data_5E2N
# 
_entry.id   5E2N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   5E2N         pdb_00005e2n 10.2210/pdb5e2n/pdb 
WWPDB D_1000214255 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-10-05 
2 'Structure model' 1 1 2017-01-18 
3 'Structure model' 1 2 2017-02-01 
4 'Structure model' 1 3 2018-03-07 
5 'Structure model' 1 4 2024-01-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Database references'    
3 4 'Structure model' 'Data collection'        
4 5 'Structure model' 'Data collection'        
5 5 'Structure model' 'Database references'    
6 5 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' diffrn_source                 
2 5 'Structure model' chem_comp_atom                
3 5 'Structure model' chem_comp_bond                
4 5 'Structure model' database_2                    
5 5 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
2 5 'Structure model' '_database_2.pdbx_DOI'                 
3 5 'Structure model' '_database_2.pdbx_database_accession'  
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5E2N 
_pdbx_database_status.recvd_initial_deposition_date   2015-10-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 5DOG unspecified 
PDB . 5DOH unspecified 
PDB . 5DRS unspecified 
PDB . 5E2M unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Manakova, E.' 1 
'Smirnov, A.'  2 
'Grazulis, S.' 3 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            ChemMedChem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1860-7187 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            12 
_citation.language                  ? 
_citation.page_first                161 
_citation.page_last                 176 
_citation.title                     
'Intrinsic Thermodynamics and Structures of 2,4- and 3,4-Substituted Fluorinated Benzenesulfonamides Binding to Carbonic Anhydrases.' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201600509 
_citation.pdbx_database_id_PubMed   28001003 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zubriene, A.'      1  ? 
primary 'Smirnov, A.'       2  ? 
primary 'Dudutiene, V.'     3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Matuliene, J.'     5  ? 
primary 'Michailoviene, V.' 6  ? 
primary 'Zaksauskas, A.'    7  ? 
primary 'Manakova, E.'      8  ? 
primary 'Grazulis, S.'      9  ? 
primary 'Matulis, D.'       10 ? 
# 
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 'Carbonic anhydrase 13'                                                              29613.318 2   4.2.1.1 ? 
'human carbonic anhydrase XIII'                                                      ? 
2 non-polymer syn 'ZINC ION'                                                                           65.409    2   ?       ? 
'3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                              106.120   1   ?       ? 
1,2-ETHANEDIOL                                                                       ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                       62.068    7   ?       ? 
'CITRATE ANION'                                                                      ? 
5 non-polymer syn '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 444.489   2   ?       ? 
'DI(HYDROXYETHYL)ETHER'                                                              ? 
6 non-polymer syn 'CITRIC ACID'                                                                        192.124   1   ?       ? ZN 
? 
7 water       nat water                                                                                18.015    483 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XIII,Carbonic anhydrase XIII,CA-XIII' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 'DI(HYDROXYETHYL)ETHER'                                                              PEG 
4 1,2-ETHANEDIOL                                                                       EDO 
5 '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V14 
6 'CITRIC ACID'                                                                        CIT 
7 water                                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   SER n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  ARG n 
1 11  GLU n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  ILE n 
1 17  HIS n 
1 18  TRP n 
1 19  LYS n 
1 20  GLU n 
1 21  PHE n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  GLY n 
1 28  ASP n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  ILE n 
1 34  GLU n 
1 35  ILE n 
1 36  LYS n 
1 37  THR n 
1 38  LYS n 
1 39  GLU n 
1 40  VAL n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  SER n 
1 45  SER n 
1 46  LEU n 
1 47  ARG n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  ILE n 
1 52  LYS n 
1 53  TYR n 
1 54  ASP n 
1 55  PRO n 
1 56  SER n 
1 57  SER n 
1 58  ALA n 
1 59  LYS n 
1 60  ILE n 
1 61  ILE n 
1 62  SER n 
1 63  ASN n 
1 64  SER n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ASP n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  LEU n 
1 82  ARG n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  SER n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ARG n 
1 94  GLN n 
1 95  VAL n 
1 96  HIS n 
1 97  LEU n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 ILE n 
1 111 VAL n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 SER n 
1 128 ASP n 
1 129 LYS n 
1 130 TYR n 
1 131 PRO n 
1 132 SER n 
1 133 PHE n 
1 134 VAL n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 GLU n 
1 140 PRO n 
1 141 ASP n 
1 142 GLY n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 VAL n 
1 149 PHE n 
1 150 LEU n 
1 151 GLN n 
1 152 ILE n 
1 153 GLY n 
1 154 GLU n 
1 155 PRO n 
1 156 ASN n 
1 157 SER n 
1 158 GLN n 
1 159 LEU n 
1 160 GLN n 
1 161 LYS n 
1 162 ILE n 
1 163 THR n 
1 164 ASP n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 SER n 
1 169 ILE n 
1 170 LYS n 
1 171 GLU n 
1 172 LYS n 
1 173 GLY n 
1 174 LYS n 
1 175 GLN n 
1 176 THR n 
1 177 ARG n 
1 178 PHE n 
1 179 THR n 
1 180 ASN n 
1 181 PHE n 
1 182 ASP n 
1 183 LEU n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 SER n 
1 191 TRP n 
1 192 ASP n 
1 193 TYR n 
1 194 TRP n 
1 195 THR n 
1 196 TYR n 
1 197 PRO n 
1 198 GLY n 
1 199 SER n 
1 200 LEU n 
1 201 THR n 
1 202 VAL n 
1 203 PRO n 
1 204 PRO n 
1 205 LEU n 
1 206 LEU n 
1 207 GLU n 
1 208 SER n 
1 209 VAL n 
1 210 THR n 
1 211 TRP n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 LYS n 
1 216 GLN n 
1 217 PRO n 
1 218 ILE n 
1 219 ASN n 
1 220 ILE n 
1 221 SER n 
1 222 SER n 
1 223 GLN n 
1 224 GLN n 
1 225 LEU n 
1 226 ALA n 
1 227 LYS n 
1 228 PHE n 
1 229 ARG n 
1 230 SER n 
1 231 LEU n 
1 232 LEU n 
1 233 CYS n 
1 234 THR n 
1 235 ALA n 
1 236 GLU n 
1 237 GLY n 
1 238 GLU n 
1 239 ALA n 
1 240 ALA n 
1 241 ALA n 
1 242 PHE n 
1 243 LEU n 
1 244 VAL n 
1 245 SER n 
1 246 ASN n 
1 247 HIS n 
1 248 ARG n 
1 249 PRO n 
1 250 PRO n 
1 251 GLN n 
1 252 PRO n 
1 253 LEU n 
1 254 LYS n 
1 255 GLY n 
1 256 ARG n 
1 257 LYS n 
1 258 VAL n 
1 259 ARG n 
1 260 ALA n 
1 261 SER n 
1 262 PHE n 
1 263 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA13 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CIT non-polymer         . 'CITRIC ACID'                                                                        ?                 
'C6 H8 O7'            192.124 
CYS 'L-peptide linking' y CYSTEINE                                                                             ?                 
'C3 H7 N O2 S'        121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                       'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                            ?                 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                      ?                 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                              ?                 
'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                            ?                 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                ?                 
'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                           ?                 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                              ?                 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                               ?                 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                           ?                 
'C5 H11 N O2 S'       149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                              ?                 
'C4 H10 O3'           106.120 
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 
V14 non-polymer         . '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C16 H23 F3 N2 O5 S2' 444.489 
VAL 'L-peptide linking' y VALINE                                                                               ?                 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                           ?                 
'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  TRP 18  18  18  TRP TRP A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  TRP 99  99  99  TRP TRP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 TRP 125 125 125 TRP TRP A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 GLN 160 160 160 GLN GLN A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 TRP 211 211 211 TRP TRP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 CYS 233 233 233 CYS CYS A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 HIS 247 247 247 HIS HIS A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 HIS 263 263 263 HIS HIS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   MET 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   ?   ?   ?   B . n 
B 1 5   LEU 5   5   ?   ?   ?   B . n 
B 1 6   SER 6   6   6   SER SER B . n 
B 1 7   TRP 7   7   7   TRP TRP B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  GLU 11  11  11  GLU GLU B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  TRP 18  18  18  TRP TRP B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  PHE 22  22  22  PHE PHE B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  GLU 34  34  34  GLU GLU B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  PRO 48  48  48  PRO PRO B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  PRO 55  55  55  PRO PRO B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  PHE 72  72  72  PHE PHE B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  SER 79  79  79  SER SER B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  TYR 90  90  90  TYR TYR B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  TRP 99  99  99  TRP TRP B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 HIS 109 109 109 HIS HIS B . n 
B 1 110 ILE 110 110 110 ILE ILE B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 ASP 112 112 112 ASP ASP B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 ALA 118 118 118 ALA ALA B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 HIS 124 124 124 HIS HIS B . n 
B 1 125 TRP 125 125 125 TRP TRP B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 TYR 130 130 130 TYR TYR B . n 
B 1 131 PRO 131 131 131 PRO PRO B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 ALA 136 136 136 ALA ALA B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 PRO 140 140 140 PRO PRO B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 GLY 142 142 142 GLY GLY B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 PHE 149 149 149 PHE PHE B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 GLN 151 151 151 GLN GLN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 PRO 155 155 155 PRO PRO B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 GLN 160 160 160 GLN GLN B . n 
B 1 161 LYS 161 161 161 LYS LYS B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 THR 163 163 163 THR THR B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 THR 165 165 165 THR THR B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 GLN 175 175 175 GLN GLN B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 LEU 186 186 186 LEU LEU B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 PRO 188 188 188 PRO PRO B . n 
B 1 189 PRO 189 189 189 PRO PRO B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 TRP 191 191 191 TRP TRP B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 TRP 194 194 194 TRP TRP B . n 
B 1 195 THR 195 195 195 THR THR B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 PRO 197 197 197 PRO PRO B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 PRO 203 203 203 PRO PRO B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 TRP 211 211 211 TRP TRP B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 PRO 217 217 217 PRO PRO B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 GLN 223 223 223 GLN GLN B . n 
B 1 224 GLN 224 224 224 GLN GLN B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 ALA 226 226 226 ALA ALA B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 PHE 228 228 228 PHE PHE B . n 
B 1 229 ARG 229 229 229 ARG ARG B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 CYS 233 233 233 CYS CYS B . n 
B 1 234 THR 234 234 234 THR THR B . n 
B 1 235 ALA 235 235 235 ALA ALA B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 GLY 237 237 237 GLY GLY B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 SER 245 245 245 SER SER B . n 
B 1 246 ASN 246 246 246 ASN ASN B . n 
B 1 247 HIS 247 247 247 HIS HIS B . n 
B 1 248 ARG 248 248 248 ARG ARG B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 PRO 250 250 250 PRO PRO B . n 
B 1 251 GLN 251 251 251 GLN GLN B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 LYS 254 254 254 LYS LYS B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 LYS 257 257 257 LYS LYS B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 HIS 263 263 263 HIS HIS B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 2   ZN  ZN  A . 
D 3 PEG 1   302 1   PEG PEG A . 
E 4 EDO 1   303 1   EDO EDO A . 
F 4 EDO 1   304 2   EDO EDO A . 
G 4 EDO 1   305 4   EDO EDO A . 
H 4 EDO 1   306 6   EDO EDO A . 
I 5 V14 1   307 1   V14 V14 A . 
J 2 ZN  1   301 1   ZN  ZN  B . 
K 6 CIT 1   302 1   CIT CIT B . 
L 4 EDO 1   303 3   EDO EDO B . 
M 4 EDO 1   304 5   EDO EDO B . 
N 4 EDO 1   305 7   EDO EDO B . 
O 5 V14 1   306 2   V14 V14 B . 
P 7 HOH 1   401 435 HOH HOH A . 
P 7 HOH 2   402 392 HOH HOH A . 
P 7 HOH 3   403 265 HOH HOH A . 
P 7 HOH 4   404 20  HOH HOH A . 
P 7 HOH 5   405 387 HOH HOH A . 
P 7 HOH 6   406 223 HOH HOH A . 
P 7 HOH 7   407 310 HOH HOH A . 
P 7 HOH 8   408 318 HOH HOH A . 
P 7 HOH 9   409 117 HOH HOH A . 
P 7 HOH 10  410 384 HOH HOH A . 
P 7 HOH 11  411 72  HOH HOH A . 
P 7 HOH 12  412 379 HOH HOH A . 
P 7 HOH 13  413 404 HOH HOH A . 
P 7 HOH 14  414 246 HOH HOH A . 
P 7 HOH 15  415 239 HOH HOH A . 
P 7 HOH 16  416 161 HOH HOH A . 
P 7 HOH 17  417 252 HOH HOH A . 
P 7 HOH 18  418 152 HOH HOH A . 
P 7 HOH 19  419 174 HOH HOH A . 
P 7 HOH 20  420 475 HOH HOH A . 
P 7 HOH 21  421 327 HOH HOH A . 
P 7 HOH 22  422 58  HOH HOH A . 
P 7 HOH 23  423 191 HOH HOH A . 
P 7 HOH 24  424 267 HOH HOH A . 
P 7 HOH 25  425 59  HOH HOH A . 
P 7 HOH 26  426 65  HOH HOH A . 
P 7 HOH 27  427 206 HOH HOH A . 
P 7 HOH 28  428 30  HOH HOH A . 
P 7 HOH 29  429 188 HOH HOH A . 
P 7 HOH 30  430 314 HOH HOH A . 
P 7 HOH 31  431 336 HOH HOH A . 
P 7 HOH 32  432 146 HOH HOH A . 
P 7 HOH 33  433 2   HOH HOH A . 
P 7 HOH 34  434 228 HOH HOH A . 
P 7 HOH 35  435 243 HOH HOH A . 
P 7 HOH 36  436 394 HOH HOH A . 
P 7 HOH 37  437 405 HOH HOH A . 
P 7 HOH 38  438 218 HOH HOH A . 
P 7 HOH 39  439 192 HOH HOH A . 
P 7 HOH 40  440 109 HOH HOH A . 
P 7 HOH 41  441 302 HOH HOH A . 
P 7 HOH 42  442 56  HOH HOH A . 
P 7 HOH 43  443 27  HOH HOH A . 
P 7 HOH 44  444 92  HOH HOH A . 
P 7 HOH 45  445 122 HOH HOH A . 
P 7 HOH 46  446 51  HOH HOH A . 
P 7 HOH 47  447 177 HOH HOH A . 
P 7 HOH 48  448 298 HOH HOH A . 
P 7 HOH 49  449 288 HOH HOH A . 
P 7 HOH 50  450 274 HOH HOH A . 
P 7 HOH 51  451 307 HOH HOH A . 
P 7 HOH 52  452 212 HOH HOH A . 
P 7 HOH 53  453 19  HOH HOH A . 
P 7 HOH 54  454 153 HOH HOH A . 
P 7 HOH 55  455 159 HOH HOH A . 
P 7 HOH 56  456 162 HOH HOH A . 
P 7 HOH 57  457 466 HOH HOH A . 
P 7 HOH 58  458 196 HOH HOH A . 
P 7 HOH 59  459 111 HOH HOH A . 
P 7 HOH 60  460 81  HOH HOH A . 
P 7 HOH 61  461 219 HOH HOH A . 
P 7 HOH 62  462 28  HOH HOH A . 
P 7 HOH 63  463 77  HOH HOH A . 
P 7 HOH 64  464 3   HOH HOH A . 
P 7 HOH 65  465 13  HOH HOH A . 
P 7 HOH 66  466 97  HOH HOH A . 
P 7 HOH 67  467 275 HOH HOH A . 
P 7 HOH 68  468 131 HOH HOH A . 
P 7 HOH 69  469 422 HOH HOH A . 
P 7 HOH 70  470 114 HOH HOH A . 
P 7 HOH 71  471 44  HOH HOH A . 
P 7 HOH 72  472 414 HOH HOH A . 
P 7 HOH 73  473 11  HOH HOH A . 
P 7 HOH 74  474 106 HOH HOH A . 
P 7 HOH 75  475 18  HOH HOH A . 
P 7 HOH 76  476 143 HOH HOH A . 
P 7 HOH 77  477 178 HOH HOH A . 
P 7 HOH 78  478 467 HOH HOH A . 
P 7 HOH 79  479 151 HOH HOH A . 
P 7 HOH 80  480 221 HOH HOH A . 
P 7 HOH 81  481 427 HOH HOH A . 
P 7 HOH 82  482 54  HOH HOH A . 
P 7 HOH 83  483 1   HOH HOH A . 
P 7 HOH 84  484 42  HOH HOH A . 
P 7 HOH 85  485 149 HOH HOH A . 
P 7 HOH 86  486 5   HOH HOH A . 
P 7 HOH 87  487 227 HOH HOH A . 
P 7 HOH 88  488 137 HOH HOH A . 
P 7 HOH 89  489 358 HOH HOH A . 
P 7 HOH 90  490 391 HOH HOH A . 
P 7 HOH 91  491 316 HOH HOH A . 
P 7 HOH 92  492 171 HOH HOH A . 
P 7 HOH 93  493 172 HOH HOH A . 
P 7 HOH 94  494 83  HOH HOH A . 
P 7 HOH 95  495 465 HOH HOH A . 
P 7 HOH 96  496 352 HOH HOH A . 
P 7 HOH 97  497 49  HOH HOH A . 
P 7 HOH 98  498 222 HOH HOH A . 
P 7 HOH 99  499 94  HOH HOH A . 
P 7 HOH 100 500 338 HOH HOH A . 
P 7 HOH 101 501 463 HOH HOH A . 
P 7 HOH 102 502 341 HOH HOH A . 
P 7 HOH 103 503 220 HOH HOH A . 
P 7 HOH 104 504 95  HOH HOH A . 
P 7 HOH 105 505 60  HOH HOH A . 
P 7 HOH 106 506 141 HOH HOH A . 
P 7 HOH 107 507 319 HOH HOH A . 
P 7 HOH 108 508 237 HOH HOH A . 
P 7 HOH 109 509 451 HOH HOH A . 
P 7 HOH 110 510 389 HOH HOH A . 
P 7 HOH 111 511 157 HOH HOH A . 
P 7 HOH 112 512 40  HOH HOH A . 
P 7 HOH 113 513 282 HOH HOH A . 
P 7 HOH 114 514 197 HOH HOH A . 
P 7 HOH 115 515 69  HOH HOH A . 
P 7 HOH 116 516 66  HOH HOH A . 
P 7 HOH 117 517 85  HOH HOH A . 
P 7 HOH 118 518 245 HOH HOH A . 
P 7 HOH 119 519 39  HOH HOH A . 
P 7 HOH 120 520 132 HOH HOH A . 
P 7 HOH 121 521 370 HOH HOH A . 
P 7 HOH 122 522 190 HOH HOH A . 
P 7 HOH 123 523 118 HOH HOH A . 
P 7 HOH 124 524 290 HOH HOH A . 
P 7 HOH 125 525 337 HOH HOH A . 
P 7 HOH 126 526 184 HOH HOH A . 
P 7 HOH 127 527 410 HOH HOH A . 
P 7 HOH 128 528 236 HOH HOH A . 
P 7 HOH 129 529 75  HOH HOH A . 
P 7 HOH 130 530 181 HOH HOH A . 
P 7 HOH 131 531 415 HOH HOH A . 
P 7 HOH 132 532 102 HOH HOH A . 
P 7 HOH 133 533 249 HOH HOH A . 
P 7 HOH 134 534 416 HOH HOH A . 
P 7 HOH 135 535 103 HOH HOH A . 
P 7 HOH 136 536 201 HOH HOH A . 
P 7 HOH 137 537 145 HOH HOH A . 
P 7 HOH 138 538 155 HOH HOH A . 
P 7 HOH 139 539 209 HOH HOH A . 
P 7 HOH 140 540 292 HOH HOH A . 
P 7 HOH 141 541 434 HOH HOH A . 
P 7 HOH 142 542 349 HOH HOH A . 
P 7 HOH 143 543 150 HOH HOH A . 
P 7 HOH 144 544 164 HOH HOH A . 
P 7 HOH 145 545 350 HOH HOH A . 
P 7 HOH 146 546 342 HOH HOH A . 
P 7 HOH 147 547 326 HOH HOH A . 
P 7 HOH 148 548 309 HOH HOH A . 
P 7 HOH 149 549 37  HOH HOH A . 
P 7 HOH 150 550 385 HOH HOH A . 
P 7 HOH 151 551 175 HOH HOH A . 
P 7 HOH 152 552 63  HOH HOH A . 
P 7 HOH 153 553 429 HOH HOH A . 
P 7 HOH 154 554 120 HOH HOH A . 
P 7 HOH 155 555 123 HOH HOH A . 
P 7 HOH 156 556 271 HOH HOH A . 
P 7 HOH 157 557 108 HOH HOH A . 
P 7 HOH 158 558 183 HOH HOH A . 
P 7 HOH 159 559 343 HOH HOH A . 
P 7 HOH 160 560 372 HOH HOH A . 
P 7 HOH 161 561 238 HOH HOH A . 
P 7 HOH 162 562 470 HOH HOH A . 
P 7 HOH 163 563 104 HOH HOH A . 
P 7 HOH 164 564 474 HOH HOH A . 
P 7 HOH 165 565 296 HOH HOH A . 
P 7 HOH 166 566 121 HOH HOH A . 
P 7 HOH 167 567 462 HOH HOH A . 
P 7 HOH 168 568 260 HOH HOH A . 
P 7 HOH 169 569 168 HOH HOH A . 
P 7 HOH 170 570 291 HOH HOH A . 
P 7 HOH 171 571 198 HOH HOH A . 
P 7 HOH 172 572 193 HOH HOH A . 
P 7 HOH 173 573 409 HOH HOH A . 
P 7 HOH 174 574 461 HOH HOH A . 
P 7 HOH 175 575 229 HOH HOH A . 
P 7 HOH 176 576 208 HOH HOH A . 
P 7 HOH 177 577 374 HOH HOH A . 
P 7 HOH 178 578 428 HOH HOH A . 
P 7 HOH 179 579 244 HOH HOH A . 
P 7 HOH 180 580 284 HOH HOH A . 
P 7 HOH 181 581 67  HOH HOH A . 
P 7 HOH 182 582 421 HOH HOH A . 
P 7 HOH 183 583 452 HOH HOH A . 
P 7 HOH 184 584 295 HOH HOH A . 
P 7 HOH 185 585 468 HOH HOH A . 
P 7 HOH 186 586 163 HOH HOH A . 
P 7 HOH 187 587 366 HOH HOH A . 
P 7 HOH 188 588 99  HOH HOH A . 
P 7 HOH 189 589 459 HOH HOH A . 
P 7 HOH 190 590 215 HOH HOH A . 
P 7 HOH 191 591 270 HOH HOH A . 
P 7 HOH 192 592 351 HOH HOH A . 
P 7 HOH 193 593 472 HOH HOH A . 
P 7 HOH 194 594 356 HOH HOH A . 
P 7 HOH 195 595 471 HOH HOH A . 
P 7 HOH 196 596 344 HOH HOH A . 
P 7 HOH 197 597 278 HOH HOH A . 
P 7 HOH 198 598 339 HOH HOH A . 
P 7 HOH 199 599 377 HOH HOH A . 
P 7 HOH 200 600 371 HOH HOH A . 
P 7 HOH 201 601 406 HOH HOH A . 
P 7 HOH 202 602 129 HOH HOH A . 
P 7 HOH 203 603 299 HOH HOH A . 
P 7 HOH 204 604 250 HOH HOH A . 
P 7 HOH 205 605 241 HOH HOH A . 
P 7 HOH 206 606 308 HOH HOH A . 
P 7 HOH 207 607 207 HOH HOH A . 
P 7 HOH 208 608 335 HOH HOH A . 
P 7 HOH 209 609 401 HOH HOH A . 
P 7 HOH 210 610 381 HOH HOH A . 
P 7 HOH 211 611 203 HOH HOH A . 
P 7 HOH 212 612 432 HOH HOH A . 
P 7 HOH 213 613 234 HOH HOH A . 
P 7 HOH 214 614 380 HOH HOH A . 
P 7 HOH 215 615 264 HOH HOH A . 
P 7 HOH 216 616 390 HOH HOH A . 
P 7 HOH 217 617 334 HOH HOH A . 
P 7 HOH 218 618 382 HOH HOH A . 
P 7 HOH 219 619 418 HOH HOH A . 
P 7 HOH 220 620 420 HOH HOH A . 
P 7 HOH 221 621 473 HOH HOH A . 
P 7 HOH 222 622 101 HOH HOH A . 
P 7 HOH 223 623 330 HOH HOH A . 
P 7 HOH 224 624 373 HOH HOH A . 
Q 7 HOH 1   401 255 HOH HOH B . 
Q 7 HOH 2   402 447 HOH HOH B . 
Q 7 HOH 3   403 53  HOH HOH B . 
Q 7 HOH 4   404 481 HOH HOH B . 
Q 7 HOH 5   405 438 HOH HOH B . 
Q 7 HOH 6   406 170 HOH HOH B . 
Q 7 HOH 7   407 233 HOH HOH B . 
Q 7 HOH 8   408 185 HOH HOH B . 
Q 7 HOH 9   409 408 HOH HOH B . 
Q 7 HOH 10  410 306 HOH HOH B . 
Q 7 HOH 11  411 199 HOH HOH B . 
Q 7 HOH 12  412 194 HOH HOH B . 
Q 7 HOH 13  413 80  HOH HOH B . 
Q 7 HOH 14  414 346 HOH HOH B . 
Q 7 HOH 15  415 263 HOH HOH B . 
Q 7 HOH 16  416 256 HOH HOH B . 
Q 7 HOH 17  417 322 HOH HOH B . 
Q 7 HOH 18  418 254 HOH HOH B . 
Q 7 HOH 19  419 180 HOH HOH B . 
Q 7 HOH 20  420 383 HOH HOH B . 
Q 7 HOH 21  421 348 HOH HOH B . 
Q 7 HOH 22  422 411 HOH HOH B . 
Q 7 HOH 23  423 34  HOH HOH B . 
Q 7 HOH 24  424 324 HOH HOH B . 
Q 7 HOH 25  425 454 HOH HOH B . 
Q 7 HOH 26  426 261 HOH HOH B . 
Q 7 HOH 27  427 31  HOH HOH B . 
Q 7 HOH 28  428 6   HOH HOH B . 
Q 7 HOH 29  429 402 HOH HOH B . 
Q 7 HOH 30  430 464 HOH HOH B . 
Q 7 HOH 31  431 213 HOH HOH B . 
Q 7 HOH 32  432 8   HOH HOH B . 
Q 7 HOH 33  433 169 HOH HOH B . 
Q 7 HOH 34  434 449 HOH HOH B . 
Q 7 HOH 35  435 61  HOH HOH B . 
Q 7 HOH 36  436 458 HOH HOH B . 
Q 7 HOH 37  437 257 HOH HOH B . 
Q 7 HOH 38  438 279 HOH HOH B . 
Q 7 HOH 39  439 240 HOH HOH B . 
Q 7 HOH 40  440 368 HOH HOH B . 
Q 7 HOH 41  441 98  HOH HOH B . 
Q 7 HOH 42  442 12  HOH HOH B . 
Q 7 HOH 43  443 87  HOH HOH B . 
Q 7 HOH 44  444 230 HOH HOH B . 
Q 7 HOH 45  445 70  HOH HOH B . 
Q 7 HOH 46  446 448 HOH HOH B . 
Q 7 HOH 47  447 210 HOH HOH B . 
Q 7 HOH 48  448 25  HOH HOH B . 
Q 7 HOH 49  449 393 HOH HOH B . 
Q 7 HOH 50  450 148 HOH HOH B . 
Q 7 HOH 51  451 21  HOH HOH B . 
Q 7 HOH 52  452 258 HOH HOH B . 
Q 7 HOH 53  453 176 HOH HOH B . 
Q 7 HOH 54  454 276 HOH HOH B . 
Q 7 HOH 55  455 247 HOH HOH B . 
Q 7 HOH 56  456 115 HOH HOH B . 
Q 7 HOH 57  457 403 HOH HOH B . 
Q 7 HOH 58  458 483 HOH HOH B . 
Q 7 HOH 59  459 64  HOH HOH B . 
Q 7 HOH 60  460 32  HOH HOH B . 
Q 7 HOH 61  461 297 HOH HOH B . 
Q 7 HOH 62  462 478 HOH HOH B . 
Q 7 HOH 63  463 317 HOH HOH B . 
Q 7 HOH 64  464 52  HOH HOH B . 
Q 7 HOH 65  465 331 HOH HOH B . 
Q 7 HOH 66  466 124 HOH HOH B . 
Q 7 HOH 67  467 47  HOH HOH B . 
Q 7 HOH 68  468 333 HOH HOH B . 
Q 7 HOH 69  469 340 HOH HOH B . 
Q 7 HOH 70  470 195 HOH HOH B . 
Q 7 HOH 71  471 57  HOH HOH B . 
Q 7 HOH 72  472 367 HOH HOH B . 
Q 7 HOH 73  473 17  HOH HOH B . 
Q 7 HOH 74  474 68  HOH HOH B . 
Q 7 HOH 75  475 29  HOH HOH B . 
Q 7 HOH 76  476 332 HOH HOH B . 
Q 7 HOH 77  477 10  HOH HOH B . 
Q 7 HOH 78  478 160 HOH HOH B . 
Q 7 HOH 79  479 386 HOH HOH B . 
Q 7 HOH 80  480 313 HOH HOH B . 
Q 7 HOH 81  481 105 HOH HOH B . 
Q 7 HOH 82  482 407 HOH HOH B . 
Q 7 HOH 83  483 154 HOH HOH B . 
Q 7 HOH 84  484 78  HOH HOH B . 
Q 7 HOH 85  485 38  HOH HOH B . 
Q 7 HOH 86  486 74  HOH HOH B . 
Q 7 HOH 87  487 36  HOH HOH B . 
Q 7 HOH 88  488 33  HOH HOH B . 
Q 7 HOH 89  489 136 HOH HOH B . 
Q 7 HOH 90  490 84  HOH HOH B . 
Q 7 HOH 91  491 365 HOH HOH B . 
Q 7 HOH 92  492 186 HOH HOH B . 
Q 7 HOH 93  493 166 HOH HOH B . 
Q 7 HOH 94  494 113 HOH HOH B . 
Q 7 HOH 95  495 450 HOH HOH B . 
Q 7 HOH 96  496 469 HOH HOH B . 
Q 7 HOH 97  497 231 HOH HOH B . 
Q 7 HOH 98  498 88  HOH HOH B . 
Q 7 HOH 99  499 217 HOH HOH B . 
Q 7 HOH 100 500 158 HOH HOH B . 
Q 7 HOH 101 501 62  HOH HOH B . 
Q 7 HOH 102 502 35  HOH HOH B . 
Q 7 HOH 103 503 22  HOH HOH B . 
Q 7 HOH 104 504 45  HOH HOH B . 
Q 7 HOH 105 505 200 HOH HOH B . 
Q 7 HOH 106 506 262 HOH HOH B . 
Q 7 HOH 107 507 242 HOH HOH B . 
Q 7 HOH 108 508 76  HOH HOH B . 
Q 7 HOH 109 509 235 HOH HOH B . 
Q 7 HOH 110 510 7   HOH HOH B . 
Q 7 HOH 111 511 216 HOH HOH B . 
Q 7 HOH 112 512 130 HOH HOH B . 
Q 7 HOH 113 513 41  HOH HOH B . 
Q 7 HOH 114 514 55  HOH HOH B . 
Q 7 HOH 115 515 300 HOH HOH B . 
Q 7 HOH 116 516 436 HOH HOH B . 
Q 7 HOH 117 517 50  HOH HOH B . 
Q 7 HOH 118 518 79  HOH HOH B . 
Q 7 HOH 119 519 4   HOH HOH B . 
Q 7 HOH 120 520 189 HOH HOH B . 
Q 7 HOH 121 521 138 HOH HOH B . 
Q 7 HOH 122 522 86  HOH HOH B . 
Q 7 HOH 123 523 187 HOH HOH B . 
Q 7 HOH 124 524 43  HOH HOH B . 
Q 7 HOH 125 525 259 HOH HOH B . 
Q 7 HOH 126 526 134 HOH HOH B . 
Q 7 HOH 127 527 9   HOH HOH B . 
Q 7 HOH 128 528 107 HOH HOH B . 
Q 7 HOH 129 529 347 HOH HOH B . 
Q 7 HOH 130 530 156 HOH HOH B . 
Q 7 HOH 131 531 116 HOH HOH B . 
Q 7 HOH 132 532 91  HOH HOH B . 
Q 7 HOH 133 533 202 HOH HOH B . 
Q 7 HOH 134 534 173 HOH HOH B . 
Q 7 HOH 135 535 224 HOH HOH B . 
Q 7 HOH 136 536 482 HOH HOH B . 
Q 7 HOH 137 537 179 HOH HOH B . 
Q 7 HOH 138 538 96  HOH HOH B . 
Q 7 HOH 139 539 426 HOH HOH B . 
Q 7 HOH 140 540 441 HOH HOH B . 
Q 7 HOH 141 541 359 HOH HOH B . 
Q 7 HOH 142 542 205 HOH HOH B . 
Q 7 HOH 143 543 16  HOH HOH B . 
Q 7 HOH 144 544 14  HOH HOH B . 
Q 7 HOH 145 545 294 HOH HOH B . 
Q 7 HOH 146 546 140 HOH HOH B . 
Q 7 HOH 147 547 305 HOH HOH B . 
Q 7 HOH 148 548 167 HOH HOH B . 
Q 7 HOH 149 549 353 HOH HOH B . 
Q 7 HOH 150 550 135 HOH HOH B . 
Q 7 HOH 151 551 355 HOH HOH B . 
Q 7 HOH 152 552 456 HOH HOH B . 
Q 7 HOH 153 553 272 HOH HOH B . 
Q 7 HOH 154 554 285 HOH HOH B . 
Q 7 HOH 155 555 315 HOH HOH B . 
Q 7 HOH 156 556 24  HOH HOH B . 
Q 7 HOH 157 557 329 HOH HOH B . 
Q 7 HOH 158 558 23  HOH HOH B . 
Q 7 HOH 159 559 125 HOH HOH B . 
Q 7 HOH 160 560 165 HOH HOH B . 
Q 7 HOH 161 561 133 HOH HOH B . 
Q 7 HOH 162 562 100 HOH HOH B . 
Q 7 HOH 163 563 248 HOH HOH B . 
Q 7 HOH 164 564 226 HOH HOH B . 
Q 7 HOH 165 565 15  HOH HOH B . 
Q 7 HOH 166 566 110 HOH HOH B . 
Q 7 HOH 167 567 211 HOH HOH B . 
Q 7 HOH 168 568 147 HOH HOH B . 
Q 7 HOH 169 569 328 HOH HOH B . 
Q 7 HOH 170 570 361 HOH HOH B . 
Q 7 HOH 171 571 325 HOH HOH B . 
Q 7 HOH 172 572 397 HOH HOH B . 
Q 7 HOH 173 573 323 HOH HOH B . 
Q 7 HOH 174 574 378 HOH HOH B . 
Q 7 HOH 175 575 89  HOH HOH B . 
Q 7 HOH 176 576 71  HOH HOH B . 
Q 7 HOH 177 577 360 HOH HOH B . 
Q 7 HOH 178 578 142 HOH HOH B . 
Q 7 HOH 179 579 126 HOH HOH B . 
Q 7 HOH 180 580 460 HOH HOH B . 
Q 7 HOH 181 581 269 HOH HOH B . 
Q 7 HOH 182 582 303 HOH HOH B . 
Q 7 HOH 183 583 301 HOH HOH B . 
Q 7 HOH 184 584 232 HOH HOH B . 
Q 7 HOH 185 585 304 HOH HOH B . 
Q 7 HOH 186 586 293 HOH HOH B . 
Q 7 HOH 187 587 277 HOH HOH B . 
Q 7 HOH 188 588 289 HOH HOH B . 
Q 7 HOH 189 589 144 HOH HOH B . 
Q 7 HOH 190 590 311 HOH HOH B . 
Q 7 HOH 191 591 457 HOH HOH B . 
Q 7 HOH 192 592 128 HOH HOH B . 
Q 7 HOH 193 593 362 HOH HOH B . 
Q 7 HOH 194 594 287 HOH HOH B . 
Q 7 HOH 195 595 321 HOH HOH B . 
Q 7 HOH 196 596 268 HOH HOH B . 
Q 7 HOH 197 597 312 HOH HOH B . 
Q 7 HOH 198 598 46  HOH HOH B . 
Q 7 HOH 199 599 283 HOH HOH B . 
Q 7 HOH 200 600 286 HOH HOH B . 
Q 7 HOH 201 601 214 HOH HOH B . 
Q 7 HOH 202 602 439 HOH HOH B . 
Q 7 HOH 203 603 388 HOH HOH B . 
Q 7 HOH 204 604 225 HOH HOH B . 
Q 7 HOH 205 605 425 HOH HOH B . 
Q 7 HOH 206 606 48  HOH HOH B . 
Q 7 HOH 207 607 139 HOH HOH B . 
Q 7 HOH 208 608 93  HOH HOH B . 
Q 7 HOH 209 609 266 HOH HOH B . 
Q 7 HOH 210 610 345 HOH HOH B . 
Q 7 HOH 211 611 112 HOH HOH B . 
Q 7 HOH 212 612 444 HOH HOH B . 
Q 7 HOH 213 613 320 HOH HOH B . 
Q 7 HOH 214 614 369 HOH HOH B . 
Q 7 HOH 215 615 417 HOH HOH B . 
Q 7 HOH 216 616 375 HOH HOH B . 
Q 7 HOH 217 617 127 HOH HOH B . 
Q 7 HOH 218 618 412 HOH HOH B . 
Q 7 HOH 219 619 443 HOH HOH B . 
Q 7 HOH 220 620 453 HOH HOH B . 
Q 7 HOH 221 621 182 HOH HOH B . 
Q 7 HOH 222 622 455 HOH HOH B . 
Q 7 HOH 223 623 280 HOH HOH B . 
Q 7 HOH 224 624 413 HOH HOH B . 
Q 7 HOH 225 625 423 HOH HOH B . 
Q 7 HOH 226 626 430 HOH HOH B . 
Q 7 HOH 227 627 73  HOH HOH B . 
Q 7 HOH 228 628 273 HOH HOH B . 
Q 7 HOH 229 629 446 HOH HOH B . 
Q 7 HOH 230 630 479 HOH HOH B . 
Q 7 HOH 231 631 376 HOH HOH B . 
Q 7 HOH 232 632 281 HOH HOH B . 
Q 7 HOH 233 633 82  HOH HOH B . 
Q 7 HOH 234 634 357 HOH HOH B . 
Q 7 HOH 235 635 119 HOH HOH B . 
Q 7 HOH 236 636 400 HOH HOH B . 
Q 7 HOH 237 637 26  HOH HOH B . 
Q 7 HOH 238 638 477 HOH HOH B . 
Q 7 HOH 239 639 251 HOH HOH B . 
Q 7 HOH 240 640 363 HOH HOH B . 
Q 7 HOH 241 641 433 HOH HOH B . 
Q 7 HOH 242 642 253 HOH HOH B . 
Q 7 HOH 243 643 399 HOH HOH B . 
Q 7 HOH 244 644 364 HOH HOH B . 
Q 7 HOH 245 645 476 HOH HOH B . 
Q 7 HOH 246 646 445 HOH HOH B . 
Q 7 HOH 247 647 440 HOH HOH B . 
Q 7 HOH 248 648 442 HOH HOH B . 
Q 7 HOH 249 649 424 HOH HOH B . 
Q 7 HOH 250 650 354 HOH HOH B . 
Q 7 HOH 251 651 419 HOH HOH B . 
Q 7 HOH 252 652 204 HOH HOH B . 
Q 7 HOH 253 653 395 HOH HOH B . 
Q 7 HOH 254 654 437 HOH HOH B . 
Q 7 HOH 255 655 396 HOH HOH B . 
Q 7 HOH 256 656 90  HOH HOH B . 
Q 7 HOH 257 657 480 HOH HOH B . 
Q 7 HOH 258 658 398 HOH HOH B . 
Q 7 HOH 259 659 431 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 10  ? CZ  ? A ARG 10  CZ  
2  1 Y 1 A ARG 10  ? NH1 ? A ARG 10  NH1 
3  1 Y 1 A ARG 10  ? NH2 ? A ARG 10  NH2 
4  1 Y 1 A LYS 38  ? CG  ? A LYS 38  CG  
5  1 Y 1 A LYS 38  ? CD  ? A LYS 38  CD  
6  1 Y 1 A LYS 38  ? CE  ? A LYS 38  CE  
7  1 Y 1 A LYS 38  ? NZ  ? A LYS 38  NZ  
8  1 Y 1 A LYS 41  ? CD  ? A LYS 41  CD  
9  1 Y 1 A LYS 41  ? CE  ? A LYS 41  CE  
10 1 Y 1 A LYS 41  ? NZ  ? A LYS 41  NZ  
11 1 Y 1 A ARG 47  ? CD  ? A ARG 47  CD  
12 1 Y 1 A ARG 47  ? NE  ? A ARG 47  NE  
13 1 Y 1 A ARG 47  ? CZ  ? A ARG 47  CZ  
14 1 Y 1 A ARG 47  ? NH1 ? A ARG 47  NH1 
15 1 Y 1 A ARG 47  ? NH2 ? A ARG 47  NH2 
16 1 Y 1 A GLU 236 ? CD  ? A GLU 236 CD  
17 1 Y 1 A GLU 236 ? OE1 ? A GLU 236 OE1 
18 1 Y 1 A GLU 236 ? OE2 ? A GLU 236 OE2 
19 1 Y 1 B PHE 21  ? CG  ? B PHE 21  CG  
20 1 Y 1 B PHE 21  ? CD1 ? B PHE 21  CD1 
21 1 Y 1 B PHE 21  ? CD2 ? B PHE 21  CD2 
22 1 Y 1 B PHE 21  ? CE1 ? B PHE 21  CE1 
23 1 Y 1 B PHE 21  ? CE2 ? B PHE 21  CE2 
24 1 Y 1 B PHE 21  ? CZ  ? B PHE 21  CZ  
25 1 Y 1 B LYS 41  ? CD  ? B LYS 41  CD  
26 1 Y 1 B LYS 41  ? CE  ? B LYS 41  CE  
27 1 Y 1 B LYS 41  ? NZ  ? B LYS 41  NZ  
28 1 Y 1 B GLU 236 ? CG  ? B GLU 236 CG  
29 1 Y 1 B GLU 236 ? CD  ? B GLU 236 CD  
30 1 Y 1 B GLU 236 ? OE1 ? B GLU 236 OE1 
31 1 Y 1 B GLU 236 ? OE2 ? B GLU 236 OE2 
# 
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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5E2N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.087 
_cell.length_a_esd                 ? 
_cell.length_b                     57.597 
_cell.length_b_esd                 ? 
_cell.length_c                     159.749 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5E2N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   5E2N 
_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            2.15 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         42.4 
_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_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              6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer: 0.1M sodium citrate (pH 5.5), 0.1M sodium acetate (pH 4.5) and
 26% PEG4000.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-12-01 
# 
_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   0.826606 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            19.548 
_reflns.entry_id                         5E2N 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.530 
_reflns.d_resolution_low                 57.597 
_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                       78022 
_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             98.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.500 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.050 
_reflns.pdbx_netI_over_av_sigmaI         6.850 
_reflns.pdbx_netI_over_sigmaI            18.800 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.059 
_reflns.pdbx_Rpim_I_all                  0.023 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         506810 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.53 1.61  ? 2.7  54154 ? ? 10413 ? 91.40  ? ? ? 0.358 0.291 ? ? ? ? ? ? ? ? 5.20 0.291 ? ? 4.50  0.36 0.15 ? 1  1 ? ? 
1.61 1.71  ? 3.5  74017 ? ? 10766 ? 99.90  ? ? ? 0.258 0.219 ? ? ? ? ? ? ? ? 6.90 0.219 ? ? 7.20  0.26 0.10 ? 2  ? ? ? 
1.71 1.83  ? 5.4  66927 ? ? 10144 ? 99.90  ? ? ? 0.167 0.140 ? ? ? ? ? ? ? ? 6.60 0.140 ? ? 10.20 0.17 0.06 ? 3  ? ? ? 
1.83 1.98  ? 8.1  64553 ? ? 9481  ? 99.90  ? ? ? 0.107 0.090 ? ? ? ? ? ? ? ? 6.80 0.090 ? ? 15.10 0.11 0.04 ? 4  ? ? ? 
1.98 2.16  ? 10.4 59176 ? ? 8749  ? 99.90  ? ? ? 0.079 0.066 ? ? ? ? ? ? ? ? 6.80 0.066 ? ? 20.50 0.08 0.03 ? 5  ? ? ? 
2.16 2.42  ? 12.1 52623 ? ? 7959  ? 100.00 ? ? ? 0.063 0.053 ? ? ? ? ? ? ? ? 6.60 0.053 ? ? 25.30 0.06 0.02 ? 6  ? ? ? 
2.42 2.79  ? 13.0 47669 ? ? 7023  ? 100.00 ? ? ? 0.055 0.046 ? ? ? ? ? ? ? ? 6.80 0.046 ? ? 29.80 0.05 0.02 ? 7  ? ? ? 
2.79 3.42  ? 13.4 39923 ? ? 6002  ? 100.00 ? ? ? 0.049 0.041 ? ? ? ? ? ? ? ? 6.70 0.041 ? ? 35.30 0.05 0.02 ? 8  ? ? ? 
3.42 4.84  ? 13.4 30688 ? ? 4737  ? 100.00 ? ? ? 0.047 0.040 ? ? ? ? ? ? ? ? 6.50 0.040 ? ? 39.30 0.05 0.02 ? 9  ? ? ? 
4.84 57.60 ? 11.7 17080 ? ? 2748  ? 100.00 ? ? ? 0.049 0.041 ? ? ? ? ? ? ? ? 6.20 0.041 ? ? 37.90 0.05 0.02 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.170 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            0.680 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -0.850 
_refine.B_iso_max                                81.93 
_refine.B_iso_mean                               22.272 
_refine.B_iso_min                                9.21 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_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                                 5E2N 
_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                            1.530 
_refine.ls_d_res_low                             54.180 
_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                     77932 
_refine.ls_number_reflns_R_free                  7856 
_refine.ls_number_reflns_R_work                  70076 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.650 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.180 
_refine.ls_R_factor_R_free                       0.212 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.176 
_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                      0.223 
_refine.ls_wR_factor_R_work                      0.184 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          0.00 
_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                      4QSJ 
_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                       0.086 
_refine.pdbx_overall_ESU_R_Free                  0.088 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.086 
_refine.overall_SU_R_free                        0.088 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.866 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        4108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         106 
_refine_hist.number_atoms_solvent             483 
_refine_hist.number_atoms_total               4697 
_refine_hist.d_res_high                       1.530 
_refine_hist.d_res_low                        54.180 
# 
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' ? 0.024  0.020  4446 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.357  1.965  6073 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.339  5.000  545  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.403 24.271 199  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.436 15.000 693  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.755 15.000 19   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.169  0.200  638  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.021  3454 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.530 
_refine_ls_shell.d_res_low                        1.570 
_refine_ls_shell.number_reflns_all                4759 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             430 
_refine_ls_shell.number_reflns_R_work             4329 
_refine_ls_shell.percent_reflns_obs               82.620 
_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                  0.300 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.262 
_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_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5E2N 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme XIII with 3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5E2N 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 2 ? 
K N N 6 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 5 ? 
P N N 7 ? 
Q N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH13_HUMAN 
_struct_ref.pdbx_db_accession          Q8N1Q1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVL
RGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQK
ITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAA
FLVSNHRPPQPLKGRKVRASFH
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5E2N A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 5E2N B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5E2N MET A 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 1 
2 5E2N MET B 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,P 
2 1 B,J,K,L,M,N,O,Q   
# 
_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 GLY A 14  ? PHE A 21  ? GLY A 14  PHE A 21  5 ? 8 
HELX_P HELX_P2  AA2 PHE A 22  ? GLY A 27  ? PHE A 22  GLY A 27  5 ? 6 
HELX_P HELX_P3  AA3 LYS A 36  ? VAL A 40  ? LYS A 36  VAL A 40  5 ? 5 
HELX_P HELX_P4  AA4 SER A 132 ? ALA A 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P5  AA5 ASN A 156 ? GLN A 158 ? ASN A 156 GLN A 158 5 ? 3 
HELX_P HELX_P6  AA6 LEU A 159 ? LEU A 166 ? LEU A 159 LEU A 166 1 ? 8 
HELX_P HELX_P7  AA7 ASP A 167 ? LYS A 170 ? ASP A 167 LYS A 170 5 ? 4 
HELX_P HELX_P8  AA8 LEU A 183 ? LEU A 187 ? LEU A 183 LEU A 187 5 ? 5 
HELX_P HELX_P9  AA9 SER A 221 ? ARG A 229 ? SER A 221 ARG A 229 1 ? 9 
HELX_P HELX_P10 AB1 GLY B 14  ? ILE B 16  ? GLY B 14  ILE B 16  5 ? 3 
HELX_P HELX_P11 AB2 HIS B 17  ? PHE B 22  ? HIS B 17  PHE B 22  1 ? 6 
HELX_P HELX_P12 AB3 PRO B 23  ? GLY B 27  ? PRO B 23  GLY B 27  5 ? 5 
HELX_P HELX_P13 AB4 SER B 132 ? ALA B 137 ? SER B 132 ALA B 137 1 ? 6 
HELX_P HELX_P14 AB5 ASN B 156 ? ASP B 164 ? ASN B 156 ASP B 164 1 ? 9 
HELX_P HELX_P15 AB6 THR B 165 ? LYS B 170 ? THR B 165 LYS B 170 5 ? 6 
HELX_P HELX_P16 AB7 ASP B 182 ? LEU B 187 ? ASP B 182 LEU B 187 1 ? 6 
HELX_P HELX_P17 AB8 SER B 221 ? ARG B 229 ? SER B 221 ARG B 229 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc2 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc3 metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc4 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 J ZN  . ZN  ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc5 metalc ? ? B HIS 98  NE2 ? ? ? 1_555 J ZN  . ZN  ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc6 metalc ? ? B HIS 121 ND1 ? ? ? 1_555 J ZN  . ZN  ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc7 metalc ? ? J ZN  .   ZN  ? ? ? 1_555 O V14 . N10 ? ? B ZN  301 B V14 306 1_555 ? ? ? ? ? ? ? 1.709 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 101.6 ? 
2 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 121 ? A HIS 121 ? 1_555 110.6 ? 
3 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 121 ? A HIS 121 ? 1_555 98.3  ? 
4 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 100.7 ? 
5 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 121 ? B HIS 121 ? 1_555 113.8 ? 
6 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 121 ? B HIS 121 ? 1_555 97.6  ? 
7 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N10 ? O V14 .   ? B V14 306 ? 1_555 118.4 ? 
8 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N10 ? O V14 .   ? B V14 306 ? 1_555 107.2 ? 
9 ND1 ? B HIS 121 ? B HIS 121 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N10 ? O V14 .   ? B V14 306 ? 1_555 115.3 ? 
# 
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 SER 31  A . ? SER 31  A PRO 32  A ? PRO 32  A 1 3.52  
2 PRO 203 A . ? PRO 203 A PRO 204 A ? PRO 204 A 1 11.34 
3 SER 31  B . ? SER 31  B PRO 32  B ? PRO 32  B 1 2.09  
4 PRO 203 B . ? PRO 203 B PRO 204 B ? PRO 204 B 1 10.66 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
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      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? 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  GLU A 34  ? ILE A 35  ? GLU A 34  ILE A 35  
AA1 2  ILE A 110 ? VAL A 111 ? ILE A 110 VAL A 111 
AA2 1  LYS A 41  ? TYR A 42  ? LYS A 41  TYR A 42  
AA2 2  ARG A 259 ? ALA A 260 ? ARG A 259 ALA A 260 
AA2 3  TYR A 193 ? GLY A 198 ? TYR A 193 GLY A 198 
AA2 4  VAL A 209 ? LEU A 214 ? VAL A 209 LEU A 214 
AA2 5  LEU A 143 ? ILE A 152 ? LEU A 143 ILE A 152 
AA2 6  ALA A 118 ? ASN A 126 ? ALA A 118 ASN A 126 
AA2 7  TYR A 90  ? TRP A 99  ? TYR A 90  TRP A 99  
AA2 8  PHE A 68  ? PHE A 72  ? PHE A 68  PHE A 72  
AA2 9  ALA A 58  ? ASN A 63  ? ALA A 58  ASN A 63  
AA2 10 GLN A 175 ? ARG A 177 ? GLN A 175 ARG A 177 
AA3 1  ARG A 47  ? LYS A 52  ? ARG A 47  LYS A 52  
AA3 2  VAL A 80  ? GLY A 84  ? VAL A 80  GLY A 84  
AA3 3  TYR A 90  ? TRP A 99  ? TYR A 90  TRP A 99  
AA3 4  ALA A 118 ? ASN A 126 ? ALA A 118 ASN A 126 
AA3 5  LEU A 143 ? ILE A 152 ? LEU A 143 ILE A 152 
AA3 6  ILE A 218 ? ILE A 220 ? ILE A 218 ILE A 220 
AA4 1  GLU B 34  ? ILE B 35  ? GLU B 34  ILE B 35  
AA4 2  ILE B 110 ? VAL B 111 ? ILE B 110 VAL B 111 
AA5 1  LYS B 41  ? TYR B 42  ? LYS B 41  TYR B 42  
AA5 2  ARG B 259 ? ALA B 260 ? ARG B 259 ALA B 260 
AA5 3  TYR B 193 ? GLY B 198 ? TYR B 193 GLY B 198 
AA5 4  VAL B 209 ? LEU B 214 ? VAL B 209 LEU B 214 
AA5 5  LEU B 143 ? ILE B 152 ? LEU B 143 ILE B 152 
AA5 6  ALA B 118 ? ASN B 126 ? ALA B 118 ASN B 126 
AA5 7  TYR B 90  ? TRP B 99  ? TYR B 90  TRP B 99  
AA5 8  PHE B 68  ? PHE B 72  ? PHE B 68  PHE B 72  
AA5 9  ALA B 58  ? ASN B 63  ? ALA B 58  ASN B 63  
AA5 10 GLN B 175 ? ARG B 177 ? GLN B 175 ARG B 177 
AA6 1  LEU B 49  ? LYS B 52  ? LEU B 49  LYS B 52  
AA6 2  VAL B 80  ? GLY B 83  ? VAL B 80  GLY B 83  
AA6 3  TYR B 90  ? TRP B 99  ? TYR B 90  TRP B 99  
AA6 4  ALA B 118 ? ASN B 126 ? ALA B 118 ASN B 126 
AA6 5  LEU B 143 ? ILE B 152 ? LEU B 143 ILE B 152 
AA6 6  ILE B 218 ? ILE B 220 ? ILE B 218 ILE B 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 35  ? N ILE A 35  O ILE A 110 ? O ILE A 110 
AA2 1 2  N LYS A 41  ? N LYS A 41  O ALA A 260 ? O ALA A 260 
AA2 2 3  O ARG A 259 ? O ARG A 259 N THR A 195 ? N THR A 195 
AA2 3 4  N GLY A 198 ? N GLY A 198 O VAL A 209 ? O VAL A 209 
AA2 4 5  O LEU A 214 ? O LEU A 214 N GLY A 147 ? N GLY A 147 
AA2 5 6  O VAL A 148 ? O VAL A 148 N LEU A 120 ? N LEU A 120 
AA2 6 7  O VAL A 123 ? O VAL A 123 N ARG A 93  ? N ARG A 93  
AA2 7 8  O VAL A 95  ? O VAL A 95  N VAL A 70  ? N VAL A 70  
AA2 8 9  O ASN A 69  ? O ASN A 69  N SER A 62  ? N SER A 62  
AA2 9 10 N ILE A 61  ? N ILE A 61  O THR A 176 ? O THR A 176 
AA3 1 2  N SER A 50  ? N SER A 50  O ARG A 82  ? O ARG A 82  
AA3 2 3  N LEU A 81  ? N LEU A 81  O TYR A 90  ? O TYR A 90  
AA3 3 4  N ARG A 93  ? N ARG A 93  O VAL A 123 ? O VAL A 123 
AA3 4 5  N LEU A 120 ? N LEU A 120 O VAL A 148 ? O VAL A 148 
AA3 5 6  N GLN A 151 ? N GLN A 151 O ILE A 218 ? O ILE A 218 
AA4 1 2  N ILE B 35  ? N ILE B 35  O ILE B 110 ? O ILE B 110 
AA5 1 2  N LYS B 41  ? N LYS B 41  O ALA B 260 ? O ALA B 260 
AA5 2 3  O ARG B 259 ? O ARG B 259 N THR B 195 ? N THR B 195 
AA5 3 4  N GLY B 198 ? N GLY B 198 O VAL B 209 ? O VAL B 209 
AA5 4 5  O ILE B 212 ? O ILE B 212 N GLY B 147 ? N GLY B 147 
AA5 5 6  O VAL B 148 ? O VAL B 148 N LEU B 120 ? N LEU B 120 
AA5 6 7  O VAL B 123 ? O VAL B 123 N ARG B 93  ? N ARG B 93  
AA5 7 8  O VAL B 95  ? O VAL B 95  N VAL B 70  ? N VAL B 70  
AA5 8 9  O ASP B 71  ? O ASP B 71  N ILE B 60  ? N ILE B 60  
AA5 9 10 N ILE B 61  ? N ILE B 61  O THR B 176 ? O THR B 176 
AA6 1 2  N SER B 50  ? N SER B 50  O ARG B 82  ? O ARG B 82  
AA6 2 3  N LEU B 81  ? N LEU B 81  O TYR B 90  ? O TYR B 90  
AA6 3 4  N ARG B 93  ? N ARG B 93  O VAL B 123 ? O VAL B 123 
AA6 4 5  N LEU B 120 ? N LEU B 120 O VAL B 148 ? O VAL B 148 
AA6 5 6  N GLN B 151 ? N GLN B 151 O ILE B 218 ? O ILE B 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A PEG 302 ? 8  'binding site for residue PEG A 302' 
AC3 Software A EDO 303 ? 7  'binding site for residue EDO A 303' 
AC4 Software A EDO 304 ? 5  'binding site for residue EDO A 304' 
AC5 Software A EDO 305 ? 5  'binding site for residue EDO A 305' 
AC6 Software A EDO 306 ? 6  'binding site for residue EDO A 306' 
AC7 Software A V14 307 ? 15 'binding site for residue V14 A 307' 
AC8 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC9 Software B CIT 302 ? 9  'binding site for residue CIT B 302' 
AD1 Software B EDO 303 ? 3  'binding site for residue EDO B 303' 
AD2 Software B EDO 304 ? 6  'binding site for residue EDO B 304' 
AD3 Software B EDO 305 ? 3  'binding site for residue EDO B 305' 
AD4 Software B V14 306 ? 18 'binding site for residue V14 B 306' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
2  AC1 4  HIS A 98  ? HIS A 98  . ? 1_555 ? 
3  AC1 4  HIS A 121 ? HIS A 121 . ? 1_555 ? 
4  AC1 4  V14 I .   ? V14 A 307 . ? 1_555 ? 
5  AC2 8  ASP A 28  ? ASP A 28  . ? 1_555 ? 
6  AC2 8  GLN A 29  ? GLN A 29  . ? 1_555 ? 
7  AC2 8  LEU A 253 ? LEU A 253 . ? 1_555 ? 
8  AC2 8  LYS A 254 ? LYS A 254 . ? 1_555 ? 
9  AC2 8  ARG A 256 ? ARG A 256 . ? 1_555 ? 
10 AC2 8  LYS B 59  ? LYS B 59  . ? 1_545 ? 
11 AC2 8  ILE B 60  ? ILE B 60  . ? 1_545 ? 
12 AC2 8  ARG B 177 ? ARG B 177 . ? 1_545 ? 
13 AC3 7  TRP A 191 ? TRP A 191 . ? 1_555 ? 
14 AC3 7  ASP A 192 ? ASP A 192 . ? 1_555 ? 
15 AC3 7  HOH P .   ? HOH A 406 . ? 1_555 ? 
16 AC3 7  HOH P .   ? HOH A 427 . ? 1_555 ? 
17 AC3 7  HOH P .   ? HOH A 438 . ? 1_555 ? 
18 AC3 7  PRO B 48  ? PRO B 48  . ? 1_555 ? 
19 AC3 7  HOH Q .   ? HOH B 440 . ? 1_555 ? 
20 AC4 5  GLN A 158 ? GLN A 158 . ? 1_555 ? 
21 AC4 5  LYS A 161 ? LYS A 161 . ? 1_555 ? 
22 AC4 5  PHE A 181 ? PHE A 181 . ? 1_555 ? 
23 AC4 5  ASP A 182 ? ASP A 182 . ? 1_555 ? 
24 AC4 5  SER A 185 ? SER A 185 . ? 1_555 ? 
25 AC5 5  LYS A 161 ? LYS A 161 . ? 1_555 ? 
26 AC5 5  ARG A 177 ? ARG A 177 . ? 1_555 ? 
27 AC5 5  PHE A 178 ? PHE A 178 . ? 1_555 ? 
28 AC5 5  THR A 179 ? THR A 179 . ? 1_555 ? 
29 AC5 5  HOH P .   ? HOH A 468 . ? 1_555 ? 
30 AC6 6  GLY A 100 ? GLY A 100 . ? 1_555 ? 
31 AC6 6  SER A 101 ? SER A 101 . ? 1_555 ? 
32 AC6 6  HIS A 105 ? HIS A 105 . ? 1_555 ? 
33 AC6 6  SER A 245 ? SER A 245 . ? 1_555 ? 
34 AC6 6  HIS A 247 ? HIS A 247 . ? 1_555 ? 
35 AC6 6  HOH P .   ? HOH A 557 . ? 1_555 ? 
36 AC7 15 SER A 64  ? SER A 64  . ? 1_555 ? 
37 AC7 15 HIS A 66  ? HIS A 66  . ? 1_555 ? 
38 AC7 15 SER A 67  ? SER A 67  . ? 1_555 ? 
39 AC7 15 ASN A 69  ? ASN A 69  . ? 1_555 ? 
40 AC7 15 GLN A 94  ? GLN A 94  . ? 1_555 ? 
41 AC7 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
42 AC7 15 HIS A 98  ? HIS A 98  . ? 1_555 ? 
43 AC7 15 HIS A 121 ? HIS A 121 . ? 1_555 ? 
44 AC7 15 VAL A 123 ? VAL A 123 . ? 1_555 ? 
45 AC7 15 PHE A 133 ? PHE A 133 . ? 1_555 ? 
46 AC7 15 LEU A 200 ? LEU A 200 . ? 1_555 ? 
47 AC7 15 THR A 201 ? THR A 201 . ? 1_555 ? 
48 AC7 15 VAL A 202 ? VAL A 202 . ? 1_555 ? 
49 AC7 15 ZN  C .   ? ZN  A 301 . ? 1_555 ? 
50 AC7 15 HOH P .   ? HOH A 474 . ? 1_555 ? 
51 AC8 4  HIS B 96  ? HIS B 96  . ? 1_555 ? 
52 AC8 4  HIS B 98  ? HIS B 98  . ? 1_555 ? 
53 AC8 4  HIS B 121 ? HIS B 121 . ? 1_555 ? 
54 AC8 4  V14 O .   ? V14 B 306 . ? 1_555 ? 
55 AC9 9  HOH P .   ? HOH A 492 . ? 4_455 ? 
56 AC9 9  GLY B 100 ? GLY B 100 . ? 1_555 ? 
57 AC9 9  SER B 101 ? SER B 101 . ? 1_555 ? 
58 AC9 9  HIS B 105 ? HIS B 105 . ? 1_555 ? 
59 AC9 9  SER B 245 ? SER B 245 . ? 1_555 ? 
60 AC9 9  HIS B 247 ? HIS B 247 . ? 1_555 ? 
61 AC9 9  HOH Q .   ? HOH B 408 . ? 1_555 ? 
62 AC9 9  HOH Q .   ? HOH B 524 . ? 1_555 ? 
63 AC9 9  HOH Q .   ? HOH B 572 . ? 1_555 ? 
64 AD1 3  SER A 50  ? SER A 50  . ? 1_555 ? 
65 AD1 3  ARG A 82  ? ARG A 82  . ? 1_555 ? 
66 AD1 3  PRO B 189 ? PRO B 189 . ? 1_555 ? 
67 AD2 6  GLU A 39  ? GLU A 39  . ? 1_565 ? 
68 AD2 6  PRO B 131 ? PRO B 131 . ? 1_555 ? 
69 AD2 6  SER B 132 ? SER B 132 . ? 1_555 ? 
70 AD2 6  HOH Q .   ? HOH B 425 . ? 1_555 ? 
71 AD2 6  HOH Q .   ? HOH B 570 . ? 1_555 ? 
72 AD2 6  HOH Q .   ? HOH B 575 . ? 1_555 ? 
73 AD3 3  ASP B 54  ? ASP B 54  . ? 1_555 ? 
74 AD3 3  SER B 56  ? SER B 56  . ? 1_555 ? 
75 AD3 3  LYS B 78  ? LYS B 78  . ? 1_555 ? 
76 AD4 18 TRP B 7   ? TRP B 7   . ? 1_555 ? 
77 AD4 18 SER B 64  ? SER B 64  . ? 1_555 ? 
78 AD4 18 HIS B 66  ? HIS B 66  . ? 1_555 ? 
79 AD4 18 SER B 67  ? SER B 67  . ? 1_555 ? 
80 AD4 18 ASN B 69  ? ASN B 69  . ? 1_555 ? 
81 AD4 18 GLN B 94  ? GLN B 94  . ? 1_555 ? 
82 AD4 18 HIS B 96  ? HIS B 96  . ? 1_555 ? 
83 AD4 18 HIS B 98  ? HIS B 98  . ? 1_555 ? 
84 AD4 18 HIS B 121 ? HIS B 121 . ? 1_555 ? 
85 AD4 18 VAL B 123 ? VAL B 123 . ? 1_555 ? 
86 AD4 18 PHE B 133 ? PHE B 133 . ? 1_555 ? 
87 AD4 18 LEU B 200 ? LEU B 200 . ? 1_555 ? 
88 AD4 18 THR B 201 ? THR B 201 . ? 1_555 ? 
89 AD4 18 VAL B 202 ? VAL B 202 . ? 1_555 ? 
90 AD4 18 TRP B 211 ? TRP B 211 . ? 1_555 ? 
91 AD4 18 ZN  J .   ? ZN  B 301 . ? 1_555 ? 
92 AD4 18 HOH Q .   ? HOH B 500 . ? 1_555 ? 
93 AD4 18 HOH Q .   ? HOH B 571 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ZN  A ZN  301 ? ? N10 A V14 307 ? ? 1.70 
2 1 NE2 B GLN 158 ? A O   B HOH 401 ? ? 2.02 
3 1 O   B HOH 594 ? ? O   B HOH 604 ? ? 2.03 
4 1 OD2 B ASP 104 ? ? O   B HOH 402 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     410 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     457 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_545 
_pdbx_validate_symm_contact.dist              2.13 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 66  ? ? CD2 A HIS 66  ? ? 1.412 1.354 0.058 0.009 N 
2 1 CG A HIS 121 ? ? CD2 A HIS 121 ? ? 1.412 1.354 0.058 0.009 N 
3 1 CG B HIS 12  ? ? CD2 B HIS 12  ? ? 1.414 1.354 0.060 0.009 N 
4 1 CG B HIS 263 ? ? CD2 B HIS 263 ? ? 1.412 1.354 0.058 0.009 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 13  ? ? -150.13 2.09    
2 1 SER A 67  ? ? -176.70 -173.69 
3 1 ASN A 77  ? ? -97.31  34.56   
4 1 ASN A 246 ? ? -153.10 44.55   
5 1 SER B 67  ? ? -175.48 -173.67 
6 1 ASN B 77  ? ? -97.90  46.06   
7 1 HIS B 105 ? ? -155.12 75.52   
8 1 PHE B 178 ? ? -160.13 116.71  
9 1 ASN B 246 ? ? -155.93 45.97   
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1 ? A MET 1 
2  1 Y 1 A MET 2 ? A MET 2 
3  1 Y 1 A SER 3 ? A SER 3 
4  1 Y 1 A ARG 4 ? A ARG 4 
5  1 Y 1 A LEU 5 ? A LEU 5 
6  1 Y 1 B MET 1 ? B MET 1 
7  1 Y 1 B MET 2 ? B MET 2 
8  1 Y 1 B SER 3 ? B SER 3 
9  1 Y 1 B ARG 4 ? B ARG 4 
10 1 Y 1 B LEU 5 ? B LEU 5 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CIT C1   C  N N 74  
CIT O1   O  N N 75  
CIT O2   O  N N 76  
CIT C2   C  N N 77  
CIT C3   C  N N 78  
CIT O7   O  N N 79  
CIT C4   C  N N 80  
CIT C5   C  N N 81  
CIT O3   O  N N 82  
CIT O4   O  N N 83  
CIT C6   C  N N 84  
CIT O5   O  N N 85  
CIT O6   O  N N 86  
CIT HO2  H  N N 87  
CIT H21  H  N N 88  
CIT H22  H  N N 89  
CIT HO7  H  N N 90  
CIT H41  H  N N 91  
CIT H42  H  N N 92  
CIT HO4  H  N N 93  
CIT HO6  H  N N 94  
CYS N    N  N N 95  
CYS CA   C  N R 96  
CYS C    C  N N 97  
CYS O    O  N N 98  
CYS CB   C  N N 99  
CYS SG   S  N N 100 
CYS OXT  O  N N 101 
CYS H    H  N N 102 
CYS H2   H  N N 103 
CYS HA   H  N N 104 
CYS HB2  H  N N 105 
CYS HB3  H  N N 106 
CYS HG   H  N N 107 
CYS HXT  H  N N 108 
EDO C1   C  N N 109 
EDO O1   O  N N 110 
EDO C2   C  N N 111 
EDO O2   O  N N 112 
EDO H11  H  N N 113 
EDO H12  H  N N 114 
EDO HO1  H  N N 115 
EDO H21  H  N N 116 
EDO H22  H  N N 117 
EDO HO2  H  N N 118 
GLN N    N  N N 119 
GLN CA   C  N S 120 
GLN C    C  N N 121 
GLN O    O  N N 122 
GLN CB   C  N N 123 
GLN CG   C  N N 124 
GLN CD   C  N N 125 
GLN OE1  O  N N 126 
GLN NE2  N  N N 127 
GLN OXT  O  N N 128 
GLN H    H  N N 129 
GLN H2   H  N N 130 
GLN HA   H  N N 131 
GLN HB2  H  N N 132 
GLN HB3  H  N N 133 
GLN HG2  H  N N 134 
GLN HG3  H  N N 135 
GLN HE21 H  N N 136 
GLN HE22 H  N N 137 
GLN HXT  H  N N 138 
GLU N    N  N N 139 
GLU CA   C  N S 140 
GLU C    C  N N 141 
GLU O    O  N N 142 
GLU CB   C  N N 143 
GLU CG   C  N N 144 
GLU CD   C  N N 145 
GLU OE1  O  N N 146 
GLU OE2  O  N N 147 
GLU OXT  O  N N 148 
GLU H    H  N N 149 
GLU H2   H  N N 150 
GLU HA   H  N N 151 
GLU HB2  H  N N 152 
GLU HB3  H  N N 153 
GLU HG2  H  N N 154 
GLU HG3  H  N N 155 
GLU HE2  H  N N 156 
GLU HXT  H  N N 157 
GLY N    N  N N 158 
GLY CA   C  N N 159 
GLY C    C  N N 160 
GLY O    O  N N 161 
GLY OXT  O  N N 162 
GLY H    H  N N 163 
GLY H2   H  N N 164 
GLY HA2  H  N N 165 
GLY HA3  H  N N 166 
GLY HXT  H  N N 167 
HIS N    N  N N 168 
HIS CA   C  N S 169 
HIS C    C  N N 170 
HIS O    O  N N 171 
HIS CB   C  N N 172 
HIS CG   C  Y N 173 
HIS ND1  N  Y N 174 
HIS CD2  C  Y N 175 
HIS CE1  C  Y N 176 
HIS NE2  N  Y N 177 
HIS OXT  O  N N 178 
HIS H    H  N N 179 
HIS H2   H  N N 180 
HIS HA   H  N N 181 
HIS HB2  H  N N 182 
HIS HB3  H  N N 183 
HIS HD1  H  N N 184 
HIS HD2  H  N N 185 
HIS HE1  H  N N 186 
HIS HE2  H  N N 187 
HIS HXT  H  N N 188 
HOH O    O  N N 189 
HOH H1   H  N N 190 
HOH H2   H  N N 191 
ILE N    N  N N 192 
ILE CA   C  N S 193 
ILE C    C  N N 194 
ILE O    O  N N 195 
ILE CB   C  N S 196 
ILE CG1  C  N N 197 
ILE CG2  C  N N 198 
ILE CD1  C  N N 199 
ILE OXT  O  N N 200 
ILE H    H  N N 201 
ILE H2   H  N N 202 
ILE HA   H  N N 203 
ILE HB   H  N N 204 
ILE HG12 H  N N 205 
ILE HG13 H  N N 206 
ILE HG21 H  N N 207 
ILE HG22 H  N N 208 
ILE HG23 H  N N 209 
ILE HD11 H  N N 210 
ILE HD12 H  N N 211 
ILE HD13 H  N N 212 
ILE HXT  H  N N 213 
LEU N    N  N N 214 
LEU CA   C  N S 215 
LEU C    C  N N 216 
LEU O    O  N N 217 
LEU CB   C  N N 218 
LEU CG   C  N N 219 
LEU CD1  C  N N 220 
LEU CD2  C  N N 221 
LEU OXT  O  N N 222 
LEU H    H  N N 223 
LEU H2   H  N N 224 
LEU HA   H  N N 225 
LEU HB2  H  N N 226 
LEU HB3  H  N N 227 
LEU HG   H  N N 228 
LEU HD11 H  N N 229 
LEU HD12 H  N N 230 
LEU HD13 H  N N 231 
LEU HD21 H  N N 232 
LEU HD22 H  N N 233 
LEU HD23 H  N N 234 
LEU HXT  H  N N 235 
LYS N    N  N N 236 
LYS CA   C  N S 237 
LYS C    C  N N 238 
LYS O    O  N N 239 
LYS CB   C  N N 240 
LYS CG   C  N N 241 
LYS CD   C  N N 242 
LYS CE   C  N N 243 
LYS NZ   N  N N 244 
LYS OXT  O  N N 245 
LYS H    H  N N 246 
LYS H2   H  N N 247 
LYS HA   H  N N 248 
LYS HB2  H  N N 249 
LYS HB3  H  N N 250 
LYS HG2  H  N N 251 
LYS HG3  H  N N 252 
LYS HD2  H  N N 253 
LYS HD3  H  N N 254 
LYS HE2  H  N N 255 
LYS HE3  H  N N 256 
LYS HZ1  H  N N 257 
LYS HZ2  H  N N 258 
LYS HZ3  H  N N 259 
LYS HXT  H  N N 260 
MET N    N  N N 261 
MET CA   C  N S 262 
MET C    C  N N 263 
MET O    O  N N 264 
MET CB   C  N N 265 
MET CG   C  N N 266 
MET SD   S  N N 267 
MET CE   C  N N 268 
MET OXT  O  N N 269 
MET H    H  N N 270 
MET H2   H  N N 271 
MET HA   H  N N 272 
MET HB2  H  N N 273 
MET HB3  H  N N 274 
MET HG2  H  N N 275 
MET HG3  H  N N 276 
MET HE1  H  N N 277 
MET HE2  H  N N 278 
MET HE3  H  N N 279 
MET HXT  H  N N 280 
PEG C1   C  N N 281 
PEG O1   O  N N 282 
PEG C2   C  N N 283 
PEG O2   O  N N 284 
PEG C3   C  N N 285 
PEG C4   C  N N 286 
PEG O4   O  N N 287 
PEG H11  H  N N 288 
PEG H12  H  N N 289 
PEG HO1  H  N N 290 
PEG H21  H  N N 291 
PEG H22  H  N N 292 
PEG H31  H  N N 293 
PEG H32  H  N N 294 
PEG H41  H  N N 295 
PEG H42  H  N N 296 
PEG HO4  H  N N 297 
PHE N    N  N N 298 
PHE CA   C  N S 299 
PHE C    C  N N 300 
PHE O    O  N N 301 
PHE CB   C  N N 302 
PHE CG   C  Y N 303 
PHE CD1  C  Y N 304 
PHE CD2  C  Y N 305 
PHE CE1  C  Y N 306 
PHE CE2  C  Y N 307 
PHE CZ   C  Y N 308 
PHE OXT  O  N N 309 
PHE H    H  N N 310 
PHE H2   H  N N 311 
PHE HA   H  N N 312 
PHE HB2  H  N N 313 
PHE HB3  H  N N 314 
PHE HD1  H  N N 315 
PHE HD2  H  N N 316 
PHE HE1  H  N N 317 
PHE HE2  H  N N 318 
PHE HZ   H  N N 319 
PHE HXT  H  N N 320 
PRO N    N  N N 321 
PRO CA   C  N S 322 
PRO C    C  N N 323 
PRO O    O  N N 324 
PRO CB   C  N N 325 
PRO CG   C  N N 326 
PRO CD   C  N N 327 
PRO OXT  O  N N 328 
PRO H    H  N N 329 
PRO HA   H  N N 330 
PRO HB2  H  N N 331 
PRO HB3  H  N N 332 
PRO HG2  H  N N 333 
PRO HG3  H  N N 334 
PRO HD2  H  N N 335 
PRO HD3  H  N N 336 
PRO HXT  H  N N 337 
SER N    N  N N 338 
SER CA   C  N S 339 
SER C    C  N N 340 
SER O    O  N N 341 
SER CB   C  N N 342 
SER OG   O  N N 343 
SER OXT  O  N N 344 
SER H    H  N N 345 
SER H2   H  N N 346 
SER HA   H  N N 347 
SER HB2  H  N N 348 
SER HB3  H  N N 349 
SER HG   H  N N 350 
SER HXT  H  N N 351 
THR N    N  N N 352 
THR CA   C  N S 353 
THR C    C  N N 354 
THR O    O  N N 355 
THR CB   C  N R 356 
THR OG1  O  N N 357 
THR CG2  C  N N 358 
THR OXT  O  N N 359 
THR H    H  N N 360 
THR H2   H  N N 361 
THR HA   H  N N 362 
THR HB   H  N N 363 
THR HG1  H  N N 364 
THR HG21 H  N N 365 
THR HG22 H  N N 366 
THR HG23 H  N N 367 
THR HXT  H  N N 368 
TRP N    N  N N 369 
TRP CA   C  N S 370 
TRP C    C  N N 371 
TRP O    O  N N 372 
TRP CB   C  N N 373 
TRP CG   C  Y N 374 
TRP CD1  C  Y N 375 
TRP CD2  C  Y N 376 
TRP NE1  N  Y N 377 
TRP CE2  C  Y N 378 
TRP CE3  C  Y N 379 
TRP CZ2  C  Y N 380 
TRP CZ3  C  Y N 381 
TRP CH2  C  Y N 382 
TRP OXT  O  N N 383 
TRP H    H  N N 384 
TRP H2   H  N N 385 
TRP HA   H  N N 386 
TRP HB2  H  N N 387 
TRP HB3  H  N N 388 
TRP HD1  H  N N 389 
TRP HE1  H  N N 390 
TRP HE3  H  N N 391 
TRP HZ2  H  N N 392 
TRP HZ3  H  N N 393 
TRP HH2  H  N N 394 
TRP HXT  H  N N 395 
TYR N    N  N N 396 
TYR CA   C  N S 397 
TYR C    C  N N 398 
TYR O    O  N N 399 
TYR CB   C  N N 400 
TYR CG   C  Y N 401 
TYR CD1  C  Y N 402 
TYR CD2  C  Y N 403 
TYR CE1  C  Y N 404 
TYR CE2  C  Y N 405 
TYR CZ   C  Y N 406 
TYR OH   O  N N 407 
TYR OXT  O  N N 408 
TYR H    H  N N 409 
TYR H2   H  N N 410 
TYR HA   H  N N 411 
TYR HB2  H  N N 412 
TYR HB3  H  N N 413 
TYR HD1  H  N N 414 
TYR HD2  H  N N 415 
TYR HE1  H  N N 416 
TYR HE2  H  N N 417 
TYR HH   H  N N 418 
TYR HXT  H  N N 419 
V14 F20  F  N N 420 
V14 C5   C  Y N 421 
V14 C4   C  Y N 422 
V14 S7   S  N N 423 
V14 O9   O  N N 424 
V14 N10  N  N N 425 
V14 O8   O  N N 426 
V14 C3   C  Y N 427 
V14 F12  F  N N 428 
V14 C2   C  Y N 429 
V14 F13  F  N N 430 
V14 C6   C  Y N 431 
V14 C1   C  Y N 432 
V14 S11  S  N N 433 
V14 O16  O  N N 434 
V14 O17  O  N N 435 
V14 C15  C  N N 436 
V14 C18  C  N N 437 
V14 O21  O  N N 438 
V14 N19  N  N N 439 
V14 C14  C  N N 440 
V14 C28  C  N N 441 
V14 C27  C  N N 442 
V14 C26  C  N N 443 
V14 C25  C  N N 444 
V14 C24  C  N N 445 
V14 C23  C  N N 446 
V14 C22  C  N N 447 
V14 H1   H  N N 448 
V14 H2   H  N N 449 
V14 H3   H  N N 450 
V14 H4   H  N N 451 
V14 H5   H  N N 452 
V14 H6   H  N N 453 
V14 H7   H  N N 454 
V14 H8   H  N N 455 
V14 H9   H  N N 456 
V14 H10  H  N N 457 
V14 H11  H  N N 458 
V14 H12  H  N N 459 
V14 H13  H  N N 460 
V14 H14  H  N N 461 
V14 H15  H  N N 462 
V14 H16  H  N N 463 
V14 H17  H  N N 464 
V14 H18  H  N N 465 
V14 H19  H  N N 466 
V14 H20  H  N N 467 
V14 H21  H  N N 468 
V14 H22  H  N N 469 
V14 H23  H  N N 470 
VAL N    N  N N 471 
VAL CA   C  N S 472 
VAL C    C  N N 473 
VAL O    O  N N 474 
VAL CB   C  N N 475 
VAL CG1  C  N N 476 
VAL CG2  C  N N 477 
VAL OXT  O  N N 478 
VAL H    H  N N 479 
VAL H2   H  N N 480 
VAL HA   H  N N 481 
VAL HB   H  N N 482 
VAL HG11 H  N N 483 
VAL HG12 H  N N 484 
VAL HG13 H  N N 485 
VAL HG21 H  N N 486 
VAL HG22 H  N N 487 
VAL HG23 H  N N 488 
VAL HXT  H  N N 489 
ZN  ZN   ZN N N 490 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
EDO C1  O1   sing N N 103 
EDO C1  C2   sing N N 104 
EDO C1  H11  sing N N 105 
EDO C1  H12  sing N N 106 
EDO O1  HO1  sing N N 107 
EDO C2  O2   sing N N 108 
EDO C2  H21  sing N N 109 
EDO C2  H22  sing N N 110 
EDO O2  HO2  sing N N 111 
GLN N   CA   sing N N 112 
GLN N   H    sing N N 113 
GLN N   H2   sing N N 114 
GLN CA  C    sing N N 115 
GLN CA  CB   sing N N 116 
GLN CA  HA   sing N N 117 
GLN C   O    doub N N 118 
GLN C   OXT  sing N N 119 
GLN CB  CG   sing N N 120 
GLN CB  HB2  sing N N 121 
GLN CB  HB3  sing N N 122 
GLN CG  CD   sing N N 123 
GLN CG  HG2  sing N N 124 
GLN CG  HG3  sing N N 125 
GLN CD  OE1  doub N N 126 
GLN CD  NE2  sing N N 127 
GLN NE2 HE21 sing N N 128 
GLN NE2 HE22 sing N N 129 
GLN OXT HXT  sing N N 130 
GLU N   CA   sing N N 131 
GLU N   H    sing N N 132 
GLU N   H2   sing N N 133 
GLU CA  C    sing N N 134 
GLU CA  CB   sing N N 135 
GLU CA  HA   sing N N 136 
GLU C   O    doub N N 137 
GLU C   OXT  sing N N 138 
GLU CB  CG   sing N N 139 
GLU CB  HB2  sing N N 140 
GLU CB  HB3  sing N N 141 
GLU CG  CD   sing N N 142 
GLU CG  HG2  sing N N 143 
GLU CG  HG3  sing N N 144 
GLU CD  OE1  doub N N 145 
GLU CD  OE2  sing N N 146 
GLU OE2 HE2  sing N N 147 
GLU OXT HXT  sing N N 148 
GLY N   CA   sing N N 149 
GLY N   H    sing N N 150 
GLY N   H2   sing N N 151 
GLY CA  C    sing N N 152 
GLY CA  HA2  sing N N 153 
GLY CA  HA3  sing N N 154 
GLY C   O    doub N N 155 
GLY C   OXT  sing N N 156 
GLY OXT HXT  sing N N 157 
HIS N   CA   sing N N 158 
HIS N   H    sing N N 159 
HIS N   H2   sing N N 160 
HIS CA  C    sing N N 161 
HIS CA  CB   sing N N 162 
HIS CA  HA   sing N N 163 
HIS C   O    doub N N 164 
HIS C   OXT  sing N N 165 
HIS CB  CG   sing N N 166 
HIS CB  HB2  sing N N 167 
HIS CB  HB3  sing N N 168 
HIS CG  ND1  sing Y N 169 
HIS CG  CD2  doub Y N 170 
HIS ND1 CE1  doub Y N 171 
HIS ND1 HD1  sing N N 172 
HIS CD2 NE2  sing Y N 173 
HIS CD2 HD2  sing N N 174 
HIS CE1 NE2  sing Y N 175 
HIS CE1 HE1  sing N N 176 
HIS NE2 HE2  sing N N 177 
HIS OXT HXT  sing N N 178 
HOH O   H1   sing N N 179 
HOH O   H2   sing N N 180 
ILE N   CA   sing N N 181 
ILE N   H    sing N N 182 
ILE N   H2   sing N N 183 
ILE CA  C    sing N N 184 
ILE CA  CB   sing N N 185 
ILE CA  HA   sing N N 186 
ILE C   O    doub N N 187 
ILE C   OXT  sing N N 188 
ILE CB  CG1  sing N N 189 
ILE CB  CG2  sing N N 190 
ILE CB  HB   sing N N 191 
ILE CG1 CD1  sing N N 192 
ILE CG1 HG12 sing N N 193 
ILE CG1 HG13 sing N N 194 
ILE CG2 HG21 sing N N 195 
ILE CG2 HG22 sing N N 196 
ILE CG2 HG23 sing N N 197 
ILE CD1 HD11 sing N N 198 
ILE CD1 HD12 sing N N 199 
ILE CD1 HD13 sing N N 200 
ILE OXT HXT  sing N N 201 
LEU N   CA   sing N N 202 
LEU N   H    sing N N 203 
LEU N   H2   sing N N 204 
LEU CA  C    sing N N 205 
LEU CA  CB   sing N N 206 
LEU CA  HA   sing N N 207 
LEU C   O    doub N N 208 
LEU C   OXT  sing N N 209 
LEU CB  CG   sing N N 210 
LEU CB  HB2  sing N N 211 
LEU CB  HB3  sing N N 212 
LEU CG  CD1  sing N N 213 
LEU CG  CD2  sing N N 214 
LEU CG  HG   sing N N 215 
LEU CD1 HD11 sing N N 216 
LEU CD1 HD12 sing N N 217 
LEU CD1 HD13 sing N N 218 
LEU CD2 HD21 sing N N 219 
LEU CD2 HD22 sing N N 220 
LEU CD2 HD23 sing N N 221 
LEU OXT HXT  sing N N 222 
LYS N   CA   sing N N 223 
LYS N   H    sing N N 224 
LYS N   H2   sing N N 225 
LYS CA  C    sing N N 226 
LYS CA  CB   sing N N 227 
LYS CA  HA   sing N N 228 
LYS C   O    doub N N 229 
LYS C   OXT  sing N N 230 
LYS CB  CG   sing N N 231 
LYS CB  HB2  sing N N 232 
LYS CB  HB3  sing N N 233 
LYS CG  CD   sing N N 234 
LYS CG  HG2  sing N N 235 
LYS CG  HG3  sing N N 236 
LYS CD  CE   sing N N 237 
LYS CD  HD2  sing N N 238 
LYS CD  HD3  sing N N 239 
LYS CE  NZ   sing N N 240 
LYS CE  HE2  sing N N 241 
LYS CE  HE3  sing N N 242 
LYS NZ  HZ1  sing N N 243 
LYS NZ  HZ2  sing N N 244 
LYS NZ  HZ3  sing N N 245 
LYS OXT HXT  sing N N 246 
MET N   CA   sing N N 247 
MET N   H    sing N N 248 
MET N   H2   sing N N 249 
MET CA  C    sing N N 250 
MET CA  CB   sing N N 251 
MET CA  HA   sing N N 252 
MET C   O    doub N N 253 
MET C   OXT  sing N N 254 
MET CB  CG   sing N N 255 
MET CB  HB2  sing N N 256 
MET CB  HB3  sing N N 257 
MET CG  SD   sing N N 258 
MET CG  HG2  sing N N 259 
MET CG  HG3  sing N N 260 
MET SD  CE   sing N N 261 
MET CE  HE1  sing N N 262 
MET CE  HE2  sing N N 263 
MET CE  HE3  sing N N 264 
MET OXT HXT  sing N N 265 
PEG C1  O1   sing N N 266 
PEG C1  C2   sing N N 267 
PEG C1  H11  sing N N 268 
PEG C1  H12  sing N N 269 
PEG O1  HO1  sing N N 270 
PEG C2  O2   sing N N 271 
PEG C2  H21  sing N N 272 
PEG C2  H22  sing N N 273 
PEG O2  C3   sing N N 274 
PEG C3  C4   sing N N 275 
PEG C3  H31  sing N N 276 
PEG C3  H32  sing N N 277 
PEG C4  O4   sing N N 278 
PEG C4  H41  sing N N 279 
PEG C4  H42  sing N N 280 
PEG O4  HO4  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
V14 C18 O21  sing N N 403 
V14 C18 C15  sing N N 404 
V14 C15 S11  sing N N 405 
V14 O17 S11  doub N N 406 
V14 C22 C23  sing N N 407 
V14 C22 C14  sing N N 408 
V14 C23 C24  sing N N 409 
V14 N19 C14  sing N N 410 
V14 N19 C6   sing N N 411 
V14 C24 C25  sing N N 412 
V14 S11 C1   sing N N 413 
V14 S11 O16  doub N N 414 
V14 C14 C28  sing N N 415 
V14 C6  C1   doub Y N 416 
V14 C6  C5   sing Y N 417 
V14 C1  C2   sing Y N 418 
V14 F20 C5   sing N N 419 
V14 C25 C26  sing N N 420 
V14 C5  C4   doub Y N 421 
V14 C26 C27  sing N N 422 
V14 C28 C27  sing N N 423 
V14 C2  F13  sing N N 424 
V14 C2  C3   doub Y N 425 
V14 C4  C3   sing Y N 426 
V14 C4  S7   sing N N 427 
V14 C3  F12  sing N N 428 
V14 N10 S7   sing N N 429 
V14 S7  O9   doub N N 430 
V14 S7  O8   doub N N 431 
V14 N10 H1   sing N N 432 
V14 N10 H2   sing N N 433 
V14 C15 H3   sing N N 434 
V14 C15 H4   sing N N 435 
V14 C18 H5   sing N N 436 
V14 C18 H6   sing N N 437 
V14 O21 H7   sing N N 438 
V14 N19 H8   sing N N 439 
V14 C14 H9   sing N N 440 
V14 C28 H10  sing N N 441 
V14 C28 H11  sing N N 442 
V14 C27 H12  sing N N 443 
V14 C27 H13  sing N N 444 
V14 C26 H14  sing N N 445 
V14 C26 H15  sing N N 446 
V14 C25 H16  sing N N 447 
V14 C25 H17  sing N N 448 
V14 C24 H18  sing N N 449 
V14 C24 H19  sing N N 450 
V14 C23 H20  sing N N 451 
V14 C23 H21  sing N N 452 
V14 C22 H22  sing N N 453 
V14 C22 H23  sing N N 454 
VAL N   CA   sing N N 455 
VAL N   H    sing N N 456 
VAL N   H2   sing N N 457 
VAL CA  C    sing N N 458 
VAL CA  CB   sing N N 459 
VAL CA  HA   sing N N 460 
VAL C   O    doub N N 461 
VAL C   OXT  sing N N 462 
VAL CB  CG1  sing N N 463 
VAL CB  CG2  sing N N 464 
VAL CB  HB   sing N N 465 
VAL CG1 HG11 sing N N 466 
VAL CG1 HG12 sing N N 467 
VAL CG1 HG13 sing N N 468 
VAL CG2 HG21 sing N N 469 
VAL CG2 HG22 sing N N 470 
VAL CG2 HG23 sing N N 471 
VAL OXT HXT  sing N N 472 
# 
_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   4QSJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5E2N 
_atom_sites.fract_transf_matrix[1][1]   0.017829 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.017362 
_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]   0.006260 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
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   . SER A 1 6   ? 23.786  -14.767 -28.766 1.00 37.65 ? 6   SER A N   1 
ATOM   2    C  CA  . SER A 1 6   ? 22.658  -14.121 -28.024 1.00 44.49 ? 6   SER A CA  1 
ATOM   3    C  C   . SER A 1 6   ? 21.408  -14.016 -28.873 1.00 38.03 ? 6   SER A C   1 
ATOM   4    O  O   . SER A 1 6   ? 21.444  -14.058 -30.098 1.00 33.36 ? 6   SER A O   1 
ATOM   5    C  CB  . SER A 1 6   ? 23.043  -12.738 -27.507 1.00 45.46 ? 6   SER A CB  1 
ATOM   6    O  OG  . SER A 1 6   ? 24.053  -12.847 -26.525 1.00 56.07 ? 6   SER A OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 20.258  -13.980 -28.210 1.00 29.50 ? 7   TRP A N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 18.983  -14.160 -28.889 1.00 24.11 ? 7   TRP A CA  1 
ATOM   9    C  C   . TRP A 1 7   ? 18.574  -13.003 -29.751 1.00 20.62 ? 7   TRP A C   1 
ATOM   10   O  O   . TRP A 1 7   ? 18.810  -11.829 -29.393 1.00 20.44 ? 7   TRP A O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 17.884  -14.467 -27.878 1.00 19.94 ? 7   TRP A CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? 17.420  -13.257 -27.102 1.00 20.20 ? 7   TRP A CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? 17.892  -12.804 -25.873 1.00 22.73 ? 7   TRP A CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? 16.370  -12.300 -27.482 1.00 19.28 ? 7   TRP A CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? 17.226  -11.670 -25.482 1.00 23.63 ? 7   TRP A NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? 16.302  -11.315 -26.400 1.00 20.66 ? 7   TRP A CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? 15.515  -12.168 -28.566 1.00 19.05 ? 7   TRP A CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? 15.412  -10.257 -26.427 1.00 17.33 ? 7   TRP A CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? 14.621  -11.095 -28.581 1.00 19.41 ? 7   TRP A CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? 14.572  -10.165 -27.536 1.00 18.98 ? 7   TRP A CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 17.947  -13.298 -30.890 1.00 19.39 ? 8   GLY A N   1 
ATOM   22   C  CA  . GLY A 1 8   ? 17.400  -12.222 -31.736 1.00 20.48 ? 8   GLY A CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 16.357  -12.742 -32.650 1.00 16.56 ? 8   GLY A C   1 
ATOM   24   O  O   . GLY A 1 8   ? 15.554  -13.632 -32.313 1.00 17.02 ? 8   GLY A O   1 
ATOM   25   N  N   . TYR A 1 9   ? 16.347  -12.218 -33.907 1.00 17.89 ? 9   TYR A N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 15.346  -12.667 -34.829 1.00 17.72 ? 9   TYR A CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 15.938  -13.015 -36.187 1.00 20.64 ? 9   TYR A C   1 
ATOM   28   O  O   . TYR A 1 9   ? 15.245  -13.015 -37.200 1.00 23.29 ? 9   TYR A O   1 
ATOM   29   C  CB  . TYR A 1 9   ? 14.366  -11.511 -35.076 1.00 18.03 ? 9   TYR A CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? 13.511  -11.140 -33.824 1.00 13.70 ? 9   TYR A CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? 12.307  -11.806 -33.564 1.00 14.38 ? 9   TYR A CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? 13.984  -10.131 -32.971 1.00 14.86 ? 9   TYR A CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? 11.551  -11.489 -32.415 1.00 14.64 ? 9   TYR A CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? 13.190  -9.807  -31.842 1.00 14.19 ? 9   TYR A CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? 12.028  -10.491 -31.624 1.00 15.94 ? 9   TYR A CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? 11.333  -10.057 -30.507 1.00 14.42 ? 9   TYR A OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 17.231  -13.273 -36.153 1.00 22.82 ? 10  ARG A N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 17.990  -13.775 -37.330 1.00 25.45 ? 10  ARG A CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 17.879  -15.286 -37.466 1.00 27.50 ? 10  ARG A C   1 
ATOM   40   O  O   . ARG A 1 10  ? 17.316  -16.013 -36.614 1.00 27.40 ? 10  ARG A O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 19.407  -13.218 -37.264 1.00 30.05 ? 10  ARG A CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? 19.412  -11.718 -37.463 1.00 35.96 ? 10  ARG A CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? 20.683  -11.002 -37.038 1.00 42.57 ? 10  ARG A CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? 21.664  -10.964 -38.126 1.00 53.64 ? 10  ARG A NE  1 
ATOM   45   N  N   . GLU A 1 11  ? 18.412  -15.812 -38.587 1.00 32.15 ? 11  GLU A N   1 
ATOM   46   C  CA  . GLU A 1 11  ? 18.303  -17.242 -38.850 1.00 31.11 ? 11  GLU A CA  1 
ATOM   47   C  C   . GLU A 1 11  ? 18.775  -18.138 -37.701 1.00 30.29 ? 11  GLU A C   1 
ATOM   48   O  O   . GLU A 1 11  ? 18.063  -19.091 -37.296 1.00 33.19 ? 11  GLU A O   1 
ATOM   49   C  CB  . GLU A 1 11  ? 19.091  -17.552 -40.153 1.00 35.96 ? 11  GLU A CB  1 
ATOM   50   C  CG  . GLU A 1 11  ? 19.451  -19.012 -40.378 1.00 53.75 ? 11  GLU A CG  1 
ATOM   51   C  CD  . GLU A 1 11  ? 18.248  -19.940 -40.467 1.00 62.14 ? 11  GLU A CD  1 
ATOM   52   O  OE1 . GLU A 1 11  ? 17.078  -19.478 -40.333 1.00 71.47 ? 11  GLU A OE1 1 
ATOM   53   O  OE2 . GLU A 1 11  ? 18.488  -21.156 -40.675 1.00 74.58 ? 11  GLU A OE2 1 
ATOM   54   N  N   . HIS A 1 12  ? 19.969  -17.858 -37.180 1.00 32.54 ? 12  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 12  ? 20.605  -18.722 -36.193 1.00 32.01 ? 12  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 12  ? 20.543  -18.215 -34.777 1.00 30.28 ? 12  HIS A C   1 
ATOM   57   O  O   . HIS A 1 12  ? 21.374  -18.597 -33.925 1.00 23.47 ? 12  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 12  ? 22.055  -18.991 -36.582 1.00 36.07 ? 12  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 12  ? 22.216  -19.574 -37.966 1.00 40.15 ? 12  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 12  ? 22.766  -18.884 -38.982 1.00 40.98 ? 12  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 12  ? 21.877  -20.825 -38.478 1.00 39.62 ? 12  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 12  ? 22.779  -19.651 -40.088 1.00 42.03 ? 12  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 12  ? 22.235  -20.839 -39.778 1.00 40.90 ? 12  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 13  ? 19.566  -17.361 -34.498 1.00 26.94 ? 13  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 13  ? 19.319  -16.816 -33.089 1.00 24.43 ? 13  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 13  ? 17.855  -16.494 -32.846 1.00 24.55 ? 13  ASN A C   1 
ATOM   67   O  O   . ASN A 1 13  ? 17.519  -16.064 -31.726 1.00 21.52 ? 13  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 13  ? 20.262  -15.654 -32.664 1.00 22.02 ? 13  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 13  ? 19.966  -14.315 -33.316 1.00 22.58 ? 13  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 13  ? 19.086  -14.240 -34.170 1.00 23.38 ? 13  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 13  ? 20.658  -13.265 -32.904 1.00 23.28 ? 13  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 14  ? 17.029  -16.767 -33.846 1.00 23.76 ? 14  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 14  ? 15.610  -16.350 -33.901 1.00 23.14 ? 14  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 14  ? 14.715  -17.283 -33.124 1.00 24.18 ? 14  GLY A C   1 
ATOM   75   O  O   . GLY A 1 14  ? 15.156  -18.265 -32.506 1.00 23.97 ? 14  GLY A O   1 
ATOM   76   N  N   . PRO A 1 15  ? 13.407  -17.027 -33.119 1.00 21.61 ? 15  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 15  ? 12.427  -17.741 -32.293 1.00 21.55 ? 15  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 15  ? 12.468  -19.252 -32.234 1.00 23.40 ? 15  PRO A C   1 
ATOM   79   O  O   . PRO A 1 15  ? 12.269  -19.809 -31.153 1.00 24.91 ? 15  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 15  ? 11.068  -17.269 -32.877 1.00 20.14 ? 15  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 15  ? 11.444  -15.849 -33.263 1.00 18.88 ? 15  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 15  ? 12.806  -15.839 -33.829 1.00 19.75 ? 15  PRO A CD  1 
ATOM   83   N  N   . ILE A 1 16  ? 12.719  -19.904 -33.381 1.00 26.23 ? 16  ILE A N   1 
ATOM   84   C  CA  . ILE A 1 16  ? 12.839  -21.368 -33.408 1.00 27.16 ? 16  ILE A CA  1 
ATOM   85   C  C   . ILE A 1 16  ? 14.008  -21.861 -32.540 1.00 26.34 ? 16  ILE A C   1 
ATOM   86   O  O   . ILE A 1 16  ? 13.977  -23.012 -32.053 1.00 30.95 ? 16  ILE A O   1 
ATOM   87   C  CB  . ILE A 1 16  ? 12.949  -21.844 -34.876 1.00 33.53 ? 16  ILE A CB  1 
ATOM   88   C  CG1 . ILE A 1 16  ? 12.394  -23.268 -34.997 1.00 40.03 ? 16  ILE A CG1 1 
ATOM   89   C  CG2 . ILE A 1 16  ? 14.347  -21.573 -35.420 1.00 30.58 ? 16  ILE A CG2 1 
ATOM   90   C  CD1 . ILE A 1 16  ? 10.881  -23.367 -34.792 1.00 43.36 ? 16  ILE A CD1 1 
ATOM   91   N  N   . HIS A 1 17  ? 15.004  -21.040 -32.267 1.00 28.05 ? 17  HIS A N   1 
ATOM   92   C  CA  . HIS A 1 17  ? 16.129  -21.445 -31.425 1.00 26.37 ? 17  HIS A CA  1 
ATOM   93   C  C   . HIS A 1 17  ? 16.027  -21.052 -29.973 1.00 25.86 ? 17  HIS A C   1 
ATOM   94   O  O   . HIS A 1 17  ? 16.947  -21.352 -29.183 1.00 25.49 ? 17  HIS A O   1 
ATOM   95   C  CB  . HIS A 1 17  ? 17.433  -20.853 -31.990 1.00 29.68 ? 17  HIS A CB  1 
ATOM   96   C  CG  . HIS A 1 17  ? 17.759  -21.400 -33.347 1.00 40.01 ? 17  HIS A CG  1 
ATOM   97   N  ND1 . HIS A 1 17  ? 18.245  -22.650 -33.522 1.00 38.86 ? 17  HIS A ND1 1 
ATOM   98   C  CD2 . HIS A 1 17  ? 17.535  -20.875 -34.625 1.00 42.12 ? 17  HIS A CD2 1 
ATOM   99   C  CE1 . HIS A 1 17  ? 18.342  -22.906 -34.851 1.00 45.14 ? 17  HIS A CE1 1 
ATOM   100  N  NE2 . HIS A 1 17  ? 17.918  -21.818 -35.523 1.00 43.88 ? 17  HIS A NE2 1 
ATOM   101  N  N   . TRP A 1 18  ? 14.987  -20.256 -29.592 1.00 20.57 ? 18  TRP A N   1 
ATOM   102  C  CA  . TRP A 1 18  ? 15.029  -19.734 -28.258 1.00 21.23 ? 18  TRP A CA  1 
ATOM   103  C  C   . TRP A 1 18  ? 14.925  -20.834 -27.230 1.00 21.89 ? 18  TRP A C   1 
ATOM   104  O  O   . TRP A 1 18  ? 15.496  -20.646 -26.202 1.00 21.96 ? 18  TRP A O   1 
ATOM   105  C  CB  . TRP A 1 18  ? 13.869  -18.730 -28.097 1.00 18.83 ? 18  TRP A CB  1 
ATOM   106  C  CG  . TRP A 1 18  ? 14.073  -17.463 -28.861 1.00 17.03 ? 18  TRP A CG  1 
ATOM   107  C  CD1 . TRP A 1 18  ? 15.167  -17.001 -29.597 1.00 19.09 ? 18  TRP A CD1 1 
ATOM   108  C  CD2 . TRP A 1 18  ? 13.024  -16.421 -29.029 1.00 16.20 ? 18  TRP A CD2 1 
ATOM   109  N  NE1 . TRP A 1 18  ? 14.904  -15.778 -30.189 1.00 17.39 ? 18  TRP A NE1 1 
ATOM   110  C  CE2 . TRP A 1 18  ? 13.646  -15.367 -29.829 1.00 13.75 ? 18  TRP A CE2 1 
ATOM   111  C  CE3 . TRP A 1 18  ? 11.712  -16.251 -28.549 1.00 14.95 ? 18  TRP A CE3 1 
ATOM   112  C  CZ2 . TRP A 1 18  ? 12.954  -14.182 -30.203 1.00 14.39 ? 18  TRP A CZ2 1 
ATOM   113  C  CZ3 . TRP A 1 18  ? 11.035  -15.080 -28.964 1.00 13.53 ? 18  TRP A CZ3 1 
ATOM   114  C  CH2 . TRP A 1 18  ? 11.656  -14.099 -29.723 1.00 12.49 ? 18  TRP A CH2 1 
ATOM   115  N  N   . LYS A 1 19  ? 14.198  -21.910 -27.536 1.00 24.03 ? 19  LYS A N   1 
ATOM   116  C  CA  . LYS A 1 19  ? 14.055  -23.085 -26.590 1.00 26.60 ? 19  LYS A CA  1 
ATOM   117  C  C   . LYS A 1 19  ? 15.427  -23.631 -26.125 1.00 30.38 ? 19  LYS A C   1 
ATOM   118  O  O   . LYS A 1 19  ? 15.548  -24.184 -25.013 1.00 28.35 ? 19  LYS A O   1 
ATOM   119  C  CB  . LYS A 1 19  ? 13.226  -24.217 -27.204 1.00 29.31 ? 19  LYS A CB  1 
ATOM   120  C  CG  . LYS A 1 19  ? 13.835  -24.795 -28.519 1.00 29.59 ? 19  LYS A CG  1 
ATOM   121  C  CD  . LYS A 1 19  ? 13.039  -25.915 -29.201 1.00 36.31 ? 19  LYS A CD  1 
ATOM   122  C  CE  . LYS A 1 19  ? 11.696  -25.535 -29.870 1.00 39.97 ? 19  LYS A CE  1 
ATOM   123  N  NZ  . LYS A 1 19  ? 11.675  -24.627 -31.091 1.00 39.34 ? 19  LYS A NZ  1 
ATOM   124  N  N   . GLU A 1 20  ? 16.451  -23.433 -26.936 1.00 27.47 ? 20  GLU A N   1 
ATOM   125  C  CA  . GLU A 1 20  ? 17.832  -23.871 -26.590 1.00 27.92 ? 20  GLU A CA  1 
ATOM   126  C  C   . GLU A 1 20  ? 18.419  -23.256 -25.340 1.00 32.47 ? 20  GLU A C   1 
ATOM   127  O  O   . GLU A 1 20  ? 19.256  -23.858 -24.614 1.00 33.49 ? 20  GLU A O   1 
ATOM   128  C  CB  . GLU A 1 20  ? 18.798  -23.606 -27.758 1.00 26.54 ? 20  GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 20  ? 18.463  -24.440 -28.935 1.00 30.29 ? 20  GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 20  ? 19.199  -24.029 -30.213 1.00 33.13 ? 20  GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 20  ? 20.351  -23.507 -30.127 1.00 38.81 ? 20  GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 20  ? 18.576  -24.256 -31.299 1.00 31.98 ? 20  GLU A OE2 1 
ATOM   133  N  N   . PHE A 1 21  ? 18.031  -22.046 -25.057 1.00 29.82 ? 21  PHE A N   1 
ATOM   134  C  CA  . PHE A 1 21  ? 18.530  -21.371 -23.893 1.00 30.34 ? 21  PHE A CA  1 
ATOM   135  C  C   . PHE A 1 21  ? 17.409  -21.016 -22.903 1.00 25.79 ? 21  PHE A C   1 
ATOM   136  O  O   . PHE A 1 21  ? 17.699  -20.611 -21.788 1.00 28.69 ? 21  PHE A O   1 
ATOM   137  C  CB  . PHE A 1 21  ? 19.269  -20.129 -24.340 1.00 38.19 ? 21  PHE A CB  1 
ATOM   138  C  CG  . PHE A 1 21  ? 20.255  -20.390 -25.450 1.00 49.42 ? 21  PHE A CG  1 
ATOM   139  C  CD1 . PHE A 1 21  ? 19.938  -20.065 -26.788 1.00 53.76 ? 21  PHE A CD1 1 
ATOM   140  C  CD2 . PHE A 1 21  ? 21.500  -20.972 -25.176 1.00 49.78 ? 21  PHE A CD2 1 
ATOM   141  C  CE1 . PHE A 1 21  ? 20.857  -20.304 -27.813 1.00 54.49 ? 21  PHE A CE1 1 
ATOM   142  C  CE2 . PHE A 1 21  ? 22.423  -21.210 -26.196 1.00 48.94 ? 21  PHE A CE2 1 
ATOM   143  C  CZ  . PHE A 1 21  ? 22.103  -20.877 -27.508 1.00 54.65 ? 21  PHE A CZ  1 
ATOM   144  N  N   . PHE A 1 22  ? 16.171  -21.133 -23.368 1.00 26.07 ? 22  PHE A N   1 
ATOM   145  C  CA  . PHE A 1 22  ? 14.943  -20.758 -22.611 1.00 27.66 ? 22  PHE A CA  1 
ATOM   146  C  C   . PHE A 1 22  ? 13.891  -21.852 -22.857 1.00 29.09 ? 22  PHE A C   1 
ATOM   147  O  O   . PHE A 1 22  ? 13.012  -21.710 -23.701 1.00 25.91 ? 22  PHE A O   1 
ATOM   148  C  CB  . PHE A 1 22  ? 14.431  -19.369 -23.135 1.00 25.23 ? 22  PHE A CB  1 
ATOM   149  C  CG  . PHE A 1 22  ? 15.460  -18.306 -23.040 1.00 23.18 ? 22  PHE A CG  1 
ATOM   150  C  CD1 . PHE A 1 22  ? 15.724  -17.727 -21.850 1.00 23.38 ? 22  PHE A CD1 1 
ATOM   151  C  CD2 . PHE A 1 22  ? 16.240  -17.969 -24.135 1.00 27.33 ? 22  PHE A CD2 1 
ATOM   152  C  CE1 . PHE A 1 22  ? 16.747  -16.761 -21.726 1.00 23.76 ? 22  PHE A CE1 1 
ATOM   153  C  CE2 . PHE A 1 22  ? 17.268  -17.021 -24.036 1.00 25.22 ? 22  PHE A CE2 1 
ATOM   154  C  CZ  . PHE A 1 22  ? 17.544  -16.416 -22.820 1.00 26.20 ? 22  PHE A CZ  1 
ATOM   155  N  N   . PRO A 1 23  ? 13.956  -23.013 -22.147 1.00 28.19 ? 23  PRO A N   1 
ATOM   156  C  CA  . PRO A 1 23  ? 13.029  -24.055 -22.560 1.00 27.52 ? 23  PRO A CA  1 
ATOM   157  C  C   . PRO A 1 23  ? 11.585  -23.781 -22.183 1.00 23.90 ? 23  PRO A C   1 
ATOM   158  O  O   . PRO A 1 23  ? 10.725  -24.453 -22.746 1.00 28.96 ? 23  PRO A O   1 
ATOM   159  C  CB  . PRO A 1 23  ? 13.545  -25.316 -21.825 1.00 30.95 ? 23  PRO A CB  1 
ATOM   160  C  CG  . PRO A 1 23  ? 14.217  -24.756 -20.609 1.00 32.84 ? 23  PRO A CG  1 
ATOM   161  C  CD  . PRO A 1 23  ? 14.785  -23.406 -20.994 1.00 35.37 ? 23  PRO A CD  1 
ATOM   162  N  N   . ILE A 1 24  ? 11.359  -22.727 -21.346 1.00 25.15 ? 24  ILE A N   1 
ATOM   163  C  CA  . ILE A 1 24  ? 9.976   -22.310 -21.096 1.00 25.42 ? 24  ILE A CA  1 
ATOM   164  C  C   . ILE A 1 24  ? 9.340   -21.874 -22.451 1.00 21.44 ? 24  ILE A C   1 
ATOM   165  O  O   . ILE A 1 24  ? 8.140   -21.769 -22.534 1.00 21.14 ? 24  ILE A O   1 
ATOM   166  C  CB  . ILE A 1 24  ? 9.822   -21.239 -19.987 1.00 22.35 ? 24  ILE A CB  1 
ATOM   167  C  CG1 . ILE A 1 24  ? 8.358   -21.192 -19.458 1.00 21.44 ? 24  ILE A CG1 1 
ATOM   168  C  CG2 . ILE A 1 24  ? 10.219  -19.877 -20.543 1.00 20.42 ? 24  ILE A CG2 1 
ATOM   169  C  CD1 . ILE A 1 24  ? 7.916   -22.469 -18.687 1.00 23.30 ? 24  ILE A CD1 1 
ATOM   170  N  N   . ALA A 1 25  ? 10.176  -21.687 -23.502 1.00 22.45 ? 25  ALA A N   1 
ATOM   171  C  CA  . ALA A 1 25  ? 9.627   -21.393 -24.841 1.00 23.07 ? 25  ALA A CA  1 
ATOM   172  C  C   . ALA A 1 25  ? 8.560   -22.384 -25.305 1.00 21.96 ? 25  ALA A C   1 
ATOM   173  O  O   . ALA A 1 25  ? 7.675   -22.062 -26.091 1.00 22.27 ? 25  ALA A O   1 
ATOM   174  C  CB  . ALA A 1 25  ? 10.766  -21.412 -25.862 1.00 22.85 ? 25  ALA A CB  1 
ATOM   175  N  N   . ASP A 1 26  ? 8.665   -23.681 -24.877 1.00 20.56 ? 26  ASP A N   1 
ATOM   176  C  CA  . ASP A 1 26  ? 7.619   -24.662 -25.193 1.00 24.60 ? 26  ASP A CA  1 
ATOM   177  C  C   . ASP A 1 26  ? 6.653   -24.946 -24.034 1.00 24.88 ? 26  ASP A C   1 
ATOM   178  O  O   . ASP A 1 26  ? 6.041   -26.037 -23.950 1.00 26.34 ? 26  ASP A O   1 
ATOM   179  C  CB  . ASP A 1 26  ? 8.302   -26.003 -25.623 1.00 30.34 ? 26  ASP A CB  1 
ATOM   180  C  CG  . ASP A 1 26  ? 9.274   -25.801 -26.770 1.00 33.46 ? 26  ASP A CG  1 
ATOM   181  O  OD1 . ASP A 1 26  ? 8.819   -25.288 -27.806 1.00 38.66 ? 26  ASP A OD1 1 
ATOM   182  O  OD2 . ASP A 1 26  ? 10.464  -26.095 -26.628 1.00 38.65 ? 26  ASP A OD2 1 
ATOM   183  N  N   . GLY A 1 27  ? 6.528   -23.967 -23.105 1.00 23.75 ? 27  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 27  ? 5.611   -24.021 -21.985 1.00 19.98 ? 27  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 27  ? 4.124   -24.052 -22.276 1.00 22.72 ? 27  GLY A C   1 
ATOM   186  O  O   . GLY A 1 27  ? 3.659   -24.060 -23.422 1.00 22.37 ? 27  GLY A O   1 
ATOM   187  N  N   . ASP A 1 28  ? 3.348   -24.009 -21.221 1.00 21.79 ? 28  ASP A N   1 
ATOM   188  C  CA  . ASP A 1 28  ? 1.948   -24.119 -21.386 1.00 20.53 ? 28  ASP A CA  1 
ATOM   189  C  C   . ASP A 1 28  ? 1.256   -22.791 -21.391 1.00 16.89 ? 28  ASP A C   1 
ATOM   190  O  O   . ASP A 1 28  ? 0.064   -22.736 -21.658 1.00 21.20 ? 28  ASP A O   1 
ATOM   191  C  CB  . ASP A 1 28  ? 1.366   -24.974 -20.250 1.00 23.86 ? 28  ASP A CB  1 
ATOM   192  C  CG  . ASP A 1 28  ? 1.680   -26.509 -20.449 1.00 26.51 ? 28  ASP A CG  1 
ATOM   193  O  OD1 . ASP A 1 28  ? 1.936   -26.947 -21.601 1.00 29.58 ? 28  ASP A OD1 1 
ATOM   194  O  OD2 . ASP A 1 28  ? 1.727   -27.201 -19.410 1.00 31.58 ? 28  ASP A OD2 1 
ATOM   195  N  N   . GLN A 1 29  ? 1.983   -21.676 -21.073 1.00 15.55 ? 29  GLN A N   1 
ATOM   196  C  CA  . GLN A 1 29  ? 1.297   -20.395 -21.053 1.00 16.45 ? 29  GLN A CA  1 
ATOM   197  C  C   . GLN A 1 29  ? 2.118   -19.385 -21.835 1.00 15.95 ? 29  GLN A C   1 
ATOM   198  O  O   . GLN A 1 29  ? 2.417   -18.285 -21.367 1.00 16.28 ? 29  GLN A O   1 
ATOM   199  C  CB  . GLN A 1 29  ? 0.982   -19.863 -19.640 1.00 17.24 ? 29  GLN A CB  1 
ATOM   200  C  CG  . GLN A 1 29  ? 0.033   -20.814 -18.955 1.00 22.91 ? 29  GLN A CG  1 
ATOM   201  C  CD  . GLN A 1 29  ? -0.876  -20.180 -17.884 1.00 26.90 ? 29  GLN A CD  1 
ATOM   202  O  OE1 . GLN A 1 29  ? -2.000  -20.718 -17.627 1.00 32.07 ? 29  GLN A OE1 1 
ATOM   203  N  NE2 . GLN A 1 29  ? -0.444  -19.065 -17.272 1.00 19.32 ? 29  GLN A NE2 1 
ATOM   204  N  N   . GLN A 1 30  ? 2.404   -19.733 -23.104 1.00 16.35 ? 30  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 30  ? 3.329   -18.906 -23.908 1.00 14.56 ? 30  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 30  ? 2.517   -18.008 -24.776 1.00 15.38 ? 30  GLN A C   1 
ATOM   207  O  O   . GLN A 1 30  ? 1.379   -18.303 -25.105 1.00 15.63 ? 30  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 30  ? 4.221   -19.780 -24.775 1.00 14.88 ? 30  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 30  ? 5.321   -20.466 -23.956 1.00 16.35 ? 30  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 30  ? 6.306   -19.418 -23.478 1.00 16.42 ? 30  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 30  ? 7.066   -18.869 -24.222 1.00 13.90 ? 30  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 30  ? 6.304   -19.154 -22.145 1.00 15.00 ? 30  GLN A NE2 1 
ATOM   213  N  N   . SER A 1 31  ? 3.090   -16.843 -25.112 1.00 14.47 ? 31  SER A N   1 
ATOM   214  C  CA  . SER A 1 31  ? 2.503   -15.875 -25.979 1.00 14.05 ? 31  SER A CA  1 
ATOM   215  C  C   . SER A 1 31  ? 3.451   -15.538 -27.109 1.00 12.70 ? 31  SER A C   1 
ATOM   216  O  O   . SER A 1 31  ? 4.640   -15.781 -27.067 1.00 12.93 ? 31  SER A O   1 
ATOM   217  C  CB  . SER A 1 31  ? 2.323   -14.579 -25.112 1.00 12.75 ? 31  SER A CB  1 
ATOM   218  O  OG  . SER A 1 31  ? 1.304   -14.799 -24.158 1.00 11.88 ? 31  SER A OG  1 
ATOM   219  N  N   . PRO A 1 32  ? 2.908   -15.004 -28.211 1.00 12.32 ? 32  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 32  ? 1.548   -14.642 -28.444 1.00 12.55 ? 32  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 32  ? 0.742   -15.883 -28.880 1.00 14.25 ? 32  PRO A C   1 
ATOM   222  O  O   . PRO A 1 32  ? 1.242   -17.010 -28.794 1.00 14.84 ? 32  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 32  ? 1.713   -13.604 -29.606 1.00 12.70 ? 32  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 32  ? 2.801   -14.234 -30.425 1.00 12.27 ? 32  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 32  ? 3.812   -14.721 -29.384 1.00 13.87 ? 32  PRO A CD  1 
ATOM   226  N  N   . ILE A 1 33  ? -0.534  -15.623 -29.216 1.00 13.12 ? 33  ILE A N   1 
ATOM   227  C  CA  . ILE A 1 33  ? -1.468  -16.774 -29.484 1.00 14.92 ? 33  ILE A CA  1 
ATOM   228  C  C   . ILE A 1 33  ? -2.327  -16.376 -30.682 1.00 17.64 ? 33  ILE A C   1 
ATOM   229  O  O   . ILE A 1 33  ? -2.338  -15.239 -31.125 1.00 14.43 ? 33  ILE A O   1 
ATOM   230  C  CB  . ILE A 1 33  ? -2.411  -17.119 -28.280 1.00 15.85 ? 33  ILE A CB  1 
ATOM   231  C  CG1 . ILE A 1 33  ? -3.333  -15.937 -27.939 1.00 13.93 ? 33  ILE A CG1 1 
ATOM   232  C  CG2 . ILE A 1 33  ? -1.579  -17.736 -27.148 1.00 15.85 ? 33  ILE A CG2 1 
ATOM   233  C  CD1 . ILE A 1 33  ? -4.516  -16.313 -27.138 1.00 16.20 ? 33  ILE A CD1 1 
ATOM   234  N  N   . GLU A 1 34  ? -3.003  -17.384 -31.256 1.00 16.98 ? 34  GLU A N   1 
ATOM   235  C  CA  . GLU A 1 34  ? -4.160  -17.133 -32.134 1.00 17.42 ? 34  GLU A CA  1 
ATOM   236  C  C   . GLU A 1 34  ? -5.441  -17.096 -31.355 1.00 15.73 ? 34  GLU A C   1 
ATOM   237  O  O   . GLU A 1 34  ? -5.661  -17.909 -30.507 1.00 19.22 ? 34  GLU A O   1 
ATOM   238  C  CB  . GLU A 1 34  ? -4.235  -18.353 -33.110 1.00 19.24 ? 34  GLU A CB  1 
ATOM   239  C  CG  . GLU A 1 34  ? -3.133  -18.379 -34.135 1.00 20.32 ? 34  GLU A CG  1 
ATOM   240  C  CD  . GLU A 1 34  ? -3.420  -19.497 -35.205 1.00 23.53 ? 34  GLU A CD  1 
ATOM   241  O  OE1 . GLU A 1 34  ? -4.043  -19.143 -36.230 1.00 27.20 ? 34  GLU A OE1 1 
ATOM   242  O  OE2 . GLU A 1 34  ? -3.092  -20.658 -34.975 1.00 21.46 ? 34  GLU A OE2 1 
ATOM   243  N  N   . ILE A 1 35  ? -6.245  -16.088 -31.646 1.00 17.64 ? 35  ILE A N   1 
ATOM   244  C  CA  . ILE A 1 35  ? -7.546  -15.883 -31.007 1.00 20.45 ? 35  ILE A CA  1 
ATOM   245  C  C   . ILE A 1 35  ? -8.587  -16.351 -32.060 1.00 20.32 ? 35  ILE A C   1 
ATOM   246  O  O   . ILE A 1 35  ? -8.696  -15.727 -33.079 1.00 19.75 ? 35  ILE A O   1 
ATOM   247  C  CB  . ILE A 1 35  ? -7.720  -14.400 -30.592 1.00 19.00 ? 35  ILE A CB  1 
ATOM   248  C  CG1 . ILE A 1 35  ? -6.528  -13.981 -29.658 1.00 18.96 ? 35  ILE A CG1 1 
ATOM   249  C  CG2 . ILE A 1 35  ? -9.125  -14.201 -30.032 1.00 23.27 ? 35  ILE A CG2 1 
ATOM   250  C  CD1 . ILE A 1 35  ? -6.602  -12.526 -29.275 1.00 21.61 ? 35  ILE A CD1 1 
ATOM   251  N  N   . LYS A 1 36  ? -9.325  -17.398 -31.695 1.00 21.32 ? 36  LYS A N   1 
ATOM   252  C  CA  . LYS A 1 36  ? -10.422 -17.961 -32.522 1.00 23.55 ? 36  LYS A CA  1 
ATOM   253  C  C   . LYS A 1 36  ? -11.708 -17.387 -31.875 1.00 22.11 ? 36  LYS A C   1 
ATOM   254  O  O   . LYS A 1 36  ? -12.149 -17.879 -30.809 1.00 26.25 ? 36  LYS A O   1 
ATOM   255  C  CB  . LYS A 1 36  ? -10.361 -19.515 -32.443 1.00 26.43 ? 36  LYS A CB  1 
ATOM   256  C  CG  . LYS A 1 36  ? -11.541 -20.261 -33.137 1.00 27.54 ? 36  LYS A CG  1 
ATOM   257  C  CD  . LYS A 1 36  ? -11.265 -21.752 -33.299 1.00 33.56 ? 36  LYS A CD  1 
ATOM   258  C  CE  . LYS A 1 36  ? -10.271 -22.081 -34.451 1.00 32.10 ? 36  LYS A CE  1 
ATOM   259  N  NZ  . LYS A 1 36  ? -10.186 -23.579 -34.734 1.00 26.20 ? 36  LYS A NZ  1 
ATOM   260  N  N   . THR A 1 37  ? -12.275 -16.321 -32.452 1.00 22.80 ? 37  THR A N   1 
ATOM   261  C  CA  . THR A 1 37  ? -13.405 -15.597 -31.810 1.00 28.47 ? 37  THR A CA  1 
ATOM   262  C  C   . THR A 1 37  ? -14.650 -16.494 -31.517 1.00 27.17 ? 37  THR A C   1 
ATOM   263  O  O   . THR A 1 37  ? -15.350 -16.291 -30.488 1.00 27.74 ? 37  THR A O   1 
ATOM   264  C  CB  . THR A 1 37  ? -13.784 -14.295 -32.535 1.00 29.30 ? 37  THR A CB  1 
ATOM   265  O  OG1 . THR A 1 37  ? -14.170 -14.575 -33.885 1.00 26.89 ? 37  THR A OG1 1 
ATOM   266  C  CG2 . THR A 1 37  ? -12.592 -13.326 -32.569 1.00 26.91 ? 37  THR A CG2 1 
ATOM   267  N  N   . LYS A 1 38  ? -14.856 -17.504 -32.371 1.00 29.63 ? 38  LYS A N   1 
ATOM   268  C  CA  . LYS A 1 38  ? -16.012 -18.416 -32.269 1.00 32.58 ? 38  LYS A CA  1 
ATOM   269  C  C   . LYS A 1 38  ? -15.984 -19.092 -30.905 1.00 35.67 ? 38  LYS A C   1 
ATOM   270  O  O   . LYS A 1 38  ? -17.025 -19.301 -30.296 1.00 33.85 ? 38  LYS A O   1 
ATOM   271  C  CB  . LYS A 1 38  ? -16.024 -19.499 -33.404 1.00 39.06 ? 38  LYS A CB  1 
ATOM   272  N  N   . GLU A 1 39  ? -14.774 -19.356 -30.419 1.00 33.82 ? 39  GLU A N   1 
ATOM   273  C  CA  . GLU A 1 39  ? -14.572 -20.007 -29.157 1.00 35.64 ? 39  GLU A CA  1 
ATOM   274  C  C   . GLU A 1 39  ? -14.487 -19.098 -27.913 1.00 36.03 ? 39  GLU A C   1 
ATOM   275  O  O   . GLU A 1 39  ? -14.702 -19.563 -26.807 1.00 44.44 ? 39  GLU A O   1 
ATOM   276  C  CB  . GLU A 1 39  ? -13.344 -20.918 -29.293 1.00 40.07 ? 39  GLU A CB  1 
ATOM   277  C  CG  . GLU A 1 39  ? -13.619 -22.074 -30.244 1.00 49.40 ? 39  GLU A CG  1 
ATOM   278  C  CD  . GLU A 1 39  ? -12.574 -23.173 -30.164 1.00 56.75 ? 39  GLU A CD  1 
ATOM   279  O  OE1 . GLU A 1 39  ? -11.362 -22.852 -30.150 1.00 63.32 ? 39  GLU A OE1 1 
ATOM   280  O  OE2 . GLU A 1 39  ? -12.971 -24.365 -30.128 1.00 60.93 ? 39  GLU A OE2 1 
ATOM   281  N  N   . VAL A 1 40  ? -14.268 -17.800 -28.104 1.00 30.66 ? 40  VAL A N   1 
ATOM   282  C  CA  . VAL A 1 40  ? -14.174 -16.815 -27.010 1.00 31.32 ? 40  VAL A CA  1 
ATOM   283  C  C   . VAL A 1 40  ? -15.505 -16.539 -26.284 1.00 33.29 ? 40  VAL A C   1 
ATOM   284  O  O   . VAL A 1 40  ? -16.518 -16.289 -26.932 1.00 36.93 ? 40  VAL A O   1 
ATOM   285  C  CB  . VAL A 1 40  ? -13.647 -15.484 -27.627 1.00 27.46 ? 40  VAL A CB  1 
ATOM   286  C  CG1 . VAL A 1 40  ? -13.605 -14.396 -26.608 1.00 27.95 ? 40  VAL A CG1 1 
ATOM   287  C  CG2 . VAL A 1 40  ? -12.249 -15.692 -28.201 1.00 27.23 ? 40  VAL A CG2 1 
ATOM   288  N  N   . LYS A 1 41  ? -15.520 -16.508 -24.953 1.00 36.04 ? 41  LYS A N   1 
ATOM   289  C  CA  . LYS A 1 41  ? -16.766 -16.156 -24.228 1.00 38.77 ? 41  LYS A CA  1 
ATOM   290  C  C   . LYS A 1 41  ? -16.670 -14.748 -23.685 1.00 34.72 ? 41  LYS A C   1 
ATOM   291  O  O   . LYS A 1 41  ? -15.628 -14.423 -23.083 1.00 30.74 ? 41  LYS A O   1 
ATOM   292  C  CB  . LYS A 1 41  ? -16.990 -17.098 -23.011 1.00 41.48 ? 41  LYS A CB  1 
ATOM   293  C  CG  . LYS A 1 41  ? -16.880 -18.604 -23.223 1.00 50.47 ? 41  LYS A CG  1 
ATOM   294  N  N   . TYR A 1 42  ? -17.711 -13.932 -23.889 1.00 27.52 ? 42  TYR A N   1 
ATOM   295  C  CA  . TYR A 1 42  ? -17.917 -12.688 -23.144 1.00 30.28 ? 42  TYR A CA  1 
ATOM   296  C  C   . TYR A 1 42  ? -17.955 -13.009 -21.651 1.00 29.69 ? 42  TYR A C   1 
ATOM   297  O  O   . TYR A 1 42  ? -18.595 -13.960 -21.218 1.00 31.53 ? 42  TYR A O   1 
ATOM   298  C  CB  . TYR A 1 42  ? -19.228 -11.950 -23.576 1.00 27.89 ? 42  TYR A CB  1 
ATOM   299  C  CG  . TYR A 1 42  ? -19.680 -10.840 -22.649 1.00 31.55 ? 42  TYR A CG  1 
ATOM   300  C  CD1 . TYR A 1 42  ? -19.000 -9.648  -22.597 1.00 29.60 ? 42  TYR A CD1 1 
ATOM   301  C  CD2 . TYR A 1 42  ? -20.798 -10.994 -21.805 1.00 30.82 ? 42  TYR A CD2 1 
ATOM   302  C  CE1 . TYR A 1 42  ? -19.375 -8.631  -21.719 1.00 34.16 ? 42  TYR A CE1 1 
ATOM   303  C  CE2 . TYR A 1 42  ? -21.187 -9.982  -20.943 1.00 36.34 ? 42  TYR A CE2 1 
ATOM   304  C  CZ  . TYR A 1 42  ? -20.486 -8.809  -20.899 1.00 34.81 ? 42  TYR A CZ  1 
ATOM   305  O  OH  . TYR A 1 42  ? -20.879 -7.800  -20.031 1.00 40.98 ? 42  TYR A OH  1 
ATOM   306  N  N   . ASP A 1 43  ? -17.327 -12.156 -20.843 1.00 27.97 ? 43  ASP A N   1 
ATOM   307  C  CA  . ASP A 1 43  ? -17.361 -12.348 -19.386 1.00 25.03 ? 43  ASP A CA  1 
ATOM   308  C  C   . ASP A 1 43  ? -17.811 -11.044 -18.732 1.00 30.47 ? 43  ASP A C   1 
ATOM   309  O  O   . ASP A 1 43  ? -17.058 -10.087 -18.680 1.00 27.60 ? 43  ASP A O   1 
ATOM   310  C  CB  . ASP A 1 43  ? -15.928 -12.674 -18.892 1.00 31.83 ? 43  ASP A CB  1 
ATOM   311  C  CG  . ASP A 1 43  ? -15.877 -12.922 -17.374 1.00 33.99 ? 43  ASP A CG  1 
ATOM   312  O  OD1 . ASP A 1 43  ? -16.826 -12.493 -16.680 1.00 31.59 ? 43  ASP A OD1 1 
ATOM   313  O  OD2 . ASP A 1 43  ? -14.874 -13.488 -16.884 1.00 34.06 ? 43  ASP A OD2 1 
ATOM   314  N  N   . SER A 1 44  ? -19.050 -11.016 -18.221 1.00 26.12 ? 44  SER A N   1 
ATOM   315  C  CA  . SER A 1 44  ? -19.662 -9.815  -17.617 1.00 27.41 ? 44  SER A CA  1 
ATOM   316  C  C   . SER A 1 44  ? -19.013 -9.389  -16.303 1.00 28.24 ? 44  SER A C   1 
ATOM   317  O  O   . SER A 1 44  ? -19.279 -8.248  -15.822 1.00 31.91 ? 44  SER A O   1 
ATOM   318  C  CB  . SER A 1 44  ? -21.170 -10.113 -17.378 1.00 29.16 ? 44  SER A CB  1 
ATOM   319  O  OG  . SER A 1 44  ? -21.265 -11.367 -16.759 1.00 34.55 ? 44  SER A OG  1 
ATOM   320  N  N   . SER A 1 45  ? -18.169 -10.289 -15.730 1.00 30.07 ? 45  SER A N   1 
ATOM   321  C  CA  . SER A 1 45  ? -17.423 -9.970  -14.476 1.00 29.38 ? 45  SER A CA  1 
ATOM   322  C  C   . SER A 1 45  ? -16.180 -9.077  -14.675 1.00 27.87 ? 45  SER A C   1 
ATOM   323  O  O   . SER A 1 45  ? -15.649 -8.512  -13.688 1.00 34.44 ? 45  SER A O   1 
ATOM   324  C  CB  . SER A 1 45  ? -17.032 -11.234 -13.654 1.00 33.24 ? 45  SER A CB  1 
ATOM   325  O  OG  . SER A 1 45  ? -16.002 -11.962 -14.267 1.00 33.87 ? 45  SER A OG  1 
ATOM   326  N  N   . LEU A 1 46  ? -15.728 -8.919  -15.897 1.00 28.93 ? 46  LEU A N   1 
ATOM   327  C  CA  . LEU A 1 46  ? -14.672 -7.940  -16.150 1.00 28.95 ? 46  LEU A CA  1 
ATOM   328  C  C   . LEU A 1 46  ? -15.114 -6.503  -15.865 1.00 27.56 ? 46  LEU A C   1 
ATOM   329  O  O   . LEU A 1 46  ? -16.207 -6.084  -16.328 1.00 27.23 ? 46  LEU A O   1 
ATOM   330  C  CB  . LEU A 1 46  ? -14.263 -8.084  -17.605 1.00 26.12 ? 46  LEU A CB  1 
ATOM   331  C  CG  . LEU A 1 46  ? -13.578 -9.414  -17.942 1.00 25.86 ? 46  LEU A CG  1 
ATOM   332  C  CD1 . LEU A 1 46  ? -13.638 -9.578  -19.429 1.00 23.34 ? 46  LEU A CD1 1 
ATOM   333  C  CD2 . LEU A 1 46  ? -12.110 -9.558  -17.504 1.00 26.72 ? 46  LEU A CD2 1 
ATOM   334  N  N   . ARG A 1 47  ? -14.338 -5.768  -15.062 1.00 26.70 ? 47  ARG A N   1 
ATOM   335  C  CA  . ARG A 1 47  ? -14.632 -4.373  -14.787 1.00 25.36 ? 47  ARG A CA  1 
ATOM   336  C  C   . ARG A 1 47  ? -14.226 -3.393  -15.865 1.00 26.78 ? 47  ARG A C   1 
ATOM   337  O  O   . ARG A 1 47  ? -13.449 -3.713  -16.777 1.00 26.05 ? 47  ARG A O   1 
ATOM   338  C  CB  . ARG A 1 47  ? -13.974 -3.910  -13.422 1.00 33.14 ? 47  ARG A CB  1 
ATOM   339  C  CG  . ARG A 1 47  ? -14.215 -4.785  -12.173 1.00 40.31 ? 47  ARG A CG  1 
ATOM   340  N  N   . PRO A 1 48  ? -14.770 -2.175  -15.839 1.00 22.72 ? 48  PRO A N   1 
ATOM   341  C  CA  . PRO A 1 48  ? -14.354 -1.270  -16.881 1.00 25.65 ? 48  PRO A CA  1 
ATOM   342  C  C   . PRO A 1 48  ? -12.807 -1.144  -16.808 1.00 24.56 ? 48  PRO A C   1 
ATOM   343  O  O   . PRO A 1 48  ? -12.240 -1.052  -15.703 1.00 24.35 ? 48  PRO A O   1 
ATOM   344  C  CB  . PRO A 1 48  ? -15.046 0.066   -16.463 1.00 26.08 ? 48  PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 48  ? -16.306 -0.442  -15.807 1.00 25.43 ? 48  PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 48  ? -15.843 -1.604  -14.974 1.00 25.68 ? 48  PRO A CD  1 
ATOM   347  N  N   . LEU A 1 49  ? -12.191 -1.076  -17.992 1.00 26.77 ? 49  LEU A N   1 
ATOM   348  C  CA  . LEU A 1 49  ? -10.738 -0.759  -18.111 1.00 24.50 ? 49  LEU A CA  1 
ATOM   349  C  C   . LEU A 1 49  ? -10.481 0.682   -17.829 1.00 25.99 ? 49  LEU A C   1 
ATOM   350  O  O   . LEU A 1 49  ? -11.261 1.526   -18.270 1.00 26.40 ? 49  LEU A O   1 
ATOM   351  C  CB  . LEU A 1 49  ? -10.371 -1.094  -19.526 1.00 27.78 ? 49  LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 49  ? -8.960  -1.458  -19.844 1.00 30.70 ? 49  LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 49  ? -8.611  -2.748  -19.180 1.00 28.12 ? 49  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 49  ? -8.793  -1.630  -21.340 1.00 33.12 ? 49  LEU A CD2 1 
ATOM   355  N  N   . SER A 1 50  ? -9.464  1.004   -16.995 1.00 21.21 ? 50  SER A N   1 
ATOM   356  C  CA  . SER A 1 50  ? -9.245  2.351   -16.554 1.00 21.90 ? 50  SER A CA  1 
ATOM   357  C  C   . SER A 1 50  ? -7.819  2.669   -16.995 1.00 16.83 ? 50  SER A C   1 
ATOM   358  O  O   . SER A 1 50  ? -6.897  2.004   -16.555 1.00 18.97 ? 50  SER A O   1 
ATOM   359  C  CB  . SER A 1 50  ? -9.372  2.447   -14.971 1.00 21.43 ? 50  SER A CB  1 
ATOM   360  O  OG  . SER A 1 50  ? -8.699  3.569   -14.440 1.00 22.93 ? 50  SER A OG  1 
ATOM   361  N  N   . ILE A 1 51  ? -7.650  3.709   -17.821 1.00 17.99 ? 51  ILE A N   1 
ATOM   362  C  CA  . ILE A 1 51  ? -6.321  4.070   -18.209 1.00 17.21 ? 51  ILE A CA  1 
ATOM   363  C  C   . ILE A 1 51  ? -6.000  5.521   -17.855 1.00 18.56 ? 51  ILE A C   1 
ATOM   364  O  O   . ILE A 1 51  ? -6.616  6.477   -18.428 1.00 20.06 ? 51  ILE A O   1 
ATOM   365  C  CB  . ILE A 1 51  ? -6.111  3.878   -19.715 1.00 17.30 ? 51  ILE A CB  1 
ATOM   366  C  CG1 . ILE A 1 51  ? -6.479  2.431   -20.119 1.00 18.31 ? 51  ILE A CG1 1 
ATOM   367  C  CG2 . ILE A 1 51  ? -4.640  4.237   -20.085 1.00 18.21 ? 51  ILE A CG2 1 
ATOM   368  C  CD1 . ILE A 1 51  ? -6.331  2.077   -21.648 1.00 17.80 ? 51  ILE A CD1 1 
ATOM   369  N  N   . LYS A 1 52  ? -5.107  5.730   -16.866 1.00 15.31 ? 52  LYS A N   1 
ATOM   370  C  CA  . LYS A 1 52  ? -4.686  7.036   -16.505 1.00 16.19 ? 52  LYS A CA  1 
ATOM   371  C  C   . LYS A 1 52  ? -3.250  7.160   -16.893 1.00 15.95 ? 52  LYS A C   1 
ATOM   372  O  O   . LYS A 1 52  ? -2.412  6.455   -16.334 1.00 16.76 ? 52  LYS A O   1 
ATOM   373  C  CB  . LYS A 1 52  ? -4.879  7.297   -14.975 1.00 14.56 ? 52  LYS A CB  1 
ATOM   374  C  CG  . LYS A 1 52  ? -4.320  8.612   -14.496 1.00 17.37 ? 52  LYS A CG  1 
ATOM   375  C  CD  . LYS A 1 52  ? -4.672  8.931   -13.012 1.00 18.63 ? 52  LYS A CD  1 
ATOM   376  C  CE  . LYS A 1 52  ? -4.034  8.059   -11.971 1.00 20.25 ? 52  LYS A CE  1 
ATOM   377  N  NZ  . LYS A 1 52  ? -4.161  8.685   -10.598 1.00 26.24 ? 52  LYS A NZ  1 
ATOM   378  N  N   A TYR A 1 53  ? -2.956  7.982   -17.903 0.50 16.24 ? 53  TYR A N   1 
ATOM   379  N  N   B TYR A 1 53  ? -3.023  8.125   -17.794 0.50 16.23 ? 53  TYR A N   1 
ATOM   380  C  CA  A TYR A 1 53  ? -1.557  8.145   -18.335 0.50 15.46 ? 53  TYR A CA  1 
ATOM   381  C  CA  B TYR A 1 53  ? -1.741  8.328   -18.415 0.50 15.86 ? 53  TYR A CA  1 
ATOM   382  C  C   A TYR A 1 53  ? -1.190  9.633   -18.361 0.50 16.12 ? 53  TYR A C   1 
ATOM   383  C  C   B TYR A 1 53  ? -1.245  9.763   -18.305 0.50 16.13 ? 53  TYR A C   1 
ATOM   384  O  O   A TYR A 1 53  ? -1.938  10.493  -18.829 0.50 16.03 ? 53  TYR A O   1 
ATOM   385  O  O   B TYR A 1 53  ? -1.950  10.713  -18.634 0.50 14.91 ? 53  TYR A O   1 
ATOM   386  C  CB  A TYR A 1 53  ? -1.290  7.537   -19.743 0.50 13.37 ? 53  TYR A CB  1 
ATOM   387  C  CB  B TYR A 1 53  ? -1.804  7.895   -19.899 0.50 13.89 ? 53  TYR A CB  1 
ATOM   388  C  CG  A TYR A 1 53  ? -1.364  6.050   -19.931 0.50 12.39 ? 53  TYR A CG  1 
ATOM   389  C  CG  B TYR A 1 53  ? -0.500  8.231   -20.526 0.50 13.98 ? 53  TYR A CG  1 
ATOM   390  C  CD1 A TYR A 1 53  ? -1.108  5.107   -18.872 0.50 11.83 ? 53  TYR A CD1 1 
ATOM   391  C  CD1 B TYR A 1 53  ? 0.641   7.568   -20.126 0.50 14.12 ? 53  TYR A CD1 1 
ATOM   392  C  CD2 A TYR A 1 53  ? -1.584  5.544   -21.226 0.50 11.64 ? 53  TYR A CD2 1 
ATOM   393  C  CD2 B TYR A 1 53  ? -0.366  9.255   -21.475 0.50 14.29 ? 53  TYR A CD2 1 
ATOM   394  C  CE1 A TYR A 1 53  ? -1.184  3.751   -19.098 0.50 13.01 ? 53  TYR A CE1 1 
ATOM   395  C  CE1 B TYR A 1 53  ? 1.892   7.932   -20.609 0.50 14.40 ? 53  TYR A CE1 1 
ATOM   396  C  CE2 A TYR A 1 53  ? -1.633  4.165   -21.426 0.50 12.19 ? 53  TYR A CE2 1 
ATOM   397  C  CE2 B TYR A 1 53  ? 0.858   9.579   -21.974 0.50 12.18 ? 53  TYR A CE2 1 
ATOM   398  C  CZ  A TYR A 1 53  ? -1.430  3.295   -20.395 0.50 11.95 ? 53  TYR A CZ  1 
ATOM   399  C  CZ  B TYR A 1 53  ? 2.001   8.883   -21.532 0.50 12.27 ? 53  TYR A CZ  1 
ATOM   400  O  OH  A TYR A 1 53  ? -1.504  1.986   -20.622 0.50 10.79 ? 53  TYR A OH  1 
ATOM   401  O  OH  B TYR A 1 53  ? 3.235   9.221   -22.055 0.50 16.31 ? 53  TYR A OH  1 
ATOM   402  N  N   . ASP A 1 54  ? -0.032  9.915   -17.774 1.00 14.96 ? 54  ASP A N   1 
ATOM   403  C  CA  . ASP A 1 54  ? 0.557   11.224  -17.681 1.00 14.76 ? 54  ASP A CA  1 
ATOM   404  C  C   . ASP A 1 54  ? 1.685   11.318  -18.687 1.00 16.18 ? 54  ASP A C   1 
ATOM   405  O  O   . ASP A 1 54  ? 2.709   10.589  -18.549 1.00 15.72 ? 54  ASP A O   1 
ATOM   406  C  CB  . ASP A 1 54  ? 1.120   11.344  -16.240 1.00 18.66 ? 54  ASP A CB  1 
ATOM   407  C  CG  . ASP A 1 54  ? 1.480   12.765  -15.903 1.00 18.00 ? 54  ASP A CG  1 
ATOM   408  O  OD1 . ASP A 1 54  ? 2.070   13.469  -16.757 1.00 17.77 ? 54  ASP A OD1 1 
ATOM   409  O  OD2 . ASP A 1 54  ? 1.322   13.174  -14.737 1.00 24.18 ? 54  ASP A OD2 1 
ATOM   410  N  N   . PRO A 1 55  ? 1.621   12.206  -19.680 1.00 14.17 ? 55  PRO A N   1 
ATOM   411  C  CA  . PRO A 1 55  ? 2.695   12.363  -20.596 1.00 16.16 ? 55  PRO A CA  1 
ATOM   412  C  C   . PRO A 1 55  ? 4.079   12.640  -19.982 1.00 16.47 ? 55  PRO A C   1 
ATOM   413  O  O   . PRO A 1 55  ? 5.109   12.403  -20.613 1.00 18.68 ? 55  PRO A O   1 
ATOM   414  C  CB  . PRO A 1 55  ? 2.208   13.531  -21.524 1.00 16.36 ? 55  PRO A CB  1 
ATOM   415  C  CG  . PRO A 1 55  ? 0.713   13.441  -21.432 1.00 15.07 ? 55  PRO A CG  1 
ATOM   416  C  CD  . PRO A 1 55  ? 0.446   13.084  -19.983 1.00 15.19 ? 55  PRO A CD  1 
ATOM   417  N  N   . SER A 1 56  ? 4.089   13.272  -18.811 1.00 16.15 ? 56  SER A N   1 
ATOM   418  C  CA  . SER A 1 56  ? 5.384   13.570  -18.196 1.00 18.40 ? 56  SER A CA  1 
ATOM   419  C  C   . SER A 1 56  ? 6.059   12.342  -17.628 1.00 19.00 ? 56  SER A C   1 
ATOM   420  O  O   . SER A 1 56  ? 7.254   12.390  -17.258 1.00 20.85 ? 56  SER A O   1 
ATOM   421  C  CB  . SER A 1 56  ? 5.228   14.681  -17.081 1.00 18.85 ? 56  SER A CB  1 
ATOM   422  O  OG  . SER A 1 56  ? 4.602   14.183  -15.914 1.00 23.07 ? 56  SER A OG  1 
ATOM   423  N  N   . SER A 1 57  ? 5.360   11.197  -17.601 1.00 16.47 ? 57  SER A N   1 
ATOM   424  C  CA  . SER A 1 57  ? 5.942   9.990   -17.049 1.00 15.80 ? 57  SER A CA  1 
ATOM   425  C  C   . SER A 1 57  ? 6.968   9.397   -17.999 1.00 16.18 ? 57  SER A C   1 
ATOM   426  O  O   . SER A 1 57  ? 7.828   8.620   -17.558 1.00 16.11 ? 57  SER A O   1 
ATOM   427  C  CB  . SER A 1 57  ? 4.859   8.930   -16.870 1.00 17.47 ? 57  SER A CB  1 
ATOM   428  O  OG  . SER A 1 57  ? 3.945   9.186   -15.753 1.00 23.03 ? 57  SER A OG  1 
ATOM   429  N  N   . ALA A 1 58  ? 6.892   9.736   -19.265 1.00 16.18 ? 58  ALA A N   1 
ATOM   430  C  CA  . ALA A 1 58  ? 7.841   9.205   -20.299 1.00 16.82 ? 58  ALA A CA  1 
ATOM   431  C  C   . ALA A 1 58  ? 9.193   9.844   -20.015 1.00 17.50 ? 58  ALA A C   1 
ATOM   432  O  O   . ALA A 1 58  ? 9.304   11.050  -19.749 1.00 20.68 ? 58  ALA A O   1 
ATOM   433  C  CB  . ALA A 1 58  ? 7.392   9.529   -21.746 1.00 15.77 ? 58  ALA A CB  1 
ATOM   434  N  N   . LYS A 1 59  ? 10.213  9.068   -20.066 1.00 16.44 ? 59  LYS A N   1 
ATOM   435  C  CA  . LYS A 1 59  ? 11.582  9.593   -19.806 1.00 17.66 ? 59  LYS A CA  1 
ATOM   436  C  C   . LYS A 1 59  ? 12.554  9.491   -20.993 1.00 15.66 ? 59  LYS A C   1 
ATOM   437  O  O   . LYS A 1 59  ? 13.155  10.489  -21.391 1.00 16.47 ? 59  LYS A O   1 
ATOM   438  C  CB  . LYS A 1 59  ? 12.192  8.900   -18.584 1.00 20.36 ? 59  LYS A CB  1 
ATOM   439  C  CG  . LYS A 1 59  ? 11.334  8.975   -17.333 1.00 24.99 ? 59  LYS A CG  1 
ATOM   440  C  CD  . LYS A 1 59  ? 11.516  10.306  -16.621 1.00 32.31 ? 59  LYS A CD  1 
ATOM   441  C  CE  . LYS A 1 59  ? 10.590  11.367  -17.193 1.00 35.01 ? 59  LYS A CE  1 
ATOM   442  N  NZ  . LYS A 1 59  ? 9.782   12.027  -16.131 1.00 35.50 ? 59  LYS A NZ  1 
ATOM   443  N  N   . ILE A 1 60  ? 12.720  8.280   -21.545 1.00 14.00 ? 60  ILE A N   1 
ATOM   444  C  CA  . ILE A 1 60  ? 13.777  8.054   -22.541 1.00 14.36 ? 60  ILE A CA  1 
ATOM   445  C  C   . ILE A 1 60  ? 13.229  7.109   -23.605 1.00 14.27 ? 60  ILE A C   1 
ATOM   446  O  O   . ILE A 1 60  ? 12.331  6.328   -23.323 1.00 14.53 ? 60  ILE A O   1 
ATOM   447  C  CB  . ILE A 1 60  ? 15.112  7.427   -22.037 1.00 15.99 ? 60  ILE A CB  1 
ATOM   448  C  CG1 . ILE A 1 60  ? 14.910  6.295   -21.146 1.00 19.12 ? 60  ILE A CG1 1 
ATOM   449  C  CG2 . ILE A 1 60  ? 15.884  8.495   -21.211 1.00 20.68 ? 60  ILE A CG2 1 
ATOM   450  C  CD1 . ILE A 1 60  ? 16.131  5.413   -21.121 1.00 21.95 ? 60  ILE A CD1 1 
ATOM   451  N  N   . ILE A 1 61  ? 13.760  7.250   -24.806 1.00 13.70 ? 61  ILE A N   1 
ATOM   452  C  CA  . ILE A 1 61  ? 13.578  6.181   -25.808 1.00 14.45 ? 61  ILE A CA  1 
ATOM   453  C  C   . ILE A 1 61  ? 14.943  5.623   -26.144 1.00 14.72 ? 61  ILE A C   1 
ATOM   454  O  O   . ILE A 1 61  ? 15.946  6.397   -26.257 1.00 15.23 ? 61  ILE A O   1 
ATOM   455  C  CB  . ILE A 1 61  ? 12.829  6.716   -27.033 1.00 15.57 ? 61  ILE A CB  1 
ATOM   456  C  CG1 . ILE A 1 61  ? 12.426  5.549   -27.952 1.00 14.12 ? 61  ILE A CG1 1 
ATOM   457  C  CG2 . ILE A 1 61  ? 13.603  7.761   -27.835 1.00 14.85 ? 61  ILE A CG2 1 
ATOM   458  C  CD1 . ILE A 1 61  ? 11.611  5.992   -29.166 1.00 16.18 ? 61  ILE A CD1 1 
ATOM   459  N  N   . SER A 1 62  ? 15.021  4.305   -26.322 1.00 14.49 ? 62  SER A N   1 
ATOM   460  C  CA  . SER A 1 62  ? 16.287  3.663   -26.639 1.00 14.98 ? 62  SER A CA  1 
ATOM   461  C  C   . SER A 1 62  ? 16.100  2.551   -27.616 1.00 16.65 ? 62  SER A C   1 
ATOM   462  O  O   . SER A 1 62  ? 14.979  2.090   -27.841 1.00 16.59 ? 62  SER A O   1 
ATOM   463  C  CB  . SER A 1 62  ? 16.908  3.198   -25.367 1.00 17.57 ? 62  SER A CB  1 
ATOM   464  O  OG  . SER A 1 62  ? 16.118  2.149   -24.813 1.00 21.26 ? 62  SER A OG  1 
ATOM   465  N  N   . ASN A 1 63  ? 17.207  2.152   -28.277 1.00 13.73 ? 63  ASN A N   1 
ATOM   466  C  CA  . ASN A 1 63  ? 17.204  1.014   -29.139 1.00 16.84 ? 63  ASN A CA  1 
ATOM   467  C  C   . ASN A 1 63  ? 17.796  -0.164  -28.341 1.00 15.98 ? 63  ASN A C   1 
ATOM   468  O  O   . ASN A 1 63  ? 18.957  -0.195  -27.977 1.00 17.18 ? 63  ASN A O   1 
ATOM   469  C  CB  . ASN A 1 63  ? 18.070  1.301   -30.407 1.00 15.29 ? 63  ASN A CB  1 
ATOM   470  C  CG  . ASN A 1 63  ? 18.142  0.094   -31.335 1.00 16.11 ? 63  ASN A CG  1 
ATOM   471  O  OD1 . ASN A 1 63  ? 17.750  -1.028  -30.986 1.00 18.76 ? 63  ASN A OD1 1 
ATOM   472  N  ND2 . ASN A 1 63  ? 18.665  0.309   -32.588 1.00 16.92 ? 63  ASN A ND2 1 
ATOM   473  N  N   . SER A 1 64  ? 17.011  -1.160  -28.008 1.00 16.47 ? 64  SER A N   1 
ATOM   474  C  CA  . SER A 1 64  ? 17.480  -2.276  -27.218 1.00 16.04 ? 64  SER A CA  1 
ATOM   475  C  C   . SER A 1 64  ? 18.162  -3.300  -28.068 1.00 17.24 ? 64  SER A C   1 
ATOM   476  O  O   . SER A 1 64  ? 18.746  -4.286  -27.556 1.00 18.56 ? 64  SER A O   1 
ATOM   477  C  CB  . SER A 1 64  ? 16.277  -2.943  -26.560 1.00 15.91 ? 64  SER A CB  1 
ATOM   478  O  OG  . SER A 1 64  ? 15.446  -3.519  -27.555 1.00 15.22 ? 64  SER A OG  1 
ATOM   479  N  N   . GLY A 1 65  ? 18.068  -3.093  -29.387 1.00 16.55 ? 65  GLY A N   1 
ATOM   480  C  CA  . GLY A 1 65  ? 18.532  -4.148  -30.326 1.00 18.31 ? 65  GLY A CA  1 
ATOM   481  C  C   . GLY A 1 65  ? 17.410  -5.040  -30.828 1.00 16.52 ? 65  GLY A C   1 
ATOM   482  O  O   . GLY A 1 65  ? 17.573  -5.731  -31.850 1.00 17.82 ? 65  GLY A O   1 
ATOM   483  N  N   . HIS A 1 66  ? 16.278  -5.067  -30.104 1.00 16.27 ? 66  HIS A N   1 
ATOM   484  C  CA  . HIS A 1 66  ? 15.148  -5.901  -30.429 1.00 14.05 ? 66  HIS A CA  1 
ATOM   485  C  C   . HIS A 1 66  ? 13.876  -5.104  -30.780 1.00 14.20 ? 66  HIS A C   1 
ATOM   486  O  O   . HIS A 1 66  ? 12.937  -5.698  -31.338 1.00 15.15 ? 66  HIS A O   1 
ATOM   487  C  CB  . HIS A 1 66  ? 14.823  -6.771  -29.200 1.00 16.81 ? 66  HIS A CB  1 
ATOM   488  C  CG  . HIS A 1 66  ? 15.973  -7.355  -28.569 1.00 18.67 ? 66  HIS A CG  1 
ATOM   489  N  ND1 . HIS A 1 66  ? 16.787  -8.247  -29.198 1.00 22.34 ? 66  HIS A ND1 1 
ATOM   490  C  CD2 . HIS A 1 66  ? 16.514  -7.155  -27.280 1.00 18.47 ? 66  HIS A CD2 1 
ATOM   491  C  CE1 . HIS A 1 66  ? 17.816  -8.628  -28.359 1.00 23.80 ? 66  HIS A CE1 1 
ATOM   492  N  NE2 . HIS A 1 66  ? 17.633  -8.000  -27.181 1.00 22.46 ? 66  HIS A NE2 1 
ATOM   493  N  N   . SER A 1 67  ? 13.874  -3.786  -30.450 1.00 12.04 ? 67  SER A N   1 
ATOM   494  C  CA  . SER A 1 67  ? 12.788  -2.859  -30.820 1.00 13.16 ? 67  SER A CA  1 
ATOM   495  C  C   . SER A 1 67  ? 13.287  -1.493  -30.301 1.00 13.39 ? 67  SER A C   1 
ATOM   496  O  O   . SER A 1 67  ? 14.437  -1.380  -29.821 1.00 14.96 ? 67  SER A O   1 
ATOM   497  C  CB  . SER A 1 67  ? 11.436  -3.186  -30.109 1.00 14.20 ? 67  SER A CB  1 
ATOM   498  O  OG  . SER A 1 67  ? 10.342  -2.391  -30.585 1.00 13.84 ? 67  SER A OG  1 
ATOM   499  N  N   . PHE A 1 68  ? 12.433  -0.489  -30.390 1.00 13.03 ? 68  PHE A N   1 
ATOM   500  C  CA  . PHE A 1 68  ? 12.701  0.732   -29.662 1.00 13.52 ? 68  PHE A CA  1 
ATOM   501  C  C   . PHE A 1 68  ? 11.949  0.471   -28.330 1.00 12.19 ? 68  PHE A C   1 
ATOM   502  O  O   . PHE A 1 68  ? 10.923  -0.288  -28.253 1.00 15.03 ? 68  PHE A O   1 
ATOM   503  C  CB  . PHE A 1 68  ? 12.164  1.992   -30.303 1.00 13.55 ? 68  PHE A CB  1 
ATOM   504  C  CG  . PHE A 1 68  ? 10.649  2.063   -30.315 1.00 12.97 ? 68  PHE A CG  1 
ATOM   505  C  CD1 . PHE A 1 68  ? 9.964   1.663   -31.441 1.00 13.95 ? 68  PHE A CD1 1 
ATOM   506  C  CD2 . PHE A 1 68  ? 9.898   2.491   -29.208 1.00 13.63 ? 68  PHE A CD2 1 
ATOM   507  C  CE1 . PHE A 1 68  ? 8.579   1.696   -31.513 1.00 12.78 ? 68  PHE A CE1 1 
ATOM   508  C  CE2 . PHE A 1 68  ? 8.497   2.521   -29.270 1.00 14.51 ? 68  PHE A CE2 1 
ATOM   509  C  CZ  . PHE A 1 68  ? 7.839   2.126   -30.428 1.00 13.29 ? 68  PHE A CZ  1 
ATOM   510  N  N   . ASN A 1 69  ? 12.468  1.059   -27.221 1.00 13.20 ? 69  ASN A N   1 
ATOM   511  C  CA  . ASN A 1 69  ? 11.693  0.984   -25.945 1.00 12.80 ? 69  ASN A CA  1 
ATOM   512  C  C   . ASN A 1 69  ? 11.564  2.381   -25.405 1.00 12.31 ? 69  ASN A C   1 
ATOM   513  O  O   . ASN A 1 69  ? 12.584  3.089   -25.223 1.00 14.37 ? 69  ASN A O   1 
ATOM   514  C  CB  . ASN A 1 69  ? 12.566  0.319   -24.876 1.00 14.25 ? 69  ASN A CB  1 
ATOM   515  C  CG  . ASN A 1 69  ? 12.697  -1.147  -25.056 1.00 18.55 ? 69  ASN A CG  1 
ATOM   516  O  OD1 . ASN A 1 69  ? 11.787  -1.822  -25.589 1.00 21.95 ? 69  ASN A OD1 1 
ATOM   517  N  ND2 . ASN A 1 69  ? 13.764  -1.724  -24.473 1.00 19.45 ? 69  ASN A ND2 1 
ATOM   518  N  N   . VAL A 1 70  ? 10.332  2.821   -25.130 1.00 13.00 ? 70  VAL A N   1 
ATOM   519  C  CA  . VAL A 1 70  ? 10.101  4.108   -24.376 1.00 12.97 ? 70  VAL A CA  1 
ATOM   520  C  C   . VAL A 1 70  ? 9.971   3.686   -22.920 1.00 11.80 ? 70  VAL A C   1 
ATOM   521  O  O   . VAL A 1 70  ? 9.144   2.835   -22.605 1.00 11.93 ? 70  VAL A O   1 
ATOM   522  C  CB  . VAL A 1 70  ? 8.800   4.809   -24.816 1.00 13.89 ? 70  VAL A CB  1 
ATOM   523  C  CG1 . VAL A 1 70  ? 8.615   6.079   -23.972 1.00 14.64 ? 70  VAL A CG1 1 
ATOM   524  C  CG2 . VAL A 1 70  ? 8.872   5.203   -26.307 1.00 16.29 ? 70  VAL A CG2 1 
ATOM   525  N  N   . ASP A 1 71  ? 10.865  4.247   -22.047 1.00 12.82 ? 71  ASP A N   1 
ATOM   526  C  CA  . ASP A 1 71  ? 10.801  3.876   -20.601 1.00 13.84 ? 71  ASP A CA  1 
ATOM   527  C  C   . ASP A 1 71  ? 10.172  4.989   -19.806 1.00 13.80 ? 71  ASP A C   1 
ATOM   528  O  O   . ASP A 1 71  ? 10.354  6.189   -20.162 1.00 14.71 ? 71  ASP A O   1 
ATOM   529  C  CB  . ASP A 1 71  ? 12.204  3.614   -20.091 1.00 15.40 ? 71  ASP A CB  1 
ATOM   530  C  CG  . ASP A 1 71  ? 12.761  2.296   -20.611 1.00 22.82 ? 71  ASP A CG  1 
ATOM   531  O  OD1 . ASP A 1 71  ? 12.018  1.306   -20.875 1.00 28.31 ? 71  ASP A OD1 1 
ATOM   532  O  OD2 . ASP A 1 71  ? 13.974  2.296   -20.881 1.00 27.05 ? 71  ASP A OD2 1 
ATOM   533  N  N   . PHE A 1 72  ? 9.398   4.567   -18.832 1.00 13.87 ? 72  PHE A N   1 
ATOM   534  C  CA  . PHE A 1 72  ? 8.604   5.529   -18.008 1.00 13.42 ? 72  PHE A CA  1 
ATOM   535  C  C   . PHE A 1 72  ? 9.089   5.467   -16.592 1.00 15.88 ? 72  PHE A C   1 
ATOM   536  O  O   . PHE A 1 72  ? 9.647   4.489   -16.129 1.00 17.53 ? 72  PHE A O   1 
ATOM   537  C  CB  . PHE A 1 72  ? 7.112   5.158   -18.057 1.00 15.82 ? 72  PHE A CB  1 
ATOM   538  C  CG  . PHE A 1 72  ? 6.523   5.283   -19.464 1.00 15.63 ? 72  PHE A CG  1 
ATOM   539  C  CD1 . PHE A 1 72  ? 6.753   4.283   -20.380 1.00 15.33 ? 72  PHE A CD1 1 
ATOM   540  C  CD2 . PHE A 1 72  ? 5.788   6.408   -19.865 1.00 16.22 ? 72  PHE A CD2 1 
ATOM   541  C  CE1 . PHE A 1 72  ? 6.179   4.397   -21.701 1.00 13.71 ? 72  PHE A CE1 1 
ATOM   542  C  CE2 . PHE A 1 72  ? 5.241   6.523   -21.133 1.00 14.75 ? 72  PHE A CE2 1 
ATOM   543  C  CZ  . PHE A 1 72  ? 5.446   5.502   -22.051 1.00 15.01 ? 72  PHE A CZ  1 
ATOM   544  N  N   . ASP A 1 73  ? 8.831   6.590   -15.948 1.00 19.03 ? 73  ASP A N   1 
ATOM   545  C  CA  . ASP A 1 73  ? 9.160   6.744   -14.578 1.00 22.89 ? 73  ASP A CA  1 
ATOM   546  C  C   . ASP A 1 73  ? 8.135   5.946   -13.955 1.00 26.67 ? 73  ASP A C   1 
ATOM   547  O  O   . ASP A 1 73  ? 6.855   6.263   -14.064 1.00 28.30 ? 73  ASP A O   1 
ATOM   548  C  CB  . ASP A 1 73  ? 8.880   8.167   -14.088 1.00 23.81 ? 73  ASP A CB  1 
ATOM   549  C  CG  . ASP A 1 73  ? 9.233   8.302   -12.583 1.00 27.48 ? 73  ASP A CG  1 
ATOM   550  O  OD1 . ASP A 1 73  ? 8.603   7.609   -11.757 1.00 25.99 ? 73  ASP A OD1 1 
ATOM   551  O  OD2 . ASP A 1 73  ? 10.179  9.049   -12.292 1.00 35.15 ? 73  ASP A OD2 1 
ATOM   552  N  N   A ASP A 1 74  ? 8.483   4.857   -13.365 0.50 20.72 ? 74  ASP A N   1 
ATOM   553  N  N   B ASP A 1 74  ? 8.730   5.061   -13.125 0.50 27.40 ? 74  ASP A N   1 
ATOM   554  C  CA  A ASP A 1 74  ? 7.529   4.080   -12.632 0.50 20.84 ? 74  ASP A CA  1 
ATOM   555  C  CA  B ASP A 1 74  ? 8.309   3.792   -12.507 0.50 30.27 ? 74  ASP A CA  1 
ATOM   556  C  C   A ASP A 1 74  ? 7.770   3.936   -11.048 0.50 23.08 ? 74  ASP A C   1 
ATOM   557  C  C   B ASP A 1 74  ? 8.390   3.786   -11.011 0.50 27.24 ? 74  ASP A C   1 
ATOM   558  O  O   A ASP A 1 74  ? 7.562   2.875   -10.504 0.50 19.61 ? 74  ASP A O   1 
ATOM   559  O  O   B ASP A 1 74  ? 8.502   2.703   -10.413 0.50 17.87 ? 74  ASP A O   1 
ATOM   560  C  CB  A ASP A 1 74  ? 7.716   2.701   -13.161 0.50 19.37 ? 74  ASP A CB  1 
ATOM   561  C  CB  B ASP A 1 74  ? 9.240   2.681   -13.075 0.50 28.77 ? 74  ASP A CB  1 
ATOM   562  C  CG  A ASP A 1 74  ? 9.085   2.141   -12.810 0.50 21.65 ? 74  ASP A CG  1 
ATOM   563  C  CG  B ASP A 1 74  ? 8.509   1.402   -13.492 0.50 28.39 ? 74  ASP A CG  1 
ATOM   564  O  OD1 A ASP A 1 74  ? 9.955   2.891   -12.272 0.50 19.23 ? 74  ASP A OD1 1 
ATOM   565  O  OD1 B ASP A 1 74  ? 7.422   1.473   -14.100 0.50 22.12 ? 74  ASP A OD1 1 
ATOM   566  O  OD2 A ASP A 1 74  ? 9.280   0.934   -13.057 0.50 22.18 ? 74  ASP A OD2 1 
ATOM   567  O  OD2 B ASP A 1 74  ? 9.064   0.309   -13.239 0.50 26.21 ? 74  ASP A OD2 1 
ATOM   568  N  N   . THR A 1 75  ? 8.323   4.980   -10.426 1.00 27.01 ? 75  THR A N   1 
ATOM   569  C  CA  . THR A 1 75  ? 8.237   4.983   -8.949  1.00 23.75 ? 75  THR A CA  1 
ATOM   570  C  C   . THR A 1 75  ? 7.040   5.776   -8.380  1.00 22.23 ? 75  THR A C   1 
ATOM   571  O  O   . THR A 1 75  ? 6.921   5.993   -7.187  1.00 19.48 ? 75  THR A O   1 
ATOM   572  C  CB  . THR A 1 75  ? 9.578   5.092   -8.134  1.00 24.23 ? 75  THR A CB  1 
ATOM   573  O  OG1 . THR A 1 75  ? 10.375  6.208   -8.552  1.00 28.71 ? 75  THR A OG1 1 
ATOM   574  C  CG2 . THR A 1 75  ? 10.411  3.765   -8.194  1.00 28.00 ? 75  THR A CG2 1 
ATOM   575  N  N   . GLU A 1 76  ? 6.132   6.123   -9.275  1.00 19.49 ? 76  GLU A N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 5.023   6.929   -9.063  1.00 20.01 ? 76  GLU A CA  1 
ATOM   577  C  C   . GLU A 1 76  ? 3.772   6.238   -9.704  1.00 19.17 ? 76  GLU A C   1 
ATOM   578  O  O   . GLU A 1 76  ? 3.914   5.425   -10.664 1.00 17.94 ? 76  GLU A O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 5.285   8.295   -9.766  1.00 23.47 ? 76  GLU A CB  1 
ATOM   580  C  CG  . GLU A 1 76  ? 6.512   9.111   -9.280  1.00 27.26 ? 76  GLU A CG  1 
ATOM   581  C  CD  . GLU A 1 76  ? 7.007   10.153  -10.306 1.00 36.57 ? 76  GLU A CD  1 
ATOM   582  O  OE1 . GLU A 1 76  ? 6.525   10.102  -11.492 1.00 34.36 ? 76  GLU A OE1 1 
ATOM   583  O  OE2 . GLU A 1 76  ? 7.898   11.029  -9.976  1.00 32.71 ? 76  GLU A OE2 1 
ATOM   584  N  N   . ASN A 1 77  ? 2.591   6.483   -9.160  1.00 18.19 ? 77  ASN A N   1 
ATOM   585  C  CA  . ASN A 1 77  ? 1.315   5.996   -9.734  1.00 17.84 ? 77  ASN A CA  1 
ATOM   586  C  C   . ASN A 1 77  ? 0.605   7.077   -10.600 1.00 17.27 ? 77  ASN A C   1 
ATOM   587  O  O   . ASN A 1 77  ? -0.600  7.063   -10.686 1.00 19.80 ? 77  ASN A O   1 
ATOM   588  C  CB  . ASN A 1 77  ? 0.372   5.400   -8.655  1.00 19.98 ? 77  ASN A CB  1 
ATOM   589  C  CG  . ASN A 1 77  ? 0.763   3.973   -8.259  1.00 21.29 ? 77  ASN A CG  1 
ATOM   590  O  OD1 . ASN A 1 77  ? 1.564   3.349   -8.952  1.00 17.96 ? 77  ASN A OD1 1 
ATOM   591  N  ND2 . ASN A 1 77  ? 0.273   3.464   -7.119  1.00 17.35 ? 77  ASN A ND2 1 
ATOM   592  N  N   . LYS A 1 78  ? 1.404   7.906   -11.298 1.00 17.70 ? 78  LYS A N   1 
ATOM   593  C  CA  . LYS A 1 78  ? 0.818   8.921   -12.236 1.00 15.19 ? 78  LYS A CA  1 
ATOM   594  C  C   . LYS A 1 78  ? 0.208   8.215   -13.493 1.00 16.55 ? 78  LYS A C   1 
ATOM   595  O  O   . LYS A 1 78  ? -0.780  8.700   -14.135 1.00 17.10 ? 78  LYS A O   1 
ATOM   596  C  CB  . LYS A 1 78  ? 1.840   9.970   -12.633 1.00 18.89 ? 78  LYS A CB  1 
ATOM   597  C  CG  . LYS A 1 78  ? 2.255   10.892  -11.470 1.00 21.56 ? 78  LYS A CG  1 
ATOM   598  C  CD  . LYS A 1 78  ? 3.292   11.949  -11.912 1.00 30.57 ? 78  LYS A CD  1 
ATOM   599  C  CE  . LYS A 1 78  ? 3.488   12.991  -10.794 1.00 34.84 ? 78  LYS A CE  1 
ATOM   600  N  NZ  . LYS A 1 78  ? 4.040   14.284  -11.262 1.00 42.35 ? 78  LYS A NZ  1 
ATOM   601  N  N   . SER A 1 79  ? 0.882   7.128   -13.905 1.00 14.36 ? 79  SER A N   1 
ATOM   602  C  CA  . SER A 1 79  ? 0.442   6.417   -15.127 1.00 13.88 ? 79  SER A CA  1 
ATOM   603  C  C   . SER A 1 79  ? 0.215   4.969   -14.768 1.00 13.06 ? 79  SER A C   1 
ATOM   604  O  O   . SER A 1 79  ? 1.177   4.182   -14.571 1.00 15.19 ? 79  SER A O   1 
ATOM   605  C  CB  . SER A 1 79  ? 1.576   6.516   -16.176 1.00 12.22 ? 79  SER A CB  1 
ATOM   606  O  OG  . SER A 1 79  ? 1.680   7.850   -16.644 1.00 14.44 ? 79  SER A OG  1 
ATOM   607  N  N   . VAL A 1 80  ? -1.024  4.577   -14.728 1.00 14.58 ? 80  VAL A N   1 
ATOM   608  C  CA  . VAL A 1 80  ? -1.441  3.247   -14.256 1.00 13.45 ? 80  VAL A CA  1 
ATOM   609  C  C   . VAL A 1 80  ? -2.619  2.666   -15.042 1.00 14.21 ? 80  VAL A C   1 
ATOM   610  O  O   . VAL A 1 80  ? -3.410  3.448   -15.619 1.00 15.51 ? 80  VAL A O   1 
ATOM   611  C  CB  . VAL A 1 80  ? -1.871  3.331   -12.775 1.00 14.59 ? 80  VAL A CB  1 
ATOM   612  C  CG1 . VAL A 1 80  ? -0.663  3.661   -11.886 1.00 15.33 ? 80  VAL A CG1 1 
ATOM   613  C  CG2 . VAL A 1 80  ? -2.973  4.438   -12.565 1.00 18.28 ? 80  VAL A CG2 1 
ATOM   614  N  N   . LEU A 1 81  ? -2.655  1.341   -15.050 1.00 14.21 ? 81  LEU A N   1 
ATOM   615  C  CA  . LEU A 1 81  ? -3.691  0.587   -15.721 1.00 13.08 ? 81  LEU A CA  1 
ATOM   616  C  C   . LEU A 1 81  ? -4.418  -0.197  -14.634 1.00 17.32 ? 81  LEU A C   1 
ATOM   617  O  O   . LEU A 1 81  ? -3.839  -0.895  -13.821 1.00 16.49 ? 81  LEU A O   1 
ATOM   618  C  CB  . LEU A 1 81  ? -3.055  -0.391  -16.757 1.00 14.00 ? 81  LEU A CB  1 
ATOM   619  C  CG  . LEU A 1 81  ? -4.073  -1.289  -17.459 1.00 15.59 ? 81  LEU A CG  1 
ATOM   620  C  CD1 . LEU A 1 81  ? -4.947  -0.451  -18.420 1.00 15.46 ? 81  LEU A CD1 1 
ATOM   621  C  CD2 . LEU A 1 81  ? -3.245  -2.349  -18.273 1.00 14.60 ? 81  LEU A CD2 1 
ATOM   622  N  N   . ARG A 1 82  ? -5.741  0.035   -14.574 1.00 17.42 ? 82  ARG A N   1 
ATOM   623  C  CA  . ARG A 1 82  ? -6.576  -0.680  -13.616 1.00 16.63 ? 82  ARG A CA  1 
ATOM   624  C  C   . ARG A 1 82  ? -7.797  -1.220  -14.295 1.00 17.31 ? 82  ARG A C   1 
ATOM   625  O  O   . ARG A 1 82  ? -8.065  -0.896  -15.466 1.00 17.44 ? 82  ARG A O   1 
ATOM   626  C  CB  . ARG A 1 82  ? -7.007  0.344   -12.516 1.00 16.55 ? 82  ARG A CB  1 
ATOM   627  C  CG  . ARG A 1 82  ? -5.844  0.730   -11.582 1.00 19.52 ? 82  ARG A CG  1 
ATOM   628  C  CD  . ARG A 1 82  ? -6.144  1.970   -10.678 1.00 19.29 ? 82  ARG A CD  1 
ATOM   629  N  NE  . ARG A 1 82  ? -6.293  3.192   -11.504 1.00 20.50 ? 82  ARG A NE  1 
ATOM   630  C  CZ  . ARG A 1 82  ? -6.514  4.423   -11.022 1.00 21.99 ? 82  ARG A CZ  1 
ATOM   631  N  NH1 . ARG A 1 82  ? -6.648  4.612   -9.702  1.00 22.87 ? 82  ARG A NH1 1 
ATOM   632  N  NH2 . ARG A 1 82  ? -6.614  5.444   -11.845 1.00 21.05 ? 82  ARG A NH2 1 
ATOM   633  N  N   . GLY A 1 83  ? -8.546  -2.090  -13.591 1.00 17.50 ? 83  GLY A N   1 
ATOM   634  C  CA  . GLY A 1 83  ? -9.849  -2.542  -14.139 1.00 18.99 ? 83  GLY A CA  1 
ATOM   635  C  C   . GLY A 1 83  ? -9.654  -3.695  -15.110 1.00 18.83 ? 83  GLY A C   1 
ATOM   636  O  O   . GLY A 1 83  ? -8.628  -4.381  -15.086 1.00 19.10 ? 83  GLY A O   1 
ATOM   637  N  N   . GLY A 1 84  ? -10.586 -3.871  -16.043 1.00 21.29 ? 84  GLY A N   1 
ATOM   638  C  CA  . GLY A 1 84  ? -10.535 -5.044  -16.858 1.00 23.37 ? 84  GLY A CA  1 
ATOM   639  C  C   . GLY A 1 84  ? -10.447 -6.323  -16.023 1.00 18.11 ? 84  GLY A C   1 
ATOM   640  O  O   . GLY A 1 84  ? -11.219 -6.530  -15.089 1.00 24.30 ? 84  GLY A O   1 
ATOM   641  N  N   . PRO A 1 85  ? -9.503  -7.216  -16.352 1.00 18.97 ? 85  PRO A N   1 
ATOM   642  C  CA  . PRO A 1 85  ? -9.280  -8.433  -15.661 1.00 16.63 ? 85  PRO A CA  1 
ATOM   643  C  C   . PRO A 1 85  ? -8.348  -8.298  -14.398 1.00 18.60 ? 85  PRO A C   1 
ATOM   644  O  O   . PRO A 1 85  ? -8.131  -9.334  -13.691 1.00 19.86 ? 85  PRO A O   1 
ATOM   645  C  CB  . PRO A 1 85  ? -8.569  -9.268  -16.729 1.00 19.95 ? 85  PRO A CB  1 
ATOM   646  C  CG  . PRO A 1 85  ? -7.716  -8.278  -17.450 1.00 20.43 ? 85  PRO A CG  1 
ATOM   647  C  CD  . PRO A 1 85  ? -8.593  -7.085  -17.506 1.00 20.06 ? 85  PRO A CD  1 
ATOM   648  N  N   . LEU A 1 86  ? -7.856  -7.078  -14.136 1.00 17.97 ? 86  LEU A N   1 
ATOM   649  C  CA  . LEU A 1 86  ? -6.770  -6.893  -13.173 1.00 17.59 ? 86  LEU A CA  1 
ATOM   650  C  C   . LEU A 1 86  ? -7.288  -6.655  -11.757 1.00 20.50 ? 86  LEU A C   1 
ATOM   651  O  O   . LEU A 1 86  ? -8.288  -5.901  -11.564 1.00 21.05 ? 86  LEU A O   1 
ATOM   652  C  CB  . LEU A 1 86  ? -5.949  -5.632  -13.544 1.00 16.63 ? 86  LEU A CB  1 
ATOM   653  C  CG  . LEU A 1 86  ? -5.362  -5.824  -14.971 1.00 15.42 ? 86  LEU A CG  1 
ATOM   654  C  CD1 . LEU A 1 86  ? -4.737  -4.498  -15.385 1.00 17.46 ? 86  LEU A CD1 1 
ATOM   655  C  CD2 . LEU A 1 86  ? -4.368  -6.962  -15.154 1.00 16.88 ? 86  LEU A CD2 1 
ATOM   656  N  N   . THR A 1 87  ? -6.548  -7.239  -10.806 1.00 20.21 ? 87  THR A N   1 
ATOM   657  C  CA  . THR A 1 87  ? -6.744  -6.863  -9.389  1.00 20.64 ? 87  THR A CA  1 
ATOM   658  C  C   . THR A 1 87  ? -5.660  -5.877  -8.956  1.00 18.18 ? 87  THR A C   1 
ATOM   659  O  O   . THR A 1 87  ? -4.453  -6.227  -9.132  1.00 19.05 ? 87  THR A O   1 
ATOM   660  C  CB  . THR A 1 87  ? -6.614  -8.114  -8.552  1.00 19.31 ? 87  THR A CB  1 
ATOM   661  O  OG1 . THR A 1 87  ? -7.682  -8.976  -8.931  1.00 26.80 ? 87  THR A OG1 1 
ATOM   662  C  CG2 . THR A 1 87  ? -6.828  -7.763  -6.992  1.00 23.54 ? 87  THR A CG2 1 
ATOM   663  N  N   . GLY A 1 88  ? -6.031  -4.659  -8.520  1.00 16.77 ? 88  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 88  ? -4.974  -3.714  -8.118  1.00 19.02 ? 88  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 88  ? -4.450  -2.849  -9.273  1.00 20.45 ? 88  GLY A C   1 
ATOM   666  O  O   . GLY A 1 88  ? -5.002  -2.856  -10.380 1.00 20.54 ? 88  GLY A O   1 
ATOM   667  N  N   . SER A 1 89  ? -3.375  -2.143  -8.996  1.00 16.79 ? 89  SER A N   1 
ATOM   668  C  CA  . SER A 1 89  ? -2.883  -1.088  -9.870  1.00 17.81 ? 89  SER A CA  1 
ATOM   669  C  C   . SER A 1 89  ? -1.588  -1.594  -10.486 1.00 17.51 ? 89  SER A C   1 
ATOM   670  O  O   . SER A 1 89  ? -0.670  -1.979  -9.801  1.00 17.15 ? 89  SER A O   1 
ATOM   671  C  CB  . SER A 1 89  ? -2.627  0.194   -9.081  1.00 16.84 ? 89  SER A CB  1 
ATOM   672  O  OG  . SER A 1 89  ? -2.326  1.306   -9.937  1.00 19.25 ? 89  SER A OG  1 
ATOM   673  N  N   . TYR A 1 90  ? -1.598  -1.539  -11.819 1.00 14.99 ? 90  TYR A N   1 
ATOM   674  C  CA  . TYR A 1 90  ? -0.375  -1.959  -12.601 1.00 13.08 ? 90  TYR A CA  1 
ATOM   675  C  C   . TYR A 1 90  ? 0.218   -0.729  -13.220 1.00 12.76 ? 90  TYR A C   1 
ATOM   676  O  O   . TYR A 1 90  ? -0.404  0.065   -13.997 1.00 15.79 ? 90  TYR A O   1 
ATOM   677  C  CB  . TYR A 1 90  ? -0.868  -2.904  -13.706 1.00 13.57 ? 90  TYR A CB  1 
ATOM   678  C  CG  . TYR A 1 90  ? -1.055  -4.276  -13.176 1.00 11.74 ? 90  TYR A CG  1 
ATOM   679  C  CD1 . TYR A 1 90  ? -2.198  -4.550  -12.331 1.00 14.07 ? 90  TYR A CD1 1 
ATOM   680  C  CD2 . TYR A 1 90  ? -0.154  -5.366  -13.435 1.00 12.54 ? 90  TYR A CD2 1 
ATOM   681  C  CE1 . TYR A 1 90  ? -2.360  -5.805  -11.866 1.00 13.52 ? 90  TYR A CE1 1 
ATOM   682  C  CE2 . TYR A 1 90  ? -0.316  -6.650  -12.946 1.00 13.07 ? 90  TYR A CE2 1 
ATOM   683  C  CZ  . TYR A 1 90  ? -1.505  -6.873  -12.176 1.00 14.94 ? 90  TYR A CZ  1 
ATOM   684  O  OH  . TYR A 1 90  ? -1.735  -8.111  -11.657 1.00 15.12 ? 90  TYR A OH  1 
ATOM   685  N  N   . ARG A 1 91  ? 1.461   -0.465  -12.841 1.00 11.52 ? 91  ARG A N   1 
ATOM   686  C  CA  . ARG A 1 91  ? 2.189   0.759   -13.148 1.00 13.42 ? 91  ARG A CA  1 
ATOM   687  C  C   . ARG A 1 91  ? 2.789   0.688   -14.546 1.00 12.21 ? 91  ARG A C   1 
ATOM   688  O  O   . ARG A 1 91  ? 3.467   -0.320  -14.842 1.00 12.92 ? 91  ARG A O   1 
ATOM   689  C  CB  . ARG A 1 91  ? 3.277   0.961   -12.058 1.00 15.52 ? 91  ARG A CB  1 
ATOM   690  C  CG  . ARG A 1 91  ? 3.987   2.340   -12.140 1.00 16.66 ? 91  ARG A CG  1 
ATOM   691  C  CD  . ARG A 1 91  ? 4.990   2.634   -11.041 1.00 16.24 ? 91  ARG A CD  1 
ATOM   692  N  NE  . ARG A 1 91  ? 4.271   2.657   -9.781  1.00 17.65 ? 91  ARG A NE  1 
ATOM   693  C  CZ  . ARG A 1 91  ? 4.782   2.304   -8.612  1.00 15.66 ? 91  ARG A CZ  1 
ATOM   694  N  NH1 . ARG A 1 91  ? 6.043   1.899   -8.518  1.00 16.52 ? 91  ARG A NH1 1 
ATOM   695  N  NH2 . ARG A 1 91  ? 4.019   2.366   -7.532  1.00 15.71 ? 91  ARG A NH2 1 
ATOM   696  N  N   . LEU A 1 92  ? 2.581   1.705   -15.333 1.00 12.09 ? 92  LEU A N   1 
ATOM   697  C  CA  . LEU A 1 92  ? 3.193   1.723   -16.674 1.00 12.70 ? 92  LEU A CA  1 
ATOM   698  C  C   . LEU A 1 92  ? 4.718   1.684   -16.605 1.00 13.53 ? 92  LEU A C   1 
ATOM   699  O  O   . LEU A 1 92  ? 5.351   2.456   -15.855 1.00 13.52 ? 92  LEU A O   1 
ATOM   700  C  CB  . LEU A 1 92  ? 2.755   2.960   -17.397 1.00 12.87 ? 92  LEU A CB  1 
ATOM   701  C  CG  . LEU A 1 92  ? 3.380   3.278   -18.746 1.00 11.84 ? 92  LEU A CG  1 
ATOM   702  C  CD1 . LEU A 1 92  ? 2.955   2.161   -19.792 1.00 11.89 ? 92  LEU A CD1 1 
ATOM   703  C  CD2 . LEU A 1 92  ? 2.925   4.654   -19.297 1.00 13.13 ? 92  LEU A CD2 1 
ATOM   704  N  N   . ARG A 1 93  ? 5.392   0.808   -17.370 1.00 11.66 ? 93  ARG A N   1 
ATOM   705  C  CA  . ARG A 1 93  ? 6.844   0.677   -17.384 1.00 12.10 ? 93  ARG A CA  1 
ATOM   706  C  C   . ARG A 1 93  ? 7.465   1.062   -18.736 1.00 12.70 ? 93  ARG A C   1 
ATOM   707  O  O   . ARG A 1 93  ? 8.380   1.844   -18.790 1.00 13.96 ? 93  ARG A O   1 
ATOM   708  C  CB  . ARG A 1 93  ? 7.214   -0.785  -17.022 1.00 16.03 ? 93  ARG A CB  1 
ATOM   709  C  CG  . ARG A 1 93  ? 8.664   -1.092  -17.355 1.00 20.01 ? 93  ARG A CG  1 
ATOM   710  C  CD  . ARG A 1 93  ? 9.521   -0.347  -16.383 1.00 22.98 ? 93  ARG A CD  1 
ATOM   711  N  NE  . ARG A 1 93  ? 10.948  -0.573  -16.592 1.00 31.81 ? 93  ARG A NE  1 
ATOM   712  C  CZ  . ARG A 1 93  ? 11.834  0.402   -16.777 1.00 42.36 ? 93  ARG A CZ  1 
ATOM   713  N  NH1 . ARG A 1 93  ? 11.436  1.666   -16.781 1.00 37.96 ? 93  ARG A NH1 1 
ATOM   714  N  NH2 . ARG A 1 93  ? 13.115  0.111   -16.953 1.00 45.61 ? 93  ARG A NH2 1 
ATOM   715  N  N   . GLN A 1 94  ? 6.954   0.455   -19.810 1.00 10.46 ? 94  GLN A N   1 
ATOM   716  C  CA  . GLN A 1 94  ? 7.498   0.715   -21.110 1.00 12.62 ? 94  GLN A CA  1 
ATOM   717  C  C   . GLN A 1 94  ? 6.615   0.417   -22.297 1.00 11.40 ? 94  GLN A C   1 
ATOM   718  O  O   . GLN A 1 94  ? 5.648   -0.336  -22.115 1.00 11.33 ? 94  GLN A O   1 
ATOM   719  C  CB  . GLN A 1 94  ? 8.859   0.014   -21.259 1.00 17.29 ? 94  GLN A CB  1 
ATOM   720  C  CG  . GLN A 1 94  ? 8.788   -1.504  -21.265 1.00 16.02 ? 94  GLN A CG  1 
ATOM   721  C  CD  . GLN A 1 94  ? 8.946   -2.074  -22.661 1.00 22.66 ? 94  GLN A CD  1 
ATOM   722  O  OE1 . GLN A 1 94  ? 8.002   -2.087  -23.452 1.00 20.90 ? 94  GLN A OE1 1 
ATOM   723  N  NE2 . GLN A 1 94  ? 10.146  -2.544  -22.974 1.00 23.27 ? 94  GLN A NE2 1 
ATOM   724  N  N   . VAL A 1 95  ? 6.973   1.009   -23.408 1.00 11.39 ? 95  VAL A N   1 
ATOM   725  C  CA  . VAL A 1 95  ? 6.196   0.783   -24.635 1.00 11.02 ? 95  VAL A CA  1 
ATOM   726  C  C   . VAL A 1 95  ? 7.235   0.339   -25.684 1.00 11.41 ? 95  VAL A C   1 
ATOM   727  O  O   . VAL A 1 95  ? 8.315   0.902   -25.772 1.00 10.97 ? 95  VAL A O   1 
ATOM   728  C  CB  . VAL A 1 95  ? 5.554   2.129   -25.052 1.00 11.22 ? 95  VAL A CB  1 
ATOM   729  C  CG1 . VAL A 1 95  ? 5.031   2.082   -26.517 1.00 14.57 ? 95  VAL A CG1 1 
ATOM   730  C  CG2 . VAL A 1 95  ? 4.362   2.359   -24.175 1.00 13.02 ? 95  VAL A CG2 1 
ATOM   731  N  N   . HIS A 1 96  ? 6.850   -0.661  -26.552 1.00 11.24 ? 96  HIS A N   1 
ATOM   732  C  CA  . HIS A 1 96  ? 7.709   -1.056  -27.711 1.00 10.57 ? 96  HIS A CA  1 
ATOM   733  C  C   . HIS A 1 96  ? 6.767   -1.566  -28.783 1.00 10.89 ? 96  HIS A C   1 
ATOM   734  O  O   . HIS A 1 96  ? 5.552   -1.597  -28.650 1.00 11.77 ? 96  HIS A O   1 
ATOM   735  C  CB  . HIS A 1 96  ? 8.748   -2.112  -27.254 1.00 10.55 ? 96  HIS A CB  1 
ATOM   736  C  CG  . HIS A 1 96  ? 8.111   -3.334  -26.788 1.00 10.11 ? 96  HIS A CG  1 
ATOM   737  N  ND1 . HIS A 1 96  ? 7.827   -3.573  -25.441 1.00 12.13 ? 96  HIS A ND1 1 
ATOM   738  C  CD2 . HIS A 1 96  ? 7.665   -4.431  -27.480 1.00 9.79  ? 96  HIS A CD2 1 
ATOM   739  C  CE1 . HIS A 1 96  ? 7.196   -4.717  -25.333 1.00 11.63 ? 96  HIS A CE1 1 
ATOM   740  N  NE2 . HIS A 1 96  ? 7.092   -5.278  -26.604 1.00 10.50 ? 96  HIS A NE2 1 
ATOM   741  N  N   . LEU A 1 97  ? 7.392   -1.923  -29.931 1.00 10.99 ? 97  LEU A N   1 
ATOM   742  C  CA  . LEU A 1 97  ? 6.608   -2.312  -31.134 1.00 11.33 ? 97  LEU A CA  1 
ATOM   743  C  C   . LEU A 1 97  ? 7.241   -3.537  -31.834 1.00 10.78 ? 97  LEU A C   1 
ATOM   744  O  O   . LEU A 1 97  ? 8.450   -3.718  -31.825 1.00 11.99 ? 97  LEU A O   1 
ATOM   745  C  CB  . LEU A 1 97  ? 6.673   -1.120  -32.102 1.00 12.19 ? 97  LEU A CB  1 
ATOM   746  C  CG  . LEU A 1 97  ? 5.777   -1.245  -33.364 1.00 11.64 ? 97  LEU A CG  1 
ATOM   747  C  CD1 . LEU A 1 97  ? 4.318   -1.076  -33.010 1.00 13.34 ? 97  LEU A CD1 1 
ATOM   748  C  CD2 . LEU A 1 97  ? 6.209   -0.111  -34.317 1.00 14.46 ? 97  LEU A CD2 1 
ATOM   749  N  N   . HIS A 1 98  ? 6.334   -4.353  -32.425 1.00 10.37 ? 98  HIS A N   1 
ATOM   750  C  CA  . HIS A 1 98  ? 6.770   -5.505  -33.202 1.00 9.82  ? 98  HIS A CA  1 
ATOM   751  C  C   . HIS A 1 98  ? 6.248   -5.285  -34.659 1.00 9.84  ? 98  HIS A C   1 
ATOM   752  O  O   . HIS A 1 98  ? 5.157   -4.818  -34.860 1.00 10.79 ? 98  HIS A O   1 
ATOM   753  C  CB  . HIS A 1 98  ? 6.200   -6.765  -32.673 1.00 10.02 ? 98  HIS A CB  1 
ATOM   754  C  CG  . HIS A 1 98  ? 6.598   -7.072  -31.247 1.00 11.02 ? 98  HIS A CG  1 
ATOM   755  N  ND1 . HIS A 1 98  ? 7.762   -7.696  -30.947 1.00 9.96  ? 98  HIS A ND1 1 
ATOM   756  C  CD2 . HIS A 1 98  ? 5.978   -6.715  -30.044 1.00 12.51 ? 98  HIS A CD2 1 
ATOM   757  C  CE1 . HIS A 1 98  ? 7.813   -7.884  -29.575 1.00 10.77 ? 98  HIS A CE1 1 
ATOM   758  N  NE2 . HIS A 1 98  ? 6.765   -7.246  -29.040 1.00 9.82  ? 98  HIS A NE2 1 
ATOM   759  N  N   . TRP A 1 99  ? 7.094   -5.724  -35.577 1.00 10.83 ? 99  TRP A N   1 
ATOM   760  C  CA  . TRP A 1 99  ? 6.700   -5.673  -37.040 1.00 12.05 ? 99  TRP A CA  1 
ATOM   761  C  C   . TRP A 1 99  ? 7.332   -6.823  -37.732 1.00 13.42 ? 99  TRP A C   1 
ATOM   762  O  O   . TRP A 1 99  ? 8.129   -7.604  -37.195 1.00 13.25 ? 99  TRP A O   1 
ATOM   763  C  CB  . TRP A 1 99  ? 7.138   -4.349  -37.615 1.00 12.92 ? 99  TRP A CB  1 
ATOM   764  C  CG  . TRP A 1 99  ? 8.621   -4.101  -37.451 1.00 12.46 ? 99  TRP A CG  1 
ATOM   765  C  CD1 . TRP A 1 99  ? 9.660   -4.550  -38.265 1.00 12.50 ? 99  TRP A CD1 1 
ATOM   766  C  CD2 . TRP A 1 99  ? 9.280   -3.338  -36.384 1.00 11.86 ? 99  TRP A CD2 1 
ATOM   767  N  NE1 . TRP A 1 99  ? 10.875  -4.125  -37.788 1.00 13.03 ? 99  TRP A NE1 1 
ATOM   768  C  CE2 . TRP A 1 99  ? 10.718  -3.394  -36.664 1.00 12.64 ? 99  TRP A CE2 1 
ATOM   769  C  CE3 . TRP A 1 99  ? 8.839   -2.642  -35.272 1.00 11.93 ? 99  TRP A CE3 1 
ATOM   770  C  CZ2 . TRP A 1 99  ? 11.646  -2.771  -35.851 1.00 13.89 ? 99  TRP A CZ2 1 
ATOM   771  C  CZ3 . TRP A 1 99  ? 9.786   -2.018  -34.460 1.00 12.57 ? 99  TRP A CZ3 1 
ATOM   772  C  CH2 . TRP A 1 99  ? 11.154  -2.082  -34.744 1.00 14.05 ? 99  TRP A CH2 1 
ATOM   773  N  N   . GLY A 1 100 ? 6.962   -6.959  -39.028 1.00 13.45 ? 100 GLY A N   1 
ATOM   774  C  CA  . GLY A 1 100 ? 7.620   -7.970  -39.893 1.00 14.91 ? 100 GLY A CA  1 
ATOM   775  C  C   . GLY A 1 100 ? 8.408   -7.306  -41.026 1.00 15.35 ? 100 GLY A C   1 
ATOM   776  O  O   . GLY A 1 100 ? 8.440   -6.091  -41.172 1.00 14.76 ? 100 GLY A O   1 
ATOM   777  N  N   . SER A 1 101 ? 9.020   -8.149  -41.883 1.00 16.24 ? 101 SER A N   1 
ATOM   778  C  CA  . SER A 1 101 ? 9.824   -7.620  -43.027 1.00 16.93 ? 101 SER A CA  1 
ATOM   779  C  C   . SER A 1 101 ? 8.959   -7.135  -44.184 1.00 17.69 ? 101 SER A C   1 
ATOM   780  O  O   . SER A 1 101 ? 9.467   -6.409  -45.018 1.00 20.02 ? 101 SER A O   1 
ATOM   781  C  CB  . SER A 1 101 ? 10.817  -8.641  -43.551 1.00 18.35 ? 101 SER A CB  1 
ATOM   782  O  OG  . SER A 1 101 ? 10.104  -9.659  -44.152 1.00 21.82 ? 101 SER A OG  1 
ATOM   783  N  N   . ALA A 1 102 ? 7.708   -7.465  -44.193 1.00 15.48 ? 102 ALA A N   1 
ATOM   784  C  CA  . ALA A 1 102 ? 6.794   -6.842  -45.123 1.00 15.99 ? 102 ALA A CA  1 
ATOM   785  C  C   . ALA A 1 102 ? 5.487   -6.412  -44.459 1.00 15.42 ? 102 ALA A C   1 
ATOM   786  O  O   . ALA A 1 102 ? 5.043   -6.988  -43.394 1.00 16.24 ? 102 ALA A O   1 
ATOM   787  C  CB  . ALA A 1 102 ? 6.530   -7.814  -46.251 1.00 17.11 ? 102 ALA A CB  1 
ATOM   788  N  N   . ASP A 1 103 ? 4.764   -5.470  -45.063 1.00 16.14 ? 103 ASP A N   1 
ATOM   789  C  CA  . ASP A 1 103 ? 3.520   -4.995  -44.446 1.00 14.81 ? 103 ASP A CA  1 
ATOM   790  C  C   . ASP A 1 103 ? 2.376   -5.939  -44.243 1.00 16.78 ? 103 ASP A C   1 
ATOM   791  O  O   . ASP A 1 103 ? 1.437   -5.673  -43.452 1.00 21.39 ? 103 ASP A O   1 
ATOM   792  C  CB  . ASP A 1 103 ? 2.945   -3.813  -45.271 1.00 19.67 ? 103 ASP A CB  1 
ATOM   793  C  CG  . ASP A 1 103 ? 3.866   -2.632  -45.384 1.00 22.02 ? 103 ASP A CG  1 
ATOM   794  O  OD1 . ASP A 1 103 ? 4.836   -2.512  -44.609 1.00 21.90 ? 103 ASP A OD1 1 
ATOM   795  O  OD2 . ASP A 1 103 ? 3.583   -1.803  -46.273 1.00 22.85 ? 103 ASP A OD2 1 
ATOM   796  N  N   . ASP A 1 104 ? 2.358   -7.075  -44.915 1.00 16.79 ? 104 ASP A N   1 
ATOM   797  C  CA  . ASP A 1 104 ? 1.194   -7.977  -44.849 1.00 19.43 ? 104 ASP A CA  1 
ATOM   798  C  C   . ASP A 1 104 ? 1.124   -8.825  -43.571 1.00 18.29 ? 104 ASP A C   1 
ATOM   799  O  O   . ASP A 1 104 ? 0.095   -9.474  -43.310 1.00 21.57 ? 104 ASP A O   1 
ATOM   800  C  CB  . ASP A 1 104 ? 1.265   -8.974  -46.058 1.00 20.52 ? 104 ASP A CB  1 
ATOM   801  C  CG  . ASP A 1 104 ? 2.482   -9.845  -46.016 1.00 23.62 ? 104 ASP A CG  1 
ATOM   802  O  OD1 . ASP A 1 104 ? 3.564   -9.380  -46.448 1.00 29.06 ? 104 ASP A OD1 1 
ATOM   803  O  OD2 . ASP A 1 104 ? 2.334   -11.020 -45.552 1.00 27.89 ? 104 ASP A OD2 1 
ATOM   804  N  N   . HIS A 1 105 ? 2.205   -8.853  -42.774 1.00 19.60 ? 105 HIS A N   1 
ATOM   805  C  CA  . HIS A 1 105 ? 2.141   -9.599  -41.492 1.00 21.49 ? 105 HIS A CA  1 
ATOM   806  C  C   . HIS A 1 105 ? 3.255   -9.052  -40.612 1.00 22.13 ? 105 HIS A C   1 
ATOM   807  O  O   . HIS A 1 105 ? 4.173   -8.415  -41.048 1.00 25.71 ? 105 HIS A O   1 
ATOM   808  C  CB  . HIS A 1 105 ? 2.124   -11.155 -41.651 1.00 26.95 ? 105 HIS A CB  1 
ATOM   809  C  CG  . HIS A 1 105 ? 3.422   -11.770 -42.125 1.00 34.69 ? 105 HIS A CG  1 
ATOM   810  N  ND1 . HIS A 1 105 ? 3.643   -12.088 -43.431 1.00 42.92 ? 105 HIS A ND1 1 
ATOM   811  C  CD2 . HIS A 1 105 ? 4.548   -12.223 -41.419 1.00 42.73 ? 105 HIS A CD2 1 
ATOM   812  C  CE1 . HIS A 1 105 ? 4.854   -12.679 -43.568 1.00 43.58 ? 105 HIS A CE1 1 
ATOM   813  N  NE2 . HIS A 1 105 ? 5.424   -12.750 -42.338 1.00 43.63 ? 105 HIS A NE2 1 
ATOM   814  N  N   . GLY A 1 106 ? 3.134   -9.195  -39.305 1.00 21.44 ? 106 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 106 ? 4.113   -8.498  -38.486 1.00 16.91 ? 106 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 106 ? 3.580   -8.485  -37.076 1.00 16.16 ? 106 GLY A C   1 
ATOM   817  O  O   . GLY A 1 106 ? 4.325   -8.369  -36.104 1.00 18.82 ? 106 GLY A O   1 
ATOM   818  N  N   . SER A 1 107 ? 2.288   -8.594  -36.955 1.00 13.30 ? 107 SER A N   1 
ATOM   819  C  CA  . SER A 1 107 ? 1.731   -8.611  -35.546 1.00 13.29 ? 107 SER A CA  1 
ATOM   820  C  C   . SER A 1 107 ? 2.111   -9.943  -34.889 1.00 13.44 ? 107 SER A C   1 
ATOM   821  O  O   . SER A 1 107 ? 2.443   -10.959 -35.527 1.00 16.05 ? 107 SER A O   1 
ATOM   822  C  CB  . SER A 1 107 ? 0.211   -8.418  -35.527 1.00 13.05 ? 107 SER A CB  1 
ATOM   823  O  OG  . SER A 1 107 ? -0.468  -9.479  -36.180 1.00 12.97 ? 107 SER A OG  1 
ATOM   824  N  N   . GLU A 1 108 ? 2.057   -9.907  -33.553 1.00 11.87 ? 108 GLU A N   1 
ATOM   825  C  CA  . GLU A 1 108 ? 2.396   -11.124 -32.810 1.00 12.03 ? 108 GLU A CA  1 
ATOM   826  C  C   . GLU A 1 108 ? 1.100   -11.969 -32.598 1.00 12.71 ? 108 GLU A C   1 
ATOM   827  O  O   . GLU A 1 108 ? 1.055   -13.163 -32.946 1.00 14.85 ? 108 GLU A O   1 
ATOM   828  C  CB  . GLU A 1 108 ? 3.030   -10.687 -31.463 1.00 12.87 ? 108 GLU A CB  1 
ATOM   829  C  CG  . GLU A 1 108 ? 4.374   -10.085 -31.758 1.00 13.89 ? 108 GLU A CG  1 
ATOM   830  C  CD  . GLU A 1 108 ? 5.372   -10.340 -30.643 1.00 13.93 ? 108 GLU A CD  1 
ATOM   831  O  OE1 . GLU A 1 108 ? 5.012   -10.118 -29.469 1.00 12.89 ? 108 GLU A OE1 1 
ATOM   832  O  OE2 . GLU A 1 108 ? 6.508   -10.769 -30.941 1.00 11.42 ? 108 GLU A OE2 1 
ATOM   833  N  N   . HIS A 1 109 ? 0.029   -11.390 -32.025 1.00 11.49 ? 109 HIS A N   1 
ATOM   834  C  CA  . HIS A 1 109 ? -1.280  -12.052 -31.985 1.00 13.40 ? 109 HIS A CA  1 
ATOM   835  C  C   . HIS A 1 109 ? -1.907  -12.020 -33.369 1.00 14.82 ? 109 HIS A C   1 
ATOM   836  O  O   . HIS A 1 109 ? -1.656  -11.114 -34.165 1.00 12.40 ? 109 HIS A O   1 
ATOM   837  C  CB  . HIS A 1 109 ? -2.181  -11.350 -30.962 1.00 13.66 ? 109 HIS A CB  1 
ATOM   838  C  CG  . HIS A 1 109 ? -1.661  -11.513 -29.527 1.00 12.72 ? 109 HIS A CG  1 
ATOM   839  N  ND1 . HIS A 1 109 ? -0.780  -10.619 -28.927 1.00 12.70 ? 109 HIS A ND1 1 
ATOM   840  C  CD2 . HIS A 1 109 ? -1.903  -12.498 -28.626 1.00 13.98 ? 109 HIS A CD2 1 
ATOM   841  C  CE1 . HIS A 1 109 ? -0.472  -11.094 -27.686 1.00 12.14 ? 109 HIS A CE1 1 
ATOM   842  N  NE2 . HIS A 1 109 ? -1.161  -12.216 -27.488 1.00 14.69 ? 109 HIS A NE2 1 
ATOM   843  N  N   . ILE A 1 110 ? -2.676  -13.052 -33.626 1.00 14.96 ? 110 ILE A N   1 
ATOM   844  C  CA  . ILE A 1 110 ? -3.374  -13.226 -34.941 1.00 16.76 ? 110 ILE A CA  1 
ATOM   845  C  C   . ILE A 1 110 ? -4.816  -13.559 -34.615 1.00 17.80 ? 110 ILE A C   1 
ATOM   846  O  O   . ILE A 1 110 ? -5.094  -14.432 -33.765 1.00 19.05 ? 110 ILE A O   1 
ATOM   847  C  CB  . ILE A 1 110 ? -2.628  -14.317 -35.760 1.00 16.62 ? 110 ILE A CB  1 
ATOM   848  C  CG1 . ILE A 1 110 ? -1.163  -13.942 -36.051 1.00 19.28 ? 110 ILE A CG1 1 
ATOM   849  C  CG2 . ILE A 1 110 ? -3.394  -14.606 -37.081 1.00 17.84 ? 110 ILE A CG2 1 
ATOM   850  C  CD1 . ILE A 1 110 ? -0.315  -14.907 -36.907 1.00 20.02 ? 110 ILE A CD1 1 
ATOM   851  N  N   . VAL A 1 111 ? -5.756  -12.882 -35.280 1.00 18.69 ? 111 VAL A N   1 
ATOM   852  C  CA  . VAL A 1 111 ? -7.203  -13.005 -34.917 1.00 18.62 ? 111 VAL A CA  1 
ATOM   853  C  C   . VAL A 1 111 ? -7.945  -13.641 -36.083 1.00 18.73 ? 111 VAL A C   1 
ATOM   854  O  O   . VAL A 1 111 ? -7.964  -13.079 -37.140 1.00 21.49 ? 111 VAL A O   1 
ATOM   855  C  CB  . VAL A 1 111 ? -7.768  -11.635 -34.645 1.00 21.21 ? 111 VAL A CB  1 
ATOM   856  C  CG1 . VAL A 1 111 ? -9.284  -11.687 -34.300 1.00 22.46 ? 111 VAL A CG1 1 
ATOM   857  C  CG2 . VAL A 1 111 ? -6.960  -11.032 -33.481 1.00 21.27 ? 111 VAL A CG2 1 
ATOM   858  N  N   . ASP A 1 112 ? -8.433  -14.855 -35.810 1.00 19.41 ? 112 ASP A N   1 
ATOM   859  C  CA  . ASP A 1 112 ? -9.187  -15.625 -36.876 1.00 23.55 ? 112 ASP A CA  1 
ATOM   860  C  C   . ASP A 1 112 ? -8.366  -15.598 -38.160 1.00 24.62 ? 112 ASP A C   1 
ATOM   861  O  O   . ASP A 1 112 ? -8.925  -15.394 -39.260 1.00 26.02 ? 112 ASP A O   1 
ATOM   862  C  CB  . ASP A 1 112 ? -10.547 -14.988 -37.072 1.00 22.41 ? 112 ASP A CB  1 
ATOM   863  C  CG  . ASP A 1 112 ? -11.462 -15.207 -35.898 1.00 23.35 ? 112 ASP A CG  1 
ATOM   864  O  OD1 . ASP A 1 112 ? -11.420 -16.295 -35.250 1.00 27.77 ? 112 ASP A OD1 1 
ATOM   865  O  OD2 . ASP A 1 112 ? -12.295 -14.347 -35.685 1.00 26.01 ? 112 ASP A OD2 1 
ATOM   866  N  N   . GLY A 1 113 ? -7.068  -15.853 -38.001 1.00 21.51 ? 113 GLY A N   1 
ATOM   867  C  CA  . GLY A 1 113 ? -6.133  -15.997 -39.141 1.00 21.46 ? 113 GLY A CA  1 
ATOM   868  C  C   . GLY A 1 113 ? -5.698  -14.675 -39.766 1.00 22.75 ? 113 GLY A C   1 
ATOM   869  O  O   . GLY A 1 113 ? -4.805  -14.693 -40.603 1.00 22.83 ? 113 GLY A O   1 
ATOM   870  N  N   . VAL A 1 114 ? -6.218  -13.550 -39.294 1.00 21.92 ? 114 VAL A N   1 
ATOM   871  C  CA  . VAL A 1 114 ? -5.774  -12.190 -39.661 1.00 21.19 ? 114 VAL A CA  1 
ATOM   872  C  C   . VAL A 1 114 ? -4.529  -11.646 -38.926 1.00 20.59 ? 114 VAL A C   1 
ATOM   873  O  O   . VAL A 1 114 ? -4.551  -11.519 -37.705 1.00 21.36 ? 114 VAL A O   1 
ATOM   874  C  CB  . VAL A 1 114 ? -6.904  -11.167 -39.586 1.00 22.60 ? 114 VAL A CB  1 
ATOM   875  C  CG1 . VAL A 1 114 ? -6.468  -9.761  -40.033 1.00 24.47 ? 114 VAL A CG1 1 
ATOM   876  C  CG2 . VAL A 1 114 ? -8.077  -11.603 -40.483 1.00 25.61 ? 114 VAL A CG2 1 
ATOM   877  N  N   . SER A 1 115 ? -3.492  -11.340 -39.687 1.00 19.21 ? 115 SER A N   1 
ATOM   878  C  CA  . SER A 1 115 ? -2.292  -10.654 -39.150 1.00 18.62 ? 115 SER A CA  1 
ATOM   879  C  C   . SER A 1 115 ? -2.361  -9.183  -39.522 1.00 22.04 ? 115 SER A C   1 
ATOM   880  O  O   . SER A 1 115 ? -2.785  -8.748  -40.616 1.00 26.32 ? 115 SER A O   1 
ATOM   881  C  CB  . SER A 1 115 ? -0.983  -11.155 -39.744 1.00 23.88 ? 115 SER A CB  1 
ATOM   882  O  OG  . SER A 1 115 ? -0.624  -12.435 -39.278 1.00 26.31 ? 115 SER A OG  1 
ATOM   883  N  N   . TYR A 1 116 ? -1.912  -8.405  -38.595 1.00 19.31 ? 116 TYR A N   1 
ATOM   884  C  CA  . TYR A 1 116 ? -1.792  -6.964  -38.883 1.00 18.87 ? 116 TYR A CA  1 
ATOM   885  C  C   . TYR A 1 116 ? -0.369  -6.625  -39.264 1.00 16.23 ? 116 TYR A C   1 
ATOM   886  O  O   . TYR A 1 116 ? 0.484   -7.510  -39.151 1.00 16.18 ? 116 TYR A O   1 
ATOM   887  C  CB  . TYR A 1 116 ? -2.286  -6.187  -37.659 1.00 17.07 ? 116 TYR A CB  1 
ATOM   888  C  CG  . TYR A 1 116 ? -3.764  -6.381  -37.492 1.00 17.10 ? 116 TYR A CG  1 
ATOM   889  C  CD1 . TYR A 1 116 ? -4.680  -5.586  -38.220 1.00 17.61 ? 116 TYR A CD1 1 
ATOM   890  C  CD2 . TYR A 1 116 ? -4.235  -7.367  -36.638 1.00 17.63 ? 116 TYR A CD2 1 
ATOM   891  C  CE1 . TYR A 1 116 ? -6.057  -5.806  -38.005 1.00 21.27 ? 116 TYR A CE1 1 
ATOM   892  C  CE2 . TYR A 1 116 ? -5.552  -7.612  -36.459 1.00 20.88 ? 116 TYR A CE2 1 
ATOM   893  C  CZ  . TYR A 1 116 ? -6.443  -6.804  -37.153 1.00 23.48 ? 116 TYR A CZ  1 
ATOM   894  O  OH  . TYR A 1 116 ? -7.784  -7.111  -36.922 1.00 33.96 ? 116 TYR A OH  1 
ATOM   895  N  N   . ALA A 1 117 ? -0.061  -5.409  -39.678 1.00 15.40 ? 117 ALA A N   1 
ATOM   896  C  CA  . ALA A 1 117 ? 1.278   -5.010  -40.036 1.00 14.36 ? 117 ALA A CA  1 
ATOM   897  C  C   . ALA A 1 117 ? 2.253   -4.944  -38.835 1.00 13.00 ? 117 ALA A C   1 
ATOM   898  O  O   . ALA A 1 117 ? 3.458   -5.062  -38.963 1.00 15.34 ? 117 ALA A O   1 
ATOM   899  C  CB  . ALA A 1 117 ? 1.278   -3.629  -40.744 1.00 15.85 ? 117 ALA A CB  1 
ATOM   900  N  N   . ALA A 1 118 ? 1.667   -4.555  -37.703 1.00 13.18 ? 118 ALA A N   1 
ATOM   901  C  CA  . ALA A 1 118 ? 2.576   -4.391  -36.494 1.00 12.74 ? 118 ALA A CA  1 
ATOM   902  C  C   . ALA A 1 118 ? 1.677   -4.474  -35.257 1.00 12.67 ? 118 ALA A C   1 
ATOM   903  O  O   . ALA A 1 118 ? 0.451   -4.575  -35.322 1.00 11.83 ? 118 ALA A O   1 
ATOM   904  C  CB  . ALA A 1 118 ? 3.267   -3.040  -36.548 1.00 12.69 ? 118 ALA A CB  1 
ATOM   905  N  N   . GLU A 1 119 ? 2.360   -4.509  -34.067 1.00 11.35 ? 119 GLU A N   1 
ATOM   906  C  CA  . GLU A 1 119 ? 1.616   -4.635  -32.811 1.00 11.01 ? 119 GLU A CA  1 
ATOM   907  C  C   . GLU A 1 119 ? 2.449   -3.832  -31.785 1.00 9.27  ? 119 GLU A C   1 
ATOM   908  O  O   . GLU A 1 119 ? 3.625   -4.079  -31.546 1.00 10.99 ? 119 GLU A O   1 
ATOM   909  C  CB  . GLU A 1 119 ? 1.468   -6.087  -32.482 1.00 11.43 ? 119 GLU A CB  1 
ATOM   910  C  CG  . GLU A 1 119 ? 0.578   -6.311  -31.267 1.00 12.03 ? 119 GLU A CG  1 
ATOM   911  C  CD  . GLU A 1 119 ? 0.315   -7.752  -30.982 1.00 13.38 ? 119 GLU A CD  1 
ATOM   912  O  OE1 . GLU A 1 119 ? 0.118   -8.540  -31.960 1.00 12.65 ? 119 GLU A OE1 1 
ATOM   913  O  OE2 . GLU A 1 119 ? 0.221   -8.183  -29.825 1.00 12.93 ? 119 GLU A OE2 1 
ATOM   914  N  N   . LEU A 1 120 ? 1.732   -2.884  -31.130 1.00 10.77 ? 120 LEU A N   1 
ATOM   915  C  CA  . LEU A 1 120 ? 2.367   -2.116  -30.045 1.00 11.66 ? 120 LEU A CA  1 
ATOM   916  C  C   . LEU A 1 120 ? 2.016   -2.809  -28.716 1.00 9.77  ? 120 LEU A C   1 
ATOM   917  O  O   . LEU A 1 120 ? 0.885   -3.247  -28.480 1.00 10.88 ? 120 LEU A O   1 
ATOM   918  C  CB  . LEU A 1 120 ? 1.662   -0.728  -30.060 1.00 12.62 ? 120 LEU A CB  1 
ATOM   919  C  CG  . LEU A 1 120 ? 2.318   0.373   -29.139 1.00 13.95 ? 120 LEU A CG  1 
ATOM   920  C  CD1 . LEU A 1 120 ? 3.514   1.004   -29.738 1.00 13.16 ? 120 LEU A CD1 1 
ATOM   921  C  CD2 . LEU A 1 120 ? 1.235   1.410   -28.796 1.00 18.06 ? 120 LEU A CD2 1 
ATOM   922  N  N   . HIS A 1 121 ? 3.052   -2.848  -27.819 1.00 10.06 ? 121 HIS A N   1 
ATOM   923  C  CA  . HIS A 1 121 ? 2.845   -3.413  -26.502 1.00 10.23 ? 121 HIS A CA  1 
ATOM   924  C  C   . HIS A 1 121 ? 3.134   -2.356  -25.434 1.00 9.75  ? 121 HIS A C   1 
ATOM   925  O  O   . HIS A 1 121 ? 4.148   -1.633  -25.499 1.00 11.42 ? 121 HIS A O   1 
ATOM   926  C  CB  . HIS A 1 121 ? 3.794   -4.590  -26.300 1.00 10.29 ? 121 HIS A CB  1 
ATOM   927  C  CG  . HIS A 1 121 ? 3.367   -5.758  -27.085 1.00 10.72 ? 121 HIS A CG  1 
ATOM   928  N  ND1 . HIS A 1 121 ? 4.251   -6.798  -27.376 1.00 12.78 ? 121 HIS A ND1 1 
ATOM   929  C  CD2 . HIS A 1 121 ? 2.126   -6.090  -27.670 1.00 11.46 ? 121 HIS A CD2 1 
ATOM   930  C  CE1 . HIS A 1 121 ? 3.586   -7.733  -28.101 1.00 12.36 ? 121 HIS A CE1 1 
ATOM   931  N  NE2 . HIS A 1 121 ? 2.303   -7.314  -28.313 1.00 11.88 ? 121 HIS A NE2 1 
ATOM   932  N  N   . VAL A 1 122 ? 2.211   -2.321  -24.438 1.00 10.99 ? 122 VAL A N   1 
ATOM   933  C  CA  . VAL A 1 122 ? 2.327   -1.305  -23.331 1.00 11.13 ? 122 VAL A CA  1 
ATOM   934  C  C   . VAL A 1 122 ? 2.428   -2.195  -22.102 1.00 10.64 ? 122 VAL A C   1 
ATOM   935  O  O   . VAL A 1 122 ? 1.469   -2.878  -21.690 1.00 10.39 ? 122 VAL A O   1 
ATOM   936  C  CB  . VAL A 1 122 ? 1.091   -0.427  -23.329 1.00 12.45 ? 122 VAL A CB  1 
ATOM   937  C  CG1 . VAL A 1 122 ? 1.391   0.649   -22.301 1.00 12.59 ? 122 VAL A CG1 1 
ATOM   938  C  CG2 . VAL A 1 122 ? 0.834   0.278   -24.688 1.00 15.07 ? 122 VAL A CG2 1 
ATOM   939  N  N   . VAL A 1 123 ? 3.608   -2.154  -21.448 1.00 11.39 ? 123 VAL A N   1 
ATOM   940  C  CA  . VAL A 1 123 ? 3.959   -3.101  -20.369 1.00 10.54 ? 123 VAL A CA  1 
ATOM   941  C  C   . VAL A 1 123 ? 3.792   -2.396  -18.995 1.00 11.42 ? 123 VAL A C   1 
ATOM   942  O  O   . VAL A 1 123 ? 4.327   -1.300  -18.825 1.00 10.15 ? 123 VAL A O   1 
ATOM   943  C  CB  . VAL A 1 123 ? 5.427   -3.537  -20.560 1.00 11.07 ? 123 VAL A CB  1 
ATOM   944  C  CG1 . VAL A 1 123 ? 5.787   -4.519  -19.428 1.00 10.91 ? 123 VAL A CG1 1 
ATOM   945  C  CG2 . VAL A 1 123 ? 5.712   -4.255  -21.923 1.00 11.59 ? 123 VAL A CG2 1 
ATOM   946  N  N   . HIS A 1 124 ? 3.068   -3.103  -18.123 1.00 11.07 ? 124 HIS A N   1 
ATOM   947  C  CA  . HIS A 1 124 ? 2.765   -2.530  -16.786 1.00 11.03 ? 124 HIS A CA  1 
ATOM   948  C  C   . HIS A 1 124 ? 3.104   -3.627  -15.824 1.00 11.51 ? 124 HIS A C   1 
ATOM   949  O  O   . HIS A 1 124 ? 3.108   -4.814  -16.068 1.00 11.58 ? 124 HIS A O   1 
ATOM   950  C  CB  . HIS A 1 124 ? 1.241   -2.261  -16.624 1.00 11.37 ? 124 HIS A CB  1 
ATOM   951  C  CG  . HIS A 1 124 ? 0.667   -1.411  -17.688 1.00 13.62 ? 124 HIS A CG  1 
ATOM   952  N  ND1 . HIS A 1 124 ? 0.421   -1.937  -18.950 1.00 13.54 ? 124 HIS A ND1 1 
ATOM   953  C  CD2 . HIS A 1 124 ? 0.239   -0.111  -17.693 1.00 13.50 ? 124 HIS A CD2 1 
ATOM   954  C  CE1 . HIS A 1 124 ? -0.143  -0.944  -19.702 1.00 13.27 ? 124 HIS A CE1 1 
ATOM   955  N  NE2 . HIS A 1 124 ? -0.219  0.181   -18.960 1.00 15.30 ? 124 HIS A NE2 1 
ATOM   956  N  N   . TRP A 1 125 ? 3.328   -3.211  -14.540 1.00 12.49 ? 125 TRP A N   1 
ATOM   957  C  CA  . TRP A 1 125 ? 3.665   -4.220  -13.526 1.00 11.59 ? 125 TRP A CA  1 
ATOM   958  C  C   . TRP A 1 125 ? 2.956   -3.930  -12.140 1.00 12.49 ? 125 TRP A C   1 
ATOM   959  O  O   . TRP A 1 125 ? 2.629   -2.796  -11.785 1.00 13.03 ? 125 TRP A O   1 
ATOM   960  C  CB  . TRP A 1 125 ? 5.179   -4.384  -13.246 1.00 12.53 ? 125 TRP A CB  1 
ATOM   961  C  CG  . TRP A 1 125 ? 5.855   -3.087  -12.809 1.00 14.01 ? 125 TRP A CG  1 
ATOM   962  C  CD1 . TRP A 1 125 ? 6.254   -2.013  -13.609 1.00 13.67 ? 125 TRP A CD1 1 
ATOM   963  C  CD2 . TRP A 1 125 ? 6.276   -2.719  -11.443 1.00 14.62 ? 125 TRP A CD2 1 
ATOM   964  N  NE1 . TRP A 1 125 ? 6.830   -0.982  -12.851 1.00 13.68 ? 125 TRP A NE1 1 
ATOM   965  C  CE2 . TRP A 1 125 ? 6.878   -1.396  -11.549 1.00 13.95 ? 125 TRP A CE2 1 
ATOM   966  C  CE3 . TRP A 1 125 ? 6.135   -3.326  -10.193 1.00 14.95 ? 125 TRP A CE3 1 
ATOM   967  C  CZ2 . TRP A 1 125 ? 7.411   -0.712  -10.441 1.00 14.46 ? 125 TRP A CZ2 1 
ATOM   968  C  CZ3 . TRP A 1 125 ? 6.710   -2.643  -9.067  1.00 15.88 ? 125 TRP A CZ3 1 
ATOM   969  C  CH2 . TRP A 1 125 ? 7.286   -1.372  -9.216  1.00 14.67 ? 125 TRP A CH2 1 
ATOM   970  N  N   . ASN A 1 126 ? 2.686   -5.020  -11.431 1.00 12.81 ? 126 ASN A N   1 
ATOM   971  C  CA  . ASN A 1 126 ? 1.924   -4.973  -10.173 1.00 12.28 ? 126 ASN A CA  1 
ATOM   972  C  C   . ASN A 1 126 ? 2.716   -4.390  -8.989  1.00 13.70 ? 126 ASN A C   1 
ATOM   973  O  O   . ASN A 1 126 ? 3.351   -5.096  -8.320  1.00 14.17 ? 126 ASN A O   1 
ATOM   974  C  CB  . ASN A 1 126 ? 1.410   -6.363  -9.876  1.00 13.81 ? 126 ASN A CB  1 
ATOM   975  C  CG  . ASN A 1 126 ? 0.452   -6.396  -8.733  1.00 18.83 ? 126 ASN A CG  1 
ATOM   976  O  OD1 . ASN A 1 126 ? 0.286   -5.395  -8.000  1.00 17.53 ? 126 ASN A OD1 1 
ATOM   977  N  ND2 . ASN A 1 126 ? -0.259  -7.519  -8.648  1.00 20.64 ? 126 ASN A ND2 1 
ATOM   978  N  N   . SER A 1 127 ? 2.593   -3.080  -8.846  1.00 13.44 ? 127 SER A N   1 
ATOM   979  C  CA  . SER A 1 127 ? 3.378   -2.339  -7.780  1.00 14.16 ? 127 SER A CA  1 
ATOM   980  C  C   . SER A 1 127 ? 2.550   -2.374  -6.503  1.00 15.64 ? 127 SER A C   1 
ATOM   981  O  O   . SER A 1 127 ? 3.059   -1.935  -5.469  1.00 16.35 ? 127 SER A O   1 
ATOM   982  C  CB  . SER A 1 127 ? 3.601   -0.925  -8.208  1.00 16.21 ? 127 SER A CB  1 
ATOM   983  O  OG  . SER A 1 127 ? 2.408   -0.231  -8.548  1.00 17.28 ? 127 SER A OG  1 
ATOM   984  N  N   . ASP A 1 128 ? 1.349   -2.915  -6.540  1.00 15.35 ? 128 ASP A N   1 
ATOM   985  C  CA  . ASP A 1 128 ? 0.568   -3.086  -5.271  1.00 16.57 ? 128 ASP A CA  1 
ATOM   986  C  C   . ASP A 1 128 ? 1.123   -4.299  -4.485  1.00 17.81 ? 128 ASP A C   1 
ATOM   987  O  O   . ASP A 1 128 ? 0.966   -4.367  -3.247  1.00 20.65 ? 128 ASP A O   1 
ATOM   988  C  CB  . ASP A 1 128 ? -0.923  -3.282  -5.557  1.00 16.55 ? 128 ASP A CB  1 
ATOM   989  C  CG  . ASP A 1 128 ? -1.662  -1.981  -5.802  1.00 19.50 ? 128 ASP A CG  1 
ATOM   990  O  OD1 . ASP A 1 128 ? -2.865  -2.060  -6.134  1.00 20.74 ? 128 ASP A OD1 1 
ATOM   991  O  OD2 . ASP A 1 128 ? -1.057  -0.896  -5.657  1.00 20.99 ? 128 ASP A OD2 1 
ATOM   992  N  N   . LYS A 1 129 ? 1.773   -5.256  -5.155  1.00 16.77 ? 129 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 129 ? 2.352   -6.463  -4.559  1.00 15.08 ? 129 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 129 ? 3.841   -6.642  -4.584  1.00 17.91 ? 129 LYS A C   1 
ATOM   995  O  O   . LYS A 1 129 ? 4.419   -7.402  -3.747  1.00 19.29 ? 129 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 129 ? 1.728   -7.734  -5.193  1.00 18.34 ? 129 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 129 ? 0.261   -7.868  -4.941  1.00 21.88 ? 129 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 129 ? -0.332  -9.180  -5.409  1.00 21.61 ? 129 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 129 ? 0.401   -10.426 -4.900  1.00 22.29 ? 129 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 129 ? -0.297  -11.691 -5.223  1.00 22.84 ? 129 LYS A NZ  1 
ATOM   1001 N  N   . TYR A 1 130 ? 4.495   -6.171  -5.653  1.00 17.66 ? 130 TYR A N   1 
ATOM   1002 C  CA  . TYR A 1 130 ? 5.901   -6.420  -5.880  1.00 15.57 ? 130 TYR A CA  1 
ATOM   1003 C  C   . TYR A 1 130 ? 6.735   -5.153  -5.827  1.00 14.30 ? 130 TYR A C   1 
ATOM   1004 O  O   . TYR A 1 130 ? 6.213   -4.067  -6.089  1.00 15.82 ? 130 TYR A O   1 
ATOM   1005 C  CB  . TYR A 1 130 ? 6.027   -7.185  -7.291  1.00 16.72 ? 130 TYR A CB  1 
ATOM   1006 C  CG  . TYR A 1 130 ? 5.175   -8.409  -7.251  1.00 17.65 ? 130 TYR A CG  1 
ATOM   1007 C  CD1 . TYR A 1 130 ? 5.372   -9.370  -6.275  1.00 18.43 ? 130 TYR A CD1 1 
ATOM   1008 C  CD2 . TYR A 1 130 ? 4.076   -8.580  -8.114  1.00 17.24 ? 130 TYR A CD2 1 
ATOM   1009 C  CE1 . TYR A 1 130 ? 4.522   -10.458 -6.158  1.00 20.55 ? 130 TYR A CE1 1 
ATOM   1010 C  CE2 . TYR A 1 130 ? 3.277   -9.689  -8.113  1.00 16.90 ? 130 TYR A CE2 1 
ATOM   1011 C  CZ  . TYR A 1 130 ? 3.477   -10.645 -7.114  1.00 17.85 ? 130 TYR A CZ  1 
ATOM   1012 O  OH  . TYR A 1 130 ? 2.653   -11.741 -7.026  1.00 21.29 ? 130 TYR A OH  1 
ATOM   1013 N  N   . PRO A 1 131 ? 8.013   -5.295  -5.519  1.00 17.52 ? 131 PRO A N   1 
ATOM   1014 C  CA  . PRO A 1 131 ? 8.913   -4.161  -5.182  1.00 17.38 ? 131 PRO A CA  1 
ATOM   1015 C  C   . PRO A 1 131 ? 9.439   -3.500  -6.430  1.00 17.71 ? 131 PRO A C   1 
ATOM   1016 O  O   . PRO A 1 131 ? 9.876   -2.383  -6.376  1.00 19.40 ? 131 PRO A O   1 
ATOM   1017 C  CB  . PRO A 1 131 ? 10.070  -4.802  -4.420  1.00 18.49 ? 131 PRO A CB  1 
ATOM   1018 C  CG  . PRO A 1 131 ? 10.080  -6.214  -4.854  1.00 20.33 ? 131 PRO A CG  1 
ATOM   1019 C  CD  . PRO A 1 131 ? 8.586   -6.536  -5.062  1.00 16.88 ? 131 PRO A CD  1 
ATOM   1020 N  N   . SER A 1 132 ? 9.424   -4.231  -7.578  1.00 17.60 ? 132 SER A N   1 
ATOM   1021 C  CA  . SER A 1 132 ? 10.113  -3.697  -8.746  1.00 17.24 ? 132 SER A CA  1 
ATOM   1022 C  C   . SER A 1 132 ? 9.527   -4.472  -9.967  1.00 14.46 ? 132 SER A C   1 
ATOM   1023 O  O   . SER A 1 132 ? 8.974   -5.575  -9.800  1.00 16.26 ? 132 SER A O   1 
ATOM   1024 C  CB  . SER A 1 132 ? 11.614  -4.010  -8.751  1.00 18.24 ? 132 SER A CB  1 
ATOM   1025 O  OG  . SER A 1 132 ? 11.874  -5.396  -8.752  1.00 20.33 ? 132 SER A OG  1 
ATOM   1026 N  N   . PHE A 1 133 ? 9.725   -3.838  -11.129 1.00 18.92 ? 133 PHE A N   1 
ATOM   1027 C  CA  . PHE A 1 133 ? 9.329   -4.468  -12.397 1.00 18.93 ? 133 PHE A CA  1 
ATOM   1028 C  C   . PHE A 1 133 ? 10.074  -5.791  -12.602 1.00 21.15 ? 133 PHE A C   1 
ATOM   1029 O  O   . PHE A 1 133 ? 9.475   -6.822  -12.969 1.00 17.36 ? 133 PHE A O   1 
ATOM   1030 C  CB  . PHE A 1 133 ? 9.647   -3.524  -13.543 1.00 19.30 ? 133 PHE A CB  1 
ATOM   1031 C  CG  . PHE A 1 133 ? 9.597   -4.175  -14.907 1.00 23.38 ? 133 PHE A CG  1 
ATOM   1032 C  CD1 . PHE A 1 133 ? 8.358   -4.612  -15.468 1.00 24.98 ? 133 PHE A CD1 1 
ATOM   1033 C  CD2 . PHE A 1 133 ? 10.774  -4.266  -15.650 1.00 32.26 ? 133 PHE A CD2 1 
ATOM   1034 C  CE1 . PHE A 1 133 ? 8.355   -5.179  -16.748 1.00 22.63 ? 133 PHE A CE1 1 
ATOM   1035 C  CE2 . PHE A 1 133 ? 10.747  -4.861  -16.915 1.00 33.07 ? 133 PHE A CE2 1 
ATOM   1036 C  CZ  . PHE A 1 133 ? 9.515   -5.288  -17.453 1.00 30.75 ? 133 PHE A CZ  1 
ATOM   1037 N  N   . VAL A 1 134 ? 11.358  -5.814  -12.255 1.00 20.88 ? 134 VAL A N   1 
ATOM   1038 C  CA  . VAL A 1 134 ? 12.158  -6.982  -12.378 1.00 20.44 ? 134 VAL A CA  1 
ATOM   1039 C  C   . VAL A 1 134 ? 11.646  -8.144  -11.532 1.00 21.33 ? 134 VAL A C   1 
ATOM   1040 O  O   . VAL A 1 134 ? 11.590  -9.296  -11.979 1.00 23.92 ? 134 VAL A O   1 
ATOM   1041 C  CB  . VAL A 1 134 ? 13.659  -6.667  -12.024 1.00 24.12 ? 134 VAL A CB  1 
ATOM   1042 C  CG1 . VAL A 1 134 ? 14.393  -7.977  -11.741 1.00 32.63 ? 134 VAL A CG1 1 
ATOM   1043 C  CG2 . VAL A 1 134 ? 14.297  -5.903  -13.179 1.00 29.46 ? 134 VAL A CG2 1 
ATOM   1044 N  N   A GLU A 1 135 ? 11.251  -7.821  -10.295 0.50 18.62 ? 135 GLU A N   1 
ATOM   1045 N  N   B GLU A 1 135 ? 11.201  -7.898  -10.294 0.50 18.11 ? 135 GLU A N   1 
ATOM   1046 C  CA  A GLU A 1 135 ? 10.682  -8.845  -9.469  0.50 18.30 ? 135 GLU A CA  1 
ATOM   1047 C  CA  B GLU A 1 135 ? 10.665  -8.997  -9.480  0.50 17.67 ? 135 GLU A CA  1 
ATOM   1048 C  C   A GLU A 1 135 ? 9.372   -9.360  -10.041 0.50 19.05 ? 135 GLU A C   1 
ATOM   1049 C  C   B GLU A 1 135 ? 9.191   -9.412  -9.871  0.50 18.96 ? 135 GLU A C   1 
ATOM   1050 O  O   A GLU A 1 135 ? 9.272   -10.530 -10.209 0.50 16.60 ? 135 GLU A O   1 
ATOM   1051 O  O   B GLU A 1 135 ? 8.735   -10.550 -9.727  0.50 19.96 ? 135 GLU A O   1 
ATOM   1052 C  CB  A GLU A 1 135 ? 10.450  -8.366  -8.012  0.50 21.16 ? 135 GLU A CB  1 
ATOM   1053 C  CB  B GLU A 1 135 ? 10.789  -8.596  -7.972  0.50 19.27 ? 135 GLU A CB  1 
ATOM   1054 C  CG  A GLU A 1 135 ? 9.623   -9.372  -7.247  0.50 21.65 ? 135 GLU A CG  1 
ATOM   1055 C  CG  B GLU A 1 135 ? 10.541  -9.717  -7.017  0.50 19.17 ? 135 GLU A CG  1 
ATOM   1056 C  CD  A GLU A 1 135 ? 10.373  -10.666 -6.969  0.50 24.16 ? 135 GLU A CD  1 
ATOM   1057 C  CD  B GLU A 1 135 ? 9.157   -10.342 -7.164  0.50 15.84 ? 135 GLU A CD  1 
ATOM   1058 O  OE1 A GLU A 1 135 ? 11.608  -10.586 -6.874  0.50 27.79 ? 135 GLU A OE1 1 
ATOM   1059 O  OE1 B GLU A 1 135 ? 8.217   -9.541  -7.294  0.50 13.94 ? 135 GLU A OE1 1 
ATOM   1060 O  OE2 A GLU A 1 135 ? 9.741   -11.728 -6.852  0.50 25.02 ? 135 GLU A OE2 1 
ATOM   1061 O  OE2 B GLU A 1 135 ? 8.974   -11.607 -7.111  0.50 16.53 ? 135 GLU A OE2 1 
ATOM   1062 N  N   . ALA A 1 136 ? 8.451   -8.440  -10.372 1.00 17.26 ? 136 ALA A N   1 
ATOM   1063 C  CA  . ALA A 1 136 ? 7.072   -8.693  -10.803 1.00 15.24 ? 136 ALA A CA  1 
ATOM   1064 C  C   . ALA A 1 136 ? 7.082   -9.554  -12.080 1.00 15.89 ? 136 ALA A C   1 
ATOM   1065 O  O   . ALA A 1 136 ? 6.196   -10.391 -12.242 1.00 16.38 ? 136 ALA A O   1 
ATOM   1066 C  CB  . ALA A 1 136 ? 6.364   -7.376  -11.114 1.00 15.69 ? 136 ALA A CB  1 
ATOM   1067 N  N   . ALA A 1 137 ? 8.105   -9.381  -12.900 1.00 17.65 ? 137 ALA A N   1 
ATOM   1068 C  CA  . ALA A 1 137 ? 8.248   -10.282 -14.090 1.00 16.40 ? 137 ALA A CA  1 
ATOM   1069 C  C   . ALA A 1 137 ? 8.361   -11.747 -13.820 1.00 16.58 ? 137 ALA A C   1 
ATOM   1070 O  O   . ALA A 1 137 ? 8.137   -12.575 -14.780 1.00 16.80 ? 137 ALA A O   1 
ATOM   1071 C  CB  . ALA A 1 137 ? 9.419   -9.838  -14.966 1.00 18.12 ? 137 ALA A CB  1 
ATOM   1072 N  N   . HIS A 1 138 ? 8.628   -12.181 -12.576 1.00 19.11 ? 138 HIS A N   1 
ATOM   1073 C  CA  . HIS A 1 138 ? 8.717   -13.555 -12.164 1.00 21.10 ? 138 HIS A CA  1 
ATOM   1074 C  C   . HIS A 1 138 ? 7.518   -14.059 -11.368 1.00 19.58 ? 138 HIS A C   1 
ATOM   1075 O  O   . HIS A 1 138 ? 7.577   -15.121 -10.753 1.00 25.97 ? 138 HIS A O   1 
ATOM   1076 C  CB  . HIS A 1 138 ? 9.998   -13.746 -11.344 1.00 21.87 ? 138 HIS A CB  1 
ATOM   1077 C  CG  . HIS A 1 138 ? 11.236  -13.582 -12.153 1.00 22.11 ? 138 HIS A CG  1 
ATOM   1078 N  ND1 . HIS A 1 138 ? 11.903  -14.658 -12.698 1.00 25.93 ? 138 HIS A ND1 1 
ATOM   1079 C  CD2 . HIS A 1 138 ? 11.957  -12.449 -12.512 1.00 23.07 ? 138 HIS A CD2 1 
ATOM   1080 C  CE1 . HIS A 1 138 ? 12.968  -14.228 -13.371 1.00 25.00 ? 138 HIS A CE1 1 
ATOM   1081 N  NE2 . HIS A 1 138 ? 13.018  -12.884 -13.288 1.00 23.42 ? 138 HIS A NE2 1 
ATOM   1082 N  N   A GLU A 1 139 ? 6.404   -13.346 -11.396 0.50 19.60 ? 139 GLU A N   1 
ATOM   1083 N  N   B GLU A 1 139 ? 6.433   -13.273 -11.411 0.50 18.07 ? 139 GLU A N   1 
ATOM   1084 C  CA  A GLU A 1 139 ? 5.255   -13.860 -10.710 0.50 20.38 ? 139 GLU A CA  1 
ATOM   1085 C  CA  B GLU A 1 139 ? 5.203   -13.504 -10.683 0.50 17.83 ? 139 GLU A CA  1 
ATOM   1086 C  C   A GLU A 1 139 ? 4.102   -13.916 -11.651 0.50 18.66 ? 139 GLU A C   1 
ATOM   1087 C  C   B GLU A 1 139 ? 3.967   -13.769 -11.628 0.50 17.67 ? 139 GLU A C   1 
ATOM   1088 O  O   A GLU A 1 139 ? 4.073   -13.115 -12.562 0.50 16.75 ? 139 GLU A O   1 
ATOM   1089 O  O   B GLU A 1 139 ? 3.718   -12.966 -12.516 0.50 16.26 ? 139 GLU A O   1 
ATOM   1090 C  CB  A GLU A 1 139 ? 4.972   -12.945 -9.548  0.50 22.69 ? 139 GLU A CB  1 
ATOM   1091 C  CB  B GLU A 1 139 ? 4.967   -12.263 -9.796  0.50 17.41 ? 139 GLU A CB  1 
ATOM   1092 C  CG  A GLU A 1 139 ? 6.160   -12.933 -8.617  0.50 27.12 ? 139 GLU A CG  1 
ATOM   1093 C  CG  B GLU A 1 139 ? 6.054   -11.947 -8.725  0.50 16.60 ? 139 GLU A CG  1 
ATOM   1094 C  CD  A GLU A 1 139 ? 5.917   -13.912 -7.520  0.50 28.71 ? 139 GLU A CD  1 
ATOM   1095 C  CD  B GLU A 1 139 ? 6.223   -13.032 -7.648  0.50 19.51 ? 139 GLU A CD  1 
ATOM   1096 O  OE1 A GLU A 1 139 ? 6.665   -14.898 -7.333  0.50 32.05 ? 139 GLU A OE1 1 
ATOM   1097 O  OE1 B GLU A 1 139 ? 5.568   -14.087 -7.746  0.50 18.93 ? 139 GLU A OE1 1 
ATOM   1098 O  OE2 A GLU A 1 139 ? 4.901   -13.686 -6.872  0.50 32.03 ? 139 GLU A OE2 1 
ATOM   1099 O  OE2 B GLU A 1 139 ? 7.102   -12.845 -6.745  0.50 17.65 ? 139 GLU A OE2 1 
ATOM   1100 N  N   . PRO A 1 140 ? 3.159   -14.833 -11.436 1.00 19.83 ? 140 PRO A N   1 
ATOM   1101 C  CA  . PRO A 1 140 ? 1.995   -14.992 -12.362 1.00 18.09 ? 140 PRO A CA  1 
ATOM   1102 C  C   . PRO A 1 140 ? 1.109   -13.812 -12.582 1.00 19.22 ? 140 PRO A C   1 
ATOM   1103 O  O   . PRO A 1 140 ? 0.601   -13.638 -13.709 1.00 20.31 ? 140 PRO A O   1 
ATOM   1104 C  CB  . PRO A 1 140 ? 1.216   -16.226 -11.809 1.00 21.54 ? 140 PRO A CB  1 
ATOM   1105 C  CG  . PRO A 1 140 ? 2.298   -16.986 -11.126 1.00 26.42 ? 140 PRO A CG  1 
ATOM   1106 C  CD  . PRO A 1 140 ? 3.223   -15.956 -10.488 1.00 24.60 ? 140 PRO A CD  1 
ATOM   1107 N  N   . ASP A 1 141 ? 0.866   -13.039 -11.519 1.00 15.16 ? 141 ASP A N   1 
ATOM   1108 C  CA  . ASP A 1 141 ? 0.068   -11.851 -11.596 1.00 16.72 ? 141 ASP A CA  1 
ATOM   1109 C  C   . ASP A 1 141 ? 0.992   -10.623 -11.606 1.00 15.20 ? 141 ASP A C   1 
ATOM   1110 O  O   . ASP A 1 141 ? 0.489   -9.525  -11.357 1.00 15.44 ? 141 ASP A O   1 
ATOM   1111 C  CB  . ASP A 1 141 ? -0.831  -11.750 -10.379 1.00 17.71 ? 141 ASP A CB  1 
ATOM   1112 C  CG  . ASP A 1 141 ? -0.030  -11.775 -9.055  1.00 16.79 ? 141 ASP A CG  1 
ATOM   1113 O  OD1 . ASP A 1 141 ? 1.128   -12.125 -9.014  1.00 18.38 ? 141 ASP A OD1 1 
ATOM   1114 O  OD2 . ASP A 1 141 ? -0.669  -11.451 -8.008  1.00 21.40 ? 141 ASP A OD2 1 
ATOM   1115 N  N   . GLY A 1 142 ? 2.262   -10.804 -12.023 1.00 15.31 ? 142 GLY A N   1 
ATOM   1116 C  CA  . GLY A 1 142 ? 3.186   -9.680  -11.921 1.00 13.38 ? 142 GLY A CA  1 
ATOM   1117 C  C   . GLY A 1 142 ? 2.962   -8.574  -13.010 1.00 13.16 ? 142 GLY A C   1 
ATOM   1118 O  O   . GLY A 1 142 ? 3.151   -7.369  -12.801 1.00 12.98 ? 142 GLY A O   1 
ATOM   1119 N  N   . LEU A 1 143 ? 2.725   -9.020  -14.290 1.00 12.69 ? 143 LEU A N   1 
ATOM   1120 C  CA  . LEU A 1 143 ? 2.724   -8.079  -15.422 1.00 13.86 ? 143 LEU A CA  1 
ATOM   1121 C  C   . LEU A 1 143 ? 1.366   -7.983  -16.133 1.00 11.51 ? 143 LEU A C   1 
ATOM   1122 O  O   . LEU A 1 143 ? 0.601   -8.985  -16.164 1.00 14.89 ? 143 LEU A O   1 
ATOM   1123 C  CB  . LEU A 1 143 ? 3.806   -8.472  -16.467 1.00 13.44 ? 143 LEU A CB  1 
ATOM   1124 C  CG  . LEU A 1 143 ? 5.210   -8.621  -15.954 1.00 12.85 ? 143 LEU A CG  1 
ATOM   1125 C  CD1 . LEU A 1 143 ? 6.199   -8.998  -17.100 1.00 12.07 ? 143 LEU A CD1 1 
ATOM   1126 C  CD2 . LEU A 1 143 ? 5.747   -7.310  -15.286 1.00 14.38 ? 143 LEU A CD2 1 
ATOM   1127 N  N   . ALA A 1 144 ? 1.120   -6.851  -16.690 1.00 12.17 ? 144 ALA A N   1 
ATOM   1128 C  CA  . ALA A 1 144 ? -0.088  -6.719  -17.596 1.00 13.74 ? 144 ALA A CA  1 
ATOM   1129 C  C   . ALA A 1 144 ? 0.330   -5.950  -18.803 1.00 13.27 ? 144 ALA A C   1 
ATOM   1130 O  O   . ALA A 1 144 ? 0.963   -4.872  -18.738 1.00 12.85 ? 144 ALA A O   1 
ATOM   1131 C  CB  . ALA A 1 144 ? -1.204  -5.927  -16.919 1.00 13.68 ? 144 ALA A CB  1 
ATOM   1132 N  N   . VAL A 1 145 ? 0.016   -6.530  -19.994 1.00 14.06 ? 145 VAL A N   1 
ATOM   1133 C  CA  . VAL A 1 145 ? 0.532   -5.945  -21.252 1.00 12.12 ? 145 VAL A CA  1 
ATOM   1134 C  C   . VAL A 1 145 ? -0.649  -5.626  -22.128 1.00 12.48 ? 145 VAL A C   1 
ATOM   1135 O  O   . VAL A 1 145 ? -1.462  -6.556  -22.321 1.00 12.60 ? 145 VAL A O   1 
ATOM   1136 C  CB  . VAL A 1 145 ? 1.567   -6.839  -22.003 1.00 12.75 ? 145 VAL A CB  1 
ATOM   1137 C  CG1 . VAL A 1 145 ? 1.997   -6.043  -23.228 1.00 11.62 ? 145 VAL A CG1 1 
ATOM   1138 C  CG2 . VAL A 1 145 ? 2.833   -7.181  -21.149 1.00 13.85 ? 145 VAL A CG2 1 
ATOM   1139 N  N   . LEU A 1 146 ? -0.753  -4.399  -22.635 1.00 12.49 ? 146 LEU A N   1 
ATOM   1140 C  CA  . LEU A 1 146 ? -1.865  -4.030  -23.490 1.00 12.97 ? 146 LEU A CA  1 
ATOM   1141 C  C   . LEU A 1 146 ? -1.276  -4.218  -24.889 1.00 15.12 ? 146 LEU A C   1 
ATOM   1142 O  O   . LEU A 1 146 ? -0.165  -3.705  -25.129 1.00 14.53 ? 146 LEU A O   1 
ATOM   1143 C  CB  . LEU A 1 146 ? -2.253  -2.572  -23.260 1.00 17.84 ? 146 LEU A CB  1 
ATOM   1144 C  CG  . LEU A 1 146 ? -3.741  -2.219  -23.185 1.00 28.23 ? 146 LEU A CG  1 
ATOM   1145 C  CD1 . LEU A 1 146 ? -4.475  -3.083  -22.170 1.00 26.64 ? 146 LEU A CD1 1 
ATOM   1146 C  CD2 . LEU A 1 146 ? -3.921  -0.742  -22.870 1.00 23.57 ? 146 LEU A CD2 1 
ATOM   1147 N  N   . GLY A 1 147 ? -2.003  -4.912  -25.767 1.00 14.24 ? 147 GLY A N   1 
ATOM   1148 C  CA  . GLY A 1 147 ? -1.545  -5.004  -27.183 1.00 14.26 ? 147 GLY A CA  1 
ATOM   1149 C  C   . GLY A 1 147 ? -2.502  -4.191  -28.072 1.00 14.24 ? 147 GLY A C   1 
ATOM   1150 O  O   . GLY A 1 147 ? -3.710  -4.386  -27.880 1.00 15.28 ? 147 GLY A O   1 
ATOM   1151 N  N   . VAL A 1 148 ? -1.950  -3.468  -29.018 1.00 11.76 ? 148 VAL A N   1 
ATOM   1152 C  CA  . VAL A 1 148 ? -2.767  -2.634  -29.963 1.00 11.32 ? 148 VAL A CA  1 
ATOM   1153 C  C   . VAL A 1 148 ? -2.218  -3.064  -31.343 1.00 11.95 ? 148 VAL A C   1 
ATOM   1154 O  O   . VAL A 1 148 ? -1.011  -2.985  -31.625 1.00 12.32 ? 148 VAL A O   1 
ATOM   1155 C  CB  . VAL A 1 148 ? -2.513  -1.167  -29.754 1.00 14.24 ? 148 VAL A CB  1 
ATOM   1156 C  CG1 . VAL A 1 148 ? -3.292  -0.389  -30.838 1.00 17.45 ? 148 VAL A CG1 1 
ATOM   1157 C  CG2 . VAL A 1 148 ? -2.992  -0.747  -28.344 1.00 17.10 ? 148 VAL A CG2 1 
ATOM   1158 N  N   . PHE A 1 149 ? -3.144  -3.542  -32.226 1.00 11.37 ? 149 PHE A N   1 
ATOM   1159 C  CA  . PHE A 1 149 ? -2.715  -3.779  -33.591 1.00 12.17 ? 149 PHE A CA  1 
ATOM   1160 C  C   . PHE A 1 149 ? -2.589  -2.566  -34.453 1.00 12.45 ? 149 PHE A C   1 
ATOM   1161 O  O   . PHE A 1 149 ? -3.348  -1.594  -34.243 1.00 13.55 ? 149 PHE A O   1 
ATOM   1162 C  CB  . PHE A 1 149 ? -3.828  -4.649  -34.225 1.00 12.10 ? 149 PHE A CB  1 
ATOM   1163 C  CG  . PHE A 1 149 ? -3.970  -5.985  -33.561 1.00 11.36 ? 149 PHE A CG  1 
ATOM   1164 C  CD1 . PHE A 1 149 ? -2.860  -6.912  -33.531 1.00 13.63 ? 149 PHE A CD1 1 
ATOM   1165 C  CD2 . PHE A 1 149 ? -5.226  -6.390  -32.987 1.00 11.91 ? 149 PHE A CD2 1 
ATOM   1166 C  CE1 . PHE A 1 149 ? -3.047  -8.172  -33.002 1.00 12.89 ? 149 PHE A CE1 1 
ATOM   1167 C  CE2 . PHE A 1 149 ? -5.400  -7.640  -32.438 1.00 12.44 ? 149 PHE A CE2 1 
ATOM   1168 C  CZ  . PHE A 1 149 ? -4.306  -8.537  -32.402 1.00 12.36 ? 149 PHE A CZ  1 
ATOM   1169 N  N   . LEU A 1 150 ? -1.625  -2.600  -35.363 1.00 11.73 ? 150 LEU A N   1 
ATOM   1170 C  CA  . LEU A 1 150 ? -1.484  -1.552  -36.374 1.00 13.42 ? 150 LEU A CA  1 
ATOM   1171 C  C   . LEU A 1 150 ? -1.780  -2.152  -37.749 1.00 14.17 ? 150 LEU A C   1 
ATOM   1172 O  O   . LEU A 1 150 ? -1.137  -3.064  -38.163 1.00 15.14 ? 150 LEU A O   1 
ATOM   1173 C  CB  . LEU A 1 150 ? -0.079  -0.921  -36.358 1.00 14.69 ? 150 LEU A CB  1 
ATOM   1174 C  CG  . LEU A 1 150 ? 0.227   -0.005  -35.143 1.00 16.00 ? 150 LEU A CG  1 
ATOM   1175 C  CD1 . LEU A 1 150 ? 0.595   -0.864  -33.882 1.00 17.08 ? 150 LEU A CD1 1 
ATOM   1176 C  CD2 . LEU A 1 150 ? 1.423   0.944   -35.381 1.00 17.89 ? 150 LEU A CD2 1 
ATOM   1177 N  N   . GLN A 1 151 ? -2.714  -1.481  -38.444 1.00 15.15 ? 151 GLN A N   1 
ATOM   1178 C  CA  . GLN A 1 151 ? -3.072  -1.897  -39.819 1.00 16.40 ? 151 GLN A CA  1 
ATOM   1179 C  C   . GLN A 1 151 ? -2.571  -0.845  -40.811 1.00 17.64 ? 151 GLN A C   1 
ATOM   1180 O  O   . GLN A 1 151 ? -2.460  0.360   -40.485 1.00 18.95 ? 151 GLN A O   1 
ATOM   1181 C  CB  . GLN A 1 151 ? -4.566  -2.076  -39.883 1.00 17.42 ? 151 GLN A CB  1 
ATOM   1182 C  CG  . GLN A 1 151 ? -5.300  -0.731  -39.879 1.00 20.99 ? 151 GLN A CG  1 
ATOM   1183 C  CD  . GLN A 1 151 ? -6.813  -0.880  -39.881 1.00 24.45 ? 151 GLN A CD  1 
ATOM   1184 O  OE1 . GLN A 1 151 ? -7.393  -1.973  -40.099 1.00 23.10 ? 151 GLN A OE1 1 
ATOM   1185 N  NE2 . GLN A 1 151 ? -7.476  0.282   -39.754 1.00 26.44 ? 151 GLN A NE2 1 
ATOM   1186 N  N   . ILE A 1 152 ? -2.177  -1.283  -42.024 1.00 17.62 ? 152 ILE A N   1 
ATOM   1187 C  CA  . ILE A 1 152 ? -1.783  -0.257  -42.995 1.00 18.92 ? 152 ILE A CA  1 
ATOM   1188 C  C   . ILE A 1 152 ? -2.960  0.625   -43.353 1.00 22.95 ? 152 ILE A C   1 
ATOM   1189 O  O   . ILE A 1 152 ? -4.074  0.140   -43.586 1.00 22.61 ? 152 ILE A O   1 
ATOM   1190 C  CB  . ILE A 1 152 ? -1.208  -0.922  -44.277 1.00 18.66 ? 152 ILE A CB  1 
ATOM   1191 C  CG1 . ILE A 1 152 ? 0.031   -1.729  -43.901 1.00 19.75 ? 152 ILE A CG1 1 
ATOM   1192 C  CG2 . ILE A 1 152 ? -0.736  0.123   -45.294 1.00 19.89 ? 152 ILE A CG2 1 
ATOM   1193 C  CD1 . ILE A 1 152 ? 1.219   -0.885  -43.474 1.00 19.88 ? 152 ILE A CD1 1 
ATOM   1194 N  N   . GLY A 1 153 ? -2.750  1.917   -43.224 1.00 20.93 ? 153 GLY A N   1 
ATOM   1195 C  CA  . GLY A 1 153 ? -3.818  2.882   -43.571 1.00 22.06 ? 153 GLY A CA  1 
ATOM   1196 C  C   . GLY A 1 153 ? -3.169  4.268   -43.653 1.00 19.28 ? 153 GLY A C   1 
ATOM   1197 O  O   . GLY A 1 153 ? -1.963  4.442   -43.937 1.00 24.30 ? 153 GLY A O   1 
ATOM   1198 N  N   . GLU A 1 154 ? -4.018  5.248   -43.423 1.00 27.54 ? 154 GLU A N   1 
ATOM   1199 C  CA  . GLU A 1 154 ? -3.541  6.654   -43.558 1.00 27.95 ? 154 GLU A CA  1 
ATOM   1200 C  C   . GLU A 1 154 ? -2.445  6.877   -42.514 1.00 25.91 ? 154 GLU A C   1 
ATOM   1201 O  O   . GLU A 1 154 ? -2.493  6.230   -41.433 1.00 26.04 ? 154 GLU A O   1 
ATOM   1202 C  CB  . GLU A 1 154 ? -4.702  7.650   -43.340 1.00 34.78 ? 154 GLU A CB  1 
ATOM   1203 C  CG  . GLU A 1 154 ? -4.974  7.933   -41.860 1.00 37.25 ? 154 GLU A CG  1 
ATOM   1204 C  CD  . GLU A 1 154 ? -5.907  9.098   -41.599 1.00 36.48 ? 154 GLU A CD  1 
ATOM   1205 O  OE1 . GLU A 1 154 ? -5.447  10.143  -41.094 1.00 46.27 ? 154 GLU A OE1 1 
ATOM   1206 O  OE2 . GLU A 1 154 ? -7.087  8.960   -41.900 1.00 40.21 ? 154 GLU A OE2 1 
ATOM   1207 N  N   . PRO A 1 155 ? -1.473  7.788   -42.776 1.00 22.36 ? 155 PRO A N   1 
ATOM   1208 C  CA  . PRO A 1 155 ? -0.417  7.914   -41.768 1.00 22.37 ? 155 PRO A CA  1 
ATOM   1209 C  C   . PRO A 1 155 ? -0.983  8.379   -40.443 1.00 22.73 ? 155 PRO A C   1 
ATOM   1210 O  O   . PRO A 1 155 ? -1.974  9.084   -40.389 1.00 21.74 ? 155 PRO A O   1 
ATOM   1211 C  CB  . PRO A 1 155 ? 0.567   8.929   -42.351 1.00 23.23 ? 155 PRO A CB  1 
ATOM   1212 C  CG  . PRO A 1 155 ? -0.110  9.442   -43.588 1.00 21.37 ? 155 PRO A CG  1 
ATOM   1213 C  CD  . PRO A 1 155 ? -1.114  8.454   -44.033 1.00 20.84 ? 155 PRO A CD  1 
ATOM   1214 N  N   . ASN A 1 156 ? -0.304  7.955   -39.376 1.00 21.35 ? 156 ASN A N   1 
ATOM   1215 C  CA  . ASN A 1 156 ? -0.733  8.236   -38.035 1.00 22.50 ? 156 ASN A CA  1 
ATOM   1216 C  C   . ASN A 1 156 ? 0.115   9.298   -37.375 1.00 21.08 ? 156 ASN A C   1 
ATOM   1217 O  O   . ASN A 1 156 ? 1.328   9.093   -37.044 1.00 20.33 ? 156 ASN A O   1 
ATOM   1218 C  CB  . ASN A 1 156 ? -0.697  6.942   -37.230 1.00 22.89 ? 156 ASN A CB  1 
ATOM   1219 C  CG  . ASN A 1 156 ? -1.413  7.062   -35.892 1.00 23.71 ? 156 ASN A CG  1 
ATOM   1220 O  OD1 . ASN A 1 156 ? -1.593  8.198   -35.287 1.00 24.80 ? 156 ASN A OD1 1 
ATOM   1221 N  ND2 . ASN A 1 156 ? -1.904  5.897   -35.407 1.00 21.01 ? 156 ASN A ND2 1 
ATOM   1222 N  N   . SER A 1 157 ? -0.494  10.482  -37.272 1.00 24.30 ? 157 SER A N   1 
ATOM   1223 C  CA  . SER A 1 157 ? 0.259   11.648  -36.738 1.00 23.44 ? 157 SER A CA  1 
ATOM   1224 C  C   . SER A 1 157 ? 0.771   11.387  -35.329 1.00 25.20 ? 157 SER A C   1 
ATOM   1225 O  O   . SER A 1 157 ? 1.752   11.978  -34.924 1.00 23.84 ? 157 SER A O   1 
ATOM   1226 C  CB  . SER A 1 157 ? -0.595  12.945  -36.757 1.00 26.02 ? 157 SER A CB  1 
ATOM   1227 O  OG  . SER A 1 157 ? -1.761  12.717  -36.015 1.00 30.81 ? 157 SER A OG  1 
ATOM   1228 N  N   . GLN A 1 158 ? 0.129   10.466  -34.595 1.00 24.79 ? 158 GLN A N   1 
ATOM   1229 C  CA  . GLN A 1 158 ? 0.531   10.207  -33.200 1.00 26.59 ? 158 GLN A CA  1 
ATOM   1230 C  C   . GLN A 1 158 ? 1.778   9.414   -33.101 1.00 25.12 ? 158 GLN A C   1 
ATOM   1231 O  O   . GLN A 1 158 ? 2.292   9.187   -32.001 1.00 27.37 ? 158 GLN A O   1 
ATOM   1232 C  CB  . GLN A 1 158 ? -0.589  9.554   -32.408 1.00 28.35 ? 158 GLN A CB  1 
ATOM   1233 C  CG  . GLN A 1 158 ? -1.889  10.307  -32.561 1.00 30.66 ? 158 GLN A CG  1 
ATOM   1234 C  CD  . GLN A 1 158 ? -1.911  11.659  -31.863 1.00 39.74 ? 158 GLN A CD  1 
ATOM   1235 O  OE1 . GLN A 1 158 ? -2.774  12.488  -32.146 1.00 44.92 ? 158 GLN A OE1 1 
ATOM   1236 N  NE2 . GLN A 1 158 ? -0.996  11.866  -30.912 1.00 36.50 ? 158 GLN A NE2 1 
ATOM   1237 N  N   . LEU A 1 159 ? 2.291   8.916   -34.223 1.00 22.75 ? 159 LEU A N   1 
ATOM   1238 C  CA  . LEU A 1 159 ? 3.580   8.211   -34.177 1.00 22.30 ? 159 LEU A CA  1 
ATOM   1239 C  C   . LEU A 1 159 ? 4.745   9.155   -34.436 1.00 22.24 ? 159 LEU A C   1 
ATOM   1240 O  O   . LEU A 1 159 ? 5.866   8.685   -34.430 1.00 20.55 ? 159 LEU A O   1 
ATOM   1241 C  CB  . LEU A 1 159 ? 3.652   7.107   -35.237 1.00 23.70 ? 159 LEU A CB  1 
ATOM   1242 C  CG  . LEU A 1 159 ? 2.773   5.875   -35.020 1.00 22.64 ? 159 LEU A CG  1 
ATOM   1243 C  CD1 . LEU A 1 159 ? 2.626   5.043   -36.286 1.00 22.54 ? 159 LEU A CD1 1 
ATOM   1244 C  CD2 . LEU A 1 159 ? 3.194   4.964   -33.842 1.00 24.26 ? 159 LEU A CD2 1 
ATOM   1245 N  N   . GLN A 1 160 ? 4.520   10.457  -34.714 1.00 22.16 ? 160 GLN A N   1 
ATOM   1246 C  CA  . GLN A 1 160 ? 5.610   11.336  -35.098 1.00 22.36 ? 160 GLN A CA  1 
ATOM   1247 C  C   . GLN A 1 160 ? 6.703   11.533  -34.019 1.00 20.16 ? 160 GLN A C   1 
ATOM   1248 O  O   . GLN A 1 160 ? 7.868   11.589  -34.349 1.00 22.07 ? 160 GLN A O   1 
ATOM   1249 C  CB  . GLN A 1 160 ? 5.087   12.739  -35.600 1.00 25.23 ? 160 GLN A CB  1 
ATOM   1250 C  CG  . GLN A 1 160 ? 6.195   13.647  -36.112 1.00 24.28 ? 160 GLN A CG  1 
ATOM   1251 C  CD  . GLN A 1 160 ? 5.883   15.137  -36.003 1.00 29.21 ? 160 GLN A CD  1 
ATOM   1252 O  OE1 . GLN A 1 160 ? 4.706   15.565  -35.926 1.00 32.36 ? 160 GLN A OE1 1 
ATOM   1253 N  NE2 . GLN A 1 160 ? 6.947   15.958  -36.049 1.00 29.69 ? 160 GLN A NE2 1 
ATOM   1254 N  N   . LYS A 1 161 ? 6.282   11.648  -32.786 1.00 23.29 ? 161 LYS A N   1 
ATOM   1255 C  CA  . LYS A 1 161 ? 7.282   11.853  -31.772 1.00 22.72 ? 161 LYS A CA  1 
ATOM   1256 C  C   . LYS A 1 161 ? 8.238   10.647  -31.794 1.00 22.64 ? 161 LYS A C   1 
ATOM   1257 O  O   . LYS A 1 161 ? 9.469   10.820  -31.749 1.00 22.67 ? 161 LYS A O   1 
ATOM   1258 C  CB  . LYS A 1 161 ? 6.644   12.081  -30.423 1.00 24.83 ? 161 LYS A CB  1 
ATOM   1259 C  CG  . LYS A 1 161 ? 7.640   12.575  -29.345 1.00 23.52 ? 161 LYS A CG  1 
ATOM   1260 C  CD  . LYS A 1 161 ? 6.931   12.547  -27.977 1.00 22.06 ? 161 LYS A CD  1 
ATOM   1261 C  CE  . LYS A 1 161 ? 7.941   12.790  -26.870 1.00 23.08 ? 161 LYS A CE  1 
ATOM   1262 N  NZ  . LYS A 1 161 ? 8.495   14.230  -26.937 1.00 26.24 ? 161 LYS A NZ  1 
ATOM   1263 N  N   . ILE A 1 162 ? 7.682   9.442   -31.959 1.00 22.79 ? 162 ILE A N   1 
ATOM   1264 C  CA  . ILE A 1 162 ? 8.584   8.285   -32.040 1.00 17.87 ? 162 ILE A CA  1 
ATOM   1265 C  C   . ILE A 1 162 ? 9.460   8.274   -33.310 1.00 18.88 ? 162 ILE A C   1 
ATOM   1266 O  O   . ILE A 1 162 ? 10.672  8.101   -33.281 1.00 19.95 ? 162 ILE A O   1 
ATOM   1267 C  CB  . ILE A 1 162 ? 7.765   6.946   -31.992 1.00 16.03 ? 162 ILE A CB  1 
ATOM   1268 C  CG1 . ILE A 1 162 ? 7.090   6.819   -30.619 1.00 16.72 ? 162 ILE A CG1 1 
ATOM   1269 C  CG2 . ILE A 1 162 ? 8.743   5.758   -32.168 1.00 14.13 ? 162 ILE A CG2 1 
ATOM   1270 C  CD1 . ILE A 1 162 ? 6.029   5.702   -30.528 1.00 16.13 ? 162 ILE A CD1 1 
ATOM   1271 N  N   . THR A 1 163 ? 8.796   8.383   -34.468 1.00 19.17 ? 163 THR A N   1 
ATOM   1272 C  CA  . THR A 1 163 ? 9.544   8.300   -35.708 1.00 21.73 ? 163 THR A CA  1 
ATOM   1273 C  C   . THR A 1 163 ? 10.640  9.357   -35.839 1.00 18.53 ? 163 THR A C   1 
ATOM   1274 O  O   . THR A 1 163 ? 11.682  9.052   -36.382 1.00 21.39 ? 163 THR A O   1 
ATOM   1275 C  CB  . THR A 1 163 ? 8.641   8.317   -36.953 1.00 22.39 ? 163 THR A CB  1 
ATOM   1276 O  OG1 . THR A 1 163 ? 7.800   9.481   -36.935 1.00 23.52 ? 163 THR A OG1 1 
ATOM   1277 C  CG2 . THR A 1 163 ? 7.759   6.991   -36.917 1.00 23.71 ? 163 THR A CG2 1 
ATOM   1278 N  N   . ASP A 1 164 ? 10.373  10.562  -35.355 1.00 21.69 ? 164 ASP A N   1 
ATOM   1279 C  CA  . ASP A 1 164 ? 11.395  11.620  -35.329 1.00 20.65 ? 164 ASP A CA  1 
ATOM   1280 C  C   . ASP A 1 164 ? 12.679  11.286  -34.594 1.00 24.48 ? 164 ASP A C   1 
ATOM   1281 O  O   . ASP A 1 164 ? 13.743  11.874  -34.862 1.00 25.61 ? 164 ASP A O   1 
ATOM   1282 C  CB  . ASP A 1 164 ? 10.817  12.876  -34.691 1.00 24.62 ? 164 ASP A CB  1 
ATOM   1283 C  CG  . ASP A 1 164 ? 9.958   13.701  -35.639 1.00 28.87 ? 164 ASP A CG  1 
ATOM   1284 O  OD1 . ASP A 1 164 ? 9.867   13.356  -36.857 1.00 30.13 ? 164 ASP A OD1 1 
ATOM   1285 O  OD2 . ASP A 1 164 ? 9.383   14.695  -35.137 1.00 29.02 ? 164 ASP A OD2 1 
ATOM   1286 N  N   . THR A 1 165 ? 12.615  10.325  -33.670 1.00 22.68 ? 165 THR A N   1 
ATOM   1287 C  CA  . THR A 1 165 ? 13.797  9.972   -32.916 1.00 21.12 ? 165 THR A CA  1 
ATOM   1288 C  C   . THR A 1 165 ? 14.620  8.849   -33.455 1.00 20.94 ? 165 THR A C   1 
ATOM   1289 O  O   . THR A 1 165 ? 15.702  8.568   -32.973 1.00 22.23 ? 165 THR A O   1 
ATOM   1290 C  CB  . THR A 1 165 ? 13.474  9.550   -31.431 1.00 20.93 ? 165 THR A CB  1 
ATOM   1291 O  OG1 . THR A 1 165 ? 12.785  8.274   -31.468 1.00 20.79 ? 165 THR A OG1 1 
ATOM   1292 C  CG2 . THR A 1 165 ? 12.647  10.613  -30.791 1.00 22.70 ? 165 THR A CG2 1 
ATOM   1293 N  N   . LEU A 1 166 ? 14.103  8.130   -34.472 1.00 18.32 ? 166 LEU A N   1 
ATOM   1294 C  CA  . LEU A 1 166 ? 14.770  6.906   -34.890 1.00 18.23 ? 166 LEU A CA  1 
ATOM   1295 C  C   . LEU A 1 166 ? 16.186  7.034   -35.427 1.00 21.14 ? 166 LEU A C   1 
ATOM   1296 O  O   . LEU A 1 166 ? 17.035  6.178   -35.156 1.00 21.91 ? 166 LEU A O   1 
ATOM   1297 C  CB  . LEU A 1 166 ? 13.912  6.070   -35.856 1.00 20.30 ? 166 LEU A CB  1 
ATOM   1298 C  CG  . LEU A 1 166 ? 12.502  5.706   -35.339 1.00 19.79 ? 166 LEU A CG  1 
ATOM   1299 C  CD1 . LEU A 1 166 ? 11.601  5.172   -36.526 1.00 20.04 ? 166 LEU A CD1 1 
ATOM   1300 C  CD2 . LEU A 1 166 ? 12.621  4.816   -34.100 1.00 20.52 ? 166 LEU A CD2 1 
ATOM   1301 N  N   . ASP A 1 167 ? 16.463  8.112   -36.150 1.00 21.80 ? 167 ASP A N   1 
ATOM   1302 C  CA  . ASP A 1 167 ? 17.856  8.280   -36.640 1.00 23.71 ? 167 ASP A CA  1 
ATOM   1303 C  C   . ASP A 1 167 ? 18.832  8.401   -35.451 1.00 24.21 ? 167 ASP A C   1 
ATOM   1304 O  O   . ASP A 1 167 ? 19.908  7.773   -35.445 1.00 26.13 ? 167 ASP A O   1 
ATOM   1305 C  CB  . ASP A 1 167 ? 17.935  9.534   -37.534 1.00 29.03 ? 167 ASP A CB  1 
ATOM   1306 C  CG  . ASP A 1 167 ? 17.349  9.281   -38.923 1.00 35.80 ? 167 ASP A CG  1 
ATOM   1307 O  OD1 . ASP A 1 167 ? 17.224  8.098   -39.365 1.00 40.53 ? 167 ASP A OD1 1 
ATOM   1308 O  OD2 . ASP A 1 167 ? 16.998  10.271  -39.584 1.00 41.35 ? 167 ASP A OD2 1 
ATOM   1309 N  N   . SER A 1 168 ? 18.373  9.098   -34.408 1.00 22.26 ? 168 SER A N   1 
ATOM   1310 C  CA  . SER A 1 168 ? 19.188  9.254   -33.195 1.00 22.93 ? 168 SER A CA  1 
ATOM   1311 C  C   . SER A 1 168 ? 19.423  7.964   -32.440 1.00 22.17 ? 168 SER A C   1 
ATOM   1312 O  O   . SER A 1 168 ? 20.393  7.872   -31.643 1.00 24.38 ? 168 SER A O   1 
ATOM   1313 C  CB  . SER A 1 168 ? 18.645  10.339  -32.301 1.00 23.96 ? 168 SER A CB  1 
ATOM   1314 O  OG  . SER A 1 168 ? 17.487  9.941   -31.554 1.00 27.74 ? 168 SER A OG  1 
ATOM   1315 N  N   . ILE A 1 169 ? 18.550  6.980   -32.669 1.00 22.06 ? 169 ILE A N   1 
ATOM   1316 C  CA  . ILE A 1 169 ? 18.745  5.707   -31.941 1.00 19.06 ? 169 ILE A CA  1 
ATOM   1317 C  C   . ILE A 1 169 ? 18.965  4.552   -32.879 1.00 19.25 ? 169 ILE A C   1 
ATOM   1318 O  O   . ILE A 1 169 ? 18.597  3.399   -32.614 1.00 19.25 ? 169 ILE A O   1 
ATOM   1319 C  CB  . ILE A 1 169 ? 17.647  5.414   -30.893 1.00 20.76 ? 169 ILE A CB  1 
ATOM   1320 C  CG1 . ILE A 1 169 ? 16.272  5.309   -31.562 1.00 20.54 ? 169 ILE A CG1 1 
ATOM   1321 C  CG2 . ILE A 1 169 ? 17.651  6.514   -29.808 1.00 19.14 ? 169 ILE A CG2 1 
ATOM   1322 C  CD1 . ILE A 1 169 ? 15.265  4.610   -30.637 1.00 20.98 ? 169 ILE A CD1 1 
ATOM   1323 N  N   . LYS A 1 170 ? 19.646  4.846   -34.016 1.00 18.85 ? 170 LYS A N   1 
ATOM   1324 C  CA  . LYS A 1 170 ? 19.824  3.814   -35.012 1.00 19.94 ? 170 LYS A CA  1 
ATOM   1325 C  C   . LYS A 1 170 ? 20.569  2.588   -34.537 1.00 17.50 ? 170 LYS A C   1 
ATOM   1326 O  O   . LYS A 1 170 ? 20.172  1.428   -34.840 1.00 21.71 ? 170 LYS A O   1 
ATOM   1327 C  CB  . LYS A 1 170 ? 20.543  4.427   -36.255 1.00 24.34 ? 170 LYS A CB  1 
ATOM   1328 C  CG  . LYS A 1 170 ? 20.713  3.443   -37.414 1.00 28.87 ? 170 LYS A CG  1 
ATOM   1329 C  CD  . LYS A 1 170 ? 21.362  4.123   -38.640 1.00 33.59 ? 170 LYS A CD  1 
ATOM   1330 C  CE  . LYS A 1 170 ? 21.383  3.175   -39.865 1.00 37.35 ? 170 LYS A CE  1 
ATOM   1331 N  NZ  . LYS A 1 170 ? 20.019  2.840   -40.478 1.00 34.60 ? 170 LYS A NZ  1 
ATOM   1332 N  N   . GLU A 1 171 ? 21.619  2.781   -33.701 1.00 20.52 ? 171 GLU A N   1 
ATOM   1333 C  CA  . GLU A 1 171 ? 22.433  1.629   -33.304 1.00 22.11 ? 171 GLU A CA  1 
ATOM   1334 C  C   . GLU A 1 171 ? 21.916  1.142   -31.963 1.00 20.73 ? 171 GLU A C   1 
ATOM   1335 O  O   . GLU A 1 171 ? 21.410  1.983   -31.165 1.00 19.02 ? 171 GLU A O   1 
ATOM   1336 C  CB  . GLU A 1 171 ? 23.908  2.029   -33.146 1.00 24.19 ? 171 GLU A CB  1 
ATOM   1337 C  CG  . GLU A 1 171 ? 24.626  2.522   -34.406 1.00 27.52 ? 171 GLU A CG  1 
ATOM   1338 C  CD  . GLU A 1 171 ? 24.242  3.934   -34.878 1.00 32.18 ? 171 GLU A CD  1 
ATOM   1339 O  OE1 . GLU A 1 171 ? 24.453  4.166   -36.097 1.00 45.54 ? 171 GLU A OE1 1 
ATOM   1340 O  OE2 . GLU A 1 171 ? 23.689  4.823   -34.141 1.00 32.68 ? 171 GLU A OE2 1 
ATOM   1341 N  N   . LYS A 1 172 ? 22.042  -0.154  -31.757 1.00 21.44 ? 172 LYS A N   1 
ATOM   1342 C  CA  . LYS A 1 172 ? 21.755  -0.777  -30.451 1.00 18.67 ? 172 LYS A CA  1 
ATOM   1343 C  C   . LYS A 1 172 ? 22.497  -0.037  -29.331 1.00 19.36 ? 172 LYS A C   1 
ATOM   1344 O  O   . LYS A 1 172 ? 23.698  0.166   -29.416 1.00 19.89 ? 172 LYS A O   1 
ATOM   1345 C  CB  . LYS A 1 172 ? 22.099  -2.242  -30.506 1.00 17.32 ? 172 LYS A CB  1 
ATOM   1346 C  CG  . LYS A 1 172 ? 21.925  -2.991  -29.188 1.00 18.46 ? 172 LYS A CG  1 
ATOM   1347 C  CD  . LYS A 1 172 ? 22.265  -4.475  -29.314 1.00 22.92 ? 172 LYS A CD  1 
ATOM   1348 C  CE  . LYS A 1 172 ? 22.046  -5.119  -27.950 1.00 24.46 ? 172 LYS A CE  1 
ATOM   1349 N  NZ  . LYS A 1 172 ? 22.311  -6.596  -28.040 1.00 32.68 ? 172 LYS A NZ  1 
ATOM   1350 N  N   . GLY A 1 173 ? 21.745  0.290   -28.269 1.00 18.48 ? 173 GLY A N   1 
ATOM   1351 C  CA  . GLY A 1 173 ? 22.345  0.890   -27.046 1.00 18.80 ? 173 GLY A CA  1 
ATOM   1352 C  C   . GLY A 1 173 ? 22.171  2.402   -27.034 1.00 19.75 ? 173 GLY A C   1 
ATOM   1353 O  O   . GLY A 1 173 ? 22.296  3.049   -25.972 1.00 22.60 ? 173 GLY A O   1 
ATOM   1354 N  N   . LYS A 1 174 ? 21.859  3.029   -28.171 1.00 17.92 ? 174 LYS A N   1 
ATOM   1355 C  CA  . LYS A 1 174 ? 21.633  4.465   -28.202 1.00 17.75 ? 174 LYS A CA  1 
ATOM   1356 C  C   . LYS A 1 174 ? 20.366  4.851   -27.462 1.00 19.08 ? 174 LYS A C   1 
ATOM   1357 O  O   . LYS A 1 174 ? 19.395  4.078   -27.496 1.00 17.77 ? 174 LYS A O   1 
ATOM   1358 C  CB  . LYS A 1 174 ? 21.532  4.953   -29.610 1.00 19.59 ? 174 LYS A CB  1 
ATOM   1359 C  CG  . LYS A 1 174 ? 22.904  4.841   -30.320 1.00 24.64 ? 174 LYS A CG  1 
ATOM   1360 C  CD  . LYS A 1 174 ? 23.484  6.239   -30.365 1.00 33.99 ? 174 LYS A CD  1 
ATOM   1361 C  CE  . LYS A 1 174 ? 24.944  6.210   -30.816 1.00 40.60 ? 174 LYS A CE  1 
ATOM   1362 N  NZ  . LYS A 1 174 ? 24.982  5.881   -32.264 1.00 45.79 ? 174 LYS A NZ  1 
ATOM   1363 N  N   . GLN A 1 175 ? 20.393  5.996   -26.809 1.00 17.55 ? 175 GLN A N   1 
ATOM   1364 C  CA  . GLN A 1 175 ? 19.203  6.518   -26.136 1.00 18.18 ? 175 GLN A CA  1 
ATOM   1365 C  C   . GLN A 1 175 ? 19.057  8.012   -26.309 1.00 20.54 ? 175 GLN A C   1 
ATOM   1366 O  O   . GLN A 1 175 ? 20.028  8.715   -26.664 1.00 22.29 ? 175 GLN A O   1 
ATOM   1367 C  CB  . GLN A 1 175 ? 19.095  6.104   -24.667 1.00 21.02 ? 175 GLN A CB  1 
ATOM   1368 C  CG  . GLN A 1 175 ? 19.949  6.995   -23.770 1.00 22.32 ? 175 GLN A CG  1 
ATOM   1369 C  CD  . GLN A 1 175 ? 19.992  6.479   -22.364 1.00 21.31 ? 175 GLN A CD  1 
ATOM   1370 O  OE1 . GLN A 1 175 ? 20.302  5.330   -22.100 1.00 25.92 ? 175 GLN A OE1 1 
ATOM   1371 N  NE2 . GLN A 1 175 ? 19.720  7.386   -21.411 1.00 22.52 ? 175 GLN A NE2 1 
ATOM   1372 N  N   A THR A 1 176 ? 17.834  8.475   -26.137 0.50 17.66 ? 176 THR A N   1 
ATOM   1373 N  N   B THR A 1 176 ? 17.848  8.537   -26.151 0.50 18.00 ? 176 THR A N   1 
ATOM   1374 C  CA  A THR A 1 176 ? 17.504  9.858   -26.343 0.50 19.29 ? 176 THR A CA  1 
ATOM   1375 C  CA  B THR A 1 176 ? 17.653  10.003  -26.152 0.50 20.30 ? 176 THR A CA  1 
ATOM   1376 C  C   A THR A 1 176 ? 16.449  10.303  -25.367 0.50 19.05 ? 176 THR A C   1 
ATOM   1377 C  C   B THR A 1 176 ? 16.492  10.432  -25.291 0.50 19.75 ? 176 THR A C   1 
ATOM   1378 O  O   A THR A 1 176 ? 15.529  9.555   -25.051 0.50 18.33 ? 176 THR A O   1 
ATOM   1379 O  O   B THR A 1 176 ? 15.566  9.642   -25.043 0.50 19.08 ? 176 THR A O   1 
ATOM   1380 C  CB  A THR A 1 176 ? 16.982  10.019  -27.774 0.50 21.28 ? 176 THR A CB  1 
ATOM   1381 C  CB  B THR A 1 176 ? 17.505  10.550  -27.592 0.50 22.71 ? 176 THR A CB  1 
ATOM   1382 O  OG1 A THR A 1 176 ? 18.074  9.824   -28.702 0.50 19.35 ? 176 THR A OG1 1 
ATOM   1383 O  OG1 B THR A 1 176 ? 17.733  11.959  -27.616 0.50 23.14 ? 176 THR A OG1 1 
ATOM   1384 C  CG2 A THR A 1 176 ? 16.386  11.406  -27.934 0.50 21.08 ? 176 THR A CG2 1 
ATOM   1385 C  CG2 B THR A 1 176 ? 16.116  10.219  -28.191 0.50 22.25 ? 176 THR A CG2 1 
ATOM   1386 N  N   A ARG A 1 177 ? 16.537  11.529  -24.892 0.50 18.08 ? 177 ARG A N   1 
ATOM   1387 N  N   B ARG A 1 177 ? 16.497  11.674  -24.820 0.50 18.91 ? 177 ARG A N   1 
ATOM   1388 C  CA  A ARG A 1 177 ? 15.526  12.094  -24.044 0.50 16.74 ? 177 ARG A CA  1 
ATOM   1389 C  CA  B ARG A 1 177 ? 15.426  12.125  -23.976 0.50 17.66 ? 177 ARG A CA  1 
ATOM   1390 C  C   A ARG A 1 177 ? 14.100  12.043  -24.674 0.50 18.67 ? 177 ARG A C   1 
ATOM   1391 C  C   B ARG A 1 177 ? 14.110  11.910  -24.721 0.50 19.29 ? 177 ARG A C   1 
ATOM   1392 O  O   A ARG A 1 177 ? 13.939  12.479  -25.808 0.50 19.20 ? 177 ARG A O   1 
ATOM   1393 O  O   B ARG A 1 177 ? 14.045  12.050  -25.977 0.50 19.61 ? 177 ARG A O   1 
ATOM   1394 C  CB  A ARG A 1 177 ? 15.907  13.551  -23.797 0.50 16.03 ? 177 ARG A CB  1 
ATOM   1395 C  CB  B ARG A 1 177 ? 15.556  13.608  -23.547 0.50 17.54 ? 177 ARG A CB  1 
ATOM   1396 C  CG  A ARG A 1 177 ? 14.738  14.364  -23.280 0.50 18.39 ? 177 ARG A CG  1 
ATOM   1397 C  CG  B ARG A 1 177 ? 14.562  13.990  -22.413 0.50 18.05 ? 177 ARG A CG  1 
ATOM   1398 C  CD  A ARG A 1 177 ? 15.142  15.730  -22.722 0.50 18.65 ? 177 ARG A CD  1 
ATOM   1399 C  CD  B ARG A 1 177 ? 14.868  15.309  -21.659 0.50 20.42 ? 177 ARG A CD  1 
ATOM   1400 N  NE  A ARG A 1 177 ? 14.234  16.057  -21.633 0.50 21.77 ? 177 ARG A NE  1 
ATOM   1401 N  NE  B ARG A 1 177 ? 13.796  15.883  -20.794 0.50 21.51 ? 177 ARG A NE  1 
ATOM   1402 C  CZ  A ARG A 1 177 ? 13.526  17.172  -21.511 0.50 24.45 ? 177 ARG A CZ  1 
ATOM   1403 C  CZ  B ARG A 1 177 ? 13.392  15.453  -19.583 0.50 23.14 ? 177 ARG A CZ  1 
ATOM   1404 N  NH1 A ARG A 1 177 ? 13.641  18.119  -22.413 0.50 31.71 ? 177 ARG A NH1 1 
ATOM   1405 N  NH1 B ARG A 1 177 ? 13.895  14.384  -19.040 0.50 21.11 ? 177 ARG A NH1 1 
ATOM   1406 N  NH2 A ARG A 1 177 ? 12.725  17.346  -20.446 0.50 28.53 ? 177 ARG A NH2 1 
ATOM   1407 N  NH2 B ARG A 1 177 ? 12.432  16.113  -18.907 0.50 26.84 ? 177 ARG A NH2 1 
ATOM   1408 N  N   . PHE A 1 178 ? 13.086  11.537  -23.959 1.00 16.59 ? 178 PHE A N   1 
ATOM   1409 C  CA  . PHE A 1 178 ? 11.759  11.353  -24.576 1.00 17.33 ? 178 PHE A CA  1 
ATOM   1410 C  C   . PHE A 1 178 ? 10.726  11.570  -23.527 1.00 16.00 ? 178 PHE A C   1 
ATOM   1411 O  O   . PHE A 1 178 ? 10.406  10.681  -22.734 1.00 18.72 ? 178 PHE A O   1 
ATOM   1412 C  CB  . PHE A 1 178 ? 11.695  9.903   -25.149 1.00 17.07 ? 178 PHE A CB  1 
ATOM   1413 C  CG  . PHE A 1 178 ? 10.582  9.707   -26.158 1.00 16.82 ? 178 PHE A CG  1 
ATOM   1414 C  CD1 . PHE A 1 178 ? 10.696  10.087  -27.467 1.00 16.30 ? 178 PHE A CD1 1 
ATOM   1415 C  CD2 . PHE A 1 178 ? 9.396   9.130   -25.753 1.00 14.28 ? 178 PHE A CD2 1 
ATOM   1416 C  CE1 . PHE A 1 178 ? 9.691   9.814   -28.361 1.00 16.78 ? 178 PHE A CE1 1 
ATOM   1417 C  CE2 . PHE A 1 178 ? 8.336   8.895   -26.644 1.00 14.88 ? 178 PHE A CE2 1 
ATOM   1418 C  CZ  . PHE A 1 178 ? 8.527   9.203   -27.952 1.00 15.06 ? 178 PHE A CZ  1 
ATOM   1419 N  N   . THR A 1 179 ? 10.238  12.802  -23.445 1.00 19.62 ? 179 THR A N   1 
ATOM   1420 C  CA  . THR A 1 179 ? 9.189   13.073  -22.471 1.00 19.93 ? 179 THR A CA  1 
ATOM   1421 C  C   . THR A 1 179 ? 8.042   13.832  -23.090 1.00 19.34 ? 179 THR A C   1 
ATOM   1422 O  O   . THR A 1 179 ? 8.067   14.183  -24.258 1.00 22.09 ? 179 THR A O   1 
ATOM   1423 C  CB  . THR A 1 179 ? 9.700   13.715  -21.187 1.00 23.09 ? 179 THR A CB  1 
ATOM   1424 O  OG1 . THR A 1 179 ? 8.658   13.637  -20.170 1.00 22.86 ? 179 THR A OG1 1 
ATOM   1425 C  CG2 . THR A 1 179 ? 10.122  15.137  -21.494 1.00 25.21 ? 179 THR A CG2 1 
ATOM   1426 N  N   . ASN A 1 180 ? 6.967   14.011  -22.314 1.00 19.77 ? 180 ASN A N   1 
ATOM   1427 C  CA  . ASN A 1 180 ? 5.764   14.662  -22.826 1.00 22.68 ? 180 ASN A CA  1 
ATOM   1428 C  C   . ASN A 1 180 ? 5.193   13.904  -23.988 1.00 22.70 ? 180 ASN A C   1 
ATOM   1429 O  O   . ASN A 1 180 ? 4.885   14.412  -25.057 1.00 22.87 ? 180 ASN A O   1 
ATOM   1430 C  CB  . ASN A 1 180 ? 5.978   16.184  -23.052 1.00 25.31 ? 180 ASN A CB  1 
ATOM   1431 C  CG  . ASN A 1 180 ? 6.329   16.867  -21.708 1.00 31.09 ? 180 ASN A CG  1 
ATOM   1432 O  OD1 . ASN A 1 180 ? 5.620   16.702  -20.693 1.00 32.64 ? 180 ASN A OD1 1 
ATOM   1433 N  ND2 . ASN A 1 180 ? 7.464   17.583  -21.688 1.00 36.90 ? 180 ASN A ND2 1 
ATOM   1434 N  N   . PHE A 1 181 ? 5.101   12.606  -23.740 1.00 18.72 ? 181 PHE A N   1 
ATOM   1435 C  CA  . PHE A 1 181 ? 4.641   11.675  -24.757 1.00 18.27 ? 181 PHE A CA  1 
ATOM   1436 C  C   . PHE A 1 181 ? 3.178   11.369  -24.546 1.00 17.50 ? 181 PHE A C   1 
ATOM   1437 O  O   . PHE A 1 181 ? 2.802   10.815  -23.556 1.00 18.45 ? 181 PHE A O   1 
ATOM   1438 C  CB  . PHE A 1 181 ? 5.491   10.379  -24.696 1.00 20.49 ? 181 PHE A CB  1 
ATOM   1439 C  CG  . PHE A 1 181 ? 4.998   9.204   -25.586 1.00 18.93 ? 181 PHE A CG  1 
ATOM   1440 C  CD1 . PHE A 1 181 ? 4.648   9.362   -26.924 1.00 18.74 ? 181 PHE A CD1 1 
ATOM   1441 C  CD2 . PHE A 1 181 ? 4.999   7.930   -25.042 1.00 18.54 ? 181 PHE A CD2 1 
ATOM   1442 C  CE1 . PHE A 1 181 ? 4.224   8.216   -27.682 1.00 18.48 ? 181 PHE A CE1 1 
ATOM   1443 C  CE2 . PHE A 1 181 ? 4.662   6.807   -25.769 1.00 20.25 ? 181 PHE A CE2 1 
ATOM   1444 C  CZ  . PHE A 1 181 ? 4.250   6.954   -27.091 1.00 18.61 ? 181 PHE A CZ  1 
ATOM   1445 N  N   . ASP A 1 182 ? 2.357   11.641  -25.577 1.00 17.77 ? 182 ASP A N   1 
ATOM   1446 C  CA  . ASP A 1 182 ? 0.903   11.281  -25.479 1.00 18.33 ? 182 ASP A CA  1 
ATOM   1447 C  C   . ASP A 1 182 ? 0.536   9.836   -25.923 1.00 18.20 ? 182 ASP A C   1 
ATOM   1448 O  O   . ASP A 1 182 ? 0.115   9.581   -27.084 1.00 20.02 ? 182 ASP A O   1 
ATOM   1449 C  CB  . ASP A 1 182 ? 0.144   12.234  -26.386 1.00 17.39 ? 182 ASP A CB  1 
ATOM   1450 C  CG  . ASP A 1 182 ? -1.358  12.085  -26.317 1.00 20.71 ? 182 ASP A CG  1 
ATOM   1451 O  OD1 . ASP A 1 182 ? -1.865  11.277  -25.516 1.00 21.80 ? 182 ASP A OD1 1 
ATOM   1452 O  OD2 . ASP A 1 182 ? -2.037  12.802  -27.085 1.00 24.35 ? 182 ASP A OD2 1 
ATOM   1453 N  N   . LEU A 1 183 ? 0.751   8.930   -24.998 1.00 18.31 ? 183 LEU A N   1 
ATOM   1454 C  CA  . LEU A 1 183 ? 0.469   7.495   -25.227 1.00 16.09 ? 183 LEU A CA  1 
ATOM   1455 C  C   . LEU A 1 183 ? -1.008  7.211   -25.435 1.00 20.68 ? 183 LEU A C   1 
ATOM   1456 O  O   . LEU A 1 183 ? -1.433  6.408   -26.296 1.00 18.18 ? 183 LEU A O   1 
ATOM   1457 C  CB  . LEU A 1 183 ? 1.063   6.685   -24.042 1.00 16.74 ? 183 LEU A CB  1 
ATOM   1458 C  CG  . LEU A 1 183 ? 0.845   5.138   -24.111 1.00 15.36 ? 183 LEU A CG  1 
ATOM   1459 C  CD1 . LEU A 1 183 ? 1.352   4.532   -25.405 1.00 16.36 ? 183 LEU A CD1 1 
ATOM   1460 C  CD2 . LEU A 1 183 ? 1.521   4.498   -22.905 1.00 16.15 ? 183 LEU A CD2 1 
ATOM   1461 N  N   . LEU A 1 184 ? -1.834  7.949   -24.705 1.00 20.44 ? 184 LEU A N   1 
ATOM   1462 C  CA  . LEU A 1 184 ? -3.239  7.672   -24.643 1.00 20.88 ? 184 LEU A CA  1 
ATOM   1463 C  C   . LEU A 1 184 ? -3.816  7.784   -26.038 1.00 20.08 ? 184 LEU A C   1 
ATOM   1464 O  O   . LEU A 1 184 ? -4.624  6.963   -26.416 1.00 22.50 ? 184 LEU A O   1 
ATOM   1465 C  CB  . LEU A 1 184 ? -3.875  8.699   -23.666 1.00 20.17 ? 184 LEU A CB  1 
ATOM   1466 C  CG  . LEU A 1 184 ? -4.953  8.389   -22.660 1.00 31.86 ? 184 LEU A CG  1 
ATOM   1467 C  CD1 . LEU A 1 184 ? -5.922  9.593   -22.791 1.00 24.37 ? 184 LEU A CD1 1 
ATOM   1468 C  CD2 . LEU A 1 184 ? -5.686  7.078   -22.786 1.00 27.23 ? 184 LEU A CD2 1 
ATOM   1469 N  N   A SER A 1 185 ? -3.317  8.746   -26.828 0.50 19.90 ? 185 SER A N   1 
ATOM   1470 N  N   B SER A 1 185 ? -3.338  8.749   -26.835 0.50 22.01 ? 185 SER A N   1 
ATOM   1471 C  CA  A SER A 1 185 ? -3.755  9.001   -28.190 0.50 19.73 ? 185 SER A CA  1 
ATOM   1472 C  CA  B SER A 1 185 ? -3.811  8.962   -28.195 0.50 23.40 ? 185 SER A CA  1 
ATOM   1473 C  C   A SER A 1 185 ? -3.242  8.063   -29.271 0.50 18.73 ? 185 SER A C   1 
ATOM   1474 C  C   B SER A 1 185 ? -3.397  7.926   -29.213 0.50 21.74 ? 185 SER A C   1 
ATOM   1475 O  O   A SER A 1 185 ? -3.576  8.247   -30.449 0.50 18.77 ? 185 SER A O   1 
ATOM   1476 O  O   B SER A 1 185 ? -3.923  7.922   -30.312 0.50 23.98 ? 185 SER A O   1 
ATOM   1477 C  CB  A SER A 1 185 ? -3.454  10.447  -28.608 0.50 18.53 ? 185 SER A CB  1 
ATOM   1478 C  CB  B SER A 1 185 ? -3.385  10.329  -28.741 0.50 24.18 ? 185 SER A CB  1 
ATOM   1479 O  OG  A SER A 1 185 ? -4.111  11.388  -27.754 0.50 16.33 ? 185 SER A OG  1 
ATOM   1480 O  OG  B SER A 1 185 ? -2.055  10.287  -29.229 0.50 28.06 ? 185 SER A OG  1 
ATOM   1481 N  N   . LEU A 1 186 ? -2.424  7.078   -28.872 1.00 20.71 ? 186 LEU A N   1 
ATOM   1482 C  CA  . LEU A 1 186 ? -1.986  6.052   -29.757 1.00 18.52 ? 186 LEU A CA  1 
ATOM   1483 C  C   . LEU A 1 186 ? -3.015  4.909   -29.726 1.00 22.37 ? 186 LEU A C   1 
ATOM   1484 O  O   . LEU A 1 186 ? -3.152  4.264   -30.780 1.00 28.20 ? 186 LEU A O   1 
ATOM   1485 C  CB  . LEU A 1 186 ? -0.622  5.522   -29.442 1.00 21.23 ? 186 LEU A CB  1 
ATOM   1486 C  CG  . LEU A 1 186 ? 0.547   6.209   -30.145 1.00 23.26 ? 186 LEU A CG  1 
ATOM   1487 C  CD1 . LEU A 1 186 ? 1.765   5.508   -29.618 1.00 21.01 ? 186 LEU A CD1 1 
ATOM   1488 C  CD2 . LEU A 1 186 ? 0.395   6.026   -31.641 1.00 22.04 ? 186 LEU A CD2 1 
ATOM   1489 N  N   . LEU A 1 187 ? -3.777  4.733   -28.648 1.00 18.24 ? 187 LEU A N   1 
ATOM   1490 C  CA  . LEU A 1 187 ? -4.884  3.816   -28.514 1.00 19.26 ? 187 LEU A CA  1 
ATOM   1491 C  C   . LEU A 1 187 ? -6.111  4.094   -29.421 1.00 17.86 ? 187 LEU A C   1 
ATOM   1492 O  O   . LEU A 1 187 ? -6.448  5.290   -29.770 1.00 18.93 ? 187 LEU A O   1 
ATOM   1493 C  CB  . LEU A 1 187 ? -5.450  3.720   -27.074 1.00 18.33 ? 187 LEU A CB  1 
ATOM   1494 C  CG  . LEU A 1 187 ? -4.340  3.557   -26.029 1.00 26.10 ? 187 LEU A CG  1 
ATOM   1495 C  CD1 . LEU A 1 187 ? -4.975  3.436   -24.653 1.00 23.66 ? 187 LEU A CD1 1 
ATOM   1496 C  CD2 . LEU A 1 187 ? -3.372  2.443   -26.245 1.00 26.09 ? 187 LEU A CD2 1 
ATOM   1497 N  N   . PRO A 1 188 ? -6.782  3.014   -29.875 1.00 19.43 ? 188 PRO A N   1 
ATOM   1498 C  CA  . PRO A 1 188 ? -7.890  3.270   -30.771 1.00 18.62 ? 188 PRO A CA  1 
ATOM   1499 C  C   . PRO A 1 188 ? -9.092  3.765   -29.969 1.00 18.36 ? 188 PRO A C   1 
ATOM   1500 O  O   . PRO A 1 188 ? -9.165  3.695   -28.696 1.00 18.19 ? 188 PRO A O   1 
ATOM   1501 C  CB  . PRO A 1 188 ? -8.186  1.856   -31.356 1.00 17.60 ? 188 PRO A CB  1 
ATOM   1502 C  CG  . PRO A 1 188 ? -7.872  0.958   -30.207 1.00 17.01 ? 188 PRO A CG  1 
ATOM   1503 C  CD  . PRO A 1 188 ? -6.586  1.549   -29.698 1.00 20.32 ? 188 PRO A CD  1 
ATOM   1504 N  N   . PRO A 1 189 ? -10.104 4.242   -30.721 1.00 18.88 ? 189 PRO A N   1 
ATOM   1505 C  CA  . PRO A 1 189 ? -11.209 4.818   -29.933 1.00 18.45 ? 189 PRO A CA  1 
ATOM   1506 C  C   . PRO A 1 189 ? -11.982 3.805   -29.122 1.00 19.03 ? 189 PRO A C   1 
ATOM   1507 O  O   . PRO A 1 189 ? -12.349 4.080   -27.978 1.00 19.16 ? 189 PRO A O   1 
ATOM   1508 C  CB  . PRO A 1 189 ? -12.089 5.437   -30.996 1.00 21.05 ? 189 PRO A CB  1 
ATOM   1509 C  CG  . PRO A 1 189 ? -11.175 5.699   -32.168 1.00 21.24 ? 189 PRO A CG  1 
ATOM   1510 C  CD  . PRO A 1 189 ? -10.156 4.605   -32.164 1.00 19.29 ? 189 PRO A CD  1 
ATOM   1511 N  N   . SER A 1 190 ? -12.232 2.594   -29.663 1.00 17.55 ? 190 SER A N   1 
ATOM   1512 C  CA  . SER A 1 190 ? -12.738 1.562   -28.804 1.00 14.90 ? 190 SER A CA  1 
ATOM   1513 C  C   . SER A 1 190 ? -11.676 0.746   -28.073 1.00 18.65 ? 190 SER A C   1 
ATOM   1514 O  O   . SER A 1 190 ? -10.693 0.386   -28.727 1.00 16.89 ? 190 SER A O   1 
ATOM   1515 C  CB  . SER A 1 190 ? -13.488 0.506   -29.682 1.00 17.03 ? 190 SER A CB  1 
ATOM   1516 O  OG  . SER A 1 190 ? -13.998 -0.537  -28.883 1.00 19.34 ? 190 SER A OG  1 
ATOM   1517 N  N   . TRP A 1 191 ? -11.952 0.428   -26.801 1.00 16.01 ? 191 TRP A N   1 
ATOM   1518 C  CA  . TRP A 1 191 ? -11.054 -0.364  -25.948 1.00 17.99 ? 191 TRP A CA  1 
ATOM   1519 C  C   . TRP A 1 191 ? -11.568 -1.745  -25.666 1.00 18.25 ? 191 TRP A C   1 
ATOM   1520 O  O   . TRP A 1 191 ? -11.115 -2.443  -24.774 1.00 20.60 ? 191 TRP A O   1 
ATOM   1521 C  CB  . TRP A 1 191 ? -10.626 0.388   -24.660 1.00 17.92 ? 191 TRP A CB  1 
ATOM   1522 C  CG  . TRP A 1 191 ? -9.952  1.708   -24.856 1.00 14.73 ? 191 TRP A CG  1 
ATOM   1523 C  CD1 . TRP A 1 191 ? -9.515  2.284   -26.018 1.00 16.62 ? 191 TRP A CD1 1 
ATOM   1524 C  CD2 . TRP A 1 191 ? -9.680  2.708   -23.838 1.00 14.97 ? 191 TRP A CD2 1 
ATOM   1525 N  NE1 . TRP A 1 191 ? -8.950  3.543   -25.808 1.00 17.97 ? 191 TRP A NE1 1 
ATOM   1526 C  CE2 . TRP A 1 191 ? -9.027  3.810   -24.474 1.00 18.17 ? 191 TRP A CE2 1 
ATOM   1527 C  CE3 . TRP A 1 191 ? -9.863  2.728   -22.487 1.00 15.16 ? 191 TRP A CE3 1 
ATOM   1528 C  CZ2 . TRP A 1 191 ? -8.609  4.936   -23.780 1.00 16.03 ? 191 TRP A CZ2 1 
ATOM   1529 C  CZ3 . TRP A 1 191 ? -9.504  3.927   -21.774 1.00 14.85 ? 191 TRP A CZ3 1 
ATOM   1530 C  CH2 . TRP A 1 191 ? -8.882  4.958   -22.406 1.00 17.51 ? 191 TRP A CH2 1 
ATOM   1531 N  N   . ASP A 1 192 ? -12.491 -2.228  -26.504 1.00 15.28 ? 192 ASP A N   1 
ATOM   1532 C  CA  . ASP A 1 192 ? -12.931 -3.591  -26.364 1.00 17.26 ? 192 ASP A CA  1 
ATOM   1533 C  C   . ASP A 1 192 ? -11.682 -4.512  -26.565 1.00 14.09 ? 192 ASP A C   1 
ATOM   1534 O  O   . ASP A 1 192 ? -10.820 -4.203  -27.382 1.00 15.18 ? 192 ASP A O   1 
ATOM   1535 C  CB  . ASP A 1 192 ? -13.909 -3.866  -27.527 1.00 19.08 ? 192 ASP A CB  1 
ATOM   1536 C  CG  . ASP A 1 192 ? -15.311 -3.275  -27.291 1.00 23.98 ? 192 ASP A CG  1 
ATOM   1537 O  OD1 . ASP A 1 192 ? -15.594 -2.828  -26.168 1.00 25.37 ? 192 ASP A OD1 1 
ATOM   1538 O  OD2 . ASP A 1 192 ? -16.104 -3.418  -28.281 1.00 25.99 ? 192 ASP A OD2 1 
ATOM   1539 N  N   . TYR A 1 193 ? -11.634 -5.564  -25.800 1.00 12.20 ? 193 TYR A N   1 
ATOM   1540 C  CA  . TYR A 1 193 ? -10.423 -6.447  -25.771 1.00 14.85 ? 193 TYR A CA  1 
ATOM   1541 C  C   . TYR A 1 193 ? -10.692 -7.891  -25.519 1.00 15.07 ? 193 TYR A C   1 
ATOM   1542 O  O   . TYR A 1 193 ? -11.768 -8.330  -24.980 1.00 16.08 ? 193 TYR A O   1 
ATOM   1543 C  CB  . TYR A 1 193 ? -9.448  -5.895  -24.635 1.00 15.69 ? 193 TYR A CB  1 
ATOM   1544 C  CG  . TYR A 1 193 ? -9.982  -6.018  -23.289 1.00 16.52 ? 193 TYR A CG  1 
ATOM   1545 C  CD1 . TYR A 1 193 ? -9.835  -7.152  -22.579 1.00 16.69 ? 193 TYR A CD1 1 
ATOM   1546 C  CD2 . TYR A 1 193 ? -10.673 -4.937  -22.744 1.00 17.09 ? 193 TYR A CD2 1 
ATOM   1547 C  CE1 . TYR A 1 193 ? -10.335 -7.273  -21.310 1.00 19.40 ? 193 TYR A CE1 1 
ATOM   1548 C  CE2 . TYR A 1 193 ? -11.185 -5.006  -21.486 1.00 14.83 ? 193 TYR A CE2 1 
ATOM   1549 C  CZ  . TYR A 1 193 ? -11.047 -6.166  -20.809 1.00 14.73 ? 193 TYR A CZ  1 
ATOM   1550 O  OH  . TYR A 1 193 ? -11.600 -6.349  -19.516 1.00 21.28 ? 193 TYR A OH  1 
ATOM   1551 N  N   . TRP A 1 194 ? -9.680  -8.693  -25.798 1.00 14.53 ? 194 TRP A N   1 
ATOM   1552 C  CA  . TRP A 1 194 ? -9.577  -10.055 -25.380 1.00 14.22 ? 194 TRP A CA  1 
ATOM   1553 C  C   . TRP A 1 194 ? -8.507  -10.183 -24.270 1.00 14.14 ? 194 TRP A C   1 
ATOM   1554 O  O   . TRP A 1 194 ? -7.545  -9.490  -24.278 1.00 15.83 ? 194 TRP A O   1 
ATOM   1555 C  CB  . TRP A 1 194 ? -9.182  -10.998 -26.509 1.00 16.60 ? 194 TRP A CB  1 
ATOM   1556 C  CG  . TRP A 1 194 ? -10.141 -10.994 -27.665 1.00 15.94 ? 194 TRP A CG  1 
ATOM   1557 C  CD1 . TRP A 1 194 ? -11.377 -11.619 -27.743 1.00 20.18 ? 194 TRP A CD1 1 
ATOM   1558 C  CD2 . TRP A 1 194 ? -9.972  -10.326 -28.943 1.00 15.60 ? 194 TRP A CD2 1 
ATOM   1559 N  NE1 . TRP A 1 194 ? -11.958 -11.381 -28.956 1.00 17.97 ? 194 TRP A NE1 1 
ATOM   1560 C  CE2 . TRP A 1 194 ? -11.175 -10.615 -29.713 1.00 17.45 ? 194 TRP A CE2 1 
ATOM   1561 C  CE3 . TRP A 1 194 ? -8.993  -9.561  -29.506 1.00 14.88 ? 194 TRP A CE3 1 
ATOM   1562 C  CZ2 . TRP A 1 194 ? -11.343 -10.139 -30.987 1.00 19.11 ? 194 TRP A CZ2 1 
ATOM   1563 C  CZ3 . TRP A 1 194 ? -9.182  -9.086  -30.794 1.00 18.29 ? 194 TRP A CZ3 1 
ATOM   1564 C  CH2 . TRP A 1 194 ? -10.346 -9.379  -31.511 1.00 18.99 ? 194 TRP A CH2 1 
ATOM   1565 N  N   . THR A 1 195 ? -8.685  -11.110 -23.377 1.00 14.85 ? 195 THR A N   1 
ATOM   1566 C  CA  . THR A 1 195 ? -7.672  -11.330 -22.319 1.00 15.47 ? 195 THR A CA  1 
ATOM   1567 C  C   . THR A 1 195 ? -7.431  -12.740 -21.989 1.00 14.33 ? 195 THR A C   1 
ATOM   1568 O  O   . THR A 1 195 ? -8.337  -13.641 -22.144 1.00 17.32 ? 195 THR A O   1 
ATOM   1569 C  CB  . THR A 1 195 ? -8.066  -10.513 -21.050 1.00 16.59 ? 195 THR A CB  1 
ATOM   1570 O  OG1 . THR A 1 195 ? -7.076  -10.720 -20.053 1.00 15.19 ? 195 THR A OG1 1 
ATOM   1571 C  CG2 . THR A 1 195 ? -9.371  -10.980 -20.437 1.00 17.88 ? 195 THR A CG2 1 
ATOM   1572 N  N   . TYR A 1 196 ? -6.179  -13.078 -21.763 1.00 14.90 ? 196 TYR A N   1 
ATOM   1573 C  CA  . TYR A 1 196 ? -5.791  -14.466 -21.430 1.00 13.16 ? 196 TYR A CA  1 
ATOM   1574 C  C   . TYR A 1 196 ? -4.455  -14.446 -20.664 1.00 14.81 ? 196 TYR A C   1 
ATOM   1575 O  O   . TYR A 1 196 ? -3.716  -13.449 -20.709 1.00 15.39 ? 196 TYR A O   1 
ATOM   1576 C  CB  . TYR A 1 196 ? -5.696  -15.354 -22.729 1.00 14.70 ? 196 TYR A CB  1 
ATOM   1577 C  CG  . TYR A 1 196 ? -4.430  -15.019 -23.547 1.00 13.75 ? 196 TYR A CG  1 
ATOM   1578 C  CD1 . TYR A 1 196 ? -4.426  -13.943 -24.431 1.00 12.57 ? 196 TYR A CD1 1 
ATOM   1579 C  CD2 . TYR A 1 196 ? -3.222  -15.754 -23.389 1.00 12.92 ? 196 TYR A CD2 1 
ATOM   1580 C  CE1 . TYR A 1 196 ? -3.273  -13.546 -25.122 1.00 12.22 ? 196 TYR A CE1 1 
ATOM   1581 C  CE2 . TYR A 1 196 ? -2.040  -15.420 -24.092 1.00 13.72 ? 196 TYR A CE2 1 
ATOM   1582 C  CZ  . TYR A 1 196 ? -2.064  -14.298 -24.986 1.00 11.33 ? 196 TYR A CZ  1 
ATOM   1583 O  OH  . TYR A 1 196 ? -0.881  -14.010 -25.627 1.00 13.05 ? 196 TYR A OH  1 
ATOM   1584 N  N   . PRO A 1 197 ? -4.109  -15.549 -19.976 1.00 14.69 ? 197 PRO A N   1 
ATOM   1585 C  CA  . PRO A 1 197 ? -2.821  -15.660 -19.233 1.00 15.47 ? 197 PRO A CA  1 
ATOM   1586 C  C   . PRO A 1 197 ? -1.718  -16.136 -20.159 1.00 15.56 ? 197 PRO A C   1 
ATOM   1587 O  O   . PRO A 1 197 ? -1.900  -17.170 -20.842 1.00 16.82 ? 197 PRO A O   1 
ATOM   1588 C  CB  . PRO A 1 197 ? -3.155  -16.695 -18.150 1.00 16.29 ? 197 PRO A CB  1 
ATOM   1589 C  CG  . PRO A 1 197 ? -4.227  -17.579 -18.816 1.00 16.46 ? 197 PRO A CG  1 
ATOM   1590 C  CD  . PRO A 1 197 ? -5.034  -16.691 -19.749 1.00 15.76 ? 197 PRO A CD  1 
ATOM   1591 N  N   . GLY A 1 198 ? -0.610  -15.373 -20.231 1.00 15.00 ? 198 GLY A N   1 
ATOM   1592 C  CA  . GLY A 1 198 ? 0.494   -15.786 -21.069 1.00 15.38 ? 198 GLY A CA  1 
ATOM   1593 C  C   . GLY A 1 198 ? 1.789   -15.216 -20.574 1.00 14.39 ? 198 GLY A C   1 
ATOM   1594 O  O   . GLY A 1 198 ? 2.060   -15.286 -19.362 1.00 14.77 ? 198 GLY A O   1 
ATOM   1595 N  N   . SER A 1 199 ? 2.634   -14.863 -21.517 1.00 13.70 ? 199 SER A N   1 
ATOM   1596 C  CA  . SER A 1 199 ? 4.098   -14.716 -21.221 1.00 12.73 ? 199 SER A CA  1 
ATOM   1597 C  C   . SER A 1 199 ? 4.690   -13.536 -21.915 1.00 11.28 ? 199 SER A C   1 
ATOM   1598 O  O   . SER A 1 199 ? 4.049   -12.895 -22.791 1.00 11.07 ? 199 SER A O   1 
ATOM   1599 C  CB  . SER A 1 199 ? 4.898   -15.972 -21.697 1.00 12.48 ? 199 SER A CB  1 
ATOM   1600 O  OG  . SER A 1 199 ? 5.024   -16.011 -23.131 1.00 12.32 ? 199 SER A OG  1 
ATOM   1601 N  N   . LEU A 1 200 ? 5.921   -13.213 -21.540 1.00 11.72 ? 200 LEU A N   1 
ATOM   1602 C  CA  . LEU A 1 200 ? 6.708   -12.272 -22.355 1.00 11.97 ? 200 LEU A CA  1 
ATOM   1603 C  C   . LEU A 1 200 ? 6.852   -12.988 -23.753 1.00 12.24 ? 200 LEU A C   1 
ATOM   1604 O  O   . LEU A 1 200 ? 7.026   -14.193 -23.845 1.00 13.32 ? 200 LEU A O   1 
ATOM   1605 C  CB  . LEU A 1 200 ? 8.103   -12.089 -21.844 1.00 13.19 ? 200 LEU A CB  1 
ATOM   1606 C  CG  . LEU A 1 200 ? 8.173   -11.479 -20.389 1.00 15.35 ? 200 LEU A CG  1 
ATOM   1607 C  CD1 . LEU A 1 200 ? 9.671   -11.403 -20.041 1.00 16.58 ? 200 LEU A CD1 1 
ATOM   1608 C  CD2 . LEU A 1 200 ? 7.511   -10.157 -20.292 1.00 15.82 ? 200 LEU A CD2 1 
ATOM   1609 N  N   . THR A 1 201 ? 6.927   -12.162 -24.790 1.00 10.77 ? 201 THR A N   1 
ATOM   1610 C  CA  . THR A 1 201 ? 7.130   -12.750 -26.147 1.00 11.28 ? 201 THR A CA  1 
ATOM   1611 C  C   . THR A 1 201 ? 8.571   -12.697 -26.568 1.00 12.65 ? 201 THR A C   1 
ATOM   1612 O  O   . THR A 1 201 ? 8.868   -12.991 -27.773 1.00 12.20 ? 201 THR A O   1 
ATOM   1613 C  CB  . THR A 1 201 ? 6.178   -12.155 -27.196 1.00 12.71 ? 201 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 201 ? 6.622   -10.814 -27.466 1.00 12.00 ? 201 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 201 ? 4.706   -12.165 -26.696 1.00 12.58 ? 201 THR A CG2 1 
ATOM   1616 N  N   . VAL A 1 202 ? 9.467   -12.279 -25.691 1.00 12.27 ? 202 VAL A N   1 
ATOM   1617 C  CA  . VAL A 1 202 ? 10.908  -12.304 -25.875 1.00 13.41 ? 202 VAL A CA  1 
ATOM   1618 C  C   . VAL A 1 202 ? 11.540  -13.053 -24.757 1.00 14.25 ? 202 VAL A C   1 
ATOM   1619 O  O   . VAL A 1 202 ? 10.942  -13.059 -23.682 1.00 13.41 ? 202 VAL A O   1 
ATOM   1620 C  CB  . VAL A 1 202 ? 11.494  -10.875 -25.924 1.00 14.16 ? 202 VAL A CB  1 
ATOM   1621 C  CG1 . VAL A 1 202 ? 11.005  -10.174 -27.210 1.00 14.91 ? 202 VAL A CG1 1 
ATOM   1622 C  CG2 . VAL A 1 202 ? 11.227  -10.020 -24.690 1.00 13.13 ? 202 VAL A CG2 1 
ATOM   1623 N  N   . PRO A 1 203 ? 12.698  -13.686 -24.979 1.00 14.74 ? 203 PRO A N   1 
ATOM   1624 C  CA  . PRO A 1 203 ? 13.467  -14.217 -23.844 1.00 15.86 ? 203 PRO A CA  1 
ATOM   1625 C  C   . PRO A 1 203 ? 13.530  -13.138 -22.792 1.00 14.12 ? 203 PRO A C   1 
ATOM   1626 O  O   . PRO A 1 203 ? 13.839  -11.968 -23.031 1.00 15.41 ? 203 PRO A O   1 
ATOM   1627 C  CB  . PRO A 1 203 ? 14.826  -14.518 -24.485 1.00 15.38 ? 203 PRO A CB  1 
ATOM   1628 C  CG  . PRO A 1 203 ? 14.431  -14.913 -25.933 1.00 15.67 ? 203 PRO A CG  1 
ATOM   1629 C  CD  . PRO A 1 203 ? 13.383  -13.855 -26.286 1.00 14.00 ? 203 PRO A CD  1 
ATOM   1630 N  N   . PRO A 1 204 ? 13.319  -13.548 -21.506 1.00 13.60 ? 204 PRO A N   1 
ATOM   1631 C  CA  . PRO A 1 204 ? 13.259  -14.879 -20.964 1.00 15.89 ? 204 PRO A CA  1 
ATOM   1632 C  C   . PRO A 1 204 ? 11.911  -15.596 -21.025 1.00 16.23 ? 204 PRO A C   1 
ATOM   1633 O  O   . PRO A 1 204 ? 11.783  -16.719 -20.460 1.00 18.06 ? 204 PRO A O   1 
ATOM   1634 C  CB  . PRO A 1 204 ? 13.712  -14.613 -19.469 1.00 16.29 ? 204 PRO A CB  1 
ATOM   1635 C  CG  . PRO A 1 204 ? 13.244  -13.180 -19.179 1.00 18.38 ? 204 PRO A CG  1 
ATOM   1636 C  CD  . PRO A 1 204 ? 13.511  -12.479 -20.539 1.00 15.73 ? 204 PRO A CD  1 
ATOM   1637 N  N   . LEU A 1 205 ? 10.902  -15.003 -21.699 1.00 12.96 ? 205 LEU A N   1 
ATOM   1638 C  CA  . LEU A 1 205 ? 9.691   -15.761 -21.986 1.00 13.15 ? 205 LEU A CA  1 
ATOM   1639 C  C   . LEU A 1 205 ? 8.888   -16.142 -20.746 1.00 13.30 ? 205 LEU A C   1 
ATOM   1640 O  O   . LEU A 1 205 ? 8.067   -17.081 -20.756 1.00 14.09 ? 205 LEU A O   1 
ATOM   1641 C  CB  . LEU A 1 205 ? 9.892   -16.989 -22.901 1.00 14.18 ? 205 LEU A CB  1 
ATOM   1642 C  CG  . LEU A 1 205 ? 10.570  -16.621 -24.279 1.00 14.33 ? 205 LEU A CG  1 
ATOM   1643 C  CD1 . LEU A 1 205 ? 11.011  -17.940 -24.953 1.00 17.74 ? 205 LEU A CD1 1 
ATOM   1644 C  CD2 . LEU A 1 205 ? 9.604   -15.934 -25.259 1.00 14.64 ? 205 LEU A CD2 1 
ATOM   1645 N  N   . LEU A 1 206 ? 9.056   -15.298 -19.707 1.00 14.51 ? 206 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 206 ? 8.412   -15.684 -18.424 1.00 14.24 ? 206 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 206 ? 6.922   -15.625 -18.459 1.00 13.12 ? 206 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 206 ? 6.325   -14.744 -19.090 1.00 12.78 ? 206 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 206 ? 8.921   -14.748 -17.333 1.00 14.39 ? 206 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 206 ? 10.457  -14.782 -17.099 1.00 15.43 ? 206 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 206 ? 10.908  -13.505 -16.304 1.00 17.36 ? 206 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 206 ? 10.776  -16.047 -16.298 1.00 19.65 ? 206 LEU A CD2 1 
ATOM   1653 N  N   . GLU A 1 207 ? 6.274   -16.580 -17.759 1.00 13.87 ? 207 GLU A N   1 
ATOM   1654 C  CA  . GLU A 1 207 ? 4.837   -16.722 -17.756 1.00 12.90 ? 207 GLU A CA  1 
ATOM   1655 C  C   . GLU A 1 207 ? 4.237   -15.918 -16.643 1.00 14.26 ? 207 GLU A C   1 
ATOM   1656 O  O   . GLU A 1 207 ? 3.722   -16.422 -15.628 1.00 16.00 ? 207 GLU A O   1 
ATOM   1657 C  CB  . GLU A 1 207 ? 4.429   -18.217 -17.790 1.00 13.78 ? 207 GLU A CB  1 
ATOM   1658 C  CG  . GLU A 1 207 ? 4.966   -18.905 -19.073 1.00 15.77 ? 207 GLU A CG  1 
ATOM   1659 C  CD  . GLU A 1 207 ? 4.696   -20.370 -19.184 1.00 18.04 ? 207 GLU A CD  1 
ATOM   1660 O  OE1 . GLU A 1 207 ? 4.586   -21.037 -18.094 1.00 18.45 ? 207 GLU A OE1 1 
ATOM   1661 O  OE2 . GLU A 1 207 ? 4.627   -20.901 -20.354 1.00 15.91 ? 207 GLU A OE2 1 
ATOM   1662 N  N   . SER A 1 208 ? 4.313   -14.634 -16.806 1.00 13.82 ? 208 SER A N   1 
ATOM   1663 C  CA  . SER A 1 208 ? 3.878   -13.667 -15.787 1.00 14.14 ? 208 SER A CA  1 
ATOM   1664 C  C   . SER A 1 208 ? 2.988   -12.596 -16.302 1.00 13.37 ? 208 SER A C   1 
ATOM   1665 O  O   . SER A 1 208 ? 2.699   -11.530 -15.624 1.00 13.88 ? 208 SER A O   1 
ATOM   1666 C  CB  . SER A 1 208 ? 5.185   -13.056 -15.267 1.00 16.35 ? 208 SER A CB  1 
ATOM   1667 O  OG  . SER A 1 208 ? 5.877   -12.384 -16.364 1.00 17.00 ? 208 SER A OG  1 
ATOM   1668 N  N   . VAL A 1 209 ? 2.454   -12.772 -17.544 1.00 12.53 ? 209 VAL A N   1 
ATOM   1669 C  CA  . VAL A 1 209 ? 1.666   -11.702 -18.132 1.00 13.79 ? 209 VAL A CA  1 
ATOM   1670 C  C   . VAL A 1 209 ? 0.156   -11.957 -18.261 1.00 13.08 ? 209 VAL A C   1 
ATOM   1671 O  O   . VAL A 1 209 ? -0.268  -12.981 -18.818 1.00 14.96 ? 209 VAL A O   1 
ATOM   1672 C  CB  . VAL A 1 209 ? 2.200   -11.464 -19.580 1.00 13.84 ? 209 VAL A CB  1 
ATOM   1673 C  CG1 . VAL A 1 209 ? 1.428   -10.322 -20.234 1.00 14.35 ? 209 VAL A CG1 1 
ATOM   1674 C  CG2 . VAL A 1 209 ? 3.720   -11.119 -19.494 1.00 14.73 ? 209 VAL A CG2 1 
ATOM   1675 N  N   . THR A 1 210 ? -0.628  -10.957 -17.811 1.00 12.97 ? 210 THR A N   1 
ATOM   1676 C  CA  . THR A 1 210 ? -2.047  -10.917 -18.151 1.00 13.30 ? 210 THR A CA  1 
ATOM   1677 C  C   . THR A 1 210 ? -2.120  -10.089 -19.403 1.00 13.67 ? 210 THR A C   1 
ATOM   1678 O  O   . THR A 1 210 ? -1.913  -8.868  -19.418 1.00 13.38 ? 210 THR A O   1 
ATOM   1679 C  CB  . THR A 1 210 ? -2.854  -10.252 -17.010 1.00 14.52 ? 210 THR A CB  1 
ATOM   1680 O  OG1 . THR A 1 210 ? -2.733  -11.107 -15.865 1.00 16.17 ? 210 THR A OG1 1 
ATOM   1681 C  CG2 . THR A 1 210 ? -4.386  -10.139 -17.422 1.00 15.61 ? 210 THR A CG2 1 
ATOM   1682 N  N   . TRP A 1 211 ? -2.440  -10.787 -20.517 1.00 13.08 ? 211 TRP A N   1 
ATOM   1683 C  CA  . TRP A 1 211 ? -2.556  -10.068 -21.816 1.00 14.01 ? 211 TRP A CA  1 
ATOM   1684 C  C   . TRP A 1 211 ? -3.916  -9.387  -21.986 1.00 12.96 ? 211 TRP A C   1 
ATOM   1685 O  O   . TRP A 1 211 ? -4.934  -9.994  -21.614 1.00 16.14 ? 211 TRP A O   1 
ATOM   1686 C  CB  . TRP A 1 211 ? -2.328  -11.123 -22.925 1.00 12.50 ? 211 TRP A CB  1 
ATOM   1687 C  CG  . TRP A 1 211 ? -0.851  -11.235 -23.198 1.00 11.70 ? 211 TRP A CG  1 
ATOM   1688 C  CD1 . TRP A 1 211 ? 0.030   -12.210 -22.741 1.00 10.70 ? 211 TRP A CD1 1 
ATOM   1689 C  CD2 . TRP A 1 211 ? -0.016  -10.289 -23.947 1.00 11.98 ? 211 TRP A CD2 1 
ATOM   1690 N  NE1 . TRP A 1 211 ? 1.308   -11.953 -23.168 1.00 11.84 ? 211 TRP A NE1 1 
ATOM   1691 C  CE2 . TRP A 1 211 ? 1.348   -10.816 -23.897 1.00 11.34 ? 211 TRP A CE2 1 
ATOM   1692 C  CE3 . TRP A 1 211 ? -0.257  -9.113  -24.640 1.00 12.24 ? 211 TRP A CE3 1 
ATOM   1693 C  CZ2 . TRP A 1 211 ? 2.405   -10.177 -24.520 1.00 13.23 ? 211 TRP A CZ2 1 
ATOM   1694 C  CZ3 . TRP A 1 211 ? 0.816   -8.478  -25.265 1.00 13.26 ? 211 TRP A CZ3 1 
ATOM   1695 C  CH2 . TRP A 1 211 ? 2.113   -8.999  -25.206 1.00 10.84 ? 211 TRP A CH2 1 
ATOM   1696 N  N   . ILE A 1 212 ? -3.945  -8.209  -22.509 1.00 12.77 ? 212 ILE A N   1 
ATOM   1697 C  CA  . ILE A 1 212 ? -5.137  -7.482  -22.830 1.00 13.12 ? 212 ILE A CA  1 
ATOM   1698 C  C   . ILE A 1 212 ? -4.920  -6.947  -24.217 1.00 12.72 ? 212 ILE A C   1 
ATOM   1699 O  O   . ILE A 1 212 ? -4.220  -5.988  -24.485 1.00 13.28 ? 212 ILE A O   1 
ATOM   1700 C  CB  . ILE A 1 212 ? -5.377  -6.320  -21.815 1.00 14.80 ? 212 ILE A CB  1 
ATOM   1701 C  CG1 . ILE A 1 212 ? -5.508  -6.876  -20.388 1.00 14.37 ? 212 ILE A CG1 1 
ATOM   1702 C  CG2 . ILE A 1 212 ? -6.556  -5.438  -22.266 1.00 15.01 ? 212 ILE A CG2 1 
ATOM   1703 C  CD1 . ILE A 1 212 ? -5.443  -5.760  -19.313 1.00 15.92 ? 212 ILE A CD1 1 
ATOM   1704 N  N   . VAL A 1 213 ? -5.566  -7.682  -25.195 1.00 12.89 ? 213 VAL A N   1 
ATOM   1705 C  CA  . VAL A 1 213 ? -5.316  -7.382  -26.583 1.00 13.05 ? 213 VAL A CA  1 
ATOM   1706 C  C   . VAL A 1 213 ? -6.578  -6.668  -27.122 1.00 14.01 ? 213 VAL A C   1 
ATOM   1707 O  O   . VAL A 1 213 ? -7.654  -7.256  -27.175 1.00 14.21 ? 213 VAL A O   1 
ATOM   1708 C  CB  . VAL A 1 213 ? -5.094  -8.681  -27.334 1.00 14.23 ? 213 VAL A CB  1 
ATOM   1709 C  CG1 . VAL A 1 213 ? -4.854  -8.399  -28.792 1.00 12.80 ? 213 VAL A CG1 1 
ATOM   1710 C  CG2 . VAL A 1 213 ? -3.864  -9.471  -26.787 1.00 15.02 ? 213 VAL A CG2 1 
ATOM   1711 N  N   . LEU A 1 214 ? -6.385  -5.431  -27.578 1.00 13.22 ? 214 LEU A N   1 
ATOM   1712 C  CA  . LEU A 1 214 ? -7.545  -4.584  -28.050 1.00 13.88 ? 214 LEU A CA  1 
ATOM   1713 C  C   . LEU A 1 214 ? -7.995  -5.081  -29.434 1.00 14.08 ? 214 LEU A C   1 
ATOM   1714 O  O   . LEU A 1 214 ? -7.151  -5.413  -30.294 1.00 13.96 ? 214 LEU A O   1 
ATOM   1715 C  CB  . LEU A 1 214 ? -7.197  -3.088  -28.089 1.00 14.88 ? 214 LEU A CB  1 
ATOM   1716 C  CG  . LEU A 1 214 ? -7.382  -2.431  -26.721 1.00 17.39 ? 214 LEU A CG  1 
ATOM   1717 C  CD1 . LEU A 1 214 ? -6.710  -3.138  -25.597 1.00 21.20 ? 214 LEU A CD1 1 
ATOM   1718 C  CD2 . LEU A 1 214 ? -6.967  -0.976  -26.921 1.00 18.94 ? 214 LEU A CD2 1 
ATOM   1719 N  N   . LYS A 1 215 ? -9.319  -5.136  -29.626 1.00 15.28 ? 215 LYS A N   1 
ATOM   1720 C  CA  . LYS A 1 215 ? -9.830  -5.609  -30.936 1.00 15.66 ? 215 LYS A CA  1 
ATOM   1721 C  C   . LYS A 1 215 ? -9.575  -4.601  -32.089 1.00 16.06 ? 215 LYS A C   1 
ATOM   1722 O  O   . LYS A 1 215 ? -9.219  -4.944  -33.263 1.00 16.98 ? 215 LYS A O   1 
ATOM   1723 C  CB  . LYS A 1 215 ? -11.323 -5.878  -30.767 1.00 16.74 ? 215 LYS A CB  1 
ATOM   1724 C  CG  . LYS A 1 215 ? -12.024 -6.177  -32.122 1.00 18.73 ? 215 LYS A CG  1 
ATOM   1725 C  CD  . LYS A 1 215 ? -13.439 -6.646  -31.886 1.00 21.34 ? 215 LYS A CD  1 
ATOM   1726 C  CE  . LYS A 1 215 ? -14.251 -6.659  -33.163 1.00 26.83 ? 215 LYS A CE  1 
ATOM   1727 N  NZ  . LYS A 1 215 ? -15.604 -7.239  -32.923 1.00 34.55 ? 215 LYS A NZ  1 
ATOM   1728 N  N   . GLN A 1 216 ? -9.765  -3.296  -31.814 1.00 15.27 ? 216 GLN A N   1 
ATOM   1729 C  CA  . GLN A 1 216 ? -9.722  -2.300  -32.896 1.00 14.18 ? 216 GLN A CA  1 
ATOM   1730 C  C   . GLN A 1 216 ? -8.312  -1.886  -33.230 1.00 15.47 ? 216 GLN A C   1 
ATOM   1731 O  O   . GLN A 1 216 ? -7.601  -1.401  -32.326 1.00 15.17 ? 216 GLN A O   1 
ATOM   1732 C  CB  . GLN A 1 216 ? -10.568 -1.021  -32.556 1.00 15.50 ? 216 GLN A CB  1 
ATOM   1733 C  CG  . GLN A 1 216 ? -10.469 0.038   -33.667 1.00 18.25 ? 216 GLN A CG  1 
ATOM   1734 C  CD  . GLN A 1 216 ? -11.376 1.219   -33.502 1.00 20.02 ? 216 GLN A CD  1 
ATOM   1735 O  OE1 . GLN A 1 216 ? -11.876 1.444   -32.443 1.00 21.68 ? 216 GLN A OE1 1 
ATOM   1736 N  NE2 . GLN A 1 216 ? -11.577 1.958   -34.592 1.00 21.83 ? 216 GLN A NE2 1 
ATOM   1737 N  N   . PRO A 1 217 ? -7.815  -2.023  -34.432 1.00 15.83 ? 217 PRO A N   1 
ATOM   1738 C  CA  . PRO A 1 217 ? -6.496  -1.566  -34.817 1.00 16.22 ? 217 PRO A CA  1 
ATOM   1739 C  C   . PRO A 1 217 ? -6.409  -0.064  -34.953 1.00 16.29 ? 217 PRO A C   1 
ATOM   1740 O  O   . PRO A 1 217 ? -7.460  0.654   -35.123 1.00 19.37 ? 217 PRO A O   1 
ATOM   1741 C  CB  . PRO A 1 217 ? -6.214  -2.239  -36.172 1.00 16.08 ? 217 PRO A CB  1 
ATOM   1742 C  CG  . PRO A 1 217 ? -7.640  -2.471  -36.663 1.00 20.41 ? 217 PRO A CG  1 
ATOM   1743 C  CD  . PRO A 1 217 ? -8.596  -2.639  -35.543 1.00 15.79 ? 217 PRO A CD  1 
ATOM   1744 N  N   . ILE A 1 218 ? -5.195  0.462   -34.861 1.00 15.69 ? 218 ILE A N   1 
ATOM   1745 C  CA  . ILE A 1 218 ? -4.888  1.831   -35.294 1.00 16.50 ? 218 ILE A CA  1 
ATOM   1746 C  C   . ILE A 1 218 ? -4.194  1.798   -36.607 1.00 16.30 ? 218 ILE A C   1 
ATOM   1747 O  O   . ILE A 1 218 ? -3.849  0.724   -37.072 1.00 17.77 ? 218 ILE A O   1 
ATOM   1748 C  CB  . ILE A 1 218 ? -4.051  2.628   -34.230 1.00 15.86 ? 218 ILE A CB  1 
ATOM   1749 C  CG1 . ILE A 1 218 ? -2.670  2.030   -34.031 1.00 15.02 ? 218 ILE A CG1 1 
ATOM   1750 C  CG2 . ILE A 1 218 ? -4.767  2.585   -32.922 1.00 14.66 ? 218 ILE A CG2 1 
ATOM   1751 C  CD1 . ILE A 1 218 ? -1.740  2.902   -33.138 1.00 14.88 ? 218 ILE A CD1 1 
ATOM   1752 N  N   . ASN A 1 219 ? -4.009  2.933   -37.308 1.00 15.46 ? 219 ASN A N   1 
ATOM   1753 C  CA  . ASN A 1 219 ? -3.351  2.903   -38.571 1.00 16.97 ? 219 ASN A CA  1 
ATOM   1754 C  C   . ASN A 1 219 ? -1.884  3.263   -38.509 1.00 15.46 ? 219 ASN A C   1 
ATOM   1755 O  O   . ASN A 1 219 ? -1.397  3.961   -37.563 1.00 16.91 ? 219 ASN A O   1 
ATOM   1756 C  CB  . ASN A 1 219 ? -3.957  3.959   -39.490 1.00 19.40 ? 219 ASN A CB  1 
ATOM   1757 C  CG  . ASN A 1 219 ? -5.361  3.681   -39.895 1.00 23.32 ? 219 ASN A CG  1 
ATOM   1758 O  OD1 . ASN A 1 219 ? -5.809  2.538   -40.075 1.00 25.51 ? 219 ASN A OD1 1 
ATOM   1759 N  ND2 . ASN A 1 219 ? -6.099  4.813   -40.137 1.00 33.10 ? 219 ASN A ND2 1 
ATOM   1760 N  N   . ILE A 1 220 ? -1.143  2.868   -39.527 1.00 15.13 ? 220 ILE A N   1 
ATOM   1761 C  CA  . ILE A 1 220 ? 0.191   3.288   -39.765 1.00 15.24 ? 220 ILE A CA  1 
ATOM   1762 C  C   . ILE A 1 220 ? 0.356   3.248   -41.285 1.00 15.21 ? 220 ILE A C   1 
ATOM   1763 O  O   . ILE A 1 220 ? -0.129  2.321   -41.938 1.00 15.05 ? 220 ILE A O   1 
ATOM   1764 C  CB  . ILE A 1 220 ? 1.262   2.327   -39.049 1.00 15.09 ? 220 ILE A CB  1 
ATOM   1765 C  CG1 . ILE A 1 220 ? 2.668   2.904   -39.162 1.00 14.89 ? 220 ILE A CG1 1 
ATOM   1766 C  CG2 . ILE A 1 220 ? 1.152   0.861   -39.589 1.00 15.59 ? 220 ILE A CG2 1 
ATOM   1767 C  CD1 . ILE A 1 220 ? 3.749   2.161   -38.273 1.00 15.47 ? 220 ILE A CD1 1 
ATOM   1768 N  N   . SER A 1 221 ? 1.079   4.214   -41.829 1.00 15.48 ? 221 SER A N   1 
ATOM   1769 C  CA  . SER A 1 221 ? 1.340   4.054   -43.258 1.00 16.13 ? 221 SER A CA  1 
ATOM   1770 C  C   . SER A 1 221 ? 2.497   3.143   -43.536 1.00 17.76 ? 221 SER A C   1 
ATOM   1771 O  O   . SER A 1 221 ? 3.366   2.904   -42.681 1.00 17.03 ? 221 SER A O   1 
ATOM   1772 C  CB  . SER A 1 221 ? 1.672   5.450   -43.855 1.00 16.01 ? 221 SER A CB  1 
ATOM   1773 O  OG  . SER A 1 221 ? 2.980   5.941   -43.567 1.00 17.53 ? 221 SER A OG  1 
ATOM   1774 N  N   A SER A 1 222 ? 2.573   2.681   -44.761 0.50 17.37 ? 222 SER A N   1 
ATOM   1775 N  N   B SER A 1 222 ? 2.674   2.652   -44.763 0.50 16.86 ? 222 SER A N   1 
ATOM   1776 C  CA  A SER A 1 222 ? 3.716   1.900   -45.158 0.50 16.57 ? 222 SER A CA  1 
ATOM   1777 C  CA  B SER A 1 222 ? 3.888   1.838   -45.131 0.50 15.86 ? 222 SER A CA  1 
ATOM   1778 C  C   A SER A 1 222 ? 5.034   2.627   -44.953 0.50 17.44 ? 222 SER A C   1 
ATOM   1779 C  C   B SER A 1 222 ? 5.219   2.611   -45.034 0.50 16.91 ? 222 SER A C   1 
ATOM   1780 O  O   A SER A 1 222 ? 5.920   2.071   -44.398 0.50 18.02 ? 222 SER A O   1 
ATOM   1781 O  O   B SER A 1 222 ? 6.320   2.087   -44.714 0.50 14.18 ? 222 SER A O   1 
ATOM   1782 C  CB  A SER A 1 222 ? 3.595   1.418   -46.609 0.50 16.15 ? 222 SER A CB  1 
ATOM   1783 C  CB  B SER A 1 222 ? 3.752   1.205   -46.566 0.50 15.52 ? 222 SER A CB  1 
ATOM   1784 O  OG  A SER A 1 222 ? 4.783   0.730   -46.932 0.50 15.43 ? 222 SER A OG  1 
ATOM   1785 O  OG  B SER A 1 222 ? 2.645   0.321   -46.714 0.50 16.89 ? 222 SER A OG  1 
ATOM   1786 N  N   . GLN A 1 223 ? 5.164   3.901   -45.366 1.00 16.59 ? 223 GLN A N   1 
ATOM   1787 C  CA  . GLN A 1 223 ? 6.342   4.705   -45.225 1.00 16.88 ? 223 GLN A CA  1 
ATOM   1788 C  C   . GLN A 1 223 ? 6.752   4.838   -43.762 1.00 17.39 ? 223 GLN A C   1 
ATOM   1789 O  O   . GLN A 1 223 ? 7.951   4.755   -43.508 1.00 19.05 ? 223 GLN A O   1 
ATOM   1790 C  CB  . GLN A 1 223 ? 6.133   6.116   -45.846 1.00 18.12 ? 223 GLN A CB  1 
ATOM   1791 C  CG  . GLN A 1 223 ? 6.290   6.150   -47.360 1.00 23.03 ? 223 GLN A CG  1 
ATOM   1792 C  CD  . GLN A 1 223 ? 6.368   7.573   -47.887 1.00 23.45 ? 223 GLN A CD  1 
ATOM   1793 O  OE1 . GLN A 1 223 ? 7.111   8.399   -47.405 1.00 24.11 ? 223 GLN A OE1 1 
ATOM   1794 N  NE2 . GLN A 1 223 ? 5.581   7.844   -48.925 1.00 24.25 ? 223 GLN A NE2 1 
ATOM   1795 N  N   . GLN A 1 224 ? 5.747   4.946   -42.891 1.00 16.73 ? 224 GLN A N   1 
ATOM   1796 C  CA  . GLN A 1 224 ? 6.136   5.121   -41.471 1.00 16.27 ? 224 GLN A CA  1 
ATOM   1797 C  C   . GLN A 1 224 ? 6.635   3.807   -40.980 1.00 17.89 ? 224 GLN A C   1 
ATOM   1798 O  O   . GLN A 1 224 ? 7.671   3.767   -40.281 1.00 18.14 ? 224 GLN A O   1 
ATOM   1799 C  CB  . GLN A 1 224 ? 4.929   5.479   -40.629 1.00 15.53 ? 224 GLN A CB  1 
ATOM   1800 C  CG  . GLN A 1 224 ? 4.394   6.901   -40.762 1.00 18.74 ? 224 GLN A CG  1 
ATOM   1801 C  CD  . GLN A 1 224 ? 3.148   7.115   -39.895 1.00 16.23 ? 224 GLN A CD  1 
ATOM   1802 O  OE1 . GLN A 1 224 ? 2.127   6.392   -39.981 1.00 17.58 ? 224 GLN A OE1 1 
ATOM   1803 N  NE2 . GLN A 1 224 ? 3.228   8.119   -39.026 1.00 19.90 ? 224 GLN A NE2 1 
ATOM   1804 N  N   . LEU A 1 225 ? 5.927   2.728   -41.348 1.00 15.67 ? 225 LEU A N   1 
ATOM   1805 C  CA  . LEU A 1 225 ? 6.425   1.432   -40.804 1.00 15.35 ? 225 LEU A CA  1 
ATOM   1806 C  C   . LEU A 1 225 ? 7.808   1.084   -41.274 1.00 17.53 ? 225 LEU A C   1 
ATOM   1807 O  O   . LEU A 1 225 ? 8.664   0.556   -40.509 1.00 18.78 ? 225 LEU A O   1 
ATOM   1808 C  CB  . LEU A 1 225 ? 5.391   0.338   -41.120 1.00 15.88 ? 225 LEU A CB  1 
ATOM   1809 C  CG  . LEU A 1 225 ? 5.664   -1.074  -40.588 1.00 17.57 ? 225 LEU A CG  1 
ATOM   1810 C  CD1 . LEU A 1 225 ? 5.833   -1.022  -39.073 1.00 18.57 ? 225 LEU A CD1 1 
ATOM   1811 C  CD2 . LEU A 1 225 ? 4.478   -1.958  -40.852 1.00 17.75 ? 225 LEU A CD2 1 
ATOM   1812 N  N   . ALA A 1 226 ? 8.159   1.357   -42.549 1.00 16.02 ? 226 ALA A N   1 
ATOM   1813 C  CA  . ALA A 1 226 ? 9.484   1.153   -43.033 1.00 17.12 ? 226 ALA A CA  1 
ATOM   1814 C  C   . ALA A 1 226 ? 10.654  1.810   -42.265 1.00 16.71 ? 226 ALA A C   1 
ATOM   1815 O  O   . ALA A 1 226 ? 11.732  1.275   -42.239 1.00 17.84 ? 226 ALA A O   1 
ATOM   1816 C  CB  . ALA A 1 226 ? 9.571   1.550   -44.544 1.00 20.79 ? 226 ALA A CB  1 
ATOM   1817 N  N   . LYS A 1 227 ? 10.402  2.947   -41.628 1.00 17.81 ? 227 LYS A N   1 
ATOM   1818 C  CA  . LYS A 1 227 ? 11.413  3.620   -40.859 1.00 18.22 ? 227 LYS A CA  1 
ATOM   1819 C  C   . LYS A 1 227 ? 11.863  2.745   -39.641 1.00 16.50 ? 227 LYS A C   1 
ATOM   1820 O  O   . LYS A 1 227 ? 13.057  2.828   -39.243 1.00 17.36 ? 227 LYS A O   1 
ATOM   1821 C  CB  . LYS A 1 227 ? 10.850  4.971   -40.333 1.00 21.22 ? 227 LYS A CB  1 
ATOM   1822 C  CG  . LYS A 1 227 ? 10.342  5.995   -41.425 1.00 26.50 ? 227 LYS A CG  1 
ATOM   1823 C  CD  . LYS A 1 227 ? 9.935   7.434   -40.884 1.00 32.58 ? 227 LYS A CD  1 
ATOM   1824 C  CE  . LYS A 1 227 ? 8.421   7.554   -40.781 1.00 35.52 ? 227 LYS A CE  1 
ATOM   1825 N  NZ  . LYS A 1 227 ? 7.934   8.961   -40.818 1.00 29.42 ? 227 LYS A NZ  1 
ATOM   1826 N  N   . PHE A 1 228 ? 10.921  1.939   -39.122 1.00 15.40 ? 228 PHE A N   1 
ATOM   1827 C  CA  . PHE A 1 228 ? 11.335  1.061   -37.986 1.00 15.04 ? 228 PHE A CA  1 
ATOM   1828 C  C   . PHE A 1 228 ? 12.299  -0.015  -38.395 1.00 14.80 ? 228 PHE A C   1 
ATOM   1829 O  O   . PHE A 1 228 ? 13.205  -0.400  -37.649 1.00 15.66 ? 228 PHE A O   1 
ATOM   1830 C  CB  . PHE A 1 228 ? 10.091  0.442   -37.296 1.00 14.74 ? 228 PHE A CB  1 
ATOM   1831 C  CG  . PHE A 1 228 ? 9.256   1.472   -36.621 1.00 13.65 ? 228 PHE A CG  1 
ATOM   1832 C  CD1 . PHE A 1 228 ? 8.148   2.015   -37.224 1.00 15.92 ? 228 PHE A CD1 1 
ATOM   1833 C  CD2 . PHE A 1 228 ? 9.660   1.960   -35.333 1.00 15.43 ? 228 PHE A CD2 1 
ATOM   1834 C  CE1 . PHE A 1 228 ? 7.378   3.011   -36.576 1.00 16.99 ? 228 PHE A CE1 1 
ATOM   1835 C  CE2 . PHE A 1 228 ? 8.913   2.945   -34.745 1.00 14.38 ? 228 PHE A CE2 1 
ATOM   1836 C  CZ  . PHE A 1 228 ? 7.752   3.494   -35.299 1.00 16.37 ? 228 PHE A CZ  1 
ATOM   1837 N  N   . ARG A 1 229 ? 12.136  -0.510  -39.639 1.00 14.88 ? 229 ARG A N   1 
ATOM   1838 C  CA  . ARG A 1 229 ? 13.054  -1.530  -40.142 1.00 17.32 ? 229 ARG A CA  1 
ATOM   1839 C  C   . ARG A 1 229 ? 14.494  -1.045  -40.441 1.00 16.70 ? 229 ARG A C   1 
ATOM   1840 O  O   . ARG A 1 229 ? 15.333  -1.868  -40.682 1.00 17.74 ? 229 ARG A O   1 
ATOM   1841 C  CB  . ARG A 1 229 ? 12.468  -2.150  -41.447 1.00 15.48 ? 229 ARG A CB  1 
ATOM   1842 C  CG  . ARG A 1 229 ? 11.103  -2.659  -41.310 1.00 14.19 ? 229 ARG A CG  1 
ATOM   1843 C  CD  . ARG A 1 229 ? 10.717  -3.511  -42.555 1.00 14.84 ? 229 ARG A CD  1 
ATOM   1844 N  NE  . ARG A 1 229 ? 9.312   -3.896  -42.468 1.00 16.83 ? 229 ARG A NE  1 
ATOM   1845 C  CZ  . ARG A 1 229 ? 8.319   -3.282  -43.103 1.00 15.97 ? 229 ARG A CZ  1 
ATOM   1846 N  NH1 . ARG A 1 229 ? 8.563   -2.251  -43.902 1.00 16.51 ? 229 ARG A NH1 1 
ATOM   1847 N  NH2 . ARG A 1 229 ? 7.073   -3.705  -42.941 1.00 15.97 ? 229 ARG A NH2 1 
ATOM   1848 N  N   A SER A 1 230 ? 14.796  0.256   -40.412 0.50 17.64 ? 230 SER A N   1 
ATOM   1849 N  N   B SER A 1 230 ? 14.714  0.280   -40.404 0.50 18.07 ? 230 SER A N   1 
ATOM   1850 C  CA  A SER A 1 230 ? 16.197  0.703   -40.536 0.50 19.58 ? 230 SER A CA  1 
ATOM   1851 C  CA  B SER A 1 230 ? 16.048  0.904   -40.495 0.50 19.75 ? 230 SER A CA  1 
ATOM   1852 C  C   A SER A 1 230 ? 16.932  0.759   -39.188 0.50 20.50 ? 230 SER A C   1 
ATOM   1853 C  C   B SER A 1 230 ? 16.812  1.012   -39.176 0.50 21.40 ? 230 SER A C   1 
ATOM   1854 O  O   A SER A 1 230 ? 18.151  1.053   -39.134 0.50 19.97 ? 230 SER A O   1 
ATOM   1855 O  O   B SER A 1 230 ? 17.940  1.518   -39.148 0.50 22.14 ? 230 SER A O   1 
ATOM   1856 C  CB  A SER A 1 230 ? 16.324  2.075   -41.187 0.50 21.00 ? 230 SER A CB  1 
ATOM   1857 C  CB  B SER A 1 230 ? 16.001  2.296   -41.116 0.50 22.09 ? 230 SER A CB  1 
ATOM   1858 O  OG  A SER A 1 230 ? 15.760  3.052   -40.356 0.50 23.11 ? 230 SER A OG  1 
ATOM   1859 O  OG  B SER A 1 230 ? 15.933  2.182   -42.524 0.50 25.76 ? 230 SER A OG  1 
ATOM   1860 N  N   . LEU A 1 231 ? 16.192  0.555   -38.086 1.00 17.97 ? 231 LEU A N   1 
ATOM   1861 C  CA  . LEU A 1 231 ? 16.904  0.447   -36.829 1.00 19.23 ? 231 LEU A CA  1 
ATOM   1862 C  C   . LEU A 1 231 ? 17.833  -0.742  -36.980 1.00 17.46 ? 231 LEU A C   1 
ATOM   1863 O  O   . LEU A 1 231 ? 17.516  -1.763  -37.641 1.00 19.15 ? 231 LEU A O   1 
ATOM   1864 C  CB  . LEU A 1 231 ? 15.922  0.081   -35.678 1.00 17.07 ? 231 LEU A CB  1 
ATOM   1865 C  CG  . LEU A 1 231 ? 15.062  1.233   -35.286 1.00 15.29 ? 231 LEU A CG  1 
ATOM   1866 C  CD1 . LEU A 1 231 ? 14.071  0.689   -34.228 1.00 17.45 ? 231 LEU A CD1 1 
ATOM   1867 C  CD2 . LEU A 1 231 ? 15.865  2.334   -34.563 1.00 17.70 ? 231 LEU A CD2 1 
ATOM   1868 N  N   . LEU A 1 232 ? 18.979  -0.697  -36.285 1.00 16.93 ? 232 LEU A N   1 
ATOM   1869 C  CA  . LEU A 1 232 ? 19.914  -1.815  -36.292 1.00 18.67 ? 232 LEU A CA  1 
ATOM   1870 C  C   . LEU A 1 232 ? 19.767  -2.704  -35.081 1.00 17.41 ? 232 LEU A C   1 
ATOM   1871 O  O   . LEU A 1 232 ? 19.383  -2.183  -33.972 1.00 19.83 ? 232 LEU A O   1 
ATOM   1872 C  CB  . LEU A 1 232 ? 21.354  -1.261  -36.347 1.00 21.43 ? 232 LEU A CB  1 
ATOM   1873 C  CG  . LEU A 1 232 ? 21.669  -0.304  -37.506 1.00 22.52 ? 232 LEU A CG  1 
ATOM   1874 C  CD1 . LEU A 1 232 ? 23.133  0.104   -37.438 1.00 26.02 ? 232 LEU A CD1 1 
ATOM   1875 C  CD2 . LEU A 1 232 ? 21.356  -1.048  -38.807 1.00 24.42 ? 232 LEU A CD2 1 
ATOM   1876 N  N   . CYS A 1 233 ? 20.083  -3.982  -35.221 1.00 19.63 ? 233 CYS A N   1 
ATOM   1877 C  CA  . CYS A 1 233 ? 20.136  -4.857  -34.041 1.00 19.36 ? 233 CYS A CA  1 
ATOM   1878 C  C   . CYS A 1 233 ? 21.572  -4.971  -33.542 1.00 21.24 ? 233 CYS A C   1 
ATOM   1879 O  O   . CYS A 1 233 ? 21.838  -5.695  -32.585 1.00 23.84 ? 233 CYS A O   1 
ATOM   1880 C  CB  . CYS A 1 233 ? 19.511  -6.259  -34.242 1.00 17.94 ? 233 CYS A CB  1 
ATOM   1881 S  SG  . CYS A 1 233 ? 20.328  -7.191  -35.643 1.00 25.10 ? 233 CYS A SG  1 
ATOM   1882 N  N   . THR A 1 234 ? 22.442  -4.240  -34.199 1.00 22.89 ? 234 THR A N   1 
ATOM   1883 C  CA  . THR A 1 234 ? 23.873  -4.207  -33.866 1.00 23.79 ? 234 THR A CA  1 
ATOM   1884 C  C   . THR A 1 234 ? 24.318  -2.863  -33.286 1.00 24.29 ? 234 THR A C   1 
ATOM   1885 O  O   . THR A 1 234 ? 23.759  -1.823  -33.546 1.00 23.30 ? 234 THR A O   1 
ATOM   1886 C  CB  . THR A 1 234 ? 24.703  -4.490  -35.148 1.00 23.63 ? 234 THR A CB  1 
ATOM   1887 O  OG1 . THR A 1 234 ? 24.249  -3.625  -36.218 1.00 24.21 ? 234 THR A OG1 1 
ATOM   1888 C  CG2 . THR A 1 234 ? 24.599  -5.972  -35.510 1.00 26.63 ? 234 THR A CG2 1 
ATOM   1889 N  N   . ALA A 1 235 ? 25.388  -2.895  -32.475 1.00 23.87 ? 235 ALA A N   1 
ATOM   1890 C  CA  . ALA A 1 235 ? 25.877  -1.692  -31.836 1.00 31.20 ? 235 ALA A CA  1 
ATOM   1891 C  C   . ALA A 1 235 ? 26.866  -0.921  -32.739 1.00 34.60 ? 235 ALA A C   1 
ATOM   1892 O  O   . ALA A 1 235 ? 27.354  -1.456  -33.726 1.00 34.14 ? 235 ALA A O   1 
ATOM   1893 C  CB  . ALA A 1 235 ? 26.496  -2.045  -30.449 1.00 31.86 ? 235 ALA A CB  1 
ATOM   1894 N  N   . GLU A 1 236 ? 27.091  0.346   -32.451 1.00 34.92 ? 236 GLU A N   1 
ATOM   1895 C  CA  . GLU A 1 236 ? 28.101  1.136   -33.148 1.00 42.01 ? 236 GLU A CA  1 
ATOM   1896 C  C   . GLU A 1 236 ? 29.476  0.410   -33.249 1.00 43.28 ? 236 GLU A C   1 
ATOM   1897 O  O   . GLU A 1 236 ? 29.943  -0.183  -32.265 1.00 39.77 ? 236 GLU A O   1 
ATOM   1898 C  CB  . GLU A 1 236 ? 28.300  2.419   -32.369 1.00 43.86 ? 236 GLU A CB  1 
ATOM   1899 C  CG  . GLU A 1 236 ? 28.694  3.615   -33.212 1.00 55.16 ? 236 GLU A CG  1 
ATOM   1900 N  N   . GLY A 1 237 ? 30.098  0.461   -34.429 1.00 48.49 ? 237 GLY A N   1 
ATOM   1901 C  CA  . GLY A 1 237 ? 31.457  -0.061  -34.633 1.00 51.66 ? 237 GLY A CA  1 
ATOM   1902 C  C   . GLY A 1 237 ? 31.439  -1.543  -34.906 1.00 55.24 ? 237 GLY A C   1 
ATOM   1903 O  O   . GLY A 1 237 ? 32.464  -2.232  -34.792 1.00 53.16 ? 237 GLY A O   1 
ATOM   1904 N  N   . GLU A 1 238 ? 30.253  -2.028  -35.264 1.00 50.08 ? 238 GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 238 ? 30.025  -3.439  -35.456 1.00 50.24 ? 238 GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 238 ? 29.368  -3.559  -36.835 1.00 49.69 ? 238 GLU A C   1 
ATOM   1907 O  O   . GLU A 1 238 ? 28.705  -2.620  -37.278 1.00 49.27 ? 238 GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 238 ? 29.143  -3.955  -34.319 1.00 51.33 ? 238 GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 238 ? 29.047  -5.453  -34.193 1.00 55.18 ? 238 GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 238 ? 27.849  -5.898  -33.367 1.00 59.77 ? 238 GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 238 ? 27.482  -5.217  -32.373 1.00 61.69 ? 238 GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 238 ? 27.274  -6.955  -33.699 1.00 60.60 ? 238 GLU A OE2 1 
ATOM   1913 N  N   . ALA A 1 239 ? 29.609  -4.660  -37.550 1.00 45.70 ? 239 ALA A N   1 
ATOM   1914 C  CA  . ALA A 1 239 ? 29.030  -4.824  -38.891 1.00 37.67 ? 239 ALA A CA  1 
ATOM   1915 C  C   . ALA A 1 239 ? 27.503  -4.748  -38.742 1.00 31.24 ? 239 ALA A C   1 
ATOM   1916 O  O   . ALA A 1 239 ? 26.901  -5.502  -37.935 1.00 31.19 ? 239 ALA A O   1 
ATOM   1917 C  CB  . ALA A 1 239 ? 29.424  -6.164  -39.485 1.00 34.32 ? 239 ALA A CB  1 
ATOM   1918 N  N   . ALA A 1 240 ? 26.915  -3.827  -39.497 1.00 36.15 ? 240 ALA A N   1 
ATOM   1919 C  CA  . ALA A 1 240 ? 25.484  -3.593  -39.386 1.00 27.74 ? 240 ALA A CA  1 
ATOM   1920 C  C   . ALA A 1 240 ? 24.594  -4.773  -39.799 1.00 30.01 ? 240 ALA A C   1 
ATOM   1921 O  O   . ALA A 1 240 ? 24.834  -5.461  -40.790 1.00 27.28 ? 240 ALA A O   1 
ATOM   1922 C  CB  . ALA A 1 240 ? 25.075  -2.312  -40.104 1.00 27.59 ? 240 ALA A CB  1 
ATOM   1923 N  N   . ALA A 1 241 ? 23.518  -4.960  -39.024 1.00 22.89 ? 241 ALA A N   1 
ATOM   1924 C  CA  . ALA A 1 241 ? 22.447  -5.853  -39.406 1.00 21.46 ? 241 ALA A CA  1 
ATOM   1925 C  C   . ALA A 1 241 ? 21.223  -5.051  -39.020 1.00 22.48 ? 241 ALA A C   1 
ATOM   1926 O  O   . ALA A 1 241 ? 21.200  -4.372  -37.957 1.00 23.00 ? 241 ALA A O   1 
ATOM   1927 C  CB  . ALA A 1 241 ? 22.429  -7.207  -38.680 1.00 21.35 ? 241 ALA A CB  1 
ATOM   1928 N  N   . PHE A 1 242 ? 20.191  -5.204  -39.830 1.00 17.44 ? 242 PHE A N   1 
ATOM   1929 C  CA  . PHE A 1 242 ? 18.969  -4.420  -39.688 1.00 18.16 ? 242 PHE A CA  1 
ATOM   1930 C  C   . PHE A 1 242 ? 17.906  -5.217  -38.969 1.00 15.74 ? 242 PHE A C   1 
ATOM   1931 O  O   . PHE A 1 242 ? 17.701  -6.410  -39.180 1.00 17.16 ? 242 PHE A O   1 
ATOM   1932 C  CB  . PHE A 1 242 ? 18.393  -3.987  -41.065 1.00 18.06 ? 242 PHE A CB  1 
ATOM   1933 C  CG  . PHE A 1 242 ? 19.242  -2.975  -41.735 1.00 19.59 ? 242 PHE A CG  1 
ATOM   1934 C  CD1 . PHE A 1 242 ? 20.287  -3.415  -42.564 1.00 22.86 ? 242 PHE A CD1 1 
ATOM   1935 C  CD2 . PHE A 1 242 ? 19.090  -1.615  -41.520 1.00 22.39 ? 242 PHE A CD2 1 
ATOM   1936 C  CE1 . PHE A 1 242 ? 21.124  -2.507  -43.196 1.00 23.59 ? 242 PHE A CE1 1 
ATOM   1937 C  CE2 . PHE A 1 242 ? 19.985  -0.689  -42.141 1.00 28.01 ? 242 PHE A CE2 1 
ATOM   1938 C  CZ  . PHE A 1 242 ? 20.998  -1.154  -42.987 1.00 22.19 ? 242 PHE A CZ  1 
ATOM   1939 N  N   . LEU A 1 243 ? 17.156  -4.484  -38.118 1.00 16.06 ? 243 LEU A N   1 
ATOM   1940 C  CA  . LEU A 1 243 ? 16.020  -5.073  -37.396 1.00 16.04 ? 243 LEU A CA  1 
ATOM   1941 C  C   . LEU A 1 243 ? 14.741  -5.057  -38.370 1.00 14.42 ? 243 LEU A C   1 
ATOM   1942 O  O   . LEU A 1 243 ? 13.781  -4.281  -38.178 1.00 15.14 ? 243 LEU A O   1 
ATOM   1943 C  CB  . LEU A 1 243 ? 15.805  -4.196  -36.084 1.00 15.16 ? 243 LEU A CB  1 
ATOM   1944 C  CG  . LEU A 1 243 ? 14.786  -4.811  -35.118 1.00 17.69 ? 243 LEU A CG  1 
ATOM   1945 C  CD1 . LEU A 1 243 ? 15.255  -6.188  -34.665 1.00 17.61 ? 243 LEU A CD1 1 
ATOM   1946 C  CD2 . LEU A 1 243 ? 14.634  -3.898  -33.923 1.00 20.68 ? 243 LEU A CD2 1 
ATOM   1947 N  N   . VAL A 1 244 ? 14.764  -5.937  -39.386 1.00 15.24 ? 244 VAL A N   1 
ATOM   1948 C  CA  . VAL A 1 244 ? 13.642  -5.857  -40.349 1.00 15.92 ? 244 VAL A CA  1 
ATOM   1949 C  C   . VAL A 1 244 ? 12.416  -6.579  -39.907 1.00 14.80 ? 244 VAL A C   1 
ATOM   1950 O  O   . VAL A 1 244 ? 11.318  -6.322  -40.413 1.00 15.76 ? 244 VAL A O   1 
ATOM   1951 C  CB  . VAL A 1 244 ? 14.064  -6.351  -41.789 1.00 17.27 ? 244 VAL A CB  1 
ATOM   1952 C  CG1 . VAL A 1 244 ? 15.122  -5.374  -42.369 1.00 16.74 ? 244 VAL A CG1 1 
ATOM   1953 C  CG2 . VAL A 1 244 ? 14.542  -7.784  -41.807 1.00 17.04 ? 244 VAL A CG2 1 
ATOM   1954 N  N   . SER A 1 245 ? 12.561  -7.470  -38.867 1.00 14.79 ? 245 SER A N   1 
ATOM   1955 C  CA  . SER A 1 245 ? 11.438  -8.231  -38.397 1.00 14.66 ? 245 SER A CA  1 
ATOM   1956 C  C   . SER A 1 245 ? 11.785  -8.542  -36.934 1.00 14.81 ? 245 SER A C   1 
ATOM   1957 O  O   . SER A 1 245 ? 12.888  -8.897  -36.586 1.00 15.30 ? 245 SER A O   1 
ATOM   1958 C  CB  . SER A 1 245 ? 11.254  -9.573  -39.157 1.00 14.96 ? 245 SER A CB  1 
ATOM   1959 O  OG  . SER A 1 245 ? 10.039  -10.239 -38.818 1.00 16.36 ? 245 SER A OG  1 
ATOM   1960 N  N   . ASN A 1 246 ? 10.746  -8.446  -36.119 1.00 13.79 ? 246 ASN A N   1 
ATOM   1961 C  CA  . ASN A 1 246 ? 10.978  -8.679  -34.652 1.00 12.66 ? 246 ASN A CA  1 
ATOM   1962 C  C   . ASN A 1 246 ? 9.701   -9.177  -34.011 1.00 12.46 ? 246 ASN A C   1 
ATOM   1963 O  O   . ASN A 1 246 ? 9.408   -8.755  -32.845 1.00 12.87 ? 246 ASN A O   1 
ATOM   1964 C  CB  . ASN A 1 246 ? 11.529  -7.433  -33.998 1.00 12.41 ? 246 ASN A CB  1 
ATOM   1965 C  CG  . ASN A 1 246 ? 10.526  -6.299  -34.000 1.00 11.62 ? 246 ASN A CG  1 
ATOM   1966 O  OD1 . ASN A 1 246 ? 9.535   -6.383  -34.673 1.00 12.22 ? 246 ASN A OD1 1 
ATOM   1967 N  ND2 . ASN A 1 246 ? 10.742  -5.282  -33.212 1.00 12.12 ? 246 ASN A ND2 1 
ATOM   1968 N  N   . HIS A 1 247 ? 8.976   -10.117 -34.606 1.00 11.50 ? 247 HIS A N   1 
ATOM   1969 C  CA  . HIS A 1 247 ? 7.790   -10.737 -34.064 1.00 12.52 ? 247 HIS A CA  1 
ATOM   1970 C  C   . HIS A 1 247 ? 7.900   -12.220 -33.846 1.00 13.35 ? 247 HIS A C   1 
ATOM   1971 O  O   . HIS A 1 247 ? 8.438   -12.961 -34.725 1.00 16.32 ? 247 HIS A O   1 
ATOM   1972 C  CB  . HIS A 1 247 ? 6.534   -10.371 -34.902 1.00 13.41 ? 247 HIS A CB  1 
ATOM   1973 C  CG  . HIS A 1 247 ? 6.580   -10.963 -36.330 1.00 14.37 ? 247 HIS A CG  1 
ATOM   1974 N  ND1 . HIS A 1 247 ? 5.886   -12.083 -36.694 1.00 17.63 ? 247 HIS A ND1 1 
ATOM   1975 C  CD2 . HIS A 1 247 ? 7.310   -10.554 -37.403 1.00 14.04 ? 247 HIS A CD2 1 
ATOM   1976 C  CE1 . HIS A 1 247 ? 6.156   -12.313 -38.024 1.00 17.37 ? 247 HIS A CE1 1 
ATOM   1977 N  NE2 . HIS A 1 247 ? 7.020   -11.436 -38.420 1.00 17.17 ? 247 HIS A NE2 1 
ATOM   1978 N  N   . ARG A 1 248 ? 7.409   -12.729 -32.733 1.00 12.73 ? 248 ARG A N   1 
ATOM   1979 C  CA  . ARG A 1 248 ? 7.448   -14.182 -32.468 1.00 13.06 ? 248 ARG A CA  1 
ATOM   1980 C  C   . ARG A 1 248 ? 6.128   -14.715 -33.028 1.00 13.98 ? 248 ARG A C   1 
ATOM   1981 O  O   . ARG A 1 248 ? 5.049   -14.106 -32.889 1.00 14.21 ? 248 ARG A O   1 
ATOM   1982 C  CB  . ARG A 1 248 ? 7.408   -14.328 -30.928 1.00 13.65 ? 248 ARG A CB  1 
ATOM   1983 C  CG  . ARG A 1 248 ? 7.534   -15.839 -30.531 1.00 13.43 ? 248 ARG A CG  1 
ATOM   1984 C  CD  . ARG A 1 248 ? 7.342   -16.095 -29.048 1.00 13.81 ? 248 ARG A CD  1 
ATOM   1985 N  NE  . ARG A 1 248 ? 7.887   -17.418 -28.760 1.00 15.28 ? 248 ARG A NE  1 
ATOM   1986 C  CZ  . ARG A 1 248 ? 7.617   -18.147 -27.680 1.00 17.10 ? 248 ARG A CZ  1 
ATOM   1987 N  NH1 . ARG A 1 248 ? 6.809   -17.683 -26.735 1.00 15.37 ? 248 ARG A NH1 1 
ATOM   1988 N  NH2 . ARG A 1 248 ? 8.171   -19.348 -27.539 1.00 18.06 ? 248 ARG A NH2 1 
ATOM   1989 N  N   . PRO A 1 249 ? 6.162   -15.923 -33.644 1.00 15.34 ? 249 PRO A N   1 
ATOM   1990 C  CA  . PRO A 1 249 ? 4.904   -16.516 -34.042 1.00 15.22 ? 249 PRO A CA  1 
ATOM   1991 C  C   . PRO A 1 249 ? 4.001   -16.978 -32.895 1.00 16.05 ? 249 PRO A C   1 
ATOM   1992 O  O   . PRO A 1 249 ? 4.542   -17.220 -31.775 1.00 15.50 ? 249 PRO A O   1 
ATOM   1993 C  CB  . PRO A 1 249 ? 5.326   -17.809 -34.831 1.00 17.79 ? 249 PRO A CB  1 
ATOM   1994 C  CG  . PRO A 1 249 ? 6.786   -17.701 -35.007 1.00 19.37 ? 249 PRO A CG  1 
ATOM   1995 C  CD  . PRO A 1 249 ? 7.363   -16.679 -33.974 1.00 16.93 ? 249 PRO A CD  1 
ATOM   1996 N  N   . PRO A 1 250 ? 2.704   -17.084 -33.096 1.00 15.73 ? 250 PRO A N   1 
ATOM   1997 C  CA  . PRO A 1 250 ? 1.807   -17.584 -32.038 1.00 16.46 ? 250 PRO A CA  1 
ATOM   1998 C  C   . PRO A 1 250 ? 2.206   -18.956 -31.589 1.00 17.17 ? 250 PRO A C   1 
ATOM   1999 O  O   . PRO A 1 250 ? 2.583   -19.819 -32.468 1.00 17.58 ? 250 PRO A O   1 
ATOM   2000 C  CB  . PRO A 1 250 ? 0.408   -17.638 -32.714 1.00 17.96 ? 250 PRO A CB  1 
ATOM   2001 C  CG  . PRO A 1 250 ? 0.483   -16.637 -33.836 1.00 19.61 ? 250 PRO A CG  1 
ATOM   2002 C  CD  . PRO A 1 250 ? 1.903   -16.663 -34.321 1.00 18.22 ? 250 PRO A CD  1 
ATOM   2003 N  N   . GLN A 1 251 ? 1.959   -19.225 -30.311 1.00 15.20 ? 251 GLN A N   1 
ATOM   2004 C  CA  . GLN A 1 251 ? 2.248   -20.511 -29.691 1.00 15.81 ? 251 GLN A CA  1 
ATOM   2005 C  C   . GLN A 1 251 ? 0.875   -21.139 -29.338 1.00 14.74 ? 251 GLN A C   1 
ATOM   2006 O  O   . GLN A 1 251 ? -0.151  -20.460 -29.183 1.00 15.05 ? 251 GLN A O   1 
ATOM   2007 C  CB  . GLN A 1 251 ? 3.073   -20.217 -28.432 1.00 16.16 ? 251 GLN A CB  1 
ATOM   2008 C  CG  . GLN A 1 251 ? 4.389   -19.537 -28.760 1.00 16.31 ? 251 GLN A CG  1 
ATOM   2009 C  CD  . GLN A 1 251 ? 5.214   -20.316 -29.771 1.00 18.44 ? 251 GLN A CD  1 
ATOM   2010 O  OE1 . GLN A 1 251 ? 5.488   -21.536 -29.591 1.00 21.25 ? 251 GLN A OE1 1 
ATOM   2011 N  NE2 . GLN A 1 251 ? 5.541   -19.670 -30.896 1.00 19.59 ? 251 GLN A NE2 1 
ATOM   2012 N  N   . PRO A 1 252 ? 0.820   -22.471 -29.135 1.00 17.99 ? 252 PRO A N   1 
ATOM   2013 C  CA  . PRO A 1 252 ? -0.453  -23.132 -28.866 1.00 19.23 ? 252 PRO A CA  1 
ATOM   2014 C  C   . PRO A 1 252 ? -1.066  -22.732 -27.535 1.00 18.48 ? 252 PRO A C   1 
ATOM   2015 O  O   . PRO A 1 252 ? -0.320  -22.541 -26.547 1.00 19.31 ? 252 PRO A O   1 
ATOM   2016 C  CB  . PRO A 1 252 ? -0.047  -24.642 -28.825 1.00 17.75 ? 252 PRO A CB  1 
ATOM   2017 C  CG  . PRO A 1 252 ? 1.151   -24.708 -29.612 1.00 18.33 ? 252 PRO A CG  1 
ATOM   2018 C  CD  . PRO A 1 252 ? 1.934   -23.423 -29.272 1.00 18.88 ? 252 PRO A CD  1 
ATOM   2019 N  N   . LEU A 1 253 ? -2.396  -22.747 -27.493 1.00 19.54 ? 253 LEU A N   1 
ATOM   2020 C  CA  . LEU A 1 253 ? -3.161  -22.401 -26.296 1.00 18.85 ? 253 LEU A CA  1 
ATOM   2021 C  C   . LEU A 1 253 ? -2.978  -23.375 -25.200 1.00 23.49 ? 253 LEU A C   1 
ATOM   2022 O  O   . LEU A 1 253 ? -2.988  -22.995 -24.052 1.00 20.67 ? 253 LEU A O   1 
ATOM   2023 C  CB  . LEU A 1 253 ? -4.658  -22.277 -26.654 1.00 25.84 ? 253 LEU A CB  1 
ATOM   2024 C  CG  . LEU A 1 253 ? -4.949  -20.929 -27.237 1.00 28.31 ? 253 LEU A CG  1 
ATOM   2025 C  CD1 . LEU A 1 253 ? -6.370  -21.005 -27.779 1.00 33.68 ? 253 LEU A CD1 1 
ATOM   2026 C  CD2 . LEU A 1 253 ? -4.843  -19.853 -26.151 1.00 27.52 ? 253 LEU A CD2 1 
ATOM   2027 N  N   A LYS A 1 254 ? -2.860  -24.653 -25.577 0.50 21.70 ? 254 LYS A N   1 
ATOM   2028 N  N   B LYS A 1 254 ? -2.832  -24.654 -25.563 0.50 21.91 ? 254 LYS A N   1 
ATOM   2029 C  CA  A LYS A 1 254 ? -2.632  -25.740 -24.627 0.50 25.01 ? 254 LYS A CA  1 
ATOM   2030 C  CA  B LYS A 1 254 ? -2.593  -25.715 -24.583 0.50 25.14 ? 254 LYS A CA  1 
ATOM   2031 C  C   A LYS A 1 254 ? -3.624  -25.702 -23.491 0.50 24.80 ? 254 LYS A C   1 
ATOM   2032 C  C   B LYS A 1 254 ? -3.623  -25.682 -23.470 0.50 24.93 ? 254 LYS A C   1 
ATOM   2033 O  O   A LYS A 1 254 ? -3.233  -25.895 -22.330 0.50 28.69 ? 254 LYS A O   1 
ATOM   2034 O  O   B LYS A 1 254 ? -3.259  -25.857 -22.299 0.50 28.69 ? 254 LYS A O   1 
ATOM   2035 C  CB  A LYS A 1 254 ? -1.203  -25.700 -24.070 0.50 26.55 ? 254 LYS A CB  1 
ATOM   2036 C  CB  B LYS A 1 254 ? -1.173  -25.623 -23.980 0.50 26.87 ? 254 LYS A CB  1 
ATOM   2037 C  CG  A LYS A 1 254 ? -0.125  -25.751 -25.144 0.50 27.64 ? 254 LYS A CG  1 
ATOM   2038 C  CG  B LYS A 1 254 ? -0.033  -25.869 -24.968 0.50 28.48 ? 254 LYS A CG  1 
ATOM   2039 C  CD  A LYS A 1 254 ? 0.552   -27.101 -25.173 0.50 30.48 ? 254 LYS A CD  1 
ATOM   2040 C  CD  B LYS A 1 254 ? 0.107   -27.345 -25.268 0.50 30.55 ? 254 LYS A CD  1 
ATOM   2041 C  CE  A LYS A 1 254 ? 1.931   -27.037 -25.795 0.50 33.24 ? 254 LYS A CE  1 
ATOM   2042 C  CE  B LYS A 1 254 ? 1.508   -27.759 -25.692 0.50 32.50 ? 254 LYS A CE  1 
ATOM   2043 N  NZ  A LYS A 1 254 ? 2.895   -26.327 -24.910 0.50 35.71 ? 254 LYS A NZ  1 
ATOM   2044 N  NZ  B LYS A 1 254 ? 1.622   -29.250 -25.649 0.50 33.66 ? 254 LYS A NZ  1 
ATOM   2045 N  N   . GLY A 1 255 ? -4.887  -25.449 -23.805 1.00 23.76 ? 255 GLY A N   1 
ATOM   2046 C  CA  . GLY A 1 255 ? -5.949  -25.563 -22.799 1.00 24.22 ? 255 GLY A CA  1 
ATOM   2047 C  C   . GLY A 1 255 ? -6.451  -24.263 -22.232 1.00 23.88 ? 255 GLY A C   1 
ATOM   2048 O  O   . GLY A 1 255 ? -7.508  -24.219 -21.577 1.00 24.37 ? 255 GLY A O   1 
ATOM   2049 N  N   . ARG A 1 256 ? -5.706  -23.161 -22.469 1.00 22.44 ? 256 ARG A N   1 
ATOM   2050 C  CA  . ARG A 1 256 ? -6.191  -21.906 -21.984 1.00 22.25 ? 256 ARG A CA  1 
ATOM   2051 C  C   . ARG A 1 256 ? -7.384  -21.401 -22.758 1.00 23.47 ? 256 ARG A C   1 
ATOM   2052 O  O   . ARG A 1 256 ? -7.513  -21.706 -23.958 1.00 26.16 ? 256 ARG A O   1 
ATOM   2053 C  CB  . ARG A 1 256 ? -5.069  -20.832 -22.155 1.00 22.46 ? 256 ARG A CB  1 
ATOM   2054 C  CG  . ARG A 1 256 ? -3.877  -21.088 -21.231 1.00 20.84 ? 256 ARG A CG  1 
ATOM   2055 C  CD  . ARG A 1 256 ? -2.682  -20.150 -21.651 1.00 20.30 ? 256 ARG A CD  1 
ATOM   2056 N  NE  . ARG A 1 256 ? -2.091  -20.536 -22.941 1.00 19.91 ? 256 ARG A NE  1 
ATOM   2057 C  CZ  . ARG A 1 256 ? -1.175  -19.825 -23.585 1.00 17.25 ? 256 ARG A CZ  1 
ATOM   2058 N  NH1 . ARG A 1 256 ? -0.755  -18.634 -23.045 1.00 16.14 ? 256 ARG A NH1 1 
ATOM   2059 N  NH2 . ARG A 1 256 ? -0.619  -20.231 -24.647 1.00 16.66 ? 256 ARG A NH2 1 
ATOM   2060 N  N   . LYS A 1 257 ? -8.249  -20.654 -22.097 1.00 23.14 ? 257 LYS A N   1 
ATOM   2061 C  CA  . LYS A 1 257 ? -9.335  -20.040 -22.790 1.00 26.05 ? 257 LYS A CA  1 
ATOM   2062 C  C   . LYS A 1 257 ? -9.131  -18.488 -22.841 1.00 24.40 ? 257 LYS A C   1 
ATOM   2063 O  O   . LYS A 1 257 ? -8.599  -17.820 -21.924 1.00 29.77 ? 257 LYS A O   1 
ATOM   2064 C  CB  . LYS A 1 257 ? -10.703 -20.426 -22.211 1.00 28.92 ? 257 LYS A CB  1 
ATOM   2065 C  CG  . LYS A 1 257 ? -11.017 -21.938 -22.262 1.00 29.95 ? 257 LYS A CG  1 
ATOM   2066 C  CD  . LYS A 1 257 ? -12.216 -22.258 -21.375 1.00 38.51 ? 257 LYS A CD  1 
ATOM   2067 C  CE  . LYS A 1 257 ? -12.572 -23.745 -21.350 1.00 34.65 ? 257 LYS A CE  1 
ATOM   2068 N  NZ  . LYS A 1 257 ? -11.624 -24.533 -20.543 1.00 41.44 ? 257 LYS A NZ  1 
ATOM   2069 N  N   . VAL A 1 258 ? -9.516  -17.913 -23.943 1.00 23.75 ? 258 VAL A N   1 
ATOM   2070 C  CA  . VAL A 1 258 ? -9.510  -16.489 -24.123 1.00 21.99 ? 258 VAL A CA  1 
ATOM   2071 C  C   . VAL A 1 258 ? -10.868 -15.883 -23.769 1.00 20.58 ? 258 VAL A C   1 
ATOM   2072 O  O   . VAL A 1 258 ? -11.906 -16.427 -24.196 1.00 24.70 ? 258 VAL A O   1 
ATOM   2073 C  CB  . VAL A 1 258 ? -9.088  -16.190 -25.556 1.00 19.65 ? 258 VAL A CB  1 
ATOM   2074 C  CG1 . VAL A 1 258 ? -9.047  -14.660 -25.801 1.00 19.03 ? 258 VAL A CG1 1 
ATOM   2075 C  CG2 . VAL A 1 258 ? -7.776  -16.932 -25.869 1.00 17.99 ? 258 VAL A CG2 1 
ATOM   2076 N  N   . ARG A 1 259 ? -10.926 -14.816 -22.986 1.00 21.75 ? 259 ARG A N   1 
ATOM   2077 C  CA  . ARG A 1 259 ? -12.199 -14.120 -22.614 1.00 20.29 ? 259 ARG A CA  1 
ATOM   2078 C  C   . ARG A 1 259 ? -12.349 -12.853 -23.354 1.00 20.51 ? 259 ARG A C   1 
ATOM   2079 O  O   . ARG A 1 259 ? -11.334 -12.181 -23.608 1.00 20.40 ? 259 ARG A O   1 
ATOM   2080 C  CB  . ARG A 1 259 ? -12.244 -13.841 -21.104 1.00 21.75 ? 259 ARG A CB  1 
ATOM   2081 C  CG  . ARG A 1 259 ? -12.182 -15.172 -20.353 1.00 22.93 ? 259 ARG A CG  1 
ATOM   2082 C  CD  . ARG A 1 259 ? -12.273 -14.856 -18.872 1.00 29.21 ? 259 ARG A CD  1 
ATOM   2083 N  NE  . ARG A 1 259 ? -11.019 -14.217 -18.418 1.00 29.99 ? 259 ARG A NE  1 
ATOM   2084 C  CZ  . ARG A 1 259 ? -10.925 -13.406 -17.361 1.00 30.03 ? 259 ARG A CZ  1 
ATOM   2085 N  NH1 . ARG A 1 259 ? -11.987 -13.052 -16.663 1.00 30.91 ? 259 ARG A NH1 1 
ATOM   2086 N  NH2 . ARG A 1 259 ? -9.742  -12.937 -17.000 1.00 28.71 ? 259 ARG A NH2 1 
ATOM   2087 N  N   . ALA A 1 260 ? -13.584 -12.399 -23.609 1.00 21.07 ? 260 ALA A N   1 
ATOM   2088 C  CA  . ALA A 1 260 ? -13.834 -11.127 -24.298 1.00 22.59 ? 260 ALA A CA  1 
ATOM   2089 C  C   . ALA A 1 260 ? -14.527 -10.134 -23.374 1.00 22.45 ? 260 ALA A C   1 
ATOM   2090 O  O   . ALA A 1 260 ? -15.382 -10.540 -22.542 1.00 23.58 ? 260 ALA A O   1 
ATOM   2091 C  CB  . ALA A 1 260 ? -14.723 -11.323 -25.548 1.00 21.30 ? 260 ALA A CB  1 
ATOM   2092 N  N   . SER A 1 261 ? -14.195 -8.848  -23.567 1.00 20.08 ? 261 SER A N   1 
ATOM   2093 C  CA  . SER A 1 261 ? -14.767 -7.785  -22.805 1.00 20.17 ? 261 SER A CA  1 
ATOM   2094 C  C   . SER A 1 261 ? -16.158 -7.350  -23.295 1.00 23.11 ? 261 SER A C   1 
ATOM   2095 O  O   . SER A 1 261 ? -16.807 -6.525  -22.655 1.00 26.12 ? 261 SER A O   1 
ATOM   2096 C  CB  . SER A 1 261 ? -13.889 -6.554  -22.786 1.00 17.50 ? 261 SER A CB  1 
ATOM   2097 O  OG  . SER A 1 261 ? -13.839 -5.795  -23.983 1.00 17.23 ? 261 SER A OG  1 
ATOM   2098 N  N   . PHE A 1 262 ? -16.562 -7.858  -24.454 1.00 22.63 ? 262 PHE A N   1 
ATOM   2099 C  CA  . PHE A 1 262 ? -17.622 -7.273  -25.269 1.00 23.99 ? 262 PHE A CA  1 
ATOM   2100 C  C   . PHE A 1 262 ? -18.482 -8.447  -25.799 1.00 25.76 ? 262 PHE A C   1 
ATOM   2101 O  O   . PHE A 1 262 ? -17.983 -9.544  -25.884 1.00 25.03 ? 262 PHE A O   1 
ATOM   2102 C  CB  . PHE A 1 262 ? -17.029 -6.394  -26.411 1.00 22.31 ? 262 PHE A CB  1 
ATOM   2103 C  CG  . PHE A 1 262 ? -16.111 -7.159  -27.293 1.00 24.78 ? 262 PHE A CG  1 
ATOM   2104 C  CD1 . PHE A 1 262 ? -16.604 -7.795  -28.454 1.00 25.61 ? 262 PHE A CD1 1 
ATOM   2105 C  CD2 . PHE A 1 262 ? -14.742 -7.347  -26.961 1.00 22.01 ? 262 PHE A CD2 1 
ATOM   2106 C  CE1 . PHE A 1 262 ? -15.762 -8.560  -29.234 1.00 23.88 ? 262 PHE A CE1 1 
ATOM   2107 C  CE2 . PHE A 1 262 ? -13.903 -8.109  -27.758 1.00 22.71 ? 262 PHE A CE2 1 
ATOM   2108 C  CZ  . PHE A 1 262 ? -14.411 -8.729  -28.892 1.00 26.61 ? 262 PHE A CZ  1 
ATOM   2109 N  N   . HIS A 1 263 ? -19.785 -8.216  -26.067 1.00 33.24 ? 263 HIS A N   1 
ATOM   2110 C  CA  . HIS A 1 263 ? -20.603 -9.340  -26.609 1.00 42.88 ? 263 HIS A CA  1 
ATOM   2111 C  C   . HIS A 1 263 ? -20.994 -9.090  -28.012 1.00 50.69 ? 263 HIS A C   1 
ATOM   2112 O  O   . HIS A 1 263 ? -22.145 -9.220  -28.429 1.00 53.11 ? 263 HIS A O   1 
ATOM   2113 C  CB  . HIS A 1 263 ? -21.795 -9.838  -25.744 1.00 50.49 ? 263 HIS A CB  1 
ATOM   2114 C  CG  . HIS A 1 263 ? -22.465 -8.787  -24.896 1.00 56.08 ? 263 HIS A CG  1 
ATOM   2115 N  ND1 . HIS A 1 263 ? -22.618 -7.504  -25.294 1.00 68.70 ? 263 HIS A ND1 1 
ATOM   2116 C  CD2 . HIS A 1 263 ? -23.065 -8.881  -23.630 1.00 63.32 ? 263 HIS A CD2 1 
ATOM   2117 C  CE1 . HIS A 1 263 ? -23.260 -6.797  -24.318 1.00 69.76 ? 263 HIS A CE1 1 
ATOM   2118 N  NE2 . HIS A 1 263 ? -23.530 -7.640  -23.303 1.00 69.55 ? 263 HIS A NE2 1 
ATOM   2119 O  OXT . HIS A 1 263 ? -20.112 -8.744  -28.777 1.00 51.57 ? 263 HIS A OXT 1 
ATOM   2120 N  N   . SER B 1 6   ? -29.591 41.614  -12.552 1.00 46.21 ? 6   SER B N   1 
ATOM   2121 C  CA  . SER B 1 6   ? -29.040 40.409  -13.259 1.00 48.67 ? 6   SER B CA  1 
ATOM   2122 C  C   . SER B 1 6   ? -28.938 39.187  -12.335 1.00 46.83 ? 6   SER B C   1 
ATOM   2123 O  O   . SER B 1 6   ? -28.992 39.298  -11.099 1.00 47.76 ? 6   SER B O   1 
ATOM   2124 C  CB  . SER B 1 6   ? -27.678 40.705  -13.905 1.00 51.83 ? 6   SER B CB  1 
ATOM   2125 O  OG  . SER B 1 6   ? -27.492 39.908  -15.069 1.00 50.96 ? 6   SER B OG  1 
ATOM   2126 N  N   . TRP B 1 7   ? -28.758 38.018  -12.937 1.00 35.96 ? 7   TRP B N   1 
ATOM   2127 C  CA  . TRP B 1 7   ? -28.950 36.755  -12.226 1.00 27.98 ? 7   TRP B CA  1 
ATOM   2128 C  C   . TRP B 1 7   ? -27.961 36.441  -11.108 1.00 24.51 ? 7   TRP B C   1 
ATOM   2129 O  O   . TRP B 1 7   ? -26.832 36.919  -11.131 1.00 28.64 ? 7   TRP B O   1 
ATOM   2130 C  CB  . TRP B 1 7   ? -29.068 35.620  -13.256 1.00 29.16 ? 7   TRP B CB  1 
ATOM   2131 C  CG  . TRP B 1 7   ? -27.743 35.236  -13.853 1.00 27.18 ? 7   TRP B CG  1 
ATOM   2132 C  CD1 . TRP B 1 7   ? -27.093 35.724  -15.013 1.00 26.04 ? 7   TRP B CD1 1 
ATOM   2133 C  CD2 . TRP B 1 7   ? -26.849 34.212  -13.327 1.00 23.99 ? 7   TRP B CD2 1 
ATOM   2134 N  NE1 . TRP B 1 7   ? -25.911 35.094  -15.201 1.00 27.68 ? 7   TRP B NE1 1 
ATOM   2135 C  CE2 . TRP B 1 7   ? -25.711 34.152  -14.238 1.00 25.08 ? 7   TRP B CE2 1 
ATOM   2136 C  CE3 . TRP B 1 7   ? -26.937 33.309  -12.275 1.00 24.89 ? 7   TRP B CE3 1 
ATOM   2137 C  CZ2 . TRP B 1 7   ? -24.662 33.281  -14.040 1.00 23.95 ? 7   TRP B CZ2 1 
ATOM   2138 C  CZ3 . TRP B 1 7   ? -25.879 32.428  -12.090 1.00 23.87 ? 7   TRP B CZ3 1 
ATOM   2139 C  CH2 . TRP B 1 7   ? -24.778 32.413  -12.961 1.00 25.15 ? 7   TRP B CH2 1 
ATOM   2140 N  N   . GLY B 1 8   ? -28.399 35.689  -10.114 1.00 22.80 ? 8   GLY B N   1 
ATOM   2141 C  CA  . GLY B 1 8   ? -27.496 35.118  -9.107  1.00 22.35 ? 8   GLY B CA  1 
ATOM   2142 C  C   . GLY B 1 8   ? -28.128 34.008  -8.291  1.00 19.54 ? 8   GLY B C   1 
ATOM   2143 O  O   . GLY B 1 8   ? -28.898 33.196  -8.818  1.00 22.09 ? 8   GLY B O   1 
ATOM   2144 N  N   . TYR B 1 9   ? -27.772 33.934  -6.997  1.00 20.53 ? 9   TYR B N   1 
ATOM   2145 C  CA  . TYR B 1 9   ? -28.325 32.895  -6.169  1.00 21.79 ? 9   TYR B CA  1 
ATOM   2146 C  C   . TYR B 1 9   ? -28.939 33.473  -4.894  1.00 24.16 ? 9   TYR B C   1 
ATOM   2147 O  O   . TYR B 1 9   ? -29.140 32.726  -3.933  1.00 26.75 ? 9   TYR B O   1 
ATOM   2148 C  CB  . TYR B 1 9   ? -27.195 31.927  -5.754  1.00 21.49 ? 9   TYR B CB  1 
ATOM   2149 C  CG  . TYR B 1 9   ? -26.583 31.155  -6.945  1.00 17.31 ? 9   TYR B CG  1 
ATOM   2150 C  CD1 . TYR B 1 9   ? -27.170 30.005  -7.395  1.00 18.63 ? 9   TYR B CD1 1 
ATOM   2151 C  CD2 . TYR B 1 9   ? -25.491 31.642  -7.579  1.00 18.15 ? 9   TYR B CD2 1 
ATOM   2152 C  CE1 . TYR B 1 9   ? -26.576 29.282  -8.468  1.00 15.86 ? 9   TYR B CE1 1 
ATOM   2153 C  CE2 . TYR B 1 9   ? -24.881 30.948  -8.654  1.00 17.93 ? 9   TYR B CE2 1 
ATOM   2154 C  CZ  . TYR B 1 9   ? -25.493 29.829  -9.057  1.00 17.34 ? 9   TYR B CZ  1 
ATOM   2155 O  OH  . TYR B 1 9   ? -24.895 29.100  -10.066 1.00 16.73 ? 9   TYR B OH  1 
ATOM   2156 N  N   . ARG B 1 10  ? -29.263 34.753  -4.958  1.00 28.00 ? 10  ARG B N   1 
ATOM   2157 C  CA  . ARG B 1 10  ? -29.902 35.441  -3.809  1.00 31.68 ? 10  ARG B CA  1 
ATOM   2158 C  C   . ARG B 1 10  ? -31.382 35.260  -3.940  1.00 29.28 ? 10  ARG B C   1 
ATOM   2159 O  O   . ARG B 1 10  ? -31.877 34.770  -4.945  1.00 26.28 ? 10  ARG B O   1 
ATOM   2160 C  CB  . ARG B 1 10  ? -29.518 36.903  -3.798  1.00 31.43 ? 10  ARG B CB  1 
ATOM   2161 C  CG  . ARG B 1 10  ? -28.041 37.141  -3.506  1.00 35.12 ? 10  ARG B CG  1 
ATOM   2162 C  CD  . ARG B 1 10  ? -27.668 38.535  -3.948  1.00 39.84 ? 10  ARG B CD  1 
ATOM   2163 N  NE  . ARG B 1 10  ? -27.796 39.434  -2.810  1.00 45.55 ? 10  ARG B NE  1 
ATOM   2164 C  CZ  . ARG B 1 10  ? -27.212 40.619  -2.716  1.00 45.09 ? 10  ARG B CZ  1 
ATOM   2165 N  NH1 . ARG B 1 10  ? -26.445 41.082  -3.705  1.00 47.47 ? 10  ARG B NH1 1 
ATOM   2166 N  NH2 . ARG B 1 10  ? -27.388 41.331  -1.610  1.00 45.76 ? 10  ARG B NH2 1 
ATOM   2167 N  N   . GLU B 1 11  ? -32.138 35.659  -2.911  1.00 35.82 ? 11  GLU B N   1 
ATOM   2168 C  CA  . GLU B 1 11  ? -33.576 35.378  -2.928  1.00 37.70 ? 11  GLU B CA  1 
ATOM   2169 C  C   . GLU B 1 11  ? -34.256 36.036  -4.136  1.00 30.78 ? 11  GLU B C   1 
ATOM   2170 O  O   . GLU B 1 11  ? -35.122 35.439  -4.731  1.00 31.61 ? 11  GLU B O   1 
ATOM   2171 C  CB  . GLU B 1 11  ? -34.258 35.817  -1.623  1.00 46.00 ? 11  GLU B CB  1 
ATOM   2172 C  CG  . GLU B 1 11  ? -35.791 35.788  -1.675  1.00 48.67 ? 11  GLU B CG  1 
ATOM   2173 C  CD  . GLU B 1 11  ? -36.430 37.163  -1.407  1.00 59.17 ? 11  GLU B CD  1 
ATOM   2174 O  OE1 . GLU B 1 11  ? -36.095 37.819  -0.386  1.00 55.74 ? 11  GLU B OE1 1 
ATOM   2175 O  OE2 . GLU B 1 11  ? -37.270 37.601  -2.232  1.00 64.71 ? 11  GLU B OE2 1 
ATOM   2176 N  N   . HIS B 1 12  ? -33.823 37.233  -4.507  1.00 36.68 ? 12  HIS B N   1 
ATOM   2177 C  CA  . HIS B 1 12  ? -34.489 37.992  -5.549  1.00 40.10 ? 12  HIS B CA  1 
ATOM   2178 C  C   . HIS B 1 12  ? -34.128 37.613  -6.961  1.00 38.95 ? 12  HIS B C   1 
ATOM   2179 O  O   . HIS B 1 12  ? -34.904 37.889  -7.866  1.00 38.51 ? 12  HIS B O   1 
ATOM   2180 C  CB  . HIS B 1 12  ? -34.261 39.493  -5.332  1.00 48.86 ? 12  HIS B CB  1 
ATOM   2181 C  CG  . HIS B 1 12  ? -32.792 39.915  -5.390  1.00 58.04 ? 12  HIS B CG  1 
ATOM   2182 N  ND1 . HIS B 1 12  ? -31.930 39.736  -4.345  1.00 56.23 ? 12  HIS B ND1 1 
ATOM   2183 C  CD2 . HIS B 1 12  ? -32.047 40.537  -6.418  1.00 58.50 ? 12  HIS B CD2 1 
ATOM   2184 C  CE1 . HIS B 1 12  ? -30.710 40.222  -4.689  1.00 56.32 ? 12  HIS B CE1 1 
ATOM   2185 N  NE2 . HIS B 1 12  ? -30.783 40.707  -5.953  1.00 60.13 ? 12  HIS B NE2 1 
ATOM   2186 N  N   . ASN B 1 13  ? -32.959 36.977  -7.167  1.00 30.91 ? 13  ASN B N   1 
ATOM   2187 C  CA  . ASN B 1 13  ? -32.400 36.834  -8.524  1.00 26.84 ? 13  ASN B CA  1 
ATOM   2188 C  C   . ASN B 1 13  ? -31.954 35.348  -8.717  1.00 24.10 ? 13  ASN B C   1 
ATOM   2189 O  O   . ASN B 1 13  ? -31.267 35.014  -9.722  1.00 25.94 ? 13  ASN B O   1 
ATOM   2190 C  CB  . ASN B 1 13  ? -31.225 37.814  -8.736  1.00 27.48 ? 13  ASN B CB  1 
ATOM   2191 C  CG  . ASN B 1 13  ? -30.003 37.527  -7.836  1.00 25.41 ? 13  ASN B CG  1 
ATOM   2192 O  OD1 . ASN B 1 13  ? -30.025 36.621  -6.964  1.00 27.80 ? 13  ASN B OD1 1 
ATOM   2193 N  ND2 . ASN B 1 13  ? -28.973 38.323  -7.987  1.00 26.96 ? 13  ASN B ND2 1 
ATOM   2194 N  N   . GLY B 1 14  ? -32.382 34.504  -7.775  1.00 25.22 ? 14  GLY B N   1 
ATOM   2195 C  CA  . GLY B 1 14  ? -31.855 33.129  -7.660  1.00 25.69 ? 14  GLY B CA  1 
ATOM   2196 C  C   . GLY B 1 14  ? -32.605 32.164  -8.535  1.00 26.39 ? 14  GLY B C   1 
ATOM   2197 O  O   . GLY B 1 14  ? -33.552 32.526  -9.218  1.00 24.81 ? 14  GLY B O   1 
ATOM   2198 N  N   . PRO B 1 15  ? -32.174 30.907  -8.538  1.00 23.31 ? 15  PRO B N   1 
ATOM   2199 C  CA  . PRO B 1 15  ? -32.713 29.889  -9.449  1.00 20.03 ? 15  PRO B CA  1 
ATOM   2200 C  C   . PRO B 1 15  ? -34.223 29.895  -9.740  1.00 23.73 ? 15  PRO B C   1 
ATOM   2201 O  O   . PRO B 1 15  ? -34.670 29.596  -10.901 1.00 24.89 ? 15  PRO B O   1 
ATOM   2202 C  CB  . PRO B 1 15  ? -32.192 28.581  -8.822  1.00 23.04 ? 15  PRO B CB  1 
ATOM   2203 C  CG  . PRO B 1 15  ? -30.883 28.970  -8.309  1.00 19.47 ? 15  PRO B CG  1 
ATOM   2204 C  CD  . PRO B 1 15  ? -31.091 30.361  -7.693  1.00 20.66 ? 15  PRO B CD  1 
ATOM   2205 N  N   . ILE B 1 16  ? -35.043 30.128  -8.708  1.00 25.46 ? 16  ILE B N   1 
ATOM   2206 C  CA  . ILE B 1 16  ? -36.459 29.982  -8.921  1.00 27.57 ? 16  ILE B CA  1 
ATOM   2207 C  C   . ILE B 1 16  ? -36.948 31.143  -9.844  1.00 24.76 ? 16  ILE B C   1 
ATOM   2208 O  O   . ILE B 1 16  ? -38.036 31.032  -10.416 1.00 28.33 ? 16  ILE B O   1 
ATOM   2209 C  CB  . ILE B 1 16  ? -37.204 29.902  -7.553  1.00 32.33 ? 16  ILE B CB  1 
ATOM   2210 C  CG1 . ILE B 1 16  ? -38.515 29.103  -7.664  1.00 41.10 ? 16  ILE B CG1 1 
ATOM   2211 C  CG2 . ILE B 1 16  ? -37.427 31.279  -6.964  1.00 34.21 ? 16  ILE B CG2 1 
ATOM   2212 C  CD1 . ILE B 1 16  ? -38.367 27.591  -7.604  1.00 44.31 ? 16  ILE B CD1 1 
ATOM   2213 N  N   . HIS B 1 17  ? -36.173 32.232  -9.961  1.00 25.29 ? 17  HIS B N   1 
ATOM   2214 C  CA  . HIS B 1 17  ? -36.535 33.377  -10.803 1.00 30.77 ? 17  HIS B CA  1 
ATOM   2215 C  C   . HIS B 1 17  ? -35.895 33.359  -12.152 1.00 32.87 ? 17  HIS B C   1 
ATOM   2216 O  O   . HIS B 1 17  ? -36.210 34.192  -13.020 1.00 28.95 ? 17  HIS B O   1 
ATOM   2217 C  CB  . HIS B 1 17  ? -36.206 34.715  -10.128 1.00 31.85 ? 17  HIS B CB  1 
ATOM   2218 C  CG  . HIS B 1 17  ? -36.874 34.901  -8.780  1.00 35.21 ? 17  HIS B CG  1 
ATOM   2219 N  ND1 . HIS B 1 17  ? -38.226 34.978  -8.638  1.00 40.07 ? 17  HIS B ND1 1 
ATOM   2220 C  CD2 . HIS B 1 17  ? -36.336 35.046  -7.511  1.00 39.89 ? 17  HIS B CD2 1 
ATOM   2221 C  CE1 . HIS B 1 17  ? -38.531 35.117  -7.326  1.00 42.08 ? 17  HIS B CE1 1 
ATOM   2222 N  NE2 . HIS B 1 17  ? -37.374 35.169  -6.637  1.00 40.70 ? 17  HIS B NE2 1 
ATOM   2223 N  N   . TRP B 1 18  ? -34.999 32.410  -12.405 1.00 25.39 ? 18  TRP B N   1 
ATOM   2224 C  CA  . TRP B 1 18  ? -34.281 32.471  -13.671 1.00 24.56 ? 18  TRP B CA  1 
ATOM   2225 C  C   . TRP B 1 18  ? -35.156 32.326  -14.878 1.00 25.70 ? 18  TRP B C   1 
ATOM   2226 O  O   . TRP B 1 18  ? -34.797 32.893  -15.946 1.00 29.92 ? 18  TRP B O   1 
ATOM   2227 C  CB  . TRP B 1 18  ? -33.128 31.399  -13.723 1.00 22.71 ? 18  TRP B CB  1 
ATOM   2228 C  CG  . TRP B 1 18  ? -31.997 31.610  -12.732 1.00 21.01 ? 18  TRP B CG  1 
ATOM   2229 C  CD1 . TRP B 1 18  ? -31.674 32.724  -11.963 1.00 20.61 ? 18  TRP B CD1 1 
ATOM   2230 C  CD2 . TRP B 1 18  ? -30.929 30.642  -12.475 1.00 19.10 ? 18  TRP B CD2 1 
ATOM   2231 N  NE1 . TRP B 1 18  ? -30.563 32.530  -11.204 1.00 22.75 ? 18  TRP B NE1 1 
ATOM   2232 C  CE2 . TRP B 1 18  ? -30.057 31.240  -11.469 1.00 19.29 ? 18  TRP B CE2 1 
ATOM   2233 C  CE3 . TRP B 1 18  ? -30.671 29.330  -12.937 1.00 18.37 ? 18  TRP B CE3 1 
ATOM   2234 C  CZ2 . TRP B 1 18  ? -28.919 30.584  -10.990 1.00 20.39 ? 18  TRP B CZ2 1 
ATOM   2235 C  CZ3 . TRP B 1 18  ? -29.596 28.661  -12.393 1.00 16.88 ? 18  TRP B CZ3 1 
ATOM   2236 C  CH2 . TRP B 1 18  ? -28.702 29.276  -11.503 1.00 18.63 ? 18  TRP B CH2 1 
ATOM   2237 N  N   A LYS B 1 19  ? -36.259 31.572  -14.690 0.50 25.85 ? 19  LYS B N   1 
ATOM   2238 N  N   B LYS B 1 19  ? -36.238 31.568  -14.790 0.50 27.66 ? 19  LYS B N   1 
ATOM   2239 C  CA  A LYS B 1 19  ? -37.375 31.290  -15.664 0.50 28.56 ? 19  LYS B CA  1 
ATOM   2240 C  CA  B LYS B 1 19  ? -37.186 31.444  -15.911 0.50 32.25 ? 19  LYS B CA  1 
ATOM   2241 C  C   A LYS B 1 19  ? -38.190 32.519  -16.098 0.50 32.48 ? 19  LYS B C   1 
ATOM   2242 C  C   B LYS B 1 19  ? -37.640 32.846  -16.342 0.50 35.99 ? 19  LYS B C   1 
ATOM   2243 O  O   A LYS B 1 19  ? -38.906 32.434  -17.102 0.50 25.99 ? 19  LYS B O   1 
ATOM   2244 O  O   B LYS B 1 19  ? -37.580 33.248  -17.516 0.50 27.93 ? 19  LYS B O   1 
ATOM   2245 C  CB  A LYS B 1 19  ? -38.325 30.153  -15.189 0.50 28.40 ? 19  LYS B CB  1 
ATOM   2246 C  CB  B LYS B 1 19  ? -38.384 30.583  -15.496 0.50 31.55 ? 19  LYS B CB  1 
ATOM   2247 C  CG  A LYS B 1 19  ? -39.541 30.588  -14.341 0.50 26.48 ? 19  LYS B CG  1 
ATOM   2248 C  CG  B LYS B 1 19  ? -39.413 31.301  -14.599 0.50 34.35 ? 19  LYS B CG  1 
ATOM   2249 C  CD  A LYS B 1 19  ? -40.070 29.490  -13.415 0.50 31.41 ? 19  LYS B CD  1 
ATOM   2250 C  CD  B LYS B 1 19  ? -39.890 30.476  -13.408 0.50 34.34 ? 19  LYS B CD  1 
ATOM   2251 C  CE  A LYS B 1 19  ? -39.241 29.426  -12.128 0.50 30.79 ? 19  LYS B CE  1 
ATOM   2252 C  CE  B LYS B 1 19  ? -40.454 29.104  -13.781 0.50 35.03 ? 19  LYS B CE  1 
ATOM   2253 N  NZ  A LYS B 1 19  ? -39.467 28.301  -11.173 0.50 31.55 ? 19  LYS B NZ  1 
ATOM   2254 N  NZ  B LYS B 1 19  ? -41.812 29.107  -14.381 0.50 37.58 ? 19  LYS B NZ  1 
ATOM   2255 N  N   . GLU B 1 20  ? -38.039 33.633  -15.362 1.00 38.65 ? 20  GLU B N   1 
ATOM   2256 C  CA  . GLU B 1 20  ? -38.587 34.971  -15.693 1.00 42.57 ? 20  GLU B CA  1 
ATOM   2257 C  C   . GLU B 1 20  ? -37.811 35.634  -16.839 1.00 46.80 ? 20  GLU B C   1 
ATOM   2258 O  O   . GLU B 1 20  ? -38.435 36.096  -17.808 1.00 44.16 ? 20  GLU B O   1 
ATOM   2259 C  CB  . GLU B 1 20  ? -38.599 35.875  -14.442 1.00 40.86 ? 20  GLU B CB  1 
ATOM   2260 C  CG  . GLU B 1 20  ? -39.536 35.348  -13.343 1.00 41.45 ? 20  GLU B CG  1 
ATOM   2261 C  CD  . GLU B 1 20  ? -39.143 35.778  -11.921 1.00 38.88 ? 20  GLU B CD  1 
ATOM   2262 O  OE1 . GLU B 1 20  ? -38.481 36.815  -11.758 1.00 40.53 ? 20  GLU B OE1 1 
ATOM   2263 O  OE2 . GLU B 1 20  ? -39.483 35.043  -10.954 1.00 42.20 ? 20  GLU B OE2 1 
ATOM   2264 N  N   . PHE B 1 21  ? -36.478 35.608  -16.712 1.00 44.85 ? 21  PHE B N   1 
ATOM   2265 C  CA  . PHE B 1 21  ? -35.445 36.193  -17.578 1.00 46.08 ? 21  PHE B CA  1 
ATOM   2266 C  C   . PHE B 1 21  ? -34.789 35.229  -18.657 1.00 48.66 ? 21  PHE B C   1 
ATOM   2267 O  O   . PHE B 1 21  ? -34.330 35.672  -19.715 1.00 43.15 ? 21  PHE B O   1 
ATOM   2268 C  CB  . PHE B 1 21  ? -34.336 36.683  -16.610 1.00 59.28 ? 21  PHE B CB  1 
ATOM   2269 N  N   . PHE B 1 22  ? -34.721 33.921  -18.393 1.00 38.29 ? 22  PHE B N   1 
ATOM   2270 C  CA  . PHE B 1 22  ? -34.219 32.911  -19.371 1.00 33.94 ? 22  PHE B CA  1 
ATOM   2271 C  C   . PHE B 1 22  ? -35.244 31.761  -19.504 1.00 32.97 ? 22  PHE B C   1 
ATOM   2272 O  O   . PHE B 1 22  ? -35.231 30.765  -18.779 1.00 29.66 ? 22  PHE B O   1 
ATOM   2273 C  CB  . PHE B 1 22  ? -32.799 32.396  -18.973 1.00 30.76 ? 22  PHE B CB  1 
ATOM   2274 C  CG  . PHE B 1 22  ? -31.673 33.312  -19.363 1.00 31.26 ? 22  PHE B CG  1 
ATOM   2275 C  CD1 . PHE B 1 22  ? -31.240 33.386  -20.685 1.00 33.52 ? 22  PHE B CD1 1 
ATOM   2276 C  CD2 . PHE B 1 22  ? -31.076 34.157  -18.413 1.00 31.93 ? 22  PHE B CD2 1 
ATOM   2277 C  CE1 . PHE B 1 22  ? -30.223 34.254  -21.071 1.00 39.28 ? 22  PHE B CE1 1 
ATOM   2278 C  CE2 . PHE B 1 22  ? -30.048 35.034  -18.791 1.00 31.94 ? 22  PHE B CE2 1 
ATOM   2279 C  CZ  . PHE B 1 22  ? -29.614 35.072  -20.106 1.00 38.39 ? 22  PHE B CZ  1 
ATOM   2280 N  N   . PRO B 1 23  ? -36.215 31.887  -20.410 1.00 30.25 ? 23  PRO B N   1 
ATOM   2281 C  CA  . PRO B 1 23  ? -37.328 30.944  -20.454 1.00 30.42 ? 23  PRO B CA  1 
ATOM   2282 C  C   . PRO B 1 23  ? -36.992 29.474  -20.596 1.00 29.88 ? 23  PRO B C   1 
ATOM   2283 O  O   . PRO B 1 23  ? -37.775 28.600  -20.214 1.00 28.20 ? 23  PRO B O   1 
ATOM   2284 C  CB  . PRO B 1 23  ? -38.114 31.403  -21.692 1.00 29.75 ? 23  PRO B CB  1 
ATOM   2285 C  CG  . PRO B 1 23  ? -37.867 32.850  -21.713 1.00 34.01 ? 23  PRO B CG  1 
ATOM   2286 C  CD  . PRO B 1 23  ? -36.458 33.078  -21.255 1.00 31.94 ? 23  PRO B CD  1 
ATOM   2287 N  N   . ILE B 1 24  ? -35.818 29.211  -21.196 1.00 24.93 ? 24  ILE B N   1 
ATOM   2288 C  CA  . ILE B 1 24  ? -35.390 27.817  -21.362 1.00 23.91 ? 24  ILE B CA  1 
ATOM   2289 C  C   . ILE B 1 24  ? -35.125 27.125  -19.965 1.00 21.66 ? 24  ILE B C   1 
ATOM   2290 O  O   . ILE B 1 24  ? -35.101 25.896  -19.897 1.00 21.73 ? 24  ILE B O   1 
ATOM   2291 C  CB  . ILE B 1 24  ? -34.112 27.721  -22.264 1.00 21.07 ? 24  ILE B CB  1 
ATOM   2292 C  CG1 . ILE B 1 24  ? -33.944 26.316  -22.790 1.00 23.79 ? 24  ILE B CG1 1 
ATOM   2293 C  CG2 . ILE B 1 24  ? -32.849 28.050  -21.493 1.00 22.02 ? 24  ILE B CG2 1 
ATOM   2294 C  CD1 . ILE B 1 24  ? -35.074 25.796  -23.673 1.00 26.30 ? 24  ILE B CD1 1 
ATOM   2295 N  N   . ALA B 1 25  ? -35.123 27.947  -18.917 1.00 22.45 ? 25  ALA B N   1 
ATOM   2296 C  CA  . ALA B 1 25  ? -35.033 27.405  -17.564 1.00 22.90 ? 25  ALA B CA  1 
ATOM   2297 C  C   . ALA B 1 25  ? -36.086 26.311  -17.317 1.00 21.82 ? 25  ALA B C   1 
ATOM   2298 O  O   . ALA B 1 25  ? -35.913 25.392  -16.489 1.00 20.78 ? 25  ALA B O   1 
ATOM   2299 C  CB  . ALA B 1 25  ? -35.153 28.501  -16.534 1.00 22.05 ? 25  ALA B CB  1 
ATOM   2300 N  N   . ASP B 1 26  ? -37.241 26.469  -17.986 1.00 23.12 ? 26  ASP B N   1 
ATOM   2301 C  CA  . ASP B 1 26  ? -38.317 25.489  -17.977 1.00 25.75 ? 26  ASP B CA  1 
ATOM   2302 C  C   . ASP B 1 26  ? -38.329 24.529  -19.135 1.00 27.86 ? 26  ASP B C   1 
ATOM   2303 O  O   . ASP B 1 26  ? -39.325 23.798  -19.363 1.00 24.90 ? 26  ASP B O   1 
ATOM   2304 C  CB  . ASP B 1 26  ? -39.701 26.215  -17.908 1.00 29.64 ? 26  ASP B CB  1 
ATOM   2305 C  CG  . ASP B 1 26  ? -39.909 26.973  -16.581 1.00 36.95 ? 26  ASP B CG  1 
ATOM   2306 O  OD1 . ASP B 1 26  ? -39.534 26.463  -15.495 1.00 35.55 ? 26  ASP B OD1 1 
ATOM   2307 O  OD2 . ASP B 1 26  ? -40.455 28.084  -16.649 1.00 43.69 ? 26  ASP B OD2 1 
ATOM   2308 N  N   . GLY B 1 27  ? -37.197 24.453  -19.832 1.00 26.09 ? 27  GLY B N   1 
ATOM   2309 C  CA  . GLY B 1 27  ? -37.050 23.532  -20.942 1.00 22.36 ? 27  GLY B CA  1 
ATOM   2310 C  C   . GLY B 1 27  ? -37.145 22.036  -20.628 1.00 22.52 ? 27  GLY B C   1 
ATOM   2311 O  O   . GLY B 1 27  ? -37.262 21.647  -19.417 1.00 24.52 ? 27  GLY B O   1 
ATOM   2312 N  N   . ASP B 1 28  ? -36.964 21.186  -21.661 1.00 23.48 ? 28  ASP B N   1 
ATOM   2313 C  CA  . ASP B 1 28  ? -37.137 19.749  -21.566 1.00 21.53 ? 28  ASP B CA  1 
ATOM   2314 C  C   . ASP B 1 28  ? -35.824 18.980  -21.231 1.00 18.11 ? 28  ASP B C   1 
ATOM   2315 O  O   . ASP B 1 28  ? -35.871 17.814  -20.951 1.00 22.09 ? 28  ASP B O   1 
ATOM   2316 C  CB  . ASP B 1 28  ? -37.584 19.177  -22.908 1.00 30.21 ? 28  ASP B CB  1 
ATOM   2317 C  CG  . ASP B 1 28  ? -39.141 19.187  -23.101 1.00 38.67 ? 28  ASP B CG  1 
ATOM   2318 O  OD1 . ASP B 1 28  ? -39.865 19.755  -22.251 1.00 37.98 ? 28  ASP B OD1 1 
ATOM   2319 O  OD2 . ASP B 1 28  ? -39.594 18.596  -24.111 1.00 45.66 ? 28  ASP B OD2 1 
ATOM   2320 N  N   . GLN B 1 29  ? -34.676 19.649  -21.289 1.00 17.63 ? 29  GLN B N   1 
ATOM   2321 C  CA  . GLN B 1 29  ? -33.400 18.919  -21.039 1.00 17.43 ? 29  GLN B CA  1 
ATOM   2322 C  C   . GLN B 1 29  ? -32.516 19.786  -20.102 1.00 17.31 ? 29  GLN B C   1 
ATOM   2323 O  O   . GLN B 1 29  ? -31.372 20.153  -20.407 1.00 15.90 ? 29  GLN B O   1 
ATOM   2324 C  CB  . GLN B 1 29  ? -32.657 18.627  -22.349 1.00 20.23 ? 29  GLN B CB  1 
ATOM   2325 C  CG  . GLN B 1 29  ? -33.554 17.831  -23.349 1.00 23.42 ? 29  GLN B CG  1 
ATOM   2326 C  CD  . GLN B 1 29  ? -32.735 16.928  -24.292 1.00 26.71 ? 29  GLN B CD  1 
ATOM   2327 O  OE1 . GLN B 1 29  ? -31.639 17.265  -24.693 1.00 25.13 ? 29  GLN B OE1 1 
ATOM   2328 N  NE2 . GLN B 1 29  ? -33.338 15.805  -24.701 1.00 27.97 ? 29  GLN B NE2 1 
ATOM   2329 N  N   . GLN B 1 30  ? -33.128 20.209  -18.967 1.00 16.46 ? 30  GLN B N   1 
ATOM   2330 C  CA  . GLN B 1 30  ? -32.410 21.066  -18.002 1.00 15.47 ? 30  GLN B CA  1 
ATOM   2331 C  C   . GLN B 1 30  ? -31.644 20.232  -16.965 1.00 14.67 ? 30  GLN B C   1 
ATOM   2332 O  O   . GLN B 1 30  ? -31.948 19.104  -16.702 1.00 13.92 ? 30  GLN B O   1 
ATOM   2333 C  CB  . GLN B 1 30  ? -33.433 21.926  -17.276 1.00 16.67 ? 30  GLN B CB  1 
ATOM   2334 C  CG  . GLN B 1 30  ? -33.957 23.026  -18.247 1.00 13.68 ? 30  GLN B CG  1 
ATOM   2335 C  CD  . GLN B 1 30  ? -32.870 24.054  -18.536 1.00 17.29 ? 30  GLN B CD  1 
ATOM   2336 O  OE1 . GLN B 1 30  ? -32.465 24.831  -17.722 1.00 18.19 ? 30  GLN B OE1 1 
ATOM   2337 N  NE2 . GLN B 1 30  ? -32.439 24.110  -19.850 1.00 16.02 ? 30  GLN B NE2 1 
ATOM   2338 N  N   . SER B 1 31  ? -30.584 20.840  -16.502 1.00 14.32 ? 31  SER B N   1 
ATOM   2339 C  CA  . SER B 1 31  ? -29.684 20.250  -15.456 1.00 11.92 ? 31  SER B CA  1 
ATOM   2340 C  C   . SER B 1 31  ? -29.566 21.149  -14.260 1.00 12.58 ? 31  SER B C   1 
ATOM   2341 O  O   . SER B 1 31  ? -29.740 22.352  -14.362 1.00 12.99 ? 31  SER B O   1 
ATOM   2342 C  CB  . SER B 1 31  ? -28.292 20.174  -16.089 1.00 12.45 ? 31  SER B CB  1 
ATOM   2343 O  OG  . SER B 1 31  ? -28.373 19.125  -17.128 1.00 12.94 ? 31  SER B OG  1 
ATOM   2344 N  N   . PRO B 1 32  ? -29.207 20.589  -13.102 1.00 12.26 ? 32  PRO B N   1 
ATOM   2345 C  CA  . PRO B 1 32  ? -28.856 19.212  -12.778 1.00 12.30 ? 32  PRO B CA  1 
ATOM   2346 C  C   . PRO B 1 32  ? -30.090 18.393  -12.552 1.00 11.81 ? 32  PRO B C   1 
ATOM   2347 O  O   . PRO B 1 32  ? -31.225 18.899  -12.715 1.00 13.26 ? 32  PRO B O   1 
ATOM   2348 C  CB  . PRO B 1 32  ? -27.999 19.368  -11.484 1.00 12.91 ? 32  PRO B CB  1 
ATOM   2349 C  CG  . PRO B 1 32  ? -28.740 20.505  -10.775 1.00 12.27 ? 32  PRO B CG  1 
ATOM   2350 C  CD  . PRO B 1 32  ? -29.039 21.501  -11.911 1.00 12.27 ? 32  PRO B CD  1 
ATOM   2351 N  N   . ILE B 1 33  ? -29.889 17.161  -12.203 1.00 13.57 ? 33  ILE B N   1 
ATOM   2352 C  CA  . ILE B 1 33  ? -31.004 16.223  -11.998 1.00 14.38 ? 33  ILE B CA  1 
ATOM   2353 C  C   . ILE B 1 33  ? -30.700 15.355  -10.779 1.00 15.06 ? 33  ILE B C   1 
ATOM   2354 O  O   . ILE B 1 33  ? -29.557 15.282  -10.278 1.00 15.69 ? 33  ILE B O   1 
ATOM   2355 C  CB  . ILE B 1 33  ? -31.182 15.264  -13.236 1.00 15.12 ? 33  ILE B CB  1 
ATOM   2356 C  CG1 . ILE B 1 33  ? -29.938 14.376  -13.484 1.00 14.66 ? 33  ILE B CG1 1 
ATOM   2357 C  CG2 . ILE B 1 33  ? -31.640 16.116  -14.444 1.00 16.21 ? 33  ILE B CG2 1 
ATOM   2358 C  CD1 . ILE B 1 33  ? -30.236 13.179  -14.395 1.00 16.43 ? 33  ILE B CD1 1 
ATOM   2359 N  N   . GLU B 1 34  ? -31.747 14.676  -10.316 1.00 16.96 ? 34  GLU B N   1 
ATOM   2360 C  CA  . GLU B 1 34  ? -31.643 13.565  -9.366  1.00 16.37 ? 34  GLU B CA  1 
ATOM   2361 C  C   . GLU B 1 34  ? -31.218 12.354  -10.134 1.00 16.18 ? 34  GLU B C   1 
ATOM   2362 O  O   . GLU B 1 34  ? -31.891 11.970  -11.164 1.00 18.14 ? 34  GLU B O   1 
ATOM   2363 C  CB  . GLU B 1 34  ? -33.006 13.174  -8.755  1.00 21.85 ? 34  GLU B CB  1 
ATOM   2364 C  CG  . GLU B 1 34  ? -33.738 14.299  -8.121  1.00 29.12 ? 34  GLU B CG  1 
ATOM   2365 C  CD  . GLU B 1 34  ? -33.270 14.626  -6.730  1.00 27.00 ? 34  GLU B CD  1 
ATOM   2366 O  OE1 . GLU B 1 34  ? -32.570 13.769  -6.043  1.00 24.17 ? 34  GLU B OE1 1 
ATOM   2367 O  OE2 . GLU B 1 34  ? -33.752 15.747  -6.319  1.00 31.34 ? 34  GLU B OE2 1 
ATOM   2368 N  N   . ILE B 1 35  ? -30.133 11.731  -9.699  1.00 14.98 ? 35  ILE B N   1 
ATOM   2369 C  CA  . ILE B 1 35  ? -29.721 10.427  -10.237 1.00 15.02 ? 35  ILE B CA  1 
ATOM   2370 C  C   . ILE B 1 35  ? -30.229 9.292   -9.349  1.00 16.58 ? 35  ILE B C   1 
ATOM   2371 O  O   . ILE B 1 35  ? -29.829 9.181   -8.232  1.00 17.61 ? 35  ILE B O   1 
ATOM   2372 C  CB  . ILE B 1 35  ? -28.162 10.401  -10.427 1.00 18.61 ? 35  ILE B CB  1 
ATOM   2373 C  CG1 . ILE B 1 35  ? -27.761 11.530  -11.433 1.00 19.65 ? 35  ILE B CG1 1 
ATOM   2374 C  CG2 . ILE B 1 35  ? -27.696 9.002   -10.881 1.00 19.55 ? 35  ILE B CG2 1 
ATOM   2375 C  CD1 . ILE B 1 35  ? -26.273 11.850  -11.422 1.00 19.75 ? 35  ILE B CD1 1 
ATOM   2376 N  N   . LYS B 1 36  ? -31.171 8.482   -9.844  1.00 19.63 ? 36  LYS B N   1 
ATOM   2377 C  CA  . LYS B 1 36  ? -31.734 7.356   -9.132  1.00 18.65 ? 36  LYS B CA  1 
ATOM   2378 C  C   . LYS B 1 36  ? -31.099 6.082   -9.689  1.00 19.66 ? 36  LYS B C   1 
ATOM   2379 O  O   . LYS B 1 36  ? -31.396 5.676   -10.829 1.00 20.67 ? 36  LYS B O   1 
ATOM   2380 C  CB  . LYS B 1 36  ? -33.282 7.326   -9.339  1.00 18.11 ? 36  LYS B CB  1 
ATOM   2381 C  CG  . LYS B 1 36  ? -34.046 8.497   -8.662  1.00 21.23 ? 36  LYS B CG  1 
ATOM   2382 C  CD  . LYS B 1 36  ? -35.537 8.375   -8.915  1.00 20.02 ? 36  LYS B CD  1 
ATOM   2383 C  CE  . LYS B 1 36  ? -36.378 9.422   -8.293  1.00 26.41 ? 36  LYS B CE  1 
ATOM   2384 N  NZ  . LYS B 1 36  ? -37.770 9.318   -8.797  1.00 25.83 ? 36  LYS B NZ  1 
ATOM   2385 N  N   . THR B 1 37  ? -30.238 5.522   -8.890  1.00 23.38 ? 37  THR B N   1 
ATOM   2386 C  CA  . THR B 1 37  ? -29.338 4.470   -9.387  1.00 25.01 ? 37  THR B CA  1 
ATOM   2387 C  C   . THR B 1 37  ? -30.077 3.220   -9.865  1.00 29.27 ? 37  THR B C   1 
ATOM   2388 O  O   . THR B 1 37  ? -29.599 2.583   -10.773 1.00 33.75 ? 37  THR B O   1 
ATOM   2389 C  CB  . THR B 1 37  ? -28.222 4.126   -8.427  1.00 27.25 ? 37  THR B CB  1 
ATOM   2390 O  OG1 . THR B 1 37  ? -28.751 3.768   -7.155  1.00 27.48 ? 37  THR B OG1 1 
ATOM   2391 C  CG2 . THR B 1 37  ? -27.341 5.323   -8.195  1.00 27.41 ? 37  THR B CG2 1 
ATOM   2392 N  N   . LYS B 1 38  ? -31.257 2.930   -9.308  1.00 25.81 ? 38  LYS B N   1 
ATOM   2393 C  CA  . LYS B 1 38  ? -32.031 1.807   -9.705  1.00 26.42 ? 38  LYS B CA  1 
ATOM   2394 C  C   . LYS B 1 38  ? -32.793 2.060   -10.976 1.00 24.82 ? 38  LYS B C   1 
ATOM   2395 O  O   . LYS B 1 38  ? -33.345 1.113   -11.560 1.00 29.21 ? 38  LYS B O   1 
ATOM   2396 C  CB  . LYS B 1 38  ? -33.047 1.435   -8.613  1.00 29.35 ? 38  LYS B CB  1 
ATOM   2397 C  CG  . LYS B 1 38  ? -32.381 0.753   -7.404  1.00 39.57 ? 38  LYS B CG  1 
ATOM   2398 C  CD  . LYS B 1 38  ? -31.886 -0.677  -7.685  1.00 51.44 ? 38  LYS B CD  1 
ATOM   2399 C  CE  . LYS B 1 38  ? -32.974 -1.605  -8.234  1.00 56.33 ? 38  LYS B CE  1 
ATOM   2400 N  NZ  . LYS B 1 38  ? -33.546 -2.460  -7.158  1.00 59.22 ? 38  LYS B NZ  1 
ATOM   2401 N  N   . GLU B 1 39  ? -32.882 3.322   -11.414 1.00 22.67 ? 39  GLU B N   1 
ATOM   2402 C  CA  . GLU B 1 39  ? -33.524 3.673   -12.618 1.00 22.84 ? 39  GLU B CA  1 
ATOM   2403 C  C   . GLU B 1 39  ? -32.610 3.846   -13.810 1.00 22.07 ? 39  GLU B C   1 
ATOM   2404 O  O   . GLU B 1 39  ? -33.092 3.983   -14.952 1.00 27.03 ? 39  GLU B O   1 
ATOM   2405 C  CB  . GLU B 1 39  ? -34.309 4.984   -12.452 1.00 25.36 ? 39  GLU B CB  1 
ATOM   2406 C  CG  . GLU B 1 39  ? -35.214 5.000   -11.243 1.00 30.34 ? 39  GLU B CG  1 
ATOM   2407 C  CD  . GLU B 1 39  ? -36.140 3.833   -11.263 1.00 36.61 ? 39  GLU B CD  1 
ATOM   2408 O  OE1 . GLU B 1 39  ? -36.175 3.082   -10.260 1.00 33.98 ? 39  GLU B OE1 1 
ATOM   2409 O  OE2 . GLU B 1 39  ? -36.781 3.671   -12.336 1.00 42.91 ? 39  GLU B OE2 1 
ATOM   2410 N  N   . VAL B 1 40  ? -31.299 3.958   -13.533 1.00 21.73 ? 40  VAL B N   1 
ATOM   2411 C  CA  . VAL B 1 40  ? -30.361 4.210   -14.604 1.00 22.20 ? 40  VAL B CA  1 
ATOM   2412 C  C   . VAL B 1 40  ? -30.190 2.967   -15.443 1.00 23.78 ? 40  VAL B C   1 
ATOM   2413 O  O   . VAL B 1 40  ? -30.348 1.852   -14.908 1.00 28.14 ? 40  VAL B O   1 
ATOM   2414 C  CB  . VAL B 1 40  ? -28.963 4.711   -14.123 1.00 25.33 ? 40  VAL B CB  1 
ATOM   2415 C  CG1 . VAL B 1 40  ? -29.103 5.929   -13.235 1.00 27.45 ? 40  VAL B CG1 1 
ATOM   2416 C  CG2 . VAL B 1 40  ? -28.179 3.610   -13.458 1.00 26.58 ? 40  VAL B CG2 1 
ATOM   2417 N  N   . LYS B 1 41  ? -29.984 3.147   -16.745 1.00 21.66 ? 41  LYS B N   1 
ATOM   2418 C  CA  . LYS B 1 41  ? -29.762 1.982   -17.637 1.00 26.37 ? 41  LYS B CA  1 
ATOM   2419 C  C   . LYS B 1 41  ? -28.270 1.749   -17.838 1.00 24.49 ? 41  LYS B C   1 
ATOM   2420 O  O   . LYS B 1 41  ? -27.585 2.613   -18.421 1.00 23.01 ? 41  LYS B O   1 
ATOM   2421 C  CB  . LYS B 1 41  ? -30.350 2.205   -19.041 1.00 28.84 ? 41  LYS B CB  1 
ATOM   2422 C  CG  . LYS B 1 41  ? -31.847 2.407   -19.127 1.00 41.88 ? 41  LYS B CG  1 
ATOM   2423 N  N   . TYR B 1 42  ? -27.779 0.561   -17.468 1.00 23.55 ? 42  TYR B N   1 
ATOM   2424 C  CA  . TYR B 1 42  ? -26.423 0.188   -17.844 1.00 24.45 ? 42  TYR B CA  1 
ATOM   2425 C  C   . TYR B 1 42  ? -26.381 0.100   -19.366 1.00 23.13 ? 42  TYR B C   1 
ATOM   2426 O  O   . TYR B 1 42  ? -27.246 -0.551  -19.950 1.00 26.14 ? 42  TYR B O   1 
ATOM   2427 C  CB  . TYR B 1 42  ? -26.009 -1.159  -17.218 1.00 23.42 ? 42  TYR B CB  1 
ATOM   2428 C  CG  . TYR B 1 42  ? -24.746 -1.705  -17.806 1.00 26.16 ? 42  TYR B CG  1 
ATOM   2429 C  CD1 . TYR B 1 42  ? -23.489 -1.132  -17.535 1.00 24.42 ? 42  TYR B CD1 1 
ATOM   2430 C  CD2 . TYR B 1 42  ? -24.783 -2.807  -18.685 1.00 26.59 ? 42  TYR B CD2 1 
ATOM   2431 C  CE1 . TYR B 1 42  ? -22.341 -1.595  -18.156 1.00 28.76 ? 42  TYR B CE1 1 
ATOM   2432 C  CE2 . TYR B 1 42  ? -23.638 -3.307  -19.264 1.00 24.99 ? 42  TYR B CE2 1 
ATOM   2433 C  CZ  . TYR B 1 42  ? -22.404 -2.733  -18.978 1.00 28.82 ? 42  TYR B CZ  1 
ATOM   2434 O  OH  . TYR B 1 42  ? -21.255 -3.169  -19.566 1.00 34.48 ? 42  TYR B OH  1 
ATOM   2435 N  N   . ASP B 1 43  ? -25.414 0.729   -20.014 1.00 22.05 ? 43  ASP B N   1 
ATOM   2436 C  CA  . ASP B 1 43  ? -25.289 0.727   -21.445 1.00 20.74 ? 43  ASP B CA  1 
ATOM   2437 C  C   . ASP B 1 43  ? -23.893 0.212   -21.804 1.00 22.65 ? 43  ASP B C   1 
ATOM   2438 O  O   . ASP B 1 43  ? -22.915 0.974   -21.662 1.00 22.82 ? 43  ASP B O   1 
ATOM   2439 C  CB  . ASP B 1 43  ? -25.544 2.107   -22.054 1.00 19.61 ? 43  ASP B CB  1 
ATOM   2440 C  CG  . ASP B 1 43  ? -25.615 2.103   -23.581 1.00 21.46 ? 43  ASP B CG  1 
ATOM   2441 O  OD1 . ASP B 1 43  ? -25.101 1.150   -24.252 1.00 23.32 ? 43  ASP B OD1 1 
ATOM   2442 O  OD2 . ASP B 1 43  ? -26.185 3.045   -24.132 1.00 27.55 ? 43  ASP B OD2 1 
ATOM   2443 N  N   . SER B 1 44  ? -23.784 -1.042  -22.291 1.00 24.43 ? 44  SER B N   1 
ATOM   2444 C  CA  . SER B 1 44  ? -22.480 -1.622  -22.631 1.00 26.06 ? 44  SER B CA  1 
ATOM   2445 C  C   . SER B 1 44  ? -21.830 -0.980  -23.872 1.00 24.38 ? 44  SER B C   1 
ATOM   2446 O  O   . SER B 1 44  ? -20.626 -1.239  -24.135 1.00 24.81 ? 44  SER B O   1 
ATOM   2447 C  CB  . SER B 1 44  ? -22.558 -3.188  -22.818 1.00 26.85 ? 44  SER B CB  1 
ATOM   2448 O  OG  . SER B 1 44  ? -23.443 -3.442  -23.896 1.00 28.87 ? 44  SER B OG  1 
ATOM   2449 N  N   . SER B 1 45  ? -22.536 -0.116  -24.591 1.00 21.78 ? 45  SER B N   1 
ATOM   2450 C  CA  . SER B 1 45  ? -21.936 0.638   -25.734 1.00 23.54 ? 45  SER B CA  1 
ATOM   2451 C  C   . SER B 1 45  ? -21.148 1.896   -25.240 1.00 22.16 ? 45  SER B C   1 
ATOM   2452 O  O   . SER B 1 45  ? -20.399 2.478   -26.058 1.00 23.69 ? 45  SER B O   1 
ATOM   2453 C  CB  . SER B 1 45  ? -22.939 1.047   -26.790 1.00 26.62 ? 45  SER B CB  1 
ATOM   2454 O  OG  . SER B 1 45  ? -23.778 2.135   -26.343 1.00 25.54 ? 45  SER B OG  1 
ATOM   2455 N  N   . LEU B 1 46  ? -21.332 2.261   -23.955 1.00 22.00 ? 46  LEU B N   1 
ATOM   2456 C  CA  . LEU B 1 46  ? -20.601 3.396   -23.381 1.00 19.95 ? 46  LEU B CA  1 
ATOM   2457 C  C   . LEU B 1 46  ? -19.131 2.985   -23.262 1.00 22.14 ? 46  LEU B C   1 
ATOM   2458 O  O   . LEU B 1 46  ? -18.791 1.841   -22.928 1.00 23.66 ? 46  LEU B O   1 
ATOM   2459 C  CB  . LEU B 1 46  ? -21.156 3.735   -21.979 1.00 18.88 ? 46  LEU B CB  1 
ATOM   2460 C  CG  . LEU B 1 46  ? -22.445 4.594   -22.040 1.00 17.63 ? 46  LEU B CG  1 
ATOM   2461 C  CD1 . LEU B 1 46  ? -23.049 4.764   -20.634 1.00 20.34 ? 46  LEU B CD1 1 
ATOM   2462 C  CD2 . LEU B 1 46  ? -22.239 5.945   -22.811 1.00 18.57 ? 46  LEU B CD2 1 
ATOM   2463 N  N   . ARG B 1 47  ? -18.258 3.952   -23.427 1.00 19.20 ? 47  ARG B N   1 
ATOM   2464 C  CA  . ARG B 1 47  ? -16.828 3.649   -23.375 1.00 19.30 ? 47  ARG B CA  1 
ATOM   2465 C  C   . ARG B 1 47  ? -16.241 4.227   -22.098 1.00 18.64 ? 47  ARG B C   1 
ATOM   2466 O  O   . ARG B 1 47  ? -16.768 5.169   -21.564 1.00 18.94 ? 47  ARG B O   1 
ATOM   2467 C  CB  . ARG B 1 47  ? -16.149 4.320   -24.565 1.00 17.48 ? 47  ARG B CB  1 
ATOM   2468 C  CG  . ARG B 1 47  ? -16.562 3.637   -25.879 1.00 19.77 ? 47  ARG B CG  1 
ATOM   2469 C  CD  . ARG B 1 47  ? -15.976 4.307   -27.054 1.00 25.25 ? 47  ARG B CD  1 
ATOM   2470 N  NE  . ARG B 1 47  ? -16.299 3.423   -28.185 1.00 29.45 ? 47  ARG B NE  1 
ATOM   2471 C  CZ  . ARG B 1 47  ? -16.064 3.779   -29.454 1.00 27.93 ? 47  ARG B CZ  1 
ATOM   2472 N  NH1 . ARG B 1 47  ? -15.503 4.952   -29.684 1.00 35.09 ? 47  ARG B NH1 1 
ATOM   2473 N  NH2 . ARG B 1 47  ? -16.382 2.946   -30.421 1.00 35.85 ? 47  ARG B NH2 1 
ATOM   2474 N  N   . PRO B 1 48  ? -15.122 3.667   -21.599 1.00 15.45 ? 48  PRO B N   1 
ATOM   2475 C  CA  . PRO B 1 48  ? -14.361 4.401   -20.538 1.00 15.22 ? 48  PRO B CA  1 
ATOM   2476 C  C   . PRO B 1 48  ? -13.965 5.794   -20.963 1.00 15.68 ? 48  PRO B C   1 
ATOM   2477 O  O   . PRO B 1 48  ? -13.778 6.068   -22.179 1.00 15.11 ? 48  PRO B O   1 
ATOM   2478 C  CB  . PRO B 1 48  ? -13.086 3.539   -20.403 1.00 16.59 ? 48  PRO B CB  1 
ATOM   2479 C  CG  . PRO B 1 48  ? -13.468 2.129   -20.881 1.00 18.38 ? 48  PRO B CG  1 
ATOM   2480 C  CD  . PRO B 1 48  ? -14.377 2.444   -22.029 1.00 16.58 ? 48  PRO B CD  1 
ATOM   2481 N  N   . LEU B 1 49  ? -13.766 6.679   -19.988 1.00 14.33 ? 49  LEU B N   1 
ATOM   2482 C  CA  . LEU B 1 49  ? -13.332 8.021   -20.402 1.00 16.60 ? 49  LEU B CA  1 
ATOM   2483 C  C   . LEU B 1 49  ? -11.824 7.978   -20.833 1.00 15.52 ? 49  LEU B C   1 
ATOM   2484 O  O   . LEU B 1 49  ? -11.038 7.269   -20.225 1.00 15.89 ? 49  LEU B O   1 
ATOM   2485 C  CB  . LEU B 1 49  ? -13.447 8.913   -19.183 1.00 16.57 ? 49  LEU B CB  1 
ATOM   2486 C  CG  . LEU B 1 49  ? -14.921 8.999   -18.706 1.00 17.21 ? 49  LEU B CG  1 
ATOM   2487 C  CD1 . LEU B 1 49  ? -14.973 9.860   -17.459 1.00 17.48 ? 49  LEU B CD1 1 
ATOM   2488 C  CD2 . LEU B 1 49  ? -15.761 9.601   -19.880 1.00 18.71 ? 49  LEU B CD2 1 
ATOM   2489 N  N   . SER B 1 50  ? -11.507 8.722   -21.885 1.00 14.03 ? 50  SER B N   1 
ATOM   2490 C  CA  . SER B 1 50  ? -10.153 8.924   -22.353 1.00 14.49 ? 50  SER B CA  1 
ATOM   2491 C  C   . SER B 1 50  ? -9.759  10.382  -22.058 1.00 15.36 ? 50  SER B C   1 
ATOM   2492 O  O   . SER B 1 50  ? -10.312 11.291  -22.654 1.00 14.97 ? 50  SER B O   1 
ATOM   2493 C  CB  . SER B 1 50  ? -10.123 8.674   -23.848 1.00 16.15 ? 50  SER B CB  1 
ATOM   2494 O  OG  . SER B 1 50  ? -8.857  9.011   -24.361 1.00 17.85 ? 50  SER B OG  1 
ATOM   2495 N  N   . ILE B 1 51  ? -8.906  10.558  -21.037 1.00 13.07 ? 51  ILE B N   1 
ATOM   2496 C  CA  . ILE B 1 51  ? -8.668  11.924  -20.509 1.00 14.55 ? 51  ILE B CA  1 
ATOM   2497 C  C   . ILE B 1 51  ? -7.227  12.360  -20.629 1.00 13.92 ? 51  ILE B C   1 
ATOM   2498 O  O   . ILE B 1 51  ? -6.342  11.640  -20.183 1.00 15.25 ? 51  ILE B O   1 
ATOM   2499 C  CB  . ILE B 1 51  ? -9.055  11.916  -19.028 1.00 14.77 ? 51  ILE B CB  1 
ATOM   2500 C  CG1 . ILE B 1 51  ? -10.440 11.255  -18.839 1.00 15.83 ? 51  ILE B CG1 1 
ATOM   2501 C  CG2 . ILE B 1 51  ? -8.998  13.388  -18.535 1.00 17.95 ? 51  ILE B CG2 1 
ATOM   2502 C  CD1 . ILE B 1 51  ? -10.961 11.467  -17.382 1.00 15.54 ? 51  ILE B CD1 1 
ATOM   2503 N  N   . LYS B 1 52  ? -6.971  13.500  -21.264 1.00 13.51 ? 52  LYS B N   1 
ATOM   2504 C  CA  . LYS B 1 52  ? -5.675  14.107  -21.328 1.00 13.63 ? 52  LYS B CA  1 
ATOM   2505 C  C   . LYS B 1 52  ? -5.750  15.566  -20.943 1.00 13.98 ? 52  LYS B C   1 
ATOM   2506 O  O   . LYS B 1 52  ? -6.393  16.362  -21.613 1.00 14.80 ? 52  LYS B O   1 
ATOM   2507 C  CB  . LYS B 1 52  ? -5.149  14.021  -22.748 1.00 14.35 ? 52  LYS B CB  1 
ATOM   2508 C  CG  . LYS B 1 52  ? -3.703  14.479  -22.849 1.00 18.01 ? 52  LYS B CG  1 
ATOM   2509 C  CD  . LYS B 1 52  ? -3.398  14.569  -24.331 1.00 18.12 ? 52  LYS B CD  1 
ATOM   2510 C  CE  . LYS B 1 52  ? -1.964  15.071  -24.539 1.00 19.02 ? 52  LYS B CE  1 
ATOM   2511 N  NZ  . LYS B 1 52  ? -1.590  16.325  -23.791 1.00 19.18 ? 52  LYS B NZ  1 
ATOM   2512 N  N   . TYR B 1 53  ? -5.111  15.909  -19.826 1.00 13.93 ? 53  TYR B N   1 
ATOM   2513 C  CA  . TYR B 1 53  ? -5.127  17.309  -19.335 1.00 14.78 ? 53  TYR B CA  1 
ATOM   2514 C  C   . TYR B 1 53  ? -3.690  17.718  -19.053 1.00 14.99 ? 53  TYR B C   1 
ATOM   2515 O  O   . TYR B 1 53  ? -3.054  17.105  -18.248 1.00 17.33 ? 53  TYR B O   1 
ATOM   2516 C  CB  . TYR B 1 53  ? -5.929  17.399  -17.992 1.00 17.11 ? 53  TYR B CB  1 
ATOM   2517 C  CG  . TYR B 1 53  ? -7.433  17.165  -18.091 1.00 12.61 ? 53  TYR B CG  1 
ATOM   2518 C  CD1 . TYR B 1 53  ? -8.155  17.491  -19.276 1.00 14.51 ? 53  TYR B CD1 1 
ATOM   2519 C  CD2 . TYR B 1 53  ? -8.165  16.606  -17.024 1.00 12.64 ? 53  TYR B CD2 1 
ATOM   2520 C  CE1 . TYR B 1 53  ? -9.534  17.285  -19.334 1.00 12.92 ? 53  TYR B CE1 1 
ATOM   2521 C  CE2 . TYR B 1 53  ? -9.545  16.393  -17.114 1.00 12.93 ? 53  TYR B CE2 1 
ATOM   2522 C  CZ  . TYR B 1 53  ? -10.262 16.732  -18.273 1.00 11.74 ? 53  TYR B CZ  1 
ATOM   2523 O  OH  . TYR B 1 53  ? -11.568 16.557  -18.277 1.00 13.01 ? 53  TYR B OH  1 
ATOM   2524 N  N   . ASP B 1 54  ? -3.197  18.737  -19.765 1.00 14.17 ? 54  ASP B N   1 
ATOM   2525 C  CA  . ASP B 1 54  ? -1.835  19.225  -19.683 1.00 16.80 ? 54  ASP B CA  1 
ATOM   2526 C  C   . ASP B 1 54  ? -1.848  20.268  -18.533 1.00 16.57 ? 54  ASP B C   1 
ATOM   2527 O  O   . ASP B 1 54  ? -2.639  21.212  -18.572 1.00 18.74 ? 54  ASP B O   1 
ATOM   2528 C  CB  . ASP B 1 54  ? -1.490  19.861  -20.986 1.00 16.69 ? 54  ASP B CB  1 
ATOM   2529 C  CG  . ASP B 1 54  ? -0.045  20.316  -21.073 1.00 23.35 ? 54  ASP B CG  1 
ATOM   2530 O  OD1 . ASP B 1 54  ? 0.573   20.707  -20.031 1.00 22.85 ? 54  ASP B OD1 1 
ATOM   2531 O  OD2 . ASP B 1 54  ? 0.458   20.207  -22.211 1.00 26.44 ? 54  ASP B OD2 1 
ATOM   2532 N  N   . PRO B 1 55  ? -1.072  20.015  -17.444 1.00 19.68 ? 55  PRO B N   1 
ATOM   2533 C  CA  . PRO B 1 55  ? -1.052  20.967  -16.300 1.00 19.45 ? 55  PRO B CA  1 
ATOM   2534 C  C   . PRO B 1 55  ? -0.712  22.408  -16.759 1.00 20.38 ? 55  PRO B C   1 
ATOM   2535 O  O   . PRO B 1 55  ? -1.050  23.345  -16.021 1.00 21.40 ? 55  PRO B O   1 
ATOM   2536 C  CB  . PRO B 1 55  ? 0.049   20.409  -15.399 1.00 20.58 ? 55  PRO B CB  1 
ATOM   2537 C  CG  . PRO B 1 55  ? -0.034  18.890  -15.712 1.00 21.51 ? 55  PRO B CG  1 
ATOM   2538 C  CD  . PRO B 1 55  ? -0.147  18.873  -17.232 1.00 19.86 ? 55  PRO B CD  1 
ATOM   2539 N  N   . SER B 1 56  ? -0.069  22.581  -17.912 1.00 19.94 ? 56  SER B N   1 
ATOM   2540 C  CA  . SER B 1 56  ? 0.373   23.891  -18.404 1.00 21.31 ? 56  SER B CA  1 
ATOM   2541 C  C   . SER B 1 56  ? -0.766  24.635  -19.109 1.00 23.29 ? 56  SER B C   1 
ATOM   2542 O  O   . SER B 1 56  ? -0.662  25.827  -19.431 1.00 24.05 ? 56  SER B O   1 
ATOM   2543 C  CB  . SER B 1 56  ? 1.626   23.727  -19.286 1.00 24.66 ? 56  SER B CB  1 
ATOM   2544 O  OG  . SER B 1 56  ? 1.265   23.406  -20.642 1.00 32.60 ? 56  SER B OG  1 
ATOM   2545 N  N   . SER B 1 57  ? -1.885  23.922  -19.391 1.00 18.70 ? 57  SER B N   1 
ATOM   2546 C  CA  . SER B 1 57  ? -3.068  24.520  -20.051 1.00 20.75 ? 57  SER B CA  1 
ATOM   2547 C  C   . SER B 1 57  ? -3.723  25.567  -19.153 1.00 19.66 ? 57  SER B C   1 
ATOM   2548 O  O   . SER B 1 57  ? -4.304  26.492  -19.703 1.00 18.70 ? 57  SER B O   1 
ATOM   2549 C  CB  . SER B 1 57  ? -4.134  23.437  -20.341 1.00 20.27 ? 57  SER B CB  1 
ATOM   2550 O  OG  . SER B 1 57  ? -3.673  22.638  -21.401 1.00 20.94 ? 57  SER B OG  1 
ATOM   2551 N  N   . ALA B 1 58  ? -3.716  25.371  -17.809 1.00 18.19 ? 58  ALA B N   1 
ATOM   2552 C  CA  . ALA B 1 58  ? -4.392  26.338  -16.903 1.00 18.04 ? 58  ALA B CA  1 
ATOM   2553 C  C   . ALA B 1 58  ? -3.607  27.630  -16.961 1.00 18.20 ? 58  ALA B C   1 
ATOM   2554 O  O   . ALA B 1 58  ? -2.387  27.577  -16.939 1.00 18.31 ? 58  ALA B O   1 
ATOM   2555 C  CB  . ALA B 1 58  ? -4.432  25.778  -15.468 1.00 18.08 ? 58  ALA B CB  1 
ATOM   2556 N  N   . LYS B 1 59  ? -4.333  28.749  -17.068 1.00 14.80 ? 59  LYS B N   1 
ATOM   2557 C  CA  . LYS B 1 59  ? -3.624  30.028  -17.202 1.00 16.77 ? 59  LYS B CA  1 
ATOM   2558 C  C   . LYS B 1 59  ? -4.051  31.122  -16.180 1.00 18.34 ? 59  LYS B C   1 
ATOM   2559 O  O   . LYS B 1 59  ? -3.160  31.842  -15.671 1.00 18.98 ? 59  LYS B O   1 
ATOM   2560 C  CB  . LYS B 1 59  ? -3.843  30.610  -18.618 1.00 17.32 ? 59  LYS B CB  1 
ATOM   2561 C  CG  . LYS B 1 59  ? -3.317  29.748  -19.743 1.00 17.77 ? 59  LYS B CG  1 
ATOM   2562 C  CD  . LYS B 1 59  ? -1.825  29.565  -19.682 1.00 17.94 ? 59  LYS B CD  1 
ATOM   2563 C  CE  . LYS B 1 59  ? -1.340  28.782  -20.916 1.00 19.21 ? 59  LYS B CE  1 
ATOM   2564 N  NZ  . LYS B 1 59  ? 0.012   28.252  -20.725 1.00 21.40 ? 59  LYS B NZ  1 
ATOM   2565 N  N   . ILE B 1 60  ? -5.354  31.176  -15.881 1.00 18.66 ? 60  ILE B N   1 
ATOM   2566 C  CA  . ILE B 1 60  ? -5.885  32.288  -15.097 1.00 21.91 ? 60  ILE B CA  1 
ATOM   2567 C  C   . ILE B 1 60  ? -6.971  31.757  -14.231 1.00 18.44 ? 60  ILE B C   1 
ATOM   2568 O  O   . ILE B 1 60  ? -7.758  30.882  -14.691 1.00 18.87 ? 60  ILE B O   1 
ATOM   2569 C  CB  . ILE B 1 60  ? -6.478  33.310  -16.108 1.00 20.64 ? 60  ILE B CB  1 
ATOM   2570 C  CG1 . ILE B 1 60  ? -5.312  33.954  -16.908 1.00 26.76 ? 60  ILE B CG1 1 
ATOM   2571 C  CG2 . ILE B 1 60  ? -7.327  34.416  -15.453 1.00 23.96 ? 60  ILE B CG2 1 
ATOM   2572 C  CD1 . ILE B 1 60  ? -5.760  34.941  -17.970 1.00 29.69 ? 60  ILE B CD1 1 
ATOM   2573 N  N   . ILE B 1 61  ? -7.066  32.260  -13.002 1.00 16.70 ? 61  ILE B N   1 
ATOM   2574 C  CA  . ILE B 1 61  ? -8.241  32.031  -12.109 1.00 15.77 ? 61  ILE B CA  1 
ATOM   2575 C  C   . ILE B 1 61  ? -8.948  33.390  -11.841 1.00 19.14 ? 61  ILE B C   1 
ATOM   2576 O  O   . ILE B 1 61  ? -8.250  34.408  -11.654 1.00 19.73 ? 61  ILE B O   1 
ATOM   2577 C  CB  . ILE B 1 61  ? -7.845  31.267  -10.838 1.00 16.63 ? 61  ILE B CB  1 
ATOM   2578 C  CG1 . ILE B 1 61  ? -9.119  30.800  -10.124 1.00 16.05 ? 61  ILE B CG1 1 
ATOM   2579 C  CG2 . ILE B 1 61  ? -6.879  32.126  -9.985  1.00 16.98 ? 61  ILE B CG2 1 
ATOM   2580 C  CD1 . ILE B 1 61  ? -8.818  29.963  -8.924  1.00 20.23 ? 61  ILE B CD1 1 
ATOM   2581 N  N   . SER B 1 62  ? -10.262 33.389  -11.914 1.00 20.40 ? 62  SER B N   1 
ATOM   2582 C  CA  . SER B 1 62  ? -11.016 34.647  -11.712 1.00 18.43 ? 62  SER B CA  1 
ATOM   2583 C  C   . SER B 1 62  ? -12.266 34.402  -10.879 1.00 22.83 ? 62  SER B C   1 
ATOM   2584 O  O   . SER B 1 62  ? -12.724 33.270  -10.732 1.00 18.29 ? 62  SER B O   1 
ATOM   2585 C  CB  . SER B 1 62  ? -11.387 35.313  -13.025 1.00 21.63 ? 62  SER B CB  1 
ATOM   2586 O  OG  . SER B 1 62  ? -12.177 34.469  -13.825 1.00 25.67 ? 62  SER B OG  1 
ATOM   2587 N  N   . ASN B 1 63  ? -12.748 35.492  -10.240 1.00 20.87 ? 63  ASN B N   1 
ATOM   2588 C  CA  . ASN B 1 63  ? -14.061 35.441  -9.634  1.00 20.64 ? 63  ASN B CA  1 
ATOM   2589 C  C   . ASN B 1 63  ? -15.092 35.992  -10.593 1.00 19.43 ? 63  ASN B C   1 
ATOM   2590 O  O   . ASN B 1 63  ? -15.073 37.207  -10.925 1.00 22.64 ? 63  ASN B O   1 
ATOM   2591 C  CB  . ASN B 1 63  ? -14.034 36.228  -8.300  1.00 20.21 ? 63  ASN B CB  1 
ATOM   2592 C  CG  . ASN B 1 63  ? -15.376 36.272  -7.577  1.00 19.07 ? 63  ASN B CG  1 
ATOM   2593 O  OD1 . ASN B 1 63  ? -16.412 35.747  -8.008  1.00 19.38 ? 63  ASN B OD1 1 
ATOM   2594 N  ND2 . ASN B 1 63  ? -15.330 36.915  -6.356  1.00 17.89 ? 63  ASN B ND2 1 
ATOM   2595 N  N   . SER B 1 64  ? -15.975 35.160  -11.099 1.00 19.17 ? 64  SER B N   1 
ATOM   2596 C  CA  . SER B 1 64  ? -17.050 35.652  -11.986 1.00 21.14 ? 64  SER B CA  1 
ATOM   2597 C  C   . SER B 1 64  ? -18.231 36.301  -11.294 1.00 21.74 ? 64  SER B C   1 
ATOM   2598 O  O   . SER B 1 64  ? -19.161 36.772  -11.929 1.00 25.21 ? 64  SER B O   1 
ATOM   2599 C  CB  . SER B 1 64  ? -17.621 34.507  -12.751 1.00 22.06 ? 64  SER B CB  1 
ATOM   2600 O  OG  . SER B 1 64  ? -18.230 33.550  -11.855 1.00 20.08 ? 64  SER B OG  1 
ATOM   2601 N  N   . GLY B 1 65  ? -18.205 36.289  -9.970  1.00 19.64 ? 65  GLY B N   1 
ATOM   2602 C  CA  . GLY B 1 65  ? -19.390 36.630  -9.174  1.00 20.36 ? 65  GLY B CA  1 
ATOM   2603 C  C   . GLY B 1 65  ? -20.316 35.436  -8.879  1.00 21.87 ? 65  GLY B C   1 
ATOM   2604 O  O   . GLY B 1 65  ? -21.042 35.483  -7.918  1.00 20.18 ? 65  GLY B O   1 
ATOM   2605 N  N   . HIS B 1 66  ? -20.207 34.311  -9.649  1.00 18.88 ? 66  HIS B N   1 
ATOM   2606 C  CA  . HIS B 1 66  ? -21.035 33.101  -9.525  1.00 17.47 ? 66  HIS B CA  1 
ATOM   2607 C  C   . HIS B 1 66  ? -20.283 31.868  -9.095  1.00 15.41 ? 66  HIS B C   1 
ATOM   2608 O  O   . HIS B 1 66  ? -20.910 30.885  -8.676  1.00 16.86 ? 66  HIS B O   1 
ATOM   2609 C  CB  . HIS B 1 66  ? -21.662 32.822  -10.871 1.00 21.39 ? 66  HIS B CB  1 
ATOM   2610 C  CG  . HIS B 1 66  ? -22.173 34.079  -11.533 1.00 24.02 ? 66  HIS B CG  1 
ATOM   2611 N  ND1 . HIS B 1 66  ? -23.189 34.827  -10.994 1.00 24.52 ? 66  HIS B ND1 1 
ATOM   2612 C  CD2 . HIS B 1 66  ? -21.768 34.726  -12.674 1.00 26.09 ? 66  HIS B CD2 1 
ATOM   2613 C  CE1 . HIS B 1 66  ? -23.384 35.931  -11.765 1.00 26.62 ? 66  HIS B CE1 1 
ATOM   2614 N  NE2 . HIS B 1 66  ? -22.555 35.851  -12.803 1.00 28.56 ? 66  HIS B NE2 1 
ATOM   2615 N  N   . SER B 1 67  ? -18.949 31.896  -9.220  1.00 17.20 ? 67  SER B N   1 
ATOM   2616 C  CA  . SER B 1 67  ? -18.036 30.834  -8.762  1.00 16.00 ? 67  SER B CA  1 
ATOM   2617 C  C   . SER B 1 67  ? -16.644 31.370  -9.018  1.00 16.55 ? 67  SER B C   1 
ATOM   2618 O  O   . SER B 1 67  ? -16.496 32.549  -9.423  1.00 17.08 ? 67  SER B O   1 
ATOM   2619 C  CB  . SER B 1 67  ? -18.267 29.497  -9.559  1.00 17.21 ? 67  SER B CB  1 
ATOM   2620 O  OG  . SER B 1 67  ? -17.402 28.481  -8.994  1.00 16.02 ? 67  SER B OG  1 
ATOM   2621 N  N   . PHE B 1 68  ? -15.593 30.577  -8.821  1.00 14.97 ? 68  PHE B N   1 
ATOM   2622 C  CA  . PHE B 1 68  ? -14.282 30.951  -9.447  1.00 15.72 ? 68  PHE B CA  1 
ATOM   2623 C  C   . PHE B 1 68  ? -14.307 30.235  -10.805 1.00 17.12 ? 68  PHE B C   1 
ATOM   2624 O  O   . PHE B 1 68  ? -14.963 29.230  -10.936 1.00 17.46 ? 68  PHE B O   1 
ATOM   2625 C  CB  . PHE B 1 68  ? -13.040 30.459  -8.671  1.00 16.91 ? 68  PHE B CB  1 
ATOM   2626 C  CG  . PHE B 1 68  ? -12.941 28.948  -8.561  1.00 17.93 ? 68  PHE B CG  1 
ATOM   2627 C  CD1 . PHE B 1 68  ? -13.539 28.245  -7.518  1.00 18.97 ? 68  PHE B CD1 1 
ATOM   2628 C  CD2 . PHE B 1 68  ? -12.254 28.210  -9.549  1.00 17.52 ? 68  PHE B CD2 1 
ATOM   2629 C  CE1 . PHE B 1 68  ? -13.437 26.850  -7.455  1.00 18.97 ? 68  PHE B CE1 1 
ATOM   2630 C  CE2 . PHE B 1 68  ? -12.138 26.830  -9.463  1.00 19.63 ? 68  PHE B CE2 1 
ATOM   2631 C  CZ  . PHE B 1 68  ? -12.740 26.134  -8.435  1.00 18.92 ? 68  PHE B CZ  1 
ATOM   2632 N  N   . ASN B 1 69  ? -13.521 30.705  -11.744 1.00 17.05 ? 69  ASN B N   1 
ATOM   2633 C  CA  . ASN B 1 69  ? -13.303 30.010  -13.029 1.00 17.56 ? 69  ASN B CA  1 
ATOM   2634 C  C   . ASN B 1 69  ? -11.835 29.905  -13.260 1.00 17.24 ? 69  ASN B C   1 
ATOM   2635 O  O   . ASN B 1 69  ? -11.109 30.955  -13.258 1.00 16.12 ? 69  ASN B O   1 
ATOM   2636 C  CB  . ASN B 1 69  ? -13.835 30.833  -14.214 1.00 19.10 ? 69  ASN B CB  1 
ATOM   2637 C  CG  . ASN B 1 69  ? -15.317 30.942  -14.216 1.00 23.87 ? 69  ASN B CG  1 
ATOM   2638 O  OD1 . ASN B 1 69  ? -16.021 30.035  -13.813 1.00 25.72 ? 69  ASN B OD1 1 
ATOM   2639 N  ND2 . ASN B 1 69  ? -15.819 32.033  -14.757 1.00 26.00 ? 69  ASN B ND2 1 
ATOM   2640 N  N   . VAL B 1 70  ? -11.318 28.685  -13.437 1.00 16.75 ? 70  VAL B N   1 
ATOM   2641 C  CA  . VAL B 1 70  ? -10.037 28.466  -13.978 1.00 15.19 ? 70  VAL B CA  1 
ATOM   2642 C  C   . VAL B 1 70  ? -10.176 28.395  -15.474 1.00 15.32 ? 70  VAL B C   1 
ATOM   2643 O  O   . VAL B 1 70  ? -10.966 27.587  -16.027 1.00 16.21 ? 70  VAL B O   1 
ATOM   2644 C  CB  . VAL B 1 70  ? -9.336  27.174  -13.409 1.00 16.50 ? 70  VAL B CB  1 
ATOM   2645 C  CG1 . VAL B 1 70  ? -7.986  26.947  -14.072 1.00 18.38 ? 70  VAL B CG1 1 
ATOM   2646 C  CG2 . VAL B 1 70  ? -9.187  27.328  -11.879 1.00 16.75 ? 70  VAL B CG2 1 
ATOM   2647 N  N   . ASP B 1 71  ? -9.520  29.318  -16.164 1.00 15.39 ? 71  ASP B N   1 
ATOM   2648 C  CA  . ASP B 1 71  ? -9.545  29.337  -17.638 1.00 16.79 ? 71  ASP B CA  1 
ATOM   2649 C  C   . ASP B 1 71  ? -8.294  28.672  -18.168 1.00 15.24 ? 71  ASP B C   1 
ATOM   2650 O  O   . ASP B 1 71  ? -7.162  28.866  -17.717 1.00 14.98 ? 71  ASP B O   1 
ATOM   2651 C  CB  . ASP B 1 71  ? -9.668  30.762  -18.204 1.00 19.03 ? 71  ASP B CB  1 
ATOM   2652 C  CG  . ASP B 1 71  ? -11.000 31.408  -17.854 1.00 28.37 ? 71  ASP B CG  1 
ATOM   2653 O  OD1 . ASP B 1 71  ? -12.048 30.725  -17.694 1.00 30.48 ? 71  ASP B OD1 1 
ATOM   2654 O  OD2 . ASP B 1 71  ? -10.982 32.656  -17.765 1.00 30.43 ? 71  ASP B OD2 1 
ATOM   2655 N  N   . PHE B 1 72  ? -8.532  27.829  -19.193 1.00 15.35 ? 72  PHE B N   1 
ATOM   2656 C  CA  . PHE B 1 72  ? -7.423  27.053  -19.862 1.00 15.58 ? 72  PHE B CA  1 
ATOM   2657 C  C   . PHE B 1 72  ? -7.268  27.610  -21.248 1.00 16.46 ? 72  PHE B C   1 
ATOM   2658 O  O   . PHE B 1 72  ? -8.226  28.063  -21.866 1.00 21.88 ? 72  PHE B O   1 
ATOM   2659 C  CB  . PHE B 1 72  ? -7.762  25.543  -19.929 1.00 16.55 ? 72  PHE B CB  1 
ATOM   2660 C  CG  . PHE B 1 72  ? -7.936  24.907  -18.560 1.00 16.26 ? 72  PHE B CG  1 
ATOM   2661 C  CD1 . PHE B 1 72  ? -9.129  25.160  -17.852 1.00 17.58 ? 72  PHE B CD1 1 
ATOM   2662 C  CD2 . PHE B 1 72  ? -6.931  24.142  -17.988 1.00 15.98 ? 72  PHE B CD2 1 
ATOM   2663 C  CE1 . PHE B 1 72  ? -9.264  24.635  -16.546 1.00 17.04 ? 72  PHE B CE1 1 
ATOM   2664 C  CE2 . PHE B 1 72  ? -7.085  23.530  -16.712 1.00 17.21 ? 72  PHE B CE2 1 
ATOM   2665 C  CZ  . PHE B 1 72  ? -8.313  23.822  -16.024 1.00 15.67 ? 72  PHE B CZ  1 
ATOM   2666 N  N   . ASP B 1 73  ? -6.055  27.514  -21.737 1.00 16.51 ? 73  ASP B N   1 
ATOM   2667 C  CA  . ASP B 1 73  ? -5.710  27.953  -23.122 1.00 16.82 ? 73  ASP B CA  1 
ATOM   2668 C  C   . ASP B 1 73  ? -6.303  26.877  -23.989 1.00 20.20 ? 73  ASP B C   1 
ATOM   2669 O  O   . ASP B 1 73  ? -5.823  25.760  -23.908 1.00 20.68 ? 73  ASP B O   1 
ATOM   2670 C  CB  . ASP B 1 73  ? -4.200  28.020  -23.280 1.00 18.84 ? 73  ASP B CB  1 
ATOM   2671 C  CG  . ASP B 1 73  ? -3.817  28.398  -24.705 1.00 17.81 ? 73  ASP B CG  1 
ATOM   2672 O  OD1 . ASP B 1 73  ? -4.714  28.677  -25.451 1.00 21.22 ? 73  ASP B OD1 1 
ATOM   2673 O  OD2 . ASP B 1 73  ? -2.600  28.431  -24.924 1.00 23.57 ? 73  ASP B OD2 1 
ATOM   2674 N  N   . ASP B 1 74  ? -7.398  27.185  -24.647 1.00 18.05 ? 74  ASP B N   1 
ATOM   2675 C  CA  . ASP B 1 74  ? -7.997  26.204  -25.562 1.00 19.22 ? 74  ASP B CA  1 
ATOM   2676 C  C   . ASP B 1 74  ? -7.725  26.579  -27.054 1.00 20.54 ? 74  ASP B C   1 
ATOM   2677 O  O   . ASP B 1 74  ? -8.576  26.334  -27.904 1.00 19.87 ? 74  ASP B O   1 
ATOM   2678 C  CB  . ASP B 1 74  ? -9.516  26.116  -25.291 1.00 19.32 ? 74  ASP B CB  1 
ATOM   2679 C  CG  . ASP B 1 74  ? -10.285 27.382  -25.687 1.00 22.82 ? 74  ASP B CG  1 
ATOM   2680 O  OD1 . ASP B 1 74  ? -9.625  28.442  -25.856 1.00 25.76 ? 74  ASP B OD1 1 
ATOM   2681 O  OD2 . ASP B 1 74  ? -11.495 27.398  -25.844 1.00 21.77 ? 74  ASP B OD2 1 
ATOM   2682 N  N   . THR B 1 75  ? -6.554  27.196  -27.280 1.00 21.21 ? 75  THR B N   1 
ATOM   2683 C  CA  . THR B 1 75  ? -5.999  27.499  -28.658 1.00 21.16 ? 75  THR B CA  1 
ATOM   2684 C  C   . THR B 1 75  ? -5.799  26.198  -29.443 1.00 24.00 ? 75  THR B C   1 
ATOM   2685 O  O   . THR B 1 75  ? -5.975  26.210  -30.649 1.00 24.22 ? 75  THR B O   1 
ATOM   2686 C  CB  . THR B 1 75  ? -4.599  28.170  -28.578 1.00 22.32 ? 75  THR B CB  1 
ATOM   2687 O  OG1 . THR B 1 75  ? -4.772  29.389  -27.897 1.00 23.39 ? 75  THR B OG1 1 
ATOM   2688 C  CG2 . THR B 1 75  ? -3.961  28.471  -29.965 1.00 25.21 ? 75  THR B CG2 1 
ATOM   2689 N  N   . GLU B 1 76  ? -5.296  25.141  -28.835 1.00 22.14 ? 76  GLU B N   1 
ATOM   2690 C  CA  . GLU B 1 76  ? -5.246  23.887  -29.625 1.00 27.34 ? 76  GLU B CA  1 
ATOM   2691 C  C   . GLU B 1 76  ? -5.580  22.682  -28.737 1.00 24.96 ? 76  GLU B C   1 
ATOM   2692 O  O   . GLU B 1 76  ? -6.272  22.879  -27.723 1.00 23.98 ? 76  GLU B O   1 
ATOM   2693 C  CB  . GLU B 1 76  ? -3.942  23.746  -30.387 1.00 33.46 ? 76  GLU B CB  1 
ATOM   2694 C  CG  . GLU B 1 76  ? -2.727  23.544  -29.477 1.00 33.57 ? 76  GLU B CG  1 
ATOM   2695 C  CD  . GLU B 1 76  ? -1.450  23.285  -30.273 1.00 41.13 ? 76  GLU B CD  1 
ATOM   2696 O  OE1 . GLU B 1 76  ? -0.351  23.072  -29.668 1.00 44.07 ? 76  GLU B OE1 1 
ATOM   2697 O  OE2 . GLU B 1 76  ? -1.566  23.264  -31.512 1.00 41.32 ? 76  GLU B OE2 1 
ATOM   2698 N  N   . ASN B 1 77  ? -5.278  21.477  -29.167 1.00 21.94 ? 77  ASN B N   1 
ATOM   2699 C  CA  . ASN B 1 77  ? -5.759  20.283  -28.565 1.00 21.38 ? 77  ASN B CA  1 
ATOM   2700 C  C   . ASN B 1 77  ? -4.789  19.650  -27.615 1.00 18.74 ? 77  ASN B C   1 
ATOM   2701 O  O   . ASN B 1 77  ? -4.618  18.402  -27.646 1.00 24.28 ? 77  ASN B O   1 
ATOM   2702 C  CB  . ASN B 1 77  ? -6.056  19.213  -29.663 1.00 25.06 ? 77  ASN B CB  1 
ATOM   2703 C  CG  . ASN B 1 77  ? -7.461  19.244  -30.147 1.00 21.08 ? 77  ASN B CG  1 
ATOM   2704 O  OD1 . ASN B 1 77  ? -8.354  19.841  -29.547 1.00 17.57 ? 77  ASN B OD1 1 
ATOM   2705 N  ND2 . ASN B 1 77  ? -7.717  18.581  -31.318 1.00 22.05 ? 77  ASN B ND2 1 
ATOM   2706 N  N   . LYS B 1 78  ? -4.172  20.427  -26.729 1.00 16.53 ? 78  LYS B N   1 
ATOM   2707 C  CA  . LYS B 1 78  ? -3.319  19.815  -25.698 1.00 17.06 ? 78  LYS B CA  1 
ATOM   2708 C  C   . LYS B 1 78  ? -4.143  19.069  -24.606 1.00 17.37 ? 78  LYS B C   1 
ATOM   2709 O  O   . LYS B 1 78  ? -3.696  18.010  -24.092 1.00 18.27 ? 78  LYS B O   1 
ATOM   2710 C  CB  . LYS B 1 78  ? -2.447  20.887  -25.022 1.00 18.90 ? 78  LYS B CB  1 
ATOM   2711 C  CG  . LYS B 1 78  ? -1.370  21.498  -25.958 1.00 27.82 ? 78  LYS B CG  1 
ATOM   2712 C  CD  . LYS B 1 78  ? -0.416  22.381  -25.124 1.00 33.62 ? 78  LYS B CD  1 
ATOM   2713 C  CE  . LYS B 1 78  ? 0.720   23.059  -25.924 1.00 42.03 ? 78  LYS B CE  1 
ATOM   2714 N  NZ  . LYS B 1 78  ? 0.359   24.448  -26.369 1.00 39.91 ? 78  LYS B NZ  1 
ATOM   2715 N  N   . SER B 1 79  ? -5.334  19.606  -24.244 1.00 15.47 ? 79  SER B N   1 
ATOM   2716 C  CA  . SER B 1 79  ? -6.161  19.018  -23.154 1.00 14.98 ? 79  SER B CA  1 
ATOM   2717 C  C   . SER B 1 79  ? -7.491  18.674  -23.764 1.00 13.46 ? 79  SER B C   1 
ATOM   2718 O  O   . SER B 1 79  ? -8.245  19.591  -24.184 1.00 13.10 ? 79  SER B O   1 
ATOM   2719 C  CB  . SER B 1 79  ? -6.305  20.058  -22.030 1.00 13.14 ? 79  SER B CB  1 
ATOM   2720 O  OG  . SER B 1 79  ? -4.983  20.269  -21.480 1.00 15.00 ? 79  SER B OG  1 
ATOM   2721 N  N   . VAL B 1 80  ? -7.808  17.353  -23.785 1.00 12.96 ? 80  VAL B N   1 
ATOM   2722 C  CA  . VAL B 1 80  ? -9.034  16.909  -24.430 1.00 12.68 ? 80  VAL B CA  1 
ATOM   2723 C  C   . VAL B 1 80  ? -9.691  15.765  -23.692 1.00 12.87 ? 80  VAL B C   1 
ATOM   2724 O  O   . VAL B 1 80  ? -8.969  14.929  -23.014 1.00 14.03 ? 80  VAL B O   1 
ATOM   2725 C  CB  . VAL B 1 80  ? -8.796  16.473  -25.896 1.00 13.94 ? 80  VAL B CB  1 
ATOM   2726 C  CG1 . VAL B 1 80  ? -8.296  17.669  -26.759 1.00 15.55 ? 80  VAL B CG1 1 
ATOM   2727 C  CG2 . VAL B 1 80  ? -7.764  15.346  -26.025 1.00 17.24 ? 80  VAL B CG2 1 
ATOM   2728 N  N   . LEU B 1 81  ? -11.018 15.662  -23.831 1.00 12.14 ? 81  LEU B N   1 
ATOM   2729 C  CA  . LEU B 1 81  ? -11.750 14.507  -23.342 1.00 12.38 ? 81  LEU B CA  1 
ATOM   2730 C  C   . LEU B 1 81  ? -12.339 13.808  -24.516 1.00 12.78 ? 81  LEU B C   1 
ATOM   2731 O  O   . LEU B 1 81  ? -12.958 14.421  -25.387 1.00 13.00 ? 81  LEU B O   1 
ATOM   2732 C  CB  . LEU B 1 81  ? -12.892 15.063  -22.418 1.00 13.76 ? 81  LEU B CB  1 
ATOM   2733 C  CG  . LEU B 1 81  ? -13.871 14.013  -21.812 1.00 13.78 ? 81  LEU B CG  1 
ATOM   2734 C  CD1 . LEU B 1 81  ? -13.129 13.079  -20.900 1.00 14.58 ? 81  LEU B CD1 1 
ATOM   2735 C  CD2 . LEU B 1 81  ? -14.961 14.781  -21.043 1.00 17.42 ? 81  LEU B CD2 1 
ATOM   2736 N  N   . ARG B 1 82  ? -12.179 12.477  -24.478 1.00 13.53 ? 82  ARG B N   1 
ATOM   2737 C  CA  . ARG B 1 82  ? -12.768 11.595  -25.528 1.00 13.92 ? 82  ARG B CA  1 
ATOM   2738 C  C   . ARG B 1 82  ? -13.310 10.392  -24.845 1.00 14.26 ? 82  ARG B C   1 
ATOM   2739 O  O   . ARG B 1 82  ? -13.247 10.218  -23.626 1.00 13.84 ? 82  ARG B O   1 
ATOM   2740 C  CB  . ARG B 1 82  ? -11.615 11.120  -26.474 1.00 15.20 ? 82  ARG B CB  1 
ATOM   2741 C  CG  . ARG B 1 82  ? -11.138 12.311  -27.295 1.00 16.71 ? 82  ARG B CG  1 
ATOM   2742 C  CD  . ARG B 1 82  ? -9.924  11.959  -28.160 1.00 20.12 ? 82  ARG B CD  1 
ATOM   2743 N  NE  . ARG B 1 82  ? -8.791  11.866  -27.276 1.00 18.80 ? 82  ARG B NE  1 
ATOM   2744 C  CZ  . ARG B 1 82  ? -7.531  11.619  -27.616 1.00 26.94 ? 82  ARG B CZ  1 
ATOM   2745 N  NH1 . ARG B 1 82  ? -7.195  11.468  -28.901 1.00 28.81 ? 82  ARG B NH1 1 
ATOM   2746 N  NH2 . ARG B 1 82  ? -6.613  11.537  -26.659 1.00 25.81 ? 82  ARG B NH2 1 
ATOM   2747 N  N   . GLY B 1 83  ? -13.950 9.500   -25.656 1.00 13.85 ? 83  GLY B N   1 
ATOM   2748 C  CA  . GLY B 1 83  ? -14.552 8.307   -25.070 1.00 14.51 ? 83  GLY B CA  1 
ATOM   2749 C  C   . GLY B 1 83  ? -15.824 8.631   -24.314 1.00 13.52 ? 83  GLY B C   1 
ATOM   2750 O  O   . GLY B 1 83  ? -16.516 9.571   -24.643 1.00 15.37 ? 83  GLY B O   1 
ATOM   2751 N  N   . GLY B 1 84  ? -16.102 7.848   -23.263 1.00 17.33 ? 84  GLY B N   1 
ATOM   2752 C  CA  . GLY B 1 84  ? -17.379 8.029   -22.548 1.00 17.08 ? 84  GLY B CA  1 
ATOM   2753 C  C   . GLY B 1 84  ? -18.499 7.878   -23.567 1.00 17.49 ? 84  GLY B C   1 
ATOM   2754 O  O   . GLY B 1 84  ? -18.449 6.928   -24.380 1.00 18.16 ? 84  GLY B O   1 
ATOM   2755 N  N   . PRO B 1 85  ? -19.546 8.743   -23.504 1.00 15.92 ? 85  PRO B N   1 
ATOM   2756 C  CA  . PRO B 1 85  ? -20.659 8.750   -24.480 1.00 16.12 ? 85  PRO B CA  1 
ATOM   2757 C  C   . PRO B 1 85  ? -20.360 9.582   -25.698 1.00 13.46 ? 85  PRO B C   1 
ATOM   2758 O  O   . PRO B 1 85  ? -21.236 9.784   -26.549 1.00 18.42 ? 85  PRO B O   1 
ATOM   2759 C  CB  . PRO B 1 85  ? -21.815 9.530   -23.739 1.00 15.04 ? 85  PRO B CB  1 
ATOM   2760 C  CG  . PRO B 1 85  ? -20.994 10.530  -22.831 1.00 15.35 ? 85  PRO B CG  1 
ATOM   2761 C  CD  . PRO B 1 85  ? -19.717 9.768   -22.405 1.00 16.36 ? 85  PRO B CD  1 
ATOM   2762 N  N   . LEU B 1 86  ? -19.168 10.159  -25.787 1.00 14.45 ? 86  LEU B N   1 
ATOM   2763 C  CA  . LEU B 1 86  ? -18.846 11.208  -26.759 1.00 12.92 ? 86  LEU B CA  1 
ATOM   2764 C  C   . LEU B 1 86  ? -18.397 10.673  -28.134 1.00 17.81 ? 86  LEU B C   1 
ATOM   2765 O  O   . LEU B 1 86  ? -17.647 9.750   -28.168 1.00 17.42 ? 86  LEU B O   1 
ATOM   2766 C  CB  . LEU B 1 86  ? -17.731 12.112  -26.206 1.00 14.28 ? 86  LEU B CB  1 
ATOM   2767 C  CG  . LEU B 1 86  ? -18.060 12.756  -24.847 1.00 13.41 ? 86  LEU B CG  1 
ATOM   2768 C  CD1 . LEU B 1 86  ? -16.795 13.444  -24.353 1.00 13.76 ? 86  LEU B CD1 1 
ATOM   2769 C  CD2 . LEU B 1 86  ? -19.225 13.739  -24.945 1.00 13.85 ? 86  LEU B CD2 1 
ATOM   2770 N  N   . THR B 1 87  ? -18.892 11.348  -29.159 1.00 16.49 ? 87  THR B N   1 
ATOM   2771 C  CA  . THR B 1 87  ? -18.363 11.202  -30.550 1.00 18.14 ? 87  THR B CA  1 
ATOM   2772 C  C   . THR B 1 87  ? -17.336 12.299  -30.754 1.00 17.56 ? 87  THR B C   1 
ATOM   2773 O  O   . THR B 1 87  ? -17.638 13.520  -30.660 1.00 18.99 ? 87  THR B O   1 
ATOM   2774 C  CB  . THR B 1 87  ? -19.501 11.342  -31.535 1.00 18.76 ? 87  THR B CB  1 
ATOM   2775 O  OG1 . THR B 1 87  ? -20.322 10.183  -31.335 1.00 24.61 ? 87  THR B OG1 1 
ATOM   2776 C  CG2 . THR B 1 87  ? -18.947 11.266  -32.986 1.00 21.74 ? 87  THR B CG2 1 
ATOM   2777 N  N   . GLY B 1 88  ? -16.088 11.895  -31.037 1.00 16.92 ? 88  GLY B N   1 
ATOM   2778 C  CA  . GLY B 1 88  ? -15.071 12.944  -31.323 1.00 18.65 ? 88  GLY B CA  1 
ATOM   2779 C  C   . GLY B 1 88  ? -14.440 13.541  -30.036 1.00 15.33 ? 88  GLY B C   1 
ATOM   2780 O  O   . GLY B 1 88  ? -14.578 12.982  -28.957 1.00 18.06 ? 88  GLY B O   1 
ATOM   2781 N  N   . SER B 1 89  ? -13.728 14.616  -30.257 1.00 15.71 ? 89  SER B N   1 
ATOM   2782 C  CA  . SER B 1 89  ? -12.818 15.196  -29.274 1.00 15.16 ? 89  SER B CA  1 
ATOM   2783 C  C   . SER B 1 89  ? -13.320 16.517  -28.717 1.00 15.00 ? 89  SER B C   1 
ATOM   2784 O  O   . SER B 1 89  ? -13.676 17.439  -29.496 1.00 16.01 ? 89  SER B O   1 
ATOM   2785 C  CB  . SER B 1 89  ? -11.433 15.454  -29.973 1.00 15.95 ? 89  SER B CB  1 
ATOM   2786 O  OG  . SER B 1 89  ? -10.517 15.808  -28.983 1.00 15.83 ? 89  SER B OG  1 
ATOM   2787 N  N   . TYR B 1 90  ? -13.378 16.586  -27.361 1.00 13.56 ? 90  TYR B N   1 
ATOM   2788 C  CA  . TYR B 1 90  ? -13.909 17.782  -26.705 1.00 12.15 ? 90  TYR B CA  1 
ATOM   2789 C  C   . TYR B 1 90  ? -12.797 18.460  -25.917 1.00 12.65 ? 90  TYR B C   1 
ATOM   2790 O  O   . TYR B 1 90  ? -12.113 17.810  -25.116 1.00 13.22 ? 90  TYR B O   1 
ATOM   2791 C  CB  . TYR B 1 90  ? -15.047 17.334  -25.769 1.00 12.36 ? 90  TYR B CB  1 
ATOM   2792 C  CG  . TYR B 1 90  ? -16.354 17.040  -26.490 1.00 10.70 ? 90  TYR B CG  1 
ATOM   2793 C  CD1 . TYR B 1 90  ? -16.445 15.890  -27.336 1.00 12.53 ? 90  TYR B CD1 1 
ATOM   2794 C  CD2 . TYR B 1 90  ? -17.479 17.841  -26.336 1.00 12.21 ? 90  TYR B CD2 1 
ATOM   2795 C  CE1 . TYR B 1 90  ? -17.661 15.616  -27.999 1.00 13.72 ? 90  TYR B CE1 1 
ATOM   2796 C  CE2 . TYR B 1 90  ? -18.719 17.558  -26.965 1.00 13.37 ? 90  TYR B CE2 1 
ATOM   2797 C  CZ  . TYR B 1 90  ? -18.754 16.425  -27.822 1.00 13.63 ? 90  TYR B CZ  1 
ATOM   2798 O  OH  . TYR B 1 90  ? -19.926 16.135  -28.498 1.00 14.60 ? 90  TYR B OH  1 
ATOM   2799 N  N   . ARG B 1 91  ? -12.533 19.717  -26.258 1.00 11.47 ? 91  ARG B N   1 
ATOM   2800 C  CA  . ARG B 1 91  ? -11.404 20.486  -25.793 1.00 12.55 ? 91  ARG B CA  1 
ATOM   2801 C  C   . ARG B 1 91  ? -11.707 21.129  -24.434 1.00 11.87 ? 91  ARG B C   1 
ATOM   2802 O  O   . ARG B 1 91  ? -12.744 21.764  -24.251 1.00 13.13 ? 91  ARG B O   1 
ATOM   2803 C  CB  . ARG B 1 91  ? -11.089 21.561  -26.832 1.00 13.93 ? 91  ARG B CB  1 
ATOM   2804 C  CG  . ARG B 1 91  ? -9.773  22.277  -26.553 1.00 15.40 ? 91  ARG B CG  1 
ATOM   2805 C  CD  . ARG B 1 91  ? -9.408  23.248  -27.669 1.00 16.32 ? 91  ARG B CD  1 
ATOM   2806 N  NE  . ARG B 1 91  ? -9.283  22.570  -28.959 1.00 14.43 ? 91  ARG B NE  1 
ATOM   2807 C  CZ  . ARG B 1 91  ? -9.150  23.211  -30.111 1.00 16.40 ? 91  ARG B CZ  1 
ATOM   2808 N  NH1 . ARG B 1 91  ? -9.143  24.535  -30.162 1.00 18.33 ? 91  ARG B NH1 1 
ATOM   2809 N  NH2 . ARG B 1 91  ? -9.029  22.532  -31.248 1.00 15.88 ? 91  ARG B NH2 1 
ATOM   2810 N  N   . LEU B 1 92  ? -10.735 20.978  -23.520 1.00 11.26 ? 92  LEU B N   1 
ATOM   2811 C  CA  . LEU B 1 92  ? -10.922 21.622  -22.208 1.00 12.92 ? 92  LEU B CA  1 
ATOM   2812 C  C   . LEU B 1 92  ? -10.934 23.164  -22.299 1.00 13.62 ? 92  LEU B C   1 
ATOM   2813 O  O   . LEU B 1 92  ? -10.057 23.781  -22.919 1.00 14.99 ? 92  LEU B O   1 
ATOM   2814 C  CB  . LEU B 1 92  ? -9.733  21.204  -21.362 1.00 12.04 ? 92  LEU B CB  1 
ATOM   2815 C  CG  . LEU B 1 92  ? -9.686  21.785  -19.943 1.00 11.50 ? 92  LEU B CG  1 
ATOM   2816 C  CD1 . LEU B 1 92  ? -10.928 21.378  -19.148 1.00 13.61 ? 92  LEU B CD1 1 
ATOM   2817 C  CD2 . LEU B 1 92  ? -8.350  21.389  -19.287 1.00 13.49 ? 92  LEU B CD2 1 
ATOM   2818 N  N   . ARG B 1 93  ? -11.913 23.754  -21.612 1.00 13.45 ? 93  ARG B N   1 
ATOM   2819 C  CA  . ARG B 1 93  ? -12.058 25.246  -21.613 1.00 13.03 ? 93  ARG B CA  1 
ATOM   2820 C  C   . ARG B 1 93  ? -11.927 25.877  -20.231 1.00 13.37 ? 93  ARG B C   1 
ATOM   2821 O  O   . ARG B 1 93  ? -11.261 26.840  -20.064 1.00 16.20 ? 93  ARG B O   1 
ATOM   2822 C  CB  . ARG B 1 93  ? -13.461 25.600  -22.152 1.00 16.39 ? 93  ARG B CB  1 
ATOM   2823 C  CG  . ARG B 1 93  ? -13.904 27.067  -21.982 1.00 19.27 ? 93  ARG B CG  1 
ATOM   2824 C  CD  . ARG B 1 93  ? -13.414 27.856  -23.117 1.00 20.67 ? 93  ARG B CD  1 
ATOM   2825 N  NE  . ARG B 1 93  ? -13.968 29.208  -23.062 1.00 22.19 ? 93  ARG B NE  1 
ATOM   2826 C  CZ  . ARG B 1 93  ? -13.685 30.131  -23.985 1.00 24.05 ? 93  ARG B CZ  1 
ATOM   2827 N  NH1 . ARG B 1 93  ? -12.959 29.802  -25.053 1.00 23.09 ? 93  ARG B NH1 1 
ATOM   2828 N  NH2 . ARG B 1 93  ? -14.188 31.331  -23.843 1.00 23.48 ? 93  ARG B NH2 1 
ATOM   2829 N  N   . GLN B 1 94  ? -12.632 25.270  -19.262 1.00 13.38 ? 94  GLN B N   1 
ATOM   2830 C  CA  . GLN B 1 94  ? -12.669 25.910  -17.972 1.00 14.41 ? 94  GLN B CA  1 
ATOM   2831 C  C   . GLN B 1 94  ? -13.148 24.970  -16.882 1.00 12.87 ? 94  GLN B C   1 
ATOM   2832 O  O   . GLN B 1 94  ? -13.774 23.953  -17.146 1.00 12.85 ? 94  GLN B O   1 
ATOM   2833 C  CB  . GLN B 1 94  ? -13.542 27.130  -18.071 1.00 19.48 ? 94  GLN B CB  1 
ATOM   2834 C  CG  . GLN B 1 94  ? -14.947 26.986  -18.173 1.00 20.64 ? 94  GLN B CG  1 
ATOM   2835 C  CD  . GLN B 1 94  ? -15.596 27.243  -16.818 1.00 29.44 ? 94  GLN B CD  1 
ATOM   2836 O  OE1 . GLN B 1 94  ? -15.731 26.319  -16.054 1.00 23.27 ? 94  GLN B OE1 1 
ATOM   2837 N  NE2 . GLN B 1 94  ? -15.828 28.492  -16.467 1.00 30.05 ? 94  GLN B NE2 1 
ATOM   2838 N  N   . VAL B 1 95  ? -12.803 25.321  -15.625 1.00 14.26 ? 95  VAL B N   1 
ATOM   2839 C  CA  . VAL B 1 95  ? -13.238 24.507  -14.466 1.00 12.38 ? 95  VAL B CA  1 
ATOM   2840 C  C   . VAL B 1 95  ? -13.861 25.494  -13.486 1.00 12.38 ? 95  VAL B C   1 
ATOM   2841 O  O   . VAL B 1 95  ? -13.319 26.590  -13.302 1.00 13.48 ? 95  VAL B O   1 
ATOM   2842 C  CB  . VAL B 1 95  ? -12.007 23.875  -13.800 1.00 11.85 ? 95  VAL B CB  1 
ATOM   2843 C  CG1 . VAL B 1 95  ? -12.298 23.292  -12.381 1.00 13.83 ? 95  VAL B CG1 1 
ATOM   2844 C  CG2 . VAL B 1 95  ? -11.512 22.671  -14.689 1.00 12.28 ? 95  VAL B CG2 1 
ATOM   2845 N  N   . HIS B 1 96  ? -14.892 25.030  -12.808 1.00 11.49 ? 96  HIS B N   1 
ATOM   2846 C  CA  . HIS B 1 96  ? -15.466 25.844  -11.675 1.00 11.02 ? 96  HIS B CA  1 
ATOM   2847 C  C   . HIS B 1 96  ? -16.106 24.920  -10.691 1.00 12.26 ? 96  HIS B C   1 
ATOM   2848 O  O   . HIS B 1 96  ? -16.026 23.738  -10.834 1.00 11.52 ? 96  HIS B O   1 
ATOM   2849 C  CB  . HIS B 1 96  ? -16.417 26.919  -12.257 1.00 12.38 ? 96  HIS B CB  1 
ATOM   2850 C  CG  . HIS B 1 96  ? -17.602 26.266  -12.906 1.00 11.01 ? 96  HIS B CG  1 
ATOM   2851 N  ND1 . HIS B 1 96  ? -17.643 25.971  -14.278 1.00 11.90 ? 96  HIS B ND1 1 
ATOM   2852 C  CD2 . HIS B 1 96  ? -18.771 25.792  -12.373 1.00 11.10 ? 96  HIS B CD2 1 
ATOM   2853 C  CE1 . HIS B 1 96  ? -18.799 25.331  -14.520 1.00 12.73 ? 96  HIS B CE1 1 
ATOM   2854 N  NE2 . HIS B 1 96  ? -19.526 25.217  -13.376 1.00 14.16 ? 96  HIS B NE2 1 
ATOM   2855 N  N   . LEU B 1 97  ? -16.658 25.469  -9.606  1.00 10.40 ? 97  LEU B N   1 
ATOM   2856 C  CA  . LEU B 1 97  ? -17.131 24.729  -8.468  1.00 10.91 ? 97  LEU B CA  1 
ATOM   2857 C  C   . LEU B 1 97  ? -18.505 25.221  -7.991  1.00 11.32 ? 97  LEU B C   1 
ATOM   2858 O  O   . LEU B 1 97  ? -18.689 26.446  -7.977  1.00 11.67 ? 97  LEU B O   1 
ATOM   2859 C  CB  . LEU B 1 97  ? -16.039 24.830  -7.334  1.00 11.51 ? 97  LEU B CB  1 
ATOM   2860 C  CG  . LEU B 1 97  ? -16.320 23.923  -6.121  1.00 11.53 ? 97  LEU B CG  1 
ATOM   2861 C  CD1 . LEU B 1 97  ? -16.059 22.465  -6.479  1.00 12.94 ? 97  LEU B CD1 1 
ATOM   2862 C  CD2 . LEU B 1 97  ? -15.389 24.386  -5.031  1.00 13.65 ? 97  LEU B CD2 1 
ATOM   2863 N  N   . HIS B 1 98  ? -19.363 24.307  -7.538  1.00 10.44 ? 98  HIS B N   1 
ATOM   2864 C  CA  . HIS B 1 98  ? -20.604 24.695  -6.864  1.00 12.18 ? 98  HIS B CA  1 
ATOM   2865 C  C   . HIS B 1 98  ? -20.598 24.108  -5.469  1.00 12.51 ? 98  HIS B C   1 
ATOM   2866 O  O   . HIS B 1 98  ? -20.089 23.050  -5.181  1.00 12.64 ? 98  HIS B O   1 
ATOM   2867 C  CB  . HIS B 1 98  ? -21.821 24.059  -7.622  1.00 11.98 ? 98  HIS B CB  1 
ATOM   2868 C  CG  . HIS B 1 98  ? -21.907 24.492  -9.056  1.00 14.13 ? 98  HIS B CG  1 
ATOM   2869 N  ND1 . HIS B 1 98  ? -22.531 25.667  -9.412  1.00 13.33 ? 98  HIS B ND1 1 
ATOM   2870 C  CD2 . HIS B 1 98  ? -21.341 23.974  -10.214 1.00 14.96 ? 98  HIS B CD2 1 
ATOM   2871 C  CE1 . HIS B 1 98  ? -22.451 25.859  -10.737 1.00 14.61 ? 98  HIS B CE1 1 
ATOM   2872 N  NE2 . HIS B 1 98  ? -21.759 24.801  -11.250 1.00 10.30 ? 98  HIS B NE2 1 
ATOM   2873 N  N   . TRP B 1 99  ? -21.202 24.901  -4.563  1.00 10.81 ? 99  TRP B N   1 
ATOM   2874 C  CA  . TRP B 1 99  ? -21.245 24.538  -3.088  1.00 11.29 ? 99  TRP B CA  1 
ATOM   2875 C  C   . TRP B 1 99  ? -22.524 25.099  -2.541  1.00 11.43 ? 99  TRP B C   1 
ATOM   2876 O  O   . TRP B 1 99  ? -23.359 25.725  -3.226  1.00 13.25 ? 99  TRP B O   1 
ATOM   2877 C  CB  . TRP B 1 99  ? -20.002 25.062  -2.374  1.00 12.12 ? 99  TRP B CB  1 
ATOM   2878 C  CG  . TRP B 1 99  ? -19.795 26.564  -2.431  1.00 12.51 ? 99  TRP B CG  1 
ATOM   2879 C  CD1 . TRP B 1 99  ? -20.439 27.525  -1.638  1.00 12.82 ? 99  TRP B CD1 1 
ATOM   2880 C  CD2 . TRP B 1 99  ? -19.002 27.287  -3.382  1.00 12.89 ? 99  TRP B CD2 1 
ATOM   2881 N  NE1 . TRP B 1 99  ? -20.045 28.775  -2.009  1.00 12.18 ? 99  TRP B NE1 1 
ATOM   2882 C  CE2 . TRP B 1 99  ? -19.179 28.684  -3.113  1.00 13.84 ? 99  TRP B CE2 1 
ATOM   2883 C  CE3 . TRP B 1 99  ? -18.189 26.883  -4.486  1.00 11.51 ? 99  TRP B CE3 1 
ATOM   2884 C  CZ2 . TRP B 1 99  ? -18.563 29.672  -3.864  1.00 13.07 ? 99  TRP B CZ2 1 
ATOM   2885 C  CZ3 . TRP B 1 99  ? -17.524 27.882  -5.255  1.00 12.68 ? 99  TRP B CZ3 1 
ATOM   2886 C  CH2 . TRP B 1 99  ? -17.705 29.261  -4.960  1.00 12.36 ? 99  TRP B CH2 1 
ATOM   2887 N  N   . GLY B 1 100 ? -22.686 24.828  -1.243  1.00 12.41 ? 100 GLY B N   1 
ATOM   2888 C  CA  . GLY B 1 100 ? -23.863 25.316  -0.514  1.00 12.88 ? 100 GLY B CA  1 
ATOM   2889 C  C   . GLY B 1 100 ? -23.392 25.996  0.763   1.00 11.97 ? 100 GLY B C   1 
ATOM   2890 O  O   . GLY B 1 100 ? -22.205 26.106  1.020   1.00 13.63 ? 100 GLY B O   1 
ATOM   2891 N  N   . SER B 1 101 ? -24.390 26.526  1.503   1.00 13.28 ? 101 SER B N   1 
ATOM   2892 C  CA  . SER B 1 101 ? -23.967 27.121  2.804   1.00 13.80 ? 101 SER B CA  1 
ATOM   2893 C  C   . SER B 1 101 ? -23.588 26.141  3.871   1.00 15.19 ? 101 SER B C   1 
ATOM   2894 O  O   . SER B 1 101 ? -22.889 26.545  4.849   1.00 15.60 ? 101 SER B O   1 
ATOM   2895 C  CB  . SER B 1 101 ? -25.032 28.127  3.282   1.00 14.18 ? 101 SER B CB  1 
ATOM   2896 O  OG  . SER B 1 101 ? -26.141 27.447  3.799   1.00 18.69 ? 101 SER B OG  1 
ATOM   2897 N  N   . ALA B 1 102 ? -24.006 24.911  3.725   1.00 13.38 ? 102 ALA B N   1 
ATOM   2898 C  CA  . ALA B 1 102 ? -23.656 23.874  4.646   1.00 15.51 ? 102 ALA B CA  1 
ATOM   2899 C  C   . ALA B 1 102 ? -22.995 22.708  3.930   1.00 15.14 ? 102 ALA B C   1 
ATOM   2900 O  O   . ALA B 1 102 ? -23.338 22.391  2.746   1.00 16.92 ? 102 ALA B O   1 
ATOM   2901 C  CB  . ALA B 1 102 ? -24.942 23.388  5.285   1.00 19.90 ? 102 ALA B CB  1 
ATOM   2902 N  N   . ASP B 1 103 ? -22.151 21.980  4.614   1.00 15.54 ? 103 ASP B N   1 
ATOM   2903 C  CA  . ASP B 1 103 ? -21.416 20.843  4.013   1.00 15.28 ? 103 ASP B CA  1 
ATOM   2904 C  C   . ASP B 1 103 ? -22.320 19.720  3.622   1.00 21.07 ? 103 ASP B C   1 
ATOM   2905 O  O   . ASP B 1 103 ? -21.902 18.898  2.833   1.00 25.92 ? 103 ASP B O   1 
ATOM   2906 C  CB  . ASP B 1 103 ? -20.328 20.291  4.939   1.00 18.59 ? 103 ASP B CB  1 
ATOM   2907 C  CG  . ASP B 1 103 ? -19.202 21.246  5.157   1.00 18.96 ? 103 ASP B CG  1 
ATOM   2908 O  OD1 . ASP B 1 103 ? -19.110 22.283  4.507   1.00 18.99 ? 103 ASP B OD1 1 
ATOM   2909 O  OD2 . ASP B 1 103 ? -18.367 20.955  6.056   1.00 25.48 ? 103 ASP B OD2 1 
ATOM   2910 N  N   . ASP B 1 104 ? -23.508 19.622  4.169   1.00 26.25 ? 104 ASP B N   1 
ATOM   2911 C  CA  . ASP B 1 104 ? -24.291 18.456  3.851   1.00 28.73 ? 104 ASP B CA  1 
ATOM   2912 C  C   . ASP B 1 104 ? -25.181 18.669  2.635   1.00 27.23 ? 104 ASP B C   1 
ATOM   2913 O  O   . ASP B 1 104 ? -25.934 17.760  2.281   1.00 24.35 ? 104 ASP B O   1 
ATOM   2914 C  CB  . ASP B 1 104 ? -25.098 18.195  5.130   1.00 33.64 ? 104 ASP B CB  1 
ATOM   2915 C  CG  . ASP B 1 104 ? -25.502 19.493  5.778   1.00 35.66 ? 104 ASP B CG  1 
ATOM   2916 O  OD1 . ASP B 1 104 ? -24.934 19.853  6.827   1.00 37.75 ? 104 ASP B OD1 1 
ATOM   2917 O  OD2 . ASP B 1 104 ? -26.332 20.201  5.174   1.00 40.04 ? 104 ASP B OD2 1 
ATOM   2918 N  N   . HIS B 1 105 ? -25.126 19.851  1.981   1.00 22.58 ? 105 HIS B N   1 
ATOM   2919 C  CA  . HIS B 1 105 ? -26.014 20.076  0.878   1.00 21.65 ? 105 HIS B CA  1 
ATOM   2920 C  C   . HIS B 1 105 ? -25.410 21.127  -0.073  1.00 18.31 ? 105 HIS B C   1 
ATOM   2921 O  O   . HIS B 1 105 ? -25.820 22.297  -0.073  1.00 21.43 ? 105 HIS B O   1 
ATOM   2922 C  CB  . HIS B 1 105 ? -27.393 20.464  1.485   1.00 25.40 ? 105 HIS B CB  1 
ATOM   2923 C  CG  . HIS B 1 105 ? -28.519 20.452  0.534   1.00 33.02 ? 105 HIS B CG  1 
ATOM   2924 N  ND1 . HIS B 1 105 ? -29.315 19.340  0.319   1.00 33.66 ? 105 HIS B ND1 1 
ATOM   2925 C  CD2 . HIS B 1 105 ? -29.007 21.461  -0.294  1.00 31.20 ? 105 HIS B CD2 1 
ATOM   2926 C  CE1 . HIS B 1 105 ? -30.245 19.655  -0.639  1.00 30.92 ? 105 HIS B CE1 1 
ATOM   2927 N  NE2 . HIS B 1 105 ? -30.067 20.948  -0.992  1.00 34.44 ? 105 HIS B NE2 1 
ATOM   2928 N  N   . GLY B 1 106 ? -24.411 20.712  -0.857  1.00 15.79 ? 106 GLY B N   1 
ATOM   2929 C  CA  . GLY B 1 106 ? -23.727 21.648  -1.785  1.00 15.00 ? 106 GLY B CA  1 
ATOM   2930 C  C   . GLY B 1 106 ? -23.636 21.276  -3.265  1.00 14.27 ? 106 GLY B C   1 
ATOM   2931 O  O   . GLY B 1 106 ? -23.319 22.163  -4.098  1.00 16.79 ? 106 GLY B O   1 
ATOM   2932 N  N   . SER B 1 107 ? -23.873 20.011  -3.600  1.00 13.26 ? 107 SER B N   1 
ATOM   2933 C  CA  . SER B 1 107 ? -23.732 19.599  -4.998  1.00 11.91 ? 107 SER B CA  1 
ATOM   2934 C  C   . SER B 1 107 ? -24.982 20.019  -5.776  1.00 12.03 ? 107 SER B C   1 
ATOM   2935 O  O   . SER B 1 107 ? -26.044 20.431  -5.297  1.00 14.72 ? 107 SER B O   1 
ATOM   2936 C  CB  . SER B 1 107 ? -23.435 18.122  -5.066  1.00 12.75 ? 107 SER B CB  1 
ATOM   2937 O  OG  . SER B 1 107 ? -24.532 17.338  -4.594  1.00 12.78 ? 107 SER B OG  1 
ATOM   2938 N  N   . GLU B 1 108 ? -24.833 19.922  -7.119  1.00 12.07 ? 108 GLU B N   1 
ATOM   2939 C  CA  . GLU B 1 108 ? -25.946 20.151  -8.027  1.00 11.88 ? 108 GLU B CA  1 
ATOM   2940 C  C   . GLU B 1 108 ? -26.688 18.833  -8.395  1.00 11.35 ? 108 GLU B C   1 
ATOM   2941 O  O   . GLU B 1 108 ? -27.864 18.685  -8.138  1.00 13.28 ? 108 GLU B O   1 
ATOM   2942 C  CB  . GLU B 1 108 ? -25.341 20.805  -9.310  1.00 12.04 ? 108 GLU B CB  1 
ATOM   2943 C  CG  . GLU B 1 108 ? -24.923 22.227  -8.986  1.00 14.67 ? 108 GLU B CG  1 
ATOM   2944 C  CD  . GLU B 1 108 ? -25.074 23.239  -10.108 1.00 14.22 ? 108 GLU B CD  1 
ATOM   2945 O  OE1 . GLU B 1 108 ? -24.541 22.943  -11.209 1.00 14.54 ? 108 GLU B OE1 1 
ATOM   2946 O  OE2 . GLU B 1 108 ? -25.563 24.353  -9.905  1.00 14.80 ? 108 GLU B OE2 1 
ATOM   2947 N  N   . HIS B 1 109 ? -25.954 17.857  -8.919  1.00 12.09 ? 109 HIS B N   1 
ATOM   2948 C  CA  . HIS B 1 109 ? -26.524 16.553  -9.037  1.00 13.18 ? 109 HIS B CA  1 
ATOM   2949 C  C   . HIS B 1 109 ? -26.652 15.903  -7.645  1.00 13.43 ? 109 HIS B C   1 
ATOM   2950 O  O   . HIS B 1 109 ? -25.835 16.129  -6.755  1.00 12.68 ? 109 HIS B O   1 
ATOM   2951 C  CB  . HIS B 1 109 ? -25.655 15.644  -9.965  1.00 12.49 ? 109 HIS B CB  1 
ATOM   2952 C  CG  . HIS B 1 109 ? -25.631 16.186  -11.388 1.00 12.26 ? 109 HIS B CG  1 
ATOM   2953 N  ND1 . HIS B 1 109 ? -24.738 17.128  -11.836 1.00 11.28 ? 109 HIS B ND1 1 
ATOM   2954 C  CD2 . HIS B 1 109 ? -26.540 15.953  -12.427 1.00 12.38 ? 109 HIS B CD2 1 
ATOM   2955 C  CE1 . HIS B 1 109 ? -25.120 17.474  -13.128 1.00 11.08 ? 109 HIS B CE1 1 
ATOM   2956 N  NE2 . HIS B 1 109 ? -26.176 16.748  -13.459 1.00 12.12 ? 109 HIS B NE2 1 
ATOM   2957 N  N   . ILE B 1 110 ? -27.689 15.089  -7.473  1.00 14.07 ? 110 ILE B N   1 
ATOM   2958 C  CA  . ILE B 1 110 ? -28.060 14.434  -6.194  1.00 15.76 ? 110 ILE B CA  1 
ATOM   2959 C  C   . ILE B 1 110 ? -28.199 12.931  -6.541  1.00 16.59 ? 110 ILE B C   1 
ATOM   2960 O  O   . ILE B 1 110 ? -28.750 12.620  -7.632  1.00 17.43 ? 110 ILE B O   1 
ATOM   2961 C  CB  . ILE B 1 110 ? -29.327 15.120  -5.673  1.00 17.31 ? 110 ILE B CB  1 
ATOM   2962 C  CG1 . ILE B 1 110 ? -29.014 16.673  -5.511  1.00 20.98 ? 110 ILE B CG1 1 
ATOM   2963 C  CG2 . ILE B 1 110 ? -29.760 14.420  -4.312  1.00 17.48 ? 110 ILE B CG2 1 
ATOM   2964 C  CD1 . ILE B 1 110 ? -30.020 17.538  -4.814  1.00 28.99 ? 110 ILE B CD1 1 
ATOM   2965 N  N   . VAL B 1 111 ? -27.574 12.068  -5.745  1.00 15.45 ? 111 VAL B N   1 
ATOM   2966 C  CA  . VAL B 1 111 ? -27.547 10.653  -6.014  1.00 15.18 ? 111 VAL B CA  1 
ATOM   2967 C  C   . VAL B 1 111 ? -28.361 9.847   -4.970  1.00 17.86 ? 111 VAL B C   1 
ATOM   2968 O  O   . VAL B 1 111 ? -27.947 9.728   -3.819  1.00 18.43 ? 111 VAL B O   1 
ATOM   2969 C  CB  . VAL B 1 111 ? -26.102 10.037  -6.086  1.00 15.90 ? 111 VAL B CB  1 
ATOM   2970 C  CG1 . VAL B 1 111 ? -26.233 8.529   -6.375  1.00 17.59 ? 111 VAL B CG1 1 
ATOM   2971 C  CG2 . VAL B 1 111 ? -25.225 10.731  -7.136  1.00 18.37 ? 111 VAL B CG2 1 
ATOM   2972 N  N   . ASP B 1 112 ? -29.539 9.367   -5.382  1.00 16.55 ? 112 ASP B N   1 
ATOM   2973 C  CA  . ASP B 1 112 ? -30.468 8.700   -4.437  1.00 17.78 ? 112 ASP B CA  1 
ATOM   2974 C  C   . ASP B 1 112 ? -30.641 9.577   -3.205  1.00 17.35 ? 112 ASP B C   1 
ATOM   2975 O  O   . ASP B 1 112 ? -30.648 9.071   -2.020  1.00 19.19 ? 112 ASP B O   1 
ATOM   2976 C  CB  . ASP B 1 112 ? -29.959 7.261   -4.138  1.00 19.37 ? 112 ASP B CB  1 
ATOM   2977 C  CG  . ASP B 1 112 ? -30.083 6.376   -5.355  1.00 23.41 ? 112 ASP B CG  1 
ATOM   2978 O  OD1 . ASP B 1 112 ? -31.137 6.408   -5.981  1.00 26.66 ? 112 ASP B OD1 1 
ATOM   2979 O  OD2 . ASP B 1 112 ? -29.119 5.642   -5.652  1.00 29.96 ? 112 ASP B OD2 1 
ATOM   2980 N  N   . GLY B 1 113 ? -30.871 10.872  -3.436  1.00 15.34 ? 113 GLY B N   1 
ATOM   2981 C  CA  . GLY B 1 113 ? -31.139 11.817  -2.334  1.00 16.67 ? 113 GLY B CA  1 
ATOM   2982 C  C   . GLY B 1 113 ? -29.898 12.333  -1.615  1.00 16.27 ? 113 GLY B C   1 
ATOM   2983 O  O   . GLY B 1 113 ? -29.994 13.205  -0.721  1.00 17.78 ? 113 GLY B O   1 
ATOM   2984 N  N   . VAL B 1 114 ? -28.704 11.828  -1.979  1.00 17.85 ? 114 VAL B N   1 
ATOM   2985 C  CA  . VAL B 1 114 ? -27.473 12.328  -1.270  1.00 20.60 ? 114 VAL B CA  1 
ATOM   2986 C  C   . VAL B 1 114 ? -26.943 13.526  -2.033  1.00 19.50 ? 114 VAL B C   1 
ATOM   2987 O  O   . VAL B 1 114 ? -26.642 13.379  -3.273  1.00 18.59 ? 114 VAL B O   1 
ATOM   2988 C  CB  . VAL B 1 114 ? -26.387 11.235  -1.216  1.00 20.87 ? 114 VAL B CB  1 
ATOM   2989 C  CG1 . VAL B 1 114 ? -25.075 11.821  -0.629  1.00 22.91 ? 114 VAL B CG1 1 
ATOM   2990 C  CG2 . VAL B 1 114 ? -26.900 10.052  -0.354  1.00 23.10 ? 114 VAL B CG2 1 
ATOM   2991 N  N   . SER B 1 115 ? -26.909 14.686  -1.369  1.00 20.05 ? 115 SER B N   1 
ATOM   2992 C  CA  . SER B 1 115 ? -26.226 15.869  -1.883  1.00 17.14 ? 115 SER B CA  1 
ATOM   2993 C  C   . SER B 1 115 ? -24.849 15.870  -1.256  1.00 21.19 ? 115 SER B C   1 
ATOM   2994 O  O   . SER B 1 115 ? -24.686 15.721  -0.012  1.00 21.47 ? 115 SER B O   1 
ATOM   2995 C  CB  . SER B 1 115 ? -27.042 17.113  -1.570  1.00 20.08 ? 115 SER B CB  1 
ATOM   2996 O  OG  . SER B 1 115 ? -26.336 18.320  -1.803  1.00 27.32 ? 115 SER B OG  1 
ATOM   2997 N  N   . TYR B 1 116 ? -23.817 16.070  -2.093  1.00 14.44 ? 116 TYR B N   1 
ATOM   2998 C  CA  . TYR B 1 116 ? -22.473 16.136  -1.606  1.00 15.27 ? 116 TYR B CA  1 
ATOM   2999 C  C   . TYR B 1 116 ? -22.086 17.536  -1.158  1.00 12.95 ? 116 TYR B C   1 
ATOM   3000 O  O   . TYR B 1 116 ? -22.844 18.472  -1.303  1.00 15.59 ? 116 TYR B O   1 
ATOM   3001 C  CB  . TYR B 1 116 ? -21.506 15.556  -2.698  1.00 13.65 ? 116 TYR B CB  1 
ATOM   3002 C  CG  . TYR B 1 116 ? -21.722 14.119  -2.933  1.00 16.54 ? 116 TYR B CG  1 
ATOM   3003 C  CD1 . TYR B 1 116 ? -21.026 13.162  -2.187  1.00 17.37 ? 116 TYR B CD1 1 
ATOM   3004 C  CD2 . TYR B 1 116 ? -22.639 13.689  -3.892  1.00 16.18 ? 116 TYR B CD2 1 
ATOM   3005 C  CE1 . TYR B 1 116 ? -21.282 11.798  -2.366  1.00 18.03 ? 116 TYR B CE1 1 
ATOM   3006 C  CE2 . TYR B 1 116 ? -22.881 12.379  -4.092  1.00 17.75 ? 116 TYR B CE2 1 
ATOM   3007 C  CZ  . TYR B 1 116 ? -22.168 11.441  -3.363  1.00 19.23 ? 116 TYR B CZ  1 
ATOM   3008 O  OH  . TYR B 1 116 ? -22.442 10.101  -3.581  1.00 26.47 ? 116 TYR B OH  1 
ATOM   3009 N  N   . ALA B 1 117 ? -20.904 17.687  -0.561  1.00 13.77 ? 117 ALA B N   1 
ATOM   3010 C  CA  . ALA B 1 117 ? -20.505 18.987  -0.098  1.00 14.56 ? 117 ALA B CA  1 
ATOM   3011 C  C   . ALA B 1 117 ? -20.260 20.019  -1.192  1.00 14.72 ? 117 ALA B C   1 
ATOM   3012 O  O   . ALA B 1 117 ? -20.476 21.187  -1.013  1.00 14.04 ? 117 ALA B O   1 
ATOM   3013 C  CB  . ALA B 1 117 ? -19.241 18.844  0.766   1.00 15.75 ? 117 ALA B CB  1 
ATOM   3014 N  N   . ALA B 1 118 ? -19.853 19.532  -2.388  1.00 11.47 ? 118 ALA B N   1 
ATOM   3015 C  CA  . ALA B 1 118 ? -19.631 20.509  -3.481  1.00 12.13 ? 118 ALA B CA  1 
ATOM   3016 C  C   . ALA B 1 118 ? -19.549 19.643  -4.759  1.00 11.23 ? 118 ALA B C   1 
ATOM   3017 O  O   . ALA B 1 118 ? -19.557 18.402  -4.719  1.00 11.16 ? 118 ALA B O   1 
ATOM   3018 C  CB  . ALA B 1 118 ? -18.331 21.297  -3.289  1.00 14.04 ? 118 ALA B CB  1 
ATOM   3019 N  N   . GLU B 1 119 ? -19.461 20.359  -5.893  1.00 11.32 ? 119 GLU B N   1 
ATOM   3020 C  CA  . GLU B 1 119 ? -19.402 19.627  -7.171  1.00 10.56 ? 119 GLU B CA  1 
ATOM   3021 C  C   . GLU B 1 119 ? -18.550 20.509  -8.118  1.00 10.93 ? 119 GLU B C   1 
ATOM   3022 O  O   . GLU B 1 119 ? -18.873 21.643  -8.378  1.00 10.74 ? 119 GLU B O   1 
ATOM   3023 C  CB  . GLU B 1 119 ? -20.821 19.412  -7.740  1.00 10.84 ? 119 GLU B CB  1 
ATOM   3024 C  CG  . GLU B 1 119 ? -20.822 18.553  -8.983  1.00 11.36 ? 119 GLU B CG  1 
ATOM   3025 C  CD  . GLU B 1 119 ? -22.224 18.249  -9.442  1.00 12.34 ? 119 GLU B CD  1 
ATOM   3026 O  OE1 . GLU B 1 119 ? -23.163 18.142  -8.603  1.00 11.92 ? 119 GLU B OE1 1 
ATOM   3027 O  OE2 . GLU B 1 119 ? -22.421 18.090  -10.708 1.00 14.08 ? 119 GLU B OE2 1 
ATOM   3028 N  N   . LEU B 1 120 ? -17.532 19.828  -8.644  1.00 10.14 ? 120 LEU B N   1 
ATOM   3029 C  CA  . LEU B 1 120 ? -16.597 20.414  -9.600  1.00 9.84  ? 120 LEU B CA  1 
ATOM   3030 C  C   . LEU B 1 120 ? -17.103 20.137  -11.048 1.00 11.82 ? 120 LEU B C   1 
ATOM   3031 O  O   . LEU B 1 120 ? -17.461 19.022  -11.322 1.00 11.30 ? 120 LEU B O   1 
ATOM   3032 C  CB  . LEU B 1 120 ? -15.217 19.829  -9.446  1.00 11.07 ? 120 LEU B CB  1 
ATOM   3033 C  CG  . LEU B 1 120 ? -14.077 20.510  -10.218 1.00 13.02 ? 120 LEU B CG  1 
ATOM   3034 C  CD1 . LEU B 1 120 ? -13.619 21.690  -9.408  1.00 13.81 ? 120 LEU B CD1 1 
ATOM   3035 C  CD2 . LEU B 1 120 ? -12.932 19.506  -10.462 1.00 16.06 ? 120 LEU B CD2 1 
ATOM   3036 N  N   . HIS B 1 121 ? -17.093 21.173  -11.861 1.00 10.01 ? 121 HIS B N   1 
ATOM   3037 C  CA  . HIS B 1 121 ? -17.434 21.014  -13.307 1.00 10.03 ? 121 HIS B CA  1 
ATOM   3038 C  C   . HIS B 1 121 ? -16.270 21.396  -14.152 1.00 9.21  ? 121 HIS B C   1 
ATOM   3039 O  O   . HIS B 1 121 ? -15.629 22.408  -14.040 1.00 10.79 ? 121 HIS B O   1 
ATOM   3040 C  CB  . HIS B 1 121 ? -18.641 21.945  -13.630 1.00 10.12 ? 121 HIS B CB  1 
ATOM   3041 C  CG  . HIS B 1 121 ? -19.908 21.470  -12.980 1.00 9.96  ? 121 HIS B CG  1 
ATOM   3042 N  ND1 . HIS B 1 121 ? -21.026 22.231  -12.825 1.00 12.12 ? 121 HIS B ND1 1 
ATOM   3043 C  CD2 . HIS B 1 121 ? -20.229 20.217  -12.475 1.00 10.32 ? 121 HIS B CD2 1 
ATOM   3044 C  CE1 . HIS B 1 121 ? -21.988 21.483  -12.235 1.00 11.04 ? 121 HIS B CE1 1 
ATOM   3045 N  NE2 . HIS B 1 121 ? -21.519 20.291  -12.009 1.00 11.50 ? 121 HIS B NE2 1 
ATOM   3046 N  N   . VAL B 1 122 ? -15.991 20.449  -15.111 1.00 10.08 ? 122 VAL B N   1 
ATOM   3047 C  CA  . VAL B 1 122 ? -14.919 20.625  -16.090 1.00 10.38 ? 122 VAL B CA  1 
ATOM   3048 C  C   . VAL B 1 122 ? -15.599 20.709  -17.480 1.00 10.95 ? 122 VAL B C   1 
ATOM   3049 O  O   . VAL B 1 122 ? -16.247 19.733  -17.927 1.00 11.36 ? 122 VAL B O   1 
ATOM   3050 C  CB  . VAL B 1 122 ? -14.014 19.388  -16.080 1.00 11.18 ? 122 VAL B CB  1 
ATOM   3051 C  CG1 . VAL B 1 122 ? -12.816 19.666  -16.974 1.00 13.10 ? 122 VAL B CG1 1 
ATOM   3052 C  CG2 . VAL B 1 122 ? -13.589 19.015  -14.594 1.00 13.46 ? 122 VAL B CG2 1 
ATOM   3053 N  N   . VAL B 1 123 ? -15.498 21.896  -18.077 1.00 9.79  ? 123 VAL B N   1 
ATOM   3054 C  CA  . VAL B 1 123 ? -16.288 22.204  -19.308 1.00 10.77 ? 123 VAL B CA  1 
ATOM   3055 C  C   . VAL B 1 123 ? -15.394 22.107  -20.533 1.00 9.62  ? 123 VAL B C   1 
ATOM   3056 O  O   . VAL B 1 123 ? -14.259 22.591  -20.574 1.00 12.73 ? 123 VAL B O   1 
ATOM   3057 C  CB  . VAL B 1 123 ? -16.799 23.665  -19.189 1.00 11.63 ? 123 VAL B CB  1 
ATOM   3058 C  CG1 . VAL B 1 123 ? -17.611 24.128  -20.383 1.00 12.91 ? 123 VAL B CG1 1 
ATOM   3059 C  CG2 . VAL B 1 123 ? -17.597 23.878  -17.877 1.00 12.57 ? 123 VAL B CG2 1 
ATOM   3060 N  N   . HIS B 1 124 ? -15.979 21.331  -21.505 1.00 11.72 ? 124 HIS B N   1 
ATOM   3061 C  CA  . HIS B 1 124 ? -15.247 21.066  -22.766 1.00 11.72 ? 124 HIS B CA  1 
ATOM   3062 C  C   . HIS B 1 124 ? -16.145 21.367  -23.918 1.00 11.81 ? 124 HIS B C   1 
ATOM   3063 O  O   . HIS B 1 124 ? -17.344 21.243  -23.834 1.00 11.71 ? 124 HIS B O   1 
ATOM   3064 C  CB  . HIS B 1 124 ? -14.891 19.552  -22.892 1.00 11.61 ? 124 HIS B CB  1 
ATOM   3065 C  CG  . HIS B 1 124 ? -14.247 18.938  -21.627 1.00 10.85 ? 124 HIS B CG  1 
ATOM   3066 N  ND1 . HIS B 1 124 ? -15.002 18.661  -20.531 1.00 11.52 ? 124 HIS B ND1 1 
ATOM   3067 C  CD2 . HIS B 1 124 ? -12.959 18.470  -21.337 1.00 11.28 ? 124 HIS B CD2 1 
ATOM   3068 C  CE1 . HIS B 1 124 ? -14.208 18.081  -19.615 1.00 11.63 ? 124 HIS B CE1 1 
ATOM   3069 N  NE2 . HIS B 1 124 ? -12.980 17.928  -20.119 1.00 11.93 ? 124 HIS B NE2 1 
ATOM   3070 N  N   . TRP B 1 125 ? -15.539 21.598  -25.098 1.00 12.61 ? 125 TRP B N   1 
ATOM   3071 C  CA  . TRP B 1 125 ? -16.342 21.842  -26.291 1.00 13.83 ? 125 TRP B CA  1 
ATOM   3072 C  C   . TRP B 1 125 ? -15.821 21.059  -27.510 1.00 13.52 ? 125 TRP B C   1 
ATOM   3073 O  O   . TRP B 1 125 ? -14.638 20.833  -27.702 1.00 13.92 ? 125 TRP B O   1 
ATOM   3074 C  CB  . TRP B 1 125 ? -16.386 23.335  -26.600 1.00 13.29 ? 125 TRP B CB  1 
ATOM   3075 C  CG  . TRP B 1 125 ? -15.082 24.011  -26.868 1.00 13.39 ? 125 TRP B CG  1 
ATOM   3076 C  CD1 . TRP B 1 125 ? -14.220 24.538  -25.948 1.00 14.80 ? 125 TRP B CD1 1 
ATOM   3077 C  CD2 . TRP B 1 125 ? -14.483 24.319  -28.173 1.00 14.33 ? 125 TRP B CD2 1 
ATOM   3078 N  NE1 . TRP B 1 125 ? -13.158 25.161  -26.508 1.00 15.75 ? 125 TRP B NE1 1 
ATOM   3079 C  CE2 . TRP B 1 125 ? -13.270 25.053  -27.891 1.00 14.35 ? 125 TRP B CE2 1 
ATOM   3080 C  CE3 . TRP B 1 125 ? -14.870 24.066  -29.523 1.00 16.79 ? 125 TRP B CE3 1 
ATOM   3081 C  CZ2 . TRP B 1 125 ? -12.421 25.491  -28.863 1.00 17.65 ? 125 TRP B CZ2 1 
ATOM   3082 C  CZ3 . TRP B 1 125 ? -14.012 24.561  -30.498 1.00 17.37 ? 125 TRP B CZ3 1 
ATOM   3083 C  CH2 . TRP B 1 125 ? -12.840 25.284  -30.178 1.00 18.37 ? 125 TRP B CH2 1 
ATOM   3084 N  N   . ASN B 1 126 ? -16.775 20.760  -28.377 1.00 14.92 ? 126 ASN B N   1 
ATOM   3085 C  CA  . ASN B 1 126 ? -16.508 19.891  -29.547 1.00 14.80 ? 126 ASN B CA  1 
ATOM   3086 C  C   . ASN B 1 126 ? -15.811 20.671  -30.670 1.00 14.59 ? 126 ASN B C   1 
ATOM   3087 O  O   . ASN B 1 126 ? -16.504 21.319  -31.542 1.00 15.58 ? 126 ASN B O   1 
ATOM   3088 C  CB  . ASN B 1 126 ? -17.868 19.351  -29.992 1.00 14.31 ? 126 ASN B CB  1 
ATOM   3089 C  CG  . ASN B 1 126 ? -17.747 18.356  -31.114 1.00 16.33 ? 126 ASN B CG  1 
ATOM   3090 O  OD1 . ASN B 1 126 ? -16.672 18.187  -31.700 1.00 15.78 ? 126 ASN B OD1 1 
ATOM   3091 N  ND2 . ASN B 1 126 ? -18.810 17.620  -31.307 1.00 17.85 ? 126 ASN B ND2 1 
ATOM   3092 N  N   . SER B 1 127 ? -14.500 20.509  -30.687 1.00 14.38 ? 127 SER B N   1 
ATOM   3093 C  CA  . SER B 1 127 ? -13.709 21.204  -31.717 1.00 13.92 ? 127 SER B CA  1 
ATOM   3094 C  C   . SER B 1 127 ? -13.670 20.412  -32.983 1.00 15.61 ? 127 SER B C   1 
ATOM   3095 O  O   . SER B 1 127 ? -13.185 20.946  -34.001 1.00 18.07 ? 127 SER B O   1 
ATOM   3096 C  CB  . SER B 1 127 ? -12.299 21.604  -31.226 1.00 14.25 ? 127 SER B CB  1 
ATOM   3097 O  OG  . SER B 1 127 ? -11.632 20.467  -30.797 1.00 19.56 ? 127 SER B OG  1 
ATOM   3098 N  N   . ASP B 1 128 ? -14.080 19.136  -32.944 1.00 17.11 ? 128 ASP B N   1 
ATOM   3099 C  CA  . ASP B 1 128 ? -14.107 18.359  -34.195 1.00 18.03 ? 128 ASP B CA  1 
ATOM   3100 C  C   . ASP B 1 128 ? -15.272 18.807  -35.097 1.00 19.08 ? 128 ASP B C   1 
ATOM   3101 O  O   . ASP B 1 128 ? -15.222 18.590  -36.302 1.00 21.92 ? 128 ASP B O   1 
ATOM   3102 C  CB  . ASP B 1 128 ? -14.321 16.896  -33.921 1.00 17.99 ? 128 ASP B CB  1 
ATOM   3103 C  CG  . ASP B 1 128 ? -13.066 16.174  -33.461 1.00 18.83 ? 128 ASP B CG  1 
ATOM   3104 O  OD1 . ASP B 1 128 ? -13.194 14.995  -33.047 1.00 20.87 ? 128 ASP B OD1 1 
ATOM   3105 O  OD2 . ASP B 1 128 ? -11.937 16.719  -33.455 1.00 26.52 ? 128 ASP B OD2 1 
ATOM   3106 N  N   . LYS B 1 129 ? -16.316 19.438  -34.565 1.00 17.79 ? 129 LYS B N   1 
ATOM   3107 C  CA  . LYS B 1 129 ? -17.449 19.901  -35.337 1.00 17.30 ? 129 LYS B CA  1 
ATOM   3108 C  C   . LYS B 1 129 ? -17.624 21.393  -35.332 1.00 17.84 ? 129 LYS B C   1 
ATOM   3109 O  O   . LYS B 1 129 ? -18.304 21.927  -36.263 1.00 17.24 ? 129 LYS B O   1 
ATOM   3110 C  CB  . LYS B 1 129 ? -18.740 19.279  -34.834 1.00 18.90 ? 129 LYS B CB  1 
ATOM   3111 C  CG  . LYS B 1 129 ? -18.956 17.798  -35.200 1.00 22.97 ? 129 LYS B CG  1 
ATOM   3112 C  CD  . LYS B 1 129 ? -20.416 17.341  -34.941 1.00 24.33 ? 129 LYS B CD  1 
ATOM   3113 C  CE  . LYS B 1 129 ? -21.499 18.190  -35.669 1.00 28.23 ? 129 LYS B CE  1 
ATOM   3114 N  NZ  . LYS B 1 129 ? -22.878 17.602  -35.392 1.00 26.66 ? 129 LYS B NZ  1 
ATOM   3115 N  N   . TYR B 1 130 ? -17.111 22.128  -34.309 1.00 15.66 ? 130 TYR B N   1 
ATOM   3116 C  CA  . TYR B 1 130 ? -17.386 23.531  -34.181 1.00 15.90 ? 130 TYR B CA  1 
ATOM   3117 C  C   . TYR B 1 130 ? -16.107 24.322  -34.108 1.00 15.83 ? 130 TYR B C   1 
ATOM   3118 O  O   . TYR B 1 130 ? -15.061 23.811  -33.636 1.00 15.99 ? 130 TYR B O   1 
ATOM   3119 C  CB  . TYR B 1 130 ? -18.282 23.829  -32.907 1.00 17.74 ? 130 TYR B CB  1 
ATOM   3120 C  CG  . TYR B 1 130 ? -19.579 23.073  -33.059 1.00 16.21 ? 130 TYR B CG  1 
ATOM   3121 C  CD1 . TYR B 1 130 ? -20.525 23.400  -34.070 1.00 18.75 ? 130 TYR B CD1 1 
ATOM   3122 C  CD2 . TYR B 1 130 ? -19.848 21.894  -32.321 1.00 14.35 ? 130 TYR B CD2 1 
ATOM   3123 C  CE1 . TYR B 1 130 ? -21.647 22.613  -34.254 1.00 20.69 ? 130 TYR B CE1 1 
ATOM   3124 C  CE2 . TYR B 1 130 ? -20.984 21.086  -32.502 1.00 14.33 ? 130 TYR B CE2 1 
ATOM   3125 C  CZ  . TYR B 1 130 ? -21.918 21.481  -33.498 1.00 18.40 ? 130 TYR B CZ  1 
ATOM   3126 O  OH  . TYR B 1 130 ? -22.963 20.652  -33.598 1.00 19.90 ? 130 TYR B OH  1 
ATOM   3127 N  N   . PRO B 1 131 ? -16.110 25.567  -34.612 1.00 16.39 ? 131 PRO B N   1 
ATOM   3128 C  CA  . PRO B 1 131 ? -14.848 26.328  -34.631 1.00 17.57 ? 131 PRO B CA  1 
ATOM   3129 C  C   . PRO B 1 131 ? -14.470 27.042  -33.315 1.00 17.71 ? 131 PRO B C   1 
ATOM   3130 O  O   . PRO B 1 131 ? -13.366 27.595  -33.203 1.00 19.22 ? 131 PRO B O   1 
ATOM   3131 C  CB  . PRO B 1 131 ? -15.099 27.415  -35.722 1.00 16.69 ? 131 PRO B CB  1 
ATOM   3132 C  CG  . PRO B 1 131 ? -16.549 27.600  -35.688 1.00 15.83 ? 131 PRO B CG  1 
ATOM   3133 C  CD  . PRO B 1 131 ? -17.184 26.254  -35.351 1.00 17.12 ? 131 PRO B CD  1 
ATOM   3134 N  N   . SER B 1 132 ? -15.431 27.113  -32.389 1.00 17.45 ? 132 SER B N   1 
ATOM   3135 C  CA  . SER B 1 132 ? -15.131 27.856  -31.147 1.00 17.67 ? 132 SER B CA  1 
ATOM   3136 C  C   . SER B 1 132 ? -16.148 27.330  -30.114 1.00 15.55 ? 132 SER B C   1 
ATOM   3137 O  O   . SER B 1 132 ? -17.209 26.795  -30.386 1.00 14.98 ? 132 SER B O   1 
ATOM   3138 C  CB  . SER B 1 132 ? -15.412 29.333  -31.320 1.00 17.95 ? 132 SER B CB  1 
ATOM   3139 O  OG  . SER B 1 132 ? -16.784 29.575  -31.528 1.00 20.58 ? 132 SER B OG  1 
ATOM   3140 N  N   . PHE B 1 133 ? -15.751 27.532  -28.850 1.00 17.31 ? 133 PHE B N   1 
ATOM   3141 C  CA  . PHE B 1 133 ? -16.641 27.296  -27.726 1.00 19.18 ? 133 PHE B CA  1 
ATOM   3142 C  C   . PHE B 1 133 ? -17.968 28.031  -27.849 1.00 17.78 ? 133 PHE B C   1 
ATOM   3143 O  O   . PHE B 1 133 ? -18.999 27.430  -27.633 1.00 16.55 ? 133 PHE B O   1 
ATOM   3144 C  CB  . PHE B 1 133 ? -15.946 27.856  -26.480 1.00 17.31 ? 133 PHE B CB  1 
ATOM   3145 C  CG  . PHE B 1 133 ? -16.804 27.831  -25.228 1.00 19.96 ? 133 PHE B CG  1 
ATOM   3146 C  CD1 . PHE B 1 133 ? -17.087 26.604  -24.582 1.00 19.71 ? 133 PHE B CD1 1 
ATOM   3147 C  CD2 . PHE B 1 133 ? -17.385 29.031  -24.734 1.00 22.70 ? 133 PHE B CD2 1 
ATOM   3148 C  CE1 . PHE B 1 133 ? -17.955 26.588  -23.473 1.00 21.97 ? 133 PHE B CE1 1 
ATOM   3149 C  CE2 . PHE B 1 133 ? -18.222 29.013  -23.614 1.00 23.62 ? 133 PHE B CE2 1 
ATOM   3150 C  CZ  . PHE B 1 133 ? -18.476 27.794  -22.990 1.00 21.03 ? 133 PHE B CZ  1 
ATOM   3151 N  N   . VAL B 1 134 ? -17.965 29.304  -28.279 1.00 19.05 ? 134 VAL B N   1 
ATOM   3152 C  CA  . VAL B 1 134 ? -19.232 30.033  -28.461 1.00 22.48 ? 134 VAL B CA  1 
ATOM   3153 C  C   . VAL B 1 134 ? -20.220 29.343  -29.405 1.00 20.81 ? 134 VAL B C   1 
ATOM   3154 O  O   . VAL B 1 134 ? -21.421 29.210  -29.141 1.00 20.69 ? 134 VAL B O   1 
ATOM   3155 C  CB  . VAL B 1 134 ? -18.932 31.462  -28.975 1.00 26.41 ? 134 VAL B CB  1 
ATOM   3156 C  CG1 . VAL B 1 134 ? -20.224 32.106  -29.473 1.00 34.00 ? 134 VAL B CG1 1 
ATOM   3157 C  CG2 . VAL B 1 134 ? -18.338 32.267  -27.813 1.00 28.53 ? 134 VAL B CG2 1 
ATOM   3158 N  N   . GLU B 1 135 ? -19.729 28.829  -30.562 1.00 19.19 ? 135 GLU B N   1 
ATOM   3159 C  CA  . GLU B 1 135 ? -20.649 28.166  -31.450 1.00 21.01 ? 135 GLU B CA  1 
ATOM   3160 C  C   . GLU B 1 135 ? -21.094 26.815  -30.916 1.00 20.19 ? 135 GLU B C   1 
ATOM   3161 O  O   . GLU B 1 135 ? -22.239 26.362  -31.073 1.00 19.75 ? 135 GLU B O   1 
ATOM   3162 C  CB  . GLU B 1 135 ? -19.969 27.941  -32.848 1.00 21.08 ? 135 GLU B CB  1 
ATOM   3163 C  CG  . GLU B 1 135 ? -19.668 29.292  -33.552 1.00 23.24 ? 135 GLU B CG  1 
ATOM   3164 C  CD  . GLU B 1 135 ? -20.907 29.924  -34.117 1.00 25.40 ? 135 GLU B CD  1 
ATOM   3165 O  OE1 . GLU B 1 135 ? -22.050 29.342  -34.032 1.00 26.83 ? 135 GLU B OE1 1 
ATOM   3166 O  OE2 . GLU B 1 135 ? -20.691 31.012  -34.677 1.00 31.23 ? 135 GLU B OE2 1 
ATOM   3167 N  N   . ALA B 1 136 ? -20.137 26.143  -30.262 1.00 17.24 ? 136 ALA B N   1 
ATOM   3168 C  CA  . ALA B 1 136 ? -20.424 24.790  -29.777 1.00 15.65 ? 136 ALA B CA  1 
ATOM   3169 C  C   . ALA B 1 136 ? -21.514 24.889  -28.658 1.00 16.09 ? 136 ALA B C   1 
ATOM   3170 O  O   . ALA B 1 136 ? -22.315 23.997  -28.504 1.00 16.10 ? 136 ALA B O   1 
ATOM   3171 C  CB  . ALA B 1 136 ? -19.145 24.144  -29.256 1.00 15.80 ? 136 ALA B CB  1 
ATOM   3172 N  N   . ALA B 1 137 ? -21.481 26.001  -27.937 1.00 17.02 ? 137 ALA B N   1 
ATOM   3173 C  CA  . ALA B 1 137 ? -22.406 26.154  -26.797 1.00 19.76 ? 137 ALA B CA  1 
ATOM   3174 C  C   . ALA B 1 137 ? -23.894 26.215  -27.203 1.00 18.78 ? 137 ALA B C   1 
ATOM   3175 O  O   . ALA B 1 137 ? -24.792 26.047  -26.331 1.00 17.94 ? 137 ALA B O   1 
ATOM   3176 C  CB  . ALA B 1 137 ? -22.028 27.355  -25.919 1.00 15.95 ? 137 ALA B CB  1 
ATOM   3177 N  N   . HIS B 1 138 ? -24.177 26.374  -28.500 1.00 19.39 ? 138 HIS B N   1 
ATOM   3178 C  CA  . HIS B 1 138 ? -25.543 26.471  -28.983 1.00 22.08 ? 138 HIS B CA  1 
ATOM   3179 C  C   . HIS B 1 138 ? -25.993 25.287  -29.780 1.00 20.82 ? 138 HIS B C   1 
ATOM   3180 O  O   . HIS B 1 138 ? -26.980 25.348  -30.500 1.00 24.11 ? 138 HIS B O   1 
ATOM   3181 C  CB  . HIS B 1 138 ? -25.632 27.749  -29.846 1.00 22.97 ? 138 HIS B CB  1 
ATOM   3182 C  CG  . HIS B 1 138 ? -25.607 28.998  -29.031 1.00 24.11 ? 138 HIS B CG  1 
ATOM   3183 N  ND1 . HIS B 1 138 ? -26.751 29.523  -28.505 1.00 28.19 ? 138 HIS B ND1 1 
ATOM   3184 C  CD2 . HIS B 1 138 ? -24.550 29.782  -28.566 1.00 25.43 ? 138 HIS B CD2 1 
ATOM   3185 C  CE1 . HIS B 1 138 ? -26.428 30.624  -27.790 1.00 28.11 ? 138 HIS B CE1 1 
ATOM   3186 N  NE2 . HIS B 1 138 ? -25.096 30.784  -27.828 1.00 26.88 ? 138 HIS B NE2 1 
ATOM   3187 N  N   . GLU B 1 139 ? -25.304 24.171  -29.629 1.00 20.47 ? 139 GLU B N   1 
ATOM   3188 C  CA  . GLU B 1 139 ? -25.634 22.967  -30.277 1.00 20.42 ? 139 GLU B CA  1 
ATOM   3189 C  C   . GLU B 1 139 ? -25.812 21.769  -29.358 1.00 20.10 ? 139 GLU B C   1 
ATOM   3190 O  O   . GLU B 1 139 ? -25.016 21.660  -28.400 1.00 17.84 ? 139 GLU B O   1 
ATOM   3191 C  CB  . GLU B 1 139 ? -24.484 22.594  -31.266 1.00 23.47 ? 139 GLU B CB  1 
ATOM   3192 C  CG  . GLU B 1 139 ? -24.220 23.594  -32.355 1.00 31.94 ? 139 GLU B CG  1 
ATOM   3193 C  CD  . GLU B 1 139 ? -25.197 23.417  -33.516 1.00 34.24 ? 139 GLU B CD  1 
ATOM   3194 O  OE1 . GLU B 1 139 ? -24.763 23.731  -34.646 1.00 42.12 ? 139 GLU B OE1 1 
ATOM   3195 O  OE2 . GLU B 1 139 ? -26.377 23.018  -33.316 1.00 38.97 ? 139 GLU B OE2 1 
ATOM   3196 N  N   . PRO B 1 140 ? -26.705 20.828  -29.645 1.00 18.98 ? 140 PRO B N   1 
ATOM   3197 C  CA  . PRO B 1 140 ? -26.962 19.743  -28.688 1.00 17.99 ? 140 PRO B CA  1 
ATOM   3198 C  C   . PRO B 1 140 ? -25.739 18.893  -28.416 1.00 18.95 ? 140 PRO B C   1 
ATOM   3199 O  O   . PRO B 1 140 ? -25.585 18.439  -27.250 1.00 18.47 ? 140 PRO B O   1 
ATOM   3200 C  CB  . PRO B 1 140 ? -28.058 18.863  -29.377 1.00 18.30 ? 140 PRO B CB  1 
ATOM   3201 C  CG  . PRO B 1 140 ? -28.765 19.901  -30.228 1.00 25.06 ? 140 PRO B CG  1 
ATOM   3202 C  CD  . PRO B 1 140 ? -27.714 20.845  -30.738 1.00 22.29 ? 140 PRO B CD  1 
ATOM   3203 N  N   . ASP B 1 141 ? -24.856 18.696  -29.403 1.00 16.29 ? 141 ASP B N   1 
ATOM   3204 C  CA  . ASP B 1 141 ? -23.675 17.900  -29.207 1.00 16.70 ? 141 ASP B CA  1 
ATOM   3205 C  C   . ASP B 1 141 ? -22.422 18.827  -28.963 1.00 15.79 ? 141 ASP B C   1 
ATOM   3206 O  O   . ASP B 1 141 ? -21.255 18.406  -29.110 1.00 16.87 ? 141 ASP B O   1 
ATOM   3207 C  CB  . ASP B 1 141 ? -23.417 16.980  -30.398 1.00 18.81 ? 141 ASP B CB  1 
ATOM   3208 C  CG  . ASP B 1 141 ? -23.251 17.759  -31.675 1.00 20.65 ? 141 ASP B CG  1 
ATOM   3209 O  OD1 . ASP B 1 141 ? -23.485 18.990  -31.714 1.00 18.10 ? 141 ASP B OD1 1 
ATOM   3210 O  OD2 . ASP B 1 141 ? -22.838 17.076  -32.684 1.00 22.81 ? 141 ASP B OD2 1 
ATOM   3211 N  N   . GLY B 1 142 ? -22.649 20.086  -28.578 1.00 13.53 ? 142 GLY B N   1 
ATOM   3212 C  CA  . GLY B 1 142 ? -21.516 21.029  -28.541 1.00 13.80 ? 142 GLY B CA  1 
ATOM   3213 C  C   . GLY B 1 142 ? -20.588 20.931  -27.313 1.00 12.74 ? 142 GLY B C   1 
ATOM   3214 O  O   . GLY B 1 142 ? -19.376 21.148  -27.415 1.00 14.57 ? 142 GLY B O   1 
ATOM   3215 N  N   . LEU B 1 143 ? -21.230 20.656  -26.160 1.00 13.31 ? 143 LEU B N   1 
ATOM   3216 C  CA  . LEU B 1 143 ? -20.439 20.708  -24.917 1.00 12.15 ? 143 LEU B CA  1 
ATOM   3217 C  C   . LEU B 1 143 ? -20.473 19.392  -24.165 1.00 10.96 ? 143 LEU B C   1 
ATOM   3218 O  O   . LEU B 1 143 ? -21.392 18.620  -24.267 1.00 12.45 ? 143 LEU B O   1 
ATOM   3219 C  CB  . LEU B 1 143 ? -21.050 21.815  -24.001 1.00 12.41 ? 143 LEU B CB  1 
ATOM   3220 C  CG  . LEU B 1 143 ? -21.133 23.239  -24.530 1.00 13.29 ? 143 LEU B CG  1 
ATOM   3221 C  CD1 . LEU B 1 143 ? -21.665 24.159  -23.375 1.00 13.97 ? 143 LEU B CD1 1 
ATOM   3222 C  CD2 . LEU B 1 143 ? -19.759 23.715  -25.006 1.00 13.76 ? 143 LEU B CD2 1 
ATOM   3223 N  N   . ALA B 1 144 ? -19.397 19.200  -23.390 1.00 11.92 ? 144 ALA B N   1 
ATOM   3224 C  CA  . ALA B 1 144 ? -19.327 17.979  -22.513 1.00 10.72 ? 144 ALA B CA  1 
ATOM   3225 C  C   . ALA B 1 144 ? -18.813 18.574  -21.202 1.00 9.66  ? 144 ALA B C   1 
ATOM   3226 O  O   . ALA B 1 144 ? -17.803 19.230  -21.174 1.00 12.70 ? 144 ALA B O   1 
ATOM   3227 C  CB  . ALA B 1 144 ? -18.379 16.909  -23.013 1.00 12.72 ? 144 ALA B CB  1 
ATOM   3228 N  N   . VAL B 1 145 ? -19.605 18.236  -20.135 1.00 10.66 ? 145 VAL B N   1 
ATOM   3229 C  CA  . VAL B 1 145 ? -19.131 18.659  -18.795 1.00 10.54 ? 145 VAL B CA  1 
ATOM   3230 C  C   . VAL B 1 145 ? -18.976 17.450  -17.881 1.00 10.61 ? 145 VAL B C   1 
ATOM   3231 O  O   . VAL B 1 145 ? -19.885 16.585  -17.811 1.00 11.05 ? 145 VAL B O   1 
ATOM   3232 C  CB  . VAL B 1 145 ? -20.135 19.615  -18.147 1.00 11.93 ? 145 VAL B CB  1 
ATOM   3233 C  CG1 . VAL B 1 145 ? -19.594 20.125  -16.776 1.00 14.18 ? 145 VAL B CG1 1 
ATOM   3234 C  CG2 . VAL B 1 145 ? -20.342 20.825  -19.075 1.00 13.21 ? 145 VAL B CG2 1 
ATOM   3235 N  N   . LEU B 1 146 ? -17.771 17.357  -17.316 1.00 11.19 ? 146 LEU B N   1 
ATOM   3236 C  CA  . LEU B 1 146 ? -17.494 16.320  -16.359 1.00 11.91 ? 146 LEU B CA  1 
ATOM   3237 C  C   . LEU B 1 146 ? -17.851 16.818  -14.983 1.00 12.79 ? 146 LEU B C   1 
ATOM   3238 O  O   . LEU B 1 146 ? -17.305 17.870  -14.620 1.00 13.45 ? 146 LEU B O   1 
ATOM   3239 C  CB  . LEU B 1 146 ? -16.001 15.954  -16.508 1.00 14.02 ? 146 LEU B CB  1 
ATOM   3240 C  CG  . LEU B 1 146 ? -15.467 14.844  -15.623 1.00 16.54 ? 146 LEU B CG  1 
ATOM   3241 C  CD1 . LEU B 1 146 ? -16.169 13.516  -15.993 1.00 19.32 ? 146 LEU B CD1 1 
ATOM   3242 C  CD2 . LEU B 1 146 ? -13.924 14.768  -15.810 1.00 17.30 ? 146 LEU B CD2 1 
ATOM   3243 N  N   . GLY B 1 147 ? -18.657 16.071  -14.242 1.00 10.77 ? 147 GLY B N   1 
ATOM   3244 C  CA  . GLY B 1 147 ? -18.997 16.544  -12.858 1.00 12.66 ? 147 GLY B CA  1 
ATOM   3245 C  C   . GLY B 1 147 ? -18.294 15.630  -11.883 1.00 12.80 ? 147 GLY B C   1 
ATOM   3246 O  O   . GLY B 1 147 ? -18.318 14.368  -12.044 1.00 13.48 ? 147 GLY B O   1 
ATOM   3247 N  N   . VAL B 1 148 ? -17.637 16.197  -10.854 1.00 10.92 ? 148 VAL B N   1 
ATOM   3248 C  CA  . VAL B 1 148 ? -16.920 15.398  -9.828  1.00 11.25 ? 148 VAL B CA  1 
ATOM   3249 C  C   . VAL B 1 148 ? -17.464 15.892  -8.486  1.00 10.64 ? 148 VAL B C   1 
ATOM   3250 O  O   . VAL B 1 148 ? -17.380 17.082  -8.175  1.00 12.48 ? 148 VAL B O   1 
ATOM   3251 C  CB  . VAL B 1 148 ? -15.417 15.674  -9.900  1.00 12.48 ? 148 VAL B CB  1 
ATOM   3252 C  CG1 . VAL B 1 148 ? -14.703 14.770  -8.836  1.00 13.05 ? 148 VAL B CG1 1 
ATOM   3253 C  CG2 . VAL B 1 148 ? -14.910 15.364  -11.366 1.00 12.84 ? 148 VAL B CG2 1 
ATOM   3254 N  N   . PHE B 1 149 ? -18.002 14.972  -7.676  1.00 10.51 ? 149 PHE B N   1 
ATOM   3255 C  CA  . PHE B 1 149 ? -18.492 15.352  -6.362  1.00 11.77 ? 149 PHE B CA  1 
ATOM   3256 C  C   . PHE B 1 149 ? -17.304 15.500  -5.424  1.00 12.07 ? 149 PHE B C   1 
ATOM   3257 O  O   . PHE B 1 149 ? -16.267 14.822  -5.557  1.00 11.91 ? 149 PHE B O   1 
ATOM   3258 C  CB  . PHE B 1 149 ? -19.366 14.219  -5.787  1.00 12.63 ? 149 PHE B CB  1 
ATOM   3259 C  CG  . PHE B 1 149 ? -20.645 14.013  -6.609  1.00 11.46 ? 149 PHE B CG  1 
ATOM   3260 C  CD1 . PHE B 1 149 ? -21.525 15.073  -6.774  1.00 11.40 ? 149 PHE B CD1 1 
ATOM   3261 C  CD2 . PHE B 1 149 ? -20.917 12.737  -7.137  1.00 13.22 ? 149 PHE B CD2 1 
ATOM   3262 C  CE1 . PHE B 1 149 ? -22.732 14.870  -7.492  1.00 11.54 ? 149 PHE B CE1 1 
ATOM   3263 C  CE2 . PHE B 1 149 ? -22.126 12.535  -7.852  1.00 12.35 ? 149 PHE B CE2 1 
ATOM   3264 C  CZ  . PHE B 1 149 ? -22.977 13.605  -8.004  1.00 12.26 ? 149 PHE B CZ  1 
ATOM   3265 N  N   . LEU B 1 150 ? -17.473 16.425  -4.486  1.00 11.34 ? 150 LEU B N   1 
ATOM   3266 C  CA  . LEU B 1 150 ? -16.532 16.589  -3.303  1.00 12.89 ? 150 LEU B CA  1 
ATOM   3267 C  C   . LEU B 1 150 ? -17.276 16.261  -1.991  1.00 12.00 ? 150 LEU B C   1 
ATOM   3268 O  O   . LEU B 1 150 ? -18.433 16.710  -1.712  1.00 13.15 ? 150 LEU B O   1 
ATOM   3269 C  CB  . LEU B 1 150 ? -16.027 18.037  -3.207  1.00 13.11 ? 150 LEU B CB  1 
ATOM   3270 C  CG  . LEU B 1 150 ? -14.957 18.455  -4.238  1.00 13.44 ? 150 LEU B CG  1 
ATOM   3271 C  CD1 . LEU B 1 150 ? -15.591 18.540  -5.662  1.00 13.58 ? 150 LEU B CD1 1 
ATOM   3272 C  CD2 . LEU B 1 150 ? -14.518 19.862  -3.773  1.00 14.03 ? 150 LEU B CD2 1 
ATOM   3273 N  N   . GLN B 1 151 ? -16.595 15.423  -1.195  1.00 14.24 ? 151 GLN B N   1 
ATOM   3274 C  CA  . GLN B 1 151 ? -17.132 15.082  0.145   1.00 16.84 ? 151 GLN B CA  1 
ATOM   3275 C  C   . GLN B 1 151 ? -16.100 15.600  1.164   1.00 16.82 ? 151 GLN B C   1 
ATOM   3276 O  O   . GLN B 1 151 ? -14.913 15.771  0.855   1.00 15.78 ? 151 GLN B O   1 
ATOM   3277 C  CB  . GLN B 1 151 ? -17.405 13.617  0.224   1.00 22.37 ? 151 GLN B CB  1 
ATOM   3278 C  CG  . GLN B 1 151 ? -16.202 12.801  0.204   1.00 22.48 ? 151 GLN B CG  1 
ATOM   3279 C  CD  . GLN B 1 151 ? -16.607 11.333  0.338   1.00 25.27 ? 151 GLN B CD  1 
ATOM   3280 O  OE1 . GLN B 1 151 ? -17.771 10.998  0.541   1.00 27.49 ? 151 GLN B OE1 1 
ATOM   3281 N  NE2 . GLN B 1 151 ? -15.637 10.482  0.229   1.00 31.36 ? 151 GLN B NE2 1 
ATOM   3282 N  N   . ILE B 1 152 ? -16.543 15.903  2.398   1.00 16.02 ? 152 ILE B N   1 
ATOM   3283 C  CA  . ILE B 1 152 ? -15.592 16.379  3.416   1.00 16.39 ? 152 ILE B CA  1 
ATOM   3284 C  C   . ILE B 1 152 ? -14.704 15.190  3.855   1.00 17.23 ? 152 ILE B C   1 
ATOM   3285 O  O   . ILE B 1 152 ? -15.197 14.078  4.181   1.00 20.77 ? 152 ILE B O   1 
ATOM   3286 C  CB  . ILE B 1 152 ? -16.387 16.976  4.628   1.00 15.96 ? 152 ILE B CB  1 
ATOM   3287 C  CG1 . ILE B 1 152 ? -17.224 18.185  4.148   1.00 15.32 ? 152 ILE B CG1 1 
ATOM   3288 C  CG2 . ILE B 1 152 ? -15.418 17.393  5.730   1.00 17.16 ? 152 ILE B CG2 1 
ATOM   3289 C  CD1 . ILE B 1 152 ? -16.456 19.334  3.476   1.00 16.34 ? 152 ILE B CD1 1 
ATOM   3290 N  N   . GLY B 1 153 ? -13.432 15.449  3.894   1.00 16.06 ? 153 GLY B N   1 
ATOM   3291 C  CA  . GLY B 1 153 ? -12.461 14.487  4.452   1.00 19.03 ? 153 GLY B CA  1 
ATOM   3292 C  C   . GLY B 1 153 ? -11.155 15.174  4.626   1.00 16.75 ? 153 GLY B C   1 
ATOM   3293 O  O   . GLY B 1 153 ? -11.095 16.360  5.052   1.00 20.66 ? 153 GLY B O   1 
ATOM   3294 N  N   . GLU B 1 154 ? -10.094 14.467  4.212   1.00 17.70 ? 154 GLU B N   1 
ATOM   3295 C  CA  . GLU B 1 154 ? -8.747  15.030  4.366   1.00 20.49 ? 154 GLU B CA  1 
ATOM   3296 C  C   . GLU B 1 154 ? -8.579  16.222  3.415   1.00 18.08 ? 154 GLU B C   1 
ATOM   3297 O  O   . GLU B 1 154 ? -9.222  16.195  2.289   1.00 18.71 ? 154 GLU B O   1 
ATOM   3298 C  CB  . GLU B 1 154 ? -7.727  13.928  4.016   1.00 26.40 ? 154 GLU B CB  1 
ATOM   3299 C  CG  . GLU B 1 154 ? -6.459  14.200  3.166   1.00 30.55 ? 154 GLU B CG  1 
ATOM   3300 C  CD  . GLU B 1 154 ? -5.509  12.949  3.051   1.00 34.41 ? 154 GLU B CD  1 
ATOM   3301 O  OE1 . GLU B 1 154 ? -5.007  12.563  1.929   1.00 29.59 ? 154 GLU B OE1 1 
ATOM   3302 O  OE2 . GLU B 1 154 ? -5.274  12.294  4.130   1.00 37.47 ? 154 GLU B OE2 1 
ATOM   3303 N  N   . PRO B 1 155 ? -7.741  17.190  3.757   1.00 18.87 ? 155 PRO B N   1 
ATOM   3304 C  CA  . PRO B 1 155 ? -7.479  18.299  2.912   1.00 16.37 ? 155 PRO B CA  1 
ATOM   3305 C  C   . PRO B 1 155 ? -6.921  17.753  1.573   1.00 15.55 ? 155 PRO B C   1 
ATOM   3306 O  O   . PRO B 1 155 ? -6.244  16.735  1.498   1.00 18.55 ? 155 PRO B O   1 
ATOM   3307 C  CB  . PRO B 1 155 ? -6.347  19.094  3.623   1.00 18.60 ? 155 PRO B CB  1 
ATOM   3308 C  CG  . PRO B 1 155 ? -6.401  18.649  5.057   1.00 17.31 ? 155 PRO B CG  1 
ATOM   3309 C  CD  . PRO B 1 155 ? -7.033  17.290  5.102   1.00 16.22 ? 155 PRO B CD  1 
ATOM   3310 N  N   . ASN B 1 156 ? -7.254  18.478  0.505   1.00 16.45 ? 156 ASN B N   1 
ATOM   3311 C  CA  . ASN B 1 156 ? -6.821  18.041  -0.819  1.00 16.17 ? 156 ASN B CA  1 
ATOM   3312 C  C   . ASN B 1 156 ? -5.696  18.926  -1.270  1.00 17.80 ? 156 ASN B C   1 
ATOM   3313 O  O   . ASN B 1 156 ? -5.847  20.122  -1.429  1.00 16.26 ? 156 ASN B O   1 
ATOM   3314 C  CB  . ASN B 1 156 ? -8.037  18.174  -1.723  1.00 15.77 ? 156 ASN B CB  1 
ATOM   3315 C  CG  . ASN B 1 156 ? -7.815  17.647  -3.069  1.00 19.46 ? 156 ASN B CG  1 
ATOM   3316 O  OD1 . ASN B 1 156 ? -6.893  18.090  -3.755  1.00 22.34 ? 156 ASN B OD1 1 
ATOM   3317 N  ND2 . ASN B 1 156 ? -8.692  16.737  -3.506  1.00 17.79 ? 156 ASN B ND2 1 
ATOM   3318 N  N   . SER B 1 157 ? -4.524  18.319  -1.471  1.00 19.54 ? 157 SER B N   1 
ATOM   3319 C  CA  . SER B 1 157 ? -3.387  19.177  -1.767  1.00 18.95 ? 157 SER B CA  1 
ATOM   3320 C  C   . SER B 1 157 ? -3.464  19.942  -3.097  1.00 20.12 ? 157 SER B C   1 
ATOM   3321 O  O   . SER B 1 157 ? -2.901  21.046  -3.170  1.00 22.60 ? 157 SER B O   1 
ATOM   3322 C  CB  . SER B 1 157 ? -2.043  18.358  -1.649  1.00 22.81 ? 157 SER B CB  1 
ATOM   3323 O  OG  . SER B 1 157 ? -2.031  17.325  -2.622  1.00 24.29 ? 157 SER B OG  1 
ATOM   3324 N  N   A GLN B 1 158 ? -4.125  19.373  -4.105  0.50 19.57 ? 158 GLN B N   1 
ATOM   3325 N  N   B GLN B 1 158 ? -4.158  19.435  -4.112  0.50 19.78 ? 158 GLN B N   1 
ATOM   3326 C  CA  A GLN B 1 158 ? -4.295  20.088  -5.404  0.50 19.13 ? 158 GLN B CA  1 
ATOM   3327 C  CA  B GLN B 1 158 ? -4.292  20.245  -5.361  0.50 19.27 ? 158 GLN B CA  1 
ATOM   3328 C  C   A GLN B 1 158 ? -5.284  21.271  -5.271  0.50 19.30 ? 158 GLN B C   1 
ATOM   3329 C  C   B GLN B 1 158 ? -5.243  21.391  -5.170  0.50 19.36 ? 158 GLN B C   1 
ATOM   3330 O  O   A GLN B 1 158 ? -5.104  22.317  -5.898  0.50 21.23 ? 158 GLN B O   1 
ATOM   3331 O  O   B GLN B 1 158 ? -5.054  22.496  -5.710  0.50 20.42 ? 158 GLN B O   1 
ATOM   3332 C  CB  A GLN B 1 158 ? -4.802  19.168  -6.526  0.50 22.78 ? 158 GLN B CB  1 
ATOM   3333 C  CB  B GLN B 1 158 ? -4.942  19.504  -6.495  0.50 22.64 ? 158 GLN B CB  1 
ATOM   3334 C  CG  A GLN B 1 158 ? -3.865  18.590  -7.622  0.50 24.61 ? 158 GLN B CG  1 
ATOM   3335 C  CG  B GLN B 1 158 ? -5.192  18.062  -6.226  0.50 24.33 ? 158 GLN B CG  1 
ATOM   3336 C  CD  A GLN B 1 158 ? -2.598  19.354  -7.924  0.50 22.05 ? 158 GLN B CD  1 
ATOM   3337 C  CD  B GLN B 1 158 ? -4.095  17.268  -6.848  0.50 25.33 ? 158 GLN B CD  1 
ATOM   3338 O  OE1 A GLN B 1 158 ? -1.618  19.137  -7.218  0.50 27.06 ? 158 GLN B OE1 1 
ATOM   3339 O  OE1 B GLN B 1 158 ? -4.343  16.241  -7.435  0.50 21.67 ? 158 GLN B OE1 1 
ATOM   3340 N  NE2 A GLN B 1 158 ? -2.571  20.228  -9.018  0.50 19.29 ? 158 GLN B NE2 1 
ATOM   3341 N  NE2 B GLN B 1 158 ? -2.881  17.767  -6.756  0.50 27.86 ? 158 GLN B NE2 1 
ATOM   3342 N  N   . LEU B 1 159 ? -6.308  21.117  -4.432  1.00 18.13 ? 159 LEU B N   1 
ATOM   3343 C  CA  . LEU B 1 159 ? -7.269  22.194  -4.181  1.00 18.05 ? 159 LEU B CA  1 
ATOM   3344 C  C   . LEU B 1 159 ? -6.696  23.271  -3.327  1.00 20.83 ? 159 LEU B C   1 
ATOM   3345 O  O   . LEU B 1 159 ? -7.185  24.406  -3.418  1.00 21.47 ? 159 LEU B O   1 
ATOM   3346 C  CB  . LEU B 1 159 ? -8.569  21.682  -3.571  1.00 16.98 ? 159 LEU B CB  1 
ATOM   3347 C  CG  . LEU B 1 159 ? -9.269  20.624  -4.412  1.00 18.08 ? 159 LEU B CG  1 
ATOM   3348 C  CD1 . LEU B 1 159 ? -10.471 20.084  -3.659  1.00 18.72 ? 159 LEU B CD1 1 
ATOM   3349 C  CD2 . LEU B 1 159 ? -9.633  21.246  -5.773  1.00 20.71 ? 159 LEU B CD2 1 
ATOM   3350 N  N   . GLN B 1 160 ? -5.696  22.949  -2.491  1.00 21.69 ? 160 GLN B N   1 
ATOM   3351 C  CA  . GLN B 1 160 ? -5.033  24.002  -1.714  1.00 24.88 ? 160 GLN B CA  1 
ATOM   3352 C  C   . GLN B 1 160 ? -4.476  25.065  -2.664  1.00 24.42 ? 160 GLN B C   1 
ATOM   3353 O  O   . GLN B 1 160 ? -4.448  26.249  -2.348  1.00 23.89 ? 160 GLN B O   1 
ATOM   3354 C  CB  . GLN B 1 160 ? -3.941  23.387  -0.798  1.00 29.26 ? 160 GLN B CB  1 
ATOM   3355 C  CG  . GLN B 1 160 ? -3.397  24.390  0.241   1.00 25.89 ? 160 GLN B CG  1 
ATOM   3356 C  CD  . GLN B 1 160 ? -4.130  24.405  1.581   1.00 32.98 ? 160 GLN B CD  1 
ATOM   3357 O  OE1 . GLN B 1 160 ? -5.156  23.795  1.778   1.00 29.63 ? 160 GLN B OE1 1 
ATOM   3358 N  NE2 . GLN B 1 160 ? -3.561  25.120  2.528   1.00 32.14 ? 160 GLN B NE2 1 
ATOM   3359 N  N   . LYS B 1 161 ? -4.020  24.677  -3.875  1.00 25.36 ? 161 LYS B N   1 
ATOM   3360 C  CA  . LYS B 1 161 ? -3.484  25.644  -4.807  1.00 25.56 ? 161 LYS B CA  1 
ATOM   3361 C  C   . LYS B 1 161 ? -4.528  26.716  -5.206  1.00 23.14 ? 161 LYS B C   1 
ATOM   3362 O  O   . LYS B 1 161 ? -4.233  27.911  -5.424  1.00 24.54 ? 161 LYS B O   1 
ATOM   3363 C  CB  . LYS B 1 161 ? -2.954  24.935  -6.029  1.00 28.32 ? 161 LYS B CB  1 
ATOM   3364 C  CG  . LYS B 1 161 ? -2.320  25.825  -7.080  1.00 34.31 ? 161 LYS B CG  1 
ATOM   3365 C  CD  . LYS B 1 161 ? -1.838  24.990  -8.277  1.00 42.78 ? 161 LYS B CD  1 
ATOM   3366 C  CE  . LYS B 1 161 ? -1.486  25.896  -9.447  1.00 36.53 ? 161 LYS B CE  1 
ATOM   3367 N  NZ  . LYS B 1 161 ? -0.250  26.630  -9.086  1.00 37.57 ? 161 LYS B NZ  1 
ATOM   3368 N  N   . ILE B 1 162 ? -5.763  26.219  -5.342  1.00 22.52 ? 162 ILE B N   1 
ATOM   3369 C  CA  . ILE B 1 162 ? -6.879  27.097  -5.585  1.00 19.44 ? 162 ILE B CA  1 
ATOM   3370 C  C   . ILE B 1 162 ? -7.243  27.950  -4.372  1.00 18.78 ? 162 ILE B C   1 
ATOM   3371 O  O   . ILE B 1 162 ? -7.374  29.193  -4.520  1.00 18.47 ? 162 ILE B O   1 
ATOM   3372 C  CB  . ILE B 1 162 ? -8.131  26.305  -6.114  1.00 18.77 ? 162 ILE B CB  1 
ATOM   3373 C  CG1 . ILE B 1 162 ? -7.805  25.732  -7.519  1.00 19.24 ? 162 ILE B CG1 1 
ATOM   3374 C  CG2 . ILE B 1 162 ? -9.275  27.252  -6.362  1.00 18.94 ? 162 ILE B CG2 1 
ATOM   3375 C  CD1 . ILE B 1 162 ? -8.821  24.723  -8.083  1.00 22.48 ? 162 ILE B CD1 1 
ATOM   3376 N  N   . THR B 1 163 ? -7.427  27.308  -3.218  1.00 19.99 ? 163 THR B N   1 
ATOM   3377 C  CA  . THR B 1 163 ? -7.757  28.085  -2.009  1.00 19.68 ? 163 THR B CA  1 
ATOM   3378 C  C   . THR B 1 163 ? -6.724  29.191  -1.715  1.00 22.37 ? 163 THR B C   1 
ATOM   3379 O  O   . THR B 1 163 ? -7.116  30.233  -1.248  1.00 23.53 ? 163 THR B O   1 
ATOM   3380 C  CB  . THR B 1 163 ? -8.149  27.213  -0.815  1.00 19.98 ? 163 THR B CB  1 
ATOM   3381 O  OG1 . THR B 1 163 ? -7.054  26.431  -0.421  1.00 25.55 ? 163 THR B OG1 1 
ATOM   3382 C  CG2 . THR B 1 163 ? -9.287  26.349  -1.141  1.00 18.69 ? 163 THR B CG2 1 
ATOM   3383 N  N   . ASP B 1 164 ? -5.436  28.964  -2.006  1.00 24.49 ? 164 ASP B N   1 
ATOM   3384 C  CA  . ASP B 1 164 ? -4.404  29.977  -1.756  1.00 26.87 ? 164 ASP B CA  1 
ATOM   3385 C  C   . ASP B 1 164 ? -4.553  31.233  -2.582  1.00 24.88 ? 164 ASP B C   1 
ATOM   3386 O  O   . ASP B 1 164 ? -3.994  32.288  -2.224  1.00 30.03 ? 164 ASP B O   1 
ATOM   3387 C  CB  . ASP B 1 164 ? -3.028  29.391  -2.003  1.00 25.04 ? 164 ASP B CB  1 
ATOM   3388 C  CG  . ASP B 1 164 ? -2.592  28.470  -0.913  1.00 28.90 ? 164 ASP B CG  1 
ATOM   3389 O  OD1 . ASP B 1 164 ? -3.166  28.498  0.179   1.00 29.76 ? 164 ASP B OD1 1 
ATOM   3390 O  OD2 . ASP B 1 164 ? -1.682  27.651  -1.142  1.00 30.79 ? 164 ASP B OD2 1 
ATOM   3391 N  N   . THR B 1 165 ? -5.254  31.152  -3.713  1.00 21.85 ? 165 THR B N   1 
ATOM   3392 C  CA  . THR B 1 165 ? -5.455  32.250  -4.588  1.00 20.49 ? 165 THR B CA  1 
ATOM   3393 C  C   . THR B 1 165 ? -6.652  33.075  -4.182  1.00 21.28 ? 165 THR B C   1 
ATOM   3394 O  O   . THR B 1 165 ? -6.844  34.170  -4.697  1.00 23.05 ? 165 THR B O   1 
ATOM   3395 C  CB  . THR B 1 165 ? -5.681  31.912  -6.106  1.00 23.23 ? 165 THR B CB  1 
ATOM   3396 O  OG1 . THR B 1 165 ? -6.976  31.248  -6.297  1.00 24.85 ? 165 THR B OG1 1 
ATOM   3397 C  CG2 . THR B 1 165 ? -4.505  31.077  -6.663  1.00 24.21 ? 165 THR B CG2 1 
ATOM   3398 N  N   . LEU B 1 166 ? -7.521  32.561  -3.314  1.00 19.78 ? 166 LEU B N   1 
ATOM   3399 C  CA  . LEU B 1 166 ? -8.831  33.176  -3.229  1.00 20.34 ? 166 LEU B CA  1 
ATOM   3400 C  C   . LEU B 1 166 ? -8.775  34.577  -2.599  1.00 21.33 ? 166 LEU B C   1 
ATOM   3401 O  O   . LEU B 1 166 ? -9.523  35.428  -3.069  1.00 22.81 ? 166 LEU B O   1 
ATOM   3402 C  CB  . LEU B 1 166 ? -9.853  32.303  -2.481  1.00 20.70 ? 166 LEU B CB  1 
ATOM   3403 C  CG  . LEU B 1 166 ? -10.157 30.938  -3.109  1.00 19.13 ? 166 LEU B CG  1 
ATOM   3404 C  CD1 . LEU B 1 166 ? -11.115 30.141  -2.258  1.00 20.36 ? 166 LEU B CD1 1 
ATOM   3405 C  CD2 . LEU B 1 166 ? -10.750 31.071  -4.516  1.00 20.00 ? 166 LEU B CD2 1 
ATOM   3406 N  N   . ASP B 1 167 ? -7.886  34.792  -1.643  1.00 22.26 ? 167 ASP B N   1 
ATOM   3407 C  CA  . ASP B 1 167 ? -7.798  36.182  -1.095  1.00 28.03 ? 167 ASP B CA  1 
ATOM   3408 C  C   . ASP B 1 167 ? -7.528  37.212  -2.189  1.00 27.59 ? 167 ASP B C   1 
ATOM   3409 O  O   . ASP B 1 167 ? -8.026  38.378  -2.119  1.00 31.50 ? 167 ASP B O   1 
ATOM   3410 C  CB  . ASP B 1 167 ? -6.786  36.286  0.053   1.00 28.88 ? 167 ASP B CB  1 
ATOM   3411 C  CG  . ASP B 1 167 ? -7.250  35.545  1.304   1.00 33.03 ? 167 ASP B CG  1 
ATOM   3412 O  OD1 . ASP B 1 167 ? -8.455  35.193  1.440   1.00 35.66 ? 167 ASP B OD1 1 
ATOM   3413 O  OD2 . ASP B 1 167 ? -6.400  35.326  2.204   1.00 41.46 ? 167 ASP B OD2 1 
ATOM   3414 N  N   . SER B 1 168 ? -6.768  36.846  -3.220  1.00 23.02 ? 168 SER B N   1 
ATOM   3415 C  CA  . SER B 1 168 ? -6.463  37.765  -4.304  1.00 23.75 ? 168 SER B CA  1 
ATOM   3416 C  C   . SER B 1 168 ? -7.594  38.007  -5.304  1.00 26.18 ? 168 SER B C   1 
ATOM   3417 O  O   . SER B 1 168 ? -7.519  38.895  -6.124  1.00 28.45 ? 168 SER B O   1 
ATOM   3418 C  CB  . SER B 1 168 ? -5.211  37.294  -5.075  1.00 26.64 ? 168 SER B CB  1 
ATOM   3419 O  OG  . SER B 1 168 ? -5.480  36.066  -5.756  1.00 31.18 ? 168 SER B OG  1 
ATOM   3420 N  N   . ILE B 1 169 ? -8.633  37.168  -5.278  1.00 21.48 ? 169 ILE B N   1 
ATOM   3421 C  CA  . ILE B 1 169 ? -9.775  37.353  -6.153  1.00 20.29 ? 169 ILE B CA  1 
ATOM   3422 C  C   . ILE B 1 169 ? -11.122 37.427  -5.396  1.00 20.36 ? 169 ILE B C   1 
ATOM   3423 O  O   . ILE B 1 169 ? -12.188 37.068  -5.921  1.00 18.16 ? 169 ILE B O   1 
ATOM   3424 C  CB  . ILE B 1 169 ? -9.836  36.216  -7.260  1.00 17.78 ? 169 ILE B CB  1 
ATOM   3425 C  CG1 . ILE B 1 169 ? -9.990  34.840  -6.613  1.00 19.09 ? 169 ILE B CG1 1 
ATOM   3426 C  CG2 . ILE B 1 169 ? -8.589  36.240  -8.116  1.00 20.01 ? 169 ILE B CG2 1 
ATOM   3427 C  CD1 . ILE B 1 169 ? -10.372 33.777  -7.654  1.00 19.37 ? 169 ILE B CD1 1 
ATOM   3428 N  N   . LYS B 1 170 ? -11.084 38.036  -4.194  1.00 22.20 ? 170 LYS B N   1 
ATOM   3429 C  CA  . LYS B 1 170 ? -12.305 38.129  -3.412  1.00 22.74 ? 170 LYS B CA  1 
ATOM   3430 C  C   . LYS B 1 170 ? -13.443 38.888  -4.133  1.00 18.97 ? 170 LYS B C   1 
ATOM   3431 O  O   . LYS B 1 170 ? -14.606 38.501  -4.062  1.00 21.97 ? 170 LYS B O   1 
ATOM   3432 C  CB  . LYS B 1 170 ? -11.957 38.760  -2.049  1.00 25.82 ? 170 LYS B CB  1 
ATOM   3433 C  CG  . LYS B 1 170 ? -13.139 39.353  -1.346  1.00 34.94 ? 170 LYS B CG  1 
ATOM   3434 C  CD  . LYS B 1 170 ? -12.737 39.874  0.027   1.00 40.83 ? 170 LYS B CD  1 
ATOM   3435 C  CE  . LYS B 1 170 ? -13.958 40.390  0.759   1.00 45.28 ? 170 LYS B CE  1 
ATOM   3436 N  NZ  . LYS B 1 170 ? -13.479 41.188  1.915   1.00 56.59 ? 170 LYS B NZ  1 
ATOM   3437 N  N   . GLU B 1 171 ? -13.144 40.013  -4.790  1.00 22.55 ? 171 GLU B N   1 
ATOM   3438 C  CA  . GLU B 1 171 ? -14.174 40.748  -5.500  1.00 22.53 ? 171 GLU B CA  1 
ATOM   3439 C  C   . GLU B 1 171 ? -14.562 40.267  -6.836  1.00 25.10 ? 171 GLU B C   1 
ATOM   3440 O  O   . GLU B 1 171 ? -13.651 39.833  -7.570  1.00 26.35 ? 171 GLU B O   1 
ATOM   3441 C  CB  . GLU B 1 171 ? -13.763 42.250  -5.650  1.00 26.30 ? 171 GLU B CB  1 
ATOM   3442 C  CG  . GLU B 1 171 ? -13.755 42.975  -4.311  1.00 34.48 ? 171 GLU B CG  1 
ATOM   3443 C  CD  . GLU B 1 171 ? -12.490 42.793  -3.490  1.00 36.88 ? 171 GLU B CD  1 
ATOM   3444 O  OE1 . GLU B 1 171 ? -12.575 43.076  -2.259  1.00 49.18 ? 171 GLU B OE1 1 
ATOM   3445 O  OE2 . GLU B 1 171 ? -11.423 42.351  -4.009  1.00 42.07 ? 171 GLU B OE2 1 
ATOM   3446 N  N   . LYS B 1 172 ? -15.836 40.437  -7.194  1.00 25.57 ? 172 LYS B N   1 
ATOM   3447 C  CA  . LYS B 1 172 ? -16.309 40.039  -8.505  1.00 24.94 ? 172 LYS B CA  1 
ATOM   3448 C  C   . LYS B 1 172 ? -15.465 40.739  -9.551  1.00 28.32 ? 172 LYS B C   1 
ATOM   3449 O  O   . LYS B 1 172 ? -15.149 41.947  -9.408  1.00 27.63 ? 172 LYS B O   1 
ATOM   3450 C  CB  . LYS B 1 172 ? -17.785 40.350  -8.737  1.00 25.81 ? 172 LYS B CB  1 
ATOM   3451 C  CG  . LYS B 1 172 ? -18.362 40.018  -10.099 1.00 26.02 ? 172 LYS B CG  1 
ATOM   3452 C  CD  . LYS B 1 172 ? -19.812 40.470  -10.097 1.00 27.90 ? 172 LYS B CD  1 
ATOM   3453 C  CE  . LYS B 1 172 ? -20.450 40.150  -11.449 1.00 30.04 ? 172 LYS B CE  1 
ATOM   3454 N  NZ  . LYS B 1 172 ? -21.924 40.333  -11.489 1.00 35.82 ? 172 LYS B NZ  1 
ATOM   3455 N  N   . GLY B 1 173 ? -15.006 39.957  -10.528 1.00 22.47 ? 173 GLY B N   1 
ATOM   3456 C  CA  . GLY B 1 173 ? -14.189 40.474  -11.606 1.00 22.29 ? 173 GLY B CA  1 
ATOM   3457 C  C   . GLY B 1 173 ? -12.707 40.366  -11.399 1.00 21.42 ? 173 GLY B C   1 
ATOM   3458 O  O   . GLY B 1 173 ? -11.942 40.610  -12.374 1.00 25.81 ? 173 GLY B O   1 
ATOM   3459 N  N   . LYS B 1 174 ? -12.227 40.067  -10.198 1.00 21.12 ? 174 LYS B N   1 
ATOM   3460 C  CA  . LYS B 1 174 ? -10.790 39.971  -9.974  1.00 22.36 ? 174 LYS B CA  1 
ATOM   3461 C  C   . LYS B 1 174 ? -10.236 38.698  -10.652 1.00 23.16 ? 174 LYS B C   1 
ATOM   3462 O  O   . LYS B 1 174 ? -10.929 37.707  -10.698 1.00 24.46 ? 174 LYS B O   1 
ATOM   3463 C  CB  . LYS B 1 174 ? -10.410 39.943  -8.496  1.00 27.14 ? 174 LYS B CB  1 
ATOM   3464 C  CG  . LYS B 1 174 ? -10.657 41.267  -7.744  1.00 33.94 ? 174 LYS B CG  1 
ATOM   3465 C  CD  . LYS B 1 174 ? -9.681  42.301  -8.205  1.00 34.31 ? 174 LYS B CD  1 
ATOM   3466 C  CE  . LYS B 1 174 ? -9.894  43.613  -7.421  1.00 36.70 ? 174 LYS B CE  1 
ATOM   3467 N  NZ  . LYS B 1 174 ? -9.583  43.475  -5.964  1.00 41.17 ? 174 LYS B NZ  1 
ATOM   3468 N  N   . GLN B 1 175 ? -9.032  38.811  -11.185 1.00 21.59 ? 175 GLN B N   1 
ATOM   3469 C  CA  . GLN B 1 175 ? -8.304  37.671  -11.748 1.00 25.60 ? 175 GLN B CA  1 
ATOM   3470 C  C   . GLN B 1 175 ? -6.860  37.635  -11.352 1.00 27.73 ? 175 GLN B C   1 
ATOM   3471 O  O   . GLN B 1 175 ? -6.245  38.680  -11.000 1.00 24.11 ? 175 GLN B O   1 
ATOM   3472 C  CB  . GLN B 1 175 ? -8.450  37.586  -13.272 1.00 29.02 ? 175 GLN B CB  1 
ATOM   3473 C  CG  . GLN B 1 175 ? -7.700  38.570  -14.163 1.00 38.85 ? 175 GLN B CG  1 
ATOM   3474 C  CD  . GLN B 1 175 ? -8.002  38.266  -15.654 1.00 44.87 ? 175 GLN B CD  1 
ATOM   3475 O  OE1 . GLN B 1 175 ? -7.085  38.226  -16.516 1.00 41.58 ? 175 GLN B OE1 1 
ATOM   3476 N  NE2 . GLN B 1 175 ? -9.288  37.968  -15.945 1.00 45.03 ? 175 GLN B NE2 1 
ATOM   3477 N  N   . THR B 1 176 ? -6.270  36.439  -11.451 1.00 22.70 ? 176 THR B N   1 
ATOM   3478 C  CA  . THR B 1 176 ? -4.875  36.300  -11.174 1.00 24.61 ? 176 THR B CA  1 
ATOM   3479 C  C   . THR B 1 176 ? -4.298  35.094  -11.903 1.00 23.96 ? 176 THR B C   1 
ATOM   3480 O  O   . THR B 1 176 ? -5.074  34.237  -12.364 1.00 22.14 ? 176 THR B O   1 
ATOM   3481 C  CB  . THR B 1 176 ? -4.586  36.232  -9.691  1.00 26.90 ? 176 THR B CB  1 
ATOM   3482 O  OG1 . THR B 1 176 ? -3.222  36.617  -9.490  1.00 29.94 ? 176 THR B OG1 1 
ATOM   3483 C  CG2 . THR B 1 176 ? -4.785  34.896  -9.120  1.00 27.59 ? 176 THR B CG2 1 
ATOM   3484 N  N   . ARG B 1 177 ? -2.979  35.051  -12.056 1.00 22.23 ? 177 ARG B N   1 
ATOM   3485 C  CA  . ARG B 1 177 ? -2.429  34.021  -12.887 1.00 21.40 ? 177 ARG B CA  1 
ATOM   3486 C  C   . ARG B 1 177 ? -2.435  32.758  -12.075 1.00 21.10 ? 177 ARG B C   1 
ATOM   3487 O  O   . ARG B 1 177 ? -2.254  32.771  -10.885 1.00 21.85 ? 177 ARG B O   1 
ATOM   3488 C  CB  . ARG B 1 177 ? -1.011  34.373  -13.319 1.00 24.47 ? 177 ARG B CB  1 
ATOM   3489 C  CG  . ARG B 1 177 ? -1.204  35.598  -14.194 1.00 26.76 ? 177 ARG B CG  1 
ATOM   3490 C  CD  . ARG B 1 177 ? 0.123   36.094  -14.702 1.00 33.47 ? 177 ARG B CD  1 
ATOM   3491 N  NE  . ARG B 1 177 ? 0.813   35.078  -15.494 1.00 33.48 ? 177 ARG B NE  1 
ATOM   3492 C  CZ  . ARG B 1 177 ? 1.929   35.325  -16.158 1.00 35.21 ? 177 ARG B CZ  1 
ATOM   3493 N  NH1 . ARG B 1 177 ? 2.432   36.562  -16.170 1.00 23.22 ? 177 ARG B NH1 1 
ATOM   3494 N  NH2 . ARG B 1 177 ? 2.502   34.322  -16.811 1.00 36.10 ? 177 ARG B NH2 1 
ATOM   3495 N  N   . PHE B 1 178 ? -2.593  31.643  -12.768 1.00 21.63 ? 178 PHE B N   1 
ATOM   3496 C  CA  . PHE B 1 178 ? -2.713  30.367  -12.137 1.00 18.38 ? 178 PHE B CA  1 
ATOM   3497 C  C   . PHE B 1 178 ? -2.377  29.280  -13.194 1.00 19.01 ? 178 PHE B C   1 
ATOM   3498 O  O   . PHE B 1 178 ? -3.108  29.132  -14.215 1.00 19.66 ? 178 PHE B O   1 
ATOM   3499 C  CB  . PHE B 1 178 ? -4.206  30.129  -11.770 1.00 23.00 ? 178 PHE B CB  1 
ATOM   3500 C  CG  . PHE B 1 178 ? -4.473  28.868  -11.049 1.00 22.45 ? 178 PHE B CG  1 
ATOM   3501 C  CD1 . PHE B 1 178 ? -4.297  28.762  -9.686  1.00 21.61 ? 178 PHE B CD1 1 
ATOM   3502 C  CD2 . PHE B 1 178 ? -5.016  27.806  -11.731 1.00 21.58 ? 178 PHE B CD2 1 
ATOM   3503 C  CE1 . PHE B 1 178 ? -4.531  27.585  -9.016  1.00 26.65 ? 178 PHE B CE1 1 
ATOM   3504 C  CE2 . PHE B 1 178 ? -5.247  26.618  -11.050 1.00 22.14 ? 178 PHE B CE2 1 
ATOM   3505 C  CZ  . PHE B 1 178 ? -5.034  26.511  -9.716  1.00 24.25 ? 178 PHE B CZ  1 
ATOM   3506 N  N   . THR B 1 179 ? -1.314  28.535  -12.945 1.00 22.07 ? 179 THR B N   1 
ATOM   3507 C  CA  . THR B 1 179 ? -0.900  27.497  -13.940 1.00 24.41 ? 179 THR B CA  1 
ATOM   3508 C  C   . THR B 1 179 ? -0.304  26.300  -13.208 1.00 25.58 ? 179 THR B C   1 
ATOM   3509 O  O   . THR B 1 179 ? -0.290  26.262  -11.988 1.00 25.30 ? 179 THR B O   1 
ATOM   3510 C  CB  . THR B 1 179 ? -0.056  28.079  -15.100 1.00 25.69 ? 179 THR B CB  1 
ATOM   3511 O  OG1 . THR B 1 179 ? 0.035   27.110  -16.187 1.00 25.76 ? 179 THR B OG1 1 
ATOM   3512 C  CG2 . THR B 1 179 ? 1.387   28.456  -14.622 1.00 28.52 ? 179 THR B CG2 1 
ATOM   3513 N  N   A ASN B 1 180 ? 0.162   25.346  -14.016 0.50 26.09 ? 180 ASN B N   1 
ATOM   3514 N  N   B ASN B 1 180 ? 0.185   25.295  -13.927 0.50 24.74 ? 180 ASN B N   1 
ATOM   3515 C  CA  A ASN B 1 180 ? 0.673   24.061  -13.543 0.50 25.42 ? 180 ASN B CA  1 
ATOM   3516 C  CA  B ASN B 1 180 ? 0.641   24.038  -13.275 0.50 22.91 ? 180 ASN B CA  1 
ATOM   3517 C  C   A ASN B 1 180 ? -0.328  23.421  -12.538 0.50 26.12 ? 180 ASN B C   1 
ATOM   3518 C  C   B ASN B 1 180 ? -0.421  23.396  -12.404 0.50 24.17 ? 180 ASN B C   1 
ATOM   3519 O  O   A ASN B 1 180 ? 0.005   23.183  -11.391 0.50 28.94 ? 180 ASN B O   1 
ATOM   3520 O  O   B ASN B 1 180 ? -0.224  23.084  -11.231 0.50 25.51 ? 180 ASN B O   1 
ATOM   3521 C  CB  A ASN B 1 180 ? 2.148   24.194  -13.054 0.50 28.73 ? 180 ASN B CB  1 
ATOM   3522 C  CB  B ASN B 1 180 ? 1.934   24.196  -12.478 0.50 25.46 ? 180 ASN B CB  1 
ATOM   3523 C  CG  A ASN B 1 180 ? 3.083   24.849  -14.096 0.50 30.74 ? 180 ASN B CG  1 
ATOM   3524 C  CG  B ASN B 1 180 ? 2.674   22.880  -12.343 0.50 24.15 ? 180 ASN B CG  1 
ATOM   3525 O  OD1 A ASN B 1 180 ? 3.059   24.530  -15.290 0.50 30.50 ? 180 ASN B OD1 1 
ATOM   3526 O  OD1 B ASN B 1 180 ? 2.396   21.916  -13.080 0.50 25.99 ? 180 ASN B OD1 1 
ATOM   3527 N  ND2 A ASN B 1 180 ? 3.919   25.791  -13.624 0.50 30.91 ? 180 ASN B ND2 1 
ATOM   3528 N  ND2 B ASN B 1 180 ? 3.611   22.820  -11.406 0.50 26.70 ? 180 ASN B ND2 1 
ATOM   3529 N  N   . PHE B 1 181 ? -1.572  23.186  -13.013 1.00 20.83 ? 181 PHE B N   1 
ATOM   3530 C  CA  . PHE B 1 181 ? -2.681  22.575  -12.288 1.00 21.19 ? 181 PHE B CA  1 
ATOM   3531 C  C   . PHE B 1 181 ? -2.932  21.170  -12.847 1.00 19.56 ? 181 PHE B C   1 
ATOM   3532 O  O   . PHE B 1 181 ? -3.284  21.058  -14.029 1.00 21.55 ? 181 PHE B O   1 
ATOM   3533 C  CB  . PHE B 1 181 ? -3.906  23.485  -12.473 1.00 21.36 ? 181 PHE B CB  1 
ATOM   3534 C  CG  . PHE B 1 181 ? -5.183  22.961  -11.848 1.00 22.82 ? 181 PHE B CG  1 
ATOM   3535 C  CD1 . PHE B 1 181 ? -5.242  22.588  -10.527 1.00 24.35 ? 181 PHE B CD1 1 
ATOM   3536 C  CD2 . PHE B 1 181 ? -6.430  23.001  -12.597 1.00 23.62 ? 181 PHE B CD2 1 
ATOM   3537 C  CE1 . PHE B 1 181 ? -6.466  22.161  -9.957  1.00 23.66 ? 181 PHE B CE1 1 
ATOM   3538 C  CE2 . PHE B 1 181 ? -7.640  22.636  -12.029 1.00 24.91 ? 181 PHE B CE2 1 
ATOM   3539 C  CZ  . PHE B 1 181 ? -7.659  22.196  -10.698 1.00 24.24 ? 181 PHE B CZ  1 
ATOM   3540 N  N   . ASP B 1 182 ? -2.708  20.136  -12.007 1.00 18.47 ? 182 ASP B N   1 
ATOM   3541 C  CA  . ASP B 1 182 ? -2.679  18.763  -12.509 1.00 19.51 ? 182 ASP B CA  1 
ATOM   3542 C  C   . ASP B 1 182 ? -4.090  18.234  -12.305 1.00 16.60 ? 182 ASP B C   1 
ATOM   3543 O  O   . ASP B 1 182 ? -4.448  17.519  -11.362 1.00 19.32 ? 182 ASP B O   1 
ATOM   3544 C  CB  . ASP B 1 182 ? -1.664  17.962  -11.687 1.00 19.28 ? 182 ASP B CB  1 
ATOM   3545 C  CG  . ASP B 1 182 ? -1.411  16.578  -12.278 1.00 22.28 ? 182 ASP B CG  1 
ATOM   3546 O  OD1 . ASP B 1 182 ? -2.197  16.188  -13.146 1.00 20.82 ? 182 ASP B OD1 1 
ATOM   3547 O  OD2 . ASP B 1 182 ? -0.454  15.866  -11.874 1.00 20.80 ? 182 ASP B OD2 1 
ATOM   3548 N  N   . LEU B 1 183 ? -4.974  18.661  -13.232 1.00 17.03 ? 183 LEU B N   1 
ATOM   3549 C  CA  . LEU B 1 183 ? -6.327  18.342  -13.155 1.00 16.35 ? 183 LEU B CA  1 
ATOM   3550 C  C   . LEU B 1 183 ? -6.547  16.826  -13.237 1.00 14.65 ? 183 LEU B C   1 
ATOM   3551 O  O   . LEU B 1 183 ? -7.484  16.250  -12.638 1.00 16.84 ? 183 LEU B O   1 
ATOM   3552 C  CB  . LEU B 1 183 ? -7.087  19.139  -14.286 1.00 16.80 ? 183 LEU B CB  1 
ATOM   3553 C  CG  . LEU B 1 183 ? -8.573  18.848  -14.394 1.00 16.19 ? 183 LEU B CG  1 
ATOM   3554 C  CD1 . LEU B 1 183 ? -9.338  19.214  -13.119 1.00 18.28 ? 183 LEU B CD1 1 
ATOM   3555 C  CD2 . LEU B 1 183 ? -9.117  19.642  -15.628 1.00 15.37 ? 183 LEU B CD2 1 
ATOM   3556 N  N   . LEU B 1 184 ? -5.678  16.149  -14.062 1.00 14.63 ? 184 LEU B N   1 
ATOM   3557 C  CA  . LEU B 1 184 ? -5.802  14.740  -14.186 1.00 17.22 ? 184 LEU B CA  1 
ATOM   3558 C  C   . LEU B 1 184 ? -5.673  14.000  -12.842 1.00 14.41 ? 184 LEU B C   1 
ATOM   3559 O  O   . LEU B 1 184 ? -6.437  13.060  -12.525 1.00 16.12 ? 184 LEU B O   1 
ATOM   3560 C  CB  . LEU B 1 184 ? -4.800  14.116  -15.262 1.00 15.85 ? 184 LEU B CB  1 
ATOM   3561 C  CG  . LEU B 1 184 ? -5.065  12.631  -15.635 1.00 16.13 ? 184 LEU B CG  1 
ATOM   3562 C  CD1 . LEU B 1 184 ? -6.336  12.297  -16.345 1.00 19.64 ? 184 LEU B CD1 1 
ATOM   3563 C  CD2 . LEU B 1 184 ? -3.885  12.126  -16.499 1.00 20.32 ? 184 LEU B CD2 1 
ATOM   3564 N  N   A SER B 1 185 ? -4.688  14.437  -12.053 0.50 16.94 ? 185 SER B N   1 
ATOM   3565 N  N   B SER B 1 185 ? -4.671  14.409  -12.059 0.50 17.00 ? 185 SER B N   1 
ATOM   3566 C  CA  A SER B 1 185 ? -4.451  13.802  -10.747 0.50 16.74 ? 185 SER B CA  1 
ATOM   3567 C  CA  B SER B 1 185 ? -4.435  13.747  -10.765 0.50 16.79 ? 185 SER B CA  1 
ATOM   3568 C  C   A SER B 1 185 ? -5.519  14.133  -9.718  0.50 16.06 ? 185 SER B C   1 
ATOM   3569 C  C   B SER B 1 185 ? -5.465  14.173  -9.696  0.50 16.38 ? 185 SER B C   1 
ATOM   3570 O  O   A SER B 1 185 ? -5.713  13.418  -8.737  0.50 17.81 ? 185 SER B O   1 
ATOM   3571 O  O   B SER B 1 185 ? -5.562  13.571  -8.639  0.50 19.83 ? 185 SER B O   1 
ATOM   3572 C  CB  A SER B 1 185 ? -3.101  14.271  -10.189 0.50 18.06 ? 185 SER B CB  1 
ATOM   3573 C  CB  B SER B 1 185 ? -3.034  14.115  -10.229 0.50 18.31 ? 185 SER B CB  1 
ATOM   3574 O  OG  A SER B 1 185 ? -2.114  13.801  -11.061 0.50 19.09 ? 185 SER B OG  1 
ATOM   3575 O  OG  B SER B 1 185 ? -3.041  15.478  -9.866  0.50 19.14 ? 185 SER B OG  1 
ATOM   3576 N  N   . LEU B 1 186 ? -6.256  15.194  -9.978  1.00 17.05 ? 186 LEU B N   1 
ATOM   3577 C  CA  . LEU B 1 186 ? -7.342  15.564  -9.062  1.00 14.03 ? 186 LEU B CA  1 
ATOM   3578 C  C   . LEU B 1 186 ? -8.527  14.607  -9.133  1.00 14.03 ? 186 LEU B C   1 
ATOM   3579 O  O   . LEU B 1 186 ? -9.307  14.430  -8.161  1.00 14.78 ? 186 LEU B O   1 
ATOM   3580 C  CB  . LEU B 1 186 ? -7.737  17.020  -9.389  1.00 13.41 ? 186 LEU B CB  1 
ATOM   3581 C  CG  . LEU B 1 186 ? -8.857  17.626  -8.605  1.00 16.92 ? 186 LEU B CG  1 
ATOM   3582 C  CD1 . LEU B 1 186 ? -8.278  18.031  -7.243  1.00 19.14 ? 186 LEU B CD1 1 
ATOM   3583 C  CD2 . LEU B 1 186 ? -9.319  18.966  -9.192  1.00 17.23 ? 186 LEU B CD2 1 
ATOM   3584 N  N   . LEU B 1 187 ? -8.739  13.954  -10.292 1.00 13.90 ? 187 LEU B N   1 
ATOM   3585 C  CA  . LEU B 1 187 ? -9.871  13.064  -10.432 1.00 13.27 ? 187 LEU B CA  1 
ATOM   3586 C  C   . LEU B 1 187 ? -9.827  11.817  -9.517  1.00 14.21 ? 187 LEU B C   1 
ATOM   3587 O  O   . LEU B 1 187 ? -8.729  11.422  -9.048  1.00 15.53 ? 187 LEU B O   1 
ATOM   3588 C  CB  . LEU B 1 187 ? -9.954  12.574  -11.911 1.00 12.52 ? 187 LEU B CB  1 
ATOM   3589 C  CG  . LEU B 1 187 ? -10.018 13.747  -12.906 1.00 12.29 ? 187 LEU B CG  1 
ATOM   3590 C  CD1 . LEU B 1 187 ? -10.150 13.097  -14.293 1.00 14.18 ? 187 LEU B CD1 1 
ATOM   3591 C  CD2 . LEU B 1 187 ? -11.240 14.705  -12.628 1.00 14.96 ? 187 LEU B CD2 1 
ATOM   3592 N  N   . PRO B 1 188 ? -10.989 11.259  -9.122  1.00 14.03 ? 188 PRO B N   1 
ATOM   3593 C  CA  . PRO B 1 188 ? -10.995 10.135  -8.155  1.00 15.57 ? 188 PRO B CA  1 
ATOM   3594 C  C   . PRO B 1 188 ? -10.383 8.881   -8.768  1.00 16.83 ? 188 PRO B C   1 
ATOM   3595 O  O   . PRO B 1 188 ? -10.201 8.822   -10.001 1.00 15.88 ? 188 PRO B O   1 
ATOM   3596 C  CB  . PRO B 1 188 ? -12.483 9.869   -7.925  1.00 16.53 ? 188 PRO B CB  1 
ATOM   3597 C  CG  . PRO B 1 188 ? -13.214 10.543  -9.127  1.00 16.05 ? 188 PRO B CG  1 
ATOM   3598 C  CD  . PRO B 1 188 ? -12.343 11.687  -9.516  1.00 14.26 ? 188 PRO B CD  1 
ATOM   3599 N  N   . PRO B 1 189 ? -10.091 7.884   -7.945  1.00 14.80 ? 189 PRO B N   1 
ATOM   3600 C  CA  . PRO B 1 189 ? -9.491  6.671   -8.480  1.00 17.62 ? 189 PRO B CA  1 
ATOM   3601 C  C   . PRO B 1 189 ? -10.416 6.002   -9.581  1.00 16.71 ? 189 PRO B C   1 
ATOM   3602 O  O   . PRO B 1 189 ? -9.902  5.564   -10.667 1.00 17.27 ? 189 PRO B O   1 
ATOM   3603 C  CB  . PRO B 1 189 ? -9.450  5.810   -7.188  1.00 17.54 ? 189 PRO B CB  1 
ATOM   3604 C  CG  . PRO B 1 189 ? -9.165  6.800   -6.097  1.00 18.65 ? 189 PRO B CG  1 
ATOM   3605 C  CD  . PRO B 1 189 ? -10.098 7.919   -6.447  1.00 18.38 ? 189 PRO B CD  1 
ATOM   3606 N  N   . SER B 1 190 ? -11.747 5.913   -9.339  1.00 15.99 ? 190 SER B N   1 
ATOM   3607 C  CA  . SER B 1 190 ? -12.629 5.299   -10.326 1.00 15.61 ? 190 SER B CA  1 
ATOM   3608 C  C   . SER B 1 190 ? -13.240 6.359   -11.234 1.00 19.57 ? 190 SER B C   1 
ATOM   3609 O  O   . SER B 1 190 ? -13.676 7.429   -10.755 1.00 16.14 ? 190 SER B O   1 
ATOM   3610 C  CB  . SER B 1 190 ? -13.775 4.556   -9.578  1.00 17.42 ? 190 SER B CB  1 
ATOM   3611 O  OG  . SER B 1 190 ? -14.703 3.998   -10.533 1.00 18.65 ? 190 SER B OG  1 
ATOM   3612 N  N   . TRP B 1 191 ? -13.286 6.082   -12.537 1.00 16.64 ? 191 TRP B N   1 
ATOM   3613 C  CA  . TRP B 1 191 ? -14.003 6.988   -13.463 1.00 16.24 ? 191 TRP B CA  1 
ATOM   3614 C  C   . TRP B 1 191 ? -15.271 6.364   -13.996 1.00 15.82 ? 191 TRP B C   1 
ATOM   3615 O  O   . TRP B 1 191 ? -15.705 6.700   -15.106 1.00 18.61 ? 191 TRP B O   1 
ATOM   3616 C  CB  . TRP B 1 191 ? -13.101 7.341   -14.594 1.00 14.76 ? 191 TRP B CB  1 
ATOM   3617 C  CG  . TRP B 1 191 ? -11.868 8.086   -14.135 1.00 14.71 ? 191 TRP B CG  1 
ATOM   3618 C  CD1 . TRP B 1 191 ? -11.606 8.704   -12.900 1.00 16.19 ? 191 TRP B CD1 1 
ATOM   3619 C  CD2 . TRP B 1 191 ? -10.680 8.334   -14.943 1.00 15.51 ? 191 TRP B CD2 1 
ATOM   3620 N  NE1 . TRP B 1 191 ? -10.342 9.263   -12.881 1.00 15.40 ? 191 TRP B NE1 1 
ATOM   3621 C  CE2 . TRP B 1 191 ? -9.756  9.101   -14.146 1.00 15.10 ? 191 TRP B CE2 1 
ATOM   3622 C  CE3 . TRP B 1 191 ? -10.298 7.972   -16.239 1.00 17.66 ? 191 TRP B CE3 1 
ATOM   3623 C  CZ2 . TRP B 1 191 ? -8.491  9.457   -14.622 1.00 18.47 ? 191 TRP B CZ2 1 
ATOM   3624 C  CZ3 . TRP B 1 191 ? -9.042  8.350   -16.712 1.00 20.13 ? 191 TRP B CZ3 1 
ATOM   3625 C  CH2 . TRP B 1 191 ? -8.153  9.076   -15.932 1.00 18.64 ? 191 TRP B CH2 1 
ATOM   3626 N  N   . ASP B 1 192 ? -15.894 5.528   -13.200 1.00 16.45 ? 192 ASP B N   1 
ATOM   3627 C  CA  . ASP B 1 192 ? -17.195 5.013   -13.605 1.00 17.85 ? 192 ASP B CA  1 
ATOM   3628 C  C   . ASP B 1 192 ? -18.199 6.227   -13.467 1.00 16.17 ? 192 ASP B C   1 
ATOM   3629 O  O   . ASP B 1 192 ? -18.064 7.095   -12.565 1.00 15.65 ? 192 ASP B O   1 
ATOM   3630 C  CB  . ASP B 1 192 ? -17.588 3.879   -12.726 1.00 21.58 ? 192 ASP B CB  1 
ATOM   3631 C  CG  . ASP B 1 192 ? -16.726 2.634   -12.985 1.00 18.16 ? 192 ASP B CG  1 
ATOM   3632 O  OD1 . ASP B 1 192 ? -16.001 2.584   -14.002 1.00 23.08 ? 192 ASP B OD1 1 
ATOM   3633 O  OD2 . ASP B 1 192 ? -16.790 1.705   -12.170 1.00 25.47 ? 192 ASP B OD2 1 
ATOM   3634 N  N   . TYR B 1 193 ? -19.155 6.309   -14.411 1.00 14.38 ? 193 TYR B N   1 
ATOM   3635 C  CA  . TYR B 1 193 ? -19.944 7.526   -14.502 1.00 14.57 ? 193 TYR B CA  1 
ATOM   3636 C  C   . TYR B 1 193 ? -21.356 7.247   -14.951 1.00 15.95 ? 193 TYR B C   1 
ATOM   3637 O  O   . TYR B 1 193 ? -21.635 6.149   -15.488 1.00 14.46 ? 193 TYR B O   1 
ATOM   3638 C  CB  . TYR B 1 193 ? -19.329 8.541   -15.565 1.00 13.88 ? 193 TYR B CB  1 
ATOM   3639 C  CG  . TYR B 1 193 ? -19.223 7.951   -17.019 1.00 12.61 ? 193 TYR B CG  1 
ATOM   3640 C  CD1 . TYR B 1 193 ? -20.348 8.057   -17.886 1.00 13.72 ? 193 TYR B CD1 1 
ATOM   3641 C  CD2 . TYR B 1 193 ? -18.095 7.230   -17.408 1.00 14.98 ? 193 TYR B CD2 1 
ATOM   3642 C  CE1 . TYR B 1 193 ? -20.288 7.499   -19.159 1.00 15.22 ? 193 TYR B CE1 1 
ATOM   3643 C  CE2 . TYR B 1 193 ? -18.029 6.685   -18.667 1.00 13.35 ? 193 TYR B CE2 1 
ATOM   3644 C  CZ  . TYR B 1 193 ? -19.119 6.828   -19.539 1.00 16.08 ? 193 TYR B CZ  1 
ATOM   3645 O  OH  . TYR B 1 193 ? -19.140 6.271   -20.836 1.00 16.80 ? 193 TYR B OH  1 
ATOM   3646 N  N   . TRP B 1 194 ? -22.225 8.229   -14.757 1.00 13.61 ? 194 TRP B N   1 
ATOM   3647 C  CA  . TRP B 1 194 ? -23.532 8.325   -15.360 1.00 13.12 ? 194 TRP B CA  1 
ATOM   3648 C  C   . TRP B 1 194 ? -23.544 9.414   -16.404 1.00 15.28 ? 194 TRP B C   1 
ATOM   3649 O  O   . TRP B 1 194 ? -22.745 10.402  -16.326 1.00 13.60 ? 194 TRP B O   1 
ATOM   3650 C  CB  . TRP B 1 194 ? -24.569 8.706   -14.293 1.00 14.37 ? 194 TRP B CB  1 
ATOM   3651 C  CG  . TRP B 1 194 ? -24.645 7.693   -13.160 1.00 15.45 ? 194 TRP B CG  1 
ATOM   3652 C  CD1 . TRP B 1 194 ? -25.222 6.426   -13.176 1.00 15.81 ? 194 TRP B CD1 1 
ATOM   3653 C  CD2 . TRP B 1 194 ? -24.189 7.883   -11.810 1.00 14.48 ? 194 TRP B CD2 1 
ATOM   3654 N  NE1 . TRP B 1 194 ? -25.157 5.863   -11.941 1.00 15.41 ? 194 TRP B NE1 1 
ATOM   3655 C  CE2 . TRP B 1 194 ? -24.539 6.687   -11.076 1.00 15.57 ? 194 TRP B CE2 1 
ATOM   3656 C  CE3 . TRP B 1 194 ? -23.538 8.927   -11.138 1.00 13.70 ? 194 TRP B CE3 1 
ATOM   3657 C  CZ2 . TRP B 1 194 ? -24.217 6.523   -9.704  1.00 16.19 ? 194 TRP B CZ2 1 
ATOM   3658 C  CZ3 . TRP B 1 194 ? -23.276 8.769   -9.762  1.00 15.07 ? 194 TRP B CZ3 1 
ATOM   3659 C  CH2 . TRP B 1 194 ? -23.567 7.586   -9.080  1.00 15.49 ? 194 TRP B CH2 1 
ATOM   3660 N  N   . THR B 1 195 ? -24.424 9.256   -17.414 1.00 13.25 ? 195 THR B N   1 
ATOM   3661 C  CA  . THR B 1 195 ? -24.480 10.255  -18.434 1.00 13.09 ? 195 THR B CA  1 
ATOM   3662 C  C   . THR B 1 195 ? -25.883 10.509  -18.934 1.00 13.34 ? 195 THR B C   1 
ATOM   3663 O  O   . THR B 1 195 ? -26.717 9.575   -18.989 1.00 14.29 ? 195 THR B O   1 
ATOM   3664 C  CB  . THR B 1 195 ? -23.526 9.892   -19.640 1.00 12.61 ? 195 THR B CB  1 
ATOM   3665 O  OG1 . THR B 1 195 ? -23.563 10.901  -20.639 1.00 13.59 ? 195 THR B OG1 1 
ATOM   3666 C  CG2 . THR B 1 195 ? -24.019 8.534   -20.344 1.00 13.39 ? 195 THR B CG2 1 
ATOM   3667 N  N   . TYR B 1 196 ? -26.157 11.732  -19.283 1.00 13.45 ? 196 TYR B N   1 
ATOM   3668 C  CA  . TYR B 1 196 ? -27.497 12.119  -19.802 1.00 13.88 ? 196 TYR B CA  1 
ATOM   3669 C  C   . TYR B 1 196 ? -27.359 13.424  -20.560 1.00 13.44 ? 196 TYR B C   1 
ATOM   3670 O  O   . TYR B 1 196 ? -26.425 14.215  -20.352 1.00 13.50 ? 196 TYR B O   1 
ATOM   3671 C  CB  . TYR B 1 196 ? -28.571 12.227  -18.700 1.00 13.61 ? 196 TYR B CB  1 
ATOM   3672 C  CG  . TYR B 1 196 ? -28.359 13.456  -17.828 1.00 13.40 ? 196 TYR B CG  1 
ATOM   3673 C  CD1 . TYR B 1 196 ? -27.377 13.480  -16.840 1.00 12.93 ? 196 TYR B CD1 1 
ATOM   3674 C  CD2 . TYR B 1 196 ? -29.118 14.603  -18.018 1.00 14.67 ? 196 TYR B CD2 1 
ATOM   3675 C  CE1 . TYR B 1 196 ? -27.175 14.606  -16.057 1.00 13.36 ? 196 TYR B CE1 1 
ATOM   3676 C  CE2 . TYR B 1 196 ? -28.924 15.730  -17.241 1.00 14.15 ? 196 TYR B CE2 1 
ATOM   3677 C  CZ  . TYR B 1 196 ? -27.954 15.729  -16.263 1.00 12.53 ? 196 TYR B CZ  1 
ATOM   3678 O  OH  . TYR B 1 196 ? -27.775 16.861  -15.498 1.00 13.35 ? 196 TYR B OH  1 
ATOM   3679 N  N   . PRO B 1 197 ? -28.293 13.740  -21.496 1.00 13.83 ? 197 PRO B N   1 
ATOM   3680 C  CA  . PRO B 1 197 ? -28.268 14.978  -22.190 1.00 13.23 ? 197 PRO B CA  1 
ATOM   3681 C  C   . PRO B 1 197 ? -28.906 16.068  -21.324 1.00 12.50 ? 197 PRO B C   1 
ATOM   3682 O  O   . PRO B 1 197 ? -30.022 15.853  -20.816 1.00 14.04 ? 197 PRO B O   1 
ATOM   3683 C  CB  . PRO B 1 197 ? -29.142 14.695  -23.476 1.00 13.70 ? 197 PRO B CB  1 
ATOM   3684 C  CG  . PRO B 1 197 ? -30.121 13.595  -22.928 1.00 13.94 ? 197 PRO B CG  1 
ATOM   3685 C  CD  . PRO B 1 197 ? -29.292 12.742  -21.952 1.00 14.60 ? 197 PRO B CD  1 
ATOM   3686 N  N   . GLY B 1 198 ? -28.257 17.211  -21.260 1.00 12.81 ? 198 GLY B N   1 
ATOM   3687 C  CA  . GLY B 1 198 ? -28.779 18.315  -20.468 1.00 13.05 ? 198 GLY B CA  1 
ATOM   3688 C  C   . GLY B 1 198 ? -28.285 19.639  -20.833 1.00 13.83 ? 198 GLY B C   1 
ATOM   3689 O  O   . GLY B 1 198 ? -28.128 19.986  -22.041 1.00 13.46 ? 198 GLY B O   1 
ATOM   3690 N  N   . SER B 1 199 ? -28.128 20.499  -19.805 1.00 13.08 ? 199 SER B N   1 
ATOM   3691 C  CA  . SER B 1 199 ? -27.930 21.907  -20.040 1.00 13.29 ? 199 SER B CA  1 
ATOM   3692 C  C   . SER B 1 199 ? -26.842 22.533  -19.214 1.00 12.56 ? 199 SER B C   1 
ATOM   3693 O  O   . SER B 1 199 ? -26.355 21.914  -18.200 1.00 13.10 ? 199 SER B O   1 
ATOM   3694 C  CB  . SER B 1 199 ? -29.239 22.663  -19.719 1.00 13.85 ? 199 SER B CB  1 
ATOM   3695 O  OG  . SER B 1 199 ? -29.446 22.754  -18.315 1.00 13.83 ? 199 SER B OG  1 
ATOM   3696 N  N   . LEU B 1 200 ? -26.476 23.761  -19.524 1.00 13.44 ? 200 LEU B N   1 
ATOM   3697 C  CA  . LEU B 1 200 ? -25.764 24.564  -18.542 1.00 13.00 ? 200 LEU B CA  1 
ATOM   3698 C  C   . LEU B 1 200 ? -26.643 24.724  -17.286 1.00 14.90 ? 200 LEU B C   1 
ATOM   3699 O  O   . LEU B 1 200 ? -27.836 24.779  -17.375 1.00 15.08 ? 200 LEU B O   1 
ATOM   3700 C  CB  . LEU B 1 200 ? -25.555 25.978  -19.034 1.00 13.67 ? 200 LEU B CB  1 
ATOM   3701 C  CG  . LEU B 1 200 ? -24.727 26.117  -20.350 1.00 17.69 ? 200 LEU B CG  1 
ATOM   3702 C  CD1 . LEU B 1 200 ? -24.525 27.580  -20.627 1.00 18.85 ? 200 LEU B CD1 1 
ATOM   3703 C  CD2 . LEU B 1 200 ? -23.409 25.397  -20.332 1.00 18.13 ? 200 LEU B CD2 1 
ATOM   3704 N  N   . THR B 1 201 ? -25.981 24.791  -16.118 1.00 14.05 ? 201 THR B N   1 
ATOM   3705 C  CA  . THR B 1 201 ? -26.751 24.922  -14.854 1.00 14.14 ? 201 THR B CA  1 
ATOM   3706 C  C   . THR B 1 201 ? -26.739 26.364  -14.415 1.00 14.75 ? 201 THR B C   1 
ATOM   3707 O  O   . THR B 1 201 ? -27.197 26.655  -13.293 1.00 13.54 ? 201 THR B O   1 
ATOM   3708 C  CB  . THR B 1 201 ? -26.208 23.993  -13.697 1.00 13.06 ? 201 THR B CB  1 
ATOM   3709 O  OG1 . THR B 1 201 ? -24.937 24.447  -13.255 1.00 12.66 ? 201 THR B OG1 1 
ATOM   3710 C  CG2 . THR B 1 201 ? -26.170 22.480  -14.200 1.00 14.12 ? 201 THR B CG2 1 
ATOM   3711 N  N   . VAL B 1 202 ? -26.285 27.275  -15.263 1.00 14.15 ? 202 VAL B N   1 
ATOM   3712 C  CA  . VAL B 1 202 ? -26.348 28.740  -15.036 1.00 15.07 ? 202 VAL B CA  1 
ATOM   3713 C  C   . VAL B 1 202 ? -26.928 29.369  -16.293 1.00 17.06 ? 202 VAL B C   1 
ATOM   3714 O  O   . VAL B 1 202 ? -26.780 28.843  -17.377 1.00 17.06 ? 202 VAL B O   1 
ATOM   3715 C  CB  . VAL B 1 202 ? -24.970 29.319  -14.751 1.00 16.95 ? 202 VAL B CB  1 
ATOM   3716 C  CG1 . VAL B 1 202 ? -24.485 28.817  -13.378 1.00 17.08 ? 202 VAL B CG1 1 
ATOM   3717 C  CG2 . VAL B 1 202 ? -23.954 29.016  -15.877 1.00 16.97 ? 202 VAL B CG2 1 
ATOM   3718 N  N   . PRO B 1 203 ? -27.599 30.486  -16.184 1.00 17.47 ? 203 PRO B N   1 
ATOM   3719 C  CA  . PRO B 1 203 ? -27.914 31.286  -17.324 1.00 18.29 ? 203 PRO B CA  1 
ATOM   3720 C  C   . PRO B 1 203 ? -26.676 31.394  -18.213 1.00 16.61 ? 203 PRO B C   1 
ATOM   3721 O  O   . PRO B 1 203 ? -25.555 31.686  -17.780 1.00 18.14 ? 203 PRO B O   1 
ATOM   3722 C  CB  . PRO B 1 203 ? -28.300 32.648  -16.667 1.00 18.12 ? 203 PRO B CB  1 
ATOM   3723 C  CG  . PRO B 1 203 ? -28.984 32.130  -15.404 1.00 17.90 ? 203 PRO B CG  1 
ATOM   3724 C  CD  . PRO B 1 203 ? -27.933 31.160  -14.905 1.00 17.40 ? 203 PRO B CD  1 
ATOM   3725 N  N   . PRO B 1 204 ? -26.918 31.211  -19.545 1.00 19.44 ? 204 PRO B N   1 
ATOM   3726 C  CA  . PRO B 1 204 ? -28.160 31.131  -20.298 1.00 19.00 ? 204 PRO B CA  1 
ATOM   3727 C  C   . PRO B 1 204 ? -28.868 29.787  -20.385 1.00 17.14 ? 204 PRO B C   1 
ATOM   3728 O  O   . PRO B 1 204 ? -29.864 29.641  -21.111 1.00 18.34 ? 204 PRO B O   1 
ATOM   3729 C  CB  . PRO B 1 204 ? -27.727 31.607  -21.727 1.00 19.74 ? 204 PRO B CB  1 
ATOM   3730 C  CG  . PRO B 1 204 ? -26.342 31.107  -21.805 1.00 19.27 ? 204 PRO B CG  1 
ATOM   3731 C  CD  . PRO B 1 204 ? -25.737 31.319  -20.420 1.00 20.61 ? 204 PRO B CD  1 
ATOM   3732 N  N   . LEU B 1 205 ? -28.376 28.758  -19.604 1.00 14.59 ? 205 LEU B N   1 
ATOM   3733 C  CA  . LEU B 1 205 ? -29.136 27.504  -19.451 1.00 13.91 ? 205 LEU B CA  1 
ATOM   3734 C  C   . LEU B 1 205 ? -29.326 26.713  -20.788 1.00 13.26 ? 205 LEU B C   1 
ATOM   3735 O  O   . LEU B 1 205 ? -30.248 25.878  -20.901 1.00 14.19 ? 205 LEU B O   1 
ATOM   3736 C  CB  . LEU B 1 205 ? -30.508 27.630  -18.765 1.00 16.38 ? 205 LEU B CB  1 
ATOM   3737 C  CG  . LEU B 1 205 ? -30.353 28.302  -17.353 1.00 17.49 ? 205 LEU B CG  1 
ATOM   3738 C  CD1 . LEU B 1 205 ? -31.759 28.803  -16.824 1.00 17.79 ? 205 LEU B CD1 1 
ATOM   3739 C  CD2 . LEU B 1 205 ? -29.633 27.460  -16.324 1.00 17.89 ? 205 LEU B CD2 1 
ATOM   3740 N  N   . LEU B 1 206 ? -28.326 26.885  -21.675 1.00 16.49 ? 206 LEU B N   1 
ATOM   3741 C  CA  . LEU B 1 206 ? -28.449 26.290  -23.045 1.00 15.71 ? 206 LEU B CA  1 
ATOM   3742 C  C   . LEU B 1 206 ? -28.364 24.789  -23.003 1.00 15.61 ? 206 LEU B C   1 
ATOM   3743 O  O   . LEU B 1 206 ? -27.607 24.216  -22.208 1.00 15.64 ? 206 LEU B O   1 
ATOM   3744 C  CB  . LEU B 1 206 ? -27.321 26.801  -23.934 1.00 15.53 ? 206 LEU B CB  1 
ATOM   3745 C  CG  . LEU B 1 206 ? -27.231 28.314  -24.108 1.00 17.70 ? 206 LEU B CG  1 
ATOM   3746 C  CD1 . LEU B 1 206 ? -25.944 28.752  -24.746 1.00 19.52 ? 206 LEU B CD1 1 
ATOM   3747 C  CD2 . LEU B 1 206 ? -28.440 28.830  -24.934 1.00 22.82 ? 206 LEU B CD2 1 
ATOM   3748 N  N   . GLU B 1 207 ? -29.198 24.110  -23.780 1.00 14.12 ? 207 GLU B N   1 
ATOM   3749 C  CA  . GLU B 1 207 ? -29.358 22.667  -23.776 1.00 14.66 ? 207 GLU B CA  1 
ATOM   3750 C  C   . GLU B 1 207 ? -28.381 22.050  -24.793 1.00 17.75 ? 207 GLU B C   1 
ATOM   3751 O  O   . GLU B 1 207 ? -28.782 21.474  -25.826 1.00 16.13 ? 207 GLU B O   1 
ATOM   3752 C  CB  . GLU B 1 207 ? -30.808 22.226  -24.059 1.00 15.81 ? 207 GLU B CB  1 
ATOM   3753 C  CG  . GLU B 1 207 ? -31.680 22.818  -22.950 1.00 17.26 ? 207 GLU B CG  1 
ATOM   3754 C  CD  . GLU B 1 207 ? -33.157 22.478  -23.018 1.00 20.43 ? 207 GLU B CD  1 
ATOM   3755 O  OE1 . GLU B 1 207 ? -33.684 22.165  -24.100 1.00 21.79 ? 207 GLU B OE1 1 
ATOM   3756 O  OE2 . GLU B 1 207 ? -33.821 22.540  -21.966 1.00 19.69 ? 207 GLU B OE2 1 
ATOM   3757 N  N   . SER B 1 208 ? -27.127 22.188  -24.448 1.00 14.93 ? 208 SER B N   1 
ATOM   3758 C  CA  . SER B 1 208 ? -25.977 21.844  -25.315 1.00 13.36 ? 208 SER B CA  1 
ATOM   3759 C  C   . SER B 1 208 ? -25.003 20.942  -24.612 1.00 12.49 ? 208 SER B C   1 
ATOM   3760 O  O   . SER B 1 208 ? -23.886 20.693  -25.123 1.00 13.34 ? 208 SER B O   1 
ATOM   3761 C  CB  . SER B 1 208 ? -25.287 23.120  -25.722 1.00 17.09 ? 208 SER B CB  1 
ATOM   3762 O  OG  . SER B 1 208 ? -24.868 23.904  -24.596 1.00 16.48 ? 208 SER B OG  1 
ATOM   3763 N  N   . VAL B 1 209 ? -25.398 20.359  -23.464 1.00 12.57 ? 209 VAL B N   1 
ATOM   3764 C  CA  . VAL B 1 209 ? -24.380 19.644  -22.694 1.00 13.17 ? 209 VAL B CA  1 
ATOM   3765 C  C   . VAL B 1 209 ? -24.606 18.145  -22.590 1.00 12.29 ? 209 VAL B C   1 
ATOM   3766 O  O   . VAL B 1 209 ? -25.670 17.687  -22.182 1.00 13.34 ? 209 VAL B O   1 
ATOM   3767 C  CB  . VAL B 1 209 ? -24.357 20.209  -21.231 1.00 12.37 ? 209 VAL B CB  1 
ATOM   3768 C  CG1 . VAL B 1 209 ? -23.349 19.430  -20.421 1.00 11.90 ? 209 VAL B CG1 1 
ATOM   3769 C  CG2 . VAL B 1 209 ? -23.997 21.707  -21.243 1.00 12.80 ? 209 VAL B CG2 1 
ATOM   3770 N  N   . THR B 1 210 ? -23.555 17.317  -22.891 1.00 11.86 ? 210 THR B N   1 
ATOM   3771 C  CA  . THR B 1 210 ? -23.559 15.940  -22.592 1.00 11.86 ? 210 THR B CA  1 
ATOM   3772 C  C   . THR B 1 210 ? -22.879 15.914  -21.173 1.00 10.76 ? 210 THR B C   1 
ATOM   3773 O  O   . THR B 1 210 ? -21.698 16.193  -21.028 1.00 12.00 ? 210 THR B O   1 
ATOM   3774 C  CB  . THR B 1 210 ? -22.675 15.114  -23.522 1.00 13.10 ? 210 THR B CB  1 
ATOM   3775 O  OG1 . THR B 1 210 ? -23.294 15.242  -24.833 1.00 14.76 ? 210 THR B OG1 1 
ATOM   3776 C  CG2 . THR B 1 210 ? -22.735 13.630  -23.177 1.00 13.12 ? 210 THR B CG2 1 
ATOM   3777 N  N   . TRP B 1 211 ? -23.719 15.524  -20.211 1.00 11.59 ? 211 TRP B N   1 
ATOM   3778 C  CA  . TRP B 1 211 ? -23.194 15.415  -18.841 1.00 11.19 ? 211 TRP B CA  1 
ATOM   3779 C  C   . TRP B 1 211 ? -22.573 14.043  -18.634 1.00 11.69 ? 211 TRP B C   1 
ATOM   3780 O  O   . TRP B 1 211 ? -23.124 13.034  -18.947 1.00 12.33 ? 211 TRP B O   1 
ATOM   3781 C  CB  . TRP B 1 211 ? -24.376 15.570  -17.890 1.00 10.70 ? 211 TRP B CB  1 
ATOM   3782 C  CG  . TRP B 1 211 ? -24.625 17.021  -17.603 1.00 11.42 ? 211 TRP B CG  1 
ATOM   3783 C  CD1 . TRP B 1 211 ? -25.570 17.894  -18.230 1.00 11.60 ? 211 TRP B CD1 1 
ATOM   3784 C  CD2 . TRP B 1 211 ? -23.876 17.855  -16.715 1.00 11.77 ? 211 TRP B CD2 1 
ATOM   3785 N  NE1 . TRP B 1 211 ? -25.419 19.178  -17.803 1.00 11.87 ? 211 TRP B NE1 1 
ATOM   3786 C  CE2 . TRP B 1 211 ? -24.353 19.218  -16.906 1.00 12.36 ? 211 TRP B CE2 1 
ATOM   3787 C  CE3 . TRP B 1 211 ? -22.796 17.632  -15.855 1.00 11.67 ? 211 TRP B CE3 1 
ATOM   3788 C  CZ2 . TRP B 1 211 ? -23.851 20.297  -16.181 1.00 11.42 ? 211 TRP B CZ2 1 
ATOM   3789 C  CZ3 . TRP B 1 211 ? -22.262 18.756  -15.157 1.00 11.34 ? 211 TRP B CZ3 1 
ATOM   3790 C  CH2 . TRP B 1 211 ? -22.787 20.056  -15.336 1.00 11.93 ? 211 TRP B CH2 1 
ATOM   3791 N  N   . ILE B 1 212 ? -21.444 14.080  -17.962 1.00 11.91 ? 212 ILE B N   1 
ATOM   3792 C  CA  . ILE B 1 212 ? -20.709 12.885  -17.551 1.00 11.40 ? 212 ILE B CA  1 
ATOM   3793 C  C   . ILE B 1 212 ? -20.445 13.091  -16.009 1.00 11.25 ? 212 ILE B C   1 
ATOM   3794 O  O   . ILE B 1 212 ? -19.575 13.916  -15.631 1.00 11.71 ? 212 ILE B O   1 
ATOM   3795 C  CB  . ILE B 1 212 ? -19.393 12.749  -18.331 1.00 11.71 ? 212 ILE B CB  1 
ATOM   3796 C  CG1 . ILE B 1 212 ? -19.704 12.622  -19.825 1.00 13.10 ? 212 ILE B CG1 1 
ATOM   3797 C  CG2 . ILE B 1 212 ? -18.571 11.525  -17.798 1.00 13.21 ? 212 ILE B CG2 1 
ATOM   3798 C  CD1 . ILE B 1 212 ? -18.452 12.748  -20.692 1.00 15.09 ? 212 ILE B CD1 1 
ATOM   3799 N  N   . VAL B 1 213 ? -21.170 12.383  -15.167 1.00 12.51 ? 213 VAL B N   1 
ATOM   3800 C  CA  . VAL B 1 213 ? -21.034 12.638  -13.702 1.00 12.19 ? 213 VAL B CA  1 
ATOM   3801 C  C   . VAL B 1 213 ? -20.371 11.405  -13.081 1.00 13.35 ? 213 VAL B C   1 
ATOM   3802 O  O   . VAL B 1 213 ? -20.905 10.276  -13.201 1.00 14.64 ? 213 VAL B O   1 
ATOM   3803 C  CB  . VAL B 1 213 ? -22.426 12.773  -13.074 1.00 14.14 ? 213 VAL B CB  1 
ATOM   3804 C  CG1 . VAL B 1 213 ? -22.345 12.954  -11.530 1.00 16.32 ? 213 VAL B CG1 1 
ATOM   3805 C  CG2 . VAL B 1 213 ? -23.088 14.005  -13.661 1.00 13.63 ? 213 VAL B CG2 1 
ATOM   3806 N  N   . LEU B 1 214 ? -19.180 11.576  -12.533 1.00 12.90 ? 214 LEU B N   1 
ATOM   3807 C  CA  . LEU B 1 214 ? -18.461 10.462  -11.853 1.00 13.78 ? 214 LEU B CA  1 
ATOM   3808 C  C   . LEU B 1 214 ? -19.140 10.063  -10.563 1.00 14.38 ? 214 LEU B C   1 
ATOM   3809 O  O   . LEU B 1 214 ? -19.551 10.915  -9.755  1.00 14.11 ? 214 LEU B O   1 
ATOM   3810 C  CB  . LEU B 1 214 ? -17.010 10.894  -11.482 1.00 12.56 ? 214 LEU B CB  1 
ATOM   3811 C  CG  . LEU B 1 214 ? -16.176 11.242  -12.710 1.00 14.18 ? 214 LEU B CG  1 
ATOM   3812 C  CD1 . LEU B 1 214 ? -14.694 11.380  -12.359 1.00 14.77 ? 214 LEU B CD1 1 
ATOM   3813 C  CD2 . LEU B 1 214 ? -16.263 10.233  -13.886 1.00 16.11 ? 214 LEU B CD2 1 
ATOM   3814 N  N   . LYS B 1 215 ? -19.269 8.716   -10.370 1.00 13.90 ? 215 LYS B N   1 
ATOM   3815 C  CA  . LYS B 1 215 ? -19.849 8.192   -9.121  1.00 12.76 ? 215 LYS B CA  1 
ATOM   3816 C  C   . LYS B 1 215 ? -18.974 8.438   -7.844  1.00 12.24 ? 215 LYS B C   1 
ATOM   3817 O  O   . LYS B 1 215 ? -19.530 8.711   -6.767  1.00 15.91 ? 215 LYS B O   1 
ATOM   3818 C  CB  . LYS B 1 215 ? -20.048 6.667   -9.273  1.00 14.27 ? 215 LYS B CB  1 
ATOM   3819 C  CG  . LYS B 1 215 ? -20.510 6.055   -7.931  1.00 16.71 ? 215 LYS B CG  1 
ATOM   3820 C  CD  . LYS B 1 215 ? -20.970 4.623   -8.235  1.00 20.88 ? 215 LYS B CD  1 
ATOM   3821 C  CE  . LYS B 1 215 ? -21.163 3.899   -6.910  1.00 23.23 ? 215 LYS B CE  1 
ATOM   3822 N  NZ  . LYS B 1 215 ? -21.610 2.517   -7.122  1.00 27.94 ? 215 LYS B NZ  1 
ATOM   3823 N  N   . GLN B 1 216 ? -17.689 8.368   -7.977  1.00 14.72 ? 216 GLN B N   1 
ATOM   3824 C  CA  . GLN B 1 216 ? -16.834 8.424   -6.771  1.00 14.49 ? 216 GLN B CA  1 
ATOM   3825 C  C   . GLN B 1 216 ? -16.434 9.861   -6.437  1.00 14.45 ? 216 GLN B C   1 
ATOM   3826 O  O   . GLN B 1 216 ? -15.831 10.530  -7.280  1.00 14.04 ? 216 GLN B O   1 
ATOM   3827 C  CB  . GLN B 1 216 ? -15.610 7.596   -6.953  1.00 16.19 ? 216 GLN B CB  1 
ATOM   3828 C  CG  . GLN B 1 216 ? -14.764 7.622   -5.679  1.00 15.57 ? 216 GLN B CG  1 
ATOM   3829 C  CD  . GLN B 1 216 ? -13.505 6.704   -5.642  1.00 20.30 ? 216 GLN B CD  1 
ATOM   3830 O  OE1 . GLN B 1 216 ? -12.988 6.427   -4.535  1.00 23.51 ? 216 GLN B OE1 1 
ATOM   3831 N  NE2 . GLN B 1 216 ? -12.998 6.248   -6.770  1.00 16.12 ? 216 GLN B NE2 1 
ATOM   3832 N  N   . PRO B 1 217 ? -16.760 10.323  -5.227  1.00 15.72 ? 217 PRO B N   1 
ATOM   3833 C  CA  . PRO B 1 217 ? -16.319 11.678  -4.851  1.00 14.56 ? 217 PRO B CA  1 
ATOM   3834 C  C   . PRO B 1 217 ? -14.804 11.783  -4.530  1.00 15.19 ? 217 PRO B C   1 
ATOM   3835 O  O   . PRO B 1 217 ? -14.138 10.770  -4.259  1.00 17.38 ? 217 PRO B O   1 
ATOM   3836 C  CB  . PRO B 1 217 ? -17.086 11.985  -3.537  1.00 15.87 ? 217 PRO B CB  1 
ATOM   3837 C  CG  . PRO B 1 217 ? -18.087 10.857  -3.427  1.00 24.35 ? 217 PRO B CG  1 
ATOM   3838 C  CD  . PRO B 1 217 ? -17.470 9.669   -4.107  1.00 16.83 ? 217 PRO B CD  1 
ATOM   3839 N  N   . ILE B 1 218 ? -14.284 12.983  -4.651  1.00 13.15 ? 218 ILE B N   1 
ATOM   3840 C  CA  . ILE B 1 218 ? -12.958 13.318  -4.093  1.00 13.33 ? 218 ILE B CA  1 
ATOM   3841 C  C   . ILE B 1 218 ? -13.144 14.014  -2.774  1.00 13.40 ? 218 ILE B C   1 
ATOM   3842 O  O   . ILE B 1 218 ? -14.278 14.403  -2.430  1.00 14.46 ? 218 ILE B O   1 
ATOM   3843 C  CB  . ILE B 1 218 ? -12.105 14.149  -5.082  1.00 13.46 ? 218 ILE B CB  1 
ATOM   3844 C  CG1 . ILE B 1 218 ? -12.733 15.506  -5.359  1.00 13.02 ? 218 ILE B CG1 1 
ATOM   3845 C  CG2 . ILE B 1 218 ? -11.981 13.408  -6.417  1.00 13.75 ? 218 ILE B CG2 1 
ATOM   3846 C  CD1 . ILE B 1 218 ? -11.875 16.459  -6.191  1.00 14.18 ? 218 ILE B CD1 1 
ATOM   3847 N  N   A ASN B 1 219 ? -12.048 14.235  -2.023  0.50 14.08 ? 219 ASN B N   1 
ATOM   3848 N  N   B ASN B 1 219 ? -11.999 14.250  -2.080  0.50 13.50 ? 219 ASN B N   1 
ATOM   3849 C  CA  A ASN B 1 219 ? -12.179 14.813  -0.680  0.50 14.34 ? 219 ASN B CA  1 
ATOM   3850 C  CA  B ASN B 1 219 ? -11.990 14.881  -0.752  0.50 13.83 ? 219 ASN B CA  1 
ATOM   3851 C  C   A ASN B 1 219 ? -11.709 16.256  -0.657  0.50 14.27 ? 219 ASN B C   1 
ATOM   3852 C  C   B ASN B 1 219 ? -11.697 16.368  -0.739  0.50 13.86 ? 219 ASN B C   1 
ATOM   3853 O  O   A ASN B 1 219 ? -10.859 16.640  -1.445  0.50 14.85 ? 219 ASN B O   1 
ATOM   3854 O  O   B ASN B 1 219 ? -10.975 16.905  -1.604  0.50 14.21 ? 219 ASN B O   1 
ATOM   3855 C  CB  A ASN B 1 219 ? -11.359 13.957  0.346   0.50 16.02 ? 219 ASN B CB  1 
ATOM   3856 C  CB  B ASN B 1 219 ? -10.962 14.159  0.221   0.50 13.92 ? 219 ASN B CB  1 
ATOM   3857 C  CG  A ASN B 1 219 ? -11.844 12.527  0.399   0.50 17.90 ? 219 ASN B CG  1 
ATOM   3858 C  CG  B ASN B 1 219 ? -9.570  14.100  -0.353  0.50 16.51 ? 219 ASN B CG  1 
ATOM   3859 O  OD1 A ASN B 1 219 ? -11.286 11.640  -0.272  0.50 26.51 ? 219 ASN B OD1 1 
ATOM   3860 O  OD1 B ASN B 1 219 ? -8.600  14.748  0.140   0.50 19.13 ? 219 ASN B OD1 1 
ATOM   3861 N  ND2 A ASN B 1 219 ? -12.928 12.284  1.144   0.50 20.78 ? 219 ASN B ND2 1 
ATOM   3862 N  ND2 B ASN B 1 219 ? -9.435  13.350  -1.435  0.50 15.69 ? 219 ASN B ND2 1 
ATOM   3863 N  N   . ILE B 1 220 ? -12.287 17.054  0.245   1.00 13.32 ? 220 ILE B N   1 
ATOM   3864 C  CA  . ILE B 1 220 ? -11.889 18.409  0.515   1.00 13.70 ? 220 ILE B CA  1 
ATOM   3865 C  C   . ILE B 1 220 ? -12.051 18.592  2.069   1.00 13.44 ? 220 ILE B C   1 
ATOM   3866 O  O   . ILE B 1 220 ? -12.941 17.951  2.634   1.00 13.11 ? 220 ILE B O   1 
ATOM   3867 C  CB  . ILE B 1 220 ? -12.771 19.457  -0.288  1.00 12.05 ? 220 ILE B CB  1 
ATOM   3868 C  CG1 . ILE B 1 220 ? -12.152 20.833  -0.102  1.00 12.64 ? 220 ILE B CG1 1 
ATOM   3869 C  CG2 . ILE B 1 220 ? -14.236 19.334  0.059   1.00 13.57 ? 220 ILE B CG2 1 
ATOM   3870 C  CD1 . ILE B 1 220 ? -12.784 21.893  -1.044  1.00 13.32 ? 220 ILE B CD1 1 
ATOM   3871 N  N   . SER B 1 221 ? -11.218 19.448  2.643   1.00 13.79 ? 221 SER B N   1 
ATOM   3872 C  CA  . SER B 1 221 ? -11.477 19.612  4.094   1.00 13.66 ? 221 SER B CA  1 
ATOM   3873 C  C   . SER B 1 221 ? -12.625 20.644  4.244   1.00 13.86 ? 221 SER B C   1 
ATOM   3874 O  O   . SER B 1 221 ? -12.845 21.457  3.352   1.00 14.23 ? 221 SER B O   1 
ATOM   3875 C  CB  . SER B 1 221 ? -10.226 20.117  4.832   1.00 12.75 ? 221 SER B CB  1 
ATOM   3876 O  OG  . SER B 1 221 ? -9.914  21.465  4.500   1.00 14.10 ? 221 SER B OG  1 
ATOM   3877 N  N   A SER B 1 222 ? -13.234 20.547  5.424   0.50 15.51 ? 222 SER B N   1 
ATOM   3878 N  N   B SER B 1 222 ? -13.276 20.715  5.424   0.50 13.94 ? 222 SER B N   1 
ATOM   3879 C  CA  A SER B 1 222 ? -14.192 21.519  5.772   0.50 16.06 ? 222 SER B CA  1 
ATOM   3880 C  CA  B SER B 1 222 ? -14.276 21.806  5.659   0.50 13.68 ? 222 SER B CA  1 
ATOM   3881 C  C   A SER B 1 222 ? -13.677 22.959  5.686   0.50 14.20 ? 222 SER B C   1 
ATOM   3882 C  C   B SER B 1 222 ? -13.631 23.177  5.584   0.50 12.64 ? 222 SER B C   1 
ATOM   3883 O  O   A SER B 1 222 ? -14.454 23.790  5.276   0.50 14.13 ? 222 SER B O   1 
ATOM   3884 O  O   B SER B 1 222 ? -14.199 24.197  5.129   0.50 12.01 ? 222 SER B O   1 
ATOM   3885 C  CB  A SER B 1 222 ? -14.823 21.226  7.106   0.50 17.77 ? 222 SER B CB  1 
ATOM   3886 C  CB  B SER B 1 222 ? -14.970 21.658  7.007   0.50 12.39 ? 222 SER B CB  1 
ATOM   3887 O  OG  A SER B 1 222 ? -15.633 22.327  7.342   0.50 24.65 ? 222 SER B OG  1 
ATOM   3888 O  OG  B SER B 1 222 ? -14.015 21.508  8.054   0.50 13.09 ? 222 SER B OG  1 
ATOM   3889 N  N   . GLN B 1 223 ? -12.409 23.248  6.089   1.00 15.90 ? 223 GLN B N   1 
ATOM   3890 C  CA  . GLN B 1 223 ? -11.803 24.566  6.049   1.00 15.76 ? 223 GLN B CA  1 
ATOM   3891 C  C   . GLN B 1 223 ? -11.465 25.056  4.627   1.00 15.65 ? 223 GLN B C   1 
ATOM   3892 O  O   . GLN B 1 223 ? -11.648 26.227  4.331   1.00 18.49 ? 223 GLN B O   1 
ATOM   3893 C  CB  . GLN B 1 223 ? -10.529 24.604  6.931   1.00 18.17 ? 223 GLN B CB  1 
ATOM   3894 C  CG  . GLN B 1 223 ? -10.831 24.328  8.427   1.00 20.44 ? 223 GLN B CG  1 
ATOM   3895 C  CD  . GLN B 1 223 ? -10.875 22.866  8.823   1.00 22.87 ? 223 GLN B CD  1 
ATOM   3896 O  OE1 . GLN B 1 223 ? -10.738 21.919  8.032   1.00 21.59 ? 223 GLN B OE1 1 
ATOM   3897 N  NE2 . GLN B 1 223 ? -11.112 22.634  10.153  1.00 21.31 ? 223 GLN B NE2 1 
ATOM   3898 N  N   . GLN B 1 224 ? -10.978 24.156  3.782   1.00 16.04 ? 224 GLN B N   1 
ATOM   3899 C  CA  . GLN B 1 224 ? -10.772 24.591  2.405   1.00 14.78 ? 224 GLN B CA  1 
ATOM   3900 C  C   . GLN B 1 224 ? -12.116 24.894  1.751   1.00 13.54 ? 224 GLN B C   1 
ATOM   3901 O  O   . GLN B 1 224 ? -12.205 25.886  1.072   1.00 13.32 ? 224 GLN B O   1 
ATOM   3902 C  CB  . GLN B 1 224 ? -10.198 23.415  1.644   1.00 13.46 ? 224 GLN B CB  1 
ATOM   3903 C  CG  . GLN B 1 224 ? -8.745  23.069  1.976   1.00 15.25 ? 224 GLN B CG  1 
ATOM   3904 C  CD  . GLN B 1 224 ? -8.274  21.859  1.144   1.00 14.94 ? 224 GLN B CD  1 
ATOM   3905 O  OE1 . GLN B 1 224 ? -8.944  20.821  1.068   1.00 14.89 ? 224 GLN B OE1 1 
ATOM   3906 N  NE2 . GLN B 1 224 ? -7.021  21.982  0.573   1.00 16.47 ? 224 GLN B NE2 1 
ATOM   3907 N  N   . LEU B 1 225 ? -13.149 24.079  1.969   1.00 12.80 ? 225 LEU B N   1 
ATOM   3908 C  CA  . LEU B 1 225 ? -14.451 24.408  1.337   1.00 12.83 ? 225 LEU B CA  1 
ATOM   3909 C  C   . LEU B 1 225 ? -14.997 25.766  1.764   1.00 13.92 ? 225 LEU B C   1 
ATOM   3910 O  O   . LEU B 1 225 ? -15.475 26.571  1.005   1.00 13.00 ? 225 LEU B O   1 
ATOM   3911 C  CB  . LEU B 1 225 ? -15.422 23.304  1.549   1.00 12.13 ? 225 LEU B CB  1 
ATOM   3912 C  CG  . LEU B 1 225 ? -16.799 23.487  0.857   1.00 10.94 ? 225 LEU B CG  1 
ATOM   3913 C  CD1 . LEU B 1 225 ? -16.631 23.586  -0.721  1.00 15.41 ? 225 LEU B CD1 1 
ATOM   3914 C  CD2 . LEU B 1 225 ? -17.719 22.332  1.125   1.00 13.09 ? 225 LEU B CD2 1 
ATOM   3915 N  N   . ALA B 1 226 ? -14.864 26.046  3.096   1.00 14.30 ? 226 ALA B N   1 
ATOM   3916 C  CA  . ALA B 1 226 ? -15.376 27.299  3.581   1.00 13.84 ? 226 ALA B CA  1 
ATOM   3917 C  C   . ALA B 1 226 ? -14.730 28.499  2.976   1.00 14.39 ? 226 ALA B C   1 
ATOM   3918 O  O   . ALA B 1 226 ? -15.369 29.543  2.919   1.00 15.94 ? 226 ALA B O   1 
ATOM   3919 C  CB  . ALA B 1 226 ? -15.124 27.335  5.101   1.00 14.49 ? 226 ALA B CB  1 
ATOM   3920 N  N   . LYS B 1 227 ? -13.487 28.400  2.528   1.00 14.72 ? 227 LYS B N   1 
ATOM   3921 C  CA  . LYS B 1 227 ? -12.813 29.521  1.883   1.00 16.53 ? 227 LYS B CA  1 
ATOM   3922 C  C   . LYS B 1 227 ? -13.560 30.050  0.648   1.00 15.27 ? 227 LYS B C   1 
ATOM   3923 O  O   . LYS B 1 227 ? -13.603 31.248  0.399   1.00 17.77 ? 227 LYS B O   1 
ATOM   3924 C  CB  . LYS B 1 227 ? -11.397 29.207  1.507   1.00 20.78 ? 227 LYS B CB  1 
ATOM   3925 C  CG  . LYS B 1 227 ? -10.520 29.249  2.766   1.00 29.52 ? 227 LYS B CG  1 
ATOM   3926 C  CD  . LYS B 1 227 ? -9.031  29.565  2.547   1.00 35.02 ? 227 LYS B CD  1 
ATOM   3927 C  CE  . LYS B 1 227 ? -8.783  30.684  1.548   1.00 35.48 ? 227 LYS B CE  1 
ATOM   3928 N  NZ  . LYS B 1 227 ? -8.638  32.059  2.107   1.00 39.56 ? 227 LYS B NZ  1 
ATOM   3929 N  N   . PHE B 1 228 ? -14.205 29.118  -0.085  1.00 15.54 ? 228 PHE B N   1 
ATOM   3930 C  CA  . PHE B 1 228 ? -14.958 29.561  -1.232  1.00 14.01 ? 228 PHE B CA  1 
ATOM   3931 C  C   . PHE B 1 228 ? -16.142 30.477  -0.957  1.00 14.92 ? 228 PHE B C   1 
ATOM   3932 O  O   . PHE B 1 228 ? -16.519 31.339  -1.762  1.00 16.28 ? 228 PHE B O   1 
ATOM   3933 C  CB  . PHE B 1 228 ? -15.468 28.353  -2.083  1.00 14.03 ? 228 PHE B CB  1 
ATOM   3934 C  CG  . PHE B 1 228 ? -14.342 27.567  -2.647  1.00 14.26 ? 228 PHE B CG  1 
ATOM   3935 C  CD1 . PHE B 1 228 ? -13.943 26.402  -2.090  1.00 14.60 ? 228 PHE B CD1 1 
ATOM   3936 C  CD2 . PHE B 1 228 ? -13.685 28.083  -3.798  1.00 14.91 ? 228 PHE B CD2 1 
ATOM   3937 C  CE1 . PHE B 1 228 ? -12.813 25.701  -2.573  1.00 15.01 ? 228 PHE B CE1 1 
ATOM   3938 C  CE2 . PHE B 1 228 ? -12.578 27.398  -4.293  1.00 14.34 ? 228 PHE B CE2 1 
ATOM   3939 C  CZ  . PHE B 1 228 ? -12.154 26.226  -3.723  1.00 13.34 ? 228 PHE B CZ  1 
ATOM   3940 N  N   . ARG B 1 229 ? -16.778 30.295  0.214   1.00 14.59 ? 229 ARG B N   1 
ATOM   3941 C  CA  . ARG B 1 229 ? -17.916 31.122  0.587   1.00 15.43 ? 229 ARG B CA  1 
ATOM   3942 C  C   . ARG B 1 229 ? -17.534 32.545  0.939   1.00 14.35 ? 229 ARG B C   1 
ATOM   3943 O  O   . ARG B 1 229 ? -18.447 33.339  0.993   1.00 16.68 ? 229 ARG B O   1 
ATOM   3944 C  CB  . ARG B 1 229 ? -18.558 30.430  1.847   1.00 13.69 ? 229 ARG B CB  1 
ATOM   3945 C  CG  . ARG B 1 229 ? -19.015 29.037  1.629   1.00 14.18 ? 229 ARG B CG  1 
ATOM   3946 C  CD  . ARG B 1 229 ? -19.913 28.514  2.783   1.00 15.19 ? 229 ARG B CD  1 
ATOM   3947 N  NE  . ARG B 1 229 ? -20.263 27.083  2.643   1.00 14.35 ? 229 ARG B NE  1 
ATOM   3948 C  CZ  . ARG B 1 229 ? -19.630 26.061  3.198   1.00 14.07 ? 229 ARG B CZ  1 
ATOM   3949 N  NH1 . ARG B 1 229 ? -18.636 26.289  4.108   1.00 16.42 ? 229 ARG B NH1 1 
ATOM   3950 N  NH2 . ARG B 1 229 ? -19.961 24.763  2.879   1.00 15.89 ? 229 ARG B NH2 1 
ATOM   3951 N  N   . SER B 1 230 ? -16.232 32.829  1.064   1.00 17.19 ? 230 SER B N   1 
ATOM   3952 C  CA  . SER B 1 230 ? -15.743 34.205  1.311   1.00 17.09 ? 230 SER B CA  1 
ATOM   3953 C  C   . SER B 1 230 ? -15.603 35.013  0.012   1.00 17.47 ? 230 SER B C   1 
ATOM   3954 O  O   . SER B 1 230 ? -15.408 36.255  0.043   1.00 19.03 ? 230 SER B O   1 
ATOM   3955 C  CB  . SER B 1 230 ? -14.464 34.176  2.164   1.00 21.49 ? 230 SER B CB  1 
ATOM   3956 O  OG  . SER B 1 230 ? -13.401 33.702  1.368   1.00 29.48 ? 230 SER B OG  1 
ATOM   3957 N  N   . LEU B 1 231 ? -15.738 34.366  -1.182  1.00 17.64 ? 231 LEU B N   1 
ATOM   3958 C  CA  . LEU B 1 231 ? -15.824 35.135  -2.425  1.00 16.53 ? 231 LEU B CA  1 
ATOM   3959 C  C   . LEU B 1 231 ? -17.038 36.028  -2.392  1.00 17.22 ? 231 LEU B C   1 
ATOM   3960 O  O   . LEU B 1 231 ? -18.082 35.638  -1.895  1.00 18.27 ? 231 LEU B O   1 
ATOM   3961 C  CB  . LEU B 1 231 ? -15.946 34.177  -3.630  1.00 17.36 ? 231 LEU B CB  1 
ATOM   3962 C  CG  . LEU B 1 231 ? -14.707 33.355  -3.867  1.00 15.96 ? 231 LEU B CG  1 
ATOM   3963 C  CD1 . LEU B 1 231 ? -15.049 32.255  -4.921  1.00 17.13 ? 231 LEU B CD1 1 
ATOM   3964 C  CD2 . LEU B 1 231 ? -13.533 34.267  -4.287  1.00 17.12 ? 231 LEU B CD2 1 
ATOM   3965 N  N   . LEU B 1 232 ? -16.904 37.216  -2.978  1.00 20.03 ? 232 LEU B N   1 
ATOM   3966 C  CA  . LEU B 1 232 ? -18.085 38.084  -3.116  1.00 22.05 ? 232 LEU B CA  1 
ATOM   3967 C  C   . LEU B 1 232 ? -18.794 37.872  -4.420  1.00 22.31 ? 232 LEU B C   1 
ATOM   3968 O  O   . LEU B 1 232 ? -18.146 37.531  -5.445  1.00 20.59 ? 232 LEU B O   1 
ATOM   3969 C  CB  . LEU B 1 232 ? -17.691 39.585  -3.041  1.00 23.21 ? 232 LEU B CB  1 
ATOM   3970 C  CG  . LEU B 1 232 ? -16.819 39.958  -1.843  1.00 22.93 ? 232 LEU B CG  1 
ATOM   3971 C  CD1 . LEU B 1 232 ? -16.341 41.414  -1.992  1.00 28.17 ? 232 LEU B CD1 1 
ATOM   3972 C  CD2 . LEU B 1 232 ? -17.458 39.646  -0.517  1.00 29.23 ? 232 LEU B CD2 1 
ATOM   3973 N  N   . CYS B 1 233 ? -20.105 38.057  -4.431  1.00 21.54 ? 233 CYS B N   1 
ATOM   3974 C  CA  . CYS B 1 233 ? -20.855 38.057  -5.667  1.00 22.39 ? 233 CYS B CA  1 
ATOM   3975 C  C   . CYS B 1 233 ? -21.061 39.479  -6.138  1.00 24.60 ? 233 CYS B C   1 
ATOM   3976 O  O   . CYS B 1 233 ? -21.759 39.691  -7.172  1.00 26.17 ? 233 CYS B O   1 
ATOM   3977 C  CB  . CYS B 1 233 ? -22.233 37.353  -5.594  1.00 21.49 ? 233 CYS B CB  1 
ATOM   3978 S  SG  . CYS B 1 233 ? -23.321 38.055  -4.280  1.00 28.49 ? 233 CYS B SG  1 
ATOM   3979 N  N   . THR B 1 234 ? -20.436 40.405  -5.402  1.00 26.60 ? 234 THR B N   1 
ATOM   3980 C  CA  . THR B 1 234 ? -20.482 41.850  -5.730  1.00 29.70 ? 234 THR B CA  1 
ATOM   3981 C  C   . THR B 1 234 ? -19.113 42.400  -6.144  1.00 29.22 ? 234 THR B C   1 
ATOM   3982 O  O   . THR B 1 234 ? -18.039 41.940  -5.669  1.00 29.73 ? 234 THR B O   1 
ATOM   3983 C  CB  . THR B 1 234 ? -21.001 42.625  -4.496  1.00 27.39 ? 234 THR B CB  1 
ATOM   3984 O  OG1 . THR B 1 234 ? -20.218 42.239  -3.355  1.00 31.22 ? 234 THR B OG1 1 
ATOM   3985 C  CG2 . THR B 1 234 ? -22.490 42.403  -4.247  1.00 30.03 ? 234 THR B CG2 1 
ATOM   3986 N  N   . ALA B 1 235 ? -19.130 43.351  -7.090  1.00 38.02 ? 235 ALA B N   1 
ATOM   3987 C  CA  . ALA B 1 235 ? -17.897 44.019  -7.610  1.00 38.69 ? 235 ALA B CA  1 
ATOM   3988 C  C   . ALA B 1 235 ? -17.301 45.007  -6.605  1.00 45.37 ? 235 ALA B C   1 
ATOM   3989 O  O   . ALA B 1 235 ? -17.955 45.422  -5.642  1.00 42.78 ? 235 ALA B O   1 
ATOM   3990 C  CB  . ALA B 1 235 ? -18.181 44.728  -8.949  1.00 39.52 ? 235 ALA B CB  1 
ATOM   3991 N  N   . GLU B 1 236 ? -16.038 45.357  -6.816  1.00 52.58 ? 236 GLU B N   1 
ATOM   3992 C  CA  . GLU B 1 236 ? -15.374 46.368  -5.983  1.00 58.07 ? 236 GLU B CA  1 
ATOM   3993 C  C   . GLU B 1 236 ? -16.260 47.638  -5.961  1.00 53.18 ? 236 GLU B C   1 
ATOM   3994 O  O   . GLU B 1 236 ? -16.789 48.042  -7.003  1.00 44.73 ? 236 GLU B O   1 
ATOM   3995 C  CB  . GLU B 1 236 ? -13.984 46.656  -6.560  1.00 60.92 ? 236 GLU B CB  1 
ATOM   3996 N  N   . GLY B 1 237 ? -16.487 48.217  -4.775  1.00 58.62 ? 237 GLY B N   1 
ATOM   3997 C  CA  . GLY B 1 237 ? -17.283 49.468  -4.654  1.00 54.20 ? 237 GLY B CA  1 
ATOM   3998 C  C   . GLY B 1 237 ? -18.809 49.348  -4.588  1.00 54.18 ? 237 GLY B C   1 
ATOM   3999 O  O   . GLY B 1 237 ? -19.514 50.356  -4.494  1.00 46.99 ? 237 GLY B O   1 
ATOM   4000 N  N   . GLU B 1 238 ? -19.323 48.116  -4.619  1.00 47.03 ? 238 GLU B N   1 
ATOM   4001 C  CA  . GLU B 1 238 ? -20.752 47.805  -4.423  1.00 48.45 ? 238 GLU B CA  1 
ATOM   4002 C  C   . GLU B 1 238 ? -20.939 47.352  -2.975  1.00 48.67 ? 238 GLU B C   1 
ATOM   4003 O  O   . GLU B 1 238 ? -19.982 46.922  -2.327  1.00 45.07 ? 238 GLU B O   1 
ATOM   4004 C  CB  . GLU B 1 238 ? -21.106 46.593  -5.276  1.00 49.79 ? 238 GLU B CB  1 
ATOM   4005 C  CG  . GLU B 1 238 ? -22.077 46.774  -6.417  1.00 56.53 ? 238 GLU B CG  1 
ATOM   4006 C  CD  . GLU B 1 238 ? -22.599 45.421  -6.879  1.00 66.38 ? 238 GLU B CD  1 
ATOM   4007 O  OE1 . GLU B 1 238 ? -21.867 44.711  -7.638  1.00 63.90 ? 238 GLU B OE1 1 
ATOM   4008 O  OE2 . GLU B 1 238 ? -23.729 45.056  -6.454  1.00 65.20 ? 238 GLU B OE2 1 
ATOM   4009 N  N   . ALA B 1 239 ? -22.170 47.372  -2.478  1.00 47.12 ? 239 ALA B N   1 
ATOM   4010 C  CA  . ALA B 1 239 ? -22.427 46.825  -1.147  1.00 48.01 ? 239 ALA B CA  1 
ATOM   4011 C  C   . ALA B 1 239 ? -22.076 45.302  -1.165  1.00 41.25 ? 239 ALA B C   1 
ATOM   4012 O  O   . ALA B 1 239 ? -22.678 44.584  -1.973  1.00 43.33 ? 239 ALA B O   1 
ATOM   4013 C  CB  . ALA B 1 239 ? -23.902 47.045  -0.777  1.00 41.89 ? 239 ALA B CB  1 
ATOM   4014 N  N   . ALA B 1 240 ? -21.117 44.866  -0.320  1.00 38.85 ? 240 ALA B N   1 
ATOM   4015 C  CA  . ALA B 1 240 ? -20.629 43.439  -0.237  1.00 34.32 ? 240 ALA B CA  1 
ATOM   4016 C  C   . ALA B 1 240 ? -21.711 42.379  0.078   1.00 35.37 ? 240 ALA B C   1 
ATOM   4017 O  O   . ALA B 1 240 ? -22.500 42.519  1.033   1.00 31.04 ? 240 ALA B O   1 
ATOM   4018 C  CB  . ALA B 1 240 ? -19.455 43.293  0.746   1.00 37.57 ? 240 ALA B CB  1 
ATOM   4019 N  N   . ALA B 1 241 ? -21.784 41.338  -0.755  1.00 27.74 ? 241 ALA B N   1 
ATOM   4020 C  CA  . ALA B 1 241 ? -22.616 40.171  -0.414  1.00 25.75 ? 241 ALA B CA  1 
ATOM   4021 C  C   . ALA B 1 241 ? -21.751 38.972  -0.732  1.00 24.03 ? 241 ALA B C   1 
ATOM   4022 O  O   . ALA B 1 241 ? -20.932 39.019  -1.658  1.00 22.39 ? 241 ALA B O   1 
ATOM   4023 C  CB  . ALA B 1 241 ? -23.936 40.123  -1.179  1.00 25.49 ? 241 ALA B CB  1 
ATOM   4024 N  N   . PHE B 1 242 ? -21.899 37.947  0.085   1.00 18.68 ? 242 PHE B N   1 
ATOM   4025 C  CA  . PHE B 1 242 ? -21.083 36.741  -0.050  1.00 19.83 ? 242 PHE B CA  1 
ATOM   4026 C  C   . PHE B 1 242 ? -21.725 35.629  -0.867  1.00 16.63 ? 242 PHE B C   1 
ATOM   4027 O  O   . PHE B 1 242 ? -22.898 35.400  -0.715  1.00 18.36 ? 242 PHE B O   1 
ATOM   4028 C  CB  . PHE B 1 242 ? -20.672 36.253  1.359   1.00 18.28 ? 242 PHE B CB  1 
ATOM   4029 C  CG  . PHE B 1 242 ? -19.827 37.242  2.084   1.00 21.28 ? 242 PHE B CG  1 
ATOM   4030 C  CD1 . PHE B 1 242 ? -20.423 38.214  2.945   1.00 21.42 ? 242 PHE B CD1 1 
ATOM   4031 C  CD2 . PHE B 1 242 ? -18.468 37.261  1.908   1.00 20.77 ? 242 PHE B CD2 1 
ATOM   4032 C  CE1 . PHE B 1 242 ? -19.610 39.177  3.543   1.00 23.06 ? 242 PHE B CE1 1 
ATOM   4033 C  CE2 . PHE B 1 242 ? -17.638 38.184  2.562   1.00 25.56 ? 242 PHE B CE2 1 
ATOM   4034 C  CZ  . PHE B 1 242 ? -18.217 39.119  3.387   1.00 26.24 ? 242 PHE B CZ  1 
ATOM   4035 N  N   . LEU B 1 243 ? -20.875 34.941  -1.653  1.00 17.55 ? 243 LEU B N   1 
ATOM   4036 C  CA  . LEU B 1 243 ? -21.294 33.778  -2.451  1.00 17.04 ? 243 LEU B CA  1 
ATOM   4037 C  C   . LEU B 1 243 ? -21.340 32.552  -1.529  1.00 15.95 ? 243 LEU B C   1 
ATOM   4038 O  O   . LEU B 1 243 ? -20.529 31.625  -1.676  1.00 14.82 ? 243 LEU B O   1 
ATOM   4039 C  CB  . LEU B 1 243 ? -20.383 33.721  -3.718  1.00 16.40 ? 243 LEU B CB  1 
ATOM   4040 C  CG  . LEU B 1 243 ? -20.877 32.633  -4.686  1.00 16.91 ? 243 LEU B CG  1 
ATOM   4041 C  CD1 . LEU B 1 243 ? -22.178 33.033  -5.288  1.00 15.64 ? 243 LEU B CD1 1 
ATOM   4042 C  CD2 . LEU B 1 243 ? -19.745 32.572  -5.775  1.00 18.29 ? 243 LEU B CD2 1 
ATOM   4043 N  N   . VAL B 1 244 ? -22.285 32.537  -0.559  1.00 14.89 ? 244 VAL B N   1 
ATOM   4044 C  CA  . VAL B 1 244 ? -22.251 31.377  0.396   1.00 14.87 ? 244 VAL B CA  1 
ATOM   4045 C  C   . VAL B 1 244 ? -22.788 30.092  -0.194  1.00 14.04 ? 244 VAL B C   1 
ATOM   4046 O  O   . VAL B 1 244 ? -22.582 29.017  0.356   1.00 13.72 ? 244 VAL B O   1 
ATOM   4047 C  CB  . VAL B 1 244 ? -22.972 31.761  1.753   1.00 16.00 ? 244 VAL B CB  1 
ATOM   4048 C  CG1 . VAL B 1 244 ? -22.257 32.930  2.427   1.00 15.51 ? 244 VAL B CG1 1 
ATOM   4049 C  CG2 . VAL B 1 244 ? -24.469 31.993  1.508   1.00 17.74 ? 244 VAL B CG2 1 
ATOM   4050 N  N   . SER B 1 245 ? -23.519 30.207  -1.343  1.00 14.96 ? 245 SER B N   1 
ATOM   4051 C  CA  . SER B 1 245 ? -24.213 29.063  -1.951  1.00 14.82 ? 245 SER B CA  1 
ATOM   4052 C  C   . SER B 1 245 ? -24.405 29.399  -3.410  1.00 14.13 ? 245 SER B C   1 
ATOM   4053 O  O   . SER B 1 245 ? -24.738 30.525  -3.784  1.00 16.14 ? 245 SER B O   1 
ATOM   4054 C  CB  . SER B 1 245 ? -25.547 28.773  -1.309  1.00 15.61 ? 245 SER B CB  1 
ATOM   4055 O  OG  . SER B 1 245 ? -26.160 27.629  -1.830  1.00 15.75 ? 245 SER B OG  1 
ATOM   4056 N  N   . ASN B 1 246 ? -24.176 28.382  -4.288  1.00 14.00 ? 246 ASN B N   1 
ATOM   4057 C  CA  . ASN B 1 246 ? -24.247 28.693  -5.739  1.00 12.68 ? 246 ASN B CA  1 
ATOM   4058 C  C   . ASN B 1 246 ? -24.558 27.415  -6.472  1.00 13.39 ? 246 ASN B C   1 
ATOM   4059 O  O   . ASN B 1 246 ? -23.940 27.148  -7.512  1.00 14.45 ? 246 ASN B O   1 
ATOM   4060 C  CB  . ASN B 1 246 ? -22.914 29.294  -6.251  1.00 12.55 ? 246 ASN B CB  1 
ATOM   4061 C  CG  . ASN B 1 246 ? -21.737 28.379  -6.137  1.00 11.89 ? 246 ASN B CG  1 
ATOM   4062 O  OD1 . ASN B 1 246 ? -21.826 27.348  -5.465  1.00 14.45 ? 246 ASN B OD1 1 
ATOM   4063 N  ND2 . ASN B 1 246 ? -20.621 28.692  -6.864  1.00 14.15 ? 246 ASN B ND2 1 
ATOM   4064 N  N   . HIS B 1 247 ? -25.528 26.660  -5.973  1.00 14.09 ? 247 HIS B N   1 
ATOM   4065 C  CA  . HIS B 1 247 ? -25.944 25.429  -6.665  1.00 13.35 ? 247 HIS B CA  1 
ATOM   4066 C  C   . HIS B 1 247 ? -27.403 25.531  -7.034  1.00 15.37 ? 247 HIS B C   1 
ATOM   4067 O  O   . HIS B 1 247 ? -28.282 26.098  -6.293  1.00 17.32 ? 247 HIS B O   1 
ATOM   4068 C  CB  . HIS B 1 247 ? -25.750 24.161  -5.845  1.00 14.93 ? 247 HIS B CB  1 
ATOM   4069 C  CG  . HIS B 1 247 ? -26.456 24.222  -4.501  1.00 15.24 ? 247 HIS B CG  1 
ATOM   4070 N  ND1 . HIS B 1 247 ? -27.709 23.749  -4.255  1.00 19.84 ? 247 HIS B ND1 1 
ATOM   4071 C  CD2 . HIS B 1 247 ? -26.008 24.817  -3.351  1.00 12.73 ? 247 HIS B CD2 1 
ATOM   4072 C  CE1 . HIS B 1 247 ? -27.985 23.982  -2.880  1.00 16.47 ? 247 HIS B CE1 1 
ATOM   4073 N  NE2 . HIS B 1 247 ? -26.955 24.653  -2.389  1.00 18.64 ? 247 HIS B NE2 1 
ATOM   4074 N  N   . ARG B 1 248 ? -27.726 25.069  -8.264  1.00 14.81 ? 248 ARG B N   1 
ATOM   4075 C  CA  . ARG B 1 248 ? -29.099 25.079  -8.752  1.00 14.76 ? 248 ARG B CA  1 
ATOM   4076 C  C   . ARG B 1 248 ? -29.790 23.804  -8.305  1.00 14.28 ? 248 ARG B C   1 
ATOM   4077 O  O   . ARG B 1 248 ? -29.184 22.767  -8.294  1.00 16.33 ? 248 ARG B O   1 
ATOM   4078 C  CB  . ARG B 1 248 ? -29.046 25.102  -10.336 1.00 14.32 ? 248 ARG B CB  1 
ATOM   4079 C  CG  . ARG B 1 248 ? -30.433 25.276  -10.981 1.00 15.21 ? 248 ARG B CG  1 
ATOM   4080 C  CD  . ARG B 1 248 ? -30.435 25.066  -12.510 1.00 15.02 ? 248 ARG B CD  1 
ATOM   4081 N  NE  . ARG B 1 248 ? -31.716 25.554  -12.991 1.00 16.27 ? 248 ARG B NE  1 
ATOM   4082 C  CZ  . ARG B 1 248 ? -32.247 25.199  -14.178 1.00 18.41 ? 248 ARG B CZ  1 
ATOM   4083 N  NH1 . ARG B 1 248 ? -31.572 24.485  -15.062 1.00 15.83 ? 248 ARG B NH1 1 
ATOM   4084 N  NH2 . ARG B 1 248 ? -33.397 25.740  -14.567 1.00 18.20 ? 248 ARG B NH2 1 
ATOM   4085 N  N   . PRO B 1 249 ? -31.099 23.903  -7.927  1.00 15.81 ? 249 PRO B N   1 
ATOM   4086 C  CA  . PRO B 1 249 ? -31.852 22.721  -7.600  1.00 16.69 ? 249 PRO B CA  1 
ATOM   4087 C  C   . PRO B 1 249 ? -32.016 21.733  -8.719  1.00 18.29 ? 249 PRO B C   1 
ATOM   4088 O  O   . PRO B 1 249 ? -31.900 22.151  -9.861  1.00 16.94 ? 249 PRO B O   1 
ATOM   4089 C  CB  . PRO B 1 249 ? -33.269 23.272  -7.284  1.00 20.81 ? 249 PRO B CB  1 
ATOM   4090 C  CG  . PRO B 1 249 ? -33.049 24.692  -6.955  1.00 20.72 ? 249 PRO B CG  1 
ATOM   4091 C  CD  . PRO B 1 249 ? -31.836 25.173  -7.702  1.00 18.89 ? 249 PRO B CD  1 
ATOM   4092 N  N   . PRO B 1 250 ? -32.285 20.483  -8.416  1.00 18.33 ? 250 PRO B N   1 
ATOM   4093 C  CA  . PRO B 1 250 ? -32.529 19.483  -9.514  1.00 19.92 ? 250 PRO B CA  1 
ATOM   4094 C  C   . PRO B 1 250 ? -33.807 19.826  -10.344 1.00 17.88 ? 250 PRO B C   1 
ATOM   4095 O  O   . PRO B 1 250 ? -34.805 20.435  -9.835  1.00 18.52 ? 250 PRO B O   1 
ATOM   4096 C  CB  . PRO B 1 250 ? -32.667 18.160  -8.802  1.00 20.49 ? 250 PRO B CB  1 
ATOM   4097 C  CG  . PRO B 1 250 ? -33.208 18.575  -7.438  1.00 24.70 ? 250 PRO B CG  1 
ATOM   4098 C  CD  . PRO B 1 250 ? -32.569 19.896  -7.082  1.00 21.07 ? 250 PRO B CD  1 
ATOM   4099 N  N   . GLN B 1 251 ? -33.737 19.506  -11.652 1.00 14.68 ? 251 GLN B N   1 
ATOM   4100 C  CA  . GLN B 1 251 ? -34.784 19.851  -12.606 1.00 15.63 ? 251 GLN B CA  1 
ATOM   4101 C  C   . GLN B 1 251 ? -35.427 18.555  -13.094 1.00 15.53 ? 251 GLN B C   1 
ATOM   4102 O  O   . GLN B 1 251 ? -34.867 17.454  -13.081 1.00 16.83 ? 251 GLN B O   1 
ATOM   4103 C  CB  . GLN B 1 251 ? -34.113 20.576  -13.800 1.00 15.12 ? 251 GLN B CB  1 
ATOM   4104 C  CG  . GLN B 1 251 ? -33.379 21.797  -13.331 1.00 15.23 ? 251 GLN B CG  1 
ATOM   4105 C  CD  . GLN B 1 251 ? -34.287 22.796  -12.601 1.00 21.02 ? 251 GLN B CD  1 
ATOM   4106 O  OE1 . GLN B 1 251 ? -33.973 23.306  -11.489 1.00 23.55 ? 251 GLN B OE1 1 
ATOM   4107 N  NE2 . GLN B 1 251 ? -35.453 23.089  -13.207 1.00 18.82 ? 251 GLN B NE2 1 
ATOM   4108 N  N   . PRO B 1 252 ? -36.703 18.640  -13.578 1.00 15.91 ? 252 PRO B N   1 
ATOM   4109 C  CA  . PRO B 1 252 ? -37.424 17.441  -14.049 1.00 17.51 ? 252 PRO B CA  1 
ATOM   4110 C  C   . PRO B 1 252 ? -36.719 16.721  -15.186 1.00 17.07 ? 252 PRO B C   1 
ATOM   4111 O  O   . PRO B 1 252 ? -36.266 17.332  -16.154 1.00 18.09 ? 252 PRO B O   1 
ATOM   4112 C  CB  . PRO B 1 252 ? -38.785 18.020  -14.480 1.00 18.70 ? 252 PRO B CB  1 
ATOM   4113 C  CG  . PRO B 1 252 ? -38.767 19.467  -14.009 1.00 21.32 ? 252 PRO B CG  1 
ATOM   4114 C  CD  . PRO B 1 252 ? -37.369 19.920  -13.850 1.00 16.65 ? 252 PRO B CD  1 
ATOM   4115 N  N   . LEU B 1 253 ? -36.706 15.417  -15.020 1.00 17.73 ? 253 LEU B N   1 
ATOM   4116 C  CA  . LEU B 1 253 ? -36.073 14.551  -16.026 1.00 18.24 ? 253 LEU B CA  1 
ATOM   4117 C  C   . LEU B 1 253 ? -36.758 14.623  -17.417 1.00 20.61 ? 253 LEU B C   1 
ATOM   4118 O  O   . LEU B 1 253 ? -36.105 14.504  -18.458 1.00 18.53 ? 253 LEU B O   1 
ATOM   4119 C  CB  . LEU B 1 253 ? -35.957 13.127  -15.548 1.00 21.99 ? 253 LEU B CB  1 
ATOM   4120 C  CG  . LEU B 1 253 ? -34.918 12.243  -16.286 1.00 22.07 ? 253 LEU B CG  1 
ATOM   4121 C  CD1 . LEU B 1 253 ? -33.478 12.784  -16.383 1.00 20.75 ? 253 LEU B CD1 1 
ATOM   4122 C  CD2 . LEU B 1 253 ? -34.947 10.890  -15.564 1.00 23.86 ? 253 LEU B CD2 1 
ATOM   4123 N  N   . LYS B 1 254 ? -38.084 14.778  -17.389 1.00 20.93 ? 254 LYS B N   1 
ATOM   4124 C  CA  . LYS B 1 254 ? -38.862 14.911  -18.596 1.00 19.97 ? 254 LYS B CA  1 
ATOM   4125 C  C   . LYS B 1 254 ? -38.533 13.747  -19.645 1.00 17.45 ? 254 LYS B C   1 
ATOM   4126 O  O   . LYS B 1 254 ? -38.422 14.009  -20.830 1.00 20.66 ? 254 LYS B O   1 
ATOM   4127 C  CB  . LYS B 1 254 ? -38.743 16.320  -19.160 1.00 22.02 ? 254 LYS B CB  1 
ATOM   4128 C  CG  . LYS B 1 254 ? -39.428 17.384  -18.252 1.00 25.14 ? 254 LYS B CG  1 
ATOM   4129 C  CD  . LYS B 1 254 ? -39.592 18.679  -18.978 1.00 29.35 ? 254 LYS B CD  1 
ATOM   4130 C  CE  . LYS B 1 254 ? -40.268 19.821  -18.193 1.00 31.02 ? 254 LYS B CE  1 
ATOM   4131 N  NZ  . LYS B 1 254 ? -41.542 19.427  -17.590 1.00 39.37 ? 254 LYS B NZ  1 
ATOM   4132 N  N   . GLY B 1 255 ? -38.464 12.519  -19.169 1.00 18.14 ? 255 GLY B N   1 
ATOM   4133 C  CA  . GLY B 1 255 ? -38.342 11.371  -20.114 1.00 18.27 ? 255 GLY B CA  1 
ATOM   4134 C  C   . GLY B 1 255 ? -36.957 11.041  -20.648 1.00 20.08 ? 255 GLY B C   1 
ATOM   4135 O  O   . GLY B 1 255 ? -36.799 10.169  -21.470 1.00 19.45 ? 255 GLY B O   1 
ATOM   4136 N  N   . ARG B 1 256 ? -35.944 11.784  -20.215 1.00 17.92 ? 256 ARG B N   1 
ATOM   4137 C  CA  . ARG B 1 256 ? -34.560 11.464  -20.598 1.00 17.89 ? 256 ARG B CA  1 
ATOM   4138 C  C   . ARG B 1 256 ? -34.075 10.201  -19.977 1.00 18.09 ? 256 ARG B C   1 
ATOM   4139 O  O   . ARG B 1 256 ? -34.525 9.776   -18.883 1.00 20.41 ? 256 ARG B O   1 
ATOM   4140 C  CB  . ARG B 1 256 ? -33.627 12.644  -20.228 1.00 15.76 ? 256 ARG B CB  1 
ATOM   4141 C  CG  . ARG B 1 256 ? -33.881 13.854  -21.029 1.00 15.65 ? 256 ARG B CG  1 
ATOM   4142 C  CD  . ARG B 1 256 ? -33.054 15.039  -20.482 1.00 14.98 ? 256 ARG B CD  1 
ATOM   4143 N  NE  . ARG B 1 256 ? -33.634 15.556  -19.256 1.00 15.56 ? 256 ARG B NE  1 
ATOM   4144 C  CZ  . ARG B 1 256 ? -33.052 16.507  -18.510 1.00 15.57 ? 256 ARG B CZ  1 
ATOM   4145 N  NH1 . ARG B 1 256 ? -31.823 17.012  -18.814 1.00 13.94 ? 256 ARG B NH1 1 
ATOM   4146 N  NH2 . ARG B 1 256 ? -33.689 16.991  -17.446 1.00 15.88 ? 256 ARG B NH2 1 
ATOM   4147 N  N   . LYS B 1 257 ? -33.160 9.547   -20.698 1.00 19.64 ? 257 LYS B N   1 
ATOM   4148 C  CA  . LYS B 1 257 ? -32.568 8.277   -20.288 1.00 19.61 ? 257 LYS B CA  1 
ATOM   4149 C  C   . LYS B 1 257 ? -31.189 8.591   -19.608 1.00 17.06 ? 257 LYS B C   1 
ATOM   4150 O  O   . LYS B 1 257 ? -30.366 9.239   -20.224 1.00 19.23 ? 257 LYS B O   1 
ATOM   4151 C  CB  . LYS B 1 257 ? -32.290 7.433   -21.536 1.00 26.52 ? 257 LYS B CB  1 
ATOM   4152 C  CG  . LYS B 1 257 ? -31.755 6.056   -21.217 1.00 28.61 ? 257 LYS B CG  1 
ATOM   4153 C  CD  . LYS B 1 257 ? -31.221 5.294   -22.447 1.00 29.33 ? 257 LYS B CD  1 
ATOM   4154 C  CE  . LYS B 1 257 ? -32.318 4.620   -23.286 1.00 32.79 ? 257 LYS B CE  1 
ATOM   4155 N  NZ  . LYS B 1 257 ? -31.659 3.684   -24.263 1.00 29.26 ? 257 LYS B NZ  1 
ATOM   4156 N  N   . VAL B 1 258 ? -31.066 8.255   -18.330 1.00 17.93 ? 258 VAL B N   1 
ATOM   4157 C  CA  . VAL B 1 258 ? -29.734 8.355   -17.631 1.00 16.55 ? 258 VAL B CA  1 
ATOM   4158 C  C   . VAL B 1 258 ? -29.090 7.004   -17.764 1.00 17.41 ? 258 VAL B C   1 
ATOM   4159 O  O   . VAL B 1 258 ? -29.674 5.939   -17.366 1.00 19.26 ? 258 VAL B O   1 
ATOM   4160 C  CB  . VAL B 1 258 ? -29.845 8.714   -16.155 1.00 18.20 ? 258 VAL B CB  1 
ATOM   4161 C  CG1 . VAL B 1 258 ? -28.453 8.887   -15.562 1.00 18.13 ? 258 VAL B CG1 1 
ATOM   4162 C  CG2 . VAL B 1 258 ? -30.663 9.992   -16.044 1.00 20.09 ? 258 VAL B CG2 1 
ATOM   4163 N  N   . ARG B 1 259 ? -27.886 6.996   -18.306 1.00 17.34 ? 259 ARG B N   1 
ATOM   4164 C  CA  . ARG B 1 259 ? -27.218 5.726   -18.531 1.00 15.72 ? 259 ARG B CA  1 
ATOM   4165 C  C   . ARG B 1 259 ? -26.012 5.551   -17.553 1.00 16.18 ? 259 ARG B C   1 
ATOM   4166 O  O   . ARG B 1 259 ? -25.419 6.552   -17.192 1.00 18.08 ? 259 ARG B O   1 
ATOM   4167 C  CB  . ARG B 1 259 ? -26.710 5.675   -19.971 1.00 15.02 ? 259 ARG B CB  1 
ATOM   4168 C  CG  . ARG B 1 259 ? -27.890 5.616   -20.966 1.00 16.29 ? 259 ARG B CG  1 
ATOM   4169 C  CD  . ARG B 1 259 ? -27.381 5.579   -22.423 1.00 16.93 ? 259 ARG B CD  1 
ATOM   4170 N  NE  . ARG B 1 259 ? -26.762 6.822   -22.810 1.00 16.50 ? 259 ARG B NE  1 
ATOM   4171 C  CZ  . ARG B 1 259 ? -25.817 6.914   -23.745 1.00 15.98 ? 259 ARG B CZ  1 
ATOM   4172 N  NH1 . ARG B 1 259 ? -25.417 5.806   -24.433 1.00 17.53 ? 259 ARG B NH1 1 
ATOM   4173 N  NH2 . ARG B 1 259 ? -25.344 8.113   -24.088 1.00 15.61 ? 259 ARG B NH2 1 
ATOM   4174 N  N   . ALA B 1 260 ? -25.599 4.310   -17.264 1.00 16.71 ? 260 ALA B N   1 
ATOM   4175 C  CA  . ALA B 1 260 ? -24.410 4.020   -16.418 1.00 17.44 ? 260 ALA B CA  1 
ATOM   4176 C  C   . ALA B 1 260 ? -23.428 3.334   -17.262 1.00 21.72 ? 260 ALA B C   1 
ATOM   4177 O  O   . ALA B 1 260 ? -23.771 2.445   -18.119 1.00 19.01 ? 260 ALA B O   1 
ATOM   4178 C  CB  . ALA B 1 260 ? -24.787 3.147   -15.226 1.00 19.09 ? 260 ALA B CB  1 
ATOM   4179 N  N   . SER B 1 261 ? -22.168 3.700   -17.047 1.00 18.03 ? 261 SER B N   1 
ATOM   4180 C  CA  . SER B 1 261 ? -21.047 3.025   -17.664 1.00 19.44 ? 261 SER B CA  1 
ATOM   4181 C  C   . SER B 1 261 ? -20.660 1.733   -16.978 1.00 18.18 ? 261 SER B C   1 
ATOM   4182 O  O   . SER B 1 261 ? -19.665 1.070   -17.389 1.00 18.75 ? 261 SER B O   1 
ATOM   4183 C  CB  . SER B 1 261 ? -19.852 3.982   -17.689 1.00 18.73 ? 261 SER B CB  1 
ATOM   4184 O  OG  . SER B 1 261 ? -19.198 4.050   -16.411 1.00 17.24 ? 261 SER B OG  1 
ATOM   4185 N  N   . PHE B 1 262 ? -21.337 1.395   -15.895 1.00 17.97 ? 262 PHE B N   1 
ATOM   4186 C  CA  . PHE B 1 262 ? -20.887 0.302   -15.058 1.00 20.67 ? 262 PHE B CA  1 
ATOM   4187 C  C   . PHE B 1 262 ? -22.127 -0.361  -14.478 1.00 22.23 ? 262 PHE B C   1 
ATOM   4188 O  O   . PHE B 1 262 ? -23.219 0.219   -14.483 1.00 22.05 ? 262 PHE B O   1 
ATOM   4189 C  CB  . PHE B 1 262 ? -20.036 0.783   -13.913 1.00 21.43 ? 262 PHE B CB  1 
ATOM   4190 C  CG  . PHE B 1 262 ? -20.792 1.766   -13.016 1.00 21.03 ? 262 PHE B CG  1 
ATOM   4191 C  CD1 . PHE B 1 262 ? -21.352 1.324   -11.830 1.00 22.27 ? 262 PHE B CD1 1 
ATOM   4192 C  CD2 . PHE B 1 262 ? -21.026 3.120   -13.424 1.00 19.17 ? 262 PHE B CD2 1 
ATOM   4193 C  CE1 . PHE B 1 262 ? -22.113 2.184   -11.013 1.00 25.54 ? 262 PHE B CE1 1 
ATOM   4194 C  CE2 . PHE B 1 262 ? -21.754 3.977   -12.627 1.00 19.88 ? 262 PHE B CE2 1 
ATOM   4195 C  CZ  . PHE B 1 262 ? -22.326 3.537   -11.416 1.00 21.96 ? 262 PHE B CZ  1 
ATOM   4196 N  N   . HIS B 1 263 ? -21.933 -1.586  -13.957 1.00 25.38 ? 263 HIS B N   1 
ATOM   4197 C  CA  . HIS B 1 263 ? -23.028 -2.323  -13.229 1.00 31.02 ? 263 HIS B CA  1 
ATOM   4198 C  C   . HIS B 1 263 ? -22.424 -3.259  -12.213 1.00 38.20 ? 263 HIS B C   1 
ATOM   4199 O  O   . HIS B 1 263 ? -23.144 -3.855  -11.397 1.00 43.46 ? 263 HIS B O   1 
ATOM   4200 C  CB  . HIS B 1 263 ? -24.020 -3.055  -14.158 1.00 34.39 ? 263 HIS B CB  1 
ATOM   4201 C  CG  . HIS B 1 263 ? -23.414 -4.109  -15.089 1.00 39.74 ? 263 HIS B CG  1 
ATOM   4202 N  ND1 . HIS B 1 263 ? -22.091 -4.201  -15.377 1.00 43.75 ? 263 HIS B ND1 1 
ATOM   4203 C  CD2 . HIS B 1 263 ? -24.048 -5.089  -15.884 1.00 39.51 ? 263 HIS B CD2 1 
ATOM   4204 C  CE1 . HIS B 1 263 ? -21.879 -5.211  -16.260 1.00 39.47 ? 263 HIS B CE1 1 
ATOM   4205 N  NE2 . HIS B 1 263 ? -23.079 -5.736  -16.584 1.00 45.18 ? 263 HIS B NE2 1 
ATOM   4206 O  OXT . HIS B 1 263 ? -21.194 -3.439  -12.141 1.00 35.83 ? 263 HIS B OXT 1 
HETATM 4207 ZN ZN  . ZN  C 2 .   ? 6.215   -7.043  -27.095 1.00 11.37 ? 301 ZN  A ZN  1 
HETATM 4208 C  C1  . PEG D 3 .   ? -2.186  -23.473 -19.953 1.00 26.23 ? 302 PEG A C1  1 
HETATM 4209 O  O1  . PEG D 3 .   ? -1.773  -24.382 -20.868 1.00 26.79 ? 302 PEG A O1  1 
HETATM 4210 C  C2  . PEG D 3 .   ? -2.302  -23.523 -18.396 1.00 23.76 ? 302 PEG A C2  1 
HETATM 4211 O  O2  . PEG D 3 .   ? -1.281  -23.867 -17.556 1.00 27.94 ? 302 PEG A O2  1 
HETATM 4212 C  C3  . PEG D 3 .   ? -1.066  -24.823 -16.569 1.00 29.40 ? 302 PEG A C3  1 
HETATM 4213 C  C4  . PEG D 3 .   ? -0.005  -25.776 -16.359 1.00 28.73 ? 302 PEG A C4  1 
HETATM 4214 O  O4  . PEG D 3 .   ? 1.173   -26.196 -17.038 1.00 30.87 ? 302 PEG A O4  1 
HETATM 4215 C  C1  . EDO E 4 .   ? -14.323 -0.857  -23.089 1.00 31.67 ? 303 EDO A C1  1 
HETATM 4216 O  O1  . EDO E 4 .   ? -13.083 -1.519  -22.866 1.00 35.17 ? 303 EDO A O1  1 
HETATM 4217 C  C2  . EDO E 4 .   ? -14.817 -0.438  -24.486 1.00 29.39 ? 303 EDO A C2  1 
HETATM 4218 O  O2  . EDO E 4 .   ? -14.368 0.693   -25.165 1.00 26.44 ? 303 EDO A O2  1 
HETATM 4219 C  C1  . EDO F 4 .   ? 1.701   11.459  -29.564 1.00 37.51 ? 304 EDO A C1  1 
HETATM 4220 O  O1  . EDO F 4 .   ? 1.126   10.188  -29.620 1.00 40.70 ? 304 EDO A O1  1 
HETATM 4221 C  C2  . EDO F 4 .   ? 3.156   11.608  -29.057 1.00 34.62 ? 304 EDO A C2  1 
HETATM 4222 O  O2  . EDO F 4 .   ? 3.321   12.608  -28.040 1.00 30.34 ? 304 EDO A O2  1 
HETATM 4223 C  C1  . EDO G 4 .   ? 11.938  14.850  -26.553 1.00 31.81 ? 305 EDO A C1  1 
HETATM 4224 O  O1  . EDO G 4 .   ? 11.077  14.826  -25.394 1.00 26.41 ? 305 EDO A O1  1 
HETATM 4225 C  C2  . EDO G 4 .   ? 11.763  13.898  -27.773 1.00 32.65 ? 305 EDO A C2  1 
HETATM 4226 O  O2  . EDO G 4 .   ? 10.853  14.294  -28.779 1.00 31.66 ? 305 EDO A O2  1 
HETATM 4227 C  C1  . EDO H 4 .   ? 8.477   -13.872 -40.769 1.00 35.03 ? 306 EDO A C1  1 
HETATM 4228 O  O1  . EDO H 4 .   ? 7.081   -14.066 -40.532 1.00 34.83 ? 306 EDO A O1  1 
HETATM 4229 C  C2  . EDO H 4 .   ? 9.091   -12.469 -41.140 1.00 35.03 ? 306 EDO A C2  1 
HETATM 4230 O  O2  . EDO H 4 .   ? 8.316   -11.251 -41.143 1.00 26.64 ? 306 EDO A O2  1 
HETATM 4231 F  F20 . V14 I 5 .   ? 9.177   -7.464  -25.693 1.00 28.39 ? 307 V14 A F20 1 
HETATM 4232 C  C5  . V14 I 5 .   ? 9.112   -7.244  -24.366 1.00 28.93 ? 307 V14 A C5  1 
HETATM 4233 C  C4  . V14 I 5 .   ? 8.010   -7.551  -23.622 1.00 29.58 ? 307 V14 A C4  1 
HETATM 4234 S  S7  . V14 I 5 .   ? 6.716   -8.315  -24.423 1.00 23.20 ? 307 V14 A S7  1 
HETATM 4235 O  O9  . V14 I 5 .   ? 5.671   -7.464  -24.158 1.00 22.41 ? 307 V14 A O9  1 
HETATM 4236 N  N10 . V14 I 5 .   ? 6.807   -8.376  -26.230 1.00 20.64 ? 307 V14 A N10 1 
HETATM 4237 O  O8  . V14 I 5 .   ? 6.191   -9.442  -23.798 1.00 28.25 ? 307 V14 A O8  1 
HETATM 4238 C  C3  . V14 I 5 .   ? 7.852   -7.351  -22.278 1.00 30.79 ? 307 V14 A C3  1 
HETATM 4239 F  F12 . V14 I 5 .   ? 6.651   -7.715  -21.727 1.00 37.86 ? 307 V14 A F12 1 
HETATM 4240 C  C2  . V14 I 5 .   ? 8.900   -6.837  -21.592 1.00 39.29 ? 307 V14 A C2  1 
HETATM 4241 F  F13 . V14 I 5 .   ? 8.752   -6.614  -20.236 1.00 43.35 ? 307 V14 A F13 1 
HETATM 4242 C  C6  . V14 I 5 .   ? 10.186  -6.677  -23.655 1.00 31.75 ? 307 V14 A C6  1 
HETATM 4243 C  C1  . V14 I 5 .   ? 10.020  -6.498  -22.290 1.00 41.15 ? 307 V14 A C1  1 
HETATM 4244 S  S11 . V14 I 5 .   ? 11.372  -5.835  -21.310 1.00 57.25 ? 307 V14 A S11 1 
HETATM 4245 O  O16 . V14 I 5 .   ? 10.753  -4.559  -20.754 1.00 57.51 ? 307 V14 A O16 1 
HETATM 4246 O  O17 . V14 I 5 .   ? 12.169  -5.437  -22.569 1.00 30.48 ? 307 V14 A O17 1 
HETATM 4247 C  C15 . V14 I 5 .   ? 12.312  -6.736  -20.088 1.00 56.07 ? 307 V14 A C15 1 
HETATM 4248 C  C18 . V14 I 5 .   ? 11.453  -7.741  -19.366 1.00 54.30 ? 307 V14 A C18 1 
HETATM 4249 O  O21 . V14 I 5 .   ? 12.225  -8.185  -18.293 1.00 63.26 ? 307 V14 A O21 1 
HETATM 4250 N  N19 . V14 I 5 .   ? 11.327  -6.336  -24.442 1.00 30.83 ? 307 V14 A N19 1 
HETATM 4251 C  C14 . V14 I 5 .   ? 11.915  -6.897  -25.670 1.00 37.12 ? 307 V14 A C14 1 
HETATM 4252 C  C28 . V14 I 5 .   ? 11.565  -6.259  -27.014 1.00 26.44 ? 307 V14 A C28 1 
HETATM 4253 C  C27 . V14 I 5 .   ? 11.602  -4.734  -27.080 1.00 38.11 ? 307 V14 A C27 1 
HETATM 4254 C  C26 . V14 I 5 .   ? 12.983  -4.082  -26.802 1.00 19.55 ? 307 V14 A C26 1 
HETATM 4255 C  C25 . V14 I 5 .   ? 13.419  -3.948  -25.299 1.00 33.99 ? 307 V14 A C25 1 
HETATM 4256 C  C24 . V14 I 5 .   ? 13.377  -5.105  -24.338 1.00 31.88 ? 307 V14 A C24 1 
HETATM 4257 C  C23 . V14 I 5 .   ? 14.340  -6.156  -24.867 1.00 39.48 ? 307 V14 A C23 1 
HETATM 4258 C  C22 . V14 I 5 .   ? 13.471  -7.210  -25.511 1.00 36.31 ? 307 V14 A C22 1 
HETATM 4259 ZN ZN  . ZN  J 2 .   ? -21.243 24.252  -13.168 1.00 13.57 ? 301 ZN  B ZN  1 
HETATM 4260 C  C1  . CIT K 6 .   ? -27.969 26.807  1.072   1.00 39.81 ? 302 CIT B C1  1 
HETATM 4261 O  O1  . CIT K 6 .   ? -26.964 26.400  0.713   1.00 26.60 ? 302 CIT B O1  1 
HETATM 4262 O  O2  . CIT K 6 .   ? -28.146 26.884  2.315   1.00 39.89 ? 302 CIT B O2  1 
HETATM 4263 C  C2  . CIT K 6 .   ? -29.002 27.052  -0.093  1.00 41.25 ? 302 CIT B C2  1 
HETATM 4264 C  C3  . CIT K 6 .   ? -30.078 26.025  0.121   1.00 52.01 ? 302 CIT B C3  1 
HETATM 4265 O  O7  . CIT K 6 .   ? -30.593 26.462  1.298   1.00 60.34 ? 302 CIT B O7  1 
HETATM 4266 C  C4  . CIT K 6 .   ? -31.359 26.143  -0.731  1.00 61.12 ? 302 CIT B C4  1 
HETATM 4267 C  C5  . CIT K 6 .   ? -31.606 24.847  -1.361  1.00 70.84 ? 302 CIT B C5  1 
HETATM 4268 O  O3  . CIT K 6 .   ? -30.769 24.163  -1.782  1.00 59.29 ? 302 CIT B O3  1 
HETATM 4269 O  O4  . CIT K 6 .   ? -32.666 24.440  -1.460  1.00 77.36 ? 302 CIT B O4  1 
HETATM 4270 C  C6  . CIT K 6 .   ? -29.795 24.610  0.482   1.00 48.56 ? 302 CIT B C6  1 
HETATM 4271 O  O5  . CIT K 6 .   ? -28.746 24.201  0.269   1.00 31.03 ? 302 CIT B O5  1 
HETATM 4272 O  O6  . CIT K 6 .   ? -30.591 23.863  0.995   1.00 51.29 ? 302 CIT B O6  1 
HETATM 4273 C  C1  . EDO L 4 .   ? -10.246 1.990   -11.479 1.00 31.16 ? 303 EDO B C1  1 
HETATM 4274 O  O1  . EDO L 4 .   ? -10.412 0.559   -11.608 1.00 34.86 ? 303 EDO B O1  1 
HETATM 4275 C  C2  . EDO L 4 .   ? -9.874  2.363   -10.057 1.00 32.34 ? 303 EDO B C2  1 
HETATM 4276 O  O2  . EDO L 4 .   ? -10.922 2.172   -9.158  1.00 38.13 ? 303 EDO B O2  1 
HETATM 4277 C  C1  . EDO M 4 .   ? -11.733 29.128  -30.715 1.00 44.49 ? 304 EDO B C1  1 
HETATM 4278 O  O1  . EDO M 4 .   ? -10.525 28.454  -30.371 1.00 50.55 ? 304 EDO B O1  1 
HETATM 4279 C  C2  . EDO M 4 .   ? -11.745 30.003  -31.987 1.00 42.88 ? 304 EDO B C2  1 
HETATM 4280 O  O2  . EDO M 4 .   ? -11.897 31.402  -31.783 1.00 39.28 ? 304 EDO B O2  1 
HETATM 4281 C  C1  . EDO N 4 .   ? 4.040   20.749  -21.317 1.00 50.26 ? 305 EDO B C1  1 
HETATM 4282 O  O1  . EDO N 4 .   ? 3.284   20.318  -20.180 1.00 43.98 ? 305 EDO B O1  1 
HETATM 4283 C  C2  . EDO N 4 .   ? 3.378   20.609  -22.710 1.00 40.43 ? 305 EDO B C2  1 
HETATM 4284 O  O2  . EDO N 4 .   ? 2.642   21.707  -23.258 1.00 43.51 ? 305 EDO B O2  1 
HETATM 4285 F  F20 . V14 O 5 .   ? -21.495 27.154  -14.876 1.00 29.07 ? 306 V14 B F20 1 
HETATM 4286 C  C5  . V14 O 5 .   ? -21.110 27.070  -16.157 1.00 36.53 ? 306 V14 B C5  1 
HETATM 4287 C  C4  . V14 O 5 .   ? -21.336 25.874  -16.804 1.00 34.63 ? 306 V14 B C4  1 
HETATM 4288 S  S7  . V14 O 5 .   ? -22.117 24.529  -16.032 1.00 29.25 ? 306 V14 B S7  1 
HETATM 4289 O  O9  . V14 O 5 .   ? -21.126 23.553  -15.817 1.00 27.72 ? 306 V14 B O9  1 
HETATM 4290 N  N10 . V14 O 5 .   ? -22.546 24.685  -14.185 1.00 24.88 ? 306 V14 B N10 1 
HETATM 4291 O  O8  . V14 O 5 .   ? -22.887 23.644  -16.813 1.00 38.95 ? 306 V14 B O8  1 
HETATM 4292 C  C3  . V14 O 5 .   ? -20.958 25.684  -18.084 1.00 36.43 ? 306 V14 B C3  1 
HETATM 4293 F  F12 . V14 O 5 .   ? -21.212 24.451  -18.623 1.00 32.86 ? 306 V14 B F12 1 
HETATM 4294 C  C2  . V14 O 5 .   ? -20.365 26.754  -18.735 1.00 39.30 ? 306 V14 B C2  1 
HETATM 4295 F  F13 . V14 O 5 .   ? -20.011 26.473  -20.007 1.00 37.07 ? 306 V14 B F13 1 
HETATM 4296 C  C6  . V14 O 5 .   ? -20.493 28.188  -16.767 1.00 38.03 ? 306 V14 B C6  1 
HETATM 4297 C  C1  . V14 O 5 .   ? -20.116 27.985  -18.111 1.00 48.96 ? 306 V14 B C1  1 
HETATM 4298 S  S11 . V14 O 5 .   ? -19.307 29.198  -19.182 1.00 65.48 ? 306 V14 B S11 1 
HETATM 4299 O  O16 . V14 O 5 .   ? -20.389 29.249  -20.249 1.00 62.17 ? 306 V14 B O16 1 
HETATM 4300 O  O17 . V14 O 5 .   ? -18.150 28.421  -19.722 1.00 72.19 ? 306 V14 B O17 1 
HETATM 4301 C  C15 . V14 O 5 .   ? -18.692 30.859  -18.898 1.00 72.11 ? 306 V14 B C15 1 
HETATM 4302 C  C18 . V14 O 5 .   ? -19.244 31.407  -17.629 1.00 67.81 ? 306 V14 B C18 1 
HETATM 4303 O  O21 . V14 O 5 .   ? -18.537 30.699  -16.674 1.00 66.43 ? 306 V14 B O21 1 
HETATM 4304 N  N19 . V14 O 5 .   ? -20.342 29.343  -15.900 1.00 40.91 ? 306 V14 B N19 1 
HETATM 4305 C  C14 . V14 O 5 .   ? -21.148 29.687  -14.666 1.00 46.58 ? 306 V14 B C14 1 
HETATM 4306 C  C28 . V14 O 5 .   ? -20.614 29.352  -13.251 1.00 35.64 ? 306 V14 B C28 1 
HETATM 4307 C  C27 . V14 O 5 .   ? -19.125 29.610  -13.058 1.00 47.81 ? 306 V14 B C27 1 
HETATM 4308 C  C26 . V14 O 5 .   ? -18.616 31.077  -12.926 1.00 36.51 ? 306 V14 B C26 1 
HETATM 4309 C  C25 . V14 O 5 .   ? -18.843 32.083  -14.088 1.00 53.35 ? 306 V14 B C25 1 
HETATM 4310 C  C24 . V14 O 5 .   ? -20.152 32.877  -14.186 1.00 53.86 ? 306 V14 B C24 1 
HETATM 4311 C  C23 . V14 O 5 .   ? -21.105 32.259  -15.185 1.00 49.85 ? 306 V14 B C23 1 
HETATM 4312 C  C22 . V14 O 5 .   ? -21.823 31.091  -14.596 1.00 47.68 ? 306 V14 B C22 1 
HETATM 4313 O  O   . HOH P 7 .   ? -20.317 -12.931 -15.488 1.00 44.59 ? 401 HOH A O   1 
HETATM 4314 O  O   . HOH P 7 .   ? 4.014   -24.702 -26.120 1.00 34.76 ? 402 HOH A O   1 
HETATM 4315 O  O   . HOH P 7 .   ? 14.423  12.124  -19.437 1.00 22.70 ? 403 HOH A O   1 
HETATM 4316 O  O   . HOH P 7 .   ? 5.032   5.185   -15.101 1.00 16.63 ? 404 HOH A O   1 
HETATM 4317 O  O   . HOH P 7 .   ? 8.754   7.788   -9.246  1.00 35.14 ? 405 HOH A O   1 
HETATM 4318 O  O   . HOH P 7 .   ? -15.418 -3.494  -23.863 1.00 32.34 ? 406 HOH A O   1 
HETATM 4319 O  O   . HOH P 7 .   ? -3.397  10.731  -42.230 1.00 38.13 ? 407 HOH A O   1 
HETATM 4320 O  O   . HOH P 7 .   ? 20.520  -25.952 -24.658 1.00 31.56 ? 408 HOH A O   1 
HETATM 4321 O  O   . HOH P 7 .   ? -13.581 -4.411  -19.129 1.00 24.84 ? 409 HOH A O   1 
HETATM 4322 O  O   . HOH P 7 .   ? 1.623   -29.462 -18.447 1.00 37.14 ? 410 HOH A O   1 
HETATM 4323 O  O   . HOH P 7 .   ? 6.527   -0.727  -44.989 1.00 20.82 ? 411 HOH A O   1 
HETATM 4324 O  O   . HOH P 7 .   ? 3.230   17.272  -21.117 1.00 40.90 ? 412 HOH A O   1 
HETATM 4325 O  O   . HOH P 7 .   ? -7.529  7.168   -31.027 1.00 46.90 ? 413 HOH A O   1 
HETATM 4326 O  O   . HOH P 7 .   ? 15.719  -26.571 -24.265 1.00 35.90 ? 414 HOH A O   1 
HETATM 4327 O  O   . HOH P 7 .   ? 1.889   15.125  -13.252 1.00 34.83 ? 415 HOH A O   1 
HETATM 4328 O  O   . HOH P 7 .   ? -1.810  -21.288 -32.899 1.00 21.82 ? 416 HOH A O   1 
HETATM 4329 O  O   . HOH P 7 .   ? -12.456 -24.170 -35.668 1.00 38.21 ? 417 HOH A O   1 
HETATM 4330 O  O   . HOH P 7 .   ? 9.199   11.428  -38.363 1.00 28.67 ? 418 HOH A O   1 
HETATM 4331 O  O   . HOH P 7 .   ? -1.540  4.291   -46.445 1.00 24.68 ? 419 HOH A O   1 
HETATM 4332 O  O   . HOH P 7 .   ? 13.705  2.060   -43.779 1.00 37.82 ? 420 HOH A O   1 
HETATM 4333 O  O   . HOH P 7 .   ? 8.853   15.059  -32.656 1.00 34.83 ? 421 HOH A O   1 
HETATM 4334 O  O   . HOH P 7 .   ? -8.120  7.794   -20.036 1.00 19.87 ? 422 HOH A O   1 
HETATM 4335 O  O   . HOH P 7 .   ? -10.126 5.330   -13.232 1.00 25.55 ? 423 HOH A O   1 
HETATM 4336 O  O   . HOH P 7 .   ? 1.589   -1.807  -47.895 1.00 33.37 ? 424 HOH A O   1 
HETATM 4337 O  O   . HOH P 7 .   ? 0.813   -16.817 -17.327 1.00 23.67 ? 425 HOH A O   1 
HETATM 4338 O  O   . HOH P 7 .   ? 3.950   -9.323  -2.087  1.00 21.25 ? 426 HOH A O   1 
HETATM 4339 O  O   . HOH P 7 .   ? -13.783 -1.462  -20.381 1.00 25.11 ? 427 HOH A O   1 
HETATM 4340 O  O   . HOH P 7 .   ? -3.458  11.570  -20.628 1.00 17.70 ? 428 HOH A O   1 
HETATM 4341 O  O   . HOH P 7 .   ? 6.531   8.564   -42.959 1.00 25.43 ? 429 HOH A O   1 
HETATM 4342 O  O   . HOH P 7 .   ? 5.044   8.996   -13.412 1.00 30.39 ? 430 HOH A O   1 
HETATM 4343 O  O   . HOH P 7 .   ? -5.983  9.396   -30.871 1.00 29.16 ? 431 HOH A O   1 
HETATM 4344 O  O   . HOH P 7 .   ? 1.312   15.929  -17.089 1.00 24.37 ? 432 HOH A O   1 
HETATM 4345 O  O   . HOH P 7 .   ? 9.059   -11.195 -29.956 1.00 12.40 ? 433 HOH A O   1 
HETATM 4346 O  O   . HOH P 7 .   ? -1.732  11.243  -22.905 1.00 30.08 ? 434 HOH A O   1 
HETATM 4347 O  O   . HOH P 7 .   ? 5.327   -11.183 -47.151 1.00 28.28 ? 435 HOH A O   1 
HETATM 4348 O  O   . HOH P 7 .   ? -6.623  0.733   -43.455 1.00 38.24 ? 436 HOH A O   1 
HETATM 4349 O  O   . HOH P 7 .   ? 8.357   -14.622 -36.755 1.00 33.02 ? 437 HOH A O   1 
HETATM 4350 O  O   . HOH P 7 .   ? -13.168 3.154   -25.663 1.00 30.45 ? 438 HOH A O   1 
HETATM 4351 O  O   . HOH P 7 .   ? 0.959   -21.872 -32.678 1.00 26.66 ? 439 HOH A O   1 
HETATM 4352 O  O   . HOH P 7 .   ? 26.206  -1.873  -36.267 1.00 29.12 ? 440 HOH A O   1 
HETATM 4353 O  O   . HOH P 7 .   ? -13.354 -20.263 -24.660 1.00 41.34 ? 441 HOH A O   1 
HETATM 4354 O  O   . HOH P 7 .   ? 3.610   6.417   -13.087 1.00 17.55 ? 442 HOH A O   1 
HETATM 4355 O  O   . HOH P 7 .   ? 14.469  3.541   -23.161 1.00 19.63 ? 443 HOH A O   1 
HETATM 4356 O  O   . HOH P 7 .   ? 3.731   17.630  -37.264 1.00 23.84 ? 444 HOH A O   1 
HETATM 4357 O  O   . HOH P 7 .   ? -1.272  13.658  -14.437 1.00 22.05 ? 445 HOH A O   1 
HETATM 4358 O  O   . HOH P 7 .   ? 3.794   -13.461 -35.143 1.00 18.47 ? 446 HOH A O   1 
HETATM 4359 O  O   . HOH P 7 .   ? -8.474  -4.290  -7.534  1.00 31.87 ? 447 HOH A O   1 
HETATM 4360 O  O   . HOH P 7 .   ? 14.982  0.135   -22.064 1.00 39.96 ? 448 HOH A O   1 
HETATM 4361 O  O   . HOH P 7 .   ? 25.916  1.519   -29.997 1.00 31.64 ? 449 HOH A O   1 
HETATM 4362 O  O   . HOH P 7 .   ? 12.240  2.212   -13.462 1.00 33.77 ? 450 HOH A O   1 
HETATM 4363 O  O   . HOH P 7 .   ? 12.255  -1.321  -21.267 1.00 33.76 ? 451 HOH A O   1 
HETATM 4364 O  O   . HOH P 7 .   ? -4.905  -0.355  -5.898  1.00 28.95 ? 452 HOH A O   1 
HETATM 4365 O  O   . HOH P 7 .   ? 0.328   1.051   -10.063 1.00 15.42 ? 453 HOH A O   1 
HETATM 4366 O  O   . HOH P 7 .   ? -7.609  -10.343 -11.274 1.00 28.47 ? 454 HOH A O   1 
HETATM 4367 O  O   . HOH P 7 .   ? -9.618  0.986   -36.668 1.00 27.50 ? 455 HOH A O   1 
HETATM 4368 O  O   . HOH P 7 .   ? 12.447  -18.499 -18.574 1.00 25.66 ? 456 HOH A O   1 
HETATM 4369 O  O   . HOH P 7 .   ? 14.310  -6.000  -7.815  1.00 36.93 ? 457 HOH A O   1 
HETATM 4370 O  O   . HOH P 7 .   ? 5.195   -22.800 -27.237 1.00 28.01 ? 458 HOH A O   1 
HETATM 4371 O  O   . HOH P 7 .   ? -6.021  3.596   -14.209 1.00 24.11 ? 459 HOH A O   1 
HETATM 4372 O  O   . HOH P 7 .   ? -0.559  -15.205 -15.560 1.00 22.41 ? 460 HOH A O   1 
HETATM 4373 O  O   . HOH P 7 .   ? 18.322  2.762   -43.626 1.00 38.81 ? 461 HOH A O   1 
HETATM 4374 O  O   . HOH P 7 .   ? -0.339  -11.108 -14.627 1.00 17.30 ? 462 HOH A O   1 
HETATM 4375 O  O   . HOH P 7 .   ? 15.155  -8.997  -38.048 1.00 21.11 ? 463 HOH A O   1 
HETATM 4376 O  O   . HOH P 7 .   ? 5.787   -1.580  -5.124  1.00 17.13 ? 464 HOH A O   1 
HETATM 4377 O  O   . HOH P 7 .   ? -10.872 -2.312  -29.315 1.00 18.78 ? 465 HOH A O   1 
HETATM 4378 O  O   . HOH P 7 .   ? -13.656 -17.821 -35.126 1.00 26.35 ? 466 HOH A O   1 
HETATM 4379 O  O   . HOH P 7 .   ? -4.741  -2.369  -44.366 1.00 39.40 ? 467 HOH A O   1 
HETATM 4380 O  O   . HOH P 7 .   ? 10.627  13.391  -31.326 1.00 25.04 ? 468 HOH A O   1 
HETATM 4381 O  O   . HOH P 7 .   ? -2.439  -8.803  -44.009 1.00 46.12 ? 469 HOH A O   1 
HETATM 4382 O  O   . HOH P 7 .   ? 12.102  -21.937 -29.478 1.00 27.88 ? 470 HOH A O   1 
HETATM 4383 O  O   . HOH P 7 .   ? 5.654   9.567   -38.594 1.00 20.60 ? 471 HOH A O   1 
HETATM 4384 O  O   . HOH P 7 .   ? -13.675 -18.340 -23.433 1.00 35.71 ? 472 HOH A O   1 
HETATM 4385 O  O   . HOH P 7 .   ? 1.022   0.713   -6.345  1.00 16.12 ? 473 HOH A O   1 
HETATM 4386 O  O   . HOH P 7 .   ? 11.355  -7.437  -29.781 1.00 20.77 ? 474 HOH A O   1 
HETATM 4387 O  O   . HOH P 7 .   ? 10.446  -11.990 -36.777 1.00 17.82 ? 475 HOH A O   1 
HETATM 4388 O  O   . HOH P 7 .   ? 16.396  11.279  -34.754 1.00 32.52 ? 476 HOH A O   1 
HETATM 4389 O  O   . HOH P 7 .   ? -2.312  10.689  -10.599 1.00 26.30 ? 477 HOH A O   1 
HETATM 4390 O  O   . HOH P 7 .   ? -16.352 0.566   -28.054 1.00 37.69 ? 478 HOH A O   1 
HETATM 4391 O  O   . HOH P 7 .   ? -10.819 -5.545  -12.522 1.00 22.78 ? 479 HOH A O   1 
HETATM 4392 O  O   . HOH P 7 .   ? -2.144  -14.209 -40.995 1.00 28.35 ? 480 HOH A O   1 
HETATM 4393 O  O   . HOH P 7 .   ? 0.731   -6.033  -1.091  1.00 33.54 ? 481 HOH A O   1 
HETATM 4394 O  O   . HOH P 7 .   ? 9.536   0.324   -6.118  1.00 20.17 ? 482 HOH A O   1 
HETATM 4395 O  O   . HOH P 7 .   ? -5.740  -3.225  -31.403 1.00 14.08 ? 483 HOH A O   1 
HETATM 4396 O  O   . HOH P 7 .   ? -7.658  -3.096  -11.023 1.00 21.28 ? 484 HOH A O   1 
HETATM 4397 O  O   . HOH P 7 .   ? -3.180  -10.384 -7.716  1.00 27.60 ? 485 HOH A O   1 
HETATM 4398 O  O   . HOH P 7 .   ? 5.324   -5.429  -40.943 1.00 13.42 ? 486 HOH A O   1 
HETATM 4399 O  O   . HOH P 7 .   ? -8.744  -15.174 -19.901 1.00 35.43 ? 487 HOH A O   1 
HETATM 4400 O  O   . HOH P 7 .   ? -3.000  -13.810 -16.277 1.00 25.33 ? 488 HOH A O   1 
HETATM 4401 O  O   . HOH P 7 .   ? 8.743   15.408  -18.066 1.00 43.46 ? 489 HOH A O   1 
HETATM 4402 O  O   . HOH P 7 .   ? -9.777  -25.591 -22.318 1.00 43.17 ? 490 HOH A O   1 
HETATM 4403 O  O   . HOH P 7 .   ? 15.527  13.601  -27.796 1.00 31.98 ? 491 HOH A O   1 
HETATM 4404 O  O   . HOH P 7 .   ? -2.087  1.428   -4.592  1.00 35.60 ? 492 HOH A O   1 
HETATM 4405 O  O   . HOH P 7 .   ? -3.098  3.663   -8.722  1.00 26.66 ? 493 HOH A O   1 
HETATM 4406 O  O   . HOH P 7 .   ? -4.319  -9.110  -11.564 1.00 18.51 ? 494 HOH A O   1 
HETATM 4407 O  O   . HOH P 7 .   ? 20.596  2.990   -23.782 1.00 32.14 ? 495 HOH A O   1 
HETATM 4408 O  O   . HOH P 7 .   ? 18.840  13.282  -25.442 1.00 31.42 ? 496 HOH A O   1 
HETATM 4409 O  O   . HOH P 7 .   ? 6.178   -20.825 -15.830 1.00 22.15 ? 497 HOH A O   1 
HETATM 4410 O  O   . HOH P 7 .   ? -17.531 -7.098  -18.555 1.00 27.73 ? 498 HOH A O   1 
HETATM 4411 O  O   . HOH P 7 .   ? -2.628  -20.167 -30.421 1.00 18.85 ? 499 HOH A O   1 
HETATM 4412 O  O   . HOH P 7 .   ? -6.776  4.892   -43.257 1.00 36.10 ? 500 HOH A O   1 
HETATM 4413 O  O   . HOH P 7 .   ? 16.767  -0.433  -23.990 1.00 35.05 ? 501 HOH A O   1 
HETATM 4414 O  O   . HOH P 7 .   ? 18.564  -8.314  -41.023 1.00 35.76 ? 502 HOH A O   1 
HETATM 4415 O  O   . HOH P 7 .   ? 20.015  -10.276 -27.416 1.00 36.90 ? 503 HOH A O   1 
HETATM 4416 O  O   . HOH P 7 .   ? 9.712   -19.136 -30.255 1.00 21.55 ? 504 HOH A O   1 
HETATM 4417 O  O   . HOH P 7 .   ? -7.200  -13.090 -18.581 1.00 23.95 ? 505 HOH A O   1 
HETATM 4418 O  O   . HOH P 7 .   ? 14.210  9.743   -37.355 1.00 31.33 ? 506 HOH A O   1 
HETATM 4419 O  O   . HOH P 7 .   ? -3.422  -17.933 -38.673 1.00 29.15 ? 507 HOH A O   1 
HETATM 4420 O  O   . HOH P 7 .   ? -6.076  -25.657 -26.341 1.00 32.41 ? 508 HOH A O   1 
HETATM 4421 O  O   . HOH P 7 .   ? -14.598 2.064   -32.781 1.00 44.68 ? 509 HOH A O   1 
HETATM 4422 O  O   . HOH P 7 .   ? -0.761  -18.016 -14.680 1.00 32.10 ? 510 HOH A O   1 
HETATM 4423 O  O   . HOH P 7 .   ? -4.686  -10.740 -13.867 1.00 26.59 ? 511 HOH A O   1 
HETATM 4424 O  O   . HOH P 7 .   ? 1.824   -22.285 -24.630 1.00 19.20 ? 512 HOH A O   1 
HETATM 4425 O  O   . HOH P 7 .   ? 6.834   2.321   -48.051 1.00 27.92 ? 513 HOH A O   1 
HETATM 4426 O  O   . HOH P 7 .   ? -4.120  -4.103  -4.636  1.00 29.81 ? 514 HOH A O   1 
HETATM 4427 O  O   . HOH P 7 .   ? 0.799   3.174   -46.909 1.00 17.70 ? 515 HOH A O   1 
HETATM 4428 O  O   . HOH P 7 .   ? -11.707 6.309   -26.356 1.00 19.13 ? 516 HOH A O   1 
HETATM 4429 O  O   . HOH P 7 .   ? -9.006  -7.560  -34.340 1.00 22.27 ? 517 HOH A O   1 
HETATM 4430 O  O   . HOH P 7 .   ? 14.927  -11.386 -39.507 1.00 29.98 ? 518 HOH A O   1 
HETATM 4431 O  O   . HOH P 7 .   ? 2.027   -11.727 -38.233 1.00 21.18 ? 519 HOH A O   1 
HETATM 4432 O  O   . HOH P 7 .   ? -16.117 -5.414  -20.128 1.00 24.90 ? 520 HOH A O   1 
HETATM 4433 O  O   . HOH P 7 .   ? -3.094  11.030  -38.302 1.00 38.12 ? 521 HOH A O   1 
HETATM 4434 O  O   . HOH P 7 .   ? -1.864  11.160  -13.187 1.00 24.05 ? 522 HOH A O   1 
HETATM 4435 O  O   . HOH P 7 .   ? -5.993  -16.913 -35.583 1.00 22.06 ? 523 HOH A O   1 
HETATM 4436 O  O   . HOH P 7 .   ? -18.316 -5.545  -14.038 1.00 41.91 ? 524 HOH A O   1 
HETATM 4437 O  O   . HOH P 7 .   ? -7.303  6.496   -27.280 1.00 30.22 ? 525 HOH A O   1 
HETATM 4438 O  O   . HOH P 7 .   ? 7.939   9.810   -45.065 1.00 26.91 ? 526 HOH A O   1 
HETATM 4439 O  O   . HOH P 7 .   ? -9.279  -11.886 -14.279 1.00 34.15 ? 527 HOH A O   1 
HETATM 4440 O  O   . HOH P 7 .   ? -8.203  3.344   -34.476 1.00 27.67 ? 528 HOH A O   1 
HETATM 4441 O  O   . HOH P 7 .   ? 17.113  -8.530  -32.283 1.00 19.07 ? 529 HOH A O   1 
HETATM 4442 O  O   . HOH P 7 .   ? 22.995  7.159   -26.467 1.00 26.79 ? 530 HOH A O   1 
HETATM 4443 O  O   . HOH P 7 .   ? 17.061  12.957  -38.569 1.00 45.05 ? 531 HOH A O   1 
HETATM 4444 O  O   . HOH P 7 .   ? 10.893  -1.219  -10.961 1.00 22.05 ? 532 HOH A O   1 
HETATM 4445 O  O   . HOH P 7 .   ? 20.408  -10.522 -33.720 1.00 32.78 ? 533 HOH A O   1 
HETATM 4446 O  O   . HOH P 7 .   ? 20.949  9.440   -29.297 1.00 42.25 ? 534 HOH A O   1 
HETATM 4447 O  O   . HOH P 7 .   ? 12.969  -18.519 -35.892 1.00 31.27 ? 535 HOH A O   1 
HETATM 4448 O  O   . HOH P 7 .   ? -8.968  -23.399 -19.230 1.00 32.65 ? 536 HOH A O   1 
HETATM 4449 O  O   . HOH P 7 .   ? 9.301   10.375  -7.540  1.00 30.88 ? 537 HOH A O   1 
HETATM 4450 O  O   . HOH P 7 .   ? -3.600  6.104   -32.959 1.00 26.11 ? 538 HOH A O   1 
HETATM 4451 O  O   . HOH P 7 .   ? -5.439  5.329   -36.554 1.00 27.29 ? 539 HOH A O   1 
HETATM 4452 O  O   . HOH P 7 .   ? 20.470  -7.156  -30.498 1.00 28.73 ? 540 HOH A O   1 
HETATM 4453 O  O   . HOH P 7 .   ? 20.098  -19.400 -20.717 1.00 45.37 ? 541 HOH A O   1 
HETATM 4454 O  O   . HOH P 7 .   ? -7.317  2.677   -7.643  1.00 32.97 ? 542 HOH A O   1 
HETATM 4455 O  O   . HOH P 7 .   ? -6.033  7.177   -8.481  1.00 28.46 ? 543 HOH A O   1 
HETATM 4456 O  O   . HOH P 7 .   ? -2.782  -7.692  -7.207  1.00 29.51 ? 544 HOH A O   1 
HETATM 4457 O  O   . HOH P 7 .   ? -17.724 -16.301 -19.723 1.00 45.56 ? 545 HOH A O   1 
HETATM 4458 O  O   . HOH P 7 .   ? 23.772  -7.837  -32.165 1.00 44.15 ? 546 HOH A O   1 
HETATM 4459 O  O   . HOH P 7 .   ? -10.302 -18.867 -36.095 1.00 36.47 ? 547 HOH A O   1 
HETATM 4460 O  O   . HOH P 7 .   ? -3.027  6.351   -9.205  1.00 27.21 ? 548 HOH A O   1 
HETATM 4461 O  O   . HOH P 7 .   ? 7.851   -18.551 -16.251 1.00 20.28 ? 549 HOH A O   1 
HETATM 4462 O  O   . HOH P 7 .   ? 14.066  -9.082  -22.503 1.00 37.98 ? 550 HOH A O   1 
HETATM 4463 O  O   . HOH P 7 .   ? -10.867 -19.618 -25.927 1.00 28.20 ? 551 HOH A O   1 
HETATM 4464 O  O   . HOH P 7 .   ? 0.464   0.941   -48.611 1.00 22.39 ? 552 HOH A O   1 
HETATM 4465 O  O   . HOH P 7 .   ? -1.235  -6.525  -42.516 1.00 32.64 ? 553 HOH A O   1 
HETATM 4466 O  O   . HOH P 7 .   ? 13.210  -21.036 -19.764 1.00 25.49 ? 554 HOH A O   1 
HETATM 4467 O  O   . HOH P 7 .   ? 17.888  -9.725  -34.359 1.00 24.92 ? 555 HOH A O   1 
HETATM 4468 O  O   . HOH P 7 .   ? -13.651 4.076   -34.702 1.00 39.69 ? 556 HOH A O   1 
HETATM 4469 O  O   . HOH P 7 .   ? 6.349   -9.795  -42.820 1.00 25.73 ? 557 HOH A O   1 
HETATM 4470 O  O   . HOH P 7 .   ? -3.723  -17.275 -41.605 1.00 27.22 ? 558 HOH A O   1 
HETATM 4471 O  O   . HOH P 7 .   ? -0.434  -12.156 -44.503 1.00 45.12 ? 559 HOH A O   1 
HETATM 4472 O  O   . HOH P 7 .   ? 19.787  -9.753  -31.327 1.00 43.78 ? 560 HOH A O   1 
HETATM 4473 O  O   . HOH P 7 .   ? 3.358   12.400  -32.422 1.00 31.36 ? 561 HOH A O   1 
HETATM 4474 O  O   . HOH P 7 .   ? 18.602  -17.933 -29.636 1.00 42.69 ? 562 HOH A O   1 
HETATM 4475 O  O   . HOH P 7 .   ? -14.722 -11.994 -29.970 1.00 25.57 ? 563 HOH A O   1 
HETATM 4476 O  O   . HOH P 7 .   ? 23.045  9.115   -32.329 1.00 46.09 ? 564 HOH A O   1 
HETATM 4477 O  O   . HOH P 7 .   ? 10.444  -17.293 -12.661 1.00 29.90 ? 565 HOH A O   1 
HETATM 4478 O  O   . HOH P 7 .   ? 5.485   -16.438 -13.181 1.00 30.20 ? 566 HOH A O   1 
HETATM 4479 O  O   . HOH P 7 .   ? -7.138  7.827   -44.700 1.00 35.84 ? 567 HOH A O   1 
HETATM 4480 O  O   . HOH P 7 .   ? 8.826   -25.748 -20.784 1.00 44.09 ? 568 HOH A O   1 
HETATM 4481 O  O   . HOH P 7 .   ? -3.823  -23.899 -29.921 1.00 26.65 ? 569 HOH A O   1 
HETATM 4482 O  O   . HOH P 7 .   ? 7.770   11.887  -13.621 1.00 37.86 ? 570 HOH A O   1 
HETATM 4483 O  O   . HOH P 7 .   ? -2.264  -4.330  -41.889 1.00 24.91 ? 571 HOH A O   1 
HETATM 4484 O  O   . HOH P 7 .   ? -13.385 -2.736  -30.927 1.00 28.17 ? 572 HOH A O   1 
HETATM 4485 O  O   . HOH P 7 .   ? -1.301  12.073  -40.467 1.00 34.69 ? 573 HOH A O   1 
HETATM 4486 O  O   . HOH P 7 .   ? 14.673  12.531  -37.727 1.00 36.75 ? 574 HOH A O   1 
HETATM 4487 O  O   . HOH P 7 .   ? 17.497  -8.569  -36.974 1.00 30.35 ? 575 HOH A O   1 
HETATM 4488 O  O   . HOH P 7 .   ? 17.350  4.509   -37.754 1.00 31.38 ? 576 HOH A O   1 
HETATM 4489 O  O   . HOH P 7 .   ? -1.340  5.688   -5.631  1.00 34.31 ? 577 HOH A O   1 
HETATM 4490 O  O   . HOH P 7 .   ? 6.282   19.024  -35.982 1.00 37.70 ? 578 HOH A O   1 
HETATM 4491 O  O   . HOH P 7 .   ? -14.901 -10.281 -32.438 1.00 31.64 ? 579 HOH A O   1 
HETATM 4492 O  O   . HOH P 7 .   ? 22.278  -14.639 -24.588 1.00 56.19 ? 580 HOH A O   1 
HETATM 4493 O  O   . HOH P 7 .   ? 2.876   4.884   -47.356 1.00 18.15 ? 581 HOH A O   1 
HETATM 4494 O  O   . HOH P 7 .   ? -9.188  2.842   -38.920 1.00 34.61 ? 582 HOH A O   1 
HETATM 4495 O  O   . HOH P 7 .   ? -18.616 -7.641  -31.405 1.00 55.10 ? 583 HOH A O   1 
HETATM 4496 O  O   . HOH P 7 .   ? -20.294 -5.126  -25.271 1.00 38.24 ? 584 HOH A O   1 
HETATM 4497 O  O   . HOH P 7 .   ? 13.301  -2.132  -14.634 1.00 43.94 ? 585 HOH A O   1 
HETATM 4498 O  O   . HOH P 7 .   ? 12.805  -2.928  -12.054 1.00 26.93 ? 586 HOH A O   1 
HETATM 4499 O  O   . HOH P 7 .   ? 8.935   17.264  -25.466 1.00 43.50 ? 587 HOH A O   1 
HETATM 4500 O  O   . HOH P 7 .   ? -12.427 4.071   -16.598 1.00 21.45 ? 588 HOH A O   1 
HETATM 4501 O  O   . HOH P 7 .   ? 5.052   -21.440 -34.026 1.00 36.16 ? 589 HOH A O   1 
HETATM 4502 O  O   . HOH P 7 .   ? -9.973  4.706   -35.806 1.00 34.18 ? 590 HOH A O   1 
HETATM 4503 O  O   . HOH P 7 .   ? -9.578  -18.962 -28.608 1.00 45.35 ? 591 HOH A O   1 
HETATM 4504 O  O   . HOH P 7 .   ? 9.174   -20.417 -32.671 1.00 35.88 ? 592 HOH A O   1 
HETATM 4505 O  O   . HOH P 7 .   ? 10.983  -24.728 -18.498 1.00 39.67 ? 593 HOH A O   1 
HETATM 4506 O  O   . HOH P 7 .   ? -6.632  -12.447 -14.339 1.00 32.12 ? 594 HOH A O   1 
HETATM 4507 O  O   . HOH P 7 .   ? -19.768 -5.289  -29.647 1.00 40.44 ? 595 HOH A O   1 
HETATM 4508 O  O   . HOH P 7 .   ? 1.435   11.935  -39.931 1.00 32.13 ? 596 HOH A O   1 
HETATM 4509 O  O   . HOH P 7 .   ? -4.222  7.556   -38.023 1.00 41.73 ? 597 HOH A O   1 
HETATM 4510 O  O   . HOH P 7 .   ? -4.158  13.245  -42.413 1.00 33.67 ? 598 HOH A O   1 
HETATM 4511 O  O   . HOH P 7 .   ? -16.801 -2.748  -18.779 1.00 39.28 ? 599 HOH A O   1 
HETATM 4512 O  O   . HOH P 7 .   ? 3.074   17.362  -15.018 1.00 40.13 ? 600 HOH A O   1 
HETATM 4513 O  O   . HOH P 7 .   ? -12.392 -10.204 -14.066 1.00 43.94 ? 601 HOH A O   1 
HETATM 4514 O  O   . HOH P 7 .   ? 10.970  0.369   -8.650  1.00 30.43 ? 602 HOH A O   1 
HETATM 4515 O  O   . HOH P 7 .   ? 6.147   15.356  -32.087 1.00 39.15 ? 603 HOH A O   1 
HETATM 4516 O  O   . HOH P 7 .   ? 7.892   -16.920 -14.122 1.00 30.37 ? 604 HOH A O   1 
HETATM 4517 O  O   . HOH P 7 .   ? -4.625  -11.156 -9.735  1.00 28.23 ? 605 HOH A O   1 
HETATM 4518 O  O   . HOH P 7 .   ? 17.689  -12.769 -21.804 1.00 50.43 ? 606 HOH A O   1 
HETATM 4519 O  O   . HOH P 7 .   ? -6.470  0.042   -7.919  1.00 27.10 ? 607 HOH A O   1 
HETATM 4520 O  O   . HOH P 7 .   ? -11.211 -8.409  -35.389 1.00 35.79 ? 608 HOH A O   1 
HETATM 4521 O  O   . HOH P 7 .   ? -13.168 -10.029 -34.421 1.00 40.67 ? 609 HOH A O   1 
HETATM 4522 O  O   . HOH P 7 .   ? -5.721  -14.000 -16.654 1.00 30.73 ? 610 HOH A O   1 
HETATM 4523 O  O   . HOH P 7 .   ? -0.576  -27.959 -28.747 1.00 28.36 ? 611 HOH A O   1 
HETATM 4524 O  O   . HOH P 7 .   ? 26.546  0.960   -37.431 1.00 37.90 ? 612 HOH A O   1 
HETATM 4525 O  O   . HOH P 7 .   ? -11.336 -0.915  -37.444 1.00 30.17 ? 613 HOH A O   1 
HETATM 4526 O  O   . HOH P 7 .   ? -3.555  3.276   -47.493 1.00 39.04 ? 614 HOH A O   1 
HETATM 4527 O  O   . HOH P 7 .   ? 15.926  11.794  -43.215 1.00 42.63 ? 615 HOH A O   1 
HETATM 4528 O  O   . HOH P 7 .   ? -16.114 -0.499  -20.323 1.00 33.89 ? 616 HOH A O   1 
HETATM 4529 O  O   . HOH P 7 .   ? 13.726  -8.030  -4.357  1.00 37.88 ? 617 HOH A O   1 
HETATM 4530 O  O   . HOH P 7 .   ? -6.526  5.406   -33.968 1.00 35.50 ? 618 HOH A O   1 
HETATM 4531 O  O   . HOH P 7 .   ? -2.449  7.551   -6.933  1.00 40.69 ? 619 HOH A O   1 
HETATM 4532 O  O   . HOH P 7 .   ? -25.910 -5.735  -20.339 1.00 44.70 ? 620 HOH A O   1 
HETATM 4533 O  O   . HOH P 7 .   ? 8.006   -23.284 -15.429 1.00 39.55 ? 621 HOH A O   1 
HETATM 4534 O  O   . HOH P 7 .   ? 10.407  -19.613 -16.732 1.00 25.40 ? 622 HOH A O   1 
HETATM 4535 O  O   . HOH P 7 .   ? 10.880  -22.202 -16.350 1.00 29.02 ? 623 HOH A O   1 
HETATM 4536 O  O   . HOH P 7 .   ? -13.660 6.738   -34.348 1.00 39.45 ? 624 HOH A O   1 
HETATM 4537 O  O   . HOH Q 7 .   ? -3.012  21.911  -7.997  1.00 37.03 ? 401 HOH B O   1 
HETATM 4538 O  O   . HOH Q 7 .   ? -26.991 20.517  7.210   1.00 30.68 ? 402 HOH B O   1 
HETATM 4539 O  O   . HOH Q 7 .   ? -31.541 11.770  -6.075  1.00 21.65 ? 403 HOH B O   1 
HETATM 4540 O  O   . HOH Q 7 .   ? -14.259 35.280  -14.496 1.00 41.08 ? 404 HOH B O   1 
HETATM 4541 O  O   . HOH Q 7 .   ? -14.675 11.816  3.635   1.00 43.70 ? 405 HOH B O   1 
HETATM 4542 O  O   . HOH Q 7 .   ? -36.731 23.064  -15.265 1.00 26.71 ? 406 HOH B O   1 
HETATM 4543 O  O   . HOH Q 7 .   ? -17.634 2.193   -9.867  1.00 32.93 ? 407 HOH B O   1 
HETATM 4544 O  O   . HOH Q 7 .   ? -31.331 23.267  -4.054  1.00 29.89 ? 408 HOH B O   1 
HETATM 4545 O  O   . HOH Q 7 .   ? -39.582 24.064  -14.755 1.00 40.05 ? 409 HOH B O   1 
HETATM 4546 O  O   . HOH Q 7 .   ? -29.533 0.306   -11.843 1.00 40.96 ? 410 HOH B O   1 
HETATM 4547 O  O   . HOH Q 7 .   ? 0.552   16.511  -9.618  1.00 33.89 ? 411 HOH B O   1 
HETATM 4548 O  O   . HOH Q 7 .   ? -21.728 14.776  -32.708 1.00 30.77 ? 412 HOH B O   1 
HETATM 4549 O  O   . HOH Q 7 .   ? -27.491 20.294  -2.944  1.00 22.94 ? 413 HOH B O   1 
HETATM 4550 O  O   . HOH Q 7 .   ? -8.178  30.256  -24.782 1.00 28.70 ? 414 HOH B O   1 
HETATM 4551 O  O   . HOH Q 7 .   ? 0.626   18.425  -24.037 1.00 32.82 ? 415 HOH B O   1 
HETATM 4552 O  O   . HOH Q 7 .   ? -12.702 30.238  -20.155 1.00 39.59 ? 416 HOH B O   1 
HETATM 4553 O  O   . HOH Q 7 .   ? -4.431  26.134  4.760   1.00 41.73 ? 417 HOH B O   1 
HETATM 4554 O  O   . HOH Q 7 .   ? -26.942 5.507   -4.234  1.00 38.14 ? 418 HOH B O   1 
HETATM 4555 O  O   . HOH Q 7 .   ? -33.512 20.168  -25.776 1.00 30.33 ? 419 HOH B O   1 
HETATM 4556 O  O   . HOH Q 7 .   ? 1.981   19.356  -12.651 1.00 37.27 ? 420 HOH B O   1 
HETATM 4557 O  O   . HOH Q 7 .   ? 0.297   19.152  -9.021  1.00 43.03 ? 421 HOH B O   1 
HETATM 4558 O  O   . HOH Q 7 .   ? -14.659 13.500  -34.654 1.00 34.97 ? 422 HOH B O   1 
HETATM 4559 O  O   . HOH Q 7 .   ? -8.395  14.715  -5.699  1.00 19.98 ? 423 HOH B O   1 
HETATM 4560 O  O   . HOH Q 7 .   ? -29.322 -2.107  -19.455 1.00 43.65 ? 424 HOH B O   1 
HETATM 4561 O  O   . HOH Q 7 .   ? -9.645  29.994  -27.994 1.00 40.32 ? 425 HOH B O   1 
HETATM 4562 O  O   . HOH Q 7 .   ? -11.530 28.269  6.005   1.00 25.05 ? 426 HOH B O   1 
HETATM 4563 O  O   . HOH Q 7 .   ? -29.323 20.562  -6.843  1.00 20.38 ? 427 HOH B O   1 
HETATM 4564 O  O   . HOH Q 7 .   ? -25.908 26.794  -10.893 1.00 15.17 ? 428 HOH B O   1 
HETATM 4565 O  O   . HOH Q 7 .   ? -26.489 7.865   -2.614  1.00 36.29 ? 429 HOH B O   1 
HETATM 4566 O  O   . HOH Q 7 .   ? -35.104 2.749   -16.171 1.00 47.23 ? 430 HOH B O   1 
HETATM 4567 O  O   . HOH Q 7 .   ? -36.854 15.620  -22.246 1.00 31.51 ? 431 HOH B O   1 
HETATM 4568 O  O   . HOH Q 7 .   ? -21.211 28.175  6.114   1.00 15.86 ? 432 HOH B O   1 
HETATM 4569 O  O   . HOH Q 7 .   ? -10.410 32.980  -15.187 1.00 27.70 ? 433 HOH B O   1 
HETATM 4570 O  O   . HOH Q 7 .   ? -14.067 37.555  1.940   1.00 33.77 ? 434 HOH B O   1 
HETATM 4571 O  O   . HOH Q 7 .   ? -17.105 24.027  4.752   1.00 20.79 ? 435 HOH B O   1 
HETATM 4572 O  O   . HOH Q 7 .   ? -11.214 13.214  -32.875 1.00 37.40 ? 436 HOH B O   1 
HETATM 4573 O  O   . HOH Q 7 .   ? -36.818 9.222   -17.633 1.00 30.91 ? 437 HOH B O   1 
HETATM 4574 O  O   . HOH Q 7 .   ? -0.346  27.442  -3.445  1.00 44.76 ? 438 HOH B O   1 
HETATM 4575 O  O   . HOH Q 7 .   ? -5.781  27.991  1.335   1.00 31.39 ? 439 HOH B O   1 
HETATM 4576 O  O   . HOH Q 7 .   ? -17.094 -0.223  -22.950 1.00 37.63 ? 440 HOH B O   1 
HETATM 4577 O  O   . HOH Q 7 .   ? -3.512  24.290  -23.497 1.00 24.53 ? 441 HOH B O   1 
HETATM 4578 O  O   . HOH Q 7 .   ? -23.097 17.596  -26.088 1.00 16.17 ? 442 HOH B O   1 
HETATM 4579 O  O   . HOH Q 7 .   ? -6.268  24.598  -32.764 1.00 27.19 ? 443 HOH B O   1 
HETATM 4580 O  O   . HOH Q 7 .   ? -38.288 21.564  -16.944 1.00 30.20 ? 444 HOH B O   1 
HETATM 4581 O  O   . HOH Q 7 .   ? -7.647  22.272  5.677   1.00 19.62 ? 445 HOH B O   1 
HETATM 4582 O  O   . HOH Q 7 .   ? -23.702 17.912  8.208   1.00 36.13 ? 446 HOH B O   1 
HETATM 4583 O  O   . HOH Q 7 .   ? -36.360 22.057  -24.255 1.00 28.50 ? 447 HOH B O   1 
HETATM 4584 O  O   . HOH Q 7 .   ? -17.683 12.324  -8.436  1.00 13.07 ? 448 HOH B O   1 
HETATM 4585 O  O   . HOH Q 7 .   ? -9.636  17.201  7.145   1.00 34.22 ? 449 HOH B O   1 
HETATM 4586 O  O   . HOH Q 7 .   ? -36.413 29.436  -12.939 1.00 27.79 ? 450 HOH B O   1 
HETATM 4587 O  O   . HOH Q 7 .   ? -14.860 10.392  -28.294 1.00 20.17 ? 451 HOH B O   1 
HETATM 4588 O  O   . HOH Q 7 .   ? -38.610 11.399  -16.729 1.00 31.41 ? 452 HOH B O   1 
HETATM 4589 O  O   . HOH Q 7 .   ? -31.246 30.647  -23.190 1.00 27.50 ? 453 HOH B O   1 
HETATM 4590 O  O   . HOH Q 7 .   ? -15.249 31.373  4.901   1.00 29.84 ? 454 HOH B O   1 
HETATM 4591 O  O   . HOH Q 7 .   ? -0.267  27.725  -23.757 1.00 36.63 ? 455 HOH B O   1 
HETATM 4592 O  O   . HOH Q 7 .   ? -21.980 10.323  -29.202 1.00 23.87 ? 456 HOH B O   1 
HETATM 4593 O  O   . HOH Q 7 .   ? 2.520   26.690  -17.171 1.00 34.95 ? 457 HOH B O   1 
HETATM 4594 O  O   . HOH Q 7 .   ? -14.854 30.598  -17.863 1.00 39.37 ? 458 HOH B O   1 
HETATM 4595 O  O   . HOH Q 7 .   ? -12.103 5.080   -24.065 1.00 19.26 ? 459 HOH B O   1 
HETATM 4596 O  O   . HOH Q 7 .   ? -10.740 18.509  -28.899 1.00 16.95 ? 460 HOH B O   1 
HETATM 4597 O  O   . HOH Q 7 .   ? -6.032  39.591  -8.455  1.00 38.91 ? 461 HOH B O   1 
HETATM 4598 O  O   . HOH Q 7 .   ? -23.364 27.015  -33.572 1.00 29.62 ? 462 HOH B O   1 
HETATM 4599 O  O   . HOH Q 7 .   ? -9.307  7.930   -26.807 1.00 28.57 ? 463 HOH B O   1 
HETATM 4600 O  O   . HOH Q 7 .   ? -22.153 8.894   -6.100  1.00 20.53 ? 464 HOH B O   1 
HETATM 4601 O  O   . HOH Q 7 .   ? -13.792 1.452   -10.293 1.00 30.29 ? 465 HOH B O   1 
HETATM 4602 O  O   . HOH Q 7 .   ? -32.129 13.174  0.962   1.00 24.06 ? 466 HOH B O   1 
HETATM 4603 O  O   . HOH Q 7 .   ? -6.062  22.234  -25.087 1.00 22.19 ? 467 HOH B O   1 
HETATM 4604 O  O   . HOH Q 7 .   ? -19.627 1.145   -8.390  1.00 31.08 ? 468 HOH B O   1 
HETATM 4605 O  O   . HOH Q 7 .   ? -27.117 3.337   -26.678 1.00 34.68 ? 469 HOH B O   1 
HETATM 4606 O  O   . HOH Q 7 .   ? -30.498 25.988  -4.706  1.00 31.31 ? 470 HOH B O   1 
HETATM 4607 O  O   . HOH Q 7 .   ? -20.601 21.897  -37.735 1.00 24.70 ? 471 HOH B O   1 
HETATM 4608 O  O   . HOH Q 7 .   ? -40.153 29.647  -18.865 1.00 42.90 ? 472 HOH B O   1 
HETATM 4609 O  O   . HOH Q 7 .   ? -28.191 9.087   -21.867 1.00 16.57 ? 473 HOH B O   1 
HETATM 4610 O  O   . HOH Q 7 .   ? -32.530 4.286   -6.989  1.00 21.01 ? 474 HOH B O   1 
HETATM 4611 O  O   . HOH Q 7 .   ? -16.472 7.176   -10.345 1.00 16.55 ? 475 HOH B O   1 
HETATM 4612 O  O   . HOH Q 7 .   ? -1.664  28.828  -5.596  1.00 33.83 ? 476 HOH B O   1 
HETATM 4613 O  O   . HOH Q 7 .   ? -21.425 23.087  0.712   1.00 13.36 ? 477 HOH B O   1 
HETATM 4614 O  O   . HOH Q 7 .   ? -3.429  20.953  -31.116 1.00 36.67 ? 478 HOH B O   1 
HETATM 4615 O  O   . HOH Q 7 .   ? -22.879 16.432  1.929   1.00 28.54 ? 479 HOH B O   1 
HETATM 4616 O  O   . HOH Q 7 .   ? -15.264 9.412   -31.875 1.00 36.03 ? 480 HOH B O   1 
HETATM 4617 O  O   . HOH Q 7 .   ? -25.299 32.736  -2.252  1.00 21.49 ? 481 HOH B O   1 
HETATM 4618 O  O   . HOH Q 7 .   ? -0.487  18.623  -4.492  1.00 37.91 ? 482 HOH B O   1 
HETATM 4619 O  O   . HOH Q 7 .   ? -4.414  34.979  -2.618  1.00 29.69 ? 483 HOH B O   1 
HETATM 4620 O  O   . HOH Q 7 .   ? -8.328  12.065  -24.398 1.00 23.49 ? 484 HOH B O   1 
HETATM 4621 O  O   . HOH Q 7 .   ? -1.501  16.120  -21.044 1.00 20.29 ? 485 HOH B O   1 
HETATM 4622 O  O   . HOH Q 7 .   ? -29.250 18.554  -24.207 1.00 18.39 ? 486 HOH B O   1 
HETATM 4623 O  O   . HOH Q 7 .   ? -34.348 15.442  -11.266 1.00 21.84 ? 487 HOH B O   1 
HETATM 4624 O  O   . HOH Q 7 .   ? -3.394  17.345  -15.520 1.00 19.51 ? 488 HOH B O   1 
HETATM 4625 O  O   . HOH Q 7 .   ? -7.260  28.102  -32.194 1.00 27.37 ? 489 HOH B O   1 
HETATM 4626 O  O   . HOH Q 7 .   ? -10.413 19.154  -32.898 1.00 22.51 ? 490 HOH B O   1 
HETATM 4627 O  O   . HOH Q 7 .   ? -24.631 35.683  -17.576 1.00 52.20 ? 491 HOH B O   1 
HETATM 4628 O  O   . HOH Q 7 .   ? -6.527  32.666  -0.082  1.00 28.49 ? 492 HOH B O   1 
HETATM 4629 O  O   . HOH Q 7 .   ? -22.439 38.418  -9.564  1.00 27.58 ? 493 HOH B O   1 
HETATM 4630 O  O   . HOH Q 7 .   ? 4.477   33.822  -18.679 1.00 25.16 ? 494 HOH B O   1 
HETATM 4631 O  O   . HOH Q 7 .   ? -39.515 4.002   -12.081 1.00 43.46 ? 495 HOH B O   1 
HETATM 4632 O  O   . HOH Q 7 .   ? -0.542  21.772  -1.921  1.00 31.62 ? 496 HOH B O   1 
HETATM 4633 O  O   . HOH Q 7 .   ? -34.169 30.542  -6.113  1.00 35.26 ? 497 HOH B O   1 
HETATM 4634 O  O   . HOH Q 7 .   ? -7.788  8.125   -11.168 1.00 21.59 ? 498 HOH B O   1 
HETATM 4635 O  O   . HOH Q 7 .   ? -11.522 9.861   -4.142  1.00 30.51 ? 499 HOH B O   1 
HETATM 4636 O  O   . HOH Q 7 .   ? -22.102 29.250  -10.571 1.00 22.45 ? 500 HOH B O   1 
HETATM 4637 O  O   . HOH Q 7 .   ? -3.042  31.521  -28.289 1.00 26.09 ? 501 HOH B O   1 
HETATM 4638 O  O   . HOH Q 7 .   ? -7.301  23.435  -22.969 1.00 16.25 ? 502 HOH B O   1 
HETATM 4639 O  O   . HOH Q 7 .   ? -20.803 13.508  -28.721 1.00 18.12 ? 503 HOH B O   1 
HETATM 4640 O  O   . HOH Q 7 .   ? -12.207 23.463  -34.659 1.00 23.73 ? 504 HOH B O   1 
HETATM 4641 O  O   . HOH Q 7 .   ? -8.038  15.242  -30.107 1.00 26.52 ? 505 HOH B O   1 
HETATM 4642 O  O   . HOH Q 7 .   ? -29.196 7.120   -0.670  1.00 26.55 ? 506 HOH B O   1 
HETATM 4643 O  O   . HOH Q 7 .   ? -13.071 17.573  -37.745 1.00 30.82 ? 507 HOH B O   1 
HETATM 4644 O  O   . HOH Q 7 .   ? 2.019   39.013  -14.909 1.00 24.81 ? 508 HOH B O   1 
HETATM 4645 O  O   . HOH Q 7 .   ? -19.113 15.323  3.308   1.00 24.80 ? 509 HOH B O   1 
HETATM 4646 O  O   . HOH Q 7 .   ? -14.626 5.592   -17.427 1.00 18.20 ? 510 HOH B O   1 
HETATM 4647 O  O   . HOH Q 7 .   ? -34.297 12.782  -12.331 1.00 29.14 ? 511 HOH B O   1 
HETATM 4648 O  O   . HOH Q 7 .   ? -10.547 29.582  -21.520 1.00 33.58 ? 512 HOH B O   1 
HETATM 4649 O  O   . HOH Q 7 .   ? -17.374 7.232   -26.943 1.00 22.78 ? 513 HOH B O   1 
HETATM 4650 O  O   . HOH Q 7 .   ? -33.854 27.095  -11.852 1.00 21.41 ? 514 HOH B O   1 
HETATM 4651 O  O   . HOH Q 7 .   ? -7.161  9.642   -7.562  1.00 27.67 ? 515 HOH B O   1 
HETATM 4652 O  O   . HOH Q 7 .   ? -41.436 33.304  -11.956 1.00 44.44 ? 516 HOH B O   1 
HETATM 4653 O  O   . HOH Q 7 .   ? -27.596 28.029  -4.202  1.00 21.47 ? 517 HOH B O   1 
HETATM 4654 O  O   . HOH Q 7 .   ? -6.764  10.730  -10.926 1.00 19.38 ? 518 HOH B O   1 
HETATM 4655 O  O   . HOH Q 7 .   ? -26.069 14.840  -24.762 1.00 16.19 ? 519 HOH B O   1 
HETATM 4656 O  O   . HOH Q 7 .   ? -32.287 10.645  -23.128 1.00 26.70 ? 520 HOH B O   1 
HETATM 4657 O  O   . HOH Q 7 .   ? -30.906 19.980  -26.892 1.00 26.24 ? 521 HOH B O   1 
HETATM 4658 O  O   . HOH Q 7 .   ? -35.737 19.529  -17.824 1.00 21.72 ? 522 HOH B O   1 
HETATM 4659 O  O   . HOH Q 7 .   ? 0.428   29.464  -10.929 1.00 30.00 ? 523 HOH B O   1 
HETATM 4660 O  O   . HOH Q 7 .   ? -26.243 23.898  2.213   1.00 21.66 ? 524 HOH B O   1 
HETATM 4661 O  O   . HOH Q 7 .   ? -23.411 4.967   -26.236 1.00 31.38 ? 525 HOH B O   1 
HETATM 4662 O  O   . HOH Q 7 .   ? -18.900 14.929  -32.761 1.00 24.80 ? 526 HOH B O   1 
HETATM 4663 O  O   . HOH Q 7 .   ? -27.531 17.051  -25.739 1.00 17.09 ? 527 HOH B O   1 
HETATM 4664 O  O   . HOH Q 7 .   ? -11.065 26.154  -34.008 1.00 24.20 ? 528 HOH B O   1 
HETATM 4665 O  O   . HOH Q 7 .   ? -17.795 12.952  4.282   1.00 31.47 ? 529 HOH B O   1 
HETATM 4666 O  O   . HOH Q 7 .   ? -17.390 1.772   -18.926 1.00 26.20 ? 530 HOH B O   1 
HETATM 4667 O  O   . HOH Q 7 .   ? -25.331 0.869   -12.708 1.00 25.35 ? 531 HOH B O   1 
HETATM 4668 O  O   . HOH Q 7 .   ? -16.454 3.420   -16.747 1.00 23.06 ? 532 HOH B O   1 
HETATM 4669 O  O   . HOH Q 7 .   ? -20.114 0.511   -20.801 1.00 32.52 ? 533 HOH B O   1 
HETATM 4670 O  O   . HOH Q 7 .   ? -12.350 18.645  7.339   1.00 24.99 ? 534 HOH B O   1 
HETATM 4671 O  O   . HOH Q 7 .   ? -30.195 16.039  -0.805  1.00 32.25 ? 535 HOH B O   1 
HETATM 4672 O  O   . HOH Q 7 .   ? -37.808 27.049  -13.311 1.00 38.84 ? 536 HOH B O   1 
HETATM 4673 O  O   . HOH Q 7 .   ? -3.997  24.594  -26.364 1.00 33.82 ? 537 HOH B O   1 
HETATM 4674 O  O   . HOH Q 7 .   ? -23.814 8.359   -26.474 1.00 23.02 ? 538 HOH B O   1 
HETATM 4675 O  O   . HOH Q 7 .   ? -29.224 28.182  -28.952 1.00 33.32 ? 539 HOH B O   1 
HETATM 4676 O  O   . HOH Q 7 .   ? -1.623  28.668  2.572   1.00 40.09 ? 540 HOH B O   1 
HETATM 4677 O  O   . HOH Q 7 .   ? -5.918  13.949  -0.434  1.00 32.26 ? 541 HOH B O   1 
HETATM 4678 O  O   . HOH Q 7 .   ? -26.190 -2.553  -22.621 1.00 33.22 ? 542 HOH B O   1 
HETATM 4679 O  O   . HOH Q 7 .   ? -5.508  9.298   -18.768 1.00 16.08 ? 543 HOH B O   1 
HETATM 4680 O  O   . HOH Q 7 .   ? -25.764 10.582  -22.440 1.00 16.91 ? 544 HOH B O   1 
HETATM 4681 O  O   . HOH Q 7 .   ? -18.263 44.323  -3.006  1.00 31.09 ? 545 HOH B O   1 
HETATM 4682 O  O   . HOH Q 7 .   ? -23.826 34.789  -8.061  1.00 24.14 ? 546 HOH B O   1 
HETATM 4683 O  O   . HOH Q 7 .   ? -35.982 10.903  -24.125 1.00 30.07 ? 547 HOH B O   1 
HETATM 4684 O  O   . HOH Q 7 .   ? -4.651  10.808  -8.173  1.00 25.28 ? 548 HOH B O   1 
HETATM 4685 O  O   . HOH Q 7 .   ? -14.319 8.545   -2.448  1.00 30.33 ? 549 HOH B O   1 
HETATM 4686 O  O   . HOH Q 7 .   ? -4.034  22.509  -16.418 1.00 26.19 ? 550 HOH B O   1 
HETATM 4687 O  O   . HOH Q 7 .   ? -6.119  13.441  -5.820  1.00 34.42 ? 551 HOH B O   1 
HETATM 4688 O  O   . HOH Q 7 .   ? -13.999 6.867   -28.148 1.00 33.83 ? 552 HOH B O   1 
HETATM 4689 O  O   . HOH Q 7 .   ? -0.722  26.106  1.094   1.00 38.27 ? 553 HOH B O   1 
HETATM 4690 O  O   . HOH Q 7 .   ? -40.051 14.440  -15.306 1.00 34.84 ? 554 HOH B O   1 
HETATM 4691 O  O   . HOH Q 7 .   ? -4.852  15.980  -4.603  1.00 41.24 ? 555 HOH B O   1 
HETATM 4692 O  O   . HOH Q 7 .   ? -2.885  14.131  -19.336 1.00 17.19 ? 556 HOH B O   1 
HETATM 4693 O  O   . HOH Q 7 .   ? -29.204 -1.792  -16.565 1.00 40.28 ? 557 HOH B O   1 
HETATM 4694 O  O   . HOH Q 7 .   ? -22.557 13.114  -26.657 1.00 17.76 ? 558 HOH B O   1 
HETATM 4695 O  O   . HOH Q 7 .   ? -12.877 3.561   -13.919 1.00 25.43 ? 559 HOH B O   1 
HETATM 4696 O  O   . HOH Q 7 .   ? -10.499 11.766  3.209   1.00 25.75 ? 560 HOH B O   1 
HETATM 4697 O  O   . HOH Q 7 .   ? -34.019 31.097  -22.491 1.00 26.47 ? 561 HOH B O   1 
HETATM 4698 O  O   . HOH Q 7 .   ? -5.497  22.284  4.243   1.00 24.32 ? 562 HOH B O   1 
HETATM 4699 O  O   . HOH Q 7 .   ? -33.151 6.819   -16.892 1.00 33.20 ? 563 HOH B O   1 
HETATM 4700 O  O   . HOH Q 7 .   ? -25.523 35.554  -6.087  1.00 25.66 ? 564 HOH B O   1 
HETATM 4701 O  O   . HOH Q 7 .   ? -10.137 5.176   -18.400 1.00 16.97 ? 565 HOH B O   1 
HETATM 4702 O  O   . HOH Q 7 .   ? -32.171 9.348   -12.471 1.00 25.27 ? 566 HOH B O   1 
HETATM 4703 O  O   . HOH Q 7 .   ? -8.924  25.029  -33.054 1.00 32.69 ? 567 HOH B O   1 
HETATM 4704 O  O   . HOH Q 7 .   ? -37.962 14.171  -12.669 1.00 29.34 ? 568 HOH B O   1 
HETATM 4705 O  O   . HOH Q 7 .   ? -7.929  41.530  -11.487 1.00 29.81 ? 569 HOH B O   1 
HETATM 4706 O  O   . HOH Q 7 .   ? -9.232  32.575  -32.255 1.00 26.06 ? 570 HOH B O   1 
HETATM 4707 O  O   . HOH Q 7 .   ? -15.801 29.875  -20.757 1.00 32.69 ? 571 HOH B O   1 
HETATM 4708 O  O   . HOH Q 7 .   ? -34.246 23.196  -3.624  1.00 40.83 ? 572 HOH B O   1 
HETATM 4709 O  O   . HOH Q 7 .   ? -25.509 36.642  -0.065  1.00 48.04 ? 573 HOH B O   1 
HETATM 4710 O  O   . HOH Q 7 .   ? -28.712 -0.088  -22.485 1.00 44.84 ? 574 HOH B O   1 
HETATM 4711 O  O   . HOH Q 7 .   ? -13.136 28.856  -28.379 1.00 24.25 ? 575 HOH B O   1 
HETATM 4712 O  O   . HOH Q 7 .   ? -25.953 3.104   -11.173 1.00 23.89 ? 576 HOH B O   1 
HETATM 4713 O  O   . HOH Q 7 .   ? -27.128 -0.706  -25.400 1.00 42.85 ? 577 HOH B O   1 
HETATM 4714 O  O   . HOH Q 7 .   ? -27.273 14.966  1.579   1.00 29.71 ? 578 HOH B O   1 
HETATM 4715 O  O   . HOH Q 7 .   ? -30.808 25.800  -25.639 1.00 22.50 ? 579 HOH B O   1 
HETATM 4716 O  O   . HOH Q 7 .   ? -3.372  14.754  -3.336  1.00 35.53 ? 580 HOH B O   1 
HETATM 4717 O  O   . HOH Q 7 .   ? -24.061 40.850  2.965   1.00 37.14 ? 581 HOH B O   1 
HETATM 4718 O  O   . HOH Q 7 .   ? -12.271 3.350   -6.571  1.00 33.74 ? 582 HOH B O   1 
HETATM 4719 O  O   . HOH Q 7 .   ? -29.232 2.464   -23.001 1.00 38.36 ? 583 HOH B O   1 
HETATM 4720 O  O   . HOH Q 7 .   ? -35.418 25.511  -10.066 1.00 30.41 ? 584 HOH B O   1 
HETATM 4721 O  O   . HOH Q 7 .   ? -14.296 24.111  9.514   1.00 33.03 ? 585 HOH B O   1 
HETATM 4722 O  O   . HOH Q 7 .   ? -4.022  9.730   3.186   1.00 35.81 ? 586 HOH B O   1 
HETATM 4723 O  O   . HOH Q 7 .   ? 0.712   16.072  -2.295  1.00 47.04 ? 587 HOH B O   1 
HETATM 4724 O  O   . HOH Q 7 .   ? -19.215 -2.751  -14.681 1.00 31.22 ? 588 HOH B O   1 
HETATM 4725 O  O   . HOH Q 7 .   ? -15.362 30.918  -28.119 1.00 27.60 ? 589 HOH B O   1 
HETATM 4726 O  O   . HOH Q 7 .   ? -22.964 -2.931  -26.892 1.00 36.52 ? 590 HOH B O   1 
HETATM 4727 O  O   . HOH Q 7 .   ? -8.465  36.914  -18.952 1.00 43.20 ? 591 HOH B O   1 
HETATM 4728 O  O   . HOH Q 7 .   ? -28.343 23.231  -28.362 1.00 26.80 ? 592 HOH B O   1 
HETATM 4729 O  O   . HOH Q 7 .   ? -20.556 12.196  1.271   1.00 36.48 ? 593 HOH B O   1 
HETATM 4730 O  O   . HOH Q 7 .   ? -11.126 36.778  1.067   1.00 33.94 ? 594 HOH B O   1 
HETATM 4731 O  O   . HOH Q 7 .   ? -15.731 4.954   -32.808 1.00 41.13 ? 595 HOH B O   1 
HETATM 4732 O  O   . HOH Q 7 .   ? 0.664   24.152  -33.537 1.00 49.53 ? 596 HOH B O   1 
HETATM 4733 O  O   . HOH Q 7 .   ? -10.776 4.237   -4.105  1.00 32.43 ? 597 HOH B O   1 
HETATM 4734 O  O   . HOH Q 7 .   ? -24.507 2.957   -8.259  1.00 23.41 ? 598 HOH B O   1 
HETATM 4735 O  O   . HOH Q 7 .   ? -27.679 32.373  -1.161  1.00 33.62 ? 599 HOH B O   1 
HETATM 4736 O  O   . HOH Q 7 .   ? -26.093 38.223  -6.702  1.00 35.47 ? 600 HOH B O   1 
HETATM 4737 O  O   . HOH Q 7 .   ? -33.183 24.175  -26.487 1.00 30.25 ? 601 HOH B O   1 
HETATM 4738 O  O   . HOH Q 7 .   ? -1.294  37.738  -11.829 1.00 34.42 ? 602 HOH B O   1 
HETATM 4739 O  O   . HOH Q 7 .   ? -29.891 15.769  -26.909 1.00 36.60 ? 603 HOH B O   1 
HETATM 4740 O  O   . HOH Q 7 .   ? -11.658 35.634  -0.522  1.00 30.72 ? 604 HOH B O   1 
HETATM 4741 O  O   . HOH Q 7 .   ? -25.053 38.084  -16.121 1.00 47.88 ? 605 HOH B O   1 
HETATM 4742 O  O   . HOH Q 7 .   ? -17.294 4.607   -8.710  1.00 22.06 ? 606 HOH B O   1 
HETATM 4743 O  O   . HOH Q 7 .   ? -20.599 14.874  1.032   1.00 24.56 ? 607 HOH B O   1 
HETATM 4744 O  O   . HOH Q 7 .   ? -30.101 20.829  -4.240  1.00 22.80 ? 608 HOH B O   1 
HETATM 4745 O  O   . HOH Q 7 .   ? -35.272 4.522   -7.487  1.00 23.38 ? 609 HOH B O   1 
HETATM 4746 O  O   . HOH Q 7 .   ? -3.709  33.000  0.951   1.00 41.97 ? 610 HOH B O   1 
HETATM 4747 O  O   . HOH Q 7 .   ? -1.325  14.586  -17.093 1.00 21.82 ? 611 HOH B O   1 
HETATM 4748 O  O   . HOH Q 7 .   ? -4.796  15.213  -28.364 1.00 37.40 ? 612 HOH B O   1 
HETATM 4749 O  O   . HOH Q 7 .   ? -24.914 35.107  -3.340  1.00 35.69 ? 613 HOH B O   1 
HETATM 4750 O  O   . HOH Q 7 .   ? 1.383   15.157  -24.715 1.00 34.75 ? 614 HOH B O   1 
HETATM 4751 O  O   . HOH Q 7 .   ? -0.928  26.348  -28.802 1.00 37.55 ? 615 HOH B O   1 
HETATM 4752 O  O   . HOH Q 7 .   ? -4.009  38.026  -15.164 1.00 37.73 ? 616 HOH B O   1 
HETATM 4753 O  O   . HOH Q 7 .   ? -24.341 11.148  -26.247 1.00 25.29 ? 617 HOH B O   1 
HETATM 4754 O  O   . HOH Q 7 .   ? -40.973 22.627  -16.491 1.00 46.47 ? 618 HOH B O   1 
HETATM 4755 O  O   . HOH Q 7 .   ? -38.979 26.280  -22.437 1.00 43.12 ? 619 HOH B O   1 
HETATM 4756 O  O   . HOH Q 7 .   ? -20.466 16.592  4.970   1.00 42.25 ? 620 HOH B O   1 
HETATM 4757 O  O   . HOH Q 7 .   ? -28.791 25.707  -27.489 1.00 30.48 ? 621 HOH B O   1 
HETATM 4758 O  O   . HOH Q 7 .   ? -22.483 31.795  -25.671 1.00 49.43 ? 622 HOH B O   1 
HETATM 4759 O  O   . HOH Q 7 .   ? -9.427  11.610  -4.531  1.00 34.33 ? 623 HOH B O   1 
HETATM 4760 O  O   . HOH Q 7 .   ? -37.694 18.068  -10.190 1.00 42.49 ? 624 HOH B O   1 
HETATM 4761 O  O   . HOH Q 7 .   ? -1.027  25.526  -22.998 1.00 33.15 ? 625 HOH B O   1 
HETATM 4762 O  O   . HOH Q 7 .   ? -42.561 32.096  -17.162 1.00 36.53 ? 626 HOH B O   1 
HETATM 4763 O  O   . HOH Q 7 .   ? -29.871 9.570   -23.910 1.00 20.74 ? 627 HOH B O   1 
HETATM 4764 O  O   . HOH Q 7 .   ? -24.471 4.587   -5.896  1.00 32.79 ? 628 HOH B O   1 
HETATM 4765 O  O   . HOH Q 7 .   ? -33.190 7.700   -14.565 1.00 49.36 ? 629 HOH B O   1 
HETATM 4766 O  O   . HOH Q 7 .   ? -29.856 6.866   -25.120 1.00 44.74 ? 630 HOH B O   1 
HETATM 4767 O  O   . HOH Q 7 .   ? -20.148 6.415   -27.948 1.00 41.86 ? 631 HOH B O   1 
HETATM 4768 O  O   . HOH Q 7 .   ? -41.009 10.483  -17.180 1.00 33.88 ? 632 HOH B O   1 
HETATM 4769 O  O   . HOH Q 7 .   ? 0.880   16.868  -19.819 1.00 21.30 ? 633 HOH B O   1 
HETATM 4770 O  O   . HOH Q 7 .   ? -14.994 1.106   -7.955  1.00 40.30 ? 634 HOH B O   1 
HETATM 4771 O  O   . HOH Q 7 .   ? -22.623 13.279  -30.749 1.00 26.63 ? 635 HOH B O   1 
HETATM 4772 O  O   . HOH Q 7 .   ? -6.082  32.724  -29.521 1.00 36.01 ? 636 HOH B O   1 
HETATM 4773 O  O   . HOH Q 7 .   ? -26.424 12.260  -24.628 1.00 18.10 ? 637 HOH B O   1 
HETATM 4774 O  O   . HOH Q 7 .   ? -11.528 11.424  -31.003 1.00 44.70 ? 638 HOH B O   1 
HETATM 4775 O  O   . HOH Q 7 .   ? -22.835 6.514   -5.244  1.00 31.86 ? 639 HOH B O   1 
HETATM 4776 O  O   . HOH Q 7 .   ? -9.845  8.498   -29.459 1.00 35.86 ? 640 HOH B O   1 
HETATM 4777 O  O   . HOH Q 7 .   ? -36.699 13.201  -8.533  1.00 33.95 ? 641 HOH B O   1 
HETATM 4778 O  O   . HOH Q 7 .   ? -7.394  26.087  4.300   1.00 38.22 ? 642 HOH B O   1 
HETATM 4779 O  O   . HOH Q 7 .   ? -17.764 5.945   -4.338  1.00 34.80 ? 643 HOH B O   1 
HETATM 4780 O  O   . HOH Q 7 .   ? -13.061 9.192   -29.792 1.00 36.27 ? 644 HOH B O   1 
HETATM 4781 O  O   . HOH Q 7 .   ? -27.301 -0.490  -13.275 1.00 36.34 ? 645 HOH B O   1 
HETATM 4782 O  O   . HOH Q 7 .   ? -17.263 35.814  -15.824 1.00 44.66 ? 646 HOH B O   1 
HETATM 4783 O  O   . HOH Q 7 .   ? -30.828 29.802  -27.486 1.00 36.42 ? 647 HOH B O   1 
HETATM 4784 O  O   . HOH Q 7 .   ? -25.353 14.510  -28.901 1.00 45.85 ? 648 HOH B O   1 
HETATM 4785 O  O   . HOH Q 7 .   ? 6.270   32.374  -17.573 1.00 38.81 ? 649 HOH B O   1 
HETATM 4786 O  O   . HOH Q 7 .   ? -13.280 27.249  8.313   1.00 43.03 ? 650 HOH B O   1 
HETATM 4787 O  O   . HOH Q 7 .   ? -17.243 4.366   -6.082  1.00 31.58 ? 651 HOH B O   1 
HETATM 4788 O  O   . HOH Q 7 .   ? -17.429 14.483  -35.013 1.00 34.09 ? 652 HOH B O   1 
HETATM 4789 O  O   . HOH Q 7 .   ? -30.176 13.310  -26.867 1.00 26.77 ? 653 HOH B O   1 
HETATM 4790 O  O   . HOH Q 7 .   ? -37.734 25.374  -24.362 1.00 51.80 ? 654 HOH B O   1 
HETATM 4791 O  O   . HOH Q 7 .   ? -36.598 24.122  -7.480  1.00 33.91 ? 655 HOH B O   1 
HETATM 4792 O  O   . HOH Q 7 .   ? -28.592 11.233  -25.736 1.00 23.22 ? 656 HOH B O   1 
HETATM 4793 O  O   . HOH Q 7 .   ? -27.678 9.587   -28.026 1.00 45.57 ? 657 HOH B O   1 
HETATM 4794 O  O   . HOH Q 7 .   ? -32.023 28.229  -25.290 1.00 31.62 ? 658 HOH B O   1 
HETATM 4795 O  O   . HOH Q 7 .   ? -35.086 8.499   -12.884 1.00 39.01 ? 659 HOH B O   1 
# 
