C C   . GLU D 2 46  ? 33.008  -1.808  -5.831  1.00 32.63 ?  46  GLU D C   1 
ATOM   6212 O O   . GLU D 2 46  ? 33.941  -1.045  -5.563  1.00 31.98 ?  46  GLU D O   1 
ATOM   6213 C CB  . GLU D 2 46  ? 33.206  -4.062  -4.753  1.00 35.46 ?  46  GLU D CB  1 
ATOM   6214 C CG  . GLU D 2 46  ? 34.307  -3.712  -3.771  1.00 39.67 ?  46  GLU D CG  1 
ATOM   6215 C CD  . GLU D 2 46  ? 33.996  -4.190  -2.365  1.00 45.31 ?  46  GLU D CD  1 
ATOM   6216 O OE1 . GLU D 2 46  ? 33.304  -3.460  -1.625  1.00 43.46 ?  46  GLU D OE1 1 
ATOM   6217 O OE2 . GLU D 2 46  ? 34.443  -5.299  -2.001  1.00 51.45 ?  46  GLU D OE2 1 
ATOM   6218 N N   . PHE D 2 47  ? 31.739  -1.422  -5.926  1.00 30.55 ?  47  PHE D N   1 
ATOM   6219 C CA  . PHE D 2 47  ? 31.310  -0.049  -5.705  1.00 29.73 ?  47  PHE D CA  1 
ATOM   6220 C C   . PHE D 2 47  ? 31.503  0.349   -4.245  1.00 28.45 ?  47  PHE D C   1 
ATOM   6221 O O   . PHE D 2 47  ? 31.386  -0.470  -3.333  1.00 25.32 ?  47  PHE D O   1 
ATOM   6222 C CB  . PHE D 2 47  ? 29.843  0.090   -6.122  1.00 26.89 ?  47  PHE D CB  1 
ATOM   6223 C CG  . PHE D 2 47  ? 29.172  1.343   -5.639  1.00 26.65 ?  47  PHE D CG  1 
ATOM   6224 C CD1 . PHE D 2 47  ? 29.256  2.515   -6.371  1.00 27.21 ?  47  PHE D CD1 1 
ATOM   6225 C CD2 . PHE D 2 47  ? 28.422  1.338   -4.474  1.00 26.11 ?  47  PHE D CD2 1 
ATOM   6226 C CE1 . PHE D 2 47  ? 28.625  3.664   -5.937  1.00 26.66 ?  47  PHE D CE1 1 
ATOM   6227 C CE2 . PHE D 2 47  ? 27.790  2.484   -4.034  1.00 25.84 ?  47  PHE D CE2 1 
ATOM   6228 C CZ  . PHE D 2 47  ? 27.890  3.648   -4.767  1.00 25.66 ?  47  PHE D CZ  1 
ATOM   6229 N N   . VAL D 2 48  ? 31.810  1.626   -4.029  1.00 28.25 ?  48  VAL D N   1 
ATOM   6230 C CA  . VAL D 2 48  ? 32.034  2.131   -2.679  1.00 26.53 ?  48  VAL D CA  1 
ATOM   6231 C C   . VAL D 2 48  ? 31.065  3.269   -2.387  1.00 26.96 ?  48  VAL D C   1 
ATOM   6232 O O   . VAL D 2 48  ? 30.301  3.212   -1.417  1.00 29.41 ?  48  VAL D O   1 
ATOM   6233 C CB  . VAL D 2 48  ? 33.491  2.588   -2.478  1.00 26.55 ?  48  VAL D CB  1 
ATOM   6234 C CG1 . VAL D 2 48  ? 33.700  3.054   -1.050  1.00 25.20 ?  48  VAL D CG1 1 
ATOM   6235 C CG2 . VAL D 2 48  ? 34.452  1.456   -2.809  1.00 26.70 ?  48  VAL D CG2 1 
ATOM   6236 N N   . ALA D 2 49  ? 31.090  4.306   -3.223  1.00 25.36 ?  49  ALA D N   1 
ATOM   6237 C CA  . ALA D 2 49  ? 30.240  5.472   -3.017  1.00 24.68 ?  49  ALA D CA  1 
ATOM   6238 C C   . ALA D 2 49  ? 30.116  6.249   -4.322  1.00 25.13 ?  49  ALA D C   1 
ATOM   6239 O O   . ALA D 2 49  ? 30.905  6.066   -5.252  1.00 23.95 ?  49  ALA D O   1 
ATOM   6240 C CB  . ALA D 2 49  ? 30.786  6.372   -1.905  1.00 24.93 ?  49  ALA D CB  1 
ATOM   6241 N N   . SER D 2 50  ? 29.107  7.121   -4.375  1.00 22.73 ?  50  SER D N   1 
ATOM   6242 C CA  . SER D 2 50  ? 28.863  7.967   -5.537  1.00 24.01 ?  50  SER D CA  1 
ATOM   6243 C C   . SER D 2 50  ? 28.129  9.226   -5.094  1.00 24.46 ?  50  SER D C   1 
ATOM   6244 O O   . SER D 2 50  ? 27.475  9.253   -4.048  1.00 26.79 ?  50  SER D O   1 
ATOM   6245 C CB  . SER D 2 50  ? 28.062  7.230   -6.619  1.00 27.01 ?  50  SER D CB  1 
ATOM   6246 O OG  . SER D 2 50  ? 26.711  7.045   -6.230  1.00 28.80 ?  50  SER D OG  1 
ATOM   6247 N N   . ILE D 2 51  ? 28.244  10.273  -5.906  1.00 27.36 ?  51  ILE D N   1 
ATOM   6248 C CA  . ILE D 2 51  ? 27.665  11.569  -5.576  1.00 29.69 ?  51  ILE D CA  1 
ATOM   6249 C C   . ILE D 2 51  ? 27.533  12.375  -6.861  1.00 26.27 ?  51  ILE D C   1 
ATOM   6250 O O   . ILE D 2 51  ? 28.431  12.376  -7.707  1.00 27.87 ?  51  ILE D O   1 
ATOM   6251 C CB  . ILE D 2 51  ? 28.514  12.306  -4.510  1.00 29.36 ?  51  ILE D CB  1 
ATOM   6252 C CG1 . ILE D 2 51  ? 27.833  13.604  -4.068  1.00 28.09 ?  51  ILE D CG1 1 
ATOM   6253 C CG2 . ILE D 2 51  ? 29.926  12.577  -5.017  1.00 28.44 ?  51  ILE D CG2 1 
ATOM   6254 C CD1 . ILE D 2 51  ? 28.639  14.401  -3.061  1.00 29.72 ?  51  ILE D CD1 1 
ATOM   6255 N N   . ASP D 2 52  ? 26.393  13.046  -7.009  1.00 25.26 ?  52  ASP D N   1 
ATOM   6256 C CA  . ASP D 2 52  ? 26.132  13.847  -8.194  1.00 29.14 ?  52  ASP D CA  1 
ATOM   6257 C C   . ASP D 2 52  ? 26.945  15.140  -8.154  1.00 29.55 ?  52  ASP D C   1 
ATOM   6258 O O   . ASP D 2 52  ? 27.597  15.472  -7.160  1.00 29.47 ?  52  ASP D O   1 
ATOM   6259 C CB  . ASP D 2 52  ? 24.638  14.160  -8.313  1.00 28.59 ?  52  ASP D CB  1 
ATOM   6260 C CG  . ASP D 2 52  ? 24.059  14.760  -7.043  1.00 30.27 ?  52  ASP D CG  1 
ATOM   6261 O OD1 . ASP D 2 52  ? 23.710  13.992  -6.121  1.00 33.35 ?  52  ASP D OD1 1 
ATOM   6262 O OD2 . ASP D 2 52  ? 23.952  16.002  -6.967  1.00 26.55 ?  52  ASP D OD2 1 
ATOM   6263 N N   . TRP D 2 53  ? 26.892  15.881  -9.264  1.00 29.17 ?  53  TRP D N   1 
ATOM   6264 C CA  . TRP D 2 53  ? 27.660  17.115  -9.395  1.00 30.00 ?  53  TRP D CA  1 
ATOM   6265 C C   . TRP D 2 53  ? 27.166  18.227  -8.480  1.00 31.58 ?  53  TRP D C   1 
ATOM   6266 O O   . TRP D 2 53  ? 27.844  19.254  -8.364  1.00 34.99 ?  53  TRP D O   1 
ATOM   6267 C CB  . TRP D 2 53  ? 27.636  17.599  -10.847 1.00 28.08 ?  53  TRP D CB  1 
ATOM   6268 C CG  . TRP D 2 53  ? 26.349  18.260  -11.243 1.00 29.43 ?  53  TRP D CG  1 
ATOM   6269 C CD1 . TRP D 2 53  ? 25.106  17.697  -11.247 1.00 27.60 ?  53  TRP D CD1 1 
ATOM   6270 C CD2 . TRP D 2 53  ? 26.179  19.611  -11.690 1.00 30.59 ?  53  TRP D CD2 1 
ATOM   6271 N NE1 . TRP D 2 53  ? 24.173  18.613  -11.669 1.00 29.44 ?  53  TRP D NE1 1 
ATOM   6272 C CE2 . TRP D 2 53  ? 24.806  19.796  -11.947 1.00 30.83 ?  53  TRP D CE2 1 
ATOM   6273 C CE3 . TRP D 2 53  ? 27.054  20.682  -11.897 1.00 27.75 ?  53  TRP D CE3 1 
ATOM   6274 C CZ2 . TRP D 2 53  ? 24.287  21.008  -12.401 1.00 25.93 ?  53  TRP D CZ2 1 
ATOM   6275 C CZ3 . TRP D 2 53  ? 26.537  21.884  -12.349 1.00 30.53 ?  53  TRP D CZ3 1 
ATOM   6276 C CH2 . TRP D 2 53  ? 25.167  22.037  -12.595 1.00 27.42 ?  53  TRP D CH2 1 
ATOM   6277 N N   . ARG D 2 54  ? 26.015  18.055  -7.834  1.00 30.81 ?  54  ARG D N   1 
ATOM   6278 C CA  . ARG D 2 54  ? 25.458  19.064  -6.946  1.00 28.98 ?  54  ARG D CA  1 
ATOM   6279 C C   . ARG D 2 54  ? 25.450  18.637  -5.486  1.00 29.63 ?  54  ARG D C   1 
ATOM   6280 O O   . ARG D 2 54  ? 24.962  19.395  -4.640  1.00 32.27 ?  54  ARG D O   1 
ATOM   6281 C CB  . ARG D 2 54  ? 24.029  19.414  -7.375  1.00 30.64 ?  54  ARG D CB  1 
ATOM   6282 C CG  . ARG D 2 54  ? 23.932  20.348  -8.562  1.00 34.40 ?  54  ARG D CG  1 
ATOM   6283 C CD  . ARG D 2 54  ? 22.650  21.154  -8.482  1.00 33.29 ?  54  ARG D CD  1 
ATOM   6284 N NE  . ARG D 2 54  ? 21.541  20.477  -9.142  1.00 35.29 ?  54  ARG D NE  1 
ATOM   6285 C CZ  . ARG D 2 54  ? 20.435  20.080  -8.526  1.00 38.18 ?  54  ARG D CZ  1 
ATOM   6286 N NH1 . ARG D 2 54  ? 20.253  20.287  -7.231  1.00 35.99 ?  54  ARG D NH1 1 
ATOM   6287 N NH2 . ARG D 2 54  ? 19.490  19.458  -9.225  1.00 38.30 ?  54  ARG D NH2 1 
ATOM   6288 N N   . SER D 2 55  ? 25.968  17.448  -5.171  1.00 29.80 ?  55  SER D N   1 
ATOM   6289 C CA  . SER D 2 55  ? 25.916  16.886  -3.821  1.00 32.42 ?  55  SER D CA  1 
ATOM   6290 C C   . SER D 2 55  ? 24.479  16.767  -3.319  1.00 31.35 ?  55  SER D C   1 
ATOM   6291 O O   . SER D 2 55  ? 24.217  16.850  -2.117  1.00 32.82 ?  55  SER D O   1 
ATOM   6292 C CB  . SER D 2 55  ? 26.764  17.703  -2.840  1.00 24.83 ?  55  SER D CB  1 
ATOM   6293 O OG  . SER D 2 55  ? 28.098  17.829  -3.306  1.00 29.92 ?  55  SER D OG  1 
ATOM   6294 N N   . SER D 2 56  ? 23.534  16.572  -4.243  1.00 30.03 ?  56  SER D N   1 
ATOM   6295 C CA  . SER D 2 56  ? 22.136  16.442  -3.849  1.00 29.77 ?  56  SER D CA  1 
ATOM   6296 C C   . SER D 2 56  ? 21.847  15.066  -3.267  1.00 30.44 ?  56  SER D C   1 
ATOM   6297 O O   . SER D 2 56  ? 21.023  14.940  -2.354  1.00 30.89 ?  56  SER D O   1 
ATOM   6298 C CB  . SER D 2 56  ? 21.219  16.700  -5.047  1.00 29.10 ?  56  SER D CB  1 
ATOM   6299 O OG  . SER D 2 56  ? 21.724  17.731  -5.879  1.00 34.80 ?  56  SER D OG  1 
ATOM   6300 N N   . SER D 2 57  ? 22.511  14.031  -3.775  1.00 26.61 ?  57  SER D N   1 
ATOM   6301 C CA  . SER D 2 57  ? 22.203  12.656  -3.405  1.00 28.25 ?  57  SER D CA  1 
ATOM   6302 C C   . SER D 2 57  ? 23.504  11.902  -3.190  1.00 32.36 ?  57  SER D C   1 
ATOM   6303 O O   . SER D 2 57  ? 24.319  11.792  -4.110  1.00 31.90 ?  57  SER D O   1 
ATOM   6304 C CB  . SER D 2 57  ? 21.360  11.976  -4.487  1.00 27.52 ?  57  SER D CB  1 
ATOM   6305 O OG  . SER D 2 57  ? 20.384  12.866  -5.001  1.00 32.02 ?  57  SER D OG  1 
ATOM   6306 N N   . THR D 2 58  ? 23.695  11.386  -1.983  1.00 28.63 ?  58  THR D N   1 
ATOM   6307 C CA  . THR D 2 58  ? 24.864  10.588  -1.654  1.00 30.04 ?  58  THR D CA  1 
ATOM   6308 C C   . THR D 2 58  ? 24.474  9.116   -1.596  1.00 29.42 ?  58  THR D C   1 
ATOM   6309 O O   . THR D 2 58  ? 23.359  8.773   -1.190  1.00 29.49 ?  58  THR D O   1 
ATOM   6310 C CB  . THR D 2 58  ? 25.473  11.031  -0.322  1.00 28.95 ?  58  THR D CB  1 
ATOM   6311 O OG1 . THR D 2 58  ? 26.579  10.183  0.001   1.00 34.97 ?  58  THR D OG1 1 
ATOM   6312 C CG2 . THR D 2 58  ? 24.437  10.965  0.795   1.00 30.09 ?  58  THR D CG2 1 
ATOM   6313 N N   . THR D 2 59  ? 25.390  8.250   -2.022  1.00 25.55 ?  59  THR D N   1 
ATOM   6314 C CA  . THR D 2 59  ? 25.151  6.815   -2.055  1.00 27.43 ?  59  THR D CA  1 
ATOM   6315 C C   . THR D 2 59  ? 26.382  6.096   -1.527  1.00 26.50 ?  59  THR D C   1 
ATOM   6316 O O   . THR D 2 59  ? 27.511  6.467   -1.856  1.00 24.84 ?  59  THR D O   1 
ATOM   6317 C CB  . THR D 2 59  ? 24.827  6.329   -3.477  1.00 27.26 ?  59  THR D CB  1 
ATOM   6318 O OG1 . THR D 2 59  ? 23.911  7.241   -4.097  1.00 30.61 ?  59  THR D OG1 1 
ATOM   6319 C CG2 . THR D 2 59  ? 24.203  4.940   -3.443  1.00 21.58 ?  59  THR D CG2 1 
ATOM   6320 N N   . TYR D 2 60  ? 26.160  5.073   -0.705  1.00 28.05 ?  60  TYR D N   1 
ATOM   6321 C CA  . TYR D 2 60  ? 27.248  4.321   -0.099  1.00 28.30 ?  60  TYR D CA  1 
ATOM   6322 C C   . TYR D 2 60  ? 26.959  2.833   -0.187  1.00 26.61 ?  60  TYR D C   1 
ATOM   6323 O O   . TYR D 2 60  ? 25.811  2.405   -0.039  1.00 27.46 ?  60  TYR D O   1 
ATOM   6324 C CB  . TYR D 2 60  ? 27.454  4.699   1.374   1.00 27.11 ?  60  TYR D CB  1 
ATOM   6325 C CG  . TYR D 2 60  ? 27.852  6.135   1.608   1.00 26.18 ?  60  TYR D CG  1 
ATOM   6326 C CD1 . TYR D 2 60  ? 29.166  6.549   1.438   1.00 27.50 ?  60  TYR D CD1 1 
ATOM   6327 C CD2 . TYR D 2 60  ? 26.917  7.074   2.021   1.00 26.99 ?  60  TYR D CD2 1 
ATOM   6328 C CE1 . TYR D 2 60  ? 29.536  7.861   1.658   1.00 29.32 ?  60  TYR D CE1 1 
ATOM   6329 C CE2 . TYR D 2 60  ? 27.277  8.385   2.248   1.00 28.48 ?  60  TYR D CE2 1 
ATOM   6330 C CZ  . TYR D 2 60  ? 28.586  8.776   2.061   1.00 30.94 ?  60  TYR D CZ  1 
ATOM   6331 O OH  . TYR D 2 60  ? 28.945  10.085  2.282   1.00 31.04 ?  60  TYR D OH  1 
ATOM   6332 N N   . ALA D 2 61  ? 28.006  2.049   -0.426  1.00 28.26 ?  61  ALA D N   1 
ATOM   6333 C CA  . ALA D 2 61  ? 27.892  0.608   -0.264  1.00 32.79 ?  61  ALA D CA  1 
ATOM   6334 C C   . ALA D 2 61  ? 27.620  0.277   1.198   1.00 36.77 ?  61  ALA D C   1 
ATOM   6335 O O   . ALA D 2 61  ? 28.099  0.957   2.110   1.00 33.65 ?  61  ALA D O   1 
ATOM   6336 C CB  . ALA D 2 61  ? 29.165  -0.090  -0.743  1.00 29.66 ?  61  ALA D CB  1 
ATOM   6337 N N   . ASP D 2 62  ? 26.830  -0.778  1.416   1.00 37.24 ?  62  ASP D N   1 
ATOM   6338 C CA  . ASP D 2 62  ? 26.421  -1.136  2.772   1.00 38.69 ?  62  ASP D CA  1 
ATOM   6339 C C   . ASP D 2 62  ? 27.624  -1.384  3.672   1.00 42.97 ?  62  ASP D C   1 
ATOM   6340 O O   . ASP D 2 62  ? 27.604  -1.034  4.858   1.00 44.86 ?  62  ASP D O   1 
ATOM   6341 C CB  . ASP D 2 62  ? 25.523  -2.371  2.740   1.00 41.70 ?  62  ASP D CB  1 
ATOM   6342 C CG  . ASP D 2 62  ? 24.121  -2.061  2.261   1.00 44.73 ?  62  ASP D CG  1 
ATOM   6343 O OD1 . ASP D 2 62  ? 23.732  -0.875  2.278   1.00 44.34 ?  62  ASP D OD1 1 
ATOM   6344 O OD2 . ASP D 2 62  ? 23.407  -3.009  1.872   1.00 46.10 ?  62  ASP D OD2 1 
ATOM   6345 N N   . SER D 2 63  ? 28.686  -1.973  3.126   1.00 40.09 ?  63  SER D N   1 
ATOM   6346 C CA  . SER D 2 63  ? 29.857  -2.322  3.922   1.00 38.46 ?  63  SER D CA  1 
ATOM   6347 C C   . SER D 2 63  ? 30.694  -1.117  4.343   1.00 39.03 ?  63  SER D C   1 
ATOM   6348 O O   . SER D 2 63  ? 31.741  -1.322  4.965   1.00 39.82 ?  63  SER D O   1 
ATOM   6349 C CB  . SER D 2 63  ? 30.735  -3.308  3.147   1.00 39.58 ?  63  SER D CB  1 
ATOM   6350 O OG  . SER D 2 63  ? 31.413  -2.663  2.083   1.00 41.39 ?  63  SER D OG  1 
ATOM   6351 N N   . VAL D 2 64  ? 30.292  0.118   4.026   1.00 37.63 ?  64  VAL D N   1 
ATOM   6352 C CA  . VAL D 2 64  ? 31.098  1.290   4.369   1.00 37.86 ?  64  VAL D CA  1 
ATOM   6353 C C   . VAL D 2 64  ? 30.235  2.409   4.943   1.00 38.88 ?  64  VAL D C   1 
ATOM   6354 O O   . VAL D 2 64  ? 30.749  3.480   5.288   1.00 38.47 ?  64  VAL D O   1 
ATOM   6355 C CB  . VAL D 2 64  ? 31.892  1.810   3.153   1.00 38.94 ?  64  VAL D CB  1 
ATOM   6356 C CG1 . VAL D 2 64  ? 32.635  0.684   2.443   1.00 37.10 ?  64  VAL D CG1 1 
ATOM   6357 C CG2 . VAL D 2 64  ? 30.969  2.536   2.185   1.00 35.00 ?  64  VAL D CG2 1 
ATOM   6358 N N   . LYS D 2 65  ? 28.925  2.181   5.047   1.00 41.29 ?  65  LYS D N   1 
ATOM   6359 C CA  . LYS D 2 65  ? 28.036  3.230   5.533   1.00 43.71 ?  65  LYS D CA  1 
ATOM   6360 C C   . LYS D 2 65  ? 28.359  3.573   6.982   1.00 42.19 ?  65  LYS D C   1 
ATOM   6361 O O   . LYS D 2 65  ? 28.593  2.690   7.812   1.00 40.85 ?  65  LYS D O   1 
ATOM   6362 C CB  . LYS D 2 65  ? 26.568  2.809   5.405   1.00 45.57 ?  65  LYS D CB  1 
ATOM   6363 C CG  . LYS D 2 65  ? 26.201  1.519   6.122   1.00 49.26 ?  65  LYS D CG  1 
ATOM   6364 C CD  . LYS D 2 65  ? 24.753  1.539   6.599   1.00 49.53 ?  65  LYS D CD  1 
ATOM   6365 C CE  . LYS D 2 65  ? 24.607  2.329   7.893   1.00 49.61 ?  65  LYS D CE  1 
ATOM   6366 N NZ  . LYS D 2 65  ? 23.189  2.686   8.174   1.00 48.58 ?  65  LYS D NZ  1 
ATOM   6367 N N   . GLY D 2 66  ? 28.383  4.871   7.282   1.00 44.15 ?  66  GLY D N   1 
ATOM   6368 C CA  . GLY D 2 66  ? 28.695  5.360   8.604   1.00 40.92 ?  66  GLY D CA  1 
ATOM   6369 C C   . GLY D 2 66  ? 30.172  5.571   8.869   1.00 44.84 ?  66  GLY D C   1 
ATOM   6370 O O   . GLY D 2 66  ? 30.528  6.399   9.714   1.00 45.64 ?  66  GLY D O   1 
ATOM   6371 N N   . ARG D 2 67  ? 31.042  4.840   8.173   1.00 43.19 ?  67  ARG D N   1 
ATOM   6372 C CA  . ARG D 2 67  ? 32.482  4.997   8.327   1.00 39.35 ?  67  ARG D CA  1 
ATOM   6373 C C   . ARG D 2 67  ? 33.107  5.872   7.252   1.00 39.33 ?  67  ARG D C   1 
ATOM   6374 O O   . ARG D 2 67  ? 34.108  6.544   7.521   1.00 40.53 ?  67  ARG D O   1 
ATOM   6375 C CB  . ARG D 2 67  ? 33.174  3.628   8.317   1.00 40.89 ?  67  ARG D CB  1 
ATOM   6376 C CG  . ARG D 2 67  ? 32.499  2.579   9.185   1.00 42.32 ?  67  ARG D CG  1 
ATOM   6377 C CD  . ARG D 2 67  ? 33.366  1.337   9.320   1.00 37.27 ?  67  ARG D CD  1 
ATOM   6378 N NE  . ARG D 2 67  ? 33.256  0.466   8.156   1.00 43.84 ?  67  ARG D NE  1 
ATOM   6379 C CZ  . ARG D 2 67  ? 34.278  0.104   7.393   1.00 39.91 ?  67  ARG D CZ  1 
ATOM   6380 N NH1 . ARG D 2 67  ? 35.508  0.520   7.642   1.00 35.77 ?  67  ARG D NH1 1 
ATOM   6381 N NH2 . ARG D 2 67  ? 34.058  -0.695  6.352   1.00 37.02 ?  67  ARG D NH2 1 
ATOM   6382 N N   . PHE D 2 68  ? 32.550  5.873   6.045   1.00 39.42 ?  68  PHE D N   1 
ATOM   6383 C CA  . PHE D 2 68  ? 33.075  6.651   4.934   1.00 37.14 ?  68  PHE D CA  1 
ATOM   6384 C C   . PHE D 2 68  ? 32.117  7.789   4.609   1.00 35.81 ?  68  PHE D C   1 
ATOM   6385 O O   . PHE D 2 68  ? 30.905  7.681   4.818   1.00 37.54 ?  68  PHE D O   1 
ATOM   6386 C CB  . PHE D 2 68  ? 33.279  5.787   3.679   1.00 34.08 ?  68  PHE D CB  1 
ATOM   6387 C CG  . PHE D 2 68  ? 34.343  4.718   3.814   1.00 38.53 ?  68  PHE D CG  1 
ATOM   6388 C CD1 . PHE D 2 68  ? 34.935  4.430   5.036   1.00 37.32 ?  68  PHE D CD1 1 
ATOM   6389 C CD2 . PHE D 2 68  ? 34.745  3.995   2.702   1.00 34.89 ?  68  PHE D CD2 1 
ATOM   6390 C CE1 . PHE D 2 68  ? 35.898  3.445   5.146   1.00 34.85 ?  68  PHE D CE1 1 
ATOM   6391 C CE2 . PHE D 2 68  ? 35.711  3.010   2.806   1.00 36.24 ?  68  PHE D CE2 1 
ATOM   6392 C CZ  . PHE D 2 68  ? 36.287  2.734   4.030   1.00 35.48 ?  68  PHE D CZ  1 
ATOM   6393 N N   . THR D 2 69  ? 32.670  8.885   4.094   1.00 35.12 ?  69  THR D N   1 
ATOM   6394 C CA  . THR D 2 69  ? 31.873  10.016  3.638   1.00 36.02 ?  69  THR D CA  1 
ATOM   6395 C C   . THR D 2 69  ? 32.451  10.519  2.326   1.00 34.39 ?  69  THR D C   1 
ATOM   6396 O O   . THR D 2 69  ? 33.662  10.736  2.223   1.00 34.59 ?  69  THR D O   1 
ATOM   6397 C CB  . THR D 2 69  ? 31.846  11.145  4.677   1.00 38.46 ?  69  THR D CB  1 
ATOM   6398 O OG1 . THR D 2 69  ? 31.287  10.655  5.902   1.00 43.34 ?  69  THR D OG1 1 
ATOM   6399 C CG2 . THR D 2 69  ? 31.003  12.310  4.178   1.00 31.11 ?  69  THR D CG2 1 
ATOM   6400 N N   . ILE D 2 70  ? 31.589  10.692  1.326   1.00 33.58 ?  70  ILE D N   1 
ATOM   6401 C CA  . ILE D 2 70  ? 32.006  11.125  -0.002  1.00 31.48 ?  70  ILE D CA  1 
ATOM   6402 C C   . ILE D 2 70  ? 31.718  12.614  -0.149  1.00 33.77 ?  70  ILE D C   1 
ATOM   6403 O O   . ILE D 2 70  ? 30.741  13.141  0.397   1.00 31.13 ?  70  ILE D O   1 
ATOM   6404 C CB  . ILE D 2 70  ? 31.313  10.286  -1.099  1.00 29.99 ?  70  ILE D CB  1 
ATOM   6405 C CG1 . ILE D 2 70  ? 31.890  10.608  -2.478  1.00 30.13 ?  70  ILE D CG1 1 
ATOM   6406 C CG2 . ILE D 2 70  ? 29.800  10.480  -1.062  1.00 28.46 ?  70  ILE D CG2 1 
ATOM   6407 C CD1 . ILE D 2 70  ? 31.437  9.654   -3.557  1.00 28.79 ?  70  ILE D CD1 1 
ATOM   6408 N N   . SER D 2 71  ? 32.591  13.304  -0.884  1.00 32.80 ?  71  SER D N   1 
ATOM   6409 C CA  . SER D 2 71  ? 32.581  14.759  -0.935  1.00 35.51 ?  71  SER D CA  1 
ATOM   6410 C C   . SER D 2 71  ? 33.031  15.221  -2.314  1.00 33.96 ?  71  SER D C   1 
ATOM   6411 O O   . SER D 2 71  ? 33.874  14.584  -2.951  1.00 32.55 ?  71  SER D O   1 
ATOM   6412 C CB  . SER D 2 71  ? 33.489  15.347  0.153   1.00 35.51 ?  71  SER D CB  1 
ATOM   6413 O OG  . SER D 2 71  ? 33.365  16.755  0.234   1.00 40.14 ?  71  SER D OG  1 
ATOM   6414 N N   . ARG D 2 72  ? 32.472  16.345  -2.764  1.00 29.59 ?  72  ARG D N   1 
ATOM   6415 C CA  . ARG D 2 72  ? 32.746  16.859  -4.101  1.00 33.12 ?  72  ARG D CA  1 
ATOM   6416 C C   . ARG D 2 72  ? 32.845  18.377  -4.071  1.00 31.39 ?  72  ARG D C   1 
ATOM   6417 O O   . ARG D 2 72  ? 31.996  19.047  -3.474  1.00 27.83 ?  72  ARG D O   1 
ATOM   6418 C CB  . ARG D 2 72  ? 31.659  16.421  -5.090  1.00 30.92 ?  72  ARG D CB  1 
ATOM   6419 C CG  . ARG D 2 72  ? 32.149  16.254  -6.519  1.00 30.89 ?  72  ARG D CG  1 
ATOM   6420 C CD  . ARG D 2 72  ? 31.099  15.573  -7.384  1.00 32.95 ?  72  ARG D CD  1 
ATOM   6421 N NE  . ARG D 2 72  ? 31.226  15.936  -8.790  1.00 34.65 ?  72  ARG D NE  1 
ATOM   6422 C CZ  . ARG D 2 72  ? 30.596  15.321  -9.782  1.00 31.07 ?  72  ARG D CZ  1 
ATOM   6423 N NH1 . ARG D 2 72  ? 29.783  14.302  -9.558  1.00 27.74 ?  72  ARG D NH1 1 
ATOM   6424 N NH2 . ARG D 2 72  ? 30.785  15.742  -11.030 1.00 31.44 ?  72  ARG D NH2 1 
ATOM   6425 N N   . ASP D 2 73  ? 33.880  18.909  -4.723  1.00 36.53 ?  73  ASP D N   1 
ATOM   6426 C CA  . ASP D 2 73  ? 34.106  20.350  -4.846  1.00 39.76 ?  73  ASP D CA  1 
ATOM   6427 C C   . ASP D 2 73  ? 34.401  20.631  -6.317  1.00 38.69 ?  73  ASP D C   1 
ATOM   6428 O O   . ASP D 2 73  ? 35.502  20.350  -6.801  1.00 40.14 ?  73  ASP D O   1 
ATOM   6429 C CB  . ASP D 2 73  ? 35.252  20.809  -3.942  1.00 38.41 ?  73  ASP D CB  1 
ATOM   6430 C CG  . ASP D 2 73  ? 35.489  22.318  -3.989  1.00 42.87 ?  73  ASP D CG  1 
ATOM   6431 O OD1 . ASP D 2 73  ? 35.043  22.992  -4.941  1.00 43.36 ?  73  ASP D OD1 1 
ATOM   6432 O OD2 . ASP D 2 73  ? 36.135  22.837  -3.053  1.00 42.39 ?  73  ASP D OD2 1 
ATOM   6433 N N   . ASN D 2 74  ? 33.417  21.194  -7.024  1.00 38.57 ?  74  ASN D N   1 
ATOM   6434 C CA  . ASN D 2 74  ? 33.603  21.499  -8.440  1.00 42.88 ?  74  ASN D CA  1 
ATOM   6435 C C   . ASN D 2 74  ? 34.603  22.631  -8.639  1.00 44.93 ?  74  ASN D C   1 
ATOM   6436 O O   . ASN D 2 74  ? 35.411  22.594  -9.574  1.00 45.02 ?  74  ASN D O   1 
ATOM   6437 C CB  . ASN D 2 74  ? 32.261  21.852  -9.082  1.00 40.78 ?  74  ASN D CB  1 
ATOM   6438 C CG  . ASN D 2 74  ? 31.472  20.626  -9.496  1.00 41.92 ?  74  ASN D CG  1 
ATOM   6439 O OD1 . ASN D 2 74  ? 30.736  20.048  -8.697  1.00 37.81 ?  74  ASN D OD1 1 
ATOM   6440 N ND2 . ASN D 2 74  ? 31.623  20.222  -10.753 1.00 40.24 ?  74  ASN D ND2 1 
ATOM   6441 N N   . ALA D 2 75  ? 34.565  23.645  -7.770  1.00 48.56 ?  75  ALA D N   1 
ATOM   6442 C CA  . ALA D 2 75  ? 35.468  24.783  -7.903  1.00 43.19 ?  75  ALA D CA  1 
ATOM   6443 C C   . ALA D 2 75  ? 36.930  24.380  -7.773  1.00 46.28 ?  75  ALA D C   1 
ATOM   6444 O O   . ALA D 2 75  ? 37.806  25.099  -8.266  1.00 52.43 ?  75  ALA D O   1 
ATOM   6445 C CB  . ALA D 2 75  ? 35.126  25.851  -6.864  1.00 43.33 ?  75  ALA D CB  1 
ATOM   6446 N N   . LYS D 2 76  ? 37.214  23.256  -7.119  1.00 46.81 ?  76  LYS D N   1 
ATOM   6447 C CA  . LYS D 2 76  ? 38.563  22.715  -7.041  1.00 44.65 ?  76  LYS D CA  1 
ATOM   6448 C C   . LYS D 2 76  ? 38.771  21.528  -7.972  1.00 44.03 ?  76  LYS D C   1 
ATOM   6449 O O   . LYS D 2 76  ? 39.879  20.981  -8.013  1.00 42.24 ?  76  LYS D O   1 
ATOM   6450 C CB  . LYS D 2 76  ? 38.889  22.303  -5.601  1.00 42.79 ?  76  LYS D CB  1 
ATOM   6451 C CG  . LYS D 2 76  ? 39.715  23.325  -4.834  1.00 44.51 ?  76  LYS D CG  1 
ATOM   6452 C CD  . LYS D 2 76  ? 40.236  22.752  -3.525  1.00 40.02 ?  76  LYS D CD  1 
ATOM   6453 C CE  . LYS D 2 76  ? 41.484  23.485  -3.059  1.00 49.91 ?  76  LYS D CE  1 
ATOM   6454 N NZ  . LYS D 2 76  ? 42.608  22.551  -2.771  1.00 53.18 ?  76  LYS D NZ  1 
ATOM   6455 N N   . ASN D 2 77  ? 37.739  21.125  -8.717  1.00 43.97 ?  77  ASN D N   1 
ATOM   6456 C CA  . ASN D 2 77  ? 37.807  19.965  -9.607  1.00 42.11 ?  77  ASN D CA  1 
ATOM   6457 C C   . ASN D 2 77  ? 38.246  18.718  -8.843  1.00 38.30 ?  77  ASN D C   1 
ATOM   6458 O O   . ASN D 2 77  ? 39.056  17.922  -9.322  1.00 37.00 ?  77  ASN D O   1 
ATOM   6459 C CB  . ASN D 2 77  ? 38.735  20.233  -10.795 1.00 41.89 ?  77  ASN D CB  1 
ATOM   6460 C CG  . ASN D 2 77  ? 37.988  20.706  -12.028 1.00 41.72 ?  77  ASN D CG  1 
ATOM   6461 O OD1 . ASN D 2 77  ? 36.762  20.814  -12.023 1.00 45.78 ?  77  ASN D OD1 1 
ATOM   6462 N ND2 . ASN D 2 77  ? 38.727  20.988  -13.095 1.00 44.88 ?  77  ASN D ND2 1 
ATOM   6463 N N   . THR D 2 78  ? 37.701  18.545  -7.640  1.00 32.87 ?  78  THR D N   1 
ATOM   6464 C CA  . THR D 2 78  ? 38.183  17.517  -6.730  1.00 33.66 ?  78  THR D CA  1 
ATOM   6465 C C   . THR D 2 78  ? 37.020  16.790  -6.070  1.00 33.64 ?  78  THR D C   1 
ATOM   6466 O O   . THR D 2 78  ? 36.001  17.400  -5.735  1.00 33.25 ?  78  THR D O   1 
ATOM   6467 C CB  . THR D 2 78  ? 39.103  18.122  -5.657  1.00 36.88 ?  78  THR D CB  1 
ATOM   6468 O OG1 . THR D 2 78  ? 40.156  18.857  -6.292  1.00 38.30 ?  78  THR D OG1 1 
ATOM   6469 C CG2 . THR D 2 78  ? 39.720  17.031  -4.794  1.00 34.27 ?  78  THR D CG2 1 
ATOM   6470 N N   . MET D 2 79  ? 37.184  15.479  -5.896  1.00 33.67 ?  79  MET D N   1 
ATOM   6471 C CA  . MET D 2 79  ? 36.263  14.633  -5.151  1.00 34.08 ?  79  MET D CA  1 
ATOM   6472 C C   . MET D 2 79  ? 37.028  13.952  -4.023  1.00 34.09 ?  79  MET D C   1 
ATOM   6473 O O   . MET D 2 79  ? 38.170  13.520  -4.212  1.00 33.61 ?  79  MET D O   1 
ATOM   6474 C CB  . MET D 2 79  ? 35.613  13.585  -6.065  1.00 33.83 ?  79  MET D CB  1 
ATOM   6475 C CG  . MET D 2 79  ? 34.592  12.693  -5.377  1.00 30.21 ?  79  MET D CG  1 
ATOM   6476 S SD  . MET D 2 79  ? 33.677  11.653  -6.530  1.00 34.46 ?  79  MET D SD  1 
ATOM   6477 C CE  . MET D 2 79  ? 34.934  10.465  -6.985  1.00 31.38 ?  79  MET D CE  1 
ATOM   6478 N N   . TYR D 2 80  ? 36.403  13.858  -2.851  1.00 34.68 ?  80  TYR D N   1 
ATOM   6479 C CA  . TYR D 2 80  ? 37.067  13.357  -1.656  1.00 36.06 ?  80  TYR D CA  1 
ATOM   6480 C C   . TYR D 2 80  ? 36.344  12.138  -1.099  1.00 36.83 ?  80  TYR D C   1 
ATOM   6481 O O   . TYR D 2 80  ? 35.128  11.988  -1.255  1.00 35.79 ?  80  TYR D O   1 
ATOM   6482 C CB  . TYR D 2 80  ? 37.151  14.428  -0.557  1.00 33.06 ?  80  TYR D CB  1 
ATOM   6483 C CG  . TYR D 2 80  ? 37.580  15.800  -1.025  1.00 38.14 ?  80  TYR D CG  1 
ATOM   6484 C CD1 . TYR D 2 80  ? 36.683  16.660  -1.647  1.00 36.86 ?  80  TYR D CD1 1 
ATOM   6485 C CD2 . TYR D 2 80  ? 38.883  16.241  -0.832  1.00 40.55 ?  80  TYR D CD2 1 
ATOM   6486 C CE1 . TYR D 2 80  ? 37.073  17.915  -2.070  1.00 35.40 ?  80  TYR D CE1 1 
ATOM   6487 C CE2 . TYR D 2 80  ? 39.282  17.495  -1.251  1.00 37.97 ?  80  TYR D CE2 1 
ATOM   6488 C CZ  . TYR D 2 80  ? 38.372  18.327  -1.869  1.00 37.33 ?  80  TYR D CZ  1 
ATOM   6489 O OH  . TYR D 2 80  ? 38.764  19.577  -2.289  1.00 41.15 ?  80  TYR D OH  1 
ATOM   6490 N N   . LEU D 2 81  ? 37.110  11.273  -0.436  1.00 34.78 ?  81  LEU D N   1 
ATOM   6491 C CA  . LEU D 2 81  ? 36.577  10.124  0.294   1.00 33.50 ?  81  LEU D CA  1 
ATOM   6492 C C   . LEU D 2 81  ? 37.168  10.156  1.701   1.00 36.00 ?  81  LEU D C   1 
ATOM   6493 O O   . LEU D 2 81  ? 38.309  9.733   1.912   1.00 30.71 ?  81  LEU D O   1 
ATOM   6494 C CB  . LEU D 2 81  ? 36.898  8.810   -0.413  1.00 30.29 ?  81  LEU D CB  1 
ATOM   6495 C CG  . LEU D 2 81  ? 36.361  7.544   0.263   1.00 33.27 ?  81  LEU D CG  1 
ATOM   6496 C CD1 . LEU D 2 81  ? 34.871  7.666   0.546   1.00 32.79 ?  81  LEU D CD1 1 
ATOM   6497 C CD2 . LEU D 2 81  ? 36.650  6.309   -0.578  1.00 32.94 ?  81  LEU D CD2 1 
ATOM   6498 N N   . GLN D 2 82  ? 36.395  10.666  2.657   1.00 35.61 ?  82  GLN D N   1 
ATOM   6499 C CA  . GLN D 2 82  ? 36.816  10.692  4.053   1.00 37.58 ?  82  GLN D CA  1 
ATOM   6500 C C   . GLN D 2 82  ? 36.571  9.322   4.673   1.00 34.85 ?  82  GLN D C   1 
ATOM   6501 O O   . GLN D 2 82  ? 35.427  8.858   4.729   1.00 36.40 ?  82  GLN D O   1 
ATOM   6502 C CB  . GLN D 2 82  ? 36.061  11.779  4.814   1.00 37.44 ?  82  GLN D CB  1 
ATOM   6503 C CG  . GLN D 2 82  ? 36.218  13.176  4.226   1.00 36.66 ?  82  GLN D CG  1 
ATOM   6504 C CD  . GLN D 2 82  ? 34.984  13.639  3.473   1.00 48.36 ?  82  GLN D CD  1 
ATOM   6505 O OE1 . GLN D 2 82  ? 34.779  13.283  2.311   1.00 36.85 ?  82  GLN D OE1 1 
ATOM   6506 N NE2 . GLN D 2 82  ? 34.154  14.440  4.133   1.00 47.49 ?  82  GLN D NE2 1 
ATOM   6507 N N   . MET D 2 83  ? 37.637  8.676   5.143   1.00 34.50 ?  83  MET D N   1 
ATOM   6508 C CA  . MET D 2 83  ? 37.581  7.289   5.590   1.00 34.84 ?  83  MET D CA  1 
ATOM   6509 C C   . MET D 2 83  ? 37.998  7.209   7.052   1.00 37.88 ?  83  MET D C   1 
ATOM   6510 O O   . MET D 2 83  ? 39.084  7.673   7.415   1.00 39.25 ?  83  MET D O   1 
ATOM   6511 C CB  . MET D 2 83  ? 38.487  6.409   4.728   1.00 38.00 ?  83  MET D CB  1 
ATOM   6512 C CG  . MET D 2 83  ? 37.796  5.817   3.516   1.00 36.44 ?  83  MET D CG  1 
ATOM   6513 S SD  . MET D 2 83  ? 38.830  4.628   2.647   1.00 46.64 ?  83  MET D SD  1 
ATOM   6514 C CE  . MET D 2 83  ? 40.272  5.633   2.330   1.00 28.73 ?  83  MET D CE  1 
ATOM   6515 N N   . THR D 2 84  ? 37.137  6.624   7.885   1.00 34.85 ?  84  THR D N   1 
ATOM   6516 C CA  . THR D 2 84  ? 37.418  6.419   9.300   1.00 38.05 ?  84  THR D CA  1 
ATOM   6517 C C   . THR D 2 84  ? 37.105  4.978   9.684   1.00 37.64 ?  84  THR D C   1 
ATOM   6518 O O   . THR D 2 84  ? 36.418  4.254   8.958   1.00 34.32 ?  84  THR D O   1 
ATOM   6519 C CB  . THR D 2 84  ? 36.606  7.370   10.200  1.00 32.90 ?  84  THR D CB  1 
ATOM   6520 O OG1 . THR D 2 84  ? 35.338  6.776   10.505  1.00 36.42 ?  84  THR D OG1 1 
ATOM   6521 C CG2 . THR D 2 84  ? 36.380  8.714   9.522   1.00 35.62 ?  84  THR D CG2 1 
ATOM   6522 N N   . GLY D 2 85  ? 37.621  4.573   10.843  1.00 36.51 ?  85  GLY D N   1 
ATOM   6523 C CA  . GLY D 2 85  ? 37.340  3.251   11.391  1.00 31.26 ?  85  GLY D CA  1 
ATOM   6524 C C   . GLY D 2 85  ? 37.715  2.101   10.483  1.00 36.61 ?  85  GLY D C   1 
ATOM   6525 O O   . GLY D 2 85  ? 36.974  1.113   10.398  1.00 37.61 ?  85  GLY D O   1 
ATOM   6526 N N   . LEU D 2 86  ? 38.863  2.198   9.816   1.00 38.36 ?  86  LEU D N   1 
ATOM   6527 C CA  . LEU D 2 86  ? 39.221  1.240   8.779   1.00 37.09 ?  86  LEU D CA  1 
ATOM   6528 C C   . LEU D 2 86  ? 39.435  -0.156  9.354   1.00 38.56 ?  86  LEU D C   1 
ATOM   6529 O O   . LEU D 2 86  ? 39.775  -0.331  10.528  1.00 38.21 ?  86  LEU D O   1 
ATOM   6530 C CB  . LEU D 2 86  ? 40.482  1.702   8.047   1.00 38.46 ?  86  LEU D CB  1 
ATOM   6531 C CG  . LEU D 2 86  ? 40.296  2.880   7.088   1.00 37.63 ?  86  LEU D CG  1 
ATOM   6532 C CD1 . LEU D 2 86  ? 41.483  3.829   7.153   1.00 38.27 ?  86  LEU D CD1 1 
ATOM   6533 C CD2 . LEU D 2 86  ? 40.077  2.386   5.667   1.00 40.53 ?  86  LEU D CD2 1 
ATOM   6534 N N   . LYS D 2 87  ? 39.227  -1.154  8.506   1.00 37.98 ?  87  LYS D N   1 
ATOM   6535 C CA  . LYS D 2 87  ? 39.418  -2.562  8.809   1.00 37.29 ?  87  LYS D CA  1 
ATOM   6536 C C   . LYS D 2 87  ? 40.324  -3.171  7.752   1.00 36.84 ?  87  LYS D C   1 
ATOM   6537 O O   . LYS D 2 87  ? 40.483  -2.608  6.664   1.00 37.22 ?  87  LYS D O   1 
ATOM   6538 C CB  . LYS D 2 87  ? 38.078  -3.315  8.839   1.00 35.80 ?  87  LYS D CB  1 
ATOM   6539 C CG  . LYS D 2 87  ? 36.910  -2.533  9.418   1.00 35.20 ?  87  LYS D CG  1 
ATOM   6540 C CD  . LYS D 2 87  ? 35.589  -3.084  8.897   1.00 36.85 ?  87  LYS D CD  1 
ATOM   6541 C CE  . LYS D 2 87  ? 34.493  -3.017  9.949   1.00 36.10 ?  87  LYS D CE  1 
ATOM   6542 N NZ  . LYS D 2 87  ? 34.677  -1.872  10.881  1.00 40.58 ?  87  LYS D NZ  1 
ATOM   6543 N N   . PRO D 2 88  ? 40.943  -4.319  8.043   1.00 36.88 ?  88  PRO D N   1 
ATOM   6544 C CA  . PRO D 2 88  ? 41.748  -4.995  7.011   1.00 37.15 ?  88  PRO D CA  1 
ATOM   6545 C C   . PRO D 2 88  ? 40.962  -5.353  5.761   1.00 38.24 ?  88  PRO D C   1 
ATOM   6546 O O   . PRO D 2 88  ? 41.566  -5.507  4.693   1.00 39.45 ?  88  PRO D O   1 
ATOM   6547 C CB  . PRO D 2 88  ? 42.256  -6.251  7.733   1.00 38.91 ?  88  PRO D CB  1 
ATOM   6548 C CG  . PRO D 2 88  ? 42.280  -5.859  9.172   1.00 37.37 ?  88  PRO D CG  1 
ATOM   6549 C CD  . PRO D 2 88  ? 41.080  -4.972  9.358   1.00 38.00 ?  88  PRO D CD  1 
ATOM   6550 N N   . GLU D 2 89  ? 39.636  -5.486  5.856   1.00 39.43 ?  89  GLU D N   1 
ATOM   6551 C CA  . GLU D 2 89  ? 38.825  -5.747  4.674   1.00 36.26 ?  89  GLU D CA  1 
ATOM   6552 C C   . GLU D 2 89  ? 38.829  -4.576  3.701   1.00 37.68 ?  89  GLU D C   1 
ATOM   6553 O O   . GLU D 2 89  ? 38.527  -4.767  2.518   1.00 39.24 ?  89  GLU D O   1 
ATOM   6554 C CB  . GLU D 2 89  ? 37.387  -6.074  5.082   1.00 32.48 ?  89  GLU D CB  1 
ATOM   6555 C CG  . GLU D 2 89  ? 37.242  -7.336  5.917   1.00 34.99 ?  89  GLU D CG  1 
ATOM   6556 C CD  . GLU D 2 89  ? 37.308  -7.061  7.407   1.00 38.41 ?  89  GLU D CD  1 
ATOM   6557 O OE1 . GLU D 2 89  ? 38.329  -6.508  7.867   1.00 36.56 ?  89  GLU D OE1 1 
ATOM   6558 O OE2 . GLU D 2 89  ? 36.337  -7.395  8.119   1.00 37.21 ?  89  GLU D OE2 1 
ATOM   6559 N N   . ASP D 2 90  ? 39.160  -3.373  4.169   1.00 38.77 ?  90  ASP D N   1 
ATOM   6560 C CA  . ASP D 2 90  ? 39.213  -2.192  3.317   1.00 35.85 ?  90  ASP D CA  1 
ATOM   6561 C C   . ASP D 2 90  ? 40.475  -2.128  2.466   1.00 37.42 ?  90  ASP D C   1 
ATOM   6562 O O   . ASP D 2 90  ? 40.638  -1.169  1.705   1.00 36.83 ?  90  ASP D O   1 
ATOM   6563 C CB  . ASP D 2 90  ? 39.108  -0.924  4.170   1.00 36.51 ?  90  ASP D CB  1 
ATOM   6564 C CG  . ASP D 2 90  ? 37.794  -0.833  4.921   1.00 37.61 ?  90  ASP D CG  1 
ATOM   6565 O OD1 . ASP D 2 90  ? 36.771  -1.320  4.395   1.00 37.05 ?  90  ASP D OD1 1 
ATOM   6566 O OD2 . ASP D 2 90  ? 37.784  -0.272  6.038   1.00 34.16 ?  90  ASP D OD2 1 
ATOM   6567 N N   . THR D 2 91  ? 41.365  -3.111  2.577   1.00 36.83 ?  91  THR D N   1 
ATOM   6568 C CA  . THR D 2 91  ? 42.600  -3.111  1.801   1.00 37.83 ?  91  THR D CA  1 
ATOM   6569 C C   . THR D 2 91  ? 42.291  -3.369  0.332   1.00 33.80 ?  91  THR D C   1 
ATOM   6570 O O   . THR D 2 91  ? 41.750  -4.423  -0.018  1.00 32.09 ?  91  THR D O   1 
ATOM   6571 C CB  . THR D 2 91  ? 43.561  -4.169  2.335   1.00 36.16 ?  91  THR D CB  1 
ATOM   6572 O OG1 . THR D 2 91  ? 43.981  -3.814  3.659   1.00 35.72 ?  91  THR D OG1 1 
ATOM   6573 C CG2 . THR D 2 91  ? 44.780  -4.282  1.432   1.00 36.68 ?  91  THR D CG2 1 
ATOM   6574 N N   . ALA D 2 92  ? 42.644  -2.415  -0.526  1.00 33.46 ?  92  ALA D N   1 
ATOM   6575 C CA  . ALA D 2 92  ? 42.375  -2.512  -1.958  1.00 38.42 ?  92  ALA D CA  1 
ATOM   6576 C C   . ALA D 2 92  ? 43.061  -1.348  -2.664  1.00 35.37 ?  92  ALA D C   1 
ATOM   6577 O O   . ALA D 2 92  ? 43.678  -0.484  -2.033  1.00 36.39 ?  92  ALA D O   1 
ATOM   6578 C CB  . ALA D 2 92  ? 40.872  -2.510  -2.248  1.00 37.57 ?  92  ALA D CB  1 
ATOM   6579 N N   . VAL D 2 93  ? 42.949  -1.341  -3.988  1.00 35.61 ?  93  VAL D N   1 
ATOM   6580 C CA  . VAL D 2 93  ? 43.273  -0.173  -4.796  1.00 38.91 ?  93  VAL D CA  1 
ATOM   6581 C C   . VAL D 2 93  ? 41.977  0.591   -5.027  1.00 38.93 ?  93  VAL D C   1 
ATOM   6582 O O   . VAL D 2 93  ? 41.004  0.032   -5.543  1.00 37.22 ?  93  VAL D O   1 
ATOM   6583 C CB  . VAL D 2 93  ? 43.924  -0.572  -6.129  1.00 38.22 ?  93  VAL D CB  1 
ATOM   6584 C CG1 . VAL D 2 93  ? 44.280  0.668   -6.934  1.00 38.91 ?  93  VAL D CG1 1 
ATOM   6585 C CG2 . VAL D 2 93  ? 45.157  -1.426  -5.886  1.00 35.81 ?  93  VAL D CG2 1 
ATOM   6586 N N   . TYR D 2 94  ? 41.953  1.860   -4.634  1.00 37.91 ?  94  TYR D N   1 
ATOM   6587 C CA  . TYR D 2 94  ? 40.750  2.676   -4.720  1.00 37.06 ?  94  TYR D CA  1 
ATOM   6588 C C   . TYR D 2 94  ? 40.783  3.506   -5.996  1.00 36.40 ?  94  TYR D C   1 
ATOM   6589 O O   . TYR D 2 94  ? 41.792  4.155   -6.294  1.00 40.88 ?  94  TYR D O   1 
ATOM   6590 C CB  . TYR D 2 94  ? 40.615  3.577   -3.492  1.00 30.28 ?  94  TYR D CB  1 
ATOM   6591 C CG  . TYR D 2 94  ? 40.089  2.851   -2.275  1.00 37.44 ?  94  TYR D CG  1 
ATOM   6592 C CD1 . TYR D 2 94  ? 40.852  1.878   -1.640  1.00 35.07 ?  94  TYR D CD1 1 
ATOM   6593 C CD2 . TYR D 2 94  ? 38.827  3.128   -1.766  1.00 32.46 ?  94  TYR D CD2 1 
ATOM   6594 C CE1 . TYR D 2 94  ? 40.377  1.208   -0.531  1.00 35.59 ?  94  TYR D CE1 1 
ATOM   6595 C CE2 . TYR D 2 94  ? 38.343  2.462   -0.656  1.00 34.69 ?  94  TYR D CE2 1 
ATOM   6596 C CZ  . TYR D 2 94  ? 39.122  1.502   -0.043  1.00 38.17 ?  94  TYR D CZ  1 
ATOM   6597 O OH  . TYR D 2 94  ? 38.646  0.835   1.062   1.00 37.29 ?  94  TYR D OH  1 
ATOM   6598 N N   . TYR D 2 95  ? 39.682  3.482   -6.743  1.00 32.23 ?  95  TYR D N   1 
ATOM   6599 C CA  . TYR D 2 95  ? 39.602  4.125   -8.047  1.00 35.21 ?  95  TYR D CA  1 
ATOM   6600 C C   . TYR D 2 95  ? 38.566  5.237   -8.035  1.00 33.82 ?  95  TYR D C   1 
ATOM   6601 O O   . TYR D 2 95  ? 37.416  5.021   -7.636  1.00 34.68 ?  95  TYR D O   1 
ATOM   6602 C CB  . TYR D 2 95  ? 39.252  3.120   -9.147  1.00 35.63 ?  95  TYR D CB  1 
ATOM   6603 C CG  . TYR D 2 95  ? 40.283  2.041   -9.363  1.00 38.44 ?  95  TYR D CG  1 
ATOM   6604 C CD1 . TYR D 2 95  ? 40.279  0.885   -8.596  1.00 36.46 ?  95  TYR D CD1 1 
ATOM   6605 C CD2 . TYR D 2 95  ? 41.261  2.179   -10.340 1.00 39.77 ?  95  TYR D CD2 1 
ATOM   6606 C CE1 . TYR D 2 95  ? 41.220  -0.105  -8.795  1.00 39.32 ?  95  TYR D CE1 1 
ATOM   6607 C CE2 . TYR D 2 95  ? 42.207  1.195   -10.546 1.00 42.16 ?  95  TYR D CE2 1 
ATOM   6608 C CZ  . TYR D 2 95  ? 42.181  0.055   -9.770  1.00 43.58 ?  95  TYR D CZ  1 
ATOM   6609 O OH  . TYR D 2 95  ? 43.120  -0.931  -9.969  1.00 46.92 ?  95  TYR D OH  1 
ATOM   6610 N N   . CYS D 2 96  ? 38.982  6.420   -8.474  1.00 31.58 ?  96  CYS D N   1 
ATOM   6611 C CA  . CYS D 2 96  ? 38.049  7.470   -8.850  1.00 33.10 ?  96  CYS D CA  1 
ATOM   6612 C C   . CYS D 2 96  ? 37.439  7.141   -10.209 1.00 30.68 ?  96  CYS D C   1 
ATOM   6613 O O   . CYS D 2 96  ? 38.067  6.495   -11.052 1.00 27.89 ?  96  CYS D O   1 
ATOM   6614 C CB  . CYS D 2 96  ? 38.775  8.815   -8.896  1.00 34.18 ?  96  CYS D CB  1 
ATOM   6615 S SG  . CYS D 2 96  ? 37.749  10.280  -9.097  1.00 54.36 ?  96  CYS D SG  1 
ATOM   6616 N N   . ALA D 2 97  ? 36.200  7.579   -10.420 1.00 29.92 ?  97  ALA D N   1 
ATOM   6617 C CA  . ALA D 2 97  ? 35.516  7.269   -11.670 1.00 30.94 ?  97  ALA D CA  1 
ATOM   6618 C C   . ALA D 2 97  ? 34.410  8.285   -11.916 1.00 31.68 ?  97  ALA D C   1 
ATOM   6619 O O   . ALA D 2 97  ? 33.926  8.941   -10.991 1.00 31.81 ?  97  ALA D O   1 
ATOM   6620 C CB  . ALA D 2 97  ? 34.950  5.844   -11.660 1.00 30.29 ?  97  ALA D CB  1 
ATOM   6621 N N   . SER D 2 98  ? 34.015  8.398   -13.186 1.00 30.64 ?  98  SER D N   1 
ATOM   6622 C CA  . SER D 2 98  ? 32.992  9.347   -13.605 1.00 31.62 ?  98  SER D CA  1 
ATOM   6623 C C   . SER D 2 98  ? 32.267  8.814   -14.834 1.00 29.61 ?  98  SER D C   1 
ATOM   6624 O O   . SER D 2 98  ? 32.891  8.252   -15.738 1.00 30.91 ?  98  SER D O   1 
ATOM   6625 C CB  . SER D 2 98  ? 33.596  10.726  -13.904 1.00 29.40 ?  98  SER D CB  1 
ATOM   6626 O OG  . SER D 2 98  ? 34.010  10.832  -15.254 1.00 33.12 ?  98  SER D OG  1 
ATOM   6627 N N   . ASP D 2 99  ? 30.948  9.007   -14.862 1.00 26.77 ?  99  ASP D N   1 
ATOM   6628 C CA  . ASP D 2 99  ? 30.085  8.537   -15.943 1.00 28.04 ?  99  ASP D CA  1 
ATOM   6629 C C   . ASP D 2 99  ? 29.629  9.742   -16.758 1.00 27.03 ?  99  ASP D C   1 
ATOM   6630 O O   . ASP D 2 99  ? 28.880  10.589  -16.259 1.00 27.49 ?  99  ASP D O   1 
ATOM   6631 C CB  . ASP D 2 99  ? 28.888  7.767   -15.383 1.00 26.53 ?  99  ASP D CB  1 
ATOM   6632 C CG  . ASP D 2 99  ? 27.991  7.199   -16.471 1.00 26.48 ?  99  ASP D CG  1 
ATOM   6633 O OD1 . ASP D 2 99  ? 28.363  7.272   -17.662 1.00 23.28 ?  99  ASP D OD1 1 
ATOM   6634 O OD2 . ASP D 2 99  ? 26.913  6.667   -16.133 1.00 25.36 ?  99  ASP D OD2 1 
ATOM   6635 N N   . ARG D 2 100 ? 30.069  9.809   -18.016 1.00 26.57 ?  100 ARG D N   1 
ATOM   6636 C CA  . ARG D 2 100 ? 29.719  10.928  -18.881 1.00 27.78 ?  100 ARG D CA  1 
ATOM   6637 C C   . ARG D 2 100 ? 28.277  10.882  -19.368 1.00 26.58 ?  100 ARG D C   1 
ATOM   6638 O O   . ARG D 2 100 ? 27.789  11.889  -19.891 1.00 27.79 ?  100 ARG D O   1 
ATOM   6639 C CB  . ARG D 2 100 ? 30.656  10.974  -20.089 1.00 27.22 ?  100 ARG D CB  1 
ATOM   6640 C CG  . ARG D 2 100 ? 30.365  9.911   -21.135 1.00 25.89 ?  100 ARG D CG  1 
ATOM   6641 C CD  . ARG D 2 100 ? 31.549  9.713   -22.066 1.00 27.76 ?  100 ARG D CD  1 
ATOM   6642 N NE  . ARG D 2 100 ? 31.230  8.815   -23.169 1.00 29.86 ?  100 ARG D NE  1 
ATOM   6643 C CZ  . ARG D 2 100 ? 31.835  8.836   -24.349 1.00 30.46 ?  100 ARG D CZ  1 
ATOM   6644 N NH1 . ARG D 2 100 ? 32.796  9.705   -24.617 1.00 32.31 ?  100 ARG D NH1 1 
ATOM   6645 N NH2 . ARG D 2 100 ? 31.466  7.964   -25.283 1.00 25.66 ?  100 ARG D NH2 1 
ATOM   6646 N N   . ASP D 2 101 ? 27.586  9.753   -19.213 1.00 25.64 ?  101 ASP D N   1 
ATOM   6647 C CA  . ASP D 2 101 ? 26.240  9.610   -19.752 1.00 24.26 ?  101 ASP D CA  1 
ATOM   6648 C C   . ASP D 2 101 ? 25.151  10.071  -18.795 1.00 26.73 ?  101 ASP D C   1 
ATOM   6649 O O   . ASP D 2 101 ? 24.035  10.360  -19.245 1.00 25.58 ?  101 ASP D O   1 
ATOM   6650 C CB  . ASP D 2 101 ? 25.975  8.150   -20.138 1.00 24.28 ?  101 ASP D CB  1 
ATOM   6651 C CG  . ASP D 2 101 ? 26.981  7.619   -21.142 1.00 27.20 ?  101 ASP D CG  1 
ATOM   6652 O OD1 . ASP D 2 101 ? 26.833  7.918   -22.346 1.00 29.07 ?  101 ASP D OD1 1 
ATOM   6653 O OD2 . ASP D 2 101 ? 27.917  6.903   -20.729 1.00 27.29 ?  101 ASP D OD2 1 
ATOM   6654 N N   . HIS D 2 102 ? 25.437  10.155  -17.500 1.00 23.85 ?  102 HIS D N   1 
ATOM   6655 C CA  . HIS D 2 102 ? 24.407  10.417  -16.509 1.00 25.80 ?  102 HIS D CA  1 
ATOM   6656 C C   . HIS D 2 102 ? 24.837  11.537  -15.573 1.00 25.50 ?  102 HIS D C   1 
ATOM   6657 O O   . HIS D 2 102 ? 26.015  11.898  -15.492 1.00 25.17 ?  102 HIS D O   1 
ATOM   6658 C CB  . HIS D 2 102 ? 24.080  9.150   -15.712 1.00 26.68 ?  102 HIS D CB  1 
ATOM   6659 C CG  . HIS D 2 102 ? 23.603  8.016   -16.565 1.00 28.64 ?  102 HIS D CG  1 
ATOM   6660 N ND1 . HIS D 2 102 ? 24.439  7.014   -17.007 1.00 27.85 ?  102 HIS D ND1 1 
ATOM   6661 C CD2 . HIS D 2 102 ? 22.378  7.733   -17.066 1.00 26.38 ?  102 HIS D CD2 1 
ATOM   6662 C CE1 . HIS D 2 102 ? 23.749  6.159   -17.740 1.00 27.00 ?  102 HIS D CE1 1 
ATOM   6663 N NE2 . HIS D 2 102 ? 22.495  6.572   -17.791 1.00 29.01 ?  102 HIS D NE2 1 
ATOM   6664 N N   . TYR D 2 103 ? 23.848  12.080  -14.862 1.00 23.00 ?  103 TYR D N   1 
ATOM   6665 C CA  . TYR D 2 103 ? 24.039  13.200  -13.948 1.00 22.57 ?  103 TYR D CA  1 
ATOM   6666 C C   . TYR D 2 103 ? 23.354  12.945  -12.611 1.00 23.88 ?  103 TYR D C   1 
ATOM   6667 O O   . TYR D 2 103 ? 23.791  13.456  -11.575 1.00 25.43 ?  103 TYR D O   1 
ATOM   6668 C CB  . TYR D 2 103 ? 23.490  14.488  -14.568 1.00 24.67 ?  103 TYR D CB  1 
ATOM   6669 C CG  . TYR D 2 103 ? 21.976  14.519  -14.644 1.00 27.19 ?  103 TYR D CG  1 
ATOM   6670 C CD1 . TYR D 2 103 ? 21.306  13.962  -15.727 1.00 23.81 ?  103 TYR D CD1 1 
ATOM   6671 C CD2 . TYR D 2 103 ? 21.215  15.085  -13.625 1.00 23.86 ?  103 TYR D CD2 1 
ATOM   6672 C CE1 . TYR D 2 103 ? 19.923  13.979  -15.799 1.00 22.40 ?  103 TYR D CE1 1 
ATOM   6673 C CE2 . TYR D 2 103 ? 19.835  15.105  -13.689 1.00 26.68 ?  103 TYR D CE2 1 
ATOM   6674 C CZ  . TYR D 2 103 ? 19.194  14.552  -14.776 1.00 24.50 ?  103 TYR D CZ  1 
ATOM   6675 O OH  . TYR D 2 103 ? 17.820  14.577  -14.832 1.00 24.32 ?  103 TYR D OH  1 
ATOM   6676 N N   . SER D 2 104 ? 22.268  12.175  -12.629 1.00 22.36 ?  104 SER D N   1 
ATOM   6677 C CA  . SER D 2 104 ? 21.418  12.036  -11.454 1.00 22.33 ?  104 SER D CA  1 
ATOM   6678 C C   . SER D 2 104 ? 22.110  11.213  -10.374 1.00 26.70 ?  104 SER D C   1 
ATOM   6679 O O   . SER D 2 104 ? 22.658  10.141  -10.648 1.00 22.66 ?  104 SER D O   1 
ATOM   6680 C CB  . SER D 2 104 ? 20.090  11.386  -11.842 1.00 24.13 ?  104 SER D CB  1 
ATOM   6681 O OG  . SER D 2 104 ? 19.172  11.384  -10.761 1.00 28.20 ?  104 SER D OG  1 
ATOM   6682 N N   . GLY D 2 105 ? 22.081  11.718  -9.141  1.00 24.54 ?  105 GLY D N   1 
ATOM   6683 C CA  . GLY D 2 105 ? 22.584  10.956  -8.015  1.00 24.33 ?  105 GLY D CA  1 
ATOM   6684 C C   . GLY D 2 105 ? 21.763  9.731   -7.675  1.00 26.33 ?  105 GLY D C   1 
ATOM   6685 O O   . GLY D 2 105 ? 22.195  8.933   -6.837  1.00 25.60 ?  105 GLY D O   1 
ATOM   6686 N N   . THR D 2 106 ? 20.595  9.565   -8.300  1.00 27.36 ?  106 THR D N   1 
ATOM   6687 C CA  . THR D 2 106 ? 19.754  8.392   -8.087  1.00 25.44 ?  106 THR D CA  1 
ATOM   6688 C C   . THR D 2 106 ? 19.606  7.556   -9.354  1.00 24.48 ?  106 THR D C   1 
ATOM   6689 O O   . THR D 2 106 ? 18.652  6.780   -9.468  1.00 27.86 ?  106 THR D O   1 
ATOM   6690 C CB  . THR D 2 106 ? 18.377  8.798   -7.559  1.00 24.92 ?  106 THR D CB  1 
ATOM   6691 O OG1 . THR D 2 106 ? 17.783  9.753   -8.447  1.00 32.07 ?  106 THR D OG1 1 
ATOM   6692 C CG2 . THR D 2 106 ? 18.497  9.407   -6.169  1.00 25.34 ?  106 THR D CG2 1 
ATOM   6693 N N   . TYR D 2 107 ? 20.518  7.712   -10.314 1.00 23.81 ?  107 TYR D N   1 
ATOM   6694 C CA  . TYR D 2 107 ? 20.571  6.816   -11.463 1.00 26.10 ?  107 TYR D CA  1 
ATOM   6695 C C   . TYR D 2 107 ? 20.660  5.374   -10.984 1.00 26.25 ?  107 TYR D C   1 
ATOM   6696 O O   . TYR D 2 107 ? 21.598  5.004   -10.273 1.00 28.49 ?  107 TYR D O   1 
ATOM   6697 C CB  . TYR D 2 107 ? 21.773  7.167   -12.346 1.00 25.06 ?  107 TYR D CB  1 
ATOM   6698 C CG  . TYR D 2 107 ? 22.106  6.123   -13.391 1.00 26.84 ?  107 TYR D CG  1 
ATOM   6699 C CD1 . TYR D 2 107 ? 21.130  5.630   -14.248 1.00 29.24 ?  107 TYR D CD1 1 
ATOM   6700 C CD2 . TYR D 2 107 ? 23.399  5.627   -13.516 1.00 25.72 ?  107 TYR D CD2 1 
ATOM   6701 C CE1 . TYR D 2 107 ? 21.431  4.674   -15.200 1.00 28.54 ?  107 TYR D CE1 1 
ATOM   6702 C CE2 . TYR D 2 107 ? 23.709  4.669   -14.467 1.00 27.53 ?  107 TYR D CE2 1 
ATOM   6703 C CZ  . TYR D 2 107 ? 22.720  4.197   -15.305 1.00 27.84 ?  107 TYR D CZ  1 
ATOM   6704 O OH  . TYR D 2 107 ? 23.016  3.246   -16.255 1.00 28.05 ?  107 TYR D OH  1 
ATOM   6705 N N   . TYR D 2 108 ? 19.673  4.562   -11.366 1.00 27.10 ?  108 TYR D N   1 
ATOM   6706 C CA  . TYR D 2 108 ? 19.511  3.243   -10.762 1.00 26.49 ?  108 TYR D CA  1 
ATOM   6707 C C   . TYR D 2 108 ? 20.661  2.291   -11.072 1.00 24.51 ?  108 TYR D C   1 
ATOM   6708 O O   . TYR D 2 108 ? 20.752  1.235   -10.438 1.00 24.62 ?  108 TYR D O   1 
ATOM   6709 C CB  . TYR D 2 108 ? 18.170  2.638   -11.197 1.00 28.69 ?  108 TYR D CB  1 
ATOM   6710 C CG  . TYR D 2 108 ? 18.239  1.560   -12.261 1.00 25.22 ?  108 TYR D CG  1 
ATOM   6711 C CD1 . TYR D 2 108 ? 18.789  1.812   -13.514 1.00 26.84 ?  108 TYR D CD1 1 
ATOM   6712 C CD2 . TYR D 2 108 ? 17.732  0.291   -12.013 1.00 20.65 ?  108 TYR D CD2 1 
ATOM   6713 C CE1 . TYR D 2 108 ? 18.850  0.824   -14.478 1.00 27.25 ?  108 TYR D CE1 1 
ATOM   6714 C CE2 . TYR D 2 108 ? 17.782  -0.700  -12.974 1.00 26.06 ?  108 TYR D CE2 1 
ATOM   6715 C CZ  . TYR D 2 108 ? 18.340  -0.427  -14.205 1.00 30.37 ?  108 TYR D CZ  1 
ATOM   6716 O OH  . TYR D 2 108 ? 18.391  -1.414  -15.163 1.00 28.24 ?  108 TYR D OH  1 
ATOM   6717 N N   . GLY D 2 109 ? 21.536  2.636   -12.015 1.00 25.82 ?  109 GLY D N   1 
ATOM   6718 C CA  . GLY D 2 109 ? 22.686  1.806   -12.319 1.00 24.92 ?  109 GLY D CA  1 
ATOM   6719 C C   . GLY D 2 109 ? 24.003  2.390   -11.843 1.00 28.08 ?  109 GLY D C   1 
ATOM   6720 O O   . GLY D 2 109 ? 25.068  2.014   -12.342 1.00 26.06 ?  109 GLY D O   1 
ATOM   6721 N N   . ARG D 2 110 ? 23.947  3.295   -10.860 1.00 26.36 ?  110 ARG D N   1 
ATOM   6722 C CA  . ARG D 2 110 ? 25.139  4.032   -10.448 1.00 26.25 ?  110 ARG D CA  1 
ATOM   6723 C C   . ARG D 2 110 ? 26.156  3.165   -9.716  1.00 27.25 ?  110 ARG D C   1 
ATOM   6724 O O   . ARG D 2 110 ? 27.309  3.582   -9.568  1.00 24.29 ?  110 ARG D O   1 
ATOM   6725 C CB  . ARG D 2 110 ? 24.749  5.220   -9.566  1.00 29.36 ?  110 ARG D CB  1 
ATOM   6726 C CG  . ARG D 2 110 ? 23.999  4.854   -8.291  1.00 27.37 ?  110 ARG D CG  1 
ATOM   6727 C CD  . ARG D 2 110 ? 23.327  6.088   -7.708  1.00 26.40 ?  110 ARG D CD  1 
ATOM   6728 N NE  . ARG D 2 110 ? 22.653  5.835   -6.440  1.00 26.55 ?  110 ARG D NE  1 
ATOM   6729 C CZ  . ARG D 2 110 ? 21.393  5.436   -6.325  1.00 25.53 ?  110 ARG D CZ  1 
ATOM   6730 N NH1 . ARG D 2 110 ? 20.642  5.202   -7.389  1.00 25.91 ?  110 ARG D NH1 1 
ATOM   6731 N NH2 . ARG D 2 110 ? 20.873  5.271   -5.112  1.00 25.80 ?  110 ARG D NH2 1 
ATOM   6732 N N   . ARG D 2 111 ? 25.767  1.980   -9.256  1.00 26.02 ?  111 ARG D N   1 
ATOM   6733 C CA  . ARG D 2 111 ? 26.681  1.099   -8.543  1.00 27.80 ?  111 ARG D CA  1 
ATOM   6734 C C   . ARG D 2 111 ? 27.456  0.168   -9.468  1.00 28.83 ?  111 ARG D C   1 
ATOM   6735 O O   . ARG D 2 111 ? 28.313  -0.582  -8.989  1.00 29.96 ?  111 ARG D O   1 
ATOM   6736 C CB  . ARG D 2 111 ? 25.915  0.267   -7.509  1.00 25.00 ?  111 ARG D CB  1 
ATOM   6737 C CG  . ARG D 2 111 ? 25.340  1.075   -6.358  1.00 24.73 ?  111 ARG D CG  1 
ATOM   6738 C CD  . ARG D 2 111 ? 24.349  0.252   -5.552  1.00 24.53 ?  111 ARG D CD  1 
ATOM   6739 N NE  . ARG D 2 111 ? 23.612  1.067   -4.594  1.00 27.46 ?  111 ARG D NE  1 
ATOM   6740 C CZ  . ARG D 2 111 ? 22.442  1.640   -4.842  1.00 29.49 ?  111 ARG D CZ  1 
ATOM   6741 N NH1 . ARG D 2 111 ? 21.839  1.503   -6.011  1.00 32.79 ?  111 ARG D NH1 1 
ATOM   6742 N NH2 . ARG D 2 111 ? 21.863  2.370   -3.892  1.00 26.65 ?  111 ARG D NH2 1 
ATOM   6743 N N   . PHE D 2 112 ? 27.190  0.203   -10.771 1.00 26.96 ?  112 PHE D N   1 
ATOM   6744 C CA  . PHE D 2 112 ? 27.771  -0.752  -11.705 1.00 25.26 ?  112 PHE D CA  1 
ATOM   6745 C C   . PHE D 2 112 ? 29.075  -0.215  -12.281 1.00 27.93 ?  112 PHE D C   1 
ATOM   6746 O O   . PHE D 2 112 ? 29.135  0.929   -12.744 1.00 28.12 ?  112 PHE D O   1 
ATOM   6747 C CB  . PHE D 2 112 ? 26.779  -1.066  -12.825 1.00 29.60 ?  112 PHE D CB  1 
ATOM   6748 C CG  . PHE D 2 112 ? 25.684  -2.006  -12.412 1.00 33.84 ?  112 PHE D CG  1 
ATOM   6749 C CD1 . PHE D 2 112 ? 25.981  -3.187  -11.752 1.00 36.69 ?  112 PHE D CD1 1 
ATOM   6750 C CD2 . PHE D 2 112 ? 24.358  -1.706  -12.676 1.00 28.48 ?  112 PHE D CD2 1 
ATOM   6751 C CE1 . PHE D 2 112 ? 24.976  -4.055  -11.367 1.00 35.55 ?  112 PHE D CE1 1 
ATOM   6752 C CE2 . PHE D 2 112 ? 23.348  -2.568  -12.292 1.00 29.56 ?  112 PHE D CE2 1 
ATOM   6753 C CZ  . PHE D 2 112 ? 23.658  -3.745  -11.638 1.00 36.93 ?  112 PHE D CZ  1 
ATOM   6754 N N   . VAL D 2 113 ? 30.115  -1.055  -12.254 1.00 29.57 ?  113 VAL D N   1 
ATOM   6755 C CA  . VAL D 2 113 ? 31.430  -0.654  -12.750 1.00 31.13 ?  113 VAL D CA  1 
ATOM   6756 C C   . VAL D 2 113 ? 31.358  -0.282  -14.226 1.00 31.90 ?  113 VAL D C   1 
ATOM   6757 O O   . VAL D 2 113 ? 31.980  0.693   -14.669 1.00 28.79 ?  113 VAL D O   1 
ATOM   6758 C CB  . VAL D 2 113 ? 32.455  -1.778  -12.497 1.00 32.27 ?  113 VAL D CB  1 
ATOM   6759 C CG1 . VAL D 2 113 ? 33.580  -1.741  -13.526 1.00 38.65 ?  113 VAL D CG1 1 
ATOM   6760 C CG2 . VAL D 2 113 ? 33.013  -1.687  -11.086 1.00 37.74 ?  113 VAL D CG2 1 
ATOM   6761 N N   . GLU D 2 114 ? 30.584  -1.039  -15.007 1.00 33.57 ?  114 GLU D N   1 
ATOM   6762 C CA  . GLU D 2 114 ? 30.553  -0.841  -16.452 1.00 29.95 ?  114 GLU D CA  1 
ATOM   6763 C C   . GLU D 2 114 ? 29.887  0.467   -16.858 1.00 29.85 ?  114 GLU D C   1 
ATOM   6764 O O   . GLU D 2 114 ? 30.160  0.968   -17.954 1.00 28.15 ?  114 GLU D O   1 
ATOM   6765 C CB  . GLU D 2 114 ? 29.837  -2.009  -17.130 1.00 30.46 ?  114 GLU D CB  1 
ATOM   6766 C CG  . GLU D 2 114 ? 30.547  -3.349  -17.009 1.00 36.24 ?  114 GLU D CG  1 
ATOM   6767 C CD  . GLU D 2 114 ? 30.239  -4.062  -15.706 1.00 37.27 ?  114 GLU D CD  1 
ATOM   6768 O OE1 . GLU D 2 114 ? 29.414  -3.545  -14.922 1.00 36.36 ?  114 GLU D OE1 1 
ATOM   6769 O OE2 . GLU D 2 114 ? 30.815  -5.144  -15.470 1.00 41.78 ?  114 GLU D OE2 1 
ATOM   6770 N N   . GLU D 2 115 ? 29.020  1.029   -16.013 1.00 32.85 ?  115 GLU D N   1 
ATOM   6771 C CA  . GLU D 2 115 ? 28.356  2.278   -16.367 1.00 32.67 ?  115 GLU D CA  1 
ATOM   6772 C C   . GLU D 2 115 ? 29.324  3.451   -16.436 1.00 29.17 ?  115 GLU D C   1 
ATOM   6773 O O   . GLU D 2 115 ? 29.000  4.470   -17.053 1.00 29.31 ?  115 GLU D O   1 
ATOM   6774 C CB  . GLU D 2 115 ? 27.239  2.589   -15.369 1.00 31.00 ?  115 GLU D CB  1 
ATOM   6775 C CG  . GLU D 2 115 ? 25.923  1.884   -15.662 1.00 29.91 ?  115 GLU D CG  1 
ATOM   6776 C CD  . GLU D 2 115 ? 25.620  1.792   -17.146 1.00 33.45 ?  115 GLU D CD  1 
ATOM   6777 O OE1 . GLU D 2 115 ? 25.553  2.849   -17.811 1.00 37.01 ?  115 GLU D OE1 1 
ATOM   6778 O OE2 . GLU D 2 115 ? 25.445  0.662   -17.648 1.00 36.34 ?  115 GLU D OE2 1 
ATOM   6779 N N   . TYR D 2 116 ? 30.500  3.328   -15.830 1.00 29.39 ?  116 TYR D N   1 
ATOM   6780 C CA  . TYR D 2 116 ? 31.456  4.423   -15.780 1.00 29.54 ?  116 TYR D CA  1 
ATOM   6781 C C   . TYR D 2 116 ? 32.454  4.305   -16.923 1.00 30.53 ?  116 TYR D C   1 
ATOM   6782 O O   . TYR D 2 116 ? 32.880  3.205   -17.285 1.00 31.91 ?  116 TYR D O   1 
ATOM   6783 C CB  . TYR D 2 116 ? 32.173  4.440   -14.431 1.00 27.15 ?  116 TYR D CB  1 
ATOM   6784 C CG  . TYR D 2 116 ? 31.246  4.816   -13.300 1.00 26.51 ?  116 TYR D CG  1 
ATOM   6785 C CD1 . TYR D 2 116 ? 30.358  3.890   -12.769 1.00 25.60 ?  116 TYR D CD1 1 
ATOM   6786 C CD2 . TYR D 2 116 ? 31.238  6.103   -12.780 1.00 25.44 ?  116 TYR D CD2 1 
ATOM   6787 C CE1 . TYR D 2 116 ? 29.497  4.231   -11.749 1.00 22.21 ?  116 TYR D CE1 1 
ATOM   6788 C CE2 . TYR D 2 116 ? 30.381  6.452   -11.754 1.00 24.48 ?  116 TYR D CE2 1 
ATOM   6789 C CZ  . TYR D 2 116 ? 29.514  5.511   -11.242 1.00 22.50 ?  116 TYR D CZ  1 
ATOM   6790 O OH  . TYR D 2 116 ? 28.657  5.849   -10.221 1.00 23.55 ?  116 TYR D OH  1 
ATOM   6791 N N   . ASP D 2 117 ? 32.817  5.454   -17.492 1.00 29.55 ?  117 ASP D N   1 
ATOM   6792 C CA  . ASP D 2 117 ? 33.604  5.501   -18.712 1.00 30.35 ?  117 ASP D CA  1 
ATOM   6793 C C   . ASP D 2 117 ? 34.990  6.100   -18.534 1.00 33.73 ?  117 ASP D C   1 
ATOM   6794 O O   . ASP D 2 117 ? 35.821  5.961   -19.439 1.00 34.40 ?  117 ASP D O   1 
ATOM   6795 C CB  . ASP D 2 117 ? 32.848  6.290   -19.792 1.00 29.45 ?  117 ASP D CB  1 
ATOM   6796 C CG  . ASP D 2 117 ? 31.350  6.068   -19.728 1.00 29.44 ?  117 ASP D CG  1 
ATOM   6797 O OD1 . ASP D 2 117 ? 30.905  4.930   -19.988 1.00 36.32 ?  117 ASP D OD1 1 
ATOM   6798 O OD2 . ASP D 2 117 ? 30.616  7.025   -19.404 1.00 26.42 ?  117 ASP D OD2 1 
ATOM   6799 N N   . TYR D 2 118 ? 35.264  6.760   -17.411 1.00 35.24 ?  118 TYR D N   1 
ATOM   6800 C CA  . TYR D 2 118 ? 36.588  7.282   -17.110 1.00 34.45 ?  118 TYR D CA  1 
ATOM   6801 C C   . TYR D 2 118 ? 36.995  6.836   -15.712 1.00 37.14 ?  118 TYR D C   1 
ATOM   6802 O O   . TYR D 2 118 ? 36.156  6.703   -14.816 1.00 38.12 ?  118 TYR D O   1 
ATOM   6803 C CB  . TYR D 2 118 ? 36.631  8.813   -17.224 1.00 36.87 ?  118 TYR D CB  1 
ATOM   6804 C CG  . TYR D 2 118 ? 36.290  9.330   -18.606 1.00 36.49 ?  118 TYR D CG  1 
ATOM   6805 C CD1 . TYR D 2 118 ? 36.939  8.841   -19.732 1.00 39.27 ?  118 TYR D CD1 1 
ATOM   6806 C CD2 . TYR D 2 118 ? 35.320  10.306  -18.784 1.00 36.25 ?  118 TYR D CD2 1 
ATOM   6807 C CE1 . TYR D 2 118 ? 36.631  9.308   -20.997 1.00 45.29 ?  118 TYR D CE1 1 
ATOM   6808 C CE2 . TYR D 2 118 ? 35.005  10.779  -20.045 1.00 37.29 ?  118 TYR D CE2 1 
ATOM   6809 C CZ  . TYR D 2 118 ? 35.663  10.277  -21.147 1.00 40.36 ?  118 TYR D CZ  1 
ATOM   6810 O OH  . TYR D 2 118 ? 35.353  10.747  -22.402 1.00 40.40 ?  118 TYR D OH  1 
ATOM   6811 N N   . TRP D 2 119 ? 38.297  6.612   -15.536 1.00 38.29 ?  119 TRP D N   1 
ATOM   6812 C CA  . TRP D 2 119 ? 38.833  5.957   -14.352 1.00 37.00 ?  119 TRP D CA  1 
ATOM   6813 C C   . TRP D 2 119 ? 40.196  6.538   -14.009 1.00 40.09 ?  119 TRP D C   1 
ATOM   6814 O O   . TRP D 2 119 ? 40.972  6.909   -14.893 1.00 39.52 ?  119 TRP D O   1 
ATOM   6815 C CB  . TRP D 2 119 ? 38.984  4.443   -14.561 1.00 36.33 ?  119 TRP D CB  1 
ATOM   6816 C CG  . TRP D 2 119 ? 37.698  3.689   -14.660 1.00 34.34 ?  119 TRP D CG  1 
ATOM   6817 C CD1 . TRP D 2 119 ? 36.964  3.466   -15.788 1.00 37.13 ?  119 TRP D CD1 1 
ATOM   6818 C CD2 . TRP D 2 119 ? 37.004  3.034   -13.592 1.00 37.91 ?  119 TRP D CD2 1 
ATOM   6819 N NE1 . TRP D 2 119 ? 35.848  2.722   -15.487 1.00 36.67 ?  119 TRP D NE1 1 
ATOM   6820 C CE2 . TRP D 2 119 ? 35.850  2.444   -14.145 1.00 37.85 ?  119 TRP D CE2 1 
ATOM   6821 C CE3 . TRP D 2 119 ? 37.242  2.893   -12.221 1.00 35.62 ?  119 TRP D CE3 1 
ATOM   6822 C CZ2 . TRP D 2 119 ? 34.936  1.725   -13.376 1.00 37.32 ?  119 TRP D CZ2 1 
ATOM   6823 C CZ3 . TRP D 2 119 ? 36.334  2.180   -11.459 1.00 35.36 ?  119 TRP D CZ3 1 
ATOM   6824 C CH2 . TRP D 2 119 ? 35.196  1.605   -12.039 1.00 37.34 ?  119 TRP D CH2 1 
ATOM   6825 N N   . GLY D 2 120 ? 40.490  6.596   -12.715 1.00 37.50 ?  120 GLY D N   1 
ATOM   6826 C CA  . GLY D 2 120 ? 41.841  6.870   -12.284 1.00 38.58 ?  120 GLY D CA  1 
ATOM   6827 C C   . GLY D 2 120 ? 42.712  5.632   -12.377 1.00 42.64 ?  120 GLY D C   1 
ATOM   6828 O O   . GLY D 2 120 ? 42.248  4.528   -12.663 1.00 38.74 ?  120 GLY D O   1 
ATOM   6829 N N   . GLN D 2 121 ? 44.009  5.826   -12.138 1.00 44.69 ?  121 GLN D N   1 
ATOM   6830 C CA  . GLN D 2 121 ? 44.930  4.696   -12.121 1.00 43.98 ?  121 GLN D CA  1 
ATOM   6831 C C   . GLN D 2 121 ? 44.941  3.980   -10.778 1.00 42.10 ?  121 GLN D C   1 
ATOM   6832 O O   . GLN D 2 121 ? 45.401  2.835   -10.706 1.00 43.07 ?  121 GLN D O   1 
ATOM   6833 C CB  . GLN D 2 121 ? 46.347  5.151   -12.483 1.00 43.94 ?  121 GLN D CB  1 
ATOM   6834 C CG  . GLN D 2 121 ? 47.035  5.993   -11.423 1.00 49.33 ?  121 GLN D CG  1 
ATOM   6835 C CD  . GLN D 2 121 ? 46.413  7.364   -11.272 1.00 52.91 ?  121 GLN D CD  1 
ATOM   6836 O OE1 . GLN D 2 121 ? 45.953  7.962   -12.245 1.00 54.19 ?  121 GLN D OE1 1 
ATOM   6837 N NE2 . GLN D 2 121 ? 46.389  7.869   -10.044 1.00 46.68 ?  121 GLN D NE2 1 
ATOM   6838 N N   . GLY D 2 122 ? 44.454  4.618   -9.728  1.00 45.03 ?  122 GLY D N   1 
ATOM   6839 C CA  . GLY D 2 122 ? 44.272  3.955   -8.455  1.00 43.33 ?  122 GLY D CA  1 
ATOM   6840 C C   . GLY D 2 122 ? 45.238  4.457   -7.396  1.00 43.02 ?  122 GLY D C   1 
ATOM   6841 O O   . GLY D 2 122 ? 46.376  4.855   -7.683  1.00 40.27 ?  122 GLY D O   1 
ATOM   6842 N N   . THR D 2 123 ? 44.773  4.446   -6.150  1.00 40.42 ?  123 THR D N   1 
ATOM   6843 C CA  . THR D 2 123 ? 45.603  4.704   -4.983  1.00 37.56 ?  123 THR D CA  1 
ATOM   6844 C C   . THR D 2 123 ? 45.512  3.503   -4.050  1.00 38.82 ?  123 THR D C   1 
ATOM   6845 O O   . THR D 2 123 ? 44.443  2.903   -3.897  1.00 36.93 ?  123 THR D O   1 
ATOM   6846 C CB  . THR D 2 123 ? 45.180  5.998   -4.261  1.00 35.59 ?  123 THR D CB  1 
ATOM   6847 O OG1 . THR D 2 123 ? 46.120  6.302   -3.222  1.00 41.00 ?  123 THR D OG1 1 
ATOM   6848 C CG2 . THR D 2 123 ? 43.780  5.877   -3.668  1.00 33.17 ?  123 THR D CG2 1 
ATOM   6849 N N   . GLN D 2 124 ? 46.641  3.133   -3.453  1.00 39.99 ?  124 GLN D N   1 
ATOM   6850 C CA  . GLN D 2 124 ? 46.715  1.921   -2.647  1.00 35.81 ?  124 GLN D CA  1 
ATOM   6851 C C   . GLN D 2 124 ? 46.467  2.255   -1.182  1.00 35.53 ?  124 GLN D C   1 
ATOM   6852 O O   . GLN D 2 124 ? 47.197  3.055   -0.587  1.00 37.97 ?  124 GLN D O   1 
ATOM   6853 C CB  . GLN D 2 124 ? 48.067  1.231   -2.815  1.00 35.98 ?  124 GLN D CB  1 
ATOM   6854 C CG  . GLN D 2 124 ? 48.248  0.025   -1.904  1.00 34.06 ?  124 GLN D CG  1 
ATOM   6855 C CD  . GLN D 2 124 ? 47.333  -1.128  -2.273  1.00 39.48 ?  124 GLN D CD  1 
ATOM   6856 O OE1 . GLN D 2 124 ? 46.509  -1.564  -1.469  1.00 36.57 ?  124 GLN D OE1 1 
ATOM   6857 N NE2 . GLN D 2 124 ? 47.478  -1.633  -3.492  1.00 38.13 ?  124 GLN D NE2 1 
ATOM   6858 N N   . VAL D 2 125 ? 45.436  1.641   -0.609  1.00 35.55 ?  125 VAL D N   1 
ATOM   6859 C CA  . VAL D 2 125 ? 45.152  1.712   0.818   1.00 35.50 ?  125 VAL D CA  1 
ATOM   6860 C C   . VAL D 2 125 ? 45.350  0.320   1.400   1.00 37.74 ?  125 VAL D C   1 
ATOM   6861 O O   . VAL D 2 125 ? 44.784  -0.657  0.895   1.00 36.05 ?  125 VAL D O   1 
ATOM   6862 C CB  . VAL D 2 125 ? 43.728  2.226   1.090   1.00 37.53 ?  125 VAL D CB  1 
ATOM   6863 C CG1 . VAL D 2 125 ? 43.467  2.297   2.589   1.00 34.39 ?  125 VAL D CG1 1 
ATOM   6864 C CG2 . VAL D 2 125 ? 43.523  3.587   0.441   1.00 36.97 ?  125 VAL D CG2 1 
ATOM   6865 N N   . THR D 2 126 ? 46.159  0.229   2.453   1.00 41.23 ?  126 THR D N   1 
ATOM   6866 C CA  . THR D 2 126 ? 46.454  -1.039  3.106   1.00 41.93 ?  126 THR D CA  1 
ATOM   6867 C C   . THR D 2 126 ? 46.277  -0.875  4.607   1.00 38.88 ?  126 THR D C   1 
ATOM   6868 O O   . THR D 2 126 ? 46.886  0.012   5.214   1.00 41.81 ?  126 THR D O   1 
ATOM   6869 C CB  . THR D 2 126 ? 47.874  -1.515  2.781   1.00 40.35 ?  126 THR D CB  1 
ATOM   6870 O OG1 . THR D 2 126 ? 48.763  -0.392  2.753   1.00 46.65 ?  126 THR D OG1 1 
ATOM   6871 C CG2 . THR D 2 126 ? 47.902  -2.207  1.427   1.00 37.22 ?  126 THR D CG2 1 
ATOM   6872 N N   . VAL D 2 127 ? 45.444  -1.728  5.198   1.00 38.96 ?  127 VAL D N   1 
ATOM   6873 C CA  . VAL D 2 127 ? 45.090  -1.653  6.611   1.00 41.20 ?  127 VAL D CA  1 
ATOM   6874 C C   . VAL D 2 127 ? 45.567  -2.937  7.275   1.00 41.19 ?  127 VAL D C   1 
ATOM   6875 O O   . VAL D 2 127 ? 45.063  -4.026  6.970   1.00 40.57 ?  127 VAL D O   1 
ATOM   6876 C CB  . VAL D 2 127 ? 43.582  -1.454  6.813   1.00 40.21 ?  127 VAL D CB  1 
ATOM   6877 C CG1 . VAL D 2 127 ? 43.275  -1.170  8.273   1.00 39.32 ?  127 VAL D CG1 1 
ATOM   6878 C CG2 . VAL D 2 127 ? 43.068  -0.333  5.919   1.00 38.22 ?  127 VAL D CG2 1 
ATOM   6879 N N   . SER D 2 128 ? 46.527  -2.813  8.185   1.00 48.17 ?  128 SER D N   1 
ATOM   6880 C CA  . SER D 2 128 ? 47.141  -3.956  8.844   1.00 49.89 ?  128 SER D CA  1 
ATOM   6881 C C   . SER D 2 128 ? 46.562  -4.158  10.239  1.00 48.99 ?  128 SER D C   1 
ATOM   6882 O O   . SER D 2 128 ? 45.946  -3.263  10.823  1.00 46.34 ?  128 SER D O   1 
ATOM   6883 C CB  . SER D 2 128 ? 48.660  -3.778  8.932   1.00 49.52 ?  128 SER D CB  1 
ATOM   6884 O OG  . SER D 2 128 ? 48.997  -2.476  9.378   1.00 51.43 ?  128 SER D OG  1 
ATOM   6885 N N   . SER D 2 129 ? 46.775  -5.358  10.769  1.00 51.21 ?  129 SER D N   1 
ATOM   6886 C CA  . SER D 2 129 ? 46.290  -5.711  12.097  1.00 54.24 ?  129 SER D CA  1 
ATOM   6887 C C   . SER D 2 129 ? 47.432  -6.202  12.981  1.00 50.68 ?  129 SER D C   1 
ATOM   6888 O O   . SER D 2 129 ? 48.386  -6.811  12.496  1.00 50.26 ?  129 SER D O   1 
ATOM   6889 C CB  . SER D 2 129 ? 45.196  -6.777  12.003  1.00 48.54 ?  129 SER D CB  1 
ATOM   6890 O OG  . SER D 2 129 ? 45.537  -7.783  11.065  1.00 45.20 ?  129 SER D OG  1 
HETATM 6891 O O   . HOH E 3 .   ? -4.166  23.086  -31.656 1.00 21.68 ?  601 HOH A O   1 
HETATM 6892 O O   . HOH E 3 .   ? 18.398  -3.544  -25.995 1.00 28.38 ?  602 HOH A O   1 
HETATM 6893 O O   . HOH E 3 .   ? -3.400  29.197  -18.377 1.00 26.87 ?  603 HOH A O   1 
HETATM 6894 O O   . HOH E 3 .   ? -9.229  10.128  -39.198 1.00 24.65 ?  604 HOH A O   1 
HETATM 6895 O O   . HOH E 3 .   ? 15.534  -15.767 -18.096 1.00 30.69 ?  605 HOH A O   1 
HETATM 6896 O O   . HOH E 3 .   ? 10.297  5.414   -24.782 1.00 20.92 ?  606 HOH A O   1 
HETATM 6897 O O   . HOH E 3 .   ? -20.261 36.480  -17.921 1.00 25.66 ?  607 HOH A O   1 
HETATM 6898 O O   . HOH E 3 .   ? 4.076   -7.694  -9.753  1.00 26.97 ?  608 HOH A O   1 
HETATM 6899 O O   . HOH E 3 .   ? 0.303   11.641  -21.030 1.00 18.81 ?  609 HOH A O   1 
HETATM 6900 O O   . HOH E 3 .   ? -23.485 18.257  -35.598 1.00 29.06 ?  610 HOH A O   1 
HETATM 6901 O O   . HOH E 3 .   ? -13.049 18.139  -39.432 1.00 18.95 ?  611 HOH A O   1 
HETATM 6902 O O   . HOH E 3 .   ? -19.574 25.494  -32.269 1.00 21.55 ?  612 HOH A O   1 
HETATM 6903 O O   . HOH E 3 .   ? -19.580 13.460  -22.411 1.00 22.11 ?  613 HOH A O   1 
HETATM 6904 O O   . HOH E 3 .   ? -10.781 17.351  -23.184 1.00 19.48 ?  614 HOH A O   1 
HETATM 6905 O O   . HOH E 3 .   ? 8.245   -19.671 -9.810  1.00 39.84 ?  615 HOH A O   1 
HETATM 6906 O O   . HOH E 3 .   ? 11.211  -2.505  -25.901 1.00 22.39 ?  616 HOH A O   1 
HETATM 6907 O O   . HOH E 3 .   ? -11.384 -10.616 -23.466 1.00 39.37 ?  617 HOH A O   1 
HETATM 6908 O O   . HOH E 3 .   ? -1.544  5.731   -15.046 1.00 13.60 ?  618 HOH A O   1 
HETATM 6909 O O   . HOH E 3 .   ? -14.980 0.138   -30.251 1.00 22.92 ?  619 HOH A O   1 
HETATM 6910 O O   . HOH E 3 .   ? 13.430  7.979   -21.091 1.00 20.17 ?  620 HOH A O   1 
HETATM 6911 O O   . HOH E 3 .   ? -4.729  10.548  -2.642  1.00 26.08 ?  621 HOH A O   1 
HETATM 6912 O O   . HOH E 3 .   ? 4.404   -19.274 -18.903 1.00 35.46 ?  622 HOH A O   1 
HETATM 6913 O O   . HOH E 3 .   ? -16.642 11.117  -15.319 1.00 22.67 ?  623 HOH A O   1 
HETATM 6914 O O   . HOH E 3 .   ? 11.097  -0.787  -8.271  1.00 25.37 ?  624 HOH A O   1 
HETATM 6915 O O   . HOH E 3 .   ? -3.289  6.361   -34.710 1.00 26.21 ?  625 HOH A O   1 
HETATM 6916 O O   . HOH E 3 .   ? -26.050 11.281  -20.927 1.00 31.81 ?  626 HOH A O   1 
HETATM 6917 O O   . HOH E 3 .   ? -2.557  5.476   -20.511 1.00 19.86 ?  627 HOH A O   1 
HETATM 6918 O O   . HOH E 3 .   ? -10.681 1.415   -10.918 1.00 33.21 ?  628 HOH A O   1 
HETATM 6919 O O   . HOH E 3 .   ? -20.178 21.993  -19.078 1.00 31.95 ?  629 HOH A O   1 
HETATM 6920 O O   . HOH E 3 .   ? -2.238  2.586   -4.795  1.00 20.66 ?  630 HOH A O   1 
HETATM 6921 O O   . HOH E 3 .   ? -25.828 25.852  -26.642 1.00 25.08 ?  631 HOH A O   1 
HETATM 6922 O O   . HOH E 3 .   ? 22.221  -3.317  -18.642 1.00 27.10 ?  632 HOH A O   1 
HETATM 6923 O O   . HOH E 3 .   ? -23.015 25.629  -23.901 1.00 24.66 ?  633 HOH A O   1 
HETATM 6924 O O   . HOH E 3 .   ? -8.036  18.313  -13.813 1.00 22.15 ?  634 HOH A O   1 
HETATM 6925 O O   . HOH E 3 .   ? -14.751 -2.292  -24.248 1.00 23.47 ?  635 HOH A O   1 
HETATM 6926 O O   . HOH E 3 .   ? 17.305  -7.397  -15.737 1.00 23.84 ?  636 HOH A O   1 
HETATM 6927 O O   . HOH E 3 .   ? 9.118   -22.487 -17.252 1.00 41.65 ?  637 HOH A O   1 
HETATM 6928 O O   . HOH E 3 .   ? -11.592 23.900  -14.573 1.00 18.46 ?  638 HOH A O   1 
HETATM 6929 O O   . HOH E 3 .   ? -23.204 7.610   -21.144 1.00 31.77 ?  639 HOH A O   1 
HETATM 6930 O O   . HOH E 3 .   ? 0.285   28.059  -20.489 1.00 26.72 ?  640 HOH A O   1 
HETATM 6931 O O   . HOH E 3 .   ? 3.195   -16.818 -13.169 1.00 39.40 ?  641 HOH A O   1 
HETATM 6932 O O   . HOH E 3 .   ? -12.759 0.483   -23.874 1.00 21.63 ?  642 HOH A O   1 
HETATM 6933 O O   . HOH E 3 .   ? -20.100 23.699  -29.352 1.00 21.93 ?  643 HOH A O   1 
HETATM 6934 O O   . HOH E 3 .   ? -9.516  37.269  -23.159 1.00 26.02 ?  644 HOH A O   1 
HETATM 6935 O O   . HOH E 3 .   ? -23.640 7.173   -32.359 1.00 27.79 ?  645 HOH A O   1 
HETATM 6936 O O   . HOH E 3 .   ? -7.779  35.224  -31.682 1.00 32.51 ?  646 HOH A O   1 
HETATM 6937 O O   . HOH E 3 .   ? -6.383  17.402  -17.136 1.00 16.41 ?  647 HOH A O   1 
HETATM 6938 O O   . HOH E 3 .   ? -3.859  18.469  -41.149 1.00 26.05 ?  648 HOH A O   1 
HETATM 6939 O O   . HOH E 3 .   ? -11.249 6.642   -16.306 1.00 22.34 ?  649 HOH A O   1 
HETATM 6940 O O   . HOH E 3 .   ? -4.193  0.706   -5.762  1.00 21.60 ?  650 HOH A O   1 
HETATM 6941 O O   . HOH E 3 .   ? -7.337  -5.978  -23.354 1.00 23.00 ?  651 HOH A O   1 
HETATM 6942 O O   . HOH E 3 .   ? -18.733 25.160  -18.601 1.00 31.00 ?  652 HOH A O   1 
HETATM 6943 O O   . HOH E 3 .   ? -0.115  28.660  -23.311 1.00 24.09 ?  653 HOH A O   1 
HETATM 6944 O O   . HOH E 3 .   ? 5.004   -8.283  -29.969 1.00 25.55 ?  654 HOH A O   1 
HETATM 6945 O O   . HOH E 3 .   ? -6.079  12.641  -21.056 1.00 16.77 ?  655 HOH A O   1 
HETATM 6946 O O   . HOH E 3 .   ? 3.343   14.630  -13.040 1.00 19.51 ?  656 HOH A O   1 
HETATM 6947 O O   . HOH E 3 .   ? -18.569 -5.902  -25.554 1.00 28.60 ?  657 HOH A O   1 
HETATM 6948 O O   . HOH E 3 .   ? -24.240 9.493   -35.011 1.00 28.59 ?  658 HOH A O   1 
HETATM 6949 O O   . HOH E 3 .   ? 9.699   10.874  -19.176 1.00 22.68 ?  659 HOH A O   1 
HETATM 6950 O O   . HOH E 3 .   ? -15.802 3.886   -15.569 1.00 18.24 ?  660 HOH A O   1 
HETATM 6951 O O   . HOH E 3 .   ? -2.363  -12.339 -20.872 1.00 33.89 ?  661 HOH A O   1 
HETATM 6952 O O   . HOH E 3 .   ? -4.062  35.494  -21.793 1.00 25.63 ?  662 HOH A O   1 
HETATM 6953 O O   . HOH E 3 .   ? 22.527  -11.535 -27.326 1.00 21.27 ?  663 HOH A O   1 
HETATM 6954 O O   . HOH E 3 .   ? -12.605 12.735  -8.866  1.00 29.21 ?  664 HOH A O   1 
HETATM 6955 O O   . HOH E 3 .   ? -4.094  29.834  -29.598 1.00 24.56 ?  665 HOH A O   1 
HETATM 6956 O O   . HOH E 3 .   ? -2.503  4.638   -6.681  1.00 18.46 ?  666 HOH A O   1 
HETATM 6957 O O   . HOH E 3 .   ? 14.176  -22.400 -24.998 1.00 42.41 ?  667 HOH A O   1 
HETATM 6958 O O   . HOH E 3 .   ? -14.320 1.504   -20.083 1.00 15.41 ?  668 HOH A O   1 
HETATM 6959 O O   . HOH E 3 .   ? -22.128 13.007  -20.690 1.00 25.01 ?  669 HOH A O   1 
HETATM 6960 O O   . HOH E 3 .   ? -2.738  14.717  -9.493  1.00 17.17 ?  670 HOH A O   1 
HETATM 6961 O O   . HOH E 3 .   ? 14.067  1.626   -8.752  1.00 23.71 ?  671 HOH A O   1 
HETATM 6962 O O   . HOH E 3 .   ? -4.056  -4.586  -9.891  1.00 32.37 ?  672 HOH A O   1 
HETATM 6963 O O   . HOH E 3 .   ? 8.439   14.190  -17.913 1.00 23.18 ?  673 HOH A O   1 
HETATM 6964 O O   . HOH E 3 .   ? -4.875  0.313   -0.156  1.00 31.23 ?  674 HOH A O   1 
HETATM 6965 O O   . HOH E 3 .   ? 2.212   10.343  -19.570 1.00 16.60 ?  675 HOH A O   1 
HETATM 6966 O O   . HOH E 3 .   ? 18.704  2.186   -4.597  1.00 36.34 ?  676 HOH A O   1 
HETATM 6967 O O   . HOH E 3 .   ? -9.672  4.376   -8.652  1.00 25.99 ?  677 HOH A O   1 
HETATM 6968 O O   . HOH E 3 .   ? 10.001  8.071   -8.279  1.00 30.52 ?  678 HOH A O   1 
HETATM 6969 O O   . HOH E 3 .   ? -12.000 4.502   -13.345 1.00 24.54 ?  679 HOH A O   1 
HETATM 6970 O O   . HOH E 3 .   ? 6.147   13.843  -3.776  1.00 24.80 ?  680 HOH A O   1 
HETATM 6971 O O   . HOH E 3 .   ? 1.247   -7.161  -14.061 1.00 28.26 ?  681 HOH A O   1 
HETATM 6972 O O   . HOH E 3 .   ? 21.203  -13.736 -15.247 1.00 27.23 ?  682 HOH A O   1 
HETATM 6973 O O   . HOH E 3 .   ? 14.953  3.898   -25.677 1.00 23.29 ?  683 HOH A O   1 
HETATM 6974 O O   . HOH E 3 .   ? 1.775   14.463  -11.143 1.00 21.61 ?  684 HOH A O   1 
HETATM 6975 O O   . HOH E 3 .   ? -12.797 -0.756  -31.695 1.00 19.39 ?  685 HOH A O   1 
HETATM 6976 O O   . HOH E 3 .   ? -13.757 9.039   -8.786  1.00 30.32 ?  686 HOH A O   1 
HETATM 6977 O O   . HOH E 3 .   ? -20.806 12.965  -18.306 1.00 32.47 ?  687 HOH A O   1 
HETATM 6978 O O   . HOH E 3 .   ? -14.604 15.345  -9.717  1.00 34.64 ?  688 HOH A O   1 
HETATM 6979 O O   . HOH E 3 .   ? -15.962 7.719   -24.627 1.00 19.15 ?  689 HOH A O   1 
HETATM 6980 O O   . HOH E 3 .   ? 15.497  6.191   -22.002 1.00 27.11 ?  690 HOH A O   1 
HETATM 6981 O O   . HOH E 3 .   ? 0.295   -15.134 -14.246 1.00 34.04 ?  691 HOH A O   1 
HETATM 6982 O O   . HOH E 3 .   ? -19.857 -10.494 -30.279 1.00 18.80 ?  692 HOH A O   1 
HETATM 6983 O O   . HOH E 3 .   ? -1.147  -13.298 -28.306 1.00 28.42 ?  693 HOH A O   1 
HETATM 6984 O O   . HOH E 3 .   ? 2.766   2.383   -30.754 1.00 30.49 ?  694 HOH A O   1 
HETATM 6985 O O   . HOH E 3 .   ? 0.657   -10.360 -16.601 1.00 28.35 ?  695 HOH A O   1 
HETATM 6986 O O   . HOH E 3 .   ? 8.235   7.995   -11.725 1.00 20.57 ?  696 HOH A O   1 
HETATM 6987 O O   . HOH E 3 .   ? -11.413 -15.916 -34.063 1.00 36.14 ?  697 HOH A O   1 
HETATM 6988 O O   . HOH E 3 .   ? 16.847  -1.235  -24.286 1.00 28.61 ?  698 HOH A O   1 
HETATM 6989 O O   . HOH E 3 .   ? -22.115 -8.680  -22.303 1.00 30.01 ?  699 HOH A O   1 
HETATM 6990 O O   . HOH E 3 .   ? -13.184 -2.837  -33.960 1.00 22.71 ?  700 HOH A O   1 
HETATM 6991 O O   . HOH F 3 .   ? -5.907  -14.695 -38.171 1.00 33.05 ?  601 HOH B O   1 
HETATM 6992 O O   . HOH F 3 .   ? 12.055  36.870  -35.563 1.00 34.04 ?  602 HOH B O   1 
HETATM 6993 O O   . HOH F 3 .   ? 22.283  28.152  -42.287 1.00 19.87 ?  603 HOH B O   1 
HETATM 6994 O O   . HOH F 3 .   ? 15.194  7.930   -39.664 1.00 22.74 ?  604 HOH B O   1 
HETATM 6995 O O   . HOH F 3 .   ? 28.841  16.242  -43.513 1.00 27.06 ?  605 HOH B O   1 
HETATM 6996 O O   . HOH F 3 .   ? -1.302  8.236   -38.894 1.00 23.84 ?  606 HOH B O   1 
HETATM 6997 O O   . HOH F 3 .   ? 25.237  -12.943 -41.392 1.00 42.77 ?  607 HOH B O   1 
HETATM 6998 O O   . HOH F 3 .   ? 23.636  3.240   -35.180 1.00 26.73 ?  608 HOH B O   1 
HETATM 6999 O O   . HOH F 3 .   ? 27.176  22.539  -43.051 1.00 34.90 ?  609 HOH B O   1 
HETATM 7000 O O   . HOH F 3 .   ? 21.153  -11.390 -34.320 1.00 32.67 ?  610 HOH B O   1 
HETATM 7001 O O   . HOH F 3 .   ? -8.784  -2.791  -43.104 1.00 24.79 ?  611 HOH B O   1 
HETATM 7002 O O   . HOH F 3 .   ? 2.220   -13.643 -34.393 1.00 33.69 ?  612 HOH B O   1 
HETATM 7003 O O   . HOH F 3 .   ? 10.911  29.874  -32.949 1.00 26.18 ?  613 HOH B O   1 
HETATM 7004 O O   . HOH F 3 .   ? 13.946  9.254   -44.739 1.00 20.66 ?  614 HOH B O   1 
HETATM 7005 O O   . HOH F 3 .   ? -2.826  -5.844  -50.221 1.00 25.71 ?  615 HOH B O   1 
HETATM 7006 O O   . HOH F 3 .   ? 10.382  29.626  -35.934 1.00 21.98 ?  616 HOH B O   1 
HETATM 7007 O O   . HOH F 3 .   ? -2.851  11.611  -51.646 1.00 21.94 ?  617 HOH B O   1 
HETATM 7008 O O   . HOH F 3 .   ? 30.522  27.461  -24.615 1.00 27.01 ?  618 HOH B O   1 
HETATM 7009 O O   . HOH F 3 .   ? 18.498  -7.175  -51.319 1.00 30.99 ?  619 HOH B O   1 
HETATM 7010 O O   . HOH F 3 .   ? 36.953  22.036  -26.977 1.00 45.17 ?  620 HOH B O   1 
HETATM 7011 O O   . HOH F 3 .   ? 26.180  1.024   -29.393 1.00 24.18 ?  621 HOH B O   1 
HETATM 7012 O O   . HOH F 3 .   ? 14.951  7.767   -55.759 1.00 19.76 ?  622 HOH B O   1 
HETATM 7013 O O   . HOH F 3 .   ? 22.396  3.084   -49.900 1.00 32.01 ?  623 HOH B O   1 
HETATM 7014 O O   . HOH F 3 .   ? 31.049  26.449  -27.807 1.00 25.60 ?  624 HOH B O   1 
HETATM 7015 O O   . HOH F 3 .   ? 4.367   -14.219 -54.695 1.00 37.83 ?  625 HOH B O   1 
HETATM 7016 O O   . HOH F 3 .   ? -6.872  10.179  -45.270 1.00 23.31 ?  626 HOH B O   1 
HETATM 7017 O O   . HOH F 3 .   ? 21.237  -3.412  -38.710 1.00 25.07 ?  627 HOH B O   1 
HETATM 7018 O O   . HOH F 3 .   ? 25.516  3.322   -36.870 1.00 20.81 ?  628 HOH B O   1 
HETATM 7019 O O   . HOH F 3 .   ? 16.941  -0.445  -51.746 1.00 27.19 ?  629 HOH B O   1 
HETATM 7020 O O   . HOH F 3 .   ? 21.568  9.063   -42.899 1.00 22.78 ?  630 HOH B O   1 
HETATM 7021 O O   . HOH F 3 .   ? -6.599  4.436   -53.450 1.00 23.03 ?  631 HOH B O   1 
HETATM 7022 O O   . HOH F 3 .   ? -12.417 -5.439  -32.699 1.00 19.10 ?  632 HOH B O   1 
HETATM 7023 O O   . HOH F 3 .   ? 14.038  -0.508  -57.745 1.00 22.48 ?  633 HOH B O   1 
HETATM 7024 O O   . HOH F 3 .   ? 2.311   2.865   -52.721 1.00 28.69 ?  634 HOH B O   1 
HETATM 7025 O O   . HOH F 3 .   ? 16.695  6.015   -54.955 1.00 23.45 ?  635 HOH B O   1 
HETATM 7026 O O   . HOH F 3 .   ? 11.587  13.774  -38.010 1.00 19.18 ?  636 HOH B O   1 
HETATM 7027 O O   . HOH F 3 .   ? 14.669  18.315  -48.771 1.00 23.41 ?  637 HOH B O   1 
HETATM 7028 O O   . HOH F 3 .   ? 0.905   -17.626 -38.673 1.00 30.81 ?  638 HOH B O   1 
HETATM 7029 O O   . HOH F 3 .   ? 18.669  0.834   -49.753 1.00 24.43 ?  639 HOH B O   1 
HETATM 7030 O O   . HOH F 3 .   ? 14.285  28.567  -24.622 1.00 29.66 ?  640 HOH B O   1 
HETATM 7031 O O   . HOH F 3 .   ? -3.578  -5.850  -46.641 1.00 21.45 ?  641 HOH B O   1 
HETATM 7032 O O   . HOH F 3 .   ? 13.520  37.114  -33.648 1.00 31.11 ?  642 HOH B O   1 
HETATM 7033 O O   . HOH F 3 .   ? 18.564  35.577  -43.244 1.00 34.03 ?  643 HOH B O   1 
HETATM 7034 O O   . HOH F 3 .   ? 28.366  8.419   -44.735 1.00 28.81 ?  644 HOH B O   1 
HETATM 7035 O O   . HOH F 3 .   ? 3.425   -19.376 -49.827 1.00 41.02 ?  645 HOH B O   1 
HETATM 7036 O O   . HOH F 3 .   ? 9.319   -3.928  -52.753 1.00 31.07 ?  646 HOH B O   1 
HETATM 7037 O O   . HOH F 3 .   ? 18.089  15.383  -37.881 1.00 19.87 ?  647 HOH B O   1 
HETATM 7038 O O   . HOH F 3 .   ? 7.412   2.784   -31.821 1.00 25.85 ?  648 HOH B O   1 
HETATM 7039 O O   . HOH F 3 .   ? 17.561  20.802  -41.127 1.00 24.08 ?  649 HOH B O   1 
HETATM 7040 O O   . HOH F 3 .   ? -4.395  -3.820  -35.899 1.00 21.02 ?  650 HOH B O   1 
HETATM 7041 O O   . HOH F 3 .   ? 2.476   11.894  -39.750 1.00 21.75 ?  651 HOH B O   1 
HETATM 7042 O O   . HOH F 3 .   ? 27.988  6.793   -35.455 1.00 32.56 ?  652 HOH B O   1 
HETATM 7043 O O   . HOH F 3 .   ? 2.972   4.147   -33.284 1.00 26.13 ?  653 HOH B O   1 
HETATM 7044 O O   . HOH F 3 .   ? 19.256  21.995  -43.950 1.00 25.13 ?  654 HOH B O   1 
HETATM 7045 O O   . HOH F 3 .   ? 15.171  10.857  -21.646 1.00 23.31 ?  655 HOH B O   1 
HETATM 7046 O O   . HOH F 3 .   ? 9.386   -7.544  -32.675 1.00 21.62 ?  656 HOH B O   1 
HETATM 7047 O O   . HOH F 3 .   ? 21.428  10.754  -56.234 1.00 26.14 ?  657 HOH B O   1 
HETATM 7048 O O   . HOH F 3 .   ? 4.296   10.038  -45.852 1.00 25.42 ?  658 HOH B O   1 
HETATM 7049 O O   . HOH F 3 .   ? -9.164  -8.667  -51.559 1.00 30.51 ?  659 HOH B O   1 
HETATM 7050 O O   . HOH F 3 .   ? 14.904  9.357   -53.629 1.00 17.67 ?  660 HOH B O   1 
HETATM 7051 O O   . HOH F 3 .   ? 13.311  -6.113  -45.821 1.00 29.24 ?  661 HOH B O   1 
HETATM 7052 O O   . HOH F 3 .   ? -6.285  6.077   -56.009 1.00 24.73 ?  662 HOH B O   1 
HETATM 7053 O O   . HOH F 3 .   ? 22.586  -2.338  -49.566 1.00 36.36 ?  663 HOH B O   1 
HETATM 7054 O O   . HOH F 3 .   ? -2.910  -1.814  -37.438 1.00 19.36 ?  664 HOH B O   1 
HETATM 7055 O O   . HOH F 3 .   ? -0.963  -14.203 -46.358 1.00 27.58 ?  665 HOH B O   1 
HETATM 7056 O O   . HOH F 3 .   ? 31.569  17.579  -36.439 1.00 27.81 ?  666 HOH B O   1 
HETATM 7057 O O   . HOH F 3 .   ? 21.391  7.597   -53.968 1.00 28.08 ?  667 HOH B O   1 
HETATM 7058 O O   . HOH F 3 .   ? 19.235  15.531  -53.726 1.00 22.65 ?  668 HOH B O   1 
HETATM 7059 O O   . HOH F 3 .   ? 10.020  12.658  -40.001 1.00 20.36 ?  669 HOH B O   1 
HETATM 7060 O O   . HOH F 3 .   ? -6.641  -12.093 -48.125 1.00 23.23 ?  670 HOH B O   1 
HETATM 7061 O O   . HOH F 3 .   ? 12.429  -3.935  -47.975 1.00 27.16 ?  671 HOH B O   1 
HETATM 7062 O O   . HOH F 3 .   ? -1.330  4.599   -51.931 1.00 25.05 ?  672 HOH B O   1 
HETATM 7063 O O   . HOH F 3 .   ? 35.356  11.981  -38.261 1.00 36.33 ?  673 HOH B O   1 
HETATM 7064 O O   . HOH F 3 .   ? 27.102  5.043   -40.722 1.00 22.03 ?  674 HOH B O   1 
HETATM 7065 O O   . HOH F 3 .   ? 31.228  15.857  -42.547 1.00 32.67 ?  675 HOH B O   1 
HETATM 7066 O O   . HOH F 3 .   ? 22.175  9.613   -51.637 1.00 25.31 ?  676 HOH B O   1 
HETATM 7067 O O   . HOH F 3 .   ? 24.592  18.160  -49.896 1.00 27.27 ?  677 HOH B O   1 
HETATM 7068 O O   . HOH F 3 .   ? 32.854  36.506  -29.667 1.00 35.05 ?  678 HOH B O   1 
HETATM 7069 O O   . HOH F 3 .   ? -1.805  -11.829 -50.121 1.00 24.79 ?  679 HOH B O   1 
HETATM 7070 O O   . HOH F 3 .   ? 27.848  5.200   -33.589 1.00 37.36 ?  680 HOH B O   1 
HETATM 7071 O O   . HOH F 3 .   ? 16.930  16.072  -56.991 1.00 26.16 ?  681 HOH B O   1 
HETATM 7072 O O   . HOH F 3 .   ? -1.800  3.957   -35.156 1.00 21.08 ?  682 HOH B O   1 
HETATM 7073 O O   . HOH F 3 .   ? 3.110   16.472  -48.586 1.00 36.09 ?  683 HOH B O   1 
HETATM 7074 O O   . HOH F 3 .   ? 14.367  30.353  -26.077 1.00 29.70 ?  684 HOH B O   1 
HETATM 7075 O O   . HOH F 3 .   ? 22.065  -12.376 -29.628 1.00 28.23 ?  685 HOH B O   1 
HETATM 7076 O O   . HOH F 3 .   ? -3.077  4.250   -37.865 1.00 28.64 ?  686 HOH B O   1 
HETATM 7077 O O   . HOH F 3 .   ? 35.697  19.827  -22.612 1.00 44.21 ?  687 HOH B O   1 
HETATM 7078 O O   . HOH F 3 .   ? 19.322  -0.134  -25.919 1.00 29.83 ?  688 HOH B O   1 
HETATM 7079 O O   . HOH F 3 .   ? 1.139   11.533  -50.307 1.00 21.31 ?  689 HOH B O   1 
HETATM 7080 O O   . HOH F 3 .   ? 28.012  10.946  -34.846 1.00 25.14 ?  690 HOH B O   1 
HETATM 7081 O O   . HOH F 3 .   ? 3.464   -10.204 -32.400 1.00 33.10 ?  691 HOH B O   1 
HETATM 7082 O O   . HOH F 3 .   ? 4.148   10.937  -48.013 1.00 14.55 ?  692 HOH B O   1 
HETATM 7083 O O   . HOH F 3 .   ? 34.183  17.813  -38.060 1.00 24.76 ?  693 HOH B O   1 
HETATM 7084 O O   . HOH F 3 .   ? 1.932   27.401  -31.768 1.00 30.19 ?  694 HOH B O   1 
HETATM 7085 O O   . HOH F 3 .   ? 16.378  20.337  -48.995 1.00 30.46 ?  695 HOH B O   1 
HETATM 7086 O O   . HOH F 3 .   ? 2.920   16.789  -56.909 1.00 33.22 ?  696 HOH B O   1 
HETATM 7087 O O   . HOH F 3 .   ? 26.983  23.184  -8.165  1.00 34.75 ?  697 HOH B O   1 
HETATM 7088 O O   . HOH F 3 .   ? -10.959 -5.837  -49.487 1.00 34.17 ?  698 HOH B O   1 
HETATM 7089 O O   . HOH F 3 .   ? 20.209  10.838  -17.545 1.00 27.16 ?  699 HOH B O   1 
HETATM 7090 O O   . HOH F 3 .   ? 7.199   -9.371  -31.410 1.00 14.38 ?  700 HOH B O   1 
HETATM 7091 O O   . HOH F 3 .   ? 11.830  22.896  -59.534 0.50 28.79 ?  701 HOH B O   1 
HETATM 7092 O O   . HOH F 3 .   ? 11.830  10.704  -59.534 0.50 8.66  ?  702 HOH B O   1 
HETATM 7093 O O   . HOH G 3 .   ? -13.001 -4.793  -46.853 1.00 24.84 ?  201 HOH C O   1 
HETATM 7094 O O   . HOH G 3 .   ? -37.869 1.026   -61.479 1.00 28.62 ?  202 HOH C O   1 
HETATM 7095 O O   . HOH G 3 .   ? -15.400 14.931  -61.612 1.00 29.93 ?  203 HOH C O   1 
HETATM 7096 O O   . HOH G 3 .   ? -21.841 0.304   -65.074 1.00 34.44 ?  204 HOH C O   1 
HETATM 7097 O O   . HOH G 3 .   ? -34.124 14.746  -56.756 1.00 31.99 ?  205 HOH C O   1 
HETATM 7098 O O   . HOH G 3 .   ? -23.172 20.714  -44.858 1.00 35.24 ?  206 HOH C O   1 
HETATM 7099 O O   . HOH G 3 .   ? -33.000 13.631  -51.780 1.00 28.56 ?  207 HOH C O   1 
HETATM 7100 O O   . HOH G 3 .   ? -30.136 -2.309  -75.156 1.00 26.85 ?  208 HOH C O   1 
HETATM 7101 O O   . HOH G 3 .   ? -20.028 23.105  -51.220 1.00 33.35 ?  209 HOH C O   1 
HETATM 7102 O O   . HOH G 3 .   ? -12.399 11.477  -54.026 1.00 19.39 ?  210 HOH C O   1 
HETATM 7103 O O   . HOH G 3 .   ? -8.859  3.499   -42.226 1.00 26.94 ?  211 HOH C O   1 
HETATM 7104 O O   . HOH G 3 .   ? -11.542 8.612   -60.569 1.00 25.40 ?  212 HOH C O   1 
HETATM 7105 O O   . HOH G 3 .   ? -11.637 3.909   -58.743 1.00 27.39 ?  213 HOH C O   1 
HETATM 7106 O O   . HOH G 3 .   ? -24.369 12.365  -35.487 1.00 26.97 ?  214 HOH C O   1 
HETATM 7107 O O   . HOH G 3 .   ? -18.883 20.016  -56.270 1.00 26.80 ?  215 HOH C O   1 
HETATM 7108 O O   . HOH G 3 .   ? -14.435 15.456  -47.164 1.00 19.88 ?  216 HOH C O   1 
HETATM 7109 O O   . HOH G 3 .   ? -16.734 -1.532  -55.613 1.00 24.28 ?  217 HOH C O   1 
HETATM 7110 O O   . HOH G 3 .   ? -16.212 -2.286  -50.763 1.00 27.19 ?  218 HOH C O   1 
HETATM 7111 O O   . HOH G 3 .   ? -10.795 0.409   -41.137 1.00 33.96 ?  219 HOH C O   1 
HETATM 7112 O O   . HOH G 3 .   ? -39.803 6.074   -63.391 1.00 33.51 ?  220 HOH C O   1 
HETATM 7113 O O   . HOH G 3 .   ? -23.930 -4.341  -57.957 1.00 33.80 ?  221 HOH C O   1 
HETATM 7114 O O   . HOH G 3 .   ? -37.170 10.583  -56.283 1.00 32.08 ?  222 HOH C O   1 
HETATM 7115 O O   . HOH G 3 .   ? -11.477 5.630   -62.906 1.00 29.96 ?  223 HOH C O   1 
HETATM 7116 O O   . HOH G 3 .   ? -33.072 7.554   -47.265 1.00 31.70 ?  224 HOH C O   1 
HETATM 7117 O O   . HOH G 3 .   ? -30.834 4.215   -44.282 1.00 24.45 ?  225 HOH C O   1 
HETATM 7118 O O   . HOH G 3 .   ? -16.812 -0.355  -58.499 1.00 26.85 ?  226 HOH C O   1 
HETATM 7119 O O   . HOH G 3 .   ? -10.306 2.703   -52.035 1.00 22.70 ?  227 HOH C O   1 
HETATM 7120 O O   . HOH G 3 .   ? -25.993 18.839  -30.869 1.00 24.80 ?  228 HOH C O   1 
HETATM 7121 O O   . HOH G 3 .   ? -22.458 -5.724  -50.491 1.00 35.16 ?  229 HOH C O   1 
HETATM 7122 O O   . HOH G 3 .   ? -30.400 12.288  -30.331 1.00 31.78 ?  230 HOH C O   1 
HETATM 7123 O O   . HOH G 3 .   ? -27.792 7.703   -37.361 1.00 30.36 ?  231 HOH C O   1 
HETATM 7124 O O   . HOH G 3 .   ? -31.119 18.873  -39.791 1.00 28.31 ?  232 HOH C O   1 
HETATM 7125 O O   . HOH G 3 .   ? -9.252  19.980  -45.555 1.00 14.48 ?  233 HOH C O   1 
HETATM 7126 O O   . HOH G 3 .   ? -8.911  11.555  -44.157 1.00 20.13 ?  234 HOH C O   1 
HETATM 7127 O O   . HOH G 3 .   ? -35.377 15.529  -43.513 1.00 36.57 ?  235 HOH C O   1 
HETATM 7128 O O   . HOH G 3 .   ? -37.409 -17.306 -75.376 1.00 33.55 ?  236 HOH C O   1 
HETATM 7129 O O   . HOH G 3 .   ? -39.319 -16.953 -70.779 1.00 34.15 ?  237 HOH C O   1 
HETATM 7130 O O   . HOH G 3 .   ? -24.828 -4.705  -48.760 1.00 29.78 ?  238 HOH C O   1 
HETATM 7131 O O   . HOH G 3 .   ? -20.831 13.651  -69.404 1.00 32.59 ?  239 HOH C O   1 
HETATM 7132 O O   . HOH G 3 .   ? -8.824  11.710  -41.662 1.00 26.37 ?  240 HOH C O   1 
HETATM 7133 O O   . HOH G 3 .   ? -22.487 14.709  -44.482 1.00 25.54 ?  241 HOH C O   1 
HETATM 7134 O O   . HOH G 3 .   ? -26.008 20.423  -37.732 1.00 30.55 ?  242 HOH C O   1 
HETATM 7135 O O   . HOH G 3 .   ? -38.120 3.401   -60.467 1.00 39.26 ?  243 HOH C O   1 
HETATM 7136 O O   . HOH G 3 .   ? -13.842 1.460   -58.185 1.00 30.50 ?  244 HOH C O   1 
HETATM 7137 O O   . HOH H 3 .   ? 44.225  15.248  -12.520 1.00 36.91 ?  201 HOH D O   1 
HETATM 7138 O O   . HOH H 3 .   ? 28.429  5.489   -19.114 1.00 18.71 ?  202 HOH D O   1 
HETATM 7139 O O   . HOH H 3 .   ? 24.409  9.232   -5.198  1.00 21.26 ?  203 HOH D O   1 
HETATM 7140 O O   . HOH H 3 .   ? 17.141  12.278  -8.396  1.00 35.18 ?  204 HOH D O   1 
HETATM 7141 O O   . HOH H 3 .   ? 16.997  13.325  -12.681 1.00 28.85 ?  205 HOH D O   1 
HETATM 7142 O O   . HOH H 3 .   ? 26.191  14.737  -11.585 1.00 26.43 ?  206 HOH D O   1 
HETATM 7143 O O   . HOH H 3 .   ? 29.099  7.117   -23.536 1.00 27.19 ?  207 HOH D O   1 
HETATM 7144 O O   . HOH H 3 .   ? 30.256  17.675  -1.700  1.00 31.40 ?  208 HOH D O   1 
HETATM 7145 O O   . HOH H 3 .   ? 23.954  0.871   -1.448  1.00 28.25 ?  209 HOH D O   1 
HETATM 7146 O O   . HOH H 3 .   ? 30.038  -3.626  -6.141  1.00 31.46 ?  210 HOH D O   1 
HETATM 7147 O O   . HOH H 3 .   ? 28.497  -3.482  0.773   1.00 37.38 ?  211 HOH D O   1 
HETATM 7148 O O   . HOH H 3 .   ? 33.651  -5.727  0.660   1.00 43.99 ?  212 HOH D O   1 
HETATM 7149 O O   . HOH H 3 .   ? 21.392  10.718  -14.964 1.00 23.85 ?  213 HOH D O   1 
HETATM 7150 O O   . HOH H 3 .   ? 23.200  0.841   -9.086  1.00 25.62 ?  214 HOH D O   1 
HETATM 7151 O O   . HOH H 3 .   ? 26.753  11.762  2.973   1.00 31.05 ?  215 HOH D O   1 
HETATM 7152 O O   . HOH H 3 .   ? 15.000  9.075   -7.878  1.00 25.07 ?  216 HOH D O   1 
HETATM 7153 O O   . HOH H 3 .   ? 44.921  6.720   11.422  1.00 36.77 ?  217 HOH D O   1 
HETATM 7154 O O   . HOH H 3 .   ? 23.494  5.461   0.812   1.00 21.57 ?  218 HOH D O   1 
HETATM 7155 O O   . HOH H 3 .   ? 20.631  18.799  -12.035 1.00 19.43 ?  219 HOH D O   1 
HETATM 7156 O O   . HOH H 3 .   ? 36.286  25.661  -1.740  1.00 39.62 ?  220 HOH D O   1 
HETATM 7157 O O   . HOH H 3 .   ? 20.374  5.046   -19.606 1.00 32.06 ?  221 HOH D O   1 
HETATM 7158 O O   . HOH H 3 .   ? 29.330  24.422  -13.906 1.00 30.54 ?  222 HOH D O   1 
HETATM 7159 O O   . HOH H 3 .   ? 30.110  -3.778  -10.539 1.00 30.83 ?  223 HOH D O   1 
HETATM 7160 O O   . HOH H 3 .   ? 21.790  2.176   -0.652  1.00 25.83 ?  224 HOH D O   1 
HETATM 7161 O O   . HOH H 3 .   ? 47.156  4.331   12.343  1.00 48.13 ?  225 HOH D O   1 
HETATM 7162 O O   . HOH H 3 .   ? 20.600  11.690  -0.605  1.00 33.84 ?  226 HOH D O   1 
HETATM 7163 O O   . HOH H 3 .   ? 18.335  0.025   -5.805  1.00 30.48 ?  227 HOH D O   1 
# 
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   THR 1   224 224 THR THR A . n 
A 1 2   LYS 2   225 225 LYS LYS A . n 
A 1 3   PRO 3   226 226 PRO PRO A . n 
A 1 4   PHE 4   227 227 PHE PHE A . n 
A 1 5   SER 5   228 228 SER SER A . n 
A 1 6   VAL 6   229 229 VAL VAL A . n 
A 1 7   PRO 7   230 230 PRO PRO A . n 
A 1 8   VAL 8   231 231 VAL VAL A . n 
A 1 9   LEU 9   232 232 LEU LEU A . n 
A 1 10  THR 10  233 233 THR THR A . n 
A 1 11  VAL 11  234 234 VAL VAL A . n 
A 1 12  GLU 12  235 235 GLU GLU A . n 
A 1 13  GLU 13  236 236 GLU GLU A . n 
A 1 14  MET 14  237 237 MET MET A . n 
A 1 15  THR 15  238 238 THR THR A . n 
A 1 16  ASN 16  239 239 ASN ASN A . n 
A 1 17  SER 17  240 240 SER SER A . n 
A 1 18  ARG 18  241 241 ARG ARG A . n 
A 1 19  PHE 19  242 242 PHE PHE A . n 
A 1 20  PRO 20  243 243 PRO PRO A . n 
A 1 21  ILE 21  244 244 ILE ILE A . n 
A 1 22  PRO 22  245 245 PRO PRO A . n 
A 1 23  LEU 23  246 246 LEU LEU A . n 
A 1 24  GLU 24  247 247 GLU GLU A . n 
A 1 25  LYS 25  248 248 LYS LYS A . n 
A 1 26  LEU 26  249 249 LEU LEU A . n 
A 1 27  PHE 27  250 250 PHE PHE A . n 
A 1 28  THR 28  251 251 THR THR A . n 
A 1 29  GLY 29  252 252 GLY GLY A . n 
A 1 30  PRO 30  253 253 PRO PRO A . n 
A 1 31  SER 31  254 254 SER SER A . n 
A 1 32  SER 32  255 255 SER SER A . n 
A 1 33  ALA 33  256 256 ALA ALA A . n 
A 1 34  PHE 34  257 257 PHE PHE A . n 
A 1 35  VAL 35  258 258 VAL VAL A . n 
A 1 36  VAL 36  259 259 VAL VAL A . n 
A 1 37  GLN 37  260 260 GLN GLN A . n 
A 1 38  PRO 38  261 261 PRO PRO A . n 
A 1 39  GLN 39  262 262 GLN GLN A . n 
A 1 40  ASN 40  263 263 ASN ASN A . n 
A 1 41  GLY 41  264 264 GLY GLY A . n 
A 1 42  ARG 42  265 265 ARG ARG A . n 
A 1 43  CYS 43  266 266 CYS CYS A . n 
A 1 44  THR 44  267 267 THR THR A . n 
A 1 45  THR 45  268 268 THR THR A . n 
A 1 46  ASP 46  269 269 ASP ASP A . n 
A 1 47  GLY 47  270 270 GLY GLY A . n 
A 1 48  VAL 48  271 271 VAL VAL A . n 
A 1 49  LEU 49  272 272 LEU LEU A . n 
A 1 50  LEU 50  273 273 LEU LEU A . n 
A 1 51  GLY 51  274 274 GLY GLY A . n 
A 1 52  THR 52  275 275 THR THR A . n 
A 1 53  THR 53  276 276 THR THR A . n 
A 1 54  GLN 54  277 277 GLN GLN A . n 
A 1 55  LEU 55  278 278 LEU LEU A . n 
A 1 56  SER 56  279 279 SER SER A . n 
A 1 57  PRO 57  280 280 PRO PRO A . n 
A 1 58  VAL 58  281 281 VAL VAL A . n 
A 1 59  ASN 59  282 282 ASN ASN A . n 
A 1 60  ILE 60  283 283 ILE ILE A . n 
A 1 61  CYS 61  284 284 CYS CYS A . n 
A 1 62  THR 62  285 285 THR THR A . n 
A 1 63  PHE 63  286 286 PHE PHE A . n 
A 1 64  ARG 64  287 287 ARG ARG A . n 
A 1 65  GLY 65  288 288 GLY GLY A . n 
A 1 66  ASP 66  289 289 ASP ASP A . n 
A 1 67  VAL 67  290 290 VAL VAL A . n 
A 1 68  THR 68  291 291 THR THR A . n 
A 1 69  HIS 69  292 292 HIS HIS A . n 
A 1 70  ILE 70  293 293 ILE ILE A . n 
A 1 71  THR 71  294 294 THR THR A . n 
A 1 72  GLY 72  295 295 GLY GLY A . n 
A 1 73  SER 73  296 296 SER SER A . n 
A 1 74  ARG 74  297 297 ARG ARG A . n 
A 1 75  ASN 75  298 298 ASN ASN A . n 
A 1 76  TYR 76  299 299 TYR TYR A . n 
A 1 77  THR 77  300 300 THR THR A . n 
A 1 78  MET 78  301 301 MET MET A . n 
A 1 79  ASN 79  302 302 ASN ASN A . n 
A 1 80  LEU 80  303 303 LEU LEU A . n 
A 1 81  ALA 81  304 304 ALA ALA A . n 
A 1 82  SER 82  305 305 SER SER A . n 
A 1 83  GLN 83  306 306 GLN GLN A . n 
A 1 84  ASN 84  307 307 ASN ASN A . n 
A 1 85  TRP 85  308 308 TRP TRP A . n 
A 1 86  ASN 86  309 309 ASN ASN A . n 
A 1 87  ASP 87  310 310 ASP ASP A . n 
A 1 88  TYR 88  311 311 TYR TYR A . n 
A 1 89  ASP 89  312 312 ASP ASP A . n 
A 1 90  PRO 90  313 313 PRO PRO A . n 
A 1 91  THR 91  314 314 THR THR A . n 
A 1 92  GLU 92  315 315 GLU GLU A . n 
A 1 93  GLU 93  316 316 GLU GLU A . n 
A 1 94  ILE 94  317 317 ILE ILE A . n 
A 1 95  PRO 95  318 318 PRO PRO A . n 
A 1 96  ALA 96  319 319 ALA ALA A . n 
A 1 97  PRO 97  320 320 PRO PRO A . n 
A 1 98  LEU 98  321 321 LEU LEU A . n 
A 1 99  GLY 99  322 322 GLY GLY A . n 
A 1 100 THR 100 323 323 THR THR A . n 
A 1 101 PRO 101 324 324 PRO PRO A . n 
A 1 102 ASP 102 325 325 ASP ASP A . n 
A 1 103 PHE 103 326 326 PHE PHE A . n 
A 1 104 VAL 104 327 327 VAL VAL A . n 
A 1 105 GLY 105 328 328 GLY GLY A . n 
A 1 106 LYS 106 329 329 LYS LYS A . n 
A 1 107 ILE 107 330 330 ILE ILE A . n 
A 1 108 GLN 108 331 331 GLN GLN A . n 
A 1 109 GLY 109 332 332 GLY GLY A . n 
A 1 110 VAL 110 333 333 VAL VAL A . n 
A 1 111 LEU 111 334 334 LEU LEU A . n 
A 1 112 THR 112 335 335 THR THR A . n 
A 1 113 GLN 113 336 336 GLN GLN A . n 
A 1 114 THR 114 337 337 THR THR A . n 
A 1 115 THR 115 338 338 THR THR A . n 
A 1 116 ARG 116 339 339 ARG ARG A . n 
A 1 117 THR 117 340 340 THR THR A . n 
A 1 118 ASP 118 341 341 ASP ASP A . n 
A 1 119 GLY 119 342 342 GLY GLY A . n 
A 1 120 SER 120 343 343 SER SER A . n 
A 1 121 THR 121 344 344 THR THR A . n 
A 1 122 ARG 122 345 345 ARG ARG A . n 
A 1 123 GLY 123 346 346 GLY GLY A . n 
A 1 124 HIS 124 347 347 HIS HIS A . n 
A 1 125 LYS 125 348 348 LYS LYS A . n 
A 1 126 ALA 126 349 349 ALA ALA A . n 
A 1 127 THR 127 350 350 THR THR A . n 
A 1 128 VAL 128 351 351 VAL VAL A . n 
A 1 129 TYR 129 352 352 TYR TYR A . n 
A 1 130 THR 130 353 353 THR THR A . n 
A 1 131 GLY 131 354 354 GLY GLY A . n 
A 1 132 SER 132 355 355 SER SER A . n 
A 1 133 ALA 133 356 356 ALA ALA A . n 
A 1 134 ASP 134 357 357 ASP ASP A . n 
A 1 135 PHE 135 358 358 PHE PHE A . n 
A 1 136 ALA 136 359 359 ALA ALA A . n 
A 1 137 PRO 137 360 360 PRO PRO A . n 
A 1 138 LYS 138 361 361 LYS LYS A . n 
A 1 139 LEU 139 362 362 LEU LEU A . n 
A 1 140 GLY 140 363 363 GLY GLY A . n 
A 1 141 ARG 141 364 364 ARG ARG A . n 
A 1 142 VAL 142 365 365 VAL VAL A . n 
A 1 143 GLN 143 366 366 GLN GLN A . n 
A 1 144 PHE 144 367 367 PHE PHE A . n 
A 1 145 GLU 145 368 368 GLU GLU A . n 
A 1 146 THR 146 369 369 THR THR A . n 
A 1 147 ASP 147 370 370 ASP ASP A . n 
A 1 148 THR 148 371 371 THR THR A . n 
A 1 149 ASP 149 372 372 ASP ASP A . n 
A 1 150 ARG 150 373 373 ARG ARG A . n 
A 1 151 ASP 151 374 374 ASP ASP A . n 
A 1 152 PHE 152 375 375 PHE PHE A . n 
A 1 153 GLU 153 376 376 GLU GLU A . n 
A 1 154 ALA 154 377 377 ALA ALA A . n 
A 1 155 ASN 155 378 378 ASN ASN A . n 
A 1 156 GLN 156 379 379 GLN GLN A . n 
A 1 157 ASN 157 380 380 ASN ASN A . n 
A 1 158 THR 158 381 381 THR THR A . n 
A 1 159 LYS 159 382 382 LYS LYS A . n 
A 1 160 PHE 160 383 383 PHE PHE A . n 
A 1 161 THR 161 384 384 THR THR A . n 
A 1 162 PRO 162 385 385 PRO PRO A . n 
A 1 163 VAL 163 386 386 VAL VAL A . n 
A 1 164 GLY 164 387 387 GLY GLY A . n 
A 1 165 VAL 165 388 388 VAL VAL A . n 
A 1 166 ILE 166 389 389 ILE ILE A . n 
A 1 167 GLN 167 390 390 GLN GLN A . n 
A 1 168 ASP 168 391 391 ASP ASP A . n 
A 1 169 GLY 169 392 392 GLY GLY A . n 
A 1 170 GLY 170 393 393 GLY GLY A . n 
A 1 171 THR 171 394 394 THR THR A . n 
A 1 172 THR 172 395 395 THR THR A . n 
A 1 173 HIS 173 396 396 HIS HIS A . n 
A 1 174 ARG 174 397 397 ARG ARG A . n 
A 1 175 ASN 175 398 398 ASN ASN A . n 
A 1 176 GLU 176 399 399 GLU GLU A . n 
A 1 177 PRO 177 400 400 PRO PRO A . n 
A 1 178 GLN 178 401 401 GLN GLN A . n 
A 1 179 GLN 179 402 402 GLN GLN A . n 
A 1 180 TRP 180 403 403 TRP TRP A . n 
A 1 181 VAL 181 404 404 VAL VAL A . n 
A 1 182 LEU 182 405 405 LEU LEU A . n 
A 1 183 PRO 183 406 406 PRO PRO A . n 
A 1 184 SER 184 407 407 SER SER A . n 
A 1 185 TYR 185 408 408 TYR TYR A . n 
A 1 186 SER 186 409 409 SER SER A . n 
A 1 187 GLY 187 410 410 GLY GLY A . n 
A 1 188 ARG 188 411 411 ARG ARG A . n 
A 1 189 ASN 189 412 412 ASN ASN A . n 
A 1 190 THR 190 413 413 THR THR A . n 
A 1 191 HIS 191 414 414 HIS HIS A . n 
A 1 192 ASN 192 415 415 ASN ASN A . n 
A 1 193 VAL 193 416 416 VAL VAL A . n 
A 1 194 HIS 194 417 417 HIS HIS A . n 
A 1 195 LEU 195 418 418 LEU LEU A . n 
A 1 196 ALA 196 419 419 ALA ALA A . n 
A 1 197 PRO 197 420 420 PRO PRO A . n 
A 1 198 ALA 198 421 421 ALA ALA A . n 
A 1 199 VAL 199 422 422 VAL VAL A . n 
A 1 200 ALA 200 423 423 ALA ALA A . n 
A 1 201 PRO 201 424 424 PRO PRO A . n 
A 1 202 THR 202 425 425 THR THR A . n 
A 1 203 PHE 203 426 426 PHE PHE A . n 
A 1 204 PRO 204 427 427 PRO PRO A . n 
A 1 205 GLY 205 428 428 GLY GLY A . n 
A 1 206 GLU 206 429 429 GLU GLU A . n 
A 1 207 GLN 207 430 430 GLN GLN A . n 
A 1 208 LEU 208 431 431 LEU LEU A . n 
A 1 209 LEU 209 432 432 LEU LEU A . n 
A 1 210 PHE 210 433 433 PHE PHE A . n 
A 1 211 PHE 211 434 434 PHE PHE A . n 
A 1 212 ARG 212 435 435 ARG ARG A . n 
A 1 213 SER 213 436 436 SER SER A . n 
A 1 214 THR 214 437 437 THR THR A . n 
A 1 215 MET 215 438 438 MET MET A . n 
A 1 216 PRO 216 439 439 PRO PRO A . n 
A 1 217 GLY 217 440 440 GLY GLY A . n 
A 1 218 CYS 218 441 441 CYS CYS A . n 
A 1 219 SER 219 442 442 SER SER A . n 
A 1 220 GLY 220 443 443 GLY GLY A . n 
A 1 221 TYR 221 444 444 TYR TYR A . n 
A 1 222 PRO 222 445 445 PRO PRO A . n 
A 1 223 ASN 223 446 446 ASN ASN A . n 
A 1 224 MET 224 447 447 MET MET A . n 
A 1 225 ASP 225 448 448 ASP ASP A . n 
A 1 226 LEU 226 449 449 LEU LEU A . n 
A 1 227 ASP 227 450 450 ASP ASP A . n 
A 1 228 CYS 228 451 451 CYS CYS A . n 
A 1 229 LEU 229 452 452 LEU LEU A . n 
A 1 230 LEU 230 453 453 LEU LEU A . n 
A 1 231 PRO 231 454 454 PRO PRO A . n 
A 1 232 GLN 232 455 455 GLN GLN A . n 
A 1 233 GLU 233 456 456 GLU GLU A . n 
A 1 234 TRP 234 457 457 TRP TRP A . n 
A 1 235 VAL 235 458 458 VAL VAL A . n 
A 1 236 GLN 236 459 459 GLN GLN A . n 
A 1 237 TYR 237 460 460 TYR TYR A . n 
A 1 238 PHE 238 461 461 PHE PHE A . n 
A 1 239 TYR 239 462 462 TYR TYR A . n 
A 1 240 GLN 240 463 463 GLN GLN A . n 
A 1 241 GLU 241 464 464 GLU GLU A . n 
A 1 242 ALA 242 465 465 ALA ALA A . n 
A 1 243 ALA 243 466 466 ALA ALA A . n 
A 1 244 PRO 244 467 467 PRO PRO A . n 
A 1 245 ALA 245 468 468 ALA ALA A . n 
A 1 246 GLN 246 469 469 GLN GLN A . n 
A 1 247 SER 247 470 470 SER SER A . n 
A 1 248 ASP 248 471 471 ASP ASP A . n 
A 1 249 VAL 249 472 472 VAL VAL A . n 
A 1 250 ALA 250 473 473 ALA ALA A . n 
A 1 251 LEU 251 474 474 LEU LEU A . n 
A 1 252 LEU 252 475 475 LEU LEU A . n 
A 1 253 ARG 253 476 476 ARG ARG A . n 
A 1 254 PHE 254 477 477 PHE PHE A . n 
A 1 255 VAL 255 478 478 VAL VAL A . n 
A 1 256 ASN 256 479 479 ASN ASN A . n 
A 1 257 PRO 257 480 480 PRO PRO A . n 
A 1 258 ASP 258 481 481 ASP ASP A . n 
A 1 259 THR 259 482 482 THR THR A . n 
A 1 260 GLY 260 483 483 GLY GLY A . n 
A 1 261 ARG 261 484 484 ARG ARG A . n 
A 1 262 VAL 262 485 485 VAL VAL A . n 
A 1 263 LEU 263 486 486 LEU LEU A . n 
A 1 264 PHE 264 487 487 PHE PHE A . n 
A 1 265 GLU 265 488 488 GLU GLU A . n 
A 1 266 CYS 266 489 489 CYS CYS A . n 
A 1 267 LYS 267 490 490 LYS LYS A . n 
A 1 268 LEU 268 491 491 LEU LEU A . n 
A 1 269 HIS 269 492 492 HIS HIS A . n 
A 1 270 LYS 270 493 493 LYS LYS A . n 
A 1 271 SER 271 494 494 SER SER A . n 
A 1 272 GLY 272 495 495 GLY GLY A . n 
A 1 273 TYR 273 496 496 TYR TYR A . n 
A 1 274 VAL 274 497 497 VAL VAL A . n 
A 1 275 THR 275 498 498 THR THR A . n 
A 1 276 VAL 276 499 499 VAL VAL A . n 
A 1 277 ALA 277 500 500 ALA ALA A . n 
A 1 278 HIS 278 501 501 HIS HIS A . n 
A 1 279 THR 279 502 502 THR THR A . n 
A 1 280 GLY 280 503 503 GLY GLY A . n 
A 1 281 GLN 281 504 504 GLN GLN A . n 
A 1 282 HIS 282 505 505 HIS HIS A . n 
A 1 283 ASP 283 506 506 ASP ASP A . n 
A 1 284 LEU 284 507 507 LEU LEU A . n 
A 1 285 VAL 285 508 508 VAL VAL A . n 
A 1 286 ILE 286 509 509 ILE ILE A . n 
A 1 287 PRO 287 510 510 PRO PRO A . n 
A 1 288 PRO 288 511 511 PRO PRO A . n 
A 1 289 ASN 289 512 512 ASN ASN A . n 
A 1 290 GLY 290 513 513 GLY GLY A . n 
A 1 291 TYR 291 514 514 TYR TYR A . n 
A 1 292 PHE 292 515 515 PHE PHE A . n 
A 1 293 ARG 293 516 516 ARG ARG A . n 
A 1 294 PHE 294 517 517 PHE PHE A . n 
A 1 295 ASP 295 518 518 ASP ASP A . n 
A 1 296 SER 296 519 519 SER SER A . n 
A 1 297 TRP 297 520 520 TRP TRP A . n 
A 1 298 VAL 298 521 521 VAL VAL A . n 
A 1 299 ASN 299 522 522 ASN ASN A . n 
A 1 300 GLN 300 523 523 GLN GLN A . n 
A 1 301 PHE 301 524 524 PHE PHE A . n 
A 1 302 TYR 302 525 525 TYR TYR A . n 
A 1 303 THR 303 526 526 THR THR A . n 
A 1 304 LEU 304 527 527 LEU LEU A . n 
A 1 305 ALA 305 528 528 ALA ALA A . n 
A 1 306 PRO 306 529 529 PRO PRO A . n 
A 1 307 MET 307 530 530 MET MET A . n 
A 1 308 GLY 308 531 ?   ?   ?   A . n 
A 1 309 ASN 309 532 ?   ?   ?   A . n 
A 1 310 GLY 310 533 ?   ?   ?   A . n 
A 1 311 THR 311 534 ?   ?   ?   A . n 
A 1 312 GLY 312 535 ?   ?   ?   A . n 
A 1 313 ARG 313 536 ?   ?   ?   A . n 
A 1 314 ARG 314 537 ?   ?   ?   A . n 
A 1 315 ARG 315 538 ?   ?   ?   A . n 
A 1 316 ALA 316 539 ?   ?   ?   A . n 
A 1 317 VAL 317 540 ?   ?   ?   A . n 
B 1 1   THR 1   224 224 THR THR B . n 
B 1 2   LYS 2   225 225 LYS LYS B . n 
B 1 3   PRO 3   226 226 PRO PRO B . n 
B 1 4   PHE 4   227 227 PHE PHE B . n 
B 1 5   SER 5   228 228 SER SER B . n 
B 1 6   VAL 6   229 229 VAL VAL B . n 
B 1 7   PRO 7   230 230 PRO PRO B . n 
B 1 8   VAL 8   231 231 VAL VAL B . n 
B 1 9   LEU 9   232 232 LEU LEU B . n 
B 1 10  THR 10  233 233 THR THR B . n 
B 1 11  VAL 11  234 234 VAL VAL B . n 
B 1 12  GLU 12  235 235 GLU GLU B . n 
B 1 13  GLU 13  236 236 GLU GLU B . n 
B 1 14  MET 14  237 237 MET MET B . n 
B 1 15  THR 15  238 238 THR THR B . n 
B 1 16  ASN 16  239 239 ASN ASN B . n 
B 1 17  SER 17  240 240 SER SER B . n 
B 1 18  ARG 18  241 241 ARG ARG B . n 
B 1 19  PHE 19  242 242 PHE PHE B . n 
B 1 20  PRO 20  243 243 PRO PRO B . n 
B 1 21  ILE 21  244 244 ILE ILE B . n 
B 1 22  PRO 22  245 245 PRO PRO B . n 
B 1 23  LEU 23  246 246 LEU LEU B . n 
B 1 24  GLU 24  247 247 GLU GLU B . n 
B 1 25  LYS 25  248 248 LYS LYS B . n 
B 1 26  LEU 26  249 249 LEU LEU B . n 
B 1 27  PHE 27  250 250 PHE PHE B . n 
B 1 28  THR 28  251 251 THR THR B . n 
B 1 29  GLY 29  252 252 GLY GLY B . n 
B 1 30  PRO 30  253 253 PRO PRO B . n 
B 1 31  SER 31  254 254 SER SER B . n 
B 1 32  SER 32  255 255 SER SER B . n 
B 1 33  ALA 33  256 256 ALA ALA B . n 
B 1 34  PHE 34  257 257 PHE PHE B . n 
B 1 35  VAL 35  258 258 VAL VAL B . n 
B 1 36  VAL 36  259 259 VAL VAL B . n 
B 1 37  GLN 37  260 260 GLN GLN B . n 
B 1 38  PRO 38  261 261 PRO PRO B . n 
B 1 39  GLN 39  262 262 GLN GLN B . n 
B 1 40  ASN 40  263 263 ASN ASN B . n 
B 1 41  GLY 41  264 264 GLY GLY B . n 
B 1 42  ARG 42  265 265 ARG ARG B . n 
B 1 43  CYS 43  266 266 CYS CYS B . n 
B 1 44  THR 44  267 267 THR THR B . n 
B 1 45  THR 45  268 268 THR THR B . n 
B 1 46  ASP 46  269 269 ASP ASP B . n 
B 1 47  GLY 47  270 270 GLY GLY B . n 
B 1 48  VAL 48  271 271 VAL VAL B . n 
B 1 49  LEU 49  272 272 LEU LEU B . n 
B 1 50  LEU 50  273 273 LEU LEU B . n 
B 1 51  GLY 51  274 274 GLY GLY B . n 
B 1 52  THR 52  275 275 THR THR B . n 
B 1 53  THR 53  276 276 THR THR B . n 
B 1 54  GLN 54  277 277 GLN GLN B . n 
B 1 55  LEU 55  278 278 LEU LEU B . n 
B 1 56  SER 56  279 279 SER SER B . n 
B 1 57  PRO 57  280 280 PRO PRO B . n 
B 1 58  VAL 58  281 281 VAL VAL B . n 
B 1 59  ASN 59  282 282 ASN ASN B . n 
B 1 60  ILE 60  283 283 ILE ILE B . n 
B 1 61  CYS 61  284 284 CYS CYS B . n 
B 1 62  THR 62  285 285 THR THR B . n 
B 1 63  PHE 63  286 286 PHE PHE B . n 
B 1 64  ARG 64  287 287 ARG ARG B . n 
B 1 65  GLY 65  288 288 GLY GLY B . n 
B 1 66  ASP 66  289 289 ASP ASP B . n 
B 1 67  VAL 67  290 290 VAL VAL B . n 
B 1 68  THR 68  291 291 THR THR B . n 
B 1 69  HIS 69  292 292 HIS HIS B . n 
B 1 70  ILE 70  293 293 ILE ILE B . n 
B 1 71  THR 71  294 294 THR THR B . n 
B 1 72  GLY 72  295 295 GLY GLY B . n 
B 1 73  SER 73  296 296 SER SER B . n 
B 1 74  ARG 74  297 297 ARG ARG B . n 
B 1 75  ASN 75  298 298 ASN ASN B . n 
B 1 76  TYR 76  299 299 TYR TYR B . n 
B 1 77  THR 77  300 300 THR THR B . n 
B 1 78  MET 78  301 301 MET MET B . n 
B 1 79  ASN 79  302 302 ASN ASN B . n 
B 1 80  LEU 80  303 303 LEU LEU B . n 
B 1 81  ALA 81  304 304 ALA ALA B . n 
B 1 82  SER 82  305 305 SER SER B . n 
B 1 83  GLN 83  306 306 GLN GLN B . n 
B 1 84  ASN 84  307 307 ASN ASN B . n 
B 1 85  TRP 85  308 308 TRP TRP B . n 
B 1 86  ASN 86  309 309 ASN ASN B . n 
B 1 87  ASP 87  310 310 ASP ASP B . n 
B 1 88  TYR 88  311 311 TYR TYR B . n 
B 1 89  ASP 89  312 312 ASP ASP B . n 
B 1 90  PRO 90  313 313 PRO PRO B . n 
B 1 91  THR 91  314 314 THR THR B . n 
B 1 92  GLU 92  315 315 GLU GLU B . n 
B 1 93  GLU 93  316 316 GLU GLU B . n 
B 1 94  ILE 94  317 317 ILE ILE B . n 
B 1 95  PRO 95  318 318 PRO PRO B . n 
B 1 96  ALA 96  319 319 ALA ALA B . n 
B 1 97  PRO 97  320 320 PRO PRO B . n 
B 1 98  LEU 98  321 321 LEU LEU B . n 
B 1 99  GLY 99  322 322 GLY GLY B . n 
B 1 100 THR 100 323 323 THR THR B . n 
B 1 101 PRO 101 324 324 PRO PRO B . n 
B 1 102 ASP 102 325 325 ASP ASP B . n 
B 1 103 PHE 103 326 326 PHE PHE B . n 
B 1 104 VAL 104 327 327 VAL VAL B . n 
B 1 105 GLY 105 328 328 GLY GLY B . n 
B 1 106 LYS 106 329 329 LYS LYS B . n 
B 1 107 ILE 107 330 330 ILE ILE B . n 
B 1 108 GLN 108 331 331 GLN GLN B . n 
B 1 109 GLY 109 332 332 GLY GLY B . n 
B 1 110 VAL 110 333 333 VAL VAL B . n 
B 1 111 LEU 111 334 334 LEU LEU B . n 
B 1 112 THR 112 335 335 THR THR B . n 
B 1 113 GLN 113 336 336 GLN GLN B . n 
B 1 114 THR 114 337 337 THR THR B . n 
B 1 115 THR 115 338 338 THR THR B . n 
B 1 116 ARG 116 339 339 ARG ARG B . n 
B 1 117 THR 117 340 340 THR THR B . n 
B 1 118 ASP 118 341 341 ASP ASP B . n 
B 1 119 GLY 119 342 342 GLY GLY B . n 
B 1 120 SER 120 343 343 SER SER B . n 
B 1 121 THR 121 344 344 THR THR B . n 
B 1 122 ARG 122 345 345 ARG ARG B . n 
B 1 123 GLY 123 346 346 GLY GLY B . n 
B 1 124 HIS 124 347 347 HIS HIS B . n 
B 1 125 LYS 125 348 348 LYS LYS B . n 
B 1 126 ALA 126 349 349 ALA ALA B . n 
B 1 127 THR 127 350 350 THR THR B . n 
B 1 128 VAL 128 351 351 VAL VAL B . n 
B 1 129 TYR 129 352 352 TYR TYR B . n 
B 1 130 THR 130 353 353 THR THR B . n 
B 1 131 GLY 131 354 354 GLY GLY B . n 
B 1 132 SER 132 355 355 SER SER B . n 
B 1 133 ALA 133 356 356 ALA ALA B . n 
B 1 134 ASP 134 357 357 ASP ASP B . n 
B 1 135 PHE 135 358 358 PHE PHE B . n 
B 1 136 ALA 136 359 359 ALA ALA B . n 
B 1 137 PRO 137 360 360 PRO PRO B . n 
B 1 138 LYS 138 361 361 LYS LYS B . n 
B 1 139 LEU 139 362 362 LEU LEU B . n 
B 1 140 GLY 140 363 363 GLY GLY B . n 
B 1 141 ARG 141 364 364 ARG ARG B . n 
B 1 142 VAL 142 365 365 VAL VAL B . n 
B 1 143 GLN 143 366 366 GLN GLN B . n 
B 1 144 PHE 144 367 367 PHE PHE B . n 
B 1 145 GLU 145 368 368 GLU GLU B . n 
B 1 146 THR 146 369 369 THR THR B . n 
B 1 147 ASP 147 370 370 ASP ASP B . n 
B 1 148 THR 148 371 371 THR THR B . n 
B 1 149 ASP 149 372 372 ASP ASP B . n 
B 1 150 ARG 150 373 373 ARG ARG B . n 
B 1 151 ASP 151 374 374 ASP ASP B . n 
B 1 152 PHE 152 375 375 PHE PHE B . n 
B 1 153 GLU 153 376 376 GLU GLU B . n 
B 1 154 ALA 154 377 377 ALA ALA B . n 
B 1 155 ASN 155 378 378 ASN ASN B . n 
B 1 156 GLN 156 379 379 GLN GLN B . n 
B 1 157 ASN 157 380 380 ASN ASN B . n 
B 1 158 THR 158 381 381 THR THR B . n 
B 1 159 LYS 159 382 382 LYS LYS B . n 
B 1 160 PHE 160 383 383 PHE PHE B . n 
B 1 161 THR 161 384 384 THR THR B . n 
B 1 162 PRO 162 385 385 PRO PRO B . n 
B 1 163 VAL 163 386 386 VAL VAL B . n 
B 1 164 GLY 164 387 387 GLY GLY B . n 
B 1 165 VAL 165 388 388 VAL VAL B . n 
B 1 166 ILE 166 389 389 ILE ILE B . n 
B 1 167 GLN 167 390 390 GLN GLN B . n 
B 1 168 ASP 168 391 391 ASP ASP B . n 
B 1 169 GLY 169 392 392 GLY GLY B . n 
B 1 170 GLY 170 393 393 GLY GLY B . n 
B 1 171 THR 171 394 394 THR THR B . n 
B 1 172 THR 172 395 395 THR THR B . n 
B 1 173 HIS 173 396 396 HIS HIS B . n 
B 1 174 ARG 174 397 397 ARG ARG B . n 
B 1 175 ASN 175 398 398 ASN ASN B . n 
B 1 176 GLU 176 399 399 GLU GLU B . n 
B 1 177 PRO 177 400 400 PRO PRO B . n 
B 1 178 GLN 178 401 401 GLN GLN B . n 
B 1 179 GLN 179 402 402 GLN GLN B . n 
B 1 180 TRP 180 403 403 TRP TRP B . n 
B 1 181 VAL 181 404 404 VAL VAL B . n 
B 1 182 LEU 182 405 405 LEU LEU B . n 
B 1 183 PRO 183 406 406 PRO PRO B . n 
B 1 184 SER 184 407 407 SER SER B . n 
B 1 185 TYR 185 408 408 TYR TYR B . n 
B 1 186 SER 186 409 409 SER SER B . n 
B 1 187 GLY 187 410 410 GLY GLY B . n 
B 1 188 ARG 188 411 411 ARG ARG B . n 
B 1 189 ASN 189 412 412 ASN ASN B . n 
B 1 190 THR 190 413 413 THR THR B . n 
B 1 191 HIS 191 414 414 HIS HIS B . n 
B 1 192 ASN 192 415 415 ASN ASN B . n 
B 1 193 VAL 193 416 416 VAL VAL B . n 
B 1 194 HIS 194 417 417 HIS HIS B . n 
B 1 195 LEU 195 418 418 LEU LEU B . n 
B 1 196 ALA 196 419 419 ALA ALA B . n 
B 1 197 PRO 197 420 420 PRO PRO B . n 
B 1 198 ALA 198 421 421 ALA ALA B . n 
B 1 199 VAL 199 422 422 VAL VAL B . n 
B 1 200 ALA 200 423 423 ALA ALA B . n 
B 1 201 PRO 201 424 424 PRO PRO B . n 
B 1 202 THR 202 425 425 THR THR B . n 
B 1 203 PHE 203 426 426 PHE PHE B . n 
B 1 204 PRO 204 427 427 PRO PRO B . n 
B 1 205 GLY 205 428 428 GLY GLY B . n 
B 1 206 GLU 206 429 429 GLU GLU B . n 
B 1 207 GLN 207 430 430 GLN GLN B . n 
B 1 208 LEU 208 431 431 LEU LEU B . n 
B 1 209 LEU 209 432 432 LEU LEU B . n 
B 1 210 PHE 210 433 433 PHE PHE B . n 
B 1 211 PHE 211 434 434 PHE PHE B . n 
B 1 212 ARG 212 435 435 ARG ARG B . n 
B 1 213 SER 213 436 436 SER SER B . n 
B 1 214 THR 214 437 437 THR THR B . n 
B 1 215 MET 215 438 438 MET MET B . n 
B 1 216 PRO 216 439 439 PRO PRO B . n 
B 1 217 GLY 217 440 440 GLY GLY B . n 
B 1 218 CYS 218 441 441 CYS CYS B . n 
B 1 219 SER 219 442 442 SER SER B . n 
B 1 220 GLY 220 443 443 GLY GLY B . n 
B 1 221 TYR 221 444 444 TYR TYR B . n 
B 1 222 PRO 222 445 445 PRO PRO B . n 
B 1 223 ASN 223 446 446 ASN ASN B . n 
B 1 224 MET 224 447 447 MET MET B . n 
B 1 225 ASP 225 448 448 ASP ASP B . n 
B 1 226 LEU 226 449 449 LEU LEU B . n 
B 1 227 ASP 227 450 450 ASP ASP B . n 
B 1 228 CYS 228 451 451 CYS CYS B . n 
B 1 229 LEU 229 452 452 LEU LEU B . n 
B 1 230 LEU 230 453 453 LEU LEU B . n 
B 1 231 PRO 231 454 454 PRO PRO B . n 
B 1 232 GLN 232 455 455 GLN GLN B . n 
B 1 233 GLU 233 456 456 GLU GLU B . n 
B 1 234 TRP 234 457 457 TRP TRP B . n 
B 1 235 VAL 235 458 458 VAL VAL B . n 
B 1 236 GLN 236 459 459 GLN GLN B . n 
B 1 237 TYR 237 460 460 TYR TYR B . n 
B 1 238 PHE 238 461 461 PHE PHE B . n 
B 1 239 TYR 239 462 462 TYR TYR B . n 
B 1 240 GLN 240 463 463 GLN GLN B . n 
B 1 241 GLU 241 464 464 GLU GLU B . n 
B 1 242 ALA 242 465 465 ALA ALA B . n 
B 1 243 ALA 243 466 466 ALA ALA B . n 
B 1 244 PRO 244 467 467 PRO PRO B . n 
B 1 245 ALA 245 468 468 ALA ALA B . n 
B 1 246 GLN 246 469 469 GLN GLN B . n 
B 1 247 SER 247 470 470 SER SER B . n 
B 1 248 ASP 248 471 471 ASP ASP B . n 
B 1 249 VAL 249 472 472 VAL VAL B . n 
B 1 250 ALA 250 473 473 ALA ALA B . n 
B 1 251 LEU 251 474 474 LEU LEU B . n 
B 1 252 LEU 252 475 475 LEU LEU B . n 
B 1 253 ARG 253 476 476 ARG ARG B . n 
B 1 254 PHE 254 477 477 PHE PHE B . n 
B 1 255 VAL 255 478 478 VAL VAL B . n 
B 1 256 ASN 256 479 479 ASN ASN B . n 
B 1 257 PRO 257 480 480 PRO PRO B . n 
B 1 258 ASP 258 481 481 ASP ASP B . n 
B 1 259 THR 259 482 482 THR THR B . n 
B 1 260 GLY 260 483 483 GLY GLY B . n 
B 1 261 ARG 261 484 484 ARG ARG B . n 
B 1 262 VAL 262 485 485 VAL VAL B . n 
B 1 263 LEU 263 486 486 LEU LEU B . n 
B 1 264 PHE 264 487 487 PHE PHE B . n 
B 1 265 GLU 265 488 488 GLU GLU B . n 
B 1 266 CYS 266 489 489 CYS CYS B . n 
B 1 267 LYS 267 490 490 LYS LYS B . n 
B 1 268 LEU 268 491 491 LEU LEU B . n 
B 1 269 HIS 269 492 492 HIS HIS B . n 
B 1 270 LYS 270 493 493 LYS LYS B . n 
B 1 271 SER 271 494 494 SER SER B . n 
B 1 272 GLY 272 495 495 GLY GLY B . n 
B 1 273 TYR 273 496 496 TYR TYR B . n 
B 1 274 VAL 274 497 497 VAL VAL B . n 
B 1 275 THR 275 498 498 THR THR B . n 
B 1 276 VAL 276 499 499 VAL VAL B . n 
B 1 277 ALA 277 500 500 ALA ALA B . n 
B 1 278 HIS 278 501 501 HIS HIS B . n 
B 1 279 THR 279 502 502 THR THR B . n 
B 1 280 GLY 280 503 503 GLY GLY B . n 
B 1 281 GLN 281 504 504 GLN GLN B . n 
B 1 282 HIS 282 505 505 HIS HIS B . n 
B 1 283 ASP 283 506 506 ASP ASP B . n 
B 1 284 LEU 284 507 507 LEU LEU B . n 
B 1 285 VAL 285 508 508 VAL VAL B . n 
B 1 286 ILE 286 509 509 ILE ILE B . n 
B 1 287 PRO 287 510 510 PRO PRO B . n 
B 1 288 PRO 288 511 511 PRO PRO B . n 
B 1 289 ASN 289 512 512 ASN ASN B . n 
B 1 290 GLY 290 513 513 GLY GLY B . n 
B 1 291 TYR 291 514 514 TYR TYR B . n 
B 1 292 PHE 292 515 515 PHE PHE B . n 
B 1 293 ARG 293 516 516 ARG ARG B . n 
B 1 294 PHE 294 517 517 PHE PHE B . n 
B 1 295 ASP 295 518 518 ASP ASP B . n 
B 1 296 SER 296 519 519 SER SER B . n 
B 1 297 TRP 297 520 520 TRP TRP B . n 
B 1 298 VAL 298 521 521 VAL VAL B . n 
B 1 299 ASN 299 522 522 ASN ASN B . n 
B 1 300 GLN 300 523 523 GLN GLN B . n 
B 1 301 PHE 301 524 524 PHE PHE B . n 
B 1 302 TYR 302 525 525 TYR TYR B . n 
B 1 303 THR 303 526 526 THR THR B . n 
B 1 304 LEU 304 527 527 LEU LEU B . n 
B 1 305 ALA 305 528 528 ALA ALA B . n 
B 1 306 PRO 306 529 529 PRO PRO B . n 
B 1 307 MET 307 530 530 MET MET B . n 
B 1 308 GLY 308 531 ?   ?   ?   B . n 
B 1 309 ASN 309 532 ?   ?   ?   B . n 
B 1 310 GLY 310 533 ?   ?   ?   B . n 
B 1 311 THR 311 534 ?   ?   ?   B . n 
B 1 312 GLY 312 535 ?   ?   ?   B . n 
B 1 313 ARG 313 536 ?   ?   ?   B . n 
B 1 314 ARG 314 537 ?   ?   ?   B . n 
B 1 315 ARG 315 538 ?   ?   ?   B . n 
B 1 316 ALA 316 539 ?   ?   ?   B . n 
B 1 317 VAL 317 540 ?   ?   ?   B . n 
C 2 1   GLN 1   1   1   GLN GLN C . n 
C 2 2   VAL 2   2   2   VAL VAL C . n 
C 2 3   GLN 3   3   3   GLN GLN C . n 
C 2 4   LEU 4   4   4   LEU LEU C . n 
C 2 5   GLN 5   5   5   GLN GLN C . n 
C 2 6   GLU 6   6   6   GLU GLU C . n 
C 2 7   SER 7   7   7   SER SER C . n 
C 2 8   GLY 8   8   8   GLY GLY C . n 
C 2 9   GLY 9   9   9   GLY GLY C . n 
C 2 10  GLY 10  10  10  GLY GLY C . n 
C 2 11  LEU 11  11  11  LEU LEU C . n 
C 2 12  VAL 12  12  12  VAL VAL C . n 
C 2 13  GLN 13  13  13  GLN GLN C . n 
C 2 14  ALA 14  14  14  ALA ALA C . n 
C 2 15  GLY 15  15  15  GLY GLY C . n 
C 2 16  GLY 16  16  16  GLY GLY C . n 
C 2 17  SER 17  17  17  SER SER C . n 
C 2 18  LEU 18  18  18  LEU LEU C . n 
C 2 19  ASN 19  19  19  ASN ASN C . n 
C 2 20  LEU 20  20  20  LEU LEU C . n 
C 2 21  ALA 21  21  21  ALA ALA C . n 
C 2 22  CYS 22  22  22  CYS CYS C . n 
C 2 23  VAL 23  23  23  VAL VAL C . n 
C 2 24  SER 24  24  24  SER SER C . n 
C 2 25  SER 25  25  25  SER SER C . n 
C 2 26  GLY 26  26  26  GLY GLY C . n 
C 2 27  ARG 27  27  27  ARG ARG C . n 
C 2 28  THR 28  28  28  THR THR C . n 
C 2 29  PHE 29  29  29  PHE PHE C . n 
C 2 30  SER 30  30  30  SER SER C . n 
C 2 31  THR 31  31  31  THR THR C . n 
C 2 32  TRP 32  32  32  TRP TRP C . n 
C 2 33  LEU 33  33  33  LEU LEU C . n 
C 2 34  MET 34  34  34  MET MET C . n 
C 2 35  GLY 35  35  35  GLY GLY C . n 
C 2 36  TRP 36  36  36  TRP TRP C . n 
C 2 37  PHE 37  37  37  PHE PHE C . n 
C 2 38  ARG 38  38  38  ARG ARG C . n 
C 2 39  GLN 39  39  39  GLN GLN C . n 
C 2 40  ALA 40  40  40  ALA ALA C . n 
C 2 41  PRO 41  41  41  PRO PRO C . n 
C 2 42  GLY 42  42  42  GLY GLY C . n 
C 2 43  LYS 43  43  43  LYS LYS C . n 
C 2 44  GLU 44  44  44  GLU GLU C . n 
C 2 45  ARG 45  45  45  ARG ARG C . n 
C 2 46  GLU 46  46  46  GLU GLU C . n 
C 2 47  PHE 47  47  47  PHE PHE C . n 
C 2 48  VAL 48  48  48  VAL VAL C . n 
C 2 49  ALA 49  49  49  ALA ALA C . n 
C 2 50  SER 50  50  50  SER SER C . n 
C 2 51  ILE 51  51  51  ILE ILE C . n 
C 2 52  ASP 52  52  52  ASP ASP C . n 
C 2 53  TRP 53  53  53  TRP TRP C . n 
C 2 54  ARG 54  54  54  ARG ARG C . n 
C 2 55  SER 55  55  55  SER SER C . n 
C 2 56  SER 56  56  56  SER SER C . n 
C 2 57  SER 57  57  57  SER SER C . n 
C 2 58  THR 58  58  58  THR THR C . n 
C 2 59  THR 59  59  59  THR THR C . n 
C 2 60  TYR 60  60  60  TYR TYR C . n 
C 2 61  ALA 61  61  61  ALA ALA C . n 
C 2 62  ASP 62  62  62  ASP ASP C . n 
C 2 63  SER 63  63  63  SER SER C . n 
C 2 64  VAL 64  64  64  VAL VAL C . n 
C 2 65  LYS 65  65  65  LYS LYS C . n 
C 2 66  GLY 66  66  66  GLY GLY C . n 
C 2 67  ARG 67  67  67  ARG ARG C . n 
C 2 68  PHE 68  68  68  PHE PHE C . n 
C 2 69  THR 69  69  69  THR THR C . n 
C 2 70  ILE 70  70  70  ILE ILE C . n 
C 2 71  SER 71  71  71  SER SER C . n 
C 2 72  ARG 72  72  72  ARG ARG C . n 
C 2 73  ASP 73  73  73  ASP ASP C . n 
C 2 74  ASN 74  74  74  ASN ASN C . n 
C 2 75  ALA 75  75  75  ALA ALA C . n 
C 2 76  LYS 76  76  76  LYS LYS C . n 
C 2 77  ASN 77  77  77  ASN ASN C . n 
C 2 78  THR 78  78  78  THR THR C . n 
C 2 79  MET 79  79  79  MET MET C . n 
C 2 80  TYR 80  80  80  TYR TYR C . n 
C 2 81  LEU 81  81  81  LEU LEU C . n 
C 2 82  GLN 82  82  82  GLN GLN C . n 
C 2 83  MET 83  83  83  MET MET C . n 
C 2 84  THR 84  84  84  THR THR C . n 
C 2 85  GLY 85  85  85  GLY GLY C . n 
C 2 86  LEU 86  86  86  LEU LEU C . n 
C 2 87  LYS 87  87  87  LYS LYS C . n 
C 2 88  PRO 88  88  88  PRO PRO C . n 
C 2 89  GLU 89  89  89  GLU GLU C . n 
C 2 90  ASP 90  90  90  ASP ASP C . n 
C 2 91  THR 91  91  91  THR THR C . n 
C 2 92  ALA 92  92  92  ALA ALA C . n 
C 2 93  VAL 93  93  93  VAL VAL C . n 
C 2 94  TYR 94  94  94  TYR TYR C . n 
C 2 95  TYR 95  95  95  TYR TYR C . n 
C 2 96  CYS 96  96  96  CYS CYS C . n 
C 2 97  ALA 97  97  97  ALA ALA C . n 
C 2 98  SER 98  98  98  SER SER C . n 
C 2 99  ASP 99  99  99  ASP ASP C . n 
C 2 100 ARG 100 100 100 ARG ARG C . n 
C 2 101 ASP 101 101 101 ASP ASP C . n 
C 2 102 HIS 102 102 102 HIS HIS C . n 
C 2 103 TYR 103 103 103 TYR TYR C . n 
C 2 104 SER 104 104 104 SER SER C . n 
C 2 105 GLY 105 105 105 GLY GLY C . n 
C 2 106 THR 106 106 106 THR THR C . n 
C 2 107 TYR 107 107 107 TYR TYR C . n 
C 2 108 TYR 108 108 108 TYR TYR C . n 
C 2 109 GLY 109 109 109 GLY GLY C . n 
C 2 110 ARG 110 110 110 ARG ARG C . n 
C 2 111 ARG 111 111 111 ARG ARG C . n 
C 2 112 PHE 112 112 112 PHE PHE C . n 
C 2 113 VAL 113 113 113 VAL VAL C . n 
C 2 114 GLU 114 114 114 GLU GLU C . n 
C 2 115 GLU 115 115 115 GLU GLU C . n 
C 2 116 TYR 116 116 116 TYR TYR C . n 
C 2 117 ASP 117 117 117 ASP ASP C . n 
C 2 118 TYR 118 118 118 TYR TYR C . n 
C 2 119 TRP 119 119 119 TRP TRP C . n 
C 2 120 GLY 120 120 120 GLY GLY C . n 
C 2 121 GLN 121 121 121 GLN GLN C . n 
C 2 122 GLY 122 122 122 GLY GLY C . n 
C 2 123 THR 123 123 123 THR THR C . n 
C 2 124 GLN 124 124 124 GLN GLN C . n 
C 2 125 VAL 125 125 125 VAL VAL C . n 
C 2 126 THR 126 126 126 THR THR C . n 
C 2 127 VAL 127 127 127 VAL VAL C . n 
C 2 128 SER 128 128 128 SER SER C . n 
C 2 129 SER 129 129 129 SER SER C . n 
C 2 130 HIS 130 130 130 HIS HIS C . n 
C 2 131 HIS 131 131 131 HIS HIS C . n 
C 2 132 HIS 132 132 132 HIS HIS C . n 
C 2 133 HIS 133 133 133 HIS HIS C . n 
C 2 134 HIS 134 134 134 HIS HIS C . n 
C 2 135 HIS 135 135 ?   ?   ?   C . n 
D 2 1   GLN 1   1   1   GLN GLN D . n 
D 2 2   VAL 2   2   2   VAL VAL D . n 
D 2 3   GLN 3   3   3   GLN GLN D . n 
D 2 4   LEU 4   4   4   LEU LEU D . n 
D 2 5   GLN 5   5   5   GLN GLN D . n 
D 2 6   GLU 6   6   6   GLU GLU D . n 
D 2 7   SER 7   7   7   SER SER D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   GLY 9   9   9   GLY GLY D . n 
D 2 10  GLY 10  10  10  GLY GLY D . n 
D 2 11  LEU 11  11  11  LEU LEU D . n 
D 2 12  VAL 12  12  12  VAL VAL D . n 
D 2 13  GLN 13  13  13  GLN GLN D . n 
D 2 14  ALA 14  14  14  ALA ALA D . n 
D 2 15  GLY 15  15  15  GLY GLY D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  SER 17  17  17  SER SER D . n 
D 2 18  LEU 18  18  18  LEU LEU D . n 
D 2 19  ASN 19  19  19  ASN ASN D . n 
D 2 20  LEU 20  20  20  LEU LEU D . n 
D 2 21  ALA 21  21  21  ALA ALA D . n 
D 2 22  CYS 22  22  22  CYS CYS D . n 
D 2 23  VAL 23  23  23  VAL VAL D . n 
D 2 24  SER 24  24  24  SER SER D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  GLY 26  26  26  GLY GLY D . n 
D 2 27  ARG 27  27  27  ARG ARG D . n 
D 2 28  THR 28  28  28  THR THR D . n 
D 2 29  PHE 29  29  29  PHE PHE D . n 
D 2 30  SER 30  30  30  SER SER D . n 
D 2 31  THR 31  31  31  THR THR D . n 
D 2 32  TRP 32  32  32  TRP TRP D . n 
D 2 33  LEU 33  33  33  LEU LEU D . n 
D 2 34  MET 34  34  34  MET MET D . n 
D 2 35  GLY 35  35  35  GLY GLY D . n 
D 2 36  TRP 36  36  36  TRP TRP D . n 
D 2 37  PHE 37  37  37  PHE PHE D . n 
D 2 38  ARG 38  38  38  ARG ARG D . n 
D 2 39  GLN 39  39  39  GLN GLN D . n 
D 2 40  ALA 40  40  40  ALA ALA D . n 
D 2 41  PRO 41  41  41  PRO PRO D . n 
D 2 42  GLY 42  42  42  GLY GLY D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  GLU 44  44  44  GLU GLU D . n 
D 2 45  ARG 45  45  45  ARG ARG D . n 
D 2 46  GLU 46  46  46  GLU GLU D . n 
D 2 47  PHE 47  47  47  PHE PHE D . n 
D 2 48  VAL 48  48  48  VAL VAL D . n 
D 2 49  ALA 49  49  49  ALA ALA D . n 
D 2 50  SER 50  50  50  SER SER D . n 
D 2 51  ILE 51  51  51  ILE ILE D . n 
D 2 52  ASP 52  52  52  ASP ASP D . n 
D 2 53  TRP 53  53  53  TRP TRP D . n 
D 2 54  ARG 54  54  54  ARG ARG D . n 
D 2 55  SER 55  55  55  SER SER D . n 
D 2 56  SER 56  56  56  SER SER D . n 
D 2 57  SER 57  57  57  SER SER D . n 
D 2 58  THR 58  58  58  THR THR D . n 
D 2 59  THR 59  59  59  THR THR D . n 
D 2 60  TYR 60  60  60  TYR TYR D . n 
D 2 61  ALA 61  61  61  ALA ALA D . n 
D 2 62  ASP 62  62  62  ASP ASP D . n 
D 2 63  SER 63  63  63  SER SER D . n 
D 2 64  VAL 64  64  64  VAL VAL D . n 
D 2 65  LYS 65  65  65  LYS LYS D . n 
D 2 66  GLY 66  66  66  GLY GLY D . n 
D 2 67  ARG 67  67  67  ARG ARG D . n 
D 2 68  PHE 68  68  68  PHE PHE D . n 
D 2 69  THR 69  69  69  THR THR D . n 
D 2 70  ILE 70  70  70  ILE ILE D . n 
D 2 71  SER 71  71  71  SER SER D . n 
D 2 72  ARG 72  72  72  ARG ARG D . n 
D 2 73  ASP 73  73  73  ASP ASP D . n 
D 2 74  ASN 74  74  74  ASN ASN D . n 
D 2 75  ALA 75  75  75  ALA ALA D . n 
D 2 76  LYS 76  76  76  LYS LYS D . n 
D 2 77  ASN 77  77  77  ASN ASN D . n 
D 2 78  THR 78  78  78  THR THR D . n 
D 2 79  MET 79  79  79  MET MET D . n 
D 2 80  TYR 80  80  80  TYR TYR D . n 
D 2 81  LEU 81  81  81  LEU LEU D . n 
D 2 82  GLN 82  82  82  GLN GLN D . n 
D 2 83  MET 83  83  83  MET MET D . n 
D 2 84  THR 84  84  84  THR THR D . n 
D 2 85  GLY 85  85  85  GLY GLY D . n 
D 2 86  LEU 86  86  86  LEU LEU D . n 
D 2 87  LYS 87  87  87  LYS LYS D . n 
D 2 88  PRO 88  88  88  PRO PRO D . n 
D 2 89  GLU 89  89  89  GLU GLU D . n 
D 2 90  ASP 90  90  90  ASP ASP D . n 
D 2 91  THR 91  91  91  THR THR D . n 
D 2 92  ALA 92  92  92  ALA ALA D . n 
D 2 93  VAL 93  93  93  VAL VAL D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  TYR 95  95  95  TYR TYR D . n 
D 2 96  CYS 96  96  96  CYS CYS D . n 
D 2 97  ALA 97  97  97  ALA ALA D . n 
D 2 98  SER 98  98  98  SER SER D . n 
D 2 99  ASP 99  99  99  ASP ASP D . n 
D 2 100 ARG 100 100 100 ARG ARG D . n 
D 2 101 ASP 101 101 101 ASP ASP D . n 
D 2 102 HIS 102 102 102 HIS HIS D . n 
D 2 103 TYR 103 103 103 TYR TYR D . n 
D 2 104 SER 104 104 104 SER SER D . n 
D 2 105 GLY 105 105 105 GLY GLY D . n 
D 2 106 THR 106 106 106 THR THR D . n 
D 2 107 TYR 107 107 107 TYR TYR D . n 
D 2 108 TYR 108 108 108 TYR TYR D . n 
D 2 109 GLY 109 109 109 GLY GLY D . n 
D 2 110 ARG 110 110 110 ARG ARG D . n 
D 2 111 ARG 111 111 111 ARG ARG D . n 
D 2 112 PHE 112 112 112 PHE PHE D . n 
D 2 113 VAL 113 113 113 VAL VAL D . n 
D 2 114 GLU 114 114 114 GLU GLU D . n 
D 2 115 GLU 115 115 115 GLU GLU D . n 
D 2 116 TYR 116 116 116 TYR TYR D . n 
D 2 117 ASP 117 117 117 ASP ASP D . n 
D 2 118 TYR 118 118 118 TYR TYR D . n 
D 2 119 TRP 119 119 119 TRP TRP D . n 
D 2 120 GLY 120 120 120 GLY GLY D . n 
D 2 121 GLN 121 121 121 GLN GLN D . n 
D 2 122 GLY 122 122 122 GLY GLY D . n 
D 2 123 THR 123 123 123 THR THR D . n 
D 2 124 GLN 124 124 124 GLN GLN D . n 
D 2 125 VAL 125 125 125 VAL VAL D . n 
D 2 126 THR 126 126 126 THR THR D . n 
D 2 127 VAL 127 127 127 VAL VAL D . n 
D 2 128 SER 128 128 128 SER SER D . n 
D 2 129 SER 129 129 129 SER SER D . n 
D 2 130 HIS 130 130 ?   ?   ?   D . n 
D 2 131 HIS 131 131 ?   ?   ?   D . n 
D 2 132 HIS 132 132 ?   ?   ?   D . n 
D 2 133 HIS 133 133 ?   ?   ?   D . n 
D 2 134 HIS 134 134 ?   ?   ?   D . n 
D 2 135 HIS 135 135 ?   ?   ?   D . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              g.hansman@griffith.edu.au 
_pdbx_contact_author.name_first         Grant 
_pdbx_contact_author.name_last          Hansman 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8735-4618 
# 
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 3 HOH 1   601 70  HOH HOH A . 
E 3 HOH 2   602 177 HOH HOH A . 
E 3 HOH 3   603 240 HOH HOH A . 
E 3 HOH 4   604 147 HOH HOH A . 
E 3 HOH 5   605 136 HOH HOH A . 
E 3 HOH 6   606 67  HOH HOH A . 
E 3 HOH 7   607 72  HOH HOH A . 
E 3 HOH 8   608 97  HOH HOH A . 
E 3 HOH 9   609 257 HOH HOH A . 
E 3 HOH 10  610 144 HOH HOH A . 
E 3 HOH 11  611 79  HOH HOH A . 
E 3 HOH 12  612 34  HOH HOH A . 
E 3 HOH 13  613 179 HOH HOH A . 
E 3 HOH 14  614 258 HOH HOH A . 
E 3 HOH 15  615 155 HOH HOH A . 
E 3 HOH 16  616 166 HOH HOH A . 
E 3 HOH 17  617 233 HOH HOH A . 
E 3 HOH 18  618 29  HOH HOH A . 
E 3 HOH 19  619 151 HOH HOH A . 
E 3 HOH 20  620 58  HOH HOH A . 
E 3 HOH 21  621 163 HOH HOH A . 
E 3 HOH 22  622 129 HOH HOH A . 
E 3 HOH 23  623 93  HOH HOH A . 
E 3 HOH 24  624 65  HOH HOH A . 
E 3 HOH 25  625 248 HOH HOH A . 
E 3 HOH 26  626 231 HOH HOH A . 
E 3 HOH 27  627 114 HOH HOH A . 
E 3 HOH 28  628 238 HOH HOH A . 
E 3 HOH 29  629 239 HOH HOH A . 
E 3 HOH 30  630 30  HOH HOH A . 
E 3 HOH 31  631 245 HOH HOH A . 
E 3 HOH 32  632 181 HOH HOH A . 
E 3 HOH 33  633 10  HOH HOH A . 
E 3 HOH 34  634 159 HOH HOH A . 
E 3 HOH 35  635 33  HOH HOH A . 
E 3 HOH 36  636 104 HOH HOH A . 
E 3 HOH 37  637 124 HOH HOH A . 
E 3 HOH 38  638 4   HOH HOH A . 
E 3 HOH 39  639 86  HOH HOH A . 
E 3 HOH 40  640 52  HOH HOH A . 
E 3 HOH 41  641 173 HOH HOH A . 
E 3 HOH 42  642 26  HOH HOH A . 
E 3 HOH 43  643 20  HOH HOH A . 
E 3 HOH 44  644 54  HOH HOH A . 
E 3 HOH 45  645 107 HOH HOH A . 
E 3 HOH 46  646 210 HOH HOH A . 
E 3 HOH 47  647 117 HOH HOH A . 
E 3 HOH 48  648 247 HOH HOH A . 
E 3 HOH 49  649 7   HOH HOH A . 
E 3 HOH 50  650 25  HOH HOH A . 
E 3 HOH 51  651 108 HOH HOH A . 
E 3 HOH 52  652 42  HOH HOH A . 
E 3 HOH 53  653 158 HOH HOH A . 
E 3 HOH 54  654 227 HOH HOH A . 
E 3 HOH 55  655 46  HOH HOH A . 
E 3 HOH 56  656 220 HOH HOH A . 
E 3 HOH 57  657 228 HOH HOH A . 
E 3 HOH 58  658 208 HOH HOH A . 
E 3 HOH 59  659 232 HOH HOH A . 
E 3 HOH 60  660 44  HOH HOH A . 
E 3 HOH 61  661 198 HOH HOH A . 
E 3 HOH 62  662 111 HOH HOH A . 
E 3 HOH 63  663 223 HOH HOH A . 
E 3 HOH 64  664 156 HOH HOH A . 
E 3 HOH 65  665 99  HOH HOH A . 
E 3 HOH 66  666 234 HOH HOH A . 
E 3 HOH 67  667 134 HOH HOH A . 
E 3 HOH 68  668 11  HOH HOH A . 
E 3 HOH 69  669 96  HOH HOH A . 
E 3 HOH 70  670 21  HOH HOH A . 
E 3 HOH 71  671 48  HOH HOH A . 
E 3 HOH 72  672 203 HOH HOH A . 
E 3 HOH 73  673 6   HOH HOH A . 
E 3 HOH 74  674 57  HOH HOH A . 
E 3 HOH 75  675 75  HOH HOH A . 
E 3 HOH 76  676 98  HOH HOH A . 
E 3 HOH 77  677 237 HOH HOH A . 
E 3 HOH 78  678 160 HOH HOH A . 
E 3 HOH 79  679 77  HOH HOH A . 
E 3 HOH 80  680 83  HOH HOH A . 
E 3 HOH 81  681 244 HOH HOH A . 
E 3 HOH 82  682 115 HOH HOH A . 
E 3 HOH 83  683 15  HOH HOH A . 
E 3 HOH 84  684 260 HOH HOH A . 
E 3 HOH 85  685 23  HOH HOH A . 
E 3 HOH 86  686 171 HOH HOH A . 
E 3 HOH 87  687 189 HOH HOH A . 
E 3 HOH 88  688 207 HOH HOH A . 
E 3 HOH 89  689 264 HOH HOH A . 
E 3 HOH 90  690 41  HOH HOH A . 
E 3 HOH 91  691 197 HOH HOH A . 
E 3 HOH 92  692 262 HOH HOH A . 
E 3 HOH 93  693 120 HOH HOH A . 
E 3 HOH 94  694 219 HOH HOH A . 
E 3 HOH 95  695 139 HOH HOH A . 
E 3 HOH 96  696 265 HOH HOH A . 
E 3 HOH 97  697 112 HOH HOH A . 
E 3 HOH 98  698 2   HOH HOH A . 
E 3 HOH 99  699 215 HOH HOH A . 
E 3 HOH 100 700 78  HOH HOH A . 
F 3 HOH 1   601 126 HOH HOH B . 
F 3 HOH 2   602 259 HOH HOH B . 
F 3 HOH 3   603 222 HOH HOH B . 
F 3 HOH 4   604 230 HOH HOH B . 
F 3 HOH 5   605 175 HOH HOH B . 
F 3 HOH 6   606 63  HOH HOH B . 
F 3 HOH 7   607 241 HOH HOH B . 
F 3 HOH 8   608 5   HOH HOH B . 
F 3 HOH 9   609 121 HOH HOH B . 
F 3 HOH 10  610 206 HOH HOH B . 
F 3 HOH 11  611 196 HOH HOH B . 
F 3 HOH 12  612 194 HOH HOH B . 
F 3 HOH 13  613 82  HOH HOH B . 
F 3 HOH 14  614 87  HOH HOH B . 
F 3 HOH 15  615 229 HOH HOH B . 
F 3 HOH 16  616 17  HOH HOH B . 
F 3 HOH 17  617 66  HOH HOH B . 
F 3 HOH 18  618 102 HOH HOH B . 
F 3 HOH 19  619 49  HOH HOH B . 
F 3 HOH 20  620 211 HOH HOH B . 
F 3 HOH 21  621 8   HOH HOH B . 
F 3 HOH 22  622 236 HOH HOH B . 
F 3 HOH 23  623 61  HOH HOH B . 
F 3 HOH 24  624 84  HOH HOH B . 
F 3 HOH 25  625 143 HOH HOH B . 
F 3 HOH 26  626 105 HOH HOH B . 
F 3 HOH 27  627 24  HOH HOH B . 
F 3 HOH 28  628 235 HOH HOH B . 
F 3 HOH 29  629 202 HOH HOH B . 
F 3 HOH 30  630 27  HOH HOH B . 
F 3 HOH 31  631 116 HOH HOH B . 
F 3 HOH 32  632 14  HOH HOH B . 
F 3 HOH 33  633 62  HOH HOH B . 
F 3 HOH 34  634 101 HOH HOH B . 
F 3 HOH 35  635 64  HOH HOH B . 
F 3 HOH 36  636 47  HOH HOH B . 
F 3 HOH 37  637 35  HOH HOH B . 
F 3 HOH 38  638 182 HOH HOH B . 
F 3 HOH 39  639 76  HOH HOH B . 
F 3 HOH 40  640 122 HOH HOH B . 
F 3 HOH 41  641 149 HOH HOH B . 
F 3 HOH 42  642 90  HOH HOH B . 
F 3 HOH 43  643 32  HOH HOH B . 
F 3 HOH 44  644 16  HOH HOH B . 
F 3 HOH 45  645 162 HOH HOH B . 
F 3 HOH 46  646 146 HOH HOH B . 
F 3 HOH 47  647 40  HOH HOH B . 
F 3 HOH 48  648 100 HOH HOH B . 
F 3 HOH 49  649 56  HOH HOH B . 
F 3 HOH 50  650 224 HOH HOH B . 
F 3 HOH 51  651 94  HOH HOH B . 
F 3 HOH 52  652 68  HOH HOH B . 
F 3 HOH 53  653 167 HOH HOH B . 
F 3 HOH 54  654 45  HOH HOH B . 
F 3 HOH 55  655 204 HOH HOH B . 
F 3 HOH 56  656 85  HOH HOH B . 
F 3 HOH 57  657 225 HOH HOH B . 
F 3 HOH 58  658 201 HOH HOH B . 
F 3 HOH 59  659 185 HOH HOH B . 
F 3 HOH 60  660 22  HOH HOH B . 
F 3 HOH 61  661 128 HOH HOH B . 
F 3 HOH 62  662 191 HOH HOH B . 
F 3 HOH 63  663 69  HOH HOH B . 
F 3 HOH 64  664 253 HOH HOH B . 
F 3 HOH 65  665 74  HOH HOH B . 
F 3 HOH 66  666 148 HOH HOH B . 
F 3 HOH 67  667 36  HOH HOH B . 
F 3 HOH 68  668 141 HOH HOH B . 
F 3 HOH 69  669 106 HOH HOH B . 
F 3 HOH 70  670 140 HOH HOH B . 
F 3 HOH 71  671 81  HOH HOH B . 
F 3 HOH 72  672 12  HOH HOH B . 
F 3 HOH 73  673 152 HOH HOH B . 
F 3 HOH 74  674 1   HOH HOH B . 
F 3 HOH 75  675 37  HOH HOH B . 
F 3 HOH 76  676 88  HOH HOH B . 
F 3 HOH 77  677 209 HOH HOH B . 
F 3 HOH 78  678 246 HOH HOH B . 
F 3 HOH 79  679 267 HOH HOH B . 
F 3 HOH 80  680 165 HOH HOH B . 
F 3 HOH 81  681 110 HOH HOH B . 
F 3 HOH 82  682 53  HOH HOH B . 
F 3 HOH 83  683 145 HOH HOH B . 
F 3 HOH 84  684 59  HOH HOH B . 
F 3 HOH 85  685 9   HOH HOH B . 
F 3 HOH 86  686 123 HOH HOH B . 
F 3 HOH 87  687 176 HOH HOH B . 
F 3 HOH 88  688 103 HOH HOH B . 
F 3 HOH 89  689 92  HOH HOH B . 
F 3 HOH 90  690 43  HOH HOH B . 
F 3 HOH 91  691 172 HOH HOH B . 
F 3 HOH 92  692 214 HOH HOH B . 
F 3 HOH 93  693 216 HOH HOH B . 
F 3 HOH 94  694 200 HOH HOH B . 
F 3 HOH 95  695 205 HOH HOH B . 
F 3 HOH 96  696 170 HOH HOH B . 
F 3 HOH 97  697 183 HOH HOH B . 
F 3 HOH 98  698 132 HOH HOH B . 
F 3 HOH 99  699 254 HOH HOH B . 
F 3 HOH 100 700 213 HOH HOH B . 
F 3 HOH 101 701 273 HOH HOH B . 
F 3 HOH 102 702 269 HOH HOH B . 
G 3 HOH 1   201 51  HOH HOH C . 
G 3 HOH 2   202 190 HOH HOH C . 
G 3 HOH 3   203 142 HOH HOH C . 
G 3 HOH 4   204 249 HOH HOH C . 
G 3 HOH 5   205 125 HOH HOH C . 
G 3 HOH 6   206 193 HOH HOH C . 
G 3 HOH 7   207 186 HOH HOH C . 
G 3 HOH 8   208 256 HOH HOH C . 
G 3 HOH 9   209 127 HOH HOH C . 
G 3 HOH 10  210 153 HOH HOH C . 
G 3 HOH 11  211 161 HOH HOH C . 
G 3 HOH 12  212 71  HOH HOH C . 
G 3 HOH 13  213 174 HOH HOH C . 
G 3 HOH 14  214 38  HOH HOH C . 
G 3 HOH 15  215 50  HOH HOH C . 
G 3 HOH 16  216 31  HOH HOH C . 
G 3 HOH 17  217 91  HOH HOH C . 
G 3 HOH 18  218 138 HOH HOH C . 
G 3 HOH 19  219 60  HOH HOH C . 
G 3 HOH 20  220 13  HOH HOH C . 
G 3 HOH 21  221 150 HOH HOH C . 
G 3 HOH 22  222 133 HOH HOH C . 
G 3 HOH 23  223 130 HOH HOH C . 
G 3 HOH 24  224 266 HOH HOH C . 
G 3 HOH 25  225 109 HOH HOH C . 
G 3 HOH 26  226 89  HOH HOH C . 
G 3 HOH 27  227 28  HOH HOH C . 
G 3 HOH 28  228 272 HOH HOH C . 
G 3 HOH 29  229 19  HOH HOH C . 
G 3 HOH 30  230 187 HOH HOH C . 
G 3 HOH 31  231 226 HOH HOH C . 
G 3 HOH 32  232 73  HOH HOH C . 
G 3 HOH 33  233 255 HOH HOH C . 
G 3 HOH 34  234 188 HOH HOH C . 
G 3 HOH 35  235 137 HOH HOH C . 
G 3 HOH 36  236 80  HOH HOH C . 
G 3 HOH 37  237 221 HOH HOH C . 
G 3 HOH 38  238 243 HOH HOH C . 
G 3 HOH 39  239 252 HOH HOH C . 
G 3 HOH 40  240 199 HOH HOH C . 
G 3 HOH 41  241 263 HOH HOH C . 
G 3 HOH 42  242 212 HOH HOH C . 
G 3 HOH 43  243 218 HOH HOH C . 
G 3 HOH 44  244 168 HOH HOH C . 
H 3 HOH 1   201 271 HOH HOH D . 
H 3 HOH 2   202 268 HOH HOH D . 
H 3 HOH 3   203 270 HOH HOH D . 
H 3 HOH 4   204 169 HOH HOH D . 
H 3 HOH 5   205 195 HOH HOH D . 
H 3 HOH 6   206 261 HOH HOH D . 
H 3 HOH 7   207 131 HOH HOH D . 
H 3 HOH 8   208 119 HOH HOH D . 
H 3 HOH 9   209 157 HOH HOH D . 
H 3 HOH 10  210 164 HOH HOH D . 
H 3 HOH 11  211 180 HOH HOH D . 
H 3 HOH 12  212 250 HOH HOH D . 
H 3 HOH 13  213 242 HOH HOH D . 
H 3 HOH 14  214 55  HOH HOH D . 
H 3 HOH 15  215 251 HOH HOH D . 
H 3 HOH 16  216 39  HOH HOH D . 
H 3 HOH 17  217 135 HOH HOH D . 
H 3 HOH 18  218 18  HOH HOH D . 
H 3 HOH 19  219 3   HOH HOH D . 
H 3 HOH 20  220 178 HOH HOH D . 
H 3 HOH 21  221 184 HOH HOH D . 
H 3 HOH 22  222 113 HOH HOH D . 
H 3 HOH 23  223 118 HOH HOH D . 
H 3 HOH 24  224 217 HOH HOH D . 
H 3 HOH 25  225 95  HOH HOH D . 
H 3 HOH 26  226 192 HOH HOH D . 
H 3 HOH 27  227 154 HOH HOH D . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_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_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 701 ? F HOH . 
2 1 B HOH 702 ? F HOH . 
# 
_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       2023-03-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -x,y,-z             
3 x+1/2,y+1/2,z+1/2   
4 -x+1/2,y+1/2,-z+1/2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG B SER 470 ? ? O   B VAL 521 ? ? 2.16 
2 1 OG D SER 25  ? ? O   D HOH 201 ? ? 2.18 
3 1 NZ B LYS 329 ? ? OD1 B ASP 391 ? ? 2.18 
# 
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 ASN A 282 ? ? -89.51  40.49   
2  1 ASP A 341 ? ? -151.87 4.01    
3  1 ARG A 373 ? ? -153.18 -28.58  
4  1 VAL A 386 ? ? -120.17 -54.12  
5  1 ASP A 391 ? ? -127.04 -169.36 
6  1 THR A 425 ? ? -106.90 -64.34  
7  1 SER A 442 ? ? -174.21 144.66  
8  1 GLN B 260 ? ? -141.18 59.66   
9  1 ASN B 282 ? ? -93.67  40.31   
10 1 THR B 369 ? ? -113.12 -166.46 
11 1 ARG B 373 ? ? -156.27 -32.07  
12 1 VAL B 386 ? ? -121.77 -54.48  
13 1 GLN B 390 ? ? -168.70 109.27  
14 1 ASP B 391 ? ? -148.94 25.47   
15 1 THR B 394 ? ? 42.17   -136.93 
16 1 THR B 395 ? ? -36.97  -29.74  
17 1 HIS B 396 ? ? -38.01  136.82  
18 1 SER B 442 ? ? -171.03 143.95  
19 1 THR B 502 ? ? -153.05 28.83   
20 1 VAL C 48  ? ? -120.16 -56.48  
21 1 VAL D 48  ? ? -121.95 -56.78  
# 
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 GLY 531 ? A GLY 308 
2  1 Y 1 A ASN 532 ? A ASN 309 
3  1 Y 1 A GLY 533 ? A GLY 310 
4  1 Y 1 A THR 534 ? A THR 311 
5  1 Y 1 A GLY 535 ? A GLY 312 
6  1 Y 1 A ARG 536 ? A ARG 313 
7  1 Y 1 A ARG 537 ? A ARG 314 
8  1 Y 1 A ARG 538 ? A ARG 315 
9  1 Y 1 A ALA 539 ? A ALA 316 
10 1 Y 1 A VAL 540 ? A VAL 317 
11 1 Y 1 B GLY 531 ? B GLY 308 
12 1 Y 1 B ASN 532 ? B ASN 309 
13 1 Y 1 B GLY 533 ? B GLY 310 
14 1 Y 1 B THR 534 ? B THR 311 
15 1 Y 1 B GLY 535 ? B GLY 312 
16 1 Y 1 B ARG 536 ? B ARG 313 
17 1 Y 1 B ARG 537 ? B ARG 314 
18 1 Y 1 B ARG 538 ? B ARG 315 
19 1 Y 1 B ALA 539 ? B ALA 316 
20 1 Y 1 B VAL 540 ? B VAL 317 
21 1 Y 1 C HIS 135 ? C HIS 135 
22 1 Y 1 D HIS 130 ? D HIS 130 
23 1 Y 1 D HIS 131 ? D HIS 131 
24 1 Y 1 D HIS 132 ? D HIS 132 
25 1 Y 1 D HIS 133 ? D HIS 133 
26 1 Y 1 D HIS 134 ? D HIS 134 
27 1 Y 1 D HIS 135 ? D HIS 135 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
_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                ? 
# 
_space_group.name_H-M_alt     'I 1 2 1' 
_space_group.name_Hall        'C 2y (x,y,-x+z)' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
