data_9G4W
# 
_entry.id   9G4W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9G4W         pdb_00009g4w 10.2210/pdb9g4w/pdb 
WWPDB D_1292140342 ?            ?                   
# 
_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       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G4W 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9G4S unspecified 
PDB . 9G4U unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gdutheuil@epicstx.com 
_pdbx_contact_author.name_first         Guillaume 
_pdbx_contact_author.name_last          Dutheuil 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8887-4823 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dutheuil, G.' 1 0000-0002-8887-4823 
'Oukoloff, K.' 2 0009-0002-6603-1136 
# 
_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                     
'Crystal structure of the human METTL3-METTL14 in complex with small molecule inhibitor Compound 59' 
_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 'Dutheuil, G.' 1 0000-0002-8887-4823 
primary 'Oukoloff, K.' 2 0009-0002-6603-1136 
# 
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 'N6-adenosine-methyltransferase catalytic subunit' 24527.184 1   2.1.1.348 ? ? ? 
2 polymer     man 'N6-adenosine-methyltransferase non-catalytic subunit' 32411.834 1   ?         ? ? ? 
3 non-polymer syn 
;4-[(3~{R})-3-(cyclopropylmethylamino)piperidin-1-yl]-1-[(1~{R})-1-[4-(6-pyrrolidin-1-ylpyrazin-2-yl)-1,2,3-triazol-1-yl]ethyl]pyridin-2-one
;
489.616   1   ?         ? ? ? 
4 non-polymer syn 'CALCIUM ION' 40.078    3   ?         ? ? ? 
5 water       nat water 18.015    325 ?         ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Methyltransferase-like protein 3,hMETTL3,N6-adenosine-methyltransferase 70 kDa subunit,MT-A70' 
2 'Methyltransferase-like protein 14,hMETTL14'                                                    
# 
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 
;ADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECL
NLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERL
SPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKP
;
;ADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECL
NLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERL
SPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKP
;
A ? 
2 'polypeptide(L)' no no 
;NDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLE
EYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLD
PKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPG
WLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERL
;
;NDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLE
EYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLD
PKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPG
WLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERL
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;4-[(3~{R})-3-(cyclopropylmethylamino)piperidin-1-yl]-1-[(1~{R})-1-[4-(6-pyrrolidin-1-ylpyrazin-2-yl)-1,2,3-triazol-1-yl]ethyl]pyridin-2-one
;
A1IIM 
4 'CALCIUM ION' CA    
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   ARG n 
1 4   LEU n 
1 5   PHE n 
1 6   PRO n 
1 7   PRO n 
1 8   GLN n 
1 9   TRP n 
1 10  ILE n 
1 11  CYS n 
1 12  CYS n 
1 13  ASP n 
1 14  ILE n 
1 15  ARG n 
1 16  TYR n 
1 17  LEU n 
1 18  ASP n 
1 19  VAL n 
1 20  SER n 
1 21  ILE n 
1 22  LEU n 
1 23  GLY n 
1 24  LYS n 
1 25  PHE n 
1 26  ALA n 
1 27  VAL n 
1 28  VAL n 
1 29  MET n 
1 30  ALA n 
1 31  ASP n 
1 32  PRO n 
1 33  PRO n 
1 34  TRP n 
1 35  ASP n 
1 36  ILE n 
1 37  HIS n 
1 38  MET n 
1 39  GLU n 
1 40  LEU n 
1 41  PRO n 
1 42  TYR n 
1 43  GLY n 
1 44  THR n 
1 45  LEU n 
1 46  THR n 
1 47  ASP n 
1 48  ASP n 
1 49  GLU n 
1 50  MET n 
1 51  ARG n 
1 52  ARG n 
1 53  LEU n 
1 54  ASN n 
1 55  ILE n 
1 56  PRO n 
1 57  VAL n 
1 58  LEU n 
1 59  GLN n 
1 60  ASP n 
1 61  ASP n 
1 62  GLY n 
1 63  PHE n 
1 64  LEU n 
1 65  PHE n 
1 66  LEU n 
1 67  TRP n 
1 68  VAL n 
1 69  THR n 
1 70  GLY n 
1 71  ARG n 
1 72  ALA n 
1 73  MET n 
1 74  GLU n 
1 75  LEU n 
1 76  GLY n 
1 77  ARG n 
1 78  GLU n 
1 79  CYS n 
1 80  LEU n 
1 81  ASN n 
1 82  LEU n 
1 83  TRP n 
1 84  GLY n 
1 85  TYR n 
1 86  GLU n 
1 87  ARG n 
1 88  VAL n 
1 89  ASP n 
1 90  GLU n 
1 91  ILE n 
1 92  ILE n 
1 93  TRP n 
1 94  VAL n 
1 95  LYS n 
1 96  THR n 
1 97  ASN n 
1 98  GLN n 
1 99  LEU n 
1 100 GLN n 
1 101 ARG n 
1 102 ILE n 
1 103 ILE n 
1 104 ARG n 
1 105 THR n 
1 106 GLY n 
1 107 ARG n 
1 108 THR n 
1 109 GLY n 
1 110 HIS n 
1 111 TRP n 
1 112 LEU n 
1 113 ASN n 
1 114 HIS n 
1 115 GLY n 
1 116 LYS n 
1 117 GLU n 
1 118 HIS n 
1 119 CYS n 
1 120 LEU n 
1 121 VAL n 
1 122 GLY n 
1 123 VAL n 
1 124 LYS n 
1 125 GLY n 
1 126 ASN n 
1 127 PRO n 
1 128 GLN n 
1 129 GLY n 
1 130 PHE n 
1 131 ASN n 
1 132 GLN n 
1 133 GLY n 
1 134 LEU n 
1 135 ASP n 
1 136 CYS n 
1 137 ASP n 
1 138 VAL n 
1 139 ILE n 
1 140 VAL n 
1 141 ALA n 
1 142 GLU n 
1 143 VAL n 
1 144 ARG n 
1 145 SER n 
1 146 THR n 
1 147 SER n 
1 148 HIS n 
1 149 LYS n 
1 150 PRO n 
1 151 ASP n 
1 152 GLU n 
1 153 ILE n 
1 154 TYR n 
1 155 GLY n 
1 156 MET n 
1 157 ILE n 
1 158 GLU n 
1 159 ARG n 
1 160 LEU n 
1 161 SER n 
1 162 PRO n 
1 163 GLY n 
1 164 THR n 
1 165 ARG n 
1 166 LYS n 
1 167 ILE n 
1 168 GLU n 
1 169 LEU n 
1 170 PHE n 
1 171 GLY n 
1 172 ARG n 
1 173 PRO n 
1 174 HIS n 
1 175 ASN n 
1 176 VAL n 
1 177 GLN n 
1 178 PRO n 
1 179 ASN n 
1 180 TRP n 
1 181 ILE n 
1 182 THR n 
1 183 LEU n 
1 184 GLY n 
1 185 ASN n 
1 186 GLN n 
1 187 LEU n 
1 188 ASP n 
1 189 GLY n 
1 190 ILE n 
1 191 HIS n 
1 192 LEU n 
1 193 LEU n 
1 194 ASP n 
1 195 PRO n 
1 196 ASP n 
1 197 VAL n 
1 198 VAL n 
1 199 ALA n 
1 200 ARG n 
1 201 PHE n 
1 202 LYS n 
1 203 GLN n 
1 204 ARG n 
1 205 TYR n 
1 206 PRO n 
1 207 ASP n 
1 208 GLY n 
1 209 ILE n 
1 210 ILE n 
1 211 SER n 
1 212 LYS n 
1 213 PRO n 
2 1   ASN n 
2 2   ASP n 
2 3   TYR n 
2 4   CYS n 
2 5   GLN n 
2 6   HIS n 
2 7   PHE n 
2 8   VAL n 
2 9   ASP n 
2 10  THR n 
2 11  GLY n 
2 12  HIS n 
2 13  ARG n 
2 14  PRO n 
2 15  GLN n 
2 16  ASN n 
2 17  PHE n 
2 18  ILE n 
2 19  ARG n 
2 20  ASP n 
2 21  VAL n 
2 22  GLY n 
2 23  LEU n 
2 24  ALA n 
2 25  ASP n 
2 26  ARG n 
2 27  PHE n 
2 28  GLU n 
2 29  GLU n 
2 30  TYR n 
2 31  PRO n 
2 32  LYS n 
2 33  LEU n 
2 34  ARG n 
2 35  GLU n 
2 36  LEU n 
2 37  ILE n 
2 38  ARG n 
2 39  LEU n 
2 40  LYS n 
2 41  ASP n 
2 42  GLU n 
2 43  LEU n 
2 44  ILE n 
2 45  ALA n 
2 46  LYS n 
2 47  SER n 
2 48  ASN n 
2 49  THR n 
2 50  PRO n 
2 51  PRO n 
2 52  MET n 
2 53  TYR n 
2 54  LEU n 
2 55  GLN n 
2 56  ALA n 
2 57  ASP n 
2 58  ILE n 
2 59  GLU n 
2 60  ALA n 
2 61  PHE n 
2 62  ASP n 
2 63  ILE n 
2 64  ARG n 
2 65  GLU n 
2 66  LEU n 
2 67  THR n 
2 68  PRO n 
2 69  LYS n 
2 70  PHE n 
2 71  ASP n 
2 72  VAL n 
2 73  ILE n 
2 74  LEU n 
2 75  LEU n 
2 76  GLU n 
2 77  PRO n 
2 78  PRO n 
2 79  LEU n 
2 80  GLU n 
2 81  GLU n 
2 82  TYR n 
2 83  TYR n 
2 84  ARG n 
2 85  GLU n 
2 86  THR n 
2 87  GLY n 
2 88  ILE n 
2 89  THR n 
2 90  ALA n 
2 91  ASN n 
2 92  GLU n 
2 93  LYS n 
2 94  CYS n 
2 95  TRP n 
2 96  THR n 
2 97  TRP n 
2 98  ASP n 
2 99  ASP n 
2 100 ILE n 
2 101 MET n 
2 102 LYS n 
2 103 LEU n 
2 104 GLU n 
2 105 ILE n 
2 106 ASP n 
2 107 GLU n 
2 108 ILE n 
2 109 ALA n 
2 110 ALA n 
2 111 PRO n 
2 112 ARG n 
2 113 SER n 
2 114 PHE n 
2 115 ILE n 
2 116 PHE n 
2 117 LEU n 
2 118 TRP n 
2 119 CYS n 
2 120 GLY n 
2 121 SER n 
2 122 GLY n 
2 123 GLU n 
2 124 GLY n 
2 125 LEU n 
2 126 ASP n 
2 127 LEU n 
2 128 GLY n 
2 129 ARG n 
2 130 VAL n 
2 131 CYS n 
2 132 LEU n 
2 133 ARG n 
2 134 LYS n 
2 135 TRP n 
2 136 GLY n 
2 137 TYR n 
2 138 ARG n 
2 139 ARG n 
2 140 CYS n 
2 141 GLU n 
2 142 ASP n 
2 143 ILE n 
2 144 CYS n 
2 145 TRP n 
2 146 ILE n 
2 147 LYS n 
2 148 THR n 
2 149 ASN n 
2 150 LYS n 
2 151 ASN n 
2 152 ASN n 
2 153 PRO n 
2 154 GLY n 
2 155 LYS n 
2 156 THR n 
2 157 LYS n 
2 158 THR n 
2 159 LEU n 
2 160 ASP n 
2 161 PRO n 
2 162 LYS n 
2 163 ALA n 
2 164 VAL n 
2 165 PHE n 
2 166 GLN n 
2 167 ARG n 
2 168 THR n 
2 169 LYS n 
2 170 GLU n 
2 171 HIS n 
2 172 CYS n 
2 173 LEU n 
2 174 MET n 
2 175 GLY n 
2 176 ILE n 
2 177 LYS n 
2 178 GLY n 
2 179 THR n 
2 180 VAL n 
2 181 LYS n 
2 182 ARG n 
2 183 SER n 
2 184 THR n 
2 185 ASP n 
2 186 GLY n 
2 187 ASP n 
2 188 PHE n 
2 189 ILE n 
2 190 HIS n 
2 191 ALA n 
2 192 ASN n 
2 193 VAL n 
2 194 ASP n 
2 195 ILE n 
2 196 ASP n 
2 197 LEU n 
2 198 ILE n 
2 199 ILE n 
2 200 THR n 
2 201 GLU n 
2 202 GLU n 
2 203 PRO n 
2 204 GLU n 
2 205 ILE n 
2 206 GLY n 
2 207 ASN n 
2 208 ILE n 
2 209 GLU n 
2 210 LYS n 
2 211 PRO n 
2 212 VAL n 
2 213 GLU n 
2 214 ILE n 
2 215 PHE n 
2 216 HIS n 
2 217 ILE n 
2 218 ILE n 
2 219 GLU n 
2 220 HIS n 
2 221 PHE n 
2 222 CYS n 
2 223 LEU n 
2 224 GLY n 
2 225 ARG n 
2 226 ARG n 
2 227 ARG n 
2 228 LEU n 
2 229 HIS n 
2 230 LEU n 
2 231 PHE n 
2 232 GLY n 
2 233 ARG n 
2 234 ASP n 
2 235 SER n 
2 236 THR n 
2 237 ILE n 
2 238 ARG n 
2 239 PRO n 
2 240 GLY n 
2 241 TRP n 
2 242 LEU n 
2 243 THR n 
2 244 VAL n 
2 245 GLY n 
2 246 PRO n 
2 247 THR n 
2 248 LEU n 
2 249 THR n 
2 250 ASN n 
2 251 SER n 
2 252 ASN n 
2 253 TYR n 
2 254 ASN n 
2 255 ALA n 
2 256 GLU n 
2 257 THR n 
2 258 TYR n 
2 259 ALA n 
2 260 SER n 
2 261 TYR n 
2 262 PHE n 
2 263 SER n 
2 264 ALA n 
2 265 PRO n 
2 266 ASN n 
2 267 SER n 
2 268 TYR n 
2 269 LEU n 
2 270 THR n 
2 271 GLY n 
2 272 CYS n 
2 273 THR n 
2 274 GLU n 
2 275 GLU n 
2 276 ILE n 
2 277 GLU n 
2 278 ARG n 
2 279 LEU 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' 1 213 human ? 'METTL3, MTA70'     ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? Sf21 ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 279 human ? 'METTL14, KIAA1627' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? Sf21 ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1IIM non-polymer         . 
;4-[(3~{R})-3-(cyclopropylmethylamino)piperidin-1-yl]-1-[(1~{R})-1-[4-(6-pyrrolidin-1-ylpyrazin-2-yl)-1,2,3-triazol-1-yl]ethyl]pyridin-2-one
;
? 'C26 H35 N9 O'   489.616 
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 
CA    non-polymer         . 'CALCIUM ION' ? 'Ca 2'           40.078  
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 
# 
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   ALA 1   365 365 ALA ALA A . n 
A 1 2   ASP 2   366 366 ASP ASP A . n 
A 1 3   ARG 3   367 367 ARG ARG A . n 
A 1 4   LEU 4   368 368 LEU LEU A . n 
A 1 5   PHE 5   369 369 PHE PHE A . n 
A 1 6   PRO 6   370 370 PRO PRO A . n 
A 1 7   PRO 7   371 371 PRO PRO A . n 
A 1 8   GLN 8   372 372 GLN GLN A . n 
A 1 9   TRP 9   373 373 TRP TRP A . n 
A 1 10  ILE 10  374 374 ILE ILE A . n 
A 1 11  CYS 11  375 375 CYS CYS A . n 
A 1 12  CYS 12  376 376 CYS CYS A . n 
A 1 13  ASP 13  377 377 ASP ASP A . n 
A 1 14  ILE 14  378 378 ILE ILE A . n 
A 1 15  ARG 15  379 379 ARG ARG A . n 
A 1 16  TYR 16  380 380 TYR TYR A . n 
A 1 17  LEU 17  381 381 LEU LEU A . n 
A 1 18  ASP 18  382 382 ASP ASP A . n 
A 1 19  VAL 19  383 383 VAL VAL A . n 
A 1 20  SER 20  384 384 SER SER A . n 
A 1 21  ILE 21  385 385 ILE ILE A . n 
A 1 22  LEU 22  386 386 LEU LEU A . n 
A 1 23  GLY 23  387 387 GLY GLY A . n 
A 1 24  LYS 24  388 388 LYS LYS A . n 
A 1 25  PHE 25  389 389 PHE PHE A . n 
A 1 26  ALA 26  390 390 ALA ALA A . n 
A 1 27  VAL 27  391 391 VAL VAL A . n 
A 1 28  VAL 28  392 392 VAL VAL A . n 
A 1 29  MET 29  393 393 MET MET A . n 
A 1 30  ALA 30  394 394 ALA ALA A . n 
A 1 31  ASP 31  395 395 ASP ASP A . n 
A 1 32  PRO 32  396 396 PRO PRO A . n 
A 1 33  PRO 33  397 397 PRO PRO A . n 
A 1 34  TRP 34  398 398 TRP TRP A . n 
A 1 35  ASP 35  399 399 ASP ASP A . n 
A 1 36  ILE 36  400 400 ILE ILE A . n 
A 1 37  HIS 37  401 401 HIS HIS A . n 
A 1 38  MET 38  402 402 MET MET A . n 
A 1 39  GLU 39  403 403 GLU GLU A . n 
A 1 40  LEU 40  404 404 LEU LEU A . n 
A 1 41  PRO 41  405 405 PRO PRO A . n 
A 1 42  TYR 42  406 406 TYR TYR A . n 
A 1 43  GLY 43  407 407 GLY GLY A . n 
A 1 44  THR 44  408 408 THR THR A . n 
A 1 45  LEU 45  409 409 LEU LEU A . n 
A 1 46  THR 46  410 410 THR THR A . n 
A 1 47  ASP 47  411 411 ASP ASP A . n 
A 1 48  ASP 48  412 412 ASP ASP A . n 
A 1 49  GLU 49  413 413 GLU GLU A . n 
A 1 50  MET 50  414 414 MET MET A . n 
A 1 51  ARG 51  415 415 ARG ARG A . n 
A 1 52  ARG 52  416 416 ARG ARG A . n 
A 1 53  LEU 53  417 417 LEU LEU A . n 
A 1 54  ASN 54  418 418 ASN ASN A . n 
A 1 55  ILE 55  419 419 ILE ILE A . n 
A 1 56  PRO 56  420 420 PRO PRO A . n 
A 1 57  VAL 57  421 421 VAL VAL A . n 
A 1 58  LEU 58  422 422 LEU LEU A . n 
A 1 59  GLN 59  423 423 GLN GLN A . n 
A 1 60  ASP 60  424 424 ASP ASP A . n 
A 1 61  ASP 61  425 425 ASP ASP A . n 
A 1 62  GLY 62  426 426 GLY GLY A . n 
A 1 63  PHE 63  427 427 PHE PHE A . n 
A 1 64  LEU 64  428 428 LEU LEU A . n 
A 1 65  PHE 65  429 429 PHE PHE A . n 
A 1 66  LEU 66  430 430 LEU LEU A . n 
A 1 67  TRP 67  431 431 TRP TRP A . n 
A 1 68  VAL 68  432 432 VAL VAL A . n 
A 1 69  THR 69  433 433 THR THR A . n 
A 1 70  GLY 70  434 434 GLY GLY A . n 
A 1 71  ARG 71  435 435 ARG ARG A . n 
A 1 72  ALA 72  436 436 ALA ALA A . n 
A 1 73  MET 73  437 437 MET MET A . n 
A 1 74  GLU 74  438 438 GLU GLU A . n 
A 1 75  LEU 75  439 439 LEU LEU A . n 
A 1 76  GLY 76  440 440 GLY GLY A . n 
A 1 77  ARG 77  441 441 ARG ARG A . n 
A 1 78  GLU 78  442 442 GLU GLU A . n 
A 1 79  CYS 79  443 443 CYS CYS A . n 
A 1 80  LEU 80  444 444 LEU LEU A . n 
A 1 81  ASN 81  445 445 ASN ASN A . n 
A 1 82  LEU 82  446 446 LEU LEU A . n 
A 1 83  TRP 83  447 447 TRP TRP A . n 
A 1 84  GLY 84  448 448 GLY GLY A . n 
A 1 85  TYR 85  449 449 TYR TYR A . n 
A 1 86  GLU 86  450 450 GLU GLU A . n 
A 1 87  ARG 87  451 451 ARG ARG A . n 
A 1 88  VAL 88  452 452 VAL VAL A . n 
A 1 89  ASP 89  453 453 ASP ASP A . n 
A 1 90  GLU 90  454 454 GLU GLU A . n 
A 1 91  ILE 91  455 455 ILE ILE A . n 
A 1 92  ILE 92  456 456 ILE ILE A . n 
A 1 93  TRP 93  457 457 TRP TRP A . n 
A 1 94  VAL 94  458 458 VAL VAL A . n 
A 1 95  LYS 95  459 459 LYS LYS A . n 
A 1 96  THR 96  460 460 THR THR A . n 
A 1 97  ASN 97  461 461 ASN ASN A . n 
A 1 98  GLN 98  462 462 GLN GLN A . n 
A 1 99  LEU 99  463 463 LEU LEU A . n 
A 1 100 GLN 100 464 464 GLN GLN A . n 
A 1 101 ARG 101 465 465 ARG ARG A . n 
A 1 102 ILE 102 466 466 ILE ILE A . n 
A 1 103 ILE 103 467 467 ILE ILE A . n 
A 1 104 ARG 104 468 468 ARG ARG A . n 
A 1 105 THR 105 469 469 THR THR A . n 
A 1 106 GLY 106 470 470 GLY GLY A . n 
A 1 107 ARG 107 471 471 ARG ARG A . n 
A 1 108 THR 108 472 472 THR THR A . n 
A 1 109 GLY 109 473 473 GLY GLY A . n 
A 1 110 HIS 110 474 474 HIS HIS A . n 
A 1 111 TRP 111 475 475 TRP TRP A . n 
A 1 112 LEU 112 476 476 LEU LEU A . n 
A 1 113 ASN 113 477 477 ASN ASN A . n 
A 1 114 HIS 114 478 478 HIS HIS A . n 
A 1 115 GLY 115 479 479 GLY GLY A . n 
A 1 116 LYS 116 480 480 LYS LYS A . n 
A 1 117 GLU 117 481 481 GLU GLU A . n 
A 1 118 HIS 118 482 482 HIS HIS A . n 
A 1 119 CYS 119 483 483 CYS CYS A . n 
A 1 120 LEU 120 484 484 LEU LEU A . n 
A 1 121 VAL 121 485 485 VAL VAL A . n 
A 1 122 GLY 122 486 486 GLY GLY A . n 
A 1 123 VAL 123 487 487 VAL VAL A . n 
A 1 124 LYS 124 488 488 LYS LYS A . n 
A 1 125 GLY 125 489 489 GLY GLY A . n 
A 1 126 ASN 126 490 490 ASN ASN A . n 
A 1 127 PRO 127 491 491 PRO PRO A . n 
A 1 128 GLN 128 492 492 GLN GLN A . n 
A 1 129 GLY 129 493 493 GLY GLY A . n 
A 1 130 PHE 130 494 494 PHE PHE A . n 
A 1 131 ASN 131 495 495 ASN ASN A . n 
A 1 132 GLN 132 496 496 GLN GLN A . n 
A 1 133 GLY 133 497 497 GLY GLY A . n 
A 1 134 LEU 134 498 498 LEU LEU A . n 
A 1 135 ASP 135 499 499 ASP ASP A . n 
A 1 136 CYS 136 500 500 CYS CYS A . n 
A 1 137 ASP 137 501 501 ASP ASP A . n 
A 1 138 VAL 138 502 502 VAL VAL A . n 
A 1 139 ILE 139 503 503 ILE ILE A . n 
A 1 140 VAL 140 504 504 VAL VAL A . n 
A 1 141 ALA 141 505 505 ALA ALA A . n 
A 1 142 GLU 142 506 506 GLU GLU A . n 
A 1 143 VAL 143 507 507 VAL VAL A . n 
A 1 144 ARG 144 508 508 ARG ARG A . n 
A 1 145 SER 145 509 509 SER SER A . n 
A 1 146 THR 146 510 510 THR THR A . n 
A 1 147 SER 147 511 511 SER SER A . n 
A 1 148 HIS 148 512 512 HIS HIS A . n 
A 1 149 LYS 149 513 513 LYS LYS A . n 
A 1 150 PRO 150 514 514 PRO PRO A . n 
A 1 151 ASP 151 515 515 ASP ASP A . n 
A 1 152 GLU 152 516 516 GLU GLU A . n 
A 1 153 ILE 153 517 517 ILE ILE A . n 
A 1 154 TYR 154 518 518 TYR TYR A . n 
A 1 155 GLY 155 519 519 GLY GLY A . n 
A 1 156 MET 156 520 520 MET MET A . n 
A 1 157 ILE 157 521 521 ILE ILE A . n 
A 1 158 GLU 158 522 522 GLU GLU A . n 
A 1 159 ARG 159 523 523 ARG ARG A . n 
A 1 160 LEU 160 524 524 LEU LEU A . n 
A 1 161 SER 161 525 525 SER SER A . n 
A 1 162 PRO 162 526 526 PRO PRO A . n 
A 1 163 GLY 163 527 527 GLY GLY A . n 
A 1 164 THR 164 528 528 THR THR A . n 
A 1 165 ARG 165 529 529 ARG ARG A . n 
A 1 166 LYS 166 530 530 LYS LYS A . n 
A 1 167 ILE 167 531 531 ILE ILE A . n 
A 1 168 GLU 168 532 532 GLU GLU A . n 
A 1 169 LEU 169 533 533 LEU LEU A . n 
A 1 170 PHE 170 534 534 PHE PHE A . n 
A 1 171 GLY 171 535 535 GLY GLY A . n 
A 1 172 ARG 172 536 536 ARG ARG A . n 
A 1 173 PRO 173 537 537 PRO PRO A . n 
A 1 174 HIS 174 538 538 HIS HIS A . n 
A 1 175 ASN 175 539 539 ASN ASN A . n 
A 1 176 VAL 176 540 540 VAL VAL A . n 
A 1 177 GLN 177 541 541 GLN GLN A . n 
A 1 178 PRO 178 542 542 PRO PRO A . n 
A 1 179 ASN 179 543 543 ASN ASN A . n 
A 1 180 TRP 180 544 544 TRP TRP A . n 
A 1 181 ILE 181 545 545 ILE ILE A . n 
A 1 182 THR 182 546 546 THR THR A . n 
A 1 183 LEU 183 547 547 LEU LEU A . n 
A 1 184 GLY 184 548 548 GLY GLY A . n 
A 1 185 ASN 185 549 549 ASN ASN A . n 
A 1 186 GLN 186 550 550 GLN GLN A . n 
A 1 187 LEU 187 551 551 LEU LEU A . n 
A 1 188 ASP 188 552 552 ASP ASP A . n 
A 1 189 GLY 189 553 553 GLY GLY A . n 
A 1 190 ILE 190 554 554 ILE ILE A . n 
A 1 191 HIS 191 555 555 HIS HIS A . n 
A 1 192 LEU 192 556 556 LEU LEU A . n 
A 1 193 LEU 193 557 557 LEU LEU A . n 
A 1 194 ASP 194 558 558 ASP ASP A . n 
A 1 195 PRO 195 559 559 PRO PRO A . n 
A 1 196 ASP 196 560 560 ASP ASP A . n 
A 1 197 VAL 197 561 561 VAL VAL A . n 
A 1 198 VAL 198 562 562 VAL VAL A . n 
A 1 199 ALA 199 563 563 ALA ALA A . n 
A 1 200 ARG 200 564 564 ARG ARG A . n 
A 1 201 PHE 201 565 565 PHE PHE A . n 
A 1 202 LYS 202 566 566 LYS LYS A . n 
A 1 203 GLN 203 567 567 GLN GLN A . n 
A 1 204 ARG 204 568 568 ARG ARG A . n 
A 1 205 TYR 205 569 569 TYR TYR A . n 
A 1 206 PRO 206 570 570 PRO PRO A . n 
A 1 207 ASP 207 571 571 ASP ASP A . n 
A 1 208 GLY 208 572 572 GLY GLY A . n 
A 1 209 ILE 209 573 573 ILE ILE A . n 
A 1 210 ILE 210 574 574 ILE ILE A . n 
A 1 211 SER 211 575 575 SER SER A . n 
A 1 212 LYS 212 576 576 LYS LYS A . n 
A 1 213 PRO 213 577 577 PRO PRO A . n 
B 2 1   ASN 1   117 117 ASN ASN B . n 
B 2 2   ASP 2   118 118 ASP ASP B . n 
B 2 3   TYR 3   119 119 TYR TYR B . n 
B 2 4   CYS 4   120 120 CYS CYS B . n 
B 2 5   GLN 5   121 121 GLN GLN B . n 
B 2 6   HIS 6   122 122 HIS HIS B . n 
B 2 7   PHE 7   123 123 PHE PHE B . n 
B 2 8   VAL 8   124 124 VAL VAL B . n 
B 2 9   ASP 9   125 125 ASP ASP B . n 
B 2 10  THR 10  126 126 THR THR B . n 
B 2 11  GLY 11  127 127 GLY GLY B . n 
B 2 12  HIS 12  128 128 HIS HIS B . n 
B 2 13  ARG 13  129 129 ARG ARG B . n 
B 2 14  PRO 14  130 130 PRO PRO B . n 
B 2 15  GLN 15  131 131 GLN GLN B . n 
B 2 16  ASN 16  132 132 ASN ASN B . n 
B 2 17  PHE 17  133 133 PHE PHE B . n 
B 2 18  ILE 18  134 134 ILE ILE B . n 
B 2 19  ARG 19  135 135 ARG ARG B . n 
B 2 20  ASP 20  136 136 ASP ASP B . n 
B 2 21  VAL 21  137 137 VAL VAL B . n 
B 2 22  GLY 22  138 ?   ?   ?   B . n 
B 2 23  LEU 23  139 ?   ?   ?   B . n 
B 2 24  ALA 24  140 ?   ?   ?   B . n 
B 2 25  ASP 25  141 ?   ?   ?   B . n 
B 2 26  ARG 26  142 ?   ?   ?   B . n 
B 2 27  PHE 27  143 ?   ?   ?   B . n 
B 2 28  GLU 28  144 ?   ?   ?   B . n 
B 2 29  GLU 29  145 ?   ?   ?   B . n 
B 2 30  TYR 30  146 ?   ?   ?   B . n 
B 2 31  PRO 31  147 ?   ?   ?   B . n 
B 2 32  LYS 32  148 ?   ?   ?   B . n 
B 2 33  LEU 33  149 149 LEU LEU B . n 
B 2 34  ARG 34  150 150 ARG ARG B . n 
B 2 35  GLU 35  151 151 GLU GLU B . n 
B 2 36  LEU 36  152 152 LEU LEU B . n 
B 2 37  ILE 37  153 153 ILE ILE B . n 
B 2 38  ARG 38  154 154 ARG ARG B . n 
B 2 39  LEU 39  155 155 LEU LEU B . n 
B 2 40  LYS 40  156 156 LYS LYS B . n 
B 2 41  ASP 41  157 157 ASP ASP B . n 
B 2 42  GLU 42  158 158 GLU GLU B . n 
B 2 43  LEU 43  159 159 LEU LEU B . n 
B 2 44  ILE 44  160 160 ILE ILE B . n 
B 2 45  ALA 45  161 161 ALA ALA B . n 
B 2 46  LYS 46  162 162 LYS LYS B . n 
B 2 47  SER 47  163 163 SER SER B . n 
B 2 48  ASN 48  164 164 ASN ASN B . n 
B 2 49  THR 49  165 165 THR THR B . n 
B 2 50  PRO 50  166 166 PRO PRO B . n 
B 2 51  PRO 51  167 167 PRO PRO B . n 
B 2 52  MET 52  168 168 MET MET B . n 
B 2 53  TYR 53  169 169 TYR TYR B . n 
B 2 54  LEU 54  170 170 LEU LEU B . n 
B 2 55  GLN 55  171 171 GLN GLN B . n 
B 2 56  ALA 56  172 172 ALA ALA B . n 
B 2 57  ASP 57  173 173 ASP ASP B . n 
B 2 58  ILE 58  174 174 ILE ILE B . n 
B 2 59  GLU 59  175 175 GLU GLU B . n 
B 2 60  ALA 60  176 176 ALA ALA B . n 
B 2 61  PHE 61  177 177 PHE PHE B . n 
B 2 62  ASP 62  178 178 ASP ASP B . n 
B 2 63  ILE 63  179 179 ILE ILE B . n 
B 2 64  ARG 64  180 180 ARG ARG B . n 
B 2 65  GLU 65  181 181 GLU GLU B . n 
B 2 66  LEU 66  182 182 LEU LEU B . n 
B 2 67  THR 67  183 183 THR THR B . n 
B 2 68  PRO 68  184 184 PRO PRO B . n 
B 2 69  LYS 69  185 185 LYS LYS B . n 
B 2 70  PHE 70  186 186 PHE PHE B . n 
B 2 71  ASP 71  187 187 ASP ASP B . n 
B 2 72  VAL 72  188 188 VAL VAL B . n 
B 2 73  ILE 73  189 189 ILE ILE B . n 
B 2 74  LEU 74  190 190 LEU LEU B . n 
B 2 75  LEU 75  191 191 LEU LEU B . n 
B 2 76  GLU 76  192 192 GLU GLU B . n 
B 2 77  PRO 77  193 193 PRO PRO B . n 
B 2 78  PRO 78  194 194 PRO PRO B . n 
B 2 79  LEU 79  195 195 LEU LEU B . n 
B 2 80  GLU 80  196 196 GLU GLU B . n 
B 2 81  GLU 81  197 197 GLU GLU B . n 
B 2 82  TYR 82  198 198 TYR TYR B . n 
B 2 83  TYR 83  199 199 TYR TYR B . n 
B 2 84  ARG 84  200 200 ARG ARG B . n 
B 2 85  GLU 85  201 201 GLU GLU B . n 
B 2 86  THR 86  202 ?   ?   ?   B . n 
B 2 87  GLY 87  203 ?   ?   ?   B . n 
B 2 88  ILE 88  204 ?   ?   ?   B . n 
B 2 89  THR 89  205 ?   ?   ?   B . n 
B 2 90  ALA 90  206 ?   ?   ?   B . n 
B 2 91  ASN 91  207 ?   ?   ?   B . n 
B 2 92  GLU 92  208 208 GLU GLU B . n 
B 2 93  LYS 93  209 209 LYS LYS B . n 
B 2 94  CYS 94  210 210 CYS CYS B . n 
B 2 95  TRP 95  211 211 TRP TRP B . n 
B 2 96  THR 96  212 212 THR THR B . n 
B 2 97  TRP 97  213 213 TRP TRP B . n 
B 2 98  ASP 98  214 214 ASP ASP B . n 
B 2 99  ASP 99  215 215 ASP ASP B . n 
B 2 100 ILE 100 216 216 ILE ILE B . n 
B 2 101 MET 101 217 217 MET MET B . n 
B 2 102 LYS 102 218 218 LYS LYS B . n 
B 2 103 LEU 103 219 219 LEU LEU B . n 
B 2 104 GLU 104 220 220 GLU GLU B . n 
B 2 105 ILE 105 221 221 ILE ILE B . n 
B 2 106 ASP 106 222 222 ASP ASP B . n 
B 2 107 GLU 107 223 223 GLU GLU B . n 
B 2 108 ILE 108 224 224 ILE ILE B . n 
B 2 109 ALA 109 225 225 ALA ALA B . n 
B 2 110 ALA 110 226 226 ALA ALA B . n 
B 2 111 PRO 111 227 227 PRO PRO B . n 
B 2 112 ARG 112 228 228 ARG ARG B . n 
B 2 113 SER 113 229 229 SER SER B . n 
B 2 114 PHE 114 230 230 PHE PHE B . n 
B 2 115 ILE 115 231 231 ILE ILE B . n 
B 2 116 PHE 116 232 232 PHE PHE B . n 
B 2 117 LEU 117 233 233 LEU LEU B . n 
B 2 118 TRP 118 234 234 TRP TRP B . n 
B 2 119 CYS 119 235 235 CYS CYS B . n 
B 2 120 GLY 120 236 236 GLY GLY B . n 
B 2 121 SER 121 237 237 SER SER B . n 
B 2 122 GLY 122 238 238 GLY GLY B . n 
B 2 123 GLU 123 239 239 GLU GLU B . n 
B 2 124 GLY 124 240 240 GLY GLY B . n 
B 2 125 LEU 125 241 241 LEU LEU B . n 
B 2 126 ASP 126 242 242 ASP ASP B . n 
B 2 127 LEU 127 243 243 LEU LEU B . n 
B 2 128 GLY 128 244 244 GLY GLY B . n 
B 2 129 ARG 129 245 245 ARG ARG B . n 
B 2 130 VAL 130 246 246 VAL VAL B . n 
B 2 131 CYS 131 247 247 CYS CYS B . n 
B 2 132 LEU 132 248 248 LEU LEU B . n 
B 2 133 ARG 133 249 249 ARG ARG B . n 
B 2 134 LYS 134 250 250 LYS LYS B . n 
B 2 135 TRP 135 251 251 TRP TRP B . n 
B 2 136 GLY 136 252 252 GLY GLY B . n 
B 2 137 TYR 137 253 253 TYR TYR B . n 
B 2 138 ARG 138 254 254 ARG ARG B . n 
B 2 139 ARG 139 255 255 ARG ARG B . n 
B 2 140 CYS 140 256 256 CYS CYS B . n 
B 2 141 GLU 141 257 257 GLU GLU B . n 
B 2 142 ASP 142 258 258 ASP ASP B . n 
B 2 143 ILE 143 259 259 ILE ILE B . n 
B 2 144 CYS 144 260 260 CYS CYS B . n 
B 2 145 TRP 145 261 261 TRP TRP B . n 
B 2 146 ILE 146 262 262 ILE ILE B . n 
B 2 147 LYS 147 263 263 LYS LYS B . n 
B 2 148 THR 148 264 264 THR THR B . n 
B 2 149 ASN 149 265 265 ASN ASN B . n 
B 2 150 LYS 150 266 266 LYS LYS B . n 
B 2 151 ASN 151 267 267 ASN ASN B . n 
B 2 152 ASN 152 268 268 ASN ASN B . n 
B 2 153 PRO 153 269 269 PRO PRO B . n 
B 2 154 GLY 154 270 270 GLY GLY B . n 
B 2 155 LYS 155 271 271 LYS LYS B . n 
B 2 156 THR 156 272 272 THR THR B . n 
B 2 157 LYS 157 273 273 LYS LYS B . n 
B 2 158 THR 158 274 274 THR THR B . n 
B 2 159 LEU 159 275 275 LEU LEU B . n 
B 2 160 ASP 160 276 276 ASP ASP B . n 
B 2 161 PRO 161 277 277 PRO PRO B . n 
B 2 162 LYS 162 278 278 LYS LYS B . n 
B 2 163 ALA 163 279 279 ALA ALA B . n 
B 2 164 VAL 164 280 280 VAL VAL B . n 
B 2 165 PHE 165 281 281 PHE PHE B . n 
B 2 166 GLN 166 282 282 GLN GLN B . n 
B 2 167 ARG 167 283 283 ARG ARG B . n 
B 2 168 THR 168 284 284 THR THR B . n 
B 2 169 LYS 169 285 285 LYS LYS B . n 
B 2 170 GLU 170 286 286 GLU GLU B . n 
B 2 171 HIS 171 287 287 HIS HIS B . n 
B 2 172 CYS 172 288 288 CYS CYS B . n 
B 2 173 LEU 173 289 289 LEU LEU B . n 
B 2 174 MET 174 290 290 MET MET B . n 
B 2 175 GLY 175 291 291 GLY GLY B . n 
B 2 176 ILE 176 292 292 ILE ILE B . n 
B 2 177 LYS 177 293 293 LYS LYS B . n 
B 2 178 GLY 178 294 294 GLY GLY B . n 
B 2 179 THR 179 295 295 THR THR B . n 
B 2 180 VAL 180 296 296 VAL VAL B . n 
B 2 181 LYS 181 297 ?   ?   ?   B . n 
B 2 182 ARG 182 298 ?   ?   ?   B . n 
B 2 183 SER 183 299 ?   ?   ?   B . n 
B 2 184 THR 184 300 ?   ?   ?   B . n 
B 2 185 ASP 185 301 ?   ?   ?   B . n 
B 2 186 GLY 186 302 ?   ?   ?   B . n 
B 2 187 ASP 187 303 ?   ?   ?   B . n 
B 2 188 PHE 188 304 ?   ?   ?   B . n 
B 2 189 ILE 189 305 305 ILE ILE B . n 
B 2 190 HIS 190 306 306 HIS HIS B . n 
B 2 191 ALA 191 307 307 ALA ALA B . n 
B 2 192 ASN 192 308 308 ASN ASN B . n 
B 2 193 VAL 193 309 309 VAL VAL B . n 
B 2 194 ASP 194 310 310 ASP ASP B . n 
B 2 195 ILE 195 311 311 ILE ILE B . n 
B 2 196 ASP 196 312 312 ASP ASP B . n 
B 2 197 LEU 197 313 313 LEU LEU B . n 
B 2 198 ILE 198 314 314 ILE ILE B . n 
B 2 199 ILE 199 315 315 ILE ILE B . n 
B 2 200 THR 200 316 316 THR THR B . n 
B 2 201 GLU 201 317 317 GLU GLU B . n 
B 2 202 GLU 202 318 318 GLU GLU B . n 
B 2 203 PRO 203 319 319 PRO PRO B . n 
B 2 204 GLU 204 320 320 GLU GLU B . n 
B 2 205 ILE 205 321 321 ILE ILE B . n 
B 2 206 GLY 206 322 322 GLY GLY B . n 
B 2 207 ASN 207 323 323 ASN ASN B . n 
B 2 208 ILE 208 324 324 ILE ILE B . n 
B 2 209 GLU 209 325 325 GLU GLU B . n 
B 2 210 LYS 210 326 326 LYS LYS B . n 
B 2 211 PRO 211 327 327 PRO PRO B . n 
B 2 212 VAL 212 328 328 VAL VAL B . n 
B 2 213 GLU 213 329 329 GLU GLU B . n 
B 2 214 ILE 214 330 330 ILE ILE B . n 
B 2 215 PHE 215 331 331 PHE PHE B . n 
B 2 216 HIS 216 332 332 HIS HIS B . n 
B 2 217 ILE 217 333 333 ILE ILE B . n 
B 2 218 ILE 218 334 334 ILE ILE B . n 
B 2 219 GLU 219 335 335 GLU GLU B . n 
B 2 220 HIS 220 336 336 HIS HIS B . n 
B 2 221 PHE 221 337 337 PHE PHE B . n 
B 2 222 CYS 222 338 338 CYS CYS B . n 
B 2 223 LEU 223 339 339 LEU LEU B . n 
B 2 224 GLY 224 340 340 GLY GLY B . n 
B 2 225 ARG 225 341 341 ARG ARG B . n 
B 2 226 ARG 226 342 342 ARG ARG B . n 
B 2 227 ARG 227 343 343 ARG ARG B . n 
B 2 228 LEU 228 344 344 LEU LEU B . n 
B 2 229 HIS 229 345 345 HIS HIS B . n 
B 2 230 LEU 230 346 346 LEU LEU B . n 
B 2 231 PHE 231 347 347 PHE PHE B . n 
B 2 232 GLY 232 348 348 GLY GLY B . n 
B 2 233 ARG 233 349 349 ARG ARG B . n 
B 2 234 ASP 234 350 350 ASP ASP B . n 
B 2 235 SER 235 351 351 SER SER B . n 
B 2 236 THR 236 352 352 THR THR B . n 
B 2 237 ILE 237 353 353 ILE ILE B . n 
B 2 238 ARG 238 354 354 ARG ARG B . n 
B 2 239 PRO 239 355 355 PRO PRO B . n 
B 2 240 GLY 240 356 356 GLY GLY B . n 
B 2 241 TRP 241 357 357 TRP TRP B . n 
B 2 242 LEU 242 358 358 LEU LEU B . n 
B 2 243 THR 243 359 359 THR THR B . n 
B 2 244 VAL 244 360 360 VAL VAL B . n 
B 2 245 GLY 245 361 361 GLY GLY B . n 
B 2 246 PRO 246 362 362 PRO PRO B . n 
B 2 247 THR 247 363 363 THR THR B . n 
B 2 248 LEU 248 364 364 LEU LEU B . n 
B 2 249 THR 249 365 365 THR THR B . n 
B 2 250 ASN 250 366 366 ASN ASN B . n 
B 2 251 SER 251 367 367 SER SER B . n 
B 2 252 ASN 252 368 368 ASN ASN B . n 
B 2 253 TYR 253 369 369 TYR TYR B . n 
B 2 254 ASN 254 370 370 ASN ASN B . n 
B 2 255 ALA 255 371 371 ALA ALA B . n 
B 2 256 GLU 256 372 372 GLU GLU B . n 
B 2 257 THR 257 373 373 THR THR B . n 
B 2 258 TYR 258 374 374 TYR TYR B . n 
B 2 259 ALA 259 375 375 ALA ALA B . n 
B 2 260 SER 260 376 376 SER SER B . n 
B 2 261 TYR 261 377 377 TYR TYR B . n 
B 2 262 PHE 262 378 378 PHE PHE B . n 
B 2 263 SER 263 379 379 SER SER B . n 
B 2 264 ALA 264 380 380 ALA ALA B . n 
B 2 265 PRO 265 381 381 PRO PRO B . n 
B 2 266 ASN 266 382 382 ASN ASN B . n 
B 2 267 SER 267 383 383 SER SER B . n 
B 2 268 TYR 268 384 384 TYR TYR B . n 
B 2 269 LEU 269 385 385 LEU LEU B . n 
B 2 270 THR 270 386 386 THR THR B . n 
B 2 271 GLY 271 387 387 GLY GLY B . n 
B 2 272 CYS 272 388 388 CYS CYS B . n 
B 2 273 THR 273 389 389 THR THR B . n 
B 2 274 GLU 274 390 390 GLU GLU B . n 
B 2 275 GLU 275 391 391 GLU GLU B . n 
B 2 276 ILE 276 392 392 ILE ILE B . n 
B 2 277 GLU 277 393 393 GLU GLU B . n 
B 2 278 ARG 278 394 394 ARG ARG B . n 
B 2 279 LEU 279 395 395 LEU LEU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IIM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IIM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1IIM 1   601 600 A1IIM 241 A . 
D 4 CA    1   602 630 CA    CA  A . 
E 4 CA    1   401 610 CA    CA  B . 
F 4 CA    1   402 620 CA    CA  B . 
G 5 HOH   1   701 290 HOH   HOH A . 
G 5 HOH   2   702 317 HOH   HOH A . 
G 5 HOH   3   703 271 HOH   HOH A . 
G 5 HOH   4   704 78  HOH   HOH A . 
G 5 HOH   5   705 227 HOH   HOH A . 
G 5 HOH   6   706 146 HOH   HOH A . 
G 5 HOH   7   707 292 HOH   HOH A . 
G 5 HOH   8   708 98  HOH   HOH A . 
G 5 HOH   9   709 201 HOH   HOH A . 
G 5 HOH   10  710 179 HOH   HOH A . 
G 5 HOH   11  711 282 HOH   HOH A . 
G 5 HOH   12  712 20  HOH   HOH A . 
G 5 HOH   13  713 109 HOH   HOH A . 
G 5 HOH   14  714 116 HOH   HOH A . 
G 5 HOH   15  715 102 HOH   HOH A . 
G 5 HOH   16  716 66  HOH   HOH A . 
G 5 HOH   17  717 34  HOH   HOH A . 
G 5 HOH   18  718 280 HOH   HOH A . 
G 5 HOH   19  719 32  HOH   HOH A . 
G 5 HOH   20  720 49  HOH   HOH A . 
G 5 HOH   21  721 164 HOH   HOH A . 
G 5 HOH   22  722 221 HOH   HOH A . 
G 5 HOH   23  723 163 HOH   HOH A . 
G 5 HOH   24  724 21  HOH   HOH A . 
G 5 HOH   25  725 197 HOH   HOH A . 
G 5 HOH   26  726 43  HOH   HOH A . 
G 5 HOH   27  727 112 HOH   HOH A . 
G 5 HOH   28  728 45  HOH   HOH A . 
G 5 HOH   29  729 48  HOH   HOH A . 
G 5 HOH   30  730 114 HOH   HOH A . 
G 5 HOH   31  731 132 HOH   HOH A . 
G 5 HOH   32  732 94  HOH   HOH A . 
G 5 HOH   33  733 288 HOH   HOH A . 
G 5 HOH   34  734 55  HOH   HOH A . 
G 5 HOH   35  735 224 HOH   HOH A . 
G 5 HOH   36  736 277 HOH   HOH A . 
G 5 HOH   37  737 61  HOH   HOH A . 
G 5 HOH   38  738 256 HOH   HOH A . 
G 5 HOH   39  739 81  HOH   HOH A . 
G 5 HOH   40  740 100 HOH   HOH A . 
G 5 HOH   41  741 22  HOH   HOH A . 
G 5 HOH   42  742 142 HOH   HOH A . 
G 5 HOH   43  743 185 HOH   HOH A . 
G 5 HOH   44  744 5   HOH   HOH A . 
G 5 HOH   45  745 111 HOH   HOH A . 
G 5 HOH   46  746 113 HOH   HOH A . 
G 5 HOH   47  747 265 HOH   HOH A . 
G 5 HOH   48  748 16  HOH   HOH A . 
G 5 HOH   49  749 72  HOH   HOH A . 
G 5 HOH   50  750 223 HOH   HOH A . 
G 5 HOH   51  751 190 HOH   HOH A . 
G 5 HOH   52  752 181 HOH   HOH A . 
G 5 HOH   53  753 176 HOH   HOH A . 
G 5 HOH   54  754 130 HOH   HOH A . 
G 5 HOH   55  755 172 HOH   HOH A . 
G 5 HOH   56  756 189 HOH   HOH A . 
G 5 HOH   57  757 17  HOH   HOH A . 
G 5 HOH   58  758 213 HOH   HOH A . 
G 5 HOH   59  759 178 HOH   HOH A . 
G 5 HOH   60  760 35  HOH   HOH A . 
G 5 HOH   61  761 134 HOH   HOH A . 
G 5 HOH   62  762 169 HOH   HOH A . 
G 5 HOH   63  763 80  HOH   HOH A . 
G 5 HOH   64  764 127 HOH   HOH A . 
G 5 HOH   65  765 284 HOH   HOH A . 
G 5 HOH   66  766 28  HOH   HOH A . 
G 5 HOH   67  767 118 HOH   HOH A . 
G 5 HOH   68  768 167 HOH   HOH A . 
G 5 HOH   69  769 124 HOH   HOH A . 
G 5 HOH   70  770 320 HOH   HOH A . 
G 5 HOH   71  771 40  HOH   HOH A . 
G 5 HOH   72  772 247 HOH   HOH A . 
G 5 HOH   73  773 82  HOH   HOH A . 
G 5 HOH   74  774 153 HOH   HOH A . 
G 5 HOH   75  775 136 HOH   HOH A . 
G 5 HOH   76  776 77  HOH   HOH A . 
G 5 HOH   77  777 264 HOH   HOH A . 
G 5 HOH   78  778 145 HOH   HOH A . 
G 5 HOH   79  779 215 HOH   HOH A . 
G 5 HOH   80  780 50  HOH   HOH A . 
G 5 HOH   81  781 148 HOH   HOH A . 
G 5 HOH   82  782 245 HOH   HOH A . 
G 5 HOH   83  783 90  HOH   HOH A . 
G 5 HOH   84  784 168 HOH   HOH A . 
G 5 HOH   85  785 41  HOH   HOH A . 
G 5 HOH   86  786 165 HOH   HOH A . 
G 5 HOH   87  787 75  HOH   HOH A . 
G 5 HOH   88  788 3   HOH   HOH A . 
G 5 HOH   89  789 240 HOH   HOH A . 
G 5 HOH   90  790 96  HOH   HOH A . 
G 5 HOH   91  791 272 HOH   HOH A . 
G 5 HOH   92  792 9   HOH   HOH A . 
G 5 HOH   93  793 217 HOH   HOH A . 
G 5 HOH   94  794 26  HOH   HOH A . 
G 5 HOH   95  795 128 HOH   HOH A . 
G 5 HOH   96  796 202 HOH   HOH A . 
G 5 HOH   97  797 62  HOH   HOH A . 
G 5 HOH   98  798 319 HOH   HOH A . 
G 5 HOH   99  799 188 HOH   HOH A . 
G 5 HOH   100 800 149 HOH   HOH A . 
G 5 HOH   101 801 69  HOH   HOH A . 
G 5 HOH   102 802 108 HOH   HOH A . 
G 5 HOH   103 803 209 HOH   HOH A . 
G 5 HOH   104 804 63  HOH   HOH A . 
G 5 HOH   105 805 91  HOH   HOH A . 
G 5 HOH   106 806 27  HOH   HOH A . 
G 5 HOH   107 807 39  HOH   HOH A . 
G 5 HOH   108 808 141 HOH   HOH A . 
G 5 HOH   109 809 131 HOH   HOH A . 
G 5 HOH   110 810 107 HOH   HOH A . 
G 5 HOH   111 811 192 HOH   HOH A . 
G 5 HOH   112 812 2   HOH   HOH A . 
G 5 HOH   113 813 218 HOH   HOH A . 
G 5 HOH   114 814 270 HOH   HOH A . 
G 5 HOH   115 815 150 HOH   HOH A . 
G 5 HOH   116 816 196 HOH   HOH A . 
G 5 HOH   117 817 138 HOH   HOH A . 
G 5 HOH   118 818 263 HOH   HOH A . 
G 5 HOH   119 819 293 HOH   HOH A . 
G 5 HOH   120 820 243 HOH   HOH A . 
G 5 HOH   121 821 274 HOH   HOH A . 
G 5 HOH   122 822 159 HOH   HOH A . 
G 5 HOH   123 823 249 HOH   HOH A . 
G 5 HOH   124 824 95  HOH   HOH A . 
G 5 HOH   125 825 285 HOH   HOH A . 
G 5 HOH   126 826 253 HOH   HOH A . 
G 5 HOH   127 827 289 HOH   HOH A . 
G 5 HOH   128 828 273 HOH   HOH A . 
G 5 HOH   129 829 250 HOH   HOH A . 
G 5 HOH   130 830 278 HOH   HOH A . 
G 5 HOH   131 831 276 HOH   HOH A . 
G 5 HOH   132 832 156 HOH   HOH A . 
G 5 HOH   133 833 323 HOH   HOH A . 
G 5 HOH   134 834 283 HOH   HOH A . 
G 5 HOH   135 835 318 HOH   HOH A . 
G 5 HOH   136 836 286 HOH   HOH A . 
G 5 HOH   137 837 325 HOH   HOH A . 
G 5 HOH   138 838 177 HOH   HOH A . 
G 5 HOH   139 839 294 HOH   HOH A . 
G 5 HOH   140 840 184 HOH   HOH A . 
G 5 HOH   141 841 326 HOH   HOH A . 
G 5 HOH   142 842 312 HOH   HOH A . 
G 5 HOH   143 843 231 HOH   HOH A . 
G 5 HOH   144 844 275 HOH   HOH A . 
G 5 HOH   145 845 291 HOH   HOH A . 
H 5 HOH   1   501 314 HOH   HOH B . 
H 5 HOH   2   502 302 HOH   HOH B . 
H 5 HOH   3   503 241 HOH   HOH B . 
H 5 HOH   4   504 161 HOH   HOH B . 
H 5 HOH   5   505 266 HOH   HOH B . 
H 5 HOH   6   506 295 HOH   HOH B . 
H 5 HOH   7   507 226 HOH   HOH B . 
H 5 HOH   8   508 310 HOH   HOH B . 
H 5 HOH   9   509 162 HOH   HOH B . 
H 5 HOH   10  510 230 HOH   HOH B . 
H 5 HOH   11  511 238 HOH   HOH B . 
H 5 HOH   12  512 309 HOH   HOH B . 
H 5 HOH   13  513 203 HOH   HOH B . 
H 5 HOH   14  514 64  HOH   HOH B . 
H 5 HOH   15  515 73  HOH   HOH B . 
H 5 HOH   16  516 25  HOH   HOH B . 
H 5 HOH   17  517 175 HOH   HOH B . 
H 5 HOH   18  518 144 HOH   HOH B . 
H 5 HOH   19  519 53  HOH   HOH B . 
H 5 HOH   20  520 135 HOH   HOH B . 
H 5 HOH   21  521 92  HOH   HOH B . 
H 5 HOH   22  522 65  HOH   HOH B . 
H 5 HOH   23  523 29  HOH   HOH B . 
H 5 HOH   24  524 267 HOH   HOH B . 
H 5 HOH   25  525 236 HOH   HOH B . 
H 5 HOH   26  526 47  HOH   HOH B . 
H 5 HOH   27  527 122 HOH   HOH B . 
H 5 HOH   28  528 237 HOH   HOH B . 
H 5 HOH   29  529 166 HOH   HOH B . 
H 5 HOH   30  530 194 HOH   HOH B . 
H 5 HOH   31  531 4   HOH   HOH B . 
H 5 HOH   32  532 173 HOH   HOH B . 
H 5 HOH   33  533 235 HOH   HOH B . 
H 5 HOH   34  534 31  HOH   HOH B . 
H 5 HOH   35  535 191 HOH   HOH B . 
H 5 HOH   36  536 198 HOH   HOH B . 
H 5 HOH   37  537 258 HOH   HOH B . 
H 5 HOH   38  538 74  HOH   HOH B . 
H 5 HOH   39  539 38  HOH   HOH B . 
H 5 HOH   40  540 157 HOH   HOH B . 
H 5 HOH   41  541 125 HOH   HOH B . 
H 5 HOH   42  542 211 HOH   HOH B . 
H 5 HOH   43  543 242 HOH   HOH B . 
H 5 HOH   44  544 97  HOH   HOH B . 
H 5 HOH   45  545 89  HOH   HOH B . 
H 5 HOH   46  546 183 HOH   HOH B . 
H 5 HOH   47  547 222 HOH   HOH B . 
H 5 HOH   48  548 99  HOH   HOH B . 
H 5 HOH   49  549 8   HOH   HOH B . 
H 5 HOH   50  550 101 HOH   HOH B . 
H 5 HOH   51  551 244 HOH   HOH B . 
H 5 HOH   52  552 208 HOH   HOH B . 
H 5 HOH   53  553 139 HOH   HOH B . 
H 5 HOH   54  554 19  HOH   HOH B . 
H 5 HOH   55  555 59  HOH   HOH B . 
H 5 HOH   56  556 37  HOH   HOH B . 
H 5 HOH   57  557 42  HOH   HOH B . 
H 5 HOH   58  558 70  HOH   HOH B . 
H 5 HOH   59  559 117 HOH   HOH B . 
H 5 HOH   60  560 210 HOH   HOH B . 
H 5 HOH   61  561 171 HOH   HOH B . 
H 5 HOH   62  562 257 HOH   HOH B . 
H 5 HOH   63  563 305 HOH   HOH B . 
H 5 HOH   64  564 160 HOH   HOH B . 
H 5 HOH   65  565 214 HOH   HOH B . 
H 5 HOH   66  566 260 HOH   HOH B . 
H 5 HOH   67  567 313 HOH   HOH B . 
H 5 HOH   68  568 44  HOH   HOH B . 
H 5 HOH   69  569 12  HOH   HOH B . 
H 5 HOH   70  570 52  HOH   HOH B . 
H 5 HOH   71  571 232 HOH   HOH B . 
H 5 HOH   72  572 6   HOH   HOH B . 
H 5 HOH   73  573 140 HOH   HOH B . 
H 5 HOH   74  574 233 HOH   HOH B . 
H 5 HOH   75  575 13  HOH   HOH B . 
H 5 HOH   76  576 228 HOH   HOH B . 
H 5 HOH   77  577 259 HOH   HOH B . 
H 5 HOH   78  578 170 HOH   HOH B . 
H 5 HOH   79  579 308 HOH   HOH B . 
H 5 HOH   80  580 207 HOH   HOH B . 
H 5 HOH   81  581 18  HOH   HOH B . 
H 5 HOH   82  582 1   HOH   HOH B . 
H 5 HOH   83  583 71  HOH   HOH B . 
H 5 HOH   84  584 321 HOH   HOH B . 
H 5 HOH   85  585 85  HOH   HOH B . 
H 5 HOH   86  586 269 HOH   HOH B . 
H 5 HOH   87  587 86  HOH   HOH B . 
H 5 HOH   88  588 195 HOH   HOH B . 
H 5 HOH   89  589 23  HOH   HOH B . 
H 5 HOH   90  590 200 HOH   HOH B . 
H 5 HOH   91  591 174 HOH   HOH B . 
H 5 HOH   92  592 316 HOH   HOH B . 
H 5 HOH   93  593 10  HOH   HOH B . 
H 5 HOH   94  594 7   HOH   HOH B . 
H 5 HOH   95  595 315 HOH   HOH B . 
H 5 HOH   96  596 322 HOH   HOH B . 
H 5 HOH   97  597 30  HOH   HOH B . 
H 5 HOH   98  598 51  HOH   HOH B . 
H 5 HOH   99  599 36  HOH   HOH B . 
H 5 HOH   100 600 15  HOH   HOH B . 
H 5 HOH   101 601 151 HOH   HOH B . 
H 5 HOH   102 602 46  HOH   HOH B . 
H 5 HOH   103 603 83  HOH   HOH B . 
H 5 HOH   104 604 68  HOH   HOH B . 
H 5 HOH   105 605 105 HOH   HOH B . 
H 5 HOH   106 606 106 HOH   HOH B . 
H 5 HOH   107 607 137 HOH   HOH B . 
H 5 HOH   108 608 225 HOH   HOH B . 
H 5 HOH   109 609 133 HOH   HOH B . 
H 5 HOH   110 610 206 HOH   HOH B . 
H 5 HOH   111 611 57  HOH   HOH B . 
H 5 HOH   112 612 239 HOH   HOH B . 
H 5 HOH   113 613 11  HOH   HOH B . 
H 5 HOH   114 614 147 HOH   HOH B . 
H 5 HOH   115 615 219 HOH   HOH B . 
H 5 HOH   116 616 187 HOH   HOH B . 
H 5 HOH   117 617 104 HOH   HOH B . 
H 5 HOH   118 618 311 HOH   HOH B . 
H 5 HOH   119 619 261 HOH   HOH B . 
H 5 HOH   120 620 126 HOH   HOH B . 
H 5 HOH   121 621 193 HOH   HOH B . 
H 5 HOH   122 622 58  HOH   HOH B . 
H 5 HOH   123 623 121 HOH   HOH B . 
H 5 HOH   124 624 155 HOH   HOH B . 
H 5 HOH   125 625 182 HOH   HOH B . 
H 5 HOH   126 626 129 HOH   HOH B . 
H 5 HOH   127 627 56  HOH   HOH B . 
H 5 HOH   128 628 115 HOH   HOH B . 
H 5 HOH   129 629 54  HOH   HOH B . 
H 5 HOH   130 630 60  HOH   HOH B . 
H 5 HOH   131 631 24  HOH   HOH B . 
H 5 HOH   132 632 67  HOH   HOH B . 
H 5 HOH   133 633 87  HOH   HOH B . 
H 5 HOH   134 634 120 HOH   HOH B . 
H 5 HOH   135 635 152 HOH   HOH B . 
H 5 HOH   136 636 186 HOH   HOH B . 
H 5 HOH   137 637 279 HOH   HOH B . 
H 5 HOH   138 638 84  HOH   HOH B . 
H 5 HOH   139 639 88  HOH   HOH B . 
H 5 HOH   140 640 103 HOH   HOH B . 
H 5 HOH   141 641 251 HOH   HOH B . 
H 5 HOH   142 642 296 HOH   HOH B . 
H 5 HOH   143 643 262 HOH   HOH B . 
H 5 HOH   144 644 93  HOH   HOH B . 
H 5 HOH   145 645 154 HOH   HOH B . 
H 5 HOH   146 646 14  HOH   HOH B . 
H 5 HOH   147 647 76  HOH   HOH B . 
H 5 HOH   148 648 33  HOH   HOH B . 
H 5 HOH   149 649 303 HOH   HOH B . 
H 5 HOH   150 650 324 HOH   HOH B . 
H 5 HOH   151 651 300 HOH   HOH B . 
H 5 HOH   152 652 229 HOH   HOH B . 
H 5 HOH   153 653 79  HOH   HOH B . 
H 5 HOH   154 654 297 HOH   HOH B . 
H 5 HOH   155 655 143 HOH   HOH B . 
H 5 HOH   156 656 220 HOH   HOH B . 
H 5 HOH   157 657 246 HOH   HOH B . 
H 5 HOH   158 658 255 HOH   HOH B . 
H 5 HOH   159 659 304 HOH   HOH B . 
H 5 HOH   160 660 301 HOH   HOH B . 
H 5 HOH   161 661 216 HOH   HOH B . 
H 5 HOH   162 662 119 HOH   HOH B . 
H 5 HOH   163 663 205 HOH   HOH B . 
H 5 HOH   164 664 212 HOH   HOH B . 
H 5 HOH   165 665 204 HOH   HOH B . 
H 5 HOH   166 666 110 HOH   HOH B . 
H 5 HOH   167 667 123 HOH   HOH B . 
H 5 HOH   168 668 158 HOH   HOH B . 
H 5 HOH   169 669 234 HOH   HOH B . 
H 5 HOH   170 670 287 HOH   HOH B . 
H 5 HOH   171 671 299 HOH   HOH B . 
H 5 HOH   172 672 268 HOH   HOH B . 
H 5 HOH   173 673 281 HOH   HOH B . 
H 5 HOH   174 674 307 HOH   HOH B . 
H 5 HOH   175 675 306 HOH   HOH B . 
H 5 HOH   176 676 199 HOH   HOH B . 
H 5 HOH   177 677 252 HOH   HOH B . 
H 5 HOH   178 678 180 HOH   HOH B . 
H 5 HOH   179 679 254 HOH   HOH B . 
H 5 HOH   180 680 298 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G4W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.295 
_cell.length_a_esd                 ? 
_cell.length_b                     64.295 
_cell.length_b_esd                 ? 
_cell.length_c                     226.790 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9G4W 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G4W 
_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             2.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.77 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M calcium chloride, 0.1 M Tris:HCl pH 8.0, 18% (w/v) PEG 4000, 20C, sitting
drop, protein:precipitant solution ratio = 1:1
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.978565 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978565 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G4W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               44.87 
_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                                     45188 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                16.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.85 
_reflns_shell.d_res_low                                     1.89 
_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                             3458 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.97 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.02 
_refine.aniso_B[1][2]                            -0.01 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.02 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.06 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.778 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9G4W 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             44.87 
_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                     45188 
_refine.ls_number_reflns_R_free                  2290 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.70 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18607 
_refine.ls_R_factor_R_free                       0.22633 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18400 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.134 
_refine.pdbx_overall_ESU_R_Free                  0.130 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.714 
_refine.overall_SU_ML                            0.107 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        44.87 
_refine_hist.number_atoms_solvent             326 
_refine_hist.number_atoms_total               4174 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3809 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.013  3989 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  3761 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.597  1.648  5419 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.291  1.583  8667 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.582  5.000  472  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.532 21.325 234  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.075 15.000 685  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.149 15.000 36   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.200  508  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  4470 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  948  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.732  4.021  1882 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.732  4.018  1881 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.606  5.984  2350 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.605  5.988  2351 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.887  4.432  2107 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.879  4.432  2107 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.962  6.489  3064 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.733  46.140 4527 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.743  45.870 4473 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.850 
_refine_ls_shell.d_res_low                        1.898 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             162 
_refine_ls_shell.number_reflns_R_work             3296 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.324 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.369 
# 
_struct.entry_id                     9G4W 
_struct.title                        
'Crystal structure of the human METTL3-METTL14 in complex with small molecule inhibitor Compound 59' 
_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        9G4W 
_struct_keywords.text            'METTL3 METTL14 inhibitor Epics, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
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 MTA70_HUMAN Q86U44 ? 1 
;ADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECL
NLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERL
SPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKP
;
365 
2 UNP MET14_HUMAN Q9HCE5 ? 2 
;NDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLE
EYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLD
PKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPG
WLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERL
;
117 
# 
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 9G4W A 1 ? 213 ? Q86U44 365 ? 577 ? 365 577 
2 2 9G4W B 1 ? 279 ? Q9HCE5 117 ? 395 ? 117 395 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4520  ? 
1 MORE         -45   ? 
1 'SSA (A^2)'  21450 ? 
# 
_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_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 18  ? GLY A 23  ? ASP A 382 GLY A 387 5 ? 6  
HELX_P HELX_P2  AA2 THR A 46  ? LEU A 53  ? THR A 410 LEU A 417 1 ? 8  
HELX_P HELX_P3  AA3 ASN A 54  ? GLN A 59  ? ASN A 418 GLN A 423 5 ? 6  
HELX_P HELX_P4  AA4 ARG A 71  ? TRP A 83  ? ARG A 435 TRP A 447 1 ? 13 
HELX_P HELX_P5  AA5 ASP A 151 ? SER A 161 ? ASP A 515 SER A 525 1 ? 11 
HELX_P HELX_P6  AA6 ARG A 172 ? VAL A 176 ? ARG A 536 VAL A 540 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 194 ? TYR A 205 ? ASP A 558 TYR A 569 1 ? 12 
HELX_P HELX_P8  AA8 ASP B 2   ? GLY B 11  ? ASP B 118 GLY B 127 1 ? 10 
HELX_P HELX_P9  AA9 ARG B 13  ? ILE B 18  ? ARG B 129 ILE B 134 5 ? 6  
HELX_P HELX_P10 AB1 ARG B 34  ? ASN B 48  ? ARG B 150 ASN B 164 1 ? 15 
HELX_P HELX_P11 AB2 ASP B 62  ? LEU B 66  ? ASP B 178 LEU B 182 5 ? 5  
HELX_P HELX_P12 AB3 LEU B 79  ? TYR B 83  ? LEU B 195 TYR B 199 5 ? 5  
HELX_P HELX_P13 AB4 THR B 96  ? LYS B 102 ? THR B 212 LYS B 218 1 ? 7  
HELX_P HELX_P14 AB5 GLU B 104 ? GLU B 107 ? GLU B 220 GLU B 223 5 ? 4  
HELX_P HELX_P15 AB6 GLU B 123 ? TRP B 135 ? GLU B 239 TRP B 251 1 ? 13 
HELX_P HELX_P16 AB7 VAL B 212 ? PHE B 221 ? VAL B 328 PHE B 337 1 ? 10 
HELX_P HELX_P17 AB8 ARG B 233 ? ILE B 237 ? ARG B 349 ILE B 353 5 ? 5  
HELX_P HELX_P18 AB9 ASN B 254 ? TYR B 261 ? ASN B 370 TYR B 377 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? B CYS 222 SG ? ? ? 1_555 B CYS 272 SG ? ? B CYS 338 B CYS 388 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc1 metalc ? ? A PHE 130 O  ? ? ? 1_555 D CA  .   CA ? ? A PHE 494 A CA  602 1_555 ? ? ? ? ? ? ? 2.580 ? ? 
metalc2 metalc ? ? F CA  .   CA ? ? ? 1_555 H HOH .   O  ? ? B CA  402 B HOH 614 1_555 ? ? ? ? ? ? ? 3.086 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       222 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      272 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        338 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       388 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
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 THR 67  B . ? THR 183 B PRO 68  B ? PRO 184 B 1 -4.88 
2 ALA 264 B . ? ALA 380 B PRO 265 B ? PRO 381 B 1 3.65  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 138 ? GLU A 142 ? VAL A 502 GLU A 506 
AA1 2 GLU A 86  ? THR A 96  ? GLU A 450 THR A 460 
AA1 3 LYS A 116 ? LYS A 124 ? LYS A 480 LYS A 488 
AA1 4 GLY A 62  ? VAL A 68  ? GLY A 426 VAL A 432 
AA1 5 VAL A 27  ? ALA A 30  ? VAL A 391 ALA A 394 
AA1 6 LYS A 166 ? LEU A 169 ? LYS A 530 LEU A 533 
AA1 7 TRP A 180 ? GLY A 184 ? TRP A 544 GLY A 548 
AA1 8 GLN A 8   ? CYS A 11  ? GLN A 372 CYS A 375 
AA1 9 ILE A 190 ? HIS A 191 ? ILE A 554 HIS A 555 
AA2 1 MET B 52  ? GLN B 55  ? MET B 168 GLN B 171 
AA2 2 LEU B 242 ? GLY B 245 ? LEU B 358 GLY B 361 
AA2 3 ARG B 227 ? LEU B 230 ? ARG B 343 LEU B 346 
AA2 4 PHE B 70  ? LEU B 75  ? PHE B 186 LEU B 191 
AA2 5 ALA B 109 ? GLY B 120 ? ALA B 225 GLY B 236 
AA2 6 LYS B 169 ? LYS B 177 ? LYS B 285 LYS B 293 
AA2 7 ARG B 138 ? THR B 148 ? ARG B 254 THR B 264 
AA2 8 LEU B 197 ? GLU B 201 ? LEU B 313 GLU B 317 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 139 ? O ILE A 503 N VAL A 94  ? N VAL A 458 
AA1 2 3 N VAL A 88  ? N VAL A 452 O VAL A 121 ? O VAL A 485 
AA1 3 4 O GLY A 122 ? O GLY A 486 N LEU A 64  ? N LEU A 428 
AA1 4 5 O PHE A 65  ? O PHE A 429 N VAL A 28  ? N VAL A 392 
AA1 5 6 N MET A 29  ? N MET A 393 O LEU A 169 ? O LEU A 533 
AA1 6 7 N GLU A 168 ? N GLU A 532 O LEU A 183 ? O LEU A 547 
AA1 7 8 O THR A 182 ? O THR A 546 N ILE A 10  ? N ILE A 374 
AA1 8 9 N TRP A 9   ? N TRP A 373 O HIS A 191 ? O HIS A 555 
AA2 1 2 N LEU B 54  ? N LEU B 170 O THR B 243 ? O THR B 359 
AA2 2 3 O LEU B 242 ? O LEU B 358 N HIS B 229 ? N HIS B 345 
AA2 3 4 O LEU B 228 ? O LEU B 344 N LEU B 74  ? N LEU B 190 
AA2 4 5 N LEU B 75  ? N LEU B 191 O PHE B 116 ? O PHE B 232 
AA2 5 6 N CYS B 119 ? N CYS B 235 O HIS B 171 ? O HIS B 287 
AA2 6 7 O GLU B 170 ? O GLU B 286 N TRP B 145 ? N TRP B 261 
AA2 7 8 N ILE B 146 ? N ILE B 262 O ILE B 198 ? O ILE B 314 
# 
_pdbx_entry_details.entry_id                   9G4W 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    382 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 399 ? ? -68.67  99.45   
2  1 PHE A 534 ? ? 75.19   34.43   
3  1 ASN A 543 ? ? 79.94   -6.70   
4  1 ILE A 574 ? ? -117.46 75.31   
5  1 ARG B 150 ? ? -147.09 34.45   
6  1 ARG B 200 ? ? -149.56 55.94   
7  1 GLU B 220 ? ? -93.67  54.73   
8  1 ASN B 268 ? ? -156.51 63.91   
9  1 HIS B 306 ? ? -164.56 66.53   
10 1 ALA B 307 ? ? -94.21  -123.89 
11 1 ASN B 308 ? ? -177.20 98.54   
12 1 ASP B 312 ? ? -87.72  32.64   
# 
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 B GLY 138 ? B GLY 22  
2  1 Y 1 B LEU 139 ? B LEU 23  
3  1 Y 1 B ALA 140 ? B ALA 24  
4  1 Y 1 B ASP 141 ? B ASP 25  
5  1 Y 1 B ARG 142 ? B ARG 26  
6  1 Y 1 B PHE 143 ? B PHE 27  
7  1 Y 1 B GLU 144 ? B GLU 28  
8  1 Y 1 B GLU 145 ? B GLU 29  
9  1 Y 1 B TYR 146 ? B TYR 30  
10 1 Y 1 B PRO 147 ? B PRO 31  
11 1 Y 1 B LYS 148 ? B LYS 32  
12 1 Y 1 B THR 202 ? B THR 86  
13 1 Y 1 B GLY 203 ? B GLY 87  
14 1 Y 1 B ILE 204 ? B ILE 88  
15 1 Y 1 B THR 205 ? B THR 89  
16 1 Y 1 B ALA 206 ? B ALA 90  
17 1 Y 1 B ASN 207 ? B ASN 91  
18 1 Y 1 B LYS 297 ? B LYS 181 
19 1 Y 1 B ARG 298 ? B ARG 182 
20 1 Y 1 B SER 299 ? B SER 183 
21 1 Y 1 B THR 300 ? B THR 184 
22 1 Y 1 B ASP 301 ? B ASP 185 
23 1 Y 1 B GLY 302 ? B GLY 186 
24 1 Y 1 B ASP 303 ? B ASP 187 
25 1 Y 1 B PHE 304 ? B PHE 188 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1IIM C1   C  N N 1   
A1IIM C2   C  N N 2   
A1IIM C3   C  N N 3   
A1IIM C4   C  N N 4   
A1IIM N1   N  N N 5   
A1IIM C5   C  Y N 6   
A1IIM C6   C  Y N 7   
A1IIM N2   N  Y N 8   
A1IIM C7   C  Y N 9   
A1IIM C8   C  Y N 10  
A1IIM N3   N  Y N 11  
A1IIM C9   C  Y N 12  
A1IIM C10  C  Y N 13  
A1IIM N4   N  Y N 14  
A1IIM N5   N  Y N 15  
A1IIM N6   N  Y N 16  
A1IIM C11  C  N R 17  
A1IIM C12  C  N N 18  
A1IIM N7   N  N N 19  
A1IIM C13  C  N N 20  
A1IIM C14  C  N N 21  
A1IIM C15  C  N N 22  
A1IIM C16  C  N N 23  
A1IIM C17  C  N N 24  
A1IIM O1   O  N N 25  
A1IIM N8   N  N N 26  
A1IIM C18  C  N N 27  
A1IIM C19  C  N N 28  
A1IIM C20  C  N N 29  
A1IIM C21  C  N R 30  
A1IIM C22  C  N N 31  
A1IIM N9   N  N N 32  
A1IIM C23  C  N N 33  
A1IIM C24  C  N N 34  
A1IIM C25  C  N N 35  
A1IIM C26  C  N N 36  
A1IIM H1   H  N N 37  
A1IIM H2   H  N N 38  
A1IIM H3   H  N N 39  
A1IIM H4   H  N N 40  
A1IIM H5   H  N N 41  
A1IIM H6   H  N N 42  
A1IIM H7   H  N N 43  
A1IIM H8   H  N N 44  
A1IIM H9   H  N N 45  
A1IIM H10  H  N N 46  
A1IIM H11  H  N N 47  
A1IIM H12  H  N N 48  
A1IIM H13  H  N N 49  
A1IIM H14  H  N N 50  
A1IIM H15  H  N N 51  
A1IIM H16  H  N N 52  
A1IIM H17  H  N N 53  
A1IIM H18  H  N N 54  
A1IIM H19  H  N N 55  
A1IIM H20  H  N N 56  
A1IIM H21  H  N N 57  
A1IIM H22  H  N N 58  
A1IIM H23  H  N N 59  
A1IIM H24  H  N N 60  
A1IIM H25  H  N N 61  
A1IIM H26  H  N N 62  
A1IIM H27  H  N N 63  
A1IIM H28  H  N N 64  
A1IIM H30  H  N N 65  
A1IIM H31  H  N N 66  
A1IIM H32  H  N N 67  
A1IIM H33  H  N N 68  
A1IIM H34  H  N N 69  
A1IIM H35  H  N N 70  
A1IIM H36  H  N N 71  
ALA   N    N  N N 72  
ALA   CA   C  N S 73  
ALA   C    C  N N 74  
ALA   O    O  N N 75  
ALA   CB   C  N N 76  
ALA   OXT  O  N N 77  
ALA   H    H  N N 78  
ALA   H2   H  N N 79  
ALA   HA   H  N N 80  
ALA   HB1  H  N N 81  
ALA   HB2  H  N N 82  
ALA   HB3  H  N N 83  
ALA   HXT  H  N N 84  
ARG   N    N  N N 85  
ARG   CA   C  N S 86  
ARG   C    C  N N 87  
ARG   O    O  N N 88  
ARG   CB   C  N N 89  
ARG   CG   C  N N 90  
ARG   CD   C  N N 91  
ARG   NE   N  N N 92  
ARG   CZ   C  N N 93  
ARG   NH1  N  N N 94  
ARG   NH2  N  N N 95  
ARG   OXT  O  N N 96  
ARG   H    H  N N 97  
ARG   H2   H  N N 98  
ARG   HA   H  N N 99  
ARG   HB2  H  N N 100 
ARG   HB3  H  N N 101 
ARG   HG2  H  N N 102 
ARG   HG3  H  N N 103 
ARG   HD2  H  N N 104 
ARG   HD3  H  N N 105 
ARG   HE   H  N N 106 
ARG   HH11 H  N N 107 
ARG   HH12 H  N N 108 
ARG   HH21 H  N N 109 
ARG   HH22 H  N N 110 
ARG   HXT  H  N N 111 
ASN   N    N  N N 112 
ASN   CA   C  N S 113 
ASN   C    C  N N 114 
ASN   O    O  N N 115 
ASN   CB   C  N N 116 
ASN   CG   C  N N 117 
ASN   OD1  O  N N 118 
ASN   ND2  N  N N 119 
ASN   OXT  O  N N 120 
ASN   H    H  N N 121 
ASN   H2   H  N N 122 
ASN   HA   H  N N 123 
ASN   HB2  H  N N 124 
ASN   HB3  H  N N 125 
ASN   HD21 H  N N 126 
ASN   HD22 H  N N 127 
ASN   HXT  H  N N 128 
ASP   N    N  N N 129 
ASP   CA   C  N S 130 
ASP   C    C  N N 131 
ASP   O    O  N N 132 
ASP   CB   C  N N 133 
ASP   CG   C  N N 134 
ASP   OD1  O  N N 135 
ASP   OD2  O  N N 136 
ASP   OXT  O  N N 137 
ASP   H    H  N N 138 
ASP   H2   H  N N 139 
ASP   HA   H  N N 140 
ASP   HB2  H  N N 141 
ASP   HB3  H  N N 142 
ASP   HD2  H  N N 143 
ASP   HXT  H  N N 144 
CA    CA   CA N N 145 
CYS   N    N  N N 146 
CYS   CA   C  N R 147 
CYS   C    C  N N 148 
CYS   O    O  N N 149 
CYS   CB   C  N N 150 
CYS   SG   S  N N 151 
CYS   OXT  O  N N 152 
CYS   H    H  N N 153 
CYS   H2   H  N N 154 
CYS   HA   H  N N 155 
CYS   HB2  H  N N 156 
CYS   HB3  H  N N 157 
CYS   HG   H  N N 158 
CYS   HXT  H  N N 159 
GLN   N    N  N N 160 
GLN   CA   C  N S 161 
GLN   C    C  N N 162 
GLN   O    O  N N 163 
GLN   CB   C  N N 164 
GLN   CG   C  N N 165 
GLN   CD   C  N N 166 
GLN   OE1  O  N N 167 
GLN   NE2  N  N N 168 
GLN   OXT  O  N N 169 
GLN   H    H  N N 170 
GLN   H2   H  N N 171 
GLN   HA   H  N N 172 
GLN   HB2  H  N N 173 
GLN   HB3  H  N N 174 
GLN   HG2  H  N N 175 
GLN   HG3  H  N N 176 
GLN   HE21 H  N N 177 
GLN   HE22 H  N N 178 
GLN   HXT  H  N N 179 
GLU   N    N  N N 180 
GLU   CA   C  N S 181 
GLU   C    C  N N 182 
GLU   O    O  N N 183 
GLU   CB   C  N N 184 
GLU   CG   C  N N 185 
GLU   CD   C  N N 186 
GLU   OE1  O  N N 187 
GLU   OE2  O  N N 188 
GLU   OXT  O  N N 189 
GLU   H    H  N N 190 
GLU   H2   H  N N 191 
GLU   HA   H  N N 192 
GLU   HB2  H  N N 193 
GLU   HB3  H  N N 194 
GLU   HG2  H  N N 195 
GLU   HG3  H  N N 196 
GLU   HE2  H  N N 197 
GLU   HXT  H  N N 198 
GLY   N    N  N N 199 
GLY   CA   C  N N 200 
GLY   C    C  N N 201 
GLY   O    O  N N 202 
GLY   OXT  O  N N 203 
GLY   H    H  N N 204 
GLY   H2   H  N N 205 
GLY   HA2  H  N N 206 
GLY   HA3  H  N N 207 
GLY   HXT  H  N N 208 
HIS   N    N  N N 209 
HIS   CA   C  N S 210 
HIS   C    C  N N 211 
HIS   O    O  N N 212 
HIS   CB   C  N N 213 
HIS   CG   C  Y N 214 
HIS   ND1  N  Y N 215 
HIS   CD2  C  Y N 216 
HIS   CE1  C  Y N 217 
HIS   NE2  N  Y N 218 
HIS   OXT  O  N N 219 
HIS   H    H  N N 220 
HIS   H2   H  N N 221 
HIS   HA   H  N N 222 
HIS   HB2  H  N N 223 
HIS   HB3  H  N N 224 
HIS   HD1  H  N N 225 
HIS   HD2  H  N N 226 
HIS   HE1  H  N N 227 
HIS   HE2  H  N N 228 
HIS   HXT  H  N N 229 
HOH   O    O  N N 230 
HOH   H1   H  N N 231 
HOH   H2   H  N N 232 
ILE   N    N  N N 233 
ILE   CA   C  N S 234 
ILE   C    C  N N 235 
ILE   O    O  N N 236 
ILE   CB   C  N S 237 
ILE   CG1  C  N N 238 
ILE   CG2  C  N N 239 
ILE   CD1  C  N N 240 
ILE   OXT  O  N N 241 
ILE   H    H  N N 242 
ILE   H2   H  N N 243 
ILE   HA   H  N N 244 
ILE   HB   H  N N 245 
ILE   HG12 H  N N 246 
ILE   HG13 H  N N 247 
ILE   HG21 H  N N 248 
ILE   HG22 H  N N 249 
ILE   HG23 H  N N 250 
ILE   HD11 H  N N 251 
ILE   HD12 H  N N 252 
ILE   HD13 H  N N 253 
ILE   HXT  H  N N 254 
LEU   N    N  N N 255 
LEU   CA   C  N S 256 
LEU   C    C  N N 257 
LEU   O    O  N N 258 
LEU   CB   C  N N 259 
LEU   CG   C  N N 260 
LEU   CD1  C  N N 261 
LEU   CD2  C  N N 262 
LEU   OXT  O  N N 263 
LEU   H    H  N N 264 
LEU   H2   H  N N 265 
LEU   HA   H  N N 266 
LEU   HB2  H  N N 267 
LEU   HB3  H  N N 268 
LEU   HG   H  N N 269 
LEU   HD11 H  N N 270 
LEU   HD12 H  N N 271 
LEU   HD13 H  N N 272 
LEU   HD21 H  N N 273 
LEU   HD22 H  N N 274 
LEU   HD23 H  N N 275 
LEU   HXT  H  N N 276 
LYS   N    N  N N 277 
LYS   CA   C  N S 278 
LYS   C    C  N N 279 
LYS   O    O  N N 280 
LYS   CB   C  N N 281 
LYS   CG   C  N N 282 
LYS   CD   C  N N 283 
LYS   CE   C  N N 284 
LYS   NZ   N  N N 285 
LYS   OXT  O  N N 286 
LYS   H    H  N N 287 
LYS   H2   H  N N 288 
LYS   HA   H  N N 289 
LYS   HB2  H  N N 290 
LYS   HB3  H  N N 291 
LYS   HG2  H  N N 292 
LYS   HG3  H  N N 293 
LYS   HD2  H  N N 294 
LYS   HD3  H  N N 295 
LYS   HE2  H  N N 296 
LYS   HE3  H  N N 297 
LYS   HZ1  H  N N 298 
LYS   HZ2  H  N N 299 
LYS   HZ3  H  N N 300 
LYS   HXT  H  N N 301 
MET   N    N  N N 302 
MET   CA   C  N S 303 
MET   C    C  N N 304 
MET   O    O  N N 305 
MET   CB   C  N N 306 
MET   CG   C  N N 307 
MET   SD   S  N N 308 
MET   CE   C  N N 309 
MET   OXT  O  N N 310 
MET   H    H  N N 311 
MET   H2   H  N N 312 
MET   HA   H  N N 313 
MET   HB2  H  N N 314 
MET   HB3  H  N N 315 
MET   HG2  H  N N 316 
MET   HG3  H  N N 317 
MET   HE1  H  N N 318 
MET   HE2  H  N N 319 
MET   HE3  H  N N 320 
MET   HXT  H  N N 321 
PHE   N    N  N N 322 
PHE   CA   C  N S 323 
PHE   C    C  N N 324 
PHE   O    O  N N 325 
PHE   CB   C  N N 326 
PHE   CG   C  Y N 327 
PHE   CD1  C  Y N 328 
PHE   CD2  C  Y N 329 
PHE   CE1  C  Y N 330 
PHE   CE2  C  Y N 331 
PHE   CZ   C  Y N 332 
PHE   OXT  O  N N 333 
PHE   H    H  N N 334 
PHE   H2   H  N N 335 
PHE   HA   H  N N 336 
PHE   HB2  H  N N 337 
PHE   HB3  H  N N 338 
PHE   HD1  H  N N 339 
PHE   HD2  H  N N 340 
PHE   HE1  H  N N 341 
PHE   HE2  H  N N 342 
PHE   HZ   H  N N 343 
PHE   HXT  H  N N 344 
PRO   N    N  N N 345 
PRO   CA   C  N S 346 
PRO   C    C  N N 347 
PRO   O    O  N N 348 
PRO   CB   C  N N 349 
PRO   CG   C  N N 350 
PRO   CD   C  N N 351 
PRO   OXT  O  N N 352 
PRO   H    H  N N 353 
PRO   HA   H  N N 354 
PRO   HB2  H  N N 355 
PRO   HB3  H  N N 356 
PRO   HG2  H  N N 357 
PRO   HG3  H  N N 358 
PRO   HD2  H  N N 359 
PRO   HD3  H  N N 360 
PRO   HXT  H  N N 361 
SER   N    N  N N 362 
SER   CA   C  N S 363 
SER   C    C  N N 364 
SER   O    O  N N 365 
SER   CB   C  N N 366 
SER   OG   O  N N 367 
SER   OXT  O  N N 368 
SER   H    H  N N 369 
SER   H2   H  N N 370 
SER   HA   H  N N 371 
SER   HB2  H  N N 372 
SER   HB3  H  N N 373 
SER   HG   H  N N 374 
SER   HXT  H  N N 375 
THR   N    N  N N 376 
THR   CA   C  N S 377 
THR   C    C  N N 378 
THR   O    O  N N 379 
THR   CB   C  N R 380 
THR   OG1  O  N N 381 
THR   CG2  C  N N 382 
THR   OXT  O  N N 383 
THR   H    H  N N 384 
THR   H2   H  N N 385 
THR   HA   H  N N 386 
THR   HB   H  N N 387 
THR   HG1  H  N N 388 
THR   HG21 H  N N 389 
THR   HG22 H  N N 390 
THR   HG23 H  N N 391 
THR   HXT  H  N N 392 
TRP   N    N  N N 393 
TRP   CA   C  N S 394 
TRP   C    C  N N 395 
TRP   O    O  N N 396 
TRP   CB   C  N N 397 
TRP   CG   C  Y N 398 
TRP   CD1  C  Y N 399 
TRP   CD2  C  Y N 400 
TRP   NE1  N  Y N 401 
TRP   CE2  C  Y N 402 
TRP   CE3  C  Y N 403 
TRP   CZ2  C  Y N 404 
TRP   CZ3  C  Y N 405 
TRP   CH2  C  Y N 406 
TRP   OXT  O  N N 407 
TRP   H    H  N N 408 
TRP   H2   H  N N 409 
TRP   HA   H  N N 410 
TRP   HB2  H  N N 411 
TRP   HB3  H  N N 412 
TRP   HD1  H  N N 413 
TRP   HE1  H  N N 414 
TRP   HE3  H  N N 415 
TRP   HZ2  H  N N 416 
TRP   HZ3  H  N N 417 
TRP   HH2  H  N N 418 
TRP   HXT  H  N N 419 
TYR   N    N  N N 420 
TYR   CA   C  N S 421 
TYR   C    C  N N 422 
TYR   O    O  N N 423 
TYR   CB   C  N N 424 
TYR   CG   C  Y N 425 
TYR   CD1  C  Y N 426 
TYR   CD2  C  Y N 427 
TYR   CE1  C  Y N 428 
TYR   CE2  C  Y N 429 
TYR   CZ   C  Y N 430 
TYR   OH   O  N N 431 
TYR   OXT  O  N N 432 
TYR   H    H  N N 433 
TYR   H2   H  N N 434 
TYR   HA   H  N N 435 
TYR   HB2  H  N N 436 
TYR   HB3  H  N N 437 
TYR   HD1  H  N N 438 
TYR   HD2  H  N N 439 
TYR   HE1  H  N N 440 
TYR   HE2  H  N N 441 
TYR   HH   H  N N 442 
TYR   HXT  H  N N 443 
VAL   N    N  N N 444 
VAL   CA   C  N S 445 
VAL   C    C  N N 446 
VAL   O    O  N N 447 
VAL   CB   C  N N 448 
VAL   CG1  C  N N 449 
VAL   CG2  C  N N 450 
VAL   OXT  O  N N 451 
VAL   H    H  N N 452 
VAL   H2   H  N N 453 
VAL   HA   H  N N 454 
VAL   HB   H  N N 455 
VAL   HG11 H  N N 456 
VAL   HG12 H  N N 457 
VAL   HG13 H  N N 458 
VAL   HG21 H  N N 459 
VAL   HG22 H  N N 460 
VAL   HG23 H  N N 461 
VAL   HXT  H  N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1IIM C18 C19  sing N N 1   
A1IIM C18 N8   sing N N 2   
A1IIM C19 C20  sing N N 3   
A1IIM C20 C21  sing N N 4   
A1IIM C3  C2   sing N N 5   
A1IIM C3  C4   sing N N 6   
A1IIM C2  C1   sing N N 7   
A1IIM N8  C22  sing N N 8   
A1IIM N8  C15  sing N N 9   
A1IIM C22 C21  sing N N 10  
A1IIM N9  C21  sing N N 11  
A1IIM N9  C23  sing N N 12  
A1IIM C23 C24  sing N N 13  
A1IIM C4  N1   sing N N 14  
A1IIM C24 C26  sing N N 15  
A1IIM C24 C25  sing N N 16  
A1IIM C1  N1   sing N N 17  
A1IIM C16 C15  doub N N 18  
A1IIM C16 C17  sing N N 19  
A1IIM C15 C14  sing N N 20  
A1IIM C26 C25  sing N N 21  
A1IIM N1  C5   sing N N 22  
A1IIM O1  C17  doub N N 23  
A1IIM C17 N7   sing N N 24  
A1IIM C14 C13  doub N N 25  
A1IIM C5  N3   doub Y N 26  
A1IIM C5  C6   sing Y N 27  
A1IIM N3  C8   sing Y N 28  
A1IIM N7  C13  sing N N 29  
A1IIM N7  C11  sing N N 30  
A1IIM C6  N2   doub Y N 31  
A1IIM C10 C9   doub Y N 32  
A1IIM C10 N4   sing Y N 33  
A1IIM C8  C9   sing N N 34  
A1IIM C8  C7   doub Y N 35  
A1IIM C11 N4   sing N N 36  
A1IIM C11 C12  sing N N 37  
A1IIM C9  N6   sing Y N 38  
A1IIM N4  N5   sing Y N 39  
A1IIM N2  C7   sing Y N 40  
A1IIM N6  N5   doub Y N 41  
A1IIM C1  H1   sing N N 42  
A1IIM C1  H2   sing N N 43  
A1IIM C2  H3   sing N N 44  
A1IIM C2  H4   sing N N 45  
A1IIM C3  H5   sing N N 46  
A1IIM C3  H6   sing N N 47  
A1IIM C4  H7   sing N N 48  
A1IIM C4  H8   sing N N 49  
A1IIM C6  H9   sing N N 50  
A1IIM C7  H10  sing N N 51  
A1IIM C10 H11  sing N N 52  
A1IIM C11 H12  sing N N 53  
A1IIM C12 H13  sing N N 54  
A1IIM C12 H14  sing N N 55  
A1IIM C12 H15  sing N N 56  
A1IIM C13 H16  sing N N 57  
A1IIM C14 H17  sing N N 58  
A1IIM C16 H18  sing N N 59  
A1IIM C18 H19  sing N N 60  
A1IIM C18 H20  sing N N 61  
A1IIM C19 H21  sing N N 62  
A1IIM C19 H22  sing N N 63  
A1IIM C20 H23  sing N N 64  
A1IIM C20 H24  sing N N 65  
A1IIM C21 H25  sing N N 66  
A1IIM C22 H26  sing N N 67  
A1IIM C22 H27  sing N N 68  
A1IIM N9  H28  sing N N 69  
A1IIM C23 H30  sing N N 70  
A1IIM C23 H31  sing N N 71  
A1IIM C24 H32  sing N N 72  
A1IIM C25 H33  sing N N 73  
A1IIM C25 H34  sing N N 74  
A1IIM C26 H35  sing N N 75  
A1IIM C26 H36  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
GLN   N   CA   sing N N 159 
GLN   N   H    sing N N 160 
GLN   N   H2   sing N N 161 
GLN   CA  C    sing N N 162 
GLN   CA  CB   sing N N 163 
GLN   CA  HA   sing N N 164 
GLN   C   O    doub N N 165 
GLN   C   OXT  sing N N 166 
GLN   CB  CG   sing N N 167 
GLN   CB  HB2  sing N N 168 
GLN   CB  HB3  sing N N 169 
GLN   CG  CD   sing N N 170 
GLN   CG  HG2  sing N N 171 
GLN   CG  HG3  sing N N 172 
GLN   CD  OE1  doub N N 173 
GLN   CD  NE2  sing N N 174 
GLN   NE2 HE21 sing N N 175 
GLN   NE2 HE22 sing N N 176 
GLN   OXT HXT  sing N N 177 
GLU   N   CA   sing N N 178 
GLU   N   H    sing N N 179 
GLU   N   H2   sing N N 180 
GLU   CA  C    sing N N 181 
GLU   CA  CB   sing N N 182 
GLU   CA  HA   sing N N 183 
GLU   C   O    doub N N 184 
GLU   C   OXT  sing N N 185 
GLU   CB  CG   sing N N 186 
GLU   CB  HB2  sing N N 187 
GLU   CB  HB3  sing N N 188 
GLU   CG  CD   sing N N 189 
GLU   CG  HG2  sing N N 190 
GLU   CG  HG3  sing N N 191 
GLU   CD  OE1  doub N N 192 
GLU   CD  OE2  sing N N 193 
GLU   OE2 HE2  sing N N 194 
GLU   OXT HXT  sing N N 195 
GLY   N   CA   sing N N 196 
GLY   N   H    sing N N 197 
GLY   N   H2   sing N N 198 
GLY   CA  C    sing N N 199 
GLY   CA  HA2  sing N N 200 
GLY   CA  HA3  sing N N 201 
GLY   C   O    doub N N 202 
GLY   C   OXT  sing N N 203 
GLY   OXT HXT  sing N N 204 
HIS   N   CA   sing N N 205 
HIS   N   H    sing N N 206 
HIS   N   H2   sing N N 207 
HIS   CA  C    sing N N 208 
HIS   CA  CB   sing N N 209 
HIS   CA  HA   sing N N 210 
HIS   C   O    doub N N 211 
HIS   C   OXT  sing N N 212 
HIS   CB  CG   sing N N 213 
HIS   CB  HB2  sing N N 214 
HIS   CB  HB3  sing N N 215 
HIS   CG  ND1  sing Y N 216 
HIS   CG  CD2  doub Y N 217 
HIS   ND1 CE1  doub Y N 218 
HIS   ND1 HD1  sing N N 219 
HIS   CD2 NE2  sing Y N 220 
HIS   CD2 HD2  sing N N 221 
HIS   CE1 NE2  sing Y N 222 
HIS   CE1 HE1  sing N N 223 
HIS   NE2 HE2  sing N N 224 
HIS   OXT HXT  sing N N 225 
HOH   O   H1   sing N N 226 
HOH   O   H2   sing N N 227 
ILE   N   CA   sing N N 228 
ILE   N   H    sing N N 229 
ILE   N   H2   sing N N 230 
ILE   CA  C    sing N N 231 
ILE   CA  CB   sing N N 232 
ILE   CA  HA   sing N N 233 
ILE   C   O    doub N N 234 
ILE   C   OXT  sing N N 235 
ILE   CB  CG1  sing N N 236 
ILE   CB  CG2  sing N N 237 
ILE   CB  HB   sing N N 238 
ILE   CG1 CD1  sing N N 239 
ILE   CG1 HG12 sing N N 240 
ILE   CG1 HG13 sing N N 241 
ILE   CG2 HG21 sing N N 242 
ILE   CG2 HG22 sing N N 243 
ILE   CG2 HG23 sing N N 244 
ILE   CD1 HD11 sing N N 245 
ILE   CD1 HD12 sing N N 246 
ILE   CD1 HD13 sing N N 247 
ILE   OXT HXT  sing N N 248 
LEU   N   CA   sing N N 249 
LEU   N   H    sing N N 250 
LEU   N   H2   sing N N 251 
LEU   CA  C    sing N N 252 
LEU   CA  CB   sing N N 253 
LEU   CA  HA   sing N N 254 
LEU   C   O    doub N N 255 
LEU   C   OXT  sing N N 256 
LEU   CB  CG   sing N N 257 
LEU   CB  HB2  sing N N 258 
LEU   CB  HB3  sing N N 259 
LEU   CG  CD1  sing N N 260 
LEU   CG  CD2  sing N N 261 
LEU   CG  HG   sing N N 262 
LEU   CD1 HD11 sing N N 263 
LEU   CD1 HD12 sing N N 264 
LEU   CD1 HD13 sing N N 265 
LEU   CD2 HD21 sing N N 266 
LEU   CD2 HD22 sing N N 267 
LEU   CD2 HD23 sing N N 268 
LEU   OXT HXT  sing N N 269 
LYS   N   CA   sing N N 270 
LYS   N   H    sing N N 271 
LYS   N   H2   sing N N 272 
LYS   CA  C    sing N N 273 
LYS   CA  CB   sing N N 274 
LYS   CA  HA   sing N N 275 
LYS   C   O    doub N N 276 
LYS   C   OXT  sing N N 277 
LYS   CB  CG   sing N N 278 
LYS   CB  HB2  sing N N 279 
LYS   CB  HB3  sing N N 280 
LYS   CG  CD   sing N N 281 
LYS   CG  HG2  sing N N 282 
LYS   CG  HG3  sing N N 283 
LYS   CD  CE   sing N N 284 
LYS   CD  HD2  sing N N 285 
LYS   CD  HD3  sing N N 286 
LYS   CE  NZ   sing N N 287 
LYS   CE  HE2  sing N N 288 
LYS   CE  HE3  sing N N 289 
LYS   NZ  HZ1  sing N N 290 
LYS   NZ  HZ2  sing N N 291 
LYS   NZ  HZ3  sing N N 292 
LYS   OXT HXT  sing N N 293 
MET   N   CA   sing N N 294 
MET   N   H    sing N N 295 
MET   N   H2   sing N N 296 
MET   CA  C    sing N N 297 
MET   CA  CB   sing N N 298 
MET   CA  HA   sing N N 299 
MET   C   O    doub N N 300 
MET   C   OXT  sing N N 301 
MET   CB  CG   sing N N 302 
MET   CB  HB2  sing N N 303 
MET   CB  HB3  sing N N 304 
MET   CG  SD   sing N N 305 
MET   CG  HG2  sing N N 306 
MET   CG  HG3  sing N N 307 
MET   SD  CE   sing N N 308 
MET   CE  HE1  sing N N 309 
MET   CE  HE2  sing N N 310 
MET   CE  HE3  sing N N 311 
MET   OXT HXT  sing N N 312 
PHE   N   CA   sing N N 313 
PHE   N   H    sing N N 314 
PHE   N   H2   sing N N 315 
PHE   CA  C    sing N N 316 
PHE   CA  CB   sing N N 317 
PHE   CA  HA   sing N N 318 
PHE   C   O    doub N N 319 
PHE   C   OXT  sing N N 320 
PHE   CB  CG   sing N N 321 
PHE   CB  HB2  sing N N 322 
PHE   CB  HB3  sing N N 323 
PHE   CG  CD1  doub Y N 324 
PHE   CG  CD2  sing Y N 325 
PHE   CD1 CE1  sing Y N 326 
PHE   CD1 HD1  sing N N 327 
PHE   CD2 CE2  doub Y N 328 
PHE   CD2 HD2  sing N N 329 
PHE   CE1 CZ   doub Y N 330 
PHE   CE1 HE1  sing N N 331 
PHE   CE2 CZ   sing Y N 332 
PHE   CE2 HE2  sing N N 333 
PHE   CZ  HZ   sing N N 334 
PHE   OXT HXT  sing N N 335 
PRO   N   CA   sing N N 336 
PRO   N   CD   sing N N 337 
PRO   N   H    sing N N 338 
PRO   CA  C    sing N N 339 
PRO   CA  CB   sing N N 340 
PRO   CA  HA   sing N N 341 
PRO   C   O    doub N N 342 
PRO   C   OXT  sing N N 343 
PRO   CB  CG   sing N N 344 
PRO   CB  HB2  sing N N 345 
PRO   CB  HB3  sing N N 346 
PRO   CG  CD   sing N N 347 
PRO   CG  HG2  sing N N 348 
PRO   CG  HG3  sing N N 349 
PRO   CD  HD2  sing N N 350 
PRO   CD  HD3  sing N N 351 
PRO   OXT HXT  sing N N 352 
SER   N   CA   sing N N 353 
SER   N   H    sing N N 354 
SER   N   H2   sing N N 355 
SER   CA  C    sing N N 356 
SER   CA  CB   sing N N 357 
SER   CA  HA   sing N N 358 
SER   C   O    doub N N 359 
SER   C   OXT  sing N N 360 
SER   CB  OG   sing N N 361 
SER   CB  HB2  sing N N 362 
SER   CB  HB3  sing N N 363 
SER   OG  HG   sing N N 364 
SER   OXT HXT  sing N N 365 
THR   N   CA   sing N N 366 
THR   N   H    sing N N 367 
THR   N   H2   sing N N 368 
THR   CA  C    sing N N 369 
THR   CA  CB   sing N N 370 
THR   CA  HA   sing N N 371 
THR   C   O    doub N N 372 
THR   C   OXT  sing N N 373 
THR   CB  OG1  sing N N 374 
THR   CB  CG2  sing N N 375 
THR   CB  HB   sing N N 376 
THR   OG1 HG1  sing N N 377 
THR   CG2 HG21 sing N N 378 
THR   CG2 HG22 sing N N 379 
THR   CG2 HG23 sing N N 380 
THR   OXT HXT  sing N N 381 
TRP   N   CA   sing N N 382 
TRP   N   H    sing N N 383 
TRP   N   H2   sing N N 384 
TRP   CA  C    sing N N 385 
TRP   CA  CB   sing N N 386 
TRP   CA  HA   sing N N 387 
TRP   C   O    doub N N 388 
TRP   C   OXT  sing N N 389 
TRP   CB  CG   sing N N 390 
TRP   CB  HB2  sing N N 391 
TRP   CB  HB3  sing N N 392 
TRP   CG  CD1  doub Y N 393 
TRP   CG  CD2  sing Y N 394 
TRP   CD1 NE1  sing Y N 395 
TRP   CD1 HD1  sing N N 396 
TRP   CD2 CE2  doub Y N 397 
TRP   CD2 CE3  sing Y N 398 
TRP   NE1 CE2  sing Y N 399 
TRP   NE1 HE1  sing N N 400 
TRP   CE2 CZ2  sing Y N 401 
TRP   CE3 CZ3  doub Y N 402 
TRP   CE3 HE3  sing N N 403 
TRP   CZ2 CH2  doub Y N 404 
TRP   CZ2 HZ2  sing N N 405 
TRP   CZ3 CH2  sing Y N 406 
TRP   CZ3 HZ3  sing N N 407 
TRP   CH2 HH2  sing N N 408 
TRP   OXT HXT  sing N N 409 
TYR   N   CA   sing N N 410 
TYR   N   H    sing N N 411 
TYR   N   H2   sing N N 412 
TYR   CA  C    sing N N 413 
TYR   CA  CB   sing N N 414 
TYR   CA  HA   sing N N 415 
TYR   C   O    doub N N 416 
TYR   C   OXT  sing N N 417 
TYR   CB  CG   sing N N 418 
TYR   CB  HB2  sing N N 419 
TYR   CB  HB3  sing N N 420 
TYR   CG  CD1  doub Y N 421 
TYR   CG  CD2  sing Y N 422 
TYR   CD1 CE1  sing Y N 423 
TYR   CD1 HD1  sing N N 424 
TYR   CD2 CE2  doub Y N 425 
TYR   CD2 HD2  sing N N 426 
TYR   CE1 CZ   doub Y N 427 
TYR   CE1 HE1  sing N N 428 
TYR   CE2 CZ   sing Y N 429 
TYR   CE2 HE2  sing N N 430 
TYR   CZ  OH   sing N N 431 
TYR   OH  HH   sing N N 432 
TYR   OXT HXT  sing N N 433 
VAL   N   CA   sing N N 434 
VAL   N   H    sing N N 435 
VAL   N   H2   sing N N 436 
VAL   CA  C    sing N N 437 
VAL   CA  CB   sing N N 438 
VAL   CA  HA   sing N N 439 
VAL   C   O    doub N N 440 
VAL   C   OXT  sing N N 441 
VAL   CB  CG1  sing N N 442 
VAL   CB  CG2  sing N N 443 
VAL   CB  HB   sing N N 444 
VAL   CG1 HG11 sing N N 445 
VAL   CG1 HG12 sing N N 446 
VAL   CG1 HG13 sing N N 447 
VAL   CG2 HG21 sing N N 448 
VAL   CG2 HG22 sing N N 449 
VAL   CG2 HG23 sing N N 450 
VAL   OXT HXT  sing N N 451 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7O2I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G4W 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.015553 
_atom_sites.fract_transf_matrix[1][2]   0.008980 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017959 
_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]   0.004409 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA   A 1 1   ? -26.486 20.212  46.314  1.00 75.18  ? 365 ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 1   ? -27.496 19.312  45.678  1.00 73.88  ? 365 ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 1   ? -28.819 19.346  46.470  1.00 82.82  ? 365 ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 1   ? -29.897 19.251  45.837  1.00 81.04  ? 365 ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 1   ? -26.922 17.916  45.545  1.00 68.09  ? 365 ALA   A CB  1 
ATOM   6    N  N   . ASP   A 1 2   ? -28.750 19.507  47.798  1.00 96.97  ? 366 ASP   A N   1 
ATOM   7    C  CA  . ASP   A 1 2   ? -29.924 19.538  48.717  1.00 102.07 ? 366 ASP   A CA  1 
ATOM   8    C  C   . ASP   A 1 2   ? -30.805 20.755  48.386  1.00 104.62 ? 366 ASP   A C   1 
ATOM   9    O  O   . ASP   A 1 2   ? -32.041 20.581  48.366  1.00 102.93 ? 366 ASP   A O   1 
ATOM   10   C  CB  . ASP   A 1 2   ? -29.491 19.568  50.190  1.00 101.88 ? 366 ASP   A CB  1 
ATOM   11   C  CG  . ASP   A 1 2   ? -28.443 18.532  50.563  1.00 97.33  ? 366 ASP   A CG  1 
ATOM   12   O  OD1 . ASP   A 1 2   ? -28.437 17.456  49.939  1.00 96.88  ? 366 ASP   A OD1 1 
ATOM   13   O  OD2 . ASP   A 1 2   ? -27.632 18.817  51.468  1.00 92.28  ? 366 ASP   A OD2 1 
ATOM   14   N  N   . ARG   A 1 3   ? -30.176 21.913  48.120  1.00 100.29 ? 367 ARG   A N   1 
ATOM   15   C  CA  . ARG   A 1 3   ? -30.779 23.278  48.013  1.00 101.77 ? 367 ARG   A CA  1 
ATOM   16   C  C   . ARG   A 1 3   ? -32.107 23.235  47.235  1.00 100.61 ? 367 ARG   A C   1 
ATOM   17   O  O   . ARG   A 1 3   ? -32.167 22.532  46.192  1.00 103.49 ? 367 ARG   A O   1 
ATOM   18   C  CB  . ARG   A 1 3   ? -29.751 24.232  47.382  1.00 102.23 ? 367 ARG   A CB  1 
ATOM   19   C  CG  . ARG   A 1 3   ? -30.260 25.621  47.006  1.00 106.80 ? 367 ARG   A CG  1 
ATOM   20   C  CD  . ARG   A 1 3   ? -30.645 26.519  48.173  1.00 107.12 ? 367 ARG   A CD  1 
ATOM   21   N  NE  . ARG   A 1 3   ? -30.155 27.885  47.995  1.00 105.59 ? 367 ARG   A NE  1 
ATOM   22   C  CZ  . ARG   A 1 3   ? -29.542 28.625  48.926  1.00 105.41 ? 367 ARG   A CZ  1 
ATOM   23   N  NH1 . ARG   A 1 3   ? -29.350 28.158  50.149  1.00 102.68 ? 367 ARG   A NH1 1 
ATOM   24   N  NH2 . ARG   A 1 3   ? -29.137 29.851  48.634  1.00 104.54 ? 367 ARG   A NH2 1 
ATOM   25   N  N   . LEU   A 1 4   ? -33.128 23.946  47.750  1.00 91.66  ? 368 LEU   A N   1 
ATOM   26   C  CA  . LEU   A 1 4   ? -34.464 24.174  47.118  1.00 82.35  ? 368 LEU   A CA  1 
ATOM   27   C  C   . LEU   A 1 4   ? -34.934 25.596  47.470  1.00 77.25  ? 368 LEU   A C   1 
ATOM   28   O  O   . LEU   A 1 4   ? -35.940 25.742  48.197  1.00 76.74  ? 368 LEU   A O   1 
ATOM   29   C  CB  . LEU   A 1 4   ? -35.466 23.103  47.582  1.00 87.70  ? 368 LEU   A CB  1 
ATOM   30   C  CG  . LEU   A 1 4   ? -35.279 21.697  46.995  1.00 94.46  ? 368 LEU   A CG  1 
ATOM   31   C  CD1 . LEU   A 1 4   ? -36.110 20.664  47.745  1.00 94.31  ? 368 LEU   A CD1 1 
ATOM   32   C  CD2 . LEU   A 1 4   ? -35.615 21.658  45.507  1.00 95.08  ? 368 LEU   A CD2 1 
ATOM   33   N  N   . PHE   A 1 5   ? -34.206 26.603  46.974  1.00 70.60  ? 369 PHE   A N   1 
ATOM   34   C  CA  . PHE   A 1 5   ? -34.503 28.057  47.092  1.00 57.25  ? 369 PHE   A CA  1 
ATOM   35   C  C   . PHE   A 1 5   ? -35.821 28.383  46.387  1.00 53.20  ? 369 PHE   A C   1 
ATOM   36   O  O   . PHE   A 1 5   ? -36.062 27.922  45.277  1.00 42.49  ? 369 PHE   A O   1 
ATOM   37   C  CB  . PHE   A 1 5   ? -33.348 28.856  46.503  1.00 55.34  ? 369 PHE   A CB  1 
ATOM   38   C  CG  . PHE   A 1 5   ? -33.323 30.282  46.971  1.00 54.19  ? 369 PHE   A CG  1 
ATOM   39   C  CD1 . PHE   A 1 5   ? -34.238 31.191  46.486  1.00 52.72  ? 369 PHE   A CD1 1 
ATOM   40   C  CD2 . PHE   A 1 5   ? -32.386 30.703  47.903  1.00 56.31  ? 369 PHE   A CD2 1 
ATOM   41   C  CE1 . PHE   A 1 5   ? -34.217 32.500  46.937  1.00 58.12  ? 369 PHE   A CE1 1 
ATOM   42   C  CE2 . PHE   A 1 5   ? -32.372 32.008  48.360  1.00 53.61  ? 369 PHE   A CE2 1 
ATOM   43   C  CZ  . PHE   A 1 5   ? -33.290 32.902  47.876  1.00 56.82  ? 369 PHE   A CZ  1 
ATOM   44   N  N   . PRO   A 1 6   ? -36.758 29.148  46.999  1.00 49.17  ? 370 PRO   A N   1 
ATOM   45   C  CA  . PRO   A 1 6   ? -38.112 29.244  46.452  1.00 47.20  ? 370 PRO   A CA  1 
ATOM   46   C  C   . PRO   A 1 6   ? -38.182 29.997  45.128  1.00 45.34  ? 370 PRO   A C   1 
ATOM   47   O  O   . PRO   A 1 6   ? -37.254 30.705  44.767  1.00 46.37  ? 370 PRO   A O   1 
ATOM   48   C  CB  . PRO   A 1 6   ? -38.929 29.983  47.533  1.00 49.92  ? 370 PRO   A CB  1 
ATOM   49   C  CG  . PRO   A 1 6   ? -38.036 29.998  48.756  1.00 52.82  ? 370 PRO   A CG  1 
ATOM   50   C  CD  . PRO   A 1 6   ? -36.608 29.913  48.245  1.00 49.51  ? 370 PRO   A CD  1 
ATOM   51   N  N   . PRO   A 1 7   ? -39.297 29.878  44.377  1.00 44.15  ? 371 PRO   A N   1 
ATOM   52   C  CA  . PRO   A 1 7   ? -39.425 30.521  43.075  1.00 42.28  ? 371 PRO   A CA  1 
ATOM   53   C  C   . PRO   A 1 7   ? -39.258 32.047  43.121  1.00 47.72  ? 371 PRO   A C   1 
ATOM   54   O  O   . PRO   A 1 7   ? -39.755 32.652  44.039  1.00 40.71  ? 371 PRO   A O   1 
ATOM   55   C  CB  . PRO   A 1 7   ? -40.858 30.231  42.628  1.00 42.03  ? 371 PRO   A CB  1 
ATOM   56   C  CG  . PRO   A 1 7   ? -41.308 29.034  43.457  1.00 44.28  ? 371 PRO   A CG  1 
ATOM   57   C  CD  . PRO   A 1 7   ? -40.466 29.052  44.717  1.00 42.49  ? 371 PRO   A CD  1 
ATOM   58   N  N   . GLN   A 1 8   ? -38.600 32.619  42.107  1.00 40.80  ? 372 GLN   A N   1 
ATOM   59   C  CA  . GLN   A 1 8   ? -38.413 34.078  41.935  1.00 35.24  ? 372 GLN   A CA  1 
ATOM   60   C  C   . GLN   A 1 8   ? -38.660 34.383  40.474  1.00 36.32  ? 372 GLN   A C   1 
ATOM   61   O  O   . GLN   A 1 8   ? -38.419 33.479  39.638  1.00 33.41  ? 372 GLN   A O   1 
ATOM   62   C  CB  . GLN   A 1 8   ? -37.009 34.572  42.291  1.00 37.62  ? 372 GLN   A CB  1 
ATOM   63   C  CG  . GLN   A 1 8   ? -36.502 34.096  43.633  1.00 37.96  ? 372 GLN   A CG  1 
ATOM   64   C  CD  . GLN   A 1 8   ? -35.052 34.425  43.862  1.00 38.00  ? 372 GLN   A CD  1 
ATOM   65   O  OE1 . GLN   A 1 8   ? -34.692 35.546  44.227  1.00 37.99  ? 372 GLN   A OE1 1 
ATOM   66   N  NE2 . GLN   A 1 8   ? -34.202 33.426  43.718  1.00 37.46  ? 372 GLN   A NE2 1 
ATOM   67   N  N   . TRP   A 1 9   ? -39.121 35.598  40.194  1.00 32.81  ? 373 TRP   A N   1 
ATOM   68   C  CA  . TRP   A 1 9   ? -39.440 36.077  38.839  1.00 33.51  ? 373 TRP   A CA  1 
ATOM   69   C  C   . TRP   A 1 9   ? -39.294 37.595  38.711  1.00 32.87  ? 373 TRP   A C   1 
ATOM   70   O  O   . TRP   A 1 9   ? -39.249 38.297  39.723  1.00 39.46  ? 373 TRP   A O   1 
ATOM   71   C  CB  . TRP   A 1 9   ? -40.834 35.610  38.411  1.00 35.85  ? 373 TRP   A CB  1 
ATOM   72   C  CG  . TRP   A 1 9   ? -41.974 36.095  39.245  1.00 39.34  ? 373 TRP   A CG  1 
ATOM   73   C  CD1 . TRP   A 1 9   ? -42.703 37.225  39.042  1.00 42.52  ? 373 TRP   A CD1 1 
ATOM   74   C  CD2 . TRP   A 1 9   ? -42.571 35.419  40.366  1.00 41.01  ? 373 TRP   A CD2 1 
ATOM   75   N  NE1 . TRP   A 1 9   ? -43.712 37.297  39.957  1.00 45.73  ? 373 TRP   A NE1 1 
ATOM   76   C  CE2 . TRP   A 1 9   ? -43.647 36.218  40.795  1.00 45.13  ? 373 TRP   A CE2 1 
ATOM   77   C  CE3 . TRP   A 1 9   ? -42.303 34.223  41.043  1.00 45.37  ? 373 TRP   A CE3 1 
ATOM   78   C  CZ2 . TRP   A 1 9   ? -44.466 35.856  41.868  1.00 44.25  ? 373 TRP   A CZ2 1 
ATOM   79   C  CZ3 . TRP   A 1 9   ? -43.093 33.877  42.117  1.00 49.81  ? 373 TRP   A CZ3 1 
ATOM   80   C  CH2 . TRP   A 1 9   ? -44.170 34.679  42.513  1.00 44.83  ? 373 TRP   A CH2 1 
ATOM   81   N  N   . ILE   A 1 10  ? -39.306 38.061  37.474  1.00 33.16  ? 374 ILE   A N   1 
ATOM   82   C  CA  . ILE   A 1 10  ? -39.220 39.489  37.083  1.00 33.89  ? 374 ILE   A CA  1 
ATOM   83   C  C   . ILE   A 1 10  ? -40.050 39.625  35.834  1.00 35.39  ? 374 ILE   A C   1 
ATOM   84   O  O   . ILE   A 1 10  ? -39.635 39.041  34.797  1.00 37.21  ? 374 ILE   A O   1 
ATOM   85   C  CB  . ILE   A 1 10  ? -37.763 39.934  36.855  1.00 35.50  ? 374 ILE   A CB  1 
ATOM   86   C  CG1 . ILE   A 1 10  ? -36.874 39.651  38.068  1.00 34.51  ? 374 ILE   A CG1 1 
ATOM   87   C  CG2 . ILE   A 1 10  ? -37.697 41.386  36.439  1.00 34.89  ? 374 ILE   A CG2 1 
ATOM   88   C  CD1 . ILE   A 1 10  ? -35.419 40.116  37.880  1.00 36.64  ? 374 ILE   A CD1 1 
ATOM   89   N  N   . CYS   A 1 11  ? -41.184 40.321  35.929  1.00 31.16  ? 375 CYS   A N   1 
ATOM   90   C  CA  . CYS   A 1 11  ? -41.929 40.818  34.772  1.00 32.08  ? 375 CYS   A CA  1 
ATOM   91   C  C   . CYS   A 1 11  ? -41.062 41.873  34.093  1.00 39.52  ? 375 CYS   A C   1 
ATOM   92   O  O   . CYS   A 1 11  ? -40.676 42.837  34.775  1.00 34.48  ? 375 CYS   A O   1 
ATOM   93   C  CB  . CYS   A 1 11  ? -43.302 41.339  35.154  1.00 33.17  ? 375 CYS   A CB  1 
ATOM   94   S  SG  . CYS   A 1 11  ? -44.260 41.802  33.707  1.00 38.88  ? 375 CYS   A SG  1 
ATOM   95   N  N   . CYS   A 1 12  ? -40.700 41.654  32.824  1.00 34.51  ? 376 CYS   A N   1 
ATOM   96   C  CA  . CYS   A 1 12  ? -39.894 42.607  32.035  1.00 38.14  ? 376 CYS   A CA  1 
ATOM   97   C  C   . CYS   A 1 12  ? -40.064 42.352  30.549  1.00 40.24  ? 376 CYS   A C   1 
ATOM   98   O  O   . CYS   A 1 12  ? -40.509 41.239  30.148  1.00 34.96  ? 376 CYS   A O   1 
ATOM   99   C  CB  . CYS   A 1 12  ? -38.420 42.512  32.401  1.00 39.53  ? 376 CYS   A CB  1 
ATOM   100  S  SG  . CYS   A 1 12  ? -37.751 40.826  32.306  1.00 40.25  ? 376 CYS   A SG  1 
ATOM   101  N  N   . ASP   A 1 13  ? -39.661 43.354  29.780  1.00 37.51  ? 377 ASP   A N   1 
ATOM   102  C  CA  . ASP   A 1 13  ? -39.201 43.199  28.381  1.00 37.00  ? 377 ASP   A CA  1 
ATOM   103  C  C   . ASP   A 1 13  ? -37.760 42.690  28.456  1.00 32.92  ? 377 ASP   A C   1 
ATOM   104  O  O   . ASP   A 1 13  ? -36.896 43.388  28.982  1.00 33.41  ? 377 ASP   A O   1 
ATOM   105  C  CB  . ASP   A 1 13  ? -39.346 44.507  27.609  1.00 37.98  ? 377 ASP   A CB  1 
ATOM   106  C  CG  . ASP   A 1 13  ? -39.251 44.308  26.116  1.00 39.64  ? 377 ASP   A CG  1 
ATOM   107  O  OD1 . ASP   A 1 13  ? -38.285 43.658  25.678  1.00 36.44  ? 377 ASP   A OD1 1 
ATOM   108  O  OD2 . ASP   A 1 13  ? -40.123 44.823  25.405  1.00 39.96  ? 377 ASP   A OD2 1 
ATOM   109  N  N   . ILE   A 1 14  ? -37.523 41.467  27.998  1.00 33.21  ? 378 ILE   A N   1 
ATOM   110  C  CA  . ILE   A 1 14  ? -36.217 40.781  28.189  1.00 31.16  ? 378 ILE   A CA  1 
ATOM   111  C  C   . ILE   A 1 14  ? -35.179 41.469  27.296  1.00 31.13  ? 378 ILE   A C   1 
ATOM   112  O  O   . ILE   A 1 14  ? -33.968 41.289  27.554  1.00 30.61  ? 378 ILE   A O   1 
ATOM   113  C  CB  . ILE   A 1 14  ? -36.390 39.262  27.936  1.00 31.64  ? 378 ILE   A CB  1 
ATOM   114  C  CG1 . ILE   A 1 14  ? -37.179 38.641  29.087  1.00 29.11  ? 378 ILE   A CG1 1 
ATOM   115  C  CG2 . ILE   A 1 14  ? -35.049 38.565  27.713  1.00 32.41  ? 378 ILE   A CG2 1 
ATOM   116  C  CD1 . ILE   A 1 14  ? -37.749 37.253  28.825  1.00 31.75  ? 378 ILE   A CD1 1 
ATOM   117  N  N   . ARG   A 1 15  ? -35.625 42.215  26.287  1.00 29.57  ? 379 ARG   A N   1 
ATOM   118  C  CA  . ARG   A 1 15  ? -34.735 43.031  25.435  1.00 33.41  ? 379 ARG   A CA  1 
ATOM   119  C  C   . ARG   A 1 15  ? -34.066 44.112  26.293  1.00 35.21  ? 379 ARG   A C   1 
ATOM   120  O  O   . ARG   A 1 15  ? -32.939 44.411  25.986  1.00 35.64  ? 379 ARG   A O   1 
ATOM   121  C  CB  . ARG   A 1 15  ? -35.483 43.705  24.286  1.00 35.63  ? 379 ARG   A CB  1 
ATOM   122  C  CG  . ARG   A 1 15  ? -36.093 42.748  23.278  1.00 35.18  ? 379 ARG   A CG  1 
ATOM   123  C  CD  . ARG   A 1 15  ? -36.785 43.548  22.221  1.00 35.53  ? 379 ARG   A CD  1 
ATOM   124  N  NE  . ARG   A 1 15  ? -37.944 44.211  22.801  1.00 38.13  ? 379 ARG   A NE  1 
ATOM   125  C  CZ  . ARG   A 1 15  ? -38.785 44.991  22.129  1.00 36.99  ? 379 ARG   A CZ  1 
ATOM   126  N  NH1 . ARG   A 1 15  ? -38.621 45.214  20.838  1.00 36.31  ? 379 ARG   A NH1 1 
ATOM   127  N  NH2 . ARG   A 1 15  ? -39.836 45.493  22.740  1.00 38.03  ? 379 ARG   A NH2 1 
ATOM   128  N  N   . TYR   A 1 16  ? -34.704 44.580  27.377  1.00 35.34  ? 380 TYR   A N   1 
ATOM   129  C  CA  . TYR   A 1 16  ? -34.309 45.819  28.106  1.00 37.52  ? 380 TYR   A CA  1 
ATOM   130  C  C   . TYR   A 1 16  ? -33.716 45.513  29.478  1.00 38.95  ? 380 TYR   A C   1 
ATOM   131  O  O   . TYR   A 1 16  ? -32.872 46.297  29.946  1.00 38.16  ? 380 TYR   A O   1 
ATOM   132  C  CB  . TYR   A 1 16  ? -35.515 46.756  28.156  1.00 38.67  ? 380 TYR   A CB  1 
ATOM   133  C  CG  . TYR   A 1 16  ? -36.072 47.074  26.793  1.00 38.06  ? 380 TYR   A CG  1 
ATOM   134  C  CD1 . TYR   A 1 16  ? -35.241 47.126  25.696  1.00 40.70  ? 380 TYR   A CD1 1 
ATOM   135  C  CD2 . TYR   A 1 16  ? -37.415 47.325  26.596  1.00 43.60  ? 380 TYR   A CD2 1 
ATOM   136  C  CE1 . TYR   A 1 16  ? -35.721 47.439  24.437  1.00 48.57  ? 380 TYR   A CE1 1 
ATOM   137  C  CE2 . TYR   A 1 16  ? -37.918 47.642  25.343  1.00 47.47  ? 380 TYR   A CE2 1 
ATOM   138  C  CZ  . TYR   A 1 16  ? -37.065 47.687  24.255  1.00 47.88  ? 380 TYR   A CZ  1 
ATOM   139  O  OH  . TYR   A 1 16  ? -37.505 47.970  22.994  1.00 57.78  ? 380 TYR   A OH  1 
ATOM   140  N  N   . LEU   A 1 17  ? -34.052 44.376  30.088  1.00 35.86  ? 381 LEU   A N   1 
ATOM   141  C  CA  . LEU   A 1 17  ? -33.554 44.081  31.449  1.00 36.62  ? 381 LEU   A CA  1 
ATOM   142  C  C   . LEU   A 1 17  ? -32.038 43.935  31.394  1.00 40.20  ? 381 LEU   A C   1 
ATOM   143  O  O   . LEU   A 1 17  ? -31.521 43.246  30.462  1.00 34.94  ? 381 LEU   A O   1 
ATOM   144  C  CB  . LEU   A 1 17  ? -34.193 42.813  32.019  1.00 36.86  ? 381 LEU   A CB  1 
ATOM   145  C  CG  . LEU   A 1 17  ? -33.646 42.361  33.365  1.00 36.64  ? 381 LEU   A CG  1 
ATOM   146  C  CD1 . LEU   A 1 17  ? -34.041 43.349  34.447  1.00 39.84  ? 381 LEU   A CD1 1 
ATOM   147  C  CD2 . LEU   A 1 17  ? -34.131 40.961  33.732  1.00 34.65  ? 381 LEU   A CD2 1 
ATOM   148  N  N   . ASP   A 1 18  ? -31.363 44.505  32.390  1.00 35.25  ? 382 ASP   A N   1 
ATOM   149  C  CA  . ASP   A 1 18  ? -29.911 44.319  32.601  1.00 36.25  ? 382 ASP   A CA  1 
ATOM   150  C  C   . ASP   A 1 18  ? -29.709 43.007  33.370  1.00 38.37  ? 382 ASP   A C   1 
ATOM   151  O  O   . ASP   A 1 18  ? -29.821 42.990  34.611  1.00 36.91  ? 382 ASP   A O   1 
ATOM   152  C  CB  . ASP   A 1 18  ? -29.326 45.536  33.319  1.00 41.42  ? 382 ASP   A CB  1 
ATOM   153  C  CG  . ASP   A 1 18  ? -27.842 45.400  33.607  1.00 46.39  ? 382 ASP   A CG  1 
ATOM   154  O  OD1 . ASP   A 1 18  ? -27.213 44.411  33.106  1.00 45.14  ? 382 ASP   A OD1 1 
ATOM   155  O  OD2 . ASP   A 1 18  ? -27.321 46.275  34.340  1.00 47.64  ? 382 ASP   A OD2 1 
ATOM   156  N  N   . VAL   A 1 19  ? -29.419 41.915  32.670  1.00 35.24  ? 383 VAL   A N   1 
ATOM   157  C  CA  . VAL   A 1 19  ? -29.321 40.582  33.320  1.00 37.13  ? 383 VAL   A CA  1 
ATOM   158  C  C   . VAL   A 1 19  ? -27.992 40.415  34.058  1.00 36.76  ? 383 VAL   A C   1 
ATOM   159  O  O   . VAL   A 1 19  ? -27.822 39.363  34.679  1.00 34.74  ? 383 VAL   A O   1 
ATOM   160  C  CB  . VAL   A 1 19  ? -29.571 39.433  32.315  1.00 38.66  ? 383 VAL   A CB  1 
ATOM   161  C  CG1 . VAL   A 1 19  ? -31.034 39.376  31.934  1.00 35.10  ? 383 VAL   A CG1 1 
ATOM   162  C  CG2 . VAL   A 1 19  ? -28.682 39.534  31.088  1.00 38.69  ? 383 VAL   A CG2 1 
ATOM   163  N  N   . SER   A 1 20  ? -27.068 41.383  34.004  1.00 41.40  ? 384 SER   A N   1 
ATOM   164  C  CA  . SER   A 1 20  ? -25.799 41.332  34.784  1.00 40.39  ? 384 SER   A CA  1 
ATOM   165  C  C   . SER   A 1 20  ? -26.101 41.335  36.282  1.00 40.08  ? 384 SER   A C   1 
ATOM   166  O  O   . SER   A 1 20  ? -25.261 40.838  37.013  1.00 41.40  ? 384 SER   A O   1 
ATOM   167  C  CB  . SER   A 1 20  ? -24.870 42.450  34.444  1.00 44.30  ? 384 SER   A CB  1 
ATOM   168  O  OG  . SER   A 1 20  ? -25.502 43.692  34.681  1.00 41.74  ? 384 SER   A OG  1 
ATOM   169  N  N   . ILE   A 1 21  ? -27.276 41.807  36.721  1.00 41.54  ? 385 ILE   A N   1 
ATOM   170  C  CA  . ILE   A 1 21  ? -27.617 41.920  38.174  1.00 42.93  ? 385 ILE   A CA  1 
ATOM   171  C  C   . ILE   A 1 21  ? -27.949 40.535  38.748  1.00 44.32  ? 385 ILE   A C   1 
ATOM   172  O  O   . ILE   A 1 21  ? -27.947 40.396  39.973  1.00 43.55  ? 385 ILE   A O   1 
ATOM   173  C  CB  . ILE   A 1 21  ? -28.760 42.922  38.438  1.00 46.97  ? 385 ILE   A CB  1 
ATOM   174  C  CG1 . ILE   A 1 21  ? -30.115 42.415  37.931  1.00 44.91  ? 385 ILE   A CG1 1 
ATOM   175  C  CG2 . ILE   A 1 21  ? -28.411 44.285  37.872  1.00 51.38  ? 385 ILE   A CG2 1 
ATOM   176  C  CD1 . ILE   A 1 21  ? -31.214 43.451  37.953  1.00 45.79  ? 385 ILE   A CD1 1 
ATOM   177  N  N   . LEU   A 1 22  ? -28.151 39.517  37.903  1.00 41.75  ? 386 LEU   A N   1 
ATOM   178  C  CA  . LEU   A 1 22  ? -28.763 38.227  38.317  1.00 33.85  ? 386 LEU   A CA  1 
ATOM   179  C  C   . LEU   A 1 22  ? -27.677 37.236  38.730  1.00 33.23  ? 386 LEU   A C   1 
ATOM   180  O  O   . LEU   A 1 22  ? -28.008 36.173  39.278  1.00 36.66  ? 386 LEU   A O   1 
ATOM   181  C  CB  . LEU   A 1 22  ? -29.625 37.721  37.155  1.00 35.85  ? 386 LEU   A CB  1 
ATOM   182  C  CG  . LEU   A 1 22  ? -30.744 38.668  36.714  1.00 34.83  ? 386 LEU   A CG  1 
ATOM   183  C  CD1 . LEU   A 1 22  ? -31.617 38.045  35.645  1.00 35.32  ? 386 LEU   A CD1 1 
ATOM   184  C  CD2 . LEU   A 1 22  ? -31.617 39.075  37.894  1.00 38.79  ? 386 LEU   A CD2 1 
ATOM   185  N  N   . GLY   A 1 23  ? -26.409 37.552  38.468  1.00 33.99  ? 387 GLY   A N   1 
ATOM   186  C  CA  . GLY   A 1 23  ? -25.305 36.612  38.696  1.00 35.23  ? 387 GLY   A CA  1 
ATOM   187  C  C   . GLY   A 1 23  ? -25.285 35.501  37.647  1.00 33.92  ? 387 GLY   A C   1 
ATOM   188  O  O   . GLY   A 1 23  ? -25.835 35.695  36.532  1.00 35.30  ? 387 GLY   A O   1 
ATOM   189  N  N   . LYS   A 1 24  ? -24.705 34.370  38.036  1.00 31.83  ? 388 LYS   A N   1 
ATOM   190  C  CA  . LYS   A 1 24  ? -24.280 33.245  37.189  1.00 32.36  ? 388 LYS   A CA  1 
ATOM   191  C  C   . LYS   A 1 24  ? -25.131 32.020  37.516  1.00 36.41  ? 388 LYS   A C   1 
ATOM   192  O  O   . LYS   A 1 24  ? -25.457 31.807  38.701  1.00 35.29  ? 388 LYS   A O   1 
ATOM   193  C  CB  . LYS   A 1 24  ? -22.814 32.886  37.435  1.00 33.91  ? 388 LYS   A CB  1 
ATOM   194  C  CG  . LYS   A 1 24  ? -21.797 34.003  37.253  1.00 34.22  ? 388 LYS   A CG  1 
ATOM   195  C  CD  . LYS   A 1 24  ? -21.830 34.656  35.908  1.00 35.73  ? 388 LYS   A CD  1 
ATOM   196  C  CE  . LYS   A 1 24  ? -20.818 35.776  35.791  1.00 36.00  ? 388 LYS   A CE  1 
ATOM   197  N  NZ  . LYS   A 1 24  ? -21.137 36.660  34.642  1.00 37.44  ? 388 LYS   A NZ  1 
ATOM   198  N  N   . PHE   A 1 25  ? -25.395 31.194  36.500  1.00 36.97  ? 389 PHE   A N   1 
ATOM   199  C  CA  . PHE   A 1 25  ? -26.376 30.080  36.553  1.00 33.29  ? 389 PHE   A CA  1 
ATOM   200  C  C   . PHE   A 1 25  ? -25.745 28.823  35.973  1.00 32.37  ? 389 PHE   A C   1 
ATOM   201  O  O   . PHE   A 1 25  ? -24.978 28.934  34.984  1.00 31.34  ? 389 PHE   A O   1 
ATOM   202  C  CB  . PHE   A 1 25  ? -27.634 30.486  35.784  1.00 31.98  ? 389 PHE   A CB  1 
ATOM   203  C  CG  . PHE   A 1 25  ? -28.377 31.628  36.407  1.00 32.35  ? 389 PHE   A CG  1 
ATOM   204  C  CD1 . PHE   A 1 25  ? -29.287 31.406  37.432  1.00 35.79  ? 389 PHE   A CD1 1 
ATOM   205  C  CD2 . PHE   A 1 25  ? -28.129 32.938  36.014  1.00 31.09  ? 389 PHE   A CD2 1 
ATOM   206  C  CE1 . PHE   A 1 25  ? -29.964 32.470  38.013  1.00 35.21  ? 389 PHE   A CE1 1 
ATOM   207  C  CE2 . PHE   A 1 25  ? -28.782 34.002  36.616  1.00 34.34  ? 389 PHE   A CE2 1 
ATOM   208  C  CZ  . PHE   A 1 25  ? -29.719 33.764  37.604  1.00 36.23  ? 389 PHE   A CZ  1 
ATOM   209  N  N   . ALA   A 1 26  ? -26.047 27.682  36.583  1.00 30.14  ? 390 ALA   A N   1 
ATOM   210  C  CA  . ALA   A 1 26  ? -25.608 26.361  36.105  1.00 30.67  ? 390 ALA   A CA  1 
ATOM   211  C  C   . ALA   A 1 26  ? -26.351 26.033  34.801  1.00 30.95  ? 390 ALA   A C   1 
ATOM   212  O  O   . ALA   A 1 26  ? -25.787 25.278  33.978  1.00 27.11  ? 390 ALA   A O   1 
ATOM   213  C  CB  . ALA   A 1 26  ? -25.843 25.312  37.161  1.00 33.05  ? 390 ALA   A CB  1 
ATOM   214  N  N   . VAL   A 1 27  ? -27.616 26.469  34.686  1.00 29.56  ? 391 VAL   A N   1 
ATOM   215  C  CA  . VAL   A 1 27  ? -28.500 26.170  33.528  1.00 29.07  ? 391 VAL   A CA  1 
ATOM   216  C  C   . VAL   A 1 27  ? -29.282 27.416  33.156  1.00 27.09  ? 391 VAL   A C   1 
ATOM   217  O  O   . VAL   A 1 27  ? -29.794 28.137  34.050  1.00 29.33  ? 391 VAL   A O   1 
ATOM   218  C  CB  . VAL   A 1 27  ? -29.458 25.002  33.804  1.00 30.68  ? 391 VAL   A CB  1 
ATOM   219  C  CG1 . VAL   A 1 27  ? -30.339 24.745  32.603  1.00 33.02  ? 391 VAL   A CG1 1 
ATOM   220  C  CG2 . VAL   A 1 27  ? -28.721 23.732  34.190  1.00 32.27  ? 391 VAL   A CG2 1 
ATOM   221  N  N   . VAL   A 1 28  ? -29.296 27.713  31.868  1.00 26.69  ? 392 VAL   A N   1 
ATOM   222  C  CA  . VAL   A 1 28  ? -30.167 28.722  31.233  1.00 24.52  ? 392 VAL   A CA  1 
ATOM   223  C  C   . VAL   A 1 28  ? -31.163 27.943  30.405  1.00 25.44  ? 392 VAL   A C   1 
ATOM   224  O  O   . VAL   A 1 28  ? -30.719 27.091  29.624  1.00 26.11  ? 392 VAL   A O   1 
ATOM   225  C  CB  . VAL   A 1 28  ? -29.365 29.713  30.378  1.00 25.08  ? 392 VAL   A CB  1 
ATOM   226  C  CG1 . VAL   A 1 28  ? -30.280 30.689  29.659  1.00 25.40  ? 392 VAL   A CG1 1 
ATOM   227  C  CG2 . VAL   A 1 28  ? -28.369 30.479  31.235  1.00 27.80  ? 392 VAL   A CG2 1 
ATOM   228  N  N   . MET   A 1 29  ? -32.446 28.275  30.489  1.00 25.25  ? 393 MET   A N   1 
ATOM   229  C  CA  . MET   A 1 29  ? -33.404 27.833  29.458  1.00 26.83  ? 393 MET   A CA  1 
ATOM   230  C  C   . MET   A 1 29  ? -34.086 29.037  28.832  1.00 25.52  ? 393 MET   A C   1 
ATOM   231  O  O   . MET   A 1 29  ? -34.437 29.996  29.558  1.00 26.59  ? 393 MET   A O   1 
ATOM   232  C  CB  . MET   A 1 29  ? -34.425 26.850  30.030  1.00 28.96  ? 393 MET   A CB  1 
ATOM   233  C  CG  . MET   A 1 29  ? -35.389 26.338  28.990  1.00 30.35  ? 393 MET   A CG  1 
ATOM   234  S  SD  . MET   A 1 29  ? -36.274 24.887  29.579  1.00 29.16  ? 393 MET   A SD  1 
ATOM   235  C  CE  . MET   A 1 29  ? -37.236 25.533  30.957  1.00 31.88  ? 393 MET   A CE  1 
ATOM   236  N  N   . ALA   A 1 30  ? -34.261 29.005  27.520  1.00 25.05  ? 394 ALA   A N   1 
ATOM   237  C  CA  . ALA   A 1 30  ? -35.037 30.041  26.802  1.00 26.12  ? 394 ALA   A CA  1 
ATOM   238  C  C   . ALA   A 1 30  ? -36.037 29.418  25.851  1.00 25.88  ? 394 ALA   A C   1 
ATOM   239  O  O   . ALA   A 1 30  ? -35.668 28.484  25.129  1.00 26.08  ? 394 ALA   A O   1 
ATOM   240  C  CB  . ALA   A 1 30  ? -34.112 30.943  26.046  1.00 23.85  ? 394 ALA   A CB  1 
ATOM   241  N  N   . ASP   A 1 31  ? -37.234 29.999  25.795  1.00 26.07  ? 395 ASP   A N   1 
ATOM   242  C  CA  . ASP   A 1 31  ? -38.301 29.590  24.859  1.00 25.93  ? 395 ASP   A CA  1 
ATOM   243  C  C   . ASP   A 1 31  ? -38.743 30.817  24.083  1.00 27.25  ? 395 ASP   A C   1 
ATOM   244  O  O   . ASP   A 1 31  ? -39.834 31.335  24.288  1.00 28.37  ? 395 ASP   A O   1 
ATOM   245  C  CB  . ASP   A 1 31  ? -39.409 28.858  25.624  1.00 27.56  ? 395 ASP   A CB  1 
ATOM   246  C  CG  . ASP   A 1 31  ? -40.576 28.475  24.745  1.00 26.73  ? 395 ASP   A CG  1 
ATOM   247  O  OD1 . ASP   A 1 31  ? -40.356 28.290  23.522  1.00 26.37  ? 395 ASP   A OD1 1 
ATOM   248  O  OD2 . ASP   A 1 31  ? -41.717 28.496  25.274  1.00 28.96  ? 395 ASP   A OD2 1 
ATOM   249  N  N   . PRO   A 1 32  ? -37.931 31.305  23.122  1.00 27.38  ? 396 PRO   A N   1 
ATOM   250  C  CA  . PRO   A 1 32  ? -38.183 32.607  22.519  1.00 26.85  ? 396 PRO   A CA  1 
ATOM   251  C  C   . PRO   A 1 32  ? -39.343 32.575  21.553  1.00 28.64  ? 396 PRO   A C   1 
ATOM   252  O  O   . PRO   A 1 32  ? -39.570 31.551  20.914  1.00 25.47  ? 396 PRO   A O   1 
ATOM   253  C  CB  . PRO   A 1 32  ? -36.907 32.949  21.726  1.00 26.00  ? 396 PRO   A CB  1 
ATOM   254  C  CG  . PRO   A 1 32  ? -35.876 31.976  22.252  1.00 26.59  ? 396 PRO   A CG  1 
ATOM   255  C  CD  . PRO   A 1 32  ? -36.642 30.760  22.703  1.00 27.33  ? 396 PRO   A CD  1 
ATOM   256  N  N   . PRO   A 1 33  ? -40.069 33.711  21.424  1.00 27.76  ? 397 PRO   A N   1 
ATOM   257  C  CA  . PRO   A 1 33  ? -41.010 33.927  20.341  1.00 27.67  ? 397 PRO   A CA  1 
ATOM   258  C  C   . PRO   A 1 33  ? -40.221 34.347  19.110  1.00 33.40  ? 397 PRO   A C   1 
ATOM   259  O  O   . PRO   A 1 33  ? -40.096 35.554  18.799  1.00 29.88  ? 397 PRO   A O   1 
ATOM   260  C  CB  . PRO   A 1 33  ? -41.935 35.027  20.872  1.00 30.66  ? 397 PRO   A CB  1 
ATOM   261  C  CG  . PRO   A 1 33  ? -41.058 35.818  21.832  1.00 27.78  ? 397 PRO   A CG  1 
ATOM   262  C  CD  . PRO   A 1 33  ? -40.047 34.836  22.382  1.00 29.15  ? 397 PRO   A CD  1 
ATOM   263  N  N   . TRP   A 1 34  ? -39.634 33.335  18.489  1.00 27.49  ? 398 TRP   A N   1 
ATOM   264  C  CA  . TRP   A 1 34  ? -38.835 33.499  17.269  1.00 30.96  ? 398 TRP   A CA  1 
ATOM   265  C  C   . TRP   A 1 34  ? -39.700 34.173  16.210  1.00 32.14  ? 398 TRP   A C   1 
ATOM   266  O  O   . TRP   A 1 34  ? -40.889 33.891  16.122  1.00 32.19  ? 398 TRP   A O   1 
ATOM   267  C  CB  . TRP   A 1 34  ? -38.320 32.143  16.789  1.00 28.02  ? 398 TRP   A CB  1 
ATOM   268  C  CG  . TRP   A 1 34  ? -37.395 31.430  17.722  1.00 25.57  ? 398 TRP   A CG  1 
ATOM   269  C  CD1 . TRP   A 1 34  ? -37.687 30.322  18.459  1.00 25.68  ? 398 TRP   A CD1 1 
ATOM   270  C  CD2 . TRP   A 1 34  ? -36.015 31.707  17.957  1.00 25.51  ? 398 TRP   A CD2 1 
ATOM   271  N  NE1 . TRP   A 1 34  ? -36.580 29.902  19.129  1.00 24.90  ? 398 TRP   A NE1 1 
ATOM   272  C  CE2 . TRP   A 1 34  ? -35.544 30.728  18.847  1.00 25.00  ? 398 TRP   A CE2 1 
ATOM   273  C  CE3 . TRP   A 1 34  ? -35.124 32.669  17.473  1.00 25.49  ? 398 TRP   A CE3 1 
ATOM   274  C  CZ2 . TRP   A 1 34  ? -34.228 30.686  19.289  1.00 25.50  ? 398 TRP   A CZ2 1 
ATOM   275  C  CZ3 . TRP   A 1 34  ? -33.824 32.635  17.914  1.00 26.97  ? 398 TRP   A CZ3 1 
ATOM   276  C  CH2 . TRP   A 1 34  ? -33.382 31.653  18.805  1.00 25.65  ? 398 TRP   A CH2 1 
ATOM   277  N  N   . ASP   A 1 35  ? -39.079 35.032  15.422  1.00 34.05  ? 399 ASP   A N   1 
ATOM   278  C  CA  . ASP   A 1 35  ? -39.620 35.489  14.126  1.00 37.19  ? 399 ASP   A CA  1 
ATOM   279  C  C   . ASP   A 1 35  ? -39.590 34.300  13.162  1.00 38.75  ? 399 ASP   A C   1 
ATOM   280  O  O   . ASP   A 1 35  ? -38.481 33.994  12.625  1.00 39.95  ? 399 ASP   A O   1 
ATOM   281  C  CB  . ASP   A 1 35  ? -38.765 36.636  13.586  1.00 39.86  ? 399 ASP   A CB  1 
ATOM   282  C  CG  . ASP   A 1 35  ? -39.302 37.221  12.295  1.00 44.14  ? 399 ASP   A CG  1 
ATOM   283  O  OD1 . ASP   A 1 35  ? -40.249 36.630  11.715  1.00 45.35  ? 399 ASP   A OD1 1 
ATOM   284  O  OD2 . ASP   A 1 35  ? -38.765 38.262  11.893  1.00 49.46  ? 399 ASP   A OD2 1 
ATOM   285  N  N   . ILE   A 1 36  ? -40.716 33.617  12.962  1.00 36.27  ? 400 ILE   A N   1 
ATOM   286  C  CA  . ILE   A 1 36  ? -40.715 32.432  12.058  1.00 42.87  ? 400 ILE   A CA  1 
ATOM   287  C  C   . ILE   A 1 36  ? -41.251 32.832  10.670  1.00 51.21  ? 400 ILE   A C   1 
ATOM   288  O  O   . ILE   A 1 36  ? -41.546 31.935  9.851   1.00 47.65  ? 400 ILE   A O   1 
ATOM   289  C  CB  . ILE   A 1 36  ? -41.416 31.243  12.722  1.00 40.91  ? 400 ILE   A CB  1 
ATOM   290  C  CG1 . ILE   A 1 36  ? -42.824 31.564  13.214  1.00 45.40  ? 400 ILE   A CG1 1 
ATOM   291  C  CG2 . ILE   A 1 36  ? -40.567 30.733  13.874  1.00 40.63  ? 400 ILE   A CG2 1 
ATOM   292  C  CD1 . ILE   A 1 36  ? -43.564 30.332  13.701  1.00 49.06  ? 400 ILE   A CD1 1 
ATOM   293  N  N   . HIS   A 1 37  ? -41.193 34.130  10.359  1.00 53.99  ? 401 HIS   A N   1 
ATOM   294  C  CA  . HIS   A 1 37  ? -41.580 34.716  9.050   1.00 53.99  ? 401 HIS   A CA  1 
ATOM   295  C  C   . HIS   A 1 37  ? -43.033 34.358  8.780   1.00 56.47  ? 401 HIS   A C   1 
ATOM   296  O  O   . HIS   A 1 37  ? -43.284 33.667  7.801   1.00 56.92  ? 401 HIS   A O   1 
ATOM   297  C  CB  . HIS   A 1 37  ? -40.714 34.202  7.884   1.00 52.04  ? 401 HIS   A CB  1 
ATOM   298  C  CG  . HIS   A 1 37  ? -39.316 34.711  7.852   1.00 45.34  ? 401 HIS   A CG  1 
ATOM   299  N  ND1 . HIS   A 1 37  ? -38.896 35.778  8.623   1.00 45.78  ? 401 HIS   A ND1 1 
ATOM   300  C  CD2 . HIS   A 1 37  ? -38.259 34.333  7.101   1.00 45.30  ? 401 HIS   A CD2 1 
ATOM   301  C  CE1 . HIS   A 1 37  ? -37.621 36.008  8.391   1.00 46.65  ? 401 HIS   A CE1 1 
ATOM   302  N  NE2 . HIS   A 1 37  ? -37.201 35.131  7.452   1.00 48.33  ? 401 HIS   A NE2 1 
ATOM   303  N  N   . MET   A 1 38  ? -43.941 34.763  9.652   1.00 63.10  ? 402 MET   A N   1 
ATOM   304  C  CA  . MET   A 1 38  ? -45.384 34.747  9.318   1.00 70.79  ? 402 MET   A CA  1 
ATOM   305  C  C   . MET   A 1 38  ? -46.131 35.615  10.322  1.00 67.39  ? 402 MET   A C   1 
ATOM   306  O  O   . MET   A 1 38  ? -45.604 35.813  11.429  1.00 67.21  ? 402 MET   A O   1 
ATOM   307  C  CB  . MET   A 1 38  ? -45.963 33.328  9.305   1.00 72.26  ? 402 MET   A CB  1 
ATOM   308  C  CG  . MET   A 1 38  ? -45.770 32.560  10.587  1.00 78.37  ? 402 MET   A CG  1 
ATOM   309  S  SD  . MET   A 1 38  ? -46.486 30.894  10.507  1.00 82.30  ? 402 MET   A SD  1 
ATOM   310  C  CE  . MET   A 1 38  ? -48.206 31.272  10.167  1.00 86.43  ? 402 MET   A CE  1 
ATOM   311  N  N   . GLU   A 1 39  ? -47.262 36.162  9.879   1.00 64.22  ? 403 GLU   A N   1 
ATOM   312  C  CA  . GLU   A 1 39  ? -48.307 36.815  10.703  1.00 70.84  ? 403 GLU   A CA  1 
ATOM   313  C  C   . GLU   A 1 39  ? -48.595 35.909  11.904  1.00 66.06  ? 403 GLU   A C   1 
ATOM   314  O  O   . GLU   A 1 39  ? -48.962 34.751  11.673  1.00 66.92  ? 403 GLU   A O   1 
ATOM   315  C  CB  . GLU   A 1 39  ? -49.560 37.009  9.843   1.00 82.13  ? 403 GLU   A CB  1 
ATOM   316  C  CG  . GLU   A 1 39  ? -50.566 37.993  10.412  1.00 89.74  ? 403 GLU   A CG  1 
ATOM   317  C  CD  . GLU   A 1 39  ? -50.324 39.445  10.037  1.00 97.37  ? 403 GLU   A CD  1 
ATOM   318  O  OE1 . GLU   A 1 39  ? -51.230 40.275  10.271  1.00 102.45 ? 403 GLU   A OE1 1 
ATOM   319  O  OE2 . GLU   A 1 39  ? -49.231 39.745  9.514   1.00 105.97 ? 403 GLU   A OE2 1 
ATOM   320  N  N   . LEU   A 1 40  ? -48.383 36.392  13.130  1.00 60.23  ? 404 LEU   A N   1 
ATOM   321  C  CA  . LEU   A 1 40  ? -48.654 35.613  14.368  1.00 62.13  ? 404 LEU   A CA  1 
ATOM   322  C  C   . LEU   A 1 40  ? -49.541 36.424  15.311  1.00 57.53  ? 404 LEU   A C   1 
ATOM   323  O  O   . LEU   A 1 40  ? -49.554 37.649  15.273  1.00 59.05  ? 404 LEU   A O   1 
ATOM   324  C  CB  . LEU   A 1 40  ? -47.323 35.227  15.029  1.00 62.27  ? 404 LEU   A CB  1 
ATOM   325  C  CG  . LEU   A 1 40  ? -46.546 34.101  14.341  1.00 62.99  ? 404 LEU   A CG  1 
ATOM   326  C  CD1 . LEU   A 1 40  ? -45.070 34.145  14.706  1.00 63.18  ? 404 LEU   A CD1 1 
ATOM   327  C  CD2 . LEU   A 1 40  ? -47.132 32.744  14.690  1.00 63.81  ? 404 LEU   A CD2 1 
ATOM   328  N  N   . PRO   A 1 41  ? -50.314 35.752  16.189  1.00 55.79  ? 405 PRO   A N   1 
ATOM   329  C  CA  . PRO   A 1 41  ? -51.103 36.443  17.209  1.00 57.05  ? 405 PRO   A CA  1 
ATOM   330  C  C   . PRO   A 1 41  ? -50.318 37.015  18.403  1.00 60.68  ? 405 PRO   A C   1 
ATOM   331  O  O   . PRO   A 1 41  ? -50.938 37.656  19.226  1.00 59.35  ? 405 PRO   A O   1 
ATOM   332  C  CB  . PRO   A 1 41  ? -52.024 35.326  17.732  1.00 57.33  ? 405 PRO   A CB  1 
ATOM   333  C  CG  . PRO   A 1 41  ? -51.217 34.055  17.534  1.00 55.09  ? 405 PRO   A CG  1 
ATOM   334  C  CD  . PRO   A 1 41  ? -50.483 34.288  16.231  1.00 55.20  ? 405 PRO   A CD  1 
ATOM   335  N  N   . TYR   A 1 42  ? -49.008 36.751  18.501  1.00 51.47  ? 406 TYR   A N   1 
ATOM   336  C  CA  . TYR   A 1 42  ? -48.147 37.219  19.618  1.00 46.05  ? 406 TYR   A CA  1 
ATOM   337  C  C   . TYR   A 1 42  ? -46.985 38.023  19.026  1.00 40.52  ? 406 TYR   A C   1 
ATOM   338  O  O   . TYR   A 1 42  ? -46.685 37.898  17.807  1.00 42.52  ? 406 TYR   A O   1 
ATOM   339  C  CB  . TYR   A 1 42  ? -47.714 36.042  20.502  1.00 48.77  ? 406 TYR   A CB  1 
ATOM   340  C  CG  . TYR   A 1 42  ? -47.048 34.931  19.734  1.00 48.17  ? 406 TYR   A CG  1 
ATOM   341  C  CD1 . TYR   A 1 42  ? -45.703 35.014  19.422  1.00 42.78  ? 406 TYR   A CD1 1 
ATOM   342  C  CD2 . TYR   A 1 42  ? -47.766 33.837  19.265  1.00 47.52  ? 406 TYR   A CD2 1 
ATOM   343  C  CE1 . TYR   A 1 42  ? -45.085 34.048  18.654  1.00 44.78  ? 406 TYR   A CE1 1 
ATOM   344  C  CE2 . TYR   A 1 42  ? -47.156 32.847  18.511  1.00 46.17  ? 406 TYR   A CE2 1 
ATOM   345  C  CZ  . TYR   A 1 42  ? -45.811 32.959  18.206  1.00 42.08  ? 406 TYR   A CZ  1 
ATOM   346  O  OH  . TYR   A 1 42  ? -45.167 32.041  17.453  1.00 37.36  ? 406 TYR   A OH  1 
ATOM   347  N  N   . GLY   A 1 43  ? -46.368 38.850  19.864  1.00 37.14  ? 407 GLY   A N   1 
ATOM   348  C  CA  . GLY   A 1 43  ? -45.142 39.591  19.533  1.00 38.30  ? 407 GLY   A CA  1 
ATOM   349  C  C   . GLY   A 1 43  ? -43.953 38.644  19.441  1.00 34.14  ? 407 GLY   A C   1 
ATOM   350  O  O   . GLY   A 1 43  ? -43.857 37.736  20.272  1.00 33.52  ? 407 GLY   A O   1 
ATOM   351  N  N   . THR   A 1 44  ? -43.088 38.881  18.462  1.00 38.86  ? 408 THR   A N   1 
ATOM   352  C  CA  . THR   A 1 44  ? -41.835 38.138  18.227  1.00 38.71  ? 408 THR   A CA  1 
ATOM   353  C  C   . THR   A 1 44  ? -40.645 39.081  18.392  1.00 40.24  ? 408 THR   A C   1 
ATOM   354  O  O   . THR   A 1 44  ? -40.805 40.315  18.289  1.00 37.86  ? 408 THR   A O   1 
ATOM   355  C  CB  . THR   A 1 44  ? -41.846 37.480  16.845  1.00 40.38  ? 408 THR   A CB  1 
ATOM   356  O  OG1 . THR   A 1 44  ? -41.992 38.518  15.868  1.00 40.76  ? 408 THR   A OG1 1 
ATOM   357  C  CG2 . THR   A 1 44  ? -42.954 36.455  16.740  1.00 35.29  ? 408 THR   A CG2 1 
ATOM   358  N  N   . LEU   A 1 45  ? -39.486 38.510  18.688  1.00 33.54  ? 409 LEU   A N   1 
ATOM   359  C  CA  . LEU   A 1 45  ? -38.200 39.240  18.648  1.00 32.11  ? 409 LEU   A CA  1 
ATOM   360  C  C   . LEU   A 1 45  ? -37.631 39.092  17.234  1.00 32.28  ? 409 LEU   A C   1 
ATOM   361  O  O   . LEU   A 1 45  ? -37.704 37.981  16.645  1.00 33.70  ? 409 LEU   A O   1 
ATOM   362  C  CB  . LEU   A 1 45  ? -37.255 38.696  19.725  1.00 33.91  ? 409 LEU   A CB  1 
ATOM   363  C  CG  . LEU   A 1 45  ? -37.356 39.332  21.115  1.00 33.18  ? 409 LEU   A CG  1 
ATOM   364  C  CD1 . LEU   A 1 45  ? -38.555 38.834  21.875  1.00 34.68  ? 409 LEU   A CD1 1 
ATOM   365  C  CD2 . LEU   A 1 45  ? -36.129 39.042  21.949  1.00 35.68  ? 409 LEU   A CD2 1 
ATOM   366  N  N   . THR   A 1 46  ? -37.105 40.172  16.676  1.00 28.71  ? 410 THR   A N   1 
ATOM   367  C  CA  . THR   A 1 46  ? -36.352 40.114  15.406  1.00 28.15  ? 410 THR   A CA  1 
ATOM   368  C  C   . THR   A 1 46  ? -35.117 39.261  15.627  1.00 27.83  ? 410 THR   A C   1 
ATOM   369  O  O   . THR   A 1 46  ? -34.641 39.122  16.770  1.00 30.31  ? 410 THR   A O   1 
ATOM   370  C  CB  . THR   A 1 46  ? -35.954 41.500  14.864  1.00 32.27  ? 410 THR   A CB  1 
ATOM   371  O  OG1 . THR   A 1 46  ? -35.031 42.084  15.794  1.00 32.22  ? 410 THR   A OG1 1 
ATOM   372  C  CG2 . THR   A 1 46  ? -37.168 42.372  14.640  1.00 34.92  ? 410 THR   A CG2 1 
ATOM   373  N  N   . ASP   A 1 47  ? -34.579 38.754  14.527  1.00 30.92  ? 411 ASP   A N   1 
ATOM   374  C  CA  . ASP   A 1 47  ? -33.314 38.015  14.532  1.00 28.04  ? 411 ASP   A CA  1 
ATOM   375  C  C   . ASP   A 1 47  ? -32.249 38.840  15.259  1.00 31.68  ? 411 ASP   A C   1 
ATOM   376  O  O   . ASP   A 1 47  ? -31.520 38.273  16.091  1.00 29.46  ? 411 ASP   A O   1 
ATOM   377  C  CB  . ASP   A 1 47  ? -32.961 37.621  13.105  1.00 31.49  ? 411 ASP   A CB  1 
ATOM   378  C  CG  . ASP   A 1 47  ? -33.949 36.703  12.389  1.00 29.93  ? 411 ASP   A CG  1 
ATOM   379  O  OD1 . ASP   A 1 47  ? -35.014 36.296  12.956  1.00 30.51  ? 411 ASP   A OD1 1 
ATOM   380  O  OD2 . ASP   A 1 47  ? -33.643 36.430  11.233  1.00 34.68  ? 411 ASP   A OD2 1 
ATOM   381  N  N   . ASP   A 1 48  ? -32.152 40.144  14.986  1.00 34.87  ? 412 ASP   A N   1 
ATOM   382  C  CA  . ASP   A 1 48  ? -31.088 40.993  15.590  1.00 37.20  ? 412 ASP   A CA  1 
ATOM   383  C  C   . ASP   A 1 48  ? -31.313 41.143  17.097  1.00 29.15  ? 412 ASP   A C   1 
ATOM   384  O  O   . ASP   A 1 48  ? -30.315 41.044  17.837  1.00 30.37  ? 412 ASP   A O   1 
ATOM   385  C  CB  . ASP   A 1 48  ? -30.954 42.332  14.863  1.00 39.08  ? 412 ASP   A CB  1 
ATOM   386  C  CG  . ASP   A 1 48  ? -30.133 42.205  13.592  1.00 46.01  ? 412 ASP   A CG  1 
ATOM   387  O  OD1 . ASP   A 1 48  ? -29.259 41.273  13.518  1.00 43.33  ? 412 ASP   A OD1 1 
ATOM   388  O  OD2 . ASP   A 1 48  ? -30.361 43.033  12.686  1.00 50.52  ? 412 ASP   A OD2 1 
ATOM   389  N  N   . GLU   A 1 49  ? -32.566 41.280  17.534  1.00 29.21  ? 413 GLU   A N   1 
ATOM   390  C  CA  . GLU   A 1 49  ? -32.924 41.367  18.968  1.00 30.03  ? 413 GLU   A CA  1 
ATOM   391  C  C   . GLU   A 1 49  ? -32.549 40.071  19.687  1.00 30.52  ? 413 GLU   A C   1 
ATOM   392  O  O   . GLU   A 1 49  ? -32.027 40.139  20.848  1.00 27.78  ? 413 GLU   A O   1 
ATOM   393  C  CB  . GLU   A 1 49  ? -34.404 41.659  19.129  1.00 35.81  ? 413 GLU   A CB  1 
ATOM   394  C  CG  . GLU   A 1 49  ? -34.761 43.101  18.778  1.00 36.36  ? 413 GLU   A CG  1 
ATOM   395  C  CD  . GLU   A 1 49  ? -36.254 43.413  18.754  1.00 40.77  ? 413 GLU   A CD  1 
ATOM   396  O  OE1 . GLU   A 1 49  ? -37.089 42.493  18.544  1.00 36.75  ? 413 GLU   A OE1 1 
ATOM   397  O  OE2 . GLU   A 1 49  ? -36.592 44.600  18.939  1.00 37.52  ? 413 GLU   A OE2 1 
ATOM   398  N  N   . MET   A 1 50  ? -32.769 38.926  19.034  1.00 28.62  ? 414 MET   A N   1 
ATOM   399  C  CA  . MET   A 1 50  ? -32.371 37.618  19.612  1.00 28.96  ? 414 MET   A CA  1 
ATOM   400  C  C   . MET   A 1 50  ? -30.849 37.540  19.696  1.00 25.88  ? 414 MET   A C   1 
ATOM   401  O  O   . MET   A 1 50  ? -30.327 37.161  20.778  1.00 24.49  ? 414 MET   A O   1 
ATOM   402  C  CB  . MET   A 1 50  ? -32.936 36.476  18.763  1.00 29.36  ? 414 MET   A CB  1 
ATOM   403  C  CG  . MET   A 1 50  ? -34.439 36.336  18.909  1.00 28.29  ? 414 MET   A CG  1 
ATOM   404  S  SD  . MET   A 1 50  ? -34.891 35.951  20.590  1.00 28.80  ? 414 MET   A SD  1 
ATOM   405  C  CE  . MET   A 1 50  ? -33.802 34.594  21.045  1.00 30.87  ? 414 MET   A CE  1 
ATOM   406  N  N   . ARG   A 1 51  ? -30.142 37.958  18.644  1.00 29.38  ? 415 ARG   A N   1 
ATOM   407  C  CA  . ARG   A 1 51  ? -28.665 37.871  18.601  1.00 29.93  ? 415 ARG   A CA  1 
ATOM   408  C  C   . ARG   A 1 51  ? -28.085 38.720  19.737  1.00 29.75  ? 415 ARG   A C   1 
ATOM   409  O  O   . ARG   A 1 51  ? -27.071 38.294  20.343  1.00 27.47  ? 415 ARG   A O   1 
ATOM   410  C  CB  . ARG   A 1 51  ? -28.102 38.353  17.253  1.00 32.85  ? 415 ARG   A CB  1 
ATOM   411  C  CG  . ARG   A 1 51  ? -28.257 37.377  16.098  1.00 35.49  ? 415 ARG   A CG  1 
ATOM   412  C  CD  . ARG   A 1 51  ? -27.690 38.037  14.844  1.00 37.17  ? 415 ARG   A CD  1 
ATOM   413  N  NE  . ARG   A 1 51  ? -27.948 37.171  13.725  1.00 38.32  ? 415 ARG   A NE  1 
ATOM   414  C  CZ  . ARG   A 1 51  ? -28.863 37.348  12.796  1.00 36.01  ? 415 ARG   A CZ  1 
ATOM   415  N  NH1 . ARG   A 1 51  ? -29.032 36.402  11.887  1.00 38.38  ? 415 ARG   A NH1 1 
ATOM   416  N  NH2 . ARG   A 1 51  ? -29.601 38.442  12.757  1.00 40.27  ? 415 ARG   A NH2 1 
ATOM   417  N  N   . ARG   A 1 52  ? -28.705 39.869  20.007  1.00 33.29  ? 416 ARG   A N   1 
ATOM   418  C  CA  . ARG   A 1 52  ? -28.201 40.911  20.943  1.00 34.72  ? 416 ARG   A CA  1 
ATOM   419  C  C   . ARG   A 1 52  ? -28.537 40.561  22.401  1.00 33.37  ? 416 ARG   A C   1 
ATOM   420  O  O   . ARG   A 1 52  ? -27.940 41.170  23.293  1.00 31.36  ? 416 ARG   A O   1 
ATOM   421  C  CB  . ARG   A 1 52  ? -28.767 42.288  20.559  1.00 38.24  ? 416 ARG   A CB  1 
ATOM   422  C  CG  . ARG   A 1 52  ? -28.100 42.908  19.338  1.00 48.78  ? 416 ARG   A CG  1 
ATOM   423  C  CD  . ARG   A 1 52  ? -28.335 44.412  19.202  1.00 52.36  ? 416 ARG   A CD  1 
ATOM   424  N  NE  . ARG   A 1 52  ? -29.760 44.669  19.114  1.00 53.38  ? 416 ARG   A NE  1 
ATOM   425  C  CZ  . ARG   A 1 52  ? -30.435 44.996  18.011  1.00 56.75  ? 416 ARG   A CZ  1 
ATOM   426  N  NH1 . ARG   A 1 52  ? -29.823 45.178  16.849  1.00 54.41  ? 416 ARG   A NH1 1 
ATOM   427  N  NH2 . ARG   A 1 52  ? -31.744 45.162  18.084  1.00 56.46  ? 416 ARG   A NH2 1 
ATOM   428  N  N   . LEU   A 1 53  ? -29.398 39.584  22.673  1.00 29.62  ? 417 LEU   A N   1 
ATOM   429  C  CA  . LEU   A 1 53  ? -29.665 39.171  24.079  1.00 30.33  ? 417 LEU   A CA  1 
ATOM   430  C  C   . LEU   A 1 53  ? -28.356 38.886  24.799  1.00 32.04  ? 417 LEU   A C   1 
ATOM   431  O  O   . LEU   A 1 53  ? -27.471 38.223  24.209  1.00 28.67  ? 417 LEU   A O   1 
ATOM   432  C  CB  . LEU   A 1 53  ? -30.560 37.934  24.119  1.00 30.96  ? 417 LEU   A CB  1 
ATOM   433  C  CG  . LEU   A 1 53  ? -31.989 38.178  23.675  1.00 32.76  ? 417 LEU   A CG  1 
ATOM   434  C  CD1 . LEU   A 1 53  ? -32.825 36.924  23.878  1.00 31.73  ? 417 LEU   A CD1 1 
ATOM   435  C  CD2 . LEU   A 1 53  ? -32.597 39.351  24.427  1.00 35.88  ? 417 LEU   A CD2 1 
ATOM   436  N  N   . ASN   A 1 54  ? -28.221 39.395  26.030  1.00 30.05  ? 418 ASN   A N   1 
ATOM   437  C  CA  . ASN   A 1 54  ? -26.946 39.332  26.788  1.00 28.40  ? 418 ASN   A CA  1 
ATOM   438  C  C   . ASN   A 1 54  ? -26.835 37.987  27.508  1.00 29.74  ? 418 ASN   A C   1 
ATOM   439  O  O   . ASN   A 1 54  ? -26.438 37.944  28.668  1.00 30.01  ? 418 ASN   A O   1 
ATOM   440  C  CB  . ASN   A 1 54  ? -26.755 40.569  27.665  1.00 33.21  ? 418 ASN   A CB  1 
ATOM   441  C  CG  . ASN   A 1 54  ? -25.324 40.668  28.151  1.00 39.32  ? 418 ASN   A CG  1 
ATOM   442  O  OD1 . ASN   A 1 54  ? -24.443 39.919  27.709  1.00 40.03  ? 418 ASN   A OD1 1 
ATOM   443  N  ND2 . ASN   A 1 54  ? -25.107 41.523  29.132  1.00 37.93  ? 418 ASN   A ND2 1 
ATOM   444  N  N   . ILE   A 1 55  ? -27.035 36.889  26.768  1.00 26.89  ? 419 ILE   A N   1 
ATOM   445  C  CA  . ILE   A 1 55  ? -26.892 35.514  27.294  1.00 24.98  ? 419 ILE   A CA  1 
ATOM   446  C  C   . ILE   A 1 55  ? -25.488 35.278  27.810  1.00 25.91  ? 419 ILE   A C   1 
ATOM   447  O  O   . ILE   A 1 55  ? -25.305 34.583  28.802  1.00 26.37  ? 419 ILE   A O   1 
ATOM   448  C  CB  . ILE   A 1 55  ? -27.257 34.486  26.209  1.00 26.64  ? 419 ILE   A CB  1 
ATOM   449  C  CG1 . ILE   A 1 55  ? -28.663 34.715  25.662  1.00 27.71  ? 419 ILE   A CG1 1 
ATOM   450  C  CG2 . ILE   A 1 55  ? -27.060 33.093  26.769  1.00 24.17  ? 419 ILE   A CG2 1 
ATOM   451  C  CD1 . ILE   A 1 55  ? -29.709 34.886  26.738  1.00 31.31  ? 419 ILE   A CD1 1 
ATOM   452  N  N   . PRO   A 1 56  ? -24.425 35.790  27.169  1.00 28.92  ? 420 PRO   A N   1 
ATOM   453  C  CA  . PRO   A 1 56  ? -23.078 35.527  27.658  1.00 30.03  ? 420 PRO   A CA  1 
ATOM   454  C  C   . PRO   A 1 56  ? -22.764 35.893  29.118  1.00 28.78  ? 420 PRO   A C   1 
ATOM   455  O  O   . PRO   A 1 56  ? -21.891 35.242  29.644  1.00 30.04  ? 420 PRO   A O   1 
ATOM   456  C  CB  . PRO   A 1 56  ? -22.205 36.363  26.706  1.00 30.23  ? 420 PRO   A CB  1 
ATOM   457  C  CG  . PRO   A 1 56  ? -23.001 36.385  25.456  1.00 30.19  ? 420 PRO   A CG  1 
ATOM   458  C  CD  . PRO   A 1 56  ? -24.421 36.601  25.947  1.00 31.02  ? 420 PRO   A CD  1 
ATOM   459  N  N   . VAL   A 1 57  ? -23.451 36.878  29.711  1.00 29.41  ? 421 VAL   A N   1 
ATOM   460  C  CA  . VAL   A 1 57  ? -23.254 37.340  31.122  1.00 31.99  ? 421 VAL   A CA  1 
ATOM   461  C  C   . VAL   A 1 57  ? -23.866 36.339  32.111  1.00 36.82  ? 421 VAL   A C   1 
ATOM   462  O  O   . VAL   A 1 57  ? -23.442 36.329  33.285  1.00 35.65  ? 421 VAL   A O   1 
ATOM   463  C  CB  . VAL   A 1 57  ? -23.772 38.780  31.334  1.00 36.97  ? 421 VAL   A CB  1 
ATOM   464  C  CG1 . VAL   A 1 57  ? -25.278 38.886  31.464  1.00 38.42  ? 421 VAL   A CG1 1 
ATOM   465  C  CG2 . VAL   A 1 57  ? -23.127 39.436  32.533  1.00 42.80  ? 421 VAL   A CG2 1 
ATOM   466  N  N   . LEU   A 1 58  ? -24.742 35.435  31.661  1.00 35.36  ? 422 LEU   A N   1 
ATOM   467  C  CA  . LEU   A 1 58  ? -25.527 34.565  32.570  1.00 31.52  ? 422 LEU   A CA  1 
ATOM   468  C  C   . LEU   A 1 58  ? -24.727 33.373  33.091  1.00 33.56  ? 422 LEU   A C   1 
ATOM   469  O  O   . LEU   A 1 58  ? -25.167 32.835  34.097  1.00 31.83  ? 422 LEU   A O   1 
ATOM   470  C  CB  . LEU   A 1 58  ? -26.798 34.083  31.861  1.00 30.04  ? 422 LEU   A CB  1 
ATOM   471  C  CG  . LEU   A 1 58  ? -27.812 35.160  31.515  1.00 29.25  ? 422 LEU   A CG  1 
ATOM   472  C  CD1 . LEU   A 1 58  ? -28.992 34.571  30.768  1.00 29.16  ? 422 LEU   A CD1 1 
ATOM   473  C  CD2 . LEU   A 1 58  ? -28.280 35.883  32.763  1.00 31.18  ? 422 LEU   A CD2 1 
ATOM   474  N  N   . GLN   A 1 59  ? -23.668 32.902  32.426  1.00 29.60  ? 423 GLN   A N   1 
ATOM   475  C  CA  . GLN   A 1 59  ? -22.997 31.656  32.831  1.00 31.51  ? 423 GLN   A CA  1 
ATOM   476  C  C   . GLN   A 1 59  ? -21.485 31.785  32.628  1.00 34.12  ? 423 GLN   A C   1 
ATOM   477  O  O   . GLN   A 1 59  ? -21.100 32.458  31.691  1.00 32.55  ? 423 GLN   A O   1 
ATOM   478  C  CB  . GLN   A 1 59  ? -23.462 30.432  32.039  1.00 32.68  ? 423 GLN   A CB  1 
ATOM   479  C  CG  . GLN   A 1 59  ? -24.970 30.272  31.942  1.00 34.54  ? 423 GLN   A CG  1 
ATOM   480  C  CD  . GLN   A 1 59  ? -25.291 28.905  31.396  1.00 35.13  ? 423 GLN   A CD  1 
ATOM   481  O  OE1 . GLN   A 1 59  ? -25.399 28.718  30.182  1.00 37.06  ? 423 GLN   A OE1 1 
ATOM   482  N  NE2 . GLN   A 1 59  ? -25.393 27.933  32.290  1.00 32.42  ? 423 GLN   A NE2 1 
ATOM   483  N  N   . ASP   A 1 60  ? -20.696 31.078  33.436  1.00 37.33  ? 424 ASP   A N   1 
ATOM   484  C  CA  . ASP   A 1 60  ? -19.264 30.820  33.147  1.00 42.16  ? 424 ASP   A CA  1 
ATOM   485  C  C   . ASP   A 1 60  ? -19.139 29.386  32.633  1.00 36.65  ? 424 ASP   A C   1 
ATOM   486  O  O   . ASP   A 1 60  ? -18.467 29.173  31.619  1.00 39.75  ? 424 ASP   A O   1 
ATOM   487  C  CB  . ASP   A 1 60  ? -18.385 31.072  34.377  1.00 45.50  ? 424 ASP   A CB  1 
ATOM   488  C  CG  . ASP   A 1 60  ? -18.408 32.522  34.814  1.00 44.55  ? 424 ASP   A CG  1 
ATOM   489  O  OD1 . ASP   A 1 60  ? -18.332 33.385  33.933  1.00 48.79  ? 424 ASP   A OD1 1 
ATOM   490  O  OD2 . ASP   A 1 60  ? -18.580 32.764  36.025  1.00 46.09  ? 424 ASP   A OD2 1 
ATOM   491  N  N   . ASP   A 1 61  ? -19.764 28.440  33.323  1.00 35.14  ? 425 ASP   A N   1 
ATOM   492  C  CA  . ASP   A 1 61  ? -19.658 26.994  33.050  1.00 34.85  ? 425 ASP   A CA  1 
ATOM   493  C  C   . ASP   A 1 61  ? -21.057 26.408  33.119  1.00 36.57  ? 425 ASP   A C   1 
ATOM   494  O  O   . ASP   A 1 61  ? -21.644 26.443  34.195  1.00 36.85  ? 425 ASP   A O   1 
ATOM   495  C  CB  . ASP   A 1 61  ? -18.707 26.354  34.060  1.00 38.70  ? 425 ASP   A CB  1 
ATOM   496  C  CG  . ASP   A 1 61  ? -17.342 27.022  33.980  1.00 42.38  ? 425 ASP   A CG  1 
ATOM   497  O  OD1 . ASP   A 1 61  ? -16.550 26.641  33.102  1.00 45.32  ? 425 ASP   A OD1 1 
ATOM   498  O  OD2 . ASP   A 1 61  ? -17.129 27.956  34.738  1.00 45.19  ? 425 ASP   A OD2 1 
ATOM   499  N  N   . GLY   A 1 62  ? -21.599 25.899  32.025  1.00 32.87  ? 426 GLY   A N   1 
ATOM   500  C  CA  . GLY   A 1 62  ? -22.875 25.193  32.204  1.00 32.75  ? 426 GLY   A CA  1 
ATOM   501  C  C   . GLY   A 1 62  ? -23.628 24.992  30.923  1.00 31.33  ? 426 GLY   A C   1 
ATOM   502  O  O   . GLY   A 1 62  ? -23.018 25.078  29.843  1.00 27.19  ? 426 GLY   A O   1 
ATOM   503  N  N   . PHE   A 1 63  ? -24.931 24.733  31.062  1.00 28.60  ? 427 PHE   A N   1 
ATOM   504  C  CA  . PHE   A 1 63  ? -25.765 24.294  29.926  1.00 30.93  ? 427 PHE   A CA  1 
ATOM   505  C  C   . PHE   A 1 63  ? -26.837 25.334  29.619  1.00 26.63  ? 427 PHE   A C   1 
ATOM   506  O  O   . PHE   A 1 63  ? -27.344 25.991  30.550  1.00 26.54  ? 427 PHE   A O   1 
ATOM   507  C  CB  . PHE   A 1 63  ? -26.337 22.902  30.220  1.00 28.24  ? 427 PHE   A CB  1 
ATOM   508  C  CG  . PHE   A 1 63  ? -25.249 21.865  30.349  1.00 32.84  ? 427 PHE   A CG  1 
ATOM   509  C  CD1 . PHE   A 1 63  ? -24.622 21.341  29.217  1.00 36.69  ? 427 PHE   A CD1 1 
ATOM   510  C  CD2 . PHE   A 1 63  ? -24.834 21.426  31.596  1.00 33.77  ? 427 PHE   A CD2 1 
ATOM   511  C  CE1 . PHE   A 1 63  ? -23.626 20.376  29.330  1.00 36.74  ? 427 PHE   A CE1 1 
ATOM   512  C  CE2 . PHE   A 1 63  ? -23.851 20.453  31.715  1.00 33.23  ? 427 PHE   A CE2 1 
ATOM   513  C  CZ  . PHE   A 1 63  ? -23.245 19.931  30.581  1.00 34.97  ? 427 PHE   A CZ  1 
ATOM   514  N  N   . LEU   A 1 64  ? -27.184 25.387  28.336  1.00 26.06  ? 428 LEU   A N   1 
ATOM   515  C  CA  . LEU   A 1 64  ? -28.249 26.219  27.739  1.00 28.12  ? 428 LEU   A CA  1 
ATOM   516  C  C   . LEU   A 1 64  ? -29.254 25.303  27.071  1.00 26.81  ? 428 LEU   A C   1 
ATOM   517  O  O   . LEU   A 1 64  ? -28.851 24.457  26.262  1.00 25.89  ? 428 LEU   A O   1 
ATOM   518  C  CB  . LEU   A 1 64  ? -27.699 27.134  26.653  1.00 28.69  ? 428 LEU   A CB  1 
ATOM   519  C  CG  . LEU   A 1 64  ? -28.780 27.802  25.799  1.00 30.07  ? 428 LEU   A CG  1 
ATOM   520  C  CD1 . LEU   A 1 64  ? -29.480 28.859  26.631  1.00 28.41  ? 428 LEU   A CD1 1 
ATOM   521  C  CD2 . LEU   A 1 64  ? -28.159 28.450  24.565  1.00 35.27  ? 428 LEU   A CD2 1 
ATOM   522  N  N   . PHE   A 1 65  ? -30.517 25.443  27.426  1.00 24.10  ? 429 PHE   A N   1 
ATOM   523  C  CA  . PHE   A 1 65  ? -31.615 24.714  26.756  1.00 25.06  ? 429 PHE   A CA  1 
ATOM   524  C  C   . PHE   A 1 65  ? -32.356 25.730  25.909  1.00 23.35  ? 429 PHE   A C   1 
ATOM   525  O  O   . PHE   A 1 65  ? -32.957 26.624  26.515  1.00 24.90  ? 429 PHE   A O   1 
ATOM   526  C  CB  . PHE   A 1 65  ? -32.488 24.011  27.807  1.00 26.60  ? 429 PHE   A CB  1 
ATOM   527  C  CG  . PHE   A 1 65  ? -31.780 22.885  28.499  1.00 25.37  ? 429 PHE   A CG  1 
ATOM   528  C  CD1 . PHE   A 1 65  ? -30.802 23.139  29.447  1.00 24.63  ? 429 PHE   A CD1 1 
ATOM   529  C  CD2 . PHE   A 1 65  ? -32.095 21.572  28.210  1.00 24.24  ? 429 PHE   A CD2 1 
ATOM   530  C  CE1 . PHE   A 1 65  ? -30.136 22.101  30.069  1.00 23.38  ? 429 PHE   A CE1 1 
ATOM   531  C  CE2 . PHE   A 1 65  ? -31.412 20.538  28.822  1.00 24.74  ? 429 PHE   A CE2 1 
ATOM   532  C  CZ  . PHE   A 1 65  ? -30.440 20.803  29.754  1.00 23.55  ? 429 PHE   A CZ  1 
ATOM   533  N  N   . LEU   A 1 66  ? -32.359 25.580  24.583  1.00 22.56  ? 430 LEU   A N   1 
ATOM   534  C  CA  . LEU   A 1 66  ? -32.943 26.594  23.665  1.00 23.57  ? 430 LEU   A CA  1 
ATOM   535  C  C   . LEU   A 1 66  ? -33.996 25.949  22.773  1.00 22.91  ? 430 LEU   A C   1 
ATOM   536  O  O   . LEU   A 1 66  ? -33.626 25.203  21.840  1.00 24.35  ? 430 LEU   A O   1 
ATOM   537  C  CB  . LEU   A 1 66  ? -31.831 27.262  22.837  1.00 24.21  ? 430 LEU   A CB  1 
ATOM   538  C  CG  . LEU   A 1 66  ? -32.273 28.336  21.845  1.00 23.55  ? 430 LEU   A CG  1 
ATOM   539  C  CD1 . LEU   A 1 66  ? -32.858 29.518  22.582  1.00 23.62  ? 430 LEU   A CD1 1 
ATOM   540  C  CD2 . LEU   A 1 66  ? -31.114 28.800  20.961  1.00 23.32  ? 430 LEU   A CD2 1 
ATOM   541  N  N   . TRP   A 1 67  ? -35.266 26.231  23.039  1.00 22.06  ? 431 TRP   A N   1 
ATOM   542  C  CA  . TRP   A 1 67  ? -36.383 25.710  22.208  1.00 24.20  ? 431 TRP   A CA  1 
ATOM   543  C  C   . TRP   A 1 67  ? -36.324 26.376  20.842  1.00 25.88  ? 431 TRP   A C   1 
ATOM   544  O  O   . TRP   A 1 67  ? -36.137 27.586  20.812  1.00 24.85  ? 431 TRP   A O   1 
ATOM   545  C  CB  . TRP   A 1 67  ? -37.736 25.902  22.917  1.00 25.36  ? 431 TRP   A CB  1 
ATOM   546  C  CG  . TRP   A 1 67  ? -37.814 25.118  24.189  1.00 25.09  ? 431 TRP   A CG  1 
ATOM   547  C  CD1 . TRP   A 1 67  ? -37.397 25.520  25.429  1.00 25.37  ? 431 TRP   A CD1 1 
ATOM   548  C  CD2 . TRP   A 1 67  ? -38.249 23.750  24.342  1.00 24.85  ? 431 TRP   A CD2 1 
ATOM   549  N  NE1 . TRP   A 1 67  ? -37.574 24.506  26.327  1.00 25.20  ? 431 TRP   A NE1 1 
ATOM   550  C  CE2 . TRP   A 1 67  ? -38.109 23.421  25.694  1.00 22.97  ? 431 TRP   A CE2 1 
ATOM   551  C  CE3 . TRP   A 1 67  ? -38.754 22.790  23.467  1.00 28.27  ? 431 TRP   A CE3 1 
ATOM   552  C  CZ2 . TRP   A 1 67  ? -38.394 22.150  26.192  1.00 25.93  ? 431 TRP   A CZ2 1 
ATOM   553  C  CZ3 . TRP   A 1 67  ? -39.077 21.546  23.960  1.00 23.82  ? 431 TRP   A CZ3 1 
ATOM   554  C  CH2 . TRP   A 1 67  ? -38.909 21.243  25.302  1.00 25.41  ? 431 TRP   A CH2 1 
ATOM   555  N  N   . VAL   A 1 68  ? -36.486 25.599  19.762  1.00 23.32  ? 432 VAL   A N   1 
ATOM   556  C  CA  . VAL   A 1 68  ? -36.395 26.046  18.351  1.00 24.77  ? 432 VAL   A CA  1 
ATOM   557  C  C   . VAL   A 1 68  ? -37.494 25.368  17.530  1.00 27.51  ? 432 VAL   A C   1 
ATOM   558  O  O   . VAL   A 1 68  ? -37.866 24.247  17.810  1.00 27.77  ? 432 VAL   A O   1 
ATOM   559  C  CB  . VAL   A 1 68  ? -34.984 25.776  17.780  1.00 25.89  ? 432 VAL   A CB  1 
ATOM   560  C  CG1 . VAL   A 1 68  ? -33.942 26.569  18.518  1.00 24.50  ? 432 VAL   A CG1 1 
ATOM   561  C  CG2 . VAL   A 1 68  ? -34.586 24.316  17.823  1.00 25.69  ? 432 VAL   A CG2 1 
ATOM   562  N  N   . THR   A 1 69  ? -38.016 26.090  16.559  1.00 26.26  ? 433 THR   A N   1 
ATOM   563  C  CA  . THR   A 1 69  ? -39.052 25.639  15.629  1.00 30.51  ? 433 THR   A CA  1 
ATOM   564  C  C   . THR   A 1 69  ? -38.775 26.297  14.288  1.00 28.00  ? 433 THR   A C   1 
ATOM   565  O  O   . THR   A 1 69  ? -38.234 27.435  14.295  1.00 27.29  ? 433 THR   A O   1 
ATOM   566  C  CB  . THR   A 1 69  ? -40.440 25.983  16.187  1.00 34.07  ? 433 THR   A CB  1 
ATOM   567  O  OG1 . THR   A 1 69  ? -41.328 25.330  15.289  1.00 36.63  ? 433 THR   A OG1 1 
ATOM   568  C  CG2 . THR   A 1 69  ? -40.712 27.466  16.191  1.00 37.69  ? 433 THR   A CG2 1 
ATOM   569  N  N   . GLY   A 1 70  ? -39.138 25.618  13.196  1.00 30.41  ? 434 GLY   A N   1 
ATOM   570  C  CA  . GLY   A 1 70  ? -39.105 26.165  11.826  1.00 30.68  ? 434 GLY   A CA  1 
ATOM   571  C  C   . GLY   A 1 70  ? -37.727 26.733  11.532  1.00 29.28  ? 434 GLY   A C   1 
ATOM   572  O  O   . GLY   A 1 70  ? -36.740 26.093  11.864  1.00 26.30  ? 434 GLY   A O   1 
ATOM   573  N  N   . ARG   A 1 71  ? -37.654 27.927  10.963  1.00 30.75  ? 435 ARG   A N   1 
ATOM   574  C  CA  . ARG   A 1 71  ? -36.350 28.506  10.562  1.00 30.45  ? 435 ARG   A CA  1 
ATOM   575  C  C   . ARG   A 1 71  ? -35.452 28.735  11.788  1.00 27.92  ? 435 ARG   A C   1 
ATOM   576  O  O   . ARG   A 1 71  ? -34.229 28.892  11.570  1.00 28.86  ? 435 ARG   A O   1 
ATOM   577  C  CB  . ARG   A 1 71  ? -36.501 29.826  9.796   1.00 31.00  ? 435 ARG   A CB  1 
ATOM   578  C  CG  . ARG   A 1 71  ? -37.206 30.932  10.567  1.00 33.86  ? 435 ARG   A CG  1 
ATOM   579  C  CD  . ARG   A 1 71  ? -37.404 32.171  9.695   1.00 34.58  ? 435 ARG   A CD  1 
ATOM   580  N  NE  . ARG   A 1 71  ? -36.131 32.808  9.455   1.00 37.95  ? 435 ARG   A NE  1 
ATOM   581  C  CZ  . ARG   A 1 71  ? -35.549 33.711  10.257  1.00 38.90  ? 435 ARG   A CZ  1 
ATOM   582  N  NH1 . ARG   A 1 71  ? -34.375 34.222  9.924   1.00 37.79  ? 435 ARG   A NH1 1 
ATOM   583  N  NH2 . ARG   A 1 71  ? -36.137 34.118  11.368  1.00 36.54  ? 435 ARG   A NH2 1 
ATOM   584  N  N   . ALA   A 1 72  ? -36.006 28.762  13.003  1.00 23.88  ? 436 ALA   A N   1 
ATOM   585  C  CA  . ALA   A 1 72  ? -35.209 28.950  14.232  1.00 26.16  ? 436 ALA   A CA  1 
ATOM   586  C  C   . ALA   A 1 72  ? -34.407 27.686  14.544  1.00 24.23  ? 436 ALA   A C   1 
ATOM   587  O  O   . ALA   A 1 72  ? -33.479 27.741  15.353  1.00 24.96  ? 436 ALA   A O   1 
ATOM   588  C  CB  . ALA   A 1 72  ? -36.068 29.385  15.375  1.00 26.13  ? 436 ALA   A CB  1 
ATOM   589  N  N   . MET   A 1 73  ? -34.641 26.565  13.864  1.00 25.89  ? 437 MET   A N   1 
ATOM   590  C  CA  . MET   A 1 73  ? -33.688 25.434  14.027  1.00 24.90  ? 437 MET   A CA  1 
ATOM   591  C  C   . MET   A 1 73  ? -32.289 25.873  13.588  1.00 24.86  ? 437 MET   A C   1 
ATOM   592  O  O   . MET   A 1 73  ? -31.260 25.425  14.205  1.00 26.20  ? 437 MET   A O   1 
ATOM   593  C  CB  . MET   A 1 73  ? -34.166 24.220  13.226  1.00 27.21  ? 437 MET   A CB  1 
ATOM   594  C  CG  . MET   A 1 73  ? -35.440 23.622  13.824  1.00 28.40  ? 437 MET   A CG  1 
ATOM   595  S  SD  . MET   A 1 73  ? -35.762 22.032  12.997  1.00 33.47  ? 437 MET   A SD  1 
ATOM   596  C  CE  . MET   A 1 73  ? -36.994 21.387  14.123  1.00 39.41  ? 437 MET   A CE  1 
ATOM   597  N  N   . GLU   A 1 74  ? -32.226 26.737  12.583  1.00 26.49  ? 438 GLU   A N   1 
ATOM   598  C  CA  . GLU   A 1 74  ? -30.958 27.284  12.042  1.00 25.63  ? 438 GLU   A CA  1 
ATOM   599  C  C   . GLU   A 1 74  ? -30.591 28.580  12.801  1.00 24.38  ? 438 GLU   A C   1 
ATOM   600  O  O   . GLU   A 1 74  ? -29.469 28.675  13.294  1.00 24.34  ? 438 GLU   A O   1 
ATOM   601  C  CB  . GLU   A 1 74  ? -31.126 27.479  10.536  1.00 25.14  ? 438 GLU   A CB  1 
ATOM   602  C  CG  . GLU   A 1 74  ? -31.095 26.186  9.729   1.00 27.67  ? 438 GLU   A CG  1 
ATOM   603  C  CD  . GLU   A 1 74  ? -32.353 25.325  9.819   1.00 29.58  ? 438 GLU   A CD  1 
ATOM   604  O  OE1 . GLU   A 1 74  ? -33.460 25.860  9.850   1.00 30.20  ? 438 GLU   A OE1 1 
ATOM   605  O  OE2 . GLU   A 1 74  ? -32.227 24.106  9.854   1.00 34.41  ? 438 GLU   A OE2 1 
ATOM   606  N  N   . LEU   A 1 75  ? -31.534 29.478  13.031  1.00 26.38  ? 439 LEU   A N   1 
ATOM   607  C  CA  . LEU   A 1 75  ? -31.195 30.762  13.732  1.00 26.24  ? 439 LEU   A CA  1 
ATOM   608  C  C   . LEU   A 1 75  ? -30.778 30.451  15.163  1.00 27.77  ? 439 LEU   A C   1 
ATOM   609  O  O   . LEU   A 1 75  ? -29.822 31.093  15.651  1.00 26.67  ? 439 LEU   A O   1 
ATOM   610  C  CB  . LEU   A 1 75  ? -32.365 31.740  13.676  1.00 27.42  ? 439 LEU   A CB  1 
ATOM   611  C  CG  . LEU   A 1 75  ? -32.139 33.084  14.380  1.00 31.57  ? 439 LEU   A CG  1 
ATOM   612  C  CD1 . LEU   A 1 75  ? -30.923 33.792  13.801  1.00 34.02  ? 439 LEU   A CD1 1 
ATOM   613  C  CD2 . LEU   A 1 75  ? -33.381 33.960  14.270  1.00 31.54  ? 439 LEU   A CD2 1 
ATOM   614  N  N   . GLY   A 1 76  ? -31.450 29.501  15.831  1.00 26.39  ? 440 GLY   A N   1 
ATOM   615  C  CA  . GLY   A 1 76  ? -31.109 29.135  17.211  1.00 24.85  ? 440 GLY   A CA  1 
ATOM   616  C  C   . GLY   A 1 76  ? -29.695 28.607  17.307  1.00 23.87  ? 440 GLY   A C   1 
ATOM   617  O  O   . GLY   A 1 76  ? -29.017 28.857  18.303  1.00 24.09  ? 440 GLY   A O   1 
ATOM   618  N  N   . ARG   A 1 77  ? -29.273 27.799  16.330  1.00 24.95  ? 441 ARG   A N   1 
ATOM   619  C  CA  . ARG   A 1 77  ? -27.880 27.300  16.239  1.00 23.95  ? 441 ARG   A CA  1 
ATOM   620  C  C   . ARG   A 1 77  ? -26.915 28.484  16.104  1.00 22.69  ? 441 ARG   A C   1 
ATOM   621  O  O   . ARG   A 1 77  ? -25.905 28.499  16.788  1.00 23.95  ? 441 ARG   A O   1 
ATOM   622  C  CB  . ARG   A 1 77  ? -27.718 26.353  15.049  1.00 23.60  ? 441 ARG   A CB  1 
ATOM   623  C  CG  . ARG   A 1 77  ? -28.186 24.938  15.351  1.00 24.00  ? 441 ARG   A CG  1 
ATOM   624  C  CD  . ARG   A 1 77  ? -28.183 24.024  14.129  1.00 23.51  ? 441 ARG   A CD  1 
ATOM   625  N  NE  . ARG   A 1 77  ? -28.265 22.642  14.573  1.00 24.00  ? 441 ARG   A NE  1 
ATOM   626  C  CZ  . ARG   A 1 77  ? -29.388 21.996  14.900  1.00 24.09  ? 441 ARG   A CZ  1 
ATOM   627  N  NH1 . ARG   A 1 77  ? -30.565 22.566  14.793  1.00 24.12  ? 441 ARG   A NH1 1 
ATOM   628  N  NH2 . ARG   A 1 77  ? -29.328 20.764  15.364  1.00 24.83  ? 441 ARG   A NH2 1 
ATOM   629  N  N   . GLU   A 1 78  ? -27.254 29.448  15.266  1.00 24.27  ? 442 GLU   A N   1 
ATOM   630  C  CA  . GLU   A 1 78  ? -26.407 30.670  15.111  1.00 26.24  ? 442 GLU   A CA  1 
ATOM   631  C  C   . GLU   A 1 78  ? -26.292 31.407  16.465  1.00 25.55  ? 442 GLU   A C   1 
ATOM   632  O  O   . GLU   A 1 78  ? -25.144 31.743  16.907  1.00 27.25  ? 442 GLU   A O   1 
ATOM   633  C  CB  . GLU   A 1 78  ? -26.995 31.535  14.008  1.00 27.58  ? 442 GLU   A CB  1 
ATOM   634  C  CG  . GLU   A 1 78  ? -26.296 32.883  13.931  1.00 28.54  ? 442 GLU   A CG  1 
ATOM   635  C  CD  . GLU   A 1 78  ? -26.648 33.626  12.661  1.00 31.13  ? 442 GLU   A CD  1 
ATOM   636  O  OE1 . GLU   A 1 78  ? -26.967 32.967  11.627  1.00 29.33  ? 442 GLU   A OE1 1 
ATOM   637  O  OE2 . GLU   A 1 78  ? -26.658 34.845  12.746  1.00 33.94  ? 442 GLU   A OE2 1 
ATOM   638  N  N   . CYS   A 1 79  ? -27.429 31.641  17.126  1.00 26.14  ? 443 CYS   A N   1 
ATOM   639  C  CA  . CYS   A 1 79  ? -27.472 32.355  18.415  1.00 25.38  ? 443 CYS   A CA  1 
ATOM   640  C  C   . CYS   A 1 79  ? -26.642 31.594  19.415  1.00 26.03  ? 443 CYS   A C   1 
ATOM   641  O  O   . CYS   A 1 79  ? -25.814 32.203  20.137  1.00 23.79  ? 443 CYS   A O   1 
ATOM   642  C  CB  . CYS   A 1 79  ? -28.887 32.535  18.926  1.00 26.57  ? 443 CYS   A CB  1 
ATOM   643  S  SG  . CYS   A 1 79  ? -29.825 33.729  17.970  1.00 29.13  ? 443 CYS   A SG  1 
ATOM   644  N  N   . LEU   A 1 80  ? -26.891 30.283  19.502  1.00 27.33  ? 444 LEU   A N   1 
ATOM   645  C  CA  . LEU   A 1 80  ? -26.186 29.449  20.468  1.00 26.09  ? 444 LEU   A CA  1 
ATOM   646  C  C   . LEU   A 1 80  ? -24.686 29.673  20.268  1.00 26.01  ? 444 LEU   A C   1 
ATOM   647  O  O   . LEU   A 1 80  ? -23.977 29.875  21.280  1.00 26.41  ? 444 LEU   A O   1 
ATOM   648  C  CB  . LEU   A 1 80  ? -26.656 28.013  20.190  1.00 32.62  ? 444 LEU   A CB  1 
ATOM   649  C  CG  . LEU   A 1 80  ? -26.129 26.947  21.118  1.00 34.37  ? 444 LEU   A CG  1 
ATOM   650  C  CD1 . LEU   A 1 80  ? -27.118 25.796  21.284  1.00 33.15  ? 444 LEU   A CD1 1 
ATOM   651  C  CD2 . LEU   A 1 80  ? -24.810 26.416  20.579  1.00 35.51  ? 444 LEU   A CD2 1 
ATOM   652  N  N   . ASN   A 1 81  ? -24.201 29.642  19.015  1.00 28.81  ? 445 ASN   A N   1 
ATOM   653  C  CA  . ASN   A 1 81  ? -22.728 29.731  18.754  1.00 27.34  ? 445 ASN   A CA  1 
ATOM   654  C  C   . ASN   A 1 81  ? -22.267 31.172  19.051  1.00 25.51  ? 445 ASN   A C   1 
ATOM   655  O  O   . ASN   A 1 81  ? -21.197 31.342  19.683  1.00 28.46  ? 445 ASN   A O   1 
ATOM   656  C  CB  . ASN   A 1 81  ? -22.316 29.264  17.348  1.00 28.99  ? 445 ASN   A CB  1 
ATOM   657  C  CG  . ASN   A 1 81  ? -22.413 27.757  17.151  1.00 28.90  ? 445 ASN   A CG  1 
ATOM   658  O  OD1 . ASN   A 1 81  ? -22.276 26.955  18.082  1.00 32.26  ? 445 ASN   A OD1 1 
ATOM   659  N  ND2 . ASN   A 1 81  ? -22.720 27.342  15.952  1.00 31.99  ? 445 ASN   A ND2 1 
ATOM   660  N  N   . LEU   A 1 82  ? -23.012 32.151  18.556  1.00 25.87  ? 446 LEU   A N   1 
ATOM   661  C  CA  . LEU   A 1 82  ? -22.733 33.581  18.828  1.00 29.69  ? 446 LEU   A CA  1 
ATOM   662  C  C   . LEU   A 1 82  ? -22.591 33.808  20.339  1.00 31.67  ? 446 LEU   A C   1 
ATOM   663  O  O   . LEU   A 1 82  ? -21.617 34.468  20.733  1.00 31.14  ? 446 LEU   A O   1 
ATOM   664  C  CB  . LEU   A 1 82  ? -23.832 34.434  18.204  1.00 32.59  ? 446 LEU   A CB  1 
ATOM   665  C  CG  . LEU   A 1 82  ? -23.691 35.929  18.477  1.00 41.10  ? 446 LEU   A CG  1 
ATOM   666  C  CD1 . LEU   A 1 82  ? -22.397 36.451  17.864  1.00 49.84  ? 446 LEU   A CD1 1 
ATOM   667  C  CD2 . LEU   A 1 82  ? -24.888 36.701  17.933  1.00 46.43  ? 446 LEU   A CD2 1 
ATOM   668  N  N   . TRP   A 1 83  ? -23.464 33.230  21.183  1.00 28.45  ? 447 TRP   A N   1 
ATOM   669  C  CA  . TRP   A 1 83  ? -23.445 33.445  22.655  1.00 29.61  ? 447 TRP   A CA  1 
ATOM   670  C  C   . TRP   A 1 83  ? -22.323 32.675  23.346  1.00 29.35  ? 447 TRP   A C   1 
ATOM   671  O  O   . TRP   A 1 83  ? -22.170 32.854  24.563  1.00 30.72  ? 447 TRP   A O   1 
ATOM   672  C  CB  . TRP   A 1 83  ? -24.803 33.072  23.234  1.00 29.18  ? 447 TRP   A CB  1 
ATOM   673  C  CG  . TRP   A 1 83  ? -25.946 33.872  22.709  1.00 25.70  ? 447 TRP   A CG  1 
ATOM   674  C  CD1 . TRP   A 1 83  ? -25.966 35.164  22.252  1.00 26.47  ? 447 TRP   A CD1 1 
ATOM   675  C  CD2 . TRP   A 1 83  ? -27.300 33.426  22.696  1.00 26.75  ? 447 TRP   A CD2 1 
ATOM   676  N  NE1 . TRP   A 1 83  ? -27.240 35.525  21.911  1.00 24.23  ? 447 TRP   A NE1 1 
ATOM   677  C  CE2 . TRP   A 1 83  ? -28.083 34.482  22.198  1.00 25.90  ? 447 TRP   A CE2 1 
ATOM   678  C  CE3 . TRP   A 1 83  ? -27.912 32.206  23.022  1.00 27.42  ? 447 TRP   A CE3 1 
ATOM   679  C  CZ2 . TRP   A 1 83  ? -29.457 34.364  22.037  1.00 25.92  ? 447 TRP   A CZ2 1 
ATOM   680  C  CZ3 . TRP   A 1 83  ? -29.269 32.108  22.880  1.00 23.96  ? 447 TRP   A CZ3 1 
ATOM   681  C  CH2 . TRP   A 1 83  ? -30.026 33.158  22.378  1.00 26.28  ? 447 TRP   A CH2 1 
ATOM   682  N  N   . GLY   A 1 84  ? -21.563 31.845  22.602  1.00 27.32  ? 448 GLY   A N   1 
ATOM   683  C  CA  . GLY   A 1 84  ? -20.364 31.136  23.083  1.00 26.99  ? 448 GLY   A CA  1 
ATOM   684  C  C   . GLY   A 1 84  ? -20.646 29.710  23.533  1.00 28.07  ? 448 GLY   A C   1 
ATOM   685  O  O   . GLY   A 1 84  ? -19.882 29.190  24.341  1.00 28.38  ? 448 GLY   A O   1 
ATOM   686  N  N   . TYR   A 1 85  ? -21.701 29.086  23.026  1.00 27.51  ? 449 TYR   A N   1 
ATOM   687  C  CA  . TYR   A 1 85  ? -22.032 27.677  23.328  1.00 28.52  ? 449 TYR   A CA  1 
ATOM   688  C  C   . TYR   A 1 85  ? -21.689 26.797  22.125  1.00 25.63  ? 449 TYR   A C   1 
ATOM   689  O  O   . TYR   A 1 85  ? -21.749 27.267  20.997  1.00 30.28  ? 449 TYR   A O   1 
ATOM   690  C  CB  . TYR   A 1 85  ? -23.519 27.544  23.672  1.00 25.41  ? 449 TYR   A CB  1 
ATOM   691  C  CG  . TYR   A 1 85  ? -23.920 28.271  24.923  1.00 23.37  ? 449 TYR   A CG  1 
ATOM   692  C  CD1 . TYR   A 1 85  ? -24.105 29.640  24.944  1.00 26.40  ? 449 TYR   A CD1 1 
ATOM   693  C  CD2 . TYR   A 1 85  ? -24.059 27.583  26.118  1.00 23.47  ? 449 TYR   A CD2 1 
ATOM   694  C  CE1 . TYR   A 1 85  ? -24.427 30.303  26.121  1.00 26.82  ? 449 TYR   A CE1 1 
ATOM   695  C  CE2 . TYR   A 1 85  ? -24.346 28.234  27.304  1.00 22.98  ? 449 TYR   A CE2 1 
ATOM   696  C  CZ  . TYR   A 1 85  ? -24.574 29.605  27.307  1.00 25.63  ? 449 TYR   A CZ  1 
ATOM   697  O  OH  . TYR   A 1 85  ? -24.887 30.259  28.483  1.00 28.59  ? 449 TYR   A OH  1 
ATOM   698  N  N   . GLU   A 1 86  ? -21.360 25.539  22.398  1.00 27.61  ? 450 GLU   A N   1 
ATOM   699  C  CA  . GLU   A 1 86  ? -21.319 24.426  21.408  1.00 25.58  ? 450 GLU   A CA  1 
ATOM   700  C  C   . GLU   A 1 86  ? -22.596 23.586  21.602  1.00 25.95  ? 450 GLU   A C   1 
ATOM   701  O  O   . GLU   A 1 86  ? -22.859 23.210  22.762  1.00 25.90  ? 450 GLU   A O   1 
ATOM   702  C  CB  . GLU   A 1 86  ? -20.045 23.614  21.642  1.00 28.51  ? 450 GLU   A CB  1 
ATOM   703  C  CG  . GLU   A 1 86  ? -19.915 22.448  20.661  1.00 33.72  ? 450 GLU   A CG  1 
ATOM   704  C  CD  . GLU   A 1 86  ? -18.784 21.458  20.917  1.00 36.17  ? 450 GLU   A CD  1 
ATOM   705  O  OE1 . GLU   A 1 86  ? -18.104 21.546  21.967  1.00 38.66  ? 450 GLU   A OE1 1 
ATOM   706  O  OE2 . GLU   A 1 86  ? -18.630 20.547  20.074  1.00 39.99  ? 450 GLU   A OE2 1 
ATOM   707  N  N   . ARG   A 1 87  ? -23.362 23.300  20.536  1.00 24.95  ? 451 ARG   A N   1 
ATOM   708  C  CA  . ARG   A 1 87  ? -24.553 22.394  20.660  1.00 25.65  ? 451 ARG   A CA  1 
ATOM   709  C  C   . ARG   A 1 87  ? -24.045 20.975  20.898  1.00 30.17  ? 451 ARG   A C   1 
ATOM   710  O  O   . ARG   A 1 87  ? -23.256 20.475  20.065  1.00 30.49  ? 451 ARG   A O   1 
ATOM   711  C  CB  . ARG   A 1 87  ? -25.448 22.421  19.429  1.00 26.67  ? 451 ARG   A CB  1 
ATOM   712  C  CG  . ARG   A 1 87  ? -26.771 21.685  19.639  1.00 24.96  ? 451 ARG   A CG  1 
ATOM   713  C  CD  . ARG   A 1 87  ? -27.528 21.337  18.365  1.00 27.17  ? 451 ARG   A CD  1 
ATOM   714  N  NE  . ARG   A 1 87  ? -26.665 20.455  17.625  1.00 26.06  ? 451 ARG   A NE  1 
ATOM   715  C  CZ  . ARG   A 1 87  ? -26.453 19.190  17.932  1.00 28.97  ? 451 ARG   A CZ  1 
ATOM   716  N  NH1 . ARG   A 1 87  ? -25.534 18.515  17.264  1.00 28.21  ? 451 ARG   A NH1 1 
ATOM   717  N  NH2 . ARG   A 1 87  ? -27.152 18.589  18.889  1.00 28.09  ? 451 ARG   A NH2 1 
ATOM   718  N  N   . VAL   A 1 88  ? -24.437 20.344  22.001  1.00 28.56  ? 452 VAL   A N   1 
ATOM   719  C  CA  . VAL   A 1 88  ? -23.966 18.961  22.317  1.00 28.39  ? 452 VAL   A CA  1 
ATOM   720  C  C   . VAL   A 1 88  ? -25.136 17.981  22.470  1.00 30.60  ? 452 VAL   A C   1 
ATOM   721  O  O   . VAL   A 1 88  ? -24.886 16.809  22.767  1.00 31.20  ? 452 VAL   A O   1 
ATOM   722  C  CB  . VAL   A 1 88  ? -23.091 18.964  23.577  1.00 29.14  ? 452 VAL   A CB  1 
ATOM   723  C  CG1 . VAL   A 1 88  ? -21.774 19.688  23.317  1.00 29.03  ? 452 VAL   A CG1 1 
ATOM   724  C  CG2 . VAL   A 1 88  ? -23.828 19.577  24.767  1.00 31.90  ? 452 VAL   A CG2 1 
ATOM   725  N  N   . ASP   A 1 89  ? -26.370 18.416  22.304  1.00 26.67  ? 453 ASP   A N   1 
ATOM   726  C  CA  . ASP   A 1 89  ? -27.502 17.472  22.390  1.00 27.99  ? 453 ASP   A CA  1 
ATOM   727  C  C   . ASP   A 1 89  ? -28.714 18.162  21.800  1.00 27.43  ? 453 ASP   A C   1 
ATOM   728  O  O   . ASP   A 1 89  ? -28.654 19.385  21.572  1.00 25.78  ? 453 ASP   A O   1 
ATOM   729  C  CB  . ASP   A 1 89  ? -27.673 16.933  23.812  1.00 28.73  ? 453 ASP   A CB  1 
ATOM   730  C  CG  . ASP   A 1 89  ? -27.270 15.465  23.996  1.00 33.17  ? 453 ASP   A CG  1 
ATOM   731  O  OD1 . ASP   A 1 89  ? -27.361 14.664  23.025  1.00 34.42  ? 453 ASP   A OD1 1 
ATOM   732  O  OD2 . ASP   A 1 89  ? -26.834 15.152  25.077  1.00 35.88  ? 453 ASP   A OD2 1 
ATOM   733  N  N   . GLU   A 1 90  ? -29.748 17.392  21.473  1.00 23.74  ? 454 GLU   A N   1 
ATOM   734  C  CA  . GLU   A 1 90  ? -30.990 17.967  20.947  1.00 24.28  ? 454 GLU   A CA  1 
ATOM   735  C  C   . GLU   A 1 90  ? -32.117 17.107  21.507  1.00 28.48  ? 454 GLU   A C   1 
ATOM   736  O  O   . GLU   A 1 90  ? -32.148 15.909  21.171  1.00 27.92  ? 454 GLU   A O   1 
ATOM   737  C  CB  . GLU   A 1 90  ? -30.983 18.018  19.435  1.00 24.71  ? 454 GLU   A CB  1 
ATOM   738  C  CG  . GLU   A 1 90  ? -32.281 18.496  18.833  1.00 24.91  ? 454 GLU   A CG  1 
ATOM   739  C  CD  . GLU   A 1 90  ? -32.147 19.043  17.435  1.00 22.93  ? 454 GLU   A CD  1 
ATOM   740  O  OE1 . GLU   A 1 90  ? -30.985 19.254  17.015  1.00 28.28  ? 454 GLU   A OE1 1 
ATOM   741  O  OE2 . GLU   A 1 90  ? -33.192 19.303  16.808  1.00 27.24  ? 454 GLU   A OE2 1 
ATOM   742  N  N   . ILE   A 1 91  ? -32.917 17.681  22.383  1.00 24.29  ? 455 ILE   A N   1 
ATOM   743  C  CA  . ILE   A 1 91  ? -34.088 16.980  22.988  1.00 25.76  ? 455 ILE   A CA  1 
ATOM   744  C  C   . ILE   A 1 91  ? -35.289 17.138  22.056  1.00 23.79  ? 455 ILE   A C   1 
ATOM   745  O  O   . ILE   A 1 91  ? -35.474 18.200  21.453  1.00 24.10  ? 455 ILE   A O   1 
ATOM   746  C  CB  . ILE   A 1 91  ? -34.411 17.511  24.393  1.00 27.67  ? 455 ILE   A CB  1 
ATOM   747  C  CG1 . ILE   A 1 91  ? -33.289 17.217  25.370  1.00 28.39  ? 455 ILE   A CG1 1 
ATOM   748  C  CG2 . ILE   A 1 91  ? -35.743 16.924  24.878  1.00 30.42  ? 455 ILE   A CG2 1 
ATOM   749  C  CD1 . ILE   A 1 91  ? -33.344 18.032  26.618  1.00 31.28  ? 455 ILE   A CD1 1 
ATOM   750  N  N   . ILE   A 1 92  ? -36.088 16.089  21.879  1.00 23.35  ? 456 ILE   A N   1 
ATOM   751  C  CA  . ILE   A 1 92  ? -37.385 16.263  21.198  1.00 25.72  ? 456 ILE   A CA  1 
ATOM   752  C  C   . ILE   A 1 92  ? -38.513 15.884  22.160  1.00 25.60  ? 456 ILE   A C   1 
ATOM   753  O  O   . ILE   A 1 92  ? -38.406 14.877  22.885  1.00 26.90  ? 456 ILE   A O   1 
ATOM   754  C  CB  . ILE   A 1 92  ? -37.459 15.539  19.854  1.00 28.52  ? 456 ILE   A CB  1 
ATOM   755  C  CG1 . ILE   A 1 92  ? -37.393 14.026  20.033  1.00 30.72  ? 456 ILE   A CG1 1 
ATOM   756  C  CG2 . ILE   A 1 92  ? -36.391 16.076  18.876  1.00 30.61  ? 456 ILE   A CG2 1 
ATOM   757  C  CD1 . ILE   A 1 92  ? -37.940 13.270  18.861  1.00 34.53  ? 456 ILE   A CD1 1 
ATOM   758  N  N   . TRP   A 1 93  ? -39.551 16.703  22.135  1.00 25.34  ? 457 TRP   A N   1 
ATOM   759  C  CA  . TRP   A 1 93  ? -40.799 16.492  22.890  1.00 27.11  ? 457 TRP   A CA  1 
ATOM   760  C  C   . TRP   A 1 93  ? -41.862 16.037  21.894  1.00 25.20  ? 457 TRP   A C   1 
ATOM   761  O  O   . TRP   A 1 93  ? -42.259 16.811  20.994  1.00 29.42  ? 457 TRP   A O   1 
ATOM   762  C  CB  . TRP   A 1 93  ? -41.187 17.759  23.661  1.00 30.92  ? 457 TRP   A CB  1 
ATOM   763  C  CG  . TRP   A 1 93  ? -42.594 17.741  24.160  1.00 30.79  ? 457 TRP   A CG  1 
ATOM   764  C  CD1 . TRP   A 1 93  ? -43.278 16.685  24.689  1.00 30.43  ? 457 TRP   A CD1 1 
ATOM   765  C  CD2 . TRP   A 1 93  ? -43.510 18.853  24.160  1.00 32.19  ? 457 TRP   A CD2 1 
ATOM   766  N  NE1 . TRP   A 1 93  ? -44.562 17.066  24.994  1.00 31.37  ? 457 TRP   A NE1 1 
ATOM   767  C  CE2 . TRP   A 1 93  ? -44.736 18.386  24.684  1.00 32.29  ? 457 TRP   A CE2 1 
ATOM   768  C  CE3 . TRP   A 1 93  ? -43.412 20.189  23.772  1.00 30.35  ? 457 TRP   A CE3 1 
ATOM   769  C  CZ2 . TRP   A 1 93  ? -45.842 19.224  24.857  1.00 36.27  ? 457 TRP   A CZ2 1 
ATOM   770  C  CZ3 . TRP   A 1 93  ? -44.506 21.008  23.925  1.00 34.35  ? 457 TRP   A CZ3 1 
ATOM   771  C  CH2 . TRP   A 1 93  ? -45.705 20.535  24.470  1.00 36.04  ? 457 TRP   A CH2 1 
ATOM   772  N  N   . VAL   A 1 94  ? -42.231 14.766  21.991  1.00 26.79  ? 458 VAL   A N   1 
ATOM   773  C  CA  . VAL   A 1 94  ? -43.384 14.190  21.262  1.00 28.36  ? 458 VAL   A CA  1 
ATOM   774  C  C   . VAL   A 1 94  ? -44.639 14.582  22.037  1.00 28.85  ? 458 VAL   A C   1 
ATOM   775  O  O   . VAL   A 1 94  ? -44.762 14.184  23.225  1.00 32.01  ? 458 VAL   A O   1 
ATOM   776  C  CB  . VAL   A 1 94  ? -43.257 12.660  21.124  1.00 32.12  ? 458 VAL   A CB  1 
ATOM   777  C  CG1 . VAL   A 1 94  ? -44.449 12.076  20.392  1.00 31.43  ? 458 VAL   A CG1 1 
ATOM   778  C  CG2 . VAL   A 1 94  ? -41.942 12.272  20.474  1.00 32.63  ? 458 VAL   A CG2 1 
ATOM   779  N  N   . LYS   A 1 95  ? -45.487 15.391  21.409  1.00 33.23  ? 459 LYS   A N   1 
ATOM   780  C  CA  . LYS   A 1 95  ? -46.720 15.943  22.005  1.00 36.06  ? 459 LYS   A CA  1 
ATOM   781  C  C   . LYS   A 1 95  ? -47.776 14.842  21.879  1.00 35.25  ? 459 LYS   A C   1 
ATOM   782  O  O   . LYS   A 1 95  ? -47.959 14.365  20.780  1.00 34.88  ? 459 LYS   A O   1 
ATOM   783  C  CB  . LYS   A 1 95  ? -47.109 17.231  21.274  1.00 40.68  ? 459 LYS   A CB  1 
ATOM   784  C  CG  . LYS   A 1 95  ? -46.005 18.286  21.195  1.00 45.30  ? 459 LYS   A CG  1 
ATOM   785  C  CD  . LYS   A 1 95  ? -46.140 19.243  20.026  1.00 47.74  ? 459 LYS   A CD  1 
ATOM   786  C  CE  . LYS   A 1 95  ? -47.266 20.236  20.201  1.00 53.27  ? 459 LYS   A CE  1 
ATOM   787  N  NZ  . LYS   A 1 95  ? -47.469 21.047  18.976  1.00 55.58  ? 459 LYS   A NZ  1 
ATOM   788  N  N   . THR   A 1 96  ? -48.366 14.406  22.986  1.00 39.17  ? 460 THR   A N   1 
ATOM   789  C  CA  . THR   A 1 96  ? -49.457 13.402  22.989  1.00 40.03  ? 460 THR   A CA  1 
ATOM   790  C  C   . THR   A 1 96  ? -50.719 13.988  23.620  1.00 43.06  ? 460 THR   A C   1 
ATOM   791  O  O   . THR   A 1 96  ? -50.625 15.051  24.276  1.00 40.60  ? 460 THR   A O   1 
ATOM   792  C  CB  . THR   A 1 96  ? -49.074 12.168  23.797  1.00 40.26  ? 460 THR   A CB  1 
ATOM   793  O  OG1 . THR   A 1 96  ? -49.070 12.536  25.171  1.00 43.76  ? 460 THR   A OG1 1 
ATOM   794  C  CG2 . THR   A 1 96  ? -47.723 11.603  23.421  1.00 46.05  ? 460 THR   A CG2 1 
ATOM   795  N  N   . ASN   A 1 97  ? -51.838 13.269  23.499  1.00 47.72  ? 461 ASN   A N   1 
ATOM   796  C  CA  . ASN   A 1 97  ? -53.056 13.514  24.326  1.00 49.28  ? 461 ASN   A CA  1 
ATOM   797  C  C   . ASN   A 1 97  ? -52.971 12.694  25.625  1.00 53.41  ? 461 ASN   A C   1 
ATOM   798  O  O   . ASN   A 1 97  ? -51.895 12.092  25.907  1.00 47.21  ? 461 ASN   A O   1 
ATOM   799  C  CB  . ASN   A 1 97  ? -54.322 13.234  23.517  1.00 47.48  ? 461 ASN   A CB  1 
ATOM   800  C  CG  . ASN   A 1 97  ? -54.403 11.814  23.004  1.00 46.87  ? 461 ASN   A CG  1 
ATOM   801  O  OD1 . ASN   A 1 97  ? -53.739 10.908  23.510  1.00 51.44  ? 461 ASN   A OD1 1 
ATOM   802  N  ND2 . ASN   A 1 97  ? -55.220 11.613  21.990  1.00 50.81  ? 461 ASN   A ND2 1 
ATOM   803  N  N   . GLN   A 1 98  ? -54.066 12.662  26.395  1.00 62.74  ? 462 GLN   A N   1 
ATOM   804  C  CA  . GLN   A 1 98  ? -54.183 11.904  27.673  1.00 63.80  ? 462 GLN   A CA  1 
ATOM   805  C  C   . GLN   A 1 98  ? -53.991 10.403  27.404  1.00 63.38  ? 462 GLN   A C   1 
ATOM   806  O  O   . GLN   A 1 98  ? -53.639 9.697   28.368  1.00 64.94  ? 462 GLN   A O   1 
ATOM   807  C  CB  . GLN   A 1 98  ? -55.530 12.136  28.383  1.00 70.77  ? 462 GLN   A CB  1 
ATOM   808  C  CG  . GLN   A 1 98  ? -55.827 13.573  28.831  1.00 77.05  ? 462 GLN   A CG  1 
ATOM   809  C  CD  . GLN   A 1 98  ? -54.790 14.205  29.738  1.00 86.21  ? 462 GLN   A CD  1 
ATOM   810  O  OE1 . GLN   A 1 98  ? -54.929 14.246  30.965  1.00 68.57  ? 462 GLN   A OE1 1 
ATOM   811  N  NE2 . GLN   A 1 98  ? -53.745 14.750  29.130  1.00 89.37  ? 462 GLN   A NE2 1 
ATOM   812  N  N   . LEU   A 1 99  ? -54.194 9.927   26.166  1.00 60.07  ? 463 LEU   A N   1 
ATOM   813  C  CA  . LEU   A 1 99  ? -54.124 8.474   25.815  1.00 65.79  ? 463 LEU   A CA  1 
ATOM   814  C  C   . LEU   A 1 99  ? -52.812 8.107   25.103  1.00 61.27  ? 463 LEU   A C   1 
ATOM   815  O  O   . LEU   A 1 99  ? -52.753 7.017   24.481  1.00 50.47  ? 463 LEU   A O   1 
ATOM   816  C  CB  . LEU   A 1 99  ? -55.338 8.118   24.954  1.00 73.54  ? 463 LEU   A CB  1 
ATOM   817  C  CG  . LEU   A 1 99  ? -56.699 8.290   25.641  1.00 78.89  ? 463 LEU   A CG  1 
ATOM   818  C  CD1 . LEU   A 1 99  ? -57.774 7.490   24.913  1.00 72.97  ? 463 LEU   A CD1 1 
ATOM   819  C  CD2 . LEU   A 1 99  ? -56.642 7.893   27.117  1.00 75.24  ? 463 LEU   A CD2 1 
ATOM   820  N  N   . GLN   A 1 100 ? -51.790 8.957   25.240  1.00 56.44  ? 464 GLN   A N   1 
ATOM   821  C  CA  . GLN   A 1 100 ? -50.412 8.750   24.716  1.00 53.70  ? 464 GLN   A CA  1 
ATOM   822  C  C   . GLN   A 1 100 ? -50.463 8.549   23.200  1.00 43.27  ? 464 GLN   A C   1 
ATOM   823  O  O   . GLN   A 1 100 ? -49.617 7.825   22.658  1.00 41.01  ? 464 GLN   A O   1 
ATOM   824  C  CB  . GLN   A 1 100 ? -49.724 7.595   25.445  1.00 52.52  ? 464 GLN   A CB  1 
ATOM   825  C  CG  . GLN   A 1 100 ? -49.200 7.991   26.820  1.00 59.33  ? 464 GLN   A CG  1 
ATOM   826  C  CD  . GLN   A 1 100 ? -50.322 8.428   27.728  1.00 65.98  ? 464 GLN   A CD  1 
ATOM   827  O  OE1 . GLN   A 1 100 ? -50.326 9.538   28.265  1.00 66.68  ? 464 GLN   A OE1 1 
ATOM   828  N  NE2 . GLN   A 1 100 ? -51.311 7.559   27.867  1.00 61.90  ? 464 GLN   A NE2 1 
ATOM   829  N  N   . ARG   A 1 101 ? -51.418 9.188   22.546  1.00 37.52  ? 465 ARG   A N   1 
ATOM   830  C  CA  . ARG   A 1 101 ? -51.498 9.248   21.068  1.00 47.16  ? 465 ARG   A CA  1 
ATOM   831  C  C   . ARG   A 1 101 ? -50.855 10.574  20.632  1.00 41.22  ? 465 ARG   A C   1 
ATOM   832  O  O   . ARG   A 1 101 ? -51.155 11.602  21.246  1.00 38.94  ? 465 ARG   A O   1 
ATOM   833  C  CB  . ARG   A 1 101 ? -52.956 9.111   20.614  1.00 52.28  ? 465 ARG   A CB  1 
ATOM   834  C  CG  . ARG   A 1 101 ? -53.154 8.209   19.403  1.00 64.03  ? 465 ARG   A CG  1 
ATOM   835  C  CD  . ARG   A 1 101 ? -54.495 7.497   19.442  1.00 76.30  ? 465 ARG   A CD  1 
ATOM   836  N  NE  . ARG   A 1 101 ? -54.437 6.295   20.271  1.00 86.33  ? 465 ARG   A NE  1 
ATOM   837  C  CZ  . ARG   A 1 101 ? -55.112 6.088   21.402  1.00 90.57  ? 465 ARG   A CZ  1 
ATOM   838  N  NH1 . ARG   A 1 101 ? -55.945 7.002   21.873  1.00 88.71  ? 465 ARG   A NH1 1 
ATOM   839  N  NH2 . ARG   A 1 101 ? -54.953 4.949   22.061  1.00 90.72  ? 465 ARG   A NH2 1 
ATOM   840  N  N   . ILE   A 1 102 ? -50.009 10.548  19.616  1.00 42.19  ? 466 ILE   A N   1 
ATOM   841  C  CA  . ILE   A 1 102 ? -49.321 11.767  19.095  1.00 43.78  ? 466 ILE   A CA  1 
ATOM   842  C  C   . ILE   A 1 102 ? -50.364 12.795  18.626  1.00 44.04  ? 466 ILE   A C   1 
ATOM   843  O  O   . ILE   A 1 102 ? -51.220 12.439  17.819  1.00 44.01  ? 466 ILE   A O   1 
ATOM   844  C  CB  . ILE   A 1 102 ? -48.339 11.404  17.964  1.00 43.59  ? 466 ILE   A CB  1 
ATOM   845  C  CG1 . ILE   A 1 102 ? -47.232 10.485  18.471  1.00 40.13  ? 466 ILE   A CG1 1 
ATOM   846  C  CG2 . ILE   A 1 102 ? -47.764 12.669  17.341  1.00 43.59  ? 466 ILE   A CG2 1 
ATOM   847  C  CD1 . ILE   A 1 102 ? -46.599 9.660   17.383  1.00 45.60  ? 466 ILE   A CD1 1 
ATOM   848  N  N   . ILE   A 1 103 ? -50.223 14.047  19.047  1.00 47.30  ? 467 ILE   A N   1 
ATOM   849  C  CA  . ILE   A 1 103 ? -50.948 15.217  18.467  1.00 55.04  ? 467 ILE   A CA  1 
ATOM   850  C  C   . ILE   A 1 103 ? -50.155 15.728  17.244  1.00 65.12  ? 467 ILE   A C   1 
ATOM   851  O  O   . ILE   A 1 103 ? -49.008 16.222  17.417  1.00 63.15  ? 467 ILE   A O   1 
ATOM   852  C  CB  . ILE   A 1 103 ? -51.182 16.285  19.564  1.00 58.47  ? 467 ILE   A CB  1 
ATOM   853  C  CG1 . ILE   A 1 103 ? -52.192 15.783  20.599  1.00 62.58  ? 467 ILE   A CG1 1 
ATOM   854  C  CG2 . ILE   A 1 103 ? -51.622 17.628  18.985  1.00 58.05  ? 467 ILE   A CG2 1 
ATOM   855  C  CD1 . ILE   A 1 103 ? -52.152 16.534  21.908  1.00 69.19  ? 467 ILE   A CD1 1 
ATOM   856  N  N   . ARG   A 1 104 ? -50.732 15.613  16.042  1.00 64.42  ? 468 ARG   A N   1 
ATOM   857  C  CA  . ARG   A 1 104 ? -50.031 15.903  14.766  1.00 70.83  ? 468 ARG   A CA  1 
ATOM   858  C  C   . ARG   A 1 104 ? -50.654 17.123  14.082  1.00 72.56  ? 468 ARG   A C   1 
ATOM   859  O  O   . ARG   A 1 104 ? -51.761 16.990  13.529  1.00 66.00  ? 468 ARG   A O   1 
ATOM   860  C  CB  . ARG   A 1 104 ? -50.019 14.677  13.847  1.00 78.56  ? 468 ARG   A CB  1 
ATOM   861  C  CG  . ARG   A 1 104 ? -51.374 14.190  13.351  1.00 79.56  ? 468 ARG   A CG  1 
ATOM   862  C  CD  . ARG   A 1 104 ? -51.218 12.834  12.686  1.00 79.64  ? 468 ARG   A CD  1 
ATOM   863  N  NE  . ARG   A 1 104 ? -50.712 11.833  13.621  1.00 78.12  ? 468 ARG   A NE  1 
ATOM   864  C  CZ  . ARG   A 1 104 ? -50.081 10.704  13.285  1.00 82.54  ? 468 ARG   A CZ  1 
ATOM   865  N  NH1 . ARG   A 1 104 ? -49.673 9.872   14.231  1.00 82.82  ? 468 ARG   A NH1 1 
ATOM   866  N  NH2 . ARG   A 1 104 ? -49.853 10.407  12.016  1.00 79.13  ? 468 ARG   A NH2 1 
ATOM   867  N  N   . THR   A 1 105 ? -49.907 18.237  14.074  1.00 72.04  ? 469 THR   A N   1 
ATOM   868  C  CA  . THR   A 1 105 ? -50.301 19.571  13.547  1.00 71.21  ? 469 THR   A CA  1 
ATOM   869  C  C   . THR   A 1 105 ? -49.652 19.806  12.169  1.00 70.52  ? 469 THR   A C   1 
ATOM   870  O  O   . THR   A 1 105 ? -48.512 19.328  11.944  1.00 53.83  ? 469 THR   A O   1 
ATOM   871  C  CB  . THR   A 1 105 ? -49.944 20.640  14.586  1.00 71.90  ? 469 THR   A CB  1 
ATOM   872  O  OG1 . THR   A 1 105 ? -48.525 20.652  14.722  1.00 72.49  ? 469 THR   A OG1 1 
ATOM   873  C  CG2 . THR   A 1 105 ? -50.568 20.378  15.939  1.00 77.23  ? 469 THR   A CG2 1 
ATOM   874  N  N   . GLY   A 1 106 ? -50.342 20.526  11.277  1.00 69.38  ? 470 GLY   A N   1 
ATOM   875  C  CA  . GLY   A 1 106 ? -49.883 20.815  9.904   1.00 76.41  ? 470 GLY   A CA  1 
ATOM   876  C  C   . GLY   A 1 106 ? -49.892 22.302  9.589   1.00 84.39  ? 470 GLY   A C   1 
ATOM   877  O  O   . GLY   A 1 106 ? -50.986 22.902  9.669   1.00 90.90  ? 470 GLY   A O   1 
ATOM   878  N  N   . ARG   A 1 107 ? -48.723 22.869  9.247   1.00 88.40  ? 471 ARG   A N   1 
ATOM   879  C  CA  . ARG   A 1 107 ? -48.568 24.230  8.655   1.00 86.35  ? 471 ARG   A CA  1 
ATOM   880  C  C   . ARG   A 1 107 ? -48.804 24.132  7.146   1.00 83.78  ? 471 ARG   A C   1 
ATOM   881  O  O   . ARG   A 1 107 ? -48.440 23.090  6.554   1.00 67.10  ? 471 ARG   A O   1 
ATOM   882  C  CB  . ARG   A 1 107 ? -47.168 24.832  8.840   1.00 94.58  ? 471 ARG   A CB  1 
ATOM   883  C  CG  . ARG   A 1 107 ? -46.508 24.579  10.188  1.00 103.84 ? 471 ARG   A CG  1 
ATOM   884  C  CD  . ARG   A 1 107 ? -47.282 25.148  11.360  1.00 108.98 ? 471 ARG   A CD  1 
ATOM   885  N  NE  . ARG   A 1 107 ? -46.743 24.668  12.623  1.00 116.36 ? 471 ARG   A NE  1 
ATOM   886  C  CZ  . ARG   A 1 107 ? -46.902 23.434  13.105  1.00 124.33 ? 471 ARG   A CZ  1 
ATOM   887  N  NH1 . ARG   A 1 107 ? -47.593 22.526  12.432  1.00 122.65 ? 471 ARG   A NH1 1 
ATOM   888  N  NH2 . ARG   A 1 107 ? -46.362 23.109  14.266  1.00 124.36 ? 471 ARG   A NH2 1 
ATOM   889  N  N   . THR   A 1 108 ? -49.334 25.198  6.540   1.00 82.60  ? 472 THR   A N   1 
ATOM   890  C  CA  . THR   A 1 108 ? -49.555 25.299  5.071   1.00 84.65  ? 472 THR   A CA  1 
ATOM   891  C  C   . THR   A 1 108 ? -48.195 25.402  4.348   1.00 80.20  ? 472 THR   A C   1 
ATOM   892  O  O   . THR   A 1 108 ? -48.145 25.005  3.161   1.00 79.53  ? 472 THR   A O   1 
ATOM   893  C  CB  . THR   A 1 108 ? -50.553 26.420  4.750   1.00 85.41  ? 472 THR   A CB  1 
ATOM   894  O  OG1 . THR   A 1 108 ? -50.104 27.625  5.372   1.00 89.80  ? 472 THR   A OG1 1 
ATOM   895  C  CG2 . THR   A 1 108 ? -51.955 26.098  5.220   1.00 79.97  ? 472 THR   A CG2 1 
ATOM   896  N  N   . GLY   A 1 109 ? -47.122 25.841  5.028   1.00 70.70  ? 473 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 109 ? -45.763 25.906  4.444   1.00 75.04  ? 473 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 109 ? -45.054 24.549  4.338   1.00 76.37  ? 473 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 109 ? -43.951 24.513  3.759   1.00 67.31  ? 473 GLY   A O   1 
ATOM   900  N  N   . HIS   A 1 110 ? -45.626 23.454  4.861   1.00 67.74  ? 474 HIS   A N   1 
ATOM   901  C  CA  . HIS   A 1 110 ? -44.834 22.261  5.264   1.00 58.74  ? 474 HIS   A CA  1 
ATOM   902  C  C   . HIS   A 1 110 ? -45.232 20.999  4.499   1.00 52.26  ? 474 HIS   A C   1 
ATOM   903  O  O   . HIS   A 1 110 ? -46.384 20.827  4.115   1.00 52.21  ? 474 HIS   A O   1 
ATOM   904  C  CB  . HIS   A 1 110 ? -44.863 22.089  6.788   1.00 55.68  ? 474 HIS   A CB  1 
ATOM   905  C  CG  . HIS   A 1 110 ? -43.809 22.897  7.473   1.00 64.46  ? 474 HIS   A CG  1 
ATOM   906  N  ND1 . HIS   A 1 110 ? -44.054 24.179  7.958   1.00 68.63  ? 474 HIS   A ND1 1 
ATOM   907  C  CD2 . HIS   A 1 110 ? -42.512 22.625  7.756   1.00 62.97  ? 474 HIS   A CD2 1 
ATOM   908  C  CE1 . HIS   A 1 110 ? -42.950 24.653  8.506   1.00 71.59  ? 474 HIS   A CE1 1 
ATOM   909  N  NE2 . HIS   A 1 110 ? -41.987 23.711  8.406   1.00 69.82  ? 474 HIS   A NE2 1 
ATOM   910  N  N   . TRP   A 1 111 ? -44.259 20.108  4.364   1.00 50.17  ? 475 TRP   A N   1 
ATOM   911  C  CA  . TRP   A 1 111 ? -44.348 18.817  3.636   1.00 51.71  ? 475 TRP   A CA  1 
ATOM   912  C  C   . TRP   A 1 111 ? -44.928 17.723  4.539   1.00 45.19  ? 475 TRP   A C   1 
ATOM   913  O  O   . TRP   A 1 111 ? -45.586 16.815  4.035   1.00 47.16  ? 475 TRP   A O   1 
ATOM   914  C  CB  . TRP   A 1 111 ? -42.933 18.499  3.149   1.00 54.11  ? 475 TRP   A CB  1 
ATOM   915  C  CG  . TRP   A 1 111 ? -42.516 19.509  2.134   1.00 54.06  ? 475 TRP   A CG  1 
ATOM   916  C  CD1 . TRP   A 1 111 ? -41.864 20.697  2.319   1.00 51.61  ? 475 TRP   A CD1 1 
ATOM   917  C  CD2 . TRP   A 1 111 ? -42.888 19.451  0.751   1.00 53.57  ? 475 TRP   A CD2 1 
ATOM   918  N  NE1 . TRP   A 1 111 ? -41.747 21.356  1.118   1.00 56.53  ? 475 TRP   A NE1 1 
ATOM   919  C  CE2 . TRP   A 1 111 ? -42.364 20.609  0.138   1.00 54.32  ? 475 TRP   A CE2 1 
ATOM   920  C  CE3 . TRP   A 1 111 ? -43.594 18.516  -0.015  1.00 54.63  ? 475 TRP   A CE3 1 
ATOM   921  C  CZ2 . TRP   A 1 111 ? -42.528 20.849  -1.225  1.00 54.39  ? 475 TRP   A CZ2 1 
ATOM   922  C  CZ3 . TRP   A 1 111 ? -43.745 18.753  -1.364  1.00 60.30  ? 475 TRP   A CZ3 1 
ATOM   923  C  CH2 . TRP   A 1 111 ? -43.213 19.902  -1.957  1.00 57.90  ? 475 TRP   A CH2 1 
ATOM   924  N  N   . LEU   A 1 112 ? -44.687 17.834  5.840   1.00 42.89  ? 476 LEU   A N   1 
ATOM   925  C  CA  . LEU   A 1 112 ? -45.029 16.791  6.835   1.00 40.24  ? 476 LEU   A CA  1 
ATOM   926  C  C   . LEU   A 1 112 ? -45.872 17.396  7.956   1.00 41.10  ? 476 LEU   A C   1 
ATOM   927  O  O   . LEU   A 1 112 ? -45.633 18.555  8.338   1.00 37.00  ? 476 LEU   A O   1 
ATOM   928  C  CB  . LEU   A 1 112 ? -43.719 16.243  7.398   1.00 36.42  ? 476 LEU   A CB  1 
ATOM   929  C  CG  . LEU   A 1 112 ? -43.007 15.227  6.512   1.00 39.17  ? 476 LEU   A CG  1 
ATOM   930  C  CD1 . LEU   A 1 112 ? -41.659 14.860  7.108   1.00 37.06  ? 476 LEU   A CD1 1 
ATOM   931  C  CD2 . LEU   A 1 112 ? -43.871 13.986  6.327   1.00 40.12  ? 476 LEU   A CD2 1 
ATOM   932  N  N   . ASN   A 1 113 ? -46.771 16.601  8.513   1.00 40.30  ? 477 ASN   A N   1 
ATOM   933  C  CA  . ASN   A 1 113 ? -47.374 16.914  9.827   1.00 42.85  ? 477 ASN   A CA  1 
ATOM   934  C  C   . ASN   A 1 113 ? -46.217 16.889  10.826  1.00 37.72  ? 477 ASN   A C   1 
ATOM   935  O  O   . ASN   A 1 113 ? -45.262 16.134  10.608  1.00 36.09  ? 477 ASN   A O   1 
ATOM   936  C  CB  . ASN   A 1 113 ? -48.569 15.996  10.108  1.00 41.91  ? 477 ASN   A CB  1 
ATOM   937  C  CG  . ASN   A 1 113 ? -49.660 16.191  9.068   1.00 48.35  ? 477 ASN   A CG  1 
ATOM   938  O  OD1 . ASN   A 1 113 ? -49.977 15.285  8.301   1.00 54.23  ? 477 ASN   A OD1 1 
ATOM   939  N  ND2 . ASN   A 1 113 ? -50.197 17.391  8.978   1.00 45.56  ? 477 ASN   A ND2 1 
ATOM   940  N  N   . HIS   A 1 114 ? -46.265 17.741  11.835  1.00 34.07  ? 478 HIS   A N   1 
ATOM   941  C  CA  . HIS   A 1 114 ? -45.213 17.861  12.872  1.00 34.92  ? 478 HIS   A CA  1 
ATOM   942  C  C   . HIS   A 1 114 ? -45.723 17.181  14.135  1.00 39.25  ? 478 HIS   A C   1 
ATOM   943  O  O   . HIS   A 1 114 ? -46.853 17.542  14.565  1.00 37.78  ? 478 HIS   A O   1 
ATOM   944  C  CB  . HIS   A 1 114 ? -44.858 19.331  13.114  1.00 36.23  ? 478 HIS   A CB  1 
ATOM   945  C  CG  . HIS   A 1 114 ? -44.179 20.013  11.974  1.00 40.72  ? 478 HIS   A CG  1 
ATOM   946  N  ND1 . HIS   A 1 114 ? -43.470 19.325  10.991  1.00 43.25  ? 478 HIS   A ND1 1 
ATOM   947  C  CD2 . HIS   A 1 114 ? -44.057 21.330  11.672  1.00 40.72  ? 478 HIS   A CD2 1 
ATOM   948  C  CE1 . HIS   A 1 114 ? -43.006 20.193  10.099  1.00 38.79  ? 478 HIS   A CE1 1 
ATOM   949  N  NE2 . HIS   A 1 114 ? -43.342 21.431  10.500  1.00 45.07  ? 478 HIS   A NE2 1 
ATOM   950  N  N   . GLY   A 1 115 ? -44.940 16.241  14.686  1.00 34.01  ? 479 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 115 ? -45.278 15.506  15.914  1.00 33.14  ? 479 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 115 ? -44.466 15.940  17.115  1.00 33.66  ? 479 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 115 ? -44.686 15.377  18.185  1.00 34.32  ? 479 GLY   A O   1 
ATOM   954  N  N   . LYS   A 1 116 ? -43.548 16.904  16.978  1.00 28.77  ? 480 LYS   A N   1 
ATOM   955  C  CA  . LYS   A 1 116 ? -42.573 17.161  18.060  1.00 27.44  ? 480 LYS   A CA  1 
ATOM   956  C  C   . LYS   A 1 116 ? -42.121 18.627  18.087  1.00 27.82  ? 480 LYS   A C   1 
ATOM   957  O  O   . LYS   A 1 116 ? -42.279 19.339  17.076  1.00 30.42  ? 480 LYS   A O   1 
ATOM   958  C  CB  . LYS   A 1 116 ? -41.342 16.288  17.829  1.00 32.27  ? 480 LYS   A CB  1 
ATOM   959  C  CG  . LYS   A 1 116 ? -40.852 16.351  16.380  1.00 33.23  ? 480 LYS   A CG  1 
ATOM   960  C  CD  . LYS   A 1 116 ? -39.624 15.566  16.095  1.00 33.87  ? 480 LYS   A CD  1 
ATOM   961  C  CE  . LYS   A 1 116 ? -39.316 15.437  14.614  1.00 28.10  ? 480 LYS   A CE  1 
ATOM   962  N  NZ  . LYS   A 1 116 ? -39.204 16.761  13.991  1.00 27.67  ? 480 LYS   A NZ  1 
ATOM   963  N  N   . GLU   A 1 117 ? -41.538 19.029  19.210  1.00 29.02  ? 481 GLU   A N   1 
ATOM   964  C  CA  . GLU   A 1 117 ? -40.858 20.319  19.397  1.00 29.12  ? 481 GLU   A CA  1 
ATOM   965  C  C   . GLU   A 1 117 ? -39.415 20.012  19.800  1.00 27.70  ? 481 GLU   A C   1 
ATOM   966  O  O   . GLU   A 1 117 ? -39.165 19.069  20.618  1.00 29.07  ? 481 GLU   A O   1 
ATOM   967  C  CB  . GLU   A 1 117 ? -41.587 21.134  20.465  1.00 32.65  ? 481 GLU   A CB  1 
ATOM   968  C  CG  . GLU   A 1 117 ? -42.904 21.717  19.976  1.00 35.09  ? 481 GLU   A CG  1 
ATOM   969  C  CD  . GLU   A 1 117 ? -42.765 22.895  19.029  1.00 43.28  ? 481 GLU   A CD  1 
ATOM   970  O  OE1 . GLU   A 1 117 ? -41.612 23.353  18.781  1.00 39.11  ? 481 GLU   A OE1 1 
ATOM   971  O  OE2 . GLU   A 1 117 ? -43.798 23.335  18.518  1.00 48.14  ? 481 GLU   A OE2 1 
ATOM   972  N  N   . HIS   A 1 118 ? -38.490 20.782  19.247  1.00 25.31  ? 482 HIS   A N   1 
ATOM   973  C  CA  . HIS   A 1 118 ? -37.042 20.589  19.452  1.00 24.25  ? 482 HIS   A CA  1 
ATOM   974  C  C   . HIS   A 1 118 ? -36.531 21.551  20.512  1.00 24.05  ? 482 HIS   A C   1 
ATOM   975  O  O   . HIS   A 1 118 ? -36.971 22.720  20.498  1.00 25.38  ? 482 HIS   A O   1 
ATOM   976  C  CB  . HIS   A 1 118 ? -36.293 20.800  18.136  1.00 24.47  ? 482 HIS   A CB  1 
ATOM   977  C  CG  . HIS   A 1 118 ? -36.634 19.766  17.126  1.00 25.79  ? 482 HIS   A CG  1 
ATOM   978  N  ND1 . HIS   A 1 118 ? -35.674 18.955  16.565  1.00 27.38  ? 482 HIS   A ND1 1 
ATOM   979  C  CD2 . HIS   A 1 118 ? -37.811 19.430  16.558  1.00 27.41  ? 482 HIS   A CD2 1 
ATOM   980  C  CE1 . HIS   A 1 118 ? -36.250 18.156  15.694  1.00 27.24  ? 482 HIS   A CE1 1 
ATOM   981  N  NE2 . HIS   A 1 118 ? -37.570 18.395  15.698  1.00 26.18  ? 482 HIS   A NE2 1 
ATOM   982  N  N   . CYS   A 1 119 ? -35.572 21.068  21.295  1.00 24.51  ? 483 CYS   A N   1 
ATOM   983  C  CA  . CYS   A 1 119 ? -34.821 21.835  22.296  1.00 23.52  ? 483 CYS   A CA  1 
ATOM   984  C  C   . CYS   A 1 119 ? -33.335 21.554  22.077  1.00 24.55  ? 483 CYS   A C   1 
ATOM   985  O  O   . CYS   A 1 119 ? -32.845 20.457  22.403  1.00 23.86  ? 483 CYS   A O   1 
ATOM   986  C  CB  . CYS   A 1 119 ? -35.263 21.517  23.725  1.00 24.41  ? 483 CYS   A CB  1 
ATOM   987  S  SG  . CYS   A 1 119 ? -34.517 22.645  24.938  1.00 25.99  ? 483 CYS   A SG  1 
ATOM   988  N  N   . LEU   A 1 120 ? -32.602 22.565  21.624  1.00 25.94  ? 484 LEU   A N   1 
ATOM   989  C  CA  . LEU   A 1 120 ? -31.125 22.450  21.513  1.00 23.40  ? 484 LEU   A CA  1 
ATOM   990  C  C   . LEU   A 1 120 ? -30.504 22.486  22.898  1.00 23.98  ? 484 LEU   A C   1 
ATOM   991  O  O   . LEU   A 1 120 ? -30.960 23.282  23.768  1.00 24.59  ? 484 LEU   A O   1 
ATOM   992  C  CB  . LEU   A 1 120 ? -30.589 23.614  20.677  1.00 24.41  ? 484 LEU   A CB  1 
ATOM   993  C  CG  . LEU   A 1 120 ? -31.217 23.813  19.313  1.00 26.66  ? 484 LEU   A CG  1 
ATOM   994  C  CD1 . LEU   A 1 120 ? -30.428 24.840  18.519  1.00 29.82  ? 484 LEU   A CD1 1 
ATOM   995  C  CD2 . LEU   A 1 120 ? -31.339 22.511  18.543  1.00 25.35  ? 484 LEU   A CD2 1 
ATOM   996  N  N   . VAL   A 1 121 ? -29.472 21.683  23.113  1.00 24.72  ? 485 VAL   A N   1 
ATOM   997  C  CA  . VAL   A 1 121 ? -28.671 21.737  24.359  1.00 22.10  ? 485 VAL   A CA  1 
ATOM   998  C  C   . VAL   A 1 121 ? -27.280 22.244  24.010  1.00 24.44  ? 485 VAL   A C   1 
ATOM   999  O  O   . VAL   A 1 121 ? -26.551 21.553  23.271  1.00 23.73  ? 485 VAL   A O   1 
ATOM   1000 C  CB  . VAL   A 1 121 ? -28.627 20.366  25.034  1.00 23.11  ? 485 VAL   A CB  1 
ATOM   1001 C  CG1 . VAL   A 1 121 ? -27.900 20.446  26.343  1.00 22.93  ? 485 VAL   A CG1 1 
ATOM   1002 C  CG2 . VAL   A 1 121 ? -30.039 19.800  25.198  1.00 23.92  ? 485 VAL   A CG2 1 
ATOM   1003 N  N   . GLY   A 1 122 ? -26.908 23.362  24.602  1.00 22.76  ? 486 GLY   A N   1 
ATOM   1004 C  CA  . GLY   A 1 122 ? -25.573 23.948  24.437  1.00 25.74  ? 486 GLY   A CA  1 
ATOM   1005 C  C   . GLY   A 1 122 ? -24.752 23.812  25.684  1.00 26.91  ? 486 GLY   A C   1 
ATOM   1006 O  O   . GLY   A 1 122 ? -25.325 23.862  26.817  1.00 26.61  ? 486 GLY   A O   1 
ATOM   1007 N  N   . VAL   A 1 123 ? -23.432 23.751  25.512  1.00 25.80  ? 487 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 123 ? -22.512 23.798  26.678  1.00 26.14  ? 487 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 123 ? -21.518 24.953  26.495  1.00 29.27  ? 487 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 123 ? -21.093 25.223  25.349  1.00 27.01  ? 487 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 123 ? -21.814 22.448  26.866  1.00 28.82  ? 487 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 123 ? -20.967 22.062  25.662  1.00 29.14  ? 487 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 123 ? -20.976 22.444  28.143  1.00 30.67  ? 487 VAL   A CG2 1 
ATOM   1014 N  N   . LYS   A 1 124 ? -21.195 25.622  27.601  1.00 28.93  ? 488 LYS   A N   1 
ATOM   1015 C  CA  . LYS   A 1 124 ? -20.204 26.730  27.670  1.00 31.94  ? 488 LYS   A CA  1 
ATOM   1016 C  C   . LYS   A 1 124 ? -19.209 26.336  28.756  1.00 33.80  ? 488 LYS   A C   1 
ATOM   1017 O  O   . LYS   A 1 124 ? -19.642 25.877  29.838  1.00 33.33  ? 488 LYS   A O   1 
ATOM   1018 C  CB  . LYS   A 1 124 ? -20.897 28.049  27.993  1.00 31.67  ? 488 LYS   A CB  1 
ATOM   1019 C  CG  . LYS   A 1 124 ? -19.997 29.258  28.130  1.00 37.48  ? 488 LYS   A CG  1 
ATOM   1020 C  CD  . LYS   A 1 124 ? -20.756 30.535  28.379  1.00 33.96  ? 488 LYS   A CD  1 
ATOM   1021 C  CE  . LYS   A 1 124 ? -19.849 31.603  28.944  1.00 35.11  ? 488 LYS   A CE  1 
ATOM   1022 N  NZ  . LYS   A 1 124 ? -20.558 32.891  29.110  1.00 36.33  ? 488 LYS   A NZ  1 
ATOM   1023 N  N   . GLY   A 1 125 ? -17.924 26.549  28.508  1.00 34.42  ? 489 GLY   A N   1 
ATOM   1024 C  CA  . GLY   A 1 125 ? -16.910 26.428  29.574  1.00 40.87  ? 489 GLY   A CA  1 
ATOM   1025 C  C   . GLY   A 1 125 ? -16.661 24.983  29.968  1.00 38.97  ? 489 GLY   A C   1 
ATOM   1026 O  O   . GLY   A 1 125 ? -16.724 24.113  29.097  1.00 43.41  ? 489 GLY   A O   1 
ATOM   1027 N  N   . ASN   A 1 126 ? -16.362 24.755  31.245  1.00 45.40  ? 490 ASN   A N   1 
ATOM   1028 C  CA  . ASN   A 1 126 ? -15.936 23.439  31.799  1.00 53.03  ? 490 ASN   A CA  1 
ATOM   1029 C  C   . ASN   A 1 126 ? -16.892 23.012  32.901  1.00 48.72  ? 490 ASN   A C   1 
ATOM   1030 O  O   . ASN   A 1 126 ? -16.559 23.095  34.076  1.00 54.83  ? 490 ASN   A O   1 
ATOM   1031 C  CB  . ASN   A 1 126 ? -14.530 23.523  32.398  1.00 58.14  ? 490 ASN   A CB  1 
ATOM   1032 C  CG  . ASN   A 1 126 ? -13.493 23.859  31.354  1.00 55.82  ? 490 ASN   A CG  1 
ATOM   1033 O  OD1 . ASN   A 1 126 ? -12.734 24.816  31.509  1.00 50.94  ? 490 ASN   A OD1 1 
ATOM   1034 N  ND2 . ASN   A 1 126 ? -13.504 23.096  30.273  1.00 58.68  ? 490 ASN   A ND2 1 
ATOM   1035 N  N   . PRO   A 1 127 ? -18.145 22.640  32.580  1.00 47.50  ? 491 PRO   A N   1 
ATOM   1036 C  CA  . PRO   A 1 127 ? -19.094 22.275  33.623  1.00 46.38  ? 491 PRO   A CA  1 
ATOM   1037 C  C   . PRO   A 1 127 ? -18.567 21.052  34.386  1.00 40.97  ? 491 PRO   A C   1 
ATOM   1038 O  O   . PRO   A 1 127 ? -18.138 20.080  33.777  1.00 42.24  ? 491 PRO   A O   1 
ATOM   1039 C  CB  . PRO   A 1 127 ? -20.399 21.980  32.869  1.00 46.59  ? 491 PRO   A CB  1 
ATOM   1040 C  CG  . PRO   A 1 127 ? -19.945 21.688  31.457  1.00 46.56  ? 491 PRO   A CG  1 
ATOM   1041 C  CD  . PRO   A 1 127 ? -18.719 22.551  31.230  1.00 48.29  ? 491 PRO   A CD  1 
ATOM   1042 N  N   . GLN   A 1 128 ? -18.583 21.131  35.711  1.00 38.09  ? 492 GLN   A N   1 
ATOM   1043 C  CA  . GLN   A 1 128 ? -18.166 20.001  36.584  1.00 39.10  ? 492 GLN   A CA  1 
ATOM   1044 C  C   . GLN   A 1 128 ? -19.316 19.634  37.517  1.00 36.85  ? 492 GLN   A C   1 
ATOM   1045 O  O   . GLN   A 1 128 ? -19.975 20.561  38.039  1.00 37.92  ? 492 GLN   A O   1 
ATOM   1046 C  CB  . GLN   A 1 128 ? -16.893 20.367  37.355  1.00 36.46  ? 492 GLN   A CB  1 
ATOM   1047 C  CG  . GLN   A 1 128 ? -15.726 20.721  36.445  1.00 36.23  ? 492 GLN   A CG  1 
ATOM   1048 C  CD  . GLN   A 1 128 ? -14.395 20.790  37.168  1.00 39.59  ? 492 GLN   A CD  1 
ATOM   1049 O  OE1 . GLN   A 1 128 ? -14.085 19.977  38.034  1.00 40.32  ? 492 GLN   A OE1 1 
ATOM   1050 N  NE2 . GLN   A 1 128 ? -13.585 21.765  36.792  1.00 43.32  ? 492 GLN   A NE2 1 
ATOM   1051 N  N   . GLY   A 1 129 ? -19.481 18.336  37.790  1.00 37.83  ? 493 GLY   A N   1 
ATOM   1052 C  CA  . GLY   A 1 129 ? -20.441 17.832  38.789  1.00 40.44  ? 493 GLY   A CA  1 
ATOM   1053 C  C   . GLY   A 1 129 ? -21.873 17.787  38.253  1.00 41.89  ? 493 GLY   A C   1 
ATOM   1054 O  O   . GLY   A 1 129 ? -22.791 17.871  39.037  1.00 43.88  ? 493 GLY   A O   1 
ATOM   1055 N  N   . PHE   A 1 130 ? -22.073 17.663  36.946  1.00 41.58  ? 494 PHE   A N   1 
ATOM   1056 C  CA  . PHE   A 1 130 ? -23.425 17.463  36.360  1.00 39.65  ? 494 PHE   A CA  1 
ATOM   1057 C  C   . PHE   A 1 130 ? -23.643 15.951  36.247  1.00 41.38  ? 494 PHE   A C   1 
ATOM   1058 O  O   . PHE   A 1 130 ? -22.637 15.214  36.169  1.00 41.62  ? 494 PHE   A O   1 
ATOM   1059 C  CB  . PHE   A 1 130 ? -23.500 18.212  35.032  1.00 38.91  ? 494 PHE   A CB  1 
ATOM   1060 C  CG  . PHE   A 1 130 ? -23.536 19.704  35.200  1.00 38.67  ? 494 PHE   A CG  1 
ATOM   1061 C  CD1 . PHE   A 1 130 ? -22.379 20.408  35.531  1.00 39.32  ? 494 PHE   A CD1 1 
ATOM   1062 C  CD2 . PHE   A 1 130 ? -24.723 20.414  35.038  1.00 38.59  ? 494 PHE   A CD2 1 
ATOM   1063 C  CE1 . PHE   A 1 130 ? -22.419 21.783  35.705  1.00 39.53  ? 494 PHE   A CE1 1 
ATOM   1064 C  CE2 . PHE   A 1 130 ? -24.748 21.797  35.183  1.00 37.01  ? 494 PHE   A CE2 1 
ATOM   1065 C  CZ  . PHE   A 1 130 ? -23.602 22.475  35.541  1.00 38.07  ? 494 PHE   A CZ  1 
ATOM   1066 N  N   . ASN   A 1 131 ? -24.883 15.474  36.231  1.00 38.09  ? 495 ASN   A N   1 
ATOM   1067 C  CA  . ASN   A 1 131 ? -25.137 14.019  36.104  1.00 36.65  ? 495 ASN   A CA  1 
ATOM   1068 C  C   . ASN   A 1 131 ? -25.574 13.685  34.687  1.00 36.54  ? 495 ASN   A C   1 
ATOM   1069 O  O   . ASN   A 1 131 ? -26.789 13.538  34.470  1.00 36.30  ? 495 ASN   A O   1 
ATOM   1070 C  CB  . ASN   A 1 131 ? -26.165 13.584  37.132  1.00 37.68  ? 495 ASN   A CB  1 
ATOM   1071 C  CG  . ASN   A 1 131 ? -25.703 13.981  38.504  1.00 40.60  ? 495 ASN   A CG  1 
ATOM   1072 O  OD1 . ASN   A 1 131 ? -24.613 13.599  38.899  1.00 41.09  ? 495 ASN   A OD1 1 
ATOM   1073 N  ND2 . ASN   A 1 131 ? -26.500 14.771  39.197  1.00 41.54  ? 495 ASN   A ND2 1 
ATOM   1074 N  N   . GLN   A 1 132 ? -24.625 13.563  33.765  1.00 36.06  ? 496 GLN   A N   1 
ATOM   1075 C  CA  . GLN   A 1 132 ? -24.929 13.389  32.327  1.00 37.35  ? 496 GLN   A CA  1 
ATOM   1076 C  C   . GLN   A 1 132 ? -25.464 11.967  32.144  1.00 36.95  ? 496 GLN   A C   1 
ATOM   1077 O  O   . GLN   A 1 132 ? -25.020 11.070  32.855  1.00 39.43  ? 496 GLN   A O   1 
ATOM   1078 C  CB  . GLN   A 1 132 ? -23.686 13.740  31.507  1.00 44.27  ? 496 GLN   A CB  1 
ATOM   1079 C  CG  . GLN   A 1 132 ? -23.370 15.228  31.609  1.00 52.62  ? 496 GLN   A CG  1 
ATOM   1080 C  CD  . GLN   A 1 132 ? -21.990 15.646  31.157  1.00 67.19  ? 496 GLN   A CD  1 
ATOM   1081 O  OE1 . GLN   A 1 132 ? -21.568 15.392  30.020  1.00 75.59  ? 496 GLN   A OE1 1 
ATOM   1082 N  NE2 . GLN   A 1 132 ? -21.294 16.348  32.041  1.00 59.63  ? 496 GLN   A NE2 1 
ATOM   1083 N  N   . GLY   A 1 133 ? -26.452 11.779  31.286  1.00 33.40  ? 497 GLY   A N   1 
ATOM   1084 C  CA  . GLY   A 1 133 ? -26.856 10.430  30.845  1.00 36.81  ? 497 GLY   A CA  1 
ATOM   1085 C  C   . GLY   A 1 133 ? -27.844 9.770   31.786  1.00 35.35  ? 497 GLY   A C   1 
ATOM   1086 O  O   . GLY   A 1 133 ? -28.116 8.575   31.597  1.00 35.66  ? 497 GLY   A O   1 
ATOM   1087 N  N   . LEU   A 1 134 ? -28.452 10.517  32.705  1.00 35.63  ? 498 LEU   A N   1 
ATOM   1088 C  CA  . LEU   A 1 134 ? -29.553 9.959   33.547  1.00 37.51  ? 498 LEU   A CA  1 
ATOM   1089 C  C   . LEU   A 1 134 ? -30.822 9.887   32.722  1.00 38.63  ? 498 LEU   A C   1 
ATOM   1090 O  O   . LEU   A 1 134 ? -31.513 8.870   32.758  1.00 35.50  ? 498 LEU   A O   1 
ATOM   1091 C  CB  . LEU   A 1 134 ? -29.785 10.834  34.775  1.00 39.82  ? 498 LEU   A CB  1 
ATOM   1092 C  CG  . LEU   A 1 134 ? -28.705 10.768  35.843  1.00 38.06  ? 498 LEU   A CG  1 
ATOM   1093 C  CD1 . LEU   A 1 134 ? -29.111 11.670  36.986  1.00 38.80  ? 498 LEU   A CD1 1 
ATOM   1094 C  CD2 . LEU   A 1 134 ? -28.476 9.343   36.327  1.00 43.07  ? 498 LEU   A CD2 1 
ATOM   1095 N  N   . ASP   A 1 135 ? -31.128 10.964  32.015  1.00 32.52  ? 499 ASP   A N   1 
ATOM   1096 C  CA  . ASP   A 1 135 ? -32.355 11.035  31.197  1.00 32.97  ? 499 ASP   A CA  1 
ATOM   1097 C  C   . ASP   A 1 135 ? -32.015 10.770  29.742  1.00 31.06  ? 499 ASP   A C   1 
ATOM   1098 O  O   . ASP   A 1 135 ? -30.852 10.887  29.316  1.00 30.20  ? 499 ASP   A O   1 
ATOM   1099 C  CB  . ASP   A 1 135 ? -33.036 12.387  31.397  1.00 31.96  ? 499 ASP   A CB  1 
ATOM   1100 C  CG  . ASP   A 1 135 ? -33.819 12.404  32.700  1.00 31.14  ? 499 ASP   A CG  1 
ATOM   1101 O  OD1 . ASP   A 1 135 ? -34.983 12.002  32.654  1.00 30.90  ? 499 ASP   A OD1 1 
ATOM   1102 O  OD2 . ASP   A 1 135 ? -33.253 12.839  33.733  1.00 33.83  ? 499 ASP   A OD2 1 
ATOM   1103 N  N   A CYS   A 1 136 ? -33.001 10.416  28.953  0.50 29.48  ? 500 CYS   A N   1 
ATOM   1104 N  N   B CYS   A 1 136 ? -33.071 10.435  29.010  0.50 31.08  ? 500 CYS   A N   1 
ATOM   1105 C  CA  A CYS   A 1 136 ? -32.775 10.279  27.501  0.50 30.08  ? 500 CYS   A CA  1 
ATOM   1106 C  CA  B CYS   A 1 136 ? -33.125 10.246  27.540  0.50 32.63  ? 500 CYS   A CA  1 
ATOM   1107 C  C   A CYS   A 1 136 ? -33.368 11.509  26.810  0.50 30.28  ? 500 CYS   A C   1 
ATOM   1108 C  C   B CYS   A 1 136 ? -33.263 11.602  26.850  0.50 31.30  ? 500 CYS   A C   1 
ATOM   1109 O  O   A CYS   A 1 136 ? -34.114 12.281  27.455  0.50 28.72  ? 500 CYS   A O   1 
ATOM   1110 O  O   B CYS   A 1 136 ? -33.620 12.576  27.558  0.50 29.12  ? 500 CYS   A O   1 
ATOM   1111 C  CB  A CYS   A 1 136 ? -33.340 8.972   26.976  0.50 28.53  ? 500 CYS   A CB  1 
ATOM   1112 C  CB  B CYS   A 1 136 ? -34.342 9.419   27.161  0.50 32.01  ? 500 CYS   A CB  1 
ATOM   1113 S  SG  A CYS   A 1 136 ? -35.140 8.988   26.855  0.50 27.41  ? 500 CYS   A SG  1 
ATOM   1114 S  SG  B CYS   A 1 136 ? -34.094 7.657   27.449  0.50 38.19  ? 500 CYS   A SG  1 
ATOM   1115 N  N   . ASP   A 1 137 ? -33.065 11.639  25.526  1.00 28.52  ? 501 ASP   A N   1 
ATOM   1116 C  CA  . ASP   A 1 137 ? -33.284 12.871  24.720  1.00 29.87  ? 501 ASP   A CA  1 
ATOM   1117 C  C   . ASP   A 1 137 ? -34.659 12.869  24.055  1.00 28.06  ? 501 ASP   A C   1 
ATOM   1118 O  O   . ASP   A 1 137 ? -34.876 13.703  23.135  1.00 27.25  ? 501 ASP   A O   1 
ATOM   1119 C  CB  . ASP   A 1 137 ? -32.144 13.078  23.714  1.00 30.79  ? 501 ASP   A CB  1 
ATOM   1120 C  CG  . ASP   A 1 137 ? -31.917 11.959  22.709  1.00 32.80  ? 501 ASP   A CG  1 
ATOM   1121 O  OD1 . ASP   A 1 137 ? -32.640 10.905  22.747  1.00 29.75  ? 501 ASP   A OD1 1 
ATOM   1122 O  OD2 . ASP   A 1 137 ? -31.056 12.186  21.837  1.00 34.44  ? 501 ASP   A OD2 1 
ATOM   1123 N  N   . VAL   A 1 138 ? -35.598 12.034  24.505  1.00 25.86  ? 502 VAL   A N   1 
ATOM   1124 C  CA  . VAL   A 1 138 ? -36.991 12.079  23.982  1.00 26.70  ? 502 VAL   A CA  1 
ATOM   1125 C  C   . VAL   A 1 138 ? -37.951 12.251  25.175  1.00 26.09  ? 502 VAL   A C   1 
ATOM   1126 O  O   . VAL   A 1 138 ? -37.863 11.456  26.131  1.00 30.19  ? 502 VAL   A O   1 
ATOM   1127 C  CB  . VAL   A 1 138 ? -37.333 10.811  23.163  1.00 24.99  ? 502 VAL   A CB  1 
ATOM   1128 C  CG1 . VAL   A 1 138 ? -38.792 10.776  22.783  1.00 26.43  ? 502 VAL   A CG1 1 
ATOM   1129 C  CG2 . VAL   A 1 138 ? -36.454 10.690  21.933  1.00 24.89  ? 502 VAL   A CG2 1 
ATOM   1130 N  N   . ILE   A 1 139 ? -38.789 13.279  25.135  1.00 26.11  ? 503 ILE   A N   1 
ATOM   1131 C  CA  . ILE   A 1 139 ? -39.870 13.515  26.138  1.00 25.62  ? 503 ILE   A CA  1 
ATOM   1132 C  C   . ILE   A 1 139 ? -41.166 13.113  25.456  1.00 26.32  ? 503 ILE   A C   1 
ATOM   1133 O  O   . ILE   A 1 139 ? -41.436 13.568  24.335  1.00 28.93  ? 503 ILE   A O   1 
ATOM   1134 C  CB  . ILE   A 1 139 ? -39.941 14.978  26.610  1.00 26.37  ? 503 ILE   A CB  1 
ATOM   1135 C  CG1 . ILE   A 1 139 ? -38.612 15.462  27.176  1.00 25.11  ? 503 ILE   A CG1 1 
ATOM   1136 C  CG2 . ILE   A 1 139 ? -41.085 15.161  27.592  1.00 28.68  ? 503 ILE   A CG2 1 
ATOM   1137 C  CD1 . ILE   A 1 139 ? -38.562 16.959  27.447  1.00 28.99  ? 503 ILE   A CD1 1 
ATOM   1138 N  N   . VAL   A 1 140 ? -41.967 12.303  26.146  1.00 29.93  ? 504 VAL   A N   1 
ATOM   1139 C  CA  . VAL   A 1 140 ? -43.348 11.994  25.714  1.00 27.56  ? 504 VAL   A CA  1 
ATOM   1140 C  C   . VAL   A 1 140 ? -44.279 12.572  26.797  1.00 29.70  ? 504 VAL   A C   1 
ATOM   1141 O  O   . VAL   A 1 140 ? -44.141 12.152  27.963  1.00 34.59  ? 504 VAL   A O   1 
ATOM   1142 C  CB  . VAL   A 1 140 ? -43.525 10.480  25.531  1.00 29.71  ? 504 VAL   A CB  1 
ATOM   1143 C  CG1 . VAL   A 1 140 ? -44.966 10.136  25.239  1.00 29.95  ? 504 VAL   A CG1 1 
ATOM   1144 C  CG2 . VAL   A 1 140 ? -42.627 9.975   24.409  1.00 30.60  ? 504 VAL   A CG2 1 
ATOM   1145 N  N   . ALA   A 1 141 ? -45.063 13.585  26.447  1.00 31.07  ? 505 ALA   A N   1 
ATOM   1146 C  CA  . ALA   A 1 141 ? -45.803 14.384  27.439  1.00 35.27  ? 505 ALA   A CA  1 
ATOM   1147 C  C   . ALA   A 1 141 ? -46.958 15.102  26.768  1.00 36.13  ? 505 ALA   A C   1 
ATOM   1148 O  O   . ALA   A 1 141 ? -46.923 15.341  25.552  1.00 34.70  ? 505 ALA   A O   1 
ATOM   1149 C  CB  . ALA   A 1 141 ? -44.872 15.332  28.152  1.00 36.91  ? 505 ALA   A CB  1 
ATOM   1150 N  N   . GLU   A 1 142 ? -47.971 15.405  27.581  1.00 41.39  ? 506 GLU   A N   1 
ATOM   1151 C  CA  . GLU   A 1 142 ? -49.263 15.987  27.159  1.00 43.95  ? 506 GLU   A CA  1 
ATOM   1152 C  C   . GLU   A 1 142 ? -49.095 17.499  26.956  1.00 44.16  ? 506 GLU   A C   1 
ATOM   1153 O  O   . GLU   A 1 142 ? -48.351 18.120  27.723  1.00 42.02  ? 506 GLU   A O   1 
ATOM   1154 C  CB  . GLU   A 1 142 ? -50.315 15.673  28.231  1.00 47.80  ? 506 GLU   A CB  1 
ATOM   1155 C  CG  . GLU   A 1 142 ? -50.342 14.200  28.643  1.00 57.08  ? 506 GLU   A CG  1 
ATOM   1156 C  CD  . GLU   A 1 142 ? -51.180 13.872  29.873  1.00 63.66  ? 506 GLU   A CD  1 
ATOM   1157 O  OE1 . GLU   A 1 142 ? -51.327 14.757  30.750  1.00 74.46  ? 506 GLU   A OE1 1 
ATOM   1158 O  OE2 . GLU   A 1 142 ? -51.697 12.741  29.947  1.00 55.41  ? 506 GLU   A OE2 1 
ATOM   1159 N  N   . VAL   A 1 143 ? -49.766 18.055  25.946  1.00 58.66  ? 507 VAL   A N   1 
ATOM   1160 C  CA  . VAL   A 1 143 ? -49.931 19.525  25.730  1.00 62.97  ? 507 VAL   A CA  1 
ATOM   1161 C  C   . VAL   A 1 143 ? -50.786 20.106  26.872  1.00 69.11  ? 507 VAL   A C   1 
ATOM   1162 O  O   . VAL   A 1 143 ? -51.836 19.519  27.161  1.00 75.20  ? 507 VAL   A O   1 
ATOM   1163 C  CB  . VAL   A 1 143 ? -50.559 19.779  24.344  1.00 67.48  ? 507 VAL   A CB  1 
ATOM   1164 C  CG1 . VAL   A 1 143 ? -50.909 21.249  24.136  1.00 72.93  ? 507 VAL   A CG1 1 
ATOM   1165 C  CG2 . VAL   A 1 143 ? -49.654 19.270  23.222  1.00 64.92  ? 507 VAL   A CG2 1 
ATOM   1166 N  N   . ARG   A 1 144 ? -50.347 21.200  27.507  1.00 70.86  ? 508 ARG   A N   1 
ATOM   1167 C  CA  . ARG   A 1 144 ? -51.088 21.919  28.590  1.00 78.63  ? 508 ARG   A CA  1 
ATOM   1168 C  C   . ARG   A 1 144 ? -51.436 23.346  28.124  1.00 74.61  ? 508 ARG   A C   1 
ATOM   1169 O  O   . ARG   A 1 144 ? -50.721 23.879  27.250  1.00 71.06  ? 508 ARG   A O   1 
ATOM   1170 C  CB  . ARG   A 1 144 ? -50.258 21.975  29.879  1.00 84.27  ? 508 ARG   A CB  1 
ATOM   1171 C  CG  . ARG   A 1 144 ? -49.714 20.631  30.346  1.00 87.17  ? 508 ARG   A CG  1 
ATOM   1172 C  CD  . ARG   A 1 144 ? -50.800 19.616  30.667  1.00 97.28  ? 508 ARG   A CD  1 
ATOM   1173 N  NE  . ARG   A 1 144 ? -50.296 18.459  31.413  1.00 105.10 ? 508 ARG   A NE  1 
ATOM   1174 C  CZ  . ARG   A 1 144 ? -51.044 17.462  31.903  1.00 100.03 ? 508 ARG   A CZ  1 
ATOM   1175 N  NH1 . ARG   A 1 144 ? -50.472 16.464  32.558  1.00 97.07  ? 508 ARG   A NH1 1 
ATOM   1176 N  NH2 . ARG   A 1 144 ? -52.355 17.457  31.735  1.00 99.17  ? 508 ARG   A NH2 1 
ATOM   1177 N  N   . SER   A 1 145 ? -52.489 23.951  28.688  1.00 65.68  ? 509 SER   A N   1 
ATOM   1178 C  CA  . SER   A 1 145 ? -53.007 25.291  28.294  1.00 57.16  ? 509 SER   A CA  1 
ATOM   1179 C  C   . SER   A 1 145 ? -52.222 26.410  28.998  1.00 49.46  ? 509 SER   A C   1 
ATOM   1180 O  O   . SER   A 1 145 ? -52.204 27.536  28.468  1.00 54.32  ? 509 SER   A O   1 
ATOM   1181 C  CB  . SER   A 1 145 ? -54.488 25.405  28.585  1.00 62.24  ? 509 SER   A CB  1 
ATOM   1182 O  OG  . SER   A 1 145 ? -54.726 25.308  29.984  1.00 60.68  ? 509 SER   A OG  1 
ATOM   1183 N  N   . THR   A 1 146 ? -51.577 26.112  30.128  1.00 47.51  ? 510 THR   A N   1 
ATOM   1184 C  CA  . THR   A 1 146 ? -50.922 27.110  31.019  1.00 49.40  ? 510 THR   A CA  1 
ATOM   1185 C  C   . THR   A 1 146 ? -49.423 27.247  30.688  1.00 47.77  ? 510 THR   A C   1 
ATOM   1186 O  O   . THR   A 1 146 ? -48.744 28.121  31.299  1.00 44.48  ? 510 THR   A O   1 
ATOM   1187 C  CB  . THR   A 1 146 ? -51.106 26.709  32.488  1.00 51.98  ? 510 THR   A CB  1 
ATOM   1188 O  OG1 . THR   A 1 146 ? -50.672 25.352  32.578  1.00 57.83  ? 510 THR   A OG1 1 
ATOM   1189 C  CG2 . THR   A 1 146 ? -52.530 26.870  32.982  1.00 55.79  ? 510 THR   A CG2 1 
ATOM   1190 N  N   . SER   A 1 147 ? -48.895 26.392  29.808  1.00 47.74  ? 511 SER   A N   1 
ATOM   1191 C  CA  . SER   A 1 147 ? -47.446 26.347  29.475  1.00 46.80  ? 511 SER   A CA  1 
ATOM   1192 C  C   . SER   A 1 147 ? -47.242 25.987  28.004  1.00 47.01  ? 511 SER   A C   1 
ATOM   1193 O  O   . SER   A 1 147 ? -48.043 25.218  27.425  1.00 44.13  ? 511 SER   A O   1 
ATOM   1194 C  CB  . SER   A 1 147 ? -46.684 25.397  30.360  1.00 48.62  ? 511 SER   A CB  1 
ATOM   1195 O  OG  . SER   A 1 147 ? -45.299 25.419  30.023  1.00 43.21  ? 511 SER   A OG  1 
ATOM   1196 N  N   . HIS   A 1 148 ? -46.186 26.540  27.409  1.00 40.94  ? 512 HIS   A N   1 
ATOM   1197 C  CA  . HIS   A 1 148 ? -45.819 26.265  26.000  1.00 42.46  ? 512 HIS   A CA  1 
ATOM   1198 C  C   . HIS   A 1 148 ? -45.100 24.916  25.907  1.00 37.04  ? 512 HIS   A C   1 
ATOM   1199 O  O   . HIS   A 1 148 ? -45.026 24.370  24.803  1.00 41.40  ? 512 HIS   A O   1 
ATOM   1200 C  CB  . HIS   A 1 148 ? -44.940 27.401  25.470  1.00 37.22  ? 512 HIS   A CB  1 
ATOM   1201 C  CG  . HIS   A 1 148 ? -45.700 28.661  25.275  1.00 40.89  ? 512 HIS   A CG  1 
ATOM   1202 N  ND1 . HIS   A 1 148 ? -46.774 28.736  24.427  1.00 43.25  ? 512 HIS   A ND1 1 
ATOM   1203 C  CD2 . HIS   A 1 148 ? -45.548 29.889  25.815  1.00 43.63  ? 512 HIS   A CD2 1 
ATOM   1204 C  CE1 . HIS   A 1 148 ? -47.243 29.972  24.428  1.00 45.29  ? 512 HIS   A CE1 1 
ATOM   1205 N  NE2 . HIS   A 1 148 ? -46.519 30.694  25.284  1.00 40.10  ? 512 HIS   A NE2 1 
ATOM   1206 N  N   . LYS   A 1 149 ? -44.547 24.448  27.021  1.00 33.87  ? 513 LYS   A N   1 
ATOM   1207 C  CA  . LYS   A 1 149 ? -43.572 23.334  27.072  1.00 34.89  ? 513 LYS   A CA  1 
ATOM   1208 C  C   . LYS   A 1 149 ? -43.956 22.410  28.219  1.00 35.59  ? 513 LYS   A C   1 
ATOM   1209 O  O   . LYS   A 1 149 ? -44.696 22.804  29.125  1.00 33.03  ? 513 LYS   A O   1 
ATOM   1210 C  CB  . LYS   A 1 149 ? -42.161 23.915  27.266  1.00 36.91  ? 513 LYS   A CB  1 
ATOM   1211 C  CG  . LYS   A 1 149 ? -41.849 24.294  28.713  1.00 40.99  ? 513 LYS   A CG  1 
ATOM   1212 C  CD  . LYS   A 1 149 ? -40.551 25.052  28.978  1.00 40.07  ? 513 LYS   A CD  1 
ATOM   1213 C  CE  . LYS   A 1 149 ? -40.506 26.452  28.389  1.00 40.33  ? 513 LYS   A CE  1 
ATOM   1214 N  NZ  . LYS   A 1 149 ? -41.287 27.431  29.189  1.00 38.47  ? 513 LYS   A NZ  1 
ATOM   1215 N  N   . PRO   A 1 150 ? -43.472 21.150  28.214  1.00 35.93  ? 514 PRO   A N   1 
ATOM   1216 C  CA  . PRO   A 1 150 ? -43.842 20.178  29.250  1.00 36.59  ? 514 PRO   A CA  1 
ATOM   1217 C  C   . PRO   A 1 150 ? -43.050 20.384  30.540  1.00 36.03  ? 514 PRO   A C   1 
ATOM   1218 O  O   . PRO   A 1 150 ? -41.910 20.720  30.452  1.00 32.74  ? 514 PRO   A O   1 
ATOM   1219 C  CB  . PRO   A 1 150 ? -43.489 18.854  28.554  1.00 36.25  ? 514 PRO   A CB  1 
ATOM   1220 C  CG  . PRO   A 1 150 ? -42.288 19.199  27.701  1.00 39.59  ? 514 PRO   A CG  1 
ATOM   1221 C  CD  . PRO   A 1 150 ? -42.588 20.590  27.185  1.00 38.64  ? 514 PRO   A CD  1 
ATOM   1222 N  N   . ASP   A 1 151 ? -43.644 20.127  31.706  1.00 33.59  ? 515 ASP   A N   1 
ATOM   1223 C  CA  . ASP   A 1 151 ? -42.946 20.305  33.008  1.00 33.99  ? 515 ASP   A CA  1 
ATOM   1224 C  C   . ASP   A 1 151 ? -41.831 19.269  33.159  1.00 29.46  ? 515 ASP   A C   1 
ATOM   1225 O  O   . ASP   A 1 151 ? -40.964 19.461  33.997  1.00 30.65  ? 515 ASP   A O   1 
ATOM   1226 C  CB  . ASP   A 1 151 ? -43.915 20.199  34.184  1.00 41.38  ? 515 ASP   A CB  1 
ATOM   1227 C  CG  . ASP   A 1 151 ? -44.984 21.273  34.139  1.00 48.72  ? 515 ASP   A CG  1 
ATOM   1228 O  OD1 . ASP   A 1 151 ? -44.787 22.268  33.394  1.00 46.80  ? 515 ASP   A OD1 1 
ATOM   1229 O  OD2 . ASP   A 1 151 ? -46.002 21.102  34.825  1.00 51.10  ? 515 ASP   A OD2 1 
ATOM   1230 N  N   . GLU   A 1 152 ? -41.892 18.171  32.413  1.00 29.50  ? 516 GLU   A N   1 
ATOM   1231 C  CA  . GLU   A 1 152 ? -40.837 17.131  32.453  1.00 30.16  ? 516 GLU   A CA  1 
ATOM   1232 C  C   . GLU   A 1 152 ? -39.465 17.784  32.243  1.00 27.58  ? 516 GLU   A C   1 
ATOM   1233 O  O   . GLU   A 1 152 ? -38.484 17.278  32.830  1.00 29.49  ? 516 GLU   A O   1 
ATOM   1234 C  CB  . GLU   A 1 152 ? -41.105 16.066  31.386  1.00 32.66  ? 516 GLU   A CB  1 
ATOM   1235 C  CG  . GLU   A 1 152 ? -42.206 15.087  31.760  1.00 34.72  ? 516 GLU   A CG  1 
ATOM   1236 C  CD  . GLU   A 1 152 ? -43.641 15.509  31.488  1.00 36.03  ? 516 GLU   A CD  1 
ATOM   1237 O  OE1 . GLU   A 1 152 ? -43.870 16.675  31.107  1.00 35.27  ? 516 GLU   A OE1 1 
ATOM   1238 O  OE2 . GLU   A 1 152 ? -44.533 14.637  31.592  1.00 37.25  ? 516 GLU   A OE2 1 
ATOM   1239 N  N   . ILE   A 1 153 ? -39.352 18.840  31.429  1.00 28.63  ? 517 ILE   A N   1 
ATOM   1240 C  CA  . ILE   A 1 153 ? -37.994 19.434  31.186  1.00 29.54  ? 517 ILE   A CA  1 
ATOM   1241 C  C   . ILE   A 1 153 ? -37.355 19.847  32.529  1.00 31.44  ? 517 ILE   A C   1 
ATOM   1242 O  O   . ILE   A 1 153 ? -36.084 19.686  32.702  1.00 28.54  ? 517 ILE   A O   1 
ATOM   1243 C  CB  . ILE   A 1 153 ? -38.006 20.580  30.154  1.00 29.49  ? 517 ILE   A CB  1 
ATOM   1244 C  CG1 . ILE   A 1 153 ? -36.574 20.950  29.728  1.00 29.51  ? 517 ILE   A CG1 1 
ATOM   1245 C  CG2 . ILE   A 1 153 ? -38.759 21.787  30.683  1.00 31.28  ? 517 ILE   A CG2 1 
ATOM   1246 C  CD1 . ILE   A 1 153 ? -35.854 19.921  28.899  1.00 30.77  ? 517 ILE   A CD1 1 
ATOM   1247 N  N   . TYR   A 1 154 ? -38.152 20.346  33.488  1.00 30.20  ? 518 TYR   A N   1 
ATOM   1248 C  CA  . TYR   A 1 154 ? -37.617 20.849  34.786  1.00 28.48  ? 518 TYR   A CA  1 
ATOM   1249 C  C   . TYR   A 1 154 ? -37.057 19.680  35.587  1.00 26.45  ? 518 TYR   A C   1 
ATOM   1250 O  O   . TYR   A 1 154 ? -35.991 19.836  36.193  1.00 27.36  ? 518 TYR   A O   1 
ATOM   1251 C  CB  . TYR   A 1 154 ? -38.654 21.674  35.560  1.00 28.66  ? 518 TYR   A CB  1 
ATOM   1252 C  CG  . TYR   A 1 154 ? -39.125 22.885  34.808  1.00 29.91  ? 518 TYR   A CG  1 
ATOM   1253 C  CD1 . TYR   A 1 154 ? -38.385 24.054  34.793  1.00 28.22  ? 518 TYR   A CD1 1 
ATOM   1254 C  CD2 . TYR   A 1 154 ? -40.307 22.857  34.091  1.00 30.16  ? 518 TYR   A CD2 1 
ATOM   1255 C  CE1 . TYR   A 1 154 ? -38.808 25.147  34.070  1.00 29.16  ? 518 TYR   A CE1 1 
ATOM   1256 C  CE2 . TYR   A 1 154 ? -40.753 23.951  33.380  1.00 31.75  ? 518 TYR   A CE2 1 
ATOM   1257 C  CZ  . TYR   A 1 154 ? -39.996 25.108  33.366  1.00 30.79  ? 518 TYR   A CZ  1 
ATOM   1258 O  OH  . TYR   A 1 154 ? -40.432 26.176  32.638  1.00 33.15  ? 518 TYR   A OH  1 
ATOM   1259 N  N   . GLY   A 1 155 ? -37.710 18.512  35.565  1.00 27.37  ? 519 GLY   A N   1 
ATOM   1260 C  CA  . GLY   A 1 155 ? -37.160 17.312  36.222  1.00 28.15  ? 519 GLY   A CA  1 
ATOM   1261 C  C   . GLY   A 1 155 ? -35.858 16.835  35.600  1.00 28.39  ? 519 GLY   A C   1 
ATOM   1262 O  O   . GLY   A 1 155 ? -34.911 16.492  36.356  1.00 31.60  ? 519 GLY   A O   1 
ATOM   1263 N  N   . MET   A 1 156 ? -35.792 16.760  34.276  1.00 29.56  ? 520 MET   A N   1 
ATOM   1264 C  CA  . MET   A 1 156 ? -34.537 16.389  33.558  1.00 27.49  ? 520 MET   A CA  1 
ATOM   1265 C  C   . MET   A 1 156 ? -33.416 17.345  33.984  1.00 26.14  ? 520 MET   A C   1 
ATOM   1266 O  O   . MET   A 1 156 ? -32.306 16.904  34.333  1.00 27.96  ? 520 MET   A O   1 
ATOM   1267 C  CB  . MET   A 1 156 ? -34.744 16.484  32.050  1.00 28.55  ? 520 MET   A CB  1 
ATOM   1268 C  CG  . MET   A 1 156 ? -35.721 15.477  31.515  1.00 31.48  ? 520 MET   A CG  1 
ATOM   1269 S  SD  . MET   A 1 156 ? -36.141 15.755  29.778  1.00 34.85  ? 520 MET   A SD  1 
ATOM   1270 C  CE  . MET   A 1 156 ? -34.513 15.564  29.070  1.00 28.38  ? 520 MET   A CE  1 
ATOM   1271 N  N   . ILE   A 1 157 ? -33.716 18.639  34.038  1.00 28.24  ? 521 ILE   A N   1 
ATOM   1272 C  CA  . ILE   A 1 157 ? -32.679 19.660  34.353  1.00 28.81  ? 521 ILE   A CA  1 
ATOM   1273 C  C   . ILE   A 1 157 ? -32.253 19.515  35.810  1.00 27.26  ? 521 ILE   A C   1 
ATOM   1274 O  O   . ILE   A 1 157 ? -31.057 19.684  36.109  1.00 29.60  ? 521 ILE   A O   1 
ATOM   1275 C  CB  . ILE   A 1 157 ? -33.173 21.067  33.974  1.00 28.99  ? 521 ILE   A CB  1 
ATOM   1276 C  CG1 . ILE   A 1 157 ? -33.261 21.175  32.452  1.00 27.44  ? 521 ILE   A CG1 1 
ATOM   1277 C  CG2 . ILE   A 1 157 ? -32.287 22.140  34.572  1.00 28.33  ? 521 ILE   A CG2 1 
ATOM   1278 C  CD1 . ILE   A 1 157 ? -33.821 22.460  31.948  1.00 25.79  ? 521 ILE   A CD1 1 
ATOM   1279 N  N   . GLU   A 1 158 ? -33.192 19.219  36.706  1.00 31.80  ? 522 GLU   A N   1 
ATOM   1280 C  CA  . GLU   A 1 158 ? -32.884 19.109  38.148  1.00 30.60  ? 522 GLU   A CA  1 
ATOM   1281 C  C   . GLU   A 1 158 ? -31.995 17.879  38.341  1.00 30.69  ? 522 GLU   A C   1 
ATOM   1282 O  O   . GLU   A 1 158 ? -31.072 17.958  39.161  1.00 33.91  ? 522 GLU   A O   1 
ATOM   1283 C  CB  . GLU   A 1 158 ? -34.170 19.020  38.990  1.00 33.03  ? 522 GLU   A CB  1 
ATOM   1284 C  CG  . GLU   A 1 158 ? -33.944 19.455  40.433  1.00 39.46  ? 522 GLU   A CG  1 
ATOM   1285 C  CD  . GLU   A 1 158 ? -33.267 20.815  40.668  1.00 41.88  ? 522 GLU   A CD  1 
ATOM   1286 O  OE1 . GLU   A 1 158 ? -33.444 21.795  39.821  1.00 38.35  ? 522 GLU   A OE1 1 
ATOM   1287 O  OE2 . GLU   A 1 158 ? -32.577 20.922  41.715  1.00 41.59  ? 522 GLU   A OE2 1 
ATOM   1288 N  N   . ARG   A 1 159 ? -32.308 16.771  37.650  1.00 30.76  ? 523 ARG   A N   1 
ATOM   1289 C  CA  . ARG   A 1 159 ? -31.543 15.507  37.807  1.00 33.25  ? 523 ARG   A CA  1 
ATOM   1290 C  C   . ARG   A 1 159 ? -30.146 15.757  37.271  1.00 30.60  ? 523 ARG   A C   1 
ATOM   1291 O  O   . ARG   A 1 159 ? -29.182 15.243  37.855  1.00 33.61  ? 523 ARG   A O   1 
ATOM   1292 C  CB  . ARG   A 1 159 ? -32.259 14.324  37.159  1.00 33.29  ? 523 ARG   A CB  1 
ATOM   1293 C  CG  . ARG   A 1 159 ? -33.495 13.895  37.948  1.00 34.39  ? 523 ARG   A CG  1 
ATOM   1294 C  CD  . ARG   A 1 159 ? -34.078 12.600  37.414  1.00 32.54  ? 523 ARG   A CD  1 
ATOM   1295 N  NE  . ARG   A 1 159 ? -34.702 12.786  36.120  1.00 30.15  ? 523 ARG   A NE  1 
ATOM   1296 C  CZ  . ARG   A 1 159 ? -35.927 13.254  35.911  1.00 30.22  ? 523 ARG   A CZ  1 
ATOM   1297 N  NH1 . ARG   A 1 159 ? -36.712 13.627  36.920  1.00 31.31  ? 523 ARG   A NH1 1 
ATOM   1298 N  NH2 . ARG   A 1 159 ? -36.390 13.346  34.680  1.00 28.21  ? 523 ARG   A NH2 1 
ATOM   1299 N  N   . LEU   A 1 160 ? -30.053 16.556  36.210  1.00 31.55  ? 524 LEU   A N   1 
ATOM   1300 C  CA  . LEU   A 1 160 ? -28.757 16.858  35.551  1.00 30.54  ? 524 LEU   A CA  1 
ATOM   1301 C  C   . LEU   A 1 160 ? -27.896 17.681  36.506  1.00 29.07  ? 524 LEU   A C   1 
ATOM   1302 O  O   . LEU   A 1 160 ? -26.685 17.432  36.569  1.00 32.39  ? 524 LEU   A O   1 
ATOM   1303 C  CB  . LEU   A 1 160 ? -29.032 17.605  34.240  1.00 30.41  ? 524 LEU   A CB  1 
ATOM   1304 C  CG  . LEU   A 1 160 ? -27.777 18.089  33.522  1.00 29.11  ? 524 LEU   A CG  1 
ATOM   1305 C  CD1 . LEU   A 1 160 ? -26.889 16.910  33.134  1.00 29.71  ? 524 LEU   A CD1 1 
ATOM   1306 C  CD2 . LEU   A 1 160 ? -28.118 18.916  32.308  1.00 28.28  ? 524 LEU   A CD2 1 
ATOM   1307 N  N   . SER   A 1 161 ? -28.501 18.630  37.212  1.00 31.10  ? 525 SER   A N   1 
ATOM   1308 C  CA  . SER   A 1 161 ? -27.828 19.688  38.007  1.00 32.37  ? 525 SER   A CA  1 
ATOM   1309 C  C   . SER   A 1 161 ? -28.651 19.984  39.260  1.00 32.42  ? 525 SER   A C   1 
ATOM   1310 O  O   . SER   A 1 161 ? -29.277 21.040  39.341  1.00 29.68  ? 525 SER   A O   1 
ATOM   1311 C  CB  . SER   A 1 161 ? -27.680 20.932  37.182  1.00 32.74  ? 525 SER   A CB  1 
ATOM   1312 O  OG  . SER   A 1 161 ? -26.800 21.883  37.774  1.00 34.37  ? 525 SER   A OG  1 
ATOM   1313 N  N   . PRO   A 1 162 ? -28.706 19.055  40.244  1.00 38.35  ? 526 PRO   A N   1 
ATOM   1314 C  CA  . PRO   A 1 162 ? -29.544 19.250  41.434  1.00 38.33  ? 526 PRO   A CA  1 
ATOM   1315 C  C   . PRO   A 1 162 ? -29.027 20.389  42.327  1.00 34.19  ? 526 PRO   A C   1 
ATOM   1316 O  O   . PRO   A 1 162 ? -27.853 20.490  42.570  1.00 33.83  ? 526 PRO   A O   1 
ATOM   1317 C  CB  . PRO   A 1 162 ? -29.531 17.881  42.155  1.00 42.32  ? 526 PRO   A CB  1 
ATOM   1318 C  CG  . PRO   A 1 162 ? -28.303 17.146  41.614  1.00 41.66  ? 526 PRO   A CG  1 
ATOM   1319 C  CD  . PRO   A 1 162 ? -27.973 17.770  40.263  1.00 39.38  ? 526 PRO   A CD  1 
ATOM   1320 N  N   . GLY   A 1 163 ? -29.933 21.275  42.725  1.00 37.13  ? 527 GLY   A N   1 
ATOM   1321 C  CA  . GLY   A 1 163 ? -29.696 22.285  43.767  1.00 39.68  ? 527 GLY   A CA  1 
ATOM   1322 C  C   . GLY   A 1 163 ? -29.041 23.554  43.264  1.00 39.79  ? 527 GLY   A C   1 
ATOM   1323 O  O   . GLY   A 1 163 ? -28.948 24.505  44.057  1.00 39.38  ? 527 GLY   A O   1 
ATOM   1324 N  N   . THR   A 1 164 ? -28.617 23.600  42.000  1.00 36.63  ? 528 THR   A N   1 
ATOM   1325 C  CA  . THR   A 1 164 ? -27.919 24.765  41.392  1.00 34.29  ? 528 THR   A CA  1 
ATOM   1326 C  C   . THR   A 1 164 ? -28.942 25.827  41.013  1.00 31.62  ? 528 THR   A C   1 
ATOM   1327 O  O   . THR   A 1 164 ? -30.117 25.481  40.743  1.00 34.32  ? 528 THR   A O   1 
ATOM   1328 C  CB  . THR   A 1 164 ? -27.085 24.317  40.184  1.00 33.86  ? 528 THR   A CB  1 
ATOM   1329 O  OG1 . THR   A 1 164 ? -27.970 23.707  39.220  1.00 32.11  ? 528 THR   A OG1 1 
ATOM   1330 C  CG2 . THR   A 1 164 ? -25.969 23.382  40.608  1.00 34.18  ? 528 THR   A CG2 1 
ATOM   1331 N  N   . ARG   A 1 165 ? -28.532 27.088  40.984  1.00 32.52  ? 529 ARG   A N   1 
ATOM   1332 C  CA  . ARG   A 1 165 ? -29.408 28.178  40.503  1.00 36.01  ? 529 ARG   A CA  1 
ATOM   1333 C  C   . ARG   A 1 165 ? -29.530 28.131  38.968  1.00 37.60  ? 529 ARG   A C   1 
ATOM   1334 O  O   . ARG   A 1 165 ? -28.562 27.815  38.235  1.00 32.64  ? 529 ARG   A O   1 
ATOM   1335 C  CB  . ARG   A 1 165 ? -29.003 29.537  41.089  1.00 40.15  ? 529 ARG   A CB  1 
ATOM   1336 C  CG  . ARG   A 1 165 ? -27.581 29.989  40.815  1.00 42.81  ? 529 ARG   A CG  1 
ATOM   1337 C  CD  . ARG   A 1 165 ? -27.222 31.119  41.762  1.00 36.17  ? 529 ARG   A CD  1 
ATOM   1338 N  NE  . ARG   A 1 165 ? -28.208 32.177  41.772  1.00 35.44  ? 529 ARG   A NE  1 
ATOM   1339 C  CZ  . ARG   A 1 165 ? -28.165 33.303  41.048  1.00 34.18  ? 529 ARG   A CZ  1 
ATOM   1340 N  NH1 . ARG   A 1 165 ? -27.197 33.548  40.175  1.00 36.52  ? 529 ARG   A NH1 1 
ATOM   1341 N  NH2 . ARG   A 1 165 ? -29.127 34.181  41.177  1.00 34.47  ? 529 ARG   A NH2 1 
ATOM   1342 N  N   . LYS   A 1 166 ? -30.740 28.385  38.496  1.00 33.72  ? 530 LYS   A N   1 
ATOM   1343 C  CA  . LYS   A 1 166 ? -31.128 28.263  37.072  1.00 33.41  ? 530 LYS   A CA  1 
ATOM   1344 C  C   . LYS   A 1 166 ? -31.910 29.504  36.656  1.00 36.28  ? 530 LYS   A C   1 
ATOM   1345 O  O   . LYS   A 1 166 ? -32.534 30.184  37.524  1.00 32.57  ? 530 LYS   A O   1 
ATOM   1346 C  CB  . LYS   A 1 166 ? -31.912 26.956  36.887  1.00 33.85  ? 530 LYS   A CB  1 
ATOM   1347 C  CG  . LYS   A 1 166 ? -31.090 25.732  37.269  1.00 33.91  ? 530 LYS   A CG  1 
ATOM   1348 C  CD  . LYS   A 1 166 ? -31.817 24.439  37.440  1.00 33.76  ? 530 LYS   A CD  1 
ATOM   1349 C  CE  . LYS   A 1 166 ? -30.907 23.308  37.870  1.00 34.06  ? 530 LYS   A CE  1 
ATOM   1350 N  NZ  . LYS   A 1 166 ? -30.825 23.192  39.345  1.00 34.59  ? 530 LYS   A NZ  1 
ATOM   1351 N  N   . ILE   A 1 167 ? -31.880 29.835  35.369  1.00 31.18  ? 531 ILE   A N   1 
ATOM   1352 C  CA  . ILE   A 1 167 ? -32.650 30.995  34.888  1.00 29.94  ? 531 ILE   A CA  1 
ATOM   1353 C  C   . ILE   A 1 167 ? -33.440 30.575  33.651  1.00 31.93  ? 531 ILE   A C   1 
ATOM   1354 O  O   . ILE   A 1 167 ? -32.871 29.859  32.805  1.00 32.35  ? 531 ILE   A O   1 
ATOM   1355 C  CB  . ILE   A 1 167 ? -31.758 32.226  34.646  1.00 28.73  ? 531 ILE   A CB  1 
ATOM   1356 C  CG1 . ILE   A 1 167 ? -32.655 33.410  34.295  1.00 30.57  ? 531 ILE   A CG1 1 
ATOM   1357 C  CG2 . ILE   A 1 167 ? -30.716 31.949  33.572  1.00 27.67  ? 531 ILE   A CG2 1 
ATOM   1358 C  CD1 . ILE   A 1 167 ? -31.962 34.738  34.218  1.00 33.31  ? 531 ILE   A CD1 1 
ATOM   1359 N  N   . GLU   A 1 168 ? -34.692 31.035  33.569  1.00 27.34  ? 532 GLU   A N   1 
ATOM   1360 C  CA  . GLU   A 1 168 ? -35.585 30.838  32.411  1.00 27.16  ? 532 GLU   A CA  1 
ATOM   1361 C  C   . GLU   A 1 168 ? -35.925 32.172  31.787  1.00 29.15  ? 532 GLU   A C   1 
ATOM   1362 O  O   . GLU   A 1 168 ? -36.365 33.112  32.525  1.00 31.69  ? 532 GLU   A O   1 
ATOM   1363 C  CB  . GLU   A 1 168 ? -36.874 30.139  32.828  1.00 28.53  ? 532 GLU   A CB  1 
ATOM   1364 C  CG  . GLU   A 1 168 ? -37.758 29.903  31.650  1.00 28.81  ? 532 GLU   A CG  1 
ATOM   1365 C  CD  . GLU   A 1 168 ? -38.878 28.893  31.832  1.00 26.41  ? 532 GLU   A CD  1 
ATOM   1366 O  OE1 . GLU   A 1 168 ? -38.977 28.275  32.882  1.00 27.88  ? 532 GLU   A OE1 1 
ATOM   1367 O  OE2 . GLU   A 1 168 ? -39.576 28.686  30.851  1.00 34.68  ? 532 GLU   A OE2 1 
ATOM   1368 N  N   . LEU   A 1 169 ? -35.777 32.246  30.469  1.00 27.66  ? 533 LEU   A N   1 
ATOM   1369 C  CA  . LEU   A 1 169 ? -36.218 33.382  29.630  1.00 26.07  ? 533 LEU   A CA  1 
ATOM   1370 C  C   . LEU   A 1 169 ? -37.468 33.006  28.844  1.00 28.80  ? 533 LEU   A C   1 
ATOM   1371 O  O   . LEU   A 1 169 ? -37.467 31.960  28.195  1.00 27.21  ? 533 LEU   A O   1 
ATOM   1372 C  CB  . LEU   A 1 169 ? -35.095 33.794  28.674  1.00 27.70  ? 533 LEU   A CB  1 
ATOM   1373 C  CG  . LEU   A 1 169 ? -33.994 34.679  29.275  1.00 33.54  ? 533 LEU   A CG  1 
ATOM   1374 C  CD1 . LEU   A 1 169 ? -33.158 33.940  30.282  1.00 35.49  ? 533 LEU   A CD1 1 
ATOM   1375 C  CD2 . LEU   A 1 169 ? -33.086 35.239  28.194  1.00 34.63  ? 533 LEU   A CD2 1 
ATOM   1376 N  N   . PHE   A 1 170 ? -38.471 33.888  28.870  1.00 28.13  ? 534 PHE   A N   1 
ATOM   1377 C  CA  . PHE   A 1 170 ? -39.743 33.821  28.099  1.00 25.95  ? 534 PHE   A CA  1 
ATOM   1378 C  C   . PHE   A 1 170 ? -40.649 32.769  28.741  1.00 27.83  ? 534 PHE   A C   1 
ATOM   1379 O  O   . PHE   A 1 170 ? -41.431 32.101  28.030  1.00 30.01  ? 534 PHE   A O   1 
ATOM   1380 C  CB  . PHE   A 1 170 ? -39.472 33.548  26.631  1.00 26.01  ? 534 PHE   A CB  1 
ATOM   1381 C  CG  . PHE   A 1 170 ? -38.513 34.533  25.996  1.00 30.30  ? 534 PHE   A CG  1 
ATOM   1382 C  CD1 . PHE   A 1 170 ? -38.941 35.797  25.638  1.00 31.80  ? 534 PHE   A CD1 1 
ATOM   1383 C  CD2 . PHE   A 1 170 ? -37.204 34.188  25.715  1.00 29.08  ? 534 PHE   A CD2 1 
ATOM   1384 C  CE1 . PHE   A 1 170 ? -38.088 36.706  25.034  1.00 31.70  ? 534 PHE   A CE1 1 
ATOM   1385 C  CE2 . PHE   A 1 170 ? -36.353 35.100  25.117  1.00 33.88  ? 534 PHE   A CE2 1 
ATOM   1386 C  CZ  . PHE   A 1 170 ? -36.795 36.357  24.769  1.00 33.59  ? 534 PHE   A CZ  1 
ATOM   1387 N  N   . GLY   A 1 171 ? -40.551 32.682  30.054  1.00 28.90  ? 535 GLY   A N   1 
ATOM   1388 C  CA  . GLY   A 1 171 ? -41.374 31.806  30.901  1.00 31.45  ? 535 GLY   A CA  1 
ATOM   1389 C  C   . GLY   A 1 171 ? -42.721 32.425  31.191  1.00 37.11  ? 535 GLY   A C   1 
ATOM   1390 O  O   . GLY   A 1 171 ? -42.831 33.675  31.214  1.00 36.12  ? 535 GLY   A O   1 
ATOM   1391 N  N   . ARG   A 1 172 ? -43.719 31.570  31.409  1.00 41.95  ? 536 ARG   A N   1 
ATOM   1392 C  CA  . ARG   A 1 172 ? -45.064 31.973  31.868  1.00 40.80  ? 536 ARG   A CA  1 
ATOM   1393 C  C   . ARG   A 1 172 ? -45.160 31.764  33.378  1.00 37.43  ? 536 ARG   A C   1 
ATOM   1394 O  O   . ARG   A 1 172 ? -44.314 31.133  34.012  1.00 33.60  ? 536 ARG   A O   1 
ATOM   1395 C  CB  . ARG   A 1 172 ? -46.105 31.170  31.095  1.00 49.26  ? 536 ARG   A CB  1 
ATOM   1396 C  CG  . ARG   A 1 172 ? -46.322 31.672  29.678  1.00 55.68  ? 536 ARG   A CG  1 
ATOM   1397 C  CD  . ARG   A 1 172 ? -47.748 31.411  29.238  1.00 60.39  ? 536 ARG   A CD  1 
ATOM   1398 N  NE  . ARG   A 1 172 ? -47.838 30.256  28.370  1.00 66.64  ? 536 ARG   A NE  1 
ATOM   1399 C  CZ  . ARG   A 1 172 ? -48.972 29.614  28.081  1.00 70.72  ? 536 ARG   A CZ  1 
ATOM   1400 N  NH1 . ARG   A 1 172 ? -50.115 30.011  28.620  1.00 63.05  ? 536 ARG   A NH1 1 
ATOM   1401 N  NH2 . ARG   A 1 172 ? -48.958 28.576  27.257  1.00 67.24  ? 536 ARG   A NH2 1 
ATOM   1402 N  N   . PRO   A 1 173 ? -46.206 32.318  34.025  1.00 38.40  ? 537 PRO   A N   1 
ATOM   1403 C  CA  . PRO   A 1 173 ? -46.367 32.153  35.470  1.00 35.57  ? 537 PRO   A CA  1 
ATOM   1404 C  C   . PRO   A 1 173 ? -46.402 30.706  35.987  1.00 32.06  ? 537 PRO   A C   1 
ATOM   1405 O  O   . PRO   A 1 173 ? -45.876 30.434  37.055  1.00 33.47  ? 537 PRO   A O   1 
ATOM   1406 C  CB  . PRO   A 1 173 ? -47.746 32.806  35.713  1.00 40.13  ? 537 PRO   A CB  1 
ATOM   1407 C  CG  . PRO   A 1 173 ? -47.862 33.853  34.632  1.00 41.33  ? 537 PRO   A CG  1 
ATOM   1408 C  CD  . PRO   A 1 173 ? -47.175 33.250  33.423  1.00 37.44  ? 537 PRO   A CD  1 
ATOM   1409 N  N   . HIS   A 1 174 ? -47.028 29.784  35.249  1.00 37.22  ? 538 HIS   A N   1 
ATOM   1410 C  CA  . HIS   A 1 174 ? -47.012 28.332  35.606  1.00 39.67  ? 538 HIS   A CA  1 
ATOM   1411 C  C   . HIS   A 1 174 ? -45.569 27.794  35.680  1.00 37.88  ? 538 HIS   A C   1 
ATOM   1412 O  O   . HIS   A 1 174 ? -45.325 26.825  36.420  1.00 37.62  ? 538 HIS   A O   1 
ATOM   1413 C  CB  . HIS   A 1 174 ? -47.882 27.526  34.633  1.00 50.49  ? 538 HIS   A CB  1 
ATOM   1414 C  CG  . HIS   A 1 174 ? -47.935 26.071  34.975  1.00 66.37  ? 538 HIS   A CG  1 
ATOM   1415 N  ND1 . HIS   A 1 174 ? -47.481 25.084  34.102  1.00 75.12  ? 538 HIS   A ND1 1 
ATOM   1416 C  CD2 . HIS   A 1 174 ? -48.340 25.427  36.096  1.00 71.53  ? 538 HIS   A CD2 1 
ATOM   1417 C  CE1 . HIS   A 1 174 ? -47.623 23.899  34.669  1.00 72.88  ? 538 HIS   A CE1 1 
ATOM   1418 N  NE2 . HIS   A 1 174 ? -48.151 24.079  35.892  1.00 71.00  ? 538 HIS   A NE2 1 
ATOM   1419 N  N   . ASN   A 1 175 ? -44.615 28.437  34.996  1.00 36.80  ? 539 ASN   A N   1 
ATOM   1420 C  CA  . ASN   A 1 175 ? -43.209 27.939  34.863  1.00 35.46  ? 539 ASN   A CA  1 
ATOM   1421 C  C   . ASN   A 1 175 ? -42.361 28.271  36.081  1.00 36.28  ? 539 ASN   A C   1 
ATOM   1422 O  O   . ASN   A 1 175 ? -41.256 27.713  36.188  1.00 31.13  ? 539 ASN   A O   1 
ATOM   1423 C  CB  . ASN   A 1 175 ? -42.564 28.500  33.599  1.00 36.52  ? 539 ASN   A CB  1 
ATOM   1424 C  CG  . ASN   A 1 175 ? -43.266 28.012  32.351  1.00 33.97  ? 539 ASN   A CG  1 
ATOM   1425 O  OD1 . ASN   A 1 175 ? -43.432 28.741  31.379  1.00 38.89  ? 539 ASN   A OD1 1 
ATOM   1426 N  ND2 . ASN   A 1 175 ? -43.781 26.792  32.392  1.00 40.67  ? 539 ASN   A ND2 1 
ATOM   1427 N  N   . VAL   A 1 176 ? -42.816 29.150  36.990  1.00 38.89  ? 540 VAL   A N   1 
ATOM   1428 C  CA  . VAL   A 1 176 ? -41.969 29.537  38.156  1.00 39.62  ? 540 VAL   A CA  1 
ATOM   1429 C  C   . VAL   A 1 176 ? -41.749 28.261  38.959  1.00 40.94  ? 540 VAL   A C   1 
ATOM   1430 O  O   . VAL   A 1 176 ? -42.681 27.459  39.003  1.00 39.14  ? 540 VAL   A O   1 
ATOM   1431 C  CB  . VAL   A 1 176 ? -42.561 30.703  38.980  1.00 40.73  ? 540 VAL   A CB  1 
ATOM   1432 C  CG1 . VAL   A 1 176 ? -42.774 31.903  38.074  1.00 38.93  ? 540 VAL   A CG1 1 
ATOM   1433 C  CG2 . VAL   A 1 176 ? -43.865 30.329  39.713  1.00 39.81  ? 540 VAL   A CG2 1 
ATOM   1434 N  N   . GLN   A 1 177 ? -40.541 28.048  39.487  1.00 39.71  ? 541 GLN   A N   1 
ATOM   1435 C  CA  . GLN   A 1 177 ? -40.097 26.774  40.113  1.00 42.44  ? 541 GLN   A CA  1 
ATOM   1436 C  C   . GLN   A 1 177 ? -39.043 27.072  41.160  1.00 44.05  ? 541 GLN   A C   1 
ATOM   1437 O  O   . GLN   A 1 177 ? -38.246 28.002  40.985  1.00 41.78  ? 541 GLN   A O   1 
ATOM   1438 C  CB  . GLN   A 1 177 ? -39.324 25.846  39.168  1.00 44.08  ? 541 GLN   A CB  1 
ATOM   1439 C  CG  . GLN   A 1 177 ? -39.942 25.648  37.806  1.00 47.83  ? 541 GLN   A CG  1 
ATOM   1440 C  CD  . GLN   A 1 177 ? -40.901 24.496  37.837  1.00 57.54  ? 541 GLN   A CD  1 
ATOM   1441 O  OE1 . GLN   A 1 177 ? -40.890 23.695  38.776  1.00 62.70  ? 541 GLN   A OE1 1 
ATOM   1442 N  NE2 . GLN   A 1 177 ? -41.746 24.430  36.821  1.00 57.07  ? 541 GLN   A NE2 1 
ATOM   1443 N  N   . PRO   A 1 178 ? -38.894 26.221  42.197  1.00 42.46  ? 542 PRO   A N   1 
ATOM   1444 C  CA  . PRO   A 1 178 ? -37.774 26.370  43.121  1.00 42.78  ? 542 PRO   A CA  1 
ATOM   1445 C  C   . PRO   A 1 178 ? -36.438 26.246  42.363  1.00 45.84  ? 542 PRO   A C   1 
ATOM   1446 O  O   . PRO   A 1 178 ? -36.348 25.426  41.445  1.00 43.22  ? 542 PRO   A O   1 
ATOM   1447 C  CB  . PRO   A 1 178 ? -37.952 25.216  44.120  1.00 44.01  ? 542 PRO   A CB  1 
ATOM   1448 C  CG  . PRO   A 1 178 ? -39.411 24.845  43.994  1.00 42.85  ? 542 PRO   A CG  1 
ATOM   1449 C  CD  . PRO   A 1 178 ? -39.761 25.082  42.541  1.00 45.59  ? 542 PRO   A CD  1 
ATOM   1450 N  N   . ASN   A 1 179 ? -35.461 27.068  42.756  1.00 42.01  ? 543 ASN   A N   1 
ATOM   1451 C  CA  . ASN   A 1 179 ? -34.075 27.128  42.225  1.00 43.92  ? 543 ASN   A CA  1 
ATOM   1452 C  C   . ASN   A 1 179 ? -34.038 27.913  40.909  1.00 39.12  ? 543 ASN   A C   1 
ATOM   1453 O  O   . ASN   A 1 179 ? -32.924 28.112  40.378  1.00 43.73  ? 543 ASN   A O   1 
ATOM   1454 C  CB  . ASN   A 1 179 ? -33.477 25.730  42.038  1.00 43.59  ? 543 ASN   A CB  1 
ATOM   1455 C  CG  . ASN   A 1 179 ? -33.078 25.089  43.350  1.00 48.32  ? 543 ASN   A CG  1 
ATOM   1456 O  OD1 . ASN   A 1 179 ? -32.674 25.782  44.283  1.00 48.59  ? 543 ASN   A OD1 1 
ATOM   1457 N  ND2 . ASN   A 1 179 ? -33.167 23.764  43.414  1.00 52.37  ? 543 ASN   A ND2 1 
ATOM   1458 N  N   . TRP   A 1 180 ? -35.190 28.293  40.368  1.00 33.62  ? 544 TRP   A N   1 
ATOM   1459 C  CA  . TRP   A 1 180 ? -35.283 29.089  39.121  1.00 33.65  ? 544 TRP   A CA  1 
ATOM   1460 C  C   . TRP   A 1 180 ? -35.646 30.553  39.396  1.00 36.23  ? 544 TRP   A C   1 
ATOM   1461 O  O   . TRP   A 1 180 ? -36.553 30.817  40.165  1.00 37.55  ? 544 TRP   A O   1 
ATOM   1462 C  CB  . TRP   A 1 180 ? -36.291 28.509  38.145  1.00 31.65  ? 544 TRP   A CB  1 
ATOM   1463 C  CG  . TRP   A 1 180 ? -35.859 27.217  37.519  1.00 32.95  ? 544 TRP   A CG  1 
ATOM   1464 C  CD1 . TRP   A 1 180 ? -35.850 25.999  38.126  1.00 33.76  ? 544 TRP   A CD1 1 
ATOM   1465 C  CD2 . TRP   A 1 180 ? -35.353 27.011  36.185  1.00 31.81  ? 544 TRP   A CD2 1 
ATOM   1466 N  NE1 . TRP   A 1 180 ? -35.411 25.037  37.261  1.00 34.51  ? 544 TRP   A NE1 1 
ATOM   1467 C  CE2 . TRP   A 1 180 ? -35.136 25.615  36.047  1.00 31.73  ? 544 TRP   A CE2 1 
ATOM   1468 C  CE3 . TRP   A 1 180 ? -35.129 27.841  35.079  1.00 27.71  ? 544 TRP   A CE3 1 
ATOM   1469 C  CZ2 . TRP   A 1 180 ? -34.690 25.038  34.861  1.00 29.79  ? 544 TRP   A CZ2 1 
ATOM   1470 C  CZ3 . TRP   A 1 180 ? -34.656 27.267  33.912  1.00 29.85  ? 544 TRP   A CZ3 1 
ATOM   1471 C  CH2 . TRP   A 1 180 ? -34.457 25.887  33.801  1.00 29.26  ? 544 TRP   A CH2 1 
ATOM   1472 N  N   . ILE   A 1 181 ? -35.019 31.446  38.643  1.00 35.29  ? 545 ILE   A N   1 
ATOM   1473 C  CA  . ILE   A 1 181 ? -35.530 32.818  38.398  1.00 32.05  ? 545 ILE   A CA  1 
ATOM   1474 C  C   . ILE   A 1 181 ? -36.124 32.810  37.003  1.00 31.40  ? 545 ILE   A C   1 
ATOM   1475 O  O   . ILE   A 1 181 ? -35.421 32.358  36.065  1.00 30.51  ? 545 ILE   A O   1 
ATOM   1476 C  CB  . ILE   A 1 181 ? -34.402 33.854  38.537  1.00 35.63  ? 545 ILE   A CB  1 
ATOM   1477 C  CG1 . ILE   A 1 181 ? -33.678 33.726  39.885  1.00 38.28  ? 545 ILE   A CG1 1 
ATOM   1478 C  CG2 . ILE   A 1 181 ? -34.955 35.242  38.280  1.00 36.43  ? 545 ILE   A CG2 1 
ATOM   1479 C  CD1 . ILE   A 1 181 ? -32.665 34.829  40.136  1.00 41.81  ? 545 ILE   A CD1 1 
ATOM   1480 N  N   . THR   A 1 182 ? -37.371 33.240  36.885  1.00 26.82  ? 546 THR   A N   1 
ATOM   1481 C  CA  . THR   A 1 182 ? -38.165 33.262  35.641  1.00 30.30  ? 546 THR   A CA  1 
ATOM   1482 C  C   . THR   A 1 182 ? -38.262 34.705  35.145  1.00 34.40  ? 546 THR   A C   1 
ATOM   1483 O  O   . THR   A 1 182 ? -38.657 35.603  35.955  1.00 34.39  ? 546 THR   A O   1 
ATOM   1484 C  CB  . THR   A 1 182 ? -39.556 32.629  35.865  1.00 28.06  ? 546 THR   A CB  1 
ATOM   1485 O  OG1 . THR   A 1 182 ? -39.382 31.382  36.538  1.00 33.16  ? 546 THR   A OG1 1 
ATOM   1486 C  CG2 . THR   A 1 182 ? -40.326 32.452  34.582  1.00 30.58  ? 546 THR   A CG2 1 
ATOM   1487 N  N   . LEU   A 1 183 ? -37.953 34.922  33.868  1.00 28.84  ? 547 LEU   A N   1 
ATOM   1488 C  CA  . LEU   A 1 183 ? -38.120 36.225  33.184  1.00 31.15  ? 547 LEU   A CA  1 
ATOM   1489 C  C   . LEU   A 1 183 ? -39.162 36.048  32.103  1.00 32.20  ? 547 LEU   A C   1 
ATOM   1490 O  O   . LEU   A 1 183 ? -39.104 35.042  31.408  1.00 31.28  ? 547 LEU   A O   1 
ATOM   1491 C  CB  . LEU   A 1 183 ? -36.802 36.725  32.563  1.00 33.23  ? 547 LEU   A CB  1 
ATOM   1492 C  CG  . LEU   A 1 183 ? -35.535 36.636  33.425  1.00 34.49  ? 547 LEU   A CG  1 
ATOM   1493 C  CD1 . LEU   A 1 183 ? -34.338 37.220  32.689  1.00 34.03  ? 547 LEU   A CD1 1 
ATOM   1494 C  CD2 . LEU   A 1 183 ? -35.704 37.371  34.748  1.00 38.40  ? 547 LEU   A CD2 1 
ATOM   1495 N  N   . GLY   A 1 184 ? -40.022 37.046  31.937  1.00 27.07  ? 548 GLY   A N   1 
ATOM   1496 C  CA  . GLY   A 1 184 ? -41.041 37.123  30.892  1.00 32.41  ? 548 GLY   A CA  1 
ATOM   1497 C  C   . GLY   A 1 184 ? -41.921 38.347  31.116  1.00 33.39  ? 548 GLY   A C   1 
ATOM   1498 O  O   . GLY   A 1 184 ? -41.829 38.916  32.212  1.00 33.53  ? 548 GLY   A O   1 
ATOM   1499 N  N   . ASN   A 1 185 ? -42.686 38.736  30.102  1.00 37.69  ? 549 ASN   A N   1 
ATOM   1500 C  CA  . ASN   A 1 185 ? -43.515 39.969  30.117  1.00 40.28  ? 549 ASN   A CA  1 
ATOM   1501 C  C   . ASN   A 1 185 ? -44.977 39.660  30.483  1.00 45.68  ? 549 ASN   A C   1 
ATOM   1502 O  O   . ASN   A 1 185 ? -45.775 40.594  30.388  1.00 43.94  ? 549 ASN   A O   1 
ATOM   1503 C  CB  . ASN   A 1 185 ? -43.452 40.687  28.773  1.00 37.56  ? 549 ASN   A CB  1 
ATOM   1504 C  CG  . ASN   A 1 185 ? -44.082 39.904  27.652  1.00 38.62  ? 549 ASN   A CG  1 
ATOM   1505 O  OD1 . ASN   A 1 185 ? -44.554 38.800  27.872  1.00 40.21  ? 549 ASN   A OD1 1 
ATOM   1506 N  ND2 . ASN   A 1 185 ? -44.067 40.455  26.449  1.00 39.33  ? 549 ASN   A ND2 1 
ATOM   1507 N  N   . GLN   A 1 186 ? -45.340 38.413  30.825  1.00 41.62  ? 550 GLN   A N   1 
ATOM   1508 C  CA  . GLN   A 1 186 ? -46.720 38.039  31.250  1.00 43.79  ? 550 GLN   A CA  1 
ATOM   1509 C  C   . GLN   A 1 186 ? -46.702 37.712  32.743  1.00 41.90  ? 550 GLN   A C   1 
ATOM   1510 O  O   . GLN   A 1 186 ? -47.723 37.297  33.257  1.00 42.81  ? 550 GLN   A O   1 
ATOM   1511 C  CB  . GLN   A 1 186 ? -47.264 36.821  30.498  1.00 43.16  ? 550 GLN   A CB  1 
ATOM   1512 C  CG  . GLN   A 1 186 ? -47.593 37.086  29.045  1.00 51.66  ? 550 GLN   A CG  1 
ATOM   1513 C  CD  . GLN   A 1 186 ? -47.786 35.819  28.247  1.00 52.38  ? 550 GLN   A CD  1 
ATOM   1514 O  OE1 . GLN   A 1 186 ? -47.627 35.812  27.033  1.00 56.90  ? 550 GLN   A OE1 1 
ATOM   1515 N  NE2 . GLN   A 1 186 ? -48.137 34.737  28.923  1.00 59.10  ? 550 GLN   A NE2 1 
ATOM   1516 N  N   . LEU   A 1 187 ? -45.556 37.831  33.390  1.00 37.68  ? 551 LEU   A N   1 
ATOM   1517 C  CA  . LEU   A 1 187 ? -45.417 37.546  34.836  1.00 37.13  ? 551 LEU   A CA  1 
ATOM   1518 C  C   . LEU   A 1 187 ? -46.011 38.721  35.603  1.00 37.63  ? 551 LEU   A C   1 
ATOM   1519 O  O   . LEU   A 1 187 ? -46.228 39.787  34.999  1.00 41.31  ? 551 LEU   A O   1 
ATOM   1520 C  CB  . LEU   A 1 187 ? -43.951 37.333  35.209  1.00 38.01  ? 551 LEU   A CB  1 
ATOM   1521 C  CG  . LEU   A 1 187 ? -43.230 36.257  34.390  1.00 39.62  ? 551 LEU   A CG  1 
ATOM   1522 C  CD1 . LEU   A 1 187 ? -41.845 36.005  34.933  1.00 38.41  ? 551 LEU   A CD1 1 
ATOM   1523 C  CD2 . LEU   A 1 187 ? -44.030 34.965  34.396  1.00 42.79  ? 551 LEU   A CD2 1 
ATOM   1524 N  N   . ASP   A 1 188 ? -46.257 38.512  36.887  1.00 37.08  ? 552 ASP   A N   1 
ATOM   1525 C  CA  . ASP   A 1 188 ? -46.998 39.497  37.708  1.00 40.02  ? 552 ASP   A CA  1 
ATOM   1526 C  C   . ASP   A 1 188 ? -45.988 40.186  38.630  1.00 33.59  ? 552 ASP   A C   1 
ATOM   1527 O  O   . ASP   A 1 188 ? -45.555 39.589  39.607  1.00 33.50  ? 552 ASP   A O   1 
ATOM   1528 C  CB  . ASP   A 1 188 ? -48.219 38.820  38.322  1.00 44.41  ? 552 ASP   A CB  1 
ATOM   1529 C  CG  . ASP   A 1 188 ? -49.230 39.801  38.874  1.00 45.01  ? 552 ASP   A CG  1 
ATOM   1530 O  OD1 . ASP   A 1 188 ? -48.882 41.014  39.005  1.00 43.95  ? 552 ASP   A OD1 1 
ATOM   1531 O  OD2 . ASP   A 1 188 ? -50.325 39.348  39.175  1.00 45.72  ? 552 ASP   A OD2 1 
ATOM   1532 N  N   . GLY   A 1 189 ? -45.574 41.398  38.241  1.00 40.26  ? 553 GLY   A N   1 
ATOM   1533 C  CA  . GLY   A 1 189 ? -44.553 42.203  38.943  1.00 44.15  ? 553 GLY   A CA  1 
ATOM   1534 C  C   . GLY   A 1 189 ? -43.243 41.461  39.122  1.00 44.82  ? 553 GLY   A C   1 
ATOM   1535 O  O   . GLY   A 1 189 ? -42.870 40.674  38.231  1.00 42.06  ? 553 GLY   A O   1 
ATOM   1536 N  N   . ILE   A 1 190 ? -42.586 41.689  40.256  1.00 46.49  ? 554 ILE   A N   1 
ATOM   1537 C  CA  . ILE   A 1 190 ? -41.201 41.238  40.568  1.00 49.42  ? 554 ILE   A CA  1 
ATOM   1538 C  C   . ILE   A 1 190 ? -41.254 40.506  41.907  1.00 48.78  ? 554 ILE   A C   1 
ATOM   1539 O  O   . ILE   A 1 190 ? -41.930 40.994  42.788  1.00 59.65  ? 554 ILE   A O   1 
ATOM   1540 C  CB  . ILE   A 1 190 ? -40.263 42.463  40.592  1.00 47.45  ? 554 ILE   A CB  1 
ATOM   1541 C  CG1 . ILE   A 1 190 ? -40.226 43.173  39.238  1.00 55.70  ? 554 ILE   A CG1 1 
ATOM   1542 C  CG2 . ILE   A 1 190 ? -38.873 42.097  41.069  1.00 47.93  ? 554 ILE   A CG2 1 
ATOM   1543 C  CD1 . ILE   A 1 190 ? -39.793 44.633  39.318  1.00 61.15  ? 554 ILE   A CD1 1 
ATOM   1544 N  N   . HIS   A 1 191 ? -40.584 39.369  42.047  1.00 47.35  ? 555 HIS   A N   1 
ATOM   1545 C  CA  . HIS   A 1 191 ? -40.535 38.568  43.296  1.00 47.31  ? 555 HIS   A CA  1 
ATOM   1546 C  C   . HIS   A 1 191 ? -39.127 37.987  43.454  1.00 51.50  ? 555 HIS   A C   1 
ATOM   1547 O  O   . HIS   A 1 191 ? -38.846 36.998  42.747  1.00 44.87  ? 555 HIS   A O   1 
ATOM   1548 C  CB  . HIS   A 1 191 ? -41.667 37.521  43.276  1.00 50.63  ? 555 HIS   A CB  1 
ATOM   1549 C  CG  . HIS   A 1 191 ? -41.739 36.688  44.513  1.00 53.31  ? 555 HIS   A CG  1 
ATOM   1550 N  ND1 . HIS   A 1 191 ? -41.995 37.234  45.758  1.00 64.33  ? 555 HIS   A ND1 1 
ATOM   1551 C  CD2 . HIS   A 1 191 ? -41.563 35.366  44.717  1.00 55.99  ? 555 HIS   A CD2 1 
ATOM   1552 C  CE1 . HIS   A 1 191 ? -41.963 36.280  46.670  1.00 62.86  ? 555 HIS   A CE1 1 
ATOM   1553 N  NE2 . HIS   A 1 191 ? -41.693 35.127  46.057  1.00 56.18  ? 555 HIS   A NE2 1 
ATOM   1554 N  N   . LEU   A 1 192 ? -38.310 38.567  44.356  1.00 47.04  ? 556 LEU   A N   1 
ATOM   1555 C  CA  . LEU   A 1 192 ? -36.857 38.306  44.546  1.00 46.62  ? 556 LEU   A CA  1 
ATOM   1556 C  C   . LEU   A 1 192 ? -36.532 38.100  46.034  1.00 49.69  ? 556 LEU   A C   1 
ATOM   1557 O  O   . LEU   A 1 192 ? -36.870 38.969  46.837  1.00 51.35  ? 556 LEU   A O   1 
ATOM   1558 C  CB  . LEU   A 1 192 ? -36.050 39.479  43.967  1.00 46.81  ? 556 LEU   A CB  1 
ATOM   1559 C  CG  . LEU   A 1 192 ? -36.116 39.670  42.445  1.00 48.66  ? 556 LEU   A CG  1 
ATOM   1560 C  CD1 . LEU   A 1 192 ? -35.375 40.923  41.984  1.00 42.51  ? 556 LEU   A CD1 1 
ATOM   1561 C  CD2 . LEU   A 1 192 ? -35.551 38.457  41.725  1.00 47.56  ? 556 LEU   A CD2 1 
ATOM   1562 N  N   . LEU   A 1 193 ? -35.821 37.020  46.358  1.00 46.65  ? 557 LEU   A N   1 
ATOM   1563 C  CA  . LEU   A 1 193 ? -35.533 36.547  47.733  1.00 53.45  ? 557 LEU   A CA  1 
ATOM   1564 C  C   . LEU   A 1 193 ? -34.028 36.366  47.961  1.00 56.35  ? 557 LEU   A C   1 
ATOM   1565 O  O   . LEU   A 1 193 ? -33.593 36.404  49.151  1.00 51.81  ? 557 LEU   A O   1 
ATOM   1566 C  CB  . LEU   A 1 193 ? -36.262 35.216  47.916  1.00 52.85  ? 557 LEU   A CB  1 
ATOM   1567 C  CG  . LEU   A 1 193 ? -37.715 35.182  47.437  1.00 61.97  ? 557 LEU   A CG  1 
ATOM   1568 C  CD1 . LEU   A 1 193 ? -38.303 33.790  47.649  1.00 65.88  ? 557 LEU   A CD1 1 
ATOM   1569 C  CD2 . LEU   A 1 193 ? -38.568 36.239  48.132  1.00 61.77  ? 557 LEU   A CD2 1 
ATOM   1570 N  N   . ASP   A 1 194 ? -33.266 36.074  46.898  1.00 53.97  ? 558 ASP   A N   1 
ATOM   1571 C  CA  . ASP   A 1 194 ? -31.794 35.899  46.983  1.00 54.77  ? 558 ASP   A CA  1 
ATOM   1572 C  C   . ASP   A 1 194 ? -31.200 37.243  47.383  1.00 54.30  ? 558 ASP   A C   1 
ATOM   1573 O  O   . ASP   A 1 194 ? -31.328 38.210  46.640  1.00 48.08  ? 558 ASP   A O   1 
ATOM   1574 C  CB  . ASP   A 1 194 ? -31.185 35.400  45.670  1.00 54.54  ? 558 ASP   A CB  1 
ATOM   1575 C  CG  . ASP   A 1 194 ? -29.703 35.085  45.781  1.00 54.95  ? 558 ASP   A CG  1 
ATOM   1576 O  OD1 . ASP   A 1 194 ? -29.025 35.687  46.657  1.00 54.30  ? 558 ASP   A OD1 1 
ATOM   1577 O  OD2 . ASP   A 1 194 ? -29.228 34.233  44.985  1.00 58.91  ? 558 ASP   A OD2 1 
ATOM   1578 N  N   . PRO   A 1 195 ? -30.580 37.348  48.578  1.00 59.20  ? 559 PRO   A N   1 
ATOM   1579 C  CA  . PRO   A 1 195 ? -30.078 38.631  49.067  1.00 59.59  ? 559 PRO   A CA  1 
ATOM   1580 C  C   . PRO   A 1 195 ? -29.065 39.247  48.089  1.00 50.47  ? 559 PRO   A C   1 
ATOM   1581 O  O   . PRO   A 1 195 ? -29.198 40.398  47.820  1.00 50.41  ? 559 PRO   A O   1 
ATOM   1582 C  CB  . PRO   A 1 195 ? -29.443 38.304  50.429  1.00 59.60  ? 559 PRO   A CB  1 
ATOM   1583 C  CG  . PRO   A 1 195 ? -30.064 36.984  50.833  1.00 58.81  ? 559 PRO   A CG  1 
ATOM   1584 C  CD  . PRO   A 1 195 ? -30.341 36.255  49.535  1.00 59.09  ? 559 PRO   A CD  1 
ATOM   1585 N  N   . ASP   A 1 196 ? -28.125 38.459  47.551  1.00 55.82  ? 560 ASP   A N   1 
ATOM   1586 C  CA  . ASP   A 1 196 ? -27.156 38.930  46.522  1.00 54.70  ? 560 ASP   A CA  1 
ATOM   1587 C  C   . ASP   A 1 196 ? -27.922 39.635  45.396  1.00 51.71  ? 560 ASP   A C   1 
ATOM   1588 O  O   . ASP   A 1 196 ? -27.583 40.779  45.120  1.00 49.77  ? 560 ASP   A O   1 
ATOM   1589 C  CB  . ASP   A 1 196 ? -26.287 37.792  45.985  1.00 63.12  ? 560 ASP   A CB  1 
ATOM   1590 C  CG  . ASP   A 1 196 ? -25.358 37.207  47.030  1.00 68.98  ? 560 ASP   A CG  1 
ATOM   1591 O  OD1 . ASP   A 1 196 ? -24.839 37.988  47.847  1.00 74.84  ? 560 ASP   A OD1 1 
ATOM   1592 O  OD2 . ASP   A 1 196 ? -25.172 35.974  47.020  1.00 81.00  ? 560 ASP   A OD2 1 
ATOM   1593 N  N   . VAL   A 1 197 ? -28.953 38.994  44.831  1.00 46.03  ? 561 VAL   A N   1 
ATOM   1594 C  CA  . VAL   A 1 197 ? -29.775 39.510  43.696  1.00 44.64  ? 561 VAL   A CA  1 
ATOM   1595 C  C   . VAL   A 1 197 ? -30.608 40.707  44.156  1.00 47.13  ? 561 VAL   A C   1 
ATOM   1596 O  O   . VAL   A 1 197 ? -30.804 41.650  43.358  1.00 44.13  ? 561 VAL   A O   1 
ATOM   1597 C  CB  . VAL   A 1 197 ? -30.721 38.433  43.128  1.00 39.35  ? 561 VAL   A CB  1 
ATOM   1598 C  CG1 . VAL   A 1 197 ? -31.701 39.031  42.141  1.00 39.85  ? 561 VAL   A CG1 1 
ATOM   1599 C  CG2 . VAL   A 1 197 ? -29.969 37.276  42.514  1.00 42.28  ? 561 VAL   A CG2 1 
ATOM   1600 N  N   . VAL   A 1 198 ? -31.209 40.634  45.343  1.00 52.46  ? 562 VAL   A N   1 
ATOM   1601 C  CA  . VAL   A 1 198 ? -32.071 41.760  45.818  1.00 50.06  ? 562 VAL   A CA  1 
ATOM   1602 C  C   . VAL   A 1 198 ? -31.208 43.029  45.924  1.00 46.18  ? 562 VAL   A C   1 
ATOM   1603 O  O   . VAL   A 1 198 ? -31.633 44.066  45.413  1.00 46.85  ? 562 VAL   A O   1 
ATOM   1604 C  CB  . VAL   A 1 198 ? -32.779 41.440  47.143  1.00 54.98  ? 562 VAL   A CB  1 
ATOM   1605 C  CG1 . VAL   A 1 198 ? -33.296 42.719  47.799  1.00 57.83  ? 562 VAL   A CG1 1 
ATOM   1606 C  CG2 . VAL   A 1 198 ? -33.895 40.419  46.939  1.00 53.00  ? 562 VAL   A CG2 1 
ATOM   1607 N  N   . ALA   A 1 199 ? -30.048 42.947  46.575  1.00 49.30  ? 563 ALA   A N   1 
ATOM   1608 C  CA  . ALA   A 1 199 ? -29.070 44.061  46.645  1.00 53.33  ? 563 ALA   A CA  1 
ATOM   1609 C  C   . ALA   A 1 199 ? -28.838 44.585  45.220  1.00 61.06  ? 563 ALA   A C   1 
ATOM   1610 O  O   . ALA   A 1 199 ? -29.293 45.732  44.909  1.00 60.43  ? 563 ALA   A O   1 
ATOM   1611 C  CB  . ALA   A 1 199 ? -27.784 43.600  47.287  1.00 53.27  ? 563 ALA   A CB  1 
ATOM   1612 N  N   . ARG   A 1 200 ? -28.240 43.755  44.352  1.00 53.15  ? 564 ARG   A N   1 
ATOM   1613 C  CA  . ARG   A 1 200 ? -27.786 44.215  43.010  1.00 46.50  ? 564 ARG   A CA  1 
ATOM   1614 C  C   . ARG   A 1 200 ? -29.004 44.820  42.303  1.00 43.93  ? 564 ARG   A C   1 
ATOM   1615 O  O   . ARG   A 1 200 ? -28.847 45.851  41.622  1.00 42.73  ? 564 ARG   A O   1 
ATOM   1616 C  CB  . ARG   A 1 200 ? -27.081 43.094  42.235  1.00 46.46  ? 564 ARG   A CB  1 
ATOM   1617 C  CG  . ARG   A 1 200 ? -25.630 42.885  42.642  1.00 49.40  ? 564 ARG   A CG  1 
ATOM   1618 C  CD  . ARG   A 1 200 ? -24.879 41.798  41.876  1.00 52.58  ? 564 ARG   A CD  1 
ATOM   1619 N  NE  . ARG   A 1 200 ? -25.691 40.615  41.637  1.00 56.53  ? 564 ARG   A NE  1 
ATOM   1620 C  CZ  . ARG   A 1 200 ? -25.506 39.404  42.171  1.00 61.93  ? 564 ARG   A CZ  1 
ATOM   1621 N  NH1 . ARG   A 1 200 ? -24.507 39.168  43.011  1.00 59.08  ? 564 ARG   A NH1 1 
ATOM   1622 N  NH2 . ARG   A 1 200 ? -26.343 38.423  41.864  1.00 53.26  ? 564 ARG   A NH2 1 
ATOM   1623 N  N   . PHE   A 1 201 ? -30.206 44.266  42.485  1.00 44.30  ? 565 PHE   A N   1 
ATOM   1624 C  CA  . PHE   A 1 201 ? -31.410 44.822  41.805  1.00 44.15  ? 565 PHE   A CA  1 
ATOM   1625 C  C   . PHE   A 1 201 ? -31.754 46.220  42.351  1.00 51.48  ? 565 PHE   A C   1 
ATOM   1626 O  O   . PHE   A 1 201 ? -32.110 47.155  41.575  1.00 41.51  ? 565 PHE   A O   1 
ATOM   1627 C  CB  . PHE   A 1 201 ? -32.628 43.908  41.954  1.00 48.21  ? 565 PHE   A CB  1 
ATOM   1628 C  CG  . PHE   A 1 201 ? -33.832 44.383  41.174  1.00 43.88  ? 565 PHE   A CG  1 
ATOM   1629 C  CD1 . PHE   A 1 201 ? -34.657 45.377  41.664  1.00 48.80  ? 565 PHE   A CD1 1 
ATOM   1630 C  CD2 . PHE   A 1 201 ? -34.134 43.849  39.932  1.00 54.41  ? 565 PHE   A CD2 1 
ATOM   1631 C  CE1 . PHE   A 1 201 ? -35.757 45.815  40.941  1.00 47.73  ? 565 PHE   A CE1 1 
ATOM   1632 C  CE2 . PHE   A 1 201 ? -35.235 44.283  39.210  1.00 49.22  ? 565 PHE   A CE2 1 
ATOM   1633 C  CZ  . PHE   A 1 201 ? -36.045 45.270  39.714  1.00 51.34  ? 565 PHE   A CZ  1 
ATOM   1634 N  N   . LYS   A 1 202 ? -31.766 46.357  43.679  1.00 54.27  ? 566 LYS   A N   1 
ATOM   1635 C  CA  . LYS   A 1 202 ? -32.048 47.670  44.317  1.00 60.95  ? 566 LYS   A CA  1 
ATOM   1636 C  C   . LYS   A 1 202 ? -31.072 48.692  43.724  1.00 56.69  ? 566 LYS   A C   1 
ATOM   1637 O  O   . LYS   A 1 202 ? -31.528 49.720  43.170  1.00 52.43  ? 566 LYS   A O   1 
ATOM   1638 C  CB  . LYS   A 1 202 ? -31.935 47.566  45.841  1.00 64.07  ? 566 LYS   A CB  1 
ATOM   1639 C  CG  . LYS   A 1 202 ? -33.272 47.454  46.548  1.00 69.97  ? 566 LYS   A CG  1 
ATOM   1640 C  CD  . LYS   A 1 202 ? -33.170 47.068  48.005  1.00 75.21  ? 566 LYS   A CD  1 
ATOM   1641 C  CE  . LYS   A 1 202 ? -34.498 46.550  48.508  1.00 79.65  ? 566 LYS   A CE  1 
ATOM   1642 N  NZ  . LYS   A 1 202 ? -34.419 46.152  49.927  1.00 81.68  ? 566 LYS   A NZ  1 
ATOM   1643 N  N   . GLN   A 1 203 ? -29.788 48.331  43.771  1.00 54.90  ? 567 GLN   A N   1 
ATOM   1644 C  CA  . GLN   A 1 203 ? -28.626 49.178  43.404  1.00 55.37  ? 567 GLN   A CA  1 
ATOM   1645 C  C   . GLN   A 1 203 ? -28.705 49.574  41.918  1.00 53.47  ? 567 GLN   A C   1 
ATOM   1646 O  O   . GLN   A 1 203 ? -28.346 50.690  41.632  1.00 45.06  ? 567 GLN   A O   1 
ATOM   1647 C  CB  . GLN   A 1 203 ? -27.361 48.422  43.812  1.00 61.86  ? 567 GLN   A CB  1 
ATOM   1648 C  CG  . GLN   A 1 203 ? -26.120 49.291  43.900  1.00 75.64  ? 567 GLN   A CG  1 
ATOM   1649 C  CD  . GLN   A 1 203 ? -25.240 49.078  42.697  1.00 83.09  ? 567 GLN   A CD  1 
ATOM   1650 O  OE1 . GLN   A 1 203 ? -24.993 49.996  41.917  1.00 90.44  ? 567 GLN   A OE1 1 
ATOM   1651 N  NE2 . GLN   A 1 203 ? -24.779 47.847  42.530  1.00 85.24  ? 567 GLN   A NE2 1 
ATOM   1652 N  N   . ARG   A 1 204 ? -29.189 48.707  41.012  1.00 55.13  ? 568 ARG   A N   1 
ATOM   1653 C  CA  . ARG   A 1 204 ? -29.307 48.977  39.547  1.00 46.68  ? 568 ARG   A CA  1 
ATOM   1654 C  C   . ARG   A 1 204 ? -30.614 49.698  39.212  1.00 43.23  ? 568 ARG   A C   1 
ATOM   1655 O  O   . ARG   A 1 204 ? -30.633 50.505  38.245  1.00 44.29  ? 568 ARG   A O   1 
ATOM   1656 C  CB  . ARG   A 1 204 ? -29.266 47.650  38.772  1.00 50.51  ? 568 ARG   A CB  1 
ATOM   1657 C  CG  . ARG   A 1 204 ? -29.492 47.777  37.269  1.00 49.21  ? 568 ARG   A CG  1 
ATOM   1658 C  CD  . ARG   A 1 204 ? -28.389 48.585  36.597  1.00 49.40  ? 568 ARG   A CD  1 
ATOM   1659 N  NE  . ARG   A 1 204 ? -28.608 48.773  35.171  1.00 46.76  ? 568 ARG   A NE  1 
ATOM   1660 C  CZ  . ARG   A 1 204 ? -29.477 49.616  34.643  1.00 44.27  ? 568 ARG   A CZ  1 
ATOM   1661 N  NH1 . ARG   A 1 204 ? -30.226 50.380  35.414  1.00 51.62  ? 568 ARG   A NH1 1 
ATOM   1662 N  NH2 . ARG   A 1 204 ? -29.603 49.699  33.331  1.00 44.31  ? 568 ARG   A NH2 1 
ATOM   1663 N  N   . TYR   A 1 205 ? -31.696 49.348  39.906  1.00 47.37  ? 569 TYR   A N   1 
ATOM   1664 C  CA  . TYR   A 1 205 ? -33.082 49.786  39.604  1.00 48.77  ? 569 TYR   A CA  1 
ATOM   1665 C  C   . TYR   A 1 205 ? -33.722 50.373  40.874  1.00 62.48  ? 569 TYR   A C   1 
ATOM   1666 O  O   . TYR   A 1 205 ? -34.782 49.932  41.328  1.00 58.11  ? 569 TYR   A O   1 
ATOM   1667 C  CB  . TYR   A 1 205 ? -33.887 48.600  39.063  1.00 49.82  ? 569 TYR   A CB  1 
ATOM   1668 C  CG  . TYR   A 1 205 ? -33.550 48.130  37.665  1.00 47.08  ? 569 TYR   A CG  1 
ATOM   1669 C  CD1 . TYR   A 1 205 ? -33.685 48.962  36.565  1.00 45.54  ? 569 TYR   A CD1 1 
ATOM   1670 C  CD2 . TYR   A 1 205 ? -33.159 46.819  37.432  1.00 46.97  ? 569 TYR   A CD2 1 
ATOM   1671 C  CE1 . TYR   A 1 205 ? -33.409 48.517  35.283  1.00 47.20  ? 569 TYR   A CE1 1 
ATOM   1672 C  CE2 . TYR   A 1 205 ? -32.853 46.366  36.156  1.00 46.57  ? 569 TYR   A CE2 1 
ATOM   1673 C  CZ  . TYR   A 1 205 ? -32.989 47.215  35.076  1.00 44.40  ? 569 TYR   A CZ  1 
ATOM   1674 O  OH  . TYR   A 1 205 ? -32.732 46.762  33.813  1.00 45.41  ? 569 TYR   A OH  1 
ATOM   1675 N  N   . PRO   A 1 206 ? -33.131 51.426  41.482  1.00 68.07  ? 570 PRO   A N   1 
ATOM   1676 C  CA  . PRO   A 1 206 ? -33.590 51.905  42.791  1.00 72.20  ? 570 PRO   A CA  1 
ATOM   1677 C  C   . PRO   A 1 206 ? -35.068 52.341  42.795  1.00 69.29  ? 570 PRO   A C   1 
ATOM   1678 O  O   . PRO   A 1 206 ? -35.723 52.113  43.794  1.00 75.52  ? 570 PRO   A O   1 
ATOM   1679 C  CB  . PRO   A 1 206 ? -32.618 53.056  43.101  1.00 70.51  ? 570 PRO   A CB  1 
ATOM   1680 C  CG  . PRO   A 1 206 ? -32.151 53.520  41.734  1.00 69.94  ? 570 PRO   A CG  1 
ATOM   1681 C  CD  . PRO   A 1 206 ? -32.042 52.243  40.927  1.00 66.46  ? 570 PRO   A CD  1 
ATOM   1682 N  N   . ASP   A 1 207 ? -35.562 52.901  41.686  1.00 66.22  ? 571 ASP   A N   1 
ATOM   1683 C  CA  . ASP   A 1 207 ? -36.989 53.278  41.486  1.00 67.75  ? 571 ASP   A CA  1 
ATOM   1684 C  C   . ASP   A 1 207 ? -37.752 52.135  40.798  1.00 73.69  ? 571 ASP   A C   1 
ATOM   1685 O  O   . ASP   A 1 207 ? -38.717 52.436  40.064  1.00 72.03  ? 571 ASP   A O   1 
ATOM   1686 C  CB  . ASP   A 1 207 ? -37.108 54.548  40.638  1.00 71.56  ? 571 ASP   A CB  1 
ATOM   1687 C  CG  . ASP   A 1 207 ? -36.656 55.823  41.333  1.00 77.48  ? 571 ASP   A CG  1 
ATOM   1688 O  OD1 . ASP   A 1 207 ? -36.753 55.881  42.572  1.00 71.77  ? 571 ASP   A OD1 1 
ATOM   1689 O  OD2 . ASP   A 1 207 ? -36.233 56.765  40.621  1.00 78.69  ? 571 ASP   A OD2 1 
ATOM   1690 N  N   . GLY   A 1 208 ? -37.315 50.884  40.988  1.00 75.69  ? 572 GLY   A N   1 
ATOM   1691 C  CA  . GLY   A 1 208 ? -37.994 49.650  40.533  1.00 73.91  ? 572 GLY   A CA  1 
ATOM   1692 C  C   . GLY   A 1 208 ? -38.700 49.760  39.183  1.00 77.42  ? 572 GLY   A C   1 
ATOM   1693 O  O   . GLY   A 1 208 ? -39.754 49.123  39.044  1.00 89.84  ? 572 GLY   A O   1 
ATOM   1694 N  N   . ILE   A 1 209 ? -38.152 50.488  38.200  1.00 80.47  ? 573 ILE   A N   1 
ATOM   1695 C  CA  . ILE   A 1 209 ? -38.709 50.565  36.810  1.00 80.99  ? 573 ILE   A CA  1 
ATOM   1696 C  C   . ILE   A 1 209 ? -37.633 50.111  35.810  1.00 79.41  ? 573 ILE   A C   1 
ATOM   1697 O  O   . ILE   A 1 209 ? -36.469 50.511  35.971  1.00 73.91  ? 573 ILE   A O   1 
ATOM   1698 C  CB  . ILE   A 1 209 ? -39.259 51.975  36.490  1.00 84.41  ? 573 ILE   A CB  1 
ATOM   1699 C  CG1 . ILE   A 1 209 ? -40.733 52.097  36.893  1.00 86.26  ? 573 ILE   A CG1 1 
ATOM   1700 C  CG2 . ILE   A 1 209 ? -39.048 52.341  35.023  1.00 81.56  ? 573 ILE   A CG2 1 
ATOM   1701 C  CD1 . ILE   A 1 209 ? -41.322 53.487  36.737  1.00 87.36  ? 573 ILE   A CD1 1 
ATOM   1702 N  N   . ILE   A 1 210 ? -38.027 49.316  34.805  1.00 75.89  ? 574 ILE   A N   1 
ATOM   1703 C  CA  . ILE   A 1 210 ? -37.115 48.637  33.827  1.00 72.87  ? 574 ILE   A CA  1 
ATOM   1704 C  C   . ILE   A 1 210 ? -37.418 49.164  32.414  1.00 73.33  ? 574 ILE   A C   1 
ATOM   1705 O  O   . ILE   A 1 210 ? -38.056 48.440  31.627  1.00 74.14  ? 574 ILE   A O   1 
ATOM   1706 C  CB  . ILE   A 1 210 ? -37.259 47.098  33.932  1.00 67.57  ? 574 ILE   A CB  1 
ATOM   1707 C  CG1 . ILE   A 1 210 ? -37.014 46.600  35.360  1.00 57.00  ? 574 ILE   A CG1 1 
ATOM   1708 C  CG2 . ILE   A 1 210 ? -36.361 46.383  32.922  1.00 69.45  ? 574 ILE   A CG2 1 
ATOM   1709 C  CD1 . ILE   A 1 210 ? -37.522 45.198  35.640  1.00 58.59  ? 574 ILE   A CD1 1 
ATOM   1710 N  N   . SER   A 1 211 ? -36.978 50.386  32.106  1.00 79.28  ? 575 SER   A N   1 
ATOM   1711 C  CA  . SER   A 1 211 ? -37.288 51.110  30.844  1.00 80.80  ? 575 SER   A CA  1 
ATOM   1712 C  C   . SER   A 1 211 ? -36.250 50.778  29.768  1.00 77.73  ? 575 SER   A C   1 
ATOM   1713 O  O   . SER   A 1 211 ? -35.140 50.328  30.119  1.00 76.29  ? 575 SER   A O   1 
ATOM   1714 C  CB  . SER   A 1 211 ? -37.372 52.599  31.080  1.00 81.17  ? 575 SER   A CB  1 
ATOM   1715 O  OG  . SER   A 1 211 ? -36.351 53.016  31.976  1.00 82.36  ? 575 SER   A OG  1 
ATOM   1716 N  N   . LYS   A 1 212 ? -36.631 50.982  28.506  1.00 80.43  ? 576 LYS   A N   1 
ATOM   1717 C  CA  . LYS   A 1 212 ? -35.732 50.978  27.321  1.00 89.37  ? 576 LYS   A CA  1 
ATOM   1718 C  C   . LYS   A 1 212 ? -34.449 51.718  27.704  1.00 96.49  ? 576 LYS   A C   1 
ATOM   1719 O  O   . LYS   A 1 212 ? -34.510 52.877  28.110  1.00 93.39  ? 576 LYS   A O   1 
ATOM   1720 C  CB  . LYS   A 1 212 ? -36.481 51.634  26.156  1.00 88.17  ? 576 LYS   A CB  1 
ATOM   1721 C  CG  . LYS   A 1 212 ? -35.898 51.436  24.765  1.00 89.21  ? 576 LYS   A CG  1 
ATOM   1722 C  CD  . LYS   A 1 212 ? -36.564 52.349  23.746  1.00 90.85  ? 576 LYS   A CD  1 
ATOM   1723 C  CE  . LYS   A 1 212 ? -36.486 51.839  22.322  1.00 95.32  ? 576 LYS   A CE  1 
ATOM   1724 N  NZ  . LYS   A 1 212 ? -35.116 51.391  21.970  1.00 96.29  ? 576 LYS   A NZ  1 
ATOM   1725 N  N   . PRO   A 1 213 ? -33.260 51.068  27.672  1.00 97.98  ? 577 PRO   A N   1 
ATOM   1726 C  CA  . PRO   A 1 213 ? -32.015 51.721  28.071  1.00 97.42  ? 577 PRO   A CA  1 
ATOM   1727 C  C   . PRO   A 1 213 ? -31.347 52.459  26.900  1.00 94.19  ? 577 PRO   A C   1 
ATOM   1728 O  O   . PRO   A 1 213 ? -31.326 53.688  26.874  1.00 88.40  ? 577 PRO   A O   1 
ATOM   1729 C  CB  . PRO   A 1 213 ? -31.171 50.538  28.567  1.00 98.13  ? 577 PRO   A CB  1 
ATOM   1730 C  CG  . PRO   A 1 213 ? -31.612 49.367  27.702  1.00 97.73  ? 577 PRO   A CG  1 
ATOM   1731 C  CD  . PRO   A 1 213 ? -33.044 49.662  27.294  1.00 99.59  ? 577 PRO   A CD  1 
ATOM   1732 N  N   . ASN   B 2 1   ? -48.117 9.700   34.436  1.00 64.24  ? 117 ASN   B N   1 
ATOM   1733 C  CA  . ASN   B 2 1   ? -47.582 11.090  34.513  1.00 66.77  ? 117 ASN   B CA  1 
ATOM   1734 C  C   . ASN   B 2 1   ? -46.200 11.133  33.833  1.00 53.08  ? 117 ASN   B C   1 
ATOM   1735 O  O   . ASN   B 2 1   ? -46.200 11.285  32.589  1.00 56.95  ? 117 ASN   B O   1 
ATOM   1736 C  CB  . ASN   B 2 1   ? -47.603 11.656  35.937  1.00 69.76  ? 117 ASN   B CB  1 
ATOM   1737 C  CG  . ASN   B 2 1   ? -47.080 10.691  36.981  1.00 81.07  ? 117 ASN   B CG  1 
ATOM   1738 O  OD1 . ASN   B 2 1   ? -45.998 10.891  37.537  1.00 78.52  ? 117 ASN   B OD1 1 
ATOM   1739 N  ND2 . ASN   B 2 1   ? -47.838 9.639   37.250  1.00 84.36  ? 117 ASN   B ND2 1 
ATOM   1740 N  N   . ASP   B 2 2   ? -45.088 10.985  34.575  1.00 41.48  ? 118 ASP   B N   1 
ATOM   1741 C  CA  . ASP   B 2 2   ? -43.750 11.478  34.118  1.00 41.92  ? 118 ASP   B CA  1 
ATOM   1742 C  C   . ASP   B 2 2   ? -42.903 10.329  33.559  1.00 36.09  ? 118 ASP   B C   1 
ATOM   1743 O  O   . ASP   B 2 2   ? -42.229 9.641   34.354  1.00 37.52  ? 118 ASP   B O   1 
ATOM   1744 C  CB  . ASP   B 2 2   ? -42.984 12.222  35.211  1.00 40.20  ? 118 ASP   B CB  1 
ATOM   1745 C  CG  . ASP   B 2 2   ? -41.688 12.874  34.721  1.00 45.85  ? 118 ASP   B CG  1 
ATOM   1746 O  OD1 . ASP   B 2 2   ? -41.023 12.315  33.778  1.00 35.85  ? 118 ASP   B OD1 1 
ATOM   1747 O  OD2 . ASP   B 2 2   ? -41.315 13.910  35.309  1.00 42.93  ? 118 ASP   B OD2 1 
ATOM   1748 N  N   . TYR   B 2 3   ? -42.886 10.172  32.230  1.00 34.65  ? 119 TYR   B N   1 
ATOM   1749 C  CA  . TYR   B 2 3   ? -42.139 9.089   31.542  1.00 31.85  ? 119 TYR   B CA  1 
ATOM   1750 C  C   . TYR   B 2 3   ? -40.639 9.309   31.652  1.00 30.95  ? 119 TYR   B C   1 
ATOM   1751 O  O   . TYR   B 2 3   ? -39.910 8.326   31.532  1.00 29.18  ? 119 TYR   B O   1 
ATOM   1752 C  CB  . TYR   B 2 3   ? -42.647 8.943   30.118  1.00 37.19  ? 119 TYR   B CB  1 
ATOM   1753 C  CG  . TYR   B 2 3   ? -44.047 8.377   30.062  1.00 36.35  ? 119 TYR   B CG  1 
ATOM   1754 C  CD1 . TYR   B 2 3   ? -44.329 7.126   30.593  1.00 41.38  ? 119 TYR   B CD1 1 
ATOM   1755 C  CD2 . TYR   B 2 3   ? -45.086 9.091   29.505  1.00 44.38  ? 119 TYR   B CD2 1 
ATOM   1756 C  CE1 . TYR   B 2 3   ? -45.609 6.593   30.548  1.00 40.90  ? 119 TYR   B CE1 1 
ATOM   1757 C  CE2 . TYR   B 2 3   ? -46.377 8.585   29.470  1.00 46.85  ? 119 TYR   B CE2 1 
ATOM   1758 C  CZ  . TYR   B 2 3   ? -46.636 7.329   29.989  1.00 44.05  ? 119 TYR   B CZ  1 
ATOM   1759 O  OH  . TYR   B 2 3   ? -47.901 6.832   29.914  1.00 43.65  ? 119 TYR   B OH  1 
ATOM   1760 N  N   . CYS   B 2 4   ? -40.171 10.533  31.916  1.00 29.12  ? 120 CYS   B N   1 
ATOM   1761 C  CA  . CYS   B 2 4   ? -38.722 10.795  32.112  1.00 28.52  ? 120 CYS   B CA  1 
ATOM   1762 C  C   . CYS   B 2 4   ? -38.272 10.153  33.425  1.00 32.65  ? 120 CYS   B C   1 
ATOM   1763 O  O   . CYS   B 2 4   ? -37.283 9.378   33.400  1.00 33.69  ? 120 CYS   B O   1 
ATOM   1764 C  CB  . CYS   B 2 4   ? -38.405 12.289  32.108  1.00 29.60  ? 120 CYS   B CB  1 
ATOM   1765 S  SG  . CYS   B 2 4   ? -38.903 13.142  30.584  1.00 30.87  ? 120 CYS   B SG  1 
ATOM   1766 N  N   . GLN   B 2 5   ? -38.949 10.485  34.533  1.00 37.84  ? 121 GLN   B N   1 
ATOM   1767 C  CA  . GLN   B 2 5   ? -38.700 9.873   35.866  1.00 42.28  ? 121 GLN   B CA  1 
ATOM   1768 C  C   . GLN   B 2 5   ? -38.775 8.349   35.723  1.00 38.44  ? 121 GLN   B C   1 
ATOM   1769 O  O   . GLN   B 2 5   ? -37.903 7.664   36.278  1.00 37.62  ? 121 GLN   B O   1 
ATOM   1770 C  CB  . GLN   B 2 5   ? -39.739 10.319  36.894  1.00 44.43  ? 121 GLN   B CB  1 
ATOM   1771 C  CG  . GLN   B 2 5   ? -39.481 9.755   38.283  1.00 50.46  ? 121 GLN   B CG  1 
ATOM   1772 C  CD  . GLN   B 2 5   ? -38.179 10.263  38.841  1.00 54.27  ? 121 GLN   B CD  1 
ATOM   1773 O  OE1 . GLN   B 2 5   ? -38.011 11.458  39.069  1.00 58.15  ? 121 GLN   B OE1 1 
ATOM   1774 N  NE2 . GLN   B 2 5   ? -37.241 9.356   39.065  1.00 59.03  ? 121 GLN   B NE2 1 
ATOM   1775 N  N   . HIS   B 2 6   ? -39.785 7.871   34.992  1.00 36.05  ? 122 HIS   B N   1 
ATOM   1776 C  CA  . HIS   B 2 6   ? -40.033 6.425   34.758  1.00 39.12  ? 122 HIS   B CA  1 
ATOM   1777 C  C   . HIS   B 2 6   ? -38.829 5.805   34.048  1.00 38.86  ? 122 HIS   B C   1 
ATOM   1778 O  O   . HIS   B 2 6   ? -38.419 4.697   34.451  1.00 36.81  ? 122 HIS   B O   1 
ATOM   1779 C  CB  . HIS   B 2 6   ? -41.342 6.214   34.006  1.00 40.20  ? 122 HIS   B CB  1 
ATOM   1780 C  CG  . HIS   B 2 6   ? -41.725 4.777   33.919  1.00 46.15  ? 122 HIS   B CG  1 
ATOM   1781 N  ND1 . HIS   B 2 6   ? -42.091 4.047   35.035  1.00 52.23  ? 122 HIS   B ND1 1 
ATOM   1782 C  CD2 . HIS   B 2 6   ? -41.801 3.931   32.873  1.00 49.64  ? 122 HIS   B CD2 1 
ATOM   1783 C  CE1 . HIS   B 2 6   ? -42.386 2.813   34.673  1.00 54.78  ? 122 HIS   B CE1 1 
ATOM   1784 N  NE2 . HIS   B 2 6   ? -42.224 2.717   33.356  1.00 52.03  ? 122 HIS   B NE2 1 
ATOM   1785 N  N   . PHE   B 2 7   ? -38.234 6.497   33.064  1.00 33.63  ? 123 PHE   B N   1 
ATOM   1786 C  CA  . PHE   B 2 7   ? -37.020 5.996   32.382  1.00 35.84  ? 123 PHE   B CA  1 
ATOM   1787 C  C   . PHE   B 2 7   ? -35.862 5.904   33.379  1.00 35.51  ? 123 PHE   B C   1 
ATOM   1788 O  O   . PHE   B 2 7   ? -35.078 4.914   33.334  1.00 33.96  ? 123 PHE   B O   1 
ATOM   1789 C  CB  . PHE   B 2 7   ? -36.633 6.856   31.166  1.00 33.30  ? 123 PHE   B CB  1 
ATOM   1790 C  CG  . PHE   B 2 7   ? -35.267 6.503   30.647  1.00 33.31  ? 123 PHE   B CG  1 
ATOM   1791 C  CD1 . PHE   B 2 7   ? -35.060 5.342   29.909  1.00 34.03  ? 123 PHE   B CD1 1 
ATOM   1792 C  CD2 . PHE   B 2 7   ? -34.172 7.281   30.972  1.00 34.00  ? 123 PHE   B CD2 1 
ATOM   1793 C  CE1 . PHE   B 2 7   ? -33.791 4.994   29.483  1.00 35.08  ? 123 PHE   B CE1 1 
ATOM   1794 C  CE2 . PHE   B 2 7   ? -32.903 6.943   30.528  1.00 37.35  ? 123 PHE   B CE2 1 
ATOM   1795 C  CZ  . PHE   B 2 7   ? -32.717 5.819   29.758  1.00 36.83  ? 123 PHE   B CZ  1 
ATOM   1796 N  N   . VAL   B 2 8   ? -35.704 6.938   34.214  1.00 34.73  ? 124 VAL   B N   1 
ATOM   1797 C  CA  . VAL   B 2 8   ? -34.627 6.995   35.245  1.00 35.75  ? 124 VAL   B CA  1 
ATOM   1798 C  C   . VAL   B 2 8   ? -34.847 5.810   36.205  1.00 37.21  ? 124 VAL   B C   1 
ATOM   1799 O  O   . VAL   B 2 8   ? -33.866 5.255   36.657  1.00 35.13  ? 124 VAL   B O   1 
ATOM   1800 C  CB  . VAL   B 2 8   ? -34.651 8.337   36.007  1.00 40.16  ? 124 VAL   B CB  1 
ATOM   1801 C  CG1 . VAL   B 2 8   ? -33.738 8.321   37.230  1.00 40.50  ? 124 VAL   B CG1 1 
ATOM   1802 C  CG2 . VAL   B 2 8   ? -34.313 9.516   35.104  1.00 38.22  ? 124 VAL   B CG2 1 
ATOM   1803 N  N   . ASP   B 2 9   ? -36.108 5.478   36.487  1.00 38.67  ? 125 ASP   B N   1 
ATOM   1804 C  CA  . ASP   B 2 9   ? -36.505 4.464   37.501  1.00 42.44  ? 125 ASP   B CA  1 
ATOM   1805 C  C   . ASP   B 2 9   ? -36.292 3.041   36.962  1.00 44.89  ? 125 ASP   B C   1 
ATOM   1806 O  O   . ASP   B 2 9   ? -35.802 2.217   37.732  1.00 47.73  ? 125 ASP   B O   1 
ATOM   1807 C  CB  . ASP   B 2 9   ? -37.959 4.671   37.936  1.00 40.27  ? 125 ASP   B CB  1 
ATOM   1808 C  CG  . ASP   B 2 9   ? -38.160 5.869   38.849  1.00 43.00  ? 125 ASP   B CG  1 
ATOM   1809 O  OD1 . ASP   B 2 9   ? -37.157 6.351   39.400  1.00 41.56  ? 125 ASP   B OD1 1 
ATOM   1810 O  OD2 . ASP   B 2 9   ? -39.331 6.311   38.980  1.00 48.77  ? 125 ASP   B OD2 1 
ATOM   1811 N  N   . THR   B 2 10  ? -36.631 2.780   35.692  1.00 44.18  ? 126 THR   B N   1 
ATOM   1812 C  CA  . THR   B 2 10  ? -36.850 1.423   35.116  1.00 39.43  ? 126 THR   B CA  1 
ATOM   1813 C  C   . THR   B 2 10  ? -35.972 1.152   33.892  1.00 46.20  ? 126 THR   B C   1 
ATOM   1814 O  O   . THR   B 2 10  ? -35.847 -0.025  33.527  1.00 38.27  ? 126 THR   B O   1 
ATOM   1815 C  CB  . THR   B 2 10  ? -38.323 1.226   34.732  1.00 41.73  ? 126 THR   B CB  1 
ATOM   1816 O  OG1 . THR   B 2 10  ? -38.685 2.044   33.612  1.00 37.16  ? 126 THR   B OG1 1 
ATOM   1817 C  CG2 . THR   B 2 10  ? -39.281 1.514   35.876  1.00 41.45  ? 126 THR   B CG2 1 
ATOM   1818 N  N   . GLY   B 2 11  ? -35.462 2.189   33.215  1.00 42.32  ? 127 GLY   B N   1 
ATOM   1819 C  CA  . GLY   B 2 11  ? -34.750 2.045   31.933  1.00 38.81  ? 127 GLY   B CA  1 
ATOM   1820 C  C   . GLY   B 2 11  ? -35.673 1.869   30.730  1.00 34.38  ? 127 GLY   B C   1 
ATOM   1821 O  O   . GLY   B 2 11  ? -35.144 1.644   29.641  1.00 39.66  ? 127 GLY   B O   1 
ATOM   1822 N  N   . HIS   B 2 12  ? -36.994 1.898   30.907  1.00 32.82  ? 128 HIS   B N   1 
ATOM   1823 C  CA  . HIS   B 2 12  ? -37.978 1.965   29.806  1.00 36.09  ? 128 HIS   B CA  1 
ATOM   1824 C  C   . HIS   B 2 12  ? -38.027 3.401   29.260  1.00 37.66  ? 128 HIS   B C   1 
ATOM   1825 O  O   . HIS   B 2 12  ? -38.405 4.350   30.041  1.00 32.72  ? 128 HIS   B O   1 
ATOM   1826 C  CB  . HIS   B 2 12  ? -39.374 1.526   30.258  1.00 38.95  ? 128 HIS   B CB  1 
ATOM   1827 C  CG  . HIS   B 2 12  ? -39.478 0.054   30.499  1.00 44.62  ? 128 HIS   B CG  1 
ATOM   1828 N  ND1 . HIS   B 2 12  ? -38.716 -0.600  31.446  1.00 53.91  ? 128 HIS   B ND1 1 
ATOM   1829 C  CD2 . HIS   B 2 12  ? -40.260 -0.887  29.941  1.00 53.61  ? 128 HIS   B CD2 1 
ATOM   1830 C  CE1 . HIS   B 2 12  ? -39.021 -1.879  31.455  1.00 50.32  ? 128 HIS   B CE1 1 
ATOM   1831 N  NE2 . HIS   B 2 12  ? -39.969 -2.076  30.556  1.00 53.95  ? 128 HIS   B NE2 1 
ATOM   1832 N  N   . ARG   B 2 13  ? -37.647 3.563   27.989  1.00 35.38  ? 129 ARG   B N   1 
ATOM   1833 C  CA  . ARG   B 2 13  ? -37.622 4.890   27.296  1.00 35.85  ? 129 ARG   B CA  1 
ATOM   1834 C  C   . ARG   B 2 13  ? -39.054 5.411   27.192  1.00 31.38  ? 129 ARG   B C   1 
ATOM   1835 O  O   . ARG   B 2 13  ? -40.005 4.651   26.932  1.00 31.23  ? 129 ARG   B O   1 
ATOM   1836 C  CB  . ARG   B 2 13  ? -36.961 4.762   25.912  1.00 32.20  ? 129 ARG   B CB  1 
ATOM   1837 C  CG  . ARG   B 2 13  ? -35.474 4.478   25.970  1.00 32.40  ? 129 ARG   B CG  1 
ATOM   1838 C  CD  . ARG   B 2 13  ? -35.010 4.028   24.604  1.00 31.96  ? 129 ARG   B CD  1 
ATOM   1839 N  NE  . ARG   B 2 13  ? -33.629 3.622   24.607  1.00 31.30  ? 129 ARG   B NE  1 
ATOM   1840 C  CZ  . ARG   B 2 13  ? -32.968 3.219   23.524  1.00 33.62  ? 129 ARG   B CZ  1 
ATOM   1841 N  NH1 . ARG   B 2 13  ? -33.576 3.130   22.338  1.00 32.60  ? 129 ARG   B NH1 1 
ATOM   1842 N  NH2 . ARG   B 2 13  ? -31.707 2.870   23.659  1.00 33.33  ? 129 ARG   B NH2 1 
ATOM   1843 N  N   . PRO   B 2 14  ? -39.275 6.726   27.406  1.00 29.03  ? 130 PRO   B N   1 
ATOM   1844 C  CA  . PRO   B 2 14  ? -40.609 7.304   27.270  1.00 28.94  ? 130 PRO   B CA  1 
ATOM   1845 C  C   . PRO   B 2 14  ? -41.344 6.920   25.983  1.00 30.63  ? 130 PRO   B C   1 
ATOM   1846 O  O   . PRO   B 2 14  ? -42.575 6.755   26.030  1.00 30.92  ? 130 PRO   B O   1 
ATOM   1847 C  CB  . PRO   B 2 14  ? -40.315 8.822   27.268  1.00 30.33  ? 130 PRO   B CB  1 
ATOM   1848 C  CG  . PRO   B 2 14  ? -39.080 8.964   28.104  1.00 28.50  ? 130 PRO   B CG  1 
ATOM   1849 C  CD  . PRO   B 2 14  ? -38.264 7.730   27.815  1.00 28.89  ? 130 PRO   B CD  1 
ATOM   1850 N  N   . GLN   B 2 15  ? -40.610 6.843   24.851  1.00 29.51  ? 131 GLN   B N   1 
ATOM   1851 C  CA  . GLN   B 2 15  ? -41.199 6.484   23.527  1.00 28.18  ? 131 GLN   B CA  1 
ATOM   1852 C  C   . GLN   B 2 15  ? -41.839 5.073   23.572  1.00 29.00  ? 131 GLN   B C   1 
ATOM   1853 O  O   . GLN   B 2 15  ? -42.697 4.804   22.716  1.00 30.21  ? 131 GLN   B O   1 
ATOM   1854 C  CB  . GLN   B 2 15  ? -40.180 6.572   22.374  1.00 28.88  ? 131 GLN   B CB  1 
ATOM   1855 C  CG  . GLN   B 2 15  ? -38.847 5.879   22.619  1.00 28.92  ? 131 GLN   B CG  1 
ATOM   1856 C  CD  . GLN   B 2 15  ? -37.797 6.827   23.152  1.00 28.77  ? 131 GLN   B CD  1 
ATOM   1857 O  OE1 . GLN   B 2 15  ? -38.054 7.576   24.092  1.00 26.76  ? 131 GLN   B OE1 1 
ATOM   1858 N  NE2 . GLN   B 2 15  ? -36.618 6.810   22.548  1.00 29.92  ? 131 GLN   B NE2 1 
ATOM   1859 N  N   . ASN   B 2 16  ? -41.425 4.216   24.508  1.00 33.49  ? 132 ASN   B N   1 
ATOM   1860 C  CA  . ASN   B 2 16  ? -42.014 2.850   24.706  1.00 35.06  ? 132 ASN   B CA  1 
ATOM   1861 C  C   . ASN   B 2 16  ? -43.521 2.946   24.962  1.00 36.97  ? 132 ASN   B C   1 
ATOM   1862 O  O   . ASN   B 2 16  ? -44.217 1.938   24.735  1.00 38.93  ? 132 ASN   B O   1 
ATOM   1863 C  CB  . ASN   B 2 16  ? -41.363 2.084   25.863  1.00 33.24  ? 132 ASN   B CB  1 
ATOM   1864 C  CG  . ASN   B 2 16  ? -39.963 1.649   25.543  1.00 36.64  ? 132 ASN   B CG  1 
ATOM   1865 O  OD1 . ASN   B 2 16  ? -39.406 2.070   24.532  1.00 37.73  ? 132 ASN   B OD1 1 
ATOM   1866 N  ND2 . ASN   B 2 16  ? -39.390 0.802   26.379  1.00 38.47  ? 132 ASN   B ND2 1 
ATOM   1867 N  N   . PHE   B 2 17  ? -44.009 4.105   25.388  1.00 32.54  ? 133 PHE   B N   1 
ATOM   1868 C  CA  . PHE   B 2 17  ? -45.368 4.286   25.943  1.00 34.89  ? 133 PHE   B CA  1 
ATOM   1869 C  C   . PHE   B 2 17  ? -46.222 5.064   24.959  1.00 38.16  ? 133 PHE   B C   1 
ATOM   1870 O  O   . PHE   B 2 17  ? -47.397 5.338   25.279  1.00 38.59  ? 133 PHE   B O   1 
ATOM   1871 C  CB  . PHE   B 2 17  ? -45.297 4.892   27.345  1.00 33.61  ? 133 PHE   B CB  1 
ATOM   1872 C  CG  . PHE   B 2 17  ? -44.515 4.011   28.261  1.00 34.46  ? 133 PHE   B CG  1 
ATOM   1873 C  CD1 . PHE   B 2 17  ? -45.093 2.851   28.770  1.00 41.15  ? 133 PHE   B CD1 1 
ATOM   1874 C  CD2 . PHE   B 2 17  ? -43.187 4.267   28.526  1.00 34.22  ? 133 PHE   B CD2 1 
ATOM   1875 C  CE1 . PHE   B 2 17  ? -44.348 1.987   29.550  1.00 38.49  ? 133 PHE   B CE1 1 
ATOM   1876 C  CE2 . PHE   B 2 17  ? -42.449 3.419   29.329  1.00 39.67  ? 133 PHE   B CE2 1 
ATOM   1877 C  CZ  . PHE   B 2 17  ? -43.029 2.270   29.831  1.00 45.88  ? 133 PHE   B CZ  1 
ATOM   1878 N  N   . ILE   B 2 18  ? -45.695 5.346   23.769  1.00 37.51  ? 134 ILE   B N   1 
ATOM   1879 C  CA  . ILE   B 2 18  ? -46.529 5.931   22.691  1.00 36.66  ? 134 ILE   B CA  1 
ATOM   1880 C  C   . ILE   B 2 18  ? -47.438 4.814   22.159  1.00 39.99  ? 134 ILE   B C   1 
ATOM   1881 O  O   . ILE   B 2 18  ? -46.929 3.739   21.843  1.00 37.18  ? 134 ILE   B O   1 
ATOM   1882 C  CB  . ILE   B 2 18  ? -45.684 6.591   21.592  1.00 34.79  ? 134 ILE   B CB  1 
ATOM   1883 C  CG1 . ILE   B 2 18  ? -44.672 7.586   22.188  1.00 32.99  ? 134 ILE   B CG1 1 
ATOM   1884 C  CG2 . ILE   B 2 18  ? -46.586 7.261   20.560  1.00 34.30  ? 134 ILE   B CG2 1 
ATOM   1885 C  CD1 . ILE   B 2 18  ? -43.655 8.070   21.170  1.00 32.94  ? 134 ILE   B CD1 1 
ATOM   1886 N  N   . ARG   B 2 19  ? -48.727 5.111   22.038  1.00 46.06  ? 135 ARG   B N   1 
ATOM   1887 C  CA  . ARG   B 2 19  ? -49.768 4.163   21.574  1.00 57.61  ? 135 ARG   B CA  1 
ATOM   1888 C  C   . ARG   B 2 19  ? -49.967 4.329   20.063  1.00 55.30  ? 135 ARG   B C   1 
ATOM   1889 O  O   . ARG   B 2 19  ? -49.586 5.386   19.515  1.00 54.41  ? 135 ARG   B O   1 
ATOM   1890 C  CB  . ARG   B 2 19  ? -51.076 4.387   22.344  1.00 65.30  ? 135 ARG   B CB  1 
ATOM   1891 C  CG  . ARG   B 2 19  ? -51.199 3.562   23.621  1.00 76.37  ? 135 ARG   B CG  1 
ATOM   1892 C  CD  . ARG   B 2 19  ? -52.648 3.232   23.962  1.00 85.85  ? 135 ARG   B CD  1 
ATOM   1893 N  NE  . ARG   B 2 19  ? -52.782 2.019   24.762  1.00 91.39  ? 135 ARG   B NE  1 
ATOM   1894 C  CZ  . ARG   B 2 19  ? -52.588 0.774   24.317  1.00 95.33  ? 135 ARG   B CZ  1 
ATOM   1895 N  NH1 . ARG   B 2 19  ? -52.235 0.547   23.061  1.00 91.88  ? 135 ARG   B NH1 1 
ATOM   1896 N  NH2 . ARG   B 2 19  ? -52.735 -0.248  25.145  1.00 99.86  ? 135 ARG   B NH2 1 
ATOM   1897 N  N   . ASP   B 2 20  ? -50.554 3.302   19.436  1.00 60.22  ? 136 ASP   B N   1 
ATOM   1898 C  CA  . ASP   B 2 20  ? -50.929 3.242   17.998  1.00 67.71  ? 136 ASP   B CA  1 
ATOM   1899 C  C   . ASP   B 2 20  ? -49.648 3.305   17.160  1.00 74.81  ? 136 ASP   B C   1 
ATOM   1900 O  O   . ASP   B 2 20  ? -49.538 4.209   16.303  1.00 68.90  ? 136 ASP   B O   1 
ATOM   1901 C  CB  . ASP   B 2 20  ? -51.957 4.323   17.650  1.00 74.90  ? 136 ASP   B CB  1 
ATOM   1902 C  CG  . ASP   B 2 20  ? -53.363 4.048   18.166  1.00 80.42  ? 136 ASP   B CG  1 
ATOM   1903 O  OD1 . ASP   B 2 20  ? -53.565 3.023   18.889  1.00 67.12  ? 136 ASP   B OD1 1 
ATOM   1904 O  OD2 . ASP   B 2 20  ? -54.256 4.862   17.838  1.00 83.55  ? 136 ASP   B OD2 1 
ATOM   1905 N  N   . VAL   B 2 21  ? -48.725 2.374   17.433  1.00 81.18  ? 137 VAL   B N   1 
ATOM   1906 C  CA  . VAL   B 2 21  ? -47.433 2.190   16.708  1.00 90.25  ? 137 VAL   B CA  1 
ATOM   1907 C  C   . VAL   B 2 21  ? -46.741 0.937   17.269  1.00 98.89  ? 137 VAL   B C   1 
ATOM   1908 O  O   . VAL   B 2 21  ? -46.572 -0.028  16.492  1.00 99.93  ? 137 VAL   B O   1 
ATOM   1909 C  CB  . VAL   B 2 21  ? -46.539 3.444   16.823  1.00 86.68  ? 137 VAL   B CB  1 
ATOM   1910 C  CG1 . VAL   B 2 21  ? -45.827 3.524   18.168  1.00 77.16  ? 137 VAL   B CG1 1 
ATOM   1911 C  CG2 . VAL   B 2 21  ? -45.546 3.535   15.672  1.00 86.14  ? 137 VAL   B CG2 1 
ATOM   1912 N  N   . LEU   B 2 33  ? -61.011 6.249   6.330   1.00 106.41 ? 149 LEU   B N   1 
ATOM   1913 C  CA  . LEU   B 2 33  ? -59.911 7.030   6.961   1.00 105.05 ? 149 LEU   B CA  1 
ATOM   1914 C  C   . LEU   B 2 33  ? -58.741 7.189   5.972   1.00 105.84 ? 149 LEU   B C   1 
ATOM   1915 O  O   . LEU   B 2 33  ? -58.301 8.349   5.766   1.00 92.07  ? 149 LEU   B O   1 
ATOM   1916 C  CB  . LEU   B 2 33  ? -59.478 6.325   8.254   1.00 97.08  ? 149 LEU   B CB  1 
ATOM   1917 C  CG  . LEU   B 2 33  ? -60.532 6.265   9.362   1.00 95.62  ? 149 LEU   B CG  1 
ATOM   1918 C  CD1 . LEU   B 2 33  ? -60.120 5.287   10.455  1.00 95.04  ? 149 LEU   B CD1 1 
ATOM   1919 C  CD2 . LEU   B 2 33  ? -60.782 7.647   9.951   1.00 90.07  ? 149 LEU   B CD2 1 
ATOM   1920 N  N   . ARG   B 2 34  ? -58.268 6.080   5.380   1.00 113.96 ? 150 ARG   B N   1 
ATOM   1921 C  CA  . ARG   B 2 34  ? -57.012 6.001   4.573   1.00 111.93 ? 150 ARG   B CA  1 
ATOM   1922 C  C   . ARG   B 2 34  ? -57.129 4.973   3.432   1.00 106.26 ? 150 ARG   B C   1 
ATOM   1923 O  O   . ARG   B 2 34  ? -56.102 4.342   3.108   1.00 103.74 ? 150 ARG   B O   1 
ATOM   1924 C  CB  . ARG   B 2 34  ? -55.833 5.589   5.463   1.00 108.96 ? 150 ARG   B CB  1 
ATOM   1925 C  CG  . ARG   B 2 34  ? -55.442 6.582   6.547   1.00 111.74 ? 150 ARG   B CG  1 
ATOM   1926 C  CD  . ARG   B 2 34  ? -54.592 5.845   7.564   1.00 117.35 ? 150 ARG   B CD  1 
ATOM   1927 N  NE  . ARG   B 2 34  ? -53.932 6.693   8.546   1.00 125.09 ? 150 ARG   B NE  1 
ATOM   1928 C  CZ  . ARG   B 2 34  ? -53.117 6.248   9.507   1.00 128.06 ? 150 ARG   B CZ  1 
ATOM   1929 N  NH1 . ARG   B 2 34  ? -52.856 4.955   9.624   1.00 121.60 ? 150 ARG   B NH1 1 
ATOM   1930 N  NH2 . ARG   B 2 34  ? -52.562 7.099   10.353  1.00 126.55 ? 150 ARG   B NH2 1 
ATOM   1931 N  N   . GLU   B 2 35  ? -58.308 4.809   2.823   1.00 105.41 ? 151 GLU   B N   1 
ATOM   1932 C  CA  . GLU   B 2 35  ? -58.498 3.959   1.611   1.00 103.26 ? 151 GLU   B CA  1 
ATOM   1933 C  C   . GLU   B 2 35  ? -57.990 4.721   0.384   1.00 105.37 ? 151 GLU   B C   1 
ATOM   1934 O  O   . GLU   B 2 35  ? -57.950 4.121   -0.714  1.00 96.00  ? 151 GLU   B O   1 
ATOM   1935 C  CB  . GLU   B 2 35  ? -59.961 3.539   1.466   1.00 108.49 ? 151 GLU   B CB  1 
ATOM   1936 C  CG  . GLU   B 2 35  ? -60.419 2.604   2.570   1.00 114.17 ? 151 GLU   B CG  1 
ATOM   1937 C  CD  . GLU   B 2 35  ? -59.396 1.541   2.937   1.00 122.01 ? 151 GLU   B CD  1 
ATOM   1938 O  OE1 . GLU   B 2 35  ? -59.596 0.372   2.554   1.00 121.84 ? 151 GLU   B OE1 1 
ATOM   1939 O  OE2 . GLU   B 2 35  ? -58.390 1.888   3.595   1.00 128.27 ? 151 GLU   B OE2 1 
ATOM   1940 N  N   . LEU   B 2 36  ? -57.669 6.006   0.584   1.00 101.57 ? 152 LEU   B N   1 
ATOM   1941 C  CA  . LEU   B 2 36  ? -56.714 6.819   -0.221  1.00 98.01  ? 152 LEU   B CA  1 
ATOM   1942 C  C   . LEU   B 2 36  ? -55.432 6.020   -0.454  1.00 82.55  ? 152 LEU   B C   1 
ATOM   1943 O  O   . LEU   B 2 36  ? -55.027 5.851   -1.622  1.00 82.57  ? 152 LEU   B O   1 
ATOM   1944 C  CB  . LEU   B 2 36  ? -56.382 8.105   0.552   1.00 101.98 ? 152 LEU   B CB  1 
ATOM   1945 C  CG  . LEU   B 2 36  ? -54.992 8.709   0.313   1.00 103.88 ? 152 LEU   B CG  1 
ATOM   1946 C  CD1 . LEU   B 2 36  ? -54.869 9.261   -1.099  1.00 104.35 ? 152 LEU   B CD1 1 
ATOM   1947 C  CD2 . LEU   B 2 36  ? -54.675 9.799   1.330   1.00 99.59  ? 152 LEU   B CD2 1 
ATOM   1948 N  N   . ILE   B 2 37  ? -54.810 5.592   0.643   1.00 78.27  ? 153 ILE   B N   1 
ATOM   1949 C  CA  . ILE   B 2 37  ? -53.380 5.178   0.678   1.00 82.18  ? 153 ILE   B CA  1 
ATOM   1950 C  C   . ILE   B 2 37  ? -53.238 3.918   -0.180  1.00 80.25  ? 153 ILE   B C   1 
ATOM   1951 O  O   . ILE   B 2 37  ? -52.210 3.786   -0.849  1.00 76.48  ? 153 ILE   B O   1 
ATOM   1952 C  CB  . ILE   B 2 37  ? -52.887 4.997   2.128   1.00 82.25  ? 153 ILE   B CB  1 
ATOM   1953 C  CG1 . ILE   B 2 37  ? -53.234 6.208   3.000   1.00 87.35  ? 153 ILE   B CG1 1 
ATOM   1954 C  CG2 . ILE   B 2 37  ? -51.396 4.706   2.164   1.00 82.25  ? 153 ILE   B CG2 1 
ATOM   1955 C  CD1 . ILE   B 2 37  ? -52.575 7.498   2.568   1.00 89.07  ? 153 ILE   B CD1 1 
ATOM   1956 N  N   . ARG   B 2 38  ? -54.259 3.060   -0.185  1.00 87.18  ? 154 ARG   B N   1 
ATOM   1957 C  CA  . ARG   B 2 38  ? -54.345 1.876   -1.077  1.00 96.77  ? 154 ARG   B CA  1 
ATOM   1958 C  C   . ARG   B 2 38  ? -54.174 2.330   -2.530  1.00 94.04  ? 154 ARG   B C   1 
ATOM   1959 O  O   . ARG   B 2 38  ? -53.212 1.858   -3.164  1.00 81.04  ? 154 ARG   B O   1 
ATOM   1960 C  CB  . ARG   B 2 38  ? -55.683 1.155   -0.907  1.00 107.40 ? 154 ARG   B CB  1 
ATOM   1961 C  CG  . ARG   B 2 38  ? -55.809 0.374   0.392   1.00 120.72 ? 154 ARG   B CG  1 
ATOM   1962 C  CD  . ARG   B 2 38  ? -57.245 -0.068  0.583   1.00 128.25 ? 154 ARG   B CD  1 
ATOM   1963 N  NE  . ARG   B 2 38  ? -57.733 -0.787  -0.589  1.00 133.62 ? 154 ARG   B NE  1 
ATOM   1964 C  CZ  . ARG   B 2 38  ? -58.985 -0.763  -1.047  1.00 131.90 ? 154 ARG   B CZ  1 
ATOM   1965 N  NH1 . ARG   B 2 38  ? -59.915 -0.041  -0.444  1.00 129.16 ? 154 ARG   B NH1 1 
ATOM   1966 N  NH2 . ARG   B 2 38  ? -59.302 -1.461  -2.123  1.00 132.82 ? 154 ARG   B NH2 1 
ATOM   1967 N  N   . LEU   B 2 39  ? -55.055 3.228   -3.002  1.00 89.41  ? 155 LEU   B N   1 
ATOM   1968 C  CA  . LEU   B 2 39  ? -55.132 3.737   -4.408  1.00 82.85  ? 155 LEU   B CA  1 
ATOM   1969 C  C   . LEU   B 2 39  ? -53.820 4.437   -4.809  1.00 76.12  ? 155 LEU   B C   1 
ATOM   1970 O  O   . LEU   B 2 39  ? -53.527 4.491   -6.021  1.00 80.06  ? 155 LEU   B O   1 
ATOM   1971 C  CB  . LEU   B 2 39  ? -56.320 4.701   -4.542  1.00 84.33  ? 155 LEU   B CB  1 
ATOM   1972 C  CG  . LEU   B 2 39  ? -57.695 4.073   -4.799  1.00 92.63  ? 155 LEU   B CG  1 
ATOM   1973 C  CD1 . LEU   B 2 39  ? -57.845 3.664   -6.258  1.00 96.07  ? 155 LEU   B CD1 1 
ATOM   1974 C  CD2 . LEU   B 2 39  ? -57.965 2.886   -3.878  1.00 95.11  ? 155 LEU   B CD2 1 
ATOM   1975 N  N   . LYS   B 2 40  ? -53.055 4.924   -3.826  1.00 62.32  ? 156 LYS   B N   1 
ATOM   1976 C  CA  . LYS   B 2 40  ? -51.856 5.778   -4.000  1.00 55.65  ? 156 LYS   B CA  1 
ATOM   1977 C  C   . LYS   B 2 40  ? -50.557 4.962   -3.934  1.00 61.90  ? 156 LYS   B C   1 
ATOM   1978 O  O   . LYS   B 2 40  ? -49.709 5.133   -4.842  1.00 60.35  ? 156 LYS   B O   1 
ATOM   1979 C  CB  . LYS   B 2 40  ? -51.868 6.821   -2.889  1.00 53.02  ? 156 LYS   B CB  1 
ATOM   1980 C  CG  . LYS   B 2 40  ? -50.594 7.633   -2.751  1.00 53.48  ? 156 LYS   B CG  1 
ATOM   1981 C  CD  . LYS   B 2 40  ? -50.860 8.986   -2.154  1.00 49.85  ? 156 LYS   B CD  1 
ATOM   1982 C  CE  . LYS   B 2 40  ? -49.610 9.655   -1.630  1.00 57.38  ? 156 LYS   B CE  1 
ATOM   1983 N  NZ  . LYS   B 2 40  ? -49.690 11.128  -1.778  1.00 57.36  ? 156 LYS   B NZ  1 
ATOM   1984 N  N   . ASP   B 2 41  ? -50.368 4.172   -2.864  1.00 56.82  ? 157 ASP   B N   1 
ATOM   1985 C  CA  . ASP   B 2 41  ? -49.280 3.160   -2.771  1.00 53.56  ? 157 ASP   B CA  1 
ATOM   1986 C  C   . ASP   B 2 41  ? -49.367 2.308   -4.044  1.00 47.07  ? 157 ASP   B C   1 
ATOM   1987 O  O   . ASP   B 2 41  ? -48.322 1.860   -4.552  1.00 45.28  ? 157 ASP   B O   1 
ATOM   1988 C  CB  . ASP   B 2 41  ? -49.343 2.347   -1.469  1.00 55.64  ? 157 ASP   B CB  1 
ATOM   1989 C  CG  . ASP   B 2 41  ? -48.547 2.931   -0.306  1.00 63.85  ? 157 ASP   B CG  1 
ATOM   1990 O  OD1 . ASP   B 2 41  ? -47.468 3.518   -0.542  1.00 68.92  ? 157 ASP   B OD1 1 
ATOM   1991 O  OD2 . ASP   B 2 41  ? -49.000 2.782   0.837   1.00 69.27  ? 157 ASP   B OD2 1 
ATOM   1992 N  N   . GLU   B 2 42  ? -50.575 2.138   -4.580  1.00 46.20  ? 158 GLU   B N   1 
ATOM   1993 C  CA  . GLU   B 2 42  ? -50.833 1.377   -5.830  1.00 49.85  ? 158 GLU   B CA  1 
ATOM   1994 C  C   . GLU   B 2 42  ? -50.249 2.134   -7.038  1.00 44.88  ? 158 GLU   B C   1 
ATOM   1995 O  O   . GLU   B 2 42  ? -49.617 1.488   -7.890  1.00 44.79  ? 158 GLU   B O   1 
ATOM   1996 C  CB  . GLU   B 2 42  ? -52.340 1.126   -5.925  1.00 53.41  ? 158 GLU   B CB  1 
ATOM   1997 C  CG  . GLU   B 2 42  ? -52.821 0.592   -7.253  1.00 63.05  ? 158 GLU   B CG  1 
ATOM   1998 C  CD  . GLU   B 2 42  ? -54.341 0.585   -7.345  1.00 75.20  ? 158 GLU   B CD  1 
ATOM   1999 O  OE1 . GLU   B 2 42  ? -54.910 -0.507  -7.549  1.00 73.83  ? 158 GLU   B OE1 1 
ATOM   2000 O  OE2 . GLU   B 2 42  ? -54.952 1.676   -7.203  1.00 76.68  ? 158 GLU   B OE2 1 
ATOM   2001 N  N   . LEU   B 2 43  ? -50.484 3.441   -7.132  1.00 44.76  ? 159 LEU   B N   1 
ATOM   2002 C  CA  . LEU   B 2 43  ? -50.020 4.259   -8.283  1.00 47.05  ? 159 LEU   B CA  1 
ATOM   2003 C  C   . LEU   B 2 43  ? -48.492 4.371   -8.235  1.00 42.69  ? 159 LEU   B C   1 
ATOM   2004 O  O   . LEU   B 2 43  ? -47.839 4.266   -9.305  1.00 39.33  ? 159 LEU   B O   1 
ATOM   2005 C  CB  . LEU   B 2 43  ? -50.722 5.619   -8.240  1.00 50.23  ? 159 LEU   B CB  1 
ATOM   2006 C  CG  . LEU   B 2 43  ? -52.159 5.584   -8.763  1.00 57.13  ? 159 LEU   B CG  1 
ATOM   2007 C  CD1 . LEU   B 2 43  ? -52.876 6.906   -8.531  1.00 61.95  ? 159 LEU   B CD1 1 
ATOM   2008 C  CD2 . LEU   B 2 43  ? -52.189 5.201   -10.240 1.00 63.62  ? 159 LEU   B CD2 1 
ATOM   2009 N  N   . ILE   B 2 44  ? -47.933 4.515   -7.034  1.00 44.40  ? 160 ILE   B N   1 
ATOM   2010 C  CA  . ILE   B 2 44  ? -46.458 4.534   -6.834  1.00 39.73  ? 160 ILE   B CA  1 
ATOM   2011 C  C   . ILE   B 2 44  ? -45.913 3.223   -7.375  1.00 40.23  ? 160 ILE   B C   1 
ATOM   2012 O  O   . ILE   B 2 44  ? -44.971 3.280   -8.199  1.00 34.70  ? 160 ILE   B O   1 
ATOM   2013 C  CB  . ILE   B 2 44  ? -46.068 4.784   -5.363  1.00 41.99  ? 160 ILE   B CB  1 
ATOM   2014 C  CG1 . ILE   B 2 44  ? -46.446 6.197   -4.903  1.00 44.58  ? 160 ILE   B CG1 1 
ATOM   2015 C  CG2 . ILE   B 2 44  ? -44.587 4.512   -5.159  1.00 38.19  ? 160 ILE   B CG2 1 
ATOM   2016 C  CD1 . ILE   B 2 44  ? -46.661 6.317   -3.403  1.00 45.05  ? 160 ILE   B CD1 1 
ATOM   2017 N  N   . ALA   B 2 45  ? -46.501 2.095   -6.953  1.00 35.17  ? 161 ALA   B N   1 
ATOM   2018 C  CA  . ALA   B 2 45  ? -46.057 0.738   -7.344  1.00 39.24  ? 161 ALA   B CA  1 
ATOM   2019 C  C   . ALA   B 2 45  ? -46.127 0.597   -8.871  1.00 36.72  ? 161 ALA   B C   1 
ATOM   2020 O  O   . ALA   B 2 45  ? -45.188 0.009   -9.456  1.00 41.54  ? 161 ALA   B O   1 
ATOM   2021 C  CB  . ALA   B 2 45  ? -46.868 -0.338  -6.637  1.00 37.57  ? 161 ALA   B CB  1 
ATOM   2022 N  N   . LYS   B 2 46  ? -47.185 1.108   -9.501  1.00 43.31  ? 162 LYS   B N   1 
ATOM   2023 C  CA  . LYS   B 2 46  ? -47.350 0.978   -10.974 1.00 45.37  ? 162 LYS   B CA  1 
ATOM   2024 C  C   . LYS   B 2 46  ? -46.389 1.936   -11.693 1.00 45.27  ? 162 LYS   B C   1 
ATOM   2025 O  O   . LYS   B 2 46  ? -45.906 1.555   -12.740 1.00 40.98  ? 162 LYS   B O   1 
ATOM   2026 C  CB  . LYS   B 2 46  ? -48.816 1.149   -11.380 1.00 53.61  ? 162 LYS   B CB  1 
ATOM   2027 C  CG  . LYS   B 2 46  ? -49.608 -0.156  -11.333 1.00 59.15  ? 162 LYS   B CG  1 
ATOM   2028 C  CD  . LYS   B 2 46  ? -51.112 0.015   -11.213 1.00 61.97  ? 162 LYS   B CD  1 
ATOM   2029 C  CE  . LYS   B 2 46  ? -51.866 -1.302  -11.258 1.00 62.94  ? 162 LYS   B CE  1 
ATOM   2030 N  NZ  . LYS   B 2 46  ? -53.309 -1.119  -10.942 1.00 65.64  ? 162 LYS   B NZ  1 
ATOM   2031 N  N   . SER   B 2 47  ? -46.090 3.125   -11.165 1.00 45.75  ? 163 SER   B N   1 
ATOM   2032 C  CA  . SER   B 2 47  ? -45.229 4.093   -11.899 1.00 44.69  ? 163 SER   B CA  1 
ATOM   2033 C  C   . SER   B 2 47  ? -43.750 3.764   -11.671 1.00 42.87  ? 163 SER   B C   1 
ATOM   2034 O  O   . SER   B 2 47  ? -42.934 4.297   -12.440 1.00 42.19  ? 163 SER   B O   1 
ATOM   2035 C  CB  . SER   B 2 47  ? -45.523 5.542   -11.587 1.00 51.00  ? 163 SER   B CB  1 
ATOM   2036 O  OG  . SER   B 2 47  ? -45.684 5.765   -10.206 1.00 51.00  ? 163 SER   B OG  1 
ATOM   2037 N  N   . ASN   B 2 48  ? -43.414 2.946   -10.663 1.00 40.12  ? 164 ASN   B N   1 
ATOM   2038 C  CA  . ASN   B 2 48  ? -42.001 2.705   -10.251 1.00 36.07  ? 164 ASN   B CA  1 
ATOM   2039 C  C   . ASN   B 2 48  ? -41.178 2.116   -11.407 1.00 38.43  ? 164 ASN   B C   1 
ATOM   2040 O  O   . ASN   B 2 48  ? -41.575 1.106   -12.061 1.00 35.20  ? 164 ASN   B O   1 
ATOM   2041 C  CB  . ASN   B 2 48  ? -41.849 1.759   -9.060  1.00 34.68  ? 164 ASN   B CB  1 
ATOM   2042 C  CG  . ASN   B 2 48  ? -42.020 2.430   -7.717  1.00 34.75  ? 164 ASN   B CG  1 
ATOM   2043 O  OD1 . ASN   B 2 48  ? -41.830 3.628   -7.605  1.00 32.23  ? 164 ASN   B OD1 1 
ATOM   2044 N  ND2 . ASN   B 2 48  ? -42.355 1.664   -6.689  1.00 34.16  ? 164 ASN   B ND2 1 
ATOM   2045 N  N   . THR   B 2 49  ? -39.977 2.649   -11.580 1.00 33.18  ? 165 THR   B N   1 
ATOM   2046 C  CA  . THR   B 2 49  ? -38.966 2.059   -12.466 1.00 32.14  ? 165 THR   B CA  1 
ATOM   2047 C  C   . THR   B 2 49  ? -38.575 0.715   -11.879 1.00 34.82  ? 165 THR   B C   1 
ATOM   2048 O  O   . THR   B 2 49  ? -38.688 0.482   -10.676 1.00 32.23  ? 165 THR   B O   1 
ATOM   2049 C  CB  . THR   B 2 49  ? -37.760 2.996   -12.605 1.00 37.75  ? 165 THR   B CB  1 
ATOM   2050 O  OG1 . THR   B 2 49  ? -37.252 3.230   -11.290 1.00 34.38  ? 165 THR   B OG1 1 
ATOM   2051 C  CG2 . THR   B 2 49  ? -38.128 4.320   -13.242 1.00 39.53  ? 165 THR   B CG2 1 
ATOM   2052 N  N   . PRO   B 2 50  ? -38.087 -0.205  -12.722 1.00 35.03  ? 166 PRO   B N   1 
ATOM   2053 C  CA  . PRO   B 2 50  ? -37.455 -1.420  -12.237 1.00 38.20  ? 166 PRO   B CA  1 
ATOM   2054 C  C   . PRO   B 2 50  ? -36.300 -1.018  -11.332 1.00 32.94  ? 166 PRO   B C   1 
ATOM   2055 O  O   . PRO   B 2 50  ? -35.679 0.023   -11.546 1.00 32.62  ? 166 PRO   B O   1 
ATOM   2056 C  CB  . PRO   B 2 50  ? -36.932 -2.079  -13.515 1.00 40.50  ? 166 PRO   B CB  1 
ATOM   2057 C  CG  . PRO   B 2 50  ? -37.806 -1.512  -14.602 1.00 38.30  ? 166 PRO   B CG  1 
ATOM   2058 C  CD  . PRO   B 2 50  ? -38.074 -0.089  -14.188 1.00 40.63  ? 166 PRO   B CD  1 
ATOM   2059 N  N   . PRO   B 2 51  ? -35.997 -1.763  -10.261 1.00 34.11  ? 167 PRO   B N   1 
ATOM   2060 C  CA  . PRO   B 2 51  ? -34.846 -1.415  -9.439  1.00 29.24  ? 167 PRO   B CA  1 
ATOM   2061 C  C   . PRO   B 2 51  ? -33.563 -1.379  -10.282 1.00 30.50  ? 167 PRO   B C   1 
ATOM   2062 O  O   . PRO   B 2 51  ? -33.315 -2.246  -11.136 1.00 26.56  ? 167 PRO   B O   1 
ATOM   2063 C  CB  . PRO   B 2 51  ? -34.786 -2.508  -8.366  1.00 31.45  ? 167 PRO   B CB  1 
ATOM   2064 C  CG  . PRO   B 2 51  ? -35.722 -3.591  -8.861  1.00 30.73  ? 167 PRO   B CG  1 
ATOM   2065 C  CD  . PRO   B 2 51  ? -36.747 -2.911  -9.728  1.00 31.44  ? 167 PRO   B CD  1 
ATOM   2066 N  N   A MET   B 2 52  ? -32.730 -0.362  -10.070 0.50 26.58  ? 168 MET   B N   1 
ATOM   2067 N  N   B MET   B 2 52  ? -32.723 -0.394  -9.970  0.50 29.16  ? 168 MET   B N   1 
ATOM   2068 C  CA  A MET   B 2 52  ? -31.393 -0.284  -10.713 0.50 23.91  ? 168 MET   B CA  1 
ATOM   2069 C  CA  B MET   B 2 52  ? -31.407 -0.173  -10.613 0.50 27.88  ? 168 MET   B CA  1 
ATOM   2070 C  C   A MET   B 2 52  ? -30.371 -0.020  -9.612  0.50 22.67  ? 168 MET   B C   1 
ATOM   2071 C  C   B MET   B 2 52  ? -30.362 -0.056  -9.516  0.50 24.85  ? 168 MET   B C   1 
ATOM   2072 O  O   A MET   B 2 52  ? -30.708 0.710   -8.659  0.50 23.71  ? 168 MET   B O   1 
ATOM   2073 O  O   B MET   B 2 52  ? -30.653 0.538   -8.460  0.50 25.39  ? 168 MET   B O   1 
ATOM   2074 C  CB  A MET   B 2 52  ? -31.327 0.786   -11.815 0.50 24.28  ? 168 MET   B CB  1 
ATOM   2075 C  CB  B MET   B 2 52  ? -31.406 1.100   -11.461 0.50 32.68  ? 168 MET   B CB  1 
ATOM   2076 C  CG  A MET   B 2 52  ? -30.268 0.504   -12.872 0.50 23.62  ? 168 MET   B CG  1 
ATOM   2077 C  CG  B MET   B 2 52  ? -32.385 1.034   -12.591 0.50 36.61  ? 168 MET   B CG  1 
ATOM   2078 S  SD  A MET   B 2 52  ? -30.319 1.608   -14.330 0.50 30.54  ? 168 MET   B SD  1 
ATOM   2079 S  SD  B MET   B 2 52  ? -31.787 -0.080  -13.858 0.50 45.02  ? 168 MET   B SD  1 
ATOM   2080 C  CE  A MET   B 2 52  ? -31.547 0.808   -15.351 0.50 28.87  ? 168 MET   B CE  1 
ATOM   2081 C  CE  B MET   B 2 52  ? -31.086 1.110   -15.000 0.50 36.99  ? 168 MET   B CE  1 
ATOM   2082 N  N   . TYR   B 2 53  ? -29.171 -0.581  -9.749  1.00 23.03  ? 169 TYR   B N   1 
ATOM   2083 C  CA  . TYR   B 2 53  ? -28.157 -0.596  -8.690  1.00 23.82  ? 169 TYR   B CA  1 
ATOM   2084 C  C   . TYR   B 2 53  ? -26.778 -0.701  -9.330  1.00 27.12  ? 169 TYR   B C   1 
ATOM   2085 O  O   . TYR   B 2 53  ? -26.589 -1.288  -10.421 1.00 27.70  ? 169 TYR   B O   1 
ATOM   2086 C  CB  . TYR   B 2 53  ? -28.474 -1.703  -7.681  1.00 24.05  ? 169 TYR   B CB  1 
ATOM   2087 C  CG  . TYR   B 2 53  ? -28.777 -3.021  -8.341  1.00 23.65  ? 169 TYR   B CG  1 
ATOM   2088 C  CD1 . TYR   B 2 53  ? -30.062 -3.334  -8.739  1.00 24.73  ? 169 TYR   B CD1 1 
ATOM   2089 C  CD2 . TYR   B 2 53  ? -27.760 -3.915  -8.609  1.00 25.88  ? 169 TYR   B CD2 1 
ATOM   2090 C  CE1 . TYR   B 2 53  ? -30.331 -4.536  -9.376  1.00 26.26  ? 169 TYR   B CE1 1 
ATOM   2091 C  CE2 . TYR   B 2 53  ? -28.000 -5.121  -9.239  1.00 24.74  ? 169 TYR   B CE2 1 
ATOM   2092 C  CZ  . TYR   B 2 53  ? -29.300 -5.427  -9.621  1.00 27.55  ? 169 TYR   B CZ  1 
ATOM   2093 O  OH  . TYR   B 2 53  ? -29.582 -6.601  -10.262 1.00 27.08  ? 169 TYR   B OH  1 
ATOM   2094 N  N   . LEU   B 2 54  ? -25.817 -0.124  -8.628  1.00 24.04  ? 170 LEU   B N   1 
ATOM   2095 C  CA  . LEU   B 2 54  ? -24.412 -0.010  -9.088  1.00 26.08  ? 170 LEU   B CA  1 
ATOM   2096 C  C   . LEU   B 2 54  ? -23.499 -0.065  -7.879  1.00 26.00  ? 170 LEU   B C   1 
ATOM   2097 O  O   . LEU   B 2 54  ? -23.673 0.766   -6.935  1.00 28.28  ? 170 LEU   B O   1 
ATOM   2098 C  CB  . LEU   B 2 54  ? -24.253 1.297   -9.850  1.00 25.30  ? 170 LEU   B CB  1 
ATOM   2099 C  CG  . LEU   B 2 54  ? -22.831 1.610   -10.327 1.00 29.07  ? 170 LEU   B CG  1 
ATOM   2100 C  CD1 . LEU   B 2 54  ? -22.427 0.666   -11.457 1.00 29.40  ? 170 LEU   B CD1 1 
ATOM   2101 C  CD2 . LEU   B 2 54  ? -22.735 3.067   -10.759 1.00 28.83  ? 170 LEU   B CD2 1 
ATOM   2102 N  N   . GLN   B 2 55  ? -22.627 -1.053  -7.863  1.00 24.78  ? 171 GLN   B N   1 
ATOM   2103 C  CA  . GLN   B 2 55  ? -21.489 -1.117  -6.919  1.00 26.24  ? 171 GLN   B CA  1 
ATOM   2104 C  C   . GLN   B 2 55  ? -20.540 0.018   -7.319  1.00 30.06  ? 171 GLN   B C   1 
ATOM   2105 O  O   . GLN   B 2 55  ? -20.172 0.109   -8.487  1.00 28.31  ? 171 GLN   B O   1 
ATOM   2106 C  CB  . GLN   B 2 55  ? -20.751 -2.451  -6.943  1.00 29.12  ? 171 GLN   B CB  1 
ATOM   2107 C  CG  . GLN   B 2 55  ? -19.711 -2.586  -5.822  1.00 33.30  ? 171 GLN   B CG  1 
ATOM   2108 C  CD  . GLN   B 2 55  ? -18.415 -1.821  -6.074  1.00 42.24  ? 171 GLN   B CD  1 
ATOM   2109 O  OE1 . GLN   B 2 55  ? -18.045 -1.557  -7.210  1.00 47.46  ? 171 GLN   B OE1 1 
ATOM   2110 N  NE2 . GLN   B 2 55  ? -17.680 -1.466  -5.021  1.00 44.09  ? 171 GLN   B NE2 1 
ATOM   2111 N  N   . ALA   B 2 56  ? -20.186 0.872   -6.375  1.00 28.83  ? 172 ALA   B N   1 
ATOM   2112 C  CA  . ALA   B 2 56  ? -19.272 1.996   -6.645  1.00 33.02  ? 172 ALA   B CA  1 
ATOM   2113 C  C   . ALA   B 2 56  ? -18.689 2.446   -5.319  1.00 33.58  ? 172 ALA   B C   1 
ATOM   2114 O  O   . ALA   B 2 56  ? -19.439 2.578   -4.354  1.00 31.57  ? 172 ALA   B O   1 
ATOM   2115 C  CB  . ALA   B 2 56  ? -19.971 3.108   -7.380  1.00 31.55  ? 172 ALA   B CB  1 
ATOM   2116 N  N   . ASP   B 2 57  ? -17.363 2.522   -5.290  1.00 38.25  ? 173 ASP   B N   1 
ATOM   2117 C  CA  A ASP   B 2 57  ? -16.597 3.133   -4.171  0.70 43.58  ? 173 ASP   B CA  1 
ATOM   2118 C  CA  B ASP   B 2 57  ? -16.564 3.134   -4.196  0.30 40.72  ? 173 ASP   B CA  1 
ATOM   2119 C  C   . ASP   B 2 57  ? -16.733 4.653   -4.350  1.00 39.14  ? 173 ASP   B C   1 
ATOM   2120 O  O   . ASP   B 2 57  ? -16.063 5.227   -5.209  1.00 39.69  ? 173 ASP   B O   1 
ATOM   2121 C  CB  A ASP   B 2 57  ? -15.191 2.533   -4.105  0.70 44.41  ? 173 ASP   B CB  1 
ATOM   2122 C  CB  B ASP   B 2 57  ? -15.134 2.580   -4.254  0.30 41.47  ? 173 ASP   B CB  1 
ATOM   2123 C  CG  A ASP   B 2 57  ? -15.215 1.038   -3.812  0.70 47.01  ? 173 ASP   B CG  1 
ATOM   2124 C  CG  B ASP   B 2 57  ? -14.074 3.399   -3.543  0.30 43.66  ? 173 ASP   B CG  1 
ATOM   2125 O  OD1 A ASP   B 2 57  ? -15.739 0.655   -2.755  0.70 49.17  ? 173 ASP   B OD1 1 
ATOM   2126 O  OD1 B ASP   B 2 57  ? -14.084 4.623   -3.716  0.30 46.49  ? 173 ASP   B OD1 1 
ATOM   2127 O  OD2 A ASP   B 2 57  ? -14.726 0.258   -4.657  0.70 59.62  ? 173 ASP   B OD2 1 
ATOM   2128 O  OD2 B ASP   B 2 57  ? -13.229 2.798   -2.844  0.30 42.42  ? 173 ASP   B OD2 1 
ATOM   2129 N  N   . ILE   B 2 58  ? -17.650 5.253   -3.586  1.00 36.07  ? 174 ILE   B N   1 
ATOM   2130 C  CA  . ILE   B 2 58  ? -18.140 6.636   -3.836  1.00 36.86  ? 174 ILE   B CA  1 
ATOM   2131 C  C   . ILE   B 2 58  ? -17.008 7.658   -3.567  1.00 38.57  ? 174 ILE   B C   1 
ATOM   2132 O  O   . ILE   B 2 58  ? -17.096 8.762   -4.125  1.00 43.49  ? 174 ILE   B O   1 
ATOM   2133 C  CB  . ILE   B 2 58  ? -19.422 6.899   -3.015  1.00 37.56  ? 174 ILE   B CB  1 
ATOM   2134 C  CG1 . ILE   B 2 58  ? -20.586 6.051   -3.534  1.00 37.95  ? 174 ILE   B CG1 1 
ATOM   2135 C  CG2 . ILE   B 2 58  ? -19.788 8.356   -2.986  1.00 33.90  ? 174 ILE   B CG2 1 
ATOM   2136 C  CD1 . ILE   B 2 58  ? -21.707 5.878   -2.519  1.00 35.61  ? 174 ILE   B CD1 1 
ATOM   2137 N  N   . GLU   B 2 59  ? -15.991 7.309   -2.788  1.00 38.69  ? 175 GLU   B N   1 
ATOM   2138 C  CA  . GLU   B 2 59  ? -14.805 8.204   -2.562  1.00 52.09  ? 175 GLU   B CA  1 
ATOM   2139 C  C   . GLU   B 2 59  ? -13.922 8.257   -3.817  1.00 55.20  ? 175 GLU   B C   1 
ATOM   2140 O  O   . GLU   B 2 59  ? -13.385 9.352   -4.087  1.00 58.26  ? 175 GLU   B O   1 
ATOM   2141 C  CB  . GLU   B 2 59  ? -13.981 7.802   -1.336  1.00 54.19  ? 175 GLU   B CB  1 
ATOM   2142 C  CG  . GLU   B 2 59  ? -13.266 6.464   -1.446  1.00 62.79  ? 175 GLU   B CG  1 
ATOM   2143 C  CD  . GLU   B 2 59  ? -14.160 5.267   -1.159  1.00 67.91  ? 175 GLU   B CD  1 
ATOM   2144 O  OE1 . GLU   B 2 59  ? -15.336 5.286   -1.597  1.00 68.66  ? 175 GLU   B OE1 1 
ATOM   2145 O  OE2 . GLU   B 2 59  ? -13.686 4.321   -0.507  1.00 63.92  ? 175 GLU   B OE2 1 
ATOM   2146 N  N   . ALA   B 2 60  ? -13.790 7.139   -4.554  1.00 54.65  ? 176 ALA   B N   1 
ATOM   2147 C  CA  . ALA   B 2 60  ? -12.975 7.021   -5.793  1.00 54.19  ? 176 ALA   B CA  1 
ATOM   2148 C  C   . ALA   B 2 60  ? -13.774 7.502   -7.009  1.00 61.80  ? 176 ALA   B C   1 
ATOM   2149 O  O   . ALA   B 2 60  ? -13.187 8.181   -7.864  1.00 74.86  ? 176 ALA   B O   1 
ATOM   2150 C  CB  . ALA   B 2 60  ? -12.508 5.600   -5.987  1.00 54.77  ? 176 ALA   B CB  1 
ATOM   2151 N  N   . PHE   B 2 61  ? -15.072 7.195   -7.042  1.00 58.42  ? 177 PHE   B N   1 
ATOM   2152 C  CA  . PHE   B 2 61  ? -15.993 7.296   -8.205  1.00 53.17  ? 177 PHE   B CA  1 
ATOM   2153 C  C   . PHE   B 2 61  ? -16.400 8.751   -8.444  1.00 53.07  ? 177 PHE   B C   1 
ATOM   2154 O  O   . PHE   B 2 61  ? -16.614 9.469   -7.471  1.00 61.41  ? 177 PHE   B O   1 
ATOM   2155 C  CB  . PHE   B 2 61  ? -17.185 6.382   -7.912  1.00 53.12  ? 177 PHE   B CB  1 
ATOM   2156 C  CG  . PHE   B 2 61  ? -18.398 6.471   -8.799  1.00 49.28  ? 177 PHE   B CG  1 
ATOM   2157 C  CD1 . PHE   B 2 61  ? -18.429 5.844   -10.038 1.00 51.14  ? 177 PHE   B CD1 1 
ATOM   2158 C  CD2 . PHE   B 2 61  ? -19.553 7.085   -8.337  1.00 44.69  ? 177 PHE   B CD2 1 
ATOM   2159 C  CE1 . PHE   B 2 61  ? -19.576 5.880   -10.819 1.00 49.35  ? 177 PHE   B CE1 1 
ATOM   2160 C  CE2 . PHE   B 2 61  ? -20.699 7.122   -9.111  1.00 43.24  ? 177 PHE   B CE2 1 
ATOM   2161 C  CZ  . PHE   B 2 61  ? -20.716 6.504   -10.341 1.00 48.18  ? 177 PHE   B CZ  1 
ATOM   2162 N  N   . ASP   B 2 62  ? -16.471 9.150   -9.720  1.00 51.58  ? 178 ASP   B N   1 
ATOM   2163 C  CA  . ASP   B 2 62  ? -16.935 10.475  -10.210 1.00 48.22  ? 178 ASP   B CA  1 
ATOM   2164 C  C   . ASP   B 2 62  ? -18.459 10.435  -10.281 1.00 44.04  ? 178 ASP   B C   1 
ATOM   2165 O  O   . ASP   B 2 62  ? -19.014 9.817   -11.227 1.00 40.53  ? 178 ASP   B O   1 
ATOM   2166 C  CB  . ASP   B 2 62  ? -16.362 10.800  -11.591 1.00 50.60  ? 178 ASP   B CB  1 
ATOM   2167 C  CG  . ASP   B 2 62  ? -16.843 12.096  -12.240 1.00 56.58  ? 178 ASP   B CG  1 
ATOM   2168 O  OD1 . ASP   B 2 62  ? -17.546 12.911  -11.575 1.00 50.12  ? 178 ASP   B OD1 1 
ATOM   2169 O  OD2 . ASP   B 2 62  ? -16.508 12.284  -13.427 1.00 58.00  ? 178 ASP   B OD2 1 
ATOM   2170 N  N   . ILE   B 2 63  ? -19.091 11.114  -9.335  1.00 45.60  ? 179 ILE   B N   1 
ATOM   2171 C  CA  . ILE   B 2 63  ? -20.566 11.140  -9.122  1.00 51.03  ? 179 ILE   B CA  1 
ATOM   2172 C  C   . ILE   B 2 63  ? -21.266 11.609  -10.404 1.00 44.30  ? 179 ILE   B C   1 
ATOM   2173 O  O   . ILE   B 2 63  ? -22.421 11.189  -10.645 1.00 37.72  ? 179 ILE   B O   1 
ATOM   2174 C  CB  . ILE   B 2 63  ? -20.893 12.007  -7.877  1.00 58.53  ? 179 ILE   B CB  1 
ATOM   2175 C  CG1 . ILE   B 2 63  ? -21.992 11.362  -7.037  1.00 66.94  ? 179 ILE   B CG1 1 
ATOM   2176 C  CG2 . ILE   B 2 63  ? -21.212 13.453  -8.229  1.00 57.47  ? 179 ILE   B CG2 1 
ATOM   2177 C  CD1 . ILE   B 2 63  ? -21.560 10.055  -6.407  1.00 71.86  ? 179 ILE   B CD1 1 
ATOM   2178 N  N   . ARG   B 2 64  ? -20.601 12.407  -11.241 1.00 44.58  ? 180 ARG   B N   1 
ATOM   2179 C  CA  . ARG   B 2 64  ? -21.244 12.969  -12.460 1.00 50.73  ? 180 ARG   B CA  1 
ATOM   2180 C  C   . ARG   B 2 64  ? -21.584 11.863  -13.467 1.00 45.45  ? 180 ARG   B C   1 
ATOM   2181 O  O   . ARG   B 2 64  ? -22.377 12.140  -14.354 1.00 45.41  ? 180 ARG   B O   1 
ATOM   2182 C  CB  . ARG   B 2 64  ? -20.371 14.058  -13.087 1.00 58.73  ? 180 ARG   B CB  1 
ATOM   2183 C  CG  . ARG   B 2 64  ? -20.457 15.388  -12.352 1.00 67.55  ? 180 ARG   B CG  1 
ATOM   2184 C  CD  . ARG   B 2 64  ? -19.082 15.909  -11.991 1.00 81.06  ? 180 ARG   B CD  1 
ATOM   2185 N  NE  . ARG   B 2 64  ? -18.228 15.912  -13.172 1.00 85.03  ? 180 ARG   B NE  1 
ATOM   2186 C  CZ  . ARG   B 2 64  ? -16.922 15.667  -13.178 1.00 92.61  ? 180 ARG   B CZ  1 
ATOM   2187 N  NH1 . ARG   B 2 64  ? -16.278 15.393  -12.054 1.00 101.68 ? 180 ARG   B NH1 1 
ATOM   2188 N  NH2 . ARG   B 2 64  ? -16.261 15.694  -14.322 1.00 90.93  ? 180 ARG   B NH2 1 
ATOM   2189 N  N   . GLU   B 2 65  ? -21.045 10.650  -13.318 1.00 46.55  ? 181 GLU   B N   1 
ATOM   2190 C  CA  . GLU   B 2 65  ? -21.387 9.492   -14.198 1.00 49.16  ? 181 GLU   B CA  1 
ATOM   2191 C  C   . GLU   B 2 65  ? -22.836 9.049   -13.971 1.00 52.77  ? 181 GLU   B C   1 
ATOM   2192 O  O   . GLU   B 2 65  ? -23.323 8.216   -14.793 1.00 44.09  ? 181 GLU   B O   1 
ATOM   2193 C  CB  . GLU   B 2 65  ? -20.492 8.287   -13.916 1.00 52.92  ? 181 GLU   B CB  1 
ATOM   2194 C  CG  . GLU   B 2 65  ? -19.056 8.511   -14.352 1.00 62.90  ? 181 GLU   B CG  1 
ATOM   2195 C  CD  . GLU   B 2 65  ? -18.133 7.330   -14.110 1.00 62.85  ? 181 GLU   B CD  1 
ATOM   2196 O  OE1 . GLU   B 2 65  ? -16.929 7.580   -13.900 1.00 67.74  ? 181 GLU   B OE1 1 
ATOM   2197 O  OE2 . GLU   B 2 65  ? -18.622 6.168   -14.113 1.00 66.23  ? 181 GLU   B OE2 1 
ATOM   2198 N  N   . LEU   B 2 66  ? -23.467 9.510   -12.875 1.00 45.61  ? 182 LEU   B N   1 
ATOM   2199 C  CA  . LEU   B 2 66  ? -24.864 9.149   -12.536 1.00 43.13  ? 182 LEU   B CA  1 
ATOM   2200 C  C   . LEU   B 2 66  ? -25.777 10.183  -13.169 1.00 42.57  ? 182 LEU   B C   1 
ATOM   2201 O  O   . LEU   B 2 66  ? -25.852 11.298  -12.638 1.00 43.78  ? 182 LEU   B O   1 
ATOM   2202 C  CB  . LEU   B 2 66  ? -25.088 9.133   -11.022 1.00 41.57  ? 182 LEU   B CB  1 
ATOM   2203 C  CG  . LEU   B 2 66  ? -24.266 8.131   -10.225 1.00 42.10  ? 182 LEU   B CG  1 
ATOM   2204 C  CD1 . LEU   B 2 66  ? -24.559 8.319   -8.760  1.00 38.60  ? 182 LEU   B CD1 1 
ATOM   2205 C  CD2 . LEU   B 2 66  ? -24.551 6.693   -10.655 1.00 45.71  ? 182 LEU   B CD2 1 
ATOM   2206 N  N   . THR   B 2 67  ? -26.445 9.805   -14.244 1.00 35.91  ? 183 THR   B N   1 
ATOM   2207 C  CA  . THR   B 2 67  ? -27.386 10.667  -14.984 1.00 40.74  ? 183 THR   B CA  1 
ATOM   2208 C  C   . THR   B 2 67  ? -28.681 9.874   -15.099 1.00 39.28  ? 183 THR   B C   1 
ATOM   2209 O  O   . THR   B 2 67  ? -28.642 8.643   -14.994 1.00 37.75  ? 183 THR   B O   1 
ATOM   2210 C  CB  . THR   B 2 67  ? -26.786 11.070  -16.341 1.00 45.97  ? 183 THR   B CB  1 
ATOM   2211 O  OG1 . THR   B 2 67  ? -26.342 9.889   -17.029 1.00 41.04  ? 183 THR   B OG1 1 
ATOM   2212 C  CG2 . THR   B 2 67  ? -25.628 12.029  -16.188 1.00 44.08  ? 183 THR   B CG2 1 
ATOM   2213 N  N   . PRO   B 2 68  ? -29.830 10.530  -15.374 1.00 39.11  ? 184 PRO   B N   1 
ATOM   2214 C  CA  . PRO   B 2 68  ? -29.910 11.987  -15.466 1.00 38.83  ? 184 PRO   B CA  1 
ATOM   2215 C  C   . PRO   B 2 68  ? -29.930 12.599  -14.059 1.00 36.58  ? 184 PRO   B C   1 
ATOM   2216 O  O   . PRO   B 2 68  ? -29.801 11.860  -13.127 1.00 36.87  ? 184 PRO   B O   1 
ATOM   2217 C  CB  . PRO   B 2 68  ? -31.240 12.232  -16.213 1.00 41.56  ? 184 PRO   B CB  1 
ATOM   2218 C  CG  . PRO   B 2 68  ? -32.097 11.032  -15.870 1.00 41.54  ? 184 PRO   B CG  1 
ATOM   2219 C  CD  . PRO   B 2 68  ? -31.117 9.892   -15.688 1.00 43.82  ? 184 PRO   B CD  1 
ATOM   2220 N  N   . LYS   B 2 69  ? -30.192 13.899  -13.959 1.00 33.82  ? 185 LYS   B N   1 
ATOM   2221 C  CA  . LYS   B 2 69  ? -30.260 14.660  -12.686 1.00 35.10  ? 185 LYS   B CA  1 
ATOM   2222 C  C   . LYS   B 2 69  ? -31.454 14.179  -11.870 1.00 32.73  ? 185 LYS   B C   1 
ATOM   2223 O  O   . LYS   B 2 69  ? -32.502 13.951  -12.441 1.00 40.35  ? 185 LYS   B O   1 
ATOM   2224 C  CB  . LYS   B 2 69  ? -30.291 16.154  -13.013 1.00 35.21  ? 185 LYS   B CB  1 
ATOM   2225 C  CG  . LYS   B 2 69  ? -28.937 16.630  -13.543 1.00 41.09  ? 185 LYS   B CG  1 
ATOM   2226 C  CD  . LYS   B 2 69  ? -28.862 18.094  -13.804 1.00 46.46  ? 185 LYS   B CD  1 
ATOM   2227 C  CE  . LYS   B 2 69  ? -27.587 18.450  -14.538 1.00 49.34  ? 185 LYS   B CE  1 
ATOM   2228 N  NZ  . LYS   B 2 69  ? -26.393 18.037  -13.762 1.00 49.48  ? 185 LYS   B NZ  1 
ATOM   2229 N  N   . PHE   B 2 70  ? -31.270 14.042  -10.562 1.00 30.51  ? 186 PHE   B N   1 
ATOM   2230 C  CA  . PHE   B 2 70  ? -32.234 13.372  -9.658  1.00 28.80  ? 186 PHE   B CA  1 
ATOM   2231 C  C   . PHE   B 2 70  ? -33.250 14.350  -9.092  1.00 28.56  ? 186 PHE   B C   1 
ATOM   2232 O  O   . PHE   B 2 70  ? -32.915 15.494  -8.732  1.00 30.66  ? 186 PHE   B O   1 
ATOM   2233 C  CB  . PHE   B 2 70  ? -31.429 12.605  -8.607  1.00 26.33  ? 186 PHE   B CB  1 
ATOM   2234 C  CG  . PHE   B 2 70  ? -30.606 11.527  -9.256  1.00 24.82  ? 186 PHE   B CG  1 
ATOM   2235 C  CD1 . PHE   B 2 70  ? -31.210 10.328  -9.620  1.00 26.52  ? 186 PHE   B CD1 1 
ATOM   2236 C  CD2 . PHE   B 2 70  ? -29.264 11.719  -9.572  1.00 25.15  ? 186 PHE   B CD2 1 
ATOM   2237 C  CE1 . PHE   B 2 70  ? -30.471 9.329   -10.227 1.00 26.99  ? 186 PHE   B CE1 1 
ATOM   2238 C  CE2 . PHE   B 2 70  ? -28.525 10.714  -10.186 1.00 26.76  ? 186 PHE   B CE2 1 
ATOM   2239 C  CZ  . PHE   B 2 70  ? -29.137 9.527   -10.526 1.00 26.97  ? 186 PHE   B CZ  1 
ATOM   2240 N  N   . ASP   B 2 71  ? -34.480 13.867  -8.978  1.00 31.52  ? 187 ASP   B N   1 
ATOM   2241 C  CA  . ASP   B 2 71  ? -35.600 14.544  -8.271  1.00 31.64  ? 187 ASP   B CA  1 
ATOM   2242 C  C   . ASP   B 2 71  ? -35.419 14.406  -6.760  1.00 27.38  ? 187 ASP   B C   1 
ATOM   2243 O  O   . ASP   B 2 71  ? -35.782 15.352  -6.008  1.00 26.94  ? 187 ASP   B O   1 
ATOM   2244 C  CB  . ASP   B 2 71  ? -36.920 13.931  -8.741  1.00 33.84  ? 187 ASP   B CB  1 
ATOM   2245 C  CG  . ASP   B 2 71  ? -37.093 14.037  -10.243 1.00 36.24  ? 187 ASP   B CG  1 
ATOM   2246 O  OD1 . ASP   B 2 71  ? -37.033 15.177  -10.722 1.00 33.60  ? 187 ASP   B OD1 1 
ATOM   2247 O  OD2 . ASP   B 2 71  ? -37.245 12.982  -10.923 1.00 32.82  ? 187 ASP   B OD2 1 
ATOM   2248 N  N   . VAL   B 2 72  ? -34.965 13.230  -6.308  1.00 27.34  ? 188 VAL   B N   1 
ATOM   2249 C  CA  . VAL   B 2 72  ? -34.779 12.900  -4.867  1.00 27.82  ? 188 VAL   B CA  1 
ATOM   2250 C  C   . VAL   B 2 72  ? -33.458 12.175  -4.672  1.00 25.44  ? 188 VAL   B C   1 
ATOM   2251 O  O   . VAL   B 2 72  ? -33.138 11.258  -5.469  1.00 25.34  ? 188 VAL   B O   1 
ATOM   2252 C  CB  . VAL   B 2 72  ? -35.928 12.052  -4.299  1.00 32.56  ? 188 VAL   B CB  1 
ATOM   2253 C  CG1 . VAL   B 2 72  ? -35.779 11.960  -2.797  1.00 35.56  ? 188 VAL   B CG1 1 
ATOM   2254 C  CG2 . VAL   B 2 72  ? -37.277 12.644  -4.664  1.00 35.55  ? 188 VAL   B CG2 1 
ATOM   2255 N  N   . ILE   B 2 73  ? -32.706 12.594  -3.655  1.00 22.36  ? 189 ILE   B N   1 
ATOM   2256 C  CA  . ILE   B 2 73  ? -31.454 11.935  -3.240  1.00 23.77  ? 189 ILE   B CA  1 
ATOM   2257 C  C   . ILE   B 2 73  ? -31.619 11.586  -1.766  1.00 23.24  ? 189 ILE   B C   1 
ATOM   2258 O  O   . ILE   B 2 73  ? -31.875 12.484  -0.964  1.00 22.63  ? 189 ILE   B O   1 
ATOM   2259 C  CB  . ILE   B 2 73  ? -30.199 12.792  -3.530  1.00 22.37  ? 189 ILE   B CB  1 
ATOM   2260 C  CG1 . ILE   B 2 73  ? -30.055 13.113  -5.012  1.00 24.08  ? 189 ILE   B CG1 1 
ATOM   2261 C  CG2 . ILE   B 2 73  ? -28.974 12.044  -3.073  1.00 26.34  ? 189 ILE   B CG2 1 
ATOM   2262 C  CD1 . ILE   B 2 73  ? -28.974 14.141  -5.311  1.00 25.33  ? 189 ILE   B CD1 1 
ATOM   2263 N  N   . LEU   B 2 74  ? -31.465 10.301  -1.452  1.00 20.95  ? 190 LEU   B N   1 
ATOM   2264 C  CA  . LEU   B 2 74  ? -31.345 9.763   -0.085  1.00 22.94  ? 190 LEU   B CA  1 
ATOM   2265 C  C   . LEU   B 2 74  ? -29.880 9.425   0.136   1.00 20.53  ? 190 LEU   B C   1 
ATOM   2266 O  O   . LEU   B 2 74  ? -29.259 8.608   -0.632  1.00 22.18  ? 190 LEU   B O   1 
ATOM   2267 C  CB  . LEU   B 2 74  ? -32.242 8.520   0.062   1.00 20.56  ? 190 LEU   B CB  1 
ATOM   2268 C  CG  . LEU   B 2 74  ? -32.158 7.765   1.380   1.00 23.03  ? 190 LEU   B CG  1 
ATOM   2269 C  CD1 . LEU   B 2 74  ? -32.598 8.612   2.576   1.00 23.95  ? 190 LEU   B CD1 1 
ATOM   2270 C  CD2 . LEU   B 2 74  ? -33.043 6.512   1.308   1.00 22.87  ? 190 LEU   B CD2 1 
ATOM   2271 N  N   . LEU   B 2 75  ? -29.300 10.049  1.144   1.00 22.95  ? 191 LEU   B N   1 
ATOM   2272 C  CA  . LEU   B 2 75  ? -27.844 9.999   1.388   1.00 23.67  ? 191 LEU   B CA  1 
ATOM   2273 C  C   . LEU   B 2 75  ? -27.649 9.420   2.783   1.00 24.80  ? 191 LEU   B C   1 
ATOM   2274 O  O   . LEU   B 2 75  ? -28.108 10.039  3.752   1.00 25.41  ? 191 LEU   B O   1 
ATOM   2275 C  CB  . LEU   B 2 75  ? -27.302 11.420  1.181   1.00 26.98  ? 191 LEU   B CB  1 
ATOM   2276 C  CG  . LEU   B 2 75  ? -25.803 11.635  1.249   1.00 29.32  ? 191 LEU   B CG  1 
ATOM   2277 C  CD1 . LEU   B 2 75  ? -25.008 10.611  0.456   1.00 30.31  ? 191 LEU   B CD1 1 
ATOM   2278 C  CD2 . LEU   B 2 75  ? -25.453 13.048  0.766   1.00 29.05  ? 191 LEU   B CD2 1 
ATOM   2279 N  N   . GLU   B 2 76  ? -26.992 8.259   2.849   1.00 22.75  ? 192 GLU   B N   1 
ATOM   2280 C  CA  . GLU   B 2 76  ? -26.835 7.423   4.058   1.00 24.18  ? 192 GLU   B CA  1 
ATOM   2281 C  C   . GLU   B 2 76  ? -25.371 7.110   4.286   1.00 27.33  ? 192 GLU   B C   1 
ATOM   2282 O  O   . GLU   B 2 76  ? -24.984 5.953   4.473   1.00 24.61  ? 192 GLU   B O   1 
ATOM   2283 C  CB  . GLU   B 2 76  ? -27.708 6.187   3.846   1.00 24.07  ? 192 GLU   B CB  1 
ATOM   2284 C  CG  . GLU   B 2 76  ? -27.814 5.319   5.073   1.00 24.51  ? 192 GLU   B CG  1 
ATOM   2285 C  CD  . GLU   B 2 76  ? -28.747 4.123   4.877   1.00 23.79  ? 192 GLU   B CD  1 
ATOM   2286 O  OE1 . GLU   B 2 76  ? -29.680 4.235   4.073   1.00 25.00  ? 192 GLU   B OE1 1 
ATOM   2287 O  OE2 . GLU   B 2 76  ? -28.561 3.184   5.615   1.00 26.80  ? 192 GLU   B OE2 1 
ATOM   2288 N  N   . PRO   B 2 77  ? -24.478 8.138   4.376   1.00 23.32  ? 193 PRO   B N   1 
ATOM   2289 C  CA  . PRO   B 2 77  ? -23.074 7.852   4.614   1.00 23.95  ? 193 PRO   B CA  1 
ATOM   2290 C  C   . PRO   B 2 77  ? -22.856 7.075   5.897   1.00 25.97  ? 193 PRO   B C   1 
ATOM   2291 O  O   . PRO   B 2 77  ? -23.463 7.363   6.923   1.00 24.88  ? 193 PRO   B O   1 
ATOM   2292 C  CB  . PRO   B 2 77  ? -22.417 9.237   4.693   1.00 24.95  ? 193 PRO   B CB  1 
ATOM   2293 C  CG  . PRO   B 2 77  ? -23.572 10.165  5.070   1.00 22.07  ? 193 PRO   B CG  1 
ATOM   2294 C  CD  . PRO   B 2 77  ? -24.769 9.597   4.319   1.00 23.93  ? 193 PRO   B CD  1 
ATOM   2295 N  N   . PRO   B 2 78  ? -21.923 6.098   5.906   1.00 28.92  ? 194 PRO   B N   1 
ATOM   2296 C  CA  . PRO   B 2 78  ? -21.693 5.281   7.100   1.00 29.48  ? 194 PRO   B CA  1 
ATOM   2297 C  C   . PRO   B 2 78  ? -20.885 6.062   8.148   1.00 28.68  ? 194 PRO   B C   1 
ATOM   2298 O  O   . PRO   B 2 78  ? -19.680 6.156   8.054   1.00 30.40  ? 194 PRO   B O   1 
ATOM   2299 C  CB  . PRO   B 2 78  ? -20.951 4.056   6.540   1.00 29.06  ? 194 PRO   B CB  1 
ATOM   2300 C  CG  . PRO   B 2 78  ? -20.190 4.614   5.338   1.00 31.50  ? 194 PRO   B CG  1 
ATOM   2301 C  CD  . PRO   B 2 78  ? -21.134 5.641   4.745   1.00 28.51  ? 194 PRO   B CD  1 
ATOM   2302 N  N   . LEU   B 2 79  ? -21.572 6.647   9.122   1.00 29.28  ? 195 LEU   B N   1 
ATOM   2303 C  CA  . LEU   B 2 79  ? -20.931 7.464   10.185  1.00 30.06  ? 195 LEU   B CA  1 
ATOM   2304 C  C   . LEU   B 2 79  ? -20.262 6.534   11.201  1.00 34.44  ? 195 LEU   B C   1 
ATOM   2305 O  O   . LEU   B 2 79  ? -20.857 5.464   11.516  1.00 32.99  ? 195 LEU   B O   1 
ATOM   2306 C  CB  . LEU   B 2 79  ? -22.009 8.277   10.889  1.00 30.27  ? 195 LEU   B CB  1 
ATOM   2307 C  CG  . LEU   B 2 79  ? -22.805 9.234   10.008  1.00 29.67  ? 195 LEU   B CG  1 
ATOM   2308 C  CD1 . LEU   B 2 79  ? -23.722 10.074  10.881  1.00 25.47  ? 195 LEU   B CD1 1 
ATOM   2309 C  CD2 . LEU   B 2 79  ? -21.873 10.112  9.178   1.00 31.50  ? 195 LEU   B CD2 1 
ATOM   2310 N  N   . GLU   B 2 80  ? -19.156 6.968   11.797  1.00 37.42  ? 196 GLU   B N   1 
ATOM   2311 C  CA  . GLU   B 2 80  ? -18.444 6.180   12.856  1.00 47.42  ? 196 GLU   B CA  1 
ATOM   2312 C  C   . GLU   B 2 80  ? -19.435 5.836   13.983  1.00 41.13  ? 196 GLU   B C   1 
ATOM   2313 O  O   . GLU   B 2 80  ? -19.390 4.693   14.496  1.00 41.60  ? 196 GLU   B O   1 
ATOM   2314 C  CB  . GLU   B 2 80  ? -17.217 6.948   13.364  1.00 53.48  ? 196 GLU   B CB  1 
ATOM   2315 C  CG  . GLU   B 2 80  ? -16.635 6.428   14.681  1.00 70.68  ? 196 GLU   B CG  1 
ATOM   2316 C  CD  . GLU   B 2 80  ? -17.128 7.088   15.977  1.00 82.63  ? 196 GLU   B CD  1 
ATOM   2317 O  OE1 . GLU   B 2 80  ? -17.699 8.213   15.921  1.00 85.28  ? 196 GLU   B OE1 1 
ATOM   2318 O  OE2 . GLU   B 2 80  ? -16.930 6.481   17.060  1.00 89.57  ? 196 GLU   B OE2 1 
ATOM   2319 N  N   . GLU   B 2 81  ? -20.333 6.763   14.336  1.00 34.54  ? 197 GLU   B N   1 
ATOM   2320 C  CA  . GLU   B 2 81  ? -21.250 6.579   15.489  1.00 35.27  ? 197 GLU   B CA  1 
ATOM   2321 C  C   . GLU   B 2 81  ? -22.188 5.386   15.252  1.00 37.11  ? 197 GLU   B C   1 
ATOM   2322 O  O   . GLU   B 2 81  ? -22.706 4.856   16.239  1.00 35.77  ? 197 GLU   B O   1 
ATOM   2323 C  CB  . GLU   B 2 81  ? -22.022 7.858   15.819  1.00 37.44  ? 197 GLU   B CB  1 
ATOM   2324 C  CG  . GLU   B 2 81  ? -23.102 8.248   14.820  1.00 37.10  ? 197 GLU   B CG  1 
ATOM   2325 C  CD  . GLU   B 2 81  ? -23.595 9.683   14.987  1.00 35.57  ? 197 GLU   B CD  1 
ATOM   2326 O  OE1 . GLU   B 2 81  ? -22.805 10.634  14.709  1.00 37.03  ? 197 GLU   B OE1 1 
ATOM   2327 O  OE2 . GLU   B 2 81  ? -24.728 9.846   15.423  1.00 33.89  ? 197 GLU   B OE2 1 
ATOM   2328 N  N   . TYR   B 2 82  ? -22.418 4.960   14.015  1.00 35.10  ? 198 TYR   B N   1 
ATOM   2329 C  CA  . TYR   B 2 82  ? -23.319 3.800   13.758  1.00 37.93  ? 198 TYR   B CA  1 
ATOM   2330 C  C   . TYR   B 2 82  ? -22.644 2.502   14.249  1.00 42.97  ? 198 TYR   B C   1 
ATOM   2331 O  O   . TYR   B 2 82  ? -23.370 1.534   14.502  1.00 43.73  ? 198 TYR   B O   1 
ATOM   2332 C  CB  . TYR   B 2 82  ? -23.682 3.688   12.279  1.00 35.91  ? 198 TYR   B CB  1 
ATOM   2333 C  CG  . TYR   B 2 82  ? -24.377 4.882   11.679  1.00 33.62  ? 198 TYR   B CG  1 
ATOM   2334 C  CD1 . TYR   B 2 82  ? -25.032 5.823   12.469  1.00 33.74  ? 198 TYR   B CD1 1 
ATOM   2335 C  CD2 . TYR   B 2 82  ? -24.413 5.034   10.303  1.00 30.66  ? 198 TYR   B CD2 1 
ATOM   2336 C  CE1 . TYR   B 2 82  ? -25.678 6.901   11.896  1.00 30.68  ? 198 TYR   B CE1 1 
ATOM   2337 C  CE2 . TYR   B 2 82  ? -25.096 6.081   9.717   1.00 32.70  ? 198 TYR   B CE2 1 
ATOM   2338 C  CZ  . TYR   B 2 82  ? -25.712 7.026   10.517  1.00 28.92  ? 198 TYR   B CZ  1 
ATOM   2339 O  OH  . TYR   B 2 82  ? -26.356 8.071   9.938   1.00 30.05  ? 198 TYR   B OH  1 
ATOM   2340 N  N   . TYR   B 2 83  ? -21.309 2.489   14.314  1.00 47.76  ? 199 TYR   B N   1 
ATOM   2341 C  CA  . TYR   B 2 83  ? -20.443 1.327   14.654  1.00 57.25  ? 199 TYR   B CA  1 
ATOM   2342 C  C   . TYR   B 2 83  ? -19.706 1.626   15.961  1.00 67.43  ? 199 TYR   B C   1 
ATOM   2343 O  O   . TYR   B 2 83  ? -18.624 2.242   15.924  1.00 80.97  ? 199 TYR   B O   1 
ATOM   2344 C  CB  . TYR   B 2 83  ? -19.441 1.063   13.525  1.00 49.60  ? 199 TYR   B CB  1 
ATOM   2345 C  CG  . TYR   B 2 83  ? -20.052 0.986   12.149  1.00 48.82  ? 199 TYR   B CG  1 
ATOM   2346 C  CD1 . TYR   B 2 83  ? -20.345 2.132   11.429  1.00 48.87  ? 199 TYR   B CD1 1 
ATOM   2347 C  CD2 . TYR   B 2 83  ? -20.329 -0.236  11.558  1.00 46.08  ? 199 TYR   B CD2 1 
ATOM   2348 C  CE1 . TYR   B 2 83  ? -20.920 2.066   10.167  1.00 52.25  ? 199 TYR   B CE1 1 
ATOM   2349 C  CE2 . TYR   B 2 83  ? -20.872 -0.321  10.286  1.00 47.29  ? 199 TYR   B CE2 1 
ATOM   2350 C  CZ  . TYR   B 2 83  ? -21.182 0.835   9.593   1.00 52.97  ? 199 TYR   B CZ  1 
ATOM   2351 O  OH  . TYR   B 2 83  ? -21.760 0.750   8.360   1.00 52.61  ? 199 TYR   B OH  1 
ATOM   2352 N  N   . ARG   B 2 84  ? -20.288 1.248   17.094  1.00 77.94  ? 200 ARG   B N   1 
ATOM   2353 C  CA  . ARG   B 2 84  ? -19.706 1.550   18.427  1.00 87.65  ? 200 ARG   B CA  1 
ATOM   2354 C  C   . ARG   B 2 84  ? -20.099 0.436   19.400  1.00 94.86  ? 200 ARG   B C   1 
ATOM   2355 O  O   . ARG   B 2 84  ? -20.684 0.753   20.453  1.00 103.49 ? 200 ARG   B O   1 
ATOM   2356 C  CB  . ARG   B 2 84  ? -20.167 2.939   18.889  1.00 91.52  ? 200 ARG   B CB  1 
ATOM   2357 C  CG  . ARG   B 2 84  ? -19.224 4.078   18.525  1.00 92.17  ? 200 ARG   B CG  1 
ATOM   2358 C  CD  . ARG   B 2 84  ? -19.667 5.375   19.183  1.00 96.83  ? 200 ARG   B CD  1 
ATOM   2359 N  NE  . ARG   B 2 84  ? -19.557 5.338   20.642  1.00 101.61 ? 200 ARG   B NE  1 
ATOM   2360 C  CZ  . ARG   B 2 84  ? -20.200 6.142   21.498  1.00 93.55  ? 200 ARG   B CZ  1 
ATOM   2361 N  NH1 . ARG   B 2 84  ? -20.005 6.006   22.798  1.00 87.37  ? 200 ARG   B NH1 1 
ATOM   2362 N  NH2 . ARG   B 2 84  ? -21.033 7.074   21.065  1.00 92.71  ? 200 ARG   B NH2 1 
ATOM   2363 N  N   . GLU   B 2 85  ? -19.773 -0.816  19.054  1.00 105.05 ? 201 GLU   B N   1 
ATOM   2364 C  CA  . GLU   B 2 85  ? -20.078 -2.027  19.868  1.00 105.50 ? 201 GLU   B CA  1 
ATOM   2365 C  C   . GLU   B 2 85  ? -19.247 -3.215  19.363  1.00 94.87  ? 201 GLU   B C   1 
ATOM   2366 O  O   . GLU   B 2 85  ? -19.089 -3.310  18.134  1.00 88.69  ? 201 GLU   B O   1 
ATOM   2367 C  CB  . GLU   B 2 85  ? -21.580 -2.320  19.814  1.00 115.02 ? 201 GLU   B CB  1 
ATOM   2368 C  CG  . GLU   B 2 85  ? -22.394 -1.588  20.877  1.00 120.58 ? 201 GLU   B CG  1 
ATOM   2369 C  CD  . GLU   B 2 85  ? -23.709 -0.978  20.411  1.00 119.46 ? 201 GLU   B CD  1 
ATOM   2370 O  OE1 . GLU   B 2 85  ? -24.382 -1.594  19.564  1.00 123.79 ? 201 GLU   B OE1 1 
ATOM   2371 O  OE2 . GLU   B 2 85  ? -24.058 0.119   20.897  1.00 118.54 ? 201 GLU   B OE2 1 
ATOM   2372 N  N   . GLU   B 2 92  ? -12.303 2.660   9.336   1.00 105.68 ? 208 GLU   B N   1 
ATOM   2373 C  CA  . GLU   B 2 92  ? -11.652 2.531   8.003   1.00 102.45 ? 208 GLU   B CA  1 
ATOM   2374 C  C   . GLU   B 2 92  ? -12.632 2.995   6.917   1.00 93.07  ? 208 GLU   B C   1 
ATOM   2375 O  O   . GLU   B 2 92  ? -12.414 4.092   6.350   1.00 93.06  ? 208 GLU   B O   1 
ATOM   2376 C  CB  . GLU   B 2 92  ? -11.206 1.084   7.759   1.00 110.02 ? 208 GLU   B CB  1 
ATOM   2377 C  CG  . GLU   B 2 92  ? -10.053 0.634   8.641   1.00 113.41 ? 208 GLU   B CG  1 
ATOM   2378 C  CD  . GLU   B 2 92  ? -8.684  1.152   8.228   1.00 115.62 ? 208 GLU   B CD  1 
ATOM   2379 O  OE1 . GLU   B 2 92  ? -8.626  2.138   7.463   1.00 115.97 ? 208 GLU   B OE1 1 
ATOM   2380 O  OE2 . GLU   B 2 92  ? -7.677  0.565   8.670   1.00 115.82 ? 208 GLU   B OE2 1 
ATOM   2381 N  N   . LYS   B 2 93  ? -13.690 2.205   6.689   1.00 71.18  ? 209 LYS   B N   1 
ATOM   2382 C  CA  . LYS   B 2 93  ? -14.727 2.420   5.647   1.00 56.12  ? 209 LYS   B CA  1 
ATOM   2383 C  C   . LYS   B 2 93  ? -15.762 3.453   6.132   1.00 39.79  ? 209 LYS   B C   1 
ATOM   2384 O  O   . LYS   B 2 93  ? -16.729 3.651   5.416   1.00 41.72  ? 209 LYS   B O   1 
ATOM   2385 C  CB  . LYS   B 2 93  ? -15.452 1.105   5.332   1.00 62.26  ? 209 LYS   B CB  1 
ATOM   2386 C  CG  . LYS   B 2 93  ? -14.716 -0.172  5.717   1.00 74.84  ? 209 LYS   B CG  1 
ATOM   2387 C  CD  . LYS   B 2 93  ? -15.301 -1.440  5.115   1.00 79.17  ? 209 LYS   B CD  1 
ATOM   2388 C  CE  . LYS   B 2 93  ? -14.291 -2.567  5.049   1.00 81.55  ? 209 LYS   B CE  1 
ATOM   2389 N  NZ  . LYS   B 2 93  ? -13.571 -2.736  6.336   1.00 85.80  ? 209 LYS   B NZ  1 
ATOM   2390 N  N   . CYS   B 2 94  ? -15.638 3.995   7.340   1.00 35.36  ? 210 CYS   B N   1 
ATOM   2391 C  CA  . CYS   B 2 94  ? -16.575 5.031   7.863   1.00 37.90  ? 210 CYS   B CA  1 
ATOM   2392 C  C   . CYS   B 2 94  ? -16.271 6.392   7.199   1.00 36.10  ? 210 CYS   B C   1 
ATOM   2393 O  O   . CYS   B 2 94  ? -15.142 6.629   6.768   1.00 34.26  ? 210 CYS   B O   1 
ATOM   2394 C  CB  . CYS   B 2 94  ? -16.555 5.099   9.381   1.00 39.97  ? 210 CYS   B CB  1 
ATOM   2395 S  SG  . CYS   B 2 94  ? -17.493 3.740   10.138  1.00 47.69  ? 210 CYS   B SG  1 
ATOM   2396 N  N   . TRP   B 2 95  ? -17.291 7.213   7.014   1.00 28.89  ? 211 TRP   B N   1 
ATOM   2397 C  CA  . TRP   B 2 95  ? -17.180 8.535   6.354   1.00 28.58  ? 211 TRP   B CA  1 
ATOM   2398 C  C   . TRP   B 2 95  ? -17.234 9.600   7.447   1.00 30.49  ? 211 TRP   B C   1 
ATOM   2399 O  O   . TRP   B 2 95  ? -18.133 9.529   8.270   1.00 28.40  ? 211 TRP   B O   1 
ATOM   2400 C  CB  . TRP   B 2 95  ? -18.294 8.699   5.323   1.00 28.23  ? 211 TRP   B CB  1 
ATOM   2401 C  CG  . TRP   B 2 95  ? -17.959 8.017   4.035   1.00 30.48  ? 211 TRP   B CG  1 
ATOM   2402 C  CD1 . TRP   B 2 95  ? -17.680 6.694   3.815   1.00 32.65  ? 211 TRP   B CD1 1 
ATOM   2403 C  CD2 . TRP   B 2 95  ? -17.826 8.675   2.779   1.00 29.44  ? 211 TRP   B CD2 1 
ATOM   2404 N  NE1 . TRP   B 2 95  ? -17.372 6.496   2.497   1.00 31.74  ? 211 TRP   B NE1 1 
ATOM   2405 C  CE2 . TRP   B 2 95  ? -17.474 7.691   1.834   1.00 28.84  ? 211 TRP   B CE2 1 
ATOM   2406 C  CE3 . TRP   B 2 95  ? -17.975 10.009  2.369   1.00 28.32  ? 211 TRP   B CE3 1 
ATOM   2407 C  CZ2 . TRP   B 2 95  ? -17.235 8.013   0.501   1.00 30.56  ? 211 TRP   B CZ2 1 
ATOM   2408 C  CZ3 . TRP   B 2 95  ? -17.714 10.320  1.049   1.00 28.86  ? 211 TRP   B CZ3 1 
ATOM   2409 C  CH2 . TRP   B 2 95  ? -17.374 9.335   0.128   1.00 27.58  ? 211 TRP   B CH2 1 
ATOM   2410 N  N   . THR   B 2 96  ? -16.316 10.558  7.432   1.00 29.00  ? 212 THR   B N   1 
ATOM   2411 C  CA  . THR   B 2 96  ? -16.377 11.752  8.315   1.00 27.25  ? 212 THR   B CA  1 
ATOM   2412 C  C   . THR   B 2 96  ? -17.240 12.809  7.637   1.00 24.90  ? 212 THR   B C   1 
ATOM   2413 O  O   . THR   B 2 96  ? -17.455 12.755  6.397   1.00 24.73  ? 212 THR   B O   1 
ATOM   2414 C  CB  . THR   B 2 96  ? -14.979 12.291  8.621   1.00 30.41  ? 212 THR   B CB  1 
ATOM   2415 O  OG1 . THR   B 2 96  ? -14.457 12.810  7.386   1.00 27.41  ? 212 THR   B OG1 1 
ATOM   2416 C  CG2 . THR   B 2 96  ? -14.055 11.236  9.204   1.00 32.65  ? 212 THR   B CG2 1 
ATOM   2417 N  N   . TRP   B 2 97  ? -17.622 13.810  8.403   1.00 24.16  ? 213 TRP   B N   1 
ATOM   2418 C  CA  . TRP   B 2 97  ? -18.314 14.991  7.849   1.00 25.90  ? 213 TRP   B CA  1 
ATOM   2419 C  C   . TRP   B 2 97  ? -17.398 15.756  6.882   1.00 25.58  ? 213 TRP   B C   1 
ATOM   2420 O  O   . TRP   B 2 97  ? -17.944 16.261  5.893   1.00 27.44  ? 213 TRP   B O   1 
ATOM   2421 C  CB  . TRP   B 2 97  ? -18.921 15.806  8.996   1.00 24.64  ? 213 TRP   B CB  1 
ATOM   2422 C  CG  . TRP   B 2 97  ? -20.113 15.074  9.519   1.00 23.81  ? 213 TRP   B CG  1 
ATOM   2423 C  CD1 . TRP   B 2 97  ? -20.196 14.329  10.656  1.00 25.25  ? 213 TRP   B CD1 1 
ATOM   2424 C  CD2 . TRP   B 2 97  ? -21.352 14.894  8.826   1.00 23.52  ? 213 TRP   B CD2 1 
ATOM   2425 N  NE1 . TRP   B 2 97  ? -21.437 13.755  10.746  1.00 25.02  ? 213 TRP   B NE1 1 
ATOM   2426 C  CE2 . TRP   B 2 97  ? -22.163 14.077  9.635   1.00 24.46  ? 213 TRP   B CE2 1 
ATOM   2427 C  CE3 . TRP   B 2 97  ? -21.888 15.392  7.633   1.00 25.74  ? 213 TRP   B CE3 1 
ATOM   2428 C  CZ2 . TRP   B 2 97  ? -23.460 13.725  9.268   1.00 25.73  ? 213 TRP   B CZ2 1 
ATOM   2429 C  CZ3 . TRP   B 2 97  ? -23.169 15.031  7.269   1.00 28.00  ? 213 TRP   B CZ3 1 
ATOM   2430 C  CH2 . TRP   B 2 97  ? -23.955 14.221  8.087   1.00 27.90  ? 213 TRP   B CH2 1 
ATOM   2431 N  N   . ASP   B 2 98  ? -16.077 15.732  7.071   1.00 25.65  ? 214 ASP   B N   1 
ATOM   2432 C  CA  . ASP   B 2 98  ? -15.094 16.289  6.091   1.00 26.29  ? 214 ASP   B CA  1 
ATOM   2433 C  C   . ASP   B 2 98  ? -15.331 15.619  4.733   1.00 25.28  ? 214 ASP   B C   1 
ATOM   2434 O  O   . ASP   B 2 98  ? -15.436 16.304  3.721   1.00 24.48  ? 214 ASP   B O   1 
ATOM   2435 C  CB  . ASP   B 2 98  ? -13.647 16.124  6.593   1.00 29.55  ? 214 ASP   B CB  1 
ATOM   2436 C  CG  . ASP   B 2 98  ? -12.558 16.983  5.918   1.00 40.55  ? 214 ASP   B CG  1 
ATOM   2437 O  OD1 . ASP   B 2 98  ? -12.244 16.702  4.744   1.00 38.83  ? 214 ASP   B OD1 1 
ATOM   2438 O  OD2 . ASP   B 2 98  ? -11.948 17.905  6.608   1.00 41.29  ? 214 ASP   B OD2 1 
ATOM   2439 N  N   . ASP   B 2 99  ? -15.388 14.282  4.724   1.00 24.75  ? 215 ASP   B N   1 
ATOM   2440 C  CA  . ASP   B 2 99  ? -15.530 13.442  3.518   1.00 26.03  ? 215 ASP   B CA  1 
ATOM   2441 C  C   . ASP   B 2 99  ? -16.896 13.730  2.904   1.00 25.86  ? 215 ASP   B C   1 
ATOM   2442 O  O   . ASP   B 2 99  ? -16.992 13.964  1.695   1.00 27.09  ? 215 ASP   B O   1 
ATOM   2443 C  CB  . ASP   B 2 99  ? -15.475 11.944  3.848   1.00 28.59  ? 215 ASP   B CB  1 
ATOM   2444 C  CG  . ASP   B 2 99  ? -14.194 11.402  4.446   1.00 34.47  ? 215 ASP   B CG  1 
ATOM   2445 O  OD1 . ASP   B 2 99  ? -13.133 11.931  4.092   1.00 30.13  ? 215 ASP   B OD1 1 
ATOM   2446 O  OD2 . ASP   B 2 99  ? -14.284 10.427  5.268   1.00 30.23  ? 215 ASP   B OD2 1 
ATOM   2447 N  N   . ILE   B 2 100 ? -17.930 13.799  3.731   1.00 22.42  ? 216 ILE   B N   1 
ATOM   2448 C  CA  . ILE   B 2 100 ? -19.311 13.919  3.209   1.00 24.30  ? 216 ILE   B CA  1 
ATOM   2449 C  C   . ILE   B 2 100 ? -19.485 15.305  2.564   1.00 24.17  ? 216 ILE   B C   1 
ATOM   2450 O  O   . ILE   B 2 100 ? -20.027 15.390  1.468   1.00 22.82  ? 216 ILE   B O   1 
ATOM   2451 C  CB  . ILE   B 2 100 ? -20.339 13.667  4.322   1.00 23.84  ? 216 ILE   B CB  1 
ATOM   2452 C  CG1 . ILE   B 2 100 ? -20.264 12.230  4.850   1.00 23.59  ? 216 ILE   B CG1 1 
ATOM   2453 C  CG2 . ILE   B 2 100 ? -21.730 14.035  3.822   1.00 24.22  ? 216 ILE   B CG2 1 
ATOM   2454 C  CD1 . ILE   B 2 100 ? -20.881 12.030  6.215   1.00 23.81  ? 216 ILE   B CD1 1 
ATOM   2455 N  N   . MET   B 2 101 ? -19.036 16.350  3.242   1.00 25.18  ? 217 MET   B N   1 
ATOM   2456 C  CA  . MET   B 2 101 ? -19.236 17.753  2.796   1.00 28.79  ? 217 MET   B CA  1 
ATOM   2457 C  C   . MET   B 2 101 ? -18.547 17.954  1.443   1.00 30.16  ? 217 MET   B C   1 
ATOM   2458 O  O   . MET   B 2 101 ? -19.001 18.796  0.662   1.00 31.12  ? 217 MET   B O   1 
ATOM   2459 C  CB  . MET   B 2 101 ? -18.666 18.685  3.867   1.00 29.61  ? 217 MET   B CB  1 
ATOM   2460 C  CG  . MET   B 2 101 ? -19.084 20.118  3.728   1.00 40.27  ? 217 MET   B CG  1 
ATOM   2461 S  SD  . MET   B 2 101 ? -18.493 21.121  5.125   1.00 37.92  ? 217 MET   B SD  1 
ATOM   2462 C  CE  . MET   B 2 101 ? -19.351 20.356  6.501   1.00 45.94  ? 217 MET   B CE  1 
ATOM   2463 N  N   . LYS   B 2 102 ? -17.561 17.122  1.098   1.00 32.39  ? 218 LYS   B N   1 
ATOM   2464 C  CA  . LYS   B 2 102 ? -16.768 17.260  -0.157  1.00 31.19  ? 218 LYS   B CA  1 
ATOM   2465 C  C   . LYS   B 2 102 ? -17.442 16.523  -1.313  1.00 33.46  ? 218 LYS   B C   1 
ATOM   2466 O  O   . LYS   B 2 102 ? -16.993 16.702  -2.463  1.00 32.43  ? 218 LYS   B O   1 
ATOM   2467 C  CB  . LYS   B 2 102 ? -15.299 16.928  0.153   1.00 34.99  ? 218 LYS   B CB  1 
ATOM   2468 C  CG  . LYS   B 2 102 ? -14.650 17.998  1.036   1.00 38.46  ? 218 LYS   B CG  1 
ATOM   2469 C  CD  . LYS   B 2 102 ? -13.223 17.770  1.587   1.00 42.18  ? 218 LYS   B CD  1 
ATOM   2470 C  CE  . LYS   B 2 102 ? -12.791 18.915  2.502   1.00 40.39  ? 218 LYS   B CE  1 
ATOM   2471 N  NZ  . LYS   B 2 102 ? -11.445 18.731  3.107   1.00 37.08  ? 218 LYS   B NZ  1 
ATOM   2472 N  N   . LEU   B 2 103 ? -18.579 15.832  -1.090  1.00 29.10  ? 219 LEU   B N   1 
ATOM   2473 C  CA  . LEU   B 2 103 ? -19.313 15.162  -2.179  1.00 30.10  ? 219 LEU   B CA  1 
ATOM   2474 C  C   . LEU   B 2 103 ? -19.946 16.227  -3.066  1.00 31.61  ? 219 LEU   B C   1 
ATOM   2475 O  O   . LEU   B 2 103 ? -20.425 17.200  -2.556  1.00 29.67  ? 219 LEU   B O   1 
ATOM   2476 C  CB  . LEU   B 2 103 ? -20.421 14.262  -1.625  1.00 30.70  ? 219 LEU   B CB  1 
ATOM   2477 C  CG  . LEU   B 2 103 ? -19.954 12.997  -0.929  1.00 32.03  ? 219 LEU   B CG  1 
ATOM   2478 C  CD1 . LEU   B 2 103 ? -21.128 12.264  -0.298  1.00 31.88  ? 219 LEU   B CD1 1 
ATOM   2479 C  CD2 . LEU   B 2 103 ? -19.246 12.078  -1.906  1.00 34.21  ? 219 LEU   B CD2 1 
ATOM   2480 N  N   . GLU   B 2 104 ? -19.993 15.968  -4.359  1.00 31.76  ? 220 GLU   B N   1 
ATOM   2481 C  CA  . GLU   B 2 104 ? -20.406 16.962  -5.385  1.00 38.71  ? 220 GLU   B CA  1 
ATOM   2482 C  C   . GLU   B 2 104 ? -21.904 16.794  -5.652  1.00 27.99  ? 220 GLU   B C   1 
ATOM   2483 O  O   . GLU   B 2 104 ? -22.289 16.603  -6.817  1.00 29.78  ? 220 GLU   B O   1 
ATOM   2484 C  CB  . GLU   B 2 104 ? -19.557 16.728  -6.640  1.00 43.81  ? 220 GLU   B CB  1 
ATOM   2485 C  CG  . GLU   B 2 104 ? -18.080 17.008  -6.405  1.00 52.87  ? 220 GLU   B CG  1 
ATOM   2486 C  CD  . GLU   B 2 104 ? -17.692 18.473  -6.539  1.00 63.03  ? 220 GLU   B CD  1 
ATOM   2487 O  OE1 . GLU   B 2 104 ? -18.614 19.317  -6.705  1.00 76.40  ? 220 GLU   B OE1 1 
ATOM   2488 O  OE2 . GLU   B 2 104 ? -16.468 18.780  -6.484  1.00 67.13  ? 220 GLU   B OE2 1 
ATOM   2489 N  N   . ILE   B 2 105 ? -22.722 16.860  -4.594  1.00 30.39  ? 221 ILE   B N   1 
ATOM   2490 C  CA  . ILE   B 2 105 ? -24.174 16.527  -4.692  1.00 27.25  ? 221 ILE   B CA  1 
ATOM   2491 C  C   . ILE   B 2 105 ? -24.863 17.507  -5.639  1.00 28.68  ? 221 ILE   B C   1 
ATOM   2492 O  O   . ILE   B 2 105 ? -25.671 17.093  -6.453  1.00 26.60  ? 221 ILE   B O   1 
ATOM   2493 C  CB  . ILE   B 2 105 ? -24.813 16.466  -3.295  1.00 27.14  ? 221 ILE   B CB  1 
ATOM   2494 C  CG1 . ILE   B 2 105 ? -24.141 15.409  -2.428  1.00 27.60  ? 221 ILE   B CG1 1 
ATOM   2495 C  CG2 . ILE   B 2 105 ? -26.333 16.286  -3.398  1.00 27.26  ? 221 ILE   B CG2 1 
ATOM   2496 C  CD1 . ILE   B 2 105 ? -24.218 14.002  -2.979  1.00 30.43  ? 221 ILE   B CD1 1 
ATOM   2497 N  N   . ASP   B 2 106 ? -24.473 18.781  -5.602  1.00 28.46  ? 222 ASP   B N   1 
ATOM   2498 C  CA  . ASP   B 2 106 ? -25.055 19.829  -6.467  1.00 29.06  ? 222 ASP   B CA  1 
ATOM   2499 C  C   . ASP   B 2 106 ? -24.894 19.444  -7.946  1.00 27.26  ? 222 ASP   B C   1 
ATOM   2500 O  O   . ASP   B 2 106 ? -25.684 19.919  -8.762  1.00 28.20  ? 222 ASP   B O   1 
ATOM   2501 C  CB  . ASP   B 2 106 ? -24.391 21.158  -6.131  1.00 32.94  ? 222 ASP   B CB  1 
ATOM   2502 C  CG  . ASP   B 2 106 ? -22.876 21.081  -6.087  1.00 39.50  ? 222 ASP   B CG  1 
ATOM   2503 O  OD1 . ASP   B 2 106 ? -22.309 20.417  -5.145  1.00 37.79  ? 222 ASP   B OD1 1 
ATOM   2504 O  OD2 . ASP   B 2 106 ? -22.253 21.682  -6.993  1.00 50.71  ? 222 ASP   B OD2 1 
ATOM   2505 N  N   . GLU   B 2 107 ? -23.910 18.621  -8.305  1.00 27.49  ? 223 GLU   B N   1 
ATOM   2506 C  CA  . GLU   B 2 107 ? -23.605 18.292  -9.727  1.00 30.72  ? 223 GLU   B CA  1 
ATOM   2507 C  C   . GLU   B 2 107 ? -24.613 17.264  -10.250 1.00 33.20  ? 223 GLU   B C   1 
ATOM   2508 O  O   . GLU   B 2 107 ? -24.721 17.130  -11.490 1.00 33.82  ? 223 GLU   B O   1 
ATOM   2509 C  CB  . GLU   B 2 107 ? -22.174 17.800  -9.898  1.00 34.71  ? 223 GLU   B CB  1 
ATOM   2510 C  CG  . GLU   B 2 107 ? -21.127 18.827  -9.470  1.00 46.64  ? 223 GLU   B CG  1 
ATOM   2511 C  CD  . GLU   B 2 107 ? -21.012 20.024  -10.403 1.00 56.92  ? 223 GLU   B CD  1 
ATOM   2512 O  OE1 . GLU   B 2 107 ? -21.030 19.779  -11.620 1.00 61.36  ? 223 GLU   B OE1 1 
ATOM   2513 O  OE2 . GLU   B 2 107 ? -20.938 21.200  -9.914  1.00 63.08  ? 223 GLU   B OE2 1 
ATOM   2514 N  N   . ILE   B 2 108 ? -25.359 16.572  -9.380  1.00 29.54  ? 224 ILE   B N   1 
ATOM   2515 C  CA  . ILE   B 2 108 ? -26.280 15.503  -9.856  1.00 28.76  ? 224 ILE   B CA  1 
ATOM   2516 C  C   . ILE   B 2 108 ? -27.723 15.807  -9.443  1.00 29.85  ? 224 ILE   B C   1 
ATOM   2517 O  O   . ILE   B 2 108 ? -28.613 15.081  -9.880  1.00 32.18  ? 224 ILE   B O   1 
ATOM   2518 C  CB  . ILE   B 2 108 ? -25.798 14.125  -9.378  1.00 30.52  ? 224 ILE   B CB  1 
ATOM   2519 C  CG1 . ILE   B 2 108 ? -25.697 14.041  -7.856  1.00 30.19  ? 224 ILE   B CG1 1 
ATOM   2520 C  CG2 . ILE   B 2 108 ? -24.479 13.772  -10.038 1.00 31.67  ? 224 ILE   B CG2 1 
ATOM   2521 C  CD1 . ILE   B 2 108 ? -25.750 12.577  -7.329  1.00 33.00  ? 224 ILE   B CD1 1 
ATOM   2522 N  N   . ALA   B 2 109 ? -27.975 16.833  -8.641  1.00 26.60  ? 225 ALA   B N   1 
ATOM   2523 C  CA  . ALA   B 2 109 ? -29.335 17.213  -8.208  1.00 28.63  ? 225 ALA   B CA  1 
ATOM   2524 C  C   . ALA   B 2 109 ? -30.031 18.023  -9.306  1.00 32.84  ? 225 ALA   B C   1 
ATOM   2525 O  O   . ALA   B 2 109 ? -29.414 18.931  -9.872  1.00 33.55  ? 225 ALA   B O   1 
ATOM   2526 C  CB  . ALA   B 2 109 ? -29.291 17.989  -6.916  1.00 27.47  ? 225 ALA   B CB  1 
ATOM   2527 N  N   . ALA   B 2 110 ? -31.286 17.717  -9.598  1.00 28.29  ? 226 ALA   B N   1 
ATOM   2528 C  CA  . ALA   B 2 110 ? -32.107 18.531  -10.515 1.00 29.54  ? 226 ALA   B CA  1 
ATOM   2529 C  C   . ALA   B 2 110 ? -32.289 19.912  -9.890  1.00 33.33  ? 226 ALA   B C   1 
ATOM   2530 O  O   . ALA   B 2 110 ? -32.267 20.044  -8.667  1.00 32.97  ? 226 ALA   B O   1 
ATOM   2531 C  CB  . ALA   B 2 110 ? -33.437 17.855  -10.772 1.00 30.53  ? 226 ALA   B CB  1 
ATOM   2532 N  N   . PRO   B 2 111 ? -32.444 20.988  -10.700 1.00 37.05  ? 227 PRO   B N   1 
ATOM   2533 C  CA  . PRO   B 2 111 ? -32.578 22.352  -10.169 1.00 35.17  ? 227 PRO   B CA  1 
ATOM   2534 C  C   . PRO   B 2 111 ? -33.772 22.495  -9.218  1.00 33.15  ? 227 PRO   B C   1 
ATOM   2535 O  O   . PRO   B 2 111 ? -33.708 23.312  -8.359  1.00 35.24  ? 227 PRO   B O   1 
ATOM   2536 C  CB  . PRO   B 2 111 ? -32.793 23.224  -11.423 1.00 38.86  ? 227 PRO   B CB  1 
ATOM   2537 C  CG  . PRO   B 2 111 ? -32.168 22.410  -12.551 1.00 42.85  ? 227 PRO   B CG  1 
ATOM   2538 C  CD  . PRO   B 2 111 ? -32.382 20.958  -12.164 1.00 39.85  ? 227 PRO   B CD  1 
ATOM   2539 N  N   . ARG   B 2 112 ? -34.853 21.742  -9.442  1.00 35.98  ? 228 ARG   B N   1 
ATOM   2540 C  CA  . ARG   B 2 112 ? -35.921 21.528  -8.438  1.00 36.36  ? 228 ARG   B CA  1 
ATOM   2541 C  C   . ARG   B 2 112 ? -35.773 20.094  -7.960  1.00 37.59  ? 228 ARG   B C   1 
ATOM   2542 O  O   . ARG   B 2 112 ? -35.977 19.189  -8.785  1.00 35.18  ? 228 ARG   B O   1 
ATOM   2543 C  CB  . ARG   B 2 112 ? -37.343 21.734  -8.960  1.00 47.11  ? 228 ARG   B CB  1 
ATOM   2544 C  CG  . ARG   B 2 112 ? -37.575 23.071  -9.649  1.00 62.99  ? 228 ARG   B CG  1 
ATOM   2545 C  CD  . ARG   B 2 112 ? -37.104 24.231  -8.797  1.00 74.95  ? 228 ARG   B CD  1 
ATOM   2546 N  NE  . ARG   B 2 112 ? -37.353 25.571  -9.336  1.00 86.86  ? 228 ARG   B NE  1 
ATOM   2547 C  CZ  . ARG   B 2 112 ? -36.424 26.433  -9.766  1.00 93.87  ? 228 ARG   B CZ  1 
ATOM   2548 N  NH1 . ARG   B 2 112 ? -35.134 26.129  -9.749  1.00 92.09  ? 228 ARG   B NH1 1 
ATOM   2549 N  NH2 . ARG   B 2 112 ? -36.803 27.616  -10.221 1.00 96.33  ? 228 ARG   B NH2 1 
ATOM   2550 N  N   . SER   B 2 113 ? -35.396 19.903  -6.701  1.00 30.85  ? 229 SER   B N   1 
ATOM   2551 C  CA  . SER   B 2 113 ? -35.168 18.541  -6.153  1.00 32.03  ? 229 SER   B CA  1 
ATOM   2552 C  C   . SER   B 2 113 ? -35.068 18.571  -4.639  1.00 29.85  ? 229 SER   B C   1 
ATOM   2553 O  O   . SER   B 2 113 ? -35.039 19.686  -4.033  1.00 26.60  ? 229 SER   B O   1 
ATOM   2554 C  CB  . SER   B 2 113 ? -33.958 17.909  -6.789  1.00 31.88  ? 229 SER   B CB  1 
ATOM   2555 O  OG  . SER   B 2 113 ? -32.759 18.557  -6.426  1.00 30.16  ? 229 SER   B OG  1 
ATOM   2556 N  N   . PHE   B 2 114 ? -34.984 17.365  -4.066  1.00 28.14  ? 230 PHE   B N   1 
ATOM   2557 C  CA  . PHE   B 2 114 ? -35.056 17.101  -2.618  1.00 27.19  ? 230 PHE   B CA  1 
ATOM   2558 C  C   . PHE   B 2 114 ? -33.885 16.217  -2.228  1.00 24.36  ? 230 PHE   B C   1 
ATOM   2559 O  O   . PHE   B 2 114 ? -33.421 15.384  -3.010  1.00 26.46  ? 230 PHE   B O   1 
ATOM   2560 C  CB  . PHE   B 2 114 ? -36.389 16.470  -2.240  1.00 29.59  ? 230 PHE   B CB  1 
ATOM   2561 C  CG  . PHE   B 2 114 ? -37.505 17.390  -2.643  1.00 32.72  ? 230 PHE   B CG  1 
ATOM   2562 C  CD1 . PHE   B 2 114 ? -37.880 17.486  -3.980  1.00 35.93  ? 230 PHE   B CD1 1 
ATOM   2563 C  CD2 . PHE   B 2 114 ? -38.103 18.219  -1.713  1.00 33.72  ? 230 PHE   B CD2 1 
ATOM   2564 C  CE1 . PHE   B 2 114 ? -38.863 18.377  -4.373  1.00 34.34  ? 230 PHE   B CE1 1 
ATOM   2565 C  CE2 . PHE   B 2 114 ? -39.091 19.102  -2.105  1.00 35.98  ? 230 PHE   B CE2 1 
ATOM   2566 C  CZ  . PHE   B 2 114 ? -39.462 19.186  -3.435  1.00 35.31  ? 230 PHE   B CZ  1 
ATOM   2567 N  N   . ILE   B 2 115 ? -33.464 16.396  -0.998  1.00 22.29  ? 231 ILE   B N   1 
ATOM   2568 C  CA  . ILE   B 2 115 ? -32.450 15.523  -0.369  1.00 23.81  ? 231 ILE   B CA  1 
ATOM   2569 C  C   . ILE   B 2 115 ? -32.972 15.100  0.989   1.00 22.62  ? 231 ILE   B C   1 
ATOM   2570 O  O   . ILE   B 2 115 ? -33.675 15.880  1.645   1.00 24.38  ? 231 ILE   B O   1 
ATOM   2571 C  CB  . ILE   B 2 115 ? -31.107 16.244  -0.276  1.00 24.80  ? 231 ILE   B CB  1 
ATOM   2572 C  CG1 . ILE   B 2 115 ? -29.982 15.278  0.095   1.00 25.87  ? 231 ILE   B CG1 1 
ATOM   2573 C  CG2 . ILE   B 2 115 ? -31.205 17.416  0.693   1.00 24.82  ? 231 ILE   B CG2 1 
ATOM   2574 C  CD1 . ILE   B 2 115 ? -28.621 15.731  -0.363  1.00 29.50  ? 231 ILE   B CD1 1 
ATOM   2575 N  N   . PHE   B 2 116 ? -32.621 13.880  1.373   1.00 23.59  ? 232 PHE   B N   1 
ATOM   2576 C  CA  . PHE   B 2 116 ? -32.897 13.275  2.688   1.00 23.21  ? 232 PHE   B CA  1 
ATOM   2577 C  C   . PHE   B 2 116 ? -31.549 12.775  3.158   1.00 23.57  ? 232 PHE   B C   1 
ATOM   2578 O  O   . PHE   B 2 116 ? -30.950 11.875  2.471   1.00 21.98  ? 232 PHE   B O   1 
ATOM   2579 C  CB  . PHE   B 2 116 ? -33.937 12.158  2.576   1.00 23.56  ? 232 PHE   B CB  1 
ATOM   2580 C  CG  . PHE   B 2 116 ? -35.273 12.670  2.132   1.00 21.10  ? 232 PHE   B CG  1 
ATOM   2581 C  CD1 . PHE   B 2 116 ? -35.515 12.907  0.785   1.00 21.96  ? 232 PHE   B CD1 1 
ATOM   2582 C  CD2 . PHE   B 2 116 ? -36.246 13.010  3.048   1.00 24.32  ? 232 PHE   B CD2 1 
ATOM   2583 C  CE1 . PHE   B 2 116 ? -36.728 13.431  0.357   1.00 22.62  ? 232 PHE   B CE1 1 
ATOM   2584 C  CE2 . PHE   B 2 116 ? -37.464 13.530  2.623   1.00 24.25  ? 232 PHE   B CE2 1 
ATOM   2585 C  CZ  . PHE   B 2 116 ? -37.682 13.767  1.277   1.00 22.89  ? 232 PHE   B CZ  1 
ATOM   2586 N  N   . LEU   B 2 117 ? -31.015 13.408  4.201   1.00 21.58  ? 233 LEU   B N   1 
ATOM   2587 C  CA  . LEU   B 2 117 ? -29.671 13.103  4.724   1.00 20.30  ? 233 LEU   B CA  1 
ATOM   2588 C  C   . LEU   B 2 117 ? -29.797 12.538  6.125   1.00 22.87  ? 233 LEU   B C   1 
ATOM   2589 O  O   . LEU   B 2 117 ? -30.198 13.296  7.041   1.00 22.56  ? 233 LEU   B O   1 
ATOM   2590 C  CB  . LEU   B 2 117 ? -28.827 14.392  4.710   1.00 20.58  ? 233 LEU   B CB  1 
ATOM   2591 C  CG  . LEU   B 2 117 ? -27.435 14.302  5.308   1.00 20.69  ? 233 LEU   B CG  1 
ATOM   2592 C  CD1 . LEU   B 2 117 ? -26.524 13.332  4.585   1.00 22.89  ? 233 LEU   B CD1 1 
ATOM   2593 C  CD2 . LEU   B 2 117 ? -26.762 15.666  5.329   1.00 20.29  ? 233 LEU   B CD2 1 
ATOM   2594 N  N   . TRP   B 2 118 ? -29.416 11.264  6.318   1.00 22.78  ? 234 TRP   B N   1 
ATOM   2595 C  CA  . TRP   B 2 118 ? -29.269 10.656  7.665   1.00 22.06  ? 234 TRP   B CA  1 
ATOM   2596 C  C   . TRP   B 2 118 ? -28.053 11.275  8.372   1.00 22.06  ? 234 TRP   B C   1 
ATOM   2597 O  O   . TRP   B 2 118 ? -26.924 11.126  7.869   1.00 24.56  ? 234 TRP   B O   1 
ATOM   2598 C  CB  . TRP   B 2 118 ? -29.158 9.132   7.552   1.00 21.37  ? 234 TRP   B CB  1 
ATOM   2599 C  CG  . TRP   B 2 118 ? -30.434 8.424   7.210   1.00 22.67  ? 234 TRP   B CG  1 
ATOM   2600 C  CD1 . TRP   B 2 118 ? -30.792 7.835   6.036   1.00 25.73  ? 234 TRP   B CD1 1 
ATOM   2601 C  CD2 . TRP   B 2 118 ? -31.560 8.281   8.083   1.00 22.99  ? 234 TRP   B CD2 1 
ATOM   2602 N  NE1 . TRP   B 2 118 ? -32.041 7.272   6.143   1.00 25.14  ? 234 TRP   B NE1 1 
ATOM   2603 C  CE2 . TRP   B 2 118 ? -32.539 7.541   7.386   1.00 24.57  ? 234 TRP   B CE2 1 
ATOM   2604 C  CE3 . TRP   B 2 118 ? -31.781 8.633   9.416   1.00 23.86  ? 234 TRP   B CE3 1 
ATOM   2605 C  CZ2 . TRP   B 2 118 ? -33.742 7.160   7.982   1.00 25.71  ? 234 TRP   B CZ2 1 
ATOM   2606 C  CZ3 . TRP   B 2 118 ? -32.983 8.275   10.000  1.00 25.03  ? 234 TRP   B CZ3 1 
ATOM   2607 C  CH2 . TRP   B 2 118 ? -33.964 7.583   9.277   1.00 25.03  ? 234 TRP   B CH2 1 
ATOM   2608 N  N   . CYS   B 2 119 ? -28.274 11.974  9.498   1.00 20.64  ? 235 CYS   B N   1 
ATOM   2609 C  CA  . CYS   B 2 119 ? -27.278 12.821  10.185  1.00 20.93  ? 235 CYS   B CA  1 
ATOM   2610 C  C   . CYS   B 2 119 ? -26.848 12.234  11.517  1.00 20.90  ? 235 CYS   B C   1 
ATOM   2611 O  O   . CYS   B 2 119 ? -25.928 12.783  12.145  1.00 25.58  ? 235 CYS   B O   1 
ATOM   2612 C  CB  . CYS   B 2 119 ? -27.831 14.227  10.372  1.00 21.81  ? 235 CYS   B CB  1 
ATOM   2613 S  SG  . CYS   B 2 119 ? -27.949 15.088  8.787   1.00 23.95  ? 235 CYS   B SG  1 
ATOM   2614 N  N   . GLY   B 2 120 ? -27.477 11.113  11.942  1.00 22.07  ? 236 GLY   B N   1 
ATOM   2615 C  CA  . GLY   B 2 120 ? -27.147 10.548  13.256  1.00 21.78  ? 236 GLY   B CA  1 
ATOM   2616 C  C   . GLY   B 2 120 ? -27.754 11.353  14.381  1.00 22.41  ? 236 GLY   B C   1 
ATOM   2617 O  O   . GLY   B 2 120 ? -28.886 11.850  14.216  1.00 22.37  ? 236 GLY   B O   1 
ATOM   2618 N  N   . SER   B 2 121 ? -27.010 11.515  15.475  1.00 24.49  ? 237 SER   B N   1 
ATOM   2619 C  CA  . SER   B 2 121 ? -27.516 12.166  16.707  1.00 29.45  ? 237 SER   B CA  1 
ATOM   2620 C  C   . SER   B 2 121 ? -26.461 13.072  17.343  1.00 26.68  ? 237 SER   B C   1 
ATOM   2621 O  O   . SER   B 2 121 ? -26.755 13.629  18.410  1.00 28.49  ? 237 SER   B O   1 
ATOM   2622 C  CB  . SER   B 2 121 ? -27.989 11.101  17.688  1.00 33.41  ? 237 SER   B CB  1 
ATOM   2623 O  OG  . SER   B 2 121 ? -26.941 10.154  17.869  1.00 39.62  ? 237 SER   B OG  1 
ATOM   2624 N  N   . GLY   B 2 122 ? -25.312 13.263  16.697  1.00 25.90  ? 238 GLY   B N   1 
ATOM   2625 C  CA  . GLY   B 2 122 ? -24.217 14.058  17.263  1.00 25.67  ? 238 GLY   B CA  1 
ATOM   2626 C  C   . GLY   B 2 122 ? -23.959 15.288  16.426  1.00 23.07  ? 238 GLY   B C   1 
ATOM   2627 O  O   . GLY   B 2 122 ? -24.923 15.967  16.043  1.00 22.65  ? 238 GLY   B O   1 
ATOM   2628 N  N   . GLU   B 2 123 ? -22.698 15.517  16.096  1.00 25.55  ? 239 GLU   B N   1 
ATOM   2629 C  CA  . GLU   B 2 123 ? -22.229 16.692  15.311  1.00 26.73  ? 239 GLU   B CA  1 
ATOM   2630 C  C   . GLU   B 2 123 ? -22.902 16.713  13.931  1.00 25.21  ? 239 GLU   B C   1 
ATOM   2631 O  O   . GLU   B 2 123 ? -22.987 17.774  13.320  1.00 22.62  ? 239 GLU   B O   1 
ATOM   2632 C  CB  . GLU   B 2 123 ? -20.703 16.650  15.234  1.00 30.96  ? 239 GLU   B CB  1 
ATOM   2633 C  CG  . GLU   B 2 123 ? -20.209 15.516  14.357  1.00 33.95  ? 239 GLU   B CG  1 
ATOM   2634 C  CD  . GLU   B 2 123 ? -18.702 15.367  14.185  1.00 44.63  ? 239 GLU   B CD  1 
ATOM   2635 O  OE1 . GLU   B 2 123 ? -18.271 14.271  13.719  1.00 48.49  ? 239 GLU   B OE1 1 
ATOM   2636 O  OE2 . GLU   B 2 123 ? -17.978 16.316  14.546  1.00 45.83  ? 239 GLU   B OE2 1 
ATOM   2637 N  N   . GLY   B 2 124 ? -23.397 15.586  13.420  1.00 22.84  ? 240 GLY   B N   1 
ATOM   2638 C  CA  . GLY   B 2 124 ? -24.114 15.586  12.130  1.00 21.30  ? 240 GLY   B CA  1 
ATOM   2639 C  C   . GLY   B 2 124 ? -25.291 16.515  12.103  1.00 20.60  ? 240 GLY   B C   1 
ATOM   2640 O  O   . GLY   B 2 124 ? -25.733 16.919  11.019  1.00 21.90  ? 240 GLY   B O   1 
ATOM   2641 N  N   . LEU   B 2 125 ? -25.950 16.736  13.237  1.00 23.03  ? 241 LEU   B N   1 
ATOM   2642 C  CA  . LEU   B 2 125 ? -27.165 17.597  13.266  1.00 23.80  ? 241 LEU   B CA  1 
ATOM   2643 C  C   . LEU   B 2 125 ? -26.765 19.042  12.859  1.00 24.29  ? 241 LEU   B C   1 
ATOM   2644 O  O   . LEU   B 2 125 ? -27.593 19.751  12.298  1.00 22.12  ? 241 LEU   B O   1 
ATOM   2645 C  CB  . LEU   B 2 125 ? -27.757 17.542  14.678  1.00 27.26  ? 241 LEU   B CB  1 
ATOM   2646 C  CG  . LEU   B 2 125 ? -28.758 16.431  15.009  1.00 30.23  ? 241 LEU   B CG  1 
ATOM   2647 C  CD1 . LEU   B 2 125 ? -28.568 15.195  14.203  1.00 30.21  ? 241 LEU   B CD1 1 
ATOM   2648 C  CD2 . LEU   B 2 125 ? -28.808 16.149  16.506  1.00 29.95  ? 241 LEU   B CD2 1 
ATOM   2649 N  N   . ASP   B 2 126 ? -25.508 19.407  13.052  1.00 24.14  ? 242 ASP   B N   1 
ATOM   2650 C  CA  . ASP   B 2 126 ? -24.959 20.737  12.650  1.00 23.98  ? 242 ASP   B CA  1 
ATOM   2651 C  C   . ASP   B 2 126 ? -24.280 20.639  11.282  1.00 23.94  ? 242 ASP   B C   1 
ATOM   2652 O  O   . ASP   B 2 126 ? -24.643 21.412  10.388  1.00 23.98  ? 242 ASP   B O   1 
ATOM   2653 C  CB  . ASP   B 2 126 ? -23.979 21.227  13.704  1.00 25.04  ? 242 ASP   B CB  1 
ATOM   2654 C  CG  . ASP   B 2 126 ? -24.552 21.154  15.119  1.00 26.37  ? 242 ASP   B CG  1 
ATOM   2655 O  OD1 . ASP   B 2 126 ? -25.582 21.789  15.368  1.00 26.58  ? 242 ASP   B OD1 1 
ATOM   2656 O  OD2 . ASP   B 2 126 ? -23.997 20.423  15.930  1.00 27.35  ? 242 ASP   B OD2 1 
ATOM   2657 N  N   . LEU   B 2 127 ? -23.379 19.672  11.121  1.00 23.57  ? 243 LEU   B N   1 
ATOM   2658 C  CA  . LEU   B 2 127 ? -22.571 19.507  9.885   1.00 23.63  ? 243 LEU   B CA  1 
ATOM   2659 C  C   . LEU   B 2 127 ? -23.454 19.103  8.716   1.00 26.11  ? 243 LEU   B C   1 
ATOM   2660 O  O   . LEU   B 2 127 ? -23.163 19.545  7.582   1.00 23.60  ? 243 LEU   B O   1 
ATOM   2661 C  CB  . LEU   B 2 127 ? -21.431 18.539  10.181  1.00 25.03  ? 243 LEU   B CB  1 
ATOM   2662 C  CG  . LEU   B 2 127 ? -20.412 19.078  11.182  1.00 27.67  ? 243 LEU   B CG  1 
ATOM   2663 C  CD1 . LEU   B 2 127 ? -19.426 18.010  11.599  1.00 28.97  ? 243 LEU   B CD1 1 
ATOM   2664 C  CD2 . LEU   B 2 127 ? -19.661 20.253  10.600  1.00 30.60  ? 243 LEU   B CD2 1 
ATOM   2665 N  N   . GLY   B 2 128 ? -24.539 18.344  8.962   1.00 23.64  ? 244 GLY   B N   1 
ATOM   2666 C  CA  . GLY   B 2 128 ? -25.480 17.997  7.892   1.00 23.34  ? 244 GLY   B CA  1 
ATOM   2667 C  C   . GLY   B 2 128 ? -26.232 19.204  7.358   1.00 20.36  ? 244 GLY   B C   1 
ATOM   2668 O  O   . GLY   B 2 128 ? -26.580 19.229  6.170   1.00 22.61  ? 244 GLY   B O   1 
ATOM   2669 N  N   . ARG   B 2 129 ? -26.582 20.141  8.228   1.00 22.37  ? 245 ARG   B N   1 
ATOM   2670 C  CA  . ARG   B 2 129 ? -27.194 21.415  7.804   1.00 21.73  ? 245 ARG   B CA  1 
ATOM   2671 C  C   . ARG   B 2 129 ? -26.182 22.207  6.958   1.00 19.47  ? 245 ARG   B C   1 
ATOM   2672 O  O   . ARG   B 2 129 ? -26.575 22.713  5.901   1.00 22.79  ? 245 ARG   B O   1 
ATOM   2673 C  CB  . ARG   B 2 129 ? -27.699 22.181  9.020   1.00 23.25  ? 245 ARG   B CB  1 
ATOM   2674 C  CG  . ARG   B 2 129 ? -28.954 21.585  9.633   1.00 23.35  ? 245 ARG   B CG  1 
ATOM   2675 C  CD  . ARG   B 2 129 ? -29.346 22.314  10.908  1.00 24.32  ? 245 ARG   B CD  1 
ATOM   2676 N  NE  . ARG   B 2 129 ? -30.750 22.108  11.167  1.00 24.32  ? 245 ARG   B NE  1 
ATOM   2677 C  CZ  . ARG   B 2 129 ? -31.266 21.038  11.789  1.00 23.76  ? 245 ARG   B CZ  1 
ATOM   2678 N  NH1 . ARG   B 2 129 ? -30.482 20.083  12.261  1.00 23.51  ? 245 ARG   B NH1 1 
ATOM   2679 N  NH2 . ARG   B 2 129 ? -32.576 20.982  11.988  1.00 24.99  ? 245 ARG   B NH2 1 
ATOM   2680 N  N   . VAL   B 2 130 ? -24.929 22.236  7.354   1.00 23.22  ? 246 VAL   B N   1 
ATOM   2681 C  CA  . VAL   B 2 130 ? -23.873 22.921  6.542   1.00 23.69  ? 246 VAL   B CA  1 
ATOM   2682 C  C   . VAL   B 2 130 ? -23.825 22.292  5.146   1.00 23.10  ? 246 VAL   B C   1 
ATOM   2683 O  O   . VAL   B 2 130 ? -23.773 23.012  4.116   1.00 21.07  ? 246 VAL   B O   1 
ATOM   2684 C  CB  . VAL   B 2 130 ? -22.521 22.884  7.268   1.00 25.73  ? 246 VAL   B CB  1 
ATOM   2685 C  CG1 . VAL   B 2 130 ? -21.408 23.484  6.402   1.00 27.59  ? 246 VAL   B CG1 1 
ATOM   2686 C  CG2 . VAL   B 2 130 ? -22.604 23.601  8.610   1.00 24.56  ? 246 VAL   B CG2 1 
ATOM   2687 N  N   . CYS   B 2 131 ? -23.851 20.967  5.086   1.00 22.50  ? 247 CYS   B N   1 
ATOM   2688 C  CA  . CYS   B 2 131 ? -23.816 20.180  3.824   1.00 23.74  ? 247 CYS   B CA  1 
ATOM   2689 C  C   . CYS   B 2 131 ? -24.994 20.542  2.936   1.00 21.10  ? 247 CYS   B C   1 
ATOM   2690 O  O   . CYS   B 2 131 ? -24.780 20.898  1.753   1.00 21.34  ? 247 CYS   B O   1 
ATOM   2691 C  CB  . CYS   B 2 131 ? -23.880 18.674  4.098   1.00 21.86  ? 247 CYS   B CB  1 
ATOM   2692 S  SG  . CYS   B 2 131 ? -22.355 17.987  4.729   1.00 25.15  ? 247 CYS   B SG  1 
ATOM   2693 N  N   . LEU   B 2 132 ? -26.210 20.539  3.506   1.00 22.32  ? 248 LEU   B N   1 
ATOM   2694 C  CA  . LEU   B 2 132 ? -27.435 20.852  2.749   1.00 21.31  ? 248 LEU   B CA  1 
ATOM   2695 C  C   . LEU   B 2 132 ? -27.243 22.233  2.085   1.00 23.86  ? 248 LEU   B C   1 
ATOM   2696 O  O   . LEU   B 2 132 ? -27.454 22.361  0.901   1.00 23.76  ? 248 LEU   B O   1 
ATOM   2697 C  CB  . LEU   B 2 132 ? -28.663 20.831  3.657   1.00 22.45  ? 248 LEU   B CB  1 
ATOM   2698 C  CG  . LEU   B 2 132 ? -29.564 19.587  3.559   1.00 24.88  ? 248 LEU   B CG  1 
ATOM   2699 C  CD1 . LEU   B 2 132 ? -28.800 18.317  3.747   1.00 24.06  ? 248 LEU   B CD1 1 
ATOM   2700 C  CD2 . LEU   B 2 132 ? -30.699 19.694  4.552   1.00 25.01  ? 248 LEU   B CD2 1 
ATOM   2701 N  N   . ARG   B 2 133 ? -26.844 23.237  2.849   1.00 22.68  ? 249 ARG   B N   1 
ATOM   2702 C  CA  . ARG   B 2 133 ? -26.696 24.625  2.319   1.00 23.49  ? 249 ARG   B CA  1 
ATOM   2703 C  C   . ARG   B 2 133 ? -25.510 24.710  1.329   1.00 21.84  ? 249 ARG   B C   1 
ATOM   2704 O  O   . ARG   B 2 133 ? -25.625 25.439  0.308   1.00 24.54  ? 249 ARG   B O   1 
ATOM   2705 C  CB  . ARG   B 2 133 ? -26.532 25.552  3.512   1.00 22.48  ? 249 ARG   B CB  1 
ATOM   2706 C  CG  . ARG   B 2 133 ? -27.808 25.678  4.324   1.00 25.65  ? 249 ARG   B CG  1 
ATOM   2707 C  CD  . ARG   B 2 133 ? -27.745 26.822  5.313   1.00 25.04  ? 249 ARG   B CD  1 
ATOM   2708 N  NE  . ARG   B 2 133 ? -26.654 26.677  6.238   1.00 24.15  ? 249 ARG   B NE  1 
ATOM   2709 C  CZ  . ARG   B 2 133 ? -26.740 26.235  7.488   1.00 27.93  ? 249 ARG   B CZ  1 
ATOM   2710 N  NH1 . ARG   B 2 133 ? -27.885 25.811  8.023   1.00 26.56  ? 249 ARG   B NH1 1 
ATOM   2711 N  NH2 . ARG   B 2 133 ? -25.634 26.126  8.176   1.00 27.41  ? 249 ARG   B NH2 1 
ATOM   2712 N  N   . LYS   B 2 134 ? -24.452 23.968  1.584   1.00 21.73  ? 250 LYS   B N   1 
ATOM   2713 C  CA  . LYS   B 2 134 ? -23.306 23.876  0.651   1.00 25.04  ? 250 LYS   B CA  1 
ATOM   2714 C  C   . LYS   B 2 134 ? -23.784 23.368  -0.717  1.00 26.48  ? 250 LYS   B C   1 
ATOM   2715 O  O   . LYS   B 2 134 ? -23.362 23.910  -1.784  1.00 25.40  ? 250 LYS   B O   1 
ATOM   2716 C  CB  . LYS   B 2 134 ? -22.197 23.059  1.285   1.00 23.62  ? 250 LYS   B CB  1 
ATOM   2717 C  CG  . LYS   B 2 134 ? -20.935 23.034  0.445   1.00 27.07  ? 250 LYS   B CG  1 
ATOM   2718 C  CD  . LYS   B 2 134 ? -19.877 22.146  0.980   1.00 31.15  ? 250 LYS   B CD  1 
ATOM   2719 C  CE  . LYS   B 2 134 ? -18.726 22.028  0.006   1.00 37.87  ? 250 LYS   B CE  1 
ATOM   2720 N  NZ  . LYS   B 2 134 ? -17.943 23.288  -0.005  1.00 42.21  ? 250 LYS   B NZ  1 
ATOM   2721 N  N   . TRP   B 2 135 ? -24.689 22.391  -0.723  1.00 25.29  ? 251 TRP   B N   1 
ATOM   2722 C  CA  . TRP   B 2 135 ? -25.164 21.769  -1.977  1.00 23.48  ? 251 TRP   B CA  1 
ATOM   2723 C  C   . TRP   B 2 135 ? -26.307 22.581  -2.541  1.00 24.05  ? 251 TRP   B C   1 
ATOM   2724 O  O   . TRP   B 2 135 ? -26.805 22.181  -3.597  1.00 28.07  ? 251 TRP   B O   1 
ATOM   2725 C  CB  . TRP   B 2 135 ? -25.568 20.310  -1.733  1.00 23.80  ? 251 TRP   B CB  1 
ATOM   2726 C  CG  . TRP   B 2 135 ? -24.463 19.480  -1.173  1.00 22.76  ? 251 TRP   B CG  1 
ATOM   2727 C  CD1 . TRP   B 2 135 ? -23.134 19.579  -1.451  1.00 25.80  ? 251 TRP   B CD1 1 
ATOM   2728 C  CD2 . TRP   B 2 135 ? -24.606 18.398  -0.253  1.00 24.20  ? 251 TRP   B CD2 1 
ATOM   2729 N  NE1 . TRP   B 2 135 ? -22.445 18.653  -0.748  1.00 26.74  ? 251 TRP   B NE1 1 
ATOM   2730 C  CE2 . TRP   B 2 135 ? -23.313 17.912  -0.001  1.00 25.67  ? 251 TRP   B CE2 1 
ATOM   2731 C  CE3 . TRP   B 2 135 ? -25.697 17.815  0.398   1.00 24.03  ? 251 TRP   B CE3 1 
ATOM   2732 C  CZ2 . TRP   B 2 135 ? -23.086 16.842  0.850   1.00 23.30  ? 251 TRP   B CZ2 1 
ATOM   2733 C  CZ3 . TRP   B 2 135 ? -25.466 16.757  1.256   1.00 24.11  ? 251 TRP   B CZ3 1 
ATOM   2734 C  CH2 . TRP   B 2 135 ? -24.174 16.311  1.493   1.00 23.72  ? 251 TRP   B CH2 1 
ATOM   2735 N  N   . GLY   B 2 136 ? -26.767 23.646  -1.858  1.00 23.67  ? 252 GLY   B N   1 
ATOM   2736 C  CA  . GLY   B 2 136 ? -27.751 24.564  -2.437  1.00 25.20  ? 252 GLY   B CA  1 
ATOM   2737 C  C   . GLY   B 2 136 ? -29.160 24.282  -1.988  1.00 27.54  ? 252 GLY   B C   1 
ATOM   2738 O  O   . GLY   B 2 136 ? -30.107 24.805  -2.598  1.00 24.75  ? 252 GLY   B O   1 
ATOM   2739 N  N   . TYR   B 2 137 ? -29.327 23.451  -0.952  1.00 24.66  ? 253 TYR   B N   1 
ATOM   2740 C  CA  . TYR   B 2 137 ? -30.680 23.206  -0.395  1.00 25.41  ? 253 TYR   B CA  1 
ATOM   2741 C  C   . TYR   B 2 137 ? -30.945 24.077  0.841   1.00 27.56  ? 253 TYR   B C   1 
ATOM   2742 O  O   . TYR   B 2 137 ? -29.995 24.573  1.498   1.00 26.81  ? 253 TYR   B O   1 
ATOM   2743 C  CB  . TYR   B 2 137 ? -30.810 21.758  0.092   1.00 23.47  ? 253 TYR   B CB  1 
ATOM   2744 C  CG  . TYR   B 2 137 ? -30.523 20.702  -0.932  1.00 21.71  ? 253 TYR   B CG  1 
ATOM   2745 C  CD1 . TYR   B 2 137 ? -31.543 20.157  -1.716  1.00 23.46  ? 253 TYR   B CD1 1 
ATOM   2746 C  CD2 . TYR   B 2 137 ? -29.258 20.168  -1.040  1.00 21.12  ? 253 TYR   B CD2 1 
ATOM   2747 C  CE1 . TYR   B 2 137 ? -31.256 19.177  -2.653  1.00 23.03  ? 253 TYR   B CE1 1 
ATOM   2748 C  CE2 . TYR   B 2 137 ? -28.959 19.192  -1.967  1.00 22.54  ? 253 TYR   B CE2 1 
ATOM   2749 C  CZ  . TYR   B 2 137 ? -29.974 18.663  -2.748  1.00 22.96  ? 253 TYR   B CZ  1 
ATOM   2750 O  OH  . TYR   B 2 137 ? -29.672 17.696  -3.655  1.00 27.12  ? 253 TYR   B OH  1 
ATOM   2751 N  N   B ARG   B 2 138 ? -32.233 24.247  1.134   0.38 25.88  ? 254 ARG   B N   1 
ATOM   2752 N  N   C ARG   B 2 138 ? -32.219 24.213  1.161   0.62 26.76  ? 254 ARG   B N   1 
ATOM   2753 C  CA  B ARG   B 2 138 ? -32.789 24.786  2.404   0.38 27.87  ? 254 ARG   B CA  1 
ATOM   2754 C  CA  C ARG   B 2 138 ? -32.740 24.779  2.428   0.62 31.29  ? 254 ARG   B CA  1 
ATOM   2755 C  C   B ARG   B 2 138 ? -33.363 23.604  3.199   0.38 28.51  ? 254 ARG   B C   1 
ATOM   2756 C  C   C ARG   B 2 138 ? -33.376 23.621  3.211   0.62 30.23  ? 254 ARG   B C   1 
ATOM   2757 O  O   B ARG   B 2 138 ? -34.074 22.783  2.582   0.38 28.61  ? 254 ARG   B O   1 
ATOM   2758 O  O   C ARG   B 2 138 ? -34.120 22.825  2.596   0.62 30.94  ? 254 ARG   B O   1 
ATOM   2759 C  CB  B ARG   B 2 138 ? -33.890 25.811  2.103   0.38 27.98  ? 254 ARG   B CB  1 
ATOM   2760 C  CB  C ARG   B 2 138 ? -33.729 25.897  2.081   0.62 34.80  ? 254 ARG   B CB  1 
ATOM   2761 C  CG  B ARG   B 2 138 ? -33.800 26.463  0.729   0.38 29.82  ? 254 ARG   B CG  1 
ATOM   2762 C  CG  C ARG   B 2 138 ? -34.574 26.388  3.249   0.62 42.82  ? 254 ARG   B CG  1 
ATOM   2763 C  CD  B ARG   B 2 138 ? -34.782 27.601  0.464   0.38 30.16  ? 254 ARG   B CD  1 
ATOM   2764 C  CD  C ARG   B 2 138 ? -35.872 27.061  2.803   0.62 46.17  ? 254 ARG   B CD  1 
ATOM   2765 N  NE  B ARG   B 2 138 ? -36.111 27.183  0.042   0.38 30.07  ? 254 ARG   B NE  1 
ATOM   2766 N  NE  C ARG   B 2 138 ? -37.016 26.370  3.390   0.62 51.24  ? 254 ARG   B NE  1 
ATOM   2767 C  CZ  B ARG   B 2 138 ? -36.403 26.693  -1.156  0.38 31.24  ? 254 ARG   B CZ  1 
ATOM   2768 C  CZ  C ARG   B 2 138 ? -38.156 26.089  2.771   0.62 51.15  ? 254 ARG   B CZ  1 
ATOM   2769 N  NH1 B ARG   B 2 138 ? -37.649 26.353  -1.450  0.38 31.63  ? 254 ARG   B NH1 1 
ATOM   2770 N  NH1 C ARG   B 2 138 ? -39.101 25.441  3.429   0.62 53.02  ? 254 ARG   B NH1 1 
ATOM   2771 N  NH2 B ARG   B 2 138 ? -35.450 26.530  -2.053  0.38 28.96  ? 254 ARG   B NH2 1 
ATOM   2772 N  NH2 C ARG   B 2 138 ? -38.346 26.424  1.504   0.62 52.61  ? 254 ARG   B NH2 1 
ATOM   2773 N  N   . ARG   B 2 139 ? -33.037 23.489  4.484   1.00 30.77  ? 255 ARG   B N   1 
ATOM   2774 C  CA  . ARG   B 2 139 ? -33.560 22.416  5.375   1.00 31.23  ? 255 ARG   B CA  1 
ATOM   2775 C  C   . ARG   B 2 139 ? -35.035 22.719  5.597   1.00 32.58  ? 255 ARG   B C   1 
ATOM   2776 O  O   . ARG   B 2 139 ? -35.313 23.833  6.081   1.00 32.97  ? 255 ARG   B O   1 
ATOM   2777 C  CB  . ARG   B 2 139 ? -32.746 22.388  6.665   1.00 34.29  ? 255 ARG   B CB  1 
ATOM   2778 C  CG  . ARG   B 2 139 ? -32.876 21.125  7.512   1.00 36.35  ? 255 ARG   B CG  1 
ATOM   2779 C  CD  . ARG   B 2 139 ? -34.020 21.092  8.498   1.00 39.53  ? 255 ARG   B CD  1 
ATOM   2780 N  NE  . ARG   B 2 139 ? -34.276 22.385  9.125   1.00 34.01  ? 255 ARG   B NE  1 
ATOM   2781 C  CZ  . ARG   B 2 139 ? -35.478 22.830  9.444   1.00 37.37  ? 255 ARG   B CZ  1 
ATOM   2782 N  NH1 . ARG   B 2 139 ? -36.554 22.071  9.253   1.00 37.21  ? 255 ARG   B NH1 1 
ATOM   2783 N  NH2 . ARG   B 2 139 ? -35.597 24.048  9.945   1.00 34.08  ? 255 ARG   B NH2 1 
ATOM   2784 N  N   . CYS   B 2 140 ? -35.946 21.835  5.173   1.00 29.28  ? 256 CYS   B N   1 
ATOM   2785 C  CA  . CYS   B 2 140 ? -37.412 22.096  5.268   1.00 29.79  ? 256 CYS   B CA  1 
ATOM   2786 C  C   . CYS   B 2 140 ? -38.110 21.151  6.257   1.00 30.01  ? 256 CYS   B C   1 
ATOM   2787 O  O   . CYS   B 2 140 ? -39.191 21.529  6.751   1.00 31.72  ? 256 CYS   B O   1 
ATOM   2788 C  CB  . CYS   B 2 140 ? -38.087 22.141  3.908   1.00 31.57  ? 256 CYS   B CB  1 
ATOM   2789 S  SG  . CYS   B 2 140 ? -37.863 20.640  2.914   1.00 35.72  ? 256 CYS   B SG  1 
ATOM   2790 N  N   . GLU   B 2 141 ? -37.548 19.983  6.557   1.00 25.41  ? 257 GLU   B N   1 
ATOM   2791 C  CA  . GLU   B 2 141 ? -38.126 19.090  7.601   1.00 27.15  ? 257 GLU   B CA  1 
ATOM   2792 C  C   . GLU   B 2 141 ? -36.978 18.430  8.343   1.00 25.39  ? 257 GLU   B C   1 
ATOM   2793 O  O   . GLU   B 2 141 ? -35.865 18.251  7.778   1.00 25.77  ? 257 GLU   B O   1 
ATOM   2794 C  CB  . GLU   B 2 141 ? -39.089 18.046  7.010   1.00 28.59  ? 257 GLU   B CB  1 
ATOM   2795 C  CG  . GLU   B 2 141 ? -40.286 18.609  6.250   1.00 30.41  ? 257 GLU   B CG  1 
ATOM   2796 C  CD  . GLU   B 2 141 ? -41.323 19.340  7.101   1.00 30.88  ? 257 GLU   B CD  1 
ATOM   2797 O  OE1 . GLU   B 2 141 ? -41.148 19.424  8.359   1.00 31.73  ? 257 GLU   B OE1 1 
ATOM   2798 O  OE2 . GLU   B 2 141 ? -42.232 19.917  6.500   1.00 34.11  ? 257 GLU   B OE2 1 
ATOM   2799 N  N   . ASP   B 2 142 ? -37.242 18.035  9.574   1.00 25.58  ? 258 ASP   B N   1 
ATOM   2800 C  CA  . ASP   B 2 142 ? -36.309 17.270  10.419  1.00 26.34  ? 258 ASP   B CA  1 
ATOM   2801 C  C   . ASP   B 2 142 ? -37.076 16.029  10.854  1.00 30.32  ? 258 ASP   B C   1 
ATOM   2802 O  O   . ASP   B 2 142 ? -37.989 16.162  11.713  1.00 28.49  ? 258 ASP   B O   1 
ATOM   2803 C  CB  . ASP   B 2 142 ? -35.833 18.154  11.564  1.00 28.29  ? 258 ASP   B CB  1 
ATOM   2804 C  CG  . ASP   B 2 142 ? -34.755 17.559  12.439  1.00 28.72  ? 258 ASP   B CG  1 
ATOM   2805 O  OD1 . ASP   B 2 142 ? -34.697 16.343  12.505  1.00 32.79  ? 258 ASP   B OD1 1 
ATOM   2806 O  OD2 . ASP   B 2 142 ? -33.944 18.359  13.044  1.00 36.86  ? 258 ASP   B OD2 1 
ATOM   2807 N  N   . ILE   B 2 143 ? -36.774 14.890  10.226  1.00 27.97  ? 259 ILE   B N   1 
ATOM   2808 C  CA  . ILE   B 2 143 ? -37.475 13.610  10.515  1.00 26.42  ? 259 ILE   B CA  1 
ATOM   2809 C  C   . ILE   B 2 143 ? -36.687 12.870  11.580  1.00 27.55  ? 259 ILE   B C   1 
ATOM   2810 O  O   . ILE   B 2 143 ? -35.503 12.596  11.372  1.00 29.43  ? 259 ILE   B O   1 
ATOM   2811 C  CB  . ILE   B 2 143 ? -37.642 12.780  9.260   1.00 25.78  ? 259 ILE   B CB  1 
ATOM   2812 C  CG1 . ILE   B 2 143 ? -38.414 13.574  8.221   1.00 27.04  ? 259 ILE   B CG1 1 
ATOM   2813 C  CG2 . ILE   B 2 143 ? -38.316 11.454  9.600   1.00 27.62  ? 259 ILE   B CG2 1 
ATOM   2814 C  CD1 . ILE   B 2 143 ? -38.251 13.101  6.812   1.00 27.26  ? 259 ILE   B CD1 1 
ATOM   2815 N  N   . CYS   B 2 144 ? -37.322 12.561  12.708  1.00 25.16  ? 260 CYS   B N   1 
ATOM   2816 C  CA  . CYS   B 2 144 ? -36.634 11.835  13.786  1.00 24.32  ? 260 CYS   B CA  1 
ATOM   2817 C  C   . CYS   B 2 144 ? -37.087 10.385  13.812  1.00 25.22  ? 260 CYS   B C   1 
ATOM   2818 O  O   . CYS   B 2 144 ? -38.298 10.111  13.915  1.00 25.43  ? 260 CYS   B O   1 
ATOM   2819 C  CB  . CYS   B 2 144 ? -36.887 12.428  15.155  1.00 29.68  ? 260 CYS   B CB  1 
ATOM   2820 S  SG  . CYS   B 2 144 ? -36.071 14.028  15.363  1.00 37.41  ? 260 CYS   B SG  1 
ATOM   2821 N  N   . TRP   B 2 145 ? -36.098 9.525   13.738  1.00 26.96  ? 261 TRP   B N   1 
ATOM   2822 C  CA  . TRP   B 2 145 ? -36.201 8.088   14.030  1.00 26.98  ? 261 TRP   B CA  1 
ATOM   2823 C  C   . TRP   B 2 145 ? -36.017 7.879   15.537  1.00 23.02  ? 261 TRP   B C   1 
ATOM   2824 O  O   . TRP   B 2 145 ? -34.882 7.903   16.067  1.00 25.83  ? 261 TRP   B O   1 
ATOM   2825 C  CB  . TRP   B 2 145 ? -35.196 7.307   13.183  1.00 27.70  ? 261 TRP   B CB  1 
ATOM   2826 C  CG  . TRP   B 2 145 ? -35.224 5.851   13.493  1.00 26.39  ? 261 TRP   B CG  1 
ATOM   2827 C  CD1 . TRP   B 2 145 ? -36.291 5.145   13.954  1.00 27.50  ? 261 TRP   B CD1 1 
ATOM   2828 C  CD2 . TRP   B 2 145 ? -34.151 4.914   13.319  1.00 27.15  ? 261 TRP   B CD2 1 
ATOM   2829 N  NE1 . TRP   B 2 145 ? -35.940 3.838   14.124  1.00 29.70  ? 261 TRP   B NE1 1 
ATOM   2830 C  CE2 . TRP   B 2 145 ? -34.638 3.658   13.754  1.00 28.07  ? 261 TRP   B CE2 1 
ATOM   2831 C  CE3 . TRP   B 2 145 ? -32.836 5.002   12.854  1.00 26.29  ? 261 TRP   B CE3 1 
ATOM   2832 C  CZ2 . TRP   B 2 145 ? -33.853 2.511   13.741  1.00 28.44  ? 261 TRP   B CZ2 1 
ATOM   2833 C  CZ3 . TRP   B 2 145 ? -32.045 3.866   12.864  1.00 27.91  ? 261 TRP   B CZ3 1 
ATOM   2834 C  CH2 . TRP   B 2 145 ? -32.565 2.629   13.275  1.00 31.34  ? 261 TRP   B CH2 1 
ATOM   2835 N  N   . ILE   B 2 146 ? -37.153 7.668   16.201  1.00 26.31  ? 262 ILE   B N   1 
ATOM   2836 C  CA  . ILE   B 2 146 ? -37.248 7.448   17.665  1.00 27.88  ? 262 ILE   B CA  1 
ATOM   2837 C  C   . ILE   B 2 146 ? -37.211 5.947   17.925  1.00 27.59  ? 262 ILE   B C   1 
ATOM   2838 O  O   . ILE   B 2 146 ? -38.021 5.235   17.340  1.00 28.21  ? 262 ILE   B O   1 
ATOM   2839 C  CB  . ILE   B 2 146 ? -38.531 8.089   18.196  1.00 29.68  ? 262 ILE   B CB  1 
ATOM   2840 C  CG1 . ILE   B 2 146 ? -38.449 9.611   18.046  1.00 34.10  ? 262 ILE   B CG1 1 
ATOM   2841 C  CG2 . ILE   B 2 146 ? -38.767 7.650   19.630  1.00 32.57  ? 262 ILE   B CG2 1 
ATOM   2842 C  CD1 . ILE   B 2 146 ? -39.752 10.298  18.301  1.00 38.57  ? 262 ILE   B CD1 1 
ATOM   2843 N  N   . LYS   B 2 147 ? -36.247 5.503   18.700  1.00 26.89  ? 263 LYS   B N   1 
ATOM   2844 C  CA  . LYS   B 2 147 ? -36.027 4.053   18.892  1.00 31.66  ? 263 LYS   B CA  1 
ATOM   2845 C  C   . LYS   B 2 147 ? -36.511 3.595   20.278  1.00 31.18  ? 263 LYS   B C   1 
ATOM   2846 O  O   . LYS   B 2 147 ? -36.046 4.134   21.311  1.00 28.26  ? 263 LYS   B O   1 
ATOM   2847 C  CB  . LYS   B 2 147 ? -34.557 3.732   18.710  1.00 32.11  ? 263 LYS   B CB  1 
ATOM   2848 C  CG  . LYS   B 2 147 ? -33.977 4.159   17.374  1.00 32.17  ? 263 LYS   B CG  1 
ATOM   2849 C  CD  . LYS   B 2 147 ? -32.501 3.942   17.453  1.00 33.70  ? 263 LYS   B CD  1 
ATOM   2850 C  CE  . LYS   B 2 147 ? -31.706 4.463   16.289  1.00 34.67  ? 263 LYS   B CE  1 
ATOM   2851 N  NZ  . LYS   B 2 147 ? -30.282 4.370   16.632  1.00 35.63  ? 263 LYS   B NZ  1 
ATOM   2852 N  N   . THR   B 2 148 ? -37.453 2.646   20.288  1.00 32.74  ? 264 THR   B N   1 
ATOM   2853 C  CA  . THR   B 2 148 ? -37.984 2.045   21.547  1.00 33.00  ? 264 THR   B CA  1 
ATOM   2854 C  C   . THR   B 2 148 ? -37.012 0.967   22.049  1.00 36.63  ? 264 THR   B C   1 
ATOM   2855 O  O   . THR   B 2 148 ? -36.197 0.434   21.246  1.00 34.83  ? 264 THR   B O   1 
ATOM   2856 C  CB  . THR   B 2 148 ? -39.402 1.521   21.325  1.00 32.86  ? 264 THR   B CB  1 
ATOM   2857 O  OG1 . THR   B 2 148 ? -39.385 0.602   20.235  1.00 33.05  ? 264 THR   B OG1 1 
ATOM   2858 C  CG2 . THR   B 2 148 ? -40.390 2.629   21.023  1.00 29.50  ? 264 THR   B CG2 1 
ATOM   2859 N  N   . ASN   B 2 149 ? -37.057 0.679   23.346  1.00 32.49  ? 265 ASN   B N   1 
ATOM   2860 C  CA  . ASN   B 2 149 ? -36.249 -0.411  23.935  1.00 32.73  ? 265 ASN   B CA  1 
ATOM   2861 C  C   . ASN   B 2 149 ? -37.182 -1.348  24.710  1.00 34.25  ? 265 ASN   B C   1 
ATOM   2862 O  O   . ASN   B 2 149 ? -36.823 -1.733  25.839  1.00 36.25  ? 265 ASN   B O   1 
ATOM   2863 C  CB  . ASN   B 2 149 ? -35.076 0.103   24.750  1.00 31.42  ? 265 ASN   B CB  1 
ATOM   2864 C  CG  . ASN   B 2 149 ? -35.458 0.845   26.006  1.00 29.82  ? 265 ASN   B CG  1 
ATOM   2865 O  OD1 . ASN   B 2 149 ? -36.598 1.252   26.180  1.00 30.03  ? 265 ASN   B OD1 1 
ATOM   2866 N  ND2 . ASN   B 2 149 ? -34.475 1.044   26.862  1.00 32.41  ? 265 ASN   B ND2 1 
ATOM   2867 N  N   . LYS   B 2 150 ? -38.337 -1.653  24.122  1.00 38.79  ? 266 LYS   B N   1 
ATOM   2868 C  CA  . LYS   B 2 150 ? -39.370 -2.548  24.727  1.00 44.92  ? 266 LYS   B CA  1 
ATOM   2869 C  C   . LYS   B 2 150 ? -38.780 -3.951  24.971  1.00 47.04  ? 266 LYS   B C   1 
ATOM   2870 O  O   . LYS   B 2 150 ? -39.126 -4.562  25.997  1.00 46.69  ? 266 LYS   B O   1 
ATOM   2871 C  CB  . LYS   B 2 150 ? -40.589 -2.716  23.816  1.00 40.82  ? 266 LYS   B CB  1 
ATOM   2872 C  CG  . LYS   B 2 150 ? -41.473 -1.499  23.596  1.00 42.81  ? 266 LYS   B CG  1 
ATOM   2873 C  CD  . LYS   B 2 150 ? -42.647 -1.846  22.718  1.00 49.26  ? 266 LYS   B CD  1 
ATOM   2874 C  CE  . LYS   B 2 150 ? -42.904 -0.873  21.592  1.00 56.45  ? 266 LYS   B CE  1 
ATOM   2875 N  NZ  . LYS   B 2 150 ? -43.545 0.358   22.094  1.00 63.34  ? 266 LYS   B NZ  1 
ATOM   2876 N  N   . ASN   B 2 151 ? -37.955 -4.459  24.055  1.00 49.68  ? 267 ASN   B N   1 
ATOM   2877 C  CA  . ASN   B 2 151 ? -37.457 -5.862  24.102  1.00 51.58  ? 267 ASN   B CA  1 
ATOM   2878 C  C   . ASN   B 2 151 ? -36.287 -5.971  25.078  1.00 55.81  ? 267 ASN   B C   1 
ATOM   2879 O  O   . ASN   B 2 151 ? -35.997 -7.089  25.505  1.00 64.88  ? 267 ASN   B O   1 
ATOM   2880 C  CB  . ASN   B 2 151 ? -37.053 -6.407  22.732  1.00 50.89  ? 267 ASN   B CB  1 
ATOM   2881 C  CG  . ASN   B 2 151 ? -38.171 -6.330  21.718  1.00 51.41  ? 267 ASN   B CG  1 
ATOM   2882 O  OD1 . ASN   B 2 151 ? -37.916 -6.258  20.517  1.00 62.17  ? 267 ASN   B OD1 1 
ATOM   2883 N  ND2 . ASN   B 2 151 ? -39.411 -6.292  22.184  1.00 56.92  ? 267 ASN   B ND2 1 
ATOM   2884 N  N   . ASN   B 2 152 ? -35.637 -4.870  25.444  1.00 55.66  ? 268 ASN   B N   1 
ATOM   2885 C  CA  . ASN   B 2 152 ? -34.407 -4.964  26.264  1.00 55.75  ? 268 ASN   B CA  1 
ATOM   2886 C  C   . ASN   B 2 152 ? -34.190 -3.657  27.018  1.00 54.94  ? 268 ASN   B C   1 
ATOM   2887 O  O   . ASN   B 2 152 ? -33.194 -2.968  26.807  1.00 63.91  ? 268 ASN   B O   1 
ATOM   2888 C  CB  . ASN   B 2 152 ? -33.243 -5.385  25.368  1.00 60.32  ? 268 ASN   B CB  1 
ATOM   2889 C  CG  . ASN   B 2 152 ? -31.908 -5.327  26.072  1.00 70.52  ? 268 ASN   B CG  1 
ATOM   2890 O  OD1 . ASN   B 2 152 ? -31.804 -5.671  27.250  1.00 75.48  ? 268 ASN   B OD1 1 
ATOM   2891 N  ND2 . ASN   B 2 152 ? -30.887 -4.875  25.364  1.00 77.72  ? 268 ASN   B ND2 1 
ATOM   2892 N  N   . PRO   B 2 153 ? -35.104 -3.282  27.940  1.00 55.56  ? 269 PRO   B N   1 
ATOM   2893 C  CA  . PRO   B 2 153 ? -34.945 -2.056  28.726  1.00 56.91  ? 269 PRO   B CA  1 
ATOM   2894 C  C   . PRO   B 2 153 ? -33.717 -2.036  29.647  1.00 58.02  ? 269 PRO   B C   1 
ATOM   2895 O  O   . PRO   B 2 153 ? -33.349 -0.953  30.098  1.00 60.55  ? 269 PRO   B O   1 
ATOM   2896 C  CB  . PRO   B 2 153 ? -36.220 -1.997  29.575  1.00 57.77  ? 269 PRO   B CB  1 
ATOM   2897 C  CG  . PRO   B 2 153 ? -36.695 -3.441  29.636  1.00 58.40  ? 269 PRO   B CG  1 
ATOM   2898 C  CD  . PRO   B 2 153 ? -36.336 -4.013  28.283  1.00 57.52  ? 269 PRO   B CD  1 
ATOM   2899 N  N   . GLY   B 2 154 ? -33.109 -3.201  29.888  1.00 68.28  ? 270 GLY   B N   1 
ATOM   2900 C  CA  . GLY   B 2 154 ? -32.001 -3.392  30.845  1.00 82.55  ? 270 GLY   B CA  1 
ATOM   2901 C  C   . GLY   B 2 154 ? -30.639 -3.448  30.169  1.00 94.11  ? 270 GLY   B C   1 
ATOM   2902 O  O   . GLY   B 2 154 ? -29.818 -4.309  30.568  1.00 91.97  ? 270 GLY   B O   1 
ATOM   2903 N  N   . LYS   B 2 155 ? -30.401 -2.573  29.186  1.00 102.37 ? 271 LYS   B N   1 
ATOM   2904 C  CA  . LYS   B 2 155 ? -29.073 -2.376  28.551  1.00 103.46 ? 271 LYS   B CA  1 
ATOM   2905 C  C   . LYS   B 2 155 ? -28.685 -0.902  28.699  1.00 107.44 ? 271 LYS   B C   1 
ATOM   2906 O  O   . LYS   B 2 155 ? -29.591 -0.043  28.741  1.00 100.34 ? 271 LYS   B O   1 
ATOM   2907 C  CB  . LYS   B 2 155 ? -29.080 -2.849  27.092  1.00 105.97 ? 271 LYS   B CB  1 
ATOM   2908 C  CG  . LYS   B 2 155 ? -27.740 -2.760  26.364  1.00 113.11 ? 271 LYS   B CG  1 
ATOM   2909 C  CD  . LYS   B 2 155 ? -26.646 -3.655  26.941  1.00 117.77 ? 271 LYS   B CD  1 
ATOM   2910 C  CE  . LYS   B 2 155 ? -25.242 -3.121  26.730  1.00 117.33 ? 271 LYS   B CE  1 
ATOM   2911 N  NZ  . LYS   B 2 155 ? -24.837 -3.166  25.305  1.00 117.43 ? 271 LYS   B NZ  1 
ATOM   2912 N  N   . THR   B 2 156 ? -27.377 -0.650  28.789  1.00 113.09 ? 272 THR   B N   1 
ATOM   2913 C  CA  . THR   B 2 156 ? -26.748 0.648   29.147  1.00 116.81 ? 272 THR   B CA  1 
ATOM   2914 C  C   . THR   B 2 156 ? -25.707 0.990   28.071  1.00 116.72 ? 272 THR   B C   1 
ATOM   2915 O  O   . THR   B 2 156 ? -24.644 0.330   28.039  1.00 117.93 ? 272 THR   B O   1 
ATOM   2916 C  CB  . THR   B 2 156 ? -26.171 0.587   30.573  1.00 121.83 ? 272 THR   B CB  1 
ATOM   2917 O  OG1 . THR   B 2 156 ? -25.212 1.634   30.730  1.00 127.65 ? 272 THR   B OG1 1 
ATOM   2918 C  CG2 . THR   B 2 156 ? -25.517 -0.736  30.919  1.00 115.84 ? 272 THR   B CG2 1 
ATOM   2919 N  N   . LYS   B 2 157 ? -26.011 1.958   27.204  1.00 103.81 ? 273 LYS   B N   1 
ATOM   2920 C  CA  . LYS   B 2 157 ? -25.104 2.365   26.100  1.00 101.49 ? 273 LYS   B CA  1 
ATOM   2921 C  C   . LYS   B 2 157 ? -23.979 3.220   26.673  1.00 91.90  ? 273 LYS   B C   1 
ATOM   2922 O  O   . LYS   B 2 157 ? -24.260 4.032   27.564  1.00 97.00  ? 273 LYS   B O   1 
ATOM   2923 C  CB  . LYS   B 2 157 ? -25.848 3.153   25.020  1.00 107.28 ? 273 LYS   B CB  1 
ATOM   2924 C  CG  . LYS   B 2 157 ? -26.804 2.329   24.172  1.00 110.37 ? 273 LYS   B CG  1 
ATOM   2925 C  CD  . LYS   B 2 157 ? -26.905 2.816   22.747  1.00 111.63 ? 273 LYS   B CD  1 
ATOM   2926 C  CE  . LYS   B 2 157 ? -27.874 1.995   21.928  1.00 112.13 ? 273 LYS   B CE  1 
ATOM   2927 N  NZ  . LYS   B 2 157 ? -27.582 2.073   20.477  1.00 114.42 ? 273 LYS   B NZ  1 
ATOM   2928 N  N   . THR   B 2 158 ? -22.759 3.034   26.170  1.00 91.21  ? 274 THR   B N   1 
ATOM   2929 C  CA  . THR   B 2 158 ? -21.596 3.920   26.441  1.00 92.76  ? 274 THR   B CA  1 
ATOM   2930 C  C   . THR   B 2 158 ? -21.927 5.310   25.865  1.00 88.47  ? 274 THR   B C   1 
ATOM   2931 O  O   . THR   B 2 158 ? -22.251 5.399   24.660  1.00 92.40  ? 274 THR   B O   1 
ATOM   2932 C  CB  . THR   B 2 158 ? -20.285 3.269   25.960  1.00 95.68  ? 274 THR   B CB  1 
ATOM   2933 O  OG1 . THR   B 2 158 ? -19.211 4.146   26.301  1.00 94.77  ? 274 THR   B OG1 1 
ATOM   2934 C  CG2 . THR   B 2 158 ? -20.236 2.959   24.477  1.00 97.23  ? 274 THR   B CG2 1 
ATOM   2935 N  N   . LEU   B 2 159 ? -21.901 6.344   26.711  1.00 74.66  ? 275 LEU   B N   1 
ATOM   2936 C  CA  . LEU   B 2 159 ? -22.269 7.736   26.343  1.00 72.62  ? 275 LEU   B CA  1 
ATOM   2937 C  C   . LEU   B 2 159 ? -21.139 8.371   25.516  1.00 69.41  ? 275 LEU   B C   1 
ATOM   2938 O  O   . LEU   B 2 159 ? -19.973 8.283   25.937  1.00 73.33  ? 275 LEU   B O   1 
ATOM   2939 C  CB  . LEU   B 2 159 ? -22.519 8.522   27.637  1.00 76.40  ? 275 LEU   B CB  1 
ATOM   2940 C  CG  . LEU   B 2 159 ? -23.508 9.679   27.528  1.00 78.05  ? 275 LEU   B CG  1 
ATOM   2941 C  CD1 . LEU   B 2 159 ? -24.938 9.162   27.486  1.00 80.20  ? 275 LEU   B CD1 1 
ATOM   2942 C  CD2 . LEU   B 2 159 ? -23.337 10.673  28.668  1.00 74.57  ? 275 LEU   B CD2 1 
ATOM   2943 N  N   . ASP   B 2 160 ? -21.465 9.009   24.387  1.00 70.52  ? 276 ASP   B N   1 
ATOM   2944 C  CA  . ASP   B 2 160 ? -20.560 9.955   23.668  1.00 66.66  ? 276 ASP   B CA  1 
ATOM   2945 C  C   . ASP   B 2 160 ? -20.058 11.026  24.641  1.00 61.31  ? 276 ASP   B C   1 
ATOM   2946 O  O   . ASP   B 2 160 ? -20.827 11.506  25.470  1.00 58.05  ? 276 ASP   B O   1 
ATOM   2947 C  CB  . ASP   B 2 160 ? -21.284 10.661  22.525  1.00 65.07  ? 276 ASP   B CB  1 
ATOM   2948 C  CG  . ASP   B 2 160 ? -20.342 11.492  21.682  1.00 66.77  ? 276 ASP   B CG  1 
ATOM   2949 O  OD1 . ASP   B 2 160 ? -19.614 10.862  20.898  1.00 88.09  ? 276 ASP   B OD1 1 
ATOM   2950 O  OD2 . ASP   B 2 160 ? -20.289 12.752  21.863  1.00 56.02  ? 276 ASP   B OD2 1 
ATOM   2951 N  N   . PRO   B 2 161 ? -18.781 11.476  24.562  1.00 61.91  ? 277 PRO   B N   1 
ATOM   2952 C  CA  . PRO   B 2 161 ? -18.167 12.244  25.648  1.00 57.99  ? 277 PRO   B CA  1 
ATOM   2953 C  C   . PRO   B 2 161 ? -18.848 13.598  25.851  1.00 53.11  ? 277 PRO   B C   1 
ATOM   2954 O  O   . PRO   B 2 161 ? -18.914 14.047  26.972  1.00 53.64  ? 277 PRO   B O   1 
ATOM   2955 C  CB  . PRO   B 2 161 ? -16.717 12.502  25.210  1.00 60.92  ? 277 PRO   B CB  1 
ATOM   2956 C  CG  . PRO   B 2 161 ? -16.502 11.579  24.028  1.00 62.78  ? 277 PRO   B CG  1 
ATOM   2957 C  CD  . PRO   B 2 161 ? -17.870 11.346  23.413  1.00 63.20  ? 277 PRO   B CD  1 
ATOM   2958 N  N   . LYS   B 2 162 ? -19.341 14.195  24.766  1.00 45.74  ? 278 LYS   B N   1 
ATOM   2959 C  CA  . LYS   B 2 162 ? -20.005 15.527  24.801  1.00 51.60  ? 278 LYS   B CA  1 
ATOM   2960 C  C   . LYS   B 2 162 ? -21.468 15.390  25.248  1.00 40.77  ? 278 LYS   B C   1 
ATOM   2961 O  O   . LYS   B 2 162 ? -22.018 16.415  25.680  1.00 39.90  ? 278 LYS   B O   1 
ATOM   2962 C  CB  . LYS   B 2 162 ? -19.922 16.191  23.422  1.00 52.08  ? 278 LYS   B CB  1 
ATOM   2963 C  CG  . LYS   B 2 162 ? -18.499 16.490  22.988  1.00 57.50  ? 278 LYS   B CG  1 
ATOM   2964 C  CD  . LYS   B 2 162 ? -18.390 17.305  21.725  1.00 57.96  ? 278 LYS   B CD  1 
ATOM   2965 C  CE  . LYS   B 2 162 ? -17.121 18.128  21.708  1.00 57.70  ? 278 LYS   B CE  1 
ATOM   2966 N  NZ  . LYS   B 2 162 ? -16.829 18.602  20.338  1.00 60.19  ? 278 LYS   B NZ  1 
ATOM   2967 N  N   . ALA   B 2 163 ? -22.046 14.186  25.171  1.00 38.70  ? 279 ALA   B N   1 
ATOM   2968 C  CA  . ALA   B 2 163 ? -23.493 13.922  25.403  1.00 35.63  ? 279 ALA   B CA  1 
ATOM   2969 C  C   . ALA   B 2 163 ? -23.905 14.306  26.834  1.00 36.89  ? 279 ALA   B C   1 
ATOM   2970 O  O   . ALA   B 2 163 ? -23.156 14.080  27.807  1.00 39.33  ? 279 ALA   B O   1 
ATOM   2971 C  CB  . ALA   B 2 163 ? -23.843 12.490  25.099  1.00 38.46  ? 279 ALA   B CB  1 
ATOM   2972 N  N   . VAL   B 2 164 ? -25.074 14.930  26.950  1.00 35.99  ? 280 VAL   B N   1 
ATOM   2973 C  CA  . VAL   B 2 164 ? -25.672 15.313  28.255  1.00 34.04  ? 280 VAL   B CA  1 
ATOM   2974 C  C   . VAL   B 2 164 ? -26.699 14.232  28.613  1.00 31.14  ? 280 VAL   B C   1 
ATOM   2975 O  O   . VAL   B 2 164 ? -26.888 13.950  29.805  1.00 38.65  ? 280 VAL   B O   1 
ATOM   2976 C  CB  . VAL   B 2 164 ? -26.298 16.721  28.144  1.00 35.20  ? 280 VAL   B CB  1 
ATOM   2977 C  CG1 . VAL   B 2 164 ? -26.807 17.216  29.477  1.00 34.64  ? 280 VAL   B CG1 1 
ATOM   2978 C  CG2 . VAL   B 2 164 ? -25.295 17.715  27.570  1.00 35.92  ? 280 VAL   B CG2 1 
ATOM   2979 N  N   . PHE   B 2 165 ? -27.325 13.669  27.583  1.00 31.05  ? 281 PHE   B N   1 
ATOM   2980 C  CA  . PHE   B 2 165 ? -28.476 12.758  27.672  1.00 28.13  ? 281 PHE   B CA  1 
ATOM   2981 C  C   . PHE   B 2 165 ? -28.113 11.491  26.908  1.00 32.90  ? 281 PHE   B C   1 
ATOM   2982 O  O   . PHE   B 2 165 ? -27.239 11.498  26.003  1.00 30.62  ? 281 PHE   B O   1 
ATOM   2983 C  CB  . PHE   B 2 165 ? -29.718 13.458  27.130  1.00 30.75  ? 281 PHE   B CB  1 
ATOM   2984 C  CG  . PHE   B 2 165 ? -30.069 14.689  27.927  1.00 29.57  ? 281 PHE   B CG  1 
ATOM   2985 C  CD1 . PHE   B 2 165 ? -30.615 14.571  29.184  1.00 26.81  ? 281 PHE   B CD1 1 
ATOM   2986 C  CD2 . PHE   B 2 165 ? -29.782 15.958  27.460  1.00 29.59  ? 281 PHE   B CD2 1 
ATOM   2987 C  CE1 . PHE   B 2 165 ? -30.919 15.682  29.956  1.00 28.88  ? 281 PHE   B CE1 1 
ATOM   2988 C  CE2 . PHE   B 2 165 ? -30.078 17.071  28.232  1.00 30.95  ? 281 PHE   B CE2 1 
ATOM   2989 C  CZ  . PHE   B 2 165 ? -30.645 16.935  29.478  1.00 30.82  ? 281 PHE   B CZ  1 
ATOM   2990 N  N   . GLN   B 2 166 ? -28.746 10.402  27.311  1.00 32.96  ? 282 GLN   B N   1 
ATOM   2991 C  CA  . GLN   B 2 166 ? -28.764 9.158   26.534  1.00 30.94  ? 282 GLN   B CA  1 
ATOM   2992 C  C   . GLN   B 2 166 ? -29.423 9.480   25.211  1.00 29.16  ? 282 GLN   B C   1 
ATOM   2993 O  O   . GLN   B 2 166 ? -30.550 9.945   25.236  1.00 28.82  ? 282 GLN   B O   1 
ATOM   2994 C  CB  . GLN   B 2 166 ? -29.524 8.097   27.320  1.00 30.55  ? 282 GLN   B CB  1 
ATOM   2995 C  CG  . GLN   B 2 166 ? -28.722 7.695   28.539  1.00 36.27  ? 282 GLN   B CG  1 
ATOM   2996 C  CD  . GLN   B 2 166 ? -29.232 6.415   29.158  1.00 43.77  ? 282 GLN   B CD  1 
ATOM   2997 O  OE1 . GLN   B 2 166 ? -29.459 5.419   28.474  1.00 41.48  ? 282 GLN   B OE1 1 
ATOM   2998 N  NE2 . GLN   B 2 166 ? -29.438 6.452   30.463  1.00 46.51  ? 282 GLN   B NE2 1 
ATOM   2999 N  N   . ARG   B 2 167 ? -28.756 9.165   24.104  1.00 28.99  ? 283 ARG   B N   1 
ATOM   3000 C  CA  . ARG   B 2 167 ? -29.298 9.434   22.748  1.00 30.19  ? 283 ARG   B CA  1 
ATOM   3001 C  C   . ARG   B 2 167 ? -30.097 8.219   22.289  1.00 27.59  ? 283 ARG   B C   1 
ATOM   3002 O  O   . ARG   B 2 167 ? -29.496 7.112   22.173  1.00 31.34  ? 283 ARG   B O   1 
ATOM   3003 C  CB  . ARG   B 2 167 ? -28.154 9.791   21.786  1.00 31.24  ? 283 ARG   B CB  1 
ATOM   3004 C  CG  . ARG   B 2 167 ? -27.430 11.053  22.234  1.00 33.31  ? 283 ARG   B CG  1 
ATOM   3005 C  CD  . ARG   B 2 167 ? -26.410 11.575  21.248  1.00 35.69  ? 283 ARG   B CD  1 
ATOM   3006 N  NE  . ARG   B 2 167 ? -25.791 12.829  21.696  1.00 35.37  ? 283 ARG   B NE  1 
ATOM   3007 C  CZ  . ARG   B 2 167 ? -24.582 13.237  21.356  1.00 36.47  ? 283 ARG   B CZ  1 
ATOM   3008 N  NH1 . ARG   B 2 167 ? -23.838 12.474  20.562  1.00 34.39  ? 283 ARG   B NH1 1 
ATOM   3009 N  NH2 . ARG   B 2 167 ? -24.102 14.381  21.839  1.00 34.28  ? 283 ARG   B NH2 1 
ATOM   3010 N  N   . THR   B 2 168 ? -31.354 8.434   21.931  1.00 26.45  ? 284 THR   B N   1 
ATOM   3011 C  CA  . THR   B 2 168 ? -32.312 7.349   21.607  1.00 28.62  ? 284 THR   B CA  1 
ATOM   3012 C  C   . THR   B 2 168 ? -32.979 7.597   20.252  1.00 28.16  ? 284 THR   B C   1 
ATOM   3013 O  O   . THR   B 2 168 ? -34.007 6.964   19.937  1.00 28.01  ? 284 THR   B O   1 
ATOM   3014 C  CB  . THR   B 2 168 ? -33.273 7.191   22.791  1.00 29.90  ? 284 THR   B CB  1 
ATOM   3015 O  OG1 . THR   B 2 168 ? -34.070 8.355   22.947  1.00 27.07  ? 284 THR   B OG1 1 
ATOM   3016 C  CG2 . THR   B 2 168 ? -32.526 6.973   24.084  1.00 29.61  ? 284 THR   B CG2 1 
ATOM   3017 N  N   . LYS   B 2 169 ? -32.407 8.462   19.415  1.00 26.48  ? 285 LYS   B N   1 
ATOM   3018 C  CA  . LYS   B 2 169 ? -33.017 8.804   18.115  1.00 26.06  ? 285 LYS   B CA  1 
ATOM   3019 C  C   . LYS   B 2 169 ? -31.906 9.142   17.116  1.00 24.95  ? 285 LYS   B C   1 
ATOM   3020 O  O   . LYS   B 2 169 ? -30.748 9.340   17.524  1.00 24.99  ? 285 LYS   B O   1 
ATOM   3021 C  CB  . LYS   B 2 169 ? -33.977 9.981   18.245  1.00 26.76  ? 285 LYS   B CB  1 
ATOM   3022 C  CG  . LYS   B 2 169 ? -33.320 11.179  18.915  1.00 26.63  ? 285 LYS   B CG  1 
ATOM   3023 C  CD  . LYS   B 2 169 ? -34.053 12.453  18.816  1.00 30.02  ? 285 LYS   B CD  1 
ATOM   3024 C  CE  . LYS   B 2 169 ? -33.421 13.515  19.708  1.00 28.59  ? 285 LYS   B CE  1 
ATOM   3025 N  NZ  . LYS   B 2 169 ? -32.136 14.007  19.165  1.00 27.92  ? 285 LYS   B NZ  1 
ATOM   3026 N  N   . GLU   B 2 170 ? -32.272 9.126   15.852  1.00 26.35  ? 286 GLU   B N   1 
ATOM   3027 C  CA  . GLU   B 2 170 ? -31.438 9.653   14.737  1.00 27.70  ? 286 GLU   B CA  1 
ATOM   3028 C  C   . GLU   B 2 170 ? -32.287 10.597  13.910  1.00 26.80  ? 286 GLU   B C   1 
ATOM   3029 O  O   . GLU   B 2 170 ? -33.503 10.450  13.855  1.00 26.81  ? 286 GLU   B O   1 
ATOM   3030 C  CB  . GLU   B 2 170 ? -30.931 8.529   13.847  1.00 26.78  ? 286 GLU   B CB  1 
ATOM   3031 C  CG  . GLU   B 2 170 ? -30.084 7.533   14.601  1.00 26.54  ? 286 GLU   B CG  1 
ATOM   3032 C  CD  . GLU   B 2 170 ? -29.569 6.375   13.759  1.00 28.75  ? 286 GLU   B CD  1 
ATOM   3033 O  OE1 . GLU   B 2 170 ? -29.490 6.549   12.549  1.00 26.80  ? 286 GLU   B OE1 1 
ATOM   3034 O  OE2 . GLU   B 2 170 ? -29.221 5.305   14.351  1.00 28.24  ? 286 GLU   B OE2 1 
ATOM   3035 N  N   . HIS   B 2 171 ? -31.632 11.526  13.219  1.00 24.25  ? 287 HIS   B N   1 
ATOM   3036 C  CA  . HIS   B 2 171 ? -32.339 12.552  12.443  1.00 21.51  ? 287 HIS   B CA  1 
ATOM   3037 C  C   . HIS   B 2 171 ? -32.023 12.341  10.981  1.00 21.85  ? 287 HIS   B C   1 
ATOM   3038 O  O   . HIS   B 2 171 ? -30.843 12.138  10.653  1.00 21.93  ? 287 HIS   B O   1 
ATOM   3039 C  CB  . HIS   B 2 171 ? -31.894 13.963  12.899  1.00 23.77  ? 287 HIS   B CB  1 
ATOM   3040 C  CG  . HIS   B 2 171 ? -32.299 14.333  14.283  1.00 23.63  ? 287 HIS   B CG  1 
ATOM   3041 N  ND1 . HIS   B 2 171 ? -33.260 15.309  14.553  1.00 24.43  ? 287 HIS   B ND1 1 
ATOM   3042 C  CD2 . HIS   B 2 171 ? -31.835 13.901  15.476  1.00 24.50  ? 287 HIS   B CD2 1 
ATOM   3043 C  CE1 . HIS   B 2 171 ? -33.334 15.439  15.859  1.00 24.69  ? 287 HIS   B CE1 1 
ATOM   3044 N  NE2 . HIS   B 2 171 ? -32.503 14.573  16.444  1.00 21.95  ? 287 HIS   B NE2 1 
ATOM   3045 N  N   . CYS   B 2 172 ? -33.039 12.480  10.157  1.00 24.00  ? 288 CYS   B N   1 
ATOM   3046 C  CA  . CYS   B 2 172 ? -32.937 12.524  8.682   1.00 24.17  ? 288 CYS   B CA  1 
ATOM   3047 C  C   . CYS   B 2 172 ? -33.447 13.895  8.274   1.00 25.04  ? 288 CYS   B C   1 
ATOM   3048 O  O   . CYS   B 2 172 ? -34.640 14.170  8.466   1.00 26.21  ? 288 CYS   B O   1 
ATOM   3049 C  CB  . CYS   B 2 172 ? -33.716 11.374  8.050   1.00 25.28  ? 288 CYS   B CB  1 
ATOM   3050 S  SG  . CYS   B 2 172 ? -33.534 11.300  6.260   1.00 25.34  ? 288 CYS   B SG  1 
ATOM   3051 N  N   . LEU   B 2 173 ? -32.531 14.768  7.832   1.00 23.49  ? 289 LEU   B N   1 
ATOM   3052 C  CA  . LEU   B 2 173 ? -32.894 16.138  7.369   1.00 22.23  ? 289 LEU   B CA  1 
ATOM   3053 C  C   . LEU   B 2 173 ? -33.356 16.100  5.928   1.00 23.67  ? 289 LEU   B C   1 
ATOM   3054 O  O   . LEU   B 2 173 ? -32.646 15.518  5.064   1.00 24.73  ? 289 LEU   B O   1 
ATOM   3055 C  CB  . LEU   B 2 173 ? -31.688 17.061  7.533   1.00 20.97  ? 289 LEU   B CB  1 
ATOM   3056 C  CG  . LEU   B 2 173 ? -31.089 17.055  8.930   1.00 23.32  ? 289 LEU   B CG  1 
ATOM   3057 C  CD1 . LEU   B 2 173 ? -29.946 18.072  9.050   1.00 25.74  ? 289 LEU   B CD1 1 
ATOM   3058 C  CD2 . LEU   B 2 173 ? -32.155 17.353  9.961   1.00 27.45  ? 289 LEU   B CD2 1 
ATOM   3059 N  N   . MET   B 2 174 ? -34.483 16.757  5.683   1.00 20.45  ? 290 MET   B N   1 
ATOM   3060 C  CA  . MET   B 2 174 ? -35.014 16.995  4.348   1.00 22.47  ? 290 MET   B CA  1 
ATOM   3061 C  C   . MET   B 2 174 ? -34.628 18.395  3.847   1.00 24.65  ? 290 MET   B C   1 
ATOM   3062 O  O   . MET   B 2 174 ? -34.918 19.393  4.528   1.00 24.54  ? 290 MET   B O   1 
ATOM   3063 C  CB  . MET   B 2 174 ? -36.519 16.853  4.368   1.00 24.36  ? 290 MET   B CB  1 
ATOM   3064 C  CG  . MET   B 2 174 ? -37.135 16.980  3.015   1.00 27.67  ? 290 MET   B CG  1 
ATOM   3065 S  SD  . MET   B 2 174 ? -38.931 16.868  3.248   1.00 30.19  ? 290 MET   B SD  1 
ATOM   3066 C  CE  . MET   B 2 174 ? -39.485 17.220  1.595   1.00 27.27  ? 290 MET   B CE  1 
ATOM   3067 N  N   . GLY   B 2 175 ? -34.074 18.437  2.637   1.00 26.19  ? 291 GLY   B N   1 
ATOM   3068 C  CA  . GLY   B 2 175 ? -33.682 19.689  1.983   1.00 25.20  ? 291 GLY   B CA  1 
ATOM   3069 C  C   . GLY   B 2 175 ? -34.420 19.839  0.703   1.00 25.56  ? 291 GLY   B C   1 
ATOM   3070 O  O   . GLY   B 2 175 ? -34.735 18.795  0.035   1.00 23.91  ? 291 GLY   B O   1 
ATOM   3071 N  N   . ILE   B 2 176 ? -34.683 21.093  0.332   1.00 24.32  ? 292 ILE   B N   1 
ATOM   3072 C  CA  . ILE   B 2 176 ? -35.341 21.442  -0.951  1.00 23.80  ? 292 ILE   B CA  1 
ATOM   3073 C  C   . ILE   B 2 176 ? -34.467 22.457  -1.683  1.00 24.20  ? 292 ILE   B C   1 
ATOM   3074 O  O   . ILE   B 2 176 ? -33.922 23.365  -1.027  1.00 27.58  ? 292 ILE   B O   1 
ATOM   3075 C  CB  . ILE   B 2 176 ? -36.769 21.981  -0.753  1.00 28.67  ? 292 ILE   B CB  1 
ATOM   3076 C  CG1 . ILE   B 2 176 ? -37.416 22.310  -2.100  1.00 29.92  ? 292 ILE   B CG1 1 
ATOM   3077 C  CG2 . ILE   B 2 176 ? -36.807 23.182  0.167   1.00 30.06  ? 292 ILE   B CG2 1 
ATOM   3078 C  CD1 . ILE   B 2 176 ? -38.919 22.521  -2.001  1.00 36.54  ? 292 ILE   B CD1 1 
ATOM   3079 N  N   . LYS   B 2 177 ? -34.357 22.311  -2.985  1.00 26.85  ? 293 LYS   B N   1 
ATOM   3080 C  CA  . LYS   B 2 177 ? -33.773 23.338  -3.877  1.00 33.22  ? 293 LYS   B CA  1 
ATOM   3081 C  C   . LYS   B 2 177 ? -34.779 23.635  -4.972  1.00 34.20  ? 293 LYS   B C   1 
ATOM   3082 O  O   . LYS   B 2 177 ? -35.511 22.719  -5.399  1.00 31.34  ? 293 LYS   B O   1 
ATOM   3083 C  CB  . LYS   B 2 177 ? -32.408 22.964  -4.422  1.00 32.69  ? 293 LYS   B CB  1 
ATOM   3084 C  CG  . LYS   B 2 177 ? -32.323 21.950  -5.540  1.00 41.34  ? 293 LYS   B CG  1 
ATOM   3085 C  CD  . LYS   B 2 177 ? -30.973 22.048  -6.251  1.00 41.25  ? 293 LYS   B CD  1 
ATOM   3086 C  CE  . LYS   B 2 177 ? -29.812 21.776  -5.327  1.00 38.90  ? 293 LYS   B CE  1 
ATOM   3087 N  NZ  . LYS   B 2 177 ? -28.561 22.386  -5.831  1.00 40.43  ? 293 LYS   B NZ  1 
ATOM   3088 N  N   . GLY   B 2 178 ? -34.788 24.896  -5.388  1.00 38.37  ? 294 GLY   B N   1 
ATOM   3089 C  CA  . GLY   B 2 178 ? -35.799 25.440  -6.307  1.00 45.18  ? 294 GLY   B CA  1 
ATOM   3090 C  C   . GLY   B 2 178 ? -37.064 25.824  -5.561  1.00 51.87  ? 294 GLY   B C   1 
ATOM   3091 O  O   . GLY   B 2 178 ? -37.042 25.843  -4.300  1.00 57.73  ? 294 GLY   B O   1 
ATOM   3092 N  N   . THR   B 2 179 ? -38.134 26.089  -6.316  1.00 69.66  ? 295 THR   B N   1 
ATOM   3093 C  CA  . THR   B 2 179 ? -39.431 26.640  -5.839  1.00 84.23  ? 295 THR   B CA  1 
ATOM   3094 C  C   . THR   B 2 179 ? -40.324 25.542  -5.242  1.00 92.76  ? 295 THR   B C   1 
ATOM   3095 O  O   . THR   B 2 179 ? -40.137 24.354  -5.593  1.00 93.91  ? 295 THR   B O   1 
ATOM   3096 C  CB  . THR   B 2 179 ? -40.164 27.333  -6.992  1.00 83.66  ? 295 THR   B CB  1 
ATOM   3097 O  OG1 . THR   B 2 179 ? -40.429 26.310  -7.951  1.00 82.73  ? 295 THR   B OG1 1 
ATOM   3098 C  CG2 . THR   B 2 179 ? -39.364 28.462  -7.607  1.00 82.69  ? 295 THR   B CG2 1 
ATOM   3099 N  N   . VAL   B 2 180 ? -41.269 25.954  -4.388  1.00 99.12  ? 296 VAL   B N   1 
ATOM   3100 C  CA  . VAL   B 2 180 ? -42.348 25.109  -3.791  1.00 97.56  ? 296 VAL   B CA  1 
ATOM   3101 C  C   . VAL   B 2 180 ? -43.606 25.263  -4.658  1.00 97.44  ? 296 VAL   B C   1 
ATOM   3102 O  O   . VAL   B 2 180 ? -44.395 24.300  -4.699  1.00 92.48  ? 296 VAL   B O   1 
ATOM   3103 C  CB  . VAL   B 2 180 ? -42.620 25.508  -2.326  1.00 94.06  ? 296 VAL   B CB  1 
ATOM   3104 C  CG1 . VAL   B 2 180 ? -43.637 24.585  -1.664  1.00 94.14  ? 296 VAL   B CG1 1 
ATOM   3105 C  CG2 . VAL   B 2 180 ? -41.331 25.576  -1.515  1.00 92.97  ? 296 VAL   B CG2 1 
ATOM   3106 N  N   . ILE   B 2 189 ? -55.049 14.473  -5.706  1.00 110.30 ? 305 ILE   B N   1 
ATOM   3107 C  CA  . ILE   B 2 189 ? -54.382 13.230  -6.204  1.00 114.14 ? 305 ILE   B CA  1 
ATOM   3108 C  C   . ILE   B 2 189 ? -52.951 13.130  -5.639  1.00 120.40 ? 305 ILE   B C   1 
ATOM   3109 O  O   . ILE   B 2 189 ? -52.269 12.140  -5.991  1.00 113.77 ? 305 ILE   B O   1 
ATOM   3110 C  CB  . ILE   B 2 189 ? -54.415 13.154  -7.754  1.00 113.16 ? 305 ILE   B CB  1 
ATOM   3111 C  CG1 . ILE   B 2 189 ? -54.286 14.530  -8.420  1.00 112.65 ? 305 ILE   B CG1 1 
ATOM   3112 C  CG2 . ILE   B 2 189 ? -55.660 12.421  -8.242  1.00 105.37 ? 305 ILE   B CG2 1 
ATOM   3113 C  CD1 . ILE   B 2 189 ? -54.011 14.478  -9.909  1.00 111.37 ? 305 ILE   B CD1 1 
ATOM   3114 N  N   . HIS   B 2 190 ? -52.520 14.073  -4.775  1.00 125.39 ? 306 HIS   B N   1 
ATOM   3115 C  CA  . HIS   B 2 190 ? -51.110 14.251  -4.313  1.00 119.86 ? 306 HIS   B CA  1 
ATOM   3116 C  C   . HIS   B 2 190 ? -51.029 15.150  -3.065  1.00 110.25 ? 306 HIS   B C   1 
ATOM   3117 O  O   . HIS   B 2 190 ? -50.431 16.233  -3.179  1.00 103.77 ? 306 HIS   B O   1 
ATOM   3118 C  CB  . HIS   B 2 190 ? -50.251 14.892  -5.421  1.00 125.33 ? 306 HIS   B CB  1 
ATOM   3119 C  CG  . HIS   B 2 190 ? -50.265 14.195  -6.743  1.00 132.60 ? 306 HIS   B CG  1 
ATOM   3120 N  ND1 . HIS   B 2 190 ? -51.109 14.567  -7.777  1.00 137.03 ? 306 HIS   B ND1 1 
ATOM   3121 C  CD2 . HIS   B 2 190 ? -49.518 13.177  -7.218  1.00 132.27 ? 306 HIS   B CD2 1 
ATOM   3122 C  CE1 . HIS   B 2 190 ? -50.891 13.792  -8.821  1.00 135.16 ? 306 HIS   B CE1 1 
ATOM   3123 N  NE2 . HIS   B 2 190 ? -49.920 12.931  -8.503  1.00 136.07 ? 306 HIS   B NE2 1 
ATOM   3124 N  N   . ALA   B 2 191 ? -51.554 14.718  -1.911  1.00 107.23 ? 307 ALA   B N   1 
ATOM   3125 C  CA  . ALA   B 2 191 ? -51.710 15.547  -0.684  1.00 102.80 ? 307 ALA   B CA  1 
ATOM   3126 C  C   . ALA   B 2 191 ? -50.513 15.380  0.281   1.00 103.18 ? 307 ALA   B C   1 
ATOM   3127 O  O   . ALA   B 2 191 ? -49.379 15.650  -0.170  1.00 103.14 ? 307 ALA   B O   1 
ATOM   3128 C  CB  . ALA   B 2 191 ? -53.036 15.229  -0.037  1.00 101.15 ? 307 ALA   B CB  1 
ATOM   3129 N  N   . ASN   B 2 192 ? -50.742 14.990  1.554   1.00 99.51  ? 308 ASN   B N   1 
ATOM   3130 C  CA  . ASN   B 2 192 ? -49.751 15.042  2.677   1.00 98.82  ? 308 ASN   B CA  1 
ATOM   3131 C  C   . ASN   B 2 192 ? -50.365 14.444  3.964   1.00 90.63  ? 308 ASN   B C   1 
ATOM   3132 O  O   . ASN   B 2 192 ? -51.080 15.181  4.664   1.00 92.26  ? 308 ASN   B O   1 
ATOM   3133 C  CB  . ASN   B 2 192 ? -49.236 16.483  2.868   1.00 99.40  ? 308 ASN   B CB  1 
ATOM   3134 C  CG  . ASN   B 2 192 ? -48.791 16.840  4.276   1.00 91.19  ? 308 ASN   B CG  1 
ATOM   3135 O  OD1 . ASN   B 2 192 ? -48.810 16.007  5.179   1.00 89.57  ? 308 ASN   B OD1 1 
ATOM   3136 N  ND2 . ASN   B 2 192 ? -48.396 18.088  4.483   1.00 89.13  ? 308 ASN   B ND2 1 
ATOM   3137 N  N   . VAL   B 2 193 ? -50.079 13.172  4.291   1.00 77.66  ? 309 VAL   B N   1 
ATOM   3138 C  CA  . VAL   B 2 193 ? -50.666 12.450  5.472   1.00 76.00  ? 309 VAL   B CA  1 
ATOM   3139 C  C   . VAL   B 2 193 ? -49.570 12.072  6.482   1.00 61.59  ? 309 VAL   B C   1 
ATOM   3140 O  O   . VAL   B 2 193 ? -49.947 11.686  7.610   1.00 65.00  ? 309 VAL   B O   1 
ATOM   3141 C  CB  . VAL   B 2 193 ? -51.457 11.176  5.080   1.00 83.32  ? 309 VAL   B CB  1 
ATOM   3142 C  CG1 . VAL   B 2 193 ? -52.496 10.793  6.135   1.00 77.39  ? 309 VAL   B CG1 1 
ATOM   3143 C  CG2 . VAL   B 2 193 ? -52.114 11.280  3.711   1.00 87.35  ? 309 VAL   B CG2 1 
ATOM   3144 N  N   . ASP   B 2 194 ? -48.284 12.157  6.122   1.00 49.52  ? 310 ASP   B N   1 
ATOM   3145 C  CA  . ASP   B 2 194 ? -47.182 11.601  6.952   1.00 41.59  ? 310 ASP   B CA  1 
ATOM   3146 C  C   . ASP   B 2 194 ? -46.744 12.615  8.017   1.00 38.75  ? 310 ASP   B C   1 
ATOM   3147 O  O   . ASP   B 2 194 ? -46.976 13.825  7.866   1.00 37.75  ? 310 ASP   B O   1 
ATOM   3148 C  CB  . ASP   B 2 194 ? -45.986 11.136  6.116   1.00 44.94  ? 310 ASP   B CB  1 
ATOM   3149 C  CG  . ASP   B 2 194 ? -46.154 9.751   5.490   1.00 48.42  ? 310 ASP   B CG  1 
ATOM   3150 O  OD1 . ASP   B 2 194 ? -46.487 8.810   6.224   1.00 39.81  ? 310 ASP   B OD1 1 
ATOM   3151 O  OD2 . ASP   B 2 194 ? -45.938 9.623   4.269   1.00 42.40  ? 310 ASP   B OD2 1 
ATOM   3152 N  N   . ILE   B 2 195 ? -46.104 12.100  9.056   1.00 35.15  ? 311 ILE   B N   1 
ATOM   3153 C  CA  . ILE   B 2 195 ? -45.603 12.891  10.207  1.00 34.25  ? 311 ILE   B CA  1 
ATOM   3154 C  C   . ILE   B 2 195 ? -44.077 12.765  10.239  1.00 32.79  ? 311 ILE   B C   1 
ATOM   3155 O  O   . ILE   B 2 195 ? -43.552 11.784  9.658   1.00 31.06  ? 311 ILE   B O   1 
ATOM   3156 C  CB  . ILE   B 2 195 ? -46.312 12.417  11.482  1.00 37.29  ? 311 ILE   B CB  1 
ATOM   3157 C  CG1 . ILE   B 2 195 ? -46.224 13.466  12.586  1.00 41.23  ? 311 ILE   B CG1 1 
ATOM   3158 C  CG2 . ILE   B 2 195 ? -45.834 11.036  11.933  1.00 37.91  ? 311 ILE   B CG2 1 
ATOM   3159 C  CD1 . ILE   B 2 195 ? -46.929 13.067  13.863  1.00 46.17  ? 311 ILE   B CD1 1 
ATOM   3160 N  N   . ASP   B 2 196 ? -43.389 13.694  10.912  1.00 30.85  ? 312 ASP   B N   1 
ATOM   3161 C  CA  . ASP   B 2 196 ? -41.909 13.808  10.884  1.00 29.07  ? 312 ASP   B CA  1 
ATOM   3162 C  C   . ASP   B 2 196 ? -41.270 12.923  11.965  1.00 29.38  ? 312 ASP   B C   1 
ATOM   3163 O  O   . ASP   B 2 196 ? -40.184 13.254  12.478  1.00 25.73  ? 312 ASP   B O   1 
ATOM   3164 C  CB  . ASP   B 2 196 ? -41.534 15.282  10.965  1.00 31.43  ? 312 ASP   B CB  1 
ATOM   3165 C  CG  . ASP   B 2 196 ? -41.966 15.954  12.258  1.00 35.33  ? 312 ASP   B CG  1 
ATOM   3166 O  OD1 . ASP   B 2 196 ? -42.736 15.312  13.057  1.00 30.62  ? 312 ASP   B OD1 1 
ATOM   3167 O  OD2 . ASP   B 2 196 ? -41.527 17.101  12.463  1.00 33.04  ? 312 ASP   B OD2 1 
ATOM   3168 N  N   . LEU   B 2 197 ? -41.903 11.785  12.260  1.00 29.01  ? 313 LEU   B N   1 
ATOM   3169 C  CA  . LEU   B 2 197 ? -41.487 10.780  13.270  1.00 29.37  ? 313 LEU   B CA  1 
ATOM   3170 C  C   . LEU   B 2 197 ? -41.597 9.386   12.653  1.00 27.71  ? 313 LEU   B C   1 
ATOM   3171 O  O   . LEU   B 2 197 ? -42.639 9.101   12.031  1.00 29.59  ? 313 LEU   B O   1 
ATOM   3172 C  CB  . LEU   B 2 197 ? -42.418 10.851  14.482  1.00 32.50  ? 313 LEU   B CB  1 
ATOM   3173 C  CG  . LEU   B 2 197 ? -42.256 12.100  15.326  1.00 35.99  ? 313 LEU   B CG  1 
ATOM   3174 C  CD1 . LEU   B 2 197 ? -43.257 12.137  16.441  1.00 36.51  ? 313 LEU   B CD1 1 
ATOM   3175 C  CD2 . LEU   B 2 197 ? -40.836 12.168  15.854  1.00 38.30  ? 313 LEU   B CD2 1 
ATOM   3176 N  N   . ILE   B 2 198 ? -40.596 8.569   12.896  1.00 26.75  ? 314 ILE   B N   1 
ATOM   3177 C  CA  . ILE   B 2 198 ? -40.629 7.102   12.675  1.00 26.86  ? 314 ILE   B CA  1 
ATOM   3178 C  C   . ILE   B 2 198 ? -40.307 6.474   14.005  1.00 27.23  ? 314 ILE   B C   1 
ATOM   3179 O  O   . ILE   B 2 198 ? -39.291 6.823   14.618  1.00 25.50  ? 314 ILE   B O   1 
ATOM   3180 C  CB  . ILE   B 2 198 ? -39.612 6.677   11.612  1.00 27.81  ? 314 ILE   B CB  1 
ATOM   3181 C  CG1 . ILE   B 2 198 ? -39.870 7.369   10.271  1.00 26.05  ? 314 ILE   B CG1 1 
ATOM   3182 C  CG2 . ILE   B 2 198 ? -39.578 5.171   11.471  1.00 27.47  ? 314 ILE   B CG2 1 
ATOM   3183 C  CD1 . ILE   B 2 198 ? -38.684 7.242   9.351   1.00 28.12  ? 314 ILE   B CD1 1 
ATOM   3184 N  N   . ILE   B 2 199 ? -41.150 5.548   14.459  1.00 27.87  ? 315 ILE   B N   1 
ATOM   3185 C  CA  . ILE   B 2 199 ? -40.939 4.915   15.782  1.00 30.56  ? 315 ILE   B CA  1 
ATOM   3186 C  C   . ILE   B 2 199 ? -40.764 3.428   15.500  1.00 30.87  ? 315 ILE   B C   1 
ATOM   3187 O  O   . ILE   B 2 199 ? -41.700 2.852   14.943  1.00 32.78  ? 315 ILE   B O   1 
ATOM   3188 C  CB  . ILE   B 2 199 ? -42.121 5.230   16.729  1.00 33.19  ? 315 ILE   B CB  1 
ATOM   3189 C  CG1 . ILE   B 2 199 ? -42.354 6.739   16.854  1.00 32.71  ? 315 ILE   B CG1 1 
ATOM   3190 C  CG2 . ILE   B 2 199 ? -41.874 4.581   18.079  1.00 37.00  ? 315 ILE   B CG2 1 
ATOM   3191 C  CD1 . ILE   B 2 199 ? -43.683 7.165   17.401  1.00 36.42  ? 315 ILE   B CD1 1 
ATOM   3192 N  N   . THR   B 2 200 ? -39.619 2.866   15.843  1.00 32.24  ? 316 THR   B N   1 
ATOM   3193 C  CA  . THR   B 2 200 ? -39.368 1.411   15.728  1.00 32.58  ? 316 THR   B CA  1 
ATOM   3194 C  C   . THR   B 2 200 ? -38.517 0.990   16.911  1.00 34.51  ? 316 THR   B C   1 
ATOM   3195 O  O   . THR   B 2 200 ? -37.911 1.850   17.597  1.00 31.19  ? 316 THR   B O   1 
ATOM   3196 C  CB  . THR   B 2 200 ? -38.687 1.024   14.401  1.00 29.48  ? 316 THR   B CB  1 
ATOM   3197 O  OG1 . THR   B 2 200 ? -37.317 1.390   14.443  1.00 30.09  ? 316 THR   B OG1 1 
ATOM   3198 C  CG2 . THR   B 2 200 ? -39.343 1.617   13.176  1.00 33.27  ? 316 THR   B CG2 1 
ATOM   3199 N  N   . GLU   B 2 201 ? -38.423 -0.314  17.132  1.00 33.44  ? 317 GLU   B N   1 
ATOM   3200 C  CA  . GLU   B 2 201 ? -37.519 -0.837  18.173  1.00 35.60  ? 317 GLU   B CA  1 
ATOM   3201 C  C   . GLU   B 2 201 ? -36.073 -0.620  17.714  1.00 36.35  ? 317 GLU   B C   1 
ATOM   3202 O  O   . GLU   B 2 201 ? -35.781 -0.740  16.503  1.00 38.14  ? 317 GLU   B O   1 
ATOM   3203 C  CB  . GLU   B 2 201 ? -37.802 -2.323  18.430  1.00 36.79  ? 317 GLU   B CB  1 
ATOM   3204 C  CG  . GLU   B 2 201 ? -36.986 -2.883  19.571  1.00 39.03  ? 317 GLU   B CG  1 
ATOM   3205 C  CD  . GLU   B 2 201 ? -37.476 -2.596  20.975  1.00 35.44  ? 317 GLU   B CD  1 
ATOM   3206 O  OE1 . GLU   B 2 201 ? -38.551 -2.000  21.114  1.00 39.06  ? 317 GLU   B OE1 1 
ATOM   3207 O  OE2 . GLU   B 2 201 ? -36.735 -2.923  21.918  1.00 42.60  ? 317 GLU   B OE2 1 
ATOM   3208 N  N   . GLU   B 2 202 ? -35.206 -0.305  18.660  1.00 36.93  ? 318 GLU   B N   1 
ATOM   3209 C  CA  . GLU   B 2 202 ? -33.754 -0.259  18.460  1.00 39.63  ? 318 GLU   B CA  1 
ATOM   3210 C  C   . GLU   B 2 202 ? -33.260 -1.574  17.867  1.00 45.48  ? 318 GLU   B C   1 
ATOM   3211 O  O   . GLU   B 2 202 ? -33.433 -2.636  18.459  1.00 38.34  ? 318 GLU   B O   1 
ATOM   3212 C  CB  . GLU   B 2 202 ? -33.040 -0.019  19.777  1.00 43.08  ? 318 GLU   B CB  1 
ATOM   3213 C  CG  . GLU   B 2 202 ? -31.568 0.197   19.558  1.00 48.19  ? 318 GLU   B CG  1 
ATOM   3214 C  CD  . GLU   B 2 202 ? -30.979 1.082   20.623  1.00 54.04  ? 318 GLU   B CD  1 
ATOM   3215 O  OE1 . GLU   B 2 202 ? -31.278 2.301   20.614  1.00 53.40  ? 318 GLU   B OE1 1 
ATOM   3216 O  OE2 . GLU   B 2 202 ? -30.261 0.537   21.473  1.00 73.77  ? 318 GLU   B OE2 1 
ATOM   3217 N  N   . PRO   B 2 203 ? -32.584 -1.536  16.703  1.00 43.89  ? 319 PRO   B N   1 
ATOM   3218 C  CA  . PRO   B 2 203 ? -32.068 -2.752  16.077  1.00 44.37  ? 319 PRO   B CA  1 
ATOM   3219 C  C   . PRO   B 2 203 ? -31.025 -3.454  16.948  1.00 41.23  ? 319 PRO   B C   1 
ATOM   3220 O  O   . PRO   B 2 203 ? -30.423 -2.803  17.749  1.00 38.97  ? 319 PRO   B O   1 
ATOM   3221 C  CB  . PRO   B 2 203 ? -31.410 -2.244  14.783  1.00 45.01  ? 319 PRO   B CB  1 
ATOM   3222 C  CG  . PRO   B 2 203 ? -32.153 -0.963  14.499  1.00 44.86  ? 319 PRO   B CG  1 
ATOM   3223 C  CD  . PRO   B 2 203 ? -32.355 -0.343  15.871  1.00 42.92  ? 319 PRO   B CD  1 
ATOM   3224 N  N   . GLU   B 2 204 ? -30.823 -4.754  16.750  1.00 41.55  ? 320 GLU   B N   1 
ATOM   3225 C  CA  . GLU   B 2 204 ? -29.694 -5.494  17.379  1.00 50.71  ? 320 GLU   B CA  1 
ATOM   3226 C  C   . GLU   B 2 204 ? -28.396 -4.731  17.118  1.00 51.79  ? 320 GLU   B C   1 
ATOM   3227 O  O   . GLU   B 2 204 ? -28.314 -4.056  16.087  1.00 51.99  ? 320 GLU   B O   1 
ATOM   3228 C  CB  . GLU   B 2 204 ? -29.579 -6.909  16.808  1.00 57.97  ? 320 GLU   B CB  1 
ATOM   3229 C  CG  . GLU   B 2 204 ? -30.676 -7.844  17.282  1.00 73.85  ? 320 GLU   B CG  1 
ATOM   3230 C  CD  . GLU   B 2 204 ? -30.457 -9.310  16.926  1.00 90.92  ? 320 GLU   B CD  1 
ATOM   3231 O  OE1 . GLU   B 2 204 ? -29.299 -9.786  17.043  1.00 101.88 ? 320 GLU   B OE1 1 
ATOM   3232 O  OE2 . GLU   B 2 204 ? -31.440 -9.978  16.520  1.00 98.94  ? 320 GLU   B OE2 1 
ATOM   3233 N  N   . ILE   B 2 205 ? -27.423 -4.860  18.019  1.00 53.91  ? 321 ILE   B N   1 
ATOM   3234 C  CA  . ILE   B 2 205 ? -26.027 -4.346  17.882  1.00 65.12  ? 321 ILE   B CA  1 
ATOM   3235 C  C   . ILE   B 2 205 ? -25.470 -4.681  16.484  1.00 59.92  ? 321 ILE   B C   1 
ATOM   3236 O  O   . ILE   B 2 205 ? -25.680 -5.802  16.018  1.00 51.03  ? 321 ILE   B O   1 
ATOM   3237 C  CB  . ILE   B 2 205 ? -25.150 -4.934  19.011  1.00 76.20  ? 321 ILE   B CB  1 
ATOM   3238 C  CG1 . ILE   B 2 205 ? -25.531 -4.341  20.375  1.00 83.19  ? 321 ILE   B CG1 1 
ATOM   3239 C  CG2 . ILE   B 2 205 ? -23.669 -4.772  18.688  1.00 76.86  ? 321 ILE   B CG2 1 
ATOM   3240 C  CD1 . ILE   B 2 205 ? -24.522 -4.582  21.480  1.00 83.91  ? 321 ILE   B CD1 1 
ATOM   3241 N  N   . GLY   B 2 206 ? -24.798 -3.723  15.841  1.00 61.54  ? 322 GLY   B N   1 
ATOM   3242 C  CA  . GLY   B 2 206 ? -24.122 -3.905  14.539  1.00 60.91  ? 322 GLY   B CA  1 
ATOM   3243 C  C   . GLY   B 2 206 ? -25.080 -3.981  13.355  1.00 62.00  ? 322 GLY   B C   1 
ATOM   3244 O  O   . GLY   B 2 206 ? -24.592 -4.131  12.206  1.00 57.57  ? 322 GLY   B O   1 
ATOM   3245 N  N   . ASN   B 2 207 ? -26.396 -3.928  13.593  1.00 53.36  ? 323 ASN   B N   1 
ATOM   3246 C  CA  . ASN   B 2 207 ? -27.390 -3.729  12.515  1.00 44.68  ? 323 ASN   B CA  1 
ATOM   3247 C  C   . ASN   B 2 207 ? -27.492 -2.222  12.276  1.00 46.53  ? 323 ASN   B C   1 
ATOM   3248 O  O   . ASN   B 2 207 ? -28.048 -1.535  13.148  1.00 41.69  ? 323 ASN   B O   1 
ATOM   3249 C  CB  . ASN   B 2 207 ? -28.742 -4.342  12.832  1.00 43.99  ? 323 ASN   B CB  1 
ATOM   3250 C  CG  . ASN   B 2 207 ? -29.725 -4.134  11.709  1.00 46.44  ? 323 ASN   B CG  1 
ATOM   3251 O  OD1 . ASN   B 2 207 ? -29.706 -3.113  11.037  1.00 58.32  ? 323 ASN   B OD1 1 
ATOM   3252 N  ND2 . ASN   B 2 207 ? -30.591 -5.097  11.485  1.00 59.80  ? 323 ASN   B ND2 1 
ATOM   3253 N  N   . ILE   B 2 208 ? -26.954 -1.746  11.149  1.00 39.72  ? 324 ILE   B N   1 
ATOM   3254 C  CA  . ILE   B 2 208 ? -26.850 -0.297  10.812  1.00 41.43  ? 324 ILE   B CA  1 
ATOM   3255 C  C   . ILE   B 2 208 ? -27.984 0.120   9.876   1.00 34.98  ? 324 ILE   B C   1 
ATOM   3256 O  O   . ILE   B 2 208 ? -27.978 1.286   9.460   1.00 38.00  ? 324 ILE   B O   1 
ATOM   3257 C  CB  . ILE   B 2 208 ? -25.456 0.039   10.233  1.00 45.37  ? 324 ILE   B CB  1 
ATOM   3258 C  CG1 . ILE   B 2 208 ? -25.033 -0.863  9.064   1.00 51.68  ? 324 ILE   B CG1 1 
ATOM   3259 C  CG2 . ILE   B 2 208 ? -24.419 0.004   11.337  1.00 49.16  ? 324 ILE   B CG2 1 
ATOM   3260 C  CD1 . ILE   B 2 208 ? -25.973 -0.901  7.878   1.00 45.59  ? 324 ILE   B CD1 1 
ATOM   3261 N  N   . GLU   B 2 209 ? -28.954 -0.752  9.585   1.00 33.82  ? 325 GLU   B N   1 
ATOM   3262 C  CA  . GLU   B 2 209 ? -30.068 -0.434  8.662   1.00 37.25  ? 325 GLU   B CA  1 
ATOM   3263 C  C   . GLU   B 2 209 ? -30.883 0.731   9.246   1.00 33.19  ? 325 GLU   B C   1 
ATOM   3264 O  O   . GLU   B 2 209 ? -31.084 0.759   10.469  1.00 34.54  ? 325 GLU   B O   1 
ATOM   3265 C  CB  . GLU   B 2 209 ? -31.004 -1.621  8.435   1.00 44.92  ? 325 GLU   B CB  1 
ATOM   3266 C  CG  . GLU   B 2 209 ? -30.286 -2.870  7.935   1.00 63.36  ? 325 GLU   B CG  1 
ATOM   3267 C  CD  . GLU   B 2 209 ? -31.054 -4.179  8.073   1.00 71.99  ? 325 GLU   B CD  1 
ATOM   3268 O  OE1 . GLU   B 2 209 ? -32.232 -4.142  8.521   1.00 83.48  ? 325 GLU   B OE1 1 
ATOM   3269 O  OE2 . GLU   B 2 209 ? -30.464 -5.247  7.760   1.00 80.67  ? 325 GLU   B OE2 1 
ATOM   3270 N  N   . LYS   B 2 210 ? -31.397 1.600   8.382   1.00 30.27  ? 326 LYS   B N   1 
ATOM   3271 C  CA  . LYS   B 2 210 ? -32.380 2.643   8.756   1.00 29.38  ? 326 LYS   B CA  1 
ATOM   3272 C  C   . LYS   B 2 210 ? -33.742 2.079   8.433   1.00 29.52  ? 326 LYS   B C   1 
ATOM   3273 O  O   . LYS   B 2 210 ? -33.846 1.245   7.531   1.00 25.89  ? 326 LYS   B O   1 
ATOM   3274 C  CB  . LYS   B 2 210 ? -32.172 3.967   8.002   1.00 29.38  ? 326 LYS   B CB  1 
ATOM   3275 C  CG  . LYS   B 2 210 ? -30.788 4.590   8.120   1.00 29.96  ? 326 LYS   B CG  1 
ATOM   3276 C  CD  . LYS   B 2 210 ? -30.169 4.552   9.471   1.00 30.78  ? 326 LYS   B CD  1 
ATOM   3277 C  CE  . LYS   B 2 210 ? -28.752 5.081   9.494   1.00 29.52  ? 326 LYS   B CE  1 
ATOM   3278 N  NZ  . LYS   B 2 210 ? -28.087 4.779   10.790  1.00 27.98  ? 326 LYS   B NZ  1 
ATOM   3279 N  N   . PRO   B 2 211 ? -34.794 2.544   9.139   1.00 30.49  ? 327 PRO   B N   1 
ATOM   3280 C  CA  . PRO   B 2 211 ? -36.138 2.038   8.944   1.00 29.51  ? 327 PRO   B CA  1 
ATOM   3281 C  C   . PRO   B 2 211 ? -36.611 2.288   7.510   1.00 32.06  ? 327 PRO   B C   1 
ATOM   3282 O  O   . PRO   B 2 211 ? -36.478 3.385   6.986   1.00 26.99  ? 327 PRO   B O   1 
ATOM   3283 C  CB  . PRO   B 2 211 ? -36.996 2.764   10.006  1.00 32.43  ? 327 PRO   B CB  1 
ATOM   3284 C  CG  . PRO   B 2 211 ? -36.165 3.926   10.476  1.00 34.32  ? 327 PRO   B CG  1 
ATOM   3285 C  CD  . PRO   B 2 211 ? -34.728 3.559   10.197  1.00 29.93  ? 327 PRO   B CD  1 
ATOM   3286 N  N   . VAL   B 2 212 ? -37.204 1.251   6.910   1.00 28.69  ? 328 VAL   B N   1 
ATOM   3287 C  CA  . VAL   B 2 212 ? -37.672 1.280   5.509   1.00 26.95  ? 328 VAL   B CA  1 
ATOM   3288 C  C   . VAL   B 2 212 ? -38.788 2.305   5.405   1.00 24.94  ? 328 VAL   B C   1 
ATOM   3289 O  O   . VAL   B 2 212 ? -39.104 2.789   4.309   1.00 25.09  ? 328 VAL   B O   1 
ATOM   3290 C  CB  . VAL   B 2 212 ? -38.101 -0.146  5.103   1.00 31.65  ? 328 VAL   B CB  1 
ATOM   3291 C  CG1 . VAL   B 2 212 ? -39.375 -0.577  5.826   1.00 32.78  ? 328 VAL   B CG1 1 
ATOM   3292 C  CG2 . VAL   B 2 212 ? -38.239 -0.279  3.601   1.00 31.50  ? 328 VAL   B CG2 1 
ATOM   3293 N  N   . GLU   B 2 213 ? -39.379 2.679   6.541   1.00 26.10  ? 329 GLU   B N   1 
ATOM   3294 C  CA  . GLU   B 2 213 ? -40.430 3.725   6.611   1.00 27.26  ? 329 GLU   B CA  1 
ATOM   3295 C  C   . GLU   B 2 213 ? -39.954 5.042   5.966   1.00 25.78  ? 329 GLU   B C   1 
ATOM   3296 O  O   . GLU   B 2 213 ? -40.809 5.813   5.453   1.00 27.57  ? 329 GLU   B O   1 
ATOM   3297 C  CB  . GLU   B 2 213 ? -40.836 3.968   8.062   1.00 32.02  ? 329 GLU   B CB  1 
ATOM   3298 C  CG  . GLU   B 2 213 ? -41.699 2.865   8.642   1.00 38.89  ? 329 GLU   B CG  1 
ATOM   3299 C  CD  . GLU   B 2 213 ? -41.027 1.623   9.231   1.00 41.48  ? 329 GLU   B CD  1 
ATOM   3300 O  OE1 . GLU   B 2 213 ? -39.829 1.313   8.969   1.00 35.61  ? 329 GLU   B OE1 1 
ATOM   3301 O  OE2 . GLU   B 2 213 ? -41.735 0.931   9.962   1.00 50.02  ? 329 GLU   B OE2 1 
ATOM   3302 N  N   . ILE   B 2 214 ? -38.656 5.312   5.951   1.00 26.21  ? 330 ILE   B N   1 
ATOM   3303 C  CA  . ILE   B 2 214 ? -38.158 6.567   5.302   1.00 27.55  ? 330 ILE   B CA  1 
ATOM   3304 C  C   . ILE   B 2 214 ? -38.525 6.561   3.805   1.00 28.70  ? 330 ILE   B C   1 
ATOM   3305 O  O   . ILE   B 2 214 ? -38.887 7.604   3.292   1.00 26.78  ? 330 ILE   B O   1 
ATOM   3306 C  CB  . ILE   B 2 214 ? -36.656 6.799   5.567   1.00 27.21  ? 330 ILE   B CB  1 
ATOM   3307 C  CG1 . ILE   B 2 214 ? -36.267 8.230   5.174   1.00 27.05  ? 330 ILE   B CG1 1 
ATOM   3308 C  CG2 . ILE   B 2 214 ? -35.800 5.789   4.862   1.00 27.46  ? 330 ILE   B CG2 1 
ATOM   3309 C  CD1 . ILE   B 2 214 ? -36.973 9.274   6.007   1.00 29.93  ? 330 ILE   B CD1 1 
ATOM   3310 N  N   . PHE   B 2 215 ? -38.467 5.413   3.116   1.00 25.13  ? 331 PHE   B N   1 
ATOM   3311 C  CA  . PHE   B 2 215 ? -38.837 5.284   1.691   1.00 25.63  ? 331 PHE   B CA  1 
ATOM   3312 C  C   . PHE   B 2 215 ? -40.314 5.591   1.509   1.00 27.12  ? 331 PHE   B C   1 
ATOM   3313 O  O   . PHE   B 2 215 ? -40.699 6.234   0.509   1.00 28.30  ? 331 PHE   B O   1 
ATOM   3314 C  CB  . PHE   B 2 215 ? -38.485 3.906   1.124   1.00 24.64  ? 331 PHE   B CB  1 
ATOM   3315 C  CG  . PHE   B 2 215 ? -37.005 3.675   0.946   1.00 25.86  ? 331 PHE   B CG  1 
ATOM   3316 C  CD1 . PHE   B 2 215 ? -36.333 4.179   -0.159  1.00 27.20  ? 331 PHE   B CD1 1 
ATOM   3317 C  CD2 . PHE   B 2 215 ? -36.310 2.870   1.823   1.00 24.92  ? 331 PHE   B CD2 1 
ATOM   3318 C  CE1 . PHE   B 2 215 ? -34.984 3.931   -0.340  1.00 27.84  ? 331 PHE   B CE1 1 
ATOM   3319 C  CE2 . PHE   B 2 215 ? -34.956 2.629   1.646   1.00 28.10  ? 331 PHE   B CE2 1 
ATOM   3320 C  CZ  . PHE   B 2 215 ? -34.303 3.146   0.552   1.00 29.06  ? 331 PHE   B CZ  1 
ATOM   3321 N  N   . HIS   B 2 216 ? -41.138 5.115   2.438   1.00 29.56  ? 332 HIS   B N   1 
ATOM   3322 C  CA  . HIS   B 2 216 ? -42.601 5.351   2.422   1.00 28.61  ? 332 HIS   B CA  1 
ATOM   3323 C  C   . HIS   B 2 216 ? -42.871 6.856   2.481   1.00 28.06  ? 332 HIS   B C   1 
ATOM   3324 O  O   . HIS   B 2 216 ? -43.658 7.387   1.682   1.00 28.06  ? 332 HIS   B O   1 
ATOM   3325 C  CB  . HIS   B 2 216 ? -43.282 4.589   3.568   1.00 30.64  ? 332 HIS   B CB  1 
ATOM   3326 C  CG  . HIS   B 2 216 ? -43.000 3.118   3.596   1.00 36.11  ? 332 HIS   B CG  1 
ATOM   3327 N  ND1 . HIS   B 2 216 ? -43.310 2.319   4.699   1.00 43.83  ? 332 HIS   B ND1 1 
ATOM   3328 C  CD2 . HIS   B 2 216 ? -42.453 2.289   2.673   1.00 39.23  ? 332 HIS   B CD2 1 
ATOM   3329 C  CE1 . HIS   B 2 216 ? -42.977 1.062   4.440   1.00 48.74  ? 332 HIS   B CE1 1 
ATOM   3330 N  NE2 . HIS   B 2 216 ? -42.437 1.020   3.199   1.00 40.34  ? 332 HIS   B NE2 1 
ATOM   3331 N  N   . ILE   B 2 217 ? -42.252 7.534   3.424   1.00 28.73  ? 333 ILE   B N   1 
ATOM   3332 C  CA  . ILE   B 2 217 ? -42.406 9.014   3.534   1.00 29.26  ? 333 ILE   B CA  1 
ATOM   3333 C  C   . ILE   B 2 217 ? -41.971 9.679   2.210   1.00 27.95  ? 333 ILE   B C   1 
ATOM   3334 O  O   . ILE   B 2 217 ? -42.737 10.481  1.643   1.00 29.09  ? 333 ILE   B O   1 
ATOM   3335 C  CB  . ILE   B 2 217 ? -41.640 9.515   4.771   1.00 29.69  ? 333 ILE   B CB  1 
ATOM   3336 C  CG1 . ILE   B 2 217 ? -42.284 9.016   6.068   1.00 29.59  ? 333 ILE   B CG1 1 
ATOM   3337 C  CG2 . ILE   B 2 217 ? -41.561 11.025  4.743   1.00 30.68  ? 333 ILE   B CG2 1 
ATOM   3338 C  CD1 . ILE   B 2 217 ? -41.390 9.127   7.292   1.00 29.26  ? 333 ILE   B CD1 1 
ATOM   3339 N  N   . ILE   B 2 218 ? -40.817 9.316   1.675   1.00 28.62  ? 334 ILE   B N   1 
ATOM   3340 C  CA  . ILE   B 2 218 ? -40.287 10.012  0.463   1.00 27.59  ? 334 ILE   B CA  1 
ATOM   3341 C  C   . ILE   B 2 218 ? -41.208 9.764   -0.740  1.00 28.18  ? 334 ILE   B C   1 
ATOM   3342 O  O   . ILE   B 2 218 ? -41.661 10.731  -1.409  1.00 29.23  ? 334 ILE   B O   1 
ATOM   3343 C  CB  . ILE   B 2 218 ? -38.854 9.527   0.205   1.00 25.42  ? 334 ILE   B CB  1 
ATOM   3344 C  CG1 . ILE   B 2 218 ? -37.899 9.909   1.338   1.00 25.59  ? 334 ILE   B CG1 1 
ATOM   3345 C  CG2 . ILE   B 2 218 ? -38.405 10.015  -1.161  1.00 28.29  ? 334 ILE   B CG2 1 
ATOM   3346 C  CD1 . ILE   B 2 218 ? -36.541 9.241   1.295   1.00 27.03  ? 334 ILE   B CD1 1 
ATOM   3347 N  N   . GLU   B 2 219 ? -41.598 8.514   -0.950  1.00 30.62  ? 335 GLU   B N   1 
ATOM   3348 C  CA  . GLU   B 2 219 ? -42.465 8.162   -2.113  1.00 30.42  ? 335 GLU   B CA  1 
ATOM   3349 C  C   . GLU   B 2 219 ? -43.824 8.865   -2.005  1.00 29.71  ? 335 GLU   B C   1 
ATOM   3350 O  O   . GLU   B 2 219 ? -44.353 9.289   -3.076  1.00 33.58  ? 335 GLU   B O   1 
ATOM   3351 C  CB  . GLU   B 2 219 ? -42.566 6.642   -2.227  1.00 29.66  ? 335 GLU   B CB  1 
ATOM   3352 C  CG  . GLU   B 2 219 ? -41.209 6.013   -2.596  1.00 25.48  ? 335 GLU   B CG  1 
ATOM   3353 C  CD  . GLU   B 2 219 ? -41.111 4.505   -2.414  1.00 30.67  ? 335 GLU   B CD  1 
ATOM   3354 O  OE1 . GLU   B 2 219 ? -42.079 3.896   -1.876  1.00 28.45  ? 335 GLU   B OE1 1 
ATOM   3355 O  OE2 . GLU   B 2 219 ? -40.045 3.937   -2.771  1.00 26.54  ? 335 GLU   B OE2 1 
ATOM   3356 N  N   . HIS   B 2 220 ? -44.341 9.026   -0.789  1.00 31.78  ? 336 HIS   B N   1 
ATOM   3357 C  CA  . HIS   B 2 220 ? -45.678 9.629   -0.523  1.00 33.98  ? 336 HIS   B CA  1 
ATOM   3358 C  C   . HIS   B 2 220 ? -45.672 11.105  -0.920  1.00 32.05  ? 336 HIS   B C   1 
ATOM   3359 O  O   . HIS   B 2 220 ? -46.739 11.629  -1.191  1.00 30.83  ? 336 HIS   B O   1 
ATOM   3360 C  CB  . HIS   B 2 220 ? -46.113 9.419   0.941   1.00 39.50  ? 336 HIS   B CB  1 
ATOM   3361 C  CG  . HIS   B 2 220 ? -46.496 8.016   1.300   1.00 43.57  ? 336 HIS   B CG  1 
ATOM   3362 N  ND1 . HIS   B 2 220 ? -46.601 7.587   2.648   1.00 46.45  ? 336 HIS   B ND1 1 
ATOM   3363 C  CD2 . HIS   B 2 220 ? -46.743 6.929   0.526   1.00 42.30  ? 336 HIS   B CD2 1 
ATOM   3364 C  CE1 . HIS   B 2 220 ? -46.905 6.300   2.673   1.00 47.74  ? 336 HIS   B CE1 1 
ATOM   3365 N  NE2 . HIS   B 2 220 ? -46.998 5.871   1.379   1.00 53.97  ? 336 HIS   B NE2 1 
ATOM   3366 N  N   . PHE   B 2 221 ? -44.511 11.767  -1.006  1.00 35.10  ? 337 PHE   B N   1 
ATOM   3367 C  CA  . PHE   B 2 221 ? -44.461 13.198  -1.405  1.00 33.86  ? 337 PHE   B CA  1 
ATOM   3368 C  C   . PHE   B 2 221 ? -44.731 13.366  -2.908  1.00 32.04  ? 337 PHE   B C   1 
ATOM   3369 O  O   . PHE   B 2 221 ? -44.957 14.502  -3.308  1.00 32.22  ? 337 PHE   B O   1 
ATOM   3370 C  CB  . PHE   B 2 221 ? -43.105 13.848  -1.137  1.00 34.98  ? 337 PHE   B CB  1 
ATOM   3371 C  CG  . PHE   B 2 221 ? -42.754 14.055  0.309   1.00 35.10  ? 337 PHE   B CG  1 
ATOM   3372 C  CD1 . PHE   B 2 221 ? -43.610 14.735  1.162   1.00 42.99  ? 337 PHE   B CD1 1 
ATOM   3373 C  CD2 . PHE   B 2 221 ? -41.544 13.607  0.806   1.00 34.34  ? 337 PHE   B CD2 1 
ATOM   3374 C  CE1 . PHE   B 2 221 ? -43.267 14.949  2.487   1.00 42.91  ? 337 PHE   B CE1 1 
ATOM   3375 C  CE2 . PHE   B 2 221 ? -41.218 13.806  2.136   1.00 35.34  ? 337 PHE   B CE2 1 
ATOM   3376 C  CZ  . PHE   B 2 221 ? -42.075 14.475  2.977   1.00 34.75  ? 337 PHE   B CZ  1 
ATOM   3377 N  N   . CYS   B 2 222 ? -44.634 12.309  -3.723  1.00 33.30  ? 338 CYS   B N   1 
ATOM   3378 C  CA  . CYS   B 2 222 ? -44.888 12.351  -5.187  1.00 35.71  ? 338 CYS   B CA  1 
ATOM   3379 C  C   . CYS   B 2 222 ? -44.003 13.417  -5.855  1.00 41.38  ? 338 CYS   B C   1 
ATOM   3380 O  O   . CYS   B 2 222 ? -44.547 14.277  -6.552  1.00 35.31  ? 338 CYS   B O   1 
ATOM   3381 C  CB  . CYS   B 2 222 ? -46.364 12.640  -5.441  1.00 40.64  ? 338 CYS   B CB  1 
ATOM   3382 S  SG  . CYS   B 2 222 ? -47.448 11.495  -4.548  1.00 42.60  ? 338 CYS   B SG  1 
ATOM   3383 N  N   . LEU   B 2 223 ? -42.686 13.354  -5.645  1.00 39.08  ? 339 LEU   B N   1 
ATOM   3384 C  CA  . LEU   B 2 223 ? -41.708 14.421  -6.033  1.00 39.86  ? 339 LEU   B CA  1 
ATOM   3385 C  C   . LEU   B 2 223 ? -41.068 14.134  -7.395  1.00 38.18  ? 339 LEU   B C   1 
ATOM   3386 O  O   . LEU   B 2 223 ? -40.191 14.883  -7.790  1.00 44.15  ? 339 LEU   B O   1 
ATOM   3387 C  CB  . LEU   B 2 223 ? -40.584 14.450  -5.002  1.00 38.36  ? 339 LEU   B CB  1 
ATOM   3388 C  CG  . LEU   B 2 223 ? -41.023 14.594  -3.557  1.00 42.59  ? 339 LEU   B CG  1 
ATOM   3389 C  CD1 . LEU   B 2 223 ? -39.851 14.312  -2.618  1.00 40.70  ? 339 LEU   B CD1 1 
ATOM   3390 C  CD2 . LEU   B 2 223 ? -41.629 15.970  -3.344  1.00 46.84  ? 339 LEU   B CD2 1 
ATOM   3391 N  N   . GLY   B 2 224 ? -41.417 13.047  -8.060  1.00 35.36  ? 340 GLY   B N   1 
ATOM   3392 C  CA  . GLY   B 2 224 ? -40.710 12.681  -9.287  1.00 37.32  ? 340 GLY   B CA  1 
ATOM   3393 C  C   . GLY   B 2 224 ? -40.127 11.304  -9.163  1.00 35.84  ? 340 GLY   B C   1 
ATOM   3394 O  O   . GLY   B 2 224 ? -40.064 10.765  -8.040  1.00 38.75  ? 340 GLY   B O   1 
ATOM   3395 N  N   . ARG   B 2 225 ? -39.713 10.750  -10.292 1.00 35.45  ? 341 ARG   B N   1 
ATOM   3396 C  CA  . ARG   B 2 225 ? -39.415 9.305   -10.396 1.00 36.28  ? 341 ARG   B CA  1 
ATOM   3397 C  C   . ARG   B 2 225 ? -37.912 9.071   -10.404 1.00 29.21  ? 341 ARG   B C   1 
ATOM   3398 O  O   . ARG   B 2 225 ? -37.544 7.912   -10.461 1.00 29.78  ? 341 ARG   B O   1 
ATOM   3399 C  CB  . ARG   B 2 225 ? -40.109 8.751   -11.640 1.00 34.96  ? 341 ARG   B CB  1 
ATOM   3400 C  CG  . ARG   B 2 225 ? -41.614 8.967   -11.594 1.00 38.18  ? 341 ARG   B CG  1 
ATOM   3401 C  CD  . ARG   B 2 225 ? -42.316 8.533   -12.861 1.00 38.62  ? 341 ARG   B CD  1 
ATOM   3402 N  NE  . ARG   B 2 225 ? -42.085 7.141   -13.211 1.00 39.16  ? 341 ARG   B NE  1 
ATOM   3403 C  CZ  . ARG   B 2 225 ? -41.539 6.701   -14.339 1.00 39.21  ? 341 ARG   B CZ  1 
ATOM   3404 N  NH1 . ARG   B 2 225 ? -41.116 7.533   -15.271 1.00 41.61  ? 341 ARG   B NH1 1 
ATOM   3405 N  NH2 . ARG   B 2 225 ? -41.433 5.403   -14.537 1.00 43.38  ? 341 ARG   B NH2 1 
ATOM   3406 N  N   . ARG   B 2 226 ? -37.079 10.113  -10.503 1.00 28.50  ? 342 ARG   B N   1 
ATOM   3407 C  CA  A ARG   B 2 226 ? -35.600 9.938   -10.548 0.38 28.22  ? 342 ARG   B CA  1 
ATOM   3408 C  CA  C ARG   B 2 226 ? -35.607 9.903   -10.544 0.62 28.45  ? 342 ARG   B CA  1 
ATOM   3409 C  C   . ARG   B 2 226 ? -35.089 9.987   -9.102  1.00 27.39  ? 342 ARG   B C   1 
ATOM   3410 O  O   . ARG   B 2 226 ? -34.919 11.133  -8.565  1.00 27.71  ? 342 ARG   B O   1 
ATOM   3411 C  CB  A ARG   B 2 226 ? -34.922 10.984  -11.447 0.38 29.09  ? 342 ARG   B CB  1 
ATOM   3412 C  CB  C ARG   B 2 226 ? -34.901 10.873  -11.500 0.62 29.97  ? 342 ARG   B CB  1 
ATOM   3413 C  CG  A ARG   B 2 226 ? -35.466 11.063  -12.870 0.38 29.50  ? 342 ARG   B CG  1 
ATOM   3414 C  CG  C ARG   B 2 226 ? -35.454 10.881  -12.921 0.62 31.28  ? 342 ARG   B CG  1 
ATOM   3415 C  CD  A ARG   B 2 226 ? -34.958 12.270  -13.658 0.38 29.17  ? 342 ARG   B CD  1 
ATOM   3416 C  CD  C ARG   B 2 226 ? -35.049 12.161  -13.632 0.62 32.11  ? 342 ARG   B CD  1 
ATOM   3417 N  NE  A ARG   B 2 226 ? -35.626 13.531  -13.323 0.38 30.01  ? 342 ARG   B NE  1 
ATOM   3418 N  NE  C ARG   B 2 226 ? -35.706 12.452  -14.906 0.62 33.60  ? 342 ARG   B NE  1 
ATOM   3419 C  CZ  A ARG   B 2 226 ? -35.209 14.755  -13.682 0.38 28.06  ? 342 ARG   B CZ  1 
ATOM   3420 C  CZ  C ARG   B 2 226 ? -36.898 13.054  -15.057 0.62 35.92  ? 342 ARG   B CZ  1 
ATOM   3421 N  NH1 A ARG   B 2 226 ? -34.086 14.919  -14.361 0.38 25.92  ? 342 ARG   B NH1 1 
ATOM   3422 N  NH1 C ARG   B 2 226 ? -37.636 13.403  -14.011 0.62 30.30  ? 342 ARG   B NH1 1 
ATOM   3423 N  NH2 A ARG   B 2 226 ? -35.895 15.814  -13.296 0.38 25.88  ? 342 ARG   B NH2 1 
ATOM   3424 N  NH2 C ARG   B 2 226 ? -37.357 13.290  -16.282 0.62 36.14  ? 342 ARG   B NH2 1 
ATOM   3425 N  N   . ARG   B 2 227 ? -34.916 8.814   -8.491  1.00 24.97  ? 343 ARG   B N   1 
ATOM   3426 C  CA  . ARG   B 2 227 ? -34.614 8.665   -7.061  1.00 27.49  ? 343 ARG   B CA  1 
ATOM   3427 C  C   . ARG   B 2 227 ? -33.332 7.870   -6.905  1.00 26.23  ? 343 ARG   B C   1 
ATOM   3428 O  O   . ARG   B 2 227 ? -33.238 6.723   -7.393  1.00 27.47  ? 343 ARG   B O   1 
ATOM   3429 C  CB  . ARG   B 2 227 ? -35.784 8.019   -6.315  1.00 29.17  ? 343 ARG   B CB  1 
ATOM   3430 C  CG  . ARG   B 2 227 ? -37.164 8.464   -6.773  1.00 28.68  ? 343 ARG   B CG  1 
ATOM   3431 C  CD  . ARG   B 2 227 ? -38.101 7.792   -5.791  1.00 31.78  ? 343 ARG   B CD  1 
ATOM   3432 N  NE  . ARG   B 2 227 ? -39.499 7.946   -6.032  1.00 33.41  ? 343 ARG   B NE  1 
ATOM   3433 C  CZ  . ARG   B 2 227 ? -40.306 7.040   -6.571  1.00 34.13  ? 343 ARG   B CZ  1 
ATOM   3434 N  NH1 . ARG   B 2 227 ? -39.857 5.889   -7.049  1.00 37.47  ? 343 ARG   B NH1 1 
ATOM   3435 N  NH2 . ARG   B 2 227 ? -41.579 7.327   -6.672  1.00 34.59  ? 343 ARG   B NH2 1 
ATOM   3436 N  N   . LEU   B 2 228 ? -32.388 8.485   -6.201  1.00 22.64  ? 344 LEU   B N   1 
ATOM   3437 C  CA  . LEU   B 2 228 ? -31.026 7.987   -5.988  1.00 24.19  ? 344 LEU   B CA  1 
ATOM   3438 C  C   . LEU   B 2 228 ? -30.837 7.720   -4.515  1.00 23.80  ? 344 LEU   B C   1 
ATOM   3439 O  O   . LEU   B 2 228 ? -31.139 8.623   -3.677  1.00 22.16  ? 344 LEU   B O   1 
ATOM   3440 C  CB  . LEU   B 2 228 ? -30.020 9.041   -6.448  1.00 23.56  ? 344 LEU   B CB  1 
ATOM   3441 C  CG  . LEU   B 2 228 ? -28.564 8.734   -6.095  1.00 25.29  ? 344 LEU   B CG  1 
ATOM   3442 C  CD1 . LEU   B 2 228 ? -28.080 7.403   -6.692  1.00 26.49  ? 344 LEU   B CD1 1 
ATOM   3443 C  CD2 . LEU   B 2 228 ? -27.681 9.889   -6.522  1.00 24.05  ? 344 LEU   B CD2 1 
ATOM   3444 N  N   . HIS   B 2 229 ? -30.338 6.534   -4.214  1.00 22.78  ? 345 HIS   B N   1 
ATOM   3445 C  CA  . HIS   B 2 229 ? -29.954 6.169   -2.841  1.00 22.38  ? 345 HIS   B CA  1 
ATOM   3446 C  C   . HIS   B 2 229 ? -28.458 5.954   -2.824  1.00 21.22  ? 345 HIS   B C   1 
ATOM   3447 O  O   . HIS   B 2 229 ? -27.990 4.913   -3.314  1.00 22.08  ? 345 HIS   B O   1 
ATOM   3448 C  CB  . HIS   B 2 229 ? -30.780 4.989   -2.285  1.00 20.94  ? 345 HIS   B CB  1 
ATOM   3449 C  CG  . HIS   B 2 229 ? -30.460 4.635   -0.867  1.00 22.38  ? 345 HIS   B CG  1 
ATOM   3450 N  ND1 . HIS   B 2 229 ? -30.915 3.458   -0.277  1.00 21.74  ? 345 HIS   B ND1 1 
ATOM   3451 C  CD2 . HIS   B 2 229 ? -29.804 5.303   0.117   1.00 24.57  ? 345 HIS   B CD2 1 
ATOM   3452 C  CE1 . HIS   B 2 229 ? -30.508 3.405   0.978   1.00 23.56  ? 345 HIS   B CE1 1 
ATOM   3453 N  NE2 . HIS   B 2 229 ? -29.817 4.525   1.253   1.00 22.71  ? 345 HIS   B NE2 1 
ATOM   3454 N  N   . LEU   B 2 230 ? -27.737 6.910   -2.240  1.00 23.54  ? 346 LEU   B N   1 
ATOM   3455 C  CA  . LEU   B 2 230 ? -26.268 6.822   -2.121  1.00 22.56  ? 346 LEU   B CA  1 
ATOM   3456 C  C   . LEU   B 2 230 ? -25.942 6.152   -0.804  1.00 21.81  ? 346 LEU   B C   1 
ATOM   3457 O  O   . LEU   B 2 230 ? -26.439 6.630   0.226   1.00 21.63  ? 346 LEU   B O   1 
ATOM   3458 C  CB  . LEU   B 2 230 ? -25.632 8.215   -2.177  1.00 24.56  ? 346 LEU   B CB  1 
ATOM   3459 C  CG  . LEU   B 2 230 ? -25.556 8.823   -3.570  1.00 25.65  ? 346 LEU   B CG  1 
ATOM   3460 C  CD1 . LEU   B 2 230 ? -25.169 10.306  -3.450  1.00 28.65  ? 346 LEU   B CD1 1 
ATOM   3461 C  CD2 . LEU   B 2 230 ? -24.557 8.048   -4.453  1.00 24.91  ? 346 LEU   B CD2 1 
ATOM   3462 N  N   . PHE   B 2 231 ? -24.959 5.240   -0.849  1.00 20.86  ? 347 PHE   B N   1 
ATOM   3463 C  CA  . PHE   B 2 231 ? -24.532 4.347   0.255   1.00 22.39  ? 347 PHE   B CA  1 
ATOM   3464 C  C   . PHE   B 2 231 ? -25.652 3.339   0.579   1.00 23.58  ? 347 PHE   B C   1 
ATOM   3465 O  O   . PHE   B 2 231 ? -25.765 2.892   1.727   1.00 25.97  ? 347 PHE   B O   1 
ATOM   3466 C  CB  . PHE   B 2 231 ? -24.099 5.119   1.498   1.00 23.93  ? 347 PHE   B CB  1 
ATOM   3467 C  CG  . PHE   B 2 231 ? -22.939 6.044   1.225   1.00 23.45  ? 347 PHE   B CG  1 
ATOM   3468 C  CD1 . PHE   B 2 231 ? -21.640 5.559   1.177   1.00 24.42  ? 347 PHE   B CD1 1 
ATOM   3469 C  CD2 . PHE   B 2 231 ? -23.165 7.403   1.021   1.00 29.32  ? 347 PHE   B CD2 1 
ATOM   3470 C  CE1 . PHE   B 2 231 ? -20.568 6.407   0.919   1.00 25.53  ? 347 PHE   B CE1 1 
ATOM   3471 C  CE2 . PHE   B 2 231 ? -22.098 8.246   0.753   1.00 24.57  ? 347 PHE   B CE2 1 
ATOM   3472 C  CZ  . PHE   B 2 231 ? -20.804 7.746   0.711   1.00 24.20  ? 347 PHE   B CZ  1 
ATOM   3473 N  N   . GLY   B 2 232 ? -26.513 3.021   -0.377  1.00 24.47  ? 348 GLY   B N   1 
ATOM   3474 C  CA  . GLY   B 2 232 ? -27.432 1.882   -0.178  1.00 24.56  ? 348 GLY   B CA  1 
ATOM   3475 C  C   . GLY   B 2 232 ? -26.668 0.575   -0.255  1.00 25.46  ? 348 GLY   B C   1 
ATOM   3476 O  O   . GLY   B 2 232 ? -25.420 0.586   -0.470  1.00 24.50  ? 348 GLY   B O   1 
ATOM   3477 N  N   . ARG   B 2 233 ? -27.371 -0.552  -0.078  1.00 24.52  ? 349 ARG   B N   1 
ATOM   3478 C  CA  . ARG   B 2 233 ? -26.751 -1.894  0.097   1.00 22.96  ? 349 ARG   B CA  1 
ATOM   3479 C  C   . ARG   B 2 233 ? -27.634 -2.908  -0.676  1.00 21.87  ? 349 ARG   B C   1 
ATOM   3480 O  O   . ARG   B 2 233 ? -28.732 -2.539  -1.099  1.00 20.68  ? 349 ARG   B O   1 
ATOM   3481 C  CB  . ARG   B 2 233 ? -26.679 -2.259  1.587   1.00 26.03  ? 349 ARG   B CB  1 
ATOM   3482 C  CG  . ARG   B 2 233 ? -25.808 -1.341  2.457   1.00 30.06  ? 349 ARG   B CG  1 
ATOM   3483 C  CD  . ARG   B 2 233 ? -25.763 -1.723  3.938   1.00 28.53  ? 349 ARG   B CD  1 
ATOM   3484 N  NE  . ARG   B 2 233 ? -27.087 -1.591  4.513   1.00 31.40  ? 349 ARG   B NE  1 
ATOM   3485 C  CZ  . ARG   B 2 233 ? -27.732 -0.448  4.769   1.00 30.29  ? 349 ARG   B CZ  1 
ATOM   3486 N  NH1 . ARG   B 2 233 ? -27.180 0.730   4.531   1.00 31.34  ? 349 ARG   B NH1 1 
ATOM   3487 N  NH2 . ARG   B 2 233 ? -28.953 -0.492  5.245   1.00 28.63  ? 349 ARG   B NH2 1 
ATOM   3488 N  N   . ASP   B 2 234 ? -27.214 -4.157  -0.839  1.00 23.14  ? 350 ASP   B N   1 
ATOM   3489 C  CA  . ASP   B 2 234 ? -28.111 -5.169  -1.466  1.00 24.31  ? 350 ASP   B CA  1 
ATOM   3490 C  C   . ASP   B 2 234 ? -29.471 -5.138  -0.760  1.00 21.85  ? 350 ASP   B C   1 
ATOM   3491 O  O   . ASP   B 2 234 ? -30.519 -5.238  -1.454  1.00 25.38  ? 350 ASP   B O   1 
ATOM   3492 C  CB  . ASP   B 2 234 ? -27.480 -6.556  -1.431  1.00 25.28  ? 350 ASP   B CB  1 
ATOM   3493 C  CG  . ASP   B 2 234 ? -26.371 -6.765  -2.437  1.00 28.26  ? 350 ASP   B CG  1 
ATOM   3494 O  OD1 . ASP   B 2 234 ? -26.048 -5.811  -3.175  1.00 24.32  ? 350 ASP   B OD1 1 
ATOM   3495 O  OD2 . ASP   B 2 234 ? -25.881 -7.912  -2.500  1.00 27.76  ? 350 ASP   B OD2 1 
ATOM   3496 N  N   . SER   B 2 235 ? -29.464 -5.021  0.562   1.00 23.74  ? 351 SER   B N   1 
ATOM   3497 C  CA  . SER   B 2 235 ? -30.647 -5.087  1.469   1.00 24.62  ? 351 SER   B CA  1 
ATOM   3498 C  C   . SER   B 2 235 ? -31.604 -3.911  1.235   1.00 27.58  ? 351 SER   B C   1 
ATOM   3499 O  O   . SER   B 2 235 ? -32.725 -4.022  1.640   1.00 24.33  ? 351 SER   B O   1 
ATOM   3500 C  CB  . SER   B 2 235 ? -30.213 -5.164  2.923   1.00 32.28  ? 351 SER   B CB  1 
ATOM   3501 O  OG  . SER   B 2 235 ? -29.531 -3.967  3.320   1.00 28.15  ? 351 SER   B OG  1 
ATOM   3502 N  N   . THR   B 2 236 ? -31.223 -2.819  0.556   1.00 23.28  ? 352 THR   B N   1 
ATOM   3503 C  CA  . THR   B 2 236 ? -32.070 -1.599  0.472   1.00 23.19  ? 352 THR   B CA  1 
ATOM   3504 C  C   . THR   B 2 236 ? -32.589 -1.431  -0.948  1.00 21.26  ? 352 THR   B C   1 
ATOM   3505 O  O   . THR   B 2 236 ? -33.410 -0.527  -1.176  1.00 25.29  ? 352 THR   B O   1 
ATOM   3506 C  CB  . THR   B 2 236 ? -31.325 -0.324  0.908   1.00 23.17  ? 352 THR   B CB  1 
ATOM   3507 O  OG1 . THR   B 2 236 ? -30.219 -0.041  0.042   1.00 22.64  ? 352 THR   B OG1 1 
ATOM   3508 C  CG2 . THR   B 2 236 ? -30.805 -0.423  2.325   1.00 25.17  ? 352 THR   B CG2 1 
ATOM   3509 N  N   . ILE   B 2 237 ? -32.123 -2.260  -1.884  1.00 24.38  ? 353 ILE   B N   1 
ATOM   3510 C  CA  . ILE   B 2 237 ? -32.548 -2.159  -3.305  1.00 23.72  ? 353 ILE   B CA  1 
ATOM   3511 C  C   . ILE   B 2 237 ? -34.069 -2.279  -3.374  1.00 25.61  ? 353 ILE   B C   1 
ATOM   3512 O  O   . ILE   B 2 237 ? -34.639 -3.140  -2.677  1.00 25.90  ? 353 ILE   B O   1 
ATOM   3513 C  CB  . ILE   B 2 237 ? -31.811 -3.172  -4.191  1.00 22.76  ? 353 ILE   B CB  1 
ATOM   3514 C  CG1 . ILE   B 2 237 ? -30.349 -2.779  -4.333  1.00 21.72  ? 353 ILE   B CG1 1 
ATOM   3515 C  CG2 . ILE   B 2 237 ? -32.519 -3.265  -5.540  1.00 23.70  ? 353 ILE   B CG2 1 
ATOM   3516 C  CD1 . ILE   B 2 237 ? -29.446 -3.820  -4.882  1.00 22.45  ? 353 ILE   B CD1 1 
ATOM   3517 N  N   . ARG   B 2 238 ? -34.703 -1.459  -4.195  1.00 23.43  ? 354 ARG   B N   1 
ATOM   3518 C  CA  . ARG   B 2 238 ? -36.139 -1.176  -4.110  1.00 25.95  ? 354 ARG   B CA  1 
ATOM   3519 C  C   . ARG   B 2 238 ? -36.626 -0.709  -5.474  1.00 28.42  ? 354 ARG   B C   1 
ATOM   3520 O  O   . ARG   B 2 238 ? -35.957 0.082   -6.165  1.00 27.97  ? 354 ARG   B O   1 
ATOM   3521 C  CB  . ARG   B 2 238 ? -36.334 -0.120  -3.014  1.00 27.52  ? 354 ARG   B CB  1 
ATOM   3522 C  CG  . ARG   B 2 238 ? -37.766 0.233   -2.686  1.00 32.16  ? 354 ARG   B CG  1 
ATOM   3523 C  CD  . ARG   B 2 238 ? -37.787 1.164   -1.480  1.00 30.33  ? 354 ARG   B CD  1 
ATOM   3524 N  NE  . ARG   B 2 238 ? -39.125 1.661   -1.334  1.00 32.67  ? 354 ARG   B NE  1 
ATOM   3525 C  CZ  . ARG   B 2 238 ? -40.058 1.081   -0.581  1.00 29.55  ? 354 ARG   B CZ  1 
ATOM   3526 N  NH1 . ARG   B 2 238 ? -41.278 1.586   -0.550  1.00 32.59  ? 354 ARG   B NH1 1 
ATOM   3527 N  NH2 . ARG   B 2 238 ? -39.748 0.013   0.149   1.00 33.42  ? 354 ARG   B NH2 1 
ATOM   3528 N  N   . PRO   B 2 239 ? -37.819 -1.151  -5.930  1.00 27.56  ? 355 PRO   B N   1 
ATOM   3529 C  CA  . PRO   B 2 239 ? -38.370 -0.633  -7.175  1.00 28.96  ? 355 PRO   B CA  1 
ATOM   3530 C  C   . PRO   B 2 239 ? -38.504 0.878   -7.041  1.00 27.11  ? 355 PRO   B C   1 
ATOM   3531 O  O   . PRO   B 2 239 ? -38.794 1.349   -5.955  1.00 27.32  ? 355 PRO   B O   1 
ATOM   3532 C  CB  . PRO   B 2 239 ? -39.749 -1.296  -7.295  1.00 31.02  ? 355 PRO   B CB  1 
ATOM   3533 C  CG  . PRO   B 2 239 ? -39.587 -2.546  -6.484  1.00 29.88  ? 355 PRO   B CG  1 
ATOM   3534 C  CD  . PRO   B 2 239 ? -38.705 -2.157  -5.314  1.00 32.05  ? 355 PRO   B CD  1 
ATOM   3535 N  N   . GLY   B 2 240 ? -38.280 1.578   -8.150  1.00 26.90  ? 356 GLY   B N   1 
ATOM   3536 C  CA  . GLY   B 2 240 ? -38.393 3.038   -8.209  1.00 27.40  ? 356 GLY   B CA  1 
ATOM   3537 C  C   . GLY   B 2 240 ? -37.130 3.749   -7.739  1.00 24.95  ? 356 GLY   B C   1 
ATOM   3538 O  O   . GLY   B 2 240 ? -37.144 4.951   -7.802  1.00 27.57  ? 356 GLY   B O   1 
ATOM   3539 N  N   . TRP   B 2 241 ? -36.082 3.030   -7.362  1.00 25.00  ? 357 TRP   B N   1 
ATOM   3540 C  CA  . TRP   B 2 241 ? -34.814 3.609   -6.853  1.00 26.15  ? 357 TRP   B CA  1 
ATOM   3541 C  C   . TRP   B 2 241 ? -33.605 3.143   -7.664  1.00 26.10  ? 357 TRP   B C   1 
ATOM   3542 O  O   . TRP   B 2 241 ? -33.546 1.957   -8.072  1.00 24.57  ? 357 TRP   B O   1 
ATOM   3543 C  CB  . TRP   B 2 241 ? -34.634 3.277   -5.366  1.00 24.85  ? 357 TRP   B CB  1 
ATOM   3544 C  CG  . TRP   B 2 241 ? -35.595 4.056   -4.535  1.00 24.93  ? 357 TRP   B CG  1 
ATOM   3545 C  CD1 . TRP   B 2 241 ? -36.915 3.778   -4.296  1.00 26.03  ? 357 TRP   B CD1 1 
ATOM   3546 C  CD2 . TRP   B 2 241 ? -35.309 5.303   -3.898  1.00 26.09  ? 357 TRP   B CD2 1 
ATOM   3547 N  NE1 . TRP   B 2 241 ? -37.471 4.765   -3.526  1.00 24.37  ? 357 TRP   B NE1 1 
ATOM   3548 C  CE2 . TRP   B 2 241 ? -36.511 5.722   -3.281  1.00 26.46  ? 357 TRP   B CE2 1 
ATOM   3549 C  CE3 . TRP   B 2 241 ? -34.161 6.112   -3.822  1.00 25.58  ? 357 TRP   B CE3 1 
ATOM   3550 C  CZ2 . TRP   B 2 241 ? -36.577 6.897   -2.528  1.00 24.62  ? 357 TRP   B CZ2 1 
ATOM   3551 C  CZ3 . TRP   B 2 241 ? -34.240 7.277   -3.086  1.00 26.81  ? 357 TRP   B CZ3 1 
ATOM   3552 C  CH2 . TRP   B 2 241 ? -35.422 7.651   -2.443  1.00 24.76  ? 357 TRP   B CH2 1 
ATOM   3553 N  N   . LEU   B 2 242 ? -32.647 4.048   -7.830  1.00 24.30  ? 358 LEU   B N   1 
ATOM   3554 C  CA  . LEU   B 2 242 ? -31.260 3.711   -8.226  1.00 22.70  ? 358 LEU   B CA  1 
ATOM   3555 C  C   . LEU   B 2 242 ? -30.422 3.666   -6.945  1.00 23.47  ? 358 LEU   B C   1 
ATOM   3556 O  O   . LEU   B 2 242 ? -30.389 4.697   -6.216  1.00 25.45  ? 358 LEU   B O   1 
ATOM   3557 C  CB  . LEU   B 2 242 ? -30.769 4.775   -9.206  1.00 24.94  ? 358 LEU   B CB  1 
ATOM   3558 C  CG  . LEU   B 2 242 ? -29.299 4.677   -9.588  1.00 25.10  ? 358 LEU   B CG  1 
ATOM   3559 C  CD1 . LEU   B 2 242 ? -28.982 3.384   -10.333 1.00 28.41  ? 358 LEU   B CD1 1 
ATOM   3560 C  CD2 . LEU   B 2 242 ? -28.873 5.862   -10.431 1.00 26.69  ? 358 LEU   B CD2 1 
ATOM   3561 N  N   . THR   B 2 243 ? -29.811 2.528   -6.632  1.00 22.23  ? 359 THR   B N   1 
ATOM   3562 C  CA  . THR   B 2 243 ? -29.023 2.308   -5.424  1.00 22.39  ? 359 THR   B CA  1 
ATOM   3563 C  C   . THR   B 2 243 ? -27.553 2.287   -5.812  1.00 27.80  ? 359 THR   B C   1 
ATOM   3564 O  O   . THR   B 2 243 ? -27.184 1.501   -6.692  1.00 27.51  ? 359 THR   B O   1 
ATOM   3565 C  CB  . THR   B 2 243 ? -29.441 1.022   -4.699  1.00 24.05  ? 359 THR   B CB  1 
ATOM   3566 O  OG1 . THR   B 2 243 ? -30.842 1.163   -4.478  1.00 25.70  ? 359 THR   B OG1 1 
ATOM   3567 C  CG2 . THR   B 2 243 ? -28.662 0.835   -3.427  1.00 25.70  ? 359 THR   B CG2 1 
ATOM   3568 N  N   . VAL   B 2 244 ? -26.740 3.128   -5.173  1.00 25.51  ? 360 VAL   B N   1 
ATOM   3569 C  CA  . VAL   B 2 244 ? -25.284 3.163   -5.460  1.00 24.77  ? 360 VAL   B CA  1 
ATOM   3570 C  C   . VAL   B 2 244 ? -24.525 3.043   -4.151  1.00 27.75  ? 360 VAL   B C   1 
ATOM   3571 O  O   . VAL   B 2 244 ? -24.808 3.780   -3.187  1.00 30.05  ? 360 VAL   B O   1 
ATOM   3572 C  CB  . VAL   B 2 244 ? -24.914 4.434   -6.241  1.00 23.94  ? 360 VAL   B CB  1 
ATOM   3573 C  CG1 . VAL   B 2 244 ? -23.424 4.474   -6.532  1.00 26.33  ? 360 VAL   B CG1 1 
ATOM   3574 C  CG2 . VAL   B 2 244 ? -25.735 4.550   -7.479  1.00 24.69  ? 360 VAL   B CG2 1 
ATOM   3575 N  N   . GLY   B 2 245 ? -23.614 2.095   -4.084  1.00 24.76  ? 361 GLY   B N   1 
ATOM   3576 C  CA  . GLY   B 2 245 ? -22.860 1.924   -2.854  1.00 25.71  ? 361 GLY   B CA  1 
ATOM   3577 C  C   . GLY   B 2 245 ? -21.713 0.953   -3.020  1.00 28.78  ? 361 GLY   B C   1 
ATOM   3578 O  O   . GLY   B 2 245 ? -21.687 0.116   -3.929  1.00 27.45  ? 361 GLY   B O   1 
ATOM   3579 N  N   . PRO   B 2 246 ? -20.734 1.045   -2.115  1.00 29.83  ? 362 PRO   B N   1 
ATOM   3580 C  CA  . PRO   B 2 246 ? -19.544 0.206   -2.202  1.00 32.26  ? 362 PRO   B CA  1 
ATOM   3581 C  C   . PRO   B 2 246 ? -19.750 -1.283  -1.902  1.00 31.84  ? 362 PRO   B C   1 
ATOM   3582 O  O   . PRO   B 2 246 ? -18.959 -2.058  -2.394  1.00 30.48  ? 362 PRO   B O   1 
ATOM   3583 C  CB  . PRO   B 2 246 ? -18.607 0.818   -1.149  1.00 34.18  ? 362 PRO   B CB  1 
ATOM   3584 C  CG  . PRO   B 2 246 ? -19.542 1.482   -0.170  1.00 31.90  ? 362 PRO   B CG  1 
ATOM   3585 C  CD  . PRO   B 2 246 ? -20.669 2.016   -1.017  1.00 29.66  ? 362 PRO   B CD  1 
ATOM   3586 N  N   . THR   B 2 247 ? -20.759 -1.669  -1.121  1.00 30.95  ? 363 THR   B N   1 
ATOM   3587 C  CA  . THR   B 2 247 ? -20.907 -3.088  -0.686  1.00 32.88  ? 363 THR   B CA  1 
ATOM   3588 C  C   . THR   B 2 247 ? -21.826 -3.863  -1.635  1.00 32.72  ? 363 THR   B C   1 
ATOM   3589 O  O   . THR   B 2 247 ? -21.989 -5.045  -1.380  1.00 29.22  ? 363 THR   B O   1 
ATOM   3590 C  CB  . THR   B 2 247 ? -21.415 -3.227  0.762   1.00 32.79  ? 363 THR   B CB  1 
ATOM   3591 O  OG1 . THR   B 2 247 ? -22.757 -2.747  0.883   1.00 34.93  ? 363 THR   B OG1 1 
ATOM   3592 C  CG2 . THR   B 2 247 ? -20.497 -2.498  1.725   1.00 35.95  ? 363 THR   B CG2 1 
ATOM   3593 N  N   . LEU   B 2 248 ? -22.408 -3.240  -2.666  1.00 30.12  ? 364 LEU   B N   1 
ATOM   3594 C  CA  . LEU   B 2 248 ? -23.347 -3.971  -3.555  1.00 28.55  ? 364 LEU   B CA  1 
ATOM   3595 C  C   . LEU   B 2 248 ? -22.547 -5.118  -4.183  1.00 30.48  ? 364 LEU   B C   1 
ATOM   3596 O  O   . LEU   B 2 248 ? -21.384 -4.911  -4.545  1.00 28.96  ? 364 LEU   B O   1 
ATOM   3597 C  CB  . LEU   B 2 248 ? -23.959 -3.061  -4.622  1.00 26.83  ? 364 LEU   B CB  1 
ATOM   3598 C  CG  . LEU   B 2 248 ? -25.214 -2.299  -4.214  1.00 30.01  ? 364 LEU   B CG  1 
ATOM   3599 C  CD1 . LEU   B 2 248 ? -24.972 -1.507  -2.936  1.00 32.56  ? 364 LEU   B CD1 1 
ATOM   3600 C  CD2 . LEU   B 2 248 ? -25.649 -1.381  -5.332  1.00 31.08  ? 364 LEU   B CD2 1 
ATOM   3601 N  N   . THR   B 2 249 ? -23.118 -6.322  -4.233  1.00 26.10  ? 365 THR   B N   1 
ATOM   3602 C  CA  . THR   B 2 249 ? -22.453 -7.516  -4.798  1.00 27.90  ? 365 THR   B CA  1 
ATOM   3603 C  C   . THR   B 2 249 ? -22.550 -7.522  -6.316  1.00 26.88  ? 365 THR   B C   1 
ATOM   3604 O  O   . THR   B 2 249 ? -21.694 -8.163  -6.958  1.00 30.68  ? 365 THR   B O   1 
ATOM   3605 C  CB  . THR   B 2 249 ? -23.063 -8.793  -4.193  1.00 27.87  ? 365 THR   B CB  1 
ATOM   3606 O  OG1 . THR   B 2 249 ? -24.459 -8.767  -4.475  1.00 27.62  ? 365 THR   B OG1 1 
ATOM   3607 C  CG2 . THR   B 2 249 ? -22.805 -8.861  -2.707  1.00 29.78  ? 365 THR   B CG2 1 
ATOM   3608 N  N   . ASN   B 2 250 ? -23.588 -6.924  -6.854  1.00 24.35  ? 366 ASN   B N   1 
ATOM   3609 C  CA  . ASN   B 2 250 ? -23.950 -6.933  -8.291  1.00 27.36  ? 366 ASN   B CA  1 
ATOM   3610 C  C   . ASN   B 2 250 ? -24.351 -5.525  -8.722  1.00 25.87  ? 366 ASN   B C   1 
ATOM   3611 O  O   . ASN   B 2 250 ? -24.800 -4.742  -7.854  1.00 28.16  ? 366 ASN   B O   1 
ATOM   3612 C  CB  . ASN   B 2 250 ? -25.127 -7.897  -8.540  1.00 27.91  ? 366 ASN   B CB  1 
ATOM   3613 C  CG  . ASN   B 2 250 ? -24.670 -9.334  -8.427  1.00 30.35  ? 366 ASN   B CG  1 
ATOM   3614 O  OD1 . ASN   B 2 250 ? -24.351 -9.967  -9.430  1.00 31.47  ? 366 ASN   B OD1 1 
ATOM   3615 N  ND2 . ASN   B 2 250 ? -24.515 -9.811  -7.207  1.00 28.30  ? 366 ASN   B ND2 1 
ATOM   3616 N  N   . SER   B 2 251 ? -24.290 -5.266  -10.030 1.00 24.50  ? 367 SER   B N   1 
ATOM   3617 C  CA  . SER   B 2 251 ? -24.760 -4.044  -10.720 1.00 25.96  ? 367 SER   B CA  1 
ATOM   3618 C  C   . SER   B 2 251 ? -25.648 -4.414  -11.908 1.00 26.79  ? 367 SER   B C   1 
ATOM   3619 O  O   . SER   B 2 251 ? -25.419 -5.479  -12.503 1.00 29.57  ? 367 SER   B O   1 
ATOM   3620 C  CB  . SER   B 2 251 ? -23.593 -3.201  -11.167 1.00 25.83  ? 367 SER   B CB  1 
ATOM   3621 O  OG  . SER   B 2 251 ? -22.719 -2.977  -10.067 1.00 24.51  ? 367 SER   B OG  1 
ATOM   3622 N  N   . ASN   B 2 252 ? -26.623 -3.568  -12.222 1.00 25.03  ? 368 ASN   B N   1 
ATOM   3623 C  CA  . ASN   B 2 252 ? -27.402 -3.656  -13.485 1.00 28.88  ? 368 ASN   B CA  1 
ATOM   3624 C  C   . ASN   B 2 252 ? -27.475 -2.279  -14.144 1.00 28.28  ? 368 ASN   B C   1 
ATOM   3625 O  O   . ASN   B 2 252 ? -28.290 -2.108  -15.077 1.00 27.07  ? 368 ASN   B O   1 
ATOM   3626 C  CB  . ASN   B 2 252 ? -28.758 -4.321  -13.259 1.00 25.37  ? 368 ASN   B CB  1 
ATOM   3627 C  CG  . ASN   B 2 252 ? -29.744 -3.443  -12.512 1.00 28.95  ? 368 ASN   B CG  1 
ATOM   3628 O  OD1 . ASN   B 2 252 ? -29.385 -2.429  -11.881 1.00 24.89  ? 368 ASN   B OD1 1 
ATOM   3629 N  ND2 . ASN   B 2 252 ? -31.010 -3.764  -12.682 1.00 26.30  ? 368 ASN   B ND2 1 
ATOM   3630 N  N   . TYR   B 2 253 ? -26.732 -1.296  -13.634 1.00 27.46  ? 369 TYR   B N   1 
ATOM   3631 C  CA  . TYR   B 2 253 ? -26.950 0.129   -14.017 1.00 32.95  ? 369 TYR   B CA  1 
ATOM   3632 C  C   . TYR   B 2 253 ? -26.423 0.327   -15.432 1.00 32.15  ? 369 TYR   B C   1 
ATOM   3633 O  O   . TYR   B 2 253 ? -25.298 -0.103  -15.689 1.00 33.06  ? 369 TYR   B O   1 
ATOM   3634 C  CB  . TYR   B 2 253 ? -26.214 1.122   -13.114 1.00 35.99  ? 369 TYR   B CB  1 
ATOM   3635 C  CG  . TYR   B 2 253 ? -26.298 2.576   -13.544 1.00 34.19  ? 369 TYR   B CG  1 
ATOM   3636 C  CD1 . TYR   B 2 253 ? -27.486 3.268   -13.484 1.00 34.94  ? 369 TYR   B CD1 1 
ATOM   3637 C  CD2 . TYR   B 2 253 ? -25.176 3.272   -13.963 1.00 38.77  ? 369 TYR   B CD2 1 
ATOM   3638 C  CE1 . TYR   B 2 253 ? -27.581 4.595   -13.869 1.00 36.91  ? 369 TYR   B CE1 1 
ATOM   3639 C  CE2 . TYR   B 2 253 ? -25.236 4.615   -14.308 1.00 34.74  ? 369 TYR   B CE2 1 
ATOM   3640 C  CZ  . TYR   B 2 253 ? -26.441 5.281   -14.259 1.00 37.50  ? 369 TYR   B CZ  1 
ATOM   3641 O  OH  . TYR   B 2 253 ? -26.514 6.603   -14.606 1.00 40.48  ? 369 TYR   B OH  1 
ATOM   3642 N  N   . ASN   B 2 254 ? -27.236 0.938   -16.286 1.00 30.55  ? 370 ASN   B N   1 
ATOM   3643 C  CA  . ASN   B 2 254 ? -26.826 1.458   -17.608 1.00 30.83  ? 370 ASN   B CA  1 
ATOM   3644 C  C   . ASN   B 2 254 ? -27.445 2.841   -17.721 1.00 27.19  ? 370 ASN   B C   1 
ATOM   3645 O  O   . ASN   B 2 254 ? -28.661 2.943   -17.635 1.00 25.52  ? 370 ASN   B O   1 
ATOM   3646 C  CB  . ASN   B 2 254 ? -27.292 0.539   -18.740 1.00 30.97  ? 370 ASN   B CB  1 
ATOM   3647 C  CG  . ASN   B 2 254 ? -26.981 1.080   -20.116 1.00 32.66  ? 370 ASN   B CG  1 
ATOM   3648 O  OD1 . ASN   B 2 254 ? -27.533 2.096   -20.548 1.00 32.00  ? 370 ASN   B OD1 1 
ATOM   3649 N  ND2 . ASN   B 2 254 ? -26.098 0.393   -20.806 1.00 33.05  ? 370 ASN   B ND2 1 
ATOM   3650 N  N   . ALA   B 2 255 ? -26.616 3.868   -17.899 1.00 31.55  ? 371 ALA   B N   1 
ATOM   3651 C  CA  . ALA   B 2 255 ? -27.068 5.284   -17.907 1.00 33.15  ? 371 ALA   B CA  1 
ATOM   3652 C  C   . ALA   B 2 255 ? -28.110 5.489   -19.001 1.00 34.98  ? 371 ALA   B C   1 
ATOM   3653 O  O   . ALA   B 2 255 ? -29.112 6.208   -18.771 1.00 30.93  ? 371 ALA   B O   1 
ATOM   3654 C  CB  . ALA   B 2 255 ? -25.885 6.205   -18.084 1.00 34.21  ? 371 ALA   B CB  1 
ATOM   3655 N  N   . GLU   B 2 256 ? -27.910 4.868   -20.162 1.00 32.59  ? 372 GLU   B N   1 
ATOM   3656 C  CA  . GLU   B 2 256 ? -28.842 5.051   -21.300 1.00 35.92  ? 372 GLU   B CA  1 
ATOM   3657 C  C   . GLU   B 2 256 ? -30.180 4.372   -20.980 1.00 33.36  ? 372 GLU   B C   1 
ATOM   3658 O  O   . GLU   B 2 256 ? -31.225 5.001   -21.129 1.00 32.16  ? 372 GLU   B O   1 
ATOM   3659 C  CB  . GLU   B 2 256 ? -28.223 4.570   -22.617 1.00 42.36  ? 372 GLU   B CB  1 
ATOM   3660 C  CG  . GLU   B 2 256 ? -27.103 5.476   -23.090 1.00 51.74  ? 372 GLU   B CG  1 
ATOM   3661 C  CD  . GLU   B 2 256 ? -26.892 5.599   -24.593 1.00 67.57  ? 372 GLU   B CD  1 
ATOM   3662 O  OE1 . GLU   B 2 256 ? -26.151 6.534   -25.003 1.00 85.84  ? 372 GLU   B OE1 1 
ATOM   3663 O  OE2 . GLU   B 2 256 ? -27.447 4.768   -25.360 1.00 66.88  ? 372 GLU   B OE2 1 
ATOM   3664 N  N   . THR   B 2 257 ? -30.164 3.130   -20.530 1.00 28.44  ? 373 THR   B N   1 
ATOM   3665 C  CA  . THR   B 2 257 ? -31.403 2.441   -20.100 1.00 28.62  ? 373 THR   B CA  1 
ATOM   3666 C  C   . THR   B 2 257 ? -32.131 3.268   -19.034 1.00 25.19  ? 373 THR   B C   1 
ATOM   3667 O  O   . THR   B 2 257 ? -33.355 3.377   -19.094 1.00 27.84  ? 373 THR   B O   1 
ATOM   3668 C  CB  . THR   B 2 257 ? -31.087 1.022   -19.613 1.00 32.59  ? 373 THR   B CB  1 
ATOM   3669 O  OG1 . THR   B 2 257 ? -30.330 0.383   -20.642 1.00 33.08  ? 373 THR   B OG1 1 
ATOM   3670 C  CG2 . THR   B 2 257 ? -32.319 0.213   -19.265 1.00 31.58  ? 373 THR   B CG2 1 
ATOM   3671 N  N   . TYR   B 2 258 ? -31.421 3.726   -18.016 1.00 26.22  ? 374 TYR   B N   1 
ATOM   3672 C  CA  . TYR   B 2 258 ? -32.035 4.475   -16.892 1.00 27.57  ? 374 TYR   B CA  1 
ATOM   3673 C  C   . TYR   B 2 258 ? -32.728 5.726   -17.452 1.00 26.95  ? 374 TYR   B C   1 
ATOM   3674 O  O   . TYR   B 2 258 ? -33.914 5.965   -17.152 1.00 26.99  ? 374 TYR   B O   1 
ATOM   3675 C  CB  . TYR   B 2 258 ? -30.970 4.798   -15.837 1.00 25.89  ? 374 TYR   B CB  1 
ATOM   3676 C  CG  . TYR   B 2 258 ? -31.555 5.430   -14.596 1.00 28.13  ? 374 TYR   B CG  1 
ATOM   3677 C  CD1 . TYR   B 2 258 ? -32.476 4.745   -13.807 1.00 25.40  ? 374 TYR   B CD1 1 
ATOM   3678 C  CD2 . TYR   B 2 258 ? -31.186 6.701   -14.197 1.00 28.90  ? 374 TYR   B CD2 1 
ATOM   3679 C  CE1 . TYR   B 2 258 ? -32.992 5.299   -12.653 1.00 26.65  ? 374 TYR   B CE1 1 
ATOM   3680 C  CE2 . TYR   B 2 258 ? -31.717 7.285   -13.056 1.00 29.86  ? 374 TYR   B CE2 1 
ATOM   3681 C  CZ  . TYR   B 2 258 ? -32.606 6.576   -12.273 1.00 29.26  ? 374 TYR   B CZ  1 
ATOM   3682 O  OH  . TYR   B 2 258 ? -33.140 7.163   -11.167 1.00 26.57  ? 374 TYR   B OH  1 
ATOM   3683 N  N   . ALA   B 2 259 ? -31.995 6.525   -18.252 1.00 30.47  ? 375 ALA   B N   1 
ATOM   3684 C  CA  . ALA   B 2 259 ? -32.522 7.753   -18.919 1.00 29.85  ? 375 ALA   B CA  1 
ATOM   3685 C  C   . ALA   B 2 259 ? -33.809 7.436   -19.682 1.00 29.57  ? 375 ALA   B C   1 
ATOM   3686 O  O   . ALA   B 2 259 ? -34.775 8.208   -19.596 1.00 33.48  ? 375 ALA   B O   1 
ATOM   3687 C  CB  . ALA   B 2 259 ? -31.450 8.354   -19.818 1.00 28.77  ? 375 ALA   B CB  1 
ATOM   3688 N  N   . SER   B 2 260 ? -33.856 6.284   -20.353 1.00 30.68  ? 376 SER   B N   1 
ATOM   3689 C  CA  . SER   B 2 260 ? -35.015 5.847   -21.178 1.00 34.94  ? 376 SER   B CA  1 
ATOM   3690 C  C   . SER   B 2 260 ? -36.264 5.658   -20.319 1.00 33.98  ? 376 SER   B C   1 
ATOM   3691 O  O   . SER   B 2 260 ? -37.345 5.761   -20.849 1.00 33.67  ? 376 SER   B O   1 
ATOM   3692 C  CB  . SER   B 2 260 ? -34.692 4.587   -21.952 1.00 33.65  ? 376 SER   B CB  1 
ATOM   3693 O  OG  . SER   B 2 260 ? -34.799 3.433   -21.120 1.00 39.53  ? 376 SER   B OG  1 
ATOM   3694 N  N   . TYR   B 2 261 ? -36.156 5.394   -19.021 1.00 33.27  ? 377 TYR   B N   1 
ATOM   3695 C  CA  . TYR   B 2 261 ? -37.363 5.315   -18.163 1.00 30.71  ? 377 TYR   B CA  1 
ATOM   3696 C  C   . TYR   B 2 261 ? -38.058 6.671   -18.070 1.00 30.57  ? 377 TYR   B C   1 
ATOM   3697 O  O   . TYR   B 2 261 ? -39.229 6.689   -17.702 1.00 29.75  ? 377 TYR   B O   1 
ATOM   3698 C  CB  . TYR   B 2 261 ? -37.033 4.805   -16.757 1.00 34.81  ? 377 TYR   B CB  1 
ATOM   3699 C  CG  . TYR   B 2 261 ? -36.394 3.442   -16.691 1.00 33.07  ? 377 TYR   B CG  1 
ATOM   3700 C  CD1 . TYR   B 2 261 ? -36.685 2.444   -17.609 1.00 37.12  ? 377 TYR   B CD1 1 
ATOM   3701 C  CD2 . TYR   B 2 261 ? -35.504 3.146   -15.676 1.00 34.23  ? 377 TYR   B CD2 1 
ATOM   3702 C  CE1 . TYR   B 2 261 ? -36.090 1.197   -17.525 1.00 37.36  ? 377 TYR   B CE1 1 
ATOM   3703 C  CE2 . TYR   B 2 261 ? -34.927 1.893   -15.561 1.00 37.58  ? 377 TYR   B CE2 1 
ATOM   3704 C  CZ  . TYR   B 2 261 ? -35.223 0.917   -16.491 1.00 36.13  ? 377 TYR   B CZ  1 
ATOM   3705 O  OH  . TYR   B 2 261 ? -34.616 -0.302  -16.380 1.00 39.76  ? 377 TYR   B OH  1 
ATOM   3706 N  N   . PHE   B 2 262 ? -37.342 7.780   -18.276 1.00 33.82  ? 378 PHE   B N   1 
ATOM   3707 C  CA  . PHE   B 2 262 ? -37.867 9.146   -17.999 1.00 38.48  ? 378 PHE   B CA  1 
ATOM   3708 C  C   . PHE   B 2 262 ? -38.009 9.943   -19.311 1.00 40.71  ? 378 PHE   B C   1 
ATOM   3709 O  O   . PHE   B 2 262 ? -38.311 11.137  -19.255 1.00 46.76  ? 378 PHE   B O   1 
ATOM   3710 C  CB  . PHE   B 2 262 ? -36.989 9.867   -16.963 1.00 33.27  ? 378 PHE   B CB  1 
ATOM   3711 C  CG  . PHE   B 2 262 ? -36.632 9.008   -15.788 1.00 29.81  ? 378 PHE   B CG  1 
ATOM   3712 C  CD1 . PHE   B 2 262 ? -37.584 8.733   -14.823 1.00 30.46  ? 378 PHE   B CD1 1 
ATOM   3713 C  CD2 . PHE   B 2 262 ? -35.383 8.414   -15.695 1.00 29.53  ? 378 PHE   B CD2 1 
ATOM   3714 C  CE1 . PHE   B 2 262 ? -37.287 7.898   -13.762 1.00 30.89  ? 378 PHE   B CE1 1 
ATOM   3715 C  CE2 . PHE   B 2 262 ? -35.075 7.587   -14.625 1.00 29.38  ? 378 PHE   B CE2 1 
ATOM   3716 C  CZ  . PHE   B 2 262 ? -36.028 7.338   -13.652 1.00 28.66  ? 378 PHE   B CZ  1 
ATOM   3717 N  N   . SER   B 2 263 ? -37.836 9.284   -20.450 1.00 45.18  ? 379 SER   B N   1 
ATOM   3718 C  CA  . SER   B 2 263 ? -38.017 9.856   -21.810 1.00 47.76  ? 379 SER   B CA  1 
ATOM   3719 C  C   . SER   B 2 263 ? -39.491 10.155  -22.041 1.00 44.00  ? 379 SER   B C   1 
ATOM   3720 O  O   . SER   B 2 263 ? -40.316 9.432   -21.474 1.00 46.15  ? 379 SER   B O   1 
ATOM   3721 C  CB  . SER   B 2 263 ? -37.510 8.896   -22.852 1.00 50.27  ? 379 SER   B CB  1 
ATOM   3722 O  OG  . SER   B 2 263 ? -36.105 8.794   -22.752 1.00 53.77  ? 379 SER   B OG  1 
ATOM   3723 N  N   . ALA   B 2 264 ? -39.788 11.147  -22.884 1.00 42.29  ? 380 ALA   B N   1 
ATOM   3724 C  CA  . ALA   B 2 264 ? -41.149 11.540  -23.310 1.00 47.23  ? 380 ALA   B CA  1 
ATOM   3725 C  C   . ALA   B 2 264 ? -41.898 10.277  -23.695 1.00 43.07  ? 380 ALA   B C   1 
ATOM   3726 O  O   . ALA   B 2 264 ? -41.292 9.402   -24.311 1.00 46.25  ? 380 ALA   B O   1 
ATOM   3727 C  CB  . ALA   B 2 264 ? -41.093 12.517  -24.471 1.00 48.33  ? 380 ALA   B CB  1 
ATOM   3728 N  N   . PRO   B 2 265 ? -43.197 10.130  -23.326 1.00 49.40  ? 381 PRO   B N   1 
ATOM   3729 C  CA  . PRO   B 2 265 ? -43.966 11.175  -22.625 1.00 53.19  ? 381 PRO   B CA  1 
ATOM   3730 C  C   . PRO   B 2 265 ? -43.936 11.234  -21.077 1.00 53.48  ? 381 PRO   B C   1 
ATOM   3731 O  O   . PRO   B 2 265 ? -44.858 11.812  -20.501 1.00 48.33  ? 381 PRO   B O   1 
ATOM   3732 C  CB  . PRO   B 2 265 ? -45.402 10.790  -23.036 1.00 54.79  ? 381 PRO   B CB  1 
ATOM   3733 C  CG  . PRO   B 2 265 ? -45.374 9.272   -23.058 1.00 52.81  ? 381 PRO   B CG  1 
ATOM   3734 C  CD  . PRO   B 2 265 ? -44.000 8.923   -23.593 1.00 51.18  ? 381 PRO   B CD  1 
ATOM   3735 N  N   . ASN   B 2 266 ? -42.881 10.709  -20.440 1.00 52.77  ? 382 ASN   B N   1 
ATOM   3736 C  CA  . ASN   B 2 266 ? -42.861 10.269  -19.019 1.00 53.14  ? 382 ASN   B CA  1 
ATOM   3737 C  C   . ASN   B 2 266 ? -42.012 11.209  -18.157 1.00 54.62  ? 382 ASN   B C   1 
ATOM   3738 O  O   . ASN   B 2 266 ? -41.858 10.919  -16.953 1.00 54.47  ? 382 ASN   B O   1 
ATOM   3739 C  CB  . ASN   B 2 266 ? -42.373 8.819   -18.944 1.00 53.56  ? 382 ASN   B CB  1 
ATOM   3740 C  CG  . ASN   B 2 266 ? -43.408 7.881   -19.526 1.00 57.08  ? 382 ASN   B CG  1 
ATOM   3741 O  OD1 . ASN   B 2 266 ? -44.605 8.128   -19.378 1.00 49.33  ? 382 ASN   B OD1 1 
ATOM   3742 N  ND2 . ASN   B 2 266 ? -42.972 6.829   -20.203 1.00 61.05  ? 382 ASN   B ND2 1 
ATOM   3743 N  N   . SER   B 2 267 ? -41.534 12.312  -18.741 1.00 55.79  ? 383 SER   B N   1 
ATOM   3744 C  CA  . SER   B 2 267 ? -40.457 13.194  -18.206 1.00 62.84  ? 383 SER   B CA  1 
ATOM   3745 C  C   . SER   B 2 267 ? -40.842 13.862  -16.874 1.00 60.63  ? 383 SER   B C   1 
ATOM   3746 O  O   . SER   B 2 267 ? -39.936 14.032  -16.019 1.00 57.80  ? 383 SER   B O   1 
ATOM   3747 C  CB  . SER   B 2 267 ? -40.071 14.229  -19.236 1.00 62.45  ? 383 SER   B CB  1 
ATOM   3748 O  OG  . SER   B 2 267 ? -39.900 13.616  -20.502 1.00 67.96  ? 383 SER   B OG  1 
ATOM   3749 N  N   . TYR   B 2 268 ? -42.114 14.238  -16.711 1.00 62.17  ? 384 TYR   B N   1 
ATOM   3750 C  CA  . TYR   B 2 268 ? -42.601 15.148  -15.637 1.00 64.21  ? 384 TYR   B CA  1 
ATOM   3751 C  C   . TYR   B 2 268 ? -43.524 14.417  -14.649 1.00 59.65  ? 384 TYR   B C   1 
ATOM   3752 O  O   . TYR   B 2 268 ? -44.015 15.087  -13.721 1.00 57.57  ? 384 TYR   B O   1 
ATOM   3753 C  CB  . TYR   B 2 268 ? -43.325 16.350  -16.256 1.00 66.16  ? 384 TYR   B CB  1 
ATOM   3754 C  CG  . TYR   B 2 268 ? -42.554 17.028  -17.362 1.00 70.29  ? 384 TYR   B CG  1 
ATOM   3755 C  CD1 . TYR   B 2 268 ? -41.229 17.398  -17.179 1.00 67.65  ? 384 TYR   B CD1 1 
ATOM   3756 C  CD2 . TYR   B 2 268 ? -43.144 17.294  -18.589 1.00 70.71  ? 384 TYR   B CD2 1 
ATOM   3757 C  CE1 . TYR   B 2 268 ? -40.505 18.010  -18.188 1.00 73.46  ? 384 TYR   B CE1 1 
ATOM   3758 C  CE2 . TYR   B 2 268 ? -42.437 17.919  -19.603 1.00 76.37  ? 384 TYR   B CE2 1 
ATOM   3759 C  CZ  . TYR   B 2 268 ? -41.111 18.272  -19.403 1.00 75.55  ? 384 TYR   B CZ  1 
ATOM   3760 O  OH  . TYR   B 2 268 ? -40.398 18.881  -20.393 1.00 77.02  ? 384 TYR   B OH  1 
ATOM   3761 N  N   . LEU   B 2 269 ? -43.752 13.111  -14.836 1.00 50.46  ? 385 LEU   B N   1 
ATOM   3762 C  CA  . LEU   B 2 269 ? -44.528 12.249  -13.898 1.00 49.60  ? 385 LEU   B CA  1 
ATOM   3763 C  C   . LEU   B 2 269 ? -44.043 12.480  -12.460 1.00 47.32  ? 385 LEU   B C   1 
ATOM   3764 O  O   . LEU   B 2 269 ? -42.828 12.637  -12.255 1.00 46.06  ? 385 LEU   B O   1 
ATOM   3765 C  CB  . LEU   B 2 269 ? -44.345 10.778  -14.293 1.00 51.04  ? 385 LEU   B CB  1 
ATOM   3766 C  CG  . LEU   B 2 269 ? -45.004 10.343  -15.604 1.00 52.67  ? 385 LEU   B CG  1 
ATOM   3767 C  CD1 . LEU   B 2 269 ? -44.936 8.832   -15.764 1.00 54.37  ? 385 LEU   B CD1 1 
ATOM   3768 C  CD2 . LEU   B 2 269 ? -46.443 10.834  -15.678 1.00 54.96  ? 385 LEU   B CD2 1 
ATOM   3769 N  N   . THR   B 2 270 ? -44.966 12.512  -11.506 1.00 46.04  ? 386 THR   B N   1 
ATOM   3770 C  CA  . THR   B 2 270 ? -44.695 12.726  -10.064 1.00 48.93  ? 386 THR   B CA  1 
ATOM   3771 C  C   . THR   B 2 270 ? -44.338 11.387  -9.420  1.00 52.07  ? 386 THR   B C   1 
ATOM   3772 O  O   . THR   B 2 270 ? -43.724 11.409  -8.335  1.00 50.46  ? 386 THR   B O   1 
ATOM   3773 C  CB  . THR   B 2 270 ? -45.920 13.292  -9.341  1.00 47.62  ? 386 THR   B CB  1 
ATOM   3774 O  OG1 . THR   B 2 270 ? -46.967 12.347  -9.529  1.00 44.88  ? 386 THR   B OG1 1 
ATOM   3775 C  CG2 . THR   B 2 270 ? -46.363 14.643  -9.854  1.00 46.94  ? 386 THR   B CG2 1 
ATOM   3776 N  N   . GLY   B 2 271 ? -44.739 10.280  -10.062 1.00 45.83  ? 387 GLY   B N   1 
ATOM   3777 C  CA  . GLY   B 2 271 ? -44.596 8.919   -9.514  1.00 44.26  ? 387 GLY   B CA  1 
ATOM   3778 C  C   . GLY   B 2 271 ? -45.836 8.499   -8.745  1.00 49.42  ? 387 GLY   B C   1 
ATOM   3779 O  O   . GLY   B 2 271 ? -45.807 7.401   -8.163  1.00 51.68  ? 387 GLY   B O   1 
ATOM   3780 N  N   . CYS   B 2 272 ? -46.906 9.306   -8.766  1.00 41.85  ? 388 CYS   B N   1 
ATOM   3781 C  CA  . CYS   B 2 272 ? -48.179 8.991   -8.062  1.00 44.14  ? 388 CYS   B CA  1 
ATOM   3782 C  C   . CYS   B 2 272 ? -49.385 9.034   -9.015  1.00 50.74  ? 388 CYS   B C   1 
ATOM   3783 O  O   . CYS   B 2 272 ? -50.529 9.071   -8.500  1.00 51.18  ? 388 CYS   B O   1 
ATOM   3784 C  CB  . CYS   B 2 272 ? -48.398 9.970   -6.917  1.00 41.21  ? 388 CYS   B CB  1 
ATOM   3785 S  SG  . CYS   B 2 272 ? -47.198 9.768   -5.574  1.00 41.11  ? 388 CYS   B SG  1 
ATOM   3786 N  N   . THR   B 2 273 ? -49.165 9.037   -10.334 1.00 51.73  ? 389 THR   B N   1 
ATOM   3787 C  CA  . THR   B 2 273 ? -50.243 9.132   -11.367 1.00 56.19  ? 389 THR   B CA  1 
ATOM   3788 C  C   . THR   B 2 273 ? -50.223 7.892   -12.275 1.00 58.74  ? 389 THR   B C   1 
ATOM   3789 O  O   . THR   B 2 273 ? -49.233 7.120   -12.226 1.00 51.25  ? 389 THR   B O   1 
ATOM   3790 C  CB  . THR   B 2 273 ? -50.107 10.409  -12.207 1.00 56.24  ? 389 THR   B CB  1 
ATOM   3791 O  OG1 . THR   B 2 273 ? -48.843 10.346  -12.868 1.00 53.88  ? 389 THR   B OG1 1 
ATOM   3792 C  CG2 . THR   B 2 273 ? -50.206 11.674  -11.383 1.00 55.53  ? 389 THR   B CG2 1 
ATOM   3793 N  N   . GLU   B 2 274 ? -51.272 7.723   -13.088 1.00 61.97  ? 390 GLU   B N   1 
ATOM   3794 C  CA  . GLU   B 2 274 ? -51.404 6.609   -14.074 1.00 73.17  ? 390 GLU   B CA  1 
ATOM   3795 C  C   . GLU   B 2 274 ? -50.213 6.632   -15.048 1.00 73.83  ? 390 GLU   B C   1 
ATOM   3796 O  O   . GLU   B 2 274 ? -49.848 7.733   -15.533 1.00 67.94  ? 390 GLU   B O   1 
ATOM   3797 C  CB  . GLU   B 2 274 ? -52.728 6.705   -14.848 1.00 77.59  ? 390 GLU   B CB  1 
ATOM   3798 C  CG  . GLU   B 2 274 ? -53.906 6.033   -14.153 1.00 85.72  ? 390 GLU   B CG  1 
ATOM   3799 C  CD  . GLU   B 2 274 ? -54.496 6.749   -12.941 1.00 94.81  ? 390 GLU   B CD  1 
ATOM   3800 O  OE1 . GLU   B 2 274 ? -53.986 7.839   -12.562 1.00 93.32  ? 390 GLU   B OE1 1 
ATOM   3801 O  OE2 . GLU   B 2 274 ? -55.483 6.216   -12.373 1.00 97.97  ? 390 GLU   B OE2 1 
ATOM   3802 N  N   . GLU   B 2 275 ? -49.627 5.469   -15.350 1.00 77.79  ? 391 GLU   B N   1 
ATOM   3803 C  CA  . GLU   B 2 275 ? -48.616 5.363   -16.438 1.00 85.22  ? 391 GLU   B CA  1 
ATOM   3804 C  C   . GLU   B 2 275 ? -49.309 5.814   -17.735 1.00 81.81  ? 391 GLU   B C   1 
ATOM   3805 O  O   . GLU   B 2 275 ? -50.531 5.571   -17.877 1.00 71.67  ? 391 GLU   B O   1 
ATOM   3806 C  CB  . GLU   B 2 275 ? -48.004 3.959   -16.512 1.00 90.13  ? 391 GLU   B CB  1 
ATOM   3807 C  CG  . GLU   B 2 275 ? -46.527 3.953   -16.912 1.00 98.72  ? 391 GLU   B CG  1 
ATOM   3808 C  CD  . GLU   B 2 275 ? -45.522 4.407   -15.853 1.00 99.80  ? 391 GLU   B CD  1 
ATOM   3809 O  OE1 . GLU   B 2 275 ? -44.880 3.515   -15.230 1.00 87.76  ? 391 GLU   B OE1 1 
ATOM   3810 O  OE2 . GLU   B 2 275 ? -45.352 5.653   -15.671 1.00 81.73  ? 391 GLU   B OE2 1 
ATOM   3811 N  N   . ILE   B 2 276 ? -48.578 6.502   -18.616 1.00 84.96  ? 392 ILE   B N   1 
ATOM   3812 C  CA  . ILE   B 2 276 ? -49.124 7.107   -19.870 1.00 84.14  ? 392 ILE   B CA  1 
ATOM   3813 C  C   . ILE   B 2 276 ? -49.241 5.998   -20.927 1.00 77.93  ? 392 ILE   B C   1 
ATOM   3814 O  O   . ILE   B 2 276 ? -48.256 5.261   -21.136 1.00 68.61  ? 392 ILE   B O   1 
ATOM   3815 C  CB  . ILE   B 2 276 ? -48.263 8.300   -20.346 1.00 85.87  ? 392 ILE   B CB  1 
ATOM   3816 C  CG1 . ILE   B 2 276 ? -47.938 9.274   -19.209 1.00 82.92  ? 392 ILE   B CG1 1 
ATOM   3817 C  CG2 . ILE   B 2 276 ? -48.930 9.019   -21.513 1.00 86.56  ? 392 ILE   B CG2 1 
ATOM   3818 C  CD1 . ILE   B 2 276 ? -49.154 9.848   -18.512 1.00 83.39  ? 392 ILE   B CD1 1 
ATOM   3819 N  N   . GLU   B 2 277 ? -50.410 5.876   -21.562 1.00 77.48  ? 393 GLU   B N   1 
ATOM   3820 C  CA  . GLU   B 2 277 ? -50.743 4.742   -22.467 1.00 84.04  ? 393 GLU   B CA  1 
ATOM   3821 C  C   . GLU   B 2 277 ? -49.995 4.860   -23.811 1.00 81.47  ? 393 GLU   B C   1 
ATOM   3822 O  O   . GLU   B 2 277 ? -49.822 6.008   -24.300 1.00 66.62  ? 393 GLU   B O   1 
ATOM   3823 C  CB  . GLU   B 2 277 ? -52.256 4.678   -22.669 1.00 85.93  ? 393 GLU   B CB  1 
ATOM   3824 C  CG  . GLU   B 2 277 ? -52.737 3.304   -23.086 1.00 94.28  ? 393 GLU   B CG  1 
ATOM   3825 C  CD  . GLU   B 2 277 ? -54.246 3.194   -23.200 1.00 102.26 ? 393 GLU   B CD  1 
ATOM   3826 O  OE1 . GLU   B 2 277 ? -54.898 4.251   -23.322 1.00 100.29 ? 393 GLU   B OE1 1 
ATOM   3827 O  OE2 . GLU   B 2 277 ? -54.765 2.052   -23.209 1.00 106.04 ? 393 GLU   B OE2 1 
ATOM   3828 N  N   . ARG   B 2 278 ? -49.582 3.707   -24.377 1.00 83.16  ? 394 ARG   B N   1 
ATOM   3829 C  CA  . ARG   B 2 278 ? -48.908 3.550   -25.706 1.00 83.18  ? 394 ARG   B CA  1 
ATOM   3830 C  C   . ARG   B 2 278 ? -49.622 2.483   -26.561 1.00 80.64  ? 394 ARG   B C   1 
ATOM   3831 O  O   . ARG   B 2 278 ? -50.710 2.004   -26.147 1.00 71.91  ? 394 ARG   B O   1 
ATOM   3832 C  CB  . ARG   B 2 278 ? -47.429 3.181   -25.520 1.00 80.02  ? 394 ARG   B CB  1 
ATOM   3833 C  CG  . ARG   B 2 278 ? -47.148 1.729   -25.138 1.00 73.54  ? 394 ARG   B CG  1 
ATOM   3834 C  CD  . ARG   B 2 278 ? -45.751 1.550   -24.555 1.00 74.79  ? 394 ARG   B CD  1 
ATOM   3835 N  NE  . ARG   B 2 278 ? -45.532 2.575   -23.536 1.00 85.32  ? 394 ARG   B NE  1 
ATOM   3836 C  CZ  . ARG   B 2 278 ? -44.402 3.251   -23.323 1.00 85.82  ? 394 ARG   B CZ  1 
ATOM   3837 N  NH1 . ARG   B 2 278 ? -43.317 3.012   -24.045 1.00 83.67  ? 394 ARG   B NH1 1 
ATOM   3838 N  NH2 . ARG   B 2 278 ? -44.367 4.174   -22.376 1.00 86.84  ? 394 ARG   B NH2 1 
ATOM   3839 N  N   . LEU   B 2 279 ? -49.041 2.153   -27.726 1.00 91.20  ? 395 LEU   B N   1 
ATOM   3840 C  CA  . LEU   B 2 279 ? -49.421 1.011   -28.613 1.00 94.79  ? 395 LEU   B CA  1 
ATOM   3841 C  C   . LEU   B 2 279 ? -48.154 0.430   -29.271 1.00 95.99  ? 395 LEU   B C   1 
ATOM   3842 O  O   . LEU   B 2 279 ? -47.225 -0.096  -28.632 1.00 99.55  ? 395 LEU   B O   1 
ATOM   3843 C  CB  . LEU   B 2 279 ? -50.420 1.487   -29.678 1.00 91.82  ? 395 LEU   B CB  1 
ATOM   3844 C  CG  . LEU   B 2 279 ? -51.797 1.919   -29.172 1.00 95.78  ? 395 LEU   B CG  1 
ATOM   3845 C  CD1 . LEU   B 2 279 ? -52.585 2.614   -30.276 1.00 91.09  ? 395 LEU   B CD1 1 
ATOM   3846 C  CD2 . LEU   B 2 279 ? -52.568 0.728   -28.616 1.00 93.39  ? 395 LEU   B CD2 1 
ATOM   3847 O  OXT . LEU   B 2 279 ? -48.014 0.466   -30.496 1.00 84.73  ? 395 LEU   B OXT 1 
HETATM 3848 C  C1  . A1IIM C 3 .   ? -40.505 41.934  22.837  1.00 39.02  ? 601 A1IIM A C1  1 
HETATM 3849 C  C2  . A1IIM C 3 .   ? -40.916 42.030  21.392  1.00 39.73  ? 601 A1IIM A C2  1 
HETATM 3850 C  C3  . A1IIM C 3 .   ? -42.237 41.316  21.312  1.00 38.84  ? 601 A1IIM A C3  1 
HETATM 3851 C  C4  . A1IIM C 3 .   ? -42.145 40.217  22.327  1.00 36.44  ? 601 A1IIM A C4  1 
HETATM 3852 N  N1  . A1IIM C 3 .   ? -41.185 40.728  23.297  1.00 34.17  ? 601 A1IIM A N1  1 
HETATM 3853 C  C5  . A1IIM C 3 .   ? -40.930 40.152  24.496  1.00 33.55  ? 601 A1IIM A C5  1 
HETATM 3854 C  C6  . A1IIM C 3 .   ? -39.964 40.685  25.368  1.00 30.76  ? 601 A1IIM A C6  1 
HETATM 3855 N  N2  . A1IIM C 3 .   ? -39.727 40.163  26.566  1.00 30.27  ? 601 A1IIM A N2  1 
HETATM 3856 C  C7  . A1IIM C 3 .   ? -40.408 39.070  26.897  1.00 33.60  ? 601 A1IIM A C7  1 
HETATM 3857 C  C8  . A1IIM C 3 .   ? -41.349 38.515  26.036  1.00 30.62  ? 601 A1IIM A C8  1 
HETATM 3858 N  N3  . A1IIM C 3 .   ? -41.605 39.046  24.830  1.00 30.10  ? 601 A1IIM A N3  1 
HETATM 3859 C  C9  . A1IIM C 3 .   ? -42.120 37.339  26.417  1.00 30.28  ? 601 A1IIM A C9  1 
HETATM 3860 C  C10 . A1IIM C 3 .   ? -43.058 36.661  25.691  1.00 31.40  ? 601 A1IIM A C10 1 
HETATM 3861 N  N4  . A1IIM C 3 .   ? -43.448 35.657  26.494  1.00 31.24  ? 601 A1IIM A N4  1 
HETATM 3862 N  N5  . A1IIM C 3 .   ? -42.832 35.731  27.715  1.00 32.76  ? 601 A1IIM A N5  1 
HETATM 3863 N  N6  . A1IIM C 3 .   ? -41.996 36.752  27.642  1.00 31.98  ? 601 A1IIM A N6  1 
HETATM 3864 C  C11 . A1IIM C 3 .   ? -44.459 34.656  26.222  1.00 34.59  ? 601 A1IIM A C11 1 
HETATM 3865 C  C12 . A1IIM C 3 .   ? -44.727 33.784  27.446  1.00 33.34  ? 601 A1IIM A C12 1 
HETATM 3866 N  N7  . A1IIM C 3 .   ? -44.148 33.814  25.058  1.00 35.79  ? 601 A1IIM A N7  1 
HETATM 3867 C  C13 . A1IIM C 3 .   ? -43.201 32.831  25.166  1.00 37.40  ? 601 A1IIM A C13 1 
HETATM 3868 C  C14 . A1IIM C 3 .   ? -42.949 31.993  24.139  1.00 31.68  ? 601 A1IIM A C14 1 
HETATM 3869 C  C15 . A1IIM C 3 .   ? -43.668 32.115  22.941  1.00 34.95  ? 601 A1IIM A C15 1 
HETATM 3870 C  C16 . A1IIM C 3 .   ? -44.668 33.085  22.841  1.00 36.23  ? 601 A1IIM A C16 1 
HETATM 3871 C  C17 . A1IIM C 3 .   ? -44.931 33.955  23.906  1.00 34.67  ? 601 A1IIM A C17 1 
HETATM 3872 O  O1  . A1IIM C 3 .   ? -45.760 34.871  23.836  1.00 38.80  ? 601 A1IIM A O1  1 
HETATM 3873 N  N8  . A1IIM C 3 .   ? -43.521 31.242  21.907  1.00 33.68  ? 601 A1IIM A N8  1 
HETATM 3874 C  C18 . A1IIM C 3 .   ? -44.432 31.174  20.770  1.00 33.13  ? 601 A1IIM A C18 1 
HETATM 3875 C  C19 . A1IIM C 3 .   ? -45.331 29.971  20.967  1.00 34.23  ? 601 A1IIM A C19 1 
HETATM 3876 C  C20 . A1IIM C 3 .   ? -44.514 28.679  21.035  1.00 33.24  ? 601 A1IIM A C20 1 
HETATM 3877 C  C21 . A1IIM C 3 .   ? -43.385 28.786  22.057  1.00 33.98  ? 601 A1IIM A C21 1 
HETATM 3878 C  C22 . A1IIM C 3 .   ? -42.601 30.103  21.912  1.00 34.65  ? 601 A1IIM A C22 1 
HETATM 3879 N  N9  . A1IIM C 3 .   ? -42.429 27.667  21.958  1.00 32.66  ? 601 A1IIM A N9  1 
HETATM 3880 C  C23 . A1IIM C 3 .   ? -43.046 26.353  22.193  1.00 35.50  ? 601 A1IIM A C23 1 
HETATM 3881 C  C24 . A1IIM C 3 .   ? -41.966 25.334  22.363  1.00 36.31  ? 601 A1IIM A C24 1 
HETATM 3882 C  C25 . A1IIM C 3 .   ? -41.382 25.155  23.717  1.00 39.04  ? 601 A1IIM A C25 1 
HETATM 3883 C  C26 . A1IIM C 3 .   ? -42.232 24.082  23.111  1.00 38.48  ? 601 A1IIM A C26 1 
HETATM 3884 CA CA  . CA    D 4 .   ? -20.559 14.233  34.996  1.00 80.25  ? 602 CA    A CA  1 
HETATM 3885 CA CA  . CA    E 4 .   ? -13.685 7.039   3.033   1.00 91.25  ? 401 CA    B CA  1 
HETATM 3886 CA CA  . CA    F 4 .   ? -31.237 25.756  5.898   1.00 44.00  ? 402 CA    B CA  1 
HETATM 3887 O  O   . HOH   G 5 .   ? -45.232 23.569  16.157  1.00 54.92  ? 701 HOH   A O   1 
HETATM 3888 O  O   . HOH   G 5 .   ? -46.279 24.186  22.800  1.00 53.16  ? 702 HOH   A O   1 
HETATM 3889 O  O   . HOH   G 5 .   ? -31.935 41.101  28.799  1.00 43.03  ? 703 HOH   A O   1 
HETATM 3890 O  O   . HOH   G 5 .   ? -44.824 26.448  39.372  1.00 48.02  ? 704 HOH   A O   1 
HETATM 3891 O  O   . HOH   G 5 .   ? -31.139 27.655  44.286  1.00 61.89  ? 705 HOH   A O   1 
HETATM 3892 O  O   . HOH   G 5 .   ? -26.846 34.286  44.527  1.00 47.49  ? 706 HOH   A O   1 
HETATM 3893 O  O   . HOH   G 5 .   ? -33.356 19.571  43.574  1.00 54.00  ? 707 HOH   A O   1 
HETATM 3894 O  O   . HOH   G 5 .   ? -25.771 38.145  35.285  1.00 42.52  ? 708 HOH   A O   1 
HETATM 3895 O  O   . HOH   G 5 .   ? -32.773 48.200  31.804  1.00 45.40  ? 709 HOH   A O   1 
HETATM 3896 O  O   . HOH   G 5 .   ? -50.556 25.817  25.718  1.00 60.98  ? 710 HOH   A O   1 
HETATM 3897 O  O   . HOH   G 5 .   ? -34.126 27.605  8.220   1.00 43.82  ? 711 HOH   A O   1 
HETATM 3898 O  O   . HOH   G 5 .   ? -29.442 14.606  21.665  1.00 38.39  ? 712 HOH   A O   1 
HETATM 3899 O  O   . HOH   G 5 .   ? -44.547 37.127  22.594  1.00 39.03  ? 713 HOH   A O   1 
HETATM 3900 O  O   . HOH   G 5 .   ? -21.831 18.853  18.809  1.00 50.52  ? 714 HOH   A O   1 
HETATM 3901 O  O   . HOH   G 5 .   ? -34.509 44.417  15.062  1.00 45.91  ? 715 HOH   A O   1 
HETATM 3902 O  O   . HOH   G 5 .   ? -25.156 47.193  35.190  1.00 54.69  ? 716 HOH   A O   1 
HETATM 3903 O  O   . HOH   G 5 .   ? -42.313 29.558  27.467  1.00 32.55  ? 717 HOH   A O   1 
HETATM 3904 O  O   . HOH   G 5 .   ? -17.826 30.046  25.504  1.00 46.77  ? 718 HOH   A O   1 
HETATM 3905 O  O   . HOH   G 5 .   ? -53.112 13.013  32.250  1.00 60.47  ? 719 HOH   A O   1 
HETATM 3906 O  O   . HOH   G 5 .   ? -27.591 28.099  11.674  1.00 29.54  ? 720 HOH   A O   1 
HETATM 3907 O  O   . HOH   G 5 .   ? -30.837 6.771   34.053  1.00 37.25  ? 721 HOH   A O   1 
HETATM 3908 O  O   . HOH   G 5 .   ? -31.578 37.641  10.333  1.00 54.01  ? 722 HOH   A O   1 
HETATM 3909 O  O   . HOH   G 5 .   ? -25.883 42.429  24.147  1.00 53.00  ? 723 HOH   A O   1 
HETATM 3910 O  O   . HOH   G 5 .   ? -20.140 33.417  26.022  1.00 37.83  ? 724 HOH   A O   1 
HETATM 3911 O  O   . HOH   G 5 .   ? -35.051 46.339  20.031  1.00 45.95  ? 725 HOH   A O   1 
HETATM 3912 O  O   . HOH   G 5 .   ? -42.609 32.268  17.462  1.00 34.83  ? 726 HOH   A O   1 
HETATM 3913 O  O   . HOH   G 5 .   ? -36.493 12.125  28.421  1.00 31.38  ? 727 HOH   A O   1 
HETATM 3914 O  O   . HOH   G 5 .   ? -43.793 12.289  30.509  1.00 32.04  ? 728 HOH   A O   1 
HETATM 3915 O  O   . HOH   G 5 .   ? -35.559 37.582  9.923   1.00 37.07  ? 729 HOH   A O   1 
HETATM 3916 O  O   . HOH   G 5 .   ? -39.589 22.435  17.104  1.00 30.42  ? 730 HOH   A O   1 
HETATM 3917 O  O   . HOH   G 5 .   ? -25.295 38.666  22.853  1.00 37.86  ? 731 HOH   A O   1 
HETATM 3918 O  O   . HOH   G 5 .   ? -36.340 39.206  12.024  1.00 34.80  ? 732 HOH   A O   1 
HETATM 3919 O  O   . HOH   G 5 .   ? -46.551 20.748  9.412   1.00 44.80  ? 733 HOH   A O   1 
HETATM 3920 O  O   . HOH   G 5 .   ? -38.730 28.998  35.658  1.00 31.40  ? 734 HOH   A O   1 
HETATM 3921 O  O   . HOH   G 5 .   ? -47.590 26.884  22.755  1.00 53.44  ? 735 HOH   A O   1 
HETATM 3922 O  O   . HOH   G 5 .   ? -49.555 37.343  35.151  1.00 40.48  ? 736 HOH   A O   1 
HETATM 3923 O  O   . HOH   G 5 .   ? -32.480 42.267  22.340  1.00 30.93  ? 737 HOH   A O   1 
HETATM 3924 O  O   . HOH   G 5 .   ? -31.144 42.886  24.791  1.00 33.38  ? 738 HOH   A O   1 
HETATM 3925 O  O   . HOH   G 5 .   ? -46.657 37.851  25.646  1.00 45.03  ? 739 HOH   A O   1 
HETATM 3926 O  O   . HOH   G 5 .   ? -47.031 14.652  30.698  1.00 47.35  ? 740 HOH   A O   1 
HETATM 3927 O  O   . HOH   G 5 .   ? -33.055 21.412  15.200  1.00 22.02  ? 741 HOH   A O   1 
HETATM 3928 O  O   . HOH   G 5 .   ? -18.413 34.341  29.701  1.00 50.94  ? 742 HOH   A O   1 
HETATM 3929 O  O   . HOH   G 5 .   ? -22.233 21.581  38.999  1.00 43.21  ? 743 HOH   A O   1 
HETATM 3930 O  O   . HOH   G 5 .   ? -39.078 28.956  21.289  1.00 29.13  ? 744 HOH   A O   1 
HETATM 3931 O  O   . HOH   G 5 .   ? -39.050 30.545  39.289  1.00 33.67  ? 745 HOH   A O   1 
HETATM 3932 O  O   . HOH   G 5 .   ? -46.021 18.240  31.076  1.00 44.55  ? 746 HOH   A O   1 
HETATM 3933 O  O   . HOH   G 5 .   ? -44.168 35.739  30.175  1.00 40.82  ? 747 HOH   A O   1 
HETATM 3934 O  O   . HOH   G 5 .   ? -31.151 14.472  33.523  1.00 29.46  ? 748 HOH   A O   1 
HETATM 3935 O  O   . HOH   G 5 .   ? -21.191 25.381  14.942  1.00 34.10  ? 749 HOH   A O   1 
HETATM 3936 O  O   . HOH   G 5 .   ? -43.845 26.028  18.443  1.00 47.16  ? 750 HOH   A O   1 
HETATM 3937 O  O   . HOH   G 5 .   ? -34.811 51.607  33.691  1.00 68.63  ? 751 HOH   A O   1 
HETATM 3938 O  O   . HOH   G 5 .   ? -39.730 42.824  18.080  1.00 36.12  ? 752 HOH   A O   1 
HETATM 3939 O  O   . HOH   G 5 .   ? -29.746 13.603  39.930  1.00 43.75  ? 753 HOH   A O   1 
HETATM 3940 O  O   . HOH   G 5 .   ? -38.078 29.014  28.622  1.00 43.08  ? 754 HOH   A O   1 
HETATM 3941 O  O   . HOH   G 5 .   ? -39.566 24.221  20.326  1.00 38.06  ? 755 HOH   A O   1 
HETATM 3942 O  O   . HOH   G 5 .   ? -46.433 29.700  16.951  1.00 44.55  ? 756 HOH   A O   1 
HETATM 3943 O  O   . HOH   G 5 .   ? -26.168 16.115  19.392  1.00 28.71  ? 757 HOH   A O   1 
HETATM 3944 O  O   . HOH   G 5 .   ? -17.603 35.965  34.354  1.00 61.74  ? 758 HOH   A O   1 
HETATM 3945 O  O   . HOH   G 5 .   ? -48.070 22.430  26.685  1.00 47.13  ? 759 HOH   A O   1 
HETATM 3946 O  O   . HOH   G 5 .   ? -21.434 25.257  36.636  1.00 43.87  ? 760 HOH   A O   1 
HETATM 3947 O  O   . HOH   G 5 .   ? -43.839 24.521  34.603  1.00 48.53  ? 761 HOH   A O   1 
HETATM 3948 O  O   . HOH   G 5 .   ? -18.479 25.600  24.668  1.00 43.84  ? 762 HOH   A O   1 
HETATM 3949 O  O   . HOH   G 5 .   ? -40.034 28.793  9.948   1.00 38.32  ? 763 HOH   A O   1 
HETATM 3950 O  O   . HOH   G 5 .   ? -48.917 30.257  32.990  1.00 38.73  ? 764 HOH   A O   1 
HETATM 3951 O  O   . HOH   G 5 .   ? -24.269 26.149  14.045  1.00 40.28  ? 765 HOH   A O   1 
HETATM 3952 O  O   . HOH   G 5 .   ? -23.527 32.529  29.221  1.00 29.08  ? 766 HOH   A O   1 
HETATM 3953 O  O   . HOH   G 5 .   ? -26.340 46.307  40.585  1.00 47.92  ? 767 HOH   A O   1 
HETATM 3954 O  O   . HOH   G 5 .   ? -20.362 35.060  32.212  1.00 48.03  ? 768 HOH   A O   1 
HETATM 3955 O  O   . HOH   G 5 .   ? -31.028 32.891  43.388  1.00 45.83  ? 769 HOH   A O   1 
HETATM 3956 O  O   . HOH   G 5 .   ? -42.885 35.260  12.484  1.00 49.06  ? 770 HOH   A O   1 
HETATM 3957 O  O   . HOH   G 5 .   ? -36.288 35.848  15.603  1.00 28.15  ? 771 HOH   A O   1 
HETATM 3958 O  O   . HOH   G 5 .   ? -41.539 27.703  19.338  1.00 39.70  ? 772 HOH   A O   1 
HETATM 3959 O  O   . HOH   G 5 .   ? -25.422 19.794  41.445  1.00 39.66  ? 773 HOH   A O   1 
HETATM 3960 O  O   . HOH   G 5 .   ? -39.275 45.994  31.087  1.00 48.72  ? 774 HOH   A O   1 
HETATM 3961 O  O   . HOH   G 5 .   ? -35.126 22.146  37.489  1.00 36.75  ? 775 HOH   A O   1 
HETATM 3962 O  O   . HOH   G 5 .   ? -35.237 30.784  42.846  1.00 40.80  ? 776 HOH   A O   1 
HETATM 3963 O  O   . HOH   G 5 .   ? -19.250 23.597  36.835  1.00 50.26  ? 777 HOH   A O   1 
HETATM 3964 O  O   . HOH   G 5 .   ? -35.574 10.381  30.252  1.00 36.57  ? 778 HOH   A O   1 
HETATM 3965 O  O   . HOH   G 5 .   ? -16.884 27.285  26.003  1.00 49.01  ? 779 HOH   A O   1 
HETATM 3966 O  O   . HOH   G 5 .   ? -52.189 38.139  40.921  1.00 44.46  ? 780 HOH   A O   1 
HETATM 3967 O  O   . HOH   G 5 .   ? -26.486 30.458  47.862  1.00 71.24  ? 781 HOH   A O   1 
HETATM 3968 O  O   . HOH   G 5 .   ? -18.846 38.285  34.287  1.00 56.71  ? 782 HOH   A O   1 
HETATM 3969 O  O   . HOH   G 5 .   ? -44.348 28.286  28.670  1.00 43.09  ? 783 HOH   A O   1 
HETATM 3970 O  O   . HOH   G 5 .   ? -47.884 39.400  22.196  1.00 46.64  ? 784 HOH   A O   1 
HETATM 3971 O  O   . HOH   G 5 .   ? -40.696 18.061  36.459  1.00 54.44  ? 785 HOH   A O   1 
HETATM 3972 O  O   . HOH   G 5 .   ? -39.417 14.371  37.440  1.00 44.34  ? 786 HOH   A O   1 
HETATM 3973 O  O   . HOH   G 5 .   ? -14.866 29.421  33.787  1.00 48.25  ? 787 HOH   A O   1 
HETATM 3974 O  O   . HOH   G 5 .   ? -22.668 24.124  17.845  1.00 27.31  ? 788 HOH   A O   1 
HETATM 3975 O  O   . HOH   G 5 .   ? -48.093 33.069  25.653  1.00 50.37  ? 789 HOH   A O   1 
HETATM 3976 O  O   . HOH   G 5 .   ? -21.574 40.164  27.791  1.00 48.60  ? 790 HOH   A O   1 
HETATM 3977 O  O   . HOH   G 5 .   ? -30.009 41.521  26.866  1.00 33.11  ? 791 HOH   A O   1 
HETATM 3978 O  O   . HOH   G 5 .   ? -40.338 22.999  12.850  1.00 40.85  ? 792 HOH   A O   1 
HETATM 3979 O  O   . HOH   G 5 .   ? -25.362 44.952  30.934  1.00 52.84  ? 793 HOH   A O   1 
HETATM 3980 O  O   . HOH   G 5 .   ? -19.020 22.920  39.447  1.00 44.31  ? 794 HOH   A O   1 
HETATM 3981 O  O   . HOH   G 5 .   ? -48.093 11.370  27.660  1.00 48.54  ? 795 HOH   A O   1 
HETATM 3982 O  O   . HOH   G 5 .   ? -46.243 23.276  20.406  1.00 55.93  ? 796 HOH   A O   1 
HETATM 3983 O  O   . HOH   G 5 .   ? -29.047 13.334  32.218  1.00 33.25  ? 797 HOH   A O   1 
HETATM 3984 O  O   . HOH   G 5 .   ? -47.206 20.770  28.188  1.00 52.67  ? 798 HOH   A O   1 
HETATM 3985 O  O   . HOH   G 5 .   ? -25.581 15.174  41.944  1.00 59.43  ? 799 HOH   A O   1 
HETATM 3986 O  O   . HOH   G 5 .   ? -45.317 39.398  24.025  1.00 47.87  ? 800 HOH   A O   1 
HETATM 3987 O  O   . HOH   G 5 .   ? -22.174 29.515  35.603  1.00 47.23  ? 801 HOH   A O   1 
HETATM 3988 O  O   . HOH   G 5 .   ? -24.449 20.436  38.814  1.00 48.77  ? 802 HOH   A O   1 
HETATM 3989 O  O   . HOH   G 5 .   ? -23.114 38.617  35.626  1.00 43.24  ? 803 HOH   A O   1 
HETATM 3990 O  O   . HOH   G 5 .   ? -42.479 43.147  26.037  1.00 44.75  ? 804 HOH   A O   1 
HETATM 3991 O  O   . HOH   G 5 .   ? -17.698 35.192  37.471  1.00 62.29  ? 805 HOH   A O   1 
HETATM 3992 O  O   . HOH   G 5 .   ? -41.320 11.785  28.989  1.00 28.78  ? 806 HOH   A O   1 
HETATM 3993 O  O   . HOH   G 5 .   ? -33.441 41.357  12.595  1.00 39.55  ? 807 HOH   A O   1 
HETATM 3994 O  O   . HOH   G 5 .   ? -23.879 29.630  40.039  1.00 58.60  ? 808 HOH   A O   1 
HETATM 3995 O  O   . HOH   G 5 .   ? -41.166 30.357  18.664  1.00 41.25  ? 809 HOH   A O   1 
HETATM 3996 O  O   . HOH   G 5 .   ? -16.251 24.753  36.595  1.00 57.80  ? 810 HOH   A O   1 
HETATM 3997 O  O   . HOH   G 5 .   ? -39.864 40.069  14.359  1.00 50.67  ? 811 HOH   A O   1 
HETATM 3998 O  O   . HOH   G 5 .   ? -27.588 43.009  30.388  1.00 37.57  ? 812 HOH   A O   1 
HETATM 3999 O  O   . HOH   G 5 .   ? -20.164 13.343  31.846  1.00 75.22  ? 813 HOH   A O   1 
HETATM 4000 O  O   . HOH   G 5 .   ? -43.991 41.270  16.723  1.00 47.15  ? 814 HOH   A O   1 
HETATM 4001 O  O   . HOH   G 5 .   ? -19.777 37.446  30.119  1.00 54.50  ? 815 HOH   A O   1 
HETATM 4002 O  O   . HOH   G 5 .   ? -56.613 14.350  25.883  1.00 59.93  ? 816 HOH   A O   1 
HETATM 4003 O  O   . HOH   G 5 .   ? -25.418 27.320  41.207  1.00 58.68  ? 817 HOH   A O   1 
HETATM 4004 O  O   . HOH   G 5 .   ? -39.364 26.846  19.536  1.00 34.40  ? 818 HOH   A O   1 
HETATM 4005 O  O   . HOH   G 5 .   ? -23.463 34.264  40.966  1.00 39.26  ? 819 HOH   A O   1 
HETATM 4006 O  O   . HOH   G 5 .   ? -25.517 48.492  39.038  1.00 56.75  ? 820 HOH   A O   1 
HETATM 4007 O  O   . HOH   G 5 .   ? -29.688 45.990  29.034  1.00 59.50  ? 821 HOH   A O   1 
HETATM 4008 O  O   . HOH   G 5 .   ? -35.214 48.170  44.147  1.00 55.65  ? 822 HOH   A O   1 
HETATM 4009 O  O   . HOH   G 5 .   ? -32.772 44.774  21.320  1.00 43.44  ? 823 HOH   A O   1 
HETATM 4010 O  O   . HOH   G 5 .   ? -32.423 30.292  42.963  1.00 44.66  ? 824 HOH   A O   1 
HETATM 4011 O  O   . HOH   G 5 .   ? -53.805 23.198  11.637  1.00 57.20  ? 825 HOH   A O   1 
HETATM 4012 O  O   . HOH   G 5 .   ? -18.205 14.679  30.745  1.00 69.83  ? 826 HOH   A O   1 
HETATM 4013 O  O   . HOH   G 5 .   ? -45.292 21.717  0.006   1.00 53.29  ? 827 HOH   A O   1 
HETATM 4014 O  O   . HOH   G 5 .   ? -28.613 43.540  28.113  1.00 44.16  ? 828 HOH   A O   1 
HETATM 4015 O  O   . HOH   G 5 .   ? -18.868 26.327  16.543  1.00 38.13  ? 829 HOH   A O   1 
HETATM 4016 O  O   . HOH   G 5 .   ? -25.291 41.129  18.474  1.00 52.94  ? 830 HOH   A O   1 
HETATM 4017 O  O   . HOH   G 5 .   ? -18.120 15.742  40.345  1.00 50.99  ? 831 HOH   A O   1 
HETATM 4018 O  O   . HOH   G 5 .   ? -42.257 27.027  10.522  1.00 61.22  ? 832 HOH   A O   1 
HETATM 4019 O  O   . HOH   G 5 .   ? -26.495 44.184  26.560  1.00 52.09  ? 833 HOH   A O   1 
HETATM 4020 O  O   . HOH   G 5 .   ? -33.207 30.101  7.894   1.00 53.79  ? 834 HOH   A O   1 
HETATM 4021 O  O   . HOH   G 5 .   ? -48.339 22.799  23.198  1.00 52.89  ? 835 HOH   A O   1 
HETATM 4022 O  O   . HOH   G 5 .   ? -55.371 18.789  13.445  1.00 66.44  ? 836 HOH   A O   1 
HETATM 4023 O  O   . HOH   G 5 .   ? -43.421 44.092  28.482  1.00 56.67  ? 837 HOH   A O   1 
HETATM 4024 O  O   . HOH   G 5 .   ? -25.286 44.336  39.265  1.00 54.62  ? 838 HOH   A O   1 
HETATM 4025 O  O   . HOH   G 5 .   ? -53.565 19.647  35.033  1.00 50.13  ? 839 HOH   A O   1 
HETATM 4026 O  O   . HOH   G 5 .   ? -22.151 29.078  38.087  1.00 58.85  ? 840 HOH   A O   1 
HETATM 4027 O  O   . HOH   G 5 .   ? -49.816 31.896  22.854  1.00 61.52  ? 841 HOH   A O   1 
HETATM 4028 O  O   . HOH   G 5 .   ? -24.117 7.139   31.170  1.00 60.44  ? 842 HOH   A O   1 
HETATM 4029 O  O   . HOH   G 5 .   ? -44.573 45.099  36.069  1.00 60.23  ? 843 HOH   A O   1 
HETATM 4030 O  O   . HOH   G 5 .   ? -22.883 24.310  38.514  1.00 45.15  ? 844 HOH   A O   1 
HETATM 4031 O  O   . HOH   G 5 .   ? -31.626 10.860  39.322  1.00 49.18  ? 845 HOH   A O   1 
HETATM 4032 O  O   . HOH   H 5 .   ? -40.735 10.334  -15.187 1.00 40.81  ? 501 HOH   B O   1 
HETATM 4033 O  O   . HOH   H 5 .   ? -19.920 21.451  -7.286  1.00 55.45  ? 502 HOH   B O   1 
HETATM 4034 O  O   . HOH   H 5 .   ? -12.504 17.793  8.918   1.00 51.66  ? 503 HOH   B O   1 
HETATM 4035 O  O   . HOH   H 5 .   ? -34.968 2.701   -10.802 1.00 30.12  ? 504 HOH   B O   1 
HETATM 4036 O  O   . HOH   H 5 .   ? -27.077 13.372  -12.590 1.00 37.17  ? 505 HOH   B O   1 
HETATM 4037 O  O   . HOH   H 5 .   ? -32.993 -5.877  29.354  1.00 58.47  ? 506 HOH   B O   1 
HETATM 4038 O  O   . HOH   H 5 .   ? -30.586 -2.739  5.149   1.00 44.02  ? 507 HOH   B O   1 
HETATM 4039 O  O   . HOH   H 5 .   ? -21.388 14.086  20.127  1.00 47.59  ? 508 HOH   B O   1 
HETATM 4040 O  O   . HOH   H 5 .   ? -30.191 4.488   20.941  1.00 43.30  ? 509 HOH   B O   1 
HETATM 4041 O  O   . HOH   H 5 .   ? -13.605 3.987   10.965  1.00 63.76  ? 510 HOH   B O   1 
HETATM 4042 O  O   . HOH   H 5 .   ? -42.217 5.138   37.253  1.00 58.23  ? 511 HOH   B O   1 
HETATM 4043 O  O   . HOH   H 5 .   ? -16.645 21.244  -6.665  1.00 53.12  ? 512 HOH   B O   1 
HETATM 4044 O  O   . HOH   H 5 .   ? -49.009 4.146   26.746  1.00 45.92  ? 513 HOH   B O   1 
HETATM 4045 O  O   . HOH   H 5 .   ? -29.774 0.706   12.587  1.00 36.19  ? 514 HOH   B O   1 
HETATM 4046 O  O   . HOH   H 5 .   ? -19.104 19.249  -1.999  1.00 45.16  ? 515 HOH   B O   1 
HETATM 4047 O  O   . HOH   H 5 .   ? -31.639 18.312  14.038  1.00 24.03  ? 516 HOH   B O   1 
HETATM 4048 O  O   . HOH   H 5 .   ? -17.734 9.000   10.699  1.00 45.04  ? 517 HOH   B O   1 
HETATM 4049 O  O   . HOH   H 5 .   ? -12.344 9.094   6.211   1.00 51.81  ? 518 HOH   B O   1 
HETATM 4050 O  O   . HOH   H 5 .   ? -37.612 17.523  -9.786  1.00 32.86  ? 519 HOH   B O   1 
HETATM 4051 O  O   . HOH   H 5 .   ? -31.935 25.148  -8.262  1.00 38.52  ? 520 HOH   B O   1 
HETATM 4052 O  O   . HOH   H 5 .   ? -40.017 18.481  10.446  1.00 34.91  ? 521 HOH   B O   1 
HETATM 4053 O  O   . HOH   H 5 .   ? -40.365 12.319  -12.862 1.00 37.69  ? 522 HOH   B O   1 
HETATM 4054 O  O   . HOH   H 5 .   ? -44.057 9.199   37.567  1.00 61.71  ? 523 HOH   B O   1 
HETATM 4055 O  O   . HOH   H 5 .   ? -20.979 18.496  26.797  1.00 42.23  ? 524 HOH   B O   1 
HETATM 4056 O  O   . HOH   H 5 .   ? -41.208 -3.761  27.298  1.00 46.65  ? 525 HOH   B O   1 
HETATM 4057 O  O   . HOH   H 5 .   ? -46.051 9.157   8.747   1.00 44.36  ? 526 HOH   B O   1 
HETATM 4058 O  O   . HOH   H 5 .   ? -42.090 18.560  14.527  1.00 43.95  ? 527 HOH   B O   1 
HETATM 4059 O  O   . HOH   H 5 .   ? -33.768 -3.971  20.658  1.00 58.04  ? 528 HOH   B O   1 
HETATM 4060 O  O   . HOH   H 5 .   ? -43.657 -0.436  -11.829 1.00 47.30  ? 529 HOH   B O   1 
HETATM 4061 O  O   . HOH   H 5 .   ? -27.048 19.363  -10.907 1.00 44.94  ? 530 HOH   B O   1 
HETATM 4062 O  O   . HOH   H 5 .   ? -25.937 8.556   7.409   1.00 23.65  ? 531 HOH   B O   1 
HETATM 4063 O  O   . HOH   H 5 .   ? -47.388 12.080  30.398  1.00 58.33  ? 532 HOH   B O   1 
HETATM 4064 O  O   . HOH   H 5 .   ? -28.320 8.865   -18.403 1.00 48.95  ? 533 HOH   B O   1 
HETATM 4065 O  O   . HOH   H 5 .   ? -24.212 12.875  14.124  1.00 22.03  ? 534 HOH   B O   1 
HETATM 4066 O  O   . HOH   H 5 .   ? -36.156 -2.294  14.420  1.00 40.77  ? 535 HOH   B O   1 
HETATM 4067 O  O   . HOH   H 5 .   ? -22.354 6.040   -15.905 1.00 58.29  ? 536 HOH   B O   1 
HETATM 4068 O  O   . HOH   H 5 .   ? -17.739 4.520   -0.853  1.00 35.21  ? 537 HOH   B O   1 
HETATM 4069 O  O   . HOH   H 5 .   ? -31.265 -7.296  -12.165 1.00 34.62  ? 538 HOH   B O   1 
HETATM 4070 O  O   . HOH   H 5 .   ? -31.675 16.498  -4.876  1.00 27.54  ? 539 HOH   B O   1 
HETATM 4071 O  O   . HOH   H 5 .   ? -44.574 3.533   -1.112  1.00 49.50  ? 540 HOH   B O   1 
HETATM 4072 O  O   . HOH   H 5 .   ? -11.831 13.102  7.491   1.00 44.70  ? 541 HOH   B O   1 
HETATM 4073 O  O   . HOH   H 5 .   ? -12.220 14.302  3.358   1.00 41.81  ? 542 HOH   B O   1 
HETATM 4074 O  O   . HOH   H 5 .   ? -31.907 -6.506  5.931   1.00 53.05  ? 543 HOH   B O   1 
HETATM 4075 O  O   . HOH   H 5 .   ? -29.738 1.153   -23.108 1.00 49.82  ? 544 HOH   B O   1 
HETATM 4076 O  O   . HOH   H 5 .   ? -22.770 -0.191  0.178   1.00 32.11  ? 545 HOH   B O   1 
HETATM 4077 O  O   . HOH   H 5 .   ? -22.094 11.101  17.221  1.00 40.53  ? 546 HOH   B O   1 
HETATM 4078 O  O   . HOH   H 5 .   ? -23.880 9.046   -17.576 1.00 57.98  ? 547 HOH   B O   1 
HETATM 4079 O  O   . HOH   H 5 .   ? -15.308 13.192  -0.213  1.00 43.47  ? 548 HOH   B O   1 
HETATM 4080 O  O   . HOH   H 5 .   ? -31.595 1.393   -1.932  1.00 23.87  ? 549 HOH   B O   1 
HETATM 4081 O  O   . HOH   H 5 .   ? -23.253 14.632  -14.741 1.00 42.31  ? 550 HOH   B O   1 
HETATM 4082 O  O   . HOH   H 5 .   ? -49.737 1.699   -22.621 1.00 57.19  ? 551 HOH   B O   1 
HETATM 4083 O  O   . HOH   H 5 .   ? -49.176 4.502   -11.648 1.00 44.07  ? 552 HOH   B O   1 
HETATM 4084 O  O   . HOH   H 5 .   ? -40.855 1.578   -4.251  1.00 32.95  ? 553 HOH   B O   1 
HETATM 4085 O  O   . HOH   H 5 .   ? -24.005 3.621   5.372   1.00 42.56  ? 554 HOH   B O   1 
HETATM 4086 O  O   . HOH   H 5 .   ? -26.357 -9.691  -0.544  1.00 35.92  ? 555 HOH   B O   1 
HETATM 4087 O  O   . HOH   H 5 .   ? -15.318 18.575  -3.414  1.00 35.20  ? 556 HOH   B O   1 
HETATM 4088 O  O   . HOH   H 5 .   ? -44.885 11.738  2.981   1.00 35.40  ? 557 HOH   B O   1 
HETATM 4089 O  O   . HOH   H 5 .   ? -26.658 7.982   15.722  1.00 37.10  ? 558 HOH   B O   1 
HETATM 4090 O  O   . HOH   H 5 .   ? -30.021 -1.789  -17.126 1.00 35.29  ? 559 HOH   B O   1 
HETATM 4091 O  O   . HOH   H 5 .   ? -47.609 12.725  -12.530 1.00 52.70  ? 560 HOH   B O   1 
HETATM 4092 O  O   . HOH   H 5 .   ? -31.526 6.823   -23.108 1.00 49.56  ? 561 HOH   B O   1 
HETATM 4093 O  O   . HOH   H 5 .   ? -33.458 1.937   4.942   1.00 34.75  ? 562 HOH   B O   1 
HETATM 4094 O  O   . HOH   H 5 .   ? -35.470 18.429  -13.862 1.00 52.88  ? 563 HOH   B O   1 
HETATM 4095 O  O   . HOH   H 5 .   ? -40.646 5.979   30.388  1.00 35.13  ? 564 HOH   B O   1 
HETATM 4096 O  O   . HOH   H 5 .   ? -40.441 20.076  -22.830 1.00 61.83  ? 565 HOH   B O   1 
HETATM 4097 O  O   . HOH   H 5 .   ? -24.941 24.277  16.246  1.00 31.08  ? 566 HOH   B O   1 
HETATM 4098 O  O   . HOH   H 5 .   ? -43.289 9.237   -5.776  1.00 46.55  ? 567 HOH   B O   1 
HETATM 4099 O  O   . HOH   H 5 .   ? -28.762 8.724   11.021  1.00 23.54  ? 568 HOH   B O   1 
HETATM 4100 O  O   . HOH   H 5 .   ? -26.762 2.919   7.659   1.00 28.90  ? 569 HOH   B O   1 
HETATM 4101 O  O   . HOH   H 5 .   ? -29.089 7.328   18.293  1.00 49.17  ? 570 HOH   B O   1 
HETATM 4102 O  O   . HOH   H 5 .   ? -49.873 7.908   18.535  1.00 53.43  ? 571 HOH   B O   1 
HETATM 4103 O  O   . HOH   H 5 .   ? -26.406 -5.851  -5.873  1.00 23.78  ? 572 HOH   B O   1 
HETATM 4104 O  O   . HOH   H 5 .   ? -46.584 9.014   -12.128 1.00 49.69  ? 573 HOH   B O   1 
HETATM 4105 O  O   . HOH   H 5 .   ? -43.267 5.784   -8.453  1.00 46.74  ? 574 HOH   B O   1 
HETATM 4106 O  O   . HOH   H 5 .   ? -29.282 -2.029  -19.913 1.00 28.58  ? 575 HOH   B O   1 
HETATM 4107 O  O   . HOH   H 5 .   ? -18.356 10.714  -5.558  1.00 54.85  ? 576 HOH   B O   1 
HETATM 4108 O  O   . HOH   H 5 .   ? -24.485 1.717   3.833   1.00 33.67  ? 577 HOH   B O   1 
HETATM 4109 O  O   . HOH   H 5 .   ? -47.119 6.370   -24.454 1.00 56.61  ? 578 HOH   B O   1 
HETATM 4110 O  O   . HOH   H 5 .   ? -28.136 21.280  -8.294  1.00 45.75  ? 579 HOH   B O   1 
HETATM 4111 O  O   . HOH   H 5 .   ? -41.543 0.368   18.570  1.00 48.04  ? 580 HOH   B O   1 
HETATM 4112 O  O   . HOH   H 5 .   ? -32.889 0.112   -5.960  1.00 24.48  ? 581 HOH   B O   1 
HETATM 4113 O  O   . HOH   H 5 .   ? -30.747 1.535   5.706   1.00 28.59  ? 582 HOH   B O   1 
HETATM 4114 O  O   . HOH   H 5 .   ? -44.249 2.985   21.374  1.00 35.94  ? 583 HOH   B O   1 
HETATM 4115 O  O   . HOH   H 5 .   ? -26.772 5.319   15.589  1.00 51.53  ? 584 HOH   B O   1 
HETATM 4116 O  O   . HOH   H 5 .   ? -41.740 -1.316  1.937   1.00 34.90  ? 585 HOH   B O   1 
HETATM 4117 O  O   . HOH   H 5 .   ? -29.460 13.391  19.282  1.00 46.19  ? 586 HOH   B O   1 
HETATM 4118 O  O   . HOH   H 5 .   ? -43.763 0.418   -0.426  1.00 35.29  ? 587 HOH   B O   1 
HETATM 4119 O  O   . HOH   H 5 .   ? -16.034 0.023   -8.226  1.00 56.96  ? 588 HOH   B O   1 
HETATM 4120 O  O   . HOH   H 5 .   ? -38.920 14.944  34.415  1.00 30.58  ? 589 HOH   B O   1 
HETATM 4121 O  O   . HOH   H 5 .   ? -34.584 12.638  -17.419 1.00 45.11  ? 590 HOH   B O   1 
HETATM 4122 O  O   . HOH   H 5 .   ? -31.965 3.486   26.803  1.00 32.94  ? 591 HOH   B O   1 
HETATM 4123 O  O   . HOH   H 5 .   ? -42.540 13.925  -21.244 1.00 49.48  ? 592 HOH   B O   1 
HETATM 4124 O  O   . HOH   H 5 .   ? -32.325 4.907   4.484   1.00 26.92  ? 593 HOH   B O   1 
HETATM 4125 O  O   . HOH   H 5 .   ? -16.846 13.681  11.422  1.00 30.99  ? 594 HOH   B O   1 
HETATM 4126 O  O   . HOH   H 5 .   ? -42.412 1.618   -14.652 1.00 59.41  ? 595 HOH   B O   1 
HETATM 4127 O  O   . HOH   H 5 .   ? -26.135 1.726   14.408  1.00 54.13  ? 596 HOH   B O   1 
HETATM 4128 O  O   . HOH   H 5 .   ? -25.156 26.932  -1.986  1.00 36.03  ? 597 HOH   B O   1 
HETATM 4129 O  O   . HOH   H 5 .   ? -29.727 27.334  1.654   1.00 31.68  ? 598 HOH   B O   1 
HETATM 4130 O  O   . HOH   H 5 .   ? -22.855 25.632  3.892   1.00 25.97  ? 599 HOH   B O   1 
HETATM 4131 O  O   . HOH   H 5 .   ? -35.439 6.177   -9.889  1.00 26.67  ? 600 HOH   B O   1 
HETATM 4132 O  O   . HOH   H 5 .   ? -27.276 -7.566  -12.456 1.00 37.14  ? 601 HOH   B O   1 
HETATM 4133 O  O   . HOH   H 5 .   ? -24.069 10.306  18.806  1.00 35.58  ? 602 HOH   B O   1 
HETATM 4134 O  O   . HOH   H 5 .   ? -35.472 -0.711  0.712   1.00 35.86  ? 603 HOH   B O   1 
HETATM 4135 O  O   . HOH   H 5 .   ? -25.517 23.915  11.312  1.00 29.22  ? 604 HOH   B O   1 
HETATM 4136 O  O   . HOH   H 5 .   ? -36.134 -0.104  12.373  1.00 34.21  ? 605 HOH   B O   1 
HETATM 4137 O  O   . HOH   H 5 .   ? -38.276 -0.617  10.306  1.00 34.88  ? 606 HOH   B O   1 
HETATM 4138 O  O   . HOH   H 5 .   ? -28.290 2.780   12.764  1.00 44.11  ? 607 HOH   B O   1 
HETATM 4139 O  O   . HOH   H 5 .   ? -40.833 4.403   -17.329 1.00 49.72  ? 608 HOH   B O   1 
HETATM 4140 O  O   . HOH   H 5 .   ? -41.434 11.279  -4.164  1.00 46.94  ? 609 HOH   B O   1 
HETATM 4141 O  O   . HOH   H 5 .   ? -50.826 3.500   -13.705 1.00 52.14  ? 610 HOH   B O   1 
HETATM 4142 O  O   . HOH   H 5 .   ? -23.857 27.112  6.108   1.00 28.88  ? 611 HOH   B O   1 
HETATM 4143 O  O   . HOH   H 5 .   ? -33.532 27.097  -4.063  1.00 53.23  ? 612 HOH   B O   1 
HETATM 4144 O  O   . HOH   H 5 .   ? -24.675 -5.048  0.064   1.00 27.33  ? 613 HOH   B O   1 
HETATM 4145 O  O   . HOH   H 5 .   ? -34.232 26.460  6.136   1.00 50.50  ? 614 HOH   B O   1 
HETATM 4146 O  O   . HOH   H 5 .   ? -33.956 -5.623  3.652   1.00 51.44  ? 615 HOH   B O   1 
HETATM 4147 O  O   . HOH   H 5 .   ? -23.877 19.396  -13.694 1.00 59.01  ? 616 HOH   B O   1 
HETATM 4148 O  O   . HOH   H 5 .   ? -34.322 11.024  -19.349 1.00 43.20  ? 617 HOH   B O   1 
HETATM 4149 O  O   . HOH   H 5 .   ? -26.428 24.301  -5.930  1.00 48.71  ? 618 HOH   B O   1 
HETATM 4150 O  O   . HOH   H 5 .   ? -24.160 24.495  -4.482  1.00 45.00  ? 619 HOH   B O   1 
HETATM 4151 O  O   . HOH   H 5 .   ? -45.727 1.418   -3.389  1.00 47.03  ? 620 HOH   B O   1 
HETATM 4152 O  O   . HOH   H 5 .   ? -42.850 16.332  35.635  1.00 41.92  ? 621 HOH   B O   1 
HETATM 4153 O  O   . HOH   H 5 .   ? -27.296 -4.686  5.008   1.00 41.54  ? 622 HOH   B O   1 
HETATM 4154 O  O   . HOH   H 5 .   ? -37.626 -1.944  0.335   1.00 32.61  ? 623 HOH   B O   1 
HETATM 4155 O  O   . HOH   H 5 .   ? -26.393 -3.797  9.183   1.00 45.17  ? 624 HOH   B O   1 
HETATM 4156 O  O   . HOH   H 5 .   ? -46.700 3.356   2.790   1.00 54.11  ? 625 HOH   B O   1 
HETATM 4157 O  O   . HOH   H 5 .   ? -20.112 9.560   13.565  1.00 47.05  ? 626 HOH   B O   1 
HETATM 4158 O  O   . HOH   H 5 .   ? -25.811 1.787   -23.359 1.00 40.14  ? 627 HOH   B O   1 
HETATM 4159 O  O   . HOH   H 5 .   ? -20.839 11.876  12.938  1.00 42.22  ? 628 HOH   B O   1 
HETATM 4160 O  O   . HOH   H 5 .   ? -33.781 -0.133  11.162  1.00 33.89  ? 629 HOH   B O   1 
HETATM 4161 O  O   . HOH   H 5 .   ? -39.164 5.466   -10.377 1.00 37.27  ? 630 HOH   B O   1 
HETATM 4162 O  O   . HOH   H 5 .   ? -27.702 25.480  10.938  1.00 27.81  ? 631 HOH   B O   1 
HETATM 4163 O  O   . HOH   H 5 .   ? -43.536 5.077   12.807  1.00 39.89  ? 632 HOH   B O   1 
HETATM 4164 O  O   . HOH   H 5 .   ? -20.627 13.766  17.240  1.00 35.93  ? 633 HOH   B O   1 
HETATM 4165 O  O   . HOH   H 5 .   ? -39.993 -2.185  15.489  1.00 43.61  ? 634 HOH   B O   1 
HETATM 4166 O  O   . HOH   H 5 .   ? -26.350 7.521   24.531  1.00 43.65  ? 635 HOH   B O   1 
HETATM 4167 O  O   . HOH   H 5 .   ? -39.304 22.610  10.216  1.00 59.51  ? 636 HOH   B O   1 
HETATM 4168 O  O   . HOH   H 5 .   ? -19.499 -1.872  -10.614 1.00 52.51  ? 637 HOH   B O   1 
HETATM 4169 O  O   . HOH   H 5 .   ? -14.974 15.597  9.840   1.00 35.39  ? 638 HOH   B O   1 
HETATM 4170 O  O   . HOH   H 5 .   ? -37.065 -1.471  8.140   1.00 39.61  ? 639 HOH   B O   1 
HETATM 4171 O  O   . HOH   H 5 .   ? -36.359 13.709  40.210  1.00 51.30  ? 640 HOH   B O   1 
HETATM 4172 O  O   . HOH   H 5 .   ? -31.943 1.826   29.114  1.00 39.58  ? 641 HOH   B O   1 
HETATM 4173 O  O   . HOH   H 5 .   ? -30.115 3.518   31.027  1.00 59.16  ? 642 HOH   B O   1 
HETATM 4174 O  O   . HOH   H 5 .   ? -41.656 -0.999  27.483  1.00 39.93  ? 643 HOH   B O   1 
HETATM 4175 O  O   . HOH   H 5 .   ? -18.391 13.487  -5.345  1.00 46.29  ? 644 HOH   B O   1 
HETATM 4176 O  O   . HOH   H 5 .   ? -35.833 20.534  -12.145 1.00 43.50  ? 645 HOH   B O   1 
HETATM 4177 O  O   . HOH   H 5 .   ? -26.965 -5.981  2.177   1.00 28.30  ? 646 HOH   B O   1 
HETATM 4178 O  O   . HOH   H 5 .   ? -16.148 2.488   -8.190  1.00 48.02  ? 647 HOH   B O   1 
HETATM 4179 O  O   . HOH   H 5 .   ? -25.172 4.038   -21.481 1.00 42.06  ? 648 HOH   B O   1 
HETATM 4180 O  O   . HOH   H 5 .   ? -30.412 15.411  -16.729 1.00 52.72  ? 649 HOH   B O   1 
HETATM 4181 O  O   . HOH   H 5 .   ? -35.094 -2.155  -18.899 1.00 47.69  ? 650 HOH   B O   1 
HETATM 4182 O  O   . HOH   H 5 .   ? -18.180 1.667   -10.486 1.00 61.04  ? 651 HOH   B O   1 
HETATM 4183 O  O   . HOH   H 5 .   ? -27.861 -6.460  9.330   1.00 51.32  ? 652 HOH   B O   1 
HETATM 4184 O  O   . HOH   H 5 .   ? -23.412 16.488  19.357  1.00 39.18  ? 653 HOH   B O   1 
HETATM 4185 O  O   . HOH   H 5 .   ? -49.169 -1.231  -3.645  1.00 49.88  ? 654 HOH   B O   1 
HETATM 4186 O  O   . HOH   H 5 .   ? -26.056 14.731  -14.198 1.00 52.40  ? 655 HOH   B O   1 
HETATM 4187 O  O   . HOH   H 5 .   ? -35.503 -4.442  16.464  1.00 61.39  ? 656 HOH   B O   1 
HETATM 4188 O  O   . HOH   H 5 .   ? -13.659 18.038  19.219  1.00 64.89  ? 657 HOH   B O   1 
HETATM 4189 O  O   . HOH   H 5 .   ? -42.834 3.778   -18.636 1.00 66.45  ? 658 HOH   B O   1 
HETATM 4190 O  O   . HOH   H 5 .   ? -32.952 18.270  -14.562 1.00 54.00  ? 659 HOH   B O   1 
HETATM 4191 O  O   . HOH   H 5 .   ? -16.354 -2.021  0.032   1.00 59.70  ? 660 HOH   B O   1 
HETATM 4192 O  O   . HOH   H 5 .   ? -22.869 6.736   -23.534 1.00 62.89  ? 661 HOH   B O   1 
HETATM 4193 O  O   . HOH   H 5 .   ? -38.693 25.257  8.553   1.00 45.38  ? 662 HOH   B O   1 
HETATM 4194 O  O   . HOH   H 5 .   ? -24.793 6.614   -21.657 1.00 54.75  ? 663 HOH   B O   1 
HETATM 4195 O  O   . HOH   H 5 .   ? -24.420 -12.380 -3.871  1.00 48.53  ? 664 HOH   B O   1 
HETATM 4196 O  O   . HOH   H 5 .   ? -14.920 12.352  -2.570  1.00 59.46  ? 665 HOH   B O   1 
HETATM 4197 O  O   . HOH   H 5 .   ? -22.136 1.945   2.030   1.00 40.83  ? 666 HOH   B O   1 
HETATM 4198 O  O   . HOH   H 5 .   ? -16.385 20.795  -2.365  1.00 36.92  ? 667 HOH   B O   1 
HETATM 4199 O  O   . HOH   H 5 .   ? -46.856 -0.994  -2.421  1.00 45.68  ? 668 HOH   B O   1 
HETATM 4200 O  O   . HOH   H 5 .   ? -36.638 23.323  -12.583 1.00 57.79  ? 669 HOH   B O   1 
HETATM 4201 O  O   . HOH   H 5 .   ? -49.675 12.437  -16.325 1.00 56.01  ? 670 HOH   B O   1 
HETATM 4202 O  O   . HOH   H 5 .   ? -39.635 -4.020  -11.999 1.00 43.09  ? 671 HOH   B O   1 
HETATM 4203 O  O   . HOH   H 5 .   ? -34.337 -0.623  3.528   1.00 31.24  ? 672 HOH   B O   1 
HETATM 4204 O  O   . HOH   H 5 .   ? -38.553 1.635   -20.435 1.00 56.62  ? 673 HOH   B O   1 
HETATM 4205 O  O   . HOH   H 5 .   ? -12.920 14.713  0.628   1.00 46.72  ? 674 HOH   B O   1 
HETATM 4206 O  O   . HOH   H 5 .   ? -14.996 8.530   11.552  1.00 53.67  ? 675 HOH   B O   1 
HETATM 4207 O  O   . HOH   H 5 .   ? -10.751 9.803   8.040   1.00 52.96  ? 676 HOH   B O   1 
HETATM 4208 O  O   . HOH   H 5 .   ? -39.396 -2.773  11.204  1.00 45.67  ? 677 HOH   B O   1 
HETATM 4209 O  O   . HOH   H 5 .   ? -15.632 10.619  12.206  1.00 50.44  ? 678 HOH   B O   1 
HETATM 4210 O  O   . HOH   H 5 .   ? -22.811 7.733   -19.669 1.00 57.78  ? 679 HOH   B O   1 
HETATM 4211 O  O   . HOH   H 5 .   ? -43.377 -2.915  -14.321 1.00 57.94  ? 680 HOH   B O   1 
# 
